data_7OAY
# 
_entry.id   7OAY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.347 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7OAY         pdb_00007oay 10.2210/pdb7oay/pdb 
WWPDB D_1292115389 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7OAY 
_pdbx_database_status.recvd_initial_deposition_date   2021-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Naismith, J.H.' 1 0000-0001-6744-5061 
'Mikolajek, H.'  2 0000-0003-0776-9974 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Res Sq' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2693-5015 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'A potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.21203/rs.3.rs-548968/v1 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Huo, J.'          1  ? 
primary 'Mikolajek, H.'    2  ? 
primary 'Le Bas, A.'       3  ? 
primary 'Clark, J.'        4  ? 
primary 'Sharma, P.'       5  ? 
primary 'Kipar, A.'        6  ? 
primary 'Dormon, J.'       7  ? 
primary 'Norman, C.'       8  ? 
primary 'Weckener, M.'     9  ? 
primary 'Clare, D.'        10 ? 
primary 'Harrison, P.'     11 ? 
primary 'Tree, J.'         12 ? 
primary 'Buttigieg, K.'    13 ? 
primary 'Salguero, F.'     14 ? 
primary 'Watson, R.'       15 ? 
primary 'Knott, D.'        16 ? 
primary 'Carnell, O.'      17 ? 
primary 'Ngabo, D.'        18 ? 
primary 'Elmore, M.'       19 ? 
primary 'Fotheringham, S.' 20 ? 
primary 'Harding, A.'      21 ? 
primary 'Ward, P.'         22 ? 
primary 'Moynie, L.'       23 ? 
primary 'Dumoux, M.'       24 ? 
primary 'Hall, Y.'         25 ? 
primary 'Hiscox, J.'       26 ? 
primary 'Owen, A.'         27 ? 
primary 'James, W.'        28 ? 
primary 'Carroll, M.'      29 ? 
primary 'Stewart, J.'      30 ? 
primary 'Naismith, J.'     31 ? 
primary 'Owens, R.'        32 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7OAY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     108.420 
_cell.length_a_esd                 ? 
_cell.length_b                     108.420 
_cell.length_b_esd                 ? 
_cell.length_c                     165.538 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7OAY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Spike protein S1'                       23716.580 6   ? ? ? ? 
2 polymer     man 'F2 nanobody'                            14962.622 6   ? ? ? ? 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   6   ? ? ? ? 
4 water       nat water                                    18.015    323 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNKHHHHHH
;
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNKHHHHHH
;
AAA,CCC,EEE,GGG,III,KKK ? 
2 'polypeptide(L)' no no 
;QVQLVESGGGLVQAGGSLRLACIASGRTFHSYVMAWFRQAPGKEREFVAAISWSSTPTYYGESVKGRFTISRDNAKNTVY
LQMNRLKPEDTAVYFCAADRGESYYYTRPTEYEFWGQGTQVTVSSKHHHHHH
;
;QVQLVESGGGLVQAGGSLRLACIASGRTFHSYVMAWFRQAPGKEREFVAAISWSSTPTYYGESVKGRFTISRDNAKNTVY
LQMNRLKPEDTAVYFCAADRGESYYYTRPTEYEFWGQGTQVTVSSKHHHHHH
;
BBB,DDD,FFF,HHH,JJJ,LLL ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   ASN n 
1 3   ILE n 
1 4   THR n 
1 5   ASN n 
1 6   LEU n 
1 7   CYS n 
1 8   PRO n 
1 9   PHE n 
1 10  GLY n 
1 11  GLU n 
1 12  VAL n 
1 13  PHE n 
1 14  ASN n 
1 15  ALA n 
1 16  THR n 
1 17  ARG n 
1 18  PHE n 
1 19  ALA n 
1 20  SER n 
1 21  VAL n 
1 22  TYR n 
1 23  ALA n 
1 24  TRP n 
1 25  ASN n 
1 26  ARG n 
1 27  LYS n 
1 28  ARG n 
1 29  ILE n 
1 30  SER n 
1 31  ASN n 
1 32  CYS n 
1 33  VAL n 
1 34  ALA n 
1 35  ASP n 
1 36  TYR n 
1 37  SER n 
1 38  VAL n 
1 39  LEU n 
1 40  TYR n 
1 41  ASN n 
1 42  SER n 
1 43  ALA n 
1 44  SER n 
1 45  PHE n 
1 46  SER n 
1 47  THR n 
1 48  PHE n 
1 49  LYS n 
1 50  CYS n 
1 51  TYR n 
1 52  GLY n 
1 53  VAL n 
1 54  SER n 
1 55  PRO n 
1 56  THR n 
1 57  LYS n 
1 58  LEU n 
1 59  ASN n 
1 60  ASP n 
1 61  LEU n 
1 62  CYS n 
1 63  PHE n 
1 64  THR n 
1 65  ASN n 
1 66  VAL n 
1 67  TYR n 
1 68  ALA n 
1 69  ASP n 
1 70  SER n 
1 71  PHE n 
1 72  VAL n 
1 73  ILE n 
1 74  ARG n 
1 75  GLY n 
1 76  ASP n 
1 77  GLU n 
1 78  VAL n 
1 79  ARG n 
1 80  GLN n 
1 81  ILE n 
1 82  ALA n 
1 83  PRO n 
1 84  GLY n 
1 85  GLN n 
1 86  THR n 
1 87  GLY n 
1 88  LYS n 
1 89  ILE n 
1 90  ALA n 
1 91  ASP n 
1 92  TYR n 
1 93  ASN n 
1 94  TYR n 
1 95  LYS n 
1 96  LEU n 
1 97  PRO n 
1 98  ASP n 
1 99  ASP n 
1 100 PHE n 
1 101 THR n 
1 102 GLY n 
1 103 CYS n 
1 104 VAL n 
1 105 ILE n 
1 106 ALA n 
1 107 TRP n 
1 108 ASN n 
1 109 SER n 
1 110 ASN n 
1 111 ASN n 
1 112 LEU n 
1 113 ASP n 
1 114 SER n 
1 115 LYS n 
1 116 VAL n 
1 117 GLY n 
1 118 GLY n 
1 119 ASN n 
1 120 TYR n 
1 121 ASN n 
1 122 TYR n 
1 123 LEU n 
1 124 TYR n 
1 125 ARG n 
1 126 LEU n 
1 127 PHE n 
1 128 ARG n 
1 129 LYS n 
1 130 SER n 
1 131 ASN n 
1 132 LEU n 
1 133 LYS n 
1 134 PRO n 
1 135 PHE n 
1 136 GLU n 
1 137 ARG n 
1 138 ASP n 
1 139 ILE n 
1 140 SER n 
1 141 THR n 
1 142 GLU n 
1 143 ILE n 
1 144 TYR n 
1 145 GLN n 
1 146 ALA n 
1 147 GLY n 
1 148 SER n 
1 149 THR n 
1 150 PRO n 
1 151 CYS n 
1 152 ASN n 
1 153 GLY n 
1 154 VAL n 
1 155 GLU n 
1 156 GLY n 
1 157 PHE n 
1 158 ASN n 
1 159 CYS n 
1 160 TYR n 
1 161 PHE n 
1 162 PRO n 
1 163 LEU n 
1 164 GLN n 
1 165 SER n 
1 166 TYR n 
1 167 GLY n 
1 168 PHE n 
1 169 GLN n 
1 170 PRO n 
1 171 THR n 
1 172 ASN n 
1 173 GLY n 
1 174 VAL n 
1 175 GLY n 
1 176 TYR n 
1 177 GLN n 
1 178 PRO n 
1 179 TYR n 
1 180 ARG n 
1 181 VAL n 
1 182 VAL n 
1 183 VAL n 
1 184 LEU n 
1 185 SER n 
1 186 PHE n 
1 187 GLU n 
1 188 LEU n 
1 189 LEU n 
1 190 HIS n 
1 191 ALA n 
1 192 PRO n 
1 193 ALA n 
1 194 THR n 
1 195 VAL n 
1 196 CYS n 
1 197 GLY n 
1 198 PRO n 
1 199 LYS n 
1 200 LYS n 
1 201 SER n 
1 202 THR n 
1 203 ASN n 
1 204 LYS n 
1 205 HIS n 
1 206 HIS n 
1 207 HIS n 
1 208 HIS n 
1 209 HIS n 
1 210 HIS n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  ALA n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  ALA n 
2 22  CYS n 
2 23  ILE n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  ARG n 
2 28  THR n 
2 29  PHE n 
2 30  HIS n 
2 31  SER n 
2 32  TYR n 
2 33  VAL n 
2 34  MET n 
2 35  ALA n 
2 36  TRP n 
2 37  PHE n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLU n 
2 45  ARG n 
2 46  GLU n 
2 47  PHE n 
2 48  VAL n 
2 49  ALA n 
2 50  ALA n 
2 51  ILE n 
2 52  SER n 
2 53  TRP n 
2 54  SER n 
2 55  SER n 
2 56  THR n 
2 57  PRO n 
2 58  THR n 
2 59  TYR n 
2 60  TYR n 
2 61  GLY n 
2 62  GLU n 
2 63  SER n 
2 64  VAL n 
2 65  LYS n 
2 66  GLY n 
2 67  ARG n 
2 68  PHE n 
2 69  THR n 
2 70  ILE n 
2 71  SER n 
2 72  ARG n 
2 73  ASP n 
2 74  ASN n 
2 75  ALA n 
2 76  LYS n 
2 77  ASN n 
2 78  THR n 
2 79  VAL n 
2 80  TYR n 
2 81  LEU n 
2 82  GLN n 
2 83  MET n 
2 84  ASN n 
2 85  ARG n 
2 86  LEU n 
2 87  LYS n 
2 88  PRO n 
2 89  GLU n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  PHE n 
2 96  CYS n 
2 97  ALA n 
2 98  ALA n 
2 99  ASP n 
2 100 ARG n 
2 101 GLY n 
2 102 GLU n 
2 103 SER n 
2 104 TYR n 
2 105 TYR n 
2 106 TYR n 
2 107 THR n 
2 108 ARG n 
2 109 PRO n 
2 110 THR n 
2 111 GLU n 
2 112 TYR n 
2 113 GLU n 
2 114 PHE n 
2 115 TRP n 
2 116 GLY n 
2 117 GLN n 
2 118 GLY n 
2 119 THR n 
2 120 GLN n 
2 121 VAL n 
2 122 THR n 
2 123 VAL n 
2 124 SER n 
2 125 SER n 
2 126 LYS n 
2 127 HIS n 
2 128 HIS n 
2 129 HIS n 
2 130 HIS n 
2 131 HIS n 
2 132 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 210 '2019-nCoV, SARS-CoV-2' ? 'S, 2' ? ? ? ? ? ? 
'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? ? ? Human 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 132 Llama                   ? ?      ? ? ? ? ? ? 'Lama glama' 9844    ? ? ? ? ? ? ? ?     
'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SPIKE_SARS2 P0DTC2 ? 1 
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTN
;
330 
2 PDB 7OAY        7OAY   ? 2 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 7OAY AAA 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
2  2 7OAY BBB 1 ? 132 ? 7OAY   1   ? 132 ? 1   132 
3  1 7OAY CCC 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
4  2 7OAY DDD 1 ? 132 ? 7OAY   1   ? 132 ? 1   132 
5  1 7OAY EEE 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
6  2 7OAY FFF 1 ? 132 ? 7OAY   1   ? 132 ? 1   132 
7  1 7OAY GGG 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
8  2 7OAY HHH 1 ? 132 ? 7OAY   1   ? 132 ? 1   132 
9  1 7OAY III 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
10 2 7OAY JJJ 1 ? 132 ? 7OAY   1   ? 132 ? 1   132 
11 1 7OAY KKK 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
12 2 7OAY LLL 1 ? 132 ? 7OAY   1   ? 132 ? 1   132 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1  7OAY LYS AAA 204 ? UNP P0DTC2 ? ? 'expression tag' 533 1  
1  7OAY HIS AAA 205 ? UNP P0DTC2 ? ? 'expression tag' 534 2  
1  7OAY HIS AAA 206 ? UNP P0DTC2 ? ? 'expression tag' 535 3  
1  7OAY HIS AAA 207 ? UNP P0DTC2 ? ? 'expression tag' 536 4  
1  7OAY HIS AAA 208 ? UNP P0DTC2 ? ? 'expression tag' 537 5  
1  7OAY HIS AAA 209 ? UNP P0DTC2 ? ? 'expression tag' 538 6  
1  7OAY HIS AAA 210 ? UNP P0DTC2 ? ? 'expression tag' 539 7  
3  7OAY LYS CCC 204 ? UNP P0DTC2 ? ? 'expression tag' 533 8  
3  7OAY HIS CCC 205 ? UNP P0DTC2 ? ? 'expression tag' 534 9  
3  7OAY HIS CCC 206 ? UNP P0DTC2 ? ? 'expression tag' 535 10 
3  7OAY HIS CCC 207 ? UNP P0DTC2 ? ? 'expression tag' 536 11 
3  7OAY HIS CCC 208 ? UNP P0DTC2 ? ? 'expression tag' 537 12 
3  7OAY HIS CCC 209 ? UNP P0DTC2 ? ? 'expression tag' 538 13 
3  7OAY HIS CCC 210 ? UNP P0DTC2 ? ? 'expression tag' 539 14 
5  7OAY LYS EEE 204 ? UNP P0DTC2 ? ? 'expression tag' 533 15 
5  7OAY HIS EEE 205 ? UNP P0DTC2 ? ? 'expression tag' 534 16 
5  7OAY HIS EEE 206 ? UNP P0DTC2 ? ? 'expression tag' 535 17 
5  7OAY HIS EEE 207 ? UNP P0DTC2 ? ? 'expression tag' 536 18 
5  7OAY HIS EEE 208 ? UNP P0DTC2 ? ? 'expression tag' 537 19 
5  7OAY HIS EEE 209 ? UNP P0DTC2 ? ? 'expression tag' 538 20 
5  7OAY HIS EEE 210 ? UNP P0DTC2 ? ? 'expression tag' 539 21 
7  7OAY LYS GGG 204 ? UNP P0DTC2 ? ? 'expression tag' 533 22 
7  7OAY HIS GGG 205 ? UNP P0DTC2 ? ? 'expression tag' 534 23 
7  7OAY HIS GGG 206 ? UNP P0DTC2 ? ? 'expression tag' 535 24 
7  7OAY HIS GGG 207 ? UNP P0DTC2 ? ? 'expression tag' 536 25 
7  7OAY HIS GGG 208 ? UNP P0DTC2 ? ? 'expression tag' 537 26 
7  7OAY HIS GGG 209 ? UNP P0DTC2 ? ? 'expression tag' 538 27 
7  7OAY HIS GGG 210 ? UNP P0DTC2 ? ? 'expression tag' 539 28 
9  7OAY LYS III 204 ? UNP P0DTC2 ? ? 'expression tag' 533 29 
9  7OAY HIS III 205 ? UNP P0DTC2 ? ? 'expression tag' 534 30 
9  7OAY HIS III 206 ? UNP P0DTC2 ? ? 'expression tag' 535 31 
9  7OAY HIS III 207 ? UNP P0DTC2 ? ? 'expression tag' 536 32 
9  7OAY HIS III 208 ? UNP P0DTC2 ? ? 'expression tag' 537 33 
9  7OAY HIS III 209 ? UNP P0DTC2 ? ? 'expression tag' 538 34 
9  7OAY HIS III 210 ? UNP P0DTC2 ? ? 'expression tag' 539 35 
11 7OAY LYS KKK 204 ? UNP P0DTC2 ? ? 'expression tag' 533 36 
11 7OAY HIS KKK 205 ? UNP P0DTC2 ? ? 'expression tag' 534 37 
11 7OAY HIS KKK 206 ? UNP P0DTC2 ? ? 'expression tag' 535 38 
11 7OAY HIS KKK 207 ? UNP P0DTC2 ? ? 'expression tag' 536 39 
11 7OAY HIS KKK 208 ? UNP P0DTC2 ? ? 'expression tag' 537 40 
11 7OAY HIS KKK 209 ? UNP P0DTC2 ? ? 'expression tag' 538 41 
11 7OAY HIS KKK 210 ? UNP P0DTC2 ? ? 'expression tag' 539 42 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7OAY 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.42 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         49.18 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M SPG, pH 8, 25 % Peg 1500,' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-07-22 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9762 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9762 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7OAY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.34 
_reflns.d_resolution_low                               94 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     91842 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.051 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.34 
_reflns_shell.d_res_low                                     2.40 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4643 
_reflns_shell.percent_possible_all                          99.6 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.7 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.5 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.024 
_refine.aniso_B[1][2]                            0.012 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            0.024 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            -0.077 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               53.178 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7OAY 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.340 
_refine.ls_d_res_low                             93.895 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     91817 
_refine.ls_number_reflns_R_free                  4643 
_refine.ls_number_reflns_R_work                  87174 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.977 
_refine.ls_percent_reflns_R_free                 5.057 
_refine.ls_R_factor_all                          0.194 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2275 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1919 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6ZBP 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.367 
_refine.pdbx_overall_ESU_R_Free                  0.230 
_refine.pdbx_solvent_vdw_probe_radii             1.000 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             20.742 
_refine.overall_SU_ML                            0.216 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        15292 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             323 
_refine_hist.number_atoms_total               15699 
_refine_hist.d_res_high                       2.340 
_refine_hist.d_res_low                        93.895 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.012  15826 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  14182 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.611  1.660  21530 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.287  1.583  32532 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.729  5.000  1921  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 32.378 21.604 879   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.259 15.000 2358  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 18.137 15.000 108   ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.069  0.200  1986  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  18331 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  4154  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.194  0.200  2459  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.190  0.200  12959 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200  7669  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.082  0.200  7675  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.137  0.200  446   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.016  0.200  2     ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.207  0.200  29    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.257  0.200  149   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.275  0.200  10    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 1.883  3.470  7720  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.882  3.469  7719  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.086  5.194  9629  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.086  5.195  9630  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 2.103  3.678  8106  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.103  3.678  8106  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.385  5.435  11901 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.385  5.436  11902 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.505  38.729 16771 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.501  38.698 16753 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.050  6107  ? r_ncsr_local_group_1           ? ? 
'X-RAY DIFFRACTION' ? 0.070  0.050  6159  ? r_ncsr_local_group_2           ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.050  6033  ? r_ncsr_local_group_3           ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.050  6174  ? r_ncsr_local_group_4           ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.050  6029  ? r_ncsr_local_group_5           ? ? 
'X-RAY DIFFRACTION' ? 0.049  0.050  3977  ? r_ncsr_local_group_6           ? ? 
'X-RAY DIFFRACTION' ? 0.035  0.050  3967  ? r_ncsr_local_group_7           ? ? 
'X-RAY DIFFRACTION' ? 0.060  0.050  3934  ? r_ncsr_local_group_8           ? ? 
'X-RAY DIFFRACTION' ? 0.051  0.050  3946  ? r_ncsr_local_group_9           ? ? 
'X-RAY DIFFRACTION' ? 0.045  0.050  3992  ? r_ncsr_local_group_10          ? ? 
'X-RAY DIFFRACTION' ? 0.088  0.050  6002  ? r_ncsr_local_group_11          ? ? 
'X-RAY DIFFRACTION' ? 0.072  0.050  6097  ? r_ncsr_local_group_12          ? ? 
'X-RAY DIFFRACTION' ? 0.091  0.050  6067  ? r_ncsr_local_group_13          ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.050  6134  ? r_ncsr_local_group_14          ? ? 
'X-RAY DIFFRACTION' ? 0.053  0.050  3940  ? r_ncsr_local_group_15          ? ? 
'X-RAY DIFFRACTION' ? 0.063  0.050  3933  ? r_ncsr_local_group_16          ? ? 
'X-RAY DIFFRACTION' ? 0.067  0.050  3929  ? r_ncsr_local_group_17          ? ? 
'X-RAY DIFFRACTION' ? 0.044  0.050  3987  ? r_ncsr_local_group_18          ? ? 
'X-RAY DIFFRACTION' ? 0.089  0.050  5970  ? r_ncsr_local_group_19          ? ? 
'X-RAY DIFFRACTION' ? 0.076  0.050  6070  ? r_ncsr_local_group_20          ? ? 
'X-RAY DIFFRACTION' ? 0.091  0.050  6002  ? r_ncsr_local_group_21          ? ? 
'X-RAY DIFFRACTION' ? 0.064  0.050  3898  ? r_ncsr_local_group_22          ? ? 
'X-RAY DIFFRACTION' ? 0.056  0.050  3909  ? r_ncsr_local_group_23          ? ? 
'X-RAY DIFFRACTION' ? 0.042  0.050  3953  ? r_ncsr_local_group_24          ? ? 
'X-RAY DIFFRACTION' ? 0.079  0.050  6026  ? r_ncsr_local_group_25          ? ? 
'X-RAY DIFFRACTION' ? 0.059  0.050  6147  ? r_ncsr_local_group_26          ? ? 
'X-RAY DIFFRACTION' ? 0.060  0.050  3919  ? r_ncsr_local_group_27          ? ? 
'X-RAY DIFFRACTION' ? 0.064  0.050  3952  ? r_ncsr_local_group_28          ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.050  6052  ? r_ncsr_local_group_29          ? ? 
'X-RAY DIFFRACTION' ? 0.060  0.050  3943  ? r_ncsr_local_group_30          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1  ? ? 0.08731 ? 0.05009 1  'Local ncs' ? AAA ? ? ? 1  
'X-RAY DIFFRACTION' 2  ? ? 0.08731 ? 0.05009 2  'Local ncs' ? CCC ? ? ? 1  
'X-RAY DIFFRACTION' 3  ? ? 0.07032 ? 0.05009 3  'Local ncs' ? AAA ? ? ? 2  
'X-RAY DIFFRACTION' 4  ? ? 0.07032 ? 0.05009 4  'Local ncs' ? EEE ? ? ? 2  
'X-RAY DIFFRACTION' 5  ? ? 0.08477 ? 0.05009 5  'Local ncs' ? AAA ? ? ? 3  
'X-RAY DIFFRACTION' 6  ? ? 0.08477 ? 0.05009 6  'Local ncs' ? GGG ? ? ? 3  
'X-RAY DIFFRACTION' 7  ? ? 0.07656 ? 0.05009 7  'Local ncs' ? AAA ? ? ? 4  
'X-RAY DIFFRACTION' 8  ? ? 0.07656 ? 0.05009 8  'Local ncs' ? III ? ? ? 4  
'X-RAY DIFFRACTION' 9  ? ? 0.08674 ? 0.05009 9  'Local ncs' ? AAA ? ? ? 5  
'X-RAY DIFFRACTION' 10 ? ? 0.08674 ? 0.05009 10 'Local ncs' ? KKK ? ? ? 5  
'X-RAY DIFFRACTION' 11 ? ? 0.04915 ? 0.05010 11 'Local ncs' ? BBB ? ? ? 6  
'X-RAY DIFFRACTION' 12 ? ? 0.04915 ? 0.05010 12 'Local ncs' ? DDD ? ? ? 6  
'X-RAY DIFFRACTION' 13 ? ? 0.03505 ? 0.05011 13 'Local ncs' ? BBB ? ? ? 7  
'X-RAY DIFFRACTION' 14 ? ? 0.03505 ? 0.05011 14 'Local ncs' ? FFF ? ? ? 7  
'X-RAY DIFFRACTION' 15 ? ? 0.05966 ? 0.05010 15 'Local ncs' ? BBB ? ? ? 8  
'X-RAY DIFFRACTION' 16 ? ? 0.05966 ? 0.05010 16 'Local ncs' ? HHH ? ? ? 8  
'X-RAY DIFFRACTION' 17 ? ? 0.05134 ? 0.05010 17 'Local ncs' ? BBB ? ? ? 9  
'X-RAY DIFFRACTION' 18 ? ? 0.05134 ? 0.05010 18 'Local ncs' ? JJJ ? ? ? 9  
'X-RAY DIFFRACTION' 19 ? ? 0.04470 ? 0.05011 19 'Local ncs' ? BBB ? ? ? 10 
'X-RAY DIFFRACTION' 20 ? ? 0.04470 ? 0.05011 20 'Local ncs' ? LLL ? ? ? 10 
'X-RAY DIFFRACTION' 21 ? ? 0.08794 ? 0.05008 21 'Local ncs' ? CCC ? ? ? 11 
'X-RAY DIFFRACTION' 22 ? ? 0.08794 ? 0.05008 22 'Local ncs' ? EEE ? ? ? 11 
'X-RAY DIFFRACTION' 23 ? ? 0.07246 ? 0.05009 23 'Local ncs' ? CCC ? ? ? 12 
'X-RAY DIFFRACTION' 24 ? ? 0.07246 ? 0.05009 24 'Local ncs' ? GGG ? ? ? 12 
'X-RAY DIFFRACTION' 25 ? ? 0.09084 ? 0.05009 25 'Local ncs' ? CCC ? ? ? 13 
'X-RAY DIFFRACTION' 26 ? ? 0.09084 ? 0.05009 26 'Local ncs' ? III ? ? ? 13 
'X-RAY DIFFRACTION' 27 ? ? 0.07596 ? 0.05009 27 'Local ncs' ? CCC ? ? ? 14 
'X-RAY DIFFRACTION' 28 ? ? 0.07596 ? 0.05009 28 'Local ncs' ? KKK ? ? ? 14 
'X-RAY DIFFRACTION' 29 ? ? 0.05344 ? 0.05010 29 'Local ncs' ? DDD ? ? ? 15 
'X-RAY DIFFRACTION' 30 ? ? 0.05344 ? 0.05010 30 'Local ncs' ? FFF ? ? ? 15 
'X-RAY DIFFRACTION' 31 ? ? 0.06283 ? 0.05010 31 'Local ncs' ? DDD ? ? ? 16 
'X-RAY DIFFRACTION' 32 ? ? 0.06283 ? 0.05010 32 'Local ncs' ? HHH ? ? ? 16 
'X-RAY DIFFRACTION' 33 ? ? 0.06702 ? 0.05010 33 'Local ncs' ? DDD ? ? ? 17 
'X-RAY DIFFRACTION' 34 ? ? 0.06702 ? 0.05010 34 'Local ncs' ? JJJ ? ? ? 17 
'X-RAY DIFFRACTION' 35 ? ? 0.04399 ? 0.05010 35 'Local ncs' ? DDD ? ? ? 18 
'X-RAY DIFFRACTION' 36 ? ? 0.04399 ? 0.05010 36 'Local ncs' ? LLL ? ? ? 18 
'X-RAY DIFFRACTION' 37 ? ? 0.08904 ? 0.05009 37 'Local ncs' ? EEE ? ? ? 19 
'X-RAY DIFFRACTION' 38 ? ? 0.08904 ? 0.05009 38 'Local ncs' ? GGG ? ? ? 19 
'X-RAY DIFFRACTION' 39 ? ? 0.07634 ? 0.05009 39 'Local ncs' ? EEE ? ? ? 20 
'X-RAY DIFFRACTION' 40 ? ? 0.07634 ? 0.05009 40 'Local ncs' ? III ? ? ? 20 
'X-RAY DIFFRACTION' 41 ? ? 0.09072 ? 0.05009 41 'Local ncs' ? EEE ? ? ? 21 
'X-RAY DIFFRACTION' 42 ? ? 0.09072 ? 0.05009 42 'Local ncs' ? KKK ? ? ? 21 
'X-RAY DIFFRACTION' 43 ? ? 0.06434 ? 0.05010 43 'Local ncs' ? FFF ? ? ? 22 
'X-RAY DIFFRACTION' 44 ? ? 0.06434 ? 0.05010 44 'Local ncs' ? HHH ? ? ? 22 
'X-RAY DIFFRACTION' 45 ? ? 0.05553 ? 0.05010 45 'Local ncs' ? FFF ? ? ? 23 
'X-RAY DIFFRACTION' 46 ? ? 0.05553 ? 0.05010 46 'Local ncs' ? JJJ ? ? ? 23 
'X-RAY DIFFRACTION' 47 ? ? 0.04249 ? 0.05010 47 'Local ncs' ? FFF ? ? ? 24 
'X-RAY DIFFRACTION' 48 ? ? 0.04249 ? 0.05010 48 'Local ncs' ? LLL ? ? ? 24 
'X-RAY DIFFRACTION' 49 ? ? 0.07944 ? 0.05009 49 'Local ncs' ? GGG ? ? ? 25 
'X-RAY DIFFRACTION' 50 ? ? 0.07944 ? 0.05009 50 'Local ncs' ? III ? ? ? 25 
'X-RAY DIFFRACTION' 51 ? ? 0.05892 ? 0.05009 51 'Local ncs' ? GGG ? ? ? 26 
'X-RAY DIFFRACTION' 52 ? ? 0.05892 ? 0.05009 52 'Local ncs' ? KKK ? ? ? 26 
'X-RAY DIFFRACTION' 53 ? ? 0.06043 ? 0.05010 53 'Local ncs' ? HHH ? ? ? 27 
'X-RAY DIFFRACTION' 54 ? ? 0.06043 ? 0.05010 54 'Local ncs' ? JJJ ? ? ? 27 
'X-RAY DIFFRACTION' 55 ? ? 0.06366 ? 0.05010 55 'Local ncs' ? HHH ? ? ? 28 
'X-RAY DIFFRACTION' 56 ? ? 0.06366 ? 0.05010 56 'Local ncs' ? LLL ? ? ? 28 
'X-RAY DIFFRACTION' 57 ? ? 0.07700 ? 0.05009 57 'Local ncs' ? III ? ? ? 29 
'X-RAY DIFFRACTION' 58 ? ? 0.07700 ? 0.05009 58 'Local ncs' ? KKK ? ? ? 29 
'X-RAY DIFFRACTION' 59 ? ? 0.05953 ? 0.05010 59 'Local ncs' ? JJJ ? ? ? 30 
'X-RAY DIFFRACTION' 60 ? ? 0.05953 ? 0.05010 60 'Local ncs' ? LLL ? ? ? 30 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.340  2.401  6777 . 304 6473 100.0000 . 0.333 . 0.299 . 0.335 . . . . . 0.336 . 20 . 0.525 0.520 
'X-RAY DIFFRACTION' 2.401  2.466  6662 . 342 6320 100.0000 . 0.312 . 0.347 . 0.311 . . . . . 0.308 . 20 . 0.692 0.672 
'X-RAY DIFFRACTION' 2.466  2.538  6439 . 334 6100 99.9223  . 0.302 . 0.341 . 0.300 . . . . . 0.295 . 20 . 0.768 0.744 
'X-RAY DIFFRACTION' 2.538  2.616  6180 . 402 5773 99.9191  . 0.290 . 0.307 . 0.289 . . . . . 0.278 . 20 . 0.815 0.812 
'X-RAY DIFFRACTION' 2.616  2.702  6130 . 325 5802 99.9511  . 0.272 . 0.309 . 0.270 . . . . . 0.253 . 20 . 0.845 0.841 
'X-RAY DIFFRACTION' 2.702  2.796  5823 . 283 5538 99.9657  . 0.256 . 0.299 . 0.254 . . . . . 0.230 . 20 . 0.869 0.861 
'X-RAY DIFFRACTION' 2.796  2.902  5696 . 310 5385 99.9824  . 0.244 . 0.276 . 0.242 . . . . . 0.216 . 20 . 0.883 0.871 
'X-RAY DIFFRACTION' 2.902  3.020  5397 . 268 5127 99.9629  . 0.229 . 0.252 . 0.227 . . . . . 0.202 . 20 . 0.913 0.902 
'X-RAY DIFFRACTION' 3.020  3.154  5195 . 270 4925 100.0000 . 0.215 . 0.254 . 0.213 . . . . . 0.189 . 20 . 0.926 0.912 
'X-RAY DIFFRACTION' 3.154  3.308  4993 . 278 4715 100.0000 . 0.215 . 0.248 . 0.213 . . . . . 0.193 . 20 . 0.931 0.920 
'X-RAY DIFFRACTION' 3.308  3.487  4788 . 231 4556 99.9791  . 0.207 . 0.222 . 0.206 . . . . . 0.192 . 20 . 0.942 0.930 
'X-RAY DIFFRACTION' 3.487  3.698  4459 . 194 4265 100.0000 . 0.197 . 0.249 . 0.195 . . . . . 0.179 . 20 . 0.940 0.919 
'X-RAY DIFFRACTION' 3.698  3.953  4216 . 193 4023 100.0000 . 0.176 . 0.192 . 0.175 . . . . . 0.162 . 20 . 0.956 0.948 
'X-RAY DIFFRACTION' 3.953  4.269  3932 . 188 3744 100.0000 . 0.149 . 0.199 . 0.147 . . . . . 0.135 . 20 . 0.967 0.957 
'X-RAY DIFFRACTION' 4.269  4.676  3615 . 166 3448 99.9723  . 0.117 . 0.145 . 0.116 . . . . . 0.111 . 20 . 0.979 0.977 
'X-RAY DIFFRACTION' 4.676  5.226  3277 . 128 3149 100.0000 . 0.134 . 0.189 . 0.132 . . . . . 0.124 . 20 . 0.976 0.966 
'X-RAY DIFFRACTION' 5.226  6.031  2887 . 137 2750 100.0000 . 0.159 . 0.223 . 0.156 . . . . . 0.146 . 20 . 0.966 0.955 
'X-RAY DIFFRACTION' 6.031  7.379  2430 . 146 2284 100.0000 . 0.146 . 0.167 . 0.145 . . . . . 0.138 . 20 . 0.968 0.965 
'X-RAY DIFFRACTION' 7.379  10.404 1877 . 104 1772 99.9467  . 0.140 . 0.162 . 0.139 . . . . . 0.140 . 20 . 0.972 0.966 
'X-RAY DIFFRACTION' 10.404 93.895 1045 . 40  1005 100.0000 . 0.192 . 0.171 . 0.193 . . . . . 0.203 . 20 . 0.955 0.981 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1  1  AAA 
2  1  CCC 
3  2  AAA 
4  2  EEE 
5  3  AAA 
6  3  GGG 
7  4  AAA 
8  4  III 
9  5  AAA 
10 5  KKK 
11 6  BBB 
12 6  DDD 
13 7  BBB 
14 7  FFF 
15 8  BBB 
16 8  HHH 
17 9  BBB 
18 9  JJJ 
19 10 BBB 
20 10 LLL 
21 11 CCC 
22 11 EEE 
23 12 CCC 
24 12 GGG 
25 13 CCC 
26 13 III 
27 14 CCC 
28 14 KKK 
29 15 DDD 
30 15 FFF 
31 16 DDD 
32 16 HHH 
33 17 DDD 
34 17 JJJ 
35 18 DDD 
36 18 LLL 
37 19 EEE 
38 19 GGG 
39 20 EEE 
40 20 III 
41 21 EEE 
42 21 KKK 
43 22 FFF 
44 22 HHH 
45 23 FFF 
46 23 JJJ 
47 24 FFF 
48 24 LLL 
49 25 GGG 
50 25 III 
51 26 GGG 
52 26 KKK 
53 27 HHH 
54 27 JJJ 
55 28 HHH 
56 28 LLL 
57 29 III 
58 29 KKK 
59 30 JJJ 
60 30 LLL 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1  AAA 331 AAA 528 1  ? ? ? ? ? ? ? ? ? 1  ? 
2  CCC 331 CCC 528 1  ? ? ? ? ? ? ? ? ? 1  ? 
3  AAA 332 AAA 527 2  ? ? ? ? ? ? ? ? ? 2  ? 
4  EEE 332 EEE 527 2  ? ? ? ? ? ? ? ? ? 2  ? 
5  AAA 333 AAA 527 3  ? ? ? ? ? ? ? ? ? 3  ? 
6  GGG 333 GGG 527 3  ? ? ? ? ? ? ? ? ? 3  ? 
7  AAA 331 AAA 528 4  ? ? ? ? ? ? ? ? ? 4  ? 
8  III 331 III 528 4  ? ? ? ? ? ? ? ? ? 4  ? 
9  AAA 332 AAA 527 5  ? ? ? ? ? ? ? ? ? 5  ? 
10 KKK 332 KKK 527 5  ? ? ? ? ? ? ? ? ? 5  ? 
11 BBB 1   BBB 125 6  ? ? ? ? ? ? ? ? ? 6  ? 
12 DDD 1   DDD 125 6  ? ? ? ? ? ? ? ? ? 6  ? 
13 BBB 1   BBB 123 7  ? ? ? ? ? ? ? ? ? 7  ? 
14 FFF 1   FFF 123 7  ? ? ? ? ? ? ? ? ? 7  ? 
15 BBB 1   BBB 125 8  ? ? ? ? ? ? ? ? ? 8  ? 
16 HHH 1   HHH 125 8  ? ? ? ? ? ? ? ? ? 8  ? 
17 BBB 1   BBB 125 9  ? ? ? ? ? ? ? ? ? 9  ? 
18 JJJ 1   JJJ 125 9  ? ? ? ? ? ? ? ? ? 9  ? 
19 BBB 1   BBB 125 10 ? ? ? ? ? ? ? ? ? 10 ? 
20 LLL 1   LLL 125 10 ? ? ? ? ? ? ? ? ? 10 ? 
21 CCC 332 CCC 527 11 ? ? ? ? ? ? ? ? ? 11 ? 
22 EEE 332 EEE 527 11 ? ? ? ? ? ? ? ? ? 11 ? 
23 CCC 333 CCC 527 12 ? ? ? ? ? ? ? ? ? 12 ? 
24 GGG 333 GGG 527 12 ? ? ? ? ? ? ? ? ? 12 ? 
25 CCC 331 CCC 528 13 ? ? ? ? ? ? ? ? ? 13 ? 
26 III 331 III 528 13 ? ? ? ? ? ? ? ? ? 13 ? 
27 CCC 332 CCC 527 14 ? ? ? ? ? ? ? ? ? 14 ? 
28 KKK 332 KKK 527 14 ? ? ? ? ? ? ? ? ? 14 ? 
29 DDD 1   DDD 123 15 ? ? ? ? ? ? ? ? ? 15 ? 
30 FFF 1   FFF 123 15 ? ? ? ? ? ? ? ? ? 15 ? 
31 DDD 1   DDD 125 16 ? ? ? ? ? ? ? ? ? 16 ? 
32 HHH 1   HHH 125 16 ? ? ? ? ? ? ? ? ? 16 ? 
33 DDD 1   DDD 125 17 ? ? ? ? ? ? ? ? ? 17 ? 
34 JJJ 1   JJJ 125 17 ? ? ? ? ? ? ? ? ? 17 ? 
35 DDD 1   DDD 125 18 ? ? ? ? ? ? ? ? ? 18 ? 
36 LLL 1   LLL 125 18 ? ? ? ? ? ? ? ? ? 18 ? 
37 EEE 333 EEE 527 19 ? ? ? ? ? ? ? ? ? 19 ? 
38 GGG 333 GGG 527 19 ? ? ? ? ? ? ? ? ? 19 ? 
39 EEE 332 EEE 527 20 ? ? ? ? ? ? ? ? ? 20 ? 
40 III 332 III 527 20 ? ? ? ? ? ? ? ? ? 20 ? 
41 EEE 332 EEE 528 21 ? ? ? ? ? ? ? ? ? 21 ? 
42 KKK 332 KKK 528 21 ? ? ? ? ? ? ? ? ? 21 ? 
43 FFF 1   FFF 123 22 ? ? ? ? ? ? ? ? ? 22 ? 
44 HHH 1   HHH 123 22 ? ? ? ? ? ? ? ? ? 22 ? 
45 FFF 1   FFF 123 23 ? ? ? ? ? ? ? ? ? 23 ? 
46 JJJ 1   JJJ 123 23 ? ? ? ? ? ? ? ? ? 23 ? 
47 FFF 1   FFF 123 24 ? ? ? ? ? ? ? ? ? 24 ? 
48 LLL 1   LLL 123 24 ? ? ? ? ? ? ? ? ? 24 ? 
49 GGG 333 GGG 527 25 ? ? ? ? ? ? ? ? ? 25 ? 
50 III 333 III 527 25 ? ? ? ? ? ? ? ? ? 25 ? 
51 GGG 333 GGG 527 26 ? ? ? ? ? ? ? ? ? 26 ? 
52 KKK 333 KKK 527 26 ? ? ? ? ? ? ? ? ? 26 ? 
53 HHH 1   HHH 125 27 ? ? ? ? ? ? ? ? ? 27 ? 
54 JJJ 1   JJJ 125 27 ? ? ? ? ? ? ? ? ? 27 ? 
55 HHH 1   HHH 125 28 ? ? ? ? ? ? ? ? ? 28 ? 
56 LLL 1   LLL 125 28 ? ? ? ? ? ? ? ? ? 28 ? 
57 III 332 III 527 29 ? ? ? ? ? ? ? ? ? 29 ? 
58 KKK 332 KKK 527 29 ? ? ? ? ? ? ? ? ? 29 ? 
59 JJJ 1   JJJ 125 30 ? ? ? ? ? ? ? ? ? 30 ? 
60 LLL 1   LLL 125 30 ? ? ? ? ? ? ? ? ? 30 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1  'Local NCS retraints between domains:       1       2' 
2  'Local NCS retraints between domains:       3       4' 
3  'Local NCS retraints between domains:       5       6' 
4  'Local NCS retraints between domains:       7       8' 
5  'Local NCS retraints between domains:       9      10' 
6  'Local NCS retraints between domains:      11      12' 
7  'Local NCS retraints between domains:      13      14' 
8  'Local NCS retraints between domains:      15      16' 
9  'Local NCS retraints between domains:      17      18' 
10 'Local NCS retraints between domains:      19      20' 
11 'Local NCS retraints between domains:      21      22' 
12 'Local NCS retraints between domains:      23      24' 
13 'Local NCS retraints between domains:      25      26' 
14 'Local NCS retraints between domains:      27      28' 
15 'Local NCS retraints between domains:      29      30' 
16 'Local NCS retraints between domains:      31      32' 
17 'Local NCS retraints between domains:      33      34' 
18 'Local NCS retraints between domains:      35      36' 
19 'Local NCS retraints between domains:      37      38' 
20 'Local NCS retraints between domains:      39      40' 
21 'Local NCS retraints between domains:      41      42' 
22 'Local NCS retraints between domains:      43      44' 
23 'Local NCS retraints between domains:      45      46' 
24 'Local NCS retraints between domains:      47      48' 
25 'Local NCS retraints between domains:      49      50' 
26 'Local NCS retraints between domains:      51      52' 
27 'Local NCS retraints between domains:      53      54' 
28 'Local NCS retraints between domains:      55      56' 
29 'Local NCS retraints between domains:      57      58' 
30 'Local NCS retraints between domains:      59      60' 
# 
_struct.entry_id                     7OAY 
_struct.title                        'Nanobody F2 bound to RBD' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7OAY 
_struct_keywords.text            'Spike, nanobody, high affinity, ANTIVIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 1 ? 
H  N N 2 ? 
I  N N 1 ? 
J  N N 2 ? 
K  N N 1 ? 
L  N N 2 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 4 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 8   ? ASN A 14  ? PRO AAA 337 ASN AAA 343 1 ? 7 
HELX_P HELX_P2  AA2 SER A 20  ? TRP A 24  ? SER AAA 349 TRP AAA 353 5 ? 5 
HELX_P HELX_P3  AA3 TYR A 36  ? ASN A 41  ? TYR AAA 365 ASN AAA 370 1 ? 6 
HELX_P HELX_P4  AA4 SER A 54  ? ASP A 60  ? SER AAA 383 ASP AAA 389 5 ? 7 
HELX_P HELX_P5  AA5 ASP A 76  ? ILE A 81  ? ASP AAA 405 ILE AAA 410 5 ? 6 
HELX_P HELX_P6  AA6 GLY A 87  ? ASN A 93  ? GLY AAA 416 ASN AAA 422 1 ? 7 
HELX_P HELX_P7  AA7 SER A 109 ? SER A 114 ? SER AAA 438 SER AAA 443 1 ? 6 
HELX_P HELX_P8  AA8 GLY A 173 ? TYR A 176 ? GLY AAA 502 TYR AAA 505 5 ? 4 
HELX_P HELX_P9  AA9 THR B 28  ? TYR B 32  ? THR BBB 28  TYR BBB 32  5 ? 5 
HELX_P HELX_P10 AB1 ASN B 74  ? LYS B 76  ? ASN BBB 74  LYS BBB 76  5 ? 3 
HELX_P HELX_P11 AB2 LYS B 87  ? THR B 91  ? LYS BBB 87  THR BBB 91  5 ? 5 
HELX_P HELX_P12 AB3 ARG B 108 ? TYR B 112 ? ARG BBB 108 TYR BBB 112 5 ? 5 
HELX_P HELX_P13 AB4 PHE C 9   ? ASN C 14  ? PHE CCC 338 ASN CCC 343 1 ? 6 
HELX_P HELX_P14 AB5 SER C 20  ? TRP C 24  ? SER CCC 349 TRP CCC 353 5 ? 5 
HELX_P HELX_P15 AB6 TYR C 36  ? ASN C 41  ? TYR CCC 365 ASN CCC 370 1 ? 6 
HELX_P HELX_P16 AB7 SER C 54  ? ASP C 60  ? SER CCC 383 ASP CCC 389 5 ? 7 
HELX_P HELX_P17 AB8 ASP C 76  ? ILE C 81  ? ASP CCC 405 ILE CCC 410 5 ? 6 
HELX_P HELX_P18 AB9 GLY C 87  ? ASN C 93  ? GLY CCC 416 ASN CCC 422 1 ? 7 
HELX_P HELX_P19 AC1 SER C 109 ? SER C 114 ? SER CCC 438 SER CCC 443 1 ? 6 
HELX_P HELX_P20 AC2 GLY C 173 ? TYR C 176 ? GLY CCC 502 TYR CCC 505 5 ? 4 
HELX_P HELX_P21 AC3 THR D 28  ? TYR D 32  ? THR DDD 28  TYR DDD 32  5 ? 5 
HELX_P HELX_P22 AC4 ASN D 74  ? LYS D 76  ? ASN DDD 74  LYS DDD 76  5 ? 3 
HELX_P HELX_P23 AC5 LYS D 87  ? THR D 91  ? LYS DDD 87  THR DDD 91  5 ? 5 
HELX_P HELX_P24 AC6 ARG D 108 ? TYR D 112 ? ARG DDD 108 TYR DDD 112 5 ? 5 
HELX_P HELX_P25 AC7 PHE E 9   ? ASN E 14  ? PHE EEE 338 ASN EEE 343 1 ? 6 
HELX_P HELX_P26 AC8 SER E 20  ? TRP E 24  ? SER EEE 349 TRP EEE 353 5 ? 5 
HELX_P HELX_P27 AC9 TYR E 36  ? ASN E 41  ? TYR EEE 365 ASN EEE 370 1 ? 6 
HELX_P HELX_P28 AD1 SER E 54  ? ASP E 60  ? SER EEE 383 ASP EEE 389 5 ? 7 
HELX_P HELX_P29 AD2 ASP E 76  ? ILE E 81  ? ASP EEE 405 ILE EEE 410 5 ? 6 
HELX_P HELX_P30 AD3 GLY E 87  ? ASN E 93  ? GLY EEE 416 ASN EEE 422 1 ? 7 
HELX_P HELX_P31 AD4 SER E 109 ? SER E 114 ? SER EEE 438 SER EEE 443 1 ? 6 
HELX_P HELX_P32 AD5 GLY E 173 ? TYR E 176 ? GLY EEE 502 TYR EEE 505 5 ? 4 
HELX_P HELX_P33 AD6 THR F 28  ? TYR F 32  ? THR FFF 28  TYR FFF 32  5 ? 5 
HELX_P HELX_P34 AD7 ASN F 74  ? LYS F 76  ? ASN FFF 74  LYS FFF 76  5 ? 3 
HELX_P HELX_P35 AD8 LYS F 87  ? THR F 91  ? LYS FFF 87  THR FFF 91  5 ? 5 
HELX_P HELX_P36 AD9 ARG F 108 ? TYR F 112 ? ARG FFF 108 TYR FFF 112 5 ? 5 
HELX_P HELX_P37 AE1 PRO G 8   ? ASN G 14  ? PRO GGG 337 ASN GGG 343 1 ? 7 
HELX_P HELX_P38 AE2 SER G 20  ? TRP G 24  ? SER GGG 349 TRP GGG 353 5 ? 5 
HELX_P HELX_P39 AE3 TYR G 36  ? ASN G 41  ? TYR GGG 365 ASN GGG 370 1 ? 6 
HELX_P HELX_P40 AE4 SER G 54  ? ASP G 60  ? SER GGG 383 ASP GGG 389 5 ? 7 
HELX_P HELX_P41 AE5 ASP G 76  ? ILE G 81  ? ASP GGG 405 ILE GGG 410 5 ? 6 
HELX_P HELX_P42 AE6 GLY G 87  ? ASN G 93  ? GLY GGG 416 ASN GGG 422 1 ? 7 
HELX_P HELX_P43 AE7 SER G 109 ? SER G 114 ? SER GGG 438 SER GGG 443 1 ? 6 
HELX_P HELX_P44 AE8 GLY G 173 ? TYR G 176 ? GLY GGG 502 TYR GGG 505 5 ? 4 
HELX_P HELX_P45 AE9 THR H 28  ? TYR H 32  ? THR HHH 28  TYR HHH 32  5 ? 5 
HELX_P HELX_P46 AF1 ASN H 74  ? LYS H 76  ? ASN HHH 74  LYS HHH 76  5 ? 3 
HELX_P HELX_P47 AF2 LYS H 87  ? THR H 91  ? LYS HHH 87  THR HHH 91  5 ? 5 
HELX_P HELX_P48 AF3 ARG H 108 ? TYR H 112 ? ARG HHH 108 TYR HHH 112 5 ? 5 
HELX_P HELX_P49 AF4 PRO I 8   ? ASN I 14  ? PRO III 337 ASN III 343 1 ? 7 
HELX_P HELX_P50 AF5 SER I 20  ? TRP I 24  ? SER III 349 TRP III 353 5 ? 5 
HELX_P HELX_P51 AF6 TYR I 36  ? ASN I 41  ? TYR III 365 ASN III 370 1 ? 6 
HELX_P HELX_P52 AF7 SER I 54  ? ASP I 60  ? SER III 383 ASP III 389 5 ? 7 
HELX_P HELX_P53 AF8 ASP I 76  ? ILE I 81  ? ASP III 405 ILE III 410 5 ? 6 
HELX_P HELX_P54 AF9 GLY I 87  ? ASN I 93  ? GLY III 416 ASN III 422 1 ? 7 
HELX_P HELX_P55 AG1 SER I 109 ? SER I 114 ? SER III 438 SER III 443 1 ? 6 
HELX_P HELX_P56 AG2 GLY I 173 ? TYR I 176 ? GLY III 502 TYR III 505 5 ? 4 
HELX_P HELX_P57 AG3 THR J 28  ? TYR J 32  ? THR JJJ 28  TYR JJJ 32  5 ? 5 
HELX_P HELX_P58 AG4 ASN J 74  ? LYS J 76  ? ASN JJJ 74  LYS JJJ 76  5 ? 3 
HELX_P HELX_P59 AG5 LYS J 87  ? THR J 91  ? LYS JJJ 87  THR JJJ 91  5 ? 5 
HELX_P HELX_P60 AG6 ARG J 108 ? TYR J 112 ? ARG JJJ 108 TYR JJJ 112 5 ? 5 
HELX_P HELX_P61 AG7 PRO K 8   ? ASN K 14  ? PRO KKK 337 ASN KKK 343 1 ? 7 
HELX_P HELX_P62 AG8 SER K 20  ? TRP K 24  ? SER KKK 349 TRP KKK 353 5 ? 5 
HELX_P HELX_P63 AG9 TYR K 36  ? ASN K 41  ? TYR KKK 365 ASN KKK 370 1 ? 6 
HELX_P HELX_P64 AH1 SER K 54  ? ASP K 60  ? SER KKK 383 ASP KKK 389 5 ? 7 
HELX_P HELX_P65 AH2 ASP K 76  ? ILE K 81  ? ASP KKK 405 ILE KKK 410 5 ? 6 
HELX_P HELX_P66 AH3 GLY K 87  ? ASN K 93  ? GLY KKK 416 ASN KKK 422 1 ? 7 
HELX_P HELX_P67 AH4 SER K 109 ? SER K 114 ? SER KKK 438 SER KKK 443 1 ? 6 
HELX_P HELX_P68 AH5 GLY K 173 ? TYR K 176 ? GLY KKK 502 TYR KKK 505 5 ? 4 
HELX_P HELX_P69 AH6 THR L 28  ? TYR L 32  ? THR LLL 28  TYR LLL 32  5 ? 5 
HELX_P HELX_P70 AH7 ASN L 74  ? LYS L 76  ? ASN LLL 74  LYS LLL 76  5 ? 3 
HELX_P HELX_P71 AH8 LYS L 87  ? THR L 91  ? LYS LLL 87  THR LLL 91  5 ? 5 
HELX_P HELX_P72 AH9 ARG L 108 ? TYR L 112 ? ARG LLL 108 TYR LLL 112 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?   ? A CYS 7   SG  ? ? ? 1_555 A CYS 32  SG ? ? AAA CYS 336 AAA CYS 361 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
disulf2  disulf ?   ? A CYS 50  SG  ? ? ? 1_555 A CYS 103 SG ? ? AAA CYS 379 AAA CYS 432 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
disulf3  disulf ?   ? A CYS 62  SG  ? ? ? 1_555 A CYS 196 SG ? ? AAA CYS 391 AAA CYS 525 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
disulf4  disulf ?   ? A CYS 151 SG  ? ? ? 1_555 A CYS 159 SG ? ? AAA CYS 480 AAA CYS 488 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
disulf5  disulf ?   ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? BBB CYS 22  BBB CYS 96  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf6  disulf ?   ? C CYS 7   SG  ? ? ? 1_555 C CYS 32  SG ? ? CCC CYS 336 CCC CYS 361 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
disulf7  disulf ?   ? C CYS 50  SG  ? ? ? 1_555 C CYS 103 SG ? ? CCC CYS 379 CCC CYS 432 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
disulf8  disulf ?   ? C CYS 62  SG  ? ? ? 1_555 C CYS 196 SG ? ? CCC CYS 391 CCC CYS 525 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
disulf9  disulf ?   ? C CYS 151 SG  ? ? ? 1_555 C CYS 159 SG ? ? CCC CYS 480 CCC CYS 488 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
disulf10 disulf ?   ? D CYS 22  SG  ? ? ? 1_555 D CYS 96  SG ? ? DDD CYS 22  DDD CYS 96  1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf11 disulf ?   ? E CYS 7   SG  ? ? ? 1_555 E CYS 32  SG ? ? EEE CYS 336 EEE CYS 361 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
disulf12 disulf ?   ? E CYS 50  SG  ? ? ? 1_555 E CYS 103 SG ? ? EEE CYS 379 EEE CYS 432 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf13 disulf ?   ? E CYS 62  SG  ? ? ? 1_555 E CYS 196 SG ? ? EEE CYS 391 EEE CYS 525 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
disulf14 disulf ?   ? E CYS 151 SG  ? ? ? 1_555 E CYS 159 SG ? ? EEE CYS 480 EEE CYS 488 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
disulf15 disulf ?   ? F CYS 22  SG  ? ? ? 1_555 F CYS 96  SG ? ? FFF CYS 22  FFF CYS 96  1_555 ? ? ? ? ? ? ? 2.020 ? ? 
disulf16 disulf ?   ? G CYS 7   SG  ? ? ? 1_555 G CYS 32  SG ? ? GGG CYS 336 GGG CYS 361 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf17 disulf ?   ? G CYS 50  SG  ? ? ? 1_555 G CYS 103 SG ? ? GGG CYS 379 GGG CYS 432 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
disulf18 disulf ?   ? G CYS 62  SG  ? ? ? 1_555 G CYS 196 SG ? ? GGG CYS 391 GGG CYS 525 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
disulf19 disulf ?   ? G CYS 151 SG  ? ? ? 1_555 G CYS 159 SG ? ? GGG CYS 480 GGG CYS 488 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
disulf20 disulf ?   ? H CYS 22  SG  ? ? ? 1_555 H CYS 96  SG ? ? HHH CYS 22  HHH CYS 96  1_555 ? ? ? ? ? ? ? 2.021 ? ? 
disulf21 disulf ?   ? I CYS 7   SG  ? ? ? 1_555 I CYS 32  SG ? ? III CYS 336 III CYS 361 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
disulf22 disulf ?   ? I CYS 50  SG  ? ? ? 1_555 I CYS 103 SG ? ? III CYS 379 III CYS 432 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
disulf23 disulf ?   ? I CYS 62  SG  ? ? ? 1_555 I CYS 196 SG ? ? III CYS 391 III CYS 525 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
disulf24 disulf ?   ? I CYS 151 SG  ? ? ? 1_555 I CYS 159 SG ? ? III CYS 480 III CYS 488 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
disulf25 disulf ?   ? J CYS 22  SG  ? ? ? 1_555 J CYS 96  SG ? ? JJJ CYS 22  JJJ CYS 96  1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf26 disulf ?   ? K CYS 7   SG  ? ? ? 1_555 K CYS 32  SG ? ? KKK CYS 336 KKK CYS 361 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf27 disulf ?   ? K CYS 50  SG  ? ? ? 1_555 K CYS 103 SG ? ? KKK CYS 379 KKK CYS 432 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf28 disulf ?   ? K CYS 62  SG  ? ? ? 1_555 K CYS 196 SG ? ? KKK CYS 391 KKK CYS 525 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
disulf29 disulf ?   ? K CYS 151 SG  ? ? ? 1_555 K CYS 159 SG ? ? KKK CYS 480 KKK CYS 488 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf30 disulf ?   ? L CYS 22  SG  ? ? ? 1_555 L CYS 96  SG ? ? LLL CYS 22  LLL CYS 96  1_555 ? ? ? ? ? ? ? 2.060 ? ? 
covale1  covale one ? A ASN 14  ND2 ? ? ? 1_555 M NAG .   C1 ? ? AAA ASN 343 AAA NAG 601 1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale2  covale one ? C ASN 14  ND2 ? ? ? 1_555 N NAG .   C1 ? ? CCC ASN 343 CCC NAG 601 1_555 ? ? ? ? ? ? ? 1.436 ? 
N-Glycosylation 
covale3  covale one ? E ASN 14  ND2 ? ? ? 1_555 O NAG .   C1 ? ? EEE ASN 343 EEE NAG 601 1_555 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale4  covale one ? G ASN 14  ND2 ? ? ? 1_555 P NAG .   C1 ? ? GGG ASN 343 GGG NAG 601 1_555 ? ? ? ? ? ? ? 1.429 ? 
N-Glycosylation 
covale5  covale one ? I ASN 14  ND2 ? ? ? 1_555 Q NAG .   C1 ? ? III ASN 343 III NAG 601 1_555 ? ? ? ? ? ? ? 1.432 ? 
N-Glycosylation 
covale6  covale one ? K ASN 14  ND2 ? ? ? 1_555 R NAG .   C1 ? ? KKK ASN 343 KKK NAG 601 1_555 ? ? ? ? ? ? ? 1.443 ? 
N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 4 ? 
AA8 ? 6 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 4 ? 
AB6 ? 6 ? 
AB7 ? 3 ? 
AB8 ? 2 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 6 ? 
AC3 ? 4 ? 
AC4 ? 6 ? 
AC5 ? 3 ? 
AC6 ? 2 ? 
AC7 ? 2 ? 
AC8 ? 4 ? 
AC9 ? 6 ? 
AD1 ? 4 ? 
AD2 ? 6 ? 
AD3 ? 3 ? 
AD4 ? 2 ? 
AD5 ? 2 ? 
AD6 ? 4 ? 
AD7 ? 6 ? 
AD8 ? 4 ? 
AD9 ? 6 ? 
AE1 ? 3 ? 
AE2 ? 2 ? 
AE3 ? 2 ? 
AE4 ? 4 ? 
AE5 ? 6 ? 
AE6 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB6 4 5 ? anti-parallel 
AB6 5 6 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? parallel      
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC2 4 5 ? anti-parallel 
AC2 5 6 ? anti-parallel 
AC3 1 2 ? parallel      
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC4 4 5 ? anti-parallel 
AC4 5 6 ? anti-parallel 
AC5 1 2 ? parallel      
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC8 3 4 ? anti-parallel 
AC9 1 2 ? parallel      
AC9 2 3 ? anti-parallel 
AC9 3 4 ? anti-parallel 
AC9 4 5 ? anti-parallel 
AC9 5 6 ? anti-parallel 
AD1 1 2 ? parallel      
AD1 2 3 ? anti-parallel 
AD1 3 4 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD2 3 4 ? anti-parallel 
AD2 4 5 ? anti-parallel 
AD2 5 6 ? anti-parallel 
AD3 1 2 ? parallel      
AD3 2 3 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? parallel      
AD7 2 3 ? anti-parallel 
AD7 3 4 ? anti-parallel 
AD7 4 5 ? anti-parallel 
AD7 5 6 ? anti-parallel 
AD8 1 2 ? parallel      
AD8 2 3 ? anti-parallel 
AD8 3 4 ? anti-parallel 
AD9 1 2 ? anti-parallel 
AD9 2 3 ? anti-parallel 
AD9 3 4 ? anti-parallel 
AD9 4 5 ? anti-parallel 
AD9 5 6 ? anti-parallel 
AE1 1 2 ? parallel      
AE1 2 3 ? anti-parallel 
AE2 1 2 ? anti-parallel 
AE3 1 2 ? anti-parallel 
AE4 1 2 ? anti-parallel 
AE4 2 3 ? anti-parallel 
AE4 3 4 ? anti-parallel 
AE5 1 2 ? parallel      
AE5 2 3 ? anti-parallel 
AE5 3 4 ? anti-parallel 
AE5 4 5 ? anti-parallel 
AE5 5 6 ? anti-parallel 
AE6 1 2 ? parallel      
AE6 2 3 ? anti-parallel 
AE6 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASN A 25  ? ILE A 29  ? ASN AAA 354 ILE AAA 358 
AA1 2 ASN A 65  ? ARG A 74  ? ASN AAA 394 ARG AAA 403 
AA1 3 PRO A 178 ? GLU A 187 ? PRO AAA 507 GLU AAA 516 
AA1 4 GLY A 102 ? ASN A 108 ? GLY AAA 431 ASN AAA 437 
AA1 5 THR A 47  ? TYR A 51  ? THR AAA 376 TYR AAA 380 
AA1 6 GLU B 102 ? SER B 103 ? GLU BBB 102 SER BBB 103 
AA2 1 CYS A 32  ? VAL A 33  ? CYS AAA 361 VAL AAA 362 
AA2 2 VAL A 195 ? CYS A 196 ? VAL AAA 524 CYS AAA 525 
AA2 3 CYS A 62  ? PHE A 63  ? CYS AAA 391 PHE AAA 392 
AA3 1 LEU A 123 ? ARG A 125 ? LEU AAA 452 ARG AAA 454 
AA3 2 LEU A 163 ? SER A 165 ? LEU AAA 492 SER AAA 494 
AA4 1 TYR A 144 ? GLN A 145 ? TYR AAA 473 GLN AAA 474 
AA4 2 CYS A 159 ? TYR A 160 ? CYS AAA 488 TYR AAA 489 
AA5 1 LEU B 4   ? SER B 7   ? LEU BBB 4   SER BBB 7   
AA5 2 LEU B 18  ? ALA B 24  ? LEU BBB 18  ALA BBB 24  
AA5 3 THR B 78  ? MET B 83  ? THR BBB 78  MET BBB 83  
AA5 4 PHE B 68  ? ASP B 73  ? PHE BBB 68  ASP BBB 73  
AA6 1 GLY B 10  ? GLN B 13  ? GLY BBB 10  GLN BBB 13  
AA6 2 THR B 119 ? SER B 124 ? THR BBB 119 SER BBB 124 
AA6 3 ALA B 92  ? ASP B 99  ? ALA BBB 92  ASP BBB 99  
AA6 4 VAL B 33  ? GLN B 39  ? VAL BBB 33  GLN BBB 39  
AA6 5 GLU B 46  ? ILE B 51  ? GLU BBB 46  ILE BBB 51  
AA6 6 THR B 58  ? TYR B 60  ? THR BBB 58  TYR BBB 60  
AA7 1 GLY B 10  ? GLN B 13  ? GLY BBB 10  GLN BBB 13  
AA7 2 THR B 119 ? SER B 124 ? THR BBB 119 SER BBB 124 
AA7 3 ALA B 92  ? ASP B 99  ? ALA BBB 92  ASP BBB 99  
AA7 4 PHE B 114 ? TRP B 115 ? PHE BBB 114 TRP BBB 115 
AA8 1 ASN C 25  ? ILE C 29  ? ASN CCC 354 ILE CCC 358 
AA8 2 ASN C 65  ? ARG C 74  ? ASN CCC 394 ARG CCC 403 
AA8 3 PRO C 178 ? GLU C 187 ? PRO CCC 507 GLU CCC 516 
AA8 4 GLY C 102 ? ASN C 108 ? GLY CCC 431 ASN CCC 437 
AA8 5 THR C 47  ? TYR C 51  ? THR CCC 376 TYR CCC 380 
AA8 6 GLU D 102 ? SER D 103 ? GLU DDD 102 SER DDD 103 
AA9 1 CYS C 32  ? VAL C 33  ? CYS CCC 361 VAL CCC 362 
AA9 2 VAL C 195 ? CYS C 196 ? VAL CCC 524 CYS CCC 525 
AA9 3 CYS C 62  ? PHE C 63  ? CYS CCC 391 PHE CCC 392 
AB1 1 LEU C 123 ? ARG C 125 ? LEU CCC 452 ARG CCC 454 
AB1 2 LEU C 163 ? SER C 165 ? LEU CCC 492 SER CCC 494 
AB2 1 TYR C 144 ? GLN C 145 ? TYR CCC 473 GLN CCC 474 
AB2 2 CYS C 159 ? TYR C 160 ? CYS CCC 488 TYR CCC 489 
AB3 1 LEU D 4   ? SER D 7   ? LEU DDD 4   SER DDD 7   
AB3 2 LEU D 18  ? ALA D 24  ? LEU DDD 18  ALA DDD 24  
AB3 3 THR D 78  ? MET D 83  ? THR DDD 78  MET DDD 83  
AB3 4 PHE D 68  ? ASP D 73  ? PHE DDD 68  ASP DDD 73  
AB4 1 GLY D 10  ? GLN D 13  ? GLY DDD 10  GLN DDD 13  
AB4 2 THR D 119 ? SER D 124 ? THR DDD 119 SER DDD 124 
AB4 3 ALA D 92  ? ASP D 99  ? ALA DDD 92  ASP DDD 99  
AB4 4 VAL D 33  ? GLN D 39  ? VAL DDD 33  GLN DDD 39  
AB4 5 GLU D 46  ? ILE D 51  ? GLU DDD 46  ILE DDD 51  
AB4 6 THR D 58  ? TYR D 60  ? THR DDD 58  TYR DDD 60  
AB5 1 GLY D 10  ? GLN D 13  ? GLY DDD 10  GLN DDD 13  
AB5 2 THR D 119 ? SER D 124 ? THR DDD 119 SER DDD 124 
AB5 3 ALA D 92  ? ASP D 99  ? ALA DDD 92  ASP DDD 99  
AB5 4 PHE D 114 ? TRP D 115 ? PHE DDD 114 TRP DDD 115 
AB6 1 ASN E 25  ? ILE E 29  ? ASN EEE 354 ILE EEE 358 
AB6 2 ASN E 65  ? ARG E 74  ? ASN EEE 394 ARG EEE 403 
AB6 3 PRO E 178 ? GLU E 187 ? PRO EEE 507 GLU EEE 516 
AB6 4 GLY E 102 ? ASN E 108 ? GLY EEE 431 ASN EEE 437 
AB6 5 THR E 47  ? TYR E 51  ? THR EEE 376 TYR EEE 380 
AB6 6 GLU F 102 ? SER F 103 ? GLU FFF 102 SER FFF 103 
AB7 1 CYS E 32  ? VAL E 33  ? CYS EEE 361 VAL EEE 362 
AB7 2 VAL E 195 ? CYS E 196 ? VAL EEE 524 CYS EEE 525 
AB7 3 CYS E 62  ? PHE E 63  ? CYS EEE 391 PHE EEE 392 
AB8 1 LEU E 123 ? ARG E 125 ? LEU EEE 452 ARG EEE 454 
AB8 2 LEU E 163 ? SER E 165 ? LEU EEE 492 SER EEE 494 
AB9 1 TYR E 144 ? GLN E 145 ? TYR EEE 473 GLN EEE 474 
AB9 2 CYS E 159 ? TYR E 160 ? CYS EEE 488 TYR EEE 489 
AC1 1 LEU F 4   ? SER F 7   ? LEU FFF 4   SER FFF 7   
AC1 2 LEU F 18  ? ALA F 24  ? LEU FFF 18  ALA FFF 24  
AC1 3 THR F 78  ? MET F 83  ? THR FFF 78  MET FFF 83  
AC1 4 PHE F 68  ? ASP F 73  ? PHE FFF 68  ASP FFF 73  
AC2 1 GLY F 10  ? VAL F 12  ? GLY FFF 10  VAL FFF 12  
AC2 2 THR F 119 ? VAL F 123 ? THR FFF 119 VAL FFF 123 
AC2 3 ALA F 92  ? ASP F 99  ? ALA FFF 92  ASP FFF 99  
AC2 4 VAL F 33  ? GLN F 39  ? VAL FFF 33  GLN FFF 39  
AC2 5 GLU F 46  ? ILE F 51  ? GLU FFF 46  ILE FFF 51  
AC2 6 THR F 58  ? TYR F 60  ? THR FFF 58  TYR FFF 60  
AC3 1 GLY F 10  ? VAL F 12  ? GLY FFF 10  VAL FFF 12  
AC3 2 THR F 119 ? VAL F 123 ? THR FFF 119 VAL FFF 123 
AC3 3 ALA F 92  ? ASP F 99  ? ALA FFF 92  ASP FFF 99  
AC3 4 PHE F 114 ? TRP F 115 ? PHE FFF 114 TRP FFF 115 
AC4 1 ASN G 25  ? ILE G 29  ? ASN GGG 354 ILE GGG 358 
AC4 2 ASN G 65  ? ARG G 74  ? ASN GGG 394 ARG GGG 403 
AC4 3 PRO G 178 ? GLU G 187 ? PRO GGG 507 GLU GGG 516 
AC4 4 GLY G 102 ? ASN G 108 ? GLY GGG 431 ASN GGG 437 
AC4 5 THR G 47  ? TYR G 51  ? THR GGG 376 TYR GGG 380 
AC4 6 GLU H 102 ? SER H 103 ? GLU HHH 102 SER HHH 103 
AC5 1 CYS G 32  ? VAL G 33  ? CYS GGG 361 VAL GGG 362 
AC5 2 VAL G 195 ? CYS G 196 ? VAL GGG 524 CYS GGG 525 
AC5 3 CYS G 62  ? PHE G 63  ? CYS GGG 391 PHE GGG 392 
AC6 1 LEU G 123 ? ARG G 125 ? LEU GGG 452 ARG GGG 454 
AC6 2 LEU G 163 ? SER G 165 ? LEU GGG 492 SER GGG 494 
AC7 1 TYR G 144 ? GLN G 145 ? TYR GGG 473 GLN GGG 474 
AC7 2 CYS G 159 ? TYR G 160 ? CYS GGG 488 TYR GGG 489 
AC8 1 LEU H 4   ? SER H 7   ? LEU HHH 4   SER HHH 7   
AC8 2 LEU H 18  ? ALA H 24  ? LEU HHH 18  ALA HHH 24  
AC8 3 THR H 78  ? MET H 83  ? THR HHH 78  MET HHH 83  
AC8 4 PHE H 68  ? ASP H 73  ? PHE HHH 68  ASP HHH 73  
AC9 1 GLY H 10  ? GLN H 13  ? GLY HHH 10  GLN HHH 13  
AC9 2 THR H 119 ? SER H 124 ? THR HHH 119 SER HHH 124 
AC9 3 ALA H 92  ? ASP H 99  ? ALA HHH 92  ASP HHH 99  
AC9 4 VAL H 33  ? GLN H 39  ? VAL HHH 33  GLN HHH 39  
AC9 5 GLU H 46  ? ILE H 51  ? GLU HHH 46  ILE HHH 51  
AC9 6 THR H 58  ? TYR H 60  ? THR HHH 58  TYR HHH 60  
AD1 1 GLY H 10  ? GLN H 13  ? GLY HHH 10  GLN HHH 13  
AD1 2 THR H 119 ? SER H 124 ? THR HHH 119 SER HHH 124 
AD1 3 ALA H 92  ? ASP H 99  ? ALA HHH 92  ASP HHH 99  
AD1 4 PHE H 114 ? TRP H 115 ? PHE HHH 114 TRP HHH 115 
AD2 1 ASN I 25  ? ILE I 29  ? ASN III 354 ILE III 358 
AD2 2 ASN I 65  ? ARG I 74  ? ASN III 394 ARG III 403 
AD2 3 PRO I 178 ? GLU I 187 ? PRO III 507 GLU III 516 
AD2 4 GLY I 102 ? ASN I 108 ? GLY III 431 ASN III 437 
AD2 5 THR I 47  ? TYR I 51  ? THR III 376 TYR III 380 
AD2 6 GLU J 102 ? SER J 103 ? GLU JJJ 102 SER JJJ 103 
AD3 1 CYS I 32  ? VAL I 33  ? CYS III 361 VAL III 362 
AD3 2 VAL I 195 ? CYS I 196 ? VAL III 524 CYS III 525 
AD3 3 CYS I 62  ? PHE I 63  ? CYS III 391 PHE III 392 
AD4 1 LEU I 123 ? ARG I 125 ? LEU III 452 ARG III 454 
AD4 2 LEU I 163 ? SER I 165 ? LEU III 492 SER III 494 
AD5 1 TYR I 144 ? GLN I 145 ? TYR III 473 GLN III 474 
AD5 2 CYS I 159 ? TYR I 160 ? CYS III 488 TYR III 489 
AD6 1 LEU J 4   ? SER J 7   ? LEU JJJ 4   SER JJJ 7   
AD6 2 LEU J 18  ? ALA J 24  ? LEU JJJ 18  ALA JJJ 24  
AD6 3 THR J 78  ? MET J 83  ? THR JJJ 78  MET JJJ 83  
AD6 4 PHE J 68  ? ASP J 73  ? PHE JJJ 68  ASP JJJ 73  
AD7 1 GLY J 10  ? GLN J 13  ? GLY JJJ 10  GLN JJJ 13  
AD7 2 THR J 119 ? SER J 124 ? THR JJJ 119 SER JJJ 124 
AD7 3 ALA J 92  ? ASP J 99  ? ALA JJJ 92  ASP JJJ 99  
AD7 4 VAL J 33  ? GLN J 39  ? VAL JJJ 33  GLN JJJ 39  
AD7 5 GLU J 46  ? ILE J 51  ? GLU JJJ 46  ILE JJJ 51  
AD7 6 THR J 58  ? TYR J 60  ? THR JJJ 58  TYR JJJ 60  
AD8 1 GLY J 10  ? GLN J 13  ? GLY JJJ 10  GLN JJJ 13  
AD8 2 THR J 119 ? SER J 124 ? THR JJJ 119 SER JJJ 124 
AD8 3 ALA J 92  ? ASP J 99  ? ALA JJJ 92  ASP JJJ 99  
AD8 4 PHE J 114 ? TRP J 115 ? PHE JJJ 114 TRP JJJ 115 
AD9 1 ASN K 25  ? ILE K 29  ? ASN KKK 354 ILE KKK 358 
AD9 2 ASN K 65  ? ARG K 74  ? ASN KKK 394 ARG KKK 403 
AD9 3 PRO K 178 ? GLU K 187 ? PRO KKK 507 GLU KKK 516 
AD9 4 GLY K 102 ? ASN K 108 ? GLY KKK 431 ASN KKK 437 
AD9 5 THR K 47  ? TYR K 51  ? THR KKK 376 TYR KKK 380 
AD9 6 GLU L 102 ? SER L 103 ? GLU LLL 102 SER LLL 103 
AE1 1 CYS K 32  ? VAL K 33  ? CYS KKK 361 VAL KKK 362 
AE1 2 VAL K 195 ? CYS K 196 ? VAL KKK 524 CYS KKK 525 
AE1 3 CYS K 62  ? PHE K 63  ? CYS KKK 391 PHE KKK 392 
AE2 1 LEU K 123 ? ARG K 125 ? LEU KKK 452 ARG KKK 454 
AE2 2 LEU K 163 ? SER K 165 ? LEU KKK 492 SER KKK 494 
AE3 1 TYR K 144 ? GLN K 145 ? TYR KKK 473 GLN KKK 474 
AE3 2 CYS K 159 ? TYR K 160 ? CYS KKK 488 TYR KKK 489 
AE4 1 LEU L 4   ? SER L 7   ? LEU LLL 4   SER LLL 7   
AE4 2 LEU L 18  ? ALA L 24  ? LEU LLL 18  ALA LLL 24  
AE4 3 THR L 78  ? MET L 83  ? THR LLL 78  MET LLL 83  
AE4 4 PHE L 68  ? ASP L 73  ? PHE LLL 68  ASP LLL 73  
AE5 1 GLY L 10  ? GLN L 13  ? GLY LLL 10  GLN LLL 13  
AE5 2 THR L 119 ? SER L 124 ? THR LLL 119 SER LLL 124 
AE5 3 ALA L 92  ? ASP L 99  ? ALA LLL 92  ASP LLL 99  
AE5 4 VAL L 33  ? GLN L 39  ? VAL LLL 33  GLN LLL 39  
AE5 5 GLU L 46  ? ILE L 51  ? GLU LLL 46  ILE LLL 51  
AE5 6 THR L 58  ? TYR L 60  ? THR LLL 58  TYR LLL 60  
AE6 1 GLY L 10  ? GLN L 13  ? GLY LLL 10  GLN LLL 13  
AE6 2 THR L 119 ? SER L 124 ? THR LLL 119 SER LLL 124 
AE6 3 ALA L 92  ? ASP L 99  ? ALA LLL 92  ASP LLL 99  
AE6 4 PHE L 114 ? TRP L 115 ? PHE LLL 114 TRP LLL 115 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 29  ? N ILE AAA 358 O VAL A 66  ? O VAL AAA 395 
AA1 2 3 N ILE A 73  ? N ILE AAA 402 O TYR A 179 ? O TYR AAA 508 
AA1 3 4 O VAL A 182 ? O VAL AAA 511 N ILE A 105 ? N ILE AAA 434 
AA1 4 5 O VAL A 104 ? O VAL AAA 433 N LYS A 49  ? N LYS AAA 378 
AA1 5 6 N CYS A 50  ? N CYS AAA 379 O GLU B 102 ? O GLU BBB 102 
AA2 1 2 N CYS A 32  ? N CYS AAA 361 O CYS A 196 ? O CYS AAA 525 
AA2 2 3 O VAL A 195 ? O VAL AAA 524 N PHE A 63  ? N PHE AAA 392 
AA3 1 2 N TYR A 124 ? N TYR AAA 453 O GLN A 164 ? O GLN AAA 493 
AA4 1 2 N TYR A 144 ? N TYR AAA 473 O TYR A 160 ? O TYR AAA 489 
AA5 1 2 N SER B 7   ? N SER BBB 7   O ALA B 21  ? O ALA BBB 21  
AA5 2 3 N LEU B 18  ? N LEU BBB 18  O MET B 83  ? O MET BBB 83  
AA5 3 4 O THR B 78  ? O THR BBB 78  N ASP B 73  ? N ASP BBB 73  
AA6 1 2 N GLY B 10  ? N GLY BBB 10  O THR B 122 ? O THR BBB 122 
AA6 2 3 O THR B 119 ? O THR BBB 119 N TYR B 94  ? N TYR BBB 94  
AA6 3 4 O ASP B 99  ? O ASP BBB 99  N VAL B 33  ? N VAL BBB 33  
AA6 4 5 N ARG B 38  ? N ARG BBB 38  O GLU B 46  ? O GLU BBB 46  
AA6 5 6 N ALA B 50  ? N ALA BBB 50  O TYR B 59  ? O TYR BBB 59  
AA7 1 2 N GLY B 10  ? N GLY BBB 10  O THR B 122 ? O THR BBB 122 
AA7 2 3 O THR B 119 ? O THR BBB 119 N TYR B 94  ? N TYR BBB 94  
AA7 3 4 N ALA B 98  ? N ALA BBB 98  O PHE B 114 ? O PHE BBB 114 
AA8 1 2 N ILE C 29  ? N ILE CCC 358 O VAL C 66  ? O VAL CCC 395 
AA8 2 3 N ILE C 73  ? N ILE CCC 402 O TYR C 179 ? O TYR CCC 508 
AA8 3 4 O LEU C 184 ? O LEU CCC 513 N CYS C 103 ? N CYS CCC 432 
AA8 4 5 O GLY C 102 ? O GLY CCC 431 N TYR C 51  ? N TYR CCC 380 
AA8 5 6 N CYS C 50  ? N CYS CCC 379 O GLU D 102 ? O GLU DDD 102 
AA9 1 2 N CYS C 32  ? N CYS CCC 361 O CYS C 196 ? O CYS CCC 525 
AA9 2 3 O VAL C 195 ? O VAL CCC 524 N PHE C 63  ? N PHE CCC 392 
AB1 1 2 N TYR C 124 ? N TYR CCC 453 O GLN C 164 ? O GLN CCC 493 
AB2 1 2 N TYR C 144 ? N TYR CCC 473 O TYR C 160 ? O TYR CCC 489 
AB3 1 2 N SER D 7   ? N SER DDD 7   O ALA D 21  ? O ALA DDD 21  
AB3 2 3 N LEU D 18  ? N LEU DDD 18  O MET D 83  ? O MET DDD 83  
AB3 3 4 O TYR D 80  ? O TYR DDD 80  N SER D 71  ? N SER DDD 71  
AB4 1 2 N GLY D 10  ? N GLY DDD 10  O THR D 122 ? O THR DDD 122 
AB4 2 3 O THR D 119 ? O THR DDD 119 N TYR D 94  ? N TYR DDD 94  
AB4 3 4 O ASP D 99  ? O ASP DDD 99  N VAL D 33  ? N VAL DDD 33  
AB4 4 5 N ARG D 38  ? N ARG DDD 38  O GLU D 46  ? O GLU DDD 46  
AB4 5 6 N ALA D 50  ? N ALA DDD 50  O TYR D 59  ? O TYR DDD 59  
AB5 1 2 N GLY D 10  ? N GLY DDD 10  O THR D 122 ? O THR DDD 122 
AB5 2 3 O THR D 119 ? O THR DDD 119 N TYR D 94  ? N TYR DDD 94  
AB5 3 4 N ALA D 98  ? N ALA DDD 98  O PHE D 114 ? O PHE DDD 114 
AB6 1 2 N ILE E 29  ? N ILE EEE 358 O VAL E 66  ? O VAL EEE 395 
AB6 2 3 N ILE E 73  ? N ILE EEE 402 O TYR E 179 ? O TYR EEE 508 
AB6 3 4 O VAL E 182 ? O VAL EEE 511 N ILE E 105 ? N ILE EEE 434 
AB6 4 5 O GLY E 102 ? O GLY EEE 431 N TYR E 51  ? N TYR EEE 380 
AB6 5 6 N CYS E 50  ? N CYS EEE 379 O GLU F 102 ? O GLU FFF 102 
AB7 1 2 N CYS E 32  ? N CYS EEE 361 O CYS E 196 ? O CYS EEE 525 
AB7 2 3 O VAL E 195 ? O VAL EEE 524 N PHE E 63  ? N PHE EEE 392 
AB8 1 2 N TYR E 124 ? N TYR EEE 453 O GLN E 164 ? O GLN EEE 493 
AB9 1 2 N TYR E 144 ? N TYR EEE 473 O TYR E 160 ? O TYR EEE 489 
AC1 1 2 N SER F 7   ? N SER FFF 7   O ALA F 21  ? O ALA FFF 21  
AC1 2 3 N LEU F 18  ? N LEU FFF 18  O MET F 83  ? O MET FFF 83  
AC1 3 4 O THR F 78  ? O THR FFF 78  N ASP F 73  ? N ASP FFF 73  
AC2 1 2 N GLY F 10  ? N GLY FFF 10  O THR F 122 ? O THR FFF 122 
AC2 2 3 O THR F 119 ? O THR FFF 119 N TYR F 94  ? N TYR FFF 94  
AC2 3 4 O ASP F 99  ? O ASP FFF 99  N VAL F 33  ? N VAL FFF 33  
AC2 4 5 N ARG F 38  ? N ARG FFF 38  O GLU F 46  ? O GLU FFF 46  
AC2 5 6 N ALA F 50  ? N ALA FFF 50  O TYR F 59  ? O TYR FFF 59  
AC3 1 2 N GLY F 10  ? N GLY FFF 10  O THR F 122 ? O THR FFF 122 
AC3 2 3 O THR F 119 ? O THR FFF 119 N TYR F 94  ? N TYR FFF 94  
AC3 3 4 N ALA F 98  ? N ALA FFF 98  O PHE F 114 ? O PHE FFF 114 
AC4 1 2 N ILE G 29  ? N ILE GGG 358 O VAL G 66  ? O VAL GGG 395 
AC4 2 3 N ILE G 73  ? N ILE GGG 402 O TYR G 179 ? O TYR GGG 508 
AC4 3 4 O VAL G 182 ? O VAL GGG 511 N ILE G 105 ? N ILE GGG 434 
AC4 4 5 O VAL G 104 ? O VAL GGG 433 N LYS G 49  ? N LYS GGG 378 
AC4 5 6 N CYS G 50  ? N CYS GGG 379 O GLU H 102 ? O GLU HHH 102 
AC5 1 2 N CYS G 32  ? N CYS GGG 361 O CYS G 196 ? O CYS GGG 525 
AC5 2 3 O VAL G 195 ? O VAL GGG 524 N PHE G 63  ? N PHE GGG 392 
AC6 1 2 N TYR G 124 ? N TYR GGG 453 O GLN G 164 ? O GLN GGG 493 
AC7 1 2 N TYR G 144 ? N TYR GGG 473 O TYR G 160 ? O TYR GGG 489 
AC8 1 2 N SER H 7   ? N SER HHH 7   O ALA H 21  ? O ALA HHH 21  
AC8 2 3 N LEU H 18  ? N LEU HHH 18  O MET H 83  ? O MET HHH 83  
AC8 3 4 O TYR H 80  ? O TYR HHH 80  N SER H 71  ? N SER HHH 71  
AC9 1 2 N GLY H 10  ? N GLY HHH 10  O THR H 122 ? O THR HHH 122 
AC9 2 3 O THR H 119 ? O THR HHH 119 N TYR H 94  ? N TYR HHH 94  
AC9 3 4 O ASP H 99  ? O ASP HHH 99  N VAL H 33  ? N VAL HHH 33  
AC9 4 5 N ARG H 38  ? N ARG HHH 38  O GLU H 46  ? O GLU HHH 46  
AC9 5 6 N ALA H 50  ? N ALA HHH 50  O TYR H 59  ? O TYR HHH 59  
AD1 1 2 N GLY H 10  ? N GLY HHH 10  O THR H 122 ? O THR HHH 122 
AD1 2 3 O THR H 119 ? O THR HHH 119 N TYR H 94  ? N TYR HHH 94  
AD1 3 4 N ALA H 98  ? N ALA HHH 98  O PHE H 114 ? O PHE HHH 114 
AD2 1 2 N ILE I 29  ? N ILE III 358 O VAL I 66  ? O VAL III 395 
AD2 2 3 N ILE I 73  ? N ILE III 402 O TYR I 179 ? O TYR III 508 
AD2 3 4 O LEU I 184 ? O LEU III 513 N CYS I 103 ? N CYS III 432 
AD2 4 5 O VAL I 104 ? O VAL III 433 N LYS I 49  ? N LYS III 378 
AD2 5 6 N CYS I 50  ? N CYS III 379 O GLU J 102 ? O GLU JJJ 102 
AD3 1 2 N CYS I 32  ? N CYS III 361 O CYS I 196 ? O CYS III 525 
AD3 2 3 O VAL I 195 ? O VAL III 524 N PHE I 63  ? N PHE III 392 
AD4 1 2 N TYR I 124 ? N TYR III 453 O GLN I 164 ? O GLN III 493 
AD5 1 2 N TYR I 144 ? N TYR III 473 O TYR I 160 ? O TYR III 489 
AD6 1 2 N SER J 7   ? N SER JJJ 7   O ALA J 21  ? O ALA JJJ 21  
AD6 2 3 N LEU J 18  ? N LEU JJJ 18  O MET J 83  ? O MET JJJ 83  
AD6 3 4 O TYR J 80  ? O TYR JJJ 80  N SER J 71  ? N SER JJJ 71  
AD7 1 2 N GLY J 10  ? N GLY JJJ 10  O THR J 122 ? O THR JJJ 122 
AD7 2 3 O THR J 119 ? O THR JJJ 119 N TYR J 94  ? N TYR JJJ 94  
AD7 3 4 O ASP J 99  ? O ASP JJJ 99  N VAL J 33  ? N VAL JJJ 33  
AD7 4 5 N ARG J 38  ? N ARG JJJ 38  O GLU J 46  ? O GLU JJJ 46  
AD7 5 6 N ALA J 50  ? N ALA JJJ 50  O TYR J 59  ? O TYR JJJ 59  
AD8 1 2 N GLY J 10  ? N GLY JJJ 10  O THR J 122 ? O THR JJJ 122 
AD8 2 3 O THR J 119 ? O THR JJJ 119 N TYR J 94  ? N TYR JJJ 94  
AD8 3 4 N ALA J 98  ? N ALA JJJ 98  O PHE J 114 ? O PHE JJJ 114 
AD9 1 2 N ILE K 29  ? N ILE KKK 358 O VAL K 66  ? O VAL KKK 395 
AD9 2 3 N ILE K 73  ? N ILE KKK 402 O TYR K 179 ? O TYR KKK 508 
AD9 3 4 O LEU K 184 ? O LEU KKK 513 N CYS K 103 ? N CYS KKK 432 
AD9 4 5 O VAL K 104 ? O VAL KKK 433 N LYS K 49  ? N LYS KKK 378 
AD9 5 6 N CYS K 50  ? N CYS KKK 379 O GLU L 102 ? O GLU LLL 102 
AE1 1 2 N CYS K 32  ? N CYS KKK 361 O CYS K 196 ? O CYS KKK 525 
AE1 2 3 O VAL K 195 ? O VAL KKK 524 N PHE K 63  ? N PHE KKK 392 
AE2 1 2 N TYR K 124 ? N TYR KKK 453 O GLN K 164 ? O GLN KKK 493 
AE3 1 2 N TYR K 144 ? N TYR KKK 473 O TYR K 160 ? O TYR KKK 489 
AE4 1 2 N SER L 7   ? N SER LLL 7   O ALA L 21  ? O ALA LLL 21  
AE4 2 3 N LEU L 18  ? N LEU LLL 18  O MET L 83  ? O MET LLL 83  
AE4 3 4 O TYR L 80  ? O TYR LLL 80  N SER L 71  ? N SER LLL 71  
AE5 1 2 N GLY L 10  ? N GLY LLL 10  O THR L 122 ? O THR LLL 122 
AE5 2 3 O THR L 119 ? O THR LLL 119 N TYR L 94  ? N TYR LLL 94  
AE5 3 4 O ASP L 99  ? O ASP LLL 99  N VAL L 33  ? N VAL LLL 33  
AE5 4 5 N ARG L 38  ? N ARG LLL 38  O GLU L 46  ? O GLU LLL 46  
AE5 5 6 N ALA L 50  ? N ALA LLL 50  O TYR L 59  ? O TYR LLL 59  
AE6 1 2 N GLY L 10  ? N GLY LLL 10  O THR L 122 ? O THR LLL 122 
AE6 2 3 O THR L 119 ? O THR LLL 119 N TYR L 94  ? N TYR LLL 94  
AE6 3 4 N ALA L 98  ? N ALA LLL 98  O PHE L 114 ? O PHE LLL 114 
# 
_atom_sites.entry_id                    7OAY 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.009223 
_atom_sites.fract_transf_matrix[1][2]   0.005325 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010650 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006041 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H 0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N 12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O 3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.049   
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM   1     N N   . ASN A  1 2   ? 34.997  -22.338  -26.549 1.000 97.266  0 331 ASN AAA N   1 ? ?  
ATOM   2     C CA  . ASN A  1 2   ? 35.497  -21.459  -25.447 1.000 99.944  0 331 ASN AAA CA  1 ? ?  
ATOM   3     C C   . ASN A  1 2   ? 34.413  -20.465  -25.018 1.000 101.159 0 331 ASN AAA C   1 ? ?  
ATOM   4     O O   . ASN A  1 2   ? 34.008  -19.631  -25.854 1.000 114.656 0 331 ASN AAA O   1 ? ?  
ATOM   5     C CB  . ASN A  1 2   ? 36.768  -20.694  -25.835 1.000 99.575  0 331 ASN AAA CB  1 ? ?  
ATOM   6     C CG  . ASN A  1 2   ? 38.012  -21.550  -25.720 1.000 105.948 0 331 ASN AAA CG  1 ? ?  
ATOM   7     O OD1 . ASN A  1 2   ? 37.972  -22.734  -26.050 1.000 104.495 0 331 ASN AAA OD1 1 ? ?  
ATOM   8     N ND2 . ASN A  1 2   ? 39.112  -20.974  -25.245 1.000 109.906 0 331 ASN AAA ND2 1 ? ?  
ATOM   9     N N   . ILE A  1 3   ? 33.972  -20.582  -23.763 1.000 93.339  0 332 ILE AAA N   1 ? ?  
ATOM   10    C CA  . ILE A  1 3   ? 33.077  -19.621  -23.047 1.000 83.684  0 332 ILE AAA CA  1 ? ?  
ATOM   11    C C   . ILE A  1 3   ? 33.825  -18.283  -22.885 1.000 77.274  0 332 ILE AAA C   1 ? ?  
ATOM   12    O O   . ILE A  1 3   ? 34.926  -18.298  -22.302 1.000 74.669  0 332 ILE AAA O   1 ? ?  
ATOM   13    C CB  . ILE A  1 3   ? 32.585  -20.234  -21.717 1.000 82.533  0 332 ILE AAA CB  1 ? ?  
ATOM   14    C CG1 . ILE A  1 3   ? 33.735  -20.553  -20.741 1.000 82.899  0 332 ILE AAA CG1 1 ? ?  
ATOM   15    C CG2 . ILE A  1 3   ? 31.717  -21.455  -22.035 1.000 78.801  0 332 ILE AAA CG2 1 ? ?  
ATOM   16    C CD1 . ILE A  1 3   ? 33.334  -20.872  -19.319 1.000 74.799  0 332 ILE AAA CD1 1 ? ?  
ATOM   17    N N   . THR A  1 4   ? 33.244  -17.182  -23.372 1.000 71.401  0 333 THR AAA N   1 ? ?  
ATOM   18    C CA  . THR A  1 4   ? 33.909  -15.888  -23.715 1.000 73.548  0 333 THR AAA CA  1 ? ?  
ATOM   19    C C   . THR A  1 4   ? 33.015  -14.697  -23.313 1.000 67.648  0 333 THR AAA C   1 ? ?  
ATOM   20    O O   . THR A  1 4   ? 33.544  -13.619  -22.963 1.000 75.291  0 333 THR AAA O   1 ? ?  
ATOM   21    C CB  . THR A  1 4   ? 34.327  -15.916  -25.192 1.000 79.746  0 333 THR AAA CB  1 ? ?  
ATOM   22    O OG1 . THR A  1 4   ? 33.363  -16.688  -25.914 1.000 79.854  0 333 THR AAA OG1 1 ? ?  
ATOM   23    C CG2 . THR A  1 4   ? 35.705  -16.517  -25.372 1.000 81.570  0 333 THR AAA CG2 1 ? ?  
ATOM   24    N N   . ASN A  1 5   ? 31.697  -14.879  -23.350 1.000 56.503  0 334 ASN AAA N   1 ? ?  
ATOM   25    C CA  . ASN A  1 5   ? 30.678  -13.888  -22.901 1.000 61.849  0 334 ASN AAA CA  1 ? ?  
ATOM   26    C C   . ASN A  1 5   ? 30.667  -13.809  -21.368 1.000 57.343  0 334 ASN AAA C   1 ? ?  
ATOM   27    O O   . ASN A  1 5   ? 30.681  -14.859  -20.722 1.000 53.060  0 334 ASN AAA O   1 ? ?  
ATOM   28    C CB  . ASN A  1 5   ? 29.285  -14.256  -23.412 1.000 67.084  0 334 ASN AAA CB  1 ? ?  
ATOM   29    C CG  . ASN A  1 5   ? 28.936  -15.690  -23.088 1.000 79.870  0 334 ASN AAA CG  1 ? ?  
ATOM   30    O OD1 . ASN A  1 5   ? 29.706  -16.586  -23.399 1.000 85.862  0 334 ASN AAA OD1 1 ? ?  
ATOM   31    N ND2 . ASN A  1 5   ? 27.801  -15.942  -22.453 1.000 84.486  0 334 ASN AAA ND2 1 ? ?  
ATOM   32    N N   . LEU A  1 6   ? 30.630  -12.608  -20.808 1.000 50.936  0 335 LEU AAA N   1 ? ?  
ATOM   33    C CA  . LEU A  1 6   ? 30.595  -12.377  -19.342 1.000 52.654  0 335 LEU AAA CA  1 ? ?  
ATOM   34    C C   . LEU A  1 6   ? 29.258  -12.836  -18.750 1.000 48.672  0 335 LEU AAA C   1 ? ?  
ATOM   35    O O   . LEU A  1 6   ? 28.235  -12.724  -19.419 1.000 47.823  0 335 LEU AAA O   1 ? ?  
ATOM   36    C CB  . LEU A  1 6   ? 30.850  -10.894  -19.053 1.000 52.018  0 335 LEU AAA CB  1 ? ?  
ATOM   37    C CG  . LEU A  1 6   ? 32.225  -10.369  -19.447 1.000 56.241  0 335 LEU AAA CG  1 ? ?  
ATOM   38    C CD1 . LEU A  1 6   ? 32.326  -8.882   -19.132 1.000 56.560  0 335 LEU AAA CD1 1 ? ?  
ATOM   39    C CD2 . LEU A  1 6   ? 33.326  -11.170  -18.747 1.000 58.585  0 335 LEU AAA CD2 1 ? ?  
ATOM   40    N N   . CYS A  1 7   ? 29.297  -13.388  -17.544 1.000 46.724  0 336 CYS AAA N   1 ? ?  
ATOM   41    C CA  . CYS A  1 7   ? 28.102  -13.834  -16.789 1.000 50.044  0 336 CYS AAA CA  1 ? ?  
ATOM   42    C C   . CYS A  1 7   ? 27.313  -12.572  -16.472 1.000 48.654  0 336 CYS AAA C   1 ? ?  
ATOM   43    O O   . CYS A  1 7   ? 27.895  -11.577  -16.046 1.000 46.237  0 336 CYS AAA O   1 ? ?  
ATOM   44    C CB  . CYS A  1 7   ? 28.449  -14.602  -15.511 1.000 51.448  0 336 CYS AAA CB  1 ? ?  
ATOM   45    S SG  . CYS A  1 7   ? 29.269  -16.201  -15.788 1.000 53.709  0 336 CYS AAA SG  1 ? ?  
ATOM   46    N N   . PRO A  1 8   ? 25.978  -12.581  -16.682 1.000 48.176  0 337 PRO AAA N   1 ? ?  
ATOM   47    C CA  . PRO A  1 8   ? 25.176  -11.368  -16.576 1.000 49.003  0 337 PRO AAA CA  1 ? ?  
ATOM   48    C C   . PRO A  1 8   ? 24.833  -11.026  -15.113 1.000 51.279  0 337 PRO AAA C   1 ? ?  
ATOM   49    O O   . PRO A  1 8   ? 23.699  -11.154  -14.719 1.000 56.552  0 337 PRO AAA O   1 ? ?  
ATOM   50    C CB  . PRO A  1 8   ? 23.960  -11.783  -17.419 1.000 49.750  0 337 PRO AAA CB  1 ? ?  
ATOM   51    C CG  . PRO A  1 8   ? 23.759  -13.254  -17.112 1.000 46.524  0 337 PRO AAA CG  1 ? ?  
ATOM   52    C CD  . PRO A  1 8   ? 25.167  -13.779  -16.979 1.000 47.959  0 337 PRO AAA CD  1 ? ?  
ATOM   53    N N   . PHE A  1 9   ? 25.833  -10.615  -14.332 1.000 45.797  0 338 PHE AAA N   1 ? ?  
ATOM   54    C CA  . PHE A  1 9   ? 25.658  -10.247  -12.904 1.000 44.679  0 338 PHE AAA CA  1 ? ?  
ATOM   55    C C   . PHE A  1 9   ? 24.753  -9.024   -12.746 1.000 43.034  0 338 PHE AAA C   1 ? ?  
ATOM   56    O O   . PHE A  1 9   ? 24.000  -8.976   -11.748 1.000 44.915  0 338 PHE AAA O   1 ? ?  
ATOM   57    C CB  . PHE A  1 9   ? 27.017  -10.069  -12.236 1.000 49.124  0 338 PHE AAA CB  1 ? ?  
ATOM   58    C CG  . PHE A  1 9   ? 27.706  -11.366  -11.901 1.000 52.415  0 338 PHE AAA CG  1 ? ?  
ATOM   59    C CD1 . PHE A  1 9   ? 27.009  -12.443  -11.362 1.000 55.900  0 338 PHE AAA CD1 1 ? ?  
ATOM   60    C CD2 . PHE A  1 9   ? 29.062  -11.507  -12.113 1.000 56.401  0 338 PHE AAA CD2 1 ? ?  
ATOM   61    C CE1 . PHE A  1 9   ? 27.668  -13.607  -11.015 1.000 56.749  0 338 PHE AAA CE1 1 ? ?  
ATOM   62    C CE2 . PHE A  1 9   ? 29.715  -12.680  -11.758 1.000 62.100  0 338 PHE AAA CE2 1 ? ?  
ATOM   63    C CZ  . PHE A  1 9   ? 29.013  -13.730  -11.225 1.000 57.789  0 338 PHE AAA CZ  1 ? ?  
ATOM   64    N N   . GLY A  1 10  ? 24.797  -8.091   -13.693 1.000 43.340  0 339 GLY AAA N   1 ? ?  
ATOM   65    C CA  . GLY A  1 10  ? 23.894  -6.919   -13.740 1.000 44.123  0 339 GLY AAA CA  1 ? ?  
ATOM   66    C C   . GLY A  1 10  ? 22.428  -7.322   -13.629 1.000 46.411  0 339 GLY AAA C   1 ? ?  
ATOM   67    O O   . GLY A  1 10  ? 21.693  -6.708   -12.838 1.000 46.574  0 339 GLY AAA O   1 ? ?  
ATOM   68    N N   . GLU A  1 11  ? 22.014  -8.343   -14.379 1.000 48.287  0 340 GLU AAA N   1 ? ?  
ATOM   69    C CA  . GLU A  1 11  ? 20.607  -8.825   -14.411 1.000 47.494  0 340 GLU AAA CA  1 ? ?  
ATOM   70    C C   . GLU A  1 11  ? 20.202  -9.394   -13.053 1.000 44.624  0 340 GLU AAA C   1 ? ?  
ATOM   71    O O   . GLU A  1 11  ? 18.992  -9.434   -12.796 1.000 47.398  0 340 GLU AAA O   1 ? ?  
ATOM   72    C CB  . GLU A  1 11  ? 20.427  -9.925   -15.448 1.000 56.253  0 340 GLU AAA CB  1 ? ?  
ATOM   73    C CG  . GLU A  1 11  ? 20.676  -9.472   -16.866 1.000 64.006  0 340 GLU AAA CG  1 ? ?  
ATOM   74    C CD  . GLU A  1 11  ? 20.422  -10.584  -17.876 1.000 71.989  0 340 GLU AAA CD  1 ? ?  
ATOM   75    O OE1 . GLU A  1 11  ? 19.838  -11.632  -17.483 1.000 70.298  0 340 GLU AAA OE1 1 ? ?  
ATOM   76    O OE2 . GLU A  1 11  ? 20.819  -10.419  -19.057 1.000 72.424  0 340 GLU AAA OE2 1 ? ?  
ATOM   77    N N   . VAL A  1 12  ? 21.153  -9.823   -12.226 1.000 40.982  0 341 VAL AAA N   1 ? ?  
ATOM   78    C CA  . VAL A  1 12  ? 20.896  -10.372  -10.864 1.000 39.866  0 341 VAL AAA CA  1 ? ?  
ATOM   79    C C   . VAL A  1 12  ? 20.829  -9.219   -9.852  1.000 39.322  0 341 VAL AAA C   1 ? ?  
ATOM   80    O O   . VAL A  1 12  ? 19.780  -9.055   -9.194  1.000 39.491  0 341 VAL AAA O   1 ? ?  
ATOM   81    C CB  . VAL A  1 12  ? 21.967  -11.398  -10.460 1.000 38.880  0 341 VAL AAA CB  1 ? ?  
ATOM   82    C CG1 . VAL A  1 12  ? 21.698  -11.952  -9.079  1.000 41.295  0 341 VAL AAA CG1 1 ? ?  
ATOM   83    C CG2 . VAL A  1 12  ? 22.079  -12.533  -11.451 1.000 37.886  0 341 VAL AAA CG2 1 ? ?  
ATOM   84    N N   . PHE A  1 13  ? 21.921  -8.469   -9.716  1.000 37.243  0 342 PHE AAA N   1 ? ?  
ATOM   85    C CA  . PHE A  1 13  ? 22.117  -7.475   -8.632  1.000 36.283  0 342 PHE AAA CA  1 ? ?  
ATOM   86    C C   . PHE A  1 13  ? 21.224  -6.249   -8.859  1.000 38.234  0 342 PHE AAA C   1 ? ?  
ATOM   87    O O   . PHE A  1 13  ? 20.787  -5.644   -7.866  1.000 41.927  0 342 PHE AAA O   1 ? ?  
ATOM   88    C CB  . PHE A  1 13  ? 23.598  -7.127   -8.519  1.000 35.761  0 342 PHE AAA CB  1 ? ?  
ATOM   89    C CG  . PHE A  1 13  ? 24.416  -8.187   -7.835  1.000 33.538  0 342 PHE AAA CG  1 ? ?  
ATOM   90    C CD1 . PHE A  1 13  ? 24.891  -9.282   -8.531  1.000 34.785  0 342 PHE AAA CD1 1 ? ?  
ATOM   91    C CD2 . PHE A  1 13  ? 24.706  -8.089   -6.484  1.000 34.830  0 342 PHE AAA CD2 1 ? ?  
ATOM   92    C CE1 . PHE A  1 13  ? 25.620  -10.270  -7.884  1.000 37.205  0 342 PHE AAA CE1 1 ? ?  
ATOM   93    C CE2 . PHE A  1 13  ? 25.447  -9.070   -5.843  1.000 35.572  0 342 PHE AAA CE2 1 ? ?  
ATOM   94    C CZ  . PHE A  1 13  ? 25.895  -10.165  -6.540  1.000 36.133  0 342 PHE AAA CZ  1 ? ?  
ATOM   95    N N   . ASN A  1 14  ? 20.946  -5.918   -10.119 1.000 38.135  0 343 ASN AAA N   1 ? ?  
ATOM   96    C CA  . ASN A  1 14  ? 20.176  -4.717   -10.542 1.000 39.514  0 343 ASN AAA CA  1 ? ?  
ATOM   97    C C   . ASN A  1 14  ? 18.877  -5.131   -11.255 1.000 40.520  0 343 ASN AAA C   1 ? ?  
ATOM   98    O O   . ASN A  1 14  ? 18.358  -4.348   -12.071 1.000 43.716  0 343 ASN AAA O   1 ? ?  
ATOM   99    C CB  . ASN A  1 14  ? 21.045  -3.809   -11.426 1.000 41.803  0 343 ASN AAA CB  1 ? ?  
ATOM   100   C CG  . ASN A  1 14  ? 22.130  -3.096   -10.641 1.000 44.570  0 343 ASN AAA CG  1 ? ?  
ATOM   101   O OD1 . ASN A  1 14  ? 21.914  -2.774   -9.472  1.000 48.168  0 343 ASN AAA OD1 1 ? ?  
ATOM   102   N ND2 . ASN A  1 14  ? 23.298  -2.872   -11.233 1.000 47.953  0 343 ASN AAA ND2 1 ? ?  
ATOM   103   N N   . ALA A  1 15  ? 18.366  -6.331   -11.009 1.000 40.849  0 344 ALA AAA N   1 ? ?  
ATOM   104   C CA  . ALA A  1 15  ? 17.019  -6.760   -11.468 1.000 40.402  0 344 ALA AAA CA  1 ? ?  
ATOM   105   C C   . ALA A  1 15  ? 16.013  -5.679   -11.078 1.000 40.605  0 344 ALA AAA C   1 ? ?  
ATOM   106   O O   . ALA A  1 15  ? 16.152  -5.124   -9.967  1.000 44.221  0 344 ALA AAA O   1 ? ?  
ATOM   107   C CB  . ALA A  1 15  ? 16.655  -8.104   -10.881 1.000 40.483  0 344 ALA AAA CB  1 ? ?  
ATOM   108   N N   . THR A  1 16  ? 15.064  -5.376   -11.947 1.000 42.924  0 345 THR AAA N   1 ? ?  
ATOM   109   C CA  . THR A  1 16  ? 14.070  -4.297   -11.714 1.000 46.357  0 345 THR AAA CA  1 ? ?  
ATOM   110   C C   . THR A  1 16  ? 13.115  -4.735   -10.593 1.000 45.859  0 345 THR AAA C   1 ? ?  
ATOM   111   O O   . THR A  1 16  ? 12.630  -3.852   -9.871  1.000 46.861  0 345 THR AAA O   1 ? ?  
ATOM   112   C CB  . THR A  1 16  ? 13.390  -3.933   -13.041 1.000 49.184  0 345 THR AAA CB  1 ? ?  
ATOM   113   O OG1 . THR A  1 16  ? 12.988  -5.163   -13.634 1.000 45.032  0 345 THR AAA OG1 1 ? ?  
ATOM   114   C CG2 . THR A  1 16  ? 14.305  -3.204   -14.003 1.000 49.870  0 345 THR AAA CG2 1 ? ?  
ATOM   115   N N   . ARG A  1 17  ? 12.904  -6.044   -10.421 1.000 45.766  0 346 ARG AAA N   1 ? ?  
ATOM   116   C CA  . ARG A  1 17  ? 12.059  -6.616   -9.343  1.000 44.819  0 346 ARG AAA CA  1 ? ?  
ATOM   117   C C   . ARG A  1 17  ? 12.888  -7.593   -8.505  1.000 38.434  0 346 ARG AAA C   1 ? ?  
ATOM   118   O O   . ARG A  1 17  ? 13.707  -8.330   -9.081  1.000 37.695  0 346 ARG AAA O   1 ? ?  
ATOM   119   C CB  . ARG A  1 17  ? 10.846  -7.346   -9.935  1.000 46.027  0 346 ARG AAA CB  1 ? ?  
ATOM   120   C CG  . ARG A  1 17  ? 9.538   -6.838   -9.361  1.000 51.217  0 346 ARG AAA CG  1 ? ?  
ATOM   121   C CD  . ARG A  1 17  ? 8.398   -7.678   -9.880  1.000 53.374  0 346 ARG AAA CD  1 ? ?  
ATOM   122   N NE  . ARG A  1 17  ? 8.076   -7.246   -11.234 1.000 51.166  0 346 ARG AAA NE  1 ? ?  
ATOM   123   C CZ  . ARG A  1 17  ? 7.235   -6.270   -11.548 1.000 48.712  0 346 ARG AAA CZ  1 ? ?  
ATOM   124   N NH1 . ARG A  1 17  ? 6.585   -5.609   -10.599 1.000 50.220  0 346 ARG AAA NH1 1 ? ?  
ATOM   125   N NH2 . ARG A  1 17  ? 7.018   -5.984   -12.823 1.000 48.537  0 346 ARG AAA NH2 1 ? ?  
ATOM   126   N N   . PHE A  1 18  ? 12.612  -7.674   -7.209  1.000 46.604  0 347 PHE AAA N   1 ? 1  
ATOM   127   C CA  . PHE A  1 18  ? 13.187  -8.679   -6.287  1.000 44.899  0 347 PHE AAA CA  1 ? 1  
ATOM   128   C C   . PHE A  1 18  ? 12.062  -9.465   -5.620  1.000 44.567  0 347 PHE AAA C   1 ? 1  
ATOM   129   O O   . PHE A  1 18  ? 11.012  -8.887   -5.336  1.000 44.261  0 347 PHE AAA O   1 ? 1  
ATOM   130   C CB  . PHE A  1 18  ? 14.090  -8.012   -5.242  1.000 44.346  0 347 PHE AAA CB  1 ? 1  
ATOM   131   C CG  . PHE A  1 18  ? 15.550  -7.992   -5.625  1.000 42.881  0 347 PHE AAA CG  1 ? 1  
ATOM   132   C CD1 . PHE A  1 18  ? 15.969  -7.239   -6.711  1.000 41.494  0 347 PHE AAA CD1 1 ? 1  
ATOM   133   C CD2 . PHE A  1 18  ? 16.493  -8.732   -4.894  1.000 42.654  0 347 PHE AAA CD2 1 ? 1  
ATOM   134   C CE1 . PHE A  1 18  ? 17.310  -7.209   -7.056  1.000 41.382  0 347 PHE AAA CE1 1 ? 1  
ATOM   135   C CE2 . PHE A  1 18  ? 17.830  -8.690   -5.251  1.000 41.463  0 347 PHE AAA CE2 1 ? 1  
ATOM   136   C CZ  . PHE A  1 18  ? 18.225  -7.953   -6.346  1.000 40.318  0 347 PHE AAA CZ  1 ? 1  
ATOM   137   N N   . ALA A  1 19  ? 12.286  -10.752  -5.377  1.000 44.520  0 348 ALA AAA N   1 ? 1  
ATOM   138   C CA  . ALA A  1 19  ? 11.268  -11.674  -4.821  1.000 43.868  0 348 ALA AAA CA  1 ? 1  
ATOM   139   C C   . ALA A  1 19  ? 11.090  -11.442  -3.320  1.000 43.335  0 348 ALA AAA C   1 ? 1  
ATOM   140   O O   . ALA A  1 19  ? 12.026  -10.994  -2.671  1.000 40.170  0 348 ALA AAA O   1 ? 1  
ATOM   141   C CB  . ALA A  1 19  ? 11.653  -13.106  -5.087  1.000 44.459  0 348 ALA AAA CB  1 ? 1  
ATOM   142   N N   . SER A  1 20  ? 9.901   -11.765  -2.809  1.000 43.705  0 349 SER AAA N   1 ? 1  
ATOM   143   C CA  . SER A  1 20  ? 9.685   -12.106  -1.383  1.000 44.232  0 349 SER AAA CA  1 ? 1  
ATOM   144   C C   . SER A  1 20  ? 10.577  -13.303  -1.031  1.000 43.374  0 349 SER AAA C   1 ? 1  
ATOM   145   O O   . SER A  1 20  ? 10.726  -14.233  -1.870  1.000 40.699  0 349 SER AAA O   1 ? 1  
ATOM   146   C CB  . SER A  1 20  ? 8.242   -12.413  -1.093  1.000 44.002  0 349 SER AAA CB  1 ? 1  
ATOM   147   O OG  . SER A  1 20  ? 7.457   -11.252  -1.130  1.000 44.606  0 349 SER AAA OG  1 ? 1  
ATOM   148   N N   . VAL A  1 21  ? 11.130  -13.301  0.174   1.000 42.261  0 350 VAL AAA N   1 ? 1  
ATOM   149   C CA  . VAL A  1 21  ? 12.043  -14.380  0.640   1.000 41.951  0 350 VAL AAA CA  1 ? 1  
ATOM   150   C C   . VAL A  1 21  ? 11.365  -15.758  0.545   1.000 43.291  0 350 VAL AAA C   1 ? 1  
ATOM   151   O O   . VAL A  1 21  ? 12.051  -16.717  0.152   1.000 44.107  0 350 VAL AAA O   1 ? 1  
ATOM   152   C CB  . VAL A  1 21  ? 12.576  -14.076  2.045   1.000 41.416  0 350 VAL AAA CB  1 ? 1  
ATOM   153   C CG1 . VAL A  1 21  ? 11.446  -14.069  3.079   1.000 41.136  0 350 VAL AAA CG1 1 ? 1  
ATOM   154   C CG2 . VAL A  1 21  ? 13.736  -15.016  2.408   1.000 39.212  0 350 VAL AAA CG2 1 ? 1  
ATOM   155   N N   . TYR A  1 22  ? 10.077  -15.893  0.877   1.000 43.880  0 351 TYR AAA N   1 ? 1  
ATOM   156   C CA  . TYR A  1 22  ? 9.403   -17.218  0.905   1.000 44.625  0 351 TYR AAA CA  1 ? 1  
ATOM   157   C C   . TYR A  1 22  ? 9.345   -17.770  -0.527  1.000 44.411  0 351 TYR AAA C   1 ? 1  
ATOM   158   O O   . TYR A  1 22  ? 9.380   -19.012  -0.694  1.000 45.587  0 351 TYR AAA O   1 ? 1  
ATOM   159   C CB  . TYR A  1 22  ? 8.018   -17.125  1.561   1.000 46.027  0 351 TYR AAA CB  1 ? 1  
ATOM   160   C CG  . TYR A  1 22  ? 6.930   -16.720  0.606   1.000 45.536  0 351 TYR AAA CG  1 ? 1  
ATOM   161   C CD1 . TYR A  1 22  ? 6.699   -15.388  0.317   1.000 45.347  0 351 TYR AAA CD1 1 ? 1  
ATOM   162   C CD2 . TYR A  1 22  ? 6.166   -17.670  -0.049  1.000 46.868  0 351 TYR AAA CD2 1 ? 1  
ATOM   163   C CE1 . TYR A  1 22  ? 5.719   -15.001  -0.590  1.000 45.011  0 351 TYR AAA CE1 1 ? 1  
ATOM   164   C CE2 . TYR A  1 22  ? 5.187   -17.309  -0.961  1.000 46.115  0 351 TYR AAA CE2 1 ? 1  
ATOM   165   C CZ  . TYR A  1 22  ? 4.967   -15.973  -1.229  1.000 45.586  0 351 TYR AAA CZ  1 ? 1  
ATOM   166   O OH  . TYR A  1 22  ? 3.998   -15.631  -2.112  1.000 46.118  0 351 TYR AAA OH  1 ? 1  
ATOM   167   N N   . ALA A  1 23  ? 9.260   -16.877  -1.518  1.000 43.887  0 352 ALA AAA N   1 ? 1  
ATOM   168   C CA  . ALA A  1 23  ? 9.180   -17.203  -2.962  1.000 44.882  0 352 ALA AAA CA  1 ? 1  
ATOM   169   C C   . ALA A  1 23  ? 10.484  -16.786  -3.654  1.000 42.950  0 352 ALA AAA C   1 ? 1  
ATOM   170   O O   . ALA A  1 23  ? 10.435  -16.198  -4.730  1.000 43.386  0 352 ALA AAA O   1 ? 1  
ATOM   171   C CB  . ALA A  1 23  ? 7.980   -16.521  -3.576  1.000 45.480  0 352 ALA AAA CB  1 ? 1  
ATOM   172   N N   . TRP A  1 24  ? 11.613  -17.100  -3.037  1.000 42.340  0 353 TRP AAA N   1 ? 1  
ATOM   173   C CA  . TRP A  1 24  ? 12.944  -16.633  -3.481  1.000 40.613  0 353 TRP AAA CA  1 ? 1  
ATOM   174   C C   . TRP A  1 24  ? 13.192  -17.045  -4.926  1.000 40.777  0 353 TRP AAA C   1 ? 1  
ATOM   175   O O   . TRP A  1 24  ? 12.778  -18.125  -5.330  1.000 41.776  0 353 TRP AAA O   1 ? 1  
ATOM   176   C CB  . TRP A  1 24  ? 14.045  -17.124  -2.544  1.000 39.177  0 353 TRP AAA CB  1 ? 1  
ATOM   177   C CG  . TRP A  1 24  ? 14.024  -18.576  -2.202  1.000 39.087  0 353 TRP AAA CG  1 ? 1  
ATOM   178   C CD1 . TRP A  1 24  ? 13.401  -19.183  -1.149  1.000 39.724  0 353 TRP AAA CD1 1 ? 1  
ATOM   179   C CD2 . TRP A  1 24  ? 14.748  -19.604  -2.883  1.000 39.531  0 353 TRP AAA CD2 1 ? 1  
ATOM   180   N NE1 . TRP A  1 24  ? 13.675  -20.527  -1.134  1.000 39.836  0 353 TRP AAA NE1 1 ? 1  
ATOM   181   C CE2 . TRP A  1 24  ? 14.510  -20.811  -2.181  1.000 40.878  0 353 TRP AAA CE2 1 ? 1  
ATOM   182   C CE3 . TRP A  1 24  ? 15.579  -19.619  -4.005  1.000 39.146  0 353 TRP AAA CE3 1 ? 1  
ATOM   183   C CZ2 . TRP A  1 24  ? 15.069  -22.024  -2.589  1.000 42.344  0 353 TRP AAA CZ2 1 ? 1  
ATOM   184   C CZ3 . TRP A  1 24  ? 16.122  -20.823  -4.398  1.000 40.717  0 353 TRP AAA CZ3 1 ? 1  
ATOM   185   C CH2 . TRP A  1 24  ? 15.881  -22.000  -3.700  1.000 41.902  0 353 TRP AAA CH2 1 ? 1  
ATOM   186   N N   . ASN A  1 25  ? 13.829  -16.160  -5.677  1.000 40.895  0 354 ASN AAA N   1 ? 1  
ATOM   187   C CA  . ASN A  1 25  ? 14.069  -16.302  -7.129  1.000 43.053  0 354 ASN AAA CA  1 ? 1  
ATOM   188   C C   . ASN A  1 25  ? 15.439  -16.961  -7.328  1.000 43.797  0 354 ASN AAA C   1 ? 1  
ATOM   189   O O   . ASN A  1 25  ? 16.383  -16.615  -6.579  1.000 44.546  0 354 ASN AAA O   1 ? 1  
ATOM   190   C CB  . ASN A  1 25  ? 13.980  -14.925  -7.769  1.000 44.191  0 354 ASN AAA CB  1 ? 1  
ATOM   191   C CG  . ASN A  1 25  ? 14.245  -14.949  -9.248  1.000 45.631  0 354 ASN AAA CG  1 ? 1  
ATOM   192   O OD1 . ASN A  1 25  ? 15.381  -14.799  -9.693  1.000 47.657  0 354 ASN AAA OD1 1 ? 1  
ATOM   193   N ND2 . ASN A  1 25  ? 13.201  -15.200  -10.002 1.000 48.201  0 354 ASN AAA ND2 1 ? 1  
ATOM   194   N N   . ARG A  1 26  ? 15.513  -17.904  -8.272  1.000 44.288  0 355 ARG AAA N   1 ? 1  
ATOM   195   C CA  . ARG A  1 26  ? 16.748  -18.569  -8.774  1.000 45.722  0 355 ARG AAA CA  1 ? 1  
ATOM   196   C C   . ARG A  1 26  ? 17.026  -18.134  -10.212 1.000 47.559  0 355 ARG AAA C   1 ? 1  
ATOM   197   O O   . ARG A  1 26  ? 16.178  -18.435  -11.084 1.000 47.513  0 355 ARG AAA O   1 ? 1  
ATOM   198   C CB  . ARG A  1 26  ? 16.572  -20.042  -9.122  1.000 47.280  0 355 ARG AAA CB  1 ? 1  
ATOM   199   C CG  . ARG A  1 26  ? 16.974  -21.001  -8.039  1.000 48.356  0 355 ARG AAA CG  1 ? 1  
ATOM   200   C CD  . ARG A  1 26  ? 18.043  -21.966  -8.376  1.000 48.351  0 355 ARG AAA CD  1 ? 1  
ATOM   201   N NE  . ARG A  1 26  ? 18.711  -21.995  -7.079  1.000 48.225  0 355 ARG AAA NE  1 ? 1  
ATOM   202   C CZ  . ARG A  1 26  ? 18.989  -23.036  -6.352  1.000 47.300  0 355 ARG AAA CZ  1 ? 1  
ATOM   203   N NH1 . ARG A  1 26  ? 18.737  -24.237  -6.819  1.000 51.308  0 355 ARG AAA NH1 1 ? 1  
ATOM   204   N NH2 . ARG A  1 26  ? 19.629  -22.868  -5.196  1.000 47.948  0 355 ARG AAA NH2 1 ? 1  
ATOM   205   N N   . LYS A  1 27  ? 18.219  -17.629  -10.486 1.000 48.718  0 356 LYS AAA N   1 ? 1  
ATOM   206   C CA  . LYS A  1 27  ? 18.718  -17.548  -11.871 1.000 51.028  0 356 LYS AAA CA  1 ? 1  
ATOM   207   C C   . LYS A  1 27  ? 19.894  -18.513  -11.969 1.000 50.778  0 356 LYS AAA C   1 ? 1  
ATOM   208   O O   . LYS A  1 27  ? 20.759  -18.534  -11.082 1.000 48.741  0 356 LYS AAA O   1 ? 1  
ATOM   209   C CB  . LYS A  1 27  ? 19.053  -16.106  -12.223 1.000 54.582  0 356 LYS AAA CB  1 ? 1  
ATOM   210   C CG  . LYS A  1 27  ? 17.916  -15.121  -11.981 1.000 60.017  0 356 LYS AAA CG  1 ? 1  
ATOM   211   C CD  . LYS A  1 27  ? 18.285  -13.688  -12.349 1.000 62.519  0 356 LYS AAA CD  1 ? 1  
ATOM   212   C CE  . LYS A  1 27  ? 17.154  -12.716  -12.086 1.000 65.769  0 356 LYS AAA CE  1 ? 1  
ATOM   213   N NZ  . LYS A  1 27  ? 16.993  -12.455  -10.632 1.000 65.391  0 356 LYS AAA NZ  1 ? 1  
ATOM   214   N N   . ARG A  1 28  ? 19.884  -19.347  -12.994 1.000 54.446  0 357 ARG AAA N   1 ? 1  
ATOM   215   C CA  . ARG A  1 28  ? 21.026  -20.222  -13.326 1.000 54.430  0 357 ARG AAA CA  1 ? 1  
ATOM   216   C C   . ARG A  1 28  ? 22.071  -19.385  -14.050 1.000 50.546  0 357 ARG AAA C   1 ? 1  
ATOM   217   O O   . ARG A  1 28  ? 21.697  -18.618  -14.945 1.000 47.881  0 357 ARG AAA O   1 ? 1  
ATOM   218   C CB  . ARG A  1 28  ? 20.543  -21.387  -14.177 1.000 60.843  0 357 ARG AAA CB  1 ? 1  
ATOM   219   C CG  . ARG A  1 28  ? 21.601  -22.452  -14.369 1.000 66.700  0 357 ARG AAA CG  1 ? 1  
ATOM   220   C CD  . ARG A  1 28  ? 20.933  -23.751  -14.813 1.000 74.715  0 357 ARG AAA CD  1 ? 1  
ATOM   221   N NE  . ARG A  1 28  ? 21.904  -24.178  -15.795 1.000 84.968  0 357 ARG AAA NE  1 ? 1  
ATOM   222   C CZ  . ARG A  1 28  ? 22.759  -25.176  -15.655 1.000 92.252  0 357 ARG AAA CZ  1 ? 1  
ATOM   223   N NH1 . ARG A  1 28  ? 22.681  -25.954  -14.586 1.000 97.683  0 357 ARG AAA NH1 1 ? 1  
ATOM   224   N NH2 . ARG A  1 28  ? 23.687  -25.389  -16.578 1.000 90.160  0 357 ARG AAA NH2 1 ? 1  
ATOM   225   N N   . ILE A  1 29  ? 23.325  -19.515  -13.650 1.000 48.361  0 358 ILE AAA N   1 ? 1  
ATOM   226   C CA  . ILE A  1 29  ? 24.467  -18.884  -14.358 1.000 48.335  0 358 ILE AAA CA  1 ? 1  
ATOM   227   C C   . ILE A  1 29  ? 25.327  -20.015  -14.919 1.000 50.262  0 358 ILE AAA C   1 ? 1  
ATOM   228   O O   . ILE A  1 29  ? 25.765  -20.867  -14.122 1.000 52.857  0 358 ILE AAA O   1 ? 1  
ATOM   229   C CB  . ILE A  1 29  ? 25.208  -17.933  -13.409 1.000 46.961  0 358 ILE AAA CB  1 ? 1  
ATOM   230   C CG1 . ILE A  1 29  ? 24.307  -16.753  -13.058 1.000 46.877  0 358 ILE AAA CG1 1 ? 1  
ATOM   231   C CG2 . ILE A  1 29  ? 26.519  -17.472  -14.003 1.000 46.222  0 358 ILE AAA CG2 1 ? 1  
ATOM   232   C CD1 . ILE A  1 29  ? 24.825  -15.895  -11.953 1.000 47.216  0 358 ILE AAA CD1 1 ? 1  
ATOM   233   N N   . SER A  1 30  ? 25.532  -20.046  -16.232 1.000 50.663  0 359 SER AAA N   1 ? 1  
ATOM   234   C CA  . SER A  1 30  ? 26.353  -21.094  -16.900 1.000 53.092  0 359 SER AAA CA  1 ? 1  
ATOM   235   C C   . SER A  1 30  ? 26.832  -20.611  -18.261 1.000 52.565  0 359 SER AAA C   1 ? 1  
ATOM   236   O O   . SER A  1 30  ? 26.280  -19.650  -18.796 1.000 49.824  0 359 SER AAA O   1 ? 1  
ATOM   237   C CB  . SER A  1 30  ? 25.563  -22.375  -17.048 1.000 56.728  0 359 SER AAA CB  1 ? 1  
ATOM   238   O OG  . SER A  1 30  ? 24.288  -22.093  -17.568 1.000 57.367  0 359 SER AAA OG  1 ? 1  
ATOM   239   N N   . ASN A  1 31  ? 27.839  -21.293  -18.784 1.000 54.812  0 360 ASN AAA N   1 ? 1  
ATOM   240   C CA  . ASN A  1 31  ? 28.402  -21.064  -20.141 1.000 59.699  0 360 ASN AAA CA  1 ? 1  
ATOM   241   C C   . ASN A  1 31  ? 28.717  -19.587  -20.261 1.000 56.444  0 360 ASN AAA C   1 ? 1  
ATOM   242   O O   . ASN A  1 31  ? 28.210  -18.967  -21.188 1.000 55.905  0 360 ASN AAA O   1 ? 1  
ATOM   243   C CB  . ASN A  1 31  ? 27.477  -21.619  -21.215 1.000 64.109  0 360 ASN AAA CB  1 ? 1  
ATOM   244   C CG  . ASN A  1 31  ? 27.269  -23.109  -21.011 1.000 68.588  0 360 ASN AAA CG  1 ? 1  
ATOM   245   O OD1 . ASN A  1 31  ? 26.131  -23.572  -20.932 1.000 71.555  0 360 ASN AAA OD1 1 ? 1  
ATOM   246   N ND2 . ASN A  1 31  ? 28.357  -23.856  -20.827 1.000 71.200  0 360 ASN AAA ND2 1 ? 1  
ATOM   247   N N   . CYS A  1 32  ? 29.501  -19.086  -19.310 1.000 54.652  0 361 CYS AAA N   1 ? 1  
ATOM   248   C CA  . CYS A  1 32  ? 29.892  -17.668  -19.220 1.000 52.915  0 361 CYS AAA CA  1 ? 1  
ATOM   249   C C   . CYS A  1 32  ? 31.128  -17.501  -18.326 1.000 50.175  0 361 CYS AAA C   1 ? 1  
ATOM   250   O O   . CYS A  1 32  ? 31.391  -18.367  -17.516 1.000 50.271  0 361 CYS AAA O   1 ? 1  
ATOM   251   C CB  . CYS A  1 32  ? 28.712  -16.822  -18.759 1.000 52.962  0 361 CYS AAA CB  1 ? 1  
ATOM   252   S SG  . CYS A  1 32  ? 28.080  -17.259  -17.131 1.000 54.390  0 361 CYS AAA SG  1 ? 1  
ATOM   253   N N   . VAL A  1 33  ? 31.871  -16.417  -18.553 1.000 48.160  0 362 VAL AAA N   1 ? 1  
ATOM   254   C CA  . VAL A  1 33  ? 33.033  -15.962  -17.740 1.000 46.401  0 362 VAL AAA CA  1 ? 1  
ATOM   255   C C   . VAL A  1 33  ? 32.508  -15.127  -16.566 1.000 44.837  0 362 VAL AAA C   1 ? 1  
ATOM   256   O O   . VAL A  1 33  ? 31.867  -14.114  -16.825 1.000 45.049  0 362 VAL AAA O   1 ? 1  
ATOM   257   C CB  . VAL A  1 33  ? 34.028  -15.159  -18.590 1.000 45.694  0 362 VAL AAA CB  1 ? 1  
ATOM   258   C CG1 . VAL A  1 33  ? 35.220  -14.710  -17.755 1.000 46.069  0 362 VAL AAA CG1 1 ? 1  
ATOM   259   C CG2 . VAL A  1 33  ? 34.494  -15.966  -19.779 1.000 46.261  0 362 VAL AAA CG2 1 ? 1  
ATOM   260   N N   . ALA A  1 34  ? 32.739  -15.569  -15.336 1.000 44.612  0 363 ALA AAA N   1 ? 1  
ATOM   261   C CA  . ALA A  1 34  ? 32.327  -14.874  -14.092 1.000 45.891  0 363 ALA AAA CA  1 ? 1  
ATOM   262   C C   . ALA A  1 34  ? 33.411  -13.850  -13.720 1.000 45.825  0 363 ALA AAA C   1 ? 1  
ATOM   263   O O   . ALA A  1 34  ? 34.408  -14.247  -13.111 1.000 45.037  0 363 ALA AAA O   1 ? 1  
ATOM   264   C CB  . ALA A  1 34  ? 32.085  -15.873  -12.972 1.000 46.611  0 363 ALA AAA CB  1 ? 1  
ATOM   265   N N   . ASP A  1 35  ? 33.238  -12.606  -14.148 1.000 46.693  0 364 ASP AAA N   1 ? 1  
ATOM   266   C CA  . ASP A  1 35  ? 34.119  -11.497  -13.724 1.000 47.946  0 364 ASP AAA CA  1 ? 1  
ATOM   267   C C   . ASP A  1 35  ? 33.523  -10.828  -12.492 1.000 46.079  0 364 ASP AAA C   1 ? 1  
ATOM   268   O O   . ASP A  1 35  ? 32.509  -10.131  -12.626 1.000 46.405  0 364 ASP AAA O   1 ? 1  
ATOM   269   C CB  . ASP A  1 35  ? 34.352  -10.464  -14.824 1.000 49.411  0 364 ASP AAA CB  1 ? 1  
ATOM   270   C CG  . ASP A  1 35  ? 35.589  -9.658   -14.508 1.000 50.791  0 364 ASP AAA CG  1 ? 1  
ATOM   271   O OD1 . ASP A  1 35  ? 36.048  -9.749   -13.349 1.000 53.869  0 364 ASP AAA OD1 1 ? 1  
ATOM   272   O OD2 . ASP A  1 35  ? 36.101  -9.004   -15.408 1.000 55.334  0 364 ASP AAA OD2 1 ? 1  
ATOM   273   N N   . TYR A  1 36  ? 34.174  -11.010  -11.352 1.000 46.276  0 365 TYR AAA N   1 ? 1  
ATOM   274   C CA  . TYR A  1 36  ? 33.694  -10.519  -10.039 1.000 49.053  0 365 TYR AAA CA  1 ? 1  
ATOM   275   C C   . TYR A  1 36  ? 34.236  -9.114   -9.769  1.000 48.530  0 365 TYR AAA C   1 ? 1  
ATOM   276   O O   . TYR A  1 36  ? 33.886  -8.579   -8.732  1.000 48.253  0 365 TYR AAA O   1 ? 1  
ATOM   277   C CB  . TYR A  1 36  ? 34.087  -11.495  -8.927  1.000 49.476  0 365 TYR AAA CB  1 ? 1  
ATOM   278   C CG  . TYR A  1 36  ? 33.291  -12.760  -8.968  1.000 51.146  0 365 TYR AAA CG  1 ? 1  
ATOM   279   C CD1 . TYR A  1 36  ? 32.088  -12.853  -8.299  1.000 51.923  0 365 TYR AAA CD1 1 ? 1  
ATOM   280   C CD2 . TYR A  1 36  ? 33.716  -13.847  -9.711  1.000 53.096  0 365 TYR AAA CD2 1 ? 1  
ATOM   281   C CE1 . TYR A  1 36  ? 31.336  -14.016  -8.333  1.000 52.138  0 365 TYR AAA CE1 1 ? 1  
ATOM   282   C CE2 . TYR A  1 36  ? 32.976  -15.016  -9.761  1.000 53.429  0 365 TYR AAA CE2 1 ? 1  
ATOM   283   C CZ  . TYR A  1 36  ? 31.785  -15.097  -9.064  1.000 51.330  0 365 TYR AAA CZ  1 ? 1  
ATOM   284   O OH  . TYR A  1 36  ? 31.056  -16.240  -9.088  1.000 53.069  0 365 TYR AAA OH  1 ? 1  
ATOM   285   N N   . SER A  1 37  ? 35.058  -8.544   -10.647 1.000 48.801  0 366 SER AAA N   1 ? 1  
ATOM   286   C CA  . SER A  1 37  ? 35.709  -7.238   -10.359 1.000 52.633  0 366 SER AAA CA  1 ? 1  
ATOM   287   C C   . SER A  1 37  ? 34.647  -6.136   -10.233 1.000 52.100  0 366 SER AAA C   1 ? 1  
ATOM   288   O O   . SER A  1 37  ? 34.876  -5.183   -9.493  1.000 51.957  0 366 SER AAA O   1 ? 1  
ATOM   289   C CB  . SER A  1 37  ? 36.786  -6.874   -11.361 1.000 52.955  0 366 SER AAA CB  1 ? 1  
ATOM   290   O OG  . SER A  1 37  ? 36.374  -7.199   -12.666 1.000 51.681  0 366 SER AAA OG  1 ? 1  
ATOM   291   N N   . VAL A  1 38  ? 33.490  -6.289   -10.865 1.000 52.415  0 367 VAL AAA N   1 ? 1  
ATOM   292   C CA  . VAL A  1 38  ? 32.371  -5.324   -10.706 1.000 53.001  0 367 VAL AAA CA  1 ? 1  
ATOM   293   C C   . VAL A  1 38  ? 31.931  -5.341   -9.224  1.000 52.974  0 367 VAL AAA C   1 ? 1  
ATOM   294   O O   . VAL A  1 38  ? 31.765  -4.259   -8.653  1.000 54.620  0 367 VAL AAA O   1 ? 1  
ATOM   295   C CB  . VAL A  1 38  ? 31.248  -5.642   -11.713 1.000 55.841  0 367 VAL AAA CB  1 ? 1  
ATOM   296   C CG1 . VAL A  1 38  ? 30.532  -6.969   -11.406 1.000 56.589  0 367 VAL AAA CG1 1 ? 1  
ATOM   297   C CG2 . VAL A  1 38  ? 30.264  -4.496   -11.832 1.000 56.696  0 367 VAL AAA CG2 1 ? 1  
ATOM   298   N N   . LEU A  1 39  ? 31.828  -6.512   -8.593  1.000 51.772  0 368 LEU AAA N   1 ? 1  
ATOM   299   C CA  . LEU A  1 39  ? 31.455  -6.663   -7.167  1.000 52.867  0 368 LEU AAA CA  1 ? 1  
ATOM   300   C C   . LEU A  1 39  ? 32.599  -6.197   -6.247  1.000 55.384  0 368 LEU AAA C   1 ? 1  
ATOM   301   O O   . LEU A  1 39  ? 32.301  -5.645   -5.172  1.000 59.479  0 368 LEU AAA O   1 ? 1  
ATOM   302   C CB  . LEU A  1 39  ? 31.095  -8.122   -6.899  1.000 51.861  0 368 LEU AAA CB  1 ? 1  
ATOM   303   C CG  . LEU A  1 39  ? 29.956  -8.687   -7.746  1.000 52.123  0 368 LEU AAA CG  1 ? 1  
ATOM   304   C CD1 . LEU A  1 39  ? 29.690  -10.125  -7.337  1.000 53.057  0 368 LEU AAA CD1 1 ? 1  
ATOM   305   C CD2 . LEU A  1 39  ? 28.662  -7.904   -7.572  1.000 52.263  0 368 LEU AAA CD2 1 ? 1  
ATOM   306   N N   . TYR A  1 40  ? 33.855  -6.430   -6.622  1.000 51.549  0 369 TYR AAA N   1 ? 2  
ATOM   307   C CA  . TYR A  1 40  ? 35.056  -6.074   -5.817  1.000 52.330  0 369 TYR AAA CA  1 ? 2  
ATOM   308   C C   . TYR A  1 40  ? 35.138  -4.556   -5.621  1.000 53.484  0 369 TYR AAA C   1 ? 2  
ATOM   309   O O   . TYR A  1 40  ? 35.666  -4.119   -4.587  1.000 52.907  0 369 TYR AAA O   1 ? 2  
ATOM   310   C CB  . TYR A  1 40  ? 36.350  -6.537   -6.496  1.000 53.979  0 369 TYR AAA CB  1 ? 2  
ATOM   311   C CG  . TYR A  1 40  ? 36.602  -8.020   -6.528  1.000 54.387  0 369 TYR AAA CG  1 ? 2  
ATOM   312   C CD1 . TYR A  1 40  ? 36.127  -8.855   -5.522  1.000 52.862  0 369 TYR AAA CD1 1 ? 2  
ATOM   313   C CD2 . TYR A  1 40  ? 37.373  -8.582   -7.531  1.000 56.945  0 369 TYR AAA CD2 1 ? 2  
ATOM   314   C CE1 . TYR A  1 40  ? 36.425  -10.208  -5.506  1.000 53.543  0 369 TYR AAA CE1 1 ? 2  
ATOM   315   C CE2 . TYR A  1 40  ? 37.637  -9.940   -7.553  1.000 59.097  0 369 TYR AAA CE2 1 ? 2  
ATOM   316   C CZ  . TYR A  1 40  ? 37.186  -10.750  -6.525  1.000 56.498  0 369 TYR AAA CZ  1 ? 2  
ATOM   317   O OH  . TYR A  1 40  ? 37.498  -12.074  -6.526  1.000 58.710  0 369 TYR AAA OH  1 ? 2  
ATOM   318   N N   . ASN A  1 41  ? 34.630  -3.785   -6.586  1.000 53.224  0 370 ASN AAA N   1 ? 2  
ATOM   319   C CA  . ASN A  1 41  ? 34.771  -2.306   -6.646  1.000 54.700  0 370 ASN AAA CA  1 ? 2  
ATOM   320   C C   . ASN A  1 41  ? 33.544  -1.619   -6.039  1.000 52.006  0 370 ASN AAA C   1 ? 2  
ATOM   321   O O   . ASN A  1 41  ? 33.431  -0.400   -6.187  1.000 52.990  0 370 ASN AAA O   1 ? 2  
ATOM   322   C CB  . ASN A  1 41  ? 34.990  -1.840   -8.085  1.000 58.229  0 370 ASN AAA CB  1 ? 2  
ATOM   323   C CG  . ASN A  1 41  ? 36.306  -2.343   -8.644  1.000 61.737  0 370 ASN AAA CG  1 ? 2  
ATOM   324   O OD1 . ASN A  1 41  ? 37.312  -2.349   -7.942  1.000 64.854  0 370 ASN AAA OD1 1 ? 2  
ATOM   325   N ND2 . ASN A  1 41  ? 36.311  -2.773   -9.895  1.000 63.990  0 370 ASN AAA ND2 1 ? 2  
ATOM   326   N N   . SER A  1 42  ? 32.644  -2.373   -5.413  1.000 50.144  0 371 SER AAA N   1 ? 2  
ATOM   327   C CA  . SER A  1 42  ? 31.449  -1.869   -4.687  1.000 49.020  0 371 SER AAA CA  1 ? 2  
ATOM   328   C C   . SER A  1 42  ? 31.827  -1.656   -3.219  1.000 47.699  0 371 SER AAA C   1 ? 2  
ATOM   329   O O   . SER A  1 42  ? 32.483  -2.561   -2.631  1.000 46.936  0 371 SER AAA O   1 ? 2  
ATOM   330   C CB  . SER A  1 42  ? 30.298  -2.834   -4.821  1.000 48.555  0 371 SER AAA CB  1 ? 2  
ATOM   331   O OG  . SER A  1 42  ? 29.942  -2.995   -6.185  1.000 48.884  0 371 SER AAA OG  1 ? 2  
ATOM   332   N N   . ALA A  1 43  ? 31.422  -0.517   -2.666  1.000 47.990  0 372 ALA AAA N   1 ? 2  
ATOM   333   C CA  . ALA A  1 43  ? 31.610  -0.163   -1.243  1.000 49.755  0 372 ALA AAA CA  1 ? 2  
ATOM   334   C C   . ALA A  1 43  ? 30.280  -0.265   -0.482  1.000 49.343  0 372 ALA AAA C   1 ? 2  
ATOM   335   O O   . ALA A  1 43  ? 30.348  -0.205   0.748   1.000 57.356  0 372 ALA AAA O   1 ? 2  
ATOM   336   C CB  . ALA A  1 43  ? 32.233  1.211    -1.109  1.000 50.531  0 372 ALA AAA CB  1 ? 2  
ATOM   337   N N   . SER A  1 44  ? 29.123  -0.375   -1.153  1.000 46.755  0 373 SER AAA N   1 ? 2  
ATOM   338   C CA  . SER A  1 44  ? 27.803  -0.211   -0.484  1.000 46.662  0 373 SER AAA CA  1 ? 2  
ATOM   339   C C   . SER A  1 44  ? 27.220  -1.548   -0.015  1.000 43.359  0 373 SER AAA C   1 ? 2  
ATOM   340   O O   . SER A  1 44  ? 26.222  -1.533   0.685   1.000 44.830  0 373 SER AAA O   1 ? 2  
ATOM   341   C CB  . SER A  1 44  ? 26.835  0.545    -1.329  1.000 49.729  0 373 SER AAA CB  1 ? 2  
ATOM   342   O OG  . SER A  1 44  ? 27.013  1.945    -1.129  1.000 54.875  0 373 SER AAA OG  1 ? 2  
ATOM   343   N N   . PHE A  1 45  ? 27.795  -2.691   -0.357  1.000 40.662  0 374 PHE AAA N   1 ? 2  
ATOM   344   C CA  . PHE A  1 45  ? 27.347  -4.000   0.181   1.000 39.712  0 374 PHE AAA CA  1 ? 2  
ATOM   345   C C   . PHE A  1 45  ? 27.546  -4.008   1.709   1.000 38.871  0 374 PHE AAA C   1 ? 2  
ATOM   346   O O   . PHE A  1 45  ? 28.608  -3.639   2.176   1.000 36.738  0 374 PHE AAA O   1 ? 2  
ATOM   347   C CB  . PHE A  1 45  ? 28.108  -5.148   -0.497  1.000 36.847  0 374 PHE AAA CB  1 ? 2  
ATOM   348   C CG  . PHE A  1 45  ? 27.838  -5.314   -1.971  1.000 34.845  0 374 PHE AAA CG  1 ? 2  
ATOM   349   C CD1 . PHE A  1 45  ? 26.569  -5.166   -2.491  1.000 34.648  0 374 PHE AAA CD1 1 ? 2  
ATOM   350   C CD2 . PHE A  1 45  ? 28.851  -5.695   -2.829  1.000 35.276  0 374 PHE AAA CD2 1 ? 2  
ATOM   351   C CE1 . PHE A  1 45  ? 26.328  -5.349   -3.839  1.000 36.585  0 374 PHE AAA CE1 1 ? 2  
ATOM   352   C CE2 . PHE A  1 45  ? 28.614  -5.881   -4.176  1.000 35.328  0 374 PHE AAA CE2 1 ? 2  
ATOM   353   C CZ  . PHE A  1 45  ? 27.358  -5.694   -4.684  1.000 36.129  0 374 PHE AAA CZ  1 ? 2  
ATOM   354   N N   . SER A  1 46  ? 26.520  -4.407   2.452   1.000 41.537  0 375 SER AAA N   1 ? 2  
ATOM   355   C CA  . SER A  1 46  ? 26.530  -4.504   3.943   1.000 43.232  0 375 SER AAA CA  1 ? 2  
ATOM   356   C C   . SER A  1 46  ? 27.317  -5.743   4.383   1.000 41.231  0 375 SER AAA C   1 ? 2  
ATOM   357   O O   . SER A  1 46  ? 27.886  -5.709   5.462   1.000 42.484  0 375 SER AAA O   1 ? 2  
ATOM   358   C CB  . SER A  1 46  ? 25.139  -4.539   4.521   1.000 45.454  0 375 SER AAA CB  1 ? 2  
ATOM   359   O OG  . SER A  1 46  ? 24.381  -5.593   3.947   1.000 42.938  0 375 SER AAA OG  1 ? 2  
ATOM   360   N N   . THR A  1 47  ? 27.342  -6.777   3.554   1.000 38.501  0 376 THR AAA N   1 ? 2  
ATOM   361   C CA  . THR A  1 47  ? 28.067  -8.038   3.815   1.000 36.947  0 376 THR AAA CA  1 ? 2  
ATOM   362   C C   . THR A  1 47  ? 28.460  -8.659   2.462   1.000 35.938  0 376 THR AAA C   1 ? 2  
ATOM   363   O O   . THR A  1 47  ? 27.730  -8.499   1.458   1.000 32.683  0 376 THR AAA O   1 ? 2  
ATOM   364   C CB  . THR A  1 47  ? 27.204  -8.965   4.684   1.000 37.345  0 376 THR AAA CB  1 ? 2  
ATOM   365   O OG1 . THR A  1 47  ? 28.014  -10.020  5.217   1.000 35.105  0 376 THR AAA OG1 1 ? 2  
ATOM   366   C CG2 . THR A  1 47  ? 26.001  -9.503   3.917   1.000 39.157  0 376 THR AAA CG2 1 ? 2  
ATOM   367   N N   . PHE A  1 48  ? 29.595  -9.331   2.433   1.000 34.893  0 377 PHE AAA N   1 ? 2  
ATOM   368   C CA  . PHE A  1 48  ? 30.093  -10.047  1.241   1.000 36.667  0 377 PHE AAA CA  1 ? 2  
ATOM   369   C C   . PHE A  1 48  ? 31.013  -11.121  1.799   1.000 36.880  0 377 PHE AAA C   1 ? 2  
ATOM   370   O O   . PHE A  1 48  ? 32.218  -10.801  2.084   1.000 35.534  0 377 PHE AAA O   1 ? 2  
ATOM   371   C CB  . PHE A  1 48  ? 30.773  -9.069   0.280   1.000 38.632  0 377 PHE AAA CB  1 ? 2  
ATOM   372   C CG  . PHE A  1 48  ? 31.361  -9.644   -0.992  1.000 41.878  0 377 PHE AAA CG  1 ? 2  
ATOM   373   C CD1 . PHE A  1 48  ? 31.531  -11.005  -1.180  1.000 43.821  0 377 PHE AAA CD1 1 ? 2  
ATOM   374   C CD2 . PHE A  1 48  ? 31.747  -8.801   -2.018  1.000 44.972  0 377 PHE AAA CD2 1 ? 2  
ATOM   375   C CE1 . PHE A  1 48  ? 32.075  -11.504  -2.353  1.000 47.066  0 377 PHE AAA CE1 1 ? 2  
ATOM   376   C CE2 . PHE A  1 48  ? 32.296  -9.295   -3.194  1.000 47.753  0 377 PHE AAA CE2 1 ? 2  
ATOM   377   C CZ  . PHE A  1 48  ? 32.470  -10.649  -3.357  1.000 50.254  0 377 PHE AAA CZ  1 ? 2  
ATOM   378   N N   . LYS A  1 49  ? 30.443  -12.298  2.059   1.000 35.008  0 378 LYS AAA N   1 ? 2  
ATOM   379   C CA  . LYS A  1 49  ? 31.210  -13.431  2.600   1.000 38.334  0 378 LYS AAA CA  1 ? 2  
ATOM   380   C C   . LYS A  1 49  ? 31.101  -14.633  1.669   1.000 39.306  0 378 LYS AAA C   1 ? 2  
ATOM   381   O O   . LYS A  1 49  ? 29.998  -14.905  1.144   1.000 40.508  0 378 LYS AAA O   1 ? 2  
ATOM   382   C CB  . LYS A  1 49  ? 30.645  -13.850  3.948   1.000 40.890  0 378 LYS AAA CB  1 ? 2  
ATOM   383   C CG  . LYS A  1 49  ? 30.717  -12.827  5.056   1.000 42.254  0 378 LYS AAA CG  1 ? 2  
ATOM   384   C CD  . LYS A  1 49  ? 30.083  -13.391  6.296   1.000 42.241  0 378 LYS AAA CD  1 ? 2  
ATOM   385   C CE  . LYS A  1 49  ? 30.160  -12.445  7.457   1.000 42.437  0 378 LYS AAA CE  1 ? 2  
ATOM   386   N NZ  . LYS A  1 49  ? 29.466  -13.040  8.610   1.000 44.852  0 378 LYS AAA NZ  1 ? 2  
ATOM   387   N N   . CYS A  1 50  ? 32.185  -15.382  1.562   1.000 37.616  0 379 CYS AAA N   1 ? 3  
ATOM   388   C CA  . CYS A  1 50  ? 32.203  -16.685  0.845   1.000 37.281  0 379 CYS AAA CA  1 ? 3  
ATOM   389   C C   . CYS A  1 50  ? 32.481  -17.794  1.865   1.000 36.800  0 379 CYS AAA C   1 ? 3  
ATOM   390   O O   . CYS A  1 50  ? 33.073  -17.535  2.945   1.000 32.739  0 379 CYS AAA O   1 ? 3  
ATOM   391   C CB  . CYS A  1 50  ? 33.186  -16.654  -0.317  1.000 38.280  0 379 CYS AAA CB  1 ? 3  
ATOM   392   S SG  . CYS A  1 50  ? 32.827  -15.301  -1.469  1.000 39.910  0 379 CYS AAA SG  1 ? 3  
ATOM   393   N N   . TYR A  1 51  ? 31.999  -18.984  1.513   1.000 38.377  0 380 TYR AAA N   1 ? 3  
ATOM   394   C CA  . TYR A  1 51  ? 32.081  -20.235  2.295   1.000 38.167  0 380 TYR AAA CA  1 ? 3  
ATOM   395   C C   . TYR A  1 51  ? 32.671  -21.304  1.381   1.000 37.702  0 380 TYR AAA C   1 ? 3  
ATOM   396   O O   . TYR A  1 51  ? 32.149  -21.483  0.270   1.000 41.832  0 380 TYR AAA O   1 ? 3  
ATOM   397   C CB  . TYR A  1 51  ? 30.673  -20.551  2.801   1.000 38.721  0 380 TYR AAA CB  1 ? 3  
ATOM   398   C CG  . TYR A  1 51  ? 30.045  -19.444  3.610   1.000 37.820  0 380 TYR AAA CG  1 ? 3  
ATOM   399   C CD1 . TYR A  1 51  ? 29.370  -18.413  2.993   1.000 35.123  0 380 TYR AAA CD1 1 ? 3  
ATOM   400   C CD2 . TYR A  1 51  ? 30.141  -19.423  4.989   1.000 37.887  0 380 TYR AAA CD2 1 ? 3  
ATOM   401   C CE1 . TYR A  1 51  ? 28.782  -17.400  3.718   1.000 35.467  0 380 TYR AAA CE1 1 ? 3  
ATOM   402   C CE2 . TYR A  1 51  ? 29.560  -18.414  5.735   1.000 37.441  0 380 TYR AAA CE2 1 ? 3  
ATOM   403   C CZ  . TYR A  1 51  ? 28.860  -17.406  5.099   1.000 37.273  0 380 TYR AAA CZ  1 ? 3  
ATOM   404   O OH  . TYR A  1 51  ? 28.258  -16.422  5.826   1.000 36.590  0 380 TYR AAA OH  1 ? 3  
ATOM   405   N N   . GLY A  1 52  ? 33.745  -21.968  1.794   1.000 37.638  0 381 GLY AAA N   1 ? 3  
ATOM   406   C CA  . GLY A  1 52  ? 34.357  -23.050  1.000   1.000 38.288  0 381 GLY AAA CA  1 ? 3  
ATOM   407   C C   . GLY A  1 52  ? 35.295  -22.539  -0.088  1.000 38.547  0 381 GLY AAA C   1 ? 3  
ATOM   408   O O   . GLY A  1 52  ? 36.016  -23.349  -0.631  1.000 40.089  0 381 GLY AAA O   1 ? 3  
ATOM   409   N N   . VAL A  1 53  ? 35.313  -21.240  -0.375  1.000 38.708  0 382 VAL AAA N   1 ? 3  
ATOM   410   C CA  . VAL A  1 53  ? 36.319  -20.596  -1.262  1.000 43.204  0 382 VAL AAA CA  1 ? 3  
ATOM   411   C C   . VAL A  1 53  ? 36.615  -19.200  -0.730  1.000 41.262  0 382 VAL AAA C   1 ? 3  
ATOM   412   O O   . VAL A  1 53  ? 35.708  -18.581  -0.187  1.000 44.851  0 382 VAL AAA O   1 ? 3  
ATOM   413   C CB  . VAL A  1 53  ? 35.835  -20.529  -2.720  1.000 43.988  0 382 VAL AAA CB  1 ? 3  
ATOM   414   C CG1 . VAL A  1 53  ? 35.744  -21.920  -3.309  1.000 46.596  0 382 VAL AAA CG1 1 ? 3  
ATOM   415   C CG2 . VAL A  1 53  ? 34.510  -19.796  -2.846  1.000 43.085  0 382 VAL AAA CG2 1 ? 3  
ATOM   416   N N   . SER A  1 54  ? 37.822  -18.711  -0.936  1.000 39.957  0 383 SER AAA N   1 ? 3  
ATOM   417   C CA  . SER A  1 54  ? 38.200  -17.340  -0.547  1.000 40.902  0 383 SER AAA CA  1 ? 3  
ATOM   418   C C   . SER A  1 54  ? 37.635  -16.370  -1.580  1.000 40.246  0 383 SER AAA C   1 ? 3  
ATOM   419   O O   . SER A  1 54  ? 37.729  -16.627  -2.783  1.000 40.154  0 383 SER AAA O   1 ? 3  
ATOM   420   C CB  . SER A  1 54  ? 39.691  -17.213  -0.421  1.000 44.088  0 383 SER AAA CB  1 ? 3  
ATOM   421   O OG  . SER A  1 54  ? 40.028  -15.869  -0.129  1.000 45.806  0 383 SER AAA OG  1 ? 3  
ATOM   422   N N   . PRO A  1 55  ? 37.036  -15.237  -1.154  1.000 39.536  0 384 PRO AAA N   1 ? 3  
ATOM   423   C CA  . PRO A  1 55  ? 36.617  -14.186  -2.081  1.000 39.778  0 384 PRO AAA CA  1 ? 3  
ATOM   424   C C   . PRO A  1 55  ? 37.743  -13.712  -3.008  1.000 40.535  0 384 PRO AAA C   1 ? 3  
ATOM   425   O O   . PRO A  1 55  ? 37.457  -13.274  -4.115  1.000 40.237  0 384 PRO AAA O   1 ? 3  
ATOM   426   C CB  . PRO A  1 55  ? 36.197  -13.030  -1.158  1.000 39.861  0 384 PRO AAA CB  1 ? 3  
ATOM   427   C CG  . PRO A  1 55  ? 35.799  -13.701  0.133   1.000 39.099  0 384 PRO AAA CG  1 ? 3  
ATOM   428   C CD  . PRO A  1 55  ? 36.698  -14.914  0.240   1.000 39.728  0 384 PRO AAA CD  1 ? 3  
ATOM   429   N N   . THR A  1 56  ? 38.988  -13.816  -2.542  1.000 41.754  0 385 THR AAA N   1 ? 3  
ATOM   430   C CA  . THR A  1 56  ? 40.199  -13.386  -3.287  1.000 45.579  0 385 THR AAA CA  1 ? 3  
ATOM   431   C C   . THR A  1 56  ? 40.442  -14.314  -4.484  1.000 46.055  0 385 THR AAA C   1 ? 3  
ATOM   432   O O   . THR A  1 56  ? 41.244  -13.942  -5.337  1.000 47.305  0 385 THR AAA O   1 ? 3  
ATOM   433   C CB  . THR A  1 56  ? 41.442  -13.334  -2.386  1.000 47.087  0 385 THR AAA CB  1 ? 3  
ATOM   434   O OG1 . THR A  1 56  ? 41.801  -14.650  -1.941  1.000 47.338  0 385 THR AAA OG1 1 ? 3  
ATOM   435   C CG2 . THR A  1 56  ? 41.263  -12.402  -1.205  1.000 47.385  0 385 THR AAA CG2 1 ? 3  
ATOM   436   N N   . LYS A  1 57  ? 39.802  -15.480  -4.542  1.000 46.054  0 386 LYS AAA N   1 ? 3  
ATOM   437   C CA  . LYS A  1 57  ? 40.099  -16.469  -5.608  1.000 48.008  0 386 LYS AAA CA  1 ? 3  
ATOM   438   C C   . LYS A  1 57  ? 38.943  -16.586  -6.595  1.000 44.887  0 386 LYS AAA C   1 ? 3  
ATOM   439   O O   . LYS A  1 57  ? 39.081  -17.358  -7.496  1.000 43.555  0 386 LYS AAA O   1 ? 3  
ATOM   440   C CB  . LYS A  1 57  ? 40.409  -17.840  -5.005  1.000 51.520  0 386 LYS AAA CB  1 ? 3  
ATOM   441   C CG  . LYS A  1 57  ? 41.560  -17.879  -4.001  1.000 55.331  0 386 LYS AAA CG  1 ? 3  
ATOM   442   C CD  . LYS A  1 57  ? 42.939  -17.889  -4.589  1.000 59.053  0 386 LYS AAA CD  1 ? 3  
ATOM   443   C CE  . LYS A  1 57  ? 43.228  -19.100  -5.446  1.000 63.153  0 386 LYS AAA CE  1 ? 3  
ATOM   444   N NZ  . LYS A  1 57  ? 43.937  -18.691  -6.683  1.000 65.402  0 386 LYS AAA NZ  1 ? 3  
ATOM   445   N N   . LEU A  1 58  ? 37.863  -15.826  -6.453  1.000 43.252  0 387 LEU AAA N   1 ? 3  
ATOM   446   C CA  . LEU A  1 58  ? 36.653  -16.019  -7.299  1.000 44.040  0 387 LEU AAA CA  1 ? 3  
ATOM   447   C C   . LEU A  1 58  ? 36.996  -15.865  -8.785  1.000 43.926  0 387 LEU AAA C   1 ? 3  
ATOM   448   O O   . LEU A  1 58  ? 36.390  -16.571  -9.598  1.000 45.334  0 387 LEU AAA O   1 ? 3  
ATOM   449   C CB  . LEU A  1 58  ? 35.552  -15.038  -6.884  1.000 44.706  0 387 LEU AAA CB  1 ? 3  
ATOM   450   C CG  . LEU A  1 58  ? 34.949  -15.298  -5.505  1.000 44.809  0 387 LEU AAA CG  1 ? 3  
ATOM   451   C CD1 . LEU A  1 58  ? 33.868  -14.278  -5.204  1.000 43.455  0 387 LEU AAA CD1 1 ? 3  
ATOM   452   C CD2 . LEU A  1 58  ? 34.392  -16.708  -5.391  1.000 45.390  0 387 LEU AAA CD2 1 ? 3  
ATOM   453   N N   . ASN A  1 59  ? 37.937  -15.004  -9.144  1.000 45.295  0 388 ASN AAA N   1 ? 3  
ATOM   454   C CA  . ASN A  1 59  ? 38.293  -14.773  -10.567 1.000 49.317  0 388 ASN AAA CA  1 ? 3  
ATOM   455   C C   . ASN A  1 59  ? 39.181  -15.903  -11.111 1.000 51.599  0 388 ASN AAA C   1 ? 3  
ATOM   456   O O   . ASN A  1 59  ? 39.422  -15.887  -12.294 1.000 53.493  0 388 ASN AAA O   1 ? 3  
ATOM   457   C CB  . ASN A  1 59  ? 38.899  -13.392  -10.786 1.000 48.791  0 388 ASN AAA CB  1 ? 3  
ATOM   458   C CG  . ASN A  1 59  ? 37.831  -12.354  -11.060 1.000 48.502  0 388 ASN AAA CG  1 ? 3  
ATOM   459   O OD1 . ASN A  1 59  ? 36.669  -12.672  -11.301 1.000 47.533  0 388 ASN AAA OD1 1 ? 3  
ATOM   460   N ND2 . ASN A  1 59  ? 38.216  -11.100  -11.067 1.000 50.363  0 388 ASN AAA ND2 1 ? 3  
ATOM   461   N N   . ASP A  1 60  ? 39.574  -16.884  -10.307 1.000 53.881  0 389 ASP AAA N   1 ? 3  
ATOM   462   C CA  . ASP A  1 60  ? 40.509  -17.967  -10.713 1.000 55.635  0 389 ASP AAA CA  1 ? 3  
ATOM   463   C C   . ASP A  1 60  ? 39.825  -19.334  -10.692 1.000 53.131  0 389 ASP AAA C   1 ? 3  
ATOM   464   O O   . ASP A  1 60  ? 40.512  -20.297  -11.010 1.000 53.296  0 389 ASP AAA O   1 ? 3  
ATOM   465   C CB  . ASP A  1 60  ? 41.730  -18.044  -9.789  1.000 60.017  0 389 ASP AAA CB  1 ? 3  
ATOM   466   C CG  . ASP A  1 60  ? 42.510  -16.742  -9.753  1.000 65.528  0 389 ASP AAA CG  1 ? 3  
ATOM   467   O OD1 . ASP A  1 60  ? 42.987  -16.314  -10.840 1.000 74.002  0 389 ASP AAA OD1 1 ? 3  
ATOM   468   O OD2 . ASP A  1 60  ? 42.586  -16.122  -8.655  1.000 73.525  0 389 ASP AAA OD2 1 ? 3  
ATOM   469   N N   . LEU A  1 61  ? 38.549  -19.427  -10.334 1.000 50.111  0 390 LEU AAA N   1 ? 3  
ATOM   470   C CA  . LEU A  1 61  ? 37.919  -20.739  -10.064 1.000 50.260  0 390 LEU AAA CA  1 ? 3  
ATOM   471   C C   . LEU A  1 61  ? 36.868  -21.072  -11.112 1.000 49.510  0 390 LEU AAA C   1 ? 3  
ATOM   472   O O   . LEU A  1 61  ? 36.268  -20.185  -11.665 1.000 50.246  0 390 LEU AAA O   1 ? 3  
ATOM   473   C CB  . LEU A  1 61  ? 37.311  -20.746  -8.657  1.000 49.499  0 390 LEU AAA CB  1 ? 3  
ATOM   474   C CG  . LEU A  1 61  ? 38.300  -20.638  -7.508  1.000 49.196  0 390 LEU AAA CG  1 ? 3  
ATOM   475   C CD1 . LEU A  1 61  ? 37.521  -20.652  -6.204  1.000 50.691  0 390 LEU AAA CD1 1 ? 3  
ATOM   476   C CD2 . LEU A  1 61  ? 39.321  -21.763  -7.547  1.000 49.462  0 390 LEU AAA CD2 1 ? 3  
ATOM   477   N N   . CYS A  1 62  ? 36.725  -22.367  -11.367 1.000 50.043  0 391 CYS AAA N   1 ? 3  
ATOM   478   C CA  . CYS A  1 62  ? 35.784  -22.966  -12.335 1.000 49.552  0 391 CYS AAA CA  1 ? 3  
ATOM   479   C C   . CYS A  1 62  ? 34.788  -23.828  -11.559 1.000 46.584  0 391 CYS AAA C   1 ? 3  
ATOM   480   O O   . CYS A  1 62  ? 35.198  -24.452  -10.589 1.000 45.035  0 391 CYS AAA O   1 ? 3  
ATOM   481   C CB  . CYS A  1 62  ? 36.541  -23.783  -13.369 1.000 52.907  0 391 CYS AAA CB  1 ? 3  
ATOM   482   S SG  . CYS A  1 62  ? 37.554  -22.748  -14.463 1.000 55.023  0 391 CYS AAA SG  1 ? 3  
ATOM   483   N N   . PHE A  1 63  ? 33.525  -23.780  -11.952 1.000 44.870  0 392 PHE AAA N   1 ? 3  
ATOM   484   C CA  . PHE A  1 63  ? 32.409  -24.497  -11.303 1.000 44.693  0 392 PHE AAA CA  1 ? 3  
ATOM   485   C C   . PHE A  1 63  ? 31.577  -25.176  -12.389 1.000 46.901  0 392 PHE AAA C   1 ? 3  
ATOM   486   O O   . PHE A  1 63  ? 31.595  -24.700  -13.560 1.000 48.073  0 392 PHE AAA O   1 ? 3  
ATOM   487   C CB  . PHE A  1 63  ? 31.585  -23.539  -10.440 1.000 42.291  0 392 PHE AAA CB  1 ? 3  
ATOM   488   C CG  . PHE A  1 63  ? 32.413  -22.878  -9.368  1.000 40.300  0 392 PHE AAA CG  1 ? 3  
ATOM   489   C CD1 . PHE A  1 63  ? 32.880  -23.606  -8.288  1.000 40.551  0 392 PHE AAA CD1 1 ? 3  
ATOM   490   C CD2 . PHE A  1 63  ? 32.757  -21.543  -9.444  1.000 39.178  0 392 PHE AAA CD2 1 ? 3  
ATOM   491   C CE1 . PHE A  1 63  ? 33.627  -23.003  -7.289  1.000 40.338  0 392 PHE AAA CE1 1 ? 3  
ATOM   492   C CE2 . PHE A  1 63  ? 33.518  -20.949  -8.452  1.000 39.326  0 392 PHE AAA CE2 1 ? 3  
ATOM   493   C CZ  . PHE A  1 63  ? 33.966  -21.683  -7.380  1.000 39.749  0 392 PHE AAA CZ  1 ? 3  
ATOM   494   N N   . THR A  1 64  ? 30.937  -26.286  -12.006 1.000 46.618  0 393 THR AAA N   1 ? 3  
ATOM   495   C CA  . THR A  1 64  ? 30.066  -27.077  -12.898 1.000 48.428  0 393 THR AAA CA  1 ? 3  
ATOM   496   C C   . THR A  1 64  ? 28.772  -26.318  -13.120 1.000 47.953  0 393 THR AAA C   1 ? 3  
ATOM   497   O O   . THR A  1 64  ? 28.223  -26.408  -14.215 1.000 47.843  0 393 THR AAA O   1 ? 3  
ATOM   498   C CB  . THR A  1 64  ? 29.897  -28.482  -12.331 1.000 48.597  0 393 THR AAA CB  1 ? 3  
ATOM   499   O OG1 . THR A  1 64  ? 29.537  -28.519  -10.948 1.000 46.232  0 393 THR AAA OG1 1 ? 3  
ATOM   500   C CG2 . THR A  1 64  ? 31.213  -29.213  -12.495 1.000 50.469  0 393 THR AAA CG2 1 ? 3  
ATOM   501   N N   . ASN A  1 65  ? 28.339  -25.583  -12.103 1.000 48.564  0 394 ASN AAA N   1 ? 3  
ATOM   502   C CA  . ASN A  1 65  ? 27.061  -24.842  -12.113 1.000 49.164  0 394 ASN AAA CA  1 ? 3  
ATOM   503   C C   . ASN A  1 65  ? 27.142  -23.697  -11.113 1.000 45.676  0 394 ASN AAA C   1 ? 3  
ATOM   504   O O   . ASN A  1 65  ? 27.836  -23.885  -10.083 1.000 44.376  0 394 ASN AAA O   1 ? 3  
ATOM   505   C CB  . ASN A  1 65  ? 25.902  -25.784  -11.778 1.000 55.793  0 394 ASN AAA CB  1 ? 3  
ATOM   506   C CG  . ASN A  1 65  ? 24.559  -25.178  -12.117 1.000 60.968  0 394 ASN AAA CG  1 ? 3  
ATOM   507   O OD1 . ASN A  1 65  ? 24.251  -24.952  -13.288 1.000 64.557  0 394 ASN AAA OD1 1 ? 3  
ATOM   508   N ND2 . ASN A  1 65  ? 23.783  -24.857  -11.097 1.000 62.254  0 394 ASN AAA ND2 1 ? 3  
ATOM   509   N N   . VAL A  1 66  ? 26.496  -22.574  -11.420 1.000 42.459  0 395 VAL AAA N   1 ? 3  
ATOM   510   C CA  . VAL A  1 66  ? 26.327  -21.482  -10.442 1.000 40.524  0 395 VAL AAA CA  1 ? 3  
ATOM   511   C C   . VAL A  1 66  ? 24.846  -21.128  -10.402 1.000 40.689  0 395 VAL AAA C   1 ? 3  
ATOM   512   O O   . VAL A  1 66  ? 24.238  -21.051  -11.486 1.000 42.264  0 395 VAL AAA O   1 ? 3  
ATOM   513   C CB  . VAL A  1 66  ? 27.208  -20.263  -10.762 1.000 39.384  0 395 VAL AAA CB  1 ? 3  
ATOM   514   C CG1 . VAL A  1 66  ? 27.004  -19.148  -9.761  1.000 37.961  0 395 VAL AAA CG1 1 ? 3  
ATOM   515   C CG2 . VAL A  1 66  ? 28.665  -20.641  -10.824 1.000 40.504  0 395 VAL AAA CG2 1 ? 3  
ATOM   516   N N   . TYR A  1 67  ? 24.287  -20.925  -9.214  1.000 39.825  0 396 TYR AAA N   1 ? 3  
ATOM   517   C CA  . TYR A  1 67  ? 22.924  -20.402  -9.025  1.000 40.913  0 396 TYR AAA CA  1 ? 3  
ATOM   518   C C   . TYR A  1 67  ? 23.007  -19.074  -8.284  1.000 39.191  0 396 TYR AAA C   1 ? 3  
ATOM   519   O O   . TYR A  1 67  ? 23.797  -18.958  -7.322  1.000 37.103  0 396 TYR AAA O   1 ? 3  
ATOM   520   C CB  . TYR A  1 67  ? 22.074  -21.418  -8.248  1.000 44.880  0 396 TYR AAA CB  1 ? 3  
ATOM   521   C CG  . TYR A  1 67  ? 21.774  -22.656  -9.046  1.000 48.616  0 396 TYR AAA CG  1 ? 3  
ATOM   522   C CD1 . TYR A  1 67  ? 21.030  -22.565  -10.212 1.000 49.604  0 396 TYR AAA CD1 1 ? 3  
ATOM   523   C CD2 . TYR A  1 67  ? 22.034  -23.917  -8.540  1.000 52.265  0 396 TYR AAA CD2 1 ? 3  
ATOM   524   C CE1 . TYR A  1 67  ? 20.657  -23.690  -10.922 1.000 54.334  0 396 TYR AAA CE1 1 ? 3  
ATOM   525   C CE2 . TYR A  1 67  ? 21.656  -25.060  -9.230  1.000 57.188  0 396 TYR AAA CE2 1 ? 3  
ATOM   526   C CZ  . TYR A  1 67  ? 20.961  -24.942  -10.426 1.000 57.463  0 396 TYR AAA CZ  1 ? 3  
ATOM   527   O OH  . TYR A  1 67  ? 20.610  -26.035  -11.160 1.000 66.371  0 396 TYR AAA OH  1 ? 3  
ATOM   528   N N   . ALA A  1 68  ? 22.192  -18.117  -8.708  1.000 39.165  0 397 ALA AAA N   1 ? 3  
ATOM   529   C CA  . ALA A  1 68  ? 21.988  -16.819  -8.036  1.000 39.196  0 397 ALA AAA CA  1 ? 3  
ATOM   530   C C   . ALA A  1 68  ? 20.560  -16.790  -7.504  1.000 39.268  0 397 ALA AAA C   1 ? 3  
ATOM   531   O O   . ALA A  1 68  ? 19.616  -16.678  -8.318  1.000 41.798  0 397 ALA AAA O   1 ? 3  
ATOM   532   C CB  . ALA A  1 68  ? 22.259  -15.658  -8.978  1.000 38.844  0 397 ALA AAA CB  1 ? 3  
ATOM   533   N N   . ASP A  1 69  ? 20.431  -16.938  -6.193  1.000 38.298  0 398 ASP AAA N   1 ? 3  
ATOM   534   C CA  . ASP A  1 69  ? 19.166  -16.820  -5.430  1.000 40.268  0 398 ASP AAA CA  1 ? 3  
ATOM   535   C C   . ASP A  1 69  ? 19.109  -15.395  -4.879  1.000 40.047  0 398 ASP AAA C   1 ? 3  
ATOM   536   O O   . ASP A  1 69  ? 20.118  -14.910  -4.361  1.000 39.827  0 398 ASP AAA O   1 ? 3  
ATOM   537   C CB  . ASP A  1 69  ? 19.112  -17.855  -4.296  1.000 40.591  0 398 ASP AAA CB  1 ? 3  
ATOM   538   C CG  . ASP A  1 69  ? 19.275  -19.293  -4.785  1.000 39.396  0 398 ASP AAA CG  1 ? 3  
ATOM   539   O OD1 . ASP A  1 69  ? 18.900  -19.539  -5.982  1.000 36.209  0 398 ASP AAA OD1 1 ? 3  
ATOM   540   O OD2 . ASP A  1 69  ? 19.795  -20.150  -4.003  1.000 37.564  0 398 ASP AAA OD2 1 ? 3  
ATOM   541   N N   . SER A  1 70  ? 17.985  -14.720  -5.025  1.000 39.885  0 399 SER AAA N   1 ? 3  
ATOM   542   C CA  . SER A  1 70  ? 17.845  -13.322  -4.580  1.000 39.284  0 399 SER AAA CA  1 ? 3  
ATOM   543   C C   . SER A  1 70  ? 16.457  -13.110  -3.981  1.000 40.788  0 399 SER AAA C   1 ? 3  
ATOM   544   O O   . SER A  1 70  ? 15.477  -13.768  -4.417  1.000 44.313  0 399 SER AAA O   1 ? 3  
ATOM   545   C CB  . SER A  1 70  ? 18.136  -12.370  -5.722  1.000 37.466  0 399 SER AAA CB  1 ? 3  
ATOM   546   O OG  . SER A  1 70  ? 17.308  -12.644  -6.819  1.000 36.442  0 399 SER AAA OG  1 ? 3  
ATOM   547   N N   . PHE A  1 71  ? 16.380  -12.177  -3.043  1.000 38.930  0 400 PHE AAA N   1 ? 3  
ATOM   548   C CA  . PHE A  1 71  ? 15.130  -11.862  -2.307  1.000 38.614  0 400 PHE AAA CA  1 ? 3  
ATOM   549   C C   . PHE A  1 71  ? 15.368  -10.644  -1.423  1.000 38.568  0 400 PHE AAA C   1 ? 3  
ATOM   550   O O   . PHE A  1 71  ? 16.526  -10.197  -1.309  1.000 37.991  0 400 PHE AAA O   1 ? 3  
ATOM   551   C CB  . PHE A  1 71  ? 14.719  -13.070  -1.455  1.000 38.422  0 400 PHE AAA CB  1 ? 3  
ATOM   552   C CG  . PHE A  1 71  ? 15.833  -13.669  -0.638  1.000 36.432  0 400 PHE AAA CG  1 ? 3  
ATOM   553   C CD1 . PHE A  1 71  ? 16.225  -13.106  0.556   1.000 37.263  0 400 PHE AAA CD1 1 ? 3  
ATOM   554   C CD2 . PHE A  1 71  ? 16.481  -14.812  -1.065  1.000 37.203  0 400 PHE AAA CD2 1 ? 3  
ATOM   555   C CE1 . PHE A  1 71  ? 17.250  -13.681  1.309   1.000 38.203  0 400 PHE AAA CE1 1 ? 3  
ATOM   556   C CE2 . PHE A  1 71  ? 17.506  -15.383  -0.326  1.000 37.122  0 400 PHE AAA CE2 1 ? 3  
ATOM   557   C CZ  . PHE A  1 71  ? 17.899  -14.810  0.858   1.000 37.652  0 400 PHE AAA CZ  1 ? 3  
ATOM   558   N N   . VAL A  1 72  ? 14.310  -10.200  -0.745  1.000 39.880  0 401 VAL AAA N   1 ? 3  
ATOM   559   C CA  . VAL A  1 72  ? 14.345  -9.105   0.259   1.000 39.862  0 401 VAL AAA CA  1 ? 3  
ATOM   560   C C   . VAL A  1 72  ? 13.993  -9.668   1.639   1.000 40.125  0 401 VAL AAA C   1 ? 3  
ATOM   561   O O   . VAL A  1 72  ? 13.042  -10.466  1.756   1.000 41.500  0 401 VAL AAA O   1 ? 3  
ATOM   562   C CB  . VAL A  1 72  ? 13.401  -7.971   -0.162  1.000 40.795  0 401 VAL AAA CB  1 ? 3  
ATOM   563   C CG1 . VAL A  1 72  ? 13.208  -6.958   0.948   1.000 42.409  0 401 VAL AAA CG1 1 ? 3  
ATOM   564   C CG2 . VAL A  1 72  ? 13.904  -7.296   -1.423  1.000 40.183  0 401 VAL AAA CG2 1 ? 3  
ATOM   565   N N   . ILE A  1 73  ? 14.733  -9.223   2.652   1.000 39.429  0 402 ILE AAA N   1 ? 3  
ATOM   566   C CA  . ILE A  1 73  ? 14.468  -9.476   4.101   1.000 38.410  0 402 ILE AAA CA  1 ? 3  
ATOM   567   C C   . ILE A  1 73  ? 14.799  -8.188   4.879   1.000 38.217  0 402 ILE AAA C   1 ? 3  
ATOM   568   O O   . ILE A  1 73  ? 15.217  -7.218   4.251   1.000 37.649  0 402 ILE AAA O   1 ? 3  
ATOM   569   C CB  . ILE A  1 73  ? 15.270  -10.694  4.588   1.000 36.413  0 402 ILE AAA CB  1 ? 3  
ATOM   570   C CG1 . ILE A  1 73  ? 16.764  -10.573  4.285   1.000 35.399  0 402 ILE AAA CG1 1 ? 3  
ATOM   571   C CG2 . ILE A  1 73  ? 14.696  -11.966  4.016   1.000 35.944  0 402 ILE AAA CG2 1 ? 3  
ATOM   572   C CD1 . ILE A  1 73  ? 17.594  -11.666  4.924   1.000 34.633  0 402 ILE AAA CD1 1 ? 3  
ATOM   573   N N   . ARG A  1 74  ? 14.555  -8.169   6.184   1.000 41.388  0 403 ARG AAA N   1 ? 3  
ATOM   574   C CA  . ARG A  1 74  ? 14.966  -7.069   7.097   1.000 45.214  0 403 ARG AAA CA  1 ? 3  
ATOM   575   C C   . ARG A  1 74  ? 16.482  -7.134   7.314   1.000 43.495  0 403 ARG AAA C   1 ? 3  
ATOM   576   O O   . ARG A  1 74  ? 17.029  -8.247   7.315   1.000 41.028  0 403 ARG AAA O   1 ? 3  
ATOM   577   C CB  . ARG A  1 74  ? 14.393  -7.225   8.503   1.000 49.735  0 403 ARG AAA CB  1 ? 3  
ATOM   578   C CG  . ARG A  1 74  ? 12.928  -6.878   8.656   1.000 55.565  0 403 ARG AAA CG  1 ? 3  
ATOM   579   C CD  . ARG A  1 74  ? 12.377  -7.523   9.910   1.000 59.440  0 403 ARG AAA CD  1 ? 3  
ATOM   580   N NE  . ARG A  1 74  ? 13.132  -7.111   11.083  1.000 63.334  0 403 ARG AAA NE  1 ? 3  
ATOM   581   C CZ  . ARG A  1 74  ? 12.967  -7.634   12.294  1.000 68.507  0 403 ARG AAA CZ  1 ? 3  
ATOM   582   N NH1 . ARG A  1 74  ? 12.088  -8.596   12.496  1.000 68.097  0 403 ARG AAA NH1 1 ? 3  
ATOM   583   N NH2 . ARG A  1 74  ? 13.715  -7.211   13.297  1.000 72.095  0 403 ARG AAA NH2 1 ? 3  
ATOM   584   N N   . GLY A  1 75  ? 17.083  -5.990   7.605   1.000 42.404  0 404 GLY AAA N   1 ? 3  
ATOM   585   C CA  . GLY A  1 75  ? 18.502  -5.856   7.947   1.000 43.070  0 404 GLY AAA CA  1 ? 3  
ATOM   586   C C   . GLY A  1 75  ? 18.952  -6.878   8.974   1.000 41.112  0 404 GLY AAA C   1 ? 3  
ATOM   587   O O   . GLY A  1 75  ? 19.953  -7.551   8.727   1.000 37.360  0 404 GLY AAA O   1 ? 3  
ATOM   588   N N   . ASP A  1 76  ? 18.253  -7.006   10.090  1.000 42.578  0 405 ASP AAA N   1 ? 3  
ATOM   589   C CA  . ASP A  1 76  ? 18.766  -7.864   11.193  1.000 48.047  0 405 ASP AAA CA  1 ? 3  
ATOM   590   C C   . ASP A  1 76  ? 18.426  -9.350   10.935  1.000 46.810  0 405 ASP AAA C   1 ? 3  
ATOM   591   O O   . ASP A  1 76  ? 18.794  -10.170  11.736  1.000 47.578  0 405 ASP AAA O   1 ? 3  
ATOM   592   C CB  . ASP A  1 76  ? 18.440  -7.293   12.577  1.000 51.770  0 405 ASP AAA CB  1 ? 3  
ATOM   593   C CG  . ASP A  1 76  ? 16.994  -6.966   12.818  1.000 58.674  0 405 ASP AAA CG  1 ? 3  
ATOM   594   O OD1 . ASP A  1 76  ? 16.136  -7.598   12.154  1.000 61.760  0 405 ASP AAA OD1 1 ? 3  
ATOM   595   O OD2 . ASP A  1 76  ? 16.726  -6.075   13.696  1.000 66.270  0 405 ASP AAA OD2 1 ? 3  
ATOM   596   N N   . GLU A  1 77  ? 17.842  -9.700   9.798   1.000 43.815  0 406 GLU AAA N   1 ? 3  
ATOM   597   C CA  . GLU A  1 77  ? 17.656  -11.112  9.384   1.000 43.038  0 406 GLU AAA CA  1 ? 3  
ATOM   598   C C   . GLU A  1 77  ? 18.784  -11.536  8.427   1.000 41.742  0 406 GLU AAA C   1 ? 3  
ATOM   599   O O   . GLU A  1 77  ? 18.917  -12.741  8.148   1.000 39.841  0 406 GLU AAA O   1 ? 3  
ATOM   600   C CB  . GLU A  1 77  ? 16.286  -11.303  8.721   1.000 45.142  0 406 GLU AAA CB  1 ? 3  
ATOM   601   C CG  . GLU A  1 77  ? 15.099  -11.200  9.677   1.000 45.613  0 406 GLU AAA CG  1 ? 3  
ATOM   602   C CD  . GLU A  1 77  ? 13.735  -11.149  8.993   1.000 46.908  0 406 GLU AAA CD  1 ? 3  
ATOM   603   O OE1 . GLU A  1 77  ? 13.679  -10.819  7.789   1.000 45.328  0 406 GLU AAA OE1 1 ? 3  
ATOM   604   O OE2 . GLU A  1 77  ? 12.723  -11.427  9.667   1.000 49.090  0 406 GLU AAA OE2 1 ? 3  
ATOM   605   N N   . VAL A  1 78  ? 19.603  -10.612  7.918   1.000 41.644  0 407 VAL AAA N   1 ? 3  
ATOM   606   C CA  . VAL A  1 78  ? 20.676  -10.959  6.938   1.000 40.282  0 407 VAL AAA CA  1 ? 3  
ATOM   607   C C   . VAL A  1 78  ? 21.653  -11.958  7.581   1.000 40.893  0 407 VAL AAA C   1 ? 3  
ATOM   608   O O   . VAL A  1 78  ? 22.096  -12.841  6.883   1.000 40.017  0 407 VAL AAA O   1 ? 3  
ATOM   609   C CB  . VAL A  1 78  ? 21.389  -9.700   6.396   1.000 42.359  0 407 VAL AAA CB  1 ? 3  
ATOM   610   C CG1 . VAL A  1 78  ? 22.663  -10.037  5.614   1.000 40.606  0 407 VAL AAA CG1 1 ? 3  
ATOM   611   C CG2 . VAL A  1 78  ? 20.438  -8.844   5.555   1.000 41.476  0 407 VAL AAA CG2 1 ? 3  
ATOM   612   N N   . ARG A  1 79  ? 21.941  -11.871  8.880   1.000 42.516  0 408 ARG AAA N   1 ? 3  
ATOM   613   C CA  . ARG A  1 79  ? 22.796  -12.839  9.620   1.000 42.744  0 408 ARG AAA CA  1 ? 3  
ATOM   614   C C   . ARG A  1 79  ? 22.271  -14.281  9.471   1.000 40.508  0 408 ARG AAA C   1 ? 3  
ATOM   615   O O   . ARG A  1 79  ? 23.051  -15.198  9.698   1.000 42.269  0 408 ARG AAA O   1 ? 3  
ATOM   616   C CB  . ARG A  1 79  ? 22.872  -12.435  11.099  1.000 47.455  0 408 ARG AAA CB  1 ? 3  
ATOM   617   C CG  . ARG A  1 79  ? 21.574  -12.635  11.868  1.000 55.182  0 408 ARG AAA CG  1 ? 3  
ATOM   618   C CD  . ARG A  1 79  ? 21.634  -13.218  13.287  1.000 63.139  0 408 ARG AAA CD  1 ? 3  
ATOM   619   N NE  . ARG A  1 79  ? 20.317  -13.604  13.836  1.000 70.332  0 408 ARG AAA NE  1 ? 3  
ATOM   620   C CZ  . ARG A  1 79  ? 19.820  -14.846  13.946  1.000 71.455  0 408 ARG AAA CZ  1 ? 3  
ATOM   621   N NH1 . ARG A  1 79  ? 20.481  -15.906  13.501  1.000 73.993  0 408 ARG AAA NH1 1 ? 3  
ATOM   622   N NH2 . ARG A  1 79  ? 18.630  -15.030  14.485  1.000 70.713  0 408 ARG AAA NH2 1 ? 3  
ATOM   623   N N   . GLN A  1 80  ? 20.999  -14.499  9.140   1.000 39.159  0 409 GLN AAA N   1 ? 3  
ATOM   624   C CA  . GLN A  1 80  ? 20.391  -15.846  9.002   1.000 39.122  0 409 GLN AAA CA  1 ? 3  
ATOM   625   C C   . GLN A  1 80  ? 20.766  -16.470  7.662   1.000 37.594  0 409 GLN AAA C   1 ? 3  
ATOM   626   O O   . GLN A  1 80  ? 20.608  -17.688  7.513   1.000 38.067  0 409 GLN AAA O   1 ? 3  
ATOM   627   C CB  . GLN A  1 80  ? 18.869  -15.813  9.151   1.000 40.182  0 409 GLN AAA CB  1 ? 3  
ATOM   628   C CG  . GLN A  1 80  ? 18.432  -15.550  10.578  1.000 41.850  0 409 GLN AAA CG  1 ? 3  
ATOM   629   C CD  . GLN A  1 80  ? 16.939  -15.542  10.764  1.000 42.126  0 409 GLN AAA CD  1 ? 3  
ATOM   630   O OE1 . GLN A  1 80  ? 16.230  -16.448  10.325  1.000 39.808  0 409 GLN AAA OE1 1 ? 3  
ATOM   631   N NE2 . GLN A  1 80  ? 16.466  -14.531  11.459  1.000 42.724  0 409 GLN AAA NE2 1 ? 3  
ATOM   632   N N   . ILE A  1 81  ? 21.228  -15.679  6.707   1.000 37.729  0 410 ILE AAA N   1 ? 3  
ATOM   633   C CA  . ILE A  1 81  ? 21.599  -16.196  5.361   1.000 38.991  0 410 ILE AAA CA  1 ? 3  
ATOM   634   C C   . ILE A  1 81  ? 23.057  -16.637  5.443   1.000 39.372  0 410 ILE AAA C   1 ? 3  
ATOM   635   O O   . ILE A  1 81  ? 23.955  -15.976  4.852   1.000 37.797  0 410 ILE AAA O   1 ? 3  
ATOM   636   C CB  . ILE A  1 81  ? 21.329  -15.172  4.254   1.000 38.201  0 410 ILE AAA CB  1 ? 3  
ATOM   637   C CG1 . ILE A  1 81  ? 19.959  -14.510  4.442   1.000 39.530  0 410 ILE AAA CG1 1 ? 3  
ATOM   638   C CG2 . ILE A  1 81  ? 21.454  -15.838  2.893   1.000 39.249  0 410 ILE AAA CG2 1 ? 3  
ATOM   639   C CD1 . ILE A  1 81  ? 18.811  -15.493  4.519   1.000 41.504  0 410 ILE AAA CD1 1 ? 3  
ATOM   640   N N   . ALA A  1 82  ? 23.266  -17.741  6.152   1.000 38.815  0 411 ALA AAA N   1 ? 3  
ATOM   641   C CA  . ALA A  1 82  ? 24.605  -18.261  6.485   1.000 41.975  0 411 ALA AAA CA  1 ? 3  
ATOM   642   C C   . ALA A  1 82  ? 24.444  -19.683  6.996   1.000 43.980  0 411 ALA AAA C   1 ? 3  
ATOM   643   O O   . ALA A  1 82  ? 23.440  -20.010  7.625   1.000 46.242  0 411 ALA AAA O   1 ? 3  
ATOM   644   C CB  . ALA A  1 82  ? 25.288  -17.394  7.525   1.000 38.489  0 411 ALA AAA CB  1 ? 3  
ATOM   645   N N   . PRO A  1 83  ? 25.428  -20.570  6.752   1.000 44.193  0 412 PRO AAA N   1 ? 3  
ATOM   646   C CA  . PRO A  1 83  ? 25.347  -21.933  7.260   1.000 44.952  0 412 PRO AAA CA  1 ? 3  
ATOM   647   C C   . PRO A  1 83  ? 25.216  -21.941  8.783   1.000 42.753  0 412 PRO AAA C   1 ? 3  
ATOM   648   O O   . PRO A  1 83  ? 25.877  -21.168  9.402   1.000 43.473  0 412 PRO AAA O   1 ? 3  
ATOM   649   C CB  . PRO A  1 83  ? 26.664  -22.550  6.793   1.000 45.660  0 412 PRO AAA CB  1 ? 3  
ATOM   650   C CG  . PRO A  1 83  ? 27.555  -21.363  6.536   1.000 44.927  0 412 PRO AAA CG  1 ? 3  
ATOM   651   C CD  . PRO A  1 83  ? 26.622  -20.343  5.946   1.000 42.730  0 412 PRO AAA CD  1 ? 3  
ATOM   652   N N   . GLY A  1 84  ? 24.349  -22.807  9.315   1.000 43.074  0 413 GLY AAA N   1 ? 3  
ATOM   653   C CA  . GLY A  1 84  ? 24.245  -23.124  10.752  1.000 42.760  0 413 GLY AAA CA  1 ? 3  
ATOM   654   C C   . GLY A  1 84  ? 23.366  -22.145  11.509  1.000 43.598  0 413 GLY AAA C   1 ? 3  
ATOM   655   O O   . GLY A  1 84  ? 23.405  -22.161  12.734  1.000 44.566  0 413 GLY AAA O   1 ? 3  
ATOM   656   N N   . GLN A  1 85  ? 22.586  -21.319  10.813  1.000 44.994  0 414 GLN AAA N   1 ? 3  
ATOM   657   C CA  . GLN A  1 85  ? 21.723  -20.274  11.451  1.000 43.334  0 414 GLN AAA CA  1 ? 3  
ATOM   658   C C   . GLN A  1 85  ? 20.320  -20.828  11.695  1.000 43.427  0 414 GLN AAA C   1 ? 3  
ATOM   659   O O   . GLN A  1 85  ? 19.906  -21.734  10.956  1.000 44.947  0 414 GLN AAA O   1 ? 3  
ATOM   660   C CB  . GLN A  1 85  ? 21.625  -19.030  10.572  1.000 41.972  0 414 GLN AAA CB  1 ? 3  
ATOM   661   C CG  . GLN A  1 85  ? 22.925  -18.269  10.483  1.000 41.484  0 414 GLN AAA CG  1 ? 3  
ATOM   662   C CD  . GLN A  1 85  ? 23.394  -17.735  11.818  1.000 44.196  0 414 GLN AAA CD  1 ? 3  
ATOM   663   O OE1 . GLN A  1 85  ? 22.648  -17.436  12.761  1.000 44.582  0 414 GLN AAA OE1 1 ? 3  
ATOM   664   N NE2 . GLN A  1 85  ? 24.698  -17.689  11.939  1.000 45.385  0 414 GLN AAA NE2 1 ? 3  
ATOM   665   N N   . THR A  1 86  ? 19.625  -20.299  12.701  1.000 43.061  0 415 THR AAA N   1 ? 3  
ATOM   666   C CA  . THR A  1 86  ? 18.180  -20.511  12.937  1.000 45.372  0 415 THR AAA CA  1 ? 3  
ATOM   667   C C   . THR A  1 86  ? 17.470  -19.161  13.054  1.000 47.041  0 415 THR AAA C   1 ? 3  
ATOM   668   O O   . THR A  1 86  ? 18.161  -18.138  13.161  1.000 48.170  0 415 THR AAA O   1 ? 3  
ATOM   669   C CB  . THR A  1 86  ? 17.929  -21.378  14.170  1.000 47.830  0 415 THR AAA CB  1 ? 3  
ATOM   670   O OG1 . THR A  1 86  ? 18.565  -20.732  15.268  1.000 47.827  0 415 THR AAA OG1 1 ? 3  
ATOM   671   C CG2 . THR A  1 86  ? 18.429  -22.799  13.992  1.000 47.881  0 415 THR AAA CG2 1 ? 3  
ATOM   672   N N   . GLY A  1 87  ? 16.130  -19.185  13.013  1.000 47.708  0 416 GLY AAA N   1 ? 3  
ATOM   673   C CA  . GLY A  1 87  ? 15.234  -18.009  12.967  1.000 47.372  0 416 GLY AAA CA  1 ? 3  
ATOM   674   C C   . GLY A  1 87  ? 14.157  -18.215  11.920  1.000 47.951  0 416 GLY AAA C   1 ? 3  
ATOM   675   O O   . GLY A  1 87  ? 14.247  -19.209  11.175  1.000 50.884  0 416 GLY AAA O   1 ? 3  
ATOM   676   N N   . LYS A  1 88  ? 13.168  -17.325  11.865  1.000 49.099  0 417 LYS AAA N   1 ? 3  
ATOM   677   C CA  . LYS A  1 88  ? 12.027  -17.419  10.923  1.000 49.172  0 417 LYS AAA CA  1 ? 3  
ATOM   678   C C   . LYS A  1 88  ? 12.587  -17.647  9.522   1.000 45.748  0 417 LYS AAA C   1 ? 3  
ATOM   679   O O   . LYS A  1 88  ? 12.043  -18.523  8.825   1.000 44.080  0 417 LYS AAA O   1 ? 3  
ATOM   680   C CB  . LYS A  1 88  ? 11.157  -16.155  10.901  1.000 52.854  0 417 LYS AAA CB  1 ? 3  
ATOM   681   C CG  . LYS A  1 88  ? 10.450  -15.777  12.178  1.000 58.108  0 417 LYS AAA CG  1 ? 3  
ATOM   682   C CD  . LYS A  1 88  ? 9.635   -16.918  12.740  1.000 66.355  0 417 LYS AAA CD  1 ? 3  
ATOM   683   C CE  . LYS A  1 88  ? 9.035   -16.589  14.094  1.000 69.380  0 417 LYS AAA CE  1 ? 3  
ATOM   684   N NZ  . LYS A  1 88  ? 8.676   -17.820  14.834  1.000 72.592  0 417 LYS AAA NZ  1 ? 3  
ATOM   685   N N   . ILE A  1 89  ? 13.635  -16.908  9.130   1.000 43.354  0 418 ILE AAA N   1 ? 3  
ATOM   686   C CA  . ILE A  1 89  ? 14.106  -16.900  7.715   1.000 42.841  0 418 ILE AAA CA  1 ? 3  
ATOM   687   C C   . ILE A  1 89  ? 14.855  -18.204  7.422   1.000 41.542  0 418 ILE AAA C   1 ? 3  
ATOM   688   O O   . ILE A  1 89  ? 14.452  -18.914  6.493   1.000 44.508  0 418 ILE AAA O   1 ? 3  
ATOM   689   C CB  . ILE A  1 89  ? 14.912  -15.629  7.371   1.000 41.136  0 418 ILE AAA CB  1 ? 3  
ATOM   690   C CG1 . ILE A  1 89  ? 14.138  -14.355  7.733   1.000 43.160  0 418 ILE AAA CG1 1 ? 3  
ATOM   691   C CG2 . ILE A  1 89  ? 15.295  -15.631  5.911   1.000 38.993  0 418 ILE AAA CG2 1 ? 3  
ATOM   692   C CD1 . ILE A  1 89  ? 12.735  -14.276  7.153   1.000 44.625  0 418 ILE AAA CD1 1 ? 3  
ATOM   693   N N   . ALA A  1 90  ? 15.875  -18.538  8.196   1.000 41.162  0 419 ALA AAA N   1 ? 3  
ATOM   694   C CA  . ALA A  1 90  ? 16.663  -19.780  8.031   1.000 40.692  0 419 ALA AAA CA  1 ? 3  
ATOM   695   C C   . ALA A  1 90  ? 15.738  -20.997  8.100   1.000 42.954  0 419 ALA AAA C   1 ? 3  
ATOM   696   O O   . ALA A  1 90  ? 15.942  -21.944  7.286   1.000 45.091  0 419 ALA AAA O   1 ? 3  
ATOM   697   C CB  . ALA A  1 90  ? 17.750  -19.868  9.069   1.000 40.841  0 419 ALA AAA CB  1 ? 3  
ATOM   698   N N   . ASP A  1 91  ? 14.754  -20.995  9.003   1.000 43.674  0 420 ASP AAA N   1 ? 3  
ATOM   699   C CA  . ASP A  1 91  ? 13.937  -22.197  9.305   1.000 46.247  0 420 ASP AAA CA  1 ? 3  
ATOM   700   C C   . ASP A  1 91  ? 12.816  -22.364  8.266   1.000 46.173  0 420 ASP AAA C   1 ? 3  
ATOM   701   O O   . ASP A  1 91  ? 12.558  -23.516  7.884   1.000 46.319  0 420 ASP AAA O   1 ? 3  
ATOM   702   C CB  . ASP A  1 91  ? 13.336  -22.142  10.715  1.000 49.130  0 420 ASP AAA CB  1 ? 3  
ATOM   703   C CG  . ASP A  1 91  ? 14.362  -22.164  11.845  1.000 51.415  0 420 ASP AAA CG  1 ? 3  
ATOM   704   O OD1 . ASP A  1 91  ? 15.550  -22.499  11.552  1.000 51.841  0 420 ASP AAA OD1 1 ? 3  
ATOM   705   O OD2 . ASP A  1 91  ? 13.963  -21.847  13.008  1.000 51.442  0 420 ASP AAA OD2 1 ? 3  
ATOM   706   N N   . TYR A  1 92  ? 12.152  -21.276  7.855   1.000 44.745  0 421 TYR AAA N   1 ? 3  
ATOM   707   C CA  . TYR A  1 92  ? 10.839  -21.342  7.174   1.000 47.372  0 421 TYR AAA CA  1 ? 3  
ATOM   708   C C   . TYR A  1 92  ? 10.862  -20.716  5.772   1.000 45.962  0 421 TYR AAA C   1 ? 3  
ATOM   709   O O   . TYR A  1 92  ? 9.872   -20.880  5.058   1.000 45.211  0 421 TYR AAA O   1 ? 3  
ATOM   710   C CB  . TYR A  1 92  ? 9.778   -20.658  8.042   1.000 50.156  0 421 TYR AAA CB  1 ? 3  
ATOM   711   C CG  . TYR A  1 92  ? 9.464   -21.311  9.369   1.000 51.883  0 421 TYR AAA CG  1 ? 3  
ATOM   712   C CD1 . TYR A  1 92  ? 9.807   -22.623  9.657   1.000 51.662  0 421 TYR AAA CD1 1 ? 3  
ATOM   713   C CD2 . TYR A  1 92  ? 8.815   -20.605  10.362  1.000 54.745  0 421 TYR AAA CD2 1 ? 3  
ATOM   714   C CE1 . TYR A  1 92  ? 9.502   -23.208  10.871  1.000 53.196  0 421 TYR AAA CE1 1 ? 3  
ATOM   715   C CE2 . TYR A  1 92  ? 8.496   -21.174  11.584  1.000 55.854  0 421 TYR AAA CE2 1 ? 3  
ATOM   716   C CZ  . TYR A  1 92  ? 8.843   -22.486  11.848  1.000 55.589  0 421 TYR AAA CZ  1 ? 3  
ATOM   717   O OH  . TYR A  1 92  ? 8.511   -23.054  13.053  1.000 56.929  0 421 TYR AAA OH  1 ? 3  
ATOM   718   N N   . ASN A  1 93  ? 11.938  -20.038  5.363   1.000 44.403  0 422 ASN AAA N   1 ? 3  
ATOM   719   C CA  . ASN A  1 93  ? 11.929  -19.226  4.112   1.000 41.998  0 422 ASN AAA CA  1 ? 3  
ATOM   720   C C   . ASN A  1 93  ? 13.085  -19.616  3.182   1.000 42.043  0 422 ASN AAA C   1 ? 3  
ATOM   721   O O   . ASN A  1 93  ? 12.809  -19.996  2.025   1.000 42.164  0 422 ASN AAA O   1 ? 3  
ATOM   722   C CB  . ASN A  1 93  ? 11.951  -17.741  4.441   1.000 40.373  0 422 ASN AAA CB  1 ? 3  
ATOM   723   C CG  . ASN A  1 93  ? 10.665  -17.276  5.075   1.000 41.211  0 422 ASN AAA CG  1 ? 3  
ATOM   724   O OD1 . ASN A  1 93  ? 9.766   -16.820  4.393   1.000 42.489  0 422 ASN AAA OD1 1 ? 3  
ATOM   725   N ND2 . ASN A  1 93  ? 10.545  -17.415  6.375   1.000 43.939  0 422 ASN AAA ND2 1 ? 3  
ATOM   726   N N   . TYR A  1 94  ? 14.324  -19.533  3.657   1.000 42.301  0 423 TYR AAA N   1 ? 3  
ATOM   727   C CA  . TYR A  1 94  ? 15.539  -19.815  2.844   1.000 43.128  0 423 TYR AAA CA  1 ? 3  
ATOM   728   C C   . TYR A  1 94  ? 16.633  -20.399  3.740   1.000 42.135  0 423 TYR AAA C   1 ? 3  
ATOM   729   O O   . TYR A  1 94  ? 17.112  -19.684  4.663   1.000 40.912  0 423 TYR AAA O   1 ? 3  
ATOM   730   C CB  . TYR A  1 94  ? 16.036  -18.552  2.131   1.000 40.968  0 423 TYR AAA CB  1 ? 3  
ATOM   731   C CG  . TYR A  1 94  ? 17.148  -18.821  1.156   1.000 39.327  0 423 TYR AAA CG  1 ? 3  
ATOM   732   C CD1 . TYR A  1 94  ? 16.882  -19.182  -0.149  1.000 39.284  0 423 TYR AAA CD1 1 ? 3  
ATOM   733   C CD2 . TYR A  1 94  ? 18.471  -18.724  1.538   1.000 39.903  0 423 TYR AAA CD2 1 ? 3  
ATOM   734   C CE1 . TYR A  1 94  ? 17.902  -19.431  -1.056  1.000 38.363  0 423 TYR AAA CE1 1 ? 3  
ATOM   735   C CE2 . TYR A  1 94  ? 19.505  -19.006  0.658   1.000 40.026  0 423 TYR AAA CE2 1 ? 3  
ATOM   736   C CZ  . TYR A  1 94  ? 19.224  -19.371  -0.648  1.000 39.021  0 423 TYR AAA CZ  1 ? 3  
ATOM   737   O OH  . TYR A  1 94  ? 20.258  -19.599  -1.507  1.000 36.970  0 423 TYR AAA OH  1 ? 3  
ATOM   738   N N   . LYS A  1 95  ? 17.017  -21.648  3.474   1.000 41.842  0 424 LYS AAA N   1 ? 3  
ATOM   739   C CA  . LYS A  1 95  ? 17.974  -22.409  4.315   1.000 41.617  0 424 LYS AAA CA  1 ? 3  
ATOM   740   C C   . LYS A  1 95  ? 19.231  -22.724  3.501   1.000 40.373  0 424 LYS AAA C   1 ? 3  
ATOM   741   O O   . LYS A  1 95  ? 19.123  -23.362  2.426   1.000 40.062  0 424 LYS AAA O   1 ? 3  
ATOM   742   C CB  . LYS A  1 95  ? 17.345  -23.722  4.777   1.000 43.570  0 424 LYS AAA CB  1 ? 3  
ATOM   743   C CG  . LYS A  1 95  ? 18.215  -24.617  5.652   1.000 43.567  0 424 LYS AAA CG  1 ? 3  
ATOM   744   C CD  . LYS A  1 95  ? 18.764  -23.887  6.841   1.000 41.619  0 424 LYS AAA CD  1 ? 3  
ATOM   745   C CE  . LYS A  1 95  ? 19.216  -24.773  7.974   1.000 42.135  0 424 LYS AAA CE  1 ? 3  
ATOM   746   N NZ  . LYS A  1 95  ? 20.102  -23.993  8.873   1.000 42.437  0 424 LYS AAA NZ  1 ? 3  
ATOM   747   N N   . LEU A  1 96  ? 20.393  -22.315  3.993   1.000 39.449  0 425 LEU AAA N   1 ? 3  
ATOM   748   C CA  . LEU A  1 96  ? 21.690  -22.735  3.420   1.000 39.987  0 425 LEU AAA CA  1 ? 3  
ATOM   749   C C   . LEU A  1 96  ? 22.134  -24.013  4.101   1.000 42.100  0 425 LEU AAA C   1 ? 3  
ATOM   750   O O   . LEU A  1 96  ? 21.896  -24.197  5.292   1.000 44.108  0 425 LEU AAA O   1 ? 3  
ATOM   751   C CB  . LEU A  1 96  ? 22.724  -21.627  3.615   1.000 39.473  0 425 LEU AAA CB  1 ? 3  
ATOM   752   C CG  . LEU A  1 96  ? 22.587  -20.437  2.672   1.000 39.592  0 425 LEU AAA CG  1 ? 3  
ATOM   753   C CD1 . LEU A  1 96  ? 23.725  -19.494  2.966   1.000 38.649  0 425 LEU AAA CD1 1 ? 3  
ATOM   754   C CD2 . LEU A  1 96  ? 22.530  -20.860  1.189   1.000 40.379  0 425 LEU AAA CD2 1 ? 3  
ATOM   755   N N   . PRO A  1 97  ? 22.817  -24.908  3.357   1.000 41.461  0 426 PRO AAA N   1 ? 3  
ATOM   756   C CA  . PRO A  1 97  ? 23.396  -26.122  3.937   1.000 42.620  0 426 PRO AAA CA  1 ? 3  
ATOM   757   C C   . PRO A  1 97  ? 24.565  -25.785  4.881   1.000 40.976  0 426 PRO AAA C   1 ? 3  
ATOM   758   O O   . PRO A  1 97  ? 25.153  -24.734  4.762   1.000 38.836  0 426 PRO AAA O   1 ? 3  
ATOM   759   C CB  . PRO A  1 97  ? 23.895  -26.883  2.694   1.000 43.522  0 426 PRO AAA CB  1 ? 3  
ATOM   760   C CG  . PRO A  1 97  ? 24.199  -25.812  1.683   1.000 41.333  0 426 PRO AAA CG  1 ? 3  
ATOM   761   C CD  . PRO A  1 97  ? 23.131  -24.777  1.926   1.000 41.715  0 426 PRO AAA CD  1 ? 3  
ATOM   762   N N   . ASP A  1 98  ? 24.894  -26.711  5.764   1.000 43.758  0 427 ASP AAA N   1 ? 3  
ATOM   763   C CA  . ASP A  1 98  ? 25.992  -26.540  6.752   1.000 45.878  0 427 ASP AAA CA  1 ? 3  
ATOM   764   C C   . ASP A  1 98  ? 27.348  -26.423  6.042   1.000 43.054  0 427 ASP AAA C   1 ? 3  
ATOM   765   O O   . ASP A  1 98  ? 28.196  -25.727  6.560   1.000 41.009  0 427 ASP AAA O   1 ? 3  
ATOM   766   C CB  . ASP A  1 98  ? 25.995  -27.683  7.770   1.000 47.392  0 427 ASP AAA CB  1 ? 3  
ATOM   767   C CG  . ASP A  1 98  ? 24.651  -27.976  8.418   1.000 53.393  0 427 ASP AAA CG  1 ? 3  
ATOM   768   O OD1 . ASP A  1 98  ? 23.765  -27.085  8.362   1.000 53.859  0 427 ASP AAA OD1 1 ? 3  
ATOM   769   O OD2 . ASP A  1 98  ? 24.500  -29.109  9.020   1.000 62.054  0 427 ASP AAA OD2 1 ? 3  
ATOM   770   N N   . ASP A  1 99  ? 27.532  -27.087  4.905   1.000 43.781  0 428 ASP AAA N   1 ? 3  
ATOM   771   C CA  . ASP A  1 99  ? 28.814  -27.170  4.145   1.000 41.656  0 428 ASP AAA CA  1 ? 3  
ATOM   772   C C   . ASP A  1 99  ? 28.710  -26.251  2.920   1.000 39.839  0 428 ASP AAA C   1 ? 3  
ATOM   773   O O   . ASP A  1 99  ? 29.366  -26.539  1.904   1.000 36.736  0 428 ASP AAA O   1 ? 3  
ATOM   774   C CB  . ASP A  1 99  ? 29.123  -28.623  3.762   1.000 43.343  0 428 ASP AAA CB  1 ? 3  
ATOM   775   C CG  . ASP A  1 99  ? 28.159  -29.221  2.740   1.000 45.999  0 428 ASP AAA CG  1 ? 3  
ATOM   776   O OD1 . ASP A  1 99  ? 27.082  -28.614  2.555   1.000 45.064  0 428 ASP AAA OD1 1 ? 3  
ATOM   777   O OD2 . ASP A  1 99  ? 28.513  -30.255  2.071   1.000 51.306  0 428 ASP AAA OD2 1 ? 3  
ATOM   778   N N   . PHE A  1 100 ? 27.880  -25.211  2.975   1.000 38.768  0 429 PHE AAA N   1 ? 3  
ATOM   779   C CA  . PHE A  1 100 ? 27.656  -24.304  1.826   1.000 38.574  0 429 PHE AAA CA  1 ? 3  
ATOM   780   C C   . PHE A  1 100 ? 28.965  -23.931  1.127   1.000 39.427  0 429 PHE AAA C   1 ? 3  
ATOM   781   O O   . PHE A  1 100 ? 29.913  -23.518  1.782   1.000 37.942  0 429 PHE AAA O   1 ? 3  
ATOM   782   C CB  . PHE A  1 100 ? 26.924  -23.052  2.290   1.000 37.500  0 429 PHE AAA CB  1 ? 3  
ATOM   783   C CG  . PHE A  1 100 ? 26.671  -22.052  1.192   1.000 36.715  0 429 PHE AAA CG  1 ? 3  
ATOM   784   C CD1 . PHE A  1 100 ? 25.985  -22.384  0.034   1.000 37.202  0 429 PHE AAA CD1 1 ? 3  
ATOM   785   C CD2 . PHE A  1 100 ? 27.090  -20.757  1.356   1.000 36.184  0 429 PHE AAA CD2 1 ? 3  
ATOM   786   C CE1 . PHE A  1 100 ? 25.738  -21.426  -0.946  1.000 36.625  0 429 PHE AAA CE1 1 ? 3  
ATOM   787   C CE2 . PHE A  1 100 ? 26.848  -19.803  0.396   1.000 35.966  0 429 PHE AAA CE2 1 ? 3  
ATOM   788   C CZ  . PHE A  1 100 ? 26.176  -20.136  -0.754  1.000 37.558  0 429 PHE AAA CZ  1 ? 3  
ATOM   789   N N   . THR A  1 101 ? 28.971  -24.044  -0.202  1.000 41.782  0 430 THR AAA N   1 ? 3  
ATOM   790   C CA  . THR A  1 101 ? 30.030  -23.493  -1.073  1.000 42.218  0 430 THR AAA CA  1 ? 3  
ATOM   791   C C   . THR A  1 101 ? 29.444  -22.367  -1.920  1.000 41.948  0 430 THR AAA C   1 ? 3  
ATOM   792   O O   . THR A  1 101 ? 28.602  -22.665  -2.766  1.000 43.338  0 430 THR AAA O   1 ? 3  
ATOM   793   C CB  . THR A  1 101 ? 30.681  -24.571  -1.931  1.000 43.221  0 430 THR AAA CB  1 ? 3  
ATOM   794   O OG1 . THR A  1 101 ? 31.174  -25.562  -1.036  1.000 46.150  0 430 THR AAA OG1 1 ? 3  
ATOM   795   C CG2 . THR A  1 101 ? 31.860  -24.046  -2.722  1.000 43.964  0 430 THR AAA CG2 1 ? 3  
ATOM   796   N N   . GLY A  1 102 ? 29.862  -21.131  -1.666  1.000 40.437  0 431 GLY AAA N   1 ? 3  
ATOM   797   C CA  . GLY A  1 102 ? 29.339  -19.962  -2.387  1.000 41.719  0 431 GLY AAA CA  1 ? 3  
ATOM   798   C C   . GLY A  1 102 ? 29.512  -18.680  -1.599  1.000 39.291  0 431 GLY AAA C   1 ? 3  
ATOM   799   O O   . GLY A  1 102 ? 30.286  -18.665  -0.634  1.000 39.155  0 431 GLY AAA O   1 ? 3  
ATOM   800   N N   . CYS A  1 103 ? 28.838  -17.623  -2.038  1.000 37.806  0 432 CYS AAA N   1 ? 3  
ATOM   801   C CA  . CYS A  1 103 ? 28.967  -16.280  -1.427  1.000 39.034  0 432 CYS AAA CA  1 ? 3  
ATOM   802   C C   . CYS A  1 103 ? 27.574  -15.710  -1.152  1.000 37.563  0 432 CYS AAA C   1 ? 3  
ATOM   803   O O   . CYS A  1 103 ? 26.635  -16.019  -1.886  1.000 37.269  0 432 CYS AAA O   1 ? 3  
ATOM   804   C CB  . CYS A  1 103 ? 29.786  -15.342  -2.303  1.000 39.631  0 432 CYS AAA CB  1 ? 3  
ATOM   805   S SG  . CYS A  1 103 ? 31.381  -16.060  -2.799  1.000 39.631  0 432 CYS AAA SG  1 ? 3  
ATOM   806   N N   . VAL A  1 104 ? 27.487  -14.923  -0.091  1.000 36.831  0 433 VAL AAA N   1 ? 3  
ATOM   807   C CA  . VAL A  1 104 ? 26.258  -14.197  0.320   1.000 34.627  0 433 VAL AAA CA  1 ? 3  
ATOM   808   C C   . VAL A  1 104 ? 26.583  -12.706  0.328   1.000 33.512  0 433 VAL AAA C   1 ? 3  
ATOM   809   O O   . VAL A  1 104 ? 27.537  -12.309  1.007   1.000 31.871  0 433 VAL AAA O   1 ? 3  
ATOM   810   C CB  . VAL A  1 104 ? 25.778  -14.685  1.692   1.000 34.958  0 433 VAL AAA CB  1 ? 3  
ATOM   811   C CG1 . VAL A  1 104 ? 24.557  -13.912  2.128   1.000 35.018  0 433 VAL AAA CG1 1 ? 3  
ATOM   812   C CG2 . VAL A  1 104 ? 25.499  -16.184  1.686   1.000 34.980  0 433 VAL AAA CG2 1 ? 3  
ATOM   813   N N   . ILE A  1 105 ? 25.847  -11.938  -0.465  1.000 34.838  0 434 ILE AAA N   1 ? 3  
ATOM   814   C CA  . ILE A  1 105 ? 26.011  -10.470  -0.621  1.000 34.800  0 434 ILE AAA CA  1 ? 3  
ATOM   815   C C   . ILE A  1 105 ? 24.658  -9.846   -0.314  1.000 35.439  0 434 ILE AAA C   1 ? 3  
ATOM   816   O O   . ILE A  1 105 ? 23.631  -10.378  -0.774  1.000 37.661  0 434 ILE AAA O   1 ? 3  
ATOM   817   C CB  . ILE A  1 105 ? 26.539  -10.084  -2.011  1.000 35.678  0 434 ILE AAA CB  1 ? 3  
ATOM   818   C CG1 . ILE A  1 105 ? 27.898  -10.744  -2.267  1.000 38.624  0 434 ILE AAA CG1 1 ? 3  
ATOM   819   C CG2 . ILE A  1 105 ? 26.624  -8.554   -2.168  1.000 37.542  0 434 ILE AAA CG2 1 ? 3  
ATOM   820   C CD1 . ILE A  1 105 ? 28.367  -10.699  -3.710  1.000 37.680  0 434 ILE AAA CD1 1 ? 3  
ATOM   821   N N   . ALA A  1 106 ? 24.653  -8.779   0.477   1.000 36.202  0 435 ALA AAA N   1 ? 3  
ATOM   822   C CA  . ALA A  1 106 ? 23.429  -8.030   0.801   1.000 36.327  0 435 ALA AAA CA  1 ? 3  
ATOM   823   C C   . ALA A  1 106 ? 23.765  -6.538   0.773   1.000 40.176  0 435 ALA AAA C   1 ? 3  
ATOM   824   O O   . ALA A  1 106 ? 24.962  -6.174   0.920   1.000 41.869  0 435 ALA AAA O   1 ? 3  
ATOM   825   C CB  . ALA A  1 106 ? 22.860  -8.478   2.117   1.000 34.603  0 435 ALA AAA CB  1 ? 3  
ATOM   826   N N   . TRP A  1 107 ? 22.734  -5.724   0.578   1.000 39.475  0 436 TRP AAA N   1 ? 3  
ATOM   827   C CA  . TRP A  1 107 ? 22.827  -4.254   0.658   1.000 39.443  0 436 TRP AAA CA  1 ? 3  
ATOM   828   C C   . TRP A  1 107 ? 21.473  -3.693   1.088   1.000 41.721  0 436 TRP AAA C   1 ? 3  
ATOM   829   O O   . TRP A  1 107 ? 20.427  -4.297   0.784   1.000 44.874  0 436 TRP AAA O   1 ? 3  
ATOM   830   C CB  . TRP A  1 107 ? 23.306  -3.661   -0.671  1.000 37.676  0 436 TRP AAA CB  1 ? 3  
ATOM   831   C CG  . TRP A  1 107 ? 22.379  -3.865   -1.827  1.000 35.345  0 436 TRP AAA CG  1 ? 3  
ATOM   832   C CD1 . TRP A  1 107 ? 21.481  -2.971   -2.297  1.000 35.928  0 436 TRP AAA CD1 1 ? 3  
ATOM   833   C CD2 . TRP A  1 107 ? 22.261  -5.022   -2.674  1.000 35.086  0 436 TRP AAA CD2 1 ? 3  
ATOM   834   N NE1 . TRP A  1 107 ? 20.816  -3.479   -3.373  1.000 36.700  0 436 TRP AAA NE1 1 ? 3  
ATOM   835   C CE2 . TRP A  1 107 ? 21.267  -4.738   -3.626  1.000 34.755  0 436 TRP AAA CE2 1 ? 3  
ATOM   836   C CE3 . TRP A  1 107 ? 22.905  -6.263   -2.724  1.000 34.757  0 436 TRP AAA CE3 1 ? 3  
ATOM   837   C CZ2 . TRP A  1 107 ? 20.894  -5.635   -4.622  1.000 35.576  0 436 TRP AAA CZ2 1 ? 3  
ATOM   838   C CZ3 . TRP A  1 107 ? 22.524  -7.155   -3.697  1.000 34.803  0 436 TRP AAA CZ3 1 ? 3  
ATOM   839   C CH2 . TRP A  1 107 ? 21.545  -6.840   -4.650  1.000 34.740  0 436 TRP AAA CH2 1 ? 3  
ATOM   840   N N   . ASN A  1 108 ? 21.527  -2.597   1.821   1.000 41.049  0 437 ASN AAA N   1 ? 3  
ATOM   841   C CA  . ASN A  1 108 ? 20.356  -1.799   2.217   1.000 41.712  0 437 ASN AAA CA  1 ? 3  
ATOM   842   C C   . ASN A  1 108 ? 19.636  -1.338   0.943   1.000 41.122  0 437 ASN AAA C   1 ? 3  
ATOM   843   O O   . ASN A  1 108 ? 20.314  -0.762   0.074   1.000 40.682  0 437 ASN AAA O   1 ? 3  
ATOM   844   C CB  . ASN A  1 108 ? 20.806  -0.628   3.088   1.000 41.800  0 437 ASN AAA CB  1 ? 3  
ATOM   845   C CG  . ASN A  1 108 ? 19.618  0.095    3.644   1.000 43.291  0 437 ASN AAA CG  1 ? 3  
ATOM   846   O OD1 . ASN A  1 108 ? 18.885  0.712    2.889   1.000 44.312  0 437 ASN AAA OD1 1 ? 3  
ATOM   847   N ND2 . ASN A  1 108 ? 19.402  -0.038   4.941   1.000 43.259  0 437 ASN AAA ND2 1 ? 3  
ATOM   848   N N   . SER A  1 109 ? 18.328  -1.590   0.836   1.000 39.568  0 438 SER AAA N   1 ? 3  
ATOM   849   C CA  . SER A  1 109 ? 17.499  -1.190   -0.322  1.000 39.063  0 438 SER AAA CA  1 ? 3  
ATOM   850   C C   . SER A  1 109 ? 16.371  -0.276   0.141   1.000 42.272  0 438 SER AAA C   1 ? 3  
ATOM   851   O O   . SER A  1 109 ? 15.342  -0.204   -0.557  1.000 44.452  0 438 SER AAA O   1 ? 3  
ATOM   852   C CB  . SER A  1 109 ? 16.983  -2.376   -1.043  1.000 39.427  0 438 SER AAA CB  1 ? 3  
ATOM   853   O OG  . SER A  1 109 ? 16.195  -3.193   -0.188  1.000 39.832  0 438 SER AAA OG  1 ? 3  
ATOM   854   N N   . ASN A  1 110 ? 16.575  0.438    1.248   1.000 43.525  0 439 ASN AAA N   1 ? 3  
ATOM   855   C CA  . ASN A  1 110 ? 15.553  1.355    1.800   1.000 44.421  0 439 ASN AAA CA  1 ? 3  
ATOM   856   C C   . ASN A  1 110 ? 15.102  2.313    0.694   1.000 45.799  0 439 ASN AAA C   1 ? 3  
ATOM   857   O O   . ASN A  1 110 ? 13.887  2.511    0.587   1.000 46.197  0 439 ASN AAA O   1 ? 3  
ATOM   858   C CB  . ASN A  1 110 ? 16.073  2.119    3.023   1.000 45.467  0 439 ASN AAA CB  1 ? 3  
ATOM   859   C CG  . ASN A  1 110 ? 14.964  2.672    3.889   1.000 46.076  0 439 ASN AAA CG  1 ? 3  
ATOM   860   O OD1 . ASN A  1 110 ? 13.878  2.086    3.979   1.000 46.998  0 439 ASN AAA OD1 1 ? 3  
ATOM   861   N ND2 . ASN A  1 110 ? 15.234  3.772    4.558   1.000 47.877  0 439 ASN AAA ND2 1 ? 3  
ATOM   862   N N   . ASN A  1 111 ? 16.015  2.855    -0.117  1.000 46.017  0 440 ASN AAA N   1 ? 3  
ATOM   863   C CA  . ASN A  1 111 ? 15.665  3.901    -1.125  1.000 47.426  0 440 ASN AAA CA  1 ? 3  
ATOM   864   C C   . ASN A  1 111 ? 14.741  3.326    -2.213  1.000 48.598  0 440 ASN AAA C   1 ? 3  
ATOM   865   O O   . ASN A  1 111 ? 13.961  4.097    -2.797  1.000 53.027  0 440 ASN AAA O   1 ? 3  
ATOM   866   C CB  . ASN A  1 111 ? 16.891  4.556    -1.767  1.000 47.296  0 440 ASN AAA CB  1 ? 3  
ATOM   867   C CG  . ASN A  1 111 ? 16.524  5.670    -2.732  1.000 49.495  0 440 ASN AAA CG  1 ? 3  
ATOM   868   O OD1 . ASN A  1 111 ? 16.330  5.446    -3.930  1.000 51.184  0 440 ASN AAA OD1 1 ? 3  
ATOM   869   N ND2 . ASN A  1 111 ? 16.374  6.881    -2.228  1.000 50.770  0 440 ASN AAA ND2 1 ? 3  
ATOM   870   N N   . LEU A  1 112 ? 14.787  2.021    -2.482  1.000 48.234  0 441 LEU AAA N   1 ? 3  
ATOM   871   C CA  . LEU A  1 112 ? 13.991  1.396    -3.573  1.000 48.010  0 441 LEU AAA CA  1 ? 3  
ATOM   872   C C   . LEU A  1 112 ? 12.772  0.666    -3.011  1.000 47.350  0 441 LEU AAA C   1 ? 3  
ATOM   873   O O   . LEU A  1 112 ? 11.759  0.687    -3.689  1.000 47.422  0 441 LEU AAA O   1 ? 3  
ATOM   874   C CB  . LEU A  1 112 ? 14.874  0.408    -4.343  1.000 47.271  0 441 LEU AAA CB  1 ? 3  
ATOM   875   C CG  . LEU A  1 112 ? 16.002  1.010    -5.179  1.000 46.907  0 441 LEU AAA CG  1 ? 3  
ATOM   876   C CD1 . LEU A  1 112 ? 16.712  -0.069   -5.972  1.000 44.240  0 441 LEU AAA CD1 1 ? 3  
ATOM   877   C CD2 . LEU A  1 112 ? 15.476  2.071    -6.121  1.000 48.709  0 441 LEU AAA CD2 1 ? 3  
ATOM   878   N N   . ASP A  1 113 ? 12.876  0.043    -1.835  1.000 47.509  0 442 ASP AAA N   1 ? 3  
ATOM   879   C CA  . ASP A  1 113 ? 11.907  -0.980   -1.366  1.000 49.037  0 442 ASP AAA CA  1 ? 3  
ATOM   880   C C   . ASP A  1 113 ? 11.035  -0.485   -0.202  1.000 53.245  0 442 ASP AAA C   1 ? 3  
ATOM   881   O O   . ASP A  1 113 ? 10.256  -1.294   0.317   1.000 53.420  0 442 ASP AAA O   1 ? 3  
ATOM   882   C CB  . ASP A  1 113 ? 12.637  -2.250   -0.950  1.000 47.145  0 442 ASP AAA CB  1 ? 3  
ATOM   883   C CG  . ASP A  1 113 ? 13.166  -3.050   -2.117  1.000 46.403  0 442 ASP AAA CG  1 ? 3  
ATOM   884   O OD1 . ASP A  1 113 ? 12.478  -3.077   -3.188  1.000 46.141  0 442 ASP AAA OD1 1 ? 3  
ATOM   885   O OD2 . ASP A  1 113 ? 14.253  -3.665   -1.945  1.000 44.179  0 442 ASP AAA OD2 1 ? 3  
ATOM   886   N N   . SER A  1 114 ? 11.148  0.765    0.221   1.000 56.130  0 443 SER AAA N   1 ? 3  
ATOM   887   C CA  . SER A  1 114 ? 10.285  1.289    1.298   1.000 62.384  0 443 SER AAA CA  1 ? 3  
ATOM   888   C C   . SER A  1 114 ? 9.464   2.444    0.717   1.000 65.617  0 443 SER AAA C   1 ? 3  
ATOM   889   O O   . SER A  1 114 ? 9.934   3.078    -0.227  1.000 65.329  0 443 SER AAA O   1 ? 3  
ATOM   890   C CB  . SER A  1 114 ? 11.108  1.651    2.503   1.000 64.401  0 443 SER AAA CB  1 ? 3  
ATOM   891   O OG  . SER A  1 114 ? 11.618  2.968    2.383   1.000 69.588  0 443 SER AAA OG  1 ? 3  
ATOM   892   N N   . LYS A  1 115 ? 8.232   2.639    1.190   1.000 69.027  0 444 LYS AAA N   1 ? 3  
ATOM   893   C CA  . LYS A  1 115 ? 7.325   3.710    0.684   1.000 72.003  0 444 LYS AAA CA  1 ? 3  
ATOM   894   C C   . LYS A  1 115 ? 6.746   4.475    1.869   1.000 72.284  0 444 LYS AAA C   1 ? 3  
ATOM   895   O O   . LYS A  1 115 ? 6.676   3.876    2.958   1.000 69.467  0 444 LYS AAA O   1 ? 3  
ATOM   896   C CB  . LYS A  1 115 ? 6.174   3.101    -0.123  1.000 77.017  0 444 LYS AAA CB  1 ? 3  
ATOM   897   C CG  . LYS A  1 115 ? 6.413   3.052    -1.621  1.000 81.517  0 444 LYS AAA CG  1 ? 3  
ATOM   898   C CD  . LYS A  1 115 ? 5.716   1.905    -2.321  1.000 86.511  0 444 LYS AAA CD  1 ? 3  
ATOM   899   C CE  . LYS A  1 115 ? 6.534   1.366    -3.478  1.000 89.135  0 444 LYS AAA CE  1 ? 3  
ATOM   900   N NZ  . LYS A  1 115 ? 6.223   -0.060   -3.750  1.000 91.926  0 444 LYS AAA NZ  1 ? 3  
ATOM   901   N N   . VAL A  1 116 ? 6.281   5.694    1.629   1.000 74.215  0 445 VAL AAA N   1 ? 3  
ATOM   902   C CA  . VAL A  1 116 ? 5.674   6.577    2.662   1.000 76.161  0 445 VAL AAA CA  1 ? 3  
ATOM   903   C C   . VAL A  1 116 ? 4.497   5.898    3.365   1.000 77.061  0 445 VAL AAA C   1 ? 3  
ATOM   904   O O   . VAL A  1 116 ? 4.446   6.075    4.600   1.000 79.453  0 445 VAL AAA O   1 ? 3  
ATOM   905   C CB  . VAL A  1 116 ? 5.296   7.962    2.110   1.000 79.445  0 445 VAL AAA CB  1 ? 3  
ATOM   906   C CG1 . VAL A  1 116 ? 6.557   8.756    1.756   1.000 79.797  0 445 VAL AAA CG1 1 ? 3  
ATOM   907   C CG2 . VAL A  1 116 ? 4.327   7.868    0.929   1.000 80.260  0 445 VAL AAA CG2 1 ? 3  
ATOM   908   N N   . GLY A  1 117 ? 3.624   5.138    2.681   1.000 74.925  0 446 GLY AAA N   1 ? 3  
ATOM   909   C CA  . GLY A  1 117 ? 2.517   4.429    3.354   1.000 75.221  0 446 GLY AAA CA  1 ? 3  
ATOM   910   C C   . GLY A  1 117 ? 2.957   3.147    4.062   1.000 70.909  0 446 GLY AAA C   1 ? 3  
ATOM   911   O O   . GLY A  1 117 ? 2.121   2.445    4.610   1.000 69.392  0 446 GLY AAA O   1 ? 3  
ATOM   912   N N   . GLY A  1 118 ? 4.224   2.758    3.879   1.000 67.496  0 447 GLY AAA N   1 ? 3  
ATOM   913   C CA  . GLY A  1 118 ? 4.729   1.386    4.091   1.000 63.953  0 447 GLY AAA CA  1 ? 3  
ATOM   914   C C   . GLY A  1 118 ? 4.585   0.547    2.835   1.000 62.340  0 447 GLY AAA C   1 ? 3  
ATOM   915   O O   . GLY A  1 118 ? 3.496   0.577    2.217   1.000 63.419  0 447 GLY AAA O   1 ? 3  
ATOM   916   N N   . ASN A  1 119 ? 5.643   -0.178   2.456   1.000 59.575  0 448 ASN AAA N   1 ? 3  
ATOM   917   C CA  . ASN A  1 119 ? 5.594   -1.173   1.360   1.000 57.934  0 448 ASN AAA CA  1 ? 3  
ATOM   918   C C   . ASN A  1 119 ? 5.236   -2.535   1.957   1.000 58.624  0 448 ASN AAA C   1 ? 3  
ATOM   919   O O   . ASN A  1 119 ? 6.046   -3.087   2.723   1.000 58.181  0 448 ASN AAA O   1 ? 3  
ATOM   920   C CB  . ASN A  1 119 ? 6.895   -1.186   0.571   1.000 56.229  0 448 ASN AAA CB  1 ? 3  
ATOM   921   C CG  . ASN A  1 119 ? 6.886   -2.199   -0.557  1.000 55.772  0 448 ASN AAA CG  1 ? 3  
ATOM   922   O OD1 . ASN A  1 119 ? 5.847   -2.748   -0.922  1.000 56.738  0 448 ASN AAA OD1 1 ? 3  
ATOM   923   N ND2 . ASN A  1 119 ? 8.052   -2.451   -1.117  1.000 56.541  0 448 ASN AAA ND2 1 ? 3  
ATOM   924   N N   . TYR A  1 120 ? 4.060   -3.062   1.619   1.000 59.726  0 449 TYR AAA N   1 ? 3  
ATOM   925   C CA  . TYR A  1 120 ? 3.528   -4.336   2.171   1.000 60.025  0 449 TYR AAA CA  1 ? 3  
ATOM   926   C C   . TYR A  1 120 ? 3.664   -5.439   1.113   1.000 57.844  0 449 TYR AAA C   1 ? 3  
ATOM   927   O O   . TYR A  1 120 ? 3.160   -6.547   1.376   1.000 60.771  0 449 TYR AAA O   1 ? 3  
ATOM   928   C CB  . TYR A  1 120 ? 2.101   -4.113   2.705   1.000 63.732  0 449 TYR AAA CB  1 ? 3  
ATOM   929   C CG  . TYR A  1 120 ? 2.034   -3.182   3.893   1.000 67.026  0 449 TYR AAA CG  1 ? 3  
ATOM   930   C CD1 . TYR A  1 120 ? 2.375   -3.621   5.165   1.000 68.675  0 449 TYR AAA CD1 1 ? 3  
ATOM   931   C CD2 . TYR A  1 120 ? 1.682   -1.842   3.755   1.000 70.238  0 449 TYR AAA CD2 1 ? 3  
ATOM   932   C CE1 . TYR A  1 120 ? 2.371   -2.767   6.262   1.000 70.264  0 449 TYR AAA CE1 1 ? 3  
ATOM   933   C CE2 . TYR A  1 120 ? 1.662   -0.975   4.840   1.000 72.246  0 449 TYR AAA CE2 1 ? 3  
ATOM   934   C CZ  . TYR A  1 120 ? 2.000   -1.443   6.100   1.000 73.168  0 449 TYR AAA CZ  1 ? 3  
ATOM   935   O OH  . TYR A  1 120 ? 1.994   -0.632   7.193   1.000 76.623  0 449 TYR AAA OH  1 ? 3  
ATOM   936   N N   . ASN A  1 121 ? 4.368   -5.195   0.000   1.000 56.367  0 450 ASN AAA N   1 ? 3  
ATOM   937   C CA  . ASN A  1 121 ? 4.510   -6.192   -1.102  1.000 59.068  0 450 ASN AAA CA  1 ? 3  
ATOM   938   C C   . ASN A  1 121 ? 5.411   -7.374   -0.702  1.000 56.433  0 450 ASN AAA C   1 ? 3  
ATOM   939   O O   . ASN A  1 121 ? 5.204   -8.465   -1.221  1.000 55.215  0 450 ASN AAA O   1 ? 3  
ATOM   940   C CB  . ASN A  1 121 ? 5.002   -5.564   -2.405  1.000 60.930  0 450 ASN AAA CB  1 ? 3  
ATOM   941   C CG  . ASN A  1 121 ? 3.921   -4.721   -3.055  1.000 70.079  0 450 ASN AAA CG  1 ? 3  
ATOM   942   O OD1 . ASN A  1 121 ? 2.722   -4.888   -2.791  1.000 73.535  0 450 ASN AAA OD1 1 ? 3  
ATOM   943   N ND2 . ASN A  1 121 ? 4.329   -3.800   -3.916  1.000 74.375  0 450 ASN AAA ND2 1 ? 3  
ATOM   944   N N   . TYR A  1 122 ? 6.390   -7.178   0.179   1.000 54.105  0 451 TYR AAA N   1 ? 3  
ATOM   945   C CA  . TYR A  1 122 ? 7.358   -8.239   0.552   1.000 49.673  0 451 TYR AAA CA  1 ? 3  
ATOM   946   C C   . TYR A  1 122 ? 6.795   -9.036   1.731   1.000 49.846  0 451 TYR AAA C   1 ? 3  
ATOM   947   O O   . TYR A  1 122 ? 6.426   -8.445   2.779   1.000 52.380  0 451 TYR AAA O   1 ? 3  
ATOM   948   C CB  . TYR A  1 122 ? 8.729   -7.635   0.840   1.000 48.165  0 451 TYR AAA CB  1 ? 3  
ATOM   949   C CG  . TYR A  1 122 ? 9.401   -7.025   -0.364  1.000 46.315  0 451 TYR AAA CG  1 ? 3  
ATOM   950   C CD1 . TYR A  1 122 ? 9.927   -7.822   -1.362  1.000 44.897  0 451 TYR AAA CD1 1 ? 3  
ATOM   951   C CD2 . TYR A  1 122 ? 9.533   -5.653   -0.500  1.000 45.860  0 451 TYR AAA CD2 1 ? 3  
ATOM   952   C CE1 . TYR A  1 122 ? 10.578  -7.278   -2.454  1.000 43.613  0 451 TYR AAA CE1 1 ? 3  
ATOM   953   C CE2 . TYR A  1 122 ? 10.216  -5.095   -1.570  1.000 44.393  0 451 TYR AAA CE2 1 ? 3  
ATOM   954   C CZ  . TYR A  1 122 ? 10.712  -5.909   -2.564  1.000 42.890  0 451 TYR AAA CZ  1 ? 3  
ATOM   955   O OH  . TYR A  1 122 ? 11.344  -5.369   -3.642  1.000 43.849  0 451 TYR AAA OH  1 ? 3  
ATOM   956   N N   . LEU A  1 123 ? 6.737   -10.356  1.550   1.000 48.435  0 452 LEU AAA N   1 ? 3  
ATOM   957   C CA  . LEU A  1 123 ? 6.154   -11.328  2.510   1.000 49.965  0 452 LEU AAA CA  1 ? 3  
ATOM   958   C C   . LEU A  1 123 ? 7.249   -12.265  3.018   1.000 48.235  0 452 LEU AAA C   1 ? 3  
ATOM   959   O O   . LEU A  1 123 ? 8.278   -12.414  2.324   1.000 43.935  0 452 LEU AAA O   1 ? 3  
ATOM   960   C CB  . LEU A  1 123 ? 5.048   -12.131  1.808   1.000 52.009  0 452 LEU AAA CB  1 ? 3  
ATOM   961   C CG  . LEU A  1 123 ? 3.893   -11.325  1.190   1.000 52.692  0 452 LEU AAA CG  1 ? 3  
ATOM   962   C CD1 . LEU A  1 123 ? 2.844   -12.267  0.616   1.000 53.086  0 452 LEU AAA CD1 1 ? 3  
ATOM   963   C CD2 . LEU A  1 123 ? 3.239   -10.410  2.205   1.000 53.265  0 452 LEU AAA CD2 1 ? 3  
ATOM   964   N N   . TYR A  1 124 ? 7.030   -12.860  4.193   1.000 48.863  0 453 TYR AAA N   1 ? 3  
ATOM   965   C CA  . TYR A  1 124 ? 7.860   -13.959  4.742   1.000 47.223  0 453 TYR AAA CA  1 ? 3  
ATOM   966   C C   . TYR A  1 124 ? 6.931   -14.997  5.385   1.000 48.379  0 453 TYR AAA C   1 ? 3  
ATOM   967   O O   . TYR A  1 124 ? 5.847   -14.618  5.859   1.000 49.973  0 453 TYR AAA O   1 ? 3  
ATOM   968   C CB  . TYR A  1 124 ? 8.885   -13.406  5.731   1.000 45.336  0 453 TYR AAA CB  1 ? 3  
ATOM   969   C CG  . TYR A  1 124 ? 8.271   -12.787  6.955   1.000 48.535  0 453 TYR AAA CG  1 ? 3  
ATOM   970   C CD1 . TYR A  1 124 ? 7.970   -13.554  8.069   1.000 49.183  0 453 TYR AAA CD1 1 ? 3  
ATOM   971   C CD2 . TYR A  1 124 ? 7.960   -11.436  6.990   1.000 49.188  0 453 TYR AAA CD2 1 ? 3  
ATOM   972   C CE1 . TYR A  1 124 ? 7.392   -12.993  9.196   1.000 50.907  0 453 TYR AAA CE1 1 ? 3  
ATOM   973   C CE2 . TYR A  1 124 ? 7.375   -10.861  8.107   1.000 50.516  0 453 TYR AAA CE2 1 ? 3  
ATOM   974   C CZ  . TYR A  1 124 ? 7.092   -11.643  9.214   1.000 50.976  0 453 TYR AAA CZ  1 ? 3  
ATOM   975   O OH  . TYR A  1 124 ? 6.522   -11.090  10.320  1.000 50.624  0 453 TYR AAA OH  1 ? 3  
ATOM   976   N N   . ARG A  1 125 ? 7.321   -16.270  5.358   1.000 47.892  0 454 ARG AAA N   1 ? 3  
ATOM   977   C CA  . ARG A  1 125 ? 6.577   -17.361  6.033   1.000 49.807  0 454 ARG AAA CA  1 ? 3  
ATOM   978   C C   . ARG A  1 125 ? 6.862   -17.262  7.534   1.000 51.419  0 454 ARG AAA C   1 ? 3  
ATOM   979   O O   . ARG A  1 125 ? 8.044   -17.267  7.923   1.000 50.213  0 454 ARG AAA O   1 ? 3  
ATOM   980   C CB  . ARG A  1 125 ? 6.949   -18.724  5.448   1.000 49.820  0 454 ARG AAA CB  1 ? 3  
ATOM   981   C CG  . ARG A  1 125 ? 6.106   -19.879  5.984   1.000 51.523  0 454 ARG AAA CG  1 ? 3  
ATOM   982   C CD  . ARG A  1 125 ? 6.381   -21.189  5.264   1.000 51.228  0 454 ARG AAA CD  1 ? 3  
ATOM   983   N NE  . ARG A  1 125 ? 6.136   -21.023  3.848   1.000 50.631  0 454 ARG AAA NE  1 ? 3  
ATOM   984   C CZ  . ARG A  1 125 ? 4.944   -21.034  3.250   1.000 53.673  0 454 ARG AAA CZ  1 ? 3  
ATOM   985   N NH1 . ARG A  1 125 ? 3.825   -21.192  3.938   1.000 54.443  0 454 ARG AAA NH1 1 ? 3  
ATOM   986   N NH2 . ARG A  1 125 ? 4.882   -20.873  1.941   1.000 54.110  0 454 ARG AAA NH2 1 ? 3  
ATOM   987   N N   . LEU A  1 126 ? 5.807   -17.142  8.338   1.000 54.292  0 455 LEU AAA N   1 ? 3  
ATOM   988   C CA  . LEU A  1 126 ? 5.882   -16.954  9.802   1.000 56.516  0 455 LEU AAA CA  1 ? 3  
ATOM   989   C C   . LEU A  1 126 ? 5.733   -18.302  10.517  1.000 60.187  0 455 LEU AAA C   1 ? 3  
ATOM   990   O O   . LEU A  1 126 ? 6.352   -18.452  11.602  1.000 61.847  0 455 LEU AAA O   1 ? 3  
ATOM   991   C CB  . LEU A  1 126 ? 4.763   -15.986  10.192  1.000 59.391  0 455 LEU AAA CB  1 ? 3  
ATOM   992   C CG  . LEU A  1 126 ? 4.580   -15.717  11.682  1.000 62.929  0 455 LEU AAA CG  1 ? 3  
ATOM   993   C CD1 . LEU A  1 126 ? 5.861   -15.176  12.301  1.000 61.216  0 455 LEU AAA CD1 1 ? 3  
ATOM   994   C CD2 . LEU A  1 126 ? 3.417   -14.758  11.889  1.000 65.470  0 455 LEU AAA CD2 1 ? 3  
ATOM   995   N N   . PHE A  1 127 ? 4.944   -19.219  9.950   1.000 62.396  0 456 PHE AAA N   1 ? 3  
ATOM   996   C CA  . PHE A  1 127 ? 4.630   -20.551  10.544  1.000 64.706  0 456 PHE AAA CA  1 ? 3  
ATOM   997   C C   . PHE A  1 127 ? 4.904   -21.647  9.515   1.000 62.736  0 456 PHE AAA C   1 ? 3  
ATOM   998   O O   . PHE A  1 127 ? 4.588   -21.471  8.327   1.000 60.481  0 456 PHE AAA O   1 ? 3  
ATOM   999   C CB  . PHE A  1 127 ? 3.167   -20.661  10.996  1.000 68.309  0 456 PHE AAA CB  1 ? 3  
ATOM   1000  C CG  . PHE A  1 127 ? 2.713   -19.574  11.932  1.000 72.041  0 456 PHE AAA CG  1 ? 3  
ATOM   1001  C CD1 . PHE A  1 127 ? 3.199   -19.534  13.227  1.000 75.879  0 456 PHE AAA CD1 1 ? 3  
ATOM   1002  C CD2 . PHE A  1 127 ? 1.810   -18.597  11.537  1.000 74.294  0 456 PHE AAA CD2 1 ? 3  
ATOM   1003  C CE1 . PHE A  1 127 ? 2.804   -18.535  14.111  1.000 78.018  0 456 PHE AAA CE1 1 ? 3  
ATOM   1004  C CE2 . PHE A  1 127 ? 1.392   -17.620  12.433  1.000 78.114  0 456 PHE AAA CE2 1 ? 3  
ATOM   1005  C CZ  . PHE A  1 127 ? 1.898   -17.581  13.713  1.000 79.504  0 456 PHE AAA CZ  1 ? 3  
ATOM   1006  N N   . ARG A  1 128 ? 5.452   -22.768  9.968   1.000 62.372  0 457 ARG AAA N   1 ? 3  
ATOM   1007  C CA  . ARG A  1 128 ? 5.567   -23.996  9.150   1.000 63.685  0 457 ARG AAA CA  1 ? 3  
ATOM   1008  C C   . ARG A  1 128 ? 5.695   -25.213  10.069  1.000 66.437  0 457 ARG AAA C   1 ? 3  
ATOM   1009  O O   . ARG A  1 128 ? 6.259   -25.053  11.165  1.000 69.248  0 457 ARG AAA O   1 ? 3  
ATOM   1010  C CB  . ARG A  1 128 ? 6.766   -23.853  8.230   1.000 59.449  0 457 ARG AAA CB  1 ? 3  
ATOM   1011  C CG  . ARG A  1 128 ? 6.852   -24.887  7.132   1.000 58.653  0 457 ARG AAA CG  1 ? 3  
ATOM   1012  C CD  . ARG A  1 128 ? 7.987   -24.518  6.202   1.000 56.871  0 457 ARG AAA CD  1 ? 3  
ATOM   1013  N NE  . ARG A  1 128 ? 7.873   -25.284  4.974   1.000 57.211  0 457 ARG AAA NE  1 ? 3  
ATOM   1014  C CZ  . ARG A  1 128 ? 8.380   -26.490  4.773   1.000 58.061  0 457 ARG AAA CZ  1 ? 3  
ATOM   1015  N NH1 . ARG A  1 128 ? 9.075   -27.111  5.726   1.000 58.397  0 457 ARG AAA NH1 1 ? 3  
ATOM   1016  N NH2 . ARG A  1 128 ? 8.175   -27.064  3.606   1.000 58.639  0 457 ARG AAA NH2 1 ? 3  
ATOM   1017  N N   . LYS A  1 129 ? 5.181   -26.368  9.636   1.000 68.181  0 458 LYS AAA N   1 ? 3  
ATOM   1018  C CA  . LYS A  1 129 ? 5.114   -27.611  10.449  1.000 70.293  0 458 LYS AAA CA  1 ? 3  
ATOM   1019  C C   . LYS A  1 129 ? 6.527   -28.116  10.758  1.000 65.934  0 458 LYS AAA C   1 ? 3  
ATOM   1020  O O   . LYS A  1 129 ? 6.715   -28.775  11.783  1.000 69.715  0 458 LYS AAA O   1 ? 3  
ATOM   1021  C CB  . LYS A  1 129 ? 4.382   -28.726  9.701   1.000 74.518  0 458 LYS AAA CB  1 ? 3  
ATOM   1022  C CG  . LYS A  1 129 ? 2.918   -28.494  9.391   1.000 80.252  0 458 LYS AAA CG  1 ? 3  
ATOM   1023  C CD  . LYS A  1 129 ? 2.305   -29.740  8.788   1.000 83.629  0 458 LYS AAA CD  1 ? 3  
ATOM   1024  C CE  . LYS A  1 129 ? 0.897   -29.498  8.320   1.000 88.166  0 458 LYS AAA CE  1 ? 3  
ATOM   1025  N NZ  . LYS A  1 129 ? 0.357   -30.715  7.681   1.000 93.054  0 458 LYS AAA NZ  1 ? 3  
ATOM   1026  N N   . SER A  1 130 ? 7.492   -27.825  9.896   1.000 61.406  0 459 SER AAA N   1 ? 3  
ATOM   1027  C CA  . SER A  1 130 ? 8.887   -28.284  10.064  1.000 59.230  0 459 SER AAA CA  1 ? 3  
ATOM   1028  C C   . SER A  1 130 ? 9.820   -27.359  9.275   1.000 55.790  0 459 SER AAA C   1 ? 3  
ATOM   1029  O O   . SER A  1 130 ? 9.331   -26.599  8.422   1.000 52.887  0 459 SER AAA O   1 ? 3  
ATOM   1030  C CB  . SER A  1 130 ? 9.014   -29.720  9.636   1.000 59.092  0 459 SER AAA CB  1 ? 3  
ATOM   1031  O OG  . SER A  1 130 ? 9.082   -29.818  8.231   1.000 56.609  0 459 SER AAA OG  1 ? 3  
ATOM   1032  N N   . ASN A  1 131 ? 11.113  -27.417  9.580   1.000 52.307  0 460 ASN AAA N   1 ? 3  
ATOM   1033  C CA  . ASN A  1 131 ? 12.133  -26.535  8.975   1.000 49.783  0 460 ASN AAA CA  1 ? 3  
ATOM   1034  C C   . ASN A  1 131 ? 12.362  -26.949  7.524   1.000 49.029  0 460 ASN AAA C   1 ? 3  
ATOM   1035  O O   . ASN A  1 131 ? 12.248  -28.126  7.229   1.000 49.942  0 460 ASN AAA O   1 ? 3  
ATOM   1036  C CB  . ASN A  1 131 ? 13.452  -26.559  9.749   1.000 49.774  0 460 ASN AAA CB  1 ? 3  
ATOM   1037  C CG  . ASN A  1 131 ? 13.324  -25.971  11.141  1.000 50.064  0 460 ASN AAA CG  1 ? 3  
ATOM   1038  O OD1 . ASN A  1 131 ? 12.288  -25.421  11.499  1.000 49.930  0 460 ASN AAA OD1 1 ? 3  
ATOM   1039  N ND2 . ASN A  1 131 ? 14.380  -26.088  11.928  1.000 48.956  0 460 ASN AAA ND2 1 ? 3  
ATOM   1040  N N   . LEU A  1 132 ? 12.671  -25.980  6.667   1.000 47.727  0 461 LEU AAA N   1 ? 3  
ATOM   1041  C CA  . LEU A  1 132 ? 13.113  -26.211  5.282   1.000 47.056  0 461 LEU AAA CA  1 ? 3  
ATOM   1042  C C   . LEU A  1 132 ? 14.392  -27.045  5.299   1.000 47.189  0 461 LEU AAA C   1 ? 3  
ATOM   1043  O O   . LEU A  1 132 ? 15.247  -26.807  6.142   1.000 46.607  0 461 LEU AAA O   1 ? 3  
ATOM   1044  C CB  . LEU A  1 132 ? 13.366  -24.868  4.593   1.000 45.759  0 461 LEU AAA CB  1 ? 3  
ATOM   1045  C CG  . LEU A  1 132 ? 12.129  -24.017  4.282   1.000 46.486  0 461 LEU AAA CG  1 ? 3  
ATOM   1046  C CD1 . LEU A  1 132 ? 12.512  -22.782  3.504   1.000 45.245  0 461 LEU AAA CD1 1 ? 3  
ATOM   1047  C CD2 . LEU A  1 132 ? 11.096  -24.813  3.509   1.000 48.430  0 461 LEU AAA CD2 1 ? 3  
ATOM   1048  N N   . LYS A  1 133 ? 14.502  -27.987  4.360   1.000 50.854  0 462 LYS AAA N   1 ? 3  
ATOM   1049  C CA  . LYS A  1 133 ? 15.785  -28.585  3.921   1.000 50.159  0 462 LYS AAA CA  1 ? 3  
ATOM   1050  C C   . LYS A  1 133 ? 16.589  -27.515  3.192   1.000 48.525  0 462 LYS AAA C   1 ? 3  
ATOM   1051  O O   . LYS A  1 133 ? 16.029  -26.540  2.680   1.000 47.880  0 462 LYS AAA O   1 ? 3  
ATOM   1052  C CB  . LYS A  1 133 ? 15.518  -29.785  3.005   1.000 54.164  0 462 LYS AAA CB  1 ? 3  
ATOM   1053  C CG  . LYS A  1 133 ? 15.086  -31.067  3.720   1.000 59.305  0 462 LYS AAA CG  1 ? 3  
ATOM   1054  C CD  . LYS A  1 133 ? 14.067  -31.947  2.984   1.000 62.263  0 462 LYS AAA CD  1 ? 3  
ATOM   1055  C CE  . LYS A  1 133 ? 13.126  -32.619  3.963   1.000 67.267  0 462 LYS AAA CE  1 ? 3  
ATOM   1056  N NZ  . LYS A  1 133 ? 12.572  -33.881  3.425   1.000 71.351  0 462 LYS AAA NZ  1 ? 3  
ATOM   1057  N N   . PRO A  1 134 ? 17.929  -27.635  3.125   1.000 46.130  0 463 PRO AAA N   1 ? 3  
ATOM   1058  C CA  . PRO A  1 134 ? 18.731  -26.669  2.384   1.000 45.424  0 463 PRO AAA CA  1 ? 3  
ATOM   1059  C C   . PRO A  1 134 ? 18.223  -26.496  0.942   1.000 44.440  0 463 PRO AAA C   1 ? 3  
ATOM   1060  O O   . PRO A  1 134 ? 17.931  -27.498  0.295   1.000 47.550  0 463 PRO AAA O   1 ? 3  
ATOM   1061  C CB  . PRO A  1 134 ? 20.146  -27.278  2.420   1.000 45.035  0 463 PRO AAA CB  1 ? 3  
ATOM   1062  C CG  . PRO A  1 134 ? 20.133  -28.105  3.701   1.000 45.495  0 463 PRO AAA CG  1 ? 3  
ATOM   1063  C CD  . PRO A  1 134 ? 18.737  -28.662  3.794   1.000 45.491  0 463 PRO AAA CD  1 ? 3  
ATOM   1064  N N   . PHE A  1 135 ? 18.069  -25.243  0.509   1.000 43.104  0 464 PHE AAA N   1 ? 3  
ATOM   1065  C CA  . PHE A  1 135 ? 17.642  -24.854  -0.862  1.000 44.537  0 464 PHE AAA CA  1 ? 3  
ATOM   1066  C C   . PHE A  1 135 ? 16.192  -25.282  -1.134  1.000 43.996  0 464 PHE AAA C   1 ? 3  
ATOM   1067  O O   . PHE A  1 135 ? 15.780  -25.250  -2.300  1.000 45.240  0 464 PHE AAA O   1 ? 3  
ATOM   1068  C CB  . PHE A  1 135 ? 18.603  -25.426  -1.923  1.000 44.232  0 464 PHE AAA CB  1 ? 3  
ATOM   1069  C CG  . PHE A  1 135 ? 20.004  -24.881  -1.855  1.000 40.916  0 464 PHE AAA CG  1 ? 3  
ATOM   1070  C CD1 . PHE A  1 135 ? 20.203  -23.522  -1.899  1.000 42.385  0 464 PHE AAA CD1 1 ? 3  
ATOM   1071  C CD2 . PHE A  1 135 ? 21.113  -25.702  -1.702  1.000 42.066  0 464 PHE AAA CD2 1 ? 3  
ATOM   1072  C CE1 . PHE A  1 135 ? 21.467  -22.971  -1.792  1.000 40.771  0 464 PHE AAA CE1 1 ? 3  
ATOM   1073  C CE2 . PHE A  1 135 ? 22.377  -25.161  -1.531  1.000 39.750  0 464 PHE AAA CE2 1 ? 3  
ATOM   1074  C CZ  . PHE A  1 135 ? 22.547  -23.806  -1.591  1.000 39.072  0 464 PHE AAA CZ  1 ? 3  
ATOM   1075  N N   . GLU A  1 136 ? 15.429  -25.641  -0.108  1.000 43.682  0 465 GLU AAA N   1 ? 3  
ATOM   1076  C CA  . GLU A  1 136 ? 13.983  -25.944  -0.277  1.000 46.047  0 465 GLU AAA CA  1 ? 3  
ATOM   1077  C C   . GLU A  1 136 ? 13.210  -24.623  -0.404  1.000 44.169  0 465 GLU AAA C   1 ? 3  
ATOM   1078  O O   . GLU A  1 136 ? 13.664  -23.605  0.119   1.000 43.573  0 465 GLU AAA O   1 ? 3  
ATOM   1079  C CB  . GLU A  1 136 ? 13.479  -26.842  0.857   1.000 48.546  0 465 GLU AAA CB  1 ? 3  
ATOM   1080  C CG  . GLU A  1 136 ? 12.151  -27.500  0.566   1.000 50.571  0 465 GLU AAA CG  1 ? 3  
ATOM   1081  C CD  . GLU A  1 136 ? 11.555  -28.343  1.679   1.000 54.002  0 465 GLU AAA CD  1 ? 3  
ATOM   1082  O OE1 . GLU A  1 136 ? 12.236  -28.529  2.731   1.000 52.976  0 465 GLU AAA OE1 1 ? 3  
ATOM   1083  O OE2 . GLU A  1 136 ? 10.384  -28.800  1.481   1.000 54.071  0 465 GLU AAA OE2 1 ? 3  
ATOM   1084  N N   . ARG A  1 137 ? 12.097  -24.658  -1.117  1.000 45.787  0 466 ARG AAA N   1 ? 3  
ATOM   1085  C CA  . ARG A  1 137 ? 11.254  -23.475  -1.412  1.000 46.089  0 466 ARG AAA CA  1 ? 3  
ATOM   1086  C C   . ARG A  1 137 ? 9.802   -23.850  -1.153  1.000 46.899  0 466 ARG AAA C   1 ? 3  
ATOM   1087  O O   . ARG A  1 137 ? 9.386   -24.859  -1.683  1.000 46.460  0 466 ARG AAA O   1 ? 3  
ATOM   1088  C CB  . ARG A  1 137 ? 11.432  -23.071  -2.870  1.000 46.666  0 466 ARG AAA CB  1 ? 3  
ATOM   1089  C CG  . ARG A  1 137 ? 10.789  -21.749  -3.257  1.000 49.292  0 466 ARG AAA CG  1 ? 3  
ATOM   1090  C CD  . ARG A  1 137 ? 11.437  -21.374  -4.572  1.000 49.974  0 466 ARG AAA CD  1 ? 3  
ATOM   1091  N NE  . ARG A  1 137 ? 10.972  -20.128  -5.118  1.000 53.251  0 466 ARG AAA NE  1 ? 3  
ATOM   1092  C CZ  . ARG A  1 137 ? 9.893   -19.979  -5.895  1.000 57.226  0 466 ARG AAA CZ  1 ? 3  
ATOM   1093  N NH1 . ARG A  1 137 ? 9.112   -21.006  -6.192  1.000 60.635  0 466 ARG AAA NH1 1 ? 3  
ATOM   1094  N NH2 . ARG A  1 137 ? 9.582   -18.785  -6.363  1.000 57.344  0 466 ARG AAA NH2 1 ? 3  
ATOM   1095  N N   . ASP A  1 138 ? 9.089   -23.079  -0.341  1.000 47.169  0 467 ASP AAA N   1 ? 3  
ATOM   1096  C CA  . ASP A  1 138 ? 7.675   -23.344  -0.014  1.000 47.967  0 467 ASP AAA CA  1 ? 3  
ATOM   1097  C C   . ASP A  1 138 ? 6.877   -22.101  -0.377  1.000 47.692  0 467 ASP AAA C   1 ? 3  
ATOM   1098  O O   . ASP A  1 138 ? 7.116   -21.063  0.255   1.000 45.478  0 467 ASP AAA O   1 ? 3  
ATOM   1099  C CB  . ASP A  1 138 ? 7.559   -23.744  1.451   1.000 48.634  0 467 ASP AAA CB  1 ? 3  
ATOM   1100  C CG  . ASP A  1 138 ? 6.158   -24.167  1.866   1.000 51.153  0 467 ASP AAA CG  1 ? 3  
ATOM   1101  O OD1 . ASP A  1 138 ? 5.183   -23.931  1.066   1.000 52.736  0 467 ASP AAA OD1 1 ? 3  
ATOM   1102  O OD2 . ASP A  1 138 ? 6.051   -24.710  2.988   1.000 49.874  0 467 ASP AAA OD2 1 ? 3  
ATOM   1103  N N   . ILE A  1 139 ? 5.992   -22.203  -1.372  1.000 50.900  0 468 ILE AAA N   1 ? 3  
ATOM   1104  C CA  . ILE A  1 139 ? 5.115   -21.073  -1.810  1.000 50.367  0 468 ILE AAA CA  1 ? 3  
ATOM   1105  C C   . ILE A  1 139 ? 3.655   -21.393  -1.498  1.000 51.499  0 468 ILE AAA C   1 ? 3  
ATOM   1106  O O   . ILE A  1 139 ? 2.793   -20.618  -1.938  1.000 52.067  0 468 ILE AAA O   1 ? 3  
ATOM   1107  C CB  . ILE A  1 139 ? 5.354   -20.715  -3.279  1.000 50.793  0 468 ILE AAA CB  1 ? 3  
ATOM   1108  C CG1 . ILE A  1 139 ? 5.024   -21.859  -4.231  1.000 51.640  0 468 ILE AAA CG1 1 ? 3  
ATOM   1109  C CG2 . ILE A  1 139 ? 6.783   -20.230  -3.448  1.000 50.886  0 468 ILE AAA CG2 1 ? 3  
ATOM   1110  C CD1 . ILE A  1 139 ? 5.046   -21.444  -5.702  1.000 52.092  0 468 ILE AAA CD1 1 ? 3  
ATOM   1111  N N   . SER A  1 140 ? 3.403   -22.436  -0.700  1.000 52.370  0 469 SER AAA N   1 ? 3  
ATOM   1112  C CA  . SER A  1 140 ? 2.034   -22.832  -0.287  1.000 54.476  0 469 SER AAA CA  1 ? 3  
ATOM   1113  C C   . SER A  1 140 ? 1.457   -21.750  0.634   1.000 53.884  0 469 SER AAA C   1 ? 3  
ATOM   1114  O O   . SER A  1 140 ? 2.227   -21.044  1.312   1.000 50.094  0 469 SER AAA O   1 ? 3  
ATOM   1115  C CB  . SER A  1 140 ? 2.009   -24.192  0.370   1.000 55.514  0 469 SER AAA CB  1 ? 3  
ATOM   1116  O OG  . SER A  1 140 ? 2.688   -24.145  1.610   1.000 55.387  0 469 SER AAA OG  1 ? 3  
ATOM   1117  N N   . THR A  1 141 ? 0.131   -21.654  0.647   1.000 56.393  0 470 THR AAA N   1 ? 3  
ATOM   1118  C CA  . THR A  1 141 ? -0.629  -20.701  1.483   1.000 57.793  0 470 THR AAA CA  1 ? 3  
ATOM   1119  C C   . THR A  1 141 ? -1.736  -21.488  2.180   1.000 61.246  0 470 THR AAA C   1 ? 3  
ATOM   1120  O O   . THR A  1 141 ? -2.845  -20.973  2.267   1.000 65.488  0 470 THR AAA O   1 ? 3  
ATOM   1121  C CB  . THR A  1 141 ? -1.121  -19.511  0.651   1.000 57.000  0 470 THR AAA CB  1 ? 3  
ATOM   1122  O OG1 . THR A  1 141 ? -1.826  -20.025  -0.474  1.000 59.260  0 470 THR AAA OG1 1 ? 3  
ATOM   1123  C CG2 . THR A  1 141 ? -0.014  -18.653  0.085   1.000 54.524  0 470 THR AAA CG2 1 ? 3  
ATOM   1124  N N   . GLU A  1 142 ? -1.451  -22.710  2.629   1.000 62.995  0 471 GLU AAA N   1 ? 3  
ATOM   1125  C CA  . GLU A  1 142 ? -2.368  -23.505  3.467   1.000 67.360  0 471 GLU AAA CA  1 ? 3  
ATOM   1126  C C   . GLU A  1 142 ? -2.432  -22.889  4.859   1.000 68.291  0 471 GLU AAA C   1 ? 3  
ATOM   1127  O O   . GLU A  1 142 ? -1.382  -22.448  5.366   1.000 67.404  0 471 GLU AAA O   1 ? 3  
ATOM   1128  C CB  . GLU A  1 142 ? -1.946  -24.973  3.503   1.000 68.993  0 471 GLU AAA CB  1 ? 3  
ATOM   1129  C CG  . GLU A  1 142 ? -2.047  -25.629  2.141   1.000 72.191  0 471 GLU AAA CG  1 ? 3  
ATOM   1130  C CD  . GLU A  1 142 ? -3.450  -25.679  1.525   1.000 76.862  0 471 GLU AAA CD  1 ? 3  
ATOM   1131  O OE1 . GLU A  1 142 ? -4.428  -26.124  2.229   1.000 77.631  0 471 GLU AAA OE1 1 ? 3  
ATOM   1132  O OE2 . GLU A  1 142 ? -3.576  -25.216  0.364   1.000 77.060  0 471 GLU AAA OE2 1 ? 3  
ATOM   1133  N N   . ILE A  1 143 ? -3.640  -22.845  5.426   1.000 70.648  0 472 ILE AAA N   1 ? 3  
ATOM   1134  C CA  . ILE A  1 143 ? -3.879  -22.371  6.814   1.000 72.450  0 472 ILE AAA CA  1 ? 3  
ATOM   1135  C C   . ILE A  1 143 ? -3.069  -23.269  7.741   1.000 71.534  0 472 ILE AAA C   1 ? 3  
ATOM   1136  O O   . ILE A  1 143 ? -3.182  -24.487  7.609   1.000 71.889  0 472 ILE AAA O   1 ? 3  
ATOM   1137  C CB  . ILE A  1 143 ? -5.380  -22.371  7.132   1.000 77.510  0 472 ILE AAA CB  1 ? 3  
ATOM   1138  C CG1 . ILE A  1 143 ? -6.142  -21.417  6.207   1.000 78.273  0 472 ILE AAA CG1 1 ? 3  
ATOM   1139  C CG2 . ILE A  1 143 ? -5.630  -22.039  8.580   1.000 79.234  0 472 ILE AAA CG2 1 ? 3  
ATOM   1140  C CD1 . ILE A  1 143 ? -5.531  -20.020  6.115   1.000 75.439  0 472 ILE AAA CD1 1 ? 3  
ATOM   1141  N N   . TYR A  1 144 ? -2.253  -22.667  8.603   1.000 70.769  0 473 TYR AAA N   1 ? 3  
ATOM   1142  C CA  . TYR A  1 144 ? -1.383  -23.384  9.563   1.000 71.795  0 473 TYR AAA CA  1 ? 3  
ATOM   1143  C C   . TYR A  1 144 ? -2.220  -23.723  10.801  1.000 76.523  0 473 TYR AAA C   1 ? 3  
ATOM   1144  O O   . TYR A  1 144 ? -2.852  -22.826  11.382  1.000 76.201  0 473 TYR AAA O   1 ? 3  
ATOM   1145  C CB  . TYR A  1 144 ? -0.140  -22.555  9.877   1.000 68.878  0 473 TYR AAA CB  1 ? 3  
ATOM   1146  C CG  . TYR A  1 144 ? 0.750   -23.103  10.968  1.000 69.244  0 473 TYR AAA CG  1 ? 3  
ATOM   1147  C CD1 . TYR A  1 144 ? 1.734   -24.044  10.699  1.000 67.966  0 473 TYR AAA CD1 1 ? 3  
ATOM   1148  C CD2 . TYR A  1 144 ? 0.630   -22.644  12.273  1.000 70.911  0 473 TYR AAA CD2 1 ? 3  
ATOM   1149  C CE1 . TYR A  1 144 ? 2.551   -24.536  11.702  1.000 68.187  0 473 TYR AAA CE1 1 ? 3  
ATOM   1150  C CE2 . TYR A  1 144 ? 1.474   -23.096  13.273  1.000 71.425  0 473 TYR AAA CE2 1 ? 3  
ATOM   1151  C CZ  . TYR A  1 144 ? 2.441   -24.041  12.986  1.000 70.474  0 473 TYR AAA CZ  1 ? 3  
ATOM   1152  O OH  . TYR A  1 144 ? 3.196   -24.542  14.002  1.000 70.472  0 473 TYR AAA OH  1 ? 3  
ATOM   1153  N N   . GLN A  1 145 ? -2.241  -25.014  11.137  1.000 79.984  0 474 GLN AAA N   1 ? 3  
ATOM   1154  C CA  . GLN A  1 145 ? -2.859  -25.549  12.367  1.000 84.672  0 474 GLN AAA CA  1 ? 3  
ATOM   1155  C C   . GLN A  1 145 ? -1.869  -25.386  13.523  1.000 84.958  0 474 GLN AAA C   1 ? 3  
ATOM   1156  O O   . GLN A  1 145 ? -0.917  -26.185  13.600  1.000 85.382  0 474 GLN AAA O   1 ? 3  
ATOM   1157  C CB  . GLN A  1 145 ? -3.250  -27.007  12.177  1.000 86.509  0 474 GLN AAA CB  1 ? 3  
ATOM   1158  C CG  . GLN A  1 145 ? -3.799  -27.585  13.457  1.000 91.503  0 474 GLN AAA CG  1 ? 3  
ATOM   1159  C CD  . GLN A  1 145 ? -4.423  -28.928  13.216  1.000 94.617  0 474 GLN AAA CD  1 ? 3  
ATOM   1160  O OE1 . GLN A  1 145 ? -4.751  -29.302  12.093  1.000 94.296  0 474 GLN AAA OE1 1 ? 3  
ATOM   1161  N NE2 . GLN A  1 145 ? -4.612  -29.656  14.294  1.000 98.484  0 474 GLN AAA NE2 1 ? 3  
ATOM   1162  N N   . ALA A  1 146 ? -2.082  -24.368  14.354  1.000 84.801  0 475 ALA AAA N   1 ? 3  
ATOM   1163  C CA  . ALA A  1 146 ? -1.215  -24.007  15.503  1.000 85.196  0 475 ALA AAA CA  1 ? 3  
ATOM   1164  C C   . ALA A  1 146 ? -1.708  -24.732  16.764  1.000 89.676  0 475 ALA AAA C   1 ? 3  
ATOM   1165  O O   . ALA A  1 146 ? -0.957  -24.785  17.750  1.000 90.403  0 475 ALA AAA O   1 ? 3  
ATOM   1166  C CB  . ALA A  1 146 ? -1.196  -22.506  15.711  1.000 84.174  0 475 ALA AAA CB  1 ? 3  
ATOM   1167  N N   . GLY A  1 147 ? -2.924  -25.293  16.728  1.000 92.220  0 476 GLY AAA N   1 ? 3  
ATOM   1168  C CA  . GLY A  1 147 ? -3.582  -25.855  17.917  1.000 94.007  0 476 GLY AAA CA  1 ? 3  
ATOM   1169  C C   . GLY A  1 147 ? -4.124  -27.243  17.654  1.000 96.407  0 476 GLY AAA C   1 ? 3  
ATOM   1170  O O   . GLY A  1 147 ? -3.892  -27.792  16.556  1.000 94.233  0 476 GLY AAA O   1 ? 3  
ATOM   1171  N N   . SER A  1 148 ? -4.818  -27.778  18.655  1.000 100.732 0 477 SER AAA N   1 ? 3  
ATOM   1172  C CA  . SER A  1 148 ? -5.434  -29.124  18.660  1.000 104.854 0 477 SER AAA CA  1 ? 3  
ATOM   1173  C C   . SER A  1 148 ? -6.420  -29.267  17.490  1.000 107.621 0 477 SER AAA C   1 ? 3  
ATOM   1174  O O   . SER A  1 148 ? -6.348  -30.305  16.801  1.000 110.338 0 477 SER AAA O   1 ? 3  
ATOM   1175  C CB  . SER A  1 148 ? -6.077  -29.362  19.993  1.000 107.329 0 477 SER AAA CB  1 ? 3  
ATOM   1176  O OG  . SER A  1 148 ? -6.765  -30.602  20.045  1.000 112.900 0 477 SER AAA OG  1 ? 3  
ATOM   1177  N N   . THR A  1 149 ? -7.317  -28.301  17.283  1.000 108.641 0 478 THR AAA N   1 ? 3  
ATOM   1178  C CA  . THR A  1 149 ? -8.474  -28.439  16.343  1.000 110.192 0 478 THR AAA CA  1 ? 3  
ATOM   1179  C C   . THR A  1 149 ? -7.964  -28.407  14.904  1.000 105.511 0 478 THR AAA C   1 ? 3  
ATOM   1180  O O   . THR A  1 149 ? -7.065  -27.638  14.588  1.000 102.626 0 478 THR AAA O   1 ? 3  
ATOM   1181  C CB  . THR A  1 149 ? -9.543  -27.364  16.590  1.000 112.187 0 478 THR AAA CB  1 ? 3  
ATOM   1182  O OG1 . THR A  1 149 ? -8.865  -26.113  16.633  1.000 109.831 0 478 THR AAA OG1 1 ? 3  
ATOM   1183  C CG2 . THR A  1 149 ? -10.319 -27.563  17.873  1.000 114.538 0 478 THR AAA CG2 1 ? 3  
ATOM   1184  N N   . PRO A  1 150 ? -8.506  -29.234  13.981  1.000 107.690 0 479 PRO AAA N   1 ? 3  
ATOM   1185  C CA  . PRO A  1 150 ? -8.200  -29.085  12.552  1.000 104.884 0 479 PRO AAA CA  1 ? 3  
ATOM   1186  C C   . PRO A  1 150 ? -8.823  -27.781  12.011  1.000 105.131 0 479 PRO AAA C   1 ? 3  
ATOM   1187  O O   . PRO A  1 150 ? -9.818  -27.335  12.571  1.000 107.116 0 479 PRO AAA O   1 ? 3  
ATOM   1188  C CB  . PRO A  1 150 ? -8.797  -30.352  11.917  1.000 107.387 0 479 PRO AAA CB  1 ? 3  
ATOM   1189  C CG  . PRO A  1 150 ? -9.922  -30.752  12.863  1.000 111.746 0 479 PRO AAA CG  1 ? 3  
ATOM   1190  C CD  . PRO A  1 150 ? -9.454  -30.334  14.244  1.000 111.350 0 479 PRO AAA CD  1 ? 3  
ATOM   1191  N N   . CYS A  1 151 ? -8.243  -27.193  10.965  1.000 102.716 0 480 CYS AAA N   1 ? 3  
ATOM   1192  C CA  . CYS A  1 151 ? -8.570  -25.818  10.501  1.000 103.487 0 480 CYS AAA CA  1 ? 3  
ATOM   1193  C C   . CYS A  1 151 ? -9.603  -25.823  9.366   1.000 105.580 0 480 CYS AAA C   1 ? 3  
ATOM   1194  O O   . CYS A  1 151 ? -10.213 -24.758  9.126   1.000 107.202 0 480 CYS AAA O   1 ? 3  
ATOM   1195  C CB  . CYS A  1 151 ? -7.316  -25.083  10.043  1.000 97.927  0 480 CYS AAA CB  1 ? 3  
ATOM   1196  S SG  . CYS A  1 151 ? -6.262  -24.613  11.424  1.000 98.280  0 480 CYS AAA SG  1 ? 3  
ATOM   1197  N N   . ASN A  1 152 ? -9.733  -26.949  8.654   1.000 106.008 0 481 ASN AAA N   1 ? 3  
ATOM   1198  C CA  . ASN A  1 152 ? -10.595 -27.092  7.447   1.000 109.594 0 481 ASN AAA CA  1 ? 3  
ATOM   1199  C C   . ASN A  1 152 ? -10.371 -25.922  6.471   1.000 107.983 0 481 ASN AAA C   1 ? 3  
ATOM   1200  O O   . ASN A  1 152 ? -11.361 -25.477  5.855   1.000 109.009 0 481 ASN AAA O   1 ? 3  
ATOM   1201  C CB  . ASN A  1 152 ? -12.076 -27.192  7.820   1.000 112.505 0 481 ASN AAA CB  1 ? 3  
ATOM   1202  C CG  . ASN A  1 152 ? -12.375 -28.362  8.728   1.000 114.283 0 481 ASN AAA CG  1 ? 3  
ATOM   1203  O OD1 . ASN A  1 152 ? -11.531 -28.807  9.505   1.000 112.037 0 481 ASN AAA OD1 1 ? 3  
ATOM   1204  N ND2 . ASN A  1 152 ? -13.592 -28.860  8.640   1.000 119.679 0 481 ASN AAA ND2 1 ? 3  
ATOM   1205  N N   . GLY A  1 153 ? -9.127  -25.443  6.342   1.000 107.180 0 482 GLY AAA N   1 ? 3  
ATOM   1206  C CA  . GLY A  1 153 ? -8.708  -24.356  5.423   1.000 105.483 0 482 GLY AAA CA  1 ? 3  
ATOM   1207  C C   . GLY A  1 153 ? -9.471  -23.052  5.636   1.000 106.090 0 482 GLY AAA C   1 ? 3  
ATOM   1208  O O   . GLY A  1 153 ? -9.640  -22.288  4.665   1.000 105.545 0 482 GLY AAA O   1 ? 3  
ATOM   1209  N N   . VAL A  1 154 ? -9.905  -22.796  6.874   1.000 105.687 0 483 VAL AAA N   1 ? 3  
ATOM   1210  C CA  . VAL A  1 154 ? -10.584 -21.540  7.298   1.000 105.001 0 483 VAL AAA CA  1 ? 3  
ATOM   1211  C C   . VAL A  1 154 ? -9.764  -20.928  8.437   1.000 102.146 0 483 VAL AAA C   1 ? 3  
ATOM   1212  O O   . VAL A  1 154 ? -9.281  -21.689  9.297   1.000 99.824  0 483 VAL AAA O   1 ? 3  
ATOM   1213  C CB  . VAL A  1 154 ? -12.041 -21.802  7.707   1.000 108.937 0 483 VAL AAA CB  1 ? 3  
ATOM   1214  C CG1 . VAL A  1 154 ? -12.631 -20.655  8.528   1.000 110.311 0 483 VAL AAA CG1 1 ? 3  
ATOM   1215  C CG2 . VAL A  1 154 ? -12.890 -22.129  6.485   1.000 110.490 0 483 VAL AAA CG2 1 ? 3  
ATOM   1216  N N   . GLU A  1 155 ? -9.584  -19.608  8.353   1.000 100.537 0 484 GLU AAA N   1 ? 3  
ATOM   1217  C CA  . GLU A  1 155 ? -8.776  -18.807  9.295   1.000 97.030  0 484 GLU AAA CA  1 ? 3  
ATOM   1218  C C   . GLU A  1 155 ? -9.567  -18.591  10.587  1.000 98.401  0 484 GLU AAA C   1 ? 3  
ATOM   1219  O O   . GLU A  1 155 ? -10.826 -18.568  10.526  1.000 96.583  0 484 GLU AAA O   1 ? 3  
ATOM   1220  C CB  . GLU A  1 155 ? -8.443  -17.464  8.658   1.000 95.916  0 484 GLU AAA CB  1 ? 3  
ATOM   1221  C CG  . GLU A  1 155 ? -7.624  -17.627  7.403   1.000 97.392  0 484 GLU AAA CG  1 ? 3  
ATOM   1222  C CD  . GLU A  1 155 ? -6.922  -16.356  6.965   1.000 99.523  0 484 GLU AAA CD  1 ? 3  
ATOM   1223  O OE1 . GLU A  1 155 ? -6.556  -15.586  7.885   1.000 100.517 0 484 GLU AAA OE1 1 ? 3  
ATOM   1224  O OE2 . GLU A  1 155 ? -6.800  -16.112  5.718   1.000 101.961 0 484 GLU AAA OE2 1 ? 3  
ATOM   1225  N N   . GLY A  1 156 ? -8.849  -18.425  11.702  1.000 96.349  0 485 GLY AAA N   1 ? 3  
ATOM   1226  C CA  . GLY A  1 156 ? -9.430  -18.087  13.013  1.000 96.941  0 485 GLY AAA CA  1 ? 3  
ATOM   1227  C C   . GLY A  1 156 ? -8.503  -18.467  14.148  1.000 94.788  0 485 GLY AAA C   1 ? 3  
ATOM   1228  O O   . GLY A  1 156 ? -7.276  -18.515  13.914  1.000 90.238  0 485 GLY AAA O   1 ? 3  
ATOM   1229  N N   . PHE A  1 157 ? -9.083  -18.720  15.328  1.000 97.793  0 486 PHE AAA N   1 ? 3  
ATOM   1230  C CA  . PHE A  1 157 ? -8.406  -19.179  16.573  1.000 98.711  0 486 PHE AAA CA  1 ? 3  
ATOM   1231  C C   . PHE A  1 157 ? -7.445  -20.323  16.220  1.000 96.014  0 486 PHE AAA C   1 ? 3  
ATOM   1232  O O   . PHE A  1 157 ? -7.952  -21.330  15.719  1.000 96.369  0 486 PHE AAA O   1 ? 3  
ATOM   1233  C CB  . PHE A  1 157 ? -9.490  -19.538  17.610  1.000 102.379 0 486 PHE AAA CB  1 ? 3  
ATOM   1234  C CG  . PHE A  1 157 ? -9.109  -20.464  18.746  1.000 104.325 0 486 PHE AAA CG  1 ? 3  
ATOM   1235  C CD1 . PHE A  1 157 ? -7.992  -20.191  19.517  1.000 103.427 0 486 PHE AAA CD1 1 ? 3  
ATOM   1236  C CD2 . PHE A  1 157 ? -9.884  -21.581  19.071  1.000 108.974 0 486 PHE AAA CD2 1 ? 3  
ATOM   1237  C CE1 . PHE A  1 157 ? -7.650  -21.015  20.588  1.000 104.725 0 486 PHE AAA CE1 1 ? 3  
ATOM   1238  C CE2 . PHE A  1 157 ? -9.521  -22.417  20.119  1.000 110.948 0 486 PHE AAA CE2 1 ? 3  
ATOM   1239  C CZ  . PHE A  1 157 ? -8.384  -22.149  20.856  1.000 108.103 0 486 PHE AAA CZ  1 ? 3  
ATOM   1240  N N   . ASN A  1 158 ? -6.147  -20.159  16.489  1.000 92.819  0 487 ASN AAA N   1 ? 3  
ATOM   1241  C CA  . ASN A  1 158 ? -5.084  -21.185  16.278  1.000 91.357  0 487 ASN AAA CA  1 ? 3  
ATOM   1242  C C   . ASN A  1 158 ? -5.040  -21.695  14.825  1.000 89.927  0 487 ASN AAA C   1 ? 3  
ATOM   1243  O O   . ASN A  1 158 ? -4.488  -22.785  14.593  1.000 87.949  0 487 ASN AAA O   1 ? 3  
ATOM   1244  C CB  . ASN A  1 158 ? -5.294  -22.339  17.256  1.000 92.706  0 487 ASN AAA CB  1 ? 3  
ATOM   1245  C CG  . ASN A  1 158 ? -4.871  -21.945  18.654  1.000 94.392  0 487 ASN AAA CG  1 ? 3  
ATOM   1246  O OD1 . ASN A  1 158 ? -5.696  -21.700  19.519  1.000 100.196 0 487 ASN AAA OD1 1 ? 3  
ATOM   1247  N ND2 . ASN A  1 158 ? -3.571  -21.819  18.863  1.000 92.727  0 487 ASN AAA ND2 1 ? 3  
ATOM   1248  N N   . CYS A  1 159 ? -5.575  -20.912  13.893  1.000 89.184  0 488 CYS AAA N   1 ? 3  
ATOM   1249  C CA  . CYS A  1 159 ? -5.679  -21.257  12.451  1.000 87.670  0 488 CYS AAA CA  1 ? 3  
ATOM   1250  C C   . CYS A  1 159 ? -5.217  -20.060  11.618  1.000 81.899  0 488 CYS AAA C   1 ? 3  
ATOM   1251  O O   . CYS A  1 159 ? -6.063  -19.260  11.209  1.000 80.944  0 488 CYS AAA O   1 ? 3  
ATOM   1252  C CB  . CYS A  1 159 ? -7.095  -21.684  12.105  1.000 92.362  0 488 CYS AAA CB  1 ? 3  
ATOM   1253  S SG  . CYS A  1 159 ? -7.436  -23.394  12.610  1.000 97.896  0 488 CYS AAA SG  1 ? 3  
ATOM   1254  N N   . TYR A  1 160 ? -3.906  -19.950  11.419  1.000 76.423  0 489 TYR AAA N   1 ? 3  
ATOM   1255  C CA  . TYR A  1 160 ? -3.253  -18.724  10.895  1.000 74.801  0 489 TYR AAA CA  1 ? 3  
ATOM   1256  C C   . TYR A  1 160 ? -2.918  -18.918  9.420   1.000 71.789  0 489 TYR AAA C   1 ? 3  
ATOM   1257  O O   . TYR A  1 160 ? -2.494  -20.020  9.013   1.000 70.604  0 489 TYR AAA O   1 ? 3  
ATOM   1258  C CB  . TYR A  1 160 ? -2.031  -18.339  11.730  1.000 74.151  0 489 TYR AAA CB  1 ? 3  
ATOM   1259  C CG  . TYR A  1 160 ? -2.303  -18.282  13.212  1.000 77.364  0 489 TYR AAA CG  1 ? 3  
ATOM   1260  C CD1 . TYR A  1 160 ? -3.392  -17.572  13.693  1.000 80.319  0 489 TYR AAA CD1 1 ? 3  
ATOM   1261  C CD2 . TYR A  1 160 ? -1.541  -18.996  14.123  1.000 77.462  0 489 TYR AAA CD2 1 ? 3  
ATOM   1262  C CE1 . TYR A  1 160 ? -3.702  -17.544  15.039  1.000 83.068  0 489 TYR AAA CE1 1 ? 3  
ATOM   1263  C CE2 . TYR A  1 160 ? -1.849  -18.986  15.474  1.000 80.287  0 489 TYR AAA CE2 1 ? 3  
ATOM   1264  C CZ  . TYR A  1 160 ? -2.927  -18.254  15.932  1.000 83.731  0 489 TYR AAA CZ  1 ? 3  
ATOM   1265  O OH  . TYR A  1 160 ? -3.248  -18.225  17.257  1.000 91.174  0 489 TYR AAA OH  1 ? 3  
ATOM   1266  N N   . PHE A  1 161 ? -3.147  -17.865  8.649   1.000 69.014  0 490 PHE AAA N   1 ? 3  
ATOM   1267  C CA  . PHE A  1 161 ? -2.568  -17.701  7.302   1.000 66.716  0 490 PHE AAA CA  1 ? 3  
ATOM   1268  C C   . PHE A  1 161 ? -1.066  -17.643  7.492   1.000 63.184  0 490 PHE AAA C   1 ? 3  
ATOM   1269  O O   . PHE A  1 161 ? -0.610  -16.902  8.339   1.000 60.688  0 490 PHE AAA O   1 ? 3  
ATOM   1270  C CB  . PHE A  1 161 ? -3.158  -16.462  6.620   1.000 67.618  0 490 PHE AAA CB  1 ? 3  
ATOM   1271  C CG  . PHE A  1 161 ? -2.788  -16.337  5.172   1.000 66.034  0 490 PHE AAA CG  1 ? 3  
ATOM   1272  C CD1 . PHE A  1 161 ? -3.414  -17.136  4.223   1.000 67.203  0 490 PHE AAA CD1 1 ? 3  
ATOM   1273  C CD2 . PHE A  1 161 ? -1.802  -15.449  4.766   1.000 62.909  0 490 PHE AAA CD2 1 ? 3  
ATOM   1274  C CE1 . PHE A  1 161 ? -3.042  -17.062  2.887   1.000 66.110  0 490 PHE AAA CE1 1 ? 3  
ATOM   1275  C CE2 . PHE A  1 161 ? -1.438  -15.376  3.428   1.000 62.368  0 490 PHE AAA CE2 1 ? 3  
ATOM   1276  C CZ  . PHE A  1 161 ? -2.052  -16.190  2.493   1.000 64.382  0 490 PHE AAA CZ  1 ? 3  
ATOM   1277  N N   . PRO A  1 162 ? -0.265  -18.468  6.782   1.000 63.230  0 491 PRO AAA N   1 ? 3  
ATOM   1278  C CA  . PRO A  1 162 ? 1.144   -18.657  7.143   1.000 60.112  0 491 PRO AAA CA  1 ? 3  
ATOM   1279  C C   . PRO A  1 162 ? 2.112   -17.554  6.686   1.000 57.867  0 491 PRO AAA C   1 ? 3  
ATOM   1280  O O   . PRO A  1 162 ? 3.239   -17.556  7.149   1.000 55.163  0 491 PRO AAA O   1 ? 3  
ATOM   1281  C CB  . PRO A  1 162 ? 1.468   -19.991  6.455   1.000 59.451  0 491 PRO AAA CB  1 ? 3  
ATOM   1282  C CG  . PRO A  1 162 ? 0.616   -19.962  5.182   1.000 60.757  0 491 PRO AAA CG  1 ? 3  
ATOM   1283  C CD  . PRO A  1 162 ? -0.670  -19.286  5.621   1.000 63.499  0 491 PRO AAA CD  1 ? 3  
ATOM   1284  N N   . LEU A  1 163 ? 1.690   -16.656  5.798   1.000 58.652  0 492 LEU AAA N   1 ? 3  
ATOM   1285  C CA  . LEU A  1 163 ? 2.563   -15.557  5.268   1.000 56.138  0 492 LEU AAA CA  1 ? 3  
ATOM   1286  C C   . LEU A  1 163 ? 2.241   -14.248  5.989   1.000 56.715  0 492 LEU AAA C   1 ? 3  
ATOM   1287  O O   . LEU A  1 163 ? 1.073   -14.032  6.295   1.000 57.810  0 492 LEU AAA O   1 ? 3  
ATOM   1288  C CB  . LEU A  1 163 ? 2.339   -15.394  3.762   1.000 56.041  0 492 LEU AAA CB  1 ? 3  
ATOM   1289  C CG  . LEU A  1 163 ? 2.678   -16.606  2.889   1.000 56.593  0 492 LEU AAA CG  1 ? 3  
ATOM   1290  C CD1 . LEU A  1 163 ? 2.702   -16.222  1.412   1.000 55.920  0 492 LEU AAA CD1 1 ? 3  
ATOM   1291  C CD2 . LEU A  1 163 ? 4.040   -17.204  3.256   1.000 56.083  0 492 LEU AAA CD2 1 ? 3  
ATOM   1292  N N   . GLN A  1 164 ? 3.244   -13.413  6.241   1.000 57.530  0 493 GLN AAA N   1 ? 3  
ATOM   1293  C CA  . GLN A  1 164 ? 3.104   -12.088  6.885   1.000 59.728  0 493 GLN AAA CA  1 ? 3  
ATOM   1294  C C   . GLN A  1 164 ? 3.873   -11.078  6.041   1.000 57.397  0 493 GLN AAA C   1 ? 3  
ATOM   1295  O O   . GLN A  1 164 ? 4.865   -11.444  5.390   1.000 55.126  0 493 GLN AAA O   1 ? 3  
ATOM   1296  C CB  . GLN A  1 164 ? 3.586   -12.167  8.340   1.000 65.103  0 493 GLN AAA CB  1 ? 3  
ATOM   1297  C CG  . GLN A  1 164 ? 3.478   -10.867  9.125   1.000 70.019  0 493 GLN AAA CG  1 ? 3  
ATOM   1298  C CD  . GLN A  1 164 ? 2.023   -10.481  9.316   1.000 79.189  0 493 GLN AAA CD  1 ? 3  
ATOM   1299  O OE1 . GLN A  1 164 ? 1.175   -11.296  9.691   1.000 79.822  0 493 GLN AAA OE1 1 ? 3  
ATOM   1300  N NE2 . GLN A  1 164 ? 1.700   -9.231   9.015   1.000 84.197  0 493 GLN AAA NE2 1 ? 3  
ATOM   1301  N N   . SER A  1 165 ? 3.409   -9.836   6.033   1.000 60.213  0 494 SER AAA N   1 ? 3  
ATOM   1302  C CA  . SER A  1 165 ? 3.983   -8.721   5.255   1.000 59.004  0 494 SER AAA CA  1 ? 3  
ATOM   1303  C C   . SER A  1 165 ? 5.062   -8.030   6.093   1.000 56.721  0 494 SER AAA C   1 ? 3  
ATOM   1304  O O   . SER A  1 165 ? 4.904   -7.976   7.313   1.000 56.827  0 494 SER AAA O   1 ? 3  
ATOM   1305  C CB  . SER A  1 165 ? 2.874   -7.796   4.853   1.000 61.949  0 494 SER AAA CB  1 ? 3  
ATOM   1306  O OG  . SER A  1 165 ? 3.392   -6.682   4.139   1.000 68.702  0 494 SER AAA OG  1 ? 3  
ATOM   1307  N N   . TYR A  1 166 ? 6.130   -7.535   5.471   1.000 54.045  0 495 TYR AAA N   1 ? 3  
ATOM   1308  C CA  . TYR A  1 166 ? 7.193   -6.762   6.165   1.000 51.952  0 495 TYR AAA CA  1 ? 3  
ATOM   1309  C C   . TYR A  1 166 ? 6.704   -5.342   6.472   1.000 53.591  0 495 TYR AAA C   1 ? 3  
ATOM   1310  O O   . TYR A  1 166 ? 7.037   -4.810   7.532   1.000 55.030  0 495 TYR AAA O   1 ? 3  
ATOM   1311  C CB  . TYR A  1 166 ? 8.490   -6.713   5.352   1.000 48.761  0 495 TYR AAA CB  1 ? 3  
ATOM   1312  C CG  . TYR A  1 166 ? 9.401   -7.893   5.570   1.000 45.847  0 495 TYR AAA CG  1 ? 3  
ATOM   1313  C CD1 . TYR A  1 166 ? 10.074  -8.077   6.774   1.000 43.656  0 495 TYR AAA CD1 1 ? 3  
ATOM   1314  C CD2 . TYR A  1 166 ? 9.582   -8.835   4.570   1.000 43.665  0 495 TYR AAA CD2 1 ? 3  
ATOM   1315  C CE1 . TYR A  1 166 ? 10.909  -9.160   6.967   1.000 41.054  0 495 TYR AAA CE1 1 ? 3  
ATOM   1316  C CE2 . TYR A  1 166 ? 10.414  -9.924   4.750   1.000 41.000  0 495 TYR AAA CE2 1 ? 3  
ATOM   1317  C CZ  . TYR A  1 166 ? 11.081  -10.085  5.950   1.000 41.038  0 495 TYR AAA CZ  1 ? 3  
ATOM   1318  O OH  . TYR A  1 166 ? 11.900  -11.168  6.100   1.000 39.999  0 495 TYR AAA OH  1 ? 3  
ATOM   1319  N N   . GLY A  1 167 ? 5.981   -4.704   5.573   1.000 55.268  0 496 GLY AAA N   1 ? 3  
ATOM   1320  C CA  . GLY A  1 167 ? 5.596   -3.293   5.824   1.000 59.356  0 496 GLY AAA CA  1 ? 3  
ATOM   1321  C C   . GLY A  1 167 ? 6.805   -2.396   6.081   1.000 58.583  0 496 GLY AAA C   1 ? 3  
ATOM   1322  O O   . GLY A  1 167 ? 7.061   -2.019   7.238   1.000 58.519  0 496 GLY AAA O   1 ? 3  
ATOM   1323  N N   . PHE A  1 168 ? 7.570   -2.122   5.032   1.000 55.157  0 497 PHE AAA N   1 ? 3  
ATOM   1324  C CA  . PHE A  1 168 ? 8.835   -1.344   5.082   1.000 52.732  0 497 PHE AAA CA  1 ? 3  
ATOM   1325  C C   . PHE A  1 168 ? 8.524   0.144    4.956   1.000 56.216  0 497 PHE AAA C   1 ? 3  
ATOM   1326  O O   . PHE A  1 168 ? 7.995   0.553    3.904   1.000 57.858  0 497 PHE AAA O   1 ? 3  
ATOM   1327  C CB  . PHE A  1 168 ? 9.772   -1.767   3.949   1.000 49.207  0 497 PHE AAA CB  1 ? 3  
ATOM   1328  C CG  . PHE A  1 168 ? 10.384  -3.138   4.116   1.000 46.068  0 497 PHE AAA CG  1 ? 3  
ATOM   1329  C CD1 . PHE A  1 168 ? 11.197  -3.420   5.205   1.000 43.290  0 497 PHE AAA CD1 1 ? 3  
ATOM   1330  C CD2 . PHE A  1 168 ? 10.187  -4.125   3.157   1.000 45.227  0 497 PHE AAA CD2 1 ? 3  
ATOM   1331  C CE1 . PHE A  1 168 ? 11.787  -4.663   5.341   1.000 41.254  0 497 PHE AAA CE1 1 ? 3  
ATOM   1332  C CE2 . PHE A  1 168 ? 10.780  -5.372   3.293   1.000 42.172  0 497 PHE AAA CE2 1 ? 3  
ATOM   1333  C CZ  . PHE A  1 168 ? 11.568  -5.635   4.391   1.000 41.410  0 497 PHE AAA CZ  1 ? 3  
ATOM   1334  N N   . GLN A  1 169 ? 8.881   0.934    5.965   1.000 58.096  0 498 GLN AAA N   1 ? 3  
ATOM   1335  C CA  . GLN A  1 169 ? 8.735   2.410    5.936   1.000 61.867  0 498 GLN AAA CA  1 ? 3  
ATOM   1336  C C   . GLN A  1 169 ? 10.105  3.054    5.947   1.000 61.722  0 498 GLN AAA C   1 ? 3  
ATOM   1337  O O   . GLN A  1 169 ? 11.007  2.571    6.623   1.000 62.741  0 498 GLN AAA O   1 ? 3  
ATOM   1338  C CB  . GLN A  1 169 ? 7.887   2.857    7.112   1.000 65.176  0 498 GLN AAA CB  1 ? 3  
ATOM   1339  C CG  . GLN A  1 169 ? 6.488   2.321    6.925   1.000 68.322  0 498 GLN AAA CG  1 ? 3  
ATOM   1340  C CD  . GLN A  1 169 ? 5.543   2.820    7.970   1.000 73.001  0 498 GLN AAA CD  1 ? 3  
ATOM   1341  O OE1 . GLN A  1 169 ? 5.577   2.324    9.086   1.000 75.675  0 498 GLN AAA OE1 1 ? 3  
ATOM   1342  N NE2 . GLN A  1 169 ? 4.699   3.783    7.605   1.000 77.600  0 498 GLN AAA NE2 1 ? 3  
ATOM   1343  N N   . PRO A  1 170 ? 10.291  4.157    5.191   1.000 62.071  0 499 PRO AAA N   1 ? 3  
ATOM   1344  C CA  . PRO A  1 170 ? 11.603  4.787    5.064   1.000 60.717  0 499 PRO AAA CA  1 ? 3  
ATOM   1345  C C   . PRO A  1 170 ? 12.173  5.214    6.424   1.000 60.346  0 499 PRO AAA C   1 ? 3  
ATOM   1346  O O   . PRO A  1 170 ? 13.372  5.261    6.546   1.000 61.445  0 499 PRO AAA O   1 ? 3  
ATOM   1347  C CB  . PRO A  1 170 ? 11.358  5.982    4.120   1.000 63.274  0 499 PRO AAA CB  1 ? 3  
ATOM   1348  C CG  . PRO A  1 170 ? 9.857   6.195    4.100   1.000 64.772  0 499 PRO AAA CG  1 ? 3  
ATOM   1349  C CD  . PRO A  1 170 ? 9.244   4.856    4.434   1.000 64.149  0 499 PRO AAA CD  1 ? 3  
ATOM   1350  N N   . THR A  1 171 ? 11.304  5.471    7.409   1.000 59.503  0 500 THR AAA N   1 ? 3  
ATOM   1351  C CA  . THR A  1 171 ? 11.656  5.933    8.778   1.000 60.892  0 500 THR AAA CA  1 ? 3  
ATOM   1352  C C   . THR A  1 171 ? 11.996  4.763    9.731   1.000 59.682  0 500 THR AAA C   1 ? 3  
ATOM   1353  O O   . THR A  1 171 ? 12.445  5.042    10.852  1.000 59.984  0 500 THR AAA O   1 ? 3  
ATOM   1354  C CB  . THR A  1 171 ? 10.513  6.781    9.348   1.000 61.852  0 500 THR AAA CB  1 ? 3  
ATOM   1355  O OG1 . THR A  1 171 ? 9.325   6.009    9.238   1.000 61.832  0 500 THR AAA OG1 1 ? 3  
ATOM   1356  C CG2 . THR A  1 171 ? 10.316  8.072    8.600   1.000 63.015  0 500 THR AAA CG2 1 ? 3  
ATOM   1357  N N   . ASN A  1 172 ? 11.789  3.503    9.347   1.000 56.677  0 501 ASN AAA N   1 ? 3  
ATOM   1358  C CA  . ASN A  1 172 ? 12.213  2.317    10.145  1.000 55.488  0 501 ASN AAA CA  1 ? 3  
ATOM   1359  C C   . ASN A  1 172 ? 13.670  2.456    10.593  1.000 54.408  0 501 ASN AAA C   1 ? 3  
ATOM   1360  O O   . ASN A  1 172 ? 14.466  2.995    9.819   1.000 51.170  0 501 ASN AAA O   1 ? 3  
ATOM   1361  C CB  . ASN A  1 172 ? 12.088  1.021    9.349   1.000 53.545  0 501 ASN AAA CB  1 ? 3  
ATOM   1362  C CG  . ASN A  1 172 ? 10.649  0.608    9.127   1.000 54.761  0 501 ASN AAA CG  1 ? 3  
ATOM   1363  O OD1 . ASN A  1 172 ? 9.742   1.273    9.609   1.000 58.959  0 501 ASN AAA OD1 1 ? 3  
ATOM   1364  N ND2 . ASN A  1 172 ? 10.434  -0.486   8.411   1.000 53.968  0 501 ASN AAA ND2 1 ? 3  
ATOM   1365  N N   . GLY A  1 173 ? 14.010  1.951    11.784  1.000 55.158  0 502 GLY AAA N   1 ? 3  
ATOM   1366  C CA  . GLY A  1 173 ? 15.411  1.700    12.189  1.000 54.960  0 502 GLY AAA CA  1 ? 3  
ATOM   1367  C C   . GLY A  1 173 ? 16.119  0.805    11.185  1.000 52.826  0 502 GLY AAA C   1 ? 3  
ATOM   1368  O O   . GLY A  1 173 ? 15.429  0.049    10.480  1.000 55.781  0 502 GLY AAA O   1 ? 3  
ATOM   1369  N N   . VAL A  1 174 ? 17.449  0.869    11.098  1.000 53.087  0 503 VAL AAA N   1 ? 3  
ATOM   1370  C CA  . VAL A  1 174 ? 18.247  0.198    10.020  1.000 53.355  0 503 VAL AAA CA  1 ? 3  
ATOM   1371  C C   . VAL A  1 174 ? 17.953  -1.311   10.001  1.000 50.340  0 503 VAL AAA C   1 ? 3  
ATOM   1372  O O   . VAL A  1 174 ? 17.826  -1.876   8.905   1.000 49.785  0 503 VAL AAA O   1 ? 3  
ATOM   1373  C CB  . VAL A  1 174 ? 19.756  0.487    10.179  1.000 55.340  0 503 VAL AAA CB  1 ? 3  
ATOM   1374  C CG1 . VAL A  1 174 ? 20.605  -0.292   9.154   1.000 56.820  0 503 VAL AAA CG1 1 ? 3  
ATOM   1375  C CG2 . VAL A  1 174 ? 20.028  1.984    10.070  1.000 55.287  0 503 VAL AAA CG2 1 ? 3  
ATOM   1376  N N   . GLY A  1 175 ? 17.878  -1.937   11.176  1.000 50.175  0 504 GLY AAA N   1 ? 3  
ATOM   1377  C CA  . GLY A  1 175 ? 17.587  -3.373   11.349  1.000 48.211  0 504 GLY AAA CA  1 ? 3  
ATOM   1378  C C   . GLY A  1 175 ? 16.238  -3.744   10.763  1.000 49.565  0 504 GLY AAA C   1 ? 3  
ATOM   1379  O O   . GLY A  1 175 ? 16.081  -4.909   10.427  1.000 51.416  0 504 GLY AAA O   1 ? 3  
ATOM   1380  N N   . TYR A  1 176 ? 15.296  -2.807   10.638  1.000 50.423  0 505 TYR AAA N   1 ? 3  
ATOM   1381  C CA  . TYR A  1 176 ? 13.933  -3.067   10.101  1.000 52.302  0 505 TYR AAA CA  1 ? 3  
ATOM   1382  C C   . TYR A  1 176 ? 13.804  -2.526   8.672   1.000 48.015  0 505 TYR AAA C   1 ? 3  
ATOM   1383  O O   . TYR A  1 176 ? 12.707  -2.575   8.111   1.000 48.139  0 505 TYR AAA O   1 ? 3  
ATOM   1384  C CB  . TYR A  1 176 ? 12.876  -2.470   11.040  1.000 56.439  0 505 TYR AAA CB  1 ? 3  
ATOM   1385  C CG  . TYR A  1 176 ? 12.831  -3.103   12.399  1.000 63.524  0 505 TYR AAA CG  1 ? 3  
ATOM   1386  C CD1 . TYR A  1 176 ? 13.695  -2.704   13.416  1.000 67.858  0 505 TYR AAA CD1 1 ? 3  
ATOM   1387  C CD2 . TYR A  1 176 ? 11.912  -4.111   12.672  1.000 69.596  0 505 TYR AAA CD2 1 ? 3  
ATOM   1388  C CE1 . TYR A  1 176 ? 13.644  -3.294   14.672  1.000 72.731  0 505 TYR AAA CE1 1 ? 3  
ATOM   1389  C CE2 . TYR A  1 176 ? 11.853  -4.715   13.922  1.000 73.201  0 505 TYR AAA CE2 1 ? 3  
ATOM   1390  C CZ  . TYR A  1 176 ? 12.722  -4.302   14.922  1.000 74.477  0 505 TYR AAA CZ  1 ? 3  
ATOM   1391  O OH  . TYR A  1 176 ? 12.651  -4.887   16.150  1.000 78.670  0 505 TYR AAA OH  1 ? 3  
ATOM   1392  N N   . GLN A  1 177 ? 14.889  -2.033   8.081   1.000 46.247  0 506 GLN AAA N   1 ? 3  
ATOM   1393  C CA  . GLN A  1 177 ? 14.878  -1.592   6.664   1.000 46.477  0 506 GLN AAA CA  1 ? 3  
ATOM   1394  C C   . GLN A  1 177 ? 15.048  -2.800   5.752   1.000 43.592  0 506 GLN AAA C   1 ? 3  
ATOM   1395  O O   . GLN A  1 177 ? 15.629  -3.812   6.131   1.000 40.832  0 506 GLN AAA O   1 ? 3  
ATOM   1396  C CB  . GLN A  1 177 ? 15.959  -0.555   6.395   1.000 45.955  0 506 GLN AAA CB  1 ? 3  
ATOM   1397  C CG  . GLN A  1 177 ? 15.577  0.807    6.919   1.000 47.002  0 506 GLN AAA CG  1 ? 3  
ATOM   1398  C CD  . GLN A  1 177 ? 16.714  1.784    6.843   1.000 46.312  0 506 GLN AAA CD  1 ? 3  
ATOM   1399  O OE1 . GLN A  1 177 ? 17.598  1.688    6.006   1.000 44.414  0 506 GLN AAA OE1 1 ? 3  
ATOM   1400  N NE2 . GLN A  1 177 ? 16.679  2.749    7.732   1.000 47.263  0 506 GLN AAA NE2 1 ? 3  
ATOM   1401  N N   . PRO A  1 178 ? 14.554  -2.716   4.502   1.000 44.116  0 507 PRO AAA N   1 ? 3  
ATOM   1402  C CA  . PRO A  1 178 ? 14.709  -3.821   3.575   1.000 43.495  0 507 PRO AAA CA  1 ? 3  
ATOM   1403  C C   . PRO A  1 178 ? 16.170  -3.930   3.132   1.000 42.283  0 507 PRO AAA C   1 ? 3  
ATOM   1404  O O   . PRO A  1 178 ? 16.833  -2.917   2.952   1.000 42.621  0 507 PRO AAA O   1 ? 3  
ATOM   1405  C CB  . PRO A  1 178 ? 13.782  -3.430   2.419   1.000 44.743  0 507 PRO AAA CB  1 ? 3  
ATOM   1406  C CG  . PRO A  1 178 ? 13.789  -1.916   2.438   1.000 46.297  0 507 PRO AAA CG  1 ? 3  
ATOM   1407  C CD  . PRO A  1 178 ? 13.876  -1.551   3.903   1.000 46.136  0 507 PRO AAA CD  1 ? 3  
ATOM   1408  N N   . TYR A  1 179 ? 16.641  -5.165   3.009   1.000 40.896  0 508 TYR AAA N   1 ? 3  
ATOM   1409  C CA  . TYR A  1 179 ? 17.946  -5.504   2.416   1.000 39.365  0 508 TYR AAA CA  1 ? 3  
ATOM   1410  C C   . TYR A  1 179 ? 17.684  -6.493   1.296   1.000 39.308  0 508 TYR AAA C   1 ? 3  
ATOM   1411  O O   . TYR A  1 179 ? 16.904  -7.439   1.480   1.000 40.887  0 508 TYR AAA O   1 ? 3  
ATOM   1412  C CB  . TYR A  1 179 ? 18.896  -6.070   3.463   1.000 39.381  0 508 TYR AAA CB  1 ? 3  
ATOM   1413  C CG  . TYR A  1 179 ? 19.585  -5.014   4.281   1.000 41.182  0 508 TYR AAA CG  1 ? 3  
ATOM   1414  C CD1 . TYR A  1 179 ? 18.871  -4.223   5.163   1.000 42.274  0 508 TYR AAA CD1 1 ? 3  
ATOM   1415  C CD2 . TYR A  1 179 ? 20.944  -4.782   4.161   1.000 40.861  0 508 TYR AAA CD2 1 ? 3  
ATOM   1416  C CE1 . TYR A  1 179 ? 19.488  -3.245   5.922   1.000 43.894  0 508 TYR AAA CE1 1 ? 3  
ATOM   1417  C CE2 . TYR A  1 179 ? 21.567  -3.795   4.907   1.000 42.610  0 508 TYR AAA CE2 1 ? 3  
ATOM   1418  C CZ  . TYR A  1 179 ? 20.843  -3.017   5.789   1.000 45.018  0 508 TYR AAA CZ  1 ? 3  
ATOM   1419  O OH  . TYR A  1 179 ? 21.477  -2.033   6.502   1.000 46.638  0 508 TYR AAA OH  1 ? 3  
ATOM   1420  N N   . ARG A  1 180 ? 18.286  -6.222   0.145   1.000 39.326  0 509 ARG AAA N   1 ? 3  
ATOM   1421  C CA  . ARG A  1 180 ? 18.362  -7.177   -0.977  1.000 36.992  0 509 ARG AAA CA  1 ? 3  
ATOM   1422  C C   . ARG A  1 180 ? 19.537  -8.110   -0.725  1.000 36.255  0 509 ARG AAA C   1 ? 3  
ATOM   1423  O O   . ARG A  1 180 ? 20.564  -7.664   -0.233  1.000 35.836  0 509 ARG AAA O   1 ? 3  
ATOM   1424  C CB  . ARG A  1 180 ? 18.458  -6.437   -2.303  1.000 37.583  0 509 ARG AAA CB  1 ? 3  
ATOM   1425  C CG  . ARG A  1 180 ? 17.169  -5.724   -2.646  1.000 37.920  0 509 ARG AAA CG  1 ? 3  
ATOM   1426  C CD  . ARG A  1 180 ? 17.239  -4.952   -3.918  1.000 37.736  0 509 ARG AAA CD  1 ? 3  
ATOM   1427  N NE  . ARG A  1 180 ? 15.950  -4.353   -4.155  1.000 38.172  0 509 ARG AAA NE  1 ? 3  
ATOM   1428  C CZ  . ARG A  1 180 ? 15.571  -3.822   -5.305  1.000 38.584  0 509 ARG AAA CZ  1 ? 3  
ATOM   1429  N NH1 . ARG A  1 180 ? 16.407  -3.794   -6.338  1.000 38.185  0 509 ARG AAA NH1 1 ? 3  
ATOM   1430  N NH2 . ARG A  1 180 ? 14.351  -3.317   -5.404  1.000 38.491  0 509 ARG AAA NH2 1 ? 3  
ATOM   1431  N N   . VAL A  1 181 ? 19.335  -9.383   -1.031  1.000 37.433  0 510 VAL AAA N   1 ? 3  
ATOM   1432  C CA  . VAL A  1 181 ? 20.316  -10.481  -0.835  1.000 37.541  0 510 VAL AAA CA  1 ? 3  
ATOM   1433  C C   . VAL A  1 181 ? 20.493  -11.218  -2.168  1.000 37.249  0 510 VAL AAA C   1 ? 3  
ATOM   1434  O O   . VAL A  1 181 ? 19.494  -11.446  -2.874  1.000 36.891  0 510 VAL AAA O   1 ? 3  
ATOM   1435  C CB  . VAL A  1 181 ? 19.833  -11.418  0.283   1.000 38.712  0 510 VAL AAA CB  1 ? 3  
ATOM   1436  C CG1 . VAL A  1 181 ? 20.859  -12.484  0.589   1.000 37.301  0 510 VAL AAA CG1 1 ? 3  
ATOM   1437  C CG2 . VAL A  1 181 ? 19.445  -10.638  1.538   1.000 41.241  0 510 VAL AAA CG2 1 ? 3  
ATOM   1438  N N   . VAL A  1 182 ? 21.742  -11.527  -2.508  1.000 36.204  0 511 VAL AAA N   1 ? 3  
ATOM   1439  C CA  . VAL A  1 182 ? 22.112  -12.479  -3.587  1.000 34.521  0 511 VAL AAA CA  1 ? 3  
ATOM   1440  C C   . VAL A  1 182 ? 22.987  -13.546  -2.946  1.000 35.051  0 511 VAL AAA C   1 ? 3  
ATOM   1441  O O   . VAL A  1 182 ? 23.940  -13.193  -2.234  1.000 35.265  0 511 VAL AAA O   1 ? 3  
ATOM   1442  C CB  . VAL A  1 182 ? 22.830  -11.780  -4.746  1.000 35.927  0 511 VAL AAA CB  1 ? 3  
ATOM   1443  C CG1 . VAL A  1 182 ? 23.369  -12.790  -5.746  1.000 35.857  0 511 VAL AAA CG1 1 ? 3  
ATOM   1444  C CG2 . VAL A  1 182 ? 21.926  -10.756  -5.418  1.000 36.759  0 511 VAL AAA CG2 1 ? 3  
ATOM   1445  N N   . VAL A  1 183 ? 22.591  -14.797  -3.138  1.000 36.471  0 512 VAL AAA N   1 ? 3  
ATOM   1446  C CA  . VAL A  1 183 ? 23.348  -16.011  -2.738  1.000 36.592  0 512 VAL AAA CA  1 ? 3  
ATOM   1447  C C   . VAL A  1 183 ? 23.840  -16.652  -4.035  1.000 37.579  0 512 VAL AAA C   1 ? 3  
ATOM   1448  O O   . VAL A  1 183 ? 22.998  -17.006  -4.881  1.000 36.288  0 512 VAL AAA O   1 ? 3  
ATOM   1449  C CB  . VAL A  1 183 ? 22.499  -16.994  -1.916  1.000 36.712  0 512 VAL AAA CB  1 ? 3  
ATOM   1450  C CG1 . VAL A  1 183 ? 23.327  -18.190  -1.474  1.000 35.336  0 512 VAL AAA CG1 1 ? 3  
ATOM   1451  C CG2 . VAL A  1 183 ? 21.842  -16.301  -0.737  1.000 37.172  0 512 VAL AAA CG2 1 ? 3  
ATOM   1452  N N   . LEU A  1 184 ? 25.157  -16.735  -4.198  1.000 38.165  0 513 LEU AAA N   1 ? 3  
ATOM   1453  C CA  . LEU A  1 184 ? 25.787  -17.454  -5.315  1.000 39.062  0 513 LEU AAA CA  1 ? 3  
ATOM   1454  C C   . LEU A  1 184 ? 26.186  -18.831  -4.793  1.000 39.513  0 513 LEU AAA C   1 ? 3  
ATOM   1455  O O   . LEU A  1 184 ? 27.004  -18.893  -3.862  1.000 40.915  0 513 LEU AAA O   1 ? 3  
ATOM   1456  C CB  . LEU A  1 184 ? 26.985  -16.639  -5.797  1.000 39.785  0 513 LEU AAA CB  1 ? 3  
ATOM   1457  C CG  . LEU A  1 184 ? 26.694  -15.248  -6.327  1.000 39.828  0 513 LEU AAA CG  1 ? 3  
ATOM   1458  C CD1 . LEU A  1 184 ? 27.998  -14.557  -6.674  1.000 40.815  0 513 LEU AAA CD1 1 ? 3  
ATOM   1459  C CD2 . LEU A  1 184 ? 25.799  -15.306  -7.553  1.000 42.866  0 513 LEU AAA CD2 1 ? 3  
ATOM   1460  N N   . SER A  1 185 ? 25.539  -19.867  -5.312  1.000 41.150  0 514 SER AAA N   1 ? 3  
ATOM   1461  C CA  . SER A  1 185 ? 25.821  -21.296  -5.048  1.000 43.152  0 514 SER AAA CA  1 ? 3  
ATOM   1462  C C   . SER A  1 185 ? 26.791  -21.803  -6.105  1.000 45.277  0 514 SER AAA C   1 ? 3  
ATOM   1463  O O   . SER A  1 185 ? 26.490  -21.617  -7.288  1.000 46.892  0 514 SER AAA O   1 ? 3  
ATOM   1464  C CB  . SER A  1 185 ? 24.560  -22.087  -5.119  1.000 44.952  0 514 SER AAA CB  1 ? 3  
ATOM   1465  O OG  . SER A  1 185 ? 23.988  -22.008  -3.853  1.000 56.448  0 514 SER AAA OG  1 ? 3  
ATOM   1466  N N   . PHE A  1 186 ? 27.889  -22.411  -5.684  1.000 43.797  0 515 PHE AAA N   1 ? 3  
ATOM   1467  C CA  . PHE A  1 186 ? 28.909  -22.986  -6.573  1.000 43.818  0 515 PHE AAA CA  1 ? 3  
ATOM   1468  C C   . PHE A  1 186 ? 28.812  -24.489  -6.382  1.000 45.974  0 515 PHE AAA C   1 ? 3  
ATOM   1469  O O   . PHE A  1 186 ? 28.919  -24.989  -5.280  1.000 48.783  0 515 PHE AAA O   1 ? 3  
ATOM   1470  C CB  . PHE A  1 186 ? 30.302  -22.477  -6.221  1.000 43.847  0 515 PHE AAA CB  1 ? 3  
ATOM   1471  C CG  . PHE A  1 186 ? 30.478  -20.986  -6.219  1.000 42.216  0 515 PHE AAA CG  1 ? 3  
ATOM   1472  C CD1 . PHE A  1 186 ? 29.764  -20.161  -7.069  1.000 40.755  0 515 PHE AAA CD1 1 ? 3  
ATOM   1473  C CD2 . PHE A  1 186 ? 31.390  -20.413  -5.358  1.000 44.181  0 515 PHE AAA CD2 1 ? 3  
ATOM   1474  C CE1 . PHE A  1 186 ? 29.961  -18.789  -7.047  1.000 39.542  0 515 PHE AAA CE1 1 ? 3  
ATOM   1475  C CE2 . PHE A  1 186 ? 31.586  -19.043  -5.327  1.000 43.204  0 515 PHE AAA CE2 1 ? 3  
ATOM   1476  C CZ  . PHE A  1 186 ? 30.855  -18.232  -6.160  1.000 39.582  0 515 PHE AAA CZ  1 ? 3  
ATOM   1477  N N   . GLU A  1 187 ? 28.591  -25.193  -7.483  1.000 49.192  0 516 GLU AAA N   1 ? 3  
ATOM   1478  C CA  . GLU A  1 187 ? 28.603  -26.667  -7.554  1.000 46.567  0 516 GLU AAA CA  1 ? 3  
ATOM   1479  C C   . GLU A  1 187 ? 29.945  -27.090  -8.172  1.000 46.580  0 516 GLU AAA C   1 ? 3  
ATOM   1480  O O   . GLU A  1 187 ? 30.374  -26.506  -9.194  1.000 45.315  0 516 GLU AAA O   1 ? 3  
ATOM   1481  C CB  . GLU A  1 187 ? 27.435  -27.143  -8.404  1.000 49.498  0 516 GLU AAA CB  1 ? 3  
ATOM   1482  C CG  . GLU A  1 187 ? 26.153  -27.390  -7.651  1.000 51.492  0 516 GLU AAA CG  1 ? 3  
ATOM   1483  C CD  . GLU A  1 187 ? 24.943  -27.681  -8.537  1.000 56.578  0 516 GLU AAA CD  1 ? 3  
ATOM   1484  O OE1 . GLU A  1 187 ? 25.104  -28.277  -9.652  1.000 58.955  0 516 GLU AAA OE1 1 ? 3  
ATOM   1485  O OE2 . GLU A  1 187 ? 23.830  -27.233  -8.163  1.000 61.812  0 516 GLU AAA OE2 1 ? 3  
ATOM   1486  N N   . LEU A  1 188 ? 30.546  -28.134  -7.616  1.000 45.195  0 517 LEU AAA N   1 ? 3  
ATOM   1487  C CA  . LEU A  1 188 ? 31.695  -28.851  -8.213  1.000 43.951  0 517 LEU AAA CA  1 ? 3  
ATOM   1488  C C   . LEU A  1 188 ? 31.323  -30.335  -8.359  1.000 43.653  0 517 LEU AAA C   1 ? 3  
ATOM   1489  O O   . LEU A  1 188 ? 31.879  -31.196  -7.587  1.000 44.177  0 517 LEU AAA O   1 ? 3  
ATOM   1490  C CB  . LEU A  1 188 ? 32.888  -28.659  -7.272  1.000 43.695  0 517 LEU AAA CB  1 ? 3  
ATOM   1491  C CG  . LEU A  1 188 ? 33.579  -27.297  -7.359  1.000 44.133  0 517 LEU AAA CG  1 ? 3  
ATOM   1492  C CD1 . LEU A  1 188 ? 34.557  -27.086  -6.213  1.000 42.322  0 517 LEU AAA CD1 1 ? 3  
ATOM   1493  C CD2 . LEU A  1 188 ? 34.288  -27.149  -8.696  1.000 45.956  0 517 LEU AAA CD2 1 ? 3  
ATOM   1494  N N   . LEU A  1 189 ? 30.498  -30.686  -9.340  1.000 41.817  0 518 LEU AAA N   1 ? 3  
ATOM   1495  C CA  . LEU A  1 189 ? 30.077  -32.078  -9.570  1.000 44.233  0 518 LEU AAA CA  1 ? 3  
ATOM   1496  C C   . LEU A  1 189 ? 30.992  -32.760  -10.579 1.000 46.302  0 518 LEU AAA C   1 ? 3  
ATOM   1497  O O   . LEU A  1 189 ? 31.927  -32.130  -11.040 1.000 45.159  0 518 LEU AAA O   1 ? 3  
ATOM   1498  C CB  . LEU A  1 189 ? 28.633  -32.096  -10.062 1.000 44.414  0 518 LEU AAA CB  1 ? 3  
ATOM   1499  C CG  . LEU A  1 189 ? 27.630  -31.376  -9.167  1.000 42.858  0 518 LEU AAA CG  1 ? 3  
ATOM   1500  C CD1 . LEU A  1 189 ? 26.216  -31.599  -9.731  1.000 43.361  0 518 LEU AAA CD1 1 ? 3  
ATOM   1501  C CD2 . LEU A  1 189 ? 27.692  -31.906  -7.730  1.000 42.635  0 518 LEU AAA CD2 1 ? 3  
ATOM   1502  N N   . HIS A  1 190 ? 30.724  -34.039  -10.849 1.000 48.036  0 519 HIS AAA N   1 ? 3  
ATOM   1503  C CA  . HIS A  1 190 ? 31.469  -34.850  -11.828 1.000 50.730  0 519 HIS AAA CA  1 ? 3  
ATOM   1504  C C   . HIS A  1 190 ? 30.853  -34.597  -13.187 1.000 51.712  0 519 HIS AAA C   1 ? 3  
ATOM   1505  O O   . HIS A  1 190 ? 30.128  -35.485  -13.677 1.000 54.223  0 519 HIS AAA O   1 ? 3  
ATOM   1506  C CB  . HIS A  1 190 ? 31.488  -36.283  -11.313 1.000 53.328  0 519 HIS AAA CB  1 ? 3  
ATOM   1507  C CG  . HIS A  1 190 ? 32.062  -36.252  -9.910  1.000 53.056  0 519 HIS AAA CG  1 ? 3  
ATOM   1508  N ND1 . HIS A  1 190 ? 33.347  -35.819  -9.640  1.000 53.629  0 519 HIS AAA ND1 1 ? 3  
ATOM   1509  C CD2 . HIS A  1 190 ? 31.530  -36.585  -8.675  1.000 53.185  0 519 HIS AAA CD2 1 ? 3  
ATOM   1510  C CE1 . HIS A  1 190 ? 33.583  -36.001  -8.338  1.000 54.020  0 519 HIS AAA CE1 1 ? 3  
ATOM   1511  N NE2 . HIS A  1 190 ? 32.482  -36.466  -7.729  1.000 53.205  0 519 HIS AAA NE2 1 ? 3  
ATOM   1512  N N   . ALA A  1 191 ? 31.140  -33.419  -13.733 1.000 51.456  0 520 ALA AAA N   1 ? 3  
ATOM   1513  C CA  . ALA A  1 191 ? 30.534  -32.838  -14.954 1.000 52.836  0 520 ALA AAA CA  1 ? 3  
ATOM   1514  C C   . ALA A  1 191 ? 31.496  -31.785  -15.511 1.000 53.195  0 520 ALA AAA C   1 ? 3  
ATOM   1515  O O   . ALA A  1 191 ? 32.358  -31.290  -14.797 1.000 51.180  0 520 ALA AAA O   1 ? 3  
ATOM   1516  C CB  . ALA A  1 191 ? 29.183  -32.220  -14.624 1.000 51.201  0 520 ALA AAA CB  1 ? 3  
ATOM   1517  N N   . PRO A  1 192 ? 31.398  -31.398  -16.793 1.000 53.830  0 521 PRO AAA N   1 ? 3  
ATOM   1518  C CA  . PRO A  1 192 ? 32.168  -30.262  -17.290 1.000 54.605  0 521 PRO AAA CA  1 ? 3  
ATOM   1519  C C   . PRO A  1 192 ? 31.907  -28.983  -16.477 1.000 51.844  0 521 PRO AAA C   1 ? 3  
ATOM   1520  O O   . PRO A  1 192 ? 30.787  -28.734  -16.082 1.000 49.906  0 521 PRO AAA O   1 ? 3  
ATOM   1521  C CB  . PRO A  1 192 ? 31.688  -30.121  -18.752 1.000 56.343  0 521 PRO AAA CB  1 ? 3  
ATOM   1522  C CG  . PRO A  1 192 ? 31.300  -31.547  -19.114 1.000 59.388  0 521 PRO AAA CG  1 ? 3  
ATOM   1523  C CD  . PRO A  1 192 ? 30.623  -32.059  -17.848 1.000 57.657  0 521 PRO AAA CD  1 ? 3  
ATOM   1524  N N   . ALA A  1 193 ? 32.954  -28.201  -16.257 1.000 50.480  0 522 ALA AAA N   1 ? 3  
ATOM   1525  C CA  . ALA A  1 193 ? 32.844  -26.807  -15.779 1.000 50.697  0 522 ALA AAA CA  1 ? 3  
ATOM   1526  C C   . ALA A  1 193 ? 32.115  -25.979  -16.830 1.000 49.946  0 522 ALA AAA C   1 ? 3  
ATOM   1527  O O   . ALA A  1 193 ? 32.409  -26.141  -17.976 1.000 51.336  0 522 ALA AAA O   1 ? 3  
ATOM   1528  C CB  . ALA A  1 193 ? 34.188  -26.217  -15.449 1.000 50.747  0 522 ALA AAA CB  1 ? 3  
ATOM   1529  N N   . THR A  1 194 ? 31.166  -25.154  -16.436 1.000 49.494  0 523 THR AAA N   1 ? 3  
ATOM   1530  C CA  . THR A  1 194 ? 30.422  -24.270  -17.371 1.000 50.754  0 523 THR AAA CA  1 ? 3  
ATOM   1531  C C   . THR A  1 194 ? 30.692  -22.809  -16.983 1.000 48.101  0 523 THR AAA C   1 ? 3  
ATOM   1532  O O   . THR A  1 194 ? 30.438  -21.949  -17.805 1.000 47.929  0 523 THR AAA O   1 ? 3  
ATOM   1533  C CB  . THR A  1 194 ? 28.931  -24.648  -17.386 1.000 52.275  0 523 THR AAA CB  1 ? 3  
ATOM   1534  O OG1 . THR A  1 194 ? 28.318  -24.254  -16.160 1.000 49.334  0 523 THR AAA OG1 1 ? 3  
ATOM   1535  C CG2 . THR A  1 194 ? 28.692  -26.134  -17.569 1.000 52.767  0 523 THR AAA CG2 1 ? 3  
ATOM   1536  N N   . VAL A  1 195 ? 31.195  -22.522  -15.787 1.000 46.642  0 524 VAL AAA N   1 ? 3  
ATOM   1537  C CA  . VAL A  1 195 ? 31.491  -21.136  -15.343 1.000 46.496  0 524 VAL AAA CA  1 ? 3  
ATOM   1538  C C   . VAL A  1 195 ? 32.945  -21.065  -14.904 1.000 46.912  0 524 VAL AAA C   1 ? 3  
ATOM   1539  O O   . VAL A  1 195 ? 33.267  -21.784  -13.958 1.000 46.875  0 524 VAL AAA O   1 ? 3  
ATOM   1540  C CB  . VAL A  1 195 ? 30.570  -20.716  -14.172 1.000 47.229  0 524 VAL AAA CB  1 ? 3  
ATOM   1541  C CG1 . VAL A  1 195 ? 30.939  -19.335  -13.609 1.000 45.105  0 524 VAL AAA CG1 1 ? 3  
ATOM   1542  C CG2 . VAL A  1 195 ? 29.114  -20.739  -14.586 1.000 47.543  0 524 VAL AAA CG2 1 ? 3  
ATOM   1543  N N   . CYS A  1 196 ? 33.758  -20.177  -15.499 1.000 49.122  0 525 CYS AAA N   1 ? 3  
ATOM   1544  C CA  . CYS A  1 196 ? 35.146  -19.876  -15.046 1.000 49.837  0 525 CYS AAA CA  1 ? 3  
ATOM   1545  C C   . CYS A  1 196 ? 35.338  -18.368  -14.873 1.000 49.371  0 525 CYS AAA C   1 ? 3  
ATOM   1546  O O   . CYS A  1 196 ? 34.624  -17.607  -15.513 1.000 46.931  0 525 CYS AAA O   1 ? 3  
ATOM   1547  C CB  . CYS A  1 196 ? 36.169  -20.412  -16.038 1.000 52.449  0 525 CYS AAA CB  1 ? 3  
ATOM   1548  S SG  . CYS A  1 196 ? 36.243  -22.220  -16.078 1.000 57.908  0 525 CYS AAA SG  1 ? 3  
ATOM   1549  N N   . GLY A  1 197 ? 36.262  -17.959  -14.001 1.000 49.108  0 526 GLY AAA N   1 ? 3  
ATOM   1550  C CA  . GLY A  1 197 ? 36.735  -16.566  -13.918 1.000 50.247  0 526 GLY AAA CA  1 ? 3  
ATOM   1551  C C   . GLY A  1 197 ? 37.597  -16.212  -15.121 1.000 51.899  0 526 GLY AAA C   1 ? 3  
ATOM   1552  O O   . GLY A  1 197 ? 37.958  -17.080  -15.897 1.000 53.902  0 526 GLY AAA O   1 ? 3  
ATOM   1553  N N   . PRO A  1 198 ? 37.938  -14.927  -15.315 1.000 56.423  0 527 PRO AAA N   1 ? 3  
ATOM   1554  C CA  . PRO A  1 198 ? 38.800  -14.496  -16.422 1.000 63.436  0 527 PRO AAA CA  1 ? 3  
ATOM   1555  C C   . PRO A  1 198 ? 40.177  -15.173  -16.514 1.000 72.322  0 527 PRO AAA C   1 ? 3  
ATOM   1556  O O   . PRO A  1 198 ? 40.691  -15.264  -17.620 1.000 78.759  0 527 PRO AAA O   1 ? 3  
ATOM   1557  C CB  . PRO A  1 198 ? 39.045  -13.017  -16.134 1.000 60.316  0 527 PRO AAA CB  1 ? 3  
ATOM   1558  C CG  . PRO A  1 198 ? 37.843  -12.599  -15.364 1.000 57.078  0 527 PRO AAA CG  1 ? 3  
ATOM   1559  C CD  . PRO A  1 198 ? 37.441  -13.797  -14.537 1.000 55.138  0 527 PRO AAA CD  1 ? 3  
ATOM   1560  N N   . LYS A  1 199 ? 40.770  -15.549  -15.373 1.000 61.991  0 528 LYS AAA N   1 ? ?  
ATOM   1561  C CA  . LYS A  1 199 ? 42.195  -15.983  -15.254 1.000 69.968  0 528 LYS AAA CA  1 ? ?  
ATOM   1562  C C   . LYS A  1 199 ? 42.296  -17.512  -15.223 1.000 66.515  0 528 LYS AAA C   1 ? ?  
ATOM   1563  O O   . LYS A  1 199 ? 41.323  -18.254  -15.085 1.000 67.781  0 528 LYS AAA O   1 ? ?  
ATOM   1564  C CB  . LYS A  1 199 ? 42.820  -15.371  -13.997 1.000 76.282  0 528 LYS AAA CB  1 ? ?  
ATOM   1565  C CG  . LYS A  1 199 ? 42.476  -13.906  -13.750 1.000 84.337  0 528 LYS AAA CG  1 ? ?  
ATOM   1566  C CD  . LYS A  1 199 ? 43.519  -13.145  -12.953 1.000 90.862  0 528 LYS AAA CD  1 ? ?  
ATOM   1567  C CE  . LYS A  1 199 ? 43.852  -13.814  -11.638 1.000 91.903  0 528 LYS AAA CE  1 ? ?  
ATOM   1568  N NZ  . LYS A  1 199 ? 44.707  -12.960  -10.784 1.000 95.745  0 528 LYS AAA NZ  1 ? ?  
ATOM   1569  N N   . GLN B  2 1   ? 26.327  -21.079  19.169  1.000 56.404  0 1   GLN BBB N   1 ? 4  
ATOM   1570  C CA  . GLN B  2 1   ? 27.224  -20.288  19.992  1.000 57.241  0 1   GLN BBB CA  1 ? 4  
ATOM   1571  C C   . GLN B  2 1   ? 28.626  -20.918  20.014  1.000 52.896  0 1   GLN BBB C   1 ? 4  
ATOM   1572  O O   . GLN B  2 1   ? 28.760  -22.063  20.413  1.000 57.733  0 1   GLN BBB O   1 ? 4  
ATOM   1573  C CB  . GLN B  2 1   ? 26.623  -20.133  21.398  1.000 67.254  0 1   GLN BBB CB  1 ? 4  
ATOM   1574  C CG  . GLN B  2 1   ? 27.479  -19.307  22.385  1.000 75.592  0 1   GLN BBB CG  1 ? 4  
ATOM   1575  C CD  . GLN B  2 1   ? 27.730  -17.836  22.074  1.000 81.439  0 1   GLN BBB CD  1 ? 4  
ATOM   1576  O OE1 . GLN B  2 1   ? 27.213  -17.252  21.112  1.000 81.973  0 1   GLN BBB OE1 1 ? 4  
ATOM   1577  N NE2 . GLN B  2 1   ? 28.519  -17.184  22.928  1.000 81.295  0 1   GLN BBB NE2 1 ? 4  
ATOM   1578  N N   . VAL B  2 2   ? 29.649  -20.164  19.628  1.000 47.704  0 2   VAL BBB N   1 ? 4  
ATOM   1579  C CA  . VAL B  2 2   ? 31.082  -20.462  19.893  1.000 44.168  0 2   VAL BBB CA  1 ? 4  
ATOM   1580  C C   . VAL B  2 2   ? 31.594  -19.495  20.970  1.000 44.567  0 2   VAL BBB C   1 ? 4  
ATOM   1581  O O   . VAL B  2 2   ? 31.387  -18.289  20.838  1.000 44.032  0 2   VAL BBB O   1 ? 4  
ATOM   1582  C CB  . VAL B  2 2   ? 31.909  -20.291  18.608  1.000 43.774  0 2   VAL BBB CB  1 ? 4  
ATOM   1583  C CG1 . VAL B  2 2   ? 33.414  -20.481  18.874  1.000 41.252  0 2   VAL BBB CG1 1 ? 4  
ATOM   1584  C CG2 . VAL B  2 2   ? 31.388  -21.195  17.466  1.000 44.439  0 2   VAL BBB CG2 1 ? 4  
ATOM   1585  N N   . GLN B  2 3   ? 32.295  -19.992  21.982  1.000 41.333  0 3   GLN BBB N   1 ? 4  
ATOM   1586  C CA  . GLN B  2 3   ? 32.995  -19.113  22.941  1.000 40.307  0 3   GLN BBB CA  1 ? 4  
ATOM   1587  C C   . GLN B  2 3   ? 34.483  -19.102  22.581  1.000 41.491  0 3   GLN BBB C   1 ? 4  
ATOM   1588  O O   . GLN B  2 3   ? 34.999  -20.080  22.018  1.000 36.112  0 3   GLN BBB O   1 ? 4  
ATOM   1589  C CB  . GLN B  2 3   ? 32.706  -19.520  24.381  1.000 41.364  0 3   GLN BBB CB  1 ? 4  
ATOM   1590  C CG  . GLN B  2 3   ? 31.274  -19.225  24.789  1.000 41.022  0 3   GLN BBB CG  1 ? 4  
ATOM   1591  C CD  . GLN B  2 3   ? 31.066  -19.430  26.261  1.000 41.430  0 3   GLN BBB CD  1 ? 4  
ATOM   1592  O OE1 . GLN B  2 3   ? 31.700  -18.782  27.093  1.000 40.900  0 3   GLN BBB OE1 1 ? 4  
ATOM   1593  N NE2 . GLN B  2 3   ? 30.158  -20.331  26.586  1.000 42.393  0 3   GLN BBB NE2 1 ? 4  
ATOM   1594  N N   . LEU B  2 4   ? 35.137  -17.986  22.889  1.000 43.543  0 4   LEU BBB N   1 ? 4  
ATOM   1595  C CA  . LEU B  2 4   ? 36.531  -17.661  22.549  1.000 42.382  0 4   LEU BBB CA  1 ? 4  
ATOM   1596  C C   . LEU B  2 4   ? 37.174  -17.067  23.798  1.000 44.242  0 4   LEU BBB C   1 ? 4  
ATOM   1597  O O   . LEU B  2 4   ? 36.599  -16.121  24.396  1.000 43.799  0 4   LEU BBB O   1 ? 4  
ATOM   1598  C CB  . LEU B  2 4   ? 36.534  -16.645  21.396  1.000 43.772  0 4   LEU BBB CB  1 ? 4  
ATOM   1599  C CG  . LEU B  2 4   ? 35.826  -17.042  20.100  1.000 42.890  0 4   LEU BBB CG  1 ? 4  
ATOM   1600  C CD1 . LEU B  2 4   ? 35.707  -15.848  19.146  1.000 42.095  0 4   LEU BBB CD1 1 ? 4  
ATOM   1601  C CD2 . LEU B  2 4   ? 36.543  -18.209  19.427  1.000 41.213  0 4   LEU BBB CD2 1 ? 4  
ATOM   1602  N N   . VAL B  2 5   ? 38.355  -17.556  24.163  1.000 47.765  0 5   VAL BBB N   1 ? 4  
ATOM   1603  C CA  . VAL B  2 5   ? 39.138  -17.014  25.308  1.000 47.804  0 5   VAL BBB CA  1 ? 4  
ATOM   1604  C C   . VAL B  2 5   ? 40.573  -16.748  24.842  1.000 48.073  0 5   VAL BBB C   1 ? 4  
ATOM   1605  O O   . VAL B  2 5   ? 41.279  -17.711  24.441  1.000 47.592  0 5   VAL BBB O   1 ? 4  
ATOM   1606  C CB  . VAL B  2 5   ? 39.074  -17.969  26.509  1.000 48.878  0 5   VAL BBB CB  1 ? 4  
ATOM   1607  C CG1 . VAL B  2 5   ? 40.048  -17.556  27.609  1.000 51.958  0 5   VAL BBB CG1 1 ? 4  
ATOM   1608  C CG2 . VAL B  2 5   ? 37.654  -18.059  27.051  1.000 49.657  0 5   VAL BBB CG2 1 ? 4  
ATOM   1609  N N   . GLU B  2 6   ? 40.973  -15.479  24.917  1.000 48.394  0 6   GLU BBB N   1 ? 4  
ATOM   1610  C CA  . GLU B  2 6   ? 42.354  -14.994  24.664  1.000 48.624  0 6   GLU BBB CA  1 ? 4  
ATOM   1611  C C   . GLU B  2 6   ? 43.215  -15.266  25.902  1.000 50.860  0 6   GLU BBB C   1 ? 4  
ATOM   1612  O O   . GLU B  2 6   ? 42.670  -15.221  27.024  1.000 49.509  0 6   GLU BBB O   1 ? 4  
ATOM   1613  C CB  . GLU B  2 6   ? 42.352  -13.485  24.388  1.000 48.607  0 6   GLU BBB CB  1 ? 4  
ATOM   1614  C CG  . GLU B  2 6   ? 41.404  -13.061  23.275  1.000 46.297  0 6   GLU BBB CG  1 ? 4  
ATOM   1615  C CD  . GLU B  2 6   ? 39.990  -12.678  23.700  1.000 44.565  0 6   GLU BBB CD  1 ? 4  
ATOM   1616  O OE1 . GLU B  2 6   ? 39.583  -13.063  24.788  1.000 46.361  0 6   GLU BBB OE1 1 ? 4  
ATOM   1617  O OE2 . GLU B  2 6   ? 39.294  -11.995  22.910  1.000 43.474  0 6   GLU BBB OE2 1 ? 4  
ATOM   1618  N N   . SER B  2 7   ? 44.508  -15.521  25.690  1.000 53.520  0 7   SER BBB N   1 ? 4  
ATOM   1619  C CA  . SER B  2 7   ? 45.561  -15.572  26.738  1.000 54.327  0 7   SER BBB CA  1 ? 4  
ATOM   1620  C C   . SER B  2 7   ? 46.903  -15.126  26.132  1.000 57.408  0 7   SER BBB C   1 ? 4  
ATOM   1621  O O   . SER B  2 7   ? 46.983  -14.952  24.892  1.000 58.665  0 7   SER BBB O   1 ? 4  
ATOM   1622  C CB  . SER B  2 7   ? 45.659  -16.950  27.308  1.000 53.379  0 7   SER BBB CB  1 ? 4  
ATOM   1623  O OG  . SER B  2 7   ? 45.988  -17.876  26.287  1.000 50.957  0 7   SER BBB OG  1 ? 4  
ATOM   1624  N N   . GLY B  2 8   ? 47.899  -14.886  26.978  1.000 59.511  0 8   GLY BBB N   1 ? 4  
ATOM   1625  C CA  . GLY B  2 8   ? 49.264  -14.522  26.552  1.000 62.422  0 8   GLY BBB CA  1 ? 4  
ATOM   1626  C C   . GLY B  2 8   ? 49.503  -13.025  26.510  1.000 63.618  0 8   GLY BBB C   1 ? 4  
ATOM   1627  O O   . GLY B  2 8   ? 50.600  -12.629  26.103  1.000 67.044  0 8   GLY BBB O   1 ? 4  
ATOM   1628  N N   . GLY B  2 9   ? 48.528  -12.209  26.909  1.000 64.574  0 9   GLY BBB N   1 ? 4  
ATOM   1629  C CA  . GLY B  2 9   ? 48.686  -10.736  26.954  1.000 64.029  0 9   GLY BBB CA  1 ? 4  
ATOM   1630  C C   . GLY B  2 9   ? 49.498  -10.304  28.166  1.000 67.110  0 9   GLY BBB C   1 ? 4  
ATOM   1631  O O   . GLY B  2 9   ? 50.019  -11.176  28.870  1.000 69.018  0 9   GLY BBB O   1 ? 4  
ATOM   1632  N N   . GLY B  2 10  ? 49.595  -8.998   28.418  1.000 66.592  0 10  GLY BBB N   1 ? 4  
ATOM   1633  C CA  . GLY B  2 10  ? 50.285  -8.445   29.594  1.000 69.251  0 10  GLY BBB CA  1 ? 4  
ATOM   1634  C C   . GLY B  2 10  ? 51.278  -7.361   29.227  1.000 71.624  0 10  GLY BBB C   1 ? 4  
ATOM   1635  O O   . GLY B  2 10  ? 51.179  -6.823   28.103  1.000 69.705  0 10  GLY BBB O   1 ? 4  
ATOM   1636  N N   . LEU B  2 11  ? 52.212  -7.077   30.138  1.000 74.821  0 11  LEU BBB N   1 ? 4  
ATOM   1637  C CA  . LEU B  2 11  ? 53.218  -5.993   30.018  1.000 78.623  0 11  LEU BBB CA  1 ? 4  
ATOM   1638  C C   . LEU B  2 11  ? 54.413  -6.529   29.220  1.000 79.233  0 11  LEU BBB C   1 ? 4  
ATOM   1639  O O   . LEU B  2 11  ? 54.781  -7.684   29.433  1.000 79.487  0 11  LEU BBB O   1 ? 4  
ATOM   1640  C CB  . LEU B  2 11  ? 53.606  -5.562   31.438  1.000 83.353  0 11  LEU BBB CB  1 ? 4  
ATOM   1641  C CG  . LEU B  2 11  ? 54.643  -4.439   31.551  1.000 88.312  0 11  LEU BBB CG  1 ? 4  
ATOM   1642  C CD1 . LEU B  2 11  ? 54.207  -3.224   30.744  1.000 87.936  0 11  LEU BBB CD1 1 ? 4  
ATOM   1643  C CD2 . LEU B  2 11  ? 54.919  -4.065   33.001  1.000 92.015  0 11  LEU BBB CD2 1 ? 4  
ATOM   1644  N N   . VAL B  2 12  ? 54.987  -5.737   28.319  1.000 80.499  0 12  VAL BBB N   1 ? 4  
ATOM   1645  C CA  . VAL B  2 12  ? 56.223  -6.113   27.574  1.000 82.289  0 12  VAL BBB CA  1 ? 4  
ATOM   1646  C C   . VAL B  2 12  ? 56.944  -4.819   27.177  1.000 86.432  0 12  VAL BBB C   1 ? 4  
ATOM   1647  O O   . VAL B  2 12  ? 56.259  -3.801   26.985  1.000 84.880  0 12  VAL BBB O   1 ? 4  
ATOM   1648  C CB  . VAL B  2 12  ? 55.888  -7.009   26.362  1.000 79.043  0 12  VAL BBB CB  1 ? 4  
ATOM   1649  C CG1 . VAL B  2 12  ? 55.162  -6.241   25.275  1.000 76.585  0 12  VAL BBB CG1 1 ? 4  
ATOM   1650  C CG2 . VAL B  2 12  ? 57.112  -7.695   25.769  1.000 80.054  0 12  VAL BBB CG2 1 ? 4  
ATOM   1651  N N   . GLN B  2 13  ? 58.282  -4.844   27.139  1.000 92.088  0 13  GLN BBB N   1 ? 4  
ATOM   1652  C CA  . GLN B  2 13  ? 59.132  -3.679   26.773  1.000 94.282  0 13  GLN BBB CA  1 ? 4  
ATOM   1653  C C   . GLN B  2 13  ? 59.122  -3.535   25.238  1.000 92.461  0 13  GLN BBB C   1 ? 4  
ATOM   1654  O O   . GLN B  2 13  ? 59.037  -4.562   24.524  1.000 91.564  0 13  GLN BBB O   1 ? 4  
ATOM   1655  C CB  . GLN B  2 13  ? 60.547  -3.864   27.332  1.000 98.836  0 13  GLN BBB CB  1 ? 4  
ATOM   1656  C CG  . GLN B  2 13  ? 60.805  -3.195   28.678  1.000 103.791 0 13  GLN BBB CG  1 ? 4  
ATOM   1657  C CD  . GLN B  2 13  ? 62.170  -2.536   28.756  1.000 109.601 0 13  GLN BBB CD  1 ? 4  
ATOM   1658  O OE1 . GLN B  2 13  ? 62.480  -1.582   28.032  1.000 111.055 0 13  GLN BBB OE1 1 ? 4  
ATOM   1659  N NE2 . GLN B  2 13  ? 62.998  -3.018   29.669  1.000 113.143 0 13  GLN BBB NE2 1 ? 4  
ATOM   1660  N N   . ALA B  2 14  ? 59.145  -2.289   24.759  1.000 92.652  0 14  ALA BBB N   1 ? 4  
ATOM   1661  C CA  . ALA B  2 14  ? 59.295  -1.916   23.331  1.000 91.023  0 14  ALA BBB CA  1 ? 4  
ATOM   1662  C C   . ALA B  2 14  ? 60.435  -2.741   22.716  1.000 91.703  0 14  ALA BBB C   1 ? 4  
ATOM   1663  O O   . ALA B  2 14  ? 61.430  -2.980   23.404  1.000 91.561  0 14  ALA BBB O   1 ? 4  
ATOM   1664  C CB  . ALA B  2 14  ? 59.551  -0.437   23.194  1.000 93.250  0 14  ALA BBB CB  1 ? 4  
ATOM   1665  N N   . GLY B  2 15  ? 60.254  -3.203   21.476  1.000 90.114  0 15  GLY BBB N   1 ? 4  
ATOM   1666  C CA  . GLY B  2 15  ? 61.181  -4.127   20.799  1.000 91.822  0 15  GLY BBB CA  1 ? 4  
ATOM   1667  C C   . GLY B  2 15  ? 60.981  -5.573   21.235  1.000 90.969  0 15  GLY BBB C   1 ? 4  
ATOM   1668  O O   . GLY B  2 15  ? 61.574  -6.440   20.596  1.000 93.697  0 15  GLY BBB O   1 ? 4  
ATOM   1669  N N   . GLY B  2 16  ? 60.162  -5.840   22.258  1.000 89.351  0 16  GLY BBB N   1 ? 4  
ATOM   1670  C CA  . GLY B  2 16  ? 59.924  -7.197   22.781  1.000 87.511  0 16  GLY BBB CA  1 ? 4  
ATOM   1671  C C   . GLY B  2 16  ? 58.923  -7.955   21.932  1.000 85.260  0 16  GLY BBB C   1 ? 4  
ATOM   1672  O O   . GLY B  2 16  ? 58.453  -7.404   20.919  1.000 82.200  0 16  GLY BBB O   1 ? 4  
ATOM   1673  N N   . SER B  2 17  ? 58.592  -9.176   22.363  1.000 85.737  0 17  SER BBB N   1 ? 4  
ATOM   1674  C CA  . SER B  2 17  ? 57.666  -10.128  21.700  1.000 80.768  0 17  SER BBB CA  1 ? 4  
ATOM   1675  C C   . SER B  2 17  ? 56.608  -10.633  22.675  1.000 78.661  0 17  SER BBB C   1 ? 4  
ATOM   1676  O O   . SER B  2 17  ? 56.871  -10.698  23.894  1.000 80.217  0 17  SER BBB O   1 ? 4  
ATOM   1677  C CB  . SER B  2 17  ? 58.399  -11.293  21.117  1.000 82.711  0 17  SER BBB CB  1 ? 4  
ATOM   1678  O OG  . SER B  2 17  ? 59.133  -10.879  19.981  1.000 85.802  0 17  SER BBB OG  1 ? 4  
ATOM   1679  N N   . LEU B  2 18  ? 55.464  -11.006  22.107  1.000 74.646  0 18  LEU BBB N   1 ? 4  
ATOM   1680  C CA  . LEU B  2 18  ? 54.326  -11.656  22.788  1.000 72.014  0 18  LEU BBB CA  1 ? 4  
ATOM   1681  C C   . LEU B  2 18  ? 53.662  -12.576  21.779  1.000 68.003  0 18  LEU BBB C   1 ? 4  
ATOM   1682  O O   . LEU B  2 18  ? 53.506  -12.164  20.625  1.000 64.215  0 18  LEU BBB O   1 ? 4  
ATOM   1683  C CB  . LEU B  2 18  ? 53.314  -10.616  23.257  1.000 72.380  0 18  LEU BBB CB  1 ? 4  
ATOM   1684  C CG  . LEU B  2 18  ? 53.483  -10.111  24.689  1.000 76.840  0 18  LEU BBB CG  1 ? 4  
ATOM   1685  C CD1 . LEU B  2 18  ? 52.269  -9.289   25.093  1.000 75.733  0 18  LEU BBB CD1 1 ? 4  
ATOM   1686  C CD2 . LEU B  2 18  ? 53.717  -11.256  25.677  1.000 77.905  0 18  LEU BBB CD2 1 ? 4  
ATOM   1687  N N   . ARG B  2 19  ? 53.263  -13.759  22.234  1.000 67.283  0 19  ARG BBB N   1 ? 4  
ATOM   1688  C CA  . ARG B  2 19  ? 52.355  -14.635  21.473  1.000 63.822  0 19  ARG BBB CA  1 ? 4  
ATOM   1689  C C   . ARG B  2 19  ? 51.004  -14.670  22.183  1.000 62.196  0 19  ARG BBB C   1 ? 4  
ATOM   1690  O O   . ARG B  2 19  ? 50.879  -15.316  23.257  1.000 62.411  0 19  ARG BBB O   1 ? 4  
ATOM   1691  C CB  . ARG B  2 19  ? 52.958  -16.022  21.300  1.000 64.332  0 19  ARG BBB CB  1 ? 4  
ATOM   1692  C CG  . ARG B  2 19  ? 52.320  -16.782  20.155  1.000 65.052  0 19  ARG BBB CG  1 ? 4  
ATOM   1693  C CD  . ARG B  2 19  ? 52.867  -18.194  20.089  1.000 69.379  0 19  ARG BBB CD  1 ? 4  
ATOM   1694  N NE  . ARG B  2 19  ? 52.369  -18.898  21.262  1.000 73.033  0 19  ARG BBB NE  1 ? 4  
ATOM   1695  C CZ  . ARG B  2 19  ? 52.254  -20.212  21.377  1.000 76.570  0 19  ARG BBB CZ  1 ? 4  
ATOM   1696  N NH1 . ARG B  2 19  ? 52.590  -21.005  20.374  1.000 80.482  0 19  ARG BBB NH1 1 ? 4  
ATOM   1697  N NH2 . ARG B  2 19  ? 51.785  -20.723  22.499  1.000 75.236  0 19  ARG BBB NH2 1 ? 4  
ATOM   1698  N N   . LEU B  2 20  ? 50.028  -13.975  21.596  1.000 59.741  0 20  LEU BBB N   1 ? 4  
ATOM   1699  C CA  . LEU B  2 20  ? 48.606  -14.113  21.981  1.000 56.823  0 20  LEU BBB CA  1 ? 4  
ATOM   1700  C C   . LEU B  2 20  ? 48.110  -15.447  21.435  1.000 54.836  0 20  LEU BBB C   1 ? 4  
ATOM   1701  O O   . LEU B  2 20  ? 48.536  -15.869  20.322  1.000 51.213  0 20  LEU BBB O   1 ? 4  
ATOM   1702  C CB  . LEU B  2 20  ? 47.786  -12.951  21.422  1.000 55.460  0 20  LEU BBB CB  1 ? 4  
ATOM   1703  C CG  . LEU B  2 20  ? 48.191  -11.560  21.902  1.000 58.068  0 20  LEU BBB CG  1 ? 4  
ATOM   1704  C CD1 . LEU B  2 20  ? 47.113  -10.568  21.522  1.000 58.041  0 20  LEU BBB CD1 1 ? 4  
ATOM   1705  C CD2 . LEU B  2 20  ? 48.408  -11.521  23.413  1.000 61.612  0 20  LEU BBB CD2 1 ? 4  
ATOM   1706  N N   . ALA B  2 21  ? 47.275  -16.117  22.227  1.000 53.312  0 21  ALA BBB N   1 ? 4  
ATOM   1707  C CA  . ALA B  2 21  ? 46.539  -17.311  21.783  1.000 51.483  0 21  ALA BBB CA  1 ? 4  
ATOM   1708  C C   . ALA B  2 21  ? 45.063  -17.116  22.081  1.000 50.613  0 21  ALA BBB C   1 ? 4  
ATOM   1709  O O   . ALA B  2 21  ? 44.710  -16.378  23.015  1.000 54.088  0 21  ALA BBB O   1 ? 4  
ATOM   1710  C CB  . ALA B  2 21  ? 47.084  -18.551  22.438  1.000 51.070  0 21  ALA BBB CB  1 ? 4  
ATOM   1711  N N   . CYS B  2 22  ? 44.235  -17.764  21.288  1.000 50.041  0 22  CYS BBB N   1 ? 4  
ATOM   1712  C CA  . CYS B  2 22  ? 42.781  -17.756  21.491  1.000 49.889  0 22  CYS BBB CA  1 ? 4  
ATOM   1713  C C   . CYS B  2 22  ? 42.247  -19.152  21.188  1.000 47.824  0 22  CYS BBB C   1 ? 4  
ATOM   1714  O O   . CYS B  2 22  ? 42.485  -19.650  20.063  1.000 47.165  0 22  CYS BBB O   1 ? 4  
ATOM   1715  C CB  . CYS B  2 22  ? 42.139  -16.714  20.602  1.000 48.749  0 22  CYS BBB CB  1 ? 4  
ATOM   1716  S SG  . CYS B  2 22  ? 40.357  -16.926  20.543  1.000 52.076  0 22  CYS BBB SG  1 ? 4  
ATOM   1717  N N   . ILE B  2 23  ? 41.552  -19.735  22.157  1.000 44.118  0 23  ILE BBB N   1 ? 4  
ATOM   1718  C CA  . ILE B  2 23  ? 41.005  -21.112  22.040  1.000 43.617  0 23  ILE BBB CA  1 ? 4  
ATOM   1719  C C   . ILE B  2 23  ? 39.478  -20.994  21.929  1.000 42.802  0 23  ILE BBB C   1 ? 4  
ATOM   1720  O O   . ILE B  2 23  ? 38.885  -20.147  22.615  1.000 39.692  0 23  ILE BBB O   1 ? 4  
ATOM   1721  C CB  . ILE B  2 23  ? 41.489  -21.991  23.202  1.000 44.105  0 23  ILE BBB CB  1 ? 4  
ATOM   1722  C CG1 . ILE B  2 23  ? 41.116  -23.457  22.986  1.000 44.185  0 23  ILE BBB CG1 1 ? 4  
ATOM   1723  C CG2 . ILE B  2 23  ? 41.010  -21.439  24.551  1.000 44.108  0 23  ILE BBB CG2 1 ? 4  
ATOM   1724  C CD1 . ILE B  2 23  ? 41.714  -24.397  24.047  1.000 45.741  0 23  ILE BBB CD1 1 ? 4  
ATOM   1725  N N   . ALA B  2 24  ? 38.894  -21.764  21.015  1.000 43.938  0 24  ALA BBB N   1 ? 4  
ATOM   1726  C CA  . ALA B  2 24  ? 37.443  -21.782  20.703  1.000 43.064  0 24  ALA BBB CA  1 ? 4  
ATOM   1727  C C   . ALA B  2 24  ? 36.828  -23.074  21.268  1.000 41.782  0 24  ALA BBB C   1 ? 4  
ATOM   1728  O O   . ALA B  2 24  ? 37.527  -24.098  21.335  1.000 42.845  0 24  ALA BBB O   1 ? 4  
ATOM   1729  C CB  . ALA B  2 24  ? 37.232  -21.667  19.204  1.000 41.825  0 24  ALA BBB CB  1 ? 4  
ATOM   1730  N N   . SER B  2 25  ? 35.571  -22.998  21.686  1.000 40.588  0 25  SER BBB N   1 ? 4  
ATOM   1731  C CA  . SER B  2 25  ? 34.696  -24.163  21.937  1.000 42.246  0 25  SER BBB CA  1 ? 4  
ATOM   1732  C C   . SER B  2 25  ? 34.368  -24.815  20.592  1.000 40.811  0 25  SER BBB C   1 ? 4  
ATOM   1733  O O   . SER B  2 25  ? 34.726  -24.260  19.550  1.000 38.900  0 25  SER BBB O   1 ? 4  
ATOM   1734  C CB  . SER B  2 25  ? 33.439  -23.727  22.648  1.000 42.464  0 25  SER BBB CB  1 ? 4  
ATOM   1735  O OG  . SER B  2 25  ? 32.641  -22.916  21.795  1.000 39.701  0 25  SER BBB OG  1 ? 4  
ATOM   1736  N N   . GLY B  2 26  ? 33.679  -25.941  20.613  1.000 44.819  0 26  GLY BBB N   1 ? 4  
ATOM   1737  C CA  . GLY B  2 26  ? 33.060  -26.497  19.396  1.000 47.955  0 26  GLY BBB CA  1 ? 4  
ATOM   1738  C C   . GLY B  2 26  ? 33.936  -27.539  18.730  1.000 49.093  0 26  GLY BBB C   1 ? 4  
ATOM   1739  O O   . GLY B  2 26  ? 35.125  -27.645  19.036  1.000 52.504  0 26  GLY BBB O   1 ? 4  
ATOM   1740  N N   . ARG B  2 27  ? 33.327  -28.308  17.849  1.000 52.567  0 27  ARG BBB N   1 ? 4  
ATOM   1741  C CA  . ARG B  2 27  ? 33.967  -29.461  17.172  1.000 56.235  0 27  ARG BBB CA  1 ? 4  
ATOM   1742  C C   . ARG B  2 27  ? 34.150  -29.149  15.682  1.000 51.007  0 27  ARG BBB C   1 ? 4  
ATOM   1743  O O   . ARG B  2 27  ? 34.485  -30.038  14.979  1.000 50.883  0 27  ARG BBB O   1 ? 4  
ATOM   1744  C CB  . ARG B  2 27  ? 33.104  -30.698  17.418  1.000 63.611  0 27  ARG BBB CB  1 ? 4  
ATOM   1745  C CG  . ARG B  2 27  ? 33.420  -31.419  18.719  1.000 73.692  0 27  ARG BBB CG  1 ? 4  
ATOM   1746  C CD  . ARG B  2 27  ? 32.347  -32.412  19.164  1.000 86.097  0 27  ARG BBB CD  1 ? 4  
ATOM   1747  N NE  . ARG B  2 27  ? 31.055  -32.312  18.469  1.000 91.859  0 27  ARG BBB NE  1 ? 4  
ATOM   1748  C CZ  . ARG B  2 27  ? 29.911  -31.809  18.969  1.000 95.681  0 27  ARG BBB CZ  1 ? 4  
ATOM   1749  N NH1 . ARG B  2 27  ? 29.835  -31.300  20.192  1.000 95.151  0 27  ARG BBB NH1 1 ? 4  
ATOM   1750  N NH2 . ARG B  2 27  ? 28.821  -31.807  18.215  1.000 100.692 0 27  ARG BBB NH2 1 ? 4  
ATOM   1751  N N   . THR B  2 28  ? 33.929  -27.910  15.232  1.000 50.067  0 28  THR BBB N   1 ? 4  
ATOM   1752  C CA  . THR B  2 28  ? 34.043  -27.519  13.808  1.000 46.793  0 28  THR BBB CA  1 ? 4  
ATOM   1753  C C   . THR B  2 28  ? 34.903  -26.266  13.705  1.000 42.140  0 28  THR BBB C   1 ? 4  
ATOM   1754  O O   . THR B  2 28  ? 34.610  -25.427  12.840  1.000 44.276  0 28  THR BBB O   1 ? 4  
ATOM   1755  C CB  . THR B  2 28  ? 32.667  -27.346  13.144  1.000 47.046  0 28  THR BBB CB  1 ? 4  
ATOM   1756  O OG1 . THR B  2 28  ? 31.904  -26.424  13.908  1.000 47.896  0 28  THR BBB OG1 1 ? 4  
ATOM   1757  C CG2 . THR B  2 28  ? 31.898  -28.634  13.005  1.000 48.453  0 28  THR BBB CG2 1 ? 4  
ATOM   1758  N N   . PHE B  2 29  ? 35.947  -26.169  14.516  1.000 41.036  0 29  PHE BBB N   1 ? 4  
ATOM   1759  C CA  . PHE B  2 29  ? 36.933  -25.050  14.498  1.000 40.849  0 29  PHE BBB CA  1 ? 4  
ATOM   1760  C C   . PHE B  2 29  ? 37.455  -24.840  13.071  1.000 40.467  0 29  PHE BBB C   1 ? 4  
ATOM   1761  O O   . PHE B  2 29  ? 37.589  -23.670  12.677  1.000 42.842  0 29  PHE BBB O   1 ? 4  
ATOM   1762  C CB  . PHE B  2 29  ? 38.095  -25.317  15.467  1.000 41.919  0 29  PHE BBB CB  1 ? 4  
ATOM   1763  C CG  . PHE B  2 29  ? 39.111  -24.209  15.518  1.000 42.509  0 29  PHE BBB CG  1 ? 4  
ATOM   1764  C CD1 . PHE B  2 29  ? 38.845  -23.060  16.238  1.000 42.170  0 29  PHE BBB CD1 1 ? 4  
ATOM   1765  C CD2 . PHE B  2 29  ? 40.325  -24.296  14.847  1.000 44.520  0 29  PHE BBB CD2 1 ? 4  
ATOM   1766  C CE1 . PHE B  2 29  ? 39.766  -22.025  16.307  1.000 41.452  0 29  PHE BBB CE1 1 ? 4  
ATOM   1767  C CE2 . PHE B  2 29  ? 41.260  -23.267  14.928  1.000 44.976  0 29  PHE BBB CE2 1 ? 4  
ATOM   1768  C CZ  . PHE B  2 29  ? 40.973  -22.129  15.659  1.000 43.729  0 29  PHE BBB CZ  1 ? 4  
ATOM   1769  N N   . HIS B  2 30  ? 37.701  -25.926  12.322  1.000 39.868  0 30  HIS BBB N   1 ? 4  
ATOM   1770  C CA  . HIS B  2 30  ? 38.223  -25.912  10.925  1.000 40.493  0 30  HIS BBB CA  1 ? 4  
ATOM   1771  C C   . HIS B  2 30  ? 37.272  -25.129  10.004  1.000 40.338  0 30  HIS BBB C   1 ? 4  
ATOM   1772  O O   . HIS B  2 30  ? 37.728  -24.679  8.940   1.000 43.536  0 30  HIS BBB O   1 ? 4  
ATOM   1773  C CB  . HIS B  2 30  ? 38.473  -27.343  10.416  1.000 41.007  0 30  HIS BBB CB  1 ? 4  
ATOM   1774  C CG  . HIS B  2 30  ? 37.190  -28.081  10.208  1.000 41.919  0 30  HIS BBB CG  1 ? 4  
ATOM   1775  N ND1 . HIS B  2 30  ? 36.505  -28.704  11.253  1.000 41.966  0 30  HIS BBB ND1 1 ? 4  
ATOM   1776  C CD2 . HIS B  2 30  ? 36.391  -28.166  9.114   1.000 40.747  0 30  HIS BBB CD2 1 ? 4  
ATOM   1777  C CE1 . HIS B  2 30  ? 35.380  -29.212  10.785  1.000 42.009  0 30  HIS BBB CE1 1 ? 4  
ATOM   1778  N NE2 . HIS B  2 30  ? 35.297  -28.906  9.463   1.000 41.473  0 30  HIS BBB NE2 1 ? 4  
ATOM   1779  N N   . SER B  2 31  ? 35.992  -24.974  10.370  1.000 39.840  0 31  SER BBB N   1 ? 4  
ATOM   1780  C CA  . SER B  2 31  ? 34.993  -24.296  9.509   1.000 39.095  0 31  SER BBB CA  1 ? 4  
ATOM   1781  C C   . SER B  2 31  ? 35.025  -22.779  9.759   1.000 38.703  0 31  SER BBB C   1 ? 4  
ATOM   1782  O O   . SER B  2 31  ? 34.269  -22.071  9.072   1.000 38.016  0 31  SER BBB O   1 ? 4  
ATOM   1783  C CB  . SER B  2 31  ? 33.616  -24.867  9.684   1.000 38.922  0 31  SER BBB CB  1 ? 4  
ATOM   1784  O OG  . SER B  2 31  ? 33.074  -24.505  10.937  1.000 39.716  0 31  SER BBB OG  1 ? 4  
ATOM   1785  N N   . TYR B  2 32  ? 35.856  -22.288  10.690  1.000 37.545  0 32  TYR BBB N   1 ? 4  
ATOM   1786  C CA  . TYR B  2 32  ? 35.852  -20.854  11.092  1.000 37.004  0 32  TYR BBB CA  1 ? 4  
ATOM   1787  C C   . TYR B  2 32  ? 37.070  -20.144  10.527  1.000 37.592  0 32  TYR BBB C   1 ? 4  
ATOM   1788  O O   . TYR B  2 32  ? 38.183  -20.662  10.643  1.000 39.320  0 32  TYR BBB O   1 ? 4  
ATOM   1789  C CB  . TYR B  2 32  ? 35.729  -20.677  12.610  1.000 36.116  0 32  TYR BBB CB  1 ? 4  
ATOM   1790  C CG  . TYR B  2 32  ? 34.339  -20.978  13.089  1.000 35.660  0 32  TYR BBB CG  1 ? 4  
ATOM   1791  C CD1 . TYR B  2 32  ? 33.955  -22.269  13.384  1.000 38.655  0 32  TYR BBB CD1 1 ? 4  
ATOM   1792  C CD2 . TYR B  2 32  ? 33.376  -19.997  13.136  1.000 36.364  0 32  TYR BBB CD2 1 ? 4  
ATOM   1793  C CE1 . TYR B  2 32  ? 32.661  -22.576  13.775  1.000 40.393  0 32  TYR BBB CE1 1 ? 4  
ATOM   1794  C CE2 . TYR B  2 32  ? 32.061  -20.286  13.497  1.000 38.929  0 32  TYR BBB CE2 1 ? 4  
ATOM   1795  C CZ  . TYR B  2 32  ? 31.703  -21.579  13.822  1.000 40.760  0 32  TYR BBB CZ  1 ? 4  
ATOM   1796  O OH  . TYR B  2 32  ? 30.417  -21.862  14.167  1.000 43.682  0 32  TYR BBB OH  1 ? 4  
ATOM   1797  N N   . VAL B  2 33  ? 36.818  -18.993  9.901   1.000 38.362  0 33  VAL BBB N   1 ? 4  
ATOM   1798  C CA  . VAL B  2 33  ? 37.835  -17.936  9.689   1.000 39.857  0 33  VAL BBB CA  1 ? 4  
ATOM   1799  C C   . VAL B  2 33  ? 38.093  -17.315  11.061  1.000 40.002  0 33  VAL BBB C   1 ? 4  
ATOM   1800  O O   . VAL B  2 33  ? 37.115  -16.922  11.727  1.000 42.733  0 33  VAL BBB O   1 ? 4  
ATOM   1801  C CB  . VAL B  2 33  ? 37.344  -16.893  8.669   1.000 41.905  0 33  VAL BBB CB  1 ? 4  
ATOM   1802  C CG1 . VAL B  2 33  ? 38.294  -15.719  8.531   1.000 40.940  0 33  VAL BBB CG1 1 ? 4  
ATOM   1803  C CG2 . VAL B  2 33  ? 37.099  -17.542  7.318   1.000 43.864  0 33  VAL BBB CG2 1 ? 4  
ATOM   1804  N N   . MET B  2 34  ? 39.355  -17.248  11.479  1.000 41.395  0 34  MET BBB N   1 ? 4  
ATOM   1805  C CA  . MET B  2 34  ? 39.739  -16.687  12.804  1.000 40.581  0 34  MET BBB CA  1 ? 4  
ATOM   1806  C C   . MET B  2 34  ? 40.454  -15.348  12.592  1.000 41.193  0 34  MET BBB C   1 ? 4  
ATOM   1807  O O   . MET B  2 34  ? 41.171  -15.181  11.559  1.000 36.632  0 34  MET BBB O   1 ? 4  
ATOM   1808  C CB  . MET B  2 34  ? 40.644  -17.655  13.564  1.000 41.787  0 34  MET BBB CB  1 ? 4  
ATOM   1809  C CG  . MET B  2 34  ? 40.004  -19.018  13.822  1.000 42.134  0 34  MET BBB CG  1 ? 4  
ATOM   1810  S SD  . MET B  2 34  ? 38.443  -18.896  14.714  1.000 41.223  0 34  MET BBB SD  1 ? 4  
ATOM   1811  C CE  . MET B  2 34  ? 39.017  -18.226  16.291  1.000 42.175  0 34  MET BBB CE  1 ? 4  
ATOM   1812  N N   . ALA B  2 35  ? 40.220  -14.400  13.497  1.000 41.331  0 35  ALA BBB N   1 ? 4  
ATOM   1813  C CA  . ALA B  2 35  ? 40.737  -13.025  13.338  1.000 43.288  0 35  ALA BBB CA  1 ? 4  
ATOM   1814  C C   . ALA B  2 35  ? 41.125  -12.436  14.695  1.000 43.486  0 35  ALA BBB C   1 ? 4  
ATOM   1815  O O   . ALA B  2 35  ? 40.603  -12.883  15.753  1.000 42.112  0 35  ALA BBB O   1 ? 4  
ATOM   1816  C CB  . ALA B  2 35  ? 39.718  -12.162  12.623  1.000 44.003  0 35  ALA BBB CB  1 ? 4  
ATOM   1817  N N   . TRP B  2 36  ? 42.017  -11.447  14.623  1.000 43.374  0 36  TRP BBB N   1 ? 4  
ATOM   1818  C CA  . TRP B  2 36  ? 42.426  -10.562  15.742  1.000 43.390  0 36  TRP BBB CA  1 ? 4  
ATOM   1819  C C   . TRP B  2 36  ? 42.077  -9.126   15.386  1.000 43.590  0 36  TRP BBB C   1 ? 4  
ATOM   1820  O O   . TRP B  2 36  ? 42.364  -8.695   14.250  1.000 47.072  0 36  TRP BBB O   1 ? 4  
ATOM   1821  C CB  . TRP B  2 36  ? 43.921  -10.714  16.011  1.000 45.029  0 36  TRP BBB CB  1 ? 4  
ATOM   1822  C CG  . TRP B  2 36  ? 44.272  -12.034  16.617  1.000 44.900  0 36  TRP BBB CG  1 ? 4  
ATOM   1823  C CD1 . TRP B  2 36  ? 44.723  -13.137  15.966  1.000 45.004  0 36  TRP BBB CD1 1 ? 4  
ATOM   1824  C CD2 . TRP B  2 36  ? 44.162  -12.405  17.996  1.000 45.023  0 36  TRP BBB CD2 1 ? 4  
ATOM   1825  N NE1 . TRP B  2 36  ? 44.905  -14.163  16.844  1.000 46.102  0 36  TRP BBB NE1 1 ? 4  
ATOM   1826  C CE2 . TRP B  2 36  ? 44.588  -13.738  18.100  1.000 46.064  0 36  TRP BBB CE2 1 ? 4  
ATOM   1827  C CE3 . TRP B  2 36  ? 43.788  -11.730  19.156  1.000 46.779  0 36  TRP BBB CE3 1 ? 4  
ATOM   1828  C CZ2 . TRP B  2 36  ? 44.665  -14.406  19.323  1.000 47.283  0 36  TRP BBB CZ2 1 ? 4  
ATOM   1829  C CZ3 . TRP B  2 36  ? 43.826  -12.404  20.358  1.000 48.153  0 36  TRP BBB CZ3 1 ? 4  
ATOM   1830  C CH2 . TRP B  2 36  ? 44.268  -13.716  20.442  1.000 47.155  0 36  TRP BBB CH2 1 ? 4  
ATOM   1831  N N   . PHE B  2 37  ? 41.419  -8.442   16.308  1.000 41.834  0 37  PHE BBB N   1 ? 4  
ATOM   1832  C CA  . PHE B  2 37  ? 41.214  -6.980   16.276  1.000 42.564  0 37  PHE BBB CA  1 ? 4  
ATOM   1833  C C   . PHE B  2 37  ? 41.828  -6.420   17.553  1.000 44.341  0 37  PHE BBB C   1 ? 4  
ATOM   1834  O O   . PHE B  2 37  ? 42.094  -7.213   18.508  1.000 43.426  0 37  PHE BBB O   1 ? 4  
ATOM   1835  C CB  . PHE B  2 37  ? 39.730  -6.663   16.217  1.000 43.063  0 37  PHE BBB CB  1 ? 4  
ATOM   1836  C CG  . PHE B  2 37  ? 39.070  -6.923   14.893  1.000 42.624  0 37  PHE BBB CG  1 ? 4  
ATOM   1837  C CD1 . PHE B  2 37  ? 38.793  -8.214   14.482  1.000 42.160  0 37  PHE BBB CD1 1 ? 4  
ATOM   1838  C CD2 . PHE B  2 37  ? 38.682  -5.869   14.083  1.000 44.432  0 37  PHE BBB CD2 1 ? 4  
ATOM   1839  C CE1 . PHE B  2 37  ? 38.169  -8.444   13.266  1.000 42.988  0 37  PHE BBB CE1 1 ? 4  
ATOM   1840  C CE2 . PHE B  2 37  ? 38.074  -6.101   12.864  1.000 45.212  0 37  PHE BBB CE2 1 ? 4  
ATOM   1841  C CZ  . PHE B  2 37  ? 37.820  -7.382   12.456  1.000 44.228  0 37  PHE BBB CZ  1 ? 4  
ATOM   1842  N N   . ARG B  2 38  ? 42.048  -5.110   17.594  1.000 45.673  0 38  ARG BBB N   1 ? 4  
ATOM   1843  C CA  . ARG B  2 38  ? 42.502  -4.464   18.851  1.000 48.832  0 38  ARG BBB CA  1 ? 4  
ATOM   1844  C C   . ARG B  2 38  ? 41.806  -3.111   19.000  1.000 51.536  0 38  ARG BBB C   1 ? 4  
ATOM   1845  O O   . ARG B  2 38  ? 41.334  -2.526   17.994  1.000 51.536  0 38  ARG BBB O   1 ? 4  
ATOM   1846  C CB  . ARG B  2 38  ? 44.024  -4.317   18.876  1.000 49.834  0 38  ARG BBB CB  1 ? 4  
ATOM   1847  C CG  . ARG B  2 38  ? 44.546  -3.262   17.916  1.000 52.407  0 38  ARG BBB CG  1 ? 4  
ATOM   1848  C CD  . ARG B  2 38  ? 46.036  -3.396   17.726  1.000 54.881  0 38  ARG BBB CD  1 ? 4  
ATOM   1849  N NE  . ARG B  2 38  ? 46.524  -2.454   16.745  1.000 59.382  0 38  ARG BBB NE  1 ? 4  
ATOM   1850  C CZ  . ARG B  2 38  ? 47.809  -2.235   16.461  1.000 62.172  0 38  ARG BBB CZ  1 ? 4  
ATOM   1851  N NH1 . ARG B  2 38  ? 48.769  -2.909   17.080  1.000 62.068  0 38  ARG BBB NH1 1 ? 4  
ATOM   1852  N NH2 . ARG B  2 38  ? 48.107  -1.360   15.508  1.000 63.577  0 38  ARG BBB NH2 1 ? 4  
ATOM   1853  N N   . GLN B  2 39  ? 41.766  -2.622   20.229  1.000 52.009  0 39  GLN BBB N   1 ? 4  
ATOM   1854  C CA  . GLN B  2 39  ? 41.110  -1.342   20.529  1.000 55.706  0 39  GLN BBB CA  1 ? 4  
ATOM   1855  C C   . GLN B  2 39  ? 41.925  -0.628   21.599  1.000 60.646  0 39  GLN BBB C   1 ? 4  
ATOM   1856  O O   . GLN B  2 39  ? 42.001  -1.140   22.754  1.000 60.951  0 39  GLN BBB O   1 ? 4  
ATOM   1857  C CB  . GLN B  2 39  ? 39.685  -1.602   20.975  1.000 53.900  0 39  GLN BBB CB  1 ? 4  
ATOM   1858  C CG  . GLN B  2 39  ? 38.965  -0.307   21.296  1.000 56.359  0 39  GLN BBB CG  1 ? 4  
ATOM   1859  C CD  . GLN B  2 39  ? 37.505  -0.537   21.531  1.000 55.929  0 39  GLN BBB CD  1 ? 4  
ATOM   1860  O OE1 . GLN B  2 39  ? 37.091  -1.604   22.006  1.000 55.453  0 39  GLN BBB OE1 1 ? 4  
ATOM   1861  N NE2 . GLN B  2 39  ? 36.736  0.464    21.140  1.000 58.067  0 39  GLN BBB NE2 1 ? 4  
ATOM   1862  N N   . ALA B  2 40  ? 42.531  0.476    21.170  1.000 66.040  0 40  ALA BBB N   1 ? 4  
ATOM   1863  C CA  . ALA B  2 40  ? 43.243  1.448    22.012  1.000 69.119  0 40  ALA BBB CA  1 ? 4  
ATOM   1864  C C   . ALA B  2 40  ? 42.192  2.342    22.646  1.000 71.570  0 40  ALA BBB C   1 ? 4  
ATOM   1865  O O   . ALA B  2 40  ? 41.115  2.541    22.083  1.000 70.208  0 40  ALA BBB O   1 ? 4  
ATOM   1866  C CB  . ALA B  2 40  ? 44.222  2.215    21.150  1.000 70.709  0 40  ALA BBB CB  1 ? 4  
ATOM   1867  N N   . PRO B  2 41  ? 42.476  2.929    23.828  1.000 76.857  0 41  PRO BBB N   1 ? 4  
ATOM   1868  C CA  . PRO B  2 41  ? 41.570  3.913    24.420  1.000 79.199  0 41  PRO BBB CA  1 ? 4  
ATOM   1869  C C   . PRO B  2 41  ? 41.367  5.110    23.467  1.000 81.186  0 41  PRO BBB C   1 ? 4  
ATOM   1870  O O   . PRO B  2 41  ? 42.324  5.607    22.895  1.000 80.794  0 41  PRO BBB O   1 ? 4  
ATOM   1871  C CB  . PRO B  2 41  ? 42.248  4.301    25.746  1.000 82.751  0 41  PRO BBB CB  1 ? 4  
ATOM   1872  C CG  . PRO B  2 41  ? 43.715  3.830    25.633  1.000 81.864  0 41  PRO BBB CG  1 ? 4  
ATOM   1873  C CD  . PRO B  2 41  ? 43.696  2.699    24.624  1.000 78.656  0 41  PRO BBB CD  1 ? 4  
ATOM   1874  N N   . GLY B  2 42  ? 40.112  5.502    23.269  1.000 82.393  0 42  GLY BBB N   1 ? 4  
ATOM   1875  C CA  . GLY B  2 42  ? 39.722  6.612    22.381  1.000 84.585  0 42  GLY BBB CA  1 ? 4  
ATOM   1876  C C   . GLY B  2 42  ? 39.506  6.175    20.945  1.000 83.574  0 42  GLY BBB C   1 ? 4  
ATOM   1877  O O   . GLY B  2 42  ? 39.000  7.007    20.171  1.000 85.991  0 42  GLY BBB O   1 ? 4  
ATOM   1878  N N   . LYS B  2 43  ? 39.862  4.939    20.577  1.000 81.091  0 43  LYS BBB N   1 ? 4  
ATOM   1879  C CA  . LYS B  2 43  ? 39.815  4.472    19.170  1.000 80.488  0 43  LYS BBB CA  1 ? 4  
ATOM   1880  C C   . LYS B  2 43  ? 38.747  3.397    19.014  1.000 77.578  0 43  LYS BBB C   1 ? 4  
ATOM   1881  O O   . LYS B  2 43  ? 38.330  2.818    20.019  1.000 77.193  0 43  LYS BBB O   1 ? 4  
ATOM   1882  C CB  . LYS B  2 43  ? 41.167  3.919    18.726  1.000 81.836  0 43  LYS BBB CB  1 ? 4  
ATOM   1883  C CG  . LYS B  2 43  ? 42.135  4.991    18.240  1.000 86.254  0 43  LYS BBB CG  1 ? 4  
ATOM   1884  C CD  . LYS B  2 43  ? 43.512  4.466    17.934  1.000 86.384  0 43  LYS BBB CD  1 ? 4  
ATOM   1885  C CE  . LYS B  2 43  ? 44.283  5.359    16.990  1.000 90.828  0 43  LYS BBB CE  1 ? 4  
ATOM   1886  N NZ  . LYS B  2 43  ? 44.907  4.542    15.928  1.000 89.795  0 43  LYS BBB NZ  1 ? 4  
ATOM   1887  N N   . GLU B  2 44  ? 38.320  3.152    17.776  1.000 77.213  0 44  GLU BBB N   1 ? 4  
ATOM   1888  C CA  . GLU B  2 44  ? 37.381  2.051    17.443  1.000 74.688  0 44  GLU BBB CA  1 ? 4  
ATOM   1889  C C   . GLU B  2 44  ? 38.190  0.768    17.318  1.000 69.096  0 44  GLU BBB C   1 ? 4  
ATOM   1890  O O   . GLU B  2 44  ? 39.419  0.859    17.315  1.000 69.509  0 44  GLU BBB O   1 ? 4  
ATOM   1891  C CB  . GLU B  2 44  ? 36.579  2.362    16.182  1.000 77.789  0 44  GLU BBB CB  1 ? 4  
ATOM   1892  C CG  . GLU B  2 44  ? 35.908  3.730    16.203  1.000 86.367  0 44  GLU BBB CG  1 ? 4  
ATOM   1893  C CD  . GLU B  2 44  ? 34.952  3.988    17.368  1.000 91.160  0 44  GLU BBB CD  1 ? 4  
ATOM   1894  O OE1 . GLU B  2 44  ? 34.243  3.030    17.751  1.000 90.027  0 44  GLU BBB OE1 1 ? 4  
ATOM   1895  O OE2 . GLU B  2 44  ? 34.921  5.139    17.903  1.000 93.253  0 44  GLU BBB OE2 1 ? 4  
ATOM   1896  N N   . ARG B  2 45  ? 37.517  -0.372   17.252  1.000 65.821  0 45  ARG BBB N   1 ? 4  
ATOM   1897  C CA  . ARG B  2 45  ? 38.158  -1.682   16.967  1.000 66.158  0 45  ARG BBB CA  1 ? 4  
ATOM   1898  C C   . ARG B  2 45  ? 38.823  -1.617   15.593  1.000 64.123  0 45  ARG BBB C   1 ? 4  
ATOM   1899  O O   . ARG B  2 45  ? 38.142  -1.309   14.610  1.000 68.708  0 45  ARG BBB O   1 ? 4  
ATOM   1900  C CB  . ARG B  2 45  ? 37.161  -2.836   17.011  1.000 64.684  0 45  ARG BBB CB  1 ? 4  
ATOM   1901  C CG  . ARG B  2 45  ? 37.027  -3.429   18.398  1.000 67.109  0 45  ARG BBB CG  1 ? 4  
ATOM   1902  C CD  . ARG B  2 45  ? 35.792  -4.286   18.522  1.000 69.179  0 45  ARG BBB CD  1 ? 4  
ATOM   1903  N NE  . ARG B  2 45  ? 35.316  -4.257   19.892  1.000 73.207  0 45  ARG BBB NE  1 ? 4  
ATOM   1904  C CZ  . ARG B  2 45  ? 34.664  -5.246   20.495  1.000 76.431  0 45  ARG BBB CZ  1 ? 4  
ATOM   1905  N NH1 . ARG B  2 45  ? 34.393  -6.372   19.857  1.000 78.241  0 45  ARG BBB NH1 1 ? 4  
ATOM   1906  N NH2 . ARG B  2 45  ? 34.311  -5.118   21.761  1.000 77.274  0 45  ARG BBB NH2 1 ? 4  
ATOM   1907  N N   . GLU B  2 46  ? 40.118  -1.886   15.560  1.000 61.122  0 46  GLU BBB N   1 ? 4  
ATOM   1908  C CA  . GLU B  2 46  ? 40.979  -1.845   14.365  1.000 60.016  0 46  GLU BBB CA  1 ? 4  
ATOM   1909  C C   . GLU B  2 46  ? 41.331  -3.303   14.022  1.000 54.786  0 46  GLU BBB C   1 ? 4  
ATOM   1910  O O   . GLU B  2 46  ? 41.690  -4.091   14.934  1.000 51.770  0 46  GLU BBB O   1 ? 4  
ATOM   1911  C CB  . GLU B  2 46  ? 42.157  -0.932   14.720  1.000 63.316  0 46  GLU BBB CB  1 ? 4  
ATOM   1912  C CG  . GLU B  2 46  ? 43.269  -0.890   13.687  1.000 67.535  0 46  GLU BBB CG  1 ? 4  
ATOM   1913  C CD  . GLU B  2 46  ? 44.620  -0.400   14.182  1.000 68.446  0 46  GLU BBB CD  1 ? 4  
ATOM   1914  O OE1 . GLU B  2 46  ? 44.646  0.278    15.236  1.000 68.429  0 46  GLU BBB OE1 1 ? 4  
ATOM   1915  O OE2 . GLU B  2 46  ? 45.591  -0.640   13.451  1.000 70.188  0 46  GLU BBB OE2 1 ? 4  
ATOM   1916  N N   . PHE B  2 47  ? 41.186  -3.681   12.758  1.000 52.776  0 47  PHE BBB N   1 ? 4  
ATOM   1917  C CA  . PHE B  2 47  ? 41.572  -5.023   12.258  1.000 51.085  0 47  PHE BBB CA  1 ? 4  
ATOM   1918  C C   . PHE B  2 47  ? 43.086  -5.186   12.389  1.000 50.543  0 47  PHE BBB C   1 ? 4  
ATOM   1919  O O   . PHE B  2 47  ? 43.830  -4.281   11.988  1.000 51.828  0 47  PHE BBB O   1 ? 4  
ATOM   1920  C CB  . PHE B  2 47  ? 41.153  -5.201   10.802  1.000 50.446  0 47  PHE BBB CB  1 ? 4  
ATOM   1921  C CG  . PHE B  2 47  ? 41.647  -6.476   10.174  1.000 49.949  0 47  PHE BBB CG  1 ? 4  
ATOM   1922  C CD1 . PHE B  2 47  ? 40.961  -7.660   10.383  1.000 48.605  0 47  PHE BBB CD1 1 ? 4  
ATOM   1923  C CD2 . PHE B  2 47  ? 42.782  -6.491   9.377   1.000 51.221  0 47  PHE BBB CD2 1 ? 4  
ATOM   1924  C CE1 . PHE B  2 47  ? 41.400  -8.830   9.798   1.000 45.488  0 47  PHE BBB CE1 1 ? 4  
ATOM   1925  C CE2 . PHE B  2 47  ? 43.219  -7.671   8.801   1.000 49.940  0 47  PHE BBB CE2 1 ? 4  
ATOM   1926  C CZ  . PHE B  2 47  ? 42.525  -8.835   9.022   1.000 46.896  0 47  PHE BBB CZ  1 ? 4  
ATOM   1927  N N   . VAL B  2 48  ? 43.517  -6.342   12.881  1.000 49.089  0 48  VAL BBB N   1 ? 4  
ATOM   1928  C CA  . VAL B  2 48  ? 44.961  -6.685   13.029  1.000 50.178  0 48  VAL BBB CA  1 ? 4  
ATOM   1929  C C   . VAL B  2 48  ? 45.327  -7.791   12.035  1.000 48.413  0 48  VAL BBB C   1 ? 4  
ATOM   1930  O O   . VAL B  2 48  ? 46.300  -7.597   11.279  1.000 48.573  0 48  VAL BBB O   1 ? 4  
ATOM   1931  C CB  . VAL B  2 48  ? 45.294  -7.076   14.481  1.000 50.053  0 48  VAL BBB CB  1 ? 4  
ATOM   1932  C CG1 . VAL B  2 48  ? 46.730  -7.558   14.630  1.000 50.225  0 48  VAL BBB CG1 1 ? 4  
ATOM   1933  C CG2 . VAL B  2 48  ? 45.003  -5.929   15.439  1.000 53.281  0 48  VAL BBB CG2 1 ? 4  
ATOM   1934  N N   . ALA B  2 49  ? 44.618  -8.920   12.063  1.000 47.865  0 49  ALA BBB N   1 ? 4  
ATOM   1935  C CA  . ALA B  2 49  ? 44.954  -10.110  11.246  1.000 49.184  0 49  ALA BBB CA  1 ? 4  
ATOM   1936  C C   . ALA B  2 49  ? 43.780  -11.092  11.154  1.000 47.239  0 49  ALA BBB C   1 ? 4  
ATOM   1937  O O   . ALA B  2 49  ? 42.907  -11.101  12.045  1.000 47.465  0 49  ALA BBB O   1 ? 4  
ATOM   1938  C CB  . ALA B  2 49  ? 46.187  -10.788  11.805  1.000 50.900  0 49  ALA BBB CB  1 ? 4  
ATOM   1939  N N   . ALA B  2 50  ? 43.786  -11.901  10.102  1.000 47.837  0 50  ALA BBB N   1 ? 4  
ATOM   1940  C CA  . ALA B  2 50  ? 42.795  -12.967  9.859   1.000 46.723  0 50  ALA BBB CA  1 ? 4  
ATOM   1941  C C   . ALA B  2 50  ? 43.443  -14.106  9.076   1.000 46.620  0 50  ALA BBB C   1 ? 4  
ATOM   1942  O O   . ALA B  2 50  ? 44.399  -13.861  8.308   1.000 47.144  0 50  ALA BBB O   1 ? 4  
ATOM   1943  C CB  . ALA B  2 50  ? 41.596  -12.418  9.127   1.000 45.481  0 50  ALA BBB CB  1 ? 4  
ATOM   1944  N N   . ILE B  2 51  ? 42.904  -15.304  9.259   1.000 46.392  0 51  ILE BBB N   1 ? 4  
ATOM   1945  C CA  . ILE B  2 51  ? 43.413  -16.549  8.624   1.000 46.182  0 51  ILE BBB CA  1 ? 4  
ATOM   1946  C C   . ILE B  2 51  ? 42.218  -17.388  8.171   1.000 45.360  0 51  ILE BBB C   1 ? 4  
ATOM   1947  O O   . ILE B  2 51  ? 41.282  -17.643  8.981   1.000 44.383  0 51  ILE BBB O   1 ? 4  
ATOM   1948  C CB  . ILE B  2 51  ? 44.350  -17.285  9.606   1.000 46.656  0 51  ILE BBB CB  1 ? 4  
ATOM   1949  C CG1 . ILE B  2 51  ? 45.043  -18.474  8.948   1.000 48.362  0 51  ILE BBB CG1 1 ? 4  
ATOM   1950  C CG2 . ILE B  2 51  ? 43.631  -17.687  10.891  1.000 47.073  0 51  ILE BBB CG2 1 ? 4  
ATOM   1951  C CD1 . ILE B  2 51  ? 46.203  -19.013  9.732   1.000 49.554  0 51  ILE BBB CD1 1 ? 4  
ATOM   1952  N N   . SER B  2 52  ? 42.238  -17.782  6.903   1.000 46.139  0 52  SER BBB N   1 ? 4  
ATOM   1953  C CA  . SER B  2 52  ? 41.187  -18.610  6.281   1.000 44.834  0 52  SER BBB CA  1 ? 4  
ATOM   1954  C C   . SER B  2 52  ? 41.317  -20.052  6.778   1.000 43.059  0 52  SER BBB C   1 ? 4  
ATOM   1955  O O   . SER B  2 52  ? 42.247  -20.363  7.534   1.000 41.108  0 52  SER BBB O   1 ? 4  
ATOM   1956  C CB  . SER B  2 52  ? 41.246  -18.534  4.779   1.000 46.659  0 52  SER BBB CB  1 ? 4  
ATOM   1957  O OG  . SER B  2 52  ? 39.999  -18.901  4.236   1.000 46.104  0 52  SER BBB OG  1 ? 4  
ATOM   1958  N N   . TRP B  2 53  ? 40.364  -20.888  6.365   1.000 44.367  0 53  TRP BBB N   1 ? 4  
ATOM   1959  C CA  . TRP B  2 53  ? 40.152  -22.270  6.867   1.000 44.126  0 53  TRP BBB CA  1 ? 4  
ATOM   1960  C C   . TRP B  2 53  ? 41.428  -23.088  6.675   1.000 46.613  0 53  TRP BBB C   1 ? 4  
ATOM   1961  O O   . TRP B  2 53  ? 41.890  -23.661  7.656   1.000 49.838  0 53  TRP BBB O   1 ? 4  
ATOM   1962  C CB  . TRP B  2 53  ? 38.950  -22.906  6.158   1.000 43.144  0 53  TRP BBB CB  1 ? 4  
ATOM   1963  C CG  . TRP B  2 53  ? 37.742  -22.027  6.127   1.000 39.341  0 53  TRP BBB CG  1 ? 4  
ATOM   1964  C CD1 . TRP B  2 53  ? 36.903  -21.750  7.157   1.000 36.692  0 53  TRP BBB CD1 1 ? 4  
ATOM   1965  C CD2 . TRP B  2 53  ? 37.243  -21.299  4.996   1.000 39.733  0 53  TRP BBB CD2 1 ? 4  
ATOM   1966  N NE1 . TRP B  2 53  ? 35.905  -20.908  6.747   1.000 36.637  0 53  TRP BBB NE1 1 ? 4  
ATOM   1967  C CE2 . TRP B  2 53  ? 36.087  -20.614  5.425   1.000 38.933  0 53  TRP BBB CE2 1 ? 4  
ATOM   1968  C CE3 . TRP B  2 53  ? 37.670  -21.128  3.675   1.000 41.323  0 53  TRP BBB CE3 1 ? 4  
ATOM   1969  C CZ2 . TRP B  2 53  ? 35.352  -19.790  4.577   1.000 39.515  0 53  TRP BBB CZ2 1 ? 4  
ATOM   1970  C CZ3 . TRP B  2 53  ? 36.943  -20.322  2.834   1.000 41.791  0 53  TRP BBB CZ3 1 ? 4  
ATOM   1971  C CH2 . TRP B  2 53  ? 35.799  -19.664  3.279   1.000 42.374  0 53  TRP BBB CH2 1 ? 4  
ATOM   1972  N N   . SER B  2 54  ? 41.985  -23.089  5.463   1.000 48.034  0 54  SER BBB N   1 ? 4  
ATOM   1973  C CA  . SER B  2 54  ? 43.187  -23.865  5.062   1.000 50.183  0 54  SER BBB CA  1 ? 4  
ATOM   1974  C C   . SER B  2 54  ? 44.467  -23.241  5.634   1.000 49.971  0 54  SER BBB C   1 ? 4  
ATOM   1975  O O   . SER B  2 54  ? 45.540  -23.791  5.358   1.000 52.617  0 54  SER BBB O   1 ? 4  
ATOM   1976  C CB  . SER B  2 54  ? 43.299  -23.907  3.565   1.000 52.488  0 54  SER BBB CB  1 ? 4  
ATOM   1977  O OG  . SER B  2 54  ? 43.571  -22.601  3.078   1.000 55.256  0 54  SER BBB OG  1 ? 4  
ATOM   1978  N N   . SER B  2 55  ? 44.366  -22.082  6.276   1.000 47.751  0 55  SER BBB N   1 ? 4  
ATOM   1979  C CA  . SER B  2 55  ? 45.493  -21.182  6.656   1.000 50.874  0 55  SER BBB CA  1 ? 4  
ATOM   1980  C C   . SER B  2 55  ? 45.928  -20.286  5.490   1.000 52.876  0 55  SER BBB C   1 ? 4  
ATOM   1981  O O   . SER B  2 55  ? 46.830  -19.498  5.746   1.000 53.983  0 55  SER BBB O   1 ? 4  
ATOM   1982  C CB  . SER B  2 55  ? 46.695  -21.944  7.213   1.000 51.593  0 55  SER BBB CB  1 ? 4  
ATOM   1983  O OG  . SER B  2 55  ? 46.356  -22.663  8.395   1.000 49.827  0 55  SER BBB OG  1 ? 4  
ATOM   1984  N N   . THR B  2 56  ? 45.359  -20.383  4.278   1.000 57.493  0 56  THR BBB N   1 ? 4  
ATOM   1985  C CA  . THR B  2 56  ? 46.169  -20.114  3.053   1.000 66.843  0 56  THR BBB CA  1 ? 4  
ATOM   1986  C C   . THR B  2 56  ? 46.048  -18.699  2.510   1.000 67.012  0 56  THR BBB C   1 ? 4  
ATOM   1987  O O   . THR B  2 56  ? 47.007  -18.248  1.871   1.000 78.637  0 56  THR BBB O   1 ? 4  
ATOM   1988  C CB  . THR B  2 56  ? 45.914  -21.076  1.896   1.000 75.358  0 56  THR BBB CB  1 ? 4  
ATOM   1989  O OG1 . THR B  2 56  ? 46.818  -22.150  2.159   1.000 84.089  0 56  THR BBB OG1 1 ? 4  
ATOM   1990  C CG2 . THR B  2 56  ? 46.201  -20.493  0.524   1.000 78.648  0 56  THR BBB CG2 1 ? 4  
ATOM   1991  N N   . PRO B  2 57  ? 44.884  -18.021  2.567   1.000 56.170  0 57  PRO BBB N   1 ? 4  
ATOM   1992  C CA  . PRO B  2 57  ? 44.912  -16.552  2.587   1.000 51.443  0 57  PRO BBB CA  1 ? 4  
ATOM   1993  C C   . PRO B  2 57  ? 45.048  -16.184  4.078   1.000 49.602  0 57  PRO BBB C   1 ? 4  
ATOM   1994  O O   . PRO B  2 57  ? 44.276  -16.652  4.901   1.000 48.775  0 57  PRO BBB O   1 ? 4  
ATOM   1995  C CB  . PRO B  2 57  ? 43.627  -16.116  1.871   1.000 50.228  0 57  PRO BBB CB  1 ? 4  
ATOM   1996  C CG  . PRO B  2 57  ? 42.845  -17.453  1.652   1.000 51.225  0 57  PRO BBB CG  1 ? 4  
ATOM   1997  C CD  . PRO B  2 57  ? 43.546  -18.596  2.393   1.000 50.641  0 57  PRO BBB CD  1 ? 4  
ATOM   1998  N N   . THR B  2 58  ? 46.110  -15.461  4.426   1.000 49.024  0 58  THR BBB N   1 ? 4  
ATOM   1999  C CA  . THR B  2 58  ? 46.231  -14.669  5.674   1.000 47.836  0 58  THR BBB CA  1 ? 4  
ATOM   2000  C C   . THR B  2 58  ? 46.118  -13.193  5.314   1.000 48.539  0 58  THR BBB C   1 ? 4  
ATOM   2001  O O   . THR B  2 58  ? 46.402  -12.844  4.173   1.000 46.944  0 58  THR BBB O   1 ? 4  
ATOM   2002  C CB  . THR B  2 58  ? 47.522  -14.921  6.461   1.000 49.106  0 58  THR BBB CB  1 ? 4  
ATOM   2003  O OG1 . THR B  2 58  ? 48.665  -14.609  5.665   1.000 52.479  0 58  THR BBB OG1 1 ? 4  
ATOM   2004  C CG2 . THR B  2 58  ? 47.600  -16.332  6.999   1.000 48.160  0 58  THR BBB CG2 1 ? 4  
ATOM   2005  N N   . TYR B  2 59  ? 45.648  -12.380  6.255   1.000 49.731  0 59  TYR BBB N   1 ? 4  
ATOM   2006  C CA  . TYR B  2 59  ? 45.447  -10.926  6.064   1.000 49.899  0 59  TYR BBB CA  1 ? 4  
ATOM   2007  C C   . TYR B  2 59  ? 46.018  -10.195  7.280   1.000 50.143  0 59  TYR BBB C   1 ? 4  
ATOM   2008  O O   . TYR B  2 59  ? 45.938  -10.739  8.403   1.000 47.378  0 59  TYR BBB O   1 ? 4  
ATOM   2009  C CB  . TYR B  2 59  ? 43.968  -10.593  5.910   1.000 48.027  0 59  TYR BBB CB  1 ? 4  
ATOM   2010  C CG  . TYR B  2 59  ? 43.193  -11.307  4.836   1.000 48.370  0 59  TYR BBB CG  1 ? 4  
ATOM   2011  C CD1 . TYR B  2 59  ? 42.500  -12.475  5.113   1.000 47.782  0 59  TYR BBB CD1 1 ? 4  
ATOM   2012  C CD2 . TYR B  2 59  ? 43.054  -10.756  3.571   1.000 51.117  0 59  TYR BBB CD2 1 ? 4  
ATOM   2013  C CE1 . TYR B  2 59  ? 41.733  -13.112  4.147   1.000 47.795  0 59  TYR BBB CE1 1 ? 4  
ATOM   2014  C CE2 . TYR B  2 59  ? 42.276  -11.371  2.605   1.000 51.735  0 59  TYR BBB CE2 1 ? 4  
ATOM   2015  C CZ  . TYR B  2 59  ? 41.614  -12.557  2.889   1.000 50.198  0 59  TYR BBB CZ  1 ? 4  
ATOM   2016  O OH  . TYR B  2 59  ? 40.899  -13.194  1.908   1.000 52.320  0 59  TYR BBB OH  1 ? 4  
ATOM   2017  N N   . TYR B  2 60  ? 46.534  -8.985   7.055   1.000 50.877  0 60  TYR BBB N   1 ? 4  
ATOM   2018  C CA  . TYR B  2 60  ? 47.183  -8.140   8.082   1.000 51.234  0 60  TYR BBB CA  1 ? 4  
ATOM   2019  C C   . TYR B  2 60  ? 46.767  -6.683   7.885   1.000 52.669  0 60  TYR BBB C   1 ? 4  
ATOM   2020  O O   . TYR B  2 60  ? 46.679  -6.221   6.722   1.000 54.141  0 60  TYR BBB O   1 ? 4  
ATOM   2021  C CB  . TYR B  2 60  ? 48.694  -8.321   7.980   1.000 54.399  0 60  TYR BBB CB  1 ? 4  
ATOM   2022  C CG  . TYR B  2 60  ? 49.147  -9.711   8.327   1.000 54.754  0 60  TYR BBB CG  1 ? 4  
ATOM   2023  C CD1 . TYR B  2 60  ? 49.169  -10.136  9.644   1.000 55.141  0 60  TYR BBB CD1 1 ? 4  
ATOM   2024  C CD2 . TYR B  2 60  ? 49.510  -10.615  7.342   1.000 55.736  0 60  TYR BBB CD2 1 ? 4  
ATOM   2025  C CE1 . TYR B  2 60  ? 49.590  -11.412  9.982   1.000 54.678  0 60  TYR BBB CE1 1 ? 4  
ATOM   2026  C CE2 . TYR B  2 60  ? 49.904  -11.904  7.659   1.000 55.732  0 60  TYR BBB CE2 1 ? 4  
ATOM   2027  C CZ  . TYR B  2 60  ? 49.967  -12.290  8.984   1.000 54.741  0 60  TYR BBB CZ  1 ? 4  
ATOM   2028  O OH  . TYR B  2 60  ? 50.360  -13.550  9.305   1.000 54.128  0 60  TYR BBB OH  1 ? 4  
ATOM   2029  N N   . GLY B  2 61  ? 46.532  -5.973   8.985   1.000 52.241  0 61  GLY BBB N   1 ? 4  
ATOM   2030  C CA  . GLY B  2 61  ? 46.421  -4.505   8.985   1.000 55.031  0 61  GLY BBB CA  1 ? 4  
ATOM   2031  C C   . GLY B  2 61  ? 47.741  -3.871   8.570   1.000 58.757  0 61  GLY BBB C   1 ? 4  
ATOM   2032  O O   . GLY B  2 61  ? 48.817  -4.468   8.817   1.000 60.144  0 61  GLY BBB O   1 ? 4  
ATOM   2033  N N   . GLU B  2 62  ? 47.675  -2.696   7.956   1.000 64.251  0 62  GLU BBB N   1 ? 4  
ATOM   2034  C CA  . GLU B  2 62  ? 48.853  -2.036   7.345   1.000 68.359  0 62  GLU BBB CA  1 ? 4  
ATOM   2035  C C   . GLU B  2 62  ? 49.923  -1.825   8.414   1.000 66.975  0 62  GLU BBB C   1 ? 4  
ATOM   2036  O O   . GLU B  2 62  ? 51.087  -2.063   8.113   1.000 67.422  0 62  GLU BBB O   1 ? 4  
ATOM   2037  C CB  . GLU B  2 62  ? 48.411  -0.763   6.626   1.000 75.227  0 62  GLU BBB CB  1 ? 4  
ATOM   2038  C CG  . GLU B  2 62  ? 49.492  -0.171   5.727   1.000 84.988  0 62  GLU BBB CG  1 ? 4  
ATOM   2039  C CD  . GLU B  2 62  ? 50.236  -1.147   4.820   1.000 87.804  0 62  GLU BBB CD  1 ? 4  
ATOM   2040  O OE1 . GLU B  2 62  ? 49.597  -2.117   4.342   1.000 85.194  0 62  GLU BBB OE1 1 ? 4  
ATOM   2041  O OE2 . GLU B  2 62  ? 51.467  -0.971   4.666   1.000 92.831  0 62  GLU BBB OE2 1 ? 4  
ATOM   2042  N N   . SER B  2 63  ? 49.546  -1.449   9.633   1.000 66.502  0 63  SER BBB N   1 ? 4  
ATOM   2043  C CA  . SER B  2 63  ? 50.513  -0.981   10.661  1.000 67.237  0 63  SER BBB CA  1 ? 4  
ATOM   2044  C C   . SER B  2 63  ? 51.181  -2.168   11.366  1.000 65.758  0 63  SER BBB C   1 ? 4  
ATOM   2045  O O   . SER B  2 63  ? 52.165  -1.934   12.076  1.000 68.096  0 63  SER BBB O   1 ? 4  
ATOM   2046  C CB  . SER B  2 63  ? 49.878  -0.036   11.632  1.000 67.043  0 63  SER BBB CB  1 ? 4  
ATOM   2047  O OG  . SER B  2 63  ? 48.843  -0.679   12.338  1.000 64.974  0 63  SER BBB OG  1 ? 4  
ATOM   2048  N N   . VAL B  2 64  ? 50.718  -3.402   11.161  1.000 61.818  0 64  VAL BBB N   1 ? 5  
ATOM   2049  C CA  . VAL B  2 64  ? 51.371  -4.590   11.789  1.000 60.236  0 64  VAL BBB CA  1 ? 5  
ATOM   2050  C C   . VAL B  2 64  ? 52.048  -5.465   10.735  1.000 62.503  0 64  VAL BBB C   1 ? 5  
ATOM   2051  O O   . VAL B  2 64  ? 52.817  -6.350   11.149  1.000 63.282  0 64  VAL BBB O   1 ? 5  
ATOM   2052  C CB  . VAL B  2 64  ? 50.395  -5.416   12.634  1.000 58.258  0 64  VAL BBB CB  1 ? 5  
ATOM   2053  C CG1 . VAL B  2 64  ? 49.764  -4.548   13.712  1.000 60.375  0 64  VAL BBB CG1 1 ? 5  
ATOM   2054  C CG2 . VAL B  2 64  ? 49.353  -6.142   11.798  1.000 57.709  0 64  VAL BBB CG2 1 ? 5  
ATOM   2055  N N   . LYS B  2 65  ? 51.784  -5.223   9.448   1.000 65.581  0 65  LYS BBB N   1 ? 5  
ATOM   2056  C CA  . LYS B  2 65  ? 52.382  -5.998   8.332   1.000 67.049  0 65  LYS BBB CA  1 ? 5  
ATOM   2057  C C   . LYS B  2 65  ? 53.898  -6.098   8.552   1.000 66.350  0 65  LYS BBB C   1 ? 5  
ATOM   2058  O O   . LYS B  2 65  ? 54.519  -5.062   8.828   1.000 66.567  0 65  LYS BBB O   1 ? 5  
ATOM   2059  C CB  . LYS B  2 65  ? 52.039  -5.352   6.983   1.000 72.507  0 65  LYS BBB CB  1 ? 5  
ATOM   2060  C CG  . LYS B  2 65  ? 51.764  -6.344   5.851   1.000 76.543  0 65  LYS BBB CG  1 ? 5  
ATOM   2061  C CD  . LYS B  2 65  ? 52.195  -5.931   4.466   1.000 82.021  0 65  LYS BBB CD  1 ? 5  
ATOM   2062  C CE  . LYS B  2 65  ? 52.776  -7.087   3.670   1.000 82.375  0 65  LYS BBB CE  1 ? 5  
ATOM   2063  N NZ  . LYS B  2 65  ? 53.328  -6.565   2.414   1.000 85.975  0 65  LYS BBB NZ  1 ? 5  
ATOM   2064  N N   . GLY B  2 66  ? 54.447  -7.318   8.498   1.000 65.162  0 66  GLY BBB N   1 ? 5  
ATOM   2065  C CA  . GLY B  2 66  ? 55.884  -7.601   8.659   1.000 66.045  0 66  GLY BBB CA  1 ? 5  
ATOM   2066  C C   . GLY B  2 66  ? 56.255  -7.963   10.087  1.000 66.331  0 66  GLY BBB C   1 ? 5  
ATOM   2067  O O   . GLY B  2 66  ? 57.216  -8.725   10.264  1.000 66.990  0 66  GLY BBB O   1 ? 5  
ATOM   2068  N N   . ARG B  2 67  ? 55.538  -7.443   11.089  1.000 67.649  0 67  ARG BBB N   1 ? 5  
ATOM   2069  C CA  . ARG B  2 67  ? 55.896  -7.607   12.526  1.000 67.510  0 67  ARG BBB CA  1 ? 5  
ATOM   2070  C C   . ARG B  2 67  ? 55.076  -8.734   13.165  1.000 63.512  0 67  ARG BBB C   1 ? 5  
ATOM   2071  O O   . ARG B  2 67  ? 55.597  -9.364   14.104  1.000 61.497  0 67  ARG BBB O   1 ? 5  
ATOM   2072  C CB  . ARG B  2 67  ? 55.693  -6.283   13.271  1.000 68.976  0 67  ARG BBB CB  1 ? 5  
ATOM   2073  C CG  . ARG B  2 67  ? 56.577  -5.153   12.754  1.000 69.518  0 67  ARG BBB CG  1 ? 5  
ATOM   2074  C CD  . ARG B  2 67  ? 56.502  -3.907   13.608  1.000 69.988  0 67  ARG BBB CD  1 ? 5  
ATOM   2075  N NE  . ARG B  2 67  ? 55.148  -3.360   13.687  1.000 69.252  0 67  ARG BBB NE  1 ? 5  
ATOM   2076  C CZ  . ARG B  2 67  ? 54.428  -3.267   14.799  1.000 67.074  0 67  ARG BBB CZ  1 ? 5  
ATOM   2077  N NH1 . ARG B  2 67  ? 54.933  -3.658   15.960  1.000 68.696  0 67  ARG BBB NH1 1 ? 5  
ATOM   2078  N NH2 . ARG B  2 67  ? 53.179  -2.820   14.744  1.000 64.875  0 67  ARG BBB NH2 1 ? 5  
ATOM   2079  N N   . PHE B  2 68  ? 53.837  -8.943   12.707  1.000 59.471  0 68  PHE BBB N   1 ? 5  
ATOM   2080  C CA  . PHE B  2 68  ? 52.873  -9.887   13.334  1.000 58.348  0 68  PHE BBB CA  1 ? 5  
ATOM   2081  C C   . PHE B  2 68  ? 52.630  -11.073  12.390  1.000 56.038  0 68  PHE BBB C   1 ? 5  
ATOM   2082  O O   . PHE B  2 68  ? 52.530  -10.875  11.191  1.000 58.067  0 68  PHE BBB O   1 ? 5  
ATOM   2083  C CB  . PHE B  2 68  ? 51.557  -9.180   13.669  1.000 56.810  0 68  PHE BBB CB  1 ? 5  
ATOM   2084  C CG  . PHE B  2 68  ? 51.575  -8.166   14.785  1.000 57.567  0 68  PHE BBB CG  1 ? 5  
ATOM   2085  C CD1 . PHE B  2 68  ? 52.754  -7.690   15.336  1.000 58.507  0 68  PHE BBB CD1 1 ? 5  
ATOM   2086  C CD2 . PHE B  2 68  ? 50.381  -7.646   15.262  1.000 57.521  0 68  PHE BBB CD2 1 ? 5  
ATOM   2087  C CE1 . PHE B  2 68  ? 52.740  -6.735   16.342  1.000 59.797  0 68  PHE BBB CE1 1 ? 5  
ATOM   2088  C CE2 . PHE B  2 68  ? 50.365  -6.690   16.268  1.000 58.928  0 68  PHE BBB CE2 1 ? 5  
ATOM   2089  C CZ  . PHE B  2 68  ? 51.547  -6.233   16.807  1.000 59.214  0 68  PHE BBB CZ  1 ? 5  
ATOM   2090  N N   . THR B  2 69  ? 52.518  -12.277  12.936  1.000 55.479  0 69  THR BBB N   1 ? 5  
ATOM   2091  C CA  . THR B  2 69  ? 52.181  -13.505  12.186  1.000 55.666  0 69  THR BBB CA  1 ? 5  
ATOM   2092  C C   . THR B  2 69  ? 50.969  -14.168  12.842  1.000 55.742  0 69  THR BBB C   1 ? 5  
ATOM   2093  O O   . THR B  2 69  ? 51.048  -14.461  14.045  1.000 55.074  0 69  THR BBB O   1 ? 5  
ATOM   2094  C CB  . THR B  2 69  ? 53.372  -14.462  12.113  1.000 56.739  0 69  THR BBB CB  1 ? 5  
ATOM   2095  O OG1 . THR B  2 69  ? 54.432  -13.747  11.489  1.000 56.929  0 69  THR BBB OG1 1 ? 5  
ATOM   2096  C CG2 . THR B  2 69  ? 53.083  -15.718  11.323  1.000 57.198  0 69  THR BBB CG2 1 ? 5  
ATOM   2097  N N   . ILE B  2 70  ? 49.898  -14.364  12.077  1.000 52.137  0 70  ILE BBB N   1 ? 6  
ATOM   2098  C CA  . ILE B  2 70  ? 48.718  -15.149  12.515  1.000 50.471  0 70  ILE BBB CA  1 ? 6  
ATOM   2099  C C   . ILE B  2 70  ? 48.910  -16.590  12.024  1.000 49.643  0 70  ILE BBB C   1 ? 6  
ATOM   2100  O O   . ILE B  2 70  ? 49.451  -16.774  10.941  1.000 48.552  0 70  ILE BBB O   1 ? 6  
ATOM   2101  C CB  . ILE B  2 70  ? 47.396  -14.513  12.033  1.000 50.419  0 70  ILE BBB CB  1 ? 6  
ATOM   2102  C CG1 . ILE B  2 70  ? 46.196  -15.110  12.779  1.000 49.553  0 70  ILE BBB CG1 1 ? 6  
ATOM   2103  C CG2 . ILE B  2 70  ? 47.250  -14.620  10.507  1.000 51.087  0 70  ILE BBB CG2 1 ? 6  
ATOM   2104  C CD1 . ILE B  2 70  ? 44.888  -14.431  12.490  1.000 49.915  0 70  ILE BBB CD1 1 ? 6  
ATOM   2105  N N   . SER B  2 71  ? 48.505  -17.566  12.832  1.000 48.451  0 71  SER BBB N   1 ? 6  
ATOM   2106  C CA  . SER B  2 71  ? 48.558  -19.010  12.522  1.000 48.564  0 71  SER BBB CA  1 ? 6  
ATOM   2107  C C   . SER B  2 71  ? 47.444  -19.714  13.304  1.000 47.095  0 71  SER BBB C   1 ? 6  
ATOM   2108  O O   . SER B  2 71  ? 46.900  -19.123  14.229  1.000 46.101  0 71  SER BBB O   1 ? 6  
ATOM   2109  C CB  . SER B  2 71  ? 49.926  -19.579  12.804  1.000 49.697  0 71  SER BBB CB  1 ? 6  
ATOM   2110  O OG  . SER B  2 71  ? 50.244  -19.477  14.183  1.000 54.109  0 71  SER BBB OG  1 ? 6  
ATOM   2111  N N   . ARG B  2 72  ? 47.099  -20.931  12.914  1.000 48.252  0 72  ARG BBB N   1 ? 6  
ATOM   2112  C CA  . ARG B  2 72  ? 46.032  -21.717  13.562  1.000 48.890  0 72  ARG BBB CA  1 ? 6  
ATOM   2113  C C   . ARG B  2 72  ? 46.525  -23.151  13.728  1.000 49.356  0 72  ARG BBB C   1 ? 6  
ATOM   2114  O O   . ARG B  2 72  ? 47.310  -23.603  12.908  1.000 51.236  0 72  ARG BBB O   1 ? 6  
ATOM   2115  C CB  . ARG B  2 72  ? 44.738  -21.646  12.746  1.000 48.670  0 72  ARG BBB CB  1 ? 6  
ATOM   2116  C CG  . ARG B  2 72  ? 44.836  -22.209  11.336  1.000 48.108  0 72  ARG BBB CG  1 ? 6  
ATOM   2117  C CD  . ARG B  2 72  ? 43.577  -21.961  10.531  1.000 49.701  0 72  ARG BBB CD  1 ? 6  
ATOM   2118  N NE  . ARG B  2 72  ? 42.383  -22.517  11.162  1.000 48.824  0 72  ARG BBB NE  1 ? 6  
ATOM   2119  C CZ  . ARG B  2 72  ? 41.150  -22.010  11.058  1.000 48.775  0 72  ARG BBB CZ  1 ? 6  
ATOM   2120  N NH1 . ARG B  2 72  ? 40.914  -20.925  10.323  1.000 45.807  0 72  ARG BBB NH1 1 ? 6  
ATOM   2121  N NH2 . ARG B  2 72  ? 40.148  -22.589  11.714  1.000 48.992  0 72  ARG BBB NH2 1 ? 6  
ATOM   2122  N N   . ASP B  2 73  ? 46.088  -23.798  14.798  1.000 49.253  0 73  ASP BBB N   1 ? 6  
ATOM   2123  C CA  . ASP B  2 73  ? 46.291  -25.236  15.065  1.000 50.890  0 73  ASP BBB CA  1 ? 6  
ATOM   2124  C C   . ASP B  2 73  ? 44.907  -25.844  15.290  1.000 50.337  0 73  ASP BBB C   1 ? 6  
ATOM   2125  O O   . ASP B  2 73  ? 44.367  -25.705  16.392  1.000 51.106  0 73  ASP BBB O   1 ? 6  
ATOM   2126  C CB  . ASP B  2 73  ? 47.258  -25.418  16.230  1.000 53.192  0 73  ASP BBB CB  1 ? 6  
ATOM   2127  C CG  . ASP B  2 73  ? 47.553  -26.876  16.523  1.000 57.158  0 73  ASP BBB CG  1 ? 6  
ATOM   2128  O OD1 . ASP B  2 73  ? 46.869  -27.744  15.936  1.000 57.853  0 73  ASP BBB OD1 1 ? 6  
ATOM   2129  O OD2 . ASP B  2 73  ? 48.451  -27.131  17.342  1.000 61.965  0 73  ASP BBB OD2 1 ? 6  
ATOM   2130  N N   . ASN B  2 74  ? 44.342  -26.430  14.240  1.000 52.654  0 74  ASN BBB N   1 ? 6  
ATOM   2131  C CA  . ASN B  2 74  ? 42.969  -26.985  14.233  1.000 51.164  0 74  ASN BBB CA  1 ? 6  
ATOM   2132  C C   . ASN B  2 74  ? 42.860  -28.079  15.297  1.000 53.977  0 74  ASN BBB C   1 ? 6  
ATOM   2133  O O   . ASN B  2 74  ? 41.812  -28.132  15.961  1.000 56.017  0 74  ASN BBB O   1 ? 6  
ATOM   2134  C CB  . ASN B  2 74  ? 42.585  -27.430  12.826  1.000 50.300  0 74  ASN BBB CB  1 ? 6  
ATOM   2135  C CG  . ASN B  2 74  ? 42.236  -26.262  11.930  1.000 49.692  0 74  ASN BBB CG  1 ? 6  
ATOM   2136  O OD1 . ASN B  2 74  ? 42.297  -25.094  12.329  1.000 50.077  0 74  ASN BBB OD1 1 ? 6  
ATOM   2137  N ND2 . ASN B  2 74  ? 41.859  -26.569  10.704  1.000 49.263  0 74  ASN BBB ND2 1 ? 6  
ATOM   2138  N N   . ALA B  2 75  ? 43.906  -28.876  15.513  1.000 56.158  0 75  ALA BBB N   1 ? 6  
ATOM   2139  C CA  . ALA B  2 75  ? 43.912  -29.967  16.519  1.000 57.353  0 75  ALA BBB CA  1 ? 6  
ATOM   2140  C C   . ALA B  2 75  ? 43.669  -29.400  17.926  1.000 56.341  0 75  ALA BBB C   1 ? 6  
ATOM   2141  O O   . ALA B  2 75  ? 43.172  -30.155  18.773  1.000 59.715  0 75  ALA BBB O   1 ? 6  
ATOM   2142  C CB  . ALA B  2 75  ? 45.202  -30.760  16.445  1.000 56.732  0 75  ALA BBB CB  1 ? 6  
ATOM   2143  N N   . LYS B  2 76  ? 43.999  -28.130  18.174  1.000 54.696  0 76  LYS BBB N   1 ? 6  
ATOM   2144  C CA  . LYS B  2 76  ? 43.878  -27.496  19.514  1.000 53.485  0 76  LYS BBB CA  1 ? 6  
ATOM   2145  C C   . LYS B  2 76  ? 42.834  -26.383  19.526  1.000 49.368  0 76  LYS BBB C   1 ? 6  
ATOM   2146  O O   . LYS B  2 76  ? 42.795  -25.639  20.526  1.000 46.533  0 76  LYS BBB O   1 ? 6  
ATOM   2147  C CB  . LYS B  2 76  ? 45.223  -26.901  19.916  1.000 56.995  0 76  LYS BBB CB  1 ? 6  
ATOM   2148  C CG  . LYS B  2 76  ? 46.345  -27.921  19.980  1.000 60.438  0 76  LYS BBB CG  1 ? 6  
ATOM   2149  C CD  . LYS B  2 76  ? 47.543  -27.441  20.728  1.000 62.751  0 76  LYS BBB CD  1 ? 6  
ATOM   2150  C CE  . LYS B  2 76  ? 48.556  -28.554  20.870  1.000 68.186  0 76  LYS BBB CE  1 ? 6  
ATOM   2151  N NZ  . LYS B  2 76  ? 49.688  -28.137  21.725  1.000 72.755  0 76  LYS BBB NZ  1 ? 6  
ATOM   2152  N N   . ASN B  2 77  ? 42.033  -26.248  18.464  1.000 47.167  0 77  ASN BBB N   1 ? 6  
ATOM   2153  C CA  . ASN B  2 77  ? 40.976  -25.210  18.397  1.000 44.273  0 77  ASN BBB CA  1 ? 6  
ATOM   2154  C C   . ASN B  2 77  ? 41.596  -23.834  18.695  1.000 43.566  0 77  ASN BBB C   1 ? 6  
ATOM   2155  O O   . ASN B  2 77  ? 40.928  -22.999  19.347  1.000 42.624  0 77  ASN BBB O   1 ? 6  
ATOM   2156  C CB  . ASN B  2 77  ? 39.863  -25.501  19.410  1.000 43.968  0 77  ASN BBB CB  1 ? 6  
ATOM   2157  C CG  . ASN B  2 77  ? 38.771  -26.377  18.841  1.000 43.305  0 77  ASN BBB CG  1 ? 6  
ATOM   2158  O OD1 . ASN B  2 77  ? 39.050  -27.305  18.089  1.000 42.934  0 77  ASN BBB OD1 1 ? 6  
ATOM   2159  N ND2 . ASN B  2 77  ? 37.526  -26.084  19.186  1.000 41.517  0 77  ASN BBB ND2 1 ? 6  
ATOM   2160  N N   . THR B  2 78  ? 42.843  -23.587  18.289  1.000 44.038  0 78  THR BBB N   1 ? 6  
ATOM   2161  C CA  . THR B  2 78  ? 43.575  -22.370  18.712  1.000 43.295  0 78  THR BBB CA  1 ? 6  
ATOM   2162  C C   . THR B  2 78  ? 44.083  -21.591  17.489  1.000 44.349  0 78  THR BBB C   1 ? 6  
ATOM   2163  O O   . THR B  2 78  ? 44.600  -22.207  16.530  1.000 42.546  0 78  THR BBB O   1 ? 6  
ATOM   2164  C CB  . THR B  2 78  ? 44.666  -22.728  19.723  1.000 44.381  0 78  THR BBB CB  1 ? 6  
ATOM   2165  O OG1 . THR B  2 78  ? 44.044  -23.336  20.856  1.000 44.025  0 78  THR BBB OG1 1 ? 6  
ATOM   2166  C CG2 . THR B  2 78  ? 45.480  -21.524  20.158  1.000 43.909  0 78  THR BBB CG2 1 ? 6  
ATOM   2167  N N   . VAL B  2 79  ? 43.904  -20.268  17.539  1.000 44.400  0 79  VAL BBB N   1 ? 6  
ATOM   2168  C CA  . VAL B  2 79  ? 44.553  -19.277  16.641  1.000 44.991  0 79  VAL BBB CA  1 ? 6  
ATOM   2169  C C   . VAL B  2 79  ? 45.594  -18.516  17.465  1.000 46.719  0 79  VAL BBB C   1 ? 6  
ATOM   2170  O O   . VAL B  2 79  ? 45.358  -18.251  18.657  1.000 46.991  0 79  VAL BBB O   1 ? 6  
ATOM   2171  C CB  . VAL B  2 79  ? 43.506  -18.356  15.984  1.000 44.871  0 79  VAL BBB CB  1 ? 6  
ATOM   2172  C CG1 . VAL B  2 79  ? 42.717  -17.562  17.002  1.000 45.678  0 79  VAL BBB CG1 1 ? 6  
ATOM   2173  C CG2 . VAL B  2 79  ? 44.128  -17.431  14.949  1.000 44.752  0 79  VAL BBB CG2 1 ? 6  
ATOM   2174  N N   . TYR B  2 80  ? 46.749  -18.231  16.869  1.000 49.695  0 80  TYR BBB N   1 ? 6  
ATOM   2175  C CA  . TYR B  2 80  ? 47.905  -17.547  17.504  1.000 49.299  0 80  TYR BBB CA  1 ? 6  
ATOM   2176  C C   . TYR B  2 80  ? 48.167  -16.219  16.789  1.000 48.860  0 80  TYR BBB C   1 ? 6  
ATOM   2177  O O   . TYR B  2 80  ? 47.937  -16.109  15.581  1.000 47.297  0 80  TYR BBB O   1 ? 6  
ATOM   2178  C CB  . TYR B  2 80  ? 49.140  -18.440  17.441  1.000 51.888  0 80  TYR BBB CB  1 ? 6  
ATOM   2179  C CG  . TYR B  2 80  ? 48.997  -19.741  18.187  1.000 53.352  0 80  TYR BBB CG  1 ? 6  
ATOM   2180  C CD1 . TYR B  2 80  ? 49.116  -19.799  19.575  1.000 54.675  0 80  TYR BBB CD1 1 ? 6  
ATOM   2181  C CD2 . TYR B  2 80  ? 48.728  -20.920  17.512  1.000 53.900  0 80  TYR BBB CD2 1 ? 6  
ATOM   2182  C CE1 . TYR B  2 80  ? 48.955  -20.990  20.263  1.000 55.296  0 80  TYR BBB CE1 1 ? 6  
ATOM   2183  C CE2 . TYR B  2 80  ? 48.586  -22.121  18.187  1.000 54.966  0 80  TYR BBB CE2 1 ? 6  
ATOM   2184  C CZ  . TYR B  2 80  ? 48.728  -22.156  19.559  1.000 55.241  0 80  TYR BBB CZ  1 ? 6  
ATOM   2185  O OH  . TYR B  2 80  ? 48.583  -23.334  20.209  1.000 57.995  0 80  TYR BBB OH  1 ? 6  
ATOM   2186  N N   . LEU B  2 81  ? 48.636  -15.229  17.534  1.000 51.266  0 81  LEU BBB N   1 ? 6  
ATOM   2187  C CA  . LEU B  2 81  ? 49.207  -13.971  16.994  1.000 52.154  0 81  LEU BBB CA  1 ? 6  
ATOM   2188  C C   . LEU B  2 81  ? 50.608  -13.784  17.591  1.000 55.387  0 81  LEU BBB C   1 ? 6  
ATOM   2189  O O   . LEU B  2 81  ? 50.715  -13.456  18.793  1.000 56.990  0 81  LEU BBB O   1 ? 6  
ATOM   2190  C CB  . LEU B  2 81  ? 48.286  -12.791  17.315  1.000 51.519  0 81  LEU BBB CB  1 ? 6  
ATOM   2191  C CG  . LEU B  2 81  ? 48.624  -11.489  16.581  1.000 52.625  0 81  LEU BBB CG  1 ? 6  
ATOM   2192  C CD1 . LEU B  2 81  ? 48.361  -11.613  15.080  1.000 51.707  0 81  LEU BBB CD1 1 ? 6  
ATOM   2193  C CD2 . LEU B  2 81  ? 47.863  -10.310  17.185  1.000 52.379  0 81  LEU BBB CD2 1 ? 6  
ATOM   2194  N N   . GLN B  2 82  ? 51.636  -14.049  16.786  1.000 56.857  0 82  GLN BBB N   1 ? 6  
ATOM   2195  C CA  . GLN B  2 82  ? 53.053  -13.769  17.100  1.000 60.431  0 82  GLN BBB CA  1 ? 6  
ATOM   2196  C C   . GLN B  2 82  ? 53.250  -12.274  16.842  1.000 61.422  0 82  GLN BBB C   1 ? 6  
ATOM   2197  O O   . GLN B  2 82  ? 53.016  -11.851  15.713  1.000 61.210  0 82  GLN BBB O   1 ? 6  
ATOM   2198  C CB  . GLN B  2 82  ? 53.964  -14.679  16.261  1.000 61.030  0 82  GLN BBB CB  1 ? 6  
ATOM   2199  C CG  . GLN B  2 82  ? 55.427  -14.618  16.673  1.000 63.750  0 82  GLN BBB CG  1 ? 6  
ATOM   2200  C CD  . GLN B  2 82  ? 55.632  -14.876  18.149  1.000 64.114  0 82  GLN BBB CD  1 ? 6  
ATOM   2201  O OE1 . GLN B  2 82  ? 55.116  -15.851  18.715  1.000 62.187  0 82  GLN BBB OE1 1 ? 6  
ATOM   2202  N NE2 . GLN B  2 82  ? 56.386  -13.994  18.785  1.000 66.036  0 82  GLN BBB NE2 1 ? 6  
ATOM   2203  N N   . MET B  2 83  ? 53.548  -11.500  17.879  1.000 63.468  0 83  MET BBB N   1 ? 6  
ATOM   2204  C CA  . MET B  2 83  ? 53.760  -10.038  17.762  1.000 65.655  0 83  MET BBB CA  1 ? 6  
ATOM   2205  C C   . MET B  2 83  ? 55.235  -9.773   18.071  1.000 68.027  0 83  MET BBB C   1 ? 6  
ATOM   2206  O O   . MET B  2 83  ? 55.649  -9.997   19.215  1.000 67.026  0 83  MET BBB O   1 ? 6  
ATOM   2207  C CB  . MET B  2 83  ? 52.861  -9.250   18.723  1.000 66.243  0 83  MET BBB CB  1 ? 6  
ATOM   2208  C CG  . MET B  2 83  ? 51.393  -9.594   18.630  1.000 63.743  0 83  MET BBB CG  1 ? 6  
ATOM   2209  S SD  . MET B  2 83  ? 50.488  -8.958   20.069  1.000 66.313  0 83  MET BBB SD  1 ? 6  
ATOM   2210  C CE  . MET B  2 83  ? 50.329  -7.255   19.566  1.000 68.717  0 83  MET BBB CE  1 ? 6  
ATOM   2211  N N   . ASN B  2 84  ? 55.999  -9.368   17.059  1.000 69.734  0 84  ASN BBB N   1 ? 6  
ATOM   2212  C CA  . ASN B  2 84  ? 57.452  -9.078   17.176  1.000 71.627  0 84  ASN BBB CA  1 ? 6  
ATOM   2213  C C   . ASN B  2 84  ? 57.676  -7.568   17.085  1.000 72.978  0 84  ASN BBB C   1 ? 6  
ATOM   2214  O O   . ASN B  2 84  ? 56.779  -6.858   16.551  1.000 69.432  0 84  ASN BBB O   1 ? 6  
ATOM   2215  C CB  . ASN B  2 84  ? 58.255  -9.846   16.129  1.000 72.048  0 84  ASN BBB CB  1 ? 6  
ATOM   2216  C CG  . ASN B  2 84  ? 58.149  -11.344  16.317  1.000 71.602  0 84  ASN BBB CG  1 ? 6  
ATOM   2217  O OD1 . ASN B  2 84  ? 58.086  -11.827  17.448  1.000 74.021  0 84  ASN BBB OD1 1 ? 6  
ATOM   2218  N ND2 . ASN B  2 84  ? 58.120  -12.084  15.219  1.000 69.677  0 84  ASN BBB ND2 1 ? 6  
ATOM   2219  N N   . ARG B  2 85  ? 58.785  -7.103   17.658  1.000 75.719  0 85  ARG BBB N   1 ? 6  
ATOM   2220  C CA  . ARG B  2 85  ? 59.239  -5.699   17.540  1.000 78.170  0 85  ARG BBB CA  1 ? 6  
ATOM   2221  C C   . ARG B  2 85  ? 58.066  -4.782   17.897  1.000 75.321  0 85  ARG BBB C   1 ? 6  
ATOM   2222  O O   . ARG B  2 85  ? 57.695  -3.918   17.097  1.000 74.006  0 85  ARG BBB O   1 ? 6  
ATOM   2223  C CB  . ARG B  2 85  ? 59.882  -5.551   16.172  1.000 80.711  0 85  ARG BBB CB  1 ? 6  
ATOM   2224  C CG  . ARG B  2 85  ? 61.180  -6.365   16.110  1.000 84.314  0 85  ARG BBB CG  1 ? 6  
ATOM   2225  C CD  . ARG B  2 85  ? 62.110  -6.197   14.901  1.000 86.271  0 85  ARG BBB CD  1 ? 6  
ATOM   2226  N NE  . ARG B  2 85  ? 61.342  -6.109   13.660  1.000 85.491  0 85  ARG BBB NE  1 ? 6  
ATOM   2227  C CZ  . ARG B  2 85  ? 60.645  -7.101   13.092  1.000 83.696  0 85  ARG BBB CZ  1 ? 6  
ATOM   2228  N NH1 . ARG B  2 85  ? 60.635  -8.309   13.631  1.000 82.806  0 85  ARG BBB NH1 1 ? 6  
ATOM   2229  N NH2 . ARG B  2 85  ? 59.910  -6.859   12.018  1.000 82.490  0 85  ARG BBB NH2 1 ? 6  
ATOM   2230  N N   . LEU B  2 86  ? 57.520  -4.996   19.088  1.000 74.033  0 86  LEU BBB N   1 ? 6  
ATOM   2231  C CA  . LEU B  2 86  ? 56.341  -4.250   19.592  1.000 74.283  0 86  LEU BBB CA  1 ? 6  
ATOM   2232  C C   . LEU B  2 86  ? 56.735  -2.804   19.882  1.000 78.011  0 86  LEU BBB C   1 ? 6  
ATOM   2233  O O   . LEU B  2 86  ? 57.836  -2.571   20.407  1.000 81.169  0 86  LEU BBB O   1 ? 6  
ATOM   2234  C CB  . LEU B  2 86  ? 55.799  -4.946   20.841  1.000 73.567  0 86  LEU BBB CB  1 ? 6  
ATOM   2235  C CG  . LEU B  2 86  ? 55.010  -6.217   20.563  1.000 70.948  0 86  LEU BBB CG  1 ? 6  
ATOM   2236  C CD1 . LEU B  2 86  ? 54.864  -7.038   21.839  1.000 72.125  0 86  LEU BBB CD1 1 ? 6  
ATOM   2237  C CD2 . LEU B  2 86  ? 53.653  -5.882   19.974  1.000 68.197  0 86  LEU BBB CD2 1 ? 6  
ATOM   2238  N N   . LYS B  2 87  ? 55.837  -1.878   19.550  1.000 79.781  0 87  LYS BBB N   1 ? 6  
ATOM   2239  C CA  . LYS B  2 87  ? 55.987  -0.414   19.765  1.000 83.812  0 87  LYS BBB CA  1 ? 6  
ATOM   2240  C C   . LYS B  2 87  ? 54.888  0.024    20.728  1.000 81.199  0 87  LYS BBB C   1 ? 6  
ATOM   2241  O O   . LYS B  2 87  ? 53.875  -0.659   20.859  1.000 78.031  0 87  LYS BBB O   1 ? 6  
ATOM   2242  C CB  . LYS B  2 87  ? 55.881  0.317    18.421  1.000 88.005  0 87  LYS BBB CB  1 ? 6  
ATOM   2243  C CG  . LYS B  2 87  ? 56.577  -0.391   17.261  1.000 90.344  0 87  LYS BBB CG  1 ? 6  
ATOM   2244  C CD  . LYS B  2 87  ? 56.329  0.157    15.881  1.000 92.700  0 87  LYS BBB CD  1 ? 6  
ATOM   2245  C CE  . LYS B  2 87  ? 57.309  -0.476   14.911  1.000 96.735  0 87  LYS BBB CE  1 ? 6  
ATOM   2246  N NZ  . LYS B  2 87  ? 57.234  0.065    13.538  1.000 99.035  0 87  LYS BBB NZ  1 ? 6  
ATOM   2247  N N   . PRO B  2 88  ? 55.061  1.148    21.459  1.000 82.025  0 88  PRO BBB N   1 ? 6  
ATOM   2248  C CA  . PRO B  2 88  ? 54.003  1.675    22.324  1.000 80.715  0 88  PRO BBB CA  1 ? 6  
ATOM   2249  C C   . PRO B  2 88  ? 52.623  1.784    21.665  1.000 77.386  0 88  PRO BBB C   1 ? 6  
ATOM   2250  O O   . PRO B  2 88  ? 51.670  1.486    22.336  1.000 75.193  0 88  PRO BBB O   1 ? 6  
ATOM   2251  C CB  . PRO B  2 88  ? 54.570  3.043    22.726  1.000 83.733  0 88  PRO BBB CB  1 ? 6  
ATOM   2252  C CG  . PRO B  2 88  ? 56.045  2.749    22.832  1.000 85.881  0 88  PRO BBB CG  1 ? 6  
ATOM   2253  C CD  . PRO B  2 88  ? 56.312  1.904    21.602  1.000 84.441  0 88  PRO BBB CD  1 ? 6  
ATOM   2254  N N   . GLU B  2 89  ? 52.564  2.135    20.376  1.000 79.266  0 89  GLU BBB N   1 ? 6  
ATOM   2255  C CA  . GLU B  2 89  ? 51.310  2.298    19.582  1.000 79.095  0 89  GLU BBB CA  1 ? 6  
ATOM   2256  C C   . GLU B  2 89  ? 50.572  0.962    19.436  1.000 74.463  0 89  GLU BBB C   1 ? 6  
ATOM   2257  O O   . GLU B  2 89  ? 49.467  0.995    18.888  1.000 72.513  0 89  GLU BBB O   1 ? 6  
ATOM   2258  C CB  . GLU B  2 89  ? 51.571  2.804    18.158  1.000 81.430  0 89  GLU BBB CB  1 ? 6  
ATOM   2259  C CG  . GLU B  2 89  ? 52.434  4.048    18.078  1.000 88.188  0 89  GLU BBB CG  1 ? 6  
ATOM   2260  C CD  . GLU B  2 89  ? 53.938  3.778    18.056  1.000 92.116  0 89  GLU BBB CD  1 ? 6  
ATOM   2261  O OE1 . GLU B  2 89  ? 54.345  2.843    17.303  1.000 94.318  0 89  GLU BBB OE1 1 ? 6  
ATOM   2262  O OE2 . GLU B  2 89  ? 54.696  4.479    18.800  1.000 90.068  0 89  GLU BBB OE2 1 ? 6  
ATOM   2263  N N   . ASP B  2 90  ? 51.186  -0.167   19.821  1.000 72.980  0 90  ASP BBB N   1 ? 6  
ATOM   2264  C CA  . ASP B  2 90  ? 50.564  -1.521   19.758  1.000 69.929  0 90  ASP BBB CA  1 ? 6  
ATOM   2265  C C   . ASP B  2 90  ? 49.786  -1.804   21.047  1.000 68.314  0 90  ASP BBB C   1 ? 6  
ATOM   2266  O O   . ASP B  2 90  ? 49.065  -2.821   21.094  1.000 66.493  0 90  ASP BBB O   1 ? 6  
ATOM   2267  C CB  . ASP B  2 90  ? 51.610  -2.612   19.533  1.000 69.884  0 90  ASP BBB CB  1 ? 6  
ATOM   2268  C CG  . ASP B  2 90  ? 52.284  -2.539   18.169  1.000 72.085  0 90  ASP BBB CG  1 ? 6  
ATOM   2269  O OD1 . ASP B  2 90  ? 51.566  -2.331   17.158  1.000 71.179  0 90  ASP BBB OD1 1 ? 6  
ATOM   2270  O OD2 . ASP B  2 90  ? 53.523  -2.689   18.125  1.000 72.348  0 90  ASP BBB OD2 1 ? 6  
ATOM   2271  N N   . THR B  2 91  ? 49.938  -0.964   22.071  1.000 68.884  0 91  THR BBB N   1 ? 6  
ATOM   2272  C CA  . THR B  2 91  ? 49.197  -1.085   23.352  1.000 66.855  0 91  THR BBB CA  1 ? 6  
ATOM   2273  C C   . THR B  2 91  ? 47.702  -0.995   23.056  1.000 63.714  0 91  THR BBB C   1 ? 6  
ATOM   2274  O O   . THR B  2 91  ? 47.283  -0.017   22.427  1.000 64.207  0 91  THR BBB O   1 ? 6  
ATOM   2275  C CB  . THR B  2 91  ? 49.633  -0.002   24.342  1.000 68.973  0 91  THR BBB CB  1 ? 6  
ATOM   2276  O OG1 . THR B  2 91  ? 50.988  -0.299   24.670  1.000 70.197  0 91  THR BBB OG1 1 ? 6  
ATOM   2277  C CG2 . THR B  2 91  ? 48.778  0.040    25.587  1.000 68.827  0 91  THR BBB CG2 1 ? 6  
ATOM   2278  N N   . ALA B  2 92  ? 46.932  -1.986   23.490  1.000 61.796  0 92  ALA BBB N   1 ? 6  
ATOM   2279  C CA  . ALA B  2 92  ? 45.473  -2.056   23.268  1.000 60.253  0 92  ALA BBB CA  1 ? 6  
ATOM   2280  C C   . ALA B  2 92  ? 44.893  -3.312   23.909  1.000 58.650  0 92  ALA BBB C   1 ? 6  
ATOM   2281  O O   . ALA B  2 92  ? 45.661  -4.175   24.340  1.000 57.932  0 92  ALA BBB O   1 ? 6  
ATOM   2282  C CB  . ALA B  2 92  ? 45.151  -2.045   21.795  1.000 59.136  0 92  ALA BBB CB  1 ? 6  
ATOM   2283  N N   . VAL B  2 93  ? 43.568  -3.393   23.936  1.000 58.204  0 93  VAL BBB N   1 ? 6  
ATOM   2284  C CA  . VAL B  2 93  ? 42.832  -4.655   24.183  1.000 55.752  0 93  VAL BBB CA  1 ? 6  
ATOM   2285  C C   . VAL B  2 93  ? 42.815  -5.393   22.850  1.000 54.268  0 93  VAL BBB C   1 ? 6  
ATOM   2286  O O   . VAL B  2 93  ? 42.418  -4.775   21.837  1.000 54.805  0 93  VAL BBB O   1 ? 6  
ATOM   2287  C CB  . VAL B  2 93  ? 41.418  -4.388   24.724  1.000 56.216  0 93  VAL BBB CB  1 ? 6  
ATOM   2288  C CG1 . VAL B  2 93  ? 40.624  -5.691   24.870  1.000 55.775  0 93  VAL BBB CG1 1 ? 6  
ATOM   2289  C CG2 . VAL B  2 93  ? 41.453  -3.618   26.033  1.000 56.423  0 93  VAL BBB CG2 1 ? 6  
ATOM   2290  N N   . TYR B  2 94  ? 43.270  -6.646   22.853  1.000 53.263  0 94  TYR BBB N   1 ? 6  
ATOM   2291  C CA  . TYR B  2 94  ? 43.304  -7.523   21.659  1.000 51.204  0 94  TYR BBB CA  1 ? 6  
ATOM   2292  C C   . TYR B  2 94  ? 42.141  -8.505   21.777  1.000 49.058  0 94  TYR BBB C   1 ? 6  
ATOM   2293  O O   . TYR B  2 94  ? 42.055  -9.197   22.811  1.000 48.015  0 94  TYR BBB O   1 ? 6  
ATOM   2294  C CB  . TYR B  2 94  ? 44.667  -8.199   21.511  1.000 49.962  0 94  TYR BBB CB  1 ? 6  
ATOM   2295  C CG  . TYR B  2 94  ? 45.736  -7.289   20.962  1.000 51.458  0 94  TYR BBB CG  1 ? 6  
ATOM   2296  C CD1 . TYR B  2 94  ? 46.281  -6.280   21.734  1.000 51.993  0 94  TYR BBB CD1 1 ? 6  
ATOM   2297  C CD2 . TYR B  2 94  ? 46.173  -7.406   19.652  1.000 51.313  0 94  TYR BBB CD2 1 ? 6  
ATOM   2298  C CE1 . TYR B  2 94  ? 47.257  -5.429   21.237  1.000 53.700  0 94  TYR BBB CE1 1 ? 6  
ATOM   2299  C CE2 . TYR B  2 94  ? 47.152  -6.566   19.140  1.000 54.521  0 94  TYR BBB CE2 1 ? 6  
ATOM   2300  C CZ  . TYR B  2 94  ? 47.693  -5.561   19.934  1.000 54.615  0 94  TYR BBB CZ  1 ? 6  
ATOM   2301  O OH  . TYR B  2 94  ? 48.649  -4.722   19.429  1.000 55.152  0 94  TYR BBB OH  1 ? 6  
ATOM   2302  N N   . PHE B  2 95  ? 41.269  -8.498   20.760  1.000 47.695  0 95  PHE BBB N   1 ? 6  
ATOM   2303  C CA  . PHE B  2 95  ? 40.073  -9.355   20.662  1.000 46.419  0 95  PHE BBB CA  1 ? 6  
ATOM   2304  C C   . PHE B  2 95  ? 40.288  -10.437  19.606  1.000 47.052  0 95  PHE BBB C   1 ? 6  
ATOM   2305  O O   . PHE B  2 95  ? 40.685  -10.164  18.462  1.000 45.637  0 95  PHE BBB O   1 ? 6  
ATOM   2306  C CB  . PHE B  2 95  ? 38.842  -8.557   20.264  1.000 46.488  0 95  PHE BBB CB  1 ? 6  
ATOM   2307  C CG  . PHE B  2 95  ? 38.417  -7.503   21.246  1.000 46.572  0 95  PHE BBB CG  1 ? 6  
ATOM   2308  C CD1 . PHE B  2 95  ? 38.929  -6.220   21.150  1.000 48.852  0 95  PHE BBB CD1 1 ? 6  
ATOM   2309  C CD2 . PHE B  2 95  ? 37.479  -7.774   22.228  1.000 46.897  0 95  PHE BBB CD2 1 ? 6  
ATOM   2310  C CE1 . PHE B  2 95  ? 38.518  -5.226   22.034  1.000 50.229  0 95  PHE BBB CE1 1 ? 6  
ATOM   2311  C CE2 . PHE B  2 95  ? 37.084  -6.792   23.131  1.000 47.472  0 95  PHE BBB CE2 1 ? 6  
ATOM   2312  C CZ  . PHE B  2 95  ? 37.608  -5.519   23.034  1.000 48.700  0 95  PHE BBB CZ  1 ? 6  
ATOM   2313  N N   . CYS B  2 96  ? 39.985  -11.659  20.009  1.000 48.369  0 96  CYS BBB N   1 ? 6  
ATOM   2314  C CA  . CYS B  2 96  ? 39.810  -12.838  19.145  1.000 46.480  0 96  CYS BBB CA  1 ? 6  
ATOM   2315  C C   . CYS B  2 96  ? 38.429  -12.735  18.484  1.000 43.656  0 96  CYS BBB C   1 ? 6  
ATOM   2316  O O   . CYS B  2 96  ? 37.461  -12.336  19.174  1.000 41.543  0 96  CYS BBB O   1 ? 6  
ATOM   2317  C CB  . CYS B  2 96  ? 39.903  -14.077  20.021  1.000 49.107  0 96  CYS BBB CB  1 ? 6  
ATOM   2318  S SG  . CYS B  2 96  ? 39.847  -15.619  19.073  1.000 60.546  0 96  CYS BBB SG  1 ? 6  
ATOM   2319  N N   . ALA B  2 97  ? 38.313  -13.076  17.204  1.000 39.730  0 97  ALA BBB N   1 ? 6  
ATOM   2320  C CA  . ALA B  2 97  ? 36.992  -13.150  16.547  1.000 40.881  0 97  ALA BBB CA  1 ? 6  
ATOM   2321  C C   . ALA B  2 97  ? 36.942  -14.349  15.600  1.000 40.813  0 97  ALA BBB C   1 ? 6  
ATOM   2322  O O   . ALA B  2 97  ? 38.021  -14.832  15.170  1.000 43.040  0 97  ALA BBB O   1 ? 6  
ATOM   2323  C CB  . ALA B  2 97  ? 36.677  -11.856  15.839  1.000 41.518  0 97  ALA BBB CB  1 ? 6  
ATOM   2324  N N   . ALA B  2 98  ? 35.729  -14.807  15.289  1.000 39.840  0 98  ALA BBB N   1 ? 6  
ATOM   2325  C CA  . ALA B  2 98  ? 35.493  -15.993  14.444  1.000 39.922  0 98  ALA BBB CA  1 ? 6  
ATOM   2326  C C   . ALA B  2 98  ? 34.212  -15.808  13.628  1.000 40.423  0 98  ALA BBB C   1 ? 6  
ATOM   2327  O O   . ALA B  2 98  ? 33.228  -15.220  14.139  1.000 40.424  0 98  ALA BBB O   1 ? 6  
ATOM   2328  C CB  . ALA B  2 98  ? 35.410  -17.224  15.307  1.000 40.498  0 98  ALA BBB CB  1 ? 6  
ATOM   2329  N N   . ASP B  2 99  ? 34.215  -16.379  12.424  1.000 40.713  0 99  ASP BBB N   1 ? 6  
ATOM   2330  C CA  . ASP B  2 99  ? 33.033  -16.442  11.531  1.000 39.905  0 99  ASP BBB CA  1 ? 6  
ATOM   2331  C C   . ASP B  2 99  ? 33.157  -17.636  10.588  1.000 38.420  0 99  ASP BBB C   1 ? 6  
ATOM   2332  O O   . ASP B  2 99  ? 34.305  -17.991  10.230  1.000 35.587  0 99  ASP BBB O   1 ? 6  
ATOM   2333  C CB  . ASP B  2 99  ? 32.865  -15.161  10.730  1.000 39.620  0 99  ASP BBB CB  1 ? 6  
ATOM   2334  C CG  . ASP B  2 99  ? 31.432  -14.974  10.302  1.000 39.906  0 99  ASP BBB CG  1 ? 6  
ATOM   2335  O OD1 . ASP B  2 99  ? 30.629  -14.530  11.162  1.000 38.562  0 99  ASP BBB OD1 1 ? 6  
ATOM   2336  O OD2 . ASP B  2 99  ? 31.124  -15.323  9.120   1.000 41.462  0 99  ASP BBB OD2 1 ? 6  
ATOM   2337  N N   . ARG B  2 100 ? 32.011  -18.226  10.198  1.000 36.660  0 100 ARG BBB N   1 ? 6  
ATOM   2338  C CA  . ARG B  2 100 ? 32.007  -19.306  9.185   1.000 38.554  0 100 ARG BBB CA  1 ? 6  
ATOM   2339  C C   . ARG B  2 100 ? 32.521  -18.774  7.838   1.000 38.335  0 100 ARG BBB C   1 ? 6  
ATOM   2340  O O   . ARG B  2 100 ? 33.141  -19.525  7.105   1.000 38.767  0 100 ARG BBB O   1 ? 6  
ATOM   2341  C CB  . ARG B  2 100 ? 30.581  -19.826  9.017   1.000 40.675  0 100 ARG BBB CB  1 ? 6  
ATOM   2342  C CG  . ARG B  2 100 ? 30.114  -20.724  10.149  1.000 44.577  0 100 ARG BBB CG  1 ? 6  
ATOM   2343  C CD  . ARG B  2 100 ? 30.847  -22.036  10.312  1.000 43.145  0 100 ARG BBB CD  1 ? 6  
ATOM   2344  N NE  . ARG B  2 100 ? 31.044  -22.684  9.026   1.000 42.140  0 100 ARG BBB NE  1 ? 6  
ATOM   2345  C CZ  . ARG B  2 100 ? 30.222  -23.580  8.468   1.000 44.704  0 100 ARG BBB CZ  1 ? 6  
ATOM   2346  N NH1 . ARG B  2 100 ? 29.099  -23.957  9.064   1.000 43.922  0 100 ARG BBB NH1 1 ? 6  
ATOM   2347  N NH2 . ARG B  2 100 ? 30.525  -24.086  7.284   1.000 43.621  0 100 ARG BBB NH2 1 ? 6  
ATOM   2348  N N   . GLY B  2 101 ? 32.232  -17.510  7.540   1.000 38.127  0 101 GLY BBB N   1 ? 6  
ATOM   2349  C CA  . GLY B  2 101 ? 32.491  -16.884  6.245   1.000 39.159  0 101 GLY BBB CA  1 ? 6  
ATOM   2350  C C   . GLY B  2 101 ? 33.788  -16.108  6.254   1.000 40.684  0 101 GLY BBB C   1 ? 6  
ATOM   2351  O O   . GLY B  2 101 ? 34.125  -15.497  7.286   1.000 40.060  0 101 GLY BBB O   1 ? 6  
ATOM   2352  N N   . GLU B  2 102 ? 34.480  -16.135  5.106   1.000 41.437  0 102 GLU BBB N   1 ? 6  
ATOM   2353  C CA  . GLU B  2 102 ? 35.606  -15.230  4.789   1.000 41.960  0 102 GLU BBB CA  1 ? 6  
ATOM   2354  C C   . GLU B  2 102 ? 35.041  -14.049  4.003   1.000 40.263  0 102 GLU BBB C   1 ? 6  
ATOM   2355  O O   . GLU B  2 102 ? 34.431  -14.287  2.948   1.000 40.826  0 102 GLU BBB O   1 ? 6  
ATOM   2356  C CB  . GLU B  2 102 ? 36.651  -16.003  4.002   1.000 44.376  0 102 GLU BBB CB  1 ? 6  
ATOM   2357  C CG  . GLU B  2 102 ? 37.912  -15.208  3.728   1.000 45.856  0 102 GLU BBB CG  1 ? 6  
ATOM   2358  C CD  . GLU B  2 102 ? 38.957  -15.977  2.945   1.000 46.960  0 102 GLU BBB CD  1 ? 6  
ATOM   2359  O OE1 . GLU B  2 102 ? 38.903  -17.215  2.928   1.000 50.805  0 102 GLU BBB OE1 1 ? 6  
ATOM   2360  O OE2 . GLU B  2 102 ? 39.781  -15.331  2.318   1.000 51.872  0 102 GLU BBB OE2 1 ? 6  
ATOM   2361  N N   . SER B  2 103 ? 35.222  -12.836  4.518   1.000 39.251  0 103 SER BBB N   1 ? 6  
ATOM   2362  C CA  . SER B  2 103 ? 34.635  -11.594  3.963   1.000 38.176  0 103 SER BBB CA  1 ? 6  
ATOM   2363  C C   . SER B  2 103 ? 35.582  -10.974  2.932   1.000 38.731  0 103 SER BBB C   1 ? 6  
ATOM   2364  O O   . SER B  2 103 ? 36.793  -10.886  3.179   1.000 38.331  0 103 SER BBB O   1 ? 6  
ATOM   2365  C CB  . SER B  2 103 ? 34.286  -10.597  5.055   1.000 37.010  0 103 SER BBB CB  1 ? 6  
ATOM   2366  O OG  . SER B  2 103 ? 33.734  -9.434   4.487   1.000 37.252  0 103 SER BBB OG  1 ? 6  
ATOM   2367  N N   . TYR B  2 104 ? 35.024  -10.489  1.831   1.000 39.114  0 104 TYR BBB N   1 ? 6  
ATOM   2368  C CA  . TYR B  2 104 ? 35.733  -9.543   0.951   1.000 38.635  0 104 TYR BBB CA  1 ? 6  
ATOM   2369  C C   . TYR B  2 104 ? 36.135  -8.335   1.798   1.000 39.593  0 104 TYR BBB C   1 ? 6  
ATOM   2370  O O   . TYR B  2 104 ? 37.222  -7.812   1.548   1.000 42.293  0 104 TYR BBB O   1 ? 6  
ATOM   2371  C CB  . TYR B  2 104 ? 34.876  -9.122   -0.239  1.000 39.452  0 104 TYR BBB CB  1 ? 6  
ATOM   2372  C CG  . TYR B  2 104 ? 35.596  -8.172   -1.168  1.000 39.964  0 104 TYR BBB CG  1 ? 6  
ATOM   2373  C CD1 . TYR B  2 104 ? 36.687  -8.596   -1.909  1.000 39.759  0 104 TYR BBB CD1 1 ? 6  
ATOM   2374  C CD2 . TYR B  2 104 ? 35.231  -6.840   -1.262  1.000 42.415  0 104 TYR BBB CD2 1 ? 6  
ATOM   2375  C CE1 . TYR B  2 104 ? 37.391  -7.733   -2.723  1.000 40.696  0 104 TYR BBB CE1 1 ? 6  
ATOM   2376  C CE2 . TYR B  2 104 ? 35.919  -5.959   -2.089  1.000 43.450  0 104 TYR BBB CE2 1 ? 6  
ATOM   2377  C CZ  . TYR B  2 104 ? 37.001  -6.411   -2.818  1.000 42.943  0 104 TYR BBB CZ  1 ? 6  
ATOM   2378  O OH  . TYR B  2 104 ? 37.677  -5.547   -3.625  1.000 46.258  0 104 TYR BBB OH  1 ? 6  
ATOM   2379  N N   . TYR B  2 105 ? 35.281  -7.904   2.736   1.000 40.085  0 105 TYR BBB N   1 ? 7  
ATOM   2380  C CA  . TYR B  2 105 ? 35.511  -6.741   3.625   1.000 40.848  0 105 TYR BBB CA  1 ? 7  
ATOM   2381  C C   . TYR B  2 105 ? 36.047  -7.260   4.981   1.000 41.542  0 105 TYR BBB C   1 ? 7  
ATOM   2382  O O   . TYR B  2 105 ? 35.439  -7.009   6.058   1.000 41.255  0 105 TYR BBB O   1 ? 7  
ATOM   2383  C CB  . TYR B  2 105 ? 34.223  -5.925   3.760   1.000 40.352  0 105 TYR BBB CB  1 ? 7  
ATOM   2384  C CG  . TYR B  2 105 ? 33.518  -5.531   2.481   1.000 42.678  0 105 TYR BBB CG  1 ? 7  
ATOM   2385  C CD1 . TYR B  2 105 ? 34.059  -4.598   1.605   1.000 41.929  0 105 TYR BBB CD1 1 ? 7  
ATOM   2386  C CD2 . TYR B  2 105 ? 32.266  -6.044   2.164   1.000 41.493  0 105 TYR BBB CD2 1 ? 7  
ATOM   2387  C CE1 . TYR B  2 105 ? 33.395  -4.213   0.453   1.000 42.526  0 105 TYR BBB CE1 1 ? 7  
ATOM   2388  C CE2 . TYR B  2 105 ? 31.601  -5.681   1.004   1.000 41.614  0 105 TYR BBB CE2 1 ? 7  
ATOM   2389  C CZ  . TYR B  2 105 ? 32.152  -4.747   0.152   1.000 43.294  0 105 TYR BBB CZ  1 ? 7  
ATOM   2390  O OH  . TYR B  2 105 ? 31.452  -4.392   -0.973  1.000 44.986  0 105 TYR BBB OH  1 ? 7  
ATOM   2391  N N   . TYR B  2 106 ? 37.167  -7.977   4.948   1.000 41.534  0 106 TYR BBB N   1 ? 7  
ATOM   2392  C CA  . TYR B  2 106 ? 37.699  -8.756   6.106   1.000 41.774  0 106 TYR BBB CA  1 ? 7  
ATOM   2393  C C   . TYR B  2 106 ? 38.085  -7.852   7.282   1.000 42.673  0 106 TYR BBB C   1 ? 7  
ATOM   2394  O O   . TYR B  2 106 ? 38.275  -8.406   8.372   1.000 44.014  0 106 TYR BBB O   1 ? 7  
ATOM   2395  C CB  . TYR B  2 106 ? 38.911  -9.604   5.707   1.000 43.536  0 106 TYR BBB CB  1 ? 7  
ATOM   2396  C CG  . TYR B  2 106 ? 40.025  -8.830   5.065   1.000 44.414  0 106 TYR BBB CG  1 ? 7  
ATOM   2397  C CD1 . TYR B  2 106 ? 40.961  -8.143   5.827   1.000 44.921  0 106 TYR BBB CD1 1 ? 7  
ATOM   2398  C CD2 . TYR B  2 106 ? 40.145  -8.802   3.680   1.000 45.721  0 106 TYR BBB CD2 1 ? 7  
ATOM   2399  C CE1 . TYR B  2 106 ? 41.981  -7.430   5.229   1.000 46.672  0 106 TYR BBB CE1 1 ? 7  
ATOM   2400  C CE2 . TYR B  2 106 ? 41.141  -8.070   3.065   1.000 46.207  0 106 TYR BBB CE2 1 ? 7  
ATOM   2401  C CZ  . TYR B  2 106 ? 42.057  -7.384   3.846   1.000 48.503  0 106 TYR BBB CZ  1 ? 7  
ATOM   2402  O OH  . TYR B  2 106 ? 43.036  -6.679   3.225   1.000 52.019  0 106 TYR BBB OH  1 ? 7  
ATOM   2403  N N   . THR B  2 107 ? 38.226  -6.534   7.080   1.000 41.833  0 107 THR BBB N   1 ? 7  
ATOM   2404  C CA  . THR B  2 107 ? 38.583  -5.579   8.160   1.000 41.166  0 107 THR BBB CA  1 ? 7  
ATOM   2405  C C   . THR B  2 107 ? 37.334  -5.113   8.923   1.000 41.354  0 107 THR BBB C   1 ? 7  
ATOM   2406  O O   . THR B  2 107 ? 37.499  -4.454   9.949   1.000 42.958  0 107 THR BBB O   1 ? 7  
ATOM   2407  C CB  . THR B  2 107 ? 39.370  -4.356   7.653   1.000 41.022  0 107 THR BBB CB  1 ? 7  
ATOM   2408  O OG1 . THR B  2 107 ? 38.487  -3.490   6.954   1.000 40.912  0 107 THR BBB OG1 1 ? 7  
ATOM   2409  C CG2 . THR B  2 107 ? 40.534  -4.729   6.766   1.000 41.032  0 107 THR BBB CG2 1 ? 7  
ATOM   2410  N N   . ARG B  2 108 ? 36.124  -5.406   8.449   1.000 41.455  0 108 ARG BBB N   1 ? 7  
ATOM   2411  C CA  . ARG B  2 108 ? 34.889  -4.945   9.133   1.000 42.742  0 108 ARG BBB CA  1 ? 7  
ATOM   2412  C C   . ARG B  2 108 ? 34.556  -5.825   10.338  1.000 42.844  0 108 ARG BBB C   1 ? 7  
ATOM   2413  O O   . ARG B  2 108 ? 34.356  -7.029   10.217  1.000 41.274  0 108 ARG BBB O   1 ? 7  
ATOM   2414  C CB  . ARG B  2 108 ? 33.690  -5.017   8.196   1.000 44.446  0 108 ARG BBB CB  1 ? 7  
ATOM   2415  C CG  . ARG B  2 108 ? 33.679  -4.006   7.064   1.000 45.110  0 108 ARG BBB CG  1 ? 7  
ATOM   2416  C CD  . ARG B  2 108 ? 32.315  -4.102   6.415   1.000 44.388  0 108 ARG BBB CD  1 ? 7  
ATOM   2417  N NE  . ARG B  2 108 ? 32.286  -3.362   5.178   1.000 45.143  0 108 ARG BBB NE  1 ? 7  
ATOM   2418  C CZ  . ARG B  2 108 ? 31.315  -3.418   4.283   1.000 44.551  0 108 ARG BBB CZ  1 ? 7  
ATOM   2419  N NH1 . ARG B  2 108 ? 30.273  -4.212   4.447   1.000 43.586  0 108 ARG BBB NH1 1 ? 7  
ATOM   2420  N NH2 . ARG B  2 108 ? 31.403  -2.680   3.201   1.000 46.341  0 108 ARG BBB NH2 1 ? 7  
ATOM   2421  N N   . PRO B  2 109 ? 34.465  -5.249   11.553  1.000 44.303  0 109 PRO BBB N   1 ? 7  
ATOM   2422  C CA  . PRO B  2 109 ? 33.990  -5.994   12.723  1.000 42.610  0 109 PRO BBB CA  1 ? 7  
ATOM   2423  C C   . PRO B  2 109 ? 32.651  -6.714   12.520  1.000 41.262  0 109 PRO BBB C   1 ? 7  
ATOM   2424  O O   . PRO B  2 109 ? 32.516  -7.825   12.979  1.000 40.766  0 109 PRO BBB O   1 ? 7  
ATOM   2425  C CB  . PRO B  2 109 ? 33.884  -4.916   13.806  1.000 42.495  0 109 PRO BBB CB  1 ? 7  
ATOM   2426  C CG  . PRO B  2 109 ? 34.916  -3.913   13.409  1.000 43.798  0 109 PRO BBB CG  1 ? 7  
ATOM   2427  C CD  . PRO B  2 109 ? 34.901  -3.886   11.892  1.000 44.139  0 109 PRO BBB CD  1 ? 7  
ATOM   2428  N N   . THR B  2 110 ? 31.705  -6.084   11.819  1.000 42.381  0 110 THR BBB N   1 ? 7  
ATOM   2429  C CA  . THR B  2 110 ? 30.328  -6.613   11.576  1.000 40.677  0 110 THR BBB CA  1 ? 7  
ATOM   2430  C C   . THR B  2 110 ? 30.384  -7.909   10.754  1.000 40.120  0 110 THR BBB C   1 ? 7  
ATOM   2431  O O   . THR B  2 110 ? 29.386  -8.619   10.769  1.000 41.341  0 110 THR BBB O   1 ? 7  
ATOM   2432  C CB  . THR B  2 110 ? 29.428  -5.561   10.925  1.000 40.611  0 110 THR BBB CB  1 ? 7  
ATOM   2433  O OG1 . THR B  2 110 ? 30.049  -5.084   9.730   1.000 41.071  0 110 THR BBB OG1 1 ? 7  
ATOM   2434  C CG2 . THR B  2 110 ? 29.179  -4.382   11.838  1.000 42.048  0 110 THR BBB CG2 1 ? 7  
ATOM   2435  N N   . GLU B  2 111 ? 31.493  -8.220   10.070  1.000 39.620  0 111 GLU BBB N   1 ? 7  
ATOM   2436  C CA  . GLU B  2 111 ? 31.621  -9.461   9.267   1.000 41.731  0 111 GLU BBB CA  1 ? 7  
ATOM   2437  C C   . GLU B  2 111 ? 32.001  -10.660  10.161  1.000 41.902  0 111 GLU BBB C   1 ? 7  
ATOM   2438  O O   . GLU B  2 111 ? 32.078  -11.777  9.627   1.000 40.852  0 111 GLU BBB O   1 ? 7  
ATOM   2439  C CB  . GLU B  2 111 ? 32.632  -9.259   8.139   1.000 40.893  0 111 GLU BBB CB  1 ? 7  
ATOM   2440  C CG  . GLU B  2 111 ? 32.140  -8.340   7.043   1.000 42.643  0 111 GLU BBB CG  1 ? 7  
ATOM   2441  C CD  . GLU B  2 111 ? 30.983  -8.854   6.197   1.000 43.438  0 111 GLU BBB CD  1 ? 7  
ATOM   2442  O OE1 . GLU B  2 111 ? 29.847  -8.898   6.748   1.000 42.273  0 111 GLU BBB OE1 1 ? 7  
ATOM   2443  O OE2 . GLU B  2 111 ? 31.201  -9.237   4.999   1.000 42.513  0 111 GLU BBB OE2 1 ? 7  
ATOM   2444  N N   . TYR B  2 112 ? 32.230  -10.467  11.462  1.000 41.665  0 112 TYR BBB N   1 ? 7  
ATOM   2445  C CA  . TYR B  2 112 ? 32.579  -11.566  12.404  1.000 41.481  0 112 TYR BBB CA  1 ? 7  
ATOM   2446  C C   . TYR B  2 112 ? 31.487  -11.708  13.467  1.000 40.702  0 112 TYR BBB C   1 ? 7  
ATOM   2447  O O   . TYR B  2 112 ? 31.219  -10.774  14.201  1.000 38.599  0 112 TYR BBB O   1 ? 7  
ATOM   2448  C CB  . TYR B  2 112 ? 33.968  -11.317  12.990  1.000 40.317  0 112 TYR BBB CB  1 ? 7  
ATOM   2449  C CG  . TYR B  2 112 ? 35.045  -11.200  11.941  1.000 41.853  0 112 TYR BBB CG  1 ? 7  
ATOM   2450  C CD1 . TYR B  2 112 ? 35.284  -10.002  11.297  1.000 42.012  0 112 TYR BBB CD1 1 ? 7  
ATOM   2451  C CD2 . TYR B  2 112 ? 35.795  -12.298  11.550  1.000 41.799  0 112 TYR BBB CD2 1 ? 7  
ATOM   2452  C CE1 . TYR B  2 112 ? 36.252  -9.889   10.319  1.000 41.430  0 112 TYR BBB CE1 1 ? 7  
ATOM   2453  C CE2 . TYR B  2 112 ? 36.768  -12.200  10.572  1.000 42.904  0 112 TYR BBB CE2 1 ? 7  
ATOM   2454  C CZ  . TYR B  2 112 ? 37.011  -10.989  9.950   1.000 42.735  0 112 TYR BBB CZ  1 ? 7  
ATOM   2455  O OH  . TYR B  2 112 ? 37.972  -10.906  8.967   1.000 41.302  0 112 TYR BBB OH  1 ? 7  
ATOM   2456  N N   . GLU B  2 113 ? 30.839  -12.861  13.536  1.000 44.860  0 113 GLU BBB N   1 ? 7  
ATOM   2457  C CA  . GLU B  2 113 ? 29.701  -13.082  14.467  1.000 45.276  0 113 GLU BBB CA  1 ? 7  
ATOM   2458  C C   . GLU B  2 113 ? 30.190  -13.218  15.916  1.000 42.416  0 113 GLU BBB C   1 ? 7  
ATOM   2459  O O   . GLU B  2 113 ? 29.503  -12.713  16.806  1.000 39.787  0 113 GLU BBB O   1 ? 7  
ATOM   2460  C CB  . GLU B  2 113 ? 28.912  -14.323  14.085  1.000 48.929  0 113 GLU BBB CB  1 ? 7  
ATOM   2461  C CG  . GLU B  2 113 ? 27.693  -14.480  14.973  1.000 54.660  0 113 GLU BBB CG  1 ? 7  
ATOM   2462  C CD  . GLU B  2 113 ? 26.738  -15.590  14.613  1.000 58.051  0 113 GLU BBB CD  1 ? 7  
ATOM   2463  O OE1 . GLU B  2 113 ? 26.974  -16.234  13.556  1.000 56.719  0 113 GLU BBB OE1 1 ? 7  
ATOM   2464  O OE2 . GLU B  2 113 ? 25.784  -15.801  15.421  1.000 61.946  0 113 GLU BBB OE2 1 ? 7  
ATOM   2465  N N   . PHE B  2 114 ? 31.316  -13.899  16.149  1.000 40.149  0 114 PHE BBB N   1 ? 7  
ATOM   2466  C CA  . PHE B  2 114 ? 31.779  -14.302  17.502  1.000 39.669  0 114 PHE BBB CA  1 ? 7  
ATOM   2467  C C   . PHE B  2 114 ? 33.011  -13.500  17.913  1.000 39.778  0 114 PHE BBB C   1 ? 7  
ATOM   2468  O O   . PHE B  2 114 ? 33.955  -13.377  17.112  1.000 38.129  0 114 PHE BBB O   1 ? 7  
ATOM   2469  C CB  . PHE B  2 114 ? 32.061  -15.798  17.539  1.000 37.477  0 114 PHE BBB CB  1 ? 7  
ATOM   2470  C CG  . PHE B  2 114 ? 30.824  -16.594  17.232  1.000 37.510  0 114 PHE BBB CG  1 ? 7  
ATOM   2471  C CD1 . PHE B  2 114 ? 29.727  -16.522  18.090  1.000 37.273  0 114 PHE BBB CD1 1 ? 7  
ATOM   2472  C CD2 . PHE B  2 114 ? 30.728  -17.370  16.081  1.000 36.312  0 114 PHE BBB CD2 1 ? 7  
ATOM   2473  C CE1 . PHE B  2 114 ? 28.555  -17.208  17.797  1.000 37.165  0 114 PHE BBB CE1 1 ? 7  
ATOM   2474  C CE2 . PHE B  2 114 ? 29.564  -18.073  15.804  1.000 36.278  0 114 PHE BBB CE2 1 ? 7  
ATOM   2475  C CZ  . PHE B  2 114 ? 28.477  -17.988  16.662  1.000 37.259  0 114 PHE BBB CZ  1 ? 7  
ATOM   2476  N N   . TRP B  2 115 ? 32.976  -12.997  19.148  1.000 39.600  0 115 TRP BBB N   1 ? 7  
ATOM   2477  C CA  . TRP B  2 115 ? 34.032  -12.142  19.735  1.000 39.979  0 115 TRP BBB CA  1 ? 7  
ATOM   2478  C C   . TRP B  2 115 ? 34.396  -12.636  21.134  1.000 40.446  0 115 TRP BBB C   1 ? 7  
ATOM   2479  O O   . TRP B  2 115 ? 33.464  -12.825  21.961  1.000 41.460  0 115 TRP BBB O   1 ? 7  
ATOM   2480  C CB  . TRP B  2 115 ? 33.527  -10.697  19.789  1.000 41.281  0 115 TRP BBB CB  1 ? 7  
ATOM   2481  C CG  . TRP B  2 115 ? 33.413  -10.096  18.436  1.000 41.998  0 115 TRP BBB CG  1 ? 7  
ATOM   2482  C CD1 . TRP B  2 115 ? 32.395  -10.269  17.548  1.000 41.983  0 115 TRP BBB CD1 1 ? 7  
ATOM   2483  C CD2 . TRP B  2 115 ? 34.391  -9.281   17.781  1.000 42.908  0 115 TRP BBB CD2 1 ? 7  
ATOM   2484  N NE1 . TRP B  2 115 ? 32.670  -9.612   16.385  1.000 41.856  0 115 TRP BBB NE1 1 ? 7  
ATOM   2485  C CE2 . TRP B  2 115 ? 33.887  -9.001   16.495  1.000 43.374  0 115 TRP BBB CE2 1 ? 7  
ATOM   2486  C CE3 . TRP B  2 115 ? 35.624  -8.756   18.150  1.000 45.227  0 115 TRP BBB CE3 1 ? 7  
ATOM   2487  C CZ2 . TRP B  2 115 ? 34.573  -8.209   15.584  1.000 45.403  0 115 TRP BBB CZ2 1 ? 7  
ATOM   2488  C CZ3 . TRP B  2 115 ? 36.311  -7.969   17.248  1.000 47.761  0 115 TRP BBB CZ3 1 ? 7  
ATOM   2489  C CH2 . TRP B  2 115 ? 35.790  -7.707   15.980  1.000 48.026  0 115 TRP BBB CH2 1 ? 7  
ATOM   2490  N N   . GLY B  2 116 ? 35.688  -12.742  21.414  1.000 39.887  0 116 GLY BBB N   1 ? 7  
ATOM   2491  C CA  . GLY B  2 116 ? 36.190  -12.872  22.793  1.000 42.239  0 116 GLY BBB CA  1 ? 7  
ATOM   2492  C C   . GLY B  2 116 ? 35.970  -11.588  23.572  1.000 43.087  0 116 GLY BBB C   1 ? 7  
ATOM   2493  O O   . GLY B  2 116 ? 35.535  -10.571  22.946  1.000 42.032  0 116 GLY BBB O   1 ? 7  
ATOM   2494  N N   . GLN B  2 117 ? 36.255  -11.604  24.878  1.000 44.751  0 117 GLN BBB N   1 ? 7  
ATOM   2495  C CA  . GLN B  2 117 ? 36.083  -10.395  25.750  1.000 45.104  0 117 GLN BBB CA  1 ? 7  
ATOM   2496  C C   . GLN B  2 117 ? 37.324  -9.498   25.621  1.000 45.768  0 117 GLN BBB C   1 ? 7  
ATOM   2497  O O   . GLN B  2 117 ? 37.242  -8.332   26.024  1.000 46.038  0 117 GLN BBB O   1 ? 7  
ATOM   2498  C CB  . GLN B  2 117 ? 35.887  -10.784  27.213  1.000 44.938  0 117 GLN BBB CB  1 ? 7  
ATOM   2499  C CG  . GLN B  2 117 ? 34.741  -11.745  27.445  1.000 45.061  0 117 GLN BBB CG  1 ? 7  
ATOM   2500  C CD  . GLN B  2 117 ? 33.415  -11.153  27.038  1.000 45.327  0 117 GLN BBB CD  1 ? 7  
ATOM   2501  O OE1 . GLN B  2 117 ? 32.608  -11.796  26.373  1.000 47.165  0 117 GLN BBB OE1 1 ? 7  
ATOM   2502  N NE2 . GLN B  2 117 ? 33.157  -9.922   27.427  1.000 45.352  0 117 GLN BBB NE2 1 ? 7  
ATOM   2503  N N   . GLY B  2 118 ? 38.430  -10.036  25.083  1.000 46.468  0 118 GLY BBB N   1 ? 7  
ATOM   2504  C CA  . GLY B  2 118 ? 39.686  -9.295   24.859  1.000 48.896  0 118 GLY BBB CA  1 ? 7  
ATOM   2505  C C   . GLY B  2 118 ? 40.660  -9.454   26.012  1.000 51.757  0 118 GLY BBB C   1 ? 7  
ATOM   2506  O O   . GLY B  2 118 ? 40.230  -9.826   27.105  1.000 53.394  0 118 GLY BBB O   1 ? 7  
ATOM   2507  N N   . THR B  2 119 ? 41.938  -9.168   25.772  1.000 54.107  0 119 THR BBB N   1 ? 7  
ATOM   2508  C CA  . THR B  2 119 ? 43.033  -9.217   26.765  1.000 54.630  0 119 THR BBB CA  1 ? 7  
ATOM   2509  C C   . THR B  2 119 ? 43.925  -7.996   26.529  1.000 55.961  0 119 THR BBB C   1 ? 7  
ATOM   2510  O O   . THR B  2 119 ? 44.175  -7.660   25.362  1.000 54.811  0 119 THR BBB O   1 ? 7  
ATOM   2511  C CB  . THR B  2 119 ? 43.761  -10.564  26.682  1.000 56.451  0 119 THR BBB CB  1 ? 7  
ATOM   2512  O OG1 . THR B  2 119 ? 44.536  -10.703  27.878  1.000 57.832  0 119 THR BBB OG1 1 ? 7  
ATOM   2513  C CG2 . THR B  2 119 ? 44.608  -10.706  25.432  1.000 56.795  0 119 THR BBB CG2 1 ? 7  
ATOM   2514  N N   . GLN B  2 120 ? 44.366  -7.347   27.605  1.000 56.594  0 120 GLN BBB N   1 ? 7  
ATOM   2515  C CA  . GLN B  2 120 ? 45.231  -6.157   27.553  1.000 58.270  0 120 GLN BBB CA  1 ? 7  
ATOM   2516  C C   . GLN B  2 120 ? 46.642  -6.600   27.140  1.000 59.982  0 120 GLN BBB C   1 ? 7  
ATOM   2517  O O   . GLN B  2 120 ? 47.186  -7.555   27.733  1.000 63.717  0 120 GLN BBB O   1 ? 7  
ATOM   2518  C CB  . GLN B  2 120 ? 45.217  -5.451   28.910  1.000 60.658  0 120 GLN BBB CB  1 ? 7  
ATOM   2519  C CG  . GLN B  2 120 ? 45.945  -4.115   28.925  1.000 62.235  0 120 GLN BBB CG  1 ? 7  
ATOM   2520  C CD  . GLN B  2 120 ? 45.281  -3.091   28.036  1.000 61.795  0 120 GLN BBB CD  1 ? 7  
ATOM   2521  O OE1 . GLN B  2 120 ? 44.068  -2.880   28.100  1.000 60.920  0 120 GLN BBB OE1 1 ? 7  
ATOM   2522  N NE2 . GLN B  2 120 ? 46.082  -2.428   27.210  1.000 62.898  0 120 GLN BBB NE2 1 ? 7  
ATOM   2523  N N   . VAL B  2 121 ? 47.195  -5.924   26.140  1.000 58.600  0 121 VAL BBB N   1 ? 7  
ATOM   2524  C CA  . VAL B  2 121 ? 48.649  -5.873   25.849  1.000 62.005  0 121 VAL BBB CA  1 ? 7  
ATOM   2525  C C   . VAL B  2 121 ? 49.126  -4.452   26.143  1.000 63.712  0 121 VAL BBB C   1 ? 7  
ATOM   2526  O O   . VAL B  2 121 ? 48.528  -3.512   25.609  1.000 62.935  0 121 VAL BBB O   1 ? 7  
ATOM   2527  C CB  . VAL B  2 121 ? 48.927  -6.276   24.391  1.000 62.987  0 121 VAL BBB CB  1 ? 7  
ATOM   2528  C CG1 . VAL B  2 121 ? 50.402  -6.123   24.058  1.000 67.092  0 121 VAL BBB CG1 1 ? 7  
ATOM   2529  C CG2 . VAL B  2 121 ? 48.452  -7.701   24.104  1.000 62.288  0 121 VAL BBB CG2 1 ? 7  
ATOM   2530  N N   . THR B  2 122 ? 50.151  -4.296   26.976  1.000 66.122  0 122 THR BBB N   1 ? 7  
ATOM   2531  C CA  . THR B  2 122 ? 50.762  -2.975   27.289  1.000 69.720  0 122 THR BBB CA  1 ? 7  
ATOM   2532  C C   . THR B  2 122 ? 52.245  -3.026   26.896  1.000 73.321  0 122 THR BBB C   1 ? 7  
ATOM   2533  O O   . THR B  2 122 ? 52.957  -3.927   27.383  1.000 77.091  0 122 THR BBB O   1 ? 7  
ATOM   2534  C CB  . THR B  2 122 ? 50.502  -2.601   28.753  1.000 69.341  0 122 THR BBB CB  1 ? 7  
ATOM   2535  O OG1 . THR B  2 122 ? 49.083  -2.579   28.936  1.000 66.296  0 122 THR BBB OG1 1 ? 7  
ATOM   2536  C CG2 . THR B  2 122 ? 51.081  -1.260   29.135  1.000 71.984  0 122 THR BBB CG2 1 ? 7  
ATOM   2537  N N   . VAL B  2 123 ? 52.674  -2.110   26.031  1.000 73.899  0 123 VAL BBB N   1 ? 7  
ATOM   2538  C CA  . VAL B  2 123 ? 54.090  -1.965   25.590  1.000 78.047  0 123 VAL BBB CA  1 ? 7  
ATOM   2539  C C   . VAL B  2 123 ? 54.639  -0.670   26.211  1.000 83.721  0 123 VAL BBB C   1 ? 7  
ATOM   2540  O O   . VAL B  2 123 ? 54.164  0.404    25.816  1.000 80.588  0 123 VAL BBB O   1 ? 7  
ATOM   2541  C CB  . VAL B  2 123 ? 54.176  -1.979   24.050  1.000 76.285  0 123 VAL BBB CB  1 ? 7  
ATOM   2542  C CG1 . VAL B  2 123 ? 55.617  -2.067   23.563  1.000 79.706  0 123 VAL BBB CG1 1 ? 7  
ATOM   2543  C CG2 . VAL B  2 123 ? 53.352  -3.107   23.442  1.000 72.896  0 123 VAL BBB CG2 1 ? 7  
ATOM   2544  N N   . SER B  2 124 ? 55.530  -0.767   27.208  1.000 92.348  0 124 SER BBB N   1 ? 7  
ATOM   2545  C CA  . SER B  2 124 ? 56.182  0.403    27.866  1.000 100.752 0 124 SER BBB CA  1 ? 7  
ATOM   2546  C C   . SER B  2 124 ? 57.352  0.876    26.999  1.000 109.394 0 124 SER BBB C   1 ? 7  
ATOM   2547  O O   . SER B  2 124 ? 57.832  0.069    26.186  1.000 107.940 0 124 SER BBB O   1 ? 7  
ATOM   2548  C CB  . SER B  2 124 ? 56.641  0.087    29.247  1.000 101.709 0 124 SER BBB CB  1 ? 7  
ATOM   2549  O OG  . SER B  2 124 ? 57.528  -1.017   29.214  1.000 103.897 0 124 SER BBB OG  1 ? 7  
ATOM   2550  N N   . SER B  2 125 ? 57.765  2.137    27.148  1.000 68.259  0 125 SER BBB N   1 ? ?  
ATOM   2551  C CA  . SER B  2 125 ? 58.788  2.796    26.284  1.000 71.156  0 125 SER BBB CA  1 ? ?  
ATOM   2552  C C   . SER B  2 125 ? 60.059  3.032    27.104  1.000 70.549  0 125 SER BBB C   1 ? ?  
ATOM   2553  O O   . SER B  2 125 ? 60.920  2.149    27.112  1.000 79.553  0 125 SER BBB O   1 ? ?  
ATOM   2554  C CB  . SER B  2 125 ? 58.263  4.070    25.634  1.000 70.851  0 125 SER BBB CB  1 ? ?  
ATOM   2555  O OG  . SER B  2 125 ? 58.713  5.228    26.311  1.000 77.501  0 125 SER BBB OG  1 ? ?  
ATOM   2556  N N   . ASN C  1 2   ? 31.193  -80.147  -26.197 1.000 78.559  0 331 ASN CCC N   1 ? ?  
ATOM   2557  C CA  . ASN C  1 2   ? 31.621  -79.340  -25.003 1.000 80.138  0 331 ASN CCC CA  1 ? ?  
ATOM   2558  C C   . ASN C  1 2   ? 30.439  -78.502  -24.503 1.000 77.186  0 331 ASN CCC C   1 ? ?  
ATOM   2559  O O   . ASN C  1 2   ? 29.987  -77.604  -25.240 1.000 77.160  0 331 ASN CCC O   1 ? ?  
ATOM   2560  C CB  . ASN C  1 2   ? 32.788  -78.382  -25.280 1.000 83.393  0 331 ASN CCC CB  1 ? ?  
ATOM   2561  C CG  . ASN C  1 2   ? 34.088  -79.055  -25.659 1.000 85.633  0 331 ASN CCC CG  1 ? ?  
ATOM   2562  O OD1 . ASN C  1 2   ? 34.194  -80.280  -25.674 1.000 88.794  0 331 ASN CCC OD1 1 ? ?  
ATOM   2563  N ND2 . ASN C  1 2   ? 35.082  -78.252  -25.990 1.000 81.657  0 331 ASN CCC ND2 1 ? ?  
ATOM   2564  N N   . ILE C  1 3   ? 29.955  -78.778  -23.290 1.000 71.917  0 332 ILE CCC N   1 ? ?  
ATOM   2565  C CA  . ILE C  1 3   ? 29.057  -77.873  -22.504 1.000 67.366  0 332 ILE CCC CA  1 ? ?  
ATOM   2566  C C   . ILE C  1 3   ? 29.871  -76.622  -22.117 1.000 61.232  0 332 ILE CCC C   1 ? ?  
ATOM   2567  O O   . ILE C  1 3   ? 30.941  -76.795  -21.468 1.000 61.638  0 332 ILE CCC O   1 ? ?  
ATOM   2568  C CB  . ILE C  1 3   ? 28.501  -78.607  -21.265 1.000 70.469  0 332 ILE CCC CB  1 ? ?  
ATOM   2569  C CG1 . ILE C  1 3   ? 27.652  -79.836  -21.607 1.000 69.763  0 332 ILE CCC CG1 1 ? ?  
ATOM   2570  C CG2 . ILE C  1 3   ? 27.751  -77.628  -20.388 1.000 69.756  0 332 ILE CCC CG2 1 ? ?  
ATOM   2571  C CD1 . ILE C  1 3   ? 27.671  -80.898  -20.523 1.000 67.299  0 332 ILE CCC CD1 1 ? ?  
ATOM   2572  N N   . THR C  1 4   ? 29.393  -75.414  -22.468 1.000 80.826  0 333 THR CCC N   1 ? 8  
ATOM   2573  C CA  . THR C  1 4   ? 30.150  -74.134  -22.352 1.000 73.450  0 333 THR CCC CA  1 ? 8  
ATOM   2574  C C   . THR C  1 4   ? 29.329  -73.009  -21.711 1.000 64.685  0 333 THR CCC C   1 ? 8  
ATOM   2575  O O   . THR C  1 4   ? 29.945  -72.033  -21.287 1.000 59.563  0 333 THR CCC O   1 ? 8  
ATOM   2576  C CB  . THR C  1 4   ? 30.680  -73.689  -23.719 1.000 75.189  0 333 THR CCC CB  1 ? 8  
ATOM   2577  O OG1 . THR C  1 4   ? 30.918  -74.845  -24.515 1.000 82.315  0 333 THR CCC OG1 1 ? 8  
ATOM   2578  C CG2 . THR C  1 4   ? 31.967  -72.896  -23.621 1.000 74.518  0 333 THR CCC CG2 1 ? 8  
ATOM   2579  N N   . ASN C  1 5   ? 28.010  -73.150  -21.650 1.000 61.798  0 334 ASN CCC N   1 ? 8  
ATOM   2580  C CA  . ASN C  1 5   ? 27.079  -72.160  -21.040 1.000 60.619  0 334 ASN CCC CA  1 ? 8  
ATOM   2581  C C   . ASN C  1 5   ? 27.199  -72.205  -19.509 1.000 56.890  0 334 ASN CCC C   1 ? 8  
ATOM   2582  O O   . ASN C  1 5   ? 27.173  -73.301  -18.936 1.000 55.487  0 334 ASN CCC O   1 ? 8  
ATOM   2583  C CB  . ASN C  1 5   ? 25.638  -72.439  -21.464 1.000 63.068  0 334 ASN CCC CB  1 ? 8  
ATOM   2584  C CG  . ASN C  1 5   ? 25.246  -73.882  -21.220 1.000 64.199  0 334 ASN CCC CG  1 ? 8  
ATOM   2585  O OD1 . ASN C  1 5   ? 25.955  -74.801  -21.608 1.000 63.238  0 334 ASN CCC OD1 1 ? 8  
ATOM   2586  N ND2 . ASN C  1 5   ? 24.143  -74.097  -20.527 1.000 65.467  0 334 ASN CCC ND2 1 ? 8  
ATOM   2587  N N   . LEU C  1 6   ? 27.310  -71.051  -18.866 1.000 55.324  0 335 LEU CCC N   1 ? 8  
ATOM   2588  C CA  . LEU C  1 6   ? 27.472  -70.947  -17.395 1.000 52.916  0 335 LEU CCC CA  1 ? 8  
ATOM   2589  C C   . LEU C  1 6   ? 26.137  -71.293  -16.715 1.000 52.240  0 335 LEU CCC C   1 ? 8  
ATOM   2590  O O   . LEU C  1 6   ? 25.068  -71.047  -17.303 1.000 52.963  0 335 LEU CCC O   1 ? 8  
ATOM   2591  C CB  . LEU C  1 6   ? 27.947  -69.541  -17.038 1.000 53.050  0 335 LEU CCC CB  1 ? 8  
ATOM   2592  C CG  . LEU C  1 6   ? 29.333  -69.155  -17.566 1.000 55.728  0 335 LEU CCC CG  1 ? 8  
ATOM   2593  C CD1 . LEU C  1 6   ? 29.714  -67.756  -17.102 1.000 56.025  0 335 LEU CCC CD1 1 ? 8  
ATOM   2594  C CD2 . LEU C  1 6   ? 30.389  -70.115  -17.088 1.000 56.411  0 335 LEU CCC CD2 1 ? 8  
ATOM   2595  N N   . CYS C  1 7   ? 26.211  -71.930  -15.555 1.000 52.018  0 336 CYS CCC N   1 ? 8  
ATOM   2596  C CA  . CYS C  1 7   ? 25.036  -72.321  -14.745 1.000 54.453  0 336 CYS CCC CA  1 ? 8  
ATOM   2597  C C   . CYS C  1 7   ? 24.327  -71.042  -14.324 1.000 53.325  0 336 CYS CCC C   1 ? 8  
ATOM   2598  O O   . CYS C  1 7   ? 24.983  -70.088  -13.912 1.000 51.413  0 336 CYS CCC O   1 ? 8  
ATOM   2599  C CB  . CYS C  1 7   ? 25.442  -73.180  -13.540 1.000 54.460  0 336 CYS CCC CB  1 ? 8  
ATOM   2600  S SG  . CYS C  1 7   ? 26.052  -74.840  -13.994 1.000 58.237  0 336 CYS CCC SG  1 ? 8  
ATOM   2601  N N   . PRO C  1 8   ? 22.983  -70.980  -14.424 1.000 54.946  0 337 PRO CCC N   1 ? 8  
ATOM   2602  C CA  . PRO C  1 8   ? 22.244  -69.743  -14.164 1.000 53.916  0 337 PRO CCC CA  1 ? 8  
ATOM   2603  C C   . PRO C  1 8   ? 22.036  -69.497  -12.653 1.000 51.596  0 337 PRO CCC C   1 ? 8  
ATOM   2604  O O   . PRO C  1 8   ? 20.921  -69.547  -12.169 1.000 51.886  0 337 PRO CCC O   1 ? 8  
ATOM   2605  C CB  . PRO C  1 8   ? 20.942  -70.010  -14.929 1.000 56.674  0 337 PRO CCC CB  1 ? 8  
ATOM   2606  C CG  . PRO C  1 8   ? 20.705  -71.495  -14.731 1.000 58.524  0 337 PRO CCC CG  1 ? 8  
ATOM   2607  C CD  . PRO C  1 8   ? 22.091  -72.111  -14.737 1.000 58.004  0 337 PRO CCC CD  1 ? 8  
ATOM   2608  N N   . PHE C  1 9   ? 23.121  -69.226  -11.932 1.000 48.603  0 338 PHE CCC N   1 ? 8  
ATOM   2609  C CA  . PHE C  1 9   ? 23.106  -68.964  -10.471 1.000 48.639  0 338 PHE CCC CA  1 ? 8  
ATOM   2610  C C   . PHE C  1 9   ? 22.367  -67.655  -10.176 1.000 47.308  0 338 PHE CCC C   1 ? 8  
ATOM   2611  O O   . PHE C  1 9   ? 21.702  -67.571  -9.124  1.000 43.993  0 338 PHE CCC O   1 ? 8  
ATOM   2612  C CB  . PHE C  1 9   ? 24.530  -68.950  -9.913  1.000 49.441  0 338 PHE CCC CB  1 ? 8  
ATOM   2613  C CG  . PHE C  1 9   ? 25.148  -70.318  -9.776  1.000 51.387  0 338 PHE CCC CG  1 ? 8  
ATOM   2614  C CD1 . PHE C  1 9   ? 24.422  -71.367  -9.236  1.000 53.316  0 338 PHE CCC CD1 1 ? 8  
ATOM   2615  C CD2 . PHE C  1 9   ? 26.465  -70.539  -10.145 1.000 53.102  0 338 PHE CCC CD2 1 ? 8  
ATOM   2616  C CE1 . PHE C  1 9   ? 24.975  -72.630  -9.121  1.000 57.335  0 338 PHE CCC CE1 1 ? 8  
ATOM   2617  C CE2 . PHE C  1 9   ? 27.030  -71.796  -10.014 1.000 57.156  0 338 PHE CCC CE2 1 ? 8  
ATOM   2618  C CZ  . PHE C  1 9   ? 26.281  -72.837  -9.497  1.000 59.290  0 338 PHE CCC CZ  1 ? 8  
ATOM   2619  N N   . GLY C  1 10  ? 22.453  -66.673  -11.090 1.000 46.743  0 339 GLY CCC N   1 ? 8  
ATOM   2620  C CA  . GLY C  1 10  ? 21.734  -65.391  -10.974 1.000 44.944  0 339 GLY CCC CA  1 ? 8  
ATOM   2621  C C   . GLY C  1 10  ? 20.242  -65.610  -10.798 1.000 46.441  0 339 GLY CCC C   1 ? 8  
ATOM   2622  O O   . GLY C  1 10  ? 19.650  -64.938  -9.936  1.000 42.863  0 339 GLY CCC O   1 ? 8  
ATOM   2623  N N   . GLU C  1 11  ? 19.648  -66.548  -11.552 1.000 49.018  0 340 GLU CCC N   1 ? 8  
ATOM   2624  C CA  . GLU C  1 11  ? 18.194  -66.840  -11.498 1.000 52.613  0 340 GLU CCC CA  1 ? 8  
ATOM   2625  C C   . GLU C  1 11  ? 17.799  -67.378  -10.126 1.000 50.841  0 340 GLU CCC C   1 ? 8  
ATOM   2626  O O   . GLU C  1 11  ? 16.617  -67.237  -9.776  1.000 55.138  0 340 GLU CCC O   1 ? 8  
ATOM   2627  C CB  . GLU C  1 11  ? 17.795  -67.852  -12.552 1.000 56.608  0 340 GLU CCC CB  1 ? 8  
ATOM   2628  C CG  . GLU C  1 11  ? 18.021  -67.347  -13.961 1.000 61.589  0 340 GLU CCC CG  1 ? 8  
ATOM   2629  C CD  . GLU C  1 11  ? 17.569  -68.340  -15.015 1.000 68.249  0 340 GLU CCC CD  1 ? 8  
ATOM   2630  O OE1 . GLU C  1 11  ? 16.879  -69.344  -14.637 1.000 70.839  0 340 GLU CCC OE1 1 ? 8  
ATOM   2631  O OE2 . GLU C  1 11  ? 17.903  -68.115  -16.214 1.000 74.675  0 340 GLU CCC OE2 1 ? 8  
ATOM   2632  N N   . VAL C  1 12  ? 18.737  -67.975  -9.388  1.000 45.661  0 341 VAL CCC N   1 ? 8  
ATOM   2633  C CA  . VAL C  1 12  ? 18.499  -68.522  -8.020  1.000 43.261  0 341 VAL CCC CA  1 ? 8  
ATOM   2634  C C   . VAL C  1 12  ? 18.693  -67.417  -6.983  1.000 41.251  0 341 VAL CCC C   1 ? 8  
ATOM   2635  O O   . VAL C  1 12  ? 17.732  -67.125  -6.252  1.000 42.197  0 341 VAL CCC O   1 ? 8  
ATOM   2636  C CB  . VAL C  1 12  ? 19.425  -69.714  -7.727  1.000 43.226  0 341 VAL CCC CB  1 ? 8  
ATOM   2637  C CG1 . VAL C  1 12  ? 19.165  -70.270  -6.339  1.000 43.499  0 341 VAL CCC CG1 1 ? 8  
ATOM   2638  C CG2 . VAL C  1 12  ? 19.318  -70.805  -8.796  1.000 45.749  0 341 VAL CCC CG2 1 ? 8  
ATOM   2639  N N   . PHE C  1 13  ? 19.894  -66.843  -6.913  1.000 39.100  0 342 PHE CCC N   1 ? 8  
ATOM   2640  C CA  . PHE C  1 13  ? 20.318  -65.894  -5.847  1.000 39.266  0 342 PHE CCC CA  1 ? 8  
ATOM   2641  C C   . PHE C  1 13  ? 19.558  -64.560  -5.952  1.000 41.497  0 342 PHE CCC C   1 ? 8  
ATOM   2642  O O   . PHE C  1 13  ? 19.306  -63.936  -4.924  1.000 42.094  0 342 PHE CCC O   1 ? 8  
ATOM   2643  C CB  . PHE C  1 13  ? 21.833  -65.716  -5.888  1.000 37.645  0 342 PHE CCC CB  1 ? 8  
ATOM   2644  C CG  . PHE C  1 13  ? 22.599  -66.857  -5.285  1.000 36.592  0 342 PHE CCC CG  1 ? 8  
ATOM   2645  C CD1 . PHE C  1 13  ? 22.893  -67.982  -6.030  1.000 37.107  0 342 PHE CCC CD1 1 ? 8  
ATOM   2646  C CD2 . PHE C  1 13  ? 23.038  -66.812  -3.979  1.000 37.504  0 342 PHE CCC CD2 1 ? 8  
ATOM   2647  C CE1 . PHE C  1 13  ? 23.594  -69.045  -5.475  1.000 36.991  0 342 PHE CCC CE1 1 ? 8  
ATOM   2648  C CE2 . PHE C  1 13  ? 23.710  -67.892  -3.408  1.000 38.428  0 342 PHE CCC CE2 1 ? 8  
ATOM   2649  C CZ  . PHE C  1 13  ? 23.992  -68.998  -4.164  1.000 38.195  0 342 PHE CCC CZ  1 ? 8  
ATOM   2650  N N   . ASN C  1 14  ? 19.203  -64.151  -7.171  1.000 44.778  0 343 ASN CCC N   1 ? 8  
ATOM   2651  C CA  . ASN C  1 14  ? 18.585  -62.830  -7.483  1.000 48.319  0 343 ASN CCC CA  1 ? 8  
ATOM   2652  C C   . ASN C  1 14  ? 17.176  -63.021  -8.063  1.000 50.370  0 343 ASN CCC C   1 ? 8  
ATOM   2653  O O   . ASN C  1 14  ? 16.672  -62.102  -8.730  1.000 52.786  0 343 ASN CCC O   1 ? 8  
ATOM   2654  C CB  . ASN C  1 14  ? 19.466  -62.024  -8.448  1.000 50.256  0 343 ASN CCC CB  1 ? 8  
ATOM   2655  C CG  . ASN C  1 14  ? 20.774  -61.569  -7.841  1.000 52.196  0 343 ASN CCC CG  1 ? 8  
ATOM   2656  O OD1 . ASN C  1 14  ? 20.853  -61.308  -6.642  1.000 49.287  0 343 ASN CCC OD1 1 ? 8  
ATOM   2657  N ND2 . ASN C  1 14  ? 21.801  -61.462  -8.672  1.000 59.118  0 343 ASN CCC ND2 1 ? 8  
ATOM   2658  N N   . ALA C  1 15  ? 16.546  -64.171  -7.840  1.000 51.367  0 344 ALA CCC N   1 ? 8  
ATOM   2659  C CA  . ALA C  1 15  ? 15.118  -64.403  -8.164  1.000 54.604  0 344 ALA CCC CA  1 ? 8  
ATOM   2660  C C   . ALA C  1 15  ? 14.306  -63.248  -7.587  1.000 57.916  0 344 ALA CCC C   1 ? 8  
ATOM   2661  O O   . ALA C  1 15  ? 14.604  -62.796  -6.482  1.000 54.959  0 344 ALA CCC O   1 ? 8  
ATOM   2662  C CB  . ALA C  1 15  ? 14.636  -65.734  -7.645  1.000 53.274  0 344 ALA CCC CB  1 ? 8  
ATOM   2663  N N   . THR C  1 16  ? 13.329  -62.770  -8.346  1.000 64.745  0 345 THR CCC N   1 ? 8  
ATOM   2664  C CA  . THR C  1 16  ? 12.482  -61.621  -7.973  1.000 71.219  0 345 THR CCC CA  1 ? 8  
ATOM   2665  C C   . THR C  1 16  ? 11.587  -62.028  -6.798  1.000 71.582  0 345 THR CCC C   1 ? 8  
ATOM   2666  O O   . THR C  1 16  ? 11.269  -61.160  -5.993  1.000 76.201  0 345 THR CCC O   1 ? 8  
ATOM   2667  C CB  . THR C  1 16  ? 11.749  -61.140  -9.231  1.000 80.172  0 345 THR CCC CB  1 ? 8  
ATOM   2668  O OG1 . THR C  1 16  ? 11.189  -62.303  -9.848  1.000 79.218  0 345 THR CCC OG1 1 ? 8  
ATOM   2669  C CG2 . THR C  1 16  ? 12.666  -60.413  -10.196 1.000 82.074  0 345 THR CCC CG2 1 ? 8  
ATOM   2670  N N   . ARG C  1 17  ? 11.235  -63.308  -6.681  1.000 71.039  0 346 ARG CCC N   1 ? 8  
ATOM   2671  C CA  . ARG C  1 17  ? 10.409  -63.864  -5.584  1.000 70.773  0 346 ARG CCC CA  1 ? 8  
ATOM   2672  C C   . ARG C  1 17  ? 11.195  -64.962  -4.882  1.000 62.636  0 346 ARG CCC C   1 ? 8  
ATOM   2673  O O   . ARG C  1 17  ? 11.879  -65.764  -5.573  1.000 56.613  0 346 ARG CCC O   1 ? 8  
ATOM   2674  C CB  . ARG C  1 17  ? 9.115   -64.473  -6.136  1.000 79.557  0 346 ARG CCC CB  1 ? 8  
ATOM   2675  C CG  . ARG C  1 17  ? 7.856   -63.954  -5.461  1.000 88.540  0 346 ARG CCC CG  1 ? 8  
ATOM   2676  C CD  . ARG C  1 17  ? 6.724   -64.970  -5.358  1.000 95.761  0 346 ARG CCC CD  1 ? 8  
ATOM   2677  N NE  . ARG C  1 17  ? 5.595   -64.687  -6.245  1.000 106.227 0 346 ARG CCC NE  1 ? 8  
ATOM   2678  C CZ  . ARG C  1 17  ? 5.393   -65.237  -7.444  1.000 111.956 0 346 ARG CCC CZ  1 ? 8  
ATOM   2679  N NH1 . ARG C  1 17  ? 6.269   -66.102  -7.939  1.000 108.657 0 346 ARG CCC NH1 1 ? 8  
ATOM   2680  N NH2 . ARG C  1 17  ? 4.326   -64.901  -8.154  1.000 121.840 0 346 ARG CCC NH2 1 ? 8  
ATOM   2681  N N   . PHE C  1 18  ? 11.036  -65.062  -3.560  1.000 45.398  0 347 PHE CCC N   1 ? 9  
ATOM   2682  C CA  . PHE C  1 18  ? 11.538  -66.214  -2.758  1.000 43.526  0 347 PHE CCC CA  1 ? 9  
ATOM   2683  C C   . PHE C  1 18  ? 10.365  -66.900  -2.055  1.000 42.648  0 347 PHE CCC C   1 ? 9  
ATOM   2684  O O   . PHE C  1 18  ? 9.409   -66.233  -1.683  1.000 46.216  0 347 PHE CCC O   1 ? 9  
ATOM   2685  C CB  . PHE C  1 18  ? 12.616  -65.766  -1.781  1.000 42.425  0 347 PHE CCC CB  1 ? 9  
ATOM   2686  C CG  . PHE C  1 18  ? 14.025  -65.870  -2.299  1.000 42.862  0 347 PHE CCC CG  1 ? 9  
ATOM   2687  C CD1 . PHE C  1 18  ? 14.439  -65.137  -3.401  1.000 45.726  0 347 PHE CCC CD1 1 ? 9  
ATOM   2688  C CD2 . PHE C  1 18  ? 14.949  -66.670  -1.658  1.000 42.694  0 347 PHE CCC CD2 1 ? 9  
ATOM   2689  C CE1 . PHE C  1 18  ? 15.745  -65.222  -3.862  1.000 47.315  0 347 PHE CCC CE1 1 ? 9  
ATOM   2690  C CE2 . PHE C  1 18  ? 16.257  -66.753  -2.108  1.000 42.935  0 347 PHE CCC CE2 1 ? 9  
ATOM   2691  C CZ  . PHE C  1 18  ? 16.651  -66.038  -3.215  1.000 46.039  0 347 PHE CCC CZ  1 ? 9  
ATOM   2692  N N   . ALA C  1 19  ? 10.434  -68.215  -1.895  1.000 40.831  0 348 ALA CCC N   1 ? 9  
ATOM   2693  C CA  . ALA C  1 19  ? 9.403   -69.039  -1.219  1.000 39.472  0 348 ALA CCC CA  1 ? 9  
ATOM   2694  C C   . ALA C  1 19  ? 9.419   -68.811  0.295   1.000 38.944  0 348 ALA CCC C   1 ? 9  
ATOM   2695  O O   . ALA C  1 19  ? 10.466  -68.486  0.856   1.000 38.235  0 348 ALA CCC O   1 ? 9  
ATOM   2696  C CB  . ALA C  1 19  ? 9.628   -70.490  -1.541  1.000 39.730  0 348 ALA CCC CB  1 ? 9  
ATOM   2697  N N   . SER C  1 20  ? 8.271   -68.990  0.935   1.000 40.392  0 349 SER CCC N   1 ? 9  
ATOM   2698  C CA  . SER C  1 20  ? 8.171   -69.322  2.374   1.000 42.458  0 349 SER CCC CA  1 ? 9  
ATOM   2699  C C   . SER C  1 20  ? 8.927   -70.634  2.621   1.000 41.054  0 349 SER CCC C   1 ? 9  
ATOM   2700  O O   . SER C  1 20  ? 8.883   -71.550  1.763   1.000 43.377  0 349 SER CCC O   1 ? 9  
ATOM   2701  C CB  . SER C  1 20  ? 6.740   -69.440  2.811   1.000 45.039  0 349 SER CCC CB  1 ? 9  
ATOM   2702  O OG  . SER C  1 20  ? 6.097   -68.196  2.859   1.000 49.061  0 349 SER CCC OG  1 ? 9  
ATOM   2703  N N   . VAL C  1 21  ? 9.583   -70.735  3.761   1.000 39.853  0 350 VAL CCC N   1 ? 9  
ATOM   2704  C CA  . VAL C  1 21  ? 10.402  -71.923  4.138   1.000 41.933  0 350 VAL CCC CA  1 ? 9  
ATOM   2705  C C   . VAL C  1 21  ? 9.556   -73.216  4.090   1.000 44.562  0 350 VAL CCC C   1 ? 9  
ATOM   2706  O O   . VAL C  1 21  ? 10.075  -74.228  3.630   1.000 45.114  0 350 VAL CCC O   1 ? 9  
ATOM   2707  C CB  . VAL C  1 21  ? 11.067  -71.701  5.506   1.000 39.735  0 350 VAL CCC CB  1 ? 9  
ATOM   2708  C CG1 . VAL C  1 21  ? 10.044  -71.598  6.628   1.000 39.166  0 350 VAL CCC CG1 1 ? 9  
ATOM   2709  C CG2 . VAL C  1 21  ? 12.133  -72.760  5.764   1.000 40.765  0 350 VAL CCC CG2 1 ? 9  
ATOM   2710  N N   . TYR C  1 22  ? 8.293   -73.202  4.528   1.000 45.931  0 351 TYR CCC N   1 ? 9  
ATOM   2711  C CA  . TYR C  1 22  ? 7.462   -74.435  4.594   1.000 45.939  0 351 TYR CCC CA  1 ? 9  
ATOM   2712  C C   . TYR C  1 22  ? 7.208   -74.936  3.162   1.000 45.656  0 351 TYR CCC C   1 ? 9  
ATOM   2713  O O   . TYR C  1 22  ? 7.053   -76.157  2.974   1.000 47.680  0 351 TYR CCC O   1 ? 9  
ATOM   2714  C CB  . TYR C  1 22  ? 6.165   -74.190  5.377   1.000 45.631  0 351 TYR CCC CB  1 ? 9  
ATOM   2715  C CG  . TYR C  1 22  ? 5.056   -73.619  4.537   1.000 44.980  0 351 TYR CCC CG  1 ? 9  
ATOM   2716  C CD1 . TYR C  1 22  ? 4.992   -72.264  4.298   1.000 43.582  0 351 TYR CCC CD1 1 ? 9  
ATOM   2717  C CD2 . TYR C  1 22  ? 4.117   -74.435  3.925   1.000 45.316  0 351 TYR CCC CD2 1 ? 9  
ATOM   2718  C CE1 . TYR C  1 22  ? 4.020   -71.724  3.472   1.000 44.921  0 351 TYR CCC CE1 1 ? 9  
ATOM   2719  C CE2 . TYR C  1 22  ? 3.134   -73.909  3.105   1.000 45.380  0 351 TYR CCC CE2 1 ? 9  
ATOM   2720  C CZ  . TYR C  1 22  ? 3.086   -72.544  2.887   1.000 45.264  0 351 TYR CCC CZ  1 ? 9  
ATOM   2721  O OH  . TYR C  1 22  ? 2.152   -71.922  2.127   1.000 48.082  0 351 TYR CCC OH  1 ? 9  
ATOM   2722  N N   . ALA C  1 23  ? 7.156   -74.018  2.192   1.000 43.918  0 352 ALA CCC N   1 ? 9  
ATOM   2723  C CA  . ALA C  1 23  ? 6.903   -74.298  0.755   1.000 43.870  0 352 ALA CCC CA  1 ? 9  
ATOM   2724  C C   . ALA C  1 23  ? 8.185   -74.028  -0.042  1.000 42.459  0 352 ALA CCC C   1 ? 9  
ATOM   2725  O O   . ALA C  1 23  ? 8.117   -73.391  -1.110  1.000 42.827  0 352 ALA CCC O   1 ? 9  
ATOM   2726  C CB  . ALA C  1 23  ? 5.756   -73.450  0.259   1.000 43.329  0 352 ALA CCC CB  1 ? 9  
ATOM   2727  N N   . TRP C  1 24  ? 9.317   -74.488  0.476   1.000 41.565  0 353 TRP CCC N   1 ? 9  
ATOM   2728  C CA  . TRP C  1 24  ? 10.648  -74.155  -0.082  1.000 41.760  0 353 TRP CCC CA  1 ? 9  
ATOM   2729  C C   . TRP C  1 24  ? 10.726  -74.577  -1.554  1.000 42.798  0 353 TRP CCC C   1 ? 9  
ATOM   2730  O O   . TRP C  1 24  ? 10.155  -75.592  -1.928  1.000 45.486  0 353 TRP CCC O   1 ? 9  
ATOM   2731  C CB  . TRP C  1 24  ? 11.763  -74.762  0.760   1.000 40.629  0 353 TRP CCC CB  1 ? 9  
ATOM   2732  C CG  . TRP C  1 24  ? 11.621  -76.214  1.065   1.000 42.862  0 353 TRP CCC CG  1 ? 9  
ATOM   2733  C CD1 . TRP C  1 24  ? 11.003  -76.788  2.146   1.000 43.935  0 353 TRP CCC CD1 1 ? 9  
ATOM   2734  C CD2 . TRP C  1 24  ? 12.185  -77.292  0.302   1.000 43.864  0 353 TRP CCC CD2 1 ? 9  
ATOM   2735  N NE1 . TRP C  1 24  ? 11.120  -78.149  2.092   1.000 43.500  0 353 TRP CCC NE1 1 ? 9  
ATOM   2736  C CE2 . TRP C  1 24  ? 11.831  -78.484  0.977   1.000 44.254  0 353 TRP CCC CE2 1 ? 9  
ATOM   2737  C CE3 . TRP C  1 24  ? 12.943  -77.361  -0.879  1.000 42.869  0 353 TRP CCC CE3 1 ? 9  
ATOM   2738  C CZ2 . TRP C  1 24  ? 12.227  -79.732  0.518   1.000 45.909  0 353 TRP CCC CZ2 1 ? 9  
ATOM   2739  C CZ3 . TRP C  1 24  ? 13.360  -78.603  -1.325  1.000 44.230  0 353 TRP CCC CZ3 1 ? 9  
ATOM   2740  C CH2 . TRP C  1 24  ? 13.001  -79.771  -0.627  1.000 46.483  0 353 TRP CCC CH2 1 ? 9  
ATOM   2741  N N   . ASN C  1 25  ? 11.411  -73.780  -2.344  1.000 44.093  0 354 ASN CCC N   1 ? 9  
ATOM   2742  C CA  . ASN C  1 25  ? 11.526  -73.960  -3.809  1.000 46.091  0 354 ASN CCC CA  1 ? 9  
ATOM   2743  C C   . ASN C  1 25  ? 12.803  -74.755  -4.124  1.000 44.241  0 354 ASN CCC C   1 ? 9  
ATOM   2744  O O   . ASN C  1 25  ? 13.826  -74.465  -3.475  1.000 43.784  0 354 ASN CCC O   1 ? 9  
ATOM   2745  C CB  . ASN C  1 25  ? 11.482  -72.585  -4.477  1.000 48.364  0 354 ASN CCC CB  1 ? 9  
ATOM   2746  C CG  . ASN C  1 25  ? 11.500  -72.733  -5.976  1.000 53.401  0 354 ASN CCC CG  1 ? 9  
ATOM   2747  O OD1 . ASN C  1 25  ? 12.568  -72.714  -6.592  1.000 57.363  0 354 ASN CCC OD1 1 ? 9  
ATOM   2748  N ND2 . ASN C  1 25  ? 10.337  -72.947  -6.566  1.000 56.919  0 354 ASN CCC ND2 1 ? 9  
ATOM   2749  N N   . ARG C  1 26  ? 12.726  -75.729  -5.044  1.000 44.033  0 355 ARG CCC N   1 ? 9  
ATOM   2750  C CA  . ARG C  1 26  ? 13.864  -76.487  -5.653  1.000 44.117  0 355 ARG CCC CA  1 ? 9  
ATOM   2751  C C   . ARG C  1 26  ? 14.058  -76.120  -7.119  1.000 43.637  0 355 ARG CCC C   1 ? 9  
ATOM   2752  O O   . ARG C  1 26  ? 13.128  -76.380  -7.887  1.000 44.888  0 355 ARG CCC O   1 ? 9  
ATOM   2753  C CB  . ARG C  1 26  ? 13.560  -77.947  -5.963  1.000 46.669  0 355 ARG CCC CB  1 ? 9  
ATOM   2754  C CG  . ARG C  1 26  ? 14.105  -78.966  -5.004  1.000 49.147  0 355 ARG CCC CG  1 ? 9  
ATOM   2755  C CD  . ARG C  1 26  ? 15.188  -79.882  -5.551  1.000 49.264  0 355 ARG CCC CD  1 ? 9  
ATOM   2756  N NE  . ARG C  1 26  ? 15.946  -79.983  -4.310  1.000 52.204  0 355 ARG CCC NE  1 ? 9  
ATOM   2757  C CZ  . ARG C  1 26  ? 16.170  -81.063  -3.584  1.000 51.086  0 355 ARG CCC CZ  1 ? 9  
ATOM   2758  N NH1 . ARG C  1 26  ? 15.727  -82.247  -3.957  1.000 54.253  0 355 ARG CCC NH1 1 ? 9  
ATOM   2759  N NH2 . ARG C  1 26  ? 16.840  -80.937  -2.460  1.000 49.439  0 355 ARG CCC NH2 1 ? 9  
ATOM   2760  N N   . LYS C  1 27  ? 15.249  -75.725  -7.520  1.000 43.118  0 356 LYS CCC N   1 ? 9  
ATOM   2761  C CA  . LYS C  1 27  ? 15.609  -75.669  -8.948  1.000 48.192  0 356 LYS CCC CA  1 ? 9  
ATOM   2762  C C   . LYS C  1 27  ? 16.698  -76.714  -9.206  1.000 47.295  0 356 LYS CCC C   1 ? 9  
ATOM   2763  O O   . LYS C  1 27  ? 17.644  -76.764  -8.436  1.000 46.730  0 356 LYS CCC O   1 ? 9  
ATOM   2764  C CB  . LYS C  1 27  ? 15.994  -74.232  -9.324  1.000 51.776  0 356 LYS CCC CB  1 ? 9  
ATOM   2765  C CG  . LYS C  1 27  ? 16.342  -74.071  -10.794 1.000 57.013  0 356 LYS CCC CG  1 ? 9  
ATOM   2766  C CD  . LYS C  1 27  ? 16.633  -72.663  -11.230 1.000 61.645  0 356 LYS CCC CD  1 ? 9  
ATOM   2767  C CE  . LYS C  1 27  ? 16.733  -72.577  -12.742 1.000 68.268  0 356 LYS CCC CE  1 ? 9  
ATOM   2768  N NZ  . LYS C  1 27  ? 17.627  -71.472  -13.145 1.000 72.015  0 356 LYS CCC NZ  1 ? 9  
ATOM   2769  N N   . ARG C  1 28  ? 16.537  -77.518  -10.247 1.000 49.032  0 357 ARG CCC N   1 ? 9  
ATOM   2770  C CA  . ARG C  1 28  ? 17.611  -78.378  -10.787 1.000 49.685  0 357 ARG CCC CA  1 ? 9  
ATOM   2771  C C   . ARG C  1 28  ? 18.547  -77.517  -11.636 1.000 46.879  0 357 ARG CCC C   1 ? 9  
ATOM   2772  O O   . ARG C  1 28  ? 18.079  -76.762  -12.437 1.000 48.093  0 357 ARG CCC O   1 ? 9  
ATOM   2773  C CB  . ARG C  1 28  ? 17.039  -79.531  -11.603 1.000 53.787  0 357 ARG CCC CB  1 ? 9  
ATOM   2774  C CG  . ARG C  1 28  ? 18.096  -80.541  -12.039 1.000 57.047  0 357 ARG CCC CG  1 ? 9  
ATOM   2775  C CD  . ARG C  1 28  ? 17.640  -81.452  -13.147 1.000 62.853  0 357 ARG CCC CD  1 ? 9  
ATOM   2776  N NE  . ARG C  1 28  ? 17.537  -82.785  -12.578 1.000 67.935  0 357 ARG CCC NE  1 ? 9  
ATOM   2777  C CZ  . ARG C  1 28  ? 16.404  -83.325  -12.132 1.000 74.101  0 357 ARG CCC CZ  1 ? 9  
ATOM   2778  N NH1 . ARG C  1 28  ? 15.238  -82.707  -12.274 1.000 74.270  0 357 ARG CCC NH1 1 ? 9  
ATOM   2779  N NH2 . ARG C  1 28  ? 16.426  -84.540  -11.610 1.000 78.701  0 357 ARG CCC NH2 1 ? 9  
ATOM   2780  N N   . ILE C  1 29  ? 19.843  -77.659  -11.438 1.000 45.537  0 358 ILE CCC N   1 ? 9  
ATOM   2781  C CA  . ILE C  1 29  ? 20.908  -77.079  -12.295 1.000 45.358  0 358 ILE CCC CA  1 ? 9  
ATOM   2782  C C   . ILE C  1 29  ? 21.676  -78.233  -12.930 1.000 47.002  0 358 ILE CCC C   1 ? 9  
ATOM   2783  O O   . ILE C  1 29  ? 22.159  -79.098  -12.178 1.000 45.467  0 358 ILE CCC O   1 ? 9  
ATOM   2784  C CB  . ILE C  1 29  ? 21.790  -76.151  -11.429 1.000 44.007  0 358 ILE CCC CB  1 ? 9  
ATOM   2785  C CG1 . ILE C  1 29  ? 20.971  -74.920  -11.021 1.000 42.933  0 358 ILE CCC CG1 1 ? 9  
ATOM   2786  C CG2 . ILE C  1 29  ? 23.078  -75.747  -12.140 1.000 43.511  0 358 ILE CCC CG2 1 ? 9  
ATOM   2787  C CD1 . ILE C  1 29  ? 21.549  -74.159  -9.900  1.000 42.484  0 358 ILE CCC CD1 1 ? 9  
ATOM   2788  N N   . SER C  1 30  ? 21.776  -78.234  -14.267 1.000 49.121  0 359 SER CCC N   1 ? 9  
ATOM   2789  C CA  . SER C  1 30  ? 22.461  -79.295  -15.048 1.000 51.180  0 359 SER CCC CA  1 ? 9  
ATOM   2790  C C   . SER C  1 30  ? 22.898  -78.811  -16.435 1.000 50.570  0 359 SER CCC C   1 ? 9  
ATOM   2791  O O   . SER C  1 30  ? 22.439  -77.773  -16.852 1.000 49.634  0 359 SER CCC O   1 ? 9  
ATOM   2792  C CB  . SER C  1 30  ? 21.593  -80.500  -15.140 1.000 53.470  0 359 SER CCC CB  1 ? 9  
ATOM   2793  O OG  . SER C  1 30  ? 20.309  -80.110  -15.556 1.000 53.411  0 359 SER CCC OG  1 ? 9  
ATOM   2794  N N   . ASN C  1 31  ? 23.778  -79.568  -17.088 1.000 52.178  0 360 ASN CCC N   1 ? 9  
ATOM   2795  C CA  . ASN C  1 31  ? 24.262  -79.309  -18.471 1.000 54.993  0 360 ASN CCC CA  1 ? 9  
ATOM   2796  C C   . ASN C  1 31  ? 24.723  -77.860  -18.537 1.000 53.713  0 360 ASN CCC C   1 ? 9  
ATOM   2797  O O   . ASN C  1 31  ? 24.199  -77.113  -19.376 1.000 54.404  0 360 ASN CCC O   1 ? 9  
ATOM   2798  C CB  . ASN C  1 31  ? 23.203  -79.612  -19.536 1.000 58.239  0 360 ASN CCC CB  1 ? 9  
ATOM   2799  C CG  . ASN C  1 31  ? 22.740  -81.038  -19.446 1.000 62.411  0 360 ASN CCC CG  1 ? 9  
ATOM   2800  O OD1 . ASN C  1 31  ? 23.482  -81.962  -19.788 1.000 65.291  0 360 ASN CCC OD1 1 ? 9  
ATOM   2801  N ND2 . ASN C  1 31  ? 21.549  -81.216  -18.904 1.000 65.091  0 360 ASN CCC ND2 1 ? 9  
ATOM   2802  N N   . CYS C  1 32  ? 25.646  -77.506  -17.639 1.000 51.264  0 361 CYS CCC N   1 ? 9  
ATOM   2803  C CA  . CYS C  1 32  ? 26.210  -76.143  -17.546 1.000 51.376  0 361 CYS CCC CA  1 ? 9  
ATOM   2804  C C   . CYS C  1 32  ? 27.545  -76.159  -16.785 1.000 49.337  0 361 CYS CCC C   1 ? 9  
ATOM   2805  O O   . CYS C  1 32  ? 27.799  -77.101  -16.055 1.000 47.840  0 361 CYS CCC O   1 ? 9  
ATOM   2806  C CB  . CYS C  1 32  ? 25.187  -75.207  -16.914 1.000 51.093  0 361 CYS CCC CB  1 ? 9  
ATOM   2807  S SG  . CYS C  1 32  ? 24.658  -75.701  -15.260 1.000 51.628  0 361 CYS CCC SG  1 ? 9  
ATOM   2808  N N   . VAL C  1 33  ? 28.366  -75.128  -16.997 1.000 48.812  0 362 VAL CCC N   1 ? 9  
ATOM   2809  C CA  . VAL C  1 33  ? 29.648  -74.871  -16.282 1.000 47.762  0 362 VAL CCC CA  1 ? 9  
ATOM   2810  C C   . VAL C  1 33  ? 29.330  -74.083  -15.010 1.000 48.148  0 362 VAL CCC C   1 ? 9  
ATOM   2811  O O   . VAL C  1 33  ? 28.764  -72.983  -15.132 1.000 46.215  0 362 VAL CCC O   1 ? 9  
ATOM   2812  C CB  . VAL C  1 33  ? 30.641  -74.120  -17.181 1.000 48.131  0 362 VAL CCC CB  1 ? 9  
ATOM   2813  C CG1 . VAL C  1 33  ? 31.940  -73.842  -16.440 1.000 47.372  0 362 VAL CCC CG1 1 ? 9  
ATOM   2814  C CG2 . VAL C  1 33  ? 30.903  -74.853  -18.501 1.000 48.186  0 362 VAL CCC CG2 1 ? 9  
ATOM   2815  N N   . ALA C  1 34  ? 29.641  -74.660  -13.844 1.000 49.463  0 363 ALA CCC N   1 ? 9  
ATOM   2816  C CA  . ALA C  1 34  ? 29.381  -74.053  -12.518 1.000 49.976  0 363 ALA CCC CA  1 ? 9  
ATOM   2817  C C   . ALA C  1 34  ? 30.596  -73.212  -12.143 1.000 51.180  0 363 ALA CCC C   1 ? 9  
ATOM   2818  O O   . ALA C  1 34  ? 31.583  -73.782  -11.609 1.000 50.901  0 363 ALA CCC O   1 ? 9  
ATOM   2819  C CB  . ALA C  1 34  ? 29.117  -75.103  -11.460 1.000 49.007  0 363 ALA CCC CB  1 ? 9  
ATOM   2820  N N   . ASP C  1 35  ? 30.551  -71.922  -12.469 1.000 52.491  0 364 ASP CCC N   1 ? 9  
ATOM   2821  C CA  . ASP C  1 35  ? 31.595  -70.973  -12.027 1.000 53.230  0 364 ASP CCC CA  1 ? 9  
ATOM   2822  C C   . ASP C  1 35  ? 31.140  -70.322  -10.720 1.000 53.860  0 364 ASP CCC C   1 ? 9  
ATOM   2823  O O   . ASP C  1 35  ? 30.187  -69.534  -10.743 1.000 53.174  0 364 ASP CCC O   1 ? 9  
ATOM   2824  C CB  . ASP C  1 35  ? 31.901  -69.928  -13.085 1.000 55.188  0 364 ASP CCC CB  1 ? 9  
ATOM   2825  C CG  . ASP C  1 35  ? 33.226  -69.273  -12.788 1.000 57.331  0 364 ASP CCC CG  1 ? 9  
ATOM   2826  O OD1 . ASP C  1 35  ? 33.739  -69.499  -11.664 1.000 57.276  0 364 ASP CCC OD1 1 ? 9  
ATOM   2827  O OD2 . ASP C  1 35  ? 33.740  -68.588  -13.691 1.000 60.366  0 364 ASP CCC OD2 1 ? 9  
ATOM   2828  N N   . TYR C  1 36  ? 31.817  -70.643  -9.624  1.000 53.994  0 365 TYR CCC N   1 ? 9  
ATOM   2829  C CA  . TYR C  1 36  ? 31.476  -70.164  -8.261  1.000 53.250  0 365 TYR CCC CA  1 ? 9  
ATOM   2830  C C   . TYR C  1 36  ? 32.201  -68.848  -7.945  1.000 53.335  0 365 TYR CCC C   1 ? 9  
ATOM   2831  O O   . TYR C  1 36  ? 31.968  -68.283  -6.842  1.000 53.158  0 365 TYR CCC O   1 ? 9  
ATOM   2832  C CB  . TYR C  1 36  ? 31.783  -71.248  -7.227  1.000 54.954  0 365 TYR CCC CB  1 ? 9  
ATOM   2833  C CG  . TYR C  1 36  ? 30.837  -72.421  -7.302  1.000 53.235  0 365 TYR CCC CG  1 ? 9  
ATOM   2834  C CD1 . TYR C  1 36  ? 29.637  -72.404  -6.622  1.000 54.049  0 365 TYR CCC CD1 1 ? 9  
ATOM   2835  C CD2 . TYR C  1 36  ? 31.104  -73.510  -8.127  1.000 53.948  0 365 TYR CCC CD2 1 ? 9  
ATOM   2836  C CE1 . TYR C  1 36  ? 28.725  -73.438  -6.753  1.000 54.764  0 365 TYR CCC CE1 1 ? 9  
ATOM   2837  C CE2 . TYR C  1 36  ? 30.234  -74.579  -8.226  1.000 51.569  0 365 TYR CCC CE2 1 ? 9  
ATOM   2838  C CZ  . TYR C  1 36  ? 29.035  -74.536  -7.533  1.000 53.824  0 365 TYR CCC CZ  1 ? 9  
ATOM   2839  O OH  . TYR C  1 36  ? 28.146  -75.568  -7.573  1.000 56.574  0 365 TYR CCC OH  1 ? 9  
ATOM   2840  N N   . SER C  1 37  ? 33.033  -68.335  -8.854  1.000 54.560  0 366 SER CCC N   1 ? 9  
ATOM   2841  C CA  . SER C  1 37  ? 33.785  -67.073  -8.594  1.000 57.282  0 366 SER CCC CA  1 ? 9  
ATOM   2842  C C   . SER C  1 37  ? 32.825  -65.889  -8.414  1.000 57.246  0 366 SER CCC C   1 ? 9  
ATOM   2843  O O   . SER C  1 37  ? 33.176  -64.940  -7.688  1.000 61.041  0 366 SER CCC O   1 ? 9  
ATOM   2844  C CB  . SER C  1 37  ? 34.878  -66.801  -9.582  1.000 57.920  0 366 SER CCC CB  1 ? 9  
ATOM   2845  O OG  . SER C  1 37  ? 34.438  -67.056  -10.873 1.000 58.497  0 366 SER CCC OG  1 ? 9  
ATOM   2846  N N   . VAL C  1 38  ? 31.622  -65.966  -8.965  1.000 56.256  0 367 VAL CCC N   1 ? 9  
ATOM   2847  C CA  . VAL C  1 38  ? 30.573  -64.935  -8.725  1.000 57.807  0 367 VAL CCC CA  1 ? 9  
ATOM   2848  C C   . VAL C  1 38  ? 30.261  -64.894  -7.215  1.000 58.213  0 367 VAL CCC C   1 ? 9  
ATOM   2849  O O   . VAL C  1 38  ? 30.204  -63.783  -6.648  1.000 62.937  0 367 VAL CCC O   1 ? 9  
ATOM   2850  C CB  . VAL C  1 38  ? 29.344  -65.192  -9.626  1.000 56.715  0 367 VAL CCC CB  1 ? 9  
ATOM   2851  C CG1 . VAL C  1 38  ? 28.566  -66.441  -9.224  1.000 54.001  0 367 VAL CCC CG1 1 ? 9  
ATOM   2852  C CG2 . VAL C  1 38  ? 28.422  -63.988  -9.678  1.000 57.739  0 367 VAL CCC CG2 1 ? 9  
ATOM   2853  N N   . LEU C  1 39  ? 30.125  -66.050  -6.556  1.000 57.136  0 368 LEU CCC N   1 ? 9  
ATOM   2854  C CA  . LEU C  1 39  ? 29.831  -66.126  -5.098  1.000 58.075  0 368 LEU CCC CA  1 ? 9  
ATOM   2855  C C   . LEU C  1 39  ? 31.081  -65.751  -4.276  1.000 62.828  0 368 LEU CCC C   1 ? 9  
ATOM   2856  O O   . LEU C  1 39  ? 30.909  -65.175  -3.177  1.000 62.320  0 368 LEU CCC O   1 ? 9  
ATOM   2857  C CB  . LEU C  1 39  ? 29.369  -67.538  -4.755  1.000 55.551  0 368 LEU CCC CB  1 ? 9  
ATOM   2858  C CG  . LEU C  1 39  ? 28.130  -68.008  -5.501  1.000 54.222  0 368 LEU CCC CG  1 ? 9  
ATOM   2859  C CD1 . LEU C  1 39  ? 27.782  -69.425  -5.068  1.000 54.666  0 368 LEU CCC CD1 1 ? 9  
ATOM   2860  C CD2 . LEU C  1 39  ? 26.932  -67.080  -5.300  1.000 52.717  0 368 LEU CCC CD2 1 ? 9  
ATOM   2861  N N   . TYR C  1 40  ? 32.285  -66.080  -4.756  1.000 63.527  0 369 TYR CCC N   1 ? 10 
ATOM   2862  C CA  . TYR C  1 40  ? 33.565  -65.816  -4.048  1.000 66.696  0 369 TYR CCC CA  1 ? 10 
ATOM   2863  C C   . TYR C  1 40  ? 33.772  -64.303  -3.868  1.000 69.736  0 369 TYR CCC C   1 ? 10 
ATOM   2864  O O   . TYR C  1 40  ? 34.408  -63.925  -2.860  1.000 69.297  0 369 TYR CCC O   1 ? 10 
ATOM   2865  C CB  . TYR C  1 40  ? 34.772  -66.380  -4.801  1.000 67.869  0 369 TYR CCC CB  1 ? 10 
ATOM   2866  C CG  . TYR C  1 40  ? 34.898  -67.881  -4.858  1.000 68.016  0 369 TYR CCC CG  1 ? 10 
ATOM   2867  C CD1 . TYR C  1 40  ? 34.390  -68.714  -3.867  1.000 65.763  0 369 TYR CCC CD1 1 ? 10 
ATOM   2868  C CD2 . TYR C  1 40  ? 35.571  -68.469  -5.925  1.000 71.646  0 369 TYR CCC CD2 1 ? 10 
ATOM   2869  C CE1 . TYR C  1 40  ? 34.501  -70.093  -3.967  1.000 66.643  0 369 TYR CCC CE1 1 ? 10 
ATOM   2870  C CE2 . TYR C  1 40  ? 35.721  -69.840  -6.030  1.000 72.925  0 369 TYR CCC CE2 1 ? 10 
ATOM   2871  C CZ  . TYR C  1 40  ? 35.151  -70.652  -5.061  1.000 71.009  0 369 TYR CCC CZ  1 ? 10 
ATOM   2872  O OH  . TYR C  1 40  ? 35.342  -72.002  -5.132  1.000 76.078  0 369 TYR CCC OH  1 ? 10 
ATOM   2873  N N   . ASN C  1 41  ? 33.220  -63.487  -4.768  1.000 73.751  0 370 ASN CCC N   1 ? 10 
ATOM   2874  C CA  . ASN C  1 41  ? 33.443  -62.019  -4.808  1.000 81.355  0 370 ASN CCC CA  1 ? 10 
ATOM   2875  C C   . ASN C  1 41  ? 32.382  -61.244  -3.997  1.000 81.294  0 370 ASN CCC C   1 ? 10 
ATOM   2876  O O   . ASN C  1 41  ? 32.423  -60.012  -4.050  1.000 81.301  0 370 ASN CCC O   1 ? 10 
ATOM   2877  C CB  . ASN C  1 41  ? 33.515  -61.517  -6.252  1.000 88.330  0 370 ASN CCC CB  1 ? 10 
ATOM   2878  C CG  . ASN C  1 41  ? 34.713  -62.083  -6.983  1.000 90.980  0 370 ASN CCC CG  1 ? 10 
ATOM   2879  O OD1 . ASN C  1 41  ? 35.795  -62.136  -6.404  1.000 91.116  0 370 ASN CCC OD1 1 ? 10 
ATOM   2880  N ND2 . ASN C  1 41  ? 34.538  -62.509  -8.232  1.000 91.424  0 370 ASN CCC ND2 1 ? 10 
ATOM   2881  N N   . SER C  1 42  ? 31.472  -61.946  -3.323  1.000 78.653  0 371 SER CCC N   1 ? 10 
ATOM   2882  C CA  . SER C  1 42  ? 30.381  -61.358  -2.503  1.000 76.081  0 371 SER CCC CA  1 ? 10 
ATOM   2883  C C   . SER C  1 42  ? 30.829  -61.216  -1.052  1.000 68.238  0 371 SER CCC C   1 ? 10 
ATOM   2884  O O   . SER C  1 42  ? 31.394  -62.196  -0.540  1.000 66.856  0 371 SER CCC O   1 ? 10 
ATOM   2885  C CB  . SER C  1 42  ? 29.123  -62.208  -2.596  1.000 77.826  0 371 SER CCC CB  1 ? 10 
ATOM   2886  O OG  . SER C  1 42  ? 28.709  -62.354  -3.953  1.000 81.432  0 371 SER CCC OG  1 ? 10 
ATOM   2887  N N   . ALA C  1 43  ? 30.577  -60.060  -0.443  1.000 65.964  0 372 ALA CCC N   1 ? 10 
ATOM   2888  C CA  . ALA C  1 43  ? 30.929  -59.764  0.968   1.000 65.321  0 372 ALA CCC CA  1 ? 10 
ATOM   2889  C C   . ALA C  1 43  ? 29.672  -59.682  1.836   1.000 64.664  0 372 ALA CCC C   1 ? 10 
ATOM   2890  O O   . ALA C  1 43  ? 29.833  -59.625  3.070   1.000 65.168  0 372 ALA CCC O   1 ? 10 
ATOM   2891  C CB  . ALA C  1 43  ? 31.742  -58.490  1.093   1.000 69.703  0 372 ALA CCC CB  1 ? 10 
ATOM   2892  N N   . SER C  1 44  ? 28.457  -59.644  1.260   1.000 61.603  0 373 SER CCC N   1 ? 10 
ATOM   2893  C CA  . SER C  1 44  ? 27.208  -59.456  2.047   1.000 56.647  0 373 SER CCC CA  1 ? 10 
ATOM   2894  C C   . SER C  1 44  ? 26.572  -60.793  2.454   1.000 50.040  0 373 SER CCC C   1 ? 10 
ATOM   2895  O O   . SER C  1 44  ? 25.619  -60.762  3.220   1.000 46.681  0 373 SER CCC O   1 ? 10 
ATOM   2896  C CB  . SER C  1 44  ? 26.240  -58.544  1.355   1.000 59.284  0 373 SER CCC CB  1 ? 10 
ATOM   2897  O OG  . SER C  1 44  ? 26.524  -57.191  1.727   1.000 63.498  0 373 SER CCC OG  1 ? 10 
ATOM   2898  N N   . PHE C  1 45  ? 27.070  -61.957  2.039   1.000 46.706  0 374 PHE CCC N   1 ? 10 
ATOM   2899  C CA  . PHE C  1 45  ? 26.599  -63.248  2.598   1.000 43.524  0 374 PHE CCC CA  1 ? 10 
ATOM   2900  C C   . PHE C  1 45  ? 26.912  -63.302  4.105   1.000 42.700  0 374 PHE CCC C   1 ? 10 
ATOM   2901  O O   . PHE C  1 45  ? 28.029  -63.014  4.484   1.000 43.372  0 374 PHE CCC O   1 ? 10 
ATOM   2902  C CB  . PHE C  1 45  ? 27.190  -64.437  1.854   1.000 42.448  0 374 PHE CCC CB  1 ? 10 
ATOM   2903  C CG  . PHE C  1 45  ? 26.805  -64.558  0.403   1.000 43.044  0 374 PHE CCC CG  1 ? 10 
ATOM   2904  C CD1 . PHE C  1 45  ? 25.528  -64.276  -0.029  1.000 43.305  0 374 PHE CCC CD1 1 ? 10 
ATOM   2905  C CD2 . PHE C  1 45  ? 27.716  -65.031  -0.525  1.000 44.570  0 374 PHE CCC CD2 1 ? 10 
ATOM   2906  C CE1 . PHE C  1 45  ? 25.174  -64.434  -1.359  1.000 45.749  0 374 PHE CCC CE1 1 ? 10 
ATOM   2907  C CE2 . PHE C  1 45  ? 27.369  -65.179  -1.858  1.000 45.226  0 374 PHE CCC CE2 1 ? 10 
ATOM   2908  C CZ  . PHE C  1 45  ? 26.102  -64.876  -2.273  1.000 45.782  0 374 PHE CCC CZ  1 ? 10 
ATOM   2909  N N   . SER C  1 46  ? 25.924  -63.633  4.931   1.000 41.605  0 375 SER CCC N   1 ? 10 
ATOM   2910  C CA  . SER C  1 46  ? 26.046  -63.740  6.413   1.000 41.956  0 375 SER CCC CA  1 ? 10 
ATOM   2911  C C   . SER C  1 46  ? 26.728  -65.051  6.762   1.000 40.151  0 375 SER CCC C   1 ? 10 
ATOM   2912  O O   . SER C  1 46  ? 27.397  -65.103  7.782   1.000 43.583  0 375 SER CCC O   1 ? 10 
ATOM   2913  C CB  . SER C  1 46  ? 24.709  -63.647  7.131   1.000 40.834  0 375 SER CCC CB  1 ? 10 
ATOM   2914  O OG  . SER C  1 46  ? 23.781  -64.565  6.586   1.000 39.376  0 375 SER CCC OG  1 ? 10 
ATOM   2915  N N   . THR C  1 47  ? 26.562  -66.066  5.931   1.000 38.988  0 376 THR CCC N   1 ? 10 
ATOM   2916  C CA  . THR C  1 47  ? 27.167  -67.410  6.126   1.000 39.588  0 376 THR CCC CA  1 ? 10 
ATOM   2917  C C   . THR C  1 47  ? 27.394  -68.023  4.739   1.000 39.578  0 376 THR CCC C   1 ? 10 
ATOM   2918  O O   . THR C  1 47  ? 26.575  -67.760  3.791   1.000 36.386  0 376 THR CCC O   1 ? 10 
ATOM   2919  C CB  . THR C  1 47  ? 26.276  -68.257  7.045   1.000 39.137  0 376 THR CCC CB  1 ? 10 
ATOM   2920  O OG1 . THR C  1 47  ? 26.988  -69.434  7.459   1.000 39.683  0 376 THR CCC OG1 1 ? 10 
ATOM   2921  C CG2 . THR C  1 47  ? 24.975  -68.641  6.362   1.000 38.496  0 376 THR CCC CG2 1 ? 10 
ATOM   2922  N N   . PHE C  1 48  ? 28.449  -68.814  4.606   1.000 39.511  0 377 PHE CCC N   1 ? 10 
ATOM   2923  C CA  . PHE C  1 48  ? 28.744  -69.541  3.346   1.000 41.273  0 377 PHE CCC CA  1 ? 10 
ATOM   2924  C C   . PHE C  1 48  ? 29.597  -70.723  3.777   1.000 42.346  0 377 PHE CCC C   1 ? 10 
ATOM   2925  O O   . PHE C  1 48  ? 30.821  -70.563  3.936   1.000 42.718  0 377 PHE CCC O   1 ? 10 
ATOM   2926  C CB  . PHE C  1 48  ? 29.399  -68.595  2.336   1.000 41.855  0 377 PHE CCC CB  1 ? 10 
ATOM   2927  C CG  . PHE C  1 48  ? 29.828  -69.169  1.011   1.000 43.130  0 377 PHE CCC CG  1 ? 10 
ATOM   2928  C CD1 . PHE C  1 48  ? 29.848  -70.527  0.760   1.000 43.732  0 377 PHE CCC CD1 1 ? 10 
ATOM   2929  C CD2 . PHE C  1 48  ? 30.338  -68.322  0.038   1.000 46.198  0 377 PHE CCC CD2 1 ? 10 
ATOM   2930  C CE1 . PHE C  1 48  ? 30.266  -71.013  -0.469  1.000 46.129  0 377 PHE CCC CE1 1 ? 10 
ATOM   2931  C CE2 . PHE C  1 48  ? 30.819  -68.814  -1.166  1.000 48.180  0 377 PHE CCC CE2 1 ? 10 
ATOM   2932  C CZ  . PHE C  1 48  ? 30.780  -70.166  -1.419  1.000 49.120  0 377 PHE CCC CZ  1 ? 10 
ATOM   2933  N N   . LYS C  1 49  ? 28.939  -71.840  4.051   1.000 43.148  0 378 LYS CCC N   1 ? 10 
ATOM   2934  C CA  . LYS C  1 49  ? 29.617  -73.069  4.524   1.000 45.929  0 378 LYS CCC CA  1 ? 10 
ATOM   2935  C C   . LYS C  1 49  ? 29.288  -74.232  3.604   1.000 47.499  0 378 LYS CCC C   1 ? 10 
ATOM   2936  O O   . LYS C  1 49  ? 28.136  -74.341  3.147   1.000 45.220  0 378 LYS CCC O   1 ? 10 
ATOM   2937  C CB  . LYS C  1 49  ? 29.137  -73.484  5.910   1.000 46.719  0 378 LYS CCC CB  1 ? 10 
ATOM   2938  C CG  . LYS C  1 49  ? 29.359  -72.476  7.021   1.000 46.155  0 378 LYS CCC CG  1 ? 10 
ATOM   2939  C CD  . LYS C  1 49  ? 28.701  -73.046  8.243   1.000 45.895  0 378 LYS CCC CD  1 ? 10 
ATOM   2940  C CE  . LYS C  1 49  ? 28.919  -72.300  9.517   1.000 46.363  0 378 LYS CCC CE  1 ? 10 
ATOM   2941  N NZ  . LYS C  1 49  ? 28.569  -73.211  10.627  1.000 48.851  0 378 LYS CCC NZ  1 ? 10 
ATOM   2942  N N   . CYS C  1 50  ? 30.275  -75.093  3.400   1.000 43.550  0 379 CYS CCC N   1 ? 11 
ATOM   2943  C CA  . CYS C  1 50  ? 30.127  -76.316  2.586   1.000 44.795  0 379 CYS CCC CA  1 ? 11 
ATOM   2944  C C   . CYS C  1 50  ? 30.355  -77.533  3.494   1.000 43.530  0 379 CYS CCC C   1 ? 11 
ATOM   2945  O O   . CYS C  1 50  ? 31.038  -77.424  4.535   1.000 42.457  0 379 CYS CCC O   1 ? 11 
ATOM   2946  C CB  . CYS C  1 50  ? 31.057  -76.245  1.375   1.000 46.889  0 379 CYS CCC CB  1 ? 11 
ATOM   2947  S SG  . CYS C  1 50  ? 30.739  -74.799  0.330   1.000 46.586  0 379 CYS CCC SG  1 ? 11 
ATOM   2948  N N   . TYR C  1 51  ? 29.743  -78.644  3.102   1.000 42.927  0 380 TYR CCC N   1 ? 11 
ATOM   2949  C CA  . TYR C  1 51  ? 29.708  -79.944  3.804   1.000 42.907  0 380 TYR CCC CA  1 ? 11 
ATOM   2950  C C   . TYR C  1 51  ? 30.134  -81.019  2.799   1.000 44.280  0 380 TYR CCC C   1 ? 11 
ATOM   2951  O O   . TYR C  1 51  ? 29.539  -81.089  1.729   1.000 43.733  0 380 TYR CCC O   1 ? 11 
ATOM   2952  C CB  . TYR C  1 51  ? 28.306  -80.150  4.380   1.000 42.005  0 380 TYR CCC CB  1 ? 11 
ATOM   2953  C CG  . TYR C  1 51  ? 27.877  -79.048  5.317   1.000 41.875  0 380 TYR CCC CG  1 ? 11 
ATOM   2954  C CD1 . TYR C  1 51  ? 27.295  -77.885  4.845   1.000 41.274  0 380 TYR CCC CD1 1 ? 11 
ATOM   2955  C CD2 . TYR C  1 51  ? 28.050  -79.170  6.674   1.000 42.282  0 380 TYR CCC CD2 1 ? 11 
ATOM   2956  C CE1 . TYR C  1 51  ? 26.903  -76.870  5.702   1.000 40.445  0 380 TYR CCC CE1 1 ? 11 
ATOM   2957  C CE2 . TYR C  1 51  ? 27.671  -78.172  7.550   1.000 42.414  0 380 TYR CCC CE2 1 ? 11 
ATOM   2958  C CZ  . TYR C  1 51  ? 27.106  -77.009  7.061   1.000 41.882  0 380 TYR CCC CZ  1 ? 11 
ATOM   2959  O OH  . TYR C  1 51  ? 26.746  -75.998  7.907   1.000 39.892  0 380 TYR CCC OH  1 ? 11 
ATOM   2960  N N   . GLY C  1 52  ? 31.185  -81.779  3.106   1.000 46.301  0 381 GLY CCC N   1 ? 11 
ATOM   2961  C CA  . GLY C  1 52  ? 31.667  -82.830  2.199   1.000 47.097  0 381 GLY CCC CA  1 ? 11 
ATOM   2962  C C   . GLY C  1 52  ? 32.632  -82.301  1.164   1.000 48.127  0 381 GLY CCC C   1 ? 11 
ATOM   2963  O O   . GLY C  1 52  ? 33.328  -83.148  0.578   1.000 52.220  0 381 GLY CCC O   1 ? 11 
ATOM   2964  N N   . VAL C  1 53  ? 32.706  -80.994  0.910   1.000 48.225  0 382 VAL CCC N   1 ? 11 
ATOM   2965  C CA  . VAL C  1 53  ? 33.739  -80.418  -0.006  1.000 49.954  0 382 VAL CCC CA  1 ? 11 
ATOM   2966  C C   . VAL C  1 53  ? 34.174  -79.058  0.514   1.000 48.810  0 382 VAL CCC C   1 ? 11 
ATOM   2967  O O   . VAL C  1 53  ? 33.352  -78.355  1.090   1.000 47.621  0 382 VAL CCC O   1 ? 11 
ATOM   2968  C CB  . VAL C  1 53  ? 33.229  -80.295  -1.451  1.000 52.076  0 382 VAL CCC CB  1 ? 11 
ATOM   2969  C CG1 . VAL C  1 53  ? 33.009  -81.669  -2.051  1.000 56.445  0 382 VAL CCC CG1 1 ? 11 
ATOM   2970  C CG2 . VAL C  1 53  ? 31.970  -79.474  -1.524  1.000 49.909  0 382 VAL CCC CG2 1 ? 11 
ATOM   2971  N N   . SER C  1 54  ? 35.434  -78.717  0.290   1.000 49.242  0 383 SER CCC N   1 ? 11 
ATOM   2972  C CA  . SER C  1 54  ? 36.005  -77.418  0.704   1.000 49.265  0 383 SER CCC CA  1 ? 11 
ATOM   2973  C C   . SER C  1 54  ? 35.522  -76.347  -0.263  1.000 49.157  0 383 SER CCC C   1 ? 11 
ATOM   2974  O O   . SER C  1 54  ? 35.473  -76.583  -1.460  1.000 50.823  0 383 SER CCC O   1 ? 11 
ATOM   2975  C CB  . SER C  1 54  ? 37.495  -77.482  0.756   1.000 49.980  0 383 SER CCC CB  1 ? 11 
ATOM   2976  O OG  . SER C  1 54  ? 38.028  -76.196  1.022   1.000 49.015  0 383 SER CCC OG  1 ? 11 
ATOM   2977  N N   . PRO C  1 55  ? 35.104  -75.154  0.224   1.000 47.166  0 384 PRO CCC N   1 ? 11 
ATOM   2978  C CA  . PRO C  1 55  ? 34.797  -74.017  -0.641  1.000 46.692  0 384 PRO CCC CA  1 ? 11 
ATOM   2979  C C   . PRO C  1 55  ? 35.893  -73.688  -1.659  1.000 46.851  0 384 PRO CCC C   1 ? 11 
ATOM   2980  O O   . PRO C  1 55  ? 35.569  -73.215  -2.752  1.000 46.386  0 384 PRO CCC O   1 ? 11 
ATOM   2981  C CB  . PRO C  1 55  ? 34.608  -72.861  0.345   1.000 45.531  0 384 PRO CCC CB  1 ? 11 
ATOM   2982  C CG  . PRO C  1 55  ? 34.043  -73.560  1.564   1.000 44.566  0 384 PRO CCC CG  1 ? 11 
ATOM   2983  C CD  . PRO C  1 55  ? 34.846  -74.843  1.630   1.000 45.695  0 384 PRO CCC CD  1 ? 11 
ATOM   2984  N N   . THR C  1 56  ? 37.142  -73.974  -1.295  1.000 48.424  0 385 THR CCC N   1 ? 11 
ATOM   2985  C CA  . THR C  1 56  ? 38.336  -73.743  -2.158  1.000 49.924  0 385 THR CCC CA  1 ? 11 
ATOM   2986  C C   . THR C  1 56  ? 38.321  -74.674  -3.380  1.000 51.347  0 385 THR CCC C   1 ? 11 
ATOM   2987  O O   . THR C  1 56  ? 39.089  -74.428  -4.288  1.000 55.925  0 385 THR CCC O   1 ? 11 
ATOM   2988  C CB  . THR C  1 56  ? 39.650  -73.902  -1.373  1.000 49.669  0 385 THR CCC CB  1 ? 11 
ATOM   2989  O OG1 . THR C  1 56  ? 39.814  -75.250  -0.944  1.000 48.235  0 385 THR CCC OG1 1 ? 11 
ATOM   2990  C CG2 . THR C  1 56  ? 39.745  -72.976  -0.178  1.000 49.197  0 385 THR CCC CG2 1 ? 11 
ATOM   2991  N N   . LYS C  1 57  ? 37.512  -75.725  -3.393  1.000 51.976  0 386 LYS CCC N   1 ? 11 
ATOM   2992  C CA  . LYS C  1 57  ? 37.560  -76.761  -4.451  1.000 55.542  0 386 LYS CCC CA  1 ? 11 
ATOM   2993  C C   . LYS C  1 57  ? 36.321  -76.713  -5.340  1.000 51.115  0 386 LYS CCC C   1 ? 11 
ATOM   2994  O O   . LYS C  1 57  ? 36.247  -77.590  -6.252  1.000 52.662  0 386 LYS CCC O   1 ? 11 
ATOM   2995  C CB  . LYS C  1 57  ? 37.681  -78.158  -3.828  1.000 58.412  0 386 LYS CCC CB  1 ? 11 
ATOM   2996  C CG  . LYS C  1 57  ? 38.931  -78.369  -2.981  1.000 62.763  0 386 LYS CCC CG  1 ? 11 
ATOM   2997  C CD  . LYS C  1 57  ? 40.183  -78.654  -3.782  1.000 64.394  0 386 LYS CCC CD  1 ? 11 
ATOM   2998  C CE  . LYS C  1 57  ? 40.096  -79.983  -4.506  1.000 67.206  0 386 LYS CCC CE  1 ? 11 
ATOM   2999  N NZ  . LYS C  1 57  ? 40.631  -79.873  -5.880  1.000 68.427  0 386 LYS CCC NZ  1 ? 11 
ATOM   3000  N N   . LEU C  1 58  ? 35.379  -75.792  -5.112  1.000 47.456  0 387 LEU CCC N   1 ? 11 
ATOM   3001  C CA  . LEU C  1 58  ? 34.063  -75.856  -5.817  1.000 48.792  0 387 LEU CCC CA  1 ? 11 
ATOM   3002  C C   . LEU C  1 58  ? 34.247  -75.829  -7.339  1.000 46.590  0 387 LEU CCC C   1 ? 11 
ATOM   3003  O O   . LEU C  1 58  ? 33.497  -76.524  -8.057  1.000 49.289  0 387 LEU CCC O   1 ? 11 
ATOM   3004  C CB  . LEU C  1 58  ? 33.133  -74.733  -5.344  1.000 48.830  0 387 LEU CCC CB  1 ? 11 
ATOM   3005  C CG  . LEU C  1 58  ? 32.672  -74.850  -3.887  1.000 51.030  0 387 LEU CCC CG  1 ? 11 
ATOM   3006  C CD1 . LEU C  1 58  ? 31.781  -73.683  -3.459  1.000 48.816  0 387 LEU CCC CD1 1 ? 11 
ATOM   3007  C CD2 . LEU C  1 58  ? 31.935  -76.170  -3.697  1.000 51.424  0 387 LEU CCC CD2 1 ? 11 
ATOM   3008  N N   . ASN C  1 59  ? 35.242  -75.093  -7.817  1.000 48.847  0 388 ASN CCC N   1 ? 11 
ATOM   3009  C CA  . ASN C  1 59  ? 35.473  -74.914  -9.271  1.000 50.644  0 388 ASN CCC CA  1 ? 11 
ATOM   3010  C C   . ASN C  1 59  ? 36.188  -76.126  -9.879  1.000 50.768  0 388 ASN CCC C   1 ? 11 
ATOM   3011  O O   . ASN C  1 59  ? 36.407  -76.085  -11.100 1.000 53.482  0 388 ASN CCC O   1 ? 11 
ATOM   3012  C CB  . ASN C  1 59  ? 36.225  -73.606  -9.553  1.000 49.672  0 388 ASN CCC CB  1 ? 11 
ATOM   3013  C CG  . ASN C  1 59  ? 35.276  -72.443  -9.704  1.000 48.359  0 388 ASN CCC CG  1 ? 11 
ATOM   3014  O OD1 . ASN C  1 59  ? 34.069  -72.619  -9.839  1.000 47.317  0 388 ASN CCC OD1 1 ? 11 
ATOM   3015  N ND2 . ASN C  1 59  ? 35.793  -71.247  -9.558  1.000 50.514  0 388 ASN CCC ND2 1 ? 11 
ATOM   3016  N N   . ASP C  1 60  ? 36.559  -77.140  -9.093  1.000 51.694  0 389 ASP CCC N   1 ? 11 
ATOM   3017  C CA  . ASP C  1 60  ? 37.362  -78.284  -9.593  1.000 54.921  0 389 ASP CCC CA  1 ? 11 
ATOM   3018  C C   . ASP C  1 60  ? 36.579  -79.594  -9.568  1.000 54.071  0 389 ASP CCC C   1 ? 11 
ATOM   3019  O O   . ASP C  1 60  ? 37.182  -80.621  -9.858  1.000 54.696  0 389 ASP CCC O   1 ? 11 
ATOM   3020  C CB  . ASP C  1 60  ? 38.610  -78.517  -8.760  1.000 57.287  0 389 ASP CCC CB  1 ? 11 
ATOM   3021  C CG  . ASP C  1 60  ? 39.534  -77.338  -8.720  1.000 61.980  0 389 ASP CCC CG  1 ? 11 
ATOM   3022  O OD1 . ASP C  1 60  ? 39.958  -76.839  -9.783  1.000 69.557  0 389 ASP CCC OD1 1 ? 11 
ATOM   3023  O OD2 . ASP C  1 60  ? 39.885  -76.998  -7.613  1.000 65.174  0 389 ASP CCC OD2 1 ? 11 
ATOM   3024  N N   . LEU C  1 61  ? 35.287  -79.575  -9.249  1.000 53.254  0 390 LEU CCC N   1 ? 11 
ATOM   3025  C CA  . LEU C  1 61  ? 34.511  -80.832  -9.094  1.000 53.436  0 390 LEU CCC CA  1 ? 11 
ATOM   3026  C C   . LEU C  1 61  ? 33.491  -80.954  -10.239 1.000 51.278  0 390 LEU CCC C   1 ? 11 
ATOM   3027  O O   . LEU C  1 61  ? 33.022  -79.913  -10.781 1.000 52.610  0 390 LEU CCC O   1 ? 11 
ATOM   3028  C CB  . LEU C  1 61  ? 33.822  -80.811  -7.729  1.000 56.461  0 390 LEU CCC CB  1 ? 11 
ATOM   3029  C CG  . LEU C  1 61  ? 34.746  -80.647  -6.511  1.000 58.627  0 390 LEU CCC CG  1 ? 11 
ATOM   3030  C CD1 . LEU C  1 61  ? 33.950  -80.459  -5.244  1.000 56.745  0 390 LEU CCC CD1 1 ? 11 
ATOM   3031  C CD2 . LEU C  1 61  ? 35.694  -81.839  -6.397  1.000 60.565  0 390 LEU CCC CD2 1 ? 11 
ATOM   3032  N N   . CYS C  1 62  ? 33.150  -82.191  -10.581 1.000 51.366  0 391 CYS CCC N   1 ? 11 
ATOM   3033  C CA  . CYS C  1 62  ? 32.021  -82.536  -11.476 1.000 51.088  0 391 CYS CCC CA  1 ? 11 
ATOM   3034  C C   . CYS C  1 62  ? 30.961  -83.282  -10.668 1.000 48.613  0 391 CYS CCC C   1 ? 11 
ATOM   3035  O O   . CYS C  1 62  ? 31.326  -84.107  -9.835  1.000 50.759  0 391 CYS CCC O   1 ? 11 
ATOM   3036  C CB  . CYS C  1 62  ? 32.518  -83.370  -12.647 1.000 54.745  0 391 CYS CCC CB  1 ? 11 
ATOM   3037  S SG  . CYS C  1 62  ? 33.562  -82.424  -13.792 1.000 56.947  0 391 CYS CCC SG  1 ? 11 
ATOM   3038  N N   . PHE C  1 63  ? 29.695  -82.984  -10.937 1.000 46.718  0 392 PHE CCC N   1 ? 11 
ATOM   3039  C CA  . PHE C  1 63  ? 28.495  -83.637  -10.370 1.000 45.754  0 392 PHE CCC CA  1 ? 11 
ATOM   3040  C C   . PHE C  1 63  ? 27.532  -83.973  -11.511 1.000 46.647  0 392 PHE CCC C   1 ? 11 
ATOM   3041  O O   . PHE C  1 63  ? 27.696  -83.466  -12.636 1.000 46.008  0 392 PHE CCC O   1 ? 11 
ATOM   3042  C CB  . PHE C  1 63  ? 27.922  -82.701  -9.324  1.000 43.824  0 392 PHE CCC CB  1 ? 11 
ATOM   3043  C CG  . PHE C  1 63  ? 28.848  -82.464  -8.167  1.000 43.561  0 392 PHE CCC CG  1 ? 11 
ATOM   3044  C CD1 . PHE C  1 63  ? 29.168  -83.490  -7.287  1.000 44.962  0 392 PHE CCC CD1 1 ? 11 
ATOM   3045  C CD2 . PHE C  1 63  ? 29.404  -81.218  -7.968  1.000 43.637  0 392 PHE CCC CD2 1 ? 11 
ATOM   3046  C CE1 . PHE C  1 63  ? 30.026  -83.259  -6.218  1.000 44.887  0 392 PHE CCC CE1 1 ? 11 
ATOM   3047  C CE2 . PHE C  1 63  ? 30.245  -80.985  -6.887  1.000 45.007  0 392 PHE CCC CE2 1 ? 11 
ATOM   3048  C CZ  . PHE C  1 63  ? 30.542  -82.002  -6.003  1.000 45.458  0 392 PHE CCC CZ  1 ? 11 
ATOM   3049  N N   . THR C  1 64  ? 26.584  -84.875  -11.273 1.000 47.015  0 393 THR CCC N   1 ? 11 
ATOM   3050  C CA  . THR C  1 64  ? 25.526  -85.233  -12.256 1.000 49.587  0 393 THR CCC CA  1 ? 11 
ATOM   3051  C C   . THR C  1 64  ? 24.535  -84.065  -12.328 1.000 48.280  0 393 THR CCC C   1 ? 11 
ATOM   3052  O O   . THR C  1 64  ? 24.035  -83.731  -13.400 1.000 48.004  0 393 THR CCC O   1 ? 11 
ATOM   3053  C CB  . THR C  1 64  ? 24.776  -86.496  -11.850 1.000 50.956  0 393 THR CCC CB  1 ? 11 
ATOM   3054  O OG1 . THR C  1 64  ? 25.706  -87.331  -11.164 1.000 51.662  0 393 THR CCC OG1 1 ? 11 
ATOM   3055  C CG2 . THR C  1 64  ? 24.169  -87.204  -13.043 1.000 52.085  0 393 THR CCC CG2 1 ? 11 
ATOM   3056  N N   . ASN C  1 65  ? 24.301  -83.466  -11.180 1.000 47.158  0 394 ASN CCC N   1 ? 11 
ATOM   3057  C CA  . ASN C  1 65  ? 23.258  -82.450  -10.965 1.000 46.632  0 394 ASN CCC CA  1 ? 11 
ATOM   3058  C C   . ASN C  1 65  ? 23.630  -81.625  -9.742  1.000 45.032  0 394 ASN CCC C   1 ? 11 
ATOM   3059  O O   . ASN C  1 65  ? 24.299  -82.098  -8.814  1.000 44.912  0 394 ASN CCC O   1 ? 11 
ATOM   3060  C CB  . ASN C  1 65  ? 21.900  -83.091  -10.711 1.000 48.177  0 394 ASN CCC CB  1 ? 11 
ATOM   3061  C CG  . ASN C  1 65  ? 21.319  -83.742  -11.932 1.000 47.416  0 394 ASN CCC CG  1 ? 11 
ATOM   3062  O OD1 . ASN C  1 65  ? 21.013  -83.076  -12.922 1.000 49.176  0 394 ASN CCC OD1 1 ? 11 
ATOM   3063  N ND2 . ASN C  1 65  ? 21.195  -85.046  -11.836 1.000 48.632  0 394 ASN CCC ND2 1 ? 11 
ATOM   3064  N N   . VAL C  1 66  ? 23.129  -80.408  -9.739  1.000 43.321  0 395 VAL CCC N   1 ? 11 
ATOM   3065  C CA  . VAL C  1 66  ? 23.122  -79.530  -8.545  1.000 41.945  0 395 VAL CCC CA  1 ? 11 
ATOM   3066  C C   . VAL C  1 66  ? 21.679  -79.140  -8.313  1.000 40.110  0 395 VAL CCC C   1 ? 11 
ATOM   3067  O O   . VAL C  1 66  ? 20.992  -78.953  -9.272  1.000 46.599  0 395 VAL CCC O   1 ? 11 
ATOM   3068  C CB  . VAL C  1 66  ? 24.058  -78.343  -8.769  1.000 43.406  0 395 VAL CCC CB  1 ? 11 
ATOM   3069  C CG1 . VAL C  1 66  ? 24.032  -77.395  -7.587  1.000 45.058  0 395 VAL CCC CG1 1 ? 11 
ATOM   3070  C CG2 . VAL C  1 66  ? 25.485  -78.841  -8.989  1.000 44.752  0 395 VAL CCC CG2 1 ? 11 
ATOM   3071  N N   . TYR C  1 67  ? 21.249  -79.139  -7.071  1.000 39.650  0 396 TYR CCC N   1 ? 11 
ATOM   3072  C CA  . TYR C  1 67  ? 19.911  -78.639  -6.667  1.000 40.081  0 396 TYR CCC CA  1 ? 11 
ATOM   3073  C C   . TYR C  1 67  ? 20.103  -77.382  -5.848  1.000 38.376  0 396 TYR CCC C   1 ? 11 
ATOM   3074  O O   . TYR C  1 67  ? 20.978  -77.369  -4.968  1.000 36.995  0 396 TYR CCC O   1 ? 11 
ATOM   3075  C CB  . TYR C  1 67  ? 19.106  -79.657  -5.878  1.000 41.844  0 396 TYR CCC CB  1 ? 11 
ATOM   3076  C CG  . TYR C  1 67  ? 18.823  -80.880  -6.681  1.000 43.788  0 396 TYR CCC CG  1 ? 11 
ATOM   3077  C CD1 . TYR C  1 67  ? 17.953  -80.829  -7.743  1.000 43.979  0 396 TYR CCC CD1 1 ? 11 
ATOM   3078  C CD2 . TYR C  1 67  ? 19.617  -82.009  -6.522  1.000 47.177  0 396 TYR CCC CD2 1 ? 11 
ATOM   3079  C CE1 . TYR C  1 67  ? 17.759  -81.949  -8.540  1.000 48.966  0 396 TYR CCC CE1 1 ? 11 
ATOM   3080  C CE2 . TYR C  1 67  ? 19.462  -83.119  -7.330  1.000 49.064  0 396 TYR CCC CE2 1 ? 11 
ATOM   3081  C CZ  . TYR C  1 67  ? 18.525  -83.088  -8.340  1.000 50.953  0 396 TYR CCC CZ  1 ? 11 
ATOM   3082  O OH  . TYR C  1 67  ? 18.348  -84.186  -9.116  1.000 55.615  0 396 TYR CCC OH  1 ? 11 
ATOM   3083  N N   . ALA C  1 68  ? 19.325  -76.365  -6.199  1.000 35.744  0 397 ALA CCC N   1 ? 11 
ATOM   3084  C CA  . ALA C  1 68  ? 19.262  -75.088  -5.477  1.000 35.787  0 397 ALA CCC CA  1 ? 11 
ATOM   3085  C C   . ALA C  1 68  ? 17.893  -74.994  -4.803  1.000 35.826  0 397 ALA CCC C   1 ? 11 
ATOM   3086  O O   . ALA C  1 68  ? 16.886  -74.844  -5.513  1.000 37.791  0 397 ALA CCC O   1 ? 11 
ATOM   3087  C CB  . ALA C  1 68  ? 19.549  -73.984  -6.451  1.000 35.896  0 397 ALA CCC CB  1 ? 11 
ATOM   3088  N N   . ASP C  1 69  ? 17.882  -75.135  -3.491  1.000 35.960  0 398 ASP CCC N   1 ? 11 
ATOM   3089  C CA  . ASP C  1 69  ? 16.700  -74.900  -2.618  1.000 38.126  0 398 ASP CCC CA  1 ? 11 
ATOM   3090  C C   . ASP C  1 69  ? 16.822  -73.480  -2.072  1.000 35.669  0 398 ASP CCC C   1 ? 11 
ATOM   3091  O O   . ASP C  1 69  ? 17.920  -73.120  -1.626  1.000 37.063  0 398 ASP CCC O   1 ? 11 
ATOM   3092  C CB  . ASP C  1 69  ? 16.621  -75.934  -1.467  1.000 38.100  0 398 ASP CCC CB  1 ? 11 
ATOM   3093  C CG  . ASP C  1 69  ? 16.620  -77.363  -1.945  1.000 38.726  0 398 ASP CCC CG  1 ? 11 
ATOM   3094  O OD1 . ASP C  1 69  ? 16.149  -77.585  -3.055  1.000 38.614  0 398 ASP CCC OD1 1 ? 11 
ATOM   3095  O OD2 . ASP C  1 69  ? 17.151  -78.235  -1.212  1.000 41.246  0 398 ASP CCC OD2 1 ? 11 
ATOM   3096  N N   . SER C  1 70  ? 15.745  -72.723  -2.087  1.000 35.038  0 399 SER CCC N   1 ? 11 
ATOM   3097  C CA  . SER C  1 70  ? 15.770  -71.333  -1.595  1.000 35.832  0 399 SER CCC CA  1 ? 11 
ATOM   3098  C C   . SER C  1 70  ? 14.467  -71.017  -0.867  1.000 37.353  0 399 SER CCC C   1 ? 11 
ATOM   3099  O O   . SER C  1 70  ? 13.387  -71.576  -1.224  1.000 35.680  0 399 SER CCC O   1 ? 11 
ATOM   3100  C CB  . SER C  1 70  ? 16.034  -70.387  -2.739  1.000 35.302  0 399 SER CCC CB  1 ? 11 
ATOM   3101  O OG  . SER C  1 70  ? 15.044  -70.542  -3.758  1.000 36.626  0 399 SER CCC OG  1 ? 11 
ATOM   3102  N N   . PHE C  1 71  ? 14.575  -70.105  0.099   1.000 37.725  0 400 PHE CCC N   1 ? 11 
ATOM   3103  C CA  . PHE C  1 71  ? 13.452  -69.693  0.961   1.000 38.116  0 400 PHE CCC CA  1 ? 11 
ATOM   3104  C C   . PHE C  1 71  ? 13.895  -68.541  1.855   1.000 38.164  0 400 PHE CCC C   1 ? 11 
ATOM   3105  O O   . PHE C  1 71  ? 15.089  -68.209  1.860   1.000 36.113  0 400 PHE CCC O   1 ? 11 
ATOM   3106  C CB  . PHE C  1 71  ? 12.998  -70.885  1.808   1.000 38.875  0 400 PHE CCC CB  1 ? 11 
ATOM   3107  C CG  . PHE C  1 71  ? 14.106  -71.613  2.518   1.000 37.919  0 400 PHE CCC CG  1 ? 11 
ATOM   3108  C CD1 . PHE C  1 71  ? 14.636  -71.121  3.699   1.000 39.321  0 400 PHE CCC CD1 1 ? 11 
ATOM   3109  C CD2 . PHE C  1 71  ? 14.619  -72.791  2.007   1.000 38.708  0 400 PHE CCC CD2 1 ? 11 
ATOM   3110  C CE1 . PHE C  1 71  ? 15.658  -71.798  4.356   1.000 40.476  0 400 PHE CCC CE1 1 ? 11 
ATOM   3111  C CE2 . PHE C  1 71  ? 15.646  -73.458  2.664   1.000 37.788  0 400 PHE CCC CE2 1 ? 11 
ATOM   3112  C CZ  . PHE C  1 71  ? 16.166  -72.963  3.834   1.000 39.157  0 400 PHE CCC CZ  1 ? 11 
ATOM   3113  N N   . VAL C  1 72  ? 12.950  -68.009  2.635   1.000 40.075  0 401 VAL CCC N   1 ? 11 
ATOM   3114  C CA  . VAL C  1 72  ? 13.200  -66.934  3.642   1.000 39.779  0 401 VAL CCC CA  1 ? 11 
ATOM   3115  C C   . VAL C  1 72  ? 12.919  -67.483  5.041   1.000 39.899  0 401 VAL CCC C   1 ? 11 
ATOM   3116  O O   . VAL C  1 72  ? 11.887  -68.164  5.239   1.000 37.908  0 401 VAL CCC O   1 ? 11 
ATOM   3117  C CB  . VAL C  1 72  ? 12.344  -65.694  3.329   1.000 40.254  0 401 VAL CCC CB  1 ? 11 
ATOM   3118  C CG1 . VAL C  1 72  ? 12.359  -64.690  4.451   1.000 42.286  0 401 VAL CCC CG1 1 ? 11 
ATOM   3119  C CG2 . VAL C  1 72  ? 12.800  -65.060  2.034   1.000 41.542  0 401 VAL CCC CG2 1 ? 11 
ATOM   3120  N N   . ILE C  1 73  ? 13.802  -67.149  5.981   1.000 41.201  0 402 ILE CCC N   1 ? 11 
ATOM   3121  C CA  . ILE C  1 73  ? 13.627  -67.384  7.444   1.000 42.927  0 402 ILE CCC CA  1 ? 11 
ATOM   3122  C C   . ILE C  1 73  ? 14.143  -66.153  8.205   1.000 45.068  0 402 ILE CCC C   1 ? 11 
ATOM   3123  O O   . ILE C  1 73  ? 14.604  -65.209  7.555   1.000 42.195  0 402 ILE CCC O   1 ? 11 
ATOM   3124  C CB  . ILE C  1 73  ? 14.338  -68.685  7.849   1.000 42.578  0 402 ILE CCC CB  1 ? 11 
ATOM   3125  C CG1 . ILE C  1 73  ? 15.803  -68.708  7.422   1.000 40.586  0 402 ILE CCC CG1 1 ? 11 
ATOM   3126  C CG2 . ILE C  1 73  ? 13.584  -69.891  7.323   1.000 43.064  0 402 ILE CCC CG2 1 ? 11 
ATOM   3127  C CD1 . ILE C  1 73  ? 16.570  -69.872  8.020   1.000 41.095  0 402 ILE CCC CD1 1 ? 11 
ATOM   3128  N N   . ARG C  1 74  ? 14.016  -66.140  9.536   1.000 48.463  0 403 ARG CCC N   1 ? 11 
ATOM   3129  C CA  . ARG C  1 74  ? 14.599  -65.101  10.419  1.000 51.681  0 403 ARG CCC CA  1 ? 11 
ATOM   3130  C C   . ARG C  1 74  ? 16.109  -65.309  10.491  1.000 49.444  0 403 ARG CCC C   1 ? 11 
ATOM   3131  O O   . ARG C  1 74  ? 16.552  -66.503  10.430  1.000 48.800  0 403 ARG CCC O   1 ? 11 
ATOM   3132  C CB  . ARG C  1 74  ? 14.142  -65.252  11.870  1.000 56.026  0 403 ARG CCC CB  1 ? 11 
ATOM   3133  C CG  . ARG C  1 74  ? 12.740  -64.755  12.162  1.000 61.282  0 403 ARG CCC CG  1 ? 11 
ATOM   3134  C CD  . ARG C  1 74  ? 12.238  -65.378  13.456  1.000 63.958  0 403 ARG CCC CD  1 ? 11 
ATOM   3135  N NE  . ARG C  1 74  ? 13.134  -65.089  14.557  1.000 68.098  0 403 ARG CCC NE  1 ? 11 
ATOM   3136  C CZ  . ARG C  1 74  ? 13.022  -65.616  15.772  1.000 74.530  0 403 ARG CCC CZ  1 ? 11 
ATOM   3137  N NH1 . ARG C  1 74  ? 12.070  -66.494  16.036  1.000 75.948  0 403 ARG CCC NH1 1 ? 11 
ATOM   3138  N NH2 . ARG C  1 74  ? 13.884  -65.264  16.721  1.000 80.198  0 403 ARG CCC NH2 1 ? 11 
ATOM   3139  N N   . GLY C  1 75  ? 16.839  -64.225  10.752  1.000 48.028  0 404 GLY CCC N   1 ? 11 
ATOM   3140  C CA  . GLY C  1 75  ? 18.296  -64.256  10.947  1.000 47.377  0 404 GLY CCC CA  1 ? 11 
ATOM   3141  C C   . GLY C  1 75  ? 18.720  -65.341  11.916  1.000 45.698  0 404 GLY CCC C   1 ? 11 
ATOM   3142  O O   . GLY C  1 75  ? 19.620  -66.103  11.570  1.000 42.639  0 404 GLY CCC O   1 ? 11 
ATOM   3143  N N   . ASP C  1 76  ? 18.121  -65.407  13.102  1.000 46.690  0 405 ASP CCC N   1 ? 11 
ATOM   3144  C CA  . ASP C  1 76  ? 18.653  -66.328  14.146  1.000 50.978  0 405 ASP CCC CA  1 ? 11 
ATOM   3145  C C   . ASP C  1 76  ? 18.134  -67.755  13.925  1.000 47.925  0 405 ASP CCC C   1 ? 11 
ATOM   3146  O O   . ASP C  1 76  ? 18.550  -68.604  14.677  1.000 46.908  0 405 ASP CCC O   1 ? 11 
ATOM   3147  C CB  . ASP C  1 76  ? 18.520  -65.744  15.561  1.000 58.666  0 405 ASP CCC CB  1 ? 11 
ATOM   3148  C CG  . ASP C  1 76  ? 17.130  -65.284  15.946  1.000 64.598  0 405 ASP CCC CG  1 ? 11 
ATOM   3149  O OD1 . ASP C  1 76  ? 16.162  -65.814  15.352  1.000 63.611  0 405 ASP CCC OD1 1 ? 11 
ATOM   3150  O OD2 . ASP C  1 76  ? 17.032  -64.403  16.844  1.000 71.620  0 405 ASP CCC OD2 1 ? 11 
ATOM   3151  N N   . GLU C  1 77  ? 17.392  -68.034  12.847  1.000 45.757  0 406 GLU CCC N   1 ? 11 
ATOM   3152  C CA  . GLU C  1 77  ? 17.050  -69.419  12.459  1.000 46.056  0 406 GLU CCC CA  1 ? 11 
ATOM   3153  C C   . GLU C  1 77  ? 18.062  -69.969  11.422  1.000 45.668  0 406 GLU CCC C   1 ? 11 
ATOM   3154  O O   . GLU C  1 77  ? 18.040  -71.201  11.119  1.000 43.735  0 406 GLU CCC O   1 ? 11 
ATOM   3155  C CB  . GLU C  1 77  ? 15.623  -69.475  11.915  1.000 47.898  0 406 GLU CCC CB  1 ? 11 
ATOM   3156  C CG  . GLU C  1 77  ? 14.525  -69.268  12.948  1.000 46.827  0 406 GLU CCC CG  1 ? 11 
ATOM   3157  C CD  . GLU C  1 77  ? 13.125  -69.087  12.374  1.000 46.691  0 406 GLU CCC CD  1 ? 11 
ATOM   3158  O OE1 . GLU C  1 77  ? 13.008  -68.720  11.174  1.000 45.903  0 406 GLU CCC OE1 1 ? 11 
ATOM   3159  O OE2 . GLU C  1 77  ? 12.138  -69.291  13.134  1.000 51.721  0 406 GLU CCC OE2 1 ? 11 
ATOM   3160  N N   . VAL C  1 78  ? 18.930  -69.128  10.858  1.000 44.681  0 407 VAL CCC N   1 ? 11 
ATOM   3161  C CA  . VAL C  1 78  ? 19.879  -69.577  9.796   1.000 43.114  0 407 VAL CCC CA  1 ? 11 
ATOM   3162  C C   . VAL C  1 78  ? 20.782  -70.705  10.327  1.000 41.662  0 407 VAL CCC C   1 ? 11 
ATOM   3163  O O   . VAL C  1 78  ? 21.050  -71.615  9.557   1.000 41.354  0 407 VAL CCC O   1 ? 11 
ATOM   3164  C CB  . VAL C  1 78  ? 20.663  -68.397  9.188   1.000 42.034  0 407 VAL CCC CB  1 ? 11 
ATOM   3165  C CG1 . VAL C  1 78  ? 21.786  -68.858  8.284   1.000 40.640  0 407 VAL CCC CG1 1 ? 11 
ATOM   3166  C CG2 . VAL C  1 78  ? 19.751  -67.447  8.418   1.000 41.888  0 407 VAL CCC CG2 1 ? 11 
ATOM   3167  N N   . ARG C  1 79  ? 21.187  -70.688  11.592  1.000 45.262  0 408 ARG CCC N   1 ? 11 
ATOM   3168  C CA  . ARG C  1 79  ? 21.995  -71.777  12.225  1.000 48.791  0 408 ARG CCC CA  1 ? 11 
ATOM   3169  C C   . ARG C  1 79  ? 21.326  -73.167  12.045  1.000 47.020  0 408 ARG CCC C   1 ? 11 
ATOM   3170  O O   . ARG C  1 79  ? 22.042  -74.188  12.145  1.000 50.026  0 408 ARG CCC O   1 ? 11 
ATOM   3171  C CB  . ARG C  1 79  ? 22.264  -71.424  13.688  1.000 52.949  0 408 ARG CCC CB  1 ? 11 
ATOM   3172  C CG  . ARG C  1 79  ? 21.325  -72.043  14.696  1.000 61.735  0 408 ARG CCC CG  1 ? 11 
ATOM   3173  C CD  . ARG C  1 79  ? 21.318  -71.428  16.068  1.000 72.646  0 408 ARG CCC CD  1 ? 11 
ATOM   3174  N NE  . ARG C  1 79  ? 19.909  -71.117  16.275  1.000 85.820  0 408 ARG CCC NE  1 ? 11 
ATOM   3175  C CZ  . ARG C  1 79  ? 18.898  -71.997  16.469  1.000 85.417  0 408 ARG CCC CZ  1 ? 11 
ATOM   3176  N NH1 . ARG C  1 79  ? 19.126  -73.303  16.588  1.000 79.572  0 408 ARG CCC NH1 1 ? 11 
ATOM   3177  N NH2 . ARG C  1 79  ? 17.659  -71.528  16.601  1.000 83.660  0 408 ARG CCC NH2 1 ? 11 
ATOM   3178  N N   . GLN C  1 80  ? 20.000  -73.219  11.863  1.000 42.665  0 409 GLN CCC N   1 ? 11 
ATOM   3179  C CA  . GLN C  1 80  ? 19.248  -74.496  11.754  1.000 40.474  0 409 GLN CCC CA  1 ? 11 
ATOM   3180  C C   . GLN C  1 80  ? 19.396  -75.095  10.348  1.000 37.186  0 409 GLN CCC C   1 ? 11 
ATOM   3181  O O   . GLN C  1 80  ? 19.095  -76.262  10.185  1.000 35.804  0 409 GLN CCC O   1 ? 11 
ATOM   3182  C CB  . GLN C  1 80  ? 17.768  -74.276  12.064  1.000 40.463  0 409 GLN CCC CB  1 ? 11 
ATOM   3183  C CG  . GLN C  1 80  ? 17.472  -73.977  13.525  1.000 41.248  0 409 GLN CCC CG  1 ? 11 
ATOM   3184  C CD  . GLN C  1 80  ? 15.981  -73.867  13.791  1.000 42.570  0 409 GLN CCC CD  1 ? 11 
ATOM   3185  O OE1 . GLN C  1 80  ? 15.150  -74.689  13.381  1.000 39.670  0 409 GLN CCC OE1 1 ? 11 
ATOM   3186  N NE2 . GLN C  1 80  ? 15.606  -72.817  14.508  1.000 43.202  0 409 GLN CCC NE2 1 ? 11 
ATOM   3187  N N   . ILE C  1 81  ? 19.863  -74.340  9.368   1.000 39.178  0 410 ILE CCC N   1 ? 11 
ATOM   3188  C CA  . ILE C  1 81  ? 20.030  -74.862  7.981   1.000 40.235  0 410 ILE CCC CA  1 ? 11 
ATOM   3189  C C   . ILE C  1 81  ? 21.400  -75.523  7.877   1.000 40.574  0 410 ILE CCC C   1 ? 11 
ATOM   3190  O O   . ILE C  1 81  ? 22.327  -74.947  7.249   1.000 38.832  0 410 ILE CCC O   1 ? 11 
ATOM   3191  C CB  . ILE C  1 81  ? 19.789  -73.775  6.924   1.000 42.412  0 410 ILE CCC CB  1 ? 11 
ATOM   3192  C CG1 . ILE C  1 81  ? 18.548  -72.939  7.255   1.000 42.086  0 410 ILE CCC CG1 1 ? 11 
ATOM   3193  C CG2 . ILE C  1 81  ? 19.692  -74.426  5.528   1.000 42.988  0 410 ILE CCC CG2 1 ? 11 
ATOM   3194  C CD1 . ILE C  1 81  ? 17.298  -73.785  7.407   1.000 43.416  0 410 ILE CCC CD1 1 ? 11 
ATOM   3195  N N   . ALA C  1 82  ? 21.515  -76.686  8.509   1.000 41.970  0 411 ALA CCC N   1 ? 11 
ATOM   3196  C CA  . ALA C  1 82  ? 22.803  -77.415  8.651   1.000 45.036  0 411 ALA CCC CA  1 ? 11 
ATOM   3197  C C   . ALA C  1 82  ? 22.512  -78.844  9.091   1.000 44.858  0 411 ALA CCC C   1 ? 11 
ATOM   3198  O O   . ALA C  1 82  ? 21.554  -79.055  9.814   1.000 44.754  0 411 ALA CCC O   1 ? 11 
ATOM   3199  C CB  . ALA C  1 82  ? 23.720  -76.697  9.637   1.000 44.227  0 411 ALA CCC CB  1 ? 11 
ATOM   3200  N N   . PRO C  1 83  ? 23.299  -79.843  8.664   1.000 45.335  0 412 PRO CCC N   1 ? 11 
ATOM   3201  C CA  . PRO C  1 83  ? 23.079  -81.220  9.112   1.000 46.985  0 412 PRO CCC CA  1 ? 11 
ATOM   3202  C C   . PRO C  1 83  ? 23.138  -81.295  10.651  1.000 46.927  0 412 PRO CCC C   1 ? 11 
ATOM   3203  O O   . PRO C  1 83  ? 23.991  -80.688  11.201  1.000 46.132  0 412 PRO CCC O   1 ? 11 
ATOM   3204  C CB  . PRO C  1 83  ? 24.238  -82.011  8.466   1.000 47.903  0 412 PRO CCC CB  1 ? 11 
ATOM   3205  C CG  . PRO C  1 83  ? 25.279  -80.926  8.155   1.000 47.668  0 412 PRO CCC CG  1 ? 11 
ATOM   3206  C CD  . PRO C  1 83  ? 24.466  -79.706  7.768   1.000 46.234  0 412 PRO CCC CD  1 ? 11 
ATOM   3207  N N   . GLY C  1 84  ? 22.208  -82.019  11.280  1.000 47.346  0 413 GLY CCC N   1 ? 11 
ATOM   3208  C CA  . GLY C  1 84  ? 22.207  -82.368  12.705  1.000 47.627  0 413 GLY CCC CA  1 ? 11 
ATOM   3209  C C   . GLY C  1 84  ? 21.619  -81.287  13.591  1.000 48.912  0 413 GLY CCC C   1 ? 11 
ATOM   3210  O O   . GLY C  1 84  ? 21.761  -81.408  14.816  1.000 50.777  0 413 GLY CCC O   1 ? 11 
ATOM   3211  N N   . GLN C  1 85  ? 20.930  -80.299  13.031  1.000 48.728  0 414 GLN CCC N   1 ? 11 
ATOM   3212  C CA  . GLN C  1 85  ? 20.281  -79.193  13.807  1.000 49.573  0 414 GLN CCC CA  1 ? 11 
ATOM   3213  C C   . GLN C  1 85  ? 18.841  -79.554  14.214  1.000 47.304  0 414 GLN CCC C   1 ? 11 
ATOM   3214  O O   . GLN C  1 85  ? 18.233  -80.369  13.509  1.000 48.845  0 414 GLN CCC O   1 ? 11 
ATOM   3215  C CB  . GLN C  1 85  ? 20.260  -77.927  12.958  1.000 47.481  0 414 GLN CCC CB  1 ? 11 
ATOM   3216  C CG  . GLN C  1 85  ? 21.631  -77.322  12.758  1.000 46.926  0 414 GLN CCC CG  1 ? 11 
ATOM   3217  C CD  . GLN C  1 85  ? 22.234  -76.849  14.056  1.000 48.745  0 414 GLN CCC CD  1 ? 11 
ATOM   3218  O OE1 . GLN C  1 85  ? 21.551  -76.340  14.935  1.000 49.761  0 414 GLN CCC OE1 1 ? 11 
ATOM   3219  N NE2 . GLN C  1 85  ? 23.539  -76.986  14.173  1.000 48.523  0 414 GLN CCC NE2 1 ? 11 
ATOM   3220  N N   . THR C  1 86  ? 18.325  -78.963  15.286  1.000 47.190  0 415 THR CCC N   1 ? 11 
ATOM   3221  C CA  . THR C  1 86  ? 16.893  -79.028  15.677  1.000 50.337  0 415 THR CCC CA  1 ? 11 
ATOM   3222  C C   . THR C  1 86  ? 16.342  -77.616  15.890  1.000 51.563  0 415 THR CCC C   1 ? 11 
ATOM   3223  O O   . THR C  1 86  ? 17.142  -76.680  15.957  1.000 55.358  0 415 THR CCC O   1 ? 11 
ATOM   3224  C CB  . THR C  1 86  ? 16.660  -79.892  16.923  1.000 52.714  0 415 THR CCC CB  1 ? 11 
ATOM   3225  O OG1 . THR C  1 86  ? 17.469  -79.344  17.961  1.000 52.578  0 415 THR CCC OG1 1 ? 11 
ATOM   3226  C CG2 . THR C  1 86  ? 16.982  -81.351  16.683  1.000 53.248  0 415 THR CCC CG2 1 ? 11 
ATOM   3227  N N   . GLY C  1 87  ? 15.014  -77.507  15.960  1.000 52.286  0 416 GLY CCC N   1 ? 11 
ATOM   3228  C CA  . GLY C  1 87  ? 14.246  -76.251  16.054  1.000 51.289  0 416 GLY CCC CA  1 ? 11 
ATOM   3229  C C   . GLY C  1 87  ? 13.047  -76.294  15.129  1.000 49.486  0 416 GLY CCC C   1 ? 11 
ATOM   3230  O O   . GLY C  1 87  ? 12.955  -77.261  14.353  1.000 48.102  0 416 GLY CCC O   1 ? 11 
ATOM   3231  N N   . LYS C  1 88  ? 12.163  -75.301  15.209  1.000 50.660  0 417 LYS CCC N   1 ? 11 
ATOM   3232  C CA  . LYS C  1 88  ? 10.937  -75.247  14.374  1.000 55.200  0 417 LYS CCC CA  1 ? 11 
ATOM   3233  C C   . LYS C  1 88  ? 11.337  -75.436  12.906  1.000 51.319  0 417 LYS CCC C   1 ? 11 
ATOM   3234  O O   . LYS C  1 88  ? 10.644  -76.193  12.244  1.000 49.109  0 417 LYS CCC O   1 ? 11 
ATOM   3235  C CB  . LYS C  1 88  ? 10.074  -74.003  14.637  1.000 60.407  0 417 LYS CCC CB  1 ? 11 
ATOM   3236  C CG  . LYS C  1 88  ? 8.737   -74.316  15.355  1.000 68.373  0 417 LYS CCC CG  1 ? 11 
ATOM   3237  C CD  . LYS C  1 88  ? 8.347   -73.554  16.609  1.000 73.395  0 417 LYS CCC CD  1 ? 11 
ATOM   3238  C CE  . LYS C  1 88  ? 8.006   -74.446  17.801  1.000 79.025  0 417 LYS CCC CE  1 ? 11 
ATOM   3239  N NZ  . LYS C  1 88  ? 8.337   -73.799  19.095  1.000 82.550  0 417 LYS CCC NZ  1 ? 11 
ATOM   3240  N N   . ILE C  1 89  ? 12.411  -74.807  12.441  1.000 48.542  0 418 ILE CCC N   1 ? 11 
ATOM   3241  C CA  . ILE C  1 89  ? 12.739  -74.811  10.983  1.000 46.429  0 418 ILE CCC CA  1 ? 11 
ATOM   3242  C C   . ILE C  1 89  ? 13.317  -76.182  10.582  1.000 44.359  0 418 ILE CCC C   1 ? 11 
ATOM   3243  O O   . ILE C  1 89  ? 12.752  -76.813  9.677   1.000 41.148  0 418 ILE CCC O   1 ? 11 
ATOM   3244  C CB  . ILE C  1 89  ? 13.650  -73.627  10.603  1.000 45.261  0 418 ILE CCC CB  1 ? 11 
ATOM   3245  C CG1 . ILE C  1 89  ? 13.058  -72.290  11.064  1.000 46.469  0 418 ILE CCC CG1 1 ? 11 
ATOM   3246  C CG2 . ILE C  1 89  ? 13.925  -73.625  9.106   1.000 44.200  0 418 ILE CCC CG2 1 ? 11 
ATOM   3247  C CD1 . ILE C  1 89  ? 11.638  -72.042  10.566  1.000 45.687  0 418 ILE CCC CD1 1 ? 11 
ATOM   3248  N N   . ALA C  1 90  ? 14.370  -76.650  11.256  1.000 43.407  0 419 ALA CCC N   1 ? 11 
ATOM   3249  C CA  . ALA C  1 90  ? 14.981  -77.971  10.989  1.000 44.303  0 419 ALA CCC CA  1 ? 11 
ATOM   3250  C C   . ALA C  1 90  ? 13.927  -79.086  11.114  1.000 46.022  0 419 ALA CCC C   1 ? 11 
ATOM   3251  O O   . ALA C  1 90  ? 13.945  -80.022  10.281  1.000 45.266  0 419 ALA CCC O   1 ? 11 
ATOM   3252  C CB  . ALA C  1 90  ? 16.151  -78.196  11.900  1.000 42.595  0 419 ALA CCC CB  1 ? 11 
ATOM   3253  N N   . ASP C  1 91  ? 13.037  -78.996  12.100  1.000 49.073  0 420 ASP CCC N   1 ? 11 
ATOM   3254  C CA  . ASP C  1 91  ? 12.112  -80.108  12.458  1.000 52.319  0 420 ASP CCC CA  1 ? 11 
ATOM   3255  C C   . ASP C  1 91  ? 10.879  -80.093  11.556  1.000 50.614  0 420 ASP CCC C   1 ? 11 
ATOM   3256  O O   . ASP C  1 91  ? 10.443  -81.187  11.171  1.000 53.523  0 420 ASP CCC O   1 ? 11 
ATOM   3257  C CB  . ASP C  1 91  ? 11.673  -80.048  13.929  1.000 55.971  0 420 ASP CCC CB  1 ? 11 
ATOM   3258  C CG  . ASP C  1 91  ? 12.813  -80.243  14.935  1.000 56.981  0 420 ASP CCC CG  1 ? 11 
ATOM   3259  O OD1 . ASP C  1 91  ? 13.917  -80.691  14.521  1.000 57.182  0 420 ASP CCC OD1 1 ? 11 
ATOM   3260  O OD2 . ASP C  1 91  ? 12.596  -79.941  16.132  1.000 62.063  0 420 ASP CCC OD2 1 ? 11 
ATOM   3261  N N   . TYR C  1 92  ? 10.324  -78.918  11.240  1.000 46.849  0 421 TYR CCC N   1 ? 11 
ATOM   3262  C CA  . TYR C  1 92  ? 8.947   -78.794  10.699  1.000 46.549  0 421 TYR CCC CA  1 ? 11 
ATOM   3263  C C   . TYR C  1 92  ? 8.904   -78.144  9.309   1.000 45.250  0 421 TYR CCC C   1 ? 11 
ATOM   3264  O O   . TYR C  1 92  ? 7.823   -78.174  8.699   1.000 45.239  0 421 TYR CCC O   1 ? 11 
ATOM   3265  C CB  . TYR C  1 92  ? 8.076   -78.005  11.675  1.000 47.425  0 421 TYR CCC CB  1 ? 11 
ATOM   3266  C CG  . TYR C  1 92  ? 7.804   -78.631  13.021  1.000 48.892  0 421 TYR CCC CG  1 ? 11 
ATOM   3267  C CD1 . TYR C  1 92  ? 8.011   -79.977  13.279  1.000 49.042  0 421 TYR CCC CD1 1 ? 11 
ATOM   3268  C CD2 . TYR C  1 92  ? 7.221   -77.867  14.029  1.000 50.777  0 421 TYR CCC CD2 1 ? 11 
ATOM   3269  C CE1 . TYR C  1 92  ? 7.712   -80.524  14.519  1.000 50.867  0 421 TYR CCC CE1 1 ? 11 
ATOM   3270  C CE2 . TYR C  1 92  ? 6.916   -78.397  15.273  1.000 51.472  0 421 TYR CCC CE2 1 ? 11 
ATOM   3271  C CZ  . TYR C  1 92  ? 7.156   -79.734  15.519  1.000 52.365  0 421 TYR CCC CZ  1 ? 11 
ATOM   3272  O OH  . TYR C  1 92  ? 6.847   -80.266  16.742  1.000 53.721  0 421 TYR CCC OH  1 ? 11 
ATOM   3273  N N   . ASN C  1 93  ? 10.012  -77.607  8.791   1.000 44.454  0 422 ASN CCC N   1 ? 11 
ATOM   3274  C CA  . ASN C  1 93  ? 9.987   -76.781  7.554   1.000 43.295  0 422 ASN CCC CA  1 ? 11 
ATOM   3275  C C   . ASN C  1 93  ? 11.000  -77.304  6.516   1.000 42.203  0 422 ASN CCC C   1 ? 11 
ATOM   3276  O O   . ASN C  1 93  ? 10.601  -77.593  5.378   1.000 42.374  0 422 ASN CCC O   1 ? 11 
ATOM   3277  C CB  . ASN C  1 93  ? 10.217  -75.315  7.898   1.000 43.605  0 422 ASN CCC CB  1 ? 11 
ATOM   3278  C CG  . ASN C  1 93  ? 9.045   -74.713  8.653   1.000 44.767  0 422 ASN CCC CG  1 ? 11 
ATOM   3279  O OD1 . ASN C  1 93  ? 8.146   -74.150  8.047   1.000 42.886  0 422 ASN CCC OD1 1 ? 11 
ATOM   3280  N ND2 . ASN C  1 93  ? 9.025   -74.852  9.970   1.000 47.408  0 422 ASN CCC ND2 1 ? 11 
ATOM   3281  N N   . TYR C  1 94  ? 12.282  -77.380  6.864   1.000 41.912  0 423 TYR CCC N   1 ? 11 
ATOM   3282  C CA  . TYR C  1 94  ? 13.385  -77.739  5.938   1.000 40.539  0 423 TYR CCC CA  1 ? 11 
ATOM   3283  C C   . TYR C  1 94  ? 14.484  -78.459  6.712   1.000 41.228  0 423 TYR CCC C   1 ? 11 
ATOM   3284  O O   . TYR C  1 94  ? 15.117  -77.849  7.598   1.000 41.922  0 423 TYR CCC O   1 ? 11 
ATOM   3285  C CB  . TYR C  1 94  ? 13.954  -76.508  5.224   1.000 40.763  0 423 TYR CCC CB  1 ? 11 
ATOM   3286  C CG  . TYR C  1 94  ? 14.955  -76.845  4.149   1.000 40.134  0 423 TYR CCC CG  1 ? 11 
ATOM   3287  C CD1 . TYR C  1 94  ? 14.548  -77.163  2.860   1.000 38.867  0 423 TYR CCC CD1 1 ? 11 
ATOM   3288  C CD2 . TYR C  1 94  ? 16.318  -76.892  4.438   1.000 40.613  0 423 TYR CCC CD2 1 ? 11 
ATOM   3289  C CE1 . TYR C  1 94  ? 15.479  -77.460  1.871   1.000 39.791  0 423 TYR CCC CE1 1 ? 11 
ATOM   3290  C CE2 . TYR C  1 94  ? 17.264  -77.192  3.466   1.000 41.331  0 423 TYR CCC CE2 1 ? 11 
ATOM   3291  C CZ  . TYR C  1 94  ? 16.843  -77.458  2.175   1.000 40.892  0 423 TYR CCC CZ  1 ? 11 
ATOM   3292  O OH  . TYR C  1 94  ? 17.785  -77.762  1.236   1.000 41.393  0 423 TYR CCC OH  1 ? 11 
ATOM   3293  N N   . LYS C  1 95  ? 14.696  -79.728  6.377   1.000 42.441  0 424 LYS CCC N   1 ? 11 
ATOM   3294  C CA  . LYS C  1 95  ? 15.596  -80.653  7.098   1.000 48.077  0 424 LYS CCC CA  1 ? 11 
ATOM   3295  C C   . LYS C  1 95  ? 16.708  -81.091  6.149   1.000 46.455  0 424 LYS CCC C   1 ? 11 
ATOM   3296  O O   . LYS C  1 95  ? 16.378  -81.688  5.099   1.000 45.998  0 424 LYS CCC O   1 ? 11 
ATOM   3297  C CB  . LYS C  1 95  ? 14.817  -81.881  7.598   1.000 54.566  0 424 LYS CCC CB  1 ? 11 
ATOM   3298  C CG  . LYS C  1 95  ? 15.650  -82.915  8.347   1.000 60.714  0 424 LYS CCC CG  1 ? 11 
ATOM   3299  C CD  . LYS C  1 95  ? 16.446  -82.311  9.477   1.000 65.143  0 424 LYS CCC CD  1 ? 11 
ATOM   3300  C CE  . LYS C  1 95  ? 16.880  -83.349  10.488  1.000 68.746  0 424 LYS CCC CE  1 ? 11 
ATOM   3301  N NZ  . LYS C  1 95  ? 17.527  -82.695  11.651  1.000 72.369  0 424 LYS CCC NZ  1 ? 11 
ATOM   3302  N N   . LEU C  1 96  ? 17.963  -80.840  6.511   1.000 46.955  0 425 LEU CCC N   1 ? 11 
ATOM   3303  C CA  . LEU C  1 96  ? 19.123  -81.378  5.766   1.000 47.571  0 425 LEU CCC CA  1 ? 11 
ATOM   3304  C C   . LEU C  1 96  ? 19.464  -82.750  6.337   1.000 47.667  0 425 LEU CCC C   1 ? 11 
ATOM   3305  O O   . LEU C  1 96  ? 19.360  -82.985  7.544   1.000 52.859  0 425 LEU CCC O   1 ? 11 
ATOM   3306  C CB  . LEU C  1 96  ? 20.326  -80.445  5.884   1.000 46.318  0 425 LEU CCC CB  1 ? 11 
ATOM   3307  C CG  . LEU C  1 96  ? 20.257  -79.177  5.050   1.000 44.744  0 425 LEU CCC CG  1 ? 11 
ATOM   3308  C CD1 . LEU C  1 96  ? 21.519  -78.349  5.214   1.000 46.604  0 425 LEU CCC CD1 1 ? 11 
ATOM   3309  C CD2 . LEU C  1 96  ? 20.098  -79.480  3.585   1.000 46.316  0 425 LEU CCC CD2 1 ? 11 
ATOM   3310  N N   . PRO C  1 97  ? 19.879  -83.687  5.460   1.000 45.444  0 426 PRO CCC N   1 ? 11 
ATOM   3311  C CA  . PRO C  1 97  ? 20.362  -84.998  5.875   1.000 47.955  0 426 PRO CCC CA  1 ? 11 
ATOM   3312  C C   . PRO C  1 97  ? 21.690  -84.886  6.627   1.000 48.453  0 426 PRO CCC C   1 ? 11 
ATOM   3313  O O   . PRO C  1 97  ? 22.400  -83.910  6.446   1.000 51.844  0 426 PRO CCC O   1 ? 11 
ATOM   3314  C CB  . PRO C  1 97  ? 20.556  -85.730  4.528   1.000 46.277  0 426 PRO CCC CB  1 ? 11 
ATOM   3315  C CG  . PRO C  1 97  ? 20.838  -84.640  3.553   1.000 44.380  0 426 PRO CCC CG  1 ? 11 
ATOM   3316  C CD  . PRO C  1 97  ? 19.942  -83.512  4.004   1.000 44.122  0 426 PRO CCC CD  1 ? 11 
ATOM   3317  N N   . ASP C  1 98  ? 22.030  -85.903  7.397   1.000 53.751  0 427 ASP CCC N   1 ? 11 
ATOM   3318  C CA  . ASP C  1 98  ? 23.288  -85.896  8.188   1.000 57.242  0 427 ASP CCC CA  1 ? 11 
ATOM   3319  C C   . ASP C  1 98  ? 24.484  -85.978  7.239   1.000 58.316  0 427 ASP CCC C   1 ? 11 
ATOM   3320  O O   . ASP C  1 98  ? 25.526  -85.388  7.596   1.000 58.793  0 427 ASP CCC O   1 ? 11 
ATOM   3321  C CB  . ASP C  1 98  ? 23.334  -86.983  9.258   1.000 62.867  0 427 ASP CCC CB  1 ? 11 
ATOM   3322  C CG  . ASP C  1 98  ? 23.372  -86.364  10.645  1.000 70.153  0 427 ASP CCC CG  1 ? 11 
ATOM   3323  O OD1 . ASP C  1 98  ? 24.369  -85.623  10.943  1.000 71.664  0 427 ASP CCC OD1 1 ? 11 
ATOM   3324  O OD2 . ASP C  1 98  ? 22.376  -86.565  11.396  1.000 75.755  0 427 ASP CCC OD2 1 ? 11 
ATOM   3325  N N   . ASP C  1 99  ? 24.338  -86.645  6.070   1.000 55.401  0 428 ASP CCC N   1 ? 11 
ATOM   3326  C CA  . ASP C  1 99  ? 25.440  -86.857  5.100   1.000 53.612  0 428 ASP CCC CA  1 ? 11 
ATOM   3327  C C   . ASP C  1 99  ? 25.332  -85.837  3.955   1.000 51.870  0 428 ASP CCC C   1 ? 11 
ATOM   3328  O O   . ASP C  1 99  ? 25.839  -86.119  2.846   1.000 51.665  0 428 ASP CCC O   1 ? 11 
ATOM   3329  C CB  . ASP C  1 99  ? 25.418  -88.302  4.611   1.000 55.058  0 428 ASP CCC CB  1 ? 11 
ATOM   3330  C CG  . ASP C  1 99  ? 24.253  -88.652  3.679   1.000 56.497  0 428 ASP CCC CG  1 ? 11 
ATOM   3331  O OD1 . ASP C  1 99  ? 23.312  -87.868  3.581   1.000 51.788  0 428 ASP CCC OD1 1 ? 11 
ATOM   3332  O OD2 . ASP C  1 99  ? 24.316  -89.705  3.013   1.000 60.900  0 428 ASP CCC OD2 1 ? 11 
ATOM   3333  N N   . PHE C  1 100 ? 24.690  -84.690  4.198   1.000 47.379  0 429 PHE CCC N   1 ? 11 
ATOM   3334  C CA  . PHE C  1 100 ? 24.562  -83.620  3.189   1.000 46.036  0 429 PHE CCC CA  1 ? 11 
ATOM   3335  C C   . PHE C  1 100 ? 25.933  -83.343  2.533   1.000 45.054  0 429 PHE CCC C   1 ? 11 
ATOM   3336  O O   . PHE C  1 100 ? 26.958  -83.160  3.232   1.000 45.964  0 429 PHE CCC O   1 ? 11 
ATOM   3337  C CB  . PHE C  1 100 ? 24.046  -82.350  3.851   1.000 46.224  0 429 PHE CCC CB  1 ? 11 
ATOM   3338  C CG  . PHE C  1 100 ? 23.972  -81.151  2.948   1.000 43.906  0 429 PHE CCC CG  1 ? 11 
ATOM   3339  C CD1 . PHE C  1 100 ? 23.200  -81.221  1.807   1.000 43.181  0 429 PHE CCC CD1 1 ? 11 
ATOM   3340  C CD2 . PHE C  1 100 ? 24.626  -79.957  3.252   1.000 44.560  0 429 PHE CCC CD2 1 ? 11 
ATOM   3341  C CE1 . PHE C  1 100 ? 23.093  -80.134  0.974   1.000 43.271  0 429 PHE CCC CE1 1 ? 11 
ATOM   3342  C CE2 . PHE C  1 100 ? 24.520  -78.866  2.395   1.000 43.475  0 429 PHE CCC CE2 1 ? 11 
ATOM   3343  C CZ  . PHE C  1 100 ? 23.746  -78.957  1.265   1.000 42.651  0 429 PHE CCC CZ  1 ? 11 
ATOM   3344  N N   . THR C  1 101 ? 25.950  -83.257  1.212   1.000 43.845  0 430 THR CCC N   1 ? 11 
ATOM   3345  C CA  . THR C  1 101 ? 27.083  -82.747  0.412   1.000 44.551  0 430 THR CCC CA  1 ? 11 
ATOM   3346  C C   . THR C  1 101 ? 26.593  -81.492  -0.304  1.000 43.463  0 430 THR CCC C   1 ? 11 
ATOM   3347  O O   . THR C  1 101 ? 25.726  -81.610  -1.167  1.000 45.578  0 430 THR CCC O   1 ? 11 
ATOM   3348  C CB  . THR C  1 101 ? 27.610  -83.803  -0.575  1.000 45.892  0 430 THR CCC CB  1 ? 11 
ATOM   3349  O OG1 . THR C  1 101 ? 28.016  -84.925  0.203   1.000 46.505  0 430 THR CCC OG1 1 ? 11 
ATOM   3350  C CG2 . THR C  1 101 ? 28.789  -83.335  -1.394  1.000 45.330  0 430 THR CCC CG2 1 ? 11 
ATOM   3351  N N   . GLY C  1 102 ? 27.172  -80.340  0.011   1.000 43.651  0 431 GLY CCC N   1 ? 11 
ATOM   3352  C CA  . GLY C  1 102 ? 26.782  -79.074  -0.627  1.000 44.607  0 431 GLY CCC CA  1 ? 11 
ATOM   3353  C C   . GLY C  1 102 ? 27.134  -77.862  0.189   1.000 43.102  0 431 GLY CCC C   1 ? 11 
ATOM   3354  O O   . GLY C  1 102 ? 27.964  -77.989  1.098   1.000 45.278  0 431 GLY CCC O   1 ? 11 
ATOM   3355  N N   . CYS C  1 103 ? 26.538  -76.721  -0.140  1.000 41.201  0 432 CYS CCC N   1 ? 11 
ATOM   3356  C CA  . CYS C  1 103 ? 26.825  -75.445  0.557   1.000 43.821  0 432 CYS CCC CA  1 ? 11 
ATOM   3357  C C   . CYS C  1 103 ? 25.517  -74.765  0.960   1.000 41.293  0 432 CYS CCC C   1 ? 11 
ATOM   3358  O O   . CYS C  1 103 ? 24.503  -74.952  0.280   1.000 39.198  0 432 CYS CCC O   1 ? 11 
ATOM   3359  C CB  . CYS C  1 103 ? 27.678  -74.514  -0.297  1.000 45.682  0 432 CYS CCC CB  1 ? 11 
ATOM   3360  S SG  . CYS C  1 103 ? 29.164  -75.311  -0.965  1.000 48.998  0 432 CYS CCC SG  1 ? 11 
ATOM   3361  N N   . VAL C  1 104 ? 25.577  -74.025  2.056   1.000 39.920  0 433 VAL CCC N   1 ? 11 
ATOM   3362  C CA  . VAL C  1 104 ? 24.448  -73.232  2.597   1.000 39.874  0 433 VAL CCC CA  1 ? 11 
ATOM   3363  C C   . VAL C  1 104 ? 24.910  -71.778  2.643   1.000 39.070  0 433 VAL CCC C   1 ? 11 
ATOM   3364  O O   . VAL C  1 104 ? 25.957  -71.493  3.280   1.000 40.968  0 433 VAL CCC O   1 ? 11 
ATOM   3365  C CB  . VAL C  1 104 ? 24.044  -73.745  3.984   1.000 41.233  0 433 VAL CCC CB  1 ? 11 
ATOM   3366  C CG1 . VAL C  1 104 ? 22.967  -72.854  4.600   1.000 41.658  0 433 VAL CCC CG1 1 ? 11 
ATOM   3367  C CG2 . VAL C  1 104 ? 23.614  -75.206  3.930   1.000 42.969  0 433 VAL CCC CG2 1 ? 11 
ATOM   3368  N N   . ILE C  1 105 ? 24.189  -70.923  1.934   1.000 38.577  0 434 ILE CCC N   1 ? 11 
ATOM   3369  C CA  . ILE C  1 105 ? 24.507  -69.474  1.813   1.000 40.411  0 434 ILE CCC CA  1 ? 11 
ATOM   3370  C C   . ILE C  1 105 ? 23.255  -68.718  2.233   1.000 39.513  0 434 ILE CCC C   1 ? 11 
ATOM   3371  O O   . ILE C  1 105 ? 22.152  -69.116  1.838   1.000 41.417  0 434 ILE CCC O   1 ? 11 
ATOM   3372  C CB  . ILE C  1 105 ? 24.978  -69.108  0.388   1.000 39.675  0 434 ILE CCC CB  1 ? 11 
ATOM   3373  C CG1 . ILE C  1 105 ? 26.208  -69.922  -0.001  1.000 39.916  0 434 ILE CCC CG1 1 ? 11 
ATOM   3374  C CG2 . ILE C  1 105 ? 25.231  -67.622  0.271   1.000 39.211  0 434 ILE CCC CG2 1 ? 11 
ATOM   3375  C CD1 . ILE C  1 105 ? 26.524  -69.906  -1.461  1.000 41.240  0 434 ILE CCC CD1 1 ? 11 
ATOM   3376  N N   . ALA C  1 106 ? 23.433  -67.685  3.041   1.000 41.186  0 435 ALA CCC N   1 ? 11 
ATOM   3377  C CA  . ALA C  1 106 ? 22.335  -66.804  3.474   1.000 41.528  0 435 ALA CCC CA  1 ? 11 
ATOM   3378  C C   . ALA C  1 106 ? 22.824  -65.359  3.446   1.000 41.488  0 435 ALA CCC C   1 ? 11 
ATOM   3379  O O   . ALA C  1 106 ? 24.053  -65.144  3.510   1.000 43.546  0 435 ALA CCC O   1 ? 11 
ATOM   3380  C CB  . ALA C  1 106 ? 21.819  -67.226  4.823   1.000 40.013  0 435 ALA CCC CB  1 ? 11 
ATOM   3381  N N   . TRP C  1 107 ? 21.885  -64.430  3.324   1.000 41.739  0 436 TRP CCC N   1 ? 11 
ATOM   3382  C CA  . TRP C  1 107 ? 22.150  -62.977  3.406   1.000 41.633  0 436 TRP CCC CA  1 ? 11 
ATOM   3383  C C   . TRP C  1 107 ? 20.892  -62.270  3.915   1.000 42.747  0 436 TRP CCC C   1 ? 11 
ATOM   3384  O O   . TRP C  1 107 ? 19.772  -62.769  3.685   1.000 43.714  0 436 TRP CCC O   1 ? 11 
ATOM   3385  C CB  . TRP C  1 107 ? 22.609  -62.423  2.051   1.000 40.829  0 436 TRP CCC CB  1 ? 11 
ATOM   3386  C CG  . TRP C  1 107 ? 21.607  -62.492  0.949   1.000 39.576  0 436 TRP CCC CG  1 ? 11 
ATOM   3387  C CD1 . TRP C  1 107 ? 20.784  -61.490  0.557   1.000 38.871  0 436 TRP CCC CD1 1 ? 11 
ATOM   3388  C CD2 . TRP C  1 107 ? 21.289  -63.619  0.110   1.000 39.104  0 436 TRP CCC CD2 1 ? 11 
ATOM   3389  N NE1 . TRP C  1 107 ? 19.963  -61.916  -0.452  1.000 38.809  0 436 TRP CCC NE1 1 ? 11 
ATOM   3390  C CE2 . TRP C  1 107 ? 20.247  -63.209  -0.751  1.000 37.310  0 436 TRP CCC CE2 1 ? 11 
ATOM   3391  C CE3 . TRP C  1 107 ? 21.771  -64.928  0.016   1.000 40.029  0 436 TRP CCC CE3 1 ? 11 
ATOM   3392  C CZ2 . TRP C  1 107 ? 19.690  -64.040  -1.711  1.000 38.199  0 436 TRP CCC CZ2 1 ? 11 
ATOM   3393  C CZ3 . TRP C  1 107 ? 21.232  -65.754  -0.949  1.000 40.991  0 436 TRP CCC CZ3 1 ? 11 
ATOM   3394  C CH2 . TRP C  1 107 ? 20.203  -65.312  -1.805  1.000 40.305  0 436 TRP CCC CH2 1 ? 11 
ATOM   3395  N N   . ASN C  1 108 ? 21.113  -61.185  4.648   1.000 41.335  0 437 ASN CCC N   1 ? 11 
ATOM   3396  C CA  . ASN C  1 108 ? 20.059  -60.281  5.138   1.000 40.633  0 437 ASN CCC CA  1 ? 11 
ATOM   3397  C C   . ASN C  1 108 ? 19.284  -59.739  3.929   1.000 39.950  0 437 ASN CCC C   1 ? 11 
ATOM   3398  O O   . ASN C  1 108 ? 19.926  -59.231  2.993   1.000 37.710  0 437 ASN CCC O   1 ? 11 
ATOM   3399  C CB  . ASN C  1 108 ? 20.690  -59.172  5.962   1.000 41.740  0 437 ASN CCC CB  1 ? 11 
ATOM   3400  C CG  . ASN C  1 108 ? 19.630  -58.343  6.626   1.000 43.468  0 437 ASN CCC CG  1 ? 11 
ATOM   3401  O OD1 . ASN C  1 108 ? 18.904  -57.650  5.945   1.000 46.171  0 437 ASN CCC OD1 1 ? 11 
ATOM   3402  N ND2 . ASN C  1 108 ? 19.514  -58.448  7.937   1.000 44.441  0 437 ASN CCC ND2 1 ? 11 
ATOM   3403  N N   . SER C  1 109 ? 17.957  -59.856  3.939   1.000 39.133  0 438 SER CCC N   1 ? 11 
ATOM   3404  C CA  . SER C  1 109 ? 17.073  -59.364  2.851   1.000 39.101  0 438 SER CCC CA  1 ? 11 
ATOM   3405  C C   . SER C  1 109 ? 16.077  -58.362  3.412   1.000 38.842  0 438 SER CCC C   1 ? 11 
ATOM   3406  O O   . SER C  1 109 ? 14.996  -58.201  2.823   1.000 41.013  0 438 SER CCC O   1 ? 11 
ATOM   3407  C CB  . SER C  1 109 ? 16.380  -60.496  2.161   1.000 37.873  0 438 SER CCC CB  1 ? 11 
ATOM   3408  O OG  . SER C  1 109 ? 15.594  -61.236  3.078   1.000 40.036  0 438 SER CCC OG  1 ? 11 
ATOM   3409  N N   . ASN C  1 110 ? 16.450  -57.675  4.485   1.000 38.984  0 439 ASN CCC N   1 ? 11 
ATOM   3410  C CA  . ASN C  1 110 ? 15.566  -56.683  5.135   1.000 40.642  0 439 ASN CCC CA  1 ? 11 
ATOM   3411  C C   . ASN C  1 110 ? 15.100  -55.677  4.070   1.000 41.460  0 439 ASN CCC C   1 ? 11 
ATOM   3412  O O   . ASN C  1 110 ? 13.915  -55.368  4.064   1.000 41.680  0 439 ASN CCC O   1 ? 11 
ATOM   3413  C CB  . ASN C  1 110 ? 16.266  -56.020  6.328   1.000 43.014  0 439 ASN CCC CB  1 ? 11 
ATOM   3414  C CG  . ASN C  1 110 ? 15.316  -55.356  7.282   1.000 44.681  0 439 ASN CCC CG  1 ? 11 
ATOM   3415  O OD1 . ASN C  1 110 ? 14.191  -55.837  7.469   1.000 44.661  0 439 ASN CCC OD1 1 ? 11 
ATOM   3416  N ND2 . ASN C  1 110 ? 15.778  -54.291  7.918   1.000 47.154  0 439 ASN CCC ND2 1 ? 11 
ATOM   3417  N N   . ASN C  1 111 ? 15.976  -55.216  3.182   1.000 42.336  0 440 ASN CCC N   1 ? 11 
ATOM   3418  C CA  . ASN C  1 111 ? 15.658  -54.149  2.195   1.000 45.094  0 440 ASN CCC CA  1 ? 11 
ATOM   3419  C C   . ASN C  1 111 ? 14.579  -54.629  1.201   1.000 47.539  0 440 ASN CCC C   1 ? 11 
ATOM   3420  O O   . ASN C  1 111 ? 13.831  -53.778  0.669   1.000 52.191  0 440 ASN CCC O   1 ? 11 
ATOM   3421  C CB  . ASN C  1 111 ? 16.878  -53.635  1.424   1.000 45.552  0 440 ASN CCC CB  1 ? 11 
ATOM   3422  C CG  . ASN C  1 111 ? 16.520  -52.472  0.517   1.000 48.701  0 440 ASN CCC CG  1 ? 11 
ATOM   3423  O OD1 . ASN C  1 111 ? 16.212  -52.647  -0.652  1.000 49.347  0 440 ASN CCC OD1 1 ? 11 
ATOM   3424  N ND2 . ASN C  1 111 ? 16.462  -51.271  1.070   1.000 53.805  0 440 ASN CCC ND2 1 ? 11 
ATOM   3425  N N   . LEU C  1 112 ? 14.481  -55.934  0.932   1.000 46.170  0 441 LEU CCC N   1 ? 11 
ATOM   3426  C CA  . LEU C  1 112 ? 13.559  -56.480  -0.089  1.000 46.009  0 441 LEU CCC CA  1 ? 11 
ATOM   3427  C C   . LEU C  1 112 ? 12.320  -57.078  0.573   1.000 46.790  0 441 LEU CCC C   1 ? 11 
ATOM   3428  O O   . LEU C  1 112 ? 11.247  -56.947  -0.022  1.000 50.285  0 441 LEU CCC O   1 ? 11 
ATOM   3429  C CB  . LEU C  1 112 ? 14.289  -57.539  -0.913  1.000 45.007  0 441 LEU CCC CB  1 ? 11 
ATOM   3430  C CG  . LEU C  1 112 ? 15.407  -57.034  -1.834  1.000 44.178  0 441 LEU CCC CG  1 ? 11 
ATOM   3431  C CD1 . LEU C  1 112 ? 15.966  -58.142  -2.696  1.000 41.997  0 441 LEU CCC CD1 1 ? 11 
ATOM   3432  C CD2 . LEU C  1 112 ? 14.930  -55.915  -2.743  1.000 46.375  0 441 LEU CCC CD2 1 ? 11 
ATOM   3433  N N   . ASP C  1 113 ? 12.455  -57.703  1.745   1.000 46.829  0 442 ASP CCC N   1 ? 11 
ATOM   3434  C CA  . ASP C  1 113 ? 11.433  -58.628  2.298   1.000 48.337  0 442 ASP CCC CA  1 ? 11 
ATOM   3435  C C   . ASP C  1 113 ? 10.720  -58.049  3.526   1.000 52.171  0 442 ASP CCC C   1 ? 11 
ATOM   3436  O O   . ASP C  1 113 ? 9.894   -58.769  4.109   1.000 58.728  0 442 ASP CCC O   1 ? 11 
ATOM   3437  C CB  . ASP C  1 113 ? 12.078  -59.960  2.654   1.000 45.653  0 442 ASP CCC CB  1 ? 11 
ATOM   3438  C CG  . ASP C  1 113 ? 12.443  -60.801  1.446   1.000 45.162  0 442 ASP CCC CG  1 ? 11 
ATOM   3439  O OD1 . ASP C  1 113 ? 11.691  -60.760  0.440   1.000 43.666  0 442 ASP CCC OD1 1 ? 11 
ATOM   3440  O OD2 . ASP C  1 113 ? 13.479  -61.508  1.522   1.000 43.205  0 442 ASP CCC OD2 1 ? 11 
ATOM   3441  N N   . SER C  1 114 ? 10.987  -56.821  3.932   1.000 53.404  0 443 SER CCC N   1 ? 11 
ATOM   3442  C CA  . SER C  1 114 ? 10.291  -56.229  5.102   1.000 58.312  0 443 SER CCC CA  1 ? 11 
ATOM   3443  C C   . SER C  1 114 ? 9.528   -54.993  4.628   1.000 59.176  0 443 SER CCC C   1 ? 11 
ATOM   3444  O O   . SER C  1 114 ? 9.934   -54.418  3.649   1.000 60.103  0 443 SER CCC O   1 ? 11 
ATOM   3445  C CB  . SER C  1 114 ? 11.266  -55.984  6.222   1.000 59.437  0 443 SER CCC CB  1 ? 11 
ATOM   3446  O OG  . SER C  1 114 ? 11.889  -54.733  6.063   1.000 68.090  0 443 SER CCC OG  1 ? 11 
ATOM   3447  N N   . LYS C  1 115 ? 8.385   -54.692  5.228   1.000 64.312  0 444 LYS CCC N   1 ? 11 
ATOM   3448  C CA  . LYS C  1 115 ? 7.504   -53.557  4.839   1.000 71.291  0 444 LYS CCC CA  1 ? 11 
ATOM   3449  C C   . LYS C  1 115 ? 7.122   -52.766  6.080   1.000 73.376  0 444 LYS CCC C   1 ? 11 
ATOM   3450  O O   . LYS C  1 115 ? 7.134   -53.349  7.163   1.000 69.725  0 444 LYS CCC O   1 ? 11 
ATOM   3451  C CB  . LYS C  1 115 ? 6.218   -54.049  4.165   1.000 77.821  0 444 LYS CCC CB  1 ? 11 
ATOM   3452  C CG  . LYS C  1 115 ? 6.295   -54.129  2.638   1.000 84.773  0 444 LYS CCC CG  1 ? 11 
ATOM   3453  C CD  . LYS C  1 115 ? 5.676   -55.368  1.996   1.000 88.920  0 444 LYS CCC CD  1 ? 11 
ATOM   3454  C CE  . LYS C  1 115 ? 6.604   -56.056  1.012   1.000 89.187  0 444 LYS CCC CE  1 ? 11 
ATOM   3455  N NZ  . LYS C  1 115 ? 5.868   -57.161  0.367   1.000 91.098  0 444 LYS CCC NZ  1 ? 11 
ATOM   3456  N N   . VAL C  1 116 ? 6.762   -51.502  5.890   1.000 74.238  0 445 VAL CCC N   1 ? 11 
ATOM   3457  C CA  . VAL C  1 116 ? 6.394   -50.556  6.977   1.000 77.081  0 445 VAL CCC CA  1 ? 11 
ATOM   3458  C C   . VAL C  1 116 ? 5.275   -51.116  7.865   1.000 72.910  0 445 VAL CCC C   1 ? 11 
ATOM   3459  O O   . VAL C  1 116 ? 5.426   -50.951  9.084   1.000 71.726  0 445 VAL CCC O   1 ? 11 
ATOM   3460  C CB  . VAL C  1 116 ? 6.050   -49.157  6.427   1.000 82.624  0 445 VAL CCC CB  1 ? 11 
ATOM   3461  C CG1 . VAL C  1 116 ? 7.291   -48.480  5.845   1.000 82.501  0 445 VAL CCC CG1 1 ? 11 
ATOM   3462  C CG2 . VAL C  1 116 ? 4.906   -49.199  5.402   1.000 84.044  0 445 VAL CCC CG2 1 ? 11 
ATOM   3463  N N   . GLY C  1 117 ? 4.232   -51.756  7.331   1.000 69.694  0 446 GLY CCC N   1 ? 11 
ATOM   3464  C CA  . GLY C  1 117 ? 3.162   -52.324  8.173   1.000 71.218  0 446 GLY CCC CA  1 ? 11 
ATOM   3465  C C   . GLY C  1 117 ? 3.512   -53.693  8.730   1.000 68.996  0 446 GLY CCC C   1 ? 11 
ATOM   3466  O O   . GLY C  1 117 ? 2.632   -54.336  9.305   1.000 68.330  0 446 GLY CCC O   1 ? 11 
ATOM   3467  N N   . GLY C  1 118 ? 4.702   -54.212  8.417   1.000 66.868  0 447 GLY CCC N   1 ? 11 
ATOM   3468  C CA  . GLY C  1 118 ? 5.048   -55.643  8.527   1.000 65.784  0 447 GLY CCC CA  1 ? 11 
ATOM   3469  C C   . GLY C  1 118 ? 4.686   -56.413  7.262   1.000 64.975  0 447 GLY CCC C   1 ? 11 
ATOM   3470  O O   . GLY C  1 118 ? 3.553   -56.245  6.778   1.000 65.129  0 447 GLY CCC O   1 ? 11 
ATOM   3471  N N   . ASN C  1 119 ? 5.615   -57.220  6.738   1.000 62.049  0 448 ASN CCC N   1 ? 11 
ATOM   3472  C CA  . ASN C  1 119 ? 5.360   -58.175  5.636   1.000 61.227  0 448 ASN CCC CA  1 ? 11 
ATOM   3473  C C   . ASN C  1 119 ? 4.911   -59.509  6.241   1.000 61.908  0 448 ASN CCC C   1 ? 11 
ATOM   3474  O O   . ASN C  1 119 ? 5.720   -60.165  6.914   1.000 61.531  0 448 ASN CCC O   1 ? 11 
ATOM   3475  C CB  . ASN C  1 119 ? 6.582   -58.317  4.731   1.000 60.285  0 448 ASN CCC CB  1 ? 11 
ATOM   3476  C CG  . ASN C  1 119 ? 6.367   -59.290  3.594   1.000 60.609  0 448 ASN CCC CG  1 ? 11 
ATOM   3477  O OD1 . ASN C  1 119 ? 5.237   -59.696  3.312   1.000 59.605  0 448 ASN CCC OD1 1 ? 11 
ATOM   3478  N ND2 . ASN C  1 119 ? 7.452   -59.662  2.938   1.000 61.653  0 448 ASN CCC ND2 1 ? 11 
ATOM   3479  N N   . TYR C  1 120 ? 3.659   -59.890  6.002   1.000 63.461  0 449 TYR CCC N   1 ? 11 
ATOM   3480  C CA  . TYR C  1 120 ? 3.039   -61.112  6.567   1.000 64.869  0 449 TYR CCC CA  1 ? 11 
ATOM   3481  C C   . TYR C  1 120 ? 2.965   -62.194  5.481   1.000 65.853  0 449 TYR CCC C   1 ? 11 
ATOM   3482  O O   . TYR C  1 120 ? 2.403   -63.252  5.757   1.000 68.368  0 449 TYR CCC O   1 ? 11 
ATOM   3483  C CB  . TYR C  1 120 ? 1.695   -60.754  7.235   1.000 68.490  0 449 TYR CCC CB  1 ? 11 
ATOM   3484  C CG  . TYR C  1 120 ? 1.835   -59.867  8.456   1.000 69.270  0 449 TYR CCC CG  1 ? 11 
ATOM   3485  C CD1 . TYR C  1 120 ? 2.250   -60.382  9.679   1.000 68.617  0 449 TYR CCC CD1 1 ? 11 
ATOM   3486  C CD2 . TYR C  1 120 ? 1.618   -58.500  8.385   1.000 71.158  0 449 TYR CCC CD2 1 ? 11 
ATOM   3487  C CE1 . TYR C  1 120 ? 2.418   -59.579  10.794  1.000 70.502  0 449 TYR CCC CE1 1 ? 11 
ATOM   3488  C CE2 . TYR C  1 120 ? 1.789   -57.674  9.490   1.000 73.168  0 449 TYR CCC CE2 1 ? 11 
ATOM   3489  C CZ  . TYR C  1 120 ? 2.167   -58.219  10.706  1.000 73.600  0 449 TYR CCC CZ  1 ? 11 
ATOM   3490  O OH  . TYR C  1 120 ? 2.344   -57.429  11.811  1.000 74.588  0 449 TYR CCC OH  1 ? 11 
ATOM   3491  N N   . ASN C  1 121 ? 3.586   -61.985  4.312   1.000 66.225  0 450 ASN CCC N   1 ? 11 
ATOM   3492  C CA  . ASN C  1 121 ? 3.562   -62.971  3.193   1.000 63.891  0 450 ASN CCC CA  1 ? 11 
ATOM   3493  C C   . ASN C  1 121 ? 4.438   -64.197  3.506   1.000 58.666  0 450 ASN CCC C   1 ? 11 
ATOM   3494  O O   . ASN C  1 121 ? 4.112   -65.266  2.976   1.000 54.290  0 450 ASN CCC O   1 ? 11 
ATOM   3495  C CB  . ASN C  1 121 ? 3.997   -62.356  1.864   1.000 65.599  0 450 ASN CCC CB  1 ? 11 
ATOM   3496  C CG  . ASN C  1 121 ? 2.969   -61.403  1.310   1.000 70.092  0 450 ASN CCC CG  1 ? 11 
ATOM   3497  O OD1 . ASN C  1 121 ? 1.798   -61.418  1.688   1.000 68.985  0 450 ASN CCC OD1 1 ? 11 
ATOM   3498  N ND2 . ASN C  1 121 ? 3.422   -60.560  0.405   1.000 74.514  0 450 ASN CCC ND2 1 ? 11 
ATOM   3499  N N   . TYR C  1 122 ? 5.504   -64.079  4.307   1.000 53.689  0 451 TYR CCC N   1 ? 11 
ATOM   3500  C CA  . TYR C  1 122 ? 6.383   -65.232  4.597   1.000 49.385  0 451 TYR CCC CA  1 ? 11 
ATOM   3501  C C   . TYR C  1 122 ? 5.855   -65.999  5.810   1.000 48.493  0 451 TYR CCC C   1 ? 11 
ATOM   3502  O O   . TYR C  1 122 ? 5.638   -65.395  6.891   1.000 45.104  0 451 TYR CCC O   1 ? 11 
ATOM   3503  C CB  . TYR C  1 122 ? 7.831   -64.793  4.763   1.000 49.226  0 451 TYR CCC CB  1 ? 11 
ATOM   3504  C CG  . TYR C  1 122 ? 8.464   -64.293  3.496   1.000 48.308  0 451 TYR CCC CG  1 ? 11 
ATOM   3505  C CD1 . TYR C  1 122 ? 8.809   -65.162  2.470   1.000 47.500  0 451 TYR CCC CD1 1 ? 11 
ATOM   3506  C CD2 . TYR C  1 122 ? 8.747   -62.955  3.335   1.000 48.152  0 451 TYR CCC CD2 1 ? 11 
ATOM   3507  C CE1 . TYR C  1 122 ? 9.416   -64.701  1.310   1.000 46.609  0 451 TYR CCC CE1 1 ? 11 
ATOM   3508  C CE2 . TYR C  1 122 ? 9.324   -62.479  2.175   1.000 47.504  0 451 TYR CCC CE2 1 ? 11 
ATOM   3509  C CZ  . TYR C  1 122 ? 9.680   -63.356  1.168   1.000 46.542  0 451 TYR CCC CZ  1 ? 11 
ATOM   3510  O OH  . TYR C  1 122 ? 10.292  -62.894  0.037   1.000 43.544  0 451 TYR CCC OH  1 ? 11 
ATOM   3511  N N   . LEU C  1 123 ? 5.662   -67.311  5.607   1.000 47.771  0 452 LEU CCC N   1 ? 11 
ATOM   3512  C CA  . LEU C  1 123 ? 5.061   -68.238  6.590   1.000 49.375  0 452 LEU CCC CA  1 ? 11 
ATOM   3513  C C   . LEU C  1 123 ? 6.106   -69.287  6.981   1.000 48.198  0 452 LEU CCC C   1 ? 11 
ATOM   3514  O O   . LEU C  1 123 ? 7.049   -69.557  6.195   1.000 46.970  0 452 LEU CCC O   1 ? 11 
ATOM   3515  C CB  . LEU C  1 123 ? 3.824   -68.894  5.971   1.000 50.369  0 452 LEU CCC CB  1 ? 11 
ATOM   3516  C CG  . LEU C  1 123 ? 2.724   -67.951  5.475   1.000 51.903  0 452 LEU CCC CG  1 ? 11 
ATOM   3517  C CD1 . LEU C  1 123 ? 1.579   -68.682  4.823   1.000 53.717  0 452 LEU CCC CD1 1 ? 11 
ATOM   3518  C CD2 . LEU C  1 123 ? 2.230   -67.057  6.587   1.000 52.925  0 452 LEU CCC CD2 1 ? 11 
ATOM   3519  N N   . TYR C  1 124 ? 5.919   -69.882  8.156   1.000 49.299  0 453 TYR CCC N   1 ? 11 
ATOM   3520  C CA  . TYR C  1 124 ? 6.651   -71.091  8.608   1.000 47.718  0 453 TYR CCC CA  1 ? 11 
ATOM   3521  C C   . TYR C  1 124 ? 5.641   -72.022  9.285   1.000 48.952  0 453 TYR CCC C   1 ? 11 
ATOM   3522  O O   . TYR C  1 124 ? 4.662   -71.523  9.853   1.000 49.216  0 453 TYR CCC O   1 ? 11 
ATOM   3523  C CB  . TYR C  1 124 ? 7.814   -70.710  9.523   1.000 44.644  0 453 TYR CCC CB  1 ? 11 
ATOM   3524  C CG  . TYR C  1 124 ? 7.375   -70.061  10.805  1.000 45.610  0 453 TYR CCC CG  1 ? 11 
ATOM   3525  C CD1 . TYR C  1 124 ? 7.193   -68.686  10.889  1.000 45.963  0 453 TYR CCC CD1 1 ? 11 
ATOM   3526  C CD2 . TYR C  1 124 ? 7.146   -70.823  11.939  1.000 45.597  0 453 TYR CCC CD2 1 ? 11 
ATOM   3527  C CE1 . TYR C  1 124 ? 6.806   -68.084  12.072  1.000 47.263  0 453 TYR CCC CE1 1 ? 11 
ATOM   3528  C CE2 . TYR C  1 124 ? 6.748   -70.246  13.129  1.000 47.108  0 453 TYR CCC CE2 1 ? 11 
ATOM   3529  C CZ  . TYR C  1 124 ? 6.591   -68.871  13.195  1.000 48.757  0 453 TYR CCC CZ  1 ? 11 
ATOM   3530  O OH  . TYR C  1 124 ? 6.189   -68.323  14.379  1.000 51.529  0 453 TYR CCC OH  1 ? 11 
ATOM   3531  N N   . ARG C  1 125 ? 5.875   -73.333  9.218   1.000 49.309  0 454 ARG CCC N   1 ? 11 
ATOM   3532  C CA  . ARG C  1 125 ? 5.066   -74.326  9.960   1.000 51.918  0 454 ARG CCC CA  1 ? 11 
ATOM   3533  C C   . ARG C  1 125 ? 5.489   -74.278  11.430  1.000 53.230  0 454 ARG CCC C   1 ? 11 
ATOM   3534  O O   . ARG C  1 125 ? 6.688   -74.435  11.713  1.000 52.366  0 454 ARG CCC O   1 ? 11 
ATOM   3535  C CB  . ARG C  1 125 ? 5.220   -75.713  9.336   1.000 52.051  0 454 ARG CCC CB  1 ? 11 
ATOM   3536  C CG  . ARG C  1 125 ? 4.284   -76.750  9.935   1.000 54.661  0 454 ARG CCC CG  1 ? 11 
ATOM   3537  C CD  . ARG C  1 125 ? 4.352   -78.060  9.177   1.000 54.487  0 454 ARG CCC CD  1 ? 11 
ATOM   3538  N NE  . ARG C  1 125 ? 4.012   -77.890  7.778   1.000 56.580  0 454 ARG CCC NE  1 ? 11 
ATOM   3539  C CZ  . ARG C  1 125 ? 2.774   -77.734  7.297   1.000 58.892  0 454 ARG CCC CZ  1 ? 11 
ATOM   3540  N NH1 . ARG C  1 125 ? 1.709   -77.762  8.091   1.000 60.528  0 454 ARG CCC NH1 1 ? 11 
ATOM   3541  N NH2 . ARG C  1 125 ? 2.610   -77.537  6.000   1.000 60.479  0 454 ARG CCC NH2 1 ? 11 
ATOM   3542  N N   . LEU C  1 126 ? 4.532   -74.026  12.321  1.000 55.560  0 455 LEU CCC N   1 ? 11 
ATOM   3543  C CA  . LEU C  1 126 ? 4.767   -73.852  13.782  1.000 56.519  0 455 LEU CCC CA  1 ? 11 
ATOM   3544  C C   . LEU C  1 126 ? 4.497   -75.168  14.515  1.000 56.982  0 455 LEU CCC C   1 ? 11 
ATOM   3545  O O   . LEU C  1 126 ? 5.157   -75.419  15.531  1.000 59.330  0 455 LEU CCC O   1 ? 11 
ATOM   3546  C CB  . LEU C  1 126 ? 3.832   -72.738  14.259  1.000 58.780  0 455 LEU CCC CB  1 ? 11 
ATOM   3547  C CG  . LEU C  1 126 ? 3.796   -72.463  15.758  1.000 62.680  0 455 LEU CCC CG  1 ? 11 
ATOM   3548  C CD1 . LEU C  1 126 ? 5.180   -72.140  16.303  1.000 61.733  0 455 LEU CCC CD1 1 ? 11 
ATOM   3549  C CD2 . LEU C  1 126 ? 2.810   -71.332  16.036  1.000 63.670  0 455 LEU CCC CD2 1 ? 11 
ATOM   3550  N N   . PHE C  1 127 ? 3.548   -75.956  14.017  1.000 59.026  0 456 PHE CCC N   1 ? 11 
ATOM   3551  C CA  . PHE C  1 127 ? 3.062   -77.227  14.613  1.000 60.481  0 456 PHE CCC CA  1 ? 11 
ATOM   3552  C C   . PHE C  1 127 ? 3.110   -78.325  13.554  1.000 59.218  0 456 PHE CCC C   1 ? 11 
ATOM   3553  O O   . PHE C  1 127 ? 2.751   -78.108  12.400  1.000 59.669  0 456 PHE CCC O   1 ? 11 
ATOM   3554  C CB  . PHE C  1 127 ? 1.630   -77.096  15.138  1.000 62.747  0 456 PHE CCC CB  1 ? 11 
ATOM   3555  C CG  . PHE C  1 127 ? 1.418   -75.974  16.124  1.000 64.763  0 456 PHE CCC CG  1 ? 11 
ATOM   3556  C CD1 . PHE C  1 127 ? 1.996   -76.009  17.387  1.000 65.979  0 456 PHE CCC CD1 1 ? 11 
ATOM   3557  C CD2 . PHE C  1 127 ? 0.623   -74.890  15.790  1.000 65.802  0 456 PHE CCC CD2 1 ? 11 
ATOM   3558  C CE1 . PHE C  1 127 ? 1.780   -74.988  18.299  1.000 67.131  0 456 PHE CCC CE1 1 ? 11 
ATOM   3559  C CE2 . PHE C  1 127 ? 0.409   -73.865  16.705  1.000 67.820  0 456 PHE CCC CE2 1 ? 11 
ATOM   3560  C CZ  . PHE C  1 127 ? 1.000   -73.910  17.952  1.000 68.059  0 456 PHE CCC CZ  1 ? 11 
ATOM   3561  N N   . ARG C  1 128 ? 3.559   -79.503  13.953  1.000 59.634  0 457 ARG CCC N   1 ? 11 
ATOM   3562  C CA  . ARG C  1 128 ? 3.481   -80.724  13.128  1.000 59.501  0 457 ARG CCC CA  1 ? 11 
ATOM   3563  C C   . ARG C  1 128 ? 3.510   -81.939  14.051  1.000 61.435  0 457 ARG CCC C   1 ? 11 
ATOM   3564  O O   . ARG C  1 128 ? 4.188   -81.855  15.095  1.000 64.825  0 457 ARG CCC O   1 ? 11 
ATOM   3565  C CB  . ARG C  1 128 ? 4.639   -80.734  12.134  1.000 57.692  0 457 ARG CCC CB  1 ? 11 
ATOM   3566  C CG  . ARG C  1 128 ? 4.440   -81.750  11.017  1.000 56.280  0 457 ARG CCC CG  1 ? 11 
ATOM   3567  C CD  . ARG C  1 128 ? 5.484   -81.555  9.948   1.000 55.129  0 457 ARG CCC CD  1 ? 11 
ATOM   3568  N NE  . ARG C  1 128 ? 5.148   -82.269  8.731   1.000 55.395  0 457 ARG CCC NE  1 ? 11 
ATOM   3569  C CZ  . ARG C  1 128 ? 5.485   -83.520  8.479   1.000 55.576  0 457 ARG CCC CZ  1 ? 11 
ATOM   3570  N NH1 . ARG C  1 128 ? 6.184   -84.217  9.352   1.000 57.420  0 457 ARG CCC NH1 1 ? 11 
ATOM   3571  N NH2 . ARG C  1 128 ? 5.145   -84.075  7.335   1.000 56.363  0 457 ARG CCC NH2 1 ? 11 
ATOM   3572  N N   . LYS C  1 129 ? 2.818   -83.018  13.677  1.000 61.512  0 458 LYS CCC N   1 ? 11 
ATOM   3573  C CA  . LYS C  1 129 ? 2.694   -84.251  14.505  1.000 62.112  0 458 LYS CCC CA  1 ? 11 
ATOM   3574  C C   . LYS C  1 129 ? 4.064   -84.921  14.652  1.000 58.326  0 458 LYS CCC C   1 ? 11 
ATOM   3575  O O   . LYS C  1 129 ? 4.291   -85.597  15.660  1.000 57.750  0 458 LYS CCC O   1 ? 11 
ATOM   3576  C CB  . LYS C  1 129 ? 1.705   -85.246  13.902  1.000 64.462  0 458 LYS CCC CB  1 ? 11 
ATOM   3577  C CG  . LYS C  1 129 ? 0.266   -84.747  13.797  1.000 67.982  0 458 LYS CCC CG  1 ? 11 
ATOM   3578  C CD  . LYS C  1 129 ? -0.691  -85.758  13.232  1.000 71.912  0 458 LYS CCC CD  1 ? 11 
ATOM   3579  C CE  . LYS C  1 129 ? -1.710  -85.164  12.269  1.000 73.899  0 458 LYS CCC CE  1 ? 11 
ATOM   3580  N NZ  . LYS C  1 129 ? -2.761  -86.154  11.951  1.000 76.353  0 458 LYS CCC NZ  1 ? 11 
ATOM   3581  N N   . SER C  1 130 ? 4.958   -84.740  13.685  1.000 55.360  0 459 SER CCC N   1 ? 11 
ATOM   3582  C CA  . SER C  1 130 ? 6.281   -85.406  13.676  1.000 55.134  0 459 SER CCC CA  1 ? 11 
ATOM   3583  C C   . SER C  1 130 ? 7.250   -84.623  12.789  1.000 51.967  0 459 SER CCC C   1 ? 11 
ATOM   3584  O O   . SER C  1 130 ? 6.796   -83.790  12.016  1.000 51.292  0 459 SER CCC O   1 ? 11 
ATOM   3585  C CB  . SER C  1 130 ? 6.137   -86.833  13.237  1.000 55.870  0 459 SER CCC CB  1 ? 11 
ATOM   3586  O OG  . SER C  1 130 ? 6.024   -86.905  11.824  1.000 56.146  0 459 SER CCC OG  1 ? 11 
ATOM   3587  N N   . ASN C  1 131 ? 8.544   -84.881  12.934  1.000 52.134  0 460 ASN CCC N   1 ? 11 
ATOM   3588  C CA  . ASN C  1 131 ? 9.621   -84.138  12.238  1.000 49.953  0 460 ASN CCC CA  1 ? 11 
ATOM   3589  C C   . ASN C  1 131 ? 9.629   -84.520  10.760  1.000 49.490  0 460 ASN CCC C   1 ? 11 
ATOM   3590  O O   . ASN C  1 131 ? 9.315   -85.658  10.451  1.000 52.574  0 460 ASN CCC O   1 ? 11 
ATOM   3591  C CB  . ASN C  1 131 ? 10.989  -84.407  12.865  1.000 49.507  0 460 ASN CCC CB  1 ? 11 
ATOM   3592  C CG  . ASN C  1 131 ? 11.120  -83.839  14.255  1.000 50.726  0 460 ASN CCC CG  1 ? 11 
ATOM   3593  O OD1 . ASN C  1 131 ? 10.221  -83.155  14.744  1.000 52.105  0 460 ASN CCC OD1 1 ? 11 
ATOM   3594  N ND2 . ASN C  1 131 ? 12.253  -84.117  14.875  1.000 52.066  0 460 ASN CCC ND2 1 ? 11 
ATOM   3595  N N   . LEU C  1 132 ? 9.981   -83.581  9.899   1.000 47.928  0 461 LEU CCC N   1 ? 11 
ATOM   3596  C CA  . LEU C  1 132 ? 10.244  -83.844  8.466   1.000 49.509  0 461 LEU CCC CA  1 ? 11 
ATOM   3597  C C   . LEU C  1 132 ? 11.407  -84.825  8.346   1.000 51.844  0 461 LEU CCC C   1 ? 11 
ATOM   3598  O O   . LEU C  1 132 ? 12.384  -84.690  9.101   1.000 54.957  0 461 LEU CCC O   1 ? 11 
ATOM   3599  C CB  . LEU C  1 132 ? 10.603  -82.526  7.772   1.000 47.728  0 461 LEU CCC CB  1 ? 11 
ATOM   3600  C CG  . LEU C  1 132 ? 9.467   -81.520  7.612   1.000 48.180  0 461 LEU CCC CG  1 ? 11 
ATOM   3601  C CD1 . LEU C  1 132 ? 9.966   -80.335  6.801   1.000 46.714  0 461 LEU CCC CD1 1 ? 11 
ATOM   3602  C CD2 . LEU C  1 132 ? 8.248   -82.163  6.935   1.000 50.147  0 461 LEU CCC CD2 1 ? 11 
ATOM   3603  N N   . LYS C  1 133 ? 11.318  -85.728  7.384   1.000 54.933  0 462 LYS CCC N   1 ? 11 
ATOM   3604  C CA  . LYS C  1 133 ? 12.485  -86.469  6.828   1.000 56.531  0 462 LYS CCC CA  1 ? 11 
ATOM   3605  C C   . LYS C  1 133 ? 13.349  -85.496  6.026   1.000 51.614  0 462 LYS CCC C   1 ? 11 
ATOM   3606  O O   . LYS C  1 133 ? 12.889  -84.443  5.591   1.000 49.258  0 462 LYS CCC O   1 ? 11 
ATOM   3607  C CB  . LYS C  1 133 ? 12.007  -87.659  5.986   1.000 59.124  0 462 LYS CCC CB  1 ? 11 
ATOM   3608  C CG  . LYS C  1 133 ? 11.489  -88.831  6.811   1.000 62.647  0 462 LYS CCC CG  1 ? 11 
ATOM   3609  C CD  . LYS C  1 133 ? 10.857  -89.943  5.993   1.000 70.434  0 462 LYS CCC CD  1 ? 11 
ATOM   3610  C CE  . LYS C  1 133 ? 10.185  -89.481  4.701   1.000 74.728  0 462 LYS CCC CE  1 ? 11 
ATOM   3611  N NZ  . LYS C  1 133 ? 8.864   -90.133  4.453   1.000 78.011  0 462 LYS CCC NZ  1 ? 11 
ATOM   3612  N N   . PRO C  1 134 ? 14.651  -85.794  5.833   1.000 49.583  0 463 PRO CCC N   1 ? 11 
ATOM   3613  C CA  . PRO C  1 134 ? 15.516  -84.911  5.052   1.000 46.290  0 463 PRO CCC CA  1 ? 11 
ATOM   3614  C C   . PRO C  1 134 ? 14.960  -84.642  3.653   1.000 46.048  0 463 PRO CCC C   1 ? 11 
ATOM   3615  O O   . PRO C  1 134 ? 14.530  -85.561  3.024   1.000 45.592  0 463 PRO CCC O   1 ? 11 
ATOM   3616  C CB  . PRO C  1 134 ? 16.828  -85.697  5.002   1.000 47.254  0 463 PRO CCC CB  1 ? 11 
ATOM   3617  C CG  . PRO C  1 134 ? 16.826  -86.423  6.336   1.000 48.112  0 463 PRO CCC CG  1 ? 11 
ATOM   3618  C CD  . PRO C  1 134 ? 15.396  -86.913  6.442   1.000 48.007  0 463 PRO CCC CD  1 ? 11 
ATOM   3619  N N   . PHE C  1 135 ? 14.910  -83.371  3.266   1.000 45.649  0 464 PHE CCC N   1 ? 11 
ATOM   3620  C CA  . PHE C  1 135 ? 14.409  -82.883  1.966   1.000 45.732  0 464 PHE CCC CA  1 ? 11 
ATOM   3621  C C   . PHE C  1 135 ? 12.912  -83.163  1.788   1.000 45.831  0 464 PHE CCC C   1 ? 11 
ATOM   3622  O O   . PHE C  1 135 ? 12.422  -83.052  0.650   1.000 45.665  0 464 PHE CCC O   1 ? 11 
ATOM   3623  C CB  . PHE C  1 135 ? 15.229  -83.481  0.825   1.000 47.545  0 464 PHE CCC CB  1 ? 11 
ATOM   3624  C CG  . PHE C  1 135 ? 16.658  -83.009  0.789   1.000 47.179  0 464 PHE CCC CG  1 ? 11 
ATOM   3625  C CD1 . PHE C  1 135 ? 16.993  -81.655  0.848   1.000 46.777  0 464 PHE CCC CD1 1 ? 11 
ATOM   3626  C CD2 . PHE C  1 135 ? 17.667  -83.930  0.648   1.000 47.008  0 464 PHE CCC CD2 1 ? 11 
ATOM   3627  C CE1 . PHE C  1 135 ? 18.322  -81.260  0.830   1.000 47.477  0 464 PHE CCC CE1 1 ? 11 
ATOM   3628  C CE2 . PHE C  1 135 ? 18.994  -83.508  0.561   1.000 47.261  0 464 PHE CCC CE2 1 ? 11 
ATOM   3629  C CZ  . PHE C  1 135 ? 19.325  -82.164  0.628   1.000 47.144  0 464 PHE CCC CZ  1 ? 11 
ATOM   3630  N N   . GLU C  1 136 ? 12.190  -83.445  2.868   1.000 47.605  0 465 GLU CCC N   1 ? 11 
ATOM   3631  C CA  . GLU C  1 136 ? 10.707  -83.553  2.820   1.000 48.489  0 465 GLU CCC CA  1 ? 11 
ATOM   3632  C C   . GLU C  1 136 ? 10.132  -82.127  2.766   1.000 48.685  0 465 GLU CCC C   1 ? 11 
ATOM   3633  O O   . GLU C  1 136 ? 10.760  -81.184  3.289   1.000 44.371  0 465 GLU CCC O   1 ? 11 
ATOM   3634  C CB  . GLU C  1 136 ? 10.154  -84.350  4.003   1.000 50.328  0 465 GLU CCC CB  1 ? 11 
ATOM   3635  C CG  . GLU C  1 136 ? 8.712   -84.820  3.806   1.000 52.413  0 465 GLU CCC CG  1 ? 11 
ATOM   3636  C CD  . GLU C  1 136 ? 8.138   -85.644  4.966   1.000 56.633  0 465 GLU CCC CD  1 ? 11 
ATOM   3637  O OE1 . GLU C  1 136 ? 8.896   -85.962  5.930   1.000 56.013  0 465 GLU CCC OE1 1 ? 11 
ATOM   3638  O OE2 . GLU C  1 136 ? 6.931   -85.965  4.926   1.000 57.998  0 465 GLU CCC OE2 1 ? 11 
ATOM   3639  N N   . ARG C  1 137 ? 8.975   -81.990  2.127   1.000 48.925  0 466 ARG CCC N   1 ? 11 
ATOM   3640  C CA  . ARG C  1 137 ? 8.263   -80.716  1.951   1.000 48.892  0 466 ARG CCC CA  1 ? 11 
ATOM   3641  C C   . ARG C  1 137 ? 6.803   -80.944  2.314   1.000 47.635  0 466 ARG CCC C   1 ? 11 
ATOM   3642  O O   . ARG C  1 137 ? 6.226   -81.863  1.776   1.000 45.614  0 466 ARG CCC O   1 ? 11 
ATOM   3643  C CB  . ARG C  1 137 ? 8.403   -80.282  0.497   1.000 50.219  0 466 ARG CCC CB  1 ? 11 
ATOM   3644  C CG  . ARG C  1 137 ? 7.890   -78.883  0.191   1.000 53.989  0 466 ARG CCC CG  1 ? 11 
ATOM   3645  C CD  . ARG C  1 137 ? 8.384   -78.619  -1.202  1.000 58.942  0 466 ARG CCC CD  1 ? 11 
ATOM   3646  N NE  . ARG C  1 137 ? 8.070   -77.308  -1.695  1.000 63.565  0 466 ARG CCC NE  1 ? 11 
ATOM   3647  C CZ  . ARG C  1 137 ? 6.959   -76.976  -2.350  1.000 70.266  0 466 ARG CCC CZ  1 ? 11 
ATOM   3648  N NH1 . ARG C  1 137 ? 5.999   -77.858  -2.568  1.000 73.136  0 466 ARG CCC NH1 1 ? 11 
ATOM   3649  N NH2 . ARG C  1 137 ? 6.811   -75.727  -2.775  1.000 71.641  0 466 ARG CCC NH2 1 ? 11 
ATOM   3650  N N   . ASP C  1 138 ? 6.252   -80.143  3.214   1.000 47.722  0 467 ASP CCC N   1 ? 11 
ATOM   3651  C CA  . ASP C  1 138 ? 4.853   -80.275  3.688   1.000 47.817  0 467 ASP CCC CA  1 ? 11 
ATOM   3652  C C   . ASP C  1 138 ? 4.197   -78.917  3.458   1.000 48.197  0 467 ASP CCC C   1 ? 11 
ATOM   3653  O O   . ASP C  1 138 ? 4.627   -77.936  4.095   1.000 47.007  0 467 ASP CCC O   1 ? 11 
ATOM   3654  C CB  . ASP C  1 138 ? 4.819   -80.725  5.146   1.000 48.738  0 467 ASP CCC CB  1 ? 11 
ATOM   3655  C CG  . ASP C  1 138 ? 3.429   -80.947  5.709   1.000 49.678  0 467 ASP CCC CG  1 ? 11 
ATOM   3656  O OD1 . ASP C  1 138 ? 2.446   -80.575  5.028   1.000 50.064  0 467 ASP CCC OD1 1 ? 11 
ATOM   3657  O OD2 . ASP C  1 138 ? 3.345   -81.482  6.834   1.000 49.950  0 467 ASP CCC OD2 1 ? 11 
ATOM   3658  N N   . ILE C  1 139 ? 3.214   -78.863  2.559   1.000 51.392  0 468 ILE CCC N   1 ? 11 
ATOM   3659  C CA  . ILE C  1 139 ? 2.457   -77.619  2.253   1.000 51.061  0 468 ILE CCC CA  1 ? 11 
ATOM   3660  C C   . ILE C  1 139 ? 1.004   -77.766  2.713   1.000 50.245  0 468 ILE CCC C   1 ? 11 
ATOM   3661  O O   . ILE C  1 139 ? 0.233   -76.863  2.415   1.000 50.268  0 468 ILE CCC O   1 ? 11 
ATOM   3662  C CB  . ILE C  1 139 ? 2.600   -77.244  0.770   1.000 51.623  0 468 ILE CCC CB  1 ? 11 
ATOM   3663  C CG1 . ILE C  1 139 ? 1.987   -78.277  -0.166  1.000 55.006  0 468 ILE CCC CG1 1 ? 11 
ATOM   3664  C CG2 . ILE C  1 139 ? 4.052   -76.979  0.425   1.000 51.072  0 468 ILE CCC CG2 1 ? 11 
ATOM   3665  C CD1 . ILE C  1 139 ? 1.681   -77.680  -1.545  1.000 57.364  0 468 ILE CCC CD1 1 ? 11 
ATOM   3666  N N   . SER C  1 140 ? 0.689   -78.814  3.483   1.000 49.526  0 469 SER CCC N   1 ? 11 
ATOM   3667  C CA  . SER C  1 140 ? -0.670  -79.059  4.020   1.000 51.377  0 469 SER CCC CA  1 ? 11 
ATOM   3668  C C   . SER C  1 140 ? -1.013  -77.968  5.033   1.000 52.884  0 469 SER CCC C   1 ? 11 
ATOM   3669  O O   . SER C  1 140 ? -0.092  -77.405  5.665   1.000 50.671  0 469 SER CCC O   1 ? 11 
ATOM   3670  C CB  . SER C  1 140 ? -0.806  -80.433  4.640   1.000 51.892  0 469 SER CCC CB  1 ? 11 
ATOM   3671  O OG  . SER C  1 140 ? -0.021  -80.525  5.808   1.000 52.428  0 469 SER CCC OG  1 ? 11 
ATOM   3672  N N   . THR C  1 141 ? -2.306  -77.690  5.189   1.000 55.600  0 470 THR CCC N   1 ? 11 
ATOM   3673  C CA  . THR C  1 141 ? -2.822  -76.656  6.120   1.000 56.496  0 470 THR CCC CA  1 ? 11 
ATOM   3674  C C   . THR C  1 141 ? -3.946  -77.279  6.941   1.000 58.061  0 470 THR CCC C   1 ? 11 
ATOM   3675  O O   . THR C  1 141 ? -4.954  -76.613  7.134   1.000 60.350  0 470 THR CCC O   1 ? 11 
ATOM   3676  C CB  . THR C  1 141 ? -3.208  -75.383  5.364   1.000 56.028  0 470 THR CCC CB  1 ? 11 
ATOM   3677  O OG1 . THR C  1 141 ? -4.103  -75.744  4.326   1.000 56.806  0 470 THR CCC OG1 1 ? 11 
ATOM   3678  C CG2 . THR C  1 141 ? -2.031  -74.672  4.741   1.000 53.545  0 470 THR CCC CG2 1 ? 11 
ATOM   3679  N N   . GLU C  1 142 ? -3.728  -78.500  7.410   1.000 59.322  0 471 GLU CCC N   1 ? 11 
ATOM   3680  C CA  . GLU C  1 142 ? -4.707  -79.249  8.246   1.000 61.022  0 471 GLU CCC CA  1 ? 11 
ATOM   3681  C C   . GLU C  1 142 ? -4.653  -78.652  9.651   1.000 60.062  0 471 GLU CCC C   1 ? 11 
ATOM   3682  O O   . GLU C  1 142 ? -3.527  -78.326  10.118  1.000 57.262  0 471 GLU CCC O   1 ? 11 
ATOM   3683  C CB  . GLU C  1 142 ? -4.416  -80.752  8.303   1.000 62.822  0 471 GLU CCC CB  1 ? 11 
ATOM   3684  C CG  . GLU C  1 142 ? -4.268  -81.408  6.950   1.000 65.276  0 471 GLU CCC CG  1 ? 11 
ATOM   3685  C CD  . GLU C  1 142 ? -5.537  -81.508  6.133   1.000 69.021  0 471 GLU CCC CD  1 ? 11 
ATOM   3686  O OE1 . GLU C  1 142 ? -5.443  -82.076  5.044   1.000 74.117  0 471 GLU CCC OE1 1 ? 11 
ATOM   3687  O OE2 . GLU C  1 142 ? -6.617  -81.098  6.605   1.000 72.781  0 471 GLU CCC OE2 1 ? 11 
ATOM   3688  N N   . ILE C  1 143 ? -5.825  -78.495  10.274  1.000 62.088  0 472 ILE CCC N   1 ? 11 
ATOM   3689  C CA  . ILE C  1 143 ? -5.958  -77.976  11.657  1.000 64.094  0 472 ILE CCC CA  1 ? 11 
ATOM   3690  C C   . ILE C  1 143 ? -5.184  -78.931  12.559  1.000 64.030  0 472 ILE CCC C   1 ? 11 
ATOM   3691  O O   . ILE C  1 143 ? -5.425  -80.141  12.476  1.000 66.882  0 472 ILE CCC O   1 ? 11 
ATOM   3692  C CB  . ILE C  1 143 ? -7.433  -77.865  12.075  1.000 67.275  0 472 ILE CCC CB  1 ? 11 
ATOM   3693  C CG1 . ILE C  1 143 ? -8.202  -76.931  11.135  1.000 67.923  0 472 ILE CCC CG1 1 ? 11 
ATOM   3694  C CG2 . ILE C  1 143 ? -7.558  -77.444  13.543  1.000 68.660  0 472 ILE CCC CG2 1 ? 11 
ATOM   3695  C CD1 . ILE C  1 143 ? -9.669  -77.201  11.117  1.000 70.659  0 472 ILE CCC CD1 1 ? 11 
ATOM   3696  N N   . TYR C  1 144 ? -4.261  -78.398  13.352  1.000 63.088  0 473 TYR CCC N   1 ? 11 
ATOM   3697  C CA  . TYR C  1 144 ? -3.390  -79.182  14.250  1.000 63.690  0 473 TYR CCC CA  1 ? 11 
ATOM   3698  C C   . TYR C  1 144 ? -4.135  -79.362  15.565  1.000 68.049  0 473 TYR CCC C   1 ? 11 
ATOM   3699  O O   . TYR C  1 144 ? -4.592  -78.365  16.142  1.000 69.428  0 473 TYR CCC O   1 ? 11 
ATOM   3700  C CB  . TYR C  1 144 ? -2.034  -78.505  14.410  1.000 61.187  0 473 TYR CCC CB  1 ? 11 
ATOM   3701  C CG  . TYR C  1 144 ? -1.110  -79.169  15.391  1.000 61.630  0 473 TYR CCC CG  1 ? 11 
ATOM   3702  C CD1 . TYR C  1 144 ? -0.283  -80.224  15.009  1.000 60.029  0 473 TYR CCC CD1 1 ? 11 
ATOM   3703  C CD2 . TYR C  1 144 ? -1.024  -78.704  16.695  1.000 62.313  0 473 TYR CCC CD2 1 ? 11 
ATOM   3704  C CE1 . TYR C  1 144 ? 0.593   -80.816  15.909  1.000 59.345  0 473 TYR CCC CE1 1 ? 11 
ATOM   3705  C CE2 . TYR C  1 144 ? -0.158  -79.283  17.606  1.000 62.478  0 473 TYR CCC CE2 1 ? 11 
ATOM   3706  C CZ  . TYR C  1 144 ? 0.647   -80.340  17.208  1.000 60.786  0 473 TYR CCC CZ  1 ? 11 
ATOM   3707  O OH  . TYR C  1 144 ? 1.518   -80.899  18.089  1.000 62.535  0 473 TYR CCC OH  1 ? 11 
ATOM   3708  N N   . GLN C  1 145 ? -4.310  -80.618  15.985  1.000 70.922  0 474 GLN CCC N   1 ? 11 
ATOM   3709  C CA  . GLN C  1 145 ? -4.914  -80.966  17.299  1.000 73.158  0 474 GLN CCC CA  1 ? 11 
ATOM   3710  C C   . GLN C  1 145 ? -3.805  -80.919  18.356  1.000 74.550  0 474 GLN CCC C   1 ? 11 
ATOM   3711  O O   . GLN C  1 145 ? -2.993  -81.851  18.409  1.000 75.756  0 474 GLN CCC O   1 ? 11 
ATOM   3712  C CB  . GLN C  1 145 ? -5.577  -82.328  17.254  1.000 74.371  0 474 GLN CCC CB  1 ? 11 
ATOM   3713  C CG  . GLN C  1 145 ? -6.062  -82.754  18.615  1.000 77.077  0 474 GLN CCC CG  1 ? 11 
ATOM   3714  C CD  . GLN C  1 145 ? -6.979  -83.939  18.513  1.000 78.497  0 474 GLN CCC CD  1 ? 11 
ATOM   3715  O OE1 . GLN C  1 145 ? -7.541  -84.245  17.461  1.000 78.855  0 474 GLN CCC OE1 1 ? 11 
ATOM   3716  N NE2 . GLN C  1 145 ? -7.130  -84.612  19.629  1.000 81.577  0 474 GLN CCC NE2 1 ? 11 
ATOM   3717  N N   . ALA C  1 146 ? -3.763  -79.834  19.121  1.000 76.851  0 475 ALA CCC N   1 ? 11 
ATOM   3718  C CA  . ALA C  1 146 ? -2.748  -79.542  20.159  1.000 78.399  0 475 ALA CCC CA  1 ? 11 
ATOM   3719  C C   . ALA C  1 146 ? -3.232  -80.080  21.512  1.000 82.582  0 475 ALA CCC C   1 ? 11 
ATOM   3720  O O   . ALA C  1 146 ? -2.424  -80.112  22.452  1.000 86.349  0 475 ALA CCC O   1 ? 11 
ATOM   3721  C CB  . ALA C  1 146 ? -2.487  -78.051  20.216  1.000 77.115  0 475 ALA CCC CB  1 ? 11 
ATOM   3722  N N   . GLY C  1 147 ? -4.504  -80.480  21.621  1.000 83.779  0 476 GLY CCC N   1 ? 11 
ATOM   3723  C CA  . GLY C  1 147 ? -5.112  -80.899  22.893  1.000 87.035  0 476 GLY CCC CA  1 ? 11 
ATOM   3724  C C   . GLY C  1 147 ? -5.788  -82.260  22.795  1.000 87.913  0 476 GLY CCC C   1 ? 11 
ATOM   3725  O O   . GLY C  1 147 ? -5.788  -82.856  21.702  1.000 88.675  0 476 GLY CCC O   1 ? 11 
ATOM   3726  N N   . SER C  1 148 ? -6.365  -82.703  23.906  1.000 89.170  0 477 SER CCC N   1 ? 11 
ATOM   3727  C CA  . SER C  1 148 ? -7.194  -83.927  24.022  1.000 91.458  0 477 SER CCC CA  1 ? 11 
ATOM   3728  C C   . SER C  1 148 ? -8.363  -83.892  23.025  1.000 91.045  0 477 SER CCC C   1 ? 11 
ATOM   3729  O O   . SER C  1 148 ? -8.579  -84.931  22.370  1.000 90.257  0 477 SER CCC O   1 ? 11 
ATOM   3730  C CB  . SER C  1 148 ? -7.693  -84.088  25.434  1.000 95.027  0 477 SER CCC CB  1 ? 11 
ATOM   3731  O OG  . SER C  1 148 ? -6.671  -83.764  26.358  1.000 96.296  0 477 SER CCC OG  1 ? 11 
ATOM   3732  N N   . THR C  1 149 ? -9.088  -82.767  22.916  1.000 90.471  0 478 THR CCC N   1 ? 11 
ATOM   3733  C CA  . THR C  1 149 ? -10.361 -82.668  22.152  1.000 91.535  0 478 THR CCC CA  1 ? 11 
ATOM   3734  C C   . THR C  1 149 ? -10.091 -82.790  20.657  1.000 87.879  0 478 THR CCC C   1 ? 11 
ATOM   3735  O O   . THR C  1 149 ? -9.135  -82.210  20.160  1.000 83.323  0 478 THR CCC O   1 ? 11 
ATOM   3736  C CB  . THR C  1 149 ? -11.128 -81.370  22.445  1.000 94.178  0 478 THR CCC CB  1 ? 11 
ATOM   3737  O OG1 . THR C  1 149 ? -11.114 -81.095  23.843  1.000 97.371  0 478 THR CCC OG1 1 ? 11 
ATOM   3738  C CG2 . THR C  1 149 ? -12.575 -81.446  21.996  1.000 96.567  0 478 THR CCC CG2 1 ? 11 
ATOM   3739  N N   . PRO C  1 150 ? -10.916 -83.548  19.887  1.000 88.855  0 479 PRO CCC N   1 ? 11 
ATOM   3740  C CA  . PRO C  1 150 ? -10.813 -83.535  18.427  1.000 86.567  0 479 PRO CCC CA  1 ? 11 
ATOM   3741  C C   . PRO C  1 150 ? -11.276 -82.162  17.895  1.000 85.472  0 479 PRO CCC C   1 ? 11 
ATOM   3742  O O   . PRO C  1 150 ? -12.044 -81.495  18.545  1.000 86.199  0 479 PRO CCC O   1 ? 11 
ATOM   3743  C CB  . PRO C  1 150 ? -11.716 -84.708  17.998  1.000 86.588  0 479 PRO CCC CB  1 ? 11 
ATOM   3744  C CG  . PRO C  1 150 ? -12.729 -84.821  19.097  1.000 89.975  0 479 PRO CCC CG  1 ? 11 
ATOM   3745  C CD  . PRO C  1 150 ? -12.000 -84.425  20.365  1.000 90.384  0 479 PRO CCC CD  1 ? 11 
ATOM   3746  N N   . CYS C  1 151 ? -10.798 -81.774  16.720  1.000 83.794  0 480 CYS CCC N   1 ? 11 
ATOM   3747  C CA  . CYS C  1 151 ? -10.978 -80.414  16.153  1.000 85.096  0 480 CYS CCC CA  1 ? 11 
ATOM   3748  C C   . CYS C  1 151 ? -12.165 -80.344  15.191  1.000 84.965  0 480 CYS CCC C   1 ? 11 
ATOM   3749  O O   . CYS C  1 151 ? -12.640 -79.223  14.970  1.000 83.665  0 480 CYS CCC O   1 ? 11 
ATOM   3750  C CB  . CYS C  1 151 ? -9.695  -79.962  15.472  1.000 86.166  0 480 CYS CCC CB  1 ? 11 
ATOM   3751  S SG  . CYS C  1 151 ? -8.373  -79.616  16.680  1.000 93.383  0 480 CYS CCC SG  1 ? 11 
ATOM   3752  N N   . ASN C  1 152 ? -12.636 -81.478  14.670  1.000 85.806  0 481 ASN CCC N   1 ? 11 
ATOM   3753  C CA  . ASN C  1 152 ? -13.816 -81.571  13.767  1.000 87.907  0 481 ASN CCC CA  1 ? 11 
ATOM   3754  C C   . ASN C  1 152 ? -13.722 -80.536  12.627  1.000 88.268  0 481 ASN CCC C   1 ? 11 
ATOM   3755  O O   . ASN C  1 152 ? -14.771 -79.950  12.257  1.000 89.345  0 481 ASN CCC O   1 ? 11 
ATOM   3756  C CB  . ASN C  1 152 ? -15.141 -81.383  14.515  1.000 89.808  0 481 ASN CCC CB  1 ? 11 
ATOM   3757  C CG  . ASN C  1 152 ? -16.325 -81.771  13.649  1.000 91.460  0 481 ASN CCC CG  1 ? 11 
ATOM   3758  O OD1 . ASN C  1 152 ? -16.227 -82.758  12.930  1.000 89.940  0 481 ASN CCC OD1 1 ? 11 
ATOM   3759  N ND2 . ASN C  1 152 ? -17.427 -81.021  13.678  1.000 93.705  0 481 ASN CCC ND2 1 ? 11 
ATOM   3760  N N   . GLY C  1 153 ? -12.512 -80.301  12.105  1.000 87.992  0 482 GLY CCC N   1 ? 11 
ATOM   3761  C CA  . GLY C  1 153 ? -12.242 -79.394  10.971  1.000 87.715  0 482 GLY CCC CA  1 ? 11 
ATOM   3762  C C   . GLY C  1 153 ? -12.661 -77.952  11.236  1.000 89.536  0 482 GLY CCC C   1 ? 11 
ATOM   3763  O O   . GLY C  1 153 ? -12.978 -77.249  10.258  1.000 93.713  0 482 GLY CCC O   1 ? 11 
ATOM   3764  N N   . VAL C  1 154 ? -12.662 -77.521  12.503  1.000 87.707  0 483 VAL CCC N   1 ? 11 
ATOM   3765  C CA  . VAL C  1 154 ? -12.959 -76.123  12.926  1.000 85.423  0 483 VAL CCC CA  1 ? 11 
ATOM   3766  C C   . VAL C  1 154 ? -11.772 -75.623  13.750  1.000 82.287  0 483 VAL CCC C   1 ? 11 
ATOM   3767  O O   . VAL C  1 154 ? -11.218 -76.401  14.554  1.000 80.382  0 483 VAL CCC O   1 ? 11 
ATOM   3768  C CB  . VAL C  1 154 ? -14.271 -76.049  13.721  1.000 90.210  0 483 VAL CCC CB  1 ? 11 
ATOM   3769  C CG1 . VAL C  1 154 ? -14.408 -74.719  14.466  1.000 91.666  0 483 VAL CCC CG1 1 ? 11 
ATOM   3770  C CG2 . VAL C  1 154 ? -15.486 -76.326  12.838  1.000 91.514  0 483 VAL CCC CG2 1 ? 11 
ATOM   3771  N N   . GLU C  1 155 ? -11.359 -74.380  13.511  1.000 80.716  0 484 GLU CCC N   1 ? 11 
ATOM   3772  C CA  . GLU C  1 155 ? -10.236 -73.728  14.247  1.000 79.408  0 484 GLU CCC CA  1 ? 11 
ATOM   3773  C C   . GLU C  1 155 ? -10.767 -73.230  15.596  1.000 81.401  0 484 GLU CCC C   1 ? 11 
ATOM   3774  O O   . GLU C  1 155 ? -11.972 -72.897  15.647  1.000 84.768  0 484 GLU CCC O   1 ? 11 
ATOM   3775  C CB  . GLU C  1 155 ? -9.669  -72.600  13.395  1.000 77.823  0 484 GLU CCC CB  1 ? 11 
ATOM   3776  C CG  . GLU C  1 155 ? -8.282  -72.231  13.838  1.000 76.550  0 484 GLU CCC CG  1 ? 11 
ATOM   3777  C CD  . GLU C  1 155 ? -7.548  -71.273  12.942  1.000 74.954  0 484 GLU CCC CD  1 ? 11 
ATOM   3778  O OE1 . GLU C  1 155 ? -7.995  -71.072  11.791  1.000 73.704  0 484 GLU CCC OE1 1 ? 11 
ATOM   3779  O OE2 . GLU C  1 155 ? -6.470  -70.826  13.380  1.000 73.263  0 484 GLU CCC OE2 1 ? 11 
ATOM   3780  N N   . GLY C  1 156 ? -9.919  -73.159  16.624  1.000 79.946  0 485 GLY CCC N   1 ? 11 
ATOM   3781  C CA  . GLY C  1 156 ? -10.297 -72.666  17.963  1.000 82.611  0 485 GLY CCC CA  1 ? 11 
ATOM   3782  C C   . GLY C  1 156 ? -9.293  -73.070  19.027  1.000 84.297  0 485 GLY CCC C   1 ? 11 
ATOM   3783  O O   . GLY C  1 156 ? -8.138  -73.321  18.663  1.000 82.653  0 485 GLY CCC O   1 ? 11 
ATOM   3784  N N   . PHE C  1 157 ? -9.712  -73.116  20.294  1.000 91.025  0 486 PHE CCC N   1 ? 11 
ATOM   3785  C CA  . PHE C  1 157 ? -8.860  -73.484  21.456  1.000 94.161  0 486 PHE CCC CA  1 ? 11 
ATOM   3786  C C   . PHE C  1 157 ? -8.207  -74.843  21.175  1.000 90.995  0 486 PHE CCC C   1 ? 11 
ATOM   3787  O O   . PHE C  1 157 ? -8.942  -75.801  20.855  1.000 87.566  0 486 PHE CCC O   1 ? 11 
ATOM   3788  C CB  . PHE C  1 157 ? -9.681  -73.461  22.750  1.000 101.484 0 486 PHE CCC CB  1 ? 11 
ATOM   3789  C CG  . PHE C  1 157 ? -8.951  -73.857  24.016  1.000 106.493 0 486 PHE CCC CG  1 ? 11 
ATOM   3790  C CD1 . PHE C  1 157 ? -7.599  -73.571  24.225  1.000 106.576 0 486 PHE CCC CD1 1 ? 11 
ATOM   3791  C CD2 . PHE C  1 157 ? -9.649  -74.483  25.038  1.000 113.286 0 486 PHE CCC CD2 1 ? 11 
ATOM   3792  C CE1 . PHE C  1 157 ? -6.966  -73.947  25.398  1.000 109.362 0 486 PHE CCC CE1 1 ? 11 
ATOM   3793  C CE2 . PHE C  1 157 ? -9.022  -74.839  26.228  1.000 116.183 0 486 PHE CCC CE2 1 ? 11 
ATOM   3794  C CZ  . PHE C  1 157 ? -7.682  -74.563  26.407  1.000 114.580 0 486 PHE CCC CZ  1 ? 11 
ATOM   3795  N N   . ASN C  1 158 ? -6.866  -74.901  21.229  1.000 88.651  0 487 ASN CCC N   1 ? 11 
ATOM   3796  C CA  . ASN C  1 158 ? -6.044  -76.136  21.051  1.000 87.741  0 487 ASN CCC CA  1 ? 11 
ATOM   3797  C C   . ASN C  1 158 ? -6.268  -76.739  19.658  1.000 84.364  0 487 ASN CCC C   1 ? 11 
ATOM   3798  O O   . ASN C  1 158 ? -5.914  -77.906  19.463  1.000 81.760  0 487 ASN CCC O   1 ? 11 
ATOM   3799  C CB  . ASN C  1 158 ? -6.334  -77.181  22.133  1.000 89.821  0 487 ASN CCC CB  1 ? 11 
ATOM   3800  C CG  . ASN C  1 158 ? -5.853  -76.750  23.494  1.000 91.188  0 487 ASN CCC CG  1 ? 11 
ATOM   3801  O OD1 . ASN C  1 158 ? -4.783  -76.172  23.626  1.000 89.570  0 487 ASN CCC OD1 1 ? 11 
ATOM   3802  N ND2 . ASN C  1 158 ? -6.642  -77.040  24.509  1.000 95.366  0 487 ASN CCC ND2 1 ? 11 
ATOM   3803  N N   . CYS C  1 159 ? -6.789  -75.949  18.720  1.000 83.317  0 488 CYS CCC N   1 ? 11 
ATOM   3804  C CA  . CYS C  1 159 ? -7.117  -76.377  17.336  1.000 81.163  0 488 CYS CCC CA  1 ? 11 
ATOM   3805  C C   . CYS C  1 159 ? -6.579  -75.320  16.365  1.000 78.855  0 488 CYS CCC C   1 ? 11 
ATOM   3806  O O   . CYS C  1 159 ? -7.354  -74.450  15.946  1.000 79.276  0 488 CYS CCC O   1 ? 11 
ATOM   3807  C CB  . CYS C  1 159 ? -8.615  -76.594  17.172  1.000 83.579  0 488 CYS CCC CB  1 ? 11 
ATOM   3808  S SG  . CYS C  1 159 ? -9.182  -78.145  17.927  1.000 84.486  0 488 CYS CCC SG  1 ? 11 
ATOM   3809  N N   . TYR C  1 160 ? -5.286  -75.395  16.061  1.000 76.440  0 489 TYR CCC N   1 ? 11 
ATOM   3810  C CA  . TYR C  1 160 ? -4.499  -74.301  15.455  1.000 74.079  0 489 TYR CCC CA  1 ? 11 
ATOM   3811  C C   . TYR C  1 160 ? -4.326  -74.580  13.969  1.000 71.773  0 489 TYR CCC C   1 ? 11 
ATOM   3812  O O   . TYR C  1 160 ? -4.090  -75.736  13.563  1.000 71.848  0 489 TYR CCC O   1 ? 11 
ATOM   3813  C CB  . TYR C  1 160 ? -3.153  -74.147  16.168  1.000 72.461  0 489 TYR CCC CB  1 ? 11 
ATOM   3814  C CG  . TYR C  1 160 ? -3.308  -73.902  17.642  1.000 77.335  0 489 TYR CCC CG  1 ? 11 
ATOM   3815  C CD1 . TYR C  1 160 ? -4.235  -72.987  18.128  1.000 80.172  0 489 TYR CCC CD1 1 ? 11 
ATOM   3816  C CD2 . TYR C  1 160 ? -2.595  -74.648  18.553  1.000 79.546  0 489 TYR CCC CD2 1 ? 11 
ATOM   3817  C CE1 . TYR C  1 160 ? -4.394  -72.777  19.485  1.000 82.203  0 489 TYR CCC CE1 1 ? 11 
ATOM   3818  C CE2 . TYR C  1 160 ? -2.735  -74.450  19.919  1.000 82.259  0 489 TYR CCC CE2 1 ? 11 
ATOM   3819  C CZ  . TYR C  1 160 ? -3.637  -73.511  20.383  1.000 83.283  0 489 TYR CCC CZ  1 ? 11 
ATOM   3820  O OH  . TYR C  1 160 ? -3.784  -73.352  21.726  1.000 88.009  0 489 TYR CCC OH  1 ? 11 
ATOM   3821  N N   . PHE C  1 161 ? -4.482  -73.530  13.176  1.000 69.655  0 490 PHE CCC N   1 ? 11 
ATOM   3822  C CA  . PHE C  1 161 ? -3.972  -73.473  11.791  1.000 66.442  0 490 PHE CCC CA  1 ? 11 
ATOM   3823  C C   . PHE C  1 161 ? -2.457  -73.585  11.910  1.000 63.494  0 490 PHE CCC C   1 ? 11 
ATOM   3824  O O   . PHE C  1 161 ? -1.860  -72.896  12.719  1.000 61.327  0 490 PHE CCC O   1 ? 11 
ATOM   3825  C CB  . PHE C  1 161 ? -4.460  -72.192  11.129  1.000 66.925  0 490 PHE CCC CB  1 ? 11 
ATOM   3826  C CG  . PHE C  1 161 ? -4.109  -72.080  9.676   1.000 67.502  0 490 PHE CCC CG  1 ? 11 
ATOM   3827  C CD1 . PHE C  1 161 ? -4.835  -72.785  8.729   1.000 67.712  0 490 PHE CCC CD1 1 ? 11 
ATOM   3828  C CD2 . PHE C  1 161 ? -3.053  -71.282  9.260   1.000 65.615  0 490 PHE CCC CD2 1 ? 11 
ATOM   3829  C CE1 . PHE C  1 161 ? -4.547  -72.646  7.382   1.000 65.267  0 490 PHE CCC CE1 1 ? 11 
ATOM   3830  C CE2 . PHE C  1 161 ? -2.751  -71.166  7.913   1.000 65.278  0 490 PHE CCC CE2 1 ? 11 
ATOM   3831  C CZ  . PHE C  1 161 ? -3.506  -71.843  6.980   1.000 65.437  0 490 PHE CCC CZ  1 ? 11 
ATOM   3832  N N   . PRO C  1 162 ? -1.801  -74.512  11.189  1.000 63.342  0 491 PRO CCC N   1 ? 11 
ATOM   3833  C CA  . PRO C  1 162 ? -0.420  -74.888  11.504  1.000 61.327  0 491 PRO CCC CA  1 ? 11 
ATOM   3834  C C   . PRO C  1 162 ? 0.664   -73.928  10.981  1.000 57.625  0 491 PRO CCC C   1 ? 11 
ATOM   3835  O O   . PRO C  1 162 ? 1.828   -74.088  11.370  1.000 53.126  0 491 PRO CCC O   1 ? 11 
ATOM   3836  C CB  . PRO C  1 162 ? -0.286  -76.261  10.824  1.000 61.616  0 491 PRO CCC CB  1 ? 11 
ATOM   3837  C CG  . PRO C  1 162 ? -1.193  -76.170  9.641   1.000 62.015  0 491 PRO CCC CG  1 ? 11 
ATOM   3838  C CD  . PRO C  1 162 ? -2.363  -75.286  10.061  1.000 64.436  0 491 PRO CCC CD  1 ? 11 
ATOM   3839  N N   . LEU C  1 163 ? 0.291   -72.986  10.103  1.000 58.249  0 492 LEU CCC N   1 ? 11 
ATOM   3840  C CA  . LEU C  1 163 ? 1.259   -72.002  9.542   1.000 56.970  0 492 LEU CCC CA  1 ? 11 
ATOM   3841  C C   . LEU C  1 163 ? 1.144   -70.690  10.316  1.000 57.504  0 492 LEU CCC C   1 ? 11 
ATOM   3842  O O   . LEU C  1 163 ? 0.040   -70.302  10.669  1.000 58.358  0 492 LEU CCC O   1 ? 11 
ATOM   3843  C CB  . LEU C  1 163 ? 0.975   -71.774  8.055   1.000 55.820  0 492 LEU CCC CB  1 ? 11 
ATOM   3844  C CG  . LEU C  1 163 ? 1.089   -73.003  7.152   1.000 53.654  0 492 LEU CCC CG  1 ? 11 
ATOM   3845  C CD1 . LEU C  1 163 ? 1.052   -72.567  5.705   1.000 52.010  0 492 LEU CCC CD1 1 ? 11 
ATOM   3846  C CD2 . LEU C  1 163 ? 2.350   -73.817  7.411   1.000 51.839  0 492 LEU CCC CD2 1 ? 11 
ATOM   3847  N N   . GLN C  1 164 ? 2.273   -70.050  10.563  1.000 57.236  0 493 GLN CCC N   1 ? 11 
ATOM   3848  C CA  . GLN C  1 164 ? 2.359   -68.743  11.252  1.000 60.448  0 493 GLN CCC CA  1 ? 11 
ATOM   3849  C C   . GLN C  1 164 ? 3.165   -67.803  10.343  1.000 57.180  0 493 GLN CCC C   1 ? 11 
ATOM   3850  O O   . GLN C  1 164 ? 4.051   -68.254  9.574   1.000 53.750  0 493 GLN CCC O   1 ? 11 
ATOM   3851  C CB  . GLN C  1 164 ? 2.960   -68.952  12.638  1.000 65.799  0 493 GLN CCC CB  1 ? 11 
ATOM   3852  C CG  . GLN C  1 164 ? 3.117   -67.673  13.451  1.000 70.965  0 493 GLN CCC CG  1 ? 11 
ATOM   3853  C CD  . GLN C  1 164 ? 1.790   -67.079  13.827  1.000 75.032  0 493 GLN CCC CD  1 ? 11 
ATOM   3854  O OE1 . GLN C  1 164 ? 1.377   -66.063  13.273  1.000 75.235  0 493 GLN CCC OE1 1 ? 11 
ATOM   3855  N NE2 . GLN C  1 164 ? 1.110   -67.741  14.749  1.000 77.212  0 493 GLN CCC NE2 1 ? 11 
ATOM   3856  N N   . SER C  1 165 ? 2.795   -66.537  10.391  1.000 56.440  0 494 SER CCC N   1 ? 11 
ATOM   3857  C CA  . SER C  1 165 ? 3.399   -65.470  9.569   1.000 54.414  0 494 SER CCC CA  1 ? 11 
ATOM   3858  C C   . SER C  1 165 ? 4.609   -64.907  10.324  1.000 52.419  0 494 SER CCC C   1 ? 11 
ATOM   3859  O O   . SER C  1 165 ? 4.564   -64.862  11.566  1.000 54.442  0 494 SER CCC O   1 ? 11 
ATOM   3860  C CB  . SER C  1 165 ? 2.358   -64.445  9.276   1.000 55.798  0 494 SER CCC CB  1 ? 11 
ATOM   3861  O OG  . SER C  1 165 ? 2.923   -63.422  8.508   1.000 59.099  0 494 SER CCC OG  1 ? 11 
ATOM   3862  N N   . TYR C  1 166 ? 5.674   -64.530  9.623   1.000 50.284  0 495 TYR CCC N   1 ? 11 
ATOM   3863  C CA  . TYR C  1 166 ? 6.878   -63.915  10.235  1.000 50.596  0 495 TYR CCC CA  1 ? 11 
ATOM   3864  C C   . TYR C  1 166 ? 6.569   -62.460  10.589  1.000 52.007  0 495 TYR CCC C   1 ? 11 
ATOM   3865  O O   . TYR C  1 166 ? 7.046   -61.967  11.637  1.000 53.596  0 495 TYR CCC O   1 ? 11 
ATOM   3866  C CB  . TYR C  1 166 ? 8.095   -63.999  9.310   1.000 48.485  0 495 TYR CCC CB  1 ? 11 
ATOM   3867  C CG  . TYR C  1 166 ? 8.877   -65.283  9.416   1.000 46.148  0 495 TYR CCC CG  1 ? 11 
ATOM   3868  C CD1 . TYR C  1 166 ? 9.620   -65.585  10.543  1.000 45.708  0 495 TYR CCC CD1 1 ? 11 
ATOM   3869  C CD2 . TYR C  1 166 ? 8.867   -66.210  8.386   1.000 46.440  0 495 TYR CCC CD2 1 ? 11 
ATOM   3870  C CE1 . TYR C  1 166 ? 10.356  -66.762  10.630  1.000 45.472  0 495 TYR CCC CE1 1 ? 11 
ATOM   3871  C CE2 . TYR C  1 166 ? 9.616   -67.379  8.451   1.000 45.520  0 495 TYR CCC CE2 1 ? 11 
ATOM   3872  C CZ  . TYR C  1 166 ? 10.360  -67.657  9.578   1.000 44.381  0 495 TYR CCC CZ  1 ? 11 
ATOM   3873  O OH  . TYR C  1 166 ? 11.064  -68.819  9.636   1.000 44.516  0 495 TYR CCC OH  1 ? 11 
ATOM   3874  N N   . GLY C  1 167 ? 5.812   -61.744  9.760   1.000 53.309  0 496 GLY CCC N   1 ? 11 
ATOM   3875  C CA  . GLY C  1 167 ? 5.561   -60.317  10.050  1.000 58.170  0 496 GLY CCC CA  1 ? 11 
ATOM   3876  C C   . GLY C  1 167 ? 6.885   -59.560  10.168  1.000 60.396  0 496 GLY CCC C   1 ? 11 
ATOM   3877  O O   . GLY C  1 167 ? 7.270   -59.193  11.307  1.000 62.859  0 496 GLY CCC O   1 ? 11 
ATOM   3878  N N   . PHE C  1 168 ? 7.588   -59.380  9.043   1.000 57.370  0 497 PHE CCC N   1 ? 11 
ATOM   3879  C CA  . PHE C  1 168 ? 8.919   -58.744  8.980   1.000 56.335  0 497 PHE CCC CA  1 ? 11 
ATOM   3880  C C   . PHE C  1 168 ? 8.773   -57.228  8.883   1.000 57.753  0 497 PHE CCC C   1 ? 11 
ATOM   3881  O O   . PHE C  1 168 ? 8.194   -56.762  7.923   1.000 56.528  0 497 PHE CCC O   1 ? 11 
ATOM   3882  C CB  . PHE C  1 168 ? 9.699   -59.253  7.764   1.000 53.188  0 497 PHE CCC CB  1 ? 11 
ATOM   3883  C CG  . PHE C  1 168 ? 10.203  -60.667  7.886   1.000 49.053  0 497 PHE CCC CG  1 ? 11 
ATOM   3884  C CD1 . PHE C  1 168 ? 11.074  -61.037  8.901   1.000 47.285  0 497 PHE CCC CD1 1 ? 11 
ATOM   3885  C CD2 . PHE C  1 168 ? 9.843   -61.609  6.948   1.000 47.080  0 497 PHE CCC CD2 1 ? 11 
ATOM   3886  C CE1 . PHE C  1 168 ? 11.553  -62.336  8.977   1.000 46.003  0 497 PHE CCC CE1 1 ? 11 
ATOM   3887  C CE2 . PHE C  1 168 ? 10.322  -62.904  7.036   1.000 45.876  0 497 PHE CCC CE2 1 ? 11 
ATOM   3888  C CZ  . PHE C  1 168 ? 11.170  -63.264  8.051   1.000 44.189  0 497 PHE CCC CZ  1 ? 11 
ATOM   3889  N N   . GLN C  1 169 ? 9.314   -56.495  9.838   1.000 62.677  0 498 GLN CCC N   1 ? 11 
ATOM   3890  C CA  . GLN C  1 169 ? 9.327   -55.012  9.836   1.000 63.125  0 498 GLN CCC CA  1 ? 11 
ATOM   3891  C C   . GLN C  1 169 ? 10.751  -54.527  9.739   1.000 62.276  0 498 GLN CCC C   1 ? 11 
ATOM   3892  O O   . GLN C  1 169 ? 11.642  -55.111  10.343  1.000 64.742  0 498 GLN CCC O   1 ? 11 
ATOM   3893  C CB  . GLN C  1 169 ? 8.644   -54.471  11.082  1.000 66.670  0 498 GLN CCC CB  1 ? 11 
ATOM   3894  C CG  . GLN C  1 169 ? 7.220   -54.958  11.165  1.000 68.580  0 498 GLN CCC CG  1 ? 11 
ATOM   3895  C CD  . GLN C  1 169 ? 6.425   -54.117  12.119  1.000 72.240  0 498 GLN CCC CD  1 ? 11 
ATOM   3896  O OE1 . GLN C  1 169 ? 6.079   -52.969  11.822  1.000 76.563  0 498 GLN CCC OE1 1 ? 11 
ATOM   3897  N NE2 . GLN C  1 169 ? 6.143   -54.691  13.276  1.000 74.868  0 498 GLN CCC NE2 1 ? 11 
ATOM   3898  N N   . PRO C  1 170 ? 10.992  -53.443  8.968   1.000 63.949  0 499 PRO CCC N   1 ? 11 
ATOM   3899  C CA  . PRO C  1 170 ? 12.344  -52.939  8.753   1.000 62.406  0 499 PRO CCC CA  1 ? 11 
ATOM   3900  C C   . PRO C  1 170 ? 13.054  -52.586  10.075  1.000 61.389  0 499 PRO CCC C   1 ? 11 
ATOM   3901  O O   . PRO C  1 170 ? 14.265  -52.672  10.120  1.000 62.057  0 499 PRO CCC O   1 ? 11 
ATOM   3902  C CB  . PRO C  1 170 ? 12.172  -51.719  7.835   1.000 63.644  0 499 PRO CCC CB  1 ? 11 
ATOM   3903  C CG  . PRO C  1 170 ? 10.691  -51.358  7.904   1.000 65.605  0 499 PRO CCC CG  1 ? 11 
ATOM   3904  C CD  . PRO C  1 170 ? 9.966   -52.620  8.300   1.000 65.809  0 499 PRO CCC CD  1 ? 11 
ATOM   3905  N N   . THR C  1 171 ? 12.293  -52.250  11.119  1.000 60.441  0 500 THR CCC N   1 ? 11 
ATOM   3906  C CA  . THR C  1 171 ? 12.798  -51.865  12.470  1.000 60.592  0 500 THR CCC CA  1 ? 11 
ATOM   3907  C C   . THR C  1 171 ? 13.061  -53.078  13.388  1.000 57.939  0 500 THR CCC C   1 ? 11 
ATOM   3908  O O   . THR C  1 171 ? 13.632  -52.862  14.459  1.000 59.053  0 500 THR CCC O   1 ? 11 
ATOM   3909  C CB  . THR C  1 171 ? 11.810  -50.896  13.133  1.000 61.958  0 500 THR CCC CB  1 ? 11 
ATOM   3910  O OG1 . THR C  1 171 ? 10.529  -51.534  13.125  1.000 61.196  0 500 THR CCC OG1 1 ? 11 
ATOM   3911  C CG2 . THR C  1 171 ? 11.771  -49.558  12.426  1.000 62.536  0 500 THR CCC CG2 1 ? 11 
ATOM   3912  N N   . ASN C  1 172 ? 12.682  -54.300  13.012  1.000 56.866  0 501 ASN CCC N   1 ? 11 
ATOM   3913  C CA  . ASN C  1 172 ? 13.024  -55.538  13.772  1.000 55.860  0 501 ASN CCC CA  1 ? 11 
ATOM   3914  C C   . ASN C  1 172 ? 14.510  -55.566  14.129  1.000 53.978  0 501 ASN CCC C   1 ? 11 
ATOM   3915  O O   . ASN C  1 172 ? 15.304  -55.104  13.303  1.000 53.362  0 501 ASN CCC O   1 ? 11 
ATOM   3916  C CB  . ASN C  1 172 ? 12.719  -56.807  12.967  1.000 55.403  0 501 ASN CCC CB  1 ? 11 
ATOM   3917  C CG  . ASN C  1 172 ? 11.236  -57.071  12.858  1.000 56.734  0 501 ASN CCC CG  1 ? 11 
ATOM   3918  O OD1 . ASN C  1 172 ? 10.438  -56.325  13.411  1.000 58.729  0 501 ASN CCC OD1 1 ? 11 
ATOM   3919  N ND2 . ASN C  1 172 ? 10.870  -58.127  12.159  1.000 55.898  0 501 ASN CCC ND2 1 ? 11 
ATOM   3920  N N   . GLY C  1 173 ? 14.867  -56.142  15.281  1.000 53.384  0 502 GLY CCC N   1 ? 11 
ATOM   3921  C CA  . GLY C  1 173 ? 16.249  -56.559  15.587  1.000 54.028  0 502 GLY CCC CA  1 ? 11 
ATOM   3922  C C   . GLY C  1 173 ? 16.819  -57.456  14.499  1.000 53.512  0 502 GLY CCC C   1 ? 11 
ATOM   3923  O O   . GLY C  1 173 ? 16.020  -58.123  13.836  1.000 52.872  0 502 GLY CCC O   1 ? 11 
ATOM   3924  N N   . VAL C  1 174 ? 18.141  -57.506  14.315  1.000 54.356  0 503 VAL CCC N   1 ? 11 
ATOM   3925  C CA  . VAL C  1 174 ? 18.782  -58.205  13.161  1.000 53.387  0 503 VAL CCC CA  1 ? 11 
ATOM   3926  C C   . VAL C  1 174 ? 18.374  -59.692  13.157  1.000 53.154  0 503 VAL CCC C   1 ? 11 
ATOM   3927  O O   . VAL C  1 174 ? 18.102  -60.236  12.052  1.000 50.741  0 503 VAL CCC O   1 ? 11 
ATOM   3928  C CB  . VAL C  1 174 ? 20.313  -58.027  13.163  1.000 53.045  0 503 VAL CCC CB  1 ? 11 
ATOM   3929  C CG1 . VAL C  1 174 ? 20.968  -58.783  12.000  1.000 53.285  0 503 VAL CCC CG1 1 ? 11 
ATOM   3930  C CG2 . VAL C  1 174 ? 20.684  -56.557  13.103  1.000 53.464  0 503 VAL CCC CG2 1 ? 11 
ATOM   3931  N N   . GLY C  1 175 ? 18.336  -60.322  14.333  1.000 52.942  0 504 GLY CCC N   1 ? 11 
ATOM   3932  C CA  . GLY C  1 175 ? 17.919  -61.730  14.505  1.000 55.015  0 504 GLY CCC CA  1 ? 11 
ATOM   3933  C C   . GLY C  1 175 ? 16.503  -61.970  14.012  1.000 56.100  0 504 GLY CCC C   1 ? 11 
ATOM   3934  O O   . GLY C  1 175 ? 16.217  -63.115  13.651  1.000 58.088  0 504 GLY CCC O   1 ? 11 
ATOM   3935  N N   . TYR C  1 176 ? 15.644  -60.947  13.989  1.000 56.860  0 505 TYR CCC N   1 ? 11 
ATOM   3936  C CA  . TYR C  1 176 ? 14.226  -61.068  13.559  1.000 58.694  0 505 TYR CCC CA  1 ? 11 
ATOM   3937  C C   . TYR C  1 176 ? 14.031  -60.489  12.147  1.000 56.925  0 505 TYR CCC C   1 ? 11 
ATOM   3938  O O   . TYR C  1 176 ? 12.885  -60.440  11.676  1.000 57.831  0 505 TYR CCC O   1 ? 11 
ATOM   3939  C CB  . TYR C  1 176 ? 13.310  -60.411  14.586  1.000 62.796  0 505 TYR CCC CB  1 ? 11 
ATOM   3940  C CG  . TYR C  1 176 ? 13.309  -61.084  15.938  1.000 68.992  0 505 TYR CCC CG  1 ? 11 
ATOM   3941  C CD1 . TYR C  1 176 ? 14.261  -60.778  16.907  1.000 71.738  0 505 TYR CCC CD1 1 ? 11 
ATOM   3942  C CD2 . TYR C  1 176 ? 12.323  -62.011  16.265  1.000 73.072  0 505 TYR CCC CD2 1 ? 11 
ATOM   3943  C CE1 . TYR C  1 176 ? 14.233  -61.377  18.162  1.000 75.293  0 505 TYR CCC CE1 1 ? 11 
ATOM   3944  C CE2 . TYR C  1 176 ? 12.290  -62.632  17.510  1.000 75.578  0 505 TYR CCC CE2 1 ? 11 
ATOM   3945  C CZ  . TYR C  1 176 ? 13.249  -62.313  18.461  1.000 76.818  0 505 TYR CCC CZ  1 ? 11 
ATOM   3946  O OH  . TYR C  1 176 ? 13.196  -62.917  19.684  1.000 78.490  0 505 TYR CCC OH  1 ? 11 
ATOM   3947  N N   . GLN C  1 177 ? 15.109  -60.092  11.464  1.000 54.175  0 506 GLN CCC N   1 ? 11 
ATOM   3948  C CA  . GLN C  1 177 ? 15.024  -59.615  10.061  1.000 49.959  0 506 GLN CCC CA  1 ? 11 
ATOM   3949  C C   . GLN C  1 177 ? 15.000  -60.810  9.120   1.000 47.530  0 506 GLN CCC C   1 ? 11 
ATOM   3950  O O   . GLN C  1 177 ? 15.500  -61.892  9.441   1.000 48.380  0 506 GLN CCC O   1 ? 11 
ATOM   3951  C CB  . GLN C  1 177 ? 16.183  -58.693  9.720   1.000 47.902  0 506 GLN CCC CB  1 ? 11 
ATOM   3952  C CG  . GLN C  1 177 ? 15.974  -57.304  10.279  1.000 49.303  0 506 GLN CCC CG  1 ? 11 
ATOM   3953  C CD  . GLN C  1 177 ? 17.185  -56.428  10.111  1.000 47.675  0 506 GLN CCC CD  1 ? 11 
ATOM   3954  O OE1 . GLN C  1 177 ? 18.006  -56.594  9.207   1.000 46.860  0 506 GLN CCC OE1 1 ? 11 
ATOM   3955  N NE2 . GLN C  1 177 ? 17.281  -55.488  11.018  1.000 48.145  0 506 GLN CCC NE2 1 ? 11 
ATOM   3956  N N   . PRO C  1 178 ? 14.419  -60.654  7.916   1.000 45.325  0 507 PRO CCC N   1 ? 11 
ATOM   3957  C CA  . PRO C  1 178 ? 14.380  -61.754  6.967   1.000 44.582  0 507 PRO CCC CA  1 ? 11 
ATOM   3958  C C   . PRO C  1 178 ? 15.775  -62.007  6.391   1.000 44.192  0 507 PRO CCC C   1 ? 11 
ATOM   3959  O O   . PRO C  1 178 ? 16.518  -61.057  6.160   1.000 43.576  0 507 PRO CCC O   1 ? 11 
ATOM   3960  C CB  . PRO C  1 178 ? 13.407  -61.261  5.898   1.000 44.426  0 507 PRO CCC CB  1 ? 11 
ATOM   3961  C CG  . PRO C  1 178 ? 13.562  -59.764  5.926   1.000 45.277  0 507 PRO CCC CG  1 ? 11 
ATOM   3962  C CD  . PRO C  1 178 ? 13.815  -59.427  7.384   1.000 46.505  0 507 PRO CCC CD  1 ? 11 
ATOM   3963  N N   . TYR C  1 179 ? 16.105  -63.280  6.221   1.000 42.714  0 508 TYR CCC N   1 ? 11 
ATOM   3964  C CA  . TYR C  1 179 ? 17.319  -63.740  5.522   1.000 43.175  0 508 TYR CCC CA  1 ? 11 
ATOM   3965  C C   . TYR C  1 179 ? 16.863  -64.679  4.418   1.000 43.246  0 508 TYR CCC C   1 ? 11 
ATOM   3966  O O   . TYR C  1 179 ? 16.012  -65.535  4.648   1.000 43.260  0 508 TYR CCC O   1 ? 11 
ATOM   3967  C CB  . TYR C  1 179 ? 18.296  -64.419  6.484   1.000 43.125  0 508 TYR CCC CB  1 ? 11 
ATOM   3968  C CG  . TYR C  1 179 ? 19.142  -63.434  7.240   1.000 44.061  0 508 TYR CCC CG  1 ? 11 
ATOM   3969  C CD1 . TYR C  1 179 ? 18.586  -62.591  8.186   1.000 46.013  0 508 TYR CCC CD1 1 ? 11 
ATOM   3970  C CD2 . TYR C  1 179 ? 20.498  -63.331  7.018   1.000 45.173  0 508 TYR CCC CD2 1 ? 11 
ATOM   3971  C CE1 . TYR C  1 179 ? 19.352  -61.678  8.895   1.000 45.725  0 508 TYR CCC CE1 1 ? 11 
ATOM   3972  C CE2 . TYR C  1 179 ? 21.279  -62.413  7.712   1.000 46.116  0 508 TYR CCC CE2 1 ? 11 
ATOM   3973  C CZ  . TYR C  1 179 ? 20.707  -61.583  8.651   1.000 44.446  0 508 TYR CCC CZ  1 ? 11 
ATOM   3974  O OH  . TYR C  1 179 ? 21.491  -60.686  9.306   1.000 47.223  0 508 TYR CCC OH  1 ? 11 
ATOM   3975  N N   . ARG C  1 180 ? 17.388  -64.449  3.222   1.000 43.151  0 509 ARG CCC N   1 ? 11 
ATOM   3976  C CA  . ARG C  1 180 ? 17.267  -65.382  2.091   1.000 40.608  0 509 ARG CCC CA  1 ? 11 
ATOM   3977  C C   . ARG C  1 180 ? 18.345  -66.444  2.241   1.000 39.362  0 509 ARG CCC C   1 ? 11 
ATOM   3978  O O   . ARG C  1 180 ? 19.468  -66.107  2.651   1.000 37.212  0 509 ARG CCC O   1 ? 11 
ATOM   3979  C CB  . ARG C  1 180 ? 17.368  -64.611  0.782   1.000 42.009  0 509 ARG CCC CB  1 ? 11 
ATOM   3980  C CG  . ARG C  1 180 ? 16.104  -63.810  0.544   1.000 43.311  0 509 ARG CCC CG  1 ? 11 
ATOM   3981  C CD  . ARG C  1 180 ? 16.179  -63.010  -0.718  1.000 44.406  0 509 ARG CCC CD  1 ? 11 
ATOM   3982  N NE  . ARG C  1 180 ? 14.917  -62.310  -0.845  1.000 44.930  0 509 ARG CCC NE  1 ? 11 
ATOM   3983  C CZ  . ARG C  1 180 ? 14.485  -61.744  -1.942  1.000 44.500  0 509 ARG CCC CZ  1 ? 11 
ATOM   3984  N NH1 . ARG C  1 180 ? 15.213  -61.797  -3.042  1.000 43.954  0 509 ARG CCC NH1 1 ? 11 
ATOM   3985  N NH2 . ARG C  1 180 ? 13.312  -61.147  -1.927  1.000 45.545  0 509 ARG CCC NH2 1 ? 11 
ATOM   3986  N N   . VAL C  1 181 ? 17.973  -67.677  1.922   1.000 38.324  0 510 VAL CCC N   1 ? 11 
ATOM   3987  C CA  . VAL C  1 181 ? 18.850  -68.867  2.018   1.000 38.621  0 510 VAL CCC CA  1 ? 11 
ATOM   3988  C C   . VAL C  1 181 ? 18.839  -69.585  0.662   1.000 38.378  0 510 VAL CCC C   1 ? 11 
ATOM   3989  O O   . VAL C  1 181 ? 17.748  -69.714  0.039   1.000 36.492  0 510 VAL CCC O   1 ? 11 
ATOM   3990  C CB  . VAL C  1 181 ? 18.363  -69.772  3.159   1.000 39.687  0 510 VAL CCC CB  1 ? 11 
ATOM   3991  C CG1 . VAL C  1 181 ? 19.305  -70.948  3.358   1.000 40.315  0 510 VAL CCC CG1 1 ? 11 
ATOM   3992  C CG2 . VAL C  1 181 ? 18.167  -68.990  4.460   1.000 39.128  0 510 VAL CCC CG2 1 ? 11 
ATOM   3993  N N   . VAL C  1 182 ? 20.026  -69.983  0.208   1.000 38.293  0 511 VAL CCC N   1 ? 11 
ATOM   3994  C CA  . VAL C  1 182 ? 20.204  -70.918  -0.928  1.000 35.595  0 511 VAL CCC CA  1 ? 11 
ATOM   3995  C C   . VAL C  1 182 ? 21.026  -72.091  -0.403  1.000 36.663  0 511 VAL CCC C   1 ? 11 
ATOM   3996  O O   . VAL C  1 182 ? 22.091  -71.861  0.211   1.000 34.832  0 511 VAL CCC O   1 ? 11 
ATOM   3997  C CB  . VAL C  1 182 ? 20.868  -70.243  -2.130  1.000 36.828  0 511 VAL CCC CB  1 ? 11 
ATOM   3998  C CG1 . VAL C  1 182 ? 21.183  -71.254  -3.213  1.000 37.509  0 511 VAL CCC CG1 1 ? 11 
ATOM   3999  C CG2 . VAL C  1 182 ? 19.976  -69.162  -2.705  1.000 37.694  0 511 VAL CCC CG2 1 ? 11 
ATOM   4000  N N   . VAL C  1 183 ? 20.489  -73.289  -0.594  1.000 35.878  0 512 VAL CCC N   1 ? 11 
ATOM   4001  C CA  . VAL C  1 183 ? 21.161  -74.571  -0.295  1.000 38.345  0 512 VAL CCC CA  1 ? 11 
ATOM   4002  C C   . VAL C  1 183 ? 21.487  -75.223  -1.637  1.000 39.477  0 512 VAL CCC C   1 ? 11 
ATOM   4003  O O   . VAL C  1 183 ? 20.547  -75.455  -2.423  1.000 41.571  0 512 VAL CCC O   1 ? 11 
ATOM   4004  C CB  . VAL C  1 183 ? 20.282  -75.481  0.582   1.000 40.002  0 512 VAL CCC CB  1 ? 11 
ATOM   4005  C CG1 . VAL C  1 183 ? 21.000  -76.763  0.938   1.000 38.848  0 512 VAL CCC CG1 1 ? 11 
ATOM   4006  C CG2 . VAL C  1 183 ? 19.846  -74.774  1.854   1.000 40.855  0 512 VAL CCC CG2 1 ? 11 
ATOM   4007  N N   . LEU C  1 184 ? 22.770  -75.426  -1.905  1.000 38.551  0 513 LEU CCC N   1 ? 11 
ATOM   4008  C CA  . LEU C  1 184 ? 23.249  -76.129  -3.104  1.000 38.648  0 513 LEU CCC CA  1 ? 11 
ATOM   4009  C C   . LEU C  1 184 ? 23.564  -77.566  -2.686  1.000 38.775  0 513 LEU CCC C   1 ? 11 
ATOM   4010  O O   . LEU C  1 184 ? 24.467  -77.727  -1.892  1.000 39.889  0 513 LEU CCC O   1 ? 11 
ATOM   4011  C CB  . LEU C  1 184 ? 24.472  -75.393  -3.663  1.000 39.279  0 513 LEU CCC CB  1 ? 11 
ATOM   4012  C CG  . LEU C  1 184 ? 24.237  -73.957  -4.132  1.000 39.494  0 513 LEU CCC CG  1 ? 11 
ATOM   4013  C CD1 . LEU C  1 184 ? 25.542  -73.384  -4.675  1.000 38.867  0 513 LEU CCC CD1 1 ? 11 
ATOM   4014  C CD2 . LEU C  1 184 ? 23.201  -73.871  -5.246  1.000 40.815  0 513 LEU CCC CD2 1 ? 11 
ATOM   4015  N N   . SER C  1 185 ? 22.803  -78.526  -3.193  1.000 41.402  0 514 SER CCC N   1 ? 11 
ATOM   4016  C CA  . SER C  1 185 ? 23.049  -79.985  -3.120  1.000 43.128  0 514 SER CCC CA  1 ? 11 
ATOM   4017  C C   . SER C  1 185 ? 23.891  -80.435  -4.306  1.000 45.064  0 514 SER CCC C   1 ? 11 
ATOM   4018  O O   . SER C  1 185 ? 23.530  -80.089  -5.431  1.000 46.299  0 514 SER CCC O   1 ? 11 
ATOM   4019  C CB  . SER C  1 185 ? 21.773  -80.732  -3.124  1.000 43.581  0 514 SER CCC CB  1 ? 11 
ATOM   4020  O OG  . SER C  1 185 ? 21.244  -80.744  -1.833  1.000 46.295  0 514 SER CCC OG  1 ? 11 
ATOM   4021  N N   . PHE C  1 186 ? 24.943  -81.202  -4.051  1.000 44.895  0 515 PHE CCC N   1 ? 11 
ATOM   4022  C CA  . PHE C  1 186 ? 25.805  -81.787  -5.116  1.000 45.127  0 515 PHE CCC CA  1 ? 11 
ATOM   4023  C C   . PHE C  1 186 ? 25.500  -83.275  -5.267  1.000 43.734  0 515 PHE CCC C   1 ? 11 
ATOM   4024  O O   . PHE C  1 186 ? 25.664  -83.939  -4.303  1.000 45.789  0 515 PHE CCC O   1 ? 11 
ATOM   4025  C CB  . PHE C  1 186 ? 27.279  -81.507  -4.811  1.000 45.397  0 515 PHE CCC CB  1 ? 11 
ATOM   4026  C CG  . PHE C  1 186 ? 27.630  -80.045  -4.647  1.000 44.151  0 515 PHE CCC CG  1 ? 11 
ATOM   4027  C CD1 . PHE C  1 186 ? 26.972  -79.079  -5.385  1.000 44.440  0 515 PHE CCC CD1 1 ? 11 
ATOM   4028  C CD2 . PHE C  1 186 ? 28.616  -79.629  -3.765  1.000 41.728  0 515 PHE CCC CD2 1 ? 11 
ATOM   4029  C CE1 . PHE C  1 186 ? 27.233  -77.728  -5.189  1.000 42.845  0 515 PHE CCC CE1 1 ? 11 
ATOM   4030  C CE2 . PHE C  1 186 ? 28.937  -78.285  -3.643  1.000 41.827  0 515 PHE CCC CE2 1 ? 11 
ATOM   4031  C CZ  . PHE C  1 186 ? 28.251  -77.332  -4.364  1.000 40.530  0 515 PHE CCC CZ  1 ? 11 
ATOM   4032  N N   . GLU C  1 187 ? 24.976  -83.723  -6.388  1.000 45.854  0 516 GLU CCC N   1 ? 11 
ATOM   4033  C CA  . GLU C  1 187 ? 24.482  -85.109  -6.601  1.000 47.385  0 516 GLU CCC CA  1 ? 11 
ATOM   4034  C C   . GLU C  1 187 ? 25.457  -85.869  -7.512  1.000 47.717  0 516 GLU CCC C   1 ? 11 
ATOM   4035  O O   . GLU C  1 187 ? 25.889  -85.333  -8.515  1.000 46.533  0 516 GLU CCC O   1 ? 11 
ATOM   4036  C CB  . GLU C  1 187 ? 23.096  -85.062  -7.261  1.000 49.647  0 516 GLU CCC CB  1 ? 11 
ATOM   4037  C CG  . GLU C  1 187 ? 22.313  -86.364  -7.108  1.000 51.380  0 516 GLU CCC CG  1 ? 11 
ATOM   4038  C CD  . GLU C  1 187 ? 21.002  -86.383  -7.850  1.000 51.705  0 516 GLU CCC CD  1 ? 11 
ATOM   4039  O OE1 . GLU C  1 187 ? 20.960  -85.891  -9.017  1.000 50.507  0 516 GLU CCC OE1 1 ? 11 
ATOM   4040  O OE2 . GLU C  1 187 ? 20.032  -86.912  -7.254  1.000 58.712  0 516 GLU CCC OE2 1 ? 11 
ATOM   4041  N N   . LEU C  1 188 ? 25.749  -87.115  -7.180  1.000 51.430  0 517 LEU CCC N   1 ? 11 
ATOM   4042  C CA  . LEU C  1 188 ? 26.470  -88.084  -8.031  1.000 52.894  0 517 LEU CCC CA  1 ? 11 
ATOM   4043  C C   . LEU C  1 188 ? 25.591  -89.310  -8.268  1.000 52.924  0 517 LEU CCC C   1 ? 11 
ATOM   4044  O O   . LEU C  1 188 ? 25.391  -90.028  -7.336  1.000 56.951  0 517 LEU CCC O   1 ? 11 
ATOM   4045  C CB  . LEU C  1 188 ? 27.780  -88.422  -7.322  1.000 55.723  0 517 LEU CCC CB  1 ? 11 
ATOM   4046  C CG  . LEU C  1 188 ? 28.892  -87.385  -7.516  1.000 57.645  0 517 LEU CCC CG  1 ? 11 
ATOM   4047  C CD1 . LEU C  1 188 ? 30.065  -87.672  -6.574  1.000 57.349  0 517 LEU CCC CD1 1 ? 11 
ATOM   4048  C CD2 . LEU C  1 188 ? 29.353  -87.393  -8.972  1.000 57.642  0 517 LEU CCC CD2 1 ? 11 
ATOM   4049  N N   . LEU C  1 189 ? 24.962  -89.414  -9.434  1.000 52.195  0 518 LEU CCC N   1 ? 11 
ATOM   4050  C CA  . LEU C  1 189 ? 24.292  -90.654  -9.900  1.000 53.766  0 518 LEU CCC CA  1 ? 11 
ATOM   4051  C C   . LEU C  1 189 ? 25.236  -91.417  -10.818 1.000 54.279  0 518 LEU CCC C   1 ? 11 
ATOM   4052  O O   . LEU C  1 189 ? 26.299  -90.880  -11.113 1.000 54.289  0 518 LEU CCC O   1 ? 11 
ATOM   4053  C CB  . LEU C  1 189 ? 22.996  -90.298  -10.636 1.000 54.849  0 518 LEU CCC CB  1 ? 11 
ATOM   4054  C CG  . LEU C  1 189 ? 22.059  -89.398  -9.840  1.000 54.123  0 518 LEU CCC CG  1 ? 11 
ATOM   4055  C CD1 . LEU C  1 189 ? 20.838  -88.994  -10.671 1.000 56.277  0 518 LEU CCC CD1 1 ? 11 
ATOM   4056  C CD2 . LEU C  1 189 ? 21.681  -90.030  -8.495  1.000 52.043  0 518 LEU CCC CD2 1 ? 11 
ATOM   4057  N N   . HIS C  1 190 ? 24.842  -92.610  -11.265 1.000 54.435  0 519 HIS CCC N   1 ? 11 
ATOM   4058  C CA  . HIS C  1 190 ? 25.612  -93.386  -12.268 1.000 56.655  0 519 HIS CCC CA  1 ? 11 
ATOM   4059  C C   . HIS C  1 190 ? 25.153  -92.898  -13.644 1.000 58.749  0 519 HIS CCC C   1 ? 11 
ATOM   4060  O O   . HIS C  1 190 ? 24.385  -93.607  -14.331 1.000 61.714  0 519 HIS CCC O   1 ? 11 
ATOM   4061  C CB  . HIS C  1 190 ? 25.469  -94.884  -12.051 1.000 56.614  0 519 HIS CCC CB  1 ? 11 
ATOM   4062  C CG  . HIS C  1 190 ? 26.302  -95.645  -13.015 1.000 57.475  0 519 HIS CCC CG  1 ? 11 
ATOM   4063  N ND1 . HIS C  1 190 ? 27.660  -95.405  -13.176 1.000 58.356  0 519 HIS CCC ND1 1 ? 11 
ATOM   4064  C CD2 . HIS C  1 190 ? 25.979  -96.605  -13.899 1.000 58.080  0 519 HIS CCC CD2 1 ? 11 
ATOM   4065  C CE1 . HIS C  1 190 ? 28.146  -96.240  -14.085 1.000 59.193  0 519 HIS CCC CE1 1 ? 11 
ATOM   4066  N NE2 . HIS C  1 190 ? 27.134  -96.980  -14.544 1.000 58.919  0 519 HIS CCC NE2 1 ? 11 
ATOM   4067  N N   . ALA C  1 191 ? 25.600  -91.698  -13.993 1.000 57.573  0 520 ALA CCC N   1 ? 11 
ATOM   4068  C CA  . ALA C  1 191 ? 25.224  -90.925  -15.192 1.000 58.379  0 520 ALA CCC CA  1 ? 11 
ATOM   4069  C C   . ALA C  1 191 ? 26.412  -90.047  -15.571 1.000 58.844  0 520 ALA CCC C   1 ? 11 
ATOM   4070  O O   . ALA C  1 191 ? 27.273  -89.771  -14.733 1.000 56.557  0 520 ALA CCC O   1 ? 11 
ATOM   4071  C CB  . ALA C  1 191 ? 23.984  -90.118  -14.913 1.000 54.900  0 520 ALA CCC CB  1 ? 11 
ATOM   4072  N N   . PRO C  1 192 ? 26.522  -89.570  -16.831 1.000 58.955  0 521 PRO CCC N   1 ? 11 
ATOM   4073  C CA  . PRO C  1 192 ? 27.543  -88.575  -17.155 1.000 57.428  0 521 PRO CCC CA  1 ? 11 
ATOM   4074  C C   . PRO C  1 192 ? 27.428  -87.342  -16.254 1.000 54.898  0 521 PRO CCC C   1 ? 11 
ATOM   4075  O O   . PRO C  1 192 ? 26.308  -86.910  -15.937 1.000 56.468  0 521 PRO CCC O   1 ? 11 
ATOM   4076  C CB  . PRO C  1 192 ? 27.237  -88.234  -18.618 1.000 59.752  0 521 PRO CCC CB  1 ? 11 
ATOM   4077  C CG  . PRO C  1 192 ? 26.594  -89.511  -19.153 1.000 61.762  0 521 PRO CCC CG  1 ? 11 
ATOM   4078  C CD  . PRO C  1 192 ? 25.734  -89.994  -17.999 1.000 59.667  0 521 PRO CCC CD  1 ? 11 
ATOM   4079  N N   . ALA C  1 193 ? 28.563  -86.813  -15.804 1.000 52.569  0 522 ALA CCC N   1 ? 11 
ATOM   4080  C CA  . ALA C  1 193 ? 28.603  -85.563  -15.018 1.000 50.482  0 522 ALA CCC CA  1 ? 11 
ATOM   4081  C C   . ALA C  1 193 ? 28.200  -84.442  -15.975 1.000 50.582  0 522 ALA CCC C   1 ? 11 
ATOM   4082  O O   . ALA C  1 193 ? 28.668  -84.436  -17.102 1.000 55.663  0 522 ALA CCC O   1 ? 11 
ATOM   4083  C CB  . ALA C  1 193 ? 29.992  -85.346  -14.481 1.000 49.832  0 522 ALA CCC CB  1 ? 11 
ATOM   4084  N N   . THR C  1 194 ? 27.262  -83.594  -15.585 1.000 50.025  0 523 THR CCC N   1 ? 11 
ATOM   4085  C CA  . THR C  1 194 ? 26.712  -82.552  -16.495 1.000 49.074  0 523 THR CCC CA  1 ? 11 
ATOM   4086  C C   . THR C  1 194 ? 27.009  -81.170  -15.904 1.000 46.965  0 523 THR CCC C   1 ? 11 
ATOM   4087  O O   . THR C  1 194 ? 26.936  -80.215  -16.623 1.000 48.263  0 523 THR CCC O   1 ? 11 
ATOM   4088  C CB  . THR C  1 194 ? 25.225  -82.799  -16.778 1.000 48.914  0 523 THR CCC CB  1 ? 11 
ATOM   4089  O OG1 . THR C  1 194 ? 24.456  -82.391  -15.646 1.000 47.038  0 523 THR CCC OG1 1 ? 11 
ATOM   4090  C CG2 . THR C  1 194 ? 24.899  -84.237  -17.113 1.000 49.791  0 523 THR CCC CG2 1 ? 11 
ATOM   4091  N N   . VAL C  1 195 ? 27.425  -81.102  -14.652 1.000 45.540  0 524 VAL CCC N   1 ? 11 
ATOM   4092  C CA  . VAL C  1 195 ? 27.829  -79.837  -13.988 1.000 47.935  0 524 VAL CCC CA  1 ? 11 
ATOM   4093  C C   . VAL C  1 195 ? 29.292  -79.965  -13.576 1.000 49.129  0 524 VAL CCC C   1 ? 11 
ATOM   4094  O O   . VAL C  1 195 ? 29.588  -80.782  -12.737 1.000 49.975  0 524 VAL CCC O   1 ? 11 
ATOM   4095  C CB  . VAL C  1 195 ? 26.937  -79.518  -12.790 1.000 45.728  0 524 VAL CCC CB  1 ? 11 
ATOM   4096  C CG1 . VAL C  1 195 ? 27.424  -78.244  -12.155 1.000 45.125  0 524 VAL CCC CG1 1 ? 11 
ATOM   4097  C CG2 . VAL C  1 195 ? 25.470  -79.408  -13.211 1.000 46.340  0 524 VAL CCC CG2 1 ? 11 
ATOM   4098  N N   . CYS C  1 196 ? 30.151  -79.183  -14.218 1.000 49.210  0 525 CYS CCC N   1 ? 11 
ATOM   4099  C CA  . CYS C  1 196 ? 31.618  -79.164  -14.015 1.000 50.697  0 525 CYS CCC CA  1 ? 11 
ATOM   4100  C C   . CYS C  1 196 ? 32.055  -77.718  -13.813 1.000 49.178  0 525 CYS CCC C   1 ? 11 
ATOM   4101  O O   . CYS C  1 196 ? 31.341  -76.799  -14.307 1.000 47.679  0 525 CYS CCC O   1 ? 11 
ATOM   4102  C CB  . CYS C  1 196 ? 32.349  -79.791  -15.196 1.000 54.546  0 525 CYS CCC CB  1 ? 11 
ATOM   4103  S SG  . CYS C  1 196 ? 32.171  -81.603  -15.202 1.000 58.142  0 525 CYS CCC SG  1 ? 11 
ATOM   4104  N N   . GLY C  1 197 ? 33.182  -77.560  -13.124 1.000 49.240  0 526 GLY CCC N   1 ? 11 
ATOM   4105  C CA  . GLY C  1 197 ? 33.848  -76.259  -12.999 1.000 51.859  0 526 GLY CCC CA  1 ? 11 
ATOM   4106  C C   . GLY C  1 197 ? 34.486  -75.849  -14.324 1.000 52.648  0 526 GLY CCC C   1 ? 11 
ATOM   4107  O O   . GLY C  1 197 ? 34.558  -76.646  -15.266 1.000 52.161  0 526 GLY CCC O   1 ? 11 
ATOM   4108  N N   . PRO C  1 198 ? 34.951  -74.589  -14.425 1.000 56.641  0 527 PRO CCC N   1 ? 11 
ATOM   4109  C CA  . PRO C  1 198 ? 35.616  -74.119  -15.654 1.000 62.119  0 527 PRO CCC CA  1 ? 11 
ATOM   4110  C C   . PRO C  1 198 ? 36.874  -74.914  -16.038 1.000 70.799  0 527 PRO CCC C   1 ? 11 
ATOM   4111  O O   . PRO C  1 198 ? 37.404  -75.553  -15.158 1.000 67.550  0 527 PRO CCC O   1 ? 11 
ATOM   4112  C CB  . PRO C  1 198 ? 36.008  -72.686  -15.322 1.000 59.428  0 527 PRO CCC CB  1 ? 11 
ATOM   4113  C CG  . PRO C  1 198 ? 35.159  -72.297  -14.096 1.000 57.534  0 527 PRO CCC CG  1 ? 11 
ATOM   4114  C CD  . PRO C  1 198 ? 34.862  -73.581  -13.338 1.000 56.539  0 527 PRO CCC CD  1 ? 11 
ATOM   4115  N N   . LYS C  1 199 ? 37.352  -74.760  -17.282 1.000 65.841  0 528 LYS CCC N   1 ? ?  
ATOM   4116  C CA  . LYS C  1 199 ? 38.446  -75.566  -17.896 1.000 72.612  0 528 LYS CCC CA  1 ? ?  
ATOM   4117  C C   . LYS C  1 199 ? 39.794  -74.830  -17.809 1.000 68.584  0 528 LYS CCC C   1 ? ?  
ATOM   4118  O O   . LYS C  1 199 ? 39.907  -73.633  -17.524 1.000 66.174  0 528 LYS CCC O   1 ? ?  
ATOM   4119  C CB  . LYS C  1 199 ? 38.087  -75.875  -19.352 1.000 78.193  0 528 LYS CCC CB  1 ? ?  
ATOM   4120  C CG  . LYS C  1 199 ? 39.041  -76.837  -20.041 1.000 90.536  0 528 LYS CCC CG  1 ? ?  
ATOM   4121  C CD  . LYS C  1 199 ? 38.580  -77.274  -21.408 1.000 96.111  0 528 LYS CCC CD  1 ? ?  
ATOM   4122  C CE  . LYS C  1 199 ? 39.668  -77.989  -22.182 1.000 99.457  0 528 LYS CCC CE  1 ? ?  
ATOM   4123  N NZ  . LYS C  1 199 ? 39.134  -78.648  -23.398 1.000 98.308  0 528 LYS CCC NZ  1 ? ?  
ATOM   4124  N N   . GLN D  2 1   ? 25.773  -81.640  20.715  1.000 70.427  0 1   GLN DDD N   1 ? 12 
ATOM   4125  C CA  . GLN D  2 1   ? 26.674  -80.843  21.542  1.000 68.340  0 1   GLN DDD CA  1 ? 12 
ATOM   4126  C C   . GLN D  2 1   ? 28.056  -81.528  21.544  1.000 63.393  0 1   GLN DDD C   1 ? 12 
ATOM   4127  O O   . GLN D  2 1   ? 28.176  -82.703  21.938  1.000 59.478  0 1   GLN DDD O   1 ? 12 
ATOM   4128  C CB  . GLN D  2 1   ? 26.050  -80.649  22.926  1.000 75.515  0 1   GLN DDD CB  1 ? 12 
ATOM   4129  C CG  . GLN D  2 1   ? 26.959  -80.020  24.009  1.000 79.141  0 1   GLN DDD CG  1 ? 12 
ATOM   4130  C CD  . GLN D  2 1   ? 27.455  -78.597  23.826  1.000 82.129  0 1   GLN DDD CD  1 ? 12 
ATOM   4131  O OE1 . GLN D  2 1   ? 27.005  -77.855  22.951  1.000 87.865  0 1   GLN DDD OE1 1 ? 12 
ATOM   4132  N NE2 . GLN D  2 1   ? 28.385  -78.196  24.689  1.000 80.788  0 1   GLN DDD NE2 1 ? 12 
ATOM   4133  N N   . VAL D  2 2   ? 29.084  -80.783  21.138  1.000 58.003  0 2   VAL DDD N   1 ? 12 
ATOM   4134  C CA  . VAL D  2 2   ? 30.510  -81.167  21.239  1.000 53.689  0 2   VAL DDD CA  1 ? 12 
ATOM   4135  C C   . VAL D  2 2   ? 31.179  -80.323  22.331  1.000 50.870  0 2   VAL DDD C   1 ? 12 
ATOM   4136  O O   . VAL D  2 2   ? 31.046  -79.119  22.309  1.000 51.441  0 2   VAL DDD O   1 ? 12 
ATOM   4137  C CB  . VAL D  2 2   ? 31.222  -80.978  19.891  1.000 52.524  0 2   VAL DDD CB  1 ? 12 
ATOM   4138  C CG1 . VAL D  2 2   ? 32.704  -81.286  19.979  1.000 50.109  0 2   VAL DDD CG1 1 ? 12 
ATOM   4139  C CG2 . VAL D  2 2   ? 30.572  -81.796  18.795  1.000 54.945  0 2   VAL DDD CG2 1 ? 12 
ATOM   4140  N N   . GLN D  2 3   ? 31.933  -80.950  23.215  1.000 47.709  0 3   GLN DDD N   1 ? 12 
ATOM   4141  C CA  . GLN D  2 3   ? 32.809  -80.228  24.160  1.000 45.968  0 3   GLN DDD CA  1 ? 12 
ATOM   4142  C C   . GLN D  2 3   ? 34.247  -80.298  23.635  1.000 44.503  0 3   GLN DDD C   1 ? 12 
ATOM   4143  O O   . GLN D  2 3   ? 34.627  -81.280  22.950  1.000 45.585  0 3   GLN DDD O   1 ? 12 
ATOM   4144  C CB  . GLN D  2 3   ? 32.618  -80.790  25.565  1.000 45.062  0 3   GLN DDD CB  1 ? 12 
ATOM   4145  C CG  . GLN D  2 3   ? 31.336  -80.272  26.191  1.000 47.327  0 3   GLN DDD CG  1 ? 12 
ATOM   4146  C CD  . GLN D  2 3   ? 31.240  -80.643  27.646  1.000 47.491  0 3   GLN DDD CD  1 ? 12 
ATOM   4147  O OE1 . GLN D  2 3   ? 32.078  -80.259  28.461  1.000 46.161  0 3   GLN DDD OE1 1 ? 12 
ATOM   4148  N NE2 . GLN D  2 3   ? 30.212  -81.406  27.968  1.000 49.004  0 3   GLN DDD NE2 1 ? 12 
ATOM   4149  N N   . LEU D  2 4   ? 35.004  -79.251  23.933  1.000 42.850  0 4   LEU DDD N   1 ? 12 
ATOM   4150  C CA  . LEU D  2 4   ? 36.392  -79.044  23.481  1.000 42.648  0 4   LEU DDD CA  1 ? 12 
ATOM   4151  C C   . LEU D  2 4   ? 37.223  -78.616  24.700  1.000 42.297  0 4   LEU DDD C   1 ? 12 
ATOM   4152  O O   . LEU D  2 4   ? 36.805  -77.685  25.422  1.000 42.122  0 4   LEU DDD O   1 ? 12 
ATOM   4153  C CB  . LEU D  2 4   ? 36.384  -77.951  22.408  1.000 44.153  0 4   LEU DDD CB  1 ? 12 
ATOM   4154  C CG  . LEU D  2 4   ? 35.520  -78.180  21.169  1.000 46.011  0 4   LEU DDD CG  1 ? 12 
ATOM   4155  C CD1 . LEU D  2 4   ? 35.419  -76.910  20.335  1.000 47.035  0 4   LEU DDD CD1 1 ? 12 
ATOM   4156  C CD2 . LEU D  2 4   ? 36.052  -79.337  20.337  1.000 46.239  0 4   LEU DDD CD2 1 ? 12 
ATOM   4157  N N   . VAL D  2 5   ? 38.359  -79.263  24.916  1.000 42.883  0 5   VAL DDD N   1 ? 12 
ATOM   4158  C CA  . VAL D  2 5   ? 39.306  -78.883  25.996  1.000 43.696  0 5   VAL DDD CA  1 ? 12 
ATOM   4159  C C   . VAL D  2 5   ? 40.705  -78.697  25.402  1.000 44.325  0 5   VAL DDD C   1 ? 12 
ATOM   4160  O O   . VAL D  2 5   ? 41.264  -79.672  24.853  1.000 45.996  0 5   VAL DDD O   1 ? 12 
ATOM   4161  C CB  . VAL D  2 5   ? 39.270  -79.917  27.135  1.000 45.079  0 5   VAL DDD CB  1 ? 12 
ATOM   4162  C CG1 . VAL D  2 5   ? 40.388  -79.676  28.147  1.000 45.505  0 5   VAL DDD CG1 1 ? 12 
ATOM   4163  C CG2 . VAL D  2 5   ? 37.906  -79.919  27.817  1.000 44.663  0 5   VAL DDD CG2 1 ? 12 
ATOM   4164  N N   . GLU D  2 6   ? 41.223  -77.472  25.522  1.000 44.470  0 6   GLU DDD N   1 ? 12 
ATOM   4165  C CA  . GLU D  2 6   ? 42.613  -77.094  25.169  1.000 45.121  0 6   GLU DDD CA  1 ? 12 
ATOM   4166  C C   . GLU D  2 6   ? 43.563  -77.540  26.286  1.000 46.686  0 6   GLU DDD C   1 ? 12 
ATOM   4167  O O   . GLU D  2 6   ? 43.161  -77.538  27.443  1.000 48.342  0 6   GLU DDD O   1 ? 12 
ATOM   4168  C CB  . GLU D  2 6   ? 42.734  -75.584  24.975  1.000 46.179  0 6   GLU DDD CB  1 ? 12 
ATOM   4169  C CG  . GLU D  2 6   ? 41.711  -74.985  24.018  1.000 45.349  0 6   GLU DDD CG  1 ? 12 
ATOM   4170  C CD  . GLU D  2 6   ? 40.398  -74.510  24.622  1.000 45.288  0 6   GLU DDD CD  1 ? 12 
ATOM   4171  O OE1 . GLU D  2 6   ? 40.074  -74.936  25.723  1.000 46.527  0 6   GLU DDD OE1 1 ? 12 
ATOM   4172  O OE2 . GLU D  2 6   ? 39.694  -73.733  23.964  1.000 47.747  0 6   GLU DDD OE2 1 ? 12 
ATOM   4173  N N   . SER D  2 7   ? 44.791  -77.903  25.926  1.000 48.912  0 7   SER DDD N   1 ? 12 
ATOM   4174  C CA  . SER D  2 7   ? 45.943  -78.126  26.839  1.000 50.219  0 7   SER DDD CA  1 ? 12 
ATOM   4175  C C   . SER D  2 7   ? 47.244  -77.727  26.128  1.000 53.138  0 7   SER DDD C   1 ? 12 
ATOM   4176  O O   . SER D  2 7   ? 47.188  -77.430  24.914  1.000 50.558  0 7   SER DDD O   1 ? 12 
ATOM   4177  C CB  . SER D  2 7   ? 45.984  -79.537  27.305  1.000 49.669  0 7   SER DDD CB  1 ? 12 
ATOM   4178  O OG  . SER D  2 7   ? 46.120  -80.390  26.194  1.000 49.736  0 7   SER DDD OG  1 ? 12 
ATOM   4179  N N   . GLY D  2 8   ? 48.360  -77.662  26.866  1.000 55.910  0 8   GLY DDD N   1 ? 12 
ATOM   4180  C CA  . GLY D  2 8   ? 49.698  -77.388  26.307  1.000 58.777  0 8   GLY DDD CA  1 ? 12 
ATOM   4181  C C   . GLY D  2 8   ? 50.062  -75.911  26.342  1.000 60.492  0 8   GLY DDD C   1 ? 12 
ATOM   4182  O O   . GLY D  2 8   ? 51.138  -75.553  25.815  1.000 64.763  0 8   GLY DDD O   1 ? 12 
ATOM   4183  N N   . GLY D  2 9   ? 49.218  -75.074  26.955  1.000 58.713  0 9   GLY DDD N   1 ? 12 
ATOM   4184  C CA  . GLY D  2 9   ? 49.460  -73.624  27.087  1.000 59.771  0 9   GLY DDD CA  1 ? 12 
ATOM   4185  C C   . GLY D  2 9   ? 50.500  -73.333  28.154  1.000 60.999  0 9   GLY DDD C   1 ? 12 
ATOM   4186  O O   . GLY D  2 9   ? 51.043  -74.300  28.716  1.000 64.424  0 9   GLY DDD O   1 ? 12 
ATOM   4187  N N   . GLY D  2 10  ? 50.763  -72.063  28.444  1.000 60.766  0 10  GLY DDD N   1 ? 12 
ATOM   4188  C CA  . GLY D  2 10  ? 51.603  -71.666  29.591  1.000 62.519  0 10  GLY DDD CA  1 ? 12 
ATOM   4189  C C   . GLY D  2 10  ? 52.637  -70.633  29.213  1.000 64.654  0 10  GLY DDD C   1 ? 12 
ATOM   4190  O O   . GLY D  2 10  ? 52.484  -69.981  28.177  1.000 60.098  0 10  GLY DDD O   1 ? 12 
ATOM   4191  N N   . LEU D  2 11  ? 53.658  -70.509  30.057  1.000 69.432  0 11  LEU DDD N   1 ? 12 
ATOM   4192  C CA  . LEU D  2 11  ? 54.747  -69.509  29.957  1.000 73.800  0 11  LEU DDD CA  1 ? 12 
ATOM   4193  C C   . LEU D  2 11  ? 55.820  -70.041  29.004  1.000 76.402  0 11  LEU DDD C   1 ? 12 
ATOM   4194  O O   . LEU D  2 11  ? 56.107  -71.240  29.064  1.000 77.715  0 11  LEU DDD O   1 ? 12 
ATOM   4195  C CB  . LEU D  2 11  ? 55.289  -69.311  31.379  1.000 76.962  0 11  LEU DDD CB  1 ? 12 
ATOM   4196  C CG  . LEU D  2 11  ? 56.398  -68.280  31.550  1.000 81.183  0 11  LEU DDD CG  1 ? 12 
ATOM   4197  C CD1 . LEU D  2 11  ? 56.018  -66.951  30.888  1.000 80.413  0 11  LEU DDD CD1 1 ? 12 
ATOM   4198  C CD2 . LEU D  2 11  ? 56.713  -68.093  33.037  1.000 84.713  0 11  LEU DDD CD2 1 ? 12 
ATOM   4199  N N   . VAL D  2 12  ? 56.381  -69.198  28.144  1.000 79.193  0 12  VAL DDD N   1 ? 12 
ATOM   4200  C CA  . VAL D  2 12  ? 57.527  -69.590  27.265  1.000 81.159  0 12  VAL DDD CA  1 ? 12 
ATOM   4201  C C   . VAL D  2 12  ? 58.314  -68.320  26.925  1.000 82.317  0 12  VAL DDD C   1 ? 12 
ATOM   4202  O O   . VAL D  2 12  ? 57.682  -67.235  26.855  1.000 78.155  0 12  VAL DDD O   1 ? 12 
ATOM   4203  C CB  . VAL D  2 12  ? 57.024  -70.337  26.012  1.000 78.786  0 12  VAL DDD CB  1 ? 12 
ATOM   4204  C CG1 . VAL D  2 12  ? 56.286  -69.417  25.051  1.000 75.573  0 12  VAL DDD CG1 1 ? 12 
ATOM   4205  C CG2 . VAL D  2 12  ? 58.145  -71.094  25.332  1.000 82.182  0 12  VAL DDD CG2 1 ? 12 
ATOM   4206  N N   . GLN D  2 13  ? 59.637  -68.438  26.756  1.000 86.509  0 13  GLN DDD N   1 ? 12 
ATOM   4207  C CA  . GLN D  2 13  ? 60.521  -67.300  26.373  1.000 88.571  0 13  GLN DDD CA  1 ? 12 
ATOM   4208  C C   . GLN D  2 13  ? 60.380  -67.045  24.868  1.000 84.449  0 13  GLN DDD C   1 ? 12 
ATOM   4209  O O   . GLN D  2 13  ? 60.177  -68.023  24.116  1.000 82.981  0 13  GLN DDD O   1 ? 12 
ATOM   4210  C CB  . GLN D  2 13  ? 61.967  -67.558  26.791  1.000 95.768  0 13  GLN DDD CB  1 ? 12 
ATOM   4211  C CG  . GLN D  2 13  ? 62.141  -67.596  28.301  1.000 101.334 0 13  GLN DDD CG  1 ? 12 
ATOM   4212  C CD  . GLN D  2 13  ? 62.508  -66.271  28.921  1.000 105.005 0 13  GLN DDD CD  1 ? 12 
ATOM   4213  O OE1 . GLN D  2 13  ? 61.748  -65.301  28.893  1.000 105.524 0 13  GLN DDD OE1 1 ? 12 
ATOM   4214  N NE2 . GLN D  2 13  ? 63.683  -66.240  29.523  1.000 111.471 0 13  GLN DDD NE2 1 ? 12 
ATOM   4215  N N   . ALA D  2 14  ? 60.422  -65.769  24.463  1.000 82.361  0 14  ALA DDD N   1 ? 12 
ATOM   4216  C CA  . ALA D  2 14  ? 60.437  -65.304  23.056  1.000 80.468  0 14  ALA DDD CA  1 ? 12 
ATOM   4217  C C   . ALA D  2 14  ? 61.424  -66.155  22.261  1.000 83.932  0 14  ALA DDD C   1 ? 12 
ATOM   4218  O O   . ALA D  2 14  ? 62.479  -66.502  22.815  1.000 87.843  0 14  ALA DDD O   1 ? 12 
ATOM   4219  C CB  . ALA D  2 14  ? 60.789  -63.841  22.993  1.000 81.450  0 14  ALA DDD CB  1 ? 12 
ATOM   4220  N N   . GLY D  2 15  ? 61.069  -66.518  21.024  1.000 82.545  0 15  GLY DDD N   1 ? 12 
ATOM   4221  C CA  . GLY D  2 15  ? 61.851  -67.452  20.193  1.000 84.499  0 15  GLY DDD CA  1 ? 12 
ATOM   4222  C C   . GLY D  2 15  ? 61.595  -68.907  20.550  1.000 83.626  0 15  GLY DDD C   1 ? 12 
ATOM   4223  O O   . GLY D  2 15  ? 62.043  -69.758  19.796  1.000 86.763  0 15  GLY DDD O   1 ? 12 
ATOM   4224  N N   . GLY D  2 16  ? 60.901  -69.202  21.652  1.000 81.938  0 16  GLY DDD N   1 ? 12 
ATOM   4225  C CA  . GLY D  2 16  ? 60.601  -70.581  22.084  1.000 81.850  0 16  GLY DDD CA  1 ? 12 
ATOM   4226  C C   . GLY D  2 16  ? 59.429  -71.171  21.310  1.000 80.375  0 16  GLY DDD C   1 ? 12 
ATOM   4227  O O   . GLY D  2 16  ? 58.902  -70.500  20.384  1.000 77.267  0 16  GLY DDD O   1 ? 12 
ATOM   4228  N N   . SER D  2 17  ? 59.034  -72.393  21.684  1.000 81.998  0 17  SER DDD N   1 ? 12 
ATOM   4229  C CA  . SER D  2 17  ? 57.963  -73.209  21.057  1.000 78.834  0 17  SER DDD CA  1 ? 12 
ATOM   4230  C C   . SER D  2 17  ? 56.963  -73.712  22.094  1.000 76.578  0 17  SER DDD C   1 ? 12 
ATOM   4231  O O   . SER D  2 17  ? 57.327  -73.866  23.272  1.000 76.921  0 17  SER DDD O   1 ? 12 
ATOM   4232  C CB  . SER D  2 17  ? 58.527  -74.382  20.325  1.000 81.848  0 17  SER DDD CB  1 ? 12 
ATOM   4233  O OG  . SER D  2 17  ? 59.182  -73.944  19.156  1.000 85.818  0 17  SER DDD OG  1 ? 12 
ATOM   4234  N N   . LEU D  2 18  ? 55.747  -73.974  21.619  1.000 74.661  0 18  LEU DDD N   1 ? 12 
ATOM   4235  C CA  . LEU D  2 18  ? 54.629  -74.600  22.360  1.000 71.743  0 18  LEU DDD CA  1 ? 12 
ATOM   4236  C C   . LEU D  2 18  ? 53.786  -75.378  21.360  1.000 68.928  0 18  LEU DDD C   1 ? 12 
ATOM   4237  O O   . LEU D  2 18  ? 53.560  -74.852  20.263  1.000 67.918  0 18  LEU DDD O   1 ? 12 
ATOM   4238  C CB  . LEU D  2 18  ? 53.757  -73.505  22.970  1.000 70.633  0 18  LEU DDD CB  1 ? 12 
ATOM   4239  C CG  . LEU D  2 18  ? 54.070  -73.074  24.396  1.000 72.697  0 18  LEU DDD CG  1 ? 12 
ATOM   4240  C CD1 . LEU D  2 18  ? 52.913  -72.229  24.898  1.000 71.875  0 18  LEU DDD CD1 1 ? 12 
ATOM   4241  C CD2 . LEU D  2 18  ? 54.295  -74.270  25.308  1.000 74.275  0 18  LEU DDD CD2 1 ? 12 
ATOM   4242  N N   . ARG D  2 19  ? 53.324  -76.558  21.740  1.000 68.288  0 19  ARG DDD N   1 ? 12 
ATOM   4243  C CA  . ARG D  2 19  ? 52.275  -77.288  21.000  1.000 66.680  0 19  ARG DDD CA  1 ? 12 
ATOM   4244  C C   . ARG D  2 19  ? 50.995  -77.294  21.846  1.000 62.882  0 19  ARG DDD C   1 ? 12 
ATOM   4245  O O   . ARG D  2 19  ? 50.918  -78.053  22.836  1.000 60.054  0 19  ARG DDD O   1 ? 12 
ATOM   4246  C CB  . ARG D  2 19  ? 52.727  -78.694  20.614  1.000 70.352  0 19  ARG DDD CB  1 ? 12 
ATOM   4247  C CG  . ARG D  2 19  ? 51.904  -79.239  19.460  1.000 72.548  0 19  ARG DDD CG  1 ? 12 
ATOM   4248  C CD  . ARG D  2 19  ? 52.259  -80.640  19.071  1.000 78.335  0 19  ARG DDD CD  1 ? 12 
ATOM   4249  N NE  . ARG D  2 19  ? 51.961  -81.523  20.179  1.000 79.674  0 19  ARG DDD NE  1 ? 12 
ATOM   4250  C CZ  . ARG D  2 19  ? 51.765  -82.830  20.067  1.000 83.532  0 19  ARG DDD CZ  1 ? 12 
ATOM   4251  N NH1 . ARG D  2 19  ? 51.810  -83.422  18.875  1.000 83.959  0 19  ARG DDD NH1 1 ? 12 
ATOM   4252  N NH2 . ARG D  2 19  ? 51.511  -83.534  21.163  1.000 83.891  0 19  ARG DDD NH2 1 ? 12 
ATOM   4253  N N   . LEU D  2 20  ? 50.034  -76.456  21.453  1.000 62.131  0 20  LEU DDD N   1 ? 12 
ATOM   4254  C CA  . LEU D  2 20  ? 48.643  -76.506  21.950  1.000 59.877  0 20  LEU DDD CA  1 ? 12 
ATOM   4255  C C   . LEU D  2 20  ? 47.980  -77.750  21.360  1.000 60.470  0 20  LEU DDD C   1 ? 12 
ATOM   4256  O O   . LEU D  2 20  ? 48.242  -78.093  20.187  1.000 62.859  0 20  LEU DDD O   1 ? 12 
ATOM   4257  C CB  . LEU D  2 20  ? 47.877  -75.240  21.547  1.000 58.527  0 20  LEU DDD CB  1 ? 12 
ATOM   4258  C CG  . LEU D  2 20  ? 48.436  -73.927  22.076  1.000 59.628  0 20  LEU DDD CG  1 ? 12 
ATOM   4259  C CD1 . LEU D  2 20  ? 47.468  -72.785  21.806  1.000 61.044  0 20  LEU DDD CD1 1 ? 12 
ATOM   4260  C CD2 . LEU D  2 20  ? 48.720  -74.014  23.560  1.000 60.654  0 20  LEU DDD CD2 1 ? 12 
ATOM   4261  N N   . ALA D  2 21  ? 47.158  -78.412  22.163  1.000 57.553  0 21  ALA DDD N   1 ? 12 
ATOM   4262  C CA  . ALA D  2 21  ? 46.266  -79.489  21.705  1.000 54.827  0 21  ALA DDD CA  1 ? 12 
ATOM   4263  C C   . ALA D  2 21  ? 44.845  -79.192  22.161  1.000 52.369  0 21  ALA DDD C   1 ? 12 
ATOM   4264  O O   . ALA D  2 21  ? 44.653  -78.512  23.170  1.000 53.306  0 21  ALA DDD O   1 ? 12 
ATOM   4265  C CB  . ALA D  2 21  ? 46.740  -80.813  22.230  1.000 53.661  0 21  ALA DDD CB  1 ? 12 
ATOM   4266  N N   . CYS D  2 22  ? 43.885  -79.701  21.414  1.000 51.116  0 22  CYS DDD N   1 ? 12 
ATOM   4267  C CA  . CYS D  2 22  ? 42.467  -79.592  21.767  1.000 48.712  0 22  CYS DDD CA  1 ? 12 
ATOM   4268  C C   . CYS D  2 22  ? 41.780  -80.894  21.402  1.000 48.228  0 22  CYS DDD C   1 ? 12 
ATOM   4269  O O   . CYS D  2 22  ? 41.858  -81.304  20.226  1.000 46.098  0 22  CYS DDD O   1 ? 12 
ATOM   4270  C CB  . CYS D  2 22  ? 41.841  -78.432  21.029  1.000 52.028  0 22  CYS DDD CB  1 ? 12 
ATOM   4271  S SG  . CYS D  2 22  ? 40.051  -78.447  21.180  1.000 54.303  0 22  CYS DDD SG  1 ? 12 
ATOM   4272  N N   . ILE D  2 23  ? 41.140  -81.504  22.396  1.000 46.615  0 23  ILE DDD N   1 ? 12 
ATOM   4273  C CA  . ILE D  2 23  ? 40.446  -82.805  22.242  1.000 47.063  0 23  ILE DDD CA  1 ? 12 
ATOM   4274  C C   . ILE D  2 23  ? 38.934  -82.542  22.279  1.000 48.957  0 23  ILE DDD C   1 ? 12 
ATOM   4275  O O   . ILE D  2 23  ? 38.489  -81.710  23.081  1.000 51.742  0 23  ILE DDD O   1 ? 12 
ATOM   4276  C CB  . ILE D  2 23  ? 40.950  -83.805  23.292  1.000 44.439  0 23  ILE DDD CB  1 ? 12 
ATOM   4277  C CG1 . ILE D  2 23  ? 40.427  -85.218  23.004  1.000 45.362  0 23  ILE DDD CG1 1 ? 12 
ATOM   4278  C CG2 . ILE D  2 23  ? 40.621  -83.348  24.701  1.000 43.545  0 23  ILE DDD CG2 1 ? 12 
ATOM   4279  C CD1 . ILE D  2 23  ? 40.995  -86.296  23.913  1.000 44.909  0 23  ILE DDD CD1 1 ? 12 
ATOM   4280  N N   . ALA D  2 24  ? 38.198  -83.193  21.383  1.000 46.897  0 24  ALA DDD N   1 ? 13 
ATOM   4281  C CA  . ALA D  2 24  ? 36.735  -83.066  21.210  1.000 46.892  0 24  ALA DDD CA  1 ? 13 
ATOM   4282  C C   . ALA D  2 24  ? 36.062  -84.331  21.729  1.000 46.821  0 24  ALA DDD C   1 ? 13 
ATOM   4283  O O   . ALA D  2 24  ? 36.666  -85.404  21.666  1.000 48.303  0 24  ALA DDD O   1 ? 13 
ATOM   4284  C CB  . ALA D  2 24  ? 36.391  -82.813  19.754  1.000 45.562  0 24  ALA DDD CB  1 ? 13 
ATOM   4285  N N   . SER D  2 25  ? 34.863  -84.178  22.285  1.000 46.899  0 25  SER DDD N   1 ? 13 
ATOM   4286  C CA  . SER D  2 25  ? 33.916  -85.290  22.545  1.000 47.733  0 25  SER DDD CA  1 ? 13 
ATOM   4287  C C   . SER D  2 25  ? 33.389  -85.802  21.197  1.000 46.913  0 25  SER DDD C   1 ? 13 
ATOM   4288  O O   . SER D  2 25  ? 33.698  -85.214  20.176  1.000 43.465  0 25  SER DDD O   1 ? 13 
ATOM   4289  C CB  . SER D  2 25  ? 32.814  -84.827  23.446  1.000 47.837  0 25  SER DDD CB  1 ? 13 
ATOM   4290  O OG  . SER D  2 25  ? 32.017  -83.879  22.778  1.000 46.255  0 25  SER DDD OG  1 ? 13 
ATOM   4291  N N   . GLY D  2 26  ? 32.598  -86.864  21.214  1.000 49.241  0 26  GLY DDD N   1 ? 13 
ATOM   4292  C CA  . GLY D  2 26  ? 31.848  -87.315  20.039  1.000 51.015  0 26  GLY DDD CA  1 ? 13 
ATOM   4293  C C   . GLY D  2 26  ? 32.576  -88.400  19.275  1.000 53.894  0 26  GLY DDD C   1 ? 13 
ATOM   4294  O O   . GLY D  2 26  ? 33.793  -88.594  19.465  1.000 52.906  0 26  GLY DDD O   1 ? 13 
ATOM   4295  N N   . ARG D  2 27  ? 31.838  -89.081  18.400  1.000 60.397  0 27  ARG DDD N   1 ? 13 
ATOM   4296  C CA  . ARG D  2 27  ? 32.372  -90.209  17.610  1.000 64.666  0 27  ARG DDD CA  1 ? 13 
ATOM   4297  C C   . ARG D  2 27  ? 32.462  -89.827  16.132  1.000 59.596  0 27  ARG DDD C   1 ? 13 
ATOM   4298  O O   . ARG D  2 27  ? 32.735  -90.710  15.356  1.000 60.413  0 27  ARG DDD O   1 ? 13 
ATOM   4299  C CB  . ARG D  2 27  ? 31.484  -91.426  17.859  1.000 74.494  0 27  ARG DDD CB  1 ? 13 
ATOM   4300  C CG  . ARG D  2 27  ? 31.922  -92.278  19.046  1.000 86.678  0 27  ARG DDD CG  1 ? 13 
ATOM   4301  C CD  . ARG D  2 27  ? 31.179  -93.618  19.071  1.000 100.619 0 27  ARG DDD CD  1 ? 13 
ATOM   4302  N NE  . ARG D  2 27  ? 29.832  -93.518  18.486  1.000 111.083 0 27  ARG DDD NE  1 ? 13 
ATOM   4303  C CZ  . ARG D  2 27  ? 28.665  -93.548  19.141  1.000 117.616 0 27  ARG DDD CZ  1 ? 13 
ATOM   4304  N NH1 . ARG D  2 27  ? 28.607  -93.732  20.452  1.000 118.871 0 27  ARG DDD NH1 1 ? 13 
ATOM   4305  N NH2 . ARG D  2 27  ? 27.538  -93.429  18.454  1.000 121.175 0 27  ARG DDD NH2 1 ? 13 
ATOM   4306  N N   . THR D  2 28  ? 32.282  -88.558  15.764  1.000 55.828  0 28  THR DDD N   1 ? 13 
ATOM   4307  C CA  . THR D  2 28  ? 32.351  -88.119  14.341  1.000 55.424  0 28  THR DDD CA  1 ? 13 
ATOM   4308  C C   . THR D  2 28  ? 33.281  -86.912  14.244  1.000 50.637  0 28  THR DDD C   1 ? 13 
ATOM   4309  O O   . THR D  2 28  ? 32.964  -85.986  13.494  1.000 50.032  0 28  THR DDD O   1 ? 13 
ATOM   4310  C CB  . THR D  2 28  ? 30.962  -87.833  13.748  1.000 55.443  0 28  THR DDD CB  1 ? 13 
ATOM   4311  O OG1 . THR D  2 28  ? 30.293  -86.906  14.603  1.000 57.743  0 28  THR DDD OG1 1 ? 13 
ATOM   4312  C CG2 . THR D  2 28  ? 30.126  -89.077  13.587  1.000 57.081  0 28  THR DDD CG2 1 ? 13 
ATOM   4313  N N   . PHE D  2 29  ? 34.403  -86.948  14.939  1.000 47.202  0 29  PHE DDD N   1 ? 13 
ATOM   4314  C CA  . PHE D  2 29  ? 35.447  -85.890  14.888  1.000 47.247  0 29  PHE DDD CA  1 ? 13 
ATOM   4315  C C   . PHE D  2 29  ? 35.847  -85.607  13.432  1.000 47.874  0 29  PHE DDD C   1 ? 13 
ATOM   4316  O O   . PHE D  2 29  ? 36.046  -84.437  13.094  1.000 46.770  0 29  PHE DDD O   1 ? 13 
ATOM   4317  C CB  . PHE D  2 29  ? 36.672  -86.295  15.703  1.000 47.352  0 29  PHE DDD CB  1 ? 13 
ATOM   4318  C CG  . PHE D  2 29  ? 37.743  -85.246  15.746  1.000 45.698  0 29  PHE DDD CG  1 ? 13 
ATOM   4319  C CD1 . PHE D  2 29  ? 37.614  -84.132  16.558  1.000 45.435  0 29  PHE DDD CD1 1 ? 13 
ATOM   4320  C CD2 . PHE D  2 29  ? 38.883  -85.383  14.985  1.000 47.171  0 29  PHE DDD CD2 1 ? 13 
ATOM   4321  C CE1 . PHE D  2 29  ? 38.614  -83.174  16.611  1.000 45.684  0 29  PHE DDD CE1 1 ? 13 
ATOM   4322  C CE2 . PHE D  2 29  ? 39.894  -84.430  15.047  1.000 46.434  0 29  PHE DDD CE2 1 ? 13 
ATOM   4323  C CZ  . PHE D  2 29  ? 39.755  -83.322  15.854  1.000 45.894  0 29  PHE DDD CZ  1 ? 13 
ATOM   4324  N N   . HIS D  2 30  ? 35.941  -86.640  12.590  1.000 48.702  0 30  HIS DDD N   1 ? 13 
ATOM   4325  C CA  . HIS D  2 30  ? 36.310  -86.542  11.147  1.000 48.760  0 30  HIS DDD CA  1 ? 13 
ATOM   4326  C C   . HIS D  2 30  ? 35.288  -85.671  10.385  1.000 47.072  0 30  HIS DDD C   1 ? 13 
ATOM   4327  O O   . HIS D  2 30  ? 35.628  -85.191  9.307   1.000 45.038  0 30  HIS DDD O   1 ? 13 
ATOM   4328  C CB  . HIS D  2 30  ? 36.454  -87.948  10.548  1.000 50.545  0 30  HIS DDD CB  1 ? 13 
ATOM   4329  C CG  . HIS D  2 30  ? 35.146  -88.635  10.437  1.000 52.773  0 30  HIS DDD CG  1 ? 13 
ATOM   4330  N ND1 . HIS D  2 30  ? 34.524  -89.279  11.509  1.000 54.435  0 30  HIS DDD ND1 1 ? 13 
ATOM   4331  C CD2 . HIS D  2 30  ? 34.300  -88.691  9.399   1.000 54.018  0 30  HIS DDD CD2 1 ? 13 
ATOM   4332  C CE1 . HIS D  2 30  ? 33.361  -89.748  11.108  1.000 55.839  0 30  HIS DDD CE1 1 ? 13 
ATOM   4333  N NE2 . HIS D  2 30  ? 33.217  -89.429  9.792   1.000 56.101  0 30  HIS DDD NE2 1 ? 13 
ATOM   4334  N N   . SER D  2 31  ? 34.093  -85.454  10.918  1.000 46.621  0 31  SER DDD N   1 ? 13 
ATOM   4335  C CA  . SER D  2 31  ? 33.042  -84.596  10.291  1.000 46.714  0 31  SER DDD CA  1 ? 13 
ATOM   4336  C C   . SER D  2 31  ? 33.264  -83.115  10.621  1.000 44.101  0 31  SER DDD C   1 ? 13 
ATOM   4337  O O   . SER D  2 31  ? 32.476  -82.309  10.105  1.000 43.877  0 31  SER DDD O   1 ? 13 
ATOM   4338  C CB  . SER D  2 31  ? 31.640  -84.984  10.711  1.000 48.137  0 31  SER DDD CB  1 ? 13 
ATOM   4339  O OG  . SER D  2 31  ? 31.367  -86.342  10.435  1.000 54.812  0 31  SER DDD OG  1 ? 13 
ATOM   4340  N N   . TYR D  2 32  ? 34.242  -82.765  11.469  1.000 41.540  0 32  TYR DDD N   1 ? 13 
ATOM   4341  C CA  . TYR D  2 32  ? 34.396  -81.372  11.980  1.000 40.335  0 32  TYR DDD CA  1 ? 13 
ATOM   4342  C C   . TYR D  2 32  ? 35.595  -80.699  11.327  1.000 40.081  0 32  TYR DDD C   1 ? 13 
ATOM   4343  O O   . TYR D  2 32  ? 36.677  -81.280  11.279  1.000 42.770  0 32  TYR DDD O   1 ? 13 
ATOM   4344  C CB  . TYR D  2 32  ? 34.469  -81.324  13.509  1.000 39.219  0 32  TYR DDD CB  1 ? 13 
ATOM   4345  C CG  . TYR D  2 32  ? 33.122  -81.559  14.125  1.000 40.253  0 32  TYR DDD CG  1 ? 13 
ATOM   4346  C CD1 . TYR D  2 32  ? 32.661  -82.842  14.367  1.000 41.564  0 32  TYR DDD CD1 1 ? 13 
ATOM   4347  C CD2 . TYR D  2 32  ? 32.263  -80.506  14.362  1.000 41.869  0 32  TYR DDD CD2 1 ? 13 
ATOM   4348  C CE1 . TYR D  2 32  ? 31.399  -83.081  14.890  1.000 42.297  0 32  TYR DDD CE1 1 ? 13 
ATOM   4349  C CE2 . TYR D  2 32  ? 30.991  -80.732  14.870  1.000 44.785  0 32  TYR DDD CE2 1 ? 13 
ATOM   4350  C CZ  . TYR D  2 32  ? 30.554  -82.021  15.145  1.000 43.810  0 32  TYR DDD CZ  1 ? 13 
ATOM   4351  O OH  . TYR D  2 32  ? 29.287  -82.228  15.632  1.000 44.771  0 32  TYR DDD OH  1 ? 13 
ATOM   4352  N N   . VAL D  2 33  ? 35.366  -79.493  10.818  1.000 40.384  0 33  VAL DDD N   1 ? 13 
ATOM   4353  C CA  . VAL D  2 33  ? 36.432  -78.480  10.589  1.000 41.716  0 33  VAL DDD CA  1 ? 13 
ATOM   4354  C C   . VAL D  2 33  ? 36.876  -77.981  11.967  1.000 42.527  0 33  VAL DDD C   1 ? 13 
ATOM   4355  O O   . VAL D  2 33  ? 35.999  -77.591  12.766  1.000 43.568  0 33  VAL DDD O   1 ? 13 
ATOM   4356  C CB  . VAL D  2 33  ? 35.919  -77.336  9.706   1.000 41.800  0 33  VAL DDD CB  1 ? 13 
ATOM   4357  C CG1 . VAL D  2 33  ? 36.946  -76.223  9.568   1.000 41.923  0 33  VAL DDD CG1 1 ? 13 
ATOM   4358  C CG2 . VAL D  2 33  ? 35.483  -77.871  8.352   1.000 44.607  0 33  VAL DDD CG2 1 ? 13 
ATOM   4359  N N   . MET D  2 34  ? 38.172  -78.025  12.253  1.000 44.481  0 34  MET DDD N   1 ? 13 
ATOM   4360  C CA  . MET D  2 34  ? 38.728  -77.579  13.560  1.000 44.916  0 34  MET DDD CA  1 ? 13 
ATOM   4361  C C   . MET D  2 34  ? 39.516  -76.274  13.356  1.000 44.416  0 34  MET DDD C   1 ? 13 
ATOM   4362  O O   . MET D  2 34  ? 40.170  -76.108  12.307  1.000 42.321  0 34  MET DDD O   1 ? 13 
ATOM   4363  C CB  . MET D  2 34  ? 39.627  -78.660  14.166  1.000 46.341  0 34  MET DDD CB  1 ? 13 
ATOM   4364  C CG  . MET D  2 34  ? 38.907  -79.978  14.408  1.000 46.965  0 34  MET DDD CG  1 ? 13 
ATOM   4365  S SD  . MET D  2 34  ? 37.450  -79.795  15.475  1.000 46.582  0 34  MET DDD SD  1 ? 13 
ATOM   4366  C CE  . MET D  2 34  ? 38.257  -79.318  16.999  1.000 49.590  0 34  MET DDD CE  1 ? 13 
ATOM   4367  N N   . ALA D  2 35  ? 39.434  -75.367  14.325  1.000 44.643  0 35  ALA DDD N   1 ? 13 
ATOM   4368  C CA  . ALA D  2 35  ? 40.076  -74.049  14.245  1.000 45.951  0 35  ALA DDD CA  1 ? 13 
ATOM   4369  C C   . ALA D  2 35  ? 40.647  -73.622  15.604  1.000 46.696  0 35  ALA DDD C   1 ? 13 
ATOM   4370  O O   . ALA D  2 35  ? 40.199  -74.120  16.665  1.000 46.853  0 35  ALA DDD O   1 ? 13 
ATOM   4371  C CB  . ALA D  2 35  ? 39.091  -73.054  13.709  1.000 46.247  0 35  ALA DDD CB  1 ? 13 
ATOM   4372  N N   . TRP D  2 36  ? 41.606  -72.703  15.523  1.000 46.866  0 36  TRP DDD N   1 ? 13 
ATOM   4373  C CA  . TRP D  2 36  ? 42.198  -71.948  16.645  1.000 46.718  0 36  TRP DDD CA  1 ? 13 
ATOM   4374  C C   . TRP D  2 36  ? 41.942  -70.456  16.419  1.000 47.760  0 36  TRP DDD C   1 ? 13 
ATOM   4375  O O   . TRP D  2 36  ? 42.169  -69.965  15.301  1.000 46.612  0 36  TRP DDD O   1 ? 13 
ATOM   4376  C CB  . TRP D  2 36  ? 43.692  -72.244  16.745  1.000 46.966  0 36  TRP DDD CB  1 ? 13 
ATOM   4377  C CG  . TRP D  2 36  ? 43.990  -73.632  17.211  1.000 46.378  0 36  TRP DDD CG  1 ? 13 
ATOM   4378  C CD1 . TRP D  2 36  ? 44.303  -74.703  16.435  1.000 47.622  0 36  TRP DDD CD1 1 ? 13 
ATOM   4379  C CD2 . TRP D  2 36  ? 43.977  -74.106  18.563  1.000 45.082  0 36  TRP DDD CD2 1 ? 13 
ATOM   4380  N NE1 . TRP D  2 36  ? 44.505  -75.809  17.214  1.000 46.949  0 36  TRP DDD NE1 1 ? 13 
ATOM   4381  C CE2 . TRP D  2 36  ? 44.318  -75.469  18.522  1.000 46.063  0 36  TRP DDD CE2 1 ? 13 
ATOM   4382  C CE3 . TRP D  2 36  ? 43.772  -73.498  19.801  1.000 46.433  0 36  TRP DDD CE3 1 ? 13 
ATOM   4383  C CZ2 . TRP D  2 36  ? 44.445  -76.239  19.675  1.000 47.594  0 36  TRP DDD CZ2 1 ? 13 
ATOM   4384  C CZ3 . TRP D  2 36  ? 43.888  -74.259  20.941  1.000 47.900  0 36  TRP DDD CZ3 1 ? 13 
ATOM   4385  C CH2 . TRP D  2 36  ? 44.219  -75.611  20.879  1.000 48.233  0 36  TRP DDD CH2 1 ? 13 
ATOM   4386  N N   . PHE D  2 37  ? 41.444  -69.786  17.447  1.000 46.608  0 37  PHE DDD N   1 ? 13 
ATOM   4387  C CA  . PHE D  2 37  ? 41.358  -68.320  17.536  1.000 48.613  0 37  PHE DDD CA  1 ? 13 
ATOM   4388  C C   . PHE D  2 37  ? 42.123  -67.918  18.799  1.000 51.032  0 37  PHE DDD C   1 ? 13 
ATOM   4389  O O   . PHE D  2 37  ? 42.399  -68.793  19.652  1.000 51.064  0 37  PHE DDD O   1 ? 13 
ATOM   4390  C CB  . PHE D  2 37  ? 39.904  -67.868  17.619  1.000 48.493  0 37  PHE DDD CB  1 ? 13 
ATOM   4391  C CG  . PHE D  2 37  ? 39.118  -67.966  16.339  1.000 46.328  0 37  PHE DDD CG  1 ? 13 
ATOM   4392  C CD1 . PHE D  2 37  ? 38.687  -69.196  15.865  1.000 45.403  0 37  PHE DDD CD1 1 ? 13 
ATOM   4393  C CD2 . PHE D  2 37  ? 38.758  -66.824  15.642  1.000 46.461  0 37  PHE DDD CD2 1 ? 13 
ATOM   4394  C CE1 . PHE D  2 37  ? 37.923  -69.281  14.702  1.000 44.357  0 37  PHE DDD CE1 1 ? 13 
ATOM   4395  C CE2 . PHE D  2 37  ? 38.001  -66.902  14.478  1.000 46.171  0 37  PHE DDD CE2 1 ? 13 
ATOM   4396  C CZ  . PHE D  2 37  ? 37.587  -68.136  14.004  1.000 45.382  0 37  PHE DDD CZ  1 ? 13 
ATOM   4397  N N   . ARG D  2 38  ? 42.462  -66.641  18.929  1.000 52.424  0 38  ARG DDD N   1 ? 13 
ATOM   4398  C CA  . ARG D  2 38  ? 43.100  -66.138  20.166  1.000 54.208  0 38  ARG DDD CA  1 ? 13 
ATOM   4399  C C   . ARG D  2 38  ? 42.539  -64.759  20.492  1.000 56.574  0 38  ARG DDD C   1 ? 13 
ATOM   4400  O O   . ARG D  2 38  ? 42.015  -64.062  19.595  1.000 55.850  0 38  ARG DDD O   1 ? 13 
ATOM   4401  C CB  . ARG D  2 38  ? 44.623  -66.095  20.028  1.000 55.817  0 38  ARG DDD CB  1 ? 13 
ATOM   4402  C CG  . ARG D  2 38  ? 45.116  -64.997  19.100  1.000 57.993  0 38  ARG DDD CG  1 ? 13 
ATOM   4403  C CD  . ARG D  2 38  ? 46.571  -65.204  18.752  1.000 61.227  0 38  ARG DDD CD  1 ? 13 
ATOM   4404  N NE  . ARG D  2 38  ? 47.036  -64.233  17.770  1.000 63.465  0 38  ARG DDD NE  1 ? 13 
ATOM   4405  C CZ  . ARG D  2 38  ? 48.291  -64.112  17.365  1.000 65.159  0 38  ARG DDD CZ  1 ? 13 
ATOM   4406  N NH1 . ARG D  2 38  ? 49.253  -64.874  17.862  1.000 66.333  0 38  ARG DDD NH1 1 ? 13 
ATOM   4407  N NH2 . ARG D  2 38  ? 48.586  -63.202  16.465  1.000 67.703  0 38  ARG DDD NH2 1 ? 13 
ATOM   4408  N N   . GLN D  2 39  ? 42.676  -64.379  21.752  1.000 59.512  0 39  GLN DDD N   1 ? 13 
ATOM   4409  C CA  . GLN D  2 39  ? 42.171  -63.083  22.222  1.000 62.906  0 39  GLN DDD CA  1 ? 13 
ATOM   4410  C C   . GLN D  2 39  ? 43.153  -62.536  23.249  1.000 67.197  0 39  GLN DDD C   1 ? 13 
ATOM   4411  O O   . GLN D  2 39  ? 43.300  -63.157  24.327  1.000 66.152  0 39  GLN DDD O   1 ? 13 
ATOM   4412  C CB  . GLN D  2 39  ? 40.776  -63.257  22.793  1.000 62.028  0 39  GLN DDD CB  1 ? 13 
ATOM   4413  C CG  . GLN D  2 39  ? 40.192  -61.951  23.288  1.000 65.961  0 39  GLN DDD CG  1 ? 13 
ATOM   4414  C CD  . GLN D  2 39  ? 38.716  -62.097  23.540  1.000 67.056  0 39  GLN DDD CD  1 ? 13 
ATOM   4415  O OE1 . GLN D  2 39  ? 38.198  -63.178  23.841  1.000 68.893  0 39  GLN DDD OE1 1 ? 13 
ATOM   4416  N NE2 . GLN D  2 39  ? 38.017  -60.997  23.372  1.000 70.690  0 39  GLN DDD NE2 1 ? 13 
ATOM   4417  N N   . ALA D  2 40  ? 43.816  -61.450  22.866  1.000 71.558  0 40  ALA DDD N   1 ? 13 
ATOM   4418  C CA  . ALA D  2 40  ? 44.638  -60.608  23.749  1.000 78.098  0 40  ALA DDD CA  1 ? 13 
ATOM   4419  C C   . ALA D  2 40  ? 43.688  -59.692  24.511  1.000 82.576  0 40  ALA DDD C   1 ? 13 
ATOM   4420  O O   . ALA D  2 40  ? 42.613  -59.350  24.008  1.000 81.141  0 40  ALA DDD O   1 ? 13 
ATOM   4421  C CB  . ALA D  2 40  ? 45.638  -59.836  22.929  1.000 80.245  0 40  ALA DDD CB  1 ? 13 
ATOM   4422  N N   . PRO D  2 41  ? 44.047  -59.286  25.748  1.000 89.321  0 41  PRO DDD N   1 ? 13 
ATOM   4423  C CA  . PRO D  2 41  ? 43.213  -58.355  26.507  1.000 93.037  0 41  PRO DDD CA  1 ? 13 
ATOM   4424  C C   . PRO D  2 41  ? 43.031  -57.028  25.739  1.000 95.902  0 41  PRO DDD C   1 ? 13 
ATOM   4425  O O   . PRO D  2 41  ? 43.993  -56.505  25.191  1.000 95.633  0 41  PRO DDD O   1 ? 13 
ATOM   4426  C CB  . PRO D  2 41  ? 43.937  -58.178  27.854  1.000 96.044  0 41  PRO DDD CB  1 ? 13 
ATOM   4427  C CG  . PRO D  2 41  ? 45.350  -58.742  27.643  1.000 95.040  0 41  PRO DDD CG  1 ? 13 
ATOM   4428  C CD  . PRO D  2 41  ? 45.274  -59.681  26.457  1.000 90.330  0 41  PRO DDD CD  1 ? 13 
ATOM   4429  N N   . GLY D  2 42  ? 41.788  -56.554  25.658  1.000 96.073  0 42  GLY DDD N   1 ? 13 
ATOM   4430  C CA  . GLY D  2 42  ? 41.426  -55.310  24.954  1.000 98.369  0 42  GLY DDD CA  1 ? 13 
ATOM   4431  C C   . GLY D  2 42  ? 41.138  -55.523  23.478  1.000 97.107  0 42  GLY DDD C   1 ? 13 
ATOM   4432  O O   . GLY D  2 42  ? 40.643  -54.560  22.861  1.000 98.272  0 42  GLY DDD O   1 ? 13 
ATOM   4433  N N   . LYS D  2 43  ? 41.383  -56.723  22.928  1.000 93.757  0 43  LYS DDD N   1 ? 13 
ATOM   4434  C CA  . LYS D  2 43  ? 41.136  -57.012  21.495  1.000 91.618  0 43  LYS DDD CA  1 ? 13 
ATOM   4435  C C   . LYS D  2 43  ? 39.989  -57.998  21.328  1.000 87.562  0 43  LYS DDD C   1 ? 13 
ATOM   4436  O O   . LYS D  2 43  ? 39.645  -58.661  22.310  1.000 88.095  0 43  LYS DDD O   1 ? 13 
ATOM   4437  C CB  . LYS D  2 43  ? 42.405  -57.559  20.830  1.000 91.874  0 43  LYS DDD CB  1 ? 13 
ATOM   4438  C CG  . LYS D  2 43  ? 43.318  -56.469  20.292  1.000 96.807  0 43  LYS DDD CG  1 ? 13 
ATOM   4439  C CD  . LYS D  2 43  ? 44.047  -56.822  18.996  1.000 97.009  0 43  LYS DDD CD  1 ? 13 
ATOM   4440  C CE  . LYS D  2 43  ? 45.194  -55.879  18.736  1.000 103.332 0 43  LYS DDD CE  1 ? 13 
ATOM   4441  N NZ  . LYS D  2 43  ? 46.422  -56.639  18.406  1.000 103.926 0 43  LYS DDD NZ  1 ? 13 
ATOM   4442  N N   . GLU D  2 44  ? 39.479  -58.129  20.104  1.000 83.648  0 44  GLU DDD N   1 ? 13 
ATOM   4443  C CA  . GLU D  2 44  ? 38.468  -59.155  19.762  1.000 80.501  0 44  GLU DDD CA  1 ? 13 
ATOM   4444  C C   . GLU D  2 44  ? 39.193  -60.474  19.484  1.000 74.399  0 44  GLU DDD C   1 ? 13 
ATOM   4445  O O   . GLU D  2 44  ? 40.416  -60.463  19.392  1.000 74.004  0 44  GLU DDD O   1 ? 13 
ATOM   4446  C CB  . GLU D  2 44  ? 37.643  -58.732  18.554  1.000 85.417  0 44  GLU DDD CB  1 ? 13 
ATOM   4447  C CG  . GLU D  2 44  ? 37.010  -57.366  18.696  1.000 93.682  0 44  GLU DDD CG  1 ? 13 
ATOM   4448  C CD  . GLU D  2 44  ? 35.995  -57.040  17.606  1.000 97.150  0 44  GLU DDD CD  1 ? 13 
ATOM   4449  O OE1 . GLU D  2 44  ? 36.045  -57.658  16.486  1.000 94.347  0 44  GLU DDD OE1 1 ? 13 
ATOM   4450  O OE2 . GLU D  2 44  ? 35.151  -56.155  17.867  1.000 101.838 0 44  GLU DDD OE2 1 ? 13 
ATOM   4451  N N   . ARG D  2 45  ? 38.435  -61.556  19.370  1.000 70.200  0 45  ARG DDD N   1 ? 13 
ATOM   4452  C CA  . ARG D  2 45  ? 38.901  -62.858  18.865  1.000 68.777  0 45  ARG DDD CA  1 ? 13 
ATOM   4453  C C   . ARG D  2 45  ? 39.479  -62.684  17.467  1.000 67.756  0 45  ARG DDD C   1 ? 13 
ATOM   4454  O O   . ARG D  2 45  ? 38.777  -62.213  16.575  1.000 69.849  0 45  ARG DDD O   1 ? 13 
ATOM   4455  C CB  . ARG D  2 45  ? 37.767  -63.889  18.849  1.000 69.770  0 45  ARG DDD CB  1 ? 13 
ATOM   4456  C CG  . ARG D  2 45  ? 37.689  -64.681  20.136  1.000 71.425  0 45  ARG DDD CG  1 ? 13 
ATOM   4457  C CD  . ARG D  2 45  ? 36.330  -65.287  20.297  1.000 75.063  0 45  ARG DDD CD  1 ? 13 
ATOM   4458  N NE  . ARG D  2 45  ? 36.226  -65.785  21.658  1.000 81.263  0 45  ARG DDD NE  1 ? 13 
ATOM   4459  C CZ  . ARG D  2 45  ? 35.312  -66.664  22.065  1.000 82.487  0 45  ARG DDD CZ  1 ? 13 
ATOM   4460  N NH1 . ARG D  2 45  ? 34.412  -67.138  21.222  1.000 84.181  0 45  ARG DDD NH1 1 ? 13 
ATOM   4461  N NH2 . ARG D  2 45  ? 35.291  -67.060  23.320  1.000 82.586  0 45  ARG DDD NH2 1 ? 13 
ATOM   4462  N N   . GLU D  2 46  ? 40.730  -63.090  17.313  1.000 64.608  0 46  GLU DDD N   1 ? 13 
ATOM   4463  C CA  . GLU D  2 46  ? 41.511  -63.048  16.058  1.000 62.380  0 46  GLU DDD CA  1 ? 13 
ATOM   4464  C C   . GLU D  2 46  ? 41.641  -64.497  15.568  1.000 56.567  0 46  GLU DDD C   1 ? 13 
ATOM   4465  O O   . GLU D  2 46  ? 41.980  -65.386  16.382  1.000 51.943  0 46  GLU DDD O   1 ? 13 
ATOM   4466  C CB  . GLU D  2 46  ? 42.805  -62.307  16.399  1.000 66.848  0 46  GLU DDD CB  1 ? 13 
ATOM   4467  C CG  . GLU D  2 46  ? 43.893  -62.328  15.352  1.000 71.387  0 46  GLU DDD CG  1 ? 13 
ATOM   4468  C CD  . GLU D  2 46  ? 45.181  -61.618  15.792  1.000 76.660  0 46  GLU DDD CD  1 ? 13 
ATOM   4469  O OE1 . GLU D  2 46  ? 45.286  -61.154  16.959  1.000 79.844  0 46  GLU DDD OE1 1 ? 13 
ATOM   4470  O OE2 . GLU D  2 46  ? 46.138  -61.572  14.993  1.000 78.684  0 46  GLU DDD OE2 1 ? 13 
ATOM   4471  N N   . PHE D  2 47  ? 41.334  -64.744  14.294  1.000 53.832  0 47  PHE DDD N   1 ? 13 
ATOM   4472  C CA  . PHE D  2 47  ? 41.533  -66.064  13.635  1.000 50.501  0 47  PHE DDD CA  1 ? 13 
ATOM   4473  C C   . PHE D  2 47  ? 43.029  -66.395  13.620  1.000 48.916  0 47  PHE DDD C   1 ? 13 
ATOM   4474  O O   . PHE D  2 47  ? 43.817  -65.529  13.225  1.000 49.549  0 47  PHE DDD O   1 ? 13 
ATOM   4475  C CB  . PHE D  2 47  ? 40.966  -66.094  12.209  1.000 51.489  0 47  PHE DDD CB  1 ? 13 
ATOM   4476  C CG  . PHE D  2 47  ? 41.277  -67.369  11.466  1.000 51.656  0 47  PHE DDD CG  1 ? 13 
ATOM   4477  C CD1 . PHE D  2 47  ? 40.508  -68.504  11.658  1.000 49.618  0 47  PHE DDD CD1 1 ? 13 
ATOM   4478  C CD2 . PHE D  2 47  ? 42.341  -67.440  10.573  1.000 53.625  0 47  PHE DDD CD2 1 ? 13 
ATOM   4479  C CE1 . PHE D  2 47  ? 40.804  -69.683  10.997  1.000 49.316  0 47  PHE DDD CE1 1 ? 13 
ATOM   4480  C CE2 . PHE D  2 47  ? 42.623  -68.612  9.890   1.000 52.759  0 47  PHE DDD CE2 1 ? 13 
ATOM   4481  C CZ  . PHE D  2 47  ? 41.856  -69.732  10.108  1.000 52.260  0 47  PHE DDD CZ  1 ? 13 
ATOM   4482  N N   . VAL D  2 48  ? 43.390  -67.617  13.987  1.000 46.439  0 48  VAL DDD N   1 ? 13 
ATOM   4483  C CA  . VAL D  2 48  ? 44.803  -68.089  13.986  1.000 49.161  0 48  VAL DDD CA  1 ? 13 
ATOM   4484  C C   . VAL D  2 48  ? 44.997  -69.148  12.896  1.000 48.232  0 48  VAL DDD C   1 ? 13 
ATOM   4485  O O   . VAL D  2 48  ? 45.914  -68.982  12.062  1.000 51.090  0 48  VAL DDD O   1 ? 13 
ATOM   4486  C CB  . VAL D  2 48  ? 45.237  -68.606  15.376  1.000 48.775  0 48  VAL DDD CB  1 ? 13 
ATOM   4487  C CG1 . VAL D  2 48  ? 46.652  -69.190  15.349  1.000 49.405  0 48  VAL DDD CG1 1 ? 13 
ATOM   4488  C CG2 . VAL D  2 48  ? 45.135  -67.510  16.426  1.000 49.408  0 48  VAL DDD CG2 1 ? 13 
ATOM   4489  N N   . ALA D  2 49  ? 44.204  -70.217  12.916  1.000 47.545  0 49  ALA DDD N   1 ? 13 
ATOM   4490  C CA  . ALA D  2 49  ? 44.360  -71.362  11.989  1.000 48.342  0 49  ALA DDD CA  1 ? 13 
ATOM   4491  C C   . ALA D  2 49  ? 43.106  -72.238  11.940  1.000 47.339  0 49  ALA DDD C   1 ? 13 
ATOM   4492  O O   . ALA D  2 49  ? 42.327  -72.252  12.903  1.000 45.034  0 49  ALA DDD O   1 ? 13 
ATOM   4493  C CB  . ALA D  2 49  ? 45.577  -72.185  12.368  1.000 48.412  0 49  ALA DDD CB  1 ? 13 
ATOM   4494  N N   . ALA D  2 50  ? 42.945  -72.961  10.833  1.000 47.687  0 50  ALA DDD N   1 ? 13 
ATOM   4495  C CA  . ALA D  2 50  ? 41.846  -73.922  10.619  1.000 48.075  0 50  ALA DDD CA  1 ? 13 
ATOM   4496  C C   . ALA D  2 50  ? 42.311  -75.050  9.702   1.000 49.790  0 50  ALA DDD C   1 ? 13 
ATOM   4497  O O   . ALA D  2 50  ? 43.241  -74.846  8.889   1.000 54.026  0 50  ALA DDD O   1 ? 13 
ATOM   4498  C CB  . ALA D  2 50  ? 40.640  -73.217  10.063  1.000 47.307  0 50  ALA DDD CB  1 ? 13 
ATOM   4499  N N   . ILE D  2 51  ? 41.672  -76.204  9.845   1.000 48.670  0 51  ILE DDD N   1 ? 13 
ATOM   4500  C CA  . ILE D  2 51  ? 41.999  -77.437  9.076   1.000 48.476  0 51  ILE DDD CA  1 ? 13 
ATOM   4501  C C   . ILE D  2 51  ? 40.692  -78.130  8.679   1.000 47.040  0 51  ILE DDD C   1 ? 13 
ATOM   4502  O O   . ILE D  2 51  ? 39.820  -78.368  9.553   1.000 47.582  0 51  ILE DDD O   1 ? 13 
ATOM   4503  C CB  . ILE D  2 51  ? 42.959  -78.321  9.893   1.000 49.877  0 51  ILE DDD CB  1 ? 13 
ATOM   4504  C CG1 . ILE D  2 51  ? 43.493  -79.489  9.066   1.000 52.308  0 51  ILE DDD CG1 1 ? 13 
ATOM   4505  C CG2 . ILE D  2 51  ? 42.329  -78.759  11.208  1.000 49.101  0 51  ILE DDD CG2 1 ? 13 
ATOM   4506  C CD1 . ILE D  2 51  ? 44.689  -80.195  9.729   1.000 53.735  0 51  ILE DDD CD1 1 ? 13 
ATOM   4507  N N   . SER D  2 52  ? 40.553  -78.434  7.393   1.000 48.825  0 52  SER DDD N   1 ? 13 
ATOM   4508  C CA  . SER D  2 52  ? 39.404  -79.161  6.817   1.000 49.444  0 52  SER DDD CA  1 ? 13 
ATOM   4509  C C   . SER D  2 52  ? 39.436  -80.624  7.259   1.000 49.821  0 52  SER DDD C   1 ? 13 
ATOM   4510  O O   . SER D  2 52  ? 40.428  -81.063  7.877   1.000 52.228  0 52  SER DDD O   1 ? 13 
ATOM   4511  C CB  . SER D  2 52  ? 39.401  -79.072  5.313   1.000 51.389  0 52  SER DDD CB  1 ? 13 
ATOM   4512  O OG  . SER D  2 52  ? 38.093  -79.350  4.812   1.000 52.001  0 52  SER DDD OG  1 ? 13 
ATOM   4513  N N   . TRP D  2 53  ? 38.373  -81.350  6.919   1.000 50.745  0 53  TRP DDD N   1 ? 13 
ATOM   4514  C CA  . TRP D  2 53  ? 38.121  -82.761  7.308   1.000 50.141  0 53  TRP DDD CA  1 ? 13 
ATOM   4515  C C   . TRP D  2 53  ? 39.318  -83.629  6.899   1.000 52.459  0 53  TRP DDD C   1 ? 13 
ATOM   4516  O O   . TRP D  2 53  ? 39.842  -84.310  7.790   1.000 53.697  0 53  TRP DDD O   1 ? 13 
ATOM   4517  C CB  . TRP D  2 53  ? 36.818  -83.242  6.655   1.000 48.297  0 53  TRP DDD CB  1 ? 13 
ATOM   4518  C CG  . TRP D  2 53  ? 35.671  -82.284  6.790   1.000 46.274  0 53  TRP DDD CG  1 ? 13 
ATOM   4519  C CD1 . TRP D  2 53  ? 34.923  -82.045  7.907   1.000 45.248  0 53  TRP DDD CD1 1 ? 13 
ATOM   4520  C CD2 . TRP D  2 53  ? 35.144  -81.419  5.778   1.000 46.008  0 53  TRP DDD CD2 1 ? 13 
ATOM   4521  N NE1 . TRP D  2 53  ? 33.957  -81.109  7.658   1.000 44.819  0 53  TRP DDD NE1 1 ? 13 
ATOM   4522  C CE2 . TRP D  2 53  ? 34.068  -80.704  6.357   1.000 46.430  0 53  TRP DDD CE2 1 ? 13 
ATOM   4523  C CE3 . TRP D  2 53  ? 35.448  -81.210  4.434   1.000 47.894  0 53  TRP DDD CE3 1 ? 13 
ATOM   4524  C CZ2 . TRP D  2 53  ? 33.301  -79.787  5.635   1.000 47.969  0 53  TRP DDD CZ2 1 ? 13 
ATOM   4525  C CZ3 . TRP D  2 53  ? 34.709  -80.290  3.722   1.000 49.444  0 53  TRP DDD CZ3 1 ? 13 
ATOM   4526  C CH2 . TRP D  2 53  ? 33.633  -79.606  4.306   1.000 49.492  0 53  TRP DDD CH2 1 ? 13 
ATOM   4527  N N   . SER D  2 54  ? 39.756  -83.554  5.636   1.000 53.552  0 54  SER DDD N   1 ? 13 
ATOM   4528  C CA  . SER D  2 54  ? 40.832  -84.404  5.054   1.000 56.376  0 54  SER DDD CA  1 ? 13 
ATOM   4529  C C   . SER D  2 54  ? 42.214  -83.943  5.534   1.000 58.169  0 54  SER DDD C   1 ? 13 
ATOM   4530  O O   . SER D  2 54  ? 43.211  -84.581  5.117   1.000 59.203  0 54  SER DDD O   1 ? 13 
ATOM   4531  C CB  . SER D  2 54  ? 40.814  -84.348  3.556   1.000 55.866  0 54  SER DDD CB  1 ? 13 
ATOM   4532  O OG  . SER D  2 54  ? 41.166  -83.033  3.137   1.000 55.784  0 54  SER DDD OG  1 ? 13 
ATOM   4533  N N   . SER D  2 55  ? 42.282  -82.822  6.259   1.000 56.701  0 55  SER DDD N   1 ? 13 
ATOM   4534  C CA  . SER D  2 55  ? 43.526  -82.078  6.599   1.000 58.276  0 55  SER DDD CA  1 ? 13 
ATOM   4535  C C   . SER D  2 55  ? 43.984  -81.163  5.454   1.000 60.767  0 55  SER DDD C   1 ? 13 
ATOM   4536  O O   . SER D  2 55  ? 44.991  -80.479  5.677   1.000 58.483  0 55  SER DDD O   1 ? 13 
ATOM   4537  C CB  . SER D  2 55  ? 44.674  -82.990  6.995   1.000 59.039  0 55  SER DDD CB  1 ? 13 
ATOM   4538  O OG  . SER D  2 55  ? 44.354  -83.778  8.126   1.000 58.883  0 55  SER DDD OG  1 ? 13 
ATOM   4539  N N   . THR D  2 56  ? 43.298  -81.108  4.302   1.000 65.768  0 56  THR DDD N   1 ? 13 
ATOM   4540  C CA  . THR D  2 56  ? 44.006  -80.805  3.027   1.000 74.855  0 56  THR DDD CA  1 ? 13 
ATOM   4541  C C   . THR D  2 56  ? 43.951  -79.342  2.620   1.000 76.194  0 56  THR DDD C   1 ? 13 
ATOM   4542  O O   . THR D  2 56  ? 44.881  -78.912  1.931   1.000 88.858  0 56  THR DDD O   1 ? 13 
ATOM   4543  C CB  . THR D  2 56  ? 43.545  -81.635  1.830   1.000 83.473  0 56  THR DDD CB  1 ? 13 
ATOM   4544  O OG1 . THR D  2 56  ? 44.344  -82.814  1.924   1.000 94.281  0 56  THR DDD OG1 1 ? 13 
ATOM   4545  C CG2 . THR D  2 56  ? 43.770  -80.966  0.489   1.000 85.870  0 56  THR DDD CG2 1 ? 13 
ATOM   4546  N N   . PRO D  2 57  ? 42.854  -78.587  2.849   1.000 64.707  0 57  PRO DDD N   1 ? 13 
ATOM   4547  C CA  . PRO D  2 57  ? 42.984  -77.140  2.985   1.000 59.675  0 57  PRO DDD CA  1 ? 13 
ATOM   4548  C C   . PRO D  2 57  ? 43.299  -76.899  4.471   1.000 57.259  0 57  PRO DDD C   1 ? 13 
ATOM   4549  O O   . PRO D  2 57  ? 42.575  -77.383  5.325   1.000 54.926  0 57  PRO DDD O   1 ? 13 
ATOM   4550  C CB  . PRO D  2 57  ? 41.667  -76.561  2.459   1.000 58.939  0 57  PRO DDD CB  1 ? 13 
ATOM   4551  C CG  . PRO D  2 57  ? 40.792  -77.777  2.174   1.000 60.927  0 57  PRO DDD CG  1 ? 13 
ATOM   4552  C CD  . PRO D  2 57  ? 41.468  -79.026  2.735   1.000 60.285  0 57  PRO DDD CD  1 ? 13 
ATOM   4553  N N   . THR D  2 58  ? 44.447  -76.279  4.752   1.000 56.671  0 58  THR DDD N   1 ? 13 
ATOM   4554  C CA  . THR D  2 58  ? 44.753  -75.605  6.039   1.000 52.712  0 58  THR DDD CA  1 ? 13 
ATOM   4555  C C   . THR D  2 58  ? 44.744  -74.097  5.790   1.000 52.540  0 58  THR DDD C   1 ? 13 
ATOM   4556  O O   . THR D  2 58  ? 44.959  -73.676  4.661   1.000 51.239  0 58  THR DDD O   1 ? 13 
ATOM   4557  C CB  . THR D  2 58  ? 46.093  -76.014  6.657   1.000 52.776  0 58  THR DDD CB  1 ? 13 
ATOM   4558  O OG1 . THR D  2 58  ? 47.182  -75.735  5.766   1.000 56.147  0 58  THR DDD OG1 1 ? 13 
ATOM   4559  C CG2 . THR D  2 58  ? 46.097  -77.464  7.076   1.000 51.509  0 58  THR DDD CG2 1 ? 13 
ATOM   4560  N N   . TYR D  2 59  ? 44.448  -73.319  6.823   1.000 51.571  0 59  TYR DDD N   1 ? 13 
ATOM   4561  C CA  . TYR D  2 59  ? 44.324  -71.847  6.745   1.000 52.171  0 59  TYR DDD CA  1 ? 13 
ATOM   4562  C C   . TYR D  2 59  ? 45.044  -71.236  7.941   1.000 50.712  0 59  TYR DDD C   1 ? 13 
ATOM   4563  O O   . TYR D  2 59  ? 45.027  -71.852  9.026   1.000 49.192  0 59  TYR DDD O   1 ? 13 
ATOM   4564  C CB  . TYR D  2 59  ? 42.862  -71.417  6.769   1.000 52.604  0 59  TYR DDD CB  1 ? 13 
ATOM   4565  C CG  . TYR D  2 59  ? 41.932  -72.015  5.737   1.000 52.889  0 59  TYR DDD CG  1 ? 13 
ATOM   4566  C CD1 . TYR D  2 59  ? 41.182  -73.135  6.033   1.000 49.488  0 59  TYR DDD CD1 1 ? 13 
ATOM   4567  C CD2 . TYR D  2 59  ? 41.708  -71.395  4.518   1.000 53.935  0 59  TYR DDD CD2 1 ? 13 
ATOM   4568  C CE1 . TYR D  2 59  ? 40.251  -73.646  5.145   1.000 50.194  0 59  TYR DDD CE1 1 ? 13 
ATOM   4569  C CE2 . TYR D  2 59  ? 40.784  -71.891  3.615   1.000 53.305  0 59  TYR DDD CE2 1 ? 13 
ATOM   4570  C CZ  . TYR D  2 59  ? 40.055  -73.026  3.927   1.000 51.875  0 59  TYR DDD CZ  1 ? 13 
ATOM   4571  O OH  . TYR D  2 59  ? 39.159  -73.551  3.037   1.000 52.318  0 59  TYR DDD OH  1 ? 13 
ATOM   4572  N N   . TYR D  2 60  ? 45.631  -70.058  7.743   1.000 51.866  0 60  TYR DDD N   1 ? 13 
ATOM   4573  C CA  . TYR D  2 60  ? 46.451  -69.342  8.756   1.000 51.870  0 60  TYR DDD CA  1 ? 13 
ATOM   4574  C C   . TYR D  2 60  ? 46.139  -67.850  8.703   1.000 53.408  0 60  TYR DDD C   1 ? 13 
ATOM   4575  O O   . TYR D  2 60  ? 45.982  -67.303  7.604   1.000 54.461  0 60  TYR DDD O   1 ? 13 
ATOM   4576  C CB  . TYR D  2 60  ? 47.929  -69.623  8.494   1.000 52.448  0 60  TYR DDD CB  1 ? 13 
ATOM   4577  C CG  . TYR D  2 60  ? 48.293  -71.068  8.688   1.000 51.350  0 60  TYR DDD CG  1 ? 13 
ATOM   4578  C CD1 . TYR D  2 60  ? 48.401  -71.600  9.962   1.000 49.608  0 60  TYR DDD CD1 1 ? 13 
ATOM   4579  C CD2 . TYR D  2 60  ? 48.491  -71.912  7.603   1.000 51.213  0 60  TYR DDD CD2 1 ? 13 
ATOM   4580  C CE1 . TYR D  2 60  ? 48.732  -72.932  10.153  1.000 49.580  0 60  TYR DDD CE1 1 ? 13 
ATOM   4581  C CE2 . TYR D  2 60  ? 48.817  -73.245  7.775   1.000 50.316  0 60  TYR DDD CE2 1 ? 13 
ATOM   4582  C CZ  . TYR D  2 60  ? 48.944  -73.749  9.055   1.000 50.194  0 60  TYR DDD CZ  1 ? 13 
ATOM   4583  O OH  . TYR D  2 60  ? 49.262  -75.054  9.252   1.000 51.238  0 60  TYR DDD OH  1 ? 13 
ATOM   4584  N N   . GLY D  2 61  ? 46.068  -67.211  9.869   1.000 54.848  0 61  GLY DDD N   1 ? 13 
ATOM   4585  C CA  . GLY D  2 61  ? 46.079  -65.738  9.984   1.000 58.372  0 61  GLY DDD CA  1 ? 13 
ATOM   4586  C C   . GLY D  2 61  ? 47.384  -65.172  9.467   1.000 62.159  0 61  GLY DDD C   1 ? 13 
ATOM   4587  O O   . GLY D  2 61  ? 48.408  -65.860  9.584   1.000 62.738  0 61  GLY DDD O   1 ? 13 
ATOM   4588  N N   . GLU D  2 62  ? 47.355  -63.961  8.920   1.000 66.570  0 62  GLU DDD N   1 ? 13 
ATOM   4589  C CA  . GLU D  2 62  ? 48.521  -63.320  8.267   1.000 71.454  0 62  GLU DDD CA  1 ? 13 
ATOM   4590  C C   . GLU D  2 62  ? 49.721  -63.332  9.217   1.000 71.265  0 62  GLU DDD C   1 ? 13 
ATOM   4591  O O   . GLU D  2 62  ? 50.826  -63.666  8.778   1.000 72.396  0 62  GLU DDD O   1 ? 13 
ATOM   4592  C CB  . GLU D  2 62  ? 48.113  -61.909  7.860   1.000 77.410  0 62  GLU DDD CB  1 ? 13 
ATOM   4593  C CG  . GLU D  2 62  ? 47.415  -61.925  6.507   1.000 81.359  0 62  GLU DDD CG  1 ? 13 
ATOM   4594  C CD  . GLU D  2 62  ? 48.334  -62.366  5.368   1.000 84.970  0 62  GLU DDD CD  1 ? 13 
ATOM   4595  O OE1 . GLU D  2 62  ? 49.527  -61.945  5.358   1.000 87.976  0 62  GLU DDD OE1 1 ? 13 
ATOM   4596  O OE2 . GLU D  2 62  ? 47.862  -63.110  4.464   1.000 85.783  0 62  GLU DDD OE2 1 ? 13 
ATOM   4597  N N   . SER D  2 63  ? 49.494  -63.032  10.493  1.000 70.093  0 63  SER DDD N   1 ? 13 
ATOM   4598  C CA  . SER D  2 63  ? 50.565  -62.707  11.459  1.000 71.601  0 63  SER DDD CA  1 ? 13 
ATOM   4599  C C   . SER D  2 63  ? 51.211  -63.983  11.998  1.000 69.488  0 63  SER DDD C   1 ? 13 
ATOM   4600  O O   . SER D  2 63  ? 52.264  -63.856  12.620  1.000 74.507  0 63  SER DDD O   1 ? 13 
ATOM   4601  C CB  . SER D  2 63  ? 50.034  -61.834  12.567  1.000 71.526  0 63  SER DDD CB  1 ? 13 
ATOM   4602  O OG  . SER D  2 63  ? 49.002  -62.497  13.266  1.000 67.673  0 63  SER DDD OG  1 ? 13 
ATOM   4603  N N   . VAL D  2 64  ? 50.637  -65.162  11.765  1.000 65.754  0 64  VAL DDD N   1 ? 13 
ATOM   4604  C CA  . VAL D  2 64  ? 51.242  -66.432  12.258  1.000 65.885  0 64  VAL DDD CA  1 ? 13 
ATOM   4605  C C   . VAL D  2 64  ? 51.695  -67.297  11.087  1.000 66.566  0 64  VAL DDD C   1 ? 13 
ATOM   4606  O O   . VAL D  2 64  ? 52.414  -68.275  11.356  1.000 66.462  0 64  VAL DDD O   1 ? 13 
ATOM   4607  C CB  . VAL D  2 64  ? 50.287  -67.225  13.163  1.000 64.112  0 64  VAL DDD CB  1 ? 13 
ATOM   4608  C CG1 . VAL D  2 64  ? 49.872  -66.390  14.365  1.000 64.491  0 64  VAL DDD CG1 1 ? 13 
ATOM   4609  C CG2 . VAL D  2 64  ? 49.080  -67.774  12.398  1.000 61.381  0 64  VAL DDD CG2 1 ? 13 
ATOM   4610  N N   . LYS D  2 65  ? 51.306  -66.964  9.855   1.000 71.296  0 65  LYS DDD N   1 ? 13 
ATOM   4611  C CA  . LYS D  2 65  ? 51.689  -67.731  8.637   1.000 75.219  0 65  LYS DDD CA  1 ? 13 
ATOM   4612  C C   . LYS D  2 65  ? 53.210  -67.955  8.674   1.000 78.254  0 65  LYS DDD C   1 ? 13 
ATOM   4613  O O   . LYS D  2 65  ? 53.949  -66.971  8.935   1.000 82.133  0 65  LYS DDD O   1 ? 13 
ATOM   4614  C CB  . LYS D  2 65  ? 51.251  -66.994  7.363   1.000 79.067  0 65  LYS DDD CB  1 ? 13 
ATOM   4615  C CG  . LYS D  2 65  ? 50.735  -67.907  6.268   1.000 82.513  0 65  LYS DDD CG  1 ? 13 
ATOM   4616  C CD  . LYS D  2 65  ? 49.832  -67.273  5.245   1.000 86.639  0 65  LYS DDD CD  1 ? 13 
ATOM   4617  C CE  . LYS D  2 65  ? 49.078  -68.350  4.487   1.000 86.263  0 65  LYS DDD CE  1 ? 13 
ATOM   4618  N NZ  . LYS D  2 65  ? 48.811  -67.951  3.087   1.000 89.726  0 65  LYS DDD NZ  1 ? 13 
ATOM   4619  N N   . GLY D  2 66  ? 53.655  -69.202  8.493   1.000 76.371  0 66  GLY DDD N   1 ? 13 
ATOM   4620  C CA  . GLY D  2 66  ? 55.085  -69.567  8.468   1.000 78.053  0 66  GLY DDD CA  1 ? 13 
ATOM   4621  C C   . GLY D  2 66  ? 55.578  -70.060  9.818   1.000 77.639  0 66  GLY DDD C   1 ? 13 
ATOM   4622  O O   . GLY D  2 66  ? 56.481  -70.903  9.827   1.000 84.550  0 66  GLY DDD O   1 ? 13 
ATOM   4623  N N   . ARG D  2 67  ? 55.022  -69.563  10.927  1.000 74.398  0 67  ARG DDD N   1 ? 13 
ATOM   4624  C CA  . ARG D  2 67  ? 55.529  -69.855  12.297  1.000 72.204  0 67  ARG DDD CA  1 ? 13 
ATOM   4625  C C   . ARG D  2 67  ? 54.699  -70.962  12.954  1.000 68.837  0 67  ARG DDD C   1 ? 13 
ATOM   4626  O O   . ARG D  2 67  ? 55.264  -71.715  13.772  1.000 68.724  0 67  ARG DDD O   1 ? 13 
ATOM   4627  C CB  . ARG D  2 67  ? 55.516  -68.578  13.145  1.000 72.220  0 67  ARG DDD CB  1 ? 13 
ATOM   4628  C CG  . ARG D  2 67  ? 56.422  -67.477  12.615  1.000 74.688  0 67  ARG DDD CG  1 ? 13 
ATOM   4629  C CD  . ARG D  2 67  ? 56.527  -66.289  13.552  1.000 74.907  0 67  ARG DDD CD  1 ? 13 
ATOM   4630  N NE  . ARG D  2 67  ? 55.237  -65.664  13.810  1.000 70.908  0 67  ARG DDD NE  1 ? 13 
ATOM   4631  C CZ  . ARG D  2 67  ? 54.649  -65.593  14.998  1.000 69.240  0 67  ARG DDD CZ  1 ? 13 
ATOM   4632  N NH1 . ARG D  2 67  ? 55.225  -66.114  16.072  1.000 69.815  0 67  ARG DDD NH1 1 ? 13 
ATOM   4633  N NH2 . ARG D  2 67  ? 53.486  -64.974  15.110  1.000 67.828  0 67  ARG DDD NH2 1 ? 13 
ATOM   4634  N N   . PHE D  2 68  ? 53.403  -71.041  12.639  1.000 65.967  0 68  PHE DDD N   1 ? 13 
ATOM   4635  C CA  . PHE D  2 68  ? 52.428  -71.946  13.294  1.000 61.814  0 68  PHE DDD CA  1 ? 13 
ATOM   4636  C C   . PHE D  2 68  ? 51.971  -73.010  12.290  1.000 59.152  0 68  PHE DDD C   1 ? 13 
ATOM   4637  O O   . PHE D  2 68  ? 51.797  -72.717  11.118  1.000 57.870  0 68  PHE DDD O   1 ? 13 
ATOM   4638  C CB  . PHE D  2 68  ? 51.223  -71.153  13.800  1.000 61.560  0 68  PHE DDD CB  1 ? 13 
ATOM   4639  C CG  . PHE D  2 68  ? 51.440  -70.226  14.968  1.000 62.935  0 68  PHE DDD CG  1 ? 13 
ATOM   4640  C CD1 . PHE D  2 68  ? 52.702  -69.897  15.431  1.000 65.286  0 68  PHE DDD CD1 1 ? 13 
ATOM   4641  C CD2 . PHE D  2 68  ? 50.342  -69.658  15.598  1.000 63.944  0 68  PHE DDD CD2 1 ? 13 
ATOM   4642  C CE1 . PHE D  2 68  ? 52.861  -69.035  16.503  1.000 66.494  0 68  PHE DDD CE1 1 ? 13 
ATOM   4643  C CE2 . PHE D  2 68  ? 50.505  -68.796  16.670  1.000 64.996  0 68  PHE DDD CE2 1 ? 13 
ATOM   4644  C CZ  . PHE D  2 68  ? 51.767  -68.485  17.124  1.000 65.820  0 68  PHE DDD CZ  1 ? 13 
ATOM   4645  N N   . THR D  2 69  ? 51.787  -74.238  12.753  1.000 58.816  0 69  THR DDD N   1 ? 13 
ATOM   4646  C CA  . THR D  2 69  ? 51.329  -75.383  11.934  1.000 58.358  0 69  THR DDD CA  1 ? 13 
ATOM   4647  C C   . THR D  2 69  ? 50.144  -76.026  12.648  1.000 57.084  0 69  THR DDD C   1 ? 13 
ATOM   4648  O O   . THR D  2 69  ? 50.308  -76.430  13.823  1.000 55.952  0 69  THR DDD O   1 ? 13 
ATOM   4649  C CB  . THR D  2 69  ? 52.445  -76.410  11.711  1.000 61.349  0 69  THR DDD CB  1 ? 13 
ATOM   4650  O OG1 . THR D  2 69  ? 53.589  -75.712  11.209  1.000 65.754  0 69  THR DDD OG1 1 ? 13 
ATOM   4651  C CG2 . THR D  2 69  ? 51.997  -77.543  10.807  1.000 59.730  0 69  THR DDD CG2 1 ? 13 
ATOM   4652  N N   . ILE D  2 70  ? 48.997  -76.085  11.967  1.000 56.086  0 70  ILE DDD N   1 ? 13 
ATOM   4653  C CA  . ILE D  2 70  ? 47.794  -76.800  12.468  1.000 54.804  0 70  ILE DDD CA  1 ? 13 
ATOM   4654  C C   . ILE D  2 70  ? 47.827  -78.205  11.863  1.000 54.868  0 70  ILE DDD C   1 ? 13 
ATOM   4655  O O   . ILE D  2 70  ? 48.269  -78.344  10.728  1.000 56.035  0 70  ILE DDD O   1 ? 13 
ATOM   4656  C CB  . ILE D  2 70  ? 46.496  -76.026  12.170  1.000 53.312  0 70  ILE DDD CB  1 ? 13 
ATOM   4657  C CG1 . ILE D  2 70  ? 45.322  -76.588  12.975  1.000 52.464  0 70  ILE DDD CG1 1 ? 13 
ATOM   4658  C CG2 . ILE D  2 70  ? 46.199  -76.006  10.686  1.000 54.525  0 70  ILE DDD CG2 1 ? 13 
ATOM   4659  C CD1 . ILE D  2 70  ? 44.042  -75.763  12.894  1.000 52.975  0 70  ILE DDD CD1 1 ? 13 
ATOM   4660  N N   . SER D  2 71  ? 47.421  -79.210  12.640  1.000 54.228  0 71  SER DDD N   1 ? 13 
ATOM   4661  C CA  . SER D  2 71  ? 47.346  -80.631  12.221  1.000 53.064  0 71  SER DDD CA  1 ? 13 
ATOM   4662  C C   . SER D  2 71  ? 46.259  -81.309  13.060  1.000 53.502  0 71  SER DDD C   1 ? 13 
ATOM   4663  O O   . SER D  2 71  ? 45.819  -80.713  14.071  1.000 52.532  0 71  SER DDD O   1 ? 13 
ATOM   4664  C CB  . SER D  2 71  ? 48.678  -81.307  12.351  1.000 54.163  0 71  SER DDD CB  1 ? 13 
ATOM   4665  O OG  . SER D  2 71  ? 49.131  -81.314  13.705  1.000 54.627  0 71  SER DDD OG  1 ? 13 
ATOM   4666  N N   . ARG D  2 72  ? 45.777  -82.470  12.629  1.000 53.797  0 72  ARG DDD N   1 ? 13 
ATOM   4667  C CA  . ARG D  2 72  ? 44.686  -83.188  13.331  1.000 51.844  0 72  ARG DDD CA  1 ? 13 
ATOM   4668  C C   . ARG D  2 72  ? 45.024  -84.671  13.351  1.000 52.445  0 72  ARG DDD C   1 ? 13 
ATOM   4669  O O   . ARG D  2 72  ? 45.689  -85.134  12.426  1.000 54.903  0 72  ARG DDD O   1 ? 13 
ATOM   4670  C CB  . ARG D  2 72  ? 43.335  -82.913  12.659  1.000 51.462  0 72  ARG DDD CB  1 ? 13 
ATOM   4671  C CG  . ARG D  2 72  ? 43.221  -83.389  11.219  1.000 51.579  0 72  ARG DDD CG  1 ? 13 
ATOM   4672  C CD  . ARG D  2 72  ? 41.919  -82.969  10.582  1.000 50.080  0 72  ARG DDD CD  1 ? 13 
ATOM   4673  N NE  . ARG D  2 72  ? 40.754  -83.490  11.288  1.000 50.542  0 72  ARG DDD NE  1 ? 13 
ATOM   4674  C CZ  . ARG D  2 72  ? 39.567  -82.868  11.364  1.000 50.630  0 72  ARG DDD CZ  1 ? 13 
ATOM   4675  N NH1 . ARG D  2 72  ? 39.352  -81.710  10.755  1.000 51.269  0 72  ARG DDD NH1 1 ? 13 
ATOM   4676  N NH2 . ARG D  2 72  ? 38.569  -83.442  12.004  1.000 49.379  0 72  ARG DDD NH2 1 ? 13 
ATOM   4677  N N   . ASP D  2 73  ? 44.596  -85.363  14.395  1.000 52.669  0 73  ASP DDD N   1 ? 13 
ATOM   4678  C CA  . ASP D  2 73  ? 44.726  -86.826  14.558  1.000 56.170  0 73  ASP DDD CA  1 ? 13 
ATOM   4679  C C   . ASP D  2 73  ? 43.329  -87.344  14.876  1.000 56.041  0 73  ASP DDD C   1 ? 13 
ATOM   4680  O O   . ASP D  2 73  ? 42.889  -87.230  16.035  1.000 58.627  0 73  ASP DDD O   1 ? 13 
ATOM   4681  C CB  . ASP D  2 73  ? 45.768  -87.155  15.624  1.000 59.897  0 73  ASP DDD CB  1 ? 13 
ATOM   4682  C CG  . ASP D  2 73  ? 45.971  -88.645  15.825  1.000 63.830  0 73  ASP DDD CG  1 ? 13 
ATOM   4683  O OD1 . ASP D  2 73  ? 45.165  -89.422  15.254  1.000 62.836  0 73  ASP DDD OD1 1 ? 13 
ATOM   4684  O OD2 . ASP D  2 73  ? 46.915  -89.005  16.568  1.000 66.307  0 73  ASP DDD OD2 1 ? 13 
ATOM   4685  N N   . ASN D  2 74  ? 42.633  -87.825  13.847  1.000 56.744  0 74  ASN DDD N   1 ? 13 
ATOM   4686  C CA  . ASN D  2 74  ? 41.214  -88.251  13.949  1.000 54.419  0 74  ASN DDD CA  1 ? 13 
ATOM   4687  C C   . ASN D  2 74  ? 41.101  -89.410  14.946  1.000 54.894  0 74  ASN DDD C   1 ? 13 
ATOM   4688  O O   . ASN D  2 74  ? 40.119  -89.422  15.700  1.000 55.066  0 74  ASN DDD O   1 ? 13 
ATOM   4689  C CB  . ASN D  2 74  ? 40.646  -88.539  12.571  1.000 54.395  0 74  ASN DDD CB  1 ? 13 
ATOM   4690  C CG  . ASN D  2 74  ? 40.364  -87.267  11.794  1.000 55.381  0 74  ASN DDD CG  1 ? 13 
ATOM   4691  O OD1 . ASN D  2 74  ? 40.557  -86.137  12.259  1.000 53.580  0 74  ASN DDD OD1 1 ? 13 
ATOM   4692  N ND2 . ASN D  2 74  ? 39.878  -87.443  10.587  1.000 58.432  0 74  ASN DDD ND2 1 ? 13 
ATOM   4693  N N   . ALA D  2 75  ? 42.095  -90.295  15.021  1.000 56.240  0 75  ALA DDD N   1 ? 13 
ATOM   4694  C CA  . ALA D  2 75  ? 42.094  -91.446  15.951  1.000 58.504  0 75  ALA DDD CA  1 ? 13 
ATOM   4695  C C   . ALA D  2 75  ? 42.032  -90.954  17.412  1.000 58.180  0 75  ALA DDD C   1 ? 13 
ATOM   4696  O O   . ALA D  2 75  ? 41.547  -91.719  18.263  1.000 59.924  0 75  ALA DDD O   1 ? 13 
ATOM   4697  C CB  . ALA D  2 75  ? 43.294  -92.324  15.704  1.000 60.695  0 75  ALA DDD CB  1 ? 13 
ATOM   4698  N N   . LYS D  2 76  ? 42.487  -89.734  17.700  1.000 55.490  0 76  LYS DDD N   1 ? 13 
ATOM   4699  C CA  . LYS D  2 76  ? 42.528  -89.174  19.074  1.000 56.079  0 76  LYS DDD CA  1 ? 13 
ATOM   4700  C C   . LYS D  2 76  ? 41.582  -87.984  19.242  1.000 52.814  0 76  LYS DDD C   1 ? 13 
ATOM   4701  O O   . LYS D  2 76  ? 41.684  -87.315  20.264  1.000 53.710  0 76  LYS DDD O   1 ? 13 
ATOM   4702  C CB  . LYS D  2 76  ? 43.943  -88.711  19.399  1.000 57.238  0 76  LYS DDD CB  1 ? 13 
ATOM   4703  C CG  . LYS D  2 76  ? 44.973  -89.822  19.316  1.000 61.373  0 76  LYS DDD CG  1 ? 13 
ATOM   4704  C CD  . LYS D  2 76  ? 46.264  -89.472  19.988  1.000 63.492  0 76  LYS DDD CD  1 ? 13 
ATOM   4705  C CE  . LYS D  2 76  ? 47.213  -90.636  20.001  1.000 67.982  0 76  LYS DDD CE  1 ? 13 
ATOM   4706  N NZ  . LYS D  2 76  ? 48.505  -90.230  20.584  1.000 71.578  0 76  LYS DDD NZ  1 ? 13 
ATOM   4707  N N   . ASN D  2 77  ? 40.706  -87.718  18.278  1.000 52.865  0 77  ASN DDD N   1 ? 13 
ATOM   4708  C CA  . ASN D  2 77  ? 39.742  -86.589  18.382  1.000 50.142  0 77  ASN DDD CA  1 ? 13 
ATOM   4709  C C   . ASN D  2 77  ? 40.502  -85.287  18.703  1.000 48.078  0 77  ASN DDD C   1 ? 13 
ATOM   4710  O O   . ASN D  2 77  ? 39.963  -84.457  19.448  1.000 45.283  0 77  ASN DDD O   1 ? 13 
ATOM   4711  C CB  . ASN D  2 77  ? 38.695  -86.858  19.470  1.000 49.034  0 77  ASN DDD CB  1 ? 13 
ATOM   4712  C CG  . ASN D  2 77  ? 37.483  -87.593  18.946  1.000 48.289  0 77  ASN DDD CG  1 ? 13 
ATOM   4713  O OD1 . ASN D  2 77  ? 37.620  -88.481  18.119  1.000 48.715  0 77  ASN DDD OD1 1 ? 13 
ATOM   4714  N ND2 . ASN D  2 77  ? 36.295  -87.218  19.402  1.000 48.319  0 77  ASN DDD ND2 1 ? 13 
ATOM   4715  N N   . THR D  2 78  ? 41.719  -85.114  18.187  1.000 46.412  0 78  THR DDD N   1 ? 13 
ATOM   4716  C CA  . THR D  2 78  ? 42.595  -83.999  18.607  1.000 46.653  0 78  THR DDD CA  1 ? 13 
ATOM   4717  C C   . THR D  2 78  ? 43.060  -83.177  17.400  1.000 47.061  0 78  THR DDD C   1 ? 13 
ATOM   4718  O O   . THR D  2 78  ? 43.446  -83.765  16.368  1.000 49.940  0 78  THR DDD O   1 ? 13 
ATOM   4719  C CB  . THR D  2 78  ? 43.745  -84.523  19.480  1.000 48.022  0 78  THR DDD CB  1 ? 13 
ATOM   4720  O OG1 . THR D  2 78  ? 43.170  -85.132  20.635  1.000 49.206  0 78  THR DDD OG1 1 ? 13 
ATOM   4721  C CG2 . THR D  2 78  ? 44.700  -83.433  19.901  1.000 46.285  0 78  THR DDD CG2 1 ? 13 
ATOM   4722  N N   . VAL D  2 79  ? 42.997  -81.854  17.547  1.000 46.621  0 79  VAL DDD N   1 ? 13 
ATOM   4723  C CA  . VAL D  2 79  ? 43.658  -80.858  16.658  1.000 46.712  0 79  VAL DDD CA  1 ? 13 
ATOM   4724  C C   . VAL D  2 79  ? 44.843  -80.250  17.433  1.000 47.562  0 79  VAL DDD C   1 ? 13 
ATOM   4725  O O   . VAL D  2 79  ? 44.729  -80.050  18.660  1.000 48.550  0 79  VAL DDD O   1 ? 13 
ATOM   4726  C CB  . VAL D  2 79  ? 42.650  -79.802  16.178  1.000 44.332  0 79  VAL DDD CB  1 ? 13 
ATOM   4727  C CG1 . VAL D  2 79  ? 42.047  -79.008  17.328  1.000 45.822  0 79  VAL DDD CG1 1 ? 13 
ATOM   4728  C CG2 . VAL D  2 79  ? 43.255  -78.856  15.169  1.000 43.655  0 79  VAL DDD CG2 1 ? 13 
ATOM   4729  N N   . TYR D  2 80  ? 45.959  -80.018  16.747  1.000 48.156  0 80  TYR DDD N   1 ? 13 
ATOM   4730  C CA  . TYR D  2 80  ? 47.214  -79.483  17.326  1.000 51.567  0 80  TYR DDD CA  1 ? 13 
ATOM   4731  C C   . TYR D  2 80  ? 47.541  -78.129  16.696  1.000 52.427  0 80  TYR DDD C   1 ? 13 
ATOM   4732  O O   . TYR D  2 80  ? 47.218  -77.907  15.519  1.000 51.108  0 80  TYR DDD O   1 ? 13 
ATOM   4733  C CB  . TYR D  2 80  ? 48.363  -80.464  17.099  1.000 53.985  0 80  TYR DDD CB  1 ? 13 
ATOM   4734  C CG  . TYR D  2 80  ? 48.163  -81.803  17.756  1.000 55.100  0 80  TYR DDD CG  1 ? 13 
ATOM   4735  C CD1 . TYR D  2 80  ? 48.379  -81.968  19.112  1.000 56.581  0 80  TYR DDD CD1 1 ? 13 
ATOM   4736  C CD2 . TYR D  2 80  ? 47.756  -82.907  17.026  1.000 55.991  0 80  TYR DDD CD2 1 ? 13 
ATOM   4737  C CE1 . TYR D  2 80  ? 48.217  -83.198  19.728  1.000 57.040  0 80  TYR DDD CE1 1 ? 13 
ATOM   4738  C CE2 . TYR D  2 80  ? 47.586  -84.143  17.626  1.000 56.170  0 80  TYR DDD CE2 1 ? 13 
ATOM   4739  C CZ  . TYR D  2 80  ? 47.806  -84.281  18.982  1.000 56.682  0 80  TYR DDD CZ  1 ? 13 
ATOM   4740  O OH  . TYR D  2 80  ? 47.640  -85.473  19.604  1.000 58.777  0 80  TYR DDD OH  1 ? 13 
ATOM   4741  N N   . LEU D  2 81  ? 48.169  -77.250  17.478  1.000 53.227  0 81  LEU DDD N   1 ? 13 
ATOM   4742  C CA  . LEU D  2 81  ? 48.798  -76.006  16.971  1.000 55.182  0 81  LEU DDD CA  1 ? 13 
ATOM   4743  C C   . LEU D  2 81  ? 50.257  -75.984  17.435  1.000 58.062  0 81  LEU DDD C   1 ? 13 
ATOM   4744  O O   . LEU D  2 81  ? 50.500  -75.744  18.627  1.000 58.605  0 81  LEU DDD O   1 ? 13 
ATOM   4745  C CB  . LEU D  2 81  ? 48.009  -74.778  17.450  1.000 55.658  0 81  LEU DDD CB  1 ? 13 
ATOM   4746  C CG  . LEU D  2 81  ? 48.391  -73.464  16.764  1.000 56.660  0 81  LEU DDD CG  1 ? 13 
ATOM   4747  C CD1 . LEU D  2 81  ? 47.979  -73.462  15.300  1.000 56.744  0 81  LEU DDD CD1 1 ? 13 
ATOM   4748  C CD2 . LEU D  2 81  ? 47.753  -72.286  17.476  1.000 56.143  0 81  LEU DDD CD2 1 ? 13 
ATOM   4749  N N   . GLN D  2 82  ? 51.181  -76.275  16.517  1.000 58.054  0 82  GLN DDD N   1 ? 13 
ATOM   4750  C CA  . GLN D  2 82  ? 52.639  -76.132  16.710  1.000 59.875  0 82  GLN DDD CA  1 ? 13 
ATOM   4751  C C   . GLN D  2 82  ? 52.935  -74.638  16.534  1.000 60.694  0 82  GLN DDD C   1 ? 13 
ATOM   4752  O O   . GLN D  2 82  ? 52.617  -74.103  15.467  1.000 58.122  0 82  GLN DDD O   1 ? 13 
ATOM   4753  C CB  . GLN D  2 82  ? 53.380  -77.044  15.728  1.000 61.017  0 82  GLN DDD CB  1 ? 13 
ATOM   4754  C CG  . GLN D  2 82  ? 54.885  -77.113  15.966  1.000 63.391  0 82  GLN DDD CG  1 ? 13 
ATOM   4755  C CD  . GLN D  2 82  ? 55.219  -77.503  17.385  1.000 63.896  0 82  GLN DDD CD  1 ? 13 
ATOM   4756  O OE1 . GLN D  2 82  ? 54.716  -78.479  17.915  1.000 62.110  0 82  GLN DDD OE1 1 ? 13 
ATOM   4757  N NE2 . GLN D  2 82  ? 56.087  -76.740  18.021  1.000 67.288  0 82  GLN DDD NE2 1 ? 13 
ATOM   4758  N N   . MET D  2 83  ? 53.401  -73.971  17.587  1.000 63.631  0 83  MET DDD N   1 ? 13 
ATOM   4759  C CA  . MET D  2 83  ? 53.717  -72.520  17.555  1.000 66.491  0 83  MET DDD CA  1 ? 13 
ATOM   4760  C C   . MET D  2 83  ? 55.229  -72.391  17.726  1.000 70.663  0 83  MET DDD C   1 ? 13 
ATOM   4761  O O   . MET D  2 83  ? 55.728  -72.740  18.803  1.000 73.975  0 83  MET DDD O   1 ? 13 
ATOM   4762  C CB  . MET D  2 83  ? 52.994  -71.743  18.660  1.000 67.023  0 83  MET DDD CB  1 ? 13 
ATOM   4763  C CG  . MET D  2 83  ? 51.481  -71.963  18.682  1.000 65.975  0 83  MET DDD CG  1 ? 13 
ATOM   4764  S SD  . MET D  2 83  ? 50.605  -70.996  19.972  1.000 68.465  0 83  MET DDD SD  1 ? 13 
ATOM   4765  C CE  . MET D  2 83  ? 51.218  -71.834  21.434  1.000 72.236  0 83  MET DDD CE  1 ? 13 
ATOM   4766  N N   . ASN D  2 84  ? 55.930  -71.976  16.671  1.000 73.065  0 84  ASN DDD N   1 ? 13 
ATOM   4767  C CA  . ASN D  2 84  ? 57.405  -71.803  16.666  1.000 76.218  0 84  ASN DDD CA  1 ? 13 
ATOM   4768  C C   . ASN D  2 84  ? 57.734  -70.310  16.656  1.000 78.713  0 84  ASN DDD C   1 ? 13 
ATOM   4769  O O   . ASN D  2 84  ? 56.864  -69.496  16.243  1.000 79.136  0 84  ASN DDD O   1 ? 13 
ATOM   4770  C CB  . ASN D  2 84  ? 58.041  -72.549  15.495  1.000 77.605  0 84  ASN DDD CB  1 ? 13 
ATOM   4771  C CG  . ASN D  2 84  ? 57.833  -74.044  15.590  1.000 76.623  0 84  ASN DDD CG  1 ? 13 
ATOM   4772  O OD1 . ASN D  2 84  ? 57.828  -74.604  16.679  1.000 75.337  0 84  ASN DDD OD1 1 ? 13 
ATOM   4773  N ND2 . ASN D  2 84  ? 57.658  -74.697  14.458  1.000 77.829  0 84  ASN DDD ND2 1 ? 13 
ATOM   4774  N N   . ARG D  2 85  ? 58.938  -69.968  17.121  1.000 83.155  0 85  ARG DDD N   1 ? 13 
ATOM   4775  C CA  . ARG D  2 85  ? 59.500  -68.599  17.038  1.000 86.631  0 85  ARG DDD CA  1 ? 13 
ATOM   4776  C C   . ARG D  2 85  ? 58.446  -67.630  17.589  1.000 82.537  0 85  ARG DDD C   1 ? 13 
ATOM   4777  O O   . ARG D  2 85  ? 58.051  -66.673  16.893  1.000 81.259  0 85  ARG DDD O   1 ? 13 
ATOM   4778  C CB  . ARG D  2 85  ? 59.935  -68.335  15.591  1.000 90.450  0 85  ARG DDD CB  1 ? 13 
ATOM   4779  C CG  . ARG D  2 85  ? 60.951  -69.338  15.050  1.000 93.897  0 85  ARG DDD CG  1 ? 13 
ATOM   4780  C CD  . ARG D  2 85  ? 61.830  -68.890  13.890  1.000 98.479  0 85  ARG DDD CD  1 ? 13 
ATOM   4781  N NE  . ARG D  2 85  ? 61.107  -68.116  12.882  1.000 98.019  0 85  ARG DDD NE  1 ? 13 
ATOM   4782  C CZ  . ARG D  2 85  ? 60.166  -68.588  12.060  1.000 94.868  0 85  ARG DDD CZ  1 ? 13 
ATOM   4783  N NH1 . ARG D  2 85  ? 59.798  -69.860  12.097  1.000 91.930  0 85  ARG DDD NH1 1 ? 13 
ATOM   4784  N NH2 . ARG D  2 85  ? 59.569  -67.760  11.218  1.000 95.087  0 85  ARG DDD NH2 1 ? 13 
ATOM   4785  N N   . LEU D  2 86  ? 57.990  -67.897  18.813  1.000 80.710  0 86  LEU DDD N   1 ? 13 
ATOM   4786  C CA  . LEU D  2 86  ? 56.933  -67.104  19.484  1.000 80.072  0 86  LEU DDD CA  1 ? 13 
ATOM   4787  C C   . LEU D  2 86  ? 57.464  -65.708  19.826  1.000 83.221  0 86  LEU DDD C   1 ? 13 
ATOM   4788  O O   . LEU D  2 86  ? 58.643  -65.588  20.242  1.000 85.938  0 86  LEU DDD O   1 ? 13 
ATOM   4789  C CB  . LEU D  2 86  ? 56.485  -67.855  20.736  1.000 78.389  0 86  LEU DDD CB  1 ? 13 
ATOM   4790  C CG  . LEU D  2 86  ? 55.551  -69.027  20.467  1.000 74.269  0 86  LEU DDD CG  1 ? 13 
ATOM   4791  C CD1 . LEU D  2 86  ? 55.464  -69.944  21.675  1.000 74.616  0 86  LEU DDD CD1 1 ? 13 
ATOM   4792  C CD2 . LEU D  2 86  ? 54.168  -68.515  20.073  1.000 72.834  0 86  LEU DDD CD2 1 ? 13 
ATOM   4793  N N   . LYS D  2 87  ? 56.607  -64.702  19.652  1.000 82.977  0 87  LYS DDD N   1 ? 13 
ATOM   4794  C CA  . LYS D  2 87  ? 56.898  -63.275  19.933  1.000 87.362  0 87  LYS DDD CA  1 ? 13 
ATOM   4795  C C   . LYS D  2 87  ? 55.952  -62.816  21.038  1.000 85.528  0 87  LYS DDD C   1 ? 13 
ATOM   4796  O O   . LYS D  2 87  ? 54.904  -63.425  21.240  1.000 82.281  0 87  LYS DDD O   1 ? 13 
ATOM   4797  C CB  . LYS D  2 87  ? 56.720  -62.448  18.659  1.000 89.746  0 87  LYS DDD CB  1 ? 13 
ATOM   4798  C CG  . LYS D  2 87  ? 57.241  -63.097  17.390  1.000 92.375  0 87  LYS DDD CG  1 ? 13 
ATOM   4799  C CD  . LYS D  2 87  ? 56.845  -62.392  16.104  1.000 94.231  0 87  LYS DDD CD  1 ? 13 
ATOM   4800  C CE  . LYS D  2 87  ? 57.626  -62.954  14.934  1.000 96.775  0 87  LYS DDD CE  1 ? 13 
ATOM   4801  N NZ  . LYS D  2 87  ? 57.304  -62.286  13.651  1.000 97.977  0 87  LYS DDD NZ  1 ? 13 
ATOM   4802  N N   . PRO D  2 88  ? 56.303  -61.766  21.814  1.000 87.588  0 88  PRO DDD N   1 ? 13 
ATOM   4803  C CA  . PRO D  2 88  ? 55.399  -61.242  22.839  1.000 86.674  0 88  PRO DDD CA  1 ? 13 
ATOM   4804  C C   . PRO D  2 88  ? 53.972  -60.965  22.341  1.000 82.101  0 88  PRO DDD C   1 ? 13 
ATOM   4805  O O   . PRO D  2 88  ? 53.068  -61.248  23.106  1.000 78.049  0 88  PRO DDD O   1 ? 13 
ATOM   4806  C CB  . PRO D  2 88  ? 56.116  -59.956  23.281  1.000 91.268  0 88  PRO DDD CB  1 ? 13 
ATOM   4807  C CG  . PRO D  2 88  ? 57.579  -60.304  23.117  1.000 93.542  0 88  PRO DDD CG  1 ? 13 
ATOM   4808  C CD  . PRO D  2 88  ? 57.621  -61.101  21.832  1.000 91.078  0 88  PRO DDD CD  1 ? 13 
ATOM   4809  N N   . GLU D  2 89  ? 53.798  -60.488  21.092  1.000 82.157  0 89  GLU DDD N   1 ? 13 
ATOM   4810  C CA  . GLU D  2 89  ? 52.450  -60.162  20.533  1.000 80.397  0 89  GLU DDD CA  1 ? 13 
ATOM   4811  C C   . GLU D  2 89  ? 51.614  -61.432  20.308  1.000 72.978  0 89  GLU DDD C   1 ? 13 
ATOM   4812  O O   . GLU D  2 89  ? 50.456  -61.273  19.916  1.000 68.522  0 89  GLU DDD O   1 ? 13 
ATOM   4813  C CB  . GLU D  2 89  ? 52.515  -59.411  19.211  1.000 84.369  0 89  GLU DDD CB  1 ? 13 
ATOM   4814  C CG  . GLU D  2 89  ? 53.217  -60.184  18.136  1.000 86.822  0 89  GLU DDD CG  1 ? 13 
ATOM   4815  C CD  . GLU D  2 89  ? 54.461  -59.520  17.560  1.000 94.596  0 89  GLU DDD CD  1 ? 13 
ATOM   4816  O OE1 . GLU D  2 89  ? 55.146  -58.672  18.258  1.000 94.664  0 89  GLU DDD OE1 1 ? 13 
ATOM   4817  O OE2 . GLU D  2 89  ? 54.801  -59.929  16.424  1.000 95.921  0 89  GLU DDD OE2 1 ? 13 
ATOM   4818  N N   . ASP D  2 90  ? 52.178  -62.625  20.516  1.000 70.326  0 90  ASP DDD N   1 ? 13 
ATOM   4819  C CA  . ASP D  2 90  ? 51.445  -63.917  20.431  1.000 66.188  0 90  ASP DDD CA  1 ? 13 
ATOM   4820  C C   . ASP D  2 90  ? 50.795  -64.257  21.780  1.000 64.582  0 90  ASP DDD C   1 ? 13 
ATOM   4821  O O   . ASP D  2 90  ? 49.994  -65.212  21.818  1.000 61.605  0 90  ASP DDD O   1 ? 13 
ATOM   4822  C CB  . ASP D  2 90  ? 52.360  -65.067  20.006  1.000 65.635  0 90  ASP DDD CB  1 ? 13 
ATOM   4823  C CG  . ASP D  2 90  ? 52.893  -64.948  18.598  1.000 65.542  0 90  ASP DDD CG  1 ? 13 
ATOM   4824  O OD1 . ASP D  2 90  ? 52.094  -64.604  17.680  1.000 62.162  0 90  ASP DDD OD1 1 ? 13 
ATOM   4825  O OD2 . ASP D  2 90  ? 54.102  -65.217  18.431  1.000 68.048  0 90  ASP DDD OD2 1 ? 13 
ATOM   4826  N N   . THR D  2 91  ? 51.126  -63.523  22.841  1.000 66.241  0 91  THR DDD N   1 ? 13 
ATOM   4827  C CA  . THR D  2 91  ? 50.518  -63.691  24.182  1.000 66.348  0 91  THR DDD CA  1 ? 13 
ATOM   4828  C C   . THR D  2 91  ? 49.012  -63.455  24.062  1.000 65.820  0 91  THR DDD C   1 ? 13 
ATOM   4829  O O   . THR D  2 91  ? 48.619  -62.398  23.576  1.000 70.243  0 91  THR DDD O   1 ? 13 
ATOM   4830  C CB  . THR D  2 91  ? 51.154  -62.746  25.205  1.000 68.416  0 91  THR DDD CB  1 ? 13 
ATOM   4831  O OG1 . THR D  2 91  ? 52.510  -63.175  25.348  1.000 68.980  0 91  THR DDD OG1 1 ? 13 
ATOM   4832  C CG2 . THR D  2 91  ? 50.437  -62.752  26.536  1.000 67.312  0 91  THR DDD CG2 1 ? 13 
ATOM   4833  N N   . ALA D  2 92  ? 48.205  -64.420  24.484  1.000 64.483  0 92  ALA DDD N   1 ? 13 
ATOM   4834  C CA  . ALA D  2 92  ? 46.730  -64.356  24.413  1.000 62.645  0 92  ALA DDD CA  1 ? 13 
ATOM   4835  C C   . ALA D  2 92  ? 46.123  -65.621  25.010  1.000 60.034  0 92  ALA DDD C   1 ? 13 
ATOM   4836  O O   . ALA D  2 92  ? 46.859  -66.582  25.280  1.000 59.161  0 92  ALA DDD O   1 ? 13 
ATOM   4837  C CB  . ALA D  2 92  ? 46.262  -64.184  22.985  1.000 61.237  0 92  ALA DDD CB  1 ? 13 
ATOM   4838  N N   . VAL D  2 93  ? 44.804  -65.596  25.177  1.000 58.519  0 93  VAL DDD N   1 ? 13 
ATOM   4839  C CA  . VAL D  2 93  ? 43.996  -66.824  25.388  1.000 55.879  0 93  VAL DDD CA  1 ? 13 
ATOM   4840  C C   . VAL D  2 93  ? 43.767  -67.434  24.008  1.000 52.477  0 93  VAL DDD C   1 ? 13 
ATOM   4841  O O   . VAL D  2 93  ? 43.336  -66.704  23.100  1.000 50.298  0 93  VAL DDD O   1 ? 13 
ATOM   4842  C CB  . VAL D  2 93  ? 42.693  -66.506  26.139  1.000 56.518  0 93  VAL DDD CB  1 ? 13 
ATOM   4843  C CG1 . VAL D  2 93  ? 41.792  -67.725  26.234  1.000 53.828  0 93  VAL DDD CG1 1 ? 13 
ATOM   4844  C CG2 . VAL D  2 93  ? 42.991  -65.963  27.538  1.000 57.572  0 93  VAL DDD CG2 1 ? 13 
ATOM   4845  N N   . TYR D  2 94  ? 44.105  -68.709  23.856  1.000 51.734  0 94  TYR DDD N   1 ? 13 
ATOM   4846  C CA  . TYR D  2 94  ? 43.936  -69.477  22.601  1.000 50.631  0 94  TYR DDD CA  1 ? 13 
ATOM   4847  C C   . TYR D  2 94  ? 42.714  -70.375  22.775  1.000 50.356  0 94  TYR DDD C   1 ? 13 
ATOM   4848  O O   . TYR D  2 94  ? 42.660  -71.140  23.759  1.000 51.656  0 94  TYR DDD O   1 ? 13 
ATOM   4849  C CB  . TYR D  2 94  ? 45.209  -70.244  22.246  1.000 51.299  0 94  TYR DDD CB  1 ? 13 
ATOM   4850  C CG  . TYR D  2 94  ? 46.291  -69.373  21.659  1.000 55.286  0 94  TYR DDD CG  1 ? 13 
ATOM   4851  C CD1 . TYR D  2 94  ? 47.002  -68.483  22.450  1.000 58.353  0 94  TYR DDD CD1 1 ? 13 
ATOM   4852  C CD2 . TYR D  2 94  ? 46.582  -69.402  20.306  1.000 55.728  0 94  TYR DDD CD2 1 ? 13 
ATOM   4853  C CE1 . TYR D  2 94  ? 47.983  -67.663  21.920  1.000 59.757  0 94  TYR DDD CE1 1 ? 13 
ATOM   4854  C CE2 . TYR D  2 94  ? 47.554  -68.576  19.758  1.000 58.362  0 94  TYR DDD CE2 1 ? 13 
ATOM   4855  C CZ  . TYR D  2 94  ? 48.258  -67.700  20.568  1.000 60.030  0 94  TYR DDD CZ  1 ? 13 
ATOM   4856  O OH  . TYR D  2 94  ? 49.218  -66.885  20.037  1.000 61.773  0 94  TYR DDD OH  1 ? 13 
ATOM   4857  N N   . PHE D  2 95  ? 41.741  -70.218  21.875  1.000 48.863  0 95  PHE DDD N   1 ? 13 
ATOM   4858  C CA  . PHE D  2 95  ? 40.455  -70.961  21.853  1.000 47.106  0 95  PHE DDD CA  1 ? 13 
ATOM   4859  C C   . PHE D  2 95  ? 40.470  -71.959  20.703  1.000 47.300  0 95  PHE DDD C   1 ? 13 
ATOM   4860  O O   . PHE D  2 95  ? 40.773  -71.616  19.534  1.000 48.541  0 95  PHE DDD O   1 ? 13 
ATOM   4861  C CB  . PHE D  2 95  ? 39.255  -70.035  21.628  1.000 46.405  0 95  PHE DDD CB  1 ? 13 
ATOM   4862  C CG  . PHE D  2 95  ? 39.062  -69.026  22.727  1.000 47.995  0 95  PHE DDD CG  1 ? 13 
ATOM   4863  C CD1 . PHE D  2 95  ? 39.696  -67.797  22.683  1.000 50.201  0 95  PHE DDD CD1 1 ? 13 
ATOM   4864  C CD2 . PHE D  2 95  ? 38.221  -69.293  23.789  1.000 48.247  0 95  PHE DDD CD2 1 ? 13 
ATOM   4865  C CE1 . PHE D  2 95  ? 39.481  -66.856  23.674  1.000 52.251  0 95  PHE DDD CE1 1 ? 13 
ATOM   4866  C CE2 . PHE D  2 95  ? 38.042  -68.370  24.804  1.000 49.652  0 95  PHE DDD CE2 1 ? 13 
ATOM   4867  C CZ  . PHE D  2 95  ? 38.630  -67.137  24.721  1.000 51.812  0 95  PHE DDD CZ  1 ? 13 
ATOM   4868  N N   . CYS D  2 96  ? 40.099  -73.175  21.046  1.000 46.549  0 96  CYS DDD N   1 ? 13 
ATOM   4869  C CA  . CYS D  2 96  ? 39.728  -74.248  20.100  1.000 46.620  0 96  CYS DDD CA  1 ? 13 
ATOM   4870  C C   . CYS D  2 96  ? 38.309  -73.982  19.593  1.000 43.772  0 96  CYS DDD C   1 ? 13 
ATOM   4871  O O   . CYS D  2 96  ? 37.455  -73.571  20.398  1.000 42.668  0 96  CYS DDD O   1 ? 13 
ATOM   4872  C CB  . CYS D  2 96  ? 39.824  -75.564  20.853  1.000 49.602  0 96  CYS DDD CB  1 ? 13 
ATOM   4873  S SG  . CYS D  2 96  ? 39.561  -77.007  19.812  1.000 55.420  0 96  CYS DDD SG  1 ? 13 
ATOM   4874  N N   . ALA D  2 97  ? 38.040  -74.202  18.320  1.000 42.825  0 97  ALA DDD N   1 ? 13 
ATOM   4875  C CA  . ALA D  2 97  ? 36.657  -74.126  17.793  1.000 42.963  0 97  ALA DDD CA  1 ? 13 
ATOM   4876  C C   . ALA D  2 97  ? 36.423  -75.254  16.780  1.000 41.794  0 97  ALA DDD C   1 ? 13 
ATOM   4877  O O   . ALA D  2 97  ? 37.397  -75.763  16.191  1.000 39.077  0 97  ALA DDD O   1 ? 13 
ATOM   4878  C CB  . ALA D  2 97  ? 36.393  -72.768  17.193  1.000 43.530  0 97  ALA DDD CB  1 ? 13 
ATOM   4879  N N   . ALA D  2 98  ? 35.157  -75.608  16.581  1.000 41.310  0 98  ALA DDD N   1 ? 13 
ATOM   4880  C CA  . ALA D  2 98  ? 34.740  -76.709  15.688  1.000 41.006  0 98  ALA DDD CA  1 ? 13 
ATOM   4881  C C   . ALA D  2 98  ? 33.411  -76.380  15.013  1.000 39.849  0 98  ALA DDD C   1 ? 13 
ATOM   4882  O O   . ALA D  2 98  ? 32.544  -75.730  15.647  1.000 39.009  0 98  ALA DDD O   1 ? 13 
ATOM   4883  C CB  . ALA D  2 98  ? 34.647  -77.986  16.488  1.000 40.774  0 98  ALA DDD CB  1 ? 13 
ATOM   4884  N N   . ASP D  2 99  ? 33.253  -76.883  13.792  1.000 40.135  0 99  ASP DDD N   1 ? 13 
ATOM   4885  C CA  . ASP D  2 99  ? 31.986  -76.806  13.024  1.000 42.375  0 99  ASP DDD CA  1 ? 13 
ATOM   4886  C C   . ASP D  2 99  ? 31.920  -77.949  12.009  1.000 43.098  0 99  ASP DDD C   1 ? 13 
ATOM   4887  O O   . ASP D  2 99  ? 32.978  -78.356  11.511  1.000 41.928  0 99  ASP DDD O   1 ? 13 
ATOM   4888  C CB  . ASP D  2 99  ? 31.828  -75.453  12.327  1.000 41.926  0 99  ASP DDD CB  1 ? 13 
ATOM   4889  C CG  . ASP D  2 99  ? 30.367  -75.155  12.080  1.000 44.461  0 99  ASP DDD CG  1 ? 13 
ATOM   4890  O OD1 . ASP D  2 99  ? 29.703  -74.724  13.030  1.000 44.247  0 99  ASP DDD OD1 1 ? 13 
ATOM   4891  O OD2 . ASP D  2 99  ? 29.889  -75.409  10.938  1.000 46.828  0 99  ASP DDD OD2 1 ? 13 
ATOM   4892  N N   . ARG D  2 100 ? 30.716  -78.422  11.705  1.000 44.960  0 100 ARG DDD N   1 ? 14 
ATOM   4893  C CA  . ARG D  2 100 ? 30.502  -79.441  10.644  1.000 47.403  0 100 ARG DDD CA  1 ? 14 
ATOM   4894  C C   . ARG D  2 100 ? 30.883  -78.838  9.283   1.000 44.397  0 100 ARG DDD C   1 ? 14 
ATOM   4895  O O   . ARG D  2 100 ? 31.372  -79.571  8.421   1.000 44.252  0 100 ARG DDD O   1 ? 14 
ATOM   4896  C CB  . ARG D  2 100 ? 29.040  -79.888  10.621  1.000 51.963  0 100 ARG DDD CB  1 ? 14 
ATOM   4897  C CG  . ARG D  2 100 ? 28.594  -80.614  11.873  1.000 55.462  0 100 ARG DDD CG  1 ? 14 
ATOM   4898  C CD  . ARG D  2 100 ? 29.085  -82.051  11.814  1.000 59.351  0 100 ARG DDD CD  1 ? 14 
ATOM   4899  N NE  . ARG D  2 100 ? 28.348  -82.696  10.733  1.000 62.667  0 100 ARG DDD NE  1 ? 14 
ATOM   4900  C CZ  . ARG D  2 100 ? 27.177  -83.345  10.847  1.000 67.124  0 100 ARG DDD CZ  1 ? 14 
ATOM   4901  N NH1 . ARG D  2 100 ? 26.561  -83.489  12.013  1.000 68.287  0 100 ARG DDD NH1 1 ? 14 
ATOM   4902  N NH2 . ARG D  2 100 ? 26.623  -83.874  9.774   1.000 68.730  0 100 ARG DDD NH2 1 ? 14 
ATOM   4903  N N   . GLY D  2 101 ? 30.649  -77.544  9.106   1.000 41.938  0 101 GLY DDD N   1 ? 14 
ATOM   4904  C CA  . GLY D  2 101 ? 30.821  -76.847  7.824   1.000 42.236  0 101 GLY DDD CA  1 ? 14 
ATOM   4905  C C   . GLY D  2 101 ? 32.166  -76.145  7.742   1.000 41.147  0 101 GLY DDD C   1 ? 14 
ATOM   4906  O O   . GLY D  2 101 ? 32.669  -75.644  8.780   1.000 40.882  0 101 GLY DDD O   1 ? 14 
ATOM   4907  N N   . GLU D  2 102 ? 32.731  -76.131  6.541   1.000 40.428  0 102 GLU DDD N   1 ? 14 
ATOM   4908  C CA  . GLU D  2 102 ? 33.911  -75.313  6.189   1.000 40.740  0 102 GLU DDD CA  1 ? 14 
ATOM   4909  C C   . GLU D  2 102 ? 33.405  -74.034  5.534   1.000 41.955  0 102 GLU DDD C   1 ? 14 
ATOM   4910  O O   . GLU D  2 102 ? 32.692  -74.137  4.497   1.000 43.195  0 102 GLU DDD O   1 ? 14 
ATOM   4911  C CB  . GLU D  2 102 ? 34.820  -76.091  5.245   1.000 41.621  0 102 GLU DDD CB  1 ? 14 
ATOM   4912  C CG  . GLU D  2 102 ? 36.145  -75.412  5.007   1.000 41.267  0 102 GLU DDD CG  1 ? 14 
ATOM   4913  C CD  . GLU D  2 102 ? 37.092  -76.193  4.137   1.000 43.488  0 102 GLU DDD CD  1 ? 14 
ATOM   4914  O OE1 . GLU D  2 102 ? 36.936  -77.393  4.081   1.000 47.154  0 102 GLU DDD OE1 1 ? 14 
ATOM   4915  O OE2 . GLU D  2 102 ? 37.929  -75.575  3.466   1.000 47.772  0 102 GLU DDD OE2 1 ? 14 
ATOM   4916  N N   . SER D  2 103 ? 33.745  -72.879  6.119   1.000 40.795  0 103 SER DDD N   1 ? 14 
ATOM   4917  C CA  . SER D  2 103 ? 33.269  -71.556  5.655   1.000 39.886  0 103 SER DDD CA  1 ? 14 
ATOM   4918  C C   . SER D  2 103 ? 34.221  -70.976  4.607   1.000 39.624  0 103 SER DDD C   1 ? 14 
ATOM   4919  O O   . SER D  2 103 ? 35.437  -71.028  4.775   1.000 40.206  0 103 SER DDD O   1 ? 14 
ATOM   4920  C CB  . SER D  2 103 ? 33.110  -70.609  6.804   1.000 41.066  0 103 SER DDD CB  1 ? 14 
ATOM   4921  O OG  . SER D  2 103 ? 32.617  -69.359  6.345   1.000 39.171  0 103 SER DDD OG  1 ? 14 
ATOM   4922  N N   . TYR D  2 104 ? 33.665  -70.389  3.563   1.000 41.358  0 104 TYR DDD N   1 ? 14 
ATOM   4923  C CA  . TYR D  2 104 ? 34.386  -69.441  2.701   1.000 42.557  0 104 TYR DDD CA  1 ? 14 
ATOM   4924  C C   . TYR D  2 104 ? 34.942  -68.328  3.585   1.000 42.447  0 104 TYR DDD C   1 ? 14 
ATOM   4925  O O   . TYR D  2 104 ? 36.054  -67.887  3.293   1.000 43.718  0 104 TYR DDD O   1 ? 14 
ATOM   4926  C CB  . TYR D  2 104 ? 33.470  -68.849  1.631   1.000 44.659  0 104 TYR DDD CB  1 ? 14 
ATOM   4927  C CG  . TYR D  2 104 ? 34.205  -67.932  0.688   1.000 46.333  0 104 TYR DDD CG  1 ? 14 
ATOM   4928  C CD1 . TYR D  2 104 ? 35.171  -68.436  -0.163  1.000 46.421  0 104 TYR DDD CD1 1 ? 14 
ATOM   4929  C CD2 . TYR D  2 104 ? 33.986  -66.564  0.693   1.000 46.370  0 104 TYR DDD CD2 1 ? 14 
ATOM   4930  C CE1 . TYR D  2 104 ? 35.835  -67.621  -1.051  1.000 48.798  0 104 TYR DDD CE1 1 ? 14 
ATOM   4931  C CE2 . TYR D  2 104 ? 34.662  -65.727  -0.171  1.000 48.141  0 104 TYR DDD CE2 1 ? 14 
ATOM   4932  C CZ  . TYR D  2 104 ? 35.577  -66.261  -1.059  1.000 50.664  0 104 TYR DDD CZ  1 ? 14 
ATOM   4933  O OH  . TYR D  2 104 ? 36.274  -65.448  -1.917  1.000 54.222  0 104 TYR DDD OH  1 ? 14 
ATOM   4934  N N   . TYR D  2 105 ? 34.192  -67.883  4.605   1.000 42.323  0 105 TYR DDD N   1 ? 14 
ATOM   4935  C CA  . TYR D  2 105 ? 34.595  -66.802  5.548   1.000 42.403  0 105 TYR DDD CA  1 ? 14 
ATOM   4936  C C   . TYR D  2 105 ? 35.163  -67.462  6.815   1.000 42.330  0 105 TYR DDD C   1 ? 14 
ATOM   4937  O O   . TYR D  2 105 ? 34.666  -67.233  7.947   1.000 43.049  0 105 TYR DDD O   1 ? 14 
ATOM   4938  C CB  . TYR D  2 105 ? 33.417  -65.859  5.825   1.000 41.745  0 105 TYR DDD CB  1 ? 14 
ATOM   4939  C CG  . TYR D  2 105 ? 32.667  -65.333  4.618   1.000 42.754  0 105 TYR DDD CG  1 ? 14 
ATOM   4940  C CD1 . TYR D  2 105 ? 33.239  -64.412  3.757   1.000 43.458  0 105 TYR DDD CD1 1 ? 14 
ATOM   4941  C CD2 . TYR D  2 105 ? 31.348  -65.703  4.362   1.000 42.537  0 105 TYR DDD CD2 1 ? 14 
ATOM   4942  C CE1 . TYR D  2 105 ? 32.542  -63.905  2.663   1.000 44.699  0 105 TYR DDD CE1 1 ? 14 
ATOM   4943  C CE2 . TYR D  2 105 ? 30.648  -65.218  3.270   1.000 43.005  0 105 TYR DDD CE2 1 ? 14 
ATOM   4944  C CZ  . TYR D  2 105 ? 31.238  -64.302  2.418   1.000 43.813  0 105 TYR DDD CZ  1 ? 14 
ATOM   4945  O OH  . TYR D  2 105 ? 30.579  -63.817  1.327   1.000 46.416  0 105 TYR DDD OH  1 ? 14 
ATOM   4946  N N   . TYR D  2 106 ? 36.220  -68.259  6.641   1.000 42.730  0 106 TYR DDD N   1 ? 14 
ATOM   4947  C CA  . TYR D  2 106 ? 36.792  -69.138  7.689   1.000 44.170  0 106 TYR DDD CA  1 ? 14 
ATOM   4948  C C   . TYR D  2 106 ? 37.354  -68.328  8.858   1.000 44.923  0 106 TYR DDD C   1 ? 14 
ATOM   4949  O O   . TYR D  2 106 ? 37.580  -68.954  9.908   1.000 47.104  0 106 TYR DDD O   1 ? 14 
ATOM   4950  C CB  . TYR D  2 106 ? 37.882  -70.050  7.130   1.000 45.940  0 106 TYR DDD CB  1 ? 14 
ATOM   4951  C CG  . TYR D  2 106 ? 39.003  -69.335  6.429   1.000 48.698  0 106 TYR DDD CG  1 ? 14 
ATOM   4952  C CD1 . TYR D  2 106 ? 40.060  -68.770  7.128   1.000 49.697  0 106 TYR DDD CD1 1 ? 14 
ATOM   4953  C CD2 . TYR D  2 106 ? 39.004  -69.239  5.054   1.000 48.405  0 106 TYR DDD CD2 1 ? 14 
ATOM   4954  C CE1 . TYR D  2 106 ? 41.082  -68.112  6.474   1.000 50.070  0 106 TYR DDD CE1 1 ? 14 
ATOM   4955  C CE2 . TYR D  2 106 ? 40.009  -68.563  4.383   1.000 50.338  0 106 TYR DDD CE2 1 ? 14 
ATOM   4956  C CZ  . TYR D  2 106 ? 41.056  -68.013  5.097   1.000 51.943  0 106 TYR DDD CZ  1 ? 14 
ATOM   4957  O OH  . TYR D  2 106 ? 42.045  -67.371  4.415   1.000 54.051  0 106 TYR DDD OH  1 ? 14 
ATOM   4958  N N   . THR D  2 107 ? 37.581  -67.023  8.708   1.000 50.388  0 107 THR DDD N   1 ? 15 
ATOM   4959  C CA  . THR D  2 107 ? 38.104  -66.154  9.810   1.000 50.088  0 107 THR DDD CA  1 ? 15 
ATOM   4960  C C   . THR D  2 107 ? 36.964  -65.626  10.687  1.000 48.324  0 107 THR DDD C   1 ? 15 
ATOM   4961  O O   . THR D  2 107 ? 37.272  -65.037  11.722  1.000 49.700  0 107 THR DDD O   1 ? 15 
ATOM   4962  C CB  . THR D  2 107 ? 38.953  -64.981  9.293   1.000 50.047  0 107 THR DDD CB  1 ? 15 
ATOM   4963  O OG1 . THR D  2 107 ? 38.108  -64.021  8.691   1.000 52.013  0 107 THR DDD OG1 1 ? 15 
ATOM   4964  C CG2 . THR D  2 107 ? 39.985  -65.389  8.272   1.000 50.191  0 107 THR DDD CG2 1 ? 15 
ATOM   4965  N N   . ARG D  2 108 ? 35.699  -65.810  10.313  1.000 47.127  0 108 ARG DDD N   1 ? 15 
ATOM   4966  C CA  . ARG D  2 108 ? 34.557  -65.305  11.133  1.000 46.645  0 108 ARG DDD CA  1 ? 15 
ATOM   4967  C C   . ARG D  2 108 ? 34.271  -66.234  12.313  1.000 44.876  0 108 ARG DDD C   1 ? 15 
ATOM   4968  O O   . ARG D  2 108 ? 33.937  -67.404  12.117  1.000 43.092  0 108 ARG DDD O   1 ? 15 
ATOM   4969  C CB  . ARG D  2 108 ? 33.256  -65.223  10.331  1.000 47.568  0 108 ARG DDD CB  1 ? 15 
ATOM   4970  C CG  . ARG D  2 108 ? 33.237  -64.141  9.277   1.000 48.715  0 108 ARG DDD CG  1 ? 15 
ATOM   4971  C CD  . ARG D  2 108 ? 31.838  -64.049  8.720   1.000 49.795  0 108 ARG DDD CD  1 ? 15 
ATOM   4972  N NE  . ARG D  2 108 ? 31.841  -63.225  7.526   1.000 51.505  0 108 ARG DDD NE  1 ? 15 
ATOM   4973  C CZ  . ARG D  2 108 ? 30.835  -63.116  6.682   1.000 53.546  0 108 ARG DDD CZ  1 ? 15 
ATOM   4974  N NH1 . ARG D  2 108 ? 29.729  -63.809  6.871   1.000 55.651  0 108 ARG DDD NH1 1 ? 15 
ATOM   4975  N NH2 . ARG D  2 108 ? 30.948  -62.334  5.631   1.000 54.846  0 108 ARG DDD NH2 1 ? 15 
ATOM   4976  N N   . PRO D  2 109 ? 34.349  -65.736  13.562  1.000 44.606  0 109 PRO DDD N   1 ? 15 
ATOM   4977  C CA  . PRO D  2 109 ? 33.904  -66.511  14.716  1.000 44.017  0 109 PRO DDD CA  1 ? 15 
ATOM   4978  C C   . PRO D  2 109 ? 32.479  -67.102  14.584  1.000 44.401  0 109 PRO DDD C   1 ? 15 
ATOM   4979  O O   . PRO D  2 109 ? 32.284  -68.244  15.011  1.000 43.362  0 109 PRO DDD O   1 ? 15 
ATOM   4980  C CB  . PRO D  2 109 ? 33.969  -65.508  15.882  1.000 43.097  0 109 PRO DDD CB  1 ? 15 
ATOM   4981  C CG  . PRO D  2 109 ? 34.644  -64.244  15.390  1.000 43.668  0 109 PRO DDD CG  1 ? 15 
ATOM   4982  C CD  . PRO D  2 109 ? 34.908  -64.425  13.919  1.000 44.269  0 109 PRO DDD CD  1 ? 15 
ATOM   4983  N N   . THR D  2 110 ? 31.533  -66.345  14.000  1.000 45.785  0 110 THR DDD N   1 ? 15 
ATOM   4984  C CA  . THR D  2 110 ? 30.103  -66.763  13.862  1.000 46.366  0 110 THR DDD CA  1 ? 15 
ATOM   4985  C C   . THR D  2 110 ? 29.964  -68.000  12.964  1.000 45.101  0 110 THR DDD C   1 ? 15 
ATOM   4986  O O   . THR D  2 110 ? 28.920  -68.634  13.050  1.000 46.206  0 110 THR DDD O   1 ? 15 
ATOM   4987  C CB  . THR D  2 110 ? 29.216  -65.627  13.350  1.000 48.385  0 110 THR DDD CB  1 ? 15 
ATOM   4988  O OG1 . THR D  2 110 ? 29.758  -65.129  12.127  1.000 50.771  0 110 THR DDD OG1 1 ? 15 
ATOM   4989  C CG2 . THR D  2 110 ? 29.088  -64.503  14.356  1.000 48.987  0 110 THR DDD CG2 1 ? 15 
ATOM   4990  N N   . GLU D  2 111 ? 30.981  -68.365  12.170  1.000 45.206  0 111 GLU DDD N   1 ? 15 
ATOM   4991  C CA  . GLU D  2 111 ? 30.922  -69.570  11.308  1.000 44.511  0 111 GLU DDD CA  1 ? 15 
ATOM   4992  C C   . GLU D  2 111 ? 31.250  -70.846  12.099  1.000 44.652  0 111 GLU DDD C   1 ? 15 
ATOM   4993  O O   . GLU D  2 111 ? 31.155  -71.945  11.506  1.000 45.588  0 111 GLU DDD O   1 ? 15 
ATOM   4994  C CB  . GLU D  2 111 ? 31.842  -69.383  10.103  1.000 44.497  0 111 GLU DDD CB  1 ? 15 
ATOM   4995  C CG  . GLU D  2 111 ? 31.335  -68.344  9.103   1.000 45.272  0 111 GLU DDD CG  1 ? 15 
ATOM   4996  C CD  . GLU D  2 111 ? 30.067  -68.744  8.342   1.000 46.045  0 111 GLU DDD CD  1 ? 15 
ATOM   4997  O OE1 . GLU D  2 111 ? 28.993  -68.799  8.975   1.000 45.105  0 111 GLU DDD OE1 1 ? 15 
ATOM   4998  O OE2 . GLU D  2 111 ? 30.151  -69.053  7.122   1.000 48.143  0 111 GLU DDD OE2 1 ? 15 
ATOM   4999  N N   . TYR D  2 112 ? 31.628  -70.754  13.377  1.000 45.040  0 112 TYR DDD N   1 ? 15 
ATOM   5000  C CA  . TYR D  2 112 ? 31.977  -71.947  14.204  1.000 44.210  0 112 TYR DDD CA  1 ? 15 
ATOM   5001  C C   . TYR D  2 112 ? 30.991  -72.078  15.371  1.000 43.993  0 112 TYR DDD C   1 ? 15 
ATOM   5002  O O   . TYR D  2 112 ? 30.884  -71.171  16.191  1.000 43.361  0 112 TYR DDD O   1 ? 15 
ATOM   5003  C CB  . TYR D  2 112 ? 33.431  -71.837  14.662  1.000 42.896  0 112 TYR DDD CB  1 ? 15 
ATOM   5004  C CG  . TYR D  2 112 ? 34.402  -71.738  13.521  1.000 42.460  0 112 TYR DDD CG  1 ? 15 
ATOM   5005  C CD1 . TYR D  2 112 ? 34.695  -70.514  12.959  1.000 42.236  0 112 TYR DDD CD1 1 ? 15 
ATOM   5006  C CD2 . TYR D  2 112 ? 35.050  -72.860  13.030  1.000 42.436  0 112 TYR DDD CD2 1 ? 15 
ATOM   5007  C CE1 . TYR D  2 112 ? 35.606  -70.405  11.924  1.000 42.801  0 112 TYR DDD CE1 1 ? 15 
ATOM   5008  C CE2 . TYR D  2 112 ? 35.960  -72.764  11.989  1.000 42.981  0 112 TYR DDD CE2 1 ? 15 
ATOM   5009  C CZ  . TYR D  2 112 ? 36.232  -71.530  11.423  1.000 42.446  0 112 TYR DDD CZ  1 ? 15 
ATOM   5010  O OH  . TYR D  2 112 ? 37.144  -71.418  10.413  1.000 41.985  0 112 TYR DDD OH  1 ? 15 
ATOM   5011  N N   . GLU D  2 113 ? 30.270  -73.186  15.443  1.000 44.666  0 113 GLU DDD N   1 ? 15 
ATOM   5012  C CA  . GLU D  2 113 ? 29.222  -73.379  16.471  1.000 45.595  0 113 GLU DDD CA  1 ? 15 
ATOM   5013  C C   . GLU D  2 113 ? 29.847  -73.652  17.844  1.000 46.070  0 113 GLU DDD C   1 ? 15 
ATOM   5014  O O   . GLU D  2 113 ? 29.286  -73.180  18.822  1.000 49.049  0 113 GLU DDD O   1 ? 15 
ATOM   5015  C CB  . GLU D  2 113 ? 28.298  -74.528  16.102  1.000 47.889  0 113 GLU DDD CB  1 ? 15 
ATOM   5016  C CG  . GLU D  2 113 ? 27.167  -74.684  17.094  1.000 50.992  0 113 GLU DDD CG  1 ? 15 
ATOM   5017  C CD  . GLU D  2 113 ? 26.111  -75.707  16.729  1.000 54.095  0 113 GLU DDD CD  1 ? 15 
ATOM   5018  O OE1 . GLU D  2 113 ? 26.192  -76.259  15.624  1.000 58.654  0 113 GLU DDD OE1 1 ? 15 
ATOM   5019  O OE2 . GLU D  2 113 ? 25.227  -75.960  17.570  1.000 57.968  0 113 GLU DDD OE2 1 ? 15 
ATOM   5020  N N   . PHE D  2 114 ? 30.929  -74.422  17.929  1.000 45.676  0 114 PHE DDD N   1 ? 15 
ATOM   5021  C CA  . PHE D  2 114 ? 31.484  -74.965  19.204  1.000 45.231  0 114 PHE DDD CA  1 ? 15 
ATOM   5022  C C   . PHE D  2 114 ? 32.813  -74.295  19.543  1.000 45.202  0 114 PHE DDD C   1 ? 15 
ATOM   5023  O O   . PHE D  2 114 ? 33.687  -74.186  18.663  1.000 45.874  0 114 PHE DDD O   1 ? 15 
ATOM   5024  C CB  . PHE D  2 114 ? 31.659  -76.479  19.099  1.000 44.838  0 114 PHE DDD CB  1 ? 15 
ATOM   5025  C CG  . PHE D  2 114 ? 30.343  -77.162  18.838  1.000 45.257  0 114 PHE DDD CG  1 ? 15 
ATOM   5026  C CD1 . PHE D  2 114 ? 29.323  -77.085  19.785  1.000 44.369  0 114 PHE DDD CD1 1 ? 15 
ATOM   5027  C CD2 . PHE D  2 114 ? 30.104  -77.844  17.648  1.000 44.480  0 114 PHE DDD CD2 1 ? 15 
ATOM   5028  C CE1 . PHE D  2 114 ? 28.104  -77.689  19.560  1.000 43.972  0 114 PHE DDD CE1 1 ? 15 
ATOM   5029  C CE2 . PHE D  2 114 ? 28.874  -78.446  17.427  1.000 44.115  0 114 PHE DDD CE2 1 ? 15 
ATOM   5030  C CZ  . PHE D  2 114 ? 27.881  -78.368  18.386  1.000 44.796  0 114 PHE DDD CZ  1 ? 15 
ATOM   5031  N N   . TRP D  2 115 ? 32.949  -73.880  20.802  1.000 46.769  0 115 TRP DDD N   1 ? 15 
ATOM   5032  C CA  . TRP D  2 115 ? 34.127  -73.138  21.338  1.000 46.140  0 115 TRP DDD CA  1 ? 15 
ATOM   5033  C C   . TRP D  2 115 ? 34.591  -73.756  22.655  1.000 44.087  0 115 TRP DDD C   1 ? 15 
ATOM   5034  O O   . TRP D  2 115 ? 33.741  -73.947  23.554  1.000 40.441  0 115 TRP DDD O   1 ? 15 
ATOM   5035  C CB  . TRP D  2 115 ? 33.770  -71.664  21.517  1.000 46.888  0 115 TRP DDD CB  1 ? 15 
ATOM   5036  C CG  . TRP D  2 115 ? 33.575  -70.981  20.197  1.000 48.686  0 115 TRP DDD CG  1 ? 15 
ATOM   5037  C CD1 . TRP D  2 115 ? 32.462  -71.011  19.408  1.000 47.427  0 115 TRP DDD CD1 1 ? 15 
ATOM   5038  C CD2 . TRP D  2 115 ? 34.546  -70.196  19.491  1.000 48.112  0 115 TRP DDD CD2 1 ? 15 
ATOM   5039  N NE1 . TRP D  2 115 ? 32.672  -70.292  18.269  1.000 47.807  0 115 TRP DDD NE1 1 ? 15 
ATOM   5040  C CE2 . TRP D  2 115 ? 33.932  -69.762  18.294  1.000 49.083  0 115 TRP DDD CE2 1 ? 15 
ATOM   5041  C CE3 . TRP D  2 115 ? 35.836  -69.763  19.788  1.000 49.403  0 115 TRP DDD CE3 1 ? 15 
ATOM   5042  C CZ2 . TRP D  2 115 ? 34.584  -68.951  17.368  1.000 49.606  0 115 TRP DDD CZ2 1 ? 15 
ATOM   5043  C CZ3 . TRP D  2 115 ? 36.491  -68.959  18.876  1.000 51.099  0 115 TRP DDD CZ3 1 ? 15 
ATOM   5044  C CH2 . TRP D  2 115 ? 35.876  -68.571  17.673  1.000 50.809  0 115 TRP DDD CH2 1 ? 15 
ATOM   5045  N N   . GLY D  2 116 ? 35.898  -73.996  22.783  1.000 43.452  0 116 GLY DDD N   1 ? 15 
ATOM   5046  C CA  . GLY D  2 116 ? 36.524  -74.296  24.086  1.000 44.265  0 116 GLY DDD CA  1 ? 15 
ATOM   5047  C C   . GLY D  2 116 ? 36.505  -73.064  24.975  1.000 44.459  0 116 GLY DDD C   1 ? 15 
ATOM   5048  O O   . GLY D  2 116 ? 36.133  -71.979  24.470  1.000 46.613  0 116 GLY DDD O   1 ? 15 
ATOM   5049  N N   . GLN D  2 117 ? 36.911  -73.205  26.235  1.000 44.727  0 117 GLN DDD N   1 ? 15 
ATOM   5050  C CA  . GLN D  2 117 ? 36.962  -72.094  27.223  1.000 44.666  0 117 GLN DDD CA  1 ? 15 
ATOM   5051  C C   . GLN D  2 117 ? 38.258  -71.292  27.026  1.000 45.747  0 117 GLN DDD C   1 ? 15 
ATOM   5052  O O   . GLN D  2 117 ? 38.327  -70.154  27.525  1.000 47.022  0 117 GLN DDD O   1 ? 15 
ATOM   5053  C CB  . GLN D  2 117 ? 36.910  -72.630  28.655  1.000 43.685  0 117 GLN DDD CB  1 ? 15 
ATOM   5054  C CG  . GLN D  2 117 ? 35.694  -73.486  28.938  1.000 43.809  0 117 GLN DDD CG  1 ? 15 
ATOM   5055  C CD  . GLN D  2 117 ? 34.398  -72.733  28.754  1.000 43.984  0 117 GLN DDD CD  1 ? 15 
ATOM   5056  O OE1 . GLN D  2 117 ? 33.458  -73.242  28.160  1.000 45.898  0 117 GLN DDD OE1 1 ? 15 
ATOM   5057  N NE2 . GLN D  2 117 ? 34.318  -71.521  29.268  1.000 43.197  0 117 GLN DDD NE2 1 ? 15 
ATOM   5058  N N   . GLY D  2 118 ? 39.245  -71.864  26.335  1.000 46.905  0 118 GLY DDD N   1 ? 15 
ATOM   5059  C CA  . GLY D  2 118 ? 40.535  -71.215  26.039  1.000 48.714  0 118 GLY DDD CA  1 ? 15 
ATOM   5060  C C   . GLY D  2 118 ? 41.603  -71.549  27.067  1.000 50.508  0 118 GLY DDD C   1 ? 15 
ATOM   5061  O O   . GLY D  2 118 ? 41.250  -71.969  28.175  1.000 49.853  0 118 GLY DDD O   1 ? 15 
ATOM   5062  N N   . THR D  2 119 ? 42.871  -71.359  26.702  1.000 52.235  0 119 THR DDD N   1 ? 15 
ATOM   5063  C CA  . THR D  2 119 ? 44.055  -71.590  27.558  1.000 53.324  0 119 THR DDD CA  1 ? 15 
ATOM   5064  C C   . THR D  2 119 ? 45.030  -70.438  27.324  1.000 53.986  0 119 THR DDD C   1 ? 15 
ATOM   5065  O O   . THR D  2 119 ? 45.196  -70.022  26.156  1.000 55.568  0 119 THR DDD O   1 ? 15 
ATOM   5066  C CB  . THR D  2 119 ? 44.632  -72.981  27.273  1.000 56.124  0 119 THR DDD CB  1 ? 15 
ATOM   5067  O OG1 . THR D  2 119 ? 45.527  -73.319  28.334  1.000 58.616  0 119 THR DDD OG1 1 ? 15 
ATOM   5068  C CG2 . THR D  2 119 ? 45.332  -73.075  25.927  1.000 56.778  0 119 THR DDD CG2 1 ? 15 
ATOM   5069  N N   . GLN D  2 120 ? 45.631  -69.931  28.399  1.000 54.566  0 120 GLN DDD N   1 ? 15 
ATOM   5070  C CA  . GLN D  2 120 ? 46.596  -68.808  28.357  1.000 55.089  0 120 GLN DDD CA  1 ? 15 
ATOM   5071  C C   . GLN D  2 120 ? 47.913  -69.323  27.753  1.000 56.649  0 120 GLN DDD C   1 ? 15 
ATOM   5072  O O   . GLN D  2 120 ? 48.422  -70.374  28.186  1.000 56.048  0 120 GLN DDD O   1 ? 15 
ATOM   5073  C CB  . GLN D  2 120 ? 46.784  -68.232  29.762  1.000 54.644  0 120 GLN DDD CB  1 ? 15 
ATOM   5074  C CG  . GLN D  2 120 ? 47.630  -66.968  29.800  1.000 55.918  0 120 GLN DDD CG  1 ? 15 
ATOM   5075  C CD  . GLN D  2 120 ? 46.979  -65.807  29.089  1.000 54.814  0 120 GLN DDD CD  1 ? 15 
ATOM   5076  O OE1 . GLN D  2 120 ? 45.831  -65.476  29.342  1.000 53.697  0 120 GLN DDD OE1 1 ? 15 
ATOM   5077  N NE2 . GLN D  2 120 ? 47.725  -65.141  28.228  1.000 56.810  0 120 GLN DDD NE2 1 ? 15 
ATOM   5078  N N   . VAL D  2 121 ? 48.413  -68.604  26.756  1.000 59.304  0 121 VAL DDD N   1 ? 15 
ATOM   5079  C CA  . VAL D  2 121 ? 49.827  -68.637  26.298  1.000 63.269  0 121 VAL DDD CA  1 ? 15 
ATOM   5080  C C   . VAL D  2 121 ? 50.458  -67.287  26.665  1.000 66.479  0 121 VAL DDD C   1 ? 15 
ATOM   5081  O O   . VAL D  2 121 ? 49.886  -66.254  26.287  1.000 66.277  0 121 VAL DDD O   1 ? 15 
ATOM   5082  C CB  . VAL D  2 121 ? 49.903  -68.913  24.790  1.000 62.547  0 121 VAL DDD CB  1 ? 15 
ATOM   5083  C CG1 . VAL D  2 121 ? 51.333  -68.811  24.284  1.000 64.977  0 121 VAL DDD CG1 1 ? 15 
ATOM   5084  C CG2 . VAL D  2 121 ? 49.275  -70.262  24.444  1.000 62.171  0 121 VAL DDD CG2 1 ? 15 
ATOM   5085  N N   . THR D  2 122 ? 51.581  -67.288  27.382  1.000 68.718  0 122 THR DDD N   1 ? 15 
ATOM   5086  C CA  . THR D  2 122 ? 52.324  -66.059  27.749  1.000 72.715  0 122 THR DDD CA  1 ? 15 
ATOM   5087  C C   . THR D  2 122 ? 53.751  -66.183  27.207  1.000 76.077  0 122 THR DDD C   1 ? 15 
ATOM   5088  O O   . THR D  2 122 ? 54.431  -67.183  27.537  1.000 76.547  0 122 THR DDD O   1 ? 15 
ATOM   5089  C CB  . THR D  2 122 ? 52.254  -65.825  29.265  1.000 74.628  0 122 THR DDD CB  1 ? 15 
ATOM   5090  O OG1 . THR D  2 122 ? 50.873  -65.700  29.604  1.000 75.000  0 122 THR DDD OG1 1 ? 15 
ATOM   5091  C CG2 . THR D  2 122 ? 52.988  -64.584  29.728  1.000 77.151  0 122 THR DDD CG2 1 ? 15 
ATOM   5092  N N   . VAL D  2 123 ? 54.170  -65.214  26.394  1.000 78.763  0 123 VAL DDD N   1 ? 15 
ATOM   5093  C CA  . VAL D  2 123 ? 55.546  -65.133  25.821  1.000 82.832  0 123 VAL DDD CA  1 ? 15 
ATOM   5094  C C   . VAL D  2 123 ? 56.250  -63.942  26.493  1.000 87.302  0 123 VAL DDD C   1 ? 15 
ATOM   5095  O O   . VAL D  2 123 ? 55.828  -62.800  26.234  1.000 85.719  0 123 VAL DDD O   1 ? 15 
ATOM   5096  C CB  . VAL D  2 123 ? 55.477  -65.011  24.285  1.000 80.949  0 123 VAL DDD CB  1 ? 15 
ATOM   5097  C CG1 . VAL D  2 123 ? 56.835  -65.153  23.646  1.000 83.291  0 123 VAL DDD CG1 1 ? 15 
ATOM   5098  C CG2 . VAL D  2 123 ? 54.517  -66.025  23.678  1.000 77.638  0 123 VAL DDD CG2 1 ? 15 
ATOM   5099  N N   . SER D  2 124 ? 57.222  -64.193  27.378  1.000 94.063  0 124 SER DDD N   1 ? 15 
ATOM   5100  C CA  . SER D  2 124 ? 58.035  -63.144  28.058  1.000 101.515 0 124 SER DDD CA  1 ? 15 
ATOM   5101  C C   . SER D  2 124 ? 59.166  -62.698  27.125  1.000 111.399 0 124 SER DDD C   1 ? 15 
ATOM   5102  O O   . SER D  2 124 ? 59.473  -63.450  26.201  1.000 113.111 0 124 SER DDD O   1 ? 15 
ATOM   5103  C CB  . SER D  2 124 ? 58.578  -63.633  29.363  1.000 101.741 0 124 SER DDD CB  1 ? 15 
ATOM   5104  O OG  . SER D  2 124 ? 59.370  -64.792  29.160  1.000 102.827 0 124 SER DDD OG  1 ? 15 
ATOM   5105  N N   . SER D  2 125 ? 59.753  -61.522  27.362  1.000 66.407  0 125 SER DDD N   1 ? ?  
ATOM   5106  C CA  . SER D  2 125 ? 60.791  -60.894  26.495  1.000 75.283  0 125 SER DDD CA  1 ? ?  
ATOM   5107  C C   . SER D  2 125 ? 62.150  -60.938  27.202  1.000 78.695  0 125 SER DDD C   1 ? ?  
ATOM   5108  O O   . SER D  2 125 ? 62.877  -61.913  27.034  1.000 86.035  0 125 SER DDD O   1 ? ?  
ATOM   5109  C CB  . SER D  2 125 ? 60.401  -59.484  26.085  1.000 77.710  0 125 SER DDD CB  1 ? ?  
ATOM   5110  O OG  . SER D  2 125 ? 61.071  -58.499  26.862  1.000 84.887  0 125 SER DDD OG  1 ? ?  
ATOM   5111  N N   . ILE E  1 3   ? 24.669  -48.186  23.189  1.000 73.002  0 332 ILE EEE N   1 ? ?  
ATOM   5112  C CA  . ILE E  1 3   ? 23.906  -47.113  22.501  1.000 77.108  0 332 ILE EEE CA  1 ? ?  
ATOM   5113  C C   . ILE E  1 3   ? 23.504  -46.018  23.509  1.000 73.931  0 332 ILE EEE C   1 ? ?  
ATOM   5114  O O   . ILE E  1 3   ? 22.937  -46.362  24.561  1.000 81.115  0 332 ILE EEE O   1 ? ?  
ATOM   5115  C CB  . ILE E  1 3   ? 22.725  -47.749  21.720  1.000 85.744  0 332 ILE EEE CB  1 ? ?  
ATOM   5116  C CG1 . ILE E  1 3   ? 23.217  -48.316  20.376  1.000 82.963  0 332 ILE EEE CG1 1 ? ?  
ATOM   5117  C CG2 . ILE E  1 3   ? 21.548  -46.795  21.509  1.000 84.465  0 332 ILE EEE CG2 1 ? ?  
ATOM   5118  C CD1 . ILE E  1 3   ? 23.124  -49.822  20.214  1.000 78.931  0 332 ILE EEE CD1 1 ? ?  
ATOM   5119  N N   . THR E  1 4   ? 23.862  -44.774  23.190  1.000 106.813 0 333 THR EEE N   1 ? 16 
ATOM   5120  C CA  . THR E  1 4   ? 23.371  -43.461  23.721  1.000 98.428  0 333 THR EEE CA  1 ? 16 
ATOM   5121  C C   . THR E  1 4   ? 24.246  -42.353  23.091  1.000 89.067  0 333 THR EEE C   1 ? 16 
ATOM   5122  O O   . THR E  1 4   ? 23.732  -41.290  22.659  1.000 84.779  0 333 THR EEE O   1 ? 16 
ATOM   5123  C CB  . THR E  1 4   ? 23.428  -43.337  25.255  1.000 102.131 0 333 THR EEE CB  1 ? 16 
ATOM   5124  O OG1 . THR E  1 4   ? 24.582  -44.092  25.635  1.000 101.241 0 333 THR EEE OG1 1 ? 16 
ATOM   5125  C CG2 . THR E  1 4   ? 22.175  -43.809  25.967  1.000 104.090 0 333 THR EEE CG2 1 ? 16 
ATOM   5126  N N   . ASN E  1 5   ? 25.556  -42.588  23.063  1.000 84.060  0 334 ASN EEE N   1 ? 16 
ATOM   5127  C CA  . ASN E  1 5   ? 26.589  -41.686  22.485  1.000 80.356  0 334 ASN EEE CA  1 ? 16 
ATOM   5128  C C   . ASN E  1 5   ? 26.520  -41.734  20.954  1.000 72.752  0 334 ASN EEE C   1 ? 16 
ATOM   5129  O O   . ASN E  1 5   ? 26.443  -42.838  20.393  1.000 67.741  0 334 ASN EEE O   1 ? 16 
ATOM   5130  C CB  . ASN E  1 5   ? 27.984  -42.083  22.962  1.000 83.389  0 334 ASN EEE CB  1 ? 16 
ATOM   5131  C CG  . ASN E  1 5   ? 28.259  -43.552  22.741  1.000 84.604  0 334 ASN EEE CG  1 ? 16 
ATOM   5132  O OD1 . ASN E  1 5   ? 27.464  -44.386  23.153  1.000 86.430  0 334 ASN EEE OD1 1 ? 16 
ATOM   5133  N ND2 . ASN E  1 5   ? 29.354  -43.887  22.073  1.000 85.395  0 334 ASN EEE ND2 1 ? 16 
ATOM   5134  N N   . LEU E  1 6   ? 26.561  -40.570  20.307  1.000 69.000  0 335 LEU EEE N   1 ? 16 
ATOM   5135  C CA  . LEU E  1 6   ? 26.493  -40.463  18.833  1.000 67.527  0 335 LEU EEE CA  1 ? 16 
ATOM   5136  C C   . LEU E  1 6   ? 27.790  -40.990  18.200  1.000 65.602  0 335 LEU EEE C   1 ? 16 
ATOM   5137  O O   . LEU E  1 6   ? 28.850  -40.861  18.806  1.000 68.128  0 335 LEU EEE O   1 ? 16 
ATOM   5138  C CB  . LEU E  1 6   ? 26.221  -39.014  18.438  1.000 68.647  0 335 LEU EEE CB  1 ? 16 
ATOM   5139  C CG  . LEU E  1 6   ? 24.855  -38.448  18.828  1.000 73.030  0 335 LEU EEE CG  1 ? 16 
ATOM   5140  C CD1 . LEU E  1 6   ? 24.675  -37.050  18.241  1.000 74.404  0 335 LEU EEE CD1 1 ? 16 
ATOM   5141  C CD2 . LEU E  1 6   ? 23.711  -39.307  18.346  1.000 71.433  0 335 LEU EEE CD2 1 ? 16 
ATOM   5142  N N   . CYS E  1 7   ? 27.676  -41.630  17.043  1.000 61.151  0 336 CYS EEE N   1 ? 16 
ATOM   5143  C CA  . CYS E  1 7   ? 28.814  -42.163  16.268  1.000 61.145  0 336 CYS EEE CA  1 ? 16 
ATOM   5144  C C   . CYS E  1 7   ? 29.637  -40.965  15.828  1.000 58.554  0 336 CYS EEE C   1 ? 16 
ATOM   5145  O O   . CYS E  1 7   ? 29.073  -39.982  15.364  1.000 57.397  0 336 CYS EEE O   1 ? 16 
ATOM   5146  C CB  . CYS E  1 7   ? 28.371  -43.004  15.065  1.000 60.749  0 336 CYS EEE CB  1 ? 16 
ATOM   5147  S SG  . CYS E  1 7   ? 27.558  -44.564  15.518  1.000 66.444  0 336 CYS EEE SG  1 ? 16 
ATOM   5148  N N   . PRO E  1 8   ? 30.979  -41.028  15.965  1.000 58.565  0 337 PRO EEE N   1 ? 16 
ATOM   5149  C CA  . PRO E  1 8   ? 31.829  -39.867  15.727  1.000 58.619  0 337 PRO EEE CA  1 ? 16 
ATOM   5150  C C   . PRO E  1 8   ? 32.100  -39.628  14.226  1.000 54.760  0 337 PRO EEE C   1 ? 16 
ATOM   5151  O O   . PRO E  1 8   ? 33.200  -39.802  13.784  1.000 54.236  0 337 PRO EEE O   1 ? 16 
ATOM   5152  C CB  . PRO E  1 8   ? 33.080  -40.289  16.520  1.000 61.367  0 337 PRO EEE CB  1 ? 16 
ATOM   5153  C CG  . PRO E  1 8   ? 33.193  -41.795  16.270  1.000 60.633  0 337 PRO EEE CG  1 ? 16 
ATOM   5154  C CD  . PRO E  1 8   ? 31.751  -42.239  16.297  1.000 60.088  0 337 PRO EEE CD  1 ? 16 
ATOM   5155  N N   . PHE E  1 9   ? 31.076  -39.246  13.474  1.000 52.242  0 338 PHE EEE N   1 ? 16 
ATOM   5156  C CA  . PHE E  1 9   ? 31.173  -38.990  12.014  1.000 49.894  0 338 PHE EEE CA  1 ? 16 
ATOM   5157  C C   . PHE E  1 9   ? 32.079  -37.799  11.712  1.000 48.677  0 338 PHE EEE C   1 ? 16 
ATOM   5158  O O   . PHE E  1 9   ? 32.767  -37.836  10.673  1.000 46.457  0 338 PHE EEE O   1 ? 16 
ATOM   5159  C CB  . PHE E  1 9   ? 29.783  -38.821  11.401  1.000 50.737  0 338 PHE EEE CB  1 ? 16 
ATOM   5160  C CG  . PHE E  1 9   ? 29.056  -40.130  11.210  1.000 52.065  0 338 PHE EEE CG  1 ? 16 
ATOM   5161  C CD1 . PHE E  1 9   ? 29.711  -41.269  10.732  1.000 51.079  0 338 PHE EEE CD1 1 ? 16 
ATOM   5162  C CD2 . PHE E  1 9   ? 27.715  -40.218  11.522  1.000 52.882  0 338 PHE EEE CD2 1 ? 16 
ATOM   5163  C CE1 . PHE E  1 9   ? 29.019  -42.452  10.576  1.000 52.983  0 338 PHE EEE CE1 1 ? 16 
ATOM   5164  C CE2 . PHE E  1 9   ? 27.041  -41.412  11.371  1.000 55.787  0 338 PHE EEE CE2 1 ? 16 
ATOM   5165  C CZ  . PHE E  1 9   ? 27.700  -42.526  10.908  1.000 54.373  0 338 PHE EEE CZ  1 ? 16 
ATOM   5166  N N   . GLY E  1 10  ? 32.109  -36.798  12.591  1.000 50.447  0 339 GLY EEE N   1 ? 16 
ATOM   5167  C CA  . GLY E  1 10  ? 33.034  -35.649  12.500  1.000 49.358  0 339 GLY EEE CA  1 ? 16 
ATOM   5168  C C   . GLY E  1 10  ? 34.479  -36.092  12.329  1.000 48.793  0 339 GLY EEE C   1 ? 16 
ATOM   5169  O O   . GLY E  1 10  ? 35.179  -35.558  11.468  1.000 45.669  0 339 GLY EEE O   1 ? 16 
ATOM   5170  N N   . GLU E  1 11  ? 34.912  -37.067  13.113  1.000 51.046  0 340 GLU EEE N   1 ? 16 
ATOM   5171  C CA  . GLU E  1 11  ? 36.311  -37.584  13.112  1.000 53.525  0 340 GLU EEE CA  1 ? 16 
ATOM   5172  C C   . GLU E  1 11  ? 36.623  -38.263  11.786  1.000 49.871  0 340 GLU EEE C   1 ? 16 
ATOM   5173  O O   . GLU E  1 11  ? 37.799  -38.361  11.477  1.000 51.570  0 340 GLU EEE O   1 ? 16 
ATOM   5174  C CB  . GLU E  1 11  ? 36.520  -38.556  14.266  1.000 59.536  0 340 GLU EEE CB  1 ? 16 
ATOM   5175  C CG  . GLU E  1 11  ? 36.287  -37.894  15.612  1.000 66.480  0 340 GLU EEE CG  1 ? 16 
ATOM   5176  C CD  . GLU E  1 11  ? 36.527  -38.791  16.795  1.000 74.896  0 340 GLU EEE CD  1 ? 16 
ATOM   5177  O OE1 . GLU E  1 11  ? 37.154  -39.857  16.590  1.000 81.246  0 340 GLU EEE OE1 1 ? 16 
ATOM   5178  O OE2 . GLU E  1 11  ? 36.094  -38.421  17.904  1.000 77.605  0 340 GLU EEE OE2 1 ? 16 
ATOM   5179  N N   . VAL E  1 12  ? 35.622  -38.717  11.040  1.000 48.090  0 341 VAL EEE N   1 ? 16 
ATOM   5180  C CA  . VAL E  1 12  ? 35.778  -39.354  9.698   1.000 46.622  0 341 VAL EEE CA  1 ? 16 
ATOM   5181  C C   . VAL E  1 12  ? 35.808  -38.270  8.617   1.000 46.415  0 341 VAL EEE C   1 ? 16 
ATOM   5182  O O   . VAL E  1 12  ? 36.827  -38.172  7.893   1.000 50.260  0 341 VAL EEE O   1 ? 16 
ATOM   5183  C CB  . VAL E  1 12  ? 34.660  -40.375  9.422   1.000 44.851  0 341 VAL EEE CB  1 ? 16 
ATOM   5184  C CG1 . VAL E  1 12  ? 34.811  -41.012  8.058   1.000 43.912  0 341 VAL EEE CG1 1 ? 16 
ATOM   5185  C CG2 . VAL E  1 12  ? 34.585  -41.445  10.501  1.000 46.828  0 341 VAL EEE CG2 1 ? 16 
ATOM   5186  N N   . PHE E  1 13  ? 34.724  -37.507  8.490   1.000 45.058  0 342 PHE EEE N   1 ? 16 
ATOM   5187  C CA  . PHE E  1 13  ? 34.478  -36.579  7.351   1.000 44.047  0 342 PHE EEE CA  1 ? 16 
ATOM   5188  C C   . PHE E  1 13  ? 35.422  -35.378  7.437   1.000 44.469  0 342 PHE EEE C   1 ? 16 
ATOM   5189  O O   . PHE E  1 13  ? 35.795  -34.840  6.381   1.000 46.267  0 342 PHE EEE O   1 ? 16 
ATOM   5190  C CB  . PHE E  1 13  ? 32.994  -36.184  7.327   1.000 42.770  0 342 PHE EEE CB  1 ? 16 
ATOM   5191  C CG  . PHE E  1 13  ? 32.101  -37.262  6.772   1.000 40.683  0 342 PHE EEE CG  1 ? 16 
ATOM   5192  C CD1 . PHE E  1 13  ? 31.867  -37.346  5.419   1.000 39.788  0 342 PHE EEE CD1 1 ? 16 
ATOM   5193  C CD2 . PHE E  1 13  ? 31.565  -38.251  7.581   1.000 42.707  0 342 PHE EEE CD2 1 ? 16 
ATOM   5194  C CE1 . PHE E  1 13  ? 31.084  -38.363  4.887   1.000 40.342  0 342 PHE EEE CE1 1 ? 16 
ATOM   5195  C CE2 . PHE E  1 13  ? 30.790  -39.272  7.045   1.000 42.609  0 342 PHE EEE CE2 1 ? 16 
ATOM   5196  C CZ  . PHE E  1 13  ? 30.555  -39.329  5.699   1.000 40.209  0 342 PHE EEE CZ  1 ? 16 
ATOM   5197  N N   . ASN E  1 14  ? 35.774  -34.974  8.651   1.000 46.011  0 343 ASN EEE N   1 ? 16 
ATOM   5198  C CA  . ASN E  1 14  ? 36.560  -33.743  8.961   1.000 49.262  0 343 ASN EEE CA  1 ? 16 
ATOM   5199  C C   . ASN E  1 14  ? 37.895  -34.111  9.622   1.000 48.274  0 343 ASN EEE C   1 ? 16 
ATOM   5200  O O   . ASN E  1 14  ? 38.445  -33.294  10.335  1.000 52.427  0 343 ASN EEE O   1 ? 16 
ATOM   5201  C CB  . ASN E  1 14  ? 35.728  -32.788  9.833   1.000 51.685  0 343 ASN EEE CB  1 ? 16 
ATOM   5202  C CG  . ASN E  1 14  ? 34.569  -32.159  9.077   1.000 53.047  0 343 ASN EEE CG  1 ? 16 
ATOM   5203  O OD1 . ASN E  1 14  ? 34.711  -31.919  7.888   1.000 47.089  0 343 ASN EEE OD1 1 ? 16 
ATOM   5204  N ND2 . ASN E  1 14  ? 33.425  -31.921  9.720   1.000 58.709  0 343 ASN EEE ND2 1 ? 16 
ATOM   5205  N N   . ALA E  1 15  ? 38.372  -35.338  9.454   1.000 49.169  0 344 ALA EEE N   1 ? 16 
ATOM   5206  C CA  . ALA E  1 15  ? 39.718  -35.765  9.912   1.000 50.049  0 344 ALA EEE CA  1 ? 16 
ATOM   5207  C C   . ALA E  1 15  ? 40.742  -34.740  9.417   1.000 48.709  0 344 ALA EEE C   1 ? 16 
ATOM   5208  O O   . ALA E  1 15  ? 40.596  -34.258  8.276   1.000 46.625  0 344 ALA EEE O   1 ? 16 
ATOM   5209  C CB  . ALA E  1 15  ? 40.015  -37.166  9.399   1.000 48.980  0 344 ALA EEE CB  1 ? 16 
ATOM   5210  N N   . THR E  1 16  ? 41.728  -34.437  10.234  1.000 51.463  0 345 THR EEE N   1 ? 16 
ATOM   5211  C CA  . THR E  1 16  ? 42.792  -33.453  9.920   1.000 53.003  0 345 THR EEE CA  1 ? 16 
ATOM   5212  C C   . THR E  1 16  ? 43.684  -34.020  8.806   1.000 52.722  0 345 THR EEE C   1 ? 16 
ATOM   5213  O O   . THR E  1 16  ? 44.200  -33.216  8.015   1.000 55.798  0 345 THR EEE O   1 ? 16 
ATOM   5214  C CB  . THR E  1 16  ? 43.529  -33.059  11.202  1.000 55.451  0 345 THR EEE CB  1 ? 16 
ATOM   5215  O OG1 . THR E  1 16  ? 43.862  -34.275  11.851  1.000 55.449  0 345 THR EEE OG1 1 ? 16 
ATOM   5216  C CG2 . THR E  1 16  ? 42.691  -32.256  12.171  1.000 58.451  0 345 THR EEE CG2 1 ? 16 
ATOM   5217  N N   . ARG E  1 17  ? 43.814  -35.344  8.705   1.000 51.166  0 346 ARG EEE N   1 ? 16 
ATOM   5218  C CA  . ARG E  1 17  ? 44.579  -36.037  7.641   1.000 50.739  0 346 ARG EEE CA  1 ? 16 
ATOM   5219  C C   . ARG E  1 17  ? 43.640  -36.975  6.877   1.000 46.535  0 346 ARG EEE C   1 ? 16 
ATOM   5220  O O   . ARG E  1 17  ? 42.816  -37.629  7.512   1.000 45.868  0 346 ARG EEE O   1 ? 16 
ATOM   5221  C CB  . ARG E  1 17  ? 45.726  -36.853  8.247   1.000 55.404  0 346 ARG EEE CB  1 ? 16 
ATOM   5222  C CG  . ARG E  1 17  ? 47.062  -36.617  7.577   1.000 60.294  0 346 ARG EEE CG  1 ? 16 
ATOM   5223  C CD  . ARG E  1 17  ? 48.054  -37.701  7.903   1.000 66.519  0 346 ARG EEE CD  1 ? 16 
ATOM   5224  N NE  . ARG E  1 17  ? 48.533  -37.570  9.279   1.000 74.214  0 346 ARG EEE NE  1 ? 16 
ATOM   5225  C CZ  . ARG E  1 17  ? 49.534  -36.781  9.671   1.000 78.967  0 346 ARG EEE CZ  1 ? 16 
ATOM   5226  N NH1 . ARG E  1 17  ? 50.189  -36.030  8.794   1.000 79.780  0 346 ARG EEE NH1 1 ? 16 
ATOM   5227  N NH2 . ARG E  1 17  ? 49.889  -36.768  10.945  1.000 83.695  0 346 ARG EEE NH2 1 ? 16 
ATOM   5228  N N   . PHE E  1 18  ? 43.864  -37.139  5.584   1.000 39.795  0 347 PHE EEE N   1 ? 17 
ATOM   5229  C CA  . PHE E  1 18  ? 43.243  -38.188  4.746   1.000 40.188  0 347 PHE EEE CA  1 ? 17 
ATOM   5230  C C   . PHE E  1 18  ? 44.354  -39.026  4.102   1.000 41.156  0 347 PHE EEE C   1 ? 17 
ATOM   5231  O O   . PHE E  1 18  ? 45.398  -38.482  3.731   1.000 44.162  0 347 PHE EEE O   1 ? 17 
ATOM   5232  C CB  . PHE E  1 18  ? 42.327  -37.564  3.685   1.000 41.489  0 347 PHE EEE CB  1 ? 17 
ATOM   5233  C CG  . PHE E  1 18  ? 40.883  -37.451  4.096   1.000 39.851  0 347 PHE EEE CG  1 ? 17 
ATOM   5234  C CD1 . PHE E  1 18  ? 40.525  -36.612  5.139   1.000 41.543  0 347 PHE EEE CD1 1 ? 17 
ATOM   5235  C CD2 . PHE E  1 18  ? 39.896  -38.187  3.434   1.000 41.015  0 347 PHE EEE CD2 1 ? 17 
ATOM   5236  C CE1 . PHE E  1 18  ? 39.196  -36.524  5.530   1.000 43.133  0 347 PHE EEE CE1 1 ? 17 
ATOM   5237  C CE2 . PHE E  1 18  ? 38.573  -38.088  3.828   1.000 41.185  0 347 PHE EEE CE2 1 ? 17 
ATOM   5238  C CZ  . PHE E  1 18  ? 38.226  -37.269  4.878   1.000 41.251  0 347 PHE EEE CZ  1 ? 17 
ATOM   5239  N N   . ALA E  1 19  ? 44.116  -40.324  3.955   1.000 40.184  0 348 ALA EEE N   1 ? 17 
ATOM   5240  C CA  . ALA E  1 19  ? 45.096  -41.289  3.419   1.000 40.534  0 348 ALA EEE CA  1 ? 17 
ATOM   5241  C C   . ALA E  1 19  ? 45.212  -41.144  1.904   1.000 40.814  0 348 ALA EEE C   1 ? 17 
ATOM   5242  O O   . ALA E  1 19  ? 44.218  -40.713  1.245   1.000 40.811  0 348 ALA EEE O   1 ? 17 
ATOM   5243  C CB  . ALA E  1 19  ? 44.670  -42.693  3.780   1.000 41.284  0 348 ALA EEE CB  1 ? 17 
ATOM   5244  N N   . SER E  1 20  ? 46.363  -41.547  1.370   1.000 41.868  0 349 SER EEE N   1 ? 17 
ATOM   5245  C CA  . SER E  1 20  ? 46.493  -41.964  -0.050  1.000 41.875  0 349 SER EEE CA  1 ? 17 
ATOM   5246  C C   . SER E  1 20  ? 45.545  -43.144  -0.301  1.000 42.369  0 349 SER EEE C   1 ? 17 
ATOM   5247  O O   . SER E  1 20  ? 45.412  -44.018  0.590   1.000 43.717  0 349 SER EEE O   1 ? 17 
ATOM   5248  C CB  . SER E  1 20  ? 47.911  -42.321  -0.370  1.000 41.521  0 349 SER EEE CB  1 ? 17 
ATOM   5249  O OG  . SER E  1 20  ? 48.703  -41.147  -0.427  1.000 44.386  0 349 SER EEE OG  1 ? 17 
ATOM   5250  N N   . VAL E  1 21  ? 44.937  -43.194  -1.478  1.000 41.429  0 350 VAL EEE N   1 ? 17 
ATOM   5251  C CA  . VAL E  1 21  ? 43.994  -44.286  -1.851  1.000 41.980  0 350 VAL EEE CA  1 ? 17 
ATOM   5252  C C   . VAL E  1 21  ? 44.663  -45.674  -1.705  1.000 43.669  0 350 VAL EEE C   1 ? 17 
ATOM   5253  O O   . VAL E  1 21  ? 43.978  -46.592  -1.247  1.000 46.344  0 350 VAL EEE O   1 ? 17 
ATOM   5254  C CB  . VAL E  1 21  ? 43.429  -44.044  -3.260  1.000 42.216  0 350 VAL EEE CB  1 ? 17 
ATOM   5255  C CG1 . VAL E  1 21  ? 44.506  -44.147  -4.338  1.000 43.777  0 350 VAL EEE CG1 1 ? 17 
ATOM   5256  C CG2 . VAL E  1 21  ? 42.250  -44.971  -3.540  1.000 41.463  0 350 VAL EEE CG2 1 ? 17 
ATOM   5257  N N   . TYR E  1 22  ? 45.932  -45.857  -2.062  1.000 43.005  0 351 TYR EEE N   1 ? 17 
ATOM   5258  C CA  . TYR E  1 22  ? 46.580  -47.196  -2.029  1.000 43.458  0 351 TYR EEE CA  1 ? 17 
ATOM   5259  C C   . TYR E  1 22  ? 46.682  -47.665  -0.564  1.000 43.151  0 351 TYR EEE C   1 ? 17 
ATOM   5260  O O   . TYR E  1 22  ? 46.634  -48.892  -0.301  1.000 44.812  0 351 TYR EEE O   1 ? 17 
ATOM   5261  C CB  . TYR E  1 22  ? 47.943  -47.207  -2.733  1.000 42.883  0 351 TYR EEE CB  1 ? 17 
ATOM   5262  C CG  . TYR E  1 22  ? 49.074  -46.765  -1.844  1.000 43.172  0 351 TYR EEE CG  1 ? 17 
ATOM   5263  C CD1 . TYR E  1 22  ? 49.349  -45.415  -1.659  1.000 42.871  0 351 TYR EEE CD1 1 ? 17 
ATOM   5264  C CD2 . TYR E  1 22  ? 49.835  -47.693  -1.152  1.000 43.283  0 351 TYR EEE CD2 1 ? 17 
ATOM   5265  C CE1 . TYR E  1 22  ? 50.355  -44.996  -0.809  1.000 42.180  0 351 TYR EEE CE1 1 ? 17 
ATOM   5266  C CE2 . TYR E  1 22  ? 50.850  -47.297  -0.301  1.000 44.498  0 351 TYR EEE CE2 1 ? 17 
ATOM   5267  C CZ  . TYR E  1 22  ? 51.107  -45.945  -0.130  1.000 44.122  0 351 TYR EEE CZ  1 ? 17 
ATOM   5268  O OH  . TYR E  1 22  ? 52.117  -45.583  0.701   1.000 43.603  0 351 TYR EEE OH  1 ? 17 
ATOM   5269  N N   . ALA E  1 23  ? 46.811  -46.714  0.360   1.000 42.810  0 352 ALA EEE N   1 ? 17 
ATOM   5270  C CA  . ALA E  1 23  ? 46.946  -46.947  1.819   1.000 43.456  0 352 ALA EEE CA  1 ? 17 
ATOM   5271  C C   . ALA E  1 23  ? 45.680  -46.469  2.524   1.000 41.426  0 352 ALA EEE C   1 ? 17 
ATOM   5272  O O   . ALA E  1 23  ? 45.797  -45.830  3.569   1.000 43.718  0 352 ALA EEE O   1 ? 17 
ATOM   5273  C CB  . ALA E  1 23  ? 48.188  -46.252  2.350   1.000 41.453  0 352 ALA EEE CB  1 ? 17 
ATOM   5274  N N   . TRP E  1 24  ? 44.521  -46.781  1.957   1.000 39.120  0 353 TRP EEE N   1 ? 17 
ATOM   5275  C CA  . TRP E  1 24  ? 43.219  -46.252  2.414   1.000 39.458  0 353 TRP EEE CA  1 ? 17 
ATOM   5276  C C   . TRP E  1 24  ? 43.024  -46.573  3.888   1.000 39.282  0 353 TRP EEE C   1 ? 17 
ATOM   5277  O O   . TRP E  1 24  ? 43.422  -47.645  4.336   1.000 42.928  0 353 TRP EEE O   1 ? 17 
ATOM   5278  C CB  . TRP E  1 24  ? 42.076  -46.768  1.536   1.000 38.765  0 353 TRP EEE CB  1 ? 17 
ATOM   5279  C CG  . TRP E  1 24  ? 42.051  -48.243  1.284   1.000 39.679  0 353 TRP EEE CG  1 ? 17 
ATOM   5280  C CD1 . TRP E  1 24  ? 42.623  -48.926  0.250   1.000 40.337  0 353 TRP EEE CD1 1 ? 17 
ATOM   5281  C CD2 . TRP E  1 24  ? 41.337  -49.219  2.055   1.000 39.042  0 353 TRP EEE CD2 1 ? 17 
ATOM   5282  N NE1 . TRP E  1 24  ? 42.338  -50.266  0.340   1.000 43.209  0 353 TRP EEE NE1 1 ? 17 
ATOM   5283  C CE2 . TRP E  1 24  ? 41.519  -50.469  1.421   1.000 40.902  0 353 TRP EEE CE2 1 ? 17 
ATOM   5284  C CE3 . TRP E  1 24  ? 40.552  -49.150  3.207   1.000 37.829  0 353 TRP EEE CE3 1 ? 17 
ATOM   5285  C CZ2 . TRP E  1 24  ? 40.944  -51.644  1.913   1.000 41.293  0 353 TRP EEE CZ2 1 ? 17 
ATOM   5286  C CZ3 . TRP E  1 24  ? 39.987  -50.305  3.684   1.000 38.145  0 353 TRP EEE CZ3 1 ? 17 
ATOM   5287  C CH2 . TRP E  1 24  ? 40.183  -51.532  3.052   1.000 40.519  0 353 TRP EEE CH2 1 ? 17 
ATOM   5288  N N   . ASN E  1 25  ? 42.436  -45.636  4.616   1.000 39.045  0 354 ASN EEE N   1 ? 17 
ATOM   5289  C CA  . ASN E  1 25  ? 42.245  -45.690  6.083   1.000 38.625  0 354 ASN EEE CA  1 ? 17 
ATOM   5290  C C   . ASN E  1 25  ? 40.859  -46.302  6.351   1.000 39.825  0 354 ASN EEE C   1 ? 17 
ATOM   5291  O O   . ASN E  1 25  ? 39.907  -45.974  5.622   1.000 40.964  0 354 ASN EEE O   1 ? 17 
ATOM   5292  C CB  . ASN E  1 25  ? 42.392  -44.286  6.658   1.000 38.970  0 354 ASN EEE CB  1 ? 17 
ATOM   5293  C CG  . ASN E  1 25  ? 42.160  -44.250  8.148   1.000 42.787  0 354 ASN EEE CG  1 ? 17 
ATOM   5294  O OD1 . ASN E  1 25  ? 41.048  -44.046  8.607   1.000 46.465  0 354 ASN EEE OD1 1 ? 17 
ATOM   5295  N ND2 . ASN E  1 25  ? 43.186  -44.509  8.925   1.000 46.435  0 354 ASN EEE ND2 1 ? 17 
ATOM   5296  N N   . ARG E  1 26  ? 40.781  -47.201  7.332   1.000 40.207  0 355 ARG EEE N   1 ? 17 
ATOM   5297  C CA  . ARG E  1 26  ? 39.576  -47.818  7.926   1.000 40.558  0 355 ARG EEE CA  1 ? 17 
ATOM   5298  C C   . ARG E  1 26  ? 39.370  -47.319  9.345   1.000 42.361  0 355 ARG EEE C   1 ? 17 
ATOM   5299  O O   . ARG E  1 26  ? 40.244  -47.591  10.188  1.000 42.285  0 355 ARG EEE O   1 ? 17 
ATOM   5300  C CB  . ARG E  1 26  ? 39.784  -49.273  8.338   1.000 41.297  0 355 ARG EEE CB  1 ? 17 
ATOM   5301  C CG  . ARG E  1 26  ? 39.285  -50.301  7.361   1.000 42.313  0 355 ARG EEE CG  1 ? 17 
ATOM   5302  C CD  . ARG E  1 26  ? 38.160  -51.156  7.803   1.000 41.064  0 355 ARG EEE CD  1 ? 17 
ATOM   5303  N NE  . ARG E  1 26  ? 37.450  -51.232  6.529   1.000 41.888  0 355 ARG EEE NE  1 ? 17 
ATOM   5304  C CZ  . ARG E  1 26  ? 37.129  -52.311  5.868   1.000 39.494  0 355 ARG EEE CZ  1 ? 17 
ATOM   5305  N NH1 . ARG E  1 26  ? 37.350  -53.496  6.386   1.000 42.214  0 355 ARG EEE NH1 1 ? 17 
ATOM   5306  N NH2 . ARG E  1 26  ? 36.484  -52.191  4.732   1.000 38.738  0 355 ARG EEE NH2 1 ? 17 
ATOM   5307  N N   . LYS E  1 27  ? 38.204  -46.767  9.638   1.000 42.711  0 356 LYS EEE N   1 ? 17 
ATOM   5308  C CA  . LYS E  1 27  ? 37.788  -46.544  11.035  1.000 45.526  0 356 LYS EEE CA  1 ? 17 
ATOM   5309  C C   . LYS E  1 27  ? 36.600  -47.466  11.273  1.000 44.347  0 356 LYS EEE C   1 ? 17 
ATOM   5310  O O   . LYS E  1 27  ? 35.686  -47.505  10.449  1.000 45.632  0 356 LYS EEE O   1 ? 17 
ATOM   5311  C CB  . LYS E  1 27  ? 37.513  -45.068  11.297  1.000 48.440  0 356 LYS EEE CB  1 ? 17 
ATOM   5312  C CG  . LYS E  1 27  ? 38.670  -44.153  10.953  1.000 54.697  0 356 LYS EEE CG  1 ? 17 
ATOM   5313  C CD  . LYS E  1 27  ? 38.376  -42.685  11.276  1.000 60.100  0 356 LYS EEE CD  1 ? 17 
ATOM   5314  C CE  . LYS E  1 27  ? 39.539  -41.757  10.973  1.000 59.455  0 356 LYS EEE CE  1 ? 17 
ATOM   5315  N NZ  . LYS E  1 27  ? 39.648  -41.554  9.515   1.000 60.529  0 356 LYS EEE NZ  1 ? 17 
ATOM   5316  N N   . ARG E  1 28  ? 36.661  -48.238  12.341  1.000 44.646  0 357 ARG EEE N   1 ? 17 
ATOM   5317  C CA  . ARG E  1 28  ? 35.537  -49.050  12.821  1.000 45.103  0 357 ARG EEE CA  1 ? 17 
ATOM   5318  C C   . ARG E  1 28  ? 34.583  -48.136  13.567  1.000 43.428  0 357 ARG EEE C   1 ? 17 
ATOM   5319  O O   . ARG E  1 28  ? 35.036  -47.352  14.406  1.000 43.545  0 357 ARG EEE O   1 ? 17 
ATOM   5320  C CB  . ARG E  1 28  ? 36.036  -50.185  13.710  1.000 48.834  0 357 ARG EEE CB  1 ? 17 
ATOM   5321  C CG  . ARG E  1 28  ? 34.959  -51.187  14.056  1.000 55.240  0 357 ARG EEE CG  1 ? 17 
ATOM   5322  C CD  . ARG E  1 28  ? 35.660  -52.272  14.836  1.000 62.217  0 357 ARG EEE CD  1 ? 17 
ATOM   5323  N NE  . ARG E  1 28  ? 34.692  -52.948  15.655  1.000 70.458  0 357 ARG EEE NE  1 ? 17 
ATOM   5324  C CZ  . ARG E  1 28  ? 34.114  -54.099  15.357  1.000 75.546  0 357 ARG EEE CZ  1 ? 17 
ATOM   5325  N NH1 . ARG E  1 28  ? 34.404  -54.735  14.226  1.000 79.614  0 357 ARG EEE NH1 1 ? 17 
ATOM   5326  N NH2 . ARG E  1 28  ? 33.258  -54.628  16.219  1.000 75.257  0 357 ARG EEE NH2 1 ? 17 
ATOM   5327  N N   . ILE E  1 29  ? 33.300  -48.234  13.252  1.000 44.319  0 358 ILE EEE N   1 ? 17 
ATOM   5328  C CA  . ILE E  1 29  ? 32.233  -47.500  13.969  1.000 45.572  0 358 ILE EEE CA  1 ? 17 
ATOM   5329  C C   . ILE E  1 29  ? 31.356  -48.540  14.649  1.000 47.111  0 358 ILE EEE C   1 ? 17 
ATOM   5330  O O   . ILE E  1 29  ? 30.856  -49.434  13.931  1.000 49.512  0 358 ILE EEE O   1 ? 17 
ATOM   5331  C CB  . ILE E  1 29  ? 31.486  -46.568  13.009  1.000 45.896  0 358 ILE EEE CB  1 ? 17 
ATOM   5332  C CG1 . ILE E  1 29  ? 32.435  -45.456  12.555  1.000 46.610  0 358 ILE EEE CG1 1 ? 17 
ATOM   5333  C CG2 . ILE E  1 29  ? 30.245  -45.987  13.680  1.000 45.721  0 358 ILE EEE CG2 1 ? 17 
ATOM   5334  C CD1 . ILE E  1 29  ? 31.922  -44.673  11.413  1.000 49.540  0 358 ILE EEE CD1 1 ? 17 
ATOM   5335  N N   . SER E  1 30  ? 31.237  -48.462  15.976  1.000 47.724  0 359 SER EEE N   1 ? 17 
ATOM   5336  C CA  . SER E  1 30  ? 30.455  -49.444  16.767  1.000 52.030  0 359 SER EEE CA  1 ? 17 
ATOM   5337  C C   . SER E  1 30  ? 30.061  -48.848  18.115  1.000 54.398  0 359 SER EEE C   1 ? 17 
ATOM   5338  O O   . SER E  1 30  ? 30.649  -47.858  18.546  1.000 52.697  0 359 SER EEE O   1 ? 17 
ATOM   5339  C CB  . SER E  1 30  ? 31.257  -50.703  16.972  1.000 53.395  0 359 SER EEE CB  1 ? 17 
ATOM   5340  O OG  . SER E  1 30  ? 32.574  -50.361  17.374  1.000 54.227  0 359 SER EEE OG  1 ? 17 
ATOM   5341  N N   . ASN E  1 31  ? 29.085  -49.490  18.756  1.000 58.800  0 360 ASN EEE N   1 ? 17 
ATOM   5342  C CA  . ASN E  1 31  ? 28.606  -49.161  20.125  1.000 61.860  0 360 ASN EEE CA  1 ? 17 
ATOM   5343  C C   . ASN E  1 31  ? 28.309  -47.674  20.149  1.000 58.798  0 360 ASN EEE C   1 ? 17 
ATOM   5344  O O   . ASN E  1 31  ? 28.907  -46.966  20.997  1.000 57.247  0 360 ASN EEE O   1 ? 17 
ATOM   5345  C CB  . ASN E  1 31  ? 29.593  -49.613  21.191  1.000 66.504  0 360 ASN EEE CB  1 ? 17 
ATOM   5346  C CG  . ASN E  1 31  ? 29.921  -51.090  21.075  1.000 72.058  0 360 ASN EEE CG  1 ? 17 
ATOM   5347  O OD1 . ASN E  1 31  ? 31.101  -51.437  21.022  1.000 75.921  0 360 ASN EEE OD1 1 ? 17 
ATOM   5348  N ND2 . ASN E  1 31  ? 28.911  -51.950  20.918  1.000 74.289  0 360 ASN EEE ND2 1 ? 17 
ATOM   5349  N N   . CYS E  1 32  ? 27.465  -47.229  19.218  1.000 56.588  0 361 CYS EEE N   1 ? 17 
ATOM   5350  C CA  . CYS E  1 32  ? 27.090  -45.801  19.071  1.000 57.294  0 361 CYS EEE CA  1 ? 17 
ATOM   5351  C C   . CYS E  1 32  ? 25.809  -45.667  18.237  1.000 54.459  0 361 CYS EEE C   1 ? 17 
ATOM   5352  O O   . CYS E  1 32  ? 25.487  -46.600  17.483  1.000 54.228  0 361 CYS EEE O   1 ? 17 
ATOM   5353  C CB  . CYS E  1 32  ? 28.241  -44.987  18.480  1.000 56.148  0 361 CYS EEE CB  1 ? 17 
ATOM   5354  S SG  . CYS E  1 32  ? 28.799  -45.557  16.866  1.000 56.836  0 361 CYS EEE SG  1 ? 17 
ATOM   5355  N N   . VAL E  1 33  ? 25.107  -44.551  18.426  1.000 52.947  0 362 VAL EEE N   1 ? 17 
ATOM   5356  C CA  . VAL E  1 33  ? 23.911  -44.144  17.649  1.000 52.804  0 362 VAL EEE CA  1 ? 17 
ATOM   5357  C C   . VAL E  1 33  ? 24.376  -43.393  16.397  1.000 52.121  0 362 VAL EEE C   1 ? 17 
ATOM   5358  O O   . VAL E  1 33  ? 25.042  -42.370  16.544  1.000 49.369  0 362 VAL EEE O   1 ? 17 
ATOM   5359  C CB  . VAL E  1 33  ? 22.971  -43.270  18.497  1.000 53.635  0 362 VAL EEE CB  1 ? 17 
ATOM   5360  C CG1 . VAL E  1 33  ? 21.739  -42.860  17.706  1.000 52.924  0 362 VAL EEE CG1 1 ? 17 
ATOM   5361  C CG2 . VAL E  1 33  ? 22.574  -43.955  19.801  1.000 55.519  0 362 VAL EEE CG2 1 ? 17 
ATOM   5362  N N   . ALA E  1 34  ? 24.060  -43.913  15.213  1.000 52.562  0 363 ALA EEE N   1 ? 17 
ATOM   5363  C CA  . ALA E  1 34  ? 24.441  -43.333  13.901  1.000 52.495  0 363 ALA EEE CA  1 ? 17 
ATOM   5364  C C   . ALA E  1 34  ? 23.416  -42.281  13.499  1.000 52.991  0 363 ALA EEE C   1 ? 17 
ATOM   5365  O O   . ALA E  1 34  ? 22.377  -42.694  12.960  1.000 57.824  0 363 ALA EEE O   1 ? 17 
ATOM   5366  C CB  . ALA E  1 34  ? 24.595  -44.417  12.850  1.000 50.748  0 363 ALA EEE CB  1 ? 17 
ATOM   5367  N N   . ASP E  1 35  ? 23.671  -41.019  13.819  1.000 53.144  0 364 ASP EEE N   1 ? 17 
ATOM   5368  C CA  . ASP E  1 35  ? 22.788  -39.918  13.374  1.000 54.341  0 364 ASP EEE CA  1 ? 17 
ATOM   5369  C C   . ASP E  1 35  ? 23.337  -39.336  12.076  1.000 51.420  0 364 ASP EEE C   1 ? 17 
ATOM   5370  O O   . ASP E  1 35  ? 24.366  -38.657  12.115  1.000 50.216  0 364 ASP EEE O   1 ? 17 
ATOM   5371  C CB  . ASP E  1 35  ? 22.611  -38.818  14.419  1.000 57.491  0 364 ASP EEE CB  1 ? 17 
ATOM   5372  C CG  . ASP E  1 35  ? 21.375  -38.009  14.105  1.000 58.890  0 364 ASP EEE CG  1 ? 17 
ATOM   5373  O OD1 . ASP E  1 35  ? 20.872  -38.143  12.970  1.000 57.682  0 364 ASP EEE OD1 1 ? 17 
ATOM   5374  O OD2 . ASP E  1 35  ? 20.908  -37.292  14.992  1.000 63.446  0 364 ASP EEE OD2 1 ? 17 
ATOM   5375  N N   . TYR E  1 36  ? 22.629  -39.572  10.974  1.000 51.452  0 365 TYR EEE N   1 ? 17 
ATOM   5376  C CA  . TYR E  1 36  ? 23.056  -39.168  9.611   1.000 51.389  0 365 TYR EEE CA  1 ? 17 
ATOM   5377  C C   . TYR E  1 36  ? 22.492  -37.785  9.263   1.000 53.517  0 365 TYR EEE C   1 ? 17 
ATOM   5378  O O   . TYR E  1 36  ? 22.761  -37.314  8.137   1.000 53.113  0 365 TYR EEE O   1 ? 17 
ATOM   5379  C CB  . TYR E  1 36  ? 22.620  -40.223  8.601   1.000 50.534  0 365 TYR EEE CB  1 ? 17 
ATOM   5380  C CG  . TYR E  1 36  ? 23.387  -41.516  8.709   1.000 47.995  0 365 TYR EEE CG  1 ? 17 
ATOM   5381  C CD1 . TYR E  1 36  ? 24.567  -41.687  8.018   1.000 46.011  0 365 TYR EEE CD1 1 ? 17 
ATOM   5382  C CD2 . TYR E  1 36  ? 22.959  -42.541  9.534   1.000 46.014  0 365 TYR EEE CD2 1 ? 17 
ATOM   5383  C CE1 . TYR E  1 36  ? 25.288  -42.863  8.121   1.000 46.489  0 365 TYR EEE CE1 1 ? 17 
ATOM   5384  C CE2 . TYR E  1 36  ? 23.666  -43.727  9.637   1.000 44.928  0 365 TYR EEE CE2 1 ? 17 
ATOM   5385  C CZ  . TYR E  1 36  ? 24.827  -43.893  8.915   1.000 44.106  0 365 TYR EEE CZ  1 ? 17 
ATOM   5386  O OH  . TYR E  1 36  ? 25.546  -45.046  8.958   1.000 44.650  0 365 TYR EEE OH  1 ? 17 
ATOM   5387  N N   . SER E  1 37  ? 21.742  -37.133  10.154  1.000 55.360  0 366 SER EEE N   1 ? 17 
ATOM   5388  C CA  . SER E  1 37  ? 21.097  -35.830  9.804   1.000 57.284  0 366 SER EEE CA  1 ? 17 
ATOM   5389  C C   . SER E  1 37  ? 22.160  -34.753  9.543   1.000 57.281  0 366 SER EEE C   1 ? 17 
ATOM   5390  O O   . SER E  1 37  ? 21.915  -33.823  8.772   1.000 58.956  0 366 SER EEE O   1 ? 17 
ATOM   5391  C CB  . SER E  1 37  ? 20.044  -35.373  10.778  1.000 60.543  0 366 SER EEE CB  1 ? 17 
ATOM   5392  O OG  . SER E  1 37  ? 20.262  -35.841  12.089  1.000 62.411  0 366 SER EEE OG  1 ? 17 
ATOM   5393  N N   . VAL E  1 38  ? 23.349  -34.904  10.095  1.000 57.963  0 367 VAL EEE N   1 ? 17 
ATOM   5394  C CA  . VAL E  1 38  ? 24.487  -33.986  9.789   1.000 56.152  0 367 VAL EEE CA  1 ? 17 
ATOM   5395  C C   . VAL E  1 38  ? 24.828  -34.120  8.295   1.000 57.087  0 367 VAL EEE C   1 ? 17 
ATOM   5396  O O   . VAL E  1 38  ? 25.009  -33.068  7.644   1.000 61.888  0 367 VAL EEE O   1 ? 17 
ATOM   5397  C CB  . VAL E  1 38  ? 25.666  -34.270  10.737  1.000 56.636  0 367 VAL EEE CB  1 ? 17 
ATOM   5398  C CG1 . VAL E  1 38  ? 26.303  -35.660  10.483  1.000 56.842  0 367 VAL EEE CG1 1 ? 17 
ATOM   5399  C CG2 . VAL E  1 38  ? 26.668  -33.136  10.721  1.000 54.639  0 367 VAL EEE CG2 1 ? 17 
ATOM   5400  N N   . LEU E  1 39  ? 24.847  -35.332  7.726   1.000 53.525  0 368 LEU EEE N   1 ? 17 
ATOM   5401  C CA  . LEU E  1 39  ? 25.095  -35.547  6.272   1.000 50.678  0 368 LEU EEE CA  1 ? 17 
ATOM   5402  C C   . LEU E  1 39  ? 23.893  -35.093  5.429   1.000 52.223  0 368 LEU EEE C   1 ? 17 
ATOM   5403  O O   . LEU E  1 39  ? 24.113  -34.640  4.316   1.000 52.974  0 368 LEU EEE O   1 ? 17 
ATOM   5404  C CB  . LEU E  1 39  ? 25.384  -37.020  6.009   1.000 48.024  0 368 LEU EEE CB  1 ? 17 
ATOM   5405  C CG  . LEU E  1 39  ? 26.565  -37.608  6.756   1.000 48.139  0 368 LEU EEE CG  1 ? 17 
ATOM   5406  C CD1 . LEU E  1 39  ? 26.710  -39.065  6.348   1.000 47.670  0 368 LEU EEE CD1 1 ? 17 
ATOM   5407  C CD2 . LEU E  1 39  ? 27.862  -36.892  6.447   1.000 47.652  0 368 LEU EEE CD2 1 ? 17 
ATOM   5408  N N   . TYR E  1 40  ? 22.669  -35.230  5.928   1.000 52.982  0 369 TYR EEE N   1 ? 17 
ATOM   5409  C CA  . TYR E  1 40  ? 21.421  -34.856  5.207   1.000 53.772  0 369 TYR EEE CA  1 ? 17 
ATOM   5410  C C   . TYR E  1 40  ? 21.386  -33.351  4.941   1.000 54.392  0 369 TYR EEE C   1 ? 17 
ATOM   5411  O O   . TYR E  1 40  ? 20.771  -32.950  3.955   1.000 55.433  0 369 TYR EEE O   1 ? 17 
ATOM   5412  C CB  . TYR E  1 40  ? 20.160  -35.261  5.977   1.000 54.427  0 369 TYR EEE CB  1 ? 17 
ATOM   5413  C CG  . TYR E  1 40  ? 19.898  -36.742  6.102   1.000 53.004  0 369 TYR EEE CG  1 ? 17 
ATOM   5414  C CD1 . TYR E  1 40  ? 20.317  -37.638  5.126   1.000 51.678  0 369 TYR EEE CD1 1 ? 17 
ATOM   5415  C CD2 . TYR E  1 40  ? 19.195  -37.237  7.195   1.000 52.006  0 369 TYR EEE CD2 1 ? 17 
ATOM   5416  C CE1 . TYR E  1 40  ? 20.098  -38.997  5.266   1.000 52.444  0 369 TYR EEE CE1 1 ? 17 
ATOM   5417  C CE2 . TYR E  1 40  ? 18.915  -38.579  7.315   1.000 52.337  0 369 TYR EEE CE2 1 ? 17 
ATOM   5418  C CZ  . TYR E  1 40  ? 19.390  -39.464  6.361   1.000 52.941  0 369 TYR EEE CZ  1 ? 17 
ATOM   5419  O OH  . TYR E  1 40  ? 19.128  -40.793  6.464   1.000 52.977  0 369 TYR EEE OH  1 ? 17 
ATOM   5420  N N   . ASN E  1 41  ? 22.026  -32.557  5.794   1.000 55.288  0 370 ASN EEE N   1 ? 17 
ATOM   5421  C CA  . ASN E  1 41  ? 22.006  -31.065  5.754   1.000 57.603  0 370 ASN EEE CA  1 ? 17 
ATOM   5422  C C   . ASN E  1 41  ? 23.197  -30.507  4.954   1.000 54.569  0 370 ASN EEE C   1 ? 17 
ATOM   5423  O O   . ASN E  1 41  ? 23.379  -29.305  4.953   1.000 55.876  0 370 ASN EEE O   1 ? 17 
ATOM   5424  C CB  . ASN E  1 41  ? 21.988  -30.482  7.166   1.000 61.629  0 370 ASN EEE CB  1 ? 17 
ATOM   5425  C CG  . ASN E  1 41  ? 20.712  -30.839  7.892   1.000 66.153  0 370 ASN EEE CG  1 ? 17 
ATOM   5426  O OD1 . ASN E  1 41  ? 19.653  -30.755  7.283   1.000 67.679  0 370 ASN EEE OD1 1 ? 17 
ATOM   5427  N ND2 . ASN E  1 41  ? 20.794  -31.242  9.159   1.000 69.024  0 370 ASN EEE ND2 1 ? 17 
ATOM   5428  N N   . SER E  1 42  ? 23.985  -31.361  4.322   1.000 50.331  0 371 SER EEE N   1 ? 17 
ATOM   5429  C CA  . SER E  1 42  ? 25.085  -31.014  3.394   1.000 49.277  0 371 SER EEE CA  1 ? 17 
ATOM   5430  C C   . SER E  1 42  ? 24.533  -31.035  1.969   1.000 49.035  0 371 SER EEE C   1 ? 17 
ATOM   5431  O O   . SER E  1 42  ? 23.831  -32.006  1.609   1.000 48.698  0 371 SER EEE O   1 ? 17 
ATOM   5432  C CB  . SER E  1 42  ? 26.233  -31.993  3.534   1.000 47.348  0 371 SER EEE CB  1 ? 17 
ATOM   5433  O OG  . SER E  1 42  ? 26.684  -32.060  4.872   1.000 47.923  0 371 SER EEE OG  1 ? 17 
ATOM   5434  N N   . ALA E  1 43  ? 24.848  -30.015  1.183   1.000 47.984  0 372 ALA EEE N   1 ? 18 
ATOM   5435  C CA  . ALA E  1 43  ? 24.550  -29.929  -0.268  1.000 47.585  0 372 ALA EEE CA  1 ? 18 
ATOM   5436  C C   . ALA E  1 43  ? 25.852  -30.033  -1.074  1.000 46.569  0 372 ALA EEE C   1 ? 18 
ATOM   5437  O O   . ALA E  1 43  ? 25.740  -30.062  -2.301  1.000 46.789  0 372 ALA EEE O   1 ? 18 
ATOM   5438  C CB  . ALA E  1 43  ? 23.792  -28.650  -0.595  1.000 49.656  0 372 ALA EEE CB  1 ? 18 
ATOM   5439  N N   . SER E  1 44  ? 27.045  -29.981  -0.465  1.000 46.228  0 373 SER EEE N   1 ? 18 
ATOM   5440  C CA  . SER E  1 44  ? 28.327  -29.779  -1.203  1.000 45.819  0 373 SER EEE CA  1 ? 18 
ATOM   5441  C C   . SER E  1 44  ? 28.988  -31.107  -1.575  1.000 44.870  0 373 SER EEE C   1 ? 18 
ATOM   5442  O O   . SER E  1 44  ? 29.951  -31.113  -2.314  1.000 46.218  0 373 SER EEE O   1 ? 18 
ATOM   5443  C CB  . SER E  1 44  ? 29.290  -28.899  -0.464  1.000 45.437  0 373 SER EEE CB  1 ? 18 
ATOM   5444  O OG  . SER E  1 44  ? 29.013  -27.538  -0.729  1.000 48.431  0 373 SER EEE OG  1 ? 18 
ATOM   5445  N N   . PHE E  1 45  ? 28.510  -32.243  -1.100  1.000 45.971  0 374 PHE EEE N   1 ? 18 
ATOM   5446  C CA  . PHE E  1 45  ? 28.930  -33.585  -1.573  1.000 45.715  0 374 PHE EEE CA  1 ? 18 
ATOM   5447  C C   . PHE E  1 45  ? 28.664  -33.694  -3.078  1.000 44.202  0 374 PHE EEE C   1 ? 18 
ATOM   5448  O O   . PHE E  1 45  ? 27.565  -33.353  -3.529  1.000 45.239  0 374 PHE EEE O   1 ? 18 
ATOM   5449  C CB  . PHE E  1 45  ? 28.195  -34.673  -0.797  1.000 46.341  0 374 PHE EEE CB  1 ? 18 
ATOM   5450  C CG  . PHE E  1 45  ? 28.495  -34.738  0.681   1.000 48.310  0 374 PHE EEE CG  1 ? 18 
ATOM   5451  C CD1 . PHE E  1 45  ? 29.778  -34.581  1.147   1.000 47.781  0 374 PHE EEE CD1 1 ? 18 
ATOM   5452  C CD2 . PHE E  1 45  ? 27.494  -35.002  1.600   1.000 50.339  0 374 PHE EEE CD2 1 ? 18 
ATOM   5453  C CE1 . PHE E  1 45  ? 30.060  -34.665  2.496   1.000 49.562  0 374 PHE EEE CE1 1 ? 18 
ATOM   5454  C CE2 . PHE E  1 45  ? 27.777  -35.090  2.942   1.000 52.038  0 374 PHE EEE CE2 1 ? 18 
ATOM   5455  C CZ  . PHE E  1 45  ? 29.052  -34.896  3.389   1.000 51.073  0 374 PHE EEE CZ  1 ? 18 
ATOM   5456  N N   . SER E  1 46  ? 29.668  -34.133  -3.835  1.000 44.230  0 375 SER EEE N   1 ? 18 
ATOM   5457  C CA  . SER E  1 46  ? 29.591  -34.322  -5.316  1.000 44.630  0 375 SER EEE CA  1 ? 18 
ATOM   5458  C C   . SER E  1 46  ? 28.783  -35.578  -5.642  1.000 42.584  0 375 SER EEE C   1 ? 18 
ATOM   5459  O O   . SER E  1 46  ? 28.156  -35.603  -6.693  1.000 41.550  0 375 SER EEE O   1 ? 18 
ATOM   5460  C CB  . SER E  1 46  ? 30.965  -34.402  -5.947  1.000 44.223  0 375 SER EEE CB  1 ? 18 
ATOM   5461  O OG  . SER E  1 46  ? 31.751  -35.402  -5.319  1.000 42.044  0 375 SER EEE OG  1 ? 18 
ATOM   5462  N N   . THR E  1 47  ? 28.787  -36.554  -4.742  1.000 40.553  0 376 THR EEE N   1 ? 18 
ATOM   5463  C CA  . THR E  1 47  ? 28.009  -37.805  -4.881  1.000 41.806  0 376 THR EEE CA  1 ? 18 
ATOM   5464  C C   . THR E  1 47  ? 27.656  -38.313  -3.474  1.000 41.757  0 376 THR EEE C   1 ? 18 
ATOM   5465  O O   . THR E  1 47  ? 28.459  -38.120  -2.511  1.000 39.022  0 376 THR EEE O   1 ? 18 
ATOM   5466  C CB  . THR E  1 47  ? 28.824  -38.809  -5.713  1.000 41.374  0 376 THR EEE CB  1 ? 18 
ATOM   5467  O OG1 . THR E  1 47  ? 27.959  -39.863  -6.131  1.000 40.123  0 376 THR EEE OG1 1 ? 18 
ATOM   5468  C CG2 . THR E  1 47  ? 30.029  -39.343  -4.953  1.000 39.770  0 376 THR EEE CG2 1 ? 18 
ATOM   5469  N N   . PHE E  1 48  ? 26.499  -38.949  -3.346  1.000 41.079  0 377 PHE EEE N   1 ? 18 
ATOM   5470  C CA  . PHE E  1 48  ? 26.050  -39.551  -2.072  1.000 40.985  0 377 PHE EEE CA  1 ? 18 
ATOM   5471  C C   . PHE E  1 48  ? 25.076  -40.642  -2.470  1.000 39.440  0 377 PHE EEE C   1 ? 18 
ATOM   5472  O O   . PHE E  1 48  ? 23.882  -40.335  -2.673  1.000 39.853  0 377 PHE EEE O   1 ? 18 
ATOM   5473  C CB  . PHE E  1 48  ? 25.466  -38.471  -1.147  1.000 41.873  0 377 PHE EEE CB  1 ? 18 
ATOM   5474  C CG  . PHE E  1 48  ? 24.971  -38.933  0.209   1.000 42.597  0 377 PHE EEE CG  1 ? 18 
ATOM   5475  C CD1 . PHE E  1 48  ? 24.804  -40.275  0.522   1.000 42.547  0 377 PHE EEE CD1 1 ? 18 
ATOM   5476  C CD2 . PHE E  1 48  ? 24.608  -38.005  1.166   1.000 43.636  0 377 PHE EEE CD2 1 ? 18 
ATOM   5477  C CE1 . PHE E  1 48  ? 24.332  -40.678  1.763   1.000 43.872  0 377 PHE EEE CE1 1 ? 18 
ATOM   5478  C CE2 . PHE E  1 48  ? 24.118  -38.407  2.400   1.000 44.423  0 377 PHE EEE CE2 1 ? 18 
ATOM   5479  C CZ  . PHE E  1 48  ? 24.002  -39.740  2.706   1.000 43.238  0 377 PHE EEE CZ  1 ? 18 
ATOM   5480  N N   . LYS E  1 49  ? 25.598  -41.852  -2.663  1.000 36.810  0 378 LYS EEE N   1 ? 18 
ATOM   5481  C CA  . LYS E  1 49  ? 24.762  -43.012  -3.054  1.000 37.999  0 378 LYS EEE CA  1 ? 18 
ATOM   5482  C C   . LYS E  1 49  ? 24.900  -44.126  -2.018  1.000 36.400  0 378 LYS EEE C   1 ? 18 
ATOM   5483  O O   . LYS E  1 49  ? 26.000  -44.360  -1.546  1.000 37.312  0 378 LYS EEE O   1 ? 18 
ATOM   5484  C CB  . LYS E  1 49  ? 25.154  -43.583  -4.408  1.000 38.833  0 378 LYS EEE CB  1 ? 18 
ATOM   5485  C CG  . LYS E  1 49  ? 25.212  -42.605  -5.568  1.000 39.491  0 378 LYS EEE CG  1 ? 18 
ATOM   5486  C CD  . LYS E  1 49  ? 25.783  -43.224  -6.786  1.000 38.499  0 378 LYS EEE CD  1 ? 18 
ATOM   5487  C CE  . LYS E  1 49  ? 25.575  -42.344  -7.986  1.000 39.863  0 378 LYS EEE CE  1 ? 18 
ATOM   5488  N NZ  . LYS E  1 49  ? 26.013  -42.990  -9.245  1.000 42.392  0 378 LYS EEE NZ  1 ? 18 
ATOM   5489  N N   . CYS E  1 50  ? 23.816  -44.829  -1.760  1.000 36.488  0 379 CYS EEE N   1 ? 18 
ATOM   5490  C CA  . CYS E  1 50  ? 23.802  -46.074  -0.980  1.000 37.215  0 379 CYS EEE CA  1 ? 18 
ATOM   5491  C C   . CYS E  1 50  ? 23.432  -47.247  -1.915  1.000 37.884  0 379 CYS EEE C   1 ? 18 
ATOM   5492  O O   . CYS E  1 50  ? 22.798  -47.044  -2.976  1.000 36.793  0 379 CYS EEE O   1 ? 18 
ATOM   5493  C CB  . CYS E  1 50  ? 22.893  -45.911  0.230   1.000 39.400  0 379 CYS EEE CB  1 ? 18 
ATOM   5494  S SG  . CYS E  1 50  ? 23.373  -44.534  1.312   1.000 42.189  0 379 CYS EEE SG  1 ? 18 
ATOM   5495  N N   . TYR E  1 51  ? 23.875  -48.429  -1.511  1.000 38.910  0 380 TYR EEE N   1 ? 18 
ATOM   5496  C CA  . TYR E  1 51  ? 23.730  -49.722  -2.210  1.000 40.252  0 380 TYR EEE CA  1 ? 18 
ATOM   5497  C C   . TYR E  1 51  ? 23.146  -50.712  -1.192  1.000 42.379  0 380 TYR EEE C   1 ? 18 
ATOM   5498  O O   . TYR E  1 51  ? 23.747  -50.867  -0.105  1.000 42.339  0 380 TYR EEE O   1 ? 18 
ATOM   5499  C CB  . TYR E  1 51  ? 25.102  -50.114  -2.756  1.000 39.030  0 380 TYR EEE CB  1 ? 18 
ATOM   5500  C CG  . TYR E  1 51  ? 25.721  -49.077  -3.668  1.000 38.099  0 380 TYR EEE CG  1 ? 18 
ATOM   5501  C CD1 . TYR E  1 51  ? 26.450  -48.013  -3.155  1.000 36.906  0 380 TYR EEE CD1 1 ? 18 
ATOM   5502  C CD2 . TYR E  1 51  ? 25.590  -49.159  -5.036  1.000 36.851  0 380 TYR EEE CD2 1 ? 18 
ATOM   5503  C CE1 . TYR E  1 51  ? 27.059  -47.084  -3.971  1.000 36.393  0 380 TYR EEE CE1 1 ? 18 
ATOM   5504  C CE2 . TYR E  1 51  ? 26.146  -48.210  -5.872  1.000 37.668  0 380 TYR EEE CE2 1 ? 18 
ATOM   5505  C CZ  . TYR E  1 51  ? 26.919  -47.187  -5.346  1.000 36.513  0 380 TYR EEE CZ  1 ? 18 
ATOM   5506  O OH  . TYR E  1 51  ? 27.505  -46.282  -6.183  1.000 35.254  0 380 TYR EEE OH  1 ? 18 
ATOM   5507  N N   . GLY E  1 52  ? 21.994  -51.321  -1.490  1.000 41.828  0 381 GLY EEE N   1 ? 18 
ATOM   5508  C CA  . GLY E  1 52  ? 21.354  -52.265  -0.568  1.000 42.049  0 381 GLY EEE CA  1 ? 18 
ATOM   5509  C C   . GLY E  1 52  ? 20.574  -51.612  0.551   1.000 44.365  0 381 GLY EEE C   1 ? 18 
ATOM   5510  O O   . GLY E  1 52  ? 19.977  -52.360  1.317   1.000 48.445  0 381 GLY EEE O   1 ? 18 
ATOM   5511  N N   . VAL E  1 53  ? 20.616  -50.286  0.692   1.000 46.187  0 382 VAL EEE N   1 ? 18 
ATOM   5512  C CA  . VAL E  1 53  ? 19.747  -49.529  1.654   1.000 47.194  0 382 VAL EEE CA  1 ? 18 
ATOM   5513  C C   . VAL E  1 53  ? 19.415  -48.177  1.040   1.000 45.022  0 382 VAL EEE C   1 ? 18 
ATOM   5514  O O   . VAL E  1 53  ? 20.273  -47.637  0.351   1.000 43.394  0 382 VAL EEE O   1 ? 18 
ATOM   5515  C CB  . VAL E  1 53  ? 20.413  -49.336  3.032   1.000 46.436  0 382 VAL EEE CB  1 ? 18 
ATOM   5516  C CG1 . VAL E  1 53  ? 20.652  -50.651  3.724   1.000 48.715  0 382 VAL EEE CG1 1 ? 18 
ATOM   5517  C CG2 . VAL E  1 53  ? 21.737  -48.644  2.908   1.000 44.837  0 382 VAL EEE CG2 1 ? 18 
ATOM   5518  N N   . SER E  1 54  ? 18.237  -47.635  1.309   1.000 45.701  0 383 SER EEE N   1 ? 18 
ATOM   5519  C CA  . SER E  1 54  ? 17.870  -46.275  0.846   1.000 47.308  0 383 SER EEE CA  1 ? 18 
ATOM   5520  C C   . SER E  1 54  ? 18.545  -45.265  1.766   1.000 46.669  0 383 SER EEE C   1 ? 18 
ATOM   5521  O O   . SER E  1 54  ? 18.527  -45.456  2.979   1.000 46.012  0 383 SER EEE O   1 ? 18 
ATOM   5522  C CB  . SER E  1 54  ? 16.380  -46.074  0.804   1.000 49.656  0 383 SER EEE CB  1 ? 18 
ATOM   5523  O OG  . SER E  1 54  ? 16.079  -44.724  0.472   1.000 51.802  0 383 SER EEE OG  1 ? 18 
ATOM   5524  N N   . PRO E  1 55  ? 19.165  -44.187  1.240   1.000 44.486  0 384 PRO EEE N   1 ? 18 
ATOM   5525  C CA  . PRO E  1 55  ? 19.693  -43.116  2.083   1.000 46.490  0 384 PRO EEE CA  1 ? 18 
ATOM   5526  C C   . PRO E  1 55  ? 18.649  -42.540  3.054   1.000 48.342  0 384 PRO EEE C   1 ? 18 
ATOM   5527  O O   . PRO E  1 55  ? 19.019  -42.083  4.123   1.000 50.556  0 384 PRO EEE O   1 ? 18 
ATOM   5528  C CB  . PRO E  1 55  ? 20.135  -42.033  1.085   1.000 46.385  0 384 PRO EEE CB  1 ? 18 
ATOM   5529  C CG  . PRO E  1 55  ? 20.425  -42.808  -0.179  1.000 46.798  0 384 PRO EEE CG  1 ? 18 
ATOM   5530  C CD  . PRO E  1 55  ? 19.425  -43.957  -0.184  1.000 46.515  0 384 PRO EEE CD  1 ? 18 
ATOM   5531  N N   . THR E  1 56  ? 17.376  -42.592  2.671   1.000 47.866  0 385 THR EEE N   1 ? 18 
ATOM   5532  C CA  . THR E  1 56  ? 16.244  -42.061  3.473   1.000 50.593  0 385 THR EEE CA  1 ? 18 
ATOM   5533  C C   . THR E  1 56  ? 16.023  -42.922  4.724   1.000 53.497  0 385 THR EEE C   1 ? 18 
ATOM   5534  O O   . THR E  1 56  ? 15.297  -42.478  5.604   1.000 56.269  0 385 THR EEE O   1 ? 18 
ATOM   5535  C CB  . THR E  1 56  ? 14.950  -41.976  2.647   1.000 51.166  0 385 THR EEE CB  1 ? 18 
ATOM   5536  O OG1 . THR E  1 56  ? 14.521  -43.290  2.264   1.000 51.306  0 385 THR EEE OG1 1 ? 18 
ATOM   5537  C CG2 . THR E  1 56  ? 15.096  -41.098  1.425   1.000 49.641  0 385 THR EEE CG2 1 ? 18 
ATOM   5538  N N   . LYS E  1 57  ? 16.588  -44.127  4.789   1.000 54.370  0 386 LYS EEE N   1 ? 18 
ATOM   5539  C CA  . LYS E  1 57  ? 16.302  -45.082  5.876   1.000 56.726  0 386 LYS EEE CA  1 ? 18 
ATOM   5540  C C   . LYS E  1 57  ? 17.501  -45.228  6.813   1.000 53.290  0 386 LYS EEE C   1 ? 18 
ATOM   5541  O O   . LYS E  1 57  ? 17.367  -45.975  7.755   1.000 54.133  0 386 LYS EEE O   1 ? 18 
ATOM   5542  C CB  . LYS E  1 57  ? 15.938  -46.428  5.262   1.000 61.221  0 386 LYS EEE CB  1 ? 18 
ATOM   5543  C CG  . LYS E  1 57  ? 14.632  -46.417  4.480   1.000 66.987  0 386 LYS EEE CG  1 ? 18 
ATOM   5544  C CD  . LYS E  1 57  ? 13.429  -46.667  5.347   1.000 73.268  0 386 LYS EEE CD  1 ? 18 
ATOM   5545  C CE  . LYS E  1 57  ? 13.397  -48.105  5.841   1.000 76.708  0 386 LYS EEE CE  1 ? 18 
ATOM   5546  N NZ  . LYS E  1 57  ? 13.020  -48.194  7.274   1.000 79.998  0 386 LYS EEE NZ  1 ? 18 
ATOM   5547  N N   . LEU E  1 58  ? 18.611  -44.533  6.589   1.000 50.139  0 387 LEU EEE N   1 ? 18 
ATOM   5548  C CA  . LEU E  1 58  ? 19.848  -44.742  7.386   1.000 49.928  0 387 LEU EEE CA  1 ? 18 
ATOM   5549  C C   . LEU E  1 58  ? 19.584  -44.524  8.881   1.000 51.288  0 387 LEU EEE C   1 ? 18 
ATOM   5550  O O   . LEU E  1 58  ? 20.185  -45.236  9.694   1.000 53.779  0 387 LEU EEE O   1 ? 18 
ATOM   5551  C CB  . LEU E  1 58  ? 20.955  -43.819  6.874   1.000 48.477  0 387 LEU EEE CB  1 ? 18 
ATOM   5552  C CG  . LEU E  1 58  ? 21.484  -44.162  5.481   1.000 48.320  0 387 LEU EEE CG  1 ? 18 
ATOM   5553  C CD1 . LEU E  1 58  ? 22.596  -43.232  5.063   1.000 48.357  0 387 LEU EEE CD1 1 ? 18 
ATOM   5554  C CD2 . LEU E  1 58  ? 21.986  -45.586  5.415   1.000 47.987  0 387 LEU EEE CD2 1 ? 18 
ATOM   5555  N N   . ASN E  1 59  ? 18.695  -43.612  9.251   1.000 52.795  0 388 ASN EEE N   1 ? 18 
ATOM   5556  C CA  . ASN E  1 59  ? 18.422  -43.305  10.678  1.000 53.880  0 388 ASN EEE CA  1 ? 18 
ATOM   5557  C C   . ASN E  1 59  ? 17.508  -44.358  11.301  1.000 54.024  0 388 ASN EEE C   1 ? 18 
ATOM   5558  O O   . ASN E  1 59  ? 17.316  -44.277  12.505  1.000 57.580  0 388 ASN EEE O   1 ? 18 
ATOM   5559  C CB  . ASN E  1 59  ? 17.856  -41.901  10.868  1.000 57.304  0 388 ASN EEE CB  1 ? 18 
ATOM   5560  C CG  . ASN E  1 59  ? 18.945  -40.863  10.988  1.000 57.959  0 388 ASN EEE CG  1 ? 18 
ATOM   5561  O OD1 . ASN E  1 59  ? 20.108  -41.186  11.159  1.000 57.031  0 388 ASN EEE OD1 1 ? 18 
ATOM   5562  N ND2 . ASN E  1 59  ? 18.575  -39.604  10.911  1.000 61.046  0 388 ASN EEE ND2 1 ? 18 
ATOM   5563  N N   . ASP E  1 60  ? 17.018  -45.347  10.556  1.000 54.031  0 389 ASP EEE N   1 ? 18 
ATOM   5564  C CA  . ASP E  1 60  ? 16.032  -46.343  11.053  1.000 56.499  0 389 ASP EEE CA  1 ? 18 
ATOM   5565  C C   . ASP E  1 60  ? 16.609  -47.754  11.064  1.000 54.321  0 389 ASP EEE C   1 ? 18 
ATOM   5566  O O   . ASP E  1 60  ? 15.842  -48.658  11.398  1.000 55.906  0 389 ASP EEE O   1 ? 18 
ATOM   5567  C CB  . ASP E  1 60  ? 14.778  -46.379  10.181  1.000 60.423  0 389 ASP EEE CB  1 ? 18 
ATOM   5568  C CG  . ASP E  1 60  ? 14.079  -45.041  10.102  1.000 64.186  0 389 ASP EEE CG  1 ? 18 
ATOM   5569  O OD1 . ASP E  1 60  ? 13.681  -44.511  11.178  1.000 68.404  0 389 ASP EEE OD1 1 ? 18 
ATOM   5570  O OD2 . ASP E  1 60  ? 13.952  -44.540  8.972   1.000 66.955  0 389 ASP EEE OD2 1 ? 18 
ATOM   5571  N N   . LEU E  1 61  ? 17.882  -47.951  10.713  1.000 50.745  0 390 LEU EEE N   1 ? 18 
ATOM   5572  C CA  . LEU E  1 61  ? 18.426  -49.320  10.528  1.000 50.129  0 390 LEU EEE CA  1 ? 18 
ATOM   5573  C C   . LEU E  1 61  ? 19.447  -49.616  11.629  1.000 51.497  0 390 LEU EEE C   1 ? 18 
ATOM   5574  O O   . LEU E  1 61  ? 20.124  -48.696  12.099  1.000 52.017  0 390 LEU EEE O   1 ? 18 
ATOM   5575  C CB  . LEU E  1 61  ? 19.047  -49.426  9.127   1.000 48.223  0 390 LEU EEE CB  1 ? 18 
ATOM   5576  C CG  . LEU E  1 61  ? 18.084  -49.253  7.954   1.000 48.936  0 390 LEU EEE CG  1 ? 18 
ATOM   5577  C CD1 . LEU E  1 61  ? 18.816  -49.317  6.611   1.000 48.559  0 390 LEU EEE CD1 1 ? 18 
ATOM   5578  C CD2 . LEU E  1 61  ? 16.975  -50.283  7.986   1.000 50.841  0 390 LEU EEE CD2 1 ? 18 
ATOM   5579  N N   . CYS E  1 62  ? 19.626  -50.891  11.955  1.000 53.547  0 391 CYS EEE N   1 ? 18 
ATOM   5580  C CA  . CYS E  1 62  ? 20.689  -51.423  12.844  1.000 54.487  0 391 CYS EEE CA  1 ? 18 
ATOM   5581  C C   . CYS E  1 62  ? 21.630  -52.320  12.033  1.000 51.920  0 391 CYS EEE C   1 ? 18 
ATOM   5582  O O   . CYS E  1 62  ? 21.148  -52.983  11.120  1.000 49.774  0 391 CYS EEE O   1 ? 18 
ATOM   5583  C CB  . CYS E  1 62  ? 20.051  -52.190  13.995  1.000 59.030  0 391 CYS EEE CB  1 ? 18 
ATOM   5584  S SG  . CYS E  1 62  ? 19.177  -51.090  15.142  1.000 64.814  0 391 CYS EEE SG  1 ? 18 
ATOM   5585  N N   . PHE E  1 63  ? 22.918  -52.307  12.359  1.000 52.254  0 392 PHE EEE N   1 ? 18 
ATOM   5586  C CA  . PHE E  1 63  ? 23.970  -53.126  11.706  1.000 51.735  0 392 PHE EEE CA  1 ? 18 
ATOM   5587  C C   . PHE E  1 63  ? 24.834  -53.780  12.795  1.000 54.909  0 392 PHE EEE C   1 ? 18 
ATOM   5588  O O   . PHE E  1 63  ? 24.870  -53.241  13.940  1.000 57.793  0 392 PHE EEE O   1 ? 18 
ATOM   5589  C CB  . PHE E  1 63  ? 24.773  -52.249  10.747  1.000 48.551  0 392 PHE EEE CB  1 ? 18 
ATOM   5590  C CG  . PHE E  1 63  ? 23.940  -51.605  9.678   1.000 47.297  0 392 PHE EEE CG  1 ? 18 
ATOM   5591  C CD1 . PHE E  1 63  ? 23.392  -52.361  8.669   1.000 47.268  0 392 PHE EEE CD1 1 ? 18 
ATOM   5592  C CD2 . PHE E  1 63  ? 23.666  -50.252  9.691   1.000 46.947  0 392 PHE EEE CD2 1 ? 18 
ATOM   5593  C CE1 . PHE E  1 63  ? 22.619  -51.787  7.670   1.000 46.094  0 392 PHE EEE CE1 1 ? 18 
ATOM   5594  C CE2 . PHE E  1 63  ? 22.880  -49.669  8.701   1.000 46.421  0 392 PHE EEE CE2 1 ? 18 
ATOM   5595  C CZ  . PHE E  1 63  ? 22.345  -50.443  7.704   1.000 46.822  0 392 PHE EEE CZ  1 ? 18 
ATOM   5596  N N   . THR E  1 64  ? 25.463  -54.907  12.456  1.000 56.707  0 393 THR EEE N   1 ? 18 
ATOM   5597  C CA  . THR E  1 64  ? 26.392  -55.665  13.327  1.000 59.638  0 393 THR EEE CA  1 ? 18 
ATOM   5598  C C   . THR E  1 64  ? 27.679  -54.860  13.448  1.000 58.483  0 393 THR EEE C   1 ? 18 
ATOM   5599  O O   . THR E  1 64  ? 28.297  -54.877  14.504  1.000 62.218  0 393 THR EEE O   1 ? 18 
ATOM   5600  C CB  . THR E  1 64  ? 26.800  -57.006  12.683  1.000 61.350  0 393 THR EEE CB  1 ? 18 
ATOM   5601  O OG1 . THR E  1 64  ? 25.747  -57.508  11.896  1.000 59.427  0 393 THR EEE OG1 1 ? 18 
ATOM   5602  C CG2 . THR E  1 64  ? 27.165  -58.099  13.653  1.000 67.263  0 393 THR EEE CG2 1 ? 18 
ATOM   5603  N N   . ASN E  1 65  ? 28.061  -54.198  12.358  1.000 55.722  0 394 ASN EEE N   1 ? 18 
ATOM   5604  C CA  . ASN E  1 65  ? 29.354  -53.490  12.244  1.000 55.925  0 394 ASN EEE CA  1 ? 18 
ATOM   5605  C C   . ASN E  1 65  ? 29.238  -52.402  11.187  1.000 49.596  0 394 ASN EEE C   1 ? 18 
ATOM   5606  O O   . ASN E  1 65  ? 28.477  -52.631  10.206  1.000 47.827  0 394 ASN EEE O   1 ? 18 
ATOM   5607  C CB  . ASN E  1 65  ? 30.455  -54.487  11.891  1.000 61.166  0 394 ASN EEE CB  1 ? 18 
ATOM   5608  C CG  . ASN E  1 65  ? 31.827  -53.922  12.093  1.000 66.391  0 394 ASN EEE CG  1 ? 18 
ATOM   5609  O OD1 . ASN E  1 65  ? 32.222  -53.668  13.231  1.000 71.134  0 394 ASN EEE OD1 1 ? 18 
ATOM   5610  N ND2 . ASN E  1 65  ? 32.525  -53.719  10.989  1.000 67.800  0 394 ASN EEE ND2 1 ? 18 
ATOM   5611  N N   . VAL E  1 66  ? 29.933  -51.290  11.374  1.000 45.929  0 395 VAL EEE N   1 ? 18 
ATOM   5612  C CA  . VAL E  1 66  ? 30.080  -50.274  10.304  1.000 43.989  0 395 VAL EEE CA  1 ? 18 
ATOM   5613  C C   . VAL E  1 66  ? 31.564  -49.970  10.165  1.000 43.409  0 395 VAL EEE C   1 ? 18 
ATOM   5614  O O   . VAL E  1 66  ? 32.231  -49.853  11.214  1.000 45.223  0 395 VAL EEE O   1 ? 18 
ATOM   5615  C CB  . VAL E  1 66  ? 29.263  -48.998  10.572  1.000 44.611  0 395 VAL EEE CB  1 ? 18 
ATOM   5616  C CG1 . VAL E  1 66  ? 29.449  -47.972  9.477   1.000 41.687  0 395 VAL EEE CG1 1 ? 18 
ATOM   5617  C CG2 . VAL E  1 66  ? 27.795  -49.315  10.776  1.000 46.964  0 395 VAL EEE CG2 1 ? 18 
ATOM   5618  N N   . TYR E  1 67  ? 32.061  -49.873  8.930   1.000 43.112  0 396 TYR EEE N   1 ? 18 
ATOM   5619  C CA  . TYR E  1 67  ? 33.422  -49.409  8.617   1.000 42.187  0 396 TYR EEE CA  1 ? 18 
ATOM   5620  C C   . TYR E  1 67  ? 33.319  -48.138  7.786   1.000 40.687  0 396 TYR EEE C   1 ? 18 
ATOM   5621  O O   . TYR E  1 67  ? 32.507  -48.064  6.866   1.000 38.170  0 396 TYR EEE O   1 ? 18 
ATOM   5622  C CB  . TYR E  1 67  ? 34.197  -50.497  7.878   1.000 44.167  0 396 TYR EEE CB  1 ? 18 
ATOM   5623  C CG  . TYR E  1 67  ? 34.494  -51.695  8.727   1.000 49.136  0 396 TYR EEE CG  1 ? 18 
ATOM   5624  C CD1 . TYR E  1 67  ? 35.297  -51.569  9.850   1.000 52.052  0 396 TYR EEE CD1 1 ? 18 
ATOM   5625  C CD2 . TYR E  1 67  ? 34.177  -52.972  8.302   1.000 53.526  0 396 TYR EEE CD2 1 ? 18 
ATOM   5626  C CE1 . TYR E  1 67  ? 35.674  -52.665  10.605  1.000 56.216  0 396 TYR EEE CE1 1 ? 18 
ATOM   5627  C CE2 . TYR E  1 67  ? 34.565  -54.093  9.021   1.000 57.423  0 396 TYR EEE CE2 1 ? 18 
ATOM   5628  C CZ  . TYR E  1 67  ? 35.325  -53.936  10.174  1.000 59.893  0 396 TYR EEE CZ  1 ? 18 
ATOM   5629  O OH  . TYR E  1 67  ? 35.668  -55.008  10.946  1.000 64.709  0 396 TYR EEE OH  1 ? 18 
ATOM   5630  N N   . ALA E  1 68  ? 34.165  -47.165  8.107   1.000 42.879  0 397 ALA EEE N   1 ? 18 
ATOM   5631  C CA  . ALA E  1 68  ? 34.391  -45.924  7.337   1.000 40.964  0 397 ALA EEE CA  1 ? 18 
ATOM   5632  C C   . ALA E  1 68  ? 35.791  -45.975  6.739   1.000 38.802  0 397 ALA EEE C   1 ? 18 
ATOM   5633  O O   . ALA E  1 68  ? 36.756  -45.878  7.487   1.000 41.708  0 397 ALA EEE O   1 ? 18 
ATOM   5634  C CB  . ALA E  1 68  ? 34.191  -44.703  8.206   1.000 41.895  0 397 ALA EEE CB  1 ? 18 
ATOM   5635  N N   . ASP E  1 69  ? 35.858  -46.191  5.440   1.000 37.744  0 398 ASP EEE N   1 ? 18 
ATOM   5636  C CA  . ASP E  1 69  ? 37.083  -46.150  4.611   1.000 38.972  0 398 ASP EEE CA  1 ? 18 
ATOM   5637  C C   . ASP E  1 69  ? 37.141  -44.773  3.968   1.000 40.189  0 398 ASP EEE C   1 ? 18 
ATOM   5638  O O   . ASP E  1 69  ? 36.123  -44.292  3.467   1.000 41.338  0 398 ASP EEE O   1 ? 18 
ATOM   5639  C CB  . ASP E  1 69  ? 37.083  -47.250  3.542   1.000 40.589  0 398 ASP EEE CB  1 ? 18 
ATOM   5640  C CG  . ASP E  1 69  ? 36.903  -48.649  4.106   1.000 40.374  0 398 ASP EEE CG  1 ? 18 
ATOM   5641  O OD1 . ASP E  1 69  ? 37.320  -48.851  5.281   1.000 39.103  0 398 ASP EEE OD1 1 ? 18 
ATOM   5642  O OD2 . ASP E  1 69  ? 36.315  -49.506  3.399   1.000 42.031  0 398 ASP EEE OD2 1 ? 18 
ATOM   5643  N N   . SER E  1 70  ? 38.290  -44.121  4.021   1.000 41.417  0 399 SER EEE N   1 ? 18 
ATOM   5644  C CA  . SER E  1 70  ? 38.440  -42.740  3.512   1.000 41.266  0 399 SER EEE CA  1 ? 18 
ATOM   5645  C C   . SER E  1 70  ? 39.812  -42.601  2.860   1.000 43.073  0 399 SER EEE C   1 ? 18 
ATOM   5646  O O   . SER E  1 70  ? 40.788  -43.278  3.295   1.000 45.346  0 399 SER EEE O   1 ? 18 
ATOM   5647  C CB  . SER E  1 70  ? 38.229  -41.715  4.595   1.000 41.685  0 399 SER EEE CB  1 ? 18 
ATOM   5648  O OG  . SER E  1 70  ? 39.048  -42.001  5.711   1.000 45.924  0 399 SER EEE OG  1 ? 18 
ATOM   5649  N N   . PHE E  1 71  ? 39.880  -41.744  1.852   1.000 40.887  0 400 PHE EEE N   1 ? 18 
ATOM   5650  C CA  . PHE E  1 71  ? 41.087  -41.530  1.029   1.000 41.684  0 400 PHE EEE CA  1 ? 18 
ATOM   5651  C C   . PHE E  1 71  ? 40.835  -40.380  0.055   1.000 40.587  0 400 PHE EEE C   1 ? 18 
ATOM   5652  O O   . PHE E  1 71  ? 39.685  -39.895  -0.039  1.000 39.525  0 400 PHE EEE O   1 ? 18 
ATOM   5653  C CB  . PHE E  1 71  ? 41.426  -42.810  0.270   1.000 42.954  0 400 PHE EEE CB  1 ? 18 
ATOM   5654  C CG  . PHE E  1 71  ? 40.263  -43.426  -0.465  1.000 42.625  0 400 PHE EEE CG  1 ? 18 
ATOM   5655  C CD1 . PHE E  1 71  ? 39.861  -42.938  -1.702  1.000 42.429  0 400 PHE EEE CD1 1 ? 18 
ATOM   5656  C CD2 . PHE E  1 71  ? 39.576  -44.501  0.072   1.000 42.111  0 400 PHE EEE CD2 1 ? 18 
ATOM   5657  C CE1 . PHE E  1 71  ? 38.791  -43.515  -2.378  1.000 43.740  0 400 PHE EEE CE1 1 ? 18 
ATOM   5658  C CE2 . PHE E  1 71  ? 38.522  -45.092  -0.616  1.000 42.626  0 400 PHE EEE CE2 1 ? 18 
ATOM   5659  C CZ  . PHE E  1 71  ? 38.115  -44.586  -1.829  1.000 42.830  0 400 PHE EEE CZ  1 ? 18 
ATOM   5660  N N   . VAL E  1 72  ? 41.879  -40.001  -0.684  1.000 39.662  0 401 VAL EEE N   1 ? 18 
ATOM   5661  C CA  . VAL E  1 72  ? 41.809  -38.956  -1.745  1.000 40.309  0 401 VAL EEE CA  1 ? 18 
ATOM   5662  C C   . VAL E  1 72  ? 42.090  -39.601  -3.107  1.000 39.007  0 401 VAL EEE C   1 ? 18 
ATOM   5663  O O   . VAL E  1 72  ? 43.026  -40.425  -3.214  1.000 38.536  0 401 VAL EEE O   1 ? 18 
ATOM   5664  C CB  . VAL E  1 72  ? 42.782  -37.809  -1.429  1.000 40.733  0 401 VAL EEE CB  1 ? 18 
ATOM   5665  C CG1 . VAL E  1 72  ? 42.936  -36.859  -2.596  1.000 41.209  0 401 VAL EEE CG1 1 ? 18 
ATOM   5666  C CG2 . VAL E  1 72  ? 42.329  -37.049  -0.189  1.000 42.322  0 401 VAL EEE CG2 1 ? 18 
ATOM   5667  N N   . ILE E  1 73  ? 41.314  -39.204  -4.108  1.000 38.691  0 402 ILE EEE N   1 ? 18 
ATOM   5668  C CA  . ILE E  1 73  ? 41.535  -39.539  -5.552  1.000 40.741  0 402 ILE EEE CA  1 ? 18 
ATOM   5669  C C   . ILE E  1 73  ? 41.207  -38.286  -6.383  1.000 42.280  0 402 ILE EEE C   1 ? 18 
ATOM   5670  O O   . ILE E  1 73  ? 40.806  -37.263  -5.794  1.000 42.316  0 402 ILE EEE O   1 ? 18 
ATOM   5671  C CB  . ILE E  1 73  ? 40.686  -40.766  -5.945  1.000 37.944  0 402 ILE EEE CB  1 ? 18 
ATOM   5672  C CG1 . ILE E  1 73  ? 39.205  -40.582  -5.581  1.000 37.154  0 402 ILE EEE CG1 1 ? 18 
ATOM   5673  C CG2 . ILE E  1 73  ? 41.249  -42.026  -5.313  1.000 37.252  0 402 ILE EEE CG2 1 ? 18 
ATOM   5674  C CD1 . ILE E  1 73  ? 38.306  -41.669  -6.107  1.000 36.576  0 402 ILE EEE CD1 1 ? 18 
ATOM   5675  N N   . ARG E  1 74  ? 41.413  -38.351  -7.696  1.000 45.506  0 403 ARG EEE N   1 ? 18 
ATOM   5676  C CA  . ARG E  1 74  ? 40.974  -37.296  -8.655  1.000 48.082  0 403 ARG EEE CA  1 ? 18 
ATOM   5677  C C   . ARG E  1 74  ? 39.451  -37.319  -8.796  1.000 48.437  0 403 ARG EEE C   1 ? 18 
ATOM   5678  O O   . ARG E  1 74  ? 38.865  -38.420  -8.693  1.000 47.562  0 403 ARG EEE O   1 ? 18 
ATOM   5679  C CB  . ARG E  1 74  ? 41.476  -37.573  -10.069 1.000 51.930  0 403 ARG EEE CB  1 ? 18 
ATOM   5680  C CG  . ARG E  1 74  ? 42.950  -37.283  -10.298 1.000 56.691  0 403 ARG EEE CG  1 ? 18 
ATOM   5681  C CD  . ARG E  1 74  ? 43.448  -38.012  -11.535 1.000 57.815  0 403 ARG EEE CD  1 ? 18 
ATOM   5682  N NE  . ARG E  1 74  ? 42.615  -37.653  -12.682 1.000 59.521  0 403 ARG EEE NE  1 ? 18 
ATOM   5683  C CZ  . ARG E  1 74  ? 42.783  -38.134  -13.904 1.000 64.169  0 403 ARG EEE CZ  1 ? 18 
ATOM   5684  N NH1 . ARG E  1 74  ? 43.850  -38.864  -14.192 1.000 65.587  0 403 ARG EEE NH1 1 ? 18 
ATOM   5685  N NH2 . ARG E  1 74  ? 41.970  -37.771  -14.875 1.000 66.148  0 403 ARG EEE NH2 1 ? 18 
ATOM   5686  N N   . GLY E  1 75  ? 38.856  -36.175  -9.137  1.000 48.150  0 404 GLY EEE N   1 ? 18 
ATOM   5687  C CA  . GLY E  1 75  ? 37.419  -36.036  -9.421  1.000 44.672  0 404 GLY EEE CA  1 ? 18 
ATOM   5688  C C   . GLY E  1 75  ? 36.924  -37.111  -10.370 1.000 44.860  0 404 GLY EEE C   1 ? 18 
ATOM   5689  O O   . GLY E  1 75  ? 35.929  -37.739  -10.060 1.000 42.361  0 404 GLY EEE O   1 ? 18 
ATOM   5690  N N   . ASP E  1 76  ? 37.580  -37.334  -11.505 1.000 47.868  0 405 ASP EEE N   1 ? 18 
ATOM   5691  C CA  . ASP E  1 76  ? 37.012  -38.242  -12.535 1.000 51.287  0 405 ASP EEE CA  1 ? 18 
ATOM   5692  C C   . ASP E  1 76  ? 37.365  -39.701  -12.205 1.000 50.095  0 405 ASP EEE C   1 ? 18 
ATOM   5693  O O   . ASP E  1 76  ? 36.939  -40.570  -12.947 1.000 50.118  0 405 ASP EEE O   1 ? 18 
ATOM   5694  C CB  . ASP E  1 76  ? 37.279  -37.775  -13.971 1.000 56.939  0 405 ASP EEE CB  1 ? 18 
ATOM   5695  C CG  . ASP E  1 76  ? 38.718  -37.468  -14.294 1.000 64.707  0 405 ASP EEE CG  1 ? 18 
ATOM   5696  O OD1 . ASP E  1 76  ? 39.598  -38.069  -13.634 1.000 66.961  0 405 ASP EEE OD1 1 ? 18 
ATOM   5697  O OD2 . ASP E  1 76  ? 38.946  -36.638  -15.226 1.000 72.783  0 405 ASP EEE OD2 1 ? 18 
ATOM   5698  N N   . GLU E  1 77  ? 37.994  -39.988  -11.065 1.000 47.502  0 406 GLU EEE N   1 ? 18 
ATOM   5699  C CA  . GLU E  1 77  ? 38.148  -41.380  -10.568 1.000 44.459  0 406 GLU EEE CA  1 ? 18 
ATOM   5700  C C   . GLU E  1 77  ? 37.023  -41.734  -9.579  1.000 44.765  0 406 GLU EEE C   1 ? 18 
ATOM   5701  O O   . GLU E  1 77  ? 36.876  -42.929  -9.242  1.000 42.880  0 406 GLU EEE O   1 ? 18 
ATOM   5702  C CB  . GLU E  1 77  ? 39.532  -41.570  -9.942  1.000 43.457  0 406 GLU EEE CB  1 ? 18 
ATOM   5703  C CG  . GLU E  1 77  ? 40.669  -41.609  -10.959 1.000 45.620  0 406 GLU EEE CG  1 ? 18 
ATOM   5704  C CD  . GLU E  1 77  ? 42.070  -41.543  -10.350 1.000 46.465  0 406 GLU EEE CD  1 ? 18 
ATOM   5705  O OE1 . GLU E  1 77  ? 42.187  -41.127  -9.166  1.000 43.605  0 406 GLU EEE OE1 1 ? 18 
ATOM   5706  O OE2 . GLU E  1 77  ? 43.055  -41.907  -11.053 1.000 48.195  0 406 GLU EEE OE2 1 ? 18 
ATOM   5707  N N   . VAL E  1 78  ? 36.233  -40.764  -9.106  1.000 45.105  0 407 VAL EEE N   1 ? 18 
ATOM   5708  C CA  . VAL E  1 78  ? 35.179  -41.028  -8.075  1.000 41.578  0 407 VAL EEE CA  1 ? 18 
ATOM   5709  C C   . VAL E  1 78  ? 34.180  -42.059  -8.614  1.000 42.061  0 407 VAL EEE C   1 ? 18 
ATOM   5710  O O   . VAL E  1 78  ? 33.767  -42.888  -7.832  1.000 41.103  0 407 VAL EEE O   1 ? 18 
ATOM   5711  C CB  . VAL E  1 78  ? 34.500  -39.728  -7.607  1.000 42.621  0 407 VAL EEE CB  1 ? 18 
ATOM   5712  C CG1 . VAL E  1 78  ? 33.236  -39.967  -6.795  1.000 41.891  0 407 VAL EEE CG1 1 ? 18 
ATOM   5713  C CG2 . VAL E  1 78  ? 35.474  -38.857  -6.822  1.000 45.992  0 407 VAL EEE CG2 1 ? 18 
ATOM   5714  N N   . ARG E  1 79  ? 33.846  -42.053  -9.902  1.000 44.259  0 408 ARG EEE N   1 ? 18 
ATOM   5715  C CA  . ARG E  1 79  ? 32.939  -43.049  -10.535 1.000 46.404  0 408 ARG EEE CA  1 ? 18 
ATOM   5716  C C   . ARG E  1 79  ? 33.440  -44.489  -10.308 1.000 45.957  0 408 ARG EEE C   1 ? 18 
ATOM   5717  O O   . ARG E  1 79  ? 32.618  -45.411  -10.436 1.000 48.356  0 408 ARG EEE O   1 ? 18 
ATOM   5718  C CB  . ARG E  1 79  ? 32.795  -42.747  -12.026 1.000 52.167  0 408 ARG EEE CB  1 ? 18 
ATOM   5719  C CG  . ARG E  1 79  ? 34.080  -42.972  -12.805 1.000 60.348  0 408 ARG EEE CG  1 ? 18 
ATOM   5720  C CD  . ARG E  1 79  ? 33.922  -42.991  -14.303 1.000 68.447  0 408 ARG EEE CD  1 ? 18 
ATOM   5721  N NE  . ARG E  1 79  ? 33.186  -44.213  -14.645 1.000 78.672  0 408 ARG EEE NE  1 ? 18 
ATOM   5722  C CZ  . ARG E  1 79  ? 31.945  -44.282  -15.164 1.000 82.538  0 408 ARG EEE CZ  1 ? 18 
ATOM   5723  N NH1 . ARG E  1 79  ? 31.258  -43.181  -15.453 1.000 81.492  0 408 ARG EEE NH1 1 ? 18 
ATOM   5724  N NH2 . ARG E  1 79  ? 31.409  -45.471  -15.383 1.000 81.526  0 408 ARG EEE NH2 1 ? 18 
ATOM   5725  N N   . GLN E  1 80  ? 34.730  -44.707  -10.021 1.000 44.594  0 409 GLN EEE N   1 ? 18 
ATOM   5726  C CA  . GLN E  1 80  ? 35.308  -46.064  -9.829  1.000 43.281  0 409 GLN EEE CA  1 ? 18 
ATOM   5727  C C   . GLN E  1 80  ? 34.989  -46.585  -8.419  1.000 41.419  0 409 GLN EEE C   1 ? 18 
ATOM   5728  O O   . GLN E  1 80  ? 35.122  -47.787  -8.187  1.000 39.317  0 409 GLN EEE O   1 ? 18 
ATOM   5729  C CB  . GLN E  1 80  ? 36.818  -46.060  -10.047 1.000 44.158  0 409 GLN EEE CB  1 ? 18 
ATOM   5730  C CG  . GLN E  1 80  ? 37.214  -45.901  -11.504 1.000 47.836  0 409 GLN EEE CG  1 ? 18 
ATOM   5731  C CD  . GLN E  1 80  ? 38.707  -45.989  -11.729 1.000 49.347  0 409 GLN EEE CD  1 ? 18 
ATOM   5732  O OE1 . GLN E  1 80  ? 39.399  -46.888  -11.228 1.000 52.576  0 409 GLN EEE OE1 1 ? 18 
ATOM   5733  N NE2 . GLN E  1 80  ? 39.210  -45.044  -12.507 1.000 48.719  0 409 GLN EEE NE2 1 ? 18 
ATOM   5734  N N   . ILE E  1 81  ? 34.582  -45.725  -7.498  1.000 38.796  0 410 ILE EEE N   1 ? 18 
ATOM   5735  C CA  . ILE E  1 81  ? 34.255  -46.146  -6.109  1.000 38.873  0 410 ILE EEE CA  1 ? 18 
ATOM   5736  C C   . ILE E  1 81  ? 32.781  -46.529  -6.103  1.000 39.076  0 410 ILE EEE C   1 ? 18 
ATOM   5737  O O   . ILE E  1 81  ? 31.932  -45.819  -5.513  1.000 41.280  0 410 ILE EEE O   1 ? 18 
ATOM   5738  C CB  . ILE E  1 81  ? 34.599  -45.063  -5.071  1.000 38.329  0 410 ILE EEE CB  1 ? 18 
ATOM   5739  C CG1 . ILE E  1 81  ? 35.974  -44.457  -5.347  1.000 39.588  0 410 ILE EEE CG1 1 ? 18 
ATOM   5740  C CG2 . ILE E  1 81  ? 34.521  -45.633  -3.675  1.000 39.383  0 410 ILE EEE CG2 1 ? 18 
ATOM   5741  C CD1 . ILE E  1 81  ? 37.093  -45.473  -5.416  1.000 41.820  0 410 ILE EEE CD1 1 ? 18 
ATOM   5742  N N   . ALA E  1 82  ? 32.496  -47.655  -6.728  1.000 41.117  0 411 ALA EEE N   1 ? 18 
ATOM   5743  C CA  . ALA E  1 82  ? 31.137  -48.181  -6.943  1.000 41.293  0 411 ALA EEE CA  1 ? 18 
ATOM   5744  C C   . ALA E  1 82  ? 31.256  -49.646  -7.338  1.000 41.992  0 411 ALA EEE C   1 ? 18 
ATOM   5745  O O   . ALA E  1 82  ? 32.221  -50.041  -7.982  1.000 42.897  0 411 ALA EEE O   1 ? 18 
ATOM   5746  C CB  . ALA E  1 82  ? 30.422  -47.370  -8.004  1.000 38.943  0 411 ALA EEE CB  1 ? 18 
ATOM   5747  N N   . PRO E  1 83  ? 30.270  -50.489  -6.989  1.000 42.596  0 412 PRO EEE N   1 ? 18 
ATOM   5748  C CA  . PRO E  1 83  ? 30.290  -51.882  -7.412  1.000 45.403  0 412 PRO EEE CA  1 ? 18 
ATOM   5749  C C   . PRO E  1 83  ? 30.357  -51.986  -8.944  1.000 45.654  0 412 PRO EEE C   1 ? 18 
ATOM   5750  O O   . PRO E  1 83  ? 29.719  -51.208  -9.593  1.000 47.932  0 412 PRO EEE O   1 ? 18 
ATOM   5751  C CB  . PRO E  1 83  ? 28.963  -52.403  -6.855  1.000 45.920  0 412 PRO EEE CB  1 ? 18 
ATOM   5752  C CG  . PRO E  1 83  ? 28.096  -51.177  -6.702  1.000 45.070  0 412 PRO EEE CG  1 ? 18 
ATOM   5753  C CD  . PRO E  1 83  ? 29.086  -50.171  -6.181  1.000 42.841  0 412 PRO EEE CD  1 ? 18 
ATOM   5754  N N   . GLY E  1 84  ? 31.155  -52.924  -9.448  1.000 46.412  0 413 GLY EEE N   1 ? 18 
ATOM   5755  C CA  . GLY E  1 84  ? 31.183  -53.340  -10.859 1.000 48.293  0 413 GLY EEE CA  1 ? 18 
ATOM   5756  C C   . GLY E  1 84  ? 32.083  -52.470  -11.714 1.000 50.708  0 413 GLY EEE C   1 ? 18 
ATOM   5757  O O   . GLY E  1 84  ? 31.987  -52.592  -12.933 1.000 54.016  0 413 GLY EEE O   1 ? 18 
ATOM   5758  N N   . GLN E  1 85  ? 32.916  -51.601  -11.115 1.000 51.437  0 414 GLN EEE N   1 ? 18 
ATOM   5759  C CA  . GLN E  1 85  ? 33.765  -50.629  -11.869 1.000 49.158  0 414 GLN EEE CA  1 ? 18 
ATOM   5760  C C   . GLN E  1 85  ? 35.140  -51.225  -12.160 1.000 49.519  0 414 GLN EEE C   1 ? 18 
ATOM   5761  O O   . GLN E  1 85  ? 35.572  -52.097  -11.384 1.000 49.880  0 414 GLN EEE O   1 ? 18 
ATOM   5762  C CB  . GLN E  1 85  ? 33.923  -49.350  -11.053 1.000 48.096  0 414 GLN EEE CB  1 ? 18 
ATOM   5763  C CG  . GLN E  1 85  ? 32.640  -48.546  -10.958 1.000 48.097  0 414 GLN EEE CG  1 ? 18 
ATOM   5764  C CD  . GLN E  1 85  ? 32.139  -48.072  -12.289 1.000 47.938  0 414 GLN EEE CD  1 ? 18 
ATOM   5765  O OE1 . GLN E  1 85  ? 32.909  -47.664  -13.140 1.000 52.494  0 414 GLN EEE OE1 1 ? 18 
ATOM   5766  N NE2 . GLN E  1 85  ? 30.839  -48.091  -12.456 1.000 50.107  0 414 GLN EEE NE2 1 ? 18 
ATOM   5767  N N   . THR E  1 86  ? 35.801  -50.768  -13.223 1.000 50.628  0 415 THR EEE N   1 ? 18 
ATOM   5768  C CA  . THR E  1 86  ? 37.239  -51.044  -13.497 1.000 52.275  0 415 THR EEE CA  1 ? 18 
ATOM   5769  C C   . THR E  1 86  ? 37.989  -49.728  -13.726 1.000 51.312  0 415 THR EEE C   1 ? 18 
ATOM   5770  O O   . THR E  1 86  ? 37.325  -48.690  -13.909 1.000 51.985  0 415 THR EEE O   1 ? 18 
ATOM   5771  C CB  . THR E  1 86  ? 37.436  -51.996  -14.678 1.000 55.191  0 415 THR EEE CB  1 ? 18 
ATOM   5772  O OG1 . THR E  1 86  ? 36.774  -51.408  -15.793 1.000 53.757  0 415 THR EEE OG1 1 ? 18 
ATOM   5773  C CG2 . THR E  1 86  ? 36.912  -53.387  -14.392 1.000 56.731  0 415 THR EEE CG2 1 ? 18 
ATOM   5774  N N   . GLY E  1 87  ? 39.325  -49.800  -13.693 1.000 50.545  0 416 GLY EEE N   1 ? 18 
ATOM   5775  C CA  . GLY E  1 87  ? 40.258  -48.659  -13.779 1.000 48.514  0 416 GLY EEE CA  1 ? 18 
ATOM   5776  C C   . GLY E  1 87  ? 41.377  -48.824  -12.776 1.000 48.640  0 416 GLY EEE C   1 ? 18 
ATOM   5777  O O   . GLY E  1 87  ? 41.291  -49.764  -11.967 1.000 45.805  0 416 GLY EEE O   1 ? 18 
ATOM   5778  N N   . LYS E  1 88  ? 42.391  -47.950  -12.830 1.000 51.449  0 417 LYS EEE N   1 ? 18 
ATOM   5779  C CA  . LYS E  1 88  ? 43.564  -48.000  -11.923 1.000 53.070  0 417 LYS EEE CA  1 ? 18 
ATOM   5780  C C   . LYS E  1 88  ? 43.058  -48.117  -10.493 1.000 51.316  0 417 LYS EEE C   1 ? 18 
ATOM   5781  O O   . LYS E  1 88  ? 43.615  -48.952  -9.761  1.000 53.581  0 417 LYS EEE O   1 ? 18 
ATOM   5782  C CB  . LYS E  1 88  ? 44.458  -46.754  -12.018 1.000 57.311  0 417 LYS EEE CB  1 ? 18 
ATOM   5783  C CG  . LYS E  1 88  ? 45.152  -46.521  -13.337 1.000 64.181  0 417 LYS EEE CG  1 ? 18 
ATOM   5784  C CD  . LYS E  1 88  ? 45.965  -47.755  -13.746 1.000 69.622  0 417 LYS EEE CD  1 ? 18 
ATOM   5785  C CE  . LYS E  1 88  ? 46.526  -47.693  -15.151 1.000 74.961  0 417 LYS EEE CE  1 ? 18 
ATOM   5786  N NZ  . LYS E  1 88  ? 46.329  -48.973  -15.892 1.000 77.645  0 417 LYS EEE NZ  1 ? 18 
ATOM   5787  N N   . ILE E  1 89  ? 42.044  -47.330  -10.111 1.000 47.235  0 418 ILE EEE N   1 ? 18 
ATOM   5788  C CA  . ILE E  1 89  ? 41.646  -47.221  -8.683  1.000 45.704  0 418 ILE EEE CA  1 ? 18 
ATOM   5789  C C   . ILE E  1 89  ? 40.876  -48.486  -8.278  1.000 44.672  0 418 ILE EEE C   1 ? 18 
ATOM   5790  O O   . ILE E  1 89  ? 41.304  -49.144  -7.323  1.000 41.897  0 418 ILE EEE O   1 ? 18 
ATOM   5791  C CB  . ILE E  1 89  ? 40.883  -45.906  -8.406  1.000 45.046  0 418 ILE EEE CB  1 ? 18 
ATOM   5792  C CG1 . ILE E  1 89  ? 41.652  -44.669  -8.892  1.000 46.832  0 418 ILE EEE CG1 1 ? 18 
ATOM   5793  C CG2 . ILE E  1 89  ? 40.557  -45.806  -6.926  1.000 43.057  0 418 ILE EEE CG2 1 ? 18 
ATOM   5794  C CD1 . ILE E  1 89  ? 43.068  -44.585  -8.355  1.000 49.335  0 418 ILE EEE CD1 1 ? 18 
ATOM   5795  N N   . ALA E  1 90  ? 39.804  -48.836  -8.989  1.000 45.604  0 419 ALA EEE N   1 ? 18 
ATOM   5796  C CA  . ALA E  1 90  ? 38.996  -50.050  -8.711  1.000 46.118  0 419 ALA EEE CA  1 ? 18 
ATOM   5797  C C   . ALA E  1 90  ? 39.895  -51.298  -8.731  1.000 47.994  0 419 ALA EEE C   1 ? 18 
ATOM   5798  O O   . ALA E  1 90  ? 39.699  -52.177  -7.872  1.000 47.490  0 419 ALA EEE O   1 ? 18 
ATOM   5799  C CB  . ALA E  1 90  ? 37.853  -50.180  -9.700  1.000 46.742  0 419 ALA EEE CB  1 ? 18 
ATOM   5800  N N   . ASP E  1 91  ? 40.846  -51.380  -9.665  1.000 48.723  0 420 ASP EEE N   1 ? 18 
ATOM   5801  C CA  . ASP E  1 91  ? 41.623  -52.619  -9.918  1.000 50.986  0 420 ASP EEE CA  1 ? 18 
ATOM   5802  C C   . ASP E  1 91  ? 42.786  -52.738  -8.924  1.000 51.487  0 420 ASP EEE C   1 ? 18 
ATOM   5803  O O   . ASP E  1 91  ? 43.041  -53.864  -8.473  1.000 53.900  0 420 ASP EEE O   1 ? 18 
ATOM   5804  C CB  . ASP E  1 91  ? 42.155  -52.687  -11.350 1.000 53.595  0 420 ASP EEE CB  1 ? 18 
ATOM   5805  C CG  . ASP E  1 91  ? 41.081  -52.764  -12.426 1.000 56.217  0 420 ASP EEE CG  1 ? 18 
ATOM   5806  O OD1 . ASP E  1 91  ? 39.888  -53.030  -12.068 1.000 56.277  0 420 ASP EEE OD1 1 ? 18 
ATOM   5807  O OD2 . ASP E  1 91  ? 41.421  -52.527  -13.623 1.000 58.260  0 420 ASP EEE OD2 1 ? 18 
ATOM   5808  N N   . TYR E  1 92  ? 43.485  -51.647  -8.611  1.000 49.621  0 421 TYR EEE N   1 ? 18 
ATOM   5809  C CA  . TYR E  1 92  ? 44.835  -51.696  -7.987  1.000 49.380  0 421 TYR EEE CA  1 ? 18 
ATOM   5810  C C   . TYR E  1 92  ? 44.891  -50.975  -6.629  1.000 46.079  0 421 TYR EEE C   1 ? 18 
ATOM   5811  O O   . TYR E  1 92  ? 45.913  -51.110  -5.950  1.000 45.721  0 421 TYR EEE O   1 ? 18 
ATOM   5812  C CB  . TYR E  1 92  ? 45.871  -51.085  -8.939  1.000 51.197  0 421 TYR EEE CB  1 ? 18 
ATOM   5813  C CG  . TYR E  1 92  ? 46.099  -51.782  -10.256 1.000 54.271  0 421 TYR EEE CG  1 ? 18 
ATOM   5814  C CD1 . TYR E  1 92  ? 45.727  -53.095  -10.470 1.000 56.227  0 421 TYR EEE CD1 1 ? 18 
ATOM   5815  C CD2 . TYR E  1 92  ? 46.766  -51.131  -11.283 1.000 57.770  0 421 TYR EEE CD2 1 ? 18 
ATOM   5816  C CE1 . TYR E  1 92  ? 45.977  -53.732  -11.678 1.000 59.023  0 421 TYR EEE CE1 1 ? 18 
ATOM   5817  C CE2 . TYR E  1 92  ? 47.048  -51.764  -12.486 1.000 62.333  0 421 TYR EEE CE2 1 ? 18 
ATOM   5818  C CZ  . TYR E  1 92  ? 46.624  -53.066  -12.699 1.000 62.145  0 421 TYR EEE CZ  1 ? 18 
ATOM   5819  O OH  . TYR E  1 92  ? 46.908  -53.692  -13.878 1.000 66.266  0 421 TYR EEE OH  1 ? 18 
ATOM   5820  N N   . ASN E  1 93  ? 43.851  -50.248  -6.220  1.000 44.370  0 422 ASN EEE N   1 ? 18 
ATOM   5821  C CA  . ASN E  1 93  ? 43.921  -49.358  -5.029  1.000 43.314  0 422 ASN EEE CA  1 ? 18 
ATOM   5822  C C   . ASN E  1 93  ? 42.802  -49.668  -4.030  1.000 42.121  0 422 ASN EEE C   1 ? 18 
ATOM   5823  O O   . ASN E  1 93  ? 43.118  -49.978  -2.874  1.000 42.074  0 422 ASN EEE O   1 ? 18 
ATOM   5824  C CB  . ASN E  1 93  ? 43.909  -47.890  -5.445  1.000 42.871  0 422 ASN EEE CB  1 ? 18 
ATOM   5825  C CG  . ASN E  1 93  ? 45.195  -47.503  -6.156  1.000 45.677  0 422 ASN EEE CG  1 ? 18 
ATOM   5826  O OD1 . ASN E  1 93  ? 46.127  -47.030  -5.507  1.000 45.945  0 422 ASN EEE OD1 1 ? 18 
ATOM   5827  N ND2 . ASN E  1 93  ? 45.270  -47.730  -7.466  1.000 44.784  0 422 ASN EEE ND2 1 ? 18 
ATOM   5828  N N   . TYR E  1 94  ? 41.543  -49.587  -4.456  1.000 41.779  0 423 TYR EEE N   1 ? 18 
ATOM   5829  C CA  . TYR E  1 94  ? 40.357  -49.774  -3.589  1.000 40.123  0 423 TYR EEE CA  1 ? 18 
ATOM   5830  C C   . TYR E  1 94  ? 39.224  -50.386  -4.407  1.000 40.089  0 423 TYR EEE C   1 ? 18 
ATOM   5831  O O   . TYR E  1 94  ? 38.710  -49.724  -5.351  1.000 39.992  0 423 TYR EEE O   1 ? 18 
ATOM   5832  C CB  . TYR E  1 94  ? 39.916  -48.452  -2.961  1.000 39.875  0 423 TYR EEE CB  1 ? 18 
ATOM   5833  C CG  . TYR E  1 94  ? 38.819  -48.611  -1.938  1.000 41.675  0 423 TYR EEE CG  1 ? 18 
ATOM   5834  C CD1 . TYR E  1 94  ? 39.114  -48.916  -0.622  1.000 44.480  0 423 TYR EEE CD1 1 ? 18 
ATOM   5835  C CD2 . TYR E  1 94  ? 37.482  -48.501  -2.287  1.000 42.070  0 423 TYR EEE CD2 1 ? 18 
ATOM   5836  C CE1 . TYR E  1 94  ? 38.115  -49.054  0.337   1.000 44.691  0 423 TYR EEE CE1 1 ? 18 
ATOM   5837  C CE2 . TYR E  1 94  ? 36.472  -48.623  -1.343  1.000 40.868  0 423 TYR EEE CE2 1 ? 18 
ATOM   5838  C CZ  . TYR E  1 94  ? 36.785  -48.904  -0.027  1.000 42.047  0 423 TYR EEE CZ  1 ? 18 
ATOM   5839  O OH  . TYR E  1 94  ? 35.793  -49.062  0.886   1.000 40.109  0 423 TYR EEE OH  1 ? 18 
ATOM   5840  N N   . LYS E  1 95  ? 38.828  -51.605  -4.037  1.000 40.332  0 424 LYS EEE N   1 ? 18 
ATOM   5841  C CA  . LYS E  1 95  ? 37.816  -52.394  -4.767  1.000 41.936  0 424 LYS EEE CA  1 ? 18 
ATOM   5842  C C   . LYS E  1 95  ? 36.588  -52.602  -3.884  1.000 41.144  0 424 LYS EEE C   1 ? 18 
ATOM   5843  O O   . LYS E  1 95  ? 36.732  -53.183  -2.804  1.000 41.124  0 424 LYS EEE O   1 ? 18 
ATOM   5844  C CB  . LYS E  1 95  ? 38.402  -53.748  -5.175  1.000 45.194  0 424 LYS EEE CB  1 ? 18 
ATOM   5845  C CG  . LYS E  1 95  ? 37.452  -54.659  -5.955  1.000 47.512  0 424 LYS EEE CG  1 ? 18 
ATOM   5846  C CD  . LYS E  1 95  ? 36.844  -53.973  -7.157  1.000 47.776  0 424 LYS EEE CD  1 ? 18 
ATOM   5847  C CE  . LYS E  1 95  ? 36.307  -54.916  -8.201  1.000 49.471  0 424 LYS EEE CE  1 ? 18 
ATOM   5848  N NZ  . LYS E  1 95  ? 35.462  -54.147  -9.135  1.000 49.755  0 424 LYS EEE NZ  1 ? 18 
ATOM   5849  N N   . LEU E  1 96  ? 35.421  -52.162  -4.343  1.000 43.690  0 425 LEU EEE N   1 ? 18 
ATOM   5850  C CA  . LEU E  1 96  ? 34.136  -52.504  -3.689  1.000 42.853  0 425 LEU EEE CA  1 ? 18 
ATOM   5851  C C   . LEU E  1 96  ? 33.610  -53.788  -4.279  1.000 43.364  0 425 LEU EEE C   1 ? 18 
ATOM   5852  O O   . LEU E  1 96  ? 33.770  -54.019  -5.473  1.000 45.408  0 425 LEU EEE O   1 ? 18 
ATOM   5853  C CB  . LEU E  1 96  ? 33.128  -51.388  -3.907  1.000 43.950  0 425 LEU EEE CB  1 ? 18 
ATOM   5854  C CG  . LEU E  1 96  ? 33.319  -50.132  -3.086  1.000 44.968  0 425 LEU EEE CG  1 ? 18 
ATOM   5855  C CD1 . LEU E  1 96  ? 32.143  -49.205  -3.400  1.000 45.222  0 425 LEU EEE CD1 1 ? 18 
ATOM   5856  C CD2 . LEU E  1 96  ? 33.386  -50.472  -1.591  1.000 46.995  0 425 LEU EEE CD2 1 ? 18 
ATOM   5857  N N   . PRO E  1 97  ? 32.960  -54.635  -3.449  1.000 44.331  0 426 PRO EEE N   1 ? 18 
ATOM   5858  C CA  . PRO E  1 97  ? 32.324  -55.864  -3.941  1.000 45.178  0 426 PRO EEE CA  1 ? 18 
ATOM   5859  C C   . PRO E  1 97  ? 31.113  -55.546  -4.828  1.000 44.231  0 426 PRO EEE C   1 ? 18 
ATOM   5860  O O   . PRO E  1 97  ? 30.560  -54.495  -4.698  1.000 44.539  0 426 PRO EEE O   1 ? 18 
ATOM   5861  C CB  . PRO E  1 97  ? 31.899  -56.590  -2.662  1.000 45.266  0 426 PRO EEE CB  1 ? 18 
ATOM   5862  C CG  . PRO E  1 97  ? 31.708  -55.481  -1.669  1.000 44.437  0 426 PRO EEE CG  1 ? 18 
ATOM   5863  C CD  . PRO E  1 97  ? 32.771  -54.443  -2.005  1.000 42.735  0 426 PRO EEE CD  1 ? 18 
ATOM   5864  N N   . ASP E  1 98  ? 30.710  -56.461  -5.701  1.000 47.627  0 427 ASP EEE N   1 ? 18 
ATOM   5865  C CA  . ASP E  1 98  ? 29.549  -56.230  -6.596  1.000 50.205  0 427 ASP EEE CA  1 ? 18 
ATOM   5866  C C   . ASP E  1 98  ? 28.263  -56.180  -5.749  1.000 48.264  0 427 ASP EEE C   1 ? 18 
ATOM   5867  O O   . ASP E  1 98  ? 27.358  -55.452  -6.181  1.000 46.833  0 427 ASP EEE O   1 ? 18 
ATOM   5868  C CB  . ASP E  1 98  ? 29.483  -57.202  -7.776  1.000 56.344  0 427 ASP EEE CB  1 ? 18 
ATOM   5869  C CG  . ASP E  1 98  ? 28.498  -56.780  -8.898  1.000 62.815  0 427 ASP EEE CG  1 ? 18 
ATOM   5870  O OD1 . ASP E  1 98  ? 28.830  -55.854  -9.687  1.000 64.273  0 427 ASP EEE OD1 1 ? 18 
ATOM   5871  O OD2 . ASP E  1 98  ? 27.365  -57.366  -8.992  1.000 65.420  0 427 ASP EEE OD2 1 ? 18 
ATOM   5872  N N   . ASP E  1 99  ? 28.184  -56.885  -4.615  1.000 46.785  0 428 ASP EEE N   1 ? 18 
ATOM   5873  C CA  . ASP E  1 99  ? 26.974  -56.926  -3.741  1.000 48.113  0 428 ASP EEE CA  1 ? 18 
ATOM   5874  C C   . ASP E  1 99  ? 27.166  -55.983  -2.531  1.000 46.885  0 428 ASP EEE C   1 ? 18 
ATOM   5875  O O   . ASP E  1 99  ? 26.602  -56.217  -1.460  1.000 47.856  0 428 ASP EEE O   1 ? 18 
ATOM   5876  C CB  . ASP E  1 99  ? 26.657  -58.355  -3.315  1.000 49.679  0 428 ASP EEE CB  1 ? 18 
ATOM   5877  C CG  . ASP E  1 99  ? 27.658  -58.962  -2.338  1.000 51.381  0 428 ASP EEE CG  1 ? 18 
ATOM   5878  O OD1 . ASP E  1 99  ? 28.775  -58.376  -2.198  1.000 51.352  0 428 ASP EEE OD1 1 ? 18 
ATOM   5879  O OD2 . ASP E  1 99  ? 27.300  -59.999  -1.670  1.000 53.562  0 428 ASP EEE OD2 1 ? 18 
ATOM   5880  N N   . PHE E  1 100 ? 27.970  -54.951  -2.694  1.000 44.470  0 429 PHE EEE N   1 ? 18 
ATOM   5881  C CA  . PHE E  1 100 ? 28.230  -53.936  -1.646  1.000 45.359  0 429 PHE EEE CA  1 ? 18 
ATOM   5882  C C   . PHE E  1 100 ? 26.943  -53.495  -0.953  1.000 42.683  0 429 PHE EEE C   1 ? 18 
ATOM   5883  O O   . PHE E  1 100 ? 25.983  -53.144  -1.622  1.000 43.641  0 429 PHE EEE O   1 ? 18 
ATOM   5884  C CB  . PHE E  1 100 ? 28.943  -52.731  -2.257  1.000 44.933  0 429 PHE EEE CB  1 ? 18 
ATOM   5885  C CG  . PHE E  1 100 ? 29.227  -51.624  -1.286  1.000 43.838  0 429 PHE EEE CG  1 ? 18 
ATOM   5886  C CD1 . PHE E  1 100 ? 29.962  -51.864  -0.138  1.000 44.047  0 429 PHE EEE CD1 1 ? 18 
ATOM   5887  C CD2 . PHE E  1 100 ? 28.785  -50.340  -1.546  1.000 41.705  0 429 PHE EEE CD2 1 ? 18 
ATOM   5888  C CE1 . PHE E  1 100 ? 30.248  -50.838  0.746   1.000 42.655  0 429 PHE EEE CE1 1 ? 18 
ATOM   5889  C CE2 . PHE E  1 100 ? 29.075  -49.315  -0.669  1.000 42.285  0 429 PHE EEE CE2 1 ? 18 
ATOM   5890  C CZ  . PHE E  1 100 ? 29.809  -49.570  0.470   1.000 43.725  0 429 PHE EEE CZ  1 ? 18 
ATOM   5891  N N   . THR E  1 101 ? 26.970  -53.470  0.369   1.000 41.711  0 430 THR EEE N   1 ? 18 
ATOM   5892  C CA  . THR E  1 101 ? 25.933  -52.833  1.217   1.000 43.618  0 430 THR EEE CA  1 ? 18 
ATOM   5893  C C   . THR E  1 101 ? 26.581  -51.671  1.962   1.000 42.526  0 430 THR EEE C   1 ? 18 
ATOM   5894  O O   . THR E  1 101 ? 27.441  -51.925  2.810   1.000 41.613  0 430 THR EEE O   1 ? 18 
ATOM   5895  C CB  . THR E  1 101 ? 25.302  -53.835  2.189   1.000 44.631  0 430 THR EEE CB  1 ? 18 
ATOM   5896  O OG1 . THR E  1 101 ? 24.860  -54.965  1.440   1.000 45.882  0 430 THR EEE OG1 1 ? 18 
ATOM   5897  C CG2 . THR E  1 101 ? 24.145  -53.242  2.955   1.000 45.360  0 430 THR EEE CG2 1 ? 18 
ATOM   5898  N N   . GLY E  1 102 ? 26.170  -50.442  1.663   1.000 43.711  0 431 GLY EEE N   1 ? 18 
ATOM   5899  C CA  . GLY E  1 102 ? 26.742  -49.238  2.295   1.000 42.963  0 431 GLY EEE CA  1 ? 18 
ATOM   5900  C C   . GLY E  1 102 ? 26.562  -48.004  1.433   1.000 41.917  0 431 GLY EEE C   1 ? 18 
ATOM   5901  O O   . GLY E  1 102 ? 25.708  -48.024  0.527   1.000 42.461  0 431 GLY EEE O   1 ? 18 
ATOM   5902  N N   . CYS E  1 103 ? 27.297  -46.940  1.738   1.000 40.344  0 432 CYS EEE N   1 ? 18 
ATOM   5903  C CA  . CYS E  1 103 ? 27.167  -45.639  1.042   1.000 41.864  0 432 CYS EEE CA  1 ? 18 
ATOM   5904  C C   . CYS E  1 103 ? 28.542  -45.127  0.629   1.000 39.326  0 432 CYS EEE C   1 ? 18 
ATOM   5905  O O   . CYS E  1 103 ? 29.508  -45.409  1.355   1.000 39.067  0 432 CYS EEE O   1 ? 18 
ATOM   5906  C CB  . CYS E  1 103 ? 26.437  -44.605  1.902   1.000 42.738  0 432 CYS EEE CB  1 ? 18 
ATOM   5907  S SG  . CYS E  1 103 ? 24.867  -45.213  2.571   1.000 46.292  0 432 CYS EEE SG  1 ? 18 
ATOM   5908  N N   . VAL E  1 104 ? 28.583  -44.392  -0.480  1.000 37.750  0 433 VAL EEE N   1 ? 18 
ATOM   5909  C CA  . VAL E  1 104 ? 29.804  -43.746  -1.008  1.000 37.595  0 433 VAL EEE CA  1 ? 18 
ATOM   5910  C C   . VAL E  1 104 ? 29.533  -42.254  -1.106  1.000 38.033  0 433 VAL EEE C   1 ? 18 
ATOM   5911  O O   . VAL E  1 104 ? 28.551  -41.876  -1.787  1.000 38.585  0 433 VAL EEE O   1 ? 18 
ATOM   5912  C CB  . VAL E  1 104 ? 30.232  -44.339  -2.354  1.000 39.356  0 433 VAL EEE CB  1 ? 18 
ATOM   5913  C CG1 . VAL E  1 104 ? 31.450  -43.613  -2.909  1.000 39.508  0 433 VAL EEE CG1 1 ? 18 
ATOM   5914  C CG2 . VAL E  1 104 ? 30.511  -45.832  -2.230  1.000 39.739  0 433 VAL EEE CG2 1 ? 18 
ATOM   5915  N N   . ILE E  1 105 ? 30.343  -41.452  -0.404  1.000 35.497  0 434 ILE EEE N   1 ? 18 
ATOM   5916  C CA  . ILE E  1 105 ? 30.215  -39.973  -0.361  1.000 37.217  0 434 ILE EEE CA  1 ? 18 
ATOM   5917  C C   . ILE E  1 105 ? 31.558  -39.394  -0.765  1.000 37.384  0 434 ILE EEE C   1 ? 18 
ATOM   5918  O O   . ILE E  1 105 ? 32.580  -39.914  -0.322  1.000 39.474  0 434 ILE EEE O   1 ? 18 
ATOM   5919  C CB  . ILE E  1 105 ? 29.758  -39.481  1.032   1.000 37.986  0 434 ILE EEE CB  1 ? 18 
ATOM   5920  C CG1 . ILE E  1 105 ? 28.430  -40.124  1.425   1.000 38.744  0 434 ILE EEE CG1 1 ? 18 
ATOM   5921  C CG2 . ILE E  1 105 ? 29.672  -37.958  1.097   1.000 38.089  0 434 ILE EEE CG2 1 ? 18 
ATOM   5922  C CD1 . ILE E  1 105 ? 28.126  -40.075  2.891   1.000 39.973  0 434 ILE EEE CD1 1 ? 18 
ATOM   5923  N N   . ALA E  1 106 ? 31.546  -38.386  -1.625  1.000 37.999  0 435 ALA EEE N   1 ? 18 
ATOM   5924  C CA  . ALA E  1 106 ? 32.765  -37.685  -2.065  1.000 38.302  0 435 ALA EEE CA  1 ? 18 
ATOM   5925  C C   . ALA E  1 106 ? 32.472  -36.191  -2.136  1.000 40.894  0 435 ALA EEE C   1 ? 18 
ATOM   5926  O O   . ALA E  1 106 ? 31.278  -35.813  -2.261  1.000 44.077  0 435 ALA EEE O   1 ? 18 
ATOM   5927  C CB  . ALA E  1 106 ? 33.265  -38.241  -3.371  1.000 37.291  0 435 ALA EEE CB  1 ? 18 
ATOM   5928  N N   . TRP E  1 107 ? 33.524  -35.384  -1.999  1.000 39.897  0 436 TRP EEE N   1 ? 18 
ATOM   5929  C CA  . TRP E  1 107 ? 33.437  -33.912  -2.149  1.000 39.639  0 436 TRP EEE CA  1 ? 18 
ATOM   5930  C C   . TRP E  1 107 ? 34.777  -33.369  -2.638  1.000 38.904  0 436 TRP EEE C   1 ? 18 
ATOM   5931  O O   . TRP E  1 107 ? 35.812  -33.978  -2.342  1.000 38.836  0 436 TRP EEE O   1 ? 18 
ATOM   5932  C CB  . TRP E  1 107 ? 32.982  -33.246  -0.846  1.000 39.196  0 436 TRP EEE CB  1 ? 18 
ATOM   5933  C CG  . TRP E  1 107 ? 33.933  -33.397  0.297   1.000 39.543  0 436 TRP EEE CG  1 ? 18 
ATOM   5934  C CD1 . TRP E  1 107 ? 34.858  -32.481  0.687   1.000 39.981  0 436 TRP EEE CD1 1 ? 18 
ATOM   5935  C CD2 . TRP E  1 107 ? 34.061  -34.509  1.202   1.000 38.809  0 436 TRP EEE CD2 1 ? 18 
ATOM   5936  N NE1 . TRP E  1 107 ? 35.543  -32.949  1.766   1.000 41.052  0 436 TRP EEE NE1 1 ? 18 
ATOM   5937  C CE2 . TRP E  1 107 ? 35.094  -34.191  2.094   1.000 38.436  0 436 TRP EEE CE2 1 ? 18 
ATOM   5938  C CE3 . TRP E  1 107 ? 33.417  -35.740  1.336   1.000 38.938  0 436 TRP EEE CE3 1 ? 18 
ATOM   5939  C CZ2 . TRP E  1 107 ? 35.487  -35.028  3.133   1.000 40.120  0 436 TRP EEE CZ2 1 ? 18 
ATOM   5940  C CZ3 . TRP E  1 107 ? 33.823  -36.589  2.355   1.000 38.253  0 436 TRP EEE CZ3 1 ? 18 
ATOM   5941  C CH2 . TRP E  1 107 ? 34.832  -36.225  3.260   1.000 39.491  0 436 TRP EEE CH2 1 ? 18 
ATOM   5942  N N   . ASN E  1 108 ? 34.712  -32.303  -3.422  1.000 39.785  0 437 ASN EEE N   1 ? 18 
ATOM   5943  C CA  . ASN E  1 108 ? 35.881  -31.546  -3.901  1.000 41.270  0 437 ASN EEE CA  1 ? 18 
ATOM   5944  C C   . ASN E  1 108 ? 36.664  -31.031  -2.684  1.000 41.696  0 437 ASN EEE C   1 ? 18 
ATOM   5945  O O   . ASN E  1 108 ? 36.048  -30.414  -1.824  1.000 41.141  0 437 ASN EEE O   1 ? 18 
ATOM   5946  C CB  . ASN E  1 108 ? 35.427  -30.419  -4.815  1.000 42.531  0 437 ASN EEE CB  1 ? 18 
ATOM   5947  C CG  . ASN E  1 108 ? 36.611  -29.758  -5.456  1.000 45.985  0 437 ASN EEE CG  1 ? 18 
ATOM   5948  O OD1 . ASN E  1 108 ? 37.390  -29.100  -4.761  1.000 48.005  0 437 ASN EEE OD1 1 ? 18 
ATOM   5949  N ND2 . ASN E  1 108 ? 36.755  -29.958  -6.757  1.000 46.674  0 437 ASN EEE ND2 1 ? 18 
ATOM   5950  N N   . SER E  1 109 ? 37.964  -31.316  -2.610  1.000 41.115  0 438 SER EEE N   1 ? 18 
ATOM   5951  C CA  . SER E  1 109 ? 38.856  -30.875  -1.517  1.000 42.046  0 438 SER EEE CA  1 ? 18 
ATOM   5952  C C   . SER E  1 109 ? 40.000  -30.040  -2.094  1.000 44.996  0 438 SER EEE C   1 ? 18 
ATOM   5953  O O   . SER E  1 109 ? 41.069  -29.970  -1.459  1.000 47.436  0 438 SER EEE O   1 ? 18 
ATOM   5954  C CB  . SER E  1 109 ? 39.368  -32.039  -0.740  1.000 40.871  0 438 SER EEE CB  1 ? 18 
ATOM   5955  O OG  . SER E  1 109 ? 40.086  -32.928  -1.571  1.000 40.005  0 438 SER EEE OG  1 ? 18 
ATOM   5956  N N   . ASN E  1 110 ? 39.768  -29.384  -3.232  1.000 45.618  0 439 ASN EEE N   1 ? 18 
ATOM   5957  C CA  . ASN E  1 110 ? 40.811  -28.564  -3.890  1.000 47.560  0 439 ASN EEE CA  1 ? 18 
ATOM   5958  C C   . ASN E  1 110 ? 41.361  -27.557  -2.870  1.000 48.944  0 439 ASN EEE C   1 ? 18 
ATOM   5959  O O   . ASN E  1 110 ? 42.576  -27.390  -2.804  1.000 48.881  0 439 ASN EEE O   1 ? 18 
ATOM   5960  C CB  . ASN E  1 110 ? 40.283  -27.886  -5.147  1.000 48.506  0 439 ASN EEE CB  1 ? 18 
ATOM   5961  C CG  . ASN E  1 110 ? 41.391  -27.417  -6.080  1.000 50.308  0 439 ASN EEE CG  1 ? 18 
ATOM   5962  O OD1 . ASN E  1 110 ? 42.449  -28.028  -6.172  1.000 51.348  0 439 ASN EEE OD1 1 ? 18 
ATOM   5963  N ND2 . ASN E  1 110 ? 41.139  -26.348  -6.803  1.000 52.824  0 439 ASN EEE ND2 1 ? 18 
ATOM   5964  N N   . ASN E  1 111 ? 40.489  -26.933  -2.076  1.000 49.421  0 440 ASN EEE N   1 ? 18 
ATOM   5965  C CA  . ASN E  1 111 ? 40.878  -25.836  -1.153  1.000 51.523  0 440 ASN EEE CA  1 ? 18 
ATOM   5966  C C   . ASN E  1 111 ? 41.823  -26.359  -0.056  1.000 51.226  0 440 ASN EEE C   1 ? 18 
ATOM   5967  O O   . ASN E  1 111 ? 42.601  -25.563  0.475   1.000 52.598  0 440 ASN EEE O   1 ? 18 
ATOM   5968  C CB  . ASN E  1 111 ? 39.641  -25.173  -0.540  1.000 53.106  0 440 ASN EEE CB  1 ? 18 
ATOM   5969  C CG  . ASN E  1 111 ? 40.015  -23.989  0.317   1.000 57.543  0 440 ASN EEE CG  1 ? 18 
ATOM   5970  O OD1 . ASN E  1 111 ? 40.899  -23.210  -0.058  1.000 61.284  0 440 ASN EEE OD1 1 ? 18 
ATOM   5971  N ND2 . ASN E  1 111 ? 39.348  -23.843  1.448   1.000 58.022  0 440 ASN EEE ND2 1 ? 18 
ATOM   5972  N N   . LEU E  1 112 ? 41.751  -27.651  0.300   1.000 49.087  0 441 LEU EEE N   1 ? 18 
ATOM   5973  C CA  . LEU E  1 112 ? 42.553  -28.226  1.404   1.000 49.837  0 441 LEU EEE CA  1 ? 18 
ATOM   5974  C C   . LEU E  1 112 ? 43.739  -29.014  0.862   1.000 49.825  0 441 LEU EEE C   1 ? 18 
ATOM   5975  O O   . LEU E  1 112 ? 44.775  -28.972  1.500   1.000 51.787  0 441 LEU EEE O   1 ? 18 
ATOM   5976  C CB  . LEU E  1 112 ? 41.659  -29.135  2.254   1.000 49.062  0 441 LEU EEE CB  1 ? 18 
ATOM   5977  C CG  . LEU E  1 112 ? 40.557  -28.439  3.062   1.000 49.273  0 441 LEU EEE CG  1 ? 18 
ATOM   5978  C CD1 . LEU E  1 112 ? 39.821  -29.466  3.916   1.000 48.408  0 441 LEU EEE CD1 1 ? 18 
ATOM   5979  C CD2 . LEU E  1 112 ? 41.114  -27.307  3.928   1.000 51.429  0 441 LEU EEE CD2 1 ? 18 
ATOM   5980  N N   . ASP E  1 113 ? 43.585  -29.719  -0.256  1.000 49.716  0 442 ASP EEE N   1 ? 18 
ATOM   5981  C CA  . ASP E  1 113 ? 44.515  -30.799  -0.688  1.000 49.622  0 442 ASP EEE CA  1 ? 18 
ATOM   5982  C C   . ASP E  1 113 ? 45.360  -30.406  -1.908  1.000 51.700  0 442 ASP EEE C   1 ? 18 
ATOM   5983  O O   . ASP E  1 113 ? 46.097  -31.255  -2.388  1.000 50.107  0 442 ASP EEE O   1 ? 18 
ATOM   5984  C CB  . ASP E  1 113 ? 43.714  -32.057  -1.007  1.000 47.041  0 442 ASP EEE CB  1 ? 18 
ATOM   5985  C CG  . ASP E  1 113 ? 43.191  -32.769  0.224   1.000 46.897  0 442 ASP EEE CG  1 ? 18 
ATOM   5986  O OD1 . ASP E  1 113 ? 43.899  -32.756  1.269   1.000 46.237  0 442 ASP EEE OD1 1 ? 18 
ATOM   5987  O OD2 . ASP E  1 113 ? 42.079  -33.358  0.118   1.000 43.887  0 442 ASP EEE OD2 1 ? 18 
ATOM   5988  N N   . SER E  1 114 ? 45.280  -29.175  -2.402  1.000 55.151  0 443 SER EEE N   1 ? 18 
ATOM   5989  C CA  . SER E  1 114 ? 46.131  -28.731  -3.524  1.000 61.096  0 443 SER EEE CA  1 ? 18 
ATOM   5990  C C   . SER E  1 114 ? 47.006  -27.585  -3.024  1.000 67.482  0 443 SER EEE C   1 ? 18 
ATOM   5991  O O   . SER E  1 114 ? 46.584  -26.908  -2.093  1.000 70.138  0 443 SER EEE O   1 ? 18 
ATOM   5992  C CB  . SER E  1 114 ? 45.283  -28.397  -4.729  1.000 61.503  0 443 SER EEE CB  1 ? 18 
ATOM   5993  O OG  . SER E  1 114 ? 44.816  -27.063  -4.685  1.000 63.804  0 443 SER EEE OG  1 ? 18 
ATOM   5994  N N   . LYS E  1 115 ? 48.215  -27.427  -3.560  1.000 75.858  0 444 LYS EEE N   1 ? 18 
ATOM   5995  C CA  . LYS E  1 115 ? 49.159  -26.356  -3.141  1.000 81.449  0 444 LYS EEE CA  1 ? 18 
ATOM   5996  C C   . LYS E  1 115 ? 49.689  -25.658  -4.387  1.000 80.940  0 444 LYS EEE C   1 ? 18 
ATOM   5997  O O   . LYS E  1 115 ? 49.746  -26.312  -5.445  1.000 77.785  0 444 LYS EEE O   1 ? 18 
ATOM   5998  C CB  . LYS E  1 115 ? 50.343  -26.912  -2.345  1.000 86.884  0 444 LYS EEE CB  1 ? 18 
ATOM   5999  C CG  . LYS E  1 115 ? 50.163  -26.835  -0.839  1.000 91.901  0 444 LYS EEE CG  1 ? 18 
ATOM   6000  C CD  . LYS E  1 115 ? 50.841  -27.946  -0.052  1.000 96.387  0 444 LYS EEE CD  1 ? 18 
ATOM   6001  C CE  . LYS E  1 115 ? 50.005  -28.400  1.133   1.000 99.771  0 444 LYS EEE CE  1 ? 18 
ATOM   6002  N NZ  . LYS E  1 115 ? 50.181  -29.847  1.438   1.000 100.946 0 444 LYS EEE NZ  1 ? 18 
ATOM   6003  N N   . VAL E  1 116 ? 50.097  -24.399  -4.229  1.000 83.845  0 445 VAL EEE N   1 ? 18 
ATOM   6004  C CA  . VAL E  1 116 ? 50.891  -23.670  -5.255  1.000 87.051  0 445 VAL EEE CA  1 ? 18 
ATOM   6005  C C   . VAL E  1 116 ? 52.184  -24.476  -5.443  1.000 85.209  0 445 VAL EEE C   1 ? 18 
ATOM   6006  O O   . VAL E  1 116 ? 52.809  -24.864  -4.436  1.000 84.572  0 445 VAL EEE O   1 ? 18 
ATOM   6007  C CB  . VAL E  1 116 ? 51.117  -22.191  -4.884  1.000 92.548  0 445 VAL EEE CB  1 ? 18 
ATOM   6008  C CG1 . VAL E  1 116 ? 49.809  -21.424  -4.951  1.000 92.710  0 445 VAL EEE CG1 1 ? 18 
ATOM   6009  C CG2 . VAL E  1 116 ? 51.772  -22.018  -3.517  1.000 95.127  0 445 VAL EEE CG2 1 ? 18 
ATOM   6010  N N   . GLY E  1 117 ? 52.491  -24.842  -6.685  1.000 83.358  0 446 GLY EEE N   1 ? 18 
ATOM   6011  C CA  . GLY E  1 117 ? 53.643  -25.703  -7.014  1.000 83.439  0 446 GLY EEE CA  1 ? 18 
ATOM   6012  C C   . GLY E  1 117 ? 53.343  -27.179  -6.835  1.000 80.850  0 446 GLY EEE C   1 ? 18 
ATOM   6013  O O   . GLY E  1 117 ? 54.225  -27.975  -7.158  1.000 80.908  0 446 GLY EEE O   1 ? 18 
ATOM   6014  N N   . GLY E  1 118 ? 52.119  -27.530  -6.432  1.000 79.209  0 447 GLY EEE N   1 ? 18 
ATOM   6015  C CA  . GLY E  1 118 ? 51.577  -28.900  -6.524  1.000 74.112  0 447 GLY EEE CA  1 ? 18 
ATOM   6016  C C   . GLY E  1 118 ? 51.749  -29.668  -5.235  1.000 72.178  0 447 GLY EEE C   1 ? 18 
ATOM   6017  O O   . GLY E  1 118 ? 52.851  -29.638  -4.686  1.000 72.076  0 447 GLY EEE O   1 ? 18 
ATOM   6018  N N   . ASN E  1 119 ? 50.691  -30.347  -4.784  1.000 67.318  0 448 ASN EEE N   1 ? 18 
ATOM   6019  C CA  . ASN E  1 119 ? 50.750  -31.275  -3.627  1.000 64.848  0 448 ASN EEE CA  1 ? 18 
ATOM   6020  C C   . ASN E  1 119 ? 51.048  -32.677  -4.163  1.000 63.735  0 448 ASN EEE C   1 ? 18 
ATOM   6021  O O   . ASN E  1 119 ? 50.196  -33.245  -4.864  1.000 65.019  0 448 ASN EEE O   1 ? 18 
ATOM   6022  C CB  . ASN E  1 119 ? 49.464  -31.218  -2.796  1.000 61.996  0 448 ASN EEE CB  1 ? 18 
ATOM   6023  C CG  . ASN E  1 119 ? 49.482  -32.160  -1.617  1.000 59.332  0 448 ASN EEE CG  1 ? 18 
ATOM   6024  O OD1 . ASN E  1 119 ? 50.526  -32.682  -1.259  1.000 62.137  0 448 ASN EEE OD1 1 ? 18 
ATOM   6025  N ND2 . ASN E  1 119 ? 48.332  -32.397  -1.020  1.000 57.702  0 448 ASN EEE ND2 1 ? 18 
ATOM   6026  N N   . TYR E  1 120 ? 52.219  -33.217  -3.822  1.000 65.798  0 449 TYR EEE N   1 ? 18 
ATOM   6027  C CA  . TYR E  1 120 ? 52.696  -34.538  -4.309  1.000 65.716  0 449 TYR EEE CA  1 ? 18 
ATOM   6028  C C   . TYR E  1 120 ? 52.554  -35.574  -3.182  1.000 63.015  0 449 TYR EEE C   1 ? 18 
ATOM   6029  O O   . TYR E  1 120 ? 53.016  -36.713  -3.377  1.000 63.682  0 449 TYR EEE O   1 ? 18 
ATOM   6030  C CB  . TYR E  1 120 ? 54.101  -34.406  -4.929  1.000 69.840  0 449 TYR EEE CB  1 ? 18 
ATOM   6031  C CG  . TYR E  1 120 ? 54.128  -33.546  -6.177  1.000 74.451  0 449 TYR EEE CG  1 ? 18 
ATOM   6032  C CD1 . TYR E  1 120 ? 53.680  -34.028  -7.399  1.000 76.794  0 449 TYR EEE CD1 1 ? 18 
ATOM   6033  C CD2 . TYR E  1 120 ? 54.535  -32.215  -6.134  1.000 79.306  0 449 TYR EEE CD2 1 ? 18 
ATOM   6034  C CE1 . TYR E  1 120 ? 53.645  -33.230  -8.536  1.000 78.470  0 449 TYR EEE CE1 1 ? 18 
ATOM   6035  C CE2 . TYR E  1 120 ? 54.516  -31.407  -7.265  1.000 81.603  0 449 TYR EEE CE2 1 ? 18 
ATOM   6036  C CZ  . TYR E  1 120 ? 54.051  -31.909  -8.468  1.000 81.942  0 449 TYR EEE CZ  1 ? 18 
ATOM   6037  O OH  . TYR E  1 120 ? 54.011  -31.134  -9.593  1.000 82.711  0 449 TYR EEE OH  1 ? 18 
ATOM   6038  N N   . ASN E  1 121 ? 51.892  -35.236  -2.069  1.000 59.490  0 450 ASN EEE N   1 ? 18 
ATOM   6039  C CA  . ASN E  1 121 ? 51.741  -36.148  -0.899  1.000 58.400  0 450 ASN EEE CA  1 ? 18 
ATOM   6040  C C   . ASN E  1 121 ? 50.793  -37.327  -1.190  1.000 53.524  0 450 ASN EEE C   1 ? 18 
ATOM   6041  O O   . ASN E  1 121 ? 50.989  -38.385  -0.610  1.000 52.476  0 450 ASN EEE O   1 ? 18 
ATOM   6042  C CB  . ASN E  1 121 ? 51.322  -35.403  0.364   1.000 59.433  0 450 ASN EEE CB  1 ? 18 
ATOM   6043  C CG  . ASN E  1 121 ? 52.461  -34.570  0.923   1.000 65.411  0 450 ASN EEE CG  1 ? 18 
ATOM   6044  O OD1 . ASN E  1 121 ? 53.635  -34.819  0.640   1.000 65.570  0 450 ASN EEE OD1 1 ? 18 
ATOM   6045  N ND2 . ASN E  1 121 ? 52.136  -33.560  1.716   1.000 69.510  0 450 ASN EEE ND2 1 ? 18 
ATOM   6046  N N   . TYR E  1 122 ? 49.790  -37.167  -2.032  1.000 50.257  0 451 TYR EEE N   1 ? 18 
ATOM   6047  C CA  . TYR E  1 122 ? 48.788  -38.230  -2.302  1.000 47.564  0 451 TYR EEE CA  1 ? 18 
ATOM   6048  C C   . TYR E  1 122 ? 49.284  -39.130  -3.448  1.000 47.719  0 451 TYR EEE C   1 ? 18 
ATOM   6049  O O   . TYR E  1 122 ? 49.628  -38.612  -4.551  1.000 47.444  0 451 TYR EEE O   1 ? 18 
ATOM   6050  C CB  . TYR E  1 122 ? 47.423  -37.605  -2.594  1.000 45.474  0 451 TYR EEE CB  1 ? 18 
ATOM   6051  C CG  . TYR E  1 122 ? 46.799  -36.924  -1.409  1.000 45.428  0 451 TYR EEE CG  1 ? 18 
ATOM   6052  C CD1 . TYR E  1 122 ? 46.283  -37.656  -0.352  1.000 45.015  0 451 TYR EEE CD1 1 ? 18 
ATOM   6053  C CD2 . TYR E  1 122 ? 46.679  -35.549  -1.353  1.000 46.647  0 451 TYR EEE CD2 1 ? 18 
ATOM   6054  C CE1 . TYR E  1 122 ? 45.674  -37.042  0.732   1.000 44.219  0 451 TYR EEE CE1 1 ? 18 
ATOM   6055  C CE2 . TYR E  1 122 ? 46.059  -34.922  -0.282  1.000 46.907  0 451 TYR EEE CE2 1 ? 18 
ATOM   6056  C CZ  . TYR E  1 122 ? 45.573  -35.669  0.773   1.000 44.805  0 451 TYR EEE CZ  1 ? 18 
ATOM   6057  O OH  . TYR E  1 122 ? 44.988  -35.058  1.839   1.000 45.395  0 451 TYR EEE OH  1 ? 18 
ATOM   6058  N N   . LEU E  1 123 ? 49.331  -40.438  -3.182  1.000 45.714  0 452 LEU EEE N   1 ? 18 
ATOM   6059  C CA  . LEU E  1 123 ? 49.872  -41.476  -4.096  1.000 46.804  0 452 LEU EEE CA  1 ? 18 
ATOM   6060  C C   . LEU E  1 123 ? 48.752  -42.437  -4.514  1.000 46.364  0 452 LEU EEE C   1 ? 18 
ATOM   6061  O O   . LEU E  1 123 ? 47.741  -42.534  -3.772  1.000 45.331  0 452 LEU EEE O   1 ? 18 
ATOM   6062  C CB  . LEU E  1 123 ? 50.978  -42.247  -3.367  1.000 48.648  0 452 LEU EEE CB  1 ? 18 
ATOM   6063  C CG  . LEU E  1 123 ? 52.159  -41.423  -2.841  1.000 51.381  0 452 LEU EEE CG  1 ? 18 
ATOM   6064  C CD1 . LEU E  1 123 ? 53.201  -42.337  -2.213  1.000 52.525  0 452 LEU EEE CD1 1 ? 18 
ATOM   6065  C CD2 . LEU E  1 123 ? 52.805  -40.592  -3.944  1.000 53.317  0 452 LEU EEE CD2 1 ? 18 
ATOM   6066  N N   . TYR E  1 124 ? 48.927  -43.121  -5.647  1.000 45.564  0 453 TYR EEE N   1 ? 18 
ATOM   6067  C CA  . TYR E  1 124 ? 48.058  -44.233  -6.096  1.000 44.608  0 453 TYR EEE CA  1 ? 18 
ATOM   6068  C C   . TYR E  1 124 ? 48.947  -45.323  -6.708  1.000 47.444  0 453 TYR EEE C   1 ? 18 
ATOM   6069  O O   . TYR E  1 124 ? 50.016  -44.986  -7.265  1.000 48.007  0 453 TYR EEE O   1 ? 18 
ATOM   6070  C CB  . TYR E  1 124 ? 47.005  -43.726  -7.087  1.000 44.146  0 453 TYR EEE CB  1 ? 18 
ATOM   6071  C CG  . TYR E  1 124 ? 47.586  -43.199  -8.367  1.000 45.744  0 453 TYR EEE CG  1 ? 18 
ATOM   6072  C CD1 . TYR E  1 124 ? 47.839  -44.044  -9.439  1.000 47.756  0 453 TYR EEE CD1 1 ? 18 
ATOM   6073  C CD2 . TYR E  1 124 ? 47.910  -41.858  -8.501  1.000 46.956  0 453 TYR EEE CD2 1 ? 18 
ATOM   6074  C CE1 . TYR E  1 124 ? 48.375  -43.569  -10.625 1.000 49.635  0 453 TYR EEE CE1 1 ? 18 
ATOM   6075  C CE2 . TYR E  1 124 ? 48.452  -41.365  -9.680  1.000 48.156  0 453 TYR EEE CE2 1 ? 18 
ATOM   6076  C CZ  . TYR E  1 124 ? 48.677  -42.223  -10.740 1.000 50.203  0 453 TYR EEE CZ  1 ? 18 
ATOM   6077  O OH  . TYR E  1 124 ? 49.211  -41.733  -11.889 1.000 54.220  0 453 TYR EEE OH  1 ? 18 
ATOM   6078  N N   . ARG E  1 125 ? 48.543  -46.592  -6.576  1.000 47.007  0 454 ARG EEE N   1 ? 18 
ATOM   6079  C CA  . ARG E  1 125 ? 49.257  -47.744  -7.183  1.000 49.524  0 454 ARG EEE CA  1 ? 18 
ATOM   6080  C C   . ARG E  1 125 ? 48.942  -47.747  -8.687  1.000 51.828  0 454 ARG EEE C   1 ? 18 
ATOM   6081  O O   . ARG E  1 125 ? 47.753  -47.754  -9.050  1.000 51.165  0 454 ARG EEE O   1 ? 18 
ATOM   6082  C CB  . ARG E  1 125 ? 48.881  -49.058  -6.492  1.000 48.652  0 454 ARG EEE CB  1 ? 18 
ATOM   6083  C CG  . ARG E  1 125 ? 49.706  -50.254  -6.958  1.000 50.870  0 454 ARG EEE CG  1 ? 18 
ATOM   6084  C CD  . ARG E  1 125 ? 49.403  -51.516  -6.160  1.000 50.872  0 454 ARG EEE CD  1 ? 18 
ATOM   6085  N NE  . ARG E  1 125 ? 49.666  -51.311  -4.748  1.000 50.506  0 454 ARG EEE NE  1 ? 18 
ATOM   6086  C CZ  . ARG E  1 125 ? 50.877  -51.305  -4.173  1.000 52.996  0 454 ARG EEE CZ  1 ? 18 
ATOM   6087  N NH1 . ARG E  1 125 ? 51.987  -51.521  -4.866  1.000 55.230  0 454 ARG EEE NH1 1 ? 18 
ATOM   6088  N NH2 . ARG E  1 125 ? 50.969  -51.070  -2.877  1.000 53.355  0 454 ARG EEE NH2 1 ? 18 
ATOM   6089  N N   . LEU E  1 126 ? 49.973  -47.699  -9.520  1.000 55.453  0 455 LEU EEE N   1 ? 18 
ATOM   6090  C CA  . LEU E  1 126 ? 49.858  -47.587  -10.995 1.000 61.056  0 455 LEU EEE CA  1 ? 18 
ATOM   6091  C C   . LEU E  1 126 ? 49.954  -48.974  -11.644 1.000 63.017  0 455 LEU EEE C   1 ? 18 
ATOM   6092  O O   . LEU E  1 126 ? 49.318  -49.180  -12.696 1.000 62.922  0 455 LEU EEE O   1 ? 18 
ATOM   6093  C CB  . LEU E  1 126 ? 50.973  -46.656  -11.488 1.000 64.426  0 455 LEU EEE CB  1 ? 18 
ATOM   6094  C CG  . LEU E  1 126 ? 51.095  -46.486  -13.001 1.000 68.109  0 455 LEU EEE CG  1 ? 18 
ATOM   6095  C CD1 . LEU E  1 126 ? 49.769  -45.983  -13.612 1.000 68.702  0 455 LEU EEE CD1 1 ? 18 
ATOM   6096  C CD2 . LEU E  1 126 ? 52.237  -45.548  -13.323 1.000 69.930  0 455 LEU EEE CD2 1 ? 18 
ATOM   6097  N N   . PHE E  1 127 ? 50.732  -49.866  -11.040 1.000 66.951  0 456 PHE EEE N   1 ? 18 
ATOM   6098  C CA  . PHE E  1 127 ? 51.027  -51.234  -11.549 1.000 72.263  0 456 PHE EEE CA  1 ? 18 
ATOM   6099  C C   . PHE E  1 127 ? 50.692  -52.249  -10.459 1.000 69.610  0 456 PHE EEE C   1 ? 18 
ATOM   6100  O O   . PHE E  1 127 ? 51.071  -52.027  -9.275  1.000 70.430  0 456 PHE EEE O   1 ? 18 
ATOM   6101  C CB  . PHE E  1 127 ? 52.514  -51.354  -11.940 1.000 76.266  0 456 PHE EEE CB  1 ? 18 
ATOM   6102  C CG  . PHE E  1 127 ? 52.963  -50.363  -12.982 1.000 80.462  0 456 PHE EEE CG  1 ? 18 
ATOM   6103  C CD1 . PHE E  1 127 ? 52.457  -50.405  -14.279 1.000 82.768  0 456 PHE EEE CD1 1 ? 18 
ATOM   6104  C CD2 . PHE E  1 127 ? 53.883  -49.366  -12.673 1.000 82.258  0 456 PHE EEE CD2 1 ? 18 
ATOM   6105  C CE1 . PHE E  1 127 ? 52.843  -49.463  -15.227 1.000 84.331  0 456 PHE EEE CE1 1 ? 18 
ATOM   6106  C CE2 . PHE E  1 127 ? 54.291  -48.444  -13.632 1.000 83.712  0 456 PHE EEE CE2 1 ? 18 
ATOM   6107  C CZ  . PHE E  1 127 ? 53.771  -48.494  -14.906 1.000 84.800  0 456 PHE EEE CZ  1 ? 18 
ATOM   6108  N N   . ARG E  1 128 ? 50.063  -53.344  -10.849 1.000 67.828  0 457 ARG EEE N   1 ? 18 
ATOM   6109  C CA  . ARG E  1 128 ? 49.923  -54.509  -9.948  1.000 67.626  0 457 ARG EEE CA  1 ? 18 
ATOM   6110  C C   . ARG E  1 128 ? 49.756  -55.771  -10.793 1.000 71.149  0 457 ARG EEE C   1 ? 18 
ATOM   6111  O O   . ARG E  1 128 ? 49.139  -55.687  -11.871 1.000 72.050  0 457 ARG EEE O   1 ? 18 
ATOM   6112  C CB  . ARG E  1 128 ? 48.767  -54.293  -8.988  1.000 64.240  0 457 ARG EEE CB  1 ? 18 
ATOM   6113  C CG  . ARG E  1 128 ? 48.757  -55.270  -7.827  1.000 65.047  0 457 ARG EEE CG  1 ? 18 
ATOM   6114  C CD  . ARG E  1 128 ? 47.700  -54.866  -6.825  1.000 62.449  0 457 ARG EEE CD  1 ? 18 
ATOM   6115  N NE  . ARG E  1 128 ? 47.860  -55.575  -5.563  1.000 62.734  0 457 ARG EEE NE  1 ? 18 
ATOM   6116  C CZ  . ARG E  1 128 ? 47.336  -56.748  -5.273  1.000 62.063  0 457 ARG EEE CZ  1 ? 18 
ATOM   6117  N NH1 . ARG E  1 128 ? 46.592  -57.385  -6.159  1.000 63.231  0 457 ARG EEE NH1 1 ? 18 
ATOM   6118  N NH2 . ARG E  1 128 ? 47.537  -57.278  -4.082  1.000 62.076  0 457 ARG EEE NH2 1 ? 18 
ATOM   6119  N N   . LYS E  1 129 ? 50.317  -56.885  -10.311 1.000 72.691  0 458 LYS EEE N   1 ? 18 
ATOM   6120  C CA  . LYS E  1 129 ? 50.367  -58.175  -11.044 1.000 74.107  0 458 LYS EEE CA  1 ? 18 
ATOM   6121  C C   . LYS E  1 129 ? 48.962  -58.743  -11.206 1.000 71.532  0 458 LYS EEE C   1 ? 18 
ATOM   6122  O O   . LYS E  1 129 ? 48.754  -59.482  -12.140 1.000 74.530  0 458 LYS EEE O   1 ? 18 
ATOM   6123  C CB  . LYS E  1 129 ? 51.357  -59.118  -10.361 1.000 78.546  0 458 LYS EEE CB  1 ? 18 
ATOM   6124  C CG  . LYS E  1 129 ? 52.791  -58.710  -10.694 1.000 82.570  0 458 LYS EEE CG  1 ? 18 
ATOM   6125  C CD  . LYS E  1 129 ? 53.926  -59.473  -10.085 1.000 86.321  0 458 LYS EEE CD  1 ? 18 
ATOM   6126  C CE  . LYS E  1 129 ? 55.210  -58.830  -10.582 1.000 89.794  0 458 LYS EEE CE  1 ? 18 
ATOM   6127  N NZ  . LYS E  1 129 ? 56.441  -59.349  -9.930  1.000 93.655  0 458 LYS EEE NZ  1 ? 18 
ATOM   6128  N N   . SER E  1 130 ? 48.042  -58.408  -10.323 1.000 68.268  0 459 SER EEE N   1 ? 18 
ATOM   6129  C CA  . SER E  1 130 ? 46.636  -58.872  -10.400 1.000 66.226  0 459 SER EEE CA  1 ? 18 
ATOM   6130  C C   . SER E  1 130 ? 45.732  -57.884  -9.651  1.000 61.510  0 459 SER EEE C   1 ? 18 
ATOM   6131  O O   . SER E  1 130 ? 46.258  -57.075  -8.872  1.000 59.458  0 459 SER EEE O   1 ? 18 
ATOM   6132  C CB  . SER E  1 130 ? 46.525  -60.260  -9.869  1.000 68.663  0 459 SER EEE CB  1 ? 18 
ATOM   6133  O OG  . SER E  1 130 ? 46.491  -60.247  -8.451  1.000 67.510  0 459 SER EEE OG  1 ? 18 
ATOM   6134  N N   . ASN E  1 131 ? 44.428  -57.934  -9.909  1.000 58.789  0 460 ASN EEE N   1 ? 18 
ATOM   6135  C CA  . ASN E  1 131 ? 43.449  -56.972  -9.354  1.000 55.161  0 460 ASN EEE CA  1 ? 18 
ATOM   6136  C C   . ASN E  1 131 ? 43.257  -57.261  -7.867  1.000 53.302  0 460 ASN EEE C   1 ? 18 
ATOM   6137  O O   . ASN E  1 131 ? 43.364  -58.414  -7.473  1.000 53.793  0 460 ASN EEE O   1 ? 18 
ATOM   6138  C CB  . ASN E  1 131 ? 42.113  -57.038  -10.089 1.000 55.245  0 460 ASN EEE CB  1 ? 18 
ATOM   6139  C CG  . ASN E  1 131 ? 42.191  -56.539  -11.515 1.000 56.065  0 460 ASN EEE CG  1 ? 18 
ATOM   6140  O OD1 . ASN E  1 131 ? 43.218  -56.040  -11.938 1.000 58.357  0 460 ASN EEE OD1 1 ? 18 
ATOM   6141  N ND2 . ASN E  1 131 ? 41.108  -56.665  -12.263 1.000 56.443  0 460 ASN EEE ND2 1 ? 18 
ATOM   6142  N N   . LEU E  1 132 ? 43.002  -56.224  -7.076  1.000 51.413  0 461 LEU EEE N   1 ? 18 
ATOM   6143  C CA  . LEU E  1 132 ? 42.601  -56.355  -5.657  1.000 50.706  0 461 LEU EEE CA  1 ? 18 
ATOM   6144  C C   . LEU E  1 132 ? 41.297  -57.135  -5.592  1.000 52.075  0 461 LEU EEE C   1 ? 18 
ATOM   6145  O O   . LEU E  1 132 ? 40.423  -56.906  -6.429  1.000 54.656  0 461 LEU EEE O   1 ? 18 
ATOM   6146  C CB  . LEU E  1 132 ? 42.406  -54.961  -5.053  1.000 47.852  0 461 LEU EEE CB  1 ? 18 
ATOM   6147  C CG  . LEU E  1 132 ? 43.682  -54.141  -4.844  1.000 48.546  0 461 LEU EEE CG  1 ? 18 
ATOM   6148  C CD1 . LEU E  1 132 ? 43.355  -52.852  -4.144  1.000 46.321  0 461 LEU EEE CD1 1 ? 18 
ATOM   6149  C CD2 . LEU E  1 132 ? 44.693  -54.935  -4.009  1.000 50.852  0 461 LEU EEE CD2 1 ? 18 
ATOM   6150  N N   . LYS E  1 133 ? 41.177  -58.016  -4.608  1.000 53.801  0 462 LYS EEE N   1 ? 18 
ATOM   6151  C CA  . LYS E  1 133 ? 39.880  -58.567  -4.154  1.000 54.138  0 462 LYS EEE CA  1 ? 18 
ATOM   6152  C C   . LYS E  1 133 ? 39.146  -57.461  -3.411  1.000 50.535  0 462 LYS EEE C   1 ? 18 
ATOM   6153  O O   . LYS E  1 133 ? 39.746  -56.486  -2.965  1.000 48.357  0 462 LYS EEE O   1 ? 18 
ATOM   6154  C CB  . LYS E  1 133 ? 40.114  -59.800  -3.291  1.000 58.482  0 462 LYS EEE CB  1 ? 18 
ATOM   6155  C CG  . LYS E  1 133 ? 40.532  -61.061  -4.038  1.000 63.846  0 462 LYS EEE CG  1 ? 18 
ATOM   6156  C CD  . LYS E  1 133 ? 40.774  -62.242  -3.129  1.000 69.644  0 462 LYS EEE CD  1 ? 18 
ATOM   6157  C CE  . LYS E  1 133 ? 41.392  -61.852  -1.794  1.000 71.384  0 462 LYS EEE CE  1 ? 18 
ATOM   6158  N NZ  . LYS E  1 133 ? 41.558  -63.030  -0.917  1.000 75.485  0 462 LYS EEE NZ  1 ? 18 
ATOM   6159  N N   . PRO E  1 134 ? 37.807  -57.533  -3.297  1.000 50.755  0 463 PRO EEE N   1 ? 18 
ATOM   6160  C CA  . PRO E  1 134 ? 37.049  -56.498  -2.589  1.000 48.237  0 463 PRO EEE CA  1 ? 18 
ATOM   6161  C C   . PRO E  1 134 ? 37.578  -56.263  -1.175  1.000 45.573  0 463 PRO EEE C   1 ? 18 
ATOM   6162  O O   . PRO E  1 134 ? 37.832  -57.208  -0.497  1.000 47.109  0 463 PRO EEE O   1 ? 18 
ATOM   6163  C CB  . PRO E  1 134 ? 35.620  -57.049  -2.609  1.000 48.304  0 463 PRO EEE CB  1 ? 18 
ATOM   6164  C CG  . PRO E  1 134 ? 35.588  -57.851  -3.891  1.000 49.834  0 463 PRO EEE CG  1 ? 18 
ATOM   6165  C CD  . PRO E  1 134 ? 36.929  -58.533  -3.925  1.000 51.821  0 463 PRO EEE CD  1 ? 18 
ATOM   6166  N N   . PHE E  1 135 ? 37.787  -54.998  -0.826  1.000 44.971  0 464 PHE EEE N   1 ? 18 
ATOM   6167  C CA  . PHE E  1 135 ? 38.275  -54.521  0.498   1.000 45.569  0 464 PHE EEE CA  1 ? 18 
ATOM   6168  C C   . PHE E  1 135 ? 39.706  -54.992  0.766   1.000 45.918  0 464 PHE EEE C   1 ? 18 
ATOM   6169  O O   . PHE E  1 135 ? 40.140  -54.890  1.903   1.000 48.035  0 464 PHE EEE O   1 ? 18 
ATOM   6170  C CB  . PHE E  1 135 ? 37.327  -54.972  1.614   1.000 45.511  0 464 PHE EEE CB  1 ? 18 
ATOM   6171  C CG  . PHE E  1 135 ? 35.959  -54.349  1.551   1.000 44.192  0 464 PHE EEE CG  1 ? 18 
ATOM   6172  C CD1 . PHE E  1 135 ? 35.825  -52.979  1.510   1.000 43.403  0 464 PHE EEE CD1 1 ? 18 
ATOM   6173  C CD2 . PHE E  1 135 ? 34.815  -55.129  1.523   1.000 47.009  0 464 PHE EEE CD2 1 ? 18 
ATOM   6174  C CE1 . PHE E  1 135 ? 34.576  -52.386  1.458   1.000 43.403  0 464 PHE EEE CE1 1 ? 18 
ATOM   6175  C CE2 . PHE E  1 135 ? 33.564  -54.543  1.460   1.000 48.152  0 464 PHE EEE CE2 1 ? 18 
ATOM   6176  C CZ  . PHE E  1 135 ? 33.452  -53.171  1.419   1.000 45.103  0 464 PHE EEE CZ  1 ? 18 
ATOM   6177  N N   . GLU E  1 136 ? 40.430  -55.466  -0.245  1.000 48.289  0 465 GLU EEE N   1 ? 18 
ATOM   6178  C CA  . GLU E  1 136 ? 41.867  -55.796  -0.103  1.000 49.862  0 465 GLU EEE CA  1 ? 18 
ATOM   6179  C C   . GLU E  1 136 ? 42.656  -54.481  -0.106  1.000 47.641  0 465 GLU EEE C   1 ? 18 
ATOM   6180  O O   . GLU E  1 136 ? 42.210  -53.469  -0.693  1.000 44.762  0 465 GLU EEE O   1 ? 18 
ATOM   6181  C CB  . GLU E  1 136 ? 42.324  -56.759  -1.193  1.000 52.611  0 465 GLU EEE CB  1 ? 18 
ATOM   6182  C CG  . GLU E  1 136 ? 43.666  -57.433  -0.914  1.000 54.866  0 465 GLU EEE CG  1 ? 18 
ATOM   6183  C CD  . GLU E  1 136 ? 44.166  -58.381  -2.003  1.000 58.088  0 465 GLU EEE CD  1 ? 18 
ATOM   6184  O OE1 . GLU E  1 136 ? 43.434  -58.601  -2.991  1.000 58.934  0 465 GLU EEE OE1 1 ? 18 
ATOM   6185  O OE2 . GLU E  1 136 ? 45.279  -58.916  -1.865  1.000 62.248  0 465 GLU EEE OE2 1 ? 18 
ATOM   6186  N N   . ARG E  1 137 ? 43.788  -54.494  0.593   1.000 48.945  0 466 ARG EEE N   1 ? 18 
ATOM   6187  C CA  . ARG E  1 137 ? 44.668  -53.317  0.770   1.000 48.154  0 466 ARG EEE CA  1 ? 18 
ATOM   6188  C C   . ARG E  1 137 ? 46.089  -53.778  0.484   1.000 45.856  0 466 ARG EEE C   1 ? 18 
ATOM   6189  O O   . ARG E  1 137 ? 46.484  -54.748  1.059   1.000 46.404  0 466 ARG EEE O   1 ? 18 
ATOM   6190  C CB  . ARG E  1 137 ? 44.526  -52.802  2.198   1.000 48.987  0 466 ARG EEE CB  1 ? 18 
ATOM   6191  C CG  . ARG E  1 137 ? 45.225  -51.479  2.463   1.000 50.992  0 466 ARG EEE CG  1 ? 18 
ATOM   6192  C CD  . ARG E  1 137 ? 44.610  -50.984  3.763   1.000 49.371  0 466 ARG EEE CD  1 ? 18 
ATOM   6193  N NE  . ARG E  1 137 ? 45.150  -49.716  4.168   1.000 48.615  0 466 ARG EEE NE  1 ? 18 
ATOM   6194  C CZ  . ARG E  1 137 ? 46.225  -49.559  4.938   1.000 53.034  0 466 ARG EEE CZ  1 ? 18 
ATOM   6195  N NH1 . ARG E  1 137 ? 46.921  -50.614  5.361   1.000 54.267  0 466 ARG EEE NH1 1 ? 18 
ATOM   6196  N NH2 . ARG E  1 137 ? 46.607  -48.344  5.304   1.000 54.082  0 466 ARG EEE NH2 1 ? 18 
ATOM   6197  N N   . ASP E  1 138 ? 46.803  -53.090  -0.383  1.000 44.917  0 467 ASP EEE N   1 ? 18 
ATOM   6198  C CA  . ASP E  1 138 ? 48.215  -53.390  -0.695  1.000 47.454  0 467 ASP EEE CA  1 ? 18 
ATOM   6199  C C   . ASP E  1 138 ? 49.010  -52.115  -0.440  1.000 47.460  0 467 ASP EEE C   1 ? 18 
ATOM   6200  O O   . ASP E  1 138 ? 48.769  -51.113  -1.143  1.000 47.201  0 467 ASP EEE O   1 ? 18 
ATOM   6201  C CB  . ASP E  1 138 ? 48.319  -53.895  -2.126  1.000 48.264  0 467 ASP EEE CB  1 ? 18 
ATOM   6202  C CG  . ASP E  1 138 ? 49.690  -54.341  -2.549  1.000 51.590  0 467 ASP EEE CG  1 ? 18 
ATOM   6203  O OD1 . ASP E  1 138 ? 50.666  -54.062  -1.782  1.000 52.545  0 467 ASP EEE OD1 1 ? 18 
ATOM   6204  O OD2 . ASP E  1 138 ? 49.765  -54.942  -3.655  1.000 54.689  0 467 ASP EEE OD2 1 ? 18 
ATOM   6205  N N   . ILE E  1 139 ? 49.909  -52.144  0.543   1.000 48.829  0 468 ILE EEE N   1 ? 18 
ATOM   6206  C CA  . ILE E  1 139 ? 50.792  -50.985  0.878   1.000 48.091  0 468 ILE EEE CA  1 ? 18 
ATOM   6207  C C   . ILE E  1 139 ? 52.244  -51.379  0.601   1.000 51.476  0 468 ILE EEE C   1 ? 18 
ATOM   6208  O O   . ILE E  1 139 ? 53.157  -50.642  1.044   1.000 53.063  0 468 ILE EEE O   1 ? 18 
ATOM   6209  C CB  . ILE E  1 139 ? 50.562  -50.513  2.326   1.000 47.084  0 468 ILE EEE CB  1 ? 18 
ATOM   6210  C CG1 . ILE E  1 139 ? 50.859  -51.584  3.370   1.000 48.436  0 468 ILE EEE CG1 1 ? 18 
ATOM   6211  C CG2 . ILE E  1 139 ? 49.151  -50.037  2.500   1.000 44.392  0 468 ILE EEE CG2 1 ? 18 
ATOM   6212  C CD1 . ILE E  1 139 ? 51.001  -51.026  4.776   1.000 49.252  0 468 ILE EEE CD1 1 ? 18 
ATOM   6213  N N   . SER E  1 140 ? 52.477  -52.482  -0.121  1.000 52.772  0 469 SER EEE N   1 ? 18 
ATOM   6214  C CA  . SER E  1 140 ? 53.841  -52.898  -0.552  1.000 55.495  0 469 SER EEE CA  1 ? 18 
ATOM   6215  C C   . SER E  1 140 ? 54.394  -51.877  -1.550  1.000 54.771  0 469 SER EEE C   1 ? 18 
ATOM   6216  O O   . SER E  1 140 ? 53.608  -51.228  -2.243  1.000 51.272  0 469 SER EEE O   1 ? 18 
ATOM   6217  C CB  . SER E  1 140 ? 53.873  -54.283  -1.124  1.000 57.828  0 469 SER EEE CB  1 ? 18 
ATOM   6218  O OG  . SER E  1 140 ? 53.156  -54.321  -2.341  1.000 58.406  0 469 SER EEE OG  1 ? 18 
ATOM   6219  N N   . THR E  1 141 ? 55.710  -51.726  -1.564  1.000 57.961  0 470 THR EEE N   1 ? 18 
ATOM   6220  C CA  . THR E  1 141 ? 56.446  -50.774  -2.419  1.000 60.310  0 470 THR EEE CA  1 ? 18 
ATOM   6221  C C   . THR E  1 141 ? 57.646  -51.530  -2.962  1.000 64.849  0 470 THR EEE C   1 ? 18 
ATOM   6222  O O   . THR E  1 141 ? 58.698  -50.919  -3.076  1.000 66.111  0 470 THR EEE O   1 ? 18 
ATOM   6223  C CB  . THR E  1 141 ? 56.848  -49.513  -1.631  1.000 59.706  0 470 THR EEE CB  1 ? 18 
ATOM   6224  O OG1 . THR E  1 141 ? 57.485  -49.889  -0.419  1.000 60.981  0 470 THR EEE OG1 1 ? 18 
ATOM   6225  C CG2 . THR E  1 141 ? 55.689  -48.655  -1.211  1.000 56.575  0 470 THR EEE CG2 1 ? 18 
ATOM   6226  N N   . GLU E  1 142 ? 57.481  -52.807  -3.323  1.000 70.367  0 471 GLU EEE N   1 ? 18 
ATOM   6227  C CA  . GLU E  1 142 ? 58.472  -53.563  -4.120  1.000 76.297  0 471 GLU EEE CA  1 ? 18 
ATOM   6228  C C   . GLU E  1 142 ? 58.446  -53.035  -5.552  1.000 77.694  0 471 GLU EEE C   1 ? 18 
ATOM   6229  O O   . GLU E  1 142 ? 57.351  -52.711  -6.073  1.000 75.336  0 471 GLU EEE O   1 ? 18 
ATOM   6230  C CB  . GLU E  1 142 ? 58.164  -55.047  -4.041  1.000 80.005  0 471 GLU EEE CB  1 ? 18 
ATOM   6231  C CG  . GLU E  1 142 ? 58.512  -55.588  -2.669  1.000 84.686  0 471 GLU EEE CG  1 ? 18 
ATOM   6232  C CD  . GLU E  1 142 ? 58.215  -57.077  -2.526  1.000 90.430  0 471 GLU EEE CD  1 ? 18 
ATOM   6233  O OE1 . GLU E  1 142 ? 57.001  -57.420  -2.629  1.000 90.394  0 471 GLU EEE OE1 1 ? 18 
ATOM   6234  O OE2 . GLU E  1 142 ? 59.188  -57.901  -2.334  1.000 94.963  0 471 GLU EEE OE2 1 ? 18 
ATOM   6235  N N   . ILE E  1 143 ? 59.630  -52.931  -6.142  1.000 83.701  0 472 ILE EEE N   1 ? 18 
ATOM   6236  C CA  . ILE E  1 143 ? 59.821  -52.551  -7.567  1.000 88.823  0 472 ILE EEE CA  1 ? 18 
ATOM   6237  C C   . ILE E  1 143 ? 59.055  -53.573  -8.413  1.000 93.047  0 472 ILE EEE C   1 ? 18 
ATOM   6238  O O   . ILE E  1 143 ? 59.268  -54.770  -8.206  1.000 95.366  0 472 ILE EEE O   1 ? 18 
ATOM   6239  C CB  . ILE E  1 143 ? 61.318  -52.512  -7.905  1.000 93.603  0 472 ILE EEE CB  1 ? 18 
ATOM   6240  C CG1 . ILE E  1 143 ? 62.111  -51.546  -7.021  1.000 93.835  0 472 ILE EEE CG1 1 ? 18 
ATOM   6241  C CG2 . ILE E  1 143 ? 61.496  -52.169  -9.349  1.000 96.179  0 472 ILE EEE CG2 1 ? 18 
ATOM   6242  C CD1 . ILE E  1 143 ? 61.511  -50.152  -6.943  1.000 90.461  0 472 ILE EEE CD1 1 ? 18 
ATOM   6243  N N   . TYR E  1 144 ? 58.181  -53.096  -9.296  1.000 97.306  0 473 TYR EEE N   1 ? 18 
ATOM   6244  C CA  . TYR E  1 144 ? 57.272  -53.901  -10.157 1.000 104.023 0 473 TYR EEE CA  1 ? 18 
ATOM   6245  C C   . TYR E  1 144 ? 58.080  -54.358  -11.371 1.000 111.983 0 473 TYR EEE C   1 ? 18 
ATOM   6246  O O   . TYR E  1 144 ? 58.774  -53.485  -12.062 1.000 114.772 0 473 TYR EEE O   1 ? 18 
ATOM   6247  C CB  . TYR E  1 144 ? 56.032  -53.074  -10.542 1.000 104.277 0 473 TYR EEE CB  1 ? 18 
ATOM   6248  C CG  . TYR E  1 144 ? 55.112  -53.656  -11.584 1.000 106.355 0 473 TYR EEE CG  1 ? 18 
ATOM   6249  C CD1 . TYR E  1 144 ? 54.094  -54.534  -11.220 1.000 105.888 0 473 TYR EEE CD1 1 ? 18 
ATOM   6250  C CD2 . TYR E  1 144 ? 55.254  -53.347  -12.929 1.000 108.011 0 473 TYR EEE CD2 1 ? 18 
ATOM   6251  C CE1 . TYR E  1 144 ? 53.206  -55.064  -12.156 1.000 105.084 0 473 TYR EEE CE1 1 ? 18 
ATOM   6252  C CE2 . TYR E  1 144 ? 54.419  -53.895  -13.891 1.000 106.272 0 473 TYR EEE CE2 1 ? 18 
ATOM   6253  C CZ  . TYR E  1 144 ? 53.401  -54.760  -13.501 1.000 105.681 0 473 TYR EEE CZ  1 ? 18 
ATOM   6254  O OH  . TYR E  1 144 ? 52.576  -55.271  -14.453 1.000 105.495 0 473 TYR EEE OH  1 ? 18 
ATOM   6255  N N   . GLN E  1 145 ? 58.055  -55.674  -11.586 1.000 118.515 0 474 GLN EEE N   1 ? 18 
ATOM   6256  C CA  . GLN E  1 145 ? 58.710  -56.328  -12.750 1.000 125.426 0 474 GLN EEE CA  1 ? 18 
ATOM   6257  C C   . GLN E  1 145 ? 57.735  -56.223  -13.925 1.000 130.155 0 474 GLN EEE C   1 ? 18 
ATOM   6258  O O   . GLN E  1 145 ? 56.751  -57.012  -13.975 1.000 128.662 0 474 GLN EEE O   1 ? 18 
ATOM   6259  C CB  . GLN E  1 145 ? 59.032  -57.811  -12.499 1.000 123.581 0 474 GLN EEE CB  1 ? 18 
ATOM   6260  C CG  . GLN E  1 145 ? 60.462  -58.227  -12.881 1.000 125.350 0 474 GLN EEE CG  1 ? 18 
ATOM   6261  C CD  . GLN E  1 145 ? 61.369  -57.867  -11.732 1.000 123.359 0 474 GLN EEE CD  1 ? 18 
ATOM   6262  O OE1 . GLN E  1 145 ? 61.122  -56.894  -11.016 1.000 116.582 0 474 GLN EEE OE1 1 ? 18 
ATOM   6263  N NE2 . GLN E  1 145 ? 62.404  -58.664  -11.513 1.000 125.831 0 474 GLN EEE NE2 1 ? 18 
ATOM   6264  N N   . ALA E  1 146 ? 58.015  -55.294  -14.854 1.000 132.101 0 475 ALA EEE N   1 ? 18 
ATOM   6265  C CA  . ALA E  1 146 ? 57.373  -55.206  -16.181 1.000 130.690 0 475 ALA EEE CA  1 ? 18 
ATOM   6266  C C   . ALA E  1 146 ? 58.108  -56.118  -17.180 1.000 136.061 0 475 ALA EEE C   1 ? 18 
ATOM   6267  O O   . ALA E  1 146 ? 57.574  -56.308  -18.291 1.000 139.982 0 475 ALA EEE O   1 ? 18 
ATOM   6268  C CB  . ALA E  1 146 ? 57.361  -53.769  -16.616 1.000 128.038 0 475 ALA EEE CB  1 ? 18 
ATOM   6269  N N   . GLY E  1 147 ? 59.273  -56.652  -16.827 1.000 135.240 0 476 GLY EEE N   1 ? 18 
ATOM   6270  C CA  . GLY E  1 147 ? 60.089  -57.440  -17.762 1.000 136.924 0 476 GLY EEE CA  1 ? 18 
ATOM   6271  C C   . GLY E  1 147 ? 60.605  -58.718  -17.151 1.000 136.471 0 476 GLY EEE C   1 ? 18 
ATOM   6272  O O   . GLY E  1 147 ? 60.509  -58.882  -15.927 1.000 132.620 0 476 GLY EEE O   1 ? 18 
ATOM   6273  N N   . SER E  1 148 ? 61.204  -59.552  -18.002 1.000 137.962 0 477 SER EEE N   1 ? 18 
ATOM   6274  C CA  . SER E  1 148 ? 61.975  -60.768  -17.654 1.000 139.615 0 477 SER EEE CA  1 ? 18 
ATOM   6275  C C   . SER E  1 148 ? 63.079  -60.446  -16.633 1.000 140.862 0 477 SER EEE C   1 ? 18 
ATOM   6276  O O   . SER E  1 148 ? 63.204  -61.214  -15.675 1.000 139.643 0 477 SER EEE O   1 ? 18 
ATOM   6277  C CB  . SER E  1 148 ? 62.528  -61.367  -18.921 1.000 143.077 0 477 SER EEE CB  1 ? 18 
ATOM   6278  O OG  . SER E  1 148 ? 63.320  -62.515  -18.670 1.000 145.392 0 477 SER EEE OG  1 ? 18 
ATOM   6279  N N   . THR E  1 149 ? 63.860  -59.375  -16.843 1.000 143.410 0 478 THR EEE N   1 ? 18 
ATOM   6280  C CA  . THR E  1 149 ? 65.096  -59.048  -16.084 1.000 145.722 0 478 THR EEE CA  1 ? 18 
ATOM   6281  C C   . THR E  1 149 ? 64.781  -58.759  -14.614 1.000 144.981 0 478 THR EEE C   1 ? 18 
ATOM   6282  O O   . THR E  1 149 ? 63.785  -58.097  -14.297 1.000 134.419 0 478 THR EEE O   1 ? 18 
ATOM   6283  C CB  . THR E  1 149 ? 65.876  -57.890  -16.728 1.000 145.502 0 478 THR EEE CB  1 ? 18 
ATOM   6284  O OG1 . THR E  1 149 ? 66.039  -58.193  -18.112 1.000 148.494 0 478 THR EEE OG1 1 ? 18 
ATOM   6285  C CG2 . THR E  1 149 ? 67.269  -57.695  -16.169 1.000 147.450 0 478 THR EEE CG2 1 ? 18 
ATOM   6286  N N   . PRO E  1 150 ? 65.626  -59.266  -13.678 1.000 149.200 0 479 PRO EEE N   1 ? 18 
ATOM   6287  C CA  . PRO E  1 150 ? 65.532  -58.905  -12.269 1.000 145.901 0 479 PRO EEE CA  1 ? 18 
ATOM   6288  C C   . PRO E  1 150 ? 65.863  -57.420  -12.056 1.000 143.096 0 479 PRO EEE C   1 ? 18 
ATOM   6289  O O   . PRO E  1 150 ? 66.587  -56.865  -12.840 1.000 143.487 0 479 PRO EEE O   1 ? 18 
ATOM   6290  C CB  . PRO E  1 150 ? 66.553  -59.854  -11.594 1.000 149.101 0 479 PRO EEE CB  1 ? 18 
ATOM   6291  C CG  . PRO E  1 150 ? 67.576  -60.141  -12.663 1.000 152.126 0 479 PRO EEE CG  1 ? 18 
ATOM   6292  C CD  . PRO E  1 150 ? 66.723  -60.216  -13.905 1.000 151.833 0 479 PRO EEE CD  1 ? 18 
ATOM   6293  N N   . CYS E  1 151 ? 65.280  -56.809  -11.018 1.000 138.892 0 480 CYS EEE N   1 ? 18 
ATOM   6294  C CA  . CYS E  1 151 ? 65.274  -55.339  -10.791 1.000 133.735 0 480 CYS EEE CA  1 ? 18 
ATOM   6295  C C   . CYS E  1 151 ? 66.349  -54.897  -9.792  1.000 132.029 0 480 CYS EEE C   1 ? 18 
ATOM   6296  O O   . CYS E  1 151 ? 66.637  -53.683  -9.698  1.000 128.485 0 480 CYS EEE O   1 ? 18 
ATOM   6297  C CB  . CYS E  1 151 ? 63.892  -54.921  -10.312 1.000 129.161 0 480 CYS EEE CB  1 ? 18 
ATOM   6298  S SG  . CYS E  1 151 ? 62.742  -54.840  -11.711 1.000 138.603 0 480 CYS EEE SG  1 ? 18 
ATOM   6299  N N   . ASN E  1 152 ? 66.872  -55.848  -9.019  1.000 132.782 0 481 ASN EEE N   1 ? 18 
ATOM   6300  C CA  . ASN E  1 152 ? 67.866  -55.627  -7.932  1.000 132.843 0 481 ASN EEE CA  1 ? 18 
ATOM   6301  C C   . ASN E  1 152 ? 67.420  -54.475  -7.018  1.000 126.191 0 481 ASN EEE C   1 ? 18 
ATOM   6302  O O   . ASN E  1 152 ? 68.308  -53.741  -6.558  1.000 125.258 0 481 ASN EEE O   1 ? 18 
ATOM   6303  C CB  . ASN E  1 152 ? 69.260  -55.355  -8.495  1.000 136.265 0 481 ASN EEE CB  1 ? 18 
ATOM   6304  C CG  . ASN E  1 152 ? 69.778  -56.452  -9.400  1.000 138.946 0 481 ASN EEE CG  1 ? 18 
ATOM   6305  O OD1 . ASN E  1 152 ? 69.022  -57.263  -9.933  1.000 138.074 0 481 ASN EEE OD1 1 ? 18 
ATOM   6306  N ND2 . ASN E  1 152 ? 71.078  -56.467  -9.591  1.000 142.244 0 481 ASN EEE ND2 1 ? 18 
ATOM   6307  N N   . GLY E  1 153 ? 66.108  -54.322  -6.768  1.000 122.565 0 482 GLY EEE N   1 ? 18 
ATOM   6308  C CA  . GLY E  1 153 ? 65.502  -53.295  -5.890  1.000 115.498 0 482 GLY EEE CA  1 ? 18 
ATOM   6309  C C   . GLY E  1 153 ? 65.887  -51.865  -6.270  1.000 114.199 0 482 GLY EEE C   1 ? 18 
ATOM   6310  O O   . GLY E  1 153 ? 65.933  -51.011  -5.352  1.000 110.182 0 482 GLY EEE O   1 ? 18 
ATOM   6311  N N   . VAL E  1 154 ? 66.169  -51.607  -7.561  1.000 113.665 0 483 VAL EEE N   1 ? 18 
ATOM   6312  C CA  . VAL E  1 154 ? 66.441  -50.242  -8.093  1.000 107.899 0 483 VAL EEE CA  1 ? 18 
ATOM   6313  C C   . VAL E  1 154 ? 65.471  -49.973  -9.244  1.000 103.881 0 483 VAL EEE C   1 ? 18 
ATOM   6314  O O   . VAL E  1 154 ? 65.153  -50.916  -9.986  1.000 104.816 0 483 VAL EEE O   1 ? 18 
ATOM   6315  C CB  . VAL E  1 154 ? 67.900  -50.009  -8.520  1.000 111.142 0 483 VAL EEE CB  1 ? 18 
ATOM   6316  C CG1 . VAL E  1 154 ? 68.188  -50.450  -9.940  1.000 114.530 0 483 VAL EEE CG1 1 ? 18 
ATOM   6317  C CG2 . VAL E  1 154 ? 68.248  -48.536  -8.376  1.000 109.887 0 483 VAL EEE CG2 1 ? 18 
ATOM   6318  N N   . GLU E  1 155 ? 65.063  -48.714  -9.384  1.000 98.920  0 484 GLU EEE N   1 ? 18 
ATOM   6319  C CA  . GLU E  1 155 ? 64.198  -48.210  -10.472 1.000 95.988  0 484 GLU EEE CA  1 ? 18 
ATOM   6320  C C   . GLU E  1 155 ? 65.004  -48.077  -11.772 1.000 99.936  0 484 GLU EEE C   1 ? 18 
ATOM   6321  O O   . GLU E  1 155 ? 66.220  -47.841  -11.689 1.000 102.557 0 484 GLU EEE O   1 ? 18 
ATOM   6322  C CB  . GLU E  1 155 ? 63.618  -46.871  -10.045 1.000 91.917  0 484 GLU EEE CB  1 ? 18 
ATOM   6323  C CG  . GLU E  1 155 ? 62.393  -46.444  -10.798 1.000 90.124  0 484 GLU EEE CG  1 ? 18 
ATOM   6324  C CD  . GLU E  1 155 ? 61.490  -45.497  -10.016 1.000 86.461  0 484 GLU EEE CD  1 ? 18 
ATOM   6325  O OE1 . GLU E  1 155 ? 61.941  -44.946  -8.976  1.000 85.764  0 484 GLU EEE OE1 1 ? 18 
ATOM   6326  O OE2 . GLU E  1 155 ? 60.307  -45.361  -10.406 1.000 81.797  0 484 GLU EEE OE2 1 ? 18 
ATOM   6327  N N   . GLY E  1 156 ? 64.337  -48.261  -12.925 1.000 99.242  0 485 GLY EEE N   1 ? 18 
ATOM   6328  C CA  . GLY E  1 156 ? 64.985  -48.249  -14.254 1.000 103.119 0 485 GLY EEE CA  1 ? 18 
ATOM   6329  C C   . GLY E  1 156 ? 64.168  -48.991  -15.297 1.000 104.404 0 485 GLY EEE C   1 ? 18 
ATOM   6330  O O   . GLY E  1 156 ? 62.975  -49.189  -15.064 1.000 101.569 0 485 GLY EEE O   1 ? 18 
ATOM   6331  N N   . PHE E  1 157 ? 64.784  -49.336  -16.426 1.000 111.402 0 486 PHE EEE N   1 ? 18 
ATOM   6332  C CA  . PHE E  1 157 ? 64.161  -50.033  -17.583 1.000 115.856 0 486 PHE EEE CA  1 ? 18 
ATOM   6333  C C   . PHE E  1 157 ? 63.425  -51.277  -17.067 1.000 116.193 0 486 PHE EEE C   1 ? 18 
ATOM   6334  O O   . PHE E  1 157 ? 64.068  -52.107  -16.403 1.000 116.571 0 486 PHE EEE O   1 ? 18 
ATOM   6335  C CB  . PHE E  1 157 ? 65.245  -50.375  -18.619 1.000 123.630 0 486 PHE EEE CB  1 ? 18 
ATOM   6336  C CG  . PHE E  1 157 ? 64.806  -51.161  -19.836 1.000 128.785 0 486 PHE EEE CG  1 ? 18 
ATOM   6337  C CD1 . PHE E  1 157 ? 63.901  -50.608  -20.728 1.000 128.091 0 486 PHE EEE CD1 1 ? 18 
ATOM   6338  C CD2 . PHE E  1 157 ? 65.338  -52.423  -20.129 1.000 134.008 0 486 PHE EEE CD2 1 ? 18 
ATOM   6339  C CE1 . PHE E  1 157 ? 63.517  -51.302  -21.873 1.000 131.651 0 486 PHE EEE CE1 1 ? 18 
ATOM   6340  C CE2 . PHE E  1 157 ? 64.937  -53.121  -21.260 1.000 136.336 0 486 PHE EEE CE2 1 ? 18 
ATOM   6341  C CZ  . PHE E  1 157 ? 64.040  -52.553  -22.140 1.000 135.513 0 486 PHE EEE CZ  1 ? 18 
ATOM   6342  N N   . ASN E  1 158 ? 62.115  -51.379  -17.336 1.000 116.566 0 487 ASN EEE N   1 ? 18 
ATOM   6343  C CA  . ASN E  1 158 ? 61.254  -52.550  -16.996 1.000 118.759 0 487 ASN EEE CA  1 ? 18 
ATOM   6344  C C   . ASN E  1 158 ? 61.176  -52.764  -15.477 1.000 117.965 0 487 ASN EEE C   1 ? 18 
ATOM   6345  O O   . ASN E  1 158 ? 60.742  -53.863  -15.054 1.000 120.849 0 487 ASN EEE O   1 ? 18 
ATOM   6346  C CB  . ASN E  1 158 ? 61.720  -53.835  -17.698 1.000 121.991 0 487 ASN EEE CB  1 ? 18 
ATOM   6347  C CG  . ASN E  1 158 ? 61.511  -53.797  -19.198 1.000 124.265 0 487 ASN EEE CG  1 ? 18 
ATOM   6348  O OD1 . ASN E  1 158 ? 62.252  -54.452  -19.937 1.000 127.871 0 487 ASN EEE OD1 1 ? 18 
ATOM   6349  N ND2 . ASN E  1 158 ? 60.544  -53.015  -19.667 1.000 121.897 0 487 ASN EEE ND2 1 ? 18 
ATOM   6350  N N   . CYS E  1 159 ? 61.568  -51.758  -14.688 1.000 116.202 0 488 CYS EEE N   1 ? 18 
ATOM   6351  C CA  . CYS E  1 159 ? 61.682  -51.851  -13.213 1.000 112.159 0 488 CYS EEE CA  1 ? 18 
ATOM   6352  C C   . CYS E  1 159 ? 61.073  -50.603  -12.594 1.000 102.842 0 488 CYS EEE C   1 ? 18 
ATOM   6353  O O   . CYS E  1 159 ? 61.841  -49.675  -12.266 1.000 101.509 0 488 CYS EEE O   1 ? 18 
ATOM   6354  C CB  . CYS E  1 159 ? 63.144  -51.999  -12.799 1.000 118.919 0 488 CYS EEE CB  1 ? 18 
ATOM   6355  S SG  . CYS E  1 159 ? 63.774  -53.673  -13.049 1.000 126.309 0 488 CYS EEE SG  1 ? 18 
ATOM   6356  N N   . TYR E  1 160 ? 59.748  -50.583  -12.443 1.000 83.890  0 489 TYR EEE N   1 ? 19 
ATOM   6357  C CA  . TYR E  1 160 ? 59.015  -49.362  -12.008 1.000 82.289  0 489 TYR EEE CA  1 ? 19 
ATOM   6358  C C   . TYR E  1 160 ? 58.723  -49.464  -10.512 1.000 76.160  0 489 TYR EEE C   1 ? 19 
ATOM   6359  O O   . TYR E  1 160 ? 58.380  -50.521  -10.026 1.000 73.462  0 489 TYR EEE O   1 ? 19 
ATOM   6360  C CB  . TYR E  1 160 ? 57.753  -49.108  -12.838 1.000 85.255  0 489 TYR EEE CB  1 ? 19 
ATOM   6361  C CG  . TYR E  1 160 ? 57.978  -49.256  -14.323 1.000 89.416  0 489 TYR EEE CG  1 ? 19 
ATOM   6362  C CD1 . TYR E  1 160 ? 59.048  -48.617  -14.944 1.000 92.141  0 489 TYR EEE CD1 1 ? 19 
ATOM   6363  C CD2 . TYR E  1 160 ? 57.181  -50.087  -15.095 1.000 91.453  0 489 TYR EEE CD2 1 ? 19 
ATOM   6364  C CE1 . TYR E  1 160 ? 59.339  -48.820  -16.278 1.000 94.990  0 489 TYR EEE CE1 1 ? 19 
ATOM   6365  C CE2 . TYR E  1 160 ? 57.421  -50.239  -16.450 1.000 95.846  0 489 TYR EEE CE2 1 ? 19 
ATOM   6366  C CZ  . TYR E  1 160 ? 58.521  -49.632  -17.033 1.000 97.787  0 489 TYR EEE CZ  1 ? 19 
ATOM   6367  O OH  . TYR E  1 160 ? 58.791  -49.792  -18.357 1.000 104.070 0 489 TYR EEE OH  1 ? 19 
ATOM   6368  N N   . PHE E  1 161 ? 58.950  -48.378  -9.783  1.000 72.109  0 490 PHE EEE N   1 ? 19 
ATOM   6369  C CA  . PHE E  1 161 ? 58.386  -48.179  -8.431  1.000 66.892  0 490 PHE EEE CA  1 ? 19 
ATOM   6370  C C   . PHE E  1 161 ? 56.878  -48.138  -8.642  1.000 63.524  0 490 PHE EEE C   1 ? 19 
ATOM   6371  O O   . PHE E  1 161 ? 56.425  -47.444  -9.539  1.000 63.916  0 490 PHE EEE O   1 ? 19 
ATOM   6372  C CB  . PHE E  1 161 ? 58.974  -46.922  -7.795  1.000 65.590  0 490 PHE EEE CB  1 ? 19 
ATOM   6373  C CG  . PHE E  1 161 ? 58.554  -46.711  -6.370  1.000 63.107  0 490 PHE EEE CG  1 ? 19 
ATOM   6374  C CD1 . PHE E  1 161 ? 59.115  -47.460  -5.344  1.000 62.841  0 490 PHE EEE CD1 1 ? 19 
ATOM   6375  C CD2 . PHE E  1 161 ? 57.582  -45.774  -6.063  1.000 61.633  0 490 PHE EEE CD2 1 ? 19 
ATOM   6376  C CE1 . PHE E  1 161 ? 58.696  -47.285  -4.038  1.000 62.466  0 490 PHE EEE CE1 1 ? 19 
ATOM   6377  C CE2 . PHE E  1 161 ? 57.181  -45.581  -4.749  1.000 60.363  0 490 PHE EEE CE2 1 ? 19 
ATOM   6378  C CZ  . PHE E  1 161 ? 57.722  -46.354  -3.743  1.000 62.064  0 490 PHE EEE CZ  1 ? 19 
ATOM   6379  N N   . PRO E  1 162 ? 56.071  -48.931  -7.907  1.000 61.163  0 491 PRO EEE N   1 ? 19 
ATOM   6380  C CA  . PRO E  1 162 ? 54.678  -49.163  -8.274  1.000 58.914  0 491 PRO EEE CA  1 ? 19 
ATOM   6381  C C   . PRO E  1 162 ? 53.703  -48.026  -7.916  1.000 57.241  0 491 PRO EEE C   1 ? 19 
ATOM   6382  O O   . PRO E  1 162 ? 52.561  -48.063  -8.369  1.000 57.161  0 491 PRO EEE O   1 ? 19 
ATOM   6383  C CB  . PRO E  1 162 ? 54.351  -50.451  -7.502  1.000 58.002  0 491 PRO EEE CB  1 ? 19 
ATOM   6384  C CG  . PRO E  1 162 ? 55.173  -50.338  -6.239  1.000 59.412  0 491 PRO EEE CG  1 ? 19 
ATOM   6385  C CD  . PRO E  1 162 ? 56.457  -49.681  -6.710  1.000 61.507  0 491 PRO EEE CD  1 ? 19 
ATOM   6386  N N   . LEU E  1 163 ? 54.130  -47.061  -7.104  1.000 54.972  0 492 LEU EEE N   1 ? 19 
ATOM   6387  C CA  . LEU E  1 163 ? 53.276  -45.913  -6.676  1.000 54.942  0 492 LEU EEE CA  1 ? 19 
ATOM   6388  C C   . LEU E  1 163 ? 53.613  -44.686  -7.518  1.000 54.996  0 492 LEU EEE C   1 ? 19 
ATOM   6389  O O   . LEU E  1 163 ? 54.764  -44.499  -7.816  1.000 57.453  0 492 LEU EEE O   1 ? 19 
ATOM   6390  C CB  . LEU E  1 163 ? 53.459  -45.608  -5.177  1.000 54.128  0 492 LEU EEE CB  1 ? 19 
ATOM   6391  C CG  . LEU E  1 163 ? 53.203  -46.774  -4.223  1.000 53.406  0 492 LEU EEE CG  1 ? 19 
ATOM   6392  C CD1 . LEU E  1 163 ? 53.284  -46.318  -2.803  1.000 52.305  0 492 LEU EEE CD1 1 ? 19 
ATOM   6393  C CD2 . LEU E  1 163 ? 51.862  -47.472  -4.505  1.000 51.964  0 492 LEU EEE CD2 1 ? 19 
ATOM   6394  N N   . GLN E  1 164 ? 52.618  -43.861  -7.828  1.000 54.980  0 493 GLN EEE N   1 ? 19 
ATOM   6395  C CA  . GLN E  1 164 ? 52.763  -42.571  -8.541  1.000 56.746  0 493 GLN EEE CA  1 ? 19 
ATOM   6396  C C   . GLN E  1 164 ? 52.036  -41.500  -7.714  1.000 54.585  0 493 GLN EEE C   1 ? 19 
ATOM   6397  O O   . GLN E  1 164 ? 51.069  -41.810  -6.996  1.000 52.266  0 493 GLN EEE O   1 ? 19 
ATOM   6398  C CB  . GLN E  1 164 ? 52.227  -42.744  -9.963  1.000 60.147  0 493 GLN EEE CB  1 ? 19 
ATOM   6399  C CG  . GLN E  1 164 ? 52.289  -41.491  -10.820 1.000 63.510  0 493 GLN EEE CG  1 ? 19 
ATOM   6400  C CD  . GLN E  1 164 ? 53.708  -41.118  -11.119 1.000 69.114  0 493 GLN EEE CD  1 ? 19 
ATOM   6401  O OE1 . GLN E  1 164 ? 54.509  -41.961  -11.506 1.000 74.801  0 493 GLN EEE OE1 1 ? 19 
ATOM   6402  N NE2 . GLN E  1 164 ? 54.028  -39.849  -10.938 1.000 72.626  0 493 GLN EEE NE2 1 ? 19 
ATOM   6403  N N   . SER E  1 165 ? 52.506  -40.269  -7.806  1.000 55.546  0 494 SER EEE N   1 ? 19 
ATOM   6404  C CA  . SER E  1 165 ? 51.970  -39.101  -7.083  1.000 54.741  0 494 SER EEE CA  1 ? 19 
ATOM   6405  C C   . SER E  1 165 ? 50.867  -38.449  -7.925  1.000 53.179  0 494 SER EEE C   1 ? 19 
ATOM   6406  O O   . SER E  1 165 ? 50.963  -38.486  -9.136  1.000 54.173  0 494 SER EEE O   1 ? 19 
ATOM   6407  C CB  . SER E  1 165 ? 53.108  -38.170  -6.781  1.000 57.779  0 494 SER EEE CB  1 ? 19 
ATOM   6408  O OG  . SER E  1 165 ? 52.640  -37.001  -6.133  1.000 62.072  0 494 SER EEE OG  1 ? 19 
ATOM   6409  N N   . TYR E  1 166 ? 49.838  -37.893  -7.305  1.000 51.747  0 495 TYR EEE N   1 ? 19 
ATOM   6410  C CA  . TYR E  1 166 ? 48.763  -37.143  -8.007  1.000 52.628  0 495 TYR EEE CA  1 ? 19 
ATOM   6411  C C   . TYR E  1 166 ? 49.264  -35.758  -8.428  1.000 55.938  0 495 TYR EEE C   1 ? 19 
ATOM   6412  O O   . TYR E  1 166 ? 48.902  -35.289  -9.514  1.000 57.954  0 495 TYR EEE O   1 ? 19 
ATOM   6413  C CB  . TYR E  1 166 ? 47.500  -37.007  -7.152  1.000 50.839  0 495 TYR EEE CB  1 ? 19 
ATOM   6414  C CG  . TYR E  1 166 ? 46.559  -38.179  -7.261  1.000 50.882  0 495 TYR EEE CG  1 ? 19 
ATOM   6415  C CD1 . TYR E  1 166 ? 45.851  -38.428  -8.433  1.000 50.137  0 495 TYR EEE CD1 1 ? 19 
ATOM   6416  C CD2 . TYR E  1 166 ? 46.394  -39.051  -6.194  1.000 50.376  0 495 TYR EEE CD2 1 ? 19 
ATOM   6417  C CE1 . TYR E  1 166 ? 44.999  -39.511  -8.535  1.000 49.711  0 495 TYR EEE CE1 1 ? 19 
ATOM   6418  C CE2 . TYR E  1 166 ? 45.563  -40.153  -6.292  1.000 50.050  0 495 TYR EEE CE2 1 ? 19 
ATOM   6419  C CZ  . TYR E  1 166 ? 44.852  -40.378  -7.461  1.000 49.208  0 495 TYR EEE CZ  1 ? 19 
ATOM   6420  O OH  . TYR E  1 166 ? 44.007  -41.444  -7.532  1.000 45.707  0 495 TYR EEE OH  1 ? 19 
ATOM   6421  N N   . GLY E  1 167 ? 50.035  -35.075  -7.598  1.000 57.146  0 496 GLY EEE N   1 ? 19 
ATOM   6422  C CA  . GLY E  1 167 ? 50.456  -33.703  -7.955  1.000 60.962  0 496 GLY EEE CA  1 ? 19 
ATOM   6423  C C   . GLY E  1 167 ? 49.266  -32.800  -8.222  1.000 61.248  0 496 GLY EEE C   1 ? 19 
ATOM   6424  O O   . GLY E  1 167 ? 48.956  -32.500  -9.402  1.000 61.156  0 496 GLY EEE O   1 ? 19 
ATOM   6425  N N   . PHE E  1 168 ? 48.570  -32.428  -7.148  1.000 60.132  0 497 PHE EEE N   1 ? 19 
ATOM   6426  C CA  . PHE E  1 168 ? 47.326  -31.617  -7.200  1.000 60.191  0 497 PHE EEE CA  1 ? 19 
ATOM   6427  C C   . PHE E  1 168 ? 47.706  -30.136  -7.191  1.000 61.645  0 497 PHE EEE C   1 ? 19 
ATOM   6428  O O   . PHE E  1 168 ? 48.293  -29.659  -6.185  1.000 61.031  0 497 PHE EEE O   1 ? 19 
ATOM   6429  C CB  . PHE E  1 168 ? 46.414  -31.940  -6.016  1.000 57.491  0 497 PHE EEE CB  1 ? 19 
ATOM   6430  C CG  . PHE E  1 168 ? 45.749  -33.294  -6.084  1.000 56.500  0 497 PHE EEE CG  1 ? 19 
ATOM   6431  C CD1 . PHE E  1 168 ? 44.886  -33.620  -7.126  1.000 55.511  0 497 PHE EEE CD1 1 ? 19 
ATOM   6432  C CD2 . PHE E  1 168 ? 45.958  -34.232  -5.081  1.000 55.036  0 497 PHE EEE CD2 1 ? 19 
ATOM   6433  C CE1 . PHE E  1 168 ? 44.263  -34.860  -7.166  1.000 53.789  0 497 PHE EEE CE1 1 ? 19 
ATOM   6434  C CE2 . PHE E  1 168 ? 45.334  -35.466  -5.123  1.000 53.662  0 497 PHE EEE CE2 1 ? 19 
ATOM   6435  C CZ  . PHE E  1 168 ? 44.494  -35.777  -6.167  1.000 53.760  0 497 PHE EEE CZ  1 ? 19 
ATOM   6436  N N   . GLN E  1 169 ? 47.331  -29.413  -8.254  1.000 62.435  0 498 GLN EEE N   1 ? 19 
ATOM   6437  C CA  . GLN E  1 169 ? 47.518  -27.946  -8.346  1.000 63.385  0 498 GLN EEE CA  1 ? 19 
ATOM   6438  C C   . GLN E  1 169 ? 46.166  -27.267  -8.330  1.000 62.056  0 498 GLN EEE C   1 ? 19 
ATOM   6439  O O   . GLN E  1 169 ? 45.225  -27.760  -8.937  1.000 63.025  0 498 GLN EEE O   1 ? 19 
ATOM   6440  C CB  . GLN E  1 169 ? 48.335  -27.649  -9.589  1.000 65.918  0 498 GLN EEE CB  1 ? 19 
ATOM   6441  C CG  . GLN E  1 169 ? 49.729  -28.129  -9.314  1.000 67.484  0 498 GLN EEE CG  1 ? 19 
ATOM   6442  C CD  . GLN E  1 169 ? 50.680  -28.157  -10.439 1.000 69.755  0 498 GLN EEE CD  1 ? 19 
ATOM   6443  O OE1 . GLN E  1 169 ? 50.593  -29.035  -11.274 1.000 71.112  0 498 GLN EEE OE1 1 ? 19 
ATOM   6444  N NE2 . GLN E  1 169 ? 51.626  -27.250  -10.349 1.000 73.533  0 498 GLN EEE NE2 1 ? 19 
ATOM   6445  N N   . PRO E  1 170 ? 46.054  -26.118  -7.638  1.000 61.738  0 499 PRO EEE N   1 ? 19 
ATOM   6446  C CA  . PRO E  1 170 ? 44.761  -25.436  -7.493  1.000 60.390  0 499 PRO EEE CA  1 ? 19 
ATOM   6447  C C   . PRO E  1 170 ? 44.150  -25.066  -8.852  1.000 60.258  0 499 PRO EEE C   1 ? 19 
ATOM   6448  O O   . PRO E  1 170 ? 42.952  -24.979  -8.930  1.000 59.476  0 499 PRO EEE O   1 ? 19 
ATOM   6449  C CB  . PRO E  1 170 ? 45.082  -24.187  -6.645  1.000 62.025  0 499 PRO EEE CB  1 ? 19 
ATOM   6450  C CG  . PRO E  1 170 ? 46.603  -24.034  -6.699  1.000 64.283  0 499 PRO EEE CG  1 ? 19 
ATOM   6451  C CD  . PRO E  1 170 ? 47.164  -25.421  -6.969  1.000 63.501  0 499 PRO EEE CD  1 ? 19 
ATOM   6452  N N   . THR E  1 171 ? 44.980  -24.915  -9.890  1.000 62.120  0 500 THR EEE N   1 ? 19 
ATOM   6453  C CA  . THR E  1 171 ? 44.591  -24.538  -11.276 1.000 63.500  0 500 THR EEE CA  1 ? 19 
ATOM   6454  C C   . THR E  1 171 ? 44.152  -25.750  -12.127 1.000 61.003  0 500 THR EEE C   1 ? 19 
ATOM   6455  O O   . THR E  1 171 ? 43.637  -25.511  -13.230 1.000 61.485  0 500 THR EEE O   1 ? 19 
ATOM   6456  C CB  . THR E  1 171 ? 45.763  -23.807  -11.938 1.000 67.227  0 500 THR EEE CB  1 ? 19 
ATOM   6457  O OG1 . THR E  1 171 ? 46.902  -24.659  -11.862 1.000 68.857  0 500 THR EEE OG1 1 ? 19 
ATOM   6458  C CG2 . THR E  1 171 ? 46.110  -22.500  -11.266 1.000 67.869  0 500 THR EEE CG2 1 ? 19 
ATOM   6459  N N   . ASN E  1 172 ? 44.327  -26.995  -11.664 1.000 57.537  0 501 ASN EEE N   1 ? 19 
ATOM   6460  C CA  . ASN E  1 172 ? 43.838  -28.210  -12.370 1.000 55.727  0 501 ASN EEE CA  1 ? 19 
ATOM   6461  C C   . ASN E  1 172 ? 42.366  -28.045  -12.760 1.000 54.051  0 501 ASN EEE C   1 ? 19 
ATOM   6462  O O   . ASN E  1 172 ? 41.629  -27.430  -11.986 1.000 51.558  0 501 ASN EEE O   1 ? 19 
ATOM   6463  C CB  . ASN E  1 172 ? 43.951  -29.450  -11.488 1.000 53.913  0 501 ASN EEE CB  1 ? 19 
ATOM   6464  C CG  . ASN E  1 172 ? 45.380  -29.911  -11.292 1.000 54.218  0 501 ASN EEE CG  1 ? 19 
ATOM   6465  O OD1 . ASN E  1 172 ? 46.284  -29.323  -11.863 1.000 55.781  0 501 ASN EEE OD1 1 ? 19 
ATOM   6466  N ND2 . ASN E  1 172 ? 45.581  -30.958  -10.494 1.000 52.397  0 501 ASN EEE ND2 1 ? 19 
ATOM   6467  N N   . GLY E  1 173 ? 41.945  -28.597  -13.903 1.000 54.931  0 502 GLY EEE N   1 ? 19 
ATOM   6468  C CA  . GLY E  1 173 ? 40.511  -28.779  -14.216 1.000 54.899  0 502 GLY EEE CA  1 ? 19 
ATOM   6469  C C   . GLY E  1 173 ? 39.826  -29.621  -13.140 1.000 52.799  0 502 GLY EEE C   1 ? 19 
ATOM   6470  O O   . GLY E  1 173 ? 40.521  -30.371  -12.432 1.000 51.195  0 502 GLY EEE O   1 ? 19 
ATOM   6471  N N   . VAL E  1 174 ? 38.508  -29.508  -13.013 1.000 53.496  0 503 VAL EEE N   1 ? 19 
ATOM   6472  C CA  . VAL E  1 174 ? 37.706  -30.108  -11.904 1.000 53.214  0 503 VAL EEE CA  1 ? 19 
ATOM   6473  C C   . VAL E  1 174 ? 37.974  -31.627  -11.811 1.000 52.139  0 503 VAL EEE C   1 ? 19 
ATOM   6474  O O   . VAL E  1 174 ? 38.124  -32.142  -10.672 1.000 51.465  0 503 VAL EEE O   1 ? 19 
ATOM   6475  C CB  . VAL E  1 174 ? 36.192  -29.854  -12.091 1.000 54.407  0 503 VAL EEE CB  1 ? 19 
ATOM   6476  C CG1 . VAL E  1 174 ? 35.394  -30.441  -10.921 1.000 55.169  0 503 VAL EEE CG1 1 ? 19 
ATOM   6477  C CG2 . VAL E  1 174 ? 35.849  -28.385  -12.269 1.000 56.507  0 503 VAL EEE CG2 1 ? 19 
ATOM   6478  N N   . GLY E  1 175 ? 38.011  -32.320  -12.950 1.000 52.139  0 504 GLY EEE N   1 ? 19 
ATOM   6479  C CA  . GLY E  1 175 ? 38.245  -33.778  -13.020 1.000 52.102  0 504 GLY EEE CA  1 ? 19 
ATOM   6480  C C   . GLY E  1 175 ? 39.602  -34.150  -12.464 1.000 52.645  0 504 GLY EEE C   1 ? 19 
ATOM   6481  O O   . GLY E  1 175 ? 39.750  -35.300  -12.055 1.000 52.522  0 504 GLY EEE O   1 ? 19 
ATOM   6482  N N   . TYR E  1 176 ? 40.571  -33.229  -12.431 1.000 55.220  0 505 TYR EEE N   1 ? 19 
ATOM   6483  C CA  . TYR E  1 176 ? 41.947  -33.500  -11.929 1.000 56.099  0 505 TYR EEE CA  1 ? 19 
ATOM   6484  C C   . TYR E  1 176 ? 42.140  -32.887  -10.540 1.000 52.976  0 505 TYR EEE C   1 ? 19 
ATOM   6485  O O   . TYR E  1 176 ? 43.262  -32.952  -10.013 1.000 54.022  0 505 TYR EEE O   1 ? 19 
ATOM   6486  C CB  . TYR E  1 176 ? 42.983  -32.991  -12.932 1.000 60.633  0 505 TYR EEE CB  1 ? 19 
ATOM   6487  C CG  . TYR E  1 176 ? 42.960  -33.690  -14.263 1.000 65.535  0 505 TYR EEE CG  1 ? 19 
ATOM   6488  C CD1 . TYR E  1 176 ? 43.683  -34.860  -14.455 1.000 68.169  0 505 TYR EEE CD1 1 ? 19 
ATOM   6489  C CD2 . TYR E  1 176 ? 42.245  -33.175  -15.339 1.000 69.843  0 505 TYR EEE CD2 1 ? 19 
ATOM   6490  C CE1 . TYR E  1 176 ? 43.671  -35.521  -15.675 1.000 70.632  0 505 TYR EEE CE1 1 ? 19 
ATOM   6491  C CE2 . TYR E  1 176 ? 42.219  -33.826  -16.564 1.000 72.704  0 505 TYR EEE CE2 1 ? 19 
ATOM   6492  C CZ  . TYR E  1 176 ? 42.933  -35.003  -16.729 1.000 73.450  0 505 TYR EEE CZ  1 ? 19 
ATOM   6493  O OH  . TYR E  1 176 ? 42.925  -35.638  -17.936 1.000 78.450  0 505 TYR EEE OH  1 ? 19 
ATOM   6494  N N   . GLN E  1 177 ? 41.085  -32.332  -9.937  1.000 51.429  0 506 GLN EEE N   1 ? 19 
ATOM   6495  C CA  . GLN E  1 177 ? 41.166  -31.799  -8.552  1.000 49.571  0 506 GLN EEE CA  1 ? 19 
ATOM   6496  C C   . GLN E  1 177 ? 41.016  -32.940  -7.564  1.000 46.908  0 506 GLN EEE C   1 ? 19 
ATOM   6497  O O   . GLN E  1 177 ? 40.394  -33.956  -7.853  1.000 45.430  0 506 GLN EEE O   1 ? 19 
ATOM   6498  C CB  . GLN E  1 177 ? 40.123  -30.717  -8.314  1.000 48.718  0 506 GLN EEE CB  1 ? 19 
ATOM   6499  C CG  . GLN E  1 177 ? 40.525  -29.409  -8.958  1.000 49.782  0 506 GLN EEE CG  1 ? 19 
ATOM   6500  C CD  . GLN E  1 177 ? 39.434  -28.378  -8.892  1.000 48.403  0 506 GLN EEE CD  1 ? 19 
ATOM   6501  O OE1 . GLN E  1 177 ? 38.581  -28.370  -8.013  1.000 48.043  0 506 GLN EEE OE1 1 ? 19 
ATOM   6502  N NE2 . GLN E  1 177 ? 39.467  -27.468  -9.825  1.000 48.986  0 506 GLN EEE NE2 1 ? 19 
ATOM   6503  N N   . PRO E  1 178 ? 41.558  -32.798  -6.345  1.000 47.774  0 507 PRO EEE N   1 ? 19 
ATOM   6504  C CA  . PRO E  1 178 ? 41.425  -33.846  -5.342  1.000 46.205  0 507 PRO EEE CA  1 ? 19 
ATOM   6505  C C   . PRO E  1 178 ? 39.980  -33.880  -4.835  1.000 44.962  0 507 PRO EEE C   1 ? 19 
ATOM   6506  O O   . PRO E  1 178 ? 39.344  -32.825  -4.694  1.000 46.089  0 507 PRO EEE O   1 ? 19 
ATOM   6507  C CB  . PRO E  1 178 ? 42.403  -33.419  -4.247  1.000 46.149  0 507 PRO EEE CB  1 ? 19 
ATOM   6508  C CG  . PRO E  1 178 ? 42.440  -31.909  -4.364  1.000 48.068  0 507 PRO EEE CG  1 ? 19 
ATOM   6509  C CD  . PRO E  1 178 ? 42.292  -31.624  -5.846  1.000 49.873  0 507 PRO EEE CD  1 ? 19 
ATOM   6510  N N   . TYR E  1 179 ? 39.482  -35.097  -4.632  1.000 42.579  0 508 TYR EEE N   1 ? 19 
ATOM   6511  C CA  . TYR E  1 179 ? 38.194  -35.363  -3.980  1.000 39.857  0 508 TYR EEE CA  1 ? 19 
ATOM   6512  C C   . TYR E  1 179 ? 38.480  -36.285  -2.814  1.000 39.693  0 508 TYR EEE C   1 ? 19 
ATOM   6513  O O   . TYR E  1 179 ? 39.235  -37.273  -2.976  1.000 37.914  0 508 TYR EEE O   1 ? 19 
ATOM   6514  C CB  . TYR E  1 179 ? 37.184  -35.948  -4.962  1.000 39.565  0 508 TYR EEE CB  1 ? 19 
ATOM   6515  C CG  . TYR E  1 179 ? 36.504  -34.900  -5.808  1.000 39.616  0 508 TYR EEE CG  1 ? 19 
ATOM   6516  C CD1 . TYR E  1 179 ? 37.200  -34.188  -6.754  1.000 40.582  0 508 TYR EEE CD1 1 ? 19 
ATOM   6517  C CD2 . TYR E  1 179 ? 35.170  -34.616  -5.666  1.000 38.952  0 508 TYR EEE CD2 1 ? 19 
ATOM   6518  C CE1 . TYR E  1 179 ? 36.586  -33.232  -7.544  1.000 42.031  0 508 TYR EEE CE1 1 ? 19 
ATOM   6519  C CE2 . TYR E  1 179 ? 34.537  -33.653  -6.432  1.000 39.932  0 508 TYR EEE CE2 1 ? 19 
ATOM   6520  C CZ  . TYR E  1 179 ? 35.243  -32.953  -7.381  1.000 41.654  0 508 TYR EEE CZ  1 ? 19 
ATOM   6521  O OH  . TYR E  1 179 ? 34.603  -32.003  -8.135  1.000 42.283  0 508 TYR EEE OH  1 ? 19 
ATOM   6522  N N   . ARG E  1 180 ? 37.929  -35.920  -1.658  1.000 41.964  0 509 ARG EEE N   1 ? 19 
ATOM   6523  C CA  . ARG E  1 180 ? 37.891  -36.803  -0.480  1.000 43.383  0 509 ARG EEE CA  1 ? 19 
ATOM   6524  C C   . ARG E  1 180 ? 36.699  -37.742  -0.625  1.000 42.372  0 509 ARG EEE C   1 ? 19 
ATOM   6525  O O   . ARG E  1 180 ? 35.661  -37.301  -1.128  1.000 43.971  0 509 ARG EEE O   1 ? 19 
ATOM   6526  C CB  . ARG E  1 180 ? 37.846  -35.975  0.795   1.000 43.604  0 509 ARG EEE CB  1 ? 19 
ATOM   6527  C CG  . ARG E  1 180 ? 39.170  -35.291  1.057   1.000 43.818  0 509 ARG EEE CG  1 ? 19 
ATOM   6528  C CD  . ARG E  1 180 ? 39.136  -34.437  2.290   1.000 42.637  0 509 ARG EEE CD  1 ? 19 
ATOM   6529  N NE  . ARG E  1 180 ? 40.445  -33.866  2.443   1.000 43.966  0 509 ARG EEE NE  1 ? 19 
ATOM   6530  C CZ  . ARG E  1 180 ? 40.889  -33.274  3.538   1.000 43.893  0 509 ARG EEE CZ  1 ? 19 
ATOM   6531  N NH1 . ARG E  1 180 ? 40.118  -33.181  4.608   1.000 43.289  0 509 ARG EEE NH1 1 ? 19 
ATOM   6532  N NH2 . ARG E  1 180 ? 42.124  -32.807  3.554   1.000 44.055  0 509 ARG EEE NH2 1 ? 19 
ATOM   6533  N N   . VAL E  1 181 ? 36.898  -38.994  -0.227  1.000 41.988  0 510 VAL EEE N   1 ? 19 
ATOM   6534  C CA  . VAL E  1 181 ? 35.891  -40.083  -0.332  1.000 41.926  0 510 VAL EEE CA  1 ? 19 
ATOM   6535  C C   . VAL E  1 181 ? 35.740  -40.720  1.055   1.000 42.671  0 510 VAL EEE C   1 ? 19 
ATOM   6536  O O   . VAL E  1 181 ? 36.769  -40.941  1.742   1.000 40.171  0 510 VAL EEE O   1 ? 19 
ATOM   6537  C CB  . VAL E  1 181 ? 36.315  -41.104  -1.396  1.000 40.861  0 510 VAL EEE CB  1 ? 19 
ATOM   6538  C CG1 . VAL E  1 181 ? 35.244  -42.153  -1.603  1.000 39.624  0 510 VAL EEE CG1 1 ? 19 
ATOM   6539  C CG2 . VAL E  1 181 ? 36.659  -40.413  -2.717  1.000 41.925  0 510 VAL EEE CG2 1 ? 19 
ATOM   6540  N N   . VAL E  1 182 ? 34.491  -40.965  1.456   1.000 40.580  0 511 VAL EEE N   1 ? 19 
ATOM   6541  C CA  . VAL E  1 182 ? 34.145  -41.845  2.595   1.000 40.019  0 511 VAL EEE CA  1 ? 19 
ATOM   6542  C C   . VAL E  1 182 ? 33.230  -42.940  2.058   1.000 38.956  0 511 VAL EEE C   1 ? 19 
ATOM   6543  O O   . VAL E  1 182 ? 32.262  -42.615  1.368   1.000 35.251  0 511 VAL EEE O   1 ? 19 
ATOM   6544  C CB  . VAL E  1 182 ? 33.500  -41.068  3.747   1.000 40.870  0 511 VAL EEE CB  1 ? 19 
ATOM   6545  C CG1 . VAL E  1 182 ? 32.990  -42.007  4.826   1.000 40.367  0 511 VAL EEE CG1 1 ? 19 
ATOM   6546  C CG2 . VAL E  1 182 ? 34.476  -40.058  4.330   1.000 41.045  0 511 VAL EEE CG2 1 ? 19 
ATOM   6547  N N   . VAL E  1 183 ? 33.609  -44.185  2.327   1.000 38.459  0 512 VAL EEE N   1 ? 19 
ATOM   6548  C CA  . VAL E  1 183 ? 32.805  -45.402  2.067   1.000 36.778  0 512 VAL EEE CA  1 ? 19 
ATOM   6549  C C   . VAL E  1 183 ? 32.373  -45.945  3.425   1.000 36.229  0 512 VAL EEE C   1 ? 19 
ATOM   6550  O O   . VAL E  1 183 ? 33.229  -46.259  4.242   1.000 36.842  0 512 VAL EEE O   1 ? 19 
ATOM   6551  C CB  . VAL E  1 183 ? 33.591  -46.442  1.248   1.000 35.980  0 512 VAL EEE CB  1 ? 19 
ATOM   6552  C CG1 . VAL E  1 183 ? 32.747  -47.656  0.934   1.000 36.978  0 512 VAL EEE CG1 1 ? 19 
ATOM   6553  C CG2 . VAL E  1 183 ? 34.143  -45.850  -0.029  1.000 36.330  0 512 VAL EEE CG2 1 ? 19 
ATOM   6554  N N   . LEU E  1 184 ? 31.073  -45.997  3.650   1.000 37.932  0 513 LEU EEE N   1 ? 19 
ATOM   6555  C CA  . LEU E  1 184 ? 30.468  -46.629  4.838   1.000 39.263  0 513 LEU EEE CA  1 ? 19 
ATOM   6556  C C   . LEU E  1 184 ? 30.033  -48.036  4.433   1.000 39.188  0 513 LEU EEE C   1 ? 19 
ATOM   6557  O O   . LEU E  1 184 ? 29.217  -48.149  3.525   1.000 42.128  0 513 LEU EEE O   1 ? 19 
ATOM   6558  C CB  . LEU E  1 184 ? 29.299  -45.769  5.316   1.000 39.445  0 513 LEU EEE CB  1 ? 19 
ATOM   6559  C CG  . LEU E  1 184 ? 29.662  -44.350  5.749   1.000 39.588  0 513 LEU EEE CG  1 ? 19 
ATOM   6560  C CD1 . LEU E  1 184 ? 28.409  -43.579  6.123   1.000 40.727  0 513 LEU EEE CD1 1 ? 19 
ATOM   6561  C CD2 . LEU E  1 184 ? 30.607  -44.334  6.922   1.000 40.067  0 513 LEU EEE CD2 1 ? 19 
ATOM   6562  N N   . SER E  1 185 ? 30.671  -49.050  5.003   1.000 39.826  0 514 SER EEE N   1 ? 19 
ATOM   6563  C CA  . SER E  1 185 ? 30.338  -50.488  4.859   1.000 41.496  0 514 SER EEE CA  1 ? 19 
ATOM   6564  C C   . SER E  1 185 ? 29.411  -50.890  5.997   1.000 41.481  0 514 SER EEE C   1 ? 19 
ATOM   6565  O O   . SER E  1 185 ? 29.776  -50.630  7.150   1.000 39.706  0 514 SER EEE O   1 ? 19 
ATOM   6566  C CB  . SER E  1 185 ? 31.573  -51.306  4.910   1.000 43.197  0 514 SER EEE CB  1 ? 19 
ATOM   6567  O OG  . SER E  1 185 ? 32.090  -51.344  3.621   1.000 46.312  0 514 SER EEE OG  1 ? 19 
ATOM   6568  N N   . PHE E  1 186 ? 28.273  -51.487  5.672   1.000 43.336  0 515 PHE EEE N   1 ? 19 
ATOM   6569  C CA  . PHE E  1 186 ? 27.296  -51.986  6.663   1.000 45.418  0 515 PHE EEE CA  1 ? 19 
ATOM   6570  C C   . PHE E  1 186 ? 27.358  -53.504  6.601   1.000 46.259  0 515 PHE EEE C   1 ? 19 
ATOM   6571  O O   . PHE E  1 186 ? 27.163  -54.079  5.541   1.000 48.289  0 515 PHE EEE O   1 ? 19 
ATOM   6572  C CB  . PHE E  1 186 ? 25.892  -51.465  6.375   1.000 45.903  0 515 PHE EEE CB  1 ? 19 
ATOM   6573  C CG  . PHE E  1 186 ? 25.756  -49.969  6.284   1.000 45.667  0 515 PHE EEE CG  1 ? 19 
ATOM   6574  C CD1 . PHE E  1 186 ? 26.534  -49.125  7.048   1.000 46.155  0 515 PHE EEE CD1 1 ? 19 
ATOM   6575  C CD2 . PHE E  1 186 ? 24.840  -49.408  5.413   1.000 46.547  0 515 PHE EEE CD2 1 ? 19 
ATOM   6576  C CE1 . PHE E  1 186 ? 26.361  -47.744  6.972   1.000 48.350  0 515 PHE EEE CE1 1 ? 19 
ATOM   6577  C CE2 . PHE E  1 186 ? 24.698  -48.035  5.315   1.000 46.858  0 515 PHE EEE CE2 1 ? 19 
ATOM   6578  C CZ  . PHE E  1 186 ? 25.473  -47.198  6.072   1.000 46.811  0 515 PHE EEE CZ  1 ? 19 
ATOM   6579  N N   . GLU E  1 187 ? 27.635  -54.121  7.741   1.000 48.913  0 516 GLU EEE N   1 ? 19 
ATOM   6580  C CA  . GLU E  1 187 ? 27.567  -55.588  7.933   1.000 49.974  0 516 GLU EEE CA  1 ? 19 
ATOM   6581  C C   . GLU E  1 187 ? 26.262  -55.970  8.643   1.000 50.425  0 516 GLU EEE C   1 ? 19 
ATOM   6582  O O   . GLU E  1 187 ? 25.880  -55.298  9.614   1.000 49.864  0 516 GLU EEE O   1 ? 19 
ATOM   6583  C CB  . GLU E  1 187 ? 28.758  -56.039  8.757   1.000 52.813  0 516 GLU EEE CB  1 ? 19 
ATOM   6584  C CG  . GLU E  1 187 ? 29.954  -56.470  7.956   1.000 55.198  0 516 GLU EEE CG  1 ? 19 
ATOM   6585  C CD  . GLU E  1 187 ? 31.123  -56.984  8.798   1.000 60.272  0 516 GLU EEE CD  1 ? 19 
ATOM   6586  O OE1 . GLU E  1 187 ? 30.993  -57.269  10.057  1.000 59.648  0 516 GLU EEE OE1 1 ? 19 
ATOM   6587  O OE2 . GLU E  1 187 ? 32.197  -57.061  8.187   1.000 67.976  0 516 GLU EEE OE2 1 ? 19 
ATOM   6588  N N   . LEU E  1 188 ? 25.616  -57.031  8.178   1.000 49.737  0 517 LEU EEE N   1 ? 19 
ATOM   6589  C CA  . LEU E  1 188 ? 24.427  -57.652  8.796   1.000 50.385  0 517 LEU EEE CA  1 ? 19 
ATOM   6590  C C   . LEU E  1 188 ? 24.684  -59.154  8.992   1.000 50.399  0 517 LEU EEE C   1 ? 19 
ATOM   6591  O O   . LEU E  1 188 ? 24.038  -59.978  8.309   1.000 52.504  0 517 LEU EEE O   1 ? 19 
ATOM   6592  C CB  . LEU E  1 188 ? 23.233  -57.415  7.864   1.000 52.031  0 517 LEU EEE CB  1 ? 19 
ATOM   6593  C CG  . LEU E  1 188 ? 22.624  -56.014  7.912   1.000 51.920  0 517 LEU EEE CG  1 ? 19 
ATOM   6594  C CD1 . LEU E  1 188 ? 21.733  -55.727  6.707   1.000 51.017  0 517 LEU EEE CD1 1 ? 19 
ATOM   6595  C CD2 . LEU E  1 188 ? 21.911  -55.802  9.246   1.000 52.482  0 517 LEU EEE CD2 1 ? 19 
ATOM   6596  N N   . LEU E  1 189 ? 25.513  -59.544  9.958   1.000 49.661  0 518 LEU EEE N   1 ? 19 
ATOM   6597  C CA  . LEU E  1 189 ? 25.860  -60.957  10.248  1.000 48.693  0 518 LEU EEE CA  1 ? 19 
ATOM   6598  C C   . LEU E  1 189 ? 24.952  -61.510  11.348  1.000 51.102  0 518 LEU EEE C   1 ? 19 
ATOM   6599  O O   . LEU E  1 189 ? 24.098  -60.771  11.821  1.000 51.264  0 518 LEU EEE O   1 ? 19 
ATOM   6600  C CB  . LEU E  1 189 ? 27.313  -60.998  10.695  1.000 47.208  0 518 LEU EEE CB  1 ? 19 
ATOM   6601  C CG  . LEU E  1 189 ? 28.325  -60.372  9.743   1.000 45.883  0 518 LEU EEE CG  1 ? 19 
ATOM   6602  C CD1 . LEU E  1 189 ? 29.745  -60.567  10.300  1.000 46.000  0 518 LEU EEE CD1 1 ? 19 
ATOM   6603  C CD2 . LEU E  1 189 ? 28.212  -60.937  8.344   1.000 44.573  0 518 LEU EEE CD2 1 ? 19 
ATOM   6604  N N   . HIS E  1 190 ? 25.139  -62.772  11.721  1.000 52.370  0 519 HIS EEE N   1 ? 19 
ATOM   6605  C CA  . HIS E  1 190 ? 24.411  -63.442  12.815  1.000 55.631  0 519 HIS EEE CA  1 ? 19 
ATOM   6606  C C   . HIS E  1 190 ? 25.098  -63.096  14.132  1.000 58.245  0 519 HIS EEE C   1 ? 19 
ATOM   6607  O O   . HIS E  1 190 ? 25.735  -63.985  14.697  1.000 60.620  0 519 HIS EEE O   1 ? 19 
ATOM   6608  C CB  . HIS E  1 190 ? 24.370  -64.921  12.476  1.000 55.989  0 519 HIS EEE CB  1 ? 19 
ATOM   6609  C CG  . HIS E  1 190 ? 23.738  -65.099  11.139  1.000 55.150  0 519 HIS EEE CG  1 ? 19 
ATOM   6610  N ND1 . HIS E  1 190 ? 22.429  -64.731  10.925  1.000 55.265  0 519 HIS EEE ND1 1 ? 19 
ATOM   6611  C CD2 . HIS E  1 190 ? 24.206  -65.555  9.954   1.000 53.169  0 519 HIS EEE CD2 1 ? 19 
ATOM   6612  C CE1 . HIS E  1 190 ? 22.099  -64.976  9.671   1.000 54.324  0 519 HIS EEE CE1 1 ? 19 
ATOM   6613  N NE2 . HIS E  1 190 ? 23.176  -65.464  9.055   1.000 53.026  0 519 HIS EEE NE2 1 ? 19 
ATOM   6614  N N   . ALA E  1 191 ? 24.981  -61.843  14.559  1.000 59.292  0 520 ALA EEE N   1 ? 19 
ATOM   6615  C CA  . ALA E  1 191 ? 25.699  -61.232  15.701  1.000 60.988  0 520 ALA EEE CA  1 ? 19 
ATOM   6616  C C   . ALA E  1 191 ? 24.865  -60.083  16.254  1.000 61.967  0 520 ALA EEE C   1 ? 19 
ATOM   6617  O O   . ALA E  1 191 ? 23.999  -59.567  15.564  1.000 64.323  0 520 ALA EEE O   1 ? 19 
ATOM   6618  C CB  . ALA E  1 191 ? 27.067  -60.759  15.282  1.000 59.090  0 520 ALA EEE CB  1 ? 19 
ATOM   6619  N N   . PRO E  1 192 ? 25.031  -59.683  17.533  1.000 62.787  0 521 PRO EEE N   1 ? 19 
ATOM   6620  C CA  . PRO E  1 192 ? 24.321  -58.506  18.032  1.000 62.145  0 521 PRO EEE CA  1 ? 19 
ATOM   6621  C C   . PRO E  1 192 ? 24.636  -57.252  17.199  1.000 58.005  0 521 PRO EEE C   1 ? 19 
ATOM   6622  O O   . PRO E  1 192 ? 25.749  -57.082  16.770  1.000 56.703  0 521 PRO EEE O   1 ? 19 
ATOM   6623  C CB  . PRO E  1 192 ? 24.823  -58.392  19.478  1.000 63.919  0 521 PRO EEE CB  1 ? 19 
ATOM   6624  C CG  . PRO E  1 192 ? 25.183  -59.817  19.840  1.000 65.938  0 521 PRO EEE CG  1 ? 19 
ATOM   6625  C CD  . PRO E  1 192 ? 25.820  -60.361  18.577  1.000 64.455  0 521 PRO EEE CD  1 ? 19 
ATOM   6626  N N   . ALA E  1 193 ? 23.625  -56.427  16.982  1.000 57.344  0 522 ALA EEE N   1 ? 19 
ATOM   6627  C CA  . ALA E  1 193 ? 23.752  -55.081  16.401  1.000 57.555  0 522 ALA EEE CA  1 ? 19 
ATOM   6628  C C   . ALA E  1 193 ? 24.608  -54.220  17.326  1.000 59.938  0 522 ALA EEE C   1 ? 19 
ATOM   6629  O O   . ALA E  1 193 ? 24.394  -54.281  18.523  1.000 62.984  0 522 ALA EEE O   1 ? 19 
ATOM   6630  C CB  . ALA E  1 193 ? 22.396  -54.461  16.194  1.000 56.404  0 522 ALA EEE CB  1 ? 19 
ATOM   6631  N N   . THR E  1 194 ? 25.550  -53.458  16.791  1.000 60.470  0 523 THR EEE N   1 ? 19 
ATOM   6632  C CA  . THR E  1 194 ? 26.369  -52.520  17.602  1.000 61.881  0 523 THR EEE CA  1 ? 19 
ATOM   6633  C C   . THR E  1 194 ? 26.092  -51.089  17.129  1.000 61.670  0 523 THR EEE C   1 ? 19 
ATOM   6634  O O   . THR E  1 194 ? 26.411  -50.162  17.905  1.000 67.842  0 523 THR EEE O   1 ? 19 
ATOM   6635  C CB  . THR E  1 194 ? 27.855  -52.904  17.582  1.000 60.640  0 523 THR EEE CB  1 ? 19 
ATOM   6636  O OG1 . THR E  1 194 ? 28.414  -52.592  16.302  1.000 57.635  0 523 THR EEE OG1 1 ? 19 
ATOM   6637  C CG2 . THR E  1 194 ? 28.076  -54.383  17.846  1.000 61.381  0 523 THR EEE CG2 1 ? 19 
ATOM   6638  N N   . VAL E  1 195 ? 25.537  -50.887  15.928  1.000 58.372  0 524 VAL EEE N   1 ? 19 
ATOM   6639  C CA  . VAL E  1 195 ? 25.239  -49.513  15.432  1.000 57.252  0 524 VAL EEE CA  1 ? 19 
ATOM   6640  C C   . VAL E  1 195 ? 23.768  -49.429  15.070  1.000 55.918  0 524 VAL EEE C   1 ? 19 
ATOM   6641  O O   . VAL E  1 195 ? 23.374  -50.196  14.189  1.000 56.598  0 524 VAL EEE O   1 ? 19 
ATOM   6642  C CB  . VAL E  1 195 ? 26.102  -49.138  14.218  1.000 56.060  0 524 VAL EEE CB  1 ? 19 
ATOM   6643  C CG1 . VAL E  1 195 ? 25.719  -47.804  13.611  1.000 55.169  0 524 VAL EEE CG1 1 ? 19 
ATOM   6644  C CG2 . VAL E  1 195 ? 27.554  -49.121  14.590  1.000 57.511  0 524 VAL EEE CG2 1 ? 19 
ATOM   6645  N N   . CYS E  1 196 ? 23.012  -48.506  15.676  1.000 56.932  0 525 CYS EEE N   1 ? 19 
ATOM   6646  C CA  . CYS E  1 196 ? 21.603  -48.202  15.318  1.000 57.812  0 525 CYS EEE CA  1 ? 19 
ATOM   6647  C C   . CYS E  1 196 ? 21.422  -46.704  15.080  1.000 55.629  0 525 CYS EEE C   1 ? 19 
ATOM   6648  O O   . CYS E  1 196 ? 22.185  -45.917  15.604  1.000 54.477  0 525 CYS EEE O   1 ? 19 
ATOM   6649  C CB  . CYS E  1 196 ? 20.658  -48.669  16.416  1.000 61.353  0 525 CYS EEE CB  1 ? 19 
ATOM   6650  S SG  . CYS E  1 196 ? 20.591  -50.473  16.568  1.000 65.434  0 525 CYS EEE SG  1 ? 19 
ATOM   6651  N N   . GLY E  1 197 ? 20.454  -46.331  14.264  1.000 57.190  0 526 GLY EEE N   1 ? 19 
ATOM   6652  C CA  . GLY E  1 197 ? 20.037  -44.927  14.092  1.000 59.438  0 526 GLY EEE CA  1 ? 19 
ATOM   6653  C C   . GLY E  1 197 ? 19.226  -44.487  15.302  1.000 64.094  0 526 GLY EEE C   1 ? 19 
ATOM   6654  O O   . GLY E  1 197 ? 18.901  -45.288  16.173  1.000 65.904  0 526 GLY EEE O   1 ? 19 
ATOM   6655  N N   . PRO E  1 198 ? 18.910  -43.180  15.409  1.000 69.836  0 527 PRO EEE N   1 ? 19 
ATOM   6656  C CA  . PRO E  1 198 ? 18.099  -42.651  16.505  1.000 75.103  0 527 PRO EEE CA  1 ? 19 
ATOM   6657  C C   . PRO E  1 198 ? 16.742  -43.329  16.717  1.000 84.040  0 527 PRO EEE C   1 ? 19 
ATOM   6658  O O   . PRO E  1 198 ? 16.250  -43.275  17.846  1.000 86.202  0 527 PRO EEE O   1 ? 19 
ATOM   6659  C CB  . PRO E  1 198 ? 17.844  -41.210  16.054  1.000 73.476  0 527 PRO EEE CB  1 ? 19 
ATOM   6660  C CG  . PRO E  1 198 ? 19.081  -40.847  15.262  1.000 69.372  0 527 PRO EEE CG  1 ? 19 
ATOM   6661  C CD  . PRO E  1 198 ? 19.437  -42.121  14.540  1.000 67.755  0 527 PRO EEE CD  1 ? 19 
ATOM   6662  N N   . LYS E  1 199 ? 16.175  -43.933  15.659  1.000 66.245  0 528 LYS EEE N   1 ? ?  
ATOM   6663  C CA  . LYS E  1 199 ? 14.884  -44.689  15.691  1.000 76.485  0 528 LYS EEE CA  1 ? ?  
ATOM   6664  C C   . LYS E  1 199 ? 14.969  -45.879  14.729  1.000 76.517  0 528 LYS EEE C   1 ? ?  
ATOM   6665  O O   . LYS E  1 199 ? 14.845  -47.010  15.183  1.000 77.679  0 528 LYS EEE O   1 ? ?  
ATOM   6666  C CB  . LYS E  1 199 ? 13.688  -43.794  15.343  1.000 81.778  0 528 LYS EEE CB  1 ? ?  
ATOM   6667  C CG  . LYS E  1 199 ? 13.148  -42.965  16.504  1.000 87.099  0 528 LYS EEE CG  1 ? ?  
ATOM   6668  C CD  . LYS E  1 199 ? 12.261  -41.813  16.086  1.000 89.573  0 528 LYS EEE CD  1 ? ?  
ATOM   6669  C CE  . LYS E  1 199 ? 12.628  -40.513  16.776  1.000 92.867  0 528 LYS EEE CE  1 ? ?  
ATOM   6670  N NZ  . LYS E  1 199 ? 11.769  -39.391  16.327  1.000 94.865  0 528 LYS EEE NZ  1 ? ?  
ATOM   6671  N N   . GLN F  2 1   ? 28.179  -52.140  -19.237 1.000 73.583  0 1   GLN FFF N   1 ? 20 
ATOM   6672  C CA  . GLN F  2 1   ? 27.362  -51.326  -20.147 1.000 68.564  0 1   GLN FFF CA  1 ? 20 
ATOM   6673  C C   . GLN F  2 1   ? 25.925  -51.868  -20.136 1.000 61.320  0 1   GLN FFF C   1 ? 20 
ATOM   6674  O O   . GLN F  2 1   ? 25.706  -53.007  -20.481 1.000 60.086  0 1   GLN FFF O   1 ? 20 
ATOM   6675  C CB  . GLN F  2 1   ? 28.018  -51.283  -21.534 1.000 72.027  0 1   GLN FFF CB  1 ? 20 
ATOM   6676  C CG  . GLN F  2 1   ? 27.228  -50.536  -22.622 1.000 76.338  0 1   GLN FFF CG  1 ? 20 
ATOM   6677  C CD  . GLN F  2 1   ? 26.911  -49.056  -22.444 1.000 82.139  0 1   GLN FFF CD  1 ? 20 
ATOM   6678  O OE1 . GLN F  2 1   ? 27.417  -48.368  -21.546 1.000 87.878  0 1   GLN FFF OE1 1 ? 20 
ATOM   6679  N NE2 . GLN F  2 1   ? 26.051  -48.549  -23.325 1.000 81.662  0 1   GLN FFF NE2 1 ? 20 
ATOM   6680  N N   . VAL F  2 2   ? 24.975  -51.016  -19.778 1.000 57.833  0 2   VAL FFF N   1 ? 20 
ATOM   6681  C CA  . VAL F  2 2   ? 23.513  -51.245  -19.903 1.000 52.697  0 2   VAL FFF CA  1 ? 20 
ATOM   6682  C C   . VAL F  2 2   ? 22.975  -50.344  -21.017 1.000 48.476  0 2   VAL FFF C   1 ? 20 
ATOM   6683  O O   . VAL F  2 2   ? 23.245  -49.150  -21.000 1.000 49.742  0 2   VAL FFF O   1 ? 20 
ATOM   6684  C CB  . VAL F  2 2   ? 22.789  -50.941  -18.576 1.000 51.895  0 2   VAL FFF CB  1 ? 20 
ATOM   6685  C CG1 . VAL F  2 2   ? 21.293  -51.126  -18.711 1.000 48.920  0 2   VAL FFF CG1 1 ? 20 
ATOM   6686  C CG2 . VAL F  2 2   ? 23.308  -51.786  -17.438 1.000 54.121  0 2   VAL FFF CG2 1 ? 20 
ATOM   6687  N N   . GLN F  2 3   ? 22.166  -50.889  -21.908 1.000 43.970  0 3   GLN FFF N   1 ? 20 
ATOM   6688  C CA  . GLN F  2 3   ? 21.412  -50.080  -22.893 1.000 41.787  0 3   GLN FFF CA  1 ? 20 
ATOM   6689  C C   . GLN F  2 3   ? 19.976  -49.927  -22.397 1.000 39.730  0 3   GLN FFF C   1 ? 20 
ATOM   6690  O O   . GLN F  2 3   ? 19.467  -50.868  -21.740 1.000 39.130  0 3   GLN FFF O   1 ? 20 
ATOM   6691  C CB  . GLN F  2 3   ? 21.567  -50.674  -24.293 1.000 40.293  0 3   GLN FFF CB  1 ? 20 
ATOM   6692  C CG  . GLN F  2 3   ? 22.964  -50.438  -24.855 1.000 42.600  0 3   GLN FFF CG  1 ? 20 
ATOM   6693  C CD  . GLN F  2 3   ? 23.030  -50.775  -26.322 1.000 42.574  0 3   GLN FFF CD  1 ? 20 
ATOM   6694  O OE1 . GLN F  2 3   ? 22.350  -50.144  -27.130 1.000 40.693  0 3   GLN FFF OE1 1 ? 20 
ATOM   6695  N NE2 . GLN F  2 3   ? 23.840  -51.765  -26.678 1.000 42.500  0 3   GLN FFF NE2 1 ? 20 
ATOM   6696  N N   . LEU F  2 4   ? 19.389  -48.771  -22.683 1.000 38.911  0 4   LEU FFF N   1 ? 20 
ATOM   6697  C CA  . LEU F  2 4   ? 18.021  -48.403  -22.256 1.000 39.024  0 4   LEU FFF CA  1 ? 20 
ATOM   6698  C C   . LEU F  2 4   ? 17.250  -47.858  -23.468 1.000 38.806  0 4   LEU FFF C   1 ? 20 
ATOM   6699  O O   . LEU F  2 4   ? 17.775  -46.978  -24.173 1.000 40.298  0 4   LEU FFF O   1 ? 20 
ATOM   6700  C CB  . LEU F  2 4   ? 18.121  -47.339  -21.161 1.000 39.158  0 4   LEU FFF CB  1 ? 20 
ATOM   6701  C CG  . LEU F  2 4   ? 18.920  -47.684  -19.903 1.000 40.769  0 4   LEU FFF CG  1 ? 20 
ATOM   6702  C CD1 . LEU F  2 4   ? 19.077  -46.423  -19.020 1.000 41.845  0 4   LEU FFF CD1 1 ? 20 
ATOM   6703  C CD2 . LEU F  2 4   ? 18.228  -48.787  -19.114 1.000 40.214  0 4   LEU FFF CD2 1 ? 20 
ATOM   6704  N N   . VAL F  2 5   ? 16.058  -48.373  -23.717 1.000 38.230  0 5   VAL FFF N   1 ? 20 
ATOM   6705  C CA  . VAL F  2 5   ? 15.192  -47.905  -24.831 1.000 38.800  0 5   VAL FFF CA  1 ? 20 
ATOM   6706  C C   . VAL F  2 5   ? 13.801  -47.574  -24.283 1.000 40.013  0 5   VAL FFF C   1 ? 20 
ATOM   6707  O O   . VAL F  2 5   ? 13.097  -48.500  -23.785 1.000 40.232  0 5   VAL FFF O   1 ? 20 
ATOM   6708  C CB  . VAL F  2 5   ? 15.145  -48.943  -25.963 1.000 37.570  0 5   VAL FFF CB  1 ? 20 
ATOM   6709  C CG1 . VAL F  2 5   ? 14.132  -48.544  -27.027 1.000 37.438  0 5   VAL FFF CG1 1 ? 20 
ATOM   6710  C CG2 . VAL F  2 5   ? 16.526  -49.150  -26.572 1.000 38.064  0 5   VAL FFF CG2 1 ? 20 
ATOM   6711  N N   . GLU F  2 6   ? 13.429  -46.298  -24.393 1.000 40.944  0 6   GLU FFF N   1 ? 20 
ATOM   6712  C CA  . GLU F  2 6   ? 12.080  -45.763  -24.097 1.000 40.667  0 6   GLU FFF CA  1 ? 20 
ATOM   6713  C C   . GLU F  2 6   ? 11.133  -46.093  -25.253 1.000 40.644  0 6   GLU FFF C   1 ? 20 
ATOM   6714  O O   . GLU F  2 6   ? 11.593  -46.143  -26.400 1.000 41.424  0 6   GLU FFF O   1 ? 20 
ATOM   6715  C CB  . GLU F  2 6   ? 12.126  -44.242  -23.930 1.000 42.437  0 6   GLU FFF CB  1 ? 20 
ATOM   6716  C CG  . GLU F  2 6   ? 13.168  -43.767  -22.938 1.000 42.683  0 6   GLU FFF CG  1 ? 20 
ATOM   6717  C CD  . GLU F  2 6   ? 14.531  -43.441  -23.508 1.000 43.673  0 6   GLU FFF CD  1 ? 20 
ATOM   6718  O OE1 . GLU F  2 6   ? 14.843  -43.911  -24.625 1.000 42.986  0 6   GLU FFF OE1 1 ? 20 
ATOM   6719  O OE2 . GLU F  2 6   ? 15.296  -42.728  -22.812 1.000 45.867  0 6   GLU FFF OE2 1 ? 20 
ATOM   6720  N N   . SER F  2 7   ? 9.851   -46.296  -24.938 1.000 40.303  0 7   SER FFF N   1 ? 20 
ATOM   6721  C CA  . SER F  2 7   ? 8.727   -46.346  -25.905 1.000 40.722  0 7   SER FFF CA  1 ? 20 
ATOM   6722  C C   . SER F  2 7   ? 7.456   -45.802  -25.231 1.000 41.798  0 7   SER FFF C   1 ? 20 
ATOM   6723  O O   . SER F  2 7   ? 7.485   -45.537  -24.011 1.000 37.122  0 7   SER FFF O   1 ? 20 
ATOM   6724  C CB  . SER F  2 7   ? 8.532   -47.746  -26.398 1.000 41.374  0 7   SER FFF CB  1 ? 20 
ATOM   6725  O OG  . SER F  2 7   ? 8.259   -48.592  -25.297 1.000 44.088  0 7   SER FFF OG  1 ? 20 
ATOM   6726  N N   . GLY F  2 8   ? 6.376   -45.630  -26.006 1.000 45.615  0 8   GLY FFF N   1 ? 20 
ATOM   6727  C CA  . GLY F  2 8   ? 5.058   -45.209  -25.493 1.000 49.006  0 8   GLY FFF CA  1 ? 20 
ATOM   6728  C C   . GLY F  2 8   ? 4.859   -43.696  -25.541 1.000 51.285  0 8   GLY FFF C   1 ? 20 
ATOM   6729  O O   . GLY F  2 8   ? 3.812   -43.238  -25.080 1.000 56.454  0 8   GLY FFF O   1 ? 20 
ATOM   6730  N N   . GLY F  2 9   ? 5.809   -42.943  -26.089 1.000 50.764  0 9   GLY FFF N   1 ? 20 
ATOM   6731  C CA  . GLY F  2 9   ? 5.672   -41.479  -26.230 1.000 53.858  0 9   GLY FFF CA  1 ? 20 
ATOM   6732  C C   . GLY F  2 9   ? 4.796   -41.133  -27.426 1.000 54.071  0 9   GLY FFF C   1 ? 20 
ATOM   6733  O O   . GLY F  2 9   ? 4.221   -42.048  -28.018 1.000 57.755  0 9   GLY FFF O   1 ? 20 
ATOM   6734  N N   . GLY F  2 10  ? 4.706   -39.850  -27.776 1.000 53.782  0 10  GLY FFF N   1 ? 20 
ATOM   6735  C CA  . GLY F  2 10  ? 3.918   -39.367  -28.915 1.000 56.566  0 10  GLY FFF CA  1 ? 20 
ATOM   6736  C C   . GLY F  2 10  ? 2.978   -38.238  -28.520 1.000 59.298  0 10  GLY FFF C   1 ? 20 
ATOM   6737  O O   . GLY F  2 10  ? 3.163   -37.625  -27.436 1.000 57.891  0 10  GLY FFF O   1 ? 20 
ATOM   6738  N N   . LEU F  2 11  ? 2.015   -37.954  -29.396 1.000 63.803  0 11  LEU FFF N   1 ? 20 
ATOM   6739  C CA  . LEU F  2 11  ? 1.049   -36.831  -29.282 1.000 66.546  0 11  LEU FFF CA  1 ? 20 
ATOM   6740  C C   . LEU F  2 11  ? -0.117  -37.275  -28.385 1.000 66.623  0 11  LEU FFF C   1 ? 20 
ATOM   6741  O O   . LEU F  2 11  ? -0.546  -38.410  -28.510 1.000 67.786  0 11  LEU FFF O   1 ? 20 
ATOM   6742  C CB  . LEU F  2 11  ? 0.590   -36.482  -30.701 1.000 70.387  0 11  LEU FFF CB  1 ? 20 
ATOM   6743  C CG  . LEU F  2 11  ? -0.393  -35.320  -30.837 1.000 75.609  0 11  LEU FFF CG  1 ? 20 
ATOM   6744  C CD1 . LEU F  2 11  ? 0.103   -34.077  -30.109 1.000 74.027  0 11  LEU FFF CD1 1 ? 20 
ATOM   6745  C CD2 . LEU F  2 11  ? -0.665  -35.014  -32.310 1.000 80.064  0 11  LEU FFF CD2 1 ? 20 
ATOM   6746  N N   . VAL F  2 12  ? -0.605  -36.421  -27.495 1.000 65.869  0 12  VAL FFF N   1 ? 20 
ATOM   6747  C CA  . VAL F  2 12  ? -1.798  -36.718  -26.656 1.000 67.287  0 12  VAL FFF CA  1 ? 20 
ATOM   6748  C C   . VAL F  2 12  ? -2.461  -35.385  -26.308 1.000 70.079  0 12  VAL FFF C   1 ? 20 
ATOM   6749  O O   . VAL F  2 12  ? -1.731  -34.370  -26.215 1.000 68.885  0 12  VAL FFF O   1 ? 20 
ATOM   6750  C CB  . VAL F  2 12  ? -1.411  -37.542  -25.414 1.000 68.026  0 12  VAL FFF CB  1 ? 20 
ATOM   6751  C CG1 . VAL F  2 12  ? -0.587  -36.718  -24.419 1.000 68.660  0 12  VAL FFF CG1 1 ? 20 
ATOM   6752  C CG2 . VAL F  2 12  ? -2.626  -38.160  -24.717 1.000 69.618  0 12  VAL FFF CG2 1 ? 20 
ATOM   6753  N N   . GLN F  2 13  ? -3.795  -35.378  -26.174 1.000 73.926  0 13  GLN FFF N   1 ? 20 
ATOM   6754  C CA  . GLN F  2 13  ? -4.577  -34.176  -25.808 1.000 76.533  0 13  GLN FFF CA  1 ? 20 
ATOM   6755  C C   . GLN F  2 13  ? -4.435  -33.916  -24.302 1.000 71.638  0 13  GLN FFF C   1 ? 20 
ATOM   6756  O O   . GLN F  2 13  ? -4.333  -34.900  -23.527 1.000 69.746  0 13  GLN FFF O   1 ? 20 
ATOM   6757  C CB  . GLN F  2 13  ? -6.026  -34.362  -26.255 1.000 83.728  0 13  GLN FFF CB  1 ? 20 
ATOM   6758  C CG  . GLN F  2 13  ? -6.190  -34.161  -27.752 1.000 89.933  0 13  GLN FFF CG  1 ? 20 
ATOM   6759  C CD  . GLN F  2 13  ? -6.603  -32.743  -28.089 1.000 97.912  0 13  GLN FFF CD  1 ? 20 
ATOM   6760  O OE1 . GLN F  2 13  ? -5.801  -31.805  -27.997 1.000 101.404 0 13  GLN FFF OE1 1 ? 20 
ATOM   6761  N NE2 . GLN F  2 13  ? -7.869  -32.561  -28.470 1.000 103.644 0 13  GLN FFF NE2 1 ? 20 
ATOM   6762  N N   . ALA F  2 14  ? -4.392  -32.635  -23.918 1.000 69.325  0 14  ALA FFF N   1 ? 20 
ATOM   6763  C CA  . ALA F  2 14  ? -4.419  -32.161  -22.512 1.000 67.327  0 14  ALA FFF CA  1 ? 20 
ATOM   6764  C C   . ALA F  2 14  ? -5.519  -32.903  -21.755 1.000 66.546  0 14  ALA FFF C   1 ? 20 
ATOM   6765  O O   . ALA F  2 14  ? -6.574  -33.154  -22.350 1.000 69.752  0 14  ALA FFF O   1 ? 20 
ATOM   6766  C CB  . ALA F  2 14  ? -4.625  -30.669  -22.470 1.000 68.708  0 14  ALA FFF CB  1 ? 20 
ATOM   6767  N N   . GLY F  2 15  ? -5.258  -33.281  -20.505 1.000 64.461  0 15  GLY FFF N   1 ? 20 
ATOM   6768  C CA  . GLY F  2 15  ? -6.159  -34.117  -19.689 1.000 64.732  0 15  GLY FFF CA  1 ? 20 
ATOM   6769  C C   . GLY F  2 15  ? -6.042  -35.592  -20.023 1.000 64.140  0 15  GLY FFF C   1 ? 20 
ATOM   6770  O O   . GLY F  2 15  ? -6.594  -36.380  -19.268 1.000 65.284  0 15  GLY FFF O   1 ? 20 
ATOM   6771  N N   . GLY F  2 16  ? -5.352  -35.970  -21.110 1.000 63.250  0 16  GLY FFF N   1 ? 20 
ATOM   6772  C CA  . GLY F  2 16  ? -5.169  -37.368  -21.541 1.000 62.099  0 16  GLY FFF CA  1 ? 20 
ATOM   6773  C C   . GLY F  2 16  ? -4.110  -38.074  -20.710 1.000 59.937  0 16  GLY FFF C   1 ? 20 
ATOM   6774  O O   . GLY F  2 16  ? -3.553  -37.455  -19.753 1.000 56.545  0 16  GLY FFF O   1 ? 20 
ATOM   6775  N N   . SER F  2 17  ? -3.837  -39.328  -21.076 1.000 62.730  0 17  SER FFF N   1 ? 20 
ATOM   6776  C CA  . SER F  2 17  ? -2.874  -40.247  -20.407 1.000 62.904  0 17  SER FFF CA  1 ? 20 
ATOM   6777  C C   . SER F  2 17  ? -1.900  -40.845  -21.416 1.000 63.349  0 17  SER FFF C   1 ? 20 
ATOM   6778  O O   . SER F  2 17  ? -2.242  -40.967  -22.614 1.000 67.619  0 17  SER FFF O   1 ? 20 
ATOM   6779  C CB  . SER F  2 17  ? -3.568  -41.353  -19.692 1.000 64.762  0 17  SER FFF CB  1 ? 20 
ATOM   6780  O OG  . SER F  2 17  ? -4.197  -40.843  -18.533 1.000 70.272  0 17  SER FFF OG  1 ? 20 
ATOM   6781  N N   . LEU F  2 18  ? -0.734  -41.226  -20.904 1.000 61.788  0 18  LEU FFF N   1 ? 20 
ATOM   6782  C CA  . LEU F  2 18  ? 0.325   -41.973  -21.612 1.000 59.243  0 18  LEU FFF CA  1 ? 20 
ATOM   6783  C C   . LEU F  2 18  ? 1.036   -42.830  -20.579 1.000 56.153  0 18  LEU FFF C   1 ? 20 
ATOM   6784  O O   . LEU F  2 18  ? 1.289   -42.336  -19.481 1.000 55.479  0 18  LEU FFF O   1 ? 20 
ATOM   6785  C CB  . LEU F  2 18  ? 1.335   -40.998  -22.214 1.000 60.487  0 18  LEU FFF CB  1 ? 20 
ATOM   6786  C CG  . LEU F  2 18  ? 1.099   -40.561  -23.652 1.000 63.242  0 18  LEU FFF CG  1 ? 20 
ATOM   6787  C CD1 . LEU F  2 18  ? 2.322   -39.798  -24.141 1.000 65.912  0 18  LEU FFF CD1 1 ? 20 
ATOM   6788  C CD2 . LEU F  2 18  ? 0.779   -41.743  -24.554 1.000 63.004  0 18  LEU FFF CD2 1 ? 20 
ATOM   6789  N N   . ARG F  2 19  ? 1.376   -44.053  -20.950 1.000 55.313  0 19  ARG FFF N   1 ? 20 
ATOM   6790  C CA  . ARG F  2 19  ? 2.333   -44.889  -20.210 1.000 53.803  0 19  ARG FFF CA  1 ? 20 
ATOM   6791  C C   . ARG F  2 19  ? 3.622   -45.004  -21.026 1.000 52.351  0 19  ARG FFF C   1 ? 20 
ATOM   6792  O O   . ARG F  2 19  ? 3.640   -45.726  -22.058 1.000 53.129  0 19  ARG FFF O   1 ? 20 
ATOM   6793  C CB  . ARG F  2 19  ? 1.730   -46.246  -19.881 1.000 56.924  0 19  ARG FFF CB  1 ? 20 
ATOM   6794  C CG  . ARG F  2 19  ? 2.452   -46.894  -18.710 1.000 60.238  0 19  ARG FFF CG  1 ? 20 
ATOM   6795  C CD  . ARG F  2 19  ? 1.948   -48.251  -18.329 1.000 63.471  0 19  ARG FFF CD  1 ? 20 
ATOM   6796  N NE  . ARG F  2 19  ? 2.209   -49.121  -19.456 1.000 64.903  0 19  ARG FFF NE  1 ? 20 
ATOM   6797  C CZ  . ARG F  2 19  ? 2.246   -50.445  -19.403 1.000 68.545  0 19  ARG FFF CZ  1 ? 20 
ATOM   6798  N NH1 . ARG F  2 19  ? 2.064   -51.071  -18.244 1.000 71.131  0 19  ARG FFF NH1 1 ? 20 
ATOM   6799  N NH2 . ARG F  2 19  ? 2.481   -51.122  -20.519 1.000 67.767  0 19  ARG FFF NH2 1 ? 20 
ATOM   6800  N N   . LEU F  2 20  ? 4.657   -44.295  -20.579 1.000 48.784  0 20  LEU FFF N   1 ? 20 
ATOM   6801  C CA  . LEU F  2 20  ? 6.041   -44.502  -21.052 1.000 46.522  0 20  LEU FFF CA  1 ? 20 
ATOM   6802  C C   . LEU F  2 20  ? 6.546   -45.818  -20.467 1.000 47.208  0 20  LEU FFF C   1 ? 20 
ATOM   6803  O O   . LEU F  2 20  ? 6.205   -46.146  -19.299 1.000 44.959  0 20  LEU FFF O   1 ? 20 
ATOM   6804  C CB  . LEU F  2 20  ? 6.921   -43.330  -20.625 1.000 45.145  0 20  LEU FFF CB  1 ? 20 
ATOM   6805  C CG  . LEU F  2 20  ? 6.525   -41.966  -21.174 1.000 47.442  0 20  LEU FFF CG  1 ? 20 
ATOM   6806  C CD1 . LEU F  2 20  ? 7.586   -40.942  -20.910 1.000 46.633  0 20  LEU FFF CD1 1 ? 20 
ATOM   6807  C CD2 . LEU F  2 20  ? 6.246   -42.021  -22.668 1.000 50.766  0 20  LEU FFF CD2 1 ? 20 
ATOM   6808  N N   . ALA F  2 21  ? 7.302   -46.566  -21.270 1.000 46.098  0 21  ALA FFF N   1 ? 20 
ATOM   6809  C CA  . ALA F  2 21  ? 8.048   -47.745  -20.792 1.000 46.091  0 21  ALA FFF CA  1 ? 20 
ATOM   6810  C C   . ALA F  2 21  ? 9.508   -47.609  -21.198 1.000 45.725  0 21  ALA FFF C   1 ? 20 
ATOM   6811  O O   . ALA F  2 21  ? 9.809   -46.943  -22.209 1.000 47.129  0 21  ALA FFF O   1 ? 20 
ATOM   6812  C CB  . ALA F  2 21  ? 7.447   -49.012  -21.327 1.000 45.023  0 21  ALA FFF CB  1 ? 20 
ATOM   6813  N N   . CYS F  2 22  ? 10.386  -48.213  -20.417 1.000 44.799  0 22  CYS FFF N   1 ? 20 
ATOM   6814  C CA  . CYS F  2 22  ? 11.822  -48.259  -20.735 1.000 44.636  0 22  CYS FFF CA  1 ? 20 
ATOM   6815  C C   . CYS F  2 22  ? 12.368  -49.625  -20.350 1.000 42.248  0 22  CYS FFF C   1 ? 20 
ATOM   6816  O O   . CYS F  2 22  ? 12.195  -50.034  -19.191 1.000 42.743  0 22  CYS FFF O   1 ? 20 
ATOM   6817  C CB  . CYS F  2 22  ? 12.550  -47.163  -19.995 1.000 48.354  0 22  CYS FFF CB  1 ? 20 
ATOM   6818  S SG  . CYS F  2 22  ? 14.335  -47.394  -20.088 1.000 51.851  0 22  CYS FFF SG  1 ? 20 
ATOM   6819  N N   . ILE F  2 23  ? 12.974  -50.306  -21.308 1.000 39.540  0 23  ILE FFF N   1 ? 20 
ATOM   6820  C CA  . ILE F  2 23  ? 13.494  -51.685  -21.142 1.000 38.806  0 23  ILE FFF CA  1 ? 20 
ATOM   6821  C C   . ILE F  2 23  ? 15.027  -51.603  -21.148 1.000 38.486  0 23  ILE FFF C   1 ? 20 
ATOM   6822  O O   . ILE F  2 23  ? 15.586  -50.815  -21.930 1.000 38.893  0 23  ILE FFF O   1 ? 20 
ATOM   6823  C CB  . ILE F  2 23  ? 12.895  -52.623  -22.211 1.000 38.017  0 23  ILE FFF CB  1 ? 20 
ATOM   6824  C CG1 . ILE F  2 23  ? 13.247  -54.083  -21.915 1.000 38.611  0 23  ILE FFF CG1 1 ? 20 
ATOM   6825  C CG2 . ILE F  2 23  ? 13.305  -52.201  -23.604 1.000 37.532  0 23  ILE FFF CG2 1 ? 20 
ATOM   6826  C CD1 . ILE F  2 23  ? 12.617  -55.087  -22.843 1.000 37.929  0 23  ILE FFF CD1 1 ? 20 
ATOM   6827  N N   . ALA F  2 24  ? 15.665  -52.343  -20.240 1.000 38.044  0 24  ALA FFF N   1 ? 20 
ATOM   6828  C CA  . ALA F  2 24  ? 17.126  -52.407  -20.062 1.000 38.024  0 24  ALA FFF CA  1 ? 20 
ATOM   6829  C C   . ALA F  2 24  ? 17.647  -53.746  -20.600 1.000 37.725  0 24  ALA FFF C   1 ? 20 
ATOM   6830  O O   . ALA F  2 24  ? 16.904  -54.761  -20.534 1.000 39.246  0 24  ALA FFF O   1 ? 20 
ATOM   6831  C CB  . ALA F  2 24  ? 17.470  -52.216  -18.609 1.000 39.879  0 24  ALA FFF CB  1 ? 20 
ATOM   6832  N N   . SER F  2 25  ? 18.868  -53.738  -21.133 1.000 43.395  0 25  SER FFF N   1 ? 21 
ATOM   6833  C CA  . SER F  2 25  ? 19.668  -54.951  -21.396 1.000 42.819  0 25  SER FFF CA  1 ? 21 
ATOM   6834  C C   . SER F  2 25  ? 20.074  -55.566  -20.060 1.000 43.139  0 25  SER FFF C   1 ? 21 
ATOM   6835  O O   . SER F  2 25  ? 19.841  -54.940  -18.999 1.000 43.993  0 25  SER FFF O   1 ? 21 
ATOM   6836  C CB  . SER F  2 25  ? 20.876  -54.609  -22.212 1.000 43.281  0 25  SER FFF CB  1 ? 21 
ATOM   6837  O OG  . SER F  2 25  ? 21.768  -53.793  -21.465 1.000 43.447  0 25  SER FFF OG  1 ? 21 
ATOM   6838  N N   . GLY F  2 26  ? 20.676  -56.747  -20.104 1.000 45.802  0 26  GLY FFF N   1 ? 21 
ATOM   6839  C CA  . GLY F  2 26  ? 21.336  -57.341  -18.930 1.000 47.981  0 26  GLY FFF CA  1 ? 21 
ATOM   6840  C C   . GLY F  2 26  ? 20.429  -58.277  -18.160 1.000 48.310  0 26  GLY FFF C   1 ? 21 
ATOM   6841  O O   . GLY F  2 26  ? 19.231  -58.261  -18.381 1.000 47.744  0 26  GLY FFF O   1 ? 21 
ATOM   6842  N N   . ARG F  2 27  ? 20.997  -59.026  -17.231 1.000 52.140  0 27  ARG FFF N   1 ? 21 
ATOM   6843  C CA  . ARG F  2 27  ? 20.254  -59.923  -16.330 1.000 56.439  0 27  ARG FFF CA  1 ? 21 
ATOM   6844  C C   . ARG F  2 27  ? 20.415  -59.413  -14.896 1.000 53.136  0 27  ARG FFF C   1 ? 21 
ATOM   6845  O O   . ARG F  2 27  ? 20.149  -60.214  -13.975 1.000 56.563  0 27  ARG FFF O   1 ? 21 
ATOM   6846  C CB  . ARG F  2 27  ? 20.767  -61.352  -16.501 1.000 64.334  0 27  ARG FFF CB  1 ? 21 
ATOM   6847  C CG  . ARG F  2 27  ? 20.042  -62.164  -17.570 1.000 72.258  0 27  ARG FFF CG  1 ? 21 
ATOM   6848  C CD  . ARG F  2 27  ? 20.654  -63.562  -17.701 1.000 84.917  0 27  ARG FFF CD  1 ? 21 
ATOM   6849  N NE  . ARG F  2 27  ? 22.081  -63.585  -17.321 1.000 91.294  0 27  ARG FFF NE  1 ? 21 
ATOM   6850  C CZ  . ARG F  2 27  ? 23.134  -63.715  -18.134 1.000 94.530  0 27  ARG FFF CZ  1 ? 21 
ATOM   6851  N NH1 . ARG F  2 27  ? 22.978  -63.898  -19.438 1.000 97.337  0 27  ARG FFF NH1 1 ? 21 
ATOM   6852  N NH2 . ARG F  2 27  ? 24.353  -63.668  -17.614 1.000 94.920  0 27  ARG FFF NH2 1 ? 21 
ATOM   6853  N N   . THR F  2 28  ? 20.761  -58.140  -14.669 1.000 48.010  0 28  THR FFF N   1 ? 21 
ATOM   6854  C CA  . THR F  2 28  ? 20.879  -57.602  -13.287 1.000 46.514  0 28  THR FFF CA  1 ? 21 
ATOM   6855  C C   . THR F  2 28  ? 20.054  -56.327  -13.143 1.000 44.603  0 28  THR FFF C   1 ? 21 
ATOM   6856  O O   . THR F  2 28  ? 20.437  -55.484  -12.327 1.000 44.445  0 28  THR FFF O   1 ? 21 
ATOM   6857  C CB  . THR F  2 28  ? 22.332  -57.414  -12.832 1.000 46.546  0 28  THR FFF CB  1 ? 21 
ATOM   6858  O OG1 . THR F  2 28  ? 22.973  -56.599  -13.808 1.000 46.597  0 28  THR FFF OG1 1 ? 21 
ATOM   6859  C CG2 . THR F  2 28  ? 23.047  -58.731  -12.627 1.000 47.119  0 28  THR FFF CG2 1 ? 21 
ATOM   6860  N N   . PHE F  2 29  ? 18.918  -56.265  -13.836 1.000 42.416  0 29  PHE FFF N   1 ? 21 
ATOM   6861  C CA  . PHE F  2 29  ? 17.976  -55.137  -13.764 1.000 40.490  0 29  PHE FFF CA  1 ? 21 
ATOM   6862  C C   . PHE F  2 29  ? 17.587  -54.859  -12.313 1.000 40.080  0 29  PHE FFF C   1 ? 21 
ATOM   6863  O O   . PHE F  2 29  ? 17.493  -53.651  -11.969 1.000 39.822  0 29  PHE FFF O   1 ? 21 
ATOM   6864  C CB  . PHE F  2 29  ? 16.728  -55.459  -14.572 1.000 40.510  0 29  PHE FFF CB  1 ? 21 
ATOM   6865  C CG  . PHE F  2 29  ? 15.747  -54.326  -14.633 1.000 40.136  0 29  PHE FFF CG  1 ? 21 
ATOM   6866  C CD1 . PHE F  2 29  ? 16.001  -53.240  -15.459 1.000 39.709  0 29  PHE FFF CD1 1 ? 21 
ATOM   6867  C CD2 . PHE F  2 29  ? 14.594  -54.343  -13.871 1.000 39.621  0 29  PHE FFF CD2 1 ? 21 
ATOM   6868  C CE1 . PHE F  2 29  ? 15.109  -52.186  -15.528 1.000 40.098  0 29  PHE FFF CE1 1 ? 21 
ATOM   6869  C CE2 . PHE F  2 29  ? 13.703  -53.284  -13.944 1.000 40.368  0 29  PHE FFF CE2 1 ? 21 
ATOM   6870  C CZ  . PHE F  2 29  ? 13.964  -52.216  -14.775 1.000 40.215  0 29  PHE FFF CZ  1 ? 21 
ATOM   6871  N N   . HIS F  2 30  ? 17.408  -55.915  -11.495 1.000 39.736  0 30  HIS FFF N   1 ? 21 
ATOM   6872  C CA  . HIS F  2 30  ? 17.013  -55.807  -10.065 1.000 41.253  0 30  HIS FFF CA  1 ? 21 
ATOM   6873  C C   . HIS F  2 30  ? 18.030  -54.959  -9.277  1.000 40.746  0 30  HIS FFF C   1 ? 21 
ATOM   6874  O O   . HIS F  2 30  ? 17.655  -54.438  -8.205  1.000 41.557  0 30  HIS FFF O   1 ? 21 
ATOM   6875  C CB  . HIS F  2 30  ? 16.828  -57.211  -9.448  1.000 42.246  0 30  HIS FFF CB  1 ? 21 
ATOM   6876  C CG  . HIS F  2 30  ? 18.136  -57.915  -9.297  1.000 43.134  0 30  HIS FFF CG  1 ? 21 
ATOM   6877  N ND1 . HIS F  2 30  ? 18.776  -58.577  -10.342 1.000 44.761  0 30  HIS FFF ND1 1 ? 21 
ATOM   6878  C CD2 . HIS F  2 30  ? 19.013  -57.921  -8.271  1.000 43.717  0 30  HIS FFF CD2 1 ? 21 
ATOM   6879  C CE1 . HIS F  2 30  ? 19.974  -58.948  -9.951  1.000 44.710  0 30  HIS FFF CE1 1 ? 21 
ATOM   6880  N NE2 . HIS F  2 30  ? 20.148  -58.551  -8.692  1.000 44.474  0 30  HIS FFF NE2 1 ? 21 
ATOM   6881  N N   . SER F  2 31  ? 19.276  -54.846  -9.771  1.000 41.179  0 31  SER FFF N   1 ? 21 
ATOM   6882  C CA  . SER F  2 31  ? 20.362  -54.158  -9.042  1.000 41.852  0 31  SER FFF CA  1 ? 21 
ATOM   6883  C C   . SER F  2 31  ? 20.332  -52.655  -9.343  1.000 42.447  0 31  SER FFF C   1 ? 21 
ATOM   6884  O O   . SER F  2 31  ? 21.161  -51.946  -8.769  1.000 42.716  0 31  SER FFF O   1 ? 21 
ATOM   6885  C CB  . SER F  2 31  ? 21.698  -54.779  -9.351  1.000 42.314  0 31  SER FFF CB  1 ? 21 
ATOM   6886  O OG  . SER F  2 31  ? 22.127  -54.487  -10.656 1.000 43.797  0 31  SER FFF OG  1 ? 21 
ATOM   6887  N N   . TYR F  2 32  ? 19.434  -52.194  -10.220 1.000 41.996  0 32  TYR FFF N   1 ? 21 
ATOM   6888  C CA  . TYR F  2 32  ? 19.417  -50.797  -10.704 1.000 43.184  0 32  TYR FFF CA  1 ? 21 
ATOM   6889  C C   . TYR F  2 32  ? 18.263  -50.034  -10.067 1.000 44.139  0 32  TYR FFF C   1 ? 21 
ATOM   6890  O O   . TYR F  2 32  ? 17.146  -50.504  -10.042 1.000 41.026  0 32  TYR FFF O   1 ? 21 
ATOM   6891  C CB  . TYR F  2 32  ? 19.400  -50.721  -12.235 1.000 43.321  0 32  TYR FFF CB  1 ? 21 
ATOM   6892  C CG  . TYR F  2 32  ? 20.731  -51.075  -12.820 1.000 43.843  0 32  TYR FFF CG  1 ? 21 
ATOM   6893  C CD1 . TYR F  2 32  ? 21.055  -52.382  -13.077 1.000 45.177  0 32  TYR FFF CD1 1 ? 21 
ATOM   6894  C CD2 . TYR F  2 32  ? 21.709  -50.135  -13.014 1.000 45.971  0 32  TYR FFF CD2 1 ? 21 
ATOM   6895  C CE1 . TYR F  2 32  ? 22.301  -52.753  -13.573 1.000 46.136  0 32  TYR FFF CE1 1 ? 21 
ATOM   6896  C CE2 . TYR F  2 32  ? 22.962  -50.483  -13.489 1.000 48.507  0 32  TYR FFF CE2 1 ? 21 
ATOM   6897  C CZ  . TYR F  2 32  ? 23.269  -51.801  -13.771 1.000 47.780  0 32  TYR FFF CZ  1 ? 21 
ATOM   6898  O OH  . TYR F  2 32  ? 24.506  -52.178  -14.215 1.000 50.782  0 32  TYR FFF OH  1 ? 21 
ATOM   6899  N N   . VAL F  2 33  ? 18.589  -48.855  -9.548  1.000 32.911  0 33  VAL FFF N   1 ? 22 
ATOM   6900  C CA  . VAL F  2 33  ? 17.626  -47.744  -9.342  1.000 37.425  0 33  VAL FFF CA  1 ? 22 
ATOM   6901  C C   . VAL F  2 33  ? 17.281  -47.201  -10.726 1.000 39.234  0 33  VAL FFF C   1 ? 22 
ATOM   6902  O O   . VAL F  2 33  ? 18.210  -46.900  -11.487 1.000 39.302  0 33  VAL FFF O   1 ? 22 
ATOM   6903  C CB  . VAL F  2 33  ? 18.217  -46.666  -8.430  1.000 40.174  0 33  VAL FFF CB  1 ? 22 
ATOM   6904  C CG1 . VAL F  2 33  ? 17.313  -45.457  -8.307  1.000 41.672  0 33  VAL FFF CG1 1 ? 22 
ATOM   6905  C CG2 . VAL F  2 33  ? 18.519  -47.244  -7.056  1.000 43.059  0 33  VAL FFF CG2 1 ? 22 
ATOM   6906  N N   . MET F  2 34  ? 15.992  -47.117  -11.044 1.000 41.206  0 34  MET FFF N   1 ? 22 
ATOM   6907  C CA  . MET F  2 34  ? 15.516  -46.645  -12.370 1.000 41.234  0 34  MET FFF CA  1 ? 22 
ATOM   6908  C C   . MET F  2 34  ? 14.855  -45.276  -12.198 1.000 40.479  0 34  MET FFF C   1 ? 22 
ATOM   6909  O O   . MET F  2 34  ? 14.193  -45.033  -11.166 1.000 40.926  0 34  MET FFF O   1 ? 22 
ATOM   6910  C CB  . MET F  2 34  ? 14.534  -47.638  -13.007 1.000 41.031  0 34  MET FFF CB  1 ? 22 
ATOM   6911  C CG  . MET F  2 34  ? 15.121  -49.019  -13.216 1.000 40.820  0 34  MET FFF CG  1 ? 22 
ATOM   6912  S SD  . MET F  2 34  ? 16.606  -48.984  -14.242 1.000 42.604  0 34  MET FFF SD  1 ? 22 
ATOM   6913  C CE  . MET F  2 34  ? 15.934  -48.417  -15.805 1.000 45.420  0 34  MET FFF CE  1 ? 22 
ATOM   6914  N N   . ALA F  2 35  ? 15.062  -44.390  -13.173 1.000 38.928  0 35  ALA FFF N   1 ? 22 
ATOM   6915  C CA  . ALA F  2 35  ? 14.572  -43.006  -13.098 1.000 38.822  0 35  ALA FFF CA  1 ? 22 
ATOM   6916  C C   . ALA F  2 35  ? 14.099  -42.530  -14.472 1.000 39.030  0 35  ALA FFF C   1 ? 22 
ATOM   6917  O O   . ALA F  2 35  ? 14.528  -43.074  -15.514 1.000 39.554  0 35  ALA FFF O   1 ? 22 
ATOM   6918  C CB  . ALA F  2 35  ? 15.650  -42.123  -12.522 1.000 39.641  0 35  ALA FFF CB  1 ? 22 
ATOM   6919  N N   . TRP F  2 36  ? 13.228  -41.527  -14.417 1.000 40.583  0 36  TRP FFF N   1 ? 22 
ATOM   6920  C CA  . TRP F  2 36  ? 12.757  -40.713  -15.554 1.000 41.446  0 36  TRP FFF CA  1 ? 22 
ATOM   6921  C C   . TRP F  2 36  ? 13.162  -39.263  -15.326 1.000 41.324  0 36  TRP FFF C   1 ? 22 
ATOM   6922  O O   . TRP F  2 36  ? 12.952  -38.748  -14.232 1.000 41.903  0 36  TRP FFF O   1 ? 22 
ATOM   6923  C CB  . TRP F  2 36  ? 11.244  -40.856  -15.699 1.000 44.843  0 36  TRP FFF CB  1 ? 22 
ATOM   6924  C CG  . TRP F  2 36  ? 10.822  -42.203  -16.192 1.000 42.748  0 36  TRP FFF CG  1 ? 22 
ATOM   6925  C CD1 . TRP F  2 36  ? 10.390  -43.244  -15.438 1.000 43.309  0 36  TRP FFF CD1 1 ? 22 
ATOM   6926  C CD2 . TRP F  2 36  ? 10.807  -42.656  -17.552 1.000 42.988  0 36  TRP FFF CD2 1 ? 22 
ATOM   6927  N NE1 . TRP F  2 36  ? 10.088  -44.309  -16.237 1.000 43.065  0 36  TRP FFF NE1 1 ? 22 
ATOM   6928  C CE2 . TRP F  2 36  ? 10.316  -43.970  -17.540 1.000 43.337  0 36  TRP FFF CE2 1 ? 22 
ATOM   6929  C CE3 . TRP F  2 36  ? 11.126  -42.069  -18.779 1.000 43.963  0 36  TRP FFF CE3 1 ? 22 
ATOM   6930  C CZ2 . TRP F  2 36  ? 10.148  -44.713  -18.702 1.000 44.057  0 36  TRP FFF CZ2 1 ? 22 
ATOM   6931  C CZ3 . TRP F  2 36  ? 10.954  -42.794  -19.935 1.000 44.881  0 36  TRP FFF CZ3 1 ? 22 
ATOM   6932  C CH2 . TRP F  2 36  ? 10.480  -44.107  -19.895 1.000 45.570  0 36  TRP FFF CH2 1 ? 22 
ATOM   6933  N N   . PHE F  2 37  ? 13.762  -38.666  -16.341 1.000 41.363  0 37  PHE FFF N   1 ? 22 
ATOM   6934  C CA  . PHE F  2 37  ? 14.011  -37.216  -16.440 1.000 42.126  0 37  PHE FFF CA  1 ? 22 
ATOM   6935  C C   . PHE F  2 37  ? 13.321  -36.736  -17.710 1.000 43.171  0 37  PHE FFF C   1 ? 22 
ATOM   6936  O O   . PHE F  2 37  ? 12.995  -37.567  -18.572 1.000 42.735  0 37  PHE FFF O   1 ? 22 
ATOM   6937  C CB  . PHE F  2 37  ? 15.515  -36.937  -16.508 1.000 42.502  0 37  PHE FFF CB  1 ? 22 
ATOM   6938  C CG  . PHE F  2 37  ? 16.261  -37.132  -15.217 1.000 39.757  0 37  PHE FFF CG  1 ? 22 
ATOM   6939  C CD1 . PHE F  2 37  ? 16.542  -38.402  -14.744 1.000 37.424  0 37  PHE FFF CD1 1 ? 22 
ATOM   6940  C CD2 . PHE F  2 37  ? 16.712  -36.037  -14.500 1.000 41.359  0 37  PHE FFF CD2 1 ? 22 
ATOM   6941  C CE1 . PHE F  2 37  ? 17.256  -38.566  -13.565 1.000 37.399  0 37  PHE FFF CE1 1 ? 22 
ATOM   6942  C CE2 . PHE F  2 37  ? 17.401  -36.203  -13.315 1.000 41.094  0 37  PHE FFF CE2 1 ? 22 
ATOM   6943  C CZ  . PHE F  2 37  ? 17.678  -37.466  -12.852 1.000 39.946  0 37  PHE FFF CZ  1 ? 22 
ATOM   6944  N N   . ARG F  2 38  ? 13.119  -35.431  -17.830 1.000 45.144  0 38  ARG FFF N   1 ? 22 
ATOM   6945  C CA  . ARG F  2 38  ? 12.597  -34.852  -19.089 1.000 46.224  0 38  ARG FFF CA  1 ? 22 
ATOM   6946  C C   . ARG F  2 38  ? 13.314  -33.542  -19.384 1.000 47.423  0 38  ARG FFF C   1 ? 22 
ATOM   6947  O O   . ARG F  2 38  ? 13.887  -32.922  -18.469 1.000 47.447  0 38  ARG FFF O   1 ? 22 
ATOM   6948  C CB  . ARG F  2 38  ? 11.083  -34.643  -19.000 1.000 46.285  0 38  ARG FFF CB  1 ? 22 
ATOM   6949  C CG  . ARG F  2 38  ? 10.684  -33.502  -18.080 1.000 45.508  0 38  ARG FFF CG  1 ? 22 
ATOM   6950  C CD  . ARG F  2 38  ? 9.201   -33.560  -17.812 1.000 45.578  0 38  ARG FFF CD  1 ? 22 
ATOM   6951  N NE  . ARG F  2 38  ? 8.807   -32.539  -16.855 1.000 46.753  0 38  ARG FFF NE  1 ? 22 
ATOM   6952  C CZ  . ARG F  2 38  ? 7.571   -32.279  -16.482 1.000 46.686  0 38  ARG FFF CZ  1 ? 22 
ATOM   6953  N NH1 . ARG F  2 38  ? 6.549   -32.952  -16.985 1.000 47.621  0 38  ARG FFF NH1 1 ? 22 
ATOM   6954  N NH2 . ARG F  2 38  ? 7.381   -31.346  -15.583 1.000 47.936  0 38  ARG FFF NH2 1 ? 22 
ATOM   6955  N N   . GLN F  2 39  ? 13.268  -33.149  -20.642 1.000 47.510  0 39  GLN FFF N   1 ? 22 
ATOM   6956  C CA  . GLN F  2 39  ? 13.954  -31.934  -21.094 1.000 48.585  0 39  GLN FFF CA  1 ? 22 
ATOM   6957  C C   . GLN F  2 39  ? 13.078  -31.267  -22.141 1.000 50.561  0 39  GLN FFF C   1 ? 22 
ATOM   6958  O O   . GLN F  2 39  ? 12.894  -31.846  -23.238 1.000 48.834  0 39  GLN FFF O   1 ? 22 
ATOM   6959  C CB  . GLN F  2 39  ? 15.321  -32.293  -21.631 1.000 49.036  0 39  GLN FFF CB  1 ? 22 
ATOM   6960  C CG  . GLN F  2 39  ? 16.074  -31.077  -22.119 1.000 51.716  0 39  GLN FFF CG  1 ? 22 
ATOM   6961  C CD  . GLN F  2 39  ? 17.511  -31.421  -22.387 1.000 52.345  0 39  GLN FFF CD  1 ? 22 
ATOM   6962  O OE1 . GLN F  2 39  ? 17.845  -32.510  -22.809 1.000 49.518  0 39  GLN FFF OE1 1 ? 22 
ATOM   6963  N NE2 . GLN F  2 39  ? 18.388  -30.479  -22.086 1.000 57.052  0 39  GLN FFF NE2 1 ? 22 
ATOM   6964  N N   . ALA F  2 40  ? 12.534  -30.116  -21.748 1.000 52.472  0 40  ALA FFF N   1 ? 22 
ATOM   6965  C CA  . ALA F  2 40  ? 11.842  -29.171  -22.635 1.000 55.325  0 40  ALA FFF CA  1 ? 22 
ATOM   6966  C C   . ALA F  2 40  ? 12.920  -28.349  -23.331 1.000 57.481  0 40  ALA FFF C   1 ? 22 
ATOM   6967  O O   . ALA F  2 40  ? 14.021  -28.172  -22.802 1.000 54.657  0 40  ALA FFF O   1 ? 22 
ATOM   6968  C CB  . ALA F  2 40  ? 10.898  -28.328  -21.825 1.000 57.660  0 40  ALA FFF CB  1 ? 22 
ATOM   6969  N N   . PRO F  2 41  ? 12.663  -27.889  -24.573 1.000 61.987  0 41  PRO FFF N   1 ? 22 
ATOM   6970  C CA  . PRO F  2 41  ? 13.688  -27.144  -25.316 1.000 64.575  0 41  PRO FFF CA  1 ? 22 
ATOM   6971  C C   . PRO F  2 41  ? 14.067  -25.850  -24.566 1.000 66.437  0 41  PRO FFF C   1 ? 22 
ATOM   6972  O O   . PRO F  2 41  ? 13.192  -25.158  -24.056 1.000 68.181  0 41  PRO FFF O   1 ? 22 
ATOM   6973  C CB  . PRO F  2 41  ? 13.077  -26.877  -26.697 1.000 66.364  0 41  PRO FFF CB  1 ? 22 
ATOM   6974  C CG  . PRO F  2 41  ? 11.579  -27.216  -26.551 1.000 66.454  0 41  PRO FFF CG  1 ? 22 
ATOM   6975  C CD  . PRO F  2 41  ? 11.404  -28.073  -25.312 1.000 62.037  0 41  PRO FFF CD  1 ? 22 
ATOM   6976  N N   . GLY F  2 42  ? 15.367  -25.592  -24.447 1.000 65.838  0 42  GLY FFF N   1 ? 22 
ATOM   6977  C CA  . GLY F  2 42  ? 15.912  -24.408  -23.754 1.000 65.903  0 42  GLY FFF CA  1 ? 22 
ATOM   6978  C C   . GLY F  2 42  ? 16.137  -24.660  -22.274 1.000 63.760  0 42  GLY FFF C   1 ? 22 
ATOM   6979  O O   . GLY F  2 42  ? 16.837  -23.826  -21.666 1.000 63.434  0 42  GLY FFF O   1 ? 22 
ATOM   6980  N N   . LYS F  2 43  ? 15.674  -25.793  -21.729 1.000 61.506  0 43  LYS FFF N   1 ? 22 
ATOM   6981  C CA  . LYS F  2 43  ? 15.814  -26.100  -20.286 1.000 62.957  0 43  LYS FFF CA  1 ? 22 
ATOM   6982  C C   . LYS F  2 43  ? 16.776  -27.260  -20.091 1.000 62.585  0 43  LYS FFF C   1 ? 22 
ATOM   6983  O O   . LYS F  2 43  ? 17.060  -27.956  -21.064 1.000 61.235  0 43  LYS FFF O   1 ? 22 
ATOM   6984  C CB  . LYS F  2 43  ? 14.475  -26.477  -19.660 1.000 63.440  0 43  LYS FFF CB  1 ? 22 
ATOM   6985  C CG  . LYS F  2 43  ? 13.613  -25.324  -19.214 1.000 67.638  0 43  LYS FFF CG  1 ? 22 
ATOM   6986  C CD  . LYS F  2 43  ? 12.423  -25.818  -18.395 1.000 66.472  0 43  LYS FFF CD  1 ? 22 
ATOM   6987  C CE  . LYS F  2 43  ? 11.539  -24.687  -17.905 1.000 70.346  0 43  LYS FFF CE  1 ? 22 
ATOM   6988  N NZ  . LYS F  2 43  ? 10.854  -23.971  -19.015 1.000 71.323  0 43  LYS FFF NZ  1 ? 22 
ATOM   6989  N N   . GLU F  2 44  ? 17.241  -27.438  -18.855 1.000 64.804  0 44  GLU FFF N   1 ? 22 
ATOM   6990  C CA  . GLU F  2 44  ? 18.107  -28.568  -18.469 1.000 65.102  0 44  GLU FFF CA  1 ? 22 
ATOM   6991  C C   . GLU F  2 44  ? 17.229  -29.780  -18.228 1.000 59.819  0 44  GLU FFF C   1 ? 22 
ATOM   6992  O O   . GLU F  2 44  ? 16.014  -29.622  -18.186 1.000 62.149  0 44  GLU FFF O   1 ? 22 
ATOM   6993  C CB  . GLU F  2 44  ? 18.938  -28.205  -17.238 1.000 72.324  0 44  GLU FFF CB  1 ? 22 
ATOM   6994  C CG  . GLU F  2 44  ? 19.727  -26.910  -17.391 1.000 84.734  0 44  GLU FFF CG  1 ? 22 
ATOM   6995  C CD  . GLU F  2 44  ? 20.658  -26.823  -18.604 1.000 91.442  0 44  GLU FFF CD  1 ? 22 
ATOM   6996  O OE1 . GLU F  2 44  ? 21.271  -27.859  -18.954 1.000 89.136  0 44  GLU FFF OE1 1 ? 22 
ATOM   6997  O OE2 . GLU F  2 44  ? 20.754  -25.718  -19.207 1.000 101.965 0 44  GLU FFF OE2 1 ? 22 
ATOM   6998  N N   . ARG F  2 45  ? 17.837  -30.951  -18.131 1.000 55.275  0 45  ARG FFF N   1 ? 22 
ATOM   6999  C CA  . ARG F  2 45  ? 17.157  -32.197  -17.718 1.000 53.070  0 45  ARG FFF CA  1 ? 22 
ATOM   7000  C C   . ARG F  2 45  ? 16.604  -32.001  -16.313 1.000 54.537  0 45  ARG FFF C   1 ? 22 
ATOM   7001  O O   . ARG F  2 45  ? 17.369  -31.682  -15.401 1.000 57.711  0 45  ARG FFF O   1 ? 22 
ATOM   7002  C CB  . ARG F  2 45  ? 18.109  -33.390  -17.755 1.000 52.479  0 45  ARG FFF CB  1 ? 22 
ATOM   7003  C CG  . ARG F  2 45  ? 18.122  -34.070  -19.105 1.000 52.181  0 45  ARG FFF CG  1 ? 22 
ATOM   7004  C CD  . ARG F  2 45  ? 19.376  -34.873  -19.297 1.000 53.861  0 45  ARG FFF CD  1 ? 22 
ATOM   7005  N NE  . ARG F  2 45  ? 19.709  -34.972  -20.707 1.000 55.783  0 45  ARG FFF NE  1 ? 22 
ATOM   7006  C CZ  . ARG F  2 45  ? 20.281  -36.022  -21.277 1.000 57.043  0 45  ARG FFF CZ  1 ? 22 
ATOM   7007  N NH1 . ARG F  2 45  ? 20.574  -37.099  -20.567 1.000 57.624  0 45  ARG FFF NH1 1 ? 22 
ATOM   7008  N NH2 . ARG F  2 45  ? 20.530  -36.011  -22.575 1.000 61.512  0 45  ARG FFF NH2 1 ? 22 
ATOM   7009  N N   . GLU F  2 46  ? 15.296  -32.179  -16.171 1.000 55.943  0 46  GLU FFF N   1 ? 22 
ATOM   7010  C CA  . GLU F  2 46  ? 14.511  -31.987  -14.938 1.000 55.605  0 46  GLU FFF CA  1 ? 22 
ATOM   7011  C C   . GLU F  2 46  ? 14.128  -33.397  -14.457 1.000 52.449  0 46  GLU FFF C   1 ? 22 
ATOM   7012  O O   . GLU F  2 46  ? 13.687  -34.245  -15.274 1.000 51.895  0 46  GLU FFF O   1 ? 22 
ATOM   7013  C CB  . GLU F  2 46  ? 13.370  -31.039  -15.294 1.000 61.895  0 46  GLU FFF CB  1 ? 22 
ATOM   7014  C CG  . GLU F  2 46  ? 12.188  -30.969  -14.321 1.000 68.655  0 46  GLU FFF CG  1 ? 22 
ATOM   7015  C CD  . GLU F  2 46  ? 10.987  -30.195  -14.863 1.000 73.159  0 46  GLU FFF CD  1 ? 22 
ATOM   7016  O OE1 . GLU F  2 46  ? 11.206  -29.305  -15.733 1.000 78.299  0 46  GLU FFF OE1 1 ? 22 
ATOM   7017  O OE2 . GLU F  2 46  ? 9.844   -30.445  -14.393 1.000 74.178  0 46  GLU FFF OE2 1 ? 22 
ATOM   7018  N N   . PHE F  2 47  ? 14.360  -33.674  -13.184 1.000 50.294  0 47  PHE FFF N   1 ? 22 
ATOM   7019  C CA  . PHE F  2 47  ? 13.983  -34.955  -12.543 1.000 49.349  0 47  PHE FFF CA  1 ? 22 
ATOM   7020  C C   . PHE F  2 47  ? 12.454  -35.088  -12.563 1.000 48.158  0 47  PHE FFF C   1 ? 22 
ATOM   7021  O O   . PHE F  2 47  ? 11.760  -34.141  -12.195 1.000 48.492  0 47  PHE FFF O   1 ? 22 
ATOM   7022  C CB  . PHE F  2 47  ? 14.498  -35.027  -11.104 1.000 47.849  0 47  PHE FFF CB  1 ? 22 
ATOM   7023  C CG  . PHE F  2 47  ? 14.035  -36.245  -10.358 1.000 46.987  0 47  PHE FFF CG  1 ? 22 
ATOM   7024  C CD1 . PHE F  2 47  ? 14.677  -37.458  -10.537 1.000 45.642  0 47  PHE FFF CD1 1 ? 22 
ATOM   7025  C CD2 . PHE F  2 47  ? 12.960  -36.182  -9.492  1.000 49.739  0 47  PHE FFF CD2 1 ? 22 
ATOM   7026  C CE1 . PHE F  2 47  ? 14.248  -38.582  -9.861  1.000 46.659  0 47  PHE FFF CE1 1 ? 22 
ATOM   7027  C CE2 . PHE F  2 47  ? 12.532  -37.310  -8.812  1.000 49.531  0 47  PHE FFF CE2 1 ? 22 
ATOM   7028  C CZ  . PHE F  2 47  ? 13.171  -38.507  -9.001  1.000 48.337  0 47  PHE FFF CZ  1 ? 22 
ATOM   7029  N N   . VAL F  2 48  ? 11.967  -36.268  -12.939 1.000 46.445  0 48  VAL FFF N   1 ? 22 
ATOM   7030  C CA  . VAL F  2 48  ? 10.515  -36.580  -12.975 1.000 46.434  0 48  VAL FFF CA  1 ? 22 
ATOM   7031  C C   . VAL F  2 48  ? 10.196  -37.600  -11.875 1.000 45.483  0 48  VAL FFF C   1 ? 22 
ATOM   7032  O O   . VAL F  2 48  ? 9.279   -37.322  -11.059 1.000 44.700  0 48  VAL FFF O   1 ? 22 
ATOM   7033  C CB  . VAL F  2 48  ? 10.073  -37.059  -14.369 1.000 45.506  0 48  VAL FFF CB  1 ? 22 
ATOM   7034  C CG1 . VAL F  2 48  ? 8.619   -37.503  -14.370 1.000 47.708  0 48  VAL FFF CG1 1 ? 22 
ATOM   7035  C CG2 . VAL F  2 48  ? 10.302  -35.985  -15.414 1.000 45.040  0 48  VAL FFF CG2 1 ? 22 
ATOM   7036  N N   . ALA F  2 49  ? 10.874  -38.750  -11.873 1.000 43.289  0 49  ALA FFF N   1 ? 22 
ATOM   7037  C CA  . ALA F  2 49  ? 10.557  -39.858  -10.940 1.000 43.574  0 49  ALA FFF CA  1 ? 22 
ATOM   7038  C C   . ALA F  2 49  ? 11.705  -40.867  -10.857 1.000 43.098  0 49  ALA FFF C   1 ? 22 
ATOM   7039  O O   . ALA F  2 49  ? 12.507  -40.974  -11.807 1.000 43.267  0 49  ALA FFF O   1 ? 22 
ATOM   7040  C CB  . ALA F  2 49  ? 9.267   -40.533  -11.344 1.000 43.176  0 49  ALA FFF CB  1 ? 22 
ATOM   7041  N N   . ALA F  2 50  ? 11.755  -41.590  -9.738  1.000 43.084  0 50  ALA FFF N   1 ? 22 
ATOM   7042  C CA  . ALA F  2 50  ? 12.739  -42.664  -9.498  1.000 41.473  0 50  ALA FFF CA  1 ? 22 
ATOM   7043  C C   . ALA F  2 50  ? 12.118  -43.727  -8.597  1.000 39.990  0 50  ALA FFF C   1 ? 22 
ATOM   7044  O O   . ALA F  2 50  ? 11.224  -43.405  -7.780  1.000 39.452  0 50  ALA FFF O   1 ? 22 
ATOM   7045  C CB  . ALA F  2 50  ? 14.015  -42.104  -8.902  1.000 41.398  0 50  ALA FFF CB  1 ? 22 
ATOM   7046  N N   . ILE F  2 51  ? 12.622  -44.947  -8.745  1.000 38.010  0 51  ILE FFF N   1 ? 22 
ATOM   7047  C CA  . ILE F  2 51  ? 12.150  -46.131  -7.995  1.000 40.400  0 51  ILE FFF CA  1 ? 22 
ATOM   7048  C C   . ILE F  2 51  ? 13.369  -46.958  -7.560  1.000 39.547  0 51  ILE FFF C   1 ? 22 
ATOM   7049  O O   . ILE F  2 51  ? 14.241  -47.282  -8.405  1.000 38.864  0 51  ILE FFF O   1 ? 22 
ATOM   7050  C CB  . ILE F  2 51  ? 11.121  -46.904  -8.839  1.000 40.758  0 51  ILE FFF CB  1 ? 22 
ATOM   7051  C CG1 . ILE F  2 51  ? 10.457  -48.019  -8.029  1.000 42.723  0 51  ILE FFF CG1 1 ? 22 
ATOM   7052  C CG2 . ILE F  2 51  ? 11.735  -47.421  -10.132 1.000 41.774  0 51  ILE FFF CG2 1 ? 22 
ATOM   7053  C CD1 . ILE F  2 51  ? 9.223   -48.598  -8.700  1.000 44.396  0 51  ILE FFF CD1 1 ? 22 
ATOM   7054  N N   . SER F  2 52  ? 13.427  -47.279  -6.270  1.000 40.702  0 52  SER FFF N   1 ? 22 
ATOM   7055  C CA  . SER F  2 52  ? 14.515  -48.080  -5.669  1.000 41.780  0 52  SER FFF CA  1 ? 22 
ATOM   7056  C C   . SER F  2 52  ? 14.348  -49.549  -6.079  1.000 43.083  0 52  SER FFF C   1 ? 22 
ATOM   7057  O O   . SER F  2 52  ? 13.317  -49.887  -6.737  1.000 41.498  0 52  SER FFF O   1 ? 22 
ATOM   7058  C CB  . SER F  2 52  ? 14.556  -47.926  -4.192  1.000 43.280  0 52  SER FFF CB  1 ? 22 
ATOM   7059  O OG  . SER F  2 52  ? 15.839  -48.281  -3.716  1.000 46.228  0 52  SER FFF OG  1 ? 22 
ATOM   7060  N N   . TRP F  2 53  ? 15.313  -50.387  -5.696  1.000 42.544  0 53  TRP FFF N   1 ? 22 
ATOM   7061  C CA  . TRP F  2 53  ? 15.425  -51.822  -6.107  1.000 41.373  0 53  TRP FFF CA  1 ? 22 
ATOM   7062  C C   . TRP F  2 53  ? 14.135  -52.559  -5.745  1.000 41.339  0 53  TRP FFF C   1 ? 22 
ATOM   7063  O O   . TRP F  2 53  ? 13.575  -53.180  -6.634  1.000 43.211  0 53  TRP FFF O   1 ? 22 
ATOM   7064  C CB  . TRP F  2 53  ? 16.656  -52.482  -5.456  1.000 40.330  0 53  TRP FFF CB  1 ? 22 
ATOM   7065  C CG  . TRP F  2 53  ? 17.899  -51.647  -5.534  1.000 38.785  0 53  TRP FFF CG  1 ? 22 
ATOM   7066  C CD1 . TRP F  2 53  ? 18.692  -51.463  -6.637  1.000 38.280  0 53  TRP FFF CD1 1 ? 22 
ATOM   7067  C CD2 . TRP F  2 53  ? 18.469  -50.834  -4.495  1.000 37.194  0 53  TRP FFF CD2 1 ? 22 
ATOM   7068  N NE1 . TRP F  2 53  ? 19.716  -50.608  -6.354  1.000 37.159  0 53  TRP FFF NE1 1 ? 22 
ATOM   7069  C CE2 . TRP F  2 53  ? 19.606  -50.206  -5.046  1.000 38.074  0 53  TRP FFF CE2 1 ? 22 
ATOM   7070  C CE3 . TRP F  2 53  ? 18.119  -50.552  -3.177  1.000 39.114  0 53  TRP FFF CE3 1 ? 22 
ATOM   7071  C CZ2 . TRP F  2 53  ? 20.413  -49.345  -4.304  1.000 37.906  0 53  TRP FFF CZ2 1 ? 22 
ATOM   7072  C CZ3 . TRP F  2 53  ? 18.933  -49.718  -2.438  1.000 40.006  0 53  TRP FFF CZ3 1 ? 22 
ATOM   7073  C CH2 . TRP F  2 53  ? 20.055  -49.119  -2.996  1.000 39.065  0 53  TRP FFF CH2 1 ? 22 
ATOM   7074  N N   . SER F  2 54  ? 13.677  -52.429  -4.499  1.000 42.588  0 54  SER FFF N   1 ? 22 
ATOM   7075  C CA  . SER F  2 54  ? 12.505  -53.144  -3.929  1.000 44.178  0 54  SER FFF CA  1 ? 22 
ATOM   7076  C C   . SER F  2 54  ? 11.199  -52.544  -4.437  1.000 45.046  0 54  SER FFF C   1 ? 22 
ATOM   7077  O O   . SER F  2 54  ? 10.149  -53.072  -4.054  1.000 44.263  0 54  SER FFF O   1 ? 22 
ATOM   7078  C CB  . SER F  2 54  ? 12.509  -53.069  -2.431  1.000 45.834  0 54  SER FFF CB  1 ? 22 
ATOM   7079  O OG  . SER F  2 54  ? 12.289  -51.735  -2.027  1.000 45.301  0 54  SER FFF OG  1 ? 22 
ATOM   7080  N N   . SER F  2 55  ? 11.265  -51.429  -5.175  1.000 45.877  0 55  SER FFF N   1 ? 22 
ATOM   7081  C CA  . SER F  2 55  ? 10.108  -50.567  -5.548  1.000 47.581  0 55  SER FFF CA  1 ? 22 
ATOM   7082  C C   . SER F  2 55  ? 9.724   -49.601  -4.422  1.000 50.852  0 55  SER FFF C   1 ? 22 
ATOM   7083  O O   . SER F  2 55  ? 8.802   -48.816  -4.670  1.000 52.256  0 55  SER FFF O   1 ? 22 
ATOM   7084  C CB  . SER F  2 55  ? 8.885   -51.368  -5.973  1.000 46.804  0 55  SER FFF CB  1 ? 22 
ATOM   7085  O OG  . SER F  2 55  ? 9.159   -52.194  -7.099  1.000 45.735  0 55  SER FFF OG  1 ? 22 
ATOM   7086  N N   . THR F  2 56  ? 10.379  -49.609  -3.256  1.000 56.126  0 56  THR FFF N   1 ? 22 
ATOM   7087  C CA  . THR F  2 56  ? 9.677   -49.239  -1.993  1.000 64.445  0 56  THR FFF CA  1 ? 22 
ATOM   7088  C C   . THR F  2 56  ? 9.881   -47.795  -1.582  1.000 64.744  0 56  THR FFF C   1 ? 22 
ATOM   7089  O O   . THR F  2 56  ? 8.990   -47.276  -0.894  1.000 71.245  0 56  THR FFF O   1 ? 22 
ATOM   7090  C CB  . THR F  2 56  ? 10.033  -50.111  -0.788  1.000 74.006  0 56  THR FFF CB  1 ? 22 
ATOM   7091  O OG1 . THR F  2 56  ? 9.116   -51.198  -0.884  1.000 84.046  0 56  THR FFF OG1 1 ? 22 
ATOM   7092  C CG2 . THR F  2 56  ? 9.888   -49.420  0.554   1.000 76.229  0 56  THR FFF CG2 1 ? 22 
ATOM   7093  N N   . PRO F  2 57  ? 11.059  -47.158  -1.800  1.000 53.092  0 57  PRO FFF N   1 ? 22 
ATOM   7094  C CA  . PRO F  2 57  ? 11.063  -45.700  -1.917  1.000 49.417  0 57  PRO FFF CA  1 ? 22 
ATOM   7095  C C   . PRO F  2 57  ? 10.792  -45.423  -3.405  1.000 46.711  0 57  PRO FFF C   1 ? 22 
ATOM   7096  O O   . PRO F  2 57  ? 11.503  -45.975  -4.267  1.000 43.783  0 57  PRO FFF O   1 ? 22 
ATOM   7097  C CB  . PRO F  2 57  ? 12.419  -45.258  -1.356  1.000 48.244  0 57  PRO FFF CB  1 ? 22 
ATOM   7098  C CG  . PRO F  2 57  ? 13.167  -46.575  -1.084  1.000 48.075  0 57  PRO FFF CG  1 ? 22 
ATOM   7099  C CD  . PRO F  2 57  ? 12.394  -47.741  -1.693  1.000 47.100  0 57  PRO FFF CD  1 ? 22 
ATOM   7100  N N   . THR F  2 58  ? 9.715   -44.685  -3.695  1.000 45.731  0 58  THR FFF N   1 ? 22 
ATOM   7101  C CA  . THR F  2 58  ? 9.521   -43.969  -4.986  1.000 45.252  0 58  THR FFF CA  1 ? 22 
ATOM   7102  C C   . THR F  2 58  ? 9.699   -42.473  -4.741  1.000 45.615  0 58  THR FFF C   1 ? 22 
ATOM   7103  O O   . THR F  2 58  ? 9.501   -42.036  -3.625  1.000 48.534  0 58  THR FFF O   1 ? 22 
ATOM   7104  C CB  . THR F  2 58  ? 8.181   -44.243  -5.676  1.000 44.426  0 58  THR FFF CB  1 ? 22 
ATOM   7105  O OG1 . THR F  2 58  ? 7.116   -43.859  -4.812  1.000 45.279  0 58  THR FFF OG1 1 ? 22 
ATOM   7106  C CG2 . THR F  2 58  ? 8.044   -45.685  -6.121  1.000 43.188  0 58  THR FFF CG2 1 ? 22 
ATOM   7107  N N   . TYR F  2 59  ? 10.124  -41.744  -5.757  1.000 45.592  0 59  TYR FFF N   1 ? 22 
ATOM   7108  C CA  . TYR F  2 59  ? 10.392  -40.290  -5.686  1.000 47.213  0 59  TYR FFF CA  1 ? 22 
ATOM   7109  C C   . TYR F  2 59  ? 9.772   -39.630  -6.919  1.000 45.614  0 59  TYR FFF C   1 ? 22 
ATOM   7110  O O   . TYR F  2 59  ? 9.758   -40.248  -7.991  1.000 45.950  0 59  TYR FFF O   1 ? 22 
ATOM   7111  C CB  . TYR F  2 59  ? 11.895  -39.994  -5.656  1.000 48.013  0 59  TYR FFF CB  1 ? 22 
ATOM   7112  C CG  . TYR F  2 59  ? 12.719  -40.665  -4.591  1.000 48.763  0 59  TYR FFF CG  1 ? 22 
ATOM   7113  C CD1 . TYR F  2 59  ? 13.354  -41.876  -4.828  1.000 47.968  0 59  TYR FFF CD1 1 ? 22 
ATOM   7114  C CD2 . TYR F  2 59  ? 12.966  -40.040  -3.383  1.000 51.416  0 59  TYR FFF CD2 1 ? 22 
ATOM   7115  C CE1 . TYR F  2 59  ? 14.171  -42.466  -3.868  1.000 48.393  0 59  TYR FFF CE1 1 ? 22 
ATOM   7116  C CE2 . TYR F  2 59  ? 13.785  -40.610  -2.414  1.000 51.603  0 59  TYR FFF CE2 1 ? 22 
ATOM   7117  C CZ  . TYR F  2 59  ? 14.383  -41.838  -2.652  1.000 49.700  0 59  TYR FFF CZ  1 ? 22 
ATOM   7118  O OH  . TYR F  2 59  ? 15.182  -42.426  -1.714  1.000 47.973  0 59  TYR FFF OH  1 ? 22 
ATOM   7119  N N   . TYR F  2 60  ? 9.326   -38.391  -6.765  1.000 46.607  0 60  TYR FFF N   1 ? 22 
ATOM   7120  C CA  . TYR F  2 60  ? 8.617   -37.596  -7.787  1.000 46.559  0 60  TYR FFF CA  1 ? 22 
ATOM   7121  C C   . TYR F  2 60  ? 9.100   -36.149  -7.728  1.000 48.075  0 60  TYR FFF C   1 ? 22 
ATOM   7122  O O   . TYR F  2 60  ? 9.325   -35.622  -6.653  1.000 49.131  0 60  TYR FFF O   1 ? 22 
ATOM   7123  C CB  . TYR F  2 60  ? 7.109   -37.710  -7.550  1.000 47.607  0 60  TYR FFF CB  1 ? 22 
ATOM   7124  C CG  . TYR F  2 60  ? 6.583   -39.105  -7.755  1.000 46.610  0 60  TYR FFF CG  1 ? 22 
ATOM   7125  C CD1 . TYR F  2 60  ? 6.463   -39.636  -9.033  1.000 46.168  0 60  TYR FFF CD1 1 ? 22 
ATOM   7126  C CD2 . TYR F  2 60  ? 6.267   -39.918  -6.675  1.000 46.074  0 60  TYR FFF CD2 1 ? 22 
ATOM   7127  C CE1 . TYR F  2 60  ? 6.007   -40.932  -9.232  1.000 45.808  0 60  TYR FFF CE1 1 ? 22 
ATOM   7128  C CE2 . TYR F  2 60  ? 5.808   -41.214  -6.855  1.000 44.694  0 60  TYR FFF CE2 1 ? 22 
ATOM   7129  C CZ  . TYR F  2 60  ? 5.685   -41.723  -8.139  1.000 45.474  0 60  TYR FFF CZ  1 ? 22 
ATOM   7130  O OH  . TYR F  2 60  ? 5.243   -42.988  -8.360  1.000 43.389  0 60  TYR FFF OH  1 ? 22 
ATOM   7131  N N   . GLY F  2 61  ? 9.262   -35.524  -8.890  1.000 49.938  0 61  GLY FFF N   1 ? 22 
ATOM   7132  C CA  . GLY F  2 61  ? 9.416   -34.061  -9.003  1.000 51.739  0 61  GLY FFF CA  1 ? 22 
ATOM   7133  C C   . GLY F  2 61  ? 8.157   -33.367  -8.546  1.000 55.655  0 61  GLY FFF C   1 ? 22 
ATOM   7134  O O   . GLY F  2 61  ? 7.080   -33.927  -8.685  1.000 57.085  0 61  GLY FFF O   1 ? 22 
ATOM   7135  N N   . GLU F  2 62  ? 8.300   -32.161  -8.015  1.000 62.402  0 62  GLU FFF N   1 ? 22 
ATOM   7136  C CA  . GLU F  2 62  ? 7.228   -31.332  -7.426  1.000 66.774  0 62  GLU FFF CA  1 ? 22 
ATOM   7137  C C   . GLU F  2 62  ? 6.043   -31.269  -8.394  1.000 66.270  0 62  GLU FFF C   1 ? 22 
ATOM   7138  O O   . GLU F  2 62  ? 4.902   -31.465  -7.962  1.000 66.009  0 62  GLU FFF O   1 ? 22 
ATOM   7139  C CB  . GLU F  2 62  ? 7.812   -29.938  -7.175  1.000 73.289  0 62  GLU FFF CB  1 ? 22 
ATOM   7140  C CG  . GLU F  2 62  ? 6.827   -28.948  -6.609  1.000 82.486  0 62  GLU FFF CG  1 ? 22 
ATOM   7141  C CD  . GLU F  2 62  ? 6.278   -29.335  -5.251  1.000 88.407  0 62  GLU FFF CD  1 ? 22 
ATOM   7142  O OE1 . GLU F  2 62  ? 6.810   -30.285  -4.565  1.000 90.906  0 62  GLU FFF OE1 1 ? 22 
ATOM   7143  O OE2 . GLU F  2 62  ? 5.357   -28.601  -4.811  1.000 91.233  0 62  GLU FFF OE2 1 ? 22 
ATOM   7144  N N   . SER F  2 63  ? 6.324   -31.000  -9.660  1.000 64.957  0 63  SER FFF N   1 ? 22 
ATOM   7145  C CA  . SER F  2 63  ? 5.304   -30.568  -10.652 1.000 64.195  0 63  SER FFF CA  1 ? 22 
ATOM   7146  C C   . SER F  2 63  ? 4.544   -31.775  -11.192 1.000 60.236  0 63  SER FFF C   1 ? 22 
ATOM   7147  O O   . SER F  2 63  ? 3.558   -31.553  -11.857 1.000 60.473  0 63  SER FFF O   1 ? 22 
ATOM   7148  C CB  . SER F  2 63  ? 5.953   -29.768  -11.758 1.000 64.259  0 63  SER FFF CB  1 ? 22 
ATOM   7149  O OG  . SER F  2 63  ? 6.951   -30.540  -12.411 1.000 64.785  0 63  SER FFF OG  1 ? 22 
ATOM   7150  N N   . VAL F  2 64  ? 4.982   -33.007  -10.929 1.000 58.296  0 64  VAL FFF N   1 ? 22 
ATOM   7151  C CA  . VAL F  2 64  ? 4.272   -34.220  -11.416 1.000 56.906  0 64  VAL FFF CA  1 ? 22 
ATOM   7152  C C   . VAL F  2 64  ? 3.693   -35.002  -10.247 1.000 57.733  0 64  VAL FFF C   1 ? 22 
ATOM   7153  O O   . VAL F  2 64  ? 2.890   -35.902  -10.525 1.000 58.434  0 64  VAL FFF O   1 ? 22 
ATOM   7154  C CB  . VAL F  2 64  ? 5.167   -35.117  -12.287 1.000 55.364  0 64  VAL FFF CB  1 ? 22 
ATOM   7155  C CG1 . VAL F  2 64  ? 5.732   -34.355  -13.470 1.000 55.992  0 64  VAL FFF CG1 1 ? 22 
ATOM   7156  C CG2 . VAL F  2 64  ? 6.275   -35.782  -11.492 1.000 55.052  0 64  VAL FFF CG2 1 ? 22 
ATOM   7157  N N   . LYS F  2 65  ? 4.081   -34.698  -9.007  1.000 61.433  0 65  LYS FFF N   1 ? 22 
ATOM   7158  C CA  . LYS F  2 65  ? 3.592   -35.410  -7.795  1.000 64.715  0 65  LYS FFF CA  1 ? 22 
ATOM   7159  C C   . LYS F  2 65  ? 2.059   -35.479  -7.861  1.000 63.486  0 65  LYS FFF C   1 ? 22 
ATOM   7160  O O   . LYS F  2 65  ? 1.447   -34.444  -8.127  1.000 64.215  0 65  LYS FFF O   1 ? 22 
ATOM   7161  C CB  . LYS F  2 65  ? 4.094   -34.727  -6.519  1.000 71.708  0 65  LYS FFF CB  1 ? 22 
ATOM   7162  C CG  . LYS F  2 65  ? 4.479   -35.707  -5.405  1.000 76.886  0 65  LYS FFF CG  1 ? 22 
ATOM   7163  C CD  . LYS F  2 65  ? 4.454   -35.124  -3.992  1.000 83.061  0 65  LYS FFF CD  1 ? 22 
ATOM   7164  C CE  . LYS F  2 65  ? 3.769   -35.978  -2.924  1.000 86.114  0 65  LYS FFF CE  1 ? 22 
ATOM   7165  N NZ  . LYS F  2 65  ? 2.791   -35.185  -2.127  1.000 87.704  0 65  LYS FFF NZ  1 ? 22 
ATOM   7166  N N   . GLY F  2 66  ? 1.485   -36.673  -7.689  1.000 61.249  0 66  GLY FFF N   1 ? 22 
ATOM   7167  C CA  . GLY F  2 66  ? 0.036   -36.928  -7.708  1.000 61.593  0 66  GLY FFF CA  1 ? 22 
ATOM   7168  C C   . GLY F  2 66  ? -0.485  -37.327  -9.089  1.000 61.264  0 66  GLY FFF C   1 ? 22 
ATOM   7169  O O   . GLY F  2 66  ? -1.493  -38.032  -9.139  1.000 64.454  0 66  GLY FFF O   1 ? 22 
ATOM   7170  N N   . ARG F  2 67  ? 0.153   -36.888  -10.177 1.000 57.873  0 67  ARG FFF N   1 ? 22 
ATOM   7171  C CA  . ARG F  2 67  ? -0.339  -37.135  -11.561 1.000 58.359  0 67  ARG FFF CA  1 ? 22 
ATOM   7172  C C   . ARG F  2 67  ? 0.386   -38.329  -12.199 1.000 55.081  0 67  ARG FFF C   1 ? 22 
ATOM   7173  O O   . ARG F  2 67  ? -0.226  -38.999  -13.046 1.000 54.588  0 67  ARG FFF O   1 ? 22 
ATOM   7174  C CB  . ARG F  2 67  ? -0.171  -35.881  -12.418 1.000 58.379  0 67  ARG FFF CB  1 ? 22 
ATOM   7175  C CG  . ARG F  2 67  ? -1.002  -34.699  -11.929 1.000 59.267  0 67  ARG FFF CG  1 ? 22 
ATOM   7176  C CD  . ARG F  2 67  ? -0.941  -33.489  -12.856 1.000 59.127  0 67  ARG FFF CD  1 ? 22 
ATOM   7177  N NE  . ARG F  2 67  ? 0.432   -33.041  -13.083 1.000 56.829  0 67  ARG FFF NE  1 ? 22 
ATOM   7178  C CZ  . ARG F  2 67  ? 1.055   -33.050  -14.252 1.000 56.088  0 67  ARG FFF CZ  1 ? 22 
ATOM   7179  N NH1 . ARG F  2 67  ? 0.444   -33.470  -15.341 1.000 57.564  0 67  ARG FFF NH1 1 ? 22 
ATOM   7180  N NH2 . ARG F  2 67  ? 2.298   -32.631  -14.335 1.000 56.114  0 67  ARG FFF NH2 1 ? 22 
ATOM   7181  N N   . PHE F  2 68  ? 1.651   -38.555  -11.834 1.000 53.461  0 68  PHE FFF N   1 ? 22 
ATOM   7182  C CA  . PHE F  2 68  ? 2.541   -39.562  -12.455 1.000 51.073  0 68  PHE FFF CA  1 ? 22 
ATOM   7183  C C   . PHE F  2 68  ? 2.830   -40.673  -11.441 1.000 52.054  0 68  PHE FFF C   1 ? 22 
ATOM   7184  O O   . PHE F  2 68  ? 3.007   -40.391  -10.263 1.000 54.867  0 68  PHE FFF O   1 ? 22 
ATOM   7185  C CB  . PHE F  2 68  ? 3.841   -38.918  -12.931 1.000 49.702  0 68  PHE FFF CB  1 ? 22 
ATOM   7186  C CG  . PHE F  2 68  ? 3.766   -37.993  -14.120 1.000 48.254  0 68  PHE FFF CG  1 ? 22 
ATOM   7187  C CD1 . PHE F  2 68  ? 2.561   -37.516  -14.612 1.000 51.029  0 68  PHE FFF CD1 1 ? 22 
ATOM   7188  C CD2 . PHE F  2 68  ? 4.931   -37.555  -14.719 1.000 47.033  0 68  PHE FFF CD2 1 ? 22 
ATOM   7189  C CE1 . PHE F  2 68  ? 2.521   -36.639  -15.683 1.000 52.109  0 68  PHE FFF CE1 1 ? 22 
ATOM   7190  C CE2 . PHE F  2 68  ? 4.897   -36.680  -15.795 1.000 48.512  0 68  PHE FFF CE2 1 ? 22 
ATOM   7191  C CZ  . PHE F  2 68  ? 3.690   -36.226  -16.281 1.000 50.675  0 68  PHE FFF CZ  1 ? 22 
ATOM   7192  N N   . THR F  2 69  ? 2.878   -41.920  -11.901 1.000 51.526  0 69  THR FFF N   1 ? 22 
ATOM   7193  C CA  . THR F  2 69  ? 3.212   -43.098  -11.078 1.000 49.157  0 69  THR FFF CA  1 ? 22 
ATOM   7194  C C   . THR F  2 69  ? 4.338   -43.857  -11.774 1.000 48.484  0 69  THR FFF C   1 ? 22 
ATOM   7195  O O   . THR F  2 69  ? 4.164   -44.232  -12.955 1.000 46.572  0 69  THR FFF O   1 ? 22 
ATOM   7196  C CB  . THR F  2 69  ? 2.000   -43.999  -10.860 1.000 51.475  0 69  THR FFF CB  1 ? 22 
ATOM   7197  O OG1 . THR F  2 69  ? 0.979   -43.203  -10.262 1.000 54.037  0 69  THR FFF OG1 1 ? 22 
ATOM   7198  C CG2 . THR F  2 69  ? 2.310   -45.189  -9.976  1.000 52.302  0 69  THR FFF CG2 1 ? 22 
ATOM   7199  N N   . ILE F  2 70  ? 5.464   -44.027  -11.081 1.000 45.621  0 70  ILE FFF N   1 ? 22 
ATOM   7200  C CA  . ILE F  2 70  ? 6.584   -44.874  -11.564 1.000 43.247  0 70  ILE FFF CA  1 ? 22 
ATOM   7201  C C   . ILE F  2 70  ? 6.394   -46.272  -10.954 1.000 43.688  0 70  ILE FFF C   1 ? 22 
ATOM   7202  O O   . ILE F  2 70  ? 5.924   -46.367  -9.810  1.000 44.888  0 70  ILE FFF O   1 ? 22 
ATOM   7203  C CB  . ILE F  2 70  ? 7.951   -44.243  -11.231 1.000 42.914  0 70  ILE FFF CB  1 ? 22 
ATOM   7204  C CG1 . ILE F  2 70  ? 9.080   -44.936  -12.005 1.000 41.679  0 70  ILE FFF CG1 1 ? 22 
ATOM   7205  C CG2 . ILE F  2 70  ? 8.213   -44.232  -9.727  1.000 43.942  0 70  ILE FFF CG2 1 ? 22 
ATOM   7206  C CD1 . ILE F  2 70  ? 10.426  -44.259  -11.866 1.000 41.849  0 70  ILE FFF CD1 1 ? 22 
ATOM   7207  N N   . SER F  2 71  ? 6.704   -47.311  -11.715 1.000 41.408  0 71  SER FFF N   1 ? 22 
ATOM   7208  C CA  . SER F  2 71  ? 6.623   -48.724  -11.292 1.000 42.532  0 71  SER FFF CA  1 ? 22 
ATOM   7209  C C   . SER F  2 71  ? 7.668   -49.515  -12.094 1.000 44.193  0 71  SER FFF C   1 ? 22 
ATOM   7210  O O   . SER F  2 71  ? 8.191   -48.996  -13.124 1.000 43.645  0 71  SER FFF O   1 ? 22 
ATOM   7211  C CB  . SER F  2 71  ? 5.230   -49.250  -11.475 1.000 43.562  0 71  SER FFF CB  1 ? 22 
ATOM   7212  O OG  . SER F  2 71  ? 4.840   -49.245  -12.846 1.000 43.757  0 71  SER FFF OG  1 ? 22 
ATOM   7213  N N   . ARG F  2 72  ? 8.006   -50.711  -11.621 1.000 43.748  0 72  ARG FFF N   1 ? 22 
ATOM   7214  C CA  . ARG F  2 72  ? 9.025   -51.546  -12.301 1.000 44.212  0 72  ARG FFF CA  1 ? 22 
ATOM   7215  C C   . ARG F  2 72  ? 8.502   -52.975  -12.335 1.000 44.705  0 72  ARG FFF C   1 ? 22 
ATOM   7216  O O   . ARG F  2 72  ? 7.757   -53.360  -11.424 1.000 42.709  0 72  ARG FFF O   1 ? 22 
ATOM   7217  C CB  . ARG F  2 72  ? 10.393  -51.441  -11.617 1.000 44.643  0 72  ARG FFF CB  1 ? 22 
ATOM   7218  C CG  . ARG F  2 72  ? 10.410  -51.922  -10.178 1.000 46.135  0 72  ARG FFF CG  1 ? 22 
ATOM   7219  C CD  . ARG F  2 72  ? 11.739  -51.628  -9.497  1.000 47.438  0 72  ARG FFF CD  1 ? 22 
ATOM   7220  N NE  . ARG F  2 72  ? 12.867  -52.257  -10.176 1.000 45.893  0 72  ARG FFF NE  1 ? 22 
ATOM   7221  C CZ  . ARG F  2 72  ? 14.112  -51.782  -10.201 1.000 42.979  0 72  ARG FFF CZ  1 ? 22 
ATOM   7222  N NH1 . ARG F  2 72  ? 14.419  -50.671  -9.561  1.000 42.591  0 72  ARG FFF NH1 1 ? 22 
ATOM   7223  N NH2 . ARG F  2 72  ? 15.057  -52.438  -10.869 1.000 44.743  0 72  ARG FFF NH2 1 ? 22 
ATOM   7224  N N   . ASP F  2 73  ? 8.857   -53.690  -13.397 1.000 45.960  0 73  ASP FFF N   1 ? 22 
ATOM   7225  C CA  . ASP F  2 73  ? 8.613   -55.139  -13.536 1.000 48.192  0 73  ASP FFF CA  1 ? 22 
ATOM   7226  C C   . ASP F  2 73  ? 9.970   -55.789  -13.818 1.000 46.958  0 73  ASP FFF C   1 ? 22 
ATOM   7227  O O   . ASP F  2 73  ? 10.423  -55.747  -14.958 1.000 46.653  0 73  ASP FFF O   1 ? 22 
ATOM   7228  C CB  . ASP F  2 73  ? 7.554   -55.382  -14.611 1.000 49.212  0 73  ASP FFF CB  1 ? 22 
ATOM   7229  C CG  . ASP F  2 73  ? 7.181   -56.841  -14.719 1.000 51.771  0 73  ASP FFF CG  1 ? 22 
ATOM   7230  O OD1 . ASP F  2 73  ? 7.913   -57.682  -14.131 1.000 52.709  0 73  ASP FFF OD1 1 ? 22 
ATOM   7231  O OD2 . ASP F  2 73  ? 6.148   -57.124  -15.391 1.000 51.192  0 73  ASP FFF OD2 1 ? 22 
ATOM   7232  N N   . ASN F  2 74  ? 10.606  -56.307  -12.783 1.000 45.468  0 74  ASN FFF N   1 ? 22 
ATOM   7233  C CA  . ASN F  2 74  ? 11.953  -56.910  -12.854 1.000 45.607  0 74  ASN FFF CA  1 ? 22 
ATOM   7234  C C   . ASN F  2 74  ? 11.946  -58.093  -13.837 1.000 47.910  0 74  ASN FFF C   1 ? 22 
ATOM   7235  O O   . ASN F  2 74  ? 12.921  -58.232  -14.568 1.000 49.122  0 74  ASN FFF O   1 ? 22 
ATOM   7236  C CB  . ASN F  2 74  ? 12.426  -57.268  -11.445 1.000 45.521  0 74  ASN FFF CB  1 ? 22 
ATOM   7237  C CG  . ASN F  2 74  ? 12.902  -56.048  -10.679 1.000 45.225  0 74  ASN FFF CG  1 ? 22 
ATOM   7238  O OD1 . ASN F  2 74  ? 12.818  -54.905  -11.145 1.000 42.931  0 74  ASN FFF OD1 1 ? 22 
ATOM   7239  N ND2 . ASN F  2 74  ? 13.433  -56.285  -9.502  1.000 45.961  0 74  ASN FFF ND2 1 ? 22 
ATOM   7240  N N   . ALA F  2 75  ? 10.861  -58.863  -13.920 1.000 47.650  0 75  ALA FFF N   1 ? 22 
ATOM   7241  C CA  . ALA F  2 75  ? 10.747  -60.025  -14.834 1.000 48.341  0 75  ALA FFF CA  1 ? 22 
ATOM   7242  C C   . ALA F  2 75  ? 10.861  -59.559  -16.293 1.000 47.492  0 75  ALA FFF C   1 ? 22 
ATOM   7243  O O   . ALA F  2 75  ? 11.248  -60.379  -17.129 1.000 47.975  0 75  ALA FFF O   1 ? 22 
ATOM   7244  C CB  . ALA F  2 75  ? 9.449   -60.773  -14.597 1.000 48.543  0 75  ALA FFF CB  1 ? 22 
ATOM   7245  N N   . LYS F  2 76  ? 10.546  -58.296  -16.596 1.000 46.784  0 76  LYS FFF N   1 ? 22 
ATOM   7246  C CA  . LYS F  2 76  ? 10.581  -57.750  -17.978 1.000 45.694  0 76  LYS FFF CA  1 ? 22 
ATOM   7247  C C   . LYS F  2 76  ? 11.677  -56.700  -18.153 1.000 43.618  0 76  LYS FFF C   1 ? 22 
ATOM   7248  O O   . LYS F  2 76  ? 11.670  -56.037  -19.203 1.000 42.278  0 76  LYS FFF O   1 ? 22 
ATOM   7249  C CB  . LYS F  2 76  ? 9.239   -57.115  -18.299 1.000 46.954  0 76  LYS FFF CB  1 ? 22 
ATOM   7250  C CG  . LYS F  2 76  ? 8.062   -58.055  -18.179 1.000 51.527  0 76  LYS FFF CG  1 ? 22 
ATOM   7251  C CD  . LYS F  2 76  ? 6.817   -57.492  -18.811 1.000 51.531  0 76  LYS FFF CD  1 ? 22 
ATOM   7252  C CE  . LYS F  2 76  ? 5.729   -58.523  -18.898 1.000 55.654  0 76  LYS FFF CE  1 ? 22 
ATOM   7253  N NZ  . LYS F  2 76  ? 4.533   -57.878  -19.462 1.000 63.336  0 76  LYS FFF NZ  1 ? 22 
ATOM   7254  N N   . ASN F  2 77  ? 12.558  -56.515  -17.164 1.000 42.125  0 77  ASN FFF N   1 ? 22 
ATOM   7255  C CA  . ASN F  2 77  ? 13.644  -55.503  -17.260 1.000 41.173  0 77  ASN FFF CA  1 ? 22 
ATOM   7256  C C   . ASN F  2 77  ? 13.047  -54.136  -17.618 1.000 40.689  0 77  ASN FFF C   1 ? 22 
ATOM   7257  O O   . ASN F  2 77  ? 13.695  -53.382  -18.363 1.000 43.149  0 77  ASN FFF O   1 ? 22 
ATOM   7258  C CB  . ASN F  2 77  ? 14.670  -55.907  -18.327 1.000 41.333  0 77  ASN FFF CB  1 ? 22 
ATOM   7259  C CG  . ASN F  2 77  ? 15.777  -56.761  -17.771 1.000 42.456  0 77  ASN FFF CG  1 ? 22 
ATOM   7260  O OD1 . ASN F  2 77  ? 15.533  -57.615  -16.927 1.000 40.688  0 77  ASN FFF OD1 1 ? 22 
ATOM   7261  N ND2 . ASN F  2 77  ? 17.003  -56.496  -18.213 1.000 44.738  0 77  ASN FFF ND2 1 ? 22 
ATOM   7262  N N   . THR F  2 78  ? 11.853  -53.821  -17.130 1.000 37.471  0 78  THR FFF N   1 ? 22 
ATOM   7263  C CA  . THR F  2 78  ? 11.122  -52.623  -17.579 1.000 37.816  0 78  THR FFF CA  1 ? 22 
ATOM   7264  C C   . THR F  2 78  ? 10.725  -51.748  -16.385 1.000 38.289  0 78  THR FFF C   1 ? 22 
ATOM   7265  O O   . THR F  2 78  ? 10.264  -52.272  -15.337 1.000 37.516  0 78  THR FFF O   1 ? 22 
ATOM   7266  C CB  . THR F  2 78  ? 9.945   -53.029  -18.470 1.000 39.913  0 78  THR FFF CB  1 ? 22 
ATOM   7267  O OG1 . THR F  2 78  ? 10.468  -53.713  -19.609 1.000 40.014  0 78  THR FFF OG1 1 ? 22 
ATOM   7268  C CG2 . THR F  2 78  ? 9.142   -51.844  -18.947 1.000 40.553  0 78  THR FFF CG2 1 ? 22 
ATOM   7269  N N   . VAL F  2 79  ? 10.927  -50.440  -16.547 1.000 39.005  0 79  VAL FFF N   1 ? 22 
ATOM   7270  C CA  . VAL F  2 79  ? 10.372  -49.374  -15.669 1.000 38.877  0 79  VAL FFF CA  1 ? 22 
ATOM   7271  C C   . VAL F  2 79  ? 9.286   -48.648  -16.476 1.000 40.533  0 79  VAL FFF C   1 ? 22 
ATOM   7272  O O   . VAL F  2 79  ? 9.452   -48.472  -17.693 1.000 40.847  0 79  VAL FFF O   1 ? 22 
ATOM   7273  C CB  . VAL F  2 79  ? 11.483  -48.439  -15.159 1.000 36.994  0 79  VAL FFF CB  1 ? 22 
ATOM   7274  C CG1 . VAL F  2 79  ? 12.208  -47.744  -16.298 1.000 36.876  0 79  VAL FFF CG1 1 ? 22 
ATOM   7275  C CG2 . VAL F  2 79  ? 10.958  -47.440  -14.151 1.000 37.289  0 79  VAL FFF CG2 1 ? 22 
ATOM   7276  N N   . TYR F  2 80  ? 8.190   -48.293  -15.819 1.000 43.693  0 80  TYR FFF N   1 ? 22 
ATOM   7277  C CA  . TYR F  2 80  ? 7.006   -47.634  -16.425 1.000 44.519  0 80  TYR FFF CA  1 ? 22 
ATOM   7278  C C   . TYR F  2 80  ? 6.804   -46.264  -15.784 1.000 43.652  0 80  TYR FFF C   1 ? 22 
ATOM   7279  O O   . TYR F  2 80  ? 7.112   -46.091  -14.590 1.000 42.465  0 80  TYR FFF O   1 ? 22 
ATOM   7280  C CB  . TYR F  2 80  ? 5.752   -48.495  -16.228 1.000 44.312  0 80  TYR FFF CB  1 ? 22 
ATOM   7281  C CG  . TYR F  2 80  ? 5.819   -49.847  -16.876 1.000 43.103  0 80  TYR FFF CG  1 ? 22 
ATOM   7282  C CD1 . TYR F  2 80  ? 5.639   -49.995  -18.243 1.000 45.220  0 80  TYR FFF CD1 1 ? 22 
ATOM   7283  C CD2 . TYR F  2 80  ? 6.110   -50.977  -16.139 1.000 43.082  0 80  TYR FFF CD2 1 ? 22 
ATOM   7284  C CE1 . TYR F  2 80  ? 5.683   -51.239  -18.855 1.000 44.528  0 80  TYR FFF CE1 1 ? 22 
ATOM   7285  C CE2 . TYR F  2 80  ? 6.159   -52.230  -16.728 1.000 43.732  0 80  TYR FFF CE2 1 ? 22 
ATOM   7286  C CZ  . TYR F  2 80  ? 5.931   -52.361  -18.084 1.000 43.809  0 80  TYR FFF CZ  1 ? 22 
ATOM   7287  O OH  . TYR F  2 80  ? 5.990   -53.582  -18.666 1.000 45.714  0 80  TYR FFF OH  1 ? 22 
ATOM   7288  N N   . LEU F  2 81  ? 6.309   -45.314  -16.573 1.000 45.511  0 81  LEU FFF N   1 ? 22 
ATOM   7289  C CA  . LEU F  2 81  ? 5.808   -44.011  -16.067 1.000 47.563  0 81  LEU FFF CA  1 ? 22 
ATOM   7290  C C   . LEU F  2 81  ? 4.369   -43.817  -16.569 1.000 48.500  0 81  LEU FFF C   1 ? 22 
ATOM   7291  O O   . LEU F  2 81  ? 4.192   -43.567  -17.763 1.000 47.945  0 81  LEU FFF O   1 ? 22 
ATOM   7292  C CB  . LEU F  2 81  ? 6.735   -42.875  -16.514 1.000 46.637  0 81  LEU FFF CB  1 ? 22 
ATOM   7293  C CG  . LEU F  2 81  ? 6.489   -41.527  -15.843 1.000 46.894  0 81  LEU FFF CG  1 ? 22 
ATOM   7294  C CD1 . LEU F  2 81  ? 6.871   -41.567  -14.377 1.000 47.272  0 81  LEU FFF CD1 1 ? 22 
ATOM   7295  C CD2 . LEU F  2 81  ? 7.248   -40.432  -16.559 1.000 48.534  0 81  LEU FFF CD2 1 ? 22 
ATOM   7296  N N   . GLN F  2 82  ? 3.398   -43.988  -15.670 1.000 48.830  0 82  GLN FFF N   1 ? 22 
ATOM   7297  C CA  . GLN F  2 82  ? 1.969   -43.686  -15.893 1.000 51.429  0 82  GLN FFF CA  1 ? 22 
ATOM   7298  C C   . GLN F  2 82  ? 1.834   -42.176  -15.731 1.000 53.369  0 82  GLN FFF C   1 ? 22 
ATOM   7299  O O   . GLN F  2 82  ? 2.163   -41.682  -14.655 1.000 54.795  0 82  GLN FFF O   1 ? 22 
ATOM   7300  C CB  . GLN F  2 82  ? 1.098   -44.498  -14.929 1.000 51.353  0 82  GLN FFF CB  1 ? 22 
ATOM   7301  C CG  . GLN F  2 82  ? -0.388  -44.414  -15.222 1.000 55.032  0 82  GLN FFF CG  1 ? 22 
ATOM   7302  C CD  . GLN F  2 82  ? -0.713  -44.776  -16.650 1.000 58.135  0 82  GLN FFF CD  1 ? 22 
ATOM   7303  O OE1 . GLN F  2 82  ? -0.254  -45.792  -17.186 1.000 59.125  0 82  GLN FFF OE1 1 ? 22 
ATOM   7304  N NE2 . GLN F  2 82  ? -1.496  -43.923  -17.292 1.000 60.174  0 82  GLN FFF NE2 1 ? 22 
ATOM   7305  N N   . MET F  2 83  ? 1.479   -41.468  -16.799 1.000 55.347  0 83  MET FFF N   1 ? 22 
ATOM   7306  C CA  . MET F  2 83  ? 1.312   -39.995  -16.778 1.000 57.565  0 83  MET FFF CA  1 ? 22 
ATOM   7307  C C   . MET F  2 83  ? -0.174  -39.710  -16.990 1.000 58.129  0 83  MET FFF C   1 ? 22 
ATOM   7308  O O   . MET F  2 83  ? -0.673  -40.001  -18.075 1.000 59.061  0 83  MET FFF O   1 ? 22 
ATOM   7309  C CB  . MET F  2 83  ? 2.152   -39.314  -17.861 1.000 60.208  0 83  MET FFF CB  1 ? 22 
ATOM   7310  C CG  . MET F  2 83  ? 3.628   -39.708  -17.848 1.000 59.929  0 83  MET FFF CG  1 ? 22 
ATOM   7311  S SD  . MET F  2 83  ? 4.602   -38.865  -19.112 1.000 63.772  0 83  MET FFF SD  1 ? 22 
ATOM   7312  C CE  . MET F  2 83  ? 3.953   -39.575  -20.622 1.000 64.220  0 83  MET FFF CE  1 ? 22 
ATOM   7313  N N   . ASN F  2 84  ? -0.852  -39.215  -15.954 1.000 58.883  0 84  ASN FFF N   1 ? 22 
ATOM   7314  C CA  . ASN F  2 84  ? -2.296  -38.878  -15.988 1.000 60.076  0 84  ASN FFF CA  1 ? 22 
ATOM   7315  C C   . ASN F  2 84  ? -2.467  -37.357  -15.991 1.000 60.922  0 84  ASN FFF C   1 ? 22 
ATOM   7316  O O   . ASN F  2 84  ? -1.516  -36.647  -15.576 1.000 58.542  0 84  ASN FFF O   1 ? 22 
ATOM   7317  C CB  . ASN F  2 84  ? -3.030  -39.541  -14.826 1.000 61.448  0 84  ASN FFF CB  1 ? 22 
ATOM   7318  C CG  . ASN F  2 84  ? -2.996  -41.048  -14.916 1.000 61.463  0 84  ASN FFF CG  1 ? 22 
ATOM   7319  O OD1 . ASN F  2 84  ? -3.039  -41.612  -16.006 1.000 61.552  0 84  ASN FFF OD1 1 ? 22 
ATOM   7320  N ND2 . ASN F  2 84  ? -2.915  -41.706  -13.775 1.000 62.753  0 84  ASN FFF ND2 1 ? 22 
ATOM   7321  N N   . ARG F  2 85  ? -3.617  -36.887  -16.482 1.000 64.202  0 85  ARG FFF N   1 ? 22 
ATOM   7322  C CA  . ARG F  2 85  ? -4.027  -35.466  -16.425 1.000 68.012  0 85  ARG FFF CA  1 ? 22 
ATOM   7323  C C   . ARG F  2 85  ? -2.863  -34.627  -16.960 1.000 65.339  0 85  ARG FFF C   1 ? 22 
ATOM   7324  O O   . ARG F  2 85  ? -2.389  -33.711  -16.249 1.000 65.096  0 85  ARG FFF O   1 ? 22 
ATOM   7325  C CB  . ARG F  2 85  ? -4.433  -35.149  -14.970 1.000 71.242  0 85  ARG FFF CB  1 ? 22 
ATOM   7326  C CG  . ARG F  2 85  ? -5.659  -35.914  -14.527 1.000 76.734  0 85  ARG FFF CG  1 ? 22 
ATOM   7327  C CD  . ARG F  2 85  ? -6.181  -35.435  -13.174 1.000 82.090  0 85  ARG FFF CD  1 ? 22 
ATOM   7328  N NE  . ARG F  2 85  ? -5.203  -35.595  -12.100 1.000 82.454  0 85  ARG FFF NE  1 ? 22 
ATOM   7329  C CZ  . ARG F  2 85  ? -4.775  -36.765  -11.605 1.000 82.191  0 85  ARG FFF CZ  1 ? 22 
ATOM   7330  N NH1 . ARG F  2 85  ? -5.194  -37.925  -12.097 1.000 81.978  0 85  ARG FFF NH1 1 ? 22 
ATOM   7331  N NH2 . ARG F  2 85  ? -3.916  -36.776  -10.600 1.000 82.214  0 85  ARG FFF NH2 1 ? 22 
ATOM   7332  N N   . LEU F  2 86  ? -2.416  -34.950  -18.172 1.000 63.231  0 86  LEU FFF N   1 ? 22 
ATOM   7333  C CA  . LEU F  2 86  ? -1.260  -34.284  -18.814 1.000 63.386  0 86  LEU FFF CA  1 ? 22 
ATOM   7334  C C   . LEU F  2 86  ? -1.629  -32.843  -19.169 1.000 67.503  0 86  LEU FFF C   1 ? 22 
ATOM   7335  O O   . LEU F  2 86  ? -2.773  -32.600  -19.625 1.000 69.587  0 86  LEU FFF O   1 ? 22 
ATOM   7336  C CB  . LEU F  2 86  ? -0.852  -35.084  -20.051 1.000 61.835  0 86  LEU FFF CB  1 ? 22 
ATOM   7337  C CG  . LEU F  2 86  ? -0.061  -36.353  -19.750 1.000 59.575  0 86  LEU FFF CG  1 ? 22 
ATOM   7338  C CD1 . LEU F  2 86  ? -0.024  -37.265  -20.963 1.000 59.781  0 86  LEU FFF CD1 1 ? 22 
ATOM   7339  C CD2 . LEU F  2 86  ? 1.346   -36.020  -19.283 1.000 58.472  0 86  LEU FFF CD2 1 ? 22 
ATOM   7340  N N   . LYS F  2 87  ? -0.670  -31.934  -18.969 1.000 68.989  0 87  LYS FFF N   1 ? 22 
ATOM   7341  C CA  . LYS F  2 87  ? -0.792  -30.486  -19.260 1.000 71.035  0 87  LYS FFF CA  1 ? 22 
ATOM   7342  C C   . LYS F  2 87  ? 0.225   -30.145  -20.335 1.000 69.618  0 87  LYS FFF C   1 ? 22 
ATOM   7343  O O   . LYS F  2 87  ? 1.205   -30.869  -20.501 1.000 67.699  0 87  LYS FFF O   1 ? 22 
ATOM   7344  C CB  . LYS F  2 87  ? -0.552  -29.677  -17.987 1.000 73.526  0 87  LYS FFF CB  1 ? 22 
ATOM   7345  C CG  . LYS F  2 87  ? -1.183  -30.271  -16.728 1.000 75.050  0 87  LYS FFF CG  1 ? 22 
ATOM   7346  C CD  . LYS F  2 87  ? -1.336  -29.306  -15.536 1.000 78.201  0 87  LYS FFF CD  1 ? 22 
ATOM   7347  C CE  . LYS F  2 87  ? -0.448  -29.574  -14.322 1.000 76.905  0 87  LYS FFF CE  1 ? 22 
ATOM   7348  N NZ  . LYS F  2 87  ? -1.166  -29.417  -13.027 1.000 80.179  0 87  LYS FFF NZ  1 ? 22 
ATOM   7349  N N   . PRO F  2 88  ? 0.013   -29.066  -21.128 1.000 69.662  0 88  PRO FFF N   1 ? 22 
ATOM   7350  C CA  . PRO F  2 88  ? 1.010   -28.637  -22.114 1.000 68.624  0 88  PRO FFF CA  1 ? 22 
ATOM   7351  C C   . PRO F  2 88  ? 2.435   -28.501  -21.557 1.000 66.490  0 88  PRO FFF C   1 ? 22 
ATOM   7352  O O   . PRO F  2 88  ? 3.330   -28.878  -22.294 1.000 66.026  0 88  PRO FFF O   1 ? 22 
ATOM   7353  C CB  . PRO F  2 88  ? 0.428   -27.302  -22.582 1.000 71.974  0 88  PRO FFF CB  1 ? 22 
ATOM   7354  C CG  . PRO F  2 88  ? -1.061  -27.569  -22.541 1.000 72.534  0 88  PRO FFF CG  1 ? 22 
ATOM   7355  C CD  . PRO F  2 88  ? -1.232  -28.292  -21.219 1.000 70.897  0 88  PRO FFF CD  1 ? 22 
ATOM   7356  N N   . GLU F  2 89  ? 2.602   -28.059  -20.297 1.000 68.014  0 89  GLU FFF N   1 ? 22 
ATOM   7357  C CA  . GLU F  2 89  ? 3.941   -27.902  -19.642 1.000 68.386  0 89  GLU FFF CA  1 ? 22 
ATOM   7358  C C   . GLU F  2 89  ? 4.652   -29.255  -19.464 1.000 63.183  0 89  GLU FFF C   1 ? 22 
ATOM   7359  O O   . GLU F  2 89  ? 5.808   -29.226  -19.034 1.000 61.916  0 89  GLU FFF O   1 ? 22 
ATOM   7360  C CB  . GLU F  2 89  ? 3.880   -27.291  -18.236 1.000 72.577  0 89  GLU FFF CB  1 ? 22 
ATOM   7361  C CG  . GLU F  2 89  ? 3.010   -26.060  -18.104 1.000 83.016  0 89  GLU FFF CG  1 ? 22 
ATOM   7362  C CD  . GLU F  2 89  ? 1.531   -26.343  -17.856 1.000 87.600  0 89  GLU FFF CD  1 ? 22 
ATOM   7363  O OE1 . GLU F  2 89  ? 1.246   -27.238  -17.026 1.000 91.239  0 89  GLU FFF OE1 1 ? 22 
ATOM   7364  O OE2 . GLU F  2 89  ? 0.660   -25.692  -18.498 1.000 88.614  0 89  GLU FFF OE2 1 ? 22 
ATOM   7365  N N   . ASP F  2 90  ? 3.975   -30.383  -19.709 1.000 61.957  0 90  ASP FFF N   1 ? 22 
ATOM   7366  C CA  . ASP F  2 90  ? 4.562   -31.747  -19.607 1.000 59.703  0 90  ASP FFF CA  1 ? 22 
ATOM   7367  C C   . ASP F  2 90  ? 5.217   -32.142  -20.937 1.000 58.022  0 90  ASP FFF C   1 ? 22 
ATOM   7368  O O   . ASP F  2 90  ? 5.919   -33.178  -20.966 1.000 58.054  0 90  ASP FFF O   1 ? 22 
ATOM   7369  C CB  . ASP F  2 90  ? 3.515   -32.795  -19.220 1.000 59.764  0 90  ASP FFF CB  1 ? 22 
ATOM   7370  C CG  . ASP F  2 90  ? 2.958   -32.614  -17.816 1.000 61.228  0 90  ASP FFF CG  1 ? 22 
ATOM   7371  O OD1 . ASP F  2 90  ? 3.759   -32.351  -16.878 1.000 58.459  0 90  ASP FFF OD1 1 ? 22 
ATOM   7372  O OD2 . ASP F  2 90  ? 1.728   -32.737  -17.670 1.000 63.679  0 90  ASP FFF OD2 1 ? 22 
ATOM   7373  N N   . THR F  2 91  ? 4.998   -31.373  -22.003 1.000 55.745  0 91  THR FFF N   1 ? 22 
ATOM   7374  C CA  . THR F  2 91  ? 5.644   -31.594  -23.317 1.000 55.066  0 91  THR FFF CA  1 ? 22 
ATOM   7375  C C   . THR F  2 91  ? 7.163   -31.523  -23.142 1.000 53.012  0 91  THR FFF C   1 ? 22 
ATOM   7376  O O   . THR F  2 91  ? 7.651   -30.517  -22.627 1.000 53.738  0 91  THR FFF O   1 ? 22 
ATOM   7377  C CB  . THR F  2 91  ? 5.158   -30.571  -24.346 1.000 57.117  0 91  THR FFF CB  1 ? 22 
ATOM   7378  O OG1 . THR F  2 91  ? 3.766   -30.848  -24.537 1.000 60.642  0 91  THR FFF OG1 1 ? 22 
ATOM   7379  C CG2 . THR F  2 91  ? 5.916   -30.645  -25.653 1.000 56.172  0 91  THR FFF CG2 1 ? 22 
ATOM   7380  N N   . ALA F  2 92  ? 7.877   -32.565  -23.553 1.000 51.439  0 92  ALA FFF N   1 ? 22 
ATOM   7381  C CA  . ALA F  2 92  ? 9.351   -32.655  -23.436 1.000 51.059  0 92  ALA FFF CA  1 ? 22 
ATOM   7382  C C   . ALA F  2 92  ? 9.839   -33.981  -24.010 1.000 48.321  0 92  ALA FFF C   1 ? 22 
ATOM   7383  O O   . ALA F  2 92  ? 9.014   -34.851  -24.321 1.000 49.915  0 92  ALA FFF O   1 ? 22 
ATOM   7384  C CB  . ALA F  2 92  ? 9.783   -32.542  -21.989 1.000 51.458  0 92  ALA FFF CB  1 ? 22 
ATOM   7385  N N   . VAL F  2 93  ? 11.156  -34.112  -24.109 1.000 45.236  0 93  VAL FFF N   1 ? 22 
ATOM   7386  C CA  . VAL F  2 93  ? 11.834  -35.406  -24.331 1.000 42.926  0 93  VAL FFF CA  1 ? 22 
ATOM   7387  C C   . VAL F  2 93  ? 11.935  -36.056  -22.958 1.000 44.559  0 93  VAL FFF C   1 ? 22 
ATOM   7388  O O   . VAL F  2 93  ? 12.419  -35.381  -22.023 1.000 47.410  0 93  VAL FFF O   1 ? 22 
ATOM   7389  C CB  . VAL F  2 93  ? 13.201  -35.225  -25.008 1.000 41.448  0 93  VAL FFF CB  1 ? 22 
ATOM   7390  C CG1 . VAL F  2 93  ? 13.958  -36.549  -25.118 1.000 38.625  0 93  VAL FFF CG1 1 ? 22 
ATOM   7391  C CG2 . VAL F  2 93  ? 13.057  -34.537  -26.371 1.000 41.967  0 93  VAL FFF CG2 1 ? 22 
ATOM   7392  N N   . TYR F  2 94  ? 11.455  -37.295  -22.833 1.000 42.470  0 94  TYR FFF N   1 ? 22 
ATOM   7393  C CA  . TYR F  2 94  ? 11.501  -38.082  -21.580 1.000 40.826  0 94  TYR FFF CA  1 ? 22 
ATOM   7394  C C   . TYR F  2 94  ? 12.621  -39.110  -21.712 1.000 40.900  0 94  TYR FFF C   1 ? 22 
ATOM   7395  O O   . TYR F  2 94  ? 12.616  -39.868  -22.701 1.000 37.985  0 94  TYR FFF O   1 ? 22 
ATOM   7396  C CB  . TYR F  2 94  ? 10.140  -38.701  -21.267 1.000 41.711  0 94  TYR FFF CB  1 ? 22 
ATOM   7397  C CG  . TYR F  2 94  ? 9.141   -37.713  -20.713 1.000 43.431  0 94  TYR FFF CG  1 ? 22 
ATOM   7398  C CD1 . TYR F  2 94  ? 8.553   -36.757  -21.526 1.000 45.596  0 94  TYR FFF CD1 1 ? 22 
ATOM   7399  C CD2 . TYR F  2 94  ? 8.807   -37.709  -19.372 1.000 43.594  0 94  TYR FFF CD2 1 ? 22 
ATOM   7400  C CE1 . TYR F  2 94  ? 7.647   -35.835  -21.026 1.000 47.670  0 94  TYR FFF CE1 1 ? 22 
ATOM   7401  C CE2 . TYR F  2 94  ? 7.895   -36.800  -18.857 1.000 46.358  0 94  TYR FFF CE2 1 ? 22 
ATOM   7402  C CZ  . TYR F  2 94  ? 7.315   -35.855  -19.683 1.000 47.807  0 94  TYR FFF CZ  1 ? 22 
ATOM   7403  O OH  . TYR F  2 94  ? 6.428   -34.953  -19.166 1.000 50.493  0 94  TYR FFF OH  1 ? 22 
ATOM   7404  N N   . PHE F  2 95  ? 13.570  -39.058  -20.769 1.000 40.814  0 95  PHE FFF N   1 ? 22 
ATOM   7405  C CA  . PHE F  2 95  ? 14.758  -39.935  -20.697 1.000 40.797  0 95  PHE FFF CA  1 ? 22 
ATOM   7406  C C   . PHE F  2 95  ? 14.608  -40.932  -19.556 1.000 42.479  0 95  PHE FFF C   1 ? 22 
ATOM   7407  O O   . PHE F  2 95  ? 14.303  -40.564  -18.405 1.000 43.719  0 95  PHE FFF O   1 ? 22 
ATOM   7408  C CB  . PHE F  2 95  ? 16.045  -39.151  -20.433 1.000 41.228  0 95  PHE FFF CB  1 ? 22 
ATOM   7409  C CG  . PHE F  2 95  ? 16.417  -38.189  -21.522 1.000 40.811  0 95  PHE FFF CG  1 ? 22 
ATOM   7410  C CD1 . PHE F  2 95  ? 15.924  -36.896  -21.507 1.000 41.447  0 95  PHE FFF CD1 1 ? 22 
ATOM   7411  C CD2 . PHE F  2 95  ? 17.260  -38.575  -22.555 1.000 42.469  0 95  PHE FFF CD2 1 ? 22 
ATOM   7412  C CE1 . PHE F  2 95  ? 16.284  -36.001  -22.487 1.000 42.179  0 95  PHE FFF CE1 1 ? 22 
ATOM   7413  C CE2 . PHE F  2 95  ? 17.600  -37.672  -23.554 1.000 44.136  0 95  PHE FFF CE2 1 ? 22 
ATOM   7414  C CZ  . PHE F  2 95  ? 17.108  -36.398  -23.520 1.000 43.322  0 95  PHE FFF CZ  1 ? 22 
ATOM   7415  N N   . CYS F  2 96  ? 14.858  -42.185  -19.898 1.000 42.464  0 96  CYS FFF N   1 ? 22 
ATOM   7416  C CA  . CYS F  2 96  ? 15.070  -43.302  -18.964 1.000 44.021  0 96  CYS FFF CA  1 ? 22 
ATOM   7417  C C   . CYS F  2 96  ? 16.493  -43.193  -18.402 1.000 40.404  0 96  CYS FFF C   1 ? 22 
ATOM   7418  O O   . CYS F  2 96  ? 17.417  -42.874  -19.186 1.000 38.252  0 96  CYS FFF O   1 ? 22 
ATOM   7419  C CB  . CYS F  2 96  ? 14.889  -44.594  -19.750 1.000 46.424  0 96  CYS FFF CB  1 ? 22 
ATOM   7420  S SG  . CYS F  2 96  ? 14.954  -46.066  -18.697 1.000 56.965  0 96  CYS FFF SG  1 ? 22 
ATOM   7421  N N   . ALA F  2 97  ? 16.697  -43.452  -17.122 1.000 37.825  0 97  ALA FFF N   1 ? 22 
ATOM   7422  C CA  . ALA F  2 97  ? 18.071  -43.480  -16.556 1.000 38.311  0 97  ALA FFF CA  1 ? 22 
ATOM   7423  C C   . ALA F  2 97  ? 18.170  -44.582  -15.506 1.000 37.271  0 97  ALA FFF C   1 ? 22 
ATOM   7424  O O   . ALA F  2 97  ? 17.121  -44.991  -14.956 1.000 36.294  0 97  ALA FFF O   1 ? 22 
ATOM   7425  C CB  . ALA F  2 97  ? 18.459  -42.147  -15.968 1.000 39.115  0 97  ALA FFF CB  1 ? 22 
ATOM   7426  N N   . ALA F  2 98  ? 19.385  -45.076  -15.269 1.000 36.383  0 98  ALA FFF N   1 ? 22 
ATOM   7427  C CA  . ALA F  2 98  ? 19.652  -46.208  -14.367 1.000 35.534  0 98  ALA FFF CA  1 ? 22 
ATOM   7428  C C   . ALA F  2 98  ? 20.986  -46.020  -13.666 1.000 35.459  0 98  ALA FFF C   1 ? 22 
ATOM   7429  O O   . ALA F  2 98  ? 21.948  -45.517  -14.284 1.000 37.317  0 98  ALA FFF O   1 ? 22 
ATOM   7430  C CB  . ALA F  2 98  ? 19.622  -47.482  -15.148 1.000 35.177  0 98  ALA FFF CB  1 ? 22 
ATOM   7431  N N   . ASP F  2 99  ? 21.046  -46.475  -12.416 1.000 36.319  0 99  ASP FFF N   1 ? 22 
ATOM   7432  C CA  . ASP F  2 99  ? 22.294  -46.536  -11.612 1.000 35.877  0 99  ASP FFF CA  1 ? 22 
ATOM   7433  C C   . ASP F  2 99  ? 22.210  -47.671  -10.598 1.000 33.966  0 99  ASP FFF C   1 ? 22 
ATOM   7434  O O   . ASP F  2 99  ? 21.112  -47.983  -10.130 1.000 36.267  0 99  ASP FFF O   1 ? 22 
ATOM   7435  C CB  . ASP F  2 99  ? 22.540  -45.212  -10.912 1.000 38.097  0 99  ASP FFF CB  1 ? 22 
ATOM   7436  C CG  . ASP F  2 99  ? 23.999  -45.022  -10.580 1.000 41.091  0 99  ASP FFF CG  1 ? 22 
ATOM   7437  O OD1 . ASP F  2 99  ? 24.754  -44.660  -11.504 1.000 44.996  0 99  ASP FFF OD1 1 ? 22 
ATOM   7438  O OD2 . ASP F  2 99  ? 24.361  -45.282  -9.420  1.000 42.344  0 99  ASP FFF OD2 1 ? 22 
ATOM   7439  N N   . ARG F  2 100 ? 23.340  -48.243  -10.258 1.000 35.301  0 100 ARG FFF N   1 ? 22 
ATOM   7440  C CA  . ARG F  2 100 ? 23.438  -49.264  -9.186  1.000 40.032  0 100 ARG FFF CA  1 ? 22 
ATOM   7441  C C   . ARG F  2 100 ? 23.059  -48.644  -7.836  1.000 40.295  0 100 ARG FFF C   1 ? 22 
ATOM   7442  O O   . ARG F  2 100 ? 22.460  -49.356  -7.008  1.000 40.233  0 100 ARG FFF O   1 ? 22 
ATOM   7443  C CB  . ARG F  2 100 ? 24.861  -49.819  -9.129  1.000 42.484  0 100 ARG FFF CB  1 ? 22 
ATOM   7444  C CG  . ARG F  2 100 ? 25.209  -50.702  -10.325 1.000 43.441  0 100 ARG FFF CG  1 ? 22 
ATOM   7445  C CD  . ARG F  2 100 ? 24.482  -52.034  -10.366 1.000 45.659  0 100 ARG FFF CD  1 ? 22 
ATOM   7446  N NE  . ARG F  2 100 ? 24.360  -52.671  -9.059  1.000 48.255  0 100 ARG FFF NE  1 ? 22 
ATOM   7447  C CZ  . ARG F  2 100 ? 25.220  -53.516  -8.529  1.000 47.986  0 100 ARG FFF CZ  1 ? 22 
ATOM   7448  N NH1 . ARG F  2 100 ? 26.357  -53.822  -9.136  1.000 46.692  0 100 ARG FFF NH1 1 ? 22 
ATOM   7449  N NH2 . ARG F  2 100 ? 24.948  -54.001  -7.330  1.000 52.674  0 100 ARG FFF NH2 1 ? 22 
ATOM   7450  N N   . GLY F  2 101 ? 23.396  -47.374  -7.636  1.000 36.653  0 101 GLY FFF N   1 ? 22 
ATOM   7451  C CA  . GLY F  2 101 ? 23.220  -46.685  -6.356  1.000 40.211  0 101 GLY FFF CA  1 ? 22 
ATOM   7452  C C   . GLY F  2 101 ? 21.937  -45.868  -6.307  1.000 39.541  0 101 GLY FFF C   1 ? 22 
ATOM   7453  O O   . GLY F  2 101 ? 21.531  -45.321  -7.358  1.000 36.170  0 101 GLY FFF O   1 ? 22 
ATOM   7454  N N   . GLU F  2 102 ? 21.352  -45.778  -5.110  1.000 39.055  0 102 GLU FFF N   1 ? 22 
ATOM   7455  C CA  . GLU F  2 102 ? 20.258  -44.842  -4.797  1.000 39.883  0 102 GLU FFF CA  1 ? 22 
ATOM   7456  C C   . GLU F  2 102 ? 20.892  -43.612  -4.138  1.000 41.117  0 102 GLU FFF C   1 ? 22 
ATOM   7457  O O   . GLU F  2 102 ? 21.535  -43.776  -3.080  1.000 39.400  0 102 GLU FFF O   1 ? 22 
ATOM   7458  C CB  . GLU F  2 102 ? 19.227  -45.512  -3.896  1.000 40.860  0 102 GLU FFF CB  1 ? 22 
ATOM   7459  C CG  . GLU F  2 102 ? 17.991  -44.663  -3.642  1.000 42.614  0 102 GLU FFF CG  1 ? 22 
ATOM   7460  C CD  . GLU F  2 102 ? 17.021  -45.318  -2.668  1.000 44.698  0 102 GLU FFF CD  1 ? 22 
ATOM   7461  O OE1 . GLU F  2 102 ? 17.048  -46.575  -2.539  1.000 45.590  0 102 GLU FFF OE1 1 ? 22 
ATOM   7462  O OE2 . GLU F  2 102 ? 16.257  -44.591  -2.042  1.000 47.677  0 102 GLU FFF OE2 1 ? 22 
ATOM   7463  N N   . SER F  2 103 ? 20.707  -42.435  -4.752  1.000 39.970  0 103 SER FFF N   1 ? 22 
ATOM   7464  C CA  . SER F  2 103 ? 21.322  -41.164  -4.322  1.000 41.438  0 103 SER FFF CA  1 ? 22 
ATOM   7465  C C   . SER F  2 103 ? 20.431  -40.452  -3.310  1.000 41.621  0 103 SER FFF C   1 ? 22 
ATOM   7466  O O   . SER F  2 103 ? 19.231  -40.369  -3.515  1.000 43.246  0 103 SER FFF O   1 ? 22 
ATOM   7467  C CB  . SER F  2 103 ? 21.636  -40.263  -5.502  1.000 41.082  0 103 SER FFF CB  1 ? 22 
ATOM   7468  O OG  . SER F  2 103 ? 22.238  -39.054  -5.042  1.000 42.652  0 103 SER FFF OG  1 ? 22 
ATOM   7469  N N   . TYR F  2 104 ? 21.030  -39.899  -2.273  1.000 38.569  0 104 TYR FFF N   1 ? 23 
ATOM   7470  C CA  . TYR F  2 104 ? 20.376  -38.869  -1.446  1.000 40.498  0 104 TYR FFF CA  1 ? 23 
ATOM   7471  C C   . TYR F  2 104 ? 19.967  -37.713  -2.357  1.000 39.535  0 104 TYR FFF C   1 ? 23 
ATOM   7472  O O   . TYR F  2 104 ? 18.920  -37.143  -2.115  1.000 41.105  0 104 TYR FFF O   1 ? 23 
ATOM   7473  C CB  . TYR F  2 104 ? 21.284  -38.370  -0.323  1.000 41.580  0 104 TYR FFF CB  1 ? 23 
ATOM   7474  C CG  . TYR F  2 104 ? 20.595  -37.378  0.567   1.000 42.638  0 104 TYR FFF CG  1 ? 23 
ATOM   7475  C CD1 . TYR F  2 104 ? 19.528  -37.770  1.360   1.000 43.148  0 104 TYR FFF CD1 1 ? 23 
ATOM   7476  C CD2 . TYR F  2 104 ? 20.972  -36.041  0.583   1.000 44.931  0 104 TYR FFF CD2 1 ? 23 
ATOM   7477  C CE1 . TYR F  2 104 ? 18.870  -36.867  2.174   1.000 44.378  0 104 TYR FFF CE1 1 ? 23 
ATOM   7478  C CE2 . TYR F  2 104 ? 20.342  -35.127  1.421   1.000 45.545  0 104 TYR FFF CE2 1 ? 23 
ATOM   7479  C CZ  . TYR F  2 104 ? 19.281  -35.550  2.213   1.000 45.058  0 104 TYR FFF CZ  1 ? 23 
ATOM   7480  O OH  . TYR F  2 104 ? 18.610  -34.720  3.048   1.000 45.676  0 104 TYR FFF OH  1 ? 23 
ATOM   7481  N N   . TYR F  2 105 ? 20.793  -37.375  -3.351  1.000 39.301  0 105 TYR FFF N   1 ? 23 
ATOM   7482  C CA  . TYR F  2 105 ? 20.546  -36.272  -4.319  1.000 39.717  0 105 TYR FFF CA  1 ? 23 
ATOM   7483  C C   . TYR F  2 105 ? 19.973  -36.894  -5.604  1.000 40.478  0 105 TYR FFF C   1 ? 23 
ATOM   7484  O O   . TYR F  2 105 ? 20.516  -36.718  -6.706  1.000 39.388  0 105 TYR FFF O   1 ? 23 
ATOM   7485  C CB  . TYR F  2 105 ? 21.818  -35.453  -4.561  1.000 39.906  0 105 TYR FFF CB  1 ? 23 
ATOM   7486  C CG  . TYR F  2 105 ? 22.593  -35.020  -3.332  1.000 38.249  0 105 TYR FFF CG  1 ? 23 
ATOM   7487  C CD1 . TYR F  2 105 ? 22.109  -34.047  -2.484  1.000 38.527  0 105 TYR FFF CD1 1 ? 23 
ATOM   7488  C CD2 . TYR F  2 105 ? 23.849  -35.537  -3.049  1.000 38.252  0 105 TYR FFF CD2 1 ? 23 
ATOM   7489  C CE1 . TYR F  2 105 ? 22.815  -33.623  -1.364  1.000 38.610  0 105 TYR FFF CE1 1 ? 23 
ATOM   7490  C CE2 . TYR F  2 105 ? 24.573  -35.129  -1.939  1.000 39.251  0 105 TYR FFF CE2 1 ? 23 
ATOM   7491  C CZ  . TYR F  2 105 ? 24.059  -34.160  -1.094  1.000 38.846  0 105 TYR FFF CZ  1 ? 23 
ATOM   7492  O OH  . TYR F  2 105 ? 24.770  -33.776  0.005   1.000 40.749  0 105 TYR FFF OH  1 ? 23 
ATOM   7493  N N   . TYR F  2 106 ? 18.828  -37.570  -5.458  1.000 41.557  0 106 TYR FFF N   1 ? 23 
ATOM   7494  C CA  . TYR F  2 106 ? 18.197  -38.407  -6.501  1.000 41.439  0 106 TYR FFF CA  1 ? 23 
ATOM   7495  C C   . TYR F  2 106 ? 17.766  -37.555  -7.697  1.000 40.807  0 106 TYR FFF C   1 ? 23 
ATOM   7496  O O   . TYR F  2 106 ? 17.500  -38.167  -8.741  1.000 40.207  0 106 TYR FFF O   1 ? 23 
ATOM   7497  C CB  . TYR F  2 106 ? 16.990  -39.182  -5.958  1.000 42.158  0 106 TYR FFF CB  1 ? 23 
ATOM   7498  C CG  . TYR F  2 106 ? 15.948  -38.336  -5.282  1.000 41.811  0 106 TYR FFF CG  1 ? 23 
ATOM   7499  C CD1 . TYR F  2 106 ? 14.983  -37.671  -6.006  1.000 42.256  0 106 TYR FFF CD1 1 ? 23 
ATOM   7500  C CD2 . TYR F  2 106 ? 15.913  -38.232  -3.903  1.000 42.807  0 106 TYR FFF CD2 1 ? 23 
ATOM   7501  C CE1 . TYR F  2 106 ? 14.029  -36.885  -5.382  1.000 43.744  0 106 TYR FFF CE1 1 ? 23 
ATOM   7502  C CE2 . TYR F  2 106 ? 14.991  -37.428  -3.259  1.000 43.602  0 106 TYR FFF CE2 1 ? 23 
ATOM   7503  C CZ  . TYR F  2 106 ? 14.038  -36.757  -4.004  1.000 45.094  0 106 TYR FFF CZ  1 ? 23 
ATOM   7504  O OH  . TYR F  2 106 ? 13.080  -36.002  -3.388  1.000 46.419  0 106 TYR FFF OH  1 ? 23 
ATOM   7505  N N   . THR F  2 107 ? 17.674  -36.226  -7.557  1.000 39.994  0 107 THR FFF N   1 ? 23 
ATOM   7506  C CA  . THR F  2 107 ? 17.266  -35.311  -8.657  1.000 39.939  0 107 THR FFF CA  1 ? 23 
ATOM   7507  C C   . THR F  2 107 ? 18.463  -34.927  -9.531  1.000 39.259  0 107 THR FFF C   1 ? 23 
ATOM   7508  O O   . THR F  2 107 ? 18.241  -34.360  -10.579 1.000 39.847  0 107 THR FFF O   1 ? 23 
ATOM   7509  C CB  . THR F  2 107 ? 16.557  -34.049  -8.156  1.000 40.305  0 107 THR FFF CB  1 ? 23 
ATOM   7510  O OG1 . THR F  2 107 ? 17.524  -33.175  -7.576  1.000 41.610  0 107 THR FFF OG1 1 ? 23 
ATOM   7511  C CG2 . THR F  2 107 ? 15.463  -34.339  -7.155  1.000 40.230  0 107 THR FFF CG2 1 ? 23 
ATOM   7512  N N   . ARG F  2 108 ? 19.693  -35.234  -9.134  1.000 40.444  0 108 ARG FFF N   1 ? 23 
ATOM   7513  C CA  . ARG F  2 108 ? 20.891  -34.862  -9.936  1.000 41.011  0 108 ARG FFF CA  1 ? 23 
ATOM   7514  C C   . ARG F  2 108 ? 21.108  -35.837  -11.088 1.000 41.058  0 108 ARG FFF C   1 ? 23 
ATOM   7515  O O   . ARG F  2 108 ? 21.310  -37.035  -10.881 1.000 42.256  0 108 ARG FFF O   1 ? 23 
ATOM   7516  C CB  . ARG F  2 108 ? 22.147  -34.887  -9.070  1.000 40.968  0 108 ARG FFF CB  1 ? 23 
ATOM   7517  C CG  . ARG F  2 108 ? 22.232  -33.786  -8.024  1.000 40.527  0 108 ARG FFF CG  1 ? 23 
ATOM   7518  C CD  . ARG F  2 108 ? 23.622  -33.835  -7.431  1.000 41.088  0 108 ARG FFF CD  1 ? 23 
ATOM   7519  N NE  . ARG F  2 108 ? 23.720  -33.043  -6.228  1.000 41.838  0 108 ARG FFF NE  1 ? 23 
ATOM   7520  C CZ  . ARG F  2 108 ? 24.728  -33.082  -5.380  1.000 42.226  0 108 ARG FFF CZ  1 ? 23 
ATOM   7521  N NH1 . ARG F  2 108 ? 25.730  -33.928  -5.561  1.000 43.921  0 108 ARG FFF NH1 1 ? 23 
ATOM   7522  N NH2 . ARG F  2 108 ? 24.711  -32.292  -4.323  1.000 43.248  0 108 ARG FFF NH2 1 ? 23 
ATOM   7523  N N   . PRO F  2 109 ? 21.113  -35.355  -12.346 1.000 41.427  0 109 PRO FFF N   1 ? 23 
ATOM   7524  C CA  . PRO F  2 109 ? 21.515  -36.183  -13.484 1.000 40.437  0 109 PRO FFF CA  1 ? 23 
ATOM   7525  C C   . PRO F  2 109 ? 22.860  -36.914  -13.312 1.000 40.093  0 109 PRO FFF C   1 ? 23 
ATOM   7526  O O   . PRO F  2 109 ? 22.955  -38.079  -13.709 1.000 43.048  0 109 PRO FFF O   1 ? 23 
ATOM   7527  C CB  . PRO F  2 109 ? 21.591  -35.182  -14.646 1.000 40.304  0 109 PRO FFF CB  1 ? 23 
ATOM   7528  C CG  . PRO F  2 109 ? 20.532  -34.170  -14.266 1.000 41.563  0 109 PRO FFF CG  1 ? 23 
ATOM   7529  C CD  . PRO F  2 109 ? 20.673  -34.019  -12.759 1.000 41.110  0 109 PRO FFF CD  1 ? 23 
ATOM   7530  N N   . THR F  2 110 ? 23.858  -36.256  -12.722 1.000 37.664  0 110 THR FFF N   1 ? 23 
ATOM   7531  C CA  . THR F  2 110 ? 25.230  -36.800  -12.517 1.000 37.067  0 110 THR FFF CA  1 ? 23 
ATOM   7532  C C   . THR F  2 110 ? 25.213  -38.029  -11.595 1.000 36.000  0 110 THR FFF C   1 ? 23 
ATOM   7533  O O   . THR F  2 110 ? 26.187  -38.749  -11.616 1.000 37.153  0 110 THR FFF O   1 ? 23 
ATOM   7534  C CB  . THR F  2 110 ? 26.191  -35.721  -11.988 1.000 37.750  0 110 THR FFF CB  1 ? 23 
ATOM   7535  O OG1 . THR F  2 110 ? 25.630  -35.133  -10.799 1.000 38.318  0 110 THR FFF OG1 1 ? 23 
ATOM   7536  C CG2 . THR F  2 110 ? 26.485  -34.656  -13.023 1.000 37.135  0 110 THR FFF CG2 1 ? 23 
ATOM   7537  N N   . GLU F  2 111 ? 24.148  -38.281  -10.831 1.000 36.243  0 111 GLU FFF N   1 ? 23 
ATOM   7538  C CA  . GLU F  2 111 ? 24.057  -39.477  -9.952  1.000 36.421  0 111 GLU FFF CA  1 ? 23 
ATOM   7539  C C   . GLU F  2 111 ? 23.600  -40.716  -10.749 1.000 38.365  0 111 GLU FFF C   1 ? 23 
ATOM   7540  O O   . GLU F  2 111 ? 23.499  -41.771  -10.128 1.000 39.717  0 111 GLU FFF O   1 ? 23 
ATOM   7541  C CB  . GLU F  2 111 ? 23.128  -39.183  -8.769  1.000 36.358  0 111 GLU FFF CB  1 ? 23 
ATOM   7542  C CG  . GLU F  2 111 ? 23.703  -38.198  -7.770  1.000 36.770  0 111 GLU FFF CG  1 ? 23 
ATOM   7543  C CD  . GLU F  2 111 ? 24.889  -38.715  -6.963  1.000 36.719  0 111 GLU FFF CD  1 ? 23 
ATOM   7544  O OE1 . GLU F  2 111 ? 25.984  -38.843  -7.566  1.000 35.146  0 111 GLU FFF OE1 1 ? 23 
ATOM   7545  O OE2 . GLU F  2 111 ? 24.733  -38.953  -5.707  1.000 36.895  0 111 GLU FFF OE2 1 ? 23 
ATOM   7546  N N   . TYR F  2 112 ? 23.303  -40.614  -12.046 1.000 38.495  0 112 TYR FFF N   1 ? 23 
ATOM   7547  C CA  . TYR F  2 112 ? 22.849  -41.764  -12.878 1.000 39.420  0 112 TYR FFF CA  1 ? 23 
ATOM   7548  C C   . TYR F  2 112 ? 23.869  -42.033  -13.994 1.000 39.000  0 112 TYR FFF C   1 ? 23 
ATOM   7549  O O   . TYR F  2 112 ? 24.111  -41.157  -14.827 1.000 39.261  0 112 TYR FFF O   1 ? 23 
ATOM   7550  C CB  . TYR F  2 112 ? 21.426  -41.522  -13.399 1.000 39.535  0 112 TYR FFF CB  1 ? 23 
ATOM   7551  C CG  . TYR F  2 112 ? 20.429  -41.300  -12.298 1.000 40.454  0 112 TYR FFF CG  1 ? 23 
ATOM   7552  C CD1 . TYR F  2 112 ? 20.266  -40.053  -11.724 1.000 42.375  0 112 TYR FFF CD1 1 ? 23 
ATOM   7553  C CD2 . TYR F  2 112 ? 19.676  -42.342  -11.789 1.000 40.992  0 112 TYR FFF CD2 1 ? 23 
ATOM   7554  C CE1 . TYR F  2 112 ? 19.370  -39.849  -10.688 1.000 43.409  0 112 TYR FFF CE1 1 ? 23 
ATOM   7555  C CE2 . TYR F  2 112 ? 18.778  -42.156  -10.753 1.000 42.528  0 112 TYR FFF CE2 1 ? 23 
ATOM   7556  C CZ  . TYR F  2 112 ? 18.620  -40.898  -10.195 1.000 42.657  0 112 TYR FFF CZ  1 ? 23 
ATOM   7557  O OH  . TYR F  2 112 ? 17.727  -40.699  -9.174  1.000 43.432  0 112 TYR FFF OH  1 ? 23 
ATOM   7558  N N   . GLU F  2 113 ? 24.458  -43.227  -14.017 1.000 38.665  0 113 GLU FFF N   1 ? 23 
ATOM   7559  C CA  . GLU F  2 113 ? 25.506  -43.576  -14.999 1.000 40.265  0 113 GLU FFF CA  1 ? 23 
ATOM   7560  C C   . GLU F  2 113 ? 24.913  -43.786  -16.406 1.000 38.288  0 113 GLU FFF C   1 ? 23 
ATOM   7561  O O   . GLU F  2 113 ? 25.564  -43.390  -17.353 1.000 41.557  0 113 GLU FFF O   1 ? 23 
ATOM   7562  C CB  . GLU F  2 113 ? 26.244  -44.837  -14.565 1.000 44.750  0 113 GLU FFF CB  1 ? 23 
ATOM   7563  C CG  . GLU F  2 113 ? 27.368  -45.196  -15.530 1.000 48.913  0 113 GLU FFF CG  1 ? 23 
ATOM   7564  C CD  . GLU F  2 113 ? 28.233  -46.365  -15.099 1.000 55.014  0 113 GLU FFF CD  1 ? 23 
ATOM   7565  O OE1 . GLU F  2 113 ? 27.983  -46.929  -13.993 1.000 56.738  0 113 GLU FFF OE1 1 ? 23 
ATOM   7566  O OE2 . GLU F  2 113 ? 29.139  -46.729  -15.893 1.000 63.347  0 113 GLU FFF OE2 1 ? 23 
ATOM   7567  N N   . PHE F  2 114 ? 23.750  -44.418  -16.532 1.000 37.325  0 114 PHE FFF N   1 ? 23 
ATOM   7568  C CA  . PHE F  2 114 ? 23.172  -44.888  -17.817 1.000 37.326  0 114 PHE FFF CA  1 ? 23 
ATOM   7569  C C   . PHE F  2 114 ? 21.931  -44.086  -18.182 1.000 36.408  0 114 PHE FFF C   1 ? 23 
ATOM   7570  O O   . PHE F  2 114 ? 21.061  -43.872  -17.325 1.000 37.815  0 114 PHE FFF O   1 ? 23 
ATOM   7571  C CB  . PHE F  2 114 ? 22.827  -46.373  -17.725 1.000 38.381  0 114 PHE FFF CB  1 ? 23 
ATOM   7572  C CG  . PHE F  2 114 ? 24.049  -47.216  -17.503 1.000 38.696  0 114 PHE FFF CG  1 ? 23 
ATOM   7573  C CD1 . PHE F  2 114 ? 25.075  -47.255  -18.434 1.000 38.864  0 114 PHE FFF CD1 1 ? 23 
ATOM   7574  C CD2 . PHE F  2 114 ? 24.196  -47.911  -16.316 1.000 39.522  0 114 PHE FFF CD2 1 ? 23 
ATOM   7575  C CE1 . PHE F  2 114 ? 26.221  -48.011  -18.181 1.000 40.742  0 114 PHE FFF CE1 1 ? 23 
ATOM   7576  C CE2 . PHE F  2 114 ? 25.305  -48.724  -16.110 1.000 40.314  0 114 PHE FFF CE2 1 ? 23 
ATOM   7577  C CZ  . PHE F  2 114 ? 26.334  -48.741  -17.015 1.000 39.973  0 114 PHE FFF CZ  1 ? 23 
ATOM   7578  N N   . TRP F  2 115 ? 21.858  -43.675  -19.450 1.000 36.929  0 115 TRP FFF N   1 ? 23 
ATOM   7579  C CA  . TRP F  2 115 ? 20.790  -42.823  -20.017 1.000 35.970  0 115 TRP FFF CA  1 ? 23 
ATOM   7580  C C   . TRP F  2 115 ? 20.293  -43.407  -21.340 1.000 37.037  0 115 TRP FFF C   1 ? 23 
ATOM   7581  O O   . TRP F  2 115 ? 21.131  -43.708  -22.220 1.000 38.764  0 115 TRP FFF O   1 ? 23 
ATOM   7582  C CB  . TRP F  2 115 ? 21.342  -41.409  -20.213 1.000 35.272  0 115 TRP FFF CB  1 ? 23 
ATOM   7583  C CG  . TRP F  2 115 ? 21.584  -40.715  -18.914 1.000 34.972  0 115 TRP FFF CG  1 ? 23 
ATOM   7584  C CD1 . TRP F  2 115 ? 22.668  -40.862  -18.095 1.000 34.362  0 115 TRP FFF CD1 1 ? 23 
ATOM   7585  C CD2 . TRP F  2 115 ? 20.685  -39.816  -18.246 1.000 34.400  0 115 TRP FFF CD2 1 ? 23 
ATOM   7586  N NE1 . TRP F  2 115 ? 22.496  -40.107  -16.968 1.000 34.300  0 115 TRP FFF NE1 1 ? 23 
ATOM   7587  C CE2 . TRP F  2 115 ? 21.298  -39.449  -17.037 1.000 35.191  0 115 TRP FFF CE2 1 ? 23 
ATOM   7588  C CE3 . TRP F  2 115 ? 19.437  -39.278  -18.556 1.000 37.020  0 115 TRP FFF CE3 1 ? 23 
ATOM   7589  C CZ2 . TRP F  2 115 ? 20.706  -38.555  -16.149 1.000 36.260  0 115 TRP FFF CZ2 1 ? 23 
ATOM   7590  C CZ3 . TRP F  2 115 ? 18.844  -38.400  -17.674 1.000 37.426  0 115 TRP FFF CZ3 1 ? 23 
ATOM   7591  C CH2 . TRP F  2 115 ? 19.461  -38.062  -16.474 1.000 36.754  0 115 TRP FFF CH2 1 ? 23 
ATOM   7592  N N   . GLY F  2 116 ? 18.977  -43.474  -21.509 1.000 36.198  0 116 GLY FFF N   1 ? 23 
ATOM   7593  C CA  . GLY F  2 116 ? 18.357  -43.668  -22.829 1.000 36.041  0 116 GLY FFF CA  1 ? 23 
ATOM   7594  C C   . GLY F  2 116 ? 18.572  -42.464  -23.725 1.000 36.309  0 116 GLY FFF C   1 ? 23 
ATOM   7595  O O   . GLY F  2 116 ? 19.094  -41.460  -23.246 1.000 36.958  0 116 GLY FFF O   1 ? 23 
ATOM   7596  N N   . GLN F  2 117 ? 18.194  -42.567  -24.997 1.000 37.398  0 117 GLN FFF N   1 ? 23 
ATOM   7597  C CA  . GLN F  2 117 ? 18.291  -41.478  -25.996 1.000 39.174  0 117 GLN FFF CA  1 ? 23 
ATOM   7598  C C   . GLN F  2 117 ? 17.111  -40.515  -25.839 1.000 40.921  0 117 GLN FFF C   1 ? 23 
ATOM   7599  O O   . GLN F  2 117 ? 17.211  -39.397  -26.338 1.000 45.348  0 117 GLN FFF O   1 ? 23 
ATOM   7600  C CB  . GLN F  2 117 ? 18.339  -42.055  -27.410 1.000 38.537  0 117 GLN FFF CB  1 ? 23 
ATOM   7601  C CG  . GLN F  2 117 ? 19.522  -42.982  -27.633 1.000 38.908  0 117 GLN FFF CG  1 ? 23 
ATOM   7602  C CD  . GLN F  2 117 ? 20.864  -42.309  -27.438 1.000 40.070  0 117 GLN FFF CD  1 ? 23 
ATOM   7603  O OE1 . GLN F  2 117 ? 21.168  -41.304  -28.053 1.000 41.815  0 117 GLN FFF OE1 1 ? 23 
ATOM   7604  N NE2 . GLN F  2 117 ? 21.759  -42.907  -26.676 1.000 39.510  0 117 GLN FFF NE2 1 ? 23 
ATOM   7605  N N   . GLY F  2 118 ? 16.038  -40.957  -25.184 1.000 42.535  0 118 GLY FFF N   1 ? 23 
ATOM   7606  C CA  . GLY F  2 118 ? 14.817  -40.164  -24.923 1.000 42.758  0 118 GLY FFF CA  1 ? 23 
ATOM   7607  C C   . GLY F  2 118 ? 13.755  -40.371  -25.979 1.000 42.388  0 118 GLY FFF C   1 ? 23 
ATOM   7608  O O   . GLY F  2 118 ? 14.084  -40.808  -27.078 1.000 42.959  0 118 GLY FFF O   1 ? 23 
ATOM   7609  N N   . THR F  2 119 ? 12.508  -40.049  -25.649 1.000 45.969  0 119 THR FFF N   1 ? 23 
ATOM   7610  C CA  . THR F  2 119 ? 11.333  -40.129  -26.550 1.000 47.031  0 119 THR FFF CA  1 ? 23 
ATOM   7611  C C   . THR F  2 119 ? 10.494  -38.862  -26.338 1.000 47.871  0 119 THR FFF C   1 ? 23 
ATOM   7612  O O   . THR F  2 119 ? 10.336  -38.444  -25.186 1.000 48.220  0 119 THR FFF O   1 ? 23 
ATOM   7613  C CB  . THR F  2 119 ? 10.596  -41.452  -26.301 1.000 49.533  0 119 THR FFF CB  1 ? 23 
ATOM   7614  O OG1 . THR F  2 119 ? 9.712   -41.664  -27.392 1.000 53.052  0 119 THR FFF OG1 1 ? 23 
ATOM   7615  C CG2 . THR F  2 119 ? 9.835   -41.475  -24.997 1.000 49.967  0 119 THR FFF CG2 1 ? 23 
ATOM   7616  N N   . GLN F  2 120 ? 10.002  -38.274  -27.424 1.000 48.713  0 120 GLN FFF N   1 ? 23 
ATOM   7617  C CA  . GLN F  2 120 ? 9.149   -37.068  -27.413 1.000 48.811  0 120 GLN FFF CA  1 ? 23 
ATOM   7618  C C   . GLN F  2 120 ? 7.766   -37.438  -26.865 1.000 51.566  0 120 GLN FFF C   1 ? 23 
ATOM   7619  O O   . GLN F  2 120 ? 7.162   -38.426  -27.340 1.000 52.393  0 120 GLN FFF O   1 ? 23 
ATOM   7620  C CB  . GLN F  2 120 ? 9.044   -36.475  -28.822 1.000 49.103  0 120 GLN FFF CB  1 ? 23 
ATOM   7621  C CG  . GLN F  2 120 ? 8.371   -35.117  -28.884 1.000 51.804  0 120 GLN FFF CG  1 ? 23 
ATOM   7622  C CD  . GLN F  2 120 ? 9.127   -34.050  -28.118 1.000 53.662  0 120 GLN FFF CD  1 ? 23 
ATOM   7623  O OE1 . GLN F  2 120 ? 10.335  -33.890  -28.274 1.000 51.945  0 120 GLN FFF OE1 1 ? 23 
ATOM   7624  N NE2 . GLN F  2 120 ? 8.416   -33.307  -27.282 1.000 56.489  0 120 GLN FFF NE2 1 ? 23 
ATOM   7625  N N   . VAL F  2 121 ? 7.309   -36.682  -25.869 1.000 51.719  0 121 VAL FFF N   1 ? 23 
ATOM   7626  C CA  . VAL F  2 121 ? 5.880   -36.579  -25.474 1.000 52.233  0 121 VAL FFF CA  1 ? 23 
ATOM   7627  C C   . VAL F  2 121 ? 5.416   -35.165  -25.841 1.000 53.152  0 121 VAL FFF C   1 ? 23 
ATOM   7628  O O   . VAL F  2 121 ? 6.077   -34.196  -25.414 1.000 53.923  0 121 VAL FFF O   1 ? 23 
ATOM   7629  C CB  . VAL F  2 121 ? 5.721   -36.857  -23.972 1.000 51.582  0 121 VAL FFF CB  1 ? 23 
ATOM   7630  C CG1 . VAL F  2 121 ? 4.306   -36.583  -23.490 1.000 54.684  0 121 VAL FFF CG1 1 ? 23 
ATOM   7631  C CG2 . VAL F  2 121 ? 6.156   -38.266  -23.619 1.000 49.737  0 121 VAL FFF CG2 1 ? 23 
ATOM   7632  N N   . THR F  2 122 ? 4.338   -35.042  -26.602 1.000 54.113  0 122 THR FFF N   1 ? 23 
ATOM   7633  C CA  . THR F  2 122 ? 3.731   -33.725  -26.954 1.000 57.053  0 122 THR FFF CA  1 ? 23 
ATOM   7634  C C   . THR F  2 122 ? 2.283   -33.700  -26.456 1.000 59.627  0 122 THR FFF C   1 ? 23 
ATOM   7635  O O   . THR F  2 122 ? 1.522   -34.603  -26.822 1.000 61.658  0 122 THR FFF O   1 ? 23 
ATOM   7636  C CB  . THR F  2 122 ? 3.887   -33.425  -28.451 1.000 56.101  0 122 THR FFF CB  1 ? 23 
ATOM   7637  O OG1 . THR F  2 122 ? 5.289   -33.466  -28.737 1.000 54.587  0 122 THR FFF OG1 1 ? 23 
ATOM   7638  C CG2 . THR F  2 122 ? 3.336   -32.075  -28.847 1.000 58.190  0 122 THR FFF CG2 1 ? 23 
ATOM   7639  N N   . VAL F  2 123 ? 1.945   -32.714  -25.628 1.000 61.344  0 123 VAL FFF N   1 ? 23 
ATOM   7640  C CA  . VAL F  2 123 ? 0.569   -32.487  -25.107 1.000 65.779  0 123 VAL FFF CA  1 ? 23 
ATOM   7641  C C   . VAL F  2 123 ? -0.005  -31.227  -25.777 1.000 69.804  0 123 VAL FFF C   1 ? 23 
ATOM   7642  O O   . VAL F  2 123 ? 0.536   -30.145  -25.531 1.000 70.138  0 123 VAL FFF O   1 ? 23 
ATOM   7643  C CB  . VAL F  2 123 ? 0.600   -32.382  -23.568 1.000 65.439  0 123 VAL FFF CB  1 ? 23 
ATOM   7644  C CG1 . VAL F  2 123 ? -0.793  -32.387  -22.966 1.000 69.150  0 123 VAL FFF CG1 1 ? 23 
ATOM   7645  C CG2 . VAL F  2 123 ? 1.423   -33.495  -22.941 1.000 62.593  0 123 VAL FFF CG2 1 ? 23 
ATOM   7646  N N   . SER F  2 124 ? -1.092  -31.363  -26.547 1.000 75.149  0 124 SER FFF N   1 ? 23 
ATOM   7647  C CA  . SER F  2 124 ? -1.806  -30.255  -27.241 1.000 78.811  0 124 SER FFF CA  1 ? 23 
ATOM   7648  C C   . SER F  2 124 ? -3.166  -30.008  -26.579 1.000 81.421  0 124 SER FFF C   1 ? 23 
ATOM   7649  O O   . SER F  2 124 ? -3.187  -29.355  -25.542 1.000 81.566  0 124 SER FFF O   1 ? 23 
ATOM   7650  C CB  . SER F  2 124 ? -1.968  -30.567  -28.686 1.000 79.484  0 124 SER FFF CB  1 ? 23 
ATOM   7651  O OG  . SER F  2 124 ? -3.032  -31.482  -28.845 1.000 84.162  0 124 SER FFF OG  1 ? 23 
ATOM   7652  N N   . THR G  1 4   ? 24.899  -18.104  74.501  1.000 87.105  0 333 THR GGG N   1 ? 24 
ATOM   7653  C CA  . THR G  1 4   ? 24.037  -19.278  74.911  1.000 85.518  0 333 THR GGG CA  1 ? 24 
ATOM   7654  C C   . THR G  1 4   ? 22.739  -19.258  74.073  1.000 80.684  0 333 THR GGG C   1 ? 24 
ATOM   7655  O O   . THR G  1 4   ? 22.296  -20.325  73.563  1.000 79.750  0 333 THR GGG O   1 ? 24 
ATOM   7656  C CB  . THR G  1 4   ? 23.821  -19.258  76.441  1.000 92.102  0 333 THR GGG CB  1 ? 24 
ATOM   7657  O OG1 . THR G  1 4   ? 22.715  -20.064  76.869  1.000 91.654  0 333 THR GGG OG1 1 ? 24 
ATOM   7658  C CG2 . THR G  1 4   ? 23.611  -17.866  77.012  1.000 93.233  0 333 THR GGG CG2 1 ? 24 
ATOM   7659  N N   . ASN G  1 5   ? 22.141  -18.072  73.949  1.000 74.124  0 334 ASN GGG N   1 ? 24 
ATOM   7660  C CA  . ASN G  1 5   ? 20.887  -17.821  73.191  1.000 66.487  0 334 ASN GGG CA  1 ? 24 
ATOM   7661  C C   . ASN G  1 5   ? 21.166  -17.874  71.686  1.000 60.384  0 334 ASN GGG C   1 ? 24 
ATOM   7662  O O   . ASN G  1 5   ? 22.110  -17.238  71.226  1.000 57.630  0 334 ASN GGG O   1 ? 24 
ATOM   7663  C CB  . ASN G  1 5   ? 20.306  -16.462  73.569  1.000 67.678  0 334 ASN GGG CB  1 ? 24 
ATOM   7664  C CG  . ASN G  1 5   ? 21.325  -15.348  73.451  1.000 65.565  0 334 ASN GGG CG  1 ? 24 
ATOM   7665  O OD1 . ASN G  1 5   ? 22.454  -15.454  73.934  1.000 66.139  0 334 ASN GGG OD1 1 ? 24 
ATOM   7666  N ND2 . ASN G  1 5   ? 20.942  -14.288  72.774  1.000 63.979  0 334 ASN GGG ND2 1 ? 24 
ATOM   7667  N N   . LEU G  1 6   ? 20.339  -18.589  70.931  1.000 57.881  0 335 LEU GGG N   1 ? 24 
ATOM   7668  C CA  . LEU G  1 6   ? 20.478  -18.723  69.462  1.000 53.768  0 335 LEU GGG CA  1 ? 24 
ATOM   7669  C C   . LEU G  1 6   ? 20.097  -17.403  68.793  1.000 51.071  0 335 LEU GGG C   1 ? 24 
ATOM   7670  O O   . LEU G  1 6   ? 19.244  -16.680  69.307  1.000 52.331  0 335 LEU GGG O   1 ? 24 
ATOM   7671  C CB  . LEU G  1 6   ? 19.600  -19.878  68.976  1.000 54.457  0 335 LEU GGG CB  1 ? 24 
ATOM   7672  C CG  . LEU G  1 6   ? 20.002  -21.263  69.476  1.000 58.142  0 335 LEU GGG CG  1 ? 24 
ATOM   7673  C CD1 . LEU G  1 6   ? 19.022  -22.307  68.965  1.000 59.153  0 335 LEU GGG CD1 1 ? 24 
ATOM   7674  C CD2 . LEU G  1 6   ? 21.440  -21.581  69.061  1.000 59.466  0 335 LEU GGG CD2 1 ? 24 
ATOM   7675  N N   . CYS G  1 7   ? 20.775  -17.074  67.705  1.000 50.947  0 336 CYS GGG N   1 ? 24 
ATOM   7676  C CA  . CYS G  1 7   ? 20.506  -15.873  66.885  1.000 51.139  0 336 CYS GGG CA  1 ? 24 
ATOM   7677  C C   . CYS G  1 7   ? 19.109  -16.053  66.306  1.000 49.709  0 336 CYS GGG C   1 ? 24 
ATOM   7678  O O   . CYS G  1 7   ? 18.773  -17.133  65.829  1.000 45.651  0 336 CYS GGG O   1 ? 24 
ATOM   7679  C CB  . CYS G  1 7   ? 21.554  -15.684  65.793  1.000 51.862  0 336 CYS GGG CB  1 ? 24 
ATOM   7680  S SG  . CYS G  1 7   ? 23.202  -15.246  66.430  1.000 57.646  0 336 CYS GGG SG  1 ? 24 
ATOM   7681  N N   . PRO G  1 8   ? 18.259  -15.005  66.341  1.000 52.618  0 337 PRO GGG N   1 ? 24 
ATOM   7682  C CA  . PRO G  1 8   ? 16.851  -15.154  65.980  1.000 52.212  0 337 PRO GGG CA  1 ? 24 
ATOM   7683  C C   . PRO G  1 8   ? 16.654  -15.098  64.455  1.000 49.789  0 337 PRO GGG C   1 ? 24 
ATOM   7684  O O   . PRO G  1 8   ? 16.018  -14.194  63.972  1.000 51.403  0 337 PRO GGG O   1 ? 24 
ATOM   7685  C CB  . PRO G  1 8   ? 16.228  -13.973  66.745  1.000 54.429  0 337 PRO GGG CB  1 ? 24 
ATOM   7686  C CG  . PRO G  1 8   ? 17.284  -12.883  66.636  1.000 55.395  0 337 PRO GGG CG  1 ? 24 
ATOM   7687  C CD  . PRO G  1 8   ? 18.606  -13.622  66.726  1.000 54.346  0 337 PRO GGG CD  1 ? 24 
ATOM   7688  N N   . PHE G  1 9   ? 17.149  -16.107  63.743  1.000 49.979  0 338 PHE GGG N   1 ? 24 
ATOM   7689  C CA  . PHE G  1 9   ? 17.007  -16.241  62.271  1.000 49.825  0 338 PHE GGG CA  1 ? 24 
ATOM   7690  C C   . PHE G  1 9   ? 15.533  -16.460  61.907  1.000 49.140  0 338 PHE GGG C   1 ? 24 
ATOM   7691  O O   . PHE G  1 9   ? 15.101  -15.962  60.858  1.000 47.117  0 338 PHE GGG O   1 ? 24 
ATOM   7692  C CB  . PHE G  1 9   ? 17.898  -17.358  61.738  1.000 51.714  0 338 PHE GGG CB  1 ? 24 
ATOM   7693  C CG  . PHE G  1 9   ? 19.373  -17.043  61.732  1.000 54.893  0 338 PHE GGG CG  1 ? 24 
ATOM   7694  C CD1 . PHE G  1 9   ? 19.840  -15.827  61.262  1.000 54.704  0 338 PHE GGG CD1 1 ? 24 
ATOM   7695  C CD2 . PHE G  1 9   ? 20.299  -17.992  62.139  1.000 57.607  0 338 PHE GGG CD2 1 ? 24 
ATOM   7696  C CE1 . PHE G  1 9   ? 21.195  -15.548  61.236  1.000 56.240  0 338 PHE GGG CE1 1 ? 24 
ATOM   7697  C CE2 . PHE G  1 9   ? 21.655  -17.718  62.106  1.000 59.388  0 338 PHE GGG CE2 1 ? 24 
ATOM   7698  C CZ  . PHE G  1 9   ? 22.101  -16.497  61.651  1.000 59.227  0 338 PHE GGG CZ  1 ? 24 
ATOM   7699  N N   . GLY G  1 10  ? 14.781  -17.165  62.754  1.000 52.747  0 339 GLY GGG N   1 ? 24 
ATOM   7700  C CA  . GLY G  1 10  ? 13.325  -17.373  62.605  1.000 52.182  0 339 GLY GGG CA  1 ? 24 
ATOM   7701  C C   . GLY G  1 10  ? 12.582  -16.060  62.401  1.000 51.715  0 339 GLY GGG C   1 ? 24 
ATOM   7702  O O   . GLY G  1 10  ? 11.731  -15.999  61.478  1.000 50.970  0 339 GLY GGG O   1 ? 24 
ATOM   7703  N N   . GLU G  1 11  ? 12.900  -15.031  63.194  1.000 53.502  0 340 GLU GGG N   1 ? 24 
ATOM   7704  C CA  . GLU G  1 11  ? 12.224  -13.710  63.115  1.000 59.593  0 340 GLU GGG CA  1 ? 24 
ATOM   7705  C C   . GLU G  1 11  ? 12.453  -13.047  61.751  1.000 55.285  0 340 GLU GGG C   1 ? 24 
ATOM   7706  O O   . GLU G  1 11  ? 11.614  -12.212  61.351  1.000 56.752  0 340 GLU GGG O   1 ? 24 
ATOM   7707  C CB  . GLU G  1 11  ? 12.739  -12.750  64.177  1.000 68.180  0 340 GLU GGG CB  1 ? 24 
ATOM   7708  C CG  . GLU G  1 11  ? 12.419  -13.187  65.582  1.000 76.378  0 340 GLU GGG CG  1 ? 24 
ATOM   7709  C CD  . GLU G  1 11  ? 12.902  -12.202  66.634  1.000 82.756  0 340 GLU GGG CD  1 ? 24 
ATOM   7710  O OE1 . GLU G  1 11  ? 13.346  -11.078  66.246  1.000 84.641  0 340 GLU GGG OE1 1 ? 24 
ATOM   7711  O OE2 . GLU G  1 11  ? 12.854  -12.565  67.836  1.000 88.513  0 340 GLU GGG OE2 1 ? 24 
ATOM   7712  N N   . VAL G  1 12  ? 13.562  -13.393  61.089  1.000 51.639  0 341 VAL GGG N   1 ? 24 
ATOM   7713  C CA  . VAL G  1 12  ? 13.941  -12.830  59.762  1.000 51.418  0 341 VAL GGG CA  1 ? 24 
ATOM   7714  C C   . VAL G  1 12  ? 13.258  -13.638  58.649  1.000 47.906  0 341 VAL GGG C   1 ? 24 
ATOM   7715  O O   . VAL G  1 12  ? 12.488  -13.048  57.878  1.000 50.954  0 341 VAL GGG O   1 ? 24 
ATOM   7716  C CB  . VAL G  1 12  ? 15.467  -12.799  59.570  1.000 50.118  0 341 VAL GGG CB  1 ? 24 
ATOM   7717  C CG1 . VAL G  1 12  ? 15.824  -12.174  58.234  1.000 50.427  0 341 VAL GGG CG1 1 ? 24 
ATOM   7718  C CG2 . VAL G  1 12  ? 16.157  -12.052  60.693  1.000 50.537  0 341 VAL GGG CG2 1 ? 24 
ATOM   7719  N N   . PHE G  1 13  ? 13.561  -14.925  58.567  1.000 43.823  0 342 PHE GGG N   1 ? 24 
ATOM   7720  C CA  . PHE G  1 13  ? 13.188  -15.799  57.428  1.000 45.487  0 342 PHE GGG CA  1 ? 24 
ATOM   7721  C C   . PHE G  1 13  ? 11.680  -16.075  57.432  1.000 48.005  0 342 PHE GGG C   1 ? 24 
ATOM   7722  O O   . PHE G  1 13  ? 11.099  -16.234  56.332  1.000 44.786  0 342 PHE GGG O   1 ? 24 
ATOM   7723  C CB  . PHE G  1 13  ? 13.998  -17.094  57.485  1.000 44.398  0 342 PHE GGG CB  1 ? 24 
ATOM   7724  C CG  . PHE G  1 13  ? 15.407  -16.932  56.993  1.000 42.995  0 342 PHE GGG CG  1 ? 24 
ATOM   7725  C CD1 . PHE G  1 13  ? 16.398  -16.425  57.821  1.000 42.210  0 342 PHE GGG CD1 1 ? 24 
ATOM   7726  C CD2 . PHE G  1 13  ? 15.714  -17.204  55.677  1.000 44.328  0 342 PHE GGG CD2 1 ? 24 
ATOM   7727  C CE1 . PHE G  1 13  ? 17.696  -16.288  57.361  1.000 42.668  0 342 PHE GGG CE1 1 ? 24 
ATOM   7728  C CE2 . PHE G  1 13  ? 17.013  -17.059  55.220  1.000 44.769  0 342 PHE GGG CE2 1 ? 24 
ATOM   7729  C CZ  . PHE G  1 13  ? 18.007  -16.623  56.067  1.000 43.596  0 342 PHE GGG CZ  1 ? 24 
ATOM   7730  N N   . ASN G  1 14  ? 11.075  -16.113  58.626  1.000 50.657  0 343 ASN GGG N   1 ? 24 
ATOM   7731  C CA  . ASN G  1 14  ? 9.666   -16.535  58.820  1.000 52.262  0 343 ASN GGG CA  1 ? 24 
ATOM   7732  C C   . ASN G  1 14  ? 8.827   -15.354  59.313  1.000 50.470  0 343 ASN GGG C   1 ? 24 
ATOM   7733  O O   . ASN G  1 14  ? 7.675   -15.623  59.678  1.000 52.620  0 343 ASN GGG O   1 ? 24 
ATOM   7734  C CB  . ASN G  1 14  ? 9.553   -17.727  59.766  1.000 58.186  0 343 ASN GGG CB  1 ? 24 
ATOM   7735  C CG  . ASN G  1 14  ? 10.136  -19.002  59.203  1.000 65.304  0 343 ASN GGG CG  1 ? 24 
ATOM   7736  O OD1 . ASN G  1 14  ? 10.136  -19.216  57.982  1.000 67.654  0 343 ASN GGG OD1 1 ? 24 
ATOM   7737  N ND2 . ASN G  1 14  ? 10.614  -19.851  60.110  1.000 74.431  0 343 ASN GGG ND2 1 ? 24 
ATOM   7738  N N   . ALA G  1 15  ? 9.328   -14.103  59.228  1.000 47.388  0 344 ALA GGG N   1 ? 24 
ATOM   7739  C CA  . ALA G  1 15  ? 8.502   -12.899  59.426  1.000 47.997  0 344 ALA GGG CA  1 ? 24 
ATOM   7740  C C   . ALA G  1 15  ? 7.268   -13.028  58.524  1.000 51.112  0 344 ALA GGG C   1 ? 24 
ATOM   7741  O O   . ALA G  1 15  ? 7.371   -13.502  57.383  1.000 48.833  0 344 ALA GGG O   1 ? 24 
ATOM   7742  C CB  . ALA G  1 15  ? 9.286   -11.675  59.075  1.000 46.768  0 344 ALA GGG CB  1 ? 24 
ATOM   7743  N N   . THR G  1 16  ? 6.081   -12.715  59.031  1.000 56.287  0 345 THR GGG N   1 ? 24 
ATOM   7744  C CA  . THR G  1 16  ? 4.837   -12.854  58.234  1.000 61.858  0 345 THR GGG CA  1 ? 24 
ATOM   7745  C C   . THR G  1 16  ? 4.812   -11.721  57.198  1.000 62.718  0 345 THR GGG C   1 ? 24 
ATOM   7746  O O   . THR G  1 16  ? 4.208   -11.908  56.132  1.000 64.303  0 345 THR GGG O   1 ? 24 
ATOM   7747  C CB  . THR G  1 16  ? 3.634   -12.959  59.171  1.000 67.528  0 345 THR GGG CB  1 ? 24 
ATOM   7748  O OG1 . THR G  1 16  ? 3.812   -11.890  60.105  1.000 71.409  0 345 THR GGG OG1 1 ? 24 
ATOM   7749  C CG2 . THR G  1 16  ? 3.542   -14.322  59.839  1.000 67.502  0 345 THR GGG CG2 1 ? 24 
ATOM   7750  N N   . ARG G  1 17  ? 5.501   -10.617  57.478  1.000 62.059  0 346 ARG GGG N   1 ? 24 
ATOM   7751  C CA  . ARG G  1 17  ? 5.573   -9.420   56.596  1.000 61.413  0 346 ARG GGG CA  1 ? 24 
ATOM   7752  C C   . ARG G  1 17  ? 7.006   -9.184   56.121  1.000 55.094  0 346 ARG GGG C   1 ? 24 
ATOM   7753  O O   . ARG G  1 17  ? 7.940   -9.344   56.919  1.000 52.127  0 346 ARG GGG O   1 ? 24 
ATOM   7754  C CB  . ARG G  1 17  ? 5.130   -8.202   57.395  1.000 68.760  0 346 ARG GGG CB  1 ? 24 
ATOM   7755  C CG  . ARG G  1 17  ? 3.943   -7.446   56.844  1.000 77.713  0 346 ARG GGG CG  1 ? 24 
ATOM   7756  C CD  . ARG G  1 17  ? 3.334   -6.617   57.972  1.000 87.908  0 346 ARG GGG CD  1 ? 24 
ATOM   7757  N NE  . ARG G  1 17  ? 1.905   -6.874   58.077  1.000 98.446  0 346 ARG GGG NE  1 ? 24 
ATOM   7758  C CZ  . ARG G  1 17  ? 1.116   -6.484   59.086  1.000 107.351 0 346 ARG GGG CZ  1 ? 24 
ATOM   7759  N NH1 . ARG G  1 17  ? 1.618   -5.809   60.110  1.000 110.710 0 346 ARG GGG NH1 1 ? 24 
ATOM   7760  N NH2 . ARG G  1 17  ? -0.180  -6.765   59.063  1.000 110.514 0 346 ARG GGG NH2 1 ? 24 
ATOM   7761  N N   . PHE G  1 18  ? 7.160   -8.872   54.847  1.000 49.234  0 347 PHE GGG N   1 ? 25 
ATOM   7762  C CA  . PHE G  1 18  ? 8.457   -8.534   54.202  1.000 46.201  0 347 PHE GGG CA  1 ? 25 
ATOM   7763  C C   . PHE G  1 18  ? 8.327   -7.153   53.558  1.000 43.322  0 347 PHE GGG C   1 ? 25 
ATOM   7764  O O   . PHE G  1 18  ? 7.259   -6.845   53.006  1.000 43.797  0 347 PHE GGG O   1 ? 25 
ATOM   7765  C CB  . PHE G  1 18  ? 8.852   -9.599   53.169  1.000 45.918  0 347 PHE GGG CB  1 ? 25 
ATOM   7766  C CG  . PHE G  1 18  ? 9.732   -10.702  53.687  1.000 45.958  0 347 PHE GGG CG  1 ? 25 
ATOM   7767  C CD1 . PHE G  1 18  ? 9.340   -11.510  54.736  1.000 47.547  0 347 PHE GGG CD1 1 ? 25 
ATOM   7768  C CD2 . PHE G  1 18  ? 10.965  -10.938  53.124  1.000 45.272  0 347 PHE GGG CD2 1 ? 25 
ATOM   7769  C CE1 . PHE G  1 18  ? 10.164  -12.516  55.218  1.000 47.350  0 347 PHE GGG CE1 1 ? 25 
ATOM   7770  C CE2 . PHE G  1 18  ? 11.791  -11.952  53.586  1.000 45.807  0 347 PHE GGG CE2 1 ? 25 
ATOM   7771  C CZ  . PHE G  1 18  ? 11.387  -12.738  54.638  1.000 46.396  0 347 PHE GGG CZ  1 ? 25 
ATOM   7772  N N   . ALA G  1 19  ? 9.409   -6.383   53.575  1.000 41.878  0 348 ALA GGG N   1 ? 25 
ATOM   7773  C CA  . ALA G  1 19  ? 9.522   -5.026   53.003  1.000 41.767  0 348 ALA GGG CA  1 ? 25 
ATOM   7774  C C   . ALA G  1 19  ? 9.493   -5.070   51.471  1.000 42.467  0 348 ALA GGG C   1 ? 25 
ATOM   7775  O O   . ALA G  1 19  ? 9.891   -6.087   50.845  1.000 43.844  0 348 ALA GGG O   1 ? 25 
ATOM   7776  C CB  . ALA G  1 19  ? 10.811  -4.367   53.469  1.000 40.658  0 348 ALA GGG CB  1 ? 25 
ATOM   7777  N N   . SER G  1 20  ? 9.031   -3.979   50.874  1.000 43.358  0 349 SER GGG N   1 ? 25 
ATOM   7778  C CA  . SER G  1 20  ? 9.358   -3.596   49.482  1.000 44.138  0 349 SER GGG CA  1 ? 25 
ATOM   7779  C C   . SER G  1 20  ? 10.882  -3.452   49.368  1.000 42.808  0 349 SER GGG C   1 ? 25 
ATOM   7780  O O   . SER G  1 20  ? 11.514  -2.916   50.321  1.000 45.544  0 349 SER GGG O   1 ? 25 
ATOM   7781  C CB  . SER G  1 20  ? 8.636   -2.334   49.089  1.000 44.917  0 349 SER GGG CB  1 ? 25 
ATOM   7782  O OG  . SER G  1 20  ? 7.247   -2.646   48.907  1.000 49.171  0 349 SER GGG OG  1 ? 25 
ATOM   7783  N N   . VAL G  1 21  ? 11.446  -3.868   48.240  1.000 40.284  0 350 VAL GGG N   1 ? 25 
ATOM   7784  C CA  . VAL G  1 21  ? 12.917  -3.797   47.998  1.000 39.308  0 350 VAL GGG CA  1 ? 25 
ATOM   7785  C C   . VAL G  1 21  ? 13.441  -2.353   48.173  1.000 38.459  0 350 VAL GGG C   1 ? 25 
ATOM   7786  O O   . VAL G  1 21  ? 14.515  -2.195   48.726  1.000 36.961  0 350 VAL GGG O   1 ? 25 
ATOM   7787  C CB  . VAL G  1 21  ? 13.272  -4.398   46.627  1.000 38.449  0 350 VAL GGG CB  1 ? 25 
ATOM   7788  C CG1 . VAL G  1 21  ? 12.710  -3.584   45.479  1.000 38.468  0 350 VAL GGG CG1 1 ? 25 
ATOM   7789  C CG2 . VAL G  1 21  ? 14.772  -4.599   46.483  1.000 38.576  0 350 VAL GGG CG2 1 ? 25 
ATOM   7790  N N   . TYR G  1 22  ? 12.724  -1.323   47.734  1.000 39.497  0 351 TYR GGG N   1 ? 25 
ATOM   7791  C CA  . TYR G  1 22  ? 13.236  0.074    47.775  1.000 41.725  0 351 TYR GGG CA  1 ? 25 
ATOM   7792  C C   . TYR G  1 22  ? 13.368  0.503    49.246  1.000 42.857  0 351 TYR GGG C   1 ? 25 
ATOM   7793  O O   . TYR G  1 22  ? 14.260  1.338    49.562  1.000 45.154  0 351 TYR GGG O   1 ? 25 
ATOM   7794  C CB  . TYR G  1 22  ? 12.366  1.039    46.962  1.000 41.995  0 351 TYR GGG CB  1 ? 25 
ATOM   7795  C CG  . TYR G  1 22  ? 11.185  1.568    47.730  1.000 42.580  0 351 TYR GGG CG  1 ? 25 
ATOM   7796  C CD1 . TYR G  1 22  ? 10.016  0.829    47.838  1.000 41.835  0 351 TYR GGG CD1 1 ? 25 
ATOM   7797  C CD2 . TYR G  1 22  ? 11.272  2.783    48.398  1.000 44.221  0 351 TYR GGG CD2 1 ? 25 
ATOM   7798  C CE1 . TYR G  1 22  ? 8.952   1.290    48.593  1.000 44.530  0 351 TYR GGG CE1 1 ? 25 
ATOM   7799  C CE2 . TYR G  1 22  ? 10.223  3.255    49.163  1.000 46.883  0 351 TYR GGG CE2 1 ? 25 
ATOM   7800  C CZ  . TYR G  1 22  ? 9.057   2.502    49.261  1.000 46.735  0 351 TYR GGG CZ  1 ? 25 
ATOM   7801  O OH  . TYR G  1 22  ? 8.023   2.980    50.014  1.000 45.656  0 351 TYR GGG OH  1 ? 25 
ATOM   7802  N N   . ALA G  1 23  ? 12.511  -0.044   50.119  1.000 41.397  0 352 ALA GGG N   1 ? 25 
ATOM   7803  C CA  . ALA G  1 23  ? 12.485  0.256    51.571  1.000 44.048  0 352 ALA GGG CA  1 ? 25 
ATOM   7804  C C   . ALA G  1 23  ? 12.929  -0.990   52.349  1.000 42.308  0 352 ALA GGG C   1 ? 25 
ATOM   7805  O O   . ALA G  1 23  ? 12.299  -1.353   53.354  1.000 41.632  0 352 ALA GGG O   1 ? 25 
ATOM   7806  C CB  . ALA G  1 23  ? 11.102  0.699    51.969  1.000 46.285  0 352 ALA GGG CB  1 ? 25 
ATOM   7807  N N   . TRP G  1 24  ? 14.002  -1.615   51.882  1.000 42.729  0 353 TRP GGG N   1 ? 25 
ATOM   7808  C CA  . TRP G  1 24  ? 14.486  -2.914   52.403  1.000 42.354  0 353 TRP GGG CA  1 ? 25 
ATOM   7809  C C   . TRP G  1 24  ? 14.736  -2.802   53.905  1.000 44.505  0 353 TRP GGG C   1 ? 25 
ATOM   7810  O O   . TRP G  1 24  ? 15.184  -1.753   54.383  1.000 45.463  0 353 TRP GGG O   1 ? 25 
ATOM   7811  C CB  . TRP G  1 24  ? 15.716  -3.391   51.640  1.000 40.109  0 353 TRP GGG CB  1 ? 25 
ATOM   7812  C CG  . TRP G  1 24  ? 16.813  -2.385   51.473  1.000 39.521  0 353 TRP GGG CG  1 ? 25 
ATOM   7813  C CD1 . TRP G  1 24  ? 16.999  -1.519   50.434  1.000 38.790  0 353 TRP GGG CD1 1 ? 25 
ATOM   7814  C CD2 . TRP G  1 24  ? 17.942  -2.218   52.331  1.000 39.536  0 353 TRP GGG CD2 1 ? 25 
ATOM   7815  N NE1 . TRP G  1 24  ? 18.167  -0.834   50.588  1.000 38.817  0 353 TRP GGG NE1 1 ? 25 
ATOM   7816  C CE2 . TRP G  1 24  ? 18.771  -1.243   51.745  1.000 39.968  0 353 TRP GGG CE2 1 ? 25 
ATOM   7817  C CE3 . TRP G  1 24  ? 18.343  -2.813   53.527  1.000 41.996  0 353 TRP GGG CE3 1 ? 25 
ATOM   7818  C CZ2 . TRP G  1 24  ? 19.970  -0.834   52.336  1.000 42.008  0 353 TRP GGG CZ2 1 ? 25 
ATOM   7819  C CZ3 . TRP G  1 24  ? 19.530  -2.398   54.113  1.000 42.691  0 353 TRP GGG CZ3 1 ? 25 
ATOM   7820  C CH2 . TRP G  1 24  ? 20.328  -1.424   53.521  1.000 41.093  0 353 TRP GGG CH2 1 ? 25 
ATOM   7821  N N   . ASN G  1 25  ? 14.428  -3.878   54.614  1.000 44.945  0 354 ASN GGG N   1 ? 25 
ATOM   7822  C CA  . ASN G  1 25  ? 14.499  -3.938   56.090  1.000 44.714  0 354 ASN GGG CA  1 ? 25 
ATOM   7823  C C   . ASN G  1 25  ? 15.866  -4.482   56.513  1.000 43.944  0 354 ASN GGG C   1 ? 25 
ATOM   7824  O O   . ASN G  1 25  ? 16.320  -5.418   55.852  1.000 42.820  0 354 ASN GGG O   1 ? 25 
ATOM   7825  C CB  . ASN G  1 25  ? 13.326  -4.772   56.598  1.000 45.363  0 354 ASN GGG CB  1 ? 25 
ATOM   7826  C CG  . ASN G  1 25  ? 13.302  -4.831   58.098  1.000 45.889  0 354 ASN GGG CG  1 ? 25 
ATOM   7827  O OD1 . ASN G  1 25  ? 13.899  -5.719   58.718  1.000 47.312  0 354 ASN GGG OD1 1 ? 25 
ATOM   7828  N ND2 . ASN G  1 25  ? 12.671  -3.840   58.677  1.000 48.050  0 354 ASN GGG ND2 1 ? 25 
ATOM   7829  N N   . ARG G  1 26  ? 16.486  -3.879   57.533  1.000 45.598  0 355 ARG GGG N   1 ? 25 
ATOM   7830  C CA  . ARG G  1 26  ? 17.723  -4.323   58.232  1.000 46.145  0 355 ARG GGG CA  1 ? 25 
ATOM   7831  C C   . ARG G  1 26  ? 17.423  -4.796   59.653  1.000 46.800  0 355 ARG GGG C   1 ? 25 
ATOM   7832  O O   . ARG G  1 26  ? 16.967  -3.947   60.444  1.000 44.022  0 355 ARG GGG O   1 ? 25 
ATOM   7833  C CB  . ARG G  1 26  ? 18.614  -3.161   58.662  1.000 47.450  0 355 ARG GGG CB  1 ? 25 
ATOM   7834  C CG  . ARG G  1 26  ? 19.853  -2.922   57.852  1.000 47.736  0 355 ARG GGG CG  1 ? 25 
ATOM   7835  C CD  . ARG G  1 26  ? 21.201  -3.305   58.498  1.000 46.008  0 355 ARG GGG CD  1 ? 25 
ATOM   7836  N NE  . ARG G  1 26  ? 21.838  -3.730   57.255  1.000 48.204  0 355 ARG GGG NE  1 ? 25 
ATOM   7837  C CZ  . ARG G  1 26  ? 22.866  -3.178   56.642  1.000 46.705  0 355 ARG GGG CZ  1 ? 25 
ATOM   7838  N NH1 . ARG G  1 26  ? 23.563  -2.228   57.215  1.000 50.163  0 355 ARG GGG NH1 1 ? 25 
ATOM   7839  N NH2 . ARG G  1 26  ? 23.224  -3.624   55.460  1.000 47.358  0 355 ARG GGG NH2 1 ? 25 
ATOM   7840  N N   . LYS G  1 27  ? 17.823  -6.003   60.003  1.000 45.257  0 356 LYS GGG N   1 ? 25 
ATOM   7841  C CA  . LYS G  1 27  ? 17.858  -6.422   61.417  1.000 46.900  0 356 LYS GGG CA  1 ? 25 
ATOM   7842  C C   . LYS G  1 27  ? 19.324  -6.674   61.770  1.000 45.375  0 356 LYS GGG C   1 ? 25 
ATOM   7843  O O   . LYS G  1 27  ? 20.012  -7.373   61.008  1.000 45.898  0 356 LYS GGG O   1 ? 25 
ATOM   7844  C CB  . LYS G  1 27  ? 16.932  -7.620   61.660  1.000 48.146  0 356 LYS GGG CB  1 ? 25 
ATOM   7845  C CG  . LYS G  1 27  ? 17.014  -8.186   63.066  1.000 52.174  0 356 LYS GGG CG  1 ? 25 
ATOM   7846  C CD  . LYS G  1 27  ? 15.882  -9.100   63.450  1.000 57.213  0 356 LYS GGG CD  1 ? 25 
ATOM   7847  C CE  . LYS G  1 27  ? 16.064  -9.682   64.838  1.000 61.638  0 356 LYS GGG CE  1 ? 25 
ATOM   7848  N NZ  . LYS G  1 27  ? 15.878  -8.657   65.901  1.000 63.948  0 356 LYS GGG NZ  1 ? 25 
ATOM   7849  N N   . ARG G  1 28  ? 19.781  -6.077   62.858  1.000 44.288  0 357 ARG GGG N   1 ? 25 
ATOM   7850  C CA  . ARG G  1 28  ? 21.114  -6.340   63.427  1.000 46.388  0 357 ARG GGG CA  1 ? 25 
ATOM   7851  C C   . ARG G  1 28  ? 21.012  -7.620   64.257  1.000 45.339  0 357 ARG GGG C   1 ? 25 
ATOM   7852  O O   . ARG G  1 28  ? 20.073  -7.775   65.031  1.000 43.372  0 357 ARG GGG O   1 ? 25 
ATOM   7853  C CB  . ARG G  1 28  ? 21.543  -5.163   64.308  1.000 50.986  0 357 ARG GGG CB  1 ? 25 
ATOM   7854  C CG  . ARG G  1 28  ? 22.929  -5.288   64.907  1.000 55.810  0 357 ARG GGG CG  1 ? 25 
ATOM   7855  C CD  . ARG G  1 28  ? 23.398  -3.961   65.411  1.000 61.618  0 357 ARG GGG CD  1 ? 25 
ATOM   7856  N NE  . ARG G  1 28  ? 24.161  -4.320   66.582  1.000 67.787  0 357 ARG GGG NE  1 ? 25 
ATOM   7857  C CZ  . ARG G  1 28  ? 25.210  -3.655   67.036  1.000 79.929  0 357 ARG GGG CZ  1 ? 25 
ATOM   7858  N NH1 . ARG G  1 28  ? 25.641  -2.566   66.412  1.000 86.133  0 357 ARG GGG NH1 1 ? 25 
ATOM   7859  N NH2 . ARG G  1 28  ? 25.824  -4.073   68.138  1.000 81.456  0 357 ARG GGG NH2 1 ? 25 
ATOM   7860  N N   . ILE G  1 29  ? 21.963  -8.518   64.075  1.000 45.802  0 358 ILE GGG N   1 ? 25 
ATOM   7861  C CA  . ILE G  1 29  ? 22.119  -9.762   64.875  1.000 45.912  0 358 ILE GGG CA  1 ? 25 
ATOM   7862  C C   . ILE G  1 29  ? 23.468  -9.663   65.589  1.000 46.338  0 358 ILE GGG C   1 ? 25 
ATOM   7863  O O   . ILE G  1 29  ? 24.495  -9.448   64.889  1.000 45.072  0 358 ILE GGG O   1 ? 25 
ATOM   7864  C CB  . ILE G  1 29  ? 22.005  -10.974  63.927  1.000 44.830  0 358 ILE GGG CB  1 ? 25 
ATOM   7865  C CG1 . ILE G  1 29  ? 20.570  -11.095  63.429  1.000 45.210  0 358 ILE GGG CG1 1 ? 25 
ATOM   7866  C CG2 . ILE G  1 29  ? 22.467  -12.261  64.570  1.000 45.547  0 358 ILE GGG CG2 1 ? 25 
ATOM   7867  C CD1 . ILE G  1 29  ? 20.446  -11.932  62.198  1.000 46.249  0 358 ILE GGG CD1 1 ? 25 
ATOM   7868  N N   . SER G  1 30  ? 23.466  -9.822   66.916  1.000 45.842  0 359 SER GGG N   1 ? 25 
ATOM   7869  C CA  . SER G  1 30  ? 24.683  -9.798   67.760  1.000 46.855  0 359 SER GGG CA  1 ? 25 
ATOM   7870  C C   . SER G  1 30  ? 24.462  -10.504  69.101  1.000 47.012  0 359 SER GGG C   1 ? 25 
ATOM   7871  O O   . SER G  1 30  ? 23.321  -10.719  69.454  1.000 46.610  0 359 SER GGG O   1 ? 25 
ATOM   7872  C CB  . SER G  1 30  ? 25.141  -8.398   67.962  1.000 48.086  0 359 SER GGG CB  1 ? 25 
ATOM   7873  O OG  . SER G  1 30  ? 24.060  -7.602   68.378  1.000 50.214  0 359 SER GGG OG  1 ? 25 
ATOM   7874  N N   . ASN G  1 31  ? 25.540  -10.826  69.809  1.000 48.472  0 360 ASN GGG N   1 ? 25 
ATOM   7875  C CA  . ASN G  1 31  ? 25.510  -11.386  71.184  1.000 51.805  0 360 ASN GGG CA  1 ? 25 
ATOM   7876  C C   . ASN G  1 31  ? 24.573  -12.584  71.179  1.000 50.792  0 360 ASN GGG C   1 ? 25 
ATOM   7877  O O   . ASN G  1 31  ? 23.620  -12.593  71.961  1.000 53.137  0 360 ASN GGG O   1 ? 25 
ATOM   7878  C CB  . ASN G  1 31  ? 25.103  -10.336  72.221  1.000 54.635  0 360 ASN GGG CB  1 ? 25 
ATOM   7879  C CG  . ASN G  1 31  ? 26.078  -9.198   72.217  1.000 57.270  0 360 ASN GGG CG  1 ? 25 
ATOM   7880  O OD1 . ASN G  1 31  ? 27.186  -9.380   72.700  1.000 63.858  0 360 ASN GGG OD1 1 ? 25 
ATOM   7881  N ND2 . ASN G  1 31  ? 25.727  -8.089   71.593  1.000 57.501  0 360 ASN GGG ND2 1 ? 25 
ATOM   7882  N N   . CYS G  1 32  ? 24.861  -13.535  70.298  1.000 49.039  0 361 CYS GGG N   1 ? 25 
ATOM   7883  C CA  . CYS G  1 32  ? 24.050  -14.761  70.099  1.000 49.461  0 361 CYS GGG CA  1 ? 25 
ATOM   7884  C C   . CYS G  1 32  ? 24.885  -15.823  69.372  1.000 47.730  0 361 CYS GGG C   1 ? 25 
ATOM   7885  O O   . CYS G  1 32  ? 25.867  -15.445  68.672  1.000 46.637  0 361 CYS GGG O   1 ? 25 
ATOM   7886  C CB  . CYS G  1 32  ? 22.762  -14.423  69.345  1.000 49.224  0 361 CYS GGG CB  1 ? 25 
ATOM   7887  S SG  . CYS G  1 32  ? 23.020  -13.652  67.725  1.000 51.808  0 361 CYS GGG SG  1 ? 25 
ATOM   7888  N N   . VAL G  1 33  ? 24.490  -17.087  69.525  1.000 48.071  0 362 VAL GGG N   1 ? 25 
ATOM   7889  C CA  . VAL G  1 33  ? 25.069  -18.263  68.823  1.000 48.978  0 362 VAL GGG CA  1 ? 25 
ATOM   7890  C C   . VAL G  1 33  ? 24.344  -18.401  67.473  1.000 49.156  0 362 VAL GGG C   1 ? 25 
ATOM   7891  O O   . VAL G  1 33  ? 23.118  -18.573  67.471  1.000 46.701  0 362 VAL GGG O   1 ? 25 
ATOM   7892  C CB  . VAL G  1 33  ? 24.906  -19.551  69.659  1.000 49.915  0 362 VAL GGG CB  1 ? 25 
ATOM   7893  C CG1 . VAL G  1 33  ? 25.515  -20.742  68.948  1.000 49.619  0 362 VAL GGG CG1 1 ? 25 
ATOM   7894  C CG2 . VAL G  1 33  ? 25.448  -19.415  71.089  1.000 50.449  0 362 VAL GGG CG2 1 ? 25 
ATOM   7895  N N   . ALA G  1 34  ? 25.081  -18.295  66.367  1.000 51.317  0 363 ALA GGG N   1 ? 25 
ATOM   7896  C CA  . ALA G  1 34  ? 24.558  -18.404  64.978  1.000 53.029  0 363 ALA GGG CA  1 ? 25 
ATOM   7897  C C   . ALA G  1 34  ? 24.615  -19.878  64.602  1.000 52.839  0 363 ALA GGG C   1 ? 25 
ATOM   7898  O O   . ALA G  1 34  ? 25.671  -20.350  64.151  1.000 55.188  0 363 ALA GGG O   1 ? 25 
ATOM   7899  C CB  . ALA G  1 34  ? 25.349  -17.564  63.996  1.000 49.402  0 363 ALA GGG CB  1 ? 25 
ATOM   7900  N N   . ASP G  1 35  ? 23.514  -20.584  64.823  1.000 53.291  0 364 ASP GGG N   1 ? 25 
ATOM   7901  C CA  . ASP G  1 35  ? 23.348  -21.965  64.330  1.000 54.018  0 364 ASP GGG CA  1 ? 25 
ATOM   7902  C C   . ASP G  1 35  ? 22.673  -21.900  62.963  1.000 53.398  0 364 ASP GGG C   1 ? 25 
ATOM   7903  O O   . ASP G  1 35  ? 21.485  -21.561  62.903  1.000 52.008  0 364 ASP GGG O   1 ? 25 
ATOM   7904  C CB  . ASP G  1 35  ? 22.550  -22.837  65.290  1.000 55.892  0 364 ASP GGG CB  1 ? 25 
ATOM   7905  C CG  . ASP G  1 35  ? 22.820  -24.288  64.973  1.000 57.566  0 364 ASP GGG CG  1 ? 25 
ATOM   7906  O OD1 . ASP G  1 35  ? 23.387  -24.540  63.881  1.000 55.643  0 364 ASP GGG OD1 1 ? 25 
ATOM   7907  O OD2 . ASP G  1 35  ? 22.494  -25.145  65.824  1.000 61.721  0 364 ASP GGG OD2 1 ? 25 
ATOM   7908  N N   . TYR G  1 36  ? 23.420  -22.239  61.919  1.000 52.810  0 365 TYR GGG N   1 ? 25 
ATOM   7909  C CA  . TYR G  1 36  ? 22.959  -22.159  60.514  1.000 53.932  0 365 TYR GGG CA  1 ? 25 
ATOM   7910  C C   . TYR G  1 36  ? 22.309  -23.483  60.108  1.000 55.875  0 365 TYR GGG C   1 ? 25 
ATOM   7911  O O   . TYR G  1 36  ? 21.798  -23.539  58.981  1.000 55.974  0 365 TYR GGG O   1 ? 25 
ATOM   7912  C CB  . TYR G  1 36  ? 24.121  -21.803  59.581  1.000 53.461  0 365 TYR GGG CB  1 ? 25 
ATOM   7913  C CG  . TYR G  1 36  ? 24.541  -20.372  59.717  1.000 50.418  0 365 TYR GGG CG  1 ? 25 
ATOM   7914  C CD1 . TYR G  1 36  ? 25.492  -20.004  60.646  1.000 50.356  0 365 TYR GGG CD1 1 ? 25 
ATOM   7915  C CD2 . TYR G  1 36  ? 23.978  -19.384  58.935  1.000 51.883  0 365 TYR GGG CD2 1 ? 25 
ATOM   7916  C CE1 . TYR G  1 36  ? 25.878  -18.686  60.800  1.000 48.784  0 365 TYR GGG CE1 1 ? 25 
ATOM   7917  C CE2 . TYR G  1 36  ? 24.341  -18.053  59.081  1.000 51.459  0 365 TYR GGG CE2 1 ? 25 
ATOM   7918  C CZ  . TYR G  1 36  ? 25.288  -17.709  60.023  1.000 49.825  0 365 TYR GGG CZ  1 ? 25 
ATOM   7919  O OH  . TYR G  1 36  ? 25.689  -16.420  60.152  1.000 52.671  0 365 TYR GGG OH  1 ? 25 
ATOM   7920  N N   . SER G  1 37  ? 22.280  -24.497  60.979  1.000 56.559  0 366 SER GGG N   1 ? 25 
ATOM   7921  C CA  . SER G  1 37  ? 21.673  -25.800  60.619  1.000 60.822  0 366 SER GGG CA  1 ? 25 
ATOM   7922  C C   . SER G  1 37  ? 20.172  -25.608  60.373  1.000 61.175  0 366 SER GGG C   1 ? 25 
ATOM   7923  O O   . SER G  1 37  ? 19.633  -26.383  59.617  1.000 65.417  0 366 SER GGG O   1 ? 25 
ATOM   7924  C CB  . SER G  1 37  ? 21.988  -26.909  61.592  1.000 61.677  0 366 SER GGG CB  1 ? 25 
ATOM   7925  O OG  . SER G  1 37  ? 21.835  -26.464  62.908  1.000 61.011  0 366 SER GGG OG  1 ? 25 
ATOM   7926  N N   . VAL G  1 38  ? 19.533  -24.579  60.917  1.000 61.086  0 367 VAL GGG N   1 ? 25 
ATOM   7927  C CA  . VAL G  1 38  ? 18.112  -24.273  60.587  1.000 62.140  0 367 VAL GGG CA  1 ? 25 
ATOM   7928  C C   . VAL G  1 38  ? 18.004  -23.991  59.076  1.000 60.370  0 367 VAL GGG C   1 ? 25 
ATOM   7929  O O   . VAL G  1 38  ? 17.103  -24.556  58.426  1.000 64.749  0 367 VAL GGG O   1 ? 25 
ATOM   7930  C CB  . VAL G  1 38  ? 17.559  -23.148  61.486  1.000 63.136  0 367 VAL GGG CB  1 ? 25 
ATOM   7931  C CG1 . VAL G  1 38  ? 18.142  -21.788  61.167  1.000 60.959  0 367 VAL GGG CG1 1 ? 25 
ATOM   7932  C CG2 . VAL G  1 38  ? 16.044  -23.091  61.436  1.000 66.230  0 367 VAL GGG CG2 1 ? 25 
ATOM   7933  N N   . LEU G  1 39  ? 18.939  -23.225  58.508  1.000 57.040  0 368 LEU GGG N   1 ? 25 
ATOM   7934  C CA  . LEU G  1 39  ? 18.975  -22.906  57.053  1.000 55.037  0 368 LEU GGG CA  1 ? 25 
ATOM   7935  C C   . LEU G  1 39  ? 19.402  -24.121  56.230  1.000 57.134  0 368 LEU GGG C   1 ? 25 
ATOM   7936  O O   . LEU G  1 39  ? 18.882  -24.285  55.119  1.000 60.400  0 368 LEU GGG O   1 ? 25 
ATOM   7937  C CB  . LEU G  1 39  ? 19.929  -21.731  56.838  1.000 52.540  0 368 LEU GGG CB  1 ? 25 
ATOM   7938  C CG  . LEU G  1 39  ? 19.559  -20.455  57.593  1.000 51.139  0 368 LEU GGG CG  1 ? 25 
ATOM   7939  C CD1 . LEU G  1 39  ? 20.529  -19.321  57.324  1.000 47.548  0 368 LEU GGG CD1 1 ? 25 
ATOM   7940  C CD2 . LEU G  1 39  ? 18.143  -20.070  57.232  1.000 51.442  0 368 LEU GGG CD2 1 ? 25 
ATOM   7941  N N   . TYR G  1 40  ? 20.320  -24.934  56.744  1.000 58.547  0 369 TYR GGG N   1 ? 25 
ATOM   7942  C CA  . TYR G  1 40  ? 20.865  -26.128  56.042  1.000 62.868  0 369 TYR GGG CA  1 ? 25 
ATOM   7943  C C   . TYR G  1 40  ? 19.749  -27.152  55.796  1.000 66.185  0 369 TYR GGG C   1 ? 25 
ATOM   7944  O O   . TYR G  1 40  ? 19.856  -27.900  54.817  1.000 68.895  0 369 TYR GGG O   1 ? 25 
ATOM   7945  C CB  . TYR G  1 40  ? 21.986  -26.810  56.836  1.000 63.308  0 369 TYR GGG CB  1 ? 25 
ATOM   7946  C CG  . TYR G  1 40  ? 23.284  -26.056  56.970  1.000 62.053  0 369 TYR GGG CG  1 ? 25 
ATOM   7947  C CD1 . TYR G  1 40  ? 23.722  -25.150  56.005  1.000 61.406  0 369 TYR GGG CD1 1 ? 25 
ATOM   7948  C CD2 . TYR G  1 40  ? 24.100  -26.287  58.074  1.000 62.894  0 369 TYR GGG CD2 1 ? 25 
ATOM   7949  C CE1 . TYR G  1 40  ? 24.914  -24.456  56.159  1.000 61.583  0 369 TYR GGG CE1 1 ? 25 
ATOM   7950  C CE2 . TYR G  1 40  ? 25.305  -25.618  58.242  1.000 62.131  0 369 TYR GGG CE2 1 ? 25 
ATOM   7951  C CZ  . TYR G  1 40  ? 25.703  -24.694  57.283  1.000 63.457  0 369 TYR GGG CZ  1 ? 25 
ATOM   7952  O OH  . TYR G  1 40  ? 26.891  -24.057  57.435  1.000 62.610  0 369 TYR GGG OH  1 ? 25 
ATOM   7953  N N   . ASN G  1 41  ? 18.732  -27.189  56.663  1.000 67.491  0 370 ASN GGG N   1 ? 25 
ATOM   7954  C CA  . ASN G  1 41  ? 17.658  -28.223  56.669  1.000 72.994  0 370 ASN GGG CA  1 ? 25 
ATOM   7955  C C   . ASN G  1 41  ? 16.437  -27.753  55.881  1.000 75.030  0 370 ASN GGG C   1 ? 25 
ATOM   7956  O O   . ASN G  1 41  ? 15.432  -28.468  55.904  1.000 76.813  0 370 ASN GGG O   1 ? 25 
ATOM   7957  C CB  . ASN G  1 41  ? 17.256  -28.600  58.094  1.000 71.923  0 370 ASN GGG CB  1 ? 25 
ATOM   7958  C CG  . ASN G  1 41  ? 18.392  -29.293  58.818  1.000 72.298  0 370 ASN GGG CG  1 ? 25 
ATOM   7959  O OD1 . ASN G  1 41  ? 19.101  -30.107  58.235  1.000 75.474  0 370 ASN GGG OD1 1 ? 25 
ATOM   7960  N ND2 . ASN G  1 41  ? 18.582  -28.979  60.085  1.000 70.702  0 370 ASN GGG ND2 1 ? 25 
ATOM   7961  N N   . SER G  1 42  ? 16.533  -26.610  55.198  1.000 75.485  0 371 SER GGG N   1 ? 25 
ATOM   7962  C CA  . SER G  1 42  ? 15.519  -26.111  54.233  1.000 77.957  0 371 SER GGG CA  1 ? 25 
ATOM   7963  C C   . SER G  1 42  ? 15.888  -26.614  52.838  1.000 81.836  0 371 SER GGG C   1 ? 25 
ATOM   7964  O O   . SER G  1 42  ? 17.052  -26.455  52.438  1.000 83.207  0 371 SER GGG O   1 ? 25 
ATOM   7965  C CB  . SER G  1 42  ? 15.433  -24.614  54.283  1.000 76.081  0 371 SER GGG CB  1 ? 25 
ATOM   7966  O OG  . SER G  1 42  ? 15.271  -24.144  55.635  1.000 74.672  0 371 SER GGG OG  1 ? 25 
ATOM   7967  N N   . ALA G  1 43  ? 14.931  -27.230  52.135  1.000 85.148  0 372 ALA GGG N   1 ? 25 
ATOM   7968  C CA  . ALA G  1 43  ? 15.053  -27.699  50.734  1.000 83.850  0 372 ALA GGG CA  1 ? 25 
ATOM   7969  C C   . ALA G  1 43  ? 14.260  -26.758  49.815  1.000 79.681  0 372 ALA GGG C   1 ? 25 
ATOM   7970  O O   . ALA G  1 43  ? 14.233  -26.975  48.602  1.000 84.269  0 372 ALA GGG O   1 ? 25 
ATOM   7971  C CB  . ALA G  1 43  ? 14.558  -29.116  50.640  1.000 87.218  0 372 ALA GGG CB  1 ? 25 
ATOM   7972  N N   . SER G  1 44  ? 13.655  -25.720  50.380  1.000 72.798  0 373 SER GGG N   1 ? 25 
ATOM   7973  C CA  . SER G  1 44  ? 12.771  -24.765  49.665  1.000 70.591  0 373 SER GGG CA  1 ? 25 
ATOM   7974  C C   . SER G  1 44  ? 13.559  -23.612  49.038  1.000 67.334  0 373 SER GGG C   1 ? 25 
ATOM   7975  O O   . SER G  1 44  ? 13.012  -23.002  48.146  1.000 66.708  0 373 SER GGG O   1 ? 25 
ATOM   7976  C CB  . SER G  1 44  ? 11.730  -24.232  50.592  1.000 69.403  0 373 SER GGG CB  1 ? 25 
ATOM   7977  O OG  . SER G  1 44  ? 10.632  -25.124  50.630  1.000 72.833  0 373 SER GGG OG  1 ? 25 
ATOM   7978  N N   . PHE G  1 45  ? 14.770  -23.308  49.514  1.000 45.214  0 374 PHE GGG N   1 ? 26 
ATOM   7979  C CA  . PHE G  1 45  ? 15.507  -22.115  49.047  1.000 44.219  0 374 PHE GGG CA  1 ? 26 
ATOM   7980  C C   . PHE G  1 45  ? 15.847  -22.299  47.568  1.000 45.501  0 374 PHE GGG C   1 ? 26 
ATOM   7981  O O   . PHE G  1 45  ? 16.348  -23.381  47.200  1.000 47.022  0 374 PHE GGG O   1 ? 26 
ATOM   7982  C CB  . PHE G  1 45  ? 16.749  -21.876  49.899  1.000 43.797  0 374 PHE GGG CB  1 ? 26 
ATOM   7983  C CG  . PHE G  1 45  ? 16.489  -21.510  51.340  1.000 43.861  0 374 PHE GGG CG  1 ? 26 
ATOM   7984  C CD1 . PHE G  1 45  ? 15.433  -20.689  51.695  1.000 42.068  0 374 PHE GGG CD1 1 ? 26 
ATOM   7985  C CD2 . PHE G  1 45  ? 17.344  -21.953  52.346  1.000 43.431  0 374 PHE GGG CD2 1 ? 26 
ATOM   7986  C CE1 . PHE G  1 45  ? 15.233  -20.337  53.023  1.000 41.434  0 374 PHE GGG CE1 1 ? 26 
ATOM   7987  C CE2 . PHE G  1 45  ? 17.156  -21.559  53.665  1.000 42.382  0 374 PHE GGG CE2 1 ? 26 
ATOM   7988  C CZ  . PHE G  1 45  ? 16.109  -20.740  53.996  1.000 40.813  0 374 PHE GGG CZ  1 ? 26 
ATOM   7989  N N   . SER G  1 46  ? 15.578  -21.287  46.736  1.000 45.234  0 375 SER GGG N   1 ? 26 
ATOM   7990  C CA  . SER G  1 46  ? 15.890  -21.302  45.274  1.000 46.399  0 375 SER GGG CA  1 ? 26 
ATOM   7991  C C   . SER G  1 46  ? 17.399  -21.084  45.075  1.000 45.550  0 375 SER GGG C   1 ? 26 
ATOM   7992  O O   . SER G  1 46  ? 17.951  -21.589  44.105  1.000 46.625  0 375 SER GGG O   1 ? 26 
ATOM   7993  C CB  . SER G  1 46  ? 15.096  -20.262  44.514  1.000 45.806  0 375 SER GGG CB  1 ? 26 
ATOM   7994  O OG  . SER G  1 46  ? 15.297  -18.951  45.056  1.000 45.147  0 375 SER GGG OG  1 ? 26 
ATOM   7995  N N   . THR G  1 47  ? 18.032  -20.348  45.991  1.000 43.267  0 376 THR GGG N   1 ? 26 
ATOM   7996  C CA  . THR G  1 47  ? 19.455  -19.972  45.927  1.000 43.381  0 376 THR GGG CA  1 ? 26 
ATOM   7997  C C   . THR G  1 47  ? 19.978  -19.784  47.358  1.000 42.883  0 376 THR GGG C   1 ? 26 
ATOM   7998  O O   . THR G  1 47  ? 19.221  -19.358  48.240  1.000 42.180  0 376 THR GGG O   1 ? 26 
ATOM   7999  C CB  . THR G  1 47  ? 19.619  -18.750  45.018  1.000 43.752  0 376 THR GGG CB  1 ? 26 
ATOM   8000  O OG1 . THR G  1 47  ? 21.003  -18.586  44.695  1.000 48.482  0 376 THR GGG OG1 1 ? 26 
ATOM   8001  C CG2 . THR G  1 47  ? 19.072  -17.497  45.657  1.000 42.590  0 376 THR GGG CG2 1 ? 26 
ATOM   8002  N N   . PHE G  1 48  ? 21.236  -20.124  47.584  1.000 41.435  0 377 PHE GGG N   1 ? 26 
ATOM   8003  C CA  . PHE G  1 48  ? 21.900  -19.997  48.904  1.000 40.886  0 377 PHE GGG CA  1 ? 26 
ATOM   8004  C C   . PHE G  1 48  ? 23.385  -19.941  48.589  1.000 39.082  0 377 PHE GGG C   1 ? 26 
ATOM   8005  O O   . PHE G  1 48  ? 24.010  -20.984  48.458  1.000 41.077  0 377 PHE GGG O   1 ? 26 
ATOM   8006  C CB  . PHE G  1 48  ? 21.481  -21.137  49.841  1.000 42.634  0 377 PHE GGG CB  1 ? 26 
ATOM   8007  C CG  . PHE G  1 48  ? 22.088  -21.154  51.229  1.000 43.165  0 377 PHE GGG CG  1 ? 26 
ATOM   8008  C CD1 . PHE G  1 48  ? 23.148  -20.326  51.590  1.000 43.879  0 377 PHE GGG CD1 1 ? 26 
ATOM   8009  C CD2 . PHE G  1 48  ? 21.616  -22.055  52.174  1.000 44.147  0 377 PHE GGG CD2 1 ? 26 
ATOM   8010  C CE1 . PHE G  1 48  ? 23.681  -20.362  52.873  1.000 44.870  0 377 PHE GGG CE1 1 ? 26 
ATOM   8011  C CE2 . PHE G  1 48  ? 22.142  -22.086  53.458  1.000 44.788  0 377 PHE GGG CE2 1 ? 26 
ATOM   8012  C CZ  . PHE G  1 48  ? 23.175  -21.244  53.806  1.000 45.504  0 377 PHE GGG CZ  1 ? 26 
ATOM   8013  N N   . LYS G  1 49  ? 23.891  -18.737  48.385  1.000 40.436  0 378 LYS GGG N   1 ? 26 
ATOM   8014  C CA  . LYS G  1 49  ? 25.301  -18.504  47.986  1.000 41.951  0 378 LYS GGG CA  1 ? 26 
ATOM   8015  C C   . LYS G  1 49  ? 25.978  -17.583  48.985  1.000 41.059  0 378 LYS GGG C   1 ? 26 
ATOM   8016  O O   . LYS G  1 49  ? 25.354  -16.602  49.408  1.000 41.866  0 378 LYS GGG O   1 ? 26 
ATOM   8017  C CB  . LYS G  1 49  ? 25.403  -17.815  46.636  1.000 42.407  0 378 LYS GGG CB  1 ? 26 
ATOM   8018  C CG  . LYS G  1 49  ? 24.823  -18.588  45.464  1.000 44.092  0 378 LYS GGG CG  1 ? 26 
ATOM   8019  C CD  . LYS G  1 49  ? 24.961  -17.720  44.254  1.000 43.196  0 378 LYS GGG CD  1 ? 26 
ATOM   8020  C CE  . LYS G  1 49  ? 24.570  -18.372  42.966  1.000 45.988  0 378 LYS GGG CE  1 ? 26 
ATOM   8021  N NZ  . LYS G  1 49  ? 24.841  -17.405  41.884  1.000 47.123  0 378 LYS GGG NZ  1 ? 26 
ATOM   8022  N N   . CYS G  1 50  ? 27.231  -17.892  49.292  1.000 40.022  0 379 CYS GGG N   1 ? 26 
ATOM   8023  C CA  . CYS G  1 50  ? 28.082  -17.038  50.136  1.000 39.650  0 379 CYS GGG CA  1 ? 26 
ATOM   8024  C C   . CYS G  1 50  ? 29.228  -16.482  49.293  1.000 39.524  0 379 CYS GGG C   1 ? 26 
ATOM   8025  O O   . CYS G  1 50  ? 29.578  -17.073  48.253  1.000 37.532  0 379 CYS GGG O   1 ? 26 
ATOM   8026  C CB  . CYS G  1 50  ? 28.525  -17.806  51.379  1.000 42.939  0 379 CYS GGG CB  1 ? 26 
ATOM   8027  S SG  . CYS G  1 50  ? 27.119  -18.428  52.349  1.000 46.751  0 379 CYS GGG SG  1 ? 26 
ATOM   8028  N N   . TYR G  1 51  ? 29.744  -15.347  49.745  1.000 39.746  0 380 TYR GGG N   1 ? 26 
ATOM   8029  C CA  . TYR G  1 51  ? 30.837  -14.559  49.139  1.000 40.238  0 380 TYR GGG CA  1 ? 26 
ATOM   8030  C C   . TYR G  1 51  ? 31.859  -14.301  50.257  1.000 41.110  0 380 TYR GGG C   1 ? 26 
ATOM   8031  O O   . TYR G  1 51  ? 31.474  -13.783  51.323  1.000 44.826  0 380 TYR GGG O   1 ? 26 
ATOM   8032  C CB  . TYR G  1 51  ? 30.224  -13.284  48.538  1.000 39.706  0 380 TYR GGG CB  1 ? 26 
ATOM   8033  C CG  . TYR G  1 51  ? 29.120  -13.548  47.537  1.000 38.956  0 380 TYR GGG CG  1 ? 26 
ATOM   8034  C CD1 . TYR G  1 51  ? 27.807  -13.751  47.941  1.000 38.977  0 380 TYR GGG CD1 1 ? 26 
ATOM   8035  C CD2 . TYR G  1 51  ? 29.396  -13.675  46.186  1.000 39.418  0 380 TYR GGG CD2 1 ? 26 
ATOM   8036  C CE1 . TYR G  1 51  ? 26.793  -14.013  47.031  1.000 38.224  0 380 TYR GGG CE1 1 ? 26 
ATOM   8037  C CE2 . TYR G  1 51  ? 28.400  -13.935  45.265  1.000 38.775  0 380 TYR GGG CE2 1 ? 26 
ATOM   8038  C CZ  . TYR G  1 51  ? 27.101  -14.124  45.691  1.000 37.898  0 380 TYR GGG CZ  1 ? 26 
ATOM   8039  O OH  . TYR G  1 51  ? 26.155  -14.399  44.759  1.000 40.237  0 380 TYR GGG OH  1 ? 26 
ATOM   8040  N N   . GLY G  1 52  ? 33.116  -14.672  50.063  1.000 40.689  0 381 GLY GGG N   1 ? 26 
ATOM   8041  C CA  . GLY G  1 52  ? 34.168  -14.450  51.062  1.000 42.607  0 381 GLY GGG CA  1 ? 26 
ATOM   8042  C C   . GLY G  1 52  ? 34.222  -15.555  52.103  1.000 45.222  0 381 GLY GGG C   1 ? 26 
ATOM   8043  O O   . GLY G  1 52  ? 35.247  -15.641  52.808  1.000 51.076  0 381 GLY GGG O   1 ? 26 
ATOM   8044  N N   . VAL G  1 53  ? 33.209  -16.417  52.205  1.000 44.460  0 382 VAL GGG N   1 ? 26 
ATOM   8045  C CA  . VAL G  1 53  ? 33.251  -17.621  53.085  1.000 46.339  0 382 VAL GGG CA  1 ? 26 
ATOM   8046  C C   . VAL G  1 53  ? 32.515  -18.774  52.420  1.000 44.905  0 382 VAL GGG C   1 ? 26 
ATOM   8047  O O   . VAL G  1 53  ? 31.576  -18.513  51.689  1.000 44.209  0 382 VAL GGG O   1 ? 26 
ATOM   8048  C CB  . VAL G  1 53  ? 32.635  -17.312  54.455  1.000 47.191  0 382 VAL GGG CB  1 ? 26 
ATOM   8049  C CG1 . VAL G  1 53  ? 33.514  -16.347  55.232  1.000 49.425  0 382 VAL GGG CG1 1 ? 26 
ATOM   8050  C CG2 . VAL G  1 53  ? 31.202  -16.809  54.326  1.000 45.732  0 382 VAL GGG CG2 1 ? 26 
ATOM   8051  N N   . SER G  1 54  ? 32.916  -20.002  52.703  1.000 47.339  0 383 SER GGG N   1 ? 26 
ATOM   8052  C CA  . SER G  1 54  ? 32.220  -21.206  52.202  1.000 49.463  0 383 SER GGG CA  1 ? 26 
ATOM   8053  C C   . SER G  1 54  ? 30.970  -21.430  53.052  1.000 48.624  0 383 SER GGG C   1 ? 26 
ATOM   8054  O O   . SER G  1 54  ? 31.033  -21.335  54.269  1.000 47.265  0 383 SER GGG O   1 ? 26 
ATOM   8055  C CB  . SER G  1 54  ? 33.117  -22.395  52.195  1.000 52.784  0 383 SER GGG CB  1 ? 26 
ATOM   8056  O OG  . SER G  1 54  ? 32.384  -23.540  51.796  1.000 59.987  0 383 SER GGG OG  1 ? 26 
ATOM   8057  N N   . PRO G  1 55  ? 29.795  -21.710  52.436  1.000 50.330  0 384 PRO GGG N   1 ? 26 
ATOM   8058  C CA  . PRO G  1 55  ? 28.596  -22.071  53.190  1.000 51.324  0 384 PRO GGG CA  1 ? 26 
ATOM   8059  C C   . PRO G  1 55  ? 28.819  -23.252  54.151  1.000 53.958  0 384 PRO GGG C   1 ? 26 
ATOM   8060  O O   . PRO G  1 55  ? 28.139  -23.326  55.180  1.000 53.257  0 384 PRO GGG O   1 ? 26 
ATOM   8061  C CB  . PRO G  1 55  ? 27.588  -22.478  52.108  1.000 51.294  0 384 PRO GGG CB  1 ? 26 
ATOM   8062  C CG  . PRO G  1 55  ? 28.045  -21.720  50.875  1.000 50.119  0 384 PRO GGG CG  1 ? 26 
ATOM   8063  C CD  . PRO G  1 55  ? 29.550  -21.662  50.981  1.000 50.612  0 384 PRO GGG CD  1 ? 26 
ATOM   8064  N N   . THR G  1 56  ? 29.773  -24.127  53.809  1.000 54.272  0 385 THR GGG N   1 ? 26 
ATOM   8065  C CA  . THR G  1 56  ? 30.117  -25.331  54.605  1.000 55.183  0 385 THR GGG CA  1 ? 26 
ATOM   8066  C C   . THR G  1 56  ? 30.783  -24.928  55.924  1.000 53.390  0 385 THR GGG C   1 ? 26 
ATOM   8067  O O   . THR G  1 56  ? 30.903  -25.784  56.783  1.000 55.351  0 385 THR GGG O   1 ? 26 
ATOM   8068  C CB  . THR G  1 56  ? 31.021  -26.297  53.817  1.000 56.794  0 385 THR GGG CB  1 ? 26 
ATOM   8069  O OG1 . THR G  1 56  ? 32.303  -25.693  53.570  1.000 56.892  0 385 THR GGG OG1 1 ? 26 
ATOM   8070  C CG2 . THR G  1 56  ? 30.361  -26.762  52.536  1.000 54.262  0 385 THR GGG CG2 1 ? 26 
ATOM   8071  N N   . LYS G  1 57  ? 31.236  -23.690  56.070  1.000 53.114  0 386 LYS GGG N   1 ? 26 
ATOM   8072  C CA  . LYS G  1 57  ? 32.036  -23.265  57.243  1.000 54.636  0 386 LYS GGG CA  1 ? 26 
ATOM   8073  C C   . LYS G  1 57  ? 31.217  -22.348  58.160  1.000 48.521  0 386 LYS GGG C   1 ? 26 
ATOM   8074  O O   . LYS G  1 57  ? 31.794  -21.893  59.122  1.000 48.365  0 386 LYS GGG O   1 ? 26 
ATOM   8075  C CB  . LYS G  1 57  ? 33.266  -22.528  56.716  1.000 59.108  0 386 LYS GGG CB  1 ? 26 
ATOM   8076  C CG  . LYS G  1 57  ? 34.244  -23.422  55.987  1.000 65.919  0 386 LYS GGG CG  1 ? 26 
ATOM   8077  C CD  . LYS G  1 57  ? 35.403  -23.687  56.870  1.000 72.301  0 386 LYS GGG CD  1 ? 26 
ATOM   8078  C CE  . LYS G  1 57  ? 36.338  -22.491  56.964  1.000 76.459  0 386 LYS GGG CE  1 ? 26 
ATOM   8079  N NZ  . LYS G  1 57  ? 36.882  -22.364  58.335  1.000 79.650  0 386 LYS GGG NZ  1 ? 26 
ATOM   8080  N N   . LEU G  1 58  ? 29.974  -22.004  57.837  1.000 44.477  0 387 LEU GGG N   1 ? 26 
ATOM   8081  C CA  . LEU G  1 58  ? 29.258  -20.914  58.570  1.000 44.449  0 387 LEU GGG CA  1 ? 26 
ATOM   8082  C C   . LEU G  1 58  ? 29.169  -21.209  60.078  1.000 44.145  0 387 LEU GGG C   1 ? 26 
ATOM   8083  O O   . LEU G  1 58  ? 29.241  -20.255  60.857  1.000 43.303  0 387 LEU GGG O   1 ? 26 
ATOM   8084  C CB  . LEU G  1 58  ? 27.872  -20.703  57.965  1.000 42.652  0 387 LEU GGG CB  1 ? 26 
ATOM   8085  C CG  . LEU G  1 58  ? 27.845  -20.138  56.555  1.000 42.060  0 387 LEU GGG CG  1 ? 26 
ATOM   8086  C CD1 . LEU G  1 58  ? 26.431  -19.973  56.042  1.000 40.402  0 387 LEU GGG CD1 1 ? 26 
ATOM   8087  C CD2 . LEU G  1 58  ? 28.581  -18.825  56.484  1.000 43.506  0 387 LEU GGG CD2 1 ? 26 
ATOM   8088  N N   . ASN G  1 59  ? 29.082  -22.467  60.484  1.000 46.009  0 388 ASN GGG N   1 ? 26 
ATOM   8089  C CA  . ASN G  1 59  ? 28.977  -22.825  61.929  1.000 50.254  0 388 ASN GGG CA  1 ? 26 
ATOM   8090  C C   . ASN G  1 59  ? 30.323  -22.725  62.654  1.000 51.428  0 388 ASN GGG C   1 ? 26 
ATOM   8091  O O   . ASN G  1 59  ? 30.324  -22.918  63.866  1.000 54.300  0 388 ASN GGG O   1 ? 26 
ATOM   8092  C CB  . ASN G  1 59  ? 28.340  -24.207  62.123  1.000 51.389  0 388 ASN GGG CB  1 ? 26 
ATOM   8093  C CG  . ASN G  1 59  ? 26.833  -24.111  62.160  1.000 52.902  0 388 ASN GGG CG  1 ? 26 
ATOM   8094  O OD1 . ASN G  1 59  ? 26.279  -23.030  62.341  1.000 52.630  0 388 ASN GGG OD1 1 ? 26 
ATOM   8095  N ND2 . ASN G  1 59  ? 26.159  -25.218  61.925  1.000 58.585  0 388 ASN GGG ND2 1 ? 26 
ATOM   8096  N N   . ASP G  1 60  ? 31.413  -22.424  61.945  1.000 54.032  0 389 ASP GGG N   1 ? 26 
ATOM   8097  C CA  . ASP G  1 60  ? 32.786  -22.389  62.514  1.000 57.387  0 389 ASP GGG CA  1 ? 26 
ATOM   8098  C C   . ASP G  1 60  ? 33.366  -20.973  62.457  1.000 53.908  0 389 ASP GGG C   1 ? 26 
ATOM   8099  O O   . ASP G  1 60  ? 34.554  -20.821  62.685  1.000 55.485  0 389 ASP GGG O   1 ? 26 
ATOM   8100  C CB  . ASP G  1 60  ? 33.740  -23.310  61.755  1.000 62.061  0 389 ASP GGG CB  1 ? 26 
ATOM   8101  C CG  . ASP G  1 60  ? 33.270  -24.751  61.693  1.000 67.879  0 389 ASP GGG CG  1 ? 26 
ATOM   8102  O OD1 . ASP G  1 60  ? 33.107  -25.360  62.777  1.000 72.645  0 389 ASP GGG OD1 1 ? 26 
ATOM   8103  O OD2 . ASP G  1 60  ? 33.018  -25.245  60.552  1.000 70.835  0 389 ASP GGG OD2 1 ? 26 
ATOM   8104  N N   . LEU G  1 61  ? 32.575  -19.955  62.158  1.000 50.683  0 390 LEU GGG N   1 ? 26 
ATOM   8105  C CA  . LEU G  1 61  ? 33.066  -18.564  61.988  1.000 50.628  0 390 LEU GGG CA  1 ? 26 
ATOM   8106  C C   . LEU G  1 61  ? 32.568  -17.688  63.150  1.000 48.966  0 390 LEU GGG C   1 ? 26 
ATOM   8107  O O   . LEU G  1 61  ? 31.480  -17.983  63.694  1.000 48.686  0 390 LEU GGG O   1 ? 26 
ATOM   8108  C CB  . LEU G  1 61  ? 32.585  -18.006  60.651  1.000 50.433  0 390 LEU GGG CB  1 ? 26 
ATOM   8109  C CG  . LEU G  1 61  ? 32.983  -18.792  59.403  1.000 54.059  0 390 LEU GGG CG  1 ? 26 
ATOM   8110  C CD1 . LEU G  1 61  ? 32.332  -18.195  58.163  1.000 51.930  0 390 LEU GGG CD1 1 ? 26 
ATOM   8111  C CD2 . LEU G  1 61  ? 34.498  -18.898  59.228  1.000 57.420  0 390 LEU GGG CD2 1 ? 26 
ATOM   8112  N N   . CYS G  1 62  ? 33.337  -16.666  63.508  1.000 48.546  0 391 CYS GGG N   1 ? 26 
ATOM   8113  C CA  . CYS G  1 62  ? 32.948  -15.576  64.426  1.000 48.524  0 391 CYS GGG CA  1 ? 26 
ATOM   8114  C C   . CYS G  1 62  ? 32.984  -14.256  63.656  1.000 45.612  0 391 CYS GGG C   1 ? 26 
ATOM   8115  O O   . CYS G  1 62  ? 33.924  -14.048  62.901  1.000 46.421  0 391 CYS GGG O   1 ? 26 
ATOM   8116  C CB  . CYS G  1 62  ? 33.871  -15.522  65.643  1.000 52.246  0 391 CYS GGG CB  1 ? 26 
ATOM   8117  S SG  . CYS G  1 62  ? 33.689  -16.951  66.737  1.000 58.038  0 391 CYS GGG SG  1 ? 26 
ATOM   8118  N N   . PHE G  1 63  ? 32.022  -13.374  63.911  1.000 44.015  0 392 PHE GGG N   1 ? 26 
ATOM   8119  C CA  . PHE G  1 63  ? 31.921  -11.995  63.381  1.000 43.826  0 392 PHE GGG CA  1 ? 26 
ATOM   8120  C C   . PHE G  1 63  ? 31.558  -11.041  64.517  1.000 44.904  0 392 PHE GGG C   1 ? 26 
ATOM   8121  O O   . PHE G  1 63  ? 31.166  -11.513  65.592  1.000 45.122  0 392 PHE GGG O   1 ? 26 
ATOM   8122  C CB  . PHE G  1 63  ? 30.894  -11.991  62.258  1.000 42.275  0 392 PHE GGG CB  1 ? 26 
ATOM   8123  C CG  . PHE G  1 63  ? 31.302  -12.852  61.096  1.000 41.466  0 392 PHE GGG CG  1 ? 26 
ATOM   8124  C CD1 . PHE G  1 63  ? 32.385  -12.493  60.306  1.000 43.370  0 392 PHE GGG CD1 1 ? 26 
ATOM   8125  C CD2 . PHE G  1 63  ? 30.626  -14.006  60.796  1.000 39.127  0 392 PHE GGG CD2 1 ? 26 
ATOM   8126  C CE1 . PHE G  1 63  ? 32.775  -13.269  59.221  1.000 43.160  0 392 PHE GGG CE1 1 ? 26 
ATOM   8127  C CE2 . PHE G  1 63  ? 31.024  -14.786  59.726  1.000 41.147  0 392 PHE GGG CE2 1 ? 26 
ATOM   8128  C CZ  . PHE G  1 63  ? 32.082  -14.413  58.920  1.000 41.653  0 392 PHE GGG CZ  1 ? 26 
ATOM   8129  N N   . THR G  1 64  ? 31.784  -9.741   64.337  1.000 45.492  0 393 THR GGG N   1 ? 26 
ATOM   8130  C CA  . THR G  1 64  ? 31.464  -8.690   65.339  1.000 47.943  0 393 THR GGG CA  1 ? 26 
ATOM   8131  C C   . THR G  1 64  ? 29.945  -8.523   65.356  1.000 47.784  0 393 THR GGG C   1 ? 26 
ATOM   8132  O O   . THR G  1 64  ? 29.350  -8.340   66.439  1.000 49.182  0 393 THR GGG O   1 ? 26 
ATOM   8133  C CB  . THR G  1 64  ? 32.083  -7.335   64.990  1.000 48.348  0 393 THR GGG CB  1 ? 26 
ATOM   8134  O OG1 . THR G  1 64  ? 33.316  -7.572   64.331  1.000 48.343  0 393 THR GGG OG1 1 ? 26 
ATOM   8135  C CG2 . THR G  1 64  ? 32.327  -6.473   66.201  1.000 51.008  0 393 THR GGG CG2 1 ? 26 
ATOM   8136  N N   . ASN G  1 65  ? 29.361  -8.614   64.167  1.000 45.597  0 394 ASN GGG N   1 ? 26 
ATOM   8137  C CA  . ASN G  1 65  ? 27.924  -8.388   63.943  1.000 43.919  0 394 ASN GGG CA  1 ? 26 
ATOM   8138  C C   . ASN G  1 65  ? 27.535  -9.080   62.644  1.000 43.358  0 394 ASN GGG C   1 ? 26 
ATOM   8139  O O   . ASN G  1 65  ? 28.359  -9.297   61.745  1.000 44.272  0 394 ASN GGG O   1 ? 26 
ATOM   8140  C CB  . ASN G  1 65  ? 27.579  -6.917   63.813  1.000 45.248  0 394 ASN GGG CB  1 ? 26 
ATOM   8141  C CG  . ASN G  1 65  ? 27.750  -6.142   65.099  1.000 47.911  0 394 ASN GGG CG  1 ? 26 
ATOM   8142  O OD1 . ASN G  1 65  ? 26.999  -6.358   66.035  1.000 47.633  0 394 ASN GGG OD1 1 ? 26 
ATOM   8143  N ND2 . ASN G  1 65  ? 28.768  -5.284   65.146  1.000 49.551  0 394 ASN GGG ND2 1 ? 26 
ATOM   8144  N N   . VAL G  1 66  ? 26.264  -9.414   62.553  1.000 41.748  0 395 VAL GGG N   1 ? 26 
ATOM   8145  C CA  . VAL G  1 66  ? 25.636  -9.878   61.299  1.000 39.222  0 395 VAL GGG CA  1 ? 26 
ATOM   8146  C C   . VAL G  1 66  ? 24.452  -8.958   61.052  1.000 41.118  0 395 VAL GGG C   1 ? 26 
ATOM   8147  O O   . VAL G  1 66  ? 23.820  -8.546   62.012  1.000 42.072  0 395 VAL GGG O   1 ? 26 
ATOM   8148  C CB  . VAL G  1 66  ? 25.238  -11.346  61.428  1.000 38.728  0 395 VAL GGG CB  1 ? 26 
ATOM   8149  C CG1 . VAL G  1 66  ? 24.515  -11.832  60.175  1.000 37.851  0 395 VAL GGG CG1 1 ? 26 
ATOM   8150  C CG2 . VAL G  1 66  ? 26.453  -12.205  61.736  1.000 38.809  0 395 VAL GGG CG2 1 ? 26 
ATOM   8151  N N   . TYR G  1 67  ? 24.263  -8.555   59.807  1.000 41.527  0 396 TYR GGG N   1 ? 26 
ATOM   8152  C CA  . TYR G  1 67  ? 23.073  -7.780   59.383  1.000 43.356  0 396 TYR GGG CA  1 ? 26 
ATOM   8153  C C   . TYR G  1 67  ? 22.246  -8.664   58.457  1.000 42.291  0 396 TYR GGG C   1 ? 26 
ATOM   8154  O O   . TYR G  1 67  ? 22.825  -9.314   57.566  1.000 41.097  0 396 TYR GGG O   1 ? 26 
ATOM   8155  C CB  . TYR G  1 67  ? 23.493  -6.496   58.692  1.000 45.201  0 396 TYR GGG CB  1 ? 26 
ATOM   8156  C CG  . TYR G  1 67  ? 24.227  -5.563   59.607  1.000 46.776  0 396 TYR GGG CG  1 ? 26 
ATOM   8157  C CD1 . TYR G  1 67  ? 23.592  -4.957   60.675  1.000 47.591  0 396 TYR GGG CD1 1 ? 26 
ATOM   8158  C CD2 . TYR G  1 67  ? 25.614  -5.511   59.552  1.000 48.389  0 396 TYR GGG CD2 1 ? 26 
ATOM   8159  C CE1 . TYR G  1 67  ? 24.311  -4.182   61.578  1.000 50.761  0 396 TYR GGG CE1 1 ? 26 
ATOM   8160  C CE2 . TYR G  1 67  ? 26.344  -4.761   60.456  1.000 50.005  0 396 TYR GGG CE2 1 ? 26 
ATOM   8161  C CZ  . TYR G  1 67  ? 25.693  -4.100   61.476  1.000 51.368  0 396 TYR GGG CZ  1 ? 26 
ATOM   8162  O OH  . TYR G  1 67  ? 26.439  -3.361   62.342  1.000 56.527  0 396 TYR GGG OH  1 ? 26 
ATOM   8163  N N   . ALA G  1 68  ? 20.946  -8.709   58.717  1.000 42.241  0 397 ALA GGG N   1 ? 26 
ATOM   8164  C CA  . ALA G  1 68  ? 19.959  -9.435   57.891  1.000 42.681  0 397 ALA GGG CA  1 ? 26 
ATOM   8165  C C   . ALA G  1 68  ? 19.072  -8.387   57.224  1.000 43.596  0 397 ALA GGG C   1 ? 26 
ATOM   8166  O O   . ALA G  1 68  ? 18.267  -7.730   57.926  1.000 44.953  0 397 ALA GGG O   1 ? 26 
ATOM   8167  C CB  . ALA G  1 68  ? 19.165  -10.414  58.725  1.000 44.830  0 397 ALA GGG CB  1 ? 26 
ATOM   8168  N N   . ASP G  1 69  ? 19.284  -8.210   55.916  1.000 44.176  0 398 ASP GGG N   1 ? 26 
ATOM   8169  C CA  . ASP G  1 69  ? 18.464  -7.366   55.019  1.000 40.973  0 398 ASP GGG CA  1 ? 26 
ATOM   8170  C C   . ASP G  1 69  ? 17.461  -8.294   54.350  1.000 39.471  0 398 ASP GGG C   1 ? 26 
ATOM   8171  O O   . ASP G  1 69  ? 17.859  -9.353   53.884  1.000 41.046  0 398 ASP GGG O   1 ? 26 
ATOM   8172  C CB  . ASP G  1 69  ? 19.342  -6.632   54.003  1.000 41.853  0 398 ASP GGG CB  1 ? 26 
ATOM   8173  C CG  . ASP G  1 69  ? 20.425  -5.770   54.646  1.000 45.314  0 398 ASP GGG CG  1 ? 26 
ATOM   8174  O OD1 . ASP G  1 69  ? 20.203  -5.317   55.794  1.000 43.508  0 398 ASP GGG OD1 1 ? 26 
ATOM   8175  O OD2 . ASP G  1 69  ? 21.504  -5.577   54.011  1.000 46.741  0 398 ASP GGG OD2 1 ? 26 
ATOM   8176  N N   . SER G  1 70  ? 16.199  -7.907   54.293  1.000 38.074  0 399 SER GGG N   1 ? 26 
ATOM   8177  C CA  . SER G  1 70  ? 15.140  -8.740   53.680  1.000 35.674  0 399 SER GGG CA  1 ? 26 
ATOM   8178  C C   . SER G  1 70  ? 14.164  -7.861   52.906  1.000 36.180  0 399 SER GGG C   1 ? 26 
ATOM   8179  O O   . SER G  1 70  ? 13.960  -6.700   53.288  1.000 36.379  0 399 SER GGG O   1 ? 26 
ATOM   8180  C CB  . SER G  1 70  ? 14.446  -9.579   54.704  1.000 34.804  0 399 SER GGG CB  1 ? 26 
ATOM   8181  O OG  . SER G  1 70  ? 13.962  -8.762   55.756  1.000 34.189  0 399 SER GGG OG  1 ? 26 
ATOM   8182  N N   . PHE G  1 71  ? 13.587  -8.429   51.854  1.000 38.834  0 400 PHE GGG N   1 ? 26 
ATOM   8183  C CA  . PHE G  1 71  ? 12.672  -7.741   50.920  1.000 39.385  0 400 PHE GGG CA  1 ? 26 
ATOM   8184  C C   . PHE G  1 71  ? 12.117  -8.745   49.910  1.000 39.210  0 400 PHE GGG C   1 ? 26 
ATOM   8185  O O   . PHE G  1 71  ? 12.564  -9.901   49.892  1.000 37.176  0 400 PHE GGG O   1 ? 26 
ATOM   8186  C CB  . PHE G  1 71  ? 13.430  -6.634   50.199  1.000 40.453  0 400 PHE GGG CB  1 ? 26 
ATOM   8187  C CG  . PHE G  1 71  ? 14.751  -7.058   49.596  1.000 39.488  0 400 PHE GGG CG  1 ? 26 
ATOM   8188  C CD1 . PHE G  1 71  ? 14.791  -7.710   48.381  1.000 41.847  0 400 PHE GGG CD1 1 ? 26 
ATOM   8189  C CD2 . PHE G  1 71  ? 15.951  -6.805   50.235  1.000 38.217  0 400 PHE GGG CD2 1 ? 26 
ATOM   8190  C CE1 . PHE G  1 71  ? 16.000  -8.093   47.815  1.000 41.626  0 400 PHE GGG CE1 1 ? 26 
ATOM   8191  C CE2 . PHE G  1 71  ? 17.157  -7.172   49.660  1.000 37.682  0 400 PHE GGG CE2 1 ? 26 
ATOM   8192  C CZ  . PHE G  1 71  ? 17.181  -7.824   48.457  1.000 38.791  0 400 PHE GGG CZ  1 ? 26 
ATOM   8193  N N   . VAL G  1 72  ? 11.191  -8.288   49.061  1.000 41.887  0 401 VAL GGG N   1 ? 26 
ATOM   8194  C CA  . VAL G  1 72  ? 10.609  -9.088   47.944  1.000 42.447  0 401 VAL GGG CA  1 ? 26 
ATOM   8195  C C   . VAL G  1 72  ? 11.015  -8.461   46.606  1.000 44.074  0 401 VAL GGG C   1 ? 26 
ATOM   8196  O O   . VAL G  1 72  ? 10.985  -7.221   46.491  1.000 41.540  0 401 VAL GGG O   1 ? 26 
ATOM   8197  C CB  . VAL G  1 72  ? 9.082   -9.195   48.095  1.000 43.223  0 401 VAL GGG CB  1 ? 26 
ATOM   8198  C CG1 . VAL G  1 72  ? 8.404   -9.729   46.833  1.000 43.613  0 401 VAL GGG CG1 1 ? 26 
ATOM   8199  C CG2 . VAL G  1 72  ? 8.728   -10.054  49.305  1.000 45.241  0 401 VAL GGG CG2 1 ? 26 
ATOM   8200  N N   . ILE G  1 73  ? 11.356  -9.315   45.637  1.000 48.049  0 402 ILE GGG N   1 ? 26 
ATOM   8201  C CA  . ILE G  1 73  ? 11.586  -8.952   44.212  1.000 48.313  0 402 ILE GGG CA  1 ? 26 
ATOM   8202  C C   . ILE G  1 73  ? 10.992  -10.054  43.314  1.000 49.706  0 402 ILE GGG C   1 ? 26 
ATOM   8203  O O   . ILE G  1 73  ? 10.473  -11.035  43.854  1.000 47.955  0 402 ILE GGG O   1 ? 26 
ATOM   8204  C CB  . ILE G  1 73  ? 13.089  -8.713   43.962  1.000 46.753  0 402 ILE GGG CB  1 ? 26 
ATOM   8205  C CG1 . ILE G  1 73  ? 13.932  -9.909   44.403  1.000 48.870  0 402 ILE GGG CG1 1 ? 26 
ATOM   8206  C CG2 . ILE G  1 73  ? 13.554  -7.426   44.636  1.000 45.147  0 402 ILE GGG CG2 1 ? 26 
ATOM   8207  C CD1 . ILE G  1 73  ? 15.364  -9.842   43.996  1.000 48.680  0 402 ILE GGG CD1 1 ? 26 
ATOM   8208  N N   . ARG G  1 74  ? 11.035  -9.862   41.991  1.000 51.127  0 403 ARG GGG N   1 ? 26 
ATOM   8209  C CA  . ARG G  1 74  ? 10.656  -10.880  40.978  1.000 53.584  0 403 ARG GGG CA  1 ? 26 
ATOM   8210  C C   . ARG G  1 74  ? 11.720  -11.971  40.923  1.000 51.942  0 403 ARG GGG C   1 ? 26 
ATOM   8211  O O   . ARG G  1 74  ? 12.897  -11.652  41.152  1.000 48.640  0 403 ARG GGG O   1 ? 26 
ATOM   8212  C CB  . ARG G  1 74  ? 10.632  -10.314  39.559  1.000 57.657  0 403 ARG GGG CB  1 ? 26 
ATOM   8213  C CG  . ARG G  1 74  ? 9.428   -9.452   39.224  1.000 63.843  0 403 ARG GGG CG  1 ? 26 
ATOM   8214  C CD  . ARG G  1 74  ? 9.735   -8.573   38.017  1.000 65.679  0 403 ARG GGG CD  1 ? 26 
ATOM   8215  N NE  . ARG G  1 74  ? 10.159  -9.364   36.883  1.000 66.300  0 403 ARG GGG NE  1 ? 26 
ATOM   8216  C CZ  . ARG G  1 74  ? 10.609  -8.886   35.747  1.000 70.306  0 403 ARG GGG CZ  1 ? 26 
ATOM   8217  N NH1 . ARG G  1 74  ? 10.777  -7.587   35.595  1.000 73.250  0 403 ARG GGG NH1 1 ? 26 
ATOM   8218  N NH2 . ARG G  1 74  ? 10.943  -9.717   34.777  1.000 73.793  0 403 ARG GGG NH2 1 ? 26 
ATOM   8219  N N   . GLY G  1 75  ? 11.318  -13.175  40.502  1.000 51.251  0 404 GLY GGG N   1 ? 26 
ATOM   8220  C CA  . GLY G  1 75  ? 12.215  -14.321  40.297  1.000 51.872  0 404 GLY GGG CA  1 ? 26 
ATOM   8221  C C   . GLY G  1 75  ? 13.424  -13.959  39.462  1.000 50.672  0 404 GLY GGG C   1 ? 26 
ATOM   8222  O O   . GLY G  1 75  ? 14.531  -14.266  39.920  1.000 49.204  0 404 GLY GGG O   1 ? 26 
ATOM   8223  N N   . ASP G  1 76  ? 13.265  -13.298  38.315  1.000 51.900  0 405 ASP GGG N   1 ? 26 
ATOM   8224  C CA  . ASP G  1 76  ? 14.431  -13.104  37.411  1.000 55.803  0 405 ASP GGG CA  1 ? 26 
ATOM   8225  C C   . ASP G  1 76  ? 15.231  -11.876  37.854  1.000 52.063  0 405 ASP GGG C   1 ? 26 
ATOM   8226  O O   . ASP G  1 76  ? 16.248  -11.611  37.216  1.000 54.767  0 405 ASP GGG O   1 ? 26 
ATOM   8227  C CB  . ASP G  1 76  ? 14.076  -13.182  35.918  1.000 60.250  0 405 ASP GGG CB  1 ? 26 
ATOM   8228  C CG  . ASP G  1 76  ? 12.944  -12.277  35.466  1.000 64.197  0 405 ASP GGG CG  1 ? 26 
ATOM   8229  O OD1 . ASP G  1 76  ? 12.708  -11.232  36.157  1.000 65.894  0 405 ASP GGG OD1 1 ? 26 
ATOM   8230  O OD2 . ASP G  1 76  ? 12.303  -12.633  34.453  1.000 65.306  0 405 ASP GGG OD2 1 ? 26 
ATOM   8231  N N   . GLU G  1 77  ? 14.883  -11.229  38.970  1.000 47.719  0 406 GLU GGG N   1 ? 26 
ATOM   8232  C CA  . GLU G  1 77  ? 15.729  -10.161  39.555  1.000 47.672  0 406 GLU GGG CA  1 ? 26 
ATOM   8233  C C   . GLU G  1 77  ? 16.641  -10.747  40.650  1.000 45.629  0 406 GLU GGG C   1 ? 26 
ATOM   8234  O O   . GLU G  1 77  ? 17.554  -10.056  41.084  1.000 40.916  0 406 GLU GGG O   1 ? 26 
ATOM   8235  C CB  . GLU G  1 77  ? 14.849  -9.027   40.090  1.000 48.507  0 406 GLU GGG CB  1 ? 26 
ATOM   8236  C CG  . GLU G  1 77  ? 14.169  -8.179   39.019  1.000 48.734  0 406 GLU GGG CG  1 ? 26 
ATOM   8237  C CD  . GLU G  1 77  ? 13.124  -7.199   39.545  1.000 49.287  0 406 GLU GGG CD  1 ? 26 
ATOM   8238  O OE1 . GLU G  1 77  ? 12.634  -7.402   40.686  1.000 47.894  0 406 GLU GGG OE1 1 ? 26 
ATOM   8239  O OE2 . GLU G  1 77  ? 12.785  -6.240   38.815  1.000 48.863  0 406 GLU GGG OE2 1 ? 26 
ATOM   8240  N N   . VAL G  1 78  ? 16.428  -11.987  41.091  1.000 48.532  0 407 VAL GGG N   1 ? 26 
ATOM   8241  C CA  . VAL G  1 78  ? 17.219  -12.577  42.220  1.000 46.493  0 407 VAL GGG CA  1 ? 26 
ATOM   8242  C C   . VAL G  1 78  ? 18.712  -12.594  41.851  1.000 44.432  0 407 VAL GGG C   1 ? 26 
ATOM   8243  O O   . VAL G  1 78  ? 19.512  -12.302  42.727  1.000 42.230  0 407 VAL GGG O   1 ? 26 
ATOM   8244  C CB  . VAL G  1 78  ? 16.694  -13.957  42.653  1.000 45.423  0 407 VAL GGG CB  1 ? 26 
ATOM   8245  C CG1 . VAL G  1 78  ? 17.638  -14.656  43.632  1.000 45.688  0 407 VAL GGG CG1 1 ? 26 
ATOM   8246  C CG2 . VAL G  1 78  ? 15.312  -13.832  43.274  1.000 45.281  0 407 VAL GGG CG2 1 ? 26 
ATOM   8247  N N   . ARG G  1 79  ? 19.070  -12.863  40.600  1.000 44.879  0 408 ARG GGG N   1 ? 26 
ATOM   8248  C CA  . ARG G  1 79  ? 20.478  -12.864  40.138  1.000 48.712  0 408 ARG GGG CA  1 ? 26 
ATOM   8249  C C   . ARG G  1 79  ? 21.147  -11.498  40.389  1.000 45.438  0 408 ARG GGG C   1 ? 26 
ATOM   8250  O O   . ARG G  1 79  ? 22.383  -11.465  40.411  1.000 46.705  0 408 ARG GGG O   1 ? 26 
ATOM   8251  C CB  . ARG G  1 79  ? 20.548  -13.236  38.649  1.000 56.297  0 408 ARG GGG CB  1 ? 26 
ATOM   8252  C CG  . ARG G  1 79  ? 19.937  -12.188  37.730  1.000 62.698  0 408 ARG GGG CG  1 ? 26 
ATOM   8253  C CD  . ARG G  1 79  ? 20.668  -11.860  36.414  1.000 72.849  0 408 ARG GGG CD  1 ? 26 
ATOM   8254  N NE  . ARG G  1 79  ? 20.139  -10.658  35.740  1.000 80.319  0 408 ARG GGG NE  1 ? 26 
ATOM   8255  C CZ  . ARG G  1 79  ? 20.665  -9.418   35.764  1.000 83.316  0 408 ARG GGG CZ  1 ? 26 
ATOM   8256  N NH1 . ARG G  1 79  ? 21.770  -9.140   36.438  1.000 88.500  0 408 ARG GGG NH1 1 ? 26 
ATOM   8257  N NH2 . ARG G  1 79  ? 20.068  -8.436   35.118  1.000 85.107  0 408 ARG GGG NH2 1 ? 26 
ATOM   8258  N N   . GLN G  1 80  ? 20.391  -10.413  40.568  1.000 42.063  0 409 GLN GGG N   1 ? 26 
ATOM   8259  C CA  . GLN G  1 80  ? 20.939  -9.052   40.797  1.000 39.574  0 409 GLN GGG CA  1 ? 26 
ATOM   8260  C C   . GLN G  1 80  ? 21.385  -8.878   42.255  1.000 37.551  0 409 GLN GGG C   1 ? 26 
ATOM   8261  O O   . GLN G  1 80  ? 22.119  -7.924   42.540  1.000 36.194  0 409 GLN GGG O   1 ? 26 
ATOM   8262  C CB  . GLN G  1 80  ? 19.915  -7.971   40.459  1.000 39.880  0 409 GLN GGG CB  1 ? 26 
ATOM   8263  C CG  . GLN G  1 80  ? 19.669  -7.812   38.979  1.000 41.402  0 409 GLN GGG CG  1 ? 26 
ATOM   8264  C CD  . GLN G  1 80  ? 18.702  -6.695   38.656  1.000 41.454  0 409 GLN GGG CD  1 ? 26 
ATOM   8265  O OE1 . GLN G  1 80  ? 18.809  -5.559   39.148  1.000 37.643  0 409 GLN GGG OE1 1 ? 26 
ATOM   8266  N NE2 . GLN G  1 80  ? 17.807  -7.025   37.732  1.000 41.864  0 409 GLN GGG NE2 1 ? 26 
ATOM   8267  N N   . ILE G  1 81  ? 20.965  -9.752   43.154  1.000 37.064  0 410 ILE GGG N   1 ? 26 
ATOM   8268  C CA  . ILE G  1 81  ? 21.372  -9.669   44.583  1.000 36.418  0 410 ILE GGG CA  1 ? 26 
ATOM   8269  C C   . ILE G  1 81  ? 22.681  -10.439  44.713  1.000 37.895  0 410 ILE GGG C   1 ? 26 
ATOM   8270  O O   . ILE G  1 81  ? 22.716  -11.516  45.291  1.000 38.347  0 410 ILE GGG O   1 ? 26 
ATOM   8271  C CB  . ILE G  1 81  ? 20.272  -10.146  45.539  1.000 34.531  0 410 ILE GGG CB  1 ? 26 
ATOM   8272  C CG1 . ILE G  1 81  ? 18.896  -9.619   45.126  1.000 34.808  0 410 ILE GGG CG1 1 ? 26 
ATOM   8273  C CG2 . ILE G  1 81  ? 20.646  -9.766   46.963  1.000 33.234  0 410 ILE GGG CG2 1 ? 26 
ATOM   8274  C CD1 . ILE G  1 81  ? 18.843  -8.119   45.017  1.000 35.202  0 410 ILE GGG CD1 1 ? 26 
ATOM   8275  N N   . ALA G  1 82  ? 23.739  -9.833   44.191  1.000 40.151  0 411 ALA GGG N   1 ? 26 
ATOM   8276  C CA  . ALA G  1 82  ? 25.089  -10.404  44.137  1.000 41.425  0 411 ALA GGG CA  1 ? 26 
ATOM   8277  C C   . ALA G  1 82  ? 26.064  -9.277   43.846  1.000 42.738  0 411 ALA GGG C   1 ? 26 
ATOM   8278  O O   . ALA G  1 82  ? 25.734  -8.323   43.144  1.000 45.123  0 411 ALA GGG O   1 ? 26 
ATOM   8279  C CB  . ALA G  1 82  ? 25.150  -11.489  43.085  1.000 40.092  0 411 ALA GGG CB  1 ? 26 
ATOM   8280  N N   . PRO G  1 83  ? 27.314  -9.368   44.344  1.000 43.884  0 412 PRO GGG N   1 ? 26 
ATOM   8281  C CA  . PRO G  1 83  ? 28.345  -8.405   43.965  1.000 43.130  0 412 PRO GGG CA  1 ? 26 
ATOM   8282  C C   . PRO G  1 83  ? 28.522  -8.368   42.443  1.000 43.175  0 412 PRO GGG C   1 ? 26 
ATOM   8283  O O   . PRO G  1 83  ? 28.504  -9.399   41.854  1.000 47.589  0 412 PRO GGG O   1 ? 26 
ATOM   8284  C CB  . PRO G  1 83  ? 29.599  -8.932   44.665  1.000 43.794  0 412 PRO GGG CB  1 ? 26 
ATOM   8285  C CG  . PRO G  1 83  ? 29.274  -10.389  44.916  1.000 45.719  0 412 PRO GGG CG  1 ? 26 
ATOM   8286  C CD  . PRO G  1 83  ? 27.809  -10.399  45.264  1.000 44.172  0 412 PRO GGG CD  1 ? 26 
ATOM   8287  N N   . GLY G  1 84  ? 28.670  -7.179   41.874  1.000 43.296  0 413 GLY GGG N   1 ? 26 
ATOM   8288  C CA  . GLY G  1 84  ? 29.081  -6.957   40.483  1.000 44.397  0 413 GLY GGG CA  1 ? 26 
ATOM   8289  C C   . GLY G  1 84  ? 27.920  -6.955   39.517  1.000 45.513  0 413 GLY GGG C   1 ? 26 
ATOM   8290  O O   . GLY G  1 84  ? 28.209  -6.901   38.325  1.000 50.328  0 413 GLY GGG O   1 ? 26 
ATOM   8291  N N   . GLN G  1 85  ? 26.669  -6.976   39.981  1.000 45.035  0 414 GLN GGG N   1 ? 26 
ATOM   8292  C CA  . GLN G  1 85  ? 25.454  -7.049   39.109  1.000 46.080  0 414 GLN GGG CA  1 ? 26 
ATOM   8293  C C   . GLN G  1 85  ? 24.949  -5.649   38.741  1.000 45.139  0 414 GLN GGG C   1 ? 26 
ATOM   8294  O O   . GLN G  1 85  ? 25.202  -4.722   39.502  1.000 45.745  0 414 GLN GGG O   1 ? 26 
ATOM   8295  C CB  . GLN G  1 85  ? 24.356  -7.797   39.862  1.000 46.892  0 414 GLN GGG CB  1 ? 26 
ATOM   8296  C CG  . GLN G  1 85  ? 24.667  -9.276   40.034  1.000 49.330  0 414 GLN GGG CG  1 ? 26 
ATOM   8297  C CD  . GLN G  1 85  ? 24.710  -9.996   38.703  1.000 52.295  0 414 GLN GGG CD  1 ? 26 
ATOM   8298  O OE1 . GLN G  1 85  ? 23.925  -9.724   37.811  1.000 55.329  0 414 GLN GGG OE1 1 ? 26 
ATOM   8299  N NE2 . GLN G  1 85  ? 25.612  -10.944  38.549  1.000 54.121  0 414 GLN GGG NE2 1 ? 26 
ATOM   8300  N N   . THR G  1 86  ? 24.252  -5.509   37.617  1.000 46.951  0 415 THR GGG N   1 ? 26 
ATOM   8301  C CA  . THR G  1 86  ? 23.483  -4.291   37.235  1.000 46.860  0 415 THR GGG CA  1 ? 26 
ATOM   8302  C C   . THR G  1 86  ? 22.043  -4.677   36.891  1.000 46.080  0 415 THR GGG C   1 ? 26 
ATOM   8303  O O   . THR G  1 86  ? 21.778  -5.883   36.717  1.000 47.160  0 415 THR GGG O   1 ? 26 
ATOM   8304  C CB  . THR G  1 86  ? 24.133  -3.531   36.077  1.000 49.591  0 415 THR GGG CB  1 ? 26 
ATOM   8305  O OG1 . THR G  1 86  ? 24.277  -4.457   34.997  1.000 51.621  0 415 THR GGG OG1 1 ? 26 
ATOM   8306  C CG2 . THR G  1 86  ? 25.459  -2.917   36.472  1.000 50.468  0 415 THR GGG CG2 1 ? 26 
ATOM   8307  N N   . GLY G  1 87  ? 21.175  -3.666   36.811  1.000 45.420  0 416 GLY GGG N   1 ? 26 
ATOM   8308  C CA  . GLY G  1 87  ? 19.723  -3.779   36.590  1.000 46.072  0 416 GLY GGG CA  1 ? 26 
ATOM   8309  C C   . GLY G  1 87  ? 18.964  -2.852   37.514  1.000 45.347  0 416 GLY GGG C   1 ? 26 
ATOM   8310  O O   . GLY G  1 87  ? 19.623  -2.236   38.366  1.000 44.054  0 416 GLY GGG O   1 ? 26 
ATOM   8311  N N   . LYS G  1 88  ? 17.644  -2.745   37.346  1.000 47.695  0 417 LYS GGG N   1 ? 26 
ATOM   8312  C CA  . LYS G  1 88  ? 16.785  -1.846   38.160  1.000 48.036  0 417 LYS GGG CA  1 ? 26 
ATOM   8313  C C   . LYS G  1 88  ? 17.097  -2.066   39.633  1.000 44.565  0 417 LYS GGG C   1 ? 26 
ATOM   8314  O O   . LYS G  1 88  ? 17.245  -1.066   40.347  1.000 45.598  0 417 LYS GGG O   1 ? 26 
ATOM   8315  C CB  . LYS G  1 88  ? 15.288  -2.058   37.918  1.000 51.276  0 417 LYS GGG CB  1 ? 26 
ATOM   8316  C CG  . LYS G  1 88  ? 14.815  -1.645   36.535  1.000 57.444  0 417 LYS GGG CG  1 ? 26 
ATOM   8317  C CD  . LYS G  1 88  ? 15.278  -0.270   36.042  1.000 61.353  0 417 LYS GGG CD  1 ? 26 
ATOM   8318  C CE  . LYS G  1 88  ? 15.635  -0.252   34.569  1.000 65.922  0 417 LYS GGG CE  1 ? 26 
ATOM   8319  N NZ  . LYS G  1 88  ? 15.403  1.091    33.991  1.000 70.632  0 417 LYS GGG NZ  1 ? 26 
ATOM   8320  N N   . ILE G  1 89  ? 17.204  -3.325   40.069  1.000 41.822  0 418 ILE GGG N   1 ? 26 
ATOM   8321  C CA  . ILE G  1 89  ? 17.301  -3.640   41.519  1.000 39.632  0 418 ILE GGG CA  1 ? 26 
ATOM   8322  C C   . ILE G  1 89  ? 18.706  -3.303   42.022  1.000 38.971  0 418 ILE GGG C   1 ? 26 
ATOM   8323  O O   . ILE G  1 89  ? 18.806  -2.508   42.965  1.000 39.006  0 418 ILE GGG O   1 ? 26 
ATOM   8324  C CB  . ILE G  1 89  ? 16.872  -5.083   41.822  1.000 40.179  0 418 ILE GGG CB  1 ? 26 
ATOM   8325  C CG1 . ILE G  1 89  ? 15.481  -5.369   41.270  1.000 42.394  0 418 ILE GGG CG1 1 ? 26 
ATOM   8326  C CG2 . ILE G  1 89  ? 16.914  -5.346   43.322  1.000 39.493  0 418 ILE GGG CG2 1 ? 26 
ATOM   8327  C CD1 . ILE G  1 89  ? 14.408  -4.404   41.713  1.000 42.358  0 418 ILE GGG CD1 1 ? 26 
ATOM   8328  N N   . ALA G  1 90  ? 19.756  -3.851   41.410  1.000 39.883  0 419 ALA GGG N   1 ? 26 
ATOM   8329  C CA  . ALA G  1 90  ? 21.161  -3.584   41.803  1.000 39.345  0 419 ALA GGG CA  1 ? 26 
ATOM   8330  C C   . ALA G  1 90  ? 21.446  -2.071   41.745  1.000 39.288  0 419 ALA GGG C   1 ? 26 
ATOM   8331  O O   . ALA G  1 90  ? 22.137  -1.567   42.664  1.000 39.221  0 419 ALA GGG O   1 ? 26 
ATOM   8332  C CB  . ALA G  1 90  ? 22.104  -4.360   40.925  1.000 39.854  0 419 ALA GGG CB  1 ? 26 
ATOM   8333  N N   . ASP G  1 91  ? 20.908  -1.362   40.748  1.000 37.338  0 420 ASP GGG N   1 ? 26 
ATOM   8334  C CA  . ASP G  1 91  ? 21.268  0.050    40.494  1.000 40.132  0 420 ASP GGG CA  1 ? 26 
ATOM   8335  C C   . ASP G  1 91  ? 20.465  0.992    41.404  1.000 40.720  0 420 ASP GGG C   1 ? 26 
ATOM   8336  O O   . ASP G  1 91  ? 21.054  1.984    41.866  1.000 41.025  0 420 ASP GGG O   1 ? 26 
ATOM   8337  C CB  . ASP G  1 91  ? 21.058  0.440    39.026  1.000 42.456  0 420 ASP GGG CB  1 ? 26 
ATOM   8338  C CG  . ASP G  1 91  ? 21.937  -0.300   38.022  1.000 43.720  0 420 ASP GGG CG  1 ? 26 
ATOM   8339  O OD1 . ASP G  1 91  ? 22.923  -0.943   38.471  1.000 44.141  0 420 ASP GGG OD1 1 ? 26 
ATOM   8340  O OD2 . ASP G  1 91  ? 21.620  -0.240   36.798  1.000 42.708  0 420 ASP GGG OD2 1 ? 26 
ATOM   8341  N N   . TYR G  1 92  ? 19.174  0.739    41.613  1.000 38.987  0 421 TYR GGG N   1 ? 26 
ATOM   8342  C CA  . TYR G  1 92  ? 18.218  1.751    42.127  1.000 42.219  0 421 TYR GGG CA  1 ? 26 
ATOM   8343  C C   . TYR G  1 92  ? 17.553  1.339    43.454  1.000 39.345  0 421 TYR GGG C   1 ? 26 
ATOM   8344  O O   . TYR G  1 92  ? 16.886  2.196    44.054  1.000 40.534  0 421 TYR GGG O   1 ? 26 
ATOM   8345  C CB  . TYR G  1 92  ? 17.145  2.050    41.073  1.000 42.813  0 421 TYR GGG CB  1 ? 26 
ATOM   8346  C CG  . TYR G  1 92  ? 17.602  2.693    39.788  1.000 45.054  0 421 TYR GGG CG  1 ? 26 
ATOM   8347  C CD1 . TYR G  1 92  ? 18.828  3.326    39.649  1.000 45.257  0 421 TYR GGG CD1 1 ? 26 
ATOM   8348  C CD2 . TYR G  1 92  ? 16.739  2.733    38.704  1.000 48.149  0 421 TYR GGG CD2 1 ? 26 
ATOM   8349  C CE1 . TYR G  1 92  ? 19.205  3.931    38.455  1.000 46.358  0 421 TYR GGG CE1 1 ? 26 
ATOM   8350  C CE2 . TYR G  1 92  ? 17.094  3.342    37.507  1.000 50.692  0 421 TYR GGG CE2 1 ? 26 
ATOM   8351  C CZ  . TYR G  1 92  ? 18.338  3.938    37.379  1.000 49.695  0 421 TYR GGG CZ  1 ? 26 
ATOM   8352  O OH  . TYR G  1 92  ? 18.677  4.541    36.200  1.000 52.322  0 421 TYR GGG OH  1 ? 26 
ATOM   8353  N N   . ASN G  1 93  ? 17.718  0.106    43.914  1.000 37.922  0 422 ASN GGG N   1 ? 26 
ATOM   8354  C CA  . ASN G  1 93  ? 16.933  -0.430   45.054  1.000 39.427  0 422 ASN GGG CA  1 ? 26 
ATOM   8355  C C   . ASN G  1 93  ? 17.839  -0.999   46.149  1.000 38.242  0 422 ASN GGG C   1 ? 26 
ATOM   8356  O O   . ASN G  1 93  ? 17.722  -0.553   47.298  1.000 39.373  0 422 ASN GGG O   1 ? 26 
ATOM   8357  C CB  . ASN G  1 93  ? 15.921  -1.467   44.568  1.000 42.639  0 422 ASN GGG CB  1 ? 26 
ATOM   8358  C CG  . ASN G  1 93  ? 14.808  -0.827   43.769  1.000 43.439  0 422 ASN GGG CG  1 ? 26 
ATOM   8359  O OD1 . ASN G  1 93  ? 13.772  -0.466   44.342  1.000 46.055  0 422 ASN GGG OD1 1 ? 26 
ATOM   8360  N ND2 . ASN G  1 93  ? 15.029  -0.660   42.471  1.000 40.846  0 422 ASN GGG ND2 1 ? 26 
ATOM   8361  N N   . TYR G  1 94  ? 18.677  -1.967   45.813  1.000 38.960  0 423 TYR GGG N   1 ? 26 
ATOM   8362  C CA  . TYR G  1 94  ? 19.544  -2.695   46.775  1.000 39.888  0 423 TYR GGG CA  1 ? 26 
ATOM   8363  C C   . TYR G  1 94  ? 20.849  -3.098   46.087  1.000 39.232  0 423 TYR GGG C   1 ? 26 
ATOM   8364  O O   . TYR G  1 94  ? 20.817  -3.925   45.153  1.000 41.292  0 423 TYR GGG O   1 ? 26 
ATOM   8365  C CB  . TYR G  1 94  ? 18.837  -3.917   47.354  1.000 38.220  0 423 TYR GGG CB  1 ? 26 
ATOM   8366  C CG  . TYR G  1 94  ? 19.608  -4.547   48.487  1.000 39.866  0 423 TYR GGG CG  1 ? 26 
ATOM   8367  C CD1 . TYR G  1 94  ? 19.484  -4.093   49.797  1.000 38.974  0 423 TYR GGG CD1 1 ? 26 
ATOM   8368  C CD2 . TYR G  1 94  ? 20.483  -5.596   48.246  1.000 39.998  0 423 TYR GGG CD2 1 ? 26 
ATOM   8369  C CE1 . TYR G  1 94  ? 20.185  -4.687   50.828  1.000 39.498  0 423 TYR GGG CE1 1 ? 26 
ATOM   8370  C CE2 . TYR G  1 94  ? 21.194  -6.198   49.268  1.000 37.936  0 423 TYR GGG CE2 1 ? 26 
ATOM   8371  C CZ  . TYR G  1 94  ? 21.053  -5.741   50.561  1.000 40.031  0 423 TYR GGG CZ  1 ? 26 
ATOM   8372  O OH  . TYR G  1 94  ? 21.789  -6.339   51.553  1.000 38.301  0 423 TYR GGG OH  1 ? 26 
ATOM   8373  N N   . LYS G  1 95  ? 21.958  -2.522   46.551  1.000 37.903  0 424 LYS GGG N   1 ? 26 
ATOM   8374  C CA  . LYS G  1 95  ? 23.289  -2.687   45.928  1.000 39.197  0 424 LYS GGG CA  1 ? 26 
ATOM   8375  C C   . LYS G  1 95  ? 24.214  -3.394   46.918  1.000 39.061  0 424 LYS GGG C   1 ? 26 
ATOM   8376  O O   . LYS G  1 95  ? 24.435  -2.858   48.020  1.000 35.761  0 424 LYS GGG O   1 ? 26 
ATOM   8377  C CB  . LYS G  1 95  ? 23.875  -1.331   45.537  1.000 42.057  0 424 LYS GGG CB  1 ? 26 
ATOM   8378  C CG  . LYS G  1 95  ? 25.255  -1.377   44.892  1.000 45.453  0 424 LYS GGG CG  1 ? 26 
ATOM   8379  C CD  . LYS G  1 95  ? 25.311  -2.293   43.717  1.000 47.454  0 424 LYS GGG CD  1 ? 26 
ATOM   8380  C CE  . LYS G  1 95  ? 26.440  -1.983   42.758  1.000 51.226  0 424 LYS GGG CE  1 ? 26 
ATOM   8381  N NZ  . LYS G  1 95  ? 26.269  -2.790   41.532  1.000 52.279  0 424 LYS GGG NZ  1 ? 26 
ATOM   8382  N N   . LEU G  1 96  ? 24.758  -4.546   46.529  1.000 37.556  0 425 LEU GGG N   1 ? 26 
ATOM   8383  C CA  . LEU G  1 96  ? 25.845  -5.193   47.299  1.000 38.184  0 425 LEU GGG CA  1 ? 26 
ATOM   8384  C C   . LEU G  1 96  ? 27.178  -4.652   46.798  1.000 38.882  0 425 LEU GGG C   1 ? 26 
ATOM   8385  O O   . LEU G  1 96  ? 27.339  -4.407   45.615  1.000 36.874  0 425 LEU GGG O   1 ? 26 
ATOM   8386  C CB  . LEU G  1 96  ? 25.792  -6.713   47.142  1.000 39.667  0 425 LEU GGG CB  1 ? 26 
ATOM   8387  C CG  . LEU G  1 96  ? 24.646  -7.406   47.862  1.000 39.618  0 425 LEU GGG CG  1 ? 26 
ATOM   8388  C CD1 . LEU G  1 96  ? 24.692  -8.888   47.617  1.000 40.539  0 425 LEU GGG CD1 1 ? 26 
ATOM   8389  C CD2 . LEU G  1 96  ? 24.695  -7.102   49.353  1.000 40.775  0 425 LEU GGG CD2 1 ? 26 
ATOM   8390  N N   . PRO G  1 97  ? 28.155  -4.471   47.710  1.000 40.276  0 426 PRO GGG N   1 ? 26 
ATOM   8391  C CA  . PRO G  1 97  ? 29.508  -4.051   47.340  1.000 41.698  0 426 PRO GGG CA  1 ? 26 
ATOM   8392  C C   . PRO G  1 97  ? 30.226  -5.157   46.560  1.000 43.351  0 426 PRO GGG C   1 ? 26 
ATOM   8393  O O   . PRO G  1 97  ? 29.866  -6.295   46.681  1.000 44.230  0 426 PRO GGG O   1 ? 26 
ATOM   8394  C CB  . PRO G  1 97  ? 30.189  -3.827   48.711  1.000 40.705  0 426 PRO GGG CB  1 ? 26 
ATOM   8395  C CG  . PRO G  1 97  ? 29.443  -4.754   49.662  1.000 39.867  0 426 PRO GGG CG  1 ? 26 
ATOM   8396  C CD  . PRO G  1 97  ? 28.013  -4.730   49.163  1.000 39.692  0 426 PRO GGG CD  1 ? 26 
ATOM   8397  N N   . ASP G  1 98  ? 31.256  -4.800   45.815  1.000 48.631  0 427 ASP GGG N   1 ? 26 
ATOM   8398  C CA  . ASP G  1 98  ? 32.040  -5.769   45.010  1.000 52.972  0 427 ASP GGG CA  1 ? 26 
ATOM   8399  C C   . ASP G  1 98  ? 32.773  -6.749   45.931  1.000 49.292  0 427 ASP GGG C   1 ? 26 
ATOM   8400  O O   . ASP G  1 98  ? 32.952  -7.879   45.514  1.000 47.577  0 427 ASP GGG O   1 ? 26 
ATOM   8401  C CB  . ASP G  1 98  ? 32.987  -5.066   44.035  1.000 60.088  0 427 ASP GGG CB  1 ? 26 
ATOM   8402  C CG  . ASP G  1 98  ? 32.618  -5.385   42.595  1.000 70.503  0 427 ASP GGG CG  1 ? 26 
ATOM   8403  O OD1 . ASP G  1 98  ? 32.688  -6.607   42.218  1.000 69.250  0 427 ASP GGG OD1 1 ? 26 
ATOM   8404  O OD2 . ASP G  1 98  ? 32.207  -4.419   41.874  1.000 80.378  0 427 ASP GGG OD2 1 ? 26 
ATOM   8405  N N   . ASP G  1 99  ? 33.172  -6.327   47.129  1.000 47.948  0 428 ASP GGG N   1 ? 26 
ATOM   8406  C CA  . ASP G  1 99  ? 33.955  -7.140   48.100  1.000 48.928  0 428 ASP GGG CA  1 ? 26 
ATOM   8407  C C   . ASP G  1 99  ? 33.015  -7.630   49.222  1.000 47.143  0 428 ASP GGG C   1 ? 26 
ATOM   8408  O O   . ASP G  1 99  ? 33.458  -7.853   50.378  1.000 45.879  0 428 ASP GGG O   1 ? 26 
ATOM   8409  C CB  . ASP G  1 99  ? 35.139  -6.335   48.648  1.000 49.942  0 428 ASP GGG CB  1 ? 26 
ATOM   8410  C CG  . ASP G  1 99  ? 34.745  -5.154   49.517  1.000 50.977  0 428 ASP GGG CG  1 ? 26 
ATOM   8411  O OD1 . ASP G  1 99  ? 33.550  -4.808   49.536  1.000 49.188  0 428 ASP GGG OD1 1 ? 26 
ATOM   8412  O OD2 . ASP G  1 99  ? 35.643  -4.613   50.195  1.000 54.360  0 428 ASP GGG OD2 1 ? 26 
ATOM   8413  N N   . PHE G  1 100 ? 31.746  -7.808   48.909  1.000 43.740  0 429 PHE GGG N   1 ? 26 
ATOM   8414  C CA  . PHE G  1 100 ? 30.745  -8.349   49.861  1.000 43.130  0 429 PHE GGG CA  1 ? 26 
ATOM   8415  C C   . PHE G  1 100 ? 31.281  -9.601   50.570  1.000 41.556  0 429 PHE GGG C   1 ? 26 
ATOM   8416  O O   . PHE G  1 100 ? 31.789  -10.514  49.926  1.000 39.004  0 429 PHE GGG O   1 ? 26 
ATOM   8417  C CB  . PHE G  1 100 ? 29.460  -8.680   49.115  1.000 42.336  0 429 PHE GGG CB  1 ? 26 
ATOM   8418  C CG  . PHE G  1 100 ? 28.383  -9.275   49.972  1.000 42.195  0 429 PHE GGG CG  1 ? 26 
ATOM   8419  C CD1 . PHE G  1 100 ? 27.925  -8.598   51.093  1.000 43.567  0 429 PHE GGG CD1 1 ? 26 
ATOM   8420  C CD2 . PHE G  1 100 ? 27.796  -10.471  49.631  1.000 41.053  0 429 PHE GGG CD2 1 ? 26 
ATOM   8421  C CE1 . PHE G  1 100 ? 26.906  -9.120   51.873  1.000 42.365  0 429 PHE GGG CE1 1 ? 26 
ATOM   8422  C CE2 . PHE G  1 100 ? 26.768  -10.987  50.409  1.000 42.796  0 429 PHE GGG CE2 1 ? 26 
ATOM   8423  C CZ  . PHE G  1 100 ? 26.328  -10.313  51.532  1.000 42.150  0 429 PHE GGG CZ  1 ? 26 
ATOM   8424  N N   . THR G  1 101 ? 31.116  -9.651   51.884  1.000 42.325  0 430 THR GGG N   1 ? 26 
ATOM   8425  C CA  . THR G  1 101 ? 31.296  -10.869  52.711  1.000 41.660  0 430 THR GGG CA  1 ? 26 
ATOM   8426  C C   . THR G  1 101 ? 29.942  -11.210  53.328  1.000 41.991  0 430 THR GGG C   1 ? 26 
ATOM   8427  O O   . THR G  1 101 ? 29.460  -10.431  54.159  1.000 41.632  0 430 THR GGG O   1 ? 26 
ATOM   8428  C CB  . THR G  1 101 ? 32.366  -10.670  53.789  1.000 42.032  0 430 THR GGG CB  1 ? 26 
ATOM   8429  O OG1 . THR G  1 101 ? 33.558  -10.222  53.150  1.000 39.741  0 430 THR GGG OG1 1 ? 26 
ATOM   8430  C CG2 . THR G  1 101 ? 32.654  -11.936  54.559  1.000 43.402  0 430 THR GGG CG2 1 ? 26 
ATOM   8431  N N   . GLY G  1 102 ? 29.363  -12.352  52.952  1.000 42.992  0 431 GLY GGG N   1 ? 26 
ATOM   8432  C CA  . GLY G  1 102 ? 28.052  -12.778  53.471  1.000 42.380  0 431 GLY GGG CA  1 ? 26 
ATOM   8433  C C   . GLY G  1 102 ? 27.358  -13.741  52.531  1.000 42.965  0 431 GLY GGG C   1 ? 26 
ATOM   8434  O O   . GLY G  1 102 ? 28.017  -14.308  51.647  1.000 42.841  0 431 GLY GGG O   1 ? 26 
ATOM   8435  N N   . CYS G  1 103 ? 26.063  -13.965  52.755  1.000 42.825  0 432 CYS GGG N   1 ? 26 
ATOM   8436  C CA  . CYS G  1 103 ? 25.266  -14.959  52.011  1.000 41.818  0 432 CYS GGG CA  1 ? 26 
ATOM   8437  C C   . CYS G  1 103 ? 23.966  -14.317  51.549  1.000 39.032  0 432 CYS GGG C   1 ? 26 
ATOM   8438  O O   . CYS G  1 103 ? 23.449  -13.438  52.224  1.000 42.683  0 432 CYS GGG O   1 ? 26 
ATOM   8439  C CB  . CYS G  1 103 ? 25.006  -16.214  52.839  1.000 44.134  0 432 CYS GGG CB  1 ? 26 
ATOM   8440  S SG  . CYS G  1 103 ? 26.514  -16.923  53.557  1.000 49.131  0 432 CYS GGG SG  1 ? 26 
ATOM   8441  N N   . VAL G  1 104 ? 23.469  -14.789  50.421  1.000 39.060  0 433 VAL GGG N   1 ? 26 
ATOM   8442  C CA  . VAL G  1 104 ? 22.180  -14.377  49.812  1.000 38.442  0 433 VAL GGG CA  1 ? 26 
ATOM   8443  C C   . VAL G  1 104 ? 21.327  -15.628  49.681  1.000 39.154  0 433 VAL GGG C   1 ? 26 
ATOM   8444  O O   . VAL G  1 104 ? 21.786  -16.602  49.073  1.000 38.402  0 433 VAL GGG O   1 ? 26 
ATOM   8445  C CB  . VAL G  1 104 ? 22.405  -13.684  48.464  1.000 37.655  0 433 VAL GGG CB  1 ? 26 
ATOM   8446  C CG1 . VAL G  1 104 ? 21.109  -13.403  47.735  1.000 35.821  0 433 VAL GGG CG1 1 ? 26 
ATOM   8447  C CG2 . VAL G  1 104 ? 23.190  -12.398  48.661  1.000 39.092  0 433 VAL GGG CG2 1 ? 26 
ATOM   8448  N N   . ILE G  1 105 ? 20.151  -15.586  50.296  1.000 39.936  0 434 ILE GGG N   1 ? 26 
ATOM   8449  C CA  . ILE G  1 105 ? 19.168  -16.701  50.276  1.000 42.355  0 434 ILE GGG CA  1 ? 26 
ATOM   8450  C C   . ILE G  1 105 ? 17.861  -16.134  49.735  1.000 40.052  0 434 ILE GGG C   1 ? 26 
ATOM   8451  O O   . ILE G  1 105 ? 17.483  -15.015  50.138  1.000 41.873  0 434 ILE GGG O   1 ? 26 
ATOM   8452  C CB  . ILE G  1 105 ? 19.019  -17.331  51.680  1.000 43.739  0 434 ILE GGG CB  1 ? 26 
ATOM   8453  C CG1 . ILE G  1 105 ? 20.359  -17.865  52.179  1.000 46.762  0 434 ILE GGG CG1 1 ? 26 
ATOM   8454  C CG2 . ILE G  1 105 ? 17.969  -18.414  51.667  1.000 44.778  0 434 ILE GGG CG2 1 ? 26 
ATOM   8455  C CD1 . ILE G  1 105 ? 20.423  -18.168  53.635  1.000 48.923  0 434 ILE GGG CD1 1 ? 26 
ATOM   8456  N N   . ALA G  1 106 ? 17.212  -16.876  48.852  1.000 38.092  0 435 ALA GGG N   1 ? 26 
ATOM   8457  C CA  . ALA G  1 106 ? 15.894  -16.498  48.306  1.000 38.599  0 435 ALA GGG CA  1 ? 26 
ATOM   8458  C C   . ALA G  1 106 ? 15.042  -17.750  48.194  1.000 39.679  0 435 ALA GGG C   1 ? 26 
ATOM   8459  O O   . ALA G  1 106 ? 15.612  -18.897  48.182  1.000 41.112  0 435 ALA GGG O   1 ? 26 
ATOM   8460  C CB  . ALA G  1 106 ? 16.027  -15.784  46.983  1.000 38.696  0 435 ALA GGG CB  1 ? 26 
ATOM   8461  N N   . TRP G  1 107 ? 13.724  -17.539  48.163  1.000 38.396  0 436 TRP GGG N   1 ? 26 
ATOM   8462  C CA  . TRP G  1 107 ? 12.742  -18.615  47.904  1.000 39.899  0 436 TRP GGG CA  1 ? 26 
ATOM   8463  C C   . TRP G  1 107 ? 11.517  -18.022  47.229  1.000 39.783  0 436 TRP GGG C   1 ? 26 
ATOM   8464  O O   . TRP G  1 107 ? 11.190  -16.840  47.495  1.000 39.292  0 436 TRP GGG O   1 ? 26 
ATOM   8465  C CB  . TRP G  1 107 ? 12.418  -19.392  49.186  1.000 39.255  0 436 TRP GGG CB  1 ? 26 
ATOM   8466  C CG  . TRP G  1 107 ? 11.728  -18.588  50.236  1.000 39.021  0 436 TRP GGG CG  1 ? 26 
ATOM   8467  C CD1 . TRP G  1 107 ? 10.387  -18.529  50.460  1.000 39.674  0 436 TRP GGG CD1 1 ? 26 
ATOM   8468  C CD2 . TRP G  1 107 ? 12.350  -17.745  51.228  1.000 38.653  0 436 TRP GGG CD2 1 ? 26 
ATOM   8469  N NE1 . TRP G  1 107 ? 10.145  -17.729  51.551  1.000 40.949  0 436 TRP GGG NE1 1 ? 26 
ATOM   8470  C CE2 . TRP G  1 107 ? 11.321  -17.225  52.031  1.000 38.740  0 436 TRP GGG CE2 1 ? 26 
ATOM   8471  C CE3 . TRP G  1 107 ? 13.663  -17.343  51.505  1.000 38.232  0 436 TRP GGG CE3 1 ? 26 
ATOM   8472  C CZ2 . TRP G  1 107 ? 11.561  -16.357  53.089  1.000 39.244  0 436 TRP GGG CZ2 1 ? 26 
ATOM   8473  C CZ3 . TRP G  1 107 ? 13.904  -16.475  52.544  1.000 38.308  0 436 TRP GGG CZ3 1 ? 26 
ATOM   8474  C CH2 . TRP G  1 107 ? 12.871  -16.013  53.337  1.000 38.414  0 436 TRP GGG CH2 1 ? 26 
ATOM   8475  N N   . ASN G  1 108 ? 10.922  -18.818  46.350  1.000 38.680  0 437 ASN GGG N   1 ? 26 
ATOM   8476  C CA  . ASN G  1 108 ? 9.635   -18.504  45.695  1.000 40.964  0 437 ASN GGG CA  1 ? 26 
ATOM   8477  C C   . ASN G  1 108 ? 8.580   -18.322  46.792  1.000 43.032  0 437 ASN GGG C   1 ? 26 
ATOM   8478  O O   . ASN G  1 108 ? 8.455   -19.217  47.650  1.000 44.504  0 437 ASN GGG O   1 ? 26 
ATOM   8479  C CB  . ASN G  1 108 ? 9.273   -19.625  44.731  1.000 41.871  0 437 ASN GGG CB  1 ? 26 
ATOM   8480  C CG  . ASN G  1 108 ? 8.045   -19.272  43.949  1.000 44.141  0 437 ASN GGG CG  1 ? 26 
ATOM   8481  O OD1 . ASN G  1 108 ? 6.955   -19.184  44.519  1.000 45.569  0 437 ASN GGG OD1 1 ? 26 
ATOM   8482  N ND2 . ASN G  1 108 ? 8.221   -19.004  42.668  1.000 46.540  0 437 ASN GGG ND2 1 ? 26 
ATOM   8483  N N   . SER G  1 109 ? 7.869   -17.193  46.788  1.000 42.354  0 438 SER GGG N   1 ? 26 
ATOM   8484  C CA  . SER G  1 109 ? 6.815   -16.883  47.781  1.000 41.710  0 438 SER GGG CA  1 ? 26 
ATOM   8485  C C   . SER G  1 109 ? 5.490   -16.666  47.045  1.000 43.625  0 438 SER GGG C   1 ? 26 
ATOM   8486  O O   . SER G  1 109 ? 4.628   -15.990  47.586  1.000 42.346  0 438 SER GGG O   1 ? 26 
ATOM   8487  C CB  . SER G  1 109 ? 7.207   -15.709  48.632  1.000 41.146  0 438 SER GGG CB  1 ? 26 
ATOM   8488  O OG  . SER G  1 109 ? 7.422   -14.575  47.806  1.000 43.865  0 438 SER GGG OG  1 ? 26 
ATOM   8489  N N   . ASN G  1 110 ? 5.327   -17.260  45.867  1.000 44.409  0 439 ASN GGG N   1 ? 26 
ATOM   8490  C CA  . ASN G  1 110 ? 4.096   -17.111  45.057  1.000 46.041  0 439 ASN GGG CA  1 ? 26 
ATOM   8491  C C   . ASN G  1 110 ? 2.890   -17.490  45.927  1.000 47.848  0 439 ASN GGG C   1 ? 26 
ATOM   8492  O O   . ASN G  1 110 ? 1.898   -16.757  45.901  1.000 48.638  0 439 ASN GGG O   1 ? 26 
ATOM   8493  C CB  . ASN G  1 110 ? 4.179   -17.931  43.776  1.000 46.971  0 439 ASN GGG CB  1 ? 26 
ATOM   8494  C CG  . ASN G  1 110 ? 3.196   -17.491  42.717  1.000 49.441  0 439 ASN GGG CG  1 ? 26 
ATOM   8495  O OD1 . ASN G  1 110 ? 2.889   -16.309  42.604  1.000 50.346  0 439 ASN GGG OD1 1 ? 26 
ATOM   8496  N ND2 . ASN G  1 110 ? 2.711   -18.444  41.928  1.000 51.405  0 439 ASN GGG ND2 1 ? 26 
ATOM   8497  N N   . ASN G  1 111 ? 2.985   -18.568  46.699  1.000 49.059  0 440 ASN GGG N   1 ? 26 
ATOM   8498  C CA  . ASN G  1 111 ? 1.879   -19.102  47.532  1.000 51.575  0 440 ASN GGG CA  1 ? 26 
ATOM   8499  C C   . ASN G  1 111 ? 1.446   -18.075  48.602  1.000 52.528  0 440 ASN GGG C   1 ? 26 
ATOM   8500  O O   . ASN G  1 111 ? 0.298   -18.146  49.022  1.000 56.289  0 440 ASN GGG O   1 ? 26 
ATOM   8501  C CB  . ASN G  1 111 ? 2.268   -20.456  48.139  1.000 50.324  0 440 ASN GGG CB  1 ? 26 
ATOM   8502  C CG  . ASN G  1 111 ? 2.167   -21.625  47.178  1.000 51.260  0 440 ASN GGG CG  1 ? 26 
ATOM   8503  O OD1 . ASN G  1 111 ? 1.414   -21.601  46.210  1.000 54.017  0 440 ASN GGG OD1 1 ? 26 
ATOM   8504  N ND2 . ASN G  1 111 ? 2.873   -22.699  47.474  1.000 51.218  0 440 ASN GGG ND2 1 ? 26 
ATOM   8505  N N   . LEU G  1 112 ? 2.329   -17.206  49.073  1.000 52.799  0 441 LEU GGG N   1 ? 26 
ATOM   8506  C CA  . LEU G  1 112 ? 2.041   -16.241  50.164  1.000 54.197  0 441 LEU GGG CA  1 ? 26 
ATOM   8507  C C   . LEU G  1 112 ? 1.838   -14.824  49.611  1.000 52.614  0 441 LEU GGG C   1 ? 26 
ATOM   8508  O O   . LEU G  1 112 ? 1.030   -14.132  50.177  1.000 53.897  0 441 LEU GGG O   1 ? 26 
ATOM   8509  C CB  . LEU G  1 112 ? 3.214   -16.263  51.162  1.000 55.086  0 441 LEU GGG CB  1 ? 26 
ATOM   8510  C CG  . LEU G  1 112 ? 2.897   -15.731  52.562  1.000 57.724  0 441 LEU GGG CG  1 ? 26 
ATOM   8511  C CD1 . LEU G  1 112 ? 1.507   -16.130  53.054  1.000 57.816  0 441 LEU GGG CD1 1 ? 26 
ATOM   8512  C CD2 . LEU G  1 112 ? 3.948   -16.196  53.548  1.000 58.696  0 441 LEU GGG CD2 1 ? 26 
ATOM   8513  N N   . ASP G  1 113 ? 2.567   -14.407  48.575  1.000 51.442  0 442 ASP GGG N   1 ? 26 
ATOM   8514  C CA  . ASP G  1 113 ? 2.724   -12.974  48.179  1.000 50.336  0 442 ASP GGG CA  1 ? 26 
ATOM   8515  C C   . ASP G  1 113 ? 1.997   -12.629  46.875  1.000 52.613  0 442 ASP GGG C   1 ? 26 
ATOM   8516  O O   . ASP G  1 113 ? 2.169   -11.504  46.382  1.000 53.133  0 442 ASP GGG O   1 ? 26 
ATOM   8517  C CB  . ASP G  1 113 ? 4.209   -12.635  48.031  1.000 45.944  0 442 ASP GGG CB  1 ? 26 
ATOM   8518  C CG  . ASP G  1 113 ? 4.919   -12.503  49.358  1.000 45.543  0 442 ASP GGG CG  1 ? 26 
ATOM   8519  O OD1 . ASP G  1 113 ? 4.263   -11.956  50.308  1.000 44.855  0 442 ASP GGG OD1 1 ? 26 
ATOM   8520  O OD2 . ASP G  1 113 ? 6.135   -12.896  49.414  1.000 41.564  0 442 ASP GGG OD2 1 ? 26 
ATOM   8521  N N   . SER G  1 114 ? 1.248   -13.545  46.276  1.000 56.633  0 443 SER GGG N   1 ? 26 
ATOM   8522  C CA  . SER G  1 114 ? 0.498   -13.228  45.035  1.000 60.938  0 443 SER GGG CA  1 ? 26 
ATOM   8523  C C   . SER G  1 114 ? -0.989  -13.403  45.338  1.000 65.337  0 443 SER GGG C   1 ? 26 
ATOM   8524  O O   . SER G  1 114 ? -1.304  -14.182  46.231  1.000 67.778  0 443 SER GGG O   1 ? 26 
ATOM   8525  C CB  . SER G  1 114 ? 1.013   -14.058  43.880  1.000 61.287  0 443 SER GGG CB  1 ? 26 
ATOM   8526  O OG  . SER G  1 114 ? 0.402   -15.329  43.858  1.000 61.541  0 443 SER GGG OG  1 ? 26 
ATOM   8527  N N   . LYS G  1 115 ? -1.865  -12.649  44.688  1.000 71.664  0 444 LYS GGG N   1 ? 26 
ATOM   8528  C CA  . LYS G  1 115 ? -3.333  -12.700  44.927  1.000 75.819  0 444 LYS GGG CA  1 ? 26 
ATOM   8529  C C   . LYS G  1 115 ? -4.052  -12.822  43.592  1.000 77.218  0 444 LYS GGG C   1 ? 26 
ATOM   8530  O O   . LYS G  1 115 ? -3.498  -12.343  42.588  1.000 73.874  0 444 LYS GGG O   1 ? 26 
ATOM   8531  C CB  . LYS G  1 115 ? -3.840  -11.435  45.620  1.000 80.269  0 444 LYS GGG CB  1 ? 26 
ATOM   8532  C CG  . LYS G  1 115 ? -3.899  -11.540  47.135  1.000 86.066  0 444 LYS GGG CG  1 ? 26 
ATOM   8533  C CD  . LYS G  1 115 ? -3.676  -10.241  47.877  1.000 90.852  0 444 LYS GGG CD  1 ? 26 
ATOM   8534  C CE  . LYS G  1 115 ? -2.822  -10.467  49.117  1.000 91.266  0 444 LYS GGG CE  1 ? 26 
ATOM   8535  N NZ  . LYS G  1 115 ? -2.261  -9.208   49.652  1.000 88.526  0 444 LYS GGG NZ  1 ? 26 
ATOM   8536  N N   . VAL G  1 116 ? -5.253  -13.410  43.605  1.000 79.782  0 445 VAL GGG N   1 ? 26 
ATOM   8537  C CA  . VAL G  1 116 ? -6.156  -13.381  42.418  1.000 82.019  0 445 VAL GGG CA  1 ? 26 
ATOM   8538  C C   . VAL G  1 116 ? -6.496  -11.898  42.201  1.000 80.543  0 445 VAL GGG C   1 ? 26 
ATOM   8539  O O   . VAL G  1 116 ? -6.799  -11.198  43.189  1.000 78.320  0 445 VAL GGG O   1 ? 26 
ATOM   8540  C CB  . VAL G  1 116 ? -7.377  -14.303  42.577  1.000 88.245  0 445 VAL GGG CB  1 ? 26 
ATOM   8541  C CG1 . VAL G  1 116 ? -6.930  -15.762  42.613  1.000 88.068  0 445 VAL GGG CG1 1 ? 26 
ATOM   8542  C CG2 . VAL G  1 116 ? -8.221  -13.963  43.805  1.000 90.068  0 445 VAL GGG CG2 1 ? 26 
ATOM   8543  N N   . GLY G  1 117 ? -6.301  -11.393  40.989  1.000 78.503  0 446 GLY GGG N   1 ? 26 
ATOM   8544  C CA  . GLY G  1 117 ? -6.474  -9.955   40.695  1.000 78.045  0 446 GLY GGG CA  1 ? 26 
ATOM   8545  C C   . GLY G  1 117 ? -5.237  -9.145   41.018  1.000 75.609  0 446 GLY GGG C   1 ? 26 
ATOM   8546  O O   . GLY G  1 117 ? -5.271  -7.949   40.742  1.000 77.733  0 446 GLY GGG O   1 ? 26 
ATOM   8547  N N   . GLY G  1 118 ? -4.175  -9.778   41.520  1.000 75.263  0 447 GLY GGG N   1 ? 26 
ATOM   8548  C CA  . GLY G  1 118 ? -2.819  -9.197   41.594  1.000 72.759  0 447 GLY GGG CA  1 ? 26 
ATOM   8549  C C   . GLY G  1 118 ? -2.540  -8.547   42.938  1.000 69.878  0 447 GLY GGG C   1 ? 26 
ATOM   8550  O O   . GLY G  1 118 ? -3.394  -7.787   43.400  1.000 75.250  0 447 GLY GGG O   1 ? 26 
ATOM   8551  N N   . ASN G  1 119 ? -1.381  -8.827   43.538  1.000 63.211  0 448 ASN GGG N   1 ? 26 
ATOM   8552  C CA  . ASN G  1 119 ? -0.897  -8.143   44.766  1.000 60.575  0 448 ASN GGG CA  1 ? 26 
ATOM   8553  C C   . ASN G  1 119 ? -0.046  -6.947   44.324  1.000 60.084  0 448 ASN GGG C   1 ? 26 
ATOM   8554  O O   . ASN G  1 119 ? 1.033   -7.166   43.742  1.000 59.205  0 448 ASN GGG O   1 ? 26 
ATOM   8555  C CB  . ASN G  1 119 ? -0.157  -9.105   45.697  1.000 57.700  0 448 ASN GGG CB  1 ? 26 
ATOM   8556  C CG  . ASN G  1 119 ? 0.408   -8.424   46.926  1.000 56.776  0 448 ASN GGG CG  1 ? 26 
ATOM   8557  O OD1 . ASN G  1 119 ? 0.078   -7.288   47.235  1.000 58.624  0 448 ASN GGG OD1 1 ? 26 
ATOM   8558  N ND2 . ASN G  1 119 ? 1.313   -9.093   47.622  1.000 56.670  0 448 ASN GGG ND2 1 ? 26 
ATOM   8559  N N   . TYR G  1 120 ? -0.510  -5.730   44.602  1.000 61.328  0 449 TYR GGG N   1 ? 26 
ATOM   8560  C CA  . TYR G  1 120 ? 0.157   -4.473   44.163  1.000 62.353  0 449 TYR GGG CA  1 ? 26 
ATOM   8561  C C   . TYR G  1 120 ? 0.903   -3.835   45.350  1.000 62.083  0 449 TYR GGG C   1 ? 26 
ATOM   8562  O O   . TYR G  1 120 ? 1.411   -2.721   45.197  1.000 61.323  0 449 TYR GGG O   1 ? 26 
ATOM   8563  C CB  . TYR G  1 120 ? -0.848  -3.566   43.436  1.000 64.329  0 449 TYR GGG CB  1 ? 26 
ATOM   8564  C CG  . TYR G  1 120 ? -1.356  -4.146   42.131  1.000 67.012  0 449 TYR GGG CG  1 ? 26 
ATOM   8565  C CD1 . TYR G  1 120 ? -0.577  -4.114   40.982  1.000 67.182  0 449 TYR GGG CD1 1 ? 26 
ATOM   8566  C CD2 . TYR G  1 120 ? -2.584  -4.783   42.039  1.000 70.387  0 449 TYR GGG CD2 1 ? 26 
ATOM   8567  C CE1 . TYR G  1 120 ? -0.991  -4.697   39.791  1.000 69.434  0 449 TYR GGG CE1 1 ? 26 
ATOM   8568  C CE2 . TYR G  1 120 ? -3.033  -5.340   40.847  1.000 72.926  0 449 TYR GGG CE2 1 ? 26 
ATOM   8569  C CZ  . TYR G  1 120 ? -2.230  -5.308   39.718  1.000 72.685  0 449 TYR GGG CZ  1 ? 26 
ATOM   8570  O OH  . TYR G  1 120 ? -2.666  -5.848   38.541  1.000 72.204  0 449 TYR GGG OH  1 ? 26 
ATOM   8571  N N   . ASN G  1 121 ? 1.005   -4.532   46.491  1.000 60.499  0 450 ASN GGG N   1 ? 26 
ATOM   8572  C CA  . ASN G  1 121 ? 1.580   -3.954   47.738  1.000 58.839  0 450 ASN GGG CA  1 ? 26 
ATOM   8573  C C   . ASN G  1 121 ? 3.104   -3.815   47.646  1.000 55.558  0 450 ASN GGG C   1 ? 26 
ATOM   8574  O O   . ASN G  1 121 ? 3.645   -2.909   48.294  1.000 57.109  0 450 ASN GGG O   1 ? 26 
ATOM   8575  C CB  . ASN G  1 121 ? 1.176   -4.743   48.978  1.000 60.562  0 450 ASN GGG CB  1 ? 26 
ATOM   8576  C CG  . ASN G  1 121 ? -0.286  -4.531   49.318  1.000 67.033  0 450 ASN GGG CG  1 ? 26 
ATOM   8577  O OD1 . ASN G  1 121 ? -0.900  -3.536   48.931  1.000 71.341  0 450 ASN GGG OD1 1 ? 26 
ATOM   8578  N ND2 . ASN G  1 121 ? -0.860  -5.445   50.075  1.000 71.591  0 450 ASN GGG ND2 1 ? 26 
ATOM   8579  N N   . TYR G  1 122 ? 3.801   -4.662   46.895  1.000 52.327  0 451 TYR GGG N   1 ? 26 
ATOM   8580  C CA  . TYR G  1 122 ? 5.283   -4.629   46.823  1.000 48.717  0 451 TYR GGG CA  1 ? 26 
ATOM   8581  C C   . TYR G  1 122 ? 5.716   -3.657   45.714  1.000 49.039  0 451 TYR GGG C   1 ? 26 
ATOM   8582  O O   . TYR G  1 122 ? 5.242   -3.773   44.550  1.000 48.468  0 451 TYR GGG O   1 ? 26 
ATOM   8583  C CB  . TYR G  1 122 ? 5.809   -6.041   46.598  1.000 48.122  0 451 TYR GGG CB  1 ? 26 
ATOM   8584  C CG  . TYR G  1 122 ? 5.625   -6.962   47.775  1.000 49.031  0 451 TYR GGG CG  1 ? 26 
ATOM   8585  C CD1 . TYR G  1 122 ? 6.401   -6.827   48.915  1.000 48.012  0 451 TYR GGG CD1 1 ? 26 
ATOM   8586  C CD2 . TYR G  1 122 ? 4.723   -8.012   47.725  1.000 50.239  0 451 TYR GGG CD2 1 ? 26 
ATOM   8587  C CE1 . TYR G  1 122 ? 6.285   -7.708   49.978  1.000 46.231  0 451 TYR GGG CE1 1 ? 26 
ATOM   8588  C CE2 . TYR G  1 122 ? 4.612   -8.921   48.768  1.000 48.935  0 451 TYR GGG CE2 1 ? 26 
ATOM   8589  C CZ  . TYR G  1 122 ? 5.374   -8.751   49.905  1.000 46.848  0 451 TYR GGG CZ  1 ? 26 
ATOM   8590  O OH  . TYR G  1 122 ? 5.227   -9.598   50.957  1.000 48.252  0 451 TYR GGG OH  1 ? 26 
ATOM   8591  N N   . LEU G  1 123 ? 6.592   -2.716   46.078  1.000 46.749  0 452 LEU GGG N   1 ? 26 
ATOM   8592  C CA  . LEU G  1 123 ? 7.060   -1.605   45.199  1.000 47.406  0 452 LEU GGG CA  1 ? 26 
ATOM   8593  C C   . LEU G  1 123 ? 8.555   -1.742   44.917  1.000 44.172  0 452 LEU GGG C   1 ? 26 
ATOM   8594  O O   . LEU G  1 123 ? 9.240   -2.391   45.721  1.000 43.002  0 452 LEU GGG O   1 ? 26 
ATOM   8595  C CB  . LEU G  1 123 ? 6.773   -0.262   45.883  1.000 47.058  0 452 LEU GGG CB  1 ? 26 
ATOM   8596  C CG  . LEU G  1 123 ? 5.317   0.036    46.261  1.000 48.134  0 452 LEU GGG CG  1 ? 26 
ATOM   8597  C CD1 . LEU G  1 123 ? 5.232   1.480    46.783  1.000 47.246  0 452 LEU GGG CD1 1 ? 26 
ATOM   8598  C CD2 . LEU G  1 123 ? 4.376   -0.127   45.087  1.000 49.462  0 452 LEU GGG CD2 1 ? 26 
ATOM   8599  N N   . TYR G  1 124 ? 9.022   -1.162   43.813  1.000 42.954  0 453 TYR GGG N   1 ? 26 
ATOM   8600  C CA  . TYR G  1 124 ? 10.461  -1.017   43.489  1.000 43.199  0 453 TYR GGG CA  1 ? 26 
ATOM   8601  C C   . TYR G  1 124 ? 10.687  0.371    42.886  1.000 44.066  0 453 TYR GGG C   1 ? 26 
ATOM   8602  O O   . TYR G  1 124 ? 9.757   0.908    42.255  1.000 45.717  0 453 TYR GGG O   1 ? 26 
ATOM   8603  C CB  . TYR G  1 124 ? 10.910  -2.141   42.544  1.000 43.805  0 453 TYR GGG CB  1 ? 26 
ATOM   8604  C CG  . TYR G  1 124 ? 10.247  -2.107   41.196  1.000 45.318  0 453 TYR GGG CG  1 ? 26 
ATOM   8605  C CD1 . TYR G  1 124 ? 9.053   -2.771   40.991  1.000 46.643  0 453 TYR GGG CD1 1 ? 26 
ATOM   8606  C CD2 . TYR G  1 124 ? 10.803  -1.410   40.128  1.000 44.928  0 453 TYR GGG CD2 1 ? 26 
ATOM   8607  C CE1 . TYR G  1 124 ? 8.426   -2.743   39.755  1.000 46.340  0 453 TYR GGG CE1 1 ? 26 
ATOM   8608  C CE2 . TYR G  1 124 ? 10.182  -1.371   38.891  1.000 44.891  0 453 TYR GGG CE2 1 ? 26 
ATOM   8609  C CZ  . TYR G  1 124 ? 8.991   -2.048   38.708  1.000 46.636  0 453 TYR GGG CZ  1 ? 26 
ATOM   8610  O OH  . TYR G  1 124 ? 8.310   -2.058   37.523  1.000 50.794  0 453 TYR GGG OH  1 ? 26 
ATOM   8611  N N   . ARG G  1 125 ? 11.881  0.942    43.066  1.000 42.854  0 454 ARG GGG N   1 ? 26 
ATOM   8612  C CA  . ARG G  1 125 ? 12.267  2.224    42.426  1.000 44.074  0 454 ARG GGG CA  1 ? 26 
ATOM   8613  C C   . ARG G  1 125 ? 12.594  1.929    40.963  1.000 45.232  0 454 ARG GGG C   1 ? 26 
ATOM   8614  O O   . ARG G  1 125 ? 13.445  1.072    40.707  1.000 47.673  0 454 ARG GGG O   1 ? 26 
ATOM   8615  C CB  . ARG G  1 125 ? 13.417  2.886    43.186  1.000 42.354  0 454 ARG GGG CB  1 ? 26 
ATOM   8616  C CG  . ARG G  1 125 ? 13.742  4.290    42.684  1.000 42.920  0 454 ARG GGG CG  1 ? 26 
ATOM   8617  C CD  . ARG G  1 125 ? 14.795  4.980    43.536  1.000 41.925  0 454 ARG GGG CD  1 ? 26 
ATOM   8618  N NE  . ARG G  1 125 ? 14.316  5.067    44.897  1.000 41.769  0 454 ARG GGG NE  1 ? 26 
ATOM   8619  C CZ  . ARG G  1 125 ? 13.449  5.973    45.367  1.000 42.611  0 454 ARG GGG CZ  1 ? 26 
ATOM   8620  N NH1 . ARG G  1 125 ? 12.950  6.910    44.592  1.000 42.679  0 454 ARG GGG NH1 1 ? 26 
ATOM   8621  N NH2 . ARG G  1 125 ? 13.074  5.939    46.635  1.000 44.294  0 454 ARG GGG NH2 1 ? 26 
ATOM   8622  N N   . LEU G  1 126 ? 11.909  2.593    40.042  1.000 48.079  0 455 LEU GGG N   1 ? 26 
ATOM   8623  C CA  . LEU G  1 126 ? 12.035  2.364    38.579  1.000 50.986  0 455 LEU GGG CA  1 ? 26 
ATOM   8624  C C   . LEU G  1 126 ? 13.001  3.385    37.974  1.000 52.551  0 455 LEU GGG C   1 ? 26 
ATOM   8625  O O   . LEU G  1 126 ? 13.682  3.036    37.001  1.000 55.089  0 455 LEU GGG O   1 ? 26 
ATOM   8626  C CB  . LEU G  1 126 ? 10.632  2.489    37.968  1.000 53.605  0 455 LEU GGG CB  1 ? 26 
ATOM   8627  C CG  . LEU G  1 126 ? 10.544  2.412    36.443  1.000 54.157  0 455 LEU GGG CG  1 ? 26 
ATOM   8628  C CD1 . LEU G  1 126 ? 11.149  1.109    35.921  1.000 52.481  0 455 LEU GGG CD1 1 ? 26 
ATOM   8629  C CD2 . LEU G  1 126 ? 9.098   2.551    36.010  1.000 56.098  0 455 LEU GGG CD2 1 ? 26 
ATOM   8630  N N   . PHE G  1 127 ? 13.031  4.602    38.529  1.000 55.033  0 456 PHE GGG N   1 ? 26 
ATOM   8631  C CA  . PHE G  1 127 ? 13.830  5.755    38.042  1.000 55.370  0 456 PHE GGG CA  1 ? 26 
ATOM   8632  C C   . PHE G  1 127 ? 14.678  6.306    39.184  1.000 51.516  0 456 PHE GGG C   1 ? 26 
ATOM   8633  O O   . PHE G  1 127 ? 14.197  6.406    40.316  1.000 50.257  0 456 PHE GGG O   1 ? 26 
ATOM   8634  C CB  . PHE G  1 127 ? 12.927  6.860    37.498  1.000 59.752  0 456 PHE GGG CB  1 ? 26 
ATOM   8635  C CG  . PHE G  1 127 ? 11.965  6.422    36.419  1.000 64.840  0 456 PHE GGG CG  1 ? 26 
ATOM   8636  C CD1 . PHE G  1 127 ? 12.417  6.022    35.168  1.000 66.839  0 456 PHE GGG CD1 1 ? 26 
ATOM   8637  C CD2 . PHE G  1 127 ? 10.594  6.416    36.650  1.000 68.723  0 456 PHE GGG CD2 1 ? 26 
ATOM   8638  C CE1 . PHE G  1 127 ? 11.527  5.674    34.166  1.000 68.084  0 456 PHE GGG CE1 1 ? 26 
ATOM   8639  C CE2 . PHE G  1 127 ? 9.704   6.044    35.652  1.000 70.182  0 456 PHE GGG CE2 1 ? 26 
ATOM   8640  C CZ  . PHE G  1 127 ? 10.177  5.663    34.414  1.000 69.745  0 456 PHE GGG CZ  1 ? 26 
ATOM   8641  N N   . ARG G  1 128 ? 15.923  6.653    38.876  1.000 49.716  0 457 ARG GGG N   1 ? 26 
ATOM   8642  C CA  . ARG G  1 128 ? 16.795  7.406    39.805  1.000 47.999  0 457 ARG GGG CA  1 ? 26 
ATOM   8643  C C   . ARG G  1 128 ? 17.874  8.134    39.002  1.000 49.519  0 457 ARG GGG C   1 ? 26 
ATOM   8644  O O   . ARG G  1 128 ? 18.300  7.574    37.973  1.000 46.659  0 457 ARG GGG O   1 ? 26 
ATOM   8645  C CB  . ARG G  1 128 ? 17.392  6.439    40.820  1.000 44.779  0 457 ARG GGG CB  1 ? 26 
ATOM   8646  C CG  . ARG G  1 128 ? 18.002  7.145    42.019  1.000 44.035  0 457 ARG GGG CG  1 ? 26 
ATOM   8647  C CD  . ARG G  1 128 ? 18.353  6.110    43.070  1.000 43.182  0 457 ARG GGG CD  1 ? 26 
ATOM   8648  N NE  . ARG G  1 128 ? 18.631  6.740    44.350  1.000 42.397  0 457 ARG GGG NE  1 ? 26 
ATOM   8649  C CZ  . ARG G  1 128 ? 19.823  7.185    44.723  1.000 42.289  0 457 ARG GGG CZ  1 ? 26 
ATOM   8650  N NH1 . ARG G  1 128 ? 20.872  7.071    43.927  1.000 41.637  0 457 ARG GGG NH1 1 ? 26 
ATOM   8651  N NH2 . ARG G  1 128 ? 19.969  7.739    45.903  1.000 43.239  0 457 ARG GGG NH2 1 ? 26 
ATOM   8652  N N   . LYS G  1 129 ? 18.298  9.321    39.464  1.000 53.560  0 458 LYS GGG N   1 ? 26 
ATOM   8653  C CA  . LYS G  1 129 ? 19.295  10.166   38.749  1.000 56.054  0 458 LYS GGG CA  1 ? 26 
ATOM   8654  C C   . LYS G  1 129 ? 20.658  9.461    38.705  1.000 53.390  0 458 LYS GGG C   1 ? 26 
ATOM   8655  O O   . LYS G  1 129 ? 21.426  9.717    37.772  1.000 54.447  0 458 LYS GGG O   1 ? 26 
ATOM   8656  C CB  . LYS G  1 129 ? 19.509  11.510   39.444  1.000 59.159  0 458 LYS GGG CB  1 ? 26 
ATOM   8657  C CG  . LYS G  1 129 ? 18.373  12.512   39.468  1.000 62.655  0 458 LYS GGG CG  1 ? 26 
ATOM   8658  C CD  . LYS G  1 129 ? 18.778  13.633   40.425  1.000 64.908  0 458 LYS GGG CD  1 ? 26 
ATOM   8659  C CE  . LYS G  1 129 ? 18.033  14.934   40.254  1.000 72.530  0 458 LYS GGG CE  1 ? 26 
ATOM   8660  N NZ  . LYS G  1 129 ? 18.064  15.693   41.526  1.000 75.415  0 458 LYS GGG NZ  1 ? 26 
ATOM   8661  N N   . SER G  1 130 ? 20.953  8.592    39.669  1.000 49.447  0 459 SER GGG N   1 ? 26 
ATOM   8662  C CA  . SER G  1 130 ? 22.262  7.912    39.756  1.000 48.077  0 459 SER GGG CA  1 ? 26 
ATOM   8663  C C   . SER G  1 130 ? 22.123  6.623    40.560  1.000 46.794  0 459 SER GGG C   1 ? 26 
ATOM   8664  O O   . SER G  1 130 ? 21.113  6.463    41.254  1.000 47.800  0 459 SER GGG O   1 ? 26 
ATOM   8665  C CB  . SER G  1 130 ? 23.287  8.830    40.340  1.000 49.439  0 459 SER GGG CB  1 ? 26 
ATOM   8666  O OG  . SER G  1 130 ? 23.167  8.882    41.747  1.000 49.544  0 459 SER GGG OG  1 ? 26 
ATOM   8667  N N   . ASN G  1 131 ? 23.097  5.728    40.442  1.000 45.543  0 460 ASN GGG N   1 ? 26 
ATOM   8668  C CA  . ASN G  1 131 ? 23.071  4.392    41.071  1.000 43.569  0 460 ASN GGG CA  1 ? 26 
ATOM   8669  C C   . ASN G  1 131 ? 23.267  4.541    42.579  1.000 42.446  0 460 ASN GGG C   1 ? 26 
ATOM   8670  O O   . ASN G  1 131 ? 23.969  5.429    42.998  1.000 43.144  0 460 ASN GGG O   1 ? 26 
ATOM   8671  C CB  . ASN G  1 131 ? 24.125  3.460    40.468  1.000 42.693  0 460 ASN GGG CB  1 ? 26 
ATOM   8672  C CG  . ASN G  1 131 ? 23.838  3.106    39.023  1.000 43.685  0 460 ASN GGG CG  1 ? 26 
ATOM   8673  O OD1 . ASN G  1 131 ? 22.806  3.471    38.468  1.000 45.328  0 460 ASN GGG OD1 1 ? 26 
ATOM   8674  N ND2 . ASN G  1 131 ? 24.754  2.396    38.402  1.000 44.235  0 460 ASN GGG ND2 1 ? 26 
ATOM   8675  N N   . LEU G  1 132 ? 22.641  3.669    43.353  1.000 43.836  0 461 LEU GGG N   1 ? 26 
ATOM   8676  C CA  . LEU G  1 132 ? 22.879  3.535    44.806  1.000 44.625  0 461 LEU GGG CA  1 ? 26 
ATOM   8677  C C   . LEU G  1 132 ? 24.341  3.169    45.036  1.000 44.115  0 461 LEU GGG C   1 ? 26 
ATOM   8678  O O   . LEU G  1 132 ? 24.856  2.326    44.276  1.000 45.219  0 461 LEU GGG O   1 ? 26 
ATOM   8679  C CB  . LEU G  1 132 ? 21.971  2.438    45.366  1.000 46.100  0 461 LEU GGG CB  1 ? 26 
ATOM   8680  C CG  . LEU G  1 132 ? 20.484  2.742    45.428  1.000 45.589  0 461 LEU GGG CG  1 ? 26 
ATOM   8681  C CD1 . LEU G  1 132 ? 19.762  1.596    46.125  1.000 44.206  0 461 LEU GGG CD1 1 ? 26 
ATOM   8682  C CD2 . LEU G  1 132 ? 20.209  4.061    46.123  1.000 47.950  0 461 LEU GGG CD2 1 ? 26 
ATOM   8683  N N   . LYS G  1 133 ? 24.945  3.743    46.077  1.000 46.480  0 462 LYS GGG N   1 ? 26 
ATOM   8684  C CA  . LYS G  1 133 ? 26.159  3.210    46.734  1.000 46.613  0 462 LYS GGG CA  1 ? 26 
ATOM   8685  C C   . LYS G  1 133 ? 25.812  1.884    47.408  1.000 42.959  0 462 LYS GGG C   1 ? 26 
ATOM   8686  O O   . LYS G  1 133 ? 24.659  1.617    47.738  1.000 41.069  0 462 LYS GGG O   1 ? 26 
ATOM   8687  C CB  . LYS G  1 133 ? 26.667  4.217    47.769  1.000 50.468  0 462 LYS GGG CB  1 ? 26 
ATOM   8688  C CG  . LYS G  1 133 ? 27.488  5.379    47.254  1.000 57.655  0 462 LYS GGG CG  1 ? 26 
ATOM   8689  C CD  . LYS G  1 133 ? 27.005  6.173    46.065  1.000 63.596  0 462 LYS GGG CD  1 ? 26 
ATOM   8690  C CE  . LYS G  1 133 ? 28.158  6.688    45.219  1.000 67.971  0 462 LYS GGG CE  1 ? 26 
ATOM   8691  N NZ  . LYS G  1 133 ? 27.855  8.007    44.606  1.000 74.600  0 462 LYS GGG NZ  1 ? 26 
ATOM   8692  N N   . PRO G  1 134 ? 26.802  0.999    47.640  1.000 43.498  0 463 PRO GGG N   1 ? 26 
ATOM   8693  C CA  . PRO G  1 134 ? 26.529  -0.261   48.335  1.000 42.597  0 463 PRO GGG CA  1 ? 26 
ATOM   8694  C C   . PRO G  1 134 ? 25.860  -0.028   49.691  1.000 41.636  0 463 PRO GGG C   1 ? 26 
ATOM   8695  O O   . PRO G  1 134 ? 26.289  0.832    50.403  1.000 41.214  0 463 PRO GGG O   1 ? 26 
ATOM   8696  C CB  . PRO G  1 134 ? 27.916  -0.878   48.448  1.000 42.905  0 463 PRO GGG CB  1 ? 26 
ATOM   8697  C CG  . PRO G  1 134 ? 28.629  -0.339   47.223  1.000 43.854  0 463 PRO GGG CG  1 ? 26 
ATOM   8698  C CD  . PRO G  1 134 ? 28.197  1.115    47.172  1.000 43.424  0 463 PRO GGG CD  1 ? 26 
ATOM   8699  N N   . PHE G  1 135 ? 24.780  -0.765   49.958  1.000 40.549  0 464 PHE GGG N   1 ? 26 
ATOM   8700  C CA  . PHE G  1 135 ? 23.992  -0.739   51.217  1.000 40.743  0 464 PHE GGG CA  1 ? 26 
ATOM   8701  C C   . PHE G  1 135 ? 23.295  0.608    51.389  1.000 40.621  0 464 PHE GGG C   1 ? 26 
ATOM   8702  O O   . PHE G  1 135 ? 22.813  0.869    52.498  1.000 39.706  0 464 PHE GGG O   1 ? 26 
ATOM   8703  C CB  . PHE G  1 135 ? 24.887  -1.081   52.410  1.000 40.160  0 464 PHE GGG CB  1 ? 26 
ATOM   8704  C CG  . PHE G  1 135 ? 25.399  -2.495   52.415  1.000 39.470  0 464 PHE GGG CG  1 ? 26 
ATOM   8705  C CD1 . PHE G  1 135 ? 24.522  -3.557   52.332  1.000 40.382  0 464 PHE GGG CD1 1 ? 26 
ATOM   8706  C CD2 . PHE G  1 135 ? 26.750  -2.760   52.512  1.000 39.241  0 464 PHE GGG CD2 1 ? 26 
ATOM   8707  C CE1 . PHE G  1 135 ? 24.984  -4.870   52.367  1.000 41.967  0 464 PHE GGG CE1 1 ? 26 
ATOM   8708  C CE2 . PHE G  1 135 ? 27.214  -4.063   52.557  1.000 39.944  0 464 PHE GGG CE2 1 ? 26 
ATOM   8709  C CZ  . PHE G  1 135 ? 26.339  -5.117   52.447  1.000 41.036  0 464 PHE GGG CZ  1 ? 26 
ATOM   8710  N N   . GLU G  1 136 ? 23.202  1.419    50.334  1.000 42.113  0 465 GLU GGG N   1 ? 26 
ATOM   8711  C CA  . GLU G  1 136 ? 22.395  2.665    50.363  1.000 44.316  0 465 GLU GGG CA  1 ? 26 
ATOM   8712  C C   . GLU G  1 136 ? 20.915  2.279    50.261  1.000 43.369  0 465 GLU GGG C   1 ? 26 
ATOM   8713  O O   . GLU G  1 136 ? 20.583  1.250    49.695  1.000 41.008  0 465 GLU GGG O   1 ? 26 
ATOM   8714  C CB  . GLU G  1 136 ? 22.826  3.647    49.270  1.000 45.817  0 465 GLU GGG CB  1 ? 26 
ATOM   8715  C CG  . GLU G  1 136 ? 22.337  5.065    49.488  1.000 46.531  0 465 GLU GGG CG  1 ? 26 
ATOM   8716  C CD  . GLU G  1 136 ? 22.746  6.089    48.440  1.000 49.247  0 465 GLU GGG CD  1 ? 26 
ATOM   8717  O OE1 . GLU G  1 136 ? 23.535  5.756    47.515  1.000 46.136  0 465 GLU GGG OE1 1 ? 26 
ATOM   8718  O OE2 . GLU G  1 136 ? 22.250  7.247    48.549  1.000 56.160  0 465 GLU GGG OE2 1 ? 26 
ATOM   8719  N N   . ARG G  1 137 ? 20.069  3.095    50.862  1.000 44.393  0 466 ARG GGG N   1 ? 26 
ATOM   8720  C CA  . ARG G  1 137 ? 18.609  2.913    50.934  1.000 43.506  0 466 ARG GGG CA  1 ? 26 
ATOM   8721  C C   . ARG G  1 137 ? 17.981  4.249    50.568  1.000 44.684  0 466 ARG GGG C   1 ? 26 
ATOM   8722  O O   . ARG G  1 137 ? 18.370  5.257    51.163  1.000 44.988  0 466 ARG GGG O   1 ? 26 
ATOM   8723  C CB  . ARG G  1 137 ? 18.231  2.536    52.356  1.000 42.729  0 466 ARG GGG CB  1 ? 26 
ATOM   8724  C CG  . ARG G  1 137 ? 16.782  2.131    52.548  1.000 45.437  0 466 ARG GGG CG  1 ? 26 
ATOM   8725  C CD  . ARG G  1 137 ? 16.750  1.423    53.874  1.000 48.318  0 466 ARG GGG CD  1 ? 26 
ATOM   8726  N NE  . ARG G  1 137 ? 15.455  0.929    54.222  1.000 50.770  0 466 ARG GGG NE  1 ? 26 
ATOM   8727  C CZ  . ARG G  1 137 ? 14.520  1.608    54.882  1.000 58.678  0 466 ARG GGG CZ  1 ? 26 
ATOM   8728  N NH1 . ARG G  1 137 ? 14.724  2.868    55.239  1.000 61.247  0 466 ARG GGG NH1 1 ? 26 
ATOM   8729  N NH2 . ARG G  1 137 ? 13.366  1.022    55.181  1.000 61.294  0 466 ARG GGG NH2 1 ? 26 
ATOM   8730  N N   . ASP G  1 138 ? 17.074  4.255    49.598  1.000 43.644  0 467 ASP GGG N   1 ? 26 
ATOM   8731  C CA  . ASP G  1 138 ? 16.418  5.497    49.135  1.000 43.676  0 467 ASP GGG CA  1 ? 26 
ATOM   8732  C C   . ASP G  1 138 ? 14.922  5.261    49.263  1.000 44.513  0 467 ASP GGG C   1 ? 26 
ATOM   8733  O O   . ASP G  1 138 ? 14.410  4.386    48.565  1.000 44.814  0 467 ASP GGG O   1 ? 26 
ATOM   8734  C CB  . ASP G  1 138 ? 16.880  5.869    47.726  1.000 43.733  0 467 ASP GGG CB  1 ? 26 
ATOM   8735  C CG  . ASP G  1 138 ? 16.324  7.176    47.217  1.000 44.630  0 467 ASP GGG CG  1 ? 26 
ATOM   8736  O OD1 . ASP G  1 138 ? 15.428  7.729    47.873  1.000 44.249  0 467 ASP GGG OD1 1 ? 26 
ATOM   8737  O OD2 . ASP G  1 138 ? 16.791  7.633    46.150  1.000 44.266  0 467 ASP GGG OD2 1 ? 26 
ATOM   8738  N N   . ILE G  1 139 ? 14.264  5.997    50.155  1.000 45.529  0 468 ILE GGG N   1 ? 26 
ATOM   8739  C CA  . ILE G  1 139 ? 12.796  5.914    50.389  1.000 45.046  0 468 ILE GGG CA  1 ? 26 
ATOM   8740  C C   . ILE G  1 139 ? 12.160  7.239    49.971  1.000 45.564  0 468 ILE GGG C   1 ? 26 
ATOM   8741  O O   . ILE G  1 139 ? 10.983  7.405    50.239  1.000 48.292  0 468 ILE GGG O   1 ? 26 
ATOM   8742  C CB  . ILE G  1 139 ? 12.553  5.560    51.869  1.000 47.681  0 468 ILE GGG CB  1 ? 26 
ATOM   8743  C CG1 . ILE G  1 139 ? 13.130  6.601    52.838  1.000 48.416  0 468 ILE GGG CG1 1 ? 26 
ATOM   8744  C CG2 . ILE G  1 139 ? 13.075  4.142    52.166  1.000 48.069  0 468 ILE GGG CG2 1 ? 26 
ATOM   8745  C CD1 . ILE G  1 139 ? 12.586  6.488    54.231  1.000 51.106  0 468 ILE GGG CD1 1 ? 26 
ATOM   8746  N N   . SER G  1 140 ? 12.894  8.122    49.278  1.000 44.792  0 469 SER GGG N   1 ? 26 
ATOM   8747  C CA  . SER G  1 140 ? 12.371  9.412    48.769  1.000 45.179  0 469 SER GGG CA  1 ? 26 
ATOM   8748  C C   . SER G  1 140 ? 11.355  9.131    47.656  1.000 45.995  0 469 SER GGG C   1 ? 26 
ATOM   8749  O O   . SER G  1 140 ? 11.439  8.062    47.008  1.000 46.542  0 469 SER GGG O   1 ? 26 
ATOM   8750  C CB  . SER G  1 140 ? 13.475  10.309   48.286  1.000 44.849  0 469 SER GGG CB  1 ? 26 
ATOM   8751  O OG  . SER G  1 140 ? 14.049  9.785    47.106  1.000 45.456  0 469 SER GGG OG  1 ? 26 
ATOM   8752  N N   . THR G  1 141 ? 10.423  10.051   47.448  1.000 46.561  0 470 THR GGG N   1 ? 26 
ATOM   8753  C CA  . THR G  1 141 ? 9.355   9.934    46.435  1.000 48.898  0 470 THR GGG CA  1 ? 26 
ATOM   8754  C C   . THR G  1 141 ? 9.299   11.241   45.643  1.000 50.631  0 470 THR GGG C   1 ? 26 
ATOM   8755  O O   . THR G  1 141 ? 8.215   11.740   45.407  1.000 53.707  0 470 THR GGG O   1 ? 26 
ATOM   8756  C CB  . THR G  1 141 ? 8.027   9.511    47.090  1.000 50.290  0 470 THR GGG CB  1 ? 26 
ATOM   8757  O OG1 . THR G  1 141 ? 7.743   10.452   48.126  1.000 50.112  0 470 THR GGG OG1 1 ? 26 
ATOM   8758  C CG2 . THR G  1 141 ? 8.076   8.101    47.671  1.000 49.263  0 470 THR GGG CG2 1 ? 26 
ATOM   8759  N N   . GLU G  1 142 ? 10.453  11.754   45.271  1.000 52.124  0 471 GLU GGG N   1 ? 26 
ATOM   8760  C CA  . GLU G  1 142 ? 10.590  13.012   44.489  1.000 54.304  0 471 GLU GGG CA  1 ? 26 
ATOM   8761  C C   . GLU G  1 142 ? 10.229  12.691   43.032  1.000 55.524  0 471 GLU GGG C   1 ? 26 
ATOM   8762  O O   . GLU G  1 142 ? 10.577  11.590   42.546  1.000 57.077  0 471 GLU GGG O   1 ? 26 
ATOM   8763  C CB  . GLU G  1 142 ? 11.997  13.604   44.587  1.000 55.935  0 471 GLU GGG CB  1 ? 26 
ATOM   8764  C CG  . GLU G  1 142 ? 12.482  13.844   46.014  1.000 58.766  0 471 GLU GGG CG  1 ? 26 
ATOM   8765  C CD  . GLU G  1 142 ? 11.705  14.895   46.810  1.000 62.960  0 471 GLU GGG CD  1 ? 26 
ATOM   8766  O OE1 . GLU G  1 142 ? 11.609  16.039   46.311  1.000 64.942  0 471 GLU GGG OE1 1 ? 26 
ATOM   8767  O OE2 . GLU G  1 142 ? 11.160  14.565   47.905  1.000 63.347  0 471 GLU GGG OE2 1 ? 26 
ATOM   8768  N N   . ILE G  1 143 ? 9.518   13.607   42.378  1.000 57.633  0 472 ILE GGG N   1 ? 26 
ATOM   8769  C CA  . ILE G  1 143 ? 9.138   13.490   40.944  1.000 58.720  0 472 ILE GGG CA  1 ? 26 
ATOM   8770  C C   . ILE G  1 143 ? 10.426  13.414   40.134  1.000 56.926  0 472 ILE GGG C   1 ? 26 
ATOM   8771  O O   . ILE G  1 143 ? 11.273  14.279   40.322  1.000 56.121  0 472 ILE GGG O   1 ? 26 
ATOM   8772  C CB  . ILE G  1 143 ? 8.227   14.646   40.487  1.000 62.311  0 472 ILE GGG CB  1 ? 26 
ATOM   8773  C CG1 . ILE G  1 143 ? 6.940   14.657   41.311  1.000 63.921  0 472 ILE GGG CG1 1 ? 26 
ATOM   8774  C CG2 . ILE G  1 143 ? 7.947   14.569   38.980  1.000 63.088  0 472 ILE GGG CG2 1 ? 26 
ATOM   8775  C CD1 . ILE G  1 143 ? 6.247   13.302   41.386  1.000 64.031  0 472 ILE GGG CD1 1 ? 26 
ATOM   8776  N N   . TYR G  1 144 ? 10.558  12.387   39.308  1.000 55.592  0 473 TYR GGG N   1 ? 26 
ATOM   8777  C CA  . TYR G  1 144 ? 11.757  12.152   38.476  1.000 55.221  0 473 TYR GGG CA  1 ? 26 
ATOM   8778  C C   . TYR G  1 144 ? 11.596  12.921   37.171  1.000 57.562  0 473 TYR GGG C   1 ? 26 
ATOM   8779  O O   . TYR G  1 144 ? 10.552  12.736   36.517  1.000 60.579  0 473 TYR GGG O   1 ? 26 
ATOM   8780  C CB  . TYR G  1 144 ? 11.984  10.656   38.299  1.000 54.267  0 473 TYR GGG CB  1 ? 26 
ATOM   8781  C CG  . TYR G  1 144 ? 13.122  10.298   37.392  1.000 53.724  0 473 TYR GGG CG  1 ? 26 
ATOM   8782  C CD1 . TYR G  1 144 ? 14.423  10.216   37.858  1.000 52.350  0 473 TYR GGG CD1 1 ? 26 
ATOM   8783  C CD2 . TYR G  1 144 ? 12.881  9.994    36.068  1.000 53.576  0 473 TYR GGG CD2 1 ? 26 
ATOM   8784  C CE1 . TYR G  1 144 ? 15.464  9.894    36.996  1.000 52.192  0 473 TYR GGG CE1 1 ? 26 
ATOM   8785  C CE2 . TYR G  1 144 ? 13.916  9.632    35.214  1.000 53.013  0 473 TYR GGG CE2 1 ? 26 
ATOM   8786  C CZ  . TYR G  1 144 ? 15.204  9.568    35.684  1.000 51.738  0 473 TYR GGG CZ  1 ? 26 
ATOM   8787  O OH  . TYR G  1 144 ? 16.225  9.235    34.859  1.000 54.076  0 473 TYR GGG OH  1 ? 26 
ATOM   8788  N N   . GLN G  1 145 ? 12.563  13.780   36.842  1.000 56.330  0 474 GLN GGG N   1 ? 26 
ATOM   8789  C CA  . GLN G  1 145 ? 12.603  14.480   35.531  1.000 58.072  0 474 GLN GGG CA  1 ? 26 
ATOM   8790  C C   . GLN G  1 145 ? 13.250  13.552   34.494  1.000 59.479  0 474 GLN GGG C   1 ? 26 
ATOM   8791  O O   . GLN G  1 145 ? 14.489  13.421   34.517  1.000 59.129  0 474 GLN GGG O   1 ? 26 
ATOM   8792  C CB  . GLN G  1 145 ? 13.343  15.811   35.592  1.000 57.925  0 474 GLN GGG CB  1 ? 26 
ATOM   8793  C CG  . GLN G  1 145 ? 13.461  16.439   34.215  1.000 59.748  0 474 GLN GGG CG  1 ? 26 
ATOM   8794  C CD  . GLN G  1 145 ? 13.975  17.838   34.287  1.000 60.781  0 474 GLN GGG CD  1 ? 26 
ATOM   8795  O OE1 . GLN G  1 145 ? 13.925  18.477   35.319  1.000 62.083  0 474 GLN GGG OE1 1 ? 26 
ATOM   8796  N NE2 . GLN G  1 145 ? 14.468  18.328   33.173  1.000 63.093  0 474 GLN GGG NE2 1 ? 26 
ATOM   8797  N N   . ALA G  1 146 ? 12.425  12.911   33.663  1.000 62.636  0 475 ALA GGG N   1 ? 26 
ATOM   8798  C CA  . ALA G  1 146 ? 12.832  11.906   32.654  1.000 63.840  0 475 ALA GGG CA  1 ? 26 
ATOM   8799  C C   . ALA G  1 146 ? 13.131  12.588   31.323  1.000 68.024  0 475 ALA GGG C   1 ? 26 
ATOM   8800  O O   . ALA G  1 146 ? 13.761  11.944   30.461  1.000 70.190  0 475 ALA GGG O   1 ? 26 
ATOM   8801  C CB  . ALA G  1 146 ? 11.753  10.864   32.481  1.000 63.559  0 475 ALA GGG CB  1 ? 26 
ATOM   8802  N N   . GLY G  1 147 ? 12.727  13.847   31.161  1.000 69.992  0 476 GLY GGG N   1 ? 26 
ATOM   8803  C CA  . GLY G  1 147 ? 12.807  14.532   29.861  1.000 74.716  0 476 GLY GGG CA  1 ? 26 
ATOM   8804  C C   . GLY G  1 147 ? 13.405  15.911   29.984  1.000 76.854  0 476 GLY GGG C   1 ? 26 
ATOM   8805  O O   . GLY G  1 147 ? 13.867  16.278   31.086  1.000 77.559  0 476 GLY GGG O   1 ? 26 
ATOM   8806  N N   . SER G  1 148 ? 13.403  16.630   28.870  1.000 79.572  0 477 SER GGG N   1 ? 26 
ATOM   8807  C CA  . SER G  1 148 ? 13.940  18.002   28.724  1.000 81.558  0 477 SER GGG CA  1 ? 26 
ATOM   8808  C C   . SER G  1 148 ? 13.243  18.951   29.713  1.000 81.638  0 477 SER GGG C   1 ? 26 
ATOM   8809  O O   . SER G  1 148 ? 13.958  19.730   30.367  1.000 80.040  0 477 SER GGG O   1 ? 26 
ATOM   8810  C CB  . SER G  1 148 ? 13.777  18.444   27.304  1.000 84.602  0 477 SER GGG CB  1 ? 26 
ATOM   8811  O OG  . SER G  1 148 ? 14.336  19.723   27.127  1.000 89.610  0 477 SER GGG OG  1 ? 26 
ATOM   8812  N N   . THR G  1 149 ? 11.904  18.910   29.797  1.000 81.384  0 478 THR GGG N   1 ? 26 
ATOM   8813  C CA  . THR G  1 149 ? 11.082  19.902   30.546  1.000 81.059  0 478 THR GGG CA  1 ? 26 
ATOM   8814  C C   . THR G  1 149 ? 11.316  19.745   32.046  1.000 77.043  0 478 THR GGG C   1 ? 26 
ATOM   8815  O O   . THR G  1 149 ? 11.367  18.628   32.543  1.000 73.979  0 478 THR GGG O   1 ? 26 
ATOM   8816  C CB  . THR G  1 149 ? 9.584   19.787   30.234  1.000 82.671  0 478 THR GGG CB  1 ? 26 
ATOM   8817  O OG1 . THR G  1 149 ? 9.392   19.597   28.835  1.000 87.050  0 478 THR GGG OG1 1 ? 26 
ATOM   8818  C CG2 . THR G  1 149 ? 8.814   21.015   30.680  1.000 84.597  0 478 THR GGG CG2 1 ? 26 
ATOM   8819  N N   . PRO G  1 150 ? 11.458  20.852   32.818  1.000 78.338  0 479 PRO GGG N   1 ? 26 
ATOM   8820  C CA  . PRO G  1 150 ? 11.493  20.759   34.280  1.000 77.168  0 479 PRO GGG CA  1 ? 26 
ATOM   8821  C C   . PRO G  1 150 ? 10.101  20.369   34.795  1.000 78.282  0 479 PRO GGG C   1 ? 26 
ATOM   8822  O O   . PRO G  1 150 ? 9.122   20.658   34.127  1.000 81.229  0 479 PRO GGG O   1 ? 26 
ATOM   8823  C CB  . PRO G  1 150 ? 11.959  22.153   34.724  1.000 78.763  0 479 PRO GGG CB  1 ? 26 
ATOM   8824  C CG  . PRO G  1 150 ? 11.501  23.076   33.601  1.000 81.351  0 479 PRO GGG CG  1 ? 26 
ATOM   8825  C CD  . PRO G  1 150 ? 11.571  22.246   32.335  1.000 81.216  0 479 PRO GGG CD  1 ? 26 
ATOM   8826  N N   . CYS G  1 151 ? 10.029  19.727   35.961  1.000 78.549  0 480 CYS GGG N   1 ? 26 
ATOM   8827  C CA  . CYS G  1 151 ? 8.773   19.130   36.494  1.000 79.316  0 480 CYS GGG CA  1 ? 26 
ATOM   8828  C C   . CYS G  1 151 ? 8.053   20.091   37.438  1.000 80.102  0 480 CYS GGG C   1 ? 26 
ATOM   8829  O O   . CYS G  1 151 ? 6.850   19.908   37.582  1.000 79.535  0 480 CYS GGG O   1 ? 26 
ATOM   8830  C CB  . CYS G  1 151 ? 9.054   17.800   37.172  1.000 79.071  0 480 CYS GGG CB  1 ? 26 
ATOM   8831  S SG  . CYS G  1 151 ? 9.492   16.514   35.973  1.000 84.155  0 480 CYS GGG SG  1 ? 26 
ATOM   8832  N N   . ASN G  1 152 ? 8.743   21.078   38.009  1.000 82.040  0 481 ASN GGG N   1 ? 26 
ATOM   8833  C CA  . ASN G  1 152 ? 8.167   22.122   38.903  1.000 83.363  0 481 ASN GGG CA  1 ? 26 
ATOM   8834  C C   . ASN G  1 152 ? 7.269   21.479   39.979  1.000 84.120  0 481 ASN GGG C   1 ? 26 
ATOM   8835  O O   . ASN G  1 152 ? 6.197   22.056   40.298  1.000 85.264  0 481 ASN GGG O   1 ? 26 
ATOM   8836  C CB  . ASN G  1 152 ? 7.377   23.176   38.130  1.000 84.220  0 481 ASN GGG CB  1 ? 26 
ATOM   8837  C CG  . ASN G  1 152 ? 7.059   24.384   39.001  1.000 86.114  0 481 ASN GGG CG  1 ? 26 
ATOM   8838  O OD1 . ASN G  1 152 ? 7.875   24.792   39.814  1.000 84.152  0 481 ASN GGG OD1 1 ? 26 
ATOM   8839  N ND2 . ASN G  1 152 ? 5.873   24.963   38.879  1.000 88.557  0 481 ASN GGG ND2 1 ? 26 
ATOM   8840  N N   . GLY G  1 153 ? 7.687   20.317   40.503  1.000 82.867  0 482 GLY GGG N   1 ? 26 
ATOM   8841  C CA  . GLY G  1 153 ? 7.002   19.586   41.586  1.000 83.123  0 482 GLY GGG CA  1 ? 26 
ATOM   8842  C C   . GLY G  1 153 ? 5.586   19.169   41.233  1.000 86.548  0 482 GLY GGG C   1 ? 26 
ATOM   8843  O O   . GLY G  1 153 ? 4.757   19.061   42.166  1.000 88.964  0 482 GLY GGG O   1 ? 26 
ATOM   8844  N N   . VAL G  1 154 ? 5.304   18.928   39.948  1.000 87.017  0 483 VAL GGG N   1 ? 26 
ATOM   8845  C CA  . VAL G  1 154 ? 4.000   18.400   39.436  1.000 84.470  0 483 VAL GGG CA  1 ? 26 
ATOM   8846  C C   . VAL G  1 154 ? 4.285   17.144   38.611  1.000 81.296  0 483 VAL GGG C   1 ? 26 
ATOM   8847  O O   . VAL G  1 154 ? 5.277   17.127   37.875  1.000 79.672  0 483 VAL GGG O   1 ? 26 
ATOM   8848  C CB  . VAL G  1 154 ? 3.271   19.474   38.604  1.000 88.927  0 483 VAL GGG CB  1 ? 26 
ATOM   8849  C CG1 . VAL G  1 154 ? 2.122   18.890   37.807  1.000 91.392  0 483 VAL GGG CG1 1 ? 26 
ATOM   8850  C CG2 . VAL G  1 154 ? 2.813   20.666   39.440  1.000 90.893  0 483 VAL GGG CG2 1 ? 26 
ATOM   8851  N N   . GLU G  1 155 ? 3.445   16.122   38.720  1.000 81.711  0 484 GLU GGG N   1 ? 26 
ATOM   8852  C CA  . GLU G  1 155 ? 3.521   14.855   37.935  1.000 80.857  0 484 GLU GGG CA  1 ? 26 
ATOM   8853  C C   . GLU G  1 155 ? 2.967   15.106   36.523  1.000 82.238  0 484 GLU GGG C   1 ? 26 
ATOM   8854  O O   . GLU G  1 155 ? 2.105   16.003   36.375  1.000 84.537  0 484 GLU GGG O   1 ? 26 
ATOM   8855  C CB  . GLU G  1 155 ? 2.677   13.767   38.607  1.000 82.569  0 484 GLU GGG CB  1 ? 26 
ATOM   8856  C CG  . GLU G  1 155 ? 2.848   13.616   40.097  1.000 82.333  0 484 GLU GGG CG  1 ? 26 
ATOM   8857  C CD  . GLU G  1 155 ? 2.577   12.194   40.590  1.000 83.194  0 484 GLU GGG CD  1 ? 26 
ATOM   8858  O OE1 . GLU G  1 155 ? 2.588   11.237   39.757  1.000 83.840  0 484 GLU GGG OE1 1 ? 26 
ATOM   8859  O OE2 . GLU G  1 155 ? 2.384   12.028   41.814  1.000 80.768  0 484 GLU GGG OE2 1 ? 26 
ATOM   8860  N N   . GLY G  1 156 ? 3.395   14.333   35.527  1.000 80.470  0 485 GLY GGG N   1 ? 26 
ATOM   8861  C CA  . GLY G  1 156 ? 2.824   14.328   34.165  1.000 83.417  0 485 GLY GGG CA  1 ? 26 
ATOM   8862  C C   . GLY G  1 156 ? 3.738   13.652   33.159  1.000 85.538  0 485 GLY GGG C   1 ? 26 
ATOM   8863  O O   . GLY G  1 156 ? 4.569   12.844   33.576  1.000 88.766  0 485 GLY GGG O   1 ? 26 
ATOM   8864  N N   . PHE G  1 157 ? 3.601   13.983   31.873  1.000 91.182  0 486 PHE GGG N   1 ? 26 
ATOM   8865  C CA  . PHE G  1 157 ? 4.479   13.522   30.764  1.000 92.555  0 486 PHE GGG CA  1 ? 26 
ATOM   8866  C C   . PHE G  1 157 ? 5.943   13.785   31.154  1.000 88.813  0 486 PHE GGG C   1 ? 26 
ATOM   8867  O O   . PHE G  1 157 ? 6.290   14.930   31.533  1.000 87.686  0 486 PHE GGG O   1 ? 26 
ATOM   8868  C CB  . PHE G  1 157 ? 4.068   14.208   29.455  1.000 97.967  0 486 PHE GGG CB  1 ? 26 
ATOM   8869  C CG  . PHE G  1 157 ? 4.901   13.889   28.234  1.000 101.949 0 486 PHE GGG CG  1 ? 26 
ATOM   8870  C CD1 . PHE G  1 157 ? 5.475   12.634   28.024  1.000 103.834 0 486 PHE GGG CD1 1 ? 26 
ATOM   8871  C CD2 . PHE G  1 157 ? 5.063   14.850   27.248  1.000 107.565 0 486 PHE GGG CD2 1 ? 26 
ATOM   8872  C CE1 . PHE G  1 157 ? 6.232   12.379   26.889  1.000 105.463 0 486 PHE GGG CE1 1 ? 26 
ATOM   8873  C CE2 . PHE G  1 157 ? 5.803   14.589   26.098  1.000 109.631 0 486 PHE GGG CE2 1 ? 26 
ATOM   8874  C CZ  . PHE G  1 157 ? 6.385   13.353   25.921  1.000 108.082 0 486 PHE GGG CZ  1 ? 26 
ATOM   8875  N N   . ASN G  1 158 ? 6.767   12.734   31.134  1.000 85.937  0 487 ASN GGG N   1 ? 26 
ATOM   8876  C CA  . ASN G  1 158 ? 8.233   12.759   31.415  1.000 84.847  0 487 ASN GGG CA  1 ? 26 
ATOM   8877  C C   . ASN G  1 158 ? 8.504   13.245   32.845  1.000 81.333  0 487 ASN GGG C   1 ? 26 
ATOM   8878  O O   . ASN G  1 158 ? 9.661   13.607   33.129  1.000 78.501  0 487 ASN GGG O   1 ? 26 
ATOM   8879  C CB  . ASN G  1 158 ? 8.990   13.615   30.401  1.000 86.149  0 487 ASN GGG CB  1 ? 26 
ATOM   8880  C CG  . ASN G  1 158 ? 9.014   13.004   29.026  1.000 87.939  0 487 ASN GGG CG  1 ? 26 
ATOM   8881  O OD1 . ASN G  1 158 ? 9.181   11.801   28.877  1.000 89.169  0 487 ASN GGG OD1 1 ? 26 
ATOM   8882  N ND2 . ASN G  1 158 ? 8.861   13.836   28.015  1.000 95.052  0 487 ASN GGG ND2 1 ? 26 
ATOM   8883  N N   . CYS G  1 159 ? 7.495   13.212   33.716  1.000 78.901  0 488 CYS GGG N   1 ? 26 
ATOM   8884  C CA  . CYS G  1 159 ? 7.574   13.690   35.118  1.000 76.496  0 488 CYS GGG CA  1 ? 26 
ATOM   8885  C C   . CYS G  1 159 ? 6.946   12.631   36.030  1.000 74.667  0 488 CYS GGG C   1 ? 26 
ATOM   8886  O O   . CYS G  1 159 ? 5.757   12.775   36.371  1.000 76.301  0 488 CYS GGG O   1 ? 26 
ATOM   8887  C CB  . CYS G  1 159 ? 6.905   15.051   35.274  1.000 77.190  0 488 CYS GGG CB  1 ? 26 
ATOM   8888  S SG  . CYS G  1 159 ? 7.910   16.405   34.629  1.000 76.870  0 488 CYS GGG SG  1 ? 26 
ATOM   8889  N N   . TYR G  1 160 ? 7.718   11.601   36.372  1.000 71.217  0 489 TYR GGG N   1 ? 26 
ATOM   8890  C CA  . TYR G  1 160 ? 7.211   10.320   36.902  1.000 66.443  0 489 TYR GGG CA  1 ? 26 
ATOM   8891  C C   . TYR G  1 160 ? 7.417   10.274   38.413  1.000 63.327  0 489 TYR GGG C   1 ? 26 
ATOM   8892  O O   . TYR G  1 160 ? 8.464   10.728   38.924  1.000 62.321  0 489 TYR GGG O   1 ? 26 
ATOM   8893  C CB  . TYR G  1 160 ? 7.887   9.145    36.192  1.000 66.000  0 489 TYR GGG CB  1 ? 26 
ATOM   8894  C CG  . TYR G  1 160 ? 7.694   9.174    34.707  1.000 70.396  0 489 TYR GGG CG  1 ? 26 
ATOM   8895  C CD1 . TYR G  1 160 ? 6.451   9.425    34.149  1.000 74.527  0 489 TYR GGG CD1 1 ? 26 
ATOM   8896  C CD2 . TYR G  1 160 ? 8.773   9.044    33.860  1.000 71.870  0 489 TYR GGG CD2 1 ? 26 
ATOM   8897  C CE1 . TYR G  1 160 ? 6.276   9.471    32.774  1.000 77.235  0 489 TYR GGG CE1 1 ? 26 
ATOM   8898  C CE2 . TYR G  1 160 ? 8.625   9.073    32.481  1.000 76.001  0 489 TYR GGG CE2 1 ? 26 
ATOM   8899  C CZ  . TYR G  1 160 ? 7.368   9.285    31.936  1.000 77.873  0 489 TYR GGG CZ  1 ? 26 
ATOM   8900  O OH  . TYR G  1 160 ? 7.245   9.354    30.580  1.000 80.185  0 489 TYR GGG OH  1 ? 26 
ATOM   8901  N N   . PHE G  1 161 ? 6.408   9.753    39.100  1.000 61.376  0 490 PHE GGG N   1 ? 26 
ATOM   8902  C CA  . PHE G  1 161 ? 6.536   9.212    40.468  1.000 58.727  0 490 PHE GGG CA  1 ? 26 
ATOM   8903  C C   . PHE G  1 161 ? 7.508   8.051    40.362  1.000 55.567  0 490 PHE GGG C   1 ? 26 
ATOM   8904  O O   . PHE G  1 161 ? 7.345   7.210    39.497  1.000 56.551  0 490 PHE GGG O   1 ? 26 
ATOM   8905  C CB  . PHE G  1 161 ? 5.167   8.815    41.011  1.000 59.475  0 490 PHE GGG CB  1 ? 26 
ATOM   8906  C CG  . PHE G  1 161 ? 5.173   8.401    42.456  1.000 57.371  0 490 PHE GGG CG  1 ? 26 
ATOM   8907  C CD1 . PHE G  1 161 ? 5.239   9.357    43.448  1.000 58.526  0 490 PHE GGG CD1 1 ? 26 
ATOM   8908  C CD2 . PHE G  1 161 ? 5.117   7.062    42.811  1.000 55.990  0 490 PHE GGG CD2 1 ? 26 
ATOM   8909  C CE1 . PHE G  1 161 ? 5.238   8.985    44.784  1.000 58.890  0 490 PHE GGG CE1 1 ? 26 
ATOM   8910  C CE2 . PHE G  1 161 ? 5.104   6.688    44.144  1.000 55.620  0 490 PHE GGG CE2 1 ? 26 
ATOM   8911  C CZ  . PHE G  1 161 ? 5.171   7.651    45.132  1.000 56.902  0 490 PHE GGG CZ  1 ? 26 
ATOM   8912  N N   . PRO G  1 162 ? 8.587   8.010    41.175  1.000 53.319  0 491 PRO GGG N   1 ? 26 
ATOM   8913  C CA  . PRO G  1 162 ? 9.707   7.108    40.897  1.000 51.196  0 491 PRO GGG CA  1 ? 26 
ATOM   8914  C C   . PRO G  1 162 ? 9.508   5.649    41.326  1.000 51.582  0 491 PRO GGG C   1 ? 26 
ATOM   8915  O O   . PRO G  1 162 ? 10.325  4.810    40.951  1.000 51.964  0 491 PRO GGG O   1 ? 26 
ATOM   8916  C CB  . PRO G  1 162 ? 10.840  7.773    41.686  1.000 50.262  0 491 PRO GGG CB  1 ? 26 
ATOM   8917  C CG  . PRO G  1 162 ? 10.147  8.403    42.869  1.000 51.458  0 491 PRO GGG CG  1 ? 26 
ATOM   8918  C CD  . PRO G  1 162 ? 8.803   8.863    42.364  1.000 53.431  0 491 PRO GGG CD  1 ? 26 
ATOM   8919  N N   . LEU G  1 163 ? 8.459   5.352    42.098  1.000 52.808  0 492 LEU GGG N   1 ? 26 
ATOM   8920  C CA  . LEU G  1 163 ? 8.171   3.959    42.572  1.000 51.810  0 492 LEU GGG CA  1 ? 26 
ATOM   8921  C C   . LEU G  1 163 ? 7.103   3.309    41.689  1.000 50.822  0 492 LEU GGG C   1 ? 26 
ATOM   8922  O O   . LEU G  1 163 ? 6.210   4.018    41.284  1.000 52.687  0 492 LEU GGG O   1 ? 26 
ATOM   8923  C CB  . LEU G  1 163 ? 7.709   3.976    44.032  1.000 52.874  0 492 LEU GGG CB  1 ? 26 
ATOM   8924  C CG  . LEU G  1 163 ? 8.665   4.586    45.048  1.000 53.725  0 492 LEU GGG CG  1 ? 26 
ATOM   8925  C CD1 . LEU G  1 163 ? 8.119   4.345    46.460  1.000 53.703  0 492 LEU GGG CD1 1 ? 26 
ATOM   8926  C CD2 . LEU G  1 163 ? 10.073  4.029    44.874  1.000 51.129  0 492 LEU GGG CD2 1 ? 26 
ATOM   8927  N N   . GLN G  1 164 ? 7.207   2.007    41.445  1.000 58.987  0 493 GLN GGG N   1 ? 27 
ATOM   8928  C CA  . GLN G  1 164 ? 6.258   1.210    40.635  1.000 59.523  0 493 GLN GGG CA  1 ? 27 
ATOM   8929  C C   . GLN G  1 164 ? 5.909   -0.054   41.436  1.000 56.807  0 493 GLN GGG C   1 ? 27 
ATOM   8930  O O   . GLN G  1 164 ? 6.736   -0.540   42.236  1.000 52.152  0 493 GLN GGG O   1 ? 27 
ATOM   8931  C CB  . GLN G  1 164 ? 6.889   0.911    39.266  1.000 61.596  0 493 GLN GGG CB  1 ? 27 
ATOM   8932  C CG  . GLN G  1 164 ? 6.016   0.099    38.323  1.000 62.674  0 493 GLN GGG CG  1 ? 27 
ATOM   8933  C CD  . GLN G  1 164 ? 4.793   0.868    37.911  1.000 67.088  0 493 GLN GGG CD  1 ? 27 
ATOM   8934  O OE1 . GLN G  1 164 ? 3.696   0.561    38.360  1.000 69.865  0 493 GLN GGG OE1 1 ? 27 
ATOM   8935  N NE2 . GLN G  1 164 ? 4.982   1.884    37.081  1.000 69.578  0 493 GLN GGG NE2 1 ? 27 
ATOM   8936  N N   . SER G  1 165 ? 4.705   -0.566   41.234  1.000 56.828  0 494 SER GGG N   1 ? 27 
ATOM   8937  C CA  . SER G  1 165 ? 4.177   -1.767   41.912  1.000 55.191  0 494 SER GGG CA  1 ? 27 
ATOM   8938  C C   . SER G  1 165 ? 4.549   -3.010   41.095  1.000 52.237  0 494 SER GGG C   1 ? 27 
ATOM   8939  O O   . SER G  1 165 ? 4.576   -2.905   39.880  1.000 51.326  0 494 SER GGG O   1 ? 27 
ATOM   8940  C CB  . SER G  1 165 ? 2.688   -1.608   42.107  1.000 58.634  0 494 SER GGG CB  1 ? 27 
ATOM   8941  O OG  . SER G  1 165 ? 2.161   -0.467   41.408  1.000 65.866  0 494 SER GGG OG  1 ? 27 
ATOM   8942  N N   . TYR G  1 166 ? 4.809   -4.139   41.744  1.000 51.213  0 495 TYR GGG N   1 ? 27 
ATOM   8943  C CA  . TYR G  1 166 ? 5.099   -5.425   41.063  1.000 51.492  0 495 TYR GGG CA  1 ? 27 
ATOM   8944  C C   . TYR G  1 166 ? 3.811   -6.048   40.507  1.000 55.445  0 495 TYR GGG C   1 ? 27 
ATOM   8945  O O   . TYR G  1 166 ? 3.841   -6.622   39.398  1.000 56.891  0 495 TYR GGG O   1 ? 27 
ATOM   8946  C CB  . TYR G  1 166 ? 5.797   -6.428   41.978  1.000 49.091  0 495 TYR GGG CB  1 ? 27 
ATOM   8947  C CG  . TYR G  1 166 ? 7.293   -6.286   42.046  1.000 47.270  0 495 TYR GGG CG  1 ? 27 
ATOM   8948  C CD1 . TYR G  1 166 ? 8.084   -6.602   40.959  1.000 47.257  0 495 TYR GGG CD1 1 ? 27 
ATOM   8949  C CD2 . TYR G  1 166 ? 7.916   -5.808   43.187  1.000 47.561  0 495 TYR GGG CD2 1 ? 27 
ATOM   8950  C CE1 . TYR G  1 166 ? 9.463   -6.458   41.001  1.000 46.530  0 495 TYR GGG CE1 1 ? 27 
ATOM   8951  C CE2 . TYR G  1 166 ? 9.293   -5.654   43.250  1.000 47.062  0 495 TYR GGG CE2 1 ? 27 
ATOM   8952  C CZ  . TYR G  1 166 ? 10.071  -6.008   42.162  1.000 45.616  0 495 TYR GGG CZ  1 ? 27 
ATOM   8953  O OH  . TYR G  1 166 ? 11.420  -5.872   42.233  1.000 43.179  0 495 TYR GGG OH  1 ? 27 
ATOM   8954  N N   . GLY G  1 167 ? 2.703   -5.974   41.214  1.000 57.982  0 496 GLY GGG N   1 ? 27 
ATOM   8955  C CA  . GLY G  1 167 ? 1.485   -6.641   40.689  1.000 61.523  0 496 GLY GGG CA  1 ? 27 
ATOM   8956  C C   . GLY G  1 167 ? 1.685   -8.126   40.440  1.000 59.551  0 496 GLY GGG C   1 ? 27 
ATOM   8957  O O   . GLY G  1 167 ? 1.773   -8.532   39.300  1.000 61.034  0 496 GLY GGG O   1 ? 27 
ATOM   8958  N N   . PHE G  1 168 ? 1.792   -8.898   41.512  1.000 57.393  0 497 PHE GGG N   1 ? 27 
ATOM   8959  C CA  . PHE G  1 168 ? 2.090   -10.357  41.493  1.000 54.566  0 497 PHE GGG CA  1 ? 27 
ATOM   8960  C C   . PHE G  1 168 ? 0.778   -11.130  41.363  1.000 56.566  0 497 PHE GGG C   1 ? 27 
ATOM   8961  O O   . PHE G  1 168 ? -0.055  -11.034  42.274  1.000 59.210  0 497 PHE GGG O   1 ? 27 
ATOM   8962  C CB  . PHE G  1 168 ? 2.815   -10.760  42.776  1.000 51.645  0 497 PHE GGG CB  1 ? 27 
ATOM   8963  C CG  . PHE G  1 168 ? 4.236   -10.265  42.896  1.000 48.484  0 497 PHE GGG CG  1 ? 27 
ATOM   8964  C CD1 . PHE G  1 168 ? 5.182   -10.648  41.964  1.000 46.363  0 497 PHE GGG CD1 1 ? 27 
ATOM   8965  C CD2 . PHE G  1 168 ? 4.634   -9.453   43.953  1.000 46.875  0 497 PHE GGG CD2 1 ? 27 
ATOM   8966  C CE1 . PHE G  1 168 ? 6.500   -10.223  42.074  1.000 45.420  0 497 PHE GGG CE1 1 ? 27 
ATOM   8967  C CE2 . PHE G  1 168 ? 5.954   -9.038   44.064  1.000 44.308  0 497 PHE GGG CE2 1 ? 27 
ATOM   8968  C CZ  . PHE G  1 168 ? 6.885   -9.426   43.123  1.000 43.867  0 497 PHE GGG CZ  1 ? 27 
ATOM   8969  N N   . GLN G  1 169 ? 0.616   -11.905  40.291  1.000 57.539  0 498 GLN GGG N   1 ? 27 
ATOM   8970  C CA  . GLN G  1 169 ? -0.541  -12.822  40.109  1.000 58.327  0 498 GLN GGG CA  1 ? 27 
ATOM   8971  C C   . GLN G  1 169 ? -0.058  -14.258  40.159  1.000 56.429  0 498 GLN GGG C   1 ? 27 
ATOM   8972  O O   . GLN G  1 169 ? 1.007   -14.567  39.633  1.000 53.898  0 498 GLN GGG O   1 ? 27 
ATOM   8973  C CB  . GLN G  1 169 ? -1.251  -12.512  38.806  1.000 62.684  0 498 GLN GGG CB  1 ? 27 
ATOM   8974  C CG  . GLN G  1 169 ? -1.788  -11.098  38.858  1.000 67.353  0 498 GLN GGG CG  1 ? 27 
ATOM   8975  C CD  . GLN G  1 169 ? -2.493  -10.722  37.587  1.000 70.736  0 498 GLN GGG CD  1 ? 27 
ATOM   8976  O OE1 . GLN G  1 169 ? -1.879  -10.481  36.553  1.000 71.072  0 498 GLN GGG OE1 1 ? 27 
ATOM   8977  N NE2 . GLN G  1 169 ? -3.807  -10.645  37.672  1.000 76.718  0 498 GLN GGG NE2 1 ? 27 
ATOM   8978  N N   . PRO G  1 170 ? -0.831  -15.162  40.794  1.000 56.488  0 499 PRO GGG N   1 ? 27 
ATOM   8979  C CA  . PRO G  1 170 ? -0.412  -16.548  40.966  1.000 56.380  0 499 PRO GGG CA  1 ? 27 
ATOM   8980  C C   . PRO G  1 170 ? -0.113  -17.235  39.616  1.000 57.513  0 499 PRO GGG C   1 ? 27 
ATOM   8981  O O   . PRO G  1 170 ? 0.693   -18.144  39.612  1.000 56.188  0 499 PRO GGG O   1 ? 27 
ATOM   8982  C CB  . PRO G  1 170 ? -1.581  -17.227  41.717  1.000 57.083  0 499 PRO GGG CB  1 ? 27 
ATOM   8983  C CG  . PRO G  1 170 ? -2.758  -16.275  41.585  1.000 59.169  0 499 PRO GGG CG  1 ? 27 
ATOM   8984  C CD  . PRO G  1 170 ? -2.168  -14.903  41.338  1.000 59.033  0 499 PRO GGG CD  1 ? 27 
ATOM   8985  N N   . THR G  1 171 ? -0.732  -16.772  38.520  1.000 57.041  0 500 THR GGG N   1 ? 27 
ATOM   8986  C CA  . THR G  1 171 ? -0.573  -17.338  37.150  1.000 57.973  0 500 THR GGG CA  1 ? 27 
ATOM   8987  C C   . THR G  1 171 ? 0.650   -16.770  36.401  1.000 56.339  0 500 THR GGG C   1 ? 27 
ATOM   8988  O O   . THR G  1 171 ? 0.961   -17.304  35.329  1.000 56.537  0 500 THR GGG O   1 ? 27 
ATOM   8989  C CB  . THR G  1 171 ? -1.853  -17.108  36.339  1.000 60.787  0 500 THR GGG CB  1 ? 27 
ATOM   8990  O OG1 . THR G  1 171 ? -2.136  -15.707  36.422  1.000 63.450  0 500 THR GGG OG1 1 ? 27 
ATOM   8991  C CG2 . THR G  1 171 ? -3.007  -17.927  36.858  1.000 62.350  0 500 THR GGG CG2 1 ? 27 
ATOM   8992  N N   . ASN G  1 172 ? 1.326   -15.738  36.912  1.000 55.163  0 501 ASN GGG N   1 ? 27 
ATOM   8993  C CA  . ASN G  1 172 ? 2.589   -15.213  36.325  1.000 54.208  0 501 ASN GGG CA  1 ? 27 
ATOM   8994  C C   . ASN G  1 172 ? 3.574   -16.361  36.056  1.000 52.601  0 501 ASN GGG C   1 ? 27 
ATOM   8995  O O   . ASN G  1 172 ? 3.611   -17.295  36.850  1.000 51.185  0 501 ASN GGG O   1 ? 27 
ATOM   8996  C CB  . ASN G  1 172 ? 3.281   -14.223  37.259  1.000 54.322  0 501 ASN GGG CB  1 ? 27 
ATOM   8997  C CG  . ASN G  1 172 ? 2.550   -12.906  37.370  1.000 55.992  0 501 ASN GGG CG  1 ? 27 
ATOM   8998  O OD1 . ASN G  1 172 ? 1.527   -12.714  36.714  1.000 57.173  0 501 ASN GGG OD1 1 ? 27 
ATOM   8999  N ND2 . ASN G  1 172 ? 3.063   -12.010  38.207  1.000 55.782  0 501 ASN GGG ND2 1 ? 27 
ATOM   9000  N N   . GLY G  1 173 ? 4.371   -16.268  34.989  1.000 52.143  0 502 GLY GGG N   1 ? 27 
ATOM   9001  C CA  . GLY G  1 173 ? 5.550   -17.121  34.781  1.000 51.852  0 502 GLY GGG CA  1 ? 27 
ATOM   9002  C C   . GLY G  1 173 ? 6.513   -16.970  35.954  1.000 51.576  0 502 GLY GGG C   1 ? 27 
ATOM   9003  O O   . GLY G  1 173 ? 6.448   -15.935  36.694  1.000 49.553  0 502 GLY GGG O   1 ? 27 
ATOM   9004  N N   . VAL G  1 174 ? 7.380   -17.965  36.154  1.000 53.013  0 503 VAL GGG N   1 ? 27 
ATOM   9005  C CA  . VAL G  1 174 ? 8.220   -18.083  37.387  1.000 53.509  0 503 VAL GGG CA  1 ? 27 
ATOM   9006  C C   . VAL G  1 174 ? 9.084   -16.822  37.545  1.000 55.036  0 503 VAL GGG C   1 ? 27 
ATOM   9007  O O   . VAL G  1 174 ? 9.246   -16.346  38.702  1.000 50.367  0 503 VAL GGG O   1 ? 27 
ATOM   9008  C CB  . VAL G  1 174 ? 9.068   -19.363  37.421  1.000 53.410  0 503 VAL GGG CB  1 ? 27 
ATOM   9009  C CG1 . VAL G  1 174 ? 10.203  -19.342  36.399  1.000 55.208  0 503 VAL GGG CG1 1 ? 27 
ATOM   9010  C CG2 . VAL G  1 174 ? 9.611   -19.573  38.820  1.000 51.978  0 503 VAL GGG CG2 1 ? 27 
ATOM   9011  N N   . GLY G  1 175 ? 9.616   -16.312  36.424  1.000 56.500  0 504 GLY GGG N   1 ? 27 
ATOM   9012  C CA  . GLY G  1 175 ? 10.425  -15.092  36.360  1.000 55.818  0 504 GLY GGG CA  1 ? 27 
ATOM   9013  C C   . GLY G  1 175 ? 9.710   -13.882  36.931  1.000 54.669  0 504 GLY GGG C   1 ? 27 
ATOM   9014  O O   . GLY G  1 175 ? 10.399  -12.999  37.433  1.000 55.609  0 504 GLY GGG O   1 ? 27 
ATOM   9015  N N   . TYR G  1 176 ? 8.376   -13.850  36.887  1.000 55.888  0 505 TYR GGG N   1 ? 27 
ATOM   9016  C CA  . TYR G  1 176 ? 7.560   -12.700  37.359  1.000 56.707  0 505 TYR GGG CA  1 ? 27 
ATOM   9017  C C   . TYR G  1 176 ? 6.856   -13.044  38.688  1.000 55.156  0 505 TYR GGG C   1 ? 27 
ATOM   9018  O O   . TYR G  1 176 ? 5.997   -12.272  39.161  1.000 53.307  0 505 TYR GGG O   1 ? 27 
ATOM   9019  C CB  . TYR G  1 176 ? 6.579   -12.290  36.264  1.000 59.878  0 505 TYR GGG CB  1 ? 27 
ATOM   9020  C CG  . TYR G  1 176 ? 7.212   -11.724  35.019  1.000 66.593  0 505 TYR GGG CG  1 ? 27 
ATOM   9021  C CD1 . TYR G  1 176 ? 7.575   -10.381  34.932  1.000 69.267  0 505 TYR GGG CD1 1 ? 27 
ATOM   9022  C CD2 . TYR G  1 176 ? 7.446   -12.536  33.911  1.000 71.236  0 505 TYR GGG CD2 1 ? 27 
ATOM   9023  C CE1 . TYR G  1 176 ? 8.152   -9.862   33.781  1.000 71.751  0 505 TYR GGG CE1 1 ? 27 
ATOM   9024  C CE2 . TYR G  1 176 ? 8.014   -12.032  32.751  1.000 73.515  0 505 TYR GGG CE2 1 ? 27 
ATOM   9025  C CZ  . TYR G  1 176 ? 8.368   -10.691  32.691  1.000 76.142  0 505 TYR GGG CZ  1 ? 27 
ATOM   9026  O OH  . TYR G  1 176 ? 8.942   -10.178  31.563  1.000 83.024  0 505 TYR GGG OH  1 ? 27 
ATOM   9027  N N   . GLN G  1 177 ? 7.193   -14.172  39.307  1.000 51.352  0 506 GLN GGG N   1 ? 27 
ATOM   9028  C CA  . GLN G  1 177 ? 6.627   -14.534  40.639  1.000 50.759  0 506 GLN GGG CA  1 ? 27 
ATOM   9029  C C   . GLN G  1 177 ? 7.421   -13.863  41.749  1.000 48.669  0 506 GLN GGG C   1 ? 27 
ATOM   9030  O O   . GLN G  1 177 ? 8.588   -13.583  41.585  1.000 47.270  0 506 GLN GGG O   1 ? 27 
ATOM   9031  C CB  . GLN G  1 177 ? 6.615   -16.047  40.848  1.000 50.033  0 506 GLN GGG CB  1 ? 27 
ATOM   9032  C CG  . GLN G  1 177 ? 5.484   -16.687  40.081  1.000 51.191  0 506 GLN GGG CG  1 ? 27 
ATOM   9033  C CD  . GLN G  1 177 ? 5.544   -18.189  40.146  1.000 51.369  0 506 GLN GGG CD  1 ? 27 
ATOM   9034  O OE1 . GLN G  1 177 ? 6.065   -18.796  41.081  1.000 48.444  0 506 GLN GGG OE1 1 ? 27 
ATOM   9035  N NE2 . GLN G  1 177 ? 4.969   -18.804  39.133  1.000 52.899  0 506 GLN GGG NE2 1 ? 27 
ATOM   9036  N N   . PRO G  1 178 ? 6.822   -13.600  42.919  1.000 47.831  0 507 PRO GGG N   1 ? 27 
ATOM   9037  C CA  . PRO G  1 178 ? 7.548   -12.967  44.014  1.000 46.270  0 507 PRO GGG CA  1 ? 27 
ATOM   9038  C C   . PRO G  1 178 ? 8.527   -13.963  44.633  1.000 44.729  0 507 PRO GGG C   1 ? 27 
ATOM   9039  O O   . PRO G  1 178 ? 8.210   -15.140  44.745  1.000 44.130  0 507 PRO GGG O   1 ? 27 
ATOM   9040  C CB  . PRO G  1 178 ? 6.449   -12.565  45.004  1.000 47.065  0 507 PRO GGG CB  1 ? 27 
ATOM   9041  C CG  . PRO G  1 178 ? 5.370   -13.596  44.761  1.000 48.860  0 507 PRO GGG CG  1 ? 27 
ATOM   9042  C CD  . PRO G  1 178 ? 5.434   -13.900  43.268  1.000 49.163  0 507 PRO GGG CD  1 ? 27 
ATOM   9043  N N   . TYR G  1 179 ? 9.702   -13.464  44.978  1.000 43.370  0 508 TYR GGG N   1 ? 27 
ATOM   9044  C CA  . TYR G  1 179 ? 10.721  -14.191  45.767  1.000 43.840  0 508 TYR GGG CA  1 ? 27 
ATOM   9045  C C   . TYR G  1 179 ? 11.053  -13.336  46.978  1.000 41.868  0 508 TYR GGG C   1 ? 27 
ATOM   9046  O O   . TYR G  1 179 ? 11.269  -12.128  46.821  1.000 39.759  0 508 TYR GGG O   1 ? 27 
ATOM   9047  C CB  . TYR G  1 179 ? 11.953  -14.516  44.921  1.000 44.137  0 508 TYR GGG CB  1 ? 27 
ATOM   9048  C CG  . TYR G  1 179 ? 11.785  -15.721  44.034  1.000 43.436  0 508 TYR GGG CG  1 ? 27 
ATOM   9049  C CD1 . TYR G  1 179 ? 10.895  -15.703  42.962  1.000 44.896  0 508 TYR GGG CD1 1 ? 27 
ATOM   9050  C CD2 . TYR G  1 179 ? 12.504  -16.876  44.281  1.000 42.496  0 508 TYR GGG CD2 1 ? 27 
ATOM   9051  C CE1 . TYR G  1 179 ? 10.719  -16.813  42.145  1.000 44.525  0 508 TYR GGG CE1 1 ? 27 
ATOM   9052  C CE2 . TYR G  1 179 ? 12.358  -17.990  43.470  1.000 45.009  0 508 TYR GGG CE2 1 ? 27 
ATOM   9053  C CZ  . TYR G  1 179 ? 11.459  -17.961  42.401  1.000 46.708  0 508 TYR GGG CZ  1 ? 27 
ATOM   9054  O OH  . TYR G  1 179 ? 11.296  -19.063  41.606  1.000 44.878  0 508 TYR GGG OH  1 ? 27 
ATOM   9055  N N   . ARG G  1 180 ? 11.058  -13.963  48.140  1.000 44.054  0 509 ARG GGG N   1 ? 27 
ATOM   9056  C CA  . ARG G  1 180 ? 11.592  -13.369  49.390  1.000 46.258  0 509 ARG GGG CA  1 ? 27 
ATOM   9057  C C   . ARG G  1 180 ? 13.104  -13.570  49.405  1.000 43.342  0 509 ARG GGG C   1 ? 27 
ATOM   9058  O O   . ARG G  1 180 ? 13.544  -14.649  48.992  1.000 43.439  0 509 ARG GGG O   1 ? 27 
ATOM   9059  C CB  . ARG G  1 180 ? 10.910  -14.012  50.597  1.000 45.794  0 509 ARG GGG CB  1 ? 27 
ATOM   9060  C CG  . ARG G  1 180 ? 9.472   -13.544  50.714  1.000 49.835  0 509 ARG GGG CG  1 ? 27 
ATOM   9061  C CD  . ARG G  1 180 ? 8.762   -14.054  51.938  1.000 48.419  0 509 ARG GGG CD  1 ? 27 
ATOM   9062  N NE  . ARG G  1 180 ? 7.441   -13.434  51.902  1.000 49.108  0 509 ARG GGG NE  1 ? 27 
ATOM   9063  C CZ  . ARG G  1 180 ? 6.634   -13.308  52.950  1.000 47.784  0 509 ARG GGG CZ  1 ? 27 
ATOM   9064  N NH1 . ARG G  1 180 ? 6.997   -13.752  54.133  1.000 48.038  0 509 ARG GGG NH1 1 ? 27 
ATOM   9065  N NH2 . ARG G  1 180 ? 5.468   -12.734  52.811  1.000 46.413  0 509 ARG GGG NH2 1 ? 27 
ATOM   9066  N N   . VAL G  1 181 ? 13.835  -12.553  49.840  1.000 41.620  0 510 VAL GGG N   1 ? 27 
ATOM   9067  C CA  . VAL G  1 181 ? 15.323  -12.520  49.856  1.000 39.053  0 510 VAL GGG CA  1 ? 27 
ATOM   9068  C C   . VAL G  1 181 ? 15.778  -12.134  51.267  1.000 39.019  0 510 VAL GGG C   1 ? 27 
ATOM   9069  O O   . VAL G  1 181 ? 15.166  -11.212  51.882  1.000 39.833  0 510 VAL GGG O   1 ? 27 
ATOM   9070  C CB  . VAL G  1 181 ? 15.858  -11.535  48.807  1.000 37.573  0 510 VAL GGG CB  1 ? 27 
ATOM   9071  C CG1 . VAL G  1 181 ? 17.374  -11.566  48.733  1.000 37.626  0 510 VAL GGG CG1 1 ? 27 
ATOM   9072  C CG2 . VAL G  1 181 ? 15.244  -11.800  47.450  1.000 38.599  0 510 VAL GGG CG2 1 ? 27 
ATOM   9073  N N   . VAL G  1 182 ? 16.775  -12.848  51.777  1.000 38.307  0 511 VAL GGG N   1 ? 27 
ATOM   9074  C CA  . VAL G  1 182 ? 17.524  -12.457  52.992  1.000 37.274  0 511 VAL GGG CA  1 ? 27 
ATOM   9075  C C   . VAL G  1 182 ? 18.992  -12.406  52.610  1.000 37.141  0 511 VAL GGG C   1 ? 27 
ATOM   9076  O O   . VAL G  1 182 ? 19.504  -13.383  52.020  1.000 37.849  0 511 VAL GGG O   1 ? 27 
ATOM   9077  C CB  . VAL G  1 182 ? 17.271  -13.416  54.159  1.000 37.926  0 511 VAL GGG CB  1 ? 27 
ATOM   9078  C CG1 . VAL G  1 182 ? 18.147  -13.042  55.334  1.000 39.133  0 511 VAL GGG CG1 1 ? 27 
ATOM   9079  C CG2 . VAL G  1 182 ? 15.795  -13.460  54.556  1.000 38.939  0 511 VAL GGG CG2 1 ? 27 
ATOM   9080  N N   . VAL G  1 183 ? 19.613  -11.267  52.880  1.000 36.669  0 512 VAL GGG N   1 ? 27 
ATOM   9081  C CA  . VAL G  1 183 ? 21.069  -11.031  52.719  1.000 38.105  0 512 VAL GGG CA  1 ? 27 
ATOM   9082  C C   . VAL G  1 183 ? 21.672  -10.954  54.117  1.000 38.348  0 512 VAL GGG C   1 ? 27 
ATOM   9083  O O   . VAL G  1 183 ? 21.226  -10.105  54.909  1.000 38.759  0 512 VAL GGG O   1 ? 27 
ATOM   9084  C CB  . VAL G  1 183 ? 21.350  -9.743   51.931  1.000 39.550  0 512 VAL GGG CB  1 ? 27 
ATOM   9085  C CG1 . VAL G  1 183 ? 22.858  -9.534   51.719  1.000 39.488  0 512 VAL GGG CG1 1 ? 27 
ATOM   9086  C CG2 . VAL G  1 183 ? 20.590  -9.742   50.614  1.000 41.148  0 512 VAL GGG CG2 1 ? 27 
ATOM   9087  N N   . LEU G  1 184 ? 22.583  -11.873  54.420  1.000 38.094  0 513 LEU GGG N   1 ? 27 
ATOM   9088  C CA  . LEU G  1 184 ? 23.341  -11.871  55.684  1.000 38.209  0 513 LEU GGG CA  1 ? 27 
ATOM   9089  C C   . LEU G  1 184 ? 24.708  -11.249  55.376  1.000 39.970  0 513 LEU GGG C   1 ? 27 
ATOM   9090  O O   . LEU G  1 184 ? 25.445  -11.790  54.541  1.000 39.200  0 513 LEU GGG O   1 ? 27 
ATOM   9091  C CB  . LEU G  1 184 ? 23.450  -13.308  56.188  1.000 37.757  0 513 LEU GGG CB  1 ? 27 
ATOM   9092  C CG  . LEU G  1 184 ? 22.119  -14.017  56.449  1.000 37.645  0 513 LEU GGG CG  1 ? 27 
ATOM   9093  C CD1 . LEU G  1 184 ? 22.351  -15.476  56.783  1.000 38.572  0 513 LEU GGG CD1 1 ? 27 
ATOM   9094  C CD2 . LEU G  1 184 ? 21.339  -13.341  57.572  1.000 38.168  0 513 LEU GGG CD2 1 ? 27 
ATOM   9095  N N   . SER G  1 185 ? 24.963  -10.073  55.945  1.000 41.144  0 514 SER GGG N   1 ? 27 
ATOM   9096  C CA  . SER G  1 185 ? 26.268  -9.356   55.917  1.000 42.826  0 514 SER GGG CA  1 ? 27 
ATOM   9097  C C   . SER G  1 185 ? 27.071  -9.767   57.136  1.000 40.690  0 514 SER GGG C   1 ? 27 
ATOM   9098  O O   . SER G  1 185 ? 26.510  -9.713   58.237  1.000 39.817  0 514 SER GGG O   1 ? 27 
ATOM   9099  C CB  . SER G  1 185 ? 26.077  -7.890   55.929  1.000 42.666  0 514 SER GGG CB  1 ? 27 
ATOM   9100  O OG  . SER G  1 185 ? 25.729  -7.474   54.632  1.000 47.129  0 514 SER GGG OG  1 ? 27 
ATOM   9101  N N   . PHE G  1 186 ? 28.318  -10.168  56.949  1.000 41.135  0 515 PHE GGG N   1 ? 27 
ATOM   9102  C CA  . PHE G  1 186 ? 29.216  -10.577  58.062  1.000 41.948  0 515 PHE GGG CA  1 ? 27 
ATOM   9103  C C   . PHE G  1 186 ? 30.241  -9.476   58.281  1.000 41.860  0 515 PHE GGG C   1 ? 27 
ATOM   9104  O O   . PHE G  1 186 ? 30.942  -9.159   57.333  1.000 42.214  0 515 PHE GGG O   1 ? 27 
ATOM   9105  C CB  . PHE G  1 186 ? 29.870  -11.911  57.730  1.000 41.760  0 515 PHE GGG CB  1 ? 27 
ATOM   9106  C CG  . PHE G  1 186 ? 28.916  -13.046  57.484  1.000 40.139  0 515 PHE GGG CG  1 ? 27 
ATOM   9107  C CD1 . PHE G  1 186 ? 27.687  -13.109  58.117  1.000 41.282  0 515 PHE GGG CD1 1 ? 27 
ATOM   9108  C CD2 . PHE G  1 186 ? 29.286  -14.090  56.656  1.000 40.469  0 515 PHE GGG CD2 1 ? 27 
ATOM   9109  C CE1 . PHE G  1 186 ? 26.836  -14.182  57.909  1.000 40.663  0 515 PHE GGG CE1 1 ? 27 
ATOM   9110  C CE2 . PHE G  1 186 ? 28.446  -15.176  56.468  1.000 39.724  0 515 PHE GGG CE2 1 ? 27 
ATOM   9111  C CZ  . PHE G  1 186 ? 27.235  -15.233  57.119  1.000 40.406  0 515 PHE GGG CZ  1 ? 27 
ATOM   9112  N N   . GLU G  1 187 ? 30.223  -8.849   59.446  1.000 44.928  0 516 GLU GGG N   1 ? 27 
ATOM   9113  C CA  . GLU G  1 187 ? 31.018  -7.635   59.755  1.000 47.409  0 516 GLU GGG CA  1 ? 27 
ATOM   9114  C C   . GLU G  1 187 ? 32.176  -8.051   60.664  1.000 47.035  0 516 GLU GGG C   1 ? 27 
ATOM   9115  O O   . GLU G  1 187 ? 31.949  -8.803   61.620  1.000 44.236  0 516 GLU GGG O   1 ? 27 
ATOM   9116  C CB  . GLU G  1 187 ? 30.117  -6.608   60.435  1.000 49.876  0 516 GLU GGG CB  1 ? 27 
ATOM   9117  C CG  . GLU G  1 187 ? 30.668  -5.212   60.423  1.000 55.993  0 516 GLU GGG CG  1 ? 27 
ATOM   9118  C CD  . GLU G  1 187 ? 29.883  -4.184   61.238  1.000 60.132  0 516 GLU GGG CD  1 ? 27 
ATOM   9119  O OE1 . GLU G  1 187 ? 29.395  -4.511   62.333  1.000 59.498  0 516 GLU GGG OE1 1 ? 27 
ATOM   9120  O OE2 . GLU G  1 187 ? 29.778  -3.030   60.776  1.000 67.059  0 516 GLU GGG OE2 1 ? 27 
ATOM   9121  N N   . LEU G  1 188 ? 33.375  -7.571   60.358  1.000 48.977  0 517 LEU GGG N   1 ? 27 
ATOM   9122  C CA  . LEU G  1 188 ? 34.584  -7.789   61.185  1.000 51.198  0 517 LEU GGG CA  1 ? 27 
ATOM   9123  C C   . LEU G  1 188 ? 35.190  -6.446   61.561  1.000 52.156  0 517 LEU GGG C   1 ? 27 
ATOM   9124  O O   . LEU G  1 188 ? 35.808  -5.862   60.688  1.000 54.316  0 517 LEU GGG O   1 ? 27 
ATOM   9125  C CB  . LEU G  1 188 ? 35.557  -8.633   60.362  1.000 53.788  0 517 LEU GGG CB  1 ? 27 
ATOM   9126  C CG  . LEU G  1 188 ? 35.284  -10.129  60.388  1.000 55.129  0 517 LEU GGG CG  1 ? 27 
ATOM   9127  C CD1 . LEU G  1 188 ? 36.171  -10.872  59.395  1.000 56.929  0 517 LEU GGG CD1 1 ? 27 
ATOM   9128  C CD2 . LEU G  1 188 ? 35.481  -10.702  61.784  1.000 56.704  0 517 LEU GGG CD2 1 ? 27 
ATOM   9129  N N   . LEU G  1 189 ? 34.859  -5.909   62.732  1.000 52.277  0 518 LEU GGG N   1 ? 27 
ATOM   9130  C CA  . LEU G  1 189 ? 35.499  -4.660   63.251  1.000 53.478  0 518 LEU GGG CA  1 ? 27 
ATOM   9131  C C   . LEU G  1 189 ? 36.612  -5.074   64.214  1.000 53.776  0 518 LEU GGG C   1 ? 27 
ATOM   9132  O O   . LEU G  1 189 ? 36.716  -6.250   64.534  1.000 54.489  0 518 LEU GGG O   1 ? 27 
ATOM   9133  C CB  . LEU G  1 189 ? 34.463  -3.776   63.951  1.000 55.009  0 518 LEU GGG CB  1 ? 27 
ATOM   9134  C CG  . LEU G  1 189 ? 33.155  -3.585   63.173  1.000 56.039  0 518 LEU GGG CG  1 ? 27 
ATOM   9135  C CD1 . LEU G  1 189 ? 32.084  -2.864   63.976  1.000 56.011  0 518 LEU GGG CD1 1 ? 27 
ATOM   9136  C CD2 . LEU G  1 189 ? 33.423  -2.893   61.851  1.000 57.056  0 518 LEU GGG CD2 1 ? 27 
ATOM   9137  N N   . HIS G  1 190 ? 37.410  -4.125   64.667  1.000 55.848  0 519 HIS GGG N   1 ? 27 
ATOM   9138  C CA  . HIS G  1 190 ? 38.378  -4.289   65.781  1.000 56.921  0 519 HIS GGG CA  1 ? 27 
ATOM   9139  C C   . HIS G  1 190 ? 37.602  -4.158   67.091  1.000 58.062  0 519 HIS GGG C   1 ? 27 
ATOM   9140  O O   . HIS G  1 190 ? 37.647  -3.080   67.708  1.000 60.600  0 519 HIS GGG O   1 ? 27 
ATOM   9141  C CB  . HIS G  1 190 ? 39.502  -3.283   65.615  1.000 56.800  0 519 HIS GGG CB  1 ? 27 
ATOM   9142  C CG  . HIS G  1 190 ? 40.521  -3.424   66.675  1.000 59.172  0 519 HIS GGG CG  1 ? 27 
ATOM   9143  N ND1 . HIS G  1 190 ? 41.153  -4.618   66.927  1.000 60.212  0 519 HIS GGG ND1 1 ? 27 
ATOM   9144  C CD2 . HIS G  1 190 ? 41.005  -2.531   67.563  1.000 61.133  0 519 HIS GGG CD2 1 ? 27 
ATOM   9145  C CE1 . HIS G  1 190 ? 42.027  -4.448   67.914  1.000 61.955  0 519 HIS GGG CE1 1 ? 27 
ATOM   9146  N NE2 . HIS G  1 190 ? 41.951  -3.172   68.321  1.000 62.940  0 519 HIS GGG NE2 1 ? 27 
ATOM   9147  N N   . ALA G  1 191 ? 36.867  -5.220   67.427  1.000 58.100  0 520 ALA GGG N   1 ? 27 
ATOM   9148  C CA  . ALA G  1 191 ? 35.986  -5.357   68.614  1.000 58.827  0 520 ALA GGG CA  1 ? 27 
ATOM   9149  C C   . ALA G  1 191 ? 35.888  -6.836   68.975  1.000 57.981  0 520 ALA GGG C   1 ? 27 
ATOM   9150  O O   . ALA G  1 191 ? 36.213  -7.687   68.157  1.000 58.760  0 520 ALA GGG O   1 ? 27 
ATOM   9151  C CB  . ALA G  1 191 ? 34.625  -4.772   68.293  1.000 57.187  0 520 ALA GGG CB  1 ? 27 
ATOM   9152  N N   . PRO G  1 192 ? 35.429  -7.223   70.178  1.000 59.373  0 521 PRO GGG N   1 ? 27 
ATOM   9153  C CA  . PRO G  1 192 ? 35.105  -8.630   70.431  1.000 58.369  0 521 PRO GGG CA  1 ? 27 
ATOM   9154  C C   . PRO G  1 192 ? 34.075  -9.169   69.435  1.000 54.955  0 521 PRO GGG C   1 ? 27 
ATOM   9155  O O   . PRO G  1 192 ? 33.167  -8.483   69.078  1.000 55.493  0 521 PRO GGG O   1 ? 27 
ATOM   9156  C CB  . PRO G  1 192 ? 34.574  -8.628   71.873  1.000 60.207  0 521 PRO GGG CB  1 ? 27 
ATOM   9157  C CG  . PRO G  1 192 ? 35.221  -7.394   72.504  1.000 61.724  0 521 PRO GGG CG  1 ? 27 
ATOM   9158  C CD  . PRO G  1 192 ? 35.274  -6.375   71.373  1.000 61.884  0 521 PRO GGG CD  1 ? 27 
ATOM   9159  N N   . ALA G  1 193 ? 34.289  -10.387  68.944  1.000 53.499  0 522 ALA GGG N   1 ? 27 
ATOM   9160  C CA  . ALA G  1 193 ? 33.324  -11.117  68.090  1.000 50.203  0 522 ALA GGG CA  1 ? 27 
ATOM   9161  C C   . ALA G  1 193 ? 32.132  -11.465  68.977  1.000 49.679  0 522 ALA GGG C   1 ? 27 
ATOM   9162  O O   . ALA G  1 193 ? 32.351  -11.877  70.080  1.000 55.477  0 522 ALA GGG O   1 ? 27 
ATOM   9163  C CB  . ALA G  1 193 ? 33.979  -12.343  67.528  1.000 49.660  0 522 ALA GGG CB  1 ? 27 
ATOM   9164  N N   . THR G  1 194 ? 30.909  -11.219  68.544  1.000 48.259  0 523 THR GGG N   1 ? 27 
ATOM   9165  C CA  . THR G  1 194 ? 29.704  -11.406  69.389  1.000 48.589  0 523 THR GGG CA  1 ? 27 
ATOM   9166  C C   . THR G  1 194 ? 28.776  -12.420  68.722  1.000 45.628  0 523 THR GGG C   1 ? 27 
ATOM   9167  O O   . THR G  1 194 ? 27.886  -12.921  69.387  1.000 46.048  0 523 THR GGG O   1 ? 27 
ATOM   9168  C CB  . THR G  1 194 ? 29.013  -10.061  69.691  1.000 49.854  0 523 THR GGG CB  1 ? 27 
ATOM   9169  O OG1 . THR G  1 194 ? 28.324  -9.612   68.521  1.000 51.354  0 523 THR GGG OG1 1 ? 27 
ATOM   9170  C CG2 . THR G  1 194 ? 29.968  -8.990   70.176  1.000 49.899  0 523 THR GGG CG2 1 ? 27 
ATOM   9171  N N   . VAL G  1 195 ? 29.010  -12.751  67.462  1.000 44.998  0 524 VAL GGG N   1 ? 27 
ATOM   9172  C CA  . VAL G  1 195 ? 28.225  -13.797  66.749  1.000 45.697  0 524 VAL GGG CA  1 ? 27 
ATOM   9173  C C   . VAL G  1 195 ? 29.179  -14.918  66.340  1.000 47.421  0 524 VAL GGG C   1 ? 27 
ATOM   9174  O O   . VAL G  1 195 ? 30.056  -14.666  65.537  1.000 48.098  0 524 VAL GGG O   1 ? 27 
ATOM   9175  C CB  . VAL G  1 195 ? 27.513  -13.218  65.537  1.000 45.711  0 524 VAL GGG CB  1 ? 27 
ATOM   9176  C CG1 . VAL G  1 195 ? 26.749  -14.312  64.848  1.000 45.520  0 524 VAL GGG CG1 1 ? 27 
ATOM   9177  C CG2 . VAL G  1 195 ? 26.630  -12.038  65.882  1.000 46.496  0 524 VAL GGG CG2 1 ? 27 
ATOM   9178  N N   . CYS G  1 196 ? 29.014  -16.080  66.952  1.000 50.639  0 525 CYS GGG N   1 ? 27 
ATOM   9179  C CA  . CYS G  1 196 ? 29.846  -17.295  66.744  1.000 53.387  0 525 CYS GGG CA  1 ? 27 
ATOM   9180  C C   . CYS G  1 196 ? 28.909  -18.475  66.517  1.000 54.265  0 525 CYS GGG C   1 ? 27 
ATOM   9181  O O   . CYS G  1 196 ? 27.754  -18.441  67.047  1.000 52.737  0 525 CYS GGG O   1 ? 27 
ATOM   9182  C CB  . CYS G  1 196 ? 30.777  -17.590  67.911  1.000 55.906  0 525 CYS GGG CB  1 ? 27 
ATOM   9183  S SG  . CYS G  1 196 ? 32.099  -16.353  68.069  1.000 59.933  0 525 CYS GGG SG  1 ? 27 
ATOM   9184  N N   . GLY G  1 197 ? 29.381  -19.474  65.772  1.000 58.056  0 526 GLY GGG N   1 ? 27 
ATOM   9185  C CA  . GLY G  1 197 ? 28.701  -20.768  65.613  1.000 59.271  0 526 GLY GGG CA  1 ? 27 
ATOM   9186  C C   . GLY G  1 197 ? 28.707  -21.556  66.917  1.000 63.749  0 526 GLY GGG C   1 ? 27 
ATOM   9187  O O   . GLY G  1 197 ? 29.408  -21.181  67.860  1.000 65.125  0 526 GLY GGG O   1 ? 27 
ATOM   9188  N N   . PRO G  1 198 ? 27.972  -22.684  66.983  1.000 70.190  0 527 PRO GGG N   1 ? 27 
ATOM   9189  C CA  . PRO G  1 198 ? 27.943  -23.542  68.180  1.000 76.222  0 527 PRO GGG CA  1 ? 27 
ATOM   9190  C C   . PRO G  1 198 ? 29.316  -23.947  68.737  1.000 84.980  0 527 PRO GGG C   1 ? 27 
ATOM   9191  O O   . PRO G  1 198 ? 29.399  -24.290  69.899  1.000 83.701  0 527 PRO GGG O   1 ? 27 
ATOM   9192  C CB  . PRO G  1 198 ? 27.182  -24.784  67.695  1.000 74.863  0 527 PRO GGG CB  1 ? 27 
ATOM   9193  C CG  . PRO G  1 198 ? 26.340  -24.285  66.534  1.000 71.759  0 527 PRO GGG CG  1 ? 27 
ATOM   9194  C CD  . PRO G  1 198 ? 27.205  -23.238  65.851  1.000 68.974  0 527 PRO GGG CD  1 ? 27 
ATOM   9195  N N   . LYS G  1 199 ? 30.345  -23.770  67.885  1.000 83.874  0 528 LYS GGG N   1 ? ?  
ATOM   9196  C CA  . LYS G  1 199 ? 31.804  -23.626  68.196  1.000 95.316  0 528 LYS GGG CA  1 ? ?  
ATOM   9197  C C   . LYS G  1 199 ? 32.226  -22.152  68.010  1.000 89.127  0 528 LYS GGG C   1 ? ?  
ATOM   9198  O O   . LYS G  1 199 ? 33.300  -21.736  67.545  1.000 73.484  0 528 LYS GGG O   1 ? ?  
ATOM   9199  C CB  . LYS G  1 199 ? 32.651  -24.579  67.333  1.000 96.612  0 528 LYS GGG CB  1 ? ?  
ATOM   9200  C CG  . LYS G  1 199 ? 32.169  -24.835  65.905  1.000 93.548  0 528 LYS GGG CG  1 ? ?  
ATOM   9201  C CD  . LYS G  1 199 ? 32.742  -26.109  65.285  1.000 95.322  0 528 LYS GGG CD  1 ? ?  
ATOM   9202  C CE  . LYS G  1 199 ? 31.877  -27.344  65.454  1.000 94.650  0 528 LYS GGG CE  1 ? ?  
ATOM   9203  N NZ  . LYS G  1 199 ? 32.066  -27.976  66.783  1.000 96.688  0 528 LYS GGG NZ  1 ? ?  
ATOM   9204  N N   . GLN H  2 1   ? 30.644  -10.257  32.085  1.000 65.648  0 1   GLN HHH N   1 ? 28 
ATOM   9205  C CA  . GLN H  2 1   ? 30.512  -11.323  31.031  1.000 63.115  0 1   GLN HHH CA  1 ? 28 
ATOM   9206  C C   . GLN H  2 1   ? 31.834  -12.080  30.944  1.000 57.481  0 1   GLN HHH C   1 ? 28 
ATOM   9207  O O   . GLN H  2 1   ? 32.857  -11.480  30.585  1.000 55.580  0 1   GLN HHH O   1 ? 28 
ATOM   9208  C CB  . GLN H  2 1   ? 30.123  -10.676  29.710  1.000 66.330  0 1   GLN HHH CB  1 ? 28 
ATOM   9209  C CG  . GLN H  2 1   ? 30.139  -9.165   29.873  1.000 72.463  0 1   GLN HHH CG  1 ? 28 
ATOM   9210  C CD  . GLN H  2 1   ? 29.701  -8.401   28.650  1.000 77.720  0 1   GLN HHH CD  1 ? 28 
ATOM   9211  O OE1 . GLN H  2 1   ? 30.259  -8.588   27.555  1.000 74.242  0 1   GLN HHH OE1 1 ? 28 
ATOM   9212  N NE2 . GLN H  2 1   ? 28.722  -7.519   28.856  1.000 83.401  0 1   GLN HHH NE2 1 ? 28 
ATOM   9213  N N   . VAL H  2 2   ? 31.820  -13.338  31.356  1.000 55.337  0 2   VAL HHH N   1 ? 28 
ATOM   9214  C CA  . VAL H  2 2   ? 33.000  -14.247  31.321  1.000 51.585  0 2   VAL HHH CA  1 ? 28 
ATOM   9215  C C   . VAL H  2 2   ? 32.748  -15.309  30.246  1.000 48.687  0 2   VAL HHH C   1 ? 28 
ATOM   9216  O O   . VAL H  2 2   ? 31.695  -15.954  30.281  1.000 49.410  0 2   VAL HHH O   1 ? 28 
ATOM   9217  C CB  . VAL H  2 2   ? 33.233  -14.920  32.685  1.000 52.404  0 2   VAL HHH CB  1 ? 28 
ATOM   9218  C CG1 . VAL H  2 2   ? 34.396  -15.889  32.622  1.000 49.844  0 2   VAL HHH CG1 1 ? 28 
ATOM   9219  C CG2 . VAL H  2 2   ? 33.427  -13.899  33.795  1.000 55.408  0 2   VAL HHH CG2 1 ? 28 
ATOM   9220  N N   . GLN H  2 3   ? 33.720  -15.534  29.373  1.000 46.040  0 3   GLN HHH N   1 ? 28 
ATOM   9221  C CA  . GLN H  2 3   ? 33.667  -16.686  28.452  1.000 44.864  0 3   GLN HHH CA  1 ? 28 
ATOM   9222  C C   . GLN H  2 3   ? 34.571  -17.791  29.001  1.000 45.913  0 3   GLN HHH C   1 ? 28 
ATOM   9223  O O   . GLN H  2 3   ? 35.564  -17.507  29.674  1.000 45.800  0 3   GLN HHH O   1 ? 28 
ATOM   9224  C CB  . GLN H  2 3   ? 33.986  -16.245  27.030  1.000 42.194  0 3   GLN HHH CB  1 ? 28 
ATOM   9225  C CG  . GLN H  2 3   ? 32.833  -15.479  26.410  1.000 42.652  0 3   GLN HHH CG  1 ? 28 
ATOM   9226  C CD  . GLN H  2 3   ? 33.111  -15.139  24.974  1.000 41.825  0 3   GLN HHH CD  1 ? 28 
ATOM   9227  O OE1 . GLN H  2 3   ? 33.250  -16.052  24.154  1.000 40.365  0 3   GLN HHH OE1 1 ? 28 
ATOM   9228  N NE2 . GLN H  2 3   ? 33.190  -13.840  24.672  1.000 41.551  0 3   GLN HHH NE2 1 ? 28 
ATOM   9229  N N   . LEU H  2 4   ? 34.162  -19.022  28.733  1.000 47.820  0 4   LEU HHH N   1 ? 28 
ATOM   9230  C CA  . LEU H  2 4   ? 34.781  -20.269  29.231  1.000 46.498  0 4   LEU HHH CA  1 ? 28 
ATOM   9231  C C   . LEU H  2 4   ? 34.924  -21.225  28.041  1.000 46.027  0 4   LEU HHH C   1 ? 28 
ATOM   9232  O O   . LEU H  2 4   ? 33.940  -21.425  27.303  1.000 47.695  0 4   LEU HHH O   1 ? 28 
ATOM   9233  C CB  . LEU H  2 4   ? 33.862  -20.869  30.300  1.000 46.610  0 4   LEU HHH CB  1 ? 28 
ATOM   9234  C CG  . LEU H  2 4   ? 33.515  -20.001  31.510  1.000 47.530  0 4   LEU HHH CG  1 ? 28 
ATOM   9235  C CD1 . LEU H  2 4   ? 32.419  -20.695  32.345  1.000 48.256  0 4   LEU HHH CD1 1 ? 28 
ATOM   9236  C CD2 . LEU H  2 4   ? 34.751  -19.738  32.353  1.000 46.685  0 4   LEU HHH CD2 1 ? 28 
ATOM   9237  N N   . VAL H  2 5   ? 36.108  -21.780  27.848  1.000 44.192  0 5   VAL HHH N   1 ? 28 
ATOM   9238  C CA  . VAL H  2 5   ? 36.376  -22.757  26.764  1.000 44.785  0 5   VAL HHH CA  1 ? 28 
ATOM   9239  C C   . VAL H  2 5   ? 37.063  -23.986  27.379  1.000 45.875  0 5   VAL HHH C   1 ? 28 
ATOM   9240  O O   . VAL H  2 5   ? 38.195  -23.859  27.927  1.000 45.940  0 5   VAL HHH O   1 ? 28 
ATOM   9241  C CB  . VAL H  2 5   ? 37.201  -22.124  25.637  1.000 44.414  0 5   VAL HHH CB  1 ? 28 
ATOM   9242  C CG1 . VAL H  2 5   ? 37.626  -23.171  24.624  1.000 46.554  0 5   VAL HHH CG1 1 ? 28 
ATOM   9243  C CG2 . VAL H  2 5   ? 36.436  -21.001  24.963  1.000 44.483  0 5   VAL HHH CG2 1 ? 28 
ATOM   9244  N N   . GLU H  2 6   ? 36.391  -25.130  27.273  1.000 44.980  0 6   GLU HHH N   1 ? 28 
ATOM   9245  C CA  . GLU H  2 6   ? 36.903  -26.468  27.636  1.000 45.133  0 6   GLU HHH CA  1 ? 28 
ATOM   9246  C C   . GLU H  2 6   ? 37.842  -26.982  26.530  1.000 46.372  0 6   GLU HHH C   1 ? 28 
ATOM   9247  O O   . GLU H  2 6   ? 37.608  -26.662  25.383  1.000 46.071  0 6   GLU HHH O   1 ? 28 
ATOM   9248  C CB  . GLU H  2 6   ? 35.744  -27.446  27.800  1.000 45.355  0 6   GLU HHH CB  1 ? 28 
ATOM   9249  C CG  . GLU H  2 6   ? 34.634  -26.980  28.707  1.000 44.210  0 6   GLU HHH CG  1 ? 28 
ATOM   9250  C CD  . GLU H  2 6   ? 33.495  -26.198  28.086  1.000 44.719  0 6   GLU HHH CD  1 ? 28 
ATOM   9251  O OE1 . GLU H  2 6   ? 33.668  -25.692  26.988  1.000 44.383  0 6   GLU HHH OE1 1 ? 28 
ATOM   9252  O OE2 . GLU H  2 6   ? 32.426  -26.089  28.740  1.000 44.649  0 6   GLU HHH OE2 1 ? 28 
ATOM   9253  N N   . SER H  2 7   ? 38.858  -27.764  26.902  1.000 47.880  0 7   SER HHH N   1 ? 28 
ATOM   9254  C CA  . SER H  2 7   ? 39.739  -28.555  26.006  1.000 50.312  0 7   SER HHH CA  1 ? 28 
ATOM   9255  C C   . SER H  2 7   ? 40.191  -29.840  26.714  1.000 51.934  0 7   SER HHH C   1 ? 28 
ATOM   9256  O O   . SER H  2 7   ? 39.909  -29.975  27.912  1.000 49.197  0 7   SER HHH O   1 ? 28 
ATOM   9257  C CB  . SER H  2 7   ? 40.897  -27.740  25.561  1.000 51.166  0 7   SER HHH CB  1 ? 28 
ATOM   9258  O OG  . SER H  2 7   ? 41.647  -27.342  26.683  1.000 53.089  0 7   SER HHH OG  1 ? 28 
ATOM   9259  N N   . GLY H  2 8   ? 40.825  -30.774  25.983  1.000 55.076  0 8   GLY HHH N   1 ? 28 
ATOM   9260  C CA  . GLY H  2 8   ? 41.377  -32.025  26.535  1.000 56.561  0 8   GLY HHH CA  1 ? 28 
ATOM   9261  C C   . GLY H  2 8   ? 40.408  -33.193  26.463  1.000 58.954  0 8   GLY HHH C   1 ? 28 
ATOM   9262  O O   . GLY H  2 8   ? 40.759  -34.290  26.991  1.000 63.061  0 8   GLY HHH O   1 ? 28 
ATOM   9263  N N   . GLY H  2 9   ? 39.240  -33.011  25.845  1.000 60.157  0 9   GLY HHH N   1 ? 28 
ATOM   9264  C CA  . GLY H  2 9   ? 38.235  -34.088  25.724  1.000 63.941  0 9   GLY HHH CA  1 ? 28 
ATOM   9265  C C   . GLY H  2 9   ? 38.609  -35.096  24.646  1.000 69.302  0 9   GLY HHH C   1 ? 28 
ATOM   9266  O O   . GLY H  2 9   ? 39.690  -34.929  24.061  1.000 72.177  0 9   GLY HHH O   1 ? 28 
ATOM   9267  N N   . GLY H  2 10  ? 37.745  -36.072  24.371  1.000 70.714  0 10  GLY HHH N   1 ? 28 
ATOM   9268  C CA  . GLY H  2 10  ? 37.918  -37.024  23.261  1.000 73.878  0 10  GLY HHH CA  1 ? 28 
ATOM   9269  C C   . GLY H  2 10  ? 37.740  -38.466  23.715  1.000 76.348  0 10  GLY HHH C   1 ? 28 
ATOM   9270  O O   . GLY H  2 10  ? 37.099  -38.699  24.750  1.000 73.706  0 10  GLY HHH O   1 ? 28 
ATOM   9271  N N   . LEU H  2 11  ? 38.256  -39.403  22.919  1.000 81.146  0 11  LEU HHH N   1 ? 28 
ATOM   9272  C CA  . LEU H  2 11  ? 38.063  -40.865  23.065  1.000 82.472  0 11  LEU HHH CA  1 ? 28 
ATOM   9273  C C   . LEU H  2 11  ? 39.103  -41.392  24.053  1.000 82.484  0 11  LEU HHH C   1 ? 28 
ATOM   9274  O O   . LEU H  2 11  ? 40.242  -40.941  23.996  1.000 84.360  0 11  LEU HHH O   1 ? 28 
ATOM   9275  C CB  . LEU H  2 11  ? 38.230  -41.489  21.674  1.000 87.191  0 11  LEU HHH CB  1 ? 28 
ATOM   9276  C CG  . LEU H  2 11  ? 38.023  -43.000  21.553  1.000 90.983  0 11  LEU HHH CG  1 ? 28 
ATOM   9277  C CD1 . LEU H  2 11  ? 39.315  -43.797  21.751  1.000 94.660  0 11  LEU HHH CD1 1 ? 28 
ATOM   9278  C CD2 . LEU H  2 11  ? 36.902  -43.522  22.448  1.000 88.674  0 11  LEU HHH CD2 1 ? 28 
ATOM   9279  N N   . VAL H  2 12  ? 38.731  -42.316  24.932  1.000 82.376  0 12  VAL HHH N   1 ? 28 
ATOM   9280  C CA  . VAL H  2 12  ? 39.697  -43.023  25.825  1.000 82.836  0 12  VAL HHH CA  1 ? 28 
ATOM   9281  C C   . VAL H  2 12  ? 39.125  -44.403  26.160  1.000 81.216  0 12  VAL HHH C   1 ? 28 
ATOM   9282  O O   . VAL H  2 12  ? 37.882  -44.520  26.192  1.000 79.436  0 12  VAL HHH O   1 ? 28 
ATOM   9283  C CB  . VAL H  2 12  ? 39.982  -42.163  27.074  1.000 80.883  0 12  VAL HHH CB  1 ? 28 
ATOM   9284  C CG1 . VAL H  2 12  ? 38.788  -42.096  28.006  1.000 77.913  0 12  VAL HHH CG1 1 ? 28 
ATOM   9285  C CG2 . VAL H  2 12  ? 41.237  -42.615  27.782  1.000 82.990  0 12  VAL HHH CG2 1 ? 28 
ATOM   9286  N N   . GLN H  2 13  ? 39.979  -45.408  26.365  1.000 83.870  0 13  GLN HHH N   1 ? 28 
ATOM   9287  C CA  . GLN H  2 13  ? 39.513  -46.775  26.749  1.000 85.759  0 13  GLN HHH CA  1 ? 28 
ATOM   9288  C C   . GLN H  2 13  ? 39.235  -46.789  28.257  1.000 82.824  0 13  GLN HHH C   1 ? 28 
ATOM   9289  O O   . GLN H  2 13  ? 39.918  -46.047  28.996  1.000 79.779  0 13  GLN HHH O   1 ? 28 
ATOM   9290  C CB  . GLN H  2 13  ? 40.422  -47.920  26.285  1.000 91.077  0 13  GLN HHH CB  1 ? 28 
ATOM   9291  C CG  . GLN H  2 13  ? 39.717  -49.272  26.419  1.000 94.864  0 13  GLN HHH CG  1 ? 28 
ATOM   9292  C CD  . GLN H  2 13  ? 39.748  -50.182  25.211  1.000 102.611 0 13  GLN HHH CD  1 ? 28 
ATOM   9293  O OE1 . GLN H  2 13  ? 40.771  -50.786  24.922  1.000 108.544 0 13  GLN HHH OE1 1 ? 28 
ATOM   9294  N NE2 . GLN H  2 13  ? 38.617  -50.323  24.528  1.000 102.956 0 13  GLN HHH NE2 1 ? 28 
ATOM   9295  N N   . ALA H  2 14  ? 38.220  -47.560  28.669  1.000 81.076  0 14  ALA HHH N   1 ? 28 
ATOM   9296  C CA  . ALA H  2 14  ? 37.869  -47.854  30.076  1.000 77.026  0 14  ALA HHH CA  1 ? 28 
ATOM   9297  C C   . ALA H  2 14  ? 39.150  -48.145  30.871  1.000 77.158  0 14  ALA HHH C   1 ? 28 
ATOM   9298  O O   . ALA H  2 14  ? 40.049  -48.790  30.326  1.000 79.101  0 14  ALA HHH O   1 ? 28 
ATOM   9299  C CB  . ALA H  2 14  ? 36.906  -49.013  30.143  1.000 77.291  0 14  ALA HHH CB  1 ? 28 
ATOM   9300  N N   . GLY H  2 15  ? 39.233  -47.634  32.099  1.000 74.231  0 15  GLY HHH N   1 ? 28 
ATOM   9301  C CA  . GLY H  2 15  ? 40.444  -47.694  32.935  1.000 74.217  0 15  GLY HHH CA  1 ? 28 
ATOM   9302  C C   . GLY H  2 15  ? 41.463  -46.628  32.567  1.000 75.275  0 15  GLY HHH C   1 ? 28 
ATOM   9303  O O   . GLY H  2 15  ? 42.409  -46.482  33.334  1.000 77.377  0 15  GLY HHH O   1 ? 28 
ATOM   9304  N N   . GLY H  2 16  ? 41.284  -45.893  31.461  1.000 75.539  0 16  GLY HHH N   1 ? 28 
ATOM   9305  C CA  . GLY H  2 16  ? 42.231  -44.843  31.024  1.000 75.900  0 16  GLY HHH CA  1 ? 28 
ATOM   9306  C C   . GLY H  2 16  ? 42.048  -43.530  31.781  1.000 73.359  0 16  GLY HHH C   1 ? 28 
ATOM   9307  O O   . GLY H  2 16  ? 41.188  -43.488  32.684  1.000 68.589  0 16  GLY HHH O   1 ? 28 
ATOM   9308  N N   . SER H  2 17  ? 42.821  -42.499  31.404  1.000 75.027  0 17  SER HHH N   1 ? 28 
ATOM   9309  C CA  . SER H  2 17  ? 42.825  -41.134  32.003  1.000 73.285  0 17  SER HHH CA  1 ? 28 
ATOM   9310  C C   . SER H  2 17  ? 42.649  -40.043  30.947  1.000 72.047  0 17  SER HHH C   1 ? 28 
ATOM   9311  O O   . SER H  2 17  ? 42.996  -40.276  29.769  1.000 74.161  0 17  SER HHH O   1 ? 28 
ATOM   9312  C CB  . SER H  2 17  ? 44.081  -40.868  32.750  1.000 75.785  0 17  SER HHH CB  1 ? 28 
ATOM   9313  O OG  . SER H  2 17  ? 44.089  -41.621  33.935  1.000 80.271  0 17  SER HHH OG  1 ? 28 
ATOM   9314  N N   . LEU H  2 18  ? 42.143  -38.896  31.396  1.000 69.440  0 18  LEU HHH N   1 ? 28 
ATOM   9315  C CA  . LEU H  2 18  ? 42.010  -37.635  30.634  1.000 67.427  0 18  LEU HHH CA  1 ? 28 
ATOM   9316  C C   . LEU H  2 18  ? 42.115  -36.479  31.620  1.000 65.596  0 18  LEU HHH C   1 ? 28 
ATOM   9317  O O   . LEU H  2 18  ? 41.524  -36.585  32.704  1.000 66.114  0 18  LEU HHH O   1 ? 28 
ATOM   9318  C CB  . LEU H  2 18  ? 40.624  -37.580  29.990  1.000 67.458  0 18  LEU HHH CB  1 ? 28 
ATOM   9319  C CG  . LEU H  2 18  ? 40.497  -38.084  28.563  1.000 70.765  0 18  LEU HHH CG  1 ? 28 
ATOM   9320  C CD1 . LEU H  2 18  ? 39.144  -37.666  28.026  1.000 70.183  0 18  LEU HHH CD1 1 ? 28 
ATOM   9321  C CD2 . LEU H  2 18  ? 41.621  -37.563  27.679  1.000 72.876  0 18  LEU HHH CD2 1 ? 28 
ATOM   9322  N N   . ARG H  2 19  ? 42.792  -35.409  31.230  1.000 64.820  0 19  ARG HHH N   1 ? 28 
ATOM   9323  C CA  . ARG H  2 19  ? 42.734  -34.117  31.948  1.000 61.834  0 19  ARG HHH CA  1 ? 28 
ATOM   9324  C C   . ARG H  2 19  ? 41.991  -33.103  31.069  1.000 59.320  0 19  ARG HHH C   1 ? 28 
ATOM   9325  O O   . ARG H  2 19  ? 42.557  -32.628  30.061  1.000 59.297  0 19  ARG HHH O   1 ? 28 
ATOM   9326  C CB  . ARG H  2 19  ? 44.123  -33.635  32.353  1.000 64.455  0 19  ARG HHH CB  1 ? 28 
ATOM   9327  C CG  . ARG H  2 19  ? 44.054  -32.637  33.493  1.000 64.674  0 19  ARG HHH CG  1 ? 28 
ATOM   9328  C CD  . ARG H  2 19  ? 45.380  -32.074  33.912  1.000 68.773  0 19  ARG HHH CD  1 ? 28 
ATOM   9329  N NE  . ARG H  2 19  ? 45.929  -31.327  32.799  1.000 70.529  0 19  ARG HHH NE  1 ? 28 
ATOM   9330  C CZ  . ARG H  2 19  ? 46.864  -30.392  32.890  1.000 73.675  0 19  ARG HHH CZ  1 ? 28 
ATOM   9331  N NH1 . ARG H  2 19  ? 47.362  -30.055  34.075  1.000 77.721  0 19  ARG HHH NH1 1 ? 28 
ATOM   9332  N NH2 . ARG H  2 19  ? 47.289  -29.795  31.787  1.000 71.753  0 19  ARG HHH NH2 1 ? 28 
ATOM   9333  N N   . LEU H  2 20  ? 40.748  -32.810  31.441  1.000 55.815  0 20  LEU HHH N   1 ? 28 
ATOM   9334  C CA  . LEU H  2 20  ? 39.990  -31.662  30.903  1.000 54.247  0 20  LEU HHH CA  1 ? 28 
ATOM   9335  C C   . LEU H  2 20  ? 40.593  -30.387  31.491  1.000 53.362  0 20  LEU HHH C   1 ? 28 
ATOM   9336  O O   . LEU H  2 20  ? 40.990  -30.381  32.676  1.000 53.730  0 20  LEU HHH O   1 ? 28 
ATOM   9337  C CB  . LEU H  2 20  ? 38.504  -31.777  31.266  1.000 55.251  0 20  LEU HHH CB  1 ? 28 
ATOM   9338  C CG  . LEU H  2 20  ? 37.794  -33.019  30.729  1.000 56.947  0 20  LEU HHH CG  1 ? 28 
ATOM   9339  C CD1 . LEU H  2 20  ? 36.295  -32.931  31.003  1.000 56.671  0 20  LEU HHH CD1 1 ? 28 
ATOM   9340  C CD2 . LEU H  2 20  ? 38.093  -33.235  29.243  1.000 58.461  0 20  LEU HHH CD2 1 ? 28 
ATOM   9341  N N   . ALA H  2 21  ? 40.662  -29.336  30.681  1.000 52.148  0 21  ALA HHH N   1 ? 28 
ATOM   9342  C CA  . ALA H  2 21  ? 40.974  -27.972  31.139  1.000 51.078  0 21  ALA HHH CA  1 ? 28 
ATOM   9343  C C   . ALA H  2 21  ? 39.899  -27.007  30.660  1.000 51.096  0 21  ALA HHH C   1 ? 28 
ATOM   9344  O O   . ALA H  2 21  ? 39.254  -27.263  29.643  1.000 54.658  0 21  ALA HHH O   1 ? 28 
ATOM   9345  C CB  . ALA H  2 21  ? 42.326  -27.557  30.658  1.000 50.639  0 21  ALA HHH CB  1 ? 28 
ATOM   9346  N N   . CYS H  2 22  ? 39.720  -25.928  31.399  1.000 50.075  0 22  CYS HHH N   1 ? 28 
ATOM   9347  C CA  . CYS H  2 22  ? 38.800  -24.850  31.023  1.000 50.869  0 22  CYS HHH CA  1 ? 28 
ATOM   9348  C C   . CYS H  2 22  ? 39.436  -23.516  31.379  1.000 49.394  0 22  CYS HHH C   1 ? 28 
ATOM   9349  O O   . CYS H  2 22  ? 39.795  -23.335  32.545  1.000 50.143  0 22  CYS HHH O   1 ? 28 
ATOM   9350  C CB  . CYS H  2 22  ? 37.470  -25.025  31.724  1.000 54.588  0 22  CYS HHH CB  1 ? 28 
ATOM   9351  S SG  . CYS H  2 22  ? 36.450  -23.543  31.580  1.000 57.169  0 22  CYS HHH SG  1 ? 28 
ATOM   9352  N N   . ILE H  2 23  ? 39.564  -22.643  30.385  1.000 47.596  0 23  ILE HHH N   1 ? 28 
ATOM   9353  C CA  . ILE H  2 23  ? 40.197  -21.312  30.534  1.000 47.114  0 23  ILE HHH CA  1 ? 28 
ATOM   9354  C C   . ILE H  2 23  ? 39.095  -20.252  30.441  1.000 46.413  0 23  ILE HHH C   1 ? 28 
ATOM   9355  O O   . ILE H  2 23  ? 38.190  -20.391  29.627  1.000 45.786  0 23  ILE HHH O   1 ? 28 
ATOM   9356  C CB  . ILE H  2 23  ? 41.334  -21.146  29.508  1.000 47.988  0 23  ILE HHH CB  1 ? 28 
ATOM   9357  C CG1 . ILE H  2 23  ? 42.154  -19.884  29.798  1.000 50.064  0 23  ILE HHH CG1 1 ? 28 
ATOM   9358  C CG2 . ILE H  2 23  ? 40.813  -21.195  28.085  1.000 45.749  0 23  ILE HHH CG2 1 ? 28 
ATOM   9359  C CD1 . ILE H  2 23  ? 43.379  -19.727  28.910  1.000 51.104  0 23  ILE HHH CD1 1 ? 28 
ATOM   9360  N N   . ALA H  2 24  ? 39.155  -19.262  31.324  1.000 48.532  0 24  ALA HHH N   1 ? 28 
ATOM   9361  C CA  . ALA H  2 24  ? 38.202  -18.137  31.457  1.000 48.035  0 24  ALA HHH CA  1 ? 28 
ATOM   9362  C C   . ALA H  2 24  ? 38.864  -16.855  30.922  1.000 48.919  0 24  ALA HHH C   1 ? 28 
ATOM   9363  O O   . ALA H  2 24  ? 40.093  -16.712  31.020  1.000 47.031  0 24  ALA HHH O   1 ? 28 
ATOM   9364  C CB  . ALA H  2 24  ? 37.782  -17.982  32.895  1.000 46.587  0 24  ALA HHH CB  1 ? 28 
ATOM   9365  N N   . SER H  2 25  ? 38.053  -15.966  30.348  1.000 45.667  0 25  SER HHH N   1 ? 29 
ATOM   9366  C CA  . SER H  2 25  ? 38.395  -14.553  30.073  1.000 45.685  0 25  SER HHH CA  1 ? 29 
ATOM   9367  C C   . SER H  2 25  ? 38.516  -13.809  31.404  1.000 46.247  0 25  SER HHH C   1 ? 29 
ATOM   9368  O O   . SER H  2 25  ? 38.177  -14.403  32.446  1.000 46.257  0 25  SER HHH O   1 ? 29 
ATOM   9369  C CB  . SER H  2 25  ? 37.360  -13.930  29.194  1.000 45.580  0 25  SER HHH CB  1 ? 29 
ATOM   9370  O OG  . SER H  2 25  ? 36.125  -13.852  29.859  1.000 43.247  0 25  SER HHH OG  1 ? 29 
ATOM   9371  N N   . GLY H  2 26  ? 38.939  -12.549  31.375  1.000 47.640  0 26  GLY HHH N   1 ? 29 
ATOM   9372  C CA  . GLY H  2 26  ? 38.849  -11.666  32.555  1.000 48.869  0 26  GLY HHH CA  1 ? 29 
ATOM   9373  C C   . GLY H  2 26  ? 40.089  -11.666  33.434  1.000 47.481  0 26  GLY HHH C   1 ? 29 
ATOM   9374  O O   . GLY H  2 26  ? 40.930  -12.523  33.245  1.000 45.866  0 26  GLY HHH O   1 ? 29 
ATOM   9375  N N   . ARG H  2 27  ? 40.210  -10.685  34.319  1.000 48.674  0 27  ARG HHH N   1 ? 29 
ATOM   9376  C CA  . ARG H  2 27  ? 41.415  -10.498  35.154  1.000 53.195  0 27  ARG HHH CA  1 ? 29 
ATOM   9377  C C   . ARG H  2 27  ? 41.089  -10.747  36.624  1.000 50.624  0 27  ARG HHH C   1 ? 29 
ATOM   9378  O O   . ARG H  2 27  ? 41.891  -10.400  37.447  1.000 55.030  0 27  ARG HHH O   1 ? 29 
ATOM   9379  C CB  . ARG H  2 27  ? 42.003  -9.101   34.886  1.000 59.794  0 27  ARG HHH CB  1 ? 29 
ATOM   9380  C CG  . ARG H  2 27  ? 43.006  -9.044   33.736  1.000 66.987  0 27  ARG HHH CG  1 ? 29 
ATOM   9381  C CD  . ARG H  2 27  ? 42.950  -7.734   32.972  1.000 77.871  0 27  ARG HHH CD  1 ? 29 
ATOM   9382  N NE  . ARG H  2 27  ? 43.558  -6.705   33.817  1.000 88.505  0 27  ARG HHH NE  1 ? 29 
ATOM   9383  C CZ  . ARG H  2 27  ? 44.656  -5.977   33.524  1.000 94.558  0 27  ARG HHH CZ  1 ? 29 
ATOM   9384  N NH1 . ARG H  2 27  ? 45.303  -6.140   32.377  1.000 98.269  0 27  ARG HHH NH1 1 ? 29 
ATOM   9385  N NH2 . ARG H  2 27  ? 45.110  -5.091   34.399  1.000 93.875  0 27  ARG HHH NH2 1 ? 29 
ATOM   9386  N N   . THR H  2 28  ? 39.958  -11.351  36.950  1.000 50.408  0 28  THR HHH N   1 ? 29 
ATOM   9387  C CA  . THR H  2 28  ? 39.541  -11.630  38.354  1.000 49.559  0 28  THR HHH CA  1 ? 29 
ATOM   9388  C C   . THR H  2 28  ? 39.086  -13.084  38.449  1.000 47.750  0 28  THR HHH C   1 ? 29 
ATOM   9389  O O   . THR H  2 28  ? 38.076  -13.376  39.147  1.000 48.440  0 28  THR HHH O   1 ? 29 
ATOM   9390  C CB  . THR H  2 28  ? 38.446  -10.673  38.849  1.000 50.323  0 28  THR HHH CB  1 ? 29 
ATOM   9391  O OG1 . THR H  2 28  ? 37.380  -10.669  37.901  1.000 51.305  0 28  THR HHH OG1 1 ? 29 
ATOM   9392  C CG2 . THR H  2 28  ? 38.945  -9.264   39.026  1.000 52.616  0 28  THR HHH CG2 1 ? 29 
ATOM   9393  N N   . PHE H  2 29  ? 39.801  -13.985  37.783  1.000 46.309  0 29  PHE HHH N   1 ? 29 
ATOM   9394  C CA  . PHE H  2 29  ? 39.511  -15.441  37.827  1.000 45.042  0 29  PHE HHH CA  1 ? 29 
ATOM   9395  C C   . PHE H  2 29  ? 39.448  -15.934  39.284  1.000 46.096  0 29  PHE HHH C   1 ? 29 
ATOM   9396  O O   . PHE H  2 29  ? 38.599  -16.778  39.598  1.000 45.179  0 29  PHE HHH O   1 ? 29 
ATOM   9397  C CB  . PHE H  2 29  ? 40.567  -16.190  37.031  1.000 45.062  0 29  PHE HHH CB  1 ? 29 
ATOM   9398  C CG  . PHE H  2 29  ? 40.356  -17.671  36.993  1.000 43.419  0 29  PHE HHH CG  1 ? 29 
ATOM   9399  C CD1 . PHE H  2 29  ? 39.407  -18.226  36.159  1.000 42.727  0 29  PHE HHH CD1 1 ? 29 
ATOM   9400  C CD2 . PHE H  2 29  ? 41.111  -18.511  37.795  1.000 46.072  0 29  PHE HHH CD2 1 ? 29 
ATOM   9401  C CE1 . PHE H  2 29  ? 39.226  -19.600  36.104  1.000 42.073  0 29  PHE HHH CE1 1 ? 29 
ATOM   9402  C CE2 . PHE H  2 29  ? 40.927  -19.886  37.750  1.000 45.981  0 29  PHE HHH CE2 1 ? 29 
ATOM   9403  C CZ  . PHE H  2 29  ? 39.989  -20.429  36.900  1.000 44.910  0 29  PHE HHH CZ  1 ? 29 
ATOM   9404  N N   . HIS H  2 30  ? 40.316  -15.407  40.148  1.000 46.802  0 30  HIS HHH N   1 ? 29 
ATOM   9405  C CA  . HIS H  2 30  ? 40.408  -15.711  41.605  1.000 47.618  0 30  HIS HHH CA  1 ? 29 
ATOM   9406  C C   . HIS H  2 30  ? 39.082  -15.401  42.313  1.000 47.663  0 30  HIS HHH C   1 ? 29 
ATOM   9407  O O   . HIS H  2 30  ? 38.870  -15.936  43.412  1.000 50.404  0 30  HIS HHH O   1 ? 29 
ATOM   9408  C CB  . HIS H  2 30  ? 41.592  -14.966  42.231  1.000 47.741  0 30  HIS HHH CB  1 ? 29 
ATOM   9409  C CG  . HIS H  2 30  ? 41.379  -13.498  42.201  1.000 51.736  0 30  HIS HHH CG  1 ? 29 
ATOM   9410  N ND1 . HIS H  2 30  ? 40.735  -12.805  43.219  1.000 53.822  0 30  HIS HHH ND1 1 ? 29 
ATOM   9411  C CD2 . HIS H  2 30  ? 41.683  -12.583  41.253  1.000 51.949  0 30  HIS HHH CD2 1 ? 29 
ATOM   9412  C CE1 . HIS H  2 30  ? 40.653  -11.524  42.898  1.000 53.999  0 30  HIS HHH CE1 1 ? 29 
ATOM   9413  N NE2 . HIS H  2 30  ? 41.204  -11.371  41.693  1.000 54.285  0 30  HIS HHH NE2 1 ? 29 
ATOM   9414  N N   . SER H  2 31  ? 38.201  -14.593  41.734  1.000 47.147  0 31  SER HHH N   1 ? 29 
ATOM   9415  C CA  . SER H  2 31  ? 36.891  -14.223  42.340  1.000 47.159  0 31  SER HHH CA  1 ? 29 
ATOM   9416  C C   . SER H  2 31  ? 35.834  -15.292  42.043  1.000 43.867  0 31  SER HHH C   1 ? 29 
ATOM   9417  O O   . SER H  2 31  ? 34.692  -15.146  42.552  1.000 41.992  0 31  SER HHH O   1 ? 29 
ATOM   9418  C CB  . SER H  2 31  ? 36.389  -12.871  41.851  1.000 47.290  0 31  SER HHH CB  1 ? 29 
ATOM   9419  O OG  . SER H  2 31  ? 37.307  -11.829  42.126  1.000 52.676  0 31  SER HHH OG  1 ? 29 
ATOM   9420  N N   . TYR H  2 32  ? 36.152  -16.296  41.220  1.000 43.624  0 32  TYR HHH N   1 ? 29 
ATOM   9421  C CA  . TYR H  2 32  ? 35.135  -17.258  40.705  1.000 43.439  0 32  TYR HHH CA  1 ? 29 
ATOM   9422  C C   . TYR H  2 32  ? 35.308  -18.608  41.384  1.000 42.457  0 32  TYR HHH C   1 ? 29 
ATOM   9423  O O   . TYR H  2 32  ? 36.419  -19.112  41.468  1.000 48.061  0 32  TYR HHH O   1 ? 29 
ATOM   9424  C CB  . TYR H  2 32  ? 35.153  -17.365  39.174  1.000 41.230  0 32  TYR HHH CB  1 ? 29 
ATOM   9425  C CG  . TYR H  2 32  ? 34.577  -16.139  38.533  1.000 42.398  0 32  TYR HHH CG  1 ? 29 
ATOM   9426  C CD1 . TYR H  2 32  ? 33.219  -15.992  38.333  1.000 46.067  0 32  TYR HHH CD1 1 ? 29 
ATOM   9427  C CD2 . TYR H  2 32  ? 35.389  -15.060  38.235  1.000 44.644  0 32  TYR HHH CD2 1 ? 29 
ATOM   9428  C CE1 . TYR H  2 32  ? 32.682  -14.839  37.766  1.000 47.658  0 32  TYR HHH CE1 1 ? 29 
ATOM   9429  C CE2 . TYR H  2 32  ? 34.874  -13.903  37.667  1.000 46.909  0 32  TYR HHH CE2 1 ? 29 
ATOM   9430  C CZ  . TYR H  2 32  ? 33.512  -13.768  37.470  1.000 47.394  0 32  TYR HHH CZ  1 ? 29 
ATOM   9431  O OH  . TYR H  2 32  ? 33.042  -12.591  36.957  1.000 47.280  0 32  TYR HHH OH  1 ? 29 
ATOM   9432  N N   . VAL H  2 33  ? 34.200  -19.152  41.870  1.000 43.269  0 33  VAL HHH N   1 ? 29 
ATOM   9433  C CA  . VAL H  2 33  ? 34.031  -20.611  42.111  1.000 43.086  0 33  VAL HHH CA  1 ? 29 
ATOM   9434  C C   . VAL H  2 33  ? 33.920  -21.264  40.729  1.000 43.517  0 33  VAL HHH C   1 ? 29 
ATOM   9435  O O   . VAL H  2 33  ? 33.092  -20.810  39.927  1.000 41.665  0 33  VAL HHH O   1 ? 29 
ATOM   9436  C CB  . VAL H  2 33  ? 32.796  -20.884  42.983  1.000 43.108  0 33  VAL HHH CB  1 ? 29 
ATOM   9437  C CG1 . VAL H  2 33  ? 32.522  -22.372  43.133  1.000 43.504  0 33  VAL HHH CG1 1 ? 29 
ATOM   9438  C CG2 . VAL H  2 33  ? 32.922  -20.219  44.340  1.000 45.346  0 33  VAL HHH CG2 1 ? 29 
ATOM   9439  N N   . MET H  2 34  ? 34.737  -22.274  40.456  1.000 43.259  0 34  MET HHH N   1 ? 29 
ATOM   9440  C CA  . MET H  2 34  ? 34.758  -22.983  39.154  1.000 42.188  0 34  MET HHH CA  1 ? 29 
ATOM   9441  C C   . MET H  2 34  ? 34.189  -24.394  39.338  1.000 45.075  0 34  MET HHH C   1 ? 29 
ATOM   9442  O O   . MET H  2 34  ? 34.418  -25.029  40.398  1.000 46.342  0 34  MET HHH O   1 ? 29 
ATOM   9443  C CB  . MET H  2 34  ? 36.181  -23.052  38.591  1.000 43.361  0 34  MET HHH CB  1 ? 29 
ATOM   9444  C CG  . MET H  2 34  ? 36.810  -21.688  38.364  1.000 42.461  0 34  MET HHH CG  1 ? 29 
ATOM   9445  S SD  . MET H  2 34  ? 35.823  -20.650  37.263  1.000 43.789  0 34  MET HHH SD  1 ? 29 
ATOM   9446  C CE  . MET H  2 34  ? 35.932  -21.569  35.724  1.000 41.889  0 34  MET HHH CE  1 ? 29 
ATOM   9447  N N   . ALA H  2 35  ? 33.450  -24.880  38.342  1.000 45.697  0 35  ALA HHH N   1 ? 29 
ATOM   9448  C CA  . ALA H  2 35  ? 32.760  -26.183  38.427  1.000 46.535  0 35  ALA HHH CA  1 ? 29 
ATOM   9449  C C   . ALA H  2 35  ? 32.760  -26.896  37.076  1.000 46.664  0 35  ALA HHH C   1 ? 29 
ATOM   9450  O O   . ALA H  2 35  ? 32.919  -26.242  36.028  1.000 44.345  0 35  ALA HHH O   1 ? 29 
ATOM   9451  C CB  . ALA H  2 35  ? 31.359  -25.988  38.943  1.000 47.855  0 35  ALA HHH CB  1 ? 29 
ATOM   9452  N N   . TRP H  2 36  ? 32.621  -28.221  37.166  1.000 49.093  0 36  TRP HHH N   1 ? 29 
ATOM   9453  C CA  . TRP H  2 36  ? 32.401  -29.158  36.047  1.000 47.613  0 36  TRP HHH CA  1 ? 29 
ATOM   9454  C C   . TRP H  2 36  ? 31.057  -29.846  36.244  1.000 49.693  0 36  TRP HHH C   1 ? 29 
ATOM   9455  O O   . TRP H  2 36  ? 30.771  -30.314  37.351  1.000 48.004  0 36  TRP HHH O   1 ? 29 
ATOM   9456  C CB  . TRP H  2 36  ? 33.534  -30.164  35.977  1.000 48.818  0 36  TRP HHH CB  1 ? 29 
ATOM   9457  C CG  . TRP H  2 36  ? 34.824  -29.571  35.528  1.000 48.545  0 36  TRP HHH CG  1 ? 29 
ATOM   9458  C CD1 . TRP H  2 36  ? 35.852  -29.147  36.311  1.000 48.275  0 36  TRP HHH CD1 1 ? 29 
ATOM   9459  C CD2 . TRP H  2 36  ? 35.226  -29.323  34.174  1.000 49.408  0 36  TRP HHH CD2 1 ? 29 
ATOM   9460  N NE1 . TRP H  2 36  ? 36.870  -28.668  35.544  1.000 48.466  0 36  TRP HHH NE1 1 ? 29 
ATOM   9461  C CE2 . TRP H  2 36  ? 36.513  -28.759  34.228  1.000 49.142  0 36  TRP HHH CE2 1 ? 29 
ATOM   9462  C CE3 . TRP H  2 36  ? 34.631  -29.521  32.927  1.000 50.702  0 36  TRP HHH CE3 1 ? 29 
ATOM   9463  C CZ2 . TRP H  2 36  ? 37.216  -28.411  33.082  1.000 49.040  0 36  TRP HHH CZ2 1 ? 29 
ATOM   9464  C CZ3 . TRP H  2 36  ? 35.326  -29.166  31.796  1.000 50.269  0 36  TRP HHH CZ3 1 ? 29 
ATOM   9465  C CH2 . TRP H  2 36  ? 36.598  -28.605  31.876  1.000 49.410  0 36  TRP HHH CH2 1 ? 29 
ATOM   9466  N N   . PHE H  2 37  ? 30.253  -29.851  35.188  1.000 50.397  0 37  PHE HHH N   1 ? 29 
ATOM   9467  C CA  . PHE H  2 37  ? 29.018  -30.648  35.063  1.000 51.628  0 37  PHE HHH CA  1 ? 29 
ATOM   9468  C C   . PHE H  2 37  ? 29.180  -31.515  33.825  1.000 51.794  0 37  PHE HHH C   1 ? 29 
ATOM   9469  O O   . PHE H  2 37  ? 30.042  -31.213  33.006  1.000 51.397  0 37  PHE HHH O   1 ? 29 
ATOM   9470  C CB  . PHE H  2 37  ? 27.800  -29.734  34.921  1.000 51.421  0 37  PHE HHH CB  1 ? 29 
ATOM   9471  C CG  . PHE H  2 37  ? 27.388  -29.033  36.184  1.000 51.292  0 37  PHE HHH CG  1 ? 29 
ATOM   9472  C CD1 . PHE H  2 37  ? 28.116  -27.959  36.666  1.000 49.930  0 37  PHE HHH CD1 1 ? 29 
ATOM   9473  C CD2 . PHE H  2 37  ? 26.259  -29.431  36.875  1.000 52.571  0 37  PHE HHH CD2 1 ? 29 
ATOM   9474  C CE1 . PHE H  2 37  ? 27.716  -27.314  37.828  1.000 51.694  0 37  PHE HHH CE1 1 ? 29 
ATOM   9475  C CE2 . PHE H  2 37  ? 25.876  -28.786  38.033  1.000 51.405  0 37  PHE HHH CE2 1 ? 29 
ATOM   9476  C CZ  . PHE H  2 37  ? 26.605  -27.729  38.508  1.000 50.572  0 37  PHE HHH CZ  1 ? 29 
ATOM   9477  N N   . ARG H  2 38  ? 28.349  -32.537  33.687  1.000 53.058  0 38  ARG HHH N   1 ? 29 
ATOM   9478  C CA  . ARG H  2 38  ? 28.316  -33.354  32.456  1.000 55.253  0 38  ARG HHH CA  1 ? 29 
ATOM   9479  C C   . ARG H  2 38  ? 26.877  -33.719  32.109  1.000 56.853  0 38  ARG HHH C   1 ? 29 
ATOM   9480  O O   . ARG H  2 38  ? 26.000  -33.690  32.987  1.000 57.578  0 38  ARG HHH O   1 ? 29 
ATOM   9481  C CB  . ARG H  2 38  ? 29.181  -34.602  32.621  1.000 55.854  0 38  ARG HHH CB  1 ? 29 
ATOM   9482  C CG  . ARG H  2 38  ? 28.582  -35.650  33.545  1.000 56.632  0 38  ARG HHH CG  1 ? 29 
ATOM   9483  C CD  . ARG H  2 38  ? 29.614  -36.681  33.940  1.000 56.619  0 38  ARG HHH CD  1 ? 29 
ATOM   9484  N NE  . ARG H  2 38  ? 29.067  -37.633  34.899  1.000 59.259  0 38  ARG HHH NE  1 ? 29 
ATOM   9485  C CZ  . ARG H  2 38  ? 29.720  -38.702  35.348  1.000 61.380  0 38  ARG HHH CZ  1 ? 29 
ATOM   9486  N NH1 . ARG H  2 38  ? 30.948  -38.973  34.939  1.000 62.572  0 38  ARG HHH NH1 1 ? 29 
ATOM   9487  N NH2 . ARG H  2 38  ? 29.143  -39.497  36.225  1.000 64.347  0 38  ARG HHH NH2 1 ? 29 
ATOM   9488  N N   . GLN H  2 39  ? 26.658  -34.046  30.852  1.000 58.799  0 39  GLN HHH N   1 ? 29 
ATOM   9489  C CA  . GLN H  2 39  ? 25.313  -34.371  30.338  1.000 61.479  0 39  GLN HHH CA  1 ? 29 
ATOM   9490  C C   . GLN H  2 39  ? 25.451  -35.413  29.240  1.000 62.759  0 39  GLN HHH C   1 ? 29 
ATOM   9491  O O   . GLN H  2 39  ? 26.085  -35.128  28.231  1.000 61.157  0 39  GLN HHH O   1 ? 29 
ATOM   9492  C CB  . GLN H  2 39  ? 24.641  -33.104  29.815  1.000 60.950  0 39  GLN HHH CB  1 ? 29 
ATOM   9493  C CG  . GLN H  2 39  ? 23.247  -33.359  29.335  1.000 62.972  0 39  GLN HHH CG  1 ? 29 
ATOM   9494  C CD  . GLN H  2 39  ? 22.498  -32.085  29.098  1.000 63.462  0 39  GLN HHH CD  1 ? 29 
ATOM   9495  O OE1 . GLN H  2 39  ? 23.067  -31.073  28.690  1.000 62.471  0 39  GLN HHH OE1 1 ? 29 
ATOM   9496  N NE2 . GLN H  2 39  ? 21.194  -32.176  29.254  1.000 67.104  0 39  GLN HHH NE2 1 ? 29 
ATOM   9497  N N   . ALA H  2 40  ? 24.918  -36.605  29.456  1.000 66.250  0 40  ALA HHH N   1 ? 29 
ATOM   9498  C CA  . ALA H  2 40  ? 24.744  -37.658  28.431  1.000 71.221  0 40  ALA HHH CA  1 ? 29 
ATOM   9499  C C   . ALA H  2 40  ? 23.459  -37.341  27.674  1.000 75.198  0 40  ALA HHH C   1 ? 29 
ATOM   9500  O O   . ALA H  2 40  ? 22.586  -36.672  28.212  1.000 73.252  0 40  ALA HHH O   1 ? 29 
ATOM   9501  C CB  . ALA H  2 40  ? 24.707  -38.997  29.117  1.000 73.581  0 40  ALA HHH CB  1 ? 29 
ATOM   9502  N N   . PRO H  2 41  ? 23.276  -37.809  26.424  1.000 80.057  0 41  PRO HHH N   1 ? 29 
ATOM   9503  C CA  . PRO H  2 41  ? 22.108  -37.439  25.635  1.000 84.122  0 41  PRO HHH CA  1 ? 29 
ATOM   9504  C C   . PRO H  2 41  ? 20.722  -37.692  26.241  1.000 86.835  0 41  PRO HHH C   1 ? 29 
ATOM   9505  O O   . PRO H  2 41  ? 19.977  -36.795  25.979  1.000 88.002  0 41  PRO HHH O   1 ? 29 
ATOM   9506  C CB  . PRO H  2 41  ? 22.276  -38.139  24.273  1.000 87.110  0 41  PRO HHH CB  1 ? 29 
ATOM   9507  C CG  . PRO H  2 41  ? 23.734  -38.507  24.224  1.000 85.532  0 41  PRO HHH CG  1 ? 29 
ATOM   9508  C CD  . PRO H  2 41  ? 24.168  -38.685  25.668  1.000 82.939  0 41  PRO HHH CD  1 ? 29 
ATOM   9509  N N   . GLY H  2 42  ? 20.372  -38.747  27.009  1.000 89.405  0 42  GLY HHH N   1 ? 29 
ATOM   9510  C CA  . GLY H  2 42  ? 19.020  -38.897  27.580  1.000 94.725  0 42  GLY HHH CA  1 ? 29 
ATOM   9511  C C   . GLY H  2 42  ? 18.821  -38.139  28.903  1.000 96.673  0 42  GLY HHH C   1 ? 29 
ATOM   9512  O O   . GLY H  2 42  ? 17.754  -38.229  29.472  1.000 102.744 0 42  GLY HHH O   1 ? 29 
ATOM   9513  N N   . LYS H  2 43  ? 19.853  -37.470  29.405  1.000 95.744  0 43  LYS HHH N   1 ? 29 
ATOM   9514  C CA  . LYS H  2 43  ? 20.025  -37.197  30.867  1.000 95.900  0 43  LYS HHH CA  1 ? 29 
ATOM   9515  C C   . LYS H  2 43  ? 20.051  -35.694  31.097  1.000 92.529  0 43  LYS HHH C   1 ? 29 
ATOM   9516  O O   . LYS H  2 43  ? 20.279  -34.945  30.144  1.000 89.285  0 43  LYS HHH O   1 ? 29 
ATOM   9517  C CB  . LYS H  2 43  ? 21.312  -37.808  31.423  1.000 99.508  0 43  LYS HHH CB  1 ? 29 
ATOM   9518  C CG  . LYS H  2 43  ? 21.197  -39.304  31.718  1.000 106.640 0 43  LYS HHH CG  1 ? 29 
ATOM   9519  C CD  . LYS H  2 43  ? 22.426  -40.101  32.083  1.000 108.579 0 43  LYS HHH CD  1 ? 29 
ATOM   9520  C CE  . LYS H  2 43  ? 22.576  -41.419  31.318  1.000 110.118 0 43  LYS HHH CE  1 ? 29 
ATOM   9521  N NZ  . LYS H  2 43  ? 22.707  -42.595  32.209  1.000 110.323 0 43  LYS HHH NZ  1 ? 29 
ATOM   9522  N N   . GLU H  2 44  ? 19.800  -35.261  32.337  1.000 90.445  0 44  GLU HHH N   1 ? 29 
ATOM   9523  C CA  . GLU H  2 44  ? 19.943  -33.838  32.740  1.000 83.977  0 44  GLU HHH CA  1 ? 29 
ATOM   9524  C C   . GLU H  2 44  ? 21.405  -33.583  33.079  1.000 75.359  0 44  GLU HHH C   1 ? 29 
ATOM   9525  O O   . GLU H  2 44  ? 22.147  -34.545  33.159  1.000 74.249  0 44  GLU HHH O   1 ? 29 
ATOM   9526  C CB  . GLU H  2 44  ? 19.000  -33.497  33.884  1.000 88.259  0 44  GLU HHH CB  1 ? 29 
ATOM   9527  C CG  . GLU H  2 44  ? 17.546  -33.706  33.480  1.000 95.535  0 44  GLU HHH CG  1 ? 29 
ATOM   9528  C CD  . GLU H  2 44  ? 16.554  -33.823  34.625  1.000 99.943  0 44  GLU HHH CD  1 ? 29 
ATOM   9529  O OE1 . GLU H  2 44  ? 16.748  -33.079  35.623  1.000 99.104  0 44  GLU HHH OE1 1 ? 29 
ATOM   9530  O OE2 . GLU H  2 44  ? 15.600  -34.657  34.519  1.000 101.982 0 44  GLU HHH OE2 1 ? 29 
ATOM   9531  N N   . ARG H  2 45  ? 21.784  -32.316  33.211  1.000 68.194  0 45  ARG HHH N   1 ? 29 
ATOM   9532  C CA  . ARG H  2 45  ? 23.131  -31.900  33.660  1.000 66.265  0 45  ARG HHH CA  1 ? 29 
ATOM   9533  C C   . ARG H  2 45  ? 23.355  -32.452  35.070  1.000 66.044  0 45  ARG HHH C   1 ? 29 
ATOM   9534  O O   . ARG H  2 45  ? 22.554  -32.155  35.969  1.000 69.602  0 45  ARG HHH O   1 ? 29 
ATOM   9535  C CB  . ARG H  2 45  ? 23.273  -30.375  33.656  1.000 64.270  0 45  ARG HHH CB  1 ? 29 
ATOM   9536  C CG  . ARG H  2 45  ? 23.949  -29.879  32.399  1.000 64.115  0 45  ARG HHH CG  1 ? 29 
ATOM   9537  C CD  . ARG H  2 45  ? 23.758  -28.410  32.148  1.000 66.018  0 45  ARG HHH CD  1 ? 29 
ATOM   9538  N NE  . ARG H  2 45  ? 23.724  -28.160  30.715  1.000 70.221  0 45  ARG HHH NE  1 ? 29 
ATOM   9539  C CZ  . ARG H  2 45  ? 24.084  -27.032  30.109  1.000 70.683  0 45  ARG HHH CZ  1 ? 29 
ATOM   9540  N NH1 . ARG H  2 45  ? 24.488  -25.990  30.808  1.000 73.664  0 45  ARG HHH NH1 1 ? 29 
ATOM   9541  N NH2 . ARG H  2 45  ? 23.949  -26.907  28.808  1.000 71.425  0 45  ARG HHH NH2 1 ? 29 
ATOM   9542  N N   . GLU H  2 46  ? 24.421  -33.212  35.233  1.000 63.556  0 46  GLU HHH N   1 ? 29 
ATOM   9543  C CA  . GLU H  2 46  ? 24.818  -33.868  36.493  1.000 63.257  0 46  GLU HHH CA  1 ? 29 
ATOM   9544  C C   . GLU H  2 46  ? 26.071  -33.132  36.997  1.000 60.023  0 46  GLU HHH C   1 ? 29 
ATOM   9545  O O   . GLU H  2 46  ? 27.000  -32.878  36.205  1.000 57.571  0 46  GLU HHH O   1 ? 29 
ATOM   9546  C CB  . GLU H  2 46  ? 24.984  -35.358  36.186  1.000 65.606  0 46  GLU HHH CB  1 ? 29 
ATOM   9547  C CG  . GLU H  2 46  ? 25.489  -36.180  37.351  1.000 68.625  0 46  GLU HHH CG  1 ? 29 
ATOM   9548  C CD  . GLU H  2 46  ? 25.906  -37.603  36.995  1.000 73.113  0 46  GLU HHH CD  1 ? 29 
ATOM   9549  O OE1 . GLU H  2 46  ? 25.584  -38.063  35.884  1.000 76.051  0 46  GLU HHH OE1 1 ? 29 
ATOM   9550  O OE2 . GLU H  2 46  ? 26.527  -38.260  37.844  1.000 77.641  0 46  GLU HHH OE2 1 ? 29 
ATOM   9551  N N   . PHE H  2 47  ? 26.079  -32.730  38.266  1.000 59.005  0 47  PHE HHH N   1 ? 29 
ATOM   9552  C CA  . PHE H  2 47  ? 27.255  -32.119  38.923  1.000 55.324  0 47  PHE HHH CA  1 ? 29 
ATOM   9553  C C   . PHE H  2 47  ? 28.385  -33.145  38.976  1.000 54.248  0 47  PHE HHH C   1 ? 29 
ATOM   9554  O O   . PHE H  2 47  ? 28.152  -34.286  39.368  1.000 54.515  0 47  PHE HHH O   1 ? 29 
ATOM   9555  C CB  . PHE H  2 47  ? 26.917  -31.652  40.334  1.000 55.883  0 47  PHE HHH CB  1 ? 29 
ATOM   9556  C CG  . PHE H  2 47  ? 28.108  -31.142  41.108  1.000 55.581  0 47  PHE HHH CG  1 ? 29 
ATOM   9557  C CD1 . PHE H  2 47  ? 28.578  -29.854  40.912  1.000 53.212  0 47  PHE HHH CD1 1 ? 29 
ATOM   9558  C CD2 . PHE H  2 47  ? 28.742  -31.944  42.037  1.000 54.556  0 47  PHE HHH CD2 1 ? 29 
ATOM   9559  C CE1 . PHE H  2 47  ? 29.642  -29.378  41.648  1.000 51.777  0 47  PHE HHH CE1 1 ? 29 
ATOM   9560  C CE2 . PHE H  2 47  ? 29.825  -31.475  42.765  1.000 53.423  0 47  PHE HHH CE2 1 ? 29 
ATOM   9561  C CZ  . PHE H  2 47  ? 30.278  -30.194  42.561  1.000 52.338  0 47  PHE HHH CZ  1 ? 29 
ATOM   9562  N N   . VAL H  2 48  ? 29.593  -32.709  38.627  1.000 53.209  0 48  VAL HHH N   1 ? 29 
ATOM   9563  C CA  . VAL H  2 48  ? 30.817  -33.552  38.680  1.000 54.542  0 48  VAL HHH CA  1 ? 29 
ATOM   9564  C C   . VAL H  2 48  ? 31.735  -33.063  39.808  1.000 52.051  0 48  VAL HHH C   1 ? 29 
ATOM   9565  O O   . VAL H  2 48  ? 32.111  -33.895  40.671  1.000 52.506  0 48  VAL HHH O   1 ? 29 
ATOM   9566  C CB  . VAL H  2 48  ? 31.522  -33.578  37.313  1.000 55.353  0 48  VAL HHH CB  1 ? 29 
ATOM   9567  C CG1 . VAL H  2 48  ? 32.810  -34.367  37.392  1.000 56.920  0 48  VAL HHH CG1 1 ? 29 
ATOM   9568  C CG2 . VAL H  2 48  ? 30.613  -34.150  36.227  1.000 57.963  0 48  VAL HHH CG2 1 ? 29 
ATOM   9569  N N   . ALA H  2 49  ? 32.123  -31.785  39.789  1.000 49.678  0 49  ALA HHH N   1 ? 29 
ATOM   9570  C CA  . ALA H  2 49  ? 33.113  -31.231  40.751  1.000 50.838  0 49  ALA HHH CA  1 ? 29 
ATOM   9571  C C   . ALA H  2 49  ? 33.068  -29.700  40.784  1.000 48.825  0 49  ALA HHH C   1 ? 29 
ATOM   9572  O O   . ALA H  2 49  ? 32.628  -29.063  39.799  1.000 50.162  0 49  ALA HHH O   1 ? 29 
ATOM   9573  C CB  . ALA H  2 49  ? 34.500  -31.719  40.429  1.000 50.903  0 49  ALA HHH CB  1 ? 29 
ATOM   9574  N N   . ALA H  2 50  ? 33.514  -29.134  41.906  1.000 46.592  0 50  ALA HHH N   1 ? 29 
ATOM   9575  C CA  . ALA H  2 50  ? 33.614  -27.670  42.095  1.000 44.400  0 50  ALA HHH CA  1 ? 29 
ATOM   9576  C C   . ALA H  2 50  ? 34.771  -27.361  43.043  1.000 44.725  0 50  ALA HHH C   1 ? 29 
ATOM   9577  O O   . ALA H  2 50  ? 35.118  -28.216  43.908  1.000 47.720  0 50  ALA HHH O   1 ? 29 
ATOM   9578  C CB  . ALA H  2 50  ? 32.320  -27.112  42.623  1.000 43.581  0 50  ALA HHH CB  1 ? 29 
ATOM   9579  N N   . ILE H  2 51  ? 35.335  -26.170  42.879  1.000 41.944  0 51  ILE HHH N   1 ? 29 
ATOM   9580  C CA  . ILE H  2 51  ? 36.494  -25.693  43.674  1.000 43.449  0 51  ILE HHH CA  1 ? 29 
ATOM   9581  C C   . ILE H  2 51  ? 36.255  -24.229  44.047  1.000 42.844  0 51  ILE HHH C   1 ? 29 
ATOM   9582  O O   . ILE H  2 51  ? 35.944  -23.396  43.149  1.000 40.159  0 51  ILE HHH O   1 ? 29 
ATOM   9583  C CB  . ILE H  2 51  ? 37.793  -25.934  42.876  1.000 43.345  0 51  ILE HHH CB  1 ? 29 
ATOM   9584  C CG1 . ILE H  2 51  ? 39.034  -25.628  43.718  1.000 46.350  0 51  ILE HHH CG1 1 ? 29 
ATOM   9585  C CG2 . ILE H  2 51  ? 37.809  -25.187  41.564  1.000 40.724  0 51  ILE HHH CG2 1 ? 29 
ATOM   9586  C CD1 . ILE H  2 51  ? 40.334  -26.173  43.136  1.000 47.171  0 51  ILE HHH CD1 1 ? 29 
ATOM   9587  N N   . SER H  2 52  ? 36.389  -23.926  45.333  1.000 45.587  0 52  SER HHH N   1 ? 29 
ATOM   9588  C CA  . SER H  2 52  ? 36.196  -22.557  45.879  1.000 45.820  0 52  SER HHH CA  1 ? 29 
ATOM   9589  C C   . SER H  2 52  ? 37.388  -21.685  45.485  1.000 46.422  0 52  SER HHH C   1 ? 29 
ATOM   9590  O O   . SER H  2 52  ? 38.363  -22.217  44.895  1.000 48.709  0 52  SER HHH O   1 ? 29 
ATOM   9591  C CB  . SER H  2 52  ? 36.005  -22.585  47.364  1.000 47.094  0 52  SER HHH CB  1 ? 29 
ATOM   9592  O OG  . SER H  2 52  ? 35.379  -21.396  47.783  1.000 49.147  0 52  SER HHH OG  1 ? 29 
ATOM   9593  N N   . TRP H  2 53  ? 37.307  -20.400  45.812  1.000 48.613  0 53  TRP HHH N   1 ? 29 
ATOM   9594  C CA  . TRP H  2 53  ? 38.293  -19.347  45.430  1.000 47.649  0 53  TRP HHH CA  1 ? 29 
ATOM   9595  C C   . TRP H  2 53  ? 39.706  -19.761  45.848  1.000 46.078  0 53  TRP HHH C   1 ? 29 
ATOM   9596  O O   . TRP H  2 53  ? 40.578  -19.752  45.015  1.000 47.912  0 53  TRP HHH O   1 ? 29 
ATOM   9597  C CB  . TRP H  2 53  ? 37.907  -18.003  46.066  1.000 46.944  0 53  TRP HHH CB  1 ? 29 
ATOM   9598  C CG  . TRP H  2 53  ? 36.459  -17.667  45.923  1.000 45.427  0 53  TRP HHH CG  1 ? 29 
ATOM   9599  C CD1 . TRP H  2 53  ? 35.851  -17.203  44.799  1.000 44.472  0 53  TRP HHH CD1 1 ? 29 
ATOM   9600  C CD2 . TRP H  2 53  ? 35.441  -17.758  46.932  1.000 44.168  0 53  TRP HHH CD2 1 ? 29 
ATOM   9601  N NE1 . TRP H  2 53  ? 34.516  -17.018  45.023  1.000 41.674  0 53  TRP HHH NE1 1 ? 29 
ATOM   9602  C CE2 . TRP H  2 53  ? 34.234  -17.328  46.332  1.000 43.940  0 53  TRP HHH CE2 1 ? 29 
ATOM   9603  C CE3 . TRP H  2 53  ? 35.433  -18.152  48.272  1.000 44.911  0 53  TRP HHH CE3 1 ? 29 
ATOM   9604  C CZ2 . TRP H  2 53  ? 33.024  -17.295  47.030  1.000 43.469  0 53  TRP HHH CZ2 1 ? 29 
ATOM   9605  C CZ3 . TRP H  2 53  ? 34.242  -18.114  48.964  1.000 46.182  0 53  TRP HHH CZ3 1 ? 29 
ATOM   9606  C CH2 . TRP H  2 53  ? 33.054  -17.695  48.349  1.000 45.745  0 53  TRP HHH CH2 1 ? 29 
ATOM   9607  N N   . SER H  2 54  ? 39.881  -20.136  47.105  1.000 47.678  0 54  SER HHH N   1 ? 29 
ATOM   9608  C CA  . SER H  2 54  ? 41.180  -20.474  47.746  1.000 51.497  0 54  SER HHH CA  1 ? 29 
ATOM   9609  C C   . SER H  2 54  ? 41.663  -21.854  47.301  1.000 52.907  0 54  SER HHH C   1 ? 29 
ATOM   9610  O O   . SER H  2 54  ? 42.745  -22.234  47.743  1.000 54.930  0 54  SER HHH O   1 ? 29 
ATOM   9611  C CB  . SER H  2 54  ? 41.032  -20.452  49.235  1.000 53.075  0 54  SER HHH CB  1 ? 29 
ATOM   9612  O OG  . SER H  2 54  ? 40.186  -21.524  49.627  1.000 53.648  0 54  SER HHH OG  1 ? 29 
ATOM   9613  N N   . SER H  2 55  ? 40.840  -22.597  46.549  1.000 52.360  0 55  SER HHH N   1 ? 29 
ATOM   9614  C CA  . SER H  2 55  ? 41.012  -24.048  46.241  1.000 53.490  0 55  SER HHH CA  1 ? 29 
ATOM   9615  C C   . SER H  2 55  ? 40.498  -24.941  47.381  1.000 54.961  0 55  SER HHH C   1 ? 29 
ATOM   9616  O O   . SER H  2 55  ? 40.570  -26.162  47.182  1.000 53.902  0 55  SER HHH O   1 ? 29 
ATOM   9617  C CB  . SER H  2 55  ? 42.456  -24.426  45.918  1.000 54.175  0 55  SER HHH CB  1 ? 29 
ATOM   9618  O OG  . SER H  2 55  ? 42.936  -23.725  44.789  1.000 53.747  0 55  SER HHH OG  1 ? 29 
ATOM   9619  N N   . THR H  2 56  ? 40.010  -24.410  48.510  1.000 59.225  0 56  THR HHH N   1 ? 29 
ATOM   9620  C CA  . THR H  2 56  ? 40.180  -25.126  49.807  1.000 68.965  0 56  THR HHH CA  1 ? 29 
ATOM   9621  C C   . THR H  2 56  ? 38.983  -25.967  50.211  1.000 70.558  0 56  THR HHH C   1 ? 29 
ATOM   9622  O O   . THR H  2 56  ? 39.187  -26.940  50.946  1.000 77.010  0 56  THR HHH O   1 ? 29 
ATOM   9623  C CB  . THR H  2 56  ? 40.535  -24.229  50.995  1.000 76.310  0 56  THR HHH CB  1 ? 29 
ATOM   9624  O OG1 . THR H  2 56  ? 41.960  -24.149  50.934  1.000 79.013  0 56  THR HHH OG1 1 ? 29 
ATOM   9625  C CG2 . THR H  2 56  ? 40.096  -24.776  52.345  1.000 78.433  0 56  THR HHH CG2 1 ? 29 
ATOM   9626  N N   . PRO H  2 57  ? 37.722  -25.562  49.937  1.000 63.275  0 57  PRO HHH N   1 ? 29 
ATOM   9627  C CA  . PRO H  2 57  ? 36.660  -26.556  49.801  1.000 58.736  0 57  PRO HHH CA  1 ? 29 
ATOM   9628  C C   . PRO H  2 57  ? 36.695  -26.978  48.322  1.000 53.966  0 57  PRO HHH C   1 ? 29 
ATOM   9629  O O   . PRO H  2 57  ? 36.636  -26.131  47.454  1.000 49.712  0 57  PRO HHH O   1 ? 29 
ATOM   9630  C CB  . PRO H  2 57  ? 35.403  -25.854  50.318  1.000 56.575  0 57  PRO HHH CB  1 ? 29 
ATOM   9631  C CG  . PRO H  2 57  ? 35.822  -24.401  50.551  1.000 58.539  0 57  PRO HHH CG  1 ? 29 
ATOM   9632  C CD  . PRO H  2 57  ? 37.219  -24.187  49.989  1.000 58.528  0 57  PRO HHH CD  1 ? 29 
ATOM   9633  N N   . THR H  2 58  ? 36.915  -28.274  48.073  1.000 55.226  0 58  THR HHH N   1 ? 29 
ATOM   9634  C CA  . THR H  2 58  ? 36.588  -28.953  46.788  1.000 53.150  0 58  THR HHH CA  1 ? 29 
ATOM   9635  C C   . THR H  2 58  ? 35.380  -29.851  47.015  1.000 53.460  0 58  THR HHH C   1 ? 29 
ATOM   9636  O O   . THR H  2 58  ? 35.165  -30.245  48.155  1.000 54.320  0 58  THR HHH O   1 ? 29 
ATOM   9637  C CB  . THR H  2 58  ? 37.739  -29.770  46.186  1.000 53.560  0 58  THR HHH CB  1 ? 29 
ATOM   9638  O OG1 . THR H  2 58  ? 38.168  -30.783  47.095  1.000 55.847  0 58  THR HHH OG1 1 ? 29 
ATOM   9639  C CG2 . THR H  2 58  ? 38.899  -28.899  45.771  1.000 52.714  0 58  THR HHH CG2 1 ? 29 
ATOM   9640  N N   . TYR H  2 59  ? 34.606  -30.101  45.966  1.000 52.638  0 59  TYR HHH N   1 ? 29 
ATOM   9641  C CA  . TYR H  2 59  ? 33.366  -30.906  46.033  1.000 54.201  0 59  TYR HHH CA  1 ? 29 
ATOM   9642  C C   . TYR H  2 59  ? 33.331  -31.838  44.826  1.000 54.527  0 59  TYR HHH C   1 ? 29 
ATOM   9643  O O   . TYR H  2 59  ? 33.825  -31.453  43.749  1.000 55.528  0 59  TYR HHH O   1 ? 29 
ATOM   9644  C CB  . TYR H  2 59  ? 32.115  -30.022  45.990  1.000 53.254  0 59  TYR HHH CB  1 ? 29 
ATOM   9645  C CG  . TYR H  2 59  ? 32.003  -28.924  47.013  1.000 53.443  0 59  TYR HHH CG  1 ? 29 
ATOM   9646  C CD1 . TYR H  2 59  ? 31.350  -29.123  48.219  1.000 54.908  0 59  TYR HHH CD1 1 ? 29 
ATOM   9647  C CD2 . TYR H  2 59  ? 32.458  -27.647  46.725  1.000 51.953  0 59  TYR HHH CD2 1 ? 29 
ATOM   9648  C CE1 . TYR H  2 59  ? 31.236  -28.107  49.152  1.000 56.330  0 59  TYR HHH CE1 1 ? 29 
ATOM   9649  C CE2 . TYR H  2 59  ? 32.305  -26.602  47.629  1.000 51.859  0 59  TYR HHH CE2 1 ? 29 
ATOM   9650  C CZ  . TYR H  2 59  ? 31.677  -26.830  48.840  1.000 54.788  0 59  TYR HHH CZ  1 ? 29 
ATOM   9651  O OH  . TYR H  2 59  ? 31.517  -25.801  49.724  1.000 54.548  0 59  TYR HHH OH  1 ? 29 
ATOM   9652  N N   . TYR H  2 60  ? 32.729  -33.014  45.006  1.000 56.012  0 60  TYR HHH N   1 ? 29 
ATOM   9653  C CA  . TYR H  2 60  ? 32.668  -34.100  44.004  1.000 57.381  0 60  TYR HHH CA  1 ? 29 
ATOM   9654  C C   . TYR H  2 60  ? 31.285  -34.741  44.030  1.000 59.658  0 60  TYR HHH C   1 ? 29 
ATOM   9655  O O   . TYR H  2 60  ? 30.732  -34.938  45.122  1.000 62.232  0 60  TYR HHH O   1 ? 29 
ATOM   9656  C CB  . TYR H  2 60  ? 33.771  -35.115  44.305  1.000 59.766  0 60  TYR HHH CB  1 ? 29 
ATOM   9657  C CG  . TYR H  2 60  ? 35.156  -34.537  44.139  1.000 59.033  0 60  TYR HHH CG  1 ? 29 
ATOM   9658  C CD1 . TYR H  2 60  ? 35.677  -34.308  42.875  1.000 55.602  0 60  TYR HHH CD1 1 ? 29 
ATOM   9659  C CD2 . TYR H  2 60  ? 35.925  -34.173  45.239  1.000 58.973  0 60  TYR HHH CD2 1 ? 29 
ATOM   9660  C CE1 . TYR H  2 60  ? 36.936  -33.763  42.711  1.000 55.489  0 60  TYR HHH CE1 1 ? 29 
ATOM   9661  C CE2 . TYR H  2 60  ? 37.180  -33.609  45.086  1.000 58.158  0 60  TYR HHH CE2 1 ? 29 
ATOM   9662  C CZ  . TYR H  2 60  ? 37.686  -33.416  43.816  1.000 56.446  0 60  TYR HHH CZ  1 ? 29 
ATOM   9663  O OH  . TYR H  2 60  ? 38.924  -32.879  43.638  1.000 59.984  0 60  TYR HHH OH  1 ? 29 
ATOM   9664  N N   . GLY H  2 61  ? 30.749  -35.061  42.852  1.000 61.471  0 61  GLY HHH N   1 ? 29 
ATOM   9665  C CA  . GLY H  2 61  ? 29.569  -35.934  42.705  1.000 63.367  0 61  GLY HHH CA  1 ? 29 
ATOM   9666  C C   . GLY H  2 61  ? 29.866  -37.318  43.232  1.000 66.274  0 61  GLY HHH C   1 ? 29 
ATOM   9667  O O   . GLY H  2 61  ? 31.030  -37.745  43.171  1.000 64.398  0 61  GLY HHH O   1 ? 29 
ATOM   9668  N N   . GLU H  2 62  ? 28.846  -38.001  43.733  1.000 71.687  0 62  GLU HHH N   1 ? 29 
ATOM   9669  C CA  . GLU H  2 62  ? 29.005  -39.296  44.438  1.000 76.393  0 62  GLU HHH CA  1 ? 29 
ATOM   9670  C C   . GLU H  2 62  ? 29.730  -40.280  43.512  1.000 75.389  0 62  GLU HHH C   1 ? 29 
ATOM   9671  O O   . GLU H  2 62  ? 30.624  -40.981  44.004  1.000 78.182  0 62  GLU HHH O   1 ? 29 
ATOM   9672  C CB  . GLU H  2 62  ? 27.639  -39.792  44.916  1.000 80.813  0 62  GLU HHH CB  1 ? 29 
ATOM   9673  C CG  . GLU H  2 62  ? 27.723  -40.974  45.860  1.000 89.859  0 62  GLU HHH CG  1 ? 29 
ATOM   9674  C CD  . GLU H  2 62  ? 28.723  -40.833  47.011  1.000 94.781  0 62  GLU HHH CD  1 ? 29 
ATOM   9675  O OE1 . GLU H  2 62  ? 28.991  -39.679  47.482  1.000 94.289  0 62  GLU HHH OE1 1 ? 29 
ATOM   9676  O OE2 . GLU H  2 62  ? 29.256  -41.873  47.425  1.000 98.333  0 62  GLU HHH OE2 1 ? 29 
ATOM   9677  N N   . SER H  2 63  ? 29.395  -40.303  42.220  1.000 71.011  0 63  SER HHH N   1 ? 29 
ATOM   9678  C CA  . SER H  2 63  ? 29.815  -41.401  41.315  1.000 71.060  0 63  SER HHH CA  1 ? 29 
ATOM   9679  C C   . SER H  2 63  ? 31.238  -41.155  40.811  1.000 68.019  0 63  SER HHH C   1 ? 29 
ATOM   9680  O O   . SER H  2 63  ? 31.793  -42.073  40.231  1.000 71.442  0 63  SER HHH O   1 ? 29 
ATOM   9681  C CB  . SER H  2 63  ? 28.839  -41.590  40.189  1.000 70.816  0 63  SER HHH CB  1 ? 29 
ATOM   9682  O OG  . SER H  2 63  ? 28.765  -40.414  39.390  1.000 70.258  0 63  SER HHH OG  1 ? 29 
ATOM   9683  N N   . VAL H  2 64  ? 31.828  -39.985  41.038  1.000 64.629  0 64  VAL HHH N   1 ? 29 
ATOM   9684  C CA  . VAL H  2 64  ? 33.227  -39.706  40.590  1.000 64.575  0 64  VAL HHH CA  1 ? 29 
ATOM   9685  C C   . VAL H  2 64  ? 34.167  -39.558  41.785  1.000 65.542  0 64  VAL HHH C   1 ? 29 
ATOM   9686  O O   . VAL H  2 64  ? 35.385  -39.525  41.560  1.000 62.780  0 64  VAL HHH O   1 ? 29 
ATOM   9687  C CB  . VAL H  2 64  ? 33.317  -38.478  39.668  1.000 61.759  0 64  VAL HHH CB  1 ? 29 
ATOM   9688  C CG1 . VAL H  2 64  ? 32.410  -38.634  38.458  1.000 61.545  0 64  VAL HHH CG1 1 ? 29 
ATOM   9689  C CG2 . VAL H  2 64  ? 33.021  -37.176  40.402  1.000 60.107  0 64  VAL HHH CG2 1 ? 29 
ATOM   9690  N N   . LYS H  2 65  ? 33.625  -39.460  42.994  1.000 70.060  0 65  LYS HHH N   1 ? 29 
ATOM   9691  C CA  . LYS H  2 65  ? 34.417  -39.294  44.248  1.000 74.457  0 65  LYS HHH CA  1 ? 29 
ATOM   9692  C C   . LYS H  2 65  ? 35.533  -40.337  44.263  1.000 76.264  0 65  LYS HHH C   1 ? 29 
ATOM   9693  O O   . LYS H  2 65  ? 35.234  -41.519  44.009  1.000 79.101  0 65  LYS HHH O   1 ? 29 
ATOM   9694  C CB  . LYS H  2 65  ? 33.518  -39.431  45.485  1.000 78.611  0 65  LYS HHH CB  1 ? 29 
ATOM   9695  C CG  . LYS H  2 65  ? 33.735  -38.397  46.553  1.000 81.661  0 65  LYS HHH CG  1 ? 29 
ATOM   9696  C CD  . LYS H  2 65  ? 32.456  -38.259  47.419  1.000 84.324  0 65  LYS HHH CD  1 ? 29 
ATOM   9697  C CE  . LYS H  2 65  ? 32.610  -37.312  48.588  1.000 85.256  0 65  LYS HHH CE  1 ? 29 
ATOM   9698  N NZ  . LYS H  2 65  ? 32.211  -37.947  49.878  1.000 90.992  0 65  LYS HHH NZ  1 ? 29 
ATOM   9699  N N   . GLY H  2 66  ? 36.778  -39.906  44.476  1.000 76.113  0 66  GLY HHH N   1 ? 29 
ATOM   9700  C CA  . GLY H  2 66  ? 37.965  -40.788  44.530  1.000 79.880  0 66  GLY HHH CA  1 ? 29 
ATOM   9701  C C   . GLY H  2 66  ? 38.682  -40.925  43.195  1.000 80.592  0 66  GLY HHH C   1 ? 29 
ATOM   9702  O O   . GLY H  2 66  ? 39.893  -41.133  43.219  1.000 84.130  0 66  GLY HHH O   1 ? 29 
ATOM   9703  N N   . ARG H  2 67  ? 37.978  -40.800  42.070  1.000 78.500  0 67  ARG HHH N   1 ? 29 
ATOM   9704  C CA  . ARG H  2 67  ? 38.546  -41.057  40.715  1.000 77.892  0 67  ARG HHH CA  1 ? 29 
ATOM   9705  C C   . ARG H  2 67  ? 38.936  -39.741  40.033  1.000 74.579  0 67  ARG HHH C   1 ? 29 
ATOM   9706  O O   . ARG H  2 67  ? 39.884  -39.752  39.220  1.000 77.266  0 67  ARG HHH O   1 ? 29 
ATOM   9707  C CB  . ARG H  2 67  ? 37.537  -41.811  39.840  1.000 78.522  0 67  ARG HHH CB  1 ? 29 
ATOM   9708  C CG  . ARG H  2 67  ? 37.114  -43.156  40.408  1.000 83.294  0 67  ARG HHH CG  1 ? 29 
ATOM   9709  C CD  . ARG H  2 67  ? 36.310  -43.968  39.425  1.000 84.862  0 67  ARG HHH CD  1 ? 29 
ATOM   9710  N NE  . ARG H  2 67  ? 35.043  -43.314  39.120  1.000 82.369  0 67  ARG HHH NE  1 ? 29 
ATOM   9711  C CZ  . ARG H  2 67  ? 34.655  -42.886  37.921  1.000 78.500  0 67  ARG HHH CZ  1 ? 29 
ATOM   9712  N NH1 . ARG H  2 67  ? 35.428  -43.052  36.874  1.000 78.461  0 67  ARG HHH NH1 1 ? 29 
ATOM   9713  N NH2 . ARG H  2 67  ? 33.463  -42.349  37.769  1.000 76.434  0 67  ARG HHH NH2 1 ? 29 
ATOM   9714  N N   . PHE H  2 68  ? 38.223  -38.644  40.330  1.000 69.315  0 68  PHE HHH N   1 ? 29 
ATOM   9715  C CA  . PHE H  2 68  ? 38.386  -37.332  39.662  1.000 63.843  0 68  PHE HHH CA  1 ? 29 
ATOM   9716  C C   . PHE H  2 68  ? 38.983  -36.330  40.654  1.000 62.140  0 68  PHE HHH C   1 ? 29 
ATOM   9717  O O   . PHE H  2 68  ? 38.633  -36.356  41.835  1.000 64.403  0 68  PHE HHH O   1 ? 29 
ATOM   9718  C CB  . PHE H  2 68  ? 37.036  -36.844  39.134  1.000 62.712  0 68  PHE HHH CB  1 ? 29 
ATOM   9719  C CG  . PHE H  2 68  ? 36.459  -37.563  37.938  1.000 63.449  0 68  PHE HHH CG  1 ? 29 
ATOM   9720  C CD1 . PHE H  2 68  ? 36.956  -38.782  37.493  1.000 65.993  0 68  PHE HHH CD1 1 ? 29 
ATOM   9721  C CD2 . PHE H  2 68  ? 35.359  -37.034  37.282  1.000 62.060  0 68  PHE HHH CD2 1 ? 29 
ATOM   9722  C CE1 . PHE H  2 68  ? 36.382  -39.429  36.410  1.000 67.101  0 68  PHE HHH CE1 1 ? 29 
ATOM   9723  C CE2 . PHE H  2 68  ? 34.792  -37.687  36.200  1.000 64.465  0 68  PHE HHH CE2 1 ? 29 
ATOM   9724  C CZ  . PHE H  2 68  ? 35.306  -38.879  35.766  1.000 65.881  0 68  PHE HHH CZ  1 ? 29 
ATOM   9725  N N   . THR H  2 69  ? 39.868  -35.461  40.185  1.000 60.810  0 69  THR HHH N   1 ? 29 
ATOM   9726  C CA  . THR H  2 69  ? 40.481  -34.379  40.995  1.000 60.641  0 69  THR HHH CA  1 ? 29 
ATOM   9727  C C   . THR H  2 69  ? 40.281  -33.059  40.255  1.000 58.134  0 69  THR HHH C   1 ? 29 
ATOM   9728  O O   . THR H  2 69  ? 40.705  -32.964  39.084  1.000 56.602  0 69  THR HHH O   1 ? 29 
ATOM   9729  C CB  . THR H  2 69  ? 41.967  -34.636  41.258  1.000 61.842  0 69  THR HHH CB  1 ? 29 
ATOM   9730  O OG1 . THR H  2 69  ? 42.073  -35.910  41.873  1.000 63.525  0 69  THR HHH OG1 1 ? 29 
ATOM   9731  C CG2 . THR H  2 69  ? 42.587  -33.591  42.149  1.000 61.316  0 69  THR HHH CG2 1 ? 29 
ATOM   9732  N N   . ILE H  2 70  ? 39.635  -32.099  40.911  1.000 55.852  0 70  ILE HHH N   1 ? 29 
ATOM   9733  C CA  . ILE H  2 70  ? 39.498  -30.715  40.383  1.000 54.973  0 70  ILE HHH CA  1 ? 29 
ATOM   9734  C C   . ILE H  2 70  ? 40.621  -29.886  41.001  1.000 54.964  0 70  ILE HHH C   1 ? 29 
ATOM   9735  O O   . ILE H  2 70  ? 40.977  -30.141  42.157  1.000 59.107  0 70  ILE HHH O   1 ? 29 
ATOM   9736  C CB  . ILE H  2 70  ? 38.092  -30.138  40.649  1.000 54.038  0 70  ILE HHH CB  1 ? 29 
ATOM   9737  C CG1 . ILE H  2 70  ? 37.853  -28.882  39.807  1.000 53.775  0 70  ILE HHH CG1 1 ? 29 
ATOM   9738  C CG2 . ILE H  2 70  ? 37.859  -29.904  42.136  1.000 54.906  0 70  ILE HHH CG2 1 ? 29 
ATOM   9739  C CD1 . ILE H  2 70  ? 36.443  -28.346  39.871  1.000 51.700  0 70  ILE HHH CD1 1 ? 29 
ATOM   9740  N N   . SER H  2 71  ? 41.190  -28.965  40.230  1.000 52.129  0 71  SER HHH N   1 ? 29 
ATOM   9741  C CA  . SER H  2 71  ? 42.276  -28.056  40.666  1.000 52.745  0 71  SER HHH CA  1 ? 29 
ATOM   9742  C C   . SER H  2 71  ? 42.196  -26.782  39.835  1.000 51.619  0 71  SER HHH C   1 ? 29 
ATOM   9743  O O   . SER H  2 71  ? 41.496  -26.790  38.794  1.000 53.892  0 71  SER HHH O   1 ? 29 
ATOM   9744  C CB  . SER H  2 71  ? 43.626  -28.728  40.563  1.000 54.722  0 71  SER HHH CB  1 ? 29 
ATOM   9745  O OG  . SER H  2 71  ? 43.920  -29.091  39.221  1.000 55.215  0 71  SER HHH OG  1 ? 29 
ATOM   9746  N N   . ARG H  2 72  ? 42.836  -25.710  40.293  1.000 50.946  0 72  ARG HHH N   1 ? 29 
ATOM   9747  C CA  . ARG H  2 72  ? 42.796  -24.409  39.585  1.000 49.754  0 72  ARG HHH CA  1 ? 29 
ATOM   9748  C C   . ARG H  2 72  ? 44.192  -23.813  39.591  1.000 51.181  0 72  ARG HHH C   1 ? 29 
ATOM   9749  O O   . ARG H  2 72  ? 44.928  -24.075  40.526  1.000 56.248  0 72  ARG HHH O   1 ? 29 
ATOM   9750  C CB  . ARG H  2 72  ? 41.756  -23.473  40.209  1.000 48.930  0 72  ARG HHH CB  1 ? 29 
ATOM   9751  C CG  . ARG H  2 72  ? 42.018  -23.102  41.651  1.000 49.696  0 72  ARG HHH CG  1 ? 29 
ATOM   9752  C CD  . ARG H  2 72  ? 40.882  -22.300  42.263  1.000 49.383  0 72  ARG HHH CD  1 ? 29 
ATOM   9753  N NE  . ARG H  2 72  ? 40.608  -21.071  41.533  1.000 48.754  0 72  ARG HHH NE  1 ? 29 
ATOM   9754  C CZ  . ARG H  2 72  ? 39.414  -20.487  41.436  1.000 49.255  0 72  ARG HHH CZ  1 ? 29 
ATOM   9755  N NH1 . ARG H  2 72  ? 38.356  -21.005  42.030  1.000 50.098  0 72  ARG HHH NH1 1 ? 29 
ATOM   9756  N NH2 . ARG H  2 72  ? 39.277  -19.378  40.749  1.000 48.697  0 72  ARG HHH NH2 1 ? 29 
ATOM   9757  N N   . ASP H  2 73  ? 44.532  -23.086  38.537  1.000 52.574  0 73  ASP HHH N   1 ? 29 
ATOM   9758  C CA  . ASP H  2 73  ? 45.788  -22.309  38.404  1.000 53.492  0 73  ASP HHH CA  1 ? 29 
ATOM   9759  C C   . ASP H  2 73  ? 45.366  -20.883  38.046  1.000 52.058  0 73  ASP HHH C   1 ? 29 
ATOM   9760  O O   . ASP H  2 73  ? 45.042  -20.614  36.860  1.000 50.406  0 73  ASP HHH O   1 ? 29 
ATOM   9761  C CB  . ASP H  2 73  ? 46.708  -22.965  37.379  1.000 56.256  0 73  ASP HHH CB  1 ? 29 
ATOM   9762  C CG  . ASP H  2 73  ? 48.017  -22.211  37.177  1.000 60.210  0 73  ASP HHH CG  1 ? 29 
ATOM   9763  O OD1 . ASP H  2 73  ? 48.147  -21.085  37.736  1.000 61.890  0 73  ASP HHH OD1 1 ? 29 
ATOM   9764  O OD2 . ASP H  2 73  ? 48.896  -22.744  36.471  1.000 62.721  0 73  ASP HHH OD2 1 ? 29 
ATOM   9765  N N   . ASN H  2 74  ? 45.298  -20.025  39.062  1.000 50.877  0 74  ASN HHH N   1 ? 29 
ATOM   9766  C CA  . ASN H  2 74  ? 44.785  -18.639  38.924  1.000 47.833  0 74  ASN HHH CA  1 ? 29 
ATOM   9767  C C   . ASN H  2 74  ? 45.665  -17.862  37.936  1.000 47.591  0 74  ASN HHH C   1 ? 29 
ATOM   9768  O O   . ASN H  2 74  ? 45.116  -17.083  37.167  1.000 44.493  0 74  ASN HHH O   1 ? 29 
ATOM   9769  C CB  . ASN H  2 74  ? 44.643  -18.003  40.297  1.000 47.683  0 74  ASN HHH CB  1 ? 29 
ATOM   9770  C CG  . ASN H  2 74  ? 43.422  -18.519  41.045  1.000 48.352  0 74  ASN HHH CG  1 ? 29 
ATOM   9771  O OD1 . ASN H  2 74  ? 42.649  -19.358  40.566  1.000 45.377  0 74  ASN HHH OD1 1 ? 29 
ATOM   9772  N ND2 . ASN H  2 74  ? 43.222  -18.011  42.248  1.000 49.976  0 74  ASN HHH ND2 1 ? 29 
ATOM   9773  N N   . ALA H  2 75  ? 46.974  -18.121  37.889  1.000 50.360  0 75  ALA HHH N   1 ? 29 
ATOM   9774  C CA  . ALA H  2 75  ? 47.917  -17.425  36.976  1.000 52.176  0 75  ALA HHH CA  1 ? 29 
ATOM   9775  C C   . ALA H  2 75  ? 47.535  -17.694  35.511  1.000 52.729  0 75  ALA HHH C   1 ? 29 
ATOM   9776  O O   . ALA H  2 75  ? 47.864  -16.856  34.667  1.000 54.756  0 75  ALA HHH O   1 ? 29 
ATOM   9777  C CB  . ALA H  2 75  ? 49.331  -17.817  37.268  1.000 53.917  0 75  ALA HHH CB  1 ? 29 
ATOM   9778  N N   . LYS H  2 76  ? 46.846  -18.797  35.218  1.000 53.255  0 76  LYS HHH N   1 ? 29 
ATOM   9779  C CA  . LYS H  2 76  ? 46.462  -19.188  33.834  1.000 53.820  0 76  LYS HHH CA  1 ? 29 
ATOM   9780  C C   . LYS H  2 76  ? 44.951  -19.150  33.636  1.000 50.633  0 76  LYS HHH C   1 ? 29 
ATOM   9781  O O   . LYS H  2 76  ? 44.506  -19.648  32.604  1.000 51.579  0 76  LYS HHH O   1 ? 29 
ATOM   9782  C CB  . LYS H  2 76  ? 46.950  -20.600  33.534  1.000 56.319  0 76  LYS HHH CB  1 ? 29 
ATOM   9783  C CG  . LYS H  2 76  ? 48.445  -20.760  33.677  1.000 61.741  0 76  LYS HHH CG  1 ? 29 
ATOM   9784  C CD  . LYS H  2 76  ? 49.019  -21.984  33.046  1.000 65.468  0 76  LYS HHH CD  1 ? 29 
ATOM   9785  C CE  . LYS H  2 76  ? 50.529  -21.900  33.119  1.000 72.653  0 76  LYS HHH CE  1 ? 29 
ATOM   9786  N NZ  . LYS H  2 76  ? 51.180  -23.200  32.832  1.000 77.663  0 76  LYS HHH NZ  1 ? 29 
ATOM   9787  N N   . ASN H  2 77  ? 44.189  -18.601  34.577  1.000 49.939  0 77  ASN HHH N   1 ? 29 
ATOM   9788  C CA  . ASN H  2 77  ? 42.711  -18.495  34.445  1.000 48.211  0 77  ASN HHH CA  1 ? 29 
ATOM   9789  C C   . ASN H  2 77  ? 42.117  -19.873  34.119  1.000 48.052  0 77  ASN HHH C   1 ? 29 
ATOM   9790  O O   . ASN H  2 77  ? 41.154  -19.936  33.340  1.000 46.207  0 77  ASN HHH O   1 ? 29 
ATOM   9791  C CB  . ASN H  2 77  ? 42.351  -17.498  33.336  1.000 46.534  0 77  ASN HHH CB  1 ? 29 
ATOM   9792  C CG  . ASN H  2 77  ? 42.226  -16.082  33.848  1.000 45.529  0 77  ASN HHH CG  1 ? 29 
ATOM   9793  O OD1 . ASN H  2 77  ? 42.993  -15.651  34.702  1.000 43.927  0 77  ASN HHH OD1 1 ? 29 
ATOM   9794  N ND2 . ASN H  2 77  ? 41.258  -15.356  33.329  1.000 43.734  0 77  ASN HHH ND2 1 ? 29 
ATOM   9795  N N   . THR H  2 78  ? 42.685  -20.945  34.664  1.000 47.725  0 78  THR HHH N   1 ? 29 
ATOM   9796  C CA  . THR H  2 78  ? 42.333  -22.318  34.242  1.000 46.754  0 78  THR HHH CA  1 ? 29 
ATOM   9797  C C   . THR H  2 78  ? 41.929  -23.164  35.451  1.000 48.441  0 78  THR HHH C   1 ? 29 
ATOM   9798  O O   . THR H  2 78  ? 42.606  -23.109  36.514  1.000 50.526  0 78  THR HHH O   1 ? 29 
ATOM   9799  C CB  . THR H  2 78  ? 43.464  -22.927  33.408  1.000 47.054  0 78  THR HHH CB  1 ? 29 
ATOM   9800  O OG1 . THR H  2 78  ? 43.651  -22.113  32.251  1.000 44.802  0 78  THR HHH OG1 1 ? 29 
ATOM   9801  C CG2 . THR H  2 78  ? 43.171  -24.344  32.987  1.000 47.538  0 78  THR HHH CG2 1 ? 29 
ATOM   9802  N N   . VAL H  2 79  ? 40.829  -23.901  35.272  1.000 48.418  0 79  VAL HHH N   1 ? 29 
ATOM   9803  C CA  . VAL H  2 79  ? 40.388  -25.007  36.163  1.000 48.354  0 79  VAL HHH CA  1 ? 29 
ATOM   9804  C C   . VAL H  2 79  ? 40.617  -26.322  35.407  1.000 49.497  0 79  VAL HHH C   1 ? 29 
ATOM   9805  O O   . VAL H  2 79  ? 40.417  -26.359  34.175  1.000 48.241  0 79  VAL HHH O   1 ? 29 
ATOM   9806  C CB  . VAL H  2 79  ? 38.931  -24.807  36.608  1.000 47.442  0 79  VAL HHH CB  1 ? 29 
ATOM   9807  C CG1 . VAL H  2 79  ? 37.973  -24.779  35.438  1.000 47.158  0 79  VAL HHH CG1 1 ? 29 
ATOM   9808  C CG2 . VAL H  2 79  ? 38.504  -25.858  37.620  1.000 49.644  0 79  VAL HHH CG2 1 ? 29 
ATOM   9809  N N   . TYR H  2 80  ? 41.087  -27.351  36.110  1.000 50.711  0 80  TYR HHH N   1 ? 29 
ATOM   9810  C CA  . TYR H  2 80  ? 41.418  -28.683  35.542  1.000 52.196  0 80  TYR HHH CA  1 ? 29 
ATOM   9811  C C   . TYR H  2 80  ? 40.509  -29.747  36.160  1.000 52.205  0 80  TYR HHH C   1 ? 29 
ATOM   9812  O O   . TYR H  2 80  ? 40.109  -29.613  37.325  1.000 49.980  0 80  TYR HHH O   1 ? 29 
ATOM   9813  C CB  . TYR H  2 80  ? 42.884  -29.015  35.804  1.000 53.769  0 80  TYR HHH CB  1 ? 29 
ATOM   9814  C CG  . TYR H  2 80  ? 43.857  -28.066  35.160  1.000 55.001  0 80  TYR HHH CG  1 ? 29 
ATOM   9815  C CD1 . TYR H  2 80  ? 44.159  -28.158  33.811  1.000 55.406  0 80  TYR HHH CD1 1 ? 29 
ATOM   9816  C CD2 . TYR H  2 80  ? 44.483  -27.078  35.902  1.000 55.614  0 80  TYR HHH CD2 1 ? 29 
ATOM   9817  C CE1 . TYR H  2 80  ? 45.073  -27.305  33.213  1.000 55.944  0 80  TYR HHH CE1 1 ? 29 
ATOM   9818  C CE2 . TYR H  2 80  ? 45.407  -26.215  35.325  1.000 55.335  0 80  TYR HHH CE2 1 ? 29 
ATOM   9819  C CZ  . TYR H  2 80  ? 45.682  -26.320  33.975  1.000 57.159  0 80  TYR HHH CZ  1 ? 29 
ATOM   9820  O OH  . TYR H  2 80  ? 46.559  -25.454  33.401  1.000 60.717  0 80  TYR HHH OH  1 ? 29 
ATOM   9821  N N   . LEU H  2 81  ? 40.190  -30.778  35.379  1.000 54.746  0 81  LEU HHH N   1 ? 29 
ATOM   9822  C CA  . LEU H  2 81  ? 39.549  -32.020  35.885  1.000 56.387  0 81  LEU HHH CA  1 ? 29 
ATOM   9823  C C   . LEU H  2 81  ? 40.405  -33.219  35.458  1.000 59.167  0 81  LEU HHH C   1 ? 29 
ATOM   9824  O O   . LEU H  2 81  ? 40.377  -33.565  34.267  1.000 61.225  0 81  LEU HHH O   1 ? 29 
ATOM   9825  C CB  . LEU H  2 81  ? 38.105  -32.118  35.378  1.000 54.474  0 81  LEU HHH CB  1 ? 29 
ATOM   9826  C CG  . LEU H  2 81  ? 37.259  -33.192  36.062  1.000 55.902  0 81  LEU HHH CG  1 ? 29 
ATOM   9827  C CD1 . LEU H  2 81  ? 36.979  -32.827  37.509  1.000 54.820  0 81  LEU HHH CD1 1 ? 29 
ATOM   9828  C CD2 . LEU H  2 81  ? 35.957  -33.429  35.308  1.000 56.606  0 81  LEU HHH CD2 1 ? 29 
ATOM   9829  N N   . GLN H  2 82  ? 41.163  -33.781  36.405  1.000 60.899  0 82  GLN HHH N   1 ? 29 
ATOM   9830  C CA  . GLN H  2 82  ? 41.922  -35.040  36.250  1.000 63.982  0 82  GLN HHH CA  1 ? 29 
ATOM   9831  C C   . GLN H  2 82  ? 40.899  -36.161  36.415  1.000 66.009  0 82  GLN HHH C   1 ? 29 
ATOM   9832  O O   . GLN H  2 82  ? 40.258  -36.214  37.475  1.000 67.799  0 82  GLN HHH O   1 ? 29 
ATOM   9833  C CB  . GLN H  2 82  ? 43.065  -35.097  37.271  1.000 64.828  0 82  GLN HHH CB  1 ? 29 
ATOM   9834  C CG  . GLN H  2 82  ? 44.028  -36.250  37.058  1.000 68.821  0 82  GLN HHH CG  1 ? 29 
ATOM   9835  C CD  . GLN H  2 82  ? 44.574  -36.296  35.649  1.000 69.754  0 82  GLN HHH CD  1 ? 29 
ATOM   9836  O OE1 . GLN H  2 82  ? 45.060  -35.299  35.127  1.000 66.078  0 82  GLN HHH OE1 1 ? 29 
ATOM   9837  N NE2 . GLN H  2 82  ? 44.494  -37.466  35.025  1.000 72.799  0 82  GLN HHH NE2 1 ? 29 
ATOM   9838  N N   . MET H  2 83  ? 40.667  -36.948  35.369  1.000 66.048  0 83  MET HHH N   1 ? 29 
ATOM   9839  C CA  . MET H  2 83  ? 39.699  -38.070  35.400  1.000 66.604  0 83  MET HHH CA  1 ? 29 
ATOM   9840  C C   . MET H  2 83  ? 40.499  -39.356  35.270  1.000 67.396  0 83  MET HHH C   1 ? 29 
ATOM   9841  O O   . MET H  2 83  ? 41.086  -39.563  34.210  1.000 68.307  0 83  MET HHH O   1 ? 29 
ATOM   9842  C CB  . MET H  2 83  ? 38.666  -37.959  34.267  1.000 66.547  0 83  MET HHH CB  1 ? 29 
ATOM   9843  C CG  . MET H  2 83  ? 37.941  -36.620  34.211  1.000 64.412  0 83  MET HHH CG  1 ? 29 
ATOM   9844  S SD  . MET H  2 83  ? 36.700  -36.551  32.877  1.000 67.434  0 83  MET HHH SD  1 ? 29 
ATOM   9845  C CE  . MET H  2 83  ? 37.762  -36.487  31.446  1.000 70.392  0 83  MET HHH CE  1 ? 29 
ATOM   9846  N N   . ASN H  2 84  ? 40.553  -40.149  36.336  1.000 70.589  0 84  ASN HHH N   1 ? 29 
ATOM   9847  C CA  . ASN H  2 84  ? 41.281  -41.443  36.383  1.000 75.030  0 84  ASN HHH CA  1 ? 29 
ATOM   9848  C C   . ASN H  2 84  ? 40.270  -42.594  36.380  1.000 77.128  0 84  ASN HHH C   1 ? 29 
ATOM   9849  O O   . ASN H  2 84  ? 39.102  -42.371  36.752  1.000 72.481  0 84  ASN HHH O   1 ? 29 
ATOM   9850  C CB  . ASN H  2 84  ? 42.240  -41.500  37.572  1.000 76.205  0 84  ASN HHH CB  1 ? 29 
ATOM   9851  C CG  . ASN H  2 84  ? 43.322  -40.444  37.480  1.000 76.135  0 84  ASN HHH CG  1 ? 29 
ATOM   9852  O OD1 . ASN H  2 84  ? 43.801  -40.129  36.390  1.000 76.172  0 84  ASN HHH OD1 1 ? 29 
ATOM   9853  N ND2 . ASN H  2 84  ? 43.712  -39.880  38.612  1.000 76.595  0 84  ASN HHH ND2 1 ? 29 
ATOM   9854  N N   . ARG H  2 85  ? 40.719  -43.777  35.939  1.000 82.328  0 85  ARG HHH N   1 ? 29 
ATOM   9855  C CA  . ARG H  2 85  ? 39.948  -45.040  36.028  1.000 84.909  0 85  ARG HHH CA  1 ? 29 
ATOM   9856  C C   . ARG H  2 85  ? 38.552  -44.777  35.445  1.000 80.435  0 85  ARG HHH C   1 ? 29 
ATOM   9857  O O   . ARG H  2 85  ? 37.544  -45.025  36.123  1.000 78.849  0 85  ARG HHH O   1 ? 29 
ATOM   9858  C CB  . ARG H  2 85  ? 39.986  -45.535  37.475  1.000 89.228  0 85  ARG HHH CB  1 ? 29 
ATOM   9859  C CG  . ARG H  2 85  ? 41.408  -45.773  37.983  1.000 94.929  0 85  ARG HHH CG  1 ? 29 
ATOM   9860  C CD  . ARG H  2 85  ? 41.609  -46.574  39.256  1.000 101.263 0 85  ARG HHH CD  1 ? 29 
ATOM   9861  N NE  . ARG H  2 85  ? 40.618  -46.299  40.289  1.000 102.612 0 85  ARG HHH NE  1 ? 29 
ATOM   9862  C CZ  . ARG H  2 85  ? 40.484  -45.150  40.965  1.000 100.705 0 85  ARG HHH CZ  1 ? 29 
ATOM   9863  N NH1 . ARG H  2 85  ? 41.280  -44.115  40.730  1.000 99.587  0 85  ARG HHH NH1 1 ? 29 
ATOM   9864  N NH2 . ARG H  2 85  ? 39.519  -45.036  41.864  1.000 99.388  0 85  ARG HHH NH2 1 ? 29 
ATOM   9865  N N   . LEU H  2 86  ? 38.516  -44.271  34.214  1.000 77.603  0 86  LEU HHH N   1 ? 29 
ATOM   9866  C CA  . LEU H  2 86  ? 37.271  -43.893  33.510  1.000 75.303  0 86  LEU HHH CA  1 ? 29 
ATOM   9867  C C   . LEU H  2 86  ? 36.455  -45.142  33.185  1.000 78.360  0 86  LEU HHH C   1 ? 29 
ATOM   9868  O O   . LEU H  2 86  ? 37.053  -46.157  32.794  1.000 84.723  0 86  LEU HHH O   1 ? 29 
ATOM   9869  C CB  . LEU H  2 86  ? 37.639  -43.105  32.250  1.000 74.279  0 86  LEU HHH CB  1 ? 29 
ATOM   9870  C CG  . LEU H  2 86  ? 38.028  -41.651  32.508  1.000 70.778  0 86  LEU HHH CG  1 ? 29 
ATOM   9871  C CD1 . LEU H  2 86  ? 38.725  -41.038  31.321  1.000 69.905  0 86  LEU HHH CD1 1 ? 29 
ATOM   9872  C CD2 . LEU H  2 86  ? 36.814  -40.822  32.860  1.000 67.442  0 86  LEU HHH CD2 1 ? 29 
ATOM   9873  N N   . LYS H  2 87  ? 35.136  -45.042  33.329  1.000 76.656  0 87  LYS HHH N   1 ? 29 
ATOM   9874  C CA  . LYS H  2 87  ? 34.148  -46.116  33.047  1.000 79.559  0 87  LYS HHH CA  1 ? 29 
ATOM   9875  C C   . LYS H  2 87  ? 33.237  -45.632  31.929  1.000 77.805  0 87  LYS HHH C   1 ? 29 
ATOM   9876  O O   . LYS H  2 87  ? 33.120  -44.434  31.708  1.000 75.403  0 87  LYS HHH O   1 ? 29 
ATOM   9877  C CB  . LYS H  2 87  ? 33.344  -46.436  34.310  1.000 81.239  0 87  LYS HHH CB  1 ? 29 
ATOM   9878  C CG  . LYS H  2 87  ? 34.165  -46.449  35.592  1.000 82.502  0 87  LYS HHH CG  1 ? 29 
ATOM   9879  C CD  . LYS H  2 87  ? 33.383  -46.566  36.881  1.000 83.337  0 87  LYS HHH CD  1 ? 29 
ATOM   9880  C CE  . LYS H  2 87  ? 34.338  -46.857  38.019  1.000 86.138  0 87  LYS HHH CE  1 ? 29 
ATOM   9881  N NZ  . LYS H  2 87  ? 33.651  -47.042  39.321  1.000 88.734  0 87  LYS HHH NZ  1 ? 29 
ATOM   9882  N N   . PRO H  2 88  ? 32.598  -46.536  31.155  1.000 81.586  0 88  PRO HHH N   1 ? 29 
ATOM   9883  C CA  . PRO H  2 88  ? 31.645  -46.130  30.121  1.000 81.365  0 88  PRO HHH CA  1 ? 29 
ATOM   9884  C C   . PRO H  2 88  ? 30.585  -45.118  30.579  1.000 78.360  0 88  PRO HHH C   1 ? 29 
ATOM   9885  O O   . PRO H  2 88  ? 30.286  -44.239  29.809  1.000 76.958  0 88  PRO HHH O   1 ? 29 
ATOM   9886  C CB  . PRO H  2 88  ? 31.033  -47.470  29.697  1.000 84.894  0 88  PRO HHH CB  1 ? 29 
ATOM   9887  C CG  . PRO H  2 88  ? 32.212  -48.402  29.810  1.000 87.420  0 88  PRO HHH CG  1 ? 29 
ATOM   9888  C CD  . PRO H  2 88  ? 32.849  -47.986  31.123  1.000 86.105  0 88  PRO HHH CD  1 ? 29 
ATOM   9889  N N   . GLU H  2 89  ? 30.106  -45.225  31.821  1.000 78.198  0 89  GLU HHH N   1 ? 29 
ATOM   9890  C CA  . GLU H  2 89  ? 29.069  -44.346  32.435  1.000 76.202  0 89  GLU HHH CA  1 ? 29 
ATOM   9891  C C   . GLU H  2 89  ? 29.584  -42.910  32.577  1.000 71.362  0 89  GLU HHH C   1 ? 29 
ATOM   9892  O O   . GLU H  2 89  ? 28.786  -42.056  32.985  1.000 69.115  0 89  GLU HHH O   1 ? 29 
ATOM   9893  C CB  . GLU H  2 89  ? 28.669  -44.811  33.839  1.000 79.583  0 89  GLU HHH CB  1 ? 29 
ATOM   9894  C CG  . GLU H  2 89  ? 28.277  -46.277  33.929  1.000 87.273  0 89  GLU HHH CG  1 ? 29 
ATOM   9895  C CD  . GLU H  2 89  ? 29.442  -47.244  34.130  1.000 92.350  0 89  GLU HHH CD  1 ? 29 
ATOM   9896  O OE1 . GLU H  2 89  ? 30.304  -46.926  34.997  1.000 97.030  0 89  GLU HHH OE1 1 ? 29 
ATOM   9897  O OE2 . GLU H  2 89  ? 29.486  -48.302  33.433  1.000 92.112  0 89  GLU HHH OE2 1 ? 29 
ATOM   9898  N N   . ASP H  2 90  ? 30.879  -42.660  32.350  1.000 69.909  0 90  ASP HHH N   1 ? 29 
ATOM   9899  C CA  . ASP H  2 90  ? 31.495  -41.305  32.411  1.000 65.681  0 90  ASP HHH CA  1 ? 29 
ATOM   9900  C C   . ASP H  2 90  ? 31.355  -40.596  31.055  1.000 64.242  0 90  ASP HHH C   1 ? 29 
ATOM   9901  O O   . ASP H  2 90  ? 31.618  -39.393  30.995  1.000 61.764  0 90  ASP HHH O   1 ? 29 
ATOM   9902  C CB  . ASP H  2 90  ? 32.964  -41.367  32.833  1.000 65.528  0 90  ASP HHH CB  1 ? 29 
ATOM   9903  C CG  . ASP H  2 90  ? 33.172  -41.858  34.266  1.000 66.433  0 90  ASP HHH CG  1 ? 29 
ATOM   9904  O OD1 . ASP H  2 90  ? 32.423  -41.418  35.167  1.000 65.431  0 90  ASP HHH OD1 1 ? 29 
ATOM   9905  O OD2 . ASP H  2 90  ? 34.089  -42.671  34.469  1.000 67.099  0 90  ASP HHH OD2 1 ? 29 
ATOM   9906  N N   . THR H  2 91  ? 30.972  -41.321  30.005  1.000 65.769  0 91  THR HHH N   1 ? 29 
ATOM   9907  C CA  . THR H  2 91  ? 30.760  -40.757  28.650  1.000 65.820  0 91  THR HHH CA  1 ? 29 
ATOM   9908  C C   . THR H  2 91  ? 29.677  -39.684  28.719  1.000 63.729  0 91  THR HHH C   1 ? 29 
ATOM   9909  O O   . THR H  2 91  ? 28.586  -39.995  29.190  1.000 64.897  0 91  THR HHH O   1 ? 29 
ATOM   9910  C CB  . THR H  2 91  ? 30.395  -41.848  27.641  1.000 69.479  0 91  THR HHH CB  1 ? 29 
ATOM   9911  O OG1 . THR H  2 91  ? 31.535  -42.693  27.534  1.000 70.901  0 91  THR HHH OG1 1 ? 29 
ATOM   9912  C CG2 . THR H  2 91  ? 30.031  -41.293  26.282  1.000 69.798  0 91  THR HHH CG2 1 ? 29 
ATOM   9913  N N   . ALA H  2 92  ? 29.978  -38.469  28.267  1.000 61.764  0 92  ALA HHH N   1 ? 29 
ATOM   9914  C CA  . ALA H  2 92  ? 29.042  -37.318  28.265  1.000 60.720  0 92  ALA HHH CA  1 ? 29 
ATOM   9915  C C   . ALA H  2 92  ? 29.744  -36.084  27.703  1.000 60.623  0 92  ALA HHH C   1 ? 29 
ATOM   9916  O O   . ALA H  2 92  ? 30.970  -36.123  27.465  1.000 64.699  0 92  ALA HHH O   1 ? 29 
ATOM   9917  C CB  . ALA H  2 92  ? 28.573  -37.029  29.664  1.000 59.257  0 92  ALA HHH CB  1 ? 29 
ATOM   9918  N N   . VAL H  2 93  ? 28.977  -35.019  27.506  1.000 59.844  0 93  VAL HHH N   1 ? 29 
ATOM   9919  C CA  . VAL H  2 93  ? 29.499  -33.648  27.287  1.000 55.825  0 93  VAL HHH CA  1 ? 29 
ATOM   9920  C C   . VAL H  2 93  ? 29.827  -33.105  28.669  1.000 53.421  0 93  VAL HHH C   1 ? 29 
ATOM   9921  O O   . VAL H  2 93  ? 28.963  -33.177  29.562  1.000 54.324  0 93  VAL HHH O   1 ? 29 
ATOM   9922  C CB  . VAL H  2 93  ? 28.482  -32.775  26.534  1.000 55.892  0 93  VAL HHH CB  1 ? 29 
ATOM   9923  C CG1 . VAL H  2 93  ? 28.920  -31.325  26.449  1.000 54.536  0 93  VAL HHH CG1 1 ? 29 
ATOM   9924  C CG2 . VAL H  2 93  ? 28.182  -33.346  25.156  1.000 57.022  0 93  VAL HHH CG2 1 ? 29 
ATOM   9925  N N   . TYR H  2 94  ? 31.049  -32.621  28.842  1.000 53.119  0 94  TYR HHH N   1 ? 29 
ATOM   9926  C CA  . TYR H  2 94  ? 31.552  -32.022  30.103  1.000 51.760  0 94  TYR HHH CA  1 ? 29 
ATOM   9927  C C   . TYR H  2 94  ? 31.551  -30.506  29.927  1.000 51.647  0 94  TYR HHH C   1 ? 29 
ATOM   9928  O O   . TYR H  2 94  ? 32.142  -30.019  28.954  1.000 51.366  0 94  TYR HHH O   1 ? 29 
ATOM   9929  C CB  . TYR H  2 94  ? 32.919  -32.600  30.477  1.000 51.855  0 94  TYR HHH CB  1 ? 29 
ATOM   9930  C CG  . TYR H  2 94  ? 32.840  -33.985  31.073  1.000 53.387  0 94  TYR HHH CG  1 ? 29 
ATOM   9931  C CD1 . TYR H  2 94  ? 32.550  -35.090  30.290  1.000 57.000  0 94  TYR HHH CD1 1 ? 29 
ATOM   9932  C CD2 . TYR H  2 94  ? 33.015  -34.190  32.429  1.000 53.115  0 94  TYR HHH CD2 1 ? 29 
ATOM   9933  C CE1 . TYR H  2 94  ? 32.449  -36.361  30.833  1.000 59.695  0 94  TYR HHH CE1 1 ? 29 
ATOM   9934  C CE2 . TYR H  2 94  ? 32.932  -35.451  32.990  1.000 55.405  0 94  TYR HHH CE2 1 ? 29 
ATOM   9935  C CZ  . TYR H  2 94  ? 32.660  -36.542  32.192  1.000 59.716  0 94  TYR HHH CZ  1 ? 29 
ATOM   9936  O OH  . TYR H  2 94  ? 32.587  -37.777  32.768  1.000 63.359  0 94  TYR HHH OH  1 ? 29 
ATOM   9937  N N   . PHE H  2 95  ? 30.826  -29.818  30.813  1.000 50.078  0 95  PHE HHH N   1 ? 29 
ATOM   9938  C CA  . PHE H  2 95  ? 30.666  -28.343  30.840  1.000 46.798  0 95  PHE HHH CA  1 ? 29 
ATOM   9939  C C   . PHE H  2 95  ? 31.455  -27.746  31.999  1.000 46.372  0 95  PHE HHH C   1 ? 29 
ATOM   9940  O O   . PHE H  2 95  ? 31.344  -28.183  33.153  1.000 44.978  0 95  PHE HHH O   1 ? 29 
ATOM   9941  C CB  . PHE H  2 95  ? 29.215  -27.924  31.027  1.000 45.112  0 95  PHE HHH CB  1 ? 29 
ATOM   9942  C CG  . PHE H  2 95  ? 28.291  -28.345  29.928  1.000 46.294  0 95  PHE HHH CG  1 ? 29 
ATOM   9943  C CD1 . PHE H  2 95  ? 27.669  -29.583  29.973  1.000 47.367  0 95  PHE HHH CD1 1 ? 29 
ATOM   9944  C CD2 . PHE H  2 95  ? 28.037  -27.499  28.857  1.000 47.112  0 95  PHE HHH CD2 1 ? 29 
ATOM   9945  C CE1 . PHE H  2 95  ? 26.801  -29.967  28.961  1.000 50.435  0 95  PHE HHH CE1 1 ? 29 
ATOM   9946  C CE2 . PHE H  2 95  ? 27.174  -27.893  27.836  1.000 49.570  0 95  PHE HHH CE2 1 ? 29 
ATOM   9947  C CZ  . PHE H  2 95  ? 26.553  -29.125  27.895  1.000 50.537  0 95  PHE HHH CZ  1 ? 29 
ATOM   9948  N N   . CYS H  2 96  ? 32.223  -26.734  31.660  1.000 46.203  0 96  CYS HHH N   1 ? 29 
ATOM   9949  C CA  . CYS H  2 96  ? 32.860  -25.791  32.589  1.000 47.025  0 96  CYS HHH CA  1 ? 29 
ATOM   9950  C C   . CYS H  2 96  ? 31.799  -24.784  33.049  1.000 44.464  0 96  CYS HHH C   1 ? 29 
ATOM   9951  O O   . CYS H  2 96  ? 30.973  -24.339  32.221  1.000 44.594  0 96  CYS HHH O   1 ? 29 
ATOM   9952  C CB  . CYS H  2 96  ? 33.976  -25.090  31.832  1.000 51.042  0 96  CYS HHH CB  1 ? 29 
ATOM   9953  S SG  . CYS H  2 96  ? 34.984  -24.036  32.881  1.000 58.083  0 96  CYS HHH SG  1 ? 29 
ATOM   9954  N N   . ALA H  2 97  ? 31.790  -24.420  34.323  1.000 42.399  0 97  ALA HHH N   1 ? 29 
ATOM   9955  C CA  . ALA H  2 97  ? 30.875  -23.376  34.827  1.000 41.164  0 97  ALA HHH CA  1 ? 29 
ATOM   9956  C C   . ALA H  2 97  ? 31.591  -22.516  35.866  1.000 40.661  0 97  ALA HHH C   1 ? 29 
ATOM   9957  O O   . ALA H  2 97  ? 32.578  -23.001  36.472  1.000 40.471  0 97  ALA HHH O   1 ? 29 
ATOM   9958  C CB  . ALA H  2 97  ? 29.624  -23.995  35.388  1.000 41.655  0 97  ALA HHH CB  1 ? 29 
ATOM   9959  N N   . ALA H  2 98  ? 31.096  -21.291  36.070  1.000 39.372  0 98  ALA HHH N   1 ? 29 
ATOM   9960  C CA  . ALA H  2 98  ? 31.723  -20.305  36.974  1.000 40.212  0 98  ALA HHH CA  1 ? 29 
ATOM   9961  C C   . ALA H  2 98  ? 30.659  -19.418  37.615  1.000 42.160  0 98  ALA HHH C   1 ? 29 
ATOM   9962  O O   . ALA H  2 98  ? 29.659  -19.091  36.946  1.000 44.615  0 98  ALA HHH O   1 ? 29 
ATOM   9963  C CB  . ALA H  2 98  ? 32.723  -19.464  36.214  1.000 40.625  0 98  ALA HHH CB  1 ? 29 
ATOM   9964  N N   . ASP H  2 99  ? 30.930  -18.988  38.843  1.000 41.310  0 99  ASP HHH N   1 ? 29 
ATOM   9965  C CA  . ASP H  2 99  ? 30.089  -18.030  39.595  1.000 42.816  0 99  ASP HHH CA  1 ? 29 
ATOM   9966  C C   . ASP H  2 99  ? 30.936  -17.316  40.649  1.000 41.044  0 99  ASP HHH C   1 ? 29 
ATOM   9967  O O   . ASP H  2 99  ? 31.881  -17.905  41.172  1.000 39.179  0 99  ASP HHH O   1 ? 29 
ATOM   9968  C CB  . ASP H  2 99  ? 28.909  -18.733  40.271  1.000 44.671  0 99  ASP HHH CB  1 ? 29 
ATOM   9969  C CG  . ASP H  2 99  ? 27.775  -17.763  40.512  1.000 45.711  0 99  ASP HHH CG  1 ? 29 
ATOM   9970  O OD1 . ASP H  2 99  ? 27.047  -17.474  39.535  1.000 45.783  0 99  ASP HHH OD1 1 ? 29 
ATOM   9971  O OD2 . ASP H  2 99  ? 27.668  -17.259  41.661  1.000 46.241  0 99  ASP HHH OD2 1 ? 29 
ATOM   9972  N N   . ARG H  2 100 ? 30.583  -16.080  40.952  1.000 43.388  0 100 ARG HHH N   1 ? 30 
ATOM   9973  C CA  . ARG H  2 100 ? 31.218  -15.281  42.031  1.000 42.480  0 100 ARG HHH CA  1 ? 30 
ATOM   9974  C C   . ARG H  2 100 ? 30.930  -15.942  43.379  1.000 41.074  0 100 ARG HHH C   1 ? 30 
ATOM   9975  O O   . ARG H  2 100 ? 31.771  -15.867  44.243  1.000 41.024  0 100 ARG HHH O   1 ? 30 
ATOM   9976  C CB  . ARG H  2 100 ? 30.674  -13.854  41.995  1.000 44.743  0 100 ARG HHH CB  1 ? 30 
ATOM   9977  C CG  . ARG H  2 100 ? 31.093  -13.098  40.740  1.000 47.780  0 100 ARG HHH CG  1 ? 30 
ATOM   9978  C CD  . ARG H  2 100 ? 32.530  -12.623  40.805  1.000 49.532  0 100 ARG HHH CD  1 ? 30 
ATOM   9979  N NE  . ARG H  2 100 ? 32.819  -11.887  42.036  1.000 50.283  0 100 ARG HHH NE  1 ? 30 
ATOM   9980  C CZ  . ARG H  2 100 ? 32.622  -10.574  42.234  1.000 51.034  0 100 ARG HHH CZ  1 ? 30 
ATOM   9981  N NH1 . ARG H  2 100 ? 32.112  -9.794   41.298  1.000 54.453  0 100 ARG HHH NH1 1 ? 30 
ATOM   9982  N NH2 . ARG H  2 100 ? 32.926  -10.041  43.395  1.000 50.407  0 100 ARG HHH NH2 1 ? 30 
ATOM   9983  N N   . GLY H  2 101 ? 29.772  -16.569  43.541  1.000 42.727  0 101 GLY HHH N   1 ? 30 
ATOM   9984  C CA  . GLY H  2 101 ? 29.304  -17.140  44.815  1.000 41.331  0 101 GLY HHH CA  1 ? 30 
ATOM   9985  C C   . GLY H  2 101 ? 29.550  -18.629  44.897  1.000 42.883  0 101 GLY HHH C   1 ? 30 
ATOM   9986  O O   . GLY H  2 101 ? 29.474  -19.327  43.853  1.000 45.266  0 101 GLY HHH O   1 ? 30 
ATOM   9987  N N   . GLU H  2 102 ? 29.829  -19.105  46.106  1.000 43.002  0 102 GLU HHH N   1 ? 30 
ATOM   9988  C CA  . GLU H  2 102 ? 29.869  -20.543  46.460  1.000 42.219  0 102 GLU HHH CA  1 ? 30 
ATOM   9989  C C   . GLU H  2 102 ? 28.517  -20.906  47.077  1.000 40.562  0 102 GLU HHH C   1 ? 30 
ATOM   9990  O O   . GLU H  2 102 ? 28.132  -20.289  48.085  1.000 39.625  0 102 GLU HHH O   1 ? 30 
ATOM   9991  C CB  . GLU H  2 102 ? 31.020  -20.790  47.432  1.000 42.583  0 102 GLU HHH CB  1 ? 30 
ATOM   9992  C CG  . GLU H  2 102 ? 31.232  -22.262  47.744  1.000 43.657  0 102 GLU HHH CG  1 ? 30 
ATOM   9993  C CD  . GLU H  2 102 ? 32.360  -22.512  48.710  1.000 46.997  0 102 GLU HHH CD  1 ? 30 
ATOM   9994  O OE1 . GLU H  2 102 ? 33.247  -21.643  48.824  1.000 49.903  0 102 GLU HHH OE1 1 ? 30 
ATOM   9995  O OE2 . GLU H  2 102 ? 32.329  -23.551  49.352  1.000 51.555  0 102 GLU HHH OE2 1 ? 30 
ATOM   9996  N N   . SER H  2 103 ? 27.820  -21.864  46.480  1.000 41.911  0 103 SER HHH N   1 ? 30 
ATOM   9997  C CA  . SER H  2 103 ? 26.450  -22.281  46.880  1.000 42.731  0 103 SER HHH CA  1 ? 30 
ATOM   9998  C C   . SER H  2 103 ? 26.512  -23.398  47.924  1.000 44.860  0 103 SER HHH C   1 ? 30 
ATOM   9999  O O   . SER H  2 103 ? 27.304  -24.345  47.768  1.000 43.489  0 103 SER HHH O   1 ? 30 
ATOM   10000 C CB  . SER H  2 103 ? 25.639  -22.707  45.698  1.000 42.165  0 103 SER HHH CB  1 ? 30 
ATOM   10001 O OG  . SER H  2 103 ? 24.337  -23.090  46.103  1.000 40.827  0 103 SER HHH OG  1 ? 30 
ATOM   10002 N N   . TYR H  2 104 ? 25.659  -23.315  48.936  1.000 45.149  0 104 TYR HHH N   1 ? 30 
ATOM   10003 C CA  . TYR H  2 104 ? 25.334  -24.495  49.768  1.000 45.998  0 104 TYR HHH CA  1 ? 30 
ATOM   10004 C C   . TYR H  2 104 ? 24.812  -25.604  48.844  1.000 44.232  0 104 TYR HHH C   1 ? 30 
ATOM   10005 O O   . TYR H  2 104 ? 25.109  -26.749  49.127  1.000 45.374  0 104 TYR HHH O   1 ? 30 
ATOM   10006 C CB  . TYR H  2 104 ? 24.313  -24.154  50.848  1.000 46.452  0 104 TYR HHH CB  1 ? 30 
ATOM   10007 C CG  . TYR H  2 104 ? 24.002  -25.327  51.733  1.000 50.410  0 104 TYR HHH CG  1 ? 30 
ATOM   10008 C CD1 . TYR H  2 104 ? 24.968  -25.846  52.577  1.000 53.909  0 104 TYR HHH CD1 1 ? 30 
ATOM   10009 C CD2 . TYR H  2 104 ? 22.761  -25.950  51.692  1.000 53.035  0 104 TYR HHH CD2 1 ? 30 
ATOM   10010 C CE1 . TYR H  2 104 ? 24.707  -26.950  53.371  1.000 58.462  0 104 TYR HHH CE1 1 ? 30 
ATOM   10011 C CE2 . TYR H  2 104 ? 22.481  -27.046  52.493  1.000 54.687  0 104 TYR HHH CE2 1 ? 30 
ATOM   10012 C CZ  . TYR H  2 104 ? 23.462  -27.552  53.326  1.000 57.901  0 104 TYR HHH CZ  1 ? 30 
ATOM   10013 O OH  . TYR H  2 104 ? 23.233  -28.631  54.131  1.000 62.613  0 104 TYR HHH OH  1 ? 30 
ATOM   10014 N N   . TYR H  2 105 ? 24.046  -25.265  47.807  1.000 42.988  0 105 TYR HHH N   1 ? 30 
ATOM   10015 C CA  . TYR H  2 105 ? 23.460  -26.225  46.833  1.000 43.499  0 105 TYR HHH CA  1 ? 30 
ATOM   10016 C C   . TYR H  2 105 ? 24.369  -26.239  45.594  1.000 44.686  0 105 TYR HHH C   1 ? 30 
ATOM   10017 O O   . TYR H  2 105 ? 23.930  -25.956  44.453  1.000 46.962  0 105 TYR HHH O   1 ? 30 
ATOM   10018 C CB  . TYR H  2 105 ? 22.003  -25.879  46.488  1.000 44.496  0 105 TYR HHH CB  1 ? 30 
ATOM   10019 C CG  . TYR H  2 105 ? 21.086  -25.578  47.646  1.000 46.472  0 105 TYR HHH CG  1 ? 30 
ATOM   10020 C CD1 . TYR H  2 105 ? 20.700  -26.565  48.540  1.000 46.861  0 105 TYR HHH CD1 1 ? 30 
ATOM   10021 C CD2 . TYR H  2 105 ? 20.556  -24.300  47.831  1.000 47.366  0 105 TYR HHH CD2 1 ? 30 
ATOM   10022 C CE1 . TYR H  2 105 ? 19.847  -26.292  49.601  1.000 48.843  0 105 TYR HHH CE1 1 ? 30 
ATOM   10023 C CE2 . TYR H  2 105 ? 19.702  -24.014  48.889  1.000 49.112  0 105 TYR HHH CE2 1 ? 30 
ATOM   10024 C CZ  . TYR H  2 105 ? 19.350  -25.011  49.778  1.000 50.317  0 105 TYR HHH CZ  1 ? 30 
ATOM   10025 O OH  . TYR H  2 105 ? 18.504  -24.718  50.810  1.000 56.877  0 105 TYR HHH OH  1 ? 30 
ATOM   10026 N N   . TYR H  2 106 ? 25.631  -26.604  45.806  1.000 45.087  0 106 TYR HHH N   1 ? 30 
ATOM   10027 C CA  . TYR H  2 106 ? 26.724  -26.516  44.809  1.000 46.081  0 106 TYR HHH CA  1 ? 30 
ATOM   10028 C C   . TYR H  2 106 ? 26.458  -27.434  43.612  1.000 49.744  0 106 TYR HHH C   1 ? 30 
ATOM   10029 O O   . TYR H  2 106 ? 27.126  -27.249  42.603  1.000 49.141  0 106 TYR HHH O   1 ? 30 
ATOM   10030 C CB  . TYR H  2 106 ? 28.082  -26.861  45.424  1.000 47.490  0 106 TYR HHH CB  1 ? 30 
ATOM   10031 C CG  . TYR H  2 106 ? 28.133  -28.182  46.141  1.000 50.922  0 106 TYR HHH CG  1 ? 30 
ATOM   10032 C CD1 . TYR H  2 106 ? 28.325  -29.367  45.460  1.000 54.758  0 106 TYR HHH CD1 1 ? 30 
ATOM   10033 C CD2 . TYR H  2 106 ? 28.029  -28.239  47.519  1.000 51.353  0 106 TYR HHH CD2 1 ? 30 
ATOM   10034 C CE1 . TYR H  2 106 ? 28.375  -30.583  46.123  1.000 57.360  0 106 TYR HHH CE1 1 ? 30 
ATOM   10035 C CE2 . TYR H  2 106 ? 28.047  -29.445  48.199  1.000 53.752  0 106 TYR HHH CE2 1 ? 30 
ATOM   10036 C CZ  . TYR H  2 106 ? 28.233  -30.620  47.498  1.000 56.995  0 106 TYR HHH CZ  1 ? 30 
ATOM   10037 O OH  . TYR H  2 106 ? 28.280  -31.815  48.148  1.000 60.800  0 106 TYR HHH OH  1 ? 30 
ATOM   10038 N N   . THR H  2 107 ? 25.546  -28.397  43.718  1.000 50.279  0 107 THR HHH N   1 ? 31 
ATOM   10039 C CA  . THR H  2 107 ? 25.179  -29.344  42.631  1.000 49.530  0 107 THR HHH CA  1 ? 31 
ATOM   10040 C C   . THR H  2 107 ? 24.110  -28.747  41.718  1.000 48.367  0 107 THR HHH C   1 ? 31 
ATOM   10041 O O   . THR H  2 107 ? 23.861  -29.334  40.688  1.000 51.996  0 107 THR HHH O   1 ? 31 
ATOM   10042 C CB  . THR H  2 107 ? 24.701  -30.698  43.168  1.000 51.751  0 107 THR HHH CB  1 ? 31 
ATOM   10043 O OG1 . THR H  2 107 ? 23.397  -30.546  43.731  1.000 55.085  0 107 THR HHH OG1 1 ? 31 
ATOM   10044 C CG2 . THR H  2 107 ? 25.620  -31.293  44.209  1.000 51.759  0 107 THR HHH CG2 1 ? 31 
ATOM   10045 N N   . ARG H  2 108 ? 23.494  -27.620  42.056  1.000 48.282  0 108 ARG HHH N   1 ? 31 
ATOM   10046 C CA  . ARG H  2 108 ? 22.429  -27.016  41.210  1.000 46.497  0 108 ARG HHH CA  1 ? 31 
ATOM   10047 C C   . ARG H  2 108 ? 23.050  -26.221  40.067  1.000 45.759  0 108 ARG HHH C   1 ? 31 
ATOM   10048 O O   . ARG H  2 108 ? 23.784  -25.255  40.285  1.000 44.578  0 108 ARG HHH O   1 ? 31 
ATOM   10049 C CB  . ARG H  2 108 ? 21.556  -26.040  41.991  1.000 46.756  0 108 ARG HHH CB  1 ? 31 
ATOM   10050 C CG  . ARG H  2 108 ? 20.645  -26.710  42.987  1.000 47.136  0 108 ARG HHH CG  1 ? 31 
ATOM   10051 C CD  . ARG H  2 108 ? 19.677  -25.671  43.514  1.000 47.482  0 108 ARG HHH CD  1 ? 31 
ATOM   10052 N NE  . ARG H  2 108 ? 19.006  -26.243  44.676  1.000 48.530  0 108 ARG HHH NE  1 ? 31 
ATOM   10053 C CZ  . ARG H  2 108 ? 18.257  -25.564  45.510  1.000 50.318  0 108 ARG HHH CZ  1 ? 31 
ATOM   10054 N NH1 . ARG H  2 108 ? 18.060  -24.272  45.320  1.000 52.071  0 108 ARG HHH NH1 1 ? 31 
ATOM   10055 N NH2 . ARG H  2 108 ? 17.723  -26.174  46.545  1.000 52.842  0 108 ARG HHH NH2 1 ? 31 
ATOM   10056 N N   . PRO H  2 109 ? 22.729  -26.574  38.804  1.000 44.773  0 109 PRO HHH N   1 ? 31 
ATOM   10057 C CA  . PRO H  2 109 ? 23.128  -25.748  37.668  1.000 42.631  0 109 PRO HHH CA  1 ? 31 
ATOM   10058 C C   . PRO H  2 109 ? 22.749  -24.266  37.787  1.000 40.589  0 109 PRO HHH C   1 ? 31 
ATOM   10059 O O   . PRO H  2 109 ? 23.556  -23.432  37.412  1.000 37.934  0 109 PRO HHH O   1 ? 31 
ATOM   10060 C CB  . PRO H  2 109 ? 22.391  -26.401  36.488  1.000 43.967  0 109 PRO HHH CB  1 ? 31 
ATOM   10061 C CG  . PRO H  2 109 ? 22.284  -27.849  36.899  1.000 45.131  0 109 PRO HHH CG  1 ? 31 
ATOM   10062 C CD  . PRO H  2 109 ? 22.036  -27.811  38.398  1.000 45.090  0 109 PRO HHH CD  1 ? 31 
ATOM   10063 N N   . THR H  2 110 ? 21.561  -23.963  38.331  1.000 40.157  0 110 THR HHH N   1 ? 31 
ATOM   10064 C CA  . THR H  2 110 ? 21.020  -22.583  38.449  1.000 40.440  0 110 THR HHH CA  1 ? 31 
ATOM   10065 C C   . THR H  2 110 ? 21.897  -21.725  39.382  1.000 41.036  0 110 THR HHH C   1 ? 31 
ATOM   10066 O O   . THR H  2 110 ? 21.768  -20.511  39.316  1.000 42.022  0 110 THR HHH O   1 ? 31 
ATOM   10067 C CB  . THR H  2 110 ? 19.558  -22.596  38.882  1.000 40.505  0 110 THR HHH CB  1 ? 31 
ATOM   10068 O OG1 . THR H  2 110 ? 19.442  -23.310  40.109  1.000 43.994  0 110 THR HHH OG1 1 ? 31 
ATOM   10069 C CG2 . THR H  2 110 ? 18.659  -23.226  37.848  1.000 39.898  0 110 THR HHH CG2 1 ? 31 
ATOM   10070 N N   . GLU H  2 111 ? 22.772  -22.313  40.198  1.000 41.468  0 111 GLU HHH N   1 ? 31 
ATOM   10071 C CA  . GLU H  2 111 ? 23.667  -21.545  41.108  1.000 42.631  0 111 GLU HHH CA  1 ? 31 
ATOM   10072 C C   . GLU H  2 111 ? 24.911  -21.048  40.355  1.000 41.584  0 111 GLU HHH C   1 ? 31 
ATOM   10073 O O   . GLU H  2 111 ? 25.693  -20.320  40.966  1.000 44.173  0 111 GLU HHH O   1 ? 31 
ATOM   10074 C CB  . GLU H  2 111 ? 24.056  -22.390  42.329  1.000 43.680  0 111 GLU HHH CB  1 ? 31 
ATOM   10075 C CG  . GLU H  2 111 ? 22.893  -22.666  43.267  1.000 45.368  0 111 GLU HHH CG  1 ? 31 
ATOM   10076 C CD  . GLU H  2 111 ? 22.355  -21.484  44.035  1.000 46.970  0 111 GLU HHH CD  1 ? 31 
ATOM   10077 O OE1 . GLU H  2 111 ? 21.772  -20.585  43.398  1.000 47.500  0 111 GLU HHH OE1 1 ? 31 
ATOM   10078 O OE2 . GLU H  2 111 ? 22.486  -21.504  45.270  1.000 47.977  0 111 GLU HHH OE2 1 ? 31 
ATOM   10079 N N   . TYR H  2 112 ? 25.097  -21.394  39.082  1.000 41.166  0 112 TYR HHH N   1 ? 31 
ATOM   10080 C CA  . TYR H  2 112 ? 26.272  -20.945  38.277  1.000 41.713  0 112 TYR HHH CA  1 ? 31 
ATOM   10081 C C   . TYR H  2 112 ? 25.808  -20.060  37.109  1.000 40.742  0 112 TYR HHH C   1 ? 31 
ATOM   10082 O O   . TYR H  2 112 ? 25.029  -20.515  36.274  1.000 39.113  0 112 TYR HHH O   1 ? 31 
ATOM   10083 C CB  . TYR H  2 112 ? 27.090  -22.161  37.839  1.000 40.160  0 112 TYR HHH CB  1 ? 31 
ATOM   10084 C CG  . TYR H  2 112 ? 27.556  -23.011  38.990  1.000 39.019  0 112 TYR HHH CG  1 ? 31 
ATOM   10085 C CD1 . TYR H  2 112 ? 26.737  -23.991  39.528  1.000 39.795  0 112 TYR HHH CD1 1 ? 31 
ATOM   10086 C CD2 . TYR H  2 112 ? 28.807  -22.850  39.539  1.000 40.111  0 112 TYR HHH CD2 1 ? 31 
ATOM   10087 C CE1 . TYR H  2 112 ? 27.148  -24.781  40.584  1.000 40.571  0 112 TYR HHH CE1 1 ? 31 
ATOM   10088 C CE2 . TYR H  2 112 ? 29.227  -23.619  40.622  1.000 42.317  0 112 TYR HHH CE2 1 ? 31 
ATOM   10089 C CZ  . TYR H  2 112 ? 28.390  -24.580  41.159  1.000 41.379  0 112 TYR HHH CZ  1 ? 31 
ATOM   10090 O OH  . TYR H  2 112 ? 28.826  -25.349  42.195  1.000 40.865  0 112 TYR HHH OH  1 ? 31 
ATOM   10091 N N   . GLU H  2 113 ? 26.260  -18.811  37.070  1.000 41.449  0 113 GLU HHH N   1 ? 31 
ATOM   10092 C CA  . GLU H  2 113 ? 25.826  -17.830  36.040  1.000 44.732  0 113 GLU HHH CA  1 ? 31 
ATOM   10093 C C   . GLU H  2 113 ? 26.438  -18.163  34.670  1.000 43.456  0 113 GLU HHH C   1 ? 31 
ATOM   10094 O O   . GLU H  2 113 ? 25.741  -17.986  33.689  1.000 45.201  0 113 GLU HHH O   1 ? 31 
ATOM   10095 C CB  . GLU H  2 113 ? 26.237  -16.407  36.427  1.000 48.341  0 113 GLU HHH CB  1 ? 31 
ATOM   10096 C CG  . GLU H  2 113 ? 25.733  -15.383  35.429  1.000 53.033  0 113 GLU HHH CG  1 ? 31 
ATOM   10097 C CD  . GLU H  2 113 ? 25.942  -13.929  35.803  1.000 56.570  0 113 GLU HHH CD  1 ? 31 
ATOM   10098 O OE1 . GLU H  2 113 ? 26.427  -13.668  36.925  1.000 59.613  0 113 GLU HHH OE1 1 ? 31 
ATOM   10099 O OE2 . GLU H  2 113 ? 25.643  -13.063  34.950  1.000 60.791  0 113 GLU HHH OE2 1 ? 31 
ATOM   10100 N N   . PHE H  2 114 ? 27.703  -18.583  34.609  1.000 42.847  0 114 PHE HHH N   1 ? 31 
ATOM   10101 C CA  . PHE H  2 114 ? 28.489  -18.715  33.356  1.000 42.012  0 114 PHE HHH CA  1 ? 31 
ATOM   10102 C C   . PHE H  2 114 ? 28.739  -20.188  33.035  1.000 42.445  0 114 PHE HHH C   1 ? 31 
ATOM   10103 O O   . PHE H  2 114 ? 29.153  -20.961  33.926  1.000 40.357  0 114 PHE HHH O   1 ? 31 
ATOM   10104 C CB  . PHE H  2 114 ? 29.804  -17.960  33.480  1.000 41.431  0 114 PHE HHH CB  1 ? 31 
ATOM   10105 C CG  . PHE H  2 114 ? 29.601  -16.494  33.722  1.000 40.620  0 114 PHE HHH CG  1 ? 31 
ATOM   10106 C CD1 . PHE H  2 114 ? 28.976  -15.715  32.768  1.000 40.561  0 114 PHE HHH CD1 1 ? 31 
ATOM   10107 C CD2 . PHE H  2 114 ? 30.000  -15.906  34.915  1.000 40.729  0 114 PHE HHH CD2 1 ? 31 
ATOM   10108 C CE1 . PHE H  2 114 ? 28.763  -14.361  32.990  1.000 42.556  0 114 PHE HHH CE1 1 ? 31 
ATOM   10109 C CE2 . PHE H  2 114 ? 29.772  -14.559  35.150  1.000 41.205  0 114 PHE HHH CE2 1 ? 31 
ATOM   10110 C CZ  . PHE H  2 114 ? 29.166  -13.783  34.180  1.000 43.034  0 114 PHE HHH CZ  1 ? 31 
ATOM   10111 N N   . TRP H  2 115 ? 28.519  -20.538  31.762  1.000 42.645  0 115 TRP HHH N   1 ? 31 
ATOM   10112 C CA  . TRP H  2 115 ? 28.642  -21.912  31.230  1.000 41.177  0 115 TRP HHH CA  1 ? 31 
ATOM   10113 C C   . TRP H  2 115 ? 29.457  -21.910  29.938  1.000 40.727  0 115 TRP HHH C   1 ? 31 
ATOM   10114 O O   . TRP H  2 115 ? 29.162  -21.118  29.050  1.000 40.481  0 115 TRP HHH O   1 ? 31 
ATOM   10115 C CB  . TRP H  2 115 ? 27.240  -22.491  31.000  1.000 41.392  0 115 TRP HHH CB  1 ? 31 
ATOM   10116 C CG  . TRP H  2 115 ? 26.538  -22.763  32.284  1.000 43.492  0 115 TRP HHH CG  1 ? 31 
ATOM   10117 C CD1 . TRP H  2 115 ? 25.891  -21.849  33.070  1.000 44.107  0 115 TRP HHH CD1 1 ? 31 
ATOM   10118 C CD2 . TRP H  2 115 ? 26.491  -24.019  32.987  1.000 43.516  0 115 TRP HHH CD2 1 ? 31 
ATOM   10119 N NE1 . TRP H  2 115 ? 25.422  -22.468  34.198  1.000 44.715  0 115 TRP HHH NE1 1 ? 31 
ATOM   10120 C CE2 . TRP H  2 115 ? 25.780  -23.791  34.176  1.000 42.452  0 115 TRP HHH CE2 1 ? 31 
ATOM   10121 C CE3 . TRP H  2 115 ? 26.951  -25.305  32.721  1.000 43.512  0 115 TRP HHH CE3 1 ? 31 
ATOM   10122 C CZ2 . TRP H  2 115 ? 25.542  -24.801  35.101  1.000 43.002  0 115 TRP HHH CZ2 1 ? 31 
ATOM   10123 C CZ3 . TRP H  2 115 ? 26.701  -26.308  33.635  1.000 43.901  0 115 TRP HHH CZ3 1 ? 31 
ATOM   10124 C CH2 . TRP H  2 115 ? 26.027  -26.051  34.823  1.000 43.443  0 115 TRP HHH CH2 1 ? 31 
ATOM   10125 N N   . GLY H  2 116 ? 30.408  -22.830  29.828  1.000 40.740  0 116 GLY HHH N   1 ? 31 
ATOM   10126 C CA  . GLY H  2 116 ? 31.032  -23.185  28.542  1.000 41.659  0 116 GLY HHH CA  1 ? 31 
ATOM   10127 C C   . GLY H  2 116 ? 30.032  -23.915  27.656  1.000 43.842  0 116 GLY HHH C   1 ? 31 
ATOM   10128 O O   . GLY H  2 116 ? 28.918  -24.212  28.121  1.000 42.367  0 116 GLY HHH O   1 ? 31 
ATOM   10129 N N   . GLN H  2 117 ? 30.410  -24.190  26.402  1.000 44.444  0 117 GLN HHH N   1 ? 31 
ATOM   10130 C CA  . GLN H  2 117 ? 29.560  -24.904  25.416  1.000 43.692  0 117 GLN HHH CA  1 ? 31 
ATOM   10131 C C   . GLN H  2 117 ? 29.695  -26.406  25.615  1.000 44.612  0 117 GLN HHH C   1 ? 31 
ATOM   10132 O O   . GLN H  2 117 ? 28.836  -27.123  25.114  1.000 47.021  0 117 GLN HHH O   1 ? 31 
ATOM   10133 C CB  . GLN H  2 117 ? 29.920  -24.507  23.987  1.000 43.727  0 117 GLN HHH CB  1 ? 31 
ATOM   10134 C CG  . GLN H  2 117 ? 29.771  -23.025  23.714  1.000 44.270  0 117 GLN HHH CG  1 ? 31 
ATOM   10135 C CD  . GLN H  2 117 ? 28.383  -22.489  23.984  1.000 45.928  0 117 GLN HHH CD  1 ? 31 
ATOM   10136 O OE1 . GLN H  2 117 ? 28.203  -21.453  24.630  1.000 46.582  0 117 GLN HHH OE1 1 ? 31 
ATOM   10137 N NE2 . GLN H  2 117 ? 27.372  -23.198  23.513  1.000 46.200  0 117 GLN HHH NE2 1 ? 31 
ATOM   10138 N N   . GLY H  2 118 ? 30.729  -26.852  26.320  1.000 45.674  0 118 GLY HHH N   1 ? 31 
ATOM   10139 C CA  . GLY H  2 118 ? 30.976  -28.279  26.633  1.000 46.906  0 118 GLY HHH CA  1 ? 31 
ATOM   10140 C C   . GLY H  2 118 ? 31.903  -28.951  25.627  1.000 49.675  0 118 GLY HHH C   1 ? 31 
ATOM   10141 O O   . GLY H  2 118 ? 32.047  -28.437  24.514  1.000 47.928  0 118 GLY HHH O   1 ? 31 
ATOM   10142 N N   . THR H  2 119 ? 32.511  -30.073  26.018  1.000 52.076  0 119 THR HHH N   1 ? 31 
ATOM   10143 C CA  . THR H  2 119 ? 33.417  -30.903  25.197  1.000 53.209  0 119 THR HHH CA  1 ? 31 
ATOM   10144 C C   . THR H  2 119 ? 33.067  -32.377  25.431  1.000 54.822  0 119 THR HHH C   1 ? 31 
ATOM   10145 O O   . THR H  2 119 ? 32.785  -32.746  26.587  1.000 52.669  0 119 THR HHH O   1 ? 31 
ATOM   10146 C CB  . THR H  2 119 ? 34.868  -30.549  25.541  1.000 54.824  0 119 THR HHH CB  1 ? 31 
ATOM   10147 O OG1 . THR H  2 119 ? 35.756  -31.103  24.580  1.000 58.873  0 119 THR HHH OG1 1 ? 31 
ATOM   10148 C CG2 . THR H  2 119 ? 35.325  -31.050  26.889  1.000 54.718  0 119 THR HHH CG2 1 ? 31 
ATOM   10149 N N   . GLN H  2 120 ? 33.059  -33.180  24.367  1.000 55.204  0 120 GLN HHH N   1 ? 31 
ATOM   10150 C CA  . GLN H  2 120 ? 32.708  -34.618  24.428  1.000 56.677  0 120 GLN HHH CA  1 ? 31 
ATOM   10151 C C   . GLN H  2 120 ? 33.871  -35.377  25.068  1.000 56.737  0 120 GLN HHH C   1 ? 31 
ATOM   10152 O O   . GLN H  2 120 ? 35.016  -35.175  24.655  1.000 55.925  0 120 GLN HHH O   1 ? 31 
ATOM   10153 C CB  . GLN H  2 120 ? 32.375  -35.125  23.021  1.000 60.045  0 120 GLN HHH CB  1 ? 31 
ATOM   10154 C CG  . GLN H  2 120 ? 31.846  -36.554  22.984  1.000 63.192  0 120 GLN HHH CG  1 ? 31 
ATOM   10155 C CD  . GLN H  2 120 ? 30.518  -36.706  23.679  1.000 64.406  0 120 GLN HHH CD  1 ? 31 
ATOM   10156 O OE1 . GLN H  2 120 ? 29.593  -35.930  23.484  1.000 65.549  0 120 GLN HHH OE1 1 ? 31 
ATOM   10157 N NE2 . GLN H  2 120 ? 30.413  -37.711  24.528  1.000 67.911  0 120 GLN HHH NE2 1 ? 31 
ATOM   10158 N N   . VAL H  2 121 ? 33.565  -36.199  26.065  1.000 58.222  0 121 VAL HHH N   1 ? 31 
ATOM   10159 C CA  . VAL H  2 121 ? 34.423  -37.315  26.548  1.000 60.863  0 121 VAL HHH CA  1 ? 31 
ATOM   10160 C C   . VAL H  2 121 ? 33.709  -38.623  26.205  1.000 62.040  0 121 VAL HHH C   1 ? 31 
ATOM   10161 O O   . VAL H  2 121 ? 32.526  -38.761  26.577  1.000 59.894  0 121 VAL HHH O   1 ? 31 
ATOM   10162 C CB  . VAL H  2 121 ? 34.682  -37.197  28.059  1.000 61.216  0 121 VAL HHH CB  1 ? 31 
ATOM   10163 C CG1 . VAL H  2 121 ? 35.451  -38.401  28.590  1.000 63.026  0 121 VAL HHH CG1 1 ? 31 
ATOM   10164 C CG2 . VAL H  2 121 ? 35.391  -35.899  28.399  1.000 59.139  0 121 VAL HHH CG2 1 ? 31 
ATOM   10165 N N   . THR H  2 122 ? 34.382  -39.544  25.519  1.000 65.116  0 122 THR HHH N   1 ? 31 
ATOM   10166 C CA  . THR H  2 122 ? 33.821  -40.875  25.172  1.000 69.669  0 122 THR HHH CA  1 ? 31 
ATOM   10167 C C   . THR H  2 122 ? 34.739  -41.952  25.746  1.000 73.978  0 122 THR HHH C   1 ? 31 
ATOM   10168 O O   . THR H  2 122 ? 35.941  -41.929  25.437  1.000 77.454  0 122 THR HHH O   1 ? 31 
ATOM   10169 C CB  . THR H  2 122 ? 33.579  -41.006  23.662  1.000 71.089  0 122 THR HHH CB  1 ? 31 
ATOM   10170 O OG1 . THR H  2 122 ? 32.721  -39.930  23.279  1.000 69.351  0 122 THR HHH OG1 1 ? 31 
ATOM   10171 C CG2 . THR H  2 122 ? 32.946  -42.324  23.272  1.000 72.961  0 122 THR HHH CG2 1 ? 31 
ATOM   10172 N N   . VAL H  2 123 ? 34.191  -42.838  26.574  1.000 76.316  0 123 VAL HHH N   1 ? 31 
ATOM   10173 C CA  . VAL H  2 123 ? 34.916  -43.991  27.176  1.000 80.541  0 123 VAL HHH CA  1 ? 31 
ATOM   10174 C C   . VAL H  2 123 ? 34.365  -45.274  26.531  1.000 84.964  0 123 VAL HHH C   1 ? 31 
ATOM   10175 O O   . VAL H  2 123 ? 33.196  -45.589  26.773  1.000 83.265  0 123 VAL HHH O   1 ? 31 
ATOM   10176 C CB  . VAL H  2 123 ? 34.759  -43.967  28.708  1.000 79.177  0 123 VAL HHH CB  1 ? 31 
ATOM   10177 C CG1 . VAL H  2 123 ? 35.678  -44.970  29.366  1.000 82.816  0 123 VAL HHH CG1 1 ? 31 
ATOM   10178 C CG2 . VAL H  2 123 ? 34.980  -42.577  29.299  1.000 74.653  0 123 VAL HHH CG2 1 ? 31 
ATOM   10179 N N   . SER H  2 124 ? 35.140  -45.942  25.674  1.000 91.274  0 124 SER HHH N   1 ? 31 
ATOM   10180 C CA  . SER H  2 124 ? 34.754  -47.218  25.012  1.000 97.859  0 124 SER HHH CA  1 ? 31 
ATOM   10181 C C   . SER H  2 124 ? 35.018  -48.387  25.964  1.000 107.006 0 124 SER HHH C   1 ? 31 
ATOM   10182 O O   . SER H  2 124 ? 35.785  -48.205  26.916  1.000 105.211 0 124 SER HHH O   1 ? 31 
ATOM   10183 C CB  . SER H  2 124 ? 35.468  -47.397  23.716  1.000 99.392  0 124 SER HHH CB  1 ? 31 
ATOM   10184 O OG  . SER H  2 124 ? 36.862  -47.364  23.929  1.000 100.052 0 124 SER HHH OG  1 ? 31 
ATOM   10185 N N   . SER H  2 125 ? 34.387  -49.538  25.699  1.000 63.384  0 125 SER HHH N   1 ? ?  
ATOM   10186 C CA  . SER H  2 125 ? 34.379  -50.757  26.541  1.000 66.142  0 125 SER HHH CA  1 ? ?  
ATOM   10187 C C   . SER H  2 125 ? 35.262  -51.838  25.907  1.000 69.567  0 125 SER HHH C   1 ? ?  
ATOM   10188 O O   . SER H  2 125 ? 36.446  -51.902  26.209  1.000 76.663  0 125 SER HHH O   1 ? ?  
ATOM   10189 C CB  . SER H  2 125 ? 32.957  -51.216  26.684  1.000 67.572  0 125 SER HHH CB  1 ? ?  
ATOM   10190 O OG  . SER H  2 125 ? 32.566  -51.225  28.039  1.000 70.453  0 125 SER HHH OG  1 ? ?  
ATOM   10191 N N   . ASN I  1 2   ? 36.453  -82.272  80.082  1.000 97.898  0 331 ASN III N   1 ? ?  
ATOM   10192 C CA  . ASN I  1 2   ? 35.850  -82.853  78.845  1.000 100.790 0 331 ASN III CA  1 ? ?  
ATOM   10193 C C   . ASN I  1 2   ? 34.526  -82.139  78.530  1.000 104.619 0 331 ASN III C   1 ? ?  
ATOM   10194 O O   . ASN I  1 2   ? 33.565  -82.297  79.303  1.000 108.845 0 331 ASN III O   1 ? ?  
ATOM   10195 C CB  . ASN I  1 2   ? 35.626  -84.367  78.956  1.000 101.241 0 331 ASN III CB  1 ? ?  
ATOM   10196 C CG  . ASN I  1 2   ? 36.716  -85.207  78.314  1.000 102.361 0 331 ASN III CG  1 ? ?  
ATOM   10197 O OD1 . ASN I  1 2   ? 37.450  -84.732  77.452  1.000 97.980  0 331 ASN III OD1 1 ? ?  
ATOM   10198 N ND2 . ASN I  1 2   ? 36.805  -86.470  78.700  1.000 99.369  0 331 ASN III ND2 1 ? ?  
ATOM   10199 N N   . ILE I  1 3   ? 34.489  -81.421  77.404  1.000 100.623 0 332 ILE III N   1 ? ?  
ATOM   10200 C CA  . ILE I  1 3   ? 33.254  -80.924  76.724  1.000 92.863  0 332 ILE III CA  1 ? ?  
ATOM   10201 C C   . ILE I  1 3   ? 32.468  -82.150  76.228  1.000 84.550  0 332 ILE III C   1 ? ?  
ATOM   10202 O O   . ILE I  1 3   ? 33.068  -82.969  75.462  1.000 81.044  0 332 ILE III O   1 ? ?  
ATOM   10203 C CB  . ILE I  1 3   ? 33.640  -79.954  75.582  1.000 91.930  0 332 ILE III CB  1 ? ?  
ATOM   10204 C CG1 . ILE I  1 3   ? 34.264  -78.658  76.116  1.000 91.600  0 332 ILE III CG1 1 ? ?  
ATOM   10205 C CG2 . ILE I  1 3   ? 32.457  -79.683  74.662  1.000 91.006  0 332 ILE III CG2 1 ? ?  
ATOM   10206 C CD1 . ILE I  1 3   ? 35.161  -77.942  75.124  1.000 88.491  0 332 ILE III CD1 1 ? ?  
ATOM   10207 N N   . THR I  1 4   ? 31.179  -82.264  76.614  1.000 122.057 0 333 THR III N   1 ? 32 
ATOM   10208 C CA  . THR I  1 4   ? 30.305  -83.442  76.315  1.000 111.486 0 333 THR III CA  1 ? 32 
ATOM   10209 C C   . THR I  1 4   ? 28.935  -83.028  75.754  1.000 103.200 0 333 THR III C   1 ? 32 
ATOM   10210 O O   . THR I  1 4   ? 28.294  -83.920  75.181  1.000 100.095 0 333 THR III O   1 ? 32 
ATOM   10211 C CB  . THR I  1 4   ? 30.187  -84.370  77.528  1.000 112.045 0 333 THR III CB  1 ? 32 
ATOM   10212 O OG1 . THR I  1 4   ? 29.949  -83.524  78.647  1.000 116.118 0 333 THR III OG1 1 ? 32 
ATOM   10213 C CG2 . THR I  1 4   ? 31.415  -85.225  77.763  1.000 110.090 0 333 THR III CG2 1 ? 32 
ATOM   10214 N N   . ASN I  1 5   ? 28.548  -81.753  75.869  1.000 96.191  0 334 ASN III N   1 ? 32 
ATOM   10215 C CA  . ASN I  1 5   ? 27.246  -81.220  75.399  1.000 89.470  0 334 ASN III CA  1 ? 32 
ATOM   10216 C C   . ASN I  1 5   ? 27.232  -81.116  73.868  1.000 82.722  0 334 ASN III C   1 ? 32 
ATOM   10217 O O   . ASN I  1 5   ? 28.180  -80.571  73.296  1.000 79.765  0 334 ASN III O   1 ? 32 
ATOM   10218 C CB  . ASN I  1 5   ? 26.974  -79.851  76.023  1.000 91.657  0 334 ASN III CB  1 ? 32 
ATOM   10219 C CG  . ASN I  1 5   ? 28.120  -78.884  75.806  1.000 91.909  0 334 ASN III CG  1 ? 32 
ATOM   10220 O OD1 . ASN I  1 5   ? 29.273  -79.222  76.080  1.000 91.354  0 334 ASN III OD1 1 ? 32 
ATOM   10221 N ND2 . ASN I  1 5   ? 27.805  -77.710  75.284  1.000 92.335  0 334 ASN III ND2 1 ? 32 
ATOM   10222 N N   . LEU I  1 6   ? 26.171  -81.607  73.236  1.000 80.133  0 335 LEU III N   1 ? 32 
ATOM   10223 C CA  . LEU I  1 6   ? 26.084  -81.697  71.753  1.000 73.970  0 335 LEU III CA  1 ? 32 
ATOM   10224 C C   . LEU I  1 6   ? 25.814  -80.302  71.198  1.000 71.451  0 335 LEU III C   1 ? 32 
ATOM   10225 O O   . LEU I  1 6   ? 25.146  -79.531  71.864  1.000 69.917  0 335 LEU III O   1 ? 32 
ATOM   10226 C CB  . LEU I  1 6   ? 25.016  -82.720  71.350  1.000 71.220  0 335 LEU III CB  1 ? 32 
ATOM   10227 C CG  . LEU I  1 6   ? 25.332  -84.163  71.776  1.000 72.911  0 335 LEU III CG  1 ? 32 
ATOM   10228 C CD1 . LEU I  1 6   ? 24.231  -85.120  71.360  1.000 73.322  0 335 LEU III CD1 1 ? 32 
ATOM   10229 C CD2 . LEU I  1 6   ? 26.678  -84.638  71.222  1.000 73.001  0 335 LEU III CD2 1 ? 32 
ATOM   10230 N N   . CYS I  1 7   ? 26.385  -79.991  70.035  1.000 70.753  0 336 CYS III N   1 ? 32 
ATOM   10231 C CA  . CYS I  1 7   ? 26.180  -78.706  69.328  1.000 70.741  0 336 CYS III CA  1 ? 32 
ATOM   10232 C C   . CYS I  1 7   ? 24.713  -78.651  68.940  1.000 71.201  0 336 CYS III C   1 ? 32 
ATOM   10233 O O   . CYS I  1 7   ? 24.172  -79.635  68.440  1.000 69.366  0 336 CYS III O   1 ? 32 
ATOM   10234 C CB  . CYS I  1 7   ? 27.081  -78.568  68.104  1.000 69.831  0 336 CYS III CB  1 ? 32 
ATOM   10235 S SG  . CYS I  1 7   ? 28.853  -78.407  68.485  1.000 73.892  0 336 CYS III SG  1 ? 32 
ATOM   10236 N N   . PRO I  1 8   ? 24.028  -77.510  69.171  1.000 75.263  0 337 PRO III N   1 ? 32 
ATOM   10237 C CA  . PRO I  1 8   ? 22.574  -77.440  68.993  1.000 74.433  0 337 PRO III CA  1 ? 32 
ATOM   10238 C C   . PRO I  1 8   ? 22.212  -77.214  67.515  1.000 70.749  0 337 PRO III C   1 ? 32 
ATOM   10239 O O   . PRO I  1 8   ? 21.746  -76.140  67.150  1.000 70.963  0 337 PRO III O   1 ? 32 
ATOM   10240 C CB  . PRO I  1 8   ? 22.209  -76.254  69.902  1.000 78.723  0 337 PRO III CB  1 ? 32 
ATOM   10241 C CG  . PRO I  1 8   ? 23.412  -75.315  69.758  1.000 80.159  0 337 PRO III CG  1 ? 32 
ATOM   10242 C CD  . PRO I  1 8   ? 24.620  -76.224  69.595  1.000 78.735  0 337 PRO III CD  1 ? 32 
ATOM   10243 N N   . PHE I  1 9   ? 22.427  -78.231  66.678  1.000 68.142  0 338 PHE III N   1 ? 32 
ATOM   10244 C CA  . PHE I  1 9   ? 22.075  -78.210  65.236  1.000 65.856  0 338 PHE III CA  1 ? 32 
ATOM   10245 C C   . PHE I  1 9   ? 20.557  -78.074  65.061  1.000 65.503  0 338 PHE III C   1 ? 32 
ATOM   10246 O O   . PHE I  1 9   ? 20.130  -77.420  64.094  1.000 67.594  0 338 PHE III O   1 ? 32 
ATOM   10247 C CB  . PHE I  1 9   ? 22.628  -79.447  64.526  1.000 65.063  0 338 PHE III CB  1 ? 32 
ATOM   10248 C CG  . PHE I  1 9   ? 24.112  -79.407  64.277  1.000 64.846  0 338 PHE III CG  1 ? 32 
ATOM   10249 C CD1 . PHE I  1 9   ? 24.700  -78.266  63.749  1.000 65.097  0 338 PHE III CD1 1 ? 32 
ATOM   10250 C CD2 . PHE I  1 9   ? 24.918  -80.505  64.524  1.000 64.960  0 338 PHE III CD2 1 ? 32 
ATOM   10251 C CE1 . PHE I  1 9   ? 26.056  -78.223  63.472  1.000 64.336  0 338 PHE III CE1 1 ? 32 
ATOM   10252 C CE2 . PHE I  1 9   ? 26.279  -80.450  64.258  1.000 65.775  0 338 PHE III CE2 1 ? 32 
ATOM   10253 C CZ  . PHE I  1 9   ? 26.844  -79.309  63.737  1.000 64.964  0 338 PHE III CZ  1 ? 32 
ATOM   10254 N N   . GLY I  1 10  ? 19.767  -78.661  65.968  1.000 65.421  0 339 GLY III N   1 ? 32 
ATOM   10255 C CA  . GLY I  1 10  ? 18.300  -78.510  66.004  1.000 64.620  0 339 GLY III CA  1 ? 32 
ATOM   10256 C C   . GLY I  1 10  ? 17.863  -77.053  65.945  1.000 64.148  0 339 GLY III C   1 ? 32 
ATOM   10257 O O   . GLY I  1 10  ? 16.967  -76.751  65.155  1.000 62.163  0 339 GLY III O   1 ? 32 
ATOM   10258 N N   . GLU I  1 11  ? 18.485  -76.174  66.732  1.000 66.190  0 340 GLU III N   1 ? 32 
ATOM   10259 C CA  . GLU I  1 11  ? 18.133  -74.727  66.803  1.000 68.358  0 340 GLU III CA  1 ? 32 
ATOM   10260 C C   . GLU I  1 11  ? 18.364  -74.041  65.455  1.000 67.455  0 340 GLU III C   1 ? 32 
ATOM   10261 O O   . GLU I  1 11  ? 17.702  -73.013  65.211  1.000 69.783  0 340 GLU III O   1 ? 32 
ATOM   10262 C CB  . GLU I  1 11  ? 18.961  -74.000  67.854  1.000 71.536  0 340 GLU III CB  1 ? 32 
ATOM   10263 C CG  . GLU I  1 11  ? 18.650  -74.483  69.247  1.000 78.016  0 340 GLU III CG  1 ? 32 
ATOM   10264 C CD  . GLU I  1 11  ? 19.414  -73.745  70.333  1.000 84.013  0 340 GLU III CD  1 ? 32 
ATOM   10265 O OE1 . GLU I  1 11  ? 20.062  -72.722  70.006  1.000 86.522  0 340 GLU III OE1 1 ? 32 
ATOM   10266 O OE2 . GLU I  1 11  ? 19.373  -74.204  71.499  1.000 87.383  0 340 GLU III OE2 1 ? 32 
ATOM   10267 N N   . VAL I  1 12  ? 19.274  -74.577  64.635  1.000 64.611  0 341 VAL III N   1 ? 32 
ATOM   10268 C CA  . VAL I  1 12  ? 19.601  -74.027  63.293  1.000 63.285  0 341 VAL III CA  1 ? 32 
ATOM   10269 C C   . VAL I  1 12  ? 18.620  -74.586  62.246  1.000 62.347  0 341 VAL III C   1 ? 32 
ATOM   10270 O O   . VAL I  1 12  ? 17.905  -73.788  61.597  1.000 62.888  0 341 VAL III O   1 ? 32 
ATOM   10271 C CB  . VAL I  1 12  ? 21.054  -74.345  62.911  1.000 64.094  0 341 VAL III CB  1 ? 32 
ATOM   10272 C CG1 . VAL I  1 12  ? 21.385  -73.746  61.550  1.000 67.159  0 341 VAL III CG1 1 ? 32 
ATOM   10273 C CG2 . VAL I  1 12  ? 22.050  -73.881  63.959  1.000 64.855  0 341 VAL III CG2 1 ? 32 
ATOM   10274 N N   . PHE I  1 13  ? 18.607  -75.904  62.072  1.000 60.291  0 342 PHE III N   1 ? 32 
ATOM   10275 C CA  . PHE I  1 13  ? 17.918  -76.597  60.950  1.000 60.100  0 342 PHE III CA  1 ? 32 
ATOM   10276 C C   . PHE I  1 13  ? 16.400  -76.560  61.158  1.000 62.611  0 342 PHE III C   1 ? 32 
ATOM   10277 O O   . PHE I  1 13  ? 15.669  -76.523  60.149  1.000 64.029  0 342 PHE III O   1 ? 32 
ATOM   10278 C CB  . PHE I  1 13  ? 18.444  -78.024  60.816  1.000 58.542  0 342 PHE III CB  1 ? 32 
ATOM   10279 C CG  . PHE I  1 13  ? 19.803  -78.110  60.179  1.000 57.787  0 342 PHE III CG  1 ? 32 
ATOM   10280 C CD1 . PHE I  1 13  ? 20.960  -77.900  60.914  1.000 57.018  0 342 PHE III CD1 1 ? 32 
ATOM   10281 C CD2 . PHE I  1 13  ? 19.921  -78.401  58.838  1.000 58.236  0 342 PHE III CD2 1 ? 32 
ATOM   10282 C CE1 . PHE I  1 13  ? 22.205  -77.988  60.318  1.000 57.744  0 342 PHE III CE1 1 ? 32 
ATOM   10283 C CE2 . PHE I  1 13  ? 21.164  -78.502  58.240  1.000 59.247  0 342 PHE III CE2 1 ? 32 
ATOM   10284 C CZ  . PHE I  1 13  ? 22.302  -78.298  58.984  1.000 59.331  0 342 PHE III CZ  1 ? 32 
ATOM   10285 N N   . ASN I  1 14  ? 15.953  -76.552  62.415  1.000 64.946  0 343 ASN III N   1 ? 32 
ATOM   10286 C CA  . ASN I  1 14  ? 14.523  -76.622  62.811  1.000 67.378  0 343 ASN III CA  1 ? 32 
ATOM   10287 C C   . ASN I  1 14  ? 14.088  -75.328  63.508  1.000 65.869  0 343 ASN III C   1 ? 32 
ATOM   10288 O O   . ASN I  1 14  ? 13.054  -75.361  64.179  1.000 66.832  0 343 ASN III O   1 ? 32 
ATOM   10289 C CB  . ASN I  1 14  ? 14.267  -77.848  63.688  1.000 69.406  0 343 ASN III CB  1 ? 32 
ATOM   10290 C CG  . ASN I  1 14  ? 14.306  -79.141  62.914  1.000 73.805  0 343 ASN III CG  1 ? 32 
ATOM   10291 O OD1 . ASN I  1 14  ? 13.987  -79.165  61.731  1.000 72.784  0 343 ASN III OD1 1 ? 32 
ATOM   10292 N ND2 . ASN I  1 14  ? 14.688  -80.211  63.586  1.000 87.061  0 343 ASN III ND2 1 ? 32 
ATOM   10293 N N   . ALA I  1 15  ? 14.816  -74.220  63.334  1.000 65.036  0 344 ALA III N   1 ? 32 
ATOM   10294 C CA  . ALA I  1 15  ? 14.357  -72.877  63.755  1.000 65.387  0 344 ALA III CA  1 ? 32 
ATOM   10295 C C   . ALA I  1 15  ? 12.943  -72.676  63.199  1.000 65.527  0 344 ALA III C   1 ? 32 
ATOM   10296 O O   . ALA I  1 15  ? 12.689  -73.086  62.051  1.000 63.121  0 344 ALA III O   1 ? 32 
ATOM   10297 C CB  . ALA I  1 15  ? 15.308  -71.816  63.271  1.000 63.334  0 344 ALA III CB  1 ? 32 
ATOM   10298 N N   . THR I  1 16  ? 12.027  -72.116  63.986  1.000 67.174  0 345 THR III N   1 ? 32 
ATOM   10299 C CA  . THR I  1 16  ? 10.627  -71.919  63.535  1.000 69.095  0 345 THR III CA  1 ? 32 
ATOM   10300 C C   . THR I  1 16  ? 10.610  -70.804  62.470  1.000 69.628  0 345 THR III C   1 ? 32 
ATOM   10301 O O   . THR I  1 16  ? 9.739   -70.847  61.585  1.000 74.379  0 345 THR III O   1 ? 32 
ATOM   10302 C CB  . THR I  1 16  ? 9.721   -71.695  64.742  1.000 71.780  0 345 THR III CB  1 ? 32 
ATOM   10303 O OG1 . THR I  1 16  ? 10.393  -70.717  65.533  1.000 74.211  0 345 THR III OG1 1 ? 32 
ATOM   10304 C CG2 . THR I  1 16  ? 9.489   -72.961  65.543  1.000 72.327  0 345 THR III CG2 1 ? 32 
ATOM   10305 N N   . ARG I  1 17  ? 11.574  -69.881  62.519  1.000 65.930  0 346 ARG III N   1 ? 32 
ATOM   10306 C CA  . ARG I  1 17  ? 11.707  -68.758  61.564  1.000 64.254  0 346 ARG III CA  1 ? 32 
ATOM   10307 C C   . ARG I  1 17  ? 13.036  -68.850  60.807  1.000 61.765  0 346 ARG III C   1 ? 32 
ATOM   10308 O O   . ARG I  1 17  ? 14.051  -69.208  61.416  1.000 60.578  0 346 ARG III O   1 ? 32 
ATOM   10309 C CB  . ARG I  1 17  ? 11.653  -67.435  62.322  1.000 66.474  0 346 ARG III CB  1 ? 32 
ATOM   10310 C CG  . ARG I  1 17  ? 10.647  -66.451  61.756  1.000 68.930  0 346 ARG III CG  1 ? 32 
ATOM   10311 C CD  . ARG I  1 17  ? 10.948  -65.050  62.235  1.000 71.757  0 346 ARG III CD  1 ? 32 
ATOM   10312 N NE  . ARG I  1 17  ? 10.509  -64.893  63.615  1.000 75.390  0 346 ARG III NE  1 ? 32 
ATOM   10313 C CZ  . ARG I  1 17  ? 9.272   -64.560  63.993  1.000 77.238  0 346 ARG III CZ  1 ? 32 
ATOM   10314 N NH1 . ARG I  1 17  ? 8.326   -64.335  63.092  1.000 77.520  0 346 ARG III NH1 1 ? 32 
ATOM   10315 N NH2 . ARG I  1 17  ? 8.989   -64.418  65.279  1.000 78.869  0 346 ARG III NH2 1 ? 32 
ATOM   10316 N N   . PHE I  1 18  ? 12.999  -68.532  59.521  1.000 61.924  0 347 PHE III N   1 ? 33 
ATOM   10317 C CA  . PHE I  1 18  ? 14.190  -68.455  58.640  1.000 59.782  0 347 PHE III CA  1 ? 33 
ATOM   10318 C C   . PHE I  1 18  ? 14.244  -67.061  58.026  1.000 58.720  0 347 PHE III C   1 ? 33 
ATOM   10319 O O   . PHE I  1 18  ? 13.186  -66.483  57.706  1.000 60.555  0 347 PHE III O   1 ? 33 
ATOM   10320 C CB  . PHE I  1 18  ? 14.159  -69.536  57.555  1.000 60.745  0 347 PHE III CB  1 ? 33 
ATOM   10321 C CG  . PHE I  1 18  ? 14.899  -70.798  57.922  1.000 61.309  0 347 PHE III CG  1 ? 33 
ATOM   10322 C CD1 . PHE I  1 18  ? 14.467  -71.580  58.983  1.000 61.725  0 347 PHE III CD1 1 ? 33 
ATOM   10323 C CD2 . PHE I  1 18  ? 16.036  -71.195  57.217  1.000 60.576  0 347 PHE III CD2 1 ? 33 
ATOM   10324 C CE1 . PHE I  1 18  ? 15.161  -72.724  59.343  1.000 61.295  0 347 PHE III CE1 1 ? 33 
ATOM   10325 C CE2 . PHE I  1 18  ? 16.710  -72.356  57.565  1.000 59.927  0 347 PHE III CE2 1 ? 33 
ATOM   10326 C CZ  . PHE I  1 18  ? 16.278  -73.113  58.635  1.000 60.347  0 347 PHE III CZ  1 ? 33 
ATOM   10327 N N   . ALA I  1 19  ? 15.454  -66.531  57.864  1.000 56.243  0 348 ALA III N   1 ? 33 
ATOM   10328 C CA  . ALA I  1 19  ? 15.690  -65.173  57.334  1.000 54.267  0 348 ALA III CA  1 ? 33 
ATOM   10329 C C   . ALA I  1 19  ? 15.453  -65.153  55.815  1.000 54.325  0 348 ALA III C   1 ? 33 
ATOM   10330 O O   . ALA I  1 19  ? 15.590  -66.179  55.140  1.000 52.752  0 348 ALA III O   1 ? 33 
ATOM   10331 C CB  . ALA I  1 19  ? 17.090  -64.730  57.664  1.000 53.607  0 348 ALA III CB  1 ? 33 
ATOM   10332 N N   . SER I  1 20  ? 15.112  -63.979  55.302  1.000 54.930  0 349 SER III N   1 ? 33 
ATOM   10333 C CA  . SER I  1 20  ? 15.331  -63.598  53.896  1.000 55.673  0 349 SER III CA  1 ? 33 
ATOM   10334 C C   . SER I  1 20  ? 16.836  -63.679  53.605  1.000 55.226  0 349 SER III C   1 ? 33 
ATOM   10335 O O   . SER I  1 20  ? 17.651  -63.307  54.483  1.000 53.295  0 349 SER III O   1 ? 33 
ATOM   10336 C CB  . SER I  1 20  ? 14.766  -62.238  53.614  1.000 56.631  0 349 SER III CB  1 ? 33 
ATOM   10337 O OG  . SER I  1 20  ? 13.351  -62.301  53.582  1.000 58.756  0 349 SER III OG  1 ? 33 
ATOM   10338 N N   . VAL I  1 21  ? 17.189  -64.130  52.402  1.000 55.108  0 350 VAL III N   1 ? 33 
ATOM   10339 C CA  . VAL I  1 21  ? 18.601  -64.305  51.981  1.000 55.314  0 350 VAL III CA  1 ? 33 
ATOM   10340 C C   . VAL I  1 21  ? 19.375  -62.984  52.120  1.000 56.102  0 350 VAL III C   1 ? 33 
ATOM   10341 O O   . VAL I  1 21  ? 20.541  -63.042  52.541  1.000 55.869  0 350 VAL III O   1 ? 33 
ATOM   10342 C CB  . VAL I  1 21  ? 18.679  -64.892  50.560  1.000 57.042  0 350 VAL III CB  1 ? 33 
ATOM   10343 C CG1 . VAL I  1 21  ? 18.125  -63.940  49.508  1.000 58.516  0 350 VAL III CG1 1 ? 33 
ATOM   10344 C CG2 . VAL I  1 21  ? 20.098  -65.338  50.215  1.000 55.422  0 350 VAL III CG2 1 ? 33 
ATOM   10345 N N   . TYR I  1 22  ? 18.791  -61.829  51.792  1.000 57.855  0 351 TYR III N   1 ? 33 
ATOM   10346 C CA  . TYR I  1 22  ? 19.530  -60.536  51.809  1.000 59.648  0 351 TYR III CA  1 ? 33 
ATOM   10347 C C   . TYR I  1 22  ? 19.928  -60.208  53.268  1.000 57.670  0 351 TYR III C   1 ? 33 
ATOM   10348 O O   . TYR I  1 22  ? 20.971  -59.550  53.490  1.000 57.824  0 351 TYR III O   1 ? 33 
ATOM   10349 C CB  . TYR I  1 22  ? 18.711  -59.420  51.146  1.000 60.037  0 351 TYR III CB  1 ? 33 
ATOM   10350 C CG  . TYR I  1 22  ? 17.755  -58.753  52.098  1.000 60.403  0 351 TYR III CG  1 ? 33 
ATOM   10351 C CD1 . TYR I  1 22  ? 16.504  -59.299  52.340  1.000 59.996  0 351 TYR III CD1 1 ? 33 
ATOM   10352 C CD2 . TYR I  1 22  ? 18.119  -57.599  52.789  1.000 60.651  0 351 TYR III CD2 1 ? 33 
ATOM   10353 C CE1 . TYR I  1 22  ? 15.632  -58.710  53.239  1.000 59.635  0 351 TYR III CE1 1 ? 33 
ATOM   10354 C CE2 . TYR I  1 22  ? 17.261  -57.002  53.694  1.000 60.831  0 351 TYR III CE2 1 ? 33 
ATOM   10355 C CZ  . TYR I  1 22  ? 16.017  -57.563  53.918  1.000 60.702  0 351 TYR III CZ  1 ? 33 
ATOM   10356 O OH  . TYR I  1 22  ? 15.193  -56.970  54.825  1.000 62.381  0 351 TYR III OH  1 ? 33 
ATOM   10357 N N   . ALA I  1 23  ? 19.117  -60.644  54.229  1.000 56.083  0 352 ALA III N   1 ? 33 
ATOM   10358 C CA  . ALA I  1 23  ? 19.304  -60.417  55.683  1.000 56.675  0 352 ALA III CA  1 ? 33 
ATOM   10359 C C   . ALA I  1 23  ? 19.623  -61.748  56.359  1.000 55.322  0 352 ALA III C   1 ? 33 
ATOM   10360 O O   . ALA I  1 23  ? 19.061  -62.036  57.412  1.000 55.977  0 352 ALA III O   1 ? 33 
ATOM   10361 C CB  . ALA I  1 23  ? 18.070  -59.784  56.284  1.000 58.438  0 352 ALA III CB  1 ? 33 
ATOM   10362 N N   . TRP I  1 24  ? 20.512  -62.524  55.751  1.000 54.809  0 353 TRP III N   1 ? 33 
ATOM   10363 C CA  . TRP I  1 24  ? 20.822  -63.904  56.183  1.000 54.171  0 353 TRP III CA  1 ? 33 
ATOM   10364 C C   . TRP I  1 24  ? 21.255  -63.911  57.652  1.000 53.672  0 353 TRP III C   1 ? 33 
ATOM   10365 O O   . TRP I  1 24  ? 21.932  -62.991  58.105  1.000 52.896  0 353 TRP III O   1 ? 33 
ATOM   10366 C CB  . TRP I  1 24  ? 21.870  -64.537  55.266  1.000 53.060  0 353 TRP III CB  1 ? 33 
ATOM   10367 C CG  . TRP I  1 24  ? 23.081  -63.703  54.988  1.000 52.397  0 353 TRP III CG  1 ? 33 
ATOM   10368 C CD1 . TRP I  1 24  ? 23.287  -62.839  53.951  1.000 53.685  0 353 TRP III CD1 1 ? 33 
ATOM   10369 C CD2 . TRP I  1 24  ? 24.318  -63.757  55.706  1.000 51.717  0 353 TRP III CD2 1 ? 33 
ATOM   10370 N NE1 . TRP I  1 24  ? 24.559  -62.331  53.984  1.000 53.471  0 353 TRP III NE1 1 ? 33 
ATOM   10371 C CE2 . TRP I  1 24  ? 25.222  -62.891  55.042  1.000 53.022  0 353 TRP III CE2 1 ? 33 
ATOM   10372 C CE3 . TRP I  1 24  ? 24.748  -64.458  56.830  1.000 49.929  0 353 TRP III CE3 1 ? 33 
ATOM   10373 C CZ2 . TRP I  1 24  ? 26.534  -62.701  55.484  1.000 53.195  0 353 TRP III CZ2 1 ? 33 
ATOM   10374 C CZ3 . TRP I  1 24  ? 26.038  -64.266  57.271  1.000 50.017  0 353 TRP III CZ3 1 ? 33 
ATOM   10375 C CH2 . TRP I  1 24  ? 26.914  -63.392  56.617  1.000 51.613  0 353 TRP III CH2 1 ? 33 
ATOM   10376 N N   . ASN I  1 25  ? 20.828  -64.937  58.370  1.000 54.095  0 354 ASN III N   1 ? 33 
ATOM   10377 C CA  . ASN I  1 25  ? 21.029  -65.099  59.827  1.000 53.536  0 354 ASN III CA  1 ? 33 
ATOM   10378 C C   . ASN I  1 25  ? 22.309  -65.909  60.052  1.000 52.332  0 354 ASN III C   1 ? 33 
ATOM   10379 O O   . ASN I  1 25  ? 22.551  -66.871  59.287  1.000 52.144  0 354 ASN III O   1 ? 33 
ATOM   10380 C CB  . ASN I  1 25  ? 19.797  -65.777  60.410  1.000 55.549  0 354 ASN III CB  1 ? 33 
ATOM   10381 C CG  . ASN I  1 25  ? 19.904  -66.017  61.891  1.000 57.067  0 354 ASN III CG  1 ? 33 
ATOM   10382 O OD1 . ASN I  1 25  ? 20.387  -67.061  62.326  1.000 57.721  0 354 ASN III OD1 1 ? 33 
ATOM   10383 N ND2 . ASN I  1 25  ? 19.510  -65.014  62.648  1.000 57.718  0 354 ASN III ND2 1 ? 33 
ATOM   10384 N N   . ARG I  1 26  ? 23.109  -65.493  61.039  1.000 53.691  0 355 ARG III N   1 ? 33 
ATOM   10385 C CA  . ARG I  1 26  ? 24.321  -66.178  61.572  1.000 53.998  0 355 ARG III CA  1 ? 33 
ATOM   10386 C C   . ARG I  1 26  ? 24.075  -66.689  62.981  1.000 53.578  0 355 ARG III C   1 ? 33 
ATOM   10387 O O   . ARG I  1 26  ? 23.849  -65.858  63.844  1.000 52.024  0 355 ARG III O   1 ? 33 
ATOM   10388 C CB  . ARG I  1 26  ? 25.459  -65.238  61.967  1.000 55.286  0 355 ARG III CB  1 ? 33 
ATOM   10389 C CG  . ARG I  1 26  ? 26.530  -65.030  60.936  1.000 55.448  0 355 ARG III CG  1 ? 33 
ATOM   10390 C CD  . ARG I  1 26  ? 27.889  -65.528  61.312  1.000 54.961  0 355 ARG III CD  1 ? 33 
ATOM   10391 N NE  . ARG I  1 26  ? 28.322  -66.022  60.011  1.000 55.932  0 355 ARG III NE  1 ? 33 
ATOM   10392 C CZ  . ARG I  1 26  ? 29.354  -65.612  59.300  1.000 55.724  0 355 ARG III CZ  1 ? 33 
ATOM   10393 N NH1 . ARG I  1 26  ? 30.171  -64.695  59.770  1.000 57.824  0 355 ARG III NH1 1 ? 33 
ATOM   10394 N NH2 . ARG I  1 26  ? 29.578  -66.137  58.101  1.000 57.007  0 355 ARG III NH2 1 ? 33 
ATOM   10395 N N   . LYS I  1 27  ? 24.302  -67.969  63.228  1.000 55.056  0 356 LYS III N   1 ? 33 
ATOM   10396 C CA  . LYS I  1 27  ? 24.422  -68.500  64.605  1.000 57.939  0 356 LYS III CA  1 ? 33 
ATOM   10397 C C   . LYS I  1 27  ? 25.861  -68.987  64.771  1.000 56.734  0 356 LYS III C   1 ? 33 
ATOM   10398 O O   . LYS I  1 27  ? 26.386  -69.656  63.879  1.000 53.629  0 356 LYS III O   1 ? 33 
ATOM   10399 C CB  . LYS I  1 27  ? 23.357  -69.568  64.857  1.000 61.339  0 356 LYS III CB  1 ? 33 
ATOM   10400 C CG  . LYS I  1 27  ? 21.937  -69.139  64.496  1.000 66.448  0 356 LYS III CG  1 ? 33 
ATOM   10401 C CD  . LYS I  1 27  ? 20.868  -70.126  64.891  1.000 70.755  0 356 LYS III CD  1 ? 33 
ATOM   10402 C CE  . LYS I  1 27  ? 19.465  -69.685  64.527  1.000 69.973  0 356 LYS III CE  1 ? 33 
ATOM   10403 N NZ  . LYS I  1 27  ? 19.225  -69.752  63.067  1.000 69.602  0 356 LYS III NZ  1 ? 33 
ATOM   10404 N N   . ARG I  1 28  ? 26.502  -68.599  65.860  1.000 59.170  0 357 ARG III N   1 ? 33 
ATOM   10405 C CA  . ARG I  1 28  ? 27.828  -69.109  66.249  1.000 60.329  0 357 ARG III CA  1 ? 33 
ATOM   10406 C C   . ARG I  1 28  ? 27.639  -70.473  66.902  1.000 62.376  0 357 ARG III C   1 ? 33 
ATOM   10407 O O   . ARG I  1 28  ? 26.751  -70.592  67.759  1.000 68.086  0 357 ARG III O   1 ? 33 
ATOM   10408 C CB  . ARG I  1 28  ? 28.531  -68.130  67.180  1.000 63.046  0 357 ARG III CB  1 ? 33 
ATOM   10409 C CG  . ARG I  1 28  ? 29.972  -68.503  67.448  1.000 66.193  0 357 ARG III CG  1 ? 33 
ATOM   10410 C CD  . ARG I  1 28  ? 30.796  -67.323  67.903  1.000 70.297  0 357 ARG III CD  1 ? 33 
ATOM   10411 N NE  . ARG I  1 28  ? 31.996  -68.009  68.315  1.000 75.127  0 357 ARG III NE  1 ? 33 
ATOM   10412 C CZ  . ARG I  1 28  ? 32.381  -68.204  69.578  1.000 79.486  0 357 ARG III CZ  1 ? 33 
ATOM   10413 N NH1 . ARG I  1 28  ? 31.660  -67.712  70.575  1.000 81.505  0 357 ARG III NH1 1 ? 33 
ATOM   10414 N NH2 . ARG I  1 28  ? 33.497  -68.868  69.839  1.000 78.117  0 357 ARG III NH2 1 ? 33 
ATOM   10415 N N   . ILE I  1 29  ? 28.435  -71.454  66.502  1.000 61.558  0 358 ILE III N   1 ? 33 
ATOM   10416 C CA  . ILE I  1 29  ? 28.484  -72.772  67.189  1.000 60.295  0 358 ILE III CA  1 ? 33 
ATOM   10417 C C   . ILE I  1 29  ? 29.876  -72.923  67.797  1.000 61.823  0 358 ILE III C   1 ? 33 
ATOM   10418 O O   . ILE I  1 29  ? 30.864  -72.822  67.014  1.000 60.458  0 358 ILE III O   1 ? 33 
ATOM   10419 C CB  . ILE I  1 29  ? 28.118  -73.892  66.208  1.000 59.057  0 358 ILE III CB  1 ? 33 
ATOM   10420 C CG1 . ILE I  1 29  ? 26.683  -73.720  65.716  1.000 58.846  0 358 ILE III CG1 1 ? 33 
ATOM   10421 C CG2 . ILE I  1 29  ? 28.338  -75.255  66.847  1.000 59.801  0 358 ILE III CG2 1 ? 33 
ATOM   10422 C CD1 . ILE I  1 29  ? 26.355  -74.602  64.546  1.000 59.104  0 358 ILE III CD1 1 ? 33 
ATOM   10423 N N   . SER I  1 30  ? 29.964  -73.130  69.121  1.000 64.277  0 359 SER III N   1 ? 33 
ATOM   10424 C CA  . SER I  1 30  ? 31.268  -73.311  69.816  1.000 65.050  0 359 SER III CA  1 ? 33 
ATOM   10425 C C   . SER I  1 30  ? 31.090  -74.041  71.150  1.000 68.158  0 359 SER III C   1 ? 33 
ATOM   10426 O O   . SER I  1 30  ? 29.976  -74.128  71.645  1.000 68.474  0 359 SER III O   1 ? 33 
ATOM   10427 C CB  . SER I  1 30  ? 31.927  -71.998  70.020  1.000 65.216  0 359 SER III CB  1 ? 33 
ATOM   10428 O OG  . SER I  1 30  ? 31.003  -71.089  70.572  1.000 67.798  0 359 SER III OG  1 ? 33 
ATOM   10429 N N   . ASN I  1 31  ? 32.188  -74.568  71.675  1.000 71.613  0 360 ASN III N   1 ? 33 
ATOM   10430 C CA  . ASN I  1 31  ? 32.279  -75.182  73.024  1.000 72.359  0 360 ASN III CA  1 ? 33 
ATOM   10431 C C   . ASN I  1 31  ? 31.203  -76.237  73.107  1.000 69.772  0 360 ASN III C   1 ? 33 
ATOM   10432 O O   . ASN I  1 31  ? 30.391  -76.177  74.026  1.000 73.317  0 360 ASN III O   1 ? 33 
ATOM   10433 C CB  . ASN I  1 31  ? 32.270  -74.102  74.096  1.000 75.612  0 360 ASN III CB  1 ? 33 
ATOM   10434 C CG  . ASN I  1 31  ? 33.492  -73.205  73.919  1.000 77.020  0 360 ASN III CG  1 ? 33 
ATOM   10435 O OD1 . ASN I  1 31  ? 33.383  -71.985  73.805  1.000 75.262  0 360 ASN III OD1 1 ? 33 
ATOM   10436 N ND2 . ASN I  1 31  ? 34.678  -73.797  73.882  1.000 77.858  0 360 ASN III ND2 1 ? 33 
ATOM   10437 N N   . CYS I  1 32  ? 31.232  -77.160  72.151  1.000 65.581  0 361 CYS III N   1 ? 33 
ATOM   10438 C CA  . CYS I  1 32  ? 30.249  -78.266  72.022  1.000 65.038  0 361 CYS III CA  1 ? 33 
ATOM   10439 C C   . CYS I  1 32  ? 30.820  -79.373  71.129  1.000 62.071  0 361 CYS III C   1 ? 33 
ATOM   10440 O O   . CYS I  1 32  ? 31.756  -79.098  70.338  1.000 57.845  0 361 CYS III O   1 ? 33 
ATOM   10441 C CB  . CYS I  1 32  ? 28.926  -77.725  71.492  1.000 66.044  0 361 CYS III CB  1 ? 33 
ATOM   10442 S SG  . CYS I  1 32  ? 29.054  -76.885  69.878  1.000 66.518  0 361 CYS III SG  1 ? 33 
ATOM   10443 N N   . VAL I  1 33  ? 30.284  -80.585  71.276  1.000 62.977  0 362 VAL III N   1 ? 33 
ATOM   10444 C CA  . VAL I  1 33  ? 30.596  -81.774  70.432  1.000 63.124  0 362 VAL III CA  1 ? 33 
ATOM   10445 C C   . VAL I  1 33  ? 29.666  -81.732  69.221  1.000 62.499  0 362 VAL III C   1 ? 33 
ATOM   10446 O O   . VAL I  1 33  ? 28.435  -81.757  69.424  1.000 64.829  0 362 VAL III O   1 ? 33 
ATOM   10447 C CB  . VAL I  1 33  ? 30.416  -83.088  71.216  1.000 64.888  0 362 VAL III CB  1 ? 33 
ATOM   10448 C CG1 . VAL I  1 33  ? 30.714  -84.304  70.348  1.000 64.835  0 362 VAL III CG1 1 ? 33 
ATOM   10449 C CG2 . VAL I  1 33  ? 31.260  -83.096  72.476  1.000 65.575  0 362 VAL III CG2 1 ? 33 
ATOM   10450 N N   . ALA I  1 34  ? 30.226  -81.652  68.010  1.000 61.429  0 363 ALA III N   1 ? 33 
ATOM   10451 C CA  . ALA I  1 34  ? 29.462  -81.653  66.744  1.000 61.698  0 363 ALA III CA  1 ? 33 
ATOM   10452 C C   . ALA I  1 34  ? 29.225  -83.113  66.352  1.000 63.783  0 363 ALA III C   1 ? 33 
ATOM   10453 O O   . ALA I  1 34  ? 30.112  -83.732  65.736  1.000 65.447  0 363 ALA III O   1 ? 33 
ATOM   10454 C CB  . ALA I  1 34  ? 30.179  -80.882  65.659  1.000 60.255  0 363 ALA III CB  1 ? 33 
ATOM   10455 N N   . ASP I  1 35  ? 28.061  -83.636  66.717  1.000 64.608  0 364 ASP III N   1 ? 33 
ATOM   10456 C CA  . ASP I  1 35  ? 27.590  -84.943  66.219  1.000 66.991  0 364 ASP III CA  1 ? 33 
ATOM   10457 C C   . ASP I  1 35  ? 26.748  -84.703  64.972  1.000 65.234  0 364 ASP III C   1 ? 33 
ATOM   10458 O O   . ASP I  1 35  ? 25.633  -84.190  65.107  1.000 65.174  0 364 ASP III O   1 ? 33 
ATOM   10459 C CB  . ASP I  1 35  ? 26.808  -85.738  67.260  1.000 69.021  0 364 ASP III CB  1 ? 33 
ATOM   10460 C CG  . ASP I  1 35  ? 26.786  -87.195  66.864  1.000 69.654  0 364 ASP III CG  1 ? 33 
ATOM   10461 O OD1 . ASP I  1 35  ? 27.111  -87.472  65.699  1.000 68.613  0 364 ASP III OD1 1 ? 33 
ATOM   10462 O OD2 . ASP I  1 35  ? 26.505  -88.037  67.723  1.000 71.809  0 364 ASP III OD2 1 ? 33 
ATOM   10463 N N   . TYR I  1 36  ? 27.272  -85.112  63.821  1.000 64.659  0 365 TYR III N   1 ? 33 
ATOM   10464 C CA  . TYR I  1 36  ? 26.639  -84.877  62.502  1.000 65.702  0 365 TYR III CA  1 ? 33 
ATOM   10465 C C   . TYR I  1 36  ? 25.727  -86.044  62.154  1.000 67.891  0 365 TYR III C   1 ? 33 
ATOM   10466 O O   . TYR I  1 36  ? 25.098  -85.947  61.090  1.000 67.626  0 365 TYR III O   1 ? 33 
ATOM   10467 C CB  . TYR I  1 36  ? 27.705  -84.681  61.423  1.000 64.345  0 365 TYR III CB  1 ? 33 
ATOM   10468 C CG  . TYR I  1 36  ? 28.372  -83.350  61.526  1.000 63.961  0 365 TYR III CG  1 ? 33 
ATOM   10469 C CD1 . TYR I  1 36  ? 29.477  -83.167  62.328  1.000 63.410  0 365 TYR III CD1 1 ? 33 
ATOM   10470 C CD2 . TYR I  1 36  ? 27.894  -82.270  60.800  1.000 65.664  0 365 TYR III CD2 1 ? 33 
ATOM   10471 C CE1 . TYR I  1 36  ? 30.086  -81.928  62.435  1.000 63.692  0 365 TYR III CE1 1 ? 33 
ATOM   10472 C CE2 . TYR I  1 36  ? 28.499  -81.025  60.875  1.000 63.951  0 365 TYR III CE2 1 ? 33 
ATOM   10473 C CZ  . TYR I  1 36  ? 29.597  -80.861  61.702  1.000 64.186  0 365 TYR III CZ  1 ? 33 
ATOM   10474 O OH  . TYR I  1 36  ? 30.196  -79.648  61.797  1.000 67.737  0 365 TYR III OH  1 ? 33 
ATOM   10475 N N   . SER I  1 37  ? 25.643  -87.094  62.981  1.000 70.999  0 366 SER III N   1 ? 33 
ATOM   10476 C CA  . SER I  1 37  ? 24.816  -88.279  62.632  1.000 74.765  0 366 SER III CA  1 ? 33 
ATOM   10477 C C   . SER I  1 37  ? 23.343  -87.863  62.540  1.000 75.521  0 366 SER III C   1 ? 33 
ATOM   10478 O O   . SER I  1 37  ? 22.628  -88.507  61.782  1.000 79.384  0 366 SER III O   1 ? 33 
ATOM   10479 C CB  . SER I  1 37  ? 25.024  -89.453  63.569  1.000 76.479  0 366 SER III CB  1 ? 33 
ATOM   10480 O OG  . SER I  1 37  ? 25.080  -89.018  64.915  1.000 76.531  0 366 SER III OG  1 ? 33 
ATOM   10481 N N   . VAL I  1 38  ? 22.917  -86.790  63.211  1.000 73.458  0 367 VAL III N   1 ? 33 
ATOM   10482 C CA  . VAL I  1 38  ? 21.535  -86.259  63.046  1.000 75.038  0 367 VAL III CA  1 ? 33 
ATOM   10483 C C   . VAL I  1 38  ? 21.327  -85.854  61.569  1.000 71.971  0 367 VAL III C   1 ? 33 
ATOM   10484 O O   . VAL I  1 38  ? 20.296  -86.231  60.998  1.000 73.668  0 367 VAL III O   1 ? 33 
ATOM   10485 C CB  . VAL I  1 38  ? 21.258  -85.122  64.057  1.000 75.746  0 367 VAL III CB  1 ? 33 
ATOM   10486 C CG1 . VAL I  1 38  ? 22.054  -83.852  63.756  1.000 73.399  0 367 VAL III CG1 1 ? 33 
ATOM   10487 C CG2 . VAL I  1 38  ? 19.764  -84.829  64.176  1.000 77.033  0 367 VAL III CG2 1 ? 33 
ATOM   10488 N N   . LEU I  1 39  ? 22.302  -85.192  60.946  1.000 67.920  0 368 LEU III N   1 ? 33 
ATOM   10489 C CA  . LEU I  1 39  ? 22.235  -84.769  59.520  1.000 66.938  0 368 LEU III CA  1 ? 33 
ATOM   10490 C C   . LEU I  1 39  ? 22.393  -85.969  58.583  1.000 66.968  0 368 LEU III C   1 ? 33 
ATOM   10491 O O   . LEU I  1 39  ? 21.734  -85.966  57.514  1.000 67.277  0 368 LEU III O   1 ? 33 
ATOM   10492 C CB  . LEU I  1 39  ? 23.319  -83.721  59.241  1.000 63.745  0 368 LEU III CB  1 ? 33 
ATOM   10493 C CG  . LEU I  1 39  ? 23.233  -82.471  60.117  1.000 62.415  0 368 LEU III CG  1 ? 33 
ATOM   10494 C CD1 . LEU I  1 39  ? 24.330  -81.499  59.753  1.000 61.562  0 368 LEU III CD1 1 ? 33 
ATOM   10495 C CD2 . LEU I  1 39  ? 21.879  -81.800  59.999  1.000 62.388  0 368 LEU III CD2 1 ? 33 
ATOM   10496 N N   . TYR I  1 40  ? 23.231  -86.947  58.946  1.000 66.845  0 369 TYR III N   1 ? 33 
ATOM   10497 C CA  . TYR I  1 40  ? 23.519  -88.148  58.116  1.000 69.763  0 369 TYR III CA  1 ? 33 
ATOM   10498 C C   . TYR I  1 40  ? 22.236  -88.963  57.911  1.000 75.040  0 369 TYR III C   1 ? 33 
ATOM   10499 O O   . TYR I  1 40  ? 22.112  -89.619  56.862  1.000 78.497  0 369 TYR III O   1 ? 33 
ATOM   10500 C CB  . TYR I  1 40  ? 24.582  -89.045  58.759  1.000 69.154  0 369 TYR III CB  1 ? 33 
ATOM   10501 C CG  . TYR I  1 40  ? 25.993  -88.509  58.804  1.000 67.020  0 369 TYR III CG  1 ? 33 
ATOM   10502 C CD1 . TYR I  1 40  ? 26.476  -87.627  57.835  1.000 65.092  0 369 TYR III CD1 1 ? 33 
ATOM   10503 C CD2 . TYR I  1 40  ? 26.871  -88.922  59.798  1.000 66.175  0 369 TYR III CD2 1 ? 33 
ATOM   10504 C CE1 . TYR I  1 40  ? 27.784  -87.163  57.863  1.000 62.981  0 369 TYR III CE1 1 ? 33 
ATOM   10505 C CE2 . TYR I  1 40  ? 28.172  -88.447  59.857  1.000 64.842  0 369 TYR III CE2 1 ? 33 
ATOM   10506 C CZ  . TYR I  1 40  ? 28.639  -87.589  58.870  1.000 63.287  0 369 TYR III CZ  1 ? 33 
ATOM   10507 O OH  . TYR I  1 40  ? 29.925  -87.128  58.930  1.000 62.272  0 369 TYR III OH  1 ? 33 
ATOM   10508 N N   . ASN I  1 41  ? 21.318  -88.927  58.887  1.000 78.181  0 370 ASN III N   1 ? 33 
ATOM   10509 C CA  . ASN I  1 41  ? 20.106  -89.785  58.947  1.000 83.774  0 370 ASN III CA  1 ? 33 
ATOM   10510 C C   . ASN I  1 41  ? 18.888  -89.049  58.388  1.000 84.258  0 370 ASN III C   1 ? 33 
ATOM   10511 O O   . ASN I  1 41  ? 17.765  -89.558  58.585  1.000 87.630  0 370 ASN III O   1 ? 33 
ATOM   10512 C CB  . ASN I  1 41  ? 19.832  -90.234  60.383  1.000 86.303  0 370 ASN III CB  1 ? 33 
ATOM   10513 C CG  . ASN I  1 41  ? 20.913  -91.160  60.898  1.000 87.500  0 370 ASN III CG  1 ? 33 
ATOM   10514 O OD1 . ASN I  1 41  ? 21.411  -92.008  60.165  1.000 91.435  0 370 ASN III OD1 1 ? 33 
ATOM   10515 N ND2 . ASN I  1 41  ? 21.299  -90.995  62.148  1.000 86.683  0 370 ASN III ND2 1 ? 33 
ATOM   10516 N N   . SER I  1 42  ? 19.079  -87.894  57.747  1.000 82.160  0 371 SER III N   1 ? 33 
ATOM   10517 C CA  . SER I  1 42  ? 18.009  -87.113  57.075  1.000 84.328  0 371 SER III CA  1 ? 33 
ATOM   10518 C C   . SER I  1 42  ? 17.872  -87.561  55.621  1.000 86.895  0 371 SER III C   1 ? 33 
ATOM   10519 O O   . SER I  1 42  ? 18.911  -87.711  54.950  1.000 87.332  0 371 SER III O   1 ? 33 
ATOM   10520 C CB  . SER I  1 42  ? 18.264  -85.651  57.164  1.000 82.191  0 371 SER III CB  1 ? 33 
ATOM   10521 O OG  . SER I  1 42  ? 18.274  -85.268  58.528  1.000 83.999  0 371 SER III OG  1 ? 33 
ATOM   10522 N N   . ALA I  1 43  ? 16.628  -87.801  55.198  1.000 82.624  0 372 ALA III N   1 ? 34 
ATOM   10523 C CA  . ALA I  1 43  ? 16.258  -88.222  53.832  1.000 83.737  0 372 ALA III CA  1 ? 34 
ATOM   10524 C C   . ALA I  1 43  ? 15.669  -87.026  53.065  1.000 83.021  0 372 ALA III C   1 ? 34 
ATOM   10525 O O   . ALA I  1 43  ? 15.403  -87.187  51.881  1.000 84.928  0 372 ALA III O   1 ? 34 
ATOM   10526 C CB  . ALA I  1 43  ? 15.290  -89.362  53.918  1.000 85.007  0 372 ALA III CB  1 ? 34 
ATOM   10527 N N   . SER I  1 44  ? 15.561  -85.865  53.707  1.000 81.713  0 373 SER III N   1 ? 34 
ATOM   10528 C CA  . SER I  1 44  ? 14.902  -84.670  53.123  1.000 81.524  0 373 SER III CA  1 ? 34 
ATOM   10529 C C   . SER I  1 44  ? 15.900  -83.820  52.312  1.000 78.587  0 373 SER III C   1 ? 34 
ATOM   10530 O O   . SER I  1 44  ? 15.409  -83.103  51.434  1.000 79.350  0 373 SER III O   1 ? 34 
ATOM   10531 C CB  . SER I  1 44  ? 14.222  -83.844  54.189  1.000 81.634  0 373 SER III CB  1 ? 34 
ATOM   10532 O OG  . SER I  1 44  ? 15.017  -83.765  55.376  1.000 80.303  0 373 SER III OG  1 ? 34 
ATOM   10533 N N   . PHE I  1 45  ? 17.201  -83.875  52.615  1.000 73.925  0 374 PHE III N   1 ? 34 
ATOM   10534 C CA  . PHE I  1 45  ? 18.116  -82.821  52.103  1.000 68.250  0 374 PHE III CA  1 ? 34 
ATOM   10535 C C   . PHE I  1 45  ? 18.260  -82.975  50.589  1.000 65.725  0 374 PHE III C   1 ? 34 
ATOM   10536 O O   . PHE I  1 45  ? 18.515  -84.091  50.136  1.000 64.572  0 374 PHE III O   1 ? 34 
ATOM   10537 C CB  . PHE I  1 45  ? 19.472  -82.856  52.809  1.000 68.437  0 374 PHE III CB  1 ? 34 
ATOM   10538 C CG  . PHE I  1 45  ? 19.432  -82.533  54.282  1.000 70.498  0 374 PHE III CG  1 ? 34 
ATOM   10539 C CD1 . PHE I  1 45  ? 18.589  -81.552  54.790  1.000 69.627  0 374 PHE III CD1 1 ? 34 
ATOM   10540 C CD2 . PHE I  1 45  ? 20.298  -83.169  55.156  1.000 71.510  0 374 PHE III CD2 1 ? 34 
ATOM   10541 C CE1 . PHE I  1 45  ? 18.606  -81.235  56.134  1.000 69.029  0 374 PHE III CE1 1 ? 34 
ATOM   10542 C CE2 . PHE I  1 45  ? 20.315  -82.843  56.503  1.000 71.192  0 374 PHE III CE2 1 ? 34 
ATOM   10543 C CZ  . PHE I  1 45  ? 19.474  -81.870  56.984  1.000 69.532  0 374 PHE III CZ  1 ? 34 
ATOM   10544 N N   . SER I  1 46  ? 18.092  -81.880  49.836  1.000 63.688  0 375 SER III N   1 ? 34 
ATOM   10545 C CA  . SER I  1 46  ? 18.212  -81.851  48.354  1.000 62.990  0 375 SER III CA  1 ? 34 
ATOM   10546 C C   . SER I  1 46  ? 19.689  -81.882  47.964  1.000 57.595  0 375 SER III C   1 ? 34 
ATOM   10547 O O   . SER I  1 46  ? 20.011  -82.385  46.912  1.000 56.429  0 375 SER III O   1 ? 34 
ATOM   10548 C CB  . SER I  1 46  ? 17.508  -80.645  47.759  1.000 64.243  0 375 SER III CB  1 ? 34 
ATOM   10549 O OG  . SER I  1 46  ? 17.998  -79.427  48.307  1.000 64.349  0 375 SER III OG  1 ? 34 
ATOM   10550 N N   . THR I  1 47  ? 20.548  -81.335  48.813  1.000 55.544  0 376 THR III N   1 ? 34 
ATOM   10551 C CA  . THR I  1 47  ? 22.008  -81.207  48.571  1.000 53.580  0 376 THR III CA  1 ? 34 
ATOM   10552 C C   . THR I  1 47  ? 22.727  -81.192  49.923  1.000 51.792  0 376 THR III C   1 ? 34 
ATOM   10553 O O   . THR I  1 47  ? 22.151  -80.678  50.923  1.000 52.469  0 376 THR III O   1 ? 34 
ATOM   10554 C CB  . THR I  1 47  ? 22.290  -79.970  47.707  1.000 51.146  0 376 THR III CB  1 ? 34 
ATOM   10555 O OG1 . THR I  1 47  ? 23.638  -79.990  47.232  1.000 49.960  0 376 THR III OG1 1 ? 34 
ATOM   10556 C CG2 . THR I  1 47  ? 22.026  -78.689  48.462  1.000 49.903  0 376 THR III CG2 1 ? 34 
ATOM   10557 N N   . PHE I  1 48  ? 23.915  -81.776  49.966  1.000 50.214  0 377 PHE III N   1 ? 34 
ATOM   10558 C CA  . PHE I  1 48  ? 24.747  -81.824  51.193  1.000 50.244  0 377 PHE III CA  1 ? 34 
ATOM   10559 C C   . PHE I  1 48  ? 26.178  -82.006  50.703  1.000 48.900  0 377 PHE III C   1 ? 34 
ATOM   10560 O O   . PHE I  1 48  ? 26.581  -83.158  50.439  1.000 50.818  0 377 PHE III O   1 ? 34 
ATOM   10561 C CB  . PHE I  1 48  ? 24.244  -82.919  52.139  1.000 52.487  0 377 PHE III CB  1 ? 34 
ATOM   10562 C CG  . PHE I  1 48  ? 24.994  -83.117  53.437  1.000 52.143  0 377 PHE III CG  1 ? 34 
ATOM   10563 C CD1 . PHE I  1 48  ? 26.211  -82.509  53.688  1.000 49.615  0 377 PHE III CD1 1 ? 34 
ATOM   10564 C CD2 . PHE I  1 48  ? 24.478  -83.961  54.410  1.000 54.198  0 377 PHE III CD2 1 ? 34 
ATOM   10565 C CE1 . PHE I  1 48  ? 26.878  -82.708  54.889  1.000 49.818  0 377 PHE III CE1 1 ? 34 
ATOM   10566 C CE2 . PHE I  1 48  ? 25.145  -84.160  55.609  1.000 54.679  0 377 PHE III CE2 1 ? 34 
ATOM   10567 C CZ  . PHE I  1 48  ? 26.354  -83.538  55.843  1.000 51.844  0 377 PHE III CZ  1 ? 34 
ATOM   10568 N N   . LYS I  1 49  ? 26.868  -80.890  50.488  1.000 45.224  0 378 LYS III N   1 ? 34 
ATOM   10569 C CA  . LYS I  1 49  ? 28.259  -80.904  49.991  1.000 46.599  0 378 LYS III CA  1 ? 34 
ATOM   10570 C C   . LYS I  1 49  ? 29.169  -80.154  50.957  1.000 45.905  0 378 LYS III C   1 ? 34 
ATOM   10571 O O   . LYS I  1 49  ? 28.757  -79.113  51.500  1.000 45.985  0 378 LYS III O   1 ? 34 
ATOM   10572 C CB  . LYS I  1 49  ? 28.389  -80.203  48.644  1.000 48.274  0 378 LYS III CB  1 ? 34 
ATOM   10573 C CG  . LYS I  1 49  ? 27.501  -80.721  47.521  1.000 50.049  0 378 LYS III CG  1 ? 34 
ATOM   10574 C CD  . LYS I  1 49  ? 27.641  -79.833  46.342  1.000 49.615  0 378 LYS III CD  1 ? 34 
ATOM   10575 C CE  . LYS I  1 49  ? 26.958  -80.356  45.110  1.000 52.512  0 378 LYS III CE  1 ? 34 
ATOM   10576 N NZ  . LYS I  1 49  ? 27.080  -79.365  44.014  1.000 51.179  0 378 LYS III NZ  1 ? 34 
ATOM   10577 N N   . CYS I  1 50  ? 30.400  -80.628  51.088  1.000 45.516  0 379 CYS III N   1 ? 34 
ATOM   10578 C CA  . CYS I  1 50  ? 31.459  -79.953  51.864  1.000 45.140  0 379 CYS III CA  1 ? 34 
ATOM   10579 C C   . CYS I  1 50  ? 32.580  -79.535  50.907  1.000 43.174  0 379 CYS III C   1 ? 34 
ATOM   10580 O O   . CYS I  1 50  ? 32.726  -80.126  49.815  1.000 43.327  0 379 CYS III O   1 ? 34 
ATOM   10581 C CB  . CYS I  1 50  ? 31.914  -80.837  53.026  1.000 47.483  0 379 CYS III CB  1 ? 34 
ATOM   10582 S SG  . CYS I  1 50  ? 30.533  -81.274  54.124  1.000 51.335  0 379 CYS III SG  1 ? 34 
ATOM   10583 N N   . TYR I  1 51  ? 33.319  -78.516  51.324  1.000 40.825  0 380 TYR III N   1 ? 34 
ATOM   10584 C CA  . TYR I  1 51  ? 34.434  -77.862  50.604  1.000 40.695  0 380 TYR III CA  1 ? 34 
ATOM   10585 C C   . TYR I  1 51  ? 35.632  -77.831  51.562  1.000 39.542  0 380 TYR III C   1 ? 34 
ATOM   10586 O O   . TYR I  1 51  ? 35.478  -77.319  52.672  1.000 42.148  0 380 TYR III O   1 ? 34 
ATOM   10587 C CB  . TYR I  1 51  ? 33.943  -76.482  50.132  1.000 40.508  0 380 TYR III CB  1 ? 34 
ATOM   10588 C CG  . TYR I  1 51  ? 32.689  -76.532  49.284  1.000 40.461  0 380 TYR III CG  1 ? 34 
ATOM   10589 C CD1 . TYR I  1 51  ? 31.428  -76.563  49.861  1.000 41.701  0 380 TYR III CD1 1 ? 34 
ATOM   10590 C CD2 . TYR I  1 51  ? 32.755  -76.616  47.914  1.000 39.157  0 380 TYR III CD2 1 ? 34 
ATOM   10591 C CE1 . TYR I  1 51  ? 30.271  -76.618  49.103  1.000 41.747  0 380 TYR III CE1 1 ? 34 
ATOM   10592 C CE2 . TYR I  1 51  ? 31.616  -76.680  47.138  1.000 41.372  0 380 TYR III CE2 1 ? 34 
ATOM   10593 C CZ  . TYR I  1 51  ? 30.368  -76.662  47.728  1.000 42.032  0 380 TYR III CZ  1 ? 34 
ATOM   10594 O OH  . TYR I  1 51  ? 29.260  -76.722  46.937  1.000 42.952  0 380 TYR III OH  1 ? 34 
ATOM   10595 N N   . GLY I  1 52  ? 36.779  -78.382  51.170  1.000 38.367  0 381 GLY III N   1 ? 34 
ATOM   10596 C CA  . GLY I  1 52  ? 37.990  -78.423  51.994  1.000 38.881  0 381 GLY III CA  1 ? 34 
ATOM   10597 C C   . GLY I  1 52  ? 37.967  -79.515  53.061  1.000 43.220  0 381 GLY III C   1 ? 34 
ATOM   10598 O O   . GLY I  1 52  ? 39.008  -79.694  53.701  1.000 43.119  0 381 GLY III O   1 ? 34 
ATOM   10599 N N   . VAL I  1 53  ? 36.848  -80.233  53.260  1.000 45.298  0 382 VAL III N   1 ? 34 
ATOM   10600 C CA  . VAL I  1 53  ? 36.797  -81.439  54.144  1.000 45.326  0 382 VAL III CA  1 ? 34 
ATOM   10601 C C   . VAL I  1 53  ? 35.822  -82.451  53.554  1.000 44.780  0 382 VAL III C   1 ? 34 
ATOM   10602 O O   . VAL I  1 53  ? 34.862  -82.007  52.906  1.000 45.570  0 382 VAL III O   1 ? 34 
ATOM   10603 C CB  . VAL I  1 53  ? 36.362  -81.050  55.567  1.000 46.278  0 382 VAL III CB  1 ? 34 
ATOM   10604 C CG1 . VAL I  1 53  ? 37.378  -80.155  56.244  1.000 45.870  0 382 VAL III CG1 1 ? 34 
ATOM   10605 C CG2 . VAL I  1 53  ? 35.010  -80.365  55.600  1.000 46.462  0 382 VAL III CG2 1 ? 34 
ATOM   10606 N N   . SER I  1 54  ? 36.027  -83.741  53.776  1.000 44.529  0 383 SER III N   1 ? 34 
ATOM   10607 C CA  . SER I  1 54  ? 35.088  -84.783  53.299  1.000 45.636  0 383 SER III CA  1 ? 34 
ATOM   10608 C C   . SER I  1 54  ? 33.899  -84.831  54.260  1.000 48.736  0 383 SER III C   1 ? 34 
ATOM   10609 O O   . SER I  1 54  ? 34.098  -84.824  55.471  1.000 50.720  0 383 SER III O   1 ? 34 
ATOM   10610 C CB  . SER I  1 54  ? 35.748  -86.129  53.181  1.000 46.394  0 383 SER III CB  1 ? 34 
ATOM   10611 O OG  . SER I  1 54  ? 34.795  -87.108  52.807  1.000 46.229  0 383 SER III OG  1 ? 34 
ATOM   10612 N N   . PRO I  1 55  ? 32.644  -84.884  53.765  1.000 48.374  0 384 PRO III N   1 ? 34 
ATOM   10613 C CA  . PRO I  1 55  ? 31.480  -85.092  54.629  1.000 50.365  0 384 PRO III CA  1 ? 34 
ATOM   10614 C C   . PRO I  1 55  ? 31.596  -86.330  55.521  1.000 53.540  0 384 PRO III C   1 ? 34 
ATOM   10615 O O   . PRO I  1 55  ? 31.010  -86.349  56.603  1.000 55.838  0 384 PRO III O   1 ? 34 
ATOM   10616 C CB  . PRO I  1 55  ? 30.330  -85.312  53.619  1.000 50.864  0 384 PRO III CB  1 ? 34 
ATOM   10617 C CG  . PRO I  1 55  ? 30.779  -84.573  52.367  1.000 49.015  0 384 PRO III CG  1 ? 34 
ATOM   10618 C CD  . PRO I  1 55  ? 32.278  -84.737  52.343  1.000 48.502  0 384 PRO III CD  1 ? 34 
ATOM   10619 N N   . THR I  1 56  ? 32.339  -87.338  55.055  1.000 54.694  0 385 THR III N   1 ? 34 
ATOM   10620 C CA  . THR I  1 56  ? 32.533  -88.627  55.767  1.000 57.904  0 385 THR III CA  1 ? 34 
ATOM   10621 C C   . THR I  1 56  ? 33.395  -88.411  57.015  1.000 58.420  0 385 THR III C   1 ? 34 
ATOM   10622 O O   . THR I  1 56  ? 33.423  -89.313  57.847  1.000 61.871  0 385 THR III O   1 ? 34 
ATOM   10623 C CB  . THR I  1 56  ? 33.157  -89.701  54.860  1.000 58.133  0 385 THR III CB  1 ? 34 
ATOM   10624 O OG1 . THR I  1 56  ? 34.487  -89.329  54.487  1.000 56.750  0 385 THR III OG1 1 ? 34 
ATOM   10625 C CG2 . THR I  1 56  ? 32.326  -89.959  53.619  1.000 57.917  0 385 THR III CG2 1 ? 34 
ATOM   10626 N N   . LYS I  1 57  ? 34.088  -87.281  57.136  1.000 57.885  0 386 LYS III N   1 ? 34 
ATOM   10627 C CA  . LYS I  1 57  ? 35.065  -87.081  58.230  1.000 60.208  0 386 LYS III CA  1 ? 34 
ATOM   10628 C C   . LYS I  1 57  ? 34.564  -86.037  59.225  1.000 58.191  0 386 LYS III C   1 ? 34 
ATOM   10629 O O   . LYS I  1 57  ? 35.281  -85.760  60.146  1.000 58.114  0 386 LYS III O   1 ? 34 
ATOM   10630 C CB  . LYS I  1 57  ? 36.431  -86.670  57.685  1.000 61.757  0 386 LYS III CB  1 ? 34 
ATOM   10631 C CG  . LYS I  1 57  ? 37.071  -87.659  56.731  1.000 65.558  0 386 LYS III CG  1 ? 34 
ATOM   10632 C CD  . LYS I  1 57  ? 37.717  -88.840  57.387  1.000 72.240  0 386 LYS III CD  1 ? 34 
ATOM   10633 C CE  . LYS I  1 57  ? 38.975  -88.409  58.104  1.000 79.373  0 386 LYS III CE  1 ? 34 
ATOM   10634 N NZ  . LYS I  1 57  ? 39.118  -89.097  59.408  1.000 82.490  0 386 LYS III NZ  1 ? 34 
ATOM   10635 N N   . LEU I  1 58  ? 33.356  -85.503  59.078  1.000 56.389  0 387 LEU III N   1 ? 34 
ATOM   10636 C CA  . LEU I  1 58  ? 32.873  -84.414  59.958  1.000 57.106  0 387 LEU III CA  1 ? 34 
ATOM   10637 C C   . LEU I  1 58  ? 32.876  -84.848  61.428  1.000 60.871  0 387 LEU III C   1 ? 34 
ATOM   10638 O O   . LEU I  1 58  ? 33.154  -83.993  62.282  1.000 64.549  0 387 LEU III O   1 ? 34 
ATOM   10639 C CB  . LEU I  1 58  ? 31.495  -83.974  59.483  1.000 56.313  0 387 LEU III CB  1 ? 34 
ATOM   10640 C CG  . LEU I  1 58  ? 31.476  -83.219  58.150  1.000 54.388  0 387 LEU III CG  1 ? 34 
ATOM   10641 C CD1 . LEU I  1 58  ? 30.067  -82.789  57.817  1.000 53.954  0 387 LEU III CD1 1 ? 34 
ATOM   10642 C CD2 . LEU I  1 58  ? 32.407  -81.999  58.151  1.000 53.266  0 387 LEU III CD2 1 ? 34 
ATOM   10643 N N   . ASN I  1 59  ? 32.638  -86.119  61.735  1.000 63.328  0 388 ASN III N   1 ? 34 
ATOM   10644 C CA  . ASN I  1 59  ? 32.617  -86.599  63.146  1.000 65.110  0 388 ASN III CA  1 ? 34 
ATOM   10645 C C   . ASN I  1 59  ? 34.034  -86.768  63.710  1.000 65.539  0 388 ASN III C   1 ? 34 
ATOM   10646 O O   . ASN I  1 59  ? 34.138  -87.037  64.908  1.000 67.050  0 388 ASN III O   1 ? 34 
ATOM   10647 C CB  . ASN I  1 59  ? 31.787  -87.870  63.320  1.000 66.402  0 388 ASN III CB  1 ? 34 
ATOM   10648 C CG  . ASN I  1 59  ? 30.326  -87.544  63.547  1.000 66.906  0 388 ASN III CG  1 ? 34 
ATOM   10649 O OD1 . ASN I  1 59  ? 29.965  -86.402  63.801  1.000 67.510  0 388 ASN III OD1 1 ? 34 
ATOM   10650 N ND2 . ASN I  1 59  ? 29.453  -88.515  63.415  1.000 69.609  0 388 ASN III ND2 1 ? 34 
ATOM   10651 N N   . ASP I  1 60  ? 35.083  -86.552  62.920  1.000 64.382  0 389 ASP III N   1 ? 34 
ATOM   10652 C CA  . ASP I  1 60  ? 36.493  -86.783  63.340  1.000 63.887  0 389 ASP III CA  1 ? 34 
ATOM   10653 C C   . ASP I  1 60  ? 37.291  -85.483  63.359  1.000 60.309  0 389 ASP III C   1 ? 34 
ATOM   10654 O O   . ASP I  1 60  ? 38.461  -85.577  63.666  1.000 60.096  0 389 ASP III O   1 ? 34 
ATOM   10655 C CB  . ASP I  1 60  ? 37.208  -87.751  62.401  1.000 65.715  0 389 ASP III CB  1 ? 34 
ATOM   10656 C CG  . ASP I  1 60  ? 36.518  -89.098  62.303  1.000 71.757  0 389 ASP III CG  1 ? 34 
ATOM   10657 O OD1 . ASP I  1 60  ? 36.406  -89.768  63.356  1.000 76.022  0 389 ASP III OD1 1 ? 34 
ATOM   10658 O OD2 . ASP I  1 60  ? 36.061  -89.453  61.188  1.000 77.723  0 389 ASP III OD2 1 ? 34 
ATOM   10659 N N   . LEU I  1 61  ? 36.696  -84.331  63.046  1.000 58.099  0 390 LEU III N   1 ? 34 
ATOM   10660 C CA  . LEU I  1 61  ? 37.470  -83.080  62.848  1.000 56.183  0 390 LEU III CA  1 ? 34 
ATOM   10661 C C   . LEU I  1 61  ? 37.205  -82.075  63.965  1.000 55.864  0 390 LEU III C   1 ? 34 
ATOM   10662 O O   . LEU I  1 61  ? 36.131  -82.087  64.535  1.000 55.937  0 390 LEU III O   1 ? 34 
ATOM   10663 C CB  . LEU I  1 61  ? 37.126  -82.493  61.480  1.000 55.891  0 390 LEU III CB  1 ? 34 
ATOM   10664 C CG  . LEU I  1 61  ? 37.594  -83.322  60.278  1.000 57.965  0 390 LEU III CG  1 ? 34 
ATOM   10665 C CD1 . LEU I  1 61  ? 37.230  -82.601  58.978  1.000 56.525  0 390 LEU III CD1 1 ? 34 
ATOM   10666 C CD2 . LEU I  1 61  ? 39.094  -83.619  60.304  1.000 58.256  0 390 LEU III CD2 1 ? 34 
ATOM   10667 N N   . CYS I  1 62  ? 38.198  -81.237  64.248  1.000 56.019  0 391 CYS III N   1 ? 34 
ATOM   10668 C CA  . CYS I  1 62  ? 38.141  -80.126  65.230  1.000 56.484  0 391 CYS III CA  1 ? 34 
ATOM   10669 C C   . CYS I  1 62  ? 38.299  -78.796  64.495  1.000 53.134  0 391 CYS III C   1 ? 34 
ATOM   10670 O O   . CYS I  1 62  ? 39.060  -78.764  63.542  1.000 52.065  0 391 CYS III O   1 ? 34 
ATOM   10671 C CB  . CYS I  1 62  ? 39.223  -80.294  66.282  1.000 59.066  0 391 CYS III CB  1 ? 34 
ATOM   10672 S SG  . CYS I  1 62  ? 38.885  -81.701  67.364  1.000 64.858  0 391 CYS III SG  1 ? 34 
ATOM   10673 N N   . PHE I  1 63  ? 37.571  -77.773  64.925  1.000 51.626  0 392 PHE III N   1 ? 34 
ATOM   10674 C CA  . PHE I  1 63  ? 37.593  -76.410  64.345  1.000 49.187  0 392 PHE III CA  1 ? 34 
ATOM   10675 C C   . PHE I  1 63  ? 37.714  -75.397  65.484  1.000 49.538  0 392 PHE III C   1 ? 34 
ATOM   10676 O O   . PHE I  1 63  ? 37.310  -75.711  66.617  1.000 52.708  0 392 PHE III O   1 ? 34 
ATOM   10677 C CB  . PHE I  1 63  ? 36.369  -76.180  63.454  1.000 46.186  0 392 PHE III CB  1 ? 34 
ATOM   10678 C CG  . PHE I  1 63  ? 36.257  -77.197  62.347  1.000 44.503  0 392 PHE III CG  1 ? 34 
ATOM   10679 C CD1 . PHE I  1 63  ? 37.146  -77.171  61.288  1.000 43.507  0 392 PHE III CD1 1 ? 34 
ATOM   10680 C CD2 . PHE I  1 63  ? 35.301  -78.199  62.374  1.000 44.667  0 392 PHE III CD2 1 ? 34 
ATOM   10681 C CE1 . PHE I  1 63  ? 37.065  -78.107  60.266  1.000 43.407  0 392 PHE III CE1 1 ? 34 
ATOM   10682 C CE2 . PHE I  1 63  ? 35.220  -79.134  61.356  1.000 43.474  0 392 PHE III CE2 1 ? 34 
ATOM   10683 C CZ  . PHE I  1 63  ? 36.113  -79.102  60.314  1.000 44.251  0 392 PHE III CZ  1 ? 34 
ATOM   10684 N N   . THR I  1 64  ? 38.314  -74.248  65.176  1.000 49.909  0 393 THR III N   1 ? 34 
ATOM   10685 C CA  . THR I  1 64  ? 38.497  -73.131  66.133  1.000 52.247  0 393 THR III CA  1 ? 34 
ATOM   10686 C C   . THR I  1 64  ? 37.164  -72.427  66.298  1.000 52.497  0 393 THR III C   1 ? 34 
ATOM   10687 O O   . THR I  1 64  ? 36.916  -71.954  67.387  1.000 53.883  0 393 THR III O   1 ? 34 
ATOM   10688 C CB  . THR I  1 64  ? 39.674  -72.264  65.706  1.000 51.716  0 393 THR III CB  1 ? 34 
ATOM   10689 O OG1 . THR I  1 64  ? 39.616  -72.038  64.301  1.000 48.441  0 393 THR III OG1 1 ? 34 
ATOM   10690 C CG2 . THR I  1 64  ? 40.962  -73.005  65.972  1.000 54.826  0 393 THR III CG2 1 ? 34 
ATOM   10691 N N   . ASN I  1 65  ? 36.337  -72.422  65.257  1.000 52.581  0 394 ASN III N   1 ? 34 
ATOM   10692 C CA  . ASN I  1 65  ? 35.026  -71.729  65.254  1.000 54.113  0 394 ASN III CA  1 ? 34 
ATOM   10693 C C   . ASN I  1 65  ? 34.131  -72.338  64.182  1.000 50.063  0 394 ASN III C   1 ? 34 
ATOM   10694 O O   . ASN I  1 65  ? 34.705  -72.791  63.174  1.000 47.787  0 394 ASN III O   1 ? 34 
ATOM   10695 C CB  . ASN I  1 65  ? 35.192  -70.223  65.029  1.000 56.882  0 394 ASN III CB  1 ? 34 
ATOM   10696 C CG  . ASN I  1 65  ? 33.949  -69.451  65.397  1.000 60.711  0 394 ASN III CG  1 ? 34 
ATOM   10697 O OD1 . ASN I  1 65  ? 33.572  -69.443  66.587  1.000 63.034  0 394 ASN III OD1 1 ? 34 
ATOM   10698 N ND2 . ASN I  1 65  ? 33.283  -68.892  64.381  1.000 59.929  0 394 ASN III ND2 1 ? 34 
ATOM   10699 N N   . VAL I  1 66  ? 32.821  -72.393  64.414  1.000 50.080  0 395 VAL III N   1 ? 34 
ATOM   10700 C CA  . VAL I  1 66  ? 31.856  -72.781  63.358  1.000 51.537  0 395 VAL III CA  1 ? 34 
ATOM   10701 C C   . VAL I  1 66  ? 30.758  -71.720  63.313  1.000 52.166  0 395 VAL III C   1 ? 34 
ATOM   10702 O O   . VAL I  1 66  ? 30.273  -71.307  64.408  1.000 51.772  0 395 VAL III O   1 ? 34 
ATOM   10703 C CB  . VAL I  1 66  ? 31.262  -74.184  63.594  1.000 52.351  0 395 VAL III CB  1 ? 34 
ATOM   10704 C CG1 . VAL I  1 66  ? 30.268  -74.556  62.500  1.000 48.365  0 395 VAL III CG1 1 ? 34 
ATOM   10705 C CG2 . VAL I  1 66  ? 32.350  -75.245  63.784  1.000 51.729  0 395 VAL III CG2 1 ? 34 
ATOM   10706 N N   . TYR I  1 67  ? 30.370  -71.289  62.109  1.000 50.318  0 396 TYR III N   1 ? 34 
ATOM   10707 C CA  . TYR I  1 67  ? 29.206  -70.411  61.895  1.000 50.776  0 396 TYR III CA  1 ? 34 
ATOM   10708 C C   . TYR I  1 67  ? 28.164  -71.167  61.082  1.000 51.484  0 396 TYR III C   1 ? 34 
ATOM   10709 O O   . TYR I  1 67  ? 28.527  -71.853  60.103  1.000 48.905  0 396 TYR III O   1 ? 34 
ATOM   10710 C CB  . TYR I  1 67  ? 29.645  -69.125  61.194  1.000 52.598  0 396 TYR III CB  1 ? 34 
ATOM   10711 C CG  . TYR I  1 67  ? 30.459  -68.236  62.094  1.000 57.075  0 396 TYR III CG  1 ? 34 
ATOM   10712 C CD1 . TYR I  1 67  ? 29.908  -67.721  63.255  1.000 58.019  0 396 TYR III CD1 1 ? 34 
ATOM   10713 C CD2 . TYR I  1 67  ? 31.686  -67.743  61.699  1.000 59.727  0 396 TYR III CD2 1 ? 34 
ATOM   10714 C CE1 . TYR I  1 67  ? 30.605  -66.854  64.068  1.000 62.753  0 396 TYR III CE1 1 ? 34 
ATOM   10715 C CE2 . TYR I  1 67  ? 32.425  -66.910  62.524  1.000 64.903  0 396 TYR III CE2 1 ? 34 
ATOM   10716 C CZ  . TYR I  1 67  ? 31.874  -66.452  63.711  1.000 65.581  0 396 TYR III CZ  1 ? 34 
ATOM   10717 O OH  . TYR I  1 67  ? 32.562  -65.628  64.550  1.000 72.945  0 396 TYR III OH  1 ? 34 
ATOM   10718 N N   . ALA I  1 68  ? 26.902  -71.029  61.479  1.000 51.624  0 397 ALA III N   1 ? 34 
ATOM   10719 C CA  . ALA I  1 68  ? 25.726  -71.524  60.735  1.000 51.427  0 397 ALA III CA  1 ? 34 
ATOM   10720 C C   . ALA I  1 68  ? 24.958  -70.305  60.209  1.000 50.806  0 397 ALA III C   1 ? 34 
ATOM   10721 O O   . ALA I  1 68  ? 24.349  -69.573  61.012  1.000 53.518  0 397 ALA III O   1 ? 34 
ATOM   10722 C CB  . ALA I  1 68  ? 24.875  -72.396  61.614  1.000 52.628  0 397 ALA III CB  1 ? 34 
ATOM   10723 N N   . ASP I  1 69  ? 25.042  -70.088  58.903  1.000 46.431  0 398 ASP III N   1 ? 34 
ATOM   10724 C CA  . ASP I  1 69  ? 24.251  -69.091  58.150  1.000 47.395  0 398 ASP III CA  1 ? 34 
ATOM   10725 C C   . ASP I  1 69  ? 23.034  -69.819  57.578  1.000 47.642  0 398 ASP III C   1 ? 34 
ATOM   10726 O O   . ASP I  1 69  ? 23.197  -70.912  57.031  1.000 44.731  0 398 ASP III O   1 ? 34 
ATOM   10727 C CB  . ASP I  1 69  ? 25.103  -68.441  57.057  1.000 47.536  0 398 ASP III CB  1 ? 34 
ATOM   10728 C CG  . ASP I  1 69  ? 26.372  -67.784  57.583  1.000 47.244  0 398 ASP III CG  1 ? 34 
ATOM   10729 O OD1 . ASP I  1 69  ? 26.345  -67.349  58.751  1.000 48.894  0 398 ASP III OD1 1 ? 34 
ATOM   10730 O OD2 . ASP I  1 69  ? 27.395  -67.743  56.826  1.000 49.583  0 398 ASP III OD2 1 ? 34 
ATOM   10731 N N   . SER I  1 70  ? 21.852  -69.244  57.710  1.000 51.084  0 399 SER III N   1 ? 34 
ATOM   10732 C CA  . SER I  1 70  ? 20.611  -69.858  57.190  1.000 53.895  0 399 SER III CA  1 ? 34 
ATOM   10733 C C   . SER I  1 70  ? 19.715  -68.785  56.567  1.000 54.951  0 399 SER III C   1 ? 34 
ATOM   10734 O O   . SER I  1 70  ? 19.751  -67.596  57.021  1.000 54.991  0 399 SER III O   1 ? 34 
ATOM   10735 C CB  . SER I  1 70  ? 19.917  -70.619  58.268  1.000 54.528  0 399 SER III CB  1 ? 34 
ATOM   10736 O OG  . SER I  1 70  ? 19.655  -69.779  59.379  1.000 56.482  0 399 SER III OG  1 ? 34 
ATOM   10737 N N   . PHE I  1 71  ? 18.925  -69.202  55.579  1.000 55.331  0 400 PHE III N   1 ? 34 
ATOM   10738 C CA  . PHE I  1 71  ? 18.030  -68.305  54.811  1.000 55.968  0 400 PHE III CA  1 ? 34 
ATOM   10739 C C   . PHE I  1 71  ? 17.174  -69.132  53.854  1.000 56.319  0 400 PHE III C   1 ? 34 
ATOM   10740 O O   . PHE I  1 71  ? 17.414  -70.350  53.744  1.000 54.921  0 400 PHE III O   1 ? 34 
ATOM   10741 C CB  . PHE I  1 71  ? 18.868  -67.289  54.032  1.000 55.161  0 400 PHE III CB  1 ? 34 
ATOM   10742 C CG  . PHE I  1 71  ? 20.009  -67.895  53.246  1.000 53.915  0 400 PHE III CG  1 ? 34 
ATOM   10743 C CD1 . PHE I  1 71  ? 19.791  -68.494  52.014  1.000 53.327  0 400 PHE III CD1 1 ? 34 
ATOM   10744 C CD2 . PHE I  1 71  ? 21.305  -67.861  53.739  1.000 53.383  0 400 PHE III CD2 1 ? 34 
ATOM   10745 C CE1 . PHE I  1 71  ? 20.843  -69.037  51.295  1.000 51.857  0 400 PHE III CE1 1 ? 34 
ATOM   10746 C CE2 . PHE I  1 71  ? 22.356  -68.400  53.013  1.000 51.219  0 400 PHE III CE2 1 ? 34 
ATOM   10747 C CZ  . PHE I  1 71  ? 22.118  -68.995  51.798  1.000 50.407  0 400 PHE III CZ  1 ? 34 
ATOM   10748 N N   . VAL I  1 72  ? 16.255  -68.462  53.152  1.000 56.582  0 401 VAL III N   1 ? 34 
ATOM   10749 C CA  . VAL I  1 72  ? 15.392  -69.075  52.111  1.000 59.408  0 401 VAL III CA  1 ? 34 
ATOM   10750 C C   . VAL I  1 72  ? 15.729  -68.461  50.743  1.000 57.975  0 401 VAL III C   1 ? 34 
ATOM   10751 O O   . VAL I  1 72  ? 15.889  -67.231  50.649  1.000 55.588  0 401 VAL III O   1 ? 34 
ATOM   10752 C CB  . VAL I  1 72  ? 13.907  -68.907  52.474  1.000 63.535  0 401 VAL III CB  1 ? 34 
ATOM   10753 C CG1 . VAL I  1 72  ? 12.997  -69.270  51.306  1.000 66.500  0 401 VAL III CG1 1 ? 34 
ATOM   10754 C CG2 . VAL I  1 72  ? 13.560  -69.720  53.709  1.000 65.559  0 401 VAL III CG2 1 ? 34 
ATOM   10755 N N   . ILE I  1 73  ? 15.790  -69.311  49.720  1.000 57.339  0 402 ILE III N   1 ? 34 
ATOM   10756 C CA  . ILE I  1 73  ? 15.918  -68.932  48.286  1.000 57.926  0 402 ILE III CA  1 ? 34 
ATOM   10757 C C   . ILE I  1 73  ? 15.034  -69.869  47.452  1.000 62.034  0 402 ILE III C   1 ? 34 
ATOM   10758 O O   . ILE I  1 73  ? 14.420  -70.765  48.034  1.000 63.819  0 402 ILE III O   1 ? 34 
ATOM   10759 C CB  . ILE I  1 73  ? 17.401  -68.955  47.849  1.000 54.329  0 402 ILE III CB  1 ? 34 
ATOM   10760 C CG1 . ILE I  1 73  ? 18.068  -70.293  48.166  1.000 51.768  0 402 ILE III CG1 1 ? 34 
ATOM   10761 C CG2 . ILE I  1 73  ? 18.159  -67.796  48.473  1.000 53.651  0 402 ILE III CG2 1 ? 34 
ATOM   10762 C CD1 . ILE I  1 73  ? 19.445  -70.426  47.598  1.000 50.922  0 402 ILE III CD1 1 ? 34 
ATOM   10763 N N   . ARG I  1 74  ? 14.946  -69.645  46.141  1.000 65.525  0 403 ARG III N   1 ? 34 
ATOM   10764 C CA  . ARG I  1 74  ? 14.283  -70.552  45.170  1.000 69.621  0 403 ARG III CA  1 ? 34 
ATOM   10765 C C   . ARG I  1 74  ? 15.138  -71.796  44.957  1.000 66.106  0 403 ARG III C   1 ? 34 
ATOM   10766 O O   . ARG I  1 74  ? 16.372  -71.690  45.046  1.000 60.674  0 403 ARG III O   1 ? 34 
ATOM   10767 C CB  . ARG I  1 74  ? 14.176  -69.933  43.777  1.000 74.551  0 403 ARG III CB  1 ? 34 
ATOM   10768 C CG  . ARG I  1 74  ? 13.095  -68.878  43.610  1.000 78.642  0 403 ARG III CG  1 ? 34 
ATOM   10769 C CD  . ARG I  1 74  ? 13.385  -68.022  42.394  1.000 80.674  0 403 ARG III CD  1 ? 34 
ATOM   10770 N NE  . ARG I  1 74  ? 13.570  -68.820  41.201  1.000 81.821  0 403 ARG III NE  1 ? 34 
ATOM   10771 C CZ  . ARG I  1 74  ? 13.958  -68.344  40.036  1.000 84.182  0 403 ARG III CZ  1 ? 34 
ATOM   10772 N NH1 . ARG I  1 74  ? 14.211  -67.052  39.891  1.000 83.008  0 403 ARG III NH1 1 ? 34 
ATOM   10773 N NH2 . ARG I  1 74  ? 14.084  -69.166  39.014  1.000 87.546  0 403 ARG III NH2 1 ? 34 
ATOM   10774 N N   . GLY I  1 75  ? 14.488  -72.897  44.573  1.000 66.862  0 404 GLY III N   1 ? 34 
ATOM   10775 C CA  . GLY I  1 75  ? 15.134  -74.173  44.219  1.000 66.031  0 404 GLY III CA  1 ? 34 
ATOM   10776 C C   . GLY I  1 75  ? 16.299  -73.977  43.278  1.000 63.901  0 404 GLY III C   1 ? 34 
ATOM   10777 O O   . GLY I  1 75  ? 17.386  -74.480  43.585  1.000 62.033  0 404 GLY III O   1 ? 34 
ATOM   10778 N N   . ASP I  1 76  ? 16.113  -73.262  42.171  1.000 68.837  0 405 ASP III N   1 ? 34 
ATOM   10779 C CA  . ASP I  1 76  ? 17.171  -73.230  41.123  1.000 71.036  0 405 ASP III CA  1 ? 34 
ATOM   10780 C C   . ASP I  1 76  ? 18.228  -72.177  41.479  1.000 66.673  0 405 ASP III C   1 ? 34 
ATOM   10781 O O   . ASP I  1 76  ? 19.187  -72.066  40.732  1.000 65.398  0 405 ASP III O   1 ? 34 
ATOM   10782 C CB  . ASP I  1 76  ? 16.606  -73.183  39.697  1.000 75.345  0 405 ASP III CB  1 ? 34 
ATOM   10783 C CG  . ASP I  1 76  ? 15.585  -72.098  39.429  1.000 81.095  0 405 ASP III CG  1 ? 34 
ATOM   10784 O OD1 . ASP I  1 76  ? 15.632  -71.068  40.148  1.000 81.582  0 405 ASP III OD1 1 ? 34 
ATOM   10785 O OD2 . ASP I  1 76  ? 14.754  -72.295  38.495  1.000 84.269  0 405 ASP III OD2 1 ? 34 
ATOM   10786 N N   . GLU I  1 77  ? 18.136  -71.517  42.633  1.000 64.481  0 406 GLU III N   1 ? 34 
ATOM   10787 C CA  . GLU I  1 77  ? 19.210  -70.618  43.131  1.000 60.316  0 406 GLU III CA  1 ? 34 
ATOM   10788 C C   . GLU I  1 77  ? 20.128  -71.377  44.104  1.000 57.487  0 406 GLU III C   1 ? 34 
ATOM   10789 O O   . GLU I  1 77  ? 21.206  -70.855  44.415  1.000 56.422  0 406 GLU III O   1 ? 34 
ATOM   10790 C CB  . GLU I  1 77  ? 18.602  -69.378  43.785  1.000 59.655  0 406 GLU III CB  1 ? 34 
ATOM   10791 C CG  . GLU I  1 77  ? 17.936  -68.401  42.804  1.000 59.613  0 406 GLU III CG  1 ? 34 
ATOM   10792 C CD  . GLU I  1 77  ? 17.139  -67.281  43.476  1.000 59.265  0 406 GLU III CD  1 ? 34 
ATOM   10793 O OE1 . GLU I  1 77  ? 16.779  -67.437  44.667  1.000 57.084  0 406 GLU III OE1 1 ? 34 
ATOM   10794 O OE2 . GLU I  1 77  ? 16.863  -66.259  42.815  1.000 60.310  0 406 GLU III OE2 1 ? 34 
ATOM   10795 N N   . VAL I  1 78  ? 19.766  -72.582  44.552  1.000 56.742  0 407 VAL III N   1 ? 34 
ATOM   10796 C CA  . VAL I  1 78  ? 20.601  -73.342  45.532  1.000 55.001  0 407 VAL III CA  1 ? 34 
ATOM   10797 C C   . VAL I  1 78  ? 22.007  -73.591  44.948  1.000 52.696  0 407 VAL III C   1 ? 34 
ATOM   10798 O O   . VAL I  1 78  ? 22.959  -73.485  45.703  1.000 49.745  0 407 VAL III O   1 ? 34 
ATOM   10799 C CB  . VAL I  1 78  ? 19.911  -74.643  45.983  1.000 56.991  0 407 VAL III CB  1 ? 34 
ATOM   10800 C CG1 . VAL I  1 78  ? 20.849  -75.564  46.768  1.000 54.786  0 407 VAL III CG1 1 ? 34 
ATOM   10801 C CG2 . VAL I  1 78  ? 18.657  -74.320  46.797  1.000 58.182  0 407 VAL III CG2 1 ? 34 
ATOM   10802 N N   . ARG I  1 79  ? 22.150  -73.851  43.647  1.000 54.311  0 408 ARG III N   1 ? 34 
ATOM   10803 C CA  . ARG I  1 79  ? 23.477  -74.068  43.008  1.000 53.940  0 408 ARG III CA  1 ? 34 
ATOM   10804 C C   . ARG I  1 79  ? 24.389  -72.832  43.188  1.000 50.786  0 408 ARG III C   1 ? 34 
ATOM   10805 O O   . ARG I  1 79  ? 25.602  -72.985  43.027  1.000 49.536  0 408 ARG III O   1 ? 34 
ATOM   10806 C CB  . ARG I  1 79  ? 23.294  -74.431  41.538  1.000 58.162  0 408 ARG III CB  1 ? 34 
ATOM   10807 C CG  . ARG I  1 79  ? 22.815  -73.269  40.680  1.000 64.358  0 408 ARG III CG  1 ? 34 
ATOM   10808 C CD  . ARG I  1 79  ? 22.622  -73.727  39.227  1.000 72.427  0 408 ARG III CD  1 ? 34 
ATOM   10809 N NE  . ARG I  1 79  ? 21.199  -73.903  38.883  1.000 80.708  0 408 ARG III NE  1 ? 34 
ATOM   10810 C CZ  . ARG I  1 79  ? 20.530  -75.062  38.773  1.000 84.837  0 408 ARG III CZ  1 ? 34 
ATOM   10811 N NH1 . ARG I  1 79  ? 21.140  -76.226  38.953  1.000 90.334  0 408 ARG III NH1 1 ? 34 
ATOM   10812 N NH2 . ARG I  1 79  ? 19.236  -75.034  38.494  1.000 83.643  0 408 ARG III NH2 1 ? 34 
ATOM   10813 N N   . GLN I  1 80  ? 23.848  -71.654  43.488  1.000 47.660  0 409 GLN III N   1 ? 34 
ATOM   10814 C CA  . GLN I  1 80  ? 24.642  -70.412  43.687  1.000 46.967  0 409 GLN III CA  1 ? 34 
ATOM   10815 C C   . GLN I  1 80  ? 25.294  -70.382  45.074  1.000 44.610  0 409 GLN III C   1 ? 34 
ATOM   10816 O O   . GLN I  1 80  ? 26.197  -69.577  45.288  1.000 41.977  0 409 GLN III O   1 ? 34 
ATOM   10817 C CB  . GLN I  1 80  ? 23.783  -69.160  43.497  1.000 48.858  0 409 GLN III CB  1 ? 34 
ATOM   10818 C CG  . GLN I  1 80  ? 23.431  -68.890  42.047  1.000 50.012  0 409 GLN III CG  1 ? 34 
ATOM   10819 C CD  . GLN I  1 80  ? 22.656  -67.606  41.873  1.000 52.696  0 409 GLN III CD  1 ? 34 
ATOM   10820 O OE1 . GLN I  1 80  ? 23.012  -66.530  42.364  1.000 51.744  0 409 GLN III OE1 1 ? 34 
ATOM   10821 N NE2 . GLN I  1 80  ? 21.556  -67.717  41.152  1.000 57.392  0 409 GLN III NE2 1 ? 34 
ATOM   10822 N N   . ILE I  1 81  ? 24.845  -71.210  46.002  1.000 47.100  0 410 ILE III N   1 ? 34 
ATOM   10823 C CA  . ILE I  1 81  ? 25.408  -71.245  47.380  1.000 46.358  0 410 ILE III CA  1 ? 34 
ATOM   10824 C C   . ILE I  1 81  ? 26.575  -72.224  47.349  1.000 46.534  0 410 ILE III C   1 ? 34 
ATOM   10825 O O   . ILE I  1 81  ? 26.488  -73.328  47.908  1.000 45.946  0 410 ILE III O   1 ? 34 
ATOM   10826 C CB  . ILE I  1 81  ? 24.353  -71.596  48.437  1.000 48.109  0 410 ILE III CB  1 ? 34 
ATOM   10827 C CG1 . ILE I  1 81  ? 23.077  -70.793  48.204  1.000 49.749  0 410 ILE III CG1 1 ? 34 
ATOM   10828 C CG2 . ILE I  1 81  ? 24.912  -71.366  49.829  1.000 49.077  0 410 ILE III CG2 1 ? 34 
ATOM   10829 C CD1 . ILE I  1 81  ? 23.292  -69.301  48.166  1.000 49.378  0 410 ILE III CD1 1 ? 34 
ATOM   10830 N N   . ALA I  1 82  ? 27.650  -71.790  46.709  1.000 47.465  0 411 ALA III N   1 ? 34 
ATOM   10831 C CA  . ALA I  1 82  ? 28.847  -72.602  46.439  1.000 47.267  0 411 ALA III CA  1 ? 34 
ATOM   10832 C C   . ALA I  1 82  ? 29.950  -71.652  45.995  1.000 48.629  0 411 ALA III C   1 ? 34 
ATOM   10833 O O   . ALA I  1 82  ? 29.696  -70.647  45.339  1.000 46.545  0 411 ALA III O   1 ? 34 
ATOM   10834 C CB  . ALA I  1 82  ? 28.553  -73.635  45.365  1.000 45.412  0 411 ALA III CB  1 ? 34 
ATOM   10835 N N   . PRO I  1 83  ? 31.224  -71.977  46.295  1.000 50.714  0 412 PRO III N   1 ? 34 
ATOM   10836 C CA  . PRO I  1 83  ? 32.340  -71.201  45.791  1.000 49.075  0 412 PRO III CA  1 ? 34 
ATOM   10837 C C   . PRO I  1 83  ? 32.312  -71.087  44.270  1.000 46.917  0 412 PRO III C   1 ? 34 
ATOM   10838 O O   . PRO I  1 83  ? 32.011  -72.060  43.636  1.000 46.399  0 412 PRO III O   1 ? 34 
ATOM   10839 C CB  . PRO I  1 83  ? 33.556  -71.999  46.273  1.000 51.014  0 412 PRO III CB  1 ? 34 
ATOM   10840 C CG  . PRO I  1 83  ? 33.035  -73.377  46.498  1.000 51.277  0 412 PRO III CG  1 ? 34 
ATOM   10841 C CD  . PRO I  1 83  ? 31.673  -73.119  47.100  1.000 51.701  0 412 PRO III CD  1 ? 34 
ATOM   10842 N N   . GLY I  1 84  ? 32.600  -69.884  43.763  1.000 46.295  0 413 GLY III N   1 ? 34 
ATOM   10843 C CA  . GLY I  1 84  ? 32.898  -69.626  42.347  1.000 47.304  0 413 GLY III CA  1 ? 34 
ATOM   10844 C C   . GLY I  1 84  ? 31.653  -69.394  41.529  1.000 48.159  0 413 GLY III C   1 ? 34 
ATOM   10845 O O   . GLY I  1 84  ? 31.775  -69.405  40.308  1.000 53.007  0 413 GLY III O   1 ? 34 
ATOM   10846 N N   . GLN I  1 85  ? 30.493  -69.204  42.166  1.000 47.618  0 414 GLN III N   1 ? 34 
ATOM   10847 C CA  . GLN I  1 85  ? 29.185  -69.012  41.485  1.000 48.911  0 414 GLN III CA  1 ? 34 
ATOM   10848 C C   . GLN I  1 85  ? 28.928  -67.533  41.219  1.000 48.532  0 414 GLN III C   1 ? 34 
ATOM   10849 O O   . GLN I  1 85  ? 29.432  -66.711  41.969  1.000 45.747  0 414 GLN III O   1 ? 34 
ATOM   10850 C CB  . GLN I  1 85  ? 28.076  -69.599  42.357  1.000 50.489  0 414 GLN III CB  1 ? 34 
ATOM   10851 C CG  . GLN I  1 85  ? 28.120  -71.132  42.375  1.000 50.952  0 414 GLN III CG  1 ? 34 
ATOM   10852 C CD  . GLN I  1 85  ? 27.766  -71.661  40.999  1.000 52.597  0 414 GLN III CD  1 ? 34 
ATOM   10853 O OE1 . GLN I  1 85  ? 26.876  -71.162  40.320  1.000 57.234  0 414 GLN III OE1 1 ? 34 
ATOM   10854 N NE2 . GLN I  1 85  ? 28.429  -72.712  40.559  1.000 55.986  0 414 GLN III NE2 1 ? 34 
ATOM   10855 N N   . THR I  1 86  ? 28.150  -67.231  40.179  1.000 50.138  0 415 THR III N   1 ? 34 
ATOM   10856 C CA  . THR I  1 86  ? 27.554  -65.896  39.939  1.000 53.206  0 415 THR III CA  1 ? 34 
ATOM   10857 C C   . THR I  1 86  ? 26.044  -66.039  39.754  1.000 54.354  0 415 THR III C   1 ? 34 
ATOM   10858 O O   . THR I  1 86  ? 25.571  -67.181  39.582  1.000 54.065  0 415 THR III O   1 ? 34 
ATOM   10859 C CB  . THR I  1 86  ? 28.190  -65.192  38.737  1.000 57.566  0 415 THR III CB  1 ? 34 
ATOM   10860 O OG1 . THR I  1 86  ? 28.070  -66.071  37.618  1.000 60.665  0 415 THR III OG1 1 ? 34 
ATOM   10861 C CG2 . THR I  1 86  ? 29.632  -64.816  38.989  1.000 59.018  0 415 THR III CG2 1 ? 34 
ATOM   10862 N N   . GLY I  1 87  ? 25.341  -64.897  39.784  1.000 55.587  0 416 GLY III N   1 ? 34 
ATOM   10863 C CA  . GLY I  1 87  ? 23.873  -64.783  39.777  1.000 56.398  0 416 GLY III CA  1 ? 34 
ATOM   10864 C C   . GLY I  1 87  ? 23.412  -63.792  40.827  1.000 56.478  0 416 GLY III C   1 ? 34 
ATOM   10865 O O   . GLY I  1 87  ? 24.259  -63.344  41.612  1.000 54.090  0 416 GLY III O   1 ? 34 
ATOM   10866 N N   . LYS I  1 88  ? 22.120  -63.455  40.834  1.000 57.986  0 417 LYS III N   1 ? 34 
ATOM   10867 C CA  . LYS I  1 88  ? 21.537  -62.457  41.760  1.000 57.704  0 417 LYS III CA  1 ? 34 
ATOM   10868 C C   . LYS I  1 88  ? 21.959  -62.831  43.176  1.000 54.805  0 417 LYS III C   1 ? 34 
ATOM   10869 O O   . LYS I  1 88  ? 22.346  -61.919  43.913  1.000 53.513  0 417 LYS III O   1 ? 34 
ATOM   10870 C CB  . LYS I  1 88  ? 20.004  -62.401  41.700  1.000 61.753  0 417 LYS III CB  1 ? 34 
ATOM   10871 C CG  . LYS I  1 88  ? 19.393  -61.964  40.386  1.000 67.180  0 417 LYS III CG  1 ? 34 
ATOM   10872 C CD  . LYS I  1 88  ? 19.964  -60.670  39.870  1.000 71.288  0 417 LYS III CD  1 ? 34 
ATOM   10873 C CE  . LYS I  1 88  ? 19.365  -60.251  38.552  1.000 75.560  0 417 LYS III CE  1 ? 34 
ATOM   10874 N NZ  . LYS I  1 88  ? 20.230  -59.258  37.875  1.000 78.283  0 417 LYS III NZ  1 ? 34 
ATOM   10875 N N   . ILE I  1 89  ? 21.902  -64.116  43.548  1.000 52.373  0 418 ILE III N   1 ? 34 
ATOM   10876 C CA  . ILE I  1 89  ? 22.092  -64.526  44.969  1.000 51.423  0 418 ILE III CA  1 ? 34 
ATOM   10877 C C   . ILE I  1 89  ? 23.581  -64.446  45.325  1.000 49.144  0 418 ILE III C   1 ? 34 
ATOM   10878 O O   . ILE I  1 89  ? 23.909  -63.723  46.284  1.000 49.735  0 418 ILE III O   1 ? 34 
ATOM   10879 C CB  . ILE I  1 89  ? 21.464  -65.899  45.264  1.000 52.311  0 418 ILE III CB  1 ? 34 
ATOM   10880 C CG1 . ILE I  1 89  ? 19.997  -65.928  44.855  1.000 54.778  0 418 ILE III CG1 1 ? 34 
ATOM   10881 C CG2 . ILE I  1 89  ? 21.607  -66.226  46.747  1.000 53.545  0 418 ILE III CG2 1 ? 34 
ATOM   10882 C CD1 . ILE I  1 89  ? 19.147  -64.810  45.464  1.000 56.400  0 418 ILE III CD1 1 ? 34 
ATOM   10883 N N   . ALA I  1 90  ? 24.450  -65.122  44.578  1.000 46.860  0 419 ALA III N   1 ? 34 
ATOM   10884 C CA  . ALA I  1 90  ? 25.913  -65.096  44.806  1.000 47.501  0 419 ALA III CA  1 ? 34 
ATOM   10885 C C   . ALA I  1 90  ? 26.426  -63.642  44.770  1.000 48.843  0 419 ALA III C   1 ? 34 
ATOM   10886 O O   . ALA I  1 90  ? 27.272  -63.300  45.591  1.000 47.232  0 419 ALA III O   1 ? 34 
ATOM   10887 C CB  . ALA I  1 90  ? 26.622  -65.970  43.780  1.000 48.873  0 419 ALA III CB  1 ? 34 
ATOM   10888 N N   . ASP I  1 91  ? 25.922  -62.815  43.859  1.000 50.218  0 420 ASP III N   1 ? 34 
ATOM   10889 C CA  . ASP I  1 91  ? 26.486  -61.465  43.597  1.000 54.096  0 420 ASP III CA  1 ? 34 
ATOM   10890 C C   . ASP I  1 91  ? 25.948  -60.439  44.599  1.000 55.212  0 420 ASP III C   1 ? 34 
ATOM   10891 O O   . ASP I  1 91  ? 26.742  -59.582  45.008  1.000 55.347  0 420 ASP III O   1 ? 34 
ATOM   10892 C CB  . ASP I  1 91  ? 26.192  -60.989  42.169  1.000 58.373  0 420 ASP III CB  1 ? 34 
ATOM   10893 C CG  . ASP I  1 91  ? 26.828  -61.813  41.063  1.000 58.498  0 420 ASP III CG  1 ? 34 
ATOM   10894 O OD1 . ASP I  1 91  ? 27.727  -62.605  41.380  1.000 61.174  0 420 ASP III OD1 1 ? 34 
ATOM   10895 O OD2 . ASP I  1 91  ? 26.418  -61.636  39.900  1.000 61.372  0 420 ASP III OD2 1 ? 34 
ATOM   10896 N N   . TYR I  1 92  ? 24.662  -60.496  44.965  1.000 54.005  0 421 TYR III N   1 ? 34 
ATOM   10897 C CA  . TYR I  1 92  ? 23.967  -59.364  45.630  1.000 54.842  0 421 TYR III CA  1 ? 34 
ATOM   10898 C C   . TYR I  1 92  ? 23.418  -59.743  47.019  1.000 52.305  0 421 TYR III C   1 ? 34 
ATOM   10899 O O   . TYR I  1 92  ? 22.980  -58.827  47.731  1.000 53.932  0 421 TYR III O   1 ? 34 
ATOM   10900 C CB  . TYR I  1 92  ? 22.830  -58.854  44.743  1.000 57.585  0 421 TYR III CB  1 ? 34 
ATOM   10901 C CG  . TYR I  1 92  ? 23.199  -58.272  43.397  1.000 59.588  0 421 TYR III CG  1 ? 34 
ATOM   10902 C CD1 . TYR I  1 92  ? 24.479  -57.843  43.093  1.000 59.647  0 421 TYR III CD1 1 ? 34 
ATOM   10903 C CD2 . TYR I  1 92  ? 22.222  -58.085  42.433  1.000 61.676  0 421 TYR III CD2 1 ? 34 
ATOM   10904 C CE1 . TYR I  1 92  ? 24.780  -57.269  41.868  1.000 61.134  0 421 TYR III CE1 1 ? 34 
ATOM   10905 C CE2 . TYR I  1 92  ? 22.502  -57.505  41.207  1.000 64.712  0 421 TYR III CE2 1 ? 34 
ATOM   10906 C CZ  . TYR I  1 92  ? 23.782  -57.085  40.920  1.000 64.312  0 421 TYR III CZ  1 ? 34 
ATOM   10907 O OH  . TYR I  1 92  ? 24.008  -56.519  39.697  1.000 63.074  0 421 TYR III OH  1 ? 34 
ATOM   10908 N N   . ASN I  1 93  ? 23.441  -61.014  47.426  1.000 49.422  0 422 ASN III N   1 ? 34 
ATOM   10909 C CA  . ASN I  1 93  ? 22.718  -61.456  48.651  1.000 48.302  0 422 ASN III CA  1 ? 34 
ATOM   10910 C C   . ASN I  1 93  ? 23.644  -62.217  49.608  1.000 47.679  0 422 ASN III C   1 ? 34 
ATOM   10911 O O   . ASN I  1 93  ? 23.767  -61.800  50.785  1.000 47.164  0 422 ASN III O   1 ? 34 
ATOM   10912 C CB  . ASN I  1 93  ? 21.495  -62.303  48.287  1.000 47.704  0 422 ASN III CB  1 ? 34 
ATOM   10913 C CG  . ASN I  1 93  ? 20.424  -61.477  47.625  1.000 47.920  0 422 ASN III CG  1 ? 34 
ATOM   10914 O OD1 . ASN I  1 93  ? 19.533  -60.991  48.306  1.000 48.924  0 422 ASN III OD1 1 ? 34 
ATOM   10915 N ND2 . ASN I  1 93  ? 20.521  -61.289  46.322  1.000 48.234  0 422 ASN III ND2 1 ? 34 
ATOM   10916 N N   . TYR I  1 94  ? 24.222  -63.320  49.147  1.000 45.746  0 423 TYR III N   1 ? 34 
ATOM   10917 C CA  . TYR I  1 94  ? 25.082  -64.200  49.977  1.000 45.650  0 423 TYR III CA  1 ? 34 
ATOM   10918 C C   . TYR I  1 94  ? 26.195  -64.781  49.106  1.000 44.904  0 423 TYR III C   1 ? 34 
ATOM   10919 O O   . TYR I  1 94  ? 25.913  -65.547  48.174  1.000 44.361  0 423 TYR III O   1 ? 34 
ATOM   10920 C CB  . TYR I  1 94  ? 24.259  -65.304  50.634  1.000 45.000  0 423 TYR III CB  1 ? 34 
ATOM   10921 C CG  . TYR I  1 94  ? 25.041  -66.134  51.618  1.000 43.770  0 423 TYR III CG  1 ? 34 
ATOM   10922 C CD1 . TYR I  1 94  ? 25.167  -65.736  52.944  1.000 46.354  0 423 TYR III CD1 1 ? 34 
ATOM   10923 C CD2 . TYR I  1 94  ? 25.680  -67.291  51.235  1.000 42.276  0 423 TYR III CD2 1 ? 34 
ATOM   10924 C CE1 . TYR I  1 94  ? 25.893  -66.479  53.865  1.000 45.482  0 423 TYR III CE1 1 ? 34 
ATOM   10925 C CE2 . TYR I  1 94  ? 26.385  -68.058  52.142  1.000 42.208  0 423 TYR III CE2 1 ? 34 
ATOM   10926 C CZ  . TYR I  1 94  ? 26.512  -67.646  53.459  1.000 44.484  0 423 TYR III CZ  1 ? 34 
ATOM   10927 O OH  . TYR I  1 94  ? 27.246  -68.403  54.338  1.000 41.685  0 423 TYR III OH  1 ? 34 
ATOM   10928 N N   . LYS I  1 95  ? 27.429  -64.408  49.418  1.000 45.424  0 424 LYS III N   1 ? 34 
ATOM   10929 C CA  . LYS I  1 95  ? 28.633  -64.741  48.608  1.000 45.177  0 424 LYS III CA  1 ? 34 
ATOM   10930 C C   . LYS I  1 95  ? 29.552  -65.632  49.434  1.000 43.422  0 424 LYS III C   1 ? 34 
ATOM   10931 O O   . LYS I  1 95  ? 29.997  -65.192  50.501  1.000 42.102  0 424 LYS III O   1 ? 34 
ATOM   10932 C CB  . LYS I  1 95  ? 29.382  -63.478  48.182  1.000 47.580  0 424 LYS III CB  1 ? 34 
ATOM   10933 C CG  . LYS I  1 95  ? 30.628  -63.719  47.343  1.000 49.326  0 424 LYS III CG  1 ? 34 
ATOM   10934 C CD  . LYS I  1 95  ? 30.378  -64.595  46.138  1.000 50.049  0 424 LYS III CD  1 ? 34 
ATOM   10935 C CE  . LYS I  1 95  ? 31.411  -64.400  45.060  1.000 50.886  0 424 LYS III CE  1 ? 34 
ATOM   10936 N NZ  . LYS I  1 95  ? 31.180  -65.374  43.989  1.000 51.332  0 424 LYS III NZ  1 ? 34 
ATOM   10937 N N   . LEU I  1 96  ? 29.819  -66.844  48.951  1.000 42.062  0 425 LEU III N   1 ? 34 
ATOM   10938 C CA  . LEU I  1 96  ? 30.848  -67.716  49.556  1.000 41.887  0 425 LEU III CA  1 ? 34 
ATOM   10939 C C   . LEU I  1 96  ? 32.178  -67.406  48.885  1.000 41.472  0 425 LEU III C   1 ? 34 
ATOM   10940 O O   . LEU I  1 96  ? 32.214  -67.133  47.682  1.000 42.962  0 425 LEU III O   1 ? 34 
ATOM   10941 C CB  . LEU I  1 96  ? 30.487  -69.184  49.372  1.000 41.680  0 425 LEU III CB  1 ? 34 
ATOM   10942 C CG  . LEU I  1 96  ? 29.375  -69.703  50.260  1.000 41.942  0 425 LEU III CG  1 ? 34 
ATOM   10943 C CD1 . LEU I  1 96  ? 29.142  -71.178  50.001  1.000 43.682  0 425 LEU III CD1 1 ? 34 
ATOM   10944 C CD2 . LEU I  1 96  ? 29.679  -69.473  51.726  1.000 42.247  0 425 LEU III CD2 1 ? 34 
ATOM   10945 N N   . PRO I  1 97  ? 33.286  -67.446  49.664  1.000 39.641  0 426 PRO III N   1 ? 34 
ATOM   10946 C CA  . PRO I  1 97  ? 34.619  -67.240  49.122  1.000 40.786  0 426 PRO III CA  1 ? 34 
ATOM   10947 C C   . PRO I  1 97  ? 35.022  -68.405  48.202  1.000 42.014  0 426 PRO III C   1 ? 34 
ATOM   10948 O O   . PRO I  1 97  ? 34.459  -69.496  48.332  1.000 39.255  0 426 PRO III O   1 ? 34 
ATOM   10949 C CB  . PRO I  1 97  ? 35.499  -67.226  50.379  1.000 41.032  0 426 PRO III CB  1 ? 34 
ATOM   10950 C CG  . PRO I  1 97  ? 34.750  -68.051  51.389  1.000 38.216  0 426 PRO III CG  1 ? 34 
ATOM   10951 C CD  . PRO I  1 97  ? 33.302  -67.743  51.109  1.000 39.838  0 426 PRO III CD  1 ? 34 
ATOM   10952 N N   . ASP I  1 98  ? 35.985  -68.173  47.313  1.000 44.732  0 427 ASP III N   1 ? 34 
ATOM   10953 C CA  . ASP I  1 98  ? 36.421  -69.227  46.363  1.000 47.926  0 427 ASP III CA  1 ? 34 
ATOM   10954 C C   . ASP I  1 98  ? 37.120  -70.368  47.124  1.000 45.089  0 427 ASP III C   1 ? 34 
ATOM   10955 O O   . ASP I  1 98  ? 37.040  -71.489  46.643  1.000 45.385  0 427 ASP III O   1 ? 34 
ATOM   10956 C CB  . ASP I  1 98  ? 37.284  -68.685  45.221  1.000 52.449  0 427 ASP III CB  1 ? 34 
ATOM   10957 C CG  . ASP I  1 98  ? 37.114  -69.549  43.974  1.000 57.920  0 427 ASP III CG  1 ? 34 
ATOM   10958 O OD1 . ASP I  1 98  ? 36.020  -69.488  43.412  1.000 61.611  0 427 ASP III OD1 1 ? 34 
ATOM   10959 O OD2 . ASP I  1 98  ? 38.050  -70.317  43.580  1.000 63.435  0 427 ASP III OD2 1 ? 34 
ATOM   10960 N N   . ASP I  1 99  ? 37.752  -70.102  48.268  1.000 43.177  0 428 ASP III N   1 ? 34 
ATOM   10961 C CA  . ASP I  1 99  ? 38.503  -71.094  49.081  1.000 43.008  0 428 ASP III CA  1 ? 34 
ATOM   10962 C C   . ASP I  1 99  ? 37.652  -71.510  50.294  1.000 42.567  0 428 ASP III C   1 ? 34 
ATOM   10963 O O   . ASP I  1 99  ? 38.226  -71.906  51.325  1.000 45.355  0 428 ASP III O   1 ? 34 
ATOM   10964 C CB  . ASP I  1 99  ? 39.873  -70.519  49.482  1.000 42.781  0 428 ASP III CB  1 ? 34 
ATOM   10965 C CG  . ASP I  1 99  ? 39.818  -69.392  50.498  1.000 42.700  0 428 ASP III CG  1 ? 34 
ATOM   10966 O OD1 . ASP I  1 99  ? 38.729  -68.858  50.717  1.000 43.315  0 428 ASP III OD1 1 ? 34 
ATOM   10967 O OD2 . ASP I  1 99  ? 40.856  -69.100  51.120  1.000 46.341  0 428 ASP III OD2 1 ? 34 
ATOM   10968 N N   . PHE I  1 100 ? 36.337  -71.421  50.196  1.000 40.670  0 429 PHE III N   1 ? 34 
ATOM   10969 C CA  . PHE I  1 100 ? 35.412  -71.786  51.300  1.000 41.036  0 429 PHE III CA  1 ? 34 
ATOM   10970 C C   . PHE I  1 100 ? 35.794  -73.125  51.920  1.000 41.432  0 429 PHE III C   1 ? 34 
ATOM   10971 O O   . PHE I  1 100 ? 36.011  -74.095  51.207  1.000 43.847  0 429 PHE III O   1 ? 34 
ATOM   10972 C CB  . PHE I  1 100 ? 33.978  -71.855  50.782  1.000 42.339  0 429 PHE III CB  1 ? 34 
ATOM   10973 C CG  . PHE I  1 100 ? 32.951  -72.277  51.790  1.000 42.131  0 429 PHE III CG  1 ? 34 
ATOM   10974 C CD1 . PHE I  1 100 ? 32.783  -71.582  52.966  1.000 42.705  0 429 PHE III CD1 1 ? 34 
ATOM   10975 C CD2 . PHE I  1 100 ? 32.127  -73.358  51.537  1.000 45.412  0 429 PHE III CD2 1 ? 34 
ATOM   10976 C CE1 . PHE I  1 100 ? 31.803  -71.960  53.877  1.000 44.028  0 429 PHE III CE1 1 ? 34 
ATOM   10977 C CE2 . PHE I  1 100 ? 31.157  -73.747  52.442  1.000 45.163  0 429 PHE III CE2 1 ? 34 
ATOM   10978 C CZ  . PHE I  1 100 ? 31.000  -73.047  53.614  1.000 45.165  0 429 PHE III CZ  1 ? 34 
ATOM   10979 N N   . THR I  1 101 ? 35.836  -73.172  53.248  1.000 42.407  0 430 THR III N   1 ? 34 
ATOM   10980 C CA  . THR I  1 101 ? 35.919  -74.423  54.040  1.000 40.728  0 430 THR III CA  1 ? 34 
ATOM   10981 C C   . THR I  1 101 ? 34.625  -74.577  54.833  1.000 39.470  0 430 THR III C   1 ? 34 
ATOM   10982 O O   . THR I  1 101 ? 34.383  -73.748  55.721  1.000 40.905  0 430 THR III O   1 ? 34 
ATOM   10983 C CB  . THR I  1 101 ? 37.143  -74.399  54.960  1.000 41.001  0 430 THR III CB  1 ? 34 
ATOM   10984 O OG1 . THR I  1 101 ? 38.286  -74.163  54.140  1.000 40.907  0 430 THR III OG1 1 ? 34 
ATOM   10985 C CG2 . THR I  1 101 ? 37.330  -75.689  55.727  1.000 42.124  0 430 THR III CG2 1 ? 34 
ATOM   10986 N N   . GLY I  1 102 ? 33.839  -75.603  54.538  1.000 39.694  0 431 GLY III N   1 ? 34 
ATOM   10987 C CA  . GLY I  1 102 ? 32.542  -75.828  55.207  1.000 43.930  0 431 GLY III CA  1 ? 34 
ATOM   10988 C C   . GLY I  1 102 ? 31.585  -76.658  54.383  1.000 43.393  0 431 GLY III C   1 ? 34 
ATOM   10989 O O   . GLY I  1 102 ? 32.036  -77.312  53.459  1.000 44.705  0 431 GLY III O   1 ? 34 
ATOM   10990 N N   . CYS I  1 103 ? 30.318  -76.683  54.759  1.000 47.422  0 432 CYS III N   1 ? 34 
ATOM   10991 C CA  . CYS I  1 103 ? 29.280  -77.528  54.108  1.000 49.333  0 432 CYS III CA  1 ? 34 
ATOM   10992 C C   . CYS I  1 103 ? 28.039  -76.693  53.831  1.000 47.216  0 432 CYS III C   1 ? 34 
ATOM   10993 O O   . CYS I  1 103 ? 27.762  -75.751  54.586  1.000 49.083  0 432 CYS III O   1 ? 34 
ATOM   10994 C CB  . CYS I  1 103 ? 28.910  -78.749  54.948  1.000 53.341  0 432 CYS III CB  1 ? 34 
ATOM   10995 S SG  . CYS I  1 103 ? 30.354  -79.715  55.472  1.000 58.684  0 432 CYS III SG  1 ? 34 
ATOM   10996 N N   . VAL I  1 104 ? 27.347  -77.044  52.756  1.000 47.210  0 433 VAL III N   1 ? 34 
ATOM   10997 C CA  . VAL I  1 104 ? 26.098  -76.388  52.308  1.000 47.115  0 433 VAL III CA  1 ? 34 
ATOM   10998 C C   . VAL I  1 104 ? 25.031  -77.465  52.241  1.000 48.312  0 433 VAL III C   1 ? 34 
ATOM   10999 O O   . VAL I  1 104 ? 25.242  -78.479  51.543  1.000 47.725  0 433 VAL III O   1 ? 34 
ATOM   11000 C CB  . VAL I  1 104 ? 26.288  -75.670  50.964  1.000 48.454  0 433 VAL III CB  1 ? 34 
ATOM   11001 C CG1 . VAL I  1 104 ? 24.980  -75.097  50.442  1.000 49.292  0 433 VAL III CG1 1 ? 34 
ATOM   11002 C CG2 . VAL I  1 104 ? 27.345  -74.568  51.093  1.000 47.508  0 433 VAL III CG2 1 ? 34 
ATOM   11003 N N   . ILE I  1 105 ? 23.949  -77.255  52.990  1.000 49.420  0 434 ILE III N   1 ? 34 
ATOM   11004 C CA  . ILE I  1 105 ? 22.791  -78.182  53.051  1.000 49.983  0 434 ILE III CA  1 ? 34 
ATOM   11005 C C   . ILE I  1 105 ? 21.561  -77.362  52.693  1.000 50.713  0 434 ILE III C   1 ? 34 
ATOM   11006 O O   . ILE I  1 105 ? 21.430  -76.217  53.182  1.000 49.742  0 434 ILE III O   1 ? 34 
ATOM   11007 C CB  . ILE I  1 105 ? 22.685  -78.853  54.439  1.000 50.750  0 434 ILE III CB  1 ? 34 
ATOM   11008 C CG1 . ILE I  1 105 ? 23.951  -79.655  54.741  1.000 51.135  0 434 ILE III CG1 1 ? 34 
ATOM   11009 C CG2 . ILE I  1 105 ? 21.458  -79.744  54.510  1.000 52.347  0 434 ILE III CG2 1 ? 34 
ATOM   11010 C CD1 . ILE I  1 105 ? 24.125  -80.062  56.165  1.000 53.193  0 434 ILE III CD1 1 ? 34 
ATOM   11011 N N   . ALA I  1 106 ? 20.692  -77.925  51.866  1.000 51.724  0 435 ALA III N   1 ? 34 
ATOM   11012 C CA  . ALA I  1 106 ? 19.392  -77.307  51.532  1.000 53.177  0 435 ALA III CA  1 ? 34 
ATOM   11013 C C   . ALA I  1 106 ? 18.330  -78.398  51.503  1.000 54.396  0 435 ALA III C   1 ? 34 
ATOM   11014 O O   . ALA I  1 106 ? 18.688  -79.614  51.374  1.000 52.993  0 435 ALA III O   1 ? 34 
ATOM   11015 C CB  . ALA I  1 106 ? 19.481  -76.553  50.224  1.000 53.264  0 435 ALA III CB  1 ? 34 
ATOM   11016 N N   . TRP I  1 107 ? 17.078  -77.970  51.650  1.000 56.478  0 436 TRP III N   1 ? 34 
ATOM   11017 C CA  . TRP I  1 107 ? 15.893  -78.843  51.507  1.000 58.768  0 436 TRP III CA  1 ? 34 
ATOM   11018 C C   . TRP I  1 107 ? 14.711  -78.003  51.043  1.000 60.089  0 436 TRP III C   1 ? 34 
ATOM   11019 O O   . TRP I  1 107 ? 14.649  -76.806  51.372  1.000 58.719  0 436 TRP III O   1 ? 34 
ATOM   11020 C CB  . TRP I  1 107 ? 15.610  -79.603  52.810  1.000 60.008  0 436 TRP III CB  1 ? 34 
ATOM   11021 C CG  . TRP I  1 107 ? 15.227  -78.750  53.971  1.000 60.531  0 436 TRP III CG  1 ? 34 
ATOM   11022 C CD1 . TRP I  1 107 ? 13.959  -78.486  54.389  1.000 63.725  0 436 TRP III CD1 1 ? 34 
ATOM   11023 C CD2 . TRP I  1 107 ? 16.099  -78.050  54.877  1.000 58.543  0 436 TRP III CD2 1 ? 34 
ATOM   11024 N NE1 . TRP I  1 107 ? 13.980  -77.687  55.505  1.000 62.530  0 436 TRP III NE1 1 ? 34 
ATOM   11025 C CE2 . TRP I  1 107 ? 15.275  -77.396  55.825  1.000 59.206  0 436 TRP III CE2 1 ? 34 
ATOM   11026 C CE3 . TRP I  1 107 ? 17.482  -77.904  54.982  1.000 55.580  0 436 TRP III CE3 1 ? 34 
ATOM   11027 C CZ2 . TRP I  1 107 ? 15.780  -76.620  56.866  1.000 57.263  0 436 TRP III CZ2 1 ? 34 
ATOM   11028 C CZ3 . TRP I  1 107 ? 17.984  -77.131  56.005  1.000 55.840  0 436 TRP III CZ3 1 ? 34 
ATOM   11029 C CH2 . TRP I  1 107 ? 17.144  -76.504  56.939  1.000 56.847  0 436 TRP III CH2 1 ? 34 
ATOM   11030 N N   . ASN I  1 108 ? 13.849  -78.627  50.250  1.000 62.773  0 437 ASN III N   1 ? 34 
ATOM   11031 C CA  . ASN I  1 108 ? 12.562  -78.058  49.802  1.000 64.488  0 437 ASN III CA  1 ? 34 
ATOM   11032 C C   . ASN I  1 108 ? 11.724  -77.727  51.045  1.000 65.283  0 437 ASN III C   1 ? 34 
ATOM   11033 O O   . ASN I  1 108 ? 11.560  -78.618  51.886  1.000 64.063  0 437 ASN III O   1 ? 34 
ATOM   11034 C CB  . ASN I  1 108 ? 11.867  -79.043  48.874  1.000 66.925  0 437 ASN III CB  1 ? 34 
ATOM   11035 C CG  . ASN I  1 108 ? 10.638  -78.418  48.278  1.000 69.502  0 437 ASN III CG  1 ? 34 
ATOM   11036 O OD1 . ASN I  1 108 ? 9.688   -78.146  48.993  1.000 72.431  0 437 ASN III OD1 1 ? 34 
ATOM   11037 N ND2 . ASN I  1 108 ? 10.681  -78.128  46.993  1.000 71.726  0 437 ASN III ND2 1 ? 34 
ATOM   11038 N N   . SER I  1 109 ? 11.239  -76.492  51.163  1.000 66.051  0 438 SER III N   1 ? 34 
ATOM   11039 C CA  . SER I  1 109 ? 10.404  -76.031  52.297  1.000 69.501  0 438 SER III CA  1 ? 34 
ATOM   11040 C C   . SER I  1 109 ? 9.055   -75.542  51.770  1.000 72.828  0 438 SER III C   1 ? 34 
ATOM   11041 O O   . SER I  1 109 ? 8.421   -74.707  52.452  1.000 74.600  0 438 SER III O   1 ? 34 
ATOM   11042 C CB  . SER I  1 109 ? 11.106  -74.967  53.092  1.000 67.127  0 438 SER III CB  1 ? 34 
ATOM   11043 O OG  . SER I  1 109 ? 11.386  -73.847  52.275  1.000 66.805  0 438 SER III OG  1 ? 34 
ATOM   11044 N N   . ASN I  1 110 ? 8.612   -76.077  50.627  1.000 73.691  0 439 ASN III N   1 ? 34 
ATOM   11045 C CA  . ASN I  1 110 ? 7.323   -75.680  50.009  1.000 76.390  0 439 ASN III CA  1 ? 34 
ATOM   11046 C C   . ASN I  1 110 ? 6.219   -75.810  51.063  1.000 77.918  0 439 ASN III C   1 ? 34 
ATOM   11047 O O   . ASN I  1 110 ? 5.403   -74.908  51.173  1.000 76.617  0 439 ASN III O   1 ? 34 
ATOM   11048 C CB  . ASN I  1 110 ? 7.024   -76.483  48.742  1.000 77.745  0 439 ASN III CB  1 ? 34 
ATOM   11049 C CG  . ASN I  1 110 ? 5.994   -75.813  47.844  1.000 80.065  0 439 ASN III CG  1 ? 34 
ATOM   11050 O OD1 . ASN I  1 110 ? 5.898   -74.588  47.770  1.000 78.843  0 439 ASN III OD1 1 ? 34 
ATOM   11051 N ND2 . ASN I  1 110 ? 5.235   -76.608  47.119  1.000 82.549  0 439 ASN III ND2 1 ? 34 
ATOM   11052 N N   . ASN I  1 111 ? 6.239   -76.885  51.849  1.000 79.821  0 440 ASN III N   1 ? 34 
ATOM   11053 C CA  . ASN I  1 111 ? 5.153   -77.216  52.803  1.000 85.700  0 440 ASN III CA  1 ? 34 
ATOM   11054 C C   . ASN I  1 111 ? 5.099   -76.193  53.940  1.000 83.820  0 440 ASN III C   1 ? 34 
ATOM   11055 O O   . ASN I  1 111 ? 4.017   -76.030  54.496  1.000 86.803  0 440 ASN III O   1 ? 34 
ATOM   11056 C CB  . ASN I  1 111 ? 5.257   -78.669  53.259  1.000 89.087  0 440 ASN III CB  1 ? 34 
ATOM   11057 C CG  . ASN I  1 111 ? 4.949   -79.654  52.136  1.000 92.755  0 440 ASN III CG  1 ? 34 
ATOM   11058 O OD1 . ASN I  1 111 ? 5.018   -79.337  50.938  1.000 92.549  0 440 ASN III OD1 1 ? 34 
ATOM   11059 N ND2 . ASN I  1 111 ? 4.610   -80.876  52.507  1.000 98.161  0 440 ASN III ND2 1 ? 34 
ATOM   11060 N N   . LEU I  1 112 ? 6.185   -75.514  54.268  1.000 81.679  0 441 LEU III N   1 ? 34 
ATOM   11061 C CA  . LEU I  1 112 ? 6.213   -74.515  55.376  1.000 82.520  0 441 LEU III CA  1 ? 34 
ATOM   11062 C C   . LEU I  1 112 ? 6.152   -73.085  54.834  1.000 81.410  0 441 LEU III C   1 ? 34 
ATOM   11063 O O   . LEU I  1 112 ? 5.525   -72.264  55.496  1.000 82.603  0 441 LEU III O   1 ? 34 
ATOM   11064 C CB  . LEU I  1 112 ? 7.484   -74.697  56.215  1.000 80.601  0 441 LEU III CB  1 ? 34 
ATOM   11065 C CG  . LEU I  1 112 ? 7.534   -75.966  57.062  1.000 82.572  0 441 LEU III CG  1 ? 34 
ATOM   11066 C CD1 . LEU I  1 112 ? 8.804   -75.983  57.910  1.000 81.037  0 441 LEU III CD1 1 ? 34 
ATOM   11067 C CD2 . LEU I  1 112 ? 6.292   -76.114  57.941  1.000 86.613  0 441 LEU III CD2 1 ? 34 
ATOM   11068 N N   . ASP I  1 113 ? 6.800   -72.799  53.703  1.000 79.428  0 442 ASP III N   1 ? 34 
ATOM   11069 C CA  . ASP I  1 113 ? 7.161   -71.417  53.290  1.000 78.177  0 442 ASP III CA  1 ? 34 
ATOM   11070 C C   . ASP I  1 113 ? 6.336   -70.923  52.092  1.000 80.359  0 442 ASP III C   1 ? 34 
ATOM   11071 O O   . ASP I  1 113 ? 6.609   -69.829  51.614  1.000 76.693  0 442 ASP III O   1 ? 34 
ATOM   11072 C CB  . ASP I  1 113 ? 8.649   -71.344  52.963  1.000 75.479  0 442 ASP III CB  1 ? 34 
ATOM   11073 C CG  . ASP I  1 113 ? 9.549   -71.411  54.195  1.000 75.170  0 442 ASP III CG  1 ? 34 
ATOM   11074 O OD1 . ASP I  1 113 ? 9.148   -70.852  55.261  1.000 73.363  0 442 ASP III OD1 1 ? 34 
ATOM   11075 O OD2 . ASP I  1 113 ? 10.660  -72.001  54.075  1.000 76.841  0 442 ASP III OD2 1 ? 34 
ATOM   11076 N N   . SER I  1 114 ? 5.362   -71.671  51.599  1.000 87.259  0 443 SER III N   1 ? 34 
ATOM   11077 C CA  . SER I  1 114 ? 4.484   -71.202  50.501  1.000 91.564  0 443 SER III CA  1 ? 34 
ATOM   11078 C C   . SER I  1 114 ? 3.042   -71.133  51.019  1.000 95.318  0 443 SER III C   1 ? 34 
ATOM   11079 O O   . SER I  1 114 ? 2.730   -71.866  51.948  1.000 97.317  0 443 SER III O   1 ? 34 
ATOM   11080 C CB  . SER I  1 114 ? 4.665   -72.078  49.286  1.000 93.375  0 443 SER III CB  1 ? 34 
ATOM   11081 O OG  . SER I  1 114 ? 3.829   -73.222  49.345  1.000 97.669  0 443 SER III OG  1 ? 34 
ATOM   11082 N N   . LYS I  1 115 ? 2.223   -70.219  50.506  1.000 96.482  0 444 LYS III N   1 ? 34 
ATOM   11083 C CA  . LYS I  1 115 ? 0.829   -70.007  50.960  1.000 100.161 0 444 LYS III CA  1 ? 34 
ATOM   11084 C C   . LYS I  1 115 ? -0.082  -69.922  49.742  1.000 102.372 0 444 LYS III C   1 ? 34 
ATOM   11085 O O   . LYS I  1 115 ? 0.400   -69.516  48.671  1.000 99.668  0 444 LYS III O   1 ? 34 
ATOM   11086 C CB  . LYS I  1 115 ? 0.687   -68.707  51.751  1.000 101.664 0 444 LYS III CB  1 ? 34 
ATOM   11087 C CG  . LYS I  1 115 ? -0.579  -68.608  52.588  1.000 107.631 0 444 LYS III CG  1 ? 34 
ATOM   11088 C CD  . LYS I  1 115 ? -0.905  -67.202  52.992  1.000 107.938 0 444 LYS III CD  1 ? 34 
ATOM   11089 C CE  . LYS I  1 115 ? 0.305   -66.471  53.533  1.000 103.155 0 444 LYS III CE  1 ? 34 
ATOM   11090 N NZ  . LYS I  1 115 ? -0.077  -65.128  54.018  1.000 103.892 0 444 LYS III NZ  1 ? 34 
ATOM   11091 N N   . VAL I  1 116 ? -1.361  -70.265  49.925  1.000 107.711 0 445 VAL III N   1 ? 34 
ATOM   11092 C CA  . VAL I  1 116 ? -2.435  -69.979  48.933  1.000 110.600 0 445 VAL III CA  1 ? 34 
ATOM   11093 C C   . VAL I  1 116 ? -2.461  -68.451  48.758  1.000 109.425 0 445 VAL III C   1 ? 34 
ATOM   11094 O O   . VAL I  1 116 ? -2.442  -67.715  49.777  1.000 109.378 0 445 VAL III O   1 ? 34 
ATOM   11095 C CB  . VAL I  1 116 ? -3.794  -70.582  49.348  1.000 115.889 0 445 VAL III CB  1 ? 34 
ATOM   11096 C CG1 . VAL I  1 116 ? -3.743  -72.098  49.298  1.000 117.263 0 445 VAL III CG1 1 ? 34 
ATOM   11097 C CG2 . VAL I  1 116 ? -4.276  -70.110  50.716  1.000 116.539 0 445 VAL III CG2 1 ? 34 
ATOM   11098 N N   . GLY I  1 117 ? -2.362  -67.979  47.518  1.000 107.589 0 446 GLY III N   1 ? 34 
ATOM   11099 C CA  . GLY I  1 117 ? -2.286  -66.537  47.213  1.000 106.984 0 446 GLY III CA  1 ? 34 
ATOM   11100 C C   . GLY I  1 117 ? -0.864  -66.007  47.320  1.000 103.664 0 446 GLY III C   1 ? 34 
ATOM   11101 O O   . GLY I  1 117 ? -0.661  -64.822  46.960  1.000 104.297 0 446 GLY III O   1 ? 34 
ATOM   11102 N N   . GLY I  1 118 ? 0.105   -66.849  47.698  1.000 100.006 0 447 GLY III N   1 ? 34 
ATOM   11103 C CA  . GLY I  1 118 ? 1.537   -66.525  47.615  1.000 95.083  0 447 GLY III CA  1 ? 34 
ATOM   11104 C C   . GLY I  1 118 ? 2.082   -65.980  48.921  1.000 92.848  0 447 GLY III C   1 ? 34 
ATOM   11105 O O   . GLY I  1 118 ? 1.444   -65.084  49.481  1.000 92.196  0 447 GLY III O   1 ? 34 
ATOM   11106 N N   . ASN I  1 119 ? 3.231   -66.499  49.372  1.000 89.800  0 448 ASN III N   1 ? 34 
ATOM   11107 C CA  . ASN I  1 119 ? 3.987   -65.960  50.530  1.000 87.156  0 448 ASN III CA  1 ? 34 
ATOM   11108 C C   . ASN I  1 119 ? 4.980   -64.903  50.018  1.000 83.967  0 448 ASN III C   1 ? 34 
ATOM   11109 O O   . ASN I  1 119 ? 5.922   -65.266  49.298  1.000 79.047  0 448 ASN III O   1 ? 34 
ATOM   11110 C CB  . ASN I  1 119 ? 4.665   -67.073  51.325  1.000 84.679  0 448 ASN III CB  1 ? 34 
ATOM   11111 C CG  . ASN I  1 119 ? 5.440   -66.554  52.518  1.000 81.288  0 448 ASN III CG  1 ? 34 
ATOM   11112 O OD1 . ASN I  1 119 ? 5.301   -65.403  52.910  1.000 80.244  0 448 ASN III OD1 1 ? 34 
ATOM   11113 N ND2 . ASN I  1 119 ? 6.290   -67.383  53.097  1.000 81.292  0 448 ASN III ND2 1 ? 34 
ATOM   11114 N N   . TYR I  1 120 ? 4.765   -63.643  50.392  1.000 85.475  0 449 TYR III N   1 ? 34 
ATOM   11115 C CA  . TYR I  1 120 ? 5.567   -62.485  49.943  1.000 83.887  0 449 TYR III CA  1 ? 34 
ATOM   11116 C C   . TYR I  1 120 ? 6.495   -62.037  51.084  1.000 81.494  0 449 TYR III C   1 ? 34 
ATOM   11117 O O   . TYR I  1 120 ? 7.189   -61.005  50.887  1.000 80.197  0 449 TYR III O   1 ? 34 
ATOM   11118 C CB  . TYR I  1 120 ? 4.649   -61.384  49.402  1.000 87.245  0 449 TYR III CB  1 ? 34 
ATOM   11119 C CG  . TYR I  1 120 ? 3.925   -61.759  48.130  1.000 91.653  0 449 TYR III CG  1 ? 34 
ATOM   11120 C CD1 . TYR I  1 120 ? 2.773   -62.528  48.162  1.000 96.050  0 449 TYR III CD1 1 ? 34 
ATOM   11121 C CD2 . TYR I  1 120 ? 4.372   -61.321  46.889  1.000 91.637  0 449 TYR III CD2 1 ? 34 
ATOM   11122 C CE1 . TYR I  1 120 ? 2.088   -62.867  47.002  1.000 98.682  0 449 TYR III CE1 1 ? 34 
ATOM   11123 C CE2 . TYR I  1 120 ? 3.707   -61.659  45.718  1.000 95.421  0 449 TYR III CE2 1 ? 34 
ATOM   11124 C CZ  . TYR I  1 120 ? 2.569   -62.450  45.772  1.000 98.856  0 449 TYR III CZ  1 ? 34 
ATOM   11125 O OH  . TYR I  1 120 ? 1.891   -62.780  44.631  1.000 98.995  0 449 TYR III OH  1 ? 34 
ATOM   11126 N N   . ASN I  1 121 ? 6.621   -62.816  52.171  1.000 79.116  0 450 ASN III N   1 ? 34 
ATOM   11127 C CA  . ASN I  1 121 ? 7.510   -62.467  53.312  1.000 76.616  0 450 ASN III CA  1 ? 34 
ATOM   11128 C C   . ASN I  1 121 ? 8.997   -62.598  52.938  1.000 71.173  0 450 ASN III C   1 ? 34 
ATOM   11129 O O   . ASN I  1 121 ? 9.798   -61.859  53.518  1.000 69.547  0 450 ASN III O   1 ? 34 
ATOM   11130 C CB  . ASN I  1 121 ? 7.212   -63.300  54.560  1.000 78.693  0 450 ASN III CB  1 ? 34 
ATOM   11131 C CG  . ASN I  1 121 ? 5.918   -62.888  55.225  1.000 84.560  0 450 ASN III CG  1 ? 34 
ATOM   11132 O OD1 . ASN I  1 121 ? 5.386   -61.799  54.994  1.000 89.341  0 450 ASN III OD1 1 ? 34 
ATOM   11133 N ND2 . ASN I  1 121 ? 5.383   -63.775  56.038  1.000 85.610  0 450 ASN III ND2 1 ? 34 
ATOM   11134 N N   . TYR I  1 122 ? 9.375   -63.504  52.036  1.000 67.964  0 451 TYR III N   1 ? 34 
ATOM   11135 C CA  . TYR I  1 122 ? 10.810  -63.735  51.724  1.000 65.456  0 451 TYR III CA  1 ? 34 
ATOM   11136 C C   . TYR I  1 122 ? 11.256  -62.804  50.596  1.000 63.054  0 451 TYR III C   1 ? 34 
ATOM   11137 O O   . TYR I  1 122 ? 10.608  -62.780  49.529  1.000 63.464  0 451 TYR III O   1 ? 34 
ATOM   11138 C CB  . TYR I  1 122 ? 11.083  -65.208  51.432  1.000 63.525  0 451 TYR III CB  1 ? 34 
ATOM   11139 C CG  . TYR I  1 122 ? 10.900  -66.108  52.626  1.000 62.517  0 451 TYR III CG  1 ? 34 
ATOM   11140 C CD1 . TYR I  1 122 ? 11.826  -66.113  53.658  1.000 60.606  0 451 TYR III CD1 1 ? 34 
ATOM   11141 C CD2 . TYR I  1 122 ? 9.825   -66.978  52.709  1.000 64.371  0 451 TYR III CD2 1 ? 34 
ATOM   11142 C CE1 . TYR I  1 122 ? 11.707  -66.969  54.740  1.000 59.642  0 451 TYR III CE1 1 ? 34 
ATOM   11143 C CE2 . TYR I  1 122 ? 9.672   -67.814  53.801  1.000 64.619  0 451 TYR III CE2 1 ? 34 
ATOM   11144 C CZ  . TYR I  1 122 ? 10.629  -67.828  54.807  1.000 62.741  0 451 TYR III CZ  1 ? 34 
ATOM   11145 O OH  . TYR I  1 122 ? 10.492  -68.673  55.868  1.000 63.419  0 451 TYR III OH  1 ? 34 
ATOM   11146 N N   . LEU I  1 123 ? 12.339  -62.064  50.854  1.000 60.620  0 452 LEU III N   1 ? 34 
ATOM   11147 C CA  . LEU I  1 123 ? 12.889  -61.018  49.962  1.000 59.852  0 452 LEU III CA  1 ? 34 
ATOM   11148 C C   . LEU I  1 123 ? 14.287  -61.430  49.501  1.000 61.840  0 452 LEU III C   1 ? 34 
ATOM   11149 O O   . LEU I  1 123 ? 14.959  -62.205  50.207  1.000 61.794  0 452 LEU III O   1 ? 34 
ATOM   11150 C CB  . LEU I  1 123 ? 12.943  -59.685  50.716  1.000 59.163  0 452 LEU III CB  1 ? 34 
ATOM   11151 C CG  . LEU I  1 123 ? 11.617  -59.162  51.285  1.000 60.819  0 452 LEU III CG  1 ? 34 
ATOM   11152 C CD1 . LEU I  1 123 ? 11.806  -57.814  51.961  1.000 60.488  0 452 LEU III CD1 1 ? 34 
ATOM   11153 C CD2 . LEU I  1 123 ? 10.539  -59.054  50.206  1.000 63.240  0 452 LEU III CD2 1 ? 34 
ATOM   11154 N N   . TYR I  1 124 ? 14.709  -60.909  48.350  1.000 63.561  0 453 TYR III N   1 ? 34 
ATOM   11155 C CA  . TYR I  1 124 ? 16.106  -60.983  47.858  1.000 61.299  0 453 TYR III CA  1 ? 34 
ATOM   11156 C C   . TYR I  1 124 ? 16.480  -59.624  47.271  1.000 61.377  0 453 TYR III C   1 ? 34 
ATOM   11157 O O   . TYR I  1 124 ? 15.586  -58.935  46.774  1.000 63.520  0 453 TYR III O   1 ? 34 
ATOM   11158 C CB  . TYR I  1 124 ? 16.253  -62.108  46.836  1.000 61.603  0 453 TYR III CB  1 ? 34 
ATOM   11159 C CG  . TYR I  1 124 ? 15.446  -61.907  45.581  1.000 63.811  0 453 TYR III CG  1 ? 34 
ATOM   11160 C CD1 . TYR I  1 124 ? 14.130  -62.328  45.497  1.000 66.804  0 453 TYR III CD1 1 ? 34 
ATOM   11161 C CD2 . TYR I  1 124 ? 16.008  -61.307  44.479  1.000 64.271  0 453 TYR III CD2 1 ? 34 
ATOM   11162 C CE1 . TYR I  1 124 ? 13.382  -62.151  44.348  1.000 68.694  0 453 TYR III CE1 1 ? 34 
ATOM   11163 C CE2 . TYR I  1 124 ? 15.272  -61.121  43.320  1.000 67.956  0 453 TYR III CE2 1 ? 34 
ATOM   11164 C CZ  . TYR I  1 124 ? 13.953  -61.526  43.257  1.000 70.254  0 453 TYR III CZ  1 ? 34 
ATOM   11165 O OH  . TYR I  1 124 ? 13.240  -61.307  42.118  1.000 73.833  0 453 TYR III OH  1 ? 34 
ATOM   11166 N N   . ARG I  1 125 ? 17.756  -59.253  47.325  1.000 57.324  0 454 ARG III N   1 ? 34 
ATOM   11167 C CA  . ARG I  1 125 ? 18.263  -58.023  46.673  1.000 57.995  0 454 ARG III CA  1 ? 34 
ATOM   11168 C C   . ARG I  1 125 ? 18.370  -58.309  45.171  1.000 59.058  0 454 ARG III C   1 ? 34 
ATOM   11169 O O   . ARG I  1 125 ? 19.036  -59.274  44.786  1.000 57.509  0 454 ARG III O   1 ? 34 
ATOM   11170 C CB  . ARG I  1 125 ? 19.581  -57.578  47.305  1.000 55.058  0 454 ARG III CB  1 ? 34 
ATOM   11171 C CG  . ARG I  1 125 ? 20.055  -56.224  46.819  1.000 56.605  0 454 ARG III CG  1 ? 34 
ATOM   11172 C CD  . ARG I  1 125 ? 21.281  -55.744  47.577  1.000 56.745  0 454 ARG III CD  1 ? 34 
ATOM   11173 N NE  . ARG I  1 125 ? 21.002  -55.672  49.010  1.000 56.616  0 454 ARG III NE  1 ? 34 
ATOM   11174 C CZ  . ARG I  1 125 ? 20.345  -54.678  49.616  1.000 57.008  0 454 ARG III CZ  1 ? 34 
ATOM   11175 N NH1 . ARG I  1 125 ? 19.868  -53.643  48.930  1.000 60.916  0 454 ARG III NH1 1 ? 34 
ATOM   11176 N NH2 . ARG I  1 125 ? 20.147  -54.727  50.921  1.000 55.916  0 454 ARG III NH2 1 ? 34 
ATOM   11177 N N   . LEU I  1 126 ? 17.685  -57.510  44.358  1.000 62.911  0 455 LEU III N   1 ? 34 
ATOM   11178 C CA  . LEU I  1 126 ? 17.562  -57.706  42.889  1.000 65.871  0 455 LEU III CA  1 ? 34 
ATOM   11179 C C   . LEU I  1 126 ? 18.585  -56.825  42.174  1.000 66.484  0 455 LEU III C   1 ? 34 
ATOM   11180 O O   . LEU I  1 126 ? 19.080  -57.222  41.105  1.000 67.038  0 455 LEU III O   1 ? 34 
ATOM   11181 C CB  . LEU I  1 126 ? 16.133  -57.363  42.475  1.000 69.784  0 455 LEU III CB  1 ? 34 
ATOM   11182 C CG  . LEU I  1 126 ? 15.842  -57.408  40.971  1.000 72.736  0 455 LEU III CG  1 ? 34 
ATOM   11183 C CD1 . LEU I  1 126 ? 16.193  -58.738  40.322  1.000 71.110  0 455 LEU III CD1 1 ? 34 
ATOM   11184 C CD2 . LEU I  1 126 ? 14.386  -57.069  40.711  1.000 75.425  0 455 LEU III CD2 1 ? 34 
ATOM   11185 N N   . PHE I  1 127 ? 18.879  -55.659  42.753  1.000 65.886  0 456 PHE III N   1 ? 34 
ATOM   11186 C CA  . PHE I  1 127 ? 19.787  -54.622  42.211  1.000 68.770  0 456 PHE III CA  1 ? 34 
ATOM   11187 C C   . PHE I  1 127 ? 20.839  -54.274  43.264  1.000 64.976  0 456 PHE III C   1 ? 34 
ATOM   11188 O O   . PHE I  1 127 ? 20.519  -54.147  44.445  1.000 62.259  0 456 PHE III O   1 ? 34 
ATOM   11189 C CB  . PHE I  1 127 ? 18.993  -53.369  41.821  1.000 72.499  0 456 PHE III CB  1 ? 34 
ATOM   11190 C CG  . PHE I  1 127 ? 17.856  -53.606  40.859  1.000 76.053  0 456 PHE III CG  1 ? 34 
ATOM   11191 C CD1 . PHE I  1 127 ? 18.101  -53.981  39.547  1.000 77.502  0 456 PHE III CD1 1 ? 34 
ATOM   11192 C CD2 . PHE I  1 127 ? 16.538  -53.457  41.263  1.000 79.045  0 456 PHE III CD2 1 ? 34 
ATOM   11193 C CE1 . PHE I  1 127 ? 17.051  -54.230  38.670  1.000 79.134  0 456 PHE III CE1 1 ? 34 
ATOM   11194 C CE2 . PHE I  1 127 ? 15.500  -53.733  40.390  1.000 82.172  0 456 PHE III CE2 1 ? 34 
ATOM   11195 C CZ  . PHE I  1 127 ? 15.747  -54.063  39.081  1.000 82.134  0 456 PHE III CZ  1 ? 34 
ATOM   11196 N N   . ARG I  1 128 ? 22.073  -54.100  42.818  1.000 65.606  0 457 ARG III N   1 ? 34 
ATOM   11197 C CA  . ARG I  1 128 ? 23.158  -53.550  43.663  1.000 65.417  0 457 ARG III CA  1 ? 34 
ATOM   11198 C C   . ARG I  1 128 ? 24.230  -52.967  42.744  1.000 68.238  0 457 ARG III C   1 ? 34 
ATOM   11199 O O   . ARG I  1 128 ? 24.454  -53.532  41.654  1.000 69.671  0 457 ARG III O   1 ? 34 
ATOM   11200 C CB  . ARG I  1 128 ? 23.724  -54.637  44.575  1.000 62.037  0 457 ARG III CB  1 ? 34 
ATOM   11201 C CG  . ARG I  1 128 ? 24.587  -54.091  45.699  1.000 60.535  0 457 ARG III CG  1 ? 34 
ATOM   11202 C CD  . ARG I  1 128 ? 24.907  -55.189  46.687  1.000 58.863  0 457 ARG III CD  1 ? 34 
ATOM   11203 N NE  . ARG I  1 128 ? 25.439  -54.685  47.935  1.000 58.898  0 457 ARG III NE  1 ? 34 
ATOM   11204 C CZ  . ARG I  1 128 ? 26.722  -54.431  48.163  1.000 61.036  0 457 ARG III CZ  1 ? 34 
ATOM   11205 N NH1 . ARG I  1 128 ? 27.631  -54.641  47.227  1.000 62.705  0 457 ARG III NH1 1 ? 34 
ATOM   11206 N NH2 . ARG I  1 128 ? 27.108  -53.982  49.346  1.000 61.281  0 457 ARG III NH2 1 ? 34 
ATOM   11207 N N   . LYS I  1 129 ? 24.868  -51.883  43.181  1.000 71.448  0 458 LYS III N   1 ? 34 
ATOM   11208 C CA  . LYS I  1 129 ? 25.848  -51.127  42.356  1.000 76.388  0 458 LYS III CA  1 ? 34 
ATOM   11209 C C   . LYS I  1 129 ? 27.109  -51.971  42.162  1.000 73.721  0 458 LYS III C   1 ? 34 
ATOM   11210 O O   . LYS I  1 129 ? 27.791  -51.730  41.162  1.000 74.963  0 458 LYS III O   1 ? 34 
ATOM   11211 C CB  . LYS I  1 129 ? 26.101  -49.740  42.951  1.000 80.895  0 458 LYS III CB  1 ? 34 
ATOM   11212 C CG  . LYS I  1 129 ? 24.908  -48.816  42.742  1.000 84.049  0 458 LYS III CG  1 ? 34 
ATOM   11213 C CD  . LYS I  1 129 ? 24.913  -47.510  43.512  1.000 87.215  0 458 LYS III CD  1 ? 34 
ATOM   11214 C CE  . LYS I  1 129 ? 23.501  -47.004  43.747  1.000 90.061  0 458 LYS III CE  1 ? 34 
ATOM   11215 N NZ  . LYS I  1 129 ? 23.387  -45.517  43.772  1.000 94.558  0 458 LYS III NZ  1 ? 34 
ATOM   11216 N N   . SER I  1 130 ? 27.397  -52.920  43.049  1.000 67.840  0 459 SER III N   1 ? 34 
ATOM   11217 C CA  . SER I  1 130 ? 28.592  -53.791  42.932  1.000 65.249  0 459 SER III CA  1 ? 34 
ATOM   11218 C C   . SER I  1 130 ? 28.375  -55.094  43.704  1.000 61.003  0 459 SER III C   1 ? 34 
ATOM   11219 O O   . SER I  1 130 ? 27.446  -55.136  44.524  1.000 61.677  0 459 SER III O   1 ? 34 
ATOM   11220 C CB  . SER I  1 130 ? 29.818  -53.055  43.388  1.000 64.805  0 459 SER III CB  1 ? 34 
ATOM   11221 O OG  . SER I  1 130 ? 29.904  -53.076  44.792  1.000 62.875  0 459 SER III OG  1 ? 34 
ATOM   11222 N N   . ASN I  1 131 ? 29.178  -56.119  43.421  1.000 58.228  0 460 ASN III N   1 ? 34 
ATOM   11223 C CA  . ASN I  1 131 ? 29.013  -57.474  44.014  1.000 53.800  0 460 ASN III CA  1 ? 34 
ATOM   11224 C C   . ASN I  1 131 ? 29.411  -57.443  45.490  1.000 51.318  0 460 ASN III C   1 ? 34 
ATOM   11225 O O   . ASN I  1 131 ? 30.297  -56.693  45.836  1.000 50.660  0 460 ASN III O   1 ? 34 
ATOM   11226 C CB  . ASN I  1 131 ? 29.803  -58.544  43.263  1.000 52.203  0 460 ASN III CB  1 ? 34 
ATOM   11227 C CG  . ASN I  1 131 ? 29.307  -58.764  41.850  1.000 53.230  0 460 ASN III CG  1 ? 34 
ATOM   11228 O OD1 . ASN I  1 131 ? 28.274  -58.222  41.466  1.000 56.557  0 460 ASN III OD1 1 ? 34 
ATOM   11229 N ND2 . ASN I  1 131 ? 30.025  -59.547  41.057  1.000 51.863  0 460 ASN III ND2 1 ? 34 
ATOM   11230 N N   . LEU I  1 132 ? 28.741  -58.238  46.317  1.000 49.177  0 461 LEU III N   1 ? 34 
ATOM   11231 C CA  . LEU I  1 132 ? 29.140  -58.492  47.719  1.000 48.131  0 461 LEU III CA  1 ? 34 
ATOM   11232 C C   . LEU I  1 132 ? 30.534  -59.111  47.734  1.000 46.790  0 461 LEU III C   1 ? 34 
ATOM   11233 O O   . LEU I  1 132 ? 30.798  -59.984  46.888  1.000 46.827  0 461 LEU III O   1 ? 34 
ATOM   11234 C CB  . LEU I  1 132 ? 28.148  -59.461  48.365  1.000 46.383  0 461 LEU III CB  1 ? 34 
ATOM   11235 C CG  . LEU I  1 132 ? 26.761  -58.931  48.643  1.000 47.236  0 461 LEU III CG  1 ? 34 
ATOM   11236 C CD1 . LEU I  1 132 ? 25.972  -60.003  49.383  1.000 47.443  0 461 LEU III CD1 1 ? 34 
ATOM   11237 C CD2 . LEU I  1 132 ? 26.795  -57.631  49.426  1.000 48.762  0 461 LEU III CD2 1 ? 34 
ATOM   11238 N N   . LYS I  1 133 ? 31.347  -58.707  48.703  1.000 47.372  0 462 LYS III N   1 ? 34 
ATOM   11239 C CA  . LYS I  1 133 ? 32.544  -59.470  49.138  1.000 48.821  0 462 LYS III CA  1 ? 34 
ATOM   11240 C C   . LYS I  1 133 ? 32.072  -60.737  49.858  1.000 48.419  0 462 LYS III C   1 ? 34 
ATOM   11241 O O   . LYS I  1 133 ? 30.942  -60.809  50.353  1.000 46.679  0 462 LYS III O   1 ? 34 
ATOM   11242 C CB  . LYS I  1 133 ? 33.426  -58.600  50.032  1.000 50.847  0 462 LYS III CB  1 ? 34 
ATOM   11243 C CG  . LYS I  1 133 ? 34.191  -57.518  49.287  1.000 57.299  0 462 LYS III CG  1 ? 34 
ATOM   11244 C CD  . LYS I  1 133 ? 34.864  -56.460  50.117  1.000 62.641  0 462 LYS III CD  1 ? 34 
ATOM   11245 C CE  . LYS I  1 133 ? 35.548  -55.494  49.160  1.000 70.470  0 462 LYS III CE  1 ? 34 
ATOM   11246 N NZ  . LYS I  1 133 ? 36.408  -54.484  49.833  1.000 75.222  0 462 LYS III NZ  1 ? 34 
ATOM   11247 N N   . PRO I  1 134 ? 32.903  -61.799  49.909  1.000 47.271  0 463 PRO III N   1 ? 34 
ATOM   11248 C CA  . PRO I  1 134 ? 32.527  -63.021  50.616  1.000 47.176  0 463 PRO III CA  1 ? 34 
ATOM   11249 C C   . PRO I  1 134 ? 32.089  -62.748  52.064  1.000 47.088  0 463 PRO III C   1 ? 34 
ATOM   11250 O O   . PRO I  1 134 ? 32.749  -62.017  52.721  1.000 48.567  0 463 PRO III O   1 ? 34 
ATOM   11251 C CB  . PRO I  1 134 ? 33.785  -63.884  50.528  1.000 46.104  0 463 PRO III CB  1 ? 34 
ATOM   11252 C CG  . PRO I  1 134 ? 34.396  -63.430  49.218  1.000 47.105  0 463 PRO III CG  1 ? 34 
ATOM   11253 C CD  . PRO I  1 134 ? 34.172  -61.934  49.197  1.000 47.389  0 463 PRO III CD  1 ? 34 
ATOM   11254 N N   . PHE I  1 135 ? 30.947  -63.308  52.464  1.000 45.670  0 464 PHE III N   1 ? 34 
ATOM   11255 C CA  . PHE I  1 135 ? 30.334  -63.212  53.812  1.000 46.633  0 464 PHE III CA  1 ? 34 
ATOM   11256 C C   . PHE I  1 135 ? 29.921  -61.770  54.129  1.000 48.612  0 464 PHE III C   1 ? 34 
ATOM   11257 O O   . PHE I  1 135 ? 29.640  -61.494  55.301  1.000 48.812  0 464 PHE III O   1 ? 34 
ATOM   11258 C CB  . PHE I  1 135 ? 31.301  -63.757  54.860  1.000 45.346  0 464 PHE III CB  1 ? 34 
ATOM   11259 C CG  . PHE I  1 135 ? 31.553  -65.236  54.767  1.000 45.601  0 464 PHE III CG  1 ? 34 
ATOM   11260 C CD1 . PHE I  1 135 ? 30.491  -66.132  54.807  1.000 45.447  0 464 PHE III CD1 1 ? 34 
ATOM   11261 C CD2 . PHE I  1 135 ? 32.854  -65.729  54.664  1.000 46.069  0 464 PHE III CD2 1 ? 34 
ATOM   11262 C CE1 . PHE I  1 135 ? 30.727  -67.499  54.761  1.000 45.316  0 464 PHE III CE1 1 ? 34 
ATOM   11263 C CE2 . PHE I  1 135 ? 33.086  -67.090  54.590  1.000 45.523  0 464 PHE III CE2 1 ? 34 
ATOM   11264 C CZ  . PHE I  1 135 ? 32.030  -67.972  54.622  1.000 45.471  0 464 PHE III CZ  1 ? 34 
ATOM   11265 N N   . GLU I  1 136 ? 29.841  -60.888  53.132  1.000 50.636  0 465 GLU III N   1 ? 34 
ATOM   11266 C CA  . GLU I  1 136 ? 29.278  -59.530  53.324  1.000 52.268  0 465 GLU III CA  1 ? 34 
ATOM   11267 C C   . GLU I  1 136 ? 27.750  -59.665  53.406  1.000 53.626  0 465 GLU III C   1 ? 34 
ATOM   11268 O O   . GLU I  1 136 ? 27.156  -60.606  52.826  1.000 52.972  0 465 GLU III O   1 ? 34 
ATOM   11269 C CB  . GLU I  1 136 ? 29.705  -58.589  52.187  1.000 54.776  0 465 GLU III CB  1 ? 34 
ATOM   11270 C CG  . GLU I  1 136 ? 29.478  -57.110  52.495  1.000 55.484  0 465 GLU III CG  1 ? 34 
ATOM   11271 C CD  . GLU I  1 136 ? 29.934  -56.140  51.414  1.000 58.342  0 465 GLU III CD  1 ? 34 
ATOM   11272 O OE1 . GLU I  1 136 ? 30.521  -56.592  50.406  1.000 59.174  0 465 GLU III OE1 1 ? 34 
ATOM   11273 O OE2 . GLU I  1 136 ? 29.699  -54.926  51.569  1.000 60.535  0 465 GLU III OE2 1 ? 34 
ATOM   11274 N N   . ARG I  1 137 ? 27.134  -58.745  54.139  1.000 55.112  0 466 ARG III N   1 ? 34 
ATOM   11275 C CA  . ARG I  1 137 ? 25.676  -58.701  54.384  1.000 53.084  0 466 ARG III CA  1 ? 34 
ATOM   11276 C C   . ARG I  1 137 ? 25.224  -57.272  54.133  1.000 53.635  0 466 ARG III C   1 ? 34 
ATOM   11277 O O   . ARG I  1 137 ? 25.834  -56.375  54.688  1.000 52.629  0 466 ARG III O   1 ? 34 
ATOM   11278 C CB  . ARG I  1 137 ? 25.410  -59.097  55.829  1.000 52.290  0 466 ARG III CB  1 ? 34 
ATOM   11279 C CG  . ARG I  1 137 ? 23.947  -59.290  56.184  1.000 52.491  0 466 ARG III CG  1 ? 34 
ATOM   11280 C CD  . ARG I  1 137 ? 23.964  -60.074  57.482  1.000 51.240  0 466 ARG III CD  1 ? 34 
ATOM   11281 N NE  . ARG I  1 137 ? 22.648  -60.387  57.974  1.000 52.983  0 466 ARG III NE  1 ? 34 
ATOM   11282 C CZ  . ARG I  1 137 ? 21.910  -59.594  58.748  1.000 55.218  0 466 ARG III CZ  1 ? 34 
ATOM   11283 N NH1 . ARG I  1 137 ? 22.317  -58.397  59.108  1.000 57.453  0 466 ARG III NH1 1 ? 34 
ATOM   11284 N NH2 . ARG I  1 137 ? 20.736  -60.001  59.163  1.000 57.029  0 466 ARG III NH2 1 ? 34 
ATOM   11285 N N   . ASP I  1 138 ? 24.215  -57.082  53.293  1.000 53.535  0 467 ASP III N   1 ? 34 
ATOM   11286 C CA  . ASP I  1 138 ? 23.704  -55.734  52.951  1.000 53.837  0 467 ASP III CA  1 ? 34 
ATOM   11287 C C   . ASP I  1 138 ? 22.215  -55.758  53.268  1.000 55.674  0 467 ASP III C   1 ? 34 
ATOM   11288 O O   . ASP I  1 138 ? 21.488  -56.523  52.607  1.000 56.895  0 467 ASP III O   1 ? 34 
ATOM   11289 C CB  . ASP I  1 138 ? 24.013  -55.389  51.499  1.000 53.513  0 467 ASP III CB  1 ? 34 
ATOM   11290 C CG  . ASP I  1 138 ? 23.598  -53.991  51.095  1.000 57.558  0 467 ASP III CG  1 ? 34 
ATOM   11291 O OD1 . ASP I  1 138 ? 22.864  -53.325  51.878  1.000 59.970  0 467 ASP III OD1 1 ? 34 
ATOM   11292 O OD2 . ASP I  1 138 ? 23.995  -53.583  49.990  1.000 59.127  0 467 ASP III OD2 1 ? 34 
ATOM   11293 N N   . ILE I  1 139 ? 21.792  -54.983  54.264  1.000 56.073  0 468 ILE III N   1 ? 34 
ATOM   11294 C CA  . ILE I  1 139 ? 20.364  -54.881  54.682  1.000 58.118  0 468 ILE III CA  1 ? 34 
ATOM   11295 C C   . ILE I  1 139 ? 19.873  -53.458  54.402  1.000 59.341  0 468 ILE III C   1 ? 34 
ATOM   11296 O O   . ILE I  1 139 ? 18.803  -53.106  54.889  1.000 61.656  0 468 ILE III O   1 ? 34 
ATOM   11297 C CB  . ILE I  1 139 ? 20.219  -55.295  56.160  1.000 59.457  0 468 ILE III CB  1 ? 34 
ATOM   11298 C CG1 . ILE I  1 139 ? 21.044  -54.415  57.111  1.000 60.893  0 468 ILE III CG1 1 ? 34 
ATOM   11299 C CG2 . ILE I  1 139 ? 20.562  -56.770  56.310  1.000 57.039  0 468 ILE III CG2 1 ? 34 
ATOM   11300 C CD1 . ILE I  1 139 ? 20.740  -54.620  58.571  1.000 61.580  0 468 ILE III CD1 1 ? 34 
ATOM   11301 N N   . SER I  1 140 ? 20.614  -52.664  53.624  1.000 60.290  0 469 SER III N   1 ? 34 
ATOM   11302 C CA  . SER I  1 140 ? 20.199  -51.297  53.204  1.000 63.002  0 469 SER III CA  1 ? 34 
ATOM   11303 C C   . SER I  1 140 ? 18.995  -51.409  52.261  1.000 64.425  0 469 SER III C   1 ? 34 
ATOM   11304 O O   . SER I  1 140 ? 18.832  -52.450  51.593  1.000 61.768  0 469 SER III O   1 ? 34 
ATOM   11305 C CB  . SER I  1 140 ? 21.312  -50.524  52.572  1.000 63.230  0 469 SER III CB  1 ? 34 
ATOM   11306 O OG  . SER I  1 140 ? 21.669  -51.102  51.336  1.000 62.552  0 469 SER III OG  1 ? 34 
ATOM   11307 N N   . THR I  1 141 ? 18.161  -50.379  52.249  1.000 67.552  0 470 THR III N   1 ? 34 
ATOM   11308 C CA  . THR I  1 141 ? 16.896  -50.339  51.478  1.000 69.221  0 470 THR III CA  1 ? 34 
ATOM   11309 C C   . THR I  1 141 ? 16.843  -49.001  50.754  1.000 72.535  0 470 THR III C   1 ? 34 
ATOM   11310 O O   . THR I  1 141 ? 15.764  -48.424  50.713  1.000 77.678  0 470 THR III O   1 ? 34 
ATOM   11311 C CB  . THR I  1 141 ? 15.702  -50.575  52.422  1.000 67.650  0 470 THR III CB  1 ? 34 
ATOM   11312 O OG1 . THR I  1 141 ? 15.789  -49.679  53.532  1.000 66.142  0 470 THR III OG1 1 ? 34 
ATOM   11313 C CG2 . THR I  1 141 ? 15.633  -51.996  52.931  1.000 65.345  0 470 THR III CG2 1 ? 34 
ATOM   11314 N N   . GLU I  1 142 ? 17.991  -48.478  50.290  1.000 73.229  0 471 GLU III N   1 ? 34 
ATOM   11315 C CA  . GLU I  1 142 ? 18.033  -47.214  49.508  1.000 77.696  0 471 GLU III CA  1 ? 34 
ATOM   11316 C C   . GLU I  1 142 ? 17.513  -47.506  48.108  1.000 77.349  0 471 GLU III C   1 ? 34 
ATOM   11317 O O   . GLU I  1 142 ? 17.830  -48.592  47.602  1.000 75.807  0 471 GLU III O   1 ? 34 
ATOM   11318 C CB  . GLU I  1 142 ? 19.425  -46.598  49.542  1.000 80.054  0 471 GLU III CB  1 ? 34 
ATOM   11319 C CG  . GLU I  1 142 ? 19.697  -46.066  50.942  1.000 85.515  0 471 GLU III CG  1 ? 34 
ATOM   11320 C CD  . GLU I  1 142 ? 21.079  -45.587  51.330  1.000 90.159  0 471 GLU III CD  1 ? 34 
ATOM   11321 O OE1 . GLU I  1 142 ? 22.091  -46.109  50.801  1.000 89.238  0 471 GLU III OE1 1 ? 34 
ATOM   11322 O OE2 . GLU I  1 142 ? 21.122  -44.696  52.203  1.000 94.355  0 471 GLU III OE2 1 ? 34 
ATOM   11323 N N   . ILE I  1 143 ? 16.699  -46.607  47.547  1.000 80.655  0 472 ILE III N   1 ? 34 
ATOM   11324 C CA  . ILE I  1 143 ? 16.110  -46.772  46.185  1.000 82.422  0 472 ILE III CA  1 ? 34 
ATOM   11325 C C   . ILE I  1 143 ? 17.281  -46.863  45.217  1.000 82.058  0 472 ILE III C   1 ? 34 
ATOM   11326 O O   . ILE I  1 143 ? 18.153  -45.968  45.290  1.000 83.726  0 472 ILE III O   1 ? 34 
ATOM   11327 C CB  . ILE I  1 143 ? 15.171  -45.601  45.834  1.000 86.310  0 472 ILE III CB  1 ? 34 
ATOM   11328 C CG1 . ILE I  1 143 ? 14.024  -45.481  46.836  1.000 85.925  0 472 ILE III CG1 1 ? 34 
ATOM   11329 C CG2 . ILE I  1 143 ? 14.654  -45.738  44.404  1.000 88.030  0 472 ILE III CG2 1 ? 34 
ATOM   11330 C CD1 . ILE I  1 143 ? 13.256  -46.739  47.048  1.000 83.726  0 472 ILE III CD1 1 ? 34 
ATOM   11331 N N   . TYR I  1 144 ? 17.307  -47.904  44.384  1.000 81.048  0 473 TYR III N   1 ? 34 
ATOM   11332 C CA  . TYR I  1 144 ? 18.382  -48.140  43.392  1.000 83.677  0 473 TYR III CA  1 ? 34 
ATOM   11333 C C   . TYR I  1 144 ? 18.078  -47.288  42.155  1.000 87.421  0 473 TYR III C   1 ? 34 
ATOM   11334 O O   . TYR I  1 144 ? 16.929  -47.348  41.575  1.000 87.257  0 473 TYR III O   1 ? 34 
ATOM   11335 C CB  . TYR I  1 144 ? 18.461  -49.627  43.050  1.000 83.009  0 473 TYR III CB  1 ? 34 
ATOM   11336 C CG  . TYR I  1 144 ? 19.472  -49.976  41.986  1.000 84.473  0 473 TYR III CG  1 ? 34 
ATOM   11337 C CD1 . TYR I  1 144 ? 20.802  -50.237  42.311  1.000 81.972  0 473 TYR III CD1 1 ? 34 
ATOM   11338 C CD2 . TYR I  1 144 ? 19.078  -50.120  40.655  1.000 88.326  0 473 TYR III CD2 1 ? 34 
ATOM   11339 C CE1 . TYR I  1 144 ? 21.729  -50.606  41.342  1.000 81.738  0 473 TYR III CE1 1 ? 34 
ATOM   11340 C CE2 . TYR I  1 144 ? 19.984  -50.454  39.668  1.000 87.767  0 473 TYR III CE2 1 ? 34 
ATOM   11341 C CZ  . TYR I  1 144 ? 21.317  -50.664  40.015  1.000 85.074  0 473 TYR III CZ  1 ? 34 
ATOM   11342 O OH  . TYR I  1 144 ? 22.214  -51.013  39.052  1.000 85.173  0 473 TYR III OH  1 ? 34 
ATOM   11343 N N   . GLN I  1 145 ? 19.051  -46.446  41.796  1.000 89.422  0 474 GLN III N   1 ? 34 
ATOM   11344 C CA  . GLN I  1 145 ? 18.981  -45.601  40.591  1.000 92.969  0 474 GLN III CA  1 ? 34 
ATOM   11345 C C   . GLN I  1 145 ? 19.472  -46.429  39.406  1.000 90.669  0 474 GLN III C   1 ? 34 
ATOM   11346 O O   . GLN I  1 145 ? 20.699  -46.638  39.286  1.000 86.205  0 474 GLN III O   1 ? 34 
ATOM   11347 C CB  . GLN I  1 145 ? 19.829  -44.360  40.785  1.000 96.577  0 474 GLN III CB  1 ? 34 
ATOM   11348 C CG  . GLN I  1 145 ? 19.781  -43.510  39.550  1.000 102.563 0 474 GLN III CG  1 ? 34 
ATOM   11349 C CD  . GLN I  1 145 ? 20.314  -42.134  39.838  1.000 108.002 0 474 GLN III CD  1 ? 34 
ATOM   11350 O OE1 . GLN I  1 145 ? 20.394  -41.705  40.993  1.000 108.352 0 474 GLN III OE1 1 ? 34 
ATOM   11351 N NE2 . GLN I  1 145 ? 20.708  -41.469  38.764  1.000 113.698 0 474 GLN III NE2 1 ? 34 
ATOM   11352 N N   . ALA I  1 146 ? 18.523  -46.925  38.608  1.000 93.587  0 475 ALA III N   1 ? 34 
ATOM   11353 C CA  . ALA I  1 146 ? 18.755  -47.809  37.448  1.000 94.989  0 475 ALA III CA  1 ? 34 
ATOM   11354 C C   . ALA I  1 146 ? 18.966  -46.942  36.187  1.000 100.554 0 475 ALA III C   1 ? 34 
ATOM   11355 O O   . ALA I  1 146 ? 19.423  -47.484  35.184  1.000 102.245 0 475 ALA III O   1 ? 34 
ATOM   11356 C CB  . ALA I  1 146 ? 17.581  -48.756  37.322  1.000 93.819  0 475 ALA III CB  1 ? 34 
ATOM   11357 N N   . GLY I  1 147 ? 18.617  -45.659  36.240  1.000 103.086 0 476 GLY III N   1 ? 34 
ATOM   11358 C CA  . GLY I  1 147 ? 18.653  -44.776  35.066  1.000 106.641 0 476 GLY III CA  1 ? 34 
ATOM   11359 C C   . GLY I  1 147 ? 19.059  -43.371  35.438  1.000 109.931 0 476 GLY III C   1 ? 34 
ATOM   11360 O O   . GLY I  1 147 ? 19.570  -43.179  36.529  1.000 108.604 0 476 GLY III O   1 ? 34 
ATOM   11361 N N   . SER I  1 148 ? 18.850  -42.443  34.504  1.000 114.216 0 477 SER III N   1 ? 34 
ATOM   11362 C CA  . SER I  1 148 ? 19.453  -41.093  34.447  1.000 118.317 0 477 SER III CA  1 ? 34 
ATOM   11363 C C   . SER I  1 148 ? 19.060  -40.281  35.684  1.000 119.171 0 477 SER III C   1 ? 34 
ATOM   11364 O O   . SER I  1 148 ? 19.960  -39.687  36.325  1.000 120.264 0 477 SER III O   1 ? 34 
ATOM   11365 C CB  . SER I  1 148 ? 18.980  -40.411  33.200  1.000 122.920 0 477 SER III CB  1 ? 34 
ATOM   11366 O OG  . SER I  1 148 ? 17.576  -40.522  33.120  1.000 123.107 0 477 SER III OG  1 ? 34 
ATOM   11367 N N   . THR I  1 149 ? 17.754  -40.185  35.987  1.000 118.697 0 478 THR III N   1 ? 34 
ATOM   11368 C CA  . THR I  1 149 ? 17.213  -39.199  36.973  1.000 119.262 0 478 THR III CA  1 ? 34 
ATOM   11369 C C   . THR I  1 149 ? 17.594  -39.657  38.378  1.000 117.877 0 478 THR III C   1 ? 34 
ATOM   11370 O O   . THR I  1 149 ? 17.576  -40.856  38.667  1.000 112.524 0 478 THR III O   1 ? 34 
ATOM   11371 C CB  . THR I  1 149 ? 15.699  -39.012  36.829  1.000 118.952 0 478 THR III CB  1 ? 34 
ATOM   11372 O OG1 . THR I  1 149 ? 15.386  -38.794  35.461  1.000 122.212 0 478 THR III OG1 1 ? 34 
ATOM   11373 C CG2 . THR I  1 149 ? 15.177  -37.827  37.606  1.000 120.412 0 478 THR III CG2 1 ? 34 
ATOM   11374 N N   . PRO I  1 150 ? 17.957  -38.738  39.306  1.000 122.272 0 479 PRO III N   1 ? 34 
ATOM   11375 C CA  . PRO I  1 150 ? 18.112  -39.103  40.719  1.000 119.012 0 479 PRO III CA  1 ? 34 
ATOM   11376 C C   . PRO I  1 150 ? 16.739  -39.457  41.321  1.000 117.464 0 479 PRO III C   1 ? 34 
ATOM   11377 O O   . PRO I  1 150 ? 15.729  -38.953  40.831  1.000 119.278 0 479 PRO III O   1 ? 34 
ATOM   11378 C CB  . PRO I  1 150 ? 18.729  -37.852  41.366  1.000 122.197 0 479 PRO III CB  1 ? 34 
ATOM   11379 C CG  . PRO I  1 150 ? 18.298  -36.708  40.461  1.000 126.780 0 479 PRO III CG  1 ? 34 
ATOM   11380 C CD  . PRO I  1 150 ? 18.228  -37.311  39.070  1.000 127.062 0 479 PRO III CD  1 ? 34 
ATOM   11381 N N   . CYS I  1 151 ? 16.701  -40.332  42.334  1.000 111.315 0 480 CYS III N   1 ? 34 
ATOM   11382 C CA  . CYS I  1 151 ? 15.457  -41.012  42.776  1.000 109.606 0 480 CYS III CA  1 ? 34 
ATOM   11383 C C   . CYS I  1 151 ? 14.818  -40.323  43.986  1.000 109.092 0 480 CYS III C   1 ? 34 
ATOM   11384 O O   . CYS I  1 151 ? 13.621  -40.596  44.249  1.000 106.653 0 480 CYS III O   1 ? 34 
ATOM   11385 C CB  . CYS I  1 151 ? 15.763  -42.462  43.097  1.000 107.246 0 480 CYS III CB  1 ? 34 
ATOM   11386 S SG  . CYS I  1 151 ? 16.091  -43.465  41.615  1.000 110.325 0 480 CYS III SG  1 ? 34 
ATOM   11387 N N   . ASN I  1 152 ? 15.563  -39.462  44.696  1.000 107.152 0 481 ASN III N   1 ? 34 
ATOM   11388 C CA  . ASN I  1 152 ? 15.068  -38.677  45.865  1.000 105.062 0 481 ASN III CA  1 ? 34 
ATOM   11389 C C   . ASN I  1 152 ? 14.368  -39.614  46.868  1.000 99.236  0 481 ASN III C   1 ? 34 
ATOM   11390 O O   . ASN I  1 152 ? 13.371  -39.186  47.475  1.000 97.969  0 481 ASN III O   1 ? 34 
ATOM   11391 C CB  . ASN I  1 152 ? 14.119  -37.545  45.466  1.000 109.832 0 481 ASN III CB  1 ? 34 
ATOM   11392 C CG  . ASN I  1 152 ? 14.680  -36.592  44.434  1.000 112.803 0 481 ASN III CG  1 ? 34 
ATOM   11393 O OD1 . ASN I  1 152 ? 15.706  -36.848  43.805  1.000 112.371 0 481 ASN III OD1 1 ? 34 
ATOM   11394 N ND2 . ASN I  1 152 ? 13.986  -35.489  44.250  1.000 115.826 0 481 ASN III ND2 1 ? 34 
ATOM   11395 N N   . GLY I  1 153 ? 14.874  -40.844  47.035  1.000 94.318  0 482 GLY III N   1 ? 34 
ATOM   11396 C CA  . GLY I  1 153 ? 14.369  -41.849  47.992  1.000 91.488  0 482 GLY III CA  1 ? 34 
ATOM   11397 C C   . GLY I  1 153 ? 12.906  -42.222  47.770  1.000 91.965  0 482 GLY III C   1 ? 34 
ATOM   11398 O O   . GLY I  1 153 ? 12.246  -42.607  48.759  1.000 91.486  0 482 GLY III O   1 ? 34 
ATOM   11399 N N   . VAL I  1 154 ? 12.404  -42.111  46.535  1.000 93.143  0 483 VAL III N   1 ? 34 
ATOM   11400 C CA  . VAL I  1 154 ? 11.014  -42.493  46.142  1.000 91.713  0 483 VAL III CA  1 ? 34 
ATOM   11401 C C   . VAL I  1 154 ? 11.104  -43.477  44.968  1.000 89.501  0 483 VAL III C   1 ? 34 
ATOM   11402 O O   . VAL I  1 154 ? 11.971  -43.299  44.104  1.000 87.360  0 483 VAL III O   1 ? 34 
ATOM   11403 C CB  . VAL I  1 154 ? 10.172  -41.259  45.780  1.000 94.864  0 483 VAL III CB  1 ? 34 
ATOM   11404 C CG1 . VAL I  1 154 ? 8.872   -41.652  45.109  1.000 95.759  0 483 VAL III CG1 1 ? 34 
ATOM   11405 C CG2 . VAL I  1 154 ? 9.880   -40.397  46.995  1.000 96.253  0 483 VAL III CG2 1 ? 34 
ATOM   11406 N N   . GLU I  1 155 ? 10.227  -44.479  44.958  1.000 88.217  0 484 GLU III N   1 ? 34 
ATOM   11407 C CA  . GLU I  1 155 ? 10.064  -45.483  43.891  1.000 87.060  0 484 GLU III CA  1 ? 34 
ATOM   11408 C C   . GLU I  1 155 ? 9.366   -44.867  42.672  1.000 90.632  0 484 GLU III C   1 ? 34 
ATOM   11409 O O   . GLU I  1 155 ? 8.584   -43.937  42.842  1.000 93.201  0 484 GLU III O   1 ? 34 
ATOM   11410 C CB  . GLU I  1 155 ? 9.251   -46.639  44.467  1.000 85.939  0 484 GLU III CB  1 ? 34 
ATOM   11411 C CG  . GLU I  1 155 ? 9.320   -47.929  43.690  1.000 85.952  0 484 GLU III CG  1 ? 34 
ATOM   11412 C CD  . GLU I  1 155 ? 9.195   -49.179  44.550  1.000 83.601  0 484 GLU III CD  1 ? 34 
ATOM   11413 O OE1 . GLU I  1 155 ? 8.673   -49.069  45.675  1.000 83.802  0 484 GLU III OE1 1 ? 34 
ATOM   11414 O OE2 . GLU I  1 155 ? 9.643   -50.252  44.100  1.000 82.460  0 484 GLU III OE2 1 ? 34 
ATOM   11415 N N   . GLY I  1 156 ? 9.661   -45.389  41.482  1.000 90.781  0 485 GLY III N   1 ? 34 
ATOM   11416 C CA  . GLY I  1 156 ? 9.035   -44.993  40.204  1.000 94.224  0 485 GLY III CA  1 ? 34 
ATOM   11417 C C   . GLY I  1 156 ? 9.850   -45.489  39.014  1.000 94.446  0 485 GLY III C   1 ? 34 
ATOM   11418 O O   . GLY I  1 156 ? 10.677  -46.410  39.191  1.000 91.967  0 485 GLY III O   1 ? 34 
ATOM   11419 N N   . PHE I  1 157 ? 9.634   -44.902  37.839  1.000 98.703  0 486 PHE III N   1 ? 34 
ATOM   11420 C CA  . PHE I  1 157 ? 10.357  -45.214  36.579  1.000 99.996  0 486 PHE III CA  1 ? 34 
ATOM   11421 C C   . PHE I  1 157 ? 11.871  -45.121  36.847  1.000 99.441  0 486 PHE III C   1 ? 34 
ATOM   11422 O O   . PHE I  1 157 ? 12.336  -44.083  37.356  1.000 99.741  0 486 PHE III O   1 ? 34 
ATOM   11423 C CB  . PHE I  1 157 ? 9.854   -44.278  35.474  1.000 104.248 0 486 PHE III CB  1 ? 34 
ATOM   11424 C CG  . PHE I  1 157 ? 8.371   -44.344  35.164  1.000 107.052 0 486 PHE III CG  1 ? 34 
ATOM   11425 C CD1 . PHE I  1 157 ? 7.739   -45.565  34.959  1.000 105.820 0 486 PHE III CD1 1 ? 34 
ATOM   11426 C CD2 . PHE I  1 157 ? 7.611   -43.185  35.023  1.000 111.376 0 486 PHE III CD2 1 ? 34 
ATOM   11427 C CE1 . PHE I  1 157 ? 6.387   -45.622  34.642  1.000 108.379 0 486 PHE III CE1 1 ? 34 
ATOM   11428 C CE2 . PHE I  1 157 ? 6.260   -43.247  34.709  1.000 114.092 0 486 PHE III CE2 1 ? 34 
ATOM   11429 C CZ  . PHE I  1 157 ? 5.651   -44.466  34.520  1.000 112.557 0 486 PHE III CZ  1 ? 34 
ATOM   11430 N N   . ASN I  1 158 ? 12.609  -46.207  36.563  1.000 99.762  0 487 ASN III N   1 ? 34 
ATOM   11431 C CA  . ASN I  1 158 ? 14.096  -46.311  36.660  1.000 99.889  0 487 ASN III CA  1 ? 34 
ATOM   11432 C C   . ASN I  1 158 ? 14.561  -46.105  38.109  1.000 98.762  0 487 ASN III C   1 ? 34 
ATOM   11433 O O   . ASN I  1 158 ? 15.772  -45.905  38.351  1.000 97.250  0 487 ASN III O   1 ? 34 
ATOM   11434 C CB  . ASN I  1 158 ? 14.810  -45.330  35.728  1.000 103.956 0 487 ASN III CB  1 ? 34 
ATOM   11435 C CG  . ASN I  1 158 ? 14.594  -45.644  34.253  1.000 106.548 0 487 ASN III CG  1 ? 34 
ATOM   11436 O OD1 . ASN I  1 158 ? 14.630  -46.804  33.848  1.000 106.345 0 487 ASN III OD1 1 ? 34 
ATOM   11437 N ND2 . ASN I  1 158 ? 14.314  -44.629  33.444  1.000 110.097 0 487 ASN III ND2 1 ? 34 
ATOM   11438 N N   . CYS I  1 159 ? 13.634  -46.191  39.074  1.000 99.975  0 488 CYS III N   1 ? 35 
ATOM   11439 C CA  . CYS I  1 159 ? 13.883  -45.963  40.518  1.000 96.628  0 488 CYS III CA  1 ? 35 
ATOM   11440 C C   . CYS I  1 159 ? 13.257  -47.106  41.296  1.000 92.680  0 488 CYS III C   1 ? 35 
ATOM   11441 O O   . CYS I  1 159 ? 12.130  -46.943  41.761  1.000 91.805  0 488 CYS III O   1 ? 35 
ATOM   11442 C CB  . CYS I  1 159 ? 13.314  -44.612  40.930  1.000 99.070  0 488 CYS III CB  1 ? 35 
ATOM   11443 S SG  . CYS I  1 159 ? 14.392  -43.241  40.420  1.000 102.861 0 488 CYS III SG  1 ? 35 
ATOM   11444 N N   . TYR I  1 160 ? 13.984  -48.212  41.418  1.000 88.594  0 489 TYR III N   1 ? 35 
ATOM   11445 C CA  . TYR I  1 160 ? 13.450  -49.456  42.005  1.000 87.226  0 489 TYR III CA  1 ? 35 
ATOM   11446 C C   . TYR I  1 160 ? 13.890  -49.539  43.462  1.000 83.675  0 489 TYR III C   1 ? 35 
ATOM   11447 O O   . TYR I  1 160 ? 15.018  -49.177  43.820  1.000 84.295  0 489 TYR III O   1 ? 35 
ATOM   11448 C CB  . TYR I  1 160 ? 13.929  -50.643  41.186  1.000 87.702  0 489 TYR III CB  1 ? 35 
ATOM   11449 C CG  . TYR I  1 160 ? 13.480  -50.648  39.748  1.000 90.878  0 489 TYR III CG  1 ? 35 
ATOM   11450 C CD1 . TYR I  1 160 ? 14.005  -49.782  38.802  1.000 92.195  0 489 TYR III CD1 1 ? 35 
ATOM   11451 C CD2 . TYR I  1 160 ? 12.712  -51.717  39.279  1.000 91.717  0 489 TYR III CD2 1 ? 35 
ATOM   11452 C CE1 . TYR I  1 160 ? 13.615  -49.847  37.474  1.000 94.227  0 489 TYR III CE1 1 ? 35 
ATOM   11453 C CE2 . TYR I  1 160 ? 12.290  -51.780  37.965  1.000 93.933  0 489 TYR III CE2 1 ? 35 
ATOM   11454 C CZ  . TYR I  1 160 ? 12.753  -50.844  37.058  1.000 95.433  0 489 TYR III CZ  1 ? 35 
ATOM   11455 O OH  . TYR I  1 160 ? 12.385  -50.911  35.750  1.000 96.629  0 489 TYR III OH  1 ? 35 
ATOM   11456 N N   . PHE I  1 161 ? 12.956  -49.943  44.313  1.000 82.098  0 490 PHE III N   1 ? 35 
ATOM   11457 C CA  . PHE I  1 161 ? 13.256  -50.439  45.671  1.000 79.101  0 490 PHE III CA  1 ? 35 
ATOM   11458 C C   . PHE I  1 161 ? 14.084  -51.693  45.441  1.000 77.032  0 490 PHE III C   1 ? 35 
ATOM   11459 O O   . PHE I  1 161 ? 13.686  -52.521  44.615  1.000 76.868  0 490 PHE III O   1 ? 35 
ATOM   11460 C CB  . PHE I  1 161 ? 11.960  -50.670  46.437  1.000 79.562  0 490 PHE III CB  1 ? 35 
ATOM   11461 C CG  . PHE I  1 161 ? 12.159  -51.058  47.871  1.000 78.192  0 490 PHE III CG  1 ? 35 
ATOM   11462 C CD1 . PHE I  1 161 ? 12.507  -50.119  48.825  1.000 77.776  0 490 PHE III CD1 1 ? 35 
ATOM   11463 C CD2 . PHE I  1 161 ? 12.001  -52.371  48.258  1.000 77.673  0 490 PHE III CD2 1 ? 35 
ATOM   11464 C CE1 . PHE I  1 161 ? 12.711  -50.493  50.142  1.000 77.118  0 490 PHE III CE1 1 ? 35 
ATOM   11465 C CE2 . PHE I  1 161 ? 12.173  -52.748  49.575  1.000 77.313  0 490 PHE III CE2 1 ? 35 
ATOM   11466 C CZ  . PHE I  1 161 ? 12.537  -51.808  50.514  1.000 77.773  0 490 PHE III CZ  1 ? 35 
ATOM   11467 N N   . PRO I  1 162 ? 15.272  -51.829  46.075  1.000 74.085  0 491 PRO III N   1 ? 35 
ATOM   11468 C CA  . PRO I  1 162 ? 16.262  -52.813  45.643  1.000 72.207  0 491 PRO III CA  1 ? 35 
ATOM   11469 C C   . PRO I  1 162 ? 15.957  -54.259  46.073  1.000 69.968  0 491 PRO III C   1 ? 35 
ATOM   11470 O O   . PRO I  1 162 ? 16.569  -55.164  45.555  1.000 68.158  0 491 PRO III O   1 ? 35 
ATOM   11471 C CB  . PRO I  1 162 ? 17.546  -52.317  46.348  1.000 70.768  0 491 PRO III CB  1 ? 35 
ATOM   11472 C CG  . PRO I  1 162 ? 17.036  -51.684  47.649  1.000 70.630  0 491 PRO III CG  1 ? 35 
ATOM   11473 C CD  . PRO I  1 162 ? 15.748  -51.027  47.206  1.000 73.066  0 491 PRO III CD  1 ? 35 
ATOM   11474 N N   . LEU I  1 163 ? 14.985  -54.439  46.980  1.000 69.551  0 492 LEU III N   1 ? 35 
ATOM   11475 C CA  . LEU I  1 163 ? 14.525  -55.758  47.439  1.000 69.041  0 492 LEU III CA  1 ? 35 
ATOM   11476 C C   . LEU I  1 163 ? 13.268  -56.119  46.653  1.000 70.986  0 492 LEU III C   1 ? 35 
ATOM   11477 O O   . LEU I  1 163 ? 12.449  -55.261  46.383  1.000 70.620  0 492 LEU III O   1 ? 35 
ATOM   11478 C CB  . LEU I  1 163 ? 14.258  -55.761  48.944  1.000 67.835  0 492 LEU III CB  1 ? 35 
ATOM   11479 C CG  . LEU I  1 163 ? 15.411  -55.316  49.838  1.000 65.878  0 492 LEU III CG  1 ? 35 
ATOM   11480 C CD1 . LEU I  1 163 ? 15.045  -55.488  51.300  1.000 65.735  0 492 LEU III CD1 1 ? 35 
ATOM   11481 C CD2 . LEU I  1 163 ? 16.680  -56.069  49.480  1.000 65.138  0 492 LEU III CD2 1 ? 35 
ATOM   11482 N N   . GLN I  1 164 ? 13.182  -57.388  46.289  1.000 72.839  0 493 GLN III N   1 ? 35 
ATOM   11483 C CA  . GLN I  1 164 ? 12.038  -57.980  45.581  1.000 75.159  0 493 GLN III CA  1 ? 35 
ATOM   11484 C C   . GLN I  1 164 ? 11.567  -59.187  46.389  1.000 74.617  0 493 GLN III C   1 ? 35 
ATOM   11485 O O   . GLN I  1 164 ? 12.385  -59.839  47.083  1.000 73.176  0 493 GLN III O   1 ? 35 
ATOM   11486 C CB  . GLN I  1 164 ? 12.460  -58.301  44.149  1.000 77.735  0 493 GLN III CB  1 ? 35 
ATOM   11487 C CG  . GLN I  1 164 ? 11.348  -58.890  43.293  1.000 81.227  0 493 GLN III CG  1 ? 35 
ATOM   11488 C CD  . GLN I  1 164 ? 10.267  -57.859  43.058  1.000 84.201  0 493 GLN III CD  1 ? 35 
ATOM   11489 O OE1 . GLN I  1 164 ? 10.549  -56.711  42.710  1.000 85.788  0 493 GLN III OE1 1 ? 35 
ATOM   11490 N NE2 . GLN I  1 164 ? 9.021   -58.254  43.264  1.000 86.005  0 493 GLN III NE2 1 ? 35 
ATOM   11491 N N   . SER I  1 165 ? 10.265  -59.422  46.338  1.000 76.992  0 494 SER III N   1 ? 35 
ATOM   11492 C CA  . SER I  1 165 ? 9.598   -60.516  47.075  1.000 77.185  0 494 SER III CA  1 ? 35 
ATOM   11493 C C   . SER I  1 165 ? 9.626   -61.771  46.196  1.000 76.891  0 494 SER III C   1 ? 35 
ATOM   11494 O O   . SER I  1 165 ? 9.550   -61.630  44.968  1.000 77.650  0 494 SER III O   1 ? 35 
ATOM   11495 C CB  . SER I  1 165 ? 8.224   -60.092  47.445  1.000 79.203  0 494 SER III CB  1 ? 35 
ATOM   11496 O OG  . SER I  1 165 ? 7.584   -61.138  48.129  1.000 81.275  0 494 SER III OG  1 ? 35 
ATOM   11497 N N   . TYR I  1 166 ? 9.772   -62.957  46.788  1.000 76.087  0 495 TYR III N   1 ? 35 
ATOM   11498 C CA  . TYR I  1 166 ? 9.762   -64.237  46.042  1.000 75.966  0 495 TYR III CA  1 ? 35 
ATOM   11499 C C   . TYR I  1 166 ? 8.332   -64.597  45.649  1.000 79.768  0 495 TYR III C   1 ? 35 
ATOM   11500 O O   . TYR I  1 166 ? 8.130   -65.154  44.557  1.000 81.778  0 495 TYR III O   1 ? 35 
ATOM   11501 C CB  . TYR I  1 166 ? 10.402  -65.355  46.853  1.000 73.885  0 495 TYR III CB  1 ? 35 
ATOM   11502 C CG  . TYR I  1 166 ? 11.899  -65.465  46.717  1.000 71.579  0 495 TYR III CG  1 ? 35 
ATOM   11503 C CD1 . TYR I  1 166 ? 12.481  -65.889  45.538  1.000 70.732  0 495 TYR III CD1 1 ? 35 
ATOM   11504 C CD2 . TYR I  1 166 ? 12.735  -65.142  47.773  1.000 69.171  0 495 TYR III CD2 1 ? 35 
ATOM   11505 C CE1 . TYR I  1 166 ? 13.857  -66.009  45.416  1.000 69.648  0 495 TYR III CE1 1 ? 35 
ATOM   11506 C CE2 . TYR I  1 166 ? 14.104  -65.267  47.675  1.000 67.210  0 495 TYR III CE2 1 ? 35 
ATOM   11507 C CZ  . TYR I  1 166 ? 14.669  -65.716  46.495  1.000 68.099  0 495 TYR III CZ  1 ? 35 
ATOM   11508 O OH  . TYR I  1 166 ? 16.030  -65.816  46.385  1.000 66.913  0 495 TYR III OH  1 ? 35 
ATOM   11509 N N   . GLY I  1 167 ? 7.344   -64.329  46.505  1.000 82.173  0 496 GLY III N   1 ? 35 
ATOM   11510 C CA  . GLY I  1 167 ? 5.951   -64.712  46.187  1.000 86.269  0 496 GLY III CA  1 ? 35 
ATOM   11511 C C   . GLY I  1 167 ? 5.869   -66.207  45.903  1.000 87.633  0 496 GLY III C   1 ? 35 
ATOM   11512 O O   . GLY I  1 167 ? 5.715   -66.594  44.717  1.000 89.853  0 496 GLY III O   1 ? 35 
ATOM   11513 N N   . PHE I  1 168 ? 6.023   -67.033  46.943  1.000 87.191  0 497 PHE III N   1 ? 35 
ATOM   11514 C CA  . PHE I  1 168 ? 6.066   -68.509  46.843  1.000 87.026  0 497 PHE III CA  1 ? 35 
ATOM   11515 C C   . PHE I  1 168 ? 4.639   -69.058  46.888  1.000 88.305  0 497 PHE III C   1 ? 35 
ATOM   11516 O O   . PHE I  1 168 ? 3.953   -68.850  47.904  1.000 87.566  0 497 PHE III O   1 ? 35 
ATOM   11517 C CB  . PHE I  1 168 ? 6.875   -69.095  47.997  1.000 86.022  0 497 PHE III CB  1 ? 35 
ATOM   11518 C CG  . PHE I  1 168 ? 8.364   -68.875  47.917  1.000 85.063  0 497 PHE III CG  1 ? 35 
ATOM   11519 C CD1 . PHE I  1 168 ? 9.091   -69.385  46.852  1.000 83.959  0 497 PHE III CD1 1 ? 35 
ATOM   11520 C CD2 . PHE I  1 168 ? 9.042   -68.199  48.929  1.000 83.907  0 497 PHE III CD2 1 ? 35 
ATOM   11521 C CE1 . PHE I  1 168 ? 10.462  -69.211  46.785  1.000 82.272  0 497 PHE III CE1 1 ? 35 
ATOM   11522 C CE2 . PHE I  1 168 ? 10.414  -68.032  48.867  1.000 81.034  0 497 PHE III CE2 1 ? 35 
ATOM   11523 C CZ  . PHE I  1 168 ? 11.121  -68.533  47.793  1.000 81.847  0 497 PHE III CZ  1 ? 35 
ATOM   11524 N N   . GLN I  1 169 ? 4.220   -69.763  45.838  1.000 88.289  0 498 GLN III N   1 ? 35 
ATOM   11525 C CA  . GLN I  1 169 ? 2.899   -70.433  45.790  1.000 90.206  0 498 GLN III CA  1 ? 35 
ATOM   11526 C C   . GLN I  1 169 ? 3.110   -71.934  45.757  1.000 89.126  0 498 GLN III C   1 ? 35 
ATOM   11527 O O   . GLN I  1 169 ? 4.030   -72.416  45.099  1.000 88.040  0 498 GLN III O   1 ? 35 
ATOM   11528 C CB  . GLN I  1 169 ? 2.114   -69.940  44.590  1.000 92.003  0 498 GLN III CB  1 ? 35 
ATOM   11529 C CG  . GLN I  1 169 ? 1.860   -68.456  44.723  1.000 92.408  0 498 GLN III CG  1 ? 35 
ATOM   11530 C CD  . GLN I  1 169 ? 1.042   -67.942  43.571  1.000 94.738  0 498 GLN III CD  1 ? 35 
ATOM   11531 O OE1 . GLN I  1 169 ? 1.553   -67.769  42.470  1.000 95.301  0 498 GLN III OE1 1 ? 35 
ATOM   11532 N NE2 . GLN I  1 169 ? -0.233  -67.675  43.825  1.000 97.295  0 498 GLN III NE2 1 ? 35 
ATOM   11533 N N   . PRO I  1 170 ? 2.251   -72.700  46.468  1.000 89.363  0 499 PRO III N   1 ? 35 
ATOM   11534 C CA  . PRO I  1 170 ? 2.420   -74.146  46.566  1.000 88.704  0 499 PRO III CA  1 ? 35 
ATOM   11535 C C   . PRO I  1 170 ? 2.413   -74.823  45.183  1.000 89.114  0 499 PRO III C   1 ? 35 
ATOM   11536 O O   . PRO I  1 170 ? 3.026   -75.864  45.065  1.000 87.808  0 499 PRO III O   1 ? 35 
ATOM   11537 C CB  . PRO I  1 170 ? 1.248   -74.608  47.451  1.000 90.388  0 499 PRO III CB  1 ? 35 
ATOM   11538 C CG  . PRO I  1 170 ? 0.254   -73.452  47.458  1.000 92.517  0 499 PRO III CG  1 ? 35 
ATOM   11539 C CD  . PRO I  1 170 ? 1.066   -72.209  47.186  1.000 90.924  0 499 PRO III CD  1 ? 35 
ATOM   11540 N N   . THR I  1 171 ? 1.781   -74.201  44.182  1.000 90.631  0 500 THR III N   1 ? 35 
ATOM   11541 C CA  . THR I  1 171 ? 1.643   -74.723  42.794  1.000 92.377  0 500 THR III CA  1 ? 35 
ATOM   11542 C C   . THR I  1 171 ? 2.858   -74.383  41.906  1.000 90.529  0 500 THR III C   1 ? 35 
ATOM   11543 O O   . THR I  1 171 ? 2.922   -74.948  40.800  1.000 91.496  0 500 THR III O   1 ? 35 
ATOM   11544 C CB  . THR I  1 171 ? 0.348   -74.196  42.167  1.000 95.390  0 500 THR III CB  1 ? 35 
ATOM   11545 O OG1 . THR I  1 171 ? 0.383   -72.775  42.263  1.000 95.204  0 500 THR III OG1 1 ? 35 
ATOM   11546 C CG2 . THR I  1 171 ? -0.896  -74.693  42.868  1.000 97.565  0 500 THR III CG2 1 ? 35 
ATOM   11547 N N   . ASN I  1 172 ? 3.787   -73.525  42.346  1.000 87.489  0 501 ASN III N   1 ? 35 
ATOM   11548 C CA  . ASN I  1 172 ? 5.029   -73.207  41.594  1.000 85.886  0 501 ASN III CA  1 ? 35 
ATOM   11549 C C   . ASN I  1 172 ? 5.731   -74.498  41.156  1.000 84.806  0 501 ASN III C   1 ? 35 
ATOM   11550 O O   . ASN I  1 172 ? 5.687   -75.470  41.919  1.000 83.022  0 501 ASN III O   1 ? 35 
ATOM   11551 C CB  . ASN I  1 172 ? 6.018   -72.402  42.442  1.000 83.480  0 501 ASN III CB  1 ? 35 
ATOM   11552 C CG  . ASN I  1 172 ? 5.568   -70.979  42.682  1.000 84.596  0 501 ASN III CG  1 ? 35 
ATOM   11553 O OD1 . ASN I  1 172 ? 4.528   -70.572  42.169  1.000 86.320  0 501 ASN III OD1 1 ? 35 
ATOM   11554 N ND2 . ASN I  1 172 ? 6.336   -70.223  43.459  1.000 83.381  0 501 ASN III ND2 1 ? 35 
ATOM   11555 N N   . GLY I  1 173 ? 6.391   -74.495  39.994  1.000 84.985  0 502 GLY III N   1 ? 35 
ATOM   11556 C CA  . GLY I  1 173 ? 7.371   -75.533  39.623  1.000 84.568  0 502 GLY III CA  1 ? 35 
ATOM   11557 C C   . GLY I  1 173 ? 8.481   -75.629  40.669  1.000 83.592  0 502 GLY III C   1 ? 35 
ATOM   11558 O O   . GLY I  1 173 ? 8.708   -74.634  41.400  1.000 81.999  0 502 GLY III O   1 ? 35 
ATOM   11559 N N   . VAL I  1 174 ? 9.159   -76.779  40.753  1.000 83.684  0 503 VAL III N   1 ? 35 
ATOM   11560 C CA  . VAL I  1 174 ? 10.120  -77.092  41.858  1.000 82.666  0 503 VAL III CA  1 ? 35 
ATOM   11561 C C   . VAL I  1 174 ? 11.225  -76.021  41.916  1.000 81.978  0 503 VAL III C   1 ? 35 
ATOM   11562 O O   . VAL I  1 174 ? 11.603  -75.625  43.045  1.000 81.579  0 503 VAL III O   1 ? 35 
ATOM   11563 C CB  . VAL I  1 174 ? 10.725  -78.504  41.734  1.000 81.240  0 503 VAL III CB  1 ? 35 
ATOM   11564 C CG1 . VAL I  1 174 ? 11.690  -78.646  40.562  1.000 80.639  0 503 VAL III CG1 1 ? 35 
ATOM   11565 C CG2 . VAL I  1 174 ? 11.411  -78.890  43.031  1.000 79.394  0 503 VAL III CG2 1 ? 35 
ATOM   11566 N N   . GLY I  1 175 ? 11.720  -75.576  40.755  1.000 81.856  0 504 GLY III N   1 ? 35 
ATOM   11567 C CA  . GLY I  1 175 ? 12.751  -74.531  40.619  1.000 79.267  0 504 GLY III CA  1 ? 35 
ATOM   11568 C C   . GLY I  1 175 ? 12.325  -73.225  41.262  1.000 79.793  0 504 GLY III C   1 ? 35 
ATOM   11569 O O   . GLY I  1 175 ? 13.218  -72.487  41.682  1.000 78.803  0 504 GLY III O   1 ? 35 
ATOM   11570 N N   . TYR I  1 176 ? 11.015  -72.949  41.362  1.000 81.587  0 505 TYR III N   1 ? 35 
ATOM   11571 C CA  . TYR I  1 176 ? 10.479  -71.688  41.943  1.000 81.765  0 505 TYR III CA  1 ? 35 
ATOM   11572 C C   . TYR I  1 176 ? 9.895   -71.938  43.343  1.000 79.974  0 505 TYR III C   1 ? 35 
ATOM   11573 O O   . TYR I  1 176 ? 9.289   -71.022  43.921  1.000 79.688  0 505 TYR III O   1 ? 35 
ATOM   11574 C CB  . TYR I  1 176 ? 9.465   -71.070  40.983  1.000 85.594  0 505 TYR III CB  1 ? 35 
ATOM   11575 C CG  . TYR I  1 176 ? 10.065  -70.539  39.704  1.000 89.341  0 505 TYR III CG  1 ? 35 
ATOM   11576 C CD1 . TYR I  1 176 ? 10.301  -71.376  38.616  1.000 92.541  0 505 TYR III CD1 1 ? 35 
ATOM   11577 C CD2 . TYR I  1 176 ? 10.368  -69.190  39.557  1.000 90.620  0 505 TYR III CD2 1 ? 35 
ATOM   11578 C CE1 . TYR I  1 176 ? 10.825  -70.890  37.425  1.000 93.277  0 505 TYR III CE1 1 ? 35 
ATOM   11579 C CE2 . TYR I  1 176 ? 10.878  -68.686  38.368  1.000 91.943  0 505 TYR III CE2 1 ? 35 
ATOM   11580 C CZ  . TYR I  1 176 ? 11.117  -69.541  37.303  1.000 93.402  0 505 TYR III CZ  1 ? 35 
ATOM   11581 O OH  . TYR I  1 176 ? 11.636  -69.053  36.137  1.000 94.736  0 505 TYR III OH  1 ? 35 
ATOM   11582 N N   . GLN I  1 177 ? 10.071  -73.130  43.905  1.000 78.357  0 506 GLN III N   1 ? 35 
ATOM   11583 C CA  . GLN I  1 177 ? 9.624   -73.417  45.295  1.000 78.173  0 506 GLN III CA  1 ? 35 
ATOM   11584 C C   . GLN I  1 177 ? 10.683  -72.945  46.282  1.000 76.615  0 506 GLN III C   1 ? 35 
ATOM   11585 O O   . GLN I  1 177 ? 11.858  -72.876  45.966  1.000 76.620  0 506 GLN III O   1 ? 35 
ATOM   11586 C CB  . GLN I  1 177 ? 9.345   -74.902  45.499  1.000 79.067  0 506 GLN III CB  1 ? 35 
ATOM   11587 C CG  . GLN I  1 177 ? 8.020   -75.303  44.901  1.000 82.121  0 506 GLN III CG  1 ? 35 
ATOM   11588 C CD  . GLN I  1 177 ? 7.803   -76.792  44.946  1.000 82.129  0 506 GLN III CD  1 ? 35 
ATOM   11589 O OE1 . GLN I  1 177 ? 8.315   -77.516  45.800  1.000 79.598  0 506 GLN III OE1 1 ? 35 
ATOM   11590 N NE2 . GLN I  1 177 ? 7.008   -77.253  44.009  1.000 83.942  0 506 GLN III NE2 1 ? 35 
ATOM   11591 N N   . PRO I  1 178 ? 10.299  -72.616  47.526  1.000 75.742  0 507 PRO III N   1 ? 35 
ATOM   11592 C CA  . PRO I  1 178 ? 11.269  -72.174  48.515  1.000 72.679  0 507 PRO III CA  1 ? 35 
ATOM   11593 C C   . PRO I  1 178 ? 12.127  -73.358  48.974  1.000 69.847  0 507 PRO III C   1 ? 35 
ATOM   11594 O O   . PRO I  1 178 ? 11.627  -74.458  49.103  1.000 70.574  0 507 PRO III O   1 ? 35 
ATOM   11595 C CB  . PRO I  1 178 ? 10.395  -71.621  49.649  1.000 74.122  0 507 PRO III CB  1 ? 35 
ATOM   11596 C CG  . PRO I  1 178 ? 9.135   -72.430  49.551  1.000 76.404  0 507 PRO III CG  1 ? 35 
ATOM   11597 C CD  . PRO I  1 178 ? 8.934   -72.679  48.065  1.000 77.750  0 507 PRO III CD  1 ? 35 
ATOM   11598 N N   . TYR I  1 179 ? 13.408  -73.092  49.176  1.000 66.880  0 508 TYR III N   1 ? 35 
ATOM   11599 C CA  . TYR I  1 179 ? 14.377  -74.023  49.796  1.000 65.004  0 508 TYR III CA  1 ? 35 
ATOM   11600 C C   . TYR I  1 179 ? 15.017  -73.295  50.969  1.000 64.586  0 508 TYR III C   1 ? 35 
ATOM   11601 O O   . TYR I  1 179 ? 15.386  -72.122  50.836  1.000 63.298  0 508 TYR III O   1 ? 35 
ATOM   11602 C CB  . TYR I  1 179 ? 15.417  -74.497  48.788  1.000 63.881  0 508 TYR III CB  1 ? 35 
ATOM   11603 C CG  . TYR I  1 179 ? 14.936  -75.619  47.909  1.000 65.347  0 508 TYR III CG  1 ? 35 
ATOM   11604 C CD1 . TYR I  1 179 ? 13.923  -75.410  46.980  1.000 67.149  0 508 TYR III CD1 1 ? 35 
ATOM   11605 C CD2 . TYR I  1 179 ? 15.478  -76.894  48.016  1.000 64.563  0 508 TYR III CD2 1 ? 35 
ATOM   11606 C CE1 . TYR I  1 179 ? 13.464  -76.440  46.176  1.000 68.950  0 508 TYR III CE1 1 ? 35 
ATOM   11607 C CE2 . TYR I  1 179 ? 15.025  -77.932  47.221  1.000 65.974  0 508 TYR III CE2 1 ? 35 
ATOM   11608 C CZ  . TYR I  1 179 ? 14.014  -77.705  46.300  1.000 68.317  0 508 TYR III CZ  1 ? 35 
ATOM   11609 O OH  . TYR I  1 179 ? 13.550  -78.705  45.498  1.000 71.050  0 508 TYR III OH  1 ? 35 
ATOM   11610 N N   . ARG I  1 180 ? 15.069  -73.977  52.110  1.000 65.420  0 509 ARG III N   1 ? 35 
ATOM   11611 C CA  . ARG I  1 180 ? 15.853  -73.543  53.282  1.000 64.220  0 509 ARG III CA  1 ? 35 
ATOM   11612 C C   . ARG I  1 180 ? 17.286  -74.006  53.086  1.000 62.974  0 509 ARG III C   1 ? 35 
ATOM   11613 O O   . ARG I  1 180 ? 17.492  -75.120  52.565  1.000 65.795  0 509 ARG III O   1 ? 35 
ATOM   11614 C CB  . ARG I  1 180 ? 15.229  -74.076  54.565  1.000 65.676  0 509 ARG III CB  1 ? 35 
ATOM   11615 C CG  . ARG I  1 180 ? 13.929  -73.351  54.875  1.000 66.968  0 509 ARG III CG  1 ? 35 
ATOM   11616 C CD  . ARG I  1 180 ? 13.282  -73.860  56.134  1.000 67.913  0 509 ARG III CD  1 ? 35 
ATOM   11617 N NE  . ARG I  1 180 ? 12.075  -73.085  56.323  1.000 69.642  0 509 ARG III NE  1 ? 35 
ATOM   11618 C CZ  . ARG I  1 180 ? 11.399  -73.017  57.461  1.000 69.491  0 509 ARG III CZ  1 ? 35 
ATOM   11619 N NH1 . ARG I  1 180 ? 11.793  -73.696  58.530  1.000 67.587  0 509 ARG III NH1 1 ? 35 
ATOM   11620 N NH2 . ARG I  1 180 ? 10.304  -72.283  57.509  1.000 71.553  0 509 ARG III NH2 1 ? 35 
ATOM   11621 N N   . VAL I  1 181 ? 18.228  -73.147  53.457  1.000 60.588  0 510 VAL III N   1 ? 35 
ATOM   11622 C CA  . VAL I  1 181 ? 19.686  -73.381  53.292  1.000 58.826  0 510 VAL III CA  1 ? 35 
ATOM   11623 C C   . VAL I  1 181 ? 20.369  -73.164  54.643  1.000 57.929  0 510 VAL III C   1 ? 35 
ATOM   11624 O O   . VAL I  1 181 ? 20.004  -72.202  55.361  1.000 58.382  0 510 VAL III O   1 ? 35 
ATOM   11625 C CB  . VAL I  1 181 ? 20.248  -72.448  52.208  1.000 58.791  0 510 VAL III CB  1 ? 35 
ATOM   11626 C CG1 . VAL I  1 181 ? 21.700  -72.745  51.924  1.000 57.951  0 510 VAL III CG1 1 ? 35 
ATOM   11627 C CG2 . VAL I  1 181 ? 19.436  -72.528  50.933  1.000 59.347  0 510 VAL III CG2 1 ? 35 
ATOM   11628 N N   . VAL I  1 182 ? 21.292  -74.061  54.986  1.000 56.099  0 511 VAL III N   1 ? 35 
ATOM   11629 C CA  . VAL I  1 182 ? 22.254  -73.876  56.102  1.000 54.279  0 511 VAL III CA  1 ? 35 
ATOM   11630 C C   . VAL I  1 182 ? 23.648  -74.030  55.520  1.000 52.850  0 511 VAL III C   1 ? 35 
ATOM   11631 O O   . VAL I  1 182 ? 23.897  -75.015  54.800  1.000 51.639  0 511 VAL III O   1 ? 35 
ATOM   11632 C CB  . VAL I  1 182 ? 22.003  -74.863  57.252  1.000 54.908  0 511 VAL III CB  1 ? 35 
ATOM   11633 C CG1 . VAL I  1 182 ? 23.108  -74.770  58.295  1.000 53.801  0 511 VAL III CG1 1 ? 35 
ATOM   11634 C CG2 . VAL I  1 182 ? 20.615  -74.667  57.862  1.000 55.123  0 511 VAL III CG2 1 ? 35 
ATOM   11635 N N   . VAL I  1 183 ? 24.478  -73.024  55.768  1.000 53.637  0 512 VAL III N   1 ? 35 
ATOM   11636 C CA  . VAL I  1 183 ? 25.925  -73.001  55.416  1.000 52.333  0 512 VAL III CA  1 ? 35 
ATOM   11637 C C   . VAL I  1 183 ? 26.697  -73.090  56.731  1.000 52.906  0 512 VAL III C   1 ? 35 
ATOM   11638 O O   . VAL I  1 183 ? 26.508  -72.220  57.600  1.000 55.687  0 512 VAL III O   1 ? 35 
ATOM   11639 C CB  . VAL I  1 183 ? 26.298  -71.730  54.636  1.000 51.867  0 512 VAL III CB  1 ? 35 
ATOM   11640 C CG1 . VAL I  1 183 ? 27.750  -71.761  54.209  1.000 52.104  0 512 VAL III CG1 1 ? 35 
ATOM   11641 C CG2 . VAL I  1 183 ? 25.372  -71.511  53.450  1.000 52.694  0 512 VAL III CG2 1 ? 35 
ATOM   11642 N N   . LEU I  1 184 ? 27.476  -74.147  56.894  1.000 53.106  0 513 LEU III N   1 ? 35 
ATOM   11643 C CA  . LEU I  1 184 ? 28.391  -74.317  58.046  1.000 54.729  0 513 LEU III CA  1 ? 35 
ATOM   11644 C C   . LEU I  1 184 ? 29.783  -73.888  57.580  1.000 53.782  0 513 LEU III C   1 ? 35 
ATOM   11645 O O   . LEU I  1 184 ? 30.305  -74.513  56.651  1.000 51.643  0 513 LEU III O   1 ? 35 
ATOM   11646 C CB  . LEU I  1 184 ? 28.346  -75.774  58.514  1.000 56.050  0 513 LEU III CB  1 ? 35 
ATOM   11647 C CG  . LEU I  1 184 ? 26.965  -76.282  58.936  1.000 56.299  0 513 LEU III CG  1 ? 35 
ATOM   11648 C CD1 . LEU I  1 184 ? 26.993  -77.777  59.159  1.000 57.582  0 513 LEU III CD1 1 ? 35 
ATOM   11649 C CD2 . LEU I  1 184 ? 26.476  -75.559  60.177  1.000 56.355  0 513 LEU III CD2 1 ? 35 
ATOM   11650 N N   . SER I  1 185 ? 30.284  -72.790  58.146  1.000 53.986  0 514 SER III N   1 ? 35 
ATOM   11651 C CA  . SER I  1 185 ? 31.655  -72.250  57.948  1.000 52.887  0 514 SER III CA  1 ? 35 
ATOM   11652 C C   . SER I  1 185 ? 32.561  -72.822  59.020  1.000 51.827  0 514 SER III C   1 ? 35 
ATOM   11653 O O   . SER I  1 185 ? 32.195  -72.710  60.202  1.000 52.062  0 514 SER III O   1 ? 35 
ATOM   11654 C CB  . SER I  1 185 ? 31.664  -70.766  58.046  1.000 52.833  0 514 SER III CB  1 ? 35 
ATOM   11655 O OG  . SER I  1 185 ? 31.222  -70.240  56.828  1.000 55.359  0 514 SER III OG  1 ? 35 
ATOM   11656 N N   . PHE I  1 186 ? 33.679  -73.413  58.620  1.000 51.595  0 515 PHE III N   1 ? 35 
ATOM   11657 C CA  . PHE I  1 186 ? 34.672  -73.991  59.547  1.000 53.340  0 515 PHE III CA  1 ? 35 
ATOM   11658 C C   . PHE I  1 186 ? 35.892  -73.078  59.478  1.000 52.187  0 515 PHE III C   1 ? 35 
ATOM   11659 O O   . PHE I  1 186 ? 36.420  -72.837  58.414  1.000 51.604  0 515 PHE III O   1 ? 35 
ATOM   11660 C CB  . PHE I  1 186 ? 35.011  -75.432  59.165  1.000 53.722  0 515 PHE III CB  1 ? 35 
ATOM   11661 C CG  . PHE I  1 186 ? 33.845  -76.383  59.093  1.000 53.855  0 515 PHE III CG  1 ? 35 
ATOM   11662 C CD1 . PHE I  1 186 ? 32.740  -76.249  59.918  1.000 54.366  0 515 PHE III CD1 1 ? 35 
ATOM   11663 C CD2 . PHE I  1 186 ? 33.875  -77.430  58.186  1.000 52.850  0 515 PHE III CD2 1 ? 35 
ATOM   11664 C CE1 . PHE I  1 186 ? 31.716  -77.194  59.866  1.000 54.304  0 515 PHE III CE1 1 ? 35 
ATOM   11665 C CE2 . PHE I  1 186 ? 32.835  -78.335  58.103  1.000 53.708  0 515 PHE III CE2 1 ? 35 
ATOM   11666 C CZ  . PHE I  1 186 ? 31.758  -78.218  58.945  1.000 53.428  0 515 PHE III CZ  1 ? 35 
ATOM   11667 N N   . GLU I  1 187 ? 36.304  -72.585  60.633  1.000 53.468  0 516 GLU III N   1 ? 35 
ATOM   11668 C CA  . GLU I  1 187 ? 37.570  -71.846  60.827  1.000 53.815  0 516 GLU III CA  1 ? 35 
ATOM   11669 C C   . GLU I  1 187 ? 38.619  -72.782  61.427  1.000 50.245  0 516 GLU III C   1 ? 35 
ATOM   11670 O O   . GLU I  1 187 ? 38.300  -73.516  62.385  1.000 49.545  0 516 GLU III O   1 ? 35 
ATOM   11671 C CB  . GLU I  1 187 ? 37.329  -70.641  61.731  1.000 58.208  0 516 GLU III CB  1 ? 35 
ATOM   11672 C CG  . GLU I  1 187 ? 37.013  -69.372  60.974  1.000 59.866  0 516 GLU III CG  1 ? 35 
ATOM   11673 C CD  . GLU I  1 187 ? 36.640  -68.180  61.844  1.000 65.687  0 516 GLU III CD  1 ? 35 
ATOM   11674 O OE1 . GLU I  1 187 ? 36.938  -68.139  63.075  1.000 67.679  0 516 GLU III OE1 1 ? 35 
ATOM   11675 O OE2 . GLU I  1 187 ? 36.053  -67.268  61.271  1.000 74.512  0 516 GLU III OE2 1 ? 35 
ATOM   11676 N N   . LEU I  1 188 ? 39.835  -72.725  60.892  1.000 48.440  0 517 LEU III N   1 ? 35 
ATOM   11677 C CA  . LEU I  1 188 ? 41.017  -73.401  61.464  1.000 49.230  0 517 LEU III CA  1 ? 35 
ATOM   11678 C C   . LEU I  1 188 ? 42.136  -72.392  61.766  1.000 48.977  0 517 LEU III C   1 ? 35 
ATOM   11679 O O   . LEU I  1 188 ? 43.202  -72.419  61.083  1.000 50.180  0 517 LEU III O   1 ? 35 
ATOM   11680 C CB  . LEU I  1 188 ? 41.456  -74.460  60.454  1.000 48.715  0 517 LEU III CB  1 ? 35 
ATOM   11681 C CG  . LEU I  1 188 ? 40.647  -75.757  60.483  1.000 49.748  0 517 LEU III CG  1 ? 35 
ATOM   11682 C CD1 . LEU I  1 188 ? 40.944  -76.616  59.263  1.000 49.864  0 517 LEU III CD1 1 ? 35 
ATOM   11683 C CD2 . LEU I  1 188 ? 40.895  -76.522  61.783  1.000 50.827  0 517 LEU III CD2 1 ? 35 
ATOM   11684 N N   . LEU I  1 189 ? 41.991  -71.585  62.813  1.000 47.968  0 518 LEU III N   1 ? 35 
ATOM   11685 C CA  . LEU I  1 189 ? 42.946  -70.495  63.127  1.000 47.873  0 518 LEU III CA  1 ? 35 
ATOM   11686 C C   . LEU I  1 189 ? 43.976  -70.993  64.138  1.000 49.049  0 518 LEU III C   1 ? 35 
ATOM   11687 O O   . LEU I  1 189 ? 43.852  -72.134  64.585  1.000 49.638  0 518 LEU III O   1 ? 35 
ATOM   11688 C CB  . LEU I  1 189 ? 42.192  -69.291  63.680  1.000 47.473  0 518 LEU III CB  1 ? 35 
ATOM   11689 C CG  . LEU I  1 189 ? 41.016  -68.797  62.838  1.000 46.389  0 518 LEU III CG  1 ? 35 
ATOM   11690 C CD1 . LEU I  1 189 ? 40.382  -67.567  63.494  1.000 47.051  0 518 LEU III CD1 1 ? 35 
ATOM   11691 C CD2 . LEU I  1 189 ? 41.453  -68.471  61.427  1.000 44.923  0 518 LEU III CD2 1 ? 35 
ATOM   11692 N N   . HIS I  1 190 ? 44.979  -70.175  64.428  1.000 49.172  0 519 HIS III N   1 ? 35 
ATOM   11693 C CA  . HIS I  1 190 ? 45.981  -70.450  65.476  1.000 51.352  0 519 HIS III CA  1 ? 35 
ATOM   11694 C C   . HIS I  1 190 ? 45.401  -70.069  66.827  1.000 51.886  0 519 HIS III C   1 ? 35 
ATOM   11695 O O   . HIS I  1 190 ? 45.782  -69.023  67.326  1.000 52.048  0 519 HIS III O   1 ? 35 
ATOM   11696 C CB  . HIS I  1 190 ? 47.277  -69.769  65.071  1.000 51.606  0 519 HIS III CB  1 ? 35 
ATOM   11697 C CG  . HIS I  1 190 ? 47.671  -70.251  63.719  1.000 51.951  0 519 HIS III CG  1 ? 35 
ATOM   11698 N ND1 . HIS I  1 190 ? 47.669  -69.447  62.583  1.000 50.846  0 519 HIS III ND1 1 ? 35 
ATOM   11699 C CD2 . HIS I  1 190 ? 48.046  -71.474  63.297  1.000 52.272  0 519 HIS III CD2 1 ? 35 
ATOM   11700 C CE1 . HIS I  1 190 ? 48.107  -70.127  61.558  1.000 50.596  0 519 HIS III CE1 1 ? 35 
ATOM   11701 N NE2 . HIS I  1 190 ? 48.334  -71.370  61.961  1.000 52.164  0 519 HIS III NE2 1 ? 35 
ATOM   11702 N N   . ALA I  1 191 ? 44.493  -70.908  67.319  1.000 53.583  0 520 ALA III N   1 ? 35 
ATOM   11703 C CA  . ALA I  1 191 ? 43.706  -70.753  68.571  1.000 55.311  0 520 ALA III CA  1 ? 35 
ATOM   11704 C C   . ALA I  1 191 ? 43.279  -72.136  69.066  1.000 55.281  0 520 ALA III C   1 ? 35 
ATOM   11705 O O   . ALA I  1 191 ? 43.294  -73.090  68.314  1.000 54.999  0 520 ALA III O   1 ? 35 
ATOM   11706 C CB  . ALA I  1 191 ? 42.502  -69.867  68.299  1.000 53.951  0 520 ALA III CB  1 ? 35 
ATOM   11707 N N   . PRO I  1 192 ? 42.869  -72.316  70.331  1.000 57.522  0 521 PRO III N   1 ? 35 
ATOM   11708 C CA  . PRO I  1 192 ? 42.226  -73.558  70.756  1.000 57.359  0 521 PRO III CA  1 ? 35 
ATOM   11709 C C   . PRO I  1 192 ? 41.005  -73.899  69.895  1.000 56.169  0 521 PRO III C   1 ? 35 
ATOM   11710 O O   . PRO I  1 192 ? 40.260  -73.027  69.517  1.000 55.672  0 521 PRO III O   1 ? 35 
ATOM   11711 C CB  . PRO I  1 192 ? 41.831  -73.254  72.205  1.000 58.588  0 521 PRO III CB  1 ? 35 
ATOM   11712 C CG  . PRO I  1 192 ? 42.888  -72.283  72.665  1.000 59.354  0 521 PRO III CG  1 ? 35 
ATOM   11713 C CD  . PRO I  1 192 ? 43.073  -71.390  71.455  1.000 58.875  0 521 PRO III CD  1 ? 35 
ATOM   11714 N N   . ALA I  1 193 ? 40.853  -75.176  69.576  1.000 56.415  0 522 ALA III N   1 ? 35 
ATOM   11715 C CA  . ALA I  1 193 ? 39.630  -75.741  68.969  1.000 56.128  0 522 ALA III CA  1 ? 35 
ATOM   11716 C C   . ALA I  1 193 ? 38.495  -75.591  69.966  1.000 56.373  0 522 ALA III C   1 ? 35 
ATOM   11717 O O   . ALA I  1 193 ? 38.706  -75.827  71.119  1.000 55.882  0 522 ALA III O   1 ? 35 
ATOM   11718 C CB  . ALA I  1 193 ? 39.828  -77.188  68.592  1.000 57.249  0 522 ALA III CB  1 ? 35 
ATOM   11719 N N   . THR I  1 194 ? 37.320  -75.198  69.520  1.000 58.441  0 523 THR III N   1 ? 35 
ATOM   11720 C CA  . THR I  1 194 ? 36.124  -75.087  70.393  1.000 61.783  0 523 THR III CA  1 ? 35 
ATOM   11721 C C   . THR I  1 194 ? 35.075  -76.110  69.943  1.000 60.859  0 523 THR III C   1 ? 35 
ATOM   11722 O O   . THR I  1 194 ? 34.188  -76.374  70.729  1.000 61.954  0 523 THR III O   1 ? 35 
ATOM   11723 C CB  . THR I  1 194 ? 35.624  -73.631  70.422  1.000 63.172  0 523 THR III CB  1 ? 35 
ATOM   11724 O OG1 . THR I  1 194 ? 35.005  -73.313  69.168  1.000 61.973  0 523 THR III OG1 1 ? 35 
ATOM   11725 C CG2 . THR I  1 194 ? 36.738  -72.642  70.698  1.000 62.813  0 523 THR III CG2 1 ? 35 
ATOM   11726 N N   . VAL I  1 195 ? 35.158  -76.642  68.724  1.000 61.002  0 524 VAL III N   1 ? 35 
ATOM   11727 C CA  . VAL I  1 195 ? 34.158  -77.621  68.215  1.000 60.915  0 524 VAL III CA  1 ? 35 
ATOM   11728 C C   . VAL I  1 195 ? 34.903  -78.863  67.753  1.000 60.176  0 524 VAL III C   1 ? 35 
ATOM   11729 O O   . VAL I  1 195 ? 35.708  -78.715  66.842  1.000 59.026  0 524 VAL III O   1 ? 35 
ATOM   11730 C CB  . VAL I  1 195 ? 33.304  -77.033  67.073  1.000 60.626  0 524 VAL III CB  1 ? 35 
ATOM   11731 C CG1 . VAL I  1 195 ? 32.401  -78.070  66.442  1.000 60.640  0 524 VAL III CG1 1 ? 35 
ATOM   11732 C CG2 . VAL I  1 195 ? 32.460  -75.861  67.565  1.000 60.773  0 524 VAL III CG2 1 ? 35 
ATOM   11733 N N   . CYS I  1 196 ? 34.601  -80.039  68.319  1.000 62.360  0 525 CYS III N   1 ? 35 
ATOM   11734 C CA  . CYS I  1 196 ? 35.135  -81.358  67.890  1.000 64.229  0 525 CYS III CA  1 ? 35 
ATOM   11735 C C   . CYS I  1 196 ? 33.992  -82.351  67.672  1.000 64.905  0 525 CYS III C   1 ? 35 
ATOM   11736 O O   . CYS I  1 196 ? 32.936  -82.172  68.262  1.000 66.282  0 525 CYS III O   1 ? 35 
ATOM   11737 C CB  . CYS I  1 196 ? 36.114  -81.921  68.907  1.000 65.599  0 525 CYS III CB  1 ? 35 
ATOM   11738 S SG  . CYS I  1 196 ? 37.667  -81.002  68.932  1.000 70.352  0 525 CYS III SG  1 ? 35 
ATOM   11739 N N   . GLY I  1 197 ? 34.204  -83.338  66.802  1.000 65.906  0 526 GLY III N   1 ? 35 
ATOM   11740 C CA  . GLY I  1 197 ? 33.290  -84.475  66.634  1.000 69.761  0 526 GLY III CA  1 ? 35 
ATOM   11741 C C   . GLY I  1 197 ? 33.402  -85.417  67.822  1.000 74.416  0 526 GLY III C   1 ? 35 
ATOM   11742 O O   . GLY I  1 197 ? 34.278  -85.253  68.664  1.000 72.839  0 526 GLY III O   1 ? 35 
ATOM   11743 N N   . PRO I  1 198 ? 32.502  -86.417  67.939  1.000 81.621  0 527 PRO III N   1 ? 35 
ATOM   11744 C CA  . PRO I  1 198 ? 32.564  -87.401  69.022  1.000 85.866  0 527 PRO III CA  1 ? 35 
ATOM   11745 C C   . PRO I  1 198 ? 33.882  -88.175  69.142  1.000 91.739  0 527 PRO III C   1 ? 35 
ATOM   11746 O O   . PRO I  1 198 ? 34.191  -88.606  70.242  1.000 89.478  0 527 PRO III O   1 ? 35 
ATOM   11747 C CB  . PRO I  1 198 ? 31.479  -88.408  68.628  1.000 86.027  0 527 PRO III CB  1 ? 35 
ATOM   11748 C CG  . PRO I  1 198 ? 30.474  -87.590  67.840  1.000 84.437  0 527 PRO III CG  1 ? 35 
ATOM   11749 C CD  . PRO I  1 198 ? 31.308  -86.573  67.099  1.000 81.911  0 527 PRO III CD  1 ? 35 
ATOM   11750 N N   . LYS I  1 199 ? 34.586  -88.393  68.023  1.000 71.503  0 528 LYS III N   1 ? ?  
ATOM   11751 C CA  . LYS I  1 199 ? 35.762  -89.311  67.914  1.000 89.330  0 528 LYS III CA  1 ? ?  
ATOM   11752 C C   . LYS I  1 199 ? 37.086  -88.539  68.022  1.000 88.058  0 528 LYS III C   1 ? ?  
ATOM   11753 O O   . LYS I  1 199 ? 37.176  -87.317  67.972  1.000 81.774  0 528 LYS III O   1 ? ?  
ATOM   11754 C CB  . LYS I  1 199 ? 35.681  -90.090  66.599  1.000 99.802  0 528 LYS III CB  1 ? ?  
ATOM   11755 C CG  . LYS I  1 199 ? 34.314  -90.713  66.344  1.000 110.139 0 528 LYS III CG  1 ? ?  
ATOM   11756 C CD  . LYS I  1 199 ? 34.260  -91.637  65.151  1.000 115.985 0 528 LYS III CD  1 ? ?  
ATOM   11757 C CE  . LYS I  1 199 ? 33.067  -92.570  65.196  1.000 119.459 0 528 LYS III CE  1 ? ?  
ATOM   11758 N NZ  . LYS I  1 199 ? 33.112  -93.578  64.110  1.000 120.273 0 528 LYS III NZ  1 ? ?  
ATOM   11759 N N   . GLN J  2 1   ? 32.193  -71.986  34.064  1.000 64.846  0 1   GLN JJJ N   1 ? 36 
ATOM   11760 C CA  . GLN J  2 1   ? 32.013  -72.924  32.928  1.000 64.478  0 1   GLN JJJ CA  1 ? 36 
ATOM   11761 C C   . GLN J  2 1   ? 33.294  -73.751  32.774  1.000 60.108  0 1   GLN JJJ C   1 ? 36 
ATOM   11762 O O   . GLN J  2 1   ? 34.340  -73.185  32.465  1.000 62.827  0 1   GLN JJJ O   1 ? 36 
ATOM   11763 C CB  . GLN J  2 1   ? 31.651  -72.114  31.693  1.000 72.345  0 1   GLN JJJ CB  1 ? 36 
ATOM   11764 C CG  . GLN J  2 1   ? 31.861  -70.609  31.942  1.000 80.201  0 1   GLN JJJ CG  1 ? 36 
ATOM   11765 C CD  . GLN J  2 1   ? 31.711  -69.630  30.792  1.000 86.010  0 1   GLN JJJ CD  1 ? 36 
ATOM   11766 O OE1 . GLN J  2 1   ? 31.493  -69.990  29.629  1.000 85.418  0 1   GLN JJJ OE1 1 ? 36 
ATOM   11767 N NE2 . GLN J  2 1   ? 31.848  -68.344  31.115  1.000 88.116  0 1   GLN JJJ NE2 1 ? 36 
ATOM   11768 N N   . VAL J  2 2   ? 33.218  -75.044  33.057  1.000 54.891  0 2   VAL JJJ N   1 ? 36 
ATOM   11769 C CA  . VAL J  2 2   ? 34.296  -76.044  32.813  1.000 49.185  0 2   VAL JJJ CA  1 ? 36 
ATOM   11770 C C   . VAL J  2 2   ? 33.813  -76.955  31.685  1.000 46.831  0 2   VAL JJJ C   1 ? 36 
ATOM   11771 O O   . VAL J  2 2   ? 32.685  -77.496  31.795  1.000 51.166  0 2   VAL JJJ O   1 ? 36 
ATOM   11772 C CB  . VAL J  2 2   ? 34.581  -76.881  34.074  1.000 47.841  0 2   VAL JJJ CB  1 ? 36 
ATOM   11773 C CG1 . VAL J  2 2   ? 35.615  -77.947  33.807  1.000 46.668  0 2   VAL JJJ CG1 1 ? 36 
ATOM   11774 C CG2 . VAL J  2 2   ? 35.004  -76.029  35.257  1.000 48.957  0 2   VAL JJJ CG2 1 ? 36 
ATOM   11775 N N   . GLN J  2 3   ? 34.641  -77.220  30.686  1.000 42.688  0 3   GLN JJJ N   1 ? 36 
ATOM   11776 C CA  . GLN J  2 3   ? 34.343  -78.281  29.708  1.000 39.469  0 3   GLN JJJ CA  1 ? 36 
ATOM   11777 C C   . GLN J  2 3   ? 35.162  -79.526  30.076  1.000 39.237  0 3   GLN JJJ C   1 ? 36 
ATOM   11778 O O   . GLN J  2 3   ? 36.260  -79.412  30.652  1.000 37.181  0 3   GLN JJJ O   1 ? 36 
ATOM   11779 C CB  . GLN J  2 3   ? 34.539  -77.775  28.286  1.000 38.437  0 3   GLN JJJ CB  1 ? 36 
ATOM   11780 C CG  . GLN J  2 3   ? 33.401  -76.868  27.856  1.000 38.828  0 3   GLN JJJ CG  1 ? 36 
ATOM   11781 C CD  . GLN J  2 3   ? 33.508  -76.483  26.397  1.000 38.252  0 3   GLN JJJ CD  1 ? 36 
ATOM   11782 O OE1 . GLN J  2 3   ? 33.492  -77.322  25.504  1.000 35.553  0 3   GLN JJJ OE1 1 ? 36 
ATOM   11783 N NE2 . GLN J  2 3   ? 33.646  -75.198  26.141  1.000 38.725  0 3   GLN JJJ NE2 1 ? 36 
ATOM   11784 N N   . LEU J  2 4   ? 34.586  -80.678  29.760  1.000 40.383  0 4   LEU JJJ N   1 ? 36 
ATOM   11785 C CA  . LEU J  2 4   ? 35.113  -82.020  30.071  1.000 41.046  0 4   LEU JJJ CA  1 ? 36 
ATOM   11786 C C   . LEU J  2 4   ? 35.025  -82.871  28.793  1.000 43.020  0 4   LEU JJJ C   1 ? 36 
ATOM   11787 O O   . LEU J  2 4   ? 33.965  -82.888  28.135  1.000 43.237  0 4   LEU JJJ O   1 ? 36 
ATOM   11788 C CB  . LEU J  2 4   ? 34.275  -82.633  31.191  1.000 40.602  0 4   LEU JJJ CB  1 ? 36 
ATOM   11789 C CG  . LEU J  2 4   ? 34.168  -81.849  32.500  1.000 40.728  0 4   LEU JJJ CG  1 ? 36 
ATOM   11790 C CD1 . LEU J  2 4   ? 33.088  -82.493  33.393  1.000 41.337  0 4   LEU JJJ CD1 1 ? 36 
ATOM   11791 C CD2 . LEU J  2 4   ? 35.514  -81.790  33.218  1.000 40.339  0 4   LEU JJJ CD2 1 ? 36 
ATOM   11792 N N   . VAL J  2 5   ? 36.116  -83.529  28.435  1.000 43.881  0 5   VAL JJJ N   1 ? 36 
ATOM   11793 C CA  . VAL J  2 5   ? 36.179  -84.423  27.253  1.000 44.953  0 5   VAL JJJ CA  1 ? 36 
ATOM   11794 C C   . VAL J  2 5   ? 36.768  -85.769  27.691  1.000 44.924  0 5   VAL JJJ C   1 ? 36 
ATOM   11795 O O   . VAL J  2 5   ? 37.936  -85.819  28.150  1.000 43.580  0 5   VAL JJJ O   1 ? 36 
ATOM   11796 C CB  . VAL J  2 5   ? 36.992  -83.773  26.120  1.000 45.888  0 5   VAL JJJ CB  1 ? 36 
ATOM   11797 C CG1 . VAL J  2 5   ? 37.242  -84.762  24.979  1.000 46.250  0 5   VAL JJJ CG1 1 ? 36 
ATOM   11798 C CG2 . VAL J  2 5   ? 36.310  -82.503  25.619  1.000 45.937  0 5   VAL JJJ CG2 1 ? 36 
ATOM   11799 N N   . GLU J  2 6   ? 35.958  -86.820  27.538  1.000 47.100  0 6   GLU JJJ N   1 ? 36 
ATOM   11800 C CA  . GLU J  2 6   ? 36.351  -88.238  27.760  1.000 47.938  0 6   GLU JJJ CA  1 ? 36 
ATOM   11801 C C   . GLU J  2 6   ? 37.123  -88.735  26.536  1.000 48.084  0 6   GLU JJJ C   1 ? 36 
ATOM   11802 O O   . GLU J  2 6   ? 36.817  -88.282  25.423  1.000 50.827  0 6   GLU JJJ O   1 ? 36 
ATOM   11803 C CB  . GLU J  2 6   ? 35.114  -89.108  27.985  1.000 48.456  0 6   GLU JJJ CB  1 ? 36 
ATOM   11804 C CG  . GLU J  2 6   ? 34.195  -88.607  29.094  1.000 47.668  0 6   GLU JJJ CG  1 ? 36 
ATOM   11805 C CD  . GLU J  2 6   ? 33.086  -87.661  28.666  1.000 47.933  0 6   GLU JJJ CD  1 ? 36 
ATOM   11806 O OE1 . GLU J  2 6   ? 33.193  -87.073  27.555  1.000 45.746  0 6   GLU JJJ OE1 1 ? 36 
ATOM   11807 O OE2 . GLU J  2 6   ? 32.104  -87.518  29.447  1.000 48.064  0 6   GLU JJJ OE2 1 ? 36 
ATOM   11808 N N   . SER J  2 7   ? 38.077  -89.641  26.749  1.000 49.233  0 7   SER JJJ N   1 ? 36 
ATOM   11809 C CA  . SER J  2 7   ? 38.795  -90.416  25.707  1.000 51.408  0 7   SER JJJ CA  1 ? 36 
ATOM   11810 C C   . SER J  2 7   ? 39.144  -91.808  26.256  1.000 54.168  0 7   SER JJJ C   1 ? 36 
ATOM   11811 O O   . SER J  2 7   ? 38.938  -92.028  27.472  1.000 54.975  0 7   SER JJJ O   1 ? 36 
ATOM   11812 C CB  . SER J  2 7   ? 39.995  -89.683  25.232  1.000 50.028  0 7   SER JJJ CB  1 ? 36 
ATOM   11813 O OG  . SER J  2 7   ? 40.877  -89.496  26.304  1.000 50.004  0 7   SER JJJ OG  1 ? 36 
ATOM   11814 N N   . GLY J  2 8   ? 39.560  -92.731  25.386  1.000 57.551  0 8   GLY JJJ N   1 ? 36 
ATOM   11815 C CA  . GLY J  2 8   ? 39.976  -94.092  25.774  1.000 62.031  0 8   GLY JJJ CA  1 ? 36 
ATOM   11816 C C   . GLY J  2 8   ? 38.846  -95.115  25.737  1.000 64.330  0 8   GLY JJJ C   1 ? 36 
ATOM   11817 O O   . GLY J  2 8   ? 39.098  -96.281  26.103  1.000 69.649  0 8   GLY JJJ O   1 ? 36 
ATOM   11818 N N   . GLY J  2 9   ? 37.646  -94.721  25.297  1.000 63.263  0 9   GLY JJJ N   1 ? 36 
ATOM   11819 C CA  . GLY J  2 9   ? 36.491  -95.639  25.173  1.000 63.175  0 9   GLY JJJ CA  1 ? 36 
ATOM   11820 C C   . GLY J  2 9   ? 36.624  -96.513  23.944  1.000 62.844  0 9   GLY JJJ C   1 ? 36 
ATOM   11821 O O   . GLY J  2 9   ? 37.652  -96.405  23.265  1.000 65.357  0 9   GLY JJJ O   1 ? 36 
ATOM   11822 N N   . GLY J  2 10  ? 35.627  -97.349  23.658  1.000 61.069  0 10  GLY JJJ N   1 ? 36 
ATOM   11823 C CA  . GLY J  2 10  ? 35.602  -98.187  22.449  1.000 60.699  0 10  GLY JJJ CA  1 ? 36 
ATOM   11824 C C   . GLY J  2 10  ? 35.308  -99.638  22.787  1.000 62.726  0 10  GLY JJJ C   1 ? 36 
ATOM   11825 O O   . GLY J  2 10  ? 34.763  -99.928  23.875  1.000 61.889  0 10  GLY JJJ O   1 ? 36 
ATOM   11826 N N   . LEU J  2 11  ? 35.666  -100.512 21.852  1.000 64.863  0 11  LEU JJJ N   1 ? 36 
ATOM   11827 C CA  . LEU J  2 11  ? 35.334  -101.955 21.852  1.000 66.762  0 11  LEU JJJ CA  1 ? 36 
ATOM   11828 C C   . LEU J  2 11  ? 36.404  -102.688 22.665  1.000 68.111  0 11  LEU JJJ C   1 ? 36 
ATOM   11829 O O   . LEU J  2 11  ? 37.588  -102.332 22.531  1.000 67.407  0 11  LEU JJJ O   1 ? 36 
ATOM   11830 C CB  . LEU J  2 11  ? 35.310  -102.408 20.386  1.000 67.803  0 11  LEU JJJ CB  1 ? 36 
ATOM   11831 C CG  . LEU J  2 11  ? 34.961  -103.870 20.142  1.000 71.668  0 11  LEU JJJ CG  1 ? 36 
ATOM   11832 C CD1 . LEU J  2 11  ? 33.654  -104.229 20.854  1.000 72.502  0 11  LEU JJJ CD1 1 ? 36 
ATOM   11833 C CD2 . LEU J  2 11  ? 34.912  -104.181 18.649  1.000 73.062  0 11  LEU JJJ CD2 1 ? 36 
ATOM   11834 N N   . VAL J  2 12  ? 36.018  -103.660 23.486  1.000 70.594  0 12  VAL JJJ N   1 ? 36 
ATOM   11835 C CA  . VAL J  2 12  ? 36.991  -104.512 24.228  1.000 73.099  0 12  VAL JJJ CA  1 ? 36 
ATOM   11836 C C   . VAL J  2 12  ? 36.314  -105.857 24.508  1.000 76.214  0 12  VAL JJJ C   1 ? 36 
ATOM   11837 O O   . VAL J  2 12  ? 35.082  -105.874 24.668  1.000 74.144  0 12  VAL JJJ O   1 ? 36 
ATOM   11838 C CB  . VAL J  2 12  ? 37.483  -103.800 25.502  1.000 71.156  0 12  VAL JJJ CB  1 ? 36 
ATOM   11839 C CG1 . VAL J  2 12  ? 36.400  -103.704 26.557  1.000 70.157  0 12  VAL JJJ CG1 1 ? 36 
ATOM   11840 C CG2 . VAL J  2 12  ? 38.739  -104.450 26.052  1.000 74.669  0 12  VAL JJJ CG2 1 ? 36 
ATOM   11841 N N   . GLN J  2 13  ? 37.096  -106.941 24.514  1.000 80.603  0 13  GLN JJJ N   1 ? 36 
ATOM   11842 C CA  . GLN J  2 13  ? 36.614  -108.317 24.795  1.000 84.207  0 13  GLN JJJ CA  1 ? 36 
ATOM   11843 C C   . GLN J  2 13  ? 36.418  -108.470 26.309  1.000 83.491  0 13  GLN JJJ C   1 ? 36 
ATOM   11844 O O   . GLN J  2 13  ? 37.190  -107.860 27.081  1.000 81.340  0 13  GLN JJJ O   1 ? 36 
ATOM   11845 C CB  . GLN J  2 13  ? 37.569  -109.350 24.196  1.000 88.285  0 13  GLN JJJ CB  1 ? 36 
ATOM   11846 C CG  . GLN J  2 13  ? 37.435  -109.410 22.685  1.000 90.130  0 13  GLN JJJ CG  1 ? 36 
ATOM   11847 C CD  . GLN J  2 13  ? 38.200  -110.534 22.034  1.000 96.500  0 13  GLN JJJ CD  1 ? 36 
ATOM   11848 O OE1 . GLN J  2 13  ? 37.957  -111.733 22.245  1.000 100.477 0 13  GLN JJJ OE1 1 ? 36 
ATOM   11849 N NE2 . GLN J  2 13  ? 39.108  -110.141 21.159  1.000 97.353  0 13  GLN JJJ NE2 1 ? 36 
ATOM   11850 N N   . ALA J  2 14  ? 35.383  -109.219 26.707  1.000 85.022  0 14  ALA JJJ N   1 ? 36 
ATOM   11851 C CA  . ALA J  2 14  ? 35.092  -109.616 28.108  1.000 84.927  0 14  ALA JJJ CA  1 ? 36 
ATOM   11852 C C   . ALA J  2 14  ? 36.384  -110.116 28.760  1.000 85.741  0 14  ALA JJJ C   1 ? 36 
ATOM   11853 O O   . ALA J  2 14  ? 37.170  -110.769 28.071  1.000 86.578  0 14  ALA JJJ O   1 ? 36 
ATOM   11854 C CB  . ALA J  2 14  ? 34.011  -110.659 28.143  1.000 86.970  0 14  ALA JJJ CB  1 ? 36 
ATOM   11855 N N   . GLY J  2 15  ? 36.613  -109.759 30.024  1.000 85.126  0 15  GLY JJJ N   1 ? 36 
ATOM   11856 C CA  . GLY J  2 15  ? 37.869  -110.039 30.745  1.000 86.967  0 15  GLY JJJ CA  1 ? 36 
ATOM   11857 C C   . GLY J  2 15  ? 38.964  -109.038 30.404  1.000 85.321  0 15  GLY JJJ C   1 ? 36 
ATOM   11858 O O   . GLY J  2 15  ? 39.986  -109.061 31.088  1.000 86.459  0 15  GLY JJJ O   1 ? 36 
ATOM   11859 N N   . GLY J  2 16  ? 38.769  -108.173 29.405  1.000 83.367  0 16  GLY JJJ N   1 ? 36 
ATOM   11860 C CA  . GLY J  2 16  ? 39.777  -107.192 28.963  1.000 81.693  0 16  GLY JJJ CA  1 ? 36 
ATOM   11861 C C   . GLY J  2 16  ? 39.787  -105.968 29.855  1.000 78.649  0 16  GLY JJJ C   1 ? 36 
ATOM   11862 O O   . GLY J  2 16  ? 39.031  -105.940 30.854  1.000 78.628  0 16  GLY JJJ O   1 ? 36 
ATOM   11863 N N   . SER J  2 17  ? 40.632  -104.993 29.500  1.000 76.902  0 17  SER JJJ N   1 ? 36 
ATOM   11864 C CA  . SER J  2 17  ? 40.863  -103.720 30.233  1.000 72.500  0 17  SER JJJ CA  1 ? 36 
ATOM   11865 C C   . SER J  2 17  ? 40.714  -102.517 29.310  1.000 70.131  0 17  SER JJJ C   1 ? 36 
ATOM   11866 O O   . SER J  2 17  ? 40.948  -102.634 28.111  1.000 71.522  0 17  SER JJJ O   1 ? 36 
ATOM   11867 C CB  . SER J  2 17  ? 42.216  -103.696 30.873  1.000 72.391  0 17  SER JJJ CB  1 ? 36 
ATOM   11868 O OG  . SER J  2 17  ? 42.248  -104.595 31.962  1.000 74.083  0 17  SER JJJ OG  1 ? 36 
ATOM   11869 N N   . LEU J  2 18  ? 40.372  -101.387 29.915  1.000 68.162  0 18  LEU JJJ N   1 ? 36 
ATOM   11870 C CA  . LEU J  2 18  ? 40.298  -100.050 29.288  1.000 67.167  0 18  LEU JJJ CA  1 ? 36 
ATOM   11871 C C   . LEU J  2 18  ? 40.661  -99.031  30.352  1.000 66.151  0 18  LEU JJJ C   1 ? 36 
ATOM   11872 O O   . LEU J  2 18  ? 40.187  -99.189  31.490  1.000 67.719  0 18  LEU JJJ O   1 ? 36 
ATOM   11873 C CB  . LEU J  2 18  ? 38.875  -99.771  28.813  1.000 66.830  0 18  LEU JJJ CB  1 ? 36 
ATOM   11874 C CG  . LEU J  2 18  ? 38.535  -100.143 27.376  1.000 69.269  0 18  LEU JJJ CG  1 ? 36 
ATOM   11875 C CD1 . LEU J  2 18  ? 37.192  -99.538  27.012  1.000 68.008  0 18  LEU JJJ CD1 1 ? 36 
ATOM   11876 C CD2 . LEU J  2 18  ? 39.607  -99.675  26.405  1.000 69.671  0 18  LEU JJJ CD2 1 ? 36 
ATOM   11877 N N   . ARG J  2 19  ? 41.432  -98.019  29.977  1.000 64.925  0 19  ARG JJJ N   1 ? 36 
ATOM   11878 C CA  . ARG J  2 19  ? 41.615  -96.808  30.799  1.000 62.887  0 19  ARG JJJ CA  1 ? 36 
ATOM   11879 C C   . ARG J  2 19  ? 40.916  -95.641  30.093  1.000 57.975  0 19  ARG JJJ C   1 ? 36 
ATOM   11880 O O   . ARG J  2 19  ? 41.436  -95.127  29.065  1.000 52.442  0 19  ARG JJJ O   1 ? 36 
ATOM   11881 C CB  . ARG J  2 19  ? 43.090  -96.522  31.070  1.000 66.983  0 19  ARG JJJ CB  1 ? 36 
ATOM   11882 C CG  . ARG J  2 19  ? 43.269  -95.632  32.284  1.000 69.718  0 19  ARG JJJ CG  1 ? 36 
ATOM   11883 C CD  . ARG J  2 19  ? 44.719  -95.329  32.569  1.000 76.177  0 19  ARG JJJ CD  1 ? 36 
ATOM   11884 N NE  . ARG J  2 19  ? 45.286  -94.540  31.498  1.000 80.187  0 19  ARG JJJ NE  1 ? 36 
ATOM   11885 C CZ  . ARG J  2 19  ? 46.322  -93.716  31.639  1.000 83.971  0 19  ARG JJJ CZ  1 ? 36 
ATOM   11886 N NH1 . ARG J  2 19  ? 46.924  -93.551  32.813  1.000 83.239  0 19  ARG JJJ NH1 1 ? 36 
ATOM   11887 N NH2 . ARG J  2 19  ? 46.758  -93.051  30.583  1.000 84.135  0 19  ARG JJJ NH2 1 ? 36 
ATOM   11888 N N   . LEU J  2 20  ? 39.758  -95.256  30.630  1.000 56.213  0 20  LEU JJJ N   1 ? 36 
ATOM   11889 C CA  . LEU J  2 20  ? 39.081  -93.995  30.284  1.000 55.312  0 20  LEU JJJ CA  1 ? 36 
ATOM   11890 C C   . LEU J  2 20  ? 39.888  -92.860  30.911  1.000 55.274  0 20  LEU JJJ C   1 ? 36 
ATOM   11891 O O   . LEU J  2 20  ? 40.402  -93.010  32.039  1.000 56.524  0 20  LEU JJJ O   1 ? 36 
ATOM   11892 C CB  . LEU J  2 20  ? 37.641  -93.997  30.805  1.000 56.564  0 20  LEU JJJ CB  1 ? 36 
ATOM   11893 C CG  . LEU J  2 20  ? 36.733  -95.103  30.262  1.000 59.875  0 20  LEU JJJ CG  1 ? 36 
ATOM   11894 C CD1 . LEU J  2 20  ? 35.281  -94.870  30.682  1.000 60.636  0 20  LEU JJJ CD1 1 ? 36 
ATOM   11895 C CD2 . LEU J  2 20  ? 36.845  -95.207  28.752  1.000 59.980  0 20  LEU JJJ CD2 1 ? 36 
ATOM   11896 N N   . ALA J  2 21  ? 40.002  -91.750  30.188  1.000 55.179  0 21  ALA JJJ N   1 ? 36 
ATOM   11897 C CA  . ALA J  2 21  ? 40.533  -90.482  30.713  1.000 52.528  0 21  ALA JJJ CA  1 ? 36 
ATOM   11898 C C   . ALA J  2 21  ? 39.538  -89.371  30.435  1.000 50.886  0 21  ALA JJJ C   1 ? 36 
ATOM   11899 O O   . ALA J  2 21  ? 38.753  -89.464  29.476  1.000 54.230  0 21  ALA JJJ O   1 ? 36 
ATOM   11900 C CB  . ALA J  2 21  ? 41.869  -90.193  30.105  1.000 52.565  0 21  ALA JJJ CB  1 ? 36 
ATOM   11901 N N   . CYS J  2 22  ? 39.571  -88.348  31.264  1.000 48.326  0 22  CYS JJJ N   1 ? 36 
ATOM   11902 C CA  . CYS J  2 22  ? 38.744  -87.149  31.071  1.000 46.941  0 22  CYS JJJ CA  1 ? 36 
ATOM   11903 C C   . CYS J  2 22  ? 39.580  -85.936  31.448  1.000 47.611  0 22  CYS JJJ C   1 ? 36 
ATOM   11904 O O   . CYS J  2 22  ? 40.085  -85.895  32.588  1.000 49.196  0 22  CYS JJJ O   1 ? 36 
ATOM   11905 C CB  . CYS J  2 22  ? 37.492  -87.248  31.924  1.000 48.351  0 22  CYS JJJ CB  1 ? 36 
ATOM   11906 S SG  . CYS J  2 22  ? 36.644  -85.660  32.040  1.000 51.769  0 22  CYS JJJ SG  1 ? 36 
ATOM   11907 N N   . ILE J  2 23  ? 39.685  -84.990  30.521  1.000 46.298  0 23  ILE JJJ N   1 ? 36 
ATOM   11908 C CA  . ILE J  2 23  ? 40.487  -83.755  30.702  1.000 43.911  0 23  ILE JJJ CA  1 ? 36 
ATOM   11909 C C   . ILE J  2 23  ? 39.505  -82.584  30.856  1.000 44.425  0 23  ILE JJJ C   1 ? 36 
ATOM   11910 O O   . ILE J  2 23  ? 38.474  -82.558  30.144  1.000 42.708  0 23  ILE JJJ O   1 ? 36 
ATOM   11911 C CB  . ILE J  2 23  ? 41.498  -83.599  29.550  1.000 41.949  0 23  ILE JJJ CB  1 ? 36 
ATOM   11912 C CG1 . ILE J  2 23  ? 42.495  -82.485  29.851  1.000 41.377  0 23  ILE JJJ CG1 1 ? 36 
ATOM   11913 C CG2 . ILE J  2 23  ? 40.800  -83.396  28.214  1.000 42.411  0 23  ILE JJJ CG2 1 ? 36 
ATOM   11914 C CD1 . ILE J  2 23  ? 43.596  -82.310  28.852  1.000 40.768  0 23  ILE JJJ CD1 1 ? 36 
ATOM   11915 N N   . ALA J  2 24  ? 39.799  -81.681  31.791  1.000 43.296  0 24  ALA JJJ N   1 ? 36 
ATOM   11916 C CA  . ALA J  2 24  ? 38.999  -80.472  32.094  1.000 42.811  0 24  ALA JJJ CA  1 ? 36 
ATOM   11917 C C   . ALA J  2 24  ? 39.732  -79.235  31.565  1.000 43.034  0 24  ALA JJJ C   1 ? 36 
ATOM   11918 O O   . ALA J  2 24  ? 40.993  -79.239  31.509  1.000 42.690  0 24  ALA JJJ O   1 ? 36 
ATOM   11919 C CB  . ALA J  2 24  ? 38.756  -80.379  33.574  1.000 40.258  0 24  ALA JJJ CB  1 ? 36 
ATOM   11920 N N   . SER J  2 25  ? 38.968  -78.228  31.133  1.000 42.124  0 25  SER JJJ N   1 ? 36 
ATOM   11921 C CA  . SER J  2 25  ? 39.450  -76.846  30.906  1.000 41.145  0 25  SER JJJ CA  1 ? 36 
ATOM   11922 C C   . SER J  2 25  ? 39.808  -76.226  32.262  1.000 41.129  0 25  SER JJJ C   1 ? 36 
ATOM   11923 O O   . SER J  2 25  ? 39.543  -76.852  33.286  1.000 40.803  0 25  SER JJJ O   1 ? 36 
ATOM   11924 C CB  . SER J  2 25  ? 38.407  -76.053  30.194  1.000 41.542  0 25  SER JJJ CB  1 ? 36 
ATOM   11925 O OG  . SER J  2 25  ? 37.272  -75.878  31.027  1.000 41.749  0 25  SER JJJ OG  1 ? 36 
ATOM   11926 N N   . GLY J  2 26  ? 40.363  -75.020  32.271  1.000 42.719  0 26  GLY JJJ N   1 ? 36 
ATOM   11927 C CA  . GLY J  2 26  ? 40.538  -74.236  33.510  1.000 44.585  0 26  GLY JJJ CA  1 ? 36 
ATOM   11928 C C   . GLY J  2 26  ? 41.891  -74.435  34.159  1.000 45.932  0 26  GLY JJJ C   1 ? 36 
ATOM   11929 O O   . GLY J  2 26  ? 42.609  -75.351  33.786  1.000 46.807  0 26  GLY JJJ O   1 ? 36 
ATOM   11930 N N   . ARG J  2 27  ? 42.219  -73.611  35.129  1.000 49.732  0 27  ARG JJJ N   1 ? 36 
ATOM   11931 C CA  . ARG J  2 27  ? 43.518  -73.643  35.837  1.000 52.307  0 27  ARG JJJ CA  1 ? 36 
ATOM   11932 C C   . ARG J  2 27  ? 43.291  -74.024  37.300  1.000 48.134  0 27  ARG JJJ C   1 ? 36 
ATOM   11933 O O   . ARG J  2 27  ? 44.202  -73.843  38.076  1.000 47.180  0 27  ARG JJJ O   1 ? 36 
ATOM   11934 C CB  . ARG J  2 27  ? 44.189  -72.272  35.710  1.000 61.550  0 27  ARG JJJ CB  1 ? 36 
ATOM   11935 C CG  . ARG J  2 27  ? 44.995  -72.055  34.439  1.000 69.806  0 27  ARG JJJ CG  1 ? 36 
ATOM   11936 C CD  . ARG J  2 27  ? 45.292  -70.570  34.197  1.000 81.991  0 27  ARG JJJ CD  1 ? 36 
ATOM   11937 N NE  . ARG J  2 27  ? 44.419  -69.631  34.923  1.000 89.514  0 27  ARG JJJ NE  1 ? 36 
ATOM   11938 C CZ  . ARG J  2 27  ? 43.416  -68.897  34.408  1.000 94.953  0 27  ARG JJJ CZ  1 ? 36 
ATOM   11939 N NH1 . ARG J  2 27  ? 43.096  -68.947  33.123  1.000 102.040 0 27  ARG JJJ NH1 1 ? 36 
ATOM   11940 N NH2 . ARG J  2 27  ? 42.717  -68.104  35.202  1.000 96.507  0 27  ARG JJJ NH2 1 ? 36 
ATOM   11941 N N   . THR J  2 28  ? 42.118  -74.519  37.688  1.000 46.153  0 28  THR JJJ N   1 ? 36 
ATOM   11942 C CA  . THR J  2 28  ? 41.798  -74.823  39.113  1.000 45.352  0 28  THR JJJ CA  1 ? 36 
ATOM   11943 C C   . THR J  2 28  ? 41.237  -76.247  39.227  1.000 43.457  0 28  THR JJJ C   1 ? 36 
ATOM   11944 O O   . THR J  2 28  ? 40.351  -76.473  40.085  1.000 44.599  0 28  THR JJJ O   1 ? 36 
ATOM   11945 C CB  . THR J  2 28  ? 40.835  -73.784  39.711  1.000 46.220  0 28  THR JJJ CB  1 ? 36 
ATOM   11946 O OG1 . THR J  2 28  ? 39.686  -73.687  38.851  1.000 43.033  0 28  THR JJJ OG1 1 ? 36 
ATOM   11947 C CG2 . THR J  2 28  ? 41.523  -72.453  39.939  1.000 45.775  0 28  THR JJJ CG2 1 ? 36 
ATOM   11948 N N   . PHE J  2 29  ? 41.751  -77.162  38.404  1.000 40.495  0 29  PHE JJJ N   1 ? 36 
ATOM   11949 C CA  . PHE J  2 29  ? 41.322  -78.569  38.385  1.000 41.038  0 29  PHE JJJ CA  1 ? 36 
ATOM   11950 C C   . PHE J  2 29  ? 41.398  -79.181  39.787  1.000 41.731  0 29  PHE JJJ C   1 ? 36 
ATOM   11951 O O   . PHE J  2 29  ? 40.486  -79.958  40.133  1.000 45.317  0 29  PHE JJJ O   1 ? 36 
ATOM   11952 C CB  . PHE J  2 29  ? 42.211  -79.337  37.415  1.000 42.212  0 29  PHE JJJ CB  1 ? 36 
ATOM   11953 C CG  . PHE J  2 29  ? 41.832  -80.788  37.295  1.000 42.866  0 29  PHE JJJ CG  1 ? 36 
ATOM   11954 C CD1 . PHE J  2 29  ? 40.720  -81.151  36.547  1.000 42.893  0 29  PHE JJJ CD1 1 ? 36 
ATOM   11955 C CD2 . PHE J  2 29  ? 42.568  -81.779  37.947  1.000 43.100  0 29  PHE JJJ CD2 1 ? 36 
ATOM   11956 C CE1 . PHE J  2 29  ? 40.370  -82.481  36.427  1.000 44.640  0 29  PHE JJJ CE1 1 ? 36 
ATOM   11957 C CE2 . PHE J  2 29  ? 42.207  -83.105  37.832  1.000 44.239  0 29  PHE JJJ CE2 1 ? 36 
ATOM   11958 C CZ  . PHE J  2 29  ? 41.123  -83.459  37.061  1.000 44.799  0 29  PHE JJJ CZ  1 ? 36 
ATOM   11959 N N   . HIS J  2 30  ? 42.435  -78.832  40.569  1.000 40.518  0 30  HIS JJJ N   1 ? 36 
ATOM   11960 C CA  . HIS J  2 30  ? 42.658  -79.320  41.954  1.000 40.588  0 30  HIS JJJ CA  1 ? 36 
ATOM   11961 C C   . HIS J  2 30  ? 41.455  -78.998  42.854  1.000 39.718  0 30  HIS JJJ C   1 ? 36 
ATOM   11962 O O   . HIS J  2 30  ? 41.317  -79.665  43.886  1.000 41.669  0 30  HIS JJJ O   1 ? 36 
ATOM   11963 C CB  . HIS J  2 30  ? 43.983  -78.745  42.491  1.000 39.636  0 30  HIS JJJ CB  1 ? 36 
ATOM   11964 C CG  . HIS J  2 30  ? 43.891  -77.282  42.722  1.000 41.090  0 30  HIS JJJ CG  1 ? 36 
ATOM   11965 N ND1 . HIS J  2 30  ? 43.545  -76.785  43.947  1.000 42.197  0 30  HIS JJJ ND1 1 ? 36 
ATOM   11966 C CD2 . HIS J  2 30  ? 44.010  -76.212  41.890  1.000 42.770  0 30  HIS JJJ CD2 1 ? 36 
ATOM   11967 C CE1 . HIS J  2 30  ? 43.524  -75.457  43.904  1.000 44.115  0 30  HIS JJJ CE1 1 ? 36 
ATOM   11968 N NE2 . HIS J  2 30  ? 43.786  -75.086  42.644  1.000 43.991  0 30  HIS JJJ NE2 1 ? 36 
ATOM   11969 N N   . SER J  2 31  ? 40.634  -78.002  42.500  1.000 39.271  0 31  SER JJJ N   1 ? 36 
ATOM   11970 C CA  . SER J  2 31  ? 39.494  -77.562  43.332  1.000 40.875  0 31  SER JJJ CA  1 ? 36 
ATOM   11971 C C   . SER J  2 31  ? 38.257  -78.414  43.043  1.000 40.857  0 31  SER JJJ C   1 ? 36 
ATOM   11972 O O   . SER J  2 31  ? 37.244  -78.201  43.717  1.000 41.324  0 31  SER JJJ O   1 ? 36 
ATOM   11973 C CB  . SER J  2 31  ? 39.233  -76.097  43.159  1.000 42.306  0 31  SER JJJ CB  1 ? 36 
ATOM   11974 O OG  . SER J  2 31  ? 38.696  -75.792  41.897  1.000 43.635  0 31  SER JJJ OG  1 ? 36 
ATOM   11975 N N   . TYR J  2 32  ? 38.325  -79.344  42.087  1.000 40.633  0 32  TYR JJJ N   1 ? 36 
ATOM   11976 C CA  . TYR J  2 32  ? 37.153  -80.139  41.635  1.000 40.542  0 32  TYR JJJ CA  1 ? 36 
ATOM   11977 C C   . TYR J  2 32  ? 37.244  -81.564  42.174  1.000 40.901  0 32  TYR JJJ C   1 ? 36 
ATOM   11978 O O   . TYR J  2 32  ? 38.283  -82.200  42.087  1.000 38.999  0 32  TYR JJJ O   1 ? 36 
ATOM   11979 C CB  . TYR J  2 32  ? 36.991  -80.101  40.114  1.000 40.042  0 32  TYR JJJ CB  1 ? 36 
ATOM   11980 C CG  . TYR J  2 32  ? 36.482  -78.768  39.651  1.000 40.461  0 32  TYR JJJ CG  1 ? 36 
ATOM   11981 C CD1 . TYR J  2 32  ? 37.352  -77.708  39.413  1.000 40.650  0 32  TYR JJJ CD1 1 ? 36 
ATOM   11982 C CD2 . TYR J  2 32  ? 35.122  -78.527  39.561  1.000 41.658  0 32  TYR JJJ CD2 1 ? 36 
ATOM   11983 C CE1 . TYR J  2 32  ? 36.888  -76.466  39.023  1.000 40.726  0 32  TYR JJJ CE1 1 ? 36 
ATOM   11984 C CE2 . TYR J  2 32  ? 34.641  -77.279  39.192  1.000 42.441  0 32  TYR JJJ CE2 1 ? 36 
ATOM   11985 C CZ  . TYR J  2 32  ? 35.527  -76.245  38.908  1.000 41.861  0 32  TYR JJJ CZ  1 ? 36 
ATOM   11986 O OH  . TYR J  2 32  ? 35.052  -75.006  38.576  1.000 43.531  0 32  TYR JJJ OH  1 ? 36 
ATOM   11987 N N   . VAL J  2 33  ? 36.142  -82.022  42.753  1.000 43.744  0 33  VAL JJJ N   1 ? 37 
ATOM   11988 C CA  . VAL J  2 33  ? 35.819  -83.465  42.902  1.000 44.784  0 33  VAL JJJ CA  1 ? 37 
ATOM   11989 C C   . VAL J  2 33  ? 35.474  -83.982  41.509  1.000 44.797  0 33  VAL JJJ C   1 ? 37 
ATOM   11990 O O   . VAL J  2 33  ? 34.617  -83.359  40.839  1.000 49.113  0 33  VAL JJJ O   1 ? 37 
ATOM   11991 C CB  . VAL J  2 33  ? 34.667  -83.669  43.897  1.000 45.490  0 33  VAL JJJ CB  1 ? 37 
ATOM   11992 C CG1 . VAL J  2 33  ? 34.199  -85.112  43.968  1.000 46.292  0 33  VAL JJJ CG1 1 ? 37 
ATOM   11993 C CG2 . VAL J  2 33  ? 35.078  -83.177  45.261  1.000 46.746  0 33  VAL JJJ CG2 1 ? 37 
ATOM   11994 N N   . MET J  2 34  ? 36.127  -85.050  41.070  1.000 42.279  0 34  MET JJJ N   1 ? 37 
ATOM   11995 C CA  . MET J  2 34  ? 35.897  -85.637  39.731  1.000 43.238  0 34  MET JJJ CA  1 ? 37 
ATOM   11996 C C   . MET J  2 34  ? 35.165  -86.984  39.871  1.000 46.055  0 34  MET JJJ C   1 ? 37 
ATOM   11997 O O   . MET J  2 34  ? 35.409  -87.719  40.849  1.000 45.846  0 34  MET JJJ O   1 ? 37 
ATOM   11998 C CB  . MET J  2 34  ? 37.228  -85.812  39.007  1.000 43.304  0 34  MET JJJ CB  1 ? 37 
ATOM   11999 C CG  . MET J  2 34  ? 37.993  -84.513  38.794  1.000 43.421  0 34  MET JJJ CG  1 ? 37 
ATOM   12000 S SD  . MET J  2 34  ? 37.023  -83.278  37.901  1.000 42.154  0 34  MET JJJ SD  1 ? 37 
ATOM   12001 C CE  . MET J  2 34  ? 36.856  -84.055  36.300  1.000 41.852  0 34  MET JJJ CE  1 ? 37 
ATOM   12002 N N   . ALA J  2 35  ? 34.259  -87.277  38.939  1.000 48.923  0 35  ALA JJJ N   1 ? 37 
ATOM   12003 C CA  . ALA J  2 35  ? 33.403  -88.479  39.008  1.000 52.600  0 35  ALA JJJ CA  1 ? 37 
ATOM   12004 C C   . ALA J  2 35  ? 33.178  -89.080  37.622  1.000 53.780  0 35  ALA JJJ C   1 ? 37 
ATOM   12005 O O   . ALA J  2 35  ? 33.312  -88.362  36.602  1.000 58.206  0 35  ALA JJJ O   1 ? 37 
ATOM   12006 C CB  . ALA J  2 35  ? 32.098  -88.153  39.688  1.000 53.570  0 35  ALA JJJ CB  1 ? 37 
ATOM   12007 N N   . TRP J  2 36  ? 32.874  -90.377  37.628  1.000 53.903  0 36  TRP JJJ N   1 ? 37 
ATOM   12008 C CA  . TRP J  2 36  ? 32.413  -91.177  36.471  1.000 51.850  0 36  TRP JJJ CA  1 ? 37 
ATOM   12009 C C   . TRP J  2 36  ? 31.012  -91.703  36.773  1.000 52.640  0 36  TRP JJJ C   1 ? 37 
ATOM   12010 O O   . TRP J  2 36  ? 30.790  -92.243  37.860  1.000 55.751  0 36  TRP JJJ O   1 ? 37 
ATOM   12011 C CB  . TRP J  2 36  ? 33.393  -92.312  36.191  1.000 51.411  0 36  TRP JJJ CB  1 ? 37 
ATOM   12012 C CG  . TRP J  2 36  ? 34.699  -91.831  35.640  1.000 48.794  0 36  TRP JJJ CG  1 ? 37 
ATOM   12013 C CD1 . TRP J  2 36  ? 35.844  -91.614  36.338  1.000 47.717  0 36  TRP JJJ CD1 1 ? 37 
ATOM   12014 C CD2 . TRP J  2 36  ? 34.996  -91.514  34.276  1.000 45.505  0 36  TRP JJJ CD2 1 ? 37 
ATOM   12015 N NE1 . TRP J  2 36  ? 36.828  -91.162  35.507  1.000 47.282  0 36  TRP JJJ NE1 1 ? 37 
ATOM   12016 C CE2 . TRP J  2 36  ? 36.345  -91.103  34.232  1.000 44.791  0 36  TRP JJJ CE2 1 ? 37 
ATOM   12017 C CE3 . TRP J  2 36  ? 34.259  -91.521  33.091  1.000 46.403  0 36  TRP JJJ CE3 1 ? 37 
ATOM   12018 C CZ2 . TRP J  2 36  ? 36.984  -90.712  33.052  1.000 44.133  0 36  TRP JJJ CZ2 1 ? 37 
ATOM   12019 C CZ3 . TRP J  2 36  ? 34.883  -91.129  31.921  1.000 46.934  0 36  TRP JJJ CZ3 1 ? 37 
ATOM   12020 C CH2 . TRP J  2 36  ? 36.229  -90.729  31.903  1.000 44.492  0 36  TRP JJJ CH2 1 ? 37 
ATOM   12021 N N   . PHE J  2 37  ? 30.103  -91.518  35.833  1.000 51.028  0 37  PHE JJJ N   1 ? 37 
ATOM   12022 C CA  . PHE J  2 37  ? 28.783  -92.175  35.789  1.000 52.905  0 37  PHE JJJ CA  1 ? 37 
ATOM   12023 C C   . PHE J  2 37  ? 28.720  -92.951  34.474  1.000 53.752  0 37  PHE JJJ C   1 ? 37 
ATOM   12024 O O   . PHE J  2 37  ? 29.554  -92.689  33.578  1.000 51.357  0 37  PHE JJJ O   1 ? 37 
ATOM   12025 C CB  . PHE J  2 37  ? 27.669  -91.137  35.878  1.000 53.467  0 37  PHE JJJ CB  1 ? 37 
ATOM   12026 C CG  . PHE J  2 37  ? 27.469  -90.511  37.231  1.000 53.657  0 37  PHE JJJ CG  1 ? 37 
ATOM   12027 C CD1 . PHE J  2 37  ? 28.365  -89.578  37.727  1.000 52.316  0 37  PHE JJJ CD1 1 ? 37 
ATOM   12028 C CD2 . PHE J  2 37  ? 26.349  -90.821  37.992  1.000 55.753  0 37  PHE JJJ CD2 1 ? 37 
ATOM   12029 C CE1 . PHE J  2 37  ? 28.159  -88.974  38.957  1.000 52.126  0 37  PHE JJJ CE1 1 ? 37 
ATOM   12030 C CE2 . PHE J  2 37  ? 26.133  -90.217  39.232  1.000 55.413  0 37  PHE JJJ CE2 1 ? 37 
ATOM   12031 C CZ  . PHE J  2 37  ? 27.044  -89.299  39.711  1.000 54.021  0 37  PHE JJJ CZ  1 ? 37 
ATOM   12032 N N   . ARG J  2 38  ? 27.763  -93.868  34.354  1.000 54.728  0 38  ARG JJJ N   1 ? 37 
ATOM   12033 C CA  . ARG J  2 38  ? 27.518  -94.548  33.062  1.000 56.538  0 38  ARG JJJ CA  1 ? 37 
ATOM   12034 C C   . ARG J  2 38  ? 26.014  -94.702  32.848  1.000 59.140  0 38  ARG JJJ C   1 ? 37 
ATOM   12035 O O   . ARG J  2 38  ? 25.234  -94.660  33.818  1.000 59.709  0 38  ARG JJJ O   1 ? 37 
ATOM   12036 C CB  . ARG J  2 38  ? 28.228  -95.897  33.012  1.000 56.796  0 38  ARG JJJ CB  1 ? 37 
ATOM   12037 C CG  . ARG J  2 38  ? 27.592  -96.953  33.904  1.000 58.860  0 38  ARG JJJ CG  1 ? 37 
ATOM   12038 C CD  . ARG J  2 38  ? 28.515  -98.143  34.081  1.000 58.757  0 38  ARG JJJ CD  1 ? 37 
ATOM   12039 N NE  . ARG J  2 38  ? 27.995  -99.106  35.042  1.000 59.489  0 38  ARG JJJ NE  1 ? 37 
ATOM   12040 C CZ  . ARG J  2 38  ? 28.527  -100.301 35.274  1.000 60.552  0 38  ARG JJJ CZ  1 ? 37 
ATOM   12041 N NH1 . ARG J  2 38  ? 29.614  -100.708 34.633  1.000 59.089  0 38  ARG JJJ NH1 1 ? 37 
ATOM   12042 N NH2 . ARG J  2 38  ? 27.968  -101.097 36.160  1.000 63.566  0 38  ARG JJJ NH2 1 ? 37 
ATOM   12043 N N   . GLN J  2 39  ? 25.631  -94.887  31.596  1.000 60.894  0 39  GLN JJJ N   1 ? 37 
ATOM   12044 C CA  . GLN J  2 39  ? 24.215  -95.027  31.227  1.000 63.996  0 39  GLN JJJ CA  1 ? 37 
ATOM   12045 C C   . GLN J  2 39  ? 24.131  -96.039  30.100  1.000 65.579  0 39  GLN JJJ C   1 ? 37 
ATOM   12046 O O   . GLN J  2 39  ? 24.660  -95.747  29.021  1.000 66.212  0 39  GLN JJJ O   1 ? 37 
ATOM   12047 C CB  . GLN J  2 39  ? 23.627  -93.676  30.842  1.000 64.750  0 39  GLN JJJ CB  1 ? 37 
ATOM   12048 C CG  . GLN J  2 39  ? 22.161  -93.783  30.473  1.000 69.832  0 39  GLN JJJ CG  1 ? 37 
ATOM   12049 C CD  . GLN J  2 39  ? 21.520  -92.423  30.408  1.000 71.742  0 39  GLN JJJ CD  1 ? 37 
ATOM   12050 O OE1 . GLN J  2 39  ? 22.157  -91.426  30.051  1.000 74.303  0 39  GLN JJJ OE1 1 ? 37 
ATOM   12051 N NE2 . GLN J  2 39  ? 20.243  -92.380  30.738  1.000 73.789  0 39  GLN JJJ NE2 1 ? 37 
ATOM   12052 N N   . ALA J  2 40  ? 23.527  -97.185  30.399  1.000 68.376  0 40  ALA JJJ N   1 ? 37 
ATOM   12053 C CA  . ALA J  2 40  ? 23.133  -98.210  29.415  1.000 71.104  0 40  ALA JJJ CA  1 ? 37 
ATOM   12054 C C   . ALA J  2 40  ? 21.834  -97.745  28.775  1.000 73.152  0 40  ALA JJJ C   1 ? 37 
ATOM   12055 O O   . ALA J  2 40  ? 21.052  -97.026  29.397  1.000 72.451  0 40  ALA JJJ O   1 ? 37 
ATOM   12056 C CB  . ALA J  2 40  ? 22.984  -99.541  30.100  1.000 72.840  0 40  ALA JJJ CB  1 ? 37 
ATOM   12057 N N   . PRO J  2 41  ? 21.573  -98.103  27.501  1.000 77.167  0 41  PRO JJJ N   1 ? 37 
ATOM   12058 C CA  . PRO J  2 41  ? 20.297  -97.743  26.869  1.000 79.051  0 41  PRO JJJ CA  1 ? 37 
ATOM   12059 C C   . PRO J  2 41  ? 19.115  -98.369  27.643  1.000 79.953  0 41  PRO JJJ C   1 ? 37 
ATOM   12060 O O   . PRO J  2 41  ? 19.181  -99.519  28.033  1.000 77.039  0 41  PRO JJJ O   1 ? 37 
ATOM   12061 C CB  . PRO J  2 41  ? 20.413  -98.244  25.424  1.000 81.641  0 41  PRO JJJ CB  1 ? 37 
ATOM   12062 C CG  . PRO J  2 41  ? 21.627  -99.196  25.415  1.000 81.002  0 41  PRO JJJ CG  1 ? 37 
ATOM   12063 C CD  . PRO J  2 41  ? 22.476  -98.881  26.635  1.000 77.950  0 41  PRO JJJ CD  1 ? 37 
ATOM   12064 N N   . GLY J  2 42  ? 18.094  -97.566  27.917  1.000 81.988  0 42  GLY JJJ N   1 ? 37 
ATOM   12065 C CA  . GLY J  2 42  ? 16.903  -97.982  28.680  1.000 86.904  0 42  GLY JJJ CA  1 ? 37 
ATOM   12066 C C   . GLY J  2 42  ? 17.067  -97.809  30.177  1.000 87.731  0 42  GLY JJJ C   1 ? 37 
ATOM   12067 O O   . GLY J  2 42  ? 16.054  -97.970  30.869  1.000 91.524  0 42  GLY JJJ O   1 ? 37 
ATOM   12068 N N   . LYS J  2 43  ? 18.262  -97.464  30.671  1.000 87.209  0 43  LYS JJJ N   1 ? 37 
ATOM   12069 C CA  . LYS J  2 43  ? 18.532  -97.303  32.125  1.000 87.087  0 43  LYS JJJ CA  1 ? 37 
ATOM   12070 C C   . LYS J  2 43  ? 18.805  -95.843  32.456  1.000 84.521  0 43  LYS JJJ C   1 ? 37 
ATOM   12071 O O   . LYS J  2 43  ? 19.107  -95.080  31.543  1.000 84.914  0 43  LYS JJJ O   1 ? 37 
ATOM   12072 C CB  . LYS J  2 43  ? 19.710  -98.185  32.556  1.000 88.450  0 43  LYS JJJ CB  1 ? 37 
ATOM   12073 C CG  . LYS J  2 43  ? 19.270  -99.577  32.968  1.000 93.119  0 43  LYS JJJ CG  1 ? 37 
ATOM   12074 C CD  . LYS J  2 43  ? 20.319  -100.663 32.884  1.000 95.202  0 43  LYS JJJ CD  1 ? 37 
ATOM   12075 C CE  . LYS J  2 43  ? 19.752  -101.927 33.507  1.000 101.574 0 43  LYS JJJ CE  1 ? 37 
ATOM   12076 N NZ  . LYS J  2 43  ? 19.861  -103.135 32.645  1.000 104.421 0 43  LYS JJJ NZ  1 ? 37 
ATOM   12077 N N   . GLU J  2 44  ? 18.802  -95.526  33.743  1.000 85.159  0 44  GLU JJJ N   1 ? 37 
ATOM   12078 C CA  . GLU J  2 44  ? 19.153  -94.186  34.265  1.000 82.893  0 44  GLU JJJ CA  1 ? 37 
ATOM   12079 C C   . GLU J  2 44  ? 20.680  -94.131  34.385  1.000 78.610  0 44  GLU JJJ C   1 ? 37 
ATOM   12080 O O   . GLU J  2 44  ? 21.323  -95.190  34.283  1.000 76.963  0 44  GLU JJJ O   1 ? 37 
ATOM   12081 C CB  . GLU J  2 44  ? 18.505  -93.940  35.633  1.000 85.736  0 44  GLU JJJ CB  1 ? 37 
ATOM   12082 C CG  . GLU J  2 44  ? 17.030  -94.305  35.717  1.000 91.536  0 44  GLU JJJ CG  1 ? 37 
ATOM   12083 C CD  . GLU J  2 44  ? 16.131  -93.557  34.750  1.000 95.684  0 44  GLU JJJ CD  1 ? 37 
ATOM   12084 O OE1 . GLU J  2 44  ? 16.407  -92.352  34.510  1.000 94.277  0 44  GLU JJJ OE1 1 ? 37 
ATOM   12085 O OE2 . GLU J  2 44  ? 15.147  -94.180  34.242  1.000 99.913  0 44  GLU JJJ OE2 1 ? 37 
ATOM   12086 N N   . ARG J  2 45  ? 21.221  -92.927  34.576  1.000 76.330  0 45  ARG JJJ N   1 ? 37 
ATOM   12087 C CA  . ARG J  2 45  ? 22.637  -92.709  34.939  1.000 75.103  0 45  ARG JJJ CA  1 ? 37 
ATOM   12088 C C   . ARG J  2 45  ? 22.925  -93.425  36.260  1.000 74.601  0 45  ARG JJJ C   1 ? 37 
ATOM   12089 O O   . ARG J  2 45  ? 22.241  -93.152  37.250  1.000 79.716  0 45  ARG JJJ O   1 ? 37 
ATOM   12090 C CB  . ARG J  2 45  ? 22.955  -91.220  35.048  1.000 74.439  0 45  ARG JJJ CB  1 ? 37 
ATOM   12091 C CG  . ARG J  2 45  ? 23.546  -90.685  33.757  1.000 74.165  0 45  ARG JJJ CG  1 ? 37 
ATOM   12092 C CD  . ARG J  2 45  ? 23.564  -89.186  33.671  1.000 73.635  0 45  ARG JJJ CD  1 ? 37 
ATOM   12093 N NE  . ARG J  2 45  ? 23.292  -88.779  32.290  1.000 76.378  0 45  ARG JJJ NE  1 ? 37 
ATOM   12094 C CZ  . ARG J  2 45  ? 23.728  -87.656  31.729  1.000 75.396  0 45  ARG JJJ CZ  1 ? 37 
ATOM   12095 N NH1 . ARG J  2 45  ? 24.491  -86.799  32.414  1.000 73.945  0 45  ARG JJJ NH1 1 ? 37 
ATOM   12096 N NH2 . ARG J  2 45  ? 23.379  -87.399  30.479  1.000 73.094  0 45  ARG JJJ NH2 1 ? 37 
ATOM   12097 N N   . GLU J  2 46  ? 23.920  -94.298  36.243  1.000 68.838  0 46  GLU JJJ N   1 ? 37 
ATOM   12098 C CA  . GLU J  2 46  ? 24.398  -95.086  37.399  1.000 66.512  0 46  GLU JJJ CA  1 ? 37 
ATOM   12099 C C   . GLU J  2 46  ? 25.747  -94.490  37.834  1.000 61.264  0 46  GLU JJJ C   1 ? 37 
ATOM   12100 O O   . GLU J  2 46  ? 26.619  -94.265  36.963  1.000 59.693  0 46  GLU JJJ O   1 ? 37 
ATOM   12101 C CB  . GLU J  2 46  ? 24.403  -96.540  36.930  1.000 69.155  0 46  GLU JJJ CB  1 ? 37 
ATOM   12102 C CG  . GLU J  2 46  ? 25.021  -97.540  37.875  1.000 72.193  0 46  GLU JJJ CG  1 ? 37 
ATOM   12103 C CD  . GLU J  2 46  ? 25.029  -98.974  37.351  1.000 76.363  0 46  GLU JJJ CD  1 ? 37 
ATOM   12104 O OE1 . GLU J  2 46  ? 24.555  -99.234  36.218  1.000 80.079  0 46  GLU JJJ OE1 1 ? 37 
ATOM   12105 O OE2 . GLU J  2 46  ? 25.558  -99.841  38.051  1.000 78.208  0 46  GLU JJJ OE2 1 ? 37 
ATOM   12106 N N   . PHE J  2 47  ? 25.911  -94.202  39.124  1.000 58.014  0 47  PHE JJJ N   1 ? 37 
ATOM   12107 C CA  . PHE J  2 47  ? 27.203  -93.759  39.715  1.000 54.761  0 47  PHE JJJ CA  1 ? 37 
ATOM   12108 C C   . PHE J  2 47  ? 28.229  -94.882  39.550  1.000 54.029  0 47  PHE JJJ C   1 ? 37 
ATOM   12109 O O   . PHE J  2 47  ? 27.899  -96.021  39.888  1.000 55.492  0 47  PHE JJJ O   1 ? 37 
ATOM   12110 C CB  . PHE J  2 47  ? 27.066  -93.355  41.191  1.000 54.349  0 47  PHE JJJ CB  1 ? 37 
ATOM   12111 C CG  . PHE J  2 47  ? 28.383  -93.065  41.866  1.000 52.183  0 47  PHE JJJ CG  1 ? 37 
ATOM   12112 C CD1 . PHE J  2 47  ? 28.978  -91.829  41.730  1.000 50.217  0 47  PHE JJJ CD1 1 ? 37 
ATOM   12113 C CD2 . PHE J  2 47  ? 29.037  -94.024  42.626  1.000 53.906  0 47  PHE JJJ CD2 1 ? 37 
ATOM   12114 C CE1 . PHE J  2 47  ? 30.199  -91.557  42.324  1.000 49.440  0 47  PHE JJJ CE1 1 ? 37 
ATOM   12115 C CE2 . PHE J  2 47  ? 30.246  -93.752  43.240  1.000 53.230  0 47  PHE JJJ CE2 1 ? 37 
ATOM   12116 C CZ  . PHE J  2 47  ? 30.826  -92.513  43.084  1.000 51.510  0 47  PHE JJJ CZ  1 ? 37 
ATOM   12117 N N   . VAL J  2 48  ? 29.440  -94.556  39.105  1.000 52.036  0 48  VAL JJJ N   1 ? 37 
ATOM   12118 C CA  . VAL J  2 48  ? 30.541  -95.548  38.942  1.000 53.410  0 48  VAL JJJ CA  1 ? 37 
ATOM   12119 C C   . VAL J  2 48  ? 31.637  -95.275  39.980  1.000 52.114  0 48  VAL JJJ C   1 ? 37 
ATOM   12120 O O   . VAL J  2 48  ? 32.005  -96.221  40.706  1.000 53.331  0 48  VAL JJJ O   1 ? 37 
ATOM   12121 C CB  . VAL J  2 48  ? 31.091  -95.554  37.499  1.000 52.185  0 48  VAL JJJ CB  1 ? 37 
ATOM   12122 C CG1 . VAL J  2 48  ? 32.319  -96.463  37.349  1.000 51.821  0 48  VAL JJJ CG1 1 ? 37 
ATOM   12123 C CG2 . VAL J  2 48  ? 30.003  -95.956  36.508  1.000 54.400  0 48  VAL JJJ CG2 1 ? 37 
ATOM   12124 N N   . ALA J  2 49  ? 32.170  -94.055  40.019  1.000 50.542  0 49  ALA JJJ N   1 ? 37 
ATOM   12125 C CA  . ALA J  2 49  ? 33.319  -93.701  40.892  1.000 51.408  0 49  ALA JJJ CA  1 ? 37 
ATOM   12126 C C   . ALA J  2 49  ? 33.466  -92.180  41.046  1.000 48.624  0 49  ALA JJJ C   1 ? 37 
ATOM   12127 O O   . ALA J  2 49  ? 33.022  -91.415  40.180  1.000 44.536  0 49  ALA JJJ O   1 ? 37 
ATOM   12128 C CB  . ALA J  2 49  ? 34.607  -94.316  40.354  1.000 51.540  0 49  ALA JJJ CB  1 ? 37 
ATOM   12129 N N   . ALA J  2 50  ? 34.103  -91.775  42.140  1.000 50.911  0 50  ALA JJJ N   1 ? 37 
ATOM   12130 C CA  . ALA J  2 50  ? 34.431  -90.367  42.444  1.000 49.188  0 50  ALA JJJ CA  1 ? 37 
ATOM   12131 C C   . ALA J  2 50  ? 35.721  -90.297  43.257  1.000 48.031  0 50  ALA JJJ C   1 ? 37 
ATOM   12132 O O   . ALA J  2 50  ? 36.022  -91.259  43.995  1.000 49.879  0 50  ALA JJJ O   1 ? 37 
ATOM   12133 C CB  . ALA J  2 50  ? 33.270  -89.717  43.160  1.000 50.697  0 50  ALA JJJ CB  1 ? 37 
ATOM   12134 N N   . ILE J  2 51  ? 36.417  -89.173  43.133  1.000 46.577  0 51  ILE JJJ N   1 ? 37 
ATOM   12135 C CA  . ILE J  2 51  ? 37.720  -88.924  43.806  1.000 49.078  0 51  ILE JJJ CA  1 ? 37 
ATOM   12136 C C   . ILE J  2 51  ? 37.738  -87.479  44.327  1.000 48.470  0 51  ILE JJJ C   1 ? 37 
ATOM   12137 O O   . ILE J  2 51  ? 37.446  -86.532  43.556  1.000 45.643  0 51  ILE JJJ O   1 ? 37 
ATOM   12138 C CB  . ILE J  2 51  ? 38.888  -89.258  42.854  1.000 48.859  0 51  ILE JJJ CB  1 ? 37 
ATOM   12139 C CG1 . ILE J  2 51  ? 40.243  -89.191  43.561  1.000 50.989  0 51  ILE JJJ CG1 1 ? 37 
ATOM   12140 C CG2 . ILE J  2 51  ? 38.859  -88.374  41.615  1.000 47.778  0 51  ILE JJJ CG2 1 ? 37 
ATOM   12141 C CD1 . ILE J  2 51  ? 41.368  -89.797  42.769  1.000 51.879  0 51  ILE JJJ CD1 1 ? 37 
ATOM   12142 N N   . SER J  2 52  ? 38.066  -87.323  45.607  1.000 49.356  0 52  SER JJJ N   1 ? 37 
ATOM   12143 C CA  . SER J  2 52  ? 38.138  -86.009  46.285  1.000 49.787  0 52  SER JJJ CA  1 ? 37 
ATOM   12144 C C   . SER J  2 52  ? 39.421  -85.290  45.846  1.000 50.128  0 52  SER JJJ C   1 ? 37 
ATOM   12145 O O   . SER J  2 52  ? 40.228  -85.880  45.079  1.000 49.766  0 52  SER JJJ O   1 ? 37 
ATOM   12146 C CB  . SER J  2 52  ? 38.044  -86.148  47.763  1.000 51.829  0 52  SER JJJ CB  1 ? 37 
ATOM   12147 O OG  . SER J  2 52  ? 37.622  -84.933  48.326  1.000 52.914  0 52  SER JJJ OG  1 ? 37 
ATOM   12148 N N   . TRP J  2 53  ? 39.580  -84.046  46.298  1.000 48.873  0 53  TRP JJJ N   1 ? 37 
ATOM   12149 C CA  . TRP J  2 53  ? 40.640  -83.098  45.857  1.000 47.863  0 53  TRP JJJ CA  1 ? 37 
ATOM   12150 C C   . TRP J  2 53  ? 42.021  -83.741  46.069  1.000 49.723  0 53  TRP JJJ C   1 ? 37 
ATOM   12151 O O   . TRP J  2 53  ? 42.793  -83.794  45.106  1.000 49.248  0 53  TRP JJJ O   1 ? 37 
ATOM   12152 C CB  . TRP J  2 53  ? 40.507  -81.761  46.595  1.000 46.074  0 53  TRP JJJ CB  1 ? 37 
ATOM   12153 C CG  . TRP J  2 53  ? 39.109  -81.228  46.635  1.000 45.077  0 53  TRP JJJ CG  1 ? 37 
ATOM   12154 C CD1 . TRP J  2 53  ? 38.434  -80.623  45.606  1.000 43.969  0 53  TRP JJJ CD1 1 ? 37 
ATOM   12155 C CD2 . TRP J  2 53  ? 38.190  -81.276  47.747  1.000 45.787  0 53  TRP JJJ CD2 1 ? 37 
ATOM   12156 N NE1 . TRP J  2 53  ? 37.172  -80.281  46.003  1.000 44.330  0 53  TRP JJJ NE1 1 ? 37 
ATOM   12157 C CE2 . TRP J  2 53  ? 36.983  -80.684  47.305  1.000 44.859  0 53  TRP JJJ CE2 1 ? 37 
ATOM   12158 C CE3 . TRP J  2 53  ? 38.243  -81.805  49.037  1.000 46.819  0 53  TRP JJJ CE3 1 ? 37 
ATOM   12159 C CZ2 . TRP J  2 53  ? 35.855  -80.590  48.119  1.000 44.559  0 53  TRP JJJ CZ2 1 ? 37 
ATOM   12160 C CZ3 . TRP J  2 53  ? 37.147  -81.670  49.856  1.000 47.783  0 53  TRP JJJ CZ3 1 ? 37 
ATOM   12161 C CH2 . TRP J  2 53  ? 35.969  -81.080  49.397  1.000 47.123  0 53  TRP JJJ CH2 1 ? 37 
ATOM   12162 N N   . SER J  2 54  ? 42.279  -84.254  47.273  1.000 50.520  0 54  SER JJJ N   1 ? 37 
ATOM   12163 C CA  . SER J  2 54  ? 43.564  -84.847  47.709  1.000 53.639  0 54  SER JJJ CA  1 ? 37 
ATOM   12164 C C   . SER J  2 54  ? 43.781  -86.230  47.095  1.000 55.126  0 54  SER JJJ C   1 ? 37 
ATOM   12165 O O   . SER J  2 54  ? 44.844  -86.816  47.368  1.000 55.957  0 54  SER JJJ O   1 ? 37 
ATOM   12166 C CB  . SER J  2 54  ? 43.607  -84.972  49.199  1.000 54.708  0 54  SER JJJ CB  1 ? 37 
ATOM   12167 O OG  . SER J  2 54  ? 42.666  -85.940  49.610  1.000 55.383  0 54  SER JJJ OG  1 ? 37 
ATOM   12168 N N   . SER J  2 55  ? 42.776  -86.768  46.396  1.000 55.335  0 55  SER JJJ N   1 ? 37 
ATOM   12169 C CA  . SER J  2 55  ? 42.695  -88.185  45.952  1.000 57.845  0 55  SER JJJ CA  1 ? 37 
ATOM   12170 C C   . SER J  2 55  ? 42.193  -89.115  47.063  1.000 60.284  0 55  SER JJJ C   1 ? 37 
ATOM   12171 O O   . SER J  2 55  ? 42.059  -90.296  46.759  1.000 61.831  0 55  SER JJJ O   1 ? 37 
ATOM   12172 C CB  . SER J  2 55  ? 44.022  -88.707  45.405  1.000 59.237  0 55  SER JJJ CB  1 ? 37 
ATOM   12173 O OG  . SER J  2 55  ? 44.452  -87.954  44.273  1.000 60.028  0 55  SER JJJ OG  1 ? 37 
ATOM   12174 N N   . THR J  2 56  ? 41.910  -88.640  48.279  1.000 64.183  0 56  THR JJJ N   1 ? 37 
ATOM   12175 C CA  . THR J  2 56  ? 42.097  -89.497  49.485  1.000 74.260  0 56  THR JJJ CA  1 ? 37 
ATOM   12176 C C   . THR J  2 56  ? 40.829  -90.183  49.954  1.000 76.451  0 56  THR JJJ C   1 ? 37 
ATOM   12177 O O   . THR J  2 56  ? 40.958  -91.245  50.576  1.000 85.852  0 56  THR JJJ O   1 ? 37 
ATOM   12178 C CB  . THR J  2 56  ? 42.702  -88.776  50.691  1.000 80.904  0 56  THR JJJ CB  1 ? 37 
ATOM   12179 O OG1 . THR J  2 56  ? 44.108  -88.912  50.478  1.000 87.308  0 56  THR JJJ OG1 1 ? 37 
ATOM   12180 C CG2 . THR J  2 56  ? 42.308  -89.354  52.038  1.000 83.395  0 56  THR JJJ CG2 1 ? 37 
ATOM   12181 N N   . PRO J  2 57  ? 39.620  -89.573  49.861  1.000 65.598  0 57  PRO JJJ N   1 ? 37 
ATOM   12182 C CA  . PRO J  2 57  ? 38.414  -90.396  49.774  1.000 60.896  0 57  PRO JJJ CA  1 ? 37 
ATOM   12183 C C   . PRO J  2 57  ? 38.232  -90.665  48.269  1.000 57.661  0 57  PRO JJJ C   1 ? 37 
ATOM   12184 O O   . PRO J  2 57  ? 38.213  -89.740  47.484  1.000 53.429  0 57  PRO JJJ O   1 ? 37 
ATOM   12185 C CB  . PRO J  2 57  ? 37.336  -89.581  50.490  1.000 60.639  0 57  PRO JJJ CB  1 ? 37 
ATOM   12186 C CG  . PRO J  2 57  ? 38.006  -88.228  50.796  1.000 62.569  0 57  PRO JJJ CG  1 ? 37 
ATOM   12187 C CD  . PRO J  2 57  ? 39.343  -88.149  50.068  1.000 61.951  0 57  PRO JJJ CD  1 ? 37 
ATOM   12188 N N   . THR J  2 58  ? 38.231  -91.939  47.884  1.000 56.412  0 58  THR JJJ N   1 ? 37 
ATOM   12189 C CA  . THR J  2 58  ? 37.665  -92.442  46.608  1.000 53.900  0 58  THR JJJ CA  1 ? 37 
ATOM   12190 C C   . THR J  2 58  ? 36.373  -93.186  46.921  1.000 54.818  0 58  THR JJJ C   1 ? 37 
ATOM   12191 O O   . THR J  2 58  ? 36.227  -93.666  48.025  1.000 56.989  0 58  THR JJJ O   1 ? 37 
ATOM   12192 C CB  . THR J  2 58  ? 38.614  -93.337  45.801  1.000 52.691  0 58  THR JJJ CB  1 ? 37 
ATOM   12193 O OG1 . THR J  2 58  ? 38.978  -94.479  46.567  1.000 53.224  0 58  THR JJJ OG1 1 ? 37 
ATOM   12194 C CG2 . THR J  2 58  ? 39.837  -92.592  45.311  1.000 51.630  0 58  THR JJJ CG2 1 ? 37 
ATOM   12195 N N   . TYR J  2 59  ? 35.452  -93.219  45.966  1.000 55.199  0 59  TYR JJJ N   1 ? 37 
ATOM   12196 C CA  . TYR J  2 59  ? 34.132  -93.872  46.110  1.000 56.122  0 59  TYR JJJ CA  1 ? 37 
ATOM   12197 C C   . TYR J  2 59  ? 33.863  -94.696  44.847  1.000 54.570  0 59  TYR JJJ C   1 ? 37 
ATOM   12198 O O   . TYR J  2 59  ? 34.296  -94.275  43.749  1.000 52.174  0 59  TYR JJJ O   1 ? 37 
ATOM   12199 C CB  . TYR J  2 59  ? 33.026  -92.830  46.287  1.000 57.198  0 59  TYR JJJ CB  1 ? 37 
ATOM   12200 C CG  . TYR J  2 59  ? 33.186  -91.820  47.401  1.000 58.768  0 59  TYR JJJ CG  1 ? 37 
ATOM   12201 C CD1 . TYR J  2 59  ? 33.768  -90.579  47.174  1.000 57.710  0 59  TYR JJJ CD1 1 ? 37 
ATOM   12202 C CD2 . TYR J  2 59  ? 32.643  -92.057  48.653  1.000 62.526  0 59  TYR JJJ CD2 1 ? 37 
ATOM   12203 C CE1 . TYR J  2 59  ? 33.871  -89.630  48.188  1.000 58.719  0 59  TYR JJJ CE1 1 ? 37 
ATOM   12204 C CE2 . TYR J  2 59  ? 32.747  -91.125  49.675  1.000 63.766  0 59  TYR JJJ CE2 1 ? 37 
ATOM   12205 C CZ  . TYR J  2 59  ? 33.346  -89.896  49.441  1.000 61.753  0 59  TYR JJJ CZ  1 ? 37 
ATOM   12206 O OH  . TYR J  2 59  ? 33.431  -88.983  50.455  1.000 62.792  0 59  TYR JJJ OH  1 ? 37 
ATOM   12207 N N   . TYR J  2 60  ? 33.149  -95.808  45.005  1.000 56.407  0 60  TYR JJJ N   1 ? 37 
ATOM   12208 C CA  . TYR J  2 60  ? 32.857  -96.785  43.924  1.000 56.961  0 60  TYR JJJ CA  1 ? 37 
ATOM   12209 C C   . TYR J  2 60  ? 31.421  -97.288  44.051  1.000 57.299  0 60  TYR JJJ C   1 ? 37 
ATOM   12210 O O   . TYR J  2 60  ? 30.964  -97.548  45.171  1.000 56.109  0 60  TYR JJJ O   1 ? 37 
ATOM   12211 C CB  . TYR J  2 60  ? 33.863  -97.932  43.992  1.000 58.218  0 60  TYR JJJ CB  1 ? 37 
ATOM   12212 C CG  . TYR J  2 60  ? 35.281  -97.499  43.728  1.000 56.908  0 60  TYR JJJ CG  1 ? 37 
ATOM   12213 C CD1 . TYR J  2 60  ? 35.686  -97.227  42.435  1.000 55.013  0 60  TYR JJJ CD1 1 ? 37 
ATOM   12214 C CD2 . TYR J  2 60  ? 36.201  -97.330  44.753  1.000 56.444  0 60  TYR JJJ CD2 1 ? 37 
ATOM   12215 C CE1 . TYR J  2 60  ? 36.991  -96.853  42.153  1.000 54.003  0 60  TYR JJJ CE1 1 ? 37 
ATOM   12216 C CE2 . TYR J  2 60  ? 37.505  -96.969  44.484  1.000 55.827  0 60  TYR JJJ CE2 1 ? 37 
ATOM   12217 C CZ  . TYR J  2 60  ? 37.896  -96.712  43.181  1.000 54.912  0 60  TYR JJJ CZ  1 ? 37 
ATOM   12218 O OH  . TYR J  2 60  ? 39.163  -96.310  42.892  1.000 55.962  0 60  TYR JJJ OH  1 ? 37 
ATOM   12219 N N   . GLY J  2 61  ? 30.740  -97.431  42.915  1.000 58.382  0 61  GLY JJJ N   1 ? 37 
ATOM   12220 C CA  . GLY J  2 61  ? 29.457  -98.150  42.831  1.000 60.683  0 61  GLY JJJ CA  1 ? 37 
ATOM   12221 C C   . GLY J  2 61  ? 29.663  -99.619  43.150  1.000 64.204  0 61  GLY JJJ C   1 ? 37 
ATOM   12222 O O   . GLY J  2 61  ? 30.794  -100.158 42.909  1.000 63.973  0 61  GLY JJJ O   1 ? 37 
ATOM   12223 N N   . GLU J  2 62  ? 28.632  -100.254 43.695  1.000 68.063  0 62  GLU JJJ N   1 ? 37 
ATOM   12224 C CA  . GLU J  2 62  ? 28.803  -101.596 44.300  1.000 73.010  0 62  GLU JJJ CA  1 ? 37 
ATOM   12225 C C   . GLU J  2 62  ? 29.256  -102.585 43.223  1.000 71.491  0 62  GLU JJJ C   1 ? 37 
ATOM   12226 O O   . GLU J  2 62  ? 30.128  -103.406 43.510  1.000 71.520  0 62  GLU JJJ O   1 ? 37 
ATOM   12227 C CB  . GLU J  2 62  ? 27.585  -102.004 45.125  1.000 77.950  0 62  GLU JJJ CB  1 ? 37 
ATOM   12228 C CG  . GLU J  2 62  ? 27.896  -103.136 46.102  1.000 84.125  0 62  GLU JJJ CG  1 ? 37 
ATOM   12229 C CD  . GLU J  2 62  ? 29.207  -103.036 46.887  1.000 85.851  0 62  GLU JJJ CD  1 ? 37 
ATOM   12230 O OE1 . GLU J  2 62  ? 29.579  -101.915 47.261  1.000 86.753  0 62  GLU JJJ OE1 1 ? 37 
ATOM   12231 O OE2 . GLU J  2 62  ? 29.890  -104.063 47.057  1.000 89.588  0 62  GLU JJJ OE2 1 ? 37 
ATOM   12232 N N   . SER J  2 63  ? 28.765  -102.451 42.001  1.000 70.594  0 63  SER JJJ N   1 ? 37 
ATOM   12233 C CA  . SER J  2 63  ? 28.941  -103.456 40.925  1.000 73.915  0 63  SER JJJ CA  1 ? 37 
ATOM   12234 C C   . SER J  2 63  ? 30.319  -103.323 40.261  1.000 72.271  0 63  SER JJJ C   1 ? 37 
ATOM   12235 O O   . SER J  2 63  ? 30.679  -104.229 39.511  1.000 75.077  0 63  SER JJJ O   1 ? 37 
ATOM   12236 C CB  . SER J  2 63  ? 27.826  -103.372 39.920  1.000 74.022  0 63  SER JJJ CB  1 ? 37 
ATOM   12237 O OG  . SER J  2 63  ? 27.824  -102.093 39.308  1.000 72.718  0 63  SER JJJ OG  1 ? 37 
ATOM   12238 N N   . VAL J  2 64  ? 31.077  -102.264 40.528  1.000 68.921  0 64  VAL JJJ N   1 ? 37 
ATOM   12239 C CA  . VAL J  2 64  ? 32.434  -102.106 39.931  1.000 68.486  0 64  VAL JJJ CA  1 ? 37 
ATOM   12240 C C   . VAL J  2 64  ? 33.507  -102.192 41.012  1.000 70.407  0 64  VAL JJJ C   1 ? 37 
ATOM   12241 O O   . VAL J  2 64  ? 34.674  -102.305 40.642  1.000 69.814  0 64  VAL JJJ O   1 ? 37 
ATOM   12242 C CB  . VAL J  2 64  ? 32.562  -100.789 39.139  1.000 65.121  0 64  VAL JJJ CB  1 ? 37 
ATOM   12243 C CG1 . VAL J  2 64  ? 31.519  -100.710 38.031  1.000 63.367  0 64  VAL JJJ CG1 1 ? 37 
ATOM   12244 C CG2 . VAL J  2 64  ? 32.532  -99.547  40.033  1.000 63.575  0 64  VAL JJJ CG2 1 ? 37 
ATOM   12245 N N   . LYS J  2 65  ? 33.132  -102.134 42.290  1.000 74.180  0 65  LYS JJJ N   1 ? 37 
ATOM   12246 C CA  . LYS J  2 65  ? 34.088  -102.212 43.432  1.000 75.286  0 65  LYS JJJ CA  1 ? 37 
ATOM   12247 C C   . LYS J  2 65  ? 35.006  -103.423 43.213  1.000 74.181  0 65  LYS JJJ C   1 ? 37 
ATOM   12248 O O   . LYS J  2 65  ? 34.486  -104.503 42.897  1.000 76.755  0 65  LYS JJJ O   1 ? 37 
ATOM   12249 C CB  . LYS J  2 65  ? 33.351  -102.269 44.773  1.000 79.791  0 65  LYS JJJ CB  1 ? 37 
ATOM   12250 C CG  . LYS J  2 65  ? 34.000  -101.402 45.840  1.000 82.914  0 65  LYS JJJ CG  1 ? 37 
ATOM   12251 C CD  . LYS J  2 65  ? 33.236  -101.317 47.136  1.000 87.588  0 65  LYS JJJ CD  1 ? 37 
ATOM   12252 C CE  . LYS J  2 65  ? 34.101  -100.814 48.276  1.000 90.225  0 65  LYS JJJ CE  1 ? 37 
ATOM   12253 N NZ  . LYS J  2 65  ? 34.003  -101.656 49.508  1.000 95.092  0 65  LYS JJJ NZ  1 ? 37 
ATOM   12254 N N   . GLY J  2 66  ? 36.321  -103.225 43.300  1.000 71.463  0 66  GLY JJJ N   1 ? 37 
ATOM   12255 C CA  . GLY J  2 66  ? 37.331  -104.290 43.132  1.000 74.272  0 66  GLY JJJ CA  1 ? 37 
ATOM   12256 C C   . GLY J  2 66  ? 37.888  -104.342 41.722  1.000 71.675  0 66  GLY JJJ C   1 ? 37 
ATOM   12257 O O   . GLY J  2 66  ? 39.045  -104.745 41.566  1.000 73.389  0 66  GLY JJJ O   1 ? 37 
ATOM   12258 N N   . ARG J  2 67  ? 37.098  -103.979 40.713  1.000 69.121  0 67  ARG JJJ N   1 ? 37 
ATOM   12259 C CA  . ARG J  2 67  ? 37.483  -104.108 39.280  1.000 67.313  0 67  ARG JJJ CA  1 ? 37 
ATOM   12260 C C   . ARG J  2 67  ? 37.987  -102.767 38.732  1.000 64.268  0 67  ARG JJJ C   1 ? 37 
ATOM   12261 O O   . ARG J  2 67  ? 38.829  -102.801 37.820  1.000 62.761  0 67  ARG JJJ O   1 ? 37 
ATOM   12262 C CB  . ARG J  2 67  ? 36.294  -104.638 38.467  1.000 67.144  0 67  ARG JJJ CB  1 ? 37 
ATOM   12263 C CG  . ARG J  2 67  ? 35.823  -106.016 38.904  1.000 70.558  0 67  ARG JJJ CG  1 ? 37 
ATOM   12264 C CD  . ARG J  2 67  ? 34.779  -106.606 37.992  1.000 71.166  0 67  ARG JJJ CD  1 ? 37 
ATOM   12265 N NE  . ARG J  2 67  ? 33.589  -105.781 37.912  1.000 68.858  0 67  ARG JJJ NE  1 ? 37 
ATOM   12266 C CZ  . ARG J  2 67  ? 33.139  -105.202 36.807  1.000 67.126  0 67  ARG JJJ CZ  1 ? 37 
ATOM   12267 N NH1 . ARG J  2 67  ? 33.780  -105.355 35.656  1.000 67.088  0 67  ARG JJJ NH1 1 ? 37 
ATOM   12268 N NH2 . ARG J  2 67  ? 32.059  -104.438 36.859  1.000 65.608  0 67  ARG JJJ NH2 1 ? 37 
ATOM   12269 N N   . PHE J  2 68  ? 37.455  -101.643 39.216  1.000 63.868  0 68  PHE JJJ N   1 ? 37 
ATOM   12270 C CA  . PHE J  2 68  ? 37.702  -100.289 38.649  1.000 63.872  0 68  PHE JJJ CA  1 ? 37 
ATOM   12271 C C   . PHE J  2 68  ? 38.504  -99.455  39.659  1.000 63.756  0 68  PHE JJJ C   1 ? 37 
ATOM   12272 O O   . PHE J  2 68  ? 38.247  -99.541  40.867  1.000 64.859  0 68  PHE JJJ O   1 ? 37 
ATOM   12273 C CB  . PHE J  2 68  ? 36.379  -99.583  38.309  1.000 63.309  0 68  PHE JJJ CB  1 ? 37 
ATOM   12274 C CG  . PHE J  2 68  ? 35.586  -100.120 37.142  1.000 63.183  0 68  PHE JJJ CG  1 ? 37 
ATOM   12275 C CD1 . PHE J  2 68  ? 35.878  -101.332 36.542  1.000 65.229  0 68  PHE JJJ CD1 1 ? 37 
ATOM   12276 C CD2 . PHE J  2 68  ? 34.503  -99.404  36.661  1.000 63.832  0 68  PHE JJJ CD2 1 ? 37 
ATOM   12277 C CE1 . PHE J  2 68  ? 35.116  -101.811 35.486  1.000 65.979  0 68  PHE JJJ CE1 1 ? 37 
ATOM   12278 C CE2 . PHE J  2 68  ? 33.741  -99.880  35.598  1.000 65.040  0 68  PHE JJJ CE2 1 ? 37 
ATOM   12279 C CZ  . PHE J  2 68  ? 34.041  -101.094 35.015  1.000 65.220  0 68  PHE JJJ CZ  1 ? 37 
ATOM   12280 N N   . THR J  2 69  ? 39.447  -98.650  39.168  1.000 61.424  0 69  THR JJJ N   1 ? 37 
ATOM   12281 C CA  . THR J  2 69  ? 40.247  -97.717  39.993  1.000 60.172  0 69  THR JJJ CA  1 ? 37 
ATOM   12282 C C   . THR J  2 69  ? 40.135  -96.319  39.389  1.000 57.929  0 69  THR JJJ C   1 ? 37 
ATOM   12283 O O   . THR J  2 69  ? 40.449  -96.160  38.197  1.000 56.430  0 69  THR JJJ O   1 ? 37 
ATOM   12284 C CB  . THR J  2 69  ? 41.707  -98.171  40.079  1.000 60.833  0 69  THR JJJ CB  1 ? 37 
ATOM   12285 O OG1 . THR J  2 69  ? 41.714  -99.504  40.595  1.000 63.902  0 69  THR JJJ OG1 1 ? 37 
ATOM   12286 C CG2 . THR J  2 69  ? 42.543  -97.268  40.956  1.000 58.961  0 69  THR JJJ CG2 1 ? 37 
ATOM   12287 N N   . ILE J  2 70  ? 39.678  -95.357  40.181  1.000 57.442  0 70  ILE JJJ N   1 ? 37 
ATOM   12288 C CA  . ILE J  2 70  ? 39.677  -93.918  39.794  1.000 55.944  0 70  ILE JJJ CA  1 ? 37 
ATOM   12289 C C   . ILE J  2 70  ? 40.958  -93.288  40.352  1.000 55.873  0 70  ILE JJJ C   1 ? 37 
ATOM   12290 O O   . ILE J  2 70  ? 41.389  -93.687  41.435  1.000 55.771  0 70  ILE JJJ O   1 ? 37 
ATOM   12291 C CB  . ILE J  2 70  ? 38.392  -93.204  40.266  1.000 56.725  0 70  ILE JJJ CB  1 ? 37 
ATOM   12292 C CG1 . ILE J  2 70  ? 38.230  -91.845  39.578  1.000 54.474  0 70  ILE JJJ CG1 1 ? 37 
ATOM   12293 C CG2 . ILE J  2 70  ? 38.342  -93.098  41.781  1.000 56.531  0 70  ILE JJJ CG2 1 ? 37 
ATOM   12294 C CD1 . ILE J  2 70  ? 36.902  -91.172  39.852  1.000 52.621  0 70  ILE JJJ CD1 1 ? 37 
ATOM   12295 N N   . SER J  2 71  ? 41.567  -92.384  39.589  1.000 52.699  0 71  SER JJJ N   1 ? 37 
ATOM   12296 C CA  . SER J  2 71  ? 42.801  -91.653  39.964  1.000 51.506  0 71  SER JJJ CA  1 ? 37 
ATOM   12297 C C   . SER J  2 71  ? 42.799  -90.303  39.238  1.000 50.340  0 71  SER JJJ C   1 ? 37 
ATOM   12298 O O   . SER J  2 71  ? 41.992  -90.128  38.304  1.000 46.921  0 71  SER JJJ O   1 ? 37 
ATOM   12299 C CB  . SER J  2 71  ? 44.026  -92.467  39.663  1.000 52.286  0 71  SER JJJ CB  1 ? 37 
ATOM   12300 O OG  . SER J  2 71  ? 44.140  -92.715  38.273  1.000 51.896  0 71  SER JJJ OG  1 ? 37 
ATOM   12301 N N   . ARG J  2 72  ? 43.619  -89.357  39.686  1.000 50.574  0 72  ARG JJJ N   1 ? 37 
ATOM   12302 C CA  . ARG J  2 72  ? 43.679  -88.011  39.072  1.000 50.038  0 72  ARG JJJ CA  1 ? 37 
ATOM   12303 C C   . ARG J  2 72  ? 45.137  -87.590  38.948  1.000 49.199  0 72  ARG JJJ C   1 ? 37 
ATOM   12304 O O   . ARG J  2 72  ? 45.938  -88.031  39.757  1.000 49.447  0 72  ARG JJJ O   1 ? 37 
ATOM   12305 C CB  . ARG J  2 72  ? 42.864  -87.016  39.908  1.000 50.113  0 72  ARG JJJ CB  1 ? 37 
ATOM   12306 C CG  . ARG J  2 72  ? 43.340  -86.824  41.339  1.000 50.441  0 72  ARG JJJ CG  1 ? 37 
ATOM   12307 C CD  . ARG J  2 72  ? 42.363  -85.975  42.138  1.000 50.395  0 72  ARG JJJ CD  1 ? 37 
ATOM   12308 N NE  . ARG J  2 72  ? 42.142  -84.663  41.529  1.000 49.271  0 72  ARG JJJ NE  1 ? 37 
ATOM   12309 C CZ  . ARG J  2 72  ? 41.042  -83.923  41.640  1.000 49.015  0 72  ARG JJJ CZ  1 ? 37 
ATOM   12310 N NH1 . ARG J  2 72  ? 40.007  -84.347  42.348  1.000 50.593  0 72  ARG JJJ NH1 1 ? 37 
ATOM   12311 N NH2 . ARG J  2 72  ? 40.975  -82.746  41.030  1.000 47.619  0 72  ARG JJJ NH2 1 ? 37 
ATOM   12312 N N   . ASP J  2 73  ? 45.443  -86.794  37.928  1.000 47.821  0 73  ASP JJJ N   1 ? 37 
ATOM   12313 C CA  . ASP J  2 73  ? 46.750  -86.130  37.734  1.000 48.233  0 73  ASP JJJ CA  1 ? 37 
ATOM   12314 C C   . ASP J  2 73  ? 46.453  -84.639  37.547  1.000 47.669  0 73  ASP JJJ C   1 ? 37 
ATOM   12315 O O   . ASP J  2 73  ? 46.049  -84.216  36.419  1.000 48.467  0 73  ASP JJJ O   1 ? 37 
ATOM   12316 C CB  . ASP J  2 73  ? 47.497  -86.767  36.567  1.000 50.046  0 73  ASP JJJ CB  1 ? 37 
ATOM   12317 C CG  . ASP J  2 73  ? 48.844  -86.125  36.287  1.000 52.324  0 73  ASP JJJ CG  1 ? 37 
ATOM   12318 O OD1 . ASP J  2 73  ? 49.138  -85.055  36.921  1.000 53.802  0 73  ASP JJJ OD1 1 ? 37 
ATOM   12319 O OD2 . ASP J  2 73  ? 49.573  -86.683  35.451  1.000 51.351  0 73  ASP JJJ OD2 1 ? 37 
ATOM   12320 N N   . ASN J  2 74  ? 46.571  -83.891  38.641  1.000 47.191  0 74  ASN JJJ N   1 ? 37 
ATOM   12321 C CA  . ASN J  2 74  ? 46.226  -82.454  38.699  1.000 45.106  0 74  ASN JJJ CA  1 ? 37 
ATOM   12322 C C   . ASN J  2 74  ? 47.040  -81.653  37.673  1.000 45.295  0 74  ASN JJJ C   1 ? 37 
ATOM   12323 O O   . ASN J  2 74  ? 46.487  -80.760  37.056  1.000 42.318  0 74  ASN JJJ O   1 ? 37 
ATOM   12324 C CB  . ASN J  2 74  ? 46.340  -81.971  40.139  1.000 44.789  0 74  ASN JJJ CB  1 ? 37 
ATOM   12325 C CG  . ASN J  2 74  ? 45.161  -82.411  40.975  1.000 44.133  0 74  ASN JJJ CG  1 ? 37 
ATOM   12326 O OD1 . ASN J  2 74  ? 44.236  -83.063  40.498  1.000 43.824  0 74  ASN JJJ OD1 1 ? 37 
ATOM   12327 N ND2 . ASN J  2 74  ? 45.160  -82.005  42.230  1.000 44.360  0 74  ASN JJJ ND2 1 ? 37 
ATOM   12328 N N   . ALA J  2 75  ? 48.301  -82.016  37.459  1.000 49.458  0 75  ALA JJJ N   1 ? 37 
ATOM   12329 C CA  . ALA J  2 75  ? 49.222  -81.321  36.532  1.000 50.759  0 75  ALA JJJ CA  1 ? 37 
ATOM   12330 C C   . ALA J  2 75  ? 48.670  -81.399  35.103  1.000 52.461  0 75  ALA JJJ C   1 ? 37 
ATOM   12331 O O   . ALA J  2 75  ? 49.004  -80.508  34.309  1.000 56.062  0 75  ALA JJJ O   1 ? 37 
ATOM   12332 C CB  . ALA J  2 75  ? 50.608  -81.904  36.629  1.000 52.166  0 75  ALA JJJ CB  1 ? 37 
ATOM   12333 N N   . LYS J  2 76  ? 47.851  -82.407  34.781  1.000 51.975  0 76  LYS JJJ N   1 ? 37 
ATOM   12334 C CA  . LYS J  2 76  ? 47.313  -82.610  33.412  1.000 51.551  0 76  LYS JJJ CA  1 ? 37 
ATOM   12335 C C   . LYS J  2 76  ? 45.800  -82.419  33.365  1.000 47.899  0 76  LYS JJJ C   1 ? 37 
ATOM   12336 O O   . LYS J  2 76  ? 45.194  -82.764  32.341  1.000 48.280  0 76  LYS JJJ O   1 ? 37 
ATOM   12337 C CB  . LYS J  2 76  ? 47.617  -84.030  32.950  1.000 55.046  0 76  LYS JJJ CB  1 ? 37 
ATOM   12338 C CG  . LYS J  2 76  ? 49.099  -84.348  32.918  1.000 60.517  0 76  LYS JJJ CG  1 ? 37 
ATOM   12339 C CD  . LYS J  2 76  ? 49.389  -85.585  32.119  1.000 63.956  0 76  LYS JJJ CD  1 ? 37 
ATOM   12340 C CE  . LYS J  2 76  ? 50.866  -85.844  31.981  1.000 69.771  0 76  LYS JJJ CE  1 ? 37 
ATOM   12341 N NZ  . LYS J  2 76  ? 51.064  -87.177  31.368  1.000 74.579  0 76  LYS JJJ NZ  1 ? 37 
ATOM   12342 N N   . ASN J  2 77  ? 45.198  -81.879  34.420  1.000 45.191  0 77  ASN JJJ N   1 ? 37 
ATOM   12343 C CA  . ASN J  2 77  ? 43.746  -81.607  34.435  1.000 44.535  0 77  ASN JJJ CA  1 ? 37 
ATOM   12344 C C   . ASN J  2 77  ? 42.975  -82.884  34.087  1.000 42.621  0 77  ASN JJJ C   1 ? 37 
ATOM   12345 O O   . ASN J  2 77  ? 41.936  -82.758  33.446  1.000 39.679  0 77  ASN JJJ O   1 ? 37 
ATOM   12346 C CB  . ASN J  2 77  ? 43.407  -80.470  33.457  1.000 42.701  0 77  ASN JJJ CB  1 ? 37 
ATOM   12347 C CG  . ASN J  2 77  ? 43.503  -79.096  34.080  1.000 41.267  0 77  ASN JJJ CG  1 ? 37 
ATOM   12348 O OD1 . ASN J  2 77  ? 44.403  -78.831  34.870  1.000 40.341  0 77  ASN JJJ OD1 1 ? 37 
ATOM   12349 N ND2 . ASN J  2 77  ? 42.586  -78.211  33.730  1.000 40.523  0 77  ASN JJJ ND2 1 ? 37 
ATOM   12350 N N   . THR J  2 78  ? 43.464  -84.053  34.478  1.000 44.693  0 78  THR JJJ N   1 ? 37 
ATOM   12351 C CA  . THR J  2 78  ? 42.901  -85.337  33.999  1.000 44.550  0 78  THR JJJ CA  1 ? 37 
ATOM   12352 C C   . THR J  2 78  ? 42.536  -86.250  35.185  1.000 47.160  0 78  THR JJJ C   1 ? 37 
ATOM   12353 O O   . THR J  2 78  ? 43.321  -86.367  36.171  1.000 47.617  0 78  THR JJJ O   1 ? 37 
ATOM   12354 C CB  . THR J  2 78  ? 43.848  -85.983  32.989  1.000 44.377  0 78  THR JJJ CB  1 ? 37 
ATOM   12355 O OG1 . THR J  2 78  ? 44.009  -85.080  31.886  1.000 41.086  0 78  THR JJJ OG1 1 ? 37 
ATOM   12356 C CG2 . THR J  2 78  ? 43.342  -87.328  32.519  1.000 44.088  0 78  THR JJJ CG2 1 ? 37 
ATOM   12357 N N   . VAL J  2 79  ? 41.344  -86.850  35.097  1.000 46.324  0 79  VAL JJJ N   1 ? 37 
ATOM   12358 C CA  . VAL J  2 79  ? 40.881  -87.974  35.956  1.000 47.215  0 79  VAL JJJ CA  1 ? 37 
ATOM   12359 C C   . VAL J  2 79  ? 40.858  -89.230  35.084  1.000 48.440  0 79  VAL JJJ C   1 ? 37 
ATOM   12360 O O   . VAL J  2 79  ? 40.518  -89.128  33.888  1.000 50.619  0 79  VAL JJJ O   1 ? 37 
ATOM   12361 C CB  . VAL J  2 79  ? 39.508  -87.665  36.585  1.000 47.462  0 79  VAL JJJ CB  1 ? 37 
ATOM   12362 C CG1 . VAL J  2 79  ? 38.428  -87.431  35.547  1.000 47.477  0 79  VAL JJJ CG1 1 ? 37 
ATOM   12363 C CG2 . VAL J  2 79  ? 39.046  -88.744  37.555  1.000 49.233  0 79  VAL JJJ CG2 1 ? 37 
ATOM   12364 N N   . TYR J  2 80  ? 41.249  -90.372  35.648  1.000 50.832  0 80  TYR JJJ N   1 ? 37 
ATOM   12365 C CA  . TYR J  2 80  ? 41.346  -91.681  34.950  1.000 53.082  0 80  TYR JJJ CA  1 ? 37 
ATOM   12366 C C   . TYR J  2 80  ? 40.368  -92.672  35.580  1.000 53.791  0 80  TYR JJJ C   1 ? 37 
ATOM   12367 O O   . TYR J  2 80  ? 40.118  -92.600  36.793  1.000 55.881  0 80  TYR JJJ O   1 ? 37 
ATOM   12368 C CB  . TYR J  2 80  ? 42.779  -92.212  35.016  1.000 53.732  0 80  TYR JJJ CB  1 ? 37 
ATOM   12369 C CG  . TYR J  2 80  ? 43.794  -91.322  34.347  1.000 54.435  0 80  TYR JJJ CG  1 ? 37 
ATOM   12370 C CD1 . TYR J  2 80  ? 43.940  -91.317  32.965  1.000 55.498  0 80  TYR JJJ CD1 1 ? 37 
ATOM   12371 C CD2 . TYR J  2 80  ? 44.603  -90.475  35.087  1.000 55.063  0 80  TYR JJJ CD2 1 ? 37 
ATOM   12372 C CE1 . TYR J  2 80  ? 44.877  -90.511  32.340  1.000 54.349  0 80  TYR JJJ CE1 1 ? 37 
ATOM   12373 C CE2 . TYR J  2 80  ? 45.523  -89.639  34.478  1.000 54.641  0 80  TYR JJJ CE2 1 ? 37 
ATOM   12374 C CZ  . TYR J  2 80  ? 45.663  -89.664  33.102  1.000 53.453  0 80  TYR JJJ CZ  1 ? 37 
ATOM   12375 O OH  . TYR J  2 80  ? 46.567  -88.859  32.496  1.000 51.379  0 80  TYR JJJ OH  1 ? 37 
ATOM   12376 N N   . LEU J  2 81  ? 39.837  -93.586  34.768  1.000 55.431  0 81  LEU JJJ N   1 ? 37 
ATOM   12377 C CA  . LEU J  2 81  ? 39.110  -94.791  35.248  1.000 54.984  0 81  LEU JJJ CA  1 ? 37 
ATOM   12378 C C   . LEU J  2 81  ? 39.767  -96.027  34.621  1.000 55.864  0 81  LEU JJJ C   1 ? 37 
ATOM   12379 O O   . LEU J  2 81  ? 39.585  -96.250  33.413  1.000 54.358  0 81  LEU JJJ O   1 ? 37 
ATOM   12380 C CB  . LEU J  2 81  ? 37.623  -94.692  34.906  1.000 54.123  0 81  LEU JJJ CB  1 ? 37 
ATOM   12381 C CG  . LEU J  2 81  ? 36.722  -95.739  35.574  1.000 54.717  0 81  LEU JJJ CG  1 ? 37 
ATOM   12382 C CD1 . LEU J  2 81  ? 36.619  -95.510  37.072  1.000 54.282  0 81  LEU JJJ CD1 1 ? 37 
ATOM   12383 C CD2 . LEU J  2 81  ? 35.329  -95.738  34.958  1.000 54.539  0 81  LEU JJJ CD2 1 ? 37 
ATOM   12384 N N   . GLN J  2 82  ? 40.550  -96.756  35.424  1.000 57.281  0 82  GLN JJJ N   1 ? 37 
ATOM   12385 C CA  . GLN J  2 82  ? 41.130  -98.073  35.083  1.000 57.987  0 82  GLN JJJ CA  1 ? 37 
ATOM   12386 C C   . GLN J  2 82  ? 39.996  -99.084  35.263  1.000 61.231  0 82  GLN JJJ C   1 ? 37 
ATOM   12387 O O   . GLN J  2 82  ? 39.468  -99.177  36.379  1.000 61.719  0 82  GLN JJJ O   1 ? 37 
ATOM   12388 C CB  . GLN J  2 82  ? 42.353  -98.352  35.957  1.000 56.718  0 82  GLN JJJ CB  1 ? 37 
ATOM   12389 C CG  . GLN J  2 82  ? 43.138  -99.584  35.539  1.000 59.232  0 82  GLN JJJ CG  1 ? 37 
ATOM   12390 C CD  . GLN J  2 82  ? 43.535  -99.554  34.082  1.000 59.387  0 82  GLN JJJ CD  1 ? 37 
ATOM   12391 O OE1 . GLN J  2 82  ? 44.072  -98.564  33.580  1.000 56.296  0 82  GLN JJJ OE1 1 ? 37 
ATOM   12392 N NE2 . GLN J  2 82  ? 43.255  -100.646 33.385  1.000 60.285  0 82  GLN JJJ NE2 1 ? 37 
ATOM   12393 N N   . MET J  2 83  ? 39.560  -99.727  34.183  1.000 63.231  0 83  MET JJJ N   1 ? 37 
ATOM   12394 C CA  . MET J  2 83  ? 38.467  -100.729 34.226  1.000 64.627  0 83  MET JJJ CA  1 ? 37 
ATOM   12395 C C   . MET J  2 83  ? 39.097  -102.079 33.887  1.000 67.432  0 83  MET JJJ C   1 ? 37 
ATOM   12396 O O   . MET J  2 83  ? 39.552  -102.241 32.750  1.000 69.511  0 83  MET JJJ O   1 ? 37 
ATOM   12397 C CB  . MET J  2 83  ? 37.347  -100.398 33.236  1.000 63.586  0 83  MET JJJ CB  1 ? 37 
ATOM   12398 C CG  . MET J  2 83  ? 36.788  -98.996  33.367  1.000 63.445  0 83  MET JJJ CG  1 ? 37 
ATOM   12399 S SD  . MET J  2 83  ? 35.409  -98.637  32.201  1.000 64.838  0 83  MET JJJ SD  1 ? 37 
ATOM   12400 C CE  . MET J  2 83  ? 36.302  -98.618  30.654  1.000 65.707  0 83  MET JJJ CE  1 ? 37 
ATOM   12401 N N   . ASN J  2 84  ? 39.160  -102.980 34.863  1.000 68.987  0 84  ASN JJJ N   1 ? 37 
ATOM   12402 C CA  . ASN J  2 84  ? 39.729  -104.342 34.700  1.000 73.634  0 84  ASN JJJ CA  1 ? 37 
ATOM   12403 C C   . ASN J  2 84  ? 38.590  -105.369 34.696  1.000 76.738  0 84  ASN JJJ C   1 ? 37 
ATOM   12404 O O   . ASN J  2 84  ? 37.495  -105.063 35.212  1.000 77.807  0 84  ASN JJJ O   1 ? 37 
ATOM   12405 C CB  . ASN J  2 84  ? 40.784  -104.630 35.771  1.000 73.270  0 84  ASN JJJ CB  1 ? 37 
ATOM   12406 C CG  . ASN J  2 84  ? 41.970  -103.699 35.668  1.000 70.563  0 84  ASN JJJ CG  1 ? 37 
ATOM   12407 O OD1 . ASN J  2 84  ? 42.373  -103.318 34.575  1.000 69.734  0 84  ASN JJJ OD1 1 ? 37 
ATOM   12408 N ND2 . ASN J  2 84  ? 42.529  -103.311 36.801  1.000 70.938  0 84  ASN JJJ ND2 1 ? 37 
ATOM   12409 N N   . ARG J  2 85  ? 38.849  -106.532 34.102  1.000 79.031  0 85  ARG JJJ N   1 ? 37 
ATOM   12410 C CA  . ARG J  2 85  ? 37.950  -107.710 34.149  1.000 82.401  0 85  ARG JJJ CA  1 ? 37 
ATOM   12411 C C   . ARG J  2 85  ? 36.546  -107.240 33.746  1.000 78.841  0 85  ARG JJJ C   1 ? 37 
ATOM   12412 O O   . ARG J  2 85  ? 35.583  -107.448 34.503  1.000 76.909  0 85  ARG JJJ O   1 ? 37 
ATOM   12413 C CB  . ARG J  2 85  ? 38.073  -108.347 35.536  1.000 86.221  0 85  ARG JJJ CB  1 ? 37 
ATOM   12414 C CG  . ARG J  2 85  ? 39.494  -108.795 35.867  1.000 90.428  0 85  ARG JJJ CG  1 ? 37 
ATOM   12415 C CD  . ARG J  2 85  ? 39.653  -109.645 37.106  1.000 95.719  0 85  ARG JJJ CD  1 ? 37 
ATOM   12416 N NE  . ARG J  2 85  ? 39.102  -108.975 38.274  1.000 96.482  0 85  ARG JJJ NE  1 ? 37 
ATOM   12417 C CZ  . ARG J  2 85  ? 38.006  -109.343 38.946  1.000 99.528  0 85  ARG JJJ CZ  1 ? 37 
ATOM   12418 N NH1 . ARG J  2 85  ? 37.311  -110.423 38.606  1.000 102.217 0 85  ARG JJJ NH1 1 ? 37 
ATOM   12419 N NH2 . ARG J  2 85  ? 37.645  -108.651 40.015  1.000 99.352  0 85  ARG JJJ NH2 1 ? 37 
ATOM   12420 N N   . LEU J  2 86  ? 36.456  -106.616 32.575  1.000 76.788  0 86  LEU JJJ N   1 ? 37 
ATOM   12421 C CA  . LEU J  2 86  ? 35.197  -106.037 32.047  1.000 76.303  0 86  LEU JJJ CA  1 ? 37 
ATOM   12422 C C   . LEU J  2 86  ? 34.237  -107.163 31.669  1.000 79.612  0 86  LEU JJJ C   1 ? 37 
ATOM   12423 O O   . LEU J  2 86  ? 34.686  -108.183 31.111  1.000 79.577  0 86  LEU JJJ O   1 ? 37 
ATOM   12424 C CB  . LEU J  2 86  ? 35.516  -105.146 30.846  1.000 74.837  0 86  LEU JJJ CB  1 ? 37 
ATOM   12425 C CG  . LEU J  2 86  ? 36.102  -103.786 31.214  1.000 71.861  0 86  LEU JJJ CG  1 ? 37 
ATOM   12426 C CD1 . LEU J  2 86  ? 36.744  -103.121 30.012  1.000 71.047  0 86  LEU JJJ CD1 1 ? 37 
ATOM   12427 C CD2 . LEU J  2 86  ? 35.032  -102.884 31.802  1.000 69.815  0 86  LEU JJJ CD2 1 ? 37 
ATOM   12428 N N   . LYS J  2 87  ? 32.953  -106.949 31.965  1.000 81.487  0 87  LYS JJJ N   1 ? 37 
ATOM   12429 C CA  . LYS J  2 87  ? 31.839  -107.890 31.685  1.000 83.057  0 87  LYS JJJ CA  1 ? 37 
ATOM   12430 C C   . LYS J  2 87  ? 30.893  -107.203 30.711  1.000 80.192  0 87  LYS JJJ C   1 ? 37 
ATOM   12431 O O   . LYS J  2 87  ? 30.890  -105.972 30.630  1.000 76.414  0 87  LYS JJJ O   1 ? 37 
ATOM   12432 C CB  . LYS J  2 87  ? 31.129  -108.254 32.993  1.000 86.137  0 87  LYS JJJ CB  1 ? 37 
ATOM   12433 C CG  . LYS J  2 87  ? 32.061  -108.495 34.171  1.000 88.487  0 87  LYS JJJ CG  1 ? 37 
ATOM   12434 C CD  . LYS J  2 87  ? 31.396  -108.617 35.529  1.000 91.509  0 87  LYS JJJ CD  1 ? 37 
ATOM   12435 C CE  . LYS J  2 87  ? 32.387  -109.112 36.561  1.000 94.052  0 87  LYS JJJ CE  1 ? 37 
ATOM   12436 N NZ  . LYS J  2 87  ? 31.771  -109.326 37.891  1.000 95.852  0 87  LYS JJJ NZ  1 ? 37 
ATOM   12437 N N   . PRO J  2 88  ? 30.097  -107.956 29.921  1.000 82.196  0 88  PRO JJJ N   1 ? 37 
ATOM   12438 C CA  . PRO J  2 88  ? 29.109  -107.347 29.028  1.000 82.114  0 88  PRO JJJ CA  1 ? 37 
ATOM   12439 C C   . PRO J  2 88  ? 28.212  -106.294 29.695  1.000 80.428  0 88  PRO JJJ C   1 ? 37 
ATOM   12440 O O   . PRO J  2 88  ? 27.956  -105.310 29.054  1.000 81.197  0 88  PRO JJJ O   1 ? 37 
ATOM   12441 C CB  . PRO J  2 88  ? 28.313  -108.562 28.530  1.000 85.889  0 88  PRO JJJ CB  1 ? 37 
ATOM   12442 C CG  . PRO J  2 88  ? 29.354  -109.658 28.493  1.000 87.238  0 88  PRO JJJ CG  1 ? 37 
ATOM   12443 C CD  . PRO J  2 88  ? 30.178  -109.414 29.745  1.000 85.513  0 88  PRO JJJ CD  1 ? 37 
ATOM   12444 N N   . GLU J  2 89  ? 27.825  -106.488 30.957  1.000 81.968  0 89  GLU JJJ N   1 ? 37 
ATOM   12445 C CA  . GLU J  2 89  ? 26.935  -105.570 31.733  1.000 81.163  0 89  GLU JJJ CA  1 ? 37 
ATOM   12446 C C   . GLU J  2 89  ? 27.623  -104.223 31.991  1.000 75.820  0 89  GLU JJJ C   1 ? 37 
ATOM   12447 O O   . GLU J  2 89  ? 26.938  -103.334 32.530  1.000 74.498  0 89  GLU JJJ O   1 ? 37 
ATOM   12448 C CB  . GLU J  2 89  ? 26.546  -106.117 33.113  1.000 83.990  0 89  GLU JJJ CB  1 ? 37 
ATOM   12449 C CG  . GLU J  2 89  ? 26.072  -107.559 33.117  1.000 90.592  0 89  GLU JJJ CG  1 ? 37 
ATOM   12450 C CD  . GLU J  2 89  ? 27.189  -108.591 33.210  1.000 94.306  0 89  GLU JJJ CD  1 ? 37 
ATOM   12451 O OE1 . GLU J  2 89  ? 28.132  -108.373 34.021  1.000 95.860  0 89  GLU JJJ OE1 1 ? 37 
ATOM   12452 O OE2 . GLU J  2 89  ? 27.132  -109.602 32.463  1.000 97.299  0 89  GLU JJJ OE2 1 ? 37 
ATOM   12453 N N   . ASP J  2 90  ? 28.916  -104.088 31.679  1.000 72.078  0 90  ASP JJJ N   1 ? 37 
ATOM   12454 C CA  . ASP J  2 90  ? 29.674  -102.812 31.824  1.000 68.902  0 90  ASP JJJ CA  1 ? 37 
ATOM   12455 C C   . ASP J  2 90  ? 29.510  -101.944 30.568  1.000 65.307  0 90  ASP JJJ C   1 ? 37 
ATOM   12456 O O   . ASP J  2 90  ? 29.919  -100.783 30.605  1.000 59.323  0 90  ASP JJJ O   1 ? 37 
ATOM   12457 C CB  . ASP J  2 90  ? 31.160  -103.056 32.100  1.000 68.943  0 90  ASP JJJ CB  1 ? 37 
ATOM   12458 C CG  . ASP J  2 90  ? 31.430  -103.709 33.442  1.000 70.464  0 90  ASP JJJ CG  1 ? 37 
ATOM   12459 O OD1 . ASP J  2 90  ? 30.800  -103.289 34.451  1.000 69.166  0 90  ASP JJJ OD1 1 ? 37 
ATOM   12460 O OD2 . ASP J  2 90  ? 32.262  -104.642 33.467  1.000 71.456  0 90  ASP JJJ OD2 1 ? 37 
ATOM   12461 N N   . THR J  2 91  ? 28.953  -102.506 29.492  1.000 67.157  0 91  THR JJJ N   1 ? 37 
ATOM   12462 C CA  . THR J  2 91  ? 28.662  -101.772 28.239  1.000 66.064  0 91  THR JJJ CA  1 ? 37 
ATOM   12463 C C   . THR J  2 91  ? 27.716  -100.608 28.552  1.000 65.206  0 91  THR JJJ C   1 ? 37 
ATOM   12464 O O   . THR J  2 91  ? 26.647  -100.846 29.115  1.000 66.646  0 91  THR JJJ O   1 ? 37 
ATOM   12465 C CB  . THR J  2 91  ? 28.082  -102.705 27.186  1.000 67.708  0 91  THR JJJ CB  1 ? 37 
ATOM   12466 O OG1 . THR J  2 91  ? 29.121  -103.626 26.858  1.000 69.174  0 91  THR JJJ OG1 1 ? 37 
ATOM   12467 C CG2 . THR J  2 91  ? 27.625  -101.972 25.951  1.000 68.002  0 91  THR JJJ CG2 1 ? 37 
ATOM   12468 N N   . ALA J  2 92  ? 28.112  -99.390  28.204  1.000 62.860  0 92  ALA JJJ N   1 ? 37 
ATOM   12469 C CA  . ALA J  2 92  ? 27.338  -98.152  28.453  1.000 60.780  0 92  ALA JJJ CA  1 ? 37 
ATOM   12470 C C   . ALA J  2 92  ? 28.094  -96.946  27.901  1.000 58.138  0 92  ALA JJJ C   1 ? 37 
ATOM   12471 O O   . ALA J  2 92  ? 29.269  -97.087  27.519  1.000 57.374  0 92  ALA JJJ O   1 ? 37 
ATOM   12472 C CB  . ALA J  2 92  ? 27.095  -97.961  29.929  1.000 59.202  0 92  ALA JJJ CB  1 ? 37 
ATOM   12473 N N   . VAL J  2 93  ? 27.421  -95.799  27.886  1.000 57.174  0 93  VAL JJJ N   1 ? 37 
ATOM   12474 C CA  . VAL J  2 93  ? 28.080  -94.476  27.751  1.000 55.800  0 93  VAL JJJ CA  1 ? 37 
ATOM   12475 C C   . VAL J  2 93  ? 28.633  -94.120  29.132  1.000 54.088  0 93  VAL JJJ C   1 ? 37 
ATOM   12476 O O   . VAL J  2 93  ? 27.866  -94.181  30.114  1.000 53.153  0 93  VAL JJJ O   1 ? 37 
ATOM   12477 C CB  . VAL J  2 93  ? 27.099  -93.422  27.206  1.000 55.814  0 93  VAL JJJ CB  1 ? 37 
ATOM   12478 C CG1 . VAL J  2 93  ? 27.714  -92.028  27.193  1.000 54.736  0 93  VAL JJJ CG1 1 ? 37 
ATOM   12479 C CG2 . VAL J  2 93  ? 26.634  -93.786  25.804  1.000 57.957  0 93  VAL JJJ CG2 1 ? 37 
ATOM   12480 N N   . TYR J  2 94  ? 29.921  -93.803  29.193  1.000 53.939  0 94  TYR JJJ N   1 ? 37 
ATOM   12481 C CA  . TYR J  2 94  ? 30.622  -93.392  30.439  1.000 52.074  0 94  TYR JJJ CA  1 ? 37 
ATOM   12482 C C   . TYR J  2 94  ? 30.798  -91.879  30.387  1.000 50.070  0 94  TYR JJJ C   1 ? 37 
ATOM   12483 O O   . TYR J  2 94  ? 31.386  -91.378  29.399  1.000 51.132  0 94  TYR JJJ O   1 ? 37 
ATOM   12484 C CB  . TYR J  2 94  ? 31.939  -94.153  30.612  1.000 51.565  0 94  TYR JJJ CB  1 ? 37 
ATOM   12485 C CG  . TYR J  2 94  ? 31.750  -95.565  31.096  1.000 53.503  0 94  TYR JJJ CG  1 ? 37 
ATOM   12486 C CD1 . TYR J  2 94  ? 31.241  -96.544  30.252  1.000 56.382  0 94  TYR JJJ CD1 1 ? 37 
ATOM   12487 C CD2 . TYR J  2 94  ? 32.041  -95.920  32.399  1.000 53.445  0 94  TYR JJJ CD2 1 ? 37 
ATOM   12488 C CE1 . TYR J  2 94  ? 31.052  -97.845  30.683  1.000 58.614  0 94  TYR JJJ CE1 1 ? 37 
ATOM   12489 C CE2 . TYR J  2 94  ? 31.836  -97.216  32.856  1.000 55.973  0 94  TYR JJJ CE2 1 ? 37 
ATOM   12490 C CZ  . TYR J  2 94  ? 31.349  -98.186  31.994  1.000 57.491  0 94  TYR JJJ CZ  1 ? 37 
ATOM   12491 O OH  . TYR J  2 94  ? 31.170  -99.461  32.445  1.000 58.911  0 94  TYR JJJ OH  1 ? 37 
ATOM   12492 N N   . PHE J  2 95  ? 30.249  -91.199  31.399  1.000 50.161  0 95  PHE JJJ N   1 ? 37 
ATOM   12493 C CA  . PHE J  2 95  ? 30.260  -89.728  31.555  1.000 50.064  0 95  PHE JJJ CA  1 ? 37 
ATOM   12494 C C   . PHE J  2 95  ? 31.238  -89.331  32.657  1.000 48.831  0 95  PHE JJJ C   1 ? 37 
ATOM   12495 O O   . PHE J  2 95  ? 31.196  -89.861  33.770  1.000 46.861  0 95  PHE JJJ O   1 ? 37 
ATOM   12496 C CB  . PHE J  2 95  ? 28.897  -89.183  31.953  1.000 50.440  0 95  PHE JJJ CB  1 ? 37 
ATOM   12497 C CG  . PHE J  2 95  ? 27.822  -89.392  30.933  1.000 52.221  0 95  PHE JJJ CG  1 ? 37 
ATOM   12498 C CD1 . PHE J  2 95  ? 27.640  -88.494  29.888  1.000 53.689  0 95  PHE JJJ CD1 1 ? 37 
ATOM   12499 C CD2 . PHE J  2 95  ? 26.934  -90.443  31.067  1.000 54.005  0 95  PHE JJJ CD2 1 ? 37 
ATOM   12500 C CE1 . PHE J  2 95  ? 26.619  -88.682  28.970  1.000 53.851  0 95  PHE JJJ CE1 1 ? 37 
ATOM   12501 C CE2 . PHE J  2 95  ? 25.884  -90.602  30.174  1.000 54.918  0 95  PHE JJJ CE2 1 ? 37 
ATOM   12502 C CZ  . PHE J  2 95  ? 25.746  -89.736  29.116  1.000 55.591  0 95  PHE JJJ CZ  1 ? 37 
ATOM   12503 N N   . CYS J  2 96  ? 32.088  -88.379  32.304  1.000 50.928  0 96  CYS JJJ N   1 ? 37 
ATOM   12504 C CA  . CYS J  2 96  ? 32.930  -87.599  33.233  1.000 49.226  0 96  CYS JJJ CA  1 ? 37 
ATOM   12505 C C   . CYS J  2 96  ? 32.043  -86.547  33.906  1.000 45.409  0 96  CYS JJJ C   1 ? 37 
ATOM   12506 O O   . CYS J  2 96  ? 31.203  -85.949  33.222  1.000 47.128  0 96  CYS JJJ O   1 ? 37 
ATOM   12507 C CB  . CYS J  2 96  ? 34.033  -86.944  32.420  1.000 49.919  0 96  CYS JJJ CB  1 ? 37 
ATOM   12508 S SG  . CYS J  2 96  ? 35.259  -86.117  33.447  1.000 59.420  0 96  CYS JJJ SG  1 ? 37 
ATOM   12509 N N   . ALA J  2 97  ? 32.215  -86.303  35.187  1.000 43.798  0 97  ALA JJJ N   1 ? 37 
ATOM   12510 C CA  . ALA J  2 97  ? 31.523  -85.189  35.869  1.000 47.349  0 97  ALA JJJ CA  1 ? 37 
ATOM   12511 C C   . ALA J  2 97  ? 32.475  -84.509  36.857  1.000 47.797  0 97  ALA JJJ C   1 ? 37 
ATOM   12512 O O   . ALA J  2 97  ? 33.453  -85.160  37.314  1.000 51.965  0 97  ALA JJJ O   1 ? 37 
ATOM   12513 C CB  . ALA J  2 97  ? 30.263  -85.684  36.551  1.000 49.358  0 97  ALA JJJ CB  1 ? 37 
ATOM   12514 N N   . ALA J  2 98  ? 32.193  -83.244  37.170  1.000 44.675  0 98  ALA JJJ N   1 ? 37 
ATOM   12515 C CA  . ALA J  2 98  ? 33.012  -82.430  38.087  1.000 42.278  0 98  ALA JJJ CA  1 ? 37 
ATOM   12516 C C   . ALA J  2 98  ? 32.135  -81.502  38.914  1.000 42.096  0 98  ALA JJJ C   1 ? 37 
ATOM   12517 O O   . ALA J  2 98  ? 31.051  -81.018  38.403  1.000 39.435  0 98  ALA JJJ O   1 ? 37 
ATOM   12518 C CB  . ALA J  2 98  ? 33.988  -81.652  37.288  1.000 42.571  0 98  ALA JJJ CB  1 ? 37 
ATOM   12519 N N   . ASP J  2 99  ? 32.576  -81.269  40.152  1.000 40.901  0 99  ASP JJJ N   1 ? 37 
ATOM   12520 C CA  . ASP J  2 99  ? 31.945  -80.287  41.069  1.000 42.484  0 99  ASP JJJ CA  1 ? 37 
ATOM   12521 C C   . ASP J  2 99  ? 32.991  -79.746  42.045  1.000 41.883  0 99  ASP JJJ C   1 ? 37 
ATOM   12522 O O   . ASP J  2 99  ? 33.901  -80.495  42.398  1.000 43.681  0 99  ASP JJJ O   1 ? 37 
ATOM   12523 C CB  . ASP J  2 99  ? 30.762  -80.903  41.817  1.000 43.216  0 99  ASP JJJ CB  1 ? 37 
ATOM   12524 C CG  . ASP J  2 99  ? 29.803  -79.831  42.272  1.000 45.411  0 99  ASP JJJ CG  1 ? 37 
ATOM   12525 O OD1 . ASP J  2 99  ? 29.013  -79.339  41.400  1.000 43.735  0 99  ASP JJJ OD1 1 ? 37 
ATOM   12526 O OD2 . ASP J  2 99  ? 29.903  -79.438  43.467  1.000 51.208  0 99  ASP JJJ OD2 1 ? 37 
ATOM   12527 N N   . ARG J  2 100 ? 32.835  -78.504  42.487  1.000 47.416  0 100 ARG JJJ N   1 ? 38 
ATOM   12528 C CA  . ARG J  2 100 ? 33.699  -77.919  43.541  1.000 46.669  0 100 ARG JJJ CA  1 ? 38 
ATOM   12529 C C   . ARG J  2 100 ? 33.507  -78.684  44.850  1.000 45.194  0 100 ARG JJJ C   1 ? 38 
ATOM   12530 O O   . ARG J  2 100 ? 34.465  -78.812  45.603  1.000 48.490  0 100 ARG JJJ O   1 ? 38 
ATOM   12531 C CB  . ARG J  2 100 ? 33.368  -76.437  43.731  1.000 47.063  0 100 ARG JJJ CB  1 ? 38 
ATOM   12532 C CG  . ARG J  2 100 ? 33.824  -75.540  42.584  1.000 49.250  0 100 ARG JJJ CG  1 ? 38 
ATOM   12533 C CD  . ARG J  2 100 ? 35.320  -75.414  42.434  1.000 52.083  0 100 ARG JJJ CD  1 ? 38 
ATOM   12534 N NE  . ARG J  2 100 ? 35.973  -75.188  43.719  1.000 52.575  0 100 ARG JJJ NE  1 ? 38 
ATOM   12535 C CZ  . ARG J  2 100 ? 36.294  -74.000  44.215  1.000 54.038  0 100 ARG JJJ CZ  1 ? 38 
ATOM   12536 N NH1 . ARG J  2 100 ? 36.047  -72.886  43.541  1.000 53.805  0 100 ARG JJJ NH1 1 ? 38 
ATOM   12537 N NH2 . ARG J  2 100 ? 36.944  -73.952  45.370  1.000 56.010  0 100 ARG JJJ NH2 1 ? 38 
ATOM   12538 N N   . GLY J  2 101 ? 32.287  -79.155  45.108  1.000 44.116  0 101 GLY JJJ N   1 ? 38 
ATOM   12539 C CA  . GLY J  2 101 ? 31.904  -79.801  46.370  1.000 42.496  0 101 GLY JJJ CA  1 ? 38 
ATOM   12540 C C   . GLY J  2 101 ? 31.998  -81.310  46.295  1.000 42.982  0 101 GLY JJJ C   1 ? 38 
ATOM   12541 O O   . GLY J  2 101 ? 31.701  -81.886  45.248  1.000 43.888  0 101 GLY JJJ O   1 ? 38 
ATOM   12542 N N   . GLU J  2 102 ? 32.360  -81.916  47.415  1.000 44.177  0 102 GLU JJJ N   1 ? 38 
ATOM   12543 C CA  . GLU J  2 102 ? 32.262  -83.373  47.682  1.000 44.488  0 102 GLU JJJ CA  1 ? 38 
ATOM   12544 C C   . GLU J  2 102 ? 30.955  -83.590  48.438  1.000 44.715  0 102 GLU JJJ C   1 ? 38 
ATOM   12545 O O   . GLU J  2 102 ? 30.783  -82.984  49.529  1.000 43.463  0 102 GLU JJJ O   1 ? 38 
ATOM   12546 C CB  . GLU J  2 102 ? 33.479  -83.828  48.492  1.000 45.194  0 102 GLU JJJ CB  1 ? 38 
ATOM   12547 C CG  . GLU J  2 102 ? 33.526  -85.311  48.748  1.000 46.469  0 102 GLU JJJ CG  1 ? 38 
ATOM   12548 C CD  . GLU J  2 102 ? 34.662  -85.745  49.667  1.000 47.692  0 102 GLU JJJ CD  1 ? 38 
ATOM   12549 O OE1 . GLU J  2 102 ? 35.675  -85.015  49.747  1.000 48.507  0 102 GLU JJJ OE1 1 ? 38 
ATOM   12550 O OE2 . GLU J  2 102 ? 34.535  -86.811  50.277  1.000 46.965  0 102 GLU JJJ OE2 1 ? 38 
ATOM   12551 N N   . SER J  2 103 ? 30.059  -84.398  47.868  1.000 47.131  0 103 SER JJJ N   1 ? 38 
ATOM   12552 C CA  . SER J  2 103 ? 28.680  -84.596  48.393  1.000 48.473  0 103 SER JJJ CA  1 ? 38 
ATOM   12553 C C   . SER J  2 103 ? 28.663  -85.777  49.362  1.000 47.597  0 103 SER JJJ C   1 ? 38 
ATOM   12554 O O   . SER J  2 103 ? 29.253  -86.819  49.078  1.000 46.256  0 103 SER JJJ O   1 ? 38 
ATOM   12555 C CB  . SER J  2 103 ? 27.674  -84.806  47.295  1.000 51.788  0 103 SER JJJ CB  1 ? 38 
ATOM   12556 O OG  . SER J  2 103 ? 26.385  -85.003  47.847  1.000 54.371  0 103 SER JJJ OG  1 ? 38 
ATOM   12557 N N   . TYR J  2 104 ? 27.957  -85.630  50.470  1.000 48.828  0 104 TYR JJJ N   1 ? 38 
ATOM   12558 C CA  . TYR J  2 104 ? 27.578  -86.794  51.292  1.000 50.284  0 104 TYR JJJ CA  1 ? 38 
ATOM   12559 C C   . TYR J  2 104 ? 26.743  -87.728  50.418  1.000 51.540  0 104 TYR JJJ C   1 ? 38 
ATOM   12560 O O   . TYR J  2 104 ? 26.881  -88.934  50.614  1.000 54.376  0 104 TYR JJJ O   1 ? 38 
ATOM   12561 C CB  . TYR J  2 104 ? 26.831  -86.351  52.538  1.000 52.104  0 104 TYR JJJ CB  1 ? 38 
ATOM   12562 C CG  . TYR J  2 104 ? 26.438  -87.504  53.413  1.000 54.483  0 104 TYR JJJ CG  1 ? 38 
ATOM   12563 C CD1 . TYR J  2 104 ? 27.405  -88.222  54.092  1.000 55.421  0 104 TYR JJJ CD1 1 ? 38 
ATOM   12564 C CD2 . TYR J  2 104 ? 25.115  -87.885  53.551  1.000 57.440  0 104 TYR JJJ CD2 1 ? 38 
ATOM   12565 C CE1 . TYR J  2 104 ? 27.065  -89.262  54.939  1.000 57.635  0 104 TYR JJJ CE1 1 ? 38 
ATOM   12566 C CE2 . TYR J  2 104 ? 24.753  -88.921  54.403  1.000 60.166  0 104 TYR JJJ CE2 1 ? 38 
ATOM   12567 C CZ  . TYR J  2 104 ? 25.739  -89.618  55.091  1.000 59.682  0 104 TYR JJJ CZ  1 ? 38 
ATOM   12568 O OH  . TYR J  2 104 ? 25.444  -90.657  55.920  1.000 61.655  0 104 TYR JJJ OH  1 ? 38 
ATOM   12569 N N   . TYR J  2 105 ? 25.918  -87.190  49.506  1.000 51.095  0 105 TYR JJJ N   1 ? 38 
ATOM   12570 C CA  . TYR J  2 105 ? 25.091  -87.983  48.548  1.000 52.192  0 105 TYR JJJ CA  1 ? 38 
ATOM   12571 C C   . TYR J  2 105 ? 25.837  -88.102  47.198  1.000 50.656  0 105 TYR JJJ C   1 ? 38 
ATOM   12572 O O   . TYR J  2 105 ? 25.322  -87.693  46.126  1.000 48.958  0 105 TYR JJJ O   1 ? 38 
ATOM   12573 C CB  . TYR J  2 105 ? 23.690  -87.381  48.403  1.000 54.087  0 105 TYR JJJ CB  1 ? 38 
ATOM   12574 C CG  . TYR J  2 105 ? 22.973  -86.993  49.680  1.000 56.511  0 105 TYR JJJ CG  1 ? 38 
ATOM   12575 C CD1 . TYR J  2 105 ? 22.622  -87.923  50.660  1.000 57.817  0 105 TYR JJJ CD1 1 ? 38 
ATOM   12576 C CD2 . TYR J  2 105 ? 22.597  -85.675  49.898  1.000 56.300  0 105 TYR JJJ CD2 1 ? 38 
ATOM   12577 C CE1 . TYR J  2 105 ? 21.984  -87.542  51.825  1.000 59.257  0 105 TYR JJJ CE1 1 ? 38 
ATOM   12578 C CE2 . TYR J  2 105 ? 21.924  -85.281  51.053  1.000 55.995  0 105 TYR JJJ CE2 1 ? 38 
ATOM   12579 C CZ  . TYR J  2 105 ? 21.623  -86.220  52.022  1.000 58.674  0 105 TYR JJJ CZ  1 ? 38 
ATOM   12580 O OH  . TYR J  2 105 ? 20.970  -85.861  53.170  1.000 59.878  0 105 TYR JJJ OH  1 ? 38 
ATOM   12581 N N   . TYR J  2 106 ? 27.041  -88.666  47.239  1.000 49.858  0 106 TYR JJJ N   1 ? 38 
ATOM   12582 C CA  . TYR J  2 106 ? 28.014  -88.647  46.108  1.000 50.267  0 106 TYR JJJ CA  1 ? 38 
ATOM   12583 C C   . TYR J  2 106 ? 27.493  -89.427  44.904  1.000 51.583  0 106 TYR JJJ C   1 ? 38 
ATOM   12584 O O   . TYR J  2 106 ? 28.082  -89.251  43.831  1.000 55.718  0 106 TYR JJJ O   1 ? 38 
ATOM   12585 C CB  . TYR J  2 106 ? 29.383  -89.220  46.508  1.000 50.167  0 106 TYR JJJ CB  1 ? 38 
ATOM   12586 C CG  . TYR J  2 106 ? 29.328  -90.604  47.106  1.000 52.975  0 106 TYR JJJ CG  1 ? 38 
ATOM   12587 C CD1 . TYR J  2 106 ? 29.073  -90.771  48.461  1.000 52.963  0 106 TYR JJJ CD1 1 ? 38 
ATOM   12588 C CD2 . TYR J  2 106 ? 29.322  -91.733  46.289  1.000 54.099  0 106 TYR JJJ CD2 1 ? 38 
ATOM   12589 C CE1 . TYR J  2 106 ? 28.935  -92.034  49.011  1.000 55.538  0 106 TYR JJJ CE1 1 ? 38 
ATOM   12590 C CE2 . TYR J  2 106 ? 29.217  -92.996  46.835  1.000 56.829  0 106 TYR JJJ CE2 1 ? 38 
ATOM   12591 C CZ  . TYR J  2 106 ? 29.031  -93.144  48.196  1.000 56.886  0 106 TYR JJJ CZ  1 ? 38 
ATOM   12592 O OH  . TYR J  2 106 ? 28.867  -94.386  48.712  1.000 61.187  0 106 TYR JJJ OH  1 ? 38 
ATOM   12593 N N   . THR J  2 107 ? 26.471  -90.267  45.050  1.000 50.669  0 107 THR JJJ N   1 ? 39 
ATOM   12594 C CA  . THR J  2 107 ? 25.898  -91.057  43.909  1.000 51.376  0 107 THR JJJ CA  1 ? 39 
ATOM   12595 C C   . THR J  2 107 ? 24.824  -90.237  43.168  1.000 50.630  0 107 THR JJJ C   1 ? 39 
ATOM   12596 O O   . THR J  2 107 ? 24.383  -90.699  42.115  1.000 50.748  0 107 THR JJJ O   1 ? 39 
ATOM   12597 C CB  . THR J  2 107 ? 25.310  -92.407  44.348  1.000 51.351  0 107 THR JJJ CB  1 ? 39 
ATOM   12598 O OG1 . THR J  2 107 ? 24.088  -92.175  45.048  1.000 51.409  0 107 THR JJJ OG1 1 ? 39 
ATOM   12599 C CG2 . THR J  2 107 ? 26.256  -93.200  45.221  1.000 52.452  0 107 THR JJJ CG2 1 ? 39 
ATOM   12600 N N   . ARG J  2 108 ? 24.401  -89.083  43.679  1.000 51.288  0 108 ARG JJJ N   1 ? 39 
ATOM   12601 C CA  . ARG J  2 108 ? 23.332  -88.278  43.017  1.000 52.882  0 108 ARG JJJ CA  1 ? 39 
ATOM   12602 C C   . ARG J  2 108 ? 23.897  -87.457  41.859  1.000 51.354  0 108 ARG JJJ C   1 ? 39 
ATOM   12603 O O   . ARG J  2 108 ? 24.769  -86.620  42.051  1.000 50.799  0 108 ARG JJJ O   1 ? 39 
ATOM   12604 C CB  . ARG J  2 108 ? 22.683  -87.297  43.994  1.000 54.953  0 108 ARG JJJ CB  1 ? 39 
ATOM   12605 C CG  . ARG J  2 108 ? 21.837  -87.978  45.056  1.000 56.371  0 108 ARG JJJ CG  1 ? 39 
ATOM   12606 C CD  . ARG J  2 108 ? 21.009  -86.968  45.783  1.000 58.626  0 108 ARG JJJ CD  1 ? 39 
ATOM   12607 N NE  . ARG J  2 108 ? 20.483  -87.511  47.012  1.000 61.462  0 108 ARG JJJ NE  1 ? 39 
ATOM   12608 C CZ  . ARG J  2 108 ? 19.892  -86.774  47.952  1.000 65.453  0 108 ARG JJJ CZ  1 ? 39 
ATOM   12609 N NH1 . ARG J  2 108 ? 19.739  -85.467  47.791  1.000 66.407  0 108 ARG JJJ NH1 1 ? 39 
ATOM   12610 N NH2 . ARG J  2 108 ? 19.460  -87.327  49.072  1.000 68.458  0 108 ARG JJJ NH2 1 ? 39 
ATOM   12611 N N   . PRO J  2 109 ? 23.422  -87.660  40.617  1.000 50.156  0 109 PRO JJJ N   1 ? 39 
ATOM   12612 C CA  . PRO J  2 109 ? 23.810  -86.800  39.497  1.000 48.474  0 109 PRO JJJ CA  1 ? 39 
ATOM   12613 C C   . PRO J  2 109 ? 23.607  -85.292  39.755  1.000 48.869  0 109 PRO JJJ C   1 ? 39 
ATOM   12614 O O   . PRO J  2 109 ? 24.454  -84.531  39.325  1.000 46.241  0 109 PRO JJJ O   1 ? 39 
ATOM   12615 C CB  . PRO J  2 109 ? 22.878  -87.276  38.371  1.000 50.513  0 109 PRO JJJ CB  1 ? 39 
ATOM   12616 C CG  . PRO J  2 109 ? 22.611  -88.731  38.698  1.000 51.171  0 109 PRO JJJ CG  1 ? 39 
ATOM   12617 C CD  . PRO J  2 109 ? 22.535  -88.767  40.213  1.000 51.610  0 109 PRO JJJ CD  1 ? 39 
ATOM   12618 N N   . THR J  2 110 ? 22.541  -84.892  40.462  1.000 50.310  0 110 THR JJJ N   1 ? 39 
ATOM   12619 C CA  . THR J  2 110 ? 22.215  -83.469  40.776  1.000 50.736  0 110 THR JJJ CA  1 ? 39 
ATOM   12620 C C   . THR J  2 110 ? 23.301  -82.825  41.654  1.000 50.881  0 110 THR JJJ C   1 ? 39 
ATOM   12621 O O   . THR J  2 110 ? 23.343  -81.601  41.694  1.000 51.702  0 110 THR JJJ O   1 ? 39 
ATOM   12622 C CB  . THR J  2 110 ? 20.843  -83.287  41.462  1.000 52.135  0 110 THR JJJ CB  1 ? 39 
ATOM   12623 O OG1 . THR J  2 110 ? 20.762  -84.180  42.571  1.000 51.873  0 110 THR JJJ OG1 1 ? 39 
ATOM   12624 C CG2 . THR J  2 110 ? 19.654  -83.473  40.545  1.000 52.468  0 110 THR JJJ CG2 1 ? 39 
ATOM   12625 N N   . GLU J  2 111 ? 24.171  -83.593  42.309  1.000 51.209  0 111 GLU JJJ N   1 ? 39 
ATOM   12626 C CA  . GLU J  2 111 ? 25.278  -83.032  43.125  1.000 52.022  0 111 GLU JJJ CA  1 ? 39 
ATOM   12627 C C   . GLU J  2 111 ? 26.483  -82.652  42.249  1.000 51.611  0 111 GLU JJJ C   1 ? 39 
ATOM   12628 O O   . GLU J  2 111 ? 27.434  -82.097  42.806  1.000 56.255  0 111 GLU JJJ O   1 ? 39 
ATOM   12629 C CB  . GLU J  2 111 ? 25.674  -84.021  44.226  1.000 52.613  0 111 GLU JJJ CB  1 ? 39 
ATOM   12630 C CG  . GLU J  2 111 ? 24.619  -84.181  45.313  1.000 54.255  0 111 GLU JJJ CG  1 ? 39 
ATOM   12631 C CD  . GLU J  2 111 ? 24.447  -82.950  46.203  1.000 54.938  0 111 GLU JJJ CD  1 ? 39 
ATOM   12632 O OE1 . GLU J  2 111 ? 23.892  -81.957  45.701  1.000 55.399  0 111 GLU JJJ OE1 1 ? 39 
ATOM   12633 O OE2 . GLU J  2 111 ? 24.850  -82.986  47.409  1.000 52.880  0 111 GLU JJJ OE2 1 ? 39 
ATOM   12634 N N   . TYR J  2 112 ? 26.471  -82.905  40.945  1.000 52.024  0 112 TYR JJJ N   1 ? 39 
ATOM   12635 C CA  . TYR J  2 112 ? 27.604  -82.557  40.034  1.000 52.955  0 112 TYR JJJ CA  1 ? 39 
ATOM   12636 C C   . TYR J  2 112 ? 27.136  -81.524  38.992  1.000 52.012  0 112 TYR JJJ C   1 ? 39 
ATOM   12637 O O   . TYR J  2 112 ? 26.235  -81.819  38.219  1.000 52.322  0 112 TYR JJJ O   1 ? 39 
ATOM   12638 C CB  . TYR J  2 112 ? 28.186  -83.827  39.410  1.000 51.727  0 112 TYR JJJ CB  1 ? 39 
ATOM   12639 C CG  . TYR J  2 112 ? 28.638  -84.840  40.425  1.000 53.123  0 112 TYR JJJ CG  1 ? 39 
ATOM   12640 C CD1 . TYR J  2 112 ? 27.754  -85.736  40.998  1.000 53.358  0 112 TYR JJJ CD1 1 ? 39 
ATOM   12641 C CD2 . TYR J  2 112 ? 29.959  -84.887  40.838  1.000 53.179  0 112 TYR JJJ CD2 1 ? 39 
ATOM   12642 C CE1 . TYR J  2 112 ? 28.176  -86.660  41.946  1.000 51.984  0 112 TYR JJJ CE1 1 ? 39 
ATOM   12643 C CE2 . TYR J  2 112 ? 30.392  -85.798  41.787  1.000 52.278  0 112 TYR JJJ CE2 1 ? 39 
ATOM   12644 C CZ  . TYR J  2 112 ? 29.501  -86.706  42.327  1.000 51.432  0 112 TYR JJJ CZ  1 ? 39 
ATOM   12645 O OH  . TYR J  2 112 ? 29.931  -87.588  43.278  1.000 49.779  0 112 TYR JJJ OH  1 ? 39 
ATOM   12646 N N   . GLU J  2 113 ? 27.737  -80.340  38.980  1.000 51.612  0 113 GLU JJJ N   1 ? 39 
ATOM   12647 C CA  . GLU J  2 113 ? 27.318  -79.252  38.066  1.000 52.840  0 113 GLU JJJ CA  1 ? 39 
ATOM   12648 C C   . GLU J  2 113 ? 27.730  -79.545  36.611  1.000 50.960  0 113 GLU JJJ C   1 ? 39 
ATOM   12649 O O   . GLU J  2 113 ? 26.954  -79.218  35.726  1.000 49.512  0 113 GLU JJJ O   1 ? 39 
ATOM   12650 C CB  . GLU J  2 113 ? 27.912  -77.916  38.498  1.000 56.166  0 113 GLU JJJ CB  1 ? 39 
ATOM   12651 C CG  . GLU J  2 113 ? 27.407  -76.782  37.628  1.000 60.526  0 113 GLU JJJ CG  1 ? 39 
ATOM   12652 C CD  . GLU J  2 113 ? 27.806  -75.386  38.045  1.000 65.817  0 113 GLU JJJ CD  1 ? 39 
ATOM   12653 O OE1 . GLU J  2 113 ? 28.441  -75.257  39.123  1.000 68.813  0 113 GLU JJJ OE1 1 ? 39 
ATOM   12654 O OE2 . GLU J  2 113 ? 27.501  -74.440  37.275  1.000 69.221  0 113 GLU JJJ OE2 1 ? 39 
ATOM   12655 N N   . PHE J  2 114 ? 28.919  -80.104  36.374  1.000 50.984  0 114 PHE JJJ N   1 ? 39 
ATOM   12656 C CA  . PHE J  2 114 ? 29.550  -80.218  35.032  1.000 49.106  0 114 PHE JJJ CA  1 ? 39 
ATOM   12657 C C   . PHE J  2 114 ? 29.589  -81.672  34.584  1.000 49.170  0 114 PHE JJJ C   1 ? 39 
ATOM   12658 O O   . PHE J  2 114 ? 30.007  -82.540  35.361  1.000 50.599  0 114 PHE JJJ O   1 ? 39 
ATOM   12659 C CB  . PHE J  2 114 ? 30.956  -79.622  35.054  1.000 48.016  0 114 PHE JJJ CB  1 ? 39 
ATOM   12660 C CG  . PHE J  2 114 ? 30.939  -78.162  35.404  1.000 49.643  0 114 PHE JJJ CG  1 ? 39 
ATOM   12661 C CD1 . PHE J  2 114 ? 30.292  -77.254  34.576  1.000 50.104  0 114 PHE JJJ CD1 1 ? 39 
ATOM   12662 C CD2 . PHE J  2 114 ? 31.506  -77.704  36.582  1.000 48.391  0 114 PHE JJJ CD2 1 ? 39 
ATOM   12663 C CE1 . PHE J  2 114 ? 30.233  -75.910  34.908  1.000 51.468  0 114 PHE JJJ CE1 1 ? 39 
ATOM   12664 C CE2 . PHE J  2 114 ? 31.453  -76.357  36.912  1.000 50.116  0 114 PHE JJJ CE2 1 ? 39 
ATOM   12665 C CZ  . PHE J  2 114 ? 30.821  -75.458  36.068  1.000 51.416  0 114 PHE JJJ CZ  1 ? 39 
ATOM   12666 N N   . TRP J  2 115 ? 29.198  -81.901  33.331  1.000 48.412  0 115 TRP JJJ N   1 ? 39 
ATOM   12667 C CA  . TRP J  2 115 ? 29.106  -83.235  32.693  1.000 47.373  0 115 TRP JJJ CA  1 ? 39 
ATOM   12668 C C   . TRP J  2 115 ? 29.755  -83.205  31.313  1.000 46.813  0 115 TRP JJJ C   1 ? 39 
ATOM   12669 O O   . TRP J  2 115 ? 29.433  -82.296  30.523  1.000 46.317  0 115 TRP JJJ O   1 ? 39 
ATOM   12670 C CB  . TRP J  2 115 ? 27.637  -83.646  32.593  1.000 48.298  0 115 TRP JJJ CB  1 ? 39 
ATOM   12671 C CG  . TRP J  2 115 ? 27.023  -83.913  33.928  1.000 48.381  0 115 TRP JJJ CG  1 ? 39 
ATOM   12672 C CD1 . TRP J  2 115 ? 26.575  -82.995  34.836  1.000 48.754  0 115 TRP JJJ CD1 1 ? 39 
ATOM   12673 C CD2 . TRP J  2 115 ? 26.885  -85.195  34.553  1.000 48.994  0 115 TRP JJJ CD2 1 ? 39 
ATOM   12674 N NE1 . TRP J  2 115 ? 26.146  -83.622  35.971  1.000 49.542  0 115 TRP JJJ NE1 1 ? 39 
ATOM   12675 C CE2 . TRP J  2 115 ? 26.323  -84.971  35.831  1.000 50.231  0 115 TRP JJJ CE2 1 ? 39 
ATOM   12676 C CE3 . TRP J  2 115 ? 27.173  -86.501  34.156  1.000 50.008  0 115 TRP JJJ CE3 1 ? 39 
ATOM   12677 C CZ2 . TRP J  2 115 ? 26.034  -86.012  36.710  1.000 51.496  0 115 TRP JJJ CZ2 1 ? 39 
ATOM   12678 C CZ3 . TRP J  2 115 ? 26.878  -87.529  35.014  1.000 51.259  0 115 TRP JJJ CZ3 1 ? 39 
ATOM   12679 C CH2 . TRP J  2 115 ? 26.319  -87.287  36.276  1.000 51.039  0 115 TRP JJJ CH2 1 ? 39 
ATOM   12680 N N   . GLY J  2 116 ? 30.593  -84.196  31.016  1.000 45.390  0 116 GLY JJJ N   1 ? 39 
ATOM   12681 C CA  . GLY J  2 116 ? 31.035  -84.486  29.638  1.000 45.028  0 116 GLY JJJ CA  1 ? 39 
ATOM   12682 C C   . GLY J  2 116 ? 29.878  -84.999  28.797  1.000 45.321  0 116 GLY JJJ C   1 ? 39 
ATOM   12683 O O   . GLY J  2 116 ? 28.795  -85.241  29.383  1.000 46.161  0 116 GLY JJJ O   1 ? 39 
ATOM   12684 N N   . GLN J  2 117 ? 30.086  -85.199  27.495  1.000 46.591  0 117 GLN JJJ N   1 ? 39 
ATOM   12685 C CA  . GLN J  2 117 ? 29.049  -85.729  26.566  1.000 48.578  0 117 GLN JJJ CA  1 ? 39 
ATOM   12686 C C   . GLN J  2 117 ? 29.008  -87.253  26.664  1.000 51.532  0 117 GLN JJJ C   1 ? 39 
ATOM   12687 O O   . GLN J  2 117 ? 27.998  -87.851  26.211  1.000 54.794  0 117 GLN JJJ O   1 ? 39 
ATOM   12688 C CB  . GLN J  2 117 ? 29.319  -85.334  25.115  1.000 48.383  0 117 GLN JJJ CB  1 ? 39 
ATOM   12689 C CG  . GLN J  2 117 ? 29.409  -83.837  24.914  1.000 49.804  0 117 GLN JJJ CG  1 ? 39 
ATOM   12690 C CD  . GLN J  2 117 ? 28.140  -83.115  25.290  1.000 49.915  0 117 GLN JJJ CD  1 ? 39 
ATOM   12691 O OE1 . GLN J  2 117 ? 28.157  -82.101  25.975  1.000 51.874  0 117 GLN JJJ OE1 1 ? 39 
ATOM   12692 N NE2 . GLN J  2 117 ? 27.019  -83.629  24.846  1.000 50.580  0 117 GLN JJJ NE2 1 ? 39 
ATOM   12693 N N   . GLY J  2 118 ? 30.070  -87.860  27.211  1.000 51.563  0 118 GLY JJJ N   1 ? 39 
ATOM   12694 C CA  . GLY J  2 118 ? 30.180  -89.317  27.374  1.000 51.417  0 118 GLY JJJ CA  1 ? 39 
ATOM   12695 C C   . GLY J  2 118 ? 30.899  -89.968  26.212  1.000 52.805  0 118 GLY JJJ C   1 ? 39 
ATOM   12696 O O   . GLY J  2 118 ? 30.975  -89.362  25.118  1.000 51.543  0 118 GLY JJJ O   1 ? 39 
ATOM   12697 N N   . THR J  2 119 ? 31.392  -91.180  26.439  1.000 53.676  0 119 THR JJJ N   1 ? 39 
ATOM   12698 C CA  . THR J  2 119 ? 32.090  -92.005  25.428  1.000 55.396  0 119 THR JJJ CA  1 ? 39 
ATOM   12699 C C   . THR J  2 119 ? 31.575  -93.432  25.588  1.000 58.126  0 119 THR JJJ C   1 ? 39 
ATOM   12700 O O   . THR J  2 119 ? 31.387  -93.883  26.747  1.000 56.698  0 119 THR JJJ O   1 ? 39 
ATOM   12701 C CB  . THR J  2 119 ? 33.603  -91.853  25.581  1.000 57.699  0 119 THR JJJ CB  1 ? 39 
ATOM   12702 O OG1 . THR J  2 119 ? 34.232  -92.378  24.419  1.000 59.363  0 119 THR JJJ OG1 1 ? 39 
ATOM   12703 C CG2 . THR J  2 119 ? 34.154  -92.530  26.818  1.000 59.450  0 119 THR JJJ CG2 1 ? 39 
ATOM   12704 N N   . GLN J  2 120 ? 31.313  -94.097  24.456  1.000 60.587  0 120 GLN JJJ N   1 ? 39 
ATOM   12705 C CA  . GLN J  2 120 ? 30.806  -95.486  24.425  1.000 60.631  0 120 GLN JJJ CA  1 ? 39 
ATOM   12706 C C   . GLN J  2 120 ? 31.938  -96.421  24.848  1.000 59.040  0 120 GLN JJJ C   1 ? 39 
ATOM   12707 O O   . GLN J  2 120 ? 33.043  -96.305  24.316  1.000 60.358  0 120 GLN JJJ O   1 ? 39 
ATOM   12708 C CB  . GLN J  2 120 ? 30.267  -95.810  23.029  1.000 64.366  0 120 GLN JJJ CB  1 ? 39 
ATOM   12709 C CG  . GLN J  2 120 ? 29.570  -97.155  22.924  1.000 67.062  0 120 GLN JJJ CG  1 ? 39 
ATOM   12710 C CD  . GLN J  2 120 ? 28.319  -97.236  23.766  1.000 69.605  0 120 GLN JJJ CD  1 ? 39 
ATOM   12711 O OE1 . GLN J  2 120 ? 27.462  -96.358  23.748  1.000 77.337  0 120 GLN JJJ OE1 1 ? 39 
ATOM   12712 N NE2 . GLN J  2 120 ? 28.197  -98.301  24.533  1.000 71.139  0 120 GLN JJJ NE2 1 ? 39 
ATOM   12713 N N   . VAL J  2 121 ? 31.654  -97.296  25.807  1.000 58.221  0 121 VAL JJJ N   1 ? 39 
ATOM   12714 C CA  . VAL J  2 121 ? 32.431  -98.532  26.096  1.000 59.101  0 121 VAL JJJ CA  1 ? 39 
ATOM   12715 C C   . VAL J  2 121 ? 31.539  -99.711  25.707  1.000 59.301  0 121 VAL JJJ C   1 ? 39 
ATOM   12716 O O   . VAL J  2 121 ? 30.395  -99.761  26.178  1.000 57.404  0 121 VAL JJJ O   1 ? 39 
ATOM   12717 C CB  . VAL J  2 121 ? 32.843  -98.601  27.572  1.000 58.536  0 121 VAL JJJ CB  1 ? 39 
ATOM   12718 C CG1 . VAL J  2 121 ? 33.498  -99.943  27.897  1.000 60.531  0 121 VAL JJJ CG1 1 ? 39 
ATOM   12719 C CG2 . VAL J  2 121 ? 33.731  -97.414  27.944  1.000 56.753  0 121 VAL JJJ CG2 1 ? 39 
ATOM   12720 N N   . THR J  2 122 ? 32.036  -100.587 24.838  1.000 61.273  0 122 THR JJJ N   1 ? 39 
ATOM   12721 C CA  . THR J  2 122 ? 31.310  -101.810 24.417  1.000 65.075  0 122 THR JJJ CA  1 ? 39 
ATOM   12722 C C   . THR J  2 122 ? 32.175  -103.016 24.790  1.000 68.680  0 122 THR JJJ C   1 ? 39 
ATOM   12723 O O   . THR J  2 122 ? 33.350  -103.062 24.353  1.000 70.566  0 122 THR JJJ O   1 ? 39 
ATOM   12724 C CB  . THR J  2 122 ? 30.940  -101.731 22.932  1.000 65.139  0 122 THR JJJ CB  1 ? 39 
ATOM   12725 O OG1 . THR J  2 122 ? 30.122  -100.577 22.781  1.000 64.472  0 122 THR JJJ OG1 1 ? 39 
ATOM   12726 C CG2 . THR J  2 122 ? 30.191  -102.937 22.422  1.000 66.998  0 122 THR JJJ CG2 1 ? 39 
ATOM   12727 N N   . VAL J  2 123 ? 31.613  -103.934 25.578  1.000 70.969  0 123 VAL JJJ N   1 ? 39 
ATOM   12728 C CA  . VAL J  2 123 ? 32.272  -105.210 25.974  1.000 75.857  0 123 VAL JJJ CA  1 ? 39 
ATOM   12729 C C   . VAL J  2 123 ? 31.541  -106.347 25.249  1.000 78.688  0 123 VAL JJJ C   1 ? 39 
ATOM   12730 O O   . VAL J  2 123 ? 30.382  -106.595 25.578  1.000 75.697  0 123 VAL JJJ O   1 ? 39 
ATOM   12731 C CB  . VAL J  2 123 ? 32.266  -105.356 27.509  1.000 76.780  0 123 VAL JJJ CB  1 ? 39 
ATOM   12732 C CG1 . VAL J  2 123 ? 33.127  -106.521 27.971  1.000 81.195  0 123 VAL JJJ CG1 1 ? 39 
ATOM   12733 C CG2 . VAL J  2 123 ? 32.712  -104.077 28.210  1.000 73.667  0 123 VAL JJJ CG2 1 ? 39 
ATOM   12734 N N   . SER J  2 124 ? 32.172  -106.959 24.240  1.000 86.422  0 124 SER JJJ N   1 ? 39 
ATOM   12735 C CA  . SER J  2 124 ? 31.645  -108.108 23.458  1.000 93.378  0 124 SER JJJ CA  1 ? 39 
ATOM   12736 C C   . SER J  2 124 ? 31.936  -109.401 24.222  1.000 104.338 0 124 SER JJJ C   1 ? 39 
ATOM   12737 O O   . SER J  2 124 ? 32.779  -109.354 25.122  1.000 104.548 0 124 SER JJJ O   1 ? 39 
ATOM   12738 C CB  . SER J  2 124 ? 32.257  -108.132 22.086  1.000 93.411  0 124 SER JJJ CB  1 ? 39 
ATOM   12739 O OG  . SER J  2 124 ? 33.670  -108.200 22.167  1.000 93.360  0 124 SER JJJ OG  1 ? 39 
ATOM   12740 N N   . SER J  2 125 ? 31.306  -110.523 23.851  1.000 71.434  0 125 SER JJJ N   1 ? ?  
ATOM   12741 C CA  . SER J  2 125 ? 31.440  -111.841 24.537  1.000 77.631  0 125 SER JJJ CA  1 ? ?  
ATOM   12742 C C   . SER J  2 125 ? 32.249  -112.809 23.662  1.000 79.076  0 125 SER JJJ C   1 ? ?  
ATOM   12743 O O   . SER J  2 125 ? 33.476  -112.844 23.775  1.000 72.636  0 125 SER JJJ O   1 ? ?  
ATOM   12744 C CB  . SER J  2 125 ? 30.084  -112.408 24.915  1.000 81.163  0 125 SER JJJ CB  1 ? ?  
ATOM   12745 O OG  . SER J  2 125 ? 29.776  -112.175 26.291  1.000 81.289  0 125 SER JJJ OG  1 ? ?  
ATOM   12746 N N   . ILE K  1 3   ? -24.497 -48.461  -20.625 1.000 109.212 0 332 ILE KKK N   1 ? ?  
ATOM   12747 C CA  . ILE K  1 3   ? -23.697 -47.982  -19.460 1.000 105.195 0 332 ILE KKK CA  1 ? ?  
ATOM   12748 C C   . ILE K  1 3   ? -22.566 -47.063  -19.963 1.000 94.388  0 332 ILE KKK C   1 ? ?  
ATOM   12749 O O   . ILE K  1 3   ? -21.801 -47.461  -20.825 1.000 103.898 0 332 ILE KKK O   1 ? ?  
ATOM   12750 C CB  . ILE K  1 3   ? -23.225 -49.194  -18.624 1.000 113.693 0 332 ILE KKK CB  1 ? ?  
ATOM   12751 C CG1 . ILE K  1 3   ? -24.409 -49.820  -17.872 1.000 105.567 0 332 ILE KKK CG1 1 ? ?  
ATOM   12752 C CG2 . ILE K  1 3   ? -22.090 -48.819  -17.676 1.000 117.155 0 332 ILE KKK CG2 1 ? ?  
ATOM   12753 C CD1 . ILE K  1 3   ? -24.620 -51.295  -18.148 1.000 99.173  0 332 ILE KKK CD1 1 ? ?  
ATOM   12754 N N   . THR K  1 4   ? -22.526 -45.850  -19.410 1.000 126.261 0 333 THR KKK N   1 ? 40 
ATOM   12755 C CA  . THR K  1 4   ? -21.821 -44.589  -19.805 1.000 113.712 0 333 THR KKK CA  1 ? 40 
ATOM   12756 C C   . THR K  1 4   ? -22.532 -43.458  -19.031 1.000 103.470 0 333 THR KKK C   1 ? 40 
ATOM   12757 O O   . THR K  1 4   ? -21.844 -42.582  -18.441 1.000 99.305  0 333 THR KKK O   1 ? 40 
ATOM   12758 C CB  . THR K  1 4   ? -21.854 -44.270  -21.319 1.000 113.602 0 333 THR KKK CB  1 ? 40 
ATOM   12759 O OG1 . THR K  1 4   ? -20.772 -44.896  -22.005 1.000 113.051 0 333 THR KKK OG1 1 ? 40 
ATOM   12760 C CG2 . THR K  1 4   ? -21.788 -42.790  -21.640 1.000 110.902 0 333 THR KKK CG2 1 ? 40 
ATOM   12761 N N   . ASN K  1 5   ? -23.874 -43.474  -19.047 1.000 95.143  0 334 ASN KKK N   1 ? 40 
ATOM   12762 C CA  . ASN K  1 5   ? -24.763 -42.483  -18.415 1.000 87.867  0 334 ASN KKK CA  1 ? 40 
ATOM   12763 C C   . ASN K  1 5   ? -24.732 -42.666  -16.897 1.000 79.676  0 334 ASN KKK C   1 ? 40 
ATOM   12764 O O   . ASN K  1 5   ? -24.902 -43.796  -16.416 1.000 77.276  0 334 ASN KKK O   1 ? 40 
ATOM   12765 C CB  . ASN K  1 5   ? -26.183 -42.634  -18.953 1.000 91.329  0 334 ASN KKK CB  1 ? 40 
ATOM   12766 C CG  . ASN K  1 5   ? -26.703 -44.053  -18.828 1.000 93.479  0 334 ASN KKK CG  1 ? 40 
ATOM   12767 O OD1 . ASN K  1 5   ? -26.035 -45.007  -19.223 1.000 93.397  0 334 ASN KKK OD1 1 ? 40 
ATOM   12768 N ND2 . ASN K  1 5   ? -27.878 -44.190  -18.246 1.000 94.497  0 334 ASN KKK ND2 1 ? 40 
ATOM   12769 N N   . LEU K  1 6   ? -24.563 -41.567  -16.163 1.000 74.172  0 335 LEU KKK N   1 ? 40 
ATOM   12770 C CA  . LEU K  1 6   ? -24.443 -41.592  -14.689 1.000 70.254  0 335 LEU KKK CA  1 ? 40 
ATOM   12771 C C   . LEU K  1 6   ? -25.830 -41.837  -14.102 1.000 67.450  0 335 LEU KKK C   1 ? 40 
ATOM   12772 O O   . LEU K  1 6   ? -26.814 -41.422  -14.710 1.000 68.450  0 335 LEU KKK O   1 ? 40 
ATOM   12773 C CB  . LEU K  1 6   ? -23.812 -40.288  -14.197 1.000 69.624  0 335 LEU KKK CB  1 ? 40 
ATOM   12774 C CG  . LEU K  1 6   ? -22.359 -40.068  -14.650 1.000 71.507  0 335 LEU KKK CG  1 ? 40 
ATOM   12775 C CD1 . LEU K  1 6   ? -21.810 -38.749  -14.129 1.000 70.548  0 335 LEU KKK CD1 1 ? 40 
ATOM   12776 C CD2 . LEU K  1 6   ? -21.447 -41.219  -14.224 1.000 71.829  0 335 LEU KKK CD2 1 ? 40 
ATOM   12777 N N   . CYS K  1 7   ? -25.889 -42.566  -12.987 1.000 66.165  0 336 CYS KKK N   1 ? 40 
ATOM   12778 C CA  . CYS K  1 7   ? -27.146 -42.865  -12.270 1.000 65.662  0 336 CYS KKK CA  1 ? 40 
ATOM   12779 C C   . CYS K  1 7   ? -27.746 -41.554  -11.798 1.000 66.096  0 336 CYS KKK C   1 ? 40 
ATOM   12780 O O   . CYS K  1 7   ? -27.023 -40.708  -11.289 1.000 68.727  0 336 CYS KKK O   1 ? 40 
ATOM   12781 C CB  . CYS K  1 7   ? -26.890 -43.834  -11.122 1.000 65.664  0 336 CYS KKK CB  1 ? 40 
ATOM   12782 S SG  . CYS K  1 7   ? -26.479 -45.532  -11.663 1.000 69.622  0 336 CYS KKK SG  1 ? 40 
ATOM   12783 N N   . PRO K  1 8   ? -29.066 -41.333  -11.966 1.000 67.582  0 337 PRO KKK N   1 ? 40 
ATOM   12784 C CA  . PRO K  1 8   ? -29.681 -40.042  -11.662 1.000 64.950  0 337 PRO KKK CA  1 ? 40 
ATOM   12785 C C   . PRO K  1 8   ? -29.957 -39.863  -10.160 1.000 63.347  0 337 PRO KKK C   1 ? 40 
ATOM   12786 O O   . PRO K  1 8   ? -31.103 -39.718  -9.770  1.000 64.807  0 337 PRO KKK O   1 ? 40 
ATOM   12787 C CB  . PRO K  1 8   ? -30.963 -40.120  -12.506 1.000 68.046  0 337 PRO KKK CB  1 ? 40 
ATOM   12788 C CG  . PRO K  1 8   ? -31.370 -41.573  -12.399 1.000 69.294  0 337 PRO KKK CG  1 ? 40 
ATOM   12789 C CD  . PRO K  1 8   ? -30.051 -42.325  -12.430 1.000 69.262  0 337 PRO KKK CD  1 ? 40 
ATOM   12790 N N   . PHE K  1 9   ? -28.895 -39.819  -9.348  1.000 61.182  0 338 PHE KKK N   1 ? 40 
ATOM   12791 C CA  . PHE K  1 9   ? -28.927 -39.528  -7.900  1.000 58.992  0 338 PHE KKK CA  1 ? 40 
ATOM   12792 C C   . PHE K  1 9   ? -29.487 -38.114  -7.678  1.000 58.324  0 338 PHE KKK C   1 ? 40 
ATOM   12793 O O   . PHE K  1 9   ? -30.199 -37.931  -6.671  1.000 60.143  0 338 PHE KKK O   1 ? 40 
ATOM   12794 C CB  . PHE K  1 9   ? -27.528 -39.676  -7.295  1.000 59.702  0 338 PHE KKK CB  1 ? 40 
ATOM   12795 C CG  . PHE K  1 9   ? -27.014 -41.085  -7.163  1.000 61.992  0 338 PHE KKK CG  1 ? 40 
ATOM   12796 C CD1 . PHE K  1 9   ? -27.824 -42.076  -6.641  1.000 64.268  0 338 PHE KKK CD1 1 ? 40 
ATOM   12797 C CD2 . PHE K  1 9   ? -25.709 -41.414  -7.502  1.000 63.888  0 338 PHE KKK CD2 1 ? 40 
ATOM   12798 C CE1 . PHE K  1 9   ? -27.378 -43.390  -6.528  1.000 66.036  0 338 PHE KKK CE1 1 ? 40 
ATOM   12799 C CE2 . PHE K  1 9   ? -25.248 -42.717  -7.362  1.000 66.178  0 338 PHE KKK CE2 1 ? 40 
ATOM   12800 C CZ  . PHE K  1 9   ? -26.065 -43.703  -6.839  1.000 67.151  0 338 PHE KKK CZ  1 ? 40 
ATOM   12801 N N   . GLY K  1 10  ? -29.186 -37.152  -8.557  1.000 57.678  0 339 GLY KKK N   1 ? 40 
ATOM   12802 C CA  . GLY K  1 10  ? -29.692 -35.769  -8.460  1.000 58.970  0 339 GLY KKK CA  1 ? 40 
ATOM   12803 C C   . GLY K  1 10  ? -31.209 -35.721  -8.354  1.000 59.057  0 339 GLY KKK C   1 ? 40 
ATOM   12804 O O   . GLY K  1 10  ? -31.712 -34.963  -7.493  1.000 57.335  0 339 GLY KKK O   1 ? 40 
ATOM   12805 N N   . GLU K  1 11  ? -31.917 -36.536  -9.156  1.000 61.560  0 340 GLU KKK N   1 ? 40 
ATOM   12806 C CA  . GLU K  1 11  ? -33.402 -36.568  -9.175  1.000 63.690  0 340 GLU KKK CA  1 ? 40 
ATOM   12807 C C   . GLU K  1 11  ? -33.961 -37.007  -7.817  1.000 61.337  0 340 GLU KKK C   1 ? 40 
ATOM   12808 O O   . GLU K  1 11  ? -35.122 -36.615  -7.501  1.000 61.738  0 340 GLU KKK O   1 ? 40 
ATOM   12809 C CB  . GLU K  1 11  ? -33.919 -37.519  -10.239 1.000 67.777  0 340 GLU KKK CB  1 ? 40 
ATOM   12810 C CG  . GLU K  1 11  ? -33.537 -37.070  -11.631 1.000 73.569  0 340 GLU KKK CG  1 ? 40 
ATOM   12811 C CD  . GLU K  1 11  ? -34.052 -37.973  -12.731 1.000 79.553  0 340 GLU KKK CD  1 ? 40 
ATOM   12812 O OE1 . GLU K  1 11  ? -34.875 -38.873  -12.411 1.000 81.473  0 340 GLU KKK OE1 1 ? 40 
ATOM   12813 O OE2 . GLU K  1 11  ? -33.623 -37.770  -13.895 1.000 82.949  0 340 GLU KKK OE2 1 ? 40 
ATOM   12814 N N   . VAL K  1 12  ? -33.172 -37.803  -7.072  1.000 56.637  0 341 VAL KKK N   1 ? 40 
ATOM   12815 C CA  . VAL K  1 12  ? -33.567 -38.342  -5.743  1.000 54.129  0 341 VAL KKK CA  1 ? 40 
ATOM   12816 C C   . VAL K  1 12  ? -33.226 -37.321  -4.650  1.000 52.283  0 341 VAL KKK C   1 ? 40 
ATOM   12817 O O   . VAL K  1 12  ? -34.145 -36.909  -3.924  1.000 51.408  0 341 VAL KKK O   1 ? 40 
ATOM   12818 C CB  . VAL K  1 12  ? -32.868 -39.691  -5.477  1.000 53.710  0 341 VAL KKK CB  1 ? 40 
ATOM   12819 C CG1 . VAL K  1 12  ? -33.218 -40.241  -4.089  1.000 54.273  0 341 VAL KKK CG1 1 ? 40 
ATOM   12820 C CG2 . VAL K  1 12  ? -33.172 -40.696  -6.584  1.000 55.411  0 341 VAL KKK CG2 1 ? 40 
ATOM   12821 N N   . PHE K  1 13  ? -31.939 -36.974  -4.506  1.000 50.808  0 342 PHE KKK N   1 ? 40 
ATOM   12822 C CA  . PHE K  1 13  ? -31.398 -36.183  -3.370  1.000 50.483  0 342 PHE KKK CA  1 ? 40 
ATOM   12823 C C   . PHE K  1 13  ? -31.886 -34.729  -3.469  1.000 52.347  0 342 PHE KKK C   1 ? 40 
ATOM   12824 O O   . PHE K  1 13  ? -32.076 -34.103  -2.402  1.000 52.795  0 342 PHE KKK O   1 ? 40 
ATOM   12825 C CB  . PHE K  1 13  ? -29.871 -36.252  -3.363  1.000 49.351  0 342 PHE KKK CB  1 ? 40 
ATOM   12826 C CG  . PHE K  1 13  ? -29.316 -37.524  -2.795  1.000 48.857  0 342 PHE KKK CG  1 ? 40 
ATOM   12827 C CD1 . PHE K  1 13  ? -29.189 -38.658  -3.577  1.000 48.126  0 342 PHE KKK CD1 1 ? 40 
ATOM   12828 C CD2 . PHE K  1 13  ? -28.910 -37.585  -1.480  1.000 50.013  0 342 PHE KKK CD2 1 ? 40 
ATOM   12829 C CE1 . PHE K  1 13  ? -28.647 -39.826  -3.060  1.000 49.032  0 342 PHE KKK CE1 1 ? 40 
ATOM   12830 C CE2 . PHE K  1 13  ? -28.397 -38.762  -0.957  1.000 51.972  0 342 PHE KKK CE2 1 ? 40 
ATOM   12831 C CZ  . PHE K  1 13  ? -28.257 -39.880  -1.750  1.000 51.262  0 342 PHE KKK CZ  1 ? 40 
ATOM   12832 N N   . ASN K  1 14  ? -32.092 -34.225  -4.695  1.000 54.706  0 343 ASN KKK N   1 ? 40 
ATOM   12833 C CA  . ASN K  1 14  ? -32.436 -32.809  -4.960  1.000 59.325  0 343 ASN KKK CA  1 ? 40 
ATOM   12834 C C   . ASN K  1 14  ? -33.851 -32.690  -5.538  1.000 57.945  0 343 ASN KKK C   1 ? 40 
ATOM   12835 O O   . ASN K  1 14  ? -34.169 -31.612  -6.005  1.000 59.914  0 343 ASN KKK O   1 ? 40 
ATOM   12836 C CB  . ASN K  1 14  ? -31.415 -32.148  -5.872  1.000 65.241  0 343 ASN KKK CB  1 ? 40 
ATOM   12837 C CG  . ASN K  1 14  ? -30.073 -31.929  -5.222  1.000 72.149  0 343 ASN KKK CG  1 ? 40 
ATOM   12838 O OD1 . ASN K  1 14  ? -29.925 -31.833  -3.997  1.000 71.279  0 343 ASN KKK OD1 1 ? 40 
ATOM   12839 N ND2 . ASN K  1 14  ? -29.089 -31.795  -6.094  1.000 86.803  0 343 ASN KKK ND2 1 ? 40 
ATOM   12840 N N   . ALA K  1 15  ? -34.695 -33.714  -5.413  1.000 55.908  0 344 ALA KKK N   1 ? 40 
ATOM   12841 C CA  . ALA K  1 15  ? -36.157 -33.604  -5.634  1.000 57.907  0 344 ALA KKK CA  1 ? 40 
ATOM   12842 C C   . ALA K  1 15  ? -36.665 -32.406  -4.826  1.000 59.385  0 344 ALA KKK C   1 ? 40 
ATOM   12843 O O   . ALA K  1 15  ? -36.222 -32.230  -3.704  1.000 58.197  0 344 ALA KKK O   1 ? 40 
ATOM   12844 C CB  . ALA K  1 15  ? -36.866 -34.872  -5.235  1.000 56.358  0 344 ALA KKK CB  1 ? 40 
ATOM   12845 N N   . THR K  1 16  ? -37.520 -31.561  -5.388  1.000 63.900  0 345 THR KKK N   1 ? 40 
ATOM   12846 C CA  . THR K  1 16  ? -37.969 -30.329  -4.686  1.000 67.402  0 345 THR KKK CA  1 ? 40 
ATOM   12847 C C   . THR K  1 16  ? -38.945 -30.740  -3.574  1.000 65.994  0 345 THR KKK C   1 ? 40 
ATOM   12848 O O   . THR K  1 16  ? -39.026 -30.051  -2.552  1.000 65.789  0 345 THR KKK O   1 ? 40 
ATOM   12849 C CB  . THR K  1 16  ? -38.499 -29.310  -5.694  1.000 74.254  0 345 THR KKK CB  1 ? 40 
ATOM   12850 O OG1 . THR K  1 16  ? -39.384 -30.040  -6.526  1.000 77.697  0 345 THR KKK OG1 1 ? 40 
ATOM   12851 C CG2 . THR K  1 16  ? -37.420 -28.714  -6.570  1.000 76.627  0 345 THR KKK CG2 1 ? 40 
ATOM   12852 N N   . ARG K  1 17  ? -39.623 -31.871  -3.758  1.000 64.717  0 346 ARG KKK N   1 ? 40 
ATOM   12853 C CA  . ARG K  1 17  ? -40.625 -32.421  -2.818  1.000 64.954  0 346 ARG KKK CA  1 ? 40 
ATOM   12854 C C   . ARG K  1 17  ? -40.168 -33.794  -2.345  1.000 60.928  0 346 ARG KKK C   1 ? 40 
ATOM   12855 O O   . ARG K  1 17  ? -39.600 -34.573  -3.109  1.000 58.462  0 346 ARG KKK O   1 ? 40 
ATOM   12856 C CB  . ARG K  1 17  ? -41.969 -32.574  -3.501  1.000 70.545  0 346 ARG KKK CB  1 ? 40 
ATOM   12857 C CG  . ARG K  1 17  ? -43.089 -31.843  -2.781  1.000 76.671  0 346 ARG KKK CG  1 ? 40 
ATOM   12858 C CD  . ARG K  1 17  ? -44.433 -32.118  -3.413  1.000 84.722  0 346 ARG KKK CD  1 ? 40 
ATOM   12859 N NE  . ARG K  1 17  ? -45.056 -30.985  -4.091  1.000 93.272  0 346 ARG KKK NE  1 ? 40 
ATOM   12860 C CZ  . ARG K  1 17  ? -44.977 -30.728  -5.406  1.000 99.617  0 346 ARG KKK CZ  1 ? 40 
ATOM   12861 N NH1 . ARG K  1 17  ? -44.259 -31.516  -6.204  1.000 96.775  0 346 ARG KKK NH1 1 ? 40 
ATOM   12862 N NH2 . ARG K  1 17  ? -45.606 -29.672  -5.912  1.000 106.544 0 346 ARG KKK NH2 1 ? 40 
ATOM   12863 N N   . PHE K  1 18  ? -40.392 -34.044  -1.066  1.000 44.663  0 347 PHE KKK N   1 ? 41 
ATOM   12864 C CA  . PHE K  1 18  ? -40.091 -35.314  -0.373  1.000 44.217  0 347 PHE KKK CA  1 ? 41 
ATOM   12865 C C   . PHE K  1 18  ? -41.386 -35.821  0.245   1.000 42.929  0 347 PHE KKK C   1 ? 41 
ATOM   12866 O O   . PHE K  1 18  ? -42.225 -35.019  0.686   1.000 44.844  0 347 PHE KKK O   1 ? 41 
ATOM   12867 C CB  . PHE K  1 18  ? -38.994 -35.095  0.678   1.000 45.358  0 347 PHE KKK CB  1 ? 41 
ATOM   12868 C CG  . PHE K  1 18  ? -37.601 -35.395  0.191   1.000 45.586  0 347 PHE KKK CG  1 ? 41 
ATOM   12869 C CD1 . PHE K  1 18  ? -37.056 -34.706  -0.870  1.000 48.271  0 347 PHE KKK CD1 1 ? 41 
ATOM   12870 C CD2 . PHE K  1 18  ? -36.812 -36.314  0.824   1.000 44.290  0 347 PHE KKK CD2 1 ? 41 
ATOM   12871 C CE1 . PHE K  1 18  ? -35.770 -34.961  -1.317  1.000 51.121  0 347 PHE KKK CE1 1 ? 41 
ATOM   12872 C CE2 . PHE K  1 18  ? -35.514 -36.569  0.402   1.000 45.899  0 347 PHE KKK CE2 1 ? 41 
ATOM   12873 C CZ  . PHE K  1 18  ? -35.008 -35.912  -0.697  1.000 48.863  0 347 PHE KKK CZ  1 ? 41 
ATOM   12874 N N   . ALA K  1 19  ? -41.516 -37.139  0.318   1.000 42.101  0 348 ALA KKK N   1 ? 41 
ATOM   12875 C CA  . ALA K  1 19  ? -42.674 -37.836  0.903   1.000 41.840  0 348 ALA KKK CA  1 ? 41 
ATOM   12876 C C   . ALA K  1 19  ? -42.669 -37.714  2.428   1.000 41.899  0 348 ALA KKK C   1 ? 41 
ATOM   12877 O O   . ALA K  1 19  ? -41.605 -37.554  3.039   1.000 45.401  0 348 ALA KKK O   1 ? 41 
ATOM   12878 C CB  . ALA K  1 19  ? -42.621 -39.274  0.482   1.000 42.011  0 348 ALA KKK CB  1 ? 41 
ATOM   12879 N N   . SER K  1 20  ? -43.850 -37.764  3.034   1.000 42.510  0 349 SER KKK N   1 ? 41 
ATOM   12880 C CA  . SER K  1 20  ? -44.036 -38.145  4.453   1.000 42.697  0 349 SER KKK CA  1 ? 41 
ATOM   12881 C C   . SER K  1 20  ? -43.494 -39.562  4.623   1.000 43.157  0 349 SER KKK C   1 ? 41 
ATOM   12882 O O   . SER K  1 20  ? -43.652 -40.414  3.685   1.000 45.652  0 349 SER KKK O   1 ? 41 
ATOM   12883 C CB  . SER K  1 20  ? -45.471 -38.058  4.854   1.000 43.073  0 349 SER KKK CB  1 ? 41 
ATOM   12884 O OG  . SER K  1 20  ? -45.895 -36.712  4.983   1.000 42.958  0 349 SER KKK OG  1 ? 41 
ATOM   12885 N N   . VAL K  1 21  ? -42.875 -39.828  5.767   1.000 41.523  0 350 VAL KKK N   1 ? 41 
ATOM   12886 C CA  . VAL K  1 21  ? -42.240 -41.143  6.055   1.000 41.062  0 350 VAL KKK CA  1 ? 41 
ATOM   12887 C C   . VAL K  1 21  ? -43.253 -42.294  5.888   1.000 42.753  0 350 VAL KKK C   1 ? 41 
ATOM   12888 O O   . VAL K  1 21  ? -42.858 -43.332  5.362   1.000 45.504  0 350 VAL KKK O   1 ? 41 
ATOM   12889 C CB  . VAL K  1 21  ? -41.578 -41.113  7.443   1.000 41.771  0 350 VAL KKK CB  1 ? 41 
ATOM   12890 C CG1 . VAL K  1 21  ? -42.595 -40.955  8.564   1.000 42.407  0 350 VAL KKK CG1 1 ? 41 
ATOM   12891 C CG2 . VAL K  1 21  ? -40.693 -42.328  7.665   1.000 43.394  0 350 VAL KKK CG2 1 ? 41 
ATOM   12892 N N   . TYR K  1 22  ? -44.512 -42.140  6.309   1.000 40.971  0 351 TYR KKK N   1 ? 41 
ATOM   12893 C CA  . TYR K  1 22  ? -45.506 -43.244  6.270   1.000 42.192  0 351 TYR KKK CA  1 ? 41 
ATOM   12894 C C   . TYR K  1 22  ? -45.792 -43.615  4.805   1.000 43.096  0 351 TYR KKK C   1 ? 41 
ATOM   12895 O O   . TYR K  1 22  ? -46.114 -44.777  4.524   1.000 41.959  0 351 TYR KKK O   1 ? 41 
ATOM   12896 C CB  . TYR K  1 22  ? -46.779 -42.877  7.045   1.000 42.206  0 351 TYR KKK CB  1 ? 41 
ATOM   12897 C CG  . TYR K  1 22  ? -47.767 -42.093  6.232   1.000 42.247  0 351 TYR KKK CG  1 ? 41 
ATOM   12898 C CD1 . TYR K  1 22  ? -47.631 -40.722  6.065   1.000 43.760  0 351 TYR KKK CD1 1 ? 41 
ATOM   12899 C CD2 . TYR K  1 22  ? -48.791 -42.720  5.558   1.000 44.257  0 351 TYR KKK CD2 1 ? 41 
ATOM   12900 C CE1 . TYR K  1 22  ? -48.509 -39.997  5.274   1.000 42.753  0 351 TYR KKK CE1 1 ? 41 
ATOM   12901 C CE2 . TYR K  1 22  ? -49.667 -42.011  4.752   1.000 43.990  0 351 TYR KKK CE2 1 ? 41 
ATOM   12902 C CZ  . TYR K  1 22  ? -49.526 -40.648  4.620   1.000 43.533  0 351 TYR KKK CZ  1 ? 41 
ATOM   12903 O OH  . TYR K  1 22  ? -50.394 -39.921  3.881   1.000 45.177  0 351 TYR KKK OH  1 ? 41 
ATOM   12904 N N   . ALA K  1 23  ? -45.688 -42.640  3.893   1.000 44.089  0 352 ALA KKK N   1 ? 41 
ATOM   12905 C CA  . ALA K  1 23  ? -45.943 -42.790  2.439   1.000 44.306  0 352 ALA KKK CA  1 ? 41 
ATOM   12906 C C   . ALA K  1 23  ? -44.617 -42.651  1.681   1.000 44.818  0 352 ALA KKK C   1 ? 41 
ATOM   12907 O O   . ALA K  1 23  ? -44.562 -41.935  0.656   1.000 45.134  0 352 ALA KKK O   1 ? 41 
ATOM   12908 C CB  . ALA K  1 23  ? -46.943 -41.754  1.991   1.000 46.254  0 352 ALA KKK CB  1 ? 41 
ATOM   12909 N N   . TRP K  1 24  ? -43.574 -43.299  2.184   1.000 42.483  0 353 TRP KKK N   1 ? 41 
ATOM   12910 C CA  . TRP K  1 24  ? -42.199 -43.130  1.674   1.000 40.904  0 353 TRP KKK CA  1 ? 41 
ATOM   12911 C C   . TRP K  1 24  ? -42.141 -43.470  0.181   1.000 43.672  0 353 TRP KKK C   1 ? 41 
ATOM   12912 O O   . TRP K  1 24  ? -42.844 -44.375  -0.276  1.000 44.618  0 353 TRP KKK O   1 ? 41 
ATOM   12913 C CB  . TRP K  1 24  ? -41.207 -43.948  2.490   1.000 40.619  0 353 TRP KKK CB  1 ? 41 
ATOM   12914 C CG  . TRP K  1 24  ? -41.565 -45.375  2.710   1.000 40.932  0 353 TRP KKK CG  1 ? 41 
ATOM   12915 C CD1 . TRP K  1 24  ? -42.280 -45.914  3.748   1.000 41.077  0 353 TRP KKK CD1 1 ? 41 
ATOM   12916 C CD2 . TRP K  1 24  ? -41.144 -46.476  1.890   1.000 41.604  0 353 TRP KKK CD2 1 ? 41 
ATOM   12917 N NE1 . TRP K  1 24  ? -42.362 -47.271  3.604   1.000 41.532  0 353 TRP KKK NE1 1 ? 41 
ATOM   12918 C CE2 . TRP K  1 24  ? -41.677 -47.640  2.476   1.000 41.363  0 353 TRP KKK CE2 1 ? 41 
ATOM   12919 C CE3 . TRP K  1 24  ? -40.385 -46.583  0.719   1.000 41.140  0 353 TRP KKK CE3 1 ? 41 
ATOM   12920 C CZ2 . TRP K  1 24  ? -41.461 -48.893  1.929   1.000 43.687  0 353 TRP KKK CZ2 1 ? 41 
ATOM   12921 C CZ3 . TRP K  1 24  ? -40.167 -47.827  0.178   1.000 42.315  0 353 TRP KKK CZ3 1 ? 41 
ATOM   12922 C CH2 . TRP K  1 24  ? -40.666 -48.969  0.802   1.000 44.198  0 353 TRP KKK CH2 1 ? 41 
ATOM   12923 N N   . ASN K  1 25  ? -41.318 -42.737  -0.537  1.000 45.380  0 354 ASN KKK N   1 ? 41 
ATOM   12924 C CA  . ASN K  1 25  ? -41.198 -42.827  -2.006  1.000 48.391  0 354 ASN KKK CA  1 ? 41 
ATOM   12925 C C   . ASN K  1 25  ? -40.055 -43.780  -2.376  1.000 47.038  0 354 ASN KKK C   1 ? 41 
ATOM   12926 O O   . ASN K  1 25  ? -39.006 -43.698  -1.682  1.000 46.040  0 354 ASN KKK O   1 ? 41 
ATOM   12927 C CB  . ASN K  1 25  ? -41.019 -41.415  -2.560  1.000 52.705  0 354 ASN KKK CB  1 ? 41 
ATOM   12928 C CG  . ASN K  1 25  ? -40.995 -41.438  -4.060  1.000 57.835  0 354 ASN KKK CG  1 ? 41 
ATOM   12929 O OD1 . ASN K  1 25  ? -39.908 -41.516  -4.640  1.000 65.052  0 354 ASN KKK OD1 1 ? 41 
ATOM   12930 N ND2 . ASN K  1 25  ? -42.175 -41.428  -4.669  1.000 61.025  0 354 ASN KKK ND2 1 ? 41 
ATOM   12931 N N   . ARG K  1 26  ? -40.251 -44.640  -3.382  1.000 46.398  0 355 ARG KKK N   1 ? 41 
ATOM   12932 C CA  . ARG K  1 26  ? -39.214 -45.505  -4.029  1.000 49.078  0 355 ARG KKK CA  1 ? 41 
ATOM   12933 C C   . ARG K  1 26  ? -38.896 -45.050  -5.455  1.000 51.092  0 355 ARG KKK C   1 ? 41 
ATOM   12934 O O   . ARG K  1 26  ? -39.815 -45.093  -6.277  1.000 52.105  0 355 ARG KKK O   1 ? 41 
ATOM   12935 C CB  . ARG K  1 26  ? -39.722 -46.881  -4.450  1.000 49.811  0 355 ARG KKK CB  1 ? 41 
ATOM   12936 C CG  . ARG K  1 26  ? -39.352 -48.019  -3.545  1.000 50.465  0 355 ARG KKK CG  1 ? 41 
ATOM   12937 C CD  . ARG K  1 26  ? -38.366 -49.030  -4.127  1.000 50.689  0 355 ARG KKK CD  1 ? 41 
ATOM   12938 N NE  . ARG K  1 26  ? -37.741 -49.367  -2.861  1.000 50.121  0 355 ARG KKK NE  1 ? 41 
ATOM   12939 C CZ  . ARG K  1 26  ? -37.755 -50.522  -2.223  1.000 48.704  0 355 ARG KKK CZ  1 ? 41 
ATOM   12940 N NH1 . ARG K  1 26  ? -38.243 -51.604  -2.788  1.000 53.535  0 355 ARG KKK NH1 1 ? 41 
ATOM   12941 N NH2 . ARG K  1 26  ? -37.149 -50.598  -1.067  1.000 46.619  0 355 ARG KKK NH2 1 ? 41 
ATOM   12942 N N   . LYS K  1 27  ? -37.627 -44.878  -5.788  1.000 52.463  0 356 LYS KKK N   1 ? 41 
ATOM   12943 C CA  . LYS K  1 27  ? -37.181 -44.803  -7.191  1.000 54.430  0 356 LYS KKK CA  1 ? 41 
ATOM   12944 C C   . LYS K  1 27  ? -36.260 -45.994  -7.453  1.000 52.307  0 356 LYS KKK C   1 ? 41 
ATOM   12945 O O   . LYS K  1 27  ? -35.405 -46.308  -6.617  1.000 49.430  0 356 LYS KKK O   1 ? 41 
ATOM   12946 C CB  . LYS K  1 27  ? -36.545 -43.430  -7.435  1.000 56.897  0 356 LYS KKK CB  1 ? 41 
ATOM   12947 C CG  . LYS K  1 27  ? -36.006 -43.219  -8.830  1.000 63.212  0 356 LYS KKK CG  1 ? 41 
ATOM   12948 C CD  . LYS K  1 27  ? -36.012 -41.754  -9.310  1.000 68.924  0 356 LYS KKK CD  1 ? 41 
ATOM   12949 C CE  . LYS K  1 27  ? -35.994 -41.636  -10.829 1.000 73.357  0 356 LYS KKK CE  1 ? 41 
ATOM   12950 N NZ  . LYS K  1 27  ? -34.676 -42.049  -11.371 1.000 77.046  0 356 LYS KKK NZ  1 ? 41 
ATOM   12951 N N   . ARG K  1 28  ? -36.462 -46.678  -8.566  1.000 55.533  0 357 ARG KKK N   1 ? 41 
ATOM   12952 C CA  . ARG K  1 28  ? -35.516 -47.711  -9.063  1.000 56.973  0 357 ARG KKK CA  1 ? 41 
ATOM   12953 C C   . ARG K  1 28  ? -34.387 -46.986  -9.794  1.000 55.452  0 357 ARG KKK C   1 ? 41 
ATOM   12954 O O   . ARG K  1 28  ? -34.665 -46.112  -10.588 1.000 55.547  0 357 ARG KKK O   1 ? 41 
ATOM   12955 C CB  . ARG K  1 28  ? -36.218 -48.721  -9.966  1.000 60.307  0 357 ARG KKK CB  1 ? 41 
ATOM   12956 C CG  . ARG K  1 28  ? -35.306 -49.860  -10.411 1.000 64.966  0 357 ARG KKK CG  1 ? 41 
ATOM   12957 C CD  . ARG K  1 28  ? -35.707 -50.530  -11.715 1.000 69.326  0 357 ARG KKK CD  1 ? 41 
ATOM   12958 N NE  . ARG K  1 28  ? -36.989 -51.200  -11.544 1.000 71.745  0 357 ARG KKK NE  1 ? 41 
ATOM   12959 C CZ  . ARG K  1 28  ? -37.167 -52.308  -10.825 1.000 74.051  0 357 ARG KKK CZ  1 ? 41 
ATOM   12960 N NH1 . ARG K  1 28  ? -36.139 -52.883  -10.209 1.000 73.433  0 357 ARG KKK NH1 1 ? 41 
ATOM   12961 N NH2 . ARG K  1 28  ? -38.379 -52.800  -10.684 1.000 76.025  0 357 ARG KKK NH2 1 ? 41 
ATOM   12962 N N   . ILE K  1 29  ? -33.149 -47.370  -9.523  1.000 55.071  0 358 ILE KKK N   1 ? 41 
ATOM   12963 C CA  . ILE K  1 29  ? -31.947 -46.961  -10.298 1.000 55.509  0 358 ILE KKK CA  1 ? 41 
ATOM   12964 C C   . ILE K  1 29  ? -31.366 -48.210  -10.959 1.000 55.941  0 358 ILE KKK C   1 ? 41 
ATOM   12965 O O   . ILE K  1 29  ? -31.103 -49.203  -10.241 1.000 56.424  0 358 ILE KKK O   1 ? 41 
ATOM   12966 C CB  . ILE K  1 29  ? -30.981 -46.262  -9.327  1.000 54.002  0 358 ILE KKK CB  1 ? 41 
ATOM   12967 C CG1 . ILE K  1 29  ? -31.575 -44.915  -8.914  1.000 53.576  0 358 ILE KKK CG1 1 ? 41 
ATOM   12968 C CG2 . ILE K  1 29  ? -29.570 -46.117  -9.898  1.000 55.042  0 358 ILE KKK CG2 1 ? 41 
ATOM   12969 C CD1 . ILE K  1 29  ? -30.935 -44.326  -7.703  1.000 54.105  0 358 ILE KKK CD1 1 ? 41 
ATOM   12970 N N   . SER K  1 30  ? -31.181 -48.169  -12.277 1.000 57.978  0 359 SER KKK N   1 ? 41 
ATOM   12971 C CA  . SER K  1 30  ? -30.637 -49.305  -13.072 1.000 59.868  0 359 SER KKK CA  1 ? 41 
ATOM   12972 C C   . SER K  1 30  ? -30.042 -48.841  -14.400 1.000 61.600  0 359 SER KKK C   1 ? 41 
ATOM   12973 O O   . SER K  1 30  ? -30.334 -47.710  -14.796 1.000 63.146  0 359 SER KKK O   1 ? 41 
ATOM   12974 C CB  . SER K  1 30  ? -31.677 -50.340  -13.295 1.000 60.173  0 359 SER KKK CB  1 ? 41 
ATOM   12975 O OG  . SER K  1 30  ? -32.853 -49.715  -13.752 1.000 61.298  0 359 SER KKK OG  1 ? 41 
ATOM   12976 N N   . ASN K  1 31  ? -29.235 -49.689  -15.038 1.000 63.539  0 360 ASN KKK N   1 ? 41 
ATOM   12977 C CA  . ASN K  1 31  ? -28.679 -49.450  -16.393 1.000 66.534  0 360 ASN KKK CA  1 ? 41 
ATOM   12978 C C   . ASN K  1 31  ? -28.023 -48.072  -16.397 1.000 65.840  0 360 ASN KKK C   1 ? 41 
ATOM   12979 O O   . ASN K  1 31  ? -28.411 -47.212  -17.210 1.000 68.064  0 360 ASN KKK O   1 ? 41 
ATOM   12980 C CB  . ASN K  1 31  ? -29.765 -49.571  -17.466 1.000 70.087  0 360 ASN KKK CB  1 ? 41 
ATOM   12981 C CG  . ASN K  1 31  ? -30.336 -50.965  -17.501 1.000 71.776  0 360 ASN KKK CG  1 ? 41 
ATOM   12982 O OD1 . ASN K  1 31  ? -31.534 -51.195  -17.312 1.000 71.805  0 360 ASN KKK OD1 1 ? 41 
ATOM   12983 N ND2 . ASN K  1 31  ? -29.471 -51.895  -17.859 1.000 73.208  0 360 ASN KKK ND2 1 ? 41 
ATOM   12984 N N   . CYS K  1 32  ? -27.090 -47.874  -15.470 1.000 63.764  0 361 CYS KKK N   1 ? 41 
ATOM   12985 C CA  . CYS K  1 32  ? -26.341 -46.608  -15.294 1.000 64.907  0 361 CYS KKK CA  1 ? 41 
ATOM   12986 C C   . CYS K  1 32  ? -25.045 -46.849  -14.505 1.000 63.067  0 361 CYS KKK C   1 ? 41 
ATOM   12987 O O   . CYS K  1 32  ? -24.952 -47.879  -13.817 1.000 61.797  0 361 CYS KKK O   1 ? 41 
ATOM   12988 C CB  . CYS K  1 32  ? -27.249 -45.587  -14.622 1.000 64.488  0 361 CYS KKK CB  1 ? 41 
ATOM   12989 S SG  . CYS K  1 32  ? -27.901 -46.129  -13.001 1.000 63.012  0 361 CYS KKK SG  1 ? 41 
ATOM   12990 N N   . VAL K  1 33  ? -24.087 -45.928  -14.613 1.000 64.168  0 362 VAL KKK N   1 ? 41 
ATOM   12991 C CA  . VAL K  1 33  ? -22.822 -45.912  -13.821 1.000 65.504  0 362 VAL KKK CA  1 ? 41 
ATOM   12992 C C   . VAL K  1 33  ? -23.106 -45.156  -12.522 1.000 65.318  0 362 VAL KKK C   1 ? 41 
ATOM   12993 O O   . VAL K  1 33  ? -23.506 -43.973  -12.595 1.000 64.357  0 362 VAL KKK O   1 ? 41 
ATOM   12994 C CB  . VAL K  1 33  ? -21.675 -45.234  -14.595 1.000 68.855  0 362 VAL KKK CB  1 ? 41 
ATOM   12995 C CG1 . VAL K  1 33  ? -20.386 -45.209  -13.782 1.000 68.599  0 362 VAL KKK CG1 1 ? 41 
ATOM   12996 C CG2 . VAL K  1 33  ? -21.453 -45.849  -15.971 1.000 70.525  0 362 VAL KKK CG2 1 ? 41 
ATOM   12997 N N   . ALA K  1 34  ? -22.951 -45.823  -11.371 1.000 67.306  0 363 ALA KKK N   1 ? 41 
ATOM   12998 C CA  . ALA K  1 34  ? -23.142 -45.227  -10.026 1.000 66.903  0 363 ALA KKK CA  1 ? 41 
ATOM   12999 C C   . ALA K  1 34  ? -21.805 -44.614  -9.624  1.000 70.250  0 363 ALA KKK C   1 ? 41 
ATOM   13000 O O   . ALA K  1 34  ? -20.923 -45.332  -9.085  1.000 71.866  0 363 ALA KKK O   1 ? 41 
ATOM   13001 C CB  . ALA K  1 34  ? -23.591 -46.244  -9.007  1.000 65.129  0 363 ALA KKK CB  1 ? 41 
ATOM   13002 N N   . ASP K  1 35  ? -21.646 -43.321  -9.908  1.000 71.152  0 364 ASP KKK N   1 ? 41 
ATOM   13003 C CA  . ASP K  1 35  ? -20.520 -42.530  -9.380  1.000 71.718  0 364 ASP KKK CA  1 ? 41 
ATOM   13004 C C   . ASP K  1 35  ? -20.971 -41.895  -8.066  1.000 67.451  0 364 ASP KKK C   1 ? 41 
ATOM   13005 O O   . ASP K  1 35  ? -21.820 -40.979  -8.106  1.000 65.706  0 364 ASP KKK O   1 ? 41 
ATOM   13006 C CB  . ASP K  1 35  ? -20.048 -41.470  -10.364 1.000 75.818  0 364 ASP KKK CB  1 ? 41 
ATOM   13007 C CG  . ASP K  1 35  ? -18.649 -41.041  -9.991  1.000 79.132  0 364 ASP KKK CG  1 ? 41 
ATOM   13008 O OD1 . ASP K  1 35  ? -18.233 -41.371  -8.844  1.000 82.431  0 364 ASP KKK OD1 1 ? 41 
ATOM   13009 O OD2 . ASP K  1 35  ? -17.980 -40.423  -10.837 1.000 81.135  0 364 ASP KKK OD2 1 ? 41 
ATOM   13010 N N   . TYR K  1 36  ? -20.395 -42.350  -6.963  1.000 65.373  0 365 TYR KKK N   1 ? 41 
ATOM   13011 C CA  . TYR K  1 36  ? -20.763 -41.905  -5.604  1.000 64.513  0 365 TYR KKK CA  1 ? 41 
ATOM   13012 C C   . TYR K  1 36  ? -19.946 -40.669  -5.222  1.000 66.106  0 365 TYR KKK C   1 ? 41 
ATOM   13013 O O   . TYR K  1 36  ? -20.208 -40.141  -4.141  1.000 65.035  0 365 TYR KKK O   1 ? 41 
ATOM   13014 C CB  . TYR K  1 36  ? -20.579 -43.040  -4.589  1.000 63.528  0 365 TYR KKK CB  1 ? 41 
ATOM   13015 C CG  . TYR K  1 36  ? -21.625 -44.103  -4.716  1.000 61.538  0 365 TYR KKK CG  1 ? 41 
ATOM   13016 C CD1 . TYR K  1 36  ? -21.480 -45.153  -5.611  1.000 62.879  0 365 TYR KKK CD1 1 ? 41 
ATOM   13017 C CD2 . TYR K  1 36  ? -22.792 -44.026  -3.982  1.000 60.692  0 365 TYR KKK CD2 1 ? 41 
ATOM   13018 C CE1 . TYR K  1 36  ? -22.469 -46.104  -5.768  1.000 61.691  0 365 TYR KKK CE1 1 ? 41 
ATOM   13019 C CE2 . TYR K  1 36  ? -23.797 -44.972  -4.126  1.000 59.630  0 365 TYR KKK CE2 1 ? 41 
ATOM   13020 C CZ  . TYR K  1 36  ? -23.632 -46.002  -5.029  1.000 60.576  0 365 TYR KKK CZ  1 ? 41 
ATOM   13021 O OH  . TYR K  1 36  ? -24.603 -46.934  -5.171  1.000 62.648  0 365 TYR KKK OH  1 ? 41 
ATOM   13022 N N   . SER K  1 37  ? -18.991 -40.224  -6.050  1.000 67.893  0 366 SER KKK N   1 ? 41 
ATOM   13023 C CA  . SER K  1 37  ? -18.130 -39.074  -5.690  1.000 71.575  0 366 SER KKK CA  1 ? 41 
ATOM   13024 C C   . SER K  1 37  ? -18.985 -37.816  -5.538  1.000 72.725  0 366 SER KKK C   1 ? 41 
ATOM   13025 O O   . SER K  1 37  ? -18.576 -36.966  -4.766  1.000 75.988  0 366 SER KKK O   1 ? 41 
ATOM   13026 C CB  . SER K  1 37  ? -16.954 -38.879  -6.610  1.000 73.645  0 366 SER KKK CB  1 ? 41 
ATOM   13027 O OG  . SER K  1 37  ? -17.351 -39.025  -7.944  1.000 73.347  0 366 SER KKK OG  1 ? 41 
ATOM   13028 N N   . VAL K  1 38  ? -20.156 -37.722  -6.172  1.000 70.414  0 367 VAL KKK N   1 ? 41 
ATOM   13029 C CA  . VAL K  1 38  ? -21.069 -36.571  -5.931  1.000 70.102  0 367 VAL KKK CA  1 ? 41 
ATOM   13030 C C   . VAL K  1 38  ? -21.474 -36.559  -4.438  1.000 68.697  0 367 VAL KKK C   1 ? 41 
ATOM   13031 O O   . VAL K  1 38  ? -21.415 -35.474  -3.809  1.000 68.374  0 367 VAL KKK O   1 ? 41 
ATOM   13032 C CB  . VAL K  1 38  ? -22.265 -36.597  -6.903  1.000 70.944  0 367 VAL KKK CB  1 ? 41 
ATOM   13033 C CG1 . VAL K  1 38  ? -23.246 -37.737  -6.614  1.000 67.859  0 367 VAL KKK CG1 1 ? 41 
ATOM   13034 C CG2 . VAL K  1 38  ? -22.981 -35.249  -6.940  1.000 71.453  0 367 VAL KKK CG2 1 ? 41 
ATOM   13035 N N   . LEU K  1 39  ? -21.791 -37.721  -3.855  1.000 64.976  0 368 LEU KKK N   1 ? 41 
ATOM   13036 C CA  . LEU K  1 39  ? -22.168 -37.841  -2.421  1.000 63.204  0 368 LEU KKK CA  1 ? 41 
ATOM   13037 C C   . LEU K  1 39  ? -20.940 -37.665  -1.511  1.000 67.181  0 368 LEU KKK C   1 ? 41 
ATOM   13038 O O   . LEU K  1 39  ? -21.090 -37.072  -0.420  1.000 69.532  0 368 LEU KKK O   1 ? 41 
ATOM   13039 C CB  . LEU K  1 39  ? -22.832 -39.194  -2.190  1.000 59.229  0 368 LEU KKK CB  1 ? 41 
ATOM   13040 C CG  . LEU K  1 39  ? -24.063 -39.472  -3.046  1.000 57.984  0 368 LEU KKK CG  1 ? 41 
ATOM   13041 C CD1 . LEU K  1 39  ? -24.627 -40.851  -2.786  1.000 56.572  0 368 LEU KKK CD1 1 ? 41 
ATOM   13042 C CD2 . LEU K  1 39  ? -25.120 -38.394  -2.839  1.000 57.866  0 368 LEU KKK CD2 1 ? 41 
ATOM   13043 N N   . TYR K  1 40  ? -19.768 -38.155  -1.930  1.000 65.915  0 369 TYR KKK N   1 ? 42 
ATOM   13044 C CA  . TYR K  1 40  ? -18.506 -38.089  -1.144  1.000 67.325  0 369 TYR KKK CA  1 ? 42 
ATOM   13045 C C   . TYR K  1 40  ? -18.100 -36.622  -0.913  1.000 68.022  0 369 TYR KKK C   1 ? 42 
ATOM   13046 O O   . TYR K  1 40  ? -17.456 -36.353  0.104   1.000 68.967  0 369 TYR KKK O   1 ? 42 
ATOM   13047 C CB  . TYR K  1 40  ? -17.350 -38.800  -1.859  1.000 68.406  0 369 TYR KKK CB  1 ? 42 
ATOM   13048 C CG  . TYR K  1 40  ? -17.411 -40.303  -1.963  1.000 67.237  0 369 TYR KKK CG  1 ? 42 
ATOM   13049 C CD1 . TYR K  1 40  ? -18.051 -41.084  -1.009  1.000 67.711  0 369 TYR KKK CD1 1 ? 42 
ATOM   13050 C CD2 . TYR K  1 40  ? -16.772 -40.949  -3.008  1.000 66.669  0 369 TYR KKK CD2 1 ? 42 
ATOM   13051 C CE1 . TYR K  1 40  ? -18.048 -42.479  -1.094  1.000 68.819  0 369 TYR KKK CE1 1 ? 42 
ATOM   13052 C CE2 . TYR K  1 40  ? -16.806 -42.329  -3.137  1.000 67.403  0 369 TYR KKK CE2 1 ? 42 
ATOM   13053 C CZ  . TYR K  1 40  ? -17.417 -43.104  -2.163  1.000 68.037  0 369 TYR KKK CZ  1 ? 42 
ATOM   13054 O OH  . TYR K  1 40  ? -17.431 -44.461  -2.305  1.000 69.308  0 369 TYR KKK OH  1 ? 42 
ATOM   13055 N N   . ASN K  1 41  ? -18.457 -35.719  -1.833  1.000 68.704  0 370 ASN KKK N   1 ? 42 
ATOM   13056 C CA  . ASN K  1 41  ? -18.010 -34.303  -1.848  1.000 73.473  0 370 ASN KKK CA  1 ? 42 
ATOM   13057 C C   . ASN K  1 41  ? -19.036 -33.395  -1.180  1.000 74.885  0 370 ASN KKK C   1 ? 42 
ATOM   13058 O O   . ASN K  1 41  ? -18.844 -32.170  -1.252  1.000 79.535  0 370 ASN KKK O   1 ? 42 
ATOM   13059 C CB  . ASN K  1 41  ? -17.752 -33.818  -3.272  1.000 74.116  0 370 ASN KKK CB  1 ? 42 
ATOM   13060 C CG  . ASN K  1 41  ? -16.583 -34.534  -3.900  1.000 74.422  0 370 ASN KKK CG  1 ? 42 
ATOM   13061 O OD1 . ASN K  1 41  ? -15.581 -34.795  -3.229  1.000 74.987  0 370 ASN KKK OD1 1 ? 42 
ATOM   13062 N ND2 . ASN K  1 41  ? -16.717 -34.842  -5.180  1.000 74.324  0 370 ASN KKK ND2 1 ? 42 
ATOM   13063 N N   . SER K  1 42  ? -20.060 -33.956  -0.538  1.000 75.830  0 371 SER KKK N   1 ? 42 
ATOM   13064 C CA  . SER K  1 42  ? -21.017 -33.209  0.322   1.000 77.105  0 371 SER KKK CA  1 ? 42 
ATOM   13065 C C   . SER K  1 42  ? -20.496 -33.217  1.760   1.000 77.363  0 371 SER KKK C   1 ? 42 
ATOM   13066 O O   . SER K  1 42  ? -20.139 -34.304  2.259   1.000 76.926  0 371 SER KKK O   1 ? 42 
ATOM   13067 C CB  . SER K  1 42  ? -22.397 -33.778  0.240   1.000 77.134  0 371 SER KKK CB  1 ? 42 
ATOM   13068 O OG  . SER K  1 42  ? -23.297 -33.057  1.079   1.000 77.831  0 371 SER KKK OG  1 ? 42 
ATOM   13069 N N   . ALA K  1 43  ? -20.420 -32.031  2.375   1.000 77.992  0 372 ALA KKK N   1 ? 42 
ATOM   13070 C CA  . ALA K  1 43  ? -20.105 -31.820  3.801   1.000 75.506  0 372 ALA KKK CA  1 ? 42 
ATOM   13071 C C   . ALA K  1 43  ? -21.401 -31.443  4.532   1.000 72.916  0 372 ALA KKK C   1 ? 42 
ATOM   13072 O O   . ALA K  1 43  ? -21.354 -31.238  5.753   1.000 77.795  0 372 ALA KKK O   1 ? 42 
ATOM   13073 C CB  . ALA K  1 43  ? -19.068 -30.745  3.929   1.000 77.557  0 372 ALA KKK CB  1 ? 42 
ATOM   13074 N N   . SER K  1 44  ? -22.533 -31.446  3.834   1.000 68.322  0 373 SER KKK N   1 ? 42 
ATOM   13075 C CA  . SER K  1 44  ? -23.864 -31.111  4.409   1.000 65.354  0 373 SER KKK CA  1 ? 42 
ATOM   13076 C C   . SER K  1 44  ? -24.544 -32.333  5.028   1.000 57.455  0 373 SER KKK C   1 ? 42 
ATOM   13077 O O   . SER K  1 44  ? -25.399 -32.117  5.853   1.000 55.208  0 373 SER KKK O   1 ? 42 
ATOM   13078 C CB  . SER K  1 44  ? -24.766 -30.509  3.381   1.000 68.760  0 373 SER KKK CB  1 ? 42 
ATOM   13079 O OG  . SER K  1 44  ? -24.508 -29.139  3.233   1.000 73.334  0 373 SER KKK OG  1 ? 42 
ATOM   13080 N N   . PHE K  1 45  ? -24.182 -33.549  4.642   1.000 53.823  0 374 PHE KKK N   1 ? 42 
ATOM   13081 C CA  . PHE K  1 45  ? -24.899 -34.749  5.152   1.000 52.169  0 374 PHE KKK CA  1 ? 42 
ATOM   13082 C C   . PHE K  1 45  ? -24.615 -34.879  6.643   1.000 50.465  0 374 PHE KKK C   1 ? 42 
ATOM   13083 O O   . PHE K  1 45  ? -23.437 -34.769  7.033   1.000 51.054  0 374 PHE KKK O   1 ? 42 
ATOM   13084 C CB  . PHE K  1 45  ? -24.501 -36.011  4.384   1.000 50.764  0 374 PHE KKK CB  1 ? 42 
ATOM   13085 C CG  . PHE K  1 45  ? -24.895 -36.014  2.931   1.000 51.241  0 374 PHE KKK CG  1 ? 42 
ATOM   13086 C CD1 . PHE K  1 45  ? -26.109 -35.500  2.512   1.000 52.467  0 374 PHE KKK CD1 1 ? 42 
ATOM   13087 C CD2 . PHE K  1 45  ? -24.082 -36.622  2.000   1.000 52.243  0 374 PHE KKK CD2 1 ? 42 
ATOM   13088 C CE1 . PHE K  1 45  ? -26.472 -35.550  1.176   1.000 54.658  0 374 PHE KKK CE1 1 ? 42 
ATOM   13089 C CE2 . PHE K  1 45  ? -24.437 -36.639  0.660   1.000 54.580  0 374 PHE KKK CE2 1 ? 42 
ATOM   13090 C CZ  . PHE K  1 45  ? -25.643 -36.128  0.249   1.000 55.155  0 374 PHE KKK CZ  1 ? 42 
ATOM   13091 N N   . SER K  1 46  ? -25.654 -35.091  7.453   1.000 49.093  0 375 SER KKK N   1 ? 42 
ATOM   13092 C CA  . SER K  1 46  ? -25.540 -35.305  8.919   1.000 47.499  0 375 SER KKK CA  1 ? 42 
ATOM   13093 C C   . SER K  1 46  ? -25.013 -36.723  9.183   1.000 45.643  0 375 SER KKK C   1 ? 42 
ATOM   13094 O O   . SER K  1 46  ? -24.353 -36.932  10.202  1.000 44.901  0 375 SER KKK O   1 ? 42 
ATOM   13095 C CB  . SER K  1 46  ? -26.853 -35.071  9.622   1.000 47.639  0 375 SER KKK CB  1 ? 42 
ATOM   13096 O OG  . SER K  1 46  ? -27.881 -35.874  9.072   1.000 48.606  0 375 SER KKK OG  1 ? 42 
ATOM   13097 N N   . THR K  1 47  ? -25.317 -37.662  8.295   1.000 43.548  0 376 THR KKK N   1 ? 42 
ATOM   13098 C CA  . THR K  1 47  ? -25.010 -39.093  8.467   1.000 43.339  0 376 THR KKK CA  1 ? 42 
ATOM   13099 C C   . THR K  1 47  ? -24.891 -39.734  7.083   1.000 42.856  0 376 THR KKK C   1 ? 42 
ATOM   13100 O O   . THR K  1 47  ? -25.593 -39.319  6.141   1.000 43.396  0 376 THR KKK O   1 ? 42 
ATOM   13101 C CB  . THR K  1 47  ? -26.066 -39.763  9.368   1.000 43.226  0 376 THR KKK CB  1 ? 42 
ATOM   13102 O OG1 . THR K  1 47  ? -25.713 -41.089  9.740   1.000 43.019  0 376 THR KKK OG1 1 ? 42 
ATOM   13103 C CG2 . THR K  1 47  ? -27.396 -39.896  8.678   1.000 43.113  0 376 THR KKK CG2 1 ? 42 
ATOM   13104 N N   . PHE K  1 48  ? -23.993 -40.688  6.957   1.000 43.049  0 377 PHE KKK N   1 ? 42 
ATOM   13105 C CA  . PHE K  1 48  ? -23.752 -41.433  5.701   1.000 43.257  0 377 PHE KKK CA  1 ? 42 
ATOM   13106 C C   . PHE K  1 48  ? -23.118 -42.746  6.132   1.000 43.548  0 377 PHE KKK C   1 ? 42 
ATOM   13107 O O   . PHE K  1 48  ? -21.911 -42.779  6.343   1.000 44.464  0 377 PHE KKK O   1 ? 42 
ATOM   13108 C CB  . PHE K  1 48  ? -22.913 -40.590  4.743   1.000 44.299  0 377 PHE KKK CB  1 ? 42 
ATOM   13109 C CG  . PHE K  1 48  ? -22.557 -41.203  3.413   1.000 45.612  0 377 PHE KKK CG  1 ? 42 
ATOM   13110 C CD1 . PHE K  1 48  ? -22.767 -42.541  3.131   1.000 46.728  0 377 PHE KKK CD1 1 ? 42 
ATOM   13111 C CD2 . PHE K  1 48  ? -21.974 -40.415  2.430   1.000 48.175  0 377 PHE KKK CD2 1 ? 42 
ATOM   13112 C CE1 . PHE K  1 48  ? -22.433 -43.068  1.893   1.000 48.332  0 377 PHE KKK CE1 1 ? 42 
ATOM   13113 C CE2 . PHE K  1 48  ? -21.604 -40.956  1.209   1.000 49.091  0 377 PHE KKK CE2 1 ? 42 
ATOM   13114 C CZ  . PHE K  1 48  ? -21.847 -42.276  0.937   1.000 49.255  0 377 PHE KKK CZ  1 ? 42 
ATOM   13115 N N   . LYS K  1 49  ? -23.954 -43.749  6.365   1.000 44.151  0 378 LYS KKK N   1 ? 42 
ATOM   13116 C CA  . LYS K  1 49  ? -23.513 -45.070  6.851   1.000 46.289  0 378 LYS KKK CA  1 ? 42 
ATOM   13117 C C   . LYS K  1 49  ? -23.977 -46.162  5.901   1.000 49.634  0 378 LYS KKK C   1 ? 42 
ATOM   13118 O O   . LYS K  1 49  ? -25.119 -46.099  5.419   1.000 49.634  0 378 LYS KKK O   1 ? 42 
ATOM   13119 C CB  . LYS K  1 49  ? -24.131 -45.400  8.199   1.000 45.694  0 378 LYS KKK CB  1 ? 42 
ATOM   13120 C CG  . LYS K  1 49  ? -23.832 -44.444  9.336   1.000 45.041  0 378 LYS KKK CG  1 ? 42 
ATOM   13121 C CD  . LYS K  1 49  ? -24.288 -45.121  10.600  1.000 46.102  0 378 LYS KKK CD  1 ? 42 
ATOM   13122 C CE  . LYS K  1 49  ? -24.502 -44.226  11.779  1.000 44.892  0 378 LYS KKK CE  1 ? 42 
ATOM   13123 N NZ  . LYS K  1 49  ? -25.021 -45.078  12.857  1.000 45.739  0 378 LYS KKK NZ  1 ? 42 
ATOM   13124 N N   . CYS K  1 50  ? -23.128 -47.162  5.707   1.000 39.363  0 379 CYS KKK N   1 ? 43 
ATOM   13125 C CA  . CYS K  1 50  ? -23.422 -48.340  4.878   1.000 40.768  0 379 CYS KKK CA  1 ? 43 
ATOM   13126 C C   . CYS K  1 50  ? -23.430 -49.583  5.765   1.000 40.876  0 379 CYS KKK C   1 ? 43 
ATOM   13127 O O   . CYS K  1 50  ? -22.796 -49.579  6.844   1.000 41.192  0 379 CYS KKK O   1 ? 43 
ATOM   13128 C CB  . CYS K  1 50  ? -22.432 -48.418  3.720   1.000 44.775  0 379 CYS KKK CB  1 ? 43 
ATOM   13129 S SG  . CYS K  1 50  ? -22.469 -46.945  2.676   1.000 46.803  0 379 CYS KKK SG  1 ? 43 
ATOM   13130 N N   . TYR K  1 51  ? -24.184 -50.577  5.308   1.000 41.574  0 380 TYR KKK N   1 ? 43 
ATOM   13131 C CA  . TYR K  1 51  ? -24.415 -51.890  5.955   1.000 43.039  0 380 TYR KKK CA  1 ? 43 
ATOM   13132 C C   . TYR K  1 51  ? -24.101 -52.969  4.921   1.000 44.096  0 380 TYR KKK C   1 ? 43 
ATOM   13133 O O   . TYR K  1 51  ? -24.642 -52.901  3.812   1.000 44.187  0 380 TYR KKK O   1 ? 43 
ATOM   13134 C CB  . TYR K  1 51  ? -25.852 -51.924  6.492   1.000 41.372  0 380 TYR KKK CB  1 ? 43 
ATOM   13135 C CG  . TYR K  1 51  ? -26.164 -50.790  7.437   1.000 40.349  0 380 TYR KKK CG  1 ? 43 
ATOM   13136 C CD1 . TYR K  1 51  ? -26.564 -49.542  6.979   1.000 41.098  0 380 TYR KKK CD1 1 ? 43 
ATOM   13137 C CD2 . TYR K  1 51  ? -25.985 -50.944  8.794   1.000 40.234  0 380 TYR KKK CD2 1 ? 43 
ATOM   13138 C CE1 . TYR K  1 51  ? -26.783 -48.484  7.856   1.000 40.089  0 380 TYR KKK CE1 1 ? 43 
ATOM   13139 C CE2 . TYR K  1 51  ? -26.284 -49.928  9.680   1.000 40.466  0 380 TYR KKK CE2 1 ? 43 
ATOM   13140 C CZ  . TYR K  1 51  ? -26.639 -48.681  9.211   1.000 39.208  0 380 TYR KKK CZ  1 ? 43 
ATOM   13141 O OH  . TYR K  1 51  ? -26.804 -47.641  10.082  1.000 36.738  0 380 TYR KKK OH  1 ? 43 
ATOM   13142 N N   . GLY K  1 52  ? -23.220 -53.907  5.263   1.000 46.974  0 381 GLY KKK N   1 ? 43 
ATOM   13143 C CA  . GLY K  1 52  ? -22.860 -55.023  4.376   1.000 49.135  0 381 GLY KKK CA  1 ? 43 
ATOM   13144 C C   . GLY K  1 52  ? -21.808 -54.645  3.340   1.000 51.008  0 381 GLY KKK C   1 ? 43 
ATOM   13145 O O   . GLY K  1 52  ? -21.286 -55.549  2.705   1.000 55.684  0 381 GLY KKK O   1 ? 43 
ATOM   13146 N N   . VAL K  1 53  ? -21.483 -53.370  3.165   1.000 50.777  0 382 VAL KKK N   1 ? 43 
ATOM   13147 C CA  . VAL K  1 53  ? -20.354 -52.918  2.306   1.000 52.180  0 382 VAL KKK CA  1 ? 43 
ATOM   13148 C C   . VAL K  1 53  ? -19.728 -51.687  2.957   1.000 50.964  0 382 VAL KKK C   1 ? 43 
ATOM   13149 O O   . VAL K  1 53  ? -20.449 -50.886  3.570   1.000 46.446  0 382 VAL KKK O   1 ? 43 
ATOM   13150 C CB  . VAL K  1 53  ? -20.822 -52.596  0.874   1.000 53.383  0 382 VAL KKK CB  1 ? 43 
ATOM   13151 C CG1 . VAL K  1 53  ? -21.263 -53.865  0.177   1.000 56.688  0 382 VAL KKK CG1 1 ? 43 
ATOM   13152 C CG2 . VAL K  1 53  ? -21.947 -51.555  0.866   1.000 51.013  0 382 VAL KKK CG2 1 ? 43 
ATOM   13153 N N   . SER K  1 54  ? -18.429 -51.528  2.757   1.000 53.982  0 383 SER KKK N   1 ? 43 
ATOM   13154 C CA  . SER K  1 54  ? -17.676 -50.343  3.210   1.000 54.387  0 383 SER KKK CA  1 ? 43 
ATOM   13155 C C   . SER K  1 54  ? -17.976 -49.187  2.261   1.000 53.333  0 383 SER KKK C   1 ? 43 
ATOM   13156 O O   . SER K  1 54  ? -18.015 -49.364  1.051   1.000 53.454  0 383 SER KKK O   1 ? 43 
ATOM   13157 C CB  . SER K  1 54  ? -16.220 -50.645  3.280   1.000 56.921  0 383 SER KKK CB  1 ? 43 
ATOM   13158 O OG  . SER K  1 54  ? -15.511 -49.471  3.617   1.000 58.915  0 383 SER KKK OG  1 ? 43 
ATOM   13159 N N   . PRO K  1 55  ? -18.230 -47.965  2.785   1.000 53.784  0 384 PRO KKK N   1 ? 43 
ATOM   13160 C CA  . PRO K  1 55  ? -18.368 -46.765  1.956   1.000 53.436  0 384 PRO KKK CA  1 ? 43 
ATOM   13161 C C   . PRO K  1 55  ? -17.186 -46.549  0.999   1.000 55.287  0 384 PRO KKK C   1 ? 43 
ATOM   13162 O O   . PRO K  1 55  ? -17.396 -45.958  -0.069  1.000 54.563  0 384 PRO KKK O   1 ? 43 
ATOM   13163 C CB  . PRO K  1 55  ? -18.419 -45.627  2.988   1.000 49.989  0 384 PRO KKK CB  1 ? 43 
ATOM   13164 C CG  . PRO K  1 55  ? -19.087 -46.280  4.166   1.000 49.820  0 384 PRO KKK CG  1 ? 43 
ATOM   13165 C CD  . PRO K  1 55  ? -18.464 -47.663  4.206   1.000 51.617  0 384 PRO KKK CD  1 ? 43 
ATOM   13166 N N   . THR K  1 56  ? -16.006 -47.035  1.389   1.000 57.743  0 385 THR KKK N   1 ? 43 
ATOM   13167 C CA  . THR K  1 56  ? -14.757 -46.916  0.595   1.000 61.628  0 385 THR KKK CA  1 ? 43 
ATOM   13168 C C   . THR K  1 56  ? -14.846 -47.771  -0.674  1.000 65.429  0 385 THR KKK C   1 ? 43 
ATOM   13169 O O   . THR K  1 56  ? -14.012 -47.572  -1.545  1.000 68.387  0 385 THR KKK O   1 ? 43 
ATOM   13170 C CB  . THR K  1 56  ? -13.509 -47.314  1.411   1.000 61.502  0 385 THR KKK CB  1 ? 43 
ATOM   13171 O OG1 . THR K  1 56  ? -13.554 -48.702  1.759   1.000 58.875  0 385 THR KKK OG1 1 ? 43 
ATOM   13172 C CG2 . THR K  1 56  ? -13.334 -46.467  2.653   1.000 59.579  0 385 THR KKK CG2 1 ? 43 
ATOM   13173 N N   . LYS K  1 57  ? -15.791 -48.706  -0.769  1.000 67.006  0 386 LYS KKK N   1 ? 43 
ATOM   13174 C CA  . LYS K  1 57  ? -15.839 -49.668  -1.893  1.000 68.884  0 386 LYS KKK CA  1 ? 43 
ATOM   13175 C C   . LYS K  1 57  ? -17.014 -49.366  -2.823  1.000 66.708  0 386 LYS KKK C   1 ? 43 
ATOM   13176 O O   . LYS K  1 57  ? -17.123 -50.082  -3.806  1.000 69.190  0 386 LYS KKK O   1 ? 43 
ATOM   13177 C CB  . LYS K  1 57  ? -15.939 -51.099  -1.374  1.000 71.853  0 386 LYS KKK CB  1 ? 43 
ATOM   13178 C CG  . LYS K  1 57  ? -14.788 -51.536  -0.484  1.000 76.137  0 386 LYS KKK CG  1 ? 43 
ATOM   13179 C CD  . LYS K  1 57  ? -14.577 -53.074  -0.407  1.000 81.320  0 386 LYS KKK CD  1 ? 43 
ATOM   13180 C CE  . LYS K  1 57  ? -14.679 -53.666  1.000   1.000 85.720  0 386 LYS KKK CE  1 ? 43 
ATOM   13181 N NZ  . LYS K  1 57  ? -13.404 -54.237  1.532   1.000 89.071  0 386 LYS KKK NZ  1 ? 43 
ATOM   13182 N N   . LEU K  1 58  ? -17.815 -48.333  -2.578  1.000 64.188  0 387 LEU KKK N   1 ? 43 
ATOM   13183 C CA  . LEU K  1 58  ? -19.066 -48.125  -3.362  1.000 63.112  0 387 LEU KKK CA  1 ? 43 
ATOM   13184 C C   . LEU K  1 58  ? -18.748 -47.940  -4.852  1.000 63.610  0 387 LEU KKK C   1 ? 43 
ATOM   13185 O O   . LEU K  1 58  ? -19.542 -48.424  -5.693  1.000 60.946  0 387 LEU KKK O   1 ? 43 
ATOM   13186 C CB  . LEU K  1 58  ? -19.865 -46.937  -2.823  1.000 61.947  0 387 LEU KKK CB  1 ? 43 
ATOM   13187 C CG  . LEU K  1 58  ? -20.414 -47.113  -1.409  1.000 60.385  0 387 LEU KKK CG  1 ? 43 
ATOM   13188 C CD1 . LEU K  1 58  ? -21.178 -45.869  -1.005  1.000 62.335  0 387 LEU KKK CD1 1 ? 43 
ATOM   13189 C CD2 . LEU K  1 58  ? -21.297 -48.328  -1.298  1.000 58.981  0 387 LEU KKK CD2 1 ? 43 
ATOM   13190 N N   . ASN K  1 59  ? -17.614 -47.318  -5.188  1.000 64.851  0 388 ASN KKK N   1 ? 43 
ATOM   13191 C CA  . ASN K  1 59  ? -17.275 -47.065  -6.612  1.000 67.433  0 388 ASN KKK CA  1 ? 43 
ATOM   13192 C C   . ASN K  1 59  ? -16.714 -48.326  -7.283  1.000 68.559  0 388 ASN KKK C   1 ? 43 
ATOM   13193 O O   . ASN K  1 59  ? -16.476 -48.257  -8.483  1.000 70.581  0 388 ASN KKK O   1 ? 43 
ATOM   13194 C CB  . ASN K  1 59  ? -16.363 -45.855  -6.776  1.000 69.097  0 388 ASN KKK CB  1 ? 43 
ATOM   13195 C CG  . ASN K  1 59  ? -17.165 -44.569  -6.901  1.000 71.863  0 388 ASN KKK CG  1 ? 43 
ATOM   13196 O OD1 . ASN K  1 59  ? -18.371 -44.586  -7.156  1.000 74.370  0 388 ASN KKK OD1 1 ? 43 
ATOM   13197 N ND2 . ASN K  1 59  ? -16.514 -43.434  -6.717  1.000 73.803  0 388 ASN KKK ND2 1 ? 43 
ATOM   13198 N N   . ASP K  1 60  ? -16.547 -49.440  -6.565  1.000 66.393  0 389 ASP KKK N   1 ? 43 
ATOM   13199 C CA  . ASP K  1 60  ? -15.920 -50.677  -7.103  1.000 68.848  0 389 ASP KKK CA  1 ? 43 
ATOM   13200 C C   . ASP K  1 60  ? -16.912 -51.842  -7.158  1.000 67.187  0 389 ASP KKK C   1 ? 43 
ATOM   13201 O O   . ASP K  1 60  ? -16.477 -52.931  -7.513  1.000 70.550  0 389 ASP KKK O   1 ? 43 
ATOM   13202 C CB  . ASP K  1 60  ? -14.742 -51.131  -6.248  1.000 71.955  0 389 ASP KKK CB  1 ? 43 
ATOM   13203 C CG  . ASP K  1 60  ? -13.667 -50.073  -6.113  1.000 77.925  0 389 ASP KKK CG  1 ? 43 
ATOM   13204 O OD1 . ASP K  1 60  ? -13.115 -49.640  -7.141  1.000 83.968  0 389 ASP KKK OD1 1 ? 43 
ATOM   13205 O OD2 . ASP K  1 60  ? -13.399 -49.671  -4.984  1.000 84.995  0 389 ASP KKK OD2 1 ? 43 
ATOM   13206 N N   . LEU K  1 61  ? -18.181 -51.635  -6.829  1.000 63.462  0 390 LEU KKK N   1 ? 43 
ATOM   13207 C CA  . LEU K  1 61  ? -19.162 -52.742  -6.728  1.000 63.059  0 390 LEU KKK CA  1 ? 43 
ATOM   13208 C C   . LEU K  1 61  ? -20.201 -52.641  -7.847  1.000 62.004  0 390 LEU KKK C   1 ? 43 
ATOM   13209 O O   . LEU K  1 61  ? -20.498 -51.524  -8.328  1.000 61.581  0 390 LEU KKK O   1 ? 43 
ATOM   13210 C CB  . LEU K  1 61  ? -19.829 -52.693  -5.349  1.000 61.991  0 390 LEU KKK CB  1 ? 43 
ATOM   13211 C CG  . LEU K  1 61  ? -18.897 -52.953  -4.160  1.000 62.482  0 390 LEU KKK CG  1 ? 43 
ATOM   13212 C CD1 . LEU K  1 61  ? -19.657 -52.840  -2.848  1.000 60.771  0 390 LEU KKK CD1 1 ? 43 
ATOM   13213 C CD2 . LEU K  1 61  ? -18.199 -54.312  -4.266  1.000 63.548  0 390 LEU KKK CD2 1 ? 43 
ATOM   13214 N N   . CYS K  1 62  ? -20.717 -53.796  -8.256  1.000 63.111  0 391 CYS KKK N   1 ? 43 
ATOM   13215 C CA  . CYS K  1 62  ? -21.809 -53.960  -9.238  1.000 62.906  0 391 CYS KKK CA  1 ? 43 
ATOM   13216 C C   . CYS K  1 62  ? -23.005 -54.604  -8.537  1.000 58.933  0 391 CYS KKK C   1 ? 43 
ATOM   13217 O O   . CYS K  1 62  ? -22.795 -55.487  -7.719  1.000 56.951  0 391 CYS KKK O   1 ? 43 
ATOM   13218 C CB  . CYS K  1 62  ? -21.331 -54.804  -10.406 1.000 67.007  0 391 CYS KKK CB  1 ? 43 
ATOM   13219 S SG  . CYS K  1 62  ? -20.144 -53.922  -11.445 1.000 72.662  0 391 CYS KKK SG  1 ? 43 
ATOM   13220 N N   . PHE K  1 63  ? -24.213 -54.160  -8.869  1.000 57.905  0 392 PHE KKK N   1 ? 43 
ATOM   13221 C CA  . PHE K  1 63  ? -25.504 -54.659  -8.341  1.000 58.411  0 392 PHE KKK CA  1 ? 43 
ATOM   13222 C C   . PHE K  1 63  ? -26.484 -54.848  -9.503  1.000 59.318  0 392 PHE KKK C   1 ? 43 
ATOM   13223 O O   . PHE K  1 63  ? -26.246 -54.307  -10.583 1.000 60.562  0 392 PHE KKK O   1 ? 43 
ATOM   13224 C CB  . PHE K  1 63  ? -26.006 -53.660  -7.302  1.000 57.070  0 392 PHE KKK CB  1 ? 43 
ATOM   13225 C CG  . PHE K  1 63  ? -25.082 -53.508  -6.127  1.000 56.046  0 392 PHE KKK CG  1 ? 43 
ATOM   13226 C CD1 . PHE K  1 63  ? -24.886 -54.549  -5.231  1.000 55.805  0 392 PHE KKK CD1 1 ? 43 
ATOM   13227 C CD2 . PHE K  1 63  ? -24.393 -52.325  -5.937  1.000 54.643  0 392 PHE KKK CD2 1 ? 43 
ATOM   13228 C CE1 . PHE K  1 63  ? -24.017 -54.397  -4.162  1.000 55.234  0 392 PHE KKK CE1 1 ? 43 
ATOM   13229 C CE2 . PHE K  1 63  ? -23.513 -52.185  -4.881  1.000 54.217  0 392 PHE KKK CE2 1 ? 43 
ATOM   13230 C CZ  . PHE K  1 63  ? -23.337 -53.212  -3.984  1.000 54.655  0 392 PHE KKK CZ  1 ? 43 
ATOM   13231 N N   . THR K  1 64  ? -27.522 -55.649  -9.308  1.000 60.310  0 393 THR KKK N   1 ? 43 
ATOM   13232 C CA  . THR K  1 64  ? -28.595 -55.902  -10.307 1.000 63.865  0 393 THR KKK CA  1 ? 43 
ATOM   13233 C C   . THR K  1 64  ? -29.460 -54.642  -10.407 1.000 62.228  0 393 THR KKK C   1 ? 43 
ATOM   13234 O O   . THR K  1 64  ? -29.888 -54.274  -11.500 1.000 63.206  0 393 THR KKK O   1 ? 43 
ATOM   13235 C CB  . THR K  1 64  ? -29.505 -57.070  -9.907  1.000 65.039  0 393 THR KKK CB  1 ? 43 
ATOM   13236 O OG1 . THR K  1 64  ? -28.810 -57.942  -9.007  1.000 66.603  0 393 THR KKK OG1 1 ? 43 
ATOM   13237 C CG2 . THR K  1 64  ? -30.001 -57.810  -11.130 1.000 67.924  0 393 THR KKK CG2 1 ? 43 
ATOM   13238 N N   . ASN K  1 65  ? -29.666 -54.005  -9.259  1.000 60.600  0 394 ASN KKK N   1 ? 43 
ATOM   13239 C CA  . ASN K  1 65  ? -30.514 -52.808  -9.126  1.000 58.724  0 394 ASN KKK CA  1 ? 43 
ATOM   13240 C C   . ASN K  1 65  ? -30.088 -52.054  -7.876  1.000 56.608  0 394 ASN KKK C   1 ? 43 
ATOM   13241 O O   . ASN K  1 65  ? -29.549 -52.644  -6.930  1.000 53.800  0 394 ASN KKK O   1 ? 43 
ATOM   13242 C CB  . ASN K  1 65  ? -31.986 -53.197  -9.006  1.000 58.766  0 394 ASN KKK CB  1 ? 43 
ATOM   13243 C CG  . ASN K  1 65  ? -32.569 -53.631  -10.330 1.000 60.326  0 394 ASN KKK CG  1 ? 43 
ATOM   13244 O OD1 . ASN K  1 65  ? -32.682 -52.835  -11.251 1.000 61.933  0 394 ASN KKK OD1 1 ? 43 
ATOM   13245 N ND2 . ASN K  1 65  ? -32.883 -54.905  -10.459 1.000 61.720  0 394 ASN KKK ND2 1 ? 43 
ATOM   13246 N N   . VAL K  1 66  ? -30.415 -50.778  -7.852  1.000 55.302  0 395 VAL KKK N   1 ? 43 
ATOM   13247 C CA  . VAL K  1 66  ? -30.365 -49.959  -6.616  1.000 52.481  0 395 VAL KKK CA  1 ? 43 
ATOM   13248 C C   . VAL K  1 66  ? -31.750 -49.359  -6.437  1.000 52.007  0 395 VAL KKK C   1 ? 43 
ATOM   13249 O O   . VAL K  1 66  ? -32.369 -49.024  -7.432  1.000 52.910  0 395 VAL KKK O   1 ? 43 
ATOM   13250 C CB  . VAL K  1 66  ? -29.256 -48.914  -6.733  1.000 52.223  0 395 VAL KKK CB  1 ? 43 
ATOM   13251 C CG1 . VAL K  1 66  ? -29.208 -48.039  -5.496  1.000 53.320  0 395 VAL KKK CG1 1 ? 43 
ATOM   13252 C CG2 . VAL K  1 66  ? -27.904 -49.587  -6.946  1.000 52.404  0 395 VAL KKK CG2 1 ? 43 
ATOM   13253 N N   . TYR K  1 67  ? -32.240 -49.331  -5.214  1.000 50.288  0 396 TYR KKK N   1 ? 43 
ATOM   13254 C CA  . TYR K  1 67  ? -33.510 -48.649  -4.867  1.000 51.291  0 396 TYR KKK CA  1 ? 43 
ATOM   13255 C C   . TYR K  1 67  ? -33.197 -47.470  -3.965  1.000 48.054  0 396 TYR KKK C   1 ? 43 
ATOM   13256 O O   . TYR K  1 67  ? -32.361 -47.618  -3.052  1.000 47.329  0 396 TYR KKK O   1 ? 43 
ATOM   13257 C CB  . TYR K  1 67  ? -34.480 -49.591  -4.180  1.000 52.426  0 396 TYR KKK CB  1 ? 43 
ATOM   13258 C CG  . TYR K  1 67  ? -34.934 -50.695  -5.077  1.000 55.050  0 396 TYR KKK CG  1 ? 43 
ATOM   13259 C CD1 . TYR K  1 67  ? -35.710 -50.435  -6.189  1.000 56.218  0 396 TYR KKK CD1 1 ? 43 
ATOM   13260 C CD2 . TYR K  1 67  ? -34.355 -51.952  -4.941  1.000 58.982  0 396 TYR KKK CD2 1 ? 43 
ATOM   13261 C CE1 . TYR K  1 67  ? -36.038 -51.462  -7.064  1.000 61.320  0 396 TYR KKK CE1 1 ? 43 
ATOM   13262 C CE2 . TYR K  1 67  ? -34.651 -52.983  -5.823  1.000 62.886  0 396 TYR KKK CE2 1 ? 43 
ATOM   13263 C CZ  . TYR K  1 67  ? -35.494 -52.732  -6.890  1.000 62.574  0 396 TYR KKK CZ  1 ? 43 
ATOM   13264 O OH  . TYR K  1 67  ? -35.774 -53.763  -7.733  1.000 64.045  0 396 TYR KKK OH  1 ? 43 
ATOM   13265 N N   . ALA K  1 68  ? -33.800 -46.334  -4.293  1.000 47.894  0 397 ALA KKK N   1 ? 43 
ATOM   13266 C CA  . ALA K  1 68  ? -33.665 -45.079  -3.534  1.000 47.723  0 397 ALA KKK CA  1 ? 43 
ATOM   13267 C C   . ALA K  1 68  ? -35.026 -44.776  -2.910  1.000 45.199  0 397 ALA KKK C   1 ? 43 
ATOM   13268 O O   . ALA K  1 68  ? -35.963 -44.417  -3.648  1.000 42.827  0 397 ALA KKK O   1 ? 43 
ATOM   13269 C CB  . ALA K  1 68  ? -33.165 -43.980  -4.432  1.000 47.984  0 397 ALA KKK CB  1 ? 43 
ATOM   13270 N N   . ASP K  1 69  ? -35.108 -44.985  -1.594  1.000 42.005  0 398 ASP KKK N   1 ? 43 
ATOM   13271 C CA  . ASP K  1 69  ? -36.271 -44.628  -0.751  1.000 41.802  0 398 ASP KKK CA  1 ? 43 
ATOM   13272 C C   . ASP K  1 69  ? -35.969 -43.280  -0.114  1.000 41.114  0 398 ASP KKK C   1 ? 43 
ATOM   13273 O O   . ASP K  1 69  ? -34.853 -43.115  0.386   1.000 40.412  0 398 ASP KKK O   1 ? 43 
ATOM   13274 C CB  . ASP K  1 69  ? -36.532 -45.705  0.308   1.000 40.845  0 398 ASP KKK CB  1 ? 43 
ATOM   13275 C CG  . ASP K  1 69  ? -36.746 -47.089  -0.279  1.000 41.715  0 398 ASP KKK CG  1 ? 43 
ATOM   13276 O OD1 . ASP K  1 69  ? -37.218 -47.141  -1.422  1.000 43.220  0 398 ASP KKK OD1 1 ? 43 
ATOM   13277 O OD2 . ASP K  1 69  ? -36.423 -48.087  0.396   1.000 39.312  0 398 ASP KKK OD2 1 ? 43 
ATOM   13278 N N   . SER K  1 70  ? -36.921 -42.352  -0.133  1.000 42.205  0 399 SER KKK N   1 ? 43 
ATOM   13279 C CA  . SER K  1 70  ? -36.708 -41.019  0.466   1.000 42.328  0 399 SER KKK CA  1 ? 43 
ATOM   13280 C C   . SER K  1 70  ? -37.963 -40.552  1.200   1.000 40.696  0 399 SER KKK C   1 ? 43 
ATOM   13281 O O   . SER K  1 70  ? -39.082 -40.929  0.784   1.000 40.455  0 399 SER KKK O   1 ? 43 
ATOM   13282 C CB  . SER K  1 70  ? -36.267 -40.057  -0.600  1.000 45.693  0 399 SER KKK CB  1 ? 43 
ATOM   13283 O OG  . SER K  1 70  ? -37.220 -40.005  -1.648  1.000 49.290  0 399 SER KKK OG  1 ? 43 
ATOM   13284 N N   . PHE K  1 71  ? -37.760 -39.725  2.225   1.000 38.341  0 400 PHE KKK N   1 ? 43 
ATOM   13285 C CA  . PHE K  1 71  ? -38.827 -39.200  3.096   1.000 39.264  0 400 PHE KKK CA  1 ? 43 
ATOM   13286 C C   . PHE K  1 71  ? -38.253 -38.187  4.094   1.000 40.616  0 400 PHE KKK C   1 ? 43 
ATOM   13287 O O   . PHE K  1 71  ? -37.032 -38.026  4.136   1.000 39.146  0 400 PHE KKK O   1 ? 43 
ATOM   13288 C CB  . PHE K  1 71  ? -39.478 -40.365  3.841   1.000 39.955  0 400 PHE KKK CB  1 ? 43 
ATOM   13289 C CG  . PHE K  1 71  ? -38.498 -41.295  4.519   1.000 40.102  0 400 PHE KKK CG  1 ? 43 
ATOM   13290 C CD1 . PHE K  1 71  ? -37.929 -40.973  5.732   1.000 41.185  0 400 PHE KKK CD1 1 ? 43 
ATOM   13291 C CD2 . PHE K  1 71  ? -38.145 -42.501  3.938   1.000 42.344  0 400 PHE KKK CD2 1 ? 43 
ATOM   13292 C CE1 . PHE K  1 71  ? -37.040 -41.837  6.347   1.000 41.838  0 400 PHE KKK CE1 1 ? 43 
ATOM   13293 C CE2 . PHE K  1 71  ? -37.241 -43.356  4.544   1.000 41.946  0 400 PHE KKK CE2 1 ? 43 
ATOM   13294 C CZ  . PHE K  1 71  ? -36.696 -43.022  5.747   1.000 41.396  0 400 PHE KKK CZ  1 ? 43 
ATOM   13295 N N   . VAL K  1 72  ? -39.119 -37.558  4.892   1.000 41.728  0 401 VAL KKK N   1 ? 43 
ATOM   13296 C CA  . VAL K  1 72  ? -38.742 -36.600  5.971   1.000 42.251  0 401 VAL KKK CA  1 ? 43 
ATOM   13297 C C   . VAL K  1 72  ? -39.110 -37.191  7.339   1.000 41.936  0 401 VAL KKK C   1 ? 43 
ATOM   13298 O O   . VAL K  1 72  ? -40.215 -37.752  7.464   1.000 41.227  0 401 VAL KKK O   1 ? 43 
ATOM   13299 C CB  . VAL K  1 72  ? -39.408 -35.234  5.741   1.000 43.716  0 401 VAL KKK CB  1 ? 43 
ATOM   13300 C CG1 . VAL K  1 72  ? -39.276 -34.316  6.953   1.000 45.230  0 401 VAL KKK CG1 1 ? 43 
ATOM   13301 C CG2 . VAL K  1 72  ? -38.836 -34.567  4.514   1.000 45.069  0 401 VAL KKK CG2 1 ? 43 
ATOM   13302 N N   . ILE K  1 73  ? -38.220 -37.024  8.321   1.000 42.677  0 402 ILE KKK N   1 ? 43 
ATOM   13303 C CA  . ILE K  1 73  ? -38.450 -37.352  9.757   1.000 44.885  0 402 ILE KKK CA  1 ? 43 
ATOM   13304 C C   . ILE K  1 73  ? -37.790 -36.271  10.624  1.000 44.936  0 402 ILE KKK C   1 ? 43 
ATOM   13305 O O   . ILE K  1 73  ? -37.188 -35.371  10.054  1.000 43.530  0 402 ILE KKK O   1 ? 43 
ATOM   13306 C CB  . ILE K  1 73  ? -37.930 -38.771  10.078  1.000 45.361  0 402 ILE KKK CB  1 ? 43 
ATOM   13307 C CG1 . ILE K  1 73  ? -36.463 -38.946  9.683   1.000 45.818  0 402 ILE KKK CG1 1 ? 43 
ATOM   13308 C CG2 . ILE K  1 73  ? -38.819 -39.831  9.429   1.000 44.842  0 402 ILE KKK CG2 1 ? 43 
ATOM   13309 C CD1 . ILE K  1 73  ? -35.858 -40.231  10.180  1.000 46.401  0 402 ILE KKK CD1 1 ? 43 
ATOM   13310 N N   . ARG K  1 74  ? -37.961 -36.330  11.950  1.000 46.839  0 403 ARG KKK N   1 ? 43 
ATOM   13311 C CA  . ARG K  1 74  ? -37.269 -35.464  12.933  1.000 47.402  0 403 ARG KKK CA  1 ? 43 
ATOM   13312 C C   . ARG K  1 74  ? -35.801 -35.880  13.041  1.000 46.396  0 403 ARG KKK C   1 ? 43 
ATOM   13313 O O   . ARG K  1 74  ? -35.511 -37.076  12.889  1.000 45.841  0 403 ARG KKK O   1 ? 43 
ATOM   13314 C CB  . ARG K  1 74  ? -37.805 -35.670  14.348  1.000 53.368  0 403 ARG KKK CB  1 ? 43 
ATOM   13315 C CG  . ARG K  1 74  ? -39.136 -35.014  14.645  1.000 59.910  0 403 ARG KKK CG  1 ? 43 
ATOM   13316 C CD  . ARG K  1 74  ? -39.763 -35.645  15.867  1.000 65.445  0 403 ARG KKK CD  1 ? 43 
ATOM   13317 N NE  . ARG K  1 74  ? -38.894 -35.557  17.011  1.000 71.531  0 403 ARG KKK NE  1 ? 43 
ATOM   13318 C CZ  . ARG K  1 74  ? -39.125 -36.115  18.185  1.000 77.542  0 403 ARG KKK CZ  1 ? 43 
ATOM   13319 N NH1 . ARG K  1 74  ? -40.179 -36.885  18.360  1.000 83.323  0 403 ARG KKK NH1 1 ? 43 
ATOM   13320 N NH2 . ARG K  1 74  ? -38.258 -35.957  19.167  1.000 78.024  0 403 ARG KKK NH2 1 ? 43 
ATOM   13321 N N   . GLY K  1 75  ? -34.942 -34.935  13.412  1.000 46.662  0 404 GLY KKK N   1 ? 43 
ATOM   13322 C CA  . GLY K  1 75  ? -33.508 -35.156  13.660  1.000 47.722  0 404 GLY KKK CA  1 ? 43 
ATOM   13323 C C   . GLY K  1 75  ? -33.265 -36.351  14.564  1.000 48.412  0 404 GLY KKK C   1 ? 43 
ATOM   13324 O O   . GLY K  1 75  ? -32.444 -37.199  14.182  1.000 46.361  0 404 GLY KKK O   1 ? 43 
ATOM   13325 N N   . ASP K  1 76  ? -33.945 -36.465  15.704  1.000 48.285  0 405 ASP KKK N   1 ? 43 
ATOM   13326 C CA  . ASP K  1 76  ? -33.573 -37.521  16.679  1.000 52.895  0 405 ASP KKK CA  1 ? 43 
ATOM   13327 C C   . ASP K  1 76  ? -34.253 -38.841  16.306  1.000 49.225  0 405 ASP KKK C   1 ? 43 
ATOM   13328 O O   . ASP K  1 76  ? -33.998 -39.811  17.001  1.000 50.018  0 405 ASP KKK O   1 ? 43 
ATOM   13329 C CB  . ASP K  1 76  ? -33.709 -37.070  18.143  1.000 58.414  0 405 ASP KKK CB  1 ? 43 
ATOM   13330 C CG  . ASP K  1 76  ? -35.042 -36.474  18.523  1.000 65.210  0 405 ASP KKK CG  1 ? 43 
ATOM   13331 O OD1 . ASP K  1 76  ? -36.043 -36.811  17.846  1.000 68.132  0 405 ASP KKK OD1 1 ? 43 
ATOM   13332 O OD2 . ASP K  1 76  ? -35.069 -35.671  19.494  1.000 75.241  0 405 ASP KKK OD2 1 ? 43 
ATOM   13333 N N   . GLU K  1 77  ? -34.968 -38.916  15.182  1.000 48.838  0 406 GLU KKK N   1 ? 43 
ATOM   13334 C CA  . GLU K  1 77  ? -35.493 -40.198  14.653  1.000 47.108  0 406 GLU KKK CA  1 ? 43 
ATOM   13335 C C   . GLU K  1 77  ? -34.526 -40.764  13.597  1.000 46.512  0 406 GLU KKK C   1 ? 43 
ATOM   13336 O O   . GLU K  1 77  ? -34.718 -41.930  13.200  1.000 43.960  0 406 GLU KKK O   1 ? 43 
ATOM   13337 C CB  . GLU K  1 77  ? -36.895 -40.004  14.070  1.000 49.957  0 406 GLU KKK CB  1 ? 43 
ATOM   13338 C CG  . GLU K  1 77  ? -37.988 -39.758  15.107  1.000 52.697  0 406 GLU KKK CG  1 ? 43 
ATOM   13339 C CD  . GLU K  1 77  ? -39.337 -39.340  14.519  1.000 53.943  0 406 GLU KKK CD  1 ? 43 
ATOM   13340 O OE1 . GLU K  1 77  ? -39.377 -38.880  13.341  1.000 48.140  0 406 GLU KKK OE1 1 ? 43 
ATOM   13341 O OE2 . GLU K  1 77  ? -40.348 -39.453  15.250  1.000 56.592  0 406 GLU KKK OE2 1 ? 43 
ATOM   13342 N N   . VAL K  1 78  ? -33.523 -40.009  13.136  1.000 45.124  0 407 VAL KKK N   1 ? 43 
ATOM   13343 C CA  . VAL K  1 78  ? -32.623 -40.484  12.046  1.000 44.435  0 407 VAL KKK CA  1 ? 43 
ATOM   13344 C C   . VAL K  1 78  ? -31.929 -41.802  12.450  1.000 42.719  0 407 VAL KKK C   1 ? 43 
ATOM   13345 O O   . VAL K  1 78  ? -31.828 -42.679  11.594  1.000 41.050  0 407 VAL KKK O   1 ? 43 
ATOM   13346 C CB  . VAL K  1 78  ? -31.638 -39.393  11.574  1.000 43.870  0 407 VAL KKK CB  1 ? 43 
ATOM   13347 C CG1 . VAL K  1 78  ? -30.609 -39.947  10.599  1.000 42.829  0 407 VAL KKK CG1 1 ? 43 
ATOM   13348 C CG2 . VAL K  1 78  ? -32.379 -38.259  10.895  1.000 43.726  0 407 VAL KKK CG2 1 ? 43 
ATOM   13349 N N   . ARG K  1 79  ? -31.523 -41.956  13.705  1.000 43.427  0 408 ARG KKK N   1 ? 43 
ATOM   13350 C CA  . ARG K  1 79  ? -30.910 -43.203  14.239  1.000 46.226  0 408 ARG KKK CA  1 ? 43 
ATOM   13351 C C   . ARG K  1 79  ? -31.817 -44.431  14.000  1.000 45.850  0 408 ARG KKK C   1 ? 43 
ATOM   13352 O O   . ARG K  1 79  ? -31.285 -45.540  14.011  1.000 48.247  0 408 ARG KKK O   1 ? 43 
ATOM   13353 C CB  . ARG K  1 79  ? -30.615 -43.035  15.733  1.000 50.629  0 408 ARG KKK CB  1 ? 43 
ATOM   13354 C CG  . ARG K  1 79  ? -31.867 -43.011  16.610  1.000 55.433  0 408 ARG KKK CG  1 ? 43 
ATOM   13355 C CD  . ARG K  1 79  ? -31.568 -42.903  18.076  1.000 60.493  0 408 ARG KKK CD  1 ? 43 
ATOM   13356 N NE  . ARG K  1 79  ? -31.392 -41.457  18.160  1.000 63.085  0 408 ARG KKK NE  1 ? 43 
ATOM   13357 C CZ  . ARG K  1 79  ? -31.004 -40.750  19.207  1.000 68.188  0 408 ARG KKK CZ  1 ? 43 
ATOM   13358 N NH1 . ARG K  1 79  ? -30.716 -41.332  20.367  1.000 68.915  0 408 ARG KKK NH1 1 ? 43 
ATOM   13359 N NH2 . ARG K  1 79  ? -30.913 -39.428  19.078  1.000 67.301  0 408 ARG KKK NH2 1 ? 43 
ATOM   13360 N N   . GLN K  1 80  ? -33.137 -44.265  13.810  1.000 44.905  0 409 GLN KKK N   1 ? 43 
ATOM   13361 C CA  . GLN K  1 80  ? -34.086 -45.392  13.608  1.000 45.017  0 409 GLN KKK CA  1 ? 43 
ATOM   13362 C C   . GLN K  1 80  ? -34.015 -45.915  12.170  1.000 43.726  0 409 GLN KKK C   1 ? 43 
ATOM   13363 O O   . GLN K  1 80  ? -34.520 -47.029  11.927  1.000 43.755  0 409 GLN KKK O   1 ? 43 
ATOM   13364 C CB  . GLN K  1 80  ? -35.518 -44.972  13.920  1.000 46.047  0 409 GLN KKK CB  1 ? 43 
ATOM   13365 C CG  . GLN K  1 80  ? -35.798 -44.819  15.408  1.000 47.106  0 409 GLN KKK CG  1 ? 43 
ATOM   13366 C CD  . GLN K  1 80  ? -37.262 -44.548  15.692  1.000 47.857  0 409 GLN KKK CD  1 ? 43 
ATOM   13367 O OE1 . GLN K  1 80  ? -38.165 -45.232  15.197  1.000 48.187  0 409 GLN KKK OE1 1 ? 43 
ATOM   13368 N NE2 . GLN K  1 80  ? -37.534 -43.520  16.480  1.000 47.247  0 409 GLN KKK NE2 1 ? 43 
ATOM   13369 N N   . ILE K  1 81  ? -33.416 -45.171  11.242  1.000 41.010  0 410 ILE KKK N   1 ? 43 
ATOM   13370 C CA  . ILE K  1 81  ? -33.289 -45.651  9.840   1.000 41.610  0 410 ILE KKK CA  1 ? 43 
ATOM   13371 C C   . ILE K  1 81  ? -32.023 -46.497  9.744   1.000 41.745  0 410 ILE KKK C   1 ? 43 
ATOM   13372 O O   . ILE K  1 81  ? -31.020 -46.051  9.186   1.000 39.721  0 410 ILE KKK O   1 ? 43 
ATOM   13373 C CB  . ILE K  1 81  ? -33.334 -44.494  8.837   1.000 42.631  0 410 ILE KKK CB  1 ? 43 
ATOM   13374 C CG1 . ILE K  1 81  ? -34.460 -43.518  9.172   1.000 41.693  0 410 ILE KKK CG1 1 ? 43 
ATOM   13375 C CG2 . ILE K  1 81  ? -33.460 -45.036  7.419   1.000 42.318  0 410 ILE KKK CG2 1 ? 43 
ATOM   13376 C CD1 . ILE K  1 81  ? -35.808 -44.172  9.279   1.000 40.012  0 410 ILE KKK CD1 1 ? 43 
ATOM   13377 N N   . ALA K  1 82  ? -32.095 -47.692  10.308  1.000 43.719  0 411 ALA KKK N   1 ? 43 
ATOM   13378 C CA  . ALA K  1 82  ? -30.952 -48.624  10.423  1.000 44.759  0 411 ALA KKK CA  1 ? 43 
ATOM   13379 C C   . ALA K  1 82  ? -31.485 -50.004  10.755  1.000 44.606  0 411 ALA KKK C   1 ? 43 
ATOM   13380 O O   . ALA K  1 82  ? -32.474 -50.121  11.457  1.000 47.696  0 411 ALA KKK O   1 ? 43 
ATOM   13381 C CB  . ALA K  1 82  ? -29.981 -48.136  11.485  1.000 43.506  0 411 ALA KKK CB  1 ? 43 
ATOM   13382 N N   . PRO K  1 83  ? -30.836 -51.082  10.291  1.000 45.074  0 412 PRO KKK N   1 ? 43 
ATOM   13383 C CA  . PRO K  1 83  ? -31.237 -52.430  10.694  1.000 45.088  0 412 PRO KKK CA  1 ? 43 
ATOM   13384 C C   . PRO K  1 83  ? -31.175 -52.562  12.224  1.000 45.566  0 412 PRO KKK C   1 ? 43 
ATOM   13385 O O   . PRO K  1 83  ? -30.238 -52.063  12.810  1.000 45.748  0 412 PRO KKK O   1 ? 43 
ATOM   13386 C CB  . PRO K  1 83  ? -30.192 -53.343  10.034  1.000 47.180  0 412 PRO KKK CB  1 ? 43 
ATOM   13387 C CG  . PRO K  1 83  ? -29.032 -52.390  9.743   1.000 46.324  0 412 PRO KKK CG  1 ? 43 
ATOM   13388 C CD  . PRO K  1 83  ? -29.673 -51.067  9.389   1.000 44.973  0 412 PRO KKK CD  1 ? 43 
ATOM   13389 N N   . GLY K  1 84  ? -32.170 -53.216  12.830  1.000 45.964  0 413 GLY KKK N   1 ? 43 
ATOM   13390 C CA  . GLY K  1 84  ? -32.138 -53.621  14.247  1.000 45.394  0 413 GLY KKK CA  1 ? 43 
ATOM   13391 C C   . GLY K  1 84  ? -32.672 -52.547  15.164  1.000 45.791  0 413 GLY KKK C   1 ? 43 
ATOM   13392 O O   . GLY K  1 84  ? -32.598 -52.760  16.371  1.000 52.122  0 413 GLY KKK O   1 ? 43 
ATOM   13393 N N   . GLN K  1 85  ? -33.248 -51.462  14.633  1.000 45.264  0 414 GLN KKK N   1 ? 43 
ATOM   13394 C CA  . GLN K  1 85  ? -33.812 -50.328  15.411  1.000 44.452  0 414 GLN KKK CA  1 ? 43 
ATOM   13395 C C   . GLN K  1 85  ? -35.274 -50.590  15.778  1.000 45.474  0 414 GLN KKK C   1 ? 43 
ATOM   13396 O O   . GLN K  1 85  ? -35.960 -51.299  15.027  1.000 47.975  0 414 GLN KKK O   1 ? 43 
ATOM   13397 C CB  . GLN K  1 85  ? -33.690 -49.048  14.596  1.000 42.792  0 414 GLN KKK CB  1 ? 43 
ATOM   13398 C CG  . GLN K  1 85  ? -32.242 -48.581  14.495  1.000 43.544  0 414 GLN KKK CG  1 ? 43 
ATOM   13399 C CD  . GLN K  1 85  ? -31.708 -48.154  15.842  1.000 44.048  0 414 GLN KKK CD  1 ? 43 
ATOM   13400 O OE1 . GLN K  1 85  ? -32.407 -47.560  16.646  1.000 46.684  0 414 GLN KKK OE1 1 ? 43 
ATOM   13401 N NE2 . GLN K  1 85  ? -30.449 -48.444  16.106  1.000 44.845  0 414 GLN KKK NE2 1 ? 43 
ATOM   13402 N N   . THR K  1 86  ? -35.727 -50.019  16.889  1.000 45.851  0 415 THR KKK N   1 ? 43 
ATOM   13403 C CA  . THR K  1 86  ? -37.162 -49.908  17.250  1.000 46.032  0 415 THR KKK CA  1 ? 43 
ATOM   13404 C C   . THR K  1 86  ? -37.503 -48.449  17.554  1.000 45.279  0 415 THR KKK C   1 ? 43 
ATOM   13405 O O   . THR K  1 86  ? -36.560 -47.628  17.693  1.000 46.892  0 415 THR KKK O   1 ? 43 
ATOM   13406 C CB  . THR K  1 86  ? -37.546 -50.809  18.423  1.000 47.467  0 415 THR KKK CB  1 ? 43 
ATOM   13407 O OG1 . THR K  1 86  ? -36.679 -50.474  19.497  1.000 46.318  0 415 THR KKK OG1 1 ? 43 
ATOM   13408 C CG2 . THR K  1 86  ? -37.428 -52.278  18.085  1.000 49.045  0 415 THR KKK CG2 1 ? 43 
ATOM   13409 N N   . GLY K  1 87  ? -38.805 -48.161  17.602  1.000 42.913  0 416 GLY KKK N   1 ? 43 
ATOM   13410 C CA  . GLY K  1 87  ? -39.386 -46.817  17.734  1.000 43.197  0 416 GLY KKK CA  1 ? 43 
ATOM   13411 C C   . GLY K  1 87  ? -40.525 -46.644  16.749  1.000 43.909  0 416 GLY KKK C   1 ? 43 
ATOM   13412 O O   . GLY K  1 87  ? -40.727 -47.530  15.910  1.000 42.660  0 416 GLY KKK O   1 ? 43 
ATOM   13413 N N   . LYS K  1 88  ? -41.262 -45.545  16.866  1.000 46.517  0 417 LYS KKK N   1 ? 43 
ATOM   13414 C CA  . LYS K  1 88  ? -42.437 -45.219  16.023  1.000 46.611  0 417 LYS KKK CA  1 ? 43 
ATOM   13415 C C   . LYS K  1 88  ? -42.024 -45.406  14.569  1.000 43.030  0 417 LYS KKK C   1 ? 43 
ATOM   13416 O O   . LYS K  1 88  ? -42.786 -45.998  13.840  1.000 43.580  0 417 LYS KKK O   1 ? 43 
ATOM   13417 C CB  . LYS K  1 88  ? -42.931 -43.777  16.231  1.000 50.274  0 417 LYS KKK CB  1 ? 43 
ATOM   13418 C CG  . LYS K  1 88  ? -43.434 -43.441  17.630  1.000 55.658  0 417 LYS KKK CG  1 ? 43 
ATOM   13419 C CD  . LYS K  1 88  ? -44.467 -44.395  18.183  1.000 58.868  0 417 LYS KKK CD  1 ? 43 
ATOM   13420 C CE  . LYS K  1 88  ? -43.931 -45.429  19.144  1.000 60.452  0 417 LYS KKK CE  1 ? 43 
ATOM   13421 N NZ  . LYS K  1 88  ? -45.055 -46.157  19.756  1.000 60.839  0 417 LYS KKK NZ  1 ? 43 
ATOM   13422 N N   . ILE K  1 89  ? -40.856 -44.912  14.165  1.000 40.245  0 418 ILE KKK N   1 ? 43 
ATOM   13423 C CA  . ILE K  1 89  ? -40.481 -44.850  12.726  1.000 41.093  0 418 ILE KKK CA  1 ? 43 
ATOM   13424 C C   . ILE K  1 89  ? -40.089 -46.259  12.243  1.000 40.924  0 418 ILE KKK C   1 ? 43 
ATOM   13425 O O   . ILE K  1 89  ? -40.717 -46.748  11.290  1.000 39.293  0 418 ILE KKK O   1 ? 43 
ATOM   13426 C CB  . ILE K  1 89  ? -39.408 -43.780  12.453  1.000 41.492  0 418 ILE KKK CB  1 ? 43 
ATOM   13427 C CG1 . ILE K  1 89  ? -39.804 -42.411  13.017  1.000 42.347  0 418 ILE KKK CG1 1 ? 43 
ATOM   13428 C CG2 . ILE K  1 89  ? -39.134 -43.694  10.962  1.000 40.143  0 418 ILE KKK CG2 1 ? 43 
ATOM   13429 C CD1 . ILE K  1 89  ? -41.178 -41.929  12.520  1.000 45.039  0 418 ILE KKK CD1 1 ? 43 
ATOM   13430 N N   . ALA K  1 90  ? -39.134 -46.909  12.903  1.000 41.669  0 419 ALA KKK N   1 ? 43 
ATOM   13431 C CA  . ALA K  1 90  ? -38.687 -48.276  12.555  1.000 43.820  0 419 ALA KKK CA  1 ? 43 
ATOM   13432 C C   . ALA K  1 90  ? -39.876 -49.249  12.585  1.000 45.485  0 419 ALA KKK C   1 ? 43 
ATOM   13433 O O   . ALA K  1 90  ? -39.939 -50.127  11.724  1.000 47.162  0 419 ALA KKK O   1 ? 43 
ATOM   13434 C CB  . ALA K  1 90  ? -37.596 -48.718  13.495  1.000 42.173  0 419 ALA KKK CB  1 ? 43 
ATOM   13435 N N   . ASP K  1 91  ? -40.791 -49.109  13.546  1.000 46.047  0 420 ASP KKK N   1 ? 43 
ATOM   13436 C CA  . ASP K  1 91  ? -41.855 -50.116  13.788  1.000 47.433  0 420 ASP KKK CA  1 ? 43 
ATOM   13437 C C   . ASP K  1 91  ? -43.044 -49.850  12.858  1.000 47.049  0 420 ASP KKK C   1 ? 43 
ATOM   13438 O O   . ASP K  1 91  ? -43.622 -50.836  12.408  1.000 49.617  0 420 ASP KKK O   1 ? 43 
ATOM   13439 C CB  . ASP K  1 91  ? -42.323 -50.116  15.245  1.000 51.240  0 420 ASP KKK CB  1 ? 43 
ATOM   13440 C CG  . ASP K  1 91  ? -41.288 -50.505  16.274  1.000 52.469  0 420 ASP KKK CG  1 ? 43 
ATOM   13441 O OD1 . ASP K  1 91  ? -40.240 -51.084  15.847  1.000 49.255  0 420 ASP KKK OD1 1 ? 43 
ATOM   13442 O OD2 . ASP K  1 91  ? -41.547 -50.208  17.500  1.000 52.970  0 420 ASP KKK OD2 1 ? 43 
ATOM   13443 N N   . TYR K  1 92  ? -43.431 -48.597  12.618  1.000 44.313  0 421 TYR KKK N   1 ? 43 
ATOM   13444 C CA  . TYR K  1 92  ? -44.772 -48.236  12.090  1.000 44.454  0 421 TYR KKK CA  1 ? 43 
ATOM   13445 C C   . TYR K  1 92  ? -44.704 -47.474  10.756  1.000 43.807  0 421 TYR KKK C   1 ? 43 
ATOM   13446 O O   . TYR K  1 92  ? -45.760 -47.296  10.120  1.000 45.785  0 421 TYR KKK O   1 ? 43 
ATOM   13447 C CB  . TYR K  1 92  ? -45.540 -47.403  13.116  1.000 45.298  0 421 TYR KKK CB  1 ? 43 
ATOM   13448 C CG  . TYR K  1 92  ? -45.890 -48.071  14.424  1.000 46.285  0 421 TYR KKK CG  1 ? 43 
ATOM   13449 C CD1 . TYR K  1 92  ? -45.879 -49.445  14.601  1.000 45.915  0 421 TYR KKK CD1 1 ? 43 
ATOM   13450 C CD2 . TYR K  1 92  ? -46.343 -47.292  15.482  1.000 48.615  0 421 TYR KKK CD2 1 ? 43 
ATOM   13451 C CE1 . TYR K  1 92  ? -46.267 -50.018  15.806  1.000 47.823  0 421 TYR KKK CE1 1 ? 43 
ATOM   13452 C CE2 . TYR K  1 92  ? -46.731 -47.851  16.695  1.000 49.121  0 421 TYR KKK CE2 1 ? 43 
ATOM   13453 C CZ  . TYR K  1 92  ? -46.708 -49.220  16.855  1.000 49.734  0 421 TYR KKK CZ  1 ? 43 
ATOM   13454 O OH  . TYR K  1 92  ? -47.151 -49.752  18.038  1.000 50.697  0 421 TYR KKK OH  1 ? 43 
ATOM   13455 N N   . ASN K  1 93  ? -43.525 -47.053  10.299  1.000 43.945  0 422 ASN KKK N   1 ? 43 
ATOM   13456 C CA  . ASN K  1 93  ? -43.406 -46.139  9.134   1.000 43.984  0 422 ASN KKK CA  1 ? 43 
ATOM   13457 C C   . ASN K  1 93  ? -42.469 -46.717  8.071   1.000 44.527  0 422 ASN KKK C   1 ? 43 
ATOM   13458 O O   . ASN K  1 93  ? -42.923 -46.865  6.899   1.000 44.024  0 422 ASN KKK O   1 ? 43 
ATOM   13459 C CB  . ASN K  1 93  ? -42.965 -44.754  9.585   1.000 43.904  0 422 ASN KKK CB  1 ? 43 
ATOM   13460 C CG  . ASN K  1 93  ? -44.063 -44.042  10.345  1.000 44.069  0 422 ASN KKK CG  1 ? 43 
ATOM   13461 O OD1 . ASN K  1 93  ? -44.866 -43.315  9.744   1.000 41.748  0 422 ASN KKK OD1 1 ? 43 
ATOM   13462 N ND2 . ASN K  1 93  ? -44.130 -44.284  11.648  1.000 43.585  0 422 ASN KKK ND2 1 ? 43 
ATOM   13463 N N   . TYR K  1 94  ? -41.219 -47.005  8.446   1.000 43.198  0 423 TYR KKK N   1 ? 43 
ATOM   13464 C CA  . TYR K  1 94  ? -40.182 -47.488  7.505   1.000 43.638  0 423 TYR KKK CA  1 ? 43 
ATOM   13465 C C   . TYR K  1 94  ? -39.233 -48.432  8.238   1.000 43.105  0 423 TYR KKK C   1 ? 43 
ATOM   13466 O O   . TYR K  1 94  ? -38.501 -47.985  9.161   1.000 45.205  0 423 TYR KKK O   1 ? 43 
ATOM   13467 C CB  . TYR K  1 94  ? -39.428 -46.314  6.882   1.000 42.634  0 423 TYR KKK CB  1 ? 43 
ATOM   13468 C CG  . TYR K  1 94  ? -38.455 -46.714  5.806   1.000 41.632  0 423 TYR KKK CG  1 ? 43 
ATOM   13469 C CD1 . TYR K  1 94  ? -38.864 -46.876  4.496   1.000 41.349  0 423 TYR KKK CD1 1 ? 43 
ATOM   13470 C CD2 . TYR K  1 94  ? -37.124 -46.967  6.112   1.000 41.572  0 423 TYR KKK CD2 1 ? 43 
ATOM   13471 C CE1 . TYR K  1 94  ? -37.966 -47.244  3.501   1.000 40.774  0 423 TYR KKK CE1 1 ? 43 
ATOM   13472 C CE2 . TYR K  1 94  ? -36.214 -47.338  5.132   1.000 41.523  0 423 TYR KKK CE2 1 ? 43 
ATOM   13473 C CZ  . TYR K  1 94  ? -36.636 -47.477  3.823   1.000 40.356  0 423 TYR KKK CZ  1 ? 43 
ATOM   13474 O OH  . TYR K  1 94  ? -35.725 -47.866  2.883   1.000 39.476  0 423 TYR KKK OH  1 ? 43 
ATOM   13475 N N   . LYS K  1 95  ? -39.238 -49.694  7.819   1.000 44.485  0 424 LYS KKK N   1 ? 43 
ATOM   13476 C CA  . LYS K  1 95  ? -38.492 -50.788  8.487   1.000 46.684  0 424 LYS KKK CA  1 ? 43 
ATOM   13477 C C   . LYS K  1 95  ? -37.418 -51.322  7.542   1.000 46.727  0 424 LYS KKK C   1 ? 43 
ATOM   13478 O O   . LYS K  1 95  ? -37.764 -51.778  6.436   1.000 54.903  0 424 LYS KKK O   1 ? 43 
ATOM   13479 C CB  . LYS K  1 95  ? -39.449 -51.910  8.889   1.000 49.585  0 424 LYS KKK CB  1 ? 43 
ATOM   13480 C CG  . LYS K  1 95  ? -38.792 -53.121  9.557   1.000 52.933  0 424 LYS KKK CG  1 ? 43 
ATOM   13481 C CD  . LYS K  1 95  ? -39.021 -53.329  11.071  1.000 57.014  0 424 LYS KKK CD  1 ? 43 
ATOM   13482 C CE  . LYS K  1 95  ? -37.742 -53.702  11.809  1.000 63.101  0 424 LYS KKK CE  1 ? 43 
ATOM   13483 N NZ  . LYS K  1 95  ? -37.564 -52.935  13.066  1.000 65.916  0 424 LYS KKK NZ  1 ? 43 
ATOM   13484 N N   . LEU K  1 96  ? -36.162 -51.267  7.963   1.000 44.418  0 425 LEU KKK N   1 ? 43 
ATOM   13485 C CA  . LEU K  1 96  ? -35.048 -51.927  7.237   1.000 43.095  0 425 LEU KKK CA  1 ? 43 
ATOM   13486 C C   . LEU K  1 96  ? -34.929 -53.349  7.771   1.000 44.763  0 425 LEU KKK C   1 ? 43 
ATOM   13487 O O   . LEU K  1 96  ? -35.113 -53.587  8.970   1.000 41.447  0 425 LEU KKK O   1 ? 43 
ATOM   13488 C CB  . LEU K  1 96  ? -33.738 -51.171  7.411   1.000 41.369  0 425 LEU KKK CB  1 ? 43 
ATOM   13489 C CG  . LEU K  1 96  ? -33.651 -49.844  6.668   1.000 40.753  0 425 LEU KKK CG  1 ? 43 
ATOM   13490 C CD1 . LEU K  1 96  ? -32.352 -49.095  6.904   1.000 42.690  0 425 LEU KKK CD1 1 ? 43 
ATOM   13491 C CD2 . LEU K  1 96  ? -33.818 -50.057  5.196   1.000 41.921  0 425 LEU KKK CD2 1 ? 43 
ATOM   13492 N N   . PRO K  1 97  ? -34.610 -54.321  6.882   1.000 46.221  0 426 PRO KKK N   1 ? 43 
ATOM   13493 C CA  . PRO K  1 97  ? -34.378 -55.708  7.289   1.000 46.602  0 426 PRO KKK CA  1 ? 43 
ATOM   13494 C C   . PRO K  1 97  ? -33.097 -55.820  8.118   1.000 49.100  0 426 PRO KKK C   1 ? 43 
ATOM   13495 O O   . PRO K  1 97  ? -32.250 -54.949  8.017   1.000 53.415  0 426 PRO KKK O   1 ? 43 
ATOM   13496 C CB  . PRO K  1 97  ? -34.211 -56.460  5.959   1.000 47.601  0 426 PRO KKK CB  1 ? 43 
ATOM   13497 C CG  . PRO K  1 97  ? -33.708 -55.382  4.992   1.000 47.587  0 426 PRO KKK CG  1 ? 43 
ATOM   13498 C CD  . PRO K  1 97  ? -34.403 -54.102  5.434   1.000 45.778  0 426 PRO KKK CD  1 ? 43 
ATOM   13499 N N   . ASP K  1 98  ? -32.954 -56.879  8.909   1.000 51.554  0 427 ASP KKK N   1 ? 43 
ATOM   13500 C CA  . ASP K  1 98  ? -31.758 -57.070  9.760   1.000 54.540  0 427 ASP KKK CA  1 ? 43 
ATOM   13501 C C   . ASP K  1 98  ? -30.499 -57.258  8.892   1.000 54.230  0 427 ASP KKK C   1 ? 43 
ATOM   13502 O O   . ASP K  1 98  ? -29.433 -56.827  9.344   1.000 54.148  0 427 ASP KKK O   1 ? 43 
ATOM   13503 C CB  . ASP K  1 98  ? -31.973 -58.215  10.741  1.000 58.227  0 427 ASP KKK CB  1 ? 43 
ATOM   13504 C CG  . ASP K  1 98  ? -31.009 -58.137  11.903  1.000 64.293  0 427 ASP KKK CG  1 ? 43 
ATOM   13505 O OD1 . ASP K  1 98  ? -30.913 -57.036  12.552  1.000 70.565  0 427 ASP KKK OD1 1 ? 43 
ATOM   13506 O OD2 . ASP K  1 98  ? -30.304 -59.134  12.096  1.000 68.846  0 427 ASP KKK OD2 1 ? 43 
ATOM   13507 N N   . ASP K  1 99  ? -30.624 -57.864  7.708   1.000 52.603  0 428 ASP KKK N   1 ? 43 
ATOM   13508 C CA  . ASP K  1 99  ? -29.487 -58.176  6.800   1.000 53.184  0 428 ASP KKK CA  1 ? 43 
ATOM   13509 C C   . ASP K  1 99  ? -29.439 -57.146  5.661   1.000 51.527  0 428 ASP KKK C   1 ? 43 
ATOM   13510 O O   . ASP K  1 99  ? -28.914 -57.456  4.582   1.000 52.318  0 428 ASP KKK O   1 ? 43 
ATOM   13511 C CB  . ASP K  1 99  ? -29.585 -59.605  6.276   1.000 55.903  0 428 ASP KKK CB  1 ? 43 
ATOM   13512 C CG  . ASP K  1 99  ? -30.778 -59.870  5.379   1.000 58.096  0 428 ASP KKK CG  1 ? 43 
ATOM   13513 O OD1 . ASP K  1 99  ? -31.627 -58.937  5.168   1.000 59.543  0 428 ASP KKK OD1 1 ? 43 
ATOM   13514 O OD2 . ASP K  1 99  ? -30.925 -61.063  4.988   1.000 62.432  0 428 ASP KKK OD2 1 ? 43 
ATOM   13515 N N   . PHE K  1 100 ? -29.959 -55.943  5.891   1.000 47.863  0 429 PHE KKK N   1 ? 43 
ATOM   13516 C CA  . PHE K  1 100 ? -29.912 -54.825  4.929   1.000 46.565  0 429 PHE KKK CA  1 ? 43 
ATOM   13517 C C   . PHE K  1 100 ? -28.499 -54.700  4.345   1.000 46.695  0 429 PHE KKK C   1 ? 43 
ATOM   13518 O O   . PHE K  1 100 ? -27.489 -54.675  5.099   1.000 45.576  0 429 PHE KKK O   1 ? 43 
ATOM   13519 C CB  . PHE K  1 100 ? -30.275 -53.518  5.631   1.000 45.977  0 429 PHE KKK CB  1 ? 43 
ATOM   13520 C CG  . PHE K  1 100 ? -30.173 -52.287  4.778   1.000 43.405  0 429 PHE KKK CG  1 ? 43 
ATOM   13521 C CD1 . PHE K  1 100 ? -30.905 -52.212  3.612   1.000 43.417  0 429 PHE KKK CD1 1 ? 43 
ATOM   13522 C CD2 . PHE K  1 100 ? -29.396 -51.201  5.161   1.000 43.263  0 429 PHE KKK CD2 1 ? 43 
ATOM   13523 C CE1 . PHE K  1 100 ? -30.852 -51.073  2.823   1.000 43.743  0 429 PHE KKK CE1 1 ? 43 
ATOM   13524 C CE2 . PHE K  1 100 ? -29.336 -50.066  4.356   1.000 44.403  0 429 PHE KKK CE2 1 ? 43 
ATOM   13525 C CZ  . PHE K  1 100 ? -30.077 -50.003  3.189   1.000 43.132  0 429 PHE KKK CZ  1 ? 43 
ATOM   13526 N N   . THR K  1 101 ? -28.430 -54.569  3.020   1.000 46.155  0 430 THR KKK N   1 ? 43 
ATOM   13527 C CA  . THR K  1 101 ? -27.209 -54.160  2.291   1.000 47.003  0 430 THR KKK CA  1 ? 43 
ATOM   13528 C C   . THR K  1 101 ? -27.509 -52.830  1.614   1.000 45.367  0 430 THR KKK C   1 ? 43 
ATOM   13529 O O   . THR K  1 101 ? -28.390 -52.808  0.726   1.000 45.258  0 430 THR KKK O   1 ? 43 
ATOM   13530 C CB  . THR K  1 101 ? -26.772 -55.225  1.281   1.000 49.236  0 430 THR KKK CB  1 ? 43 
ATOM   13531 O OG1 . THR K  1 101 ? -26.568 -56.433  2.017   1.000 50.235  0 430 THR KKK OG1 1 ? 43 
ATOM   13532 C CG2 . THR K  1 101 ? -25.501 -54.855  0.541   1.000 49.268  0 430 THR KKK CG2 1 ? 43 
ATOM   13533 N N   . GLY K  1 102 ? -26.798 -51.772  2.003   1.000 45.479  0 431 GLY KKK N   1 ? 43 
ATOM   13534 C CA  . GLY K  1 102 ? -27.014 -50.437  1.411   1.000 44.599  0 431 GLY KKK CA  1 ? 43 
ATOM   13535 C C   . GLY K  1 102 ? -26.522 -49.331  2.315   1.000 43.866  0 431 GLY KKK C   1 ? 43 
ATOM   13536 O O   . GLY K  1 102 ? -25.767 -49.614  3.268   1.000 44.039  0 431 GLY KKK O   1 ? 43 
ATOM   13537 N N   . CYS K  1 103 ? -26.918 -48.098  2.019   1.000 44.795  0 432 CYS KKK N   1 ? 43 
ATOM   13538 C CA  . CYS K  1 103 ? -26.443 -46.898  2.745   1.000 42.485  0 432 CYS KKK CA  1 ? 43 
ATOM   13539 C C   . CYS K  1 103 ? -27.635 -46.010  3.085   1.000 40.827  0 432 CYS KKK C   1 ? 43 
ATOM   13540 O O   . CYS K  1 103 ? -28.632 -45.996  2.370   1.000 43.837  0 432 CYS KKK O   1 ? 43 
ATOM   13541 C CB  . CYS K  1 103 ? -25.412 -46.104  1.962   1.000 44.612  0 432 CYS KKK CB  1 ? 43 
ATOM   13542 S SG  . CYS K  1 103 ? -24.051 -47.116  1.355   1.000 48.501  0 432 CYS KKK SG  1 ? 43 
ATOM   13543 N N   . VAL K  1 104 ? -27.512 -45.304  4.189   1.000 40.450  0 433 VAL KKK N   1 ? 43 
ATOM   13544 C CA  . VAL K  1 104 ? -28.530 -44.374  4.738   1.000 40.663  0 433 VAL KKK CA  1 ? 43 
ATOM   13545 C C   . VAL K  1 104 ? -27.855 -43.008  4.845   1.000 41.483  0 433 VAL KKK C   1 ? 43 
ATOM   13546 O O   . VAL K  1 104 ? -26.794 -42.909  5.499   1.000 40.500  0 433 VAL KKK O   1 ? 43 
ATOM   13547 C CB  . VAL K  1 104 ? -29.020 -44.884  6.101   1.000 39.042  0 433 VAL KKK CB  1 ? 43 
ATOM   13548 C CG1 . VAL K  1 104 ? -29.956 -43.881  6.736   1.000 38.631  0 433 VAL KKK CG1 1 ? 43 
ATOM   13549 C CG2 . VAL K  1 104 ? -29.643 -46.276  5.983   1.000 40.776  0 433 VAL KKK CG2 1 ? 43 
ATOM   13550 N N   . ILE K  1 105 ? -28.422 -42.027  4.151   1.000 41.178  0 434 ILE KKK N   1 ? 43 
ATOM   13551 C CA  . ILE K  1 105 ? -27.895 -40.633  4.102   1.000 44.085  0 434 ILE KKK CA  1 ? 43 
ATOM   13552 C C   . ILE K  1 105 ? -29.027 -39.710  4.548   1.000 42.402  0 434 ILE KKK C   1 ? 43 
ATOM   13553 O O   . ILE K  1 105 ? -30.176 -39.936  4.137   1.000 41.984  0 434 ILE KKK O   1 ? 43 
ATOM   13554 C CB  . ILE K  1 105 ? -27.352 -40.279  2.702   1.000 45.207  0 434 ILE KKK CB  1 ? 43 
ATOM   13555 C CG1 . ILE K  1 105 ? -26.236 -41.252  2.303   1.000 47.367  0 434 ILE KKK CG1 1 ? 43 
ATOM   13556 C CG2 . ILE K  1 105 ? -26.905 -38.817  2.655   1.000 43.229  0 434 ILE KKK CG2 1 ? 43 
ATOM   13557 C CD1 . ILE K  1 105 ? -25.844 -41.195  0.859   1.000 52.118  0 434 ILE KKK CD1 1 ? 43 
ATOM   13558 N N   . ALA K  1 106 ? -28.708 -38.734  5.377   1.000 40.678  0 435 ALA KKK N   1 ? 43 
ATOM   13559 C CA  . ALA K  1 106 ? -29.677 -37.737  5.866   1.000 41.830  0 435 ALA KKK CA  1 ? 43 
ATOM   13560 C C   . ALA K  1 106 ? -28.979 -36.388  5.929   1.000 40.794  0 435 ALA KKK C   1 ? 43 
ATOM   13561 O O   . ALA K  1 106 ? -27.713 -36.345  5.985   1.000 42.590  0 435 ALA KKK O   1 ? 43 
ATOM   13562 C CB  . ALA K  1 106 ? -30.287 -38.140  7.207   1.000 41.320  0 435 ALA KKK CB  1 ? 43 
ATOM   13563 N N   . TRP K  1 107 ? -29.798 -35.336  5.889   1.000 40.078  0 436 TRP KKK N   1 ? 43 
ATOM   13564 C CA  . TRP K  1 107 ? -29.344 -33.939  6.091   1.000 40.331  0 436 TRP KKK CA  1 ? 43 
ATOM   13565 C C   . TRP K  1 107 ? -30.480 -33.124  6.692   1.000 39.861  0 436 TRP KKK C   1 ? 43 
ATOM   13566 O O   . TRP K  1 107 ? -31.644 -33.442  6.430   1.000 42.280  0 436 TRP KKK O   1 ? 43 
ATOM   13567 C CB  . TRP K  1 107 ? -28.790 -33.353  4.786   1.000 39.522  0 436 TRP KKK CB  1 ? 43 
ATOM   13568 C CG  . TRP K  1 107 ? -29.804 -33.192  3.703   1.000 39.663  0 436 TRP KKK CG  1 ? 43 
ATOM   13569 C CD1 . TRP K  1 107 ? -30.500 -32.062  3.399   1.000 40.301  0 436 TRP KKK CD1 1 ? 43 
ATOM   13570 C CD2 . TRP K  1 107 ? -30.229 -34.191  2.760   1.000 38.286  0 436 TRP KKK CD2 1 ? 43 
ATOM   13571 N NE1 . TRP K  1 107 ? -31.320 -32.290  2.328   1.000 39.706  0 436 TRP KKK NE1 1 ? 43 
ATOM   13572 C CE2 . TRP K  1 107 ? -31.177 -33.583  1.912   1.000 39.294  0 436 TRP KKK CE2 1 ? 43 
ATOM   13573 C CE3 . TRP K  1 107 ? -29.915 -35.536  2.549   1.000 39.098  0 436 TRP KKK CE3 1 ? 43 
ATOM   13574 C CZ2 . TRP K  1 107 ? -31.803 -34.263  0.869   1.000 39.401  0 436 TRP KKK CZ2 1 ? 43 
ATOM   13575 C CZ3 . TRP K  1 107 ? -30.538 -36.222  1.533   1.000 39.455  0 436 TRP KKK CZ3 1 ? 43 
ATOM   13576 C CH2 . TRP K  1 107 ? -31.450 -35.581  0.692   1.000 40.146  0 436 TRP KKK CH2 1 ? 43 
ATOM   13577 N N   . ASN K  1 108 ? -30.114 -32.159  7.521   1.000 39.478  0 437 ASN KKK N   1 ? 43 
ATOM   13578 C CA  . ASN K  1 108 ? -31.031 -31.150  8.093   1.000 39.973  0 437 ASN KKK CA  1 ? 43 
ATOM   13579 C C   . ASN K  1 108 ? -31.690 -30.389  6.934   1.000 39.877  0 437 ASN KKK C   1 ? 43 
ATOM   13580 O O   . ASN K  1 108 ? -30.963 -29.903  6.056   1.000 39.198  0 437 ASN KKK O   1 ? 43 
ATOM   13581 C CB  . ASN K  1 108 ? -30.242 -30.221  9.011   1.000 40.851  0 437 ASN KKK CB  1 ? 43 
ATOM   13582 C CG  . ASN K  1 108 ? -31.161 -29.266  9.721   1.000 42.990  0 437 ASN KKK CG  1 ? 43 
ATOM   13583 O OD1 . ASN K  1 108 ? -31.747 -28.378  9.072   1.000 44.744  0 437 ASN KKK OD1 1 ? 43 
ATOM   13584 N ND2 . ASN K  1 108 ? -31.339 -29.484  11.017  1.000 44.487  0 437 ASN KKK ND2 1 ? 43 
ATOM   13585 N N   . SER K  1 109 ? -33.015 -30.314  6.918   1.000 40.340  0 438 SER KKK N   1 ? 43 
ATOM   13586 C CA  . SER K  1 109 ? -33.798 -29.609  5.873   1.000 41.342  0 438 SER KKK CA  1 ? 43 
ATOM   13587 C C   . SER K  1 109 ? -34.658 -28.527  6.533   1.000 41.950  0 438 SER KKK C   1 ? 43 
ATOM   13588 O O   . SER K  1 109 ? -35.706 -28.170  5.974   1.000 43.430  0 438 SER KKK O   1 ? 43 
ATOM   13589 C CB  . SER K  1 109 ? -34.630 -30.577  5.062   1.000 40.864  0 438 SER KKK CB  1 ? 43 
ATOM   13590 O OG  . SER K  1 109 ? -35.531 -31.270  5.914   1.000 41.597  0 438 SER KKK OG  1 ? 43 
ATOM   13591 N N   . ASN K  1 110 ? -34.221 -28.008  7.668   1.000 40.802  0 439 ASN KKK N   1 ? 43 
ATOM   13592 C CA  . ASN K  1 110 ? -34.965 -26.941  8.382   1.000 43.905  0 439 ASN KKK CA  1 ? 43 
ATOM   13593 C C   . ASN K  1 110 ? -35.256 -25.783  7.407   1.000 44.651  0 439 ASN KKK C   1 ? 43 
ATOM   13594 O O   . ASN K  1 110 ? -36.387 -25.280  7.401   1.000 45.376  0 439 ASN KKK O   1 ? 43 
ATOM   13595 C CB  . ASN K  1 110 ? -34.210 -26.468  9.634   1.000 44.866  0 439 ASN KKK CB  1 ? 43 
ATOM   13596 C CG  . ASN K  1 110 ? -35.120 -25.800  10.638  1.000 46.495  0 439 ASN KKK CG  1 ? 43 
ATOM   13597 O OD1 . ASN K  1 110 ? -36.303 -26.118  10.768  1.000 47.856  0 439 ASN KKK OD1 1 ? 43 
ATOM   13598 N ND2 . ASN K  1 110 ? -34.559 -24.871  11.379  1.000 48.214  0 439 ASN KKK ND2 1 ? 43 
ATOM   13599 N N   . ASN K  1 111 ? -34.276 -25.420  6.576   1.000 44.058  0 440 ASN KKK N   1 ? 43 
ATOM   13600 C CA  . ASN K  1 111 ? -34.355 -24.291  5.615   1.000 46.502  0 440 ASN KKK CA  1 ? 43 
ATOM   13601 C C   . ASN K  1 111 ? -35.459 -24.520  4.569   1.000 50.527  0 440 ASN KKK C   1 ? 43 
ATOM   13602 O O   . ASN K  1 111 ? -35.988 -23.537  4.073   1.000 56.196  0 440 ASN KKK O   1 ? 43 
ATOM   13603 C CB  . ASN K  1 111 ? -33.000 -24.020  4.955   1.000 44.006  0 440 ASN KKK CB  1 ? 43 
ATOM   13604 C CG  . ASN K  1 111 ? -32.034 -23.264  5.847   1.000 45.259  0 440 ASN KKK CG  1 ? 43 
ATOM   13605 O OD1 . ASN K  1 111 ? -32.414 -22.636  6.837   1.000 44.739  0 440 ASN KKK OD1 1 ? 43 
ATOM   13606 N ND2 . ASN K  1 111 ? -30.760 -23.305  5.503   1.000 45.915  0 440 ASN KKK ND2 1 ? 43 
ATOM   13607 N N   . LEU K  1 112 ? -35.792 -25.757  4.225   1.000 53.747  0 441 LEU KKK N   1 ? 43 
ATOM   13608 C CA  . LEU K  1 112 ? -36.773 -26.083  3.151   1.000 56.664  0 441 LEU KKK CA  1 ? 43 
ATOM   13609 C C   . LEU K  1 112 ? -38.117 -26.477  3.781   1.000 56.767  0 441 LEU KKK C   1 ? 43 
ATOM   13610 O O   . LEU K  1 112 ? -39.145 -26.130  3.194   1.000 56.863  0 441 LEU KKK O   1 ? 43 
ATOM   13611 C CB  . LEU K  1 112 ? -36.281 -27.251  2.293   1.000 61.758  0 441 LEU KKK CB  1 ? 43 
ATOM   13612 C CG  . LEU K  1 112 ? -34.954 -27.074  1.569   1.000 67.819  0 441 LEU KKK CG  1 ? 43 
ATOM   13613 C CD1 . LEU K  1 112 ? -34.529 -28.387  0.919   1.000 68.205  0 441 LEU KKK CD1 1 ? 43 
ATOM   13614 C CD2 . LEU K  1 112 ? -35.091 -25.950  0.562   1.000 71.032  0 441 LEU KKK CD2 1 ? 43 
ATOM   13615 N N   . ASP K  1 113 ? -38.112 -27.214  4.900   1.000 54.759  0 442 ASP KKK N   1 ? 43 
ATOM   13616 C CA  . ASP K  1 113 ? -39.271 -28.029  5.349   1.000 54.302  0 442 ASP KKK CA  1 ? 43 
ATOM   13617 C C   . ASP K  1 113 ? -39.915 -27.468  6.625   1.000 57.035  0 442 ASP KKK C   1 ? 43 
ATOM   13618 O O   . ASP K  1 113 ? -40.840 -28.104  7.135   1.000 54.335  0 442 ASP KKK O   1 ? 43 
ATOM   13619 C CB  . ASP K  1 113 ? -38.839 -29.478  5.572   1.000 50.355  0 442 ASP KKK CB  1 ? 43 
ATOM   13620 C CG  . ASP K  1 113 ? -38.566 -30.243  4.288   1.000 47.386  0 442 ASP KKK CG  1 ? 43 
ATOM   13621 O OD1 . ASP K  1 113 ? -39.295 -30.001  3.307   1.000 47.866  0 442 ASP KKK OD1 1 ? 43 
ATOM   13622 O OD2 . ASP K  1 113 ? -37.633 -31.074  4.281   1.000 45.658  0 442 ASP KKK OD2 1 ? 43 
ATOM   13623 N N   . SER K  1 114 ? -39.482 -26.324  7.144   1.000 60.512  0 443 SER KKK N   1 ? 43 
ATOM   13624 C CA  . SER K  1 114 ? -40.133 -25.722  8.334   1.000 64.972  0 443 SER KKK CA  1 ? 43 
ATOM   13625 C C   . SER K  1 114 ? -40.733 -24.368  7.935   1.000 65.162  0 443 SER KKK C   1 ? 43 
ATOM   13626 O O   . SER K  1 114 ? -40.247 -23.812  6.973   1.000 65.004  0 443 SER KKK O   1 ? 43 
ATOM   13627 C CB  . SER K  1 114 ? -39.169 -25.665  9.491   1.000 66.686  0 443 SER KKK CB  1 ? 43 
ATOM   13628 O OG  . SER K  1 114 ? -38.369 -24.486  9.431   1.000 71.881  0 443 SER KKK OG  1 ? 43 
ATOM   13629 N N   . LYS K  1 115 ? -41.816 -23.930  8.569   1.000 66.328  0 444 LYS KKK N   1 ? 43 
ATOM   13630 C CA  . LYS K  1 115 ? -42.511 -22.661  8.222   1.000 72.144  0 444 LYS KKK CA  1 ? 43 
ATOM   13631 C C   . LYS K  1 115 ? -42.781 -21.892  9.511   1.000 73.104  0 444 LYS KKK C   1 ? 43 
ATOM   13632 O O   . LYS K  1 115 ? -42.918 -22.541  10.582  1.000 71.661  0 444 LYS KKK O   1 ? 43 
ATOM   13633 C CB  . LYS K  1 115 ? -43.871 -22.896  7.564   1.000 77.625  0 444 LYS KKK CB  1 ? 43 
ATOM   13634 C CG  . LYS K  1 115 ? -43.914 -23.122  6.077   1.000 82.593  0 444 LYS KKK CG  1 ? 43 
ATOM   13635 C CD  . LYS K  1 115 ? -45.297 -23.627  5.711   1.000 87.674  0 444 LYS KKK CD  1 ? 43 
ATOM   13636 C CE  . LYS K  1 115 ? -45.455 -23.942  4.239   1.000 91.113  0 444 LYS KKK CE  1 ? 43 
ATOM   13637 N NZ  . LYS K  1 115 ? -44.813 -25.228  3.852   1.000 90.760  0 444 LYS KKK NZ  1 ? 43 
ATOM   13638 N N   . VAL K  1 116 ? -42.883 -20.564  9.406   1.000 75.666  0 445 VAL KKK N   1 ? 43 
ATOM   13639 C CA  . VAL K  1 116 ? -43.383 -19.706  10.516  1.000 79.110  0 445 VAL KKK CA  1 ? 43 
ATOM   13640 C C   . VAL K  1 116 ? -44.819 -20.178  10.807  1.000 76.133  0 445 VAL KKK C   1 ? 43 
ATOM   13641 O O   . VAL K  1 116 ? -45.601 -20.365  9.851   1.000 75.630  0 445 VAL KKK O   1 ? 43 
ATOM   13642 C CB  . VAL K  1 116 ? -43.264 -18.198  10.198  1.000 84.332  0 445 VAL KKK CB  1 ? 43 
ATOM   13643 C CG1 . VAL K  1 116 ? -41.812 -17.777  10.067  1.000 83.984  0 445 VAL KKK CG1 1 ? 43 
ATOM   13644 C CG2 . VAL K  1 116 ? -44.029 -17.777  8.949   1.000 86.236  0 445 VAL KKK CG2 1 ? 43 
ATOM   13645 N N   . GLY K  1 117 ? -45.115 -20.501  12.063  1.000 73.046  0 446 GLY KKK N   1 ? 43 
ATOM   13646 C CA  . GLY K  1 117 ? -46.423 -21.044  12.468  1.000 72.332  0 446 GLY KKK CA  1 ? 43 
ATOM   13647 C C   . GLY K  1 117 ? -46.522 -22.543  12.236  1.000 70.557  0 446 GLY KKK C   1 ? 43 
ATOM   13648 O O   . GLY K  1 117 ? -47.597 -23.092  12.544  1.000 71.682  0 446 GLY KKK O   1 ? 43 
ATOM   13649 N N   . GLY K  1 118 ? -45.453 -23.179  11.743  1.000 67.961  0 447 GLY KKK N   1 ? 43 
ATOM   13650 C CA  . GLY K  1 118 ? -45.323 -24.647  11.734  1.000 64.397  0 447 GLY KKK CA  1 ? 43 
ATOM   13651 C C   . GLY K  1 118 ? -45.747 -25.254  10.412  1.000 61.984  0 447 GLY KKK C   1 ? 43 
ATOM   13652 O O   . GLY K  1 118 ? -46.814 -24.879  9.916   1.000 63.734  0 447 GLY KKK O   1 ? 43 
ATOM   13653 N N   . ASN K  1 119 ? -44.929 -26.146  9.850   1.000 58.032  0 448 ASN KKK N   1 ? 43 
ATOM   13654 C CA  . ASN K  1 119 ? -45.275 -26.955  8.656   1.000 57.697  0 448 ASN KKK CA  1 ? 43 
ATOM   13655 C C   . ASN K  1 119 ? -45.930 -28.254  9.133   1.000 56.058  0 448 ASN KKK C   1 ? 43 
ATOM   13656 O O   . ASN K  1 119 ? -45.241 -29.085  9.757   1.000 60.632  0 448 ASN KKK O   1 ? 43 
ATOM   13657 C CB  . ASN K  1 119 ? -44.057 -27.215  7.766   1.000 55.682  0 448 ASN KKK CB  1 ? 43 
ATOM   13658 C CG  . ASN K  1 119 ? -44.383 -28.018  6.532   1.000 54.146  0 448 ASN KKK CG  1 ? 43 
ATOM   13659 O OD1 . ASN K  1 119 ? -45.543 -28.229  6.205   1.000 54.960  0 448 ASN KKK OD1 1 ? 43 
ATOM   13660 N ND2 . ASN K  1 119 ? -43.363 -28.481  5.841   1.000 53.354  0 448 ASN KKK ND2 1 ? 43 
ATOM   13661 N N   . TYR K  1 120 ? -47.212 -28.421  8.840   1.000 58.583  0 449 TYR KKK N   1 ? 43 
ATOM   13662 C CA  . TYR K  1 120 ? -48.029 -29.575  9.272   1.000 60.753  0 449 TYR KKK CA  1 ? 43 
ATOM   13663 C C   . TYR K  1 120 ? -48.240 -30.521  8.081   1.000 60.353  0 449 TYR KKK C   1 ? 43 
ATOM   13664 O O   . TYR K  1 120 ? -48.946 -31.511  8.266   1.000 62.805  0 449 TYR KKK O   1 ? 43 
ATOM   13665 C CB  . TYR K  1 120 ? -49.310 -29.092  9.964   1.000 63.644  0 449 TYR KKK CB  1 ? 43 
ATOM   13666 C CG  . TYR K  1 120 ? -49.073 -28.348  11.261  1.000 67.408  0 449 TYR KKK CG  1 ? 43 
ATOM   13667 C CD1 . TYR K  1 120 ? -48.772 -29.022  12.440  1.000 67.614  0 449 TYR KKK CD1 1 ? 43 
ATOM   13668 C CD2 . TYR K  1 120 ? -49.106 -26.959  11.308  1.000 70.444  0 449 TYR KKK CD2 1 ? 43 
ATOM   13669 C CE1 . TYR K  1 120 ? -48.540 -28.348  13.631  1.000 69.508  0 449 TYR KKK CE1 1 ? 43 
ATOM   13670 C CE2 . TYR K  1 120 ? -48.860 -26.265  12.486  1.000 72.335  0 449 TYR KKK CE2 1 ? 43 
ATOM   13671 C CZ  . TYR K  1 120 ? -48.600 -26.963  13.660  1.000 72.531  0 449 TYR KKK CZ  1 ? 43 
ATOM   13672 O OH  . TYR K  1 120 ? -48.375 -26.290  14.828  1.000 73.399  0 449 TYR KKK OH  1 ? 43 
ATOM   13673 N N   . ASN K  1 121 ? -47.549 -30.320  6.956   1.000 61.484  0 450 ASN KKK N   1 ? 43 
ATOM   13674 C CA  . ASN K  1 121 ? -47.667 -31.195  5.752   1.000 61.234  0 450 ASN KKK CA  1 ? 43 
ATOM   13675 C C   . ASN K  1 121 ? -47.018 -32.565  5.983   1.000 58.158  0 450 ASN KKK C   1 ? 43 
ATOM   13676 O O   . ASN K  1 121 ? -47.509 -33.527  5.374   1.000 59.171  0 450 ASN KKK O   1 ? 43 
ATOM   13677 C CB  . ASN K  1 121 ? -47.097 -30.546  4.489   1.000 62.710  0 450 ASN KKK CB  1 ? 43 
ATOM   13678 C CG  . ASN K  1 121 ? -47.981 -29.417  4.004   1.000 69.037  0 450 ASN KKK CG  1 ? 43 
ATOM   13679 O OD1 . ASN K  1 121 ? -49.175 -29.405  4.297   1.000 72.053  0 450 ASN KKK OD1 1 ? 43 
ATOM   13680 N ND2 . ASN K  1 121 ? -47.426 -28.472  3.257   1.000 73.543  0 450 ASN KKK ND2 1 ? 43 
ATOM   13681 N N   . TYR K  1 122 ? -45.963 -32.677  6.798   1.000 55.028  0 451 TYR KKK N   1 ? 43 
ATOM   13682 C CA  . TYR K  1 122 ? -45.273 -33.973  6.988   1.000 50.630  0 451 TYR KKK CA  1 ? 43 
ATOM   13683 C C   . TYR K  1 122 ? -45.937 -34.769  8.115   1.000 50.475  0 451 TYR KKK C   1 ? 43 
ATOM   13684 O O   . TYR K  1 122 ? -46.089 -34.241  9.231   1.000 49.214  0 451 TYR KKK O   1 ? 43 
ATOM   13685 C CB  . TYR K  1 122 ? -43.783 -33.766  7.203   1.000 48.737  0 451 TYR KKK CB  1 ? 43 
ATOM   13686 C CG  . TYR K  1 122 ? -43.053 -33.282  5.984   1.000 48.513  0 451 TYR KKK CG  1 ? 43 
ATOM   13687 C CD1 . TYR K  1 122 ? -42.813 -34.118  4.898   1.000 46.329  0 451 TYR KKK CD1 1 ? 43 
ATOM   13688 C CD2 . TYR K  1 122 ? -42.577 -31.983  5.933   1.000 48.190  0 451 TYR KKK CD2 1 ? 43 
ATOM   13689 C CE1 . TYR K  1 122 ? -42.125 -33.668  3.783   1.000 47.349  0 451 TYR KKK CE1 1 ? 43 
ATOM   13690 C CE2 . TYR K  1 122 ? -41.926 -31.508  4.811   1.000 48.427  0 451 TYR KKK CE2 1 ? 43 
ATOM   13691 C CZ  . TYR K  1 122 ? -41.673 -32.361  3.747   1.000 48.210  0 451 TYR KKK CZ  1 ? 43 
ATOM   13692 O OH  . TYR K  1 122 ? -40.985 -31.877  2.674   1.000 49.074  0 451 TYR KKK OH  1 ? 43 
ATOM   13693 N N   . LEU K  1 123 ? -46.310 -36.014  7.794   1.000 49.984  0 452 LEU KKK N   1 ? 43 
ATOM   13694 C CA  . LEU K  1 123 ? -47.062 -36.928  8.680   1.000 50.274  0 452 LEU KKK CA  1 ? 43 
ATOM   13695 C C   . LEU K  1 123 ? -46.196 -38.149  9.002   1.000 48.423  0 452 LEU KKK C   1 ? 43 
ATOM   13696 O O   . LEU K  1 123 ? -45.286 -38.482  8.213   1.000 48.164  0 452 LEU KKK O   1 ? 43 
ATOM   13697 C CB  . LEU K  1 123 ? -48.354 -37.354  7.981   1.000 51.372  0 452 LEU KKK CB  1 ? 43 
ATOM   13698 C CG  . LEU K  1 123 ? -49.315 -36.234  7.556   1.000 53.013  0 452 LEU KKK CG  1 ? 43 
ATOM   13699 C CD1 . LEU K  1 123 ? -50.571 -36.805  6.918   1.000 53.949  0 452 LEU KKK CD1 1 ? 43 
ATOM   13700 C CD2 . LEU K  1 123 ? -49.691 -35.333  8.717   1.000 53.397  0 452 LEU KKK CD2 1 ? 43 
ATOM   13701 N N   . TYR K  1 124 ? -46.481 -38.792  10.130  1.000 46.612  0 453 TYR KKK N   1 ? 43 
ATOM   13702 C CA  . TYR K  1 124 ? -45.934 -40.118  10.502  1.000 46.443  0 453 TYR KKK CA  1 ? 43 
ATOM   13703 C C   . TYR K  1 124 ? -47.065 -40.949  11.116  1.000 47.006  0 453 TYR KKK C   1 ? 43 
ATOM   13704 O O   . TYR K  1 124 ? -47.992 -40.369  11.701  1.000 48.498  0 453 TYR KKK O   1 ? 43 
ATOM   13705 C CB  . TYR K  1 124 ? -44.757 -39.959  11.462  1.000 46.052  0 453 TYR KKK CB  1 ? 43 
ATOM   13706 C CG  . TYR K  1 124 ? -45.124 -39.336  12.781  1.000 47.847  0 453 TYR KKK CG  1 ? 43 
ATOM   13707 C CD1 . TYR K  1 124 ? -45.117 -37.959  12.944  1.000 47.551  0 453 TYR KKK CD1 1 ? 43 
ATOM   13708 C CD2 . TYR K  1 124 ? -45.489 -40.123  13.864  1.000 49.546  0 453 TYR KKK CD2 1 ? 43 
ATOM   13709 C CE1 . TYR K  1 124 ? -45.466 -37.372  14.149  1.000 49.489  0 453 TYR KKK CE1 1 ? 43 
ATOM   13710 C CE2 . TYR K  1 124 ? -45.841 -39.547  15.076  1.000 51.111  0 453 TYR KKK CE2 1 ? 43 
ATOM   13711 C CZ  . TYR K  1 124 ? -45.836 -38.169  15.216  1.000 50.780  0 453 TYR KKK CZ  1 ? 43 
ATOM   13712 O OH  . TYR K  1 124 ? -46.175 -37.604  16.406  1.000 52.408  0 453 TYR KKK OH  1 ? 43 
ATOM   13713 N N   . ARG K  1 125 ? -47.010 -42.266  10.967  1.000 47.189  0 454 ARG KKK N   1 ? 43 
ATOM   13714 C CA  . ARG K  1 125 ? -47.966 -43.186  11.629  1.000 48.715  0 454 ARG KKK CA  1 ? 43 
ATOM   13715 C C   . ARG K  1 125 ? -47.561 -43.301  13.100  1.000 48.454  0 454 ARG KKK C   1 ? 43 
ATOM   13716 O O   . ARG K  1 125 ? -46.404 -43.652  13.372  1.000 50.027  0 454 ARG KKK O   1 ? 43 
ATOM   13717 C CB  . ARG K  1 125 ? -48.003 -44.528  10.897  1.000 46.553  0 454 ARG KKK CB  1 ? 43 
ATOM   13718 C CG  . ARG K  1 125 ? -49.081 -45.464  11.419  1.000 48.335  0 454 ARG KKK CG  1 ? 43 
ATOM   13719 C CD  . ARG K  1 125 ? -49.176 -46.717  10.563  1.000 48.014  0 454 ARG KKK CD  1 ? 43 
ATOM   13720 N NE  . ARG K  1 125 ? -49.445 -46.373  9.159   1.000 48.008  0 454 ARG KKK NE  1 ? 43 
ATOM   13721 C CZ  . ARG K  1 125 ? -50.636 -46.021  8.687   1.000 47.836  0 454 ARG KKK CZ  1 ? 43 
ATOM   13722 N NH1 . ARG K  1 125 ? -51.702 -45.977  9.485   1.000 49.767  0 454 ARG KKK NH1 1 ? 43 
ATOM   13723 N NH2 . ARG K  1 125 ? -50.743 -45.708  7.413   1.000 47.140  0 454 ARG KKK NH2 1 ? 43 
ATOM   13724 N N   . LEU K  1 126 ? -48.477 -42.988  14.006  1.000 52.168  0 455 LEU KKK N   1 ? 43 
ATOM   13725 C CA  . LEU K  1 126 ? -48.219 -42.942  15.475  1.000 55.582  0 455 LEU KKK CA  1 ? 43 
ATOM   13726 C C   . LEU K  1 126 ? -48.658 -44.267  16.118  1.000 56.234  0 455 LEU KKK C   1 ? 43 
ATOM   13727 O O   . LEU K  1 126 ? -48.044 -44.687  17.113  1.000 56.401  0 455 LEU KKK O   1 ? 43 
ATOM   13728 C CB  . LEU K  1 126 ? -48.986 -41.751  16.053  1.000 57.369  0 455 LEU KKK CB  1 ? 43 
ATOM   13729 C CG  . LEU K  1 126 ? -48.926 -41.597  17.575  1.000 61.941  0 455 LEU KKK CG  1 ? 43 
ATOM   13730 C CD1 . LEU K  1 126 ? -47.492 -41.518  18.103  1.000 61.038  0 455 LEU KKK CD1 1 ? 43 
ATOM   13731 C CD2 . LEU K  1 126 ? -49.715 -40.375  18.005  1.000 62.938  0 455 LEU KKK CD2 1 ? 43 
ATOM   13732 N N   . PHE K  1 127 ? -49.713 -44.874  15.568  1.000 55.778  0 456 PHE KKK N   1 ? 43 
ATOM   13733 C CA  . PHE K  1 127 ? -50.357 -46.107  16.072  1.000 58.292  0 456 PHE KKK CA  1 ? 43 
ATOM   13734 C C   . PHE K  1 127 ? -50.446 -47.134  14.945  1.000 55.708  0 456 PHE KKK C   1 ? 43 
ATOM   13735 O O   . PHE K  1 127 ? -50.742 -46.784  13.806  1.000 54.745  0 456 PHE KKK O   1 ? 43 
ATOM   13736 C CB  . PHE K  1 127 ? -51.758 -45.815  16.615  1.000 60.527  0 456 PHE KKK CB  1 ? 43 
ATOM   13737 C CG  . PHE K  1 127 ? -51.813 -44.750  17.688  1.000 62.156  0 456 PHE KKK CG  1 ? 43 
ATOM   13738 C CD1 . PHE K  1 127 ? -51.241 -44.961  18.941  1.000 63.409  0 456 PHE KKK CD1 1 ? 43 
ATOM   13739 C CD2 . PHE K  1 127 ? -52.426 -43.533  17.450  1.000 61.864  0 456 PHE KKK CD2 1 ? 43 
ATOM   13740 C CE1 . PHE K  1 127 ? -51.301 -43.994  19.928  1.000 63.879  0 456 PHE KKK CE1 1 ? 43 
ATOM   13741 C CE2 . PHE K  1 127 ? -52.478 -42.561  18.439  1.000 63.242  0 456 PHE KKK CE2 1 ? 43 
ATOM   13742 C CZ  . PHE K  1 127 ? -51.914 -42.795  19.672  1.000 64.386  0 456 PHE KKK CZ  1 ? 43 
ATOM   13743 N N   . ARG K  1 128 ? -50.179 -48.386  15.279  1.000 53.945  0 457 ARG KKK N   1 ? 43 
ATOM   13744 C CA  . ARG K  1 128 ? -50.403 -49.526  14.368  1.000 53.527  0 457 ARG KKK CA  1 ? 43 
ATOM   13745 C C   . ARG K  1 128 ? -50.552 -50.805  15.196  1.000 53.785  0 457 ARG KKK C   1 ? 43 
ATOM   13746 O O   . ARG K  1 128 ? -49.908 -50.911  16.221  1.000 50.562  0 457 ARG KKK O   1 ? 43 
ATOM   13747 C CB  . ARG K  1 128 ? -49.268 -49.612  13.349  1.000 48.679  0 457 ARG KKK CB  1 ? 43 
ATOM   13748 C CG  . ARG K  1 128 ? -49.597 -50.515  12.177  1.000 48.822  0 457 ARG KKK CG  1 ? 43 
ATOM   13749 C CD  . ARG K  1 128 ? -48.530 -50.387  11.112  1.000 49.057  0 457 ARG KKK CD  1 ? 43 
ATOM   13750 N NE  . ARG K  1 128 ? -48.948 -50.942  9.833   1.000 49.931  0 457 ARG KKK NE  1 ? 43 
ATOM   13751 C CZ  . ARG K  1 128 ? -48.828 -52.232  9.500   1.000 49.234  0 457 ARG KKK CZ  1 ? 43 
ATOM   13752 N NH1 . ARG K  1 128 ? -48.272 -53.102  10.324  1.000 51.359  0 457 ARG KKK NH1 1 ? 43 
ATOM   13753 N NH2 . ARG K  1 128 ? -49.228 -52.637  8.319   1.000 48.544  0 457 ARG KKK NH2 1 ? 43 
ATOM   13754 N N   . LYS K  1 129 ? -51.391 -51.727  14.730  1.000 57.788  0 458 LYS KKK N   1 ? 43 
ATOM   13755 C CA  . LYS K  1 129 ? -51.757 -52.976  15.459  1.000 61.902  0 458 LYS KKK CA  1 ? 43 
ATOM   13756 C C   . LYS K  1 129 ? -50.531 -53.884  15.565  1.000 60.700  0 458 LYS KKK C   1 ? 43 
ATOM   13757 O O   . LYS K  1 129 ? -50.431 -54.664  16.505  1.000 63.176  0 458 LYS KKK O   1 ? 43 
ATOM   13758 C CB  . LYS K  1 129 ? -52.907 -53.711  14.763  1.000 64.430  0 458 LYS KKK CB  1 ? 43 
ATOM   13759 C CG  . LYS K  1 129 ? -54.209 -52.922  14.669  1.000 67.791  0 458 LYS KKK CG  1 ? 43 
ATOM   13760 C CD  . LYS K  1 129 ? -55.500 -53.711  14.756  1.000 72.365  0 458 LYS KKK CD  1 ? 43 
ATOM   13761 C CE  . LYS K  1 129 ? -56.579 -52.873  15.422  1.000 75.345  0 458 LYS KKK CE  1 ? 43 
ATOM   13762 N NZ  . LYS K  1 129 ? -57.813 -53.668  15.610  1.000 79.752  0 458 LYS KKK NZ  1 ? 43 
ATOM   13763 N N   . SER K  1 130 ? -49.612 -53.787  14.615  1.000 58.741  0 459 SER KKK N   1 ? 43 
ATOM   13764 C CA  . SER K  1 130 ? -48.400 -54.635  14.565  1.000 56.280  0 459 SER KKK CA  1 ? 43 
ATOM   13765 C C   . SER K  1 130 ? -47.327 -53.912  13.749  1.000 54.975  0 459 SER KKK C   1 ? 43 
ATOM   13766 O O   . SER K  1 130 ? -47.657 -52.967  13.015  1.000 54.469  0 459 SER KKK O   1 ? 43 
ATOM   13767 C CB  . SER K  1 130 ? -48.730 -55.980  14.011  1.000 55.928  0 459 SER KKK CB  1 ? 43 
ATOM   13768 O OG  . SER K  1 130 ? -48.828 -55.927  12.604  1.000 56.163  0 459 SER KKK OG  1 ? 43 
ATOM   13769 N N   . ASN K  1 131 ? -46.079 -54.344  13.898  1.000 53.212  0 460 ASN KKK N   1 ? 43 
ATOM   13770 C CA  . ASN K  1 131 ? -44.904 -53.693  13.274  1.000 50.323  0 460 ASN KKK CA  1 ? 43 
ATOM   13771 C C   . ASN K  1 131 ? -44.929 -53.974  11.769  1.000 48.179  0 460 ASN KKK C   1 ? 43 
ATOM   13772 O O   . ASN K  1 131 ? -45.382 -55.030  11.377  1.000 47.824  0 460 ASN KKK O   1 ? 43 
ATOM   13773 C CB  . ASN K  1 131 ? -43.599 -54.177  13.907  1.000 49.744  0 460 ASN KKK CB  1 ? 43 
ATOM   13774 C CG  . ASN K  1 131 ? -43.454 -53.770  15.359  1.000 50.321  0 460 ASN KKK CG  1 ? 43 
ATOM   13775 O OD1 . ASN K  1 131 ? -44.265 -53.039  15.921  1.000 49.457  0 460 ASN KKK OD1 1 ? 43 
ATOM   13776 N ND2 . ASN K  1 131 ? -42.395 -54.237  15.983  1.000 52.820  0 460 ASN KKK ND2 1 ? 43 
ATOM   13777 N N   . LEU K  1 132 ? -44.449 -53.036  10.969  1.000 47.952  0 461 LEU KKK N   1 ? 43 
ATOM   13778 C CA  . LEU K  1 132 ? -44.192 -53.222  9.529   1.000 50.028  0 461 LEU KKK CA  1 ? 43 
ATOM   13779 C C   . LEU K  1 132 ? -43.198 -54.367  9.341   1.000 52.920  0 461 LEU KKK C   1 ? 43 
ATOM   13780 O O   . LEU K  1 132 ? -42.233 -54.464  10.128  1.000 53.211  0 461 LEU KKK O   1 ? 43 
ATOM   13781 C CB  . LEU K  1 132 ? -43.611 -51.935  8.947   1.000 49.327  0 461 LEU KKK CB  1 ? 43 
ATOM   13782 C CG  . LEU K  1 132 ? -44.583 -50.763  8.835   1.000 51.710  0 461 LEU KKK CG  1 ? 43 
ATOM   13783 C CD1 . LEU K  1 132 ? -43.901 -49.605  8.125   1.000 51.666  0 461 LEU KKK CD1 1 ? 43 
ATOM   13784 C CD2 . LEU K  1 132 ? -45.864 -51.156  8.095   1.000 52.839  0 461 LEU KKK CD2 1 ? 43 
ATOM   13785 N N   . LYS K  1 133 ? -43.424 -55.176  8.306   1.000 55.008  0 462 LYS KKK N   1 ? 43 
ATOM   13786 C CA  . LYS K  1 133 ? -42.383 -56.053  7.718   1.000 55.995  0 462 LYS KKK CA  1 ? 43 
ATOM   13787 C C   . LYS K  1 133 ? -41.364 -55.167  7.002   1.000 53.103  0 462 LYS KKK C   1 ? 43 
ATOM   13788 O O   . LYS K  1 133 ? -41.650 -54.020  6.639   1.000 48.032  0 462 LYS KKK O   1 ? 43 
ATOM   13789 C CB  . LYS K  1 133 ? -43.016 -57.075  6.786   1.000 60.704  0 462 LYS KKK CB  1 ? 43 
ATOM   13790 C CG  . LYS K  1 133 ? -43.762 -58.201  7.492   1.000 67.362  0 462 LYS KKK CG  1 ? 43 
ATOM   13791 C CD  . LYS K  1 133 ? -44.102 -59.403  6.608   1.000 76.836  0 462 LYS KKK CD  1 ? 43 
ATOM   13792 C CE  . LYS K  1 133 ? -43.957 -59.199  5.100   1.000 82.947  0 462 LYS KKK CE  1 ? 43 
ATOM   13793 N NZ  . LYS K  1 133 ? -45.069 -58.424  4.480   1.000 85.016  0 462 LYS KKK NZ  1 ? 43 
ATOM   13794 N N   . PRO K  1 134 ? -40.110 -55.640  6.823   1.000 51.491  0 463 PRO KKK N   1 ? 43 
ATOM   13795 C CA  . PRO K  1 134 ? -39.100 -54.833  6.136   1.000 49.059  0 463 PRO KKK CA  1 ? 43 
ATOM   13796 C C   . PRO K  1 134 ? -39.572 -54.378  4.748   1.000 45.933  0 463 PRO KKK C   1 ? 43 
ATOM   13797 O O   . PRO K  1 134 ? -40.098 -55.161  4.052   1.000 43.887  0 463 PRO KKK O   1 ? 43 
ATOM   13798 C CB  . PRO K  1 134 ? -37.902 -55.777  6.088   1.000 49.859  0 463 PRO KKK CB  1 ? 43 
ATOM   13799 C CG  . PRO K  1 134 ? -38.084 -56.608  7.348   1.000 49.671  0 463 PRO KKK CG  1 ? 43 
ATOM   13800 C CD  . PRO K  1 134 ? -39.566 -56.892  7.373   1.000 50.820  0 463 PRO KKK CD  1 ? 43 
ATOM   13801 N N   . PHE K  1 135 ? -39.420 -53.090  4.457   1.000 44.247  0 464 PHE KKK N   1 ? 43 
ATOM   13802 C CA  . PHE K  1 135 ? -39.787 -52.443  3.174   1.000 44.927  0 464 PHE KKK CA  1 ? 43 
ATOM   13803 C C   . PHE K  1 135 ? -41.307 -52.479  2.939   1.000 44.914  0 464 PHE KKK C   1 ? 43 
ATOM   13804 O O   . PHE K  1 135 ? -41.731 -52.199  1.808   1.000 44.945  0 464 PHE KKK O   1 ? 43 
ATOM   13805 C CB  . PHE K  1 135 ? -39.027 -53.073  2.002   1.000 44.044  0 464 PHE KKK CB  1 ? 43 
ATOM   13806 C CG  . PHE K  1 135 ? -37.535 -52.871  2.046   1.000 42.634  0 464 PHE KKK CG  1 ? 43 
ATOM   13807 C CD1 . PHE K  1 135 ? -36.997 -51.595  2.170   1.000 42.351  0 464 PHE KKK CD1 1 ? 43 
ATOM   13808 C CD2 . PHE K  1 135 ? -36.668 -53.950  1.994   1.000 42.390  0 464 PHE KKK CD2 1 ? 43 
ATOM   13809 C CE1 . PHE K  1 135 ? -35.621 -51.404  2.220   1.000 42.030  0 464 PHE KKK CE1 1 ? 43 
ATOM   13810 C CE2 . PHE K  1 135 ? -35.298 -53.759  2.022   1.000 42.862  0 464 PHE KKK CE2 1 ? 43 
ATOM   13811 C CZ  . PHE K  1 135 ? -34.772 -52.482  2.128   1.000 43.339  0 464 PHE KKK CZ  1 ? 43 
ATOM   13812 N N   . GLU K  1 136 ? -42.103 -52.739  3.973   1.000 45.552  0 465 GLU KKK N   1 ? 43 
ATOM   13813 C CA  . GLU K  1 136 ? -43.580 -52.608  3.890   1.000 46.544  0 465 GLU KKK CA  1 ? 43 
ATOM   13814 C C   . GLU K  1 136 ? -43.932 -51.113  3.930   1.000 47.000  0 465 GLU KKK C   1 ? 43 
ATOM   13815 O O   . GLU K  1 136 ? -43.173 -50.307  4.563   1.000 45.343  0 465 GLU KKK O   1 ? 43 
ATOM   13816 C CB  . GLU K  1 136 ? -44.264 -53.392  5.017   1.000 48.540  0 465 GLU KKK CB  1 ? 43 
ATOM   13817 C CG  . GLU K  1 136 ? -45.746 -53.622  4.791   1.000 50.242  0 465 GLU KKK CG  1 ? 43 
ATOM   13818 C CD  . GLU K  1 136 ? -46.479 -54.423  5.862   1.000 51.908  0 465 GLU KKK CD  1 ? 43 
ATOM   13819 O OE1 . GLU K  1 136 ? -45.831 -54.896  6.840   1.000 51.385  0 465 GLU KKK OE1 1 ? 43 
ATOM   13820 O OE2 . GLU K  1 136 ? -47.720 -54.541  5.731   1.000 54.929  0 465 GLU KKK OE2 1 ? 43 
ATOM   13821 N N   . ARG K  1 137 ? -45.040 -50.762  3.292   1.000 47.651  0 466 ARG KKK N   1 ? 43 
ATOM   13822 C CA  . ARG K  1 137 ? -45.532 -49.370  3.196   1.000 50.252  0 466 ARG KKK CA  1 ? 43 
ATOM   13823 C C   . ARG K  1 137 ? -47.022 -49.370  3.502   1.000 51.311  0 466 ARG KKK C   1 ? 43 
ATOM   13824 O O   . ARG K  1 137 ? -47.730 -50.138  2.863   1.000 54.003  0 466 ARG KKK O   1 ? 43 
ATOM   13825 C CB  . ARG K  1 137 ? -45.289 -48.869  1.779   1.000 50.663  0 466 ARG KKK CB  1 ? 43 
ATOM   13826 C CG  . ARG K  1 137 ? -45.562 -47.392  1.550   1.000 52.268  0 466 ARG KKK CG  1 ? 43 
ATOM   13827 C CD  . ARG K  1 137 ? -45.044 -47.150  0.164   1.000 53.435  0 466 ARG KKK CD  1 ? 43 
ATOM   13828 N NE  . ARG K  1 137 ? -45.161 -45.764  -0.213  1.000 57.313  0 466 ARG KKK NE  1 ? 43 
ATOM   13829 C CZ  . ARG K  1 137 ? -46.201 -45.229  -0.849  1.000 61.613  0 466 ARG KKK CZ  1 ? 43 
ATOM   13830 N NH1 . ARG K  1 137 ? -47.268 -45.951  -1.149  1.000 63.371  0 466 ARG KKK NH1 1 ? 43 
ATOM   13831 N NH2 . ARG K  1 137 ? -46.158 -43.946  -1.176  1.000 61.616  0 466 ARG KKK NH2 1 ? 43 
ATOM   13832 N N   . ASP K  1 138 ? -47.469 -48.573  4.459   1.000 48.800  0 467 ASP KKK N   1 ? 43 
ATOM   13833 C CA  . ASP K  1 138 ? -48.879 -48.554  4.917   1.000 48.356  0 467 ASP KKK CA  1 ? 43 
ATOM   13834 C C   . ASP K  1 138 ? -49.356 -47.110  4.776   1.000 48.927  0 467 ASP KKK C   1 ? 43 
ATOM   13835 O O   . ASP K  1 138 ? -48.800 -46.244  5.490   1.000 48.882  0 467 ASP KKK O   1 ? 43 
ATOM   13836 C CB  . ASP K  1 138 ? -48.985 -49.109  6.341   1.000 47.806  0 467 ASP KKK CB  1 ? 43 
ATOM   13837 C CG  . ASP K  1 138 ? -50.402 -49.172  6.880   1.000 49.863  0 467 ASP KKK CG  1 ? 43 
ATOM   13838 O OD1 . ASP K  1 138 ? -51.329 -48.613  6.217   1.000 46.420  0 467 ASP KKK OD1 1 ? 43 
ATOM   13839 O OD2 . ASP K  1 138 ? -50.571 -49.762  7.973   1.000 52.086  0 467 ASP KKK OD2 1 ? 43 
ATOM   13840 N N   . ILE K  1 139 ? -50.319 -46.861  3.883   1.000 50.231  0 468 ILE KKK N   1 ? 43 
ATOM   13841 C CA  . ILE K  1 139 ? -50.891 -45.500  3.667   1.000 49.558  0 468 ILE KKK CA  1 ? 43 
ATOM   13842 C C   . ILE K  1 139 ? -52.352 -45.462  4.127   1.000 49.008  0 468 ILE KKK C   1 ? 43 
ATOM   13843 O O   . ILE K  1 139 ? -53.008 -44.457  3.894   1.000 50.464  0 468 ILE KKK O   1 ? 43 
ATOM   13844 C CB  . ILE K  1 139 ? -50.671 -45.021  2.215   1.000 50.041  0 468 ILE KKK CB  1 ? 43 
ATOM   13845 C CG1 . ILE K  1 139 ? -51.444 -45.843  1.195   1.000 52.655  0 468 ILE KKK CG1 1 ? 43 
ATOM   13846 C CG2 . ILE K  1 139 ? -49.171 -44.969  1.883   1.000 49.176  0 468 ILE KKK CG2 1 ? 43 
ATOM   13847 C CD1 . ILE K  1 139 ? -51.544 -45.153  -0.164  1.000 55.196  0 468 ILE KKK CD1 1 ? 43 
ATOM   13848 N N   . SER K  1 140 ? -52.812 -46.506  4.812   1.000 49.160  0 469 SER KKK N   1 ? 43 
ATOM   13849 C CA  . SER K  1 140 ? -54.194 -46.607  5.344   1.000 50.717  0 469 SER KKK CA  1 ? 43 
ATOM   13850 C C   . SER K  1 140 ? -54.399 -45.566  6.451   1.000 49.168  0 469 SER KKK C   1 ? 43 
ATOM   13851 O O   . SER K  1 140 ? -53.435 -45.168  7.104   1.000 47.385  0 469 SER KKK O   1 ? 43 
ATOM   13852 C CB  . SER K  1 140 ? -54.504 -48.001  5.836   1.000 52.322  0 469 SER KKK CB  1 ? 43 
ATOM   13853 O OG  . SER K  1 140 ? -53.749 -48.277  6.997   1.000 56.074  0 469 SER KKK OG  1 ? 43 
ATOM   13854 N N   . THR K  1 141 ? -55.639 -45.150  6.641   1.000 50.116  0 470 THR KKK N   1 ? 43 
ATOM   13855 C CA  . THR K  1 141 ? -56.067 -44.147  7.635   1.000 51.581  0 470 THR KKK CA  1 ? 43 
ATOM   13856 C C   . THR K  1 141 ? -57.261 -44.719  8.412   1.000 53.887  0 470 THR KKK C   1 ? 43 
ATOM   13857 O O   . THR K  1 141 ? -58.247 -44.008  8.615   1.000 58.316  0 470 THR KKK O   1 ? 43 
ATOM   13858 C CB  . THR K  1 141 ? -56.327 -42.812  6.934   1.000 51.993  0 470 THR KKK CB  1 ? 43 
ATOM   13859 O OG1 . THR K  1 141 ? -57.270 -43.012  5.891   1.000 54.525  0 470 THR KKK OG1 1 ? 43 
ATOM   13860 C CG2 . THR K  1 141 ? -55.076 -42.189  6.344   1.000 50.880  0 470 THR KKK CG2 1 ? 43 
ATOM   13861 N N   . GLU K  1 142 ? -57.165 -45.980  8.798   1.000 53.291  0 471 GLU KKK N   1 ? 43 
ATOM   13862 C CA  . GLU K  1 142 ? -58.191 -46.692  9.607   1.000 54.814  0 471 GLU KKK CA  1 ? 43 
ATOM   13863 C C   . GLU K  1 142 ? -58.090 -46.184  11.046  1.000 54.541  0 471 GLU KKK C   1 ? 43 
ATOM   13864 O O   . GLU K  1 142 ? -56.967 -45.993  11.518  1.000 50.979  0 471 GLU KKK O   1 ? 43 
ATOM   13865 C CB  . GLU K  1 142 ? -57.991 -48.214  9.564   1.000 54.455  0 471 GLU KKK CB  1 ? 43 
ATOM   13866 C CG  . GLU K  1 142 ? -57.953 -48.785  8.157   1.000 54.685  0 471 GLU KKK CG  1 ? 43 
ATOM   13867 C CD  . GLU K  1 142 ? -59.311 -48.774  7.490   1.000 57.837  0 471 GLU KKK CD  1 ? 43 
ATOM   13868 O OE1 . GLU K  1 142 ? -60.180 -49.484  8.019   1.000 61.357  0 471 GLU KKK OE1 1 ? 43 
ATOM   13869 O OE2 . GLU K  1 142 ? -59.523 -48.073  6.455   1.000 57.658  0 471 GLU KKK OE2 1 ? 43 
ATOM   13870 N N   . ILE K  1 143 ? -59.227 -45.953  11.696  1.000 56.902  0 472 ILE KKK N   1 ? 43 
ATOM   13871 C CA  . ILE K  1 143 ? -59.308 -45.543  13.124  1.000 58.513  0 472 ILE KKK CA  1 ? 43 
ATOM   13872 C C   . ILE K  1 143 ? -58.626 -46.647  13.938  1.000 57.347  0 472 ILE KKK C   1 ? 43 
ATOM   13873 O O   . ILE K  1 143 ? -58.998 -47.808  13.764  1.000 56.158  0 472 ILE KKK O   1 ? 43 
ATOM   13874 C CB  . ILE K  1 143 ? -60.759 -45.338  13.593  1.000 62.088  0 472 ILE KKK CB  1 ? 43 
ATOM   13875 C CG1 . ILE K  1 143 ? -61.513 -44.352  12.699  1.000 64.478  0 472 ILE KKK CG1 1 ? 43 
ATOM   13876 C CG2 . ILE K  1 143 ? -60.755 -44.916  15.071  1.000 63.449  0 472 ILE KKK CG2 1 ? 43 
ATOM   13877 C CD1 . ILE K  1 143 ? -60.785 -43.023  12.528  1.000 64.173  0 472 ILE KKK CD1 1 ? 43 
ATOM   13878 N N   . TYR K  1 144 ? -57.645 -46.294  14.761  1.000 56.137  0 473 TYR KKK N   1 ? 43 
ATOM   13879 C CA  . TYR K  1 144 ? -56.918 -47.259  15.607  1.000 57.285  0 473 TYR KKK CA  1 ? 43 
ATOM   13880 C C   . TYR K  1 144 ? -57.686 -47.433  16.915  1.000 59.858  0 473 TYR KKK C   1 ? 43 
ATOM   13881 O O   . TYR K  1 144 ? -57.992 -46.434  17.569  1.000 60.145  0 473 TYR KKK O   1 ? 43 
ATOM   13882 C CB  . TYR K  1 144 ? -55.481 -46.796  15.786  1.000 57.423  0 473 TYR KKK CB  1 ? 43 
ATOM   13883 C CG  . TYR K  1 144 ? -54.658 -47.622  16.738  1.000 59.883  0 473 TYR KKK CG  1 ? 43 
ATOM   13884 C CD1 . TYR K  1 144 ? -53.996 -48.758  16.316  1.000 60.004  0 473 TYR KKK CD1 1 ? 43 
ATOM   13885 C CD2 . TYR K  1 144 ? -54.516 -47.238  18.063  1.000 63.848  0 473 TYR KKK CD2 1 ? 43 
ATOM   13886 C CE1 . TYR K  1 144 ? -53.237 -49.505  17.196  1.000 61.683  0 473 TYR KKK CE1 1 ? 43 
ATOM   13887 C CE2 . TYR K  1 144 ? -53.720 -47.961  18.941  1.000 65.471  0 473 TYR KKK CE2 1 ? 43 
ATOM   13888 C CZ  . TYR K  1 144 ? -53.053 -49.079  18.493  1.000 63.988  0 473 TYR KKK CZ  1 ? 43 
ATOM   13889 O OH  . TYR K  1 144 ? -52.297 -49.799  19.358  1.000 67.499  0 473 TYR KKK OH  1 ? 43 
ATOM   13890 N N   . GLN K  1 145 ? -58.016 -48.681  17.238  1.000 62.161  0 474 GLN KKK N   1 ? 43 
ATOM   13891 C CA  . GLN K  1 145 ? -58.611 -49.076  18.535  1.000 66.258  0 474 GLN KKK CA  1 ? 43 
ATOM   13892 C C   . GLN K  1 145 ? -57.505 -49.233  19.580  1.000 67.580  0 474 GLN KKK C   1 ? 43 
ATOM   13893 O O   . GLN K  1 145 ? -56.812 -50.258  19.548  1.000 67.417  0 474 GLN KKK O   1 ? 43 
ATOM   13894 C CB  . GLN K  1 145 ? -59.412 -50.361  18.400  1.000 67.450  0 474 GLN KKK CB  1 ? 43 
ATOM   13895 C CG  . GLN K  1 145 ? -59.974 -50.789  19.734  1.000 71.190  0 474 GLN KKK CG  1 ? 43 
ATOM   13896 C CD  . GLN K  1 145 ? -60.959 -51.901  19.568  1.000 72.932  0 474 GLN KKK CD  1 ? 43 
ATOM   13897 O OE1 . GLN K  1 145 ? -61.546 -52.070  18.510  1.000 73.977  0 474 GLN KKK OE1 1 ? 43 
ATOM   13898 N NE2 . GLN K  1 145 ? -61.181 -52.637  20.638  1.000 76.720  0 474 GLN KKK NE2 1 ? 43 
ATOM   13899 N N   . ALA K  1 146 ? -57.339 -48.223  20.430  1.000 69.767  0 475 ALA KKK N   1 ? 43 
ATOM   13900 C CA  . ALA K  1 146 ? -56.299 -48.143  21.483  1.000 72.054  0 475 ALA KKK CA  1 ? 43 
ATOM   13901 C C   . ALA K  1 146 ? -56.834 -48.735  22.790  1.000 75.558  0 475 ALA KKK C   1 ? 43 
ATOM   13902 O O   . ALA K  1 146 ? -56.034 -48.955  23.711  1.000 77.357  0 475 ALA KKK O   1 ? 43 
ATOM   13903 C CB  . ALA K  1 146 ? -55.846 -46.710  21.680  1.000 71.362  0 475 ALA KKK CB  1 ? 43 
ATOM   13904 N N   . GLY K  1 147 ? -58.143 -48.992  22.878  1.000 78.874  0 476 GLY KKK N   1 ? 43 
ATOM   13905 C CA  . GLY K  1 147 ? -58.804 -49.423  24.121  1.000 83.175  0 476 GLY KKK CA  1 ? 43 
ATOM   13906 C C   . GLY K  1 147 ? -59.578 -50.719  23.946  1.000 85.978  0 476 GLY KKK C   1 ? 43 
ATOM   13907 O O   . GLY K  1 147 ? -59.637 -51.249  22.814  1.000 88.767  0 476 GLY KKK O   1 ? 43 
ATOM   13908 N N   . SER K  1 148 ? -60.173 -51.192  25.031  1.000 88.642  0 477 SER KKK N   1 ? 43 
ATOM   13909 C CA  . SER K  1 148 ? -61.157 -52.305  25.071  1.000 89.709  0 477 SER KKK CA  1 ? 43 
ATOM   13910 C C   . SER K  1 148 ? -62.327 -52.045  24.108  1.000 90.412  0 477 SER KKK C   1 ? 43 
ATOM   13911 O O   . SER K  1 148 ? -62.685 -52.970  23.365  1.000 90.889  0 477 SER KKK O   1 ? 43 
ATOM   13912 C CB  . SER K  1 148 ? -61.639 -52.551  26.478  1.000 91.727  0 477 SER KKK CB  1 ? 43 
ATOM   13913 O OG  . SER K  1 148 ? -61.341 -51.481  27.371  1.000 91.549  0 477 SER KKK OG  1 ? 43 
ATOM   13914 N N   . THR K  1 149 ? -62.904 -50.842  24.128  1.000 89.747  0 478 THR KKK N   1 ? 43 
ATOM   13915 C CA  . THR K  1 149 ? -64.122 -50.448  23.364  1.000 88.519  0 478 THR KKK CA  1 ? 43 
ATOM   13916 C C   . THR K  1 149 ? -63.860 -50.492  21.856  1.000 85.515  0 478 THR KKK C   1 ? 43 
ATOM   13917 O O   . THR K  1 149 ? -62.830 -50.016  21.397  1.000 83.863  0 478 THR KKK O   1 ? 43 
ATOM   13918 C CB  . THR K  1 149 ? -64.583 -49.040  23.769  1.000 88.547  0 478 THR KKK CB  1 ? 43 
ATOM   13919 O OG1 . THR K  1 149 ? -63.441 -48.178  23.801  1.000 84.279  0 478 THR KKK OG1 1 ? 43 
ATOM   13920 C CG2 . THR K  1 149 ? -65.178 -48.966  25.156  1.000 91.119  0 478 THR KKK CG2 1 ? 43 
ATOM   13921 N N   . PRO K  1 150 ? -64.784 -51.052  21.039  1.000 85.691  0 479 PRO KKK N   1 ? 43 
ATOM   13922 C CA  . PRO K  1 150 ? -64.668 -50.966  19.579  1.000 83.286  0 479 PRO KKK CA  1 ? 43 
ATOM   13923 C C   . PRO K  1 150 ? -64.904 -49.512  19.126  1.000 82.731  0 479 PRO KKK C   1 ? 43 
ATOM   13924 O O   . PRO K  1 150 ? -65.572 -48.774  19.833  1.000 84.605  0 479 PRO KKK O   1 ? 43 
ATOM   13925 C CB  . PRO K  1 150 ? -65.721 -51.968  19.078  1.000 84.225  0 479 PRO KKK CB  1 ? 43 
ATOM   13926 C CG  . PRO K  1 150 ? -66.766 -51.985  20.177  1.000 87.136  0 479 PRO KKK CG  1 ? 43 
ATOM   13927 C CD  . PRO K  1 150 ? -66.010 -51.754  21.474  1.000 87.748  0 479 PRO KKK CD  1 ? 43 
ATOM   13928 N N   . CYS K  1 151 ? -64.371 -49.130  17.969  1.000 79.950  0 480 CYS KKK N   1 ? 43 
ATOM   13929 C CA  . CYS K  1 151 ? -64.365 -47.725  17.483  1.000 80.001  0 480 CYS KKK CA  1 ? 43 
ATOM   13930 C C   . CYS K  1 151 ? -65.528 -47.415  16.548  1.000 79.789  0 480 CYS KKK C   1 ? 43 
ATOM   13931 O O   . CYS K  1 151 ? -65.840 -46.223  16.404  1.000 80.068  0 480 CYS KKK O   1 ? 43 
ATOM   13932 C CB  . CYS K  1 151 ? -63.053 -47.385  16.802  1.000 79.715  0 480 CYS KKK CB  1 ? 43 
ATOM   13933 S SG  . CYS K  1 151 ? -61.734 -47.208  18.025  1.000 86.373  0 480 CYS KKK SG  1 ? 43 
ATOM   13934 N N   . ASN K  1 152 ? -66.145 -48.443  15.962  1.000 78.858  0 481 ASN KKK N   1 ? 43 
ATOM   13935 C CA  . ASN K  1 152 ? -67.322 -48.315  15.066  1.000 80.720  0 481 ASN KKK CA  1 ? 43 
ATOM   13936 C C   . ASN K  1 152 ? -67.100 -47.225  13.998  1.000 78.497  0 481 ASN KKK C   1 ? 43 
ATOM   13937 O O   . ASN K  1 152 ? -68.055 -46.518  13.671  1.000 77.879  0 481 ASN KKK O   1 ? 43 
ATOM   13938 C CB  . ASN K  1 152 ? -68.571 -48.010  15.895  1.000 84.690  0 481 ASN KKK CB  1 ? 43 
ATOM   13939 C CG  . ASN K  1 152 ? -69.828 -48.099  15.088  1.000 88.380  0 481 ASN KKK CG  1 ? 43 
ATOM   13940 O OD1 . ASN K  1 152 ? -69.923 -49.027  14.298  1.000 92.034  0 481 ASN KKK OD1 1 ? 43 
ATOM   13941 N ND2 . ASN K  1 152 ? -70.763 -47.171  15.285  1.000 91.622  0 481 ASN KKK ND2 1 ? 43 
ATOM   13942 N N   . GLY K  1 153 ? -65.876 -47.108  13.478  1.000 77.908  0 482 GLY KKK N   1 ? 43 
ATOM   13943 C CA  . GLY K  1 153 ? -65.485 -46.169  12.399  1.000 77.877  0 482 GLY KKK CA  1 ? 43 
ATOM   13944 C C   . GLY K  1 153 ? -65.721 -44.708  12.757  1.000 79.228  0 482 GLY KKK C   1 ? 43 
ATOM   13945 O O   . GLY K  1 153 ? -65.978 -43.907  11.838  1.000 81.584  0 482 GLY KKK O   1 ? 43 
ATOM   13946 N N   . VAL K  1 154 ? -65.650 -44.365  14.045  1.000 79.564  0 483 VAL KKK N   1 ? 43 
ATOM   13947 C CA  . VAL K  1 154 ? -65.796 -42.972  14.573  1.000 78.687  0 483 VAL KKK CA  1 ? 43 
ATOM   13948 C C   . VAL K  1 154 ? -64.563 -42.662  15.420  1.000 76.715  0 483 VAL KKK C   1 ? 43 
ATOM   13949 O O   . VAL K  1 154 ? -64.110 -43.564  16.153  1.000 76.865  0 483 VAL KKK O   1 ? 43 
ATOM   13950 C CB  . VAL K  1 154 ? -67.097 -42.825  15.389  1.000 81.415  0 483 VAL KKK CB  1 ? 43 
ATOM   13951 C CG1 . VAL K  1 154 ? -67.118 -41.564  16.211  1.000 82.278  0 483 VAL KKK CG1 1 ? 43 
ATOM   13952 C CG2 . VAL K  1 154 ? -68.337 -42.904  14.518  1.000 82.691  0 483 VAL KKK CG2 1 ? 43 
ATOM   13953 N N   . GLU K  1 155 ? -64.033 -41.448  15.309  1.000 76.374  0 484 GLU KKK N   1 ? 43 
ATOM   13954 C CA  . GLU K  1 155 ? -62.898 -40.945  16.138  1.000 74.902  0 484 GLU KKK CA  1 ? 43 
ATOM   13955 C C   . GLU K  1 155 ? -63.423 -40.564  17.529  1.000 76.277  0 484 GLU KKK C   1 ? 43 
ATOM   13956 O O   . GLU K  1 155 ? -64.593 -40.157  17.614  1.000 78.563  0 484 GLU KKK O   1 ? 43 
ATOM   13957 C CB  . GLU K  1 155 ? -62.261 -39.717  15.490  1.000 75.615  0 484 GLU KKK CB  1 ? 43 
ATOM   13958 C CG  . GLU K  1 155 ? -61.954 -39.858  14.021  1.000 75.284  0 484 GLU KKK CG  1 ? 43 
ATOM   13959 C CD  . GLU K  1 155 ? -60.842 -38.940  13.543  1.000 75.563  0 484 GLU KKK CD  1 ? 43 
ATOM   13960 O OE1 . GLU K  1 155 ? -60.165 -38.310  14.400  1.000 75.438  0 484 GLU KKK OE1 1 ? 43 
ATOM   13961 O OE2 . GLU K  1 155 ? -60.680 -38.831  12.305  1.000 75.868  0 484 GLU KKK OE2 1 ? 43 
ATOM   13962 N N   . GLY K  1 156 ? -62.604 -40.686  18.573  1.000 75.701  0 485 GLY KKK N   1 ? 43 
ATOM   13963 C CA  . GLY K  1 156 ? -62.969 -40.346  19.959  1.000 79.956  0 485 GLY KKK CA  1 ? 43 
ATOM   13964 C C   . GLY K  1 156 ? -61.943 -40.840  20.956  1.000 82.716  0 485 GLY KKK C   1 ? 43 
ATOM   13965 O O   . GLY K  1 156 ? -60.840 -41.199  20.552  1.000 82.420  0 485 GLY KKK O   1 ? 43 
ATOM   13966 N N   . PHE K  1 157 ? -62.307 -40.887  22.236  1.000 92.165  0 486 PHE KKK N   1 ? 43 
ATOM   13967 C CA  . PHE K  1 157 ? -61.502 -41.468  23.348  1.000 95.826  0 486 PHE KKK CA  1 ? 43 
ATOM   13968 C C   . PHE K  1 157 ? -61.085 -42.891  22.947  1.000 91.203  0 486 PHE KKK C   1 ? 43 
ATOM   13969 O O   . PHE K  1 157 ? -61.947 -43.703  22.541  1.000 89.702  0 486 PHE KKK O   1 ? 43 
ATOM   13970 C CB  . PHE K  1 157 ? -62.297 -41.393  24.653  1.000 105.685 0 486 PHE KKK CB  1 ? 43 
ATOM   13971 C CG  . PHE K  1 157 ? -61.694 -42.056  25.871  1.000 111.728 0 486 PHE KKK CG  1 ? 43 
ATOM   13972 C CD1 . PHE K  1 157 ? -60.325 -42.043  26.123  1.000 109.621 0 486 PHE KKK CD1 1 ? 43 
ATOM   13973 C CD2 . PHE K  1 157 ? -62.530 -42.636  26.823  1.000 119.535 0 486 PHE KKK CD2 1 ? 43 
ATOM   13974 C CE1 . PHE K  1 157 ? -59.808 -42.649  27.262  1.000 112.137 0 486 PHE KKK CE1 1 ? 43 
ATOM   13975 C CE2 . PHE K  1 157 ? -62.016 -43.222  27.974  1.000 119.917 0 486 PHE KKK CE2 1 ? 43 
ATOM   13976 C CZ  . PHE K  1 157 ? -60.654 -43.230  28.189  1.000 117.958 0 486 PHE KKK CZ  1 ? 43 
ATOM   13977 N N   . ASN K  1 158 ? -59.778 -43.155  22.983  1.000 88.082  0 487 ASN KKK N   1 ? 43 
ATOM   13978 C CA  . ASN K  1 158 ? -59.137 -44.467  22.692  1.000 85.587  0 487 ASN KKK CA  1 ? 43 
ATOM   13979 C C   . ASN K  1 158 ? -59.407 -44.885  21.245  1.000 80.990  0 487 ASN KKK C   1 ? 43 
ATOM   13980 O O   . ASN K  1 158 ? -59.191 -46.061  20.948  1.000 78.228  0 487 ASN KKK O   1 ? 43 
ATOM   13981 C CB  . ASN K  1 158 ? -59.593 -45.562  23.665  1.000 88.473  0 487 ASN KKK CB  1 ? 43 
ATOM   13982 C CG  . ASN K  1 158 ? -59.076 -45.353  25.067  1.000 90.673  0 487 ASN KKK CG  1 ? 43 
ATOM   13983 O OD1 . ASN K  1 158 ? -57.927 -44.953  25.255  1.000 88.383  0 487 ASN KKK OD1 1 ? 43 
ATOM   13984 N ND2 . ASN K  1 158 ? -59.930 -45.603  26.046  1.000 96.273  0 487 ASN KKK ND2 1 ? 43 
ATOM   13985 N N   . CYS K  1 159 ? -59.816 -43.959  20.383  1.000 79.690  0 488 CYS KKK N   1 ? 43 
ATOM   13986 C CA  . CYS K  1 159 ? -60.191 -44.224  18.969  1.000 78.447  0 488 CYS KKK CA  1 ? 43 
ATOM   13987 C C   . CYS K  1 159 ? -59.547 -43.178  18.064  1.000 75.701  0 488 CYS KKK C   1 ? 43 
ATOM   13988 O O   . CYS K  1 159 ? -60.204 -42.191  17.743  1.000 78.582  0 488 CYS KKK O   1 ? 43 
ATOM   13989 C CB  . CYS K  1 159 ? -61.703 -44.256  18.792  1.000 80.223  0 488 CYS KKK CB  1 ? 43 
ATOM   13990 S SG  . CYS K  1 159 ? -62.426 -45.797  19.398  1.000 80.814  0 488 CYS KKK SG  1 ? 43 
ATOM   13991 N N   . TYR K  1 160 ? -58.282 -43.389  17.722  1.000 72.778  0 489 TYR KKK N   1 ? 43 
ATOM   13992 C CA  . TYR K  1 160 ? -57.391 -42.338  17.177  1.000 71.158  0 489 TYR KKK CA  1 ? 43 
ATOM   13993 C C   . TYR K  1 160 ? -57.257 -42.536  15.671  1.000 68.287  0 489 TYR KKK C   1 ? 43 
ATOM   13994 O O   . TYR K  1 160 ? -57.147 -43.694  15.192  1.000 67.538  0 489 TYR KKK O   1 ? 43 
ATOM   13995 C CB  . TYR K  1 160 ? -56.044 -42.339  17.899  1.000 70.107  0 489 TYR KKK CB  1 ? 43 
ATOM   13996 C CG  . TYR K  1 160 ? -56.164 -42.235  19.395  1.000 74.133  0 489 TYR KKK CG  1 ? 43 
ATOM   13997 C CD1 . TYR K  1 160 ? -56.951 -41.257  19.966  1.000 77.202  0 489 TYR KKK CD1 1 ? 43 
ATOM   13998 C CD2 . TYR K  1 160 ? -55.572 -43.163  20.239  1.000 77.111  0 489 TYR KKK CD2 1 ? 43 
ATOM   13999 C CE1 . TYR K  1 160 ? -57.094 -41.157  21.343  1.000 80.007  0 489 TYR KKK CE1 1 ? 43 
ATOM   14000 C CE2 . TYR K  1 160 ? -55.702 -43.081  21.615  1.000 77.661  0 489 TYR KKK CE2 1 ? 43 
ATOM   14001 C CZ  . TYR K  1 160 ? -56.463 -42.068  22.168  1.000 80.575  0 489 TYR KKK CZ  1 ? 43 
ATOM   14002 O OH  . TYR K  1 160 ? -56.619 -41.985  23.521  1.000 85.440  0 489 TYR KKK OH  1 ? 43 
ATOM   14003 N N   . PHE K  1 161 ? -57.304 -41.422  14.948  1.000 66.517  0 490 PHE KKK N   1 ? 43 
ATOM   14004 C CA  . PHE K  1 161 ? -56.801 -41.317  13.563  1.000 63.748  0 490 PHE KKK CA  1 ? 43 
ATOM   14005 C C   . PHE K  1 161 ? -55.307 -41.614  13.648  1.000 61.893  0 490 PHE KKK C   1 ? 43 
ATOM   14006 O O   . PHE K  1 161 ? -54.625 -41.054  14.491  1.000 59.527  0 490 PHE KKK O   1 ? 43 
ATOM   14007 C CB  . PHE K  1 161 ? -57.114 -39.936  12.993  1.000 63.201  0 490 PHE KKK CB  1 ? 43 
ATOM   14008 C CG  . PHE K  1 161 ? -56.780 -39.776  11.539  1.000 61.997  0 490 PHE KKK CG  1 ? 43 
ATOM   14009 C CD1 . PHE K  1 161 ? -57.608 -40.314  10.568  1.000 62.407  0 490 PHE KKK CD1 1 ? 43 
ATOM   14010 C CD2 . PHE K  1 161 ? -55.631 -39.105  11.138  1.000 60.237  0 490 PHE KKK CD2 1 ? 43 
ATOM   14011 C CE1 . PHE K  1 161 ? -57.314 -40.136  9.222   1.000 61.728  0 490 PHE KKK CE1 1 ? 43 
ATOM   14012 C CE2 . PHE K  1 161 ? -55.326 -38.965  9.790   1.000 58.930  0 490 PHE KKK CE2 1 ? 43 
ATOM   14013 C CZ  . PHE K  1 161 ? -56.187 -39.442  8.840   1.000 59.367  0 490 PHE KKK CZ  1 ? 43 
ATOM   14014 N N   . PRO K  1 162 ? -54.772 -42.563  12.854  1.000 60.063  0 491 PRO KKK N   1 ? 43 
ATOM   14015 C CA  . PRO K  1 162 ? -53.448 -43.119  13.122  1.000 59.210  0 491 PRO KKK CA  1 ? 43 
ATOM   14016 C C   . PRO K  1 162 ? -52.259 -42.262  12.651  1.000 57.434  0 491 PRO KKK C   1 ? 43 
ATOM   14017 O O   . PRO K  1 162 ? -51.132 -42.580  13.051  1.000 56.820  0 491 PRO KKK O   1 ? 43 
ATOM   14018 C CB  . PRO K  1 162 ? -53.490 -44.447  12.345  1.000 59.408  0 491 PRO KKK CB  1 ? 43 
ATOM   14019 C CG  . PRO K  1 162 ? -54.376 -44.146  11.166  1.000 60.030  0 491 PRO KKK CG  1 ? 43 
ATOM   14020 C CD  . PRO K  1 162 ? -55.426 -43.175  11.683  1.000 62.159  0 491 PRO KKK CD  1 ? 43 
ATOM   14021 N N   . LEU K  1 163 ? -52.508 -41.237  11.832  1.000 55.768  0 492 LEU KKK N   1 ? 43 
ATOM   14022 C CA  . LEU K  1 163 ? -51.433 -40.358  11.314  1.000 55.225  0 492 LEU KKK CA  1 ? 43 
ATOM   14023 C C   . LEU K  1 163 ? -51.389 -39.089  12.157  1.000 56.755  0 492 LEU KKK C   1 ? 43 
ATOM   14024 O O   . LEU K  1 163 ? -52.434 -38.585  12.536  1.000 60.100  0 492 LEU KKK O   1 ? 43 
ATOM   14025 C CB  . LEU K  1 163 ? -51.679 -40.011  9.845   1.000 55.175  0 492 LEU KKK CB  1 ? 43 
ATOM   14026 C CG  . LEU K  1 163 ? -51.704 -41.183  8.860   1.000 52.892  0 492 LEU KKK CG  1 ? 43 
ATOM   14027 C CD1 . LEU K  1 163 ? -51.651 -40.659  7.416   1.000 52.316  0 492 LEU KKK CD1 1 ? 43 
ATOM   14028 C CD2 . LEU K  1 163 ? -50.539 -42.127  9.090   1.000 51.190  0 492 LEU KKK CD2 1 ? 43 
ATOM   14029 N N   . GLN K  1 164 ? -50.183 -38.638  12.460  1.000 57.462  0 493 GLN KKK N   1 ? 43 
ATOM   14030 C CA  . GLN K  1 164 ? -49.930 -37.405  13.228  1.000 59.456  0 493 GLN KKK CA  1 ? 43 
ATOM   14031 C C   . GLN K  1 164 ? -48.980 -36.527  12.411  1.000 55.635  0 493 GLN KKK C   1 ? 43 
ATOM   14032 O O   . GLN K  1 164 ? -48.170 -37.040  11.633  1.000 54.080  0 493 GLN KKK O   1 ? 43 
ATOM   14033 C CB  . GLN K  1 164 ? -49.422 -37.784  14.618  1.000 63.366  0 493 GLN KKK CB  1 ? 43 
ATOM   14034 C CG  . GLN K  1 164 ? -49.164 -36.597  15.529  1.000 69.727  0 493 GLN KKK CG  1 ? 43 
ATOM   14035 C CD  . GLN K  1 164 ? -50.443 -35.868  15.868  1.000 75.781  0 493 GLN KKK CD  1 ? 43 
ATOM   14036 O OE1 . GLN K  1 164 ? -50.691 -34.768  15.370  1.000 77.534  0 493 GLN KKK OE1 1 ? 43 
ATOM   14037 N NE2 . GLN K  1 164 ? -51.288 -36.507  16.670  1.000 80.743  0 493 GLN KKK NE2 1 ? 43 
ATOM   14038 N N   . SER K  1 165 ? -49.142 -35.232  12.555  1.000 56.696  0 494 SER KKK N   1 ? 43 
ATOM   14039 C CA  . SER K  1 165 ? -48.369 -34.201  11.846  1.000 55.276  0 494 SER KKK CA  1 ? 43 
ATOM   14040 C C   . SER K  1 165 ? -47.124 -33.895  12.677  1.000 55.384  0 494 SER KKK C   1 ? 43 
ATOM   14041 O O   . SER K  1 165 ? -47.218 -33.930  13.918  1.000 58.158  0 494 SER KKK O   1 ? 43 
ATOM   14042 C CB  . SER K  1 165 ? -49.240 -33.015  11.627  1.000 58.526  0 494 SER KKK CB  1 ? 43 
ATOM   14043 O OG  . SER K  1 165 ? -48.504 -32.024  10.972  1.000 62.760  0 494 SER KKK OG  1 ? 43 
ATOM   14044 N N   . TYR K  1 166 ? -45.991 -33.615  12.029  1.000 54.542  0 495 TYR KKK N   1 ? 43 
ATOM   14045 C CA  . TYR K  1 166 ? -44.734 -33.231  12.714  1.000 52.195  0 495 TYR KKK CA  1 ? 43 
ATOM   14046 C C   . TYR K  1 166 ? -44.844 -31.793  13.221  1.000 53.754  0 495 TYR KKK C   1 ? 43 
ATOM   14047 O O   . TYR K  1 166 ? -44.311 -31.486  14.293  1.000 55.259  0 495 TYR KKK O   1 ? 43 
ATOM   14048 C CB  . TYR K  1 166 ? -43.520 -33.396  11.789  1.000 50.490  0 495 TYR KKK CB  1 ? 43 
ATOM   14049 C CG  . TYR K  1 166 ? -42.917 -34.780  11.780  1.000 47.560  0 495 TYR KKK CG  1 ? 43 
ATOM   14050 C CD1 . TYR K  1 166 ? -42.254 -35.276  12.886  1.000 47.079  0 495 TYR KKK CD1 1 ? 43 
ATOM   14051 C CD2 . TYR K  1 166 ? -43.030 -35.607  10.679  1.000 46.169  0 495 TYR KKK CD2 1 ? 43 
ATOM   14052 C CE1 . TYR K  1 166 ? -41.700 -36.544  12.892  1.000 46.535  0 495 TYR KKK CE1 1 ? 43 
ATOM   14053 C CE2 . TYR K  1 166 ? -42.458 -36.869  10.655  1.000 46.206  0 495 TYR KKK CE2 1 ? 43 
ATOM   14054 C CZ  . TYR K  1 166 ? -41.790 -37.343  11.767  1.000 45.973  0 495 TYR KKK CZ  1 ? 43 
ATOM   14055 O OH  . TYR K  1 166 ? -41.258 -38.601  11.754  1.000 45.117  0 495 TYR KKK OH  1 ? 43 
ATOM   14056 N N   . GLY K  1 167 ? -45.470 -30.895  12.461  1.000 56.870  0 496 GLY KKK N   1 ? 43 
ATOM   14057 C CA  . GLY K  1 167 ? -45.506 -29.475  12.867  1.000 61.799  0 496 GLY KKK CA  1 ? 43 
ATOM   14058 C C   . GLY K  1 167 ? -44.092 -28.936  13.073  1.000 60.566  0 496 GLY KKK C   1 ? 43 
ATOM   14059 O O   . GLY K  1 167 ? -43.706 -28.722  14.241  1.000 63.145  0 496 GLY KKK O   1 ? 43 
ATOM   14060 N N   . PHE K  1 168 ? -43.339 -28.758  11.987  1.000 59.160  0 497 PHE KKK N   1 ? 43 
ATOM   14061 C CA  . PHE K  1 168 ? -41.927 -28.311  12.010  1.000 58.848  0 497 PHE KKK CA  1 ? 43 
ATOM   14062 C C   . PHE K  1 168 ? -41.863 -26.779  12.051  1.000 61.037  0 497 PHE KKK C   1 ? 43 
ATOM   14063 O O   . PHE K  1 168 ? -42.347 -26.137  11.107  1.000 60.794  0 497 PHE KKK O   1 ? 43 
ATOM   14064 C CB  . PHE K  1 168 ? -41.199 -28.803  10.754  1.000 56.723  0 497 PHE KKK CB  1 ? 43 
ATOM   14065 C CG  . PHE K  1 168 ? -40.912 -30.279  10.712  1.000 53.900  0 497 PHE KKK CG  1 ? 43 
ATOM   14066 C CD1 . PHE K  1 168 ? -40.123 -30.866  11.692  1.000 54.041  0 497 PHE KKK CD1 1 ? 43 
ATOM   14067 C CD2 . PHE K  1 168 ? -41.398 -31.075  9.691   1.000 51.749  0 497 PHE KKK CD2 1 ? 43 
ATOM   14068 C CE1 . PHE K  1 168 ? -39.842 -32.219  11.666  1.000 51.061  0 497 PHE KKK CE1 1 ? 43 
ATOM   14069 C CE2 . PHE K  1 168 ? -41.106 -32.425  9.647   1.000 49.528  0 497 PHE KKK CE2 1 ? 43 
ATOM   14070 C CZ  . PHE K  1 168 ? -40.339 -32.995  10.639  1.000 50.955  0 497 PHE KKK CZ  1 ? 43 
ATOM   14071 N N   . GLN K  1 169 ? -41.268 -26.211  13.097  1.000 62.751  0 498 GLN KKK N   1 ? 43 
ATOM   14072 C CA  . GLN K  1 169 ? -41.054 -24.746  13.211  1.000 66.208  0 498 GLN KKK CA  1 ? 43 
ATOM   14073 C C   . GLN K  1 169 ? -39.565 -24.454  13.157  1.000 65.296  0 498 GLN KKK C   1 ? 43 
ATOM   14074 O O   . GLN K  1 169 ? -38.772 -25.190  13.731  1.000 63.877  0 498 GLN KKK O   1 ? 43 
ATOM   14075 C CB  . GLN K  1 169 ? -41.699 -24.229  14.488  1.000 70.007  0 498 GLN KKK CB  1 ? 43 
ATOM   14076 C CG  . GLN K  1 169 ? -43.181 -24.537  14.485  1.000 72.862  0 498 GLN KKK CG  1 ? 43 
ATOM   14077 C CD  . GLN K  1 169 ? -43.784 -24.460  15.856  1.000 75.790  0 498 GLN KKK CD  1 ? 43 
ATOM   14078 O OE1 . GLN K  1 169 ? -44.046 -23.366  16.342  1.000 79.409  0 498 GLN KKK OE1 1 ? 43 
ATOM   14079 N NE2 . GLN K  1 169 ? -44.004 -25.615  16.473  1.000 76.444  0 498 GLN KKK NE2 1 ? 43 
ATOM   14080 N N   . PRO K  1 170 ? -39.167 -23.361  12.471  1.000 66.941  0 499 PRO KKK N   1 ? 43 
ATOM   14081 C CA  . PRO K  1 170 ? -37.750 -23.049  12.282  1.000 64.196  0 499 PRO KKK CA  1 ? 43 
ATOM   14082 C C   . PRO K  1 170 ? -37.003 -22.907  13.623  1.000 61.188  0 499 PRO KKK C   1 ? 43 
ATOM   14083 O O   . PRO K  1 170 ? -35.816 -23.167  13.638  1.000 58.105  0 499 PRO KKK O   1 ? 43 
ATOM   14084 C CB  . PRO K  1 170 ? -37.758 -21.725  11.483  1.000 66.240  0 499 PRO KKK CB  1 ? 43 
ATOM   14085 C CG  . PRO K  1 170 ? -39.179 -21.159  11.626  1.000 68.817  0 499 PRO KKK CG  1 ? 43 
ATOM   14086 C CD  . PRO K  1 170 ? -40.069 -22.353  11.880  1.000 68.085  0 499 PRO KKK CD  1 ? 43 
ATOM   14087 N N   . THR K  1 171 ? -37.700 -22.538  14.706  1.000 59.819  0 500 THR KKK N   1 ? 43 
ATOM   14088 C CA  . THR K  1 171 ? -37.100 -22.324  16.059  1.000 60.061  0 500 THR KKK CA  1 ? 43 
ATOM   14089 C C   . THR K  1 171 ? -37.022 -23.620  16.888  1.000 58.901  0 500 THR KKK C   1 ? 43 
ATOM   14090 O O   . THR K  1 171 ? -36.371 -23.571  17.941  1.000 59.406  0 500 THR KKK O   1 ? 43 
ATOM   14091 C CB  . THR K  1 171 ? -37.836 -21.223  16.821  1.000 60.672  0 500 THR KKK CB  1 ? 43 
ATOM   14092 O OG1 . THR K  1 171 ? -39.210 -21.608  16.815  1.000 62.852  0 500 THR KKK OG1 1 ? 43 
ATOM   14093 C CG2 . THR K  1 171 ? -37.628 -19.869  16.189  1.000 61.091  0 500 THR KKK CG2 1 ? 43 
ATOM   14094 N N   . ASN K  1 172 ? -37.619 -24.732  16.450  1.000 58.596  0 501 ASN KKK N   1 ? 43 
ATOM   14095 C CA  . ASN K  1 172 ? -37.457 -26.064  17.111  1.000 58.492  0 501 ASN KKK CA  1 ? 43 
ATOM   14096 C C   . ASN K  1 172 ? -35.978 -26.348  17.410  1.000 56.585  0 501 ASN KKK C   1 ? 43 
ATOM   14097 O O   . ASN K  1 172 ? -35.130 -25.965  16.590  1.000 59.354  0 501 ASN KKK O   1 ? 43 
ATOM   14098 C CB  . ASN K  1 172 ? -37.965 -27.206  16.224  1.000 59.437  0 501 ASN KKK CB  1 ? 43 
ATOM   14099 C CG  . ASN K  1 172 ? -39.475 -27.239  16.093  1.000 62.492  0 501 ASN KKK CG  1 ? 43 
ATOM   14100 O OD1 . ASN K  1 172 ? -40.160 -26.420  16.699  1.000 65.662  0 501 ASN KKK OD1 1 ? 43 
ATOM   14101 N ND2 . ASN K  1 172 ? -40.007 -28.167  15.300  1.000 61.859  0 501 ASN KKK ND2 1 ? 43 
ATOM   14102 N N   . GLY K  1 173 ? -35.667 -27.036  18.508  1.000 54.573  0 502 GLY KKK N   1 ? 43 
ATOM   14103 C CA  . GLY K  1 173 ? -34.334 -27.637  18.725  1.000 51.021  0 502 GLY KKK CA  1 ? 43 
ATOM   14104 C C   . GLY K  1 173 ? -33.995 -28.609  17.604  1.000 50.269  0 502 GLY KKK C   1 ? 43 
ATOM   14105 O O   . GLY K  1 173 ? -34.935 -29.102  16.906  1.000 49.706  0 502 GLY KKK O   1 ? 43 
ATOM   14106 N N   . VAL K  1 174 ? -32.705 -28.881  17.392  1.000 49.572  0 503 VAL KKK N   1 ? 43 
ATOM   14107 C CA  . VAL K  1 174 ? -32.198 -29.642  16.209  1.000 46.747  0 503 VAL KKK CA  1 ? 43 
ATOM   14108 C C   . VAL K  1 174 ? -32.877 -31.010  16.138  1.000 46.285  0 503 VAL KKK C   1 ? 43 
ATOM   14109 O O   . VAL K  1 174 ? -33.207 -31.446  15.012  1.000 44.984  0 503 VAL KKK O   1 ? 43 
ATOM   14110 C CB  . VAL K  1 174 ? -30.664 -29.772  16.188  1.000 46.880  0 503 VAL KKK CB  1 ? 43 
ATOM   14111 C CG1 . VAL K  1 174 ? -30.119 -30.685  17.256  1.000 48.773  0 503 VAL KKK CG1 1 ? 43 
ATOM   14112 C CG2 . VAL K  1 174 ? -30.188 -30.281  14.854  1.000 46.219  0 503 VAL KKK CG2 1 ? 43 
ATOM   14113 N N   . GLY K  1 175 ? -33.064 -31.668  17.282  1.000 48.321  0 504 GLY KKK N   1 ? 43 
ATOM   14114 C CA  . GLY K  1 175 ? -33.731 -32.973  17.415  1.000 46.378  0 504 GLY KKK CA  1 ? 43 
ATOM   14115 C C   . GLY K  1 175 ? -35.138 -32.961  16.857  1.000 46.770  0 504 GLY KKK C   1 ? 43 
ATOM   14116 O O   . GLY K  1 175 ? -35.586 -34.020  16.404  1.000 44.844  0 504 GLY KKK O   1 ? 43 
ATOM   14117 N N   . TYR K  1 176 ? -35.813 -31.810  16.863  1.000 49.973  0 505 TYR KKK N   1 ? 43 
ATOM   14118 C CA  . TYR K  1 176 ? -37.210 -31.675  16.366  1.000 52.595  0 505 TYR KKK CA  1 ? 43 
ATOM   14119 C C   . TYR K  1 176 ? -37.245 -30.972  14.999  1.000 49.407  0 505 TYR KKK C   1 ? 43 
ATOM   14120 O O   . TYR K  1 176 ? -38.324 -30.644  14.512  1.000 49.804  0 505 TYR KKK O   1 ? 43 
ATOM   14121 C CB  . TYR K  1 176 ? -38.052 -30.963  17.424  1.000 57.110  0 505 TYR KKK CB  1 ? 43 
ATOM   14122 C CG  . TYR K  1 176 ? -38.261 -31.741  18.697  1.000 63.350  0 505 TYR KKK CG  1 ? 43 
ATOM   14123 C CD1 . TYR K  1 176 ? -39.276 -32.692  18.808  1.000 65.780  0 505 TYR KKK CD1 1 ? 43 
ATOM   14124 C CD2 . TYR K  1 176 ? -37.447 -31.518  19.806  1.000 65.429  0 505 TYR KKK CD2 1 ? 43 
ATOM   14125 C CE1 . TYR K  1 176 ? -39.491 -33.379  19.996  1.000 67.197  0 505 TYR KKK CE1 1 ? 43 
ATOM   14126 C CE2 . TYR K  1 176 ? -37.647 -32.194  21.000  1.000 67.996  0 505 TYR KKK CE2 1 ? 43 
ATOM   14127 C CZ  . TYR K  1 176 ? -38.675 -33.125  21.093  1.000 71.383  0 505 TYR KKK CZ  1 ? 43 
ATOM   14128 O OH  . TYR K  1 176 ? -38.862 -33.815  22.258  1.000 76.914  0 505 TYR KKK OH  1 ? 43 
ATOM   14129 N N   . GLN K  1 177 ? -36.093 -30.743  14.372  1.000 47.416  0 506 GLN KKK N   1 ? 43 
ATOM   14130 C CA  . GLN K  1 177 ? -36.037 -30.150  13.004  1.000 44.467  0 506 GLN KKK CA  1 ? 43 
ATOM   14131 C C   . GLN K  1 177 ? -36.210 -31.240  11.969  1.000 41.663  0 506 GLN KKK C   1 ? 43 
ATOM   14132 O O   . GLN K  1 177 ? -35.875 -32.381  12.201  1.000 40.137  0 506 GLN KKK O   1 ? 43 
ATOM   14133 C CB  . GLN K  1 177 ? -34.736 -29.400  12.756  1.000 44.082  0 506 GLN KKK CB  1 ? 43 
ATOM   14134 C CG  . GLN K  1 177 ? -34.751 -28.053  13.433  1.000 45.350  0 506 GLN KKK CG  1 ? 43 
ATOM   14135 C CD  . GLN K  1 177 ? -33.423 -27.366  13.340  1.000 44.194  0 506 GLN KKK CD  1 ? 43 
ATOM   14136 O OE1 . GLN K  1 177 ? -32.644 -27.581  12.420  1.000 44.871  0 506 GLN KKK OE1 1 ? 43 
ATOM   14137 N NE2 . GLN K  1 177 ? -33.183 -26.524  14.312  1.000 43.036  0 506 GLN KKK NE2 1 ? 43 
ATOM   14138 N N   . PRO K  1 178 ? -36.731 -30.913  10.774  1.000 42.802  0 507 PRO KKK N   1 ? 43 
ATOM   14139 C CA  . PRO K  1 178 ? -36.904 -31.919  9.736   1.000 42.506  0 507 PRO KKK CA  1 ? 43 
ATOM   14140 C C   . PRO K  1 178 ? -35.541 -32.319  9.158   1.000 42.131  0 507 PRO KKK C   1 ? 43 
ATOM   14141 O O   . PRO K  1 178 ? -34.679 -31.488  9.008   1.000 42.978  0 507 PRO KKK O   1 ? 43 
ATOM   14142 C CB  . PRO K  1 178 ? -37.782 -31.213  8.705   1.000 44.467  0 507 PRO KKK CB  1 ? 43 
ATOM   14143 C CG  . PRO K  1 178 ? -37.416 -29.758  8.866   1.000 45.620  0 507 PRO KKK CG  1 ? 43 
ATOM   14144 C CD  . PRO K  1 178 ? -37.146 -29.573  10.341  1.000 45.063  0 507 PRO KKK CD  1 ? 43 
ATOM   14145 N N   . TYR K  1 179 ? -35.387 -33.604  8.886   1.000 42.212  0 508 TYR KKK N   1 ? 43 
ATOM   14146 C CA  . TYR K  1 179 ? -34.242 -34.189  8.149   1.000 42.183  0 508 TYR KKK CA  1 ? 43 
ATOM   14147 C C   . TYR K  1 179 ? -34.801 -34.964  6.967   1.000 41.765  0 508 TYR KKK C   1 ? 43 
ATOM   14148 O O   . TYR K  1 179 ? -35.782 -35.687  7.118   1.000 40.789  0 508 TYR KKK O   1 ? 43 
ATOM   14149 C CB  . TYR K  1 179 ? -33.397 -35.075  9.063   1.000 42.729  0 508 TYR KKK CB  1 ? 43 
ATOM   14150 C CG  . TYR K  1 179 ? -32.432 -34.298  9.924   1.000 44.865  0 508 TYR KKK CG  1 ? 43 
ATOM   14151 C CD1 . TYR K  1 179 ? -32.895 -33.460  10.935  1.000 43.357  0 508 TYR KKK CD1 1 ? 43 
ATOM   14152 C CD2 . TYR K  1 179 ? -31.057 -34.376  9.707   1.000 43.125  0 508 TYR KKK CD2 1 ? 43 
ATOM   14153 C CE1 . TYR K  1 179 ? -32.018 -32.722  11.709  1.000 42.979  0 508 TYR KKK CE1 1 ? 43 
ATOM   14154 C CE2 . TYR K  1 179 ? -30.176 -33.643  10.482  1.000 42.806  0 508 TYR KKK CE2 1 ? 43 
ATOM   14155 C CZ  . TYR K  1 179 ? -30.658 -32.812  11.482  1.000 42.819  0 508 TYR KKK CZ  1 ? 43 
ATOM   14156 O OH  . TYR K  1 179 ? -29.796 -32.084  12.252  1.000 44.500  0 508 TYR KKK OH  1 ? 43 
ATOM   14157 N N   . ARG K  1 180 ? -34.226 -34.730  5.801   1.000 41.715  0 509 ARG KKK N   1 ? 43 
ATOM   14158 C CA  . ARG K  1 180 ? -34.470 -35.539  4.588   1.000 41.161  0 509 ARG KKK CA  1 ? 43 
ATOM   14159 C C   . ARG K  1 180 ? -33.566 -36.761  4.651   1.000 41.228  0 509 ARG KKK C   1 ? 43 
ATOM   14160 O O   . ARG K  1 180 ? -32.406 -36.620  5.084   1.000 44.460  0 509 ARG KKK O   1 ? 43 
ATOM   14161 C CB  . ARG K  1 180 ? -34.219 -34.689  3.348   1.000 44.270  0 509 ARG KKK CB  1 ? 43 
ATOM   14162 C CG  . ARG K  1 180 ? -35.345 -33.683  3.154   1.000 46.208  0 509 ARG KKK CG  1 ? 43 
ATOM   14163 C CD  . ARG K  1 180 ? -35.190 -32.851  1.906   1.000 46.743  0 509 ARG KKK CD  1 ? 43 
ATOM   14164 N NE  . ARG K  1 180 ? -36.369 -32.007  1.876   1.000 49.212  0 509 ARG KKK NE  1 ? 43 
ATOM   14165 C CZ  . ARG K  1 180 ? -36.852 -31.410  0.781   1.000 52.125  0 509 ARG KKK CZ  1 ? 43 
ATOM   14166 N NH1 . ARG K  1 180 ? -36.227 -31.524  -0.378  1.000 52.984  0 509 ARG KKK NH1 1 ? 43 
ATOM   14167 N NH2 . ARG K  1 180 ? -37.947 -30.684  0.859   1.000 51.069  0 509 ARG KKK NH2 1 ? 43 
ATOM   14168 N N   . VAL K  1 181 ? -34.101 -37.899  4.241   1.000 38.668  0 510 VAL KKK N   1 ? 43 
ATOM   14169 C CA  . VAL K  1 181 ? -33.421 -39.216  4.283   1.000 38.417  0 510 VAL KKK CA  1 ? 43 
ATOM   14170 C C   . VAL K  1 181 ? -33.495 -39.849  2.886   1.000 38.798  0 510 VAL KKK C   1 ? 43 
ATOM   14171 O O   . VAL K  1 181 ? -34.563 -39.787  2.247   1.000 41.983  0 510 VAL KKK O   1 ? 43 
ATOM   14172 C CB  . VAL K  1 181 ? -34.060 -40.113  5.355   1.000 36.287  0 510 VAL KKK CB  1 ? 43 
ATOM   14173 C CG1 . VAL K  1 181 ? -33.294 -41.404  5.517   1.000 37.262  0 510 VAL KKK CG1 1 ? 43 
ATOM   14174 C CG2 . VAL K  1 181 ? -34.163 -39.398  6.684   1.000 37.324  0 510 VAL KKK CG2 1 ? 43 
ATOM   14175 N N   . VAL K  1 182 ? -32.377 -40.398  2.434   1.000 38.177  0 511 VAL KKK N   1 ? 43 
ATOM   14176 C CA  . VAL K  1 182 ? -32.309 -41.301  1.260   1.000 39.211  0 511 VAL KKK CA  1 ? 43 
ATOM   14177 C C   . VAL K  1 182 ? -31.672 -42.603  1.727   1.000 39.146  0 511 VAL KKK C   1 ? 43 
ATOM   14178 O O   . VAL K  1 182 ? -30.614 -42.562  2.388   1.000 38.968  0 511 VAL KKK O   1 ? 43 
ATOM   14179 C CB  . VAL K  1 182 ? -31.541 -40.675  0.095   1.000 39.552  0 511 VAL KKK CB  1 ? 43 
ATOM   14180 C CG1 . VAL K  1 182 ? -31.383 -41.675  -1.029  1.000 41.889  0 511 VAL KKK CG1 1 ? 43 
ATOM   14181 C CG2 . VAL K  1 182 ? -32.210 -39.394  -0.407  1.000 39.886  0 511 VAL KKK CG2 1 ? 43 
ATOM   14182 N N   . VAL K  1 183 ? -32.368 -43.706  1.467   1.000 38.131  0 512 VAL KKK N   1 ? 43 
ATOM   14183 C CA  . VAL K  1 183 ? -31.890 -45.086  1.729   1.000 39.568  0 512 VAL KKK CA  1 ? 43 
ATOM   14184 C C   . VAL K  1 183 ? -31.615 -45.717  0.372   1.000 41.561  0 512 VAL KKK C   1 ? 43 
ATOM   14185 O O   . VAL K  1 183 ? -32.558 -45.765  -0.471  1.000 41.579  0 512 VAL KKK O   1 ? 43 
ATOM   14186 C CB  . VAL K  1 183 ? -32.912 -45.906  2.523   1.000 40.606  0 512 VAL KKK CB  1 ? 43 
ATOM   14187 C CG1 . VAL K  1 183 ? -32.377 -47.307  2.836   1.000 41.122  0 512 VAL KKK CG1 1 ? 43 
ATOM   14188 C CG2 . VAL K  1 183 ? -33.328 -45.173  3.792   1.000 41.765  0 512 VAL KKK CG2 1 ? 43 
ATOM   14189 N N   . LEU K  1 184 ? -30.361 -46.097  0.141   1.000 40.891  0 513 LEU KKK N   1 ? 43 
ATOM   14190 C CA  . LEU K  1 184 ? -29.964 -46.824  -1.079  1.000 43.529  0 513 LEU KKK CA  1 ? 43 
ATOM   14191 C C   . LEU K  1 184 ? -29.888 -48.306  -0.693  1.000 44.555  0 513 LEU KKK C   1 ? 43 
ATOM   14192 O O   . LEU K  1 184 ? -29.056 -48.654  0.165   1.000 44.522  0 513 LEU KKK O   1 ? 43 
ATOM   14193 C CB  . LEU K  1 184 ? -28.633 -46.273  -1.598  1.000 41.993  0 513 LEU KKK CB  1 ? 43 
ATOM   14194 C CG  . LEU K  1 184 ? -28.645 -44.791  -1.956  1.000 41.075  0 513 LEU KKK CG  1 ? 43 
ATOM   14195 C CD1 . LEU K  1 184 ? -27.246 -44.294  -2.249  1.000 42.342  0 513 LEU KKK CD1 1 ? 43 
ATOM   14196 C CD2 . LEU K  1 184 ? -29.586 -44.491  -3.100  1.000 42.043  0 513 LEU KKK CD2 1 ? 43 
ATOM   14197 N N   . SER K  1 185 ? -30.780 -49.105  -1.283  1.000 43.834  0 514 SER KKK N   1 ? 43 
ATOM   14198 C CA  . SER K  1 185 ? -30.781 -50.581  -1.221  1.000 46.912  0 514 SER KKK CA  1 ? 43 
ATOM   14199 C C   . SER K  1 185 ? -29.964 -51.116  -2.381  1.000 49.061  0 514 SER KKK C   1 ? 43 
ATOM   14200 O O   . SER K  1 185 ? -30.219 -50.690  -3.515  1.000 49.083  0 514 SER KKK O   1 ? 43 
ATOM   14201 C CB  . SER K  1 185 ? -32.161 -51.113  -1.292  1.000 47.723  0 514 SER KKK CB  1 ? 43 
ATOM   14202 O OG  . SER K  1 185 ? -32.769 -51.004  -0.032  1.000 48.459  0 514 SER KKK OG  1 ? 43 
ATOM   14203 N N   . PHE K  1 186 ? -29.042 -52.039  -2.110  1.000 49.554  0 515 PHE KKK N   1 ? 43 
ATOM   14204 C CA  . PHE K  1 186 ? -28.230 -52.699  -3.160  1.000 51.459  0 515 PHE KKK CA  1 ? 43 
ATOM   14205 C C   . PHE K  1 186 ? -28.765 -54.107  -3.347  1.000 53.876  0 515 PHE KKK C   1 ? 43 
ATOM   14206 O O   . PHE K  1 186 ? -28.790 -54.834  -2.380  1.000 56.862  0 515 PHE KKK O   1 ? 43 
ATOM   14207 C CB  . PHE K  1 186 ? -26.753 -52.673  -2.792  1.000 51.610  0 515 PHE KKK CB  1 ? 43 
ATOM   14208 C CG  . PHE K  1 186 ? -26.191 -51.299  -2.545  1.000 51.960  0 515 PHE KKK CG  1 ? 43 
ATOM   14209 C CD1 . PHE K  1 186 ? -26.664 -50.196  -3.250  1.000 54.596  0 515 PHE KKK CD1 1 ? 43 
ATOM   14210 C CD2 . PHE K  1 186 ? -25.138 -51.117  -1.661  1.000 52.051  0 515 PHE KKK CD2 1 ? 43 
ATOM   14211 C CE1 . PHE K  1 186 ? -26.156 -48.936  -3.003  1.000 52.845  0 515 PHE KKK CE1 1 ? 43 
ATOM   14212 C CE2 . PHE K  1 186 ? -24.600 -49.856  -1.453  1.000 51.743  0 515 PHE KKK CE2 1 ? 43 
ATOM   14213 C CZ  . PHE K  1 186 ? -25.097 -48.775  -2.141  1.000 51.662  0 515 PHE KKK CZ  1 ? 43 
ATOM   14214 N N   . GLU K  1 187 ? -29.261 -54.413  -4.532  1.000 57.997  0 516 GLU KKK N   1 ? 43 
ATOM   14215 C CA  . GLU K  1 187 ? -29.918 -55.693  -4.848  1.000 63.944  0 516 GLU KKK CA  1 ? 43 
ATOM   14216 C C   . GLU K  1 187 ? -28.926 -56.561  -5.616  1.000 68.949  0 516 GLU KKK C   1 ? 43 
ATOM   14217 O O   . GLU K  1 187 ? -28.298 -56.073  -6.567  1.000 70.471  0 516 GLU KKK O   1 ? 43 
ATOM   14218 C CB  . GLU K  1 187 ? -31.164 -55.438  -5.683  1.000 67.254  0 516 GLU KKK CB  1 ? 43 
ATOM   14219 C CG  . GLU K  1 187 ? -32.141 -56.593  -5.656  1.000 71.187  0 516 GLU KKK CG  1 ? 43 
ATOM   14220 C CD  . GLU K  1 187 ? -33.265 -56.525  -6.676  1.000 73.099  0 516 GLU KKK CD  1 ? 43 
ATOM   14221 O OE1 . GLU K  1 187 ? -32.965 -56.182  -7.813  1.000 75.390  0 516 GLU KKK OE1 1 ? 43 
ATOM   14222 O OE2 . GLU K  1 187 ? -34.413 -56.851  -6.335  1.000 71.733  0 516 GLU KKK OE2 1 ? 43 
ATOM   14223 N N   . LEU K  1 188 ? -28.759 -57.786  -5.128  1.000 75.134  0 517 LEU KKK N   1 ? 43 
ATOM   14224 C CA  . LEU K  1 188 ? -27.915 -58.800  -5.777  1.000 81.302  0 517 LEU KKK CA  1 ? 43 
ATOM   14225 C C   . LEU K  1 188 ? -28.793 -60.014  -6.018  1.000 80.775  0 517 LEU KKK C   1 ? 43 
ATOM   14226 O O   . LEU K  1 188 ? -28.943 -60.808  -5.126  1.000 80.366  0 517 LEU KKK O   1 ? 43 
ATOM   14227 C CB  . LEU K  1 188 ? -26.679 -59.089  -4.921  1.000 87.535  0 517 LEU KKK CB  1 ? 43 
ATOM   14228 C CG  . LEU K  1 188 ? -25.439 -58.330  -5.410  1.000 93.347  0 517 LEU KKK CG  1 ? 43 
ATOM   14229 C CD1 . LEU K  1 188 ? -24.286 -58.471  -4.412  1.000 95.355  0 517 LEU KKK CD1 1 ? 43 
ATOM   14230 C CD2 . LEU K  1 188 ? -24.974 -58.841  -6.785  1.000 94.137  0 517 LEU KKK CD2 1 ? 43 
ATOM   14231 N N   . LEU K  1 189 ? -29.320 -60.094  -7.229  1.000 80.939  0 518 LEU KKK N   1 ? 43 
ATOM   14232 C CA  . LEU K  1 189 ? -29.913 -61.352  -7.771  1.000 82.779  0 518 LEU KKK CA  1 ? 43 
ATOM   14233 C C   . LEU K  1 189 ? -28.754 -62.049  -8.510  1.000 88.095  0 518 LEU KKK C   1 ? 43 
ATOM   14234 O O   . LEU K  1 189 ? -27.715 -61.358  -8.815  1.000 89.992  0 518 LEU KKK O   1 ? 43 
ATOM   14235 C CB  . LEU K  1 189 ? -31.091 -60.984  -8.684  1.000 81.760  0 518 LEU KKK CB  1 ? 43 
ATOM   14236 C CG  . LEU K  1 189 ? -32.003 -59.854  -8.175  1.000 78.073  0 518 LEU KKK CG  1 ? 43 
ATOM   14237 C CD1 . LEU K  1 189 ? -33.002 -59.403  -9.225  1.000 77.989  0 518 LEU KKK CD1 1 ? 43 
ATOM   14238 C CD2 . LEU K  1 189 ? -32.699 -60.243  -6.878  1.000 75.151  0 518 LEU KKK CD2 1 ? 43 
ATOM   14239 N N   . HIS K  1 190 ? -28.840 -63.351  -8.802  1.000 94.193  0 519 HIS KKK N   1 ? 43 
ATOM   14240 C CA  . HIS K  1 190 ? -27.882 -63.985  -9.758  1.000 97.247  0 519 HIS KKK CA  1 ? 43 
ATOM   14241 C C   . HIS K  1 190 ? -28.452 -63.737  -11.163 1.000 95.776  0 519 HIS KKK C   1 ? 43 
ATOM   14242 O O   . HIS K  1 190 ? -29.126 -64.584  -11.746 1.000 100.812 0 519 HIS KKK O   1 ? 43 
ATOM   14243 C CB  . HIS K  1 190 ? -27.434 -65.402  -9.387  1.000 101.790 0 519 HIS KKK CB  1 ? 43 
ATOM   14244 C CG  . HIS K  1 190 ? -25.947 -65.581  -9.470  1.000 104.478 0 519 HIS KKK CG  1 ? 43 
ATOM   14245 N ND1 . HIS K  1 190 ? -25.350 -66.444  -10.387 1.000 109.741 0 519 HIS KKK ND1 1 ? 43 
ATOM   14246 C CD2 . HIS K  1 190 ? -24.941 -64.984  -8.789  1.000 100.573 0 519 HIS KKK CD2 1 ? 43 
ATOM   14247 C CE1 . HIS K  1 190 ? -24.040 -66.394  -10.246 1.000 106.922 0 519 HIS KKK CE1 1 ? 43 
ATOM   14248 N NE2 . HIS K  1 190 ? -23.766 -65.499  -9.272  1.000 103.867 0 519 HIS KKK NE2 1 ? 43 
ATOM   14249 N N   . ALA K  1 191 ? -28.162 -62.518  -11.624 1.000 90.954  0 520 ALA KKK N   1 ? 43 
ATOM   14250 C CA  . ALA K  1 191 ? -28.504 -61.918  -12.927 1.000 88.548  0 520 ALA KKK CA  1 ? 43 
ATOM   14251 C C   . ALA K  1 191 ? -27.386 -60.953  -13.317 1.000 84.891  0 520 ALA KKK C   1 ? 43 
ATOM   14252 O O   . ALA K  1 191 ? -26.564 -60.587  -12.481 1.000 80.486  0 520 ALA KKK O   1 ? 43 
ATOM   14253 C CB  . ALA K  1 191 ? -29.810 -61.207  -12.756 1.000 87.070  0 520 ALA KKK CB  1 ? 43 
ATOM   14254 N N   . PRO K  1 192 ? -27.273 -60.526  -14.593 1.000 84.272  0 521 PRO KKK N   1 ? 43 
ATOM   14255 C CA  . PRO K  1 192 ? -26.303 -59.496  -14.947 1.000 81.724  0 521 PRO KKK CA  1 ? 43 
ATOM   14256 C C   . PRO K  1 192 ? -26.489 -58.215  -14.117 1.000 75.847  0 521 PRO KKK C   1 ? 43 
ATOM   14257 O O   . PRO K  1 192 ? -27.610 -57.817  -13.840 1.000 74.341  0 521 PRO KKK O   1 ? 43 
ATOM   14258 C CB  . PRO K  1 192 ? -26.580 -59.264  -16.437 1.000 84.104  0 521 PRO KKK CB  1 ? 43 
ATOM   14259 C CG  . PRO K  1 192 ? -27.112 -60.586  -16.911 1.000 86.524  0 521 PRO KKK CG  1 ? 43 
ATOM   14260 C CD  . PRO K  1 192 ? -27.985 -61.043  -15.768 1.000 85.286  0 521 PRO KKK CD  1 ? 43 
ATOM   14261 N N   . ALA K  1 193 ? -25.368 -57.641  -13.696 1.000 73.799  0 522 ALA KKK N   1 ? 43 
ATOM   14262 C CA  . ALA K  1 193 ? -25.323 -56.361  -12.977 1.000 70.579  0 522 ALA KKK CA  1 ? 43 
ATOM   14263 C C   . ALA K  1 193 ? -25.756 -55.282  -13.960 1.000 69.507  0 522 ALA KKK C   1 ? 43 
ATOM   14264 O O   . ALA K  1 193 ? -25.320 -55.337  -15.103 1.000 71.830  0 522 ALA KKK O   1 ? 43 
ATOM   14265 C CB  . ALA K  1 193 ? -23.922 -56.117  -12.474 1.000 70.434  0 522 ALA KKK CB  1 ? 43 
ATOM   14266 N N   . THR K  1 194 ? -26.576 -54.331  -13.543 1.000 68.260  0 523 THR KKK N   1 ? 43 
ATOM   14267 C CA  . THR K  1 194 ? -26.935 -53.172  -14.404 1.000 67.807  0 523 THR KKK CA  1 ? 43 
ATOM   14268 C C   . THR K  1 194 ? -26.409 -51.870  -13.785 1.000 64.293  0 523 THR KKK C   1 ? 43 
ATOM   14269 O O   . THR K  1 194 ? -26.307 -50.891  -14.509 1.000 65.816  0 523 THR KKK O   1 ? 43 
ATOM   14270 C CB  . THR K  1 194 ? -28.440 -53.159  -14.701 1.000 67.712  0 523 THR KKK CB  1 ? 43 
ATOM   14271 O OG1 . THR K  1 194 ? -29.138 -52.688  -13.544 1.000 63.963  0 523 THR KKK OG1 1 ? 43 
ATOM   14272 C CG2 . THR K  1 194 ? -28.953 -54.514  -15.163 1.000 69.369  0 523 THR KKK CG2 1 ? 43 
ATOM   14273 N N   . VAL K  1 195 ? -26.029 -51.887  -12.517 1.000 60.425  0 524 VAL KKK N   1 ? 43 
ATOM   14274 C CA  . VAL K  1 195 ? -25.464 -50.691  -11.846 1.000 59.411  0 524 VAL KKK CA  1 ? 43 
ATOM   14275 C C   . VAL K  1 195 ? -24.049 -51.012  -11.372 1.000 62.264  0 524 VAL KKK C   1 ? 43 
ATOM   14276 O O   . VAL K  1 195 ? -23.910 -51.884  -10.533 1.000 62.921  0 524 VAL KKK O   1 ? 43 
ATOM   14277 C CB  . VAL K  1 195 ? -26.336 -50.248  -10.673 1.000 55.934  0 524 VAL KKK CB  1 ? 43 
ATOM   14278 C CG1 . VAL K  1 195 ? -25.687 -49.071  -9.960  1.000 54.154  0 524 VAL KKK CG1 1 ? 43 
ATOM   14279 C CG2 . VAL K  1 195 ? -27.760 -49.918  -11.095 1.000 56.226  0 524 VAL KKK CG2 1 ? 43 
ATOM   14280 N N   . CYS K  1 196 ? -23.055 -50.330  -11.927 1.000 65.422  0 525 CYS KKK N   1 ? 43 
ATOM   14281 C CA  . CYS K  1 196 ? -21.612 -50.493  -11.601 1.000 67.071  0 525 CYS KKK CA  1 ? 43 
ATOM   14282 C C   . CYS K  1 196 ? -20.994 -49.132  -11.321 1.000 66.923  0 525 CYS KKK C   1 ? 43 
ATOM   14283 O O   . CYS K  1 196 ? -21.525 -48.138  -11.848 1.000 65.187  0 525 CYS KKK O   1 ? 43 
ATOM   14284 C CB  . CYS K  1 196 ? -20.872 -51.182  -12.747 1.000 71.198  0 525 CYS KKK CB  1 ? 43 
ATOM   14285 S SG  . CYS K  1 196 ? -21.311 -52.936  -12.919 1.000 75.539  0 525 CYS KKK SG  1 ? 43 
ATOM   14286 N N   . GLY K  1 197 ? -19.929 -49.100  -10.525 1.000 70.882  0 526 GLY KKK N   1 ? 43 
ATOM   14287 C CA  . GLY K  1 197 ? -19.079 -47.912  -10.336 1.000 74.160  0 526 GLY KKK CA  1 ? 43 
ATOM   14288 C C   . GLY K  1 197 ? -18.286 -47.606  -11.605 1.000 81.658  0 526 GLY KKK C   1 ? 43 
ATOM   14289 O O   . GLY K  1 197 ? -18.247 -48.419  -12.530 1.000 83.958  0 526 GLY KKK O   1 ? 43 
ATOM   14290 N N   . PRO K  1 198 ? -17.612 -46.437  -11.671 1.000 88.158  0 527 PRO KKK N   1 ? 43 
ATOM   14291 C CA  . PRO K  1 198 ? -16.772 -46.086  -12.824 1.000 92.877  0 527 PRO KKK CA  1 ? 43 
ATOM   14292 C C   . PRO K  1 198 ? -15.675 -47.110  -13.183 1.000 103.054 0 527 PRO KKK C   1 ? 43 
ATOM   14293 O O   . PRO K  1 198 ? -15.247 -47.147  -14.318 1.000 103.810 0 527 PRO KKK O   1 ? 43 
ATOM   14294 C CB  . PRO K  1 198 ? -16.062 -44.809  -12.356 1.000 89.970  0 527 PRO KKK CB  1 ? 43 
ATOM   14295 C CG  . PRO K  1 198 ? -16.935 -44.246  -11.244 1.000 86.935  0 527 PRO KKK CG  1 ? 43 
ATOM   14296 C CD  . PRO K  1 198 ? -17.581 -45.441  -10.584 1.000 84.815  0 527 PRO KKK CD  1 ? 43 
ATOM   14297 N N   . LYS K  1 199 ? -15.295 -47.928  -12.194 1.000 81.433  0 528 LYS KKK N   1 ? ?  
ATOM   14298 C CA  . LYS K  1 199 ? -14.080 -48.785  -12.133 1.000 93.731  0 528 LYS KKK CA  1 ? ?  
ATOM   14299 C C   . LYS K  1 199 ? -14.448 -50.232  -12.511 1.000 96.777  0 528 LYS KKK C   1 ? ?  
ATOM   14300 O O   . LYS K  1 199 ? -14.637 -51.174  -11.728 1.000 91.432  0 528 LYS KKK O   1 ? ?  
ATOM   14301 C CB  . LYS K  1 199 ? -13.479 -48.628  -10.728 1.000 93.208  0 528 LYS KKK CB  1 ? ?  
ATOM   14302 C CG  . LYS K  1 199 ? -13.758 -47.271  -10.086 1.000 93.578  0 528 LYS KKK CG  1 ? ?  
ATOM   14303 C CD  . LYS K  1 199 ? -12.656 -46.722  -9.197  1.000 97.803  0 528 LYS KKK CD  1 ? ?  
ATOM   14304 C CE  . LYS K  1 199 ? -12.429 -45.244  -9.441  1.000 100.693 0 528 LYS KKK CE  1 ? ?  
ATOM   14305 N NZ  . LYS K  1 199 ? -11.316 -44.698  -8.629  1.000 98.931  0 528 LYS KKK NZ  1 ? ?  
ATOM   14306 N N   . GLN L  2 1   ? -29.724 -52.737  22.817  1.000 67.063  0 1   GLN LLL N   1 ? 44 
ATOM   14307 C CA  . GLN L  2 1   ? -28.762 -52.111  23.729  1.000 63.668  0 1   GLN LLL CA  1 ? 44 
ATOM   14308 C C   . GLN L  2 1   ? -27.504 -52.987  23.779  1.000 56.351  0 1   GLN LLL C   1 ? 44 
ATOM   14309 O O   . GLN L  2 1   ? -27.588 -54.164  24.143  1.000 53.899  0 1   GLN LLL O   1 ? 44 
ATOM   14310 C CB  . GLN L  2 1   ? -29.419 -51.876  25.101  1.000 69.089  0 1   GLN LLL CB  1 ? 44 
ATOM   14311 C CG  . GLN L  2 1   ? -28.485 -51.315  26.194  1.000 73.600  0 1   GLN LLL CG  1 ? 44 
ATOM   14312 C CD  . GLN L  2 1   ? -27.836 -49.947  25.995  1.000 76.588  0 1   GLN LLL CD  1 ? 44 
ATOM   14313 O OE1 . GLN L  2 1   ? -28.139 -49.192  25.075  1.000 84.753  0 1   GLN LLL OE1 1 ? 44 
ATOM   14314 N NE2 . GLN L  2 1   ? -26.926 -49.586  26.889  1.000 76.669  0 1   GLN LLL NE2 1 ? 44 
ATOM   14315 N N   . VAL L  2 2   ? -26.359 -52.397  23.452  1.000 51.887  0 2   VAL LLL N   1 ? 44 
ATOM   14316 C CA  . VAL L  2 2   ? -25.017 -52.998  23.678  1.000 48.604  0 2   VAL LLL CA  1 ? 44 
ATOM   14317 C C   . VAL L  2 2   ? -24.320 -52.225  24.808  1.000 45.430  0 2   VAL LLL C   1 ? 44 
ATOM   14318 O O   . VAL L  2 2   ? -24.274 -50.994  24.744  1.000 44.509  0 2   VAL LLL O   1 ? 44 
ATOM   14319 C CB  . VAL L  2 2   ? -24.170 -52.928  22.394  1.000 49.820  0 2   VAL LLL CB  1 ? 44 
ATOM   14320 C CG1 . VAL L  2 2   ? -22.780 -53.490  22.630  1.000 48.455  0 2   VAL LLL CG1 1 ? 44 
ATOM   14321 C CG2 . VAL L  2 2   ? -24.845 -53.616  21.231  1.000 52.433  0 2   VAL LLL CG2 1 ? 44 
ATOM   14322 N N   . GLN L  2 3   ? -23.727 -52.922  25.770  1.000 43.014  0 3   GLN LLL N   1 ? 44 
ATOM   14323 C CA  . GLN L  2 3   ? -22.840 -52.274  26.754  1.000 40.974  0 3   GLN LLL CA  1 ? 44 
ATOM   14324 C C   . GLN L  2 3   ? -21.387 -52.553  26.358  1.000 39.905  0 3   GLN LLL C   1 ? 44 
ATOM   14325 O O   . GLN L  2 3   ? -21.106 -53.617  25.751  1.000 42.019  0 3   GLN LLL O   1 ? 44 
ATOM   14326 C CB  . GLN L  2 3   ? -23.224 -52.724  28.159  1.000 39.688  0 3   GLN LLL CB  1 ? 44 
ATOM   14327 C CG  . GLN L  2 3   ? -24.479 -52.033  28.657  1.000 40.579  0 3   GLN LLL CG  1 ? 44 
ATOM   14328 C CD  . GLN L  2 3   ? -24.688 -52.284  30.130  1.000 41.938  0 3   GLN LLL CD  1 ? 44 
ATOM   14329 O OE1 . GLN L  2 3   ? -23.818 -51.967  30.958  1.000 41.148  0 3   GLN LLL OE1 1 ? 44 
ATOM   14330 N NE2 . GLN L  2 3   ? -25.799 -52.933  30.473  1.000 41.640  0 3   GLN LLL NE2 1 ? 44 
ATOM   14331 N N   . LEU L  2 4   ? -20.515 -51.609  26.680  1.000 37.362  0 4   LEU LLL N   1 ? 44 
ATOM   14332 C CA  . LEU L  2 4   ? -19.081 -51.610  26.323  1.000 37.062  0 4   LEU LLL CA  1 ? 44 
ATOM   14333 C C   . LEU L  2 4   ? -18.269 -51.257  27.575  1.000 36.335  0 4   LEU LLL C   1 ? 44 
ATOM   14334 O O   . LEU L  2 4   ? -18.590 -50.241  28.217  1.000 37.912  0 4   LEU LLL O   1 ? 44 
ATOM   14335 C CB  . LEU L  2 4   ? -18.852 -50.571  25.222  1.000 37.622  0 4   LEU LLL CB  1 ? 44 
ATOM   14336 C CG  . LEU L  2 4   ? -19.647 -50.737  23.931  1.000 39.177  0 4   LEU LLL CG  1 ? 44 
ATOM   14337 C CD1 . LEU L  2 4   ? -19.501 -49.500  23.056  1.000 39.346  0 4   LEU LLL CD1 1 ? 44 
ATOM   14338 C CD2 . LEU L  2 4   ? -19.238 -51.992  23.177  1.000 39.260  0 4   LEU LLL CD2 1 ? 44 
ATOM   14339 N N   . VAL L  2 5   ? -17.254 -52.055  27.900  1.000 35.482  0 5   VAL LLL N   1 ? 44 
ATOM   14340 C CA  . VAL L  2 5   ? -16.349 -51.773  29.038  1.000 35.394  0 5   VAL LLL CA  1 ? 44 
ATOM   14341 C C   . VAL L  2 5   ? -14.890 -51.812  28.565  1.000 37.012  0 5   VAL LLL C   1 ? 44 
ATOM   14342 O O   . VAL L  2 5   ? -14.426 -52.878  28.106  1.000 37.739  0 5   VAL LLL O   1 ? 44 
ATOM   14343 C CB  . VAL L  2 5   ? -16.610 -52.717  30.215  1.000 35.838  0 5   VAL LLL CB  1 ? 44 
ATOM   14344 C CG1 . VAL L  2 5   ? -15.582 -52.523  31.321  1.000 35.130  0 5   VAL LLL CG1 1 ? 44 
ATOM   14345 C CG2 . VAL L  2 5   ? -18.008 -52.524  30.765  1.000 37.125  0 5   VAL LLL CG2 1 ? 44 
ATOM   14346 N N   . GLU L  2 6   ? -14.214 -50.665  28.676  1.000 37.027  0 6   GLU LLL N   1 ? 44 
ATOM   14347 C CA  . GLU L  2 6   ? -12.767 -50.494  28.422  1.000 37.668  0 6   GLU LLL CA  1 ? 44 
ATOM   14348 C C   . GLU L  2 6   ? -11.981 -50.999  29.627  1.000 39.235  0 6   GLU LLL C   1 ? 44 
ATOM   14349 O O   . GLU L  2 6   ? -12.487 -50.872  30.764  1.000 40.170  0 6   GLU LLL O   1 ? 44 
ATOM   14350 C CB  . GLU L  2 6   ? -12.428 -49.022  28.198  1.000 38.598  0 6   GLU LLL CB  1 ? 44 
ATOM   14351 C CG  . GLU L  2 6   ? -13.268 -48.340  27.140  1.000 38.780  0 6   GLU LLL CG  1 ? 44 
ATOM   14352 C CD  . GLU L  2 6   ? -14.545 -47.673  27.625  1.000 39.909  0 6   GLU LLL CD  1 ? 44 
ATOM   14353 O OE1 . GLU L  2 6   ? -15.023 -48.014  28.745  1.000 39.001  0 6   GLU LLL OE1 1 ? 44 
ATOM   14354 O OE2 . GLU L  2 6   ? -15.063 -46.803  26.882  1.000 40.625  0 6   GLU LLL OE2 1 ? 44 
ATOM   14355 N N   . SER L  2 7   ? -10.784 -51.540  29.378  1.000 40.178  0 7   SER LLL N   1 ? 44 
ATOM   14356 C CA  . SER L  2 7   ? -9.750  -51.851  30.390  1.000 42.010  0 7   SER LLL CA  1 ? 44 
ATOM   14357 C C   . SER L  2 7   ? -8.351  -51.645  29.785  1.000 44.099  0 7   SER LLL C   1 ? 44 
ATOM   14358 O O   . SER L  2 7   ? -8.252  -51.420  28.577  1.000 45.814  0 7   SER LLL O   1 ? 44 
ATOM   14359 C CB  . SER L  2 7   ? -9.956  -53.241  30.892  1.000 42.236  0 7   SER LLL CB  1 ? 44 
ATOM   14360 O OG  . SER L  2 7   ? -9.835  -54.151  29.823  1.000 41.943  0 7   SER LLL OG  1 ? 44 
ATOM   14361 N N   . GLY L  2 8   ? -7.310  -51.718  30.608  1.000 48.127  0 8   GLY LLL N   1 ? 44 
ATOM   14362 C CA  . GLY L  2 8   ? -5.900  -51.669  30.182  1.000 51.167  0 8   GLY LLL CA  1 ? 44 
ATOM   14363 C C   . GLY L  2 8   ? -5.309  -50.269  30.276  1.000 52.739  0 8   GLY LLL C   1 ? 44 
ATOM   14364 O O   . GLY L  2 8   ? -4.120  -50.102  29.887  1.000 56.563  0 8   GLY LLL O   1 ? 44 
ATOM   14365 N N   . GLY L  2 9   ? -6.071  -49.285  30.744  1.000 52.049  0 9   GLY LLL N   1 ? 44 
ATOM   14366 C CA  . GLY L  2 9   ? -5.570  -47.904  30.855  1.000 56.155  0 9   GLY LLL CA  1 ? 44 
ATOM   14367 C C   . GLY L  2 9   ? -4.652  -47.719  32.064  1.000 56.942  0 9   GLY LLL C   1 ? 44 
ATOM   14368 O O   . GLY L  2 9   ? -4.392  -48.691  32.740  1.000 62.135  0 9   GLY LLL O   1 ? 44 
ATOM   14369 N N   . GLY L  2 10  ? -4.197  -46.496  32.310  1.000 55.336  0 10  GLY LLL N   1 ? 44 
ATOM   14370 C CA  . GLY L  2 10  ? -3.385  -46.137  33.480  1.000 57.049  0 10  GLY LLL CA  1 ? 44 
ATOM   14371 C C   . GLY L  2 10  ? -2.171  -45.313  33.093  1.000 57.745  0 10  GLY LLL C   1 ? 44 
ATOM   14372 O O   . GLY L  2 10  ? -2.154  -44.730  31.972  1.000 56.548  0 10  GLY LLL O   1 ? 44 
ATOM   14373 N N   . LEU L  2 11  ? -1.201  -45.238  34.007  1.000 59.938  0 11  LEU LLL N   1 ? 44 
ATOM   14374 C CA  . LEU L  2 11  ? 0.016   -44.400  33.909  1.000 62.645  0 11  LEU LLL CA  1 ? 44 
ATOM   14375 C C   . LEU L  2 11  ? 1.065   -45.157  33.088  1.000 64.049  0 11  LEU LLL C   1 ? 44 
ATOM   14376 O O   . LEU L  2 11  ? 1.200   -46.355  33.273  1.000 66.979  0 11  LEU LLL O   1 ? 44 
ATOM   14377 C CB  . LEU L  2 11  ? 0.492   -44.102  35.332  1.000 65.354  0 11  LEU LLL CB  1 ? 44 
ATOM   14378 C CG  . LEU L  2 11  ? 1.755   -43.250  35.483  1.000 69.416  0 11  LEU LLL CG  1 ? 44 
ATOM   14379 C CD1 . LEU L  2 11  ? 1.649   -41.951  34.691  1.000 67.944  0 11  LEU LLL CD1 1 ? 44 
ATOM   14380 C CD2 . LEU L  2 11  ? 2.051   -42.966  36.957  1.000 71.224  0 11  LEU LLL CD2 1 ? 44 
ATOM   14381 N N   . VAL L  2 12  ? 1.775   -44.482  32.189  1.000 64.020  0 12  VAL LLL N   1 ? 44 
ATOM   14382 C CA  . VAL L  2 12  ? 2.855   -45.103  31.371  1.000 64.597  0 12  VAL LLL CA  1 ? 44 
ATOM   14383 C C   . VAL L  2 12  ? 3.850   -43.996  31.018  1.000 63.585  0 12  VAL LLL C   1 ? 44 
ATOM   14384 O O   . VAL L  2 12  ? 3.410   -42.822  30.903  1.000 59.690  0 12  VAL LLL O   1 ? 44 
ATOM   14385 C CB  . VAL L  2 12  ? 2.273   -45.819  30.136  1.000 63.251  0 12  VAL LLL CB  1 ? 44 
ATOM   14386 C CG1 . VAL L  2 12  ? 1.717   -44.837  29.127  1.000 62.345  0 12  VAL LLL CG1 1 ? 44 
ATOM   14387 C CG2 . VAL L  2 12  ? 3.278   -46.713  29.423  1.000 65.396  0 12  VAL LLL CG2 1 ? 44 
ATOM   14388 N N   . GLN L  2 13  ? 5.141   -44.339  30.923  1.000 65.854  0 13  GLN LLL N   1 ? 44 
ATOM   14389 C CA  . GLN L  2 13  ? 6.209   -43.350  30.599  1.000 67.031  0 13  GLN LLL CA  1 ? 44 
ATOM   14390 C C   . GLN L  2 13  ? 6.214   -43.121  29.086  1.000 62.935  0 13  GLN LLL C   1 ? 44 
ATOM   14391 O O   . GLN L  2 13  ? 5.905   -44.079  28.339  1.000 61.167  0 13  GLN LLL O   1 ? 44 
ATOM   14392 C CB  . GLN L  2 13  ? 7.572   -43.747  31.160  1.000 73.397  0 13  GLN LLL CB  1 ? 44 
ATOM   14393 C CG  . GLN L  2 13  ? 8.102   -45.108  30.732  1.000 77.179  0 13  GLN LLL CG  1 ? 44 
ATOM   14394 C CD  . GLN L  2 13  ? 9.523   -45.338  31.209  1.000 82.883  0 13  GLN LLL CD  1 ? 44 
ATOM   14395 O OE1 . GLN L  2 13  ? 10.479  -44.711  30.737  1.000 85.328  0 13  GLN LLL OE1 1 ? 44 
ATOM   14396 N NE2 . GLN L  2 13  ? 9.697   -46.289  32.122  1.000 84.828  0 13  GLN LLL NE2 1 ? 44 
ATOM   14397 N N   . ALA L  2 14  ? 6.491   -41.879  28.665  1.000 60.862  0 14  ALA LLL N   1 ? 44 
ATOM   14398 C CA  . ALA L  2 14  ? 6.705   -41.467  27.261  1.000 58.916  0 14  ALA LLL CA  1 ? 44 
ATOM   14399 C C   . ALA L  2 14  ? 7.609   -42.495  26.570  1.000 59.929  0 14  ALA LLL C   1 ? 44 
ATOM   14400 O O   . ALA L  2 14  ? 8.548   -42.988  27.220  1.000 61.222  0 14  ALA LLL O   1 ? 44 
ATOM   14401 C CB  . ALA L  2 14  ? 7.314   -40.085  27.199  1.000 60.053  0 14  ALA LLL CB  1 ? 44 
ATOM   14402 N N   . GLY L  2 15  ? 7.298   -42.835  25.313  1.000 57.764  0 15  GLY LLL N   1 ? 44 
ATOM   14403 C CA  . GLY L  2 15  ? 7.981   -43.893  24.556  1.000 59.422  0 15  GLY LLL CA  1 ? 44 
ATOM   14404 C C   . GLY L  2 15  ? 7.490   -45.284  24.926  1.000 60.378  0 15  GLY LLL C   1 ? 44 
ATOM   14405 O O   . GLY L  2 15  ? 7.866   -46.223  24.223  1.000 62.657  0 15  GLY LLL O   1 ? 44 
ATOM   14406 N N   . GLY L  2 16  ? 6.667   -45.433  25.973  1.000 59.449  0 16  GLY LLL N   1 ? 44 
ATOM   14407 C CA  . GLY L  2 16  ? 6.155   -46.734  26.435  1.000 59.796  0 16  GLY LLL CA  1 ? 44 
ATOM   14408 C C   . GLY L  2 16  ? 5.002   -47.217  25.574  1.000 59.191  0 16  GLY LLL C   1 ? 44 
ATOM   14409 O O   . GLY L  2 16  ? 4.630   -46.508  24.606  1.000 57.019  0 16  GLY LLL O   1 ? 44 
ATOM   14410 N N   . SER L  2 17  ? 4.424   -48.361  25.958  1.000 60.808  0 17  SER LLL N   1 ? 44 
ATOM   14411 C CA  . SER L  2 17  ? 3.287   -49.044  25.288  1.000 57.427  0 17  SER LLL CA  1 ? 44 
ATOM   14412 C C   . SER L  2 17  ? 2.164   -49.348  26.275  1.000 56.207  0 17  SER LLL C   1 ? 44 
ATOM   14413 O O   . SER L  2 17  ? 2.431   -49.523  27.473  1.000 57.037  0 17  SER LLL O   1 ? 44 
ATOM   14414 C CB  . SER L  2 17  ? 3.730   -50.308  24.642  1.000 58.391  0 17  SER LLL CB  1 ? 44 
ATOM   14415 O OG  . SER L  2 17  ? 4.498   -50.010  23.505  1.000 60.041  0 17  SER LLL OG  1 ? 44 
ATOM   14416 N N   . LEU L  2 18  ? 0.959   -49.438  25.728  1.000 55.878  0 18  LEU LLL N   1 ? 44 
ATOM   14417 C CA  . LEU L  2 18  ? -0.281  -49.877  26.410  1.000 55.687  0 18  LEU LLL CA  1 ? 44 
ATOM   14418 C C   . LEU L  2 18  ? -1.159  -50.561  25.378  1.000 52.541  0 18  LEU LLL C   1 ? 44 
ATOM   14419 O O   . LEU L  2 18  ? -1.259  -50.042  24.268  1.000 52.061  0 18  LEU LLL O   1 ? 44 
ATOM   14420 C CB  . LEU L  2 18  ? -1.034  -48.661  26.956  1.000 56.156  0 18  LEU LLL CB  1 ? 44 
ATOM   14421 C CG  . LEU L  2 18  ? -0.764  -48.275  28.395  1.000 57.572  0 18  LEU LLL CG  1 ? 44 
ATOM   14422 C CD1 . LEU L  2 18  ? -1.789  -47.211  28.801  1.000 56.121  0 18  LEU LLL CD1 1 ? 44 
ATOM   14423 C CD2 . LEU L  2 18  ? -0.774  -49.503  29.316  1.000 58.671  0 18  LEU LLL CD2 1 ? 44 
ATOM   14424 N N   . ARG L  2 19  ? -1.813  -51.632  25.787  1.000 51.526  0 19  ARG LLL N   1 ? 44 
ATOM   14425 C CA  . ARG L  2 19  ? -2.940  -52.215  25.031  1.000 50.716  0 19  ARG LLL CA  1 ? 44 
ATOM   14426 C C   . ARG L  2 19  ? -4.251  -51.978  25.783  1.000 46.411  0 19  ARG LLL C   1 ? 44 
ATOM   14427 O O   . ARG L  2 19  ? -4.485  -52.586  26.826  1.000 47.194  0 19  ARG LLL O   1 ? 44 
ATOM   14428 C CB  . ARG L  2 19  ? -2.680  -53.694  24.754  1.000 53.431  0 19  ARG LLL CB  1 ? 44 
ATOM   14429 C CG  . ARG L  2 19  ? -3.496  -54.197  23.580  1.000 54.404  0 19  ARG LLL CG  1 ? 44 
ATOM   14430 C CD  . ARG L  2 19  ? -3.302  -55.670  23.379  1.000 58.461  0 19  ARG LLL CD  1 ? 44 
ATOM   14431 N NE  . ARG L  2 19  ? -3.899  -56.337  24.521  1.000 60.028  0 19  ARG LLL NE  1 ? 44 
ATOM   14432 C CZ  . ARG L  2 19  ? -4.290  -57.604  24.545  1.000 64.386  0 19  ARG LLL CZ  1 ? 44 
ATOM   14433 N NH1 . ARG L  2 19  ? -4.166  -58.356  23.456  1.000 68.430  0 19  ARG LLL NH1 1 ? 44 
ATOM   14434 N NH2 . ARG L  2 19  ? -4.811  -58.102  25.656  1.000 61.751  0 19  ARG LLL NH2 1 ? 44 
ATOM   14435 N N   . LEU L  2 20  ? -5.046  -51.057  25.272  1.000 45.495  0 20  LEU LLL N   1 ? 44 
ATOM   14436 C CA  . LEU L  2 20  ? -6.459  -50.884  25.683  1.000 46.895  0 20  LEU LLL CA  1 ? 44 
ATOM   14437 C C   . LEU L  2 20  ? -7.266  -52.043  25.095  1.000 47.351  0 20  LEU LLL C   1 ? 44 
ATOM   14438 O O   . LEU L  2 20  ? -6.977  -52.483  23.958  1.000 50.076  0 20  LEU LLL O   1 ? 44 
ATOM   14439 C CB  . LEU L  2 20  ? -6.988  -49.535  25.200  1.000 45.496  0 20  LEU LLL CB  1 ? 44 
ATOM   14440 C CG  . LEU L  2 20  ? -6.259  -48.315  25.758  1.000 47.031  0 20  LEU LLL CG  1 ? 44 
ATOM   14441 C CD1 . LEU L  2 20  ? -7.015  -47.053  25.354  1.000 46.939  0 20  LEU LLL CD1 1 ? 44 
ATOM   14442 C CD2 . LEU L  2 20  ? -6.035  -48.408  27.274  1.000 46.554  0 20  LEU LLL CD2 1 ? 44 
ATOM   14443 N N   . ALA L  2 21  ? -8.230  -52.530  25.860  1.000 46.653  0 21  ALA LLL N   1 ? 44 
ATOM   14444 C CA  . ALA L  2 21  ? -9.234  -53.495  25.371  1.000 47.968  0 21  ALA LLL CA  1 ? 44 
ATOM   14445 C C   . ALA L  2 21  ? -10.629 -52.995  25.701  1.000 45.832  0 21  ALA LLL C   1 ? 44 
ATOM   14446 O O   . ALA L  2 21  ? -10.786 -52.259  26.659  1.000 47.844  0 21  ALA LLL O   1 ? 44 
ATOM   14447 C CB  . ALA L  2 21  ? -9.002  -54.868  25.943  1.000 48.765  0 21  ALA LLL CB  1 ? 44 
ATOM   14448 N N   . CYS L  2 22  ? -11.594 -53.384  24.893  1.000 45.467  0 22  CYS LLL N   1 ? 44 
ATOM   14449 C CA  . CYS L  2 22  ? -13.005 -53.069  25.125  1.000 46.225  0 22  CYS LLL CA  1 ? 44 
ATOM   14450 C C   . CYS L  2 22  ? -13.851 -54.280  24.747  1.000 46.129  0 22  CYS LLL C   1 ? 44 
ATOM   14451 O O   . CYS L  2 22  ? -13.738 -54.745  23.602  1.000 47.633  0 22  CYS LLL O   1 ? 44 
ATOM   14452 C CB  . CYS L  2 22  ? -13.398 -51.857  24.308  1.000 48.635  0 22  CYS LLL CB  1 ? 44 
ATOM   14453 S SG  . CYS L  2 22  ? -15.194 -51.631  24.297  1.000 50.968  0 22  CYS LLL SG  1 ? 44 
ATOM   14454 N N   . ILE L  2 23  ? -14.656 -54.755  25.689  1.000 42.498  0 23  ILE LLL N   1 ? 44 
ATOM   14455 C CA  . ILE L  2 23  ? -15.523 -55.941  25.513  1.000 42.366  0 23  ILE LLL CA  1 ? 44 
ATOM   14456 C C   . ILE L  2 23  ? -16.980 -55.464  25.427  1.000 42.835  0 23  ILE LLL C   1 ? 44 
ATOM   14457 O O   . ILE L  2 23  ? -17.356 -54.558  26.157  1.000 39.499  0 23  ILE LLL O   1 ? 44 
ATOM   14458 C CB  . ILE L  2 23  ? -15.257 -56.968  26.628  1.000 41.745  0 23  ILE LLL CB  1 ? 44 
ATOM   14459 C CG1 . ILE L  2 23  ? -15.950 -58.300  26.336  1.000 41.611  0 23  ILE LLL CG1 1 ? 44 
ATOM   14460 C CG2 . ILE L  2 23  ? -15.613 -56.409  27.996  1.000 41.584  0 23  ILE LLL CG2 1 ? 44 
ATOM   14461 C CD1 . ILE L  2 23  ? -15.637 -59.398  27.322  1.000 42.052  0 23  ILE LLL CD1 1 ? 44 
ATOM   14462 N N   . ALA L  2 24  ? -17.735 -56.036  24.491  1.000 40.981  0 24  ALA LLL N   1 ? 45 
ATOM   14463 C CA  . ALA L  2 24  ? -19.153 -55.735  24.214  1.000 41.623  0 24  ALA LLL CA  1 ? 45 
ATOM   14464 C C   . ALA L  2 24  ? -20.025 -56.881  24.720  1.000 42.781  0 24  ALA LLL C   1 ? 45 
ATOM   14465 O O   . ALA L  2 24  ? -19.564 -58.040  24.720  1.000 44.835  0 24  ALA LLL O   1 ? 45 
ATOM   14466 C CB  . ALA L  2 24  ? -19.358 -55.504  22.738  1.000 40.935  0 24  ALA LLL CB  1 ? 45 
ATOM   14467 N N   . SER L  2 25  ? -21.229 -56.551  25.194  1.000 42.248  0 25  SER LLL N   1 ? 45 
ATOM   14468 C CA  . SER L  2 25  ? -22.329 -57.524  25.427  1.000 42.077  0 25  SER LLL CA  1 ? 45 
ATOM   14469 C C   . SER L  2 25  ? -22.815 -58.028  24.058  1.000 42.513  0 25  SER LLL C   1 ? 45 
ATOM   14470 O O   . SER L  2 25  ? -22.356 -57.508  23.033  1.000 42.938  0 25  SER LLL O   1 ? 45 
ATOM   14471 C CB  . SER L  2 25  ? -23.433 -56.872  26.198  1.000 40.594  0 25  SER LLL CB  1 ? 45 
ATOM   14472 O OG  . SER L  2 25  ? -24.036 -55.852  25.417  1.000 38.664  0 25  SER LLL OG  1 ? 45 
ATOM   14473 N N   . GLY L  2 26  ? -23.743 -58.969  24.023  1.000 44.583  0 26  GLY LLL N   1 ? 45 
ATOM   14474 C CA  . GLY L  2 26  ? -24.440 -59.348  22.778  1.000 46.885  0 26  GLY LLL CA  1 ? 45 
ATOM   14475 C C   . GLY L  2 26  ? -23.812 -60.547  22.096  1.000 48.439  0 26  GLY LLL C   1 ? 45 
ATOM   14476 O O   . GLY L  2 26  ? -22.667 -60.867  22.382  1.000 46.651  0 26  GLY LLL O   1 ? 45 
ATOM   14477 N N   . ARG L  2 27  ? -24.558 -61.188  21.201  1.000 54.502  0 27  ARG LLL N   1 ? 45 
ATOM   14478 C CA  . ARG L  2 27  ? -24.098 -62.374  20.443  1.000 58.362  0 27  ARG LLL CA  1 ? 45 
ATOM   14479 C C   . ARG L  2 27  ? -23.905 -62.024  18.962  1.000 55.902  0 27  ARG LLL C   1 ? 45 
ATOM   14480 O O   . ARG L  2 27  ? -23.791 -62.929  18.190  1.000 56.379  0 27  ARG LLL O   1 ? 45 
ATOM   14481 C CB  . ARG L  2 27  ? -25.095 -63.500  20.696  1.000 65.598  0 27  ARG LLL CB  1 ? 45 
ATOM   14482 C CG  . ARG L  2 27  ? -24.689 -64.398  21.865  1.000 77.228  0 27  ARG LLL CG  1 ? 45 
ATOM   14483 C CD  . ARG L  2 27  ? -25.725 -65.500  22.119  1.000 88.682  0 27  ARG LLL CD  1 ? 45 
ATOM   14484 N NE  . ARG L  2 27  ? -27.073 -64.967  21.876  1.000 97.164  0 27  ARG LLL NE  1 ? 45 
ATOM   14485 C CZ  . ARG L  2 27  ? -28.011 -64.682  22.794  1.000 105.809 0 27  ARG LLL CZ  1 ? 45 
ATOM   14486 N NH1 . ARG L  2 27  ? -27.819 -64.930  24.085  1.000 106.426 0 27  ARG LLL NH1 1 ? 45 
ATOM   14487 N NH2 . ARG L  2 27  ? -29.167 -64.169  22.396  1.000 110.019 0 27  ARG LLL NH2 1 ? 45 
ATOM   14488 N N   . THR L  2 28  ? -23.858 -60.749  18.583  1.000 54.477  0 28  THR LLL N   1 ? 45 
ATOM   14489 C CA  . THR L  2 28  ? -23.678 -60.327  17.162  1.000 53.450  0 28  THR LLL CA  1 ? 45 
ATOM   14490 C C   . THR L  2 28  ? -22.572 -59.274  17.095  1.000 49.335  0 28  THR LLL C   1 ? 45 
ATOM   14491 O O   . THR L  2 28  ? -22.702 -58.321  16.310  1.000 51.594  0 28  THR LLL O   1 ? 45 
ATOM   14492 C CB  . THR L  2 28  ? -24.988 -59.815  16.537  1.000 53.705  0 28  THR LLL CB  1 ? 45 
ATOM   14493 O OG1 . THR L  2 28  ? -25.514 -58.792  17.389  1.000 53.818  0 28  THR LLL OG1 1 ? 45 
ATOM   14494 C CG2 . THR L  2 28  ? -26.046 -60.883  16.394  1.000 55.620  0 28  THR LLL CG2 1 ? 45 
ATOM   14495 N N   . PHE L  2 29  ? -21.503 -59.467  17.852  1.000 46.299  0 29  PHE LLL N   1 ? 45 
ATOM   14496 C CA  . PHE L  2 29  ? -20.337 -58.548  17.869  1.000 45.511  0 29  PHE LLL CA  1 ? 45 
ATOM   14497 C C   . PHE L  2 29  ? -19.808 -58.325  16.439  1.000 47.689  0 29  PHE LLL C   1 ? 45 
ATOM   14498 O O   . PHE L  2 29  ? -19.433 -57.201  16.102  1.000 47.632  0 29  PHE LLL O   1 ? 45 
ATOM   14499 C CB  . PHE L  2 29  ? -19.254 -59.098  18.789  1.000 43.975  0 29  PHE LLL CB  1 ? 45 
ATOM   14500 C CG  . PHE L  2 29  ? -18.058 -58.197  18.900  1.000 43.592  0 29  PHE LLL CG  1 ? 45 
ATOM   14501 C CD1 . PHE L  2 29  ? -18.088 -57.062  19.683  1.000 43.268  0 29  PHE LLL CD1 1 ? 45 
ATOM   14502 C CD2 . PHE L  2 29  ? -16.897 -58.495  18.232  1.000 43.767  0 29  PHE LLL CD2 1 ? 45 
ATOM   14503 C CE1 . PHE L  2 29  ? -16.966 -56.253  19.798  1.000 42.717  0 29  PHE LLL CE1 1 ? 45 
ATOM   14504 C CE2 . PHE L  2 29  ? -15.774 -57.690  18.348  1.000 43.533  0 29  PHE LLL CE2 1 ? 45 
ATOM   14505 C CZ  . PHE L  2 29  ? -15.809 -56.572  19.138  1.000 42.318  0 29  PHE LLL CZ  1 ? 45 
ATOM   14506 N N   . HIS L  2 30  ? -19.780 -59.375  15.621  1.000 48.007  0 30  HIS LLL N   1 ? 45 
ATOM   14507 C CA  . HIS L  2 30  ? -19.305 -59.374  14.208  1.000 48.555  0 30  HIS LLL CA  1 ? 45 
ATOM   14508 C C   . HIS L  2 30  ? -20.164 -58.412  13.366  1.000 49.158  0 30  HIS LLL C   1 ? 45 
ATOM   14509 O O   . HIS L  2 30  ? -19.701 -58.012  12.287  1.000 48.350  0 30  HIS LLL O   1 ? 45 
ATOM   14510 C CB  . HIS L  2 30  ? -19.314 -60.796  13.628  1.000 51.078  0 30  HIS LLL CB  1 ? 45 
ATOM   14511 C CG  . HIS L  2 30  ? -20.687 -61.330  13.507  1.000 56.135  0 30  HIS LLL CG  1 ? 45 
ATOM   14512 N ND1 . HIS L  2 30  ? -21.378 -61.883  14.583  1.000 60.326  0 30  HIS LLL ND1 1 ? 45 
ATOM   14513 C CD2 . HIS L  2 30  ? -21.559 -61.274  12.481  1.000 60.462  0 30  HIS LLL CD2 1 ? 45 
ATOM   14514 C CE1 . HIS L  2 30  ? -22.597 -62.213  14.200  1.000 62.271  0 30  HIS LLL CE1 1 ? 45 
ATOM   14515 N NE2 . HIS L  2 30  ? -22.731 -61.842  12.915  1.000 63.021  0 30  HIS LLL NE2 1 ? 45 
ATOM   14516 N N   . SER L  2 31  ? -21.354 -58.024  13.811  1.000 48.375  0 31  SER LLL N   1 ? 45 
ATOM   14517 C CA  . SER L  2 31  ? -22.225 -57.049  13.081  1.000 48.943  0 31  SER LLL CA  1 ? 45 
ATOM   14518 C C   . SER L  2 31  ? -21.804 -55.599  13.346  1.000 44.275  0 31  SER LLL C   1 ? 45 
ATOM   14519 O O   . SER L  2 31  ? -22.408 -54.711  12.737  1.000 43.585  0 31  SER LLL O   1 ? 45 
ATOM   14520 C CB  . SER L  2 31  ? -23.696 -57.207  13.449  1.000 50.208  0 31  SER LLL CB  1 ? 45 
ATOM   14521 O OG  . SER L  2 31  ? -24.181 -58.501  13.206  1.000 58.386  0 31  SER LLL OG  1 ? 45 
ATOM   14522 N N   . TYR L  2 32  ? -20.858 -55.356  14.258  1.000 43.216  0 32  TYR LLL N   1 ? 45 
ATOM   14523 C CA  . TYR L  2 32  ? -20.541 -53.986  14.741  1.000 42.108  0 32  TYR LLL CA  1 ? 45 
ATOM   14524 C C   . TYR L  2 32  ? -19.203 -53.531  14.165  1.000 41.893  0 32  TYR LLL C   1 ? 45 
ATOM   14525 O O   . TYR L  2 32  ? -18.220 -54.275  14.215  1.000 42.043  0 32  TYR LLL O   1 ? 45 
ATOM   14526 C CB  . TYR L  2 32  ? -20.586 -53.891  16.271  1.000 40.835  0 32  TYR LLL CB  1 ? 45 
ATOM   14527 C CG  . TYR L  2 32  ? -21.997 -53.925  16.781  1.000 41.102  0 32  TYR LLL CG  1 ? 45 
ATOM   14528 C CD1 . TYR L  2 32  ? -22.654 -55.119  17.021  1.000 42.374  0 32  TYR LLL CD1 1 ? 45 
ATOM   14529 C CD2 . TYR L  2 32  ? -22.714 -52.754  16.925  1.000 41.794  0 32  TYR LLL CD2 1 ? 45 
ATOM   14530 C CE1 . TYR L  2 32  ? -23.973 -55.144  17.451  1.000 43.440  0 32  TYR LLL CE1 1 ? 45 
ATOM   14531 C CE2 . TYR L  2 32  ? -24.036 -52.759  17.343  1.000 42.812  0 32  TYR LLL CE2 1 ? 45 
ATOM   14532 C CZ  . TYR L  2 32  ? -24.673 -53.958  17.603  1.000 43.470  0 32  TYR LLL CZ  1 ? 45 
ATOM   14533 O OH  . TYR L  2 32  ? -25.985 -53.939  18.001  1.000 44.303  0 32  TYR LLL OH  1 ? 45 
ATOM   14534 N N   . VAL L  2 33  ? -19.210 -52.317  13.624  1.000 41.938  0 33  VAL LLL N   1 ? 45 
ATOM   14535 C CA  . VAL L  2 33  ? -17.996 -51.485  13.447  1.000 40.849  0 33  VAL LLL CA  1 ? 45 
ATOM   14536 C C   . VAL L  2 33  ? -17.585 -51.021  14.843  1.000 39.497  0 33  VAL LLL C   1 ? 45 
ATOM   14537 O O   . VAL L  2 33  ? -18.454 -50.474  15.566  1.000 38.602  0 33  VAL LLL O   1 ? 45 
ATOM   14538 C CB  . VAL L  2 33  ? -18.270 -50.298  12.505  1.000 41.486  0 33  VAL LLL CB  1 ? 45 
ATOM   14539 C CG1 . VAL L  2 33  ? -17.074 -49.359  12.420  1.000 41.191  0 33  VAL LLL CG1 1 ? 45 
ATOM   14540 C CG2 . VAL L  2 33  ? -18.673 -50.784  11.127  1.000 43.474  0 33  VAL LLL CG2 1 ? 45 
ATOM   14541 N N   . MET L  2 34  ? -16.328 -51.256  15.225  1.000 39.458  0 34  MET LLL N   1 ? 45 
ATOM   14542 C CA  . MET L  2 34  ? -15.811 -50.872  16.561  1.000 39.405  0 34  MET LLL CA  1 ? 45 
ATOM   14543 C C   . MET L  2 34  ? -14.830 -49.705  16.390  1.000 41.535  0 34  MET LLL C   1 ? 45 
ATOM   14544 O O   . MET L  2 34  ? -14.087 -49.658  15.381  1.000 39.786  0 34  MET LLL O   1 ? 45 
ATOM   14545 C CB  . MET L  2 34  ? -15.129 -52.061  17.250  1.000 39.195  0 34  MET LLL CB  1 ? 45 
ATOM   14546 C CG  . MET L  2 34  ? -16.055 -53.246  17.461  1.000 39.230  0 34  MET LLL CG  1 ? 45 
ATOM   14547 S SD  . MET L  2 34  ? -17.548 -52.810  18.408  1.000 39.863  0 34  MET LLL SD  1 ? 45 
ATOM   14548 C CE  . MET L  2 34  ? -16.834 -52.408  19.999  1.000 38.388  0 34  MET LLL CE  1 ? 45 
ATOM   14549 N N   . ALA L  2 35  ? -14.835 -48.776  17.346  1.000 43.285  0 35  ALA LLL N   1 ? 45 
ATOM   14550 C CA  . ALA L  2 35  ? -14.003 -47.557  17.268  1.000 41.563  0 35  ALA LLL CA  1 ? 45 
ATOM   14551 C C   . ALA L  2 35  ? -13.482 -47.156  18.645  1.000 39.447  0 35  ALA LLL C   1 ? 45 
ATOM   14552 O O   . ALA L  2 35  ? -14.080 -47.535  19.679  1.000 37.978  0 35  ALA LLL O   1 ? 45 
ATOM   14553 C CB  . ALA L  2 35  ? -14.798 -46.446  16.640  1.000 41.993  0 35  ALA LLL CB  1 ? 45 
ATOM   14554 N N   . TRP L  2 36  ? -12.388 -46.398  18.610  1.000 39.944  0 36  TRP LLL N   1 ? 45 
ATOM   14555 C CA  . TRP L  2 36  ? -11.768 -45.697  19.757  1.000 38.915  0 36  TRP LLL CA  1 ? 45 
ATOM   14556 C C   . TRP L  2 36  ? -11.779 -44.201  19.484  1.000 39.103  0 36  TRP LLL C   1 ? 45 
ATOM   14557 O O   . TRP L  2 36  ? -11.388 -43.794  18.402  1.000 39.880  0 36  TRP LLL O   1 ? 45 
ATOM   14558 C CB  . TRP L  2 36  ? -10.348 -46.209  19.989  1.000 39.079  0 36  TRP LLL CB  1 ? 45 
ATOM   14559 C CG  . TRP L  2 36  ? -10.302 -47.599  20.522  1.000 37.659  0 36  TRP LLL CG  1 ? 45 
ATOM   14560 C CD1 . TRP L  2 36  ? -10.116 -48.743  19.809  1.000 38.626  0 36  TRP LLL CD1 1 ? 45 
ATOM   14561 C CD2 . TRP L  2 36  ? -10.461 -47.998  21.886  1.000 36.970  0 36  TRP LLL CD2 1 ? 45 
ATOM   14562 N NE1 . TRP L  2 36  ? -10.137 -49.823  20.644  1.000 36.145  0 36  TRP LLL NE1 1 ? 45 
ATOM   14563 C CE2 . TRP L  2 36  ? -10.337 -49.397  21.922  1.000 36.153  0 36  TRP LLL CE2 1 ? 45 
ATOM   14564 C CE3 . TRP L  2 36  ? -10.653 -47.310  23.086  1.000 37.116  0 36  TRP LLL CE3 1 ? 45 
ATOM   14565 C CZ2 . TRP L  2 36  ? -10.400 -50.116  23.111  1.000 37.117  0 36  TRP LLL CZ2 1 ? 45 
ATOM   14566 C CZ3 . TRP L  2 36  ? -10.713 -48.019  24.264  1.000 36.534  0 36  TRP LLL CZ3 1 ? 45 
ATOM   14567 C CH2 . TRP L  2 36  ? -10.599 -49.410  24.273  1.000 36.837  0 36  TRP LLL CH2 1 ? 45 
ATOM   14568 N N   . PHE L  2 37  ? -12.245 -43.435  20.461  1.000 40.406  0 37  PHE LLL N   1 ? 45 
ATOM   14569 C CA  . PHE L  2 37  ? -12.114 -41.969  20.522  1.000 40.444  0 37  PHE LLL CA  1 ? 45 
ATOM   14570 C C   . PHE L  2 37  ? -11.380 -41.636  21.812  1.000 42.555  0 37  PHE LLL C   1 ? 45 
ATOM   14571 O O   . PHE L  2 37  ? -11.305 -42.513  22.691  1.000 45.812  0 37  PHE LLL O   1 ? 45 
ATOM   14572 C CB  . PHE L  2 37  ? -13.492 -41.313  20.510  1.000 39.539  0 37  PHE LLL CB  1 ? 45 
ATOM   14573 C CG  . PHE L  2 37  ? -14.196 -41.340  19.181  1.000 39.310  0 37  PHE LLL CG  1 ? 45 
ATOM   14574 C CD1 . PHE L  2 37  ? -14.764 -42.514  18.704  1.000 37.493  0 37  PHE LLL CD1 1 ? 45 
ATOM   14575 C CD2 . PHE L  2 37  ? -14.310 -40.190  18.422  1.000 39.781  0 37  PHE LLL CD2 1 ? 45 
ATOM   14576 C CE1 . PHE L  2 37  ? -15.430 -42.524  17.496  1.000 37.534  0 37  PHE LLL CE1 1 ? 45 
ATOM   14577 C CE2 . PHE L  2 37  ? -14.971 -40.207  17.212  1.000 39.039  0 37  PHE LLL CE2 1 ? 45 
ATOM   14578 C CZ  . PHE L  2 37  ? -15.522 -41.371  16.751  1.000 38.219  0 37  PHE LLL CZ  1 ? 45 
ATOM   14579 N N   . ARG L  2 38  ? -10.875 -40.411  21.928  1.000 41.560  0 38  ARG LLL N   1 ? 45 
ATOM   14580 C CA  . ARG L  2 38  ? -10.291 -39.945  23.197  1.000 43.528  0 38  ARG LLL CA  1 ? 45 
ATOM   14581 C C   . ARG L  2 38  ? -10.683 -38.488  23.439  1.000 45.075  0 38  ARG LLL C   1 ? 45 
ATOM   14582 O O   . ARG L  2 38  ? -11.051 -37.760  22.488  1.000 43.544  0 38  ARG LLL O   1 ? 45 
ATOM   14583 C CB  . ARG L  2 38  ? -8.773  -40.120  23.172  1.000 46.196  0 38  ARG LLL CB  1 ? 45 
ATOM   14584 C CG  . ARG L  2 38  ? -8.056  -39.134  22.258  1.000 48.173  0 38  ARG LLL CG  1 ? 45 
ATOM   14585 C CD  . ARG L  2 38  ? -6.623  -39.566  22.031  1.000 49.096  0 38  ARG LLL CD  1 ? 45 
ATOM   14586 N NE  . ARG L  2 38  ? -5.950  -38.692  21.087  1.000 51.142  0 38  ARG LLL NE  1 ? 45 
ATOM   14587 C CZ  . ARG L  2 38  ? -4.665  -38.782  20.765  1.000 53.147  0 38  ARG LLL CZ  1 ? 45 
ATOM   14588 N NH1 . ARG L  2 38  ? -3.881  -39.694  21.315  1.000 53.409  0 38  ARG LLL NH1 1 ? 45 
ATOM   14589 N NH2 . ARG L  2 38  ? -4.152  -37.948  19.892  1.000 55.565  0 38  ARG LLL NH2 1 ? 45 
ATOM   14590 N N   . GLN L  2 39  ? -10.597 -38.081  24.694  1.000 45.602  0 39  GLN LLL N   1 ? 45 
ATOM   14591 C CA  . GLN L  2 39  ? -10.981 -36.718  25.098  1.000 49.408  0 39  GLN LLL CA  1 ? 45 
ATOM   14592 C C   . GLN L  2 39  ? -10.063 -36.285  26.233  1.000 51.268  0 39  GLN LLL C   1 ? 45 
ATOM   14593 O O   . GLN L  2 39  ? -10.091 -36.924  27.281  1.000 53.743  0 39  GLN LLL O   1 ? 45 
ATOM   14594 C CB  . GLN L  2 39  ? -12.452 -36.683  25.501  1.000 49.602  0 39  GLN LLL CB  1 ? 45 
ATOM   14595 C CG  . GLN L  2 39  ? -12.912 -35.307  25.892  1.000 53.482  0 39  GLN LLL CG  1 ? 45 
ATOM   14596 C CD  . GLN L  2 39  ? -14.414 -35.226  25.965  1.000 53.868  0 39  GLN LLL CD  1 ? 45 
ATOM   14597 O OE1 . GLN L  2 39  ? -15.083 -36.177  26.348  1.000 57.430  0 39  GLN LLL OE1 1 ? 45 
ATOM   14598 N NE2 . GLN L  2 39  ? -14.944 -34.058  25.646  1.000 55.241  0 39  GLN LLL NE2 1 ? 45 
ATOM   14599 N N   . ALA L  2 40  ? -9.249  -35.269  26.001  1.000 53.187  0 40  ALA LLL N   1 ? 45 
ATOM   14600 C CA  . ALA L  2 40  ? -8.499  -34.543  27.050  1.000 55.975  0 40  ALA LLL CA  1 ? 45 
ATOM   14601 C C   . ALA L  2 40  ? -9.452  -33.528  27.674  1.000 58.408  0 40  ALA LLL C   1 ? 45 
ATOM   14602 O O   . ALA L  2 40  ? -10.376 -33.067  27.011  1.000 59.580  0 40  ALA LLL O   1 ? 45 
ATOM   14603 C CB  . ALA L  2 40  ? -7.280  -33.883  26.465  1.000 57.940  0 40  ALA LLL CB  1 ? 45 
ATOM   14604 N N   . PRO L  2 41  ? -9.300  -33.199  28.971  1.000 60.494  0 41  PRO LLL N   1 ? 45 
ATOM   14605 C CA  . PRO L  2 41  ? -10.224 -32.269  29.621  1.000 63.347  0 41  PRO LLL CA  1 ? 45 
ATOM   14606 C C   . PRO L  2 41  ? -10.170 -30.889  28.942  1.000 68.319  0 41  PRO LLL C   1 ? 45 
ATOM   14607 O O   . PRO L  2 41  ? -9.087  -30.405  28.638  1.000 68.255  0 41  PRO LLL O   1 ? 45 
ATOM   14608 C CB  . PRO L  2 41  ? -9.807  -32.202  31.096  1.000 63.563  0 41  PRO LLL CB  1 ? 45 
ATOM   14609 C CG  . PRO L  2 41  ? -8.545  -33.027  31.191  1.000 62.429  0 41  PRO LLL CG  1 ? 45 
ATOM   14610 C CD  . PRO L  2 41  ? -8.257  -33.715  29.868  1.000 60.194  0 41  PRO LLL CD  1 ? 45 
ATOM   14611 N N   . GLY L  2 42  ? -11.342 -30.320  28.645  1.000 71.985  0 42  GLY LLL N   1 ? 45 
ATOM   14612 C CA  . GLY L  2 42  ? -11.464 -29.009  27.980  1.000 76.298  0 42  GLY LLL CA  1 ? 45 
ATOM   14613 C C   . GLY L  2 42  ? -11.473 -29.119  26.464  1.000 77.978  0 42  GLY LLL C   1 ? 45 
ATOM   14614 O O   . GLY L  2 42  ? -11.827 -28.109  25.817  1.000 83.517  0 42  GLY LLL O   1 ? 45 
ATOM   14615 N N   . LYS L  2 43  ? -11.190 -30.298  25.892  1.000 74.686  0 43  LYS LLL N   1 ? 45 
ATOM   14616 C CA  . LYS L  2 43  ? -11.134 -30.492  24.415  1.000 74.411  0 43  LYS LLL CA  1 ? 45 
ATOM   14617 C C   . LYS L  2 43  ? -12.275 -31.390  23.949  1.000 70.730  0 43  LYS LLL C   1 ? 45 
ATOM   14618 O O   . LYS L  2 43  ? -12.905 -32.004  24.820  1.000 70.328  0 43  LYS LLL O   1 ? 45 
ATOM   14619 C CB  . LYS L  2 43  ? -9.811  -31.134  24.007  1.000 75.705  0 43  LYS LLL CB  1 ? 45 
ATOM   14620 C CG  . LYS L  2 43  ? -8.625  -30.190  23.942  1.000 80.856  0 43  LYS LLL CG  1 ? 45 
ATOM   14621 C CD  . LYS L  2 43  ? -7.320  -30.915  23.759  1.000 83.476  0 43  LYS LLL CD  1 ? 45 
ATOM   14622 C CE  . LYS L  2 43  ? -6.140  -29.976  23.883  1.000 89.522  0 43  LYS LLL CE  1 ? 45 
ATOM   14623 N NZ  . LYS L  2 43  ? -5.093  -30.563  24.750  1.000 91.016  0 43  LYS LLL NZ  1 ? 45 
ATOM   14624 N N   . GLU L  2 44  ? -12.521 -31.469  22.645  1.000 69.490  0 44  GLU LLL N   1 ? 45 
ATOM   14625 C CA  . GLU L  2 44  ? -13.660 -32.251  22.093  1.000 67.636  0 44  GLU LLL CA  1 ? 45 
ATOM   14626 C C   . GLU L  2 44  ? -13.207 -33.710  21.966  1.000 59.841  0 44  GLU LLL C   1 ? 45 
ATOM   14627 O O   . GLU L  2 44  ? -11.998 -33.946  22.046  1.000 55.318  0 44  GLU LLL O   1 ? 45 
ATOM   14628 C CB  . GLU L  2 44  ? -14.091 -31.714  20.722  1.000 72.964  0 44  GLU LLL CB  1 ? 45 
ATOM   14629 C CG  . GLU L  2 44  ? -14.219 -30.199  20.637  1.000 80.817  0 44  GLU LLL CG  1 ? 45 
ATOM   14630 C CD  . GLU L  2 44  ? -15.240 -29.596  21.592  1.000 87.694  0 44  GLU LLL CD  1 ? 45 
ATOM   14631 O OE1 . GLU L  2 44  ? -16.296 -30.253  21.816  1.000 88.023  0 44  GLU LLL OE1 1 ? 45 
ATOM   14632 O OE2 . GLU L  2 44  ? -14.983 -28.467  22.115  1.000 91.628  0 44  GLU LLL OE2 1 ? 45 
ATOM   14633 N N   . ARG L  2 45  ? -14.153 -34.635  21.799  1.000 58.582  0 45  ARG LLL N   1 ? 45 
ATOM   14634 C CA  . ARG L  2 45  ? -13.866 -36.046  21.453  1.000 57.430  0 45  ARG LLL CA  1 ? 45 
ATOM   14635 C C   . ARG L  2 45  ? -13.137 -36.064  20.106  1.000 55.756  0 45  ARG LLL C   1 ? 45 
ATOM   14636 O O   . ARG L  2 45  ? -13.677 -35.535  19.137  1.000 56.159  0 45  ARG LLL O   1 ? 45 
ATOM   14637 C CB  . ARG L  2 45  ? -15.137 -36.893  21.392  1.000 57.097  0 45  ARG LLL CB  1 ? 45 
ATOM   14638 C CG  . ARG L  2 45  ? -15.334 -37.707  22.652  1.000 61.275  0 45  ARG LLL CG  1 ? 45 
ATOM   14639 C CD  . ARG L  2 45  ? -16.733 -38.229  22.856  1.000 65.691  0 45  ARG LLL CD  1 ? 45 
ATOM   14640 N NE  . ARG L  2 45  ? -17.106 -38.188  24.266  1.000 68.322  0 45  ARG LLL NE  1 ? 45 
ATOM   14641 C CZ  . ARG L  2 45  ? -17.964 -39.006  24.863  1.000 71.820  0 45  ARG LLL CZ  1 ? 45 
ATOM   14642 N NH1 . ARG L  2 45  ? -18.543 -40.003  24.216  1.000 73.478  0 45  ARG LLL NH1 1 ? 45 
ATOM   14643 N NH2 . ARG L  2 45  ? -18.238 -38.840  26.140  1.000 74.381  0 45  ARG LLL NH2 1 ? 45 
ATOM   14644 N N   . GLU L  2 46  ? -11.964 -36.672  20.087  1.000 54.762  0 46  GLU LLL N   1 ? 45 
ATOM   14645 C CA  . GLU L  2 46  ? -11.085 -36.807  18.906  1.000 54.054  0 46  GLU LLL CA  1 ? 45 
ATOM   14646 C C   . GLU L  2 46  ? -11.134 -38.278  18.468  1.000 47.811  0 46  GLU LLL C   1 ? 45 
ATOM   14647 O O   . GLU L  2 46  ? -11.000 -39.183  19.326  1.000 43.388  0 46  GLU LLL O   1 ? 45 
ATOM   14648 C CB  . GLU L  2 46  ? -9.720  -36.270  19.336  1.000 58.355  0 46  GLU LLL CB  1 ? 45 
ATOM   14649 C CG  . GLU L  2 46  ? -8.618  -36.429  18.317  1.000 64.342  0 46  GLU LLL CG  1 ? 45 
ATOM   14650 C CD  . GLU L  2 46  ? -7.245  -35.987  18.809  1.000 69.819  0 46  GLU LLL CD  1 ? 45 
ATOM   14651 O OE1 . GLU L  2 46  ? -7.127  -35.452  19.956  1.000 73.678  0 46  GLU LLL OE1 1 ? 45 
ATOM   14652 O OE2 . GLU L  2 46  ? -6.284  -36.208  18.061  1.000 73.348  0 46  GLU LLL OE2 1 ? 45 
ATOM   14653 N N   . PHE L  2 47  ? -11.370 -38.525  17.186  1.000 45.930  0 47  PHE LLL N   1 ? 45 
ATOM   14654 C CA  . PHE L  2 47  ? -11.314 -39.892  16.602  1.000 44.542  0 47  PHE LLL CA  1 ? 45 
ATOM   14655 C C   . PHE L  2 47  ? -9.888  -40.429  16.705  1.000 44.096  0 47  PHE LLL C   1 ? 45 
ATOM   14656 O O   . PHE L  2 47  ? -8.953  -39.711  16.351  1.000 44.609  0 47  PHE LLL O   1 ? 45 
ATOM   14657 C CB  . PHE L  2 47  ? -11.763 -39.897  15.144  1.000 43.976  0 47  PHE LLL CB  1 ? 45 
ATOM   14658 C CG  . PHE L  2 47  ? -11.613 -41.230  14.463  1.000 43.082  0 47  PHE LLL CG  1 ? 45 
ATOM   14659 C CD1 . PHE L  2 47  ? -12.549 -42.232  14.622  1.000 41.488  0 47  PHE LLL CD1 1 ? 45 
ATOM   14660 C CD2 . PHE L  2 47  ? -10.536 -41.472  13.641  1.000 43.730  0 47  PHE LLL CD2 1 ? 45 
ATOM   14661 C CE1 . PHE L  2 47  ? -12.404 -43.444  13.970  1.000 41.715  0 47  PHE LLL CE1 1 ? 45 
ATOM   14662 C CE2 . PHE L  2 47  ? -10.391 -42.691  12.991  1.000 42.988  0 47  PHE LLL CE2 1 ? 45 
ATOM   14663 C CZ  . PHE L  2 47  ? -11.325 -43.675  13.157  1.000 41.229  0 47  PHE LLL CZ  1 ? 45 
ATOM   14664 N N   . VAL L  2 48  ? -9.741  -41.677  17.135  1.000 43.899  0 48  VAL LLL N   1 ? 45 
ATOM   14665 C CA  . VAL L  2 48  ? -8.421  -42.365  17.232  1.000 44.192  0 48  VAL LLL CA  1 ? 45 
ATOM   14666 C C   . VAL L  2 48  ? -8.326  -43.464  16.167  1.000 43.645  0 48  VAL LLL C   1 ? 45 
ATOM   14667 O O   . VAL L  2 48  ? -7.352  -43.451  15.388  1.000 45.170  0 48  VAL LLL O   1 ? 45 
ATOM   14668 C CB  . VAL L  2 48  ? -8.185  -42.896  18.657  1.000 42.830  0 48  VAL LLL CB  1 ? 45 
ATOM   14669 C CG1 . VAL L  2 48  ? -6.911  -43.702  18.743  1.000 44.020  0 48  VAL LLL CG1 1 ? 45 
ATOM   14670 C CG2 . VAL L  2 48  ? -8.176  -41.759  19.681  1.000 43.703  0 48  VAL LLL CG2 1 ? 45 
ATOM   14671 N N   . ALA L  2 49  ? -9.275  -44.398  16.146  1.000 43.635  0 49  ALA LLL N   1 ? 45 
ATOM   14672 C CA  . ALA L  2 49  ? -9.224  -45.588  15.251  1.000 44.693  0 49  ALA LLL CA  1 ? 45 
ATOM   14673 C C   . ALA L  2 49  ? -10.589 -46.276  15.138  1.000 41.945  0 49  ALA LLL C   1 ? 45 
ATOM   14674 O O   . ALA L  2 49  ? -11.433 -46.130  16.039  1.000 40.107  0 49  ALA LLL O   1 ? 45 
ATOM   14675 C CB  . ALA L  2 49  ? -8.171  -46.565  15.737  1.000 44.982  0 49  ALA LLL CB  1 ? 45 
ATOM   14676 N N   . ALA L  2 50  ? -10.779 -47.000  14.044  1.000 42.513  0 50  ALA LLL N   1 ? 45 
ATOM   14677 C CA  . ALA L  2 50  ? -11.996 -47.791  13.769  1.000 42.991  0 50  ALA LLL CA  1 ? 45 
ATOM   14678 C C   . ALA L  2 50  ? -11.641 -48.999  12.904  1.000 44.039  0 50  ALA LLL C   1 ? 45 
ATOM   14679 O O   . ALA L  2 50  ? -10.668 -48.942  12.133  1.000 45.219  0 50  ALA LLL O   1 ? 45 
ATOM   14680 C CB  . ALA L  2 50  ? -13.046 -46.942  13.107  1.000 42.754  0 50  ALA LLL CB  1 ? 45 
ATOM   14681 N N   . ILE L  2 51  ? -12.436 -50.054  13.043  1.000 43.428  0 51  ILE LLL N   1 ? 45 
ATOM   14682 C CA  . ILE L  2 51  ? -12.233 -51.349  12.347  1.000 42.655  0 51  ILE LLL CA  1 ? 45 
ATOM   14683 C C   . ILE L  2 51  ? -13.594 -51.863  11.872  1.000 41.621  0 51  ILE LLL C   1 ? 45 
ATOM   14684 O O   . ILE L  2 51  ? -14.563 -51.914  12.667  1.000 40.154  0 51  ILE LLL O   1 ? 45 
ATOM   14685 C CB  . ILE L  2 51  ? -11.477 -52.329  13.263  1.000 42.033  0 51  ILE LLL CB  1 ? 45 
ATOM   14686 C CG1 . ILE L  2 51  ? -11.088 -53.613  12.520  1.000 44.048  0 51  ILE LLL CG1 1 ? 45 
ATOM   14687 C CG2 . ILE L  2 51  ? -12.255 -52.628  14.534  1.000 39.735  0 51  ILE LLL CG2 1 ? 45 
ATOM   14688 C CD1 . ILE L  2 51  ? -10.055 -54.452  13.249  1.000 44.985  0 51  ILE LLL CD1 1 ? 45 
ATOM   14689 N N   . SER L  2 52  ? -13.663 -52.202  10.585  1.000 45.500  0 52  SER LLL N   1 ? 45 
ATOM   14690 C CA  . SER L  2 52  ? -14.903 -52.707  9.942   1.000 46.745  0 52  SER LLL CA  1 ? 45 
ATOM   14691 C C   . SER L  2 52  ? -15.122 -54.159  10.370  1.000 45.313  0 52  SER LLL C   1 ? 45 
ATOM   14692 O O   . SER L  2 52  ? -14.271 -54.725  11.091  1.000 47.004  0 52  SER LLL O   1 ? 45 
ATOM   14693 C CB  . SER L  2 52  ? -14.871 -52.545  8.480   1.000 48.264  0 52  SER LLL CB  1 ? 45 
ATOM   14694 O OG  . SER L  2 52  ? -16.191 -52.550  7.992   1.000 51.875  0 52  SER LLL OG  1 ? 45 
ATOM   14695 N N   . TRP L  2 53  ? -16.263 -54.710  9.977   1.000 44.951  0 53  TRP LLL N   1 ? 45 
ATOM   14696 C CA  . TRP L  2 53  ? -16.762 -56.050  10.396  1.000 46.040  0 53  TRP LLL CA  1 ? 45 
ATOM   14697 C C   . TRP L  2 53  ? -15.693 -57.126  10.121  1.000 47.520  0 53  TRP LLL C   1 ? 45 
ATOM   14698 O O   . TRP L  2 53  ? -15.345 -57.853  11.042  1.000 45.791  0 53  TRP LLL O   1 ? 45 
ATOM   14699 C CB  . TRP L  2 53  ? -18.071 -56.357  9.664   1.000 45.434  0 53  TRP LLL CB  1 ? 45 
ATOM   14700 C CG  . TRP L  2 53  ? -19.057 -55.234  9.685   1.000 44.198  0 53  TRP LLL CG  1 ? 45 
ATOM   14701 C CD1 . TRP L  2 53  ? -19.833 -54.857  10.735  1.000 42.698  0 53  TRP LLL CD1 1 ? 45 
ATOM   14702 C CD2 . TRP L  2 53  ? -19.383 -54.345  8.605   1.000 44.154  0 53  TRP LLL CD2 1 ? 45 
ATOM   14703 N NE1 . TRP L  2 53  ? -20.601 -53.781  10.395  1.000 42.313  0 53  TRP LLL NE1 1 ? 45 
ATOM   14704 C CE2 . TRP L  2 53  ? -20.362 -53.449  9.091   1.000 43.186  0 53  TRP LLL CE2 1 ? 45 
ATOM   14705 C CE3 . TRP L  2 53  ? -18.922 -54.199  7.293   1.000 44.568  0 53  TRP LLL CE3 1 ? 45 
ATOM   14706 C CZ2 . TRP L  2 53  ? -20.904 -52.432  8.305   1.000 43.984  0 53  TRP LLL CZ2 1 ? 45 
ATOM   14707 C CZ3 . TRP L  2 53  ? -19.470 -53.208  6.506   1.000 46.977  0 53  TRP LLL CZ3 1 ? 45 
ATOM   14708 C CH2 . TRP L  2 53  ? -20.457 -52.341  7.003   1.000 46.619  0 53  TRP LLL CH2 1 ? 45 
ATOM   14709 N N   . SER L  2 54  ? -15.178 -57.177  8.890   1.000 49.695  0 54  SER LLL N   1 ? 45 
ATOM   14710 C CA  . SER L  2 54  ? -14.203 -58.182  8.392   1.000 51.851  0 54  SER LLL CA  1 ? 45 
ATOM   14711 C C   . SER L  2 54  ? -12.800 -57.909  8.952   1.000 50.970  0 54  SER LLL C   1 ? 45 
ATOM   14712 O O   . SER L  2 54  ? -11.900 -58.677  8.630   1.000 52.327  0 54  SER LLL O   1 ? 45 
ATOM   14713 C CB  . SER L  2 54  ? -14.146 -58.144  6.901   1.000 53.410  0 54  SER LLL CB  1 ? 45 
ATOM   14714 O OG  . SER L  2 54  ? -13.597 -56.891  6.502   1.000 55.157  0 54  SER LLL OG  1 ? 45 
ATOM   14715 N N   . SER L  2 55  ? -12.612 -56.806  9.670   1.000 49.493  0 55  SER LLL N   1 ? 45 
ATOM   14716 C CA  . SER L  2 55  ? -11.302 -56.224  10.082  1.000 50.614  0 55  SER LLL CA  1 ? 45 
ATOM   14717 C C   . SER L  2 55  ? -10.671 -55.387  8.953   1.000 55.380  0 55  SER LLL C   1 ? 45 
ATOM   14718 O O   . SER L  2 55  ? -9.589  -54.839  9.224   1.000 52.686  0 55  SER LLL O   1 ? 45 
ATOM   14719 C CB  . SER L  2 55  ? -10.322 -57.268  10.562  1.000 49.287  0 55  SER LLL CB  1 ? 45 
ATOM   14720 O OG  . SER L  2 55  ? -10.796 -57.978  11.686  1.000 45.494  0 55  SER LLL OG  1 ? 45 
ATOM   14721 N N   . THR L  2 56  ? -11.280 -55.264  7.761   1.000 63.144  0 56  THR LLL N   1 ? 45 
ATOM   14722 C CA  . THR L  2 56  ? -10.463 -55.116  6.522   1.000 72.760  0 56  THR LLL CA  1 ? 45 
ATOM   14723 C C   . THR L  2 56  ? -10.269 -53.681  6.068   1.000 74.153  0 56  THR LLL C   1 ? 45 
ATOM   14724 O O   . THR L  2 56  ? -9.254  -53.426  5.406   1.000 88.135  0 56  THR LLL O   1 ? 45 
ATOM   14725 C CB  . THR L  2 56  ? -10.977 -55.914  5.324   1.000 78.851  0 56  THR LLL CB  1 ? 45 
ATOM   14726 O OG1 . THR L  2 56  ? -10.345 -57.185  5.492   1.000 83.066  0 56  THR LLL OG1 1 ? 45 
ATOM   14727 C CG2 . THR L  2 56  ? -10.621 -55.326  3.972   1.000 80.857  0 56  THR LLL CG2 1 ? 45 
ATOM   14728 N N   . PRO L  2 57  ? -11.244 -52.757  6.222   1.000 61.757  0 57  PRO LLL N   1 ? 45 
ATOM   14729 C CA  . PRO L  2 57  ? -10.874 -51.339  6.309   1.000 54.983  0 57  PRO LLL CA  1 ? 45 
ATOM   14730 C C   . PRO L  2 57  ? -10.603 -51.109  7.809   1.000 51.424  0 57  PRO LLL C   1 ? 45 
ATOM   14731 O O   . PRO L  2 57  ? -11.446 -51.432  8.630   1.000 47.365  0 57  PRO LLL O   1 ? 45 
ATOM   14732 C CB  . PRO L  2 57  ? -12.045 -50.569  5.679   1.000 53.305  0 57  PRO LLL CB  1 ? 45 
ATOM   14733 C CG  . PRO L  2 57  ? -13.107 -51.665  5.399   1.000 55.703  0 57  PRO LLL CG  1 ? 45 
ATOM   14734 C CD  . PRO L  2 57  ? -12.683 -52.983  6.058   1.000 55.893  0 57  PRO LLL CD  1 ? 45 
ATOM   14735 N N   . THR L  2 58  ? -9.388  -50.670  8.147   1.000 49.134  0 58  THR LLL N   1 ? 45 
ATOM   14736 C CA  . THR L  2 58  ? -9.069  -49.993  9.425   1.000 45.486  0 58  THR LLL CA  1 ? 45 
ATOM   14737 C C   . THR L  2 58  ? -8.864  -48.510  9.140   1.000 45.951  0 58  THR LLL C   1 ? 45 
ATOM   14738 O O   . THR L  2 58  ? -8.502  -48.168  8.023   1.000 47.850  0 58  THR LLL O   1 ? 45 
ATOM   14739 C CB  . THR L  2 58  ? -7.856  -50.568  10.174  1.000 45.624  0 58  THR LLL CB  1 ? 45 
ATOM   14740 O OG1 . THR L  2 58  ? -6.687  -50.469  9.353   1.000 47.766  0 58  THR LLL OG1 1 ? 45 
ATOM   14741 C CG2 . THR L  2 58  ? -8.120  -51.977  10.670  1.000 43.948  0 58  THR LLL CG2 1 ? 45 
ATOM   14742 N N   . TYR L  2 59  ? -9.121  -47.670  10.137  1.000 44.376  0 59  TYR LLL N   1 ? 45 
ATOM   14743 C CA  . TYR L  2 59  ? -8.986  -46.203  10.027  1.000 45.199  0 59  TYR LLL CA  1 ? 45 
ATOM   14744 C C   . TYR L  2 59  ? -8.253  -45.689  11.263  1.000 43.814  0 59  TYR LLL C   1 ? 45 
ATOM   14745 O O   . TYR L  2 59  ? -8.442  -46.265  12.354  1.000 41.483  0 59  TYR LLL O   1 ? 45 
ATOM   14746 C CB  . TYR L  2 59  ? -10.349 -45.535  9.924   1.000 44.796  0 59  TYR LLL CB  1 ? 45 
ATOM   14747 C CG  . TYR L  2 59  ? -11.276 -45.992  8.833   1.000 46.367  0 59  TYR LLL CG  1 ? 45 
ATOM   14748 C CD1 . TYR L  2 59  ? -12.232 -46.959  9.097   1.000 45.596  0 59  TYR LLL CD1 1 ? 45 
ATOM   14749 C CD2 . TYR L  2 59  ? -11.300 -45.374  7.592   1.000 48.267  0 59  TYR LLL CD2 1 ? 45 
ATOM   14750 C CE1 . TYR L  2 59  ? -13.169 -47.334  8.140   1.000 46.725  0 59  TYR LLL CE1 1 ? 45 
ATOM   14751 C CE2 . TYR L  2 59  ? -12.223 -45.745  6.623   1.000 49.914  0 59  TYR LLL CE2 1 ? 45 
ATOM   14752 C CZ  . TYR L  2 59  ? -13.155 -46.737  6.895   1.000 49.274  0 59  TYR LLL CZ  1 ? 45 
ATOM   14753 O OH  . TYR L  2 59  ? -14.052 -47.130  5.947   1.000 51.733  0 59  TYR LLL OH  1 ? 45 
ATOM   14754 N N   . TYR L  2 60  ? -7.485  -44.610  11.088  1.000 44.871  0 60  TYR LLL N   1 ? 45 
ATOM   14755 C CA  . TYR L  2 60  ? -6.647  -43.990  12.139  1.000 44.786  0 60  TYR LLL CA  1 ? 45 
ATOM   14756 C C   . TYR L  2 60  ? -6.735  -42.474  12.022  1.000 45.576  0 60  TYR LLL C   1 ? 45 
ATOM   14757 O O   . TYR L  2 60  ? -6.734  -41.943  10.881  1.000 44.861  0 60  TYR LLL O   1 ? 45 
ATOM   14758 C CB  . TYR L  2 60  ? -5.212  -44.492  11.988  1.000 47.240  0 60  TYR LLL CB  1 ? 45 
ATOM   14759 C CG  . TYR L  2 60  ? -5.074  -45.971  12.243  1.000 46.706  0 60  TYR LLL CG  1 ? 45 
ATOM   14760 C CD1 . TYR L  2 60  ? -5.149  -46.472  13.539  1.000 43.912  0 60  TYR LLL CD1 1 ? 45 
ATOM   14761 C CD2 . TYR L  2 60  ? -4.931  -46.868  11.193  1.000 46.294  0 60  TYR LLL CD2 1 ? 45 
ATOM   14762 C CE1 . TYR L  2 60  ? -5.034  -47.830  13.780  1.000 44.780  0 60  TYR LLL CE1 1 ? 45 
ATOM   14763 C CE2 . TYR L  2 60  ? -4.813  -48.227  11.424  1.000 46.972  0 60  TYR LLL CE2 1 ? 45 
ATOM   14764 C CZ  . TYR L  2 60  ? -4.862  -48.710  12.720  1.000 46.230  0 60  TYR LLL CZ  1 ? 45 
ATOM   14765 O OH  . TYR L  2 60  ? -4.765  -50.045  12.975  1.000 48.155  0 60  TYR LLL OH  1 ? 45 
ATOM   14766 N N   . GLY L  2 61  ? -6.785  -41.792  13.167  1.000 45.854  0 61  GLY LLL N   1 ? 45 
ATOM   14767 C CA  . GLY L  2 61  ? -6.578  -40.332  13.225  1.000 48.988  0 61  GLY LLL CA  1 ? 45 
ATOM   14768 C C   . GLY L  2 61  ? -5.172  -39.973  12.793  1.000 53.459  0 61  GLY LLL C   1 ? 45 
ATOM   14769 O O   . GLY L  2 61  ? -4.273  -40.781  13.012  1.000 54.510  0 61  GLY LLL O   1 ? 45 
ATOM   14770 N N   . GLU L  2 62  ? -4.990  -38.782  12.246  1.000 58.853  0 62  GLU LLL N   1 ? 45 
ATOM   14771 C CA  . GLU L  2 62  ? -3.703  -38.322  11.679  1.000 64.040  0 62  GLU LLL CA  1 ? 45 
ATOM   14772 C C   . GLU L  2 62  ? -2.604  -38.454  12.720  1.000 62.997  0 62  GLU LLL C   1 ? 45 
ATOM   14773 O O   . GLU L  2 62  ? -1.519  -38.948  12.353  1.000 66.178  0 62  GLU LLL O   1 ? 45 
ATOM   14774 C CB  . GLU L  2 62  ? -3.856  -36.902  11.138  1.000 72.546  0 62  GLU LLL CB  1 ? 45 
ATOM   14775 C CG  . GLU L  2 62  ? -4.599  -36.861  9.805   1.000 81.713  0 62  GLU LLL CG  1 ? 45 
ATOM   14776 C CD  . GLU L  2 62  ? -4.115  -37.865  8.754   1.000 87.282  0 62  GLU LLL CD  1 ? 45 
ATOM   14777 O OE1 . GLU L  2 62  ? -2.870  -38.016  8.656   1.000 88.279  0 62  GLU LLL OE1 1 ? 45 
ATOM   14778 O OE2 . GLU L  2 62  ? -4.978  -38.545  8.093   1.000 87.635  0 62  GLU LLL OE2 1 ? 45 
ATOM   14779 N N   . SER L  2 63  ? -2.876  -38.094  13.977  1.000 60.452  0 63  SER LLL N   1 ? 45 
ATOM   14780 C CA  . SER L  2 63  ? -1.803  -37.910  14.990  1.000 60.665  0 63  SER LLL CA  1 ? 45 
ATOM   14781 C C   . SER L  2 63  ? -1.394  -39.256  15.596  1.000 56.132  0 63  SER LLL C   1 ? 45 
ATOM   14782 O O   . SER L  2 63  ? -0.380  -39.286  16.271  1.000 54.826  0 63  SER LLL O   1 ? 45 
ATOM   14783 C CB  . SER L  2 63  ? -2.195  -36.915  16.041  1.000 61.651  0 63  SER LLL CB  1 ? 45 
ATOM   14784 O OG  . SER L  2 63  ? -3.327  -37.379  16.754  1.000 61.561  0 63  SER LLL OG  1 ? 45 
ATOM   14785 N N   . VAL L  2 64  ? -2.131  -40.337  15.343  1.000 53.549  0 64  VAL LLL N   1 ? 45 
ATOM   14786 C CA  . VAL L  2 64  ? -1.765  -41.677  15.897  1.000 52.649  0 64  VAL LLL CA  1 ? 45 
ATOM   14787 C C   . VAL L  2 64  ? -1.365  -42.634  14.774  1.000 54.206  0 64  VAL LLL C   1 ? 45 
ATOM   14788 O O   . VAL L  2 64  ? -0.834  -43.709  15.095  1.000 53.113  0 64  VAL LLL O   1 ? 45 
ATOM   14789 C CB  . VAL L  2 64  ? -2.884  -42.284  16.753  1.000 48.850  0 64  VAL LLL CB  1 ? 45 
ATOM   14790 C CG1 . VAL L  2 64  ? -3.284  -41.354  17.893  1.000 47.542  0 64  VAL LLL CG1 1 ? 45 
ATOM   14791 C CG2 . VAL L  2 64  ? -4.093  -42.672  15.926  1.000 46.917  0 64  VAL LLL CG2 1 ? 45 
ATOM   14792 N N   . LYS L  2 65  ? -1.587  -42.261  13.517  1.000 57.503  0 65  LYS LLL N   1 ? 45 
ATOM   14793 C CA  . LYS L  2 65  ? -1.214  -43.094  12.338  1.000 62.485  0 65  LYS LLL CA  1 ? 45 
ATOM   14794 C C   . LYS L  2 65  ? 0.252   -43.520  12.497  1.000 63.156  0 65  LYS LLL C   1 ? 45 
ATOM   14795 O O   . LYS L  2 65  ? 1.083   -42.657  12.806  1.000 64.382  0 65  LYS LLL O   1 ? 45 
ATOM   14796 C CB  . LYS L  2 65  ? -1.454  -42.340  11.027  1.000 69.462  0 65  LYS LLL CB  1 ? 45 
ATOM   14797 C CG  . LYS L  2 65  ? -2.081  -43.201  9.944   1.000 74.688  0 65  LYS LLL CG  1 ? 45 
ATOM   14798 C CD  . LYS L  2 65  ? -2.300  -42.465  8.640   1.000 80.497  0 65  LYS LLL CD  1 ? 45 
ATOM   14799 C CE  . LYS L  2 65  ? -2.376  -43.405  7.448   1.000 83.891  0 65  LYS LLL CE  1 ? 45 
ATOM   14800 N NZ  . LYS L  2 65  ? -1.672  -42.851  6.264   1.000 88.064  0 65  LYS LLL NZ  1 ? 45 
ATOM   14801 N N   . GLY L  2 66  ? 0.541   -44.814  12.354  1.000 62.770  0 66  GLY LLL N   1 ? 45 
ATOM   14802 C CA  . GLY L  2 66  ? 1.898   -45.390  12.473  1.000 64.773  0 66  GLY LLL CA  1 ? 45 
ATOM   14803 C C   . GLY L  2 66  ? 2.184   -45.924  13.872  1.000 64.511  0 66  GLY LLL C   1 ? 45 
ATOM   14804 O O   . GLY L  2 66  ? 2.957   -46.874  13.976  1.000 68.628  0 66  GLY LLL O   1 ? 45 
ATOM   14805 N N   . ARG L  2 67  ? 1.603   -45.332  14.923  1.000 60.255  0 67  ARG LLL N   1 ? 45 
ATOM   14806 C CA  . ARG L  2 67  ? 1.948   -45.644  16.333  1.000 57.649  0 67  ARG LLL CA  1 ? 45 
ATOM   14807 C C   . ARG L  2 67  ? 0.929   -46.613  16.944  1.000 54.317  0 67  ARG LLL C   1 ? 45 
ATOM   14808 O O   . ARG L  2 67  ? 1.311   -47.397  17.829  1.000 54.156  0 67  ARG LLL O   1 ? 45 
ATOM   14809 C CB  . ARG L  2 67  ? 2.032   -44.351  17.148  1.000 58.071  0 67  ARG LLL CB  1 ? 45 
ATOM   14810 C CG  . ARG L  2 67  ? 3.122   -43.401  16.676  1.000 61.796  0 67  ARG LLL CG  1 ? 45 
ATOM   14811 C CD  . ARG L  2 67  ? 3.361   -42.226  17.607  1.000 61.285  0 67  ARG LLL CD  1 ? 45 
ATOM   14812 N NE  . ARG L  2 67  ? 2.147   -41.437  17.761  1.000 59.362  0 67  ARG LLL NE  1 ? 45 
ATOM   14813 C CZ  . ARG L  2 67  ? 1.491   -41.240  18.888  1.000 56.625  0 67  ARG LLL CZ  1 ? 45 
ATOM   14814 N NH1 . ARG L  2 67  ? 1.921   -41.784  20.005  1.000 57.432  0 67  ARG LLL NH1 1 ? 45 
ATOM   14815 N NH2 . ARG L  2 67  ? 0.404   -40.497  18.900  1.000 54.717  0 67  ARG LLL NH2 1 ? 45 
ATOM   14816 N N   . PHE L  2 68  ? -0.334  -46.540  16.528  1.000 52.339  0 68  PHE LLL N   1 ? 45 
ATOM   14817 C CA  . PHE L  2 68  ? -1.477  -47.266  17.149  1.000 49.801  0 68  PHE LLL CA  1 ? 45 
ATOM   14818 C C   . PHE L  2 68  ? -2.011  -48.301  16.155  1.000 50.841  0 68  PHE LLL C   1 ? 45 
ATOM   14819 O O   . PHE L  2 68  ? -2.043  -48.028  14.953  1.000 53.719  0 68  PHE LLL O   1 ? 45 
ATOM   14820 C CB  . PHE L  2 68  ? -2.593  -46.289  17.540  1.000 46.585  0 68  PHE LLL CB  1 ? 45 
ATOM   14821 C CG  . PHE L  2 68  ? -2.324  -45.365  18.700  1.000 45.993  0 68  PHE LLL CG  1 ? 45 
ATOM   14822 C CD1 . PHE L  2 68  ? -1.070  -45.214  19.254  1.000 47.093  0 68  PHE LLL CD1 1 ? 45 
ATOM   14823 C CD2 . PHE L  2 68  ? -3.365  -44.623  19.233  1.000 45.308  0 68  PHE LLL CD2 1 ? 45 
ATOM   14824 C CE1 . PHE L  2 68  ? -0.858  -44.346  20.313  1.000 48.855  0 68  PHE LLL CE1 1 ? 45 
ATOM   14825 C CE2 . PHE L  2 68  ? -3.155  -43.758  20.295  1.000 46.750  0 68  PHE LLL CE2 1 ? 45 
ATOM   14826 C CZ  . PHE L  2 68  ? -1.898  -43.622  20.835  1.000 48.150  0 68  PHE LLL CZ  1 ? 45 
ATOM   14827 N N   . THR L  2 69  ? -2.408  -49.469  16.643  1.000 50.123  0 69  THR LLL N   1 ? 45 
ATOM   14828 C CA  . THR L  2 69  ? -2.973  -50.561  15.823  1.000 51.996  0 69  THR LLL CA  1 ? 45 
ATOM   14829 C C   . THR L  2 69  ? -4.283  -50.996  16.457  1.000 50.042  0 69  THR LLL C   1 ? 45 
ATOM   14830 O O   . THR L  2 69  ? -4.266  -51.374  17.665  1.000 53.206  0 69  THR LLL O   1 ? 45 
ATOM   14831 C CB  . THR L  2 69  ? -2.011  -51.748  15.699  1.000 55.964  0 69  THR LLL CB  1 ? 45 
ATOM   14832 O OG1 . THR L  2 69  ? -0.774  -51.246  15.182  1.000 62.122  0 69  THR LLL OG1 1 ? 45 
ATOM   14833 C CG2 . THR L  2 69  ? -2.564  -52.843  14.810  1.000 56.201  0 69  THR LLL CG2 1 ? 45 
ATOM   14834 N N   . ILE L  2 70  ? -5.374  -50.909  15.694  1.000 47.625  0 70  ILE LLL N   1 ? 45 
ATOM   14835 C CA  . ILE L  2 70  ? -6.700  -51.421  16.147  1.000 46.165  0 70  ILE LLL CA  1 ? 45 
ATOM   14836 C C   . ILE L  2 70  ? -6.851  -52.838  15.585  1.000 47.364  0 70  ILE LLL C   1 ? 45 
ATOM   14837 O O   . ILE L  2 70  ? -6.361  -53.096  14.481  1.000 49.689  0 70  ILE LLL O   1 ? 45 
ATOM   14838 C CB  . ILE L  2 70  ? -7.845  -50.479  15.740  1.000 44.176  0 70  ILE LLL CB  1 ? 45 
ATOM   14839 C CG1 . ILE L  2 70  ? -9.139  -50.828  16.478  1.000 41.494  0 70  ILE LLL CG1 1 ? 45 
ATOM   14840 C CG2 . ILE L  2 70  ? -8.025  -50.450  14.221  1.000 44.525  0 70  ILE LLL CG2 1 ? 45 
ATOM   14841 C CD1 . ILE L  2 70  ? -10.271 -49.851  16.259  1.000 41.504  0 70  ILE LLL CD1 1 ? 45 
ATOM   14842 N N   . SER L  2 71  ? -7.449  -53.731  16.357  1.000 46.658  0 71  SER LLL N   1 ? 45 
ATOM   14843 C CA  . SER L  2 71  ? -7.707  -55.143  15.984  1.000 47.422  0 71  SER LLL CA  1 ? 45 
ATOM   14844 C C   . SER L  2 71  ? -8.947  -55.608  16.757  1.000 45.522  0 71  SER LLL C   1 ? 45 
ATOM   14845 O O   . SER L  2 71  ? -9.351  -54.941  17.734  1.000 43.887  0 71  SER LLL O   1 ? 45 
ATOM   14846 C CB  . SER L  2 71  ? -6.512  -56.004  16.248  1.000 47.979  0 71  SER LLL CB  1 ? 45 
ATOM   14847 O OG  . SER L  2 71  ? -6.171  -56.005  17.627  1.000 48.564  0 71  SER LLL OG  1 ? 45 
ATOM   14848 N N   . ARG L  2 72  ? -9.565  -56.689  16.309  1.000 44.615  0 72  ARG LLL N   1 ? 45 
ATOM   14849 C CA  . ARG L  2 72  ? -10.779 -57.238  16.939  1.000 42.468  0 72  ARG LLL CA  1 ? 45 
ATOM   14850 C C   . ARG L  2 72  ? -10.631 -58.757  17.017  1.000 44.644  0 72  ARG LLL C   1 ? 45 
ATOM   14851 O O   . ARG L  2 72  ? -9.952  -59.333  16.175  1.000 45.211  0 72  ARG LLL O   1 ? 45 
ATOM   14852 C CB  . ARG L  2 72  ? -12.015 -56.823  16.144  1.000 43.112  0 72  ARG LLL CB  1 ? 45 
ATOM   14853 C CG  . ARG L  2 72  ? -12.071 -57.338  14.704  1.000 43.785  0 72  ARG LLL CG  1 ? 45 
ATOM   14854 C CD  . ARG L  2 72  ? -13.259 -56.772  13.938  1.000 44.305  0 72  ARG LLL CD  1 ? 45 
ATOM   14855 N NE  . ARG L  2 72  ? -14.533 -57.053  14.597  1.000 43.685  0 72  ARG LLL NE  1 ? 45 
ATOM   14856 C CZ  . ARG L  2 72  ? -15.612 -56.266  14.553  1.000 43.470  0 72  ARG LLL CZ  1 ? 45 
ATOM   14857 N NH1 . ARG L  2 72  ? -15.602 -55.125  13.880  1.000 43.579  0 72  ARG LLL NH1 1 ? 45 
ATOM   14858 N NH2 . ARG L  2 72  ? -16.705 -56.616  15.199  1.000 43.489  0 72  ARG LLL NH2 1 ? 45 
ATOM   14859 N N   . ASP L  2 73  ? -11.220 -59.347  18.045  1.000 45.286  0 73  ASP LLL N   1 ? 45 
ATOM   14860 C CA  . ASP L  2 73  ? -11.308 -60.802  18.255  1.000 47.472  0 73  ASP LLL CA  1 ? 45 
ATOM   14861 C C   . ASP L  2 73  ? -12.787 -61.089  18.506  1.000 48.133  0 73  ASP LLL C   1 ? 45 
ATOM   14862 O O   . ASP L  2 73  ? -13.280 -60.874  19.640  1.000 44.277  0 73  ASP LLL O   1 ? 45 
ATOM   14863 C CB  . ASP L  2 73  ? -10.389 -61.245  19.389  1.000 49.997  0 73  ASP LLL CB  1 ? 45 
ATOM   14864 C CG  . ASP L  2 73  ? -10.424 -62.735  19.638  1.000 53.942  0 73  ASP LLL CG  1 ? 45 
ATOM   14865 O OD1 . ASP L  2 73  ? -11.288 -63.399  19.041  1.000 54.911  0 73  ASP LLL OD1 1 ? 45 
ATOM   14866 O OD2 . ASP L  2 73  ? -9.588  -63.206  20.447  1.000 59.252  0 73  ASP LLL OD2 1 ? 45 
ATOM   14867 N N   . ASN L  2 74  ? -13.486 -61.487  17.449  1.000 49.980  0 74  ASN LLL N   1 ? 45 
ATOM   14868 C CA  . ASN L  2 74  ? -14.950 -61.690  17.475  1.000 48.862  0 74  ASN LLL CA  1 ? 45 
ATOM   14869 C C   . ASN L  2 74  ? -15.280 -62.805  18.475  1.000 50.656  0 74  ASN LLL C   1 ? 45 
ATOM   14870 O O   . ASN L  2 74  ? -16.313 -62.668  19.155  1.000 49.427  0 74  ASN LLL O   1 ? 45 
ATOM   14871 C CB  . ASN L  2 74  ? -15.477 -61.942  16.070  1.000 50.600  0 74  ASN LLL CB  1 ? 45 
ATOM   14872 C CG  . ASN L  2 74  ? -15.491 -60.692  15.223  1.000 50.214  0 74  ASN LLL CG  1 ? 45 
ATOM   14873 O OD1 . ASN L  2 74  ? -15.172 -59.590  15.676  1.000 46.427  0 74  ASN LLL OD1 1 ? 45 
ATOM   14874 N ND2 . ASN L  2 74  ? -15.883 -60.869  13.976  1.000 51.956  0 74  ASN LLL ND2 1 ? 45 
ATOM   14875 N N   . ALA L  2 75  ? -14.424 -63.823  18.634  1.000 50.924  0 75  ALA LLL N   1 ? 45 
ATOM   14876 C CA  . ALA L  2 75  ? -14.645 -64.934  19.593  1.000 51.730  0 75  ALA LLL CA  1 ? 45 
ATOM   14877 C C   . ALA L  2 75  ? -14.745 -64.394  21.030  1.000 51.353  0 75  ALA LLL C   1 ? 45 
ATOM   14878 O O   . ALA L  2 75  ? -15.389 -65.052  21.854  1.000 56.239  0 75  ALA LLL O   1 ? 45 
ATOM   14879 C CB  . ALA L  2 75  ? -13.571 -65.984  19.459  1.000 52.277  0 75  ALA LLL CB  1 ? 45 
ATOM   14880 N N   . LYS L  2 76  ? -14.144 -63.244  21.325  1.000 49.744  0 76  LYS LLL N   1 ? 45 
ATOM   14881 C CA  . LYS L  2 76  ? -14.119 -62.651  22.686  1.000 49.716  0 76  LYS LLL CA  1 ? 45 
ATOM   14882 C C   . LYS L  2 76  ? -14.904 -61.342  22.765  1.000 46.502  0 76  LYS LLL C   1 ? 45 
ATOM   14883 O O   . LYS L  2 76  ? -14.780 -60.662  23.779  1.000 46.093  0 76  LYS LLL O   1 ? 45 
ATOM   14884 C CB  . LYS L  2 76  ? -12.671 -62.377  23.081  1.000 51.507  0 76  LYS LLL CB  1 ? 45 
ATOM   14885 C CG  . LYS L  2 76  ? -11.791 -63.608  23.090  1.000 54.380  0 76  LYS LLL CG  1 ? 45 
ATOM   14886 C CD  . LYS L  2 76  ? -10.505 -63.344  23.838  1.000 55.358  0 76  LYS LLL CD  1 ? 45 
ATOM   14887 C CE  . LYS L  2 76  ? -9.684  -64.596  23.993  1.000 59.718  0 76  LYS LLL CE  1 ? 45 
ATOM   14888 N NZ  . LYS L  2 76  ? -8.726  -64.434  25.106  1.000 61.709  0 76  LYS LLL NZ  1 ? 45 
ATOM   14889 N N   . ASN L  2 77  ? -15.662 -60.989  21.736  1.000 46.267  0 77  ASN LLL N   1 ? 45 
ATOM   14890 C CA  . ASN L  2 77  ? -16.457 -59.734  21.715  1.000 44.352  0 77  ASN LLL CA  1 ? 45 
ATOM   14891 C C   . ASN L  2 77  ? -15.552 -58.538  22.066  1.000 42.458  0 77  ASN LLL C   1 ? 45 
ATOM   14892 O O   . ASN L  2 77  ? -16.017 -57.616  22.749  1.000 39.623  0 77  ASN LLL O   1 ? 45 
ATOM   14893 C CB  . ASN L  2 77  ? -17.603 -59.821  22.721  1.000 45.227  0 77  ASN LLL CB  1 ? 45 
ATOM   14894 C CG  . ASN L  2 77  ? -18.863 -60.402  22.114  1.000 44.680  0 77  ASN LLL CG  1 ? 45 
ATOM   14895 O OD1 . ASN L  2 77  ? -18.796 -61.335  21.324  1.000 45.558  0 77  ASN LLL OD1 1 ? 45 
ATOM   14896 N ND2 . ASN L  2 77  ? -20.010 -59.855  22.484  1.000 43.323  0 77  ASN LLL ND2 1 ? 45 
ATOM   14897 N N   . THR L  2 78  ? -14.292 -58.555  21.648  1.000 40.892  0 78  THR LLL N   1 ? 45 
ATOM   14898 C CA  . THR L  2 78  ? -13.295 -57.565  22.113  1.000 39.620  0 78  THR LLL CA  1 ? 45 
ATOM   14899 C C   . THR L  2 78  ? -12.625 -56.874  20.914  1.000 40.390  0 78  THR LLL C   1 ? 45 
ATOM   14900 O O   . THR L  2 78  ? -12.264 -57.539  19.910  1.000 40.935  0 78  THR LLL O   1 ? 45 
ATOM   14901 C CB  . THR L  2 78  ? -12.301 -58.223  23.086  1.000 40.645  0 78  THR LLL CB  1 ? 45 
ATOM   14902 O OG1 . THR L  2 78  ? -13.046 -58.709  24.207  1.000 38.753  0 78  THR LLL OG1 1 ? 45 
ATOM   14903 C CG2 . THR L  2 78  ? -11.228 -57.268  23.556  1.000 38.839  0 78  THR LLL CG2 1 ? 45 
ATOM   14904 N N   . VAL L  2 79  ? -12.511 -55.552  21.026  1.000 40.388  0 79  VAL LLL N   1 ? 45 
ATOM   14905 C CA  . VAL L  2 79  ? -11.663 -54.687  20.157  1.000 41.384  0 79  VAL LLL CA  1 ? 45 
ATOM   14906 C C   . VAL L  2 79  ? -10.468 -54.225  21.013  1.000 42.357  0 79  VAL LLL C   1 ? 45 
ATOM   14907 O O   . VAL L  2 79  ? -10.635 -53.967  22.212  1.000 39.385  0 79  VAL LLL O   1 ? 45 
ATOM   14908 C CB  . VAL L  2 79  ? -12.470 -53.526  19.561  1.000 40.650  0 79  VAL LLL CB  1 ? 45 
ATOM   14909 C CG1 . VAL L  2 79  ? -13.050 -52.634  20.637  1.000 41.063  0 79  VAL LLL CG1 1 ? 45 
ATOM   14910 C CG2 . VAL L  2 79  ? -11.666 -52.717  18.576  1.000 40.346  0 79  VAL LLL CG2 1 ? 45 
ATOM   14911 N N   . TYR L  2 80  ? -9.280  -54.186  20.412  1.000 44.145  0 80  TYR LLL N   1 ? 45 
ATOM   14912 C CA  . TYR L  2 80  ? -8.007  -53.815  21.070  1.000 43.763  0 80  TYR LLL CA  1 ? 45 
ATOM   14913 C C   . TYR L  2 80  ? -7.452  -52.547  20.424  1.000 42.736  0 80  TYR LLL C   1 ? 45 
ATOM   14914 O O   . TYR L  2 80  ? -7.641  -52.341  19.201  1.000 43.158  0 80  TYR LLL O   1 ? 45 
ATOM   14915 C CB  . TYR L  2 80  ? -7.002  -54.964  20.945  1.000 45.490  0 80  TYR LLL CB  1 ? 45 
ATOM   14916 C CG  . TYR L  2 80  ? -7.440  -56.234  21.619  1.000 47.153  0 80  TYR LLL CG  1 ? 45 
ATOM   14917 C CD1 . TYR L  2 80  ? -7.331  -56.384  22.995  1.000 46.744  0 80  TYR LLL CD1 1 ? 45 
ATOM   14918 C CD2 . TYR L  2 80  ? -7.968  -57.291  20.887  1.000 48.611  0 80  TYR LLL CD2 1 ? 45 
ATOM   14919 C CE1 . TYR L  2 80  ? -7.736  -57.549  23.625  1.000 48.474  0 80  TYR LLL CE1 1 ? 45 
ATOM   14920 C CE2 . TYR L  2 80  ? -8.343  -58.471  21.503  1.000 49.163  0 80  TYR LLL CE2 1 ? 45 
ATOM   14921 C CZ  . TYR L  2 80  ? -8.219  -58.600  22.872  1.000 49.671  0 80  TYR LLL CZ  1 ? 45 
ATOM   14922 O OH  . TYR L  2 80  ? -8.604  -59.742  23.488  1.000 54.408  0 80  TYR LLL OH  1 ? 45 
ATOM   14923 N N   . LEU L  2 81  ? -6.757  -51.741  21.219  1.000 43.312  0 81  LEU LLL N   1 ? 45 
ATOM   14924 C CA  . LEU L  2 81  ? -5.917  -50.624  20.706  1.000 44.433  0 81  LEU LLL CA  1 ? 45 
ATOM   14925 C C   . LEU L  2 81  ? -4.495  -50.792  21.267  1.000 44.554  0 81  LEU LLL C   1 ? 45 
ATOM   14926 O O   . LEU L  2 81  ? -4.302  -50.561  22.463  1.000 42.101  0 81  LEU LLL O   1 ? 45 
ATOM   14927 C CB  . LEU L  2 81  ? -6.543  -49.276  21.096  1.000 41.913  0 81  LEU LLL CB  1 ? 45 
ATOM   14928 C CG  . LEU L  2 81  ? -5.933  -48.057  20.412  1.000 43.518  0 81  LEU LLL CG  1 ? 45 
ATOM   14929 C CD1 . LEU L  2 81  ? -6.232  -48.048  18.916  1.000 44.326  0 81  LEU LLL CD1 1 ? 45 
ATOM   14930 C CD2 . LEU L  2 81  ? -6.408  -46.780  21.060  1.000 44.120  0 81  LEU LLL CD2 1 ? 45 
ATOM   14931 N N   . GLN L  2 82  ? -3.569  -51.227  20.412  1.000 45.788  0 82  GLN LLL N   1 ? 45 
ATOM   14932 C CA  . GLN L  2 82  ? -2.121  -51.297  20.698  1.000 48.645  0 82  GLN LLL CA  1 ? 45 
ATOM   14933 C C   . GLN L  2 82  ? -1.599  -49.873  20.504  1.000 50.037  0 82  GLN LLL C   1 ? 45 
ATOM   14934 O O   . GLN L  2 82  ? -1.760  -49.337  19.410  1.000 52.800  0 82  GLN LLL O   1 ? 45 
ATOM   14935 C CB  . GLN L  2 82  ? -1.458  -52.340  19.797  1.000 50.275  0 82  GLN LLL CB  1 ? 45 
ATOM   14936 C CG  . GLN L  2 82  ? -0.003  -52.622  20.153  1.000 54.342  0 82  GLN LLL CG  1 ? 45 
ATOM   14937 C CD  . GLN L  2 82  ? 0.174   -53.007  21.603  1.000 55.453  0 82  GLN LLL CD  1 ? 45 
ATOM   14938 O OE1 . GLN L  2 82  ? -0.537  -53.861  22.154  1.000 55.268  0 82  GLN LLL OE1 1 ? 45 
ATOM   14939 N NE2 . GLN L  2 82  ? 1.119   -52.349  22.246  1.000 57.519  0 82  GLN LLL NE2 1 ? 45 
ATOM   14940 N N   . MET L  2 83  ? -1.108  -49.242  21.563  1.000 51.673  0 83  MET LLL N   1 ? 45 
ATOM   14941 C CA  . MET L  2 83  ? -0.576  -47.863  21.517  1.000 53.430  0 83  MET LLL CA  1 ? 45 
ATOM   14942 C C   . MET L  2 83  ? 0.925   -47.950  21.786  1.000 56.881  0 83  MET LLL C   1 ? 45 
ATOM   14943 O O   . MET L  2 83  ? 1.296   -48.323  22.893  1.000 57.839  0 83  MET LLL O   1 ? 45 
ATOM   14944 C CB  . MET L  2 83  ? -1.248  -46.957  22.553  1.000 53.865  0 83  MET LLL CB  1 ? 45 
ATOM   14945 C CG  . MET L  2 83  ? -2.774  -46.950  22.484  1.000 51.856  0 83  MET LLL CG  1 ? 45 
ATOM   14946 S SD  . MET L  2 83  ? -3.497  -45.826  23.697  1.000 55.167  0 83  MET LLL SD  1 ? 45 
ATOM   14947 C CE  . MET L  2 83  ? -3.148  -46.683  25.220  1.000 53.120  0 83  MET LLL CE  1 ? 45 
ATOM   14948 N N   . ASN L  2 84  ? 1.743   -47.666  20.773  1.000 59.415  0 84  ASN LLL N   1 ? 45 
ATOM   14949 C CA  . ASN L  2 84  ? 3.223   -47.693  20.860  1.000 64.371  0 84  ASN LLL CA  1 ? 45 
ATOM   14950 C C   . ASN L  2 84  ? 3.751   -46.254  20.830  1.000 66.546  0 84  ASN LLL C   1 ? 45 
ATOM   14951 O O   . ASN L  2 84  ? 3.020   -45.345  20.364  1.000 64.197  0 84  ASN LLL O   1 ? 45 
ATOM   14952 C CB  . ASN L  2 84  ? 3.820   -48.561  19.751  1.000 67.551  0 84  ASN LLL CB  1 ? 45 
ATOM   14953 C CG  . ASN L  2 84  ? 3.392   -50.010  19.864  1.000 67.468  0 84  ASN LLL CG  1 ? 45 
ATOM   14954 O OD1 . ASN L  2 84  ? 3.235   -50.539  20.958  1.000 65.936  0 84  ASN LLL OD1 1 ? 45 
ATOM   14955 N ND2 . ASN L  2 84  ? 3.183   -50.667  18.743  1.000 71.249  0 84  ASN LLL ND2 1 ? 45 
ATOM   14956 N N   . ARG L  2 85  ? 4.964   -46.057  21.353  1.000 69.035  0 85  ARG LLL N   1 ? 45 
ATOM   14957 C CA  . ARG L  2 85  ? 5.692   -44.771  21.283  1.000 70.437  0 85  ARG LLL CA  1 ? 45 
ATOM   14958 C C   . ARG L  2 85  ? 4.750   -43.664  21.765  1.000 66.358  0 85  ARG LLL C   1 ? 45 
ATOM   14959 O O   . ARG L  2 85  ? 4.559   -42.689  21.043  1.000 65.737  0 85  ARG LLL O   1 ? 45 
ATOM   14960 C CB  . ARG L  2 85  ? 6.233   -44.602  19.855  1.000 74.401  0 85  ARG LLL CB  1 ? 45 
ATOM   14961 C CG  . ARG L  2 85  ? 7.213   -45.697  19.461  1.000 80.416  0 85  ARG LLL CG  1 ? 45 
ATOM   14962 C CD  . ARG L  2 85  ? 8.051   -45.379  18.242  1.000 85.990  0 85  ARG LLL CD  1 ? 45 
ATOM   14963 N NE  . ARG L  2 85  ? 7.167   -45.216  17.091  1.000 88.428  0 85  ARG LLL NE  1 ? 45 
ATOM   14964 C CZ  . ARG L  2 85  ? 6.984   -44.085  16.402  1.000 89.523  0 85  ARG LLL CZ  1 ? 45 
ATOM   14965 N NH1 . ARG L  2 85  ? 7.632   -42.965  16.720  1.000 90.249  0 85  ARG LLL NH1 1 ? 45 
ATOM   14966 N NH2 . ARG L  2 85  ? 6.162   -44.099  15.358  1.000 85.567  0 85  ARG LLL NH2 1 ? 45 
ATOM   14967 N N   . LEU L  2 86  ? 4.181   -43.829  22.954  1.000 63.750  0 86  LEU LLL N   1 ? 45 
ATOM   14968 C CA  . LEU L  2 86  ? 3.221   -42.872  23.552  1.000 61.777  0 86  LEU LLL CA  1 ? 45 
ATOM   14969 C C   . LEU L  2 86  ? 3.923   -41.550  23.892  1.000 64.813  0 86  LEU LLL C   1 ? 45 
ATOM   14970 O O   . LEU L  2 86  ? 5.071   -41.584  24.375  1.000 68.310  0 86  LEU LLL O   1 ? 45 
ATOM   14971 C CB  . LEU L  2 86  ? 2.590   -43.503  24.795  1.000 60.882  0 86  LEU LLL CB  1 ? 45 
ATOM   14972 C CG  . LEU L  2 86  ? 1.531   -44.561  24.479  1.000 57.929  0 86  LEU LLL CG  1 ? 45 
ATOM   14973 C CD1 . LEU L  2 86  ? 1.253   -45.423  25.696  1.000 57.989  0 86  LEU LLL CD1 1 ? 45 
ATOM   14974 C CD2 . LEU L  2 86  ? 0.255   -43.907  23.967  1.000 54.834  0 86  LEU LLL CD2 1 ? 45 
ATOM   14975 N N   . LYS L  2 87  ? 3.244   -40.434  23.638  1.000 63.095  0 87  LYS LLL N   1 ? 45 
ATOM   14976 C CA  . LYS L  2 87  ? 3.715   -39.048  23.900  1.000 65.582  0 87  LYS LLL CA  1 ? 45 
ATOM   14977 C C   . LYS L  2 87  ? 2.779   -38.414  24.924  1.000 64.397  0 87  LYS LLL C   1 ? 45 
ATOM   14978 O O   . LYS L  2 87  ? 1.646   -38.871  25.062  1.000 62.095  0 87  LYS LLL O   1 ? 45 
ATOM   14979 C CB  . LYS L  2 87  ? 3.724   -38.246  22.593  1.000 67.274  0 87  LYS LLL CB  1 ? 45 
ATOM   14980 C CG  . LYS L  2 87  ? 4.237   -39.011  21.386  1.000 69.172  0 87  LYS LLL CG  1 ? 45 
ATOM   14981 C CD  . LYS L  2 87  ? 4.028   -38.320  20.056  1.000 70.879  0 87  LYS LLL CD  1 ? 45 
ATOM   14982 C CE  . LYS L  2 87  ? 4.803   -39.025  18.965  1.000 74.060  0 87  LYS LLL CE  1 ? 45 
ATOM   14983 N NZ  . LYS L  2 87  ? 4.649   -38.358  17.652  1.000 75.910  0 87  LYS LLL NZ  1 ? 45 
ATOM   14984 N N   . PRO L  2 88  ? 3.211   -37.388  25.692  1.000 66.754  0 88  PRO LLL N   1 ? 45 
ATOM   14985 C CA  . PRO L  2 88  ? 2.312   -36.687  26.613  1.000 65.521  0 88  PRO LLL CA  1 ? 45 
ATOM   14986 C C   . PRO L  2 88  ? 0.968   -36.253  25.998  1.000 63.289  0 88  PRO LLL C   1 ? 45 
ATOM   14987 O O   . PRO L  2 88  ? -0.015  -36.365  26.683  1.000 61.537  0 88  PRO LLL O   1 ? 45 
ATOM   14988 C CB  . PRO L  2 88  ? 3.139   -35.465  27.052  1.000 68.425  0 88  PRO LLL CB  1 ? 45 
ATOM   14989 C CG  . PRO L  2 88  ? 4.576   -35.895  26.900  1.000 71.417  0 88  PRO LLL CG  1 ? 45 
ATOM   14990 C CD  . PRO L  2 88  ? 4.598   -36.893  25.765  1.000 69.882  0 88  PRO LLL CD  1 ? 45 
ATOM   14991 N N   . GLU L  2 89  ? 0.953   -35.842  24.725  1.000 63.894  0 89  GLU LLL N   1 ? 45 
ATOM   14992 C CA  . GLU L  2 89  ? -0.234  -35.396  23.946  1.000 63.487  0 89  GLU LLL CA  1 ? 45 
ATOM   14993 C C   . GLU L  2 89  ? -1.257  -36.523  23.798  1.000 56.680  0 89  GLU LLL C   1 ? 45 
ATOM   14994 O O   . GLU L  2 89  ? -2.346  -36.234  23.299  1.000 54.015  0 89  GLU LLL O   1 ? 45 
ATOM   14995 C CB  . GLU L  2 89  ? 0.143   -34.954  22.526  1.000 70.144  0 89  GLU LLL CB  1 ? 45 
ATOM   14996 C CG  . GLU L  2 89  ? 1.211   -33.870  22.488  1.000 81.863  0 89  GLU LLL CG  1 ? 45 
ATOM   14997 C CD  . GLU L  2 89  ? 2.655   -34.376  22.522  1.000 89.140  0 89  GLU LLL CD  1 ? 45 
ATOM   14998 O OE1 . GLU L  2 89  ? 2.935   -35.319  21.756  1.000 96.762  0 89  GLU LLL OE1 1 ? 45 
ATOM   14999 O OE2 . GLU L  2 89  ? 3.487   -33.813  23.297  1.000 89.553  0 89  GLU LLL OE2 1 ? 45 
ATOM   15000 N N   . ASP L  2 90  ? -0.892  -37.767  24.123  1.000 54.081  0 90  ASP LLL N   1 ? 45 
ATOM   15001 C CA  . ASP L  2 90  ? -1.787  -38.950  24.035  1.000 52.606  0 90  ASP LLL CA  1 ? 45 
ATOM   15002 C C   . ASP L  2 90  ? -2.577  -39.118  25.338  1.000 49.883  0 90  ASP LLL C   1 ? 45 
ATOM   15003 O O   . ASP L  2 90  ? -3.525  -39.925  25.336  1.000 48.337  0 90  ASP LLL O   1 ? 45 
ATOM   15004 C CB  . ASP L  2 90  ? -1.012  -40.235  23.735  1.000 53.294  0 90  ASP LLL CB  1 ? 45 
ATOM   15005 C CG  . ASP L  2 90  ? -0.380  -40.258  22.358  1.000 54.998  0 90  ASP LLL CG  1 ? 45 
ATOM   15006 O OD1 . ASP L  2 90  ? -1.043  -39.863  21.396  1.000 53.224  0 90  ASP LLL OD1 1 ? 45 
ATOM   15007 O OD2 . ASP L  2 90  ? 0.779   -40.674  22.273  1.000 60.640  0 90  ASP LLL OD2 1 ? 45 
ATOM   15008 N N   . THR L  2 91  ? -2.221  -38.383  26.391  1.000 48.995  0 91  THR LLL N   1 ? 45 
ATOM   15009 C CA  . THR L  2 91  ? -2.950  -38.387  27.678  1.000 48.194  0 91  THR LLL CA  1 ? 45 
ATOM   15010 C C   . THR L  2 91  ? -4.397  -37.955  27.426  1.000 47.059  0 91  THR LLL C   1 ? 45 
ATOM   15011 O O   . THR L  2 91  ? -4.597  -36.860  26.856  1.000 48.049  0 91  THR LLL O   1 ? 45 
ATOM   15012 C CB  . THR L  2 91  ? -2.260  -37.487  28.702  1.000 49.936  0 91  THR LLL CB  1 ? 45 
ATOM   15013 O OG1 . THR L  2 91  ? -0.983  -38.066  28.984  1.000 51.399  0 91  THR LLL OG1 1 ? 45 
ATOM   15014 C CG2 . THR L  2 91  ? -3.068  -37.342  29.972  1.000 50.806  0 91  THR LLL CG2 1 ? 45 
ATOM   15015 N N   . ALA L  2 92  ? -5.361  -38.784  27.823  1.000 45.565  0 92  ALA LLL N   1 ? 45 
ATOM   15016 C CA  . ALA L  2 92  ? -6.809  -38.521  27.654  1.000 47.514  0 92  ALA LLL CA  1 ? 45 
ATOM   15017 C C   . ALA L  2 92  ? -7.628  -39.677  28.225  1.000 45.978  0 92  ALA LLL C   1 ? 45 
ATOM   15018 O O   . ALA L  2 92  ? -7.041  -40.716  28.564  1.000 47.394  0 92  ALA LLL O   1 ? 45 
ATOM   15019 C CB  . ALA L  2 92  ? -7.158  -38.315  26.193  1.000 46.484  0 92  ALA LLL CB  1 ? 45 
ATOM   15020 N N   . VAL L  2 93  ? -8.941  -39.487  28.295  1.000 44.166  0 93  VAL LLL N   1 ? 45 
ATOM   15021 C CA  . VAL L  2 93  ? -9.912  -40.592  28.482  1.000 41.608  0 93  VAL LLL CA  1 ? 45 
ATOM   15022 C C   . VAL L  2 93  ? -10.118 -41.207  27.098  1.000 39.420  0 93  VAL LLL C   1 ? 45 
ATOM   15023 O O   . VAL L  2 93  ? -10.383 -40.450  26.135  1.000 40.255  0 93  VAL LLL O   1 ? 45 
ATOM   15024 C CB  . VAL L  2 93  ? -11.236 -40.074  29.078  1.000 42.089  0 93  VAL LLL CB  1 ? 45 
ATOM   15025 C CG1 . VAL L  2 93  ? -12.295 -41.168  29.131  1.000 40.789  0 93  VAL LLL CG1 1 ? 45 
ATOM   15026 C CG2 . VAL L  2 93  ? -11.043 -39.407  30.430  1.000 42.380  0 93  VAL LLL CG2 1 ? 45 
ATOM   15027 N N   . TYR L  2 94  ? -9.950  -42.520  27.001  1.000 38.366  0 94  TYR LLL N   1 ? 45 
ATOM   15028 C CA  . TYR L  2 94  ? -10.129 -43.296  25.756  1.000 39.272  0 94  TYR LLL CA  1 ? 45 
ATOM   15029 C C   . TYR L  2 94  ? -11.472 -44.019  25.851  1.000 39.050  0 94  TYR LLL C   1 ? 45 
ATOM   15030 O O   . TYR L  2 94  ? -11.688 -44.761  26.838  1.000 36.913  0 94  TYR LLL O   1 ? 45 
ATOM   15031 C CB  . TYR L  2 94  ? -8.945  -44.233  25.520  1.000 40.532  0 94  TYR LLL CB  1 ? 45 
ATOM   15032 C CG  . TYR L  2 94  ? -7.715  -43.538  25.006  1.000 40.876  0 94  TYR LLL CG  1 ? 45 
ATOM   15033 C CD1 . TYR L  2 94  ? -6.951  -42.732  25.828  1.000 42.936  0 94  TYR LLL CD1 1 ? 45 
ATOM   15034 C CD2 . TYR L  2 94  ? -7.333  -43.657  23.680  1.000 40.907  0 94  TYR LLL CD2 1 ? 45 
ATOM   15035 C CE1 . TYR L  2 94  ? -5.831  -42.066  25.349  1.000 44.108  0 94  TYR LLL CE1 1 ? 45 
ATOM   15036 C CE2 . TYR L  2 94  ? -6.208  -43.009  23.191  1.000 42.362  0 94  TYR LLL CE2 1 ? 45 
ATOM   15037 C CZ  . TYR L  2 94  ? -5.454  -42.218  24.028  1.000 42.346  0 94  TYR LLL CZ  1 ? 45 
ATOM   15038 O OH  . TYR L  2 94  ? -4.361  -41.579  23.541  1.000 43.493  0 94  TYR LLL OH  1 ? 45 
ATOM   15039 N N   . PHE L  2 95  ? -12.352 -43.743  24.886  1.000 39.385  0 95  PHE LLL N   1 ? 45 
ATOM   15040 C CA  . PHE L  2 95  ? -13.720 -44.294  24.779  1.000 38.694  0 95  PHE LLL CA  1 ? 45 
ATOM   15041 C C   . PHE L  2 95  ? -13.784 -45.322  23.653  1.000 38.053  0 95  PHE LLL C   1 ? 45 
ATOM   15042 O O   . PHE L  2 95  ? -13.346 -45.070  22.519  1.000 39.298  0 95  PHE LLL O   1 ? 45 
ATOM   15043 C CB  . PHE L  2 95  ? -14.742 -43.220  24.448  1.000 38.961  0 95  PHE LLL CB  1 ? 45 
ATOM   15044 C CG  . PHE L  2 95  ? -14.885 -42.142  25.479  1.000 39.495  0 95  PHE LLL CG  1 ? 45 
ATOM   15045 C CD1 . PHE L  2 95  ? -14.094 -41.017  25.423  1.000 41.157  0 95  PHE LLL CD1 1 ? 45 
ATOM   15046 C CD2 . PHE L  2 95  ? -15.843 -42.234  26.471  1.000 39.917  0 95  PHE LLL CD2 1 ? 45 
ATOM   15047 C CE1 . PHE L  2 95  ? -14.248 -40.007  26.364  1.000 42.595  0 95  PHE LLL CE1 1 ? 45 
ATOM   15048 C CE2 . PHE L  2 95  ? -15.985 -41.236  27.420  1.000 41.296  0 95  PHE LLL CE2 1 ? 45 
ATOM   15049 C CZ  . PHE L  2 95  ? -15.183 -40.120  27.360  1.000 42.403  0 95  PHE LLL CZ  1 ? 45 
ATOM   15050 N N   . CYS L  2 96  ? -14.342 -46.463  23.995  1.000 38.502  0 96  CYS LLL N   1 ? 45 
ATOM   15051 C CA  . CYS L  2 96  ? -14.796 -47.513  23.071  1.000 39.495  0 96  CYS LLL CA  1 ? 45 
ATOM   15052 C C   . CYS L  2 96  ? -16.134 -47.073  22.468  1.000 38.623  0 96  CYS LLL C   1 ? 45 
ATOM   15053 O O   . CYS L  2 96  ? -16.976 -46.513  23.197  1.000 39.532  0 96  CYS LLL O   1 ? 45 
ATOM   15054 C CB  . CYS L  2 96  ? -14.977 -48.793  23.864  1.000 42.664  0 96  CYS LLL CB  1 ? 45 
ATOM   15055 S SG  . CYS L  2 96  ? -15.344 -50.216  22.808  1.000 53.755  0 96  CYS LLL SG  1 ? 45 
ATOM   15056 N N   . ALA L  2 97  ? -16.348 -47.288  21.174  1.000 37.918  0 97  ALA LLL N   1 ? 45 
ATOM   15057 C CA  . ALA L  2 97  ? -17.662 -47.047  20.558  1.000 37.472  0 97  ALA LLL CA  1 ? 45 
ATOM   15058 C C   . ALA L  2 97  ? -17.990 -48.154  19.560  1.000 36.675  0 97  ALA LLL C   1 ? 45 
ATOM   15059 O O   . ALA L  2 97  ? -17.046 -48.818  19.064  1.000 37.529  0 97  ALA LLL O   1 ? 45 
ATOM   15060 C CB  . ALA L  2 97  ? -17.671 -45.682  19.914  1.000 40.542  0 97  ALA LLL CB  1 ? 45 
ATOM   15061 N N   . ALA L  2 98  ? -19.287 -48.316  19.274  1.000 36.044  0 98  ALA LLL N   1 ? 45 
ATOM   15062 C CA  . ALA L  2 98  ? -19.800 -49.365  18.371  1.000 36.934  0 98  ALA LLL CA  1 ? 45 
ATOM   15063 C C   . ALA L  2 98  ? -21.020 -48.870  17.599  1.000 37.438  0 98  ALA LLL C   1 ? 45 
ATOM   15064 O O   . ALA L  2 98  ? -21.830 -48.095  18.160  1.000 41.087  0 98  ALA LLL O   1 ? 45 
ATOM   15065 C CB  . ALA L  2 98  ? -20.139 -50.591  19.170  1.000 36.621  0 98  ALA LLL CB  1 ? 45 
ATOM   15066 N N   . ASP L  2 99  ? -21.155 -49.351  16.371  1.000 36.616  0 99  ASP LLL N   1 ? 45 
ATOM   15067 C CA  . ASP L  2 99  ? -22.338 -49.121  15.510  1.000 38.095  0 99  ASP LLL CA  1 ? 45 
ATOM   15068 C C   . ASP L  2 99  ? -22.475 -50.260  14.498  1.000 37.338  0 99  ASP LLL C   1 ? 45 
ATOM   15069 O O   . ASP L  2 99  ? -21.461 -50.827  14.087  1.000 37.627  0 99  ASP LLL O   1 ? 45 
ATOM   15070 C CB  . ASP L  2 99  ? -22.232 -47.787  14.771  1.000 37.903  0 99  ASP LLL CB  1 ? 45 
ATOM   15071 C CG  . ASP L  2 99  ? -23.595 -47.267  14.399  1.000 40.225  0 99  ASP LLL CG  1 ? 45 
ATOM   15072 O OD1 . ASP L  2 99  ? -24.253 -46.692  15.277  1.000 38.057  0 99  ASP LLL OD1 1 ? 45 
ATOM   15073 O OD2 . ASP L  2 99  ? -24.009 -47.483  13.232  1.000 45.979  0 99  ASP LLL OD2 1 ? 45 
ATOM   15074 N N   . ARG L  2 100 ? -23.698 -50.565  14.105  1.000 43.276  0 100 ARG LLL N   1 ? 46 
ATOM   15075 C CA  . ARG L  2 100 ? -23.982 -51.560  13.037  1.000 44.709  0 100 ARG LLL CA  1 ? 46 
ATOM   15076 C C   . ARG L  2 100 ? -23.407 -51.047  11.705  1.000 42.996  0 100 ARG LLL C   1 ? 46 
ATOM   15077 O O   . ARG L  2 100 ? -22.981 -51.857  10.897  1.000 42.854  0 100 ARG LLL O   1 ? 46 
ATOM   15078 C CB  . ARG L  2 100 ? -25.492 -51.780  12.904  1.000 45.535  0 100 ARG LLL CB  1 ? 46 
ATOM   15079 C CG  . ARG L  2 100 ? -26.135 -52.479  14.084  1.000 47.836  0 100 ARG LLL CG  1 ? 46 
ATOM   15080 C CD  . ARG L  2 100 ? -25.815 -53.932  14.152  1.000 51.250  0 100 ARG LLL CD  1 ? 46 
ATOM   15081 N NE  . ARG L  2 100 ? -26.122 -54.589  12.882  1.000 54.833  0 100 ARG LLL NE  1 ? 46 
ATOM   15082 C CZ  . ARG L  2 100 ? -27.277 -55.169  12.544  1.000 56.546  0 100 ARG LLL CZ  1 ? 46 
ATOM   15083 N NH1 . ARG L  2 100 ? -28.293 -55.237  13.384  1.000 58.985  0 100 ARG LLL NH1 1 ? 46 
ATOM   15084 N NH2 . ARG L  2 100 ? -27.407 -55.685  11.341  1.000 57.366  0 100 ARG LLL NH2 1 ? 46 
ATOM   15085 N N   . GLY L  2 101 ? -23.430 -49.739  11.487  1.000 41.833  0 101 GLY LLL N   1 ? 46 
ATOM   15086 C CA  . GLY L  2 101 ? -23.048 -49.106  10.215  1.000 42.097  0 101 GLY LLL CA  1 ? 46 
ATOM   15087 C C   . GLY L  2 101 ? -21.617 -48.603  10.227  1.000 41.579  0 101 GLY LLL C   1 ? 46 
ATOM   15088 O O   . GLY L  2 101 ? -21.127 -48.155  11.286  1.000 40.330  0 101 GLY LLL O   1 ? 46 
ATOM   15089 N N   . GLU L  2 102 ? -20.979 -48.695  9.068   1.000 42.336  0 102 GLU LLL N   1 ? 46 
ATOM   15090 C CA  . GLU L  2 102 ? -19.672 -48.058  8.777   1.000 43.768  0 102 GLU LLL CA  1 ? 46 
ATOM   15091 C C   . GLU L  2 102 ? -19.935 -46.719  8.080   1.000 42.296  0 102 GLU LLL C   1 ? 46 
ATOM   15092 O O   . GLU L  2 102 ? -20.599 -46.723  7.039   1.000 42.897  0 102 GLU LLL O   1 ? 46 
ATOM   15093 C CB  . GLU L  2 102 ? -18.836 -48.999  7.911   1.000 46.039  0 102 GLU LLL CB  1 ? 46 
ATOM   15094 C CG  . GLU L  2 102 ? -17.424 -48.518  7.701   1.000 47.127  0 102 GLU LLL CG  1 ? 46 
ATOM   15095 C CD  . GLU L  2 102 ? -16.578 -49.439  6.844   1.000 50.450  0 102 GLU LLL CD  1 ? 46 
ATOM   15096 O OE1 . GLU L  2 102 ? -16.892 -50.621  6.774   1.000 50.782  0 102 GLU LLL OE1 1 ? 46 
ATOM   15097 O OE2 . GLU L  2 102 ? -15.611 -48.954  6.248   1.000 53.213  0 102 GLU LLL OE2 1 ? 46 
ATOM   15098 N N   . SER L  2 103 ? -19.451 -45.625  8.651   1.000 39.854  0 103 SER LLL N   1 ? 46 
ATOM   15099 C CA  . SER L  2 103 ? -19.691 -44.247  8.151   1.000 38.999  0 103 SER LLL CA  1 ? 46 
ATOM   15100 C C   . SER L  2 103 ? -18.613 -43.828  7.148   1.000 39.709  0 103 SER LLL C   1 ? 46 
ATOM   15101 O O   . SER L  2 103 ? -17.424 -44.051  7.391   1.000 38.809  0 103 SER LLL O   1 ? 46 
ATOM   15102 C CB  . SER L  2 103 ? -19.766 -43.265  9.273   1.000 38.928  0 103 SER LLL CB  1 ? 46 
ATOM   15103 O OG  . SER L  2 103 ? -20.031 -41.968  8.769   1.000 41.392  0 103 SER LLL OG  1 ? 46 
ATOM   15104 N N   . TYR L  2 104 ? -19.020 -43.193  6.055   1.000 39.956  0 104 TYR LLL N   1 ? 46 
ATOM   15105 C CA  . TYR L  2 104 ? -18.102 -42.391  5.226   1.000 41.152  0 104 TYR LLL CA  1 ? 46 
ATOM   15106 C C   . TYR L  2 104 ? -17.458 -41.327  6.126   1.000 41.473  0 104 TYR LLL C   1 ? 46 
ATOM   15107 O O   . TYR L  2 104 ? -16.277 -41.058  5.893   1.000 44.744  0 104 TYR LLL O   1 ? 46 
ATOM   15108 C CB  . TYR L  2 104 ? -18.834 -41.751  4.055   1.000 43.689  0 104 TYR LLL CB  1 ? 46 
ATOM   15109 C CG  . TYR L  2 104 ? -17.920 -40.947  3.174   1.000 47.625  0 104 TYR LLL CG  1 ? 46 
ATOM   15110 C CD1 . TYR L  2 104 ? -16.965 -41.590  2.401   1.000 51.097  0 104 TYR LLL CD1 1 ? 46 
ATOM   15111 C CD2 . TYR L  2 104 ? -17.975 -39.562  3.127   1.000 49.150  0 104 TYR LLL CD2 1 ? 46 
ATOM   15112 C CE1 . TYR L  2 104 ? -16.091 -40.885  1.591   1.000 53.390  0 104 TYR LLL CE1 1 ? 46 
ATOM   15113 C CE2 . TYR L  2 104 ? -17.106 -38.840  2.313   1.000 53.294  0 104 TYR LLL CE2 1 ? 46 
ATOM   15114 C CZ  . TYR L  2 104 ? -16.155 -39.504  1.553   1.000 54.562  0 104 TYR LLL CZ  1 ? 46 
ATOM   15115 O OH  . TYR L  2 104 ? -15.291 -38.802  0.773   1.000 57.412  0 104 TYR LLL OH  1 ? 46 
ATOM   15116 N N   . TYR L  2 105 ? -18.191 -40.758  7.092   1.000 38.146  0 105 TYR LLL N   1 ? 46 
ATOM   15117 C CA  . TYR L  2 105 ? -17.670 -39.739  8.046   1.000 39.042  0 105 TYR LLL CA  1 ? 46 
ATOM   15118 C C   . TYR L  2 105 ? -17.273 -40.440  9.359   1.000 39.621  0 105 TYR LLL C   1 ? 46 
ATOM   15119 O O   . TYR L  2 105 ? -17.800 -40.118  10.454  1.000 41.006  0 105 TYR LLL O   1 ? 46 
ATOM   15120 C CB  . TYR L  2 105 ? -18.672 -38.602  8.276   1.000 38.345  0 105 TYR LLL CB  1 ? 46 
ATOM   15121 C CG  . TYR L  2 105 ? -19.281 -37.991  7.032   1.000 41.661  0 105 TYR LLL CG  1 ? 46 
ATOM   15122 C CD1 . TYR L  2 105 ? -18.523 -37.272  6.113   1.000 43.264  0 105 TYR LLL CD1 1 ? 46 
ATOM   15123 C CD2 . TYR L  2 105 ? -20.647 -38.087  6.789   1.000 41.136  0 105 TYR LLL CD2 1 ? 46 
ATOM   15124 C CE1 . TYR L  2 105 ? -19.099 -36.706  4.987   1.000 44.727  0 105 TYR LLL CE1 1 ? 46 
ATOM   15125 C CE2 . TYR L  2 105 ? -21.227 -37.533  5.662   1.000 43.286  0 105 TYR LLL CE2 1 ? 46 
ATOM   15126 C CZ  . TYR L  2 105 ? -20.450 -36.843  4.752   1.000 45.295  0 105 TYR LLL CZ  1 ? 46 
ATOM   15127 O OH  . TYR L  2 105 ? -21.018 -36.277  3.644   1.000 48.596  0 105 TYR LLL OH  1 ? 46 
ATOM   15128 N N   . TYR L  2 106 ? -16.347 -41.393  9.264   1.000 40.902  0 106 TYR LLL N   1 ? 46 
ATOM   15129 C CA  . TYR L  2 106 ? -15.998 -42.339  10.360  1.000 40.894  0 106 TYR LLL CA  1 ? 46 
ATOM   15130 C C   . TYR L  2 106 ? -15.405 -41.620  11.572  1.000 40.888  0 106 TYR LLL C   1 ? 46 
ATOM   15131 O O   . TYR L  2 106 ? -15.344 -42.267  12.632  1.000 40.971  0 106 TYR LLL O   1 ? 46 
ATOM   15132 C CB  . TYR L  2 106 ? -15.020 -43.411  9.882   1.000 42.832  0 106 TYR LLL CB  1 ? 46 
ATOM   15133 C CG  . TYR L  2 106 ? -13.757 -42.873  9.260   1.000 43.775  0 106 TYR LLL CG  1 ? 46 
ATOM   15134 C CD1 . TYR L  2 106 ? -12.682 -42.464  10.043  1.000 45.212  0 106 TYR LLL CD1 1 ? 46 
ATOM   15135 C CD2 . TYR L  2 106 ? -13.636 -42.789  7.883   1.000 44.349  0 106 TYR LLL CD2 1 ? 46 
ATOM   15136 C CE1 . TYR L  2 106 ? -11.520 -41.975  9.471   1.000 46.189  0 106 TYR LLL CE1 1 ? 46 
ATOM   15137 C CE2 . TYR L  2 106 ? -12.481 -42.301  7.300   1.000 46.435  0 106 TYR LLL CE2 1 ? 46 
ATOM   15138 C CZ  . TYR L  2 106 ? -11.425 -41.895  8.095   1.000 47.576  0 106 TYR LLL CZ  1 ? 46 
ATOM   15139 O OH  . TYR L  2 106 ? -10.303 -41.413  7.510   1.000 50.487  0 106 TYR LLL OH  1 ? 46 
ATOM   15140 N N   . THR L  2 107 ? -14.965 -40.362  11.434  1.000 35.820  0 107 THR LLL N   1 ? 47 
ATOM   15141 C CA  . THR L  2 107 ? -14.402 -39.559  12.561  1.000 34.725  0 107 THR LLL CA  1 ? 47 
ATOM   15142 C C   . THR L  2 107 ? -15.512 -38.875  13.370  1.000 34.297  0 107 THR LLL C   1 ? 47 
ATOM   15143 O O   . THR L  2 107 ? -15.199 -38.336  14.417  1.000 35.186  0 107 THR LLL O   1 ? 47 
ATOM   15144 C CB  . THR L  2 107 ? -13.381 -38.526  12.089  1.000 35.093  0 107 THR LLL CB  1 ? 47 
ATOM   15145 O OG1 . THR L  2 107 ? -14.064 -37.459  11.441  1.000 36.247  0 107 THR LLL OG1 1 ? 47 
ATOM   15146 C CG2 . THR L  2 107 ? -12.328 -39.100  11.171  1.000 36.628  0 107 THR LLL CG2 1 ? 47 
ATOM   15147 N N   . ARG L  2 108 ? -16.763 -38.889  12.918  1.000 35.621  0 108 ARG LLL N   1 ? 47 
ATOM   15148 C CA  . ARG L  2 108 ? -17.867 -38.188  13.639  1.000 38.006  0 108 ARG LLL CA  1 ? 47 
ATOM   15149 C C   . ARG L  2 108 ? -18.379 -39.028  14.799  1.000 36.459  0 108 ARG LLL C   1 ? 47 
ATOM   15150 O O   . ARG L  2 108 ? -18.853 -40.137  14.609  1.000 36.092  0 108 ARG LLL O   1 ? 47 
ATOM   15151 C CB  . ARG L  2 108 ? -19.059 -37.877  12.726  1.000 39.188  0 108 ARG LLL CB  1 ? 47 
ATOM   15152 C CG  . ARG L  2 108 ? -18.736 -36.829  11.688  1.000 39.520  0 108 ARG LLL CG  1 ? 47 
ATOM   15153 C CD  . ARG L  2 108 ? -19.989 -36.364  11.031  1.000 43.112  0 108 ARG LLL CD  1 ? 47 
ATOM   15154 N NE  . ARG L  2 108 ? -19.700 -35.615  9.821   1.000 44.227  0 108 ARG LLL NE  1 ? 47 
ATOM   15155 C CZ  . ARG L  2 108 ? -20.608 -35.303  8.921   1.000 47.539  0 108 ARG LLL CZ  1 ? 47 
ATOM   15156 N NH1 . ARG L  2 108 ? -21.865 -35.679  9.092   1.000 50.352  0 108 ARG LLL NH1 1 ? 47 
ATOM   15157 N NH2 . ARG L  2 108 ? -20.272 -34.631  7.840   1.000 50.975  0 108 ARG LLL NH2 1 ? 47 
ATOM   15158 N N   . PRO L  2 109 ? -18.328 -38.506  16.041  1.000 39.038  0 109 PRO LLL N   1 ? 47 
ATOM   15159 C CA  . PRO L  2 109 ? -18.946 -39.192  17.180  1.000 37.882  0 109 PRO LLL CA  1 ? 47 
ATOM   15160 C C   . PRO L  2 109 ? -20.415 -39.592  16.964  1.000 39.067  0 109 PRO LLL C   1 ? 47 
ATOM   15161 O O   . PRO L  2 109 ? -20.794 -40.690  17.366  1.000 39.518  0 109 PRO LLL O   1 ? 47 
ATOM   15162 C CB  . PRO L  2 109 ? -18.814 -38.182  18.314  1.000 36.917  0 109 PRO LLL CB  1 ? 47 
ATOM   15163 C CG  . PRO L  2 109 ? -17.567 -37.392  17.946  1.000 36.369  0 109 PRO LLL CG  1 ? 47 
ATOM   15164 C CD  . PRO L  2 109 ? -17.596 -37.288  16.436  1.000 37.720  0 109 PRO LLL CD  1 ? 47 
ATOM   15165 N N   . THR L  2 110 ? -21.205 -38.731  16.311  1.000 37.066  0 110 THR LLL N   1 ? 47 
ATOM   15166 C CA  . THR L  2 110 ? -22.659 -38.926  16.091  1.000 37.220  0 110 THR LLL CA  1 ? 47 
ATOM   15167 C C   . THR L  2 110 ? -22.912 -40.135  15.180  1.000 37.262  0 110 THR LLL C   1 ? 47 
ATOM   15168 O O   . THR L  2 110 ? -24.043 -40.594  15.160  1.000 37.180  0 110 THR LLL O   1 ? 47 
ATOM   15169 C CB  . THR L  2 110 ? -23.317 -37.648  15.561  1.000 39.800  0 110 THR LLL CB  1 ? 47 
ATOM   15170 O OG1 . THR L  2 110 ? -22.629 -37.222  14.377  1.000 40.608  0 110 THR LLL OG1 1 ? 47 
ATOM   15171 C CG2 . THR L  2 110 ? -23.334 -36.571  16.627  1.000 40.130  0 110 THR LLL CG2 1 ? 47 
ATOM   15172 N N   . GLU L  2 111 ? -21.915 -40.654  14.469  1.000 37.733  0 111 GLU LLL N   1 ? 47 
ATOM   15173 C CA  . GLU L  2 111 ? -22.079 -41.860  13.601  1.000 40.705  0 111 GLU LLL CA  1 ? 47 
ATOM   15174 C C   . GLU L  2 111 ? -22.011 -43.164  14.425  1.000 40.958  0 111 GLU LLL C   1 ? 47 
ATOM   15175 O O   . GLU L  2 111 ? -22.227 -44.251  13.841  1.000 41.548  0 111 GLU LLL O   1 ? 47 
ATOM   15176 C CB  . GLU L  2 111 ? -21.053 -41.854  12.472  1.000 40.203  0 111 GLU LLL CB  1 ? 47 
ATOM   15177 C CG  . GLU L  2 111 ? -21.291 -40.742  11.453  1.000 41.900  0 111 GLU LLL CG  1 ? 47 
ATOM   15178 C CD  . GLU L  2 111 ? -22.525 -40.878  10.591  1.000 44.504  0 111 GLU LLL CD  1 ? 47 
ATOM   15179 O OE1 . GLU L  2 111 ? -23.644 -40.782  11.129  1.000 43.345  0 111 GLU LLL OE1 1 ? 47 
ATOM   15180 O OE2 . GLU L  2 111 ? -22.349 -41.061  9.370   1.000 49.659  0 111 GLU LLL OE2 1 ? 47 
ATOM   15181 N N   . TYR L  2 112 ? -21.738 -43.103  15.735  1.000 38.534  0 112 TYR LLL N   1 ? 47 
ATOM   15182 C CA  . TYR L  2 112 ? -21.637 -44.314  16.592  1.000 36.109  0 112 TYR LLL CA  1 ? 47 
ATOM   15183 C C   . TYR L  2 112 ? -22.714 -44.252  17.683  1.000 36.455  0 112 TYR LLL C   1 ? 47 
ATOM   15184 O O   . TYR L  2 112 ? -22.736 -43.320  18.475  1.000 38.097  0 112 TYR LLL O   1 ? 47 
ATOM   15185 C CB  . TYR L  2 112 ? -20.217 -44.432  17.144  1.000 38.349  0 112 TYR LLL CB  1 ? 47 
ATOM   15186 C CG  . TYR L  2 112 ? -19.141 -44.465  16.080  1.000 37.985  0 112 TYR LLL CG  1 ? 47 
ATOM   15187 C CD1 . TYR L  2 112 ? -18.630 -43.308  15.536  1.000 35.264  0 112 TYR LLL CD1 1 ? 47 
ATOM   15188 C CD2 . TYR L  2 112 ? -18.658 -45.671  15.593  1.000 39.778  0 112 TYR LLL CD2 1 ? 47 
ATOM   15189 C CE1 . TYR L  2 112 ? -17.650 -43.342  14.555  1.000 36.185  0 112 TYR LLL CE1 1 ? 47 
ATOM   15190 C CE2 . TYR L  2 112 ? -17.676 -45.720  14.614  1.000 38.073  0 112 TYR LLL CE2 1 ? 47 
ATOM   15191 C CZ  . TYR L  2 112 ? -17.161 -44.553  14.097  1.000 36.238  0 112 TYR LLL CZ  1 ? 47 
ATOM   15192 O OH  . TYR L  2 112 ? -16.218 -44.614  13.116  1.000 33.240  0 112 TYR LLL OH  1 ? 47 
ATOM   15193 N N   . GLU L  2 113 ? -23.619 -45.221  17.726  1.000 37.846  0 113 GLU LLL N   1 ? 47 
ATOM   15194 C CA  . GLU L  2 113 ? -24.767 -45.210  18.658  1.000 38.863  0 113 GLU LLL CA  1 ? 47 
ATOM   15195 C C   . GLU L  2 113 ? -24.313 -45.520  20.094  1.000 38.978  0 113 GLU LLL C   1 ? 47 
ATOM   15196 O O   . GLU L  2 113 ? -24.876 -44.931  21.016  1.000 36.571  0 113 GLU LLL O   1 ? 47 
ATOM   15197 C CB  . GLU L  2 113 ? -25.833 -46.210  18.230  1.000 41.511  0 113 GLU LLL CB  1 ? 47 
ATOM   15198 C CG  . GLU L  2 113 ? -27.048 -46.169  19.131  1.000 45.114  0 113 GLU LLL CG  1 ? 47 
ATOM   15199 C CD  . GLU L  2 113 ? -28.218 -47.033  18.677  1.000 49.656  0 113 GLU LLL CD  1 ? 47 
ATOM   15200 O OE1 . GLU L  2 113 ? -28.127 -47.618  17.569  1.000 46.529  0 113 GLU LLL OE1 1 ? 47 
ATOM   15201 O OE2 . GLU L  2 113 ? -29.218 -47.151  19.448  1.000 54.992  0 113 GLU LLL OE2 1 ? 47 
ATOM   15202 N N   . PHE L  2 114 ? -23.370 -46.442  20.285  1.000 37.655  0 114 PHE LLL N   1 ? 47 
ATOM   15203 C CA  . PHE L  2 114 ? -23.003 -47.012  21.605  1.000 36.575  0 114 PHE LLL CA  1 ? 47 
ATOM   15204 C C   . PHE L  2 114 ? -21.605 -46.542  22.010  1.000 37.892  0 114 PHE LLL C   1 ? 47 
ATOM   15205 O O   . PHE L  2 114 ? -20.668 -46.603  21.196  1.000 40.473  0 114 PHE LLL O   1 ? 47 
ATOM   15206 C CB  . PHE L  2 114 ? -23.069 -48.537  21.548  1.000 36.065  0 114 PHE LLL CB  1 ? 47 
ATOM   15207 C CG  . PHE L  2 114 ? -24.446 -49.029  21.215  1.000 35.586  0 114 PHE LLL CG  1 ? 47 
ATOM   15208 C CD1 . PHE L  2 114 ? -25.507 -48.775  22.075  1.000 37.304  0 114 PHE LLL CD1 1 ? 47 
ATOM   15209 C CD2 . PHE L  2 114 ? -24.703 -49.687  20.021  1.000 37.306  0 114 PHE LLL CD2 1 ? 47 
ATOM   15210 C CE1 . PHE L  2 114 ? -26.798 -49.195  21.762  1.000 38.049  0 114 PHE LLL CE1 1 ? 47 
ATOM   15211 C CE2 . PHE L  2 114 ? -25.986 -50.111  19.700  1.000 38.768  0 114 PHE LLL CE2 1 ? 47 
ATOM   15212 C CZ  . PHE L  2 114 ? -27.030 -49.862  20.573  1.000 39.933  0 114 PHE LLL CZ  1 ? 47 
ATOM   15213 N N   . TRP L  2 115 ? -21.484 -46.111  23.264  1.000 36.536  0 115 TRP LLL N   1 ? 47 
ATOM   15214 C CA  . TRP L  2 115 ? -20.263 -45.538  23.866  1.000 35.645  0 115 TRP LLL CA  1 ? 47 
ATOM   15215 C C   . TRP L  2 115 ? -19.995 -46.169  25.226  1.000 34.516  0 115 TRP LLL C   1 ? 47 
ATOM   15216 O O   . TRP L  2 115 ? -20.923 -46.178  26.063  1.000 36.545  0 115 TRP LLL O   1 ? 47 
ATOM   15217 C CB  . TRP L  2 115 ? -20.423 -44.021  24.002  1.000 36.703  0 115 TRP LLL CB  1 ? 47 
ATOM   15218 C CG  . TRP L  2 115 ? -20.412 -43.338  22.680  1.000 36.758  0 115 TRP LLL CG  1 ? 47 
ATOM   15219 C CD1 . TRP L  2 115 ? -21.452 -43.238  21.808  1.000 37.477  0 115 TRP LLL CD1 1 ? 47 
ATOM   15220 C CD2 . TRP L  2 115 ? -19.276 -42.748  22.036  1.000 37.004  0 115 TRP LLL CD2 1 ? 47 
ATOM   15221 N NE1 . TRP L  2 115 ? -21.033 -42.625  20.661  1.000 38.330  0 115 TRP LLL NE1 1 ? 47 
ATOM   15222 C CE2 . TRP L  2 115 ? -19.704 -42.311  20.774  1.000 37.921  0 115 TRP LLL CE2 1 ? 47 
ATOM   15223 C CE3 . TRP L  2 115 ? -17.944 -42.547  22.394  1.000 40.657  0 115 TRP LLL CE3 1 ? 47 
ATOM   15224 C CZ2 . TRP L  2 115 ? -18.857 -41.669  19.876  1.000 38.234  0 115 TRP LLL CZ2 1 ? 47 
ATOM   15225 C CZ3 . TRP L  2 115 ? -17.107 -41.894  21.517  1.000 41.152  0 115 TRP LLL CZ3 1 ? 47 
ATOM   15226 C CH2 . TRP L  2 115 ? -17.563 -41.459  20.275  1.000 40.476  0 115 TRP LLL CH2 1 ? 47 
ATOM   15227 N N   . GLY L  2 116 ? -18.755 -46.576  25.460  1.000 33.175  0 116 GLY LLL N   1 ? 47 
ATOM   15228 C CA  . GLY L  2 116 ? -18.277 -46.877  26.821  1.000 37.404  0 116 GLY LLL CA  1 ? 47 
ATOM   15229 C C   . GLY L  2 116 ? -18.166 -45.607  27.655  1.000 36.438  0 116 GLY LLL C   1 ? 47 
ATOM   15230 O O   . GLY L  2 116 ? -18.368 -44.518  27.107  1.000 39.866  0 116 GLY LLL O   1 ? 47 
ATOM   15231 N N   . GLN L  2 117 ? -17.869 -45.739  28.940  1.000 38.522  0 117 GLN LLL N   1 ? 47 
ATOM   15232 C CA  . GLN L  2 117 ? -17.712 -44.586  29.881  1.000 40.360  0 117 GLN LLL CA  1 ? 47 
ATOM   15233 C C   . GLN L  2 117 ? -16.274 -44.048  29.771  1.000 40.575  0 117 GLN LLL C   1 ? 47 
ATOM   15234 O O   . GLN L  2 117 ? -16.029 -42.916  30.247  1.000 40.765  0 117 GLN LLL O   1 ? 47 
ATOM   15235 C CB  . GLN L  2 117 ? -17.998 -44.981  31.326  1.000 38.739  0 117 GLN LLL CB  1 ? 47 
ATOM   15236 C CG  . GLN L  2 117 ? -19.373 -45.601  31.518  1.000 42.292  0 117 GLN LLL CG  1 ? 47 
ATOM   15237 C CD  . GLN L  2 117 ? -20.519 -44.697  31.107  1.000 44.178  0 117 GLN LLL CD  1 ? 47 
ATOM   15238 O OE1 . GLN L  2 117 ? -20.614 -43.522  31.487  1.000 47.062  0 117 GLN LLL OE1 1 ? 47 
ATOM   15239 N NE2 . GLN L  2 117 ? -21.446 -45.265  30.364  1.000 41.144  0 117 GLN LLL NE2 1 ? 47 
ATOM   15240 N N   . GLY L  2 118 ? -15.364 -44.812  29.167  1.000 38.092  0 118 GLY LLL N   1 ? 47 
ATOM   15241 C CA  . GLY L  2 118 ? -13.967 -44.407  28.952  1.000 40.365  0 118 GLY LLL CA  1 ? 47 
ATOM   15242 C C   . GLY L  2 118 ? -13.030 -44.888  30.073  1.000 41.497  0 118 GLY LLL C   1 ? 47 
ATOM   15243 O O   . GLY L  2 118 ? -13.513 -45.204  31.174  1.000 40.221  0 118 GLY LLL O   1 ? 47 
ATOM   15244 N N   . THR L  2 119 ? -11.731 -44.930  29.785  1.000 41.451  0 119 THR LLL N   1 ? 47 
ATOM   15245 C CA  . THR L  2 119 ? -10.654 -45.263  30.744  1.000 42.280  0 119 THR LLL CA  1 ? 47 
ATOM   15246 C C   . THR L  2 119 ? -9.504  -44.257  30.541  1.000 41.839  0 119 THR LLL C   1 ? 47 
ATOM   15247 O O   . THR L  2 119 ? -9.205  -43.907  29.396  1.000 40.328  0 119 THR LLL O   1 ? 47 
ATOM   15248 C CB  . THR L  2 119 ? -10.255 -46.730  30.576  1.000 43.287  0 119 THR LLL CB  1 ? 47 
ATOM   15249 O OG1 . THR L  2 119 ? -9.468  -47.129  31.699  1.000 44.858  0 119 THR LLL OG1 1 ? 47 
ATOM   15250 C CG2 . THR L  2 119 ? -9.501  -46.984  29.289  1.000 44.149  0 119 THR LLL CG2 1 ? 47 
ATOM   15251 N N   . GLN L  2 120 ? -8.934  -43.773  31.635  1.000 42.619  0 120 GLN LLL N   1 ? 47 
ATOM   15252 C CA  . GLN L  2 120 ? -7.831  -42.789  31.644  1.000 44.225  0 120 GLN LLL CA  1 ? 47 
ATOM   15253 C C   . GLN L  2 120 ? -6.548  -43.475  31.169  1.000 45.627  0 120 GLN LLL C   1 ? 47 
ATOM   15254 O O   . GLN L  2 120 ? -6.224  -44.544  31.680  1.000 49.836  0 120 GLN LLL O   1 ? 47 
ATOM   15255 C CB  . GLN L  2 120 ? -7.677  -42.186  33.040  1.000 45.784  0 120 GLN LLL CB  1 ? 47 
ATOM   15256 C CG  . GLN L  2 120 ? -6.688  -41.032  33.122  1.000 47.764  0 120 GLN LLL CG  1 ? 47 
ATOM   15257 C CD  . GLN L  2 120 ? -7.132  -39.833  32.322  1.000 49.359  0 120 GLN LLL CD  1 ? 47 
ATOM   15258 O OE1 . GLN L  2 120 ? -8.293  -39.396  32.386  1.000 46.491  0 120 GLN LLL OE1 1 ? 47 
ATOM   15259 N NE2 . GLN L  2 120 ? -6.202  -39.299  31.533  1.000 55.054  0 120 GLN LLL NE2 1 ? 47 
ATOM   15260 N N   . VAL L  2 121 ? -5.875  -42.870  30.195  1.000 44.235  0 121 VAL LLL N   1 ? 47 
ATOM   15261 C CA  . VAL L  2 121 ? -4.451  -43.117  29.858  1.000 45.903  0 121 VAL LLL CA  1 ? 47 
ATOM   15262 C C   . VAL L  2 121 ? -3.668  -41.845  30.219  1.000 46.990  0 121 VAL LLL C   1 ? 47 
ATOM   15263 O O   . VAL L  2 121 ? -4.066  -40.764  29.768  1.000 49.225  0 121 VAL LLL O   1 ? 47 
ATOM   15264 C CB  . VAL L  2 121 ? -4.299  -43.466  28.371  1.000 45.693  0 121 VAL LLL CB  1 ? 47 
ATOM   15265 C CG1 . VAL L  2 121 ? -2.831  -43.608  27.993  1.000 48.929  0 121 VAL LLL CG1 1 ? 47 
ATOM   15266 C CG2 . VAL L  2 121 ? -5.060  -44.721  28.016  1.000 44.696  0 121 VAL LLL CG2 1 ? 47 
ATOM   15267 N N   . THR L  2 122 ? -2.618  -41.958  31.025  1.000 47.831  0 122 THR LLL N   1 ? 47 
ATOM   15268 C CA  . THR L  2 122 ? -1.753  -40.816  31.413  1.000 50.756  0 122 THR LLL CA  1 ? 47 
ATOM   15269 C C   . THR L  2 122 ? -0.311  -41.140  31.009  1.000 52.805  0 122 THR LLL C   1 ? 47 
ATOM   15270 O O   . THR L  2 122 ? 0.189   -42.204  31.418  1.000 53.150  0 122 THR LLL O   1 ? 47 
ATOM   15271 C CB  . THR L  2 122 ? -1.916  -40.474  32.903  1.000 52.304  0 122 THR LLL CB  1 ? 47 
ATOM   15272 O OG1 . THR L  2 122 ? -3.294  -40.175  33.113  1.000 49.944  0 122 THR LLL OG1 1 ? 47 
ATOM   15273 C CG2 . THR L  2 122 ? -1.075  -39.300  33.357  1.000 53.077  0 122 THR LLL CG2 1 ? 47 
ATOM   15274 N N   . VAL L  2 123 ? 0.298   -40.273  30.198  1.000 53.403  0 123 VAL LLL N   1 ? 47 
ATOM   15275 C CA  . VAL L  2 123 ? 1.699   -40.427  29.717  1.000 58.576  0 123 VAL LLL CA  1 ? 47 
ATOM   15276 C C   . VAL L  2 123 ? 2.544   -39.340  30.401  1.000 64.398  0 123 VAL LLL C   1 ? 47 
ATOM   15277 O O   . VAL L  2 123 ? 2.317   -38.155  30.070  1.000 67.712  0 123 VAL LLL O   1 ? 47 
ATOM   15278 C CB  . VAL L  2 123 ? 1.745   -40.364  28.177  1.000 55.823  0 123 VAL LLL CB  1 ? 47 
ATOM   15279 C CG1 . VAL L  2 123 ? 3.102   -40.752  27.636  1.000 59.028  0 123 VAL LLL CG1 1 ? 47 
ATOM   15280 C CG2 . VAL L  2 123 ? 0.695   -41.247  27.536  1.000 53.518  0 123 VAL LLL CG2 1 ? 47 
ATOM   15281 N N   . SER L  2 124 ? 3.418   -39.708  31.352  1.000 70.082  0 124 SER LLL N   1 ? 47 
ATOM   15282 C CA  . SER L  2 124 ? 4.348   -38.767  32.039  1.000 80.038  0 124 SER LLL CA  1 ? 47 
ATOM   15283 C C   . SER L  2 124 ? 5.564   -38.511  31.145  1.000 89.344  0 124 SER LLL C   1 ? 47 
ATOM   15284 O O   . SER L  2 124 ? 5.826   -39.355  30.266  1.000 87.484  0 124 SER LLL O   1 ? 47 
ATOM   15285 C CB  . SER L  2 124 ? 4.787   -39.283  33.372  1.000 81.603  0 124 SER LLL CB  1 ? 47 
ATOM   15286 O OG  . SER L  2 124 ? 5.392   -40.551  33.228  1.000 83.343  0 124 SER LLL OG  1 ? 47 
ATOM   15287 N N   . SER L  2 125 ? 6.273   -37.399  31.365  1.000 73.469  0 125 SER LLL N   1 ? ?  
ATOM   15288 C CA  . SER L  2 125 ? 7.444   -36.965  30.551  1.000 77.843  0 125 SER LLL CA  1 ? ?  
ATOM   15289 C C   . SER L  2 125 ? 8.730   -37.146  31.361  1.000 80.622  0 125 SER LLL C   1 ? ?  
ATOM   15290 O O   . SER L  2 125 ? 9.330   -38.223  31.338  1.000 83.523  0 125 SER LLL O   1 ? ?  
ATOM   15291 C CB  . SER L  2 125 ? 7.288   -35.542  30.087  1.000 79.455  0 125 SER LLL CB  1 ? ?  
ATOM   15292 O OG  . SER L  2 125 ? 5.918   -35.220  29.927  1.000 82.492  0 125 SER LLL OG  1 ? ?  
HETATM 15293 C C1  . NAG M  3 .   ? 24.362  -2.239   -10.493 1.000 46.401  0 601 NAG AAA C1  1 ? ?  
HETATM 15294 C C2  . NAG M  3 .   ? 25.775  -2.642   -10.921 1.000 47.558  0 601 NAG AAA C2  1 ? ?  
HETATM 15295 C C3  . NAG M  3 .   ? 26.871  -1.758   -10.314 1.000 48.547  0 601 NAG AAA C3  1 ? ?  
HETATM 15296 C C4  . NAG M  3 .   ? 26.502  -0.288   -10.317 1.000 47.824  0 601 NAG AAA C4  1 ? ?  
HETATM 15297 C C5  . NAG M  3 .   ? 25.104  -0.098   -9.750  1.000 47.459  0 601 NAG AAA C5  1 ? ?  
HETATM 15298 C C6  . NAG M  3 .   ? 24.679  1.346    -9.793  1.000 45.418  0 601 NAG AAA C6  1 ? ?  
HETATM 15299 C C7  . NAG M  3 .   ? 26.370  -4.968   -11.328 1.000 44.534  0 601 NAG AAA C7  1 ? ?  
HETATM 15300 C C8  . NAG M  3 .   ? 26.710  -6.313   -10.762 1.000 45.036  0 601 NAG AAA C8  1 ? ?  
HETATM 15301 N N2  . NAG M  3 .   ? 26.058  -4.002   -10.484 1.000 45.731  0 601 NAG AAA N2  1 ? ?  
HETATM 15302 O O3  . NAG M  3 .   ? 28.108  -1.898   -11.031 1.000 53.090  0 601 NAG AAA O3  1 ? ?  
HETATM 15303 O O4  . NAG M  3 .   ? 27.453  0.399    -9.517  1.000 44.345  0 601 NAG AAA O4  1 ? ?  
HETATM 15304 O O5  . NAG M  3 .   ? 24.167  -0.840   -10.533 1.000 49.135  0 601 NAG AAA O5  1 ? ?  
HETATM 15305 O O6  . NAG M  3 .   ? 23.277  1.395    -9.525  1.000 46.320  0 601 NAG AAA O6  1 ? ?  
HETATM 15306 O O7  . NAG M  3 .   ? 26.390  -4.774   -12.517 1.000 46.850  0 601 NAG AAA O7  1 ? ?  
HETATM 15307 C C1  . NAG N  3 .   ? 23.056  -60.999  -8.149  1.000 48.944  0 601 NAG CCC C1  1 ? ?  
HETATM 15308 C C2  . NAG N  3 .   ? 24.380  -61.643  -8.605  1.000 52.312  0 601 NAG CCC C2  1 ? ?  
HETATM 15309 C C3  . NAG N  3 .   ? 25.596  -60.842  -8.106  1.000 52.214  0 601 NAG CCC C3  1 ? ?  
HETATM 15310 C C4  . NAG N  3 .   ? 25.408  -59.328  -7.974  1.000 53.324  0 601 NAG CCC C4  1 ? ?  
HETATM 15311 C C5  . NAG N  3 .   ? 24.008  -58.992  -7.485  1.000 54.367  0 601 NAG CCC C5  1 ? ?  
HETATM 15312 C C6  . NAG N  3 .   ? 23.689  -57.513  -7.414  1.000 53.873  0 601 NAG CCC C6  1 ? ?  
HETATM 15313 C C7  . NAG N  3 .   ? 24.622  -64.100  -8.899  1.000 53.301  0 601 NAG CCC C7  1 ? ?  
HETATM 15314 C C8  . NAG N  3 .   ? 24.941  -65.410  -8.231  1.000 54.763  0 601 NAG CCC C8  1 ? ?  
HETATM 15315 N N2  . NAG N  3 .   ? 24.570  -63.015  -8.112  1.000 51.963  0 601 NAG CCC N2  1 ? ?  
HETATM 15316 O O3  . NAG N  3 .   ? 26.637  -61.115  -9.026  1.000 58.869  0 601 NAG CCC O3  1 ? ?  
HETATM 15317 O O4  . NAG N  3 .   ? 26.317  -58.805  -7.000  1.000 50.895  0 601 NAG CCC O4  1 ? ?  
HETATM 15318 O O5  . NAG N  3 .   ? 23.098  -59.595  -8.387  1.000 52.737  0 601 NAG CCC O5  1 ? ?  
HETATM 15319 O O6  . NAG N  3 .   ? 22.313  -57.434  -7.025  1.000 57.921  0 601 NAG CCC O6  1 ? ?  
HETATM 15320 O O7  . NAG N  3 .   ? 24.443  -64.055  -10.098 1.000 53.360  0 601 NAG CCC O7  1 ? ?  
HETATM 15321 C C1  . NAG O  3 .   ? 32.313  -31.327  9.015   1.000 45.567  0 601 NAG EEE C1  1 ? ?  
HETATM 15322 C C2  . NAG O  3 .   ? 30.921  -31.703  9.540   1.000 51.678  0 601 NAG EEE C2  1 ? ?  
HETATM 15323 C C3  . NAG O  3 .   ? 29.813  -30.831  8.949   1.000 50.004  0 601 NAG EEE C3  1 ? ?  
HETATM 15324 C C4  . NAG O  3 .   ? 30.162  -29.347  8.900   1.000 50.587  0 601 NAG EEE C4  1 ? ?  
HETATM 15325 C C5  . NAG O  3 .   ? 31.553  -29.165  8.308   1.000 49.160  0 601 NAG EEE C5  1 ? ?  
HETATM 15326 C C6  . NAG O  3 .   ? 32.028  -27.726  8.308   1.000 49.775  0 601 NAG EEE C6  1 ? ?  
HETATM 15327 C C7  . NAG O  3 .   ? 30.283  -34.030  10.158  1.000 57.833  0 601 NAG EEE C7  1 ? ?  
HETATM 15328 C C8  . NAG O  3 .   ? 29.815  -35.341  9.592   1.000 57.932  0 601 NAG EEE C8  1 ? ?  
HETATM 15329 N N2  . NAG O  3 .   ? 30.544  -33.081  9.233   1.000 55.737  0 601 NAG EEE N2  1 ? ?  
HETATM 15330 O O3  . NAG O  3 .   ? 28.670  -30.989  9.782   1.000 52.554  0 601 NAG EEE O3  1 ? ?  
HETATM 15331 O O4  . NAG O  3 .   ? 29.177  -28.672  8.114   1.000 44.879  0 601 NAG EEE O4  1 ? ?  
HETATM 15332 O O5  . NAG O  3 .   ? 32.479  -29.910  9.085   1.000 48.961  0 601 NAG EEE O5  1 ? ?  
HETATM 15333 O O6  . NAG O  3 .   ? 33.276  -27.676  7.585   1.000 52.498  0 601 NAG EEE O6  1 ? ?  
HETATM 15334 O O7  . NAG O  3 .   ? 30.397  -33.886  11.372  1.000 58.405  0 601 NAG EEE O7  1 ? ?  
HETATM 15335 C C1  . NAG P  3 .   ? 11.187  -21.092  59.693  1.000 77.364  0 601 NAG GGG C1  1 ? ?  
HETATM 15336 C C2  . NAG P  3 .   ? 11.638  -22.080  60.777  1.000 86.400  0 601 NAG GGG C2  1 ? ?  
HETATM 15337 C C3  . NAG P  3 .   ? 12.034  -23.453  60.181  1.000 92.470  0 601 NAG GGG C3  1 ? ?  
HETATM 15338 C C4  . NAG P  3 .   ? 11.176  -23.893  58.964  1.000 95.651  0 601 NAG GGG C4  1 ? ?  
HETATM 15339 C C5  . NAG P  3 .   ? 10.906  -22.722  58.008  1.000 94.036  0 601 NAG GGG C5  1 ? ?  
HETATM 15340 C C6  . NAG P  3 .   ? 10.058  -23.028  56.763  1.000 91.459  0 601 NAG GGG C6  1 ? ?  
HETATM 15341 C C7  . NAG P  3 .   ? 13.730  -20.755  61.483  1.000 88.642  0 601 NAG GGG C7  1 ? ?  
HETATM 15342 C C8  . NAG P  3 .   ? 14.496  -20.346  62.738  1.000 82.707  0 601 NAG GGG C8  1 ? ?  
HETATM 15343 N N2  . NAG P  3 .   ? 12.674  -21.574  61.698  1.000 92.603  0 601 NAG GGG N2  1 ? ?  
HETATM 15344 O O3  . NAG P  3 .   ? 11.906  -24.452  61.208  1.000 83.761  0 601 NAG GGG O3  1 ? ?  
HETATM 15345 O O4  . NAG P  3 .   ? 11.796  -24.961  58.230  1.000 86.739  0 601 NAG GGG O4  1 ? ?  
HETATM 15346 O O5  . NAG P  3 .   ? 10.263  -21.732  58.810  1.000 88.719  0 601 NAG GGG O5  1 ? ?  
HETATM 15347 O O6  . NAG P  3 .   ? 8.672   -23.225  57.095  1.000 84.478  0 601 NAG GGG O6  1 ? ?  
HETATM 15348 O O7  . NAG P  3 .   ? 14.065  -20.339  60.386  1.000 76.688  0 601 NAG GGG O7  1 ? ?  
HETATM 15349 C C1  . NAG Q  3 .   ? 14.706  -81.520  63.006  1.000 73.555  0 601 NAG III C1  1 ? ?  
HETATM 15350 C C2  . NAG Q  3 .   ? 15.751  -82.455  63.612  1.000 78.496  0 601 NAG III C2  1 ? ?  
HETATM 15351 C C3  . NAG Q  3 .   ? 15.539  -83.886  63.086  1.000 82.199  0 601 NAG III C3  1 ? ?  
HETATM 15352 C C4  . NAG Q  3 .   ? 14.083  -84.336  63.255  1.000 86.725  0 601 NAG III C4  1 ? ?  
HETATM 15353 C C5  . NAG Q  3 .   ? 13.094  -83.295  62.711  1.000 89.390  0 601 NAG III C5  1 ? ?  
HETATM 15354 C C6  . NAG Q  3 .   ? 11.615  -83.638  62.957  1.000 83.051  0 601 NAG III C6  1 ? ?  
HETATM 15355 C C7  . NAG Q  3 .   ? 18.041  -81.675  64.181  1.000 80.706  0 601 NAG III C7  1 ? ?  
HETATM 15356 C C8  . NAG Q  3 .   ? 19.304  -81.122  63.582  1.000 79.621  0 601 NAG III C8  1 ? ?  
HETATM 15357 N N2  . NAG Q  3 .   ? 17.074  -81.943  63.290  1.000 78.013  0 601 NAG III N2  1 ? ?  
HETATM 15358 O O3  . NAG Q  3 .   ? 16.399  -84.828  63.747  1.000 72.876  0 601 NAG III O3  1 ? ?  
HETATM 15359 O O4  . NAG Q  3 .   ? 13.912  -85.572  62.558  1.000 96.786  0 601 NAG III O4  1 ? ?  
HETATM 15360 O O5  . NAG Q  3 .   ? 13.400  -82.032  63.308  1.000 84.996  0 601 NAG III O5  1 ? ?  
HETATM 15361 O O6  . NAG Q  3 .   ? 11.171  -83.149  64.234  1.000 77.795  0 601 NAG III O6  1 ? ?  
HETATM 15362 O O7  . NAG Q  3 .   ? 17.942  -81.841  65.393  1.000 83.367  0 601 NAG III O7  1 ? ?  
HETATM 15363 C C1  . NAG R  3 .   ? -27.721 -31.526  -5.723  1.000 76.409  0 601 NAG KKK C1  1 ? ?  
HETATM 15364 C C2  . NAG R  3 .   ? -26.627 -31.964  -6.725  1.000 84.955  0 601 NAG KKK C2  1 ? ?  
HETATM 15365 C C3  . NAG R  3 .   ? -25.192 -31.500  -6.318  1.000 86.198  0 601 NAG KKK C3  1 ? ?  
HETATM 15366 C C4  . NAG R  3 .   ? -25.095 -30.371  -5.244  1.000 89.066  0 601 NAG KKK C4  1 ? ?  
HETATM 15367 C C5  . NAG R  3 .   ? -26.345 -30.153  -4.389  1.000 88.902  0 601 NAG KKK C5  1 ? ?  
HETATM 15368 C C6  . NAG R  3 .   ? -26.243 -28.844  -3.591  1.000 87.396  0 601 NAG KKK C6  1 ? ?  
HETATM 15369 C C7  . NAG R  3 .   ? -26.633 -34.350  -6.009  1.000 79.588  0 601 NAG KKK C7  1 ? ?  
HETATM 15370 C C8  . NAG R  3 .   ? -26.796 -35.780  -6.422  1.000 76.127  0 601 NAG KKK C8  1 ? ?  
HETATM 15371 N N2  . NAG R  3 .   ? -26.706 -33.419  -6.973  1.000 79.740  0 601 NAG KKK N2  1 ? ?  
HETATM 15372 O O3  . NAG R  3 .   ? -24.520 -31.043  -7.516  1.000 72.416  0 601 NAG KKK O3  1 ? ?  
HETATM 15373 O O4  . NAG R  3 .   ? -24.033 -30.560  -4.295  1.000 82.134  0 601 NAG KKK O4  1 ? ?  
HETATM 15374 O O5  . NAG R  3 .   ? -27.507 -30.188  -5.239  1.000 84.812  0 601 NAG KKK O5  1 ? ?  
HETATM 15375 O O6  . NAG R  3 .   ? -26.271 -27.727  -4.486  1.000 85.183  0 601 NAG KKK O6  1 ? ?  
HETATM 15376 O O7  . NAG R  3 .   ? -26.451 -34.076  -4.828  1.000 84.545  0 601 NAG KKK O7  1 ? ?  
HETATM 15377 O O   . HOH S  4 .   ? 26.558  -14.919  5.077   1.000 33.180  0 701 HOH AAA O   1 ? ?  
HETATM 15378 O O   . HOH S  4 .   ? 6.827   -5.342   2.264   1.000 53.901  0 702 HOH AAA O   1 ? ?  
HETATM 15379 O O   . HOH S  4 .   ? 23.427  -15.713  14.332  1.000 52.347  0 703 HOH AAA O   1 ? ?  
HETATM 15380 O O   . HOH S  4 .   ? 33.227  0.959    -8.281  1.000 43.036  0 704 HOH AAA O   1 ? ?  
HETATM 15381 O O   . HOH S  4 .   ? 12.276  0.525    5.841   1.000 64.020  0 705 HOH AAA O   1 ? ?  
HETATM 15382 O O   . HOH S  4 .   ? 10.275  -11.503  8.964   1.000 71.170  0 706 HOH AAA O   1 ? ?  
HETATM 15383 O O   . HOH S  4 .   ? 22.835  -24.653  7.619   1.000 35.641  0 707 HOH AAA O   1 ? ?  
HETATM 15384 O O   . HOH S  4 .   ? 22.178  -20.040  -4.908  1.000 44.110  0 708 HOH AAA O   1 ? ?  
HETATM 15385 O O   . HOH S  4 .   ? 17.781  -14.621  -8.378  1.000 33.462  0 709 HOH AAA O   1 ? ?  
HETATM 15386 O O   . HOH S  4 .   ? 15.128  7.225    -5.396  1.000 44.159  0 710 HOH AAA O   1 ? ?  
HETATM 15387 O O   . HOH S  4 .   ? 17.990  -10.887  -8.688  1.000 40.583  0 711 HOH AAA O   1 ? ?  
HETATM 15388 O O   . HOH S  4 .   ? 3.732   -22.915  6.309   1.000 39.267  0 712 HOH AAA O   1 ? ?  
HETATM 15389 O O   . HOH S  4 .   ? 19.262  -3.902   -6.628  1.000 31.330  0 713 HOH AAA O   1 ? ?  
HETATM 15390 O O   . HOH S  4 .   ? 17.960  3.971    4.734   1.000 49.010  0 714 HOH AAA O   1 ? ?  
HETATM 15391 O O   . HOH S  4 .   ? 10.596  -20.921  0.821   1.000 41.752  0 715 HOH AAA O   1 ? ?  
HETATM 15392 O O   . HOH S  4 .   ? 8.562   -20.523  2.716   1.000 48.990  0 716 HOH AAA O   1 ? ?  
HETATM 15393 O O   . HOH S  4 .   ? 3.920   -25.144  4.611   1.000 39.747  0 717 HOH AAA O   1 ? ?  
HETATM 15394 O O   . HOH S  4 .   ? 17.784  -12.473  12.795  1.000 36.528  0 718 HOH AAA O   1 ? ?  
HETATM 15395 O O   . HOH S  4 .   ? 21.147  -21.753  7.716   1.000 43.838  0 719 HOH AAA O   1 ? ?  
HETATM 15396 O O   . HOH S  4 .   ? 27.382  -5.137   8.093   1.000 41.292  0 720 HOH AAA O   1 ? ?  
HETATM 15397 O O   . HOH S  4 .   ? 8.271   -8.809   -5.162  1.000 42.441  0 721 HOH AAA O   1 ? ?  
HETATM 15398 O O   . HOH S  4 .   ? 13.088  -2.041   -7.851  1.000 37.384  0 722 HOH AAA O   1 ? ?  
HETATM 15399 O O   . HOH S  4 .   ? 14.564  -11.818  -6.527  1.000 41.208  0 723 HOH AAA O   1 ? ?  
HETATM 15400 O O   . HOH S  4 .   ? 10.326  -10.830  1.330   1.000 38.949  0 724 HOH AAA O   1 ? ?  
HETATM 15401 O O   . HOH S  4 .   ? 21.757  -9.156   10.137  1.000 37.172  0 725 HOH AAA O   1 ? ?  
HETATM 15402 O O   . HOH S  4 .   ? 15.782  -24.654  7.979   1.000 30.197  0 726 HOH AAA O   1 ? ?  
HETATM 15403 O O   . HOH S  4 .   ? 39.582  -20.406  -2.319  1.000 40.840  0 727 HOH AAA O   1 ? ?  
HETATM 15404 O O   . HOH S  4 .   ? 18.717  2.413    0.545   1.000 43.784  0 728 HOH AAA O   1 ? ?  
HETATM 15405 O O   . HOH S  4 .   ? 19.742  -19.694  5.689   1.000 34.776  0 729 HOH AAA O   1 ? ?  
HETATM 15406 O O   . HOH S  4 .   ? 16.239  -22.508  0.819   1.000 47.136  0 730 HOH AAA O   1 ? ?  
HETATM 15407 O O   . HOH S  4 .   ? 28.072  -15.868  -25.760 1.000 75.516  0 731 HOH AAA O   1 ? ?  
HETATM 15408 O O   . HOH S  4 .   ? 7.968   -12.875  -4.797  1.000 43.420  0 732 HOH AAA O   1 ? ?  
HETATM 15409 O O   . HOH S  4 .   ? 0.191   -9.381   6.432   1.000 61.859  0 733 HOH AAA O   1 ? ?  
HETATM 15410 O O   . HOH S  4 .   ? 43.826  -19.563  -16.160 1.000 67.861  0 734 HOH AAA O   1 ? ?  
HETATM 15411 O O   . HOH S  4 .   ? 16.540  -27.857  10.672  1.000 58.877  0 735 HOH AAA O   1 ? ?  
HETATM 15412 O O   . HOH S  4 .   ? -8.748  -28.233  20.493  1.000 73.645  0 736 HOH AAA O   1 ? ?  
HETATM 15413 O O   . HOH S  4 .   ? 24.050  -8.401   -16.853 1.000 46.857  0 737 HOH AAA O   1 ? ?  
HETATM 15414 O O   . HOH S  4 .   ? 20.784  -4.764   10.189  1.000 48.710  0 738 HOH AAA O   1 ? ?  
HETATM 15415 O O   . HOH S  4 .   ? 3.968   -26.993  6.612   1.000 43.971  0 739 HOH AAA O   1 ? ?  
HETATM 15416 O O   . HOH S  4 .   ? 11.279  -19.657  13.392  1.000 64.597  0 740 HOH AAA O   1 ? ?  
HETATM 15417 O O   . HOH S  4 .   ? 14.695  -25.502  -5.656  1.000 52.864  0 741 HOH AAA O   1 ? ?  
HETATM 15418 O O   . HOH S  4 .   ? 9.405   -5.998   14.913  1.000 66.323  0 742 HOH AAA O   1 ? ?  
HETATM 15419 O O   . HOH T  4 .   ? 40.355  -25.183  8.938   1.000 46.835  0 201 HOH BBB O   1 ? ?  
HETATM 15420 O O   . HOH T  4 .   ? 33.775  -8.753   22.783  1.000 46.116  0 202 HOH BBB O   1 ? ?  
HETATM 15421 O O   . HOH T  4 .   ? 29.061  -11.165  10.730  1.000 36.968  0 203 HOH BBB O   1 ? ?  
HETATM 15422 O O   . HOH T  4 .   ? 30.888  -24.128  20.347  1.000 42.359  0 204 HOH BBB O   1 ? ?  
HETATM 15423 O O   . HOH T  4 .   ? 43.700  -18.662  25.188  1.000 41.157  0 205 HOH BBB O   1 ? ?  
HETATM 15424 O O   . HOH T  4 .   ? 37.254  -14.041  25.946  1.000 43.929  0 206 HOH BBB O   1 ? ?  
HETATM 15425 O O   . HOH T  4 .   ? 38.696  -11.664  1.409   1.000 39.272  0 207 HOH BBB O   1 ? ?  
HETATM 15426 O O   . HOH T  4 .   ? 33.815  -12.843  7.779   1.000 36.634  0 208 HOH BBB O   1 ? ?  
HETATM 15427 O O   . HOH T  4 .   ? 37.782  -4.626   4.567   1.000 45.362  0 209 HOH BBB O   1 ? ?  
HETATM 15428 O O   . HOH T  4 .   ? 28.836  -16.812  8.652   1.000 36.402  0 210 HOH BBB O   1 ? ?  
HETATM 15429 O O   . HOH T  4 .   ? 37.075  -28.133  16.328  1.000 33.524  0 211 HOH BBB O   1 ? ?  
HETATM 15430 O O   . HOH T  4 .   ? 46.695  -1.253   10.660  1.000 49.409  0 212 HOH BBB O   1 ? ?  
HETATM 15431 O O   . HOH T  4 .   ? 31.996  -3.120   10.468  1.000 47.083  0 213 HOH BBB O   1 ? ?  
HETATM 15432 O O   . HOH T  4 .   ? 48.279  -21.858  10.388  1.000 44.553  0 214 HOH BBB O   1 ? ?  
HETATM 15433 O O   . HOH T  4 .   ? 36.484  -12.578  7.133   1.000 37.516  0 215 HOH BBB O   1 ? ?  
HETATM 15434 O O   . HOH T  4 .   ? 30.527  -13.732  20.685  1.000 35.667  0 216 HOH BBB O   1 ? ?  
HETATM 15435 O O   . HOH T  4 .   ? 30.558  -11.690  21.996  1.000 38.719  0 217 HOH BBB O   1 ? ?  
HETATM 15436 O O   . HOH T  4 .   ? 47.165  -8.168   4.066   1.000 43.104  0 218 HOH BBB O   1 ? ?  
HETATM 15437 O O   . HOH T  4 .   ? 58.177  1.583    31.552  1.000 72.972  0 219 HOH BBB O   1 ? ?  
HETATM 15438 O O   . HOH T  4 .   ? 24.061  -12.457  14.891  1.000 63.361  0 220 HOH BBB O   1 ? ?  
HETATM 15439 O O   . HOH U  4 .   ? 24.979  -74.421  7.286   1.000 42.928  0 701 HOH CCC O   1 ? ?  
HETATM 15440 O O   . HOH U  4 .   ? 27.348  -76.566  10.367  1.000 38.397  0 702 HOH CCC O   1 ? ?  
HETATM 15441 O O   . HOH U  4 .   ? 26.992  -83.781  5.775   1.000 43.212  0 703 HOH CCC O   1 ? ?  
HETATM 15442 O O   . HOH U  4 .   ? 15.656  -68.703  -5.872  1.000 37.350  0 704 HOH CCC O   1 ? ?  
HETATM 15443 O O   . HOH U  4 .   ? 13.228  -80.468  3.932   1.000 50.313  0 705 HOH CCC O   1 ? ?  
HETATM 15444 O O   . HOH U  4 .   ? 6.373   -77.496  6.587   1.000 34.890  0 706 HOH CCC O   1 ? ?  
HETATM 15445 O O   . HOH U  4 .   ? 7.983   -78.185  4.411   1.000 40.981  0 707 HOH CCC O   1 ? ?  
HETATM 15446 O O   . HOH U  4 .   ? -1.192  -79.140  7.927   1.000 46.518  0 708 HOH CCC O   1 ? ?  
HETATM 15447 O O   . HOH U  4 .   ? 23.911  -60.560  5.268   1.000 36.936  0 709 HOH CCC O   1 ? ?  
HETATM 15448 O O   . HOH U  4 .   ? 12.525  -69.618  -3.390  1.000 39.859  0 710 HOH CCC O   1 ? ?  
HETATM 15449 O O   . HOH U  4 .   ? 19.676  -78.359  -2.235  1.000 51.385  0 711 HOH CCC O   1 ? ?  
HETATM 15450 O O   . HOH U  4 .   ? 2.351   -81.234  1.512   1.000 50.475  0 712 HOH CCC O   1 ? ?  
HETATM 15451 O O   . HOH U  4 .   ? 13.694  -82.893  10.691  1.000 54.044  0 713 HOH CCC O   1 ? ?  
HETATM 15452 O O   . HOH U  4 .   ? 8.750   -84.032  0.322   1.000 44.403  0 714 HOH CCC O   1 ? ?  
HETATM 15453 O O   . HOH U  4 .   ? 9.103   -68.113  5.076   1.000 39.484  0 715 HOH CCC O   1 ? ?  
HETATM 15454 O O   . HOH U  4 .   ? 17.937  -61.935  -3.513  1.000 39.869  0 716 HOH CCC O   1 ? ?  
HETATM 15455 O O   . HOH U  4 .   ? 29.098  -77.979  -8.642  1.000 56.029  0 717 HOH CCC O   1 ? ?  
HETATM 15456 O O   . HOH U  4 .   ? 12.128  -61.944  -12.468 1.000 71.576  0 718 HOH CCC O   1 ? ?  
HETATM 15457 O O   . HOH U  4 .   ? 6.730   -71.910  -3.052  1.000 46.553  0 719 HOH CCC O   1 ? ?  
HETATM 15458 O O   . HOH U  4 .   ? 21.327  -68.105  12.712  1.000 34.395  0 720 HOH CCC O   1 ? ?  
HETATM 15459 O O   . HOH U  4 .   ? 37.228  -80.803  -0.395  1.000 43.818  0 721 HOH CCC O   1 ? ?  
HETATM 15460 O O   . HOH U  4 .   ? 26.129  -71.867  6.157   1.000 43.097  0 722 HOH CCC O   1 ? ?  
HETATM 15461 O O   . HOH U  4 .   ? 6.593   -60.923  0.392   1.000 54.274  0 723 HOH CCC O   1 ? ?  
HETATM 15462 O O   . HOH U  4 .   ? 27.374  -72.462  -24.483 1.000 51.971  0 724 HOH CCC O   1 ? ?  
HETATM 15463 O O   . HOH U  4 .   ? 19.139  -79.688  -19.999 1.000 58.301  0 725 HOH CCC O   1 ? ?  
HETATM 15464 O O   . HOH U  4 .   ? 34.731  -83.805  -2.063  1.000 54.690  0 726 HOH CCC O   1 ? ?  
HETATM 15465 O O   . HOH U  4 .   ? -9.295  -83.446  27.933  1.000 61.126  0 727 HOH CCC O   1 ? ?  
HETATM 15466 O O   . HOH U  4 .   ? 9.872   -76.507  -5.926  1.000 44.809  0 728 HOH CCC O   1 ? ?  
HETATM 15467 O O   . HOH U  4 .   ? 9.334   -66.550  14.468  1.000 48.848  0 729 HOH CCC O   1 ? ?  
HETATM 15468 O O   . HOH U  4 .   ? 4.063   -52.582  14.408  1.000 56.978  0 730 HOH CCC O   1 ? ?  
HETATM 15469 O O   . HOH U  4 .   ? 24.199  -63.337  -4.971  1.000 46.197  0 731 HOH CCC O   1 ? ?  
HETATM 15470 O O   . HOH U  4 .   ? 32.141  -83.621  5.596   1.000 48.358  0 732 HOH CCC O   1 ? ?  
HETATM 15471 O O   . HOH U  4 .   ? 3.749   -75.369  -3.905  1.000 55.302  0 733 HOH CCC O   1 ? ?  
HETATM 15472 O O   . HOH U  4 .   ? 10.279  -79.594  -3.005  1.000 55.190  0 734 HOH CCC O   1 ? ?  
HETATM 15473 O O   . HOH U  4 .   ? 8.216   -77.276  18.026  1.000 66.932  0 735 HOH CCC O   1 ? ?  
HETATM 15474 O O   . HOH U  4 .   ? -8.167  -81.768  14.021  1.000 60.711  0 736 HOH CCC O   1 ? ?  
HETATM 15475 O O   . HOH U  4 .   ? 16.978  -51.882  4.581   1.000 45.626  0 737 HOH CCC O   1 ? ?  
HETATM 15476 O O   . HOH V  4 .   ? 63.382  -57.860  27.419  1.000 59.903  0 201 HOH DDD O   1 ? ?  
HETATM 15477 O O   . HOH V  4 .   ? 27.659  -70.910  12.490  1.000 38.674  0 202 HOH DDD O   1 ? ?  
HETATM 15478 O O   . HOH V  4 .   ? 37.689  -75.599  27.108  1.000 39.390  0 203 HOH DDD O   1 ? ?  
HETATM 15479 O O   . HOH V  4 .   ? 43.255  -78.629  29.903  1.000 42.768  0 204 HOH DDD O   1 ? ?  
HETATM 15480 O O   . HOH V  4 .   ? 49.654  -76.323  6.741   1.000 46.089  0 205 HOH DDD O   1 ? ?  
HETATM 15481 O O   . HOH V  4 .   ? 35.430  -89.210  16.580  1.000 42.631  0 206 HOH DDD O   1 ? ?  
HETATM 15482 O O   . HOH V  4 .   ? 31.026  -82.232  7.436   1.000 40.876  0 207 HOH DDD O   1 ? ?  
HETATM 15483 O O   . HOH V  4 .   ? 28.803  -77.594  13.777  1.000 44.440  0 208 HOH DDD O   1 ? ?  
HETATM 15484 O O   . HOH V  4 .   ? 30.545  -74.499  22.446  1.000 32.044  0 209 HOH DDD O   1 ? ?  
HETATM 15485 O O   . HOH V  4 .   ? 33.799  -72.907  9.149   1.000 57.535  0 210 HOH DDD O   1 ? ?  
HETATM 15486 O O   . HOH V  4 .   ? 32.549  -86.972  7.757   1.000 61.818  0 211 HOH DDD O   1 ? ?  
HETATM 15487 O O   . HOH W  4 .   ? 68.357  -52.526  -4.978  1.000 49.280  0 701 HOH EEE O   1 ? ?  
HETATM 15488 O O   . HOH W  4 .   ? 52.770  -48.360  -10.771 1.000 92.558  0 702 HOH EEE O   1 ? ?  
HETATM 15489 O O   . HOH W  4 .   ? 29.410  -44.806  -5.865  1.000 33.559  0 703 HOH EEE O   1 ? ?  
HETATM 15490 O O   . HOH W  4 .   ? 40.124  -52.568  -1.636  1.000 42.903  0 704 HOH EEE O   1 ? ?  
HETATM 15491 O O   . HOH W  4 .   ? 45.477  -50.630  -1.743  1.000 35.423  0 705 HOH EEE O   1 ? ?  
HETATM 15492 O O   . HOH W  4 .   ? 64.150  -60.068  -10.320 1.000 54.481  0 706 HOH EEE O   1 ? ?  
HETATM 15493 O O   . HOH W  4 .   ? 44.250  -29.719  -7.622  1.000 73.706  0 707 HOH EEE O   1 ? ?  
HETATM 15494 O O   . HOH W  4 .   ? 38.361  -54.179  -10.359 1.000 42.631  0 708 HOH EEE O   1 ? ?  
HETATM 15495 O O   . HOH W  4 .   ? 36.227  -49.617  -6.083  1.000 46.438  0 709 HOH EEE O   1 ? ?  
HETATM 15496 O O   . HOH W  4 .   ? 38.546  -40.097  7.531   1.000 44.524  0 710 HOH EEE O   1 ? ?  
HETATM 15497 O O   . HOH W  4 .   ? 37.631  -42.910  -13.984 1.000 45.090  0 711 HOH EEE O   1 ? ?  
HETATM 15498 O O   . HOH W  4 .   ? 33.179  -32.020  12.362  1.000 46.272  0 712 HOH EEE O   1 ? ?  
HETATM 15499 O O   . HOH W  4 .   ? 47.193  -50.437  -3.697  1.000 40.496  0 713 HOH EEE O   1 ? ?  
HETATM 15500 O O   . HOH W  4 .   ? 41.081  -31.907  7.075   1.000 35.752  0 714 HOH EEE O   1 ? ?  
HETATM 15501 O O   . HOH W  4 .   ? 37.195  -33.089  4.902   1.000 39.521  0 715 HOH EEE O   1 ? ?  
HETATM 15502 O O   . HOH W  4 .   ? 45.658  -40.880  -2.818  1.000 34.551  0 716 HOH EEE O   1 ? ?  
HETATM 15503 O O   . HOH W  4 .   ? 25.001  -60.617  -0.386  1.000 47.331  0 717 HOH EEE O   1 ? ?  
HETATM 15504 O O   . HOH W  4 .   ? 49.661  -35.896  -4.661  1.000 57.295  0 718 HOH EEE O   1 ? ?  
HETATM 15505 O O   . HOH W  4 .   ? 28.553  -42.133  -4.746  1.000 40.861  0 719 HOH EEE O   1 ? ?  
HETATM 15506 O O   . HOH W  4 .   ? 41.862  -41.223  5.311   1.000 39.338  0 720 HOH EEE O   1 ? ?  
HETATM 15507 O O   . HOH W  4 .   ? 38.321  -25.912  -6.713  1.000 39.779  0 721 HOH EEE O   1 ? ?  
HETATM 15508 O O   . HOH W  4 .   ? 43.598  -30.166  -15.532 1.000 54.624  0 722 HOH EEE O   1 ? ?  
HETATM 15509 O O   . HOH W  4 .   ? 39.943  -54.924  -8.460  1.000 50.486  0 723 HOH EEE O   1 ? ?  
HETATM 15510 O O   . HOH W  4 .   ? 33.986  -39.392  -11.385 1.000 40.214  0 724 HOH EEE O   1 ? ?  
HETATM 15511 O O   . HOH W  4 .   ? 35.529  -45.898  -14.497 1.000 51.365  0 725 HOH EEE O   1 ? ?  
HETATM 15512 O O   . HOH W  4 .   ? 31.645  -58.848  -7.104  1.000 61.289  0 726 HOH EEE O   1 ? ?  
HETATM 15513 O O   . HOH W  4 .   ? 37.599  -27.421  -2.205  1.000 46.998  0 727 HOH EEE O   1 ? ?  
HETATM 15514 O O   . HOH W  4 .   ? 23.717  -56.433  -1.974  1.000 48.931  0 728 HOH EEE O   1 ? ?  
HETATM 15515 O O   . HOH W  4 .   ? 46.764  -53.645  5.047   1.000 47.822  0 729 HOH EEE O   1 ? ?  
HETATM 15516 O O   . HOH W  4 .   ? 21.719  -52.852  -4.261  1.000 46.334  0 730 HOH EEE O   1 ? ?  
HETATM 15517 O O   . HOH W  4 .   ? 34.261  -39.403  -14.564 1.000 53.212  0 731 HOH EEE O   1 ? ?  
HETATM 15518 O O   . HOH W  4 .   ? 37.418  -27.158  -15.150 1.000 53.141  0 732 HOH EEE O   1 ? ?  
HETATM 15519 O O   . HOH W  4 .   ? 29.078  -42.097  -13.077 1.000 52.889  0 733 HOH EEE O   1 ? ?  
HETATM 15520 O O   . HOH W  4 .   ? 41.807  -23.040  -3.505  1.000 49.618  0 734 HOH EEE O   1 ? ?  
HETATM 15521 O O   . HOH W  4 .   ? 67.108  -61.309  -16.269 1.000 84.069  0 735 HOH EEE O   1 ? ?  
HETATM 15522 O O   . HOH W  4 .   ? 39.011  -30.093  7.617   1.000 40.351  0 736 HOH EEE O   1 ? ?  
HETATM 15523 O O   . HOH X  4 .   ? 26.785  -41.205  -11.697 1.000 33.150  0 201 HOH FFF O   1 ? ?  
HETATM 15524 O O   . HOH X  4 .   ? 4.703   -44.149  -6.155  1.000 39.976  0 202 HOH FFF O   1 ? ?  
HETATM 15525 O O   . HOH X  4 .   ? 14.735  -50.910  -2.252  1.000 36.794  0 203 HOH FFF O   1 ? ?  
HETATM 15526 O O   . HOH X  4 .   ? -4.713  -27.833  -27.025 1.000 62.982  0 204 HOH FFF O   1 ? ?  
HETATM 15527 O O   . HOH X  4 .   ? 17.196  -44.949  -25.733 1.000 33.304  0 205 HOH FFF O   1 ? ?  
HETATM 15528 O O   . HOH X  4 .   ? 23.784  -33.338  -11.314 1.000 48.499  0 206 HOH FFF O   1 ? ?  
HETATM 15529 O O   . HOH X  4 .   ? 17.569  -58.450  -15.377 1.000 44.173  0 207 HOH FFF O   1 ? ?  
HETATM 15530 O O   . HOH X  4 .   ? 21.678  -42.737  -8.118  1.000 34.008  0 208 HOH FFF O   1 ? ?  
HETATM 15531 O O   . HOH X  4 .   ? 21.527  -55.605  -15.858 1.000 40.117  0 209 HOH FFF O   1 ? ?  
HETATM 15532 O O   . HOH X  4 .   ? 9.040   -30.677  -10.662 1.000 50.471  0 210 HOH FFF O   1 ? ?  
HETATM 15533 O O   . HOH X  4 .   ? -5.553  -38.568  -17.867 1.000 46.353  0 211 HOH FFF O   1 ? ?  
HETATM 15534 O O   . HOH X  4 .   ? 9.281   -53.921  -22.072 1.000 35.799  0 212 HOH FFF O   1 ? ?  
HETATM 15535 O O   . HOH X  4 .   ? 10.891  -54.328  -7.105  1.000 45.066  0 213 HOH FFF O   1 ? ?  
HETATM 15536 O O   . HOH X  4 .   ? 17.499  -40.923  -1.452  1.000 39.477  0 214 HOH FFF O   1 ? ?  
HETATM 15537 O O   . HOH X  4 .   ? 12.547  -51.178  0.703   1.000 57.739  0 215 HOH FFF O   1 ? ?  
HETATM 15538 O O   . HOH X  4 .   ? 19.178  -42.218  -7.323  1.000 40.740  0 216 HOH FFF O   1 ? ?  
HETATM 15539 O O   . HOH X  4 .   ? 10.520  -49.648  -23.999 1.000 35.041  0 217 HOH FFF O   1 ? ?  
HETATM 15540 O O   . HOH X  4 .   ? 23.041  -52.017  -6.126  1.000 35.653  0 218 HOH FFF O   1 ? ?  
HETATM 15541 O O   . HOH X  4 .   ? 25.469  -47.452  -12.006 1.000 41.382  0 219 HOH FFF O   1 ? ?  
HETATM 15542 O O   . HOH X  4 .   ? 6.960   -51.017  -8.885  1.000 47.286  0 220 HOH FFF O   1 ? ?  
HETATM 15543 O O   . HOH X  4 .   ? 24.188  -44.415  -21.232 1.000 44.116  0 221 HOH FFF O   1 ? ?  
HETATM 15544 O O   . HOH X  4 .   ? 11.919  -42.529  -29.278 1.000 45.477  0 222 HOH FFF O   1 ? ?  
HETATM 15545 O O   . HOH X  4 .   ? 26.490  -40.376  -17.181 1.000 48.394  0 223 HOH FFF O   1 ? ?  
HETATM 15546 O O   . HOH X  4 .   ? 13.808  -58.442  -20.618 1.000 45.798  0 224 HOH FFF O   1 ? ?  
HETATM 15547 O O   . HOH X  4 .   ? 8.692   -27.224  -5.307  1.000 72.551  0 225 HOH FFF O   1 ? ?  
HETATM 15548 O O   . HOH X  4 .   ? 19.752  -54.682  -4.662  1.000 55.198  0 226 HOH FFF O   1 ? ?  
HETATM 15549 O O   . HOH X  4 .   ? 10.027  -52.530  -24.347 1.000 35.726  0 227 HOH FFF O   1 ? ?  
HETATM 15550 O O   . HOH Y  4 .   ? 14.828  -23.973  51.814  1.000 89.493  0 701 HOH GGG O   1 ? ?  
HETATM 15551 O O   . HOH Y  4 .   ? 5.705   16.805   42.011  1.000 59.924  0 702 HOH GGG O   1 ? ?  
HETATM 15552 O O   . HOH Y  4 .   ? 11.320  -4.225   38.982  1.000 42.111  0 703 HOH GGG O   1 ? ?  
HETATM 15553 O O   . HOH Y  4 .   ? 3.179   -6.198   44.614  1.000 54.071  0 704 HOH GGG O   1 ? ?  
HETATM 15554 O O   . HOH Y  4 .   ? 2.960   -14.023  41.487  1.000 76.327  0 705 HOH GGG O   1 ? ?  
HETATM 15555 O O   . HOH Y  4 .   ? 27.483  -11.572  74.039  1.000 62.414  0 706 HOH GGG O   1 ? ?  
HETATM 15556 O O   . HOH Y  4 .   ? 15.554  -8.089   57.699  1.000 39.822  0 707 HOH GGG O   1 ? ?  
HETATM 15557 O O   . HOH Y  4 .   ? 12.891  10.621   41.859  1.000 44.111  0 708 HOH GGG O   1 ? ?  
HETATM 15558 O O   . HOH Y  4 .   ? 11.994  -21.265  42.807  1.000 48.319  0 709 HOH GGG O   1 ? ?  
HETATM 15559 O O   . HOH Y  4 .   ? 17.220  -9.317   36.460  1.000 37.768  0 710 HOH GGG O   1 ? ?  
HETATM 15560 O O   . HOH Y  4 .   ? 15.465  2.763    46.179  1.000 35.435  0 711 HOH GGG O   1 ? ?  
HETATM 15561 O O   . HOH Y  4 .   ? 16.613  1.777    48.405  1.000 36.932  0 712 HOH GGG O   1 ? ?  
HETATM 15562 O O   . HOH Y  4 .   ? 28.227  -1.771   40.032  1.000 44.910  0 713 HOH GGG O   1 ? ?  
HETATM 15563 O O   . HOH Y  4 .   ? 23.808  0.513    42.411  1.000 39.542  0 714 HOH GGG O   1 ? ?  
HETATM 15564 O O   . HOH Y  4 .   ? 8.678   -15.463  55.361  1.000 40.882  0 715 HOH GGG O   1 ? ?  
HETATM 15565 O O   . HOH Y  4 .   ? 12.562  -10.377  57.521  1.000 40.256  0 716 HOH GGG O   1 ? ?  
HETATM 15566 O O   . HOH Y  4 .   ? 21.682  -1.164   49.184  1.000 44.734  0 717 HOH GGG O   1 ? ?  
HETATM 15567 O O   . HOH Y  4 .   ? 6.089   -9.751   38.156  1.000 48.319  0 718 HOH GGG O   1 ? ?  
HETATM 15568 O O   . HOH Y  4 .   ? 22.856  -7.688   55.182  1.000 42.345  0 719 HOH GGG O   1 ? ?  
HETATM 15569 O O   . HOH Y  4 .   ? 14.796  13.576   38.476  1.000 47.948  0 720 HOH GGG O   1 ? ?  
HETATM 15570 O O   . HOH Y  4 .   ? 9.247   -5.001   46.731  1.000 39.394  0 721 HOH GGG O   1 ? ?  
HETATM 15571 O O   . HOH Y  4 .   ? 22.712  -5.913   44.413  1.000 37.235  0 722 HOH GGG O   1 ? ?  
HETATM 15572 O O   . HOH Y  4 .   ? 26.990  -14.457  42.075  1.000 39.039  0 723 HOH GGG O   1 ? ?  
HETATM 15573 O O   . HOH Y  4 .   ? 17.119  -14.085  38.767  1.000 35.750  0 724 HOH GGG O   1 ? ?  
HETATM 15574 O O   . HOH Y  4 .   ? 11.570  -5.056   34.549  1.000 53.749  0 725 HOH GGG O   1 ? ?  
HETATM 15575 O O   . HOH Y  4 .   ? 24.071  -13.822  40.481  1.000 49.609  0 726 HOH GGG O   1 ? ?  
HETATM 15576 O O   . HOH Y  4 .   ? 5.268   -20.510  46.501  1.000 40.010  0 727 HOH GGG O   1 ? ?  
HETATM 15577 O O   . HOH Y  4 .   ? 1.584   -12.434  57.339  1.000 60.095  0 728 HOH GGG O   1 ? ?  
HETATM 15578 O O   . HOH Y  4 .   ? 36.684  -13.545  63.802  1.000 45.899  0 729 HOH GGG O   1 ? ?  
HETATM 15579 O O   . HOH Y  4 .   ? 8.484   -1.773   52.785  1.000 49.876  0 730 HOH GGG O   1 ? ?  
HETATM 15580 O O   . HOH Y  4 .   ? 17.156  10.320   42.103  1.000 51.329  0 731 HOH GGG O   1 ? ?  
HETATM 15581 O O   . HOH Y  4 .   ? 30.475  -6.779   52.859  1.000 42.467  0 732 HOH GGG O   1 ? ?  
HETATM 15582 O O   . HOH Y  4 .   ? 25.058  -12.292  74.779  1.000 71.288  0 733 HOH GGG O   1 ? ?  
HETATM 15583 O O   . HOH Y  4 .   ? 14.441  -17.437  40.426  1.000 43.819  0 734 HOH GGG O   1 ? ?  
HETATM 15584 O O   . HOH Y  4 .   ? 11.567  -19.749  55.128  1.000 50.570  0 735 HOH GGG O   1 ? ?  
HETATM 15585 O O   . HOH Y  4 .   ? 11.744  16.920   25.776  1.000 72.329  0 736 HOH GGG O   1 ? ?  
HETATM 15586 O O   . HOH Y  4 .   ? 37.024  -18.864  51.507  1.000 44.181  0 737 HOH GGG O   1 ? ?  
HETATM 15587 O O   . HOH Z  4 .   ? 33.001  -23.233  25.768  1.000 38.122  0 201 HOH HHH O   1 ? ?  
HETATM 15588 O O   . HOH Z  4 .   ? 35.590  -11.690  31.247  1.000 44.692  0 202 HOH HHH O   1 ? ?  
HETATM 15589 O O   . HOH Z  4 .   ? 37.826  -20.425  48.932  1.000 40.464  0 203 HOH HHH O   1 ? ?  
HETATM 15590 O O   . HOH Z  4 .   ? 30.214  -17.976  29.273  1.000 39.880  0 204 HOH HHH O   1 ? ?  
HETATM 15591 O O   . HOH Z  4 .   ? 42.554  -13.465  36.261  1.000 39.956  0 205 HOH HHH O   1 ? ?  
HETATM 15592 O O   . HOH Z  4 .   ? 46.636  -25.203  30.595  1.000 48.716  0 206 HOH HHH O   1 ? ?  
HETATM 15593 O O   . HOH Z  4 .   ? 28.801  -22.987  43.825  1.000 42.082  0 207 HOH HHH O   1 ? ?  
HETATM 15594 O O   . HOH Z  4 .   ? 44.947  -22.958  29.830  1.000 42.215  0 208 HOH HHH O   1 ? ?  
HETATM 15595 O O   . HOH Z  4 .   ? 27.612  -18.265  30.064  1.000 41.634  0 209 HOH HHH O   1 ? ?  
HETATM 15596 O O   . HOH Z  4 .   ? 28.734  -14.853  38.839  1.000 41.380  0 210 HOH HHH O   1 ? ?  
HETATM 15597 O O   . HOH Z  4 .   ? 38.266  -14.348  45.984  1.000 50.563  0 211 HOH HHH O   1 ? ?  
HETATM 15598 O O   . HOH Z  4 .   ? 37.787  -29.873  50.593  1.000 46.575  0 212 HOH HHH O   1 ? ?  
HETATM 15599 O O   . HOH Z  4 .   ? 21.975  -20.277  35.652  1.000 51.373  0 213 HOH HHH O   1 ? ?  
HETATM 15600 O O   . HOH Z  4 .   ? 20.177  -29.053  45.390  1.000 49.918  0 214 HOH HHH O   1 ? ?  
HETATM 15601 O O   . HOH Z  4 .   ? 46.258  -21.591  42.205  1.000 50.295  0 215 HOH HHH O   1 ? ?  
HETATM 15602 O O   . HOH Z  4 .   ? 43.571  -23.333  27.335  1.000 33.984  0 216 HOH HHH O   1 ? ?  
HETATM 15603 O O   . HOH AA 4 .   ? 21.463  -69.540  61.038  1.000 42.616  0 701 HOH III O   1 ? ?  
HETATM 15604 O O   . HOH AA 4 .   ? 23.029  -59.519  52.042  1.000 37.910  0 702 HOH III O   1 ? ?  
HETATM 15605 O O   . HOH AA 4 .   ? 20.570  -52.540  46.407  1.000 57.637  0 703 HOH III O   1 ? ?  
HETATM 15606 O O   . HOH AA 4 .   ? 26.901  -75.918  47.694  1.000 40.723  0 704 HOH III O   1 ? ?  
HETATM 15607 O O   . HOH AA 4 .   ? 27.462  -63.019  51.773  1.000 52.956  0 705 HOH III O   1 ? ?  
HETATM 15608 O O   . HOH AA 4 .   ? 29.413  -61.740  45.278  1.000 48.657  0 706 HOH III O   1 ? ?  
HETATM 15609 O O   . HOH AA 4 .   ? 38.431  -69.467  64.853  1.000 38.321  0 707 HOH III O   1 ? ?  
HETATM 15610 O O   . HOH AA 4 .   ? 14.666  -64.815  50.978  1.000 67.067  0 708 HOH III O   1 ? ?  
HETATM 15611 O O   . HOH AA 4 .   ? 28.650  -70.038  57.717  1.000 46.870  0 709 HOH III O   1 ? ?  
HETATM 15612 O O   . HOH AA 4 .   ? 17.526  -68.004  59.290  1.000 51.122  0 710 HOH III O   1 ? ?  
HETATM 15613 O O   . HOH AA 4 .   ? 21.798  -58.078  50.214  1.000 43.855  0 711 HOH III O   1 ? ?  
HETATM 15614 O O   . HOH AA 4 .   ? 38.367  -84.288  55.480  1.000 41.336  0 712 HOH III O   1 ? ?  
HETATM 15615 O O   . HOH AA 4 .   ? 7.974   -78.034  54.224  1.000 65.397  0 713 HOH III O   1 ? ?  
HETATM 15616 O O   . HOH AA 4 .   ? 32.748  -66.181  58.227  1.000 52.823  0 714 HOH III O   1 ? ?  
HETATM 15617 O O   . HOH AA 4 .   ? 17.763  -43.787  51.751  1.000 66.945  0 715 HOH III O   1 ? ?  
HETATM 15618 O O   . HOH AA 4 .   ? 38.475  -64.462  64.021  1.000 43.711  0 716 HOH III O   1 ? ?  
HETATM 15619 O O   . HOH BA 4 .   ? 41.025  -107.156 33.034  1.000 55.452  0 201 HOH JJJ O   1 ? ?  
HETATM 15620 O O   . HOH BA 4 .   ? 32.520  -84.412  26.664  1.000 36.695  0 202 HOH JJJ O   1 ? ?  
HETATM 15621 O O   . HOH BA 4 .   ? 39.759  -75.142  36.650  1.000 47.859  0 203 HOH JJJ O   1 ? ?  
HETATM 15622 O O   . HOH BA 4 .   ? 44.877  -85.807  29.481  1.000 41.713  0 204 HOH JJJ O   1 ? ?  
HETATM 15623 O O   . HOH BA 4 .   ? 44.267  -76.831  36.723  1.000 43.402  0 205 HOH JJJ O   1 ? ?  
HETATM 15624 O O   . HOH BA 4 .   ? 34.178  -87.839  24.881  1.000 38.128  0 206 HOH JJJ O   1 ? ?  
HETATM 15625 O O   . HOH BA 4 .   ? 42.598  -86.375  52.317  1.000 52.450  0 207 HOH JJJ O   1 ? ?  
HETATM 15626 O O   . HOH BA 4 .   ? 36.356  -76.541  46.396  1.000 46.325  0 208 HOH JJJ O   1 ? ?  
HETATM 15627 O O   . HOH BA 4 .   ? 45.268  -85.103  44.372  1.000 53.752  0 209 HOH JJJ O   1 ? ?  
HETATM 15628 O O   . HOH BA 4 .   ? 30.262  -85.188  44.996  1.000 50.294  0 210 HOH JJJ O   1 ? ?  
HETATM 15629 O O   . HOH BA 4 .   ? 28.205  -79.457  31.888  1.000 42.607  0 211 HOH JJJ O   1 ? ?  
HETATM 15630 O O   . HOH BA 4 .   ? 18.206  -96.487  36.575  1.000 57.852  0 212 HOH JJJ O   1 ? ?  
HETATM 15631 O O   . HOH BA 4 .   ? 45.794  -96.402  35.052  1.000 57.159  0 213 HOH JJJ O   1 ? ?  
HETATM 15632 O O   . HOH BA 4 .   ? 29.783  -112.677 21.850  1.000 69.752  0 214 HOH JJJ O   1 ? ?  
HETATM 15633 O O   . HOH BA 4 .   ? 31.450  -115.595 23.911  1.000 58.713  0 215 HOH JJJ O   1 ? ?  
HETATM 15634 O O   . HOH CA 4 .   ? -28.138 -45.672  9.234   1.000 37.009  0 701 HOH KKK O   1 ? ?  
HETATM 15635 O O   . HOH CA 4 .   ? -36.022 -48.012  9.793   1.000 38.026  0 702 HOH KKK O   1 ? ?  
HETATM 15636 O O   . HOH CA 4 .   ? -34.030 -32.443  -2.043  1.000 41.574  0 703 HOH KKK O   1 ? ?  
HETATM 15637 O O   . HOH CA 4 .   ? -37.187 -42.031  -3.277  1.000 41.240  0 704 HOH KKK O   1 ? ?  
HETATM 15638 O O   . HOH CA 4 .   ? -36.476 -38.052  -3.620  1.000 48.141  0 705 HOH KKK O   1 ? ?  
HETATM 15639 O O   . HOH CA 4 .   ? -20.556 -40.765  -19.827 1.000 61.154  0 706 HOH KKK O   1 ? ?  
HETATM 15640 O O   . HOH CA 4 .   ? -52.279 -47.473  11.782  1.000 40.797  0 707 HOH KKK O   1 ? ?  
HETATM 15641 O O   . HOH CA 4 .   ? -45.739 -40.066  -0.785  1.000 52.006  0 708 HOH KKK O   1 ? ?  
HETATM 15642 O O   . HOH CA 4 .   ? -30.075 -26.987  12.607  1.000 48.889  0 709 HOH KKK O   1 ? ?  
HETATM 15643 O O   . HOH CA 4 .   ? -49.623 -48.763  18.184  1.000 41.910  0 710 HOH KKK O   1 ? ?  
HETATM 15644 O O   . HOH CA 4 .   ? -25.085 -61.665  -8.393  1.000 73.026  0 711 HOH KKK O   1 ? ?  
HETATM 15645 O O   . HOH CA 4 .   ? -45.363 -47.072  5.717   1.000 43.923  0 712 HOH KKK O   1 ? ?  
HETATM 15646 O O   . HOH CA 4 .   ? -38.293 -27.445  12.319  1.000 64.083  0 713 HOH KKK O   1 ? ?  
HETATM 15647 O O   . HOH CA 4 .   ? -34.172 -54.396  11.372  1.000 44.507  0 714 HOH KKK O   1 ? ?  
HETATM 15648 O O   . HOH CA 4 .   ? -43.060 -37.285  7.251   1.000 49.134  0 715 HOH KKK O   1 ? ?  
HETATM 15649 O O   . HOH CA 4 .   ? -27.292 -50.948  -19.174 1.000 66.929  0 716 HOH KKK O   1 ? ?  
HETATM 15650 O O   . HOH CA 4 .   ? -41.091 -35.166  21.466  1.000 67.314  0 717 HOH KKK O   1 ? ?  
HETATM 15651 O O   . HOH CA 4 .   ? -31.156 -39.342  15.264  1.000 40.193  0 718 HOH KKK O   1 ? ?  
HETATM 15652 O O   . HOH CA 4 .   ? -60.590 -51.783  29.979  1.000 61.975  0 719 HOH KKK O   1 ? ?  
HETATM 15653 O O   . HOH CA 4 .   ? -27.201 -31.842  7.938   1.000 37.405  0 720 HOH KKK O   1 ? ?  
HETATM 15654 O O   . HOH CA 4 .   ? -30.280 -58.416  -14.456 1.000 63.052  0 721 HOH KKK O   1 ? ?  
HETATM 15655 O O   . HOH CA 4 .   ? -12.494 -47.701  -14.349 1.000 54.159  0 722 HOH KKK O   1 ? ?  
HETATM 15656 O O   . HOH CA 4 .   ? -33.795 -48.406  -0.751  1.000 55.840  0 723 HOH KKK O   1 ? ?  
HETATM 15657 O O   . HOH CA 4 .   ? -27.791 -67.148  -11.657 1.000 47.684  0 724 HOH KKK O   1 ? ?  
HETATM 15658 O O   . HOH CA 4 .   ? -30.096 -35.742  13.499  1.000 48.897  0 725 HOH KKK O   1 ? ?  
HETATM 15659 O O   . HOH CA 4 .   ? -48.974 -35.900  18.464  1.000 62.205  0 726 HOH KKK O   1 ? ?  
HETATM 15660 O O   . HOH CA 4 .   ? -22.742 -40.213  -20.052 1.000 62.625  0 727 HOH KKK O   1 ? ?  
HETATM 15661 O O   . HOH CA 4 .   ? -53.201 -51.021  12.402  1.000 48.998  0 728 HOH KKK O   1 ? ?  
HETATM 15662 O O   . HOH CA 4 .   ? -33.142 -22.452  14.899  1.000 49.501  0 729 HOH KKK O   1 ? ?  
HETATM 15663 O O   . HOH CA 4 .   ? -23.354 -50.905  -15.368 1.000 86.283  0 730 HOH KKK O   1 ? ?  
HETATM 15664 O O   . HOH CA 4 .   ? -28.814 -32.817  -1.277  1.000 50.961  0 731 HOH KKK O   1 ? ?  
HETATM 15665 O O   . HOH CA 4 .   ? -27.322 -64.721  -6.469  1.000 59.163  0 732 HOH KKK O   1 ? ?  
HETATM 15666 O O   . HOH CA 4 .   ? -31.237 -25.159  11.074  1.000 48.136  0 733 HOH KKK O   1 ? ?  
HETATM 15667 O O   . HOH CA 4 .   ? -43.066 -47.275  -1.971  1.000 67.965  0 734 HOH KKK O   1 ? ?  
HETATM 15668 O O   . HOH CA 4 .   ? -23.193 -55.405  8.050   1.000 43.844  0 735 HOH KKK O   1 ? ?  
HETATM 15669 O O   . HOH CA 4 .   ? -42.482 -52.040  -1.308  1.000 54.430  0 736 HOH KKK O   1 ? ?  
HETATM 15670 O O   . HOH CA 4 .   ? -42.903 -36.372  16.418  1.000 53.955  0 737 HOH KKK O   1 ? ?  
HETATM 15671 O O   . HOH CA 4 .   ? -27.901 -29.537  2.317   1.000 50.480  0 738 HOH KKK O   1 ? ?  
HETATM 15672 O O   . HOH CA 4 .   ? -32.779 -54.920  -2.003  1.000 65.011  0 739 HOH KKK O   1 ? ?  
HETATM 15673 O O   . HOH DA 4 .   ? -6.772  -31.007  28.174  1.000 53.401  0 201 HOH LLL O   1 ? ?  
HETATM 15674 O O   . HOH DA 4 .   ? 5.940   -46.638  30.572  1.000 78.851  0 202 HOH LLL O   1 ? ?  
HETATM 15675 O O   . HOH DA 4 .   ? -23.881 -38.359  12.478  1.000 37.330  0 203 HOH LLL O   1 ? ?  
HETATM 15676 O O   . HOH DA 4 .   ? -17.558 -48.512  29.813  1.000 35.352  0 204 HOH LLL O   1 ? ?  
HETATM 15677 O O   . HOH DA 4 .   ? -26.104 -56.458  23.949  1.000 35.390  0 205 HOH LLL O   1 ? ?  
HETATM 15678 O O   . HOH DA 4 .   ? -13.913 -48.758  31.338  1.000 37.098  0 206 HOH LLL O   1 ? ?  
HETATM 15679 O O   . HOH DA 4 .   ? -25.502 -42.597  14.261  1.000 38.414  0 207 HOH LLL O   1 ? ?  
HETATM 15680 O O   . HOH DA 4 .   ? -20.739 -45.636  12.058  1.000 33.397  0 208 HOH LLL O   1 ? ?  
HETATM 15681 O O   . HOH DA 4 .   ? -26.469 -48.399  12.693  1.000 41.019  0 209 HOH LLL O   1 ? ?  
HETATM 15682 O O   . HOH DA 4 .   ? -20.676 -61.856  19.439  1.000 42.095  0 210 HOH LLL O   1 ? ?  
HETATM 15683 O O   . HOH DA 4 .   ? -24.066 -58.104  19.621  1.000 44.162  0 211 HOH LLL O   1 ? ?  
HETATM 15684 O O   . HOH DA 4 .   ? -12.653 -51.660  33.396  1.000 36.017  0 212 HOH LLL O   1 ? ?  
HETATM 15685 O O   . HOH DA 4 .   ? 4.811   -34.784  32.419  1.000 65.659  0 213 HOH LLL O   1 ? ?  
HETATM 15686 O O   . HOH DA 4 .   ? -12.325 -54.674  28.645  1.000 35.656  0 214 HOH LLL O   1 ? ?  
HETATM 15687 O O   . HOH DA 4 .   ? -12.276 -25.405  26.509  1.000 50.409  0 215 HOH LLL O   1 ? ?  
HETATM 15688 O O   . HOH DA 4 .   ? -18.228 -45.865  11.189  1.000 38.752  0 216 HOH LLL O   1 ? ?  
HETATM 15689 O O   . HOH DA 4 .   ? -19.630 -41.946  27.023  1.000 45.181  0 217 HOH LLL O   1 ? ?  
HETATM 15690 O O   . HOH DA 4 .   ? -10.098 -44.512  34.168  1.000 45.330  0 218 HOH LLL O   1 ? ?  
HETATM 15691 O O   . HOH DA 4 .   ? -11.855 -46.842  33.476  1.000 45.899  0 219 HOH LLL O   1 ? ?  
HETATM 15692 O O   . HOH DA 4 .   ? -18.402 -40.909  30.287  1.000 48.188  0 220 HOH LLL O   1 ? ?  
HETATM 15693 O O   . HOH DA 4 .   ? -23.696 -44.703  26.360  1.000 46.650  0 221 HOH LLL O   1 ? ?  
HETATM 15694 O O   . HOH DA 4 .   ? -6.758  -55.053  29.287  1.000 49.004  0 222 HOH LLL O   1 ? ?  
HETATM 15695 O O   . HOH DA 4 .   ? 8.490   -41.683  32.803  1.000 66.814  0 223 HOH LLL O   1 ? ?  
HETATM 15696 O O   . HOH DA 4 .   ? 10.983  -35.271  30.939  1.000 57.741  0 224 HOH LLL O   1 ? ?  
HETATM 15697 O O   . HOH DA 4 .   ? -26.308 -40.941  17.786  1.000 48.020  0 225 HOH LLL O   1 ? ?  
HETATM 15698 O O   . HOH DA 4 .   ? -27.162 -43.278  16.214  1.000 44.693  0 226 HOH LLL O   1 ? ?  
HETATM 15699 O O   . HOH DA 4 .   ? -12.607 -57.411  28.866  1.000 37.943  0 227 HOH LLL O   1 ? ?  
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
126   N N   . PHE A 18  ? 0.586 0.603 0.582 -0.038 0.085  0.109  347 PHE AAA N   
127   C CA  . PHE A 18  ? 0.571 0.576 0.559 -0.052 0.072  0.089  347 PHE AAA CA  
128   C C   . PHE A 18  ? 0.558 0.583 0.552 -0.055 0.062  0.096  347 PHE AAA C   
129   O O   . PHE A 18  ? 0.548 0.584 0.550 -0.046 0.072  0.111  347 PHE AAA O   
130   C CB  . PHE A 18  ? 0.573 0.552 0.559 -0.055 0.085  0.073  347 PHE AAA CB  
131   C CG  . PHE A 18  ? 0.562 0.527 0.541 -0.062 0.084  0.059  347 PHE AAA CG  
132   C CD1 . PHE A 18  ? 0.546 0.504 0.527 -0.056 0.094  0.065  347 PHE AAA CD1 
133   C CD2 . PHE A 18  ? 0.561 0.525 0.534 -0.073 0.075  0.044  347 PHE AAA CD2 
134   C CE1 . PHE A 18  ? 0.549 0.497 0.526 -0.062 0.093  0.054  347 PHE AAA CE1 
135   C CE2 . PHE A 18  ? 0.550 0.506 0.519 -0.078 0.075  0.034  347 PHE AAA CE2 
136   C CZ  . PHE A 18  ? 0.538 0.485 0.509 -0.073 0.083  0.038  347 PHE AAA CZ  
137   N N   . ALA A 19  ? 0.557 0.585 0.550 -0.067 0.047  0.087  348 ALA AAA N   
138   C CA  . ALA A 19  ? 0.540 0.585 0.542 -0.072 0.037  0.094  348 ALA AAA CA  
139   C C   . ALA A 19  ? 0.533 0.575 0.538 -0.068 0.045  0.095  348 ALA AAA C   
140   O O   . ALA A 19  ? 0.501 0.527 0.498 -0.068 0.053  0.084  348 ALA AAA O   
141   C CB  . ALA A 19  ? 0.547 0.591 0.551 -0.085 0.023  0.084  348 ALA AAA CB  
142   N N   . SER A 20  ? 0.528 0.589 0.543 -0.067 0.043  0.109  349 SER AAA N   
143   C CA  . SER A 20  ? 0.531 0.598 0.551 -0.066 0.045  0.112  349 SER AAA CA  
144   C C   . SER A 20  ? 0.522 0.583 0.543 -0.075 0.036  0.103  349 SER AAA C   
145   O O   . SER A 20  ? 0.487 0.545 0.514 -0.084 0.026  0.101  349 SER AAA O   
146   C CB  . SER A 20  ? 0.515 0.607 0.550 -0.064 0.043  0.131  349 SER AAA CB  
147   O OG  . SER A 20  ? 0.521 0.619 0.555 -0.051 0.056  0.142  349 SER AAA OG  
148   N N   . VAL A 21  ? 0.508 0.572 0.526 -0.073 0.040  0.100  350 VAL AAA N   
149   C CA  . VAL A 21  ? 0.502 0.568 0.524 -0.078 0.035  0.099  350 VAL AAA CA  
150   C C   . VAL A 21  ? 0.510 0.582 0.553 -0.083 0.028  0.112  350 VAL AAA C   
151   O O   . VAL A 21  ? 0.522 0.582 0.572 -0.088 0.024  0.109  350 VAL AAA O   
152   C CB  . VAL A 21  ? 0.491 0.576 0.507 -0.074 0.041  0.097  350 VAL AAA CB  
153   C CG1 . VAL A 21  ? 0.477 0.586 0.500 -0.068 0.045  0.111  350 VAL AAA CG1 
154   C CG2 . VAL A 21  ? 0.459 0.553 0.479 -0.075 0.038  0.098  350 VAL AAA CG2 
155   N N   . TYR A 22  ? 0.508 0.596 0.564 -0.082 0.027  0.126  351 TYR AAA N   
156   C CA  . TYR A 22  ? 0.507 0.601 0.588 -0.090 0.023  0.139  351 TYR AAA CA  
157   C C   . TYR A 22  ? 0.509 0.586 0.593 -0.103 0.015  0.128  351 TYR AAA C   
158   O O   . TYR A 22  ? 0.521 0.588 0.623 -0.113 0.014  0.128  351 TYR AAA O   
159   C CB  . TYR A 22  ? 0.512 0.631 0.606 -0.086 0.024  0.158  351 TYR AAA CB  
160   C CG  . TYR A 22  ? 0.502 0.630 0.598 -0.091 0.019  0.159  351 TYR AAA CG  
161   C CD1 . TYR A 22  ? 0.504 0.635 0.584 -0.081 0.024  0.158  351 TYR AAA CD1 
162   C CD2 . TYR A 22  ? 0.510 0.645 0.626 -0.106 0.011  0.163  351 TYR AAA CD2 
163   C CE1 . TYR A 22  ? 0.493 0.641 0.576 -0.083 0.021  0.165  351 TYR AAA CE1 
164   C CE2 . TYR A 22  ? 0.493 0.649 0.611 -0.112 0.006  0.165  351 TYR AAA CE2 
165   C CZ  . TYR A 22  ? 0.488 0.654 0.590 -0.099 0.010  0.169  351 TYR AAA CZ  
166   O OH  . TYR A 22  ? 0.484 0.679 0.589 -0.102 0.006  0.177  351 TYR AAA OH  
167   N N   . ALA A 23  ? 0.507 0.584 0.576 -0.103 0.012  0.118  352 ALA AAA N   
168   C CA  . ALA A 23  ? 0.522 0.595 0.589 -0.115 0.005  0.106  352 ALA AAA CA  
169   C C   . ALA A 23  ? 0.511 0.563 0.558 -0.112 0.007  0.090  352 ALA AAA C   
170   O O   . ALA A 23  ? 0.518 0.576 0.554 -0.112 0.004  0.084  352 ALA AAA O   
171   C CB  . ALA A 23  ? 0.520 0.621 0.587 -0.115 0.001  0.114  352 ALA AAA CB  
172   N N   . TRP A 24  ? 0.510 0.544 0.555 -0.108 0.011  0.086  353 TRP AAA N   
173   C CA  . TRP A 24  ? 0.499 0.517 0.527 -0.103 0.014  0.074  353 TRP AAA CA  
174   C C   . TRP A 24  ? 0.506 0.514 0.529 -0.111 0.009  0.060  353 TRP AAA C   
175   O O   . TRP A 24  ? 0.516 0.521 0.551 -0.123 0.006  0.055  353 TRP AAA O   
176   C CB  . TRP A 24  ? 0.482 0.493 0.513 -0.098 0.019  0.076  353 TRP AAA CB  
177   C CG  . TRP A 24  ? 0.476 0.481 0.528 -0.102 0.021  0.084  353 TRP AAA CG  
178   C CD1 . TRP A 24  ? 0.473 0.491 0.545 -0.100 0.024  0.101  353 TRP AAA CD1 
179   C CD2 . TRP A 24  ? 0.487 0.469 0.546 -0.106 0.024  0.076  353 TRP AAA CD2 
180   N NE1 . TRP A 24  ? 0.472 0.476 0.566 -0.103 0.030  0.106  353 TRP AAA NE1 
181   C CE2 . TRP A 24  ? 0.496 0.475 0.582 -0.107 0.031  0.090  353 TRP AAA CE2 
182   C CE3 . TRP A 24  ? 0.492 0.457 0.539 -0.108 0.024  0.060  353 TRP AAA CE3 
183   C CZ2 . TRP A 24  ? 0.518 0.471 0.619 -0.109 0.040  0.087  353 TRP AAA CZ2 
184   C CZ3 . TRP A 24  ? 0.516 0.457 0.574 -0.111 0.032  0.055  353 TRP AAA CZ3 
185   C CH2 . TRP A 24  ? 0.524 0.457 0.611 -0.112 0.041  0.068  353 TRP AAA CH2 
186   N N   . ASN A 25  ? 0.514 0.519 0.520 -0.106 0.010  0.053  354 ASN AAA N   
187   C CA  . ASN A 25  ? 0.545 0.549 0.541 -0.111 0.007  0.041  354 ASN AAA CA  
188   C C   . ASN A 25  ? 0.564 0.544 0.556 -0.111 0.010  0.029  354 ASN AAA C   
189   O O   . ASN A 25  ? 0.576 0.549 0.567 -0.103 0.016  0.033  354 ASN AAA O   
190   C CB  . ASN A 25  ? 0.559 0.577 0.543 -0.103 0.009  0.046  354 ASN AAA CB  
191   C CG  . ASN A 25  ? 0.578 0.605 0.551 -0.105 0.005  0.037  354 ASN AAA CG  
192   O OD1 . ASN A 25  ? 0.611 0.625 0.575 -0.101 0.009  0.029  354 ASN AAA OD1 
193   N ND2 . ASN A 25  ? 0.600 0.656 0.575 -0.113 -0.002 0.037  354 ASN AAA ND2 
194   N N   . ARG A 26  ? 0.573 0.545 0.565 -0.120 0.008  0.015  355 ARG AAA N   
195   C CA  . ARG A 26  ? 0.600 0.550 0.587 -0.119 0.014  0.003  355 ARG AAA CA  
196   C C   . ARG A 26  ? 0.627 0.586 0.595 -0.120 0.011  -0.010 355 ARG AAA C   
197   O O   . ARG A 26  ? 0.622 0.597 0.586 -0.131 0.005  -0.021 355 ARG AAA O   
198   C CB  . ARG A 26  ? 0.622 0.553 0.621 -0.131 0.018  -0.011 355 ARG AAA CB  
199   C CG  . ARG A 26  ? 0.636 0.545 0.656 -0.128 0.028  -0.001 355 ARG AAA CG  
200   C CD  . ARG A 26  ? 0.644 0.524 0.669 -0.124 0.041  -0.009 355 ARG AAA CD  
201   N NE  . ARG A 26  ? 0.638 0.519 0.676 -0.110 0.048  0.015  355 ARG AAA NE  
202   C CZ  . ARG A 26  ? 0.623 0.489 0.685 -0.104 0.061  0.028  355 ARG AAA CZ  
203   N NH1 . ARG A 26  ? 0.678 0.514 0.757 -0.113 0.073  0.016  355 ARG AAA NH1 
204   N NH2 . ARG A 26  ? 0.622 0.506 0.693 -0.090 0.065  0.052  355 ARG AAA NH2 
205   N N   . LYS A 27  ? 0.647 0.599 0.604 -0.109 0.016  -0.010 356 LYS AAA N   
206   C CA  . LYS A 27  ? 0.680 0.638 0.621 -0.109 0.016  -0.022 356 LYS AAA CA  
207   C C   . LYS A 27  ? 0.686 0.616 0.627 -0.106 0.025  -0.032 356 LYS AAA C   
208   O O   . LYS A 27  ? 0.662 0.579 0.611 -0.097 0.031  -0.021 356 LYS AAA O   
209   C CB  . LYS A 27  ? 0.723 0.697 0.654 -0.097 0.017  -0.011 356 LYS AAA CB  
210   C CG  . LYS A 27  ? 0.783 0.780 0.717 -0.096 0.013  0.004  356 LYS AAA CG  
211   C CD  . LYS A 27  ? 0.813 0.820 0.743 -0.084 0.020  0.017  356 LYS AAA CD  
212   C CE  . LYS A 27  ? 0.845 0.871 0.782 -0.079 0.022  0.035  356 LYS AAA CE  
213   N NZ  . LYS A 27  ? 0.843 0.851 0.791 -0.079 0.026  0.039  356 LYS AAA NZ  
214   N N   . ARG A 28  ? 0.737 0.661 0.671 -0.114 0.027  -0.053 357 ARG AAA N   
215   C CA  . ARG A 28  ? 0.746 0.643 0.679 -0.109 0.040  -0.063 357 ARG AAA CA  
216   C C   . ARG A 28  ? 0.699 0.607 0.615 -0.096 0.041  -0.060 357 ARG AAA C   
217   O O   . ARG A 28  ? 0.661 0.597 0.561 -0.097 0.034  -0.062 357 ARG AAA O   
218   C CB  . ARG A 28  ? 0.832 0.717 0.763 -0.125 0.044  -0.092 357 ARG AAA CB  
219   C CG  . ARG A 28  ? 0.917 0.764 0.853 -0.119 0.062  -0.103 357 ARG AAA CG  
220   C CD  . ARG A 28  ? 1.024 0.848 0.967 -0.139 0.071  -0.132 357 ARG AAA CD  
221   N NE  . ARG A 28  ? 1.164 0.972 1.092 -0.133 0.085  -0.151 357 ARG AAA NE  
222   C CZ  . ARG A 28  ? 1.267 1.031 1.207 -0.125 0.107  -0.155 357 ARG AAA CZ  
223   N NH1 . ARG A 28  ? 1.335 1.069 1.307 -0.123 0.120  -0.141 357 ARG AAA NH1 
224   N NH2 . ARG A 28  ? 1.249 1.004 1.173 -0.116 0.119  -0.170 357 ARG AAA NH2 
225   N N   . ILE A 29  ? 0.675 0.567 0.596 -0.084 0.050  -0.051 358 ILE AAA N   
226   C CA  . ILE A 29  ? 0.676 0.577 0.584 -0.072 0.054  -0.048 358 ILE AAA CA  
227   C C   . ILE A 29  ? 0.709 0.587 0.614 -0.067 0.068  -0.061 358 ILE AAA C   
228   O O   . ILE A 29  ? 0.743 0.598 0.667 -0.063 0.079  -0.054 358 ILE AAA O   
229   C CB  . ILE A 29  ? 0.652 0.563 0.569 -0.064 0.054  -0.026 358 ILE AAA CB  
230   C CG1 . ILE A 29  ? 0.645 0.574 0.562 -0.069 0.044  -0.017 358 ILE AAA CG1 
231   C CG2 . ILE A 29  ? 0.643 0.561 0.553 -0.053 0.060  -0.021 358 ILE AAA CG2 
232   C CD1 . ILE A 29  ? 0.644 0.579 0.571 -0.066 0.045  -0.003 358 ILE AAA CD1 
233   N N   . SER A 30  ? 0.718 0.603 0.604 -0.066 0.070  -0.077 359 SER AAA N   
234   C CA  . SER A 30  ? 0.758 0.620 0.639 -0.061 0.087  -0.093 359 SER AAA CA  
235   C C   . SER A 30  ? 0.752 0.637 0.609 -0.055 0.087  -0.102 359 SER AAA C   
236   O O   . SER A 30  ? 0.709 0.630 0.554 -0.058 0.074  -0.099 359 SER AAA O   
237   C CB  . SER A 30  ? 0.811 0.646 0.698 -0.076 0.094  -0.119 359 SER AAA CB  
238   O OG  . SER A 30  ? 0.815 0.675 0.690 -0.094 0.080  -0.135 359 SER AAA OG  
239   N N   . ASN A 31  ? 0.788 0.655 0.640 -0.044 0.103  -0.111 360 ASN AAA N   
240   C CA  . ASN A 31  ? 0.851 0.739 0.679 -0.037 0.107  -0.122 360 ASN AAA CA  
241   C C   . ASN A 31  ? 0.798 0.724 0.622 -0.028 0.096  -0.096 360 ASN AAA C   
242   O O   . ASN A 31  ? 0.785 0.747 0.592 -0.031 0.088  -0.100 360 ASN AAA O   
243   C CB  . ASN A 31  ? 0.910 0.809 0.717 -0.053 0.106  -0.158 360 ASN AAA CB  
244   C CG  . ASN A 31  ? 0.980 0.830 0.796 -0.064 0.122  -0.185 360 ASN AAA CG  
245   O OD1 . ASN A 31  ? 1.017 0.865 0.836 -0.085 0.116  -0.205 360 ASN AAA OD1 
246   N ND2 . ASN A 31  ? 1.022 0.835 0.848 -0.049 0.144  -0.183 360 ASN AAA ND2 
247   N N   . CYS A 32  ? 0.771 0.692 0.614 -0.019 0.097  -0.069 361 CYS AAA N   
248   C CA  . CYS A 32  ? 0.738 0.687 0.585 -0.013 0.091  -0.045 361 CYS AAA CA  
249   C C   . CYS A 32  ? 0.700 0.642 0.565 -0.004 0.097  -0.024 361 CYS AAA C   
250   O O   . CYS A 32  ? 0.703 0.625 0.581 -0.003 0.103  -0.023 361 CYS AAA O   
251   C CB  . CYS A 32  ? 0.733 0.695 0.584 -0.024 0.077  -0.039 361 CYS AAA CB  
252   S SG  . CYS A 32  ? 0.752 0.690 0.624 -0.035 0.072  -0.036 361 CYS AAA SG  
253   N N   . VAL A 33  ? 0.666 0.631 0.533 0.002  0.097  -0.007 362 VAL AAA N   
254   C CA  . VAL A 33  ? 0.634 0.608 0.521 0.006  0.101  0.014  362 VAL AAA CA  
255   C C   . VAL A 33  ? 0.608 0.586 0.510 -0.007 0.092  0.022  362 VAL AAA C   
256   O O   . VAL A 33  ? 0.609 0.594 0.508 -0.012 0.087  0.023  362 VAL AAA O   
257   C CB  . VAL A 33  ? 0.618 0.614 0.503 0.016  0.107  0.027  362 VAL AAA CB  
258   C CG1 . VAL A 33  ? 0.612 0.622 0.517 0.016  0.110  0.046  362 VAL AAA CG1 
259   C CG2 . VAL A 33  ? 0.632 0.627 0.499 0.030  0.117  0.017  362 VAL AAA CG2 
260   N N   . ALA A 34  ? 0.602 0.576 0.517 -0.010 0.091  0.027  363 ALA AAA N   
261   C CA  . ALA A 34  ? 0.612 0.592 0.540 -0.023 0.083  0.032  363 ALA AAA CA  
262   C C   . ALA A 34  ? 0.598 0.604 0.539 -0.027 0.086  0.044  363 ALA AAA C   
263   O O   . ALA A 34  ? 0.579 0.602 0.530 -0.025 0.089  0.054  363 ALA AAA O   
264   C CB  . ALA A 34  ? 0.620 0.594 0.557 -0.024 0.082  0.033  363 ALA AAA CB  
265   N N   . ASP A 35  ? 0.608 0.617 0.549 -0.033 0.086  0.044  364 ASP AAA N   
266   C CA  . ASP A 35  ? 0.612 0.640 0.569 -0.043 0.090  0.051  364 ASP AAA CA  
267   C C   . ASP A 35  ? 0.586 0.614 0.551 -0.060 0.086  0.044  364 ASP AAA C   
268   O O   . ASP A 35  ? 0.596 0.607 0.560 -0.064 0.087  0.040  364 ASP AAA O   
269   C CB  . ASP A 35  ? 0.630 0.659 0.589 -0.040 0.098  0.058  364 ASP AAA CB  
270   C CG  . ASP A 35  ? 0.634 0.684 0.612 -0.049 0.105  0.065  364 ASP AAA CG  
271   O OD1 . ASP A 35  ? 0.664 0.731 0.652 -0.062 0.101  0.062  364 ASP AAA OD1 
272   O OD2 . ASP A 35  ? 0.688 0.743 0.671 -0.045 0.113  0.075  364 ASP AAA OD2 
273   N N   . TYR A 36  ? 0.577 0.628 0.553 -0.069 0.084  0.045  365 TYR AAA N   
274   C CA  . TYR A 36  ? 0.608 0.667 0.589 -0.086 0.080  0.036  365 TYR AAA CA  
275   C C   . TYR A 36  ? 0.594 0.662 0.588 -0.105 0.087  0.029  365 TYR AAA C   
276   O O   . TYR A 36  ? 0.587 0.662 0.585 -0.121 0.086  0.017  365 TYR AAA O   
277   C CB  . TYR A 36  ? 0.603 0.691 0.587 -0.085 0.074  0.041  365 TYR AAA CB  
278   C CG  . TYR A 36  ? 0.633 0.702 0.609 -0.071 0.070  0.045  365 TYR AAA CG  
279   C CD1 . TYR A 36  ? 0.648 0.704 0.621 -0.075 0.065  0.038  365 TYR AAA CD1 
280   C CD2 . TYR A 36  ? 0.661 0.722 0.635 -0.053 0.074  0.055  365 TYR AAA CD2 
281   C CE1 . TYR A 36  ? 0.658 0.696 0.627 -0.065 0.063  0.042  365 TYR AAA CE1 
282   C CE2 . TYR A 36  ? 0.674 0.712 0.644 -0.043 0.075  0.055  365 TYR AAA CE2 
283   C CZ  . TYR A 36  ? 0.651 0.679 0.620 -0.050 0.069  0.049  365 TYR AAA CZ  
284   O OH  . TYR A 36  ? 0.681 0.687 0.649 -0.043 0.070  0.049  365 TYR AAA OH  
285   N N   . SER A 37  ? 0.594 0.665 0.596 -0.104 0.095  0.035  366 SER AAA N   
286   C CA  . SER A 37  ? 0.633 0.714 0.653 -0.125 0.105  0.028  366 SER AAA CA  
287   C C   . SER A 37  ? 0.636 0.683 0.660 -0.134 0.114  0.016  366 SER AAA C   
288   O O   . SER A 37  ? 0.629 0.679 0.667 -0.157 0.123  0.001  366 SER AAA O   
289   C CB  . SER A 37  ? 0.630 0.720 0.661 -0.121 0.113  0.041  366 SER AAA CB  
290   O OG  . SER A 37  ? 0.625 0.693 0.645 -0.098 0.116  0.053  366 SER AAA OG  
291   N N   . VAL A 38  ? 0.654 0.671 0.667 -0.118 0.114  0.022  367 VAL AAA N   
292   C CA  . VAL A 38  ? 0.669 0.657 0.688 -0.122 0.125  0.015  367 VAL AAA CA  
293   C C   . VAL A 38  ? 0.668 0.661 0.684 -0.139 0.120  -0.003 367 VAL AAA C   
294   O O   . VAL A 38  ? 0.689 0.669 0.717 -0.155 0.134  -0.017 367 VAL AAA O   
295   C CB  . VAL A 38  ? 0.715 0.685 0.722 -0.100 0.123  0.029  367 VAL AAA CB  
296   C CG1 . VAL A 38  ? 0.729 0.704 0.716 -0.092 0.106  0.026  367 VAL AAA CG1 
297   C CG2 . VAL A 38  ? 0.731 0.675 0.748 -0.099 0.139  0.032  367 VAL AAA CG2 
298   N N   . LEU A 39  ? 0.651 0.664 0.653 -0.135 0.104  -0.004 368 LEU AAA N   
299   C CA  . LEU A 39  ? 0.660 0.689 0.659 -0.147 0.098  -0.018 368 LEU AAA CA  
300   C C   . LEU A 39  ? 0.677 0.742 0.685 -0.171 0.100  -0.032 368 LEU AAA C   
301   O O   . LEU A 39  ? 0.726 0.799 0.735 -0.189 0.104  -0.051 368 LEU AAA O   
302   C CB  . LEU A 39  ? 0.647 0.690 0.634 -0.133 0.083  -0.008 368 LEU AAA CB  
303   C CG  . LEU A 39  ? 0.664 0.676 0.641 -0.115 0.080  0.001  368 LEU AAA CG  
304   C CD1 . LEU A 39  ? 0.674 0.698 0.644 -0.105 0.068  0.008  368 LEU AAA CD1 
305   C CD2 . LEU A 39  ? 0.674 0.661 0.650 -0.117 0.086  -0.005 368 LEU AAA CD2 
306   N N   . TYR A 40  ? 0.677 0.701 0.580 -0.073 0.063  -0.006 369 TYR AAA N   
307   C CA  . TYR A 40  ? 0.656 0.723 0.609 -0.088 0.076  -0.003 369 TYR AAA CA  
308   C C   . TYR A 40  ? 0.681 0.729 0.622 -0.112 0.079  0.006  369 TYR AAA C   
309   O O   . TYR A 40  ? 0.655 0.726 0.630 -0.129 0.074  0.006  369 TYR AAA O   
310   C CB  . TYR A 40  ? 0.659 0.761 0.632 -0.086 0.106  -0.004 369 TYR AAA CB  
311   C CG  . TYR A 40  ? 0.651 0.772 0.644 -0.060 0.109  -0.014 369 TYR AAA CG  
312   C CD1 . TYR A 40  ? 0.621 0.749 0.638 -0.047 0.083  -0.019 369 TYR AAA CD1 
313   C CD2 . TYR A 40  ? 0.683 0.811 0.669 -0.047 0.142  -0.018 369 TYR AAA CD2 
314   C CE1 . TYR A 40  ? 0.622 0.758 0.655 -0.023 0.088  -0.026 369 TYR AAA CE1 
315   C CE2 . TYR A 40  ? 0.703 0.838 0.704 -0.019 0.148  -0.028 369 TYR AAA CE2 
316   C CZ  . TYR A 40  ? 0.661 0.799 0.687 -0.007 0.119  -0.031 369 TYR AAA CZ  
317   O OH  . TYR A 40  ? 0.686 0.822 0.723 0.021  0.127  -0.039 369 TYR AAA OH  
318   N N   . ASN A 41  ? 0.713 0.712 0.598 -0.114 0.086  0.015  370 ASN AAA N   
319   C CA  . ASN A 41  ? 0.752 0.715 0.612 -0.137 0.095  0.026  370 ASN AAA CA  
320   C C   . ASN A 41  ? 0.738 0.658 0.579 -0.129 0.073  0.029  370 ASN AAA C   
321   O O   . ASN A 41  ? 0.778 0.650 0.586 -0.140 0.080  0.039  370 ASN AAA O   
322   C CB  . ASN A 41  ? 0.828 0.754 0.631 -0.140 0.118  0.037  370 ASN AAA CB  
323   C CG  . ASN A 41  ? 0.851 0.819 0.676 -0.150 0.152  0.035  370 ASN AAA CG  
324   O OD1 . ASN A 41  ? 0.851 0.873 0.740 -0.167 0.161  0.033  370 ASN AAA OD1 
325   N ND2 . ASN A 41  ? 0.904 0.850 0.677 -0.137 0.170  0.037  370 ASN AAA ND2 
326   N N   . SER A 42  ? 0.703 0.637 0.565 -0.109 0.052  0.022  371 SER AAA N   
327   C CA  . SER A 42  ? 0.699 0.605 0.559 -0.097 0.037  0.023  371 SER AAA CA  
328   C C   . SER A 42  ? 0.671 0.586 0.555 -0.112 0.037  0.015  371 SER AAA C   
329   O O   . SER A 42  ? 0.635 0.596 0.553 -0.116 0.034  0.007  371 SER AAA O   
330   C CB  . SER A 42  ? 0.684 0.604 0.557 -0.074 0.018  0.021  371 SER AAA CB  
331   O OG  . SER A 42  ? 0.705 0.609 0.543 -0.064 0.011  0.027  371 SER AAA OG  
332   N N   . ALA A 43  ? 0.697 0.566 0.560 -0.116 0.041  0.017  372 ALA AAA N   
333   C CA  . ALA A 43  ? 0.723 0.581 0.587 -0.130 0.041  0.007  372 ALA AAA CA  
334   C C   . ALA A 43  ? 0.723 0.563 0.588 -0.105 0.038  0.004  372 ALA AAA C   
335   O O   . ALA A 43  ? 0.830 0.660 0.688 -0.113 0.040  -0.005 372 ALA AAA O   
336   C CB  . ALA A 43  ? 0.761 0.568 0.591 -0.157 0.052  0.007  372 ALA AAA CB  
337   N N   . SER A 44  ? 0.689 0.526 0.562 -0.077 0.035  0.013  373 SER AAA N   
338   C CA  . SER A 44  ? 0.689 0.511 0.573 -0.052 0.040  0.014  373 SER AAA CA  
339   C C   . SER A 44  ? 0.616 0.489 0.542 -0.042 0.033  0.010  373 SER AAA C   
340   O O   . SER A 44  ? 0.630 0.500 0.573 -0.026 0.043  0.010  373 SER AAA O   
341   C CB  . SER A 44  ? 0.738 0.533 0.618 -0.027 0.039  0.029  373 SER AAA CB  
342   O OG  . SER A 44  ? 0.841 0.566 0.678 -0.029 0.055  0.031  373 SER AAA OG  
343   N N   . PHE A 45  ? 0.563 0.477 0.506 -0.051 0.021  0.007  374 PHE AAA N   
344   C CA  . PHE A 45  ? 0.529 0.477 0.503 -0.047 0.016  0.003  374 PHE AAA CA  
345   C C   . PHE A 45  ? 0.527 0.462 0.488 -0.054 0.028  -0.004 374 PHE AAA C   
346   O O   . PHE A 45  ? 0.513 0.435 0.448 -0.072 0.027  -0.009 374 PHE AAA O   
347   C CB  . PHE A 45  ? 0.479 0.458 0.462 -0.053 0.004  -0.000 374 PHE AAA CB  
348   C CG  . PHE A 45  ? 0.454 0.437 0.433 -0.047 -0.007 0.004  374 PHE AAA CG  
349   C CD1 . PHE A 45  ? 0.446 0.430 0.440 -0.033 -0.018 0.010  374 PHE AAA CD1 
350   C CD2 . PHE A 45  ? 0.462 0.452 0.426 -0.053 -0.008 0.001  374 PHE AAA CD2 
351   C CE1 . PHE A 45  ? 0.476 0.459 0.455 -0.029 -0.036 0.014  374 PHE AAA CE1 
352   C CE2 . PHE A 45  ? 0.472 0.455 0.415 -0.048 -0.017 0.003  374 PHE AAA CE2 
353   C CZ  . PHE A 45  ? 0.484 0.460 0.428 -0.037 -0.034 0.009  374 PHE AAA CZ  
354   N N   . SER A 46  ? 0.554 0.491 0.533 -0.044 0.038  -0.003 375 SER AAA N   
355   C CA  . SER A 46  ? 0.592 0.507 0.544 -0.049 0.053  -0.009 375 SER AAA CA  
356   C C   . SER A 46  ? 0.560 0.496 0.510 -0.060 0.039  -0.010 375 SER AAA C   
357   O O   . SER A 46  ? 0.596 0.510 0.508 -0.070 0.040  -0.014 375 SER AAA O   
358   C CB  . SER A 46  ? 0.614 0.526 0.588 -0.033 0.076  -0.005 375 SER AAA CB  
359   O OG  . SER A 46  ? 0.549 0.505 0.578 -0.027 0.069  0.002  375 SER AAA OG  
360   N N   . THR A 47  ? 0.504 0.472 0.487 -0.057 0.026  -0.006 376 THR AAA N   
361   C CA  . THR A 47  ? 0.479 0.462 0.463 -0.061 0.015  -0.006 376 THR AAA CA  
362   C C   . THR A 47  ? 0.450 0.458 0.458 -0.057 0.002  -0.007 376 THR AAA C   
363   O O   . THR A 47  ? 0.401 0.415 0.425 -0.052 -0.000 -0.007 376 THR AAA O   
364   C CB  . THR A 47  ? 0.486 0.460 0.473 -0.058 0.026  -0.001 376 THR AAA CB  
365   O OG1 . THR A 47  ? 0.463 0.435 0.435 -0.060 0.015  0.002  376 THR AAA OG1 
366   C CG2 . THR A 47  ? 0.488 0.480 0.520 -0.054 0.029  0.001  376 THR AAA CG2 
367   N N   . PHE A 48  ? 0.433 0.454 0.439 -0.057 -0.008 -0.007 377 PHE AAA N   
368   C CA  . PHE A 48  ? 0.446 0.482 0.466 -0.051 -0.013 -0.010 377 PHE AAA CA  
369   C C   . PHE A 48  ? 0.445 0.488 0.469 -0.043 -0.018 -0.008 377 PHE AAA C   
370   O O   . PHE A 48  ? 0.418 0.484 0.448 -0.045 -0.024 -0.006 377 PHE AAA O   
371   C CB  . PHE A 48  ? 0.468 0.515 0.485 -0.055 -0.010 -0.012 377 PHE AAA CB  
372   C CG  . PHE A 48  ? 0.506 0.562 0.524 -0.048 -0.007 -0.016 377 PHE AAA CG  
373   C CD1 . PHE A 48  ? 0.529 0.584 0.552 -0.036 -0.009 -0.020 377 PHE AAA CD1 
374   C CD2 . PHE A 48  ? 0.549 0.606 0.554 -0.053 0.000  -0.016 377 PHE AAA CD2 
375   C CE1 . PHE A 48  ? 0.574 0.627 0.588 -0.027 -0.000 -0.027 377 PHE AAA CE1 
376   C CE2 . PHE A 48  ? 0.587 0.645 0.582 -0.046 0.009  -0.021 377 PHE AAA CE2 
377   C CZ  . PHE A 48  ? 0.618 0.674 0.617 -0.032 0.010  -0.027 377 PHE AAA CZ  
378   N N   . LYS A 49  ? 0.427 0.452 0.451 -0.037 -0.019 -0.006 378 LYS AAA N   
379   C CA  . LYS A 49  ? 0.471 0.491 0.494 -0.025 -0.024 -0.000 378 LYS AAA CA  
380   C C   . LYS A 49  ? 0.489 0.490 0.514 -0.013 -0.021 -0.006 378 LYS AAA C   
381   O O   . LYS A 49  ? 0.512 0.493 0.534 -0.023 -0.019 -0.012 378 LYS AAA O   
382   C CB  . LYS A 49  ? 0.520 0.512 0.521 -0.028 -0.024 0.009  378 LYS AAA CB  
383   C CG  . LYS A 49  ? 0.545 0.537 0.524 -0.039 -0.026 0.013  378 LYS AAA CG  
384   C CD  . LYS A 49  ? 0.568 0.523 0.514 -0.041 -0.019 0.023  378 LYS AAA CD  
385   C CE  . LYS A 49  ? 0.589 0.530 0.493 -0.051 -0.019 0.025  378 LYS AAA CE  
386   N NZ  . LYS A 49  ? 0.648 0.546 0.510 -0.054 -0.006 0.035  378 LYS AAA NZ  
387   N N   . CYS A 50  ? 0.491 0.479 0.459 -0.050 -0.018 -0.015 379 CYS AAA N   
388   C CA  . CYS A 50  ? 0.491 0.471 0.455 -0.042 -0.018 -0.012 379 CYS AAA CA  
389   C C   . CYS A 50  ? 0.485 0.466 0.447 -0.036 -0.027 -0.009 379 CYS AAA C   
390   O O   . CYS A 50  ? 0.427 0.421 0.395 -0.037 -0.032 -0.010 379 CYS AAA O   
391   C CB  . CYS A 50  ? 0.498 0.485 0.472 -0.037 -0.011 -0.014 379 CYS AAA CB  
392   S SG  . CYS A 50  ? 0.520 0.504 0.493 -0.045 -0.000 -0.015 379 CYS AAA SG  
393   N N   . TYR A 51  ? 0.514 0.479 0.465 -0.031 -0.028 -0.006 380 TYR AAA N   
394   C CA  . TYR A 51  ? 0.516 0.473 0.461 -0.025 -0.036 -0.001 380 TYR AAA CA  
395   C C   . TYR A 51  ? 0.514 0.460 0.459 -0.015 -0.035 -0.002 380 TYR AAA C   
396   O O   . TYR A 51  ? 0.573 0.506 0.511 -0.015 -0.030 -0.004 380 TYR AAA O   
397   C CB  . TYR A 51  ? 0.532 0.475 0.463 -0.032 -0.039 0.005  380 TYR AAA CB  
398   C CG  . TYR A 51  ? 0.518 0.471 0.448 -0.040 -0.038 0.004  380 TYR AAA CG  
399   C CD1 . TYR A 51  ? 0.483 0.438 0.414 -0.046 -0.031 0.001  380 TYR AAA CD1 
400   C CD2 . TYR A 51  ? 0.518 0.479 0.443 -0.040 -0.043 0.007  380 TYR AAA CD2 
401   C CE1 . TYR A 51  ? 0.486 0.447 0.415 -0.051 -0.030 0.000  380 TYR AAA CE1 
402   C CE2 . TYR A 51  ? 0.511 0.479 0.433 -0.046 -0.041 0.006  380 TYR AAA CE2 
403   C CZ  . TYR A 51  ? 0.508 0.476 0.432 -0.051 -0.034 0.002  380 TYR AAA CZ  
404   O OH  . TYR A 51  ? 0.500 0.472 0.419 -0.055 -0.032 -0.001 380 TYR AAA OH  
405   N N   . GLY A 52  ? 0.508 0.461 0.461 -0.004 -0.039 -0.001 381 GLY AAA N   
406   C CA  . GLY A 52  ? 0.520 0.462 0.473 0.009  -0.037 -0.002 381 GLY AAA CA  
407   C C   . GLY A 52  ? 0.514 0.471 0.480 0.014  -0.027 -0.009 381 GLY AAA C   
408   O O   . GLY A 52  ? 0.534 0.487 0.502 0.027  -0.025 -0.011 381 GLY AAA O   
409   N N   . VAL A 53  ? 0.507 0.482 0.482 0.005  -0.022 -0.011 382 VAL AAA N   
410   C CA  . VAL A 53  ? 0.552 0.547 0.543 0.007  -0.011 -0.015 382 VAL AAA CA  
411   C C   . VAL A 53  ? 0.515 0.532 0.521 -0.005 -0.011 -0.015 382 VAL AAA C   
412   O O   . VAL A 53  ? 0.566 0.576 0.563 -0.015 -0.015 -0.014 382 VAL AAA O   
413   C CB  . VAL A 53  ? 0.572 0.551 0.548 0.007  -0.002 -0.019 382 VAL AAA CB  
414   C CG1 . VAL A 53  ? 0.618 0.574 0.579 0.020  -0.002 -0.021 382 VAL AAA CG1 
415   C CG2 . VAL A 53  ? 0.570 0.536 0.532 -0.006 -0.002 -0.018 382 VAL AAA CG2 
416   N N   . SER A 54  ? 0.482 0.526 0.510 -0.003 -0.006 -0.017 383 SER AAA N   
417   C CA  . SER A 54  ? 0.482 0.545 0.527 -0.016 -0.005 -0.018 383 SER AAA CA  
418   C C   . SER A 54  ? 0.480 0.533 0.516 -0.025 0.006  -0.018 383 SER AAA C   
419   O O   . SER A 54  ? 0.482 0.530 0.513 -0.019 0.016  -0.018 383 SER AAA O   
420   C CB  . SER A 54  ? 0.501 0.598 0.575 -0.013 -0.004 -0.018 383 SER AAA CB  
421   O OG  . SER A 54  ? 0.513 0.626 0.602 -0.028 -0.004 -0.020 383 SER AAA OG  
422   N N   . PRO A 55  ? 0.473 0.522 0.507 -0.038 0.004  -0.019 384 PRO AAA N   
423   C CA  . PRO A 55  ? 0.481 0.521 0.510 -0.046 0.014  -0.018 384 PRO AAA CA  
424   C C   . PRO A 55  ? 0.478 0.537 0.525 -0.048 0.026  -0.017 384 PRO AAA C   
425   O O   . PRO A 55  ? 0.480 0.530 0.518 -0.049 0.036  -0.014 384 PRO AAA O   
426   C CB  . PRO A 55  ? 0.482 0.520 0.512 -0.059 0.009  -0.020 384 PRO AAA CB  
427   C CG  . PRO A 55  ? 0.476 0.511 0.499 -0.056 -0.003 -0.021 384 PRO AAA CG  
428   C CD  . PRO A 55  ? 0.476 0.525 0.508 -0.045 -0.007 -0.020 384 PRO AAA CD  
429   N N   . THR A 56  ? 0.476 0.562 0.548 -0.047 0.024  -0.018 385 THR AAA N   
430   C CA  . THR A 56  ? 0.508 0.619 0.604 -0.049 0.036  -0.016 385 THR AAA CA  
431   C C   . THR A 56  ? 0.517 0.628 0.606 -0.034 0.047  -0.014 385 THR AAA C   
432   O O   . THR A 56  ? 0.522 0.650 0.625 -0.035 0.060  -0.011 385 THR AAA O   
433   C CB  . THR A 56  ? 0.505 0.650 0.633 -0.052 0.029  -0.017 385 THR AAA CB  
434   O OG1 . THR A 56  ? 0.505 0.658 0.635 -0.036 0.021  -0.018 385 THR AAA OG1 
435   C CG2 . THR A 56  ? 0.508 0.652 0.640 -0.067 0.017  -0.020 385 THR AAA CG2 
436   N N   . LYS A 57  ? 0.530 0.622 0.598 -0.021 0.042  -0.016 386 LYS AAA N   
437   C CA  . LYS A 57  ? 0.559 0.647 0.618 -0.006 0.052  -0.017 386 LYS AAA CA  
438   C C   . LYS A 57  ? 0.541 0.598 0.566 -0.005 0.056  -0.018 386 LYS AAA C   
439   O O   . LYS A 57  ? 0.531 0.581 0.543 0.007  0.063  -0.020 386 LYS AAA O   
440   C CB  . LYS A 57  ? 0.603 0.691 0.663 0.010  0.043  -0.020 386 LYS AAA CB  
441   C CG  . LYS A 57  ? 0.629 0.751 0.722 0.012  0.036  -0.019 386 LYS AAA CG  
442   C CD  . LYS A 57  ? 0.656 0.811 0.776 0.020  0.048  -0.018 386 LYS AAA CD  
443   C CE  . LYS A 57  ? 0.713 0.862 0.824 0.041  0.057  -0.020 386 LYS AAA CE  
444   N NZ  . LYS A 57  ? 0.733 0.900 0.852 0.043  0.077  -0.020 386 LYS AAA NZ  
445   N N   . LEU A 58  ? 0.531 0.571 0.542 -0.016 0.051  -0.016 387 LEU AAA N   
446   C CA  . LEU A 58  ? 0.560 0.572 0.541 -0.015 0.052  -0.016 387 LEU AAA CA  
447   C C   . LEU A 58  ? 0.562 0.575 0.532 -0.011 0.067  -0.015 387 LEU AAA C   
448   O O   . LEU A 58  ? 0.595 0.588 0.539 -0.003 0.067  -0.018 387 LEU AAA O   
449   C CB  . LEU A 58  ? 0.575 0.575 0.549 -0.028 0.046  -0.013 387 LEU AAA CB  
450   C CG  . LEU A 58  ? 0.577 0.572 0.553 -0.031 0.032  -0.014 387 LEU AAA CG  
451   C CD1 . LEU A 58  ? 0.566 0.550 0.535 -0.041 0.029  -0.012 387 LEU AAA CD1 
452   C CD2 . LEU A 58  ? 0.595 0.574 0.556 -0.022 0.024  -0.017 387 LEU AAA CD2 
453   N N   . ASN A 59  ? 0.566 0.600 0.554 -0.015 0.079  -0.011 388 ASN AAA N   
454   C CA  . ASN A 59  ? 0.620 0.657 0.597 -0.011 0.095  -0.008 388 ASN AAA CA  
455   C C   . ASN A 59  ? 0.646 0.693 0.622 0.005  0.104  -0.013 388 ASN AAA C   
456   O O   . ASN A 59  ? 0.674 0.722 0.636 0.011  0.117  -0.012 388 ASN AAA O   
457   C CB  . ASN A 59  ? 0.602 0.655 0.596 -0.024 0.106  0.000  388 ASN AAA CB  
458   C CG  . ASN A 59  ? 0.611 0.643 0.588 -0.035 0.105  0.006  388 ASN AAA CG  
459   O OD1 . ASN A 59  ? 0.616 0.624 0.566 -0.032 0.097  0.004  388 ASN AAA OD1 
460   N ND2 . ASN A 59  ? 0.627 0.667 0.619 -0.048 0.112  0.013  388 ASN AAA ND2 
461   N N   . ASP A 60  ? 0.669 0.721 0.658 0.015  0.095  -0.018 389 ASP AAA N   
462   C CA  . ASP A 60  ? 0.686 0.749 0.679 0.033  0.103  -0.023 389 ASP AAA CA  
463   C C   . ASP A 60  ? 0.673 0.705 0.641 0.046  0.093  -0.031 389 ASP AAA C   
464   O O   . ASP A 60  ? 0.675 0.709 0.642 0.063  0.099  -0.036 389 ASP AAA O   
465   C CB  . ASP A 60  ? 0.717 0.814 0.750 0.036  0.102  -0.022 389 ASP AAA CB  
466   C CG  . ASP A 60  ? 0.766 0.895 0.829 0.022  0.111  -0.014 389 ASP AAA CG  
467   O OD1 . ASP A 60  ? 0.870 1.011 0.931 0.022  0.129  -0.011 389 ASP AAA OD1 
468   O OD2 . ASP A 60  ? 0.856 0.997 0.940 0.009  0.100  -0.012 389 ASP AAA OD2 
469   N N   . LEU A 61  ? 0.651 0.655 0.598 0.037  0.079  -0.032 390 LEU AAA N   
470   C CA  . LEU A 61  ? 0.668 0.644 0.597 0.046  0.067  -0.038 390 LEU AAA CA  
471   C C   . LEU A 61  ? 0.682 0.626 0.573 0.046  0.066  -0.043 390 LEU AAA C   
472   O O   . LEU A 61  ? 0.695 0.638 0.576 0.036  0.069  -0.040 390 LEU AAA O   
473   C CB  . LEU A 61  ? 0.657 0.628 0.596 0.036  0.051  -0.035 390 LEU AAA CB  
474   C CG  . LEU A 61  ? 0.633 0.631 0.605 0.038  0.048  -0.031 390 LEU AAA CG  
475   C CD1 . LEU A 61  ? 0.654 0.644 0.628 0.029  0.032  -0.028 390 LEU AAA CD1 
476   C CD2 . LEU A 61  ? 0.632 0.636 0.612 0.058  0.051  -0.035 390 LEU AAA CD2 
477   N N   . CYS A 62  ? 0.703 0.623 0.576 0.057  0.062  -0.051 391 CYS AAA N   
478   C CA  . CYS A 62  ? 0.720 0.607 0.556 0.058  0.058  -0.059 391 CYS AAA CA  
479   C C   . CYS A 62  ? 0.694 0.554 0.522 0.053  0.041  -0.061 391 CYS AAA C   
480   O O   . CYS A 62  ? 0.669 0.529 0.513 0.058  0.035  -0.060 391 CYS AAA O   
481   C CB  . CYS A 62  ? 0.771 0.650 0.589 0.077  0.070  -0.069 391 CYS AAA CB  
482   S SG  . CYS A 62  ? 0.786 0.697 0.608 0.082  0.093  -0.065 391 CYS AAA SG  
483   N N   . PHE A 63  ? 0.686 0.526 0.493 0.042  0.032  -0.062 392 PHE AAA N   
484   C CA  . PHE A 63  ? 0.694 0.510 0.494 0.033  0.015  -0.062 392 PHE AAA CA  
485   C C   . PHE A 63  ? 0.743 0.530 0.509 0.032  0.009  -0.072 392 PHE AAA C   
486   O O   . PHE A 63  ? 0.763 0.552 0.511 0.034  0.016  -0.075 392 PHE AAA O   
487   C CB  . PHE A 63  ? 0.653 0.485 0.469 0.017  0.008  -0.052 392 PHE AAA CB  
488   C CG  . PHE A 63  ? 0.608 0.468 0.455 0.017  0.013  -0.045 392 PHE AAA CG  
489   C CD1 . PHE A 63  ? 0.607 0.466 0.468 0.022  0.008  -0.043 392 PHE AAA CD1 
490   C CD2 . PHE A 63  ? 0.581 0.466 0.441 0.012  0.021  -0.039 392 PHE AAA CD2 
491   C CE1 . PHE A 63  ? 0.587 0.472 0.474 0.022  0.009  -0.037 392 PHE AAA CE1 
492   C CE2 . PHE A 63  ? 0.566 0.474 0.454 0.011  0.023  -0.034 392 PHE AAA CE2 
493   C CZ  . PHE A 63  ? 0.567 0.476 0.467 0.016  0.017  -0.033 392 PHE AAA CZ  
494   N N   . THR A 64  ? 0.752 0.510 0.509 0.029  -0.004 -0.076 393 THR AAA N   
495   C CA  . THR A 64  ? 0.796 0.522 0.522 0.025  -0.013 -0.086 393 THR AAA CA  
496   C C   . THR A 64  ? 0.789 0.522 0.511 0.007  -0.022 -0.081 393 THR AAA C   
497   O O   . THR A 64  ? 0.800 0.521 0.496 0.005  -0.026 -0.088 393 THR AAA O   
498   C CB  . THR A 64  ? 0.811 0.503 0.533 0.026  -0.023 -0.091 393 THR AAA CB  
499   O OG1 . THR A 64  ? 0.771 0.469 0.516 0.017  -0.030 -0.079 393 THR AAA OG1 
500   C CG2 . THR A 64  ? 0.839 0.521 0.558 0.048  -0.013 -0.098 393 THR AAA CG2 
501   N N   . ASN A 65  ? 0.781 0.536 0.528 -0.003 -0.025 -0.069 394 ASN AAA N   
502   C CA  . ASN A 65  ? 0.784 0.550 0.534 -0.018 -0.033 -0.062 394 ASN AAA CA  
503   C C   . ASN A 65  ? 0.721 0.516 0.499 -0.022 -0.028 -0.050 394 ASN AAA C   
504   O O   . ASN A 65  ? 0.696 0.497 0.493 -0.018 -0.025 -0.047 394 ASN AAA O   
505   C CB  . ASN A 65  ? 0.876 0.622 0.622 -0.031 -0.049 -0.063 394 ASN AAA CB  
506   C CG  . ASN A 65  ? 0.939 0.695 0.683 -0.045 -0.059 -0.059 394 ASN AAA CG  
507   O OD1 . ASN A 65  ? 0.992 0.745 0.716 -0.044 -0.061 -0.064 394 ASN AAA OD1 
508   N ND2 . ASN A 65  ? 0.942 0.714 0.709 -0.055 -0.064 -0.049 394 ASN AAA ND2 
509   N N   . VAL A 66  ? 0.674 0.486 0.454 -0.029 -0.028 -0.044 395 VAL AAA N   
510   C CA  . VAL A 66  ? 0.633 0.469 0.438 -0.034 -0.025 -0.033 395 VAL AAA CA  
511   C C   . VAL A 66  ? 0.633 0.473 0.439 -0.045 -0.035 -0.028 395 VAL AAA C   
512   O O   . VAL A 66  ? 0.661 0.496 0.449 -0.047 -0.040 -0.031 395 VAL AAA O   
513   C CB  . VAL A 66  ? 0.611 0.464 0.422 -0.028 -0.012 -0.030 395 VAL AAA CB  
514   C CG1 . VAL A 66  ? 0.579 0.451 0.412 -0.034 -0.010 -0.021 395 VAL AAA CG1 
515   C CG2 . VAL A 66  ? 0.624 0.478 0.437 -0.017 -0.002 -0.035 395 VAL AAA CG2 
516   N N   . TYR A 67  ? 0.612 0.463 0.438 -0.052 -0.039 -0.021 396 TYR AAA N   
517   C CA  . TYR A 67  ? 0.620 0.482 0.453 -0.061 -0.046 -0.015 396 TYR AAA CA  
518   C C   . TYR A 67  ? 0.585 0.468 0.436 -0.060 -0.038 -0.007 396 TYR AAA C   
519   O O   . TYR A 67  ? 0.554 0.440 0.416 -0.057 -0.032 -0.007 396 TYR AAA O   
520   C CB  . TYR A 67  ? 0.670 0.526 0.510 -0.071 -0.055 -0.013 396 TYR AAA CB  
521   C CG  . TYR A 67  ? 0.730 0.564 0.553 -0.075 -0.065 -0.021 396 TYR AAA CG  
522   C CD1 . TYR A 67  ? 0.748 0.580 0.556 -0.078 -0.073 -0.024 396 TYR AAA CD1 
523   C CD2 . TYR A 67  ? 0.784 0.597 0.604 -0.077 -0.069 -0.024 396 TYR AAA CD2 
524   C CE1 . TYR A 67  ? 0.821 0.631 0.612 -0.084 -0.084 -0.032 396 TYR AAA CE1 
525   C CE2 . TYR A 67  ? 0.861 0.649 0.664 -0.082 -0.079 -0.031 396 TYR AAA CE2 
526   C CZ  . TYR A 67  ? 0.870 0.656 0.658 -0.086 -0.087 -0.036 396 TYR AAA CZ  
527   O OH  . TYR A 67  ? 0.998 0.758 0.766 -0.092 -0.098 -0.046 396 TYR AAA OH  
528   N N   . ALA A 68  ? 0.581 0.474 0.433 -0.061 -0.039 -0.002 397 ALA AAA N   
529   C CA  . ALA A 68  ? 0.571 0.480 0.438 -0.060 -0.033 0.004  397 ALA AAA CA  
530   C C   . ALA A 68  ? 0.564 0.485 0.443 -0.066 -0.040 0.010  397 ALA AAA C   
531   O O   . ALA A 68  ? 0.596 0.521 0.471 -0.067 -0.047 0.012  397 ALA AAA O   
532   C CB  . ALA A 68  ? 0.568 0.479 0.429 -0.054 -0.026 0.007  397 ALA AAA CB  
533   N N   . ASP A 69  ? 0.545 0.472 0.438 -0.069 -0.038 0.012  398 ASP AAA N   
534   C CA  . ASP A 69  ? 0.560 0.503 0.467 -0.074 -0.041 0.018  398 ASP AAA CA  
535   C C   . ASP A 69  ? 0.550 0.504 0.467 -0.067 -0.033 0.022  398 ASP AAA C   
536   O O   . ASP A 69  ? 0.549 0.499 0.465 -0.064 -0.025 0.019  398 ASP AAA O   
537   C CB  . ASP A 69  ? 0.563 0.504 0.475 -0.080 -0.043 0.019  398 ASP AAA CB  
538   C CG  . ASP A 69  ? 0.557 0.481 0.459 -0.086 -0.051 0.016  398 ASP AAA CG  
539   O OD1 . ASP A 69  ? 0.522 0.440 0.414 -0.088 -0.058 0.013  398 ASP AAA OD1 
540   O OD2 . ASP A 69  ? 0.537 0.451 0.439 -0.087 -0.051 0.015  398 ASP AAA OD2 
541   N N   . SER A 70  ? 0.541 0.509 0.466 -0.066 -0.034 0.027  399 SER AAA N   
542   C CA  . SER A 70  ? 0.529 0.503 0.461 -0.058 -0.026 0.030  399 SER AAA CA  
543   C C   . SER A 70  ? 0.535 0.531 0.483 -0.058 -0.027 0.036  399 SER AAA C   
544   O O   . SER A 70  ? 0.574 0.582 0.528 -0.063 -0.036 0.040  399 SER AAA O   
545   C CB  . SER A 70  ? 0.511 0.478 0.434 -0.052 -0.024 0.031  399 SER AAA CB  
546   O OG  . SER A 70  ? 0.498 0.470 0.417 -0.052 -0.033 0.035  399 SER AAA OG  
547   N N   . PHE A 71  ? 0.508 0.508 0.463 -0.051 -0.018 0.036  400 PHE AAA N   
548   C CA  . PHE A 71  ? 0.492 0.513 0.462 -0.048 -0.015 0.042  400 PHE AAA CA  
549   C C   . PHE A 71  ? 0.492 0.510 0.463 -0.039 -0.004 0.038  400 PHE AAA C   
550   O O   . PHE A 71  ? 0.495 0.494 0.455 -0.038 -0.001 0.032  400 PHE AAA O   
551   C CB  . PHE A 71  ? 0.483 0.516 0.460 -0.058 -0.017 0.044  400 PHE AAA CB  
552   C CG  . PHE A 71  ? 0.467 0.485 0.433 -0.063 -0.015 0.038  400 PHE AAA CG  
553   C CD1 . PHE A 71  ? 0.478 0.496 0.442 -0.058 -0.006 0.035  400 PHE AAA CD1 
554   C CD2 . PHE A 71  ? 0.484 0.489 0.441 -0.070 -0.022 0.036  400 PHE AAA CD2 
555   C CE1 . PHE A 71  ? 0.497 0.503 0.451 -0.062 -0.006 0.031  400 PHE AAA CE1 
556   C CE2 . PHE A 71  ? 0.490 0.482 0.439 -0.073 -0.020 0.033  400 PHE AAA CE2 
557   C CZ  . PHE A 71  ? 0.496 0.491 0.444 -0.068 -0.013 0.030  400 PHE AAA CZ  
558   N N   . VAL A 72  ? 0.499 0.535 0.482 -0.033 0.001  0.042  401 VAL AAA N   
559   C CA  . VAL A 72  ? 0.500 0.533 0.482 -0.023 0.012  0.038  401 VAL AAA CA  
560   C C   . VAL A 72  ? 0.497 0.544 0.483 -0.026 0.017  0.038  401 VAL AAA C   
561   O O   . VAL A 72  ? 0.503 0.573 0.501 -0.031 0.015  0.045  401 VAL AAA O   
562   C CB  . VAL A 72  ? 0.506 0.546 0.498 -0.009 0.015  0.042  401 VAL AAA CB  
563   C CG1 . VAL A 72  ? 0.527 0.565 0.519 0.002  0.027  0.037  401 VAL AAA CG1 
564   C CG2 . VAL A 72  ? 0.507 0.528 0.491 -0.006 0.011  0.044  401 VAL AAA CG2 
565   N N   . ILE A 73  ? 0.497 0.531 0.470 -0.023 0.024  0.030  402 ILE AAA N   
566   C CA  . ILE A 73  ? 0.481 0.526 0.452 -0.023 0.031  0.028  402 ILE AAA CA  
567   C C   . ILE A 73  ? 0.487 0.519 0.447 -0.013 0.040  0.018  402 ILE AAA C   
568   O O   . ILE A 73  ? 0.487 0.500 0.444 -0.007 0.040  0.014  402 ILE AAA O   
569   C CB  . ILE A 73  ? 0.461 0.501 0.422 -0.035 0.026  0.028  402 ILE AAA CB  
570   C CG1 . ILE A 73  ? 0.460 0.476 0.409 -0.038 0.021  0.020  402 ILE AAA CG1 
571   C CG2 . ILE A 73  ? 0.447 0.500 0.419 -0.045 0.019  0.037  402 ILE AAA CG2 
572   C CD1 . ILE A 73  ? 0.455 0.467 0.394 -0.047 0.017  0.019  402 ILE AAA CD1 
573   N N   . ARG A 74  ? 0.527 0.566 0.480 -0.009 0.048  0.015  403 ARG AAA N   
574   C CA  . ARG A 74  ? 0.586 0.609 0.523 -0.001 0.056  0.003  403 ARG AAA CA  
575   C C   . ARG A 74  ? 0.577 0.578 0.498 -0.009 0.049  -0.006 403 ARG AAA C   
576   O O   . ARG A 74  ? 0.545 0.550 0.465 -0.020 0.042  -0.002 403 ARG AAA O   
577   C CB  . ARG A 74  ? 0.641 0.679 0.570 0.004  0.065  0.002  403 ARG AAA CB  
578   C CG  . ARG A 74  ? 0.702 0.764 0.645 0.016  0.076  0.008  403 ARG AAA CG  
579   C CD  . ARG A 74  ? 0.746 0.830 0.683 0.015  0.085  0.011  403 ARG AAA CD  
580   N NE  . ARG A 74  ? 0.810 0.877 0.719 0.018  0.089  -0.001 403 ARG AAA NE  
581   C CZ  . ARG A 74  ? 0.876 0.956 0.771 0.017  0.096  -0.000 403 ARG AAA CZ  
582   N NH1 . ARG A 74  ? 0.857 0.966 0.765 0.012  0.101  0.014  403 ARG AAA NH1 
583   N NH2 . ARG A 74  ? 0.937 0.999 0.803 0.019  0.098  -0.013 403 ARG AAA NH2 
584   N N   . GLY A 75  ? 0.574 0.553 0.484 -0.005 0.052  -0.018 404 GLY AAA N   
585   C CA  . GLY A 75  ? 0.593 0.554 0.490 -0.013 0.046  -0.028 404 GLY AAA CA  
586   C C   . GLY A 75  ? 0.568 0.540 0.454 -0.020 0.042  -0.028 404 GLY AAA C   
587   O O   . GLY A 75  ? 0.521 0.490 0.408 -0.029 0.033  -0.027 404 GLY AAA O   
588   N N   . ASP A 76  ? 0.586 0.570 0.462 -0.014 0.049  -0.029 405 ASP AAA N   
589   C CA  . ASP A 76  ? 0.658 0.649 0.519 -0.020 0.045  -0.029 405 ASP AAA CA  
590   C C   . ASP A 76  ? 0.634 0.641 0.504 -0.027 0.042  -0.013 405 ASP AAA C   
591   O O   . ASP A 76  ? 0.646 0.658 0.504 -0.032 0.039  -0.010 405 ASP AAA O   
592   C CB  . ASP A 76  ? 0.713 0.703 0.551 -0.012 0.054  -0.038 405 ASP AAA CB  
593   C CG  . ASP A 76  ? 0.794 0.799 0.636 -0.001 0.068  -0.034 405 ASP AAA CG  
594   O OD1 . ASP A 76  ? 0.820 0.843 0.683 -0.002 0.070  -0.020 405 ASP AAA OD1 
595   O OD2 . ASP A 76  ? 0.898 0.897 0.723 0.010  0.076  -0.045 405 ASP AAA OD2 
596   N N   . GLU A 77  ? 0.587 0.601 0.477 -0.029 0.041  -0.004 406 GLU AAA N   
597   C CA  . GLU A 77  ? 0.571 0.595 0.470 -0.038 0.035  0.008  406 GLU AAA CA  
598   C C   . GLU A 77  ? 0.558 0.568 0.460 -0.044 0.024  0.007  406 GLU AAA C   
599   O O   . GLU A 77  ? 0.532 0.544 0.438 -0.051 0.018  0.015  406 GLU AAA O   
600   C CB  . GLU A 77  ? 0.585 0.627 0.503 -0.037 0.040  0.019  406 GLU AAA CB  
601   C CG  . GLU A 77  ? 0.584 0.647 0.503 -0.031 0.052  0.023  406 GLU AAA CG  
602   C CD  . GLU A 77  ? 0.585 0.670 0.527 -0.028 0.056  0.032  406 GLU AAA CD  
603   O OE1 . GLU A 77  ? 0.563 0.642 0.517 -0.027 0.050  0.032  406 GLU AAA OE1 
604   O OE2 . GLU A 77  ? 0.603 0.711 0.551 -0.027 0.065  0.040  406 GLU AAA OE2 
605   N N   . VAL A 78  ? 0.561 0.557 0.464 -0.043 0.022  -0.002 407 VAL AAA N   
606   C CA  . VAL A 78  ? 0.546 0.531 0.453 -0.048 0.014  -0.003 407 VAL AAA CA  
607   C C   . VAL A 78  ? 0.556 0.541 0.456 -0.053 0.007  -0.002 407 VAL AAA C   
608   O O   . VAL A 78  ? 0.544 0.527 0.449 -0.057 0.001  0.002  407 VAL AAA O   
609   C CB  . VAL A 78  ? 0.576 0.547 0.486 -0.046 0.015  -0.012 407 VAL AAA CB  
610   C CG1 . VAL A 78  ? 0.555 0.519 0.469 -0.052 0.008  -0.013 407 VAL AAA CG1 
611   C CG2 . VAL A 78  ? 0.563 0.532 0.480 -0.040 0.020  -0.010 407 VAL AAA CG2 
612   N N   . ARG A 79  ? 0.581 0.568 0.467 -0.052 0.007  -0.006 408 ARG AAA N   
613   C CA  . ARG A 79  ? 0.586 0.575 0.463 -0.055 -0.000 -0.004 408 ARG AAA CA  
614   C C   . ARG A 79  ? 0.556 0.548 0.435 -0.058 -0.002 0.009  408 ARG AAA C   
615   O O   . ARG A 79  ? 0.580 0.570 0.456 -0.060 -0.009 0.013  408 ARG AAA O   
616   C CB  . ARG A 79  ? 0.651 0.643 0.509 -0.052 0.001  -0.010 408 ARG AAA CB  
617   C CG  . ARG A 79  ? 0.748 0.751 0.598 -0.049 0.010  -0.003 408 ARG AAA CG  
618   C CD  . ARG A 79  ? 0.854 0.863 0.682 -0.049 0.010  0.001  408 ARG AAA CD  
619   N NE  . ARG A 79  ? 0.942 0.964 0.766 -0.047 0.021  0.011  408 ARG AAA NE  
620   C CZ  . ARG A 79  ? 0.954 0.982 0.780 -0.052 0.021  0.027  408 ARG AAA CZ  
621   N NH1 . ARG A 79  ? 0.987 1.007 0.818 -0.058 0.011  0.034  408 ARG AAA NH1 
622   N NH2 . ARG A 79  ? 0.940 0.982 0.764 -0.052 0.032  0.036  408 ARG AAA NH2 
623   N N   . GLN A 80  ? 0.534 0.533 0.421 -0.059 0.004  0.017  409 GLN AAA N   
624   C CA  . GLN A 80  ? 0.531 0.533 0.422 -0.065 0.002  0.029  409 GLN AAA CA  
625   C C   . GLN A 80  ? 0.512 0.504 0.413 -0.068 -0.005 0.030  409 GLN AAA C   
626   O O   . GLN A 80  ? 0.519 0.506 0.421 -0.073 -0.010 0.038  409 GLN AAA O   
627   C CB  . GLN A 80  ? 0.537 0.555 0.435 -0.066 0.010  0.037  409 GLN AAA CB  
628   C CG  . GLN A 80  ? 0.559 0.588 0.443 -0.063 0.018  0.039  409 GLN AAA CG  
629   C CD  . GLN A 80  ? 0.553 0.601 0.447 -0.063 0.028  0.047  409 GLN AAA CD  
630   O OE1 . GLN A 80  ? 0.517 0.571 0.424 -0.072 0.027  0.058  409 GLN AAA OE1 
631   N NE2 . GLN A 80  ? 0.559 0.617 0.447 -0.055 0.039  0.042  409 GLN AAA NE2 
632   N N   . ILE A 81  ? 0.513 0.500 0.421 -0.066 -0.006 0.022  410 ILE AAA N   
633   C CA  . ILE A 81  ? 0.530 0.507 0.444 -0.068 -0.011 0.022  410 ILE AAA CA  
634   C C   . ILE A 81  ? 0.539 0.508 0.449 -0.066 -0.017 0.018  410 ILE AAA C   
635   O O   . ILE A 81  ? 0.519 0.485 0.433 -0.063 -0.017 0.011  410 ILE AAA O   
636   C CB  . ILE A 81  ? 0.518 0.495 0.439 -0.065 -0.008 0.018  410 ILE AAA CB  
637   C CG1 . ILE A 81  ? 0.529 0.518 0.456 -0.064 -0.002 0.021  410 ILE AAA CG1 
638   C CG2 . ILE A 81  ? 0.533 0.501 0.457 -0.068 -0.014 0.019  410 ILE AAA CG2 
639   C CD1 . ILE A 81  ? 0.549 0.547 0.481 -0.070 -0.004 0.031  410 ILE AAA CD1 
640   N N   . ALA A 82  ? 0.535 0.501 0.439 -0.067 -0.021 0.024  411 ALA AAA N   
641   C CA  . ALA A 82  ? 0.578 0.539 0.478 -0.063 -0.027 0.022  411 ALA AAA CA  
642   C C   . ALA A 82  ? 0.609 0.561 0.501 -0.065 -0.032 0.033  411 ALA AAA C   
643   O O   . ALA A 82  ? 0.638 0.593 0.526 -0.069 -0.029 0.041  411 ALA AAA O   
644   C CB  . ALA A 82  ? 0.533 0.502 0.427 -0.061 -0.027 0.017  411 ALA AAA CB  
645   N N   . PRO A 83  ? 0.615 0.557 0.507 -0.061 -0.038 0.033  412 PRO AAA N   
646   C CA  . PRO A 83  ? 0.632 0.561 0.516 -0.061 -0.042 0.043  412 PRO AAA CA  
647   C C   . PRO A 83  ? 0.605 0.542 0.477 -0.061 -0.042 0.051  412 PRO AAA C   
648   O O   . PRO A 83  ? 0.611 0.560 0.481 -0.057 -0.043 0.045  412 PRO AAA O   
649   C CB  . PRO A 83  ? 0.643 0.562 0.530 -0.053 -0.048 0.040  412 PRO AAA CB  
650   C CG  . PRO A 83  ? 0.625 0.561 0.521 -0.049 -0.047 0.029  412 PRO AAA CG  
651   C CD  . PRO A 83  ? 0.594 0.535 0.494 -0.055 -0.040 0.025  412 PRO AAA CD  
652   N N   . GLY A 84  ? 0.614 0.544 0.479 -0.067 -0.041 0.063  413 GLY AAA N   
653   C CA  . GLY A 84  ? 0.614 0.548 0.463 -0.066 -0.041 0.073  413 GLY AAA CA  
654   C C   . GLY A 84  ? 0.620 0.573 0.464 -0.070 -0.033 0.072  413 GLY AAA C   
655   O O   . GLY A 84  ? 0.635 0.594 0.464 -0.068 -0.032 0.078  413 GLY AAA O   
656   N N   . GLN A 85  ? 0.631 0.592 0.487 -0.073 -0.026 0.066  414 GLN AAA N   
657   C CA  . GLN A 85  ? 0.605 0.584 0.458 -0.074 -0.016 0.064  414 GLN AAA CA  
658   C C   . GLN A 85  ? 0.603 0.589 0.459 -0.082 -0.009 0.077  414 GLN AAA C   
659   O O   . GLN A 85  ? 0.622 0.598 0.488 -0.089 -0.012 0.083  414 GLN AAA O   
660   C CB  . GLN A 85  ? 0.581 0.567 0.447 -0.071 -0.013 0.051  414 GLN AAA CB  
661   C CG  . GLN A 85  ? 0.576 0.559 0.441 -0.065 -0.018 0.038  414 GLN AAA CG  
662   C CD  . GLN A 85  ? 0.614 0.604 0.461 -0.061 -0.019 0.034  414 GLN AAA CD  
663   O OE1 . GLN A 85  ? 0.620 0.619 0.455 -0.061 -0.012 0.037  414 GLN AAA OE1 
664   N NE2 . GLN A 85  ? 0.630 0.618 0.476 -0.058 -0.027 0.028  414 GLN AAA NE2 
665   N N   . THR A 86  ? 0.596 0.598 0.443 -0.081 0.000  0.079  415 THR AAA N   
666   C CA  . THR A 86  ? 0.618 0.634 0.472 -0.088 0.011  0.090  415 THR AAA CA  
667   C C   . THR A 86  ? 0.631 0.667 0.490 -0.082 0.021  0.082  415 THR AAA C   
668   O O   . THR A 86  ? 0.648 0.682 0.500 -0.073 0.020  0.068  415 THR AAA O   
669   C CB  . THR A 86  ? 0.654 0.672 0.491 -0.091 0.015  0.106  415 THR AAA CB  
670   O OG1 . THR A 86  ? 0.660 0.682 0.474 -0.082 0.016  0.100  415 THR AAA OG1 
671   C CG2 . THR A 86  ? 0.663 0.659 0.497 -0.097 0.005  0.117  415 THR AAA CG2 
672   N N   . GLY A 87  ? 0.628 0.683 0.501 -0.086 0.031  0.090  416 GLY AAA N   
673   C CA  . GLY A 87  ? 0.614 0.689 0.497 -0.080 0.042  0.084  416 GLY AAA CA  
674   C C   . GLY A 87  ? 0.608 0.696 0.519 -0.087 0.042  0.090  416 GLY AAA C   
675   O O   . GLY A 87  ? 0.646 0.722 0.565 -0.097 0.033  0.096  416 GLY AAA O   
676   N N   . LYS A 88  ? 0.610 0.721 0.535 -0.081 0.052  0.088  417 LYS AAA N   
677   C CA  . LYS A 88  ? 0.595 0.724 0.549 -0.087 0.052  0.094  417 LYS AAA CA  
678   C C   . LYS A 88  ? 0.556 0.666 0.517 -0.091 0.037  0.089  417 LYS AAA C   
679   O O   . LYS A 88  ? 0.528 0.641 0.505 -0.103 0.031  0.097  417 LYS AAA O   
680   C CB  . LYS A 88  ? 0.630 0.782 0.596 -0.074 0.063  0.089  417 LYS AAA CB  
681   C CG  . LYS A 88  ? 0.691 0.866 0.651 -0.067 0.081  0.094  417 LYS AAA CG  
682   C CD  . LYS A 88  ? 0.785 0.981 0.755 -0.080 0.086  0.112  417 LYS AAA CD  
683   C CE  . LYS A 88  ? 0.820 1.038 0.779 -0.072 0.106  0.116  417 LYS AAA CE  
684   N NZ  . LYS A 88  ? 0.858 1.085 0.815 -0.087 0.110  0.134  417 LYS AAA NZ  
685   N N   . ILE A 89  ? 0.535 0.626 0.486 -0.082 0.032  0.075  418 ILE AAA N   
686   C CA  . ILE A 89  ? 0.532 0.607 0.489 -0.084 0.021  0.069  418 ILE AAA CA  
687   C C   . ILE A 89  ? 0.525 0.579 0.475 -0.094 0.010  0.072  418 ILE AAA C   
688   O O   . ILE A 89  ? 0.559 0.611 0.520 -0.103 0.003  0.076  418 ILE AAA O   
689   C CB  . ILE A 89  ? 0.516 0.580 0.466 -0.072 0.021  0.056  418 ILE AAA CB  
690   C CG1 . ILE A 89  ? 0.535 0.615 0.490 -0.061 0.032  0.053  418 ILE AAA CG1 
691   C CG2 . ILE A 89  ? 0.491 0.543 0.447 -0.074 0.011  0.052  418 ILE AAA CG2 
692   C CD1 . ILE A 89  ? 0.537 0.642 0.516 -0.061 0.035  0.060  418 ILE AAA CD1 
693   N N   . ALA A 90  ? 0.531 0.570 0.463 -0.092 0.009  0.071  419 ALA AAA N   
694   C CA  . ALA A 90  ? 0.535 0.553 0.459 -0.098 -0.000 0.074  419 ALA AAA CA  
695   C C   . ALA A 90  ? 0.560 0.580 0.492 -0.112 -0.001 0.088  419 ALA AAA C   
696   O O   . ALA A 90  ? 0.593 0.594 0.526 -0.119 -0.011 0.089  419 ALA AAA O   
697   C CB  . ALA A 90  ? 0.547 0.554 0.451 -0.093 -0.000 0.072  419 ALA AAA CB  
698   N N   . ASP A 91  ? 0.561 0.602 0.497 -0.115 0.008  0.098  420 ASP AAA N   
699   C CA  . ASP A 91  ? 0.590 0.634 0.533 -0.130 0.009  0.113  420 ASP AAA CA  
700   C C   . ASP A 91  ? 0.577 0.634 0.544 -0.140 0.005  0.116  420 ASP AAA C   
701   O O   . ASP A 91  ? 0.581 0.625 0.554 -0.155 -0.002 0.123  420 ASP AAA O   
702   C CB  . ASP A 91  ? 0.622 0.686 0.559 -0.130 0.022  0.124  420 ASP AAA CB  
703   C CG  . ASP A 91  ? 0.665 0.715 0.574 -0.122 0.024  0.124  420 ASP AAA CG  
704   O OD1 . ASP A 91  ? 0.683 0.707 0.580 -0.118 0.014  0.118  420 ASP AAA OD1 
705   O OD2 . ASP A 91  ? 0.663 0.730 0.562 -0.118 0.036  0.130  420 ASP AAA OD2 
706   N N   . TYR A 92  ? 0.545 0.627 0.528 -0.134 0.010  0.111  421 TYR AAA N   
707   C CA  . TYR A 92  ? 0.561 0.667 0.571 -0.143 0.008  0.117  421 TYR AAA CA  
708   C C   . TYR A 92  ? 0.541 0.646 0.559 -0.138 -0.001 0.106  421 TYR AAA C   
709   O O   . TYR A 92  ? 0.519 0.641 0.558 -0.147 -0.006 0.110  421 TYR AAA O   
710   C CB  . TYR A 92  ? 0.580 0.723 0.603 -0.139 0.024  0.124  421 TYR AAA CB  
711   C CG  . TYR A 92  ? 0.600 0.753 0.618 -0.146 0.035  0.138  421 TYR AAA CG  
712   C CD1 . TYR A 92  ? 0.609 0.738 0.616 -0.160 0.029  0.147  421 TYR AAA CD1 
713   C CD2 . TYR A 92  ? 0.626 0.808 0.646 -0.137 0.051  0.142  421 TYR AAA CD2 
714   C CE1 . TYR A 92  ? 0.628 0.765 0.629 -0.166 0.040  0.161  421 TYR AAA CE1 
715   C CE2 . TYR A 92  ? 0.639 0.831 0.652 -0.143 0.063  0.155  421 TYR AAA CE2 
716   C CZ  . TYR A 92  ? 0.647 0.816 0.650 -0.158 0.057  0.166  421 TYR AAA CZ  
717   O OH  . TYR A 92  ? 0.664 0.842 0.658 -0.164 0.069  0.182  421 TYR AAA OH  
718   N N   . ASN A 93  ? 0.533 0.618 0.536 -0.126 -0.004 0.093  422 ASN AAA N   
719   C CA  . ASN A 93  ? 0.500 0.586 0.509 -0.119 -0.010 0.085  422 ASN AAA CA  
720   C C   . ASN A 93  ? 0.517 0.571 0.510 -0.119 -0.020 0.075  422 ASN AAA C   
721   O O   . ASN A 93  ? 0.519 0.568 0.516 -0.125 -0.031 0.074  422 ASN AAA O   
722   C CB  . ASN A 93  ? 0.476 0.574 0.484 -0.103 0.000  0.079  422 ASN AAA CB  
723   C CG  . ASN A 93  ? 0.469 0.602 0.496 -0.100 0.011  0.087  422 ASN AAA CG  
724   O OD1 . ASN A 93  ? 0.472 0.625 0.518 -0.098 0.009  0.089  422 ASN AAA OD1 
725   N ND2 . ASN A 93  ? 0.502 0.644 0.524 -0.100 0.022  0.092  422 ASN AAA ND2 
726   N N   . TYR A 94  ? 0.533 0.567 0.507 -0.112 -0.018 0.070  423 TYR AAA N   
727   C CA  . TYR A 94  ? 0.557 0.564 0.518 -0.109 -0.026 0.061  423 TYR AAA CA  
728   C C   . TYR A 94  ? 0.555 0.545 0.501 -0.107 -0.025 0.060  423 TYR AAA C   
729   O O   . TYR A 94  ? 0.540 0.535 0.480 -0.099 -0.018 0.059  423 TYR AAA O   
730   C CB  . TYR A 94  ? 0.530 0.537 0.489 -0.098 -0.024 0.052  423 TYR AAA CB  
731   C CG  . TYR A 94  ? 0.521 0.505 0.468 -0.095 -0.030 0.044  423 TYR AAA CG  
732   C CD1 . TYR A 94  ? 0.523 0.500 0.470 -0.099 -0.038 0.041  423 TYR AAA CD1 
733   C CD2 . TYR A 94  ? 0.536 0.507 0.473 -0.089 -0.028 0.038  423 TYR AAA CD2 
734   C CE1 . TYR A 94  ? 0.522 0.479 0.456 -0.096 -0.042 0.034  423 TYR AAA CE1 
735   C CE2 . TYR A 94  ? 0.547 0.500 0.474 -0.086 -0.032 0.031  423 TYR AAA CE2 
736   C CZ  . TYR A 94  ? 0.537 0.483 0.463 -0.089 -0.038 0.029  423 TYR AAA CZ  
737   O OH  . TYR A 94  ? 0.520 0.449 0.435 -0.084 -0.040 0.022  423 TYR AAA OH  
738   N N   . LYS A 95  ? 0.561 0.529 0.500 -0.114 -0.032 0.062  424 LYS AAA N   
739   C CA  . LYS A 95  ? 0.568 0.519 0.494 -0.112 -0.033 0.065  424 LYS AAA CA  
740   C C   . LYS A 95  ? 0.563 0.491 0.480 -0.105 -0.039 0.055  424 LYS AAA C   
741   O O   . LYS A 95  ? 0.564 0.478 0.480 -0.109 -0.046 0.052  424 LYS AAA O   
742   C CB  . LYS A 95  ? 0.596 0.538 0.522 -0.124 -0.035 0.076  424 LYS AAA CB  
743   C CG  . LYS A 95  ? 0.607 0.529 0.519 -0.122 -0.037 0.082  424 LYS AAA CG  
744   C CD  . LYS A 95  ? 0.581 0.516 0.485 -0.112 -0.030 0.082  424 LYS AAA CD  
745   C CE  . LYS A 95  ? 0.596 0.519 0.486 -0.112 -0.031 0.093  424 LYS AAA CE  
746   N NZ  . LYS A 95  ? 0.600 0.533 0.480 -0.100 -0.028 0.089  424 LYS AAA NZ  
747   N N   . LEU A 96  ? 0.554 0.481 0.464 -0.095 -0.037 0.051  425 LEU AAA N   
748   C CA  . LEU A 96  ? 0.569 0.478 0.472 -0.088 -0.041 0.044  425 LEU AAA CA  
749   C C   . LEU A 96  ? 0.605 0.495 0.500 -0.088 -0.045 0.051  425 LEU AAA C   
750   O O   . LEU A 96  ? 0.630 0.525 0.521 -0.090 -0.043 0.060  425 LEU AAA O   
751   C CB  . LEU A 96  ? 0.559 0.478 0.463 -0.078 -0.037 0.036  425 LEU AAA CB  
752   C CG  . LEU A 96  ? 0.556 0.484 0.465 -0.076 -0.033 0.029  425 LEU AAA CG  
753   C CD1 . LEU A 96  ? 0.541 0.476 0.451 -0.069 -0.030 0.022  425 LEU AAA CD1 
754   C CD2 . LEU A 96  ? 0.570 0.486 0.478 -0.077 -0.037 0.025  425 LEU AAA CD2 
755   N N   . PRO A 97  ? 0.606 0.473 0.496 -0.084 -0.051 0.047  426 PRO AAA N   
756   C CA  . PRO A 97  ? 0.631 0.477 0.512 -0.081 -0.055 0.053  426 PRO AAA CA  
757   C C   . PRO A 97  ? 0.608 0.463 0.486 -0.069 -0.054 0.054  426 PRO AAA C   
758   O O   . PRO A 97  ? 0.573 0.446 0.457 -0.063 -0.051 0.046  426 PRO AAA O   
759   C CB  . PRO A 97  ? 0.652 0.473 0.528 -0.077 -0.060 0.045  426 PRO AAA CB  
760   C CG  . PRO A 97  ? 0.618 0.453 0.499 -0.072 -0.056 0.033  426 PRO AAA CG  
761   C CD  . PRO A 97  ? 0.612 0.471 0.501 -0.081 -0.052 0.036  426 PRO AAA CD  
762   N N   . ASP A 98  ? 0.650 0.493 0.520 -0.067 -0.058 0.063  427 ASP AAA N   
763   C CA  . ASP A 98  ? 0.674 0.527 0.542 -0.056 -0.060 0.065  427 ASP AAA CA  
764   C C   . ASP A 98  ? 0.637 0.489 0.510 -0.042 -0.062 0.055  427 ASP AAA C   
765   O O   . ASP A 98  ? 0.603 0.475 0.480 -0.036 -0.063 0.052  427 ASP AAA O   
766   C CB  . ASP A 98  ? 0.703 0.539 0.559 -0.055 -0.064 0.080  427 ASP AAA CB  
767   C CG  . ASP A 98  ? 0.782 0.616 0.631 -0.069 -0.061 0.092  427 ASP AAA CG  
768   O OD1 . ASP A 98  ? 0.779 0.633 0.635 -0.077 -0.055 0.090  427 ASP AAA OD1 
769   O OD2 . ASP A 98  ? 0.902 0.715 0.741 -0.071 -0.064 0.106  427 ASP AAA OD2 
770   N N   . ASP A 99  ? 0.652 0.485 0.526 -0.039 -0.063 0.049  428 ASP AAA N   
771   C CA  . ASP A 99  ? 0.624 0.455 0.503 -0.025 -0.063 0.040  428 ASP AAA CA  
772   C C   . ASP A 99  ? 0.595 0.437 0.481 -0.028 -0.058 0.028  428 ASP AAA C   
773   O O   . ASP A 99  ? 0.559 0.392 0.445 -0.019 -0.056 0.021  428 ASP AAA O   
774   C CB  . ASP A 99  ? 0.659 0.457 0.530 -0.017 -0.068 0.042  428 ASP AAA CB  
775   C CG  . ASP A 99  ? 0.704 0.476 0.568 -0.027 -0.068 0.038  428 ASP AAA CG  
776   O OD1 . ASP A 99  ? 0.689 0.470 0.554 -0.041 -0.066 0.038  428 ASP AAA OD1 
777   O OD2 . ASP A 99  ? 0.784 0.526 0.640 -0.019 -0.070 0.034  428 ASP AAA OD2 
778   N N   . PHE A 100 ? 0.575 0.434 0.464 -0.038 -0.054 0.028  429 PHE AAA N   
779   C CA  . PHE A 100 ? 0.568 0.435 0.462 -0.041 -0.049 0.019  429 PHE AAA CA  
780   C C   . PHE A 100 ? 0.574 0.449 0.475 -0.030 -0.045 0.011  429 PHE AAA C   
781   O O   . PHE A 100 ? 0.547 0.438 0.456 -0.024 -0.045 0.011  429 PHE AAA O   
782   C CB  . PHE A 100 ? 0.546 0.434 0.445 -0.049 -0.045 0.020  429 PHE AAA CB  
783   C CG  . PHE A 100 ? 0.532 0.428 0.435 -0.051 -0.040 0.013  429 PHE AAA CG  
784   C CD1 . PHE A 100 ? 0.545 0.427 0.442 -0.055 -0.040 0.011  429 PHE AAA CD1 
785   C CD2 . PHE A 100 ? 0.517 0.430 0.427 -0.050 -0.035 0.010  429 PHE AAA CD2 
786   C CE1 . PHE A 100 ? 0.534 0.425 0.433 -0.056 -0.036 0.006  429 PHE AAA CE1 
787   C CE2 . PHE A 100 ? 0.512 0.430 0.425 -0.052 -0.030 0.005  429 PHE AAA CE2 
788   C CZ  . PHE A 100 ? 0.538 0.445 0.444 -0.054 -0.031 0.004  429 PHE AAA CZ  
789   N N   . THR A 101 ? 0.609 0.474 0.505 -0.028 -0.042 0.004  430 THR AAA N   
790   C CA  . THR A 101 ? 0.608 0.484 0.511 -0.020 -0.035 -0.004 430 THR AAA CA  
791   C C   . THR A 101 ? 0.602 0.487 0.505 -0.027 -0.030 -0.007 430 THR AAA C   
792   O O   . THR A 101 ? 0.628 0.499 0.519 -0.031 -0.031 -0.009 430 THR AAA O   
793   C CB  . THR A 101 ? 0.630 0.487 0.525 -0.008 -0.035 -0.009 430 THR AAA CB  
794   O OG1 . THR A 101 ? 0.670 0.518 0.566 -0.001 -0.040 -0.004 430 THR AAA OG1 
795   C CG2 . THR A 101 ? 0.631 0.504 0.535 0.001  -0.026 -0.015 430 THR AAA CG2 
796   N N   . GLY A 102 ? 0.572 0.478 0.486 -0.029 -0.025 -0.007 431 GLY AAA N   
797   C CA  . GLY A 102 ? 0.586 0.499 0.500 -0.035 -0.020 -0.009 431 GLY AAA CA  
798   C C   . GLY A 102 ? 0.546 0.476 0.471 -0.039 -0.017 -0.007 431 GLY AAA C   
799   O O   . GLY A 102 ? 0.537 0.479 0.472 -0.037 -0.019 -0.007 431 GLY AAA O   
800   N N   . CYS A 103 ? 0.526 0.460 0.451 -0.044 -0.013 -0.007 432 CYS AAA N   
801   C CA  . CYS A 103 ? 0.535 0.480 0.468 -0.049 -0.010 -0.007 432 CYS AAA CA  
802   C C   . CYS A 103 ? 0.519 0.461 0.447 -0.054 -0.011 -0.004 432 CYS AAA C   
803   O O   . CYS A 103 ? 0.520 0.455 0.441 -0.054 -0.012 -0.002 432 CYS AAA O   
804   C CB  . CYS A 103 ? 0.538 0.489 0.478 -0.048 -0.002 -0.009 432 CYS AAA CB  
805   S SG  . CYS A 103 ? 0.533 0.492 0.481 -0.041 0.001  -0.012 432 CYS AAA SG  
806   N N   . VAL A 104 ? 0.506 0.455 0.439 -0.056 -0.010 -0.005 433 VAL AAA N   
807   C CA  . VAL A 104 ? 0.478 0.428 0.409 -0.059 -0.009 -0.003 433 VAL AAA CA  
808   C C   . VAL A 104 ? 0.462 0.413 0.398 -0.060 -0.004 -0.006 433 VAL AAA C   
809   O O   . VAL A 104 ? 0.438 0.394 0.379 -0.062 -0.004 -0.011 433 VAL AAA O   
810   C CB  . VAL A 104 ? 0.482 0.436 0.410 -0.060 -0.013 -0.001 433 VAL AAA CB  
811   C CG1 . VAL A 104 ? 0.482 0.439 0.409 -0.061 -0.010 0.001  433 VAL AAA CG1 
812   C CG2 . VAL A 104 ? 0.486 0.435 0.409 -0.060 -0.018 0.004  433 VAL AAA CG2 
813   N N   . ILE A 105 ? 0.481 0.427 0.415 -0.059 0.000  -0.004 434 ILE AAA N   
814   C CA  . ILE A 105 ? 0.482 0.422 0.418 -0.060 0.006  -0.005 434 ILE AAA CA  
815   C C   . ILE A 105 ? 0.491 0.430 0.425 -0.057 0.008  -0.003 434 ILE AAA C   
816   O O   . ILE A 105 ? 0.519 0.461 0.451 -0.055 0.005  0.002  434 ILE AAA O   
817   C CB  . ILE A 105 ? 0.494 0.430 0.431 -0.060 0.011  -0.003 434 ILE AAA CB  
818   C CG1 . ILE A 105 ? 0.528 0.469 0.470 -0.061 0.011  -0.005 434 ILE AAA CG1 
819   C CG2 . ILE A 105 ? 0.520 0.447 0.460 -0.062 0.017  -0.003 434 ILE AAA CG2 
820   C CD1 . ILE A 105 ? 0.518 0.457 0.457 -0.060 0.017  -0.002 434 ILE AAA CD1 
821   N N   . ALA A 106 ? 0.502 0.437 0.437 -0.057 0.011  -0.007 435 ALA AAA N   
822   C CA  . ALA A 106 ? 0.505 0.437 0.438 -0.051 0.014  -0.006 435 ALA AAA CA  
823   C C   . ALA A 106 ? 0.559 0.476 0.492 -0.051 0.019  -0.010 435 ALA AAA C   
824   O O   . ALA A 106 ? 0.581 0.493 0.517 -0.057 0.020  -0.016 435 ALA AAA O   
825   C CB  . ALA A 106 ? 0.481 0.423 0.411 -0.050 0.013  -0.008 435 ALA AAA CB  
826   N N   . TRP A 107 ? 0.552 0.463 0.484 -0.044 0.023  -0.007 436 TRP AAA N   
827   C CA  . TRP A 107 ? 0.559 0.450 0.489 -0.041 0.029  -0.011 436 TRP AAA CA  
828   C C   . TRP A 107 ? 0.589 0.479 0.518 -0.030 0.033  -0.010 436 TRP AAA C   
829   O O   . TRP A 107 ? 0.622 0.528 0.555 -0.024 0.031  -0.002 436 TRP AAA O   
830   C CB  . TRP A 107 ? 0.541 0.419 0.472 -0.043 0.031  -0.004 436 TRP AAA CB  
831   C CG  . TRP A 107 ? 0.510 0.392 0.441 -0.036 0.031  0.007  436 TRP AAA CG  
832   C CD1 . TRP A 107 ? 0.521 0.394 0.450 -0.026 0.034  0.013  436 TRP AAA CD1 
833   C CD2 . TRP A 107 ? 0.502 0.399 0.432 -0.037 0.026  0.013  436 TRP AAA CD2 
834   N NE1 . TRP A 107 ? 0.528 0.411 0.456 -0.022 0.030  0.023  436 TRP AAA NE1 
835   C CE2 . TRP A 107 ? 0.499 0.395 0.426 -0.029 0.025  0.022  436 TRP AAA CE2 
836   C CE3 . TRP A 107 ? 0.494 0.402 0.424 -0.044 0.022  0.011  436 TRP AAA CE3 
837   C CZ2 . TRP A 107 ? 0.507 0.414 0.431 -0.029 0.019  0.028  436 TRP AAA CZ2 
838   C CZ3 . TRP A 107 ? 0.493 0.409 0.420 -0.043 0.017  0.016  436 TRP AAA CZ3 
839   C CH2 . TRP A 107 ? 0.494 0.409 0.417 -0.037 0.016  0.025  436 TRP AAA CH2 
840   N N   . ASN A 108 ? 0.587 0.461 0.512 -0.027 0.037  -0.018 437 ASN AAA N   
841   C CA  . ASN A 108 ? 0.598 0.466 0.520 -0.013 0.043  -0.018 437 ASN AAA CA  
842   C C   . ASN A 108 ? 0.590 0.454 0.518 -0.005 0.044  -0.006 437 ASN AAA C   
843   O O   . ASN A 108 ? 0.591 0.437 0.518 -0.009 0.045  -0.003 437 ASN AAA O   
844   C CB  . ASN A 108 ? 0.611 0.453 0.524 -0.013 0.047  -0.031 437 ASN AAA CB  
845   C CG  . ASN A 108 ? 0.632 0.470 0.542 0.003  0.054  -0.034 437 ASN AAA CG  
846   O OD1 . ASN A 108 ? 0.646 0.477 0.561 0.014  0.057  -0.026 437 ASN AAA OD1 
847   N ND2 . ASN A 108 ? 0.633 0.477 0.534 0.006  0.056  -0.044 437 ASN AAA ND2 
848   N N   . SER A 109 ? 0.563 0.444 0.496 0.006  0.045  0.001  438 SER AAA N   
849   C CA  . SER A 109 ? 0.554 0.436 0.494 0.016  0.044  0.013  438 SER AAA CA  
850   C C   . SER A 109 ? 0.594 0.474 0.537 0.034  0.051  0.013  438 SER AAA C   
851   O O   . SER A 109 ? 0.615 0.508 0.566 0.045  0.049  0.024  438 SER AAA O   
852   C CB  . SER A 109 ? 0.547 0.457 0.494 0.013  0.037  0.022  438 SER AAA CB  
853   O OG  . SER A 109 ? 0.541 0.477 0.495 0.014  0.037  0.021  438 SER AAA OG  
854   N N   . ASN A 110 ? 0.618 0.482 0.554 0.037  0.057  0.001  439 ASN AAA N   
855   C CA  . ASN A 110 ? 0.631 0.489 0.568 0.056  0.065  -0.002 439 ASN AAA CA  
856   C C   . ASN A 110 ? 0.653 0.494 0.593 0.068  0.066  0.009  439 ASN AAA C   
857   O O   . ASN A 110 ? 0.649 0.506 0.600 0.085  0.068  0.016  439 ASN AAA O   
858   C CB  . ASN A 110 ? 0.658 0.490 0.580 0.056  0.072  -0.018 439 ASN AAA CB  
859   C CG  . ASN A 110 ? 0.664 0.500 0.586 0.076  0.081  -0.024 439 ASN AAA CG  
860   O OD1 . ASN A 110 ? 0.660 0.531 0.595 0.085  0.083  -0.016 439 ASN AAA OD1 
861   N ND2 . ASN A 110 ? 0.703 0.505 0.611 0.082  0.087  -0.037 439 ASN AAA ND2 
862   N N   . ASN A 111 ? 0.668 0.480 0.601 0.060  0.064  0.012  440 ASN AAA N   
863   C CA  . ASN A 111 ? 0.693 0.483 0.626 0.073  0.065  0.023  440 ASN AAA CA  
864   C C   . ASN A 111 ? 0.695 0.514 0.638 0.080  0.059  0.040  440 ASN AAA C   
865   O O   . ASN A 111 ? 0.752 0.564 0.698 0.097  0.059  0.050  440 ASN AAA O   
866   C CB  . ASN A 111 ? 0.707 0.461 0.629 0.060  0.066  0.024  440 ASN AAA CB  
867   C CG  . ASN A 111 ? 0.745 0.472 0.664 0.073  0.068  0.037  440 ASN AAA CG  
868   O OD1 . ASN A 111 ? 0.763 0.499 0.683 0.075  0.063  0.053  440 ASN AAA OD1 
869   N ND2 . ASN A 111 ? 0.775 0.467 0.688 0.084  0.075  0.031  440 ASN AAA ND2 
870   N N   . LEU A 112 ? 0.678 0.529 0.626 0.068  0.051  0.042  441 LEU AAA N   
871   C CA  . LEU A 112 ? 0.663 0.541 0.620 0.072  0.042  0.057  441 LEU AAA CA  
872   C C   . LEU A 112 ? 0.636 0.554 0.609 0.079  0.041  0.058  441 LEU AAA C   
873   O O   . LEU A 112 ? 0.627 0.564 0.611 0.089  0.035  0.069  441 LEU AAA O   
874   C CB  . LEU A 112 ? 0.655 0.538 0.604 0.054  0.035  0.059  441 LEU AAA CB  
875   C CG  . LEU A 112 ? 0.665 0.517 0.600 0.047  0.037  0.062  441 LEU AAA CG  
876   C CD1 . LEU A 112 ? 0.630 0.492 0.559 0.033  0.031  0.064  441 LEU AAA CD1 
877   C CD2 . LEU A 112 ? 0.695 0.530 0.626 0.061  0.037  0.075  441 LEU AAA CD2 
878   N N   . ASP A 113 ? 0.633 0.563 0.609 0.072  0.044  0.047  442 ASP AAA N   
879   C CA  . ASP A 113 ? 0.633 0.605 0.625 0.071  0.042  0.049  442 ASP AAA CA  
880   C C   . ASP A 113 ? 0.680 0.662 0.681 0.086  0.053  0.045  442 ASP AAA C   
881   O O   . ASP A 113 ? 0.666 0.683 0.681 0.085  0.053  0.047  442 ASP AAA O   
882   C CB  . ASP A 113 ? 0.608 0.588 0.595 0.051  0.038  0.043  442 ASP AAA CB  
883   C CG  . ASP A 113 ? 0.600 0.580 0.583 0.039  0.027  0.049  442 ASP AAA CG  
884   O OD1 . ASP A 113 ? 0.591 0.583 0.580 0.043  0.020  0.059  442 ASP AAA OD1 
885   O OD2 . ASP A 113 ? 0.579 0.549 0.551 0.025  0.026  0.042  442 ASP AAA OD2 
886   N N   . SER A 114 ? 0.729 0.683 0.721 0.099  0.062  0.038  443 SER AAA N   
887   C CA  . SER A 114 ? 0.803 0.766 0.802 0.116  0.073  0.033  443 SER AAA CA  
888   C C   . SER A 114 ? 0.844 0.799 0.851 0.140  0.076  0.041  443 SER AAA C   
889   O O   . SER A 114 ? 0.852 0.779 0.851 0.141  0.072  0.046  443 SER AAA O   
890   C CB  . SER A 114 ? 0.844 0.780 0.823 0.112  0.082  0.016  443 SER AAA CB  
891   O OG  . SER A 114 ? 0.929 0.821 0.894 0.121  0.086  0.010  443 SER AAA OG  
892   N N   . LYS A 115 ? 0.872 0.855 0.896 0.159  0.083  0.044  444 LYS AAA N   
893   C CA  . LYS A 115 ? 0.907 0.887 0.942 0.185  0.086  0.052  444 LYS AAA CA  
894   C C   . LYS A 115 ? 0.912 0.888 0.947 0.206  0.102  0.042  444 LYS AAA C   
895   O O   . LYS A 115 ? 0.870 0.865 0.904 0.200  0.110  0.033  444 LYS AAA O   
896   C CB  . LYS A 115 ? 0.944 0.974 1.008 0.190  0.077  0.069  444 LYS AAA CB  
897   C CG  . LYS A 115 ? 1.005 1.027 1.066 0.184  0.062  0.082  444 LYS AAA CG  
898   C CD  . LYS A 115 ? 1.045 1.116 1.127 0.174  0.048  0.094  444 LYS AAA CD  
899   C CE  . LYS A 115 ? 1.088 1.145 1.154 0.155  0.034  0.099  444 LYS AAA CE  
900   N NZ  . LYS A 115 ? 1.106 1.202 1.185 0.137  0.023  0.102  444 LYS AAA NZ  
901   N N   . VAL A 116 ? 0.943 0.897 0.979 0.231  0.108  0.044  445 VAL AAA N   
902   C CA  . VAL A 116 ? 0.971 0.917 1.006 0.256  0.124  0.034  445 VAL AAA CA  
903   C C   . VAL A 116 ? 0.954 0.959 1.014 0.265  0.132  0.037  445 VAL AAA C   
904   O O   . VAL A 116 ? 0.989 0.991 1.039 0.271  0.146  0.022  445 VAL AAA O   
905   C CB  . VAL A 116 ? 1.024 0.936 1.059 0.283  0.127  0.039  445 VAL AAA CB  
906   C CG1 . VAL A 116 ? 1.060 0.906 1.066 0.272  0.124  0.032  445 VAL AAA CG1 
907   C CG2 . VAL A 116 ? 1.014 0.960 1.075 0.295  0.117  0.061  445 VAL AAA CG2 
908   N N   . GLY A 117 ? 0.900 0.957 0.990 0.264  0.124  0.054  446 GLY AAA N   
909   C CA  . GLY A 117 ? 0.874 0.992 0.992 0.269  0.131  0.058  446 GLY AAA CA  
910   C C   . GLY A 117 ? 0.815 0.953 0.927 0.241  0.131  0.053  446 GLY AAA C   
911   O O   . GLY A 117 ? 0.772 0.959 0.905 0.241  0.138  0.058  446 GLY AAA O   
912   N N   . GLY A 118 ? 0.791 0.895 0.878 0.217  0.122  0.046  447 GLY AAA N   
913   C CA  . GLY A 118 ? 0.741 0.863 0.825 0.189  0.115  0.046  447 GLY AAA CA  
914   C C   . GLY A 118 ? 0.707 0.852 0.809 0.174  0.097  0.061  447 GLY AAA C   
915   O O   . GLY A 118 ? 0.700 0.880 0.829 0.185  0.093  0.074  447 GLY AAA O   
916   N N   . ASN A 119 ? 0.684 0.810 0.769 0.150  0.087  0.059  448 ASN AAA N   
917   C CA  . ASN A 119 ? 0.653 0.799 0.749 0.133  0.070  0.070  448 ASN AAA CA  
918   C C   . ASN A 119 ? 0.645 0.829 0.754 0.115  0.069  0.072  448 ASN AAA C   
919   O O   . ASN A 119 ? 0.650 0.819 0.741 0.101  0.073  0.064  448 ASN AAA O   
920   C CB  . ASN A 119 ? 0.653 0.758 0.725 0.119  0.060  0.066  448 ASN AAA CB  
921   C CG  . ASN A 119 ? 0.639 0.762 0.718 0.102  0.043  0.076  448 ASN AAA CG  
922   O OD1 . ASN A 119 ? 0.630 0.792 0.733 0.102  0.037  0.086  448 ASN AAA OD1 
923   N ND2 . ASN A 119 ? 0.666 0.758 0.724 0.088  0.036  0.072  448 ASN AAA ND2 
924   N N   . TYR A 120 ? 0.633 0.864 0.773 0.116  0.065  0.085  449 TYR AAA N   
925   C CA  . TYR A 120 ? 0.618 0.888 0.775 0.099  0.065  0.090  449 TYR AAA CA  
926   C C   . TYR A 120 ? 0.586 0.864 0.748 0.077  0.046  0.097  449 TYR AAA C   
927   O O   . TYR A 120 ? 0.607 0.916 0.786 0.061  0.043  0.102  449 TYR AAA O   
928   C CB  . TYR A 120 ? 0.638 0.957 0.827 0.115  0.076  0.098  449 TYR AAA CB  
929   C CG  . TYR A 120 ? 0.686 0.995 0.865 0.136  0.097  0.088  449 TYR AAA CG  
930   C CD1 . TYR A 120 ? 0.713 1.020 0.877 0.128  0.110  0.081  449 TYR AAA CD1 
931   C CD2 . TYR A 120 ? 0.730 1.028 0.911 0.164  0.104  0.087  449 TYR AAA CD2 
932   C CE1 . TYR A 120 ? 0.742 1.037 0.891 0.147  0.129  0.070  449 TYR AAA CE1 
933   C CE2 . TYR A 120 ? 0.764 1.048 0.933 0.183  0.123  0.076  449 TYR AAA CE2 
934   C CZ  . TYR A 120 ? 0.782 1.065 0.934 0.174  0.136  0.067  449 TYR AAA CZ  
935   O OH  . TYR A 120 ? 0.836 1.104 0.971 0.193  0.154  0.055  449 TYR AAA OH  
936   N N   . ASN A 121 ? 0.583 0.831 0.728 0.075  0.033  0.095  450 ASN AAA N   
937   C CA  . ASN A 121 ? 0.615 0.867 0.762 0.056  0.014  0.100  450 ASN AAA CA  
938   C C   . ASN A 121 ? 0.593 0.829 0.722 0.033  0.012  0.094  450 ASN AAA C   
939   O O   . ASN A 121 ? 0.571 0.820 0.707 0.016  -0.000 0.098  450 ASN AAA O   
940   C CB  . ASN A 121 ? 0.653 0.878 0.784 0.062  0.004  0.102  450 ASN AAA CB  
941   C CG  . ASN A 121 ? 0.754 1.003 0.905 0.082  -0.000 0.112  450 ASN AAA CG  
942   O OD1 . ASN A 121 ? 0.773 1.066 0.955 0.087  0.000  0.120  450 ASN AAA OD1 
943   N ND2 . ASN A 121 ? 0.824 1.044 0.959 0.094  -0.004 0.114  450 ASN AAA ND2 
944   N N   . TYR A 122 ? 0.581 0.787 0.688 0.033  0.023  0.084  451 TYR AAA N   
945   C CA  . TYR A 122 ? 0.536 0.725 0.626 0.013  0.021  0.078  451 TYR AAA CA  
946   C C   . TYR A 122 ? 0.526 0.740 0.628 0.005  0.029  0.081  451 TYR AAA C   
947   O O   . TYR A 122 ? 0.554 0.778 0.658 0.017  0.044  0.079  451 TYR AAA O   
948   C CB  . TYR A 122 ? 0.541 0.687 0.602 0.016  0.026  0.067  451 TYR AAA CB  
949   C CG  . TYR A 122 ? 0.530 0.650 0.579 0.019  0.018  0.065  451 TYR AAA CG  
950   C CD1 . TYR A 122 ? 0.518 0.629 0.559 0.006  0.006  0.066  451 TYR AAA CD1 
951   C CD2 . TYR A 122 ? 0.533 0.634 0.576 0.036  0.024  0.063  451 TYR AAA CD2 
952   C CE1 . TYR A 122 ? 0.514 0.601 0.542 0.009  0.000  0.066  451 TYR AAA CE1 
953   C CE2 . TYR A 122 ? 0.527 0.602 0.557 0.038  0.019  0.063  451 TYR AAA CE2 
954   C CZ  . TYR A 122 ? 0.513 0.582 0.535 0.025  0.007  0.065  451 TYR AAA CZ  
955   O OH  . TYR A 122 ? 0.537 0.584 0.545 0.027  0.003  0.067  451 TYR AAA OH  
956   N N   . LEU A 123 ? 0.503 0.727 0.610 -0.014 0.020  0.085  452 LEU AAA N   
957   C CA  . LEU A 123 ? 0.510 0.759 0.629 -0.026 0.025  0.092  452 LEU AAA CA  
958   C C   . LEU A 123 ? 0.505 0.726 0.601 -0.041 0.024  0.087  452 LEU AAA C   
959   O O   . LEU A 123 ? 0.467 0.657 0.545 -0.045 0.015  0.080  452 LEU AAA O   
960   C CB  . LEU A 123 ? 0.515 0.798 0.663 -0.038 0.014  0.102  452 LEU AAA CB  
961   C CG  . LEU A 123 ? 0.503 0.820 0.679 -0.024 0.012  0.109  452 LEU AAA CG  
962   C CD1 . LEU A 123 ? 0.486 0.840 0.691 -0.041 -0.001 0.120  452 LEU AAA CD1 
963   C CD2 . LEU A 123 ? 0.499 0.838 0.687 -0.005 0.031  0.111  452 LEU AAA CD2 
964   N N   . TYR A 124 ? 0.509 0.742 0.606 -0.047 0.034  0.091  453 TYR AAA N   
965   C CA  . TYR A 124 ? 0.501 0.713 0.580 -0.062 0.032  0.090  453 TYR AAA CA  
966   C C   . TYR A 124 ? 0.500 0.741 0.597 -0.076 0.035  0.103  453 TYR AAA C   
967   O O   . TYR A 124 ? 0.502 0.778 0.619 -0.070 0.046  0.109  453 TYR AAA O   
968   C CB  . TYR A 124 ? 0.494 0.683 0.546 -0.053 0.041  0.080  453 TYR AAA CB  
969   C CG  . TYR A 124 ? 0.527 0.736 0.581 -0.041 0.058  0.082  453 TYR AAA CG  
970   C CD1 . TYR A 124 ? 0.531 0.754 0.583 -0.049 0.067  0.089  453 TYR AAA CD1 
971   C CD2 . TYR A 124 ? 0.533 0.746 0.589 -0.022 0.067  0.076  453 TYR AAA CD2 
972   C CE1 . TYR A 124 ? 0.547 0.790 0.597 -0.038 0.084  0.090  453 TYR AAA CE1 
973   C CE2 . TYR A 124 ? 0.544 0.775 0.600 -0.010 0.084  0.075  453 TYR AAA CE2 
974   C CZ  . TYR A 124 ? 0.546 0.793 0.598 -0.018 0.093  0.082  453 TYR AAA CZ  
975   O OH  . TYR A 124 ? 0.536 0.802 0.585 -0.005 0.111  0.081  453 TYR AAA OH  
976   N N   . ARG A 125 ? 0.501 0.727 0.591 -0.094 0.027  0.106  454 ARG AAA N   
977   C CA  . ARG A 125 ? 0.514 0.761 0.618 -0.110 0.031  0.119  454 ARG AAA CA  
978   C C   . ARG A 125 ? 0.540 0.786 0.627 -0.105 0.047  0.121  454 ARG AAA C   
979   O O   . ARG A 125 ? 0.545 0.759 0.603 -0.101 0.047  0.113  454 ARG AAA O   
980   C CB  . ARG A 125 ? 0.523 0.747 0.623 -0.131 0.016  0.122  454 ARG AAA CB  
981   C CG  . ARG A 125 ? 0.533 0.775 0.649 -0.150 0.018  0.137  454 ARG AAA CG  
982   C CD  . ARG A 125 ? 0.539 0.755 0.652 -0.171 0.002  0.138  454 ARG AAA CD  
983   N NE  . ARG A 125 ? 0.528 0.745 0.651 -0.172 -0.014 0.131  454 ARG AAA NE  
984   C CZ  . ARG A 125 ? 0.545 0.796 0.699 -0.180 -0.020 0.137  454 ARG AAA CZ  
985   N NH1 . ARG A 125 ? 0.532 0.823 0.714 -0.188 -0.011 0.150  454 ARG AAA NH1 
986   N NH2 . ARG A 125 ? 0.550 0.798 0.707 -0.180 -0.036 0.130  454 ARG AAA NH2 
987   N N   . LEU A 126 ? 0.559 0.841 0.663 -0.103 0.062  0.131  455 LEU AAA N   
988   C CA  . LEU A 126 ? 0.591 0.879 0.678 -0.096 0.080  0.133  455 LEU AAA CA  
989   C C   . LEU A 126 ? 0.638 0.927 0.722 -0.115 0.082  0.148  455 LEU AAA C   
990   O O   . LEU A 126 ? 0.673 0.948 0.730 -0.113 0.090  0.148  455 LEU AAA O   
991   C CB  . LEU A 126 ? 0.607 0.935 0.714 -0.081 0.096  0.136  455 LEU AAA CB  
992   C CG  . LEU A 126 ? 0.652 0.994 0.744 -0.072 0.117  0.138  455 LEU AAA CG  
993   C CD1 . LEU A 126 ? 0.657 0.961 0.708 -0.060 0.118  0.124  455 LEU AAA CD1 
994   C CD2 . LEU A 126 ? 0.663 1.046 0.779 -0.055 0.132  0.140  455 LEU AAA CD2 
995   N N   . PHE A 127 ? 0.651 0.957 0.763 -0.134 0.075  0.159  456 PHE AAA N   
996   C CA  . PHE A 127 ? 0.678 0.987 0.793 -0.156 0.077  0.176  456 PHE AAA CA  
997   C C   . PHE A 127 ? 0.661 0.943 0.780 -0.176 0.057  0.177  456 PHE AAA C   
998   O O   . PHE A 127 ? 0.624 0.912 0.762 -0.178 0.044  0.171  456 PHE AAA O   
999   C CB  . PHE A 127 ? 0.696 1.056 0.844 -0.163 0.091  0.192  456 PHE AAA CB  
1000  C CG  . PHE A 127 ? 0.733 1.124 0.881 -0.142 0.113  0.191  456 PHE AAA CG  
1001  C CD1 . PHE A 127 ? 0.796 1.176 0.912 -0.135 0.127  0.192  456 PHE AAA CD1 
1002  C CD2 . PHE A 127 ? 0.739 1.168 0.916 -0.129 0.118  0.188  456 PHE AAA CD2 
1003  C CE1 . PHE A 127 ? 0.816 1.221 0.927 -0.115 0.148  0.189  456 PHE AAA CE1 
1004  C CE2 . PHE A 127 ? 0.780 1.234 0.954 -0.108 0.139  0.186  456 PHE AAA CE2 
1005  C CZ  . PHE A 127 ? 0.813 1.255 0.953 -0.101 0.154  0.186  456 PHE AAA CZ  
1006  N N   . ARG A 128 ? 0.672 0.925 0.773 -0.189 0.054  0.184  457 ARG AAA N   
1007  C CA  . ARG A 128 ? 0.695 0.923 0.801 -0.210 0.036  0.187  457 ARG AAA CA  
1008  C C   . ARG A 128 ? 0.740 0.950 0.834 -0.226 0.041  0.202  457 ARG AAA C   
1009  O O   . ARG A 128 ? 0.787 0.989 0.855 -0.215 0.052  0.205  457 ARG AAA O   
1010  C CB  . ARG A 128 ? 0.662 0.849 0.747 -0.201 0.021  0.169  457 ARG AAA CB  
1011  C CG  . ARG A 128 ? 0.660 0.821 0.748 -0.219 0.002  0.167  457 ARG AAA CG  
1012  C CD  . ARG A 128 ? 0.655 0.783 0.723 -0.206 -0.010 0.149  457 ARG AAA CD  
1013  N NE  . ARG A 128 ? 0.663 0.773 0.737 -0.220 -0.027 0.145  457 ARG AAA NE  
1014  C CZ  . ARG A 128 ? 0.691 0.763 0.752 -0.232 -0.037 0.145  457 ARG AAA CZ  
1015  N NH1 . ARG A 128 ? 0.710 0.758 0.751 -0.231 -0.031 0.152  457 ARG AAA NH1 
1016  N NH2 . ARG A 128 ? 0.702 0.759 0.767 -0.244 -0.053 0.139  457 ARG AAA NH2 
1017  N N   . LYS A 129 ? 0.759 0.962 0.869 -0.250 0.031  0.212  458 LYS AAA N   
1018  C CA  . LYS A 129 ? 0.794 0.980 0.897 -0.268 0.035  0.230  458 LYS AAA CA  
1019  C C   . LYS A 129 ? 0.770 0.903 0.832 -0.261 0.030  0.225  458 LYS AAA C   
1020  O O   . LYS A 129 ? 0.827 0.948 0.874 -0.265 0.038  0.240  458 LYS AAA O   
1021  C CB  . LYS A 129 ? 0.841 1.022 0.968 -0.297 0.023  0.238  458 LYS AAA CB  
1022  C CG  . LYS A 129 ? 0.881 1.116 1.053 -0.310 0.026  0.245  458 LYS AAA CG  
1023  C CD  . LYS A 129 ? 0.921 1.144 1.113 -0.342 0.012  0.253  458 LYS AAA CD  
1024  C CE  . LYS A 129 ? 0.944 1.223 1.184 -0.356 0.010  0.259  458 LYS AAA CE  
1025  N NZ  . LYS A 129 ? 1.004 1.269 1.263 -0.388 -0.006 0.265  458 LYS AAA NZ  
1026  N N   . SER A 130 ? 0.727 0.832 0.775 -0.248 0.016  0.207  459 SER AAA N   
1027  C CA  . SER A 130 ? 0.726 0.784 0.741 -0.239 0.010  0.201  459 SER AAA CA  
1028  C C   . SER A 130 ? 0.689 0.737 0.693 -0.220 0.002  0.180  459 SER AAA C   
1029  O O   . SER A 130 ? 0.639 0.709 0.661 -0.217 -0.001 0.170  459 SER AAA O   
1030  C CB  . SER A 130 ? 0.738 0.757 0.750 -0.258 -0.003 0.207  459 SER AAA CB  
1031  O OG  . SER A 130 ? 0.709 0.713 0.729 -0.262 -0.019 0.193  459 SER AAA OG  
1032  N N   . ASN A 131 ? 0.664 0.682 0.641 -0.206 -0.001 0.174  460 ASN AAA N   
1033  C CA  . ASN A 131 ? 0.639 0.648 0.604 -0.188 -0.006 0.155  460 ASN AAA CA  
1034  C C   . ASN A 131 ? 0.635 0.622 0.606 -0.193 -0.021 0.144  460 ASN AAA C   
1035  O O   . ASN A 131 ? 0.655 0.617 0.625 -0.207 -0.029 0.149  460 ASN AAA O   
1036  C CB  . ASN A 131 ? 0.656 0.643 0.593 -0.174 -0.005 0.153  460 ASN AAA CB  
1037  C CG  . ASN A 131 ? 0.655 0.665 0.582 -0.166 0.009  0.160  460 ASN AAA CG  
1038  O OD1 . ASN A 131 ? 0.638 0.680 0.579 -0.169 0.020  0.165  460 ASN AAA OD1 
1039  N ND2 . ASN A 131 ? 0.655 0.648 0.557 -0.156 0.008  0.160  460 ASN AAA ND2 
1040  N N   . LEU A 132 ? 0.616 0.609 0.589 -0.181 -0.024 0.129  461 LEU AAA N   
1041  C CA  . LEU A 132 ? 0.616 0.586 0.586 -0.181 -0.037 0.116  461 LEU AAA CA  
1042  C C   . LEU A 132 ? 0.638 0.568 0.587 -0.176 -0.043 0.113  461 LEU AAA C   
1043  O O   . LEU A 132 ? 0.637 0.563 0.571 -0.164 -0.038 0.113  461 LEU AAA O   
1044  C CB  . LEU A 132 ? 0.593 0.579 0.566 -0.167 -0.036 0.103  461 LEU AAA CB  
1045  C CG  . LEU A 132 ? 0.582 0.606 0.578 -0.169 -0.033 0.105  461 LEU AAA CG  
1046  C CD1 . LEU A 132 ? 0.565 0.594 0.560 -0.154 -0.033 0.092  461 LEU AAA CD1 
1047  C CD2 . LEU A 132 ? 0.600 0.627 0.613 -0.187 -0.043 0.109  461 LEU AAA CD2 
1048  N N   . LYS A 133 ? 0.695 0.596 0.641 -0.184 -0.055 0.108  462 LYS AAA N   
1049  C CA  . LYS A 133 ? 0.706 0.569 0.631 -0.174 -0.062 0.099  462 LYS AAA CA  
1050  C C   . LYS A 133 ? 0.684 0.555 0.605 -0.158 -0.061 0.084  462 LYS AAA C   
1051  O O   . LYS A 133 ? 0.663 0.560 0.596 -0.157 -0.059 0.080  462 LYS AAA O   
1052  C CB  . LYS A 133 ? 0.768 0.599 0.691 -0.188 -0.073 0.096  462 LYS AAA CB  
1053  C CG  . LYS A 133 ? 0.840 0.650 0.763 -0.203 -0.075 0.111  462 LYS AAA CG  
1054  C CD  . LYS A 133 ? 0.879 0.676 0.811 -0.226 -0.085 0.112  462 LYS AAA CD  
1055  C CE  . LYS A 133 ? 0.937 0.739 0.880 -0.245 -0.081 0.132  462 LYS AAA CE  
1056  N NZ  . LYS A 133 ? 0.998 0.768 0.944 -0.267 -0.092 0.134  462 LYS AAA NZ  
1057  N N   . PRO A 134 ? 0.665 0.515 0.572 -0.144 -0.062 0.077  463 PRO AAA N   
1058  C CA  . PRO A 134 ? 0.655 0.512 0.559 -0.130 -0.061 0.064  463 PRO AAA CA  
1059  C C   . PRO A 134 ? 0.642 0.498 0.549 -0.135 -0.067 0.054  463 PRO AAA C   
1060  O O   . PRO A 134 ? 0.690 0.524 0.593 -0.143 -0.075 0.053  463 PRO AAA O   
1061  C CB  . PRO A 134 ? 0.663 0.494 0.554 -0.118 -0.063 0.059  463 PRO AAA CB  
1062  C CG  . PRO A 134 ? 0.674 0.495 0.560 -0.121 -0.062 0.073  463 PRO AAA CG  
1063  C CD  . PRO A 134 ? 0.671 0.493 0.565 -0.140 -0.064 0.083  463 PRO AAA CD  
1064  N N   . PHE A 135 ? 0.615 0.495 0.529 -0.129 -0.063 0.049  464 PHE AAA N   
1065  C CA  . PHE A 135 ? 0.631 0.515 0.546 -0.130 -0.068 0.041  464 PHE AAA CA  
1066  C C   . PHE A 135 ? 0.617 0.510 0.544 -0.147 -0.075 0.047  464 PHE AAA C   
1067  O O   . PHE A 135 ? 0.634 0.526 0.559 -0.150 -0.083 0.041  464 PHE AAA O   
1068  C CB  . PHE A 135 ? 0.643 0.497 0.541 -0.124 -0.073 0.030  464 PHE AAA CB  
1069  C CG  . PHE A 135 ? 0.604 0.456 0.495 -0.108 -0.066 0.024  464 PHE AAA CG  
1070  C CD1 . PHE A 135 ? 0.613 0.488 0.510 -0.100 -0.060 0.022  464 PHE AAA CD1 
1071  C CD2 . PHE A 135 ? 0.630 0.459 0.510 -0.100 -0.067 0.021  464 PHE AAA CD2 
1072  C CE1 . PHE A 135 ? 0.594 0.469 0.487 -0.088 -0.053 0.018  464 PHE AAA CE1 
1073  C CE2 . PHE A 135 ? 0.599 0.433 0.478 -0.086 -0.060 0.017  464 PHE AAA CE2 
1074  C CZ  . PHE A 135 ? 0.581 0.437 0.466 -0.082 -0.054 0.015  464 PHE AAA CZ  
1075  N N   . GLU A 136 ? 0.605 0.510 0.544 -0.157 -0.073 0.059  465 GLU AAA N   
1076  C CA  . GLU A 136 ? 0.624 0.546 0.580 -0.174 -0.078 0.066  465 GLU AAA CA  
1077  C C   . GLU A 136 ? 0.581 0.542 0.555 -0.169 -0.073 0.067  465 GLU AAA C   
1078  O O   . GLU A 136 ? 0.570 0.543 0.542 -0.155 -0.063 0.067  465 GLU AAA O   
1079  C CB  . GLU A 136 ? 0.653 0.574 0.617 -0.187 -0.075 0.080  465 GLU AAA CB  
1080  C CG  . GLU A 136 ? 0.670 0.600 0.652 -0.209 -0.083 0.086  465 GLU AAA CG  
1081  C CD  . GLU A 136 ? 0.710 0.641 0.701 -0.224 -0.079 0.102  465 GLU AAA CD  
1082  O OE1 . GLU A 136 ? 0.704 0.625 0.684 -0.217 -0.070 0.109  465 GLU AAA OE1 
1083  O OE2 . GLU A 136 ? 0.699 0.645 0.710 -0.243 -0.084 0.109  465 GLU AAA OE2 
1084  N N   . ARG A 137 ? 0.591 0.569 0.579 -0.180 -0.082 0.069  466 ARG AAA N   
1085  C CA  . ARG A 137 ? 0.577 0.592 0.583 -0.175 -0.079 0.071  466 ARG AAA CA  
1086  C C   . ARG A 137 ? 0.568 0.613 0.601 -0.191 -0.083 0.082  466 ARG AAA C   
1087  O O   . ARG A 137 ? 0.566 0.599 0.601 -0.208 -0.095 0.082  466 ARG AAA O   
1088  C CB  . ARG A 137 ? 0.590 0.598 0.585 -0.169 -0.089 0.060  466 ARG AAA CB  
1089  C CG  . ARG A 137 ? 0.608 0.648 0.617 -0.159 -0.087 0.062  466 ARG AAA CG  
1090  C CD  . ARG A 137 ? 0.629 0.652 0.618 -0.150 -0.094 0.052  466 ARG AAA CD  
1091  N NE  . ARG A 137 ? 0.660 0.707 0.656 -0.139 -0.094 0.054  466 ARG AAA NE  
1092  C CZ  . ARG A 137 ? 0.699 0.768 0.708 -0.144 -0.105 0.057  466 ARG AAA CZ  
1093  N NH1 . ARG A 137 ? 0.737 0.811 0.755 -0.162 -0.118 0.058  466 ARG AAA NH1 
1094  N NH2 . ARG A 137 ? 0.693 0.780 0.706 -0.131 -0.104 0.059  466 ARG AAA NH2 
1095  N N   . ASP A 138 ? 0.553 0.633 0.606 -0.187 -0.071 0.091  467 ASP AAA N   
1096  C CA  . ASP A 138 ? 0.541 0.657 0.624 -0.201 -0.072 0.103  467 ASP AAA CA  
1097  C C   . ASP A 138 ? 0.518 0.674 0.621 -0.190 -0.070 0.104  467 ASP AAA C   
1098  O O   . ASP A 138 ? 0.487 0.653 0.588 -0.172 -0.056 0.105  467 ASP AAA O   
1099  C CB  . ASP A 138 ? 0.546 0.668 0.634 -0.206 -0.058 0.115  467 ASP AAA CB  
1100  C CG  . ASP A 138 ? 0.555 0.714 0.675 -0.223 -0.056 0.129  467 ASP AAA CG  
1101  O OD1 . ASP A 138 ? 0.557 0.746 0.701 -0.229 -0.065 0.130  467 ASP AAA OD1 
1102  O OD2 . ASP A 138 ? 0.537 0.698 0.659 -0.231 -0.046 0.140  467 ASP AAA OD2 
1103  N N   . ILE A 139 ? 0.546 0.721 0.666 -0.199 -0.084 0.105  468 ILE AAA N   
1104  C CA  . ILE A 139 ? 0.519 0.734 0.661 -0.187 -0.084 0.108  468 ILE AAA CA  
1105  C C   . ILE A 139 ? 0.505 0.766 0.686 -0.202 -0.086 0.121  468 ILE AAA C   
1106  O O   . ILE A 139 ? 0.492 0.791 0.696 -0.194 -0.089 0.124  468 ILE AAA O   
1107  C CB  . ILE A 139 ? 0.533 0.736 0.661 -0.181 -0.100 0.098  468 ILE AAA CB  
1108  C CG1 . ILE A 139 ? 0.548 0.740 0.674 -0.202 -0.120 0.094  468 ILE AAA CG1 
1109  C CG2 . ILE A 139 ? 0.558 0.723 0.652 -0.165 -0.094 0.087  468 ILE AAA CG2 
1110  C CD1 . ILE A 139 ? 0.559 0.747 0.673 -0.196 -0.136 0.086  468 ILE AAA CD1 
1111  N N   . SER A 140 ? 0.513 0.774 0.703 -0.220 -0.082 0.129  469 SER AAA N   
1112  C CA  . SER A 140 ? 0.511 0.818 0.741 -0.237 -0.081 0.143  469 SER AAA CA  
1113  C C   . SER A 140 ? 0.483 0.832 0.733 -0.220 -0.061 0.152  469 SER AAA C   
1114  O O   . SER A 140 ? 0.447 0.781 0.676 -0.200 -0.046 0.148  469 SER AAA O   
1115  C CB  . SER A 140 ? 0.530 0.820 0.760 -0.262 -0.080 0.150  469 SER AAA CB  
1116  O OG  . SER A 140 ? 0.539 0.813 0.752 -0.253 -0.061 0.154  469 SER AAA OG  
1117  N N   . THR A 141 ? 0.483 0.886 0.774 -0.226 -0.061 0.163  470 THR AAA N   
1118  C CA  . THR A 141 ? 0.476 0.927 0.793 -0.210 -0.042 0.172  470 THR AAA CA  
1119  C C   . THR A 141 ? 0.494 0.986 0.848 -0.232 -0.036 0.188  470 THR AAA C   
1120  O O   . THR A 141 ? 0.516 1.064 0.909 -0.227 -0.030 0.197  470 THR AAA O   
1121  C CB  . THR A 141 ? 0.452 0.930 0.784 -0.190 -0.048 0.169  470 THR AAA CB  
1122  O OG1 . THR A 141 ? 0.467 0.964 0.821 -0.207 -0.071 0.170  470 THR AAA OG1 
1123  C CG2 . THR A 141 ? 0.446 0.884 0.741 -0.168 -0.050 0.155  470 THR AAA CG2 
1124  N N   . GLU A 142 ? 0.528 0.994 0.872 -0.255 -0.036 0.193  471 GLU AAA N   
1125  C CA  . GLU A 142 ? 0.562 1.061 0.937 -0.277 -0.027 0.210  471 GLU AAA CA  
1126  C C   . GLU A 142 ? 0.567 1.087 0.941 -0.260 0.002  0.219  471 GLU AAA C   
1127  O O   . GLU A 142 ? 0.581 1.065 0.916 -0.242 0.012  0.210  471 GLU AAA O   
1128  C CB  . GLU A 142 ? 0.602 1.058 0.961 -0.306 -0.036 0.213  471 GLU AAA CB  
1129  C CG  . GLU A 142 ? 0.647 1.086 1.010 -0.324 -0.064 0.204  471 GLU AAA CG  
1130  C CD  . GLU A 142 ? 0.670 1.167 1.083 -0.340 -0.077 0.212  471 GLU AAA CD  
1131  O OE1 . GLU A 142 ? 0.654 1.192 1.104 -0.358 -0.067 0.229  471 GLU AAA OE1 
1132  O OE2 . GLU A 142 ? 0.670 1.173 1.085 -0.334 -0.095 0.201  471 GLU AAA OE2 
1133  N N   . ILE A 143 ? 0.563 1.143 0.978 -0.266 0.015  0.234  472 ILE AAA N   
1134  C CA  . ILE A 143 ? 0.577 1.182 0.993 -0.252 0.044  0.244  472 ILE AAA CA  
1135  C C   . ILE A 143 ? 0.591 1.153 0.973 -0.264 0.053  0.249  472 ILE AAA C   
1136  O O   . ILE A 143 ? 0.599 1.146 0.986 -0.293 0.043  0.257  472 ILE AAA O   
1137  C CB  . ILE A 143 ? 0.598 1.277 1.070 -0.261 0.055  0.261  472 ILE AAA CB  
1138  C CG1 . ILE A 143 ? 0.582 1.305 1.087 -0.245 0.046  0.257  472 ILE AAA CG1 
1139  C CG2 . ILE A 143 ? 0.612 1.317 1.082 -0.249 0.087  0.272  472 ILE AAA CG2 
1140  C CD1 . ILE A 143 ? 0.560 1.267 1.039 -0.207 0.052  0.242  472 ILE AAA CD1 
1141  N N   . TYR A 144 ? 0.601 1.141 0.947 -0.242 0.069  0.243  473 TYR AAA N   
1142  C CA  . TYR A 144 ? 0.641 1.138 0.949 -0.248 0.077  0.247  473 TYR AAA CA  
1143  C C   . TYR A 144 ? 0.682 1.219 1.007 -0.257 0.101  0.267  473 TYR AAA C   
1144  O O   . TYR A 144 ? 0.659 1.239 0.997 -0.239 0.120  0.270  473 TYR AAA O   
1145  C CB  . TYR A 144 ? 0.632 1.091 0.894 -0.221 0.081  0.231  473 TYR AAA CB  
1146  C CG  . TYR A 144 ? 0.662 1.084 0.885 -0.223 0.091  0.235  473 TYR AAA CG  
1147  C CD1 . TYR A 144 ? 0.672 1.042 0.869 -0.235 0.076  0.232  473 TYR AAA CD1 
1148  C CD2 . TYR A 144 ? 0.681 1.122 0.891 -0.210 0.115  0.241  473 TYR AAA CD2 
1149  C CE1 . TYR A 144 ? 0.697 1.035 0.859 -0.234 0.083  0.236  473 TYR AAA CE1 
1150  C CE2 . TYR A 144 ? 0.711 1.120 0.883 -0.209 0.122  0.244  473 TYR AAA CE2 
1151  C CZ  . TYR A 144 ? 0.724 1.082 0.872 -0.221 0.106  0.243  473 TYR AAA CZ  
1152  O OH  . TYR A 144 ? 0.745 1.075 0.858 -0.221 0.112  0.249  473 TYR AAA OH  
1153  N N   . GLN A 145 ? 0.732 1.252 1.055 -0.284 0.099  0.282  474 GLN AAA N   
1154  C CA  . GLN A 145 ? 0.780 1.327 1.111 -0.296 0.121  0.304  474 GLN AAA CA  
1155  C C   . GLN A 145 ? 0.811 1.325 1.092 -0.280 0.136  0.302  474 GLN AAA C   
1156  O O   . GLN A 145 ? 0.846 1.305 1.093 -0.288 0.126  0.302  474 GLN AAA O   
1157  C CB  . GLN A 145 ? 0.800 1.337 1.149 -0.334 0.111  0.320  474 GLN AAA CB  
1158  C CG  . GLN A 145 ? 0.854 1.414 1.208 -0.347 0.135  0.344  474 GLN AAA CG  
1159  C CD  . GLN A 145 ? 0.885 1.444 1.266 -0.386 0.127  0.362  474 GLN AAA CD  
1160  O OE1 . GLN A 145 ? 0.872 1.431 1.280 -0.404 0.104  0.356  474 GLN AAA OE1 
1161  N NE2 . GLN A 145 ? 0.936 1.496 1.310 -0.401 0.144  0.384  474 GLN AAA NE2 
1162  N N   . ALA A 146 ? 0.801 1.345 1.075 -0.255 0.158  0.301  475 ALA AAA N   
1163  C CA  . ALA A 146 ? 0.831 1.350 1.056 -0.236 0.173  0.297  475 ALA AAA CA  
1164  C C   . ALA A 146 ? 0.883 1.421 1.104 -0.249 0.195  0.321  475 ALA AAA C   
1165  O O   . ALA A 146 ? 0.916 1.427 1.092 -0.240 0.205  0.322  475 ALA AAA O   
1166  C CB  . ALA A 146 ? 0.814 1.353 1.031 -0.203 0.185  0.281  475 ALA AAA CB  
1167  N N   . GLY A 147 ? 0.885 1.468 1.151 -0.271 0.203  0.340  476 GLY AAA N   
1168  C CA  . GLY A 147 ? 0.897 1.509 1.166 -0.283 0.228  0.365  476 GLY AAA CA  
1169  C C   . GLY A 147 ? 0.918 1.530 1.215 -0.322 0.220  0.387  476 GLY AAA C   
1170  O O   . GLY A 147 ? 0.896 1.479 1.206 -0.338 0.194  0.380  476 GLY AAA O   
1171  N N   . SER A 148 ? 0.960 1.602 1.266 -0.336 0.243  0.412  477 SER AAA N   
1172  C CA  . SER A 148 ? 1.002 1.647 1.335 -0.375 0.241  0.437  477 SER AAA CA  
1173  C C   . SER A 148 ? 1.004 1.686 1.399 -0.395 0.226  0.437  477 SER AAA C   
1174  O O   . SER A 148 ? 1.045 1.695 1.452 -0.425 0.205  0.441  477 SER AAA O   
1175  C CB  . SER A 148 ? 1.022 1.703 1.353 -0.380 0.274  0.464  477 SER AAA CB  
1176  O OG  . SER A 148 ? 1.080 1.769 1.441 -0.419 0.275  0.490  477 SER AAA OG  
1177  N N   . THR A 149 ? 0.982 1.729 1.417 -0.381 0.236  0.433  478 THR AAA N   
1178  C CA  . THR A 149 ? 0.962 1.761 1.464 -0.402 0.225  0.437  478 THR AAA CA  
1179  C C   . THR A 149 ? 0.915 1.677 1.418 -0.403 0.190  0.415  478 THR AAA C   
1180  O O   . THR A 149 ? 0.901 1.629 1.369 -0.375 0.181  0.392  478 THR AAA O   
1181  C CB  . THR A 149 ? 0.946 1.827 1.489 -0.381 0.247  0.440  478 THR AAA CB  
1182  O OG1 . THR A 149 ? 0.933 1.799 1.441 -0.340 0.250  0.416  478 THR AAA OG1 
1183  C CG2 . THR A 149 ? 0.955 1.886 1.511 -0.387 0.282  0.465  478 THR AAA CG2 
1184  N N   . PRO A 150 ? 0.928 1.694 1.469 -0.436 0.168  0.419  479 PRO AAA N   
1185  C CA  . PRO A 150 ? 0.899 1.641 1.445 -0.435 0.135  0.398  479 PRO AAA CA  
1186  C C   . PRO A 150 ? 0.872 1.672 1.451 -0.409 0.136  0.386  479 PRO AAA C   
1187  O O   . PRO A 150 ? 0.862 1.730 1.478 -0.404 0.158  0.399  479 PRO AAA O   
1188  C CB  . PRO A 150 ? 0.920 1.660 1.501 -0.480 0.116  0.409  479 PRO AAA CB  
1189  C CG  . PRO A 150 ? 0.941 1.741 1.563 -0.500 0.142  0.438  479 PRO AAA CG  
1190  C CD  . PRO A 150 ? 0.951 1.746 1.533 -0.476 0.173  0.446  479 PRO AAA CD  
1191  N N   . CYS A 151 ? 0.855 1.628 1.419 -0.392 0.114  0.363  480 CYS AAA N   
1192  C CA  . CYS A 151 ? 0.846 1.659 1.427 -0.360 0.115  0.350  480 CYS AAA CA  
1193  C C   . CYS A 151 ? 0.837 1.699 1.475 -0.375 0.094  0.351  480 CYS AAA C   
1194  O O   . CYS A 151 ? 0.832 1.745 1.497 -0.351 0.099  0.347  480 CYS AAA O   
1195  C CB  . CYS A 151 ? 0.811 1.567 1.342 -0.332 0.104  0.326  480 CYS AAA CB  
1196  S SG  . CYS A 151 ? 0.848 1.567 1.320 -0.306 0.130  0.322  480 CYS AAA SG  
1197  N N   . ASN A 152 ? 0.845 1.688 1.495 -0.411 0.071  0.354  481 ASN AAA N   
1198  C CA  . ASN A 152 ? 0.862 1.742 1.560 -0.428 0.045  0.352  481 ASN AAA CA  
1199  C C   . ASN A 152 ? 0.843 1.725 1.535 -0.397 0.030  0.332  481 ASN AAA C   
1200  O O   . ASN A 152 ? 0.819 1.763 1.560 -0.396 0.021  0.334  481 ASN AAA O   
1201  C CB  . ASN A 152 ? 0.847 1.814 1.614 -0.445 0.057  0.374  481 ASN AAA CB  
1202  C CG  . ASN A 152 ? 0.866 1.833 1.643 -0.479 0.072  0.396  481 ASN AAA CG  
1203  O OD1 . ASN A 152 ? 0.871 1.784 1.601 -0.479 0.084  0.398  481 ASN AAA OD1 
1204  N ND2 . ASN A 152 ? 0.893 1.923 1.731 -0.508 0.070  0.413  481 ASN AAA ND2 
1205  N N   . GLY A 153 ? 0.872 1.693 1.508 -0.372 0.028  0.314  482 GLY AAA N   
1206  C CA  . GLY A 153 ? 0.859 1.670 1.479 -0.343 0.015  0.295  482 GLY AAA CA  
1207  C C   . GLY A 153 ? 0.835 1.709 1.487 -0.312 0.030  0.298  482 GLY AAA C   
1208  O O   . GLY A 153 ? 0.820 1.708 1.482 -0.295 0.015  0.288  482 GLY AAA O   
1209  N N   . VAL A 154 ? 0.814 1.724 1.478 -0.303 0.061  0.311  483 VAL AAA N   
1210  C CA  . VAL A 154 ? 0.778 1.745 1.467 -0.270 0.082  0.314  483 VAL AAA CA  
1211  C C   . VAL A 154 ? 0.768 1.703 1.410 -0.243 0.108  0.308  483 VAL AAA C   
1212  O O   . VAL A 154 ? 0.758 1.662 1.373 -0.258 0.120  0.314  483 VAL AAA O   
1213  C CB  . VAL A 154 ? 0.778 1.829 1.532 -0.284 0.094  0.335  483 VAL AAA CB  
1214  C CG1 . VAL A 154 ? 0.771 1.876 1.544 -0.250 0.125  0.340  483 VAL AAA CG1 
1215  C CG2 . VAL A 154 ? 0.768 1.859 1.572 -0.305 0.065  0.338  483 VAL AAA CG2 
1216  N N   . GLU A 155 ? 0.751 1.687 1.381 -0.206 0.115  0.296  484 GLU AAA N   
1217  C CA  . GLU A 155 ? 0.733 1.637 1.317 -0.177 0.137  0.286  484 GLU AAA CA  
1218  C C   . GLU A 155 ? 0.727 1.682 1.330 -0.168 0.171  0.300  484 GLU AAA C   
1219  O O   . GLU A 155 ? 0.661 1.688 1.321 -0.171 0.177  0.314  484 GLU AAA O   
1220  C CB  . GLU A 155 ? 0.728 1.618 1.298 -0.142 0.131  0.269  484 GLU AAA CB  
1221  C CG  . GLU A 155 ? 0.771 1.610 1.319 -0.149 0.100  0.256  484 GLU AAA CG  
1222  C CD  . GLU A 155 ? 0.819 1.625 1.337 -0.117 0.097  0.239  484 GLU AAA CD  
1223  O OE1 . GLU A 155 ? 0.844 1.638 1.337 -0.093 0.119  0.233  484 GLU AAA OE1 
1224  O OE2 . GLU A 155 ? 0.853 1.647 1.374 -0.115 0.074  0.232  484 GLU AAA OE2 
1225  N N   . GLY A 156 ? 0.727 1.650 1.284 -0.156 0.192  0.296  485 GLY AAA N   
1226  C CA  . GLY A 156 ? 0.719 1.683 1.281 -0.141 0.226  0.306  485 GLY AAA CA  
1227  C C   . GLY A 156 ? 0.726 1.643 1.233 -0.144 0.241  0.305  485 GLY AAA C   
1228  O O   . GLY A 156 ? 0.706 1.556 1.166 -0.143 0.226  0.290  485 GLY AAA O   
1229  N N   . PHE A 157 ? 0.750 1.703 1.262 -0.146 0.270  0.321  486 PHE AAA N   
1230  C CA  . PHE A 157 ? 0.789 1.709 1.252 -0.149 0.287  0.325  486 PHE AAA CA  
1231  C C   . PHE A 157 ? 0.785 1.644 1.219 -0.179 0.264  0.326  486 PHE AAA C   
1232  O O   . PHE A 157 ? 0.773 1.647 1.242 -0.210 0.252  0.340  486 PHE AAA O   
1233  C CB  . PHE A 157 ? 0.805 1.789 1.296 -0.157 0.318  0.348  486 PHE AAA CB  
1234  C CG  . PHE A 157 ? 0.849 1.811 1.304 -0.174 0.333  0.363  486 PHE AAA CG  
1235  C CD1 . PHE A 157 ? 0.878 1.785 1.266 -0.158 0.339  0.351  486 PHE AAA CD1 
1236  C CD2 . PHE A 157 ? 0.885 1.883 1.373 -0.207 0.342  0.390  486 PHE AAA CD2 
1237  C CE1 . PHE A 157 ? 0.912 1.801 1.265 -0.172 0.352  0.365  486 PHE AAA CE1 
1238  C CE2 . PHE A 157 ? 0.930 1.905 1.381 -0.222 0.356  0.405  486 PHE AAA CE2 
1239  C CZ  . PHE A 157 ? 0.935 1.854 1.318 -0.204 0.360  0.393  486 PHE AAA CZ  
1240  N N   . ASN A 158 ? 0.785 1.580 1.161 -0.168 0.258  0.311  487 ASN AAA N   
1241  C CA  . ASN A 158 ? 0.799 1.531 1.141 -0.190 0.238  0.310  487 ASN AAA CA  
1242  C C   . ASN A 158 ? 0.777 1.494 1.145 -0.210 0.206  0.306  487 ASN AAA C   
1243  O O   . ASN A 158 ? 0.770 1.447 1.124 -0.234 0.191  0.310  487 ASN AAA O   
1244  C CB  . ASN A 158 ? 0.816 1.553 1.153 -0.214 0.252  0.333  487 ASN AAA CB  
1245  C CG  . ASN A 158 ? 0.856 1.585 1.146 -0.195 0.277  0.333  487 ASN AAA CG  
1246  O OD1 . ASN A 158 ? 0.909 1.686 1.212 -0.188 0.304  0.345  487 ASN AAA OD1 
1247  N ND2 . ASN A 158 ? 0.872 1.542 1.109 -0.184 0.267  0.319  487 ASN AAA ND2 
1248  N N   . CYS A 159 ? 0.747 1.493 1.149 -0.197 0.197  0.297  488 CYS AAA N   
1249  C CA  . CYS A 159 ? 0.721 1.461 1.149 -0.213 0.168  0.292  488 CYS AAA CA  
1250  C C   . CYS A 159 ? 0.657 1.380 1.074 -0.185 0.156  0.271  488 CYS AAA C   
1251  O O   . CYS A 159 ? 0.618 1.387 1.070 -0.171 0.158  0.271  488 CYS AAA O   
1252  C CB  . CYS A 159 ? 0.738 1.543 1.228 -0.233 0.168  0.310  488 CYS AAA CB  
1253  S SG  . CYS A 159 ? 0.804 1.609 1.307 -0.277 0.169  0.334  488 CYS AAA SG  
1254  N N   . TYR A 160 ? 0.625 1.284 0.994 -0.178 0.145  0.255  489 TYR AAA N   
1255  C CA  . TYR A 160 ? 0.619 1.255 0.968 -0.150 0.139  0.235  489 TYR AAA CA  
1256  C C   . TYR A 160 ? 0.587 1.199 0.941 -0.159 0.110  0.226  489 TYR AAA C   
1257  O O   . TYR A 160 ? 0.585 1.166 0.931 -0.183 0.094  0.228  489 TYR AAA O   
1258  C CB  . TYR A 160 ? 0.645 1.233 0.940 -0.134 0.148  0.223  489 TYR AAA CB  
1259  C CG  . TYR A 160 ? 0.683 1.291 0.966 -0.127 0.175  0.232  489 TYR AAA CG  
1260  C CD1 . TYR A 160 ? 0.693 1.355 1.003 -0.111 0.196  0.238  489 TYR AAA CD1 
1261  C CD2 . TYR A 160 ? 0.708 1.283 0.953 -0.137 0.181  0.236  489 TYR AAA CD2 
1262  C CE1 . TYR A 160 ? 0.725 1.408 1.023 -0.105 0.223  0.246  489 TYR AAA CE1 
1263  C CE2 . TYR A 160 ? 0.741 1.336 0.973 -0.131 0.206  0.245  489 TYR AAA CE2 
1264  C CZ  . TYR A 160 ? 0.758 1.407 1.016 -0.115 0.228  0.250  489 TYR AAA CZ  
1265  O OH  . TYR A 160 ? 0.850 1.521 1.093 -0.109 0.255  0.259  489 TYR AAA OH  
1266  N N   . PHE A 161 ? 0.544 1.168 0.910 -0.138 0.104  0.217  490 PHE AAA N   
1267  C CA  . PHE A 161 ? 0.529 1.121 0.886 -0.138 0.079  0.205  490 PHE AAA CA  
1268  C C   . PHE A 161 ? 0.522 1.051 0.828 -0.132 0.076  0.191  490 PHE AAA C   
1269  O O   . PHE A 161 ? 0.503 1.019 0.784 -0.112 0.092  0.185  490 PHE AAA O   
1270  C CB  . PHE A 161 ? 0.523 1.144 0.902 -0.114 0.077  0.200  490 PHE AAA CB  
1271  C CG  . PHE A 161 ? 0.512 1.109 0.887 -0.115 0.051  0.191  490 PHE AAA CG  
1272  C CD1 . PHE A 161 ? 0.511 1.128 0.914 -0.137 0.031  0.198  490 PHE AAA CD1 
1273  C CD2 . PHE A 161 ? 0.498 1.053 0.839 -0.095 0.047  0.176  490 PHE AAA CD2 
1274  C CE1 . PHE A 161 ? 0.508 1.102 0.902 -0.138 0.007  0.189  490 PHE AAA CE1 
1275  C CE2 . PHE A 161 ? 0.501 1.034 0.835 -0.097 0.025  0.169  490 PHE AAA CE2 
1276  C CZ  . PHE A 161 ? 0.512 1.064 0.871 -0.118 0.005  0.175  490 PHE AAA CZ  
1277  N N   . PRO A 162 ? 0.543 1.029 0.830 -0.149 0.057  0.186  491 PRO AAA N   
1278  C CA  . PRO A 162 ? 0.538 0.968 0.778 -0.147 0.056  0.176  491 PRO AAA CA  
1279  C C   . PRO A 162 ? 0.529 0.927 0.743 -0.124 0.053  0.159  491 PRO AAA C   
1280  O O   . PRO A 162 ? 0.519 0.879 0.698 -0.120 0.055  0.151  491 PRO AAA O   
1281  C CB  . PRO A 162 ? 0.539 0.943 0.777 -0.173 0.037  0.178  491 PRO AAA CB  
1282  C CG  . PRO A 162 ? 0.536 0.966 0.806 -0.180 0.020  0.178  491 PRO AAA CG  
1283  C CD  . PRO A 162 ? 0.538 1.028 0.846 -0.171 0.034  0.189  491 PRO AAA CD  
1284  N N   . LEU A 163 ? 0.528 0.942 0.758 -0.111 0.047  0.154  492 LEU AAA N   
1285  C CA  . LEU A 163 ? 0.515 0.898 0.721 -0.090 0.043  0.140  492 LEU AAA CA  
1286  C C   . LEU A 163 ? 0.516 0.916 0.723 -0.064 0.062  0.137  492 LEU AAA C   
1287  O O   . LEU A 163 ? 0.504 0.950 0.743 -0.060 0.071  0.146  492 LEU AAA O   
1288  C CB  . LEU A 163 ? 0.509 0.893 0.728 -0.091 0.024  0.137  492 LEU AAA CB  
1289  C CG  . LEU A 163 ? 0.524 0.888 0.738 -0.114 0.004  0.137  492 LEU AAA CG  
1290  C CD1 . LEU A 163 ? 0.518 0.875 0.732 -0.110 -0.014 0.131  492 LEU AAA CD1 
1291  C CD2 . LEU A 163 ? 0.546 0.861 0.724 -0.121 0.004  0.129  492 LEU AAA CD2 
1292  N N   . GLN A 164 ? 0.548 0.913 0.725 -0.049 0.066  0.124  493 GLN AAA N   
1293  C CA  . GLN A 164 ? 0.576 0.946 0.747 -0.024 0.083  0.118  493 GLN AAA CA  
1294  C C   . GLN A 164 ? 0.564 0.899 0.718 -0.010 0.074  0.106  493 GLN AAA C   
1295  O O   . GLN A 164 ? 0.553 0.854 0.688 -0.020 0.061  0.100  493 GLN AAA O   
1296  C CB  . GLN A 164 ? 0.657 1.015 0.802 -0.022 0.099  0.114  493 GLN AAA CB  
1297  C CG  . GLN A 164 ? 0.722 1.081 0.857 0.004  0.116  0.105  493 GLN AAA CG  
1298  C CD  . GLN A 164 ? 0.810 1.220 0.979 0.016  0.130  0.115  493 GLN AAA CD  
1299  O OE1 . GLN A 164 ? 0.797 1.246 0.990 0.004  0.135  0.128  493 GLN AAA OE1 
1300  N NE2 . GLN A 164 ? 0.871 1.282 1.046 0.039  0.134  0.109  493 GLN AAA NE2 
1301  N N   . SER A 165 ? 0.594 0.938 0.756 0.013  0.083  0.103  494 SER AAA N   
1302  C CA  . SER A 165 ? 0.593 0.907 0.742 0.028  0.077  0.093  494 SER AAA CA  
1303  C C   . SER A 165 ? 0.589 0.863 0.703 0.037  0.087  0.079  494 SER AAA C   
1304  O O   . SER A 165 ? 0.590 0.872 0.697 0.042  0.102  0.077  494 SER AAA O   
1305  C CB  . SER A 165 ? 0.612 0.954 0.787 0.048  0.081  0.099  494 SER AAA CB  
1306  O OG  . SER A 165 ? 0.713 1.023 0.874 0.064  0.077  0.091  494 SER AAA OG  
1307  N N   . TYR A 166 ? 0.576 0.809 0.668 0.038  0.078  0.070  495 TYR AAA N   
1308  C CA  . TYR A 166 ? 0.572 0.768 0.634 0.045  0.085  0.056  495 TYR AAA CA  
1309  C C   . TYR A 166 ? 0.594 0.786 0.656 0.070  0.098  0.050  495 TYR AAA C   
1310  O O   . TYR A 166 ? 0.624 0.801 0.666 0.078  0.109  0.039  495 TYR AAA O   
1311  C CB  . TYR A 166 ? 0.551 0.707 0.594 0.037  0.073  0.049  495 TYR AAA CB  
1312  C CG  . TYR A 166 ? 0.522 0.668 0.552 0.017  0.065  0.048  495 TYR AAA CG  
1313  C CD1 . TYR A 166 ? 0.505 0.639 0.514 0.014  0.072  0.041  495 TYR AAA CD1 
1314  C CD2 . TYR A 166 ? 0.492 0.638 0.528 0.002  0.051  0.054  495 TYR AAA CD2 
1315  C CE1 . TYR A 166 ? 0.480 0.604 0.477 -0.002 0.065  0.041  495 TYR AAA CE1 
1316  C CE2 . TYR A 166 ? 0.467 0.601 0.490 -0.014 0.045  0.053  495 TYR AAA CE2 
1317  C CZ  . TYR A 166 ? 0.477 0.600 0.482 -0.016 0.052  0.048  495 TYR AAA CZ  
1318  O OH  . TYR A 166 ? 0.471 0.583 0.466 -0.030 0.045  0.048  495 TYR AAA OH  
1319  N N   . GLY A 167 ? 0.605 0.808 0.687 0.083  0.095  0.056  496 GLY AAA N   
1320  C CA  . GLY A 167 ? 0.660 0.854 0.741 0.109  0.106  0.050  496 GLY AAA CA  
1321  C C   . GLY A 167 ? 0.679 0.820 0.727 0.112  0.108  0.035  496 GLY AAA C   
1322  O O   . GLY A 167 ? 0.689 0.817 0.718 0.118  0.120  0.023  496 GLY AAA O   
1323  N N   . PHE A 168 ? 0.648 0.759 0.689 0.107  0.096  0.034  497 PHE AAA N   
1324  C CA  . PHE A 168 ? 0.643 0.705 0.656 0.105  0.095  0.022  497 PHE AAA CA  
1325  C C   . PHE A 168 ? 0.695 0.734 0.706 0.128  0.102  0.017  497 PHE AAA C   
1326  O O   . PHE A 168 ? 0.710 0.753 0.736 0.137  0.097  0.028  497 PHE AAA O   
1327  C CB  . PHE A 168 ? 0.605 0.650 0.614 0.088  0.080  0.025  497 PHE AAA CB  
1328  C CG  . PHE A 168 ? 0.564 0.618 0.568 0.067  0.073  0.026  497 PHE AAA CG  
1329  C CD1 . PHE A 168 ? 0.539 0.581 0.525 0.058  0.077  0.015  497 PHE AAA CD1 
1330  C CD2 . PHE A 168 ? 0.543 0.616 0.560 0.055  0.061  0.037  497 PHE AAA CD2 
1331  C CE1 . PHE A 168 ? 0.512 0.561 0.494 0.040  0.070  0.017  497 PHE AAA CE1 
1332  C CE2 . PHE A 168 ? 0.504 0.581 0.517 0.036  0.055  0.037  497 PHE AAA CE2 
1333  C CZ  . PHE A 168 ? 0.504 0.569 0.500 0.029  0.059  0.028  497 PHE AAA CZ  
1334  N N   . GLN A 169 ? 0.735 0.747 0.726 0.137  0.113  0.002  498 GLN AAA N   
1335  C CA  . GLN A 169 ? 0.796 0.775 0.780 0.158  0.120  -0.004 498 GLN AAA CA  
1336  C C   . GLN A 169 ? 0.820 0.747 0.778 0.148  0.117  -0.017 498 GLN AAA C   
1337  O O   . GLN A 169 ? 0.841 0.760 0.782 0.131  0.114  -0.027 498 GLN AAA O   
1338  C CB  . GLN A 169 ? 0.834 0.826 0.816 0.178  0.137  -0.012 498 GLN AAA CB  
1339  C CG  . GLN A 169 ? 0.845 0.891 0.859 0.188  0.141  0.003  498 GLN AAA CG  
1340  C CD  . GLN A 169 ? 0.898 0.961 0.915 0.212  0.160  -0.003 498 GLN AAA CD  
1341  O OE1 . GLN A 169 ? 0.932 1.007 0.936 0.207  0.169  -0.010 498 GLN AAA OE1 
1342  N NE2 . GLN A 169 ? 0.952 1.014 0.982 0.238  0.166  0.001  498 GLN AAA NE2 
1343  N N   . PRO A 170 ? 0.837 0.729 0.792 0.157  0.115  -0.016 499 PRO AAA N   
1344  C CA  . PRO A 170 ? 0.844 0.686 0.777 0.145  0.111  -0.026 499 PRO AAA CA  
1345  C C   . PRO A 170 ? 0.855 0.673 0.765 0.144  0.118  -0.047 499 PRO AAA C   
1346  O O   . PRO A 170 ? 0.883 0.675 0.777 0.126  0.112  -0.056 499 PRO AAA O   
1347  C CB  . PRO A 170 ? 0.885 0.697 0.822 0.160  0.111  -0.019 499 PRO AAA CB  
1348  C CG  . PRO A 170 ? 0.888 0.729 0.844 0.186  0.119  -0.010 499 PRO AAA CG  
1349  C CD  . PRO A 170 ? 0.856 0.753 0.828 0.180  0.117  -0.004 499 PRO AAA CD  
1350  N N   . THR A 171 ? 0.842 0.671 0.748 0.162  0.130  -0.055 500 THR AAA N   
1351  C CA  . THR A 171 ? 0.876 0.682 0.755 0.165  0.138  -0.077 500 THR AAA CA  
1352  C C   . THR A 171 ? 0.854 0.689 0.724 0.149  0.137  -0.081 500 THR AAA C   
1353  O O   . THR A 171 ? 0.872 0.690 0.717 0.148  0.141  -0.099 500 THR AAA O   
1354  C CB  . THR A 171 ? 0.889 0.693 0.767 0.195  0.154  -0.082 500 THR AAA CB  
1355  O OG1 . THR A 171 ? 0.862 0.721 0.766 0.204  0.159  -0.067 500 THR AAA OG1 
1356  C CG2 . THR A 171 ? 0.916 0.681 0.797 0.212  0.156  -0.081 500 THR AAA CG2 
1357  N N   . ASN A 172 ? 0.796 0.673 0.685 0.137  0.131  -0.066 501 ASN AAA N   
1358  C CA  . ASN A 172 ? 0.776 0.677 0.656 0.121  0.128  -0.068 501 ASN AAA CA  
1359  C C   . ASN A 172 ? 0.781 0.649 0.637 0.104  0.119  -0.082 501 ASN AAA C   
1360  O O   . ASN A 172 ? 0.750 0.588 0.606 0.096  0.111  -0.084 501 ASN AAA O   
1361  C CB  . ASN A 172 ? 0.732 0.668 0.635 0.107  0.119  -0.049 501 ASN AAA CB  
1362  C CG  . ASN A 172 ? 0.725 0.703 0.653 0.119  0.126  -0.035 501 ASN AAA CG  
1363  O OD1 . ASN A 172 ? 0.775 0.760 0.705 0.139  0.139  -0.038 501 ASN AAA OD1 
1364  N ND2 . ASN A 172 ? 0.698 0.706 0.646 0.107  0.117  -0.019 501 ASN AAA ND2 
1365  N N   . GLY A 173 ? 0.794 0.671 0.631 0.097  0.121  -0.092 502 GLY AAA N   
1366  C CA  . GLY A 173 ? 0.804 0.663 0.622 0.078  0.109  -0.102 502 GLY AAA CA  
1367  C C   . GLY A 173 ? 0.767 0.637 0.603 0.059  0.096  -0.089 502 GLY AAA C   
1368  O O   . GLY A 173 ? 0.788 0.686 0.645 0.060  0.096  -0.072 502 GLY AAA O   
1369  N N   . VAL A 174 ? 0.779 0.629 0.608 0.043  0.085  -0.096 503 VAL AAA N   
1370  C CA  . VAL A 174 ? 0.775 0.631 0.621 0.027  0.074  -0.085 503 VAL AAA CA  
1371  C C   . VAL A 174 ? 0.722 0.614 0.577 0.022  0.071  -0.071 503 VAL AAA C   
1372  O O   . VAL A 174 ? 0.704 0.609 0.578 0.017  0.067  -0.058 503 VAL AAA O   
1373  C CB  . VAL A 174 ? 0.811 0.644 0.647 0.011  0.063  -0.096 503 VAL AAA CB  
1374  C CG1 . VAL A 174 ? 0.821 0.664 0.674 -0.004 0.054  -0.085 503 VAL AAA CG1 
1375  C CG2 . VAL A 174 ? 0.826 0.619 0.655 0.014  0.066  -0.108 503 VAL AAA CG2 
1376  N N   . GLY A 175 ? 0.719 0.627 0.560 0.021  0.072  -0.075 504 GLY AAA N   
1377  C CA  . GLY A 175 ? 0.682 0.621 0.529 0.015  0.070  -0.062 504 GLY AAA CA  
1378  C C   . GLY A 175 ? 0.684 0.648 0.551 0.023  0.077  -0.047 504 GLY AAA C   
1379  O O   . GLY A 175 ? 0.697 0.681 0.576 0.015  0.073  -0.035 504 GLY AAA O   
1380  N N   . TYR A 176 ? 0.694 0.655 0.567 0.039  0.087  -0.049 505 TYR AAA N   
1381  C CA  . TYR A 176 ? 0.701 0.690 0.596 0.048  0.094  -0.035 505 TYR AAA CA  
1382  C C   . TYR A 176 ? 0.644 0.623 0.557 0.051  0.089  -0.029 505 TYR AAA C   
1383  O O   . TYR A 176 ? 0.632 0.632 0.565 0.060  0.092  -0.018 505 TYR AAA O   
1384  C CB  . TYR A 176 ? 0.752 0.751 0.642 0.066  0.109  -0.039 505 TYR AAA CB  
1385  C CG  . TYR A 176 ? 0.843 0.857 0.714 0.064  0.115  -0.042 505 TYR AAA CG  
1386  C CD1 . TYR A 176 ? 0.915 0.907 0.756 0.062  0.115  -0.059 505 TYR AAA CD1 
1387  C CD2 . TYR A 176 ? 0.903 0.955 0.787 0.062  0.121  -0.028 505 TYR AAA CD2 
1388  C CE1 . TYR A 176 ? 0.979 0.984 0.800 0.061  0.120  -0.060 505 TYR AAA CE1 
1389  C CE2 . TYR A 176 ? 0.950 1.016 0.816 0.060  0.128  -0.029 505 TYR AAA CE2 
1390  C CZ  . TYR A 176 ? 0.985 1.027 0.818 0.060  0.128  -0.045 505 TYR AAA CZ  
1391  O OH  . TYR A 176 ? 1.041 1.096 0.852 0.059  0.134  -0.044 505 TYR AAA OH  
1392  N N   . GLN A 177 ? 0.634 0.583 0.541 0.044  0.081  -0.034 506 GLN AAA N   
1393  C CA  . GLN A 177 ? 0.636 0.574 0.556 0.045  0.076  -0.027 506 GLN AAA CA  
1394  C C   . GLN A 177 ? 0.589 0.546 0.522 0.032  0.067  -0.014 506 GLN AAA C   
1395  O O   . GLN A 177 ? 0.552 0.518 0.481 0.020  0.061  -0.015 506 GLN AAA O   
1396  C CB  . GLN A 177 ? 0.646 0.545 0.555 0.042  0.074  -0.036 506 GLN AAA CB  
1397  C CG  . GLN A 177 ? 0.670 0.546 0.570 0.057  0.083  -0.047 506 GLN AAA CG  
1398  C CD  . GLN A 177 ? 0.680 0.514 0.566 0.051  0.081  -0.058 506 GLN AAA CD  
1399  O OE1 . GLN A 177 ? 0.657 0.482 0.548 0.038  0.073  -0.054 506 GLN AAA OE1 
1400  N NE2 . GLN A 177 ? 0.705 0.515 0.576 0.059  0.087  -0.073 506 GLN AAA NE2 
1401  N N   . PRO A 178 ? 0.589 0.551 0.536 0.035  0.063  -0.004 507 PRO AAA N   
1402  C CA  . PRO A 178 ? 0.574 0.549 0.530 0.024  0.053  0.006  507 PRO AAA CA  
1403  C C   . PRO A 178 ? 0.569 0.523 0.515 0.011  0.047  0.002  507 PRO AAA C   
1404  O O   . PRO A 178 ? 0.584 0.512 0.523 0.013  0.048  -0.004 507 PRO AAA O   
1405  C CB  . PRO A 178 ? 0.582 0.566 0.552 0.033  0.051  0.017  507 PRO AAA CB  
1406  C CG  . PRO A 178 ? 0.612 0.570 0.577 0.047  0.058  0.012  507 PRO AAA CG  
1407  C CD  . PRO A 178 ? 0.616 0.567 0.570 0.051  0.067  -0.000 507 PRO AAA CD  
1408  N N   . TYR A 179 ? 0.548 0.512 0.494 -0.002 0.040  0.004  508 TYR AAA N   
1409  C CA  . TYR A 179 ? 0.535 0.485 0.475 -0.013 0.033  0.002  508 TYR AAA CA  
1410  C C   . TYR A 179 ? 0.528 0.491 0.475 -0.018 0.026  0.012  508 TYR AAA C   
1411  O O   . TYR A 179 ? 0.539 0.522 0.493 -0.020 0.023  0.017  508 TYR AAA O   
1412  C CB  . TYR A 179 ? 0.538 0.488 0.470 -0.021 0.032  -0.006 508 TYR AAA CB  
1413  C CG  . TYR A 179 ? 0.571 0.501 0.493 -0.020 0.036  -0.018 508 TYR AAA CG  
1414  C CD1 . TYR A 179 ? 0.587 0.515 0.504 -0.010 0.043  -0.023 508 TYR AAA CD1 
1415  C CD2 . TYR A 179 ? 0.573 0.489 0.491 -0.029 0.032  -0.024 508 TYR AAA CD2 
1416  C CE1 . TYR A 179 ? 0.619 0.526 0.523 -0.009 0.046  -0.036 508 TYR AAA CE1 
1417  C CE2 . TYR A 179 ? 0.604 0.502 0.513 -0.030 0.034  -0.036 508 TYR AAA CE2 
1418  C CZ  . TYR A 179 ? 0.639 0.531 0.541 -0.020 0.040  -0.042 508 TYR AAA CZ  
1419  O OH  . TYR A 179 ? 0.670 0.541 0.561 -0.022 0.041  -0.056 508 TYR AAA OH  
1420  N N   . ARG A 180 ? 0.533 0.483 0.478 -0.020 0.023  0.014  509 ARG AAA N   
1421  C CA  . ARG A 180 ? 0.501 0.457 0.447 -0.025 0.016  0.020  509 ARG AAA CA  
1422  C C   . ARG A 180 ? 0.495 0.447 0.435 -0.035 0.013  0.015  509 ARG AAA C   
1423  O O   . ARG A 180 ? 0.494 0.436 0.431 -0.038 0.016  0.008  509 ARG AAA O   
1424  C CB  . ARG A 180 ? 0.514 0.458 0.456 -0.021 0.016  0.025  509 ARG AAA CB  
1425  C CG  . ARG A 180 ? 0.514 0.464 0.463 -0.010 0.016  0.033  509 ARG AAA CG  
1426  C CD  . ARG A 180 ? 0.518 0.455 0.461 -0.005 0.015  0.039  509 ARG AAA CD  
1427  N NE  . ARG A 180 ? 0.517 0.464 0.469 0.007  0.015  0.047  509 ARG AAA NE  
1428  C CZ  . ARG A 180 ? 0.525 0.468 0.473 0.014  0.012  0.057  509 ARG AAA CZ  
1429  N NH1 . ARG A 180 ? 0.529 0.457 0.464 0.010  0.010  0.059  509 ARG AAA NH1 
1430  N NH2 . ARG A 180 ? 0.516 0.472 0.475 0.027  0.010  0.064  509 ARG AAA NH2 
1431  N N   . VAL A 181 ? 0.506 0.469 0.448 -0.040 0.006  0.018  510 VAL AAA N   
1432  C CA  . VAL A 181 ? 0.510 0.470 0.447 -0.048 0.003  0.015  510 VAL AAA CA  
1433  C C   . VAL A 181 ? 0.509 0.465 0.441 -0.050 -0.003 0.017  510 VAL AAA C   
1434  O O   . VAL A 181 ? 0.501 0.465 0.436 -0.050 -0.007 0.023  510 VAL AAA O   
1435  C CB  . VAL A 181 ? 0.520 0.492 0.459 -0.051 0.001  0.016  510 VAL AAA CB  
1436  C CG1 . VAL A 181 ? 0.505 0.472 0.440 -0.057 -0.003 0.013  510 VAL AAA CG1 
1437  C CG2 . VAL A 181 ? 0.550 0.527 0.490 -0.047 0.007  0.013  510 VAL AAA CG2 
1438  N N   . VAL A 182 ? 0.500 0.448 0.428 -0.053 -0.003 0.013  511 VAL AAA N   
1439  C CA  . VAL A 182 ? 0.483 0.426 0.403 -0.055 -0.007 0.013  511 VAL AAA CA  
1440  C C   . VAL A 182 ? 0.490 0.432 0.410 -0.058 -0.009 0.009  511 VAL AAA C   
1441  O O   . VAL A 182 ? 0.492 0.433 0.415 -0.057 -0.005 0.006  511 VAL AAA O   
1442  C CB  . VAL A 182 ? 0.506 0.440 0.419 -0.052 -0.002 0.014  511 VAL AAA CB  
1443  C CG1 . VAL A 182 ? 0.510 0.439 0.413 -0.053 -0.005 0.012  511 VAL AAA CG1 
1444  C CG2 . VAL A 182 ? 0.517 0.451 0.429 -0.048 -0.001 0.020  511 VAL AAA CG2 
1445  N N   . VAL A 183 ? 0.510 0.450 0.426 -0.060 -0.016 0.010  512 VAL AAA N   
1446  C CA  . VAL A 183 ? 0.515 0.448 0.428 -0.061 -0.019 0.007  512 VAL AAA CA  
1447  C C   . VAL A 183 ? 0.534 0.457 0.437 -0.059 -0.020 0.004  512 VAL AAA C   
1448  O O   . VAL A 183 ? 0.521 0.440 0.417 -0.062 -0.025 0.005  512 VAL AAA O   
1449  C CB  . VAL A 183 ? 0.515 0.450 0.430 -0.066 -0.024 0.011  512 VAL AAA CB  
1450  C CG1 . VAL A 183 ? 0.502 0.427 0.413 -0.066 -0.027 0.010  512 VAL AAA CG1 
1451  C CG2 . VAL A 183 ? 0.514 0.462 0.436 -0.067 -0.021 0.015  512 VAL AAA CG2 
1452  N N   . LEU A 184 ? 0.543 0.462 0.445 -0.055 -0.016 0.000  513 LEU AAA N   
1453  C CA  . LEU A 184 ? 0.561 0.470 0.453 -0.051 -0.016 -0.004 513 LEU AAA CA  
1454  C C   . LEU A 184 ? 0.570 0.471 0.460 -0.049 -0.021 -0.006 513 LEU AAA C   
1455  O O   . LEU A 184 ? 0.583 0.489 0.482 -0.047 -0.019 -0.006 513 LEU AAA O   
1456  C CB  . LEU A 184 ? 0.567 0.482 0.462 -0.046 -0.006 -0.006 513 LEU AAA CB  
1457  C CG  . LEU A 184 ? 0.566 0.486 0.461 -0.048 -0.001 -0.002 513 LEU AAA CG  
1458  C CD1 . LEU A 184 ? 0.575 0.500 0.476 -0.046 0.009  -0.003 513 LEU AAA CD1 
1459  C CD2 . LEU A 184 ? 0.612 0.525 0.492 -0.047 -0.004 -0.001 513 LEU AAA CD2 
1460  N N   . SER A 185 ? 0.600 0.485 0.478 -0.051 -0.027 -0.008 514 SER AAA N   
1461  C CA  . SER A 185 ? 0.633 0.502 0.506 -0.050 -0.033 -0.010 514 SER AAA CA  
1462  C C   . SER A 185 ? 0.667 0.524 0.529 -0.040 -0.029 -0.018 514 SER AAA C   
1463  O O   . SER A 185 ? 0.694 0.546 0.542 -0.040 -0.028 -0.022 514 SER AAA O   
1464  C CB  . SER A 185 ? 0.661 0.519 0.528 -0.059 -0.042 -0.008 514 SER AAA CB  
1465  O OG  . SER A 185 ? 0.800 0.667 0.678 -0.065 -0.044 -0.001 514 SER AAA OG  
1466  N N   . PHE A 186 ? 0.648 0.502 0.514 -0.032 -0.027 -0.020 515 PHE AAA N   
1467  C CA  . PHE A 186 ? 0.655 0.499 0.511 -0.020 -0.021 -0.028 515 PHE AAA CA  
1468  C C   . PHE A 186 ? 0.694 0.512 0.541 -0.017 -0.029 -0.030 515 PHE AAA C   
1469  O O   . PHE A 186 ? 0.728 0.543 0.583 -0.017 -0.033 -0.025 515 PHE AAA O   
1470  C CB  . PHE A 186 ? 0.643 0.507 0.516 -0.011 -0.013 -0.027 515 PHE AAA CB  
1471  C CG  . PHE A 186 ? 0.611 0.498 0.495 -0.016 -0.006 -0.024 515 PHE AAA CG  
1472  C CD1 . PHE A 186 ? 0.595 0.483 0.471 -0.022 -0.003 -0.023 515 PHE AAA CD1 
1473  C CD2 . PHE A 186 ? 0.622 0.530 0.527 -0.015 -0.003 -0.021 515 PHE AAA CD2 
1474  C CE1 . PHE A 186 ? 0.570 0.476 0.457 -0.026 0.003  -0.019 515 PHE AAA CE1 
1475  C CE2 . PHE A 186 ? 0.600 0.526 0.516 -0.020 0.003  -0.019 515 PHE AAA CE2 
1476  C CZ  . PHE A 186 ? 0.558 0.481 0.465 -0.026 0.007  -0.017 515 PHE AAA CZ  
1477  N N   . GLU A 187 ? 0.749 0.545 0.575 -0.015 -0.031 -0.038 516 GLU AAA N   
1478  C CA  . GLU A 187 ? 0.731 0.494 0.544 -0.010 -0.037 -0.044 516 GLU AAA CA  
1479  C C   . GLU A 187 ? 0.735 0.493 0.542 0.008  -0.028 -0.052 516 GLU AAA C   
1480  O O   . GLU A 187 ? 0.718 0.486 0.518 0.014  -0.019 -0.057 516 GLU AAA O   
1481  C CB  . GLU A 187 ? 0.782 0.523 0.575 -0.021 -0.046 -0.049 516 GLU AAA CB  
1482  C CG  . GLU A 187 ? 0.807 0.544 0.606 -0.038 -0.057 -0.042 516 GLU AAA CG  
1483  C CD  . GLU A 187 ? 0.881 0.604 0.665 -0.050 -0.067 -0.046 516 GLU AAA CD  
1484  O OE1 . GLU A 187 ? 0.926 0.626 0.687 -0.046 -0.069 -0.059 516 GLU AAA OE1 
1485  O OE2 . GLU A 187 ? 0.939 0.677 0.733 -0.065 -0.073 -0.039 516 GLU AAA OE2 
1486  N N   . LEU A 188 ? 0.723 0.463 0.531 0.018  -0.030 -0.052 517 LEU AAA N   
1487  C CA  . LEU A 188 ? 0.713 0.442 0.515 0.038  -0.023 -0.061 517 LEU AAA CA  
1488  C C   . LEU A 188 ? 0.732 0.414 0.513 0.041  -0.031 -0.068 517 LEU AAA C   
1489  O O   . LEU A 188 ? 0.741 0.410 0.528 0.051  -0.034 -0.064 517 LEU AAA O   
1490  C CB  . LEU A 188 ? 0.693 0.447 0.520 0.050  -0.018 -0.054 517 LEU AAA CB  
1491  C CG  . LEU A 188 ? 0.678 0.474 0.525 0.050  -0.007 -0.051 517 LEU AAA CG  
1492  C CD1 . LEU A 188 ? 0.637 0.460 0.511 0.057  -0.006 -0.044 517 LEU AAA CD1 
1493  C CD2 . LEU A 188 ? 0.703 0.503 0.540 0.062  0.006  -0.061 517 LEU AAA CD2 
1494  N N   . LEU A 189 ? 0.725 0.382 0.481 0.033  -0.036 -0.077 518 LEU AAA N   
1495  C CA  . LEU A 189 ? 0.779 0.388 0.513 0.033  -0.045 -0.085 518 LEU AAA CA  
1496  C C   . LEU A 189 ? 0.820 0.406 0.533 0.054  -0.038 -0.100 518 LEU AAA C   
1497  O O   . LEU A 189 ? 0.795 0.407 0.514 0.068  -0.024 -0.103 518 LEU AAA O   
1498  C CB  . LEU A 189 ? 0.791 0.386 0.510 0.011  -0.057 -0.088 518 LEU AAA CB  
1499  C CG  . LEU A 189 ? 0.756 0.376 0.496 -0.009 -0.064 -0.073 518 LEU AAA CG  
1500  C CD1 . LEU A 189 ? 0.772 0.377 0.498 -0.029 -0.076 -0.077 518 LEU AAA CD1 
1501  C CD2 . LEU A 189 ? 0.749 0.365 0.506 -0.010 -0.067 -0.061 518 LEU AAA CD2 
1502  N N   . HIS A 190 ? 0.865 0.403 0.557 0.056  -0.045 -0.110 519 HIS AAA N   
1503  C CA  . HIS A 190 ? 0.918 0.425 0.584 0.077  -0.039 -0.127 519 HIS AAA CA  
1504  C C   . HIS A 190 ? 0.943 0.442 0.580 0.069  -0.040 -0.140 519 HIS AAA C   
1505  O O   . HIS A 190 ? 0.998 0.454 0.608 0.061  -0.051 -0.152 519 HIS AAA O   
1506  C CB  . HIS A 190 ? 0.970 0.428 0.628 0.082  -0.047 -0.129 519 HIS AAA CB  
1507  C CG  . HIS A 190 ? 0.949 0.427 0.639 0.088  -0.046 -0.111 519 HIS AAA CG  
1508  N ND1 . HIS A 190 ? 0.938 0.450 0.649 0.110  -0.033 -0.107 519 HIS AAA ND1 
1509  C CD2 . HIS A 190 ? 0.949 0.419 0.653 0.076  -0.056 -0.096 519 HIS AAA CD2 
1510  C CE1 . HIS A 190 ? 0.933 0.453 0.666 0.111  -0.038 -0.092 519 HIS AAA CE1 
1511  N NE2 . HIS A 190 ? 0.934 0.427 0.661 0.091  -0.051 -0.085 519 HIS AAA NE2 
1512  N N   . ALA A 191 ? 0.925 0.464 0.566 0.071  -0.029 -0.139 520 ALA AAA N   
1513  C CA  . ALA A 191 ? 0.949 0.493 0.565 0.063  -0.030 -0.147 520 ALA AAA CA  
1514  C C   . ALA A 191 ? 0.939 0.522 0.561 0.077  -0.011 -0.145 520 ALA AAA C   
1515  O O   . ALA A 191 ? 0.893 0.507 0.545 0.085  -0.001 -0.135 520 ALA AAA O   
1516  C CB  . ALA A 191 ? 0.921 0.478 0.546 0.037  -0.044 -0.137 520 ALA AAA CB  
1517  N N   . PRO A 192 ? 0.956 0.540 0.549 0.079  -0.006 -0.154 521 PRO AAA N   
1518  C CA  . PRO A 192 ? 0.950 0.574 0.550 0.087  0.012  -0.149 521 PRO AAA CA  
1519  C C   . PRO A 192 ? 0.890 0.555 0.525 0.072  0.012  -0.130 521 PRO AAA C   
1520  O O   . PRO A 192 ? 0.864 0.528 0.504 0.054  -0.003 -0.124 521 PRO AAA O   
1521  C CB  . PRO A 192 ? 0.990 0.602 0.548 0.086  0.012  -0.160 521 PRO AAA CB  
1522  C CG  . PRO A 192 ? 1.057 0.617 0.583 0.089  0.000  -0.179 521 PRO AAA CG  
1523  C CD  . PRO A 192 ? 1.031 0.578 0.582 0.074  -0.016 -0.171 521 PRO AAA CD  
1524  N N   . ALA A 193 ? 0.852 0.554 0.512 0.081  0.028  -0.122 522 ALA AAA N   
1525  C CA  . ALA A 193 ? 0.833 0.573 0.520 0.069  0.031  -0.106 522 ALA AAA CA  
1526  C C   . ALA A 193 ? 0.830 0.574 0.493 0.060  0.030  -0.105 522 ALA AAA C   
1527  O O   . ALA A 193 ? 0.860 0.596 0.494 0.070  0.039  -0.114 522 ALA AAA O   
1528  C CB  . ALA A 193 ? 0.813 0.587 0.528 0.080  0.048  -0.099 522 ALA AAA CB  
1529  N N   . THR A 194 ? 0.817 0.573 0.491 0.043  0.021  -0.095 523 THR AAA N   
1530  C CA  . THR A 194 ? 0.837 0.599 0.492 0.035  0.019  -0.092 523 THR AAA CA  
1531  C C   . THR A 194 ? 0.784 0.580 0.464 0.030  0.029  -0.076 523 THR AAA C   
1532  O O   . THR A 194 ? 0.783 0.588 0.450 0.028  0.033  -0.071 523 THR AAA O   
1533  C CB  . THR A 194 ? 0.867 0.610 0.508 0.021  -0.002 -0.094 523 THR AAA CB  
1534  O OG1 . THR A 194 ? 0.815 0.571 0.488 0.008  -0.010 -0.083 523 THR AAA OG1 
1535  C CG2 . THR A 194 ? 0.893 0.599 0.513 0.023  -0.012 -0.109 523 THR AAA CG2 
1536  N N   . VAL A 195 ? 0.748 0.561 0.464 0.028  0.031  -0.069 524 VAL AAA N   
1537  C CA  . VAL A 195 ? 0.727 0.570 0.469 0.022  0.039  -0.056 524 VAL AAA CA  
1538  C C   . VAL A 195 ? 0.718 0.580 0.484 0.031  0.054  -0.054 524 VAL AAA C   
1539  O O   . VAL A 195 ? 0.712 0.573 0.496 0.034  0.049  -0.057 524 VAL AAA O   
1540  C CB  . VAL A 195 ? 0.728 0.575 0.491 0.008  0.027  -0.048 524 VAL AAA CB  
1541  C CG1 . VAL A 195 ? 0.684 0.557 0.473 0.003  0.034  -0.037 524 VAL AAA CG1 
1542  C CG2 . VAL A 195 ? 0.743 0.576 0.487 -0.001 0.013  -0.048 524 VAL AAA CG2 
1543  N N   . CYS A 196 ? 0.738 0.620 0.508 0.034  0.070  -0.049 525 CYS AAA N   
1544  C CA  . CYS A 196 ? 0.727 0.638 0.529 0.040  0.084  -0.045 525 CYS AAA CA  
1545  C C   . CYS A 196 ? 0.707 0.640 0.529 0.028  0.091  -0.033 525 CYS AAA C   
1546  O O   . CYS A 196 ? 0.684 0.611 0.488 0.021  0.091  -0.028 525 CYS AAA O   
1547  C CB  . CYS A 196 ? 0.763 0.677 0.552 0.056  0.100  -0.052 525 CYS AAA CB  
1548  S SG  . CYS A 196 ? 0.848 0.734 0.619 0.073  0.094  -0.068 525 CYS AAA SG  
1549  N N   . GLY A 197 ? 0.684 0.641 0.541 0.026  0.095  -0.029 526 GLY AAA N   
1550  C CA  . GLY A 197 ? 0.684 0.664 0.562 0.015  0.105  -0.018 526 GLY AAA CA  
1551  C C   . GLY A 197 ? 0.703 0.696 0.573 0.020  0.125  -0.014 526 GLY AAA C   
1552  O O   . GLY A 197 ? 0.735 0.724 0.588 0.034  0.133  -0.021 526 GLY AAA O   
1553  N N   . PRO A 198 ? 0.751 0.759 0.634 0.010  0.135  -0.003 527 PRO AAA N   
1554  C CA  . PRO A 198 ? 0.836 0.859 0.715 0.013  0.157  0.003  527 PRO AAA CA  
1555  C C   . PRO A 198 ? 0.933 0.983 0.832 0.025  0.171  -0.002 527 PRO AAA C   
1556  O O   . PRO A 198 ? 1.017 1.075 0.901 0.034  0.188  -0.000 527 PRO AAA O   
1557  C CB  . PRO A 198 ? 0.784 0.821 0.687 -0.004 0.162  0.015  527 PRO AAA CB  
1558  C CG  . PRO A 198 ? 0.752 0.767 0.650 -0.014 0.144  0.016  527 PRO AAA CG  
1559  C CD  . PRO A 198 ? 0.730 0.737 0.629 -0.006 0.128  0.004  527 PRO AAA CD  
1569  N N   . GLN B 1   ? 0.639 0.766 0.737 -0.056 0.064  -0.048 1   GLN BBB N   
1570  C CA  . GLN B 1   ? 0.660 0.775 0.740 -0.042 0.069  -0.053 1   GLN BBB CA  
1571  C C   . GLN B 1   ? 0.629 0.711 0.670 -0.039 0.059  -0.051 1   GLN BBB C   
1572  O O   . GLN B 1   ? 0.706 0.766 0.721 -0.047 0.061  -0.045 1   GLN BBB O   
1573  C CB  . GLN B 1   ? 0.785 0.909 0.861 -0.046 0.090  -0.057 1   GLN BBB CB  
1574  C CG  . GLN B 1   ? 0.904 1.014 0.955 -0.035 0.095  -0.065 1   GLN BBB CG  
1575  C CD  . GLN B 1   ? 0.968 1.086 1.040 -0.020 0.092  -0.074 1   GLN BBB CD  
1576  O OE1 . GLN B 1   ? 0.957 1.092 1.066 -0.014 0.087  -0.073 1   GLN BBB OE1 
1577  N NE2 . GLN B 1   ? 0.980 1.083 1.027 -0.015 0.096  -0.082 1   GLN BBB NE2 
1578  N N   . VAL B 2   ? 0.565 0.643 0.605 -0.026 0.050  -0.054 2   VAL BBB N   
1579  C CA  . VAL B 2   ? 0.537 0.594 0.547 -0.020 0.043  -0.053 2   VAL BBB CA  
1580  C C   . VAL B 2   ? 0.544 0.604 0.545 -0.014 0.047  -0.059 2   VAL BBB C   
1581  O O   . VAL B 2   ? 0.527 0.599 0.547 -0.010 0.050  -0.066 2   VAL BBB O   
1582  C CB  . VAL B 2   ? 0.530 0.586 0.547 -0.013 0.030  -0.054 2   VAL BBB CB  
1583  C CG1 . VAL B 2   ? 0.508 0.554 0.506 -0.004 0.023  -0.053 2   VAL BBB CG1 
1584  C CG2 . VAL B 2   ? 0.538 0.590 0.560 -0.021 0.025  -0.051 2   VAL BBB CG2 
1585  N N   . GLN B 3   ? 0.518 0.564 0.488 -0.014 0.046  -0.057 3   GLN BBB N   
1586  C CA  . GLN B 3   ? 0.510 0.557 0.464 -0.011 0.046  -0.063 3   GLN BBB CA  
1587  C C   . GLN B 3   ? 0.527 0.573 0.477 -0.003 0.030  -0.062 3   GLN BBB C   
1588  O O   . GLN B 3   ? 0.462 0.501 0.409 0.001  0.022  -0.054 3   GLN BBB O   
1589  C CB  . GLN B 3   ? 0.537 0.576 0.459 -0.018 0.055  -0.062 3   GLN BBB CB  
1590  C CG  . GLN B 3   ? 0.526 0.574 0.458 -0.025 0.076  -0.067 3   GLN BBB CG  
1591  C CD  . GLN B 3   ? 0.547 0.587 0.440 -0.034 0.088  -0.068 3   GLN BBB CD  
1592  O OE1 . GLN B 3   ? 0.549 0.586 0.418 -0.033 0.087  -0.075 3   GLN BBB OE1 
1593  N NE2 . GLN B 3   ? 0.562 0.600 0.448 -0.045 0.100  -0.060 3   GLN BBB NE2 
1594  N N   . LEU B 4   ? 0.550 0.604 0.501 -0.003 0.027  -0.071 4   LEU BBB N   
1595  C CA  . LEU B 4   ? 0.531 0.594 0.486 0.001  0.013  -0.071 4   LEU BBB CA  
1596  C C   . LEU B 4   ? 0.561 0.626 0.493 -0.004 0.009  -0.078 4   LEU BBB C   
1597  O O   . LEU B 4   ? 0.559 0.619 0.485 -0.010 0.019  -0.089 4   LEU BBB O   
1598  C CB  . LEU B 4   ? 0.536 0.607 0.520 0.001  0.013  -0.076 4   LEU BBB CB  
1599  C CG  . LEU B 4   ? 0.519 0.589 0.522 0.004  0.016  -0.071 4   LEU BBB CG  
1600  C CD1 . LEU B 4   ? 0.500 0.575 0.525 0.003  0.016  -0.074 4   LEU BBB CD1 
1601  C CD2 . LEU B 4   ? 0.499 0.569 0.498 0.009  0.009  -0.064 4   LEU BBB CD2 
1602  N N   . VAL B 5   ? 0.607 0.680 0.528 -0.000 -0.006 -0.072 5   VAL BBB N   
1603  C CA  . VAL B 5   ? 0.613 0.693 0.511 -0.007 -0.015 -0.078 5   VAL BBB CA  
1604  C C   . VAL B 5   ? 0.602 0.706 0.519 -0.005 -0.032 -0.078 5   VAL BBB C   
1605  O O   . VAL B 5   ? 0.588 0.703 0.516 0.006  -0.041 -0.066 5   VAL BBB O   
1606  C CB  . VAL B 5   ? 0.643 0.713 0.502 -0.007 -0.019 -0.068 5   VAL BBB CB  
1607  C CG1 . VAL B 5   ? 0.686 0.768 0.520 -0.015 -0.035 -0.072 5   VAL BBB CG1 
1608  C CG2 . VAL B 5   ? 0.665 0.716 0.505 -0.014 0.000  -0.071 5   VAL BBB CG2 
1609  N N   . GLU B 6   ? 0.601 0.713 0.525 -0.017 -0.033 -0.091 6   GLU BBB N   
1610  C CA  . GLU B 6   ? 0.589 0.728 0.531 -0.022 -0.048 -0.093 6   GLU BBB CA  
1611  C C   . GLU B 6   ? 0.619 0.775 0.538 -0.026 -0.066 -0.091 6   GLU BBB C   
1612  O O   . GLU B 6   ? 0.621 0.759 0.501 -0.032 -0.064 -0.095 6   GLU BBB O   
1613  C CB  . GLU B 6   ? 0.587 0.721 0.538 -0.037 -0.042 -0.107 6   GLU BBB CB  
1614  C CG  . GLU B 6   ? 0.558 0.673 0.528 -0.034 -0.026 -0.108 6   GLU BBB CG  
1615  C CD  . GLU B 6   ? 0.551 0.636 0.506 -0.033 -0.010 -0.115 6   GLU BBB CD  
1616  O OE1 . GLU B 6   ? 0.585 0.663 0.513 -0.033 -0.008 -0.118 6   GLU BBB OE1 
1617  O OE2 . GLU B 6   ? 0.536 0.607 0.509 -0.031 -0.000 -0.117 6   GLU BBB OE2 
1618  N N   . SER B 7   ? 0.634 0.825 0.575 -0.022 -0.083 -0.085 7   SER BBB N   
1619  C CA  . SER B 7   ? 0.639 0.858 0.567 -0.028 -0.106 -0.083 7   SER BBB CA  
1620  C C   . SER B 7   ? 0.649 0.913 0.619 -0.033 -0.118 -0.085 7   SER BBB C   
1621  O O   . SER B 7   ? 0.652 0.922 0.656 -0.030 -0.106 -0.085 7   SER BBB O   
1622  C CB  . SER B 7   ? 0.633 0.851 0.544 -0.010 -0.117 -0.064 7   SER BBB CB  
1623  O OG  . SER B 7   ? 0.587 0.816 0.533 0.011  -0.116 -0.053 7   SER BBB OG  
1624  N N   . GLY B 8   ? 0.666 0.963 0.632 -0.044 -0.140 -0.086 8   GLY BBB N   
1625  C CA  . GLY B 8   ? 0.671 1.021 0.680 -0.051 -0.154 -0.087 8   GLY BBB CA  
1626  C C   . GLY B 8   ? 0.685 1.036 0.697 -0.082 -0.152 -0.105 8   GLY BBB C   
1627  O O   . GLY B 8   ? 0.700 1.097 0.750 -0.093 -0.160 -0.107 8   GLY BBB O   
1628  N N   . GLY B 9   ? 0.725 1.028 0.700 -0.097 -0.139 -0.119 9   GLY BBB N   
1629  C CA  . GLY B 9   ? 0.724 1.015 0.694 -0.127 -0.136 -0.138 9   GLY BBB CA  
1630  C C   . GLY B 9   ? 0.763 1.076 0.711 -0.150 -0.160 -0.148 9   GLY BBB C   
1631  O O   . GLY B 9   ? 0.779 1.124 0.720 -0.141 -0.181 -0.137 9   GLY BBB O   
1632  N N   . GLY B 10  ? 0.768 1.061 0.701 -0.181 -0.158 -0.168 10  GLY BBB N   
1633  C CA  . GLY B 10  ? 0.806 1.114 0.711 -0.209 -0.181 -0.182 10  GLY BBB CA  
1634  C C   . GLY B 10  ? 0.819 1.150 0.752 -0.241 -0.188 -0.194 10  GLY BBB C   
1635  O O   . GLY B 10  ? 0.789 1.107 0.753 -0.244 -0.170 -0.194 10  GLY BBB O   
1636  N N   . LEU B 11  ? 0.852 1.218 0.773 -0.267 -0.215 -0.202 11  LEU BBB N   
1637  C CA  . LEU B 11  ? 0.885 1.275 0.827 -0.307 -0.226 -0.216 11  LEU BBB CA  
1638  C C   . LEU B 11  ? 0.842 1.313 0.855 -0.301 -0.239 -0.197 11  LEU BBB C   
1639  O O   . LEU B 11  ? 0.824 1.342 0.854 -0.275 -0.255 -0.179 11  LEU BBB O   
1640  C CB  . LEU B 11  ? 0.961 1.353 0.854 -0.337 -0.252 -0.234 11  LEU BBB CB  
1641  C CG  . LEU B 11  ? 1.012 1.427 0.917 -0.385 -0.267 -0.251 11  LEU BBB CG  
1642  C CD1 . LEU B 11  ? 1.027 1.380 0.935 -0.404 -0.239 -0.267 11  LEU BBB CD1 
1643  C CD2 . LEU B 11  ? 1.079 1.491 0.926 -0.415 -0.293 -0.271 11  LEU BBB CD2 
1644  N N   . VAL B 12  ? 0.840 1.325 0.893 -0.324 -0.230 -0.201 12  VAL BBB N   
1645  C CA  . VAL B 12  ? 0.811 1.381 0.935 -0.324 -0.239 -0.187 12  VAL BBB CA  
1646  C C   . VAL B 12  ? 0.854 1.432 0.998 -0.371 -0.237 -0.200 12  VAL BBB C   
1647  O O   . VAL B 12  ? 0.870 1.374 0.981 -0.390 -0.218 -0.214 12  VAL BBB O   
1648  C CB  . VAL B 12  ? 0.756 1.332 0.915 -0.285 -0.217 -0.167 12  VAL BBB CB  
1649  C CG1 . VAL B 12  ? 0.746 1.263 0.901 -0.291 -0.185 -0.171 12  VAL BBB CG1 
1650  C CG2 . VAL B 12  ? 0.715 1.382 0.944 -0.274 -0.226 -0.152 12  VAL BBB CG2 
1651  N N   . GLN B 13  ? 0.879 1.544 1.076 -0.390 -0.257 -0.196 13  GLN BBB N   
1652  C CA  . GLN B 13  ? 0.891 1.576 1.115 -0.440 -0.257 -0.207 13  GLN BBB CA  
1653  C C   . GLN B 13  ? 0.856 1.538 1.119 -0.434 -0.225 -0.196 13  GLN BBB C   
1654  O O   . GLN B 13  ? 0.824 1.536 1.119 -0.394 -0.214 -0.178 13  GLN BBB O   
1655  C CB  . GLN B 13  ? 0.899 1.688 1.168 -0.461 -0.291 -0.206 13  GLN BBB CB  
1656  C CG  . GLN B 13  ? 0.979 1.760 1.204 -0.501 -0.322 -0.226 13  GLN BBB CG  
1657  C CD  . GLN B 13  ? 1.011 1.870 1.283 -0.550 -0.343 -0.233 13  GLN BBB CD  
1658  O OE1 . GLN B 13  ? 1.026 1.875 1.319 -0.587 -0.326 -0.241 13  GLN BBB OE1 
1659  N NE2 . GLN B 13  ? 1.024 1.963 1.313 -0.555 -0.383 -0.230 13  GLN BBB NE2 
1660  N N   . ALA B 14  ? 0.875 1.515 1.130 -0.474 -0.210 -0.207 14  ALA BBB N   
1661  C CA  . ALA B 14  ? 0.843 1.483 1.132 -0.482 -0.182 -0.196 14  ALA BBB CA  
1662  C C   . ALA B 14  ? 0.790 1.540 1.154 -0.471 -0.184 -0.181 14  ALA BBB C   
1663  O O   . ALA B 14  ? 0.751 1.580 1.148 -0.483 -0.211 -0.183 14  ALA BBB O   
1664  C CB  . ALA B 14  ? 0.890 1.488 1.165 -0.537 -0.176 -0.209 14  ALA BBB CB  
1665  N N   . GLY B 15  ? 0.760 1.515 1.149 -0.446 -0.158 -0.166 15  GLY BBB N   
1666  C CA  . GLY B 15  ? 0.727 1.579 1.183 -0.426 -0.153 -0.152 15  GLY BBB CA  
1667  C C   . GLY B 15  ? 0.704 1.584 1.168 -0.372 -0.166 -0.144 15  GLY BBB C   
1668  O O   . GLY B 15  ? 0.699 1.646 1.215 -0.346 -0.157 -0.133 15  GLY BBB O   
1669  N N   . GLY B 16  ? 0.718 1.547 1.130 -0.355 -0.182 -0.148 16  GLY BBB N   
1670  C CA  . GLY B 16  ? 0.689 1.535 1.101 -0.307 -0.196 -0.138 16  GLY BBB CA  
1671  C C   . GLY B 16  ? 0.683 1.479 1.078 -0.267 -0.169 -0.129 16  GLY BBB C   
1672  O O   . GLY B 16  ? 0.662 1.415 1.047 -0.276 -0.142 -0.129 16  GLY BBB O   
1673  N N   . SER B 17  ? 0.691 1.489 1.078 -0.224 -0.179 -0.120 17  SER BBB N   
1674  C CA  . SER B 17  ? 0.647 1.402 1.019 -0.183 -0.158 -0.111 17  SER BBB CA  
1675  C C   . SER B 17  ? 0.659 1.355 0.975 -0.163 -0.169 -0.110 17  SER BBB C   
1676  O O   . SER B 17  ? 0.679 1.390 0.979 -0.169 -0.197 -0.111 17  SER BBB O   
1677  C CB  . SER B 17  ? 0.633 1.451 1.058 -0.149 -0.155 -0.099 17  SER BBB CB  
1678  O OG  . SER B 17  ? 0.642 1.505 1.113 -0.165 -0.134 -0.100 17  SER BBB OG  
1679  N N   . LEU B 18  ? 0.638 1.273 0.925 -0.142 -0.148 -0.107 18  LEU BBB N   
1680  C CA  . LEU B 18  ? 0.640 1.218 0.878 -0.120 -0.151 -0.104 18  LEU BBB CA  
1681  C C   . LEU B 18  ? 0.596 1.150 0.838 -0.088 -0.130 -0.095 18  LEU BBB C   
1682  O O   . LEU B 18  ? 0.548 1.091 0.801 -0.095 -0.108 -0.096 18  LEU BBB O   
1683  C CB  . LEU B 18  ? 0.684 1.195 0.871 -0.143 -0.146 -0.116 18  LEU BBB CB  
1684  C CG  . LEU B 18  ? 0.752 1.260 0.907 -0.164 -0.169 -0.126 18  LEU BBB CG  
1685  C CD1 . LEU B 18  ? 0.781 1.213 0.883 -0.177 -0.157 -0.140 18  LEU BBB CD1 
1686  C CD2 . LEU B 18  ? 0.760 1.294 0.906 -0.141 -0.192 -0.115 18  LEU BBB CD2 
1687  N N   . ARG B 19  ? 0.596 1.137 0.823 -0.058 -0.136 -0.085 19  ARG BBB N   
1688  C CA  . ARG B 19  ? 0.570 1.070 0.785 -0.031 -0.117 -0.079 19  ARG BBB CA  
1689  C C   . ARG B 19  ? 0.589 1.025 0.750 -0.030 -0.116 -0.080 19  ARG BBB C   
1690  O O   . ARG B 19  ? 0.601 1.031 0.739 -0.019 -0.132 -0.074 19  ARG BBB O   
1691  C CB  . ARG B 19  ? 0.556 1.089 0.799 0.003  -0.122 -0.068 19  ARG BBB CB  
1692  C CG  . ARG B 19  ? 0.576 1.077 0.818 0.024  -0.098 -0.066 19  ARG BBB CG  
1693  C CD  . ARG B 19  ? 0.617 1.138 0.881 0.060  -0.102 -0.057 19  ARG BBB CD  
1694  N NE  . ARG B 19  ? 0.684 1.175 0.915 0.073  -0.120 -0.047 19  ARG BBB NE  
1695  C CZ  . ARG B 19  ? 0.737 1.209 0.963 0.105  -0.122 -0.036 19  ARG BBB CZ  
1696  N NH1 . ARG B 19  ? 0.775 1.254 1.029 0.128  -0.107 -0.037 19  ARG BBB NH1 
1697  N NH2 . ARG B 19  ? 0.742 1.184 0.932 0.111  -0.138 -0.026 19  ARG BBB NH2 
1698  N N   . LEU B 20  ? 0.579 0.970 0.721 -0.042 -0.098 -0.087 20  LEU BBB N   
1699  C CA  . LEU B 20  ? 0.575 0.909 0.675 -0.036 -0.090 -0.088 20  LEU BBB CA  
1700  C C   . LEU B 20  ? 0.554 0.874 0.655 -0.009 -0.082 -0.077 20  LEU BBB C   
1701  O O   . LEU B 20  ? 0.493 0.831 0.622 0.002  -0.073 -0.074 20  LEU BBB O   
1702  C CB  . LEU B 20  ? 0.574 0.870 0.663 -0.054 -0.074 -0.096 20  LEU BBB CB  
1703  C CG  . LEU B 20  ? 0.608 0.905 0.693 -0.083 -0.080 -0.109 20  LEU BBB CG  
1704  C CD1 . LEU B 20  ? 0.631 0.876 0.698 -0.093 -0.064 -0.115 20  LEU BBB CD1 
1705  C CD2 . LEU B 20  ? 0.660 0.961 0.720 -0.091 -0.098 -0.115 20  LEU BBB CD2 
1706  N N   . ALA B 21  ? 0.556 0.844 0.625 0.001  -0.085 -0.073 21  ALA BBB N   
1707  C CA  . ALA B 21  ? 0.545 0.806 0.605 0.022  -0.076 -0.064 21  ALA BBB CA  
1708  C C   . ALA B 21  ? 0.560 0.775 0.588 0.015  -0.065 -0.067 21  ALA BBB C   
1709  O O   . ALA B 21  ? 0.615 0.820 0.620 0.001  -0.067 -0.074 21  ALA BBB O   
1710  C CB  . ALA B 21  ? 0.537 0.808 0.595 0.043  -0.090 -0.052 21  ALA BBB CB  
1711  N N   . CYS B 22  ? 0.561 0.753 0.588 0.025  -0.052 -0.064 22  CYS BBB N   
1712  C CA  . CYS B 22  ? 0.579 0.734 0.582 0.020  -0.041 -0.065 22  CYS BBB CA  
1713  C C   . CYS B 22  ? 0.562 0.697 0.558 0.035  -0.037 -0.056 22  CYS BBB C   
1714  O O   . CYS B 22  ? 0.547 0.685 0.560 0.043  -0.033 -0.055 22  CYS BBB O   
1715  C CB  . CYS B 22  ? 0.564 0.711 0.578 0.010  -0.030 -0.072 22  CYS BBB CB  
1716  S SG  . CYS B 22  ? 0.621 0.735 0.622 0.010  -0.017 -0.072 22  CYS BBB SG  
1717  N N   . ILE B 23  ? 0.532 0.644 0.500 0.035  -0.037 -0.050 23  ILE BBB N   
1718  C CA  . ILE B 23  ? 0.539 0.624 0.494 0.045  -0.034 -0.041 23  ILE BBB CA  
1719  C C   . ILE B 23  ? 0.539 0.602 0.485 0.033  -0.019 -0.044 23  ILE BBB C   
1720  O O   . ILE B 23  ? 0.503 0.566 0.439 0.022  -0.015 -0.049 23  ILE BBB O   
1721  C CB  . ILE B 23  ? 0.556 0.633 0.487 0.053  -0.046 -0.028 23  ILE BBB CB  
1722  C CG1 . ILE B 23  ? 0.572 0.616 0.491 0.064  -0.043 -0.017 23  ILE BBB CG1 
1723  C CG2 . ILE B 23  ? 0.568 0.640 0.468 0.039  -0.047 -0.029 23  ILE BBB CG2 
1724  C CD1 . ILE B 23  ? 0.603 0.635 0.499 0.077  -0.058 -0.000 23  ILE BBB CD1 
1725  N N   . ALA B 24  ? 0.558 0.604 0.508 0.036  -0.013 -0.042 24  ALA BBB N   
1726  C CA  . ALA B 24  ? 0.552 0.584 0.501 0.025  -0.001 -0.043 24  ALA BBB CA  
1727  C C   . ALA B 24  ? 0.553 0.556 0.478 0.023  0.002  -0.034 24  ALA BBB C   
1728  O O   . ALA B 24  ? 0.576 0.562 0.490 0.034  -0.005 -0.026 24  ALA BBB O   
1729  C CB  . ALA B 24  ? 0.528 0.564 0.497 0.024  0.002  -0.048 24  ALA BBB CB  
1730  N N   . SER B 25  ? 0.542 0.539 0.461 0.010  0.012  -0.034 25  SER BBB N   
1731  C CA  . SER B 25  ? 0.578 0.548 0.479 0.001  0.019  -0.025 25  SER BBB CA  
1732  C C   . SER B 25  ? 0.559 0.518 0.473 -0.000 0.019  -0.028 25  SER BBB C   
1733  O O   . SER B 25  ? 0.523 0.498 0.458 0.005  0.016  -0.036 25  SER BBB O   
1734  C CB  . SER B 25  ? 0.579 0.557 0.478 -0.014 0.033  -0.027 25  SER BBB CB  
1735  O OG  . SER B 25  ? 0.525 0.526 0.457 -0.019 0.038  -0.036 25  SER BBB OG  
1736  N N   . GLY B 26  ? 0.624 0.555 0.524 -0.010 0.024  -0.022 26  GLY BBB N   
1737  C CA  . GLY B 26  ? 0.664 0.585 0.573 -0.019 0.025  -0.027 26  GLY BBB CA  
1738  C C   . GLY B 26  ? 0.694 0.582 0.590 -0.007 0.020  -0.027 26  GLY BBB C   
1739  O O   . GLY B 26  ? 0.740 0.624 0.631 0.012  0.014  -0.024 26  GLY BBB O   
1740  N N   . ARG B 27  ? 0.746 0.612 0.639 -0.019 0.022  -0.031 27  ARG BBB N   
1741  C CA  . ARG B 27  ? 0.812 0.637 0.688 -0.009 0.020  -0.035 27  ARG BBB CA  
1742  C C   . ARG B 27  ? 0.737 0.576 0.625 -0.009 0.019  -0.049 27  ARG BBB C   
1743  O O   . ARG B 27  ? 0.751 0.557 0.625 -0.005 0.020  -0.056 27  ARG BBB O   
1744  C CB  . ARG B 27  ? 0.928 0.707 0.781 -0.028 0.025  -0.029 27  ARG BBB CB  
1745  C CG  . ARG B 27  ? 1.076 0.821 0.903 -0.021 0.025  -0.013 27  ARG BBB CG  
1746  C CD  . ARG B 27  ? 1.254 0.959 1.058 -0.047 0.032  -0.004 27  ARG BBB CD  
1747  N NE  . ARG B 27  ? 1.317 1.038 1.135 -0.076 0.037  -0.013 27  ARG BBB NE  
1748  C CZ  . ARG B 27  ? 1.349 1.104 1.182 -0.098 0.044  -0.010 27  ARG BBB CZ  
1749  N NH1 . ARG B 27  ? 1.337 1.111 1.167 -0.096 0.049  0.001  27  ARG BBB NH1 
1750  N NH2 . ARG B 27  ? 1.401 1.174 1.252 -0.122 0.045  -0.018 27  ARG BBB NH2 
1751  N N   . THR B 28  ? 0.703 0.586 0.614 -0.012 0.017  -0.054 28  THR BBB N   
1752  C CA  . THR B 28  ? 0.654 0.552 0.572 -0.015 0.015  -0.065 28  THR BBB CA  
1753  C C   . THR B 28  ? 0.577 0.511 0.513 -0.001 0.013  -0.065 28  THR BBB C   
1754  O O   . THR B 28  ? 0.592 0.551 0.540 -0.008 0.010  -0.069 28  THR BBB O   
1755  C CB  . THR B 28  ? 0.651 0.560 0.576 -0.039 0.012  -0.067 28  THR BBB CB  
1756  O OG1 . THR B 28  ? 0.644 0.585 0.591 -0.044 0.012  -0.060 28  THR BBB OG1 
1757  C CG2 . THR B 28  ? 0.688 0.560 0.593 -0.056 0.013  -0.070 28  THR BBB CG2 
1758  N N   . PHE B 29  ? 0.561 0.499 0.500 0.016  0.013  -0.061 29  PHE BBB N   
1759  C CA  . PHE B 29  ? 0.541 0.514 0.498 0.027  0.011  -0.062 29  PHE BBB CA  
1760  C C   . PHE B 29  ? 0.532 0.514 0.492 0.028  0.013  -0.071 29  PHE BBB C   
1761  O O   . PHE B 29  ? 0.548 0.559 0.521 0.024  0.012  -0.071 29  PHE BBB O   
1762  C CB  . PHE B 29  ? 0.554 0.527 0.511 0.045  0.008  -0.057 29  PHE BBB CB  
1763  C CG  . PHE B 29  ? 0.542 0.553 0.520 0.052  0.005  -0.058 29  PHE BBB CG  
1764  C CD1 . PHE B 29  ? 0.528 0.560 0.514 0.044  0.002  -0.056 29  PHE BBB CD1 
1765  C CD2 . PHE B 29  ? 0.559 0.585 0.548 0.065  0.007  -0.063 29  PHE BBB CD2 
1766  C CE1 . PHE B 29  ? 0.504 0.566 0.505 0.046  -0.001 -0.058 29  PHE BBB CE1 
1767  C CE2 . PHE B 29  ? 0.545 0.609 0.555 0.067  0.004  -0.064 29  PHE BBB CE2 
1768  C CZ  . PHE B 29  ? 0.522 0.602 0.537 0.056  -0.001 -0.061 29  PHE BBB CZ  
1769  N N   . HIS B 30  ? 0.538 0.494 0.482 0.032  0.018  -0.079 30  HIS BBB N   
1770  C CA  . HIS B 30  ? 0.546 0.507 0.485 0.033  0.024  -0.090 30  HIS BBB CA  
1771  C C   . HIS B 30  ? 0.541 0.515 0.477 0.012  0.020  -0.091 30  HIS BBB C   
1772  O O   . HIS B 30  ? 0.578 0.567 0.510 0.010  0.023  -0.096 30  HIS BBB O   
1773  C CB  . HIS B 30  ? 0.573 0.494 0.491 0.041  0.031  -0.101 30  HIS BBB CB  
1774  C CG  . HIS B 30  ? 0.604 0.490 0.499 0.021  0.028  -0.103 30  HIS BBB CG  
1775  N ND1 . HIS B 30  ? 0.614 0.475 0.505 0.017  0.025  -0.094 30  HIS BBB ND1 
1776  C CD2 . HIS B 30  ? 0.597 0.476 0.475 0.001  0.027  -0.111 30  HIS BBB CD2 
1777  C CE1 . HIS B 30  ? 0.627 0.467 0.502 -0.005 0.023  -0.098 30  HIS BBB CE1 
1778  N NE2 . HIS B 30  ? 0.619 0.470 0.486 -0.015 0.023  -0.109 30  HIS BBB NE2 
1779  N N   . SER B 31  ? 0.534 0.507 0.472 -0.002 0.013  -0.084 31  SER BBB N   
1780  C CA  . SER B 31  ? 0.519 0.508 0.459 -0.020 0.006  -0.083 31  SER BBB CA  
1781  C C   . SER B 31  ? 0.496 0.517 0.458 -0.018 0.002  -0.074 31  SER BBB C   
1782  O O   . SER B 31  ? 0.481 0.516 0.448 -0.029 -0.006 -0.069 31  SER BBB O   
1783  C CB  . SER B 31  ? 0.522 0.499 0.459 -0.036 0.000  -0.081 31  SER BBB CB  
1784  O OG  . SER B 31  ? 0.521 0.509 0.478 -0.035 -0.000 -0.072 31  SER BBB OG  
1785  N N   . TYR B 32  ? 0.473 0.504 0.449 -0.005 0.005  -0.071 32  TYR BBB N   
1786  C CA  . TYR B 32  ? 0.452 0.506 0.448 -0.005 0.002  -0.064 32  TYR BBB CA  
1787  C C   . TYR B 32  ? 0.454 0.522 0.452 -0.001 0.005  -0.065 32  TYR BBB C   
1788  O O   . TYR B 32  ? 0.476 0.546 0.472 0.008  0.011  -0.070 32  TYR BBB O   
1789  C CB  . TYR B 32  ? 0.437 0.492 0.443 0.000  0.003  -0.061 32  TYR BBB CB  
1790  C CG  . TYR B 32  ? 0.432 0.481 0.441 -0.008 0.002  -0.058 32  TYR BBB CG  
1791  C CD1 . TYR B 32  ? 0.481 0.510 0.477 -0.011 0.005  -0.059 32  TYR BBB CD1 
1792  C CD2 . TYR B 32  ? 0.430 0.494 0.458 -0.013 0.000  -0.054 32  TYR BBB CD2 
1793  C CE1 . TYR B 32  ? 0.502 0.530 0.503 -0.022 0.005  -0.056 32  TYR BBB CE1 
1794  C CE2 . TYR B 32  ? 0.458 0.526 0.495 -0.020 0.001  -0.052 32  TYR BBB CE2 
1795  C CZ  . TYR B 32  ? 0.491 0.543 0.515 -0.027 0.004  -0.053 32  TYR BBB CZ  
1796  O OH  . TYR B 32  ? 0.521 0.581 0.558 -0.038 0.006  -0.051 32  TYR BBB OH  
1797  N N   . VAL B 33  ? 0.459 0.538 0.461 -0.009 0.002  -0.059 33  VAL BBB N   
1798  C CA  . VAL B 33  ? 0.470 0.564 0.480 -0.010 0.005  -0.057 33  VAL BBB CA  
1799  C C   . VAL B 33  ? 0.465 0.564 0.491 -0.005 0.004  -0.057 33  VAL BBB C   
1800  O O   . VAL B 33  ? 0.499 0.592 0.533 -0.005 0.000  -0.054 33  VAL BBB O   
1801  C CB  . VAL B 33  ? 0.497 0.592 0.503 -0.020 -0.001 -0.048 33  VAL BBB CB  
1802  C CG1 . VAL B 33  ? 0.480 0.584 0.492 -0.025 0.003  -0.044 33  VAL BBB CG1 
1803  C CG2 . VAL B 33  ? 0.531 0.622 0.514 -0.028 -0.002 -0.049 33  VAL BBB CG2 
1804  N N   . MET B 34  ? 0.476 0.588 0.509 -0.001 0.008  -0.060 34  MET BBB N   
1805  C CA  . MET B 34  ? 0.460 0.578 0.504 0.001  0.005  -0.062 34  MET BBB CA  
1806  C C   . MET B 34  ? 0.461 0.590 0.514 -0.008 0.005  -0.060 34  MET BBB C   
1807  O O   . MET B 34  ? 0.399 0.540 0.452 -0.014 0.010  -0.059 34  MET BBB O   
1808  C CB  . MET B 34  ? 0.472 0.599 0.517 0.013  0.005  -0.066 34  MET BBB CB  
1809  C CG  . MET B 34  ? 0.487 0.594 0.519 0.021  0.005  -0.066 34  MET BBB CG  
1810  S SD  . MET B 34  ? 0.484 0.573 0.510 0.016  0.003  -0.062 34  MET BBB SD  
1811  C CE  . MET B 34  ? 0.492 0.590 0.520 0.017  -0.001 -0.064 34  MET BBB CE  
1812  N N   . ALA B 35  ? 0.463 0.586 0.521 -0.013 0.002  -0.061 35  ALA BBB N   
1813  C CA  . ALA B 35  ? 0.486 0.609 0.550 -0.025 0.003  -0.060 35  ALA BBB CA  
1814  C C   . ALA B 35  ? 0.487 0.611 0.554 -0.029 -0.001 -0.067 35  ALA BBB C   
1815  O O   . ALA B 35  ? 0.474 0.591 0.535 -0.021 -0.002 -0.072 35  ALA BBB O   
1816  C CB  . ALA B 35  ? 0.503 0.605 0.565 -0.029 0.002  -0.052 35  ALA BBB CB  
1817  N N   . TRP B 36  ? 0.481 0.612 0.555 -0.043 -0.001 -0.069 36  TRP BBB N   
1818  C CA  . TRP B 36  ? 0.483 0.609 0.556 -0.053 -0.004 -0.077 36  TRP BBB CA  
1819  C C   . TRP B 36  ? 0.496 0.592 0.568 -0.065 -0.002 -0.076 36  TRP BBB C   
1820  O O   . TRP B 36  ? 0.540 0.635 0.614 -0.074 0.001  -0.067 36  TRP BBB O   
1821  C CB  . TRP B 36  ? 0.488 0.650 0.573 -0.061 -0.009 -0.081 36  TRP BBB CB  
1822  C CG  . TRP B 36  ? 0.478 0.664 0.564 -0.046 -0.014 -0.082 36  TRP BBB CG  
1823  C CD1 . TRP B 36  ? 0.468 0.677 0.565 -0.034 -0.012 -0.078 36  TRP BBB CD1 
1824  C CD2 . TRP B 36  ? 0.484 0.668 0.559 -0.041 -0.022 -0.087 36  TRP BBB CD2 
1825  N NE1 . TRP B 36  ? 0.480 0.698 0.574 -0.020 -0.019 -0.078 36  TRP BBB NE1 
1826  C CE2 . TRP B 36  ? 0.488 0.694 0.568 -0.025 -0.026 -0.083 36  TRP BBB CE2 
1827  C CE3 . TRP B 36  ? 0.518 0.684 0.576 -0.049 -0.026 -0.096 36  TRP BBB CE3 
1828  C CZ2 . TRP B 36  ? 0.507 0.716 0.574 -0.017 -0.036 -0.083 36  TRP BBB CZ2 
1829  C CZ3 . TRP B 36  ? 0.538 0.710 0.581 -0.043 -0.034 -0.098 36  TRP BBB CZ3 
1830  C CH2 . TRP B 36  ? 0.517 0.710 0.564 -0.027 -0.040 -0.090 36  TRP BBB CH2 
1831  N N   . PHE B 37  ? 0.485 0.554 0.550 -0.065 -0.001 -0.084 37  PHE BBB N   
1832  C CA  . PHE B 37  ? 0.508 0.541 0.569 -0.076 0.001  -0.086 37  PHE BBB CA  
1833  C C   . PHE B 37  ? 0.535 0.563 0.587 -0.089 -0.001 -0.102 37  PHE BBB C   
1834  O O   . PHE B 37  ? 0.518 0.569 0.564 -0.085 -0.006 -0.110 37  PHE BBB O   
1835  C CB  . PHE B 37  ? 0.524 0.526 0.586 -0.060 0.006  -0.083 37  PHE BBB CB  
1836  C CG  . PHE B 37  ? 0.516 0.519 0.585 -0.051 0.005  -0.066 37  PHE BBB CG  
1837  C CD1 . PHE B 37  ? 0.501 0.530 0.571 -0.042 0.003  -0.061 37  PHE BBB CD1 
1838  C CD2 . PHE B 37  ? 0.548 0.521 0.619 -0.053 0.004  -0.055 37  PHE BBB CD2 
1839  C CE1 . PHE B 37  ? 0.510 0.540 0.583 -0.037 0.001  -0.047 37  PHE BBB CE1 
1840  C CE2 . PHE B 37  ? 0.556 0.532 0.630 -0.047 0.000  -0.038 37  PHE BBB CE2 
1841  C CZ  . PHE B 37  ? 0.534 0.539 0.608 -0.039 -0.002 -0.035 37  PHE BBB CZ  
1842  N N   . ARG B 38  ? 0.563 0.560 0.612 -0.105 0.000  -0.107 38  ARG BBB N   
1843  C CA  . ARG B 38  ? 0.613 0.597 0.646 -0.120 -0.002 -0.126 38  ARG BBB CA  
1844  C C   . ARG B 38  ? 0.670 0.595 0.694 -0.123 0.006  -0.134 38  ARG BBB C   
1845  O O   . ARG B 38  ? 0.676 0.574 0.708 -0.118 0.010  -0.121 38  ARG BBB O   
1846  C CB  . ARG B 38  ? 0.613 0.628 0.652 -0.145 -0.010 -0.129 38  ARG BBB CB  
1847  C CG  . ARG B 38  ? 0.649 0.646 0.696 -0.166 -0.007 -0.121 38  ARG BBB CG  
1848  C CD  . ARG B 38  ? 0.659 0.705 0.721 -0.190 -0.014 -0.120 38  ARG BBB CD  
1849  N NE  . ARG B 38  ? 0.720 0.749 0.787 -0.212 -0.008 -0.111 38  ARG BBB NE  
1850  C CZ  . ARG B 38  ? 0.738 0.803 0.821 -0.239 -0.010 -0.109 38  ARG BBB CZ  
1851  N NH1 . ARG B 38  ? 0.712 0.836 0.811 -0.244 -0.020 -0.117 38  ARG BBB NH1 
1852  N NH2 . ARG B 38  ? 0.763 0.807 0.846 -0.261 -0.003 -0.098 38  ARG BBB NH2 
1853  N N   . GLN B 39  ? 0.689 0.593 0.694 -0.130 0.008  -0.155 39  GLN BBB N   
1854  C CA  . GLN B 39  ? 0.760 0.602 0.754 -0.130 0.017  -0.167 39  GLN BBB CA  
1855  C C   . GLN B 39  ? 0.837 0.661 0.806 -0.157 0.014  -0.190 39  GLN BBB C   
1856  O O   . GLN B 39  ? 0.841 0.684 0.792 -0.158 0.011  -0.206 39  GLN BBB O   
1857  C CB  . GLN B 39  ? 0.742 0.570 0.736 -0.101 0.028  -0.172 39  GLN BBB CB  
1858  C CG  . GLN B 39  ? 0.797 0.561 0.783 -0.097 0.041  -0.186 39  GLN BBB CG  
1859  C CD  . GLN B 39  ? 0.790 0.548 0.788 -0.065 0.054  -0.187 39  GLN BBB CD  
1860  O OE1 . GLN B 39  ? 0.771 0.567 0.769 -0.055 0.056  -0.188 39  GLN BBB OE1 
1861  N NE2 . GLN B 39  ? 0.829 0.539 0.838 -0.051 0.062  -0.186 39  GLN BBB NE2 
1862  N N   . ALA B 40  ? 0.916 0.708 0.885 -0.180 0.013  -0.191 40  ALA BBB N   
1863  C CA  . ALA B 40  ? 0.974 0.734 0.918 -0.211 0.011  -0.214 40  ALA BBB CA  
1864  C C   . ALA B 40  ? 1.034 0.726 0.959 -0.198 0.025  -0.233 40  ALA BBB C   
1865  O O   . ALA B 40  ? 1.022 0.685 0.960 -0.171 0.036  -0.223 40  ALA BBB O   
1866  C CB  . ALA B 40  ? 0.994 0.745 0.948 -0.241 0.006  -0.203 40  ALA BBB CB  
1867  N N   . PRO B 41  ? 1.122 0.785 1.014 -0.218 0.026  -0.262 41  PRO BBB N   
1868  C CA  . PRO B 41  ? 1.183 0.772 1.054 -0.208 0.044  -0.285 41  PRO BBB CA  
1869  C C   . PRO B 41  ? 1.226 0.750 1.109 -0.208 0.050  -0.275 41  PRO BBB C   
1870  O O   . PRO B 41  ? 1.223 0.740 1.107 -0.238 0.041  -0.266 41  PRO BBB O   
1871  C CB  . PRO B 41  ? 1.246 0.823 1.075 -0.238 0.040  -0.318 41  PRO BBB CB  
1872  C CG  . PRO B 41  ? 1.212 0.850 1.048 -0.272 0.016  -0.309 41  PRO BBB CG  
1873  C CD  . PRO B 41  ? 1.138 0.838 1.012 -0.251 0.011  -0.276 41  PRO BBB CD  
1874  N N   . GLY B 42  ? 1.253 0.733 1.145 -0.175 0.066  -0.273 42  GLY BBB N   
1875  C CA  . GLY B 42  ? 1.300 0.711 1.203 -0.167 0.071  -0.261 42  GLY BBB CA  
1876  C C   . GLY B 42  ? 1.266 0.707 1.203 -0.151 0.063  -0.221 42  GLY BBB C   
1877  O O   . GLY B 42  ? 1.311 0.698 1.258 -0.139 0.067  -0.206 42  GLY BBB O   
1878  N N   . LYS B 43  ? 1.203 0.723 1.155 -0.152 0.053  -0.205 43  LYS BBB N   
1879  C CA  . LYS B 43  ? 1.177 0.727 1.154 -0.143 0.045  -0.170 43  LYS BBB CA  
1880  C C   . LYS B 43  ? 1.118 0.713 1.116 -0.107 0.046  -0.160 43  LYS BBB C   
1881  O O   . LYS B 43  ? 1.108 0.724 1.101 -0.096 0.052  -0.178 43  LYS BBB O   
1882  C CB  . LYS B 43  ? 1.176 0.780 1.153 -0.174 0.033  -0.159 43  LYS BBB CB  
1883  C CG  . LYS B 43  ? 1.249 0.813 1.215 -0.210 0.030  -0.155 43  LYS BBB CG  
1884  C CD  . LYS B 43  ? 1.228 0.854 1.200 -0.242 0.021  -0.148 43  LYS BBB CD  
1885  C CE  . LYS B 43  ? 1.295 0.892 1.265 -0.274 0.020  -0.132 43  LYS BBB CE  
1886  N NZ  . LYS B 43  ? 1.254 0.916 1.242 -0.280 0.017  -0.108 43  LYS BBB NZ  
1887  N N   . GLU B 44  ? 1.103 0.710 1.121 -0.092 0.041  -0.130 44  GLU BBB N   
1888  C CA  . GLU B 44  ? 1.048 0.702 1.088 -0.064 0.039  -0.118 44  GLU BBB CA  
1889  C C   . GLU B 44  ? 0.955 0.677 0.994 -0.077 0.031  -0.113 44  GLU BBB C   
1890  O O   . GLU B 44  ? 0.961 0.693 0.988 -0.105 0.026  -0.116 44  GLU BBB O   
1891  C CB  . GLU B 44  ? 1.086 0.724 1.145 -0.044 0.034  -0.089 44  GLU BBB CB  
1892  C CG  . GLU B 44  ? 1.218 0.783 1.280 -0.030 0.040  -0.090 44  GLU BBB CG  
1893  C CD  . GLU B 44  ? 1.283 0.828 1.353 -0.005 0.055  -0.116 44  GLU BBB CD  
1894  O OE1 . GLU B 44  ? 1.247 0.841 1.333 0.013  0.059  -0.120 44  GLU BBB OE1 
1895  O OE2 . GLU B 44  ? 1.335 0.815 1.394 -0.006 0.065  -0.132 44  GLU BBB OE2 
1896  N N   . ARG B 45  ? 0.894 0.660 0.946 -0.057 0.030  -0.108 45  ARG BBB N   
1897  C CA  . ARG B 45  ? 0.879 0.704 0.932 -0.064 0.023  -0.101 45  ARG BBB CA  
1898  C C   . ARG B 45  ? 0.849 0.682 0.905 -0.077 0.015  -0.079 45  ARG BBB C   
1899  O O   . ARG B 45  ? 0.911 0.727 0.973 -0.066 0.013  -0.060 45  ARG BBB O   
1900  C CB  . ARG B 45  ? 0.844 0.703 0.910 -0.041 0.024  -0.097 45  ARG BBB CB  
1901  C CG  . ARG B 45  ? 0.873 0.748 0.929 -0.038 0.030  -0.117 45  ARG BBB CG  
1902  C CD  . ARG B 45  ? 0.887 0.783 0.958 -0.016 0.035  -0.114 45  ARG BBB CD  
1903  N NE  . ARG B 45  ? 0.944 0.833 1.004 -0.011 0.047  -0.135 45  ARG BBB NE  
1904  C CZ  . ARG B 45  ? 0.976 0.892 1.036 -0.002 0.053  -0.139 45  ARG BBB CZ  
1905  N NH1 . ARG B 45  ? 0.984 0.933 1.056 0.003  0.047  -0.123 45  ARG BBB NH1 
1906  N NH2 . ARG B 45  ? 0.995 0.901 1.040 -0.000 0.066  -0.158 45  ARG BBB NH2 
1907  N N   . GLU B 46  ? 0.805 0.664 0.853 -0.100 0.012  -0.081 46  GLU BBB N   
1908  C CA  . GLU B 46  ? 0.786 0.660 0.835 -0.118 0.009  -0.064 46  GLU BBB CA  
1909  C C   . GLU B 46  ? 0.698 0.630 0.754 -0.112 0.006  -0.060 46  GLU BBB C   
1910  O O   . GLU B 46  ? 0.648 0.612 0.706 -0.109 0.005  -0.074 46  GLU BBB O   
1911  C CB  . GLU B 46  ? 0.835 0.695 0.876 -0.149 0.010  -0.073 46  GLU BBB CB  
1912  C CG  . GLU B 46  ? 0.880 0.763 0.923 -0.173 0.010  -0.058 46  GLU BBB CG  
1913  C CD  . GLU B 46  ? 0.887 0.783 0.931 -0.206 0.009  -0.070 46  GLU BBB CD  
1914  O OE1 . GLU B 46  ? 0.899 0.766 0.935 -0.215 0.008  -0.088 46  GLU BBB OE1 
1915  O OE2 . GLU B 46  ? 0.894 0.827 0.946 -0.224 0.011  -0.061 46  GLU BBB OE2 
1916  N N   . PHE B 47  ? 0.668 0.613 0.724 -0.109 0.006  -0.041 47  PHE BBB N   
1917  C CA  . PHE B 47  ? 0.629 0.623 0.689 -0.104 0.005  -0.039 47  PHE BBB CA  
1918  C C   . PHE B 47  ? 0.609 0.637 0.674 -0.124 0.008  -0.045 47  PHE BBB C   
1919  O O   . PHE B 47  ? 0.629 0.648 0.692 -0.146 0.011  -0.040 47  PHE BBB O   
1920  C CB  . PHE B 47  ? 0.624 0.616 0.676 -0.101 0.005  -0.019 47  PHE BBB CB  
1921  C CG  . PHE B 47  ? 0.604 0.639 0.655 -0.099 0.007  -0.019 47  PHE BBB CG  
1922  C CD1 . PHE B 47  ? 0.581 0.631 0.635 -0.080 0.005  -0.023 47  PHE BBB CD1 
1923  C CD2 . PHE B 47  ? 0.614 0.671 0.661 -0.116 0.014  -0.014 47  PHE BBB CD2 
1924  C CE1 . PHE B 47  ? 0.532 0.614 0.583 -0.077 0.008  -0.025 47  PHE BBB CE1 
1925  C CE2 . PHE B 47  ? 0.585 0.680 0.633 -0.112 0.019  -0.016 47  PHE BBB CE2 
1926  C CZ  . PHE B 47  ? 0.544 0.647 0.591 -0.091 0.016  -0.022 47  PHE BBB CZ  
1927  N N   . VAL B 48  ? 0.574 0.643 0.648 -0.115 0.007  -0.054 48  VAL BBB N   
1928  C CA  . VAL B 48  ? 0.568 0.683 0.655 -0.128 0.008  -0.060 48  VAL BBB CA  
1929  C C   . VAL B 48  ? 0.532 0.683 0.625 -0.120 0.013  -0.054 48  VAL BBB C   
1930  O O   . VAL B 48  ? 0.523 0.699 0.624 -0.136 0.021  -0.049 48  VAL BBB O   
1931  C CB  . VAL B 48  ? 0.559 0.691 0.652 -0.124 -0.000 -0.075 48  VAL BBB CB  
1932  C CG1 . VAL B 48  ? 0.536 0.723 0.649 -0.133 -0.002 -0.079 48  VAL BBB CG1 
1933  C CG2 . VAL B 48  ? 0.616 0.710 0.698 -0.136 -0.004 -0.085 48  VAL BBB CG2 
1934  N N   . ALA B 49  ? 0.525 0.679 0.614 -0.097 0.012  -0.054 49  ALA BBB N   
1935  C CA  . ALA B 49  ? 0.532 0.714 0.623 -0.087 0.018  -0.053 49  ALA BBB CA  
1936  C C   . ALA B 49  ? 0.517 0.683 0.595 -0.066 0.016  -0.052 49  ALA BBB C   
1937  O O   . ALA B 49  ? 0.527 0.673 0.603 -0.058 0.009  -0.055 49  ALA BBB O   
1938  C CB  . ALA B 49  ? 0.531 0.759 0.644 -0.084 0.018  -0.061 49  ALA BBB CB  
1939  N N   . ALA B 50  ? 0.524 0.699 0.595 -0.061 0.022  -0.049 50  ALA BBB N   
1940  C CA  . ALA B 50  ? 0.518 0.680 0.577 -0.046 0.020  -0.049 50  ALA BBB CA  
1941  C C   . ALA B 50  ? 0.511 0.694 0.566 -0.039 0.029  -0.054 50  ALA BBB C   
1942  O O   . ALA B 50  ? 0.510 0.714 0.567 -0.049 0.039  -0.054 50  ALA BBB O   
1943  C CB  . ALA B 50  ? 0.517 0.651 0.560 -0.050 0.015  -0.039 50  ALA BBB CB  
1944  N N   . ILE B 51  ? 0.514 0.687 0.562 -0.024 0.028  -0.059 51  ILE BBB N   
1945  C CA  . ILE B 51  ? 0.510 0.693 0.552 -0.014 0.037  -0.067 51  ILE BBB CA  
1946  C C   . ILE B 51  ? 0.516 0.671 0.536 -0.010 0.034  -0.068 51  ILE BBB C   
1947  O O   . ILE B 51  ? 0.510 0.647 0.530 -0.005 0.025  -0.067 51  ILE BBB O   
1948  C CB  . ILE B 51  ? 0.501 0.705 0.566 0.002  0.037  -0.074 51  ILE BBB CB  
1949  C CG1 . ILE B 51  ? 0.519 0.734 0.584 0.016  0.050  -0.083 51  ILE BBB CG1 
1950  C CG2 . ILE B 51  ? 0.513 0.698 0.577 0.011  0.026  -0.073 51  ILE BBB CG2 
1951  C CD1 . ILE B 51  ? 0.515 0.759 0.609 0.033  0.050  -0.087 51  ILE BBB CD1 
1952  N N   . SER B 52  ? 0.534 0.686 0.533 -0.015 0.042  -0.071 52  SER BBB N   
1953  C CA  . SER B 52  ? 0.535 0.661 0.507 -0.015 0.039  -0.074 52  SER BBB CA  
1954  C C   . SER B 52  ? 0.516 0.631 0.489 0.001  0.042  -0.086 52  SER BBB C   
1955  O O   . SER B 52  ? 0.480 0.608 0.473 0.015  0.047  -0.089 52  SER BBB O   
1956  C CB  . SER B 52  ? 0.568 0.693 0.511 -0.028 0.046  -0.075 52  SER BBB CB  
1957  O OG  . SER B 52  ? 0.577 0.680 0.496 -0.035 0.035  -0.073 52  SER BBB OG  
1958  N N   . TRP B 53  ? 0.549 0.637 0.499 -0.002 0.039  -0.090 53  TRP BBB N   
1959  C CA  . TRP B 53  ? 0.556 0.620 0.501 0.009  0.040  -0.098 53  TRP BBB CA  
1960  C C   . TRP B 53  ? 0.586 0.653 0.533 0.026  0.055  -0.110 53  TRP BBB C   
1961  O O   . TRP B 53  ? 0.622 0.686 0.586 0.044  0.055  -0.111 53  TRP BBB O   
1962  C CB  . TRP B 53  ? 0.562 0.598 0.478 -0.004 0.034  -0.102 53  TRP BBB CB  
1963  C CG  . TRP B 53  ? 0.511 0.553 0.430 -0.019 0.020  -0.090 53  TRP BBB CG  
1964  C CD1 . TRP B 53  ? 0.471 0.514 0.409 -0.019 0.010  -0.081 53  TRP BBB CD1 
1965  C CD2 . TRP B 53  ? 0.519 0.569 0.422 -0.035 0.013  -0.084 53  TRP BBB CD2 
1966  N NE1 . TRP B 53  ? 0.466 0.518 0.408 -0.031 -0.001 -0.071 53  TRP BBB NE1 
1967  C CE2 . TRP B 53  ? 0.501 0.557 0.421 -0.041 -0.002 -0.071 53  TRP BBB CE2 
1968  C CE3 . TRP B 53  ? 0.547 0.600 0.423 -0.044 0.018  -0.087 53  TRP BBB CE3 
1969  C CZ2 . TRP B 53  ? 0.508 0.572 0.421 -0.053 -0.014 -0.060 53  TRP BBB CZ2 
1970  C CZ3 . TRP B 53  ? 0.556 0.614 0.418 -0.059 0.006  -0.076 53  TRP BBB CZ3 
1971  C CH2 . TRP B 53  ? 0.555 0.619 0.436 -0.063 -0.011 -0.061 53  TRP BBB CH2 
1972  N N   . SER B 54  ? 0.607 0.681 0.538 0.023  0.068  -0.119 54  SER BBB N   
1973  C CA  . SER B 54  ? 0.631 0.711 0.565 0.040  0.087  -0.134 54  SER BBB CA  
1974  C C   . SER B 54  ? 0.600 0.725 0.574 0.051  0.092  -0.129 54  SER BBB C   
1975  O O   . SER B 54  ? 0.623 0.765 0.611 0.068  0.109  -0.140 54  SER BBB O   
1976  C CB  . SER B 54  ? 0.671 0.750 0.573 0.028  0.102  -0.145 54  SER BBB CB  
1977  O OG  . SER B 54  ? 0.695 0.805 0.599 0.012  0.102  -0.135 54  SER BBB OG  
1978  N N   . SER B 55  ? 0.558 0.705 0.551 0.041  0.081  -0.115 55  SER BBB N   
1979  C CA  . SER B 55  ? 0.571 0.763 0.599 0.041  0.083  -0.110 55  SER BBB CA  
1980  C C   . SER B 55  ? 0.592 0.806 0.611 0.022  0.096  -0.110 55  SER BBB C   
1981  O O   . SER B 55  ? 0.584 0.836 0.631 0.018  0.099  -0.106 55  SER BBB O   
1982  C CB  . SER B 55  ? 0.561 0.778 0.621 0.066  0.090  -0.117 55  SER BBB CB  
1983  O OG  . SER B 55  ? 0.544 0.740 0.609 0.082  0.076  -0.113 55  SER BBB OG  
1984  N N   . THR B 56  ? 0.670 0.864 0.651 0.010  0.103  -0.113 56  THR BBB N   
1985  C CA  . THR B 56  ? 0.785 1.002 0.753 -0.000 0.124  -0.119 56  THR BBB CA  
1986  C C   . THR B 56  ? 0.787 1.014 0.745 -0.027 0.121  -0.104 56  THR BBB C   
1987  O O   . THR B 56  ? 0.923 1.180 0.885 -0.036 0.139  -0.105 56  THR BBB O   
1988  C CB  . THR B 56  ? 0.914 1.107 0.842 0.000  0.138  -0.135 56  THR BBB CB  
1989  O OG1 . THR B 56  ? 1.014 1.217 0.964 0.027  0.153  -0.151 56  THR BBB OG1 
1990  C CG2 . THR B 56  ? 0.963 1.167 0.858 -0.021 0.154  -0.135 56  THR BBB CG2 
1991  N N   . PRO B 57  ? 0.665 0.865 0.605 -0.040 0.102  -0.090 57  PRO BBB N   
1992  C CA  . PRO B 57  ? 0.600 0.808 0.546 -0.059 0.095  -0.072 57  PRO BBB CA  
1993  C C   . PRO B 57  ? 0.561 0.777 0.547 -0.050 0.084  -0.069 57  PRO BBB C   
1994  O O   . PRO B 57  ? 0.555 0.752 0.546 -0.038 0.070  -0.070 57  PRO BBB O   
1995  C CB  . PRO B 57  ? 0.608 0.784 0.517 -0.072 0.081  -0.060 57  PRO BBB CB  
1996  C CG  . PRO B 57  ? 0.635 0.789 0.522 -0.062 0.078  -0.073 57  PRO BBB CG  
1997  C CD  . PRO B 57  ? 0.616 0.780 0.528 -0.040 0.088  -0.090 57  PRO BBB CD  
1998  N N   . THR B 58  ? 0.534 0.781 0.547 -0.056 0.090  -0.067 58  THR BBB N   
1999  C CA  . THR B 58  ? 0.507 0.760 0.550 -0.058 0.077  -0.062 58  THR BBB CA  
2000  C C   . THR B 58  ? 0.523 0.765 0.556 -0.083 0.074  -0.047 58  THR BBB C   
2001  O O   . THR B 58  ? 0.508 0.754 0.522 -0.098 0.086  -0.042 58  THR BBB O   
2002  C CB  . THR B 58  ? 0.496 0.792 0.578 -0.050 0.082  -0.070 58  THR BBB CB  
2003  O OG1 . THR B 58  ? 0.523 0.856 0.615 -0.062 0.101  -0.072 58  THR BBB OG1 
2004  C CG2 . THR B 58  ? 0.479 0.779 0.572 -0.023 0.081  -0.081 58  THR BBB CG2 
2005  N N   . TYR B 59  ? 0.541 0.765 0.584 -0.086 0.060  -0.042 59  TYR BBB N   
2006  C CA  . TYR B 59  ? 0.553 0.755 0.588 -0.107 0.056  -0.028 59  TYR BBB CA  
2007  C C   . TYR B 59  ? 0.544 0.755 0.606 -0.113 0.050  -0.032 59  TYR BBB C   
2008  O O   . TYR B 59  ? 0.501 0.719 0.580 -0.098 0.043  -0.041 59  TYR BBB O   
2009  C CB  . TYR B 59  ? 0.550 0.710 0.564 -0.102 0.042  -0.017 59  TYR BBB CB  
2010  C CG  . TYR B 59  ? 0.568 0.717 0.553 -0.097 0.042  -0.014 59  TYR BBB CG  
2011  C CD1 . TYR B 59  ? 0.561 0.709 0.546 -0.080 0.037  -0.023 59  TYR BBB CD1 
2012  C CD2 . TYR B 59  ? 0.616 0.754 0.572 -0.113 0.044  0.001  59  TYR BBB CD2 
2013  C CE1 . TYR B 59  ? 0.574 0.711 0.531 -0.079 0.034  -0.021 59  TYR BBB CE1 
2014  C CE2 . TYR B 59  ? 0.638 0.765 0.563 -0.111 0.040  0.004  59  TYR BBB CE2 
2015  C CZ  . TYR B 59  ? 0.618 0.745 0.544 -0.094 0.034  -0.008 59  TYR BBB CZ  
2016  O OH  . TYR B 59  ? 0.658 0.777 0.553 -0.096 0.030  -0.007 59  TYR BBB OH  
2017  N N   . TYR B 60  ? 0.555 0.761 0.617 -0.137 0.054  -0.024 60  TYR BBB N   
2018  C CA  . TYR B 60  ? 0.550 0.762 0.634 -0.150 0.049  -0.029 60  TYR BBB CA  
2019  C C   . TYR B 60  ? 0.589 0.755 0.657 -0.170 0.046  -0.016 60  TYR BBB C   
2020  O O   . TYR B 60  ? 0.620 0.770 0.667 -0.183 0.052  -0.001 60  TYR BBB O   
2021  C CB  . TYR B 60  ? 0.563 0.831 0.673 -0.163 0.061  -0.035 60  TYR BBB CB  
2022  C CG  . TYR B 60  ? 0.546 0.857 0.678 -0.139 0.062  -0.047 60  TYR BBB CG  
2023  C CD1 . TYR B 60  ? 0.542 0.862 0.691 -0.125 0.049  -0.056 60  TYR BBB CD1 
2024  C CD2 . TYR B 60  ? 0.550 0.887 0.681 -0.130 0.078  -0.049 60  TYR BBB CD2 
2025  C CE1 . TYR B 60  ? 0.518 0.873 0.687 -0.101 0.049  -0.064 60  TYR BBB CE1 
2026  C CE2 . TYR B 60  ? 0.533 0.901 0.683 -0.105 0.080  -0.060 60  TYR BBB CE2 
2027  C CZ  . TYR B 60  ? 0.511 0.888 0.681 -0.090 0.064  -0.066 60  TYR BBB CZ  
2028  O OH  . TYR B 60  ? 0.488 0.891 0.677 -0.064 0.065  -0.074 60  TYR BBB OH  
2029  N N   . GLY B 61  ? 0.589 0.731 0.664 -0.173 0.036  -0.022 61  GLY BBB N   
2030  C CA  . GLY B 61  ? 0.643 0.740 0.707 -0.194 0.034  -0.014 61  GLY BBB CA  
2031  C C   . GLY B 61  ? 0.680 0.800 0.752 -0.227 0.044  -0.011 61  GLY BBB C   
2032  O O   . GLY B 61  ? 0.670 0.848 0.767 -0.232 0.049  -0.021 61  GLY BBB O   
2033  N N   . GLU B 62  ? 0.770 0.848 0.823 -0.249 0.047  0.004  62  GLU BBB N   
2034  C CA  . GLU B 62  ? 0.816 0.911 0.871 -0.285 0.059  0.012  62  GLU BBB CA  
2035  C C   . GLU B 62  ? 0.776 0.906 0.862 -0.304 0.057  -0.006 62  GLU BBB C   
2036  O O   . GLU B 62  ? 0.755 0.943 0.864 -0.322 0.068  -0.008 62  GLU BBB O   
2037  C CB  . GLU B 62  ? 0.935 0.964 0.960 -0.304 0.060  0.033  62  GLU BBB CB  
2038  C CG  . GLU B 62  ? 1.056 1.099 1.075 -0.343 0.076  0.046  62  GLU BBB CG  
2039  C CD  . GLU B 62  ? 1.067 1.177 1.092 -0.345 0.092  0.047  62  GLU BBB CD  
2040  O OE1 . GLU B 62  ? 1.034 1.155 1.048 -0.317 0.092  0.047  62  GLU BBB OE1 
2041  O OE2 . GLU B 62  ? 1.109 1.265 1.153 -0.374 0.106  0.044  62  GLU BBB OE2 
2042  N N   . SER B 63  ? 0.779 0.881 0.868 -0.299 0.044  -0.019 63  SER BBB N   
2043  C CA  . SER B 63  ? 0.774 0.898 0.884 -0.324 0.039  -0.035 63  SER BBB CA  
2044  C C   . SER B 63  ? 0.719 0.918 0.861 -0.309 0.034  -0.050 63  SER BBB C   
2045  O O   . SER B 63  ? 0.729 0.965 0.894 -0.331 0.029  -0.062 63  SER BBB O   
2046  C CB  . SER B 63  ? 0.798 0.857 0.891 -0.328 0.029  -0.045 63  SER BBB CB  
2047  O OG  . SER B 63  ? 0.779 0.824 0.866 -0.292 0.021  -0.053 63  SER BBB OG  
2048  N N   . VAL B 64  ? 0.655 0.841 0.853 -0.035 0.051  -0.041 64  VAL BBB N   
2049  C CA  . VAL B 64  ? 0.621 0.842 0.825 -0.051 0.050  -0.049 64  VAL BBB CA  
2050  C C   . VAL B 64  ? 0.665 0.871 0.839 -0.051 0.053  -0.039 64  VAL BBB C   
2051  O O   . VAL B 64  ? 0.661 0.889 0.855 -0.062 0.055  -0.045 64  VAL BBB O   
2052  C CB  . VAL B 64  ? 0.578 0.838 0.797 -0.055 0.033  -0.060 64  VAL BBB CB  
2053  C CG1 . VAL B 64  ? 0.589 0.866 0.839 -0.063 0.040  -0.078 64  VAL BBB CG1 
2054  C CG2 . VAL B 64  ? 0.576 0.836 0.781 -0.040 0.015  -0.055 64  VAL BBB CG2 
2055  N N   . LYS B 65  ? 0.730 0.900 0.861 -0.040 0.053  -0.026 65  LYS BBB N   
2056  C CA  . LYS B 65  ? 0.766 0.920 0.861 -0.047 0.063  -0.024 65  LYS BBB CA  
2057  C C   . LYS B 65  ? 0.748 0.901 0.872 -0.063 0.092  -0.035 65  LYS BBB C   
2058  O O   . LYS B 65  ? 0.753 0.888 0.888 -0.068 0.110  -0.035 65  LYS BBB O   
2059  C CB  . LYS B 65  ? 0.874 0.980 0.901 -0.040 0.063  -0.006 65  LYS BBB CB  
2060  C CG  . LYS B 65  ? 0.942 1.047 0.920 -0.044 0.055  -0.008 65  LYS BBB CG  
2061  C CD  . LYS B 65  ? 1.057 1.109 0.951 -0.054 0.073  0.005  65  LYS BBB CD  
2062  C CE  . LYS B 65  ? 1.067 1.125 0.938 -0.076 0.094  -0.016 65  LYS BBB CE  
2063  N NZ  . LYS B 65  ? 1.161 1.163 0.943 -0.095 0.121  -0.006 65  LYS BBB NZ  
2064  N N   . GLY B 66  ? 0.718 0.892 0.867 -0.072 0.095  -0.046 66  GLY BBB N   
2065  C CA  . GLY B 66  ? 0.711 0.890 0.908 -0.086 0.117  -0.060 66  GLY BBB CA  
2066  C C   . GLY B 66  ? 0.679 0.900 0.941 -0.088 0.097  -0.063 66  GLY BBB C   
2067  O O   . GLY B 66  ? 0.664 0.900 0.981 -0.095 0.100  -0.073 66  GLY BBB O   
2068  N N   . ARG B 67  ? 0.692 0.929 0.949 -0.084 0.078  -0.057 67  ARG BBB N   
2069  C CA  . ARG B 67  ? 0.665 0.939 0.961 -0.092 0.059  -0.058 67  ARG BBB CA  
2070  C C   . ARG B 67  ? 0.607 0.905 0.902 -0.092 0.032  -0.048 67  ARG BBB C   
2071  O O   . ARG B 67  ? 0.563 0.885 0.889 -0.100 0.012  -0.042 67  ARG BBB O   
2072  C CB  . ARG B 67  ? 0.685 0.962 0.974 -0.097 0.063  -0.065 67  ARG BBB CB  
2073  C CG  . ARG B 67  ? 0.698 0.947 0.996 -0.101 0.093  -0.075 67  ARG BBB CG  
2074  C CD  . ARG B 67  ? 0.698 0.954 1.007 -0.109 0.100  -0.088 67  ARG BBB CD  
2075  N NE  . ARG B 67  ? 0.701 0.948 0.983 -0.100 0.097  -0.083 67  ARG BBB NE  
2076  C CZ  . ARG B 67  ? 0.661 0.939 0.949 -0.109 0.085  -0.094 67  ARG BBB CZ  
2077  N NH1 . ARG B 67  ? 0.664 0.982 0.964 -0.128 0.072  -0.103 67  ARG BBB NH1 
2078  N NH2 . ARG B 67  ? 0.638 0.908 0.919 -0.100 0.085  -0.095 67  ARG BBB NH2 
2079  N N   . PHE B 68  ? 0.569 0.860 0.831 -0.083 0.029  -0.045 68  PHE BBB N   
2080  C CA  . PHE B 68  ? 0.548 0.860 0.809 -0.085 0.011  -0.040 68  PHE BBB CA  
2081  C C   . PHE B 68  ? 0.519 0.825 0.786 -0.078 0.012  -0.040 68  PHE BBB C   
2082  O O   . PHE B 68  ? 0.557 0.845 0.804 -0.070 0.024  -0.047 68  PHE BBB O   
2083  C CB  . PHE B 68  ? 0.536 0.851 0.772 -0.082 0.010  -0.047 68  PHE BBB CB  
2084  C CG  . PHE B 68  ? 0.541 0.868 0.778 -0.095 0.013  -0.055 68  PHE BBB CG  
2085  C CD1 . PHE B 68  ? 0.547 0.880 0.796 -0.107 0.015  -0.056 68  PHE BBB CD1 
2086  C CD2 . PHE B 68  ? 0.539 0.875 0.772 -0.098 0.016  -0.068 68  PHE BBB CD2 
2087  C CE1 . PHE B 68  ? 0.559 0.906 0.807 -0.122 0.021  -0.070 68  PHE BBB CE1 
2088  C CE2 . PHE B 68  ? 0.552 0.899 0.788 -0.115 0.026  -0.084 68  PHE BBB CE2 
2089  C CZ  . PHE B 68  ? 0.552 0.906 0.792 -0.128 0.029  -0.085 68  PHE BBB CZ  
2090  N N   . THR B 69  ? 0.498 0.819 0.791 -0.083 0.000  -0.033 69  THR BBB N   
2091  C CA  . THR B 69  ? 0.495 0.814 0.806 -0.079 0.004  -0.038 69  THR BBB CA  
2092  C C   . THR B 69  ? 0.493 0.825 0.800 -0.084 -0.006 -0.035 69  THR BBB C   
2093  O O   . THR B 69  ? 0.481 0.819 0.793 -0.095 -0.017 -0.019 69  THR BBB O   
2094  C CB  . THR B 69  ? 0.489 0.807 0.860 -0.083 0.005  -0.034 69  THR BBB CB  
2095  O OG1 . THR B 69  ? 0.492 0.800 0.871 -0.082 0.021  -0.044 69  THR BBB OG1 
2096  C CG2 . THR B 69  ? 0.485 0.801 0.887 -0.082 0.016  -0.046 69  THR BBB CG2 
2097  N N   . ILE B 70  ? 0.503 0.869 0.609 -0.034 0.034  -0.097 70  ILE BBB N   
2098  C CA  . ILE B 70  ? 0.503 0.822 0.593 -0.016 0.032  -0.097 70  ILE BBB CA  
2099  C C   . ILE B 70  ? 0.494 0.816 0.576 0.012  0.036  -0.094 70  ILE BBB C   
2100  O O   . ILE B 70  ? 0.473 0.814 0.557 0.015  0.043  -0.093 70  ILE BBB O   
2101  C CB  . ILE B 70  ? 0.524 0.789 0.602 -0.029 0.032  -0.095 70  ILE BBB CB  
2102  C CG1 . ILE B 70  ? 0.531 0.757 0.595 -0.016 0.028  -0.095 70  ILE BBB CG1 
2103  C CG2 . ILE B 70  ? 0.538 0.793 0.610 -0.030 0.040  -0.090 70  ILE BBB CG2 
2104  C CD1 . ILE B 70  ? 0.554 0.735 0.608 -0.027 0.028  -0.093 70  ILE BBB CD1 
2105  N N   . SER B 71  ? 0.488 0.793 0.560 0.032  0.032  -0.095 71  SER BBB N   
2106  C CA  . SER B 71  ? 0.497 0.793 0.556 0.061  0.034  -0.093 71  SER BBB CA  
2107  C C   . SER B 71  ? 0.499 0.749 0.541 0.070  0.029  -0.091 71  SER BBB C   
2108  O O   . SER B 71  ? 0.489 0.730 0.533 0.058  0.023  -0.091 71  SER BBB O   
2109  C CB  . SER B 71  ? 0.490 0.839 0.559 0.079  0.035  -0.094 71  SER BBB CB  
2110  O OG  . SER B 71  ? 0.536 0.907 0.613 0.080  0.027  -0.094 71  SER BBB OG  
2111  N N   . ARG B 72  ? 0.530 0.751 0.552 0.090  0.030  -0.088 72  ARG BBB N   
2112  C CA  . ARG B 72  ? 0.559 0.735 0.563 0.097  0.025  -0.085 72  ARG BBB CA  
2113  C C   . ARG B 72  ? 0.572 0.742 0.561 0.126  0.024  -0.083 72  ARG BBB C   
2114  O O   . ARG B 72  ? 0.592 0.776 0.579 0.141  0.029  -0.085 72  ARG BBB O   
2115  C CB  . ARG B 72  ? 0.577 0.707 0.566 0.085  0.027  -0.083 72  ARG BBB CB  
2116  C CG  . ARG B 72  ? 0.578 0.694 0.555 0.092  0.033  -0.084 72  ARG BBB CG  
2117  C CD  . ARG B 72  ? 0.615 0.693 0.581 0.076  0.034  -0.081 72  ARG BBB CD  
2118  N NE  . ARG B 72  ? 0.622 0.661 0.572 0.075  0.028  -0.076 72  ARG BBB NE  
2119  C CZ  . ARG B 72  ? 0.629 0.647 0.577 0.058  0.027  -0.073 72  ARG BBB CZ  
2120  N NH1 . ARG B 72  ? 0.586 0.611 0.544 0.042  0.031  -0.073 72  ARG BBB NH1 
2121  N NH2 . ARG B 72  ? 0.645 0.637 0.580 0.057  0.022  -0.068 72  ARG BBB NH2 
2122  N N   . ASP B 73  ? 0.581 0.732 0.558 0.134  0.017  -0.079 73  ASP BBB N   
2123  C CA  . ASP B 73  ? 0.616 0.745 0.572 0.161  0.015  -0.075 73  ASP BBB CA  
2124  C C   . ASP B 73  ? 0.636 0.708 0.569 0.155  0.010  -0.069 73  ASP BBB C   
2125  O O   . ASP B 73  ? 0.646 0.716 0.580 0.148  0.005  -0.064 73  ASP BBB O   
2126  C CB  . ASP B 73  ? 0.628 0.798 0.595 0.177  0.010  -0.073 73  ASP BBB CB  
2127  C CG  . ASP B 73  ? 0.694 0.840 0.638 0.207  0.007  -0.068 73  ASP BBB CG  
2128  O OD1 . ASP B 73  ? 0.729 0.822 0.647 0.213  0.007  -0.066 73  ASP BBB OD1 
2129  O OD2 . ASP B 73  ? 0.740 0.922 0.692 0.225  0.003  -0.066 73  ASP BBB OD2 
2130  N N   . ASN B 74  ? 0.686 0.716 0.599 0.155  0.013  -0.069 74  ASN BBB N   
2131  C CA  . ASN B 74  ? 0.692 0.670 0.582 0.145  0.009  -0.063 74  ASN BBB CA  
2132  C C   . ASN B 74  ? 0.742 0.696 0.613 0.159  0.002  -0.055 74  ASN BBB C   
2133  O O   . ASN B 74  ? 0.777 0.710 0.641 0.145  -0.003 -0.048 74  ASN BBB O   
2134  C CB  . ASN B 74  ? 0.699 0.642 0.570 0.143  0.013  -0.066 74  ASN BBB CB  
2135  C CG  . ASN B 74  ? 0.680 0.639 0.568 0.122  0.019  -0.070 74  ASN BBB CG  
2136  O OD1 . ASN B 74  ? 0.666 0.659 0.578 0.109  0.020  -0.071 74  ASN BBB OD1 
2137  N ND2 . ASN B 74  ? 0.689 0.622 0.561 0.119  0.022  -0.073 74  ASN BBB ND2 
2138  N N   . ALA B 75  ? 0.770 0.730 0.634 0.186  0.002  -0.056 75  ALA BBB N   
2139  C CA  . ALA B 75  ? 0.800 0.735 0.644 0.202  -0.006 -0.047 75  ALA BBB CA  
2140  C C   . ALA B 75  ? 0.773 0.736 0.632 0.192  -0.011 -0.041 75  ALA BBB C   
2141  O O   . ALA B 75  ? 0.831 0.767 0.671 0.195  -0.017 -0.031 75  ALA BBB O   
2142  C CB  . ALA B 75  ? 0.791 0.736 0.628 0.237  -0.005 -0.049 75  ALA BBB CB  
2143  N N   . LYS B 76  ? 0.725 0.739 0.614 0.180  -0.009 -0.047 76  LYS BBB N   
2144  C CA  . LYS B 76  ? 0.694 0.740 0.598 0.171  -0.013 -0.044 76  LYS BBB CA  
2145  C C   . LYS B 76  ? 0.638 0.685 0.553 0.143  -0.012 -0.046 76  LYS BBB C   
2146  O O   . LYS B 76  ? 0.588 0.664 0.517 0.135  -0.015 -0.047 76  LYS BBB O   
2147  C CB  . LYS B 76  ? 0.711 0.816 0.639 0.181  -0.013 -0.050 76  LYS BBB CB  
2148  C CG  . LYS B 76  ? 0.754 0.868 0.674 0.212  -0.014 -0.047 76  LYS BBB CG  
2149  C CD  . LYS B 76  ? 0.754 0.932 0.697 0.221  -0.016 -0.049 76  LYS BBB CD  
2150  C CE  . LYS B 76  ? 0.824 1.010 0.757 0.256  -0.018 -0.045 76  LYS BBB CE  
2151  N NZ  . LYS B 76  ? 0.852 1.106 0.807 0.264  -0.021 -0.045 76  LYS BBB NZ  
2152  N N   . ASN B 77  ? 0.622 0.640 0.531 0.130  -0.008 -0.048 77  ASN BBB N   
2153  C CA  . ASN B 77  ? 0.582 0.600 0.500 0.106  -0.007 -0.049 77  ASN BBB CA  
2154  C C   . ASN B 77  ? 0.549 0.612 0.494 0.098  -0.005 -0.057 77  ASN BBB C   
2155  O O   . ASN B 77  ? 0.532 0.603 0.485 0.085  -0.006 -0.058 77  ASN BBB O   
2156  C CB  . ASN B 77  ? 0.587 0.589 0.494 0.098  -0.012 -0.040 77  ASN BBB CB  
2157  C CG  . ASN B 77  ? 0.602 0.558 0.485 0.092  -0.013 -0.032 77  ASN BBB CG  
2158  O OD1 . ASN B 77  ? 0.612 0.540 0.479 0.101  -0.013 -0.031 77  ASN BBB OD1 
2159  N ND2 . ASN B 77  ? 0.582 0.533 0.463 0.075  -0.015 -0.027 77  ASN BBB ND2 
2160  N N   . THR B 78  ? 0.541 0.633 0.499 0.106  -0.002 -0.064 78  THR BBB N   
2161  C CA  . THR B 78  ? 0.509 0.645 0.491 0.097  -0.002 -0.071 78  THR BBB CA  
2162  C C   . THR B 78  ? 0.514 0.663 0.509 0.088  0.004  -0.077 78  THR BBB C   
2163  O O   . THR B 78  ? 0.493 0.640 0.484 0.099  0.009  -0.077 78  THR BBB O   
2164  C CB  . THR B 78  ? 0.509 0.681 0.497 0.112  -0.007 -0.071 78  THR BBB CB  
2165  O OG1 . THR B 78  ? 0.513 0.671 0.488 0.118  -0.013 -0.064 78  THR BBB OG1 
2166  C CG2 . THR B 78  ? 0.480 0.699 0.490 0.101  -0.008 -0.079 78  THR BBB CG2 
2167  N N   . VAL B 79  ? 0.506 0.667 0.514 0.068  0.005  -0.082 79  VAL BBB N   
2168  C CA  . VAL B 79  ? 0.502 0.683 0.525 0.055  0.010  -0.088 79  VAL BBB CA  
2169  C C   . VAL B 79  ? 0.503 0.728 0.543 0.049  0.006  -0.093 79  VAL BBB C   
2170  O O   . VAL B 79  ? 0.505 0.735 0.545 0.046  0.001  -0.095 79  VAL BBB O   
2171  C CB  . VAL B 79  ? 0.510 0.663 0.532 0.037  0.013  -0.088 79  VAL BBB CB  
2172  C CG1 . VAL B 79  ? 0.523 0.668 0.545 0.027  0.008  -0.090 79  VAL BBB CG1 
2173  C CG2 . VAL B 79  ? 0.500 0.667 0.533 0.023  0.018  -0.091 79  VAL BBB CG2 
2174  N N   . TYR B 80  ? 0.525 0.785 0.578 0.047  0.010  -0.096 80  TYR BBB N   
2175  C CA  . TYR B 80  ? 0.497 0.808 0.568 0.038  0.006  -0.101 80  TYR BBB CA  
2176  C C   . TYR B 80  ? 0.485 0.804 0.567 0.012  0.009  -0.104 80  TYR BBB C   
2177  O O   . TYR B 80  ? 0.472 0.774 0.551 0.008  0.015  -0.102 80  TYR BBB O   
2178  C CB  . TYR B 80  ? 0.513 0.867 0.591 0.059  0.007  -0.098 80  TYR BBB CB  
2179  C CG  . TYR B 80  ? 0.539 0.883 0.604 0.085  0.003  -0.094 80  TYR BBB CG  
2180  C CD1 . TYR B 80  ? 0.550 0.911 0.616 0.089  -0.004 -0.094 80  TYR BBB CD1 
2181  C CD2 . TYR B 80  ? 0.561 0.876 0.610 0.106  0.007  -0.089 80  TYR BBB CD2 
2182  C CE1 . TYR B 80  ? 0.567 0.916 0.619 0.112  -0.008 -0.088 80  TYR BBB CE1 
2183  C CE2 . TYR B 80  ? 0.585 0.884 0.619 0.130  0.003  -0.084 80  TYR BBB CE2 
2184  C CZ  . TYR B 80  ? 0.582 0.899 0.618 0.133  -0.004 -0.082 80  TYR BBB CZ  
2185  O OH  . TYR B 80  ? 0.628 0.928 0.648 0.155  -0.009 -0.075 80  TYR BBB OH  
2186  N N   . LEU B 81  ? 0.505 0.847 0.596 -0.006 0.004  -0.110 81  LEU BBB N   
2187  C CA  . LEU B 81  ? 0.508 0.865 0.609 -0.033 0.005  -0.113 81  LEU BBB CA  
2188  C C   . LEU B 81  ? 0.523 0.942 0.640 -0.039 0.001  -0.116 81  LEU BBB C   
2189  O O   . LEU B 81  ? 0.539 0.969 0.657 -0.044 -0.007 -0.122 81  LEU BBB O   
2190  C CB  . LEU B 81  ? 0.516 0.832 0.609 -0.053 0.002  -0.118 81  LEU BBB CB  
2191  C CG  . LEU B 81  ? 0.529 0.843 0.627 -0.081 0.004  -0.119 81  LEU BBB CG  
2192  C CD1 . LEU B 81  ? 0.524 0.821 0.620 -0.081 0.012  -0.112 81  LEU BBB CD1 
2193  C CD2 . LEU B 81  ? 0.543 0.817 0.630 -0.098 -0.001 -0.126 81  LEU BBB CD2 
2194  N N   . GLN B 82  ? 0.523 0.985 0.653 -0.036 0.006  -0.113 82  GLN BBB N   
2195  C CA  . GLN B 82  ? 0.539 1.070 0.688 -0.046 0.003  -0.114 82  GLN BBB CA  
2196  C C   . GLN B 82  ? 0.550 1.080 0.704 -0.084 0.001  -0.117 82  GLN BBB C   
2197  O O   . GLN B 82  ? 0.555 1.064 0.706 -0.096 0.008  -0.113 82  GLN BBB O   
2198  C CB  . GLN B 82  ? 0.528 1.104 0.687 -0.025 0.010  -0.108 82  GLN BBB CB  
2199  C CG  . GLN B 82  ? 0.529 1.186 0.708 -0.029 0.007  -0.108 82  GLN BBB CG  
2200  C CD  . GLN B 82  ? 0.527 1.203 0.706 -0.020 -0.003 -0.111 82  GLN BBB CD  
2201  O OE1 . GLN B 82  ? 0.514 1.167 0.682 0.007  -0.005 -0.110 82  GLN BBB OE1 
2202  N NE2 . GLN B 82  ? 0.532 1.252 0.725 -0.046 -0.010 -0.115 82  GLN BBB NE2 
2203  N N   . MET B 83  ? 0.571 1.113 0.727 -0.104 -0.008 -0.124 83  MET BBB N   
2204  C CA  . MET B 83  ? 0.602 1.136 0.757 -0.143 -0.011 -0.128 83  MET BBB CA  
2205  C C   . MET B 83  ? 0.600 1.210 0.774 -0.160 -0.016 -0.129 83  MET BBB C   
2206  O O   . MET B 83  ? 0.576 1.217 0.753 -0.155 -0.024 -0.133 83  MET BBB O   
2207  C CB  . MET B 83  ? 0.632 1.114 0.771 -0.154 -0.019 -0.138 83  MET BBB CB  
2208  C CG  . MET B 83  ? 0.628 1.045 0.749 -0.134 -0.015 -0.137 83  MET BBB CG  
2209  S SD  . MET B 83  ? 0.680 1.056 0.784 -0.138 -0.024 -0.149 83  MET BBB SD  
2210  C CE  . MET B 83  ? 0.728 1.061 0.822 -0.174 -0.025 -0.154 83  MET BBB CE  
2211  N N   . ASN B 84  ? 0.607 1.250 0.793 -0.178 -0.011 -0.123 84  ASN BBB N   
2212  C CA  . ASN B 84  ? 0.597 1.321 0.803 -0.198 -0.014 -0.121 84  ASN BBB CA  
2213  C C   . ASN B 84  ? 0.620 1.330 0.822 -0.246 -0.019 -0.124 84  ASN BBB C   
2214  O O   . ASN B 84  ? 0.604 1.245 0.789 -0.259 -0.017 -0.124 84  ASN BBB O   
2215  C CB  . ASN B 84  ? 0.578 1.359 0.800 -0.182 -0.004 -0.111 84  ASN BBB CB  
2216  C CG  . ASN B 84  ? 0.568 1.362 0.791 -0.134 -0.001 -0.109 84  ASN BBB CG  
2217  O OD1 . ASN B 84  ? 0.598 1.396 0.818 -0.118 -0.008 -0.113 84  ASN BBB OD1 
2218  N ND2 . ASN B 84  ? 0.543 1.339 0.766 -0.112 0.010  -0.103 84  ASN BBB ND2 
2219  N N   . ARG B 85  ? 0.631 1.401 0.845 -0.271 -0.027 -0.126 85  ARG BBB N   
2220  C CA  . ARG B 85  ? 0.664 1.432 0.875 -0.321 -0.033 -0.127 85  ARG BBB CA  
2221  C C   . ARG B 85  ? 0.669 1.340 0.852 -0.334 -0.038 -0.137 85  ARG BBB C   
2222  O O   . ARG B 85  ? 0.672 1.296 0.844 -0.357 -0.035 -0.133 85  ARG BBB O   
2223  C CB  . ARG B 85  ? 0.679 1.484 0.904 -0.335 -0.024 -0.115 85  ARG BBB CB  
2224  C CG  . ARG B 85  ? 0.680 1.591 0.932 -0.323 -0.021 -0.108 85  ARG BBB CG  
2225  C CD  . ARG B 85  ? 0.679 1.651 0.948 -0.340 -0.013 -0.096 85  ARG BBB CD  
2226  N NE  . ARG B 85  ? 0.691 1.608 0.949 -0.336 -0.002 -0.089 85  ARG BBB NE  
2227  C CZ  . ARG B 85  ? 0.679 1.569 0.932 -0.295 0.007  -0.087 85  ARG BBB CZ  
2228  N NH1 . ARG B 85  ? 0.659 1.570 0.917 -0.253 0.008  -0.091 85  ARG BBB NH1 
2229  N NH2 . ARG B 85  ? 0.686 1.522 0.926 -0.297 0.015  -0.082 85  ARG BBB NH2 
2230  N N   . LEU B 86  ? 0.664 1.312 0.837 -0.319 -0.045 -0.147 86  LEU BBB N   
2231  C CA  . LEU B 86  ? 0.706 1.265 0.851 -0.324 -0.049 -0.158 86  LEU BBB CA  
2232  C C   . LEU B 86  ? 0.764 1.304 0.897 -0.371 -0.059 -0.165 86  LEU BBB C   
2233  O O   . LEU B 86  ? 0.781 1.380 0.924 -0.394 -0.067 -0.168 86  LEU BBB O   
2234  C CB  . LEU B 86  ? 0.701 1.254 0.840 -0.294 -0.054 -0.167 86  LEU BBB CB  
2235  C CG  . LEU B 86  ? 0.671 1.212 0.812 -0.250 -0.045 -0.160 86  LEU BBB CG  
2236  C CD1 . LEU B 86  ? 0.680 1.240 0.820 -0.224 -0.050 -0.166 86  LEU BBB CD1 
2237  C CD2 . LEU B 86  ? 0.670 1.129 0.792 -0.243 -0.039 -0.159 86  LEU BBB CD2 
2238  N N   . LYS B 87  ? 0.822 1.279 0.931 -0.383 -0.059 -0.168 87  LYS BBB N   
2239  C CA  . LYS B 87  ? 0.894 1.308 0.982 -0.426 -0.068 -0.176 87  LYS BBB CA  
2240  C C   . LYS B 87  ? 0.895 1.235 0.955 -0.415 -0.073 -0.192 87  LYS BBB C   
2241  O O   . LYS B 87  ? 0.865 1.178 0.922 -0.378 -0.068 -0.192 87  LYS BBB O   
2242  C CB  . LYS B 87  ? 0.961 1.338 1.044 -0.448 -0.062 -0.165 87  LYS BBB CB  
2243  C CG  . LYS B 87  ? 0.960 1.402 1.070 -0.443 -0.051 -0.148 87  LYS BBB CG  
2244  C CD  . LYS B 87  ? 1.004 1.411 1.108 -0.458 -0.044 -0.134 87  LYS BBB CD  
2245  C CE  . LYS B 87  ? 1.019 1.507 1.150 -0.459 -0.035 -0.120 87  LYS BBB CE  
2246  N NZ  . LYS B 87  ? 1.057 1.523 1.184 -0.477 -0.028 -0.105 87  LYS BBB NZ  
2247  N N   . PRO B 88  ? 0.924 1.230 0.962 -0.447 -0.085 -0.205 88  PRO BBB N   
2248  C CA  . PRO B 88  ? 0.943 1.174 0.950 -0.436 -0.090 -0.221 88  PRO BBB CA  
2249  C C   . PRO B 88  ? 0.931 1.087 0.923 -0.410 -0.081 -0.217 88  PRO BBB C   
2250  O O   . PRO B 88  ? 0.916 1.044 0.897 -0.381 -0.080 -0.225 88  PRO BBB O   
2251  C CB  . PRO B 88  ? 0.999 1.200 0.983 -0.483 -0.102 -0.233 88  PRO BBB CB  
2252  C CG  . PRO B 88  ? 0.986 1.281 0.996 -0.508 -0.107 -0.228 88  PRO BBB CG  
2253  C CD  . PRO B 88  ? 0.942 1.285 0.982 -0.494 -0.094 -0.207 88  PRO BBB CD  
2254  N N   . GLU B 89  ? 0.962 1.095 0.955 -0.421 -0.074 -0.203 89  GLU BBB N   
2255  C CA  . GLU B 89  ? 0.986 1.052 0.967 -0.400 -0.066 -0.197 89  GLU BBB CA  
2256  C C   . GLU B 89  ? 0.914 1.004 0.911 -0.356 -0.056 -0.190 89  GLU BBB C   
2257  O O   . GLU B 89  ? 0.910 0.949 0.896 -0.336 -0.050 -0.185 89  GLU BBB O   
2258  C CB  . GLU B 89  ? 1.020 1.072 1.002 -0.422 -0.061 -0.181 89  GLU BBB CB  
2259  C CG  . GLU B 89  ? 1.116 1.151 1.084 -0.472 -0.069 -0.183 89  GLU BBB CG  
2260  C CD  . GLU B 89  ? 1.128 1.251 1.121 -0.500 -0.072 -0.178 89  GLU BBB CD  
2261  O OE1 . GLU B 89  ? 1.125 1.312 1.147 -0.488 -0.063 -0.164 89  GLU BBB OE1 
2262  O OE2 . GLU B 89  ? 1.103 1.233 1.087 -0.535 -0.084 -0.188 89  GLU BBB OE2 
2263  N N   . ASP B 90  ? 0.863 1.025 0.884 -0.342 -0.055 -0.188 90  ASP BBB N   
2264  C CA  . ASP B 90  ? 0.813 0.997 0.847 -0.301 -0.047 -0.182 90  ASP BBB CA  
2265  C C   . ASP B 90  ? 0.802 0.969 0.824 -0.277 -0.051 -0.195 90  ASP BBB C   
2266  O O   . ASP B 90  ? 0.776 0.947 0.803 -0.245 -0.046 -0.190 90  ASP BBB O   
2267  C CB  . ASP B 90  ? 0.775 1.041 0.838 -0.294 -0.044 -0.174 90  ASP BBB CB  
2268  C CG  . ASP B 90  ? 0.790 1.081 0.867 -0.310 -0.038 -0.160 90  ASP BBB CG  
2269  O OD1 . ASP B 90  ? 0.796 1.043 0.866 -0.307 -0.031 -0.152 90  ASP BBB OD1 
2270  O OD2 . ASP B 90  ? 0.766 1.122 0.861 -0.327 -0.039 -0.157 90  ASP BBB OD2 
2271  N N   . THR B 91  ? 0.821 0.970 0.826 -0.294 -0.061 -0.210 91  THR BBB N   
2272  C CA  . THR B 91  ? 0.807 0.937 0.796 -0.274 -0.065 -0.223 91  THR BBB CA  
2273  C C   . THR B 91  ? 0.793 0.862 0.766 -0.249 -0.059 -0.222 91  THR BBB C   
2274  O O   . THR B 91  ? 0.823 0.836 0.781 -0.261 -0.058 -0.222 91  THR BBB O   
2275  C CB  . THR B 91  ? 0.846 0.959 0.815 -0.301 -0.077 -0.241 91  THR BBB CB  
2276  O OG1 . THR B 91  ? 0.832 1.016 0.819 -0.320 -0.083 -0.241 91  THR BBB OG1 
2277  C CG2 . THR B 91  ? 0.860 0.947 0.808 -0.281 -0.081 -0.256 91  THR BBB CG2 
2278  N N   . ALA B 92  ? 0.763 0.844 0.741 -0.217 -0.055 -0.220 92  ALA BBB N   
2279  C CA  . ALA B 92  ? 0.763 0.798 0.729 -0.191 -0.048 -0.217 92  ALA BBB CA  
2280  C C   . ALA B 92  ? 0.730 0.794 0.704 -0.160 -0.045 -0.213 92  ALA BBB C   
2281  O O   . ALA B 92  ? 0.698 0.816 0.687 -0.158 -0.048 -0.211 92  ALA BBB O   
2282  C CB  . ALA B 92  ? 0.753 0.768 0.726 -0.191 -0.040 -0.202 92  ALA BBB CB  
2283  N N   . VAL B 93  ? 0.739 0.770 0.702 -0.138 -0.041 -0.212 93  VAL BBB N   
2284  C CA  . VAL B 93  ? 0.698 0.751 0.669 -0.111 -0.036 -0.203 93  VAL BBB CA  
2285  C C   . VAL B 93  ? 0.672 0.732 0.658 -0.106 -0.029 -0.187 93  VAL BBB C   
2286  O O   . VAL B 93  ? 0.691 0.717 0.674 -0.112 -0.025 -0.182 93  VAL BBB O   
2287  C CB  . VAL B 93  ? 0.722 0.740 0.674 -0.091 -0.034 -0.208 93  VAL BBB CB  
2288  C CG1 . VAL B 93  ? 0.706 0.747 0.666 -0.067 -0.029 -0.197 93  VAL BBB CG1 
2289  C CG2 . VAL B 93  ? 0.734 0.743 0.667 -0.094 -0.041 -0.227 93  VAL BBB CG2 
2290  N N   . TYR B 94  ? 0.639 0.743 0.642 -0.096 -0.027 -0.178 94  TYR BBB N   
2291  C CA  . TYR B 94  ? 0.606 0.719 0.621 -0.090 -0.021 -0.164 94  TYR BBB CA  
2292  C C   . TYR B 94  ? 0.582 0.688 0.594 -0.066 -0.017 -0.156 94  TYR BBB C   
2293  O O   . TYR B 94  ? 0.563 0.689 0.573 -0.054 -0.020 -0.158 94  TYR BBB O   
2294  C CB  . TYR B 94  ? 0.568 0.730 0.600 -0.095 -0.022 -0.160 94  TYR BBB CB  
2295  C CG  . TYR B 94  ? 0.581 0.754 0.620 -0.121 -0.023 -0.163 94  TYR BBB CG  
2296  C CD1 . TYR B 94  ? 0.590 0.763 0.623 -0.141 -0.031 -0.175 94  TYR BBB CD1 
2297  C CD2 . TYR B 94  ? 0.574 0.753 0.623 -0.128 -0.018 -0.153 94  TYR BBB CD2 
2298  C CE1 . TYR B 94  ? 0.608 0.788 0.645 -0.169 -0.033 -0.177 94  TYR BBB CE1 
2299  C CE2 . TYR B 94  ? 0.608 0.800 0.663 -0.154 -0.019 -0.154 94  TYR BBB CE2 
2300  C CZ  . TYR B 94  ? 0.612 0.803 0.661 -0.176 -0.027 -0.165 94  TYR BBB CZ  
2301  O OH  . TYR B 94  ? 0.613 0.816 0.667 -0.206 -0.029 -0.165 94  TYR BBB OH  
2302  N N   . PHE B 95  ? 0.575 0.653 0.584 -0.061 -0.011 -0.148 95  PHE BBB N   
2303  C CA  . PHE B 95  ? 0.564 0.632 0.568 -0.043 -0.007 -0.139 95  PHE BBB CA  
2304  C C   . PHE B 95  ? 0.565 0.644 0.579 -0.038 -0.003 -0.127 95  PHE BBB C   
2305  O O   . PHE B 95  ? 0.547 0.621 0.566 -0.048 0.001  -0.123 95  PHE BBB O   
2306  C CB  . PHE B 95  ? 0.581 0.611 0.574 -0.040 -0.004 -0.138 95  PHE BBB CB  
2307  C CG  . PHE B 95  ? 0.592 0.605 0.573 -0.040 -0.008 -0.151 95  PHE BBB CG  
2308  C CD1 . PHE B 95  ? 0.631 0.621 0.605 -0.056 -0.011 -0.160 95  PHE BBB CD1 
2309  C CD2 . PHE B 95  ? 0.598 0.614 0.570 -0.025 -0.009 -0.153 95  PHE BBB CD2 
2310  C CE1 . PHE B 95  ? 0.661 0.628 0.619 -0.054 -0.014 -0.173 95  PHE BBB CE1 
2311  C CE2 . PHE B 95  ? 0.616 0.615 0.573 -0.022 -0.011 -0.165 95  PHE BBB CE2 
2312  C CZ  . PHE B 95  ? 0.643 0.615 0.592 -0.036 -0.014 -0.176 95  PHE BBB CZ  
2313  N N   . CYS B 96  ? 0.578 0.670 0.591 -0.024 -0.003 -0.121 96  CYS BBB N   
2314  C CA  . CYS B 96  ? 0.553 0.645 0.568 -0.015 0.001  -0.110 96  CYS BBB CA  
2315  C C   . CYS B 96  ? 0.530 0.593 0.536 -0.013 0.004  -0.104 96  CYS BBB C   
2316  O O   . CYS B 96  ? 0.509 0.562 0.508 -0.009 0.003  -0.105 96  CYS BBB O   
2317  C CB  . CYS B 96  ? 0.581 0.691 0.593 -0.002 -0.002 -0.107 96  CYS BBB CB  
2318  S SG  . CYS B 96  ? 0.729 0.833 0.738 0.009  0.001  -0.095 96  CYS BBB SG  
2319  N N   . ALA B 97  ? 0.483 0.536 0.490 -0.015 0.009  -0.096 97  ALA BBB N   
2320  C CA  . ALA B 97  ? 0.508 0.538 0.507 -0.012 0.011  -0.089 97  ALA BBB CA  
2321  C C   . ALA B 97  ? 0.509 0.537 0.505 -0.009 0.014  -0.080 97  ALA BBB C   
2322  O O   . ALA B 97  ? 0.531 0.572 0.533 -0.008 0.015  -0.081 97  ALA BBB O   
2323  C CB  . ALA B 97  ? 0.522 0.534 0.521 -0.021 0.013  -0.090 97  ALA BBB CB  
2324  N N   . ALA B 98  ? 0.504 0.518 0.492 -0.006 0.014  -0.073 98  ALA BBB N   
2325  C CA  . ALA B 98  ? 0.510 0.516 0.491 -0.004 0.015  -0.065 98  ALA BBB CA  
2326  C C   . ALA B 98  ? 0.523 0.515 0.498 -0.008 0.017  -0.058 98  ALA BBB C   
2327  O O   . ALA B 98  ? 0.523 0.515 0.498 -0.007 0.016  -0.056 98  ALA BBB O   
2328  C CB  . ALA B 98  ? 0.519 0.528 0.492 0.004  0.012  -0.062 98  ALA BBB CB  
2329  N N   . ASP B 99  ? 0.532 0.514 0.501 -0.011 0.019  -0.054 99  ASP BBB N   
2330  C CA  . ASP B 99  ? 0.528 0.499 0.490 -0.016 0.020  -0.046 99  ASP BBB CA  
2331  C C   . ASP B 99  ? 0.517 0.477 0.467 -0.017 0.020  -0.042 99  ASP BBB C   
2332  O O   . ASP B 99  ? 0.480 0.441 0.431 -0.014 0.022  -0.047 99  ASP BBB O   
2333  C CB  . ASP B 99  ? 0.523 0.491 0.491 -0.021 0.023  -0.045 99  ASP BBB CB  
2334  C CG  . ASP B 99  ? 0.530 0.494 0.492 -0.023 0.022  -0.036 99  ASP BBB CG  
2335  O OD1 . ASP B 99  ? 0.511 0.480 0.475 -0.019 0.020  -0.035 99  ASP BBB OD1 
2336  O OD2 . ASP B 99  ? 0.554 0.511 0.510 -0.028 0.023  -0.031 99  ASP BBB OD2 
2337  N N   . ARG B 100 ? 0.501 0.452 0.440 -0.022 0.018  -0.035 100 ARG BBB N   
2338  C CA  . ARG B 100 ? 0.536 0.470 0.459 -0.025 0.017  -0.033 100 ARG BBB CA  
2339  C C   . ARG B 100 ? 0.533 0.466 0.458 -0.028 0.022  -0.035 100 ARG BBB C   
2340  O O   . ARG B 100 ? 0.544 0.469 0.459 -0.026 0.024  -0.038 100 ARG BBB O   
2341  C CB  . ARG B 100 ? 0.568 0.497 0.480 -0.034 0.014  -0.024 100 ARG BBB CB  
2342  C CG  . ARG B 100 ? 0.621 0.547 0.525 -0.034 0.009  -0.020 100 ARG BBB CG  
2343  C CD  . ARG B 100 ? 0.615 0.521 0.504 -0.029 0.006  -0.022 100 ARG BBB CD  
2344  N NE  . ARG B 100 ? 0.615 0.499 0.487 -0.033 0.007  -0.024 100 ARG BBB NE  
2345  C CZ  . ARG B 100 ? 0.661 0.525 0.513 -0.044 0.003  -0.019 100 ARG BBB CZ  
2346  N NH1 . ARG B 100 ? 0.652 0.518 0.499 -0.054 -0.002 -0.010 100 ARG BBB NH1 
2347  N NH2 . ARG B 100 ? 0.658 0.503 0.496 -0.045 0.004  -0.023 100 ARG BBB NH2 
2348  N N   . GLY B 101 ? 0.524 0.466 0.459 -0.032 0.024  -0.033 101 GLY BBB N   
2349  C CA  . GLY B 101 ? 0.536 0.478 0.473 -0.037 0.028  -0.032 101 GLY BBB CA  
2350  C C   . GLY B 101 ? 0.549 0.500 0.497 -0.036 0.032  -0.038 101 GLY BBB C   
2351  O O   . GLY B 101 ? 0.535 0.493 0.494 -0.033 0.032  -0.042 101 GLY BBB O   
2352  N N   . GLU B 102 ? 0.558 0.512 0.504 -0.039 0.037  -0.039 102 GLU BBB N   
2353  C CA  . GLU B 102 ? 0.557 0.523 0.514 -0.043 0.041  -0.042 102 GLU BBB CA  
2354  C C   . GLU B 102 ? 0.537 0.498 0.495 -0.052 0.042  -0.034 102 GLU BBB C   
2355  O O   . GLU B 102 ? 0.549 0.504 0.498 -0.055 0.043  -0.029 102 GLU BBB O   
2356  C CB  . GLU B 102 ? 0.586 0.562 0.538 -0.039 0.046  -0.046 102 GLU BBB CB  
2357  C CG  . GLU B 102 ? 0.593 0.590 0.558 -0.044 0.050  -0.048 102 GLU BBB CG  
2358  C CD  . GLU B 102 ? 0.604 0.617 0.564 -0.038 0.056  -0.052 102 GLU BBB CD  
2359  O OE1 . GLU B 102 ? 0.659 0.664 0.607 -0.026 0.055  -0.056 102 GLU BBB OE1 
2360  O OE2 . GLU B 102 ? 0.657 0.689 0.625 -0.045 0.060  -0.051 102 GLU BBB OE2 
2361  N N   . SER B 103 ? 0.521 0.481 0.489 -0.056 0.042  -0.034 103 SER BBB N   
2362  C CA  . SER B 103 ? 0.511 0.460 0.479 -0.062 0.042  -0.027 103 SER BBB CA  
2363  C C   . SER B 103 ? 0.516 0.470 0.485 -0.073 0.047  -0.024 103 SER BBB C   
2364  O O   . SER B 103 ? 0.504 0.472 0.481 -0.077 0.049  -0.030 103 SER BBB O   
2365  C CB  . SER B 103 ? 0.498 0.437 0.471 -0.060 0.039  -0.029 103 SER BBB CB  
2366  O OG  . SER B 103 ? 0.508 0.430 0.477 -0.064 0.039  -0.021 103 SER BBB OG  
2367  N N   . TYR B 104 ? 0.526 0.472 0.488 -0.078 0.048  -0.014 104 TYR BBB N   
2368  C CA  . TYR B 104 ? 0.519 0.466 0.482 -0.090 0.052  -0.009 104 TYR BBB CA  
2369  C C   . TYR B 104 ? 0.533 0.468 0.503 -0.096 0.050  -0.011 104 TYR BBB C   
2370  O O   . TYR B 104 ? 0.563 0.507 0.537 -0.108 0.053  -0.011 104 TYR BBB O   
2371  C CB  . TYR B 104 ? 0.536 0.474 0.489 -0.093 0.053  0.004  104 TYR BBB CB  
2372  C CG  . TYR B 104 ? 0.543 0.481 0.495 -0.107 0.056  0.012  104 TYR BBB CG  
2373  C CD1 . TYR B 104 ? 0.532 0.493 0.485 -0.114 0.062  0.010  104 TYR BBB CD1 
2374  C CD2 . TYR B 104 ? 0.583 0.497 0.531 -0.112 0.055  0.021  104 TYR BBB CD2 
2375  C CE1 . TYR B 104 ? 0.543 0.508 0.495 -0.128 0.066  0.018  104 TYR BBB CE1 
2376  C CE2 . TYR B 104 ? 0.598 0.510 0.543 -0.127 0.058  0.029  104 TYR BBB CE2 
2377  C CZ  . TYR B 104 ? 0.581 0.521 0.530 -0.136 0.063  0.029  104 TYR BBB CZ  
2378  O OH  . TYR B 104 ? 0.623 0.565 0.569 -0.153 0.067  0.039  104 TYR BBB OH  
2379  N N   . TYR B 105 ? 0.417 0.501 0.605 -0.073 0.007  -0.068 105 TYR BBB N   
2380  C CA  . TYR B 105 ? 0.432 0.497 0.623 -0.069 0.007  -0.070 105 TYR BBB CA  
2381  C C   . TYR B 105 ? 0.437 0.506 0.635 -0.059 0.005  -0.086 105 TYR BBB C   
2382  O O   . TYR B 105 ? 0.438 0.494 0.636 -0.047 0.004  -0.085 105 TYR BBB O   
2383  C CB  . TYR B 105 ? 0.434 0.479 0.620 -0.059 0.005  -0.054 105 TYR BBB CB  
2384  C CG  . TYR B 105 ? 0.466 0.510 0.645 -0.066 0.004  -0.035 105 TYR BBB CG  
2385  C CD1 . TYR B 105 ? 0.465 0.495 0.634 -0.081 0.005  -0.030 105 TYR BBB CD1 
2386  C CD2 . TYR B 105 ? 0.446 0.504 0.626 -0.058 0.001  -0.022 105 TYR BBB CD2 
2387  C CE1 . TYR B 105 ? 0.477 0.503 0.636 -0.088 0.002  -0.011 105 TYR BBB CE1 
2388  C CE2 . TYR B 105 ? 0.449 0.510 0.622 -0.064 -0.002 -0.003 105 TYR BBB CE2 
2389  C CZ  . TYR B 105 ? 0.480 0.523 0.642 -0.078 -0.002 0.003  105 TYR BBB CZ  
2390  O OH  . TYR B 105 ? 0.503 0.548 0.658 -0.084 -0.007 0.023  105 TYR BBB OH  
2391  N N   . TYR B 106 ? 0.428 0.517 0.632 -0.063 0.006  -0.100 106 TYR BBB N   
2392  C CA  . TYR B 106 ? 0.427 0.524 0.637 -0.051 0.002  -0.113 106 TYR BBB CA  
2393  C C   . TYR B 106 ? 0.441 0.528 0.653 -0.051 0.001  -0.118 106 TYR BBB C   
2394  O O   . TYR B 106 ? 0.456 0.546 0.671 -0.042 -0.004 -0.126 106 TYR BBB O   
2395  C CB  . TYR B 106 ? 0.438 0.561 0.655 -0.052 0.002  -0.126 106 TYR BBB CB  
2396  C CG  . TYR B 106 ? 0.439 0.584 0.664 -0.068 0.008  -0.132 106 TYR BBB CG  
2397  C CD1 . TYR B 106 ? 0.440 0.595 0.672 -0.074 0.007  -0.140 106 TYR BBB CD1 
2398  C CD2 . TYR B 106 ? 0.453 0.610 0.674 -0.081 0.014  -0.129 106 TYR BBB CD2 
2399  C CE1 . TYR B 106 ? 0.453 0.632 0.689 -0.095 0.012  -0.145 106 TYR BBB CE1 
2400  C CE2 . TYR B 106 ? 0.451 0.629 0.675 -0.100 0.020  -0.133 106 TYR BBB CE2 
2401  C CZ  . TYR B 106 ? 0.473 0.664 0.706 -0.108 0.019  -0.141 106 TYR BBB CZ  
2402  O OH  . TYR B 106 ? 0.509 0.725 0.742 -0.131 0.024  -0.144 106 TYR BBB OH  
2403  N N   . THR B 107 ? 0.437 0.509 0.644 -0.063 0.004  -0.115 107 THR BBB N   
2404  C CA  . THR B 107 ? 0.436 0.490 0.638 -0.067 0.004  -0.121 107 THR BBB CA  
2405  C C   . THR B 107 ? 0.451 0.475 0.645 -0.053 0.004  -0.114 107 THR BBB C   
2406  O O   . THR B 107 ? 0.480 0.486 0.666 -0.053 0.004  -0.121 107 THR BBB O   
2407  C CB  . THR B 107 ? 0.440 0.485 0.634 -0.090 0.007  -0.121 107 THR BBB CB  
2408  O OG1 . THR B 107 ? 0.455 0.466 0.634 -0.091 0.009  -0.106 107 THR BBB OG1 
2409  C CG2 . THR B 107 ? 0.424 0.507 0.627 -0.105 0.009  -0.127 107 THR BBB CG2 
2410  N N   . ARG B 108 ? 0.454 0.475 0.647 -0.042 0.004  -0.102 108 ARG BBB N   
2411  C CA  . ARG B 108 ? 0.478 0.480 0.665 -0.026 0.005  -0.096 108 ARG BBB CA  
2412  C C   . ARG B 108 ? 0.474 0.489 0.664 -0.016 0.003  -0.103 108 ARG BBB C   
2413  O O   . ARG B 108 ? 0.446 0.481 0.641 -0.014 -0.001 -0.101 108 ARG BBB O   
2414  C CB  . ARG B 108 ? 0.498 0.505 0.686 -0.018 0.006  -0.079 108 ARG BBB CB  
2415  C CG  . ARG B 108 ? 0.515 0.503 0.696 -0.025 0.007  -0.068 108 ARG BBB CG  
2416  C CD  . ARG B 108 ? 0.502 0.499 0.686 -0.014 0.006  -0.050 108 ARG BBB CD  
2417  N NE  . ARG B 108 ? 0.518 0.502 0.695 -0.022 0.005  -0.037 108 ARG BBB NE  
2418  C CZ  . ARG B 108 ? 0.506 0.502 0.684 -0.017 0.002  -0.019 108 ARG BBB CZ  
2419  N NH1 . ARG B 108 ? 0.481 0.507 0.668 -0.006 0.000  -0.013 108 ARG BBB NH1 
2420  N NH2 . ARG B 108 ? 0.538 0.517 0.705 -0.026 -0.001 -0.006 108 ARG BBB NH2 
2421  N N   . PRO B 109 ? 0.500 0.499 0.684 -0.010 0.004  -0.111 109 PRO BBB N   
2422  C CA  . PRO B 109 ? 0.476 0.486 0.658 -0.002 0.002  -0.116 109 PRO BBB CA  
2423  C C   . PRO B 109 ? 0.452 0.480 0.636 0.008  0.002  -0.104 109 PRO BBB C   
2424  O O   . PRO B 109 ? 0.441 0.484 0.624 0.006  -0.003 -0.105 109 PRO BBB O   
2425  C CB  . PRO B 109 ? 0.486 0.471 0.657 0.003  0.007  -0.124 109 PRO BBB CB  
2426  C CG  . PRO B 109 ? 0.513 0.474 0.677 -0.010 0.008  -0.129 109 PRO BBB CG  
2427  C CD  . PRO B 109 ? 0.513 0.479 0.684 -0.015 0.008  -0.116 109 PRO BBB CD  
2428  N N   . THR B 110 ? 0.465 0.492 0.653 0.016  0.006  -0.093 110 THR BBB N   
2429  C CA  . THR B 110 ? 0.434 0.487 0.625 0.024  0.007  -0.080 110 THR BBB CA  
2430  C C   . THR B 110 ? 0.420 0.492 0.612 0.011  0.000  -0.074 110 THR BBB C   
2431  O O   . THR B 110 ? 0.429 0.523 0.619 0.011  -0.001 -0.065 110 THR BBB O   
2432  C CB  . THR B 110 ? 0.433 0.482 0.628 0.038  0.011  -0.068 110 THR BBB CB  
2433  O OG1 . THR B 110 ? 0.444 0.477 0.639 0.029  0.009  -0.062 110 THR BBB OG1 
2434  C CG2 . THR B 110 ? 0.460 0.487 0.651 0.055  0.018  -0.076 110 THR BBB CG2 
2435  N N   . GLU B 111 ? 0.417 0.481 0.608 0.000  -0.002 -0.078 111 GLU BBB N   
2436  C CA  . GLU B 111 ? 0.441 0.516 0.628 -0.010 -0.007 -0.075 111 GLU BBB CA  
2437  C C   . GLU B 111 ? 0.447 0.521 0.624 -0.012 -0.013 -0.084 111 GLU BBB C   
2438  O O   . GLU B 111 ? 0.437 0.511 0.604 -0.018 -0.018 -0.082 111 GLU BBB O   
2439  C CB  . GLU B 111 ? 0.431 0.501 0.621 -0.018 -0.006 -0.077 111 GLU BBB CB  
2440  C CG  . GLU B 111 ? 0.453 0.522 0.646 -0.020 -0.002 -0.064 111 GLU BBB CG  
2441  C CD  . GLU B 111 ? 0.458 0.545 0.648 -0.023 -0.004 -0.048 111 GLU BBB CD  
2442  O OE1 . GLU B 111 ? 0.439 0.538 0.629 -0.015 -0.005 -0.041 111 GLU BBB OE1 
2443  O OE2 . GLU B 111 ? 0.446 0.538 0.631 -0.035 -0.005 -0.044 111 GLU BBB OE2 
2444  N N   . TYR B 112 ? 0.446 0.515 0.622 -0.006 -0.014 -0.092 112 TYR BBB N   
2445  C CA  . TYR B 112 ? 0.449 0.514 0.613 -0.008 -0.022 -0.099 112 TYR BBB CA  
2446  C C   . TYR B 112 ? 0.440 0.512 0.595 -0.008 -0.022 -0.095 112 TYR BBB C   
2447  O O   . TYR B 112 ? 0.411 0.485 0.571 -0.002 -0.016 -0.099 112 TYR BBB O   
2448  C CB  . TYR B 112 ? 0.435 0.492 0.605 -0.006 -0.025 -0.112 112 TYR BBB CB  
2449  C CG  . TYR B 112 ? 0.450 0.510 0.630 -0.008 -0.024 -0.117 112 TYR BBB CG  
2450  C CD1 . TYR B 112 ? 0.448 0.509 0.639 -0.012 -0.016 -0.116 112 TYR BBB CD1 
2451  C CD2 . TYR B 112 ? 0.449 0.512 0.627 -0.006 -0.030 -0.121 112 TYR BBB CD2 
2452  C CE1 . TYR B 112 ? 0.435 0.505 0.634 -0.017 -0.014 -0.119 112 TYR BBB CE1 
2453  C CE2 . TYR B 112 ? 0.456 0.530 0.644 -0.008 -0.027 -0.127 112 TYR BBB CE2 
2454  C CZ  . TYR B 112 ? 0.448 0.528 0.648 -0.015 -0.019 -0.126 112 TYR BBB CZ  
2455  O OH  . TYR B 112 ? 0.422 0.517 0.630 -0.020 -0.015 -0.131 112 TYR BBB OH  
2456  N N   . GLU B 113 ? 0.497 0.572 0.635 -0.016 -0.028 -0.089 113 GLU BBB N   
2457  C CA  . GLU B 113 ? 0.501 0.591 0.628 -0.020 -0.028 -0.084 113 GLU BBB CA  
2458  C C   . GLU B 113 ? 0.472 0.552 0.588 -0.020 -0.032 -0.094 113 GLU BBB C   
2459  O O   . GLU B 113 ? 0.434 0.528 0.550 -0.019 -0.027 -0.095 113 GLU BBB O   
2460  C CB  . GLU B 113 ? 0.553 0.648 0.658 -0.035 -0.034 -0.073 113 GLU BBB CB  
2461  C CG  . GLU B 113 ? 0.621 0.740 0.716 -0.044 -0.033 -0.067 113 GLU BBB CG  
2462  C CD  . GLU B 113 ? 0.668 0.798 0.739 -0.065 -0.039 -0.055 113 GLU BBB CD  
2463  O OE1 . GLU B 113 ? 0.661 0.773 0.721 -0.072 -0.044 -0.051 113 GLU BBB OE1 
2464  O OE2 . GLU B 113 ? 0.713 0.868 0.773 -0.076 -0.038 -0.050 113 GLU BBB OE2 
2465  N N   . PHE B 114 ? 0.453 0.511 0.561 -0.021 -0.042 -0.100 114 PHE BBB N   
2466  C CA  . PHE B 114 ? 0.456 0.504 0.548 -0.023 -0.050 -0.106 114 PHE BBB CA  
2467  C C   . PHE B 114 ? 0.453 0.497 0.561 -0.015 -0.050 -0.118 114 PHE BBB C   
2468  O O   . PHE B 114 ? 0.428 0.470 0.550 -0.009 -0.050 -0.122 114 PHE BBB O   
2469  C CB  . PHE B 114 ? 0.444 0.469 0.510 -0.029 -0.065 -0.102 114 PHE BBB CB  
2470  C CG  . PHE B 114 ? 0.452 0.478 0.495 -0.044 -0.066 -0.090 114 PHE BBB CG  
2471  C CD1 . PHE B 114 ? 0.446 0.492 0.478 -0.056 -0.063 -0.085 114 PHE BBB CD1 
2472  C CD2 . PHE B 114 ? 0.445 0.457 0.478 -0.048 -0.069 -0.085 114 PHE BBB CD2 
2473  C CE1 . PHE B 114 ? 0.448 0.504 0.460 -0.073 -0.064 -0.074 114 PHE BBB CE1 
2474  C CE2 . PHE B 114 ? 0.451 0.467 0.460 -0.066 -0.071 -0.073 114 PHE BBB CE2 
2475  C CZ  . PHE B 114 ? 0.459 0.499 0.458 -0.080 -0.069 -0.067 114 PHE BBB CZ  
2476  N N   . TRP B 115 ? 0.452 0.498 0.555 -0.017 -0.049 -0.124 115 TRP BBB N   
2477  C CA  . TRP B 115 ? 0.454 0.498 0.566 -0.015 -0.048 -0.136 115 TRP BBB CA  
2478  C C   . TRP B 115 ? 0.468 0.508 0.561 -0.021 -0.059 -0.140 115 TRP BBB C   
2479  O O   . TRP B 115 ? 0.486 0.528 0.561 -0.028 -0.057 -0.137 115 TRP BBB O   
2480  C CB  . TRP B 115 ? 0.467 0.514 0.588 -0.012 -0.033 -0.141 115 TRP BBB CB  
2481  C CG  . TRP B 115 ? 0.470 0.517 0.608 -0.006 -0.025 -0.136 115 TRP BBB CG  
2482  C CD1 . TRP B 115 ? 0.466 0.521 0.608 -0.002 -0.021 -0.126 115 TRP BBB CD1 
2483  C CD2 . TRP B 115 ? 0.480 0.519 0.631 -0.005 -0.023 -0.141 115 TRP BBB CD2 
2484  N NE1 . TRP B 115 ? 0.461 0.513 0.617 0.001  -0.016 -0.123 115 TRP BBB NE1 
2485  C CE2 . TRP B 115 ? 0.482 0.523 0.643 -0.002 -0.017 -0.133 115 TRP BBB CE2 
2486  C CE3 . TRP B 115 ? 0.510 0.545 0.663 -0.011 -0.025 -0.151 115 TRP BBB CE3 
2487  C CZ2 . TRP B 115 ? 0.507 0.541 0.678 -0.004 -0.013 -0.134 115 TRP BBB CZ2 
2488  C CZ3 . TRP B 115 ? 0.540 0.571 0.704 -0.015 -0.021 -0.153 115 TRP BBB CZ3 
2489  C CH2 . TRP B 115 ? 0.541 0.571 0.713 -0.011 -0.015 -0.144 115 TRP BBB CH2 
2490  N N   . GLY B 116 ? 0.460 0.498 0.557 -0.019 -0.068 -0.146 116 GLY BBB N   
2491  C CA  . GLY B 116 ? 0.495 0.533 0.577 -0.026 -0.078 -0.150 116 GLY BBB CA  
2492  C C   . GLY B 116 ? 0.505 0.546 0.586 -0.033 -0.067 -0.160 116 GLY BBB C   
2493  O O   . GLY B 116 ? 0.489 0.527 0.581 -0.029 -0.052 -0.163 116 GLY BBB O   
2494  N N   . GLN B 117 ? 0.532 0.572 0.596 -0.043 -0.073 -0.164 117 GLN BBB N   
2495  C CA  . GLN B 117 ? 0.541 0.578 0.595 -0.051 -0.062 -0.176 117 GLN BBB CA  
2496  C C   . GLN B 117 ? 0.545 0.583 0.611 -0.055 -0.062 -0.185 117 GLN BBB C   
2497  O O   . GLN B 117 ? 0.555 0.581 0.613 -0.061 -0.051 -0.196 117 GLN BBB O   
2498  C CB  . GLN B 117 ? 0.548 0.585 0.574 -0.063 -0.069 -0.178 117 GLN BBB CB  
2499  C CG  . GLN B 117 ? 0.554 0.594 0.564 -0.066 -0.070 -0.168 117 GLN BBB CG  
2500  C CD  . GLN B 117 ? 0.553 0.601 0.568 -0.060 -0.051 -0.169 117 GLN BBB CD  
2501  O OE1 . GLN B 117 ? 0.573 0.628 0.591 -0.057 -0.050 -0.159 117 GLN BBB OE1 
2502  N NE2 . GLN B 117 ? 0.554 0.600 0.569 -0.058 -0.036 -0.182 117 GLN BBB NE2 
2503  N N   . GLY B 118 ? 0.544 0.595 0.626 -0.052 -0.075 -0.182 118 GLY BBB N   
2504  C CA  . GLY B 118 ? 0.567 0.629 0.662 -0.059 -0.076 -0.189 118 GLY BBB CA  
2505  C C   . GLY B 118 ? 0.601 0.678 0.687 -0.070 -0.091 -0.193 118 GLY BBB C   
2506  O O   . GLY B 118 ? 0.632 0.702 0.695 -0.076 -0.096 -0.192 118 GLY BBB O   
2507  N N   . THR B 119 ? 0.618 0.719 0.719 -0.076 -0.097 -0.197 119 THR BBB N   
2508  C CA  . THR B 119 ? 0.618 0.743 0.715 -0.089 -0.113 -0.200 119 THR BBB CA  
2509  C C   . THR B 119 ? 0.628 0.766 0.732 -0.108 -0.107 -0.209 119 THR BBB C   
2510  O O   . THR B 119 ? 0.605 0.750 0.728 -0.105 -0.099 -0.209 119 THR BBB O   
2511  C CB  . THR B 119 ? 0.627 0.780 0.739 -0.071 -0.133 -0.190 119 THR BBB CB  
2512  O OG1 . THR B 119 ? 0.641 0.814 0.742 -0.082 -0.149 -0.191 119 THR BBB OG1 
2513  C CG2 . THR B 119 ? 0.610 0.793 0.755 -0.059 -0.133 -0.190 119 THR BBB CG2 
2514  N N   . GLN B 120 ? 0.643 0.782 0.726 -0.130 -0.110 -0.217 120 GLN BBB N   
2515  C CA  . GLN B 120 ? 0.662 0.810 0.742 -0.156 -0.106 -0.226 120 GLN BBB CA  
2516  C C   . GLN B 120 ? 0.654 0.862 0.764 -0.157 -0.121 -0.222 120 GLN BBB C   
2517  O O   . GLN B 120 ? 0.687 0.929 0.805 -0.148 -0.139 -0.216 120 GLN BBB O   
2518  C CB  . GLN B 120 ? 0.711 0.840 0.754 -0.181 -0.106 -0.235 120 GLN BBB CB  
2519  C CG  . GLN B 120 ? 0.739 0.860 0.766 -0.213 -0.101 -0.246 120 GLN BBB CG  
2520  C CD  . GLN B 120 ? 0.753 0.825 0.770 -0.213 -0.080 -0.251 120 GLN BBB CD  
2521  O OE1 . GLN B 120 ? 0.761 0.790 0.764 -0.199 -0.067 -0.254 120 GLN BBB OE1 
2522  N NE2 . GLN B 120 ? 0.760 0.844 0.786 -0.230 -0.079 -0.253 120 GLN BBB NE2 
2523  N N   . VAL B 121 ? 0.627 0.848 0.751 -0.167 -0.113 -0.225 121 VAL BBB N   
2524  C CA  . VAL B 121 ? 0.641 0.926 0.789 -0.180 -0.123 -0.226 121 VAL BBB CA  
2525  C C   . VAL B 121 ? 0.675 0.949 0.797 -0.221 -0.116 -0.235 121 VAL BBB C   
2526  O O   . VAL B 121 ? 0.688 0.912 0.792 -0.231 -0.100 -0.240 121 VAL BBB O   
2527  C CB  . VAL B 121 ? 0.633 0.945 0.815 -0.162 -0.118 -0.222 121 VAL BBB CB  
2528  C CG1 . VAL B 121 ? 0.652 1.038 0.859 -0.177 -0.125 -0.224 121 VAL BBB CG1 
2529  C CG2 . VAL B 121 ? 0.618 0.932 0.817 -0.123 -0.124 -0.214 121 VAL BBB CG2 
2530  N N   . THR B 122 ? 0.692 1.009 0.811 -0.245 -0.130 -0.238 122 THR BBB N   
2531  C CA  . THR B 122 ? 0.750 1.060 0.840 -0.291 -0.126 -0.247 122 THR BBB CA  
2532  C C   . THR B 122 ? 0.756 1.153 0.876 -0.308 -0.137 -0.245 122 THR BBB C   
2533  O O   . THR B 122 ? 0.774 1.236 0.919 -0.296 -0.155 -0.240 122 THR BBB O   
2534  C CB  . THR B 122 ? 0.769 1.047 0.818 -0.310 -0.130 -0.253 122 THR BBB CB  
2535  O OG1 . THR B 122 ? 0.762 0.968 0.789 -0.290 -0.117 -0.256 122 THR BBB OG1 
2536  C CG2 . THR B 122 ? 0.821 1.082 0.832 -0.360 -0.127 -0.264 122 THR BBB CG2 
2537  N N   . VAL B 123 ? 0.765 1.163 0.880 -0.335 -0.127 -0.249 123 VAL BBB N   
2538  C CA  . VAL B 123 ? 0.780 1.265 0.921 -0.360 -0.135 -0.248 123 VAL BBB CA  
2539  C C   . VAL B 123 ? 0.871 1.342 0.968 -0.417 -0.135 -0.256 123 VAL BBB C   
2540  O O   . VAL B 123 ? 0.868 1.267 0.927 -0.441 -0.121 -0.261 123 VAL BBB O   
2541  C CB  . VAL B 123 ? 0.743 1.245 0.910 -0.350 -0.123 -0.246 123 VAL BBB CB  
2542  C CG1 . VAL B 123 ? 0.740 1.347 0.941 -0.368 -0.131 -0.246 123 VAL BBB CG1 
2543  C CG2 . VAL B 123 ? 0.695 1.183 0.891 -0.297 -0.120 -0.240 123 VAL BBB CG2 
2544  N N   . SER B 124 ? 0.961 1.490 1.058 -0.439 -0.152 -0.256 124 SER BBB N   
2545  C CA  . SER B 124 ? 1.084 1.608 1.136 -0.500 -0.154 -0.264 124 SER BBB CA  
2546  C C   . SER B 124 ? 1.163 1.761 1.233 -0.535 -0.155 -0.263 124 SER BBB C   
2547  O O   . SER B 124 ? 1.101 1.776 1.225 -0.507 -0.158 -0.257 124 SER BBB O   
2548  C CB  . SER B 124 ? 1.086 1.648 1.131 -0.511 -0.173 -0.263 124 SER BBB CB  
2549  O OG  . SER B 124 ? 1.058 1.730 1.160 -0.487 -0.190 -0.254 124 SER BBB OG  
2572  N N   . THR C 4   ? 1.339 0.791 0.941 -0.020 0.177  -0.020 333 THR CCC N   
2573  C CA  . THR C 4   ? 1.225 0.717 0.849 0.009  0.139  0.008  333 THR CCC CA  
2574  C C   . THR C 4   ? 1.092 0.640 0.725 0.016  0.088  0.015  333 THR CCC C   
2575  O O   . THR C 4   ? 1.015 0.582 0.666 0.036  0.070  0.035  333 THR CCC O   
2576  C CB  . THR C 4   ? 1.264 0.741 0.852 -0.004 0.144  -0.002 333 THR CCC CB  
2577  O OG1 . THR C 4   ? 1.381 0.803 0.944 -0.026 0.194  -0.023 333 THR CCC OG1 
2578  C CG2 . THR C 4   ? 1.245 0.729 0.857 0.019  0.143  0.019  333 THR CCC CG2 
2579  N N   . ASN C 5   ? 1.050 0.627 0.670 -0.002 0.071  -0.006 334 ASN CCC N   
2580  C CA  . ASN C 5   ? 1.014 0.646 0.643 0.010  0.028  0.001  334 ASN CCC CA  
2581  C C   . ASN C 5   ? 0.951 0.586 0.625 0.026  0.025  0.019  334 ASN CCC C   
2582  O O   . ASN C 5   ? 0.938 0.547 0.623 0.019  0.053  0.016  334 ASN CCC O   
2583  C CB  . ASN C 5   ? 1.033 0.722 0.642 -0.015 0.014  -0.032 334 ASN CCC CB  
2584  C CG  . ASN C 5   ? 1.053 0.720 0.666 -0.054 0.054  -0.064 334 ASN CCC CG  
2585  O OD1 . ASN C 5   ? 1.068 0.668 0.667 -0.070 0.099  -0.071 334 ASN CCC OD1 
2586  N ND2 . ASN C 5   ? 1.049 0.761 0.677 -0.071 0.046  -0.084 334 ASN CCC ND2 
2587  N N   . LEU C 6   ? 0.918 0.577 0.607 0.046  -0.001 0.038  335 LEU CCC N   
2588  C CA  . LEU C 6   ? 0.870 0.545 0.596 0.057  -0.006 0.053  335 LEU CCC CA  
2589  C C   . LEU C 6   ? 0.851 0.549 0.585 0.047  -0.017 0.040  335 LEU CCC C   
2590  O O   . LEU C 6   ? 0.856 0.583 0.573 0.039  -0.032 0.021  335 LEU CCC O   
2591  C CB  . LEU C 6   ? 0.866 0.554 0.596 0.066  -0.020 0.065  335 LEU CCC CB  
2592  C CG  . LEU C 6   ? 0.905 0.581 0.631 0.065  -0.003 0.070  335 LEU CCC CG  
2593  C CD1 . LEU C 6   ? 0.909 0.590 0.631 0.058  -0.003 0.071  335 LEU CCC CD1 
2594  C CD2 . LEU C 6   ? 0.894 0.593 0.656 0.073  0.015  0.079  335 LEU CCC CD2 
2595  N N   . CYS C 7   ? 0.843 0.535 0.599 0.050  -0.005 0.049  336 CYS CCC N   
2596  C CA  . CYS C 7   ? 0.868 0.572 0.630 0.037  -0.006 0.035  336 CYS CCC CA  
2597  C C   . CYS C 7   ? 0.833 0.585 0.608 0.043  -0.041 0.034  336 CYS CCC C   
2598  O O   . CYS C 7   ? 0.805 0.562 0.587 0.058  -0.052 0.053  336 CYS CCC O   
2599  C CB  . CYS C 7   ? 0.875 0.550 0.645 0.048  0.019  0.055  336 CYS CCC CB  
2600  S SG  . CYS C 7   ? 0.961 0.551 0.701 0.051  0.081  0.059  336 CYS CCC SG  
2601  N N   . PRO C 8   ? 0.840 0.633 0.615 0.031  -0.054 0.010  337 PRO CCC N   
2602  C CA  . PRO C 8   ? 0.810 0.646 0.593 0.049  -0.081 0.013  337 PRO CCC CA  
2603  C C   . PRO C 8   ? 0.772 0.609 0.579 0.048  -0.082 0.020  337 PRO CCC C   
2604  O O   . PRO C 8   ? 0.758 0.633 0.580 0.040  -0.087 0.002  337 PRO CCC O   
2605  C CB  . PRO C 8   ? 0.824 0.728 0.601 0.038  -0.091 -0.018 337 PRO CCC CB  
2606  C CG  . PRO C 8   ? 0.851 0.741 0.631 -0.006 -0.061 -0.048 337 PRO CCC CG  
2607  C CD  . PRO C 8   ? 0.878 0.681 0.645 -0.004 -0.034 -0.025 337 PRO CCC CD  
2608  N N   . PHE C 9   ? 0.742 0.551 0.554 0.053  -0.076 0.042  338 PHE CCC N   
2609  C CA  . PHE C 9   ? 0.734 0.552 0.563 0.049  -0.076 0.048  338 PHE CCC CA  
2610  C C   . PHE C 9   ? 0.711 0.544 0.542 0.056  -0.086 0.043  338 PHE CCC C   
2611  O O   . PHE C 9   ? 0.659 0.507 0.505 0.048  -0.087 0.036  338 PHE CCC O   
2612  C CB  . PHE C 9   ? 0.743 0.561 0.575 0.052  -0.069 0.068  338 PHE CCC CB  
2613  C CG  . PHE C 9   ? 0.773 0.578 0.602 0.060  -0.052 0.083  338 PHE CCC CG  
2614  C CD1 . PHE C 9   ? 0.808 0.589 0.629 0.056  -0.036 0.080  338 PHE CCC CD1 
2615  C CD2 . PHE C 9   ? 0.791 0.604 0.622 0.075  -0.044 0.099  338 PHE CCC CD2 
2616  C CE1 . PHE C 9   ? 0.878 0.619 0.681 0.072  -0.005 0.099  338 PHE CCC CE1 
2617  C CE2 . PHE C 9   ? 0.851 0.646 0.675 0.097  -0.020 0.120  338 PHE CCC CE2 
2618  C CZ  . PHE C 9   ? 0.900 0.648 0.704 0.099  0.003  0.123  338 PHE CCC CZ  
2619  N N   . GLY C 10  ? 0.717 0.533 0.526 0.075  -0.088 0.048  339 GLY CCC N   
2620  C CA  . GLY C 10  ? 0.700 0.510 0.498 0.096  -0.084 0.050  339 GLY CCC CA  
2621  C C   . GLY C 10  ? 0.694 0.559 0.512 0.108  -0.098 0.037  339 GLY CCC C   
2622  O O   . GLY C 10  ? 0.645 0.511 0.472 0.114  -0.091 0.035  339 GLY CCC O   
2623  N N   . GLU C 11  ? 0.707 0.623 0.533 0.104  -0.111 0.022  340 GLU CCC N   
2624  C CA  . GLU C 11  ? 0.716 0.716 0.566 0.106  -0.123 -0.003 340 GLU CCC CA  
2625  C C   . GLU C 11  ? 0.683 0.686 0.563 0.073  -0.113 -0.020 340 GLU CCC C   
2626  O O   . GLU C 11  ? 0.708 0.775 0.612 0.077  -0.117 -0.039 340 GLU CCC O   
2627  C CB  . GLU C 11  ? 0.747 0.808 0.596 0.088  -0.130 -0.028 340 GLU CCC CB  
2628  C CG  . GLU C 11  ? 0.817 0.892 0.631 0.123  -0.142 -0.013 340 GLU CCC CG  
2629  C CD  . GLU C 11  ? 0.878 1.029 0.686 0.095  -0.149 -0.047 340 GLU CCC CD  
2630  O OE1 . GLU C 11  ? 0.886 1.086 0.720 0.048  -0.139 -0.088 340 GLU CCC OE1 
2631  O OE2 . GLU C 11  ? 0.969 1.127 0.741 0.115  -0.156 -0.036 340 GLU CCC OE2 
2632  N N   . VAL C 12  ? 0.639 0.582 0.514 0.047  -0.100 -0.011 341 VAL CCC N   
2633  C CA  . VAL C 12  ? 0.608 0.541 0.496 0.020  -0.087 -0.019 341 VAL CCC CA  
2634  C C   . VAL C 12  ? 0.587 0.504 0.477 0.028  -0.086 -0.006 341 VAL CCC C   
2635  O O   . VAL C 12  ? 0.585 0.527 0.492 0.024  -0.082 -0.021 341 VAL CCC O   
2636  C CB  . VAL C 12  ? 0.630 0.512 0.500 0.002  -0.068 -0.008 341 VAL CCC CB  
2637  C CG1 . VAL C 12  ? 0.640 0.504 0.508 -0.016 -0.051 -0.009 341 VAL CCC CG1 
2638  C CG2 . VAL C 12  ? 0.668 0.543 0.526 -0.012 -0.055 -0.025 341 VAL CCC CG2 
2639  N N   . PHE C 13  ? 0.577 0.458 0.451 0.032  -0.083 0.015  342 PHE CCC N   
2640  C CA  . PHE C 13  ? 0.585 0.452 0.454 0.021  -0.072 0.018  342 PHE CCC CA  
2641  C C   . PHE C 13  ? 0.620 0.472 0.484 0.041  -0.061 0.013  342 PHE CCC C   
2642  O O   . PHE C 13  ? 0.631 0.473 0.495 0.027  -0.045 0.005  342 PHE CCC O   
2643  C CB  . PHE C 13  ? 0.574 0.430 0.427 0.012  -0.068 0.031  342 PHE CCC CB  
2644  C CG  . PHE C 13  ? 0.551 0.432 0.407 0.003  -0.072 0.043  342 PHE CCC CG  
2645  C CD1 . PHE C 13  ? 0.561 0.433 0.416 0.017  -0.074 0.055  342 PHE CCC CD1 
2646  C CD2 . PHE C 13  ? 0.553 0.466 0.406 -0.015 -0.069 0.046  342 PHE CCC CD2 
2647  C CE1 . PHE C 13  ? 0.559 0.440 0.406 0.025  -0.068 0.075  342 PHE CCC CE1 
2648  C CE2 . PHE C 13  ? 0.557 0.499 0.404 -0.005 -0.071 0.067  342 PHE CCC CE2 
2649  C CZ  . PHE C 13  ? 0.563 0.482 0.406 0.020  -0.068 0.085  342 PHE CCC CZ  
2650  N N   . ASN C 14  ? 0.667 0.515 0.520 0.078  -0.065 0.020  343 ASN CCC N   
2651  C CA  . ASN C 14  ? 0.728 0.548 0.560 0.118  -0.046 0.029  343 ASN CCC CA  
2652  C C   . ASN C 14  ? 0.721 0.617 0.575 0.160  -0.064 0.025  343 ASN CCC C   
2653  O O   . ASN C 14  ? 0.762 0.652 0.592 0.216  -0.054 0.043  343 ASN CCC O   
2654  C CB  . ASN C 14  ? 0.791 0.543 0.576 0.137  -0.027 0.047  343 ASN CCC CB  
2655  C CG  . ASN C 14  ? 0.841 0.537 0.605 0.091  0.000  0.041  343 ASN CCC CG  
2656  O OD1 . ASN C 14  ? 0.802 0.497 0.574 0.057  0.015  0.025  343 ASN CCC OD1 
2657  N ND2 . ASN C 14  ? 0.948 0.612 0.686 0.086  0.008  0.047  343 ASN CCC ND2 
2658  N N   . ALA C 15  ? 0.697 0.666 0.589 0.135  -0.085 0.002  344 ALA CCC N   
2659  C CA  . ALA C 15  ? 0.692 0.767 0.615 0.157  -0.099 -0.017 344 ALA CCC CA  
2660  C C   . ALA C 15  ? 0.731 0.809 0.660 0.199  -0.081 -0.010 344 ALA CCC C   
2661  O O   . ALA C 15  ? 0.718 0.728 0.642 0.177  -0.057 -0.010 344 ALA CCC O   
2662  C CB  . ALA C 15  ? 0.647 0.774 0.603 0.103  -0.104 -0.053 344 ALA CCC CB  
2663  N N   . THR C 16  ? 0.788 0.949 0.723 0.261  -0.089 -0.003 345 THR CCC N   
2664  C CA  . THR C 16  ? 0.867 1.035 0.804 0.323  -0.066 0.012  345 THR CCC CA  
2665  C C   . THR C 16  ? 0.833 1.062 0.825 0.287  -0.062 -0.024 345 THR CCC C   
2666  O O   . THR C 16  ? 0.908 1.090 0.898 0.308  -0.030 -0.017 345 THR CCC O   
2667  C CB  . THR C 16  ? 0.953 1.216 0.877 0.412  -0.080 0.036  345 THR CCC CB  
2668  O OG1 . THR C 16  ? 0.876 1.294 0.841 0.384  -0.121 0.001  345 THR CCC OG1 
2669  C CG2 . THR C 16  ? 1.037 1.194 0.887 0.455  -0.065 0.080  345 THR CCC CG2 
2670  N N   . ARG C 17  ? 0.785 1.099 0.816 0.229  -0.085 -0.064 346 ARG CCC N   
2671  C CA  . ARG C 17  ? 0.749 1.115 0.825 0.183  -0.076 -0.104 346 ARG CCC CA  
2672  C C   . ARG C 17  ? 0.676 0.965 0.739 0.101  -0.071 -0.120 346 ARG CCC C   
2673  O O   . ARG C 17  ? 0.611 0.884 0.656 0.078  -0.084 -0.119 346 ARG CCC O   
2674  C CB  . ARG C 17  ? 0.782 1.331 0.909 0.185  -0.096 -0.145 346 ARG CCC CB  
2675  C CG  . ARG C 17  ? 0.849 1.492 1.024 0.213  -0.083 -0.163 346 ARG CCC CG  
2676  C CD  . ARG C 17  ? 0.867 1.672 1.099 0.160  -0.088 -0.229 346 ARG CCC CD  
2677  N NE  . ARG C 17  ? 0.914 1.932 1.190 0.220  -0.110 -0.243 346 ARG CCC NE  
2678  C CZ  . ARG C 17  ? 0.940 2.094 1.220 0.218  -0.139 -0.264 346 ARG CCC CZ  
2679  N NH1 . ARG C 17  ? 0.937 2.013 1.179 0.158  -0.144 -0.271 346 ARG CCC NH1 
2680  N NH2 . ARG C 17  ? 0.977 2.354 1.298 0.279  -0.161 -0.276 346 ARG CCC NH2 
2681  N N   . PHE C 18  ? 0.593 0.595 0.536 0.042  -0.018 0.044  347 PHE CCC N   
2682  C CA  . PHE C 18  ? 0.563 0.574 0.517 0.016  -0.037 0.028  347 PHE CCC CA  
2683  C C   . PHE C 18  ? 0.539 0.576 0.505 0.009  -0.054 0.022  347 PHE CCC C   
2684  O O   . PHE C 18  ? 0.582 0.623 0.551 0.017  -0.047 0.026  347 PHE CCC O   
2685  C CB  . PHE C 18  ? 0.552 0.544 0.516 -0.005 -0.023 0.020  347 PHE CCC CB  
2686  C CG  . PHE C 18  ? 0.563 0.543 0.523 -0.010 -0.018 0.018  347 PHE CCC CG  
2687  C CD1 . PHE C 18  ? 0.610 0.569 0.559 0.006  -0.000 0.029  347 PHE CCC CD1 
2688  C CD2 . PHE C 18  ? 0.553 0.547 0.521 -0.028 -0.028 0.009  347 PHE CCC CD2 
2689  C CE1 . PHE C 18  ? 0.633 0.584 0.581 0.000  0.006  0.028  347 PHE CCC CE1 
2690  C CE2 . PHE C 18  ? 0.558 0.548 0.525 -0.032 -0.022 0.008  347 PHE CCC CE2 
2691  C CZ  . PHE C 18  ? 0.608 0.576 0.566 -0.019 -0.006 0.017  347 PHE CCC CZ  
2692  N N   . ALA C 19  ? 0.509 0.561 0.482 -0.003 -0.071 0.012  348 ALA CCC N   
2693  C CA  . ALA C 19  ? 0.480 0.553 0.467 -0.012 -0.082 0.005  348 ALA CCC CA  
2694  C C   . ALA C 19  ? 0.472 0.538 0.470 -0.025 -0.077 0.004  348 ALA CCC C   
2695  O O   . ALA C 19  ? 0.468 0.520 0.464 -0.033 -0.068 0.003  348 ALA CCC O   
2696  C CB  . ALA C 19  ? 0.479 0.559 0.471 -0.022 -0.093 -0.005 348 ALA CCC CB  
2697  N N   . SER C 20  ? 0.481 0.562 0.491 -0.027 -0.080 0.002  349 SER CCC N   
2698  C CA  . SER C 20  ? 0.503 0.586 0.525 -0.039 -0.079 0.000  349 SER CCC CA  
2699  C C   . SER C 20  ? 0.484 0.566 0.510 -0.049 -0.083 -0.002 349 SER CCC C   
2700  O O   . SER C 20  ? 0.513 0.596 0.540 -0.049 -0.088 -0.006 349 SER CCC O   
2701  C CB  . SER C 20  ? 0.525 0.626 0.560 -0.038 -0.082 -0.000 349 SER CCC CB  
2702  O OG  . SER C 20  ? 0.578 0.678 0.609 -0.027 -0.074 0.005  349 SER CCC OG  
2703  N N   . VAL C 21  ? 0.468 0.552 0.495 -0.054 -0.077 0.000  350 VAL CCC N   
2704  C CA  . VAL C 21  ? 0.492 0.579 0.521 -0.056 -0.076 0.005  350 VAL CCC CA  
2705  C C   . VAL C 21  ? 0.522 0.606 0.565 -0.058 -0.075 0.006  350 VAL CCC C   
2706  O O   . VAL C 21  ? 0.533 0.606 0.575 -0.058 -0.071 0.007  350 VAL CCC O   
2707  C CB  . VAL C 21  ? 0.459 0.564 0.487 -0.057 -0.071 0.008  350 VAL CCC CB  
2708  C CG1 . VAL C 21  ? 0.445 0.562 0.481 -0.058 -0.068 0.010  350 VAL CCC CG1 
2709  C CG2 . VAL C 21  ? 0.470 0.584 0.495 -0.052 -0.067 0.018  350 VAL CCC CG2 
2710  N N   . TYR C 22  ? 0.533 0.624 0.588 -0.061 -0.075 0.003  351 TYR CCC N   
2711  C CA  . TYR C 22  ? 0.528 0.616 0.602 -0.067 -0.069 0.001  351 TYR CCC CA  
2712  C C   . TYR C 22  ? 0.524 0.609 0.601 -0.073 -0.074 -0.014 351 TYR CCC C   
2713  O O   . TYR C 22  ? 0.549 0.623 0.639 -0.082 -0.064 -0.021 351 TYR CCC O   
2714  C CB  . TYR C 22  ? 0.514 0.616 0.604 -0.070 -0.067 0.000  351 TYR CCC CB  
2715  C CG  . TYR C 22  ? 0.498 0.617 0.594 -0.072 -0.077 -0.011 351 TYR CCC CG  
2716  C CD1 . TYR C 22  ? 0.482 0.609 0.565 -0.062 -0.084 -0.009 351 TYR CCC CD1 
2717  C CD2 . TYR C 22  ? 0.491 0.623 0.608 -0.082 -0.078 -0.025 351 TYR CCC CD2 
2718  C CE1 . TYR C 22  ? 0.491 0.639 0.577 -0.056 -0.091 -0.014 351 TYR CCC CE1 
2719  C CE2 . TYR C 22  ? 0.480 0.643 0.601 -0.081 -0.089 -0.036 351 TYR CCC CE2 
2720  C CZ  . TYR C 22  ? 0.481 0.654 0.585 -0.064 -0.096 -0.027 351 TYR CCC CZ  
2721  O OH  . TYR C 22  ? 0.504 0.713 0.610 -0.055 -0.105 -0.031 351 TYR CCC OH  
2722  N N   . ALA C 23  ? 0.503 0.598 0.568 -0.068 -0.086 -0.020 352 ALA CCC N   
2723  C CA  . ALA C 23  ? 0.499 0.605 0.562 -0.069 -0.093 -0.034 352 ALA CCC CA  
2724  C C   . ALA C 23  ? 0.494 0.585 0.535 -0.060 -0.095 -0.030 352 ALA CCC C   
2725  O O   . ALA C 23  ? 0.498 0.602 0.527 -0.051 -0.103 -0.033 352 ALA CCC O   
2726  C CB  . ALA C 23  ? 0.480 0.620 0.546 -0.062 -0.104 -0.040 352 ALA CCC CB  
2727  N N   . TRP C 24  ? 0.491 0.560 0.528 -0.061 -0.087 -0.021 353 TRP CCC N   
2728  C CA  . TRP C 24  ? 0.504 0.561 0.522 -0.053 -0.087 -0.014 353 TRP CCC CA  
2729  C C   . TRP C 24  ? 0.520 0.576 0.530 -0.052 -0.091 -0.026 353 TRP CCC C   
2730  O O   . TRP C 24  ? 0.550 0.608 0.570 -0.060 -0.089 -0.040 353 TRP CCC O   
2731  C CB  . TRP C 24  ? 0.493 0.540 0.511 -0.053 -0.077 -0.002 353 TRP CCC CB  
2732  C CG  . TRP C 24  ? 0.522 0.555 0.551 -0.057 -0.064 -0.002 353 TRP CCC CG  
2733  C CD1 . TRP C 24  ? 0.531 0.564 0.574 -0.059 -0.054 0.004  353 TRP CCC CD1 
2734  C CD2 . TRP C 24  ? 0.543 0.555 0.568 -0.056 -0.054 -0.005 353 TRP CCC CD2 
2735  N NE1 . TRP C 24  ? 0.530 0.541 0.582 -0.061 -0.035 0.005  353 TRP CCC NE1 
2736  C CE2 . TRP C 24  ? 0.548 0.545 0.589 -0.060 -0.035 -0.001 353 TRP CCC CE2 
2737  C CE3 . TRP C 24  ? 0.538 0.542 0.549 -0.053 -0.057 -0.010 353 TRP CCC CE3 
2738  C CZ2 . TRP C 24  ? 0.578 0.545 0.621 -0.061 -0.016 -0.003 353 TRP CCC CZ2 
2739  C CZ3 . TRP C 24  ? 0.564 0.542 0.575 -0.054 -0.042 -0.013 353 TRP CCC CZ3 
2740  C CH2 . TRP C 24  ? 0.594 0.552 0.620 -0.058 -0.020 -0.010 353 TRP CCC CH2 
2741  N N   . ASN C 25  ? 0.543 0.598 0.535 -0.041 -0.094 -0.021 354 ASN CCC N   
2742  C CA  . ASN C 25  ? 0.571 0.631 0.550 -0.034 -0.099 -0.029 354 ASN CCC CA  
2743  C C   . ASN C 25  ? 0.558 0.595 0.528 -0.035 -0.092 -0.027 354 ASN CCC C   
2744  O O   . ASN C 25  ? 0.557 0.582 0.525 -0.032 -0.086 -0.013 354 ASN CCC O   
2745  C CB  . ASN C 25  ? 0.601 0.671 0.565 -0.017 -0.102 -0.021 354 ASN CCC CB  
2746  C CG  . ASN C 25  ? 0.666 0.750 0.613 -0.005 -0.107 -0.027 354 ASN CCC CG  
2747  O OD1 . ASN C 25  ? 0.726 0.794 0.659 0.002  -0.102 -0.022 354 ASN CCC OD1 
2748  N ND2 . ASN C 25  ? 0.697 0.818 0.647 -0.003 -0.117 -0.042 354 ASN CCC ND2 
2749  N N   . ARG C 26  ? 0.557 0.592 0.524 -0.038 -0.091 -0.042 355 ARG CCC N   
2750  C CA  . ARG C 26  ? 0.569 0.582 0.525 -0.035 -0.083 -0.041 355 ARG CCC CA  
2751  C C   . ARG C 26  ? 0.566 0.590 0.502 -0.024 -0.090 -0.048 355 ARG CCC C   
2752  O O   . ARG C 26  ? 0.574 0.623 0.509 -0.027 -0.097 -0.069 355 ARG CCC O   
2753  C CB  . ARG C 26  ? 0.603 0.602 0.568 -0.048 -0.073 -0.061 355 ARG CCC CB  
2754  C CG  . ARG C 26  ? 0.641 0.609 0.617 -0.052 -0.053 -0.050 355 ARG CCC CG  
2755  C CD  . ARG C 26  ? 0.656 0.595 0.621 -0.047 -0.036 -0.048 355 ARG CCC CD  
2756  N NE  . ARG C 26  ? 0.695 0.624 0.664 -0.038 -0.025 -0.020 355 ARG CCC NE  
2757  C CZ  . ARG C 26  ? 0.686 0.591 0.665 -0.035 -0.001 -0.009 355 ARG CCC CZ  
2758  N NH1 . ARG C 26  ? 0.733 0.607 0.720 -0.046 0.020  -0.026 355 ARG CCC NH1 
2759  N NH2 . ARG C 26  ? 0.662 0.576 0.641 -0.022 0.005  0.018  355 ARG CCC NH2 
2760  N N   . LYS C 27  ? 0.569 0.580 0.489 -0.012 -0.086 -0.034 356 LYS CCC N   
2761  C CA  . LYS C 27  ? 0.639 0.655 0.538 0.001  -0.088 -0.039 356 LYS CCC CA  
2762  C C   . LYS C 27  ? 0.639 0.627 0.532 -0.001 -0.076 -0.039 356 LYS CCC C   
2763  O O   . LYS C 27  ? 0.635 0.606 0.534 -0.000 -0.067 -0.022 356 LYS CCC O   
2764  C CB  . LYS C 27  ? 0.687 0.708 0.573 0.019  -0.088 -0.020 356 LYS CCC CB  
2765  C CG  . LYS C 27  ? 0.758 0.788 0.620 0.037  -0.089 -0.020 356 LYS CCC CG  
2766  C CD  . LYS C 27  ? 0.820 0.852 0.670 0.058  -0.082 0.001  356 LYS CCC CD  
2767  C CE  . LYS C 27  ? 0.907 0.956 0.731 0.081  -0.082 0.001  356 LYS CCC CE  
2768  N NZ  . LYS C 27  ? 0.965 0.994 0.777 0.100  -0.066 0.026  356 LYS CCC NZ  
2769  N N   . ARG C 28  ? 0.663 0.653 0.546 -0.002 -0.075 -0.059 357 ARG CCC N   
2770  C CA  . ARG C 28  ? 0.685 0.647 0.556 0.001  -0.062 -0.059 357 ARG CCC CA  
2771  C C   . ARG C 28  ? 0.655 0.621 0.505 0.022  -0.064 -0.042 357 ARG CCC C   
2772  O O   . ARG C 28  ? 0.666 0.658 0.503 0.033  -0.074 -0.045 357 ARG CCC O   
2773  C CB  . ARG C 28  ? 0.738 0.699 0.607 -0.010 -0.057 -0.092 357 ARG CCC CB  
2774  C CG  . ARG C 28  ? 0.795 0.719 0.653 -0.008 -0.038 -0.092 357 ARG CCC CG  
2775  C CD  . ARG C 28  ? 0.870 0.798 0.720 -0.018 -0.032 -0.130 357 ARG CCC CD  
2776  N NE  . ARG C 28  ? 0.942 0.829 0.810 -0.036 -0.007 -0.143 357 ARG CCC NE  
2777  C CZ  . ARG C 28  ? 1.011 0.902 0.902 -0.060 -0.002 -0.169 357 ARG CCC CZ  
2778  N NH1 . ARG C 28  ? 0.993 0.936 0.893 -0.068 -0.024 -0.187 357 ARG CCC NH1 
2779  N NH2 . ARG C 28  ? 1.079 0.924 0.988 -0.074 0.030  -0.176 357 ARG CCC NH2 
2780  N N   . ILE C 29  ? 0.647 0.590 0.494 0.028  -0.053 -0.024 358 ILE CCC N   
2781  C CA  . ILE C 29  ? 0.651 0.592 0.481 0.045  -0.049 -0.009 358 ILE CCC CA  
2782  C C   . ILE C 29  ? 0.684 0.601 0.501 0.049  -0.037 -0.014 358 ILE CCC C   
2783  O O   . ILE C 29  ? 0.667 0.564 0.496 0.043  -0.024 -0.008 358 ILE CCC O   
2784  C CB  . ILE C 29  ? 0.630 0.570 0.472 0.047  -0.045 0.015  358 ILE CCC CB  
2785  C CG1 . ILE C 29  ? 0.608 0.565 0.457 0.045  -0.053 0.017  358 ILE CCC CG1 
2786  C CG2 . ILE C 29  ? 0.630 0.564 0.460 0.061  -0.035 0.030  358 ILE CCC CG2 
2787  C CD1 . ILE C 29  ? 0.596 0.555 0.463 0.038  -0.048 0.030  358 ILE CCC CD1 
2788  N N   . SER C 30  ? 0.716 0.640 0.510 0.061  -0.038 -0.023 359 SER CCC N   
2789  C CA  . SER C 30  ? 0.755 0.656 0.534 0.065  -0.024 -0.032 359 SER CCC CA  
2790  C C   . SER C 30  ? 0.752 0.665 0.503 0.085  -0.026 -0.030 359 SER CCC C   
2791  O O   . SER C 30  ? 0.734 0.675 0.477 0.096  -0.037 -0.026 359 SER CCC O   
2792  C CB  . SER C 30  ? 0.785 0.678 0.568 0.048  -0.019 -0.065 359 SER CCC CB  
2793  O OG  . SER C 30  ? 0.772 0.703 0.554 0.041  -0.037 -0.088 359 SER CCC OG  
2794  N N   . ASN C 31  ? 0.785 0.676 0.521 0.093  -0.012 -0.031 360 ASN CCC N   
2795  C CA  . ASN C 31  ? 0.828 0.728 0.534 0.114  -0.011 -0.030 360 ASN CCC CA  
2796  C C   . ASN C 31  ? 0.807 0.721 0.513 0.131  -0.014 -0.000 360 ASN CCC C   
2797  O O   . ASN C 31  ? 0.813 0.754 0.500 0.147  -0.022 -0.001 360 ASN CCC O   
2798  C CB  . ASN C 31  ? 0.865 0.796 0.552 0.114  -0.021 -0.065 360 ASN CCC CB  
2799  C CG  . ASN C 31  ? 0.922 0.835 0.615 0.090  -0.012 -0.101 360 ASN CCC CG  
2800  O OD1 . ASN C 31  ? 0.972 0.852 0.657 0.091  0.007  -0.107 360 ASN CCC OD1 
2801  N ND2 . ASN C 31  ? 0.943 0.875 0.655 0.070  -0.021 -0.124 360 ASN CCC ND2 
2802  N N   . CYS C 32  ? 0.775 0.673 0.500 0.128  -0.006 0.025  361 CYS CCC N   
2803  C CA  . CYS C 32  ? 0.772 0.677 0.504 0.138  -0.002 0.050  361 CYS CCC CA  
2804  C C   . CYS C 32  ? 0.743 0.637 0.495 0.133  0.011  0.069  361 CYS CCC C   
2805  O O   . CYS C 32  ? 0.723 0.609 0.486 0.123  0.013  0.067  361 CYS CCC O   
2806  C CB  . CYS C 32  ? 0.758 0.680 0.503 0.130  -0.012 0.049  361 CYS CCC CB  
2807  S SG  . CYS C 32  ? 0.755 0.675 0.531 0.103  -0.020 0.040  361 CYS CCC SG  
2808  N N   . VAL C 33  ? 0.733 0.631 0.490 0.141  0.022  0.088  362 VAL CCC N   
2809  C CA  . VAL C 33  ? 0.710 0.613 0.491 0.134  0.033  0.104  362 VAL CCC CA  
2810  C C   . VAL C 33  ? 0.700 0.619 0.510 0.114  0.029  0.102  362 VAL CCC C   
2811  O O   . VAL C 33  ? 0.676 0.593 0.487 0.114  0.031  0.102  362 VAL CCC O   
2812  C CB  . VAL C 33  ? 0.718 0.617 0.494 0.149  0.051  0.120  362 VAL CCC CB  
2813  C CG1 . VAL C 33  ? 0.693 0.609 0.498 0.138  0.063  0.131  362 VAL CCC CG1 
2814  C CG2 . VAL C 33  ? 0.734 0.619 0.477 0.171  0.055  0.121  362 VAL CCC CG2 
2815  N N   . ALA C 34  ? 0.705 0.639 0.535 0.101  0.026  0.101  363 ALA CCC N   
2816  C CA  . ALA C 34  ? 0.696 0.652 0.552 0.082  0.021  0.097  363 ALA CCC CA  
2817  C C   . ALA C 34  ? 0.694 0.676 0.574 0.073  0.034  0.103  363 ALA CCC C   
2818  O O   . ALA C 34  ? 0.677 0.687 0.570 0.073  0.036  0.110  363 ALA CCC O   
2819  C CB  . ALA C 34  ? 0.677 0.644 0.541 0.076  0.013  0.094  363 ALA CCC CB  
2820  N N   . ASP C 35  ? 0.712 0.685 0.598 0.068  0.045  0.102  364 ASP CCC N   
2821  C CA  . ASP C 35  ? 0.703 0.700 0.619 0.052  0.061  0.100  364 ASP CCC CA  
2822  C C   . ASP C 35  ? 0.696 0.715 0.636 0.028  0.057  0.085  364 ASP CCC C   
2823  O O   . ASP C 35  ? 0.696 0.690 0.634 0.024  0.060  0.079  364 ASP CCC O   
2824  C CB  . ASP C 35  ? 0.738 0.707 0.651 0.059  0.084  0.108  364 ASP CCC CB  
2825  C CG  . ASP C 35  ? 0.746 0.741 0.691 0.042  0.105  0.104  364 ASP CCC CG  
2826  O OD1 . ASP C 35  ? 0.721 0.764 0.691 0.023  0.097  0.093  364 ASP CCC OD1 
2827  O OD2 . ASP C 35  ? 0.791 0.765 0.737 0.049  0.129  0.113  364 ASP CCC OD2 
2828  N N   . TYR C 36  ? 0.673 0.742 0.636 0.014  0.052  0.078  365 TYR CCC N   
2829  C CA  . TYR C 36  ? 0.646 0.747 0.630 -0.009 0.047  0.061  365 TYR CCC CA  
2830  C C   . TYR C 36  ? 0.629 0.752 0.646 -0.035 0.068  0.043  365 TYR CCC C   
2831  O O   . TYR C 36  ? 0.610 0.762 0.647 -0.058 0.067  0.023  365 TYR CCC O   
2832  C CB  . TYR C 36  ? 0.649 0.802 0.638 -0.006 0.031  0.064  365 TYR CCC CB  
2833  C CG  . TYR C 36  ? 0.645 0.769 0.609 0.013  0.017  0.076  365 TYR CCC CG  
2834  C CD1 . TYR C 36  ? 0.659 0.773 0.621 0.007  0.006  0.068  365 TYR CCC CD1 
2835  C CD2 . TYR C 36  ? 0.668 0.770 0.611 0.035  0.018  0.092  365 TYR CCC CD2 
2836  C CE1 . TYR C 36  ? 0.684 0.770 0.627 0.020  -0.003 0.075  365 TYR CCC CE1 
2837  C CE2 . TYR C 36  ? 0.655 0.726 0.578 0.048  0.010  0.097  365 TYR CCC CE2 
2838  C CZ  . TYR C 36  ? 0.685 0.750 0.610 0.039  -0.000 0.087  365 TYR CCC CZ  
2839  O OH  . TYR C 36  ? 0.734 0.771 0.645 0.047  -0.005 0.088  365 TYR CCC OH  
2840  N N   . SER C 37  ? 0.647 0.756 0.670 -0.034 0.089  0.048  366 SER CCC N   
2841  C CA  . SER C 37  ? 0.664 0.790 0.723 -0.064 0.116  0.028  366 SER CCC CA  
2842  C C   . SER C 37  ? 0.676 0.759 0.740 -0.078 0.133  0.015  366 SER CCC C   
2843  O O   . SER C 37  ? 0.706 0.810 0.803 -0.110 0.152  -0.012 366 SER CCC O   
2844  C CB  . SER C 37  ? 0.672 0.790 0.739 -0.060 0.139  0.036  366 SER CCC CB  
2845  O OG  . SER C 37  ? 0.710 0.769 0.743 -0.029 0.142  0.061  366 SER CCC OG  
2846  N N   . VAL C 38  ? 0.692 0.721 0.724 -0.055 0.126  0.030  367 VAL CCC N   
2847  C CA  . VAL C 38  ? 0.724 0.715 0.758 -0.063 0.141  0.023  367 VAL CCC CA  
2848  C C   . VAL C 38  ? 0.709 0.741 0.761 -0.089 0.127  -0.002 367 VAL CCC C   
2849  O O   . VAL C 38  ? 0.763 0.789 0.839 -0.114 0.151  -0.024 367 VAL CCC O   
2850  C CB  . VAL C 38  ? 0.738 0.682 0.734 -0.029 0.132  0.046  367 VAL CCC CB  
2851  C CG1 . VAL C 38  ? 0.704 0.668 0.680 -0.018 0.093  0.049  367 VAL CCC CG1 
2852  C CG2 . VAL C 38  ? 0.766 0.666 0.762 -0.027 0.156  0.047  367 VAL CCC CG2 
2853  N N   . LEU C 39  ? 0.684 0.759 0.728 -0.083 0.094  -0.000 368 LEU CCC N   
2854  C CA  . LEU C 39  ? 0.676 0.797 0.734 -0.102 0.080  -0.020 368 LEU CCC CA  
2855  C C   . LEU C 39  ? 0.701 0.892 0.794 -0.132 0.089  -0.046 368 LEU CCC C   
2856  O O   . LEU C 39  ? 0.678 0.900 0.789 -0.157 0.091  -0.073 368 LEU CCC O   
2857  C CB  . LEU C 39  ? 0.644 0.785 0.681 -0.082 0.048  -0.005 368 LEU CCC CB  
2858  C CG  . LEU C 39  ? 0.656 0.742 0.663 -0.058 0.037  0.014  368 LEU CCC CG  
2859  C CD1 . LEU C 39  ? 0.660 0.765 0.653 -0.044 0.013  0.024  368 LEU CCC CD1 
2860  C CD2 . LEU C 39  ? 0.649 0.700 0.654 -0.064 0.044  0.006  368 LEU CCC CD2 
2861  N N   . TYR C 40  ? 0.780 0.890 0.744 -0.026 0.067  -0.027 369 TYR CCC N   
2862  C CA  . TYR C 40  ? 0.788 0.940 0.806 -0.055 0.082  -0.035 369 TYR CCC CA  
2863  C C   . TYR C 40  ? 0.844 0.960 0.845 -0.090 0.112  -0.020 369 TYR CCC C   
2864  O O   . TYR C 40  ? 0.817 0.955 0.861 -0.120 0.113  -0.029 369 TYR CCC O   
2865  C CB  . TYR C 40  ? 0.774 0.986 0.818 -0.050 0.103  -0.050 369 TYR CCC CB  
2866  C CG  . TYR C 40  ? 0.757 1.003 0.824 -0.017 0.078  -0.070 369 TYR CCC CG  
2867  C CD1 . TYR C 40  ? 0.723 0.962 0.813 -0.004 0.041  -0.076 369 TYR CCC CD1 
2868  C CD2 . TYR C 40  ? 0.794 1.073 0.856 0.002  0.098  -0.082 369 TYR CCC CD2 
2869  C CE1 . TYR C 40  ? 0.727 0.978 0.828 0.027  0.024  -0.093 369 TYR CCC CE1 
2870  C CE2 . TYR C 40  ? 0.799 1.096 0.876 0.036  0.080  -0.102 369 TYR CCC CE2 
2871  C CZ  . TYR C 40  ? 0.776 1.053 0.869 0.048  0.043  -0.107 369 TYR CCC CZ  
2872  O OH  . TYR C 40  ? 0.837 1.116 0.938 0.081  0.029  -0.126 369 TYR CCC OH  
2873  N N   . ASN C 41  ? 0.938 0.994 0.871 -0.084 0.135  0.002  370 ASN CCC N   
2874  C CA  . ASN C 41  ? 1.064 1.063 0.964 -0.116 0.173  0.020  370 ASN CCC CA  
2875  C C   . ASN C 41  ? 1.096 1.026 0.967 -0.113 0.160  0.033  370 ASN CCC C   
2876  O O   . ASN C 41  ? 1.132 0.994 0.963 -0.134 0.192  0.049  370 ASN CCC O   
2877  C CB  . ASN C 41  ? 1.189 1.149 1.018 -0.106 0.212  0.042  370 ASN CCC CB  
2878  C CG  . ASN C 41  ? 1.190 1.218 1.048 -0.115 0.237  0.028  370 ASN CCC CG  
2879  O OD1 . ASN C 41  ? 1.149 1.236 1.076 -0.149 0.247  0.009  370 ASN CCC OD1 
2880  N ND2 . ASN C 41  ? 1.214 1.241 1.019 -0.082 0.245  0.035  370 ASN CCC ND2 
2881  N N   . SER C 42  ? 1.052 0.996 0.941 -0.089 0.118  0.026  371 SER CCC N   
2882  C CA  . SER C 42  ? 1.043 0.936 0.912 -0.081 0.104  0.035  371 SER CCC CA  
2883  C C   . SER C 42  ? 0.923 0.830 0.840 -0.113 0.096  0.018  371 SER CCC C   
2884  O O   . SER C 42  ? 0.866 0.838 0.836 -0.118 0.075  -0.001 371 SER CCC O   
2885  C CB  . SER C 42  ? 1.061 0.970 0.926 -0.042 0.068  0.035  371 SER CCC CB  
2886  O OG  . SER C 42  ? 1.123 1.029 0.942 -0.011 0.071  0.046  371 SER CCC OG  
2887  N N   . ALA C 43  ? 0.925 0.768 0.814 -0.130 0.111  0.024  372 ALA CCC N   
2888  C CA  . ALA C 43  ? 0.905 0.752 0.825 -0.161 0.103  0.005  372 ALA CCC CA  
2889  C C   . ALA C 43  ? 0.913 0.728 0.816 -0.137 0.083  0.009  372 ALA CCC C   
2890  O O   . ALA C 43  ? 0.910 0.733 0.833 -0.156 0.071  -0.008 372 ALA CCC O   
2891  C CB  . ALA C 43  ? 0.982 0.780 0.887 -0.208 0.141  0.001  372 ALA CCC CB  
2892  N N   . SER C 44  ? 0.897 0.681 0.762 -0.096 0.078  0.028  373 SER CCC N   
2893  C CA  . SER C 44  ? 0.846 0.607 0.699 -0.072 0.065  0.032  373 SER CCC CA  
2894  C C   . SER C 44  ? 0.727 0.554 0.621 -0.054 0.030  0.024  373 SER CCC C   
2895  O O   . SER C 44  ? 0.686 0.508 0.580 -0.040 0.020  0.024  373 SER CCC O   
2896  C CB  . SER C 44  ? 0.921 0.618 0.714 -0.037 0.080  0.055  373 SER CCC CB  
2897  O OG  . SER C 44  ? 1.017 0.627 0.768 -0.055 0.112  0.059  373 SER CCC OG  
2898  N N   . PHE C 45  ? 0.654 0.538 0.582 -0.056 0.014  0.016  374 PHE CCC N   
2899  C CA  . PHE C 45  ? 0.587 0.516 0.550 -0.048 -0.014 0.007  374 PHE CCC CA  
2900  C C   . PHE C 45  ? 0.570 0.502 0.551 -0.067 -0.021 -0.003 374 PHE CCC C   
2901  O O   . PHE C 45  ? 0.573 0.511 0.564 -0.091 -0.016 -0.013 374 PHE CCC O   
2902  C CB  . PHE C 45  ? 0.551 0.524 0.538 -0.045 -0.025 -0.001 374 PHE CCC CB  
2903  C CG  . PHE C 45  ? 0.565 0.541 0.530 -0.024 -0.023 0.004  374 PHE CCC CG  
2904  C CD1 . PHE C 45  ? 0.579 0.546 0.520 0.000  -0.028 0.013  374 PHE CCC CD1 
2905  C CD2 . PHE C 45  ? 0.576 0.574 0.544 -0.024 -0.017 -0.002 374 PHE CCC CD2 
2906  C CE1 . PHE C 45  ? 0.615 0.593 0.530 0.023  -0.032 0.016  374 PHE CCC CE1 
2907  C CE2 . PHE C 45  ? 0.593 0.594 0.531 -0.004 -0.015 0.002  374 PHE CCC CE2 
2908  C CZ  . PHE C 45  ? 0.613 0.604 0.522 0.020  -0.025 0.010  374 PHE CCC CZ  
2909  N N   . SER C 46  ? 0.555 0.487 0.538 -0.057 -0.032 -0.002 375 SER CCC N   
2910  C CA  . SER C 46  ? 0.559 0.490 0.546 -0.070 -0.039 -0.010 375 SER CCC CA  
2911  C C   . SER C 46  ? 0.514 0.483 0.528 -0.073 -0.058 -0.015 375 SER CCC C   
2912  O O   . SER C 46  ? 0.555 0.531 0.570 -0.084 -0.066 -0.023 375 SER CCC O   
2913  C CB  . SER C 46  ? 0.553 0.470 0.529 -0.057 -0.037 -0.004 375 SER CCC CB  
2914  O OG  . SER C 46  ? 0.519 0.464 0.514 -0.042 -0.046 0.001  375 SER CCC OG  
2915  N N   . THR C 47  ? 0.488 0.476 0.518 -0.061 -0.066 -0.014 376 THR CCC N   
2916  C CA  . THR C 47  ? 0.482 0.491 0.531 -0.056 -0.082 -0.018 376 THR CCC CA  
2917  C C   . THR C 47  ? 0.473 0.497 0.533 -0.046 -0.082 -0.022 376 THR CCC C   
2918  O O   . THR C 47  ? 0.438 0.456 0.489 -0.040 -0.076 -0.020 376 THR CCC O   
2919  C CB  . THR C 47  ? 0.482 0.478 0.527 -0.052 -0.089 -0.012 376 THR CCC CB  
2920  O OG1 . THR C 47  ? 0.487 0.485 0.536 -0.045 -0.101 -0.012 376 THR CCC OG1 
2921  C CG2 . THR C 47  ? 0.474 0.466 0.523 -0.048 -0.086 -0.010 376 THR CCC CG2 
2922  N N   . PHE C 48  ? 0.460 0.505 0.536 -0.040 -0.089 -0.029 377 PHE CCC N   
2923  C CA  . PHE C 48  ? 0.476 0.533 0.559 -0.027 -0.088 -0.036 377 PHE CCC CA  
2924  C C   . PHE C 48  ? 0.481 0.549 0.579 -0.012 -0.099 -0.042 377 PHE CCC C   
2925  O O   . PHE C 48  ? 0.467 0.572 0.584 -0.009 -0.100 -0.047 377 PHE CCC O   
2926  C CB  . PHE C 48  ? 0.478 0.553 0.559 -0.032 -0.071 -0.038 377 PHE CCC CB  
2927  C CG  . PHE C 48  ? 0.489 0.580 0.569 -0.018 -0.065 -0.047 377 PHE CCC CG  
2928  C CD1 . PHE C 48  ? 0.496 0.585 0.581 -0.001 -0.076 -0.057 377 PHE CCC CD1 
2929  C CD2 . PHE C 48  ? 0.528 0.630 0.597 -0.024 -0.044 -0.045 377 PHE CCC CD2 
2930  C CE1 . PHE C 48  ? 0.524 0.625 0.603 0.013  -0.069 -0.069 377 PHE CCC CE1 
2931  C CE2 . PHE C 48  ? 0.550 0.668 0.612 -0.010 -0.035 -0.053 377 PHE CCC CE2 
2932  C CZ  . PHE C 48  ? 0.559 0.680 0.627 0.010  -0.049 -0.067 377 PHE CCC CZ  
2933  N N   . LYS C 49  ? 0.505 0.540 0.594 -0.003 -0.108 -0.040 378 LYS CCC N   
2934  C CA  . LYS C 49  ? 0.544 0.567 0.634 0.018  -0.117 -0.041 378 LYS CCC CA  
2935  C C   . LYS C 49  ? 0.578 0.568 0.659 0.029  -0.116 -0.052 378 LYS CCC C   
2936  O O   . LYS C 49  ? 0.559 0.527 0.632 0.014  -0.113 -0.056 378 LYS CCC O   
2937  C CB  . LYS C 49  ? 0.572 0.560 0.643 0.017  -0.124 -0.027 378 LYS CCC CB  
2938  C CG  . LYS C 49  ? 0.558 0.569 0.627 0.007  -0.128 -0.019 378 LYS CCC CG  
2939  C CD  . LYS C 49  ? 0.579 0.546 0.618 0.008  -0.131 -0.004 378 LYS CCC CD  
2940  C CE  . LYS C 49  ? 0.586 0.567 0.609 0.003  -0.137 0.003  378 LYS CCC CE  
2941  N NZ  . LYS C 49  ? 0.646 0.580 0.630 0.015  -0.139 0.020  378 LYS CCC NZ  
2942  N N   . CYS C 50  ? 0.581 0.511 0.563 -0.046 -0.112 0.046  379 CYS CCC N   
2943  C CA  . CYS C 50  ? 0.594 0.521 0.587 -0.036 -0.109 0.045  379 CYS CCC CA  
2944  C C   . CYS C 50  ? 0.578 0.500 0.576 -0.037 -0.119 0.054  379 CYS CCC C   
2945  O O   . CYS C 50  ? 0.563 0.490 0.561 -0.043 -0.130 0.062  379 CYS CCC O   
2946  C CB  . CYS C 50  ? 0.610 0.547 0.624 -0.028 -0.103 0.042  379 CYS CCC CB  
2947  S SG  . CYS C 50  ? 0.608 0.548 0.613 -0.027 -0.092 0.034  379 CYS CCC SG  
2948  N N   . TYR C 51  ? 0.572 0.486 0.573 -0.032 -0.117 0.052  380 TYR CCC N   
2949  C CA  . TYR C 51  ? 0.574 0.478 0.579 -0.031 -0.124 0.061  380 TYR CCC CA  
2950  C C   . TYR C 51  ? 0.584 0.486 0.612 -0.020 -0.121 0.058  380 TYR CCC C   
2951  O O   . TYR C 51  ? 0.579 0.478 0.605 -0.016 -0.111 0.047  380 TYR CCC O   
2952  C CB  . TYR C 51  ? 0.573 0.466 0.557 -0.039 -0.122 0.060  380 TYR CCC CB  
2953  C CG  . TYR C 51  ? 0.579 0.473 0.539 -0.050 -0.123 0.060  380 TYR CCC CG  
2954  C CD1 . TYR C 51  ? 0.573 0.471 0.525 -0.051 -0.115 0.050  380 TYR CCC CD1 
2955  C CD2 . TYR C 51  ? 0.589 0.480 0.537 -0.058 -0.132 0.070  380 TYR CCC CD2 
2956  C CE1 . TYR C 51  ? 0.569 0.467 0.501 -0.061 -0.114 0.049  380 TYR CCC CE1 
2957  C CE2 . TYR C 51  ? 0.598 0.490 0.523 -0.069 -0.131 0.068  380 TYR CCC CE2 
2958  C CZ  . TYR C 51  ? 0.593 0.487 0.511 -0.070 -0.122 0.057  380 TYR CCC CZ  
2959  O OH  . TYR C 51  ? 0.575 0.468 0.473 -0.079 -0.120 0.054  380 TYR CCC OH  
2960  N N   . GLY C 52  ? 0.602 0.506 0.651 -0.015 -0.128 0.067  381 GLY CCC N   
2961  C CA  . GLY C 52  ? 0.605 0.506 0.678 -0.003 -0.124 0.064  381 GLY CCC CA  
2962  C C   . GLY C 52  ? 0.607 0.523 0.698 0.005  -0.116 0.057  381 GLY CCC C   
2963  O O   . GLY C 52  ? 0.651 0.566 0.767 0.015  -0.113 0.056  381 GLY CCC O   
2964  N N   . VAL C 53  ? 0.608 0.535 0.689 0.000  -0.112 0.053  382 VAL CCC N   
2965  C CA  . VAL C 53  ? 0.619 0.561 0.718 0.006  -0.104 0.049  382 VAL CCC CA  
2966  C C   . VAL C 53  ? 0.602 0.556 0.696 -0.003 -0.108 0.053  382 VAL CCC C   
2967  O O   . VAL C 53  ? 0.597 0.546 0.666 -0.012 -0.111 0.053  382 VAL CCC O   
2968  C CB  . VAL C 53  ? 0.650 0.588 0.740 0.011  -0.090 0.035  382 VAL CCC CB  
2969  C CG1 . VAL C 53  ? 0.706 0.633 0.805 0.019  -0.085 0.029  382 VAL CCC CG1 
2970  C CG2 . VAL C 53  ? 0.634 0.567 0.695 0.004  -0.087 0.030  382 VAL CCC CG2 
2971  N N   . SER C 54  ? 0.594 0.564 0.712 0.000  -0.107 0.056  383 SER CCC N   
2972  C CA  . SER C 54  ? 0.590 0.573 0.708 -0.008 -0.111 0.059  383 SER CCC CA  
2973  C C   . SER C 54  ? 0.595 0.577 0.697 -0.010 -0.097 0.050  383 SER CCC C   
2974  O O   . SER C 54  ? 0.615 0.596 0.720 -0.002 -0.085 0.043  383 SER CCC O   
2975  C CB  . SER C 54  ? 0.581 0.583 0.735 -0.005 -0.114 0.065  383 SER CCC CB  
2976  O OG  . SER C 54  ? 0.565 0.578 0.719 -0.014 -0.116 0.066  383 SER CCC OG  
2977  N N   . PRO C 55  ? 0.576 0.557 0.659 -0.020 -0.099 0.049  384 PRO CCC N   
2978  C CA  . PRO C 55  ? 0.574 0.554 0.646 -0.022 -0.087 0.043  384 PRO CCC CA  
2979  C C   . PRO C 55  ? 0.565 0.558 0.658 -0.017 -0.077 0.043  384 PRO CCC C   
2980  O O   . PRO C 55  ? 0.563 0.553 0.646 -0.014 -0.064 0.038  384 PRO CCC O   
2981  C CB  . PRO C 55  ? 0.565 0.543 0.623 -0.034 -0.094 0.045  384 PRO CCC CB  
2982  C CG  . PRO C 55  ? 0.559 0.529 0.605 -0.038 -0.106 0.048  384 PRO CCC CG  
2983  C CD  . PRO C 55  ? 0.563 0.540 0.633 -0.031 -0.112 0.054  384 PRO CCC CD  
2984  N N   . THR C 56  ? 0.570 0.578 0.693 -0.017 -0.082 0.048  385 THR CCC N   
2985  C CA  . THR C 56  ? 0.574 0.598 0.725 -0.013 -0.071 0.048  385 THR CCC CA  
2986  C C   . THR C 56  ? 0.591 0.613 0.747 -0.000 -0.058 0.042  385 THR CCC C   
2987  O O   . THR C 56  ? 0.640 0.673 0.812 0.003  -0.045 0.041  385 THR CCC O   
2988  C CB  . THR C 56  ? 0.553 0.596 0.738 -0.015 -0.082 0.056  385 THR CCC CB  
2989  O OG1 . THR C 56  ? 0.530 0.573 0.730 -0.007 -0.091 0.060  385 THR CCC OG1 
2990  C CG2 . THR C 56  ? 0.549 0.594 0.727 -0.029 -0.096 0.060  385 THR CCC CG2 
2991  N N   . LYS C 57  ? 0.607 0.616 0.751 0.006  -0.061 0.039  386 LYS CCC N   
2992  C CA  . LYS C 57  ? 0.651 0.657 0.802 0.017  -0.049 0.032  386 LYS CCC CA  
2993  C C   . LYS C 57  ? 0.611 0.602 0.729 0.018  -0.041 0.023  386 LYS CCC C   
2994  O O   . LYS C 57  ? 0.632 0.618 0.750 0.027  -0.032 0.015  386 LYS CCC O   
2995  C CB  . LYS C 57  ? 0.684 0.685 0.851 0.023  -0.059 0.034  386 LYS CCC CB  
2996  C CG  . LYS C 57  ? 0.721 0.738 0.925 0.024  -0.069 0.044  386 LYS CCC CG  
2997  C CD  . LYS C 57  ? 0.725 0.758 0.964 0.033  -0.057 0.042  386 LYS CCC CD  
2998  C CE  . LYS C 57  ? 0.760 0.784 1.009 0.046  -0.048 0.035  386 LYS CCC CE  
2999  N NZ  . LYS C 57  ? 0.771 0.802 1.028 0.053  -0.026 0.025  386 LYS CCC NZ  
3000  N N   . LEU C 58  ? 0.576 0.560 0.667 0.011  -0.045 0.023  387 LEU CCC N   
3001  C CA  . LEU C 58  ? 0.608 0.578 0.668 0.012  -0.041 0.016  387 LEU CCC CA  
3002  C C   . LEU C 58  ? 0.581 0.553 0.636 0.018  -0.025 0.009  387 LEU CCC C   
3003  O O   . LEU C 58  ? 0.624 0.587 0.663 0.023  -0.023 0.000  387 LEU CCC O   
3004  C CB  . LEU C 58  ? 0.617 0.582 0.656 0.004  -0.046 0.019  387 LEU CCC CB  
3005  C CG  . LEU C 58  ? 0.647 0.607 0.684 -0.003 -0.059 0.023  387 LEU CCC CG  
3006  C CD1 . LEU C 58  ? 0.628 0.582 0.645 -0.011 -0.062 0.024  387 LEU CCC CD1 
3007  C CD2 . LEU C 58  ? 0.657 0.607 0.690 0.001  -0.064 0.020  387 LEU CCC CD2 
3008  N N   . ASN C 59  ? 0.602 0.586 0.668 0.018  -0.016 0.012  388 ASN CCC N   
3009  C CA  . ASN C 59  ? 0.628 0.614 0.683 0.022  0.001  0.006  388 ASN CCC CA  
3010  C C   . ASN C 59  ? 0.622 0.612 0.695 0.032  0.010  -0.001 388 ASN CCC C   
3011  O O   . ASN C 59  ? 0.660 0.650 0.722 0.035  0.025  -0.007 388 ASN CCC O   
3012  C CB  . ASN C 59  ? 0.610 0.606 0.670 0.017  0.009  0.013  388 ASN CCC CB  
3013  C CG  . ASN C 59  ? 0.606 0.593 0.638 0.012  0.007  0.017  388 ASN CCC CG  
3014  O OD1 . ASN C 59  ? 0.605 0.581 0.612 0.013  0.002  0.013  388 ASN CCC OD1 
3015  N ND2 . ASN C 59  ? 0.630 0.622 0.667 0.005  0.011  0.025  388 ASN CCC ND2 
3016  N N   . ASP C 60  ? 0.625 0.615 0.723 0.035  0.002  -0.001 389 ASP CCC N   
3017  C CA  . ASP C 60  ? 0.657 0.651 0.779 0.045  0.012  -0.008 389 ASP CCC CA  
3018  C C   . ASP C 60  ? 0.654 0.631 0.769 0.050  0.007  -0.016 389 ASP CCC C   
3019  O O   . ASP C 60  ? 0.655 0.631 0.791 0.059  0.013  -0.022 389 ASP CCC O   
3020  C CB  . ASP C 60  ? 0.668 0.676 0.832 0.047  0.008  0.000  389 ASP CCC CB  
3021  C CG  . ASP C 60  ? 0.717 0.743 0.896 0.042  0.012  0.008  389 ASP CCC CG  
3022  O OD1 . ASP C 60  ? 0.812 0.844 0.987 0.043  0.030  0.005  389 ASP CCC OD1 
3023  O OD2 . ASP C 60  ? 0.749 0.783 0.945 0.036  -0.001 0.018  389 ASP CCC OD2 
3024  N N   . LEU C 61  ? 0.657 0.621 0.745 0.045  -0.004 -0.017 390 LEU CCC N   
3025  C CA  . LEU C 61  ? 0.666 0.614 0.751 0.048  -0.010 -0.024 390 LEU CCC CA  
3026  C C   . LEU C 61  ? 0.653 0.590 0.705 0.048  -0.004 -0.037 390 LEU CCC C   
3027  O O   . LEU C 61  ? 0.677 0.618 0.704 0.043  -0.002 -0.036 390 LEU CCC O   
3028  C CB  . LEU C 61  ? 0.707 0.649 0.790 0.041  -0.027 -0.015 390 LEU CCC CB  
3029  C CG  . LEU C 61  ? 0.722 0.674 0.832 0.039  -0.036 -0.001 390 LEU CCC CG  
3030  C CD1 . LEU C 61  ? 0.704 0.650 0.803 0.031  -0.052 0.007  390 LEU CCC CD1 
3031  C CD2 . LEU C 61  ? 0.735 0.688 0.879 0.049  -0.035 -0.001 390 LEU CCC CD2 
3032  N N   . CYS C 62  ? 0.658 0.583 0.711 0.052  -0.003 -0.048 391 CYS CCC N   
3033  C CA  . CYS C 62  ? 0.668 0.581 0.692 0.050  -0.002 -0.062 391 CYS CCC CA  
3034  C C   . CYS C 62  ? 0.641 0.541 0.665 0.046  -0.015 -0.062 391 CYS CCC C   
3035  O O   . CYS C 62  ? 0.662 0.556 0.710 0.048  -0.020 -0.057 391 CYS CCC O   
3036  C CB  . CYS C 62  ? 0.716 0.624 0.740 0.058  0.013  -0.078 391 CYS CCC CB  
3037  S SG  . CYS C 62  ? 0.742 0.665 0.757 0.061  0.032  -0.079 391 CYS CCC SG  
3038  N N   . PHE C 63  ? 0.627 0.523 0.624 0.040  -0.022 -0.066 392 PHE CCC N   
3039  C CA  . PHE C 63  ? 0.620 0.504 0.614 0.034  -0.033 -0.068 392 PHE CCC CA  
3040  C C   . PHE C 63  ? 0.642 0.519 0.611 0.032  -0.032 -0.083 392 PHE CCC C   
3041  O O   . PHE C 63  ? 0.638 0.522 0.588 0.035  -0.024 -0.090 392 PHE CCC O   
3042  C CB  . PHE C 63  ? 0.595 0.485 0.585 0.027  -0.043 -0.054 392 PHE CCC CB  
3043  C CG  . PHE C 63  ? 0.583 0.478 0.594 0.028  -0.046 -0.040 392 PHE CCC CG  
3044  C CD1 . PHE C 63  ? 0.596 0.483 0.629 0.029  -0.050 -0.036 392 PHE CCC CD1 
3045  C CD2 . PHE C 63  ? 0.580 0.488 0.590 0.026  -0.044 -0.031 392 PHE CCC CD2 
3046  C CE1 . PHE C 63  ? 0.587 0.481 0.637 0.029  -0.055 -0.022 392 PHE CCC CE1 
3047  C CE2 . PHE C 63  ? 0.589 0.503 0.618 0.025  -0.049 -0.019 392 PHE CCC CE2 
3048  C CZ  . PHE C 63  ? 0.591 0.498 0.638 0.027  -0.055 -0.014 392 PHE CCC CZ  
3049  N N   . THR C 64  ? 0.650 0.516 0.621 0.028  -0.039 -0.090 393 THR CCC N   
3050  C CA  . THR C 64  ? 0.691 0.552 0.641 0.024  -0.042 -0.105 393 THR CCC CA  
3051  C C   . THR C 64  ? 0.677 0.550 0.607 0.019  -0.050 -0.099 393 THR CCC C   
3052  O O   . THR C 64  ? 0.680 0.557 0.587 0.018  -0.050 -0.107 393 THR CCC O   
3053  C CB  . THR C 64  ? 0.710 0.555 0.671 0.020  -0.048 -0.113 393 THR CCC CB  
3054  O OG1 . THR C 64  ? 0.714 0.549 0.701 0.025  -0.043 -0.108 393 THR CCC OG1 
3055  C CG2 . THR C 64  ? 0.733 0.569 0.677 0.017  -0.047 -0.133 393 THR CCC CG2 
3056  N N   . ASN C 65  ? 0.658 0.536 0.598 0.015  -0.056 -0.085 394 ASN CCC N   
3057  C CA  . ASN C 65  ? 0.652 0.539 0.581 0.010  -0.064 -0.078 394 ASN CCC CA  
3058  C C   . ASN C 65  ? 0.626 0.519 0.566 0.009  -0.065 -0.062 394 ASN CCC C   
3059  O O   . ASN C 65  ? 0.621 0.508 0.578 0.009  -0.064 -0.056 394 ASN CCC O   
3060  C CB  . ASN C 65  ? 0.672 0.555 0.603 0.003  -0.073 -0.084 394 ASN CCC CB  
3061  C CG  . ASN C 65  ? 0.668 0.548 0.585 0.002  -0.075 -0.101 394 ASN CCC CG  
3062  O OD1 . ASN C 65  ? 0.695 0.583 0.591 0.003  -0.076 -0.104 394 ASN CCC OD1 
3063  N ND2 . ASN C 65  ? 0.685 0.550 0.613 -0.001 -0.075 -0.110 394 ASN CCC ND2 
3064  N N   . VAL C 66  ? 0.605 0.507 0.534 0.007  -0.067 -0.056 395 VAL CCC N   
3065  C CA  . VAL C 66  ? 0.584 0.490 0.520 0.004  -0.070 -0.043 395 VAL CCC CA  
3066  C C   . VAL C 66  ? 0.561 0.471 0.493 -0.001 -0.076 -0.043 395 VAL CCC C   
3067  O O   . VAL C 66  ? 0.645 0.559 0.566 0.000  -0.079 -0.049 395 VAL CCC O   
3068  C CB  . VAL C 66  ? 0.601 0.515 0.533 0.008  -0.064 -0.035 395 VAL CCC CB  
3069  C CG1 . VAL C 66  ? 0.620 0.536 0.557 0.003  -0.066 -0.024 395 VAL CCC CG1 
3070  C CG2 . VAL C 66  ? 0.616 0.528 0.557 0.012  -0.056 -0.036 395 VAL CCC CG2 
3071  N N   . TYR C 67  ? 0.552 0.460 0.494 -0.006 -0.079 -0.037 396 TYR CCC N   
3072  C CA  . TYR C 67  ? 0.556 0.469 0.497 -0.011 -0.084 -0.036 396 TYR CCC CA  
3073  C C   . TYR C 67  ? 0.534 0.450 0.474 -0.012 -0.081 -0.026 396 TYR CCC C   
3074  O O   . TYR C 67  ? 0.516 0.429 0.461 -0.013 -0.079 -0.020 396 TYR CCC O   
3075  C CB  . TYR C 67  ? 0.577 0.484 0.529 -0.018 -0.087 -0.038 396 TYR CCC CB  
3076  C CG  . TYR C 67  ? 0.603 0.505 0.556 -0.018 -0.089 -0.049 396 TYR CCC CG  
3077  C CD1 . TYR C 67  ? 0.605 0.514 0.552 -0.018 -0.094 -0.058 396 TYR CCC CD1 
3078  C CD2 . TYR C 67  ? 0.647 0.537 0.608 -0.017 -0.087 -0.051 396 TYR CCC CD2 
3079  C CE1 . TYR C 67  ? 0.670 0.573 0.617 -0.019 -0.096 -0.070 396 TYR CCC CE1 
3080  C CE2 . TYR C 67  ? 0.673 0.556 0.635 -0.017 -0.088 -0.063 396 TYR CCC CE2 
3081  C CZ  . TYR C 67  ? 0.698 0.586 0.652 -0.019 -0.093 -0.073 396 TYR CCC CZ  
3082  O OH  . TYR C 67  ? 0.760 0.640 0.714 -0.020 -0.094 -0.087 396 TYR CCC OH  
3083  N N   . ALA C 68  ? 0.499 0.423 0.435 -0.010 -0.082 -0.025 397 ALA CCC N   
3084  C CA  . ALA C 68  ? 0.499 0.425 0.435 -0.011 -0.080 -0.018 397 ALA CCC CA  
3085  C C   . ALA C 68  ? 0.496 0.426 0.440 -0.016 -0.081 -0.019 397 ALA CCC C   
3086  O O   . ALA C 68  ? 0.518 0.455 0.463 -0.014 -0.085 -0.023 397 ALA CCC O   
3087  C CB  . ALA C 68  ? 0.502 0.432 0.429 -0.005 -0.078 -0.015 397 ALA CCC CB  
3088  N N   . ASP C 69  ? 0.498 0.423 0.446 -0.022 -0.078 -0.016 398 ASP CCC N   
3089  C CA  . ASP C 69  ? 0.522 0.450 0.477 -0.027 -0.076 -0.017 398 ASP CCC CA  
3090  C C   . ASP C 69  ? 0.492 0.420 0.444 -0.026 -0.071 -0.013 398 ASP CCC C   
3091  O O   . ASP C 69  ? 0.514 0.436 0.459 -0.027 -0.069 -0.009 398 ASP CCC O   
3092  C CB  . ASP C 69  ? 0.523 0.444 0.481 -0.035 -0.075 -0.016 398 ASP CCC CB  
3093  C CG  . ASP C 69  ? 0.530 0.448 0.493 -0.036 -0.079 -0.020 398 ASP CCC CG  
3094  O OD1 . ASP C 69  ? 0.526 0.449 0.492 -0.033 -0.083 -0.026 398 ASP CCC OD1 
3095  O OD2 . ASP C 69  ? 0.565 0.474 0.528 -0.041 -0.079 -0.016 398 ASP CCC OD2 
3096  N N   . SER C 70  ? 0.479 0.413 0.439 -0.024 -0.069 -0.014 399 SER CCC N   
3097  C CA  . SER C 70  ? 0.491 0.422 0.449 -0.023 -0.063 -0.012 399 SER CCC CA  
3098  C C   . SER C 70  ? 0.504 0.441 0.474 -0.026 -0.058 -0.015 399 SER CCC C   
3099  O O   . SER C 70  ? 0.476 0.422 0.458 -0.025 -0.061 -0.018 399 SER CCC O   
3100  C CB  . SER C 70  ? 0.484 0.418 0.440 -0.015 -0.065 -0.009 399 SER CCC CB  
3101  O OG  . SER C 70  ? 0.495 0.438 0.458 -0.009 -0.071 -0.010 399 SER CCC OG  
3102  N N   . PHE C 71  ? 0.512 0.442 0.479 -0.028 -0.050 -0.015 400 PHE CCC N   
3103  C CA  . PHE C 71  ? 0.513 0.446 0.489 -0.031 -0.041 -0.019 400 PHE CCC CA  
3104  C C   . PHE C 71  ? 0.520 0.442 0.488 -0.034 -0.033 -0.020 400 PHE CCC C   
3105  O O   . PHE C 71  ? 0.501 0.415 0.456 -0.035 -0.035 -0.017 400 PHE CCC O   
3106  C CB  . PHE C 71  ? 0.522 0.456 0.499 -0.040 -0.039 -0.021 400 PHE CCC CB  
3107  C CG  . PHE C 71  ? 0.519 0.443 0.478 -0.048 -0.041 -0.018 400 PHE CCC CG  
3108  C CD1 . PHE C 71  ? 0.545 0.460 0.489 -0.054 -0.035 -0.017 400 PHE CCC CD1 
3109  C CD2 . PHE C 71  ? 0.530 0.454 0.487 -0.048 -0.049 -0.015 400 PHE CCC CD2 
3110  C CE1 . PHE C 71  ? 0.567 0.475 0.496 -0.061 -0.039 -0.013 400 PHE CCC CE1 
3111  C CE2 . PHE C 71  ? 0.526 0.440 0.470 -0.054 -0.051 -0.011 400 PHE CCC CE2 
3112  C CZ  . PHE C 71  ? 0.550 0.458 0.480 -0.060 -0.047 -0.009 400 PHE CCC CZ  
3113  N N   . VAL C 72  ? 0.541 0.465 0.517 -0.035 -0.023 -0.025 401 VAL CCC N   
3114  C CA  . VAL C 72  ? 0.544 0.456 0.511 -0.039 -0.012 -0.029 401 VAL CCC CA  
3115  C C   . VAL C 72  ? 0.550 0.459 0.506 -0.050 -0.004 -0.034 401 VAL CCC C   
3116  O O   . VAL C 72  ? 0.518 0.437 0.486 -0.052 0.000  -0.035 401 VAL CCC O   
3117  C CB  . VAL C 72  ? 0.544 0.457 0.529 -0.030 -0.005 -0.032 401 VAL CCC CB  
3118  C CG1 . VAL C 72  ? 0.576 0.477 0.554 -0.035 0.008  -0.039 401 VAL CCC CG1 
3119  C CG2 . VAL C 72  ? 0.559 0.471 0.549 -0.020 -0.014 -0.026 401 VAL CCC CG2 
3120  N N   . ILE C 73  ? 0.578 0.475 0.512 -0.058 -0.001 -0.035 402 ILE CCC N   
3121  C CA  . ILE C 73  ? 0.607 0.499 0.525 -0.070 0.008  -0.039 402 ILE CCC CA  
3122  C C   . ILE C 73  ? 0.644 0.522 0.546 -0.074 0.016  -0.046 402 ILE CCC C   
3123  O O   . ILE C 73  ? 0.607 0.481 0.516 -0.068 0.013  -0.046 402 ILE CCC O   
3124  C CB  . ILE C 73  ? 0.609 0.499 0.510 -0.078 -0.000 -0.032 402 ILE CCC CB  
3125  C CG1 . ILE C 73  ? 0.588 0.474 0.480 -0.077 -0.013 -0.026 402 ILE CCC CG1 
3126  C CG2 . ILE C 73  ? 0.607 0.507 0.522 -0.076 -0.003 -0.029 402 ILE CCC CG2 
3127  C CD1 . ILE C 73  ? 0.601 0.484 0.477 -0.085 -0.021 -0.019 402 ILE CCC CD1 
3128  N N   . ARG C 74  ? 0.696 0.567 0.578 -0.085 0.025  -0.052 403 ARG CCC N   
3129  C CA  . ARG C 74  ? 0.748 0.605 0.610 -0.092 0.031  -0.060 403 ARG CCC CA  
3130  C C   . ARG C 74  ? 0.727 0.580 0.571 -0.098 0.016  -0.054 403 ARG CCC C   
3131  O O   . ARG C 74  ? 0.719 0.577 0.558 -0.101 0.005  -0.044 403 ARG CCC O   
3132  C CB  . ARG C 74  ? 0.813 0.665 0.652 -0.104 0.043  -0.067 403 ARG CCC CB  
3133  C CG  . ARG C 74  ? 0.873 0.728 0.727 -0.101 0.063  -0.077 403 ARG CCC CG  
3134  C CD  . ARG C 74  ? 0.915 0.768 0.746 -0.114 0.074  -0.081 403 ARG CCC CD  
3135  N NE  . ARG C 74  ? 0.985 0.824 0.778 -0.127 0.074  -0.085 403 ARG CCC NE  
3136  C CZ  . ARG C 74  ? 1.078 0.913 0.840 -0.140 0.080  -0.086 403 ARG CCC CZ  
3137  N NH1 . ARG C 74  ? 1.092 0.935 0.858 -0.143 0.090  -0.083 403 ARG CCC NH1 
3138  N NH2 . ARG C 74  ? 1.167 0.989 0.892 -0.152 0.077  -0.090 403 ARG CCC NH2 
3139  N N   . GLY C 75  ? 0.716 0.558 0.551 -0.101 0.016  -0.060 404 GLY CCC N   
3140  C CA  . GLY C 75  ? 0.714 0.552 0.534 -0.108 0.003  -0.055 404 GLY CCC CA  
3141  C C   . GLY C 75  ? 0.700 0.540 0.496 -0.119 -0.004 -0.050 404 GLY CCC C   
3142  O O   . GLY C 75  ? 0.659 0.505 0.456 -0.119 -0.019 -0.039 404 GLY CCC O   
3143  N N   . ASP C 76  ? 0.722 0.557 0.496 -0.129 0.006  -0.056 405 ASP CCC N   
3144  C CA  . ASP C 76  ? 0.786 0.620 0.531 -0.141 -0.003 -0.050 405 ASP CCC CA  
3145  C C   . ASP C 76  ? 0.742 0.585 0.494 -0.138 -0.005 -0.038 405 ASP CCC C   
3146  O O   . ASP C 76  ? 0.737 0.578 0.468 -0.146 -0.013 -0.030 405 ASP CCC O   
3147  C CB  . ASP C 76  ? 0.898 0.721 0.610 -0.155 0.007  -0.061 405 ASP CCC CB  
3148  C CG  . ASP C 76  ? 0.975 0.793 0.686 -0.154 0.029  -0.073 405 ASP CCC CG  
3149  O OD1 . ASP C 76  ? 0.952 0.779 0.686 -0.146 0.036  -0.069 405 ASP CCC OD1 
3150  O OD2 . ASP C 76  ? 1.075 0.882 0.765 -0.163 0.040  -0.087 405 ASP CCC OD2 
3151  N N   . GLU C 77  ? 0.702 0.553 0.484 -0.126 -0.002 -0.036 406 GLU CCC N   
3152  C CA  . GLU C 77  ? 0.700 0.558 0.492 -0.123 -0.007 -0.026 406 GLU CCC CA  
3153  C C   . GLU C 77  ? 0.688 0.552 0.495 -0.116 -0.023 -0.016 406 GLU CCC C   
3154  O O   . GLU C 77  ? 0.660 0.527 0.474 -0.114 -0.030 -0.007 406 GLU CCC O   
3155  C CB  . GLU C 77  ? 0.713 0.578 0.528 -0.117 0.006  -0.031 406 GLU CCC CB  
3156  C CG  . GLU C 77  ? 0.704 0.567 0.508 -0.124 0.024  -0.038 406 GLU CCC CG  
3157  C CD  . GLU C 77  ? 0.689 0.561 0.523 -0.116 0.036  -0.044 406 GLU CCC CD  
3158  O OE1 . GLU C 77  ? 0.668 0.547 0.529 -0.104 0.031  -0.045 406 GLU CCC OE1 
3159  O OE2 . GLU C 77  ? 0.754 0.627 0.584 -0.122 0.051  -0.048 406 GLU CCC OE2 
3160  N N   . VAL C 78  ? 0.674 0.537 0.487 -0.112 -0.029 -0.018 407 VAL CCC N   
3161  C CA  . VAL C 78  ? 0.647 0.516 0.476 -0.104 -0.042 -0.010 407 VAL CCC CA  
3162  C C   . VAL C 78  ? 0.632 0.501 0.450 -0.109 -0.055 0.000  407 VAL CCC C   
3163  O O   . VAL C 78  ? 0.621 0.495 0.455 -0.102 -0.061 0.007  407 VAL CCC O   
3164  C CB  . VAL C 78  ? 0.631 0.499 0.467 -0.100 -0.044 -0.014 407 VAL CCC CB  
3165  C CG1 . VAL C 78  ? 0.607 0.481 0.456 -0.094 -0.056 -0.006 407 VAL CCC CG1 
3166  C CG2 . VAL C 78  ? 0.624 0.492 0.476 -0.092 -0.033 -0.021 407 VAL CCC CG2 
3167  N N   . ARG C 79  ? 0.687 0.551 0.481 -0.120 -0.058 0.002  408 ARG CCC N   
3168  C CA  . ARG C 79  ? 0.736 0.599 0.519 -0.126 -0.071 0.014  408 ARG CCC CA  
3169  C C   . ARG C 79  ? 0.711 0.574 0.501 -0.123 -0.070 0.022  408 ARG CCC C   
3170  O O   . ARG C 79  ? 0.749 0.612 0.540 -0.122 -0.082 0.034  408 ARG CCC O   
3171  C CB  . ARG C 79  ? 0.802 0.659 0.552 -0.140 -0.073 0.013  408 ARG CCC CB  
3172  C CG  . ARG C 79  ? 0.923 0.773 0.650 -0.148 -0.065 0.016  408 ARG CCC CG  
3173  C CD  . ARG C 79  ? 1.076 0.919 0.766 -0.162 -0.061 0.010  408 ARG CCC CD  
3174  N NE  . ARG C 79  ? 1.245 1.084 0.932 -0.164 -0.040 0.000  408 ARG CCC NE  
3175  C CZ  . ARG C 79  ? 1.240 1.079 0.927 -0.165 -0.031 0.005  408 ARG CCC CZ  
3176  N NH1 . ARG C 79  ? 1.167 1.005 0.852 -0.166 -0.040 0.020  408 ARG CCC NH1 
3177  N NH2 . ARG C 79  ? 1.218 1.055 0.906 -0.165 -0.011 -0.006 408 ARG CCC NH2 
3178  N N   . GLN C 80  ? 0.654 0.517 0.450 -0.121 -0.057 0.017  409 GLN CCC N   
3179  C CA  . GLN C 80  ? 0.624 0.486 0.427 -0.121 -0.055 0.023  409 GLN CCC CA  
3180  C C   . GLN C 80  ? 0.571 0.439 0.403 -0.109 -0.060 0.024  409 GLN CCC C   
3181  O O   . GLN C 80  ? 0.552 0.418 0.391 -0.108 -0.062 0.030  409 GLN CCC O   
3182  C CB  . GLN C 80  ? 0.625 0.487 0.426 -0.124 -0.038 0.015  409 GLN CCC CB  
3183  C CG  . GLN C 80  ? 0.647 0.502 0.418 -0.137 -0.030 0.014  409 GLN CCC CG  
3184  C CD  . GLN C 80  ? 0.662 0.519 0.436 -0.140 -0.011 0.006  409 GLN CCC CD  
3185  O OE1 . GLN C 80  ? 0.618 0.479 0.410 -0.139 -0.007 0.009  409 GLN CCC OE1 
3186  N NE2 . GLN C 80  ? 0.676 0.531 0.435 -0.146 0.001  -0.004 409 GLN CCC NE2 
3187  N N   . ILE C 81  ? 0.590 0.463 0.435 -0.100 -0.062 0.019  410 ILE CCC N   
3188  C CA  . ILE C 81  ? 0.594 0.473 0.462 -0.090 -0.067 0.020  410 ILE CCC CA  
3189  C C   . ILE C 81  ? 0.597 0.475 0.469 -0.087 -0.079 0.028  410 ILE CCC C   
3190  O O   . ILE C 81  ? 0.571 0.454 0.450 -0.082 -0.083 0.027  410 ILE CCC O   
3191  C CB  . ILE C 81  ? 0.616 0.500 0.496 -0.081 -0.062 0.011  410 ILE CCC CB  
3192  C CG1 . ILE C 81  ? 0.612 0.497 0.490 -0.084 -0.050 0.003  410 ILE CCC CG1 
3193  C CG2 . ILE C 81  ? 0.615 0.505 0.514 -0.072 -0.065 0.010  410 ILE CCC CG2 
3194  C CD1 . ILE C 81  ? 0.626 0.513 0.510 -0.086 -0.045 0.002  410 ILE CCC CD1 
3195  N N   . ALA C 82  ? 0.619 0.491 0.485 -0.091 -0.084 0.037  411 ALA CCC N   
3196  C CA  . ALA C 82  ? 0.656 0.527 0.527 -0.089 -0.097 0.048  411 ALA CCC CA  
3197  C C   . ALA C 82  ? 0.657 0.519 0.528 -0.092 -0.099 0.058  411 ALA CCC C   
3198  O O   . ALA C 82  ? 0.662 0.518 0.520 -0.100 -0.093 0.058  411 ALA CCC O   
3199  C CB  . ALA C 82  ? 0.651 0.523 0.506 -0.096 -0.104 0.052  411 ALA CCC CB  
3200  N N   . PRO C 83  ? 0.659 0.518 0.545 -0.085 -0.108 0.065  412 PRO CCC N   
3201  C CA  . PRO C 83  ? 0.683 0.531 0.571 -0.087 -0.111 0.075  412 PRO CCC CA  
3202  C C   . PRO C 83  ? 0.693 0.535 0.555 -0.099 -0.115 0.087  412 PRO CCC C   
3203  O O   . PRO C 83  ? 0.685 0.531 0.537 -0.101 -0.123 0.091  412 PRO CCC O   
3204  C CB  . PRO C 83  ? 0.687 0.535 0.598 -0.077 -0.120 0.081  412 PRO CCC CB  
3205  C CG  . PRO C 83  ? 0.679 0.540 0.593 -0.073 -0.124 0.077  412 PRO CCC CG  
3206  C CD  . PRO C 83  ? 0.661 0.528 0.567 -0.075 -0.114 0.064  412 PRO CCC CD  
3207  N N   . GLY C 84  ? 0.705 0.537 0.557 -0.106 -0.109 0.092  413 GLY CCC N   
3208  C CA  . GLY C 84  ? 0.721 0.543 0.546 -0.117 -0.113 0.106  413 GLY CCC CA  
3209  C C   . GLY C 84  ? 0.746 0.571 0.542 -0.128 -0.104 0.100  413 GLY CCC C   
3210  O O   . GLY C 84  ? 0.781 0.600 0.549 -0.138 -0.108 0.111  413 GLY CCC O   
3211  N N   . GLN C 85  ? 0.739 0.573 0.540 -0.127 -0.093 0.084  414 GLN CCC N   
3212  C CA  . GLN C 85  ? 0.757 0.593 0.534 -0.136 -0.082 0.075  414 GLN CCC CA  
3213  C C   . GLN C 85  ? 0.732 0.563 0.502 -0.144 -0.066 0.073  414 GLN CCC C   
3214  O O   . GLN C 85  ? 0.744 0.574 0.537 -0.140 -0.063 0.073  414 GLN CCC O   
3215  C CB  . GLN C 85  ? 0.723 0.569 0.512 -0.129 -0.078 0.060  414 GLN CCC CB  
3216  C CG  . GLN C 85  ? 0.713 0.565 0.505 -0.125 -0.090 0.060  414 GLN CCC CG  
3217  C CD  . GLN C 85  ? 0.748 0.596 0.508 -0.136 -0.096 0.065  414 GLN CCC CD  
3218  O OE1 . GLN C 85  ? 0.770 0.615 0.506 -0.146 -0.087 0.060  414 GLN CCC OE1 
3219  N NE2 . GLN C 85  ? 0.743 0.595 0.506 -0.134 -0.113 0.073  414 GLN CCC NE2 
3220  N N   . THR C 86  ? 0.741 0.569 0.483 -0.155 -0.057 0.071  415 THR CCC N   
3221  C CA  . THR C 86  ? 0.782 0.610 0.521 -0.162 -0.038 0.066  415 THR CCC CA  
3222  C C   . THR C 86  ? 0.798 0.633 0.528 -0.164 -0.024 0.049  415 THR CCC C   
3223  O O   . THR C 86  ? 0.849 0.685 0.569 -0.162 -0.031 0.044  415 THR CCC O   
3224  C CB  . THR C 86  ? 0.825 0.642 0.536 -0.175 -0.035 0.080  415 THR CCC CB  
3225  O OG1 . THR C 86  ? 0.837 0.649 0.512 -0.182 -0.042 0.084  415 THR CCC OG1 
3226  C CG2 . THR C 86  ? 0.831 0.638 0.554 -0.173 -0.045 0.096  415 THR CCC CG2 
3227  N N   . GLY C 87  ? 0.804 0.642 0.541 -0.167 -0.006 0.042  416 GLY CCC N   
3228  C CA  . GLY C 87  ? 0.789 0.633 0.527 -0.167 0.010  0.025  416 GLY CCC CA  
3229  C C   . GLY C 87  ? 0.750 0.605 0.525 -0.160 0.020  0.017  416 GLY CCC C   
3230  O O   . GLY C 87  ? 0.724 0.582 0.522 -0.156 0.013  0.023  416 GLY CCC O   
3231  N N   . LYS C 88  ? 0.760 0.623 0.542 -0.160 0.036  0.004  417 LYS CCC N   
3232  C CA  . LYS C 88  ? 0.801 0.676 0.620 -0.153 0.046  -0.004 417 LYS CCC CA  
3233  C C   . LYS C 88  ? 0.740 0.622 0.587 -0.140 0.030  -0.003 417 LYS CCC C   
3234  O O   . LYS C 88  ? 0.701 0.591 0.574 -0.138 0.029  -0.002 417 LYS CCC O   
3235  C CB  . LYS C 88  ? 0.863 0.745 0.688 -0.152 0.064  -0.019 417 LYS CCC CB  
3236  C CG  . LYS C 88  ? 0.960 0.848 0.790 -0.160 0.085  -0.022 417 LYS CCC CG  
3237  C CD  . LYS C 88  ? 1.034 0.916 0.838 -0.169 0.106  -0.030 417 LYS CCC CD  
3238  C CE  . LYS C 88  ? 1.117 0.992 0.894 -0.185 0.117  -0.022 417 LYS CCC CE  
3239  N NZ  . LYS C 88  ? 1.180 1.044 0.912 -0.196 0.128  -0.027 417 LYS CCC NZ  
3240  N N   . ILE C 89  ? 0.708 0.587 0.550 -0.133 0.018  -0.004 418 ILE CCC N   
3241  C CA  . ILE C 89  ? 0.670 0.556 0.538 -0.120 0.005  -0.005 418 ILE CCC CA  
3242  C C   . ILE C 89  ? 0.644 0.526 0.515 -0.120 -0.008 0.006  418 ILE CCC C   
3243  O O   . ILE C 89  ? 0.594 0.482 0.488 -0.116 -0.010 0.004  418 ILE CCC O   
3244  C CB  . ILE C 89  ? 0.658 0.542 0.520 -0.113 -0.001 -0.009 418 ILE CCC CB  
3245  C CG1 . ILE C 89  ? 0.673 0.559 0.533 -0.114 0.013  -0.020 418 ILE CCC CG1 
3246  C CG2 . ILE C 89  ? 0.634 0.526 0.520 -0.101 -0.011 -0.010 418 ILE CCC CG2 
3247  C CD1 . ILE C 89  ? 0.650 0.548 0.538 -0.108 0.025  -0.028 418 ILE CCC CD1 
3248  N N   . ALA C 90  ? 0.643 0.514 0.492 -0.125 -0.016 0.015  419 ALA CCC N   
3249  C CA  . ALA C 90  ? 0.656 0.520 0.508 -0.125 -0.028 0.026  419 ALA CCC CA  
3250  C C   . ALA C 90  ? 0.674 0.537 0.537 -0.131 -0.021 0.029  419 ALA CCC C   
3251  O O   . ALA C 90  ? 0.659 0.521 0.541 -0.127 -0.028 0.031  419 ALA CCC O   
3252  C CB  . ALA C 90  ? 0.646 0.500 0.472 -0.130 -0.037 0.037  419 ALA CCC CB  
3253  N N   . ASP C 91  ? 0.717 0.579 0.569 -0.141 -0.007 0.029  420 ASP CCC N   
3254  C CA  . ASP C 91  ? 0.757 0.616 0.615 -0.150 0.001  0.034  420 ASP CCC CA  
3255  C C   . ASP C 91  ? 0.719 0.592 0.612 -0.146 0.008  0.024  420 ASP CCC C   
3256  O O   . ASP C 91  ? 0.751 0.622 0.661 -0.149 0.006  0.027  420 ASP CCC O   
3257  C CB  . ASP C 91  ? 0.814 0.667 0.645 -0.164 0.015  0.039  420 ASP CCC CB  
3258  C CG  . ASP C 91  ? 0.844 0.683 0.638 -0.169 0.006  0.052  420 ASP CCC CG  
3259  O OD1 . ASP C 91  ? 0.848 0.681 0.644 -0.163 -0.011 0.060  420 ASP CCC OD1 
3260  O OD2 . ASP C 91  ? 0.919 0.754 0.685 -0.180 0.017  0.054  420 ASP CCC OD2 
3261  N N   . TYR C 92  ? 0.663 0.550 0.567 -0.141 0.015  0.012  421 TYR CCC N   
3262  C CA  . TYR C 92  ? 0.644 0.546 0.579 -0.140 0.024  0.003  421 TYR CCC CA  
3263  C C   . TYR C 92  ? 0.615 0.530 0.574 -0.126 0.015  -0.006 421 TYR CCC C   
3264  O O   . TYR C 92  ? 0.601 0.530 0.588 -0.124 0.018  -0.012 421 TYR CCC O   
3265  C CB  . TYR C 92  ? 0.655 0.563 0.584 -0.146 0.044  -0.003 421 TYR CCC CB  
3266  C CG  . TYR C 92  ? 0.684 0.583 0.591 -0.161 0.057  0.005  421 TYR CCC CG  
3267  C CD1 . TYR C 92  ? 0.692 0.579 0.593 -0.169 0.052  0.017  421 TYR CCC CD1 
3268  C CD2 . TYR C 92  ? 0.711 0.612 0.606 -0.167 0.076  -0.001 421 TYR CCC CD2 
3269  C CE1 . TYR C 92  ? 0.725 0.603 0.604 -0.183 0.065  0.026  421 TYR CCC CE1 
3270  C CE2 . TYR C 92  ? 0.731 0.623 0.601 -0.182 0.090  0.006  421 TYR CCC CE2 
3271  C CZ  . TYR C 92  ? 0.749 0.630 0.611 -0.190 0.084  0.020  421 TYR CCC CZ  
3272  O OH  . TYR C 92  ? 0.777 0.649 0.615 -0.205 0.098  0.029  421 TYR CCC OH  
3273  N N   . ASN C 93  ? 0.610 0.521 0.558 -0.117 0.004  -0.006 422 ASN CCC N   
3274  C CA  . ASN C 93  ? 0.586 0.507 0.551 -0.105 -0.003 -0.013 422 ASN CCC CA  
3275  C C   . ASN C 93  ? 0.574 0.491 0.539 -0.098 -0.019 -0.010 422 ASN CCC C   
3276  O O   . ASN C 93  ? 0.567 0.492 0.551 -0.092 -0.026 -0.014 422 ASN CCC O   
3277  C CB  . ASN C 93  ? 0.593 0.515 0.548 -0.100 0.003  -0.018 422 ASN CCC CB  
3278  C CG  . ASN C 93  ? 0.603 0.532 0.566 -0.105 0.020  -0.024 422 ASN CCC CG  
3279  O OD1 . ASN C 93  ? 0.566 0.509 0.555 -0.098 0.024  -0.030 422 ASN CCC OD1 
3280  N ND2 . ASN C 93  ? 0.647 0.567 0.588 -0.116 0.032  -0.022 422 ASN CCC ND2 
3281  N N   . TYR C 94  ? 0.581 0.486 0.525 -0.098 -0.025 -0.004 423 TYR CCC N   
3282  C CA  . TYR C 94  ? 0.565 0.466 0.509 -0.090 -0.038 -0.001 423 TYR CCC CA  
3283  C C   . TYR C 94  ? 0.585 0.471 0.511 -0.095 -0.043 0.009  423 TYR CCC C   
3284  O O   . TYR C 94  ? 0.601 0.484 0.508 -0.098 -0.042 0.013  423 TYR CCC O   
3285  C CB  . TYR C 94  ? 0.567 0.472 0.510 -0.080 -0.042 -0.005 423 TYR CCC CB  
3286  C CG  . TYR C 94  ? 0.559 0.463 0.504 -0.073 -0.052 -0.004 423 TYR CCC CG  
3287  C CD1 . TYR C 94  ? 0.535 0.446 0.495 -0.066 -0.057 -0.009 423 TYR CCC CD1 
3288  C CD2 . TYR C 94  ? 0.572 0.468 0.504 -0.072 -0.058 0.002  423 TYR CCC CD2 
3289  C CE1 . TYR C 94  ? 0.548 0.457 0.507 -0.059 -0.065 -0.009 423 TYR CCC CE1 
3290  C CE2 . TYR C 94  ? 0.580 0.475 0.516 -0.064 -0.066 0.003  423 TYR CCC CE2 
3291  C CZ  . TYR C 94  ? 0.568 0.469 0.517 -0.058 -0.068 -0.003 423 TYR CCC CZ  
3292  O OH  . TYR C 94  ? 0.574 0.474 0.525 -0.051 -0.074 -0.004 423 TYR CCC OH  
3293  N N   . LYS C 95  ? 0.600 0.480 0.533 -0.095 -0.050 0.013  424 LYS CCC N   
3294  C CA  . LYS C 95  ? 0.679 0.546 0.601 -0.099 -0.055 0.024  424 LYS CCC CA  
3295  C C   . LYS C 95  ? 0.657 0.521 0.587 -0.090 -0.066 0.025  424 LYS CCC C   
3296  O O   . LYS C 95  ? 0.646 0.511 0.592 -0.085 -0.068 0.019  424 LYS CCC O   
3297  C CB  . LYS C 95  ? 0.763 0.621 0.689 -0.108 -0.051 0.030  424 LYS CCC CB  
3298  C CG  . LYS C 95  ? 0.849 0.692 0.765 -0.112 -0.057 0.044  424 LYS CCC CG  
3299  C CD  . LYS C 95  ? 0.915 0.755 0.805 -0.116 -0.059 0.052  424 LYS CCC CD  
3300  C CE  . LYS C 95  ? 0.970 0.795 0.847 -0.123 -0.063 0.068  424 LYS CCC CE  
3301  N NZ  . LYS C 95  ? 1.026 0.849 0.874 -0.128 -0.065 0.076  424 LYS CCC NZ  
3302  N N   . LEU C 96  ? 0.668 0.529 0.587 -0.087 -0.072 0.032  425 LEU CCC N   
3303  C CA  . LEU C 96  ? 0.674 0.531 0.602 -0.079 -0.081 0.034  425 LEU CCC CA  
3304  C C   . LEU C 96  ? 0.679 0.523 0.609 -0.082 -0.086 0.045  425 LEU CCC C   
3305  O O   . LEU C 96  ? 0.752 0.589 0.668 -0.091 -0.085 0.055  425 LEU CCC O   
3306  C CB  . LEU C 96  ? 0.659 0.521 0.580 -0.075 -0.086 0.037  425 LEU CCC CB  
3307  C CG  . LEU C 96  ? 0.634 0.508 0.557 -0.069 -0.082 0.027  425 LEU CCC CG  
3308  C CD1 . LEU C 96  ? 0.658 0.536 0.576 -0.067 -0.087 0.030  425 LEU CCC CD1 
3309  C CD2 . LEU C 96  ? 0.648 0.526 0.586 -0.061 -0.082 0.019  425 LEU CCC CD2 
3310  N N   . PRO C 97  ? 0.647 0.485 0.594 -0.075 -0.090 0.044  426 PRO CCC N   
3311  C CA  . PRO C 97  ? 0.682 0.505 0.635 -0.075 -0.095 0.054  426 PRO CCC CA  
3312  C C   . PRO C 97  ? 0.691 0.513 0.637 -0.073 -0.103 0.067  426 PRO CCC C   
3313  O O   . PRO C 97  ? 0.731 0.564 0.674 -0.069 -0.106 0.065  426 PRO CCC O   
3314  C CB  . PRO C 97  ? 0.655 0.475 0.628 -0.066 -0.096 0.045  426 PRO CCC CB  
3315  C CG  . PRO C 97  ? 0.626 0.461 0.600 -0.059 -0.094 0.034  426 PRO CCC CG  
3316  C CD  . PRO C 97  ? 0.624 0.469 0.584 -0.066 -0.089 0.031  426 PRO CCC CD  
3317  N N   . ASP C 98  ? 0.762 0.571 0.709 -0.076 -0.109 0.081  427 ASP CCC N   
3318  C CA  . ASP C 98  ? 0.808 0.616 0.750 -0.074 -0.120 0.096  427 ASP CCC CA  
3319  C C   . ASP C 98  ? 0.813 0.626 0.777 -0.061 -0.125 0.092  427 ASP CCC C   
3320  O O   . ASP C 98  ? 0.816 0.639 0.778 -0.058 -0.133 0.098  427 ASP CCC O   
3321  C CB  . ASP C 98  ? 0.887 0.679 0.823 -0.079 -0.125 0.114  427 ASP CCC CB  
3322  C CG  . ASP C 98  ? 0.988 0.782 0.895 -0.090 -0.129 0.125  427 ASP CCC CG  
3323  O OD1 . ASP C 98  ? 1.006 0.811 0.906 -0.088 -0.138 0.128  427 ASP CCC OD1 
3324  O OD2 . ASP C 98  ? 1.068 0.854 0.956 -0.101 -0.122 0.129  427 ASP CCC OD2 
3325  N N   . ASP C 99  ? 0.771 0.580 0.755 -0.053 -0.120 0.082  428 ASP CCC N   
3326  C CA  . ASP C 99  ? 0.739 0.552 0.746 -0.040 -0.123 0.078  428 ASP CCC CA  
3327  C C   . ASP C 99  ? 0.712 0.540 0.718 -0.036 -0.116 0.061  428 ASP CCC C   
3328  O O   . ASP C 99  ? 0.704 0.533 0.726 -0.026 -0.113 0.052  428 ASP CCC O   
3329  C CB  . ASP C 99  ? 0.757 0.552 0.783 -0.034 -0.121 0.077  428 ASP CCC CB  
3330  C CG  . ASP C 99  ? 0.776 0.566 0.804 -0.037 -0.112 0.061  428 ASP CCC CG  
3331  O OD1 . ASP C 99  ? 0.718 0.517 0.732 -0.043 -0.108 0.053  428 ASP CCC OD1 
3332  O OD2 . ASP C 99  ? 0.831 0.607 0.876 -0.031 -0.110 0.055  428 ASP CCC OD2 
3333  N N   . PHE C 100 ? 0.658 0.496 0.646 -0.043 -0.112 0.057  429 PHE CCC N   
3334  C CA  . PHE C 100 ? 0.638 0.488 0.623 -0.039 -0.107 0.044  429 PHE CCC CA  
3335  C C   . PHE C 100 ? 0.618 0.477 0.617 -0.029 -0.108 0.044  429 PHE CCC C   
3336  O O   . PHE C 100 ? 0.626 0.491 0.629 -0.029 -0.115 0.054  429 PHE CCC O   
3337  C CB  . PHE C 100 ? 0.644 0.503 0.610 -0.047 -0.105 0.044  429 PHE CCC CB  
3338  C CG  . PHE C 100 ? 0.611 0.482 0.575 -0.043 -0.100 0.034  429 PHE CCC CG  
3339  C CD1 . PHE C 100 ? 0.600 0.472 0.568 -0.040 -0.094 0.023  429 PHE CCC CD1 
3340  C CD2 . PHE C 100 ? 0.618 0.498 0.576 -0.044 -0.101 0.036  429 PHE CCC CD2 
3341  C CE1 . PHE C 100 ? 0.599 0.481 0.564 -0.036 -0.090 0.016  429 PHE CCC CE1 
3342  C CE2 . PHE C 100 ? 0.602 0.491 0.559 -0.041 -0.096 0.028  429 PHE CCC CE2 
3343  C CZ  . PHE C 100 ? 0.591 0.480 0.550 -0.037 -0.090 0.019  429 PHE CCC CZ  
3344  N N   . THR C 101 ? 0.599 0.462 0.605 -0.022 -0.102 0.032  430 THR CCC N   
3345  C CA  . THR C 101 ? 0.601 0.475 0.617 -0.014 -0.100 0.029  430 THR CCC CA  
3346  C C   . THR C 101 ? 0.588 0.472 0.591 -0.015 -0.094 0.020  430 THR CCC C   
3347  O O   . THR C 101 ? 0.617 0.499 0.615 -0.014 -0.089 0.010  430 THR CCC O   
3348  C CB  . THR C 101 ? 0.614 0.482 0.648 -0.004 -0.096 0.022  430 THR CCC CB  
3349  O OG1 . THR C 101 ? 0.620 0.478 0.668 -0.003 -0.102 0.032  430 THR CCC OG1 
3350  C CG2 . THR C 101 ? 0.599 0.479 0.645 0.004  -0.091 0.019  430 THR CCC CG2 
3351  N N   . GLY C 102 ? 0.588 0.483 0.587 -0.017 -0.095 0.024  431 GLY CCC N   
3352  C CA  . GLY C 102 ? 0.602 0.504 0.590 -0.018 -0.089 0.018  431 GLY CCC CA  
3353  C C   . GLY C 102 ? 0.583 0.491 0.564 -0.024 -0.091 0.024  431 GLY CCC C   
3354  O O   . GLY C 102 ? 0.608 0.518 0.595 -0.026 -0.098 0.032  431 GLY CCC O   
3355  N N   . CYS C 103 ? 0.561 0.473 0.531 -0.025 -0.087 0.020  432 CYS CCC N   
3356  C CA  . CYS C 103 ? 0.596 0.511 0.559 -0.031 -0.087 0.023  432 CYS CCC CA  
3357  C C   . CYS C 103 ? 0.570 0.481 0.518 -0.037 -0.084 0.019  432 CYS CCC C   
3358  O O   . CYS C 103 ? 0.545 0.454 0.491 -0.034 -0.081 0.014  432 CYS CCC O   
3359  C CB  . CYS C 103 ? 0.615 0.537 0.584 -0.028 -0.082 0.022  432 CYS CCC CB  
3360  S SG  . CYS C 103 ? 0.647 0.577 0.638 -0.020 -0.082 0.024  432 CYS CCC SG  
3361  N N   . VAL C 104 ? 0.556 0.465 0.496 -0.044 -0.086 0.022  433 VAL CCC N   
3362  C CA  . VAL C 104 ? 0.561 0.466 0.488 -0.050 -0.081 0.018  433 VAL CCC CA  
3363  C C   . VAL C 104 ? 0.551 0.458 0.476 -0.052 -0.078 0.016  433 VAL CCC C   
3364  O O   . VAL C 104 ? 0.575 0.483 0.499 -0.057 -0.083 0.020  433 VAL CCC O   
3365  C CB  . VAL C 104 ? 0.584 0.483 0.500 -0.058 -0.084 0.021  433 VAL CCC CB  
3366  C CG1 . VAL C 104 ? 0.594 0.490 0.499 -0.064 -0.077 0.015  433 VAL CCC CG1 
3367  C CG2 . VAL C 104 ? 0.605 0.501 0.526 -0.057 -0.087 0.023  433 VAL CCC CG2 
3368  N N   . ILE C 105 ? 0.545 0.451 0.469 -0.048 -0.072 0.012  434 ILE CCC N   
3369  C CA  . ILE C 105 ? 0.569 0.474 0.492 -0.049 -0.067 0.011  434 ILE CCC CA  
3370  C C   . ILE C 105 ? 0.562 0.461 0.478 -0.051 -0.061 0.005  434 ILE CCC C   
3371  O O   . ILE C 105 ? 0.585 0.485 0.503 -0.047 -0.059 0.003  434 ILE CCC O   
3372  C CB  . ILE C 105 ? 0.556 0.464 0.487 -0.041 -0.065 0.012  434 ILE CCC CB  
3373  C CG1 . ILE C 105 ? 0.554 0.469 0.494 -0.039 -0.068 0.016  434 ILE CCC CG1 
3374  C CG2 . ILE C 105 ? 0.552 0.456 0.482 -0.043 -0.059 0.012  434 ILE CCC CG2 
3375  C CD1 . ILE C 105 ? 0.567 0.487 0.513 -0.031 -0.064 0.017  434 ILE CCC CD1 
3376  N N   . ALA C 106 ? 0.588 0.480 0.498 -0.058 -0.059 0.003  435 ALA CCC N   
3377  C CA  . ALA C 106 ? 0.596 0.481 0.501 -0.059 -0.051 -0.003 435 ALA CCC CA  
3378  C C   . ALA C 106 ? 0.597 0.476 0.504 -0.061 -0.046 -0.005 435 ALA CCC C   
3379  O O   . ALA C 106 ? 0.623 0.502 0.530 -0.066 -0.051 -0.003 435 ALA CCC O   
3380  C CB  . ALA C 106 ? 0.582 0.464 0.475 -0.068 -0.050 -0.007 435 ALA CCC CB  
3381  N N   . TRP C 107 ? 0.602 0.474 0.511 -0.058 -0.038 -0.010 436 TRP CCC N   
3382  C CA  . TRP C 107 ? 0.603 0.464 0.514 -0.060 -0.032 -0.013 436 TRP CCC CA  
3383  C C   . TRP C 107 ? 0.620 0.473 0.531 -0.058 -0.023 -0.020 436 TRP CCC C   
3384  O O   . TRP C 107 ? 0.629 0.487 0.545 -0.052 -0.021 -0.021 436 TRP CCC O   
3385  C CB  . TRP C 107 ? 0.590 0.451 0.511 -0.052 -0.032 -0.006 436 TRP CCC CB  
3386  C CG  . TRP C 107 ? 0.570 0.435 0.499 -0.040 -0.031 -0.002 436 TRP CCC CG  
3387  C CD1 . TRP C 107 ? 0.561 0.419 0.497 -0.033 -0.025 -0.002 436 TRP CCC CD1 
3388  C CD2 . TRP C 107 ? 0.559 0.437 0.490 -0.033 -0.036 0.002  436 TRP CCC CD2 
3389  N NE1 . TRP C 107 ? 0.555 0.422 0.497 -0.023 -0.027 0.003  436 TRP CCC NE1 
3390  C CE2 . TRP C 107 ? 0.534 0.412 0.471 -0.024 -0.034 0.004  436 TRP CCC CE2 
3391  C CE3 . TRP C 107 ? 0.569 0.455 0.497 -0.034 -0.043 0.004  436 TRP CCC CE3 
3392  C CZ2 . TRP C 107 ? 0.541 0.430 0.481 -0.016 -0.040 0.007  436 TRP CCC CZ2 
3393  C CZ3 . TRP C 107 ? 0.578 0.472 0.508 -0.027 -0.046 0.006  436 TRP CCC CZ3 
3394  C CH2 . TRP C 107 ? 0.567 0.463 0.502 -0.019 -0.045 0.007  436 TRP CCC CH2 
3395  N N   . ASN C 108 ? 0.608 0.448 0.514 -0.065 -0.017 -0.027 437 ASN CCC N   
3396  C CA  . ASN C 108 ? 0.602 0.431 0.511 -0.064 -0.005 -0.036 437 ASN CCC CA  
3397  C C   . ASN C 108 ? 0.587 0.416 0.515 -0.050 -0.002 -0.031 437 ASN CCC C   
3398  O O   . ASN C 108 ? 0.557 0.384 0.491 -0.046 -0.005 -0.023 437 ASN CCC O   
3399  C CB  . ASN C 108 ? 0.624 0.437 0.525 -0.074 -0.000 -0.045 437 ASN CCC CB  
3400  C CG  . ASN C 108 ? 0.649 0.451 0.551 -0.073 0.013  -0.056 437 ASN CCC CG  
3401  O OD1 . ASN C 108 ? 0.679 0.476 0.599 -0.062 0.020  -0.055 437 ASN CCC OD1 
3402  N ND2 . ASN C 108 ? 0.669 0.466 0.553 -0.084 0.018  -0.067 437 ASN CCC ND2 
3403  N N   . SER C 109 ? 0.572 0.406 0.509 -0.043 0.004  -0.034 438 SER CCC N   
3404  C CA  . SER C 109 ? 0.564 0.400 0.521 -0.029 0.005  -0.028 438 SER CCC CA  
3405  C C   . SER C 109 ? 0.561 0.386 0.529 -0.025 0.018  -0.036 438 SER CCC C   
3406  O O   . SER C 109 ? 0.580 0.412 0.567 -0.014 0.019  -0.033 438 SER CCC O   
3407  C CB  . SER C 109 ? 0.541 0.394 0.504 -0.022 -0.002 -0.022 438 SER CCC CB  
3408  O OG  . SER C 109 ? 0.566 0.427 0.528 -0.027 0.002  -0.030 438 SER CCC OG  
3409  N N   . ASN C 110 ? 0.571 0.381 0.529 -0.035 0.026  -0.047 439 ASN CCC N   
3410  C CA  . ASN C 110 ? 0.593 0.391 0.561 -0.032 0.041  -0.058 439 ASN CCC CA  
3411  C C   . ASN C 110 ? 0.597 0.389 0.589 -0.018 0.043  -0.050 439 ASN CCC C   
3412  O O   . ASN C 110 ? 0.592 0.387 0.605 -0.008 0.050  -0.053 439 ASN CCC O   
3413  C CB  . ASN C 110 ? 0.635 0.415 0.585 -0.046 0.048  -0.071 439 ASN CCC CB  
3414  C CG  . ASN C 110 ? 0.658 0.427 0.612 -0.046 0.065  -0.086 439 ASN CCC CG  
3415  O OD1 . ASN C 110 ? 0.651 0.432 0.615 -0.041 0.071  -0.088 439 ASN CCC OD1 
3416  N ND2 . ASN C 110 ? 0.699 0.447 0.646 -0.053 0.073  -0.097 439 ASN CCC ND2 
3417  N N   . ASN C 111 ? 0.610 0.396 0.603 -0.016 0.036  -0.040 440 ASN CCC N   
3418  C CA  . ASN C 111 ? 0.642 0.417 0.654 -0.003 0.037  -0.030 440 ASN CCC CA  
3419  C C   . ASN C 111 ? 0.661 0.455 0.690 0.012  0.031  -0.020 440 ASN CCC C   
3420  O O   . ASN C 111 ? 0.715 0.503 0.765 0.024  0.034  -0.015 440 ASN CCC O   
3421  C CB  . ASN C 111 ? 0.653 0.419 0.659 -0.005 0.032  -0.020 440 ASN CCC CB  
3422  C CG  . ASN C 111 ? 0.691 0.443 0.716 0.007  0.035  -0.010 440 ASN CCC CG  
3423  O OD1 . ASN C 111 ? 0.694 0.456 0.725 0.018  0.027  0.005  440 ASN CCC OD1 
3424  N ND2 . ASN C 111 ? 0.761 0.490 0.794 0.006  0.046  -0.017 440 ASN CCC ND2 
3425  N N   . LEU C 112 ? 0.639 0.454 0.661 0.010  0.021  -0.017 441 LEU CCC N   
3426  C CA  . LEU C 112 ? 0.626 0.459 0.662 0.022  0.012  -0.008 441 LEU CCC CA  
3427  C C   . LEU C 112 ? 0.627 0.474 0.676 0.023  0.017  -0.017 441 LEU CCC C   
3428  O O   . LEU C 112 ? 0.660 0.518 0.732 0.035  0.014  -0.012 441 LEU CCC O   
3429  C CB  . LEU C 112 ? 0.615 0.461 0.635 0.019  -0.001 0.001  441 LEU CCC CB  
3430  C CG  . LEU C 112 ? 0.611 0.447 0.620 0.020  -0.005 0.012  441 LEU CCC CG  
3431  C CD1 . LEU C 112 ? 0.583 0.434 0.579 0.019  -0.016 0.018  441 LEU CCC CD1 
3432  C CD2 . LEU C 112 ? 0.637 0.465 0.661 0.032  -0.005 0.023  441 LEU CCC CD2 
3433  N N   . ASP C 113 ? 0.632 0.480 0.668 0.012  0.023  -0.028 442 ASP CCC N   
3434  C CA  . ASP C 113 ? 0.643 0.507 0.687 0.010  0.026  -0.035 442 ASP CCC CA  
3435  C C   . ASP C 113 ? 0.691 0.548 0.743 0.007  0.043  -0.048 442 ASP CCC C   
3436  O O   . ASP C 113 ? 0.768 0.638 0.826 0.004  0.049  -0.054 442 ASP CCC O   
3437  C CB  . ASP C 113 ? 0.614 0.486 0.635 -0.002 0.019  -0.036 442 ASP CCC CB  
3438  C CG  . ASP C 113 ? 0.604 0.489 0.623 0.002  0.003  -0.025 442 ASP CCC CG  
3439  O OD1 . ASP C 113 ? 0.576 0.471 0.612 0.013  -0.003 -0.018 442 ASP CCC OD1 
3440  O OD2 . ASP C 113 ? 0.587 0.470 0.585 -0.006 -0.002 -0.023 442 ASP CCC OD2 
3441  N N   . SER C 114 ? 0.713 0.550 0.766 0.008  0.053  -0.054 443 SER CCC N   
3442  C CA  . SER C 114 ? 0.776 0.604 0.836 0.006  0.072  -0.069 443 SER CCC CA  
3443  C C   . SER C 114 ? 0.779 0.599 0.871 0.021  0.079  -0.068 443 SER CCC C   
3444  O O   . SER C 114 ? 0.791 0.604 0.889 0.029  0.071  -0.056 443 SER CCC O   
3445  C CB  . SER C 114 ? 0.806 0.616 0.836 -0.010 0.079  -0.080 443 SER CCC CB  
3446  O OG  . SER C 114 ? 0.923 0.711 0.953 -0.008 0.082  -0.081 443 SER CCC OG  
3447  N N   . LYS C 115 ? 0.835 0.659 0.950 0.026  0.094  -0.078 444 LYS CCC N   
3448  C CA  . LYS C 115 ? 0.913 0.731 1.065 0.042  0.102  -0.077 444 LYS CCC CA  
3449  C C   . LYS C 115 ? 0.944 0.745 1.099 0.039  0.126  -0.096 444 LYS CCC C   
3450  O O   . LYS C 115 ? 0.904 0.707 1.038 0.026  0.136  -0.109 444 LYS CCC O   
3451  C CB  . LYS C 115 ? 0.975 0.821 1.162 0.055  0.096  -0.069 444 LYS CCC CB  
3452  C CG  . LYS C 115 ? 1.056 0.912 1.253 0.066  0.075  -0.049 444 LYS CCC CG  
3453  C CD  . LYS C 115 ? 1.095 0.982 1.301 0.068  0.061  -0.042 444 LYS CCC CD  
3454  C CE  . LYS C 115 ? 1.106 0.997 1.286 0.064  0.041  -0.029 444 LYS CCC CE  
3455  N NZ  . LYS C 115 ? 1.117 1.036 1.309 0.066  0.027  -0.023 444 LYS CCC NZ  
3456  N N   . VAL C 116 ? 0.952 0.736 1.133 0.051  0.135  -0.098 445 VAL CCC N   
3457  C CA  . VAL C 116 ? 0.992 0.757 1.180 0.051  0.159  -0.118 445 VAL CCC CA  
3458  C C   . VAL C 116 ? 0.929 0.712 1.130 0.049  0.175  -0.131 445 VAL CCC C   
3459  O O   . VAL C 116 ? 0.926 0.695 1.105 0.037  0.193  -0.150 445 VAL CCC O   
3460  C CB  . VAL C 116 ? 1.057 0.803 1.280 0.068  0.164  -0.114 445 VAL CCC CB  
3461  C CG1 . VAL C 116 ? 1.070 0.791 1.274 0.064  0.154  -0.105 445 VAL CCC CG1 
3462  C CG2 . VAL C 116 ? 1.052 0.821 1.320 0.088  0.156  -0.098 445 VAL CCC CG2 
3463  N N   . GLY C 117 ? 0.868 0.680 1.100 0.059  0.170  -0.122 446 GLY CCC N   
3464  C CA  . GLY C 117 ? 0.877 0.707 1.122 0.057  0.187  -0.135 446 GLY CCC CA  
3465  C C   . GLY C 117 ? 0.856 0.700 1.066 0.039  0.183  -0.136 446 GLY CCC C   
3466  O O   . GLY C 117 ? 0.838 0.700 1.059 0.036  0.195  -0.143 446 GLY CCC O   
3467  N N   . GLY C 118 ? 0.843 0.681 1.017 0.029  0.165  -0.127 447 GLY CCC N   
3468  C CA  . GLY C 118 ? 0.833 0.687 0.980 0.016  0.153  -0.122 447 GLY CCC CA  
3469  C C   . GLY C 118 ? 0.807 0.686 0.976 0.025  0.133  -0.105 447 GLY CCC C   
3470  O O   . GLY C 118 ? 0.789 0.685 1.000 0.038  0.135  -0.102 447 GLY CCC O   
3471  N N   . ASN C 119 ? 0.778 0.659 0.921 0.018  0.114  -0.094 448 ASN CCC N   
3472  C CA  . ASN C 119 ? 0.756 0.660 0.911 0.022  0.094  -0.080 448 ASN CCC CA  
3473  C C   . ASN C 119 ? 0.760 0.682 0.909 0.011  0.097  -0.084 448 ASN CCC C   
3474  O O   . ASN C 119 ? 0.770 0.684 0.884 -0.003 0.097  -0.086 448 ASN CCC O   
3475  C CB  . ASN C 119 ? 0.754 0.651 0.886 0.022  0.075  -0.068 448 ASN CCC CB  
3476  C CG  . ASN C 119 ? 0.748 0.666 0.888 0.026  0.056  -0.056 448 ASN CCC CG  
3477  O OD1 . ASN C 119 ? 0.719 0.658 0.888 0.031  0.054  -0.055 448 ASN CCC OD1 
3478  N ND2 . ASN C 119 ? 0.771 0.684 0.887 0.022  0.041  -0.047 448 ASN CCC ND2 
3479  N N   . TYR C 120 ? 0.761 0.706 0.945 0.017  0.099  -0.083 449 TYR CCC N   
3480  C CA  . TYR C 120 ? 0.772 0.735 0.958 0.007  0.104  -0.086 449 TYR CCC CA  
3481  C C   . TYR C 120 ? 0.776 0.757 0.969 0.008  0.082  -0.075 449 TYR CCC C   
3482  O O   . TYR C 120 ? 0.800 0.798 1.000 -0.000 0.084  -0.076 449 TYR CCC O   
3483  C CB  . TYR C 120 ? 0.802 0.777 1.023 0.011  0.126  -0.097 449 TYR CCC CB  
3484  C CG  . TYR C 120 ? 0.824 0.778 1.030 0.006  0.150  -0.111 449 TYR CCC CG  
3485  C CD1 . TYR C 120 ? 0.832 0.775 1.000 -0.011 0.162  -0.119 449 TYR CCC CD1 
3486  C CD2 . TYR C 120 ? 0.845 0.787 1.071 0.019  0.159  -0.116 449 TYR CCC CD2 
3487  C CE1 . TYR C 120 ? 0.869 0.792 1.018 -0.016 0.183  -0.134 449 TYR CCC CE1 
3488  C CE2 . TYR C 120 ? 0.883 0.804 1.093 0.015  0.181  -0.131 449 TYR CCC CE2 
3489  C CZ  . TYR C 120 ? 0.904 0.817 1.076 -0.003 0.194  -0.141 449 TYR CCC CZ  
3490  O OH  . TYR C 120 ? 0.931 0.821 1.082 -0.009 0.215  -0.157 449 TYR CCC OH  
3491  N N   . ASN C 121 ? 0.783 0.762 0.972 0.016  0.063  -0.064 450 ASN CCC N   
3492  C CA  . ASN C 121 ? 0.747 0.742 0.939 0.017  0.042  -0.055 450 ASN CCC CA  
3493  C C   . ASN C 121 ? 0.694 0.683 0.852 0.002  0.037  -0.054 450 ASN CCC C   
3494  O O   . ASN C 121 ? 0.631 0.636 0.796 -0.001 0.025  -0.051 450 ASN CCC O   
3495  C CB  . ASN C 121 ? 0.769 0.761 0.963 0.029  0.025  -0.044 450 ASN CCC CB  
3496  C CG  . ASN C 121 ? 0.809 0.812 1.043 0.045  0.024  -0.041 450 ASN CCC CG  
3497  O OD1 . ASN C 121 ? 0.778 0.798 1.045 0.047  0.033  -0.046 450 ASN CCC OD1 
3498  N ND2 . ASN C 121 ? 0.869 0.862 1.100 0.055  0.014  -0.031 450 ASN CCC ND2 
3499  N N   . TYR C 122 ? 0.649 0.618 0.772 -0.007 0.043  -0.057 451 TYR CCC N   
3500  C CA  . TYR C 122 ? 0.607 0.570 0.699 -0.019 0.036  -0.054 451 TYR CCC CA  
3501  C C   . TYR C 122 ? 0.596 0.562 0.684 -0.032 0.050  -0.061 451 TYR CCC C   
3502  O O   . TYR C 122 ? 0.558 0.516 0.640 -0.036 0.068  -0.069 451 TYR CCC O   
3503  C CB  . TYR C 122 ? 0.623 0.565 0.682 -0.022 0.033  -0.053 451 TYR CCC CB  
3504  C CG  . TYR C 122 ? 0.612 0.551 0.672 -0.013 0.019  -0.044 451 TYR CCC CG  
3505  C CD1 . TYR C 122 ? 0.600 0.548 0.657 -0.011 0.003  -0.037 451 TYR CCC CD1 
3506  C CD2 . TYR C 122 ? 0.613 0.541 0.676 -0.005 0.023  -0.044 451 TYR CCC CD2 
3507  C CE1 . TYR C 122 ? 0.591 0.535 0.645 -0.003 -0.008 -0.030 451 TYR CCC CE1 
3508  C CE2 . TYR C 122 ? 0.606 0.530 0.668 0.003  0.011  -0.036 451 TYR CCC CE2 
3509  C CZ  . TYR C 122 ? 0.593 0.526 0.649 0.004  -0.004 -0.028 451 TYR CCC CZ  
3510  O OH  . TYR C 122 ? 0.558 0.487 0.609 0.012  -0.014 -0.019 451 TYR CCC OH  
3511  N N   . LEU C 123 ? 0.583 0.560 0.672 -0.038 0.043  -0.057 452 LEU CCC N   
3512  C CA  . LEU C 123 ? 0.602 0.584 0.691 -0.050 0.054  -0.060 452 LEU CCC CA  
3513  C C   . LEU C 123 ? 0.603 0.572 0.657 -0.062 0.047  -0.055 452 LEU CCC C   
3514  O O   . LEU C 123 ? 0.593 0.556 0.635 -0.059 0.031  -0.049 452 LEU CCC O   
3515  C CB  . LEU C 123 ? 0.594 0.599 0.720 -0.048 0.051  -0.060 452 LEU CCC CB  
3516  C CG  . LEU C 123 ? 0.595 0.616 0.761 -0.035 0.054  -0.063 452 LEU CCC CG  
3517  C CD1 . LEU C 123 ? 0.597 0.644 0.800 -0.035 0.048  -0.062 452 LEU CCC CD1 
3518  C CD2 . LEU C 123 ? 0.607 0.625 0.779 -0.036 0.078  -0.072 452 LEU CCC CD2 
3519  N N   . TYR C 124 ? 0.623 0.587 0.663 -0.074 0.059  -0.056 453 TYR CCC N   
3520  C CA  . TYR C 124 ? 0.615 0.570 0.629 -0.086 0.054  -0.050 453 TYR CCC CA  
3521  C C   . TYR C 124 ? 0.624 0.588 0.648 -0.096 0.065  -0.050 453 TYR CCC C   
3522  O O   . TYR C 124 ? 0.620 0.591 0.659 -0.097 0.083  -0.057 453 TYR CCC O   
3523  C CB  . TYR C 124 ? 0.595 0.531 0.570 -0.092 0.055  -0.049 453 TYR CCC CB  
3524  C CG  . TYR C 124 ? 0.613 0.544 0.576 -0.099 0.076  -0.057 453 TYR CCC CG  
3525  C CD1 . TYR C 124 ? 0.617 0.545 0.585 -0.092 0.085  -0.066 453 TYR CCC CD1 
3526  C CD2 . TYR C 124 ? 0.621 0.547 0.564 -0.112 0.086  -0.055 453 TYR CCC CD2 
3527  C CE1 . TYR C 124 ? 0.640 0.561 0.595 -0.099 0.105  -0.075 453 TYR CCC CE1 
3528  C CE2 . TYR C 124 ? 0.647 0.568 0.575 -0.120 0.107  -0.063 453 TYR CCC CE2 
3529  C CZ  . TYR C 124 ? 0.667 0.586 0.600 -0.113 0.116  -0.074 453 TYR CCC CZ  
3530  O OH  . TYR C 124 ? 0.710 0.622 0.626 -0.120 0.138  -0.084 453 TYR CCC OH  
3531  N N   . ARG C 125 ? 0.632 0.593 0.649 -0.104 0.057  -0.043 454 ARG CCC N   
3532  C CA  . ARG C 125 ? 0.662 0.626 0.685 -0.116 0.068  -0.041 454 ARG CCC CA  
3533  C C   . ARG C 125 ? 0.696 0.645 0.682 -0.127 0.082  -0.039 454 ARG CCC C   
3534  O O   . ARG C 125 ? 0.701 0.634 0.655 -0.130 0.072  -0.033 454 ARG CCC O   
3535  C CB  . ARG C 125 ? 0.661 0.626 0.691 -0.120 0.055  -0.033 454 ARG CCC CB  
3536  C CG  . ARG C 125 ? 0.689 0.658 0.730 -0.133 0.066  -0.031 454 ARG CCC CG  
3537  C CD  . ARG C 125 ? 0.683 0.651 0.736 -0.135 0.052  -0.026 454 ARG CCC CD  
3538  N NE  . ARG C 125 ? 0.695 0.678 0.777 -0.125 0.038  -0.032 454 ARG CCC NE  
3539  C CZ  . ARG C 125 ? 0.704 0.709 0.824 -0.123 0.041  -0.038 454 ARG CCC CZ  
3540  N NH1 . ARG C 125 ? 0.716 0.731 0.853 -0.131 0.059  -0.041 454 ARG CCC NH1 
3541  N NH2 . ARG C 125 ? 0.713 0.731 0.854 -0.113 0.026  -0.042 454 ARG CCC NH2 
3542  N N   . LEU C 126 ? 0.722 0.677 0.712 -0.134 0.103  -0.044 455 LEU CCC N   
3543  C CA  . LEU C 126 ? 0.751 0.692 0.704 -0.146 0.119  -0.044 455 LEU CCC CA  
3544  C C   . LEU C 126 ? 0.763 0.699 0.703 -0.161 0.125  -0.035 455 LEU CCC C   
3545  O O   . LEU C 126 ? 0.811 0.732 0.711 -0.171 0.128  -0.029 455 LEU CCC O   
3546  C CB  . LEU C 126 ? 0.773 0.722 0.739 -0.143 0.141  -0.058 455 LEU CCC CB  
3547  C CG  . LEU C 126 ? 0.838 0.776 0.768 -0.156 0.162  -0.062 455 LEU CCC CG  
3548  C CD1 . LEU C 126 ? 0.849 0.766 0.731 -0.159 0.153  -0.059 455 LEU CCC CD1 
3549  C CD2 . LEU C 126 ? 0.840 0.788 0.791 -0.151 0.185  -0.077 455 LEU CCC CD2 
3550  N N   . PHE C 127 ? 0.772 0.723 0.748 -0.162 0.127  -0.033 456 PHE CCC N   
3551  C CA  . PHE C 127 ? 0.792 0.741 0.766 -0.177 0.135  -0.024 456 PHE CCC CA  
3552  C C   . PHE C 127 ? 0.767 0.718 0.765 -0.175 0.116  -0.018 456 PHE CCC C   
3553  O O   . PHE C 127 ? 0.756 0.723 0.788 -0.165 0.106  -0.024 456 PHE CCC O   
3554  C CB  . PHE C 127 ? 0.807 0.772 0.806 -0.184 0.160  -0.031 456 PHE CCC CB  
3555  C CG  . PHE C 127 ? 0.839 0.803 0.819 -0.185 0.182  -0.041 456 PHE CCC CG  
3556  C CD1 . PHE C 127 ? 0.878 0.822 0.807 -0.196 0.191  -0.036 456 PHE CCC CD1 
3557  C CD2 . PHE C 127 ? 0.835 0.816 0.849 -0.174 0.192  -0.054 456 PHE CCC CD2 
3558  C CE1 . PHE C 127 ? 0.900 0.842 0.809 -0.198 0.212  -0.047 456 PHE CCC CE1 
3559  C CE2 . PHE C 127 ? 0.867 0.845 0.864 -0.175 0.214  -0.065 456 PHE CCC CE2 
3560  C CZ  . PHE C 127 ? 0.895 0.852 0.839 -0.188 0.224  -0.062 456 PHE CCC CZ  
3561  N N   . ARG C 128 ? 0.784 0.720 0.762 -0.185 0.112  -0.006 457 ARG CCC N   
3562  C CA  . ARG C 128 ? 0.775 0.710 0.776 -0.187 0.098  -0.000 457 ARG CCC CA  
3563  C C   . ARG C 128 ? 0.811 0.730 0.793 -0.203 0.105  0.014  457 ARG CCC C   
3564  O O   . ARG C 128 ? 0.873 0.776 0.814 -0.208 0.109  0.022  457 ARG CCC O   
3565  C CB  . ARG C 128 ? 0.756 0.684 0.752 -0.175 0.074  0.001  457 ARG CCC CB  
3566  C CG  . ARG C 128 ? 0.728 0.659 0.752 -0.173 0.060  0.001  457 ARG CCC CG  
3567  C CD  . ARG C 128 ? 0.716 0.643 0.736 -0.160 0.040  -0.001 457 ARG CCC CD  
3568  N NE  . ARG C 128 ? 0.707 0.641 0.757 -0.157 0.028  -0.005 457 ARG CCC NE  
3569  C CZ  . ARG C 128 ? 0.714 0.634 0.764 -0.162 0.019  0.000  457 ARG CCC CZ  
3570  N NH1 . ARG C 128 ? 0.752 0.651 0.778 -0.169 0.021  0.013  457 ARG CCC NH1 
3571  N NH2 . ARG C 128 ? 0.713 0.639 0.789 -0.159 0.009  -0.007 457 ARG CCC NH2 
3572  N N   . LYS C 129 ? 0.801 0.724 0.812 -0.210 0.105  0.016  458 LYS CCC N   
3573  C CA  . LYS C 129 ? 0.818 0.725 0.816 -0.226 0.113  0.031  458 LYS CCC CA  
3574  C C   . LYS C 129 ? 0.790 0.671 0.755 -0.224 0.096  0.044  458 LYS CCC C   
3575  O O   . LYS C 129 ? 0.798 0.661 0.736 -0.236 0.102  0.059  458 LYS CCC O   
3576  C CB  . LYS C 129 ? 0.831 0.747 0.872 -0.233 0.114  0.029  458 LYS CCC CB  
3577  C CG  . LYS C 129 ? 0.853 0.797 0.933 -0.236 0.131  0.017  458 LYS CCC CG  
3578  C CD  . LYS C 129 ? 0.885 0.839 1.008 -0.245 0.131  0.015  458 LYS CCC CD  
3579  C CE  . LYS C 129 ? 0.883 0.869 1.056 -0.238 0.129  -0.000 458 LYS CCC CE  
3580  N NZ  . LYS C 129 ? 0.897 0.893 1.111 -0.250 0.132  -0.002 458 LYS CCC NZ  
3581  N N   . SER C 130 ? 0.752 0.631 0.720 -0.211 0.075  0.041  459 SER CCC N   
3582  C CA  . SER C 130 ? 0.765 0.621 0.709 -0.208 0.059  0.053  459 SER CCC CA  
3583  C C   . SER C 130 ? 0.724 0.584 0.667 -0.191 0.042  0.045  459 SER CCC C   
3584  O O   . SER C 130 ? 0.702 0.581 0.666 -0.183 0.042  0.032  459 SER CCC O   
3585  C CB  . SER C 130 ? 0.771 0.616 0.736 -0.213 0.052  0.060  459 SER CCC CB  
3586  O OG  . SER C 130 ? 0.761 0.615 0.757 -0.203 0.040  0.047  459 SER CCC OG  
3587  N N   . ASN C 131 ? 0.739 0.583 0.658 -0.187 0.028  0.055  460 ASN CCC N   
3588  C CA  . ASN C 131 ? 0.712 0.559 0.626 -0.173 0.014  0.050  460 ASN CCC CA  
3589  C C   . ASN C 131 ? 0.695 0.546 0.639 -0.163 0.002  0.042  460 ASN CCC C   
3590  O O   . ASN C 131 ? 0.731 0.575 0.692 -0.168 0.000  0.044  460 ASN CCC O   
3591  C CB  . ASN C 131 ? 0.723 0.552 0.606 -0.172 0.003  0.064  460 ASN CCC CB  
3592  C CG  . ASN C 131 ? 0.751 0.577 0.599 -0.181 0.011  0.071  460 ASN CCC CG  
3593  O OD1 . ASN C 131 ? 0.767 0.602 0.611 -0.187 0.027  0.063  460 ASN CCC OD1 
3594  N ND2 . ASN C 131 ? 0.782 0.593 0.603 -0.182 0.000  0.084  460 ASN CCC ND2 
3595  N N   . LEU C 132 ? 0.669 0.532 0.620 -0.151 -0.005 0.031  461 LEU CCC N   
3596  C CA  . LEU C 132 ? 0.681 0.548 0.652 -0.141 -0.018 0.024  461 LEU CCC CA  
3597  C C   . LEU C 132 ? 0.719 0.568 0.683 -0.138 -0.029 0.033  461 LEU CCC C   
3598  O O   . LEU C 132 ? 0.769 0.608 0.710 -0.138 -0.032 0.043  461 LEU CCC O   
3599  C CB  . LEU C 132 ? 0.654 0.534 0.625 -0.129 -0.022 0.015  461 LEU CCC CB  
3600  C CG  . LEU C 132 ? 0.649 0.548 0.634 -0.128 -0.013 0.004  461 LEU CCC CG  
3601  C CD1 . LEU C 132 ? 0.628 0.535 0.612 -0.115 -0.019 -0.002 461 LEU CCC CD1 
3602  C CD2 . LEU C 132 ? 0.660 0.570 0.676 -0.132 -0.011 -0.002 461 LEU CCC CD2 
3603  N N   . LYS C 133 ? 0.753 0.597 0.737 -0.136 -0.036 0.028  462 LYS CCC N   
3604  C CA  . LYS C 133 ? 0.778 0.608 0.762 -0.128 -0.048 0.032  462 LYS CCC CA  
3605  C C   . LYS C 133 ? 0.714 0.554 0.693 -0.115 -0.055 0.025  462 LYS CCC C   
3606  O O   . LYS C 133 ? 0.678 0.534 0.660 -0.111 -0.053 0.016  462 LYS CCC O   
3607  C CB  . LYS C 133 ? 0.805 0.629 0.813 -0.130 -0.050 0.025  462 LYS CCC CB  
3608  C CG  . LYS C 133 ? 0.854 0.661 0.865 -0.143 -0.044 0.036  462 LYS CCC CG  
3609  C CD  . LYS C 133 ? 0.946 0.747 0.983 -0.147 -0.046 0.027  462 LYS CCC CD  
3610  C CE  . LYS C 133 ? 0.988 0.808 1.043 -0.143 -0.050 0.008  462 LYS CCC CE  
3611  N NZ  . LYS C 133 ? 1.020 0.845 1.099 -0.155 -0.046 0.001  462 LYS CCC NZ  
3612  N N   . PRO C 134 ? 0.693 0.523 0.667 -0.108 -0.064 0.030  463 PRO CCC N   
3613  C CA  . PRO C 134 ? 0.650 0.489 0.621 -0.096 -0.069 0.024  463 PRO CCC CA  
3614  C C   . PRO C 134 ? 0.638 0.489 0.623 -0.090 -0.071 0.009  463 PRO CCC C   
3615  O O   . PRO C 134 ? 0.629 0.475 0.628 -0.091 -0.072 0.004  463 PRO CCC O   
3616  C CB  . PRO C 134 ? 0.666 0.492 0.637 -0.090 -0.077 0.032  463 PRO CCC CB  
3617  C CG  . PRO C 134 ? 0.685 0.496 0.647 -0.099 -0.076 0.047  463 PRO CCC CG  
3618  C CD  . PRO C 134 ? 0.681 0.492 0.652 -0.110 -0.068 0.044  463 PRO CCC CD  
3619  N N   . PHE C 135 ? 0.629 0.495 0.610 -0.085 -0.070 0.004  464 PHE CCC N   
3620  C CA  . PHE C 135 ? 0.623 0.501 0.613 -0.078 -0.072 -0.008 464 PHE CCC CA  
3621  C C   . PHE C 135 ? 0.616 0.503 0.622 -0.085 -0.069 -0.015 464 PHE CCC C   
3622  O O   . PHE C 135 ? 0.608 0.504 0.623 -0.081 -0.074 -0.025 464 PHE CCC O   
3623  C CB  . PHE C 135 ? 0.647 0.519 0.640 -0.071 -0.079 -0.014 464 PHE CCC CB  
3624  C CG  . PHE C 135 ? 0.646 0.517 0.630 -0.063 -0.081 -0.008 464 PHE CCC CG  
3625  C CD1 . PHE C 135 ? 0.641 0.521 0.615 -0.059 -0.080 -0.007 464 PHE CCC CD1 
3626  C CD2 . PHE C 135 ? 0.647 0.505 0.634 -0.059 -0.085 -0.006 464 PHE CCC CD2 
3627  C CE1 . PHE C 135 ? 0.653 0.531 0.620 -0.053 -0.082 -0.002 464 PHE CCC CE1 
3628  C CE2 . PHE C 135 ? 0.652 0.510 0.633 -0.051 -0.087 -0.001 464 PHE CCC CE2 
3629  C CZ  . PHE C 135 ? 0.650 0.519 0.622 -0.049 -0.086 0.000  464 PHE CCC CZ  
3630  N N   . GLU C 136 ? 0.639 0.523 0.647 -0.095 -0.062 -0.010 465 GLU CCC N   
3631  C CA  . GLU C 136 ? 0.640 0.536 0.666 -0.103 -0.057 -0.016 465 GLU CCC CA  
3632  C C   . GLU C 136 ? 0.636 0.550 0.664 -0.098 -0.053 -0.020 465 GLU CCC C   
3633  O O   . GLU C 136 ? 0.587 0.500 0.599 -0.094 -0.050 -0.016 465 GLU CCC O   
3634  C CB  . GLU C 136 ? 0.665 0.553 0.694 -0.116 -0.048 -0.009 465 GLU CCC CB  
3635  C CG  . GLU C 136 ? 0.680 0.578 0.734 -0.124 -0.044 -0.015 465 GLU CCC CG  
3636  C CD  . GLU C 136 ? 0.736 0.624 0.792 -0.138 -0.034 -0.007 465 GLU CCC CD  
3637  O OE1 . GLU C 136 ? 0.740 0.612 0.776 -0.142 -0.031 0.005  465 GLU CCC OE1 
3638  O OE2 . GLU C 136 ? 0.742 0.641 0.821 -0.147 -0.028 -0.012 465 GLU CCC OE2 
3639  N N   . ARG C 137 ? 0.626 0.557 0.676 -0.099 -0.054 -0.028 466 ARG CCC N   
3640  C CA  . ARG C 137 ? 0.617 0.566 0.675 -0.094 -0.051 -0.032 466 ARG CCC CA  
3641  C C   . ARG C 137 ? 0.588 0.551 0.671 -0.102 -0.044 -0.036 466 ARG CCC C   
3642  O O   . ARG C 137 ? 0.556 0.522 0.656 -0.107 -0.049 -0.040 466 ARG CCC O   
3643  C CB  . ARG C 137 ? 0.630 0.588 0.691 -0.083 -0.063 -0.039 466 ARG CCC CB  
3644  C CG  . ARG C 137 ? 0.670 0.644 0.738 -0.075 -0.062 -0.040 466 ARG CCC CG  
3645  C CD  . ARG C 137 ? 0.734 0.711 0.795 -0.065 -0.074 -0.044 466 ARG CCC CD  
3646  N NE  . ARG C 137 ? 0.787 0.776 0.853 -0.056 -0.076 -0.043 466 ARG CCC NE  
3647  C CZ  . ARG C 137 ? 0.858 0.866 0.945 -0.053 -0.082 -0.047 466 ARG CCC CZ  
3648  N NH1 . ARG C 137 ? 0.884 0.903 0.992 -0.060 -0.086 -0.053 466 ARG CCC NH1 
3649  N NH2 . ARG C 137 ? 0.872 0.889 0.961 -0.043 -0.084 -0.045 466 ARG CCC NH2 
3650  N N   . ASP C 138 ? 0.586 0.556 0.672 -0.104 -0.031 -0.034 467 ASP CCC N   
3651  C CA  . ASP C 138 ? 0.573 0.558 0.685 -0.112 -0.021 -0.037 467 ASP CCC CA  
3652  C C   . ASP C 138 ? 0.567 0.571 0.694 -0.103 -0.017 -0.041 467 ASP CCC C   
3653  O O   . ASP C 138 ? 0.559 0.558 0.670 -0.099 -0.009 -0.039 467 ASP CCC O   
3654  C CB  . ASP C 138 ? 0.593 0.566 0.693 -0.124 -0.005 -0.030 467 ASP CCC CB  
3655  C CG  . ASP C 138 ? 0.591 0.579 0.718 -0.134 0.008  -0.032 467 ASP CCC CG  
3656  O OD1 . ASP C 138 ? 0.578 0.588 0.736 -0.131 0.006  -0.040 467 ASP CCC OD1 
3657  O OD2 . ASP C 138 ? 0.601 0.579 0.718 -0.146 0.021  -0.026 467 ASP CCC OD2 
3658  N N   . ILE C 139 ? 0.590 0.615 0.748 -0.100 -0.025 -0.048 468 ILE CCC N   
3659  C CA  . ILE C 139 ? 0.572 0.617 0.751 -0.091 -0.023 -0.051 468 ILE CCC CA  
3660  C C   . ILE C 139 ? 0.543 0.608 0.758 -0.098 -0.012 -0.055 468 ILE CCC C   
3661  O O   . ILE C 139 ? 0.528 0.613 0.769 -0.090 -0.012 -0.057 468 ILE CCC O   
3662  C CB  . ILE C 139 ? 0.575 0.629 0.758 -0.079 -0.042 -0.053 468 ILE CCC CB  
3663  C CG1 . ILE C 139 ? 0.608 0.672 0.810 -0.084 -0.056 -0.059 468 ILE CCC CG1 
3664  C CG2 . ILE C 139 ? 0.586 0.620 0.734 -0.072 -0.049 -0.049 468 ILE CCC CG2 
3665  C CD1 . ILE C 139 ? 0.628 0.710 0.841 -0.073 -0.073 -0.061 468 ILE CCC CD1 
3666  N N   . SER C 140 ? 0.534 0.595 0.753 -0.112 -0.003 -0.053 469 SER CCC N   
3667  C CA  . SER C 140 ? 0.539 0.619 0.794 -0.121 0.010  -0.056 469 SER CCC CA  
3668  C C   . SER C 140 ? 0.556 0.641 0.812 -0.118 0.031  -0.056 469 SER CCC C   
3669  O O   . SER C 140 ? 0.546 0.612 0.767 -0.115 0.037  -0.053 469 SER CCC O   
3670  C CB  . SER C 140 ? 0.550 0.619 0.803 -0.138 0.017  -0.053 469 SER CCC CB  
3671  O OG  . SER C 140 ? 0.576 0.622 0.794 -0.144 0.030  -0.046 469 SER CCC OG  
3672  N N   . THR C 141 ? 0.569 0.678 0.865 -0.120 0.041  -0.061 470 THR CCC N   
3673  C CA  . THR C 141 ? 0.575 0.691 0.880 -0.117 0.063  -0.064 470 THR CCC CA  
3674  C C   . THR C 141 ? 0.581 0.711 0.914 -0.131 0.082  -0.065 470 THR CCC C   
3675  O O   . THR C 141 ? 0.590 0.743 0.959 -0.127 0.095  -0.070 470 THR CCC O   
3676  C CB  . THR C 141 ? 0.555 0.689 0.885 -0.099 0.056  -0.067 470 THR CCC CB  
3677  O OG1 . THR C 141 ? 0.542 0.702 0.914 -0.098 0.041  -0.070 470 THR CCC OG1 
3678  C CG2 . THR C 141 ? 0.540 0.657 0.838 -0.087 0.041  -0.064 470 THR CCC CG2 
3679  N N   . GLU C 142 ? 0.607 0.723 0.924 -0.146 0.085  -0.061 471 GLU CCC N   
3680  C CA  . GLU C 142 ? 0.618 0.744 0.957 -0.162 0.105  -0.060 471 GLU CCC CA  
3681  C C   . GLU C 142 ? 0.617 0.733 0.932 -0.166 0.132  -0.059 471 GLU CCC C   
3682  O O   . GLU C 142 ? 0.606 0.697 0.873 -0.163 0.132  -0.055 471 GLU CCC O   
3683  C CB  . GLU C 142 ? 0.650 0.760 0.977 -0.178 0.099  -0.054 471 GLU CCC CB  
3684  C CG  . GLU C 142 ? 0.675 0.789 1.016 -0.175 0.072  -0.056 471 GLU CCC CG  
3685  C CD  . GLU C 142 ? 0.693 0.840 1.090 -0.176 0.065  -0.064 471 GLU CCC CD  
3686  O OE1 . GLU C 142 ? 0.754 0.903 1.160 -0.175 0.043  -0.067 471 GLU CCC OE1 
3687  O OE2 . GLU C 142 ? 0.721 0.891 1.153 -0.178 0.082  -0.067 471 GLU CCC OE2 
3688  N N   . ILE C 143 ? 0.624 0.761 0.973 -0.172 0.154  -0.064 472 ILE CCC N   
3689  C CA  . ILE C 143 ? 0.659 0.789 0.988 -0.177 0.184  -0.065 472 ILE CCC CA  
3690  C C   . ILE C 143 ? 0.684 0.785 0.964 -0.193 0.190  -0.054 472 ILE CCC C   
3691  O O   . ILE C 143 ? 0.718 0.817 1.007 -0.206 0.186  -0.048 472 ILE CCC O   
3692  C CB  . ILE C 143 ? 0.672 0.832 1.052 -0.183 0.208  -0.071 472 ILE CCC CB  
3693  C CG1 . ILE C 143 ? 0.653 0.843 1.085 -0.166 0.200  -0.080 472 ILE CCC CG1 
3694  C CG2 . ILE C 143 ? 0.702 0.852 1.055 -0.191 0.241  -0.073 472 ILE CCC CG2 
3695  C CD1 . ILE C 143 ? 0.655 0.880 1.150 -0.172 0.212  -0.084 472 ILE CCC CD1 
3696  N N   . TYR C 144 ? 0.697 0.774 0.926 -0.192 0.196  -0.052 473 TYR CCC N   
3697  C CA  . TYR C 144 ? 0.732 0.780 0.908 -0.205 0.199  -0.040 473 TYR CCC CA  
3698  C C   . TYR C 144 ? 0.789 0.838 0.959 -0.220 0.231  -0.039 473 TYR CCC C   
3699  O O   . TYR C 144 ? 0.802 0.861 0.975 -0.217 0.251  -0.049 473 TYR CCC O   
3700  C CB  . TYR C 144 ? 0.724 0.749 0.852 -0.196 0.188  -0.039 473 TYR CCC CB  
3701  C CG  . TYR C 144 ? 0.757 0.754 0.830 -0.209 0.190  -0.027 473 TYR CCC CG  
3702  C CD1 . TYR C 144 ? 0.748 0.728 0.806 -0.212 0.170  -0.015 473 TYR CCC CD1 
3703  C CD2 . TYR C 144 ? 0.782 0.768 0.818 -0.216 0.211  -0.027 473 TYR CCC CD2 
3704  C CE1 . TYR C 144 ? 0.763 0.718 0.774 -0.221 0.169  -0.002 473 TYR CCC CE1 
3705  C CE2 . TYR C 144 ? 0.809 0.771 0.794 -0.227 0.210  -0.014 473 TYR CCC CE2 
3706  C CZ  . TYR C 144 ? 0.797 0.743 0.770 -0.229 0.189  -0.001 473 TYR CCC CZ  
3707  O OH  . TYR C 144 ? 0.843 0.765 0.768 -0.239 0.186  0.013  473 TYR CCC OH  
3708  N N   . GLN C 145 ? 0.829 0.871 0.994 -0.237 0.235  -0.028 474 GLN CCC N   
3709  C CA  . GLN C 145 ? 0.863 0.902 1.014 -0.254 0.266  -0.024 474 GLN CCC CA  
3710  C C   . GLN C 145 ? 0.915 0.922 0.996 -0.260 0.269  -0.015 474 GLN CCC C   
3711  O O   . GLN C 145 ? 0.947 0.932 0.999 -0.266 0.254  -0.001 474 GLN CCC O   
3712  C CB  . GLN C 145 ? 0.869 0.911 1.046 -0.270 0.269  -0.015 474 GLN CCC CB  
3713  C CG  . GLN C 145 ? 0.913 0.948 1.068 -0.289 0.300  -0.008 474 GLN CCC CG  
3714  C CD  . GLN C 145 ? 0.914 0.959 1.109 -0.305 0.307  -0.001 474 GLN CCC CD  
3715  O OE1 . GLN C 145 ? 0.895 0.960 1.142 -0.301 0.294  -0.007 474 GLN CCC OE1 
3716  N NE2 . GLN C 145 ? 0.967 0.998 1.134 -0.323 0.329  0.011  474 GLN CCC NE2 
3717  N N   . ALA C 146 ? 0.953 0.959 1.009 -0.257 0.286  -0.024 475 ALA CCC N   
3718  C CA  . ALA C 146 ? 1.004 0.983 0.992 -0.262 0.289  -0.018 475 ALA CCC CA  
3719  C C   . ALA C 146 ? 1.069 1.041 1.029 -0.282 0.318  -0.011 475 ALA CCC C   
3720  O O   . ALA C 146 ? 1.144 1.093 1.044 -0.289 0.319  -0.003 475 ALA CCC O   
3721  C CB  . ALA C 146 ? 0.990 0.972 0.968 -0.249 0.293  -0.034 475 ALA CCC CB  
3722  N N   . GLY C 147 ? 1.064 1.055 1.064 -0.290 0.340  -0.013 476 GLY CCC N   
3723  C CA  . GLY C 147 ? 1.114 1.101 1.092 -0.310 0.372  -0.007 476 GLY CCC CA  
3724  C C   . GLY C 147 ? 1.114 1.106 1.121 -0.324 0.376  0.006  476 GLY CCC C   
3725  O O   . GLY C 147 ? 1.109 1.107 1.154 -0.319 0.353  0.009  476 GLY CCC O   
3726  N N   . SER C 148 ? 1.138 1.125 1.125 -0.343 0.405  0.014  477 SER CCC N   
3727  C CA  . SER C 148 ? 1.155 1.148 1.171 -0.360 0.418  0.026  477 SER CCC CA  
3728  C C   . SER C 148 ? 1.110 1.139 1.210 -0.355 0.420  0.013  477 SER CCC C   
3729  O O   . SER C 148 ? 1.089 1.119 1.222 -0.361 0.406  0.021  477 SER CCC O   
3730  C CB  . SER C 148 ? 1.214 1.201 1.195 -0.380 0.455  0.032  477 SER CCC CB  
3731  O OG  . SER C 148 ? 1.266 1.224 1.169 -0.382 0.453  0.039  477 SER CCC OG  
3732  N N   . THR C 149 ? 1.083 1.139 1.216 -0.344 0.436  -0.006 478 THR CCC N   
3733  C CA  . THR C 149 ? 1.056 1.151 1.271 -0.341 0.443  -0.018 478 THR CCC CA  
3734  C C   . THR C 149 ? 0.994 1.097 1.248 -0.326 0.405  -0.021 478 THR CCC C   
3735  O O   . THR C 149 ? 0.948 1.039 1.178 -0.310 0.381  -0.024 478 THR CCC O   
3736  C CB  . THR C 149 ? 1.073 1.193 1.313 -0.331 0.469  -0.037 478 THR CCC CB  
3737  O OG1 . THR C 149 ? 1.135 1.241 1.324 -0.343 0.501  -0.037 478 THR CCC OG1 
3738  C CG2 . THR C 149 ? 1.062 1.222 1.385 -0.333 0.483  -0.046 478 THR CCC CG2 
3739  N N   . PRO C 150 ? 0.978 1.104 1.294 -0.331 0.398  -0.021 479 PRO CCC N   
3740  C CA  . PRO C 150 ? 0.932 1.070 1.288 -0.317 0.364  -0.027 479 PRO CCC CA  
3741  C C   . PRO C 150 ? 0.896 1.063 1.289 -0.297 0.364  -0.044 479 PRO CCC C   
3742  O O   . PRO C 150 ? 0.893 1.078 1.304 -0.297 0.393  -0.052 479 PRO CCC O   
3743  C CB  . PRO C 150 ? 0.909 1.063 1.318 -0.332 0.364  -0.023 479 PRO CCC CB  
3744  C CG  . PRO C 150 ? 0.943 1.110 1.366 -0.349 0.404  -0.022 479 PRO CCC CG  
3745  C CD  . PRO C 150 ? 0.982 1.121 1.331 -0.352 0.423  -0.015 479 PRO CCC CD  
3746  N N   . CYS C 151 ? 0.869 1.040 1.275 -0.279 0.333  -0.049 480 CYS CCC N   
3747  C CA  . CYS C 151 ? 0.871 1.061 1.301 -0.258 0.328  -0.063 480 CYS CCC CA  
3748  C C   . CYS C 151 ? 0.829 1.060 1.339 -0.252 0.321  -0.071 480 CYS CCC C   
3749  O O   . CYS C 151 ? 0.795 1.048 1.336 -0.237 0.326  -0.082 480 CYS CCC O   
3750  C CB  . CYS C 151 ? 0.904 1.073 1.296 -0.242 0.298  -0.062 480 CYS CCC CB  
3751  S SG  . CYS C 151 ? 1.039 1.166 1.343 -0.245 0.307  -0.055 480 CYS CCC SG  
3752  N N   . ASN C 152 ? 0.825 1.067 1.368 -0.265 0.310  -0.067 481 ASN CCC N   
3753  C CA  . ASN C 152 ? 0.812 1.095 1.433 -0.263 0.302  -0.074 481 ASN CCC CA  
3754  C C   . ASN C 152 ? 0.803 1.103 1.448 -0.239 0.276  -0.082 481 ASN CCC C   
3755  O O   . ASN C 152 ? 0.783 1.121 1.490 -0.231 0.280  -0.091 481 ASN CCC O   
3756  C CB  . ASN C 152 ? 0.809 1.123 1.480 -0.271 0.337  -0.079 481 ASN CCC CB  
3757  C CG  . ASN C 152 ? 0.789 1.145 1.541 -0.275 0.327  -0.085 481 ASN CCC CG  
3758  O OD1 . ASN C 152 ? 0.768 1.121 1.528 -0.283 0.304  -0.081 481 ASN CCC OD1 
3759  N ND2 . ASN C 152 ? 0.784 1.179 1.597 -0.267 0.343  -0.094 481 ASN CCC ND2 
3760  N N   . GLY C 153 ? 0.824 1.097 1.422 -0.228 0.252  -0.079 482 GLY CCC N   
3761  C CA  . GLY C 153 ? 0.813 1.096 1.423 -0.206 0.226  -0.085 482 GLY CCC CA  
3762  C C   . GLY C 153 ? 0.825 1.124 1.454 -0.189 0.241  -0.093 482 GLY CCC C   
3763  O O   . GLY C 153 ? 0.858 1.179 1.524 -0.172 0.223  -0.097 482 GLY CCC O   
3764  N N   . VAL C 154 ? 0.813 1.101 1.418 -0.193 0.274  -0.094 483 VAL CCC N   
3765  C CA  . VAL C 154 ? 0.777 1.074 1.394 -0.178 0.293  -0.104 483 VAL CCC CA  
3766  C C   . VAL C 154 ? 0.775 1.033 1.318 -0.177 0.302  -0.103 483 VAL CCC C   
3767  O O   . VAL C 154 ? 0.776 1.009 1.270 -0.193 0.311  -0.096 483 VAL CCC O   
3768  C CB  . VAL C 154 ? 0.812 1.138 1.477 -0.186 0.328  -0.110 483 VAL CCC CB  
3769  C CG1 . VAL C 154 ? 0.832 1.157 1.494 -0.173 0.355  -0.120 483 VAL CCC CG1 
3770  C CG2 . VAL C 154 ? 0.787 1.156 1.534 -0.184 0.318  -0.113 483 VAL CCC CG2 
3771  N N   . GLU C 155 ? 0.760 1.012 1.294 -0.158 0.297  -0.108 484 GLU CCC N   
3772  C CA  . GLU C 155 ? 0.778 0.994 1.245 -0.156 0.304  -0.109 484 GLU CCC CA  
3773  C C   . GLU C 155 ? 0.805 1.021 1.267 -0.162 0.345  -0.118 484 GLU CCC C   
3774  O O   . GLU C 155 ? 0.818 1.065 1.338 -0.158 0.363  -0.126 484 GLU CCC O   
3775  C CB  . GLU C 155 ? 0.759 0.971 1.227 -0.134 0.284  -0.113 484 GLU CCC CB  
3776  C CG  . GLU C 155 ? 0.779 0.953 1.177 -0.134 0.280  -0.111 484 GLU CCC CG  
3777  C CD  . GLU C 155 ? 0.764 0.929 1.155 -0.115 0.257  -0.111 484 GLU CCC CD  
3778  O OE1 . GLU C 155 ? 0.726 0.912 1.162 -0.102 0.238  -0.110 484 GLU CCC OE1 
3779  O OE2 . GLU C 155 ? 0.770 0.905 1.108 -0.115 0.256  -0.112 484 GLU CCC OE2 
3780  N N   . GLY C 156 ? 0.819 1.004 1.214 -0.171 0.358  -0.118 485 GLY CCC N   
3781  C CA  . GLY C 156 ? 0.861 1.040 1.238 -0.178 0.397  -0.127 485 GLY CCC CA  
3782  C C   . GLY C 156 ? 0.921 1.065 1.218 -0.193 0.403  -0.121 485 GLY CCC C   
3783  O O   . GLY C 156 ? 0.921 1.042 1.177 -0.192 0.376  -0.113 485 GLY CCC O   
3784  N N   . PHE C 157 ? 1.014 1.154 1.290 -0.207 0.438  -0.126 486 PHE CCC N   
3785  C CA  . PHE C 157 ? 1.091 1.199 1.288 -0.224 0.448  -0.120 486 PHE CCC CA  
3786  C C   . PHE C 157 ? 1.063 1.158 1.236 -0.236 0.423  -0.101 486 PHE CCC C   
3787  O O   . PHE C 157 ? 1.001 1.114 1.212 -0.244 0.423  -0.093 486 PHE CCC O   
3788  C CB  . PHE C 157 ? 1.185 1.297 1.373 -0.238 0.492  -0.127 486 PHE CCC CB  
3789  C CG  . PHE C 157 ? 1.286 1.367 1.392 -0.257 0.504  -0.121 486 PHE CCC CG  
3790  C CD1 . PHE C 157 ? 1.320 1.369 1.361 -0.255 0.484  -0.118 486 PHE CCC CD1 
3791  C CD2 . PHE C 157 ? 1.375 1.460 1.470 -0.276 0.536  -0.118 486 PHE CCC CD2 
3792  C CE1 . PHE C 157 ? 1.388 1.412 1.355 -0.273 0.494  -0.111 486 PHE CCC CE1 
3793  C CE2 . PHE C 157 ? 1.447 1.503 1.464 -0.293 0.548  -0.111 486 PHE CCC CE2 
3794  C CZ  . PHE C 157 ? 1.458 1.484 1.411 -0.292 0.526  -0.107 486 PHE CCC CZ  
3795  N N   . ASN C 158 ? 1.063 1.128 1.177 -0.236 0.401  -0.093 487 ASN CCC N   
3796  C CA  . ASN C 158 ? 1.068 1.115 1.151 -0.246 0.377  -0.074 487 ASN CCC CA  
3797  C C   . ASN C 158 ? 1.001 1.066 1.138 -0.238 0.350  -0.069 487 ASN CCC C   
3798  O O   . ASN C 158 ? 0.975 1.030 1.102 -0.247 0.335  -0.055 487 ASN CCC O   
3799  C CB  . ASN C 158 ? 1.106 1.145 1.162 -0.268 0.398  -0.063 487 ASN CCC CB  
3800  C CG  . ASN C 158 ? 1.153 1.170 1.141 -0.278 0.418  -0.065 487 ASN CCC CG  
3801  O OD1 . ASN C 158 ? 1.155 1.151 1.098 -0.272 0.404  -0.066 487 ASN CCC OD1 
3802  N ND2 . ASN C 158 ? 1.208 1.228 1.188 -0.294 0.451  -0.065 487 ASN CCC ND2 
3803  N N   . CYS C 159 ? 0.963 1.050 1.152 -0.221 0.343  -0.080 488 CYS CCC N   
3804  C CA  . CYS C 159 ? 0.912 1.019 1.153 -0.212 0.318  -0.077 488 CYS CCC CA  
3805  C C   . CYS C 159 ? 0.880 0.987 1.129 -0.191 0.296  -0.084 488 CYS CCC C   
3806  O O   . CYS C 159 ? 0.862 0.992 1.158 -0.178 0.302  -0.094 488 CYS CCC O   
3807  C CB  . CYS C 159 ? 0.909 1.050 1.217 -0.215 0.335  -0.083 488 CYS CCC CB  
3808  S SG  . CYS C 159 ? 0.921 1.062 1.227 -0.242 0.352  -0.071 488 CYS CCC SG  
3809  N N   . TYR C 160 ? 0.871 0.955 1.078 -0.187 0.272  -0.077 489 TYR CCC N   
3810  C CA  . TYR C 160 ? 0.848 0.923 1.044 -0.170 0.256  -0.083 489 TYR CCC CA  
3811  C C   . TYR C 160 ? 0.806 0.891 1.031 -0.159 0.225  -0.078 489 TYR CCC C   
3812  O O   . TYR C 160 ? 0.809 0.890 1.031 -0.167 0.209  -0.069 489 TYR CCC O   
3813  C CB  . TYR C 160 ? 0.861 0.903 0.989 -0.174 0.252  -0.078 489 TYR CCC CB  
3814  C CG  . TYR C 160 ? 0.937 0.970 1.031 -0.187 0.282  -0.083 489 TYR CCC CG  
3815  C CD1 . TYR C 160 ? 0.961 1.007 1.078 -0.183 0.309  -0.097 489 TYR CCC CD1 
3816  C CD2 . TYR C 160 ? 0.991 1.001 1.031 -0.202 0.283  -0.073 489 TYR CCC CD2 
3817  C CE1 . TYR C 160 ? 1.002 1.037 1.084 -0.195 0.338  -0.102 489 TYR CCC CE1 
3818  C CE2 . TYR C 160 ? 1.041 1.041 1.044 -0.214 0.310  -0.076 489 TYR CCC CE2 
3819  C CZ  . TYR C 160 ? 1.043 1.055 1.066 -0.211 0.338  -0.092 489 TYR CCC CZ  
3820  O OH  . TYR C 160 ? 1.120 1.121 1.103 -0.224 0.366  -0.096 489 TYR CCC OH  
3821  N N   . PHE C 161 ? 0.766 0.863 1.018 -0.142 0.216  -0.085 490 PHE CCC N   
3822  C CA  . PHE C 161 ? 0.721 0.820 0.984 -0.129 0.185  -0.082 490 PHE CCC CA  
3823  C C   . PHE C 161 ? 0.713 0.781 0.919 -0.131 0.172  -0.075 490 PHE CCC C   
3824  O O   . PHE C 161 ? 0.703 0.754 0.874 -0.131 0.182  -0.078 490 PHE CCC O   
3825  C CB  . PHE C 161 ? 0.709 0.824 1.009 -0.110 0.184  -0.089 490 PHE CCC CB  
3826  C CG  . PHE C 161 ? 0.710 0.831 1.024 -0.097 0.154  -0.085 490 PHE CCC CG  
3827  C CD1 . PHE C 161 ? 0.692 0.836 1.045 -0.097 0.139  -0.083 490 PHE CCC CD1 
3828  C CD2 . PHE C 161 ? 0.702 0.804 0.987 -0.087 0.141  -0.084 490 PHE CCC CD2 
3829  C CE1 . PHE C 161 ? 0.656 0.805 1.019 -0.086 0.111  -0.080 490 PHE CCC CE1 
3830  C CE2 . PHE C 161 ? 0.692 0.800 0.988 -0.075 0.115  -0.080 490 PHE CCC CE2 
3831  C CZ  . PHE C 161 ? 0.674 0.805 1.007 -0.074 0.100  -0.078 490 PHE CCC CZ  
3832  N N   . PRO C 162 ? 0.717 0.778 0.912 -0.133 0.149  -0.067 491 PRO CCC N   
3833  C CA  . PRO C 162 ? 0.718 0.751 0.861 -0.137 0.139  -0.059 491 PRO CCC CA  
3834  C C   . PRO C 162 ? 0.682 0.703 0.805 -0.124 0.124  -0.060 491 PRO CCC C   
3835  O O   . PRO C 162 ? 0.646 0.646 0.727 -0.128 0.118  -0.055 491 PRO CCC O   
3836  C CB  . PRO C 162 ? 0.719 0.752 0.870 -0.143 0.121  -0.051 491 PRO CCC CB  
3837  C CG  . PRO C 162 ? 0.699 0.758 0.899 -0.135 0.111  -0.056 491 PRO CCC CG  
3838  C CD  . PRO C 162 ? 0.712 0.791 0.945 -0.131 0.132  -0.065 491 PRO CCC CD  
3839  N N   . LEU C 163 ? 0.675 0.710 0.828 -0.109 0.118  -0.066 492 LEU CCC N   
3840  C CA  . LEU C 163 ? 0.668 0.692 0.804 -0.097 0.106  -0.066 492 LEU CCC CA  
3841  C C   . LEU C 163 ? 0.679 0.697 0.809 -0.093 0.124  -0.075 492 LEU CCC C   
3842  O O   . LEU C 163 ? 0.675 0.708 0.834 -0.092 0.142  -0.082 492 LEU CCC O   
3843  C CB  . LEU C 163 ? 0.638 0.677 0.806 -0.083 0.087  -0.065 492 LEU CCC CB  
3844  C CG  . LEU C 163 ? 0.607 0.651 0.781 -0.087 0.067  -0.060 492 LEU CCC CG  
3845  C CD1 . LEU C 163 ? 0.575 0.631 0.770 -0.073 0.048  -0.059 492 LEU CCC CD1 
3846  C CD2 . LEU C 163 ? 0.605 0.627 0.738 -0.095 0.059  -0.053 492 LEU CCC CD2 
3847  N N   . GLN C 164 ? 0.694 0.692 0.789 -0.091 0.121  -0.075 493 GLN CCC N   
3848  C CA  . GLN C 164 ? 0.742 0.729 0.826 -0.087 0.136  -0.084 493 GLN CCC CA  
3849  C C   . GLN C 164 ? 0.704 0.683 0.786 -0.074 0.121  -0.083 493 GLN CCC C   
3850  O O   . GLN C 164 ? 0.666 0.640 0.736 -0.072 0.100  -0.075 493 GLN CCC O   
3851  C CB  . GLN C 164 ? 0.832 0.800 0.869 -0.102 0.149  -0.086 493 GLN CCC CB  
3852  C CG  . GLN C 164 ? 0.907 0.862 0.927 -0.101 0.165  -0.097 493 GLN CCC CG  
3853  C CD  . GLN C 164 ? 0.943 0.911 0.996 -0.098 0.190  -0.109 493 GLN CCC CD  
3854  O OE1 . GLN C 164 ? 0.934 0.907 1.018 -0.084 0.192  -0.115 493 GLN CCC OE1 
3855  N NE2 . GLN C 164 ? 0.971 0.944 1.019 -0.110 0.208  -0.111 493 GLN CCC NE2 
3856  N N   . SER C 165 ? 0.690 0.668 0.787 -0.065 0.132  -0.091 494 SER CCC N   
3857  C CA  . SER C 165 ? 0.666 0.635 0.767 -0.052 0.120  -0.090 494 SER CCC CA  
3858  C C   . SER C 165 ? 0.663 0.607 0.721 -0.058 0.123  -0.094 494 SER CCC C   
3859  O O   . SER C 165 ? 0.700 0.634 0.735 -0.069 0.140  -0.102 494 SER CCC O   
3860  C CB  . SER C 165 ? 0.666 0.646 0.808 -0.038 0.131  -0.097 494 SER CCC CB  
3861  O OG  . SER C 165 ? 0.710 0.680 0.855 -0.026 0.120  -0.094 494 SER CCC OG  
3862  N N   . TYR C 166 ? 0.644 0.577 0.689 -0.053 0.107  -0.088 495 TYR CCC N   
3863  C CA  . TYR C 166 ? 0.668 0.579 0.676 -0.059 0.107  -0.092 495 TYR CCC CA  
3864  C C   . TYR C 166 ? 0.687 0.586 0.703 -0.053 0.123  -0.103 495 TYR CCC C   
3865  O O   . TYR C 166 ? 0.722 0.605 0.710 -0.062 0.134  -0.113 495 TYR CCC O   
3866  C CB  . TYR C 166 ? 0.647 0.552 0.643 -0.056 0.085  -0.082 495 TYR CCC CB  
3867  C CG  . TYR C 166 ? 0.626 0.530 0.597 -0.066 0.073  -0.073 495 TYR CCC CG  
3868  C CD1 . TYR C 166 ? 0.636 0.529 0.572 -0.080 0.075  -0.075 495 TYR CCC CD1 
3869  C CD2 . TYR C 166 ? 0.621 0.538 0.606 -0.062 0.057  -0.064 495 TYR CCC CD2 
3870  C CE1 . TYR C 166 ? 0.640 0.532 0.556 -0.087 0.063  -0.065 495 TYR CCC CE1 
3871  C CE2 . TYR C 166 ? 0.616 0.532 0.582 -0.069 0.046  -0.056 495 TYR CCC CE2 
3872  C CZ  . TYR C 166 ? 0.617 0.520 0.550 -0.082 0.049  -0.056 495 TYR CCC CZ  
3873  O OH  . TYR C 166 ? 0.624 0.526 0.541 -0.088 0.038  -0.047 495 TYR CCC OH  
3874  N N   . GLY C 167 ? 0.687 0.595 0.743 -0.038 0.124  -0.103 496 GLY CCC N   
3875  C CA  . GLY C 167 ? 0.749 0.644 0.816 -0.031 0.138  -0.114 496 GLY CCC CA  
3876  C C   . GLY C 167 ? 0.796 0.666 0.833 -0.035 0.133  -0.115 496 GLY CCC C   
3877  O O   . GLY C 167 ? 0.842 0.696 0.850 -0.046 0.146  -0.127 496 GLY CCC O   
3878  N N   . PHE C 168 ? 0.757 0.626 0.797 -0.027 0.114  -0.104 497 PHE CCC N   
3879  C CA  . PHE C 168 ? 0.759 0.607 0.775 -0.031 0.107  -0.103 497 PHE CCC CA  
3880  C C   . PHE C 168 ? 0.777 0.608 0.809 -0.022 0.117  -0.110 497 PHE CCC C   
3881  O O   . PHE C 168 ? 0.748 0.586 0.813 -0.007 0.114  -0.103 497 PHE CCC O   
3882  C CB  . PHE C 168 ? 0.717 0.572 0.732 -0.027 0.084  -0.087 497 PHE CCC CB  
3883  C CG  . PHE C 168 ? 0.668 0.533 0.662 -0.037 0.073  -0.081 497 PHE CCC CG  
3884  C CD1 . PHE C 168 ? 0.661 0.516 0.620 -0.052 0.074  -0.085 497 PHE CCC CD1 
3885  C CD2 . PHE C 168 ? 0.632 0.515 0.641 -0.032 0.061  -0.071 497 PHE CCC CD2 
3886  C CE1 . PHE C 168 ? 0.647 0.510 0.590 -0.060 0.063  -0.078 497 PHE CCC CE1 
3887  C CE2 . PHE C 168 ? 0.621 0.510 0.612 -0.040 0.051  -0.065 497 PHE CCC CE2 
3888  C CZ  . PHE C 168 ? 0.613 0.493 0.573 -0.054 0.052  -0.068 497 PHE CCC CZ  
3889  N N   . GLN C 169 ? 0.854 0.664 0.864 -0.031 0.128  -0.123 498 GLN CCC N   
3890  C CA  . GLN C 169 ? 0.862 0.651 0.885 -0.025 0.138  -0.131 498 GLN CCC CA  
3891  C C   . GLN C 169 ? 0.866 0.636 0.864 -0.032 0.128  -0.129 498 GLN CCC C   
3892  O O   . GLN C 169 ? 0.909 0.677 0.874 -0.047 0.122  -0.131 498 GLN CCC O   
3893  C CB  . GLN C 169 ? 0.912 0.690 0.932 -0.029 0.163  -0.151 498 GLN CCC CB  
3894  C CG  . GLN C 169 ? 0.919 0.719 0.968 -0.021 0.174  -0.153 498 GLN CCC CG  
3895  C CD  . GLN C 169 ? 0.966 0.754 1.024 -0.020 0.201  -0.172 498 GLN CCC CD  
3896  O OE1 . GLN C 169 ? 1.016 0.792 1.102 -0.008 0.210  -0.177 498 GLN CCC OE1 
3897  N NE2 . GLN C 169 ? 1.006 0.798 1.041 -0.033 0.215  -0.184 498 GLN CCC NE2 
3898  N N   . PRO C 170 ? 0.886 0.642 0.903 -0.023 0.126  -0.125 499 PRO CCC N   
3899  C CA  . PRO C 170 ? 0.878 0.617 0.877 -0.030 0.117  -0.121 499 PRO CCC CA  
3900  C C   . PRO C 170 ? 0.882 0.602 0.848 -0.048 0.125  -0.139 499 PRO CCC C   
3901  O O   . PRO C 170 ? 0.899 0.615 0.844 -0.059 0.114  -0.136 499 PRO CCC O   
3902  C CB  . PRO C 170 ? 0.888 0.613 0.917 -0.016 0.118  -0.115 499 PRO CCC CB  
3903  C CG  . PRO C 170 ? 0.901 0.630 0.962 -0.002 0.133  -0.121 499 PRO CCC CG  
3904  C CD  . PRO C 170 ? 0.896 0.651 0.953 -0.004 0.133  -0.122 499 PRO CCC CD  
3905  N N   . THR C 171 ? 0.873 0.586 0.837 -0.051 0.144  -0.157 500 THR CCC N   
3906  C CA  . THR C 171 ? 0.893 0.587 0.823 -0.068 0.154  -0.177 500 THR CCC CA  
3907  C C   . THR C 171 ? 0.867 0.574 0.760 -0.083 0.150  -0.179 500 THR CCC C   
3908  O O   . THR C 171 ? 0.896 0.591 0.757 -0.099 0.154  -0.193 500 THR CCC O   
3909  C CB  . THR C 171 ? 0.911 0.589 0.854 -0.063 0.180  -0.196 500 THR CCC CB  
3910  O OG1 . THR C 171 ? 0.888 0.586 0.851 -0.054 0.189  -0.194 500 THR CCC OG1 
3911  C CG2 . THR C 171 ? 0.915 0.572 0.889 -0.051 0.184  -0.196 500 THR CCC CG2 
3912  N N   . ASN C 172 ? 0.844 0.575 0.742 -0.080 0.141  -0.165 501 ASN CCC N   
3913  C CA  . ASN C 172 ? 0.838 0.582 0.703 -0.094 0.134  -0.163 501 ASN CCC CA  
3914  C C   . ASN C 172 ? 0.828 0.563 0.660 -0.108 0.119  -0.162 501 ASN CCC C   
3915  O O   . ASN C 172 ? 0.817 0.548 0.662 -0.105 0.108  -0.154 501 ASN CCC O   
3916  C CB  . ASN C 172 ? 0.819 0.588 0.698 -0.087 0.122  -0.145 501 ASN CCC CB  
3917  C CG  . ASN C 172 ? 0.823 0.605 0.728 -0.076 0.135  -0.146 501 ASN CCC CG  
3918  O OD1 . ASN C 172 ? 0.848 0.622 0.762 -0.074 0.155  -0.160 501 ASN CCC OD1 
3919  N ND2 . ASN C 172 ? 0.800 0.603 0.720 -0.071 0.125  -0.132 501 ASN CCC ND2 
3920  N N   . GLY C 173 ? 0.833 0.568 0.628 -0.125 0.118  -0.168 502 GLY CCC N   
3921  C CA  . GLY C 173 ? 0.851 0.585 0.617 -0.138 0.099  -0.162 502 GLY CCC CA  
3922  C C   . GLY C 173 ? 0.833 0.585 0.615 -0.131 0.079  -0.141 502 GLY CCC C   
3923  O O   . GLY C 173 ? 0.813 0.580 0.616 -0.120 0.080  -0.131 502 GLY CCC O   
3924  N N   . VAL C 174 ? 0.847 0.599 0.620 -0.138 0.062  -0.134 503 VAL CCC N   
3925  C CA  . VAL C 174 ? 0.823 0.590 0.615 -0.130 0.044  -0.116 503 VAL CCC CA  
3926  C C   . VAL C 174 ? 0.816 0.600 0.604 -0.128 0.039  -0.104 503 VAL CCC C   
3927  O O   . VAL C 174 ? 0.773 0.570 0.585 -0.116 0.034  -0.092 503 VAL CCC O   
3928  C CB  . VAL C 174 ? 0.823 0.588 0.605 -0.139 0.028  -0.112 503 VAL CCC CB  
3929  C CG1 . VAL C 174 ? 0.814 0.595 0.615 -0.131 0.013  -0.094 503 VAL CCC CG1 
3930  C CG2 . VAL C 174 ? 0.832 0.578 0.621 -0.142 0.035  -0.123 503 VAL CCC CG2 
3931  N N   . GLY C 175 ? 0.823 0.608 0.581 -0.140 0.040  -0.108 504 GLY CCC N   
3932  C CA  . GLY C 175 ? 0.847 0.645 0.599 -0.140 0.036  -0.097 504 GLY CCC CA  
3933  C C   . GLY C 175 ? 0.850 0.656 0.626 -0.129 0.049  -0.097 504 GLY CCC C   
3934  O O   . GLY C 175 ? 0.869 0.687 0.652 -0.125 0.043  -0.086 504 GLY CCC O   
3935  N N   . TYR C 176 ? 0.858 0.656 0.647 -0.123 0.066  -0.109 505 TYR CCC N   
3936  C CA  . TYR C 176 ? 0.869 0.676 0.686 -0.112 0.079  -0.110 505 TYR CCC CA  
3937  C C   . TYR C 176 ? 0.833 0.644 0.686 -0.096 0.076  -0.105 505 TYR CCC C   
3938  O O   . TYR C 176 ? 0.832 0.652 0.713 -0.085 0.084  -0.105 505 TYR CCC O   
3939  C CB  . TYR C 176 ? 0.926 0.725 0.735 -0.116 0.102  -0.127 505 TYR CCC CB  
3940  C CG  . TYR C 176 ? 1.018 0.814 0.789 -0.132 0.108  -0.131 505 TYR CCC CG  
3941  C CD1 . TYR C 176 ? 1.070 0.853 0.802 -0.147 0.104  -0.138 505 TYR CCC CD1 
3942  C CD2 . TYR C 176 ? 1.065 0.873 0.838 -0.133 0.117  -0.128 505 TYR CCC CD2 
3943  C CE1 . TYR C 176 ? 1.129 0.909 0.822 -0.162 0.108  -0.140 505 TYR CCC CE1 
3944  C CE2 . TYR C 176 ? 1.111 0.915 0.846 -0.149 0.123  -0.130 505 TYR CCC CE2 
3945  C CZ  . TYR C 176 ? 1.145 0.935 0.839 -0.163 0.118  -0.136 505 TYR CCC CZ  
3946  O OH  . TYR C 176 ? 1.180 0.968 0.834 -0.178 0.124  -0.136 505 TYR CCC OH  
3947  N N   . GLN C 177 ? 0.799 0.605 0.654 -0.094 0.062  -0.099 506 GLN CCC N   
3948  C CA  . GLN C 177 ? 0.734 0.544 0.620 -0.079 0.058  -0.091 506 GLN CCC CA  
3949  C C   . GLN C 177 ? 0.694 0.522 0.590 -0.073 0.044  -0.077 506 GLN CCC C   
3950  O O   . GLN C 177 ? 0.708 0.542 0.588 -0.080 0.035  -0.071 506 GLN CCC O   
3951  C CB  . GLN C 177 ? 0.713 0.510 0.596 -0.081 0.051  -0.090 506 GLN CCC CB  
3952  C CG  . GLN C 177 ? 0.738 0.515 0.621 -0.082 0.065  -0.105 506 GLN CCC CG  
3953  C CD  . GLN C 177 ? 0.723 0.486 0.602 -0.088 0.059  -0.105 506 GLN CCC CD  
3954  O OE1 . GLN C 177 ? 0.709 0.477 0.594 -0.085 0.047  -0.093 506 GLN CCC OE1 
3955  N NE2 . GLN C 177 ? 0.739 0.484 0.606 -0.096 0.070  -0.121 506 GLN CCC NE2 
3956  N N   . PRO C 178 ? 0.654 0.490 0.578 -0.059 0.042  -0.070 507 PRO CCC N   
3957  C CA  . PRO C 178 ? 0.637 0.488 0.569 -0.053 0.030  -0.058 507 PRO CCC CA  
3958  C C   . PRO C 178 ? 0.635 0.486 0.558 -0.055 0.016  -0.050 507 PRO CCC C   
3959  O O   . PRO C 178 ? 0.632 0.471 0.553 -0.055 0.015  -0.050 507 PRO CCC O   
3960  C CB  . PRO C 178 ? 0.622 0.481 0.585 -0.038 0.031  -0.055 507 PRO CCC CB  
3961  C CG  . PRO C 178 ? 0.637 0.479 0.605 -0.035 0.039  -0.060 507 PRO CCC CG  
3962  C CD  . PRO C 178 ? 0.664 0.493 0.611 -0.048 0.050  -0.073 507 PRO CCC CD  
3963  N N   . TYR C 179 ? 0.615 0.476 0.531 -0.058 0.006  -0.043 508 TYR CCC N   
3964  C CA  . TYR C 179 ? 0.622 0.485 0.533 -0.058 -0.007 -0.034 508 TYR CCC CA  
3965  C C   . TYR C 179 ? 0.614 0.491 0.539 -0.049 -0.014 -0.027 508 TYR CCC C   
3966  O O   . TYR C 179 ? 0.610 0.495 0.539 -0.050 -0.013 -0.028 508 TYR CCC O   
3967  C CB  . TYR C 179 ? 0.629 0.490 0.520 -0.070 -0.013 -0.034 508 TYR CCC CB  
3968  C CG  . TYR C 179 ? 0.649 0.498 0.527 -0.078 -0.011 -0.039 508 TYR CCC CG  
3969  C CD1 . TYR C 179 ? 0.680 0.519 0.550 -0.084 0.001  -0.050 508 TYR CCC CD1 
3970  C CD2 . TYR C 179 ? 0.664 0.513 0.539 -0.082 -0.020 -0.034 508 TYR CCC CD2 
3971  C CE1 . TYR C 179 ? 0.685 0.511 0.541 -0.093 0.002  -0.057 508 TYR CCC CE1 
3972  C CE2 . TYR C 179 ? 0.683 0.522 0.548 -0.091 -0.020 -0.040 508 TYR CCC CE2 
3973  C CZ  . TYR C 179 ? 0.669 0.496 0.524 -0.097 -0.009 -0.052 508 TYR CCC CZ  
3974  O OH  . TYR C 179 ? 0.712 0.527 0.555 -0.107 -0.009 -0.059 508 TYR CCC OH  
3975  N N   . ARG C 180 ? 0.610 0.488 0.541 -0.042 -0.020 -0.021 509 ARG CCC N   
3976  C CA  . ARG C 180 ? 0.572 0.461 0.510 -0.035 -0.029 -0.015 509 ARG CCC CA  
3977  C C   . ARG C 180 ? 0.559 0.450 0.486 -0.041 -0.036 -0.011 509 ARG CCC C   
3978  O O   . ARG C 180 ? 0.536 0.422 0.456 -0.046 -0.038 -0.010 509 ARG CCC O   
3979  C CB  . ARG C 180 ? 0.587 0.477 0.533 -0.025 -0.031 -0.009 509 ARG CCC CB  
3980  C CG  . ARG C 180 ? 0.598 0.489 0.559 -0.017 -0.026 -0.011 509 ARG CCC CG  
3981  C CD  . ARG C 180 ? 0.610 0.500 0.577 -0.007 -0.029 -0.004 509 ARG CCC CD  
3982  N NE  . ARG C 180 ? 0.610 0.502 0.595 0.000  -0.025 -0.004 509 ARG CCC NE  
3983  C CZ  . ARG C 180 ? 0.601 0.495 0.595 0.011  -0.029 0.003  509 ARG CCC CZ  
3984  N NH1 . ARG C 180 ? 0.597 0.491 0.582 0.014  -0.036 0.011  509 ARG CCC NH1 
3985  N NH2 . ARG C 180 ? 0.607 0.504 0.620 0.018  -0.026 0.002  509 ARG CCC NH2 
3986  N N   . VAL C 181 ? 0.542 0.442 0.473 -0.039 -0.041 -0.010 510 VAL CCC N   
3987  C CA  . VAL C 181 ? 0.547 0.448 0.472 -0.043 -0.048 -0.007 510 VAL CCC CA  
3988  C C   . VAL C 181 ? 0.539 0.448 0.471 -0.035 -0.054 -0.004 510 VAL CCC C   
3989  O O   . VAL C 181 ? 0.511 0.425 0.451 -0.030 -0.054 -0.007 510 VAL CCC O   
3990  C CB  . VAL C 181 ? 0.563 0.463 0.482 -0.051 -0.047 -0.008 510 VAL CCC CB  
3991  C CG1 . VAL C 181 ? 0.573 0.472 0.487 -0.055 -0.055 -0.003 510 VAL CCC CG1 
3992  C CG2 . VAL C 181 ? 0.562 0.455 0.470 -0.059 -0.040 -0.012 510 VAL CCC CG2 
3993  N N   . VAL C 182 ? 0.539 0.447 0.468 -0.034 -0.058 -0.001 511 VAL CCC N   
3994  C CA  . VAL C 182 ? 0.502 0.415 0.435 -0.028 -0.063 -0.000 511 VAL CCC CA  
3995  C C   . VAL C 182 ? 0.517 0.428 0.449 -0.032 -0.067 0.002  511 VAL CCC C   
3996  O O   . VAL C 182 ? 0.495 0.404 0.425 -0.036 -0.068 0.005  511 VAL CCC O   
3997  C CB  . VAL C 182 ? 0.517 0.433 0.449 -0.022 -0.063 0.002  511 VAL CCC CB  
3998  C CG1 . VAL C 182 ? 0.525 0.444 0.457 -0.017 -0.066 0.001  511 VAL CCC CG1 
3999  C CG2 . VAL C 182 ? 0.528 0.444 0.461 -0.017 -0.060 0.003  511 VAL CCC CG2 
4000  N N   . VAL C 183 ? 0.505 0.417 0.441 -0.032 -0.070 -0.001 512 VAL CCC N   
4001  C CA  . VAL C 183 ? 0.537 0.446 0.475 -0.034 -0.074 0.002  512 VAL CCC CA  
4002  C C   . VAL C 183 ? 0.549 0.460 0.491 -0.027 -0.076 -0.002 512 VAL CCC C   
4003  O O   . VAL C 183 ? 0.574 0.488 0.518 -0.024 -0.076 -0.007 512 VAL CCC O   
4004  C CB  . VAL C 183 ? 0.559 0.464 0.497 -0.040 -0.075 0.001  512 VAL CCC CB  
4005  C CG1 . VAL C 183 ? 0.545 0.444 0.487 -0.042 -0.079 0.006  512 VAL CCC CG1 
4006  C CG2 . VAL C 183 ? 0.573 0.476 0.504 -0.048 -0.071 0.003  512 VAL CCC CG2 
4007  N N   . LEU C 184 ? 0.536 0.447 0.482 -0.024 -0.076 0.001  513 LEU CCC N   
4008  C CA  . LEU C 184 ? 0.536 0.448 0.485 -0.017 -0.076 -0.003 513 LEU CCC CA  
4009  C C   . LEU C 184 ? 0.536 0.442 0.494 -0.018 -0.079 -0.003 513 LEU CCC C   
4010  O O   . LEU C 184 ? 0.549 0.454 0.513 -0.019 -0.081 0.004  513 LEU CCC O   
4011  C CB  . LEU C 184 ? 0.542 0.459 0.492 -0.013 -0.072 0.000  513 LEU CCC CB  
4012  C CG  . LEU C 184 ? 0.546 0.467 0.488 -0.012 -0.068 0.001  513 LEU CCC CG  
4013  C CD1 . LEU C 184 ? 0.536 0.460 0.481 -0.009 -0.063 0.005  513 LEU CCC CD1 
4014  C CD2 . LEU C 184 ? 0.565 0.487 0.499 -0.008 -0.068 -0.004 513 LEU CCC CD2 
4015  N N   . SER C 185 ? 0.571 0.473 0.530 -0.017 -0.080 -0.009 514 SER CCC N   
4016  C CA  . SER C 185 ? 0.592 0.485 0.561 -0.016 -0.082 -0.011 514 SER CCC CA  
4017  C C   . SER C 185 ? 0.615 0.509 0.588 -0.008 -0.078 -0.017 514 SER CCC C   
4018  O O   . SER C 185 ? 0.633 0.530 0.597 -0.005 -0.076 -0.025 514 SER CCC O   
4019  C CB  . SER C 185 ? 0.600 0.488 0.569 -0.021 -0.083 -0.016 514 SER CCC CB  
4020  O OG  . SER C 185 ? 0.635 0.520 0.604 -0.028 -0.085 -0.010 514 SER CCC OG  
4021  N N   . PHE C 186 ? 0.611 0.499 0.596 -0.005 -0.078 -0.014 515 PHE CCC N   
4022  C CA  . PHE C 186 ? 0.611 0.499 0.604 0.003  -0.073 -0.021 515 PHE CCC CA  
4023  C C   . PHE C 186 ? 0.595 0.469 0.597 0.004  -0.073 -0.028 515 PHE CCC C   
4024  O O   . PHE C 186 ? 0.620 0.487 0.633 0.002  -0.077 -0.020 515 PHE CCC O   
4025  C CB  . PHE C 186 ? 0.608 0.502 0.615 0.008  -0.071 -0.013 515 PHE CCC CB  
4026  C CG  . PHE C 186 ? 0.591 0.496 0.590 0.005  -0.070 -0.007 515 PHE CCC CG  
4027  C CD1 . PHE C 186 ? 0.598 0.509 0.581 0.005  -0.066 -0.011 515 PHE CCC CD1 
4028  C CD2 . PHE C 186 ? 0.554 0.466 0.565 0.004  -0.073 0.003  515 PHE CCC CD2 
4029  C CE1 . PHE C 186 ? 0.577 0.496 0.555 0.002  -0.065 -0.005 515 PHE CCC CE1 
4030  C CE2 . PHE C 186 ? 0.554 0.475 0.560 0.001  -0.071 0.007  515 PHE CCC CE2 
4031  C CZ  . PHE C 186 ? 0.543 0.466 0.532 0.000  -0.067 0.003  515 PHE CCC CZ  
4032  N N   . GLU C 187 ? 0.626 0.496 0.620 0.006  -0.070 -0.041 516 GLU CCC N   
4033  C CA  . GLU C 187 ? 0.648 0.503 0.649 0.005  -0.071 -0.050 516 GLU CCC CA  
4034  C C   . GLU C 187 ? 0.651 0.501 0.661 0.014  -0.063 -0.060 516 GLU CCC C   
4035  O O   . GLU C 187 ? 0.637 0.494 0.637 0.018  -0.057 -0.066 516 GLU CCC O   
4036  C CB  . GLU C 187 ? 0.681 0.537 0.668 -0.001 -0.074 -0.061 516 GLU CCC CB  
4037  C CG  . GLU C 187 ? 0.705 0.547 0.701 -0.006 -0.077 -0.068 516 GLU CCC CG  
4038  C CD  . GLU C 187 ? 0.712 0.556 0.697 -0.012 -0.081 -0.080 516 GLU CCC CD  
4039  O OE1 . GLU C 187 ? 0.699 0.552 0.668 -0.009 -0.080 -0.089 516 GLU CCC OE1 
4040  O OE2 . GLU C 187 ? 0.800 0.639 0.792 -0.020 -0.085 -0.079 516 GLU CCC OE2 
4041  N N   . LEU C 188 ? 0.697 0.532 0.725 0.016  -0.063 -0.061 517 LEU CCC N   
4042  C CA  . LEU C 188 ? 0.716 0.540 0.754 0.024  -0.055 -0.073 517 LEU CCC CA  
4043  C C   . LEU C 188 ? 0.722 0.527 0.762 0.020  -0.057 -0.085 517 LEU CCC C   
4044  O O   . LEU C 188 ? 0.772 0.565 0.827 0.017  -0.062 -0.077 517 LEU CCC O   
4045  C CB  . LEU C 188 ? 0.743 0.566 0.807 0.032  -0.054 -0.062 517 LEU CCC CB  
4046  C CG  . LEU C 188 ? 0.761 0.602 0.827 0.037  -0.049 -0.056 517 LEU CCC CG  
4047  C CD1 . LEU C 188 ? 0.747 0.590 0.842 0.043  -0.051 -0.041 517 LEU CCC CD1 
4048  C CD2 . LEU C 188 ? 0.762 0.606 0.822 0.044  -0.036 -0.072 517 LEU CCC CD2 
4049  N N   . LEU C 189 ? 0.719 0.522 0.742 0.018  -0.054 -0.103 518 LEU CCC N   
4050  C CA  . LEU C 189 ? 0.744 0.529 0.770 0.014  -0.054 -0.119 518 LEU CCC CA  
4051  C C   . LEU C 189 ? 0.752 0.526 0.784 0.023  -0.043 -0.134 518 LEU CCC C   
4052  O O   . LEU C 189 ? 0.748 0.532 0.782 0.032  -0.035 -0.131 518 LEU CCC O   
4053  C CB  . LEU C 189 ? 0.763 0.555 0.766 0.005  -0.060 -0.131 518 LEU CCC CB  
4054  C CG  . LEU C 189 ? 0.751 0.556 0.749 -0.003 -0.069 -0.117 518 LEU CCC CG  
4055  C CD1 . LEU C 189 ? 0.782 0.597 0.760 -0.010 -0.075 -0.128 518 LEU CCC CD1 
4056  C CD2 . LEU C 189 ? 0.722 0.517 0.739 -0.009 -0.074 -0.105 518 LEU CCC CD2 
4057  N N   . HIS C 190 ? 0.759 0.513 0.796 0.021  -0.041 -0.150 519 HIS CCC N   
4058  C CA  . HIS C 190 ? 0.790 0.531 0.831 0.029  -0.028 -0.169 519 HIS CCC CA  
4059  C C   . HIS C 190 ? 0.825 0.575 0.832 0.026  -0.025 -0.187 519 HIS CCC C   
4060  O O   . HIS C 190 ? 0.871 0.607 0.867 0.019  -0.027 -0.207 519 HIS CCC O   
4061  C CB  . HIS C 190 ? 0.792 0.504 0.855 0.028  -0.027 -0.177 519 HIS CCC CB  
4062  C CG  . HIS C 190 ? 0.806 0.504 0.874 0.038  -0.013 -0.197 519 HIS CCC CG  
4063  N ND1 . HIS C 190 ? 0.810 0.516 0.891 0.051  -0.001 -0.193 519 HIS CCC ND1 
4064  C CD2 . HIS C 190 ? 0.822 0.500 0.885 0.035  -0.007 -0.222 519 HIS CCC CD2 
4065  C CE1 . HIS C 190 ? 0.825 0.515 0.910 0.058  0.013  -0.215 519 HIS CCC CE1 
4066  N NE2 . HIS C 190 ? 0.831 0.503 0.904 0.048  0.009  -0.233 519 HIS CCC NE2 
4067  N N   . ALA C 191 ? 0.809 0.579 0.799 0.030  -0.022 -0.181 520 ALA CCC N   
4068  C CA  . ALA C 191 ? 0.827 0.610 0.782 0.027  -0.021 -0.191 520 ALA CCC CA  
4069  C C   . ALA C 191 ? 0.829 0.627 0.779 0.036  -0.009 -0.185 520 ALA CCC C   
4070  O O   . ALA C 191 ? 0.790 0.594 0.764 0.042  -0.007 -0.169 520 ALA CCC O   
4071  C CB  . ALA C 191 ? 0.783 0.580 0.723 0.017  -0.036 -0.183 520 ALA CCC CB  
4072  N N   . PRO C 192 ? 0.838 0.644 0.758 0.037  -0.002 -0.197 521 PRO CCC N   
4073  C CA  . PRO C 192 ? 0.816 0.637 0.730 0.044  0.009  -0.188 521 PRO CCC CA  
4074  C C   . PRO C 192 ? 0.776 0.615 0.695 0.042  -0.000 -0.164 521 PRO CCC C   
4075  O O   . PRO C 192 ? 0.799 0.641 0.706 0.034  -0.014 -0.158 521 PRO CCC O   
4076  C CB  . PRO C 192 ? 0.858 0.682 0.730 0.041  0.014  -0.203 521 PRO CCC CB  
4077  C CG  . PRO C 192 ? 0.892 0.697 0.757 0.037  0.012  -0.226 521 PRO CCC CG  
4078  C CD  . PRO C 192 ? 0.860 0.658 0.749 0.031  -0.003 -0.219 521 PRO CCC CD  
4079  N N   . ALA C 193 ? 0.737 0.585 0.675 0.048  0.008  -0.151 522 ALA CCC N   
4080  C CA  . ALA C 193 ? 0.705 0.568 0.645 0.046  0.001  -0.130 522 ALA CCC CA  
4081  C C   . ALA C 193 ? 0.714 0.589 0.619 0.043  0.002  -0.130 522 ALA CCC C   
4082  O O   . ALA C 193 ? 0.784 0.659 0.671 0.046  0.014  -0.140 522 ALA CCC O   
4083  C CB  . ALA C 193 ? 0.684 0.556 0.653 0.053  0.010  -0.119 522 ALA CCC CB  
4084  N N   . THR C 194 ? 0.708 0.590 0.603 0.036  -0.011 -0.119 523 THR CCC N   
4085  C CA  . THR C 194 ? 0.705 0.595 0.565 0.034  -0.013 -0.118 523 THR CCC CA  
4086  C C   . THR C 194 ? 0.672 0.575 0.538 0.033  -0.014 -0.098 523 THR CCC C   
4087  O O   . THR C 194 ? 0.694 0.603 0.537 0.033  -0.012 -0.094 523 THR CCC O   
4088  C CB  . THR C 194 ? 0.709 0.596 0.553 0.027  -0.027 -0.126 523 THR CCC CB  
4089  O OG1 . THR C 194 ? 0.680 0.570 0.537 0.023  -0.040 -0.113 523 THR CCC OG1 
4090  C CG2 . THR C 194 ? 0.725 0.597 0.570 0.026  -0.028 -0.145 523 THR CCC CG2 
4091  N N   . VAL C 195 ? 0.644 0.548 0.538 0.034  -0.017 -0.087 524 VAL CCC N   
4092  C CA  . VAL C 195 ? 0.669 0.583 0.570 0.032  -0.017 -0.070 524 VAL CCC CA  
4093  C C   . VAL C 195 ? 0.674 0.592 0.601 0.037  -0.007 -0.066 524 VAL CCC C   
4094  O O   . VAL C 195 ? 0.678 0.592 0.629 0.038  -0.010 -0.065 524 VAL CCC O   
4095  C CB  . VAL C 195 ? 0.638 0.552 0.547 0.027  -0.031 -0.061 524 VAL CCC CB  
4096  C CG1 . VAL C 195 ? 0.626 0.548 0.541 0.025  -0.030 -0.046 524 VAL CCC CG1 
4097  C CG2 . VAL C 195 ? 0.653 0.566 0.542 0.023  -0.041 -0.066 524 VAL CCC CG2 
4098  N N   . CYS C 196 ? 0.674 0.600 0.595 0.039  0.005  -0.062 525 CYS CCC N   
4099  C CA  . CYS C 196 ? 0.681 0.616 0.629 0.043  0.016  -0.058 525 CYS CCC CA  
4100  C C   . CYS C 196 ? 0.659 0.604 0.606 0.040  0.018  -0.043 525 CYS CCC C   
4101  O O   . CYS C 196 ? 0.649 0.593 0.570 0.036  0.016  -0.040 525 CYS CCC O   
4102  C CB  . CYS C 196 ? 0.732 0.666 0.675 0.049  0.033  -0.070 525 CYS CCC CB  
4103  S SG  . CYS C 196 ? 0.778 0.697 0.734 0.054  0.033  -0.087 525 CYS CCC SG  
4104  N N   . GLY C 197 ? 0.646 0.601 0.624 0.040  0.022  -0.036 526 GLY CCC N   
4105  C CA  . GLY C 197 ? 0.674 0.639 0.657 0.036  0.026  -0.024 526 GLY CCC CA  
4106  C C   . GLY C 197 ? 0.687 0.657 0.657 0.039  0.045  -0.026 526 GLY CCC C   
4107  O O   . GLY C 197 ? 0.685 0.652 0.645 0.044  0.055  -0.038 526 GLY CCC O   
4108  N N   . PRO C 198 ? 0.735 0.713 0.704 0.034  0.050  -0.015 527 PRO CCC N   
4109  C CA  . PRO C 198 ? 0.807 0.790 0.763 0.035  0.070  -0.015 527 PRO CCC CA  
4110  C C   . PRO C 198 ? 0.905 0.898 0.887 0.041  0.086  -0.023 527 PRO CCC C   
4111  O O   . PRO C 198 ? 0.851 0.849 0.867 0.044  0.081  -0.023 527 PRO CCC O   
4112  C CB  . PRO C 198 ? 0.769 0.758 0.731 0.028  0.071  -0.001 527 PRO CCC CB  
4113  C CG  . PRO C 198 ? 0.746 0.729 0.711 0.024  0.051  0.005  527 PRO CCC CG  
4114  C CD  . PRO C 198 ? 0.730 0.709 0.709 0.027  0.039  -0.003 527 PRO CCC CD  
4124  N N   . GLN D 1   ? 0.634 0.871 1.172 -0.135 -0.254 0.266  1   GLN DDD N   
4125  C CA  . GLN D 1   ? 0.618 0.832 1.146 -0.097 -0.216 0.239  1   GLN DDD CA  
4126  C C   . GLN D 1   ? 0.618 0.770 1.020 -0.094 -0.214 0.205  1   GLN DDD C   
4127  O O   . GLN D 1   ? 0.603 0.720 0.937 -0.105 -0.207 0.188  1   GLN DDD O   
4128  C CB  . GLN D 1   ? 0.684 0.911 1.274 -0.080 -0.167 0.229  1   GLN DDD CB  
4129  C CG  . GLN D 1   ? 0.753 0.943 1.311 -0.049 -0.124 0.197  1   GLN DDD CG  
4130  C CD  . GLN D 1   ? 0.778 0.973 1.370 -0.024 -0.118 0.200  1   GLN DDD CD  
4131  O OE1 . GLN D 1   ? 0.817 1.047 1.475 -0.023 -0.142 0.230  1   GLN DDD OE1 
4132  N NE2 . GLN D 1   ? 0.791 0.946 1.332 -0.006 -0.086 0.171  1   GLN DDD NE2 
4133  N N   . VAL D 2   ? 0.563 0.703 0.938 -0.078 -0.217 0.196  2   VAL DDD N   
4134  C CA  . VAL D 2   ? 0.556 0.649 0.835 -0.067 -0.209 0.164  2   VAL DDD CA  
4135  C C   . VAL D 2   ? 0.518 0.607 0.808 -0.036 -0.175 0.143  2   VAL DDD C   
4136  O O   . VAL D 2   ? 0.499 0.610 0.846 -0.025 -0.168 0.153  2   VAL DDD O   
4137  C CB  . VAL D 2   ? 0.559 0.642 0.794 -0.078 -0.238 0.168  2   VAL DDD CB  
4138  C CG1 . VAL D 2   ? 0.567 0.615 0.722 -0.064 -0.225 0.136  2   VAL DDD CG1 
4139  C CG2 . VAL D 2   ? 0.601 0.678 0.809 -0.116 -0.273 0.189  2   VAL DDD CG2 
4140  N N   . GLN D 3   ? 0.509 0.565 0.739 -0.025 -0.157 0.116  3   GLN DDD N   
4141  C CA  . GLN D 3   ? 0.494 0.539 0.713 -0.004 -0.131 0.095  3   GLN DDD CA  
4142  C C   . GLN D 3   ? 0.499 0.533 0.659 0.004  -0.144 0.079  3   GLN DDD C   
4143  O O   . GLN D 3   ? 0.535 0.553 0.645 -0.003 -0.161 0.075  3   GLN DDD O   
4144  C CB  . GLN D 3   ? 0.499 0.517 0.696 -0.000 -0.105 0.081  3   GLN DDD CB  
4145  C CG  . GLN D 3   ? 0.498 0.532 0.768 -0.004 -0.078 0.093  3   GLN DDD CG  
4146  C CD  . GLN D 3   ? 0.523 0.521 0.760 -0.005 -0.046 0.075  3   GLN DDD CD  
4147  O OE1 . GLN D 3   ? 0.530 0.500 0.725 0.004  -0.030 0.056  3   GLN DDD OE1 
4148  N NE2 . GLN D 3   ? 0.539 0.534 0.789 -0.020 -0.036 0.081  3   GLN DDD NE2 
4149  N N   . LEU D 4   ? 0.473 0.515 0.640 0.015  -0.132 0.069  4   LEU DDD N   
4150  C CA  . LEU D 4   ? 0.483 0.526 0.611 0.021  -0.139 0.054  4   LEU DDD CA  
4151  C C   . LEU D 4   ? 0.487 0.523 0.597 0.033  -0.120 0.035  4   LEU DDD C   
4152  O O   . LEU D 4   ? 0.476 0.510 0.615 0.033  -0.100 0.037  4   LEU DDD O   
4153  C CB  . LEU D 4   ? 0.486 0.549 0.643 0.013  -0.149 0.067  4   LEU DDD CB  
4154  C CG  . LEU D 4   ? 0.502 0.570 0.675 -0.005 -0.174 0.091  4   LEU DDD CG  
4155  C CD1 . LEU D 4   ? 0.501 0.581 0.705 -0.013 -0.184 0.107  4   LEU DDD CD1 
4156  C CD2 . LEU D 4   ? 0.532 0.582 0.643 -0.016 -0.190 0.083  4   LEU DDD CD2 
4157  N N   . VAL D 5   ? 0.511 0.542 0.576 0.042  -0.127 0.018  5   VAL DDD N   
4158  C CA  . VAL D 5   ? 0.528 0.559 0.573 0.049  -0.118 0.003  5   VAL DDD CA  
4159  C C   . VAL D 5   ? 0.530 0.589 0.565 0.054  -0.128 -0.009 5   VAL DDD C   
4160  O O   . VAL D 5   ? 0.557 0.618 0.572 0.064  -0.140 -0.014 5   VAL DDD O   
4161  C CB  . VAL D 5   ? 0.569 0.568 0.576 0.055  -0.117 -0.003 5   VAL DDD CB  
4162  C CG1 . VAL D 5   ? 0.584 0.583 0.562 0.059  -0.119 -0.015 5   VAL DDD CG1 
4163  C CG2 . VAL D 5   ? 0.568 0.541 0.588 0.046  -0.098 0.005  5   VAL DDD CG2 
4164  N N   . GLU D 6   ? 0.523 0.599 0.568 0.046  -0.120 -0.013 6   GLU DDD N   
4165  C CA  . GLU D 6   ? 0.522 0.631 0.561 0.046  -0.126 -0.026 6   GLU DDD CA  
4166  C C   . GLU D 6   ? 0.547 0.663 0.564 0.054  -0.133 -0.036 6   GLU DDD C   
4167  O O   . GLU D 6   ? 0.583 0.671 0.582 0.051  -0.128 -0.034 6   GLU DDD O   
4168  C CB  . GLU D 6   ? 0.529 0.646 0.580 0.029  -0.115 -0.026 6   GLU DDD CB  
4169  C CG  . GLU D 6   ? 0.515 0.619 0.589 0.021  -0.112 -0.010 6   GLU DDD CG  
4170  C CD  . GLU D 6   ? 0.515 0.591 0.614 0.021  -0.097 0.004  6   GLU DDD CD  
4171  O OE1 . GLU D 6   ? 0.540 0.598 0.630 0.026  -0.087 0.000  6   GLU DDD OE1 
4172  O OE2 . GLU D 6   ? 0.539 0.610 0.666 0.016  -0.095 0.018  6   GLU DDD OE2 
4173  N N   . SER D 7   ? 0.562 0.714 0.583 0.063  -0.144 -0.045 7   SER DDD N   
4174  C CA  . SER D 7   ? 0.572 0.750 0.587 0.070  -0.157 -0.051 7   SER DDD CA  
4175  C C   . SER D 7   ? 0.580 0.817 0.622 0.069  -0.160 -0.061 7   SER DDD C   
4176  O O   . SER D 7   ? 0.540 0.786 0.595 0.063  -0.149 -0.065 7   SER DDD O   
4177  C CB  . SER D 7   ? 0.576 0.735 0.576 0.094  -0.171 -0.048 7   SER DDD CB  
4178  O OG  . SER D 7   ? 0.571 0.736 0.582 0.112  -0.170 -0.051 7   SER DDD OG  
4179  N N   . GLY D 8   ? 0.600 0.875 0.649 0.069  -0.174 -0.065 8   GLY DDD N   
4180  C CA  . GLY D 8   ? 0.601 0.945 0.687 0.068  -0.176 -0.075 8   GLY DDD CA  
4181  C C   . GLY D 8   ? 0.617 0.981 0.700 0.033  -0.168 -0.080 8   GLY DDD C   
4182  O O   . GLY D 8   ? 0.642 1.065 0.754 0.025  -0.166 -0.089 8   GLY DDD O   
4183  N N   . GLY D 9   ? 0.623 0.938 0.670 0.011  -0.160 -0.076 9   GLY DDD N   
4184  C CA  . GLY D 9   ? 0.642 0.958 0.671 -0.024 -0.148 -0.081 9   GLY DDD CA  
4185  C C   . GLY D 9   ? 0.650 0.999 0.669 -0.044 -0.166 -0.083 9   GLY DDD C   
4186  O O   . GLY D 9   ? 0.679 1.056 0.713 -0.025 -0.190 -0.078 9   GLY DDD O   
4187  N N   . GLY D 10  ? 0.659 1.001 0.650 -0.081 -0.156 -0.088 10  GLY DDD N   
4188  C CA  . GLY D 10  ? 0.684 1.043 0.648 -0.111 -0.174 -0.088 10  GLY DDD CA  
4189  C C   . GLY D 10  ? 0.693 1.101 0.663 -0.146 -0.172 -0.097 10  GLY DDD C   
4190  O O   . GLY D 10  ? 0.634 1.039 0.611 -0.153 -0.149 -0.105 10  GLY DDD O   
4191  N N   . LEU D 11  ? 0.741 1.192 0.705 -0.171 -0.197 -0.095 11  LEU DDD N   
4192  C CA  . LEU D 11  ? 0.779 1.282 0.743 -0.216 -0.200 -0.103 11  LEU DDD CA  
4193  C C   . LEU D 11  ? 0.748 1.357 0.798 -0.197 -0.209 -0.107 11  LEU DDD C   
4194  O O   . LEU D 11  ? 0.733 1.385 0.835 -0.157 -0.230 -0.099 11  LEU DDD O   
4195  C CB  . LEU D 11  ? 0.835 1.336 0.754 -0.252 -0.229 -0.095 11  LEU DDD CB  
4196  C CG  . LEU D 11  ? 0.877 1.426 0.782 -0.308 -0.237 -0.100 11  LEU DDD CG  
4197  C CD1 . LEU D 11  ? 0.900 1.396 0.759 -0.340 -0.196 -0.115 11  LEU DDD CD1 
4198  C CD2 . LEU D 11  ? 0.952 1.476 0.791 -0.350 -0.267 -0.090 11  LEU DDD CD2 
4199  N N   . VAL D 12  ? 0.768 1.411 0.830 -0.224 -0.191 -0.120 12  VAL DDD N   
4200  C CA  . VAL D 12  ? 0.730 1.479 0.875 -0.214 -0.192 -0.128 12  VAL DDD CA  
4201  C C   . VAL D 12  ? 0.739 1.520 0.869 -0.269 -0.179 -0.140 12  VAL DDD C   
4202  O O   . VAL D 12  ? 0.738 1.439 0.793 -0.302 -0.158 -0.146 12  VAL DDD O   
4203  C CB  . VAL D 12  ? 0.692 1.430 0.871 -0.170 -0.169 -0.134 12  VAL DDD CB  
4204  C CG1 . VAL D 12  ? 0.690 1.362 0.819 -0.190 -0.136 -0.143 12  VAL DDD CG1 
4205  C CG2 . VAL D 12  ? 0.672 1.511 0.940 -0.148 -0.169 -0.140 12  VAL DDD CG2 
4206  N N   . GLN D 13  ? 0.731 1.624 0.931 -0.281 -0.191 -0.144 13  GLN DDD N   
4207  C CA  . GLN D 13  ? 0.744 1.683 0.938 -0.338 -0.178 -0.157 13  GLN DDD CA  
4208  C C   . GLN D 13  ? 0.695 1.620 0.894 -0.335 -0.137 -0.175 13  GLN DDD C   
4209  O O   . GLN D 13  ? 0.656 1.593 0.904 -0.287 -0.126 -0.178 13  GLN DDD O   
4210  C CB  . GLN D 13  ? 0.764 1.835 1.041 -0.352 -0.207 -0.153 13  GLN DDD CB  
4211  C CG  . GLN D 13  ? 0.842 1.915 1.093 -0.371 -0.254 -0.133 13  GLN DDD CG  
4212  C CD  . GLN D 13  ? 0.919 1.976 1.095 -0.449 -0.259 -0.135 13  GLN DDD CD  
4213  O OE1 . GLN D 13  ? 0.995 1.944 1.070 -0.479 -0.232 -0.145 13  GLN DDD OE1 
4214  N NE2 . GLN D 13  ? 0.951 2.111 1.174 -0.481 -0.296 -0.125 13  GLN DDD NE2 
4215  N N   . ALA D 14  ? 0.701 1.589 0.839 -0.387 -0.114 -0.187 14  ALA DDD N   
4216  C CA  . ALA D 14  ? 0.686 1.559 0.812 -0.401 -0.077 -0.204 14  ALA DDD CA  
4217  C C   . ALA D 14  ? 0.661 1.642 0.886 -0.380 -0.067 -0.215 14  ALA DDD C   
4218  O O   . ALA D 14  ? 0.649 1.738 0.950 -0.382 -0.087 -0.212 14  ALA DDD O   
4219  C CB  . ALA D 14  ? 0.731 1.576 0.788 -0.469 -0.063 -0.214 14  ALA DDD CB  
4220  N N   . GLY D 15  ? 0.652 1.604 0.880 -0.359 -0.038 -0.225 15  GLY DDD N   
4221  C CA  . GLY D 15  ? 0.620 1.655 0.935 -0.333 -0.018 -0.238 15  GLY DDD CA  
4222  C C   . GLY D 15  ? 0.583 1.636 0.958 -0.266 -0.036 -0.226 15  GLY DDD C   
4223  O O   . GLY D 15  ? 0.588 1.684 1.025 -0.237 -0.014 -0.236 15  GLY DDD O   
4224  N N   . GLY D 16  ? 0.582 1.595 0.936 -0.243 -0.070 -0.205 16  GLY DDD N   
4225  C CA  . GLY D 16  ? 0.564 1.582 0.963 -0.182 -0.089 -0.192 16  GLY DDD CA  
4226  C C   . GLY D 16  ? 0.591 1.516 0.947 -0.151 -0.071 -0.193 16  GLY DDD C   
4227  O O   . GLY D 16  ? 0.592 1.455 0.889 -0.177 -0.046 -0.202 16  GLY DDD O   
4228  N N   . SER D 17  ? 0.608 1.520 0.988 -0.100 -0.086 -0.181 17  SER DDD N   
4229  C CA  . SER D 17  ? 0.605 1.437 0.953 -0.067 -0.074 -0.179 17  SER DDD CA  
4230  C C   . SER D 17  ? 0.607 1.380 0.923 -0.042 -0.103 -0.159 17  SER DDD C   
4231  O O   . SER D 17  ? 0.593 1.400 0.930 -0.036 -0.133 -0.147 17  SER DDD O   
4232  C CB  . SER D 17  ? 0.612 1.480 1.018 -0.029 -0.053 -0.189 17  SER DDD CB  
4233  O OG  . SER D 17  ? 0.649 1.546 1.066 -0.056 -0.016 -0.210 17  SER DDD OG  
4234  N N   . LEU D 18  ? 0.628 1.316 0.893 -0.032 -0.095 -0.155 18  LEU DDD N   
4235  C CA  . LEU D 18  ? 0.622 1.246 0.857 -0.007 -0.114 -0.138 18  LEU DDD CA  
4236  C C   . LEU D 18  ? 0.614 1.180 0.826 0.012  -0.098 -0.139 18  LEU DDD C   
4237  O O   . LEU D 18  ? 0.618 1.159 0.804 -0.011 -0.078 -0.147 18  LEU DDD O   
4238  C CB  . LEU D 18  ? 0.646 1.214 0.824 -0.037 -0.120 -0.130 18  LEU DDD CB  
4239  C CG  . LEU D 18  ? 0.668 1.253 0.841 -0.051 -0.143 -0.122 18  LEU DDD CG  
4240  C CD1 . LEU D 18  ? 0.705 1.210 0.816 -0.071 -0.138 -0.115 18  LEU DDD CD1 
4241  C CD2 . LEU D 18  ? 0.673 1.277 0.872 -0.016 -0.169 -0.112 18  LEU DDD CD2 
4242  N N   . ARG D 19  ? 0.614 1.153 0.828 0.048  -0.109 -0.131 19  ARG DDD N   
4243  C CA  . ARG D 19  ? 0.629 1.099 0.806 0.060  -0.100 -0.127 19  ARG DDD CA  
4244  C C   . ARG D 19  ? 0.612 1.024 0.754 0.061  -0.118 -0.110 19  ARG DDD C   
4245  O O   . ARG D 19  ? 0.576 0.983 0.723 0.085  -0.135 -0.102 19  ARG DDD O   
4246  C CB  . ARG D 19  ? 0.666 1.141 0.866 0.096  -0.091 -0.133 19  ARG DDD CB  
4247  C CG  . ARG D 19  ? 0.731 1.139 0.886 0.093  -0.073 -0.136 19  ARG DDD CG  
4248  C CD  . ARG D 19  ? 0.807 1.201 0.969 0.127  -0.058 -0.143 19  ARG DDD CD  
4249  N NE  . ARG D 19  ? 0.828 1.206 0.994 0.160  -0.082 -0.130 19  ARG DDD NE  
4250  C CZ  . ARG D 19  ? 0.897 1.230 1.046 0.189  -0.076 -0.129 19  ARG DDD CZ  
4251  N NH1 . ARG D 19  ? 0.923 1.219 1.048 0.189  -0.046 -0.142 19  ARG DDD NH1 
4252  N NH2 . ARG D 19  ? 0.908 1.224 1.055 0.216  -0.100 -0.115 19  ARG DDD NH2 
4253  N N   . LEU D 20  ? 0.628 0.996 0.736 0.036  -0.114 -0.104 20  LEU DDD N   
4254  C CA  . LEU D 20  ? 0.627 0.938 0.710 0.037  -0.123 -0.088 20  LEU DDD CA  
4255  C C   . LEU D 20  ? 0.652 0.925 0.720 0.055  -0.123 -0.083 20  LEU DDD C   
4256  O O   . LEU D 20  ? 0.686 0.956 0.746 0.052  -0.111 -0.091 20  LEU DDD O   
4257  C CB  . LEU D 20  ? 0.626 0.908 0.690 0.008  -0.116 -0.081 20  LEU DDD CB  
4258  C CG  . LEU D 20  ? 0.633 0.936 0.697 -0.014 -0.112 -0.085 20  LEU DDD CG  
4259  C CD1 . LEU D 20  ? 0.672 0.930 0.717 -0.035 -0.106 -0.074 20  LEU DDD CD1 
4260  C CD2 . LEU D 20  ? 0.641 0.956 0.708 -0.008 -0.122 -0.085 20  LEU DDD CD2 
4261  N N   . ALA D 21  ? 0.630 0.870 0.687 0.069  -0.133 -0.073 21  ALA DDD N   
4262  C CA  . ALA D 21  ? 0.618 0.812 0.652 0.078  -0.135 -0.065 21  ALA DDD CA  
4263  C C   . ALA D 21  ? 0.603 0.760 0.627 0.067  -0.141 -0.049 21  ALA DDD C   
4264  O O   . ALA D 21  ? 0.611 0.771 0.644 0.064  -0.141 -0.045 21  ALA DDD O   
4265  C CB  . ALA D 21  ? 0.606 0.795 0.637 0.109  -0.140 -0.069 21  ALA DDD CB  
4266  N N   . CYS D 22  ? 0.604 0.726 0.612 0.060  -0.143 -0.039 22  CYS DDD N   
4267  C CA  . CYS D 22  ? 0.582 0.676 0.593 0.051  -0.148 -0.022 22  CYS DDD CA  
4268  C C   . CYS D 22  ? 0.597 0.655 0.581 0.053  -0.154 -0.016 22  CYS DDD C   
4269  O O   . CYS D 22  ? 0.582 0.626 0.543 0.042  -0.155 -0.017 22  CYS DDD O   
4270  C CB  . CYS D 22  ? 0.617 0.714 0.645 0.029  -0.149 -0.009 22  CYS DDD CB  
4271  S SG  . CYS D 22  ? 0.646 0.720 0.697 0.020  -0.156 0.016  22  CYS DDD SG  
4272  N N   . ILE D 23  ? 0.585 0.622 0.564 0.061  -0.156 -0.011 23  ILE DDD N   
4273  C CA  . ILE D 23  ? 0.615 0.612 0.561 0.060  -0.160 -0.005 23  ILE DDD CA  
4274  C C   . ILE D 23  ? 0.635 0.624 0.602 0.039  -0.164 0.014  23  ILE DDD C   
4275  O O   . ILE D 23  ? 0.653 0.658 0.655 0.039  -0.157 0.019  23  ILE DDD O   
4276  C CB  . ILE D 23  ? 0.598 0.573 0.517 0.084  -0.160 -0.014 23  ILE DDD CB  
4277  C CG1 . ILE D 23  ? 0.643 0.566 0.515 0.082  -0.162 -0.012 23  ILE DDD CG1 
4278  C CG2 . ILE D 23  ? 0.582 0.559 0.514 0.085  -0.157 -0.012 23  ILE DDD CG2 
4279  C CD1 . ILE D 23  ? 0.659 0.550 0.497 0.108  -0.164 -0.019 23  ILE DDD CD1 
4280  N N   . ALA D 24  ? 0.580 0.645 0.557 0.033  -0.097 -0.019 24  ALA DDD N   
4281  C CA  . ALA D 24  ? 0.580 0.638 0.564 0.017  -0.089 -0.016 24  ALA DDD CA  
4282  C C   . ALA D 24  ? 0.595 0.622 0.562 0.010  -0.092 -0.001 24  ALA DDD C   
4283  O O   . ALA D 24  ? 0.628 0.627 0.580 0.020  -0.102 0.005  24  ALA DDD O   
4284  C CB  . ALA D 24  ? 0.559 0.614 0.558 0.016  -0.090 -0.024 24  ALA DDD CB  
4285  N N   . SER D 25  ? 0.593 0.627 0.562 -0.007 -0.083 0.005  25  SER DDD N   
4286  C CA  . SER D 25  ? 0.615 0.623 0.575 -0.023 -0.082 0.020  25  SER DDD CA  
4287  C C   . SER D 25  ? 0.607 0.596 0.579 -0.029 -0.089 0.015  25  SER DDD C   
4288  O O   . SER D 25  ? 0.555 0.555 0.541 -0.020 -0.092 0.002  25  SER DDD O   
4289  C CB  . SER D 25  ? 0.606 0.640 0.572 -0.040 -0.067 0.025  25  SER DDD CB  
4290  O OG  . SER D 25  ? 0.566 0.628 0.564 -0.044 -0.060 0.014  25  SER DDD OG  
4291  N N   . GLY D 26  ? 0.648 0.609 0.613 -0.046 -0.091 0.025  26  GLY DDD N   
4292  C CA  . GLY D 26  ? 0.671 0.619 0.648 -0.059 -0.097 0.019  26  GLY DDD CA  
4293  C C   . GLY D 26  ? 0.732 0.629 0.688 -0.049 -0.110 0.014  26  GLY DDD C   
4294  O O   . GLY D 26  ? 0.729 0.611 0.670 -0.026 -0.114 0.013  26  GLY DDD O   
4295  N N   . ARG D 27  ? 0.821 0.695 0.778 -0.066 -0.117 0.010  27  ARG DDD N   
4296  C CA  . ARG D 27  ? 0.902 0.719 0.836 -0.060 -0.127 0.001  27  ARG DDD CA  
4297  C C   . ARG D 27  ? 0.831 0.661 0.772 -0.055 -0.133 -0.020 27  ARG DDD C   
4298  O O   . ARG D 27  ? 0.863 0.648 0.784 -0.053 -0.141 -0.031 27  ARG DDD O   
4299  C CB  . ARG D 27  ? 1.046 0.817 0.967 -0.088 -0.131 0.012  27  ARG DDD CB  
4300  C CG  . ARG D 27  ? 1.224 0.951 1.119 -0.083 -0.130 0.031  27  ARG DDD CG  
4301  C CD  . ARG D 27  ? 1.427 1.092 1.304 -0.111 -0.135 0.041  27  ARG DDD CD  
4302  N NE  . ARG D 27  ? 1.544 1.234 1.443 -0.147 -0.135 0.035  27  ARG DDD NE  
4303  C CZ  . ARG D 27  ? 1.614 1.328 1.527 -0.181 -0.127 0.051  27  ARG DDD CZ  
4304  N NH1 . ARG D 27  ? 1.636 1.345 1.536 -0.187 -0.117 0.075  27  ARG DDD NH1 
4305  N NH2 . ARG D 27  ? 1.640 1.384 1.579 -0.209 -0.130 0.043  27  ARG DDD NH2 
4306  N N   . THR D 28  ? 0.758 0.641 0.722 -0.053 -0.129 -0.024 28  THR DDD N   
4307  C CA  . THR D 28  ? 0.748 0.644 0.713 -0.050 -0.135 -0.040 28  THR DDD CA  
4308  C C   . THR D 28  ? 0.673 0.604 0.646 -0.028 -0.128 -0.044 28  THR DDD C   
4309  O O   . THR D 28  ? 0.651 0.613 0.637 -0.031 -0.129 -0.047 28  THR DDD O   
4310  C CB  . THR D 28  ? 0.734 0.655 0.718 -0.075 -0.142 -0.039 28  THR DDD CB  
4311  O OG1 . THR D 28  ? 0.738 0.704 0.752 -0.079 -0.133 -0.026 28  THR DDD OG1 
4312  C CG2 . THR D 28  ? 0.769 0.655 0.744 -0.100 -0.151 -0.040 28  THR DDD CG2 
4313  N N   . PHE D 29  ? 0.634 0.560 0.600 -0.009 -0.123 -0.043 29  PHE DDD N   
4314  C CA  . PHE D 29  ? 0.621 0.580 0.595 0.009  -0.117 -0.047 29  PHE DDD CA  
4315  C C   . PHE D 29  ? 0.629 0.594 0.596 0.013  -0.118 -0.062 29  PHE DDD C   
4316  O O   . PHE D 29  ? 0.600 0.598 0.579 0.015  -0.114 -0.062 29  PHE DDD O   
4317  C CB  . PHE D 29  ? 0.627 0.578 0.593 0.029  -0.115 -0.046 29  PHE DDD CB  
4318  C CG  . PHE D 29  ? 0.590 0.579 0.567 0.042  -0.109 -0.051 29  PHE DDD CG  
4319  C CD1 . PHE D 29  ? 0.572 0.592 0.563 0.036  -0.103 -0.045 29  PHE DDD CD1 
4320  C CD2 . PHE D 29  ? 0.608 0.602 0.582 0.059  -0.108 -0.063 29  PHE DDD CD2 
4321  C CE1 . PHE D 29  ? 0.561 0.613 0.561 0.043  -0.099 -0.050 29  PHE DDD CE1 
4322  C CE2 . PHE D 29  ? 0.581 0.615 0.568 0.066  -0.102 -0.067 29  PHE DDD CE2 
4323  C CZ  . PHE D 29  ? 0.561 0.622 0.561 0.057  -0.098 -0.060 29  PHE DDD CZ  
4324  N N   . HIS D 30  ? 0.657 0.589 0.604 0.015  -0.124 -0.073 30  HIS DDD N   
4325  C CA  . HIS D 30  ? 0.662 0.596 0.594 0.018  -0.124 -0.089 30  HIS DDD CA  
4326  C C   . HIS D 30  ? 0.630 0.590 0.569 -0.000 -0.130 -0.085 30  HIS DDD C   
4327  O O   . HIS D 30  ? 0.604 0.577 0.531 0.001  -0.129 -0.092 30  HIS DDD O   
4328  C CB  . HIS D 30  ? 0.710 0.595 0.616 0.022  -0.129 -0.104 30  HIS DDD CB  
4329  C CG  . HIS D 30  ? 0.750 0.607 0.649 -0.003 -0.141 -0.102 30  HIS DDD CG  
4330  N ND1 . HIS D 30  ? 0.777 0.609 0.682 -0.014 -0.144 -0.089 30  HIS DDD ND1 
4331  C CD2 . HIS D 30  ? 0.769 0.625 0.658 -0.022 -0.150 -0.110 30  HIS DDD CD2 
4332  C CE1 . HIS D 30  ? 0.801 0.618 0.703 -0.040 -0.153 -0.090 30  HIS DDD CE1 
4333  N NE2 . HIS D 30  ? 0.803 0.635 0.694 -0.045 -0.159 -0.104 30  HIS DDD NE2 
4334  N N   . SER D 31  ? 0.615 0.584 0.572 -0.017 -0.135 -0.072 31  SER DDD N   
4335  C CA  . SER D 31  ? 0.602 0.600 0.573 -0.030 -0.142 -0.066 31  SER DDD CA  
4336  C C   . SER D 31  ? 0.551 0.583 0.542 -0.022 -0.133 -0.056 31  SER DDD C   
4337  O O   . SER D 31  ? 0.537 0.591 0.540 -0.028 -0.139 -0.048 31  SER DDD O   
4338  C CB  . SER D 31  ? 0.613 0.614 0.602 -0.050 -0.150 -0.057 31  SER DDD CB  
4339  O OG  . SER D 31  ? 0.717 0.680 0.686 -0.063 -0.158 -0.066 31  SER DDD OG  
4340  N N   . TYR D 32  ? 0.516 0.551 0.511 -0.009 -0.122 -0.055 32  TYR DDD N   
4341  C CA  . TYR D 32  ? 0.486 0.547 0.500 -0.004 -0.114 -0.047 32  TYR DDD CA  
4342  C C   . TYR D 32  ? 0.484 0.553 0.487 0.004  -0.108 -0.052 32  TYR DDD C   
4343  O O   . TYR D 32  ? 0.524 0.587 0.514 0.013  -0.103 -0.061 32  TYR DDD O   
4344  C CB  . TYR D 32  ? 0.466 0.530 0.494 -0.001 -0.106 -0.043 32  TYR DDD CB  
4345  C CG  . TYR D 32  ? 0.473 0.541 0.516 -0.012 -0.108 -0.035 32  TYR DDD CG  
4346  C CD1 . TYR D 32  ? 0.499 0.547 0.534 -0.021 -0.112 -0.034 32  TYR DDD CD1 
4347  C CD2 . TYR D 32  ? 0.477 0.569 0.545 -0.014 -0.104 -0.029 32  TYR DDD CD2 
4348  C CE1 . TYR D 32  ? 0.499 0.556 0.552 -0.036 -0.113 -0.026 32  TYR DDD CE1 
4349  C CE2 . TYR D 32  ? 0.503 0.608 0.591 -0.024 -0.104 -0.023 32  TYR DDD CE2 
4350  C CZ  . TYR D 32  ? 0.497 0.589 0.579 -0.037 -0.108 -0.021 32  TYR DDD CZ  
4351  O OH  . TYR D 32  ? 0.495 0.606 0.600 -0.050 -0.106 -0.014 32  TYR DDD OH  
4352  N N   . VAL D 33  ? 0.481 0.563 0.490 0.001  -0.107 -0.045 33  VAL DDD N   
4353  C CA  . VAL D 33  ? 0.495 0.588 0.502 0.004  -0.098 -0.045 33  VAL DDD CA  
4354  C C   . VAL D 33  ? 0.498 0.597 0.521 0.007  -0.089 -0.045 33  VAL DDD C   
4355  O O   . VAL D 33  ? 0.505 0.605 0.545 0.006  -0.089 -0.040 33  VAL DDD O   
4356  C CB  . VAL D 33  ? 0.495 0.592 0.501 -0.001 -0.101 -0.033 33  VAL DDD CB  
4357  C CG1 . VAL D 33  ? 0.496 0.598 0.499 -0.003 -0.091 -0.031 33  VAL DDD CG1 
4358  C CG2 . VAL D 33  ? 0.540 0.633 0.522 -0.006 -0.112 -0.033 33  VAL DDD CG2 
4359  N N   . MET D 34  ? 0.520 0.629 0.541 0.012  -0.082 -0.053 34  MET DDD N   
4360  C CA  . MET D 34  ? 0.518 0.637 0.551 0.013  -0.076 -0.055 34  MET DDD CA  
4361  C C   . MET D 34  ? 0.507 0.637 0.543 0.005  -0.069 -0.055 34  MET DDD C   
4362  O O   . MET D 34  ? 0.481 0.619 0.509 0.002  -0.065 -0.056 34  MET DDD O   
4363  C CB  . MET D 34  ? 0.536 0.661 0.565 0.023  -0.077 -0.062 34  MET DDD CB  
4364  C CG  . MET D 34  ? 0.553 0.657 0.575 0.028  -0.085 -0.060 34  MET DDD CG  
4365  S SD  . MET D 34  ? 0.548 0.643 0.579 0.019  -0.086 -0.051 34  MET DDD SD  
4366  C CE  . MET D 34  ? 0.580 0.691 0.614 0.022  -0.080 -0.053 34  MET DDD CE  
4367  N N   . ALA D 35  ? 0.506 0.637 0.553 0.001  -0.065 -0.056 35  ALA DDD N   
4368  C CA  . ALA D 35  ? 0.521 0.654 0.571 -0.010 -0.058 -0.056 35  ALA DDD CA  
4369  C C   . ALA D 35  ? 0.525 0.667 0.582 -0.015 -0.055 -0.066 35  ALA DDD C   
4370  O O   . ALA D 35  ? 0.527 0.669 0.585 -0.009 -0.057 -0.069 35  ALA DDD O   
4371  C CB  . ALA D 35  ? 0.532 0.641 0.584 -0.013 -0.058 -0.046 35  ALA DDD CB  
4372  N N   . TRP D 36  ? 0.523 0.674 0.583 -0.028 -0.049 -0.070 36  TRP DDD N   
4373  C CA  . TRP D 36  ? 0.518 0.675 0.582 -0.039 -0.047 -0.081 36  TRP DDD CA  
4374  C C   . TRP D 36  ? 0.541 0.668 0.605 -0.053 -0.040 -0.079 36  TRP DDD C   
4375  O O   . TRP D 36  ? 0.531 0.649 0.592 -0.061 -0.037 -0.070 36  TRP DDD O   
4376  C CB  . TRP D 36  ? 0.505 0.703 0.576 -0.046 -0.048 -0.088 36  TRP DDD CB  
4377  C CG  . TRP D 36  ? 0.490 0.711 0.562 -0.028 -0.056 -0.090 36  TRP DDD CG  
4378  C CD1 . TRP D 36  ? 0.501 0.735 0.574 -0.014 -0.057 -0.086 36  TRP DDD CD1 
4379  C CD2 . TRP D 36  ? 0.472 0.701 0.540 -0.022 -0.063 -0.094 36  TRP DDD CD2 
4380  N NE1 . TRP D 36  ? 0.488 0.735 0.561 0.001  -0.066 -0.088 36  TRP DDD NE1 
4381  C CE2 . TRP D 36  ? 0.479 0.724 0.548 -0.004 -0.070 -0.091 36  TRP DDD CE2 
4382  C CE3 . TRP D 36  ? 0.492 0.717 0.555 -0.031 -0.064 -0.102 36  TRP DDD CE3 
4383  C CZ2 . TRP D 36  ? 0.497 0.751 0.560 0.006  -0.080 -0.090 36  TRP DDD CZ2 
4384  C CZ3 . TRP D 36  ? 0.509 0.748 0.563 -0.023 -0.072 -0.103 36  TRP DDD CZ3 
4385  C CH2 . TRP D 36  ? 0.509 0.761 0.563 -0.005 -0.081 -0.095 36  TRP DDD CH2 
4386  N N   . PHE D 37  ? 0.533 0.641 0.597 -0.055 -0.038 -0.088 37  PHE DDD N   
4387  C CA  . PHE D 37  ? 0.571 0.643 0.633 -0.068 -0.031 -0.092 37  PHE DDD CA  
4388  C C   . PHE D 37  ? 0.599 0.682 0.658 -0.083 -0.030 -0.112 37  PHE DDD C   
4389  O O   . PHE D 37  ? 0.590 0.704 0.646 -0.077 -0.036 -0.119 37  PHE DDD O   
4390  C CB  . PHE D 37  ? 0.581 0.617 0.645 -0.053 -0.029 -0.088 37  PHE DDD CB  
4391  C CG  . PHE D 37  ? 0.556 0.580 0.624 -0.042 -0.032 -0.068 37  PHE DDD CG  
4392  C CD1 . PHE D 37  ? 0.536 0.583 0.606 -0.030 -0.039 -0.060 37  PHE DDD CD1 
4393  C CD2 . PHE D 37  ? 0.571 0.556 0.638 -0.044 -0.030 -0.058 37  PHE DDD CD2 
4394  C CE1 . PHE D 37  ? 0.526 0.564 0.596 -0.022 -0.045 -0.043 37  PHE DDD CE1 
4395  C CE2 . PHE D 37  ? 0.570 0.546 0.638 -0.033 -0.037 -0.038 37  PHE DDD CE2 
4396  C CZ  . PHE D 37  ? 0.550 0.556 0.619 -0.023 -0.044 -0.031 37  PHE DDD CZ  
4397  N N   . ARG D 38  ? 0.628 0.682 0.683 -0.102 -0.025 -0.120 38  ARG DDD N   
4398  C CA  . ARG D 38  ? 0.651 0.710 0.699 -0.119 -0.025 -0.142 38  ARG DDD CA  
4399  C C   . ARG D 38  ? 0.703 0.703 0.743 -0.126 -0.017 -0.153 38  ARG DDD C   
4400  O O   . ARG D 38  ? 0.707 0.665 0.750 -0.123 -0.012 -0.140 38  ARG DDD O   
4401  C CB  . ARG D 38  ? 0.656 0.754 0.711 -0.144 -0.030 -0.146 38  ARG DDD CB  
4402  C CG  . ARG D 38  ? 0.692 0.763 0.749 -0.168 -0.023 -0.140 38  ARG DDD CG  
4403  C CD  . ARG D 38  ? 0.710 0.836 0.781 -0.190 -0.025 -0.140 38  ARG DDD CD  
4404  N NE  . ARG D 38  ? 0.746 0.849 0.817 -0.216 -0.017 -0.130 38  ARG DDD NE  
4405  C CZ  . ARG D 38  ? 0.748 0.894 0.833 -0.242 -0.014 -0.130 38  ARG DDD CZ  
4406  N NH1 . ARG D 38  ? 0.733 0.951 0.836 -0.244 -0.022 -0.140 38  ARG DDD NH1 
4407  N NH2 . ARG D 38  ? 0.791 0.910 0.872 -0.268 -0.005 -0.118 38  ARG DDD NH2 
4408  N N   . GLN D 39  ? 0.746 0.742 0.774 -0.135 -0.016 -0.177 39  GLN DDD N   
4409  C CA  . GLN D 39  ? 0.812 0.748 0.829 -0.140 -0.007 -0.194 39  GLN DDD CA  
4410  C C   . GLN D 39  ? 0.870 0.811 0.872 -0.170 -0.009 -0.221 39  GLN DDD C   
4411  O O   . GLN D 39  ? 0.848 0.827 0.839 -0.168 -0.014 -0.234 39  GLN DDD O   
4412  C CB  . GLN D 39  ? 0.807 0.727 0.822 -0.111 0.001  -0.198 39  GLN DDD CB  
4413  C CG  . GLN D 39  ? 0.881 0.738 0.887 -0.110 0.013  -0.218 39  GLN DDD CG  
4414  C CD  . GLN D 39  ? 0.896 0.742 0.910 -0.076 0.023  -0.218 39  GLN DDD CD  
4415  O OE1 . GLN D 39  ? 0.903 0.793 0.922 -0.061 0.022  -0.212 39  GLN DDD OE1 
4416  N NE2 . GLN D 39  ? 0.960 0.748 0.978 -0.065 0.032  -0.223 39  GLN DDD NE2 
4417  N N   . ALA D 40  ? 0.937 0.844 0.938 -0.198 -0.007 -0.225 40  ALA DDD N   
4418  C CA  . ALA D 40  ? 1.029 0.924 1.014 -0.231 -0.009 -0.254 40  ALA DDD CA  
4419  C C   . ALA D 40  ? 1.115 0.942 1.080 -0.222 0.002  -0.277 40  ALA DDD C   
4420  O O   . ALA D 40  ? 1.111 0.890 1.081 -0.196 0.012  -0.267 40  ALA DDD O   
4421  C CB  . ALA D 40  ? 1.058 0.940 1.051 -0.267 -0.010 -0.247 40  ALA DDD CB  
4422  N N   . PRO D 41  ? 1.210 1.033 1.151 -0.241 0.001  -0.311 41  PRO DDD N   
4423  C CA  . PRO D 41  ? 1.286 1.043 1.205 -0.233 0.014  -0.339 41  PRO DDD CA  
4424  C C   . PRO D 41  ? 1.351 1.020 1.273 -0.241 0.023  -0.337 41  PRO DDD C   
4425  O O   . PRO D 41  ? 1.351 1.007 1.276 -0.275 0.018  -0.331 41  PRO DDD O   
4426  C CB  . PRO D 41  ? 1.328 1.104 1.217 -0.261 0.008  -0.375 41  PRO DDD CB  
4427  C CG  . PRO D 41  ? 1.287 1.134 1.189 -0.292 -0.011 -0.364 41  PRO DDD CG  
4428  C CD  . PRO D 41  ? 1.204 1.090 1.138 -0.270 -0.014 -0.324 41  PRO DDD CD  
4429  N N   . GLY D 42  ? 1.372 0.983 1.295 -0.207 0.037  -0.338 42  GLY DDD N   
4430  C CA  . GLY D 42  ? 1.432 0.950 1.356 -0.206 0.045  -0.333 42  GLY DDD CA  
4431  C C   . GLY D 42  ? 1.408 0.925 1.357 -0.190 0.041  -0.288 42  GLY DDD C   
4432  O O   . GLY D 42  ? 1.448 0.887 1.399 -0.180 0.047  -0.278 42  GLY DDD O   
4433  N N   . LYS D 43  ? 1.334 0.928 1.300 -0.185 0.032  -0.262 43  LYS DDD N   
4434  C CA  . LYS D 43  ? 1.299 0.898 1.284 -0.172 0.028  -0.222 43  LYS DDD CA  
4435  C C   . LYS D 43  ? 1.229 0.867 1.232 -0.130 0.027  -0.207 43  LYS DDD C   
4436  O O   . LYS D 43  ? 1.223 0.900 1.224 -0.117 0.030  -0.225 43  LYS DDD O   
4437  C CB  . LYS D 43  ? 1.283 0.936 1.272 -0.204 0.018  -0.205 43  LYS DDD CB  
4438  C CG  . LYS D 43  ? 1.364 0.970 1.345 -0.244 0.020  -0.201 43  LYS DDD CG  
4439  C CD  . LYS D 43  ? 1.352 0.992 1.342 -0.261 0.016  -0.168 43  LYS DDD CD  
4440  C CE  . LYS D 43  ? 1.444 1.057 1.426 -0.312 0.019  -0.169 43  LYS DDD CE  
4441  N NZ  . LYS D 43  ? 1.417 1.118 1.413 -0.338 0.014  -0.163 43  LYS DDD NZ  
4442  N N   . GLU D 44  ? 1.177 0.808 1.193 -0.112 0.023  -0.173 44  GLU DDD N   
4443  C CA  . GLU D 44  ? 1.116 0.791 1.152 -0.078 0.020  -0.156 44  GLU DDD CA  
4444  C C   . GLU D 44  ? 1.013 0.764 1.051 -0.089 0.011  -0.145 44  GLU DDD C   
4445  O O   . GLU D 44  ? 1.005 0.772 1.035 -0.120 0.008  -0.148 44  GLU DDD O   
4446  C CB  . GLU D 44  ? 1.186 0.825 1.234 -0.056 0.016  -0.125 44  GLU DDD CB  
4447  C CG  . GLU D 44  ? 1.319 0.875 1.365 -0.042 0.024  -0.132 44  GLU DDD CG  
4448  C CD  . GLU D 44  ? 1.367 0.895 1.429 -0.011 0.017  -0.100 44  GLU DDD CD  
4449  O OE1 . GLU D 44  ? 1.320 0.880 1.384 -0.012 0.005  -0.069 44  GLU DDD OE1 
4450  O OE2 . GLU D 44  ? 1.442 0.915 1.513 0.015  0.023  -0.107 44  GLU DDD OE2 
4451  N N   . ARG D 45  ? 0.940 0.735 0.992 -0.065 0.007  -0.135 45  ARG DDD N   
4452  C CA  . ARG D 45  ? 0.901 0.756 0.956 -0.068 -0.002 -0.121 45  ARG DDD CA  
4453  C C   . ARG D 45  ? 0.891 0.740 0.944 -0.081 -0.007 -0.097 45  ARG DDD C   
4454  O O   . ARG D 45  ? 0.928 0.743 0.983 -0.069 -0.009 -0.077 45  ARG DDD O   
4455  C CB  . ARG D 45  ? 0.898 0.785 0.967 -0.040 -0.004 -0.112 45  ARG DDD CB  
4456  C CG  . ARG D 45  ? 0.909 0.831 0.974 -0.037 -0.001 -0.131 45  ARG DDD CG  
4457  C CD  . ARG D 45  ? 0.944 0.883 1.025 -0.011 0.001  -0.125 45  ARG DDD CD  
4458  N NE  . ARG D 45  ? 1.018 0.980 1.089 -0.011 0.008  -0.144 45  ARG DDD NE  
4459  C CZ  . ARG D 45  ? 1.021 1.013 1.101 0.003  0.010  -0.141 45  ARG DDD CZ  
4460  N NH1 . ARG D 45  ? 1.032 1.034 1.133 0.017  0.006  -0.122 45  ARG DDD NH1 
4461  N NH2 . ARG D 45  ? 1.021 1.032 1.086 -0.000 0.017  -0.156 45  ARG DDD NH2 
4462  N N   . GLU D 46  ? 0.841 0.725 0.888 -0.105 -0.009 -0.098 46  GLU DDD N   
4463  C CA  . GLU D 46  ? 0.812 0.704 0.855 -0.122 -0.011 -0.078 46  GLU DDD CA  
4464  C C   . GLU D 46  ? 0.717 0.667 0.765 -0.111 -0.016 -0.070 46  GLU DDD C   
4465  O O   . GLU D 46  ? 0.643 0.635 0.696 -0.107 -0.019 -0.084 46  GLU DDD O   
4466  C CB  . GLU D 46  ? 0.871 0.760 0.909 -0.158 -0.006 -0.091 46  GLU DDD CB  
4467  C CG  . GLU D 46  ? 0.921 0.835 0.957 -0.183 -0.004 -0.076 46  GLU DDD CG  
4468  C CD  . GLU D 46  ? 0.985 0.906 1.022 -0.222 0.000  -0.090 46  GLU DDD CD  
4469  O OE1 . GLU D 46  ? 1.031 0.937 1.066 -0.231 -0.000 -0.114 46  GLU DDD OE1 
4470  O OE2 . GLU D 46  ? 1.001 0.949 1.040 -0.246 0.005  -0.079 46  GLU DDD OE2 
4471  N N   . PHE D 47  ? 0.684 0.634 0.728 -0.104 -0.019 -0.047 47  PHE DDD N   
4472  C CA  . PHE D 47  ? 0.626 0.624 0.669 -0.095 -0.024 -0.041 47  PHE DDD CA  
4473  C C   . PHE D 47  ? 0.591 0.632 0.636 -0.116 -0.019 -0.049 47  PHE DDD C   
4474  O O   . PHE D 47  ? 0.603 0.635 0.644 -0.141 -0.013 -0.045 47  PHE DDD O   
4475  C CB  . PHE D 47  ? 0.647 0.631 0.678 -0.089 -0.028 -0.017 47  PHE DDD CB  
4476  C CG  . PHE D 47  ? 0.636 0.664 0.662 -0.083 -0.031 -0.014 47  PHE DDD CG  
4477  C CD1 . PHE D 47  ? 0.603 0.648 0.635 -0.062 -0.038 -0.018 47  PHE DDD CD1 
4478  C CD2 . PHE D 47  ? 0.657 0.708 0.672 -0.100 -0.024 -0.009 47  PHE DDD CD2 
4479  C CE1 . PHE D 47  ? 0.591 0.667 0.615 -0.057 -0.041 -0.019 47  PHE DDD CE1 
4480  C CE2 . PHE D 47  ? 0.636 0.724 0.644 -0.093 -0.024 -0.011 47  PHE DDD CE2 
4481  C CZ  . PHE D 47  ? 0.626 0.722 0.638 -0.071 -0.034 -0.016 47  PHE DDD CZ  
4482  N N   . VAL D 48  ? 0.541 0.629 0.594 -0.105 -0.023 -0.059 48  VAL DDD N   
4483  C CA  . VAL D 48  ? 0.555 0.695 0.617 -0.118 -0.020 -0.067 48  VAL DDD CA  
4484  C C   . VAL D 48  ? 0.535 0.705 0.593 -0.106 -0.019 -0.059 48  VAL DDD C   
4485  O O   . VAL D 48  ? 0.564 0.757 0.620 -0.121 -0.010 -0.055 48  VAL DDD O   
4486  C CB  . VAL D 48  ? 0.536 0.707 0.610 -0.114 -0.026 -0.085 48  VAL DDD CB  
4487  C CG1 . VAL D 48  ? 0.519 0.750 0.608 -0.120 -0.025 -0.092 48  VAL DDD CG1 
4488  C CG2 . VAL D 48  ? 0.555 0.696 0.627 -0.129 -0.025 -0.097 48  VAL DDD CG2 
4489  N N   . ALA D 49  ? 0.528 0.696 0.582 -0.081 -0.026 -0.059 49  ALA DDD N   
4490  C CA  . ALA D 49  ? 0.532 0.724 0.580 -0.068 -0.027 -0.057 49  ALA DDD CA  
4491  C C   . ALA D 49  ? 0.529 0.700 0.570 -0.048 -0.036 -0.053 49  ALA DDD C   
4492  O O   . ALA D 49  ? 0.504 0.657 0.550 -0.040 -0.042 -0.056 49  ALA DDD O   
4493  C CB  . ALA D 49  ? 0.512 0.753 0.575 -0.064 -0.025 -0.070 49  ALA DDD CB  
4494  N N   . ALA D 50  ? 0.537 0.711 0.563 -0.041 -0.037 -0.049 50  ALA DDD N   
4495  C CA  . ALA D 50  ? 0.551 0.708 0.568 -0.025 -0.047 -0.048 50  ALA DDD CA  
4496  C C   . ALA D 50  ? 0.572 0.745 0.575 -0.017 -0.045 -0.055 50  ALA DDD C   
4497  O O   . ALA D 50  ? 0.621 0.815 0.616 -0.024 -0.035 -0.056 50  ALA DDD O   
4498  C CB  . ALA D 50  ? 0.554 0.681 0.563 -0.028 -0.053 -0.033 50  ALA DDD CB  
4499  N N   . ILE D 51  ? 0.562 0.725 0.562 -0.003 -0.054 -0.060 51  ILE DDD N   
4500  C CA  . ILE D 51  ? 0.563 0.731 0.548 0.007  -0.053 -0.070 51  ILE DDD CA  
4501  C C   . ILE D 51  ? 0.560 0.698 0.529 0.010  -0.066 -0.068 51  ILE DDD C   
4502  O O   . ILE D 51  ? 0.567 0.691 0.549 0.012  -0.074 -0.064 51  ILE DDD O   
4503  C CB  . ILE D 51  ? 0.570 0.756 0.569 0.022  -0.051 -0.083 51  ILE DDD CB  
4504  C CG1 . ILE D 51  ? 0.604 0.794 0.590 0.037  -0.047 -0.097 51  ILE DDD CG1 
4505  C CG2 . ILE D 51  ? 0.562 0.731 0.573 0.029  -0.061 -0.080 51  ILE DDD CG2 
4506  C CD1 . ILE D 51  ? 0.607 0.823 0.612 0.055  -0.043 -0.108 51  ILE DDD CD1 
4507  N N   . SER D 52  ? 0.592 0.727 0.536 0.007  -0.067 -0.070 52  SER DDD N   
4508  C CA  . SER D 52  ? 0.613 0.726 0.540 0.006  -0.080 -0.071 52  SER DDD CA  
4509  C C   . SER D 52  ? 0.624 0.720 0.549 0.017  -0.083 -0.086 52  SER DDD C   
4510  O O   . SER D 52  ? 0.648 0.752 0.584 0.030  -0.075 -0.095 52  SER DDD O   
4511  C CB  . SER D 52  ? 0.649 0.763 0.541 -0.002 -0.080 -0.072 52  SER DDD CB  
4512  O OG  . SER D 52  ? 0.666 0.764 0.546 -0.008 -0.097 -0.067 52  SER DDD OG  
4513  N N   . TRP D 53  ? 0.647 0.721 0.560 0.013  -0.096 -0.088 53  TRP DDD N   
4514  C CA  . TRP D 53  ? 0.650 0.695 0.559 0.019  -0.102 -0.099 53  TRP DDD CA  
4515  C C   . TRP D 53  ? 0.687 0.727 0.580 0.035  -0.092 -0.119 53  TRP DDD C   
4516  O O   . TRP D 53  ? 0.702 0.732 0.607 0.049  -0.090 -0.123 53  TRP DDD O   
4517  C CB  . TRP D 53  ? 0.638 0.665 0.532 0.004  -0.118 -0.100 53  TRP DDD CB  
4518  C CG  . TRP D 53  ? 0.601 0.643 0.514 -0.009 -0.128 -0.081 53  TRP DDD CG  
4519  C CD1 . TRP D 53  ? 0.577 0.623 0.520 -0.011 -0.130 -0.069 53  TRP DDD CD1 
4520  C CD2 . TRP D 53  ? 0.596 0.654 0.498 -0.018 -0.135 -0.071 53  TRP DDD CD2 
4521  N NE1 . TRP D 53  ? 0.561 0.625 0.518 -0.019 -0.138 -0.055 53  TRP DDD NE1 
4522  C CE2 . TRP D 53  ? 0.587 0.657 0.520 -0.023 -0.143 -0.054 53  TRP DDD CE2 
4523  C CE3 . TRP D 53  ? 0.630 0.692 0.498 -0.022 -0.136 -0.074 53  TRP DDD CE3 
4524  C CZ2 . TRP D 53  ? 0.601 0.687 0.535 -0.028 -0.154 -0.039 53  TRP DDD CZ2 
4525  C CZ3 . TRP D 53  ? 0.646 0.723 0.510 -0.031 -0.148 -0.058 53  TRP DDD CZ3 
4526  C CH2 . TRP D 53  ? 0.632 0.719 0.530 -0.032 -0.158 -0.040 53  TRP DDD CH2 
4527  N N   . SER D 54  ? 0.707 0.755 0.573 0.034  -0.086 -0.130 54  SER DDD N   
4528  C CA  . SER D 54  ? 0.749 0.796 0.598 0.051  -0.074 -0.153 54  SER DDD CA  
4529  C C   . SER D 54  ? 0.750 0.836 0.624 0.065  -0.057 -0.153 54  SER DDD C   
4530  O O   . SER D 54  ? 0.763 0.856 0.630 0.083  -0.045 -0.172 54  SER DDD O   
4531  C CB  . SER D 54  ? 0.754 0.805 0.564 0.042  -0.070 -0.164 54  SER DDD CB  
4532  O OG  . SER D 54  ? 0.740 0.829 0.551 0.032  -0.061 -0.150 54  SER DDD OG  
4533  N N   . SER D 55  ? 0.715 0.825 0.614 0.057  -0.057 -0.135 55  SER DDD N   
4534  C CA  . SER D 55  ? 0.712 0.867 0.635 0.061  -0.042 -0.133 55  SER DDD CA  
4535  C C   . SER D 55  ? 0.739 0.923 0.647 0.047  -0.029 -0.131 55  SER DDD C   
4536  O O   . SER D 55  ? 0.690 0.913 0.618 0.045  -0.016 -0.129 55  SER DDD O   
4537  C CB  . SER D 55  ? 0.712 0.881 0.651 0.087  -0.035 -0.148 55  SER DDD CB  
4538  O OG  . SER D 55  ? 0.715 0.856 0.667 0.100  -0.048 -0.146 55  SER DDD OG  
4539  N N   . THR D 56  ? 0.820 0.988 0.691 0.036  -0.032 -0.131 56  THR DDD N   
4540  C CA  . THR D 56  ? 0.935 1.129 0.780 0.029  -0.015 -0.137 56  THR DDD CA  
4541  C C   . THR D 56  ? 0.949 1.159 0.787 0.006  -0.011 -0.114 56  THR DDD C   
4542  O O   . THR D 56  ? 1.101 1.345 0.930 -0.001 0.008  -0.116 56  THR DDD O   
4543  C CB  . THR D 56  ? 1.067 1.239 0.866 0.030  -0.017 -0.153 56  THR DDD CB  
4544  O OG1 . THR D 56  ? 1.202 1.375 1.005 0.054  -0.007 -0.179 56  THR DDD OG1 
4545  C CG2 . THR D 56  ? 1.104 1.296 0.863 0.013  -0.006 -0.149 56  THR DDD CG2 
4546  N N   . PRO D 57  ? 0.811 0.998 0.650 -0.007 -0.027 -0.093 57  PRO DDD N   
4547  C CA  . PRO D 57  ? 0.740 0.937 0.590 -0.024 -0.024 -0.071 57  PRO DDD CA  
4548  C C   . PRO D 57  ? 0.693 0.895 0.587 -0.018 -0.024 -0.071 57  PRO DDD C   
4549  O O   . PRO D 57  ? 0.665 0.847 0.575 -0.008 -0.037 -0.072 57  PRO DDD O   
4550  C CB  . PRO D 57  ? 0.748 0.916 0.576 -0.034 -0.041 -0.051 57  PRO DDD CB  
4551  C CG  . PRO D 57  ? 0.784 0.934 0.597 -0.025 -0.056 -0.064 57  PRO DDD CG  
4552  C CD  . PRO D 57  ? 0.770 0.924 0.596 -0.008 -0.049 -0.090 57  PRO DDD CD  
4553  N N   . THR D 58  ? 0.669 0.903 0.582 -0.025 -0.009 -0.071 58  THR DDD N   
4554  C CA  . THR D 58  ? 0.604 0.845 0.553 -0.028 -0.010 -0.067 58  THR DDD CA  
4555  C C   . THR D 58  ? 0.606 0.839 0.551 -0.053 -0.005 -0.047 58  THR DDD C   
4556  O O   . THR D 58  ? 0.597 0.834 0.515 -0.066 0.003  -0.039 58  THR DDD O   
4557  C CB  . THR D 58  ? 0.581 0.865 0.559 -0.020 0.001  -0.082 58  THR DDD CB  
4558  O OG1 . THR D 58  ? 0.612 0.936 0.585 -0.030 0.020  -0.085 58  THR DDD OG1 
4559  C CG2 . THR D 58  ? 0.563 0.846 0.548 0.007  -0.006 -0.098 58  THR DDD CG2 
4560  N N   . TYR D 59  ? 0.593 0.809 0.558 -0.058 -0.012 -0.041 59  TYR DDD N   
4561  C CA  . TYR D 59  ? 0.608 0.803 0.571 -0.079 -0.009 -0.023 59  TYR DDD CA  
4562  C C   . TYR D 59  ? 0.576 0.783 0.568 -0.089 -0.005 -0.030 59  TYR DDD C   
4563  O O   . TYR D 59  ? 0.547 0.763 0.559 -0.075 -0.012 -0.043 59  TYR DDD O   
4564  C CB  . TYR D 59  ? 0.632 0.781 0.586 -0.074 -0.024 -0.008 59  TYR DDD CB  
4565  C CG  . TYR D 59  ? 0.648 0.786 0.576 -0.065 -0.035 -0.001 59  TYR DDD CG  
4566  C CD1 . TYR D 59  ? 0.604 0.740 0.536 -0.047 -0.046 -0.012 59  TYR DDD CD1 
4567  C CD2 . TYR D 59  ? 0.676 0.801 0.572 -0.076 -0.035 0.018  59  TYR DDD CD2 
4568  C CE1 . TYR D 59  ? 0.624 0.749 0.534 -0.043 -0.058 -0.007 59  TYR DDD CE1 
4569  C CE2 . TYR D 59  ? 0.680 0.795 0.550 -0.069 -0.049 0.024  59  TYR DDD CE2 
4570  C CZ  . TYR D 59  ? 0.658 0.776 0.537 -0.053 -0.061 0.010  59  TYR DDD CZ  
4571  O OH  . TYR D 59  ? 0.674 0.786 0.528 -0.050 -0.075 0.014  59  TYR DDD OH  
4572  N N   . TYR D 60  ? 0.592 0.796 0.583 -0.114 0.005  -0.021 60  TYR DDD N   
4573  C CA  . TYR D 60  ? 0.579 0.796 0.595 -0.131 0.009  -0.029 60  TYR DDD CA  
4574  C C   . TYR D 60  ? 0.618 0.787 0.624 -0.154 0.011  -0.013 60  TYR DDD C   
4575  O O   . TYR D 60  ? 0.647 0.795 0.628 -0.165 0.015  0.006  60  TYR DDD O   
4576  C CB  . TYR D 60  ? 0.561 0.840 0.592 -0.143 0.023  -0.038 60  TYR DDD CB  
4577  C CG  . TYR D 60  ? 0.528 0.850 0.573 -0.116 0.021  -0.055 60  TYR DDD CG  
4578  C CD1 . TYR D 60  ? 0.493 0.829 0.562 -0.101 0.011  -0.069 60  TYR DDD CD1 
4579  C CD2 . TYR D 60  ? 0.524 0.868 0.554 -0.104 0.030  -0.058 60  TYR DDD CD2 
4580  C CE1 . TYR D 60  ? 0.479 0.846 0.559 -0.075 0.007  -0.081 60  TYR DDD CE1 
4581  C CE2 . TYR D 60  ? 0.499 0.873 0.540 -0.077 0.028  -0.074 60  TYR DDD CE2 
4582  C CZ  . TYR D 60  ? 0.485 0.869 0.553 -0.062 0.016  -0.085 60  TYR DDD CZ  
4583  O OH  . TYR D 60  ? 0.487 0.894 0.566 -0.033 0.013  -0.098 60  TYR DDD OH  
4584  N N   . GLY D 61  ? 0.637 0.787 0.660 -0.159 0.006  -0.021 61  GLY DDD N   
4585  C CA  . GLY D 61  ? 0.699 0.803 0.716 -0.185 0.010  -0.012 61  GLY DDD CA  
4586  C C   . GLY D 61  ? 0.738 0.869 0.755 -0.219 0.024  -0.009 61  GLY DDD C   
4587  O O   . GLY D 61  ? 0.717 0.913 0.753 -0.223 0.030  -0.022 61  GLY DDD O   
4588  N N   . GLU D 62  ? 0.816 0.899 0.815 -0.244 0.030  0.010  62  GLU DDD N   
4589  C CA  . GLU D 62  ? 0.872 0.976 0.867 -0.284 0.046  0.019  62  GLU DDD CA  
4590  C C   . GLU D 62  ? 0.840 0.999 0.869 -0.305 0.051  -0.005 62  GLU DDD C   
4591  O O   . GLU D 62  ? 0.828 1.053 0.870 -0.321 0.063  -0.008 62  GLU DDD O   
4592  C CB  . GLU D 62  ? 0.982 1.007 0.952 -0.306 0.048  0.042  62  GLU DDD CB  
4593  C CG  . GLU D 62  ? 1.053 1.051 0.987 -0.296 0.047  0.072  62  GLU DDD CG  
4594  C CD  . GLU D 62  ? 1.085 1.140 1.004 -0.314 0.064  0.081  62  GLU DDD CD  
4595  O OE1 . GLU D 62  ? 1.108 1.196 1.039 -0.350 0.080  0.078  62  GLU DDD OE1 
4596  O OE2 . GLU D 62  ? 1.098 1.167 0.995 -0.293 0.062  0.090  62  GLU DDD OE2 
4597  N N   . SER D 63  ? 0.828 0.965 0.871 -0.302 0.040  -0.022 63  SER DDD N   
4598  C CA  . SER D 63  ? 0.825 1.000 0.895 -0.330 0.041  -0.043 63  SER DDD CA  
4599  C C   . SER D 63  ? 0.760 1.021 0.860 -0.310 0.036  -0.062 63  SER DDD C   
4600  O O   . SER D 63  ? 0.798 1.110 0.924 -0.333 0.036  -0.077 63  SER DDD O   
4601  C CB  . SER D 63  ? 0.847 0.959 0.912 -0.336 0.032  -0.055 63  SER DDD CB  
4602  O OG  . SER D 63  ? 0.804 0.900 0.867 -0.296 0.020  -0.064 63  SER DDD OG  
4603  N N   . VAL D 64  ? 0.709 0.984 0.805 -0.271 0.031  -0.061 64  VAL DDD N   
4604  C CA  . VAL D 64  ? 0.677 1.026 0.800 -0.248 0.025  -0.077 64  VAL DDD CA  
4605  C C   . VAL D 64  ? 0.669 1.066 0.794 -0.235 0.037  -0.071 64  VAL DDD C   
4606  O O   . VAL D 64  ? 0.637 1.100 0.788 -0.218 0.035  -0.084 64  VAL DDD O   
4607  C CB  . VAL D 64  ? 0.663 0.991 0.782 -0.212 0.009  -0.085 64  VAL DDD CB  
4608  C CG1 . VAL D 64  ? 0.683 0.969 0.798 -0.223 0.000  -0.095 64  VAL DDD CG1 
4609  C CG2 . VAL D 64  ? 0.650 0.937 0.745 -0.184 0.008  -0.072 64  VAL DDD CG2 
4610  N N   . LYS D 65  ? 0.749 1.115 0.845 -0.242 0.048  -0.052 65  LYS DDD N   
4611  C CA  . LYS D 65  ? 0.787 1.195 0.876 -0.233 0.062  -0.048 65  LYS DDD CA  
4612  C C   . LYS D 65  ? 0.783 1.280 0.910 -0.247 0.074  -0.060 65  LYS DDD C   
4613  O O   . LYS D 65  ? 0.822 1.334 0.964 -0.285 0.080  -0.059 65  LYS DDD O   
4614  C CB  . LYS D 65  ? 0.863 1.227 0.914 -0.251 0.072  -0.024 65  LYS DDD CB  
4615  C CG  . LYS D 65  ? 0.916 1.280 0.938 -0.226 0.075  -0.018 65  LYS DDD CG  
4616  C CD  . LYS D 65  ? 1.004 1.308 0.981 -0.234 0.075  0.007  65  LYS DDD CD  
4617  C CE  . LYS D 65  ? 1.009 1.309 0.960 -0.203 0.069  0.006  65  LYS DDD CE  
4618  N NZ  . LYS D 65  ? 1.075 1.355 0.980 -0.217 0.077  0.029  65  LYS DDD NZ  
4619  N N   . GLY D 66  ? 0.735 1.289 0.878 -0.217 0.077  -0.073 66  GLY DDD N   
4620  C CA  . GLY D 66  ? 0.710 1.360 0.896 -0.222 0.090  -0.086 66  GLY DDD CA  
4621  C C   . GLY D 66  ? 0.677 1.369 0.904 -0.206 0.072  -0.103 66  GLY DDD C   
4622  O O   . GLY D 66  ? 0.728 1.495 0.989 -0.187 0.076  -0.116 66  GLY DDD O   
4623  N N   . ARG D 67  ? 0.653 1.299 0.875 -0.213 0.053  -0.104 67  ARG DDD N   
4624  C CA  . ARG D 67  ? 0.601 1.287 0.856 -0.205 0.035  -0.119 67  ARG DDD CA  
4625  C C   . ARG D 67  ? 0.572 1.228 0.816 -0.160 0.017  -0.122 67  ARG DDD C   
4626  O O   . ARG D 67  ? 0.545 1.250 0.816 -0.140 0.004  -0.132 67  ARG DDD O   
4627  C CB  . ARG D 67  ? 0.611 1.269 0.864 -0.244 0.027  -0.120 67  ARG DDD CB  
4628  C CG  . ARG D 67  ? 0.628 1.315 0.895 -0.293 0.043  -0.117 67  ARG DDD CG  
4629  C CD  . ARG D 67  ? 0.639 1.300 0.907 -0.333 0.033  -0.123 67  ARG DDD CD  
4630  N NE  . ARG D 67  ? 0.638 1.193 0.863 -0.332 0.027  -0.117 67  ARG DDD NE  
4631  C CZ  . ARG D 67  ? 0.632 1.151 0.848 -0.322 0.010  -0.128 67  ARG DDD CZ  
4632  N NH1 . ARG D 67  ? 0.612 1.188 0.853 -0.314 -0.006 -0.144 67  ARG DDD NH1 
4633  N NH2 . ARG D 67  ? 0.656 1.084 0.837 -0.320 0.008  -0.122 67  ARG DDD NH2 
4634  N N   . PHE D 68  ? 0.574 1.153 0.779 -0.148 0.015  -0.113 68  PHE DDD N   
4635  C CA  . PHE D 68  ? 0.540 1.079 0.730 -0.114 -0.001 -0.114 68  PHE DDD CA  
4636  C C   . PHE D 68  ? 0.516 1.042 0.690 -0.084 0.005  -0.111 68  PHE DDD C   
4637  O O   . PHE D 68  ? 0.510 1.023 0.666 -0.094 0.019  -0.103 68  PHE DDD O   
4638  C CB  . PHE D 68  ? 0.570 1.035 0.733 -0.124 -0.008 -0.107 68  PHE DDD CB  
4639  C CG  . PHE D 68  ? 0.586 1.048 0.757 -0.148 -0.017 -0.115 68  PHE DDD CG  
4640  C CD1 . PHE D 68  ? 0.586 1.109 0.785 -0.169 -0.018 -0.125 68  PHE DDD CD1 
4641  C CD2 . PHE D 68  ? 0.628 1.026 0.776 -0.151 -0.023 -0.114 68  PHE DDD CD2 
4642  C CE1 . PHE D 68  ? 0.603 1.120 0.804 -0.194 -0.027 -0.134 68  PHE DDD CE1 
4643  C CE2 . PHE D 68  ? 0.644 1.033 0.793 -0.172 -0.029 -0.124 68  PHE DDD CE2 
4644  C CZ  . PHE D 68  ? 0.627 1.074 0.800 -0.195 -0.032 -0.135 68  PHE DDD CZ  
4645  N N   . THR D 69  ? 0.510 1.038 0.687 -0.050 -0.006 -0.116 69  THR DDD N   
4646  C CA  . THR D 69  ? 0.516 1.025 0.676 -0.021 -0.003 -0.117 69  THR DDD CA  
4647  C C   . THR D 69  ? 0.525 0.978 0.666 -0.002 -0.019 -0.113 69  THR DDD C   
4648  O O   . THR D 69  ? 0.504 0.965 0.657 0.009  -0.033 -0.115 69  THR DDD O   
4649  C CB  . THR D 69  ? 0.525 1.094 0.712 0.005  0.002  -0.129 69  THR DDD CB  
4650  O OG1 . THR D 69  ? 0.551 1.184 0.763 -0.017 0.018  -0.133 69  THR DDD OG1 
4651  C CG2 . THR D 69  ? 0.521 1.063 0.686 0.033  0.007  -0.134 69  THR DDD CG2 
4652  N N   . ILE D 70  ? 0.540 0.940 0.651 -0.002 -0.018 -0.106 70  ILE DDD N   
4653  C CA  . ILE D 70  ? 0.547 0.896 0.640 0.014  -0.032 -0.102 70  ILE DDD CA  
4654  C C   . ILE D 70  ? 0.552 0.896 0.637 0.041  -0.032 -0.109 70  ILE DDD C   
4655  O O   . ILE D 70  ? 0.563 0.924 0.642 0.042  -0.019 -0.115 70  ILE DDD O   
4656  C CB  . ILE D 70  ? 0.551 0.851 0.623 -0.002 -0.033 -0.091 70  ILE DDD CB  
4657  C CG1 . ILE D 70  ? 0.556 0.818 0.619 0.009  -0.045 -0.087 70  ILE DDD CG1 
4658  C CG2 . ILE D 70  ? 0.578 0.866 0.628 -0.006 -0.024 -0.087 70  ILE DDD CG2 
4659  C CD1 . ILE D 70  ? 0.580 0.802 0.631 -0.003 -0.047 -0.077 70  ILE DDD CD1 
4660  N N   . SER D 71  ? 0.552 0.874 0.635 0.060  -0.044 -0.109 71  SER DDD N   
4661  C CA  . SER D 71  ? 0.547 0.849 0.620 0.087  -0.046 -0.116 71  SER DDD CA  
4662  C C   . SER D 71  ? 0.574 0.827 0.633 0.092  -0.061 -0.108 71  SER DDD C   
4663  O O   . SER D 71  ? 0.562 0.810 0.624 0.080  -0.068 -0.099 71  SER DDD O   
4664  C CB  . SER D 71  ? 0.538 0.884 0.635 0.110  -0.044 -0.127 71  SER DDD CB  
4665  O OG  . SER D 71  ? 0.530 0.898 0.648 0.117  -0.057 -0.121 71  SER DDD OG  
4666  N N   . ARG D 72  ? 0.596 0.811 0.637 0.107  -0.064 -0.112 72  ARG DDD N   
4667  C CA  . ARG D 72  ? 0.592 0.759 0.619 0.108  -0.077 -0.103 72  ARG DDD CA  
4668  C C   . ARG D 72  ? 0.610 0.751 0.631 0.135  -0.082 -0.110 72  ARG DDD C   
4669  O O   . ARG D 72  ? 0.639 0.788 0.659 0.150  -0.074 -0.124 72  ARG DDD O   
4670  C CB  . ARG D 72  ? 0.604 0.739 0.612 0.089  -0.077 -0.100 72  ARG DDD CB  
4671  C CG  . ARG D 72  ? 0.617 0.737 0.606 0.091  -0.072 -0.111 72  ARG DDD CG  
4672  C CD  . ARG D 72  ? 0.611 0.709 0.583 0.070  -0.076 -0.105 72  ARG DDD CD  
4673  N NE  . ARG D 72  ? 0.628 0.693 0.599 0.064  -0.087 -0.097 72  ARG DDD NE  
4674  C CZ  . ARG D 72  ? 0.630 0.690 0.603 0.046  -0.092 -0.086 72  ARG DDD CZ  
4675  N NH1 . ARG D 72  ? 0.631 0.710 0.607 0.035  -0.089 -0.081 72  ARG DDD NH1 
4676  N NH2 . ARG D 72  ? 0.622 0.658 0.596 0.040  -0.100 -0.079 72  ARG DDD NH2 
4677  N N   . ASP D 73  ? 0.625 0.736 0.640 0.141  -0.093 -0.099 73  ASP DDD N   
4678  C CA  . ASP D 73  ? 0.687 0.756 0.692 0.165  -0.101 -0.100 73  ASP DDD CA  
4679  C C   . ASP D 73  ? 0.712 0.724 0.694 0.148  -0.108 -0.089 73  ASP DDD C   
4680  O O   . ASP D 73  ? 0.746 0.754 0.727 0.139  -0.115 -0.072 73  ASP DDD O   
4681  C CB  . ASP D 73  ? 0.721 0.813 0.742 0.189  -0.109 -0.092 73  ASP DDD CB  
4682  C CG  . ASP D 73  ? 0.790 0.834 0.801 0.217  -0.118 -0.091 73  ASP DDD CG  
4683  O OD1 . ASP D 73  ? 0.805 0.790 0.792 0.213  -0.118 -0.095 73  ASP DDD OD1 
4684  O OD2 . ASP D 73  ? 0.810 0.874 0.835 0.243  -0.127 -0.084 73  ASP DDD OD2 
4685  N N   . ASN D 74  ? 0.739 0.715 0.702 0.141  -0.106 -0.099 74  ASN DDD N   
4686  C CA  . ASN D 74  ? 0.730 0.661 0.676 0.118  -0.113 -0.091 74  ASN DDD CA  
4687  C C   . ASN D 74  ? 0.755 0.639 0.691 0.128  -0.122 -0.078 74  ASN DDD C   
4688  O O   . ASN D 74  ? 0.765 0.633 0.695 0.108  -0.126 -0.062 74  ASN DDD O   
4689  C CB  . ASN D 74  ? 0.743 0.651 0.672 0.108  -0.111 -0.107 74  ASN DDD CB  
4690  C CG  . ASN D 74  ? 0.740 0.689 0.675 0.091  -0.105 -0.109 74  ASN DDD CG  
4691  O OD1 . ASN D 74  ? 0.697 0.688 0.651 0.086  -0.101 -0.100 74  ASN DDD OD1 
4692  N ND2 . ASN D 74  ? 0.789 0.725 0.706 0.081  -0.105 -0.121 74  ASN DDD ND2 
4693  N N   . ALA D 75  ? 0.779 0.645 0.713 0.158  -0.125 -0.083 75  ALA DDD N   
4694  C CA  . ALA D 75  ? 0.830 0.643 0.750 0.171  -0.136 -0.068 75  ALA DDD CA  
4695  C C   . ALA D 75  ? 0.815 0.654 0.741 0.164  -0.141 -0.043 75  ALA DDD C   
4696  O O   . ALA D 75  ? 0.858 0.653 0.765 0.159  -0.149 -0.025 75  ALA DDD O   
4697  C CB  . ALA D 75  ? 0.862 0.660 0.784 0.211  -0.138 -0.078 75  ALA DDD CB  
4698  N N   . LYS D 76  ? 0.753 0.657 0.699 0.160  -0.137 -0.044 76  LYS DDD N   
4699  C CA  . LYS D 76  ? 0.750 0.683 0.698 0.154  -0.142 -0.026 76  LYS DDD CA  
4700  C C   . LYS D 76  ? 0.698 0.659 0.650 0.122  -0.133 -0.025 76  LYS DDD C   
4701  O O   . LYS D 76  ? 0.698 0.689 0.653 0.116  -0.134 -0.016 76  LYS DDD O   
4702  C CB  . LYS D 76  ? 0.739 0.728 0.708 0.176  -0.145 -0.029 76  LYS DDD CB  
4703  C CG  . LYS D 76  ? 0.796 0.768 0.768 0.214  -0.154 -0.030 76  LYS DDD CG  
4704  C CD  . LYS D 76  ? 0.795 0.827 0.791 0.235  -0.162 -0.027 76  LYS DDD CD  
4705  C CE  . LYS D 76  ? 0.856 0.870 0.857 0.277  -0.172 -0.025 76  LYS DDD CE  
4706  N NZ  . LYS D 76  ? 0.868 0.953 0.899 0.298  -0.182 -0.023 76  LYS DDD NZ  
4707  N N   . ASN D 77  ? 0.701 0.653 0.655 0.104  -0.126 -0.034 77  ASN DDD N   
4708  C CA  . ASN D 77  ? 0.656 0.632 0.618 0.079  -0.119 -0.032 77  ASN DDD CA  
4709  C C   . ASN D 77  ? 0.606 0.636 0.585 0.080  -0.114 -0.037 77  ASN DDD C   
4710  O O   . ASN D 77  ? 0.564 0.611 0.546 0.066  -0.110 -0.032 77  ASN DDD O   
4711  C CB  . ASN D 77  ? 0.651 0.610 0.602 0.062  -0.119 -0.015 77  ASN DDD CB  
4712  C CG  . ASN D 77  ? 0.657 0.578 0.600 0.044  -0.120 -0.013 77  ASN DDD CG  
4713  O OD1 . ASN D 77  ? 0.677 0.562 0.611 0.051  -0.125 -0.020 77  ASN DDD OD1 
4714  N ND2 . ASN D 77  ? 0.653 0.583 0.600 0.021  -0.114 -0.004 77  ASN DDD ND2 
4715  N N   . THR D 78  ? 0.573 0.628 0.563 0.097  -0.114 -0.048 78  THR DDD N   
4716  C CA  . THR D 78  ? 0.554 0.659 0.560 0.096  -0.111 -0.052 78  THR DDD CA  
4717  C C   . THR D 78  ? 0.545 0.677 0.566 0.093  -0.102 -0.066 78  THR DDD C   
4718  O O   . THR D 78  ? 0.584 0.709 0.604 0.105  -0.100 -0.074 78  THR DDD O   
4719  C CB  . THR D 78  ? 0.564 0.687 0.573 0.116  -0.121 -0.047 78  THR DDD CB  
4720  O OG1 . THR D 78  ? 0.595 0.691 0.584 0.115  -0.129 -0.031 78  THR DDD OG1 
4721  C CG2 . THR D 78  ? 0.518 0.696 0.545 0.112  -0.121 -0.053 78  THR DDD CG2 
4722  N N   . VAL D 79  ? 0.528 0.685 0.558 0.076  -0.096 -0.067 79  VAL DDD N   
4723  C CA  . VAL D 79  ? 0.515 0.702 0.558 0.069  -0.087 -0.077 79  VAL DDD CA  
4724  C C   . VAL D 79  ? 0.505 0.737 0.565 0.068  -0.089 -0.080 79  VAL DDD C   
4725  O O   . VAL D 79  ? 0.518 0.753 0.574 0.064  -0.095 -0.076 79  VAL DDD O   
4726  C CB  . VAL D 79  ? 0.490 0.664 0.530 0.049  -0.081 -0.074 79  VAL DDD CB  
4727  C CG1 . VAL D 79  ? 0.509 0.682 0.550 0.037  -0.081 -0.070 79  VAL DDD CG1 
4728  C CG2 . VAL D 79  ? 0.471 0.668 0.519 0.040  -0.072 -0.080 79  VAL DDD CG2 
4729  N N   . TYR D 80  ? 0.495 0.764 0.571 0.071  -0.083 -0.088 80  TYR DDD N   
4730  C CA  . TYR D 80  ? 0.514 0.835 0.611 0.069  -0.086 -0.093 80  TYR DDD CA  
4731  C C   . TYR D 80  ? 0.514 0.857 0.621 0.044  -0.074 -0.099 80  TYR DDD C   
4732  O O   . TYR D 80  ? 0.504 0.833 0.605 0.039  -0.063 -0.099 80  TYR DDD O   
4733  C CB  . TYR D 80  ? 0.527 0.882 0.642 0.095  -0.089 -0.098 80  TYR DDD CB  
4734  C CG  . TYR D 80  ? 0.554 0.881 0.658 0.121  -0.102 -0.091 80  TYR DDD CG  
4735  C CD1 . TYR D 80  ? 0.570 0.907 0.673 0.126  -0.117 -0.082 80  TYR DDD CD1 
4736  C CD2 . TYR D 80  ? 0.583 0.870 0.674 0.139  -0.100 -0.092 80  TYR DDD CD2 
4737  C CE1 . TYR D 80  ? 0.590 0.898 0.679 0.149  -0.130 -0.071 80  TYR DDD CE1 
4738  C CE2 . TYR D 80  ? 0.601 0.854 0.680 0.162  -0.112 -0.083 80  TYR DDD CE2 
4739  C CZ  . TYR D 80  ? 0.604 0.867 0.683 0.166  -0.127 -0.071 80  TYR DDD CZ  
4740  O OH  . TYR D 80  ? 0.649 0.873 0.711 0.187  -0.140 -0.059 80  TYR DDD OH  
4741  N N   . LEU D 81  ? 0.509 0.884 0.629 0.028  -0.076 -0.102 81  LEU DDD N   
4742  C CA  . LEU D 81  ? 0.521 0.922 0.654 0.003  -0.066 -0.108 81  LEU DDD CA  
4743  C C   . LEU D 81  ? 0.525 0.993 0.688 0.002  -0.071 -0.115 81  LEU DDD C   
4744  O O   . LEU D 81  ? 0.526 1.009 0.691 -0.005 -0.083 -0.118 81  LEU DDD O   
4745  C CB  . LEU D 81  ? 0.543 0.909 0.663 -0.022 -0.064 -0.107 81  LEU DDD CB  
4746  C CG  . LEU D 81  ? 0.552 0.923 0.678 -0.050 -0.052 -0.109 81  LEU DDD CG  
4747  C CD1 . LEU D 81  ? 0.564 0.913 0.679 -0.049 -0.041 -0.101 81  LEU DDD CD1 
4748  C CD2 . LEU D 81  ? 0.562 0.896 0.675 -0.071 -0.052 -0.111 81  LEU DDD CD2 
4749  N N   . GLN D 82  ? 0.504 1.014 0.687 0.008  -0.062 -0.119 82  GLN DDD N   
4750  C CA  . GLN D 82  ? 0.489 1.077 0.709 0.005  -0.063 -0.127 82  GLN DDD CA  
4751  C C   . GLN D 82  ? 0.493 1.093 0.720 -0.038 -0.054 -0.130 82  GLN DDD C   
4752  O O   . GLN D 82  ? 0.473 1.049 0.687 -0.052 -0.037 -0.126 82  GLN DDD O   
4753  C CB  . GLN D 82  ? 0.484 1.110 0.725 0.030  -0.053 -0.132 82  GLN DDD CB  
4754  C CG  . GLN D 82  ? 0.468 1.185 0.755 0.034  -0.056 -0.139 82  GLN DDD CG  
4755  C CD  . GLN D 82  ? 0.463 1.203 0.762 0.048  -0.081 -0.137 82  GLN DDD CD  
4756  O OE1 . GLN D 82  ? 0.457 1.162 0.740 0.077  -0.094 -0.131 82  GLN DDD OE1 
4757  N NE2 . GLN D 82  ? 0.476 1.277 0.803 0.024  -0.088 -0.142 82  GLN DDD NE2 
4758  N N   . MET D 83  ? 0.518 1.144 0.755 -0.058 -0.065 -0.135 83  MET DDD N   
4759  C CA  . MET D 83  ? 0.552 1.182 0.793 -0.101 -0.057 -0.140 83  MET DDD CA  
4760  C C   . MET D 83  ? 0.560 1.281 0.844 -0.114 -0.060 -0.149 83  MET DDD C   
4761  O O   . MET D 83  ? 0.584 1.344 0.883 -0.106 -0.080 -0.154 83  MET DDD O   
4762  C CB  . MET D 83  ? 0.583 1.165 0.799 -0.119 -0.067 -0.144 83  MET DDD CB  
4763  C CG  . MET D 83  ? 0.608 1.111 0.788 -0.103 -0.066 -0.136 83  MET DDD CG  
4764  S SD  . MET D 83  ? 0.666 1.117 0.818 -0.121 -0.073 -0.144 83  MET DDD SD  
4765  C CE  . MET D 83  ? 0.696 1.196 0.852 -0.107 -0.095 -0.150 83  MET DDD CE  
4766  N N   . ASN D 84  ? 0.571 1.329 0.876 -0.133 -0.042 -0.149 84  ASN DDD N   
4767  C CA  . ASN D 84  ? 0.562 1.418 0.916 -0.149 -0.040 -0.157 84  ASN DDD CA  
4768  C C   . ASN D 84  ? 0.594 1.448 0.949 -0.204 -0.033 -0.160 84  ASN DDD C   
4769  O O   . ASN D 84  ? 0.637 1.413 0.956 -0.224 -0.022 -0.153 84  ASN DDD O   
4770  C CB  . ASN D 84  ? 0.554 1.462 0.933 -0.127 -0.022 -0.156 84  ASN DDD CB  
4771  C CG  . ASN D 84  ? 0.542 1.449 0.921 -0.072 -0.031 -0.156 84  ASN DDD CG  
4772  O OD1 . ASN D 84  ? 0.522 1.435 0.906 -0.051 -0.054 -0.156 84  ASN DDD OD1 
4773  N ND2 . ASN D 84  ? 0.563 1.460 0.934 -0.050 -0.013 -0.155 84  ASN DDD ND2 
4774  N N   . ARG D 85  ? 0.608 1.546 1.005 -0.228 -0.039 -0.170 85  ARG DDD N   
4775  C CA  . ARG D 85  ? 0.645 1.595 1.052 -0.287 -0.031 -0.174 85  ARG DDD CA  
4776  C C   . ARG D 85  ? 0.644 1.490 1.002 -0.309 -0.036 -0.175 85  ARG DDD C   
4777  O O   . ARG D 85  ? 0.655 1.443 0.990 -0.339 -0.020 -0.168 85  ARG DDD O   
4778  C CB  . ARG D 85  ? 0.682 1.655 1.100 -0.304 -0.001 -0.165 85  ARG DDD CB  
4779  C CG  . ARG D 85  ? 0.675 1.751 1.142 -0.276 0.007  -0.168 85  ARG DDD CG  
4780  C CD  . ARG D 85  ? 0.704 1.841 1.197 -0.307 0.036  -0.165 85  ARG DDD CD  
4781  N NE  . ARG D 85  ? 0.740 1.797 1.187 -0.333 0.058  -0.151 85  ARG DDD NE  
4782  C CZ  . ARG D 85  ? 0.736 1.727 1.141 -0.304 0.068  -0.140 85  ARG DDD CZ  
4783  N NH1 . ARG D 85  ? 0.700 1.691 1.102 -0.249 0.061  -0.144 85  ARG DDD NH1 
4784  N NH2 . ARG D 85  ? 0.776 1.698 1.140 -0.331 0.084  -0.125 85  ARG DDD NH2 
4785  N N   . LEU D 86  ? 0.633 1.458 0.975 -0.293 -0.059 -0.183 86  LEU DDD N   
4786  C CA  . LEU D 86  ? 0.672 1.403 0.968 -0.307 -0.064 -0.187 86  LEU DDD CA  
4787  C C   . LEU D 86  ? 0.713 1.438 1.011 -0.364 -0.063 -0.200 86  LEU DDD C   
4788  O O   . LEU D 86  ? 0.707 1.516 1.042 -0.389 -0.073 -0.211 86  LEU DDD O   
4789  C CB  . LEU D 86  ? 0.657 1.384 0.938 -0.276 -0.086 -0.193 86  LEU DDD CB  
4790  C CG  . LEU D 86  ? 0.622 1.315 0.885 -0.226 -0.085 -0.180 86  LEU DDD CG  
4791  C CD1 . LEU D 86  ? 0.622 1.335 0.878 -0.197 -0.108 -0.182 86  LEU DDD CD1 
4792  C CD2 . LEU D 86  ? 0.651 1.244 0.873 -0.225 -0.072 -0.173 86  LEU DDD CD2 
4793  N N   . LYS D 87  ? 0.753 1.384 1.016 -0.384 -0.053 -0.199 87  LYS DDD N   
4794  C CA  . LYS D 87  ? 0.823 1.419 1.077 -0.438 -0.051 -0.211 87  LYS DDD CA  
4795  C C   . LYS D 87  ? 0.839 1.358 1.053 -0.435 -0.061 -0.226 87  LYS DDD C   
4796  O O   . LYS D 87  ? 0.820 1.297 1.009 -0.394 -0.063 -0.221 87  LYS DDD O   
4797  C CB  . LYS D 87  ? 0.874 1.417 1.118 -0.462 -0.027 -0.194 87  LYS DDD CB  
4798  C CG  . LYS D 87  ? 0.879 1.481 1.149 -0.451 -0.011 -0.175 87  LYS DDD CG  
4799  C CD  . LYS D 87  ? 0.931 1.471 1.179 -0.468 0.011  -0.154 87  LYS DDD CD  
4800  C CE  . LYS D 87  ? 0.929 1.545 1.203 -0.467 0.028  -0.140 87  LYS DDD CE  
4801  N NZ  . LYS D 87  ? 0.971 1.532 1.219 -0.486 0.050  -0.117 87  LYS DDD NZ  
4802  N N   . PRO D 88  ? 0.875 1.374 1.079 -0.478 -0.068 -0.248 88  PRO DDD N   
4803  C CA  . PRO D 88  ? 0.904 1.325 1.065 -0.476 -0.075 -0.266 88  PRO DDD CA  
4804  C C   . PRO D 88  ? 0.891 1.208 1.020 -0.449 -0.059 -0.254 88  PRO DDD C   
4805  O O   . PRO D 88  ? 0.860 1.143 0.963 -0.421 -0.064 -0.262 88  PRO DDD O   
4806  C CB  . PRO D 88  ? 0.968 1.374 1.127 -0.536 -0.078 -0.288 88  PRO DDD CB  
4807  C CG  . PRO D 88  ? 0.941 1.464 1.149 -0.561 -0.086 -0.288 88  PRO DDD CG  
4808  C CD  . PRO D 88  ? 0.889 1.448 1.124 -0.532 -0.071 -0.258 88  PRO DDD CD  
4809  N N   . GLU D 89  ? 0.905 1.181 1.035 -0.457 -0.041 -0.234 89  GLU DDD N   
4810  C CA  . GLU D 89  ? 0.924 1.105 1.026 -0.432 -0.029 -0.219 89  GLU DDD CA  
4811  C C   . GLU D 89  ? 0.824 1.022 0.926 -0.377 -0.030 -0.204 89  GLU DDD C   
4812  O O   . GLU D 89  ? 0.797 0.927 0.880 -0.353 -0.022 -0.193 89  GLU DDD O   
4813  C CB  . GLU D 89  ? 0.988 1.127 1.090 -0.453 -0.012 -0.197 89  GLU DDD CB  
4814  C CG  . GLU D 89  ? 0.985 1.200 1.114 -0.450 -0.006 -0.176 89  GLU DDD CG  
4815  C CD  . GLU D 89  ? 1.065 1.315 1.214 -0.502 0.003  -0.172 89  GLU DDD CD  
4816  O OE1 . GLU D 89  ? 1.065 1.314 1.218 -0.547 -0.002 -0.191 89  GLU DDD OE1 
4817  O OE2 . GLU D 89  ? 1.065 1.354 1.226 -0.499 0.015  -0.150 89  GLU DDD OE2 
4818  N N   . ASP D 90  ? 0.755 1.038 0.879 -0.359 -0.040 -0.203 90  ASP DDD N   
4819  C CA  . ASP D 90  ? 0.699 0.996 0.821 -0.310 -0.043 -0.191 90  ASP DDD CA  
4820  C C   . ASP D 90  ? 0.689 0.974 0.791 -0.290 -0.055 -0.207 90  ASP DDD C   
4821  O O   . ASP D 90  ? 0.655 0.936 0.750 -0.253 -0.056 -0.197 90  ASP DDD O   
4822  C CB  . ASP D 90  ? 0.651 1.038 0.805 -0.296 -0.048 -0.183 90  ASP DDD CB  
4823  C CG  . ASP D 90  ? 0.638 1.044 0.808 -0.308 -0.033 -0.167 90  ASP DDD CG  
4824  O OD1 . ASP D 90  ? 0.622 0.967 0.773 -0.303 -0.020 -0.151 90  ASP DDD OD1 
4825  O OD2 . ASP D 90  ? 0.633 1.117 0.835 -0.322 -0.034 -0.169 90  ASP DDD OD2 
4826  N N   . THR D 91  ? 0.716 0.994 0.806 -0.317 -0.062 -0.231 91  THR DDD N   
4827  C CA  . THR D 91  ? 0.732 0.995 0.794 -0.304 -0.071 -0.248 91  THR DDD CA  
4828  C C   . THR D 91  ? 0.759 0.943 0.799 -0.279 -0.057 -0.244 91  THR DDD C   
4829  O O   . THR D 91  ? 0.839 0.959 0.871 -0.292 -0.045 -0.245 91  THR DDD O   
4830  C CB  . THR D 91  ? 0.763 1.025 0.812 -0.343 -0.079 -0.277 91  THR DDD CB  
4831  O OG1 . THR D 91  ? 0.731 1.082 0.808 -0.361 -0.095 -0.278 91  THR DDD OG1 
4832  C CG2 . THR D 91  ? 0.770 1.006 0.782 -0.332 -0.084 -0.297 91  THR DDD CG2 
4833  N N   . ALA D 92  ? 0.743 0.934 0.773 -0.244 -0.060 -0.238 92  ALA DDD N   
4834  C CA  . ALA D 92  ? 0.745 0.876 0.759 -0.218 -0.048 -0.233 92  ALA DDD CA  
4835  C C   . ALA D 92  ? 0.705 0.864 0.712 -0.186 -0.053 -0.226 92  ALA DDD C   
4836  O O   . ALA D 92  ? 0.673 0.889 0.686 -0.182 -0.066 -0.220 92  ALA DDD O   
4837  C CB  . ALA D 92  ? 0.733 0.832 0.762 -0.208 -0.037 -0.210 92  ALA DDD CB  
4838  N N   . VAL D 93  ? 0.704 0.821 0.698 -0.165 -0.042 -0.225 93  VAL DDD N   
4839  C CA  . VAL D 93  ? 0.666 0.800 0.657 -0.136 -0.043 -0.211 93  VAL DDD CA  
4840  C C   . VAL D 93  ? 0.614 0.751 0.629 -0.120 -0.042 -0.185 93  VAL DDD C   
4841  O O   . VAL D 93  ? 0.597 0.695 0.619 -0.121 -0.033 -0.180 93  VAL DDD O   
4842  C CB  . VAL D 93  ? 0.693 0.789 0.665 -0.123 -0.030 -0.222 93  VAL DDD CB  
4843  C CG1 . VAL D 93  ? 0.653 0.766 0.626 -0.097 -0.029 -0.205 93  VAL DDD CG1 
4844  C CG2 . VAL D 93  ? 0.716 0.813 0.658 -0.140 -0.031 -0.250 93  VAL DDD CG2 
4845  N N   . TYR D 94  ? 0.589 0.766 0.610 -0.107 -0.052 -0.171 94  TYR DDD N   
4846  C CA  . TYR D 94  ? 0.568 0.750 0.606 -0.091 -0.051 -0.151 94  TYR DDD CA  
4847  C C   . TYR D 94  ? 0.570 0.741 0.602 -0.068 -0.050 -0.140 94  TYR DDD C   
4848  O O   . TYR D 94  ? 0.585 0.774 0.604 -0.061 -0.055 -0.141 94  TYR DDD O   
4849  C CB  . TYR D 94  ? 0.555 0.788 0.607 -0.092 -0.062 -0.145 94  TYR DDD CB  
4850  C CG  . TYR D 94  ? 0.595 0.843 0.662 -0.116 -0.060 -0.151 94  TYR DDD CG  
4851  C CD1 . TYR D 94  ? 0.632 0.889 0.696 -0.142 -0.063 -0.168 94  TYR DDD CD1 
4852  C CD2 . TYR D 94  ? 0.595 0.847 0.676 -0.117 -0.054 -0.139 94  TYR DDD CD2 
4853  C CE1 . TYR D 94  ? 0.641 0.911 0.719 -0.169 -0.060 -0.172 94  TYR DDD CE1 
4854  C CE2 . TYR D 94  ? 0.619 0.886 0.712 -0.142 -0.049 -0.142 94  TYR DDD CE2 
4855  C CZ  . TYR D 94  ? 0.637 0.913 0.731 -0.170 -0.053 -0.158 94  TYR DDD CZ  
4856  O OH  . TYR D 94  ? 0.649 0.941 0.757 -0.200 -0.048 -0.160 94  TYR DDD OH  
4857  N N   . PHE D 95  ? 0.559 0.700 0.598 -0.059 -0.042 -0.130 95  PHE DDD N   
4858  C CA  . PHE D 95  ? 0.540 0.671 0.579 -0.040 -0.040 -0.120 95  PHE DDD CA  
4859  C C   . PHE D 95  ? 0.536 0.677 0.584 -0.030 -0.046 -0.104 95  PHE DDD C   
4860  O O   . PHE D 95  ? 0.551 0.686 0.607 -0.034 -0.045 -0.098 95  PHE DDD O   
4861  C CB  . PHE D 95  ? 0.540 0.637 0.586 -0.036 -0.029 -0.121 95  PHE DDD CB  
4862  C CG  . PHE D 95  ? 0.570 0.649 0.605 -0.042 -0.020 -0.141 95  PHE DDD CG  
4863  C CD1 . PHE D 95  ? 0.606 0.663 0.639 -0.057 -0.017 -0.153 95  PHE DDD CD1 
4864  C CD2 . PHE D 95  ? 0.575 0.658 0.601 -0.034 -0.013 -0.148 95  PHE DDD CD2 
4865  C CE1 . PHE D 95  ? 0.644 0.677 0.664 -0.063 -0.008 -0.175 95  PHE DDD CE1 
4866  C CE2 . PHE D 95  ? 0.602 0.669 0.615 -0.039 -0.002 -0.170 95  PHE DDD CE2 
4867  C CZ  . PHE D 95  ? 0.640 0.679 0.650 -0.052 -0.000 -0.184 95  PHE DDD CZ  
4868  N N   . CYS D 96  ? 0.525 0.676 0.568 -0.019 -0.050 -0.097 96  CYS DDD N   
4869  C CA  . CYS D 96  ? 0.525 0.674 0.573 -0.009 -0.055 -0.083 96  CYS DDD CA  
4870  C C   . CYS D 96  ? 0.493 0.622 0.549 -0.005 -0.050 -0.077 96  CYS DDD C   
4871  O O   . CYS D 96  ? 0.480 0.603 0.538 -0.004 -0.043 -0.081 96  CYS DDD O   
4872  C CB  . CYS D 96  ? 0.563 0.722 0.600 -0.001 -0.062 -0.079 96  CYS DDD CB  
4873  S SG  . CYS D 96  ? 0.639 0.790 0.677 0.011  -0.069 -0.067 96  CYS DDD SG  
4874  N N   . ALA D 97  ? 0.481 0.603 0.543 -0.002 -0.054 -0.068 97  ALA DDD N   
4875  C CA  . ALA D 97  ? 0.483 0.594 0.555 0.003  -0.054 -0.060 97  ALA DDD CA  
4876  C C   . ALA D 97  ? 0.469 0.581 0.538 0.006  -0.063 -0.051 97  ALA DDD C   
4877  O O   . ALA D 97  ? 0.436 0.553 0.496 0.006  -0.067 -0.053 97  ALA DDD O   
4878  C CB  . ALA D 97  ? 0.492 0.588 0.573 0.002  -0.050 -0.058 97  ALA DDD CB  
4879  N N   . ALA D 98  ? 0.460 0.571 0.539 0.008  -0.066 -0.045 98  ALA DDD N   
4880  C CA  . ALA D 98  ? 0.458 0.567 0.533 0.007  -0.075 -0.039 98  ALA DDD CA  
4881  C C   . ALA D 98  ? 0.436 0.549 0.528 0.007  -0.081 -0.031 98  ALA DDD C   
4882  O O   . ALA D 98  ? 0.416 0.537 0.528 0.010  -0.075 -0.029 98  ALA DDD O   
4883  C CB  . ALA D 98  ? 0.458 0.565 0.526 0.006  -0.077 -0.039 98  ALA DDD CB  
4884  N N   . ASP D 99  ? 0.444 0.554 0.527 0.004  -0.091 -0.027 99  ASP DDD N   
4885  C CA  . ASP D 99  ? 0.464 0.584 0.562 0.002  -0.102 -0.018 99  ASP DDD CA  
4886  C C   . ASP D 99  ? 0.481 0.595 0.561 -0.005 -0.115 -0.019 99  ASP DDD C   
4887  O O   . ASP D 99  ? 0.479 0.581 0.534 -0.005 -0.114 -0.026 99  ASP DDD O   
4888  C CB  . ASP D 99  ? 0.456 0.575 0.561 0.009  -0.104 -0.009 99  ASP DDD CB  
4889  C CG  . ASP D 99  ? 0.473 0.610 0.606 0.013  -0.113 0.000  99  ASP DDD CG  
4890  O OD1 . ASP D 99  ? 0.457 0.606 0.618 0.019  -0.104 -0.001 99  ASP DDD OD1 
4891  O OD2 . ASP D 99  ? 0.502 0.646 0.631 0.009  -0.129 0.008  99  ASP DDD OD2 
4892  N N   . ARG D 100 ? 0.462 0.618 0.629 -0.013 -0.032 0.078  100 ARG DDD N   
4893  C CA  . ARG D 100 ? 0.490 0.611 0.700 -0.017 -0.046 0.070  100 ARG DDD CA  
4894  C C   . ARG D 100 ? 0.473 0.567 0.647 -0.020 -0.059 0.031  100 ARG DDD C   
4895  O O   . ARG D 100 ? 0.480 0.544 0.657 -0.016 -0.067 0.015  100 ARG DDD O   
4896  C CB  . ARG D 100 ? 0.531 0.645 0.798 -0.026 -0.049 0.086  100 ARG DDD CB  
4897  C CG  . ARG D 100 ? 0.551 0.692 0.864 -0.021 -0.031 0.133  100 ARG DDD CG  
4898  C CD  . ARG D 100 ? 0.593 0.710 0.953 -0.020 -0.035 0.148  100 ARG DDD CD  
4899  N NE  . ARG D 100 ? 0.632 0.705 1.044 -0.036 -0.059 0.129  100 ARG DDD NE  
4900  C CZ  . ARG D 100 ? 0.663 0.732 1.156 -0.049 -0.065 0.154  100 ARG DDD CZ  
4901  N NH1 . ARG D 100 ? 0.649 0.758 1.188 -0.044 -0.039 0.208  100 ARG DDD NH1 
4902  N NH2 . ARG D 100 ? 0.685 0.709 1.217 -0.068 -0.096 0.128  100 ARG DDD NH2 
4903  N N   . GLY D 101 ? 0.449 0.554 0.591 -0.023 -0.057 0.018  101 GLY DDD N   
4904  C CA  . GLY D 101 ? 0.469 0.556 0.580 -0.024 -0.067 -0.009 101 GLY DDD CA  
4905  C C   . GLY D 101 ? 0.464 0.561 0.539 -0.018 -0.058 -0.017 101 GLY DDD C   
4906  O O   . GLY D 101 ? 0.454 0.577 0.523 -0.020 -0.049 -0.008 101 GLY DDD O   
4907  N N   . GLU D 102 ? 0.468 0.546 0.522 -0.012 -0.060 -0.033 102 GLU DDD N   
4908  C CA  . GLU D 102 ? 0.475 0.566 0.508 -0.007 -0.049 -0.036 102 GLU DDD CA  
4909  C C   . GLU D 102 ? 0.497 0.586 0.511 -0.011 -0.049 -0.042 102 GLU DDD C   
4910  O O   . GLU D 102 ? 0.525 0.594 0.522 -0.008 -0.059 -0.051 102 GLU DDD O   
4911  C CB  . GLU D 102 ? 0.495 0.569 0.517 0.009  -0.042 -0.043 102 GLU DDD CB  
4912  C CG  . GLU D 102 ? 0.483 0.580 0.504 0.016  -0.025 -0.034 102 GLU DDD CG  
4913  C CD  . GLU D 102 ? 0.518 0.602 0.532 0.039  -0.008 -0.035 102 GLU DDD CD  
4914  O OE1 . GLU D 102 ? 0.573 0.630 0.589 0.049  -0.009 -0.043 102 GLU DDD OE1 
4915  O OE2 . GLU D 102 ? 0.570 0.668 0.577 0.049  0.010  -0.028 102 GLU DDD OE2 
4916  N N   . SER D 103 ? 0.476 0.581 0.493 -0.019 -0.042 -0.038 103 SER DDD N   
4917  C CA  . SER D 103 ? 0.468 0.568 0.479 -0.022 -0.038 -0.038 103 SER DDD CA  
4918  C C   . SER D 103 ? 0.468 0.569 0.469 -0.015 -0.028 -0.034 103 SER DDD C   
4919  O O   . SER D 103 ? 0.466 0.582 0.479 -0.016 -0.020 -0.028 103 SER DDD O   
4920  C CB  . SER D 103 ? 0.479 0.584 0.497 -0.032 -0.033 -0.040 103 SER DDD CB  
4921  O OG  . SER D 103 ? 0.458 0.551 0.479 -0.032 -0.025 -0.039 103 SER DDD OG  
4922  N N   . TYR D 104 ? 0.498 0.590 0.484 -0.009 -0.026 -0.029 104 TYR DDD N   
4923  C CA  . TYR D 104 ? 0.512 0.609 0.497 -0.003 -0.010 -0.015 104 TYR DDD CA  
4924  C C   . TYR D 104 ? 0.496 0.599 0.518 -0.019 -0.002 -0.011 104 TYR DDD C   
4925  O O   . TYR D 104 ? 0.501 0.616 0.544 -0.020 0.010  0.003  104 TYR DDD O   
4926  C CB  . TYR D 104 ? 0.547 0.637 0.512 0.007  -0.013 -0.005 104 TYR DDD CB  
4927  C CG  . TYR D 104 ? 0.567 0.664 0.530 0.017  0.008  0.019  104 TYR DDD CG  
4928  C CD1 . TYR D 104 ? 0.575 0.679 0.510 0.034  0.023  0.026  104 TYR DDD CD1 
4929  C CD2 . TYR D 104 ? 0.557 0.653 0.552 0.012  0.018  0.038  104 TYR DDD CD2 
4930  C CE1 . TYR D 104 ? 0.600 0.717 0.537 0.047  0.048  0.057  104 TYR DDD CE1 
4931  C CE2 . TYR D 104 ? 0.573 0.678 0.578 0.021  0.040  0.069  104 TYR DDD CE2 
4932  C CZ  . TYR D 104 ? 0.610 0.729 0.585 0.039  0.056  0.080  104 TYR DDD CZ  
4933  O OH  . TYR D 104 ? 0.646 0.780 0.634 0.051  0.084  0.119  104 TYR DDD OH  
4934  N N   . TYR D 105 ? 0.494 0.587 0.527 -0.030 -0.009 -0.022 105 TYR DDD N   
4935  C CA  . TYR D 105 ? 0.490 0.575 0.546 -0.047 -0.005 -0.029 105 TYR DDD CA  
4936  C C   . TYR D 105 ? 0.486 0.585 0.537 -0.058 -0.018 -0.044 105 TYR DDD C   
4937  O O   . TYR D 105 ? 0.504 0.591 0.540 -0.064 -0.022 -0.060 105 TYR DDD O   
4938  C CB  . TYR D 105 ? 0.489 0.549 0.548 -0.046 0.001  -0.034 105 TYR DDD CB  
4939  C CG  . TYR D 105 ? 0.501 0.556 0.568 -0.032 0.010  -0.013 105 TYR DDD CG  
4940  C CD1 . TYR D 105 ? 0.504 0.556 0.592 -0.030 0.022  0.008  105 TYR DDD CD1 
4941  C CD2 . TYR D 105 ? 0.500 0.557 0.559 -0.020 0.004  -0.007 105 TYR DDD CD2 
4942  C CE1 . TYR D 105 ? 0.519 0.571 0.609 -0.015 0.029  0.034  105 TYR DDD CE1 
4943  C CE2 . TYR D 105 ? 0.503 0.562 0.569 -0.008 0.005  0.017  105 TYR DDD CE2 
4944  C CZ  . TYR D 105 ? 0.510 0.567 0.587 -0.004 0.018  0.038  105 TYR DDD CZ  
4945  O OH  . TYR D 105 ? 0.540 0.605 0.619 0.011  0.018  0.068  105 TYR DDD OH  
4946  N N   . TYR D 106 ? 0.480 0.604 0.540 -0.057 -0.022 -0.034 106 TYR DDD N   
4947  C CA  . TYR D 106 ? 0.491 0.637 0.550 -0.062 -0.036 -0.037 106 TYR DDD CA  
4948  C C   . TYR D 106 ? 0.497 0.648 0.562 -0.084 -0.051 -0.050 106 TYR DDD C   
4949  O O   . TYR D 106 ? 0.523 0.693 0.574 -0.087 -0.066 -0.053 106 TYR DDD O   
4950  C CB  . TYR D 106 ? 0.498 0.670 0.578 -0.052 -0.032 -0.019 106 TYR DDD CB  
4951  C CG  . TYR D 106 ? 0.514 0.703 0.633 -0.056 -0.022 -0.002 106 TYR DDD CG  
4952  C CD1 . TYR D 106 ? 0.504 0.718 0.666 -0.077 -0.036 0.004  106 TYR DDD CD1 
4953  C CD2 . TYR D 106 ? 0.514 0.696 0.629 -0.038 -0.000 0.011  106 TYR DDD CD2 
4954  C CE1 . TYR D 106 ? 0.484 0.718 0.701 -0.082 -0.026 0.026  106 TYR DDD CE1 
4955  C CE2 . TYR D 106 ? 0.519 0.719 0.675 -0.038 0.016  0.035  106 TYR DDD CE2 
4956  C CZ  . TYR D 106 ? 0.510 0.738 0.726 -0.061 0.005  0.045  106 TYR DDD CZ  
4957  O OH  . TYR D 106 ? 0.509 0.761 0.783 -0.062 0.023  0.076  106 TYR DDD OH  
4958  N N   . THR D 107 ? 0.636 0.526 0.752 -0.119 0.065  -0.104 107 THR DDD N   
4959  C CA  . THR D 107 ? 0.630 0.527 0.746 -0.127 0.074  -0.110 107 THR DDD CA  
4960  C C   . THR D 107 ? 0.610 0.494 0.732 -0.119 0.073  -0.105 107 THR DDD C   
4961  O O   . THR D 107 ? 0.627 0.514 0.747 -0.125 0.080  -0.110 107 THR DDD O   
4962  C CB  . THR D 107 ? 0.644 0.524 0.734 -0.145 0.084  -0.116 107 THR DDD CB  
4963  O OG1 . THR D 107 ? 0.691 0.528 0.758 -0.143 0.084  -0.110 107 THR DDD OG1 
4964  C CG2 . THR D 107 ? 0.644 0.536 0.727 -0.153 0.087  -0.120 107 THR DDD CG2 
4965  N N   . ARG D 108 ? 0.597 0.470 0.724 -0.106 0.065  -0.096 108 ARG DDD N   
4966  C CA  . ARG D 108 ? 0.590 0.457 0.725 -0.096 0.065  -0.091 108 ARG DDD CA  
4967  C C   . ARG D 108 ? 0.550 0.445 0.710 -0.091 0.063  -0.092 108 ARG DDD C   
4968  O O   . ARG D 108 ? 0.517 0.428 0.692 -0.087 0.055  -0.088 108 ARG DDD O   
4969  C CB  . ARG D 108 ? 0.605 0.460 0.742 -0.083 0.056  -0.081 108 ARG DDD CB  
4970  C CG  . ARG D 108 ? 0.642 0.461 0.748 -0.082 0.057  -0.079 108 ARG DDD CG  
4971  C CD  . ARG D 108 ? 0.655 0.471 0.767 -0.065 0.047  -0.068 108 ARG DDD CD  
4972  N NE  . ARG D 108 ? 0.699 0.479 0.779 -0.064 0.046  -0.066 108 ARG DDD NE  
4973  C CZ  . ARG D 108 ? 0.728 0.502 0.805 -0.050 0.035  -0.057 108 ARG DDD CZ  
4974  N NH1 . ARG D 108 ? 0.733 0.540 0.841 -0.039 0.024  -0.049 108 ARG DDD NH1 
4975  N NH2 . ARG D 108 ? 0.769 0.504 0.811 -0.049 0.035  -0.055 108 ARG DDD NH2 
4976  N N   . PRO D 109 ? 0.546 0.442 0.707 -0.091 0.071  -0.095 109 PRO DDD N   
4977  C CA  . PRO D 109 ? 0.525 0.441 0.707 -0.086 0.070  -0.094 109 PRO DDD CA  
4978  C C   . PRO D 109 ? 0.520 0.446 0.721 -0.074 0.062  -0.085 109 PRO DDD C   
4979  O O   . PRO D 109 ? 0.496 0.440 0.711 -0.074 0.058  -0.085 109 PRO DDD O   
4980  C CB  . PRO D 109 ? 0.521 0.425 0.692 -0.087 0.080  -0.098 109 PRO DDD CB  
4981  C CG  . PRO D 109 ? 0.547 0.423 0.689 -0.097 0.087  -0.102 109 PRO DDD CG  
4982  C CD  . PRO D 109 ? 0.558 0.430 0.694 -0.100 0.081  -0.100 109 PRO DDD CD  
4983  N N   . THR D 110 ? 0.543 0.456 0.741 -0.065 0.061  -0.079 110 THR DDD N   
4984  C CA  . THR D 110 ? 0.537 0.468 0.757 -0.055 0.054  -0.069 110 THR DDD CA  
4985  C C   . THR D 110 ? 0.514 0.458 0.741 -0.061 0.042  -0.067 110 THR DDD C   
4986  O O   . THR D 110 ? 0.515 0.480 0.761 -0.059 0.035  -0.061 110 THR DDD O   
4987  C CB  . THR D 110 ? 0.570 0.487 0.782 -0.041 0.054  -0.063 110 THR DDD CB  
4988  O OG1 . THR D 110 ? 0.616 0.508 0.805 -0.044 0.051  -0.063 110 THR DDD OG1 
4989  C CG2 . THR D 110 ? 0.587 0.486 0.788 -0.032 0.067  -0.064 110 THR DDD CG2 
4990  N N   . GLU D 111 ? 0.524 0.457 0.736 -0.070 0.039  -0.071 111 GLU DDD N   
4991  C CA  . GLU D 111 ? 0.514 0.452 0.725 -0.075 0.028  -0.068 111 GLU DDD CA  
4992  C C   . GLU D 111 ? 0.511 0.460 0.726 -0.080 0.029  -0.072 111 GLU DDD C   
4993  O O   . GLU D 111 ? 0.526 0.472 0.735 -0.085 0.021  -0.070 111 GLU DDD O   
4994  C CB  . GLU D 111 ? 0.528 0.446 0.717 -0.080 0.027  -0.071 111 GLU DDD CB  
4995  C CG  . GLU D 111 ? 0.547 0.448 0.726 -0.075 0.024  -0.066 111 GLU DDD CG  
4996  C CD  . GLU D 111 ? 0.551 0.460 0.738 -0.072 0.010  -0.057 111 GLU DDD CD  
4997  O OE1 . GLU D 111 ? 0.525 0.456 0.733 -0.066 0.007  -0.052 111 GLU DDD OE1 
4998  O OE2 . GLU D 111 ? 0.588 0.483 0.759 -0.076 0.002  -0.054 111 GLU DDD OE2 
4999  N N   . TYR D 112 ? 0.511 0.467 0.733 -0.078 0.037  -0.077 112 TYR DDD N   
5000  C CA  . TYR D 112 ? 0.499 0.461 0.719 -0.080 0.038  -0.080 112 TYR DDD CA  
5001  C C   . TYR D 112 ? 0.488 0.461 0.723 -0.079 0.041  -0.078 112 TYR DDD C   
5002  O O   . TYR D 112 ? 0.476 0.453 0.719 -0.075 0.049  -0.079 112 TYR DDD O   
5003  C CB  . TYR D 112 ? 0.486 0.448 0.696 -0.080 0.044  -0.089 112 TYR DDD CB  
5004  C CG  . TYR D 112 ? 0.487 0.443 0.683 -0.082 0.043  -0.091 112 TYR DDD CG  
5005  C CD1 . TYR D 112 ? 0.488 0.437 0.680 -0.085 0.047  -0.093 112 TYR DDD CD1 
5006  C CD2 . TYR D 112 ? 0.492 0.446 0.675 -0.080 0.040  -0.093 112 TYR DDD CD2 
5007  C CE1 . TYR D 112 ? 0.501 0.446 0.680 -0.089 0.047  -0.096 112 TYR DDD CE1 
5008  C CE2 . TYR D 112 ? 0.504 0.455 0.675 -0.081 0.040  -0.096 112 TYR DDD CE2 
5009  C CZ  . TYR D 112 ? 0.498 0.446 0.668 -0.087 0.044  -0.097 112 TYR DDD CZ  
5010  O OH  . TYR D 112 ? 0.498 0.443 0.655 -0.090 0.047  -0.100 112 TYR DDD OH  
5011  N N   . GLU D 113 ? 0.495 0.472 0.731 -0.084 0.036  -0.074 113 GLU DDD N   
5012  C CA  . GLU D 113 ? 0.497 0.487 0.748 -0.085 0.040  -0.071 113 GLU DDD CA  
5013  C C   . GLU D 113 ? 0.507 0.492 0.751 -0.083 0.048  -0.077 113 GLU DDD C   
5014  O O   . GLU D 113 ? 0.538 0.532 0.794 -0.080 0.055  -0.077 113 GLU DDD O   
5015  C CB  . GLU D 113 ? 0.525 0.520 0.775 -0.096 0.032  -0.066 113 GLU DDD CB  
5016  C CG  . GLU D 113 ? 0.552 0.566 0.819 -0.100 0.037  -0.063 113 GLU DDD CG  
5017  C CD  . GLU D 113 ? 0.588 0.612 0.856 -0.116 0.030  -0.058 113 GLU DDD CD  
5018  O OE1 . GLU D 113 ? 0.654 0.667 0.908 -0.124 0.020  -0.056 113 GLU DDD OE1 
5019  O OE2 . GLU D 113 ? 0.627 0.669 0.907 -0.123 0.036  -0.056 113 GLU DDD OE2 
5020  N N   . PHE D 114 ? 0.513 0.486 0.737 -0.082 0.047  -0.082 114 PHE DDD N   
5021  C CA  . PHE D 114 ? 0.513 0.480 0.725 -0.079 0.052  -0.087 114 PHE DDD CA  
5022  C C   . PHE D 114 ? 0.513 0.483 0.721 -0.073 0.055  -0.094 114 PHE DDD C   
5023  O O   . PHE D 114 ? 0.523 0.495 0.725 -0.071 0.052  -0.097 114 PHE DDD O   
5024  C CB  . PHE D 114 ? 0.523 0.471 0.710 -0.081 0.048  -0.087 114 PHE DDD CB  
5025  C CG  . PHE D 114 ? 0.529 0.474 0.716 -0.093 0.045  -0.081 114 PHE DDD CG  
5026  C CD1 . PHE D 114 ? 0.510 0.465 0.711 -0.099 0.050  -0.079 114 PHE DDD CD1 
5027  C CD2 . PHE D 114 ? 0.527 0.461 0.702 -0.101 0.036  -0.078 114 PHE DDD CD2 
5028  C CE1 . PHE D 114 ? 0.502 0.463 0.706 -0.114 0.048  -0.074 114 PHE DDD CE1 
5029  C CE2 . PHE D 114 ? 0.522 0.457 0.697 -0.116 0.033  -0.072 114 PHE DDD CE2 
5030  C CZ  . PHE D 114 ? 0.520 0.471 0.711 -0.123 0.039  -0.070 114 PHE DDD CZ  
5031  N N   . TRP D 115 ? 0.532 0.504 0.741 -0.071 0.062  -0.098 115 TRP DDD N   
5032  C CA  . TRP D 115 ? 0.523 0.502 0.728 -0.069 0.065  -0.105 115 TRP DDD CA  
5033  C C   . TRP D 115 ? 0.502 0.479 0.694 -0.065 0.067  -0.109 115 TRP DDD C   
5034  O O   . TRP D 115 ? 0.459 0.427 0.651 -0.066 0.071  -0.107 115 TRP DDD O   
5035  C CB  . TRP D 115 ? 0.529 0.508 0.744 -0.072 0.072  -0.104 115 TRP DDD CB  
5036  C CG  . TRP D 115 ? 0.551 0.528 0.771 -0.074 0.070  -0.101 115 TRP DDD CG  
5037  C CD1 . TRP D 115 ? 0.532 0.508 0.762 -0.073 0.067  -0.094 115 TRP DDD CD1 
5038  C CD2 . TRP D 115 ? 0.546 0.524 0.759 -0.079 0.070  -0.105 115 TRP DDD CD2 
5039  N NE1 . TRP D 115 ? 0.539 0.510 0.767 -0.075 0.065  -0.093 115 TRP DDD NE1 
5040  C CE2 . TRP D 115 ? 0.559 0.530 0.776 -0.079 0.068  -0.100 115 TRP DDD CE2 
5041  C CE3 . TRP D 115 ? 0.562 0.548 0.767 -0.085 0.072  -0.113 115 TRP DDD CE3 
5042  C CZ2 . TRP D 115 ? 0.571 0.535 0.779 -0.084 0.068  -0.102 115 TRP DDD CZ2 
5043  C CZ3 . TRP D 115 ? 0.586 0.571 0.784 -0.092 0.074  -0.116 115 TRP DDD CZ3 
5044  C CH2 . TRP D 115 ? 0.587 0.558 0.785 -0.092 0.072  -0.110 115 TRP DDD CH2 
5045  N N   . GLY D 116 ? 0.494 0.481 0.676 -0.060 0.063  -0.114 116 GLY DDD N   
5046  C CA  . GLY D 116 ? 0.507 0.498 0.677 -0.055 0.064  -0.119 116 GLY DDD CA  
5047  C C   . GLY D 116 ? 0.507 0.500 0.682 -0.063 0.070  -0.122 116 GLY DDD C   
5048  O O   . GLY D 116 ? 0.532 0.523 0.717 -0.070 0.074  -0.121 116 GLY DDD O   
5049  N N   . GLN D 117 ? 0.515 0.507 0.677 -0.060 0.071  -0.126 117 GLN DDD N   
5050  C CA  . GLN D 117 ? 0.516 0.505 0.676 -0.069 0.077  -0.130 117 GLN DDD CA  
5051  C C   . GLN D 117 ? 0.522 0.535 0.681 -0.077 0.074  -0.136 117 GLN DDD C   
5052  O O   . GLN D 117 ? 0.543 0.548 0.696 -0.088 0.079  -0.140 117 GLN DDD O   
5053  C CB  . GLN D 117 ? 0.514 0.491 0.656 -0.064 0.078  -0.131 117 GLN DDD CB  
5054  C CG  . GLN D 117 ? 0.524 0.478 0.663 -0.060 0.082  -0.126 117 GLN DDD CG  
5055  C CD  . GLN D 117 ? 0.524 0.469 0.678 -0.066 0.092  -0.121 117 GLN DDD CD  
5056  O OE1 . GLN D 117 ? 0.546 0.488 0.710 -0.065 0.093  -0.115 117 GLN DDD OE1 
5057  N NE2 . GLN D 117 ? 0.516 0.456 0.670 -0.071 0.099  -0.123 117 GLN DDD NE2 
5058  N N   . GLY D 118 ? 0.527 0.565 0.689 -0.072 0.066  -0.138 118 GLY DDD N   
5059  C CA  . GLY D 118 ? 0.539 0.609 0.703 -0.081 0.063  -0.145 118 GLY DDD CA  
5060  C C   . GLY D 118 ? 0.555 0.652 0.711 -0.077 0.057  -0.151 118 GLY DDD C   
5061  O O   . GLY D 118 ? 0.557 0.637 0.700 -0.071 0.056  -0.150 118 GLY DDD O   
5062  N N   . THR D 119 ? 0.561 0.700 0.723 -0.082 0.052  -0.156 119 THR DDD N   
5063  C CA  . THR D 119 ? 0.563 0.742 0.721 -0.079 0.044  -0.162 119 THR DDD CA  
5064  C C   . THR D 119 ? 0.557 0.772 0.722 -0.103 0.045  -0.169 119 THR DDD C   
5065  O O   . THR D 119 ? 0.571 0.794 0.746 -0.112 0.049  -0.169 119 THR DDD O   
5066  C CB  . THR D 119 ? 0.591 0.793 0.749 -0.051 0.037  -0.160 119 THR DDD CB  
5067  O OG1 . THR D 119 ? 0.614 0.848 0.765 -0.043 0.028  -0.164 119 THR DDD OG1 
5068  C CG2 . THR D 119 ? 0.583 0.817 0.757 -0.049 0.037  -0.160 119 THR DDD CG2 
5069  N N   . GLN D 120 ? 0.562 0.794 0.717 -0.116 0.041  -0.174 120 GLN DDD N   
5070  C CA  . GLN D 120 ? 0.557 0.823 0.713 -0.145 0.042  -0.182 120 GLN DDD CA  
5071  C C   . GLN D 120 ? 0.547 0.884 0.722 -0.139 0.034  -0.185 120 GLN DDD C   
5072  O O   . GLN D 120 ? 0.527 0.896 0.707 -0.114 0.025  -0.185 120 GLN DDD O   
5073  C CB  . GLN D 120 ? 0.560 0.821 0.696 -0.161 0.039  -0.187 120 GLN DDD CB  
5074  C CG  . GLN D 120 ? 0.571 0.855 0.699 -0.198 0.040  -0.195 120 GLN DDD CG  
5075  C CD  . GLN D 120 ? 0.578 0.813 0.692 -0.220 0.054  -0.195 120 GLN DDD CD  
5076  O OE1 . GLN D 120 ? 0.589 0.763 0.687 -0.216 0.062  -0.190 120 GLN DDD OE1 
5077  N NE2 . GLN D 120 ? 0.593 0.855 0.711 -0.243 0.057  -0.199 120 GLN DDD NE2 
5078  N N   . VAL D 121 ? 0.570 0.928 0.755 -0.159 0.040  -0.189 121 VAL DDD N   
5079  C CA  . VAL D 121 ? 0.589 1.024 0.791 -0.166 0.036  -0.194 121 VAL DDD CA  
5080  C C   . VAL D 121 ? 0.627 1.080 0.819 -0.209 0.038  -0.203 121 VAL DDD C   
5081  O O   . VAL D 121 ? 0.646 1.050 0.822 -0.233 0.049  -0.203 121 VAL DDD O   
5082  C CB  . VAL D 121 ? 0.572 1.015 0.789 -0.158 0.042  -0.192 121 VAL DDD CB  
5083  C CG1 . VAL D 121 ? 0.569 1.094 0.806 -0.168 0.041  -0.198 121 VAL DDD CG1 
5084  C CG2 . VAL D 121 ? 0.574 0.994 0.794 -0.119 0.040  -0.184 121 VAL DDD CG2 
5085  N N   . THR D 122 ? 0.631 1.150 0.830 -0.218 0.028  -0.209 122 THR DDD N   
5086  C CA  . THR D 122 ? 0.677 1.221 0.865 -0.263 0.029  -0.218 122 THR DDD CA  
5087  C C   . THR D 122 ? 0.678 1.320 0.893 -0.272 0.025  -0.224 122 THR DDD C   
5088  O O   . THR D 122 ? 0.655 1.361 0.892 -0.243 0.014  -0.223 122 THR DDD O   
5089  C CB  . THR D 122 ? 0.713 1.244 0.879 -0.272 0.021  -0.221 122 THR DDD CB  
5090  O OG1 . THR D 122 ? 0.756 1.196 0.898 -0.262 0.028  -0.215 122 THR DDD OG1 
5091  C CG2 . THR D 122 ? 0.745 1.295 0.891 -0.321 0.021  -0.230 122 THR DDD CG2 
5092  N N   . VAL D 123 ? 0.710 1.361 0.922 -0.308 0.035  -0.229 123 VAL DDD N   
5093  C CA  . VAL D 123 ? 0.721 1.469 0.958 -0.325 0.035  -0.235 123 VAL DDD CA  
5094  C C   . VAL D 123 ? 0.775 1.548 0.994 -0.379 0.033  -0.245 123 VAL DDD C   
5095  O O   . VAL D 123 ? 0.787 1.497 0.972 -0.416 0.045  -0.248 123 VAL DDD O   
5096  C CB  . VAL D 123 ? 0.698 1.435 0.943 -0.328 0.049  -0.234 123 VAL DDD CB  
5097  C CG1 . VAL D 123 ? 0.683 1.523 0.959 -0.336 0.049  -0.239 123 VAL DDD CG1 
5098  C CG2 . VAL D 123 ? 0.670 1.358 0.922 -0.281 0.050  -0.224 123 VAL DDD CG2 
5099  N N   . SER D 124 ? 0.829 1.683 1.062 -0.383 0.019  -0.250 124 SER DDD N   
5100  C CA  . SER D 124 ? 0.916 1.808 1.133 -0.437 0.015  -0.260 124 SER DDD CA  
5101  C C   . SER D 124 ? 1.007 1.981 1.245 -0.470 0.022  -0.267 124 SER DDD C   
5102  O O   . SER D 124 ? 1.002 2.022 1.274 -0.441 0.025  -0.264 124 SER DDD O   
5103  C CB  . SER D 124 ? 0.897 1.846 1.122 -0.426 -0.004 -0.262 124 SER DDD CB  
5104  O OG  . SER D 124 ? 0.864 1.910 1.134 -0.386 -0.014 -0.259 124 SER DDD OG  
5119  N N   . THR E 4   ? 1.512 1.489 1.058 -0.247 0.237  -0.002 333 THR EEE N   
5120  C CA  . THR E 4   ? 1.391 1.413 0.935 -0.259 0.238  -0.051 333 THR EEE CA  
5121  C C   . THR E 4   ? 1.264 1.290 0.829 -0.245 0.210  -0.075 333 THR EEE C   
5122  O O   . THR E 4   ? 1.197 1.226 0.798 -0.243 0.212  -0.118 333 THR EEE O   
5123  C CB  . THR E 4   ? 1.442 1.513 0.925 -0.278 0.248  -0.046 333 THR EEE CB  
5124  O OG1 . THR E 4   ? 1.442 1.520 0.885 -0.268 0.232  0.009  333 THR EEE OG1 
5125  C CG2 . THR E 4   ? 1.469 1.549 0.938 -0.299 0.284  -0.049 333 THR EEE CG2 
5126  N N   . ASN E 5   ? 1.207 1.235 0.752 -0.233 0.185  -0.044 334 ASN EEE N   
5127  C CA  . ASN E 5   ? 1.153 1.187 0.713 -0.222 0.158  -0.059 334 ASN EEE CA  
5128  C C   . ASN E 5   ? 1.053 1.041 0.670 -0.203 0.150  -0.063 334 ASN EEE C   
5129  O O   . ASN E 5   ? 0.997 0.952 0.625 -0.194 0.154  -0.033 334 ASN EEE O   
5130  C CB  . ASN E 5   ? 1.193 1.258 0.717 -0.216 0.136  -0.018 334 ASN EEE CB  
5131  C CG  . ASN E 5   ? 1.219 1.255 0.741 -0.197 0.139  0.041  334 ASN EEE CG  
5132  O OD1 . ASN E 5   ? 1.252 1.270 0.761 -0.203 0.164  0.060  334 ASN EEE OD1 
5133  N ND2 . ASN E 5   ? 1.227 1.252 0.765 -0.174 0.120  0.070  334 ASN EEE ND2 
5134  N N   . LEU E 6   ? 0.996 0.981 0.645 -0.198 0.141  -0.099 335 LEU EEE N   
5135  C CA  . LEU E 6   ? 0.970 0.925 0.671 -0.181 0.132  -0.103 335 LEU EEE CA  
5136  C C   . LEU E 6   ? 0.951 0.891 0.651 -0.166 0.109  -0.072 335 LEU EEE C   
5137  O O   . LEU E 6   ? 0.985 0.948 0.655 -0.167 0.095  -0.058 335 LEU EEE O   
5138  C CB  . LEU E 6   ? 0.973 0.930 0.706 -0.177 0.133  -0.142 335 LEU EEE CB  
5139  C CG  . LEU E 6   ? 1.019 0.988 0.768 -0.182 0.160  -0.172 335 LEU EEE CG  
5140  C CD1 . LEU E 6   ? 1.025 0.986 0.816 -0.169 0.165  -0.202 335 LEU EEE CD1 
5141  C CD2 . LEU E 6   ? 0.989 0.960 0.765 -0.182 0.172  -0.163 335 LEU EEE CD2 
5142  N N   . CYS E 7   ? 0.895 0.803 0.625 -0.155 0.107  -0.060 336 CYS EEE N   
5143  C CA  . CYS E 7   ? 0.899 0.788 0.636 -0.139 0.091  -0.034 336 CYS EEE CA  
5144  C C   . CYS E 7   ? 0.857 0.760 0.608 -0.133 0.070  -0.052 336 CYS EEE C   
5145  O O   . CYS E 7   ? 0.834 0.737 0.611 -0.134 0.071  -0.081 336 CYS EEE O   
5146  C CB  . CYS E 7   ? 0.896 0.749 0.663 -0.136 0.100  -0.031 336 CYS EEE CB  
5147  S SG  . CYS E 7   ? 0.984 0.806 0.734 -0.150 0.133  -0.010 336 CYS EEE SG  
5148  N N   . PRO E 8   ? 0.857 0.774 0.594 -0.125 0.052  -0.031 337 PRO EEE N   
5149  C CA  . PRO E 8   ? 0.849 0.784 0.594 -0.126 0.034  -0.049 337 PRO EEE CA  
5150  C C   . PRO E 8   ? 0.796 0.704 0.581 -0.112 0.025  -0.053 337 PRO EEE C   
5151  O O   . PRO E 8   ? 0.786 0.699 0.575 -0.103 0.011  -0.036 337 PRO EEE O   
5152  C CB  . PRO E 8   ? 0.881 0.856 0.595 -0.125 0.020  -0.018 337 PRO EEE CB  
5153  C CG  . PRO E 8   ? 0.879 0.830 0.595 -0.105 0.027  0.026  337 PRO EEE CG  
5154  C CD  . PRO E 8   ? 0.883 0.800 0.600 -0.113 0.051  0.015  337 PRO EEE CD  
5155  N N   . PHE E 9   ? 0.761 0.650 0.574 -0.111 0.035  -0.073 338 PHE EEE N   
5156  C CA  . PHE E 9   ? 0.725 0.598 0.573 -0.100 0.027  -0.075 338 PHE EEE CA  
5157  C C   . PHE E 9   ? 0.705 0.583 0.562 -0.098 0.015  -0.085 338 PHE EEE C   
5158  O O   . PHE E 9   ? 0.673 0.544 0.548 -0.089 0.003  -0.075 338 PHE EEE O   
5159  C CB  . PHE E 9   ? 0.726 0.599 0.603 -0.099 0.039  -0.089 338 PHE EEE CB  
5160  C CG  . PHE E 9   ? 0.746 0.612 0.620 -0.106 0.050  -0.080 338 PHE EEE CG  
5161  C CD1 . PHE E 9   ? 0.743 0.588 0.610 -0.104 0.050  -0.061 338 PHE EEE CD1 
5162  C CD2 . PHE E 9   ? 0.749 0.629 0.631 -0.115 0.067  -0.093 338 PHE EEE CD2 
5163  C CE1 . PHE E 9   ? 0.773 0.602 0.638 -0.115 0.068  -0.059 338 PHE EEE CE1 
5164  C CE2 . PHE E 9   ? 0.788 0.663 0.668 -0.128 0.081  -0.089 338 PHE EEE CE2 
5165  C CZ  . PHE E 9   ? 0.784 0.628 0.654 -0.130 0.083  -0.073 338 PHE EEE CZ  
5166  N N   . GLY E 10  ? 0.728 0.615 0.574 -0.110 0.020  -0.106 339 GLY EEE N   
5167  C CA  . GLY E 10  ? 0.712 0.601 0.562 -0.117 0.014  -0.121 339 GLY EEE CA  
5168  C C   . GLY E 10  ? 0.702 0.611 0.542 -0.117 -0.006 -0.101 339 GLY EEE C   
5169  O O   . GLY E 10  ? 0.658 0.560 0.518 -0.113 -0.014 -0.101 339 GLY EEE O   
5170  N N   . GLU E 11  ? 0.730 0.667 0.543 -0.118 -0.013 -0.080 340 GLU EEE N   
5171  C CA  . GLU E 11  ? 0.752 0.723 0.559 -0.113 -0.031 -0.054 340 GLU EEE CA  
5172  C C   . GLU E 11  ? 0.705 0.650 0.540 -0.090 -0.035 -0.032 340 GLU EEE C   
5173  O O   . GLU E 11  ? 0.716 0.685 0.559 -0.084 -0.048 -0.017 340 GLU EEE O   
5174  C CB  . GLU E 11  ? 0.826 0.835 0.601 -0.112 -0.034 -0.026 340 GLU EEE CB  
5175  C CG  . GLU E 11  ? 0.913 0.960 0.653 -0.139 -0.030 -0.049 340 GLU EEE CG  
5176  C CD  . GLU E 11  ? 1.015 1.112 0.719 -0.139 -0.034 -0.017 340 GLU EEE CD  
5177  O OE1 . GLU E 11  ? 1.090 1.197 0.800 -0.114 -0.041 0.029  340 GLU EEE OE1 
5178  O OE2 . GLU E 11  ? 1.050 1.177 0.721 -0.162 -0.027 -0.035 340 GLU EEE OE2 
5179  N N   . VAL E 12  ? 0.690 0.597 0.540 -0.081 -0.024 -0.034 341 VAL EEE N   
5180  C CA  . VAL E 12  ? 0.672 0.555 0.545 -0.067 -0.023 -0.022 341 VAL EEE CA  
5181  C C   . VAL E 12  ? 0.663 0.539 0.561 -0.068 -0.029 -0.039 341 VAL EEE C   
5182  O O   . VAL E 12  ? 0.706 0.588 0.616 -0.063 -0.038 -0.031 341 VAL EEE O   
5183  C CB  . VAL E 12  ? 0.658 0.513 0.533 -0.065 -0.006 -0.020 341 VAL EEE CB  
5184  C CG1 . VAL E 12  ? 0.647 0.481 0.541 -0.058 -0.002 -0.016 341 VAL EEE CG1 
5185  C CG2 . VAL E 12  ? 0.692 0.544 0.543 -0.063 0.005  0.002  341 VAL EEE CG2 
5186  N N   . PHE E 13  ? 0.646 0.512 0.554 -0.073 -0.021 -0.058 342 PHE EEE N   
5187  C CA  . PHE E 13  ? 0.627 0.485 0.562 -0.068 -0.022 -0.065 342 PHE EEE CA  
5188  C C   . PHE E 13  ? 0.631 0.489 0.569 -0.074 -0.026 -0.072 342 PHE EEE C   
5189  O O   . PHE E 13  ? 0.650 0.502 0.607 -0.069 -0.029 -0.068 342 PHE EEE O   
5190  C CB  . PHE E 13  ? 0.607 0.463 0.555 -0.065 -0.009 -0.075 342 PHE EEE CB  
5191  C CG  . PHE E 13  ? 0.576 0.441 0.529 -0.064 -0.006 -0.070 342 PHE EEE CG  
5192  C CD1 . PHE E 13  ? 0.554 0.431 0.526 -0.060 -0.010 -0.064 342 PHE EEE CD1 
5193  C CD2 . PHE E 13  ? 0.608 0.471 0.544 -0.072 0.003  -0.071 342 PHE EEE CD2 
5194  C CE1 . PHE E 13  ? 0.556 0.447 0.530 -0.068 -0.005 -0.066 342 PHE EEE CE1 
5195  C CE2 . PHE E 13  ? 0.604 0.471 0.544 -0.079 0.011  -0.070 342 PHE EEE CE2 
5196  C CZ  . PHE E 13  ? 0.562 0.445 0.521 -0.079 0.007  -0.071 342 PHE EEE CZ  
5197  N N   . ASN E 14  ? 0.654 0.521 0.573 -0.089 -0.024 -0.086 343 ASN EEE N   
5198  C CA  . ASN E 14  ? 0.696 0.563 0.614 -0.106 -0.021 -0.104 343 ASN EEE CA  
5199  C C   . ASN E 14  ? 0.676 0.585 0.573 -0.120 -0.036 -0.099 343 ASN EEE C   
5200  O O   . ASN E 14  ? 0.727 0.652 0.613 -0.145 -0.034 -0.121 343 ASN EEE O   
5201  C CB  . ASN E 14  ? 0.734 0.583 0.647 -0.118 -0.000 -0.133 343 ASN EEE CB  
5202  C CG  . ASN E 14  ? 0.753 0.567 0.696 -0.099 0.017  -0.133 343 ASN EEE CG  
5203  O OD1 . ASN E 14  ? 0.673 0.476 0.640 -0.085 0.013  -0.116 343 ASN EEE OD1 
5204  N ND2 . ASN E 14  ? 0.827 0.632 0.772 -0.097 0.035  -0.147 343 ASN EEE ND2 
5205  N N   . ALA E 15  ? 0.681 0.612 0.575 -0.106 -0.049 -0.072 344 ALA EEE N   
5206  C CA  . ALA E 15  ? 0.678 0.661 0.563 -0.110 -0.065 -0.056 344 ALA EEE CA  
5207  C C   . ALA E 15  ? 0.651 0.648 0.551 -0.126 -0.069 -0.069 344 ALA EEE C   
5208  O O   . ALA E 15  ? 0.630 0.589 0.552 -0.119 -0.063 -0.072 344 ALA EEE O   
5209  C CB  . ALA E 15  ? 0.661 0.646 0.554 -0.083 -0.069 -0.021 344 ALA EEE CB  
5210  N N   . THR E 16  ? 0.671 0.725 0.559 -0.148 -0.079 -0.075 345 THR EEE N   
5211  C CA  . THR E 16  ? 0.679 0.756 0.579 -0.173 -0.081 -0.092 345 THR EEE CA  
5212  C C   . THR E 16  ? 0.662 0.752 0.589 -0.151 -0.092 -0.063 345 THR EEE C   
5213  O O   . THR E 16  ? 0.699 0.777 0.644 -0.163 -0.087 -0.074 345 THR EEE O   
5214  C CB  . THR E 16  ? 0.694 0.844 0.569 -0.209 -0.089 -0.110 345 THR EEE CB  
5215  O OG1 . THR E 16  ? 0.677 0.890 0.540 -0.190 -0.106 -0.074 345 THR EEE OG1 
5216  C CG2 . THR E 16  ? 0.748 0.876 0.597 -0.238 -0.071 -0.150 345 THR EEE CG2 
5217  N N   . ARG E 17  ? 0.635 0.743 0.566 -0.120 -0.099 -0.029 346 ARG EEE N   
5218  C CA  . ARG E 17  ? 0.619 0.733 0.576 -0.095 -0.102 -0.003 346 ARG EEE CA  
5219  C C   . ARG E 17  ? 0.584 0.639 0.545 -0.067 -0.091 0.010  346 ARG EEE C   
5220  O O   . ARG E 17  ? 0.587 0.625 0.531 -0.059 -0.086 0.016  346 ARG EEE O   
5221  C CB  . ARG E 17  ? 0.650 0.844 0.612 -0.082 -0.115 0.028  346 ARG EEE CB  
5222  C CG  . ARG E 17  ? 0.686 0.928 0.677 -0.084 -0.122 0.035  346 ARG EEE CG  
5223  C CD  . ARG E 17  ? 0.735 1.050 0.743 -0.055 -0.129 0.077  346 ARG EEE CD  
5224  N NE  . ARG E 17  ? 0.807 1.214 0.799 -0.071 -0.146 0.085  346 ARG EEE NE  
5225  C CZ  . ARG E 17  ? 0.836 1.332 0.833 -0.103 -0.161 0.072  346 ARG EEE CZ  
5226  N NH1 . ARG E 17  ? 0.839 1.335 0.858 -0.121 -0.159 0.053  346 ARG EEE NH1 
5227  N NH2 . ARG E 17  ? 0.871 1.461 0.848 -0.119 -0.177 0.080  346 ARG EEE NH2 
5228  N N   . PHE E 18  ? 0.579 0.437 0.495 -0.055 -0.035 -0.062 347 PHE EEE N   
5229  C CA  . PHE E 18  ? 0.576 0.446 0.505 -0.046 -0.034 -0.055 347 PHE EEE CA  
5230  C C   . PHE E 18  ? 0.575 0.468 0.521 -0.049 -0.040 -0.055 347 PHE EEE C   
5231  O O   . PHE E 18  ? 0.610 0.508 0.560 -0.059 -0.041 -0.058 347 PHE EEE O   
5232  C CB  . PHE E 18  ? 0.596 0.455 0.525 -0.041 -0.027 -0.051 347 PHE EEE CB  
5233  C CG  . PHE E 18  ? 0.581 0.429 0.504 -0.031 -0.022 -0.049 347 PHE EEE CG  
5234  C CD1 . PHE E 18  ? 0.614 0.442 0.523 -0.032 -0.019 -0.055 347 PHE EEE CD1 
5235  C CD2 . PHE E 18  ? 0.590 0.447 0.521 -0.022 -0.020 -0.045 347 PHE EEE CD2 
5236  C CE1 . PHE E 18  ? 0.638 0.458 0.543 -0.022 -0.013 -0.055 347 PHE EEE CE1 
5237  C CE2 . PHE E 18  ? 0.596 0.445 0.523 -0.013 -0.015 -0.044 347 PHE EEE CE2 
5238  C CZ  . PHE E 18  ? 0.607 0.438 0.522 -0.013 -0.011 -0.049 347 PHE EEE CZ  
5239  N N   . ALA E 19  ? 0.553 0.460 0.514 -0.042 -0.042 -0.052 348 ALA EEE N   
5240  C CA  . ALA E 19  ? 0.543 0.472 0.525 -0.043 -0.046 -0.054 348 ALA EEE CA  
5241  C C   . ALA E 19  ? 0.539 0.479 0.532 -0.046 -0.042 -0.056 348 ALA EEE C   
5242  O O   . ALA E 19  ? 0.544 0.477 0.529 -0.043 -0.036 -0.053 348 ALA EEE O   
5243  C CB  . ALA E 19  ? 0.545 0.482 0.542 -0.035 -0.048 -0.050 348 ALA EEE CB  
5244  N N   . SER E 20  ? 0.540 0.500 0.550 -0.051 -0.044 -0.061 349 SER EEE N   
5245  C CA  . SER E 20  ? 0.528 0.509 0.554 -0.052 -0.040 -0.065 349 SER EEE CA  
5246  C C   . SER E 20  ? 0.528 0.515 0.567 -0.042 -0.037 -0.067 349 SER EEE C   
5247  O O   . SER E 20  ? 0.543 0.526 0.592 -0.036 -0.041 -0.066 349 SER EEE O   
5248  C CB  . SER E 20  ? 0.510 0.513 0.555 -0.058 -0.042 -0.072 349 SER EEE CB  
5249  O OG  . SER E 20  ? 0.551 0.551 0.584 -0.069 -0.042 -0.072 349 SER EEE OG  
5250  N N   . VAL E 21  ? 0.511 0.510 0.553 -0.042 -0.032 -0.071 350 VAL EEE N   
5251  C CA  . VAL E 21  ? 0.510 0.518 0.567 -0.035 -0.029 -0.076 350 VAL EEE CA  
5252  C C   . VAL E 21  ? 0.517 0.537 0.605 -0.032 -0.030 -0.085 350 VAL EEE C   
5253  O O   . VAL E 21  ? 0.549 0.563 0.649 -0.026 -0.029 -0.084 350 VAL EEE O   
5254  C CB  . VAL E 21  ? 0.508 0.534 0.562 -0.037 -0.023 -0.080 350 VAL EEE CB  
5255  C CG1 . VAL E 21  ? 0.515 0.569 0.580 -0.045 -0.021 -0.089 350 VAL EEE CG1 
5256  C CG2 . VAL E 21  ? 0.492 0.526 0.557 -0.031 -0.020 -0.086 350 VAL EEE CG2 
5257  N N   . TYR E 22  ? 0.498 0.535 0.601 -0.037 -0.032 -0.091 351 TYR EEE N   
5258  C CA  . TYR E 22  ? 0.487 0.537 0.627 -0.033 -0.032 -0.100 351 TYR EEE CA  
5259  C C   . TYR E 22  ? 0.488 0.520 0.632 -0.026 -0.039 -0.089 351 TYR EEE C   
5260  O O   . TYR E 22  ? 0.499 0.532 0.672 -0.019 -0.039 -0.090 351 TYR EEE O   
5261  C CB  . TYR E 22  ? 0.466 0.541 0.623 -0.039 -0.032 -0.111 351 TYR EEE CB  
5262  C CG  . TYR E 22  ? 0.471 0.543 0.626 -0.041 -0.039 -0.104 351 TYR EEE CG  
5263  C CD1 . TYR E 22  ? 0.480 0.543 0.606 -0.050 -0.041 -0.097 351 TYR EEE CD1 
5264  C CD2 . TYR E 22  ? 0.462 0.538 0.645 -0.035 -0.045 -0.104 351 TYR EEE CD2 
5265  C CE1 . TYR E 22  ? 0.472 0.534 0.596 -0.053 -0.049 -0.092 351 TYR EEE CE1 
5266  C CE2 . TYR E 22  ? 0.478 0.555 0.659 -0.037 -0.054 -0.097 351 TYR EEE CE2 
5267  C CZ  . TYR E 22  ? 0.485 0.556 0.636 -0.047 -0.056 -0.093 351 TYR EEE CZ  
5268  O OH  . TYR E 22  ? 0.477 0.553 0.627 -0.050 -0.064 -0.089 351 TYR EEE OH  
5269  N N   . ALA E 23  ? 0.498 0.514 0.615 -0.028 -0.045 -0.078 352 ALA EEE N   
5270  C CA  . ALA E 23  ? 0.512 0.515 0.624 -0.024 -0.052 -0.065 352 ALA EEE CA  
5271  C C   . ALA E 23  ? 0.502 0.484 0.587 -0.022 -0.050 -0.057 352 ALA EEE C   
5272  O O   . ALA E 23  ? 0.542 0.514 0.605 -0.024 -0.055 -0.049 352 ALA EEE O   
5273  C CB  . ALA E 23  ? 0.486 0.497 0.592 -0.030 -0.060 -0.063 352 ALA EEE CB  
5274  N N   . TRP E 24  ? 0.474 0.452 0.561 -0.019 -0.043 -0.060 353 TRP EEE N   
5275  C CA  . TRP E 24  ? 0.492 0.453 0.555 -0.017 -0.039 -0.054 353 TRP EEE CA  
5276  C C   . TRP E 24  ? 0.496 0.445 0.551 -0.013 -0.043 -0.042 353 TRP EEE C   
5277  O O   . TRP E 24  ? 0.534 0.487 0.610 -0.009 -0.046 -0.037 353 TRP EEE O   
5278  C CB  . TRP E 24  ? 0.478 0.444 0.551 -0.014 -0.032 -0.060 353 TRP EEE CB  
5279  C CG  . TRP E 24  ? 0.475 0.450 0.583 -0.010 -0.030 -0.065 353 TRP EEE CG  
5280  C CD1 . TRP E 24  ? 0.468 0.462 0.603 -0.012 -0.028 -0.078 353 TRP EEE CD1 
5281  C CD2 . TRP E 24  ? 0.466 0.431 0.586 -0.005 -0.028 -0.059 353 TRP EEE CD2 
5282  N NE1 . TRP E 24  ? 0.494 0.488 0.660 -0.007 -0.024 -0.082 353 TRP EEE NE1 
5283  C CE2 . TRP E 24  ? 0.474 0.449 0.631 -0.004 -0.024 -0.068 353 TRP EEE CE2 
5284  C CE3 . TRP E 24  ? 0.462 0.411 0.565 -0.003 -0.027 -0.046 353 TRP EEE CE3 
5285  C CZ2 . TRP E 24  ? 0.474 0.440 0.655 0.000  -0.021 -0.064 353 TRP EEE CZ2 
5286  C CZ3 . TRP E 24  ? 0.461 0.404 0.584 0.001  -0.024 -0.041 353 TRP EEE CZ3 
5287  C CH2 . TRP E 24  ? 0.476 0.426 0.638 0.002  -0.021 -0.049 353 TRP EEE CH2 
5288  N N   . ASN E 25  ? 0.507 0.443 0.533 -0.014 -0.043 -0.038 354 ASN EEE N   
5289  C CA  . ASN E 25  ? 0.510 0.437 0.520 -0.013 -0.046 -0.028 354 ASN EEE CA  
5290  C C   . ASN E 25  ? 0.527 0.447 0.539 -0.008 -0.038 -0.024 354 ASN EEE C   
5291  O O   . ASN E 25  ? 0.543 0.460 0.553 -0.007 -0.032 -0.030 354 ASN EEE O   
5292  C CB  . ASN E 25  ? 0.527 0.446 0.508 -0.019 -0.047 -0.031 354 ASN EEE CB  
5293  C CG  . ASN E 25  ? 0.583 0.498 0.544 -0.019 -0.049 -0.024 354 ASN EEE CG  
5294  O OD1 . ASN E 25  ? 0.637 0.543 0.585 -0.017 -0.043 -0.023 354 ASN EEE OD1 
5295  N ND2 . ASN E 25  ? 0.626 0.552 0.586 -0.022 -0.058 -0.018 354 ASN EEE ND2 
5296  N N   . ARG E 26  ? 0.530 0.450 0.547 -0.006 -0.040 -0.012 355 ARG EEE N   
5297  C CA  . ARG E 26  ? 0.537 0.451 0.553 -0.002 -0.034 -0.004 355 ARG EEE CA  
5298  C C   . ARG E 26  ? 0.571 0.482 0.557 -0.005 -0.035 0.004  355 ARG EEE C   
5299  O O   . ARG E 26  ? 0.569 0.487 0.551 -0.006 -0.043 0.015  355 ARG EEE O   
5300  C CB  . ARG E 26  ? 0.537 0.453 0.579 0.001  -0.035 0.009  355 ARG EEE CB  
5301  C CG  . ARG E 26  ? 0.538 0.455 0.615 0.004  -0.029 0.003  355 ARG EEE CG  
5302  C CD  . ARG E 26  ? 0.521 0.431 0.608 0.005  -0.021 0.011  355 ARG EEE CD  
5303  N NE  . ARG E 26  ? 0.525 0.439 0.628 0.004  -0.013 -0.006 355 ARG EEE NE  
5304  C CZ  . ARG E 26  ? 0.483 0.398 0.620 0.005  -0.008 -0.012 355 ARG EEE CZ  
5305  N NH1 . ARG E 26  ? 0.511 0.420 0.674 0.006  -0.007 -0.001 355 ARG EEE NH1 
5306  N NH2 . ARG E 26  ? 0.467 0.392 0.613 0.003  -0.002 -0.030 355 ARG EEE NH2 
5307  N N   . LYS E 27  ? 0.583 0.488 0.552 -0.005 -0.027 0.001  356 LYS EEE N   
5308  C CA  . LYS E 27  ? 0.628 0.532 0.570 -0.007 -0.025 0.009  356 LYS EEE CA  
5309  C C   . LYS E 27  ? 0.610 0.513 0.563 -0.004 -0.016 0.017  356 LYS EEE C   
5310  O O   . LYS E 27  ? 0.623 0.523 0.588 -0.002 -0.009 0.009  356 LYS EEE O   
5311  C CB  . LYS E 27  ? 0.676 0.574 0.591 -0.010 -0.022 -0.004 356 LYS EEE CB  
5312  C CG  . LYS E 27  ? 0.757 0.655 0.666 -0.014 -0.030 -0.013 356 LYS EEE CG  
5313  C CD  . LYS E 27  ? 0.836 0.725 0.722 -0.018 -0.025 -0.026 356 LYS EEE CD  
5314  C CE  . LYS E 27  ? 0.830 0.717 0.712 -0.024 -0.032 -0.035 356 LYS EEE CE  
5315  N NZ  . LYS E 27  ? 0.840 0.720 0.740 -0.021 -0.030 -0.038 356 LYS EEE NZ  
5316  N N   . ARG E 28  ? 0.613 0.521 0.562 -0.006 -0.018 0.034  357 ARG EEE N   
5317  C CA  . ARG E 28  ? 0.617 0.525 0.572 -0.006 -0.008 0.044  357 ARG EEE CA  
5318  C C   . ARG E 28  ? 0.605 0.515 0.530 -0.008 0.000  0.038  357 ARG EEE C   
5319  O O   . ARG E 28  ? 0.614 0.530 0.510 -0.012 -0.004 0.036  357 ARG EEE O   
5320  C CB  . ARG E 28  ? 0.660 0.573 0.622 -0.006 -0.013 0.068  357 ARG EEE CB  
5321  C CG  . ARG E 28  ? 0.738 0.648 0.713 -0.007 -0.002 0.081  357 ARG EEE CG  
5322  C CD  . ARG E 28  ? 0.822 0.735 0.807 -0.006 -0.008 0.108  357 ARG EEE CD  
5323  N NE  . ARG E 28  ? 0.927 0.840 0.910 -0.010 0.002  0.126  357 ARG EEE NE  
5324  C CZ  . ARG E 28  ? 0.984 0.887 1.000 -0.010 0.010  0.135  357 ARG EEE CZ  
5325  N NH1 . ARG E 28  ? 1.025 0.918 1.082 -0.006 0.009  0.127  357 ARG EEE NH1 
5326  N NH2 . ARG E 28  ? 0.981 0.887 0.992 -0.015 0.020  0.153  357 ARG EEE NH2 
5327  N N   . ILE E 29  ? 0.615 0.522 0.547 -0.007 0.012  0.032  358 ILE EEE N   
5328  C CA  . ILE E 29  ? 0.637 0.548 0.547 -0.009 0.022  0.025  358 ILE EEE CA  
5329  C C   . ILE E 29  ? 0.652 0.569 0.568 -0.012 0.031  0.040  358 ILE EEE C   
5330  O O   . ILE E 29  ? 0.674 0.587 0.620 -0.010 0.035  0.043  358 ILE EEE O   
5331  C CB  . ILE E 29  ? 0.641 0.547 0.556 -0.004 0.027  0.006  358 ILE EEE CB  
5332  C CG1 . ILE E 29  ? 0.656 0.555 0.560 -0.003 0.019  -0.005 358 ILE EEE CG1 
5333  C CG2 . ILE E 29  ? 0.642 0.553 0.542 -0.004 0.039  -0.001 358 ILE EEE CG2 
5334  C CD1 . ILE E 29  ? 0.692 0.585 0.606 0.003  0.021  -0.019 358 ILE EEE CD1 
5335  N N   . SER E 30  ? 0.666 0.593 0.555 -0.017 0.034  0.050  359 SER EEE N   
5336  C CA  . SER E 30  ? 0.717 0.652 0.608 -0.021 0.043  0.068  359 SER EEE CA  
5337  C C   . SER E 30  ? 0.754 0.705 0.608 -0.027 0.050  0.068  359 SER EEE C   
5338  O O   . SER E 30  ? 0.740 0.695 0.567 -0.028 0.044  0.058  359 SER EEE O   
5339  C CB  . SER E 30  ? 0.730 0.662 0.637 -0.022 0.036  0.093  359 SER EEE CB  
5340  O OG  . SER E 30  ? 0.744 0.682 0.635 -0.022 0.022  0.098  359 SER EEE OG  
5341  N N   . ASN E 31  ? 0.807 0.766 0.661 -0.032 0.062  0.080  360 ASN EEE N   
5342  C CA  . ASN E 31  ? 0.851 0.830 0.669 -0.040 0.071  0.083  360 ASN EEE CA  
5343  C C   . ASN E 31  ? 0.817 0.800 0.616 -0.038 0.075  0.053  360 ASN EEE C   
5344  O O   . ASN E 31  ? 0.805 0.799 0.571 -0.042 0.070  0.048  360 ASN EEE O   
5345  C CB  . ASN E 31  ? 0.913 0.906 0.708 -0.045 0.061  0.108  360 ASN EEE CB  
5346  C CG  . ASN E 31  ? 0.977 0.962 0.799 -0.045 0.057  0.139  360 ASN EEE CG  
5347  O OD1 . ASN E 31  ? 1.025 1.007 0.852 -0.042 0.042  0.152  360 ASN EEE OD1 
5348  N ND2 . ASN E 31  ? 0.999 0.979 0.845 -0.047 0.070  0.148  360 ASN EEE ND2 
5349  N N   . CYS E 32  ? 0.786 0.759 0.605 -0.031 0.082  0.035  361 CYS EEE N   
5350  C CA  . CYS E 32  ? 0.799 0.770 0.608 -0.027 0.086  0.007  361 CYS EEE CA  
5351  C C   . CYS E 32  ? 0.755 0.724 0.591 -0.020 0.097  -0.006 361 CYS EEE C   
5352  O O   . CYS E 32  ? 0.744 0.708 0.608 -0.019 0.097  0.004  361 CYS EEE O   
5353  C CB  . CYS E 32  ? 0.790 0.747 0.596 -0.023 0.073  -0.004 361 CYS EEE CB  
5354  S SG  . CYS E 32  ? 0.793 0.731 0.635 -0.016 0.061  0.002  361 CYS EEE SG  
5355  N N   . VAL E 33  ? 0.737 0.710 0.565 -0.016 0.106  -0.027 362 VAL EEE N   
5356  C CA  . VAL E 33  ? 0.727 0.699 0.580 -0.008 0.115  -0.042 362 VAL EEE CA  
5357  C C   . VAL E 33  ? 0.719 0.673 0.588 0.002  0.105  -0.052 362 VAL EEE C   
5358  O O   . VAL E 33  ? 0.693 0.637 0.546 0.004  0.100  -0.062 362 VAL EEE O   
5359  C CB  . VAL E 33  ? 0.737 0.723 0.578 -0.007 0.131  -0.060 362 VAL EEE CB  
5360  C CG1 . VAL E 33  ? 0.717 0.706 0.587 0.004  0.139  -0.073 362 VAL EEE CG1 
5361  C CG2 . VAL E 33  ? 0.760 0.769 0.581 -0.019 0.142  -0.050 362 VAL EEE CG2 
5362  N N   . ALA E 34  ? 0.716 0.667 0.614 0.008  0.101  -0.048 363 ALA EEE N   
5363  C CA  . ALA E 34  ? 0.715 0.652 0.628 0.016  0.092  -0.054 363 ALA EEE CA  
5364  C C   . ALA E 34  ? 0.716 0.657 0.641 0.027  0.099  -0.069 363 ALA EEE C   
5365  O O   . ALA E 34  ? 0.765 0.719 0.713 0.031  0.104  -0.070 363 ALA EEE O   
5366  C CB  . ALA E 34  ? 0.684 0.623 0.622 0.016  0.085  -0.044 363 ALA EEE CB  
5367  N N   . ASP E 35  ? 0.726 0.656 0.637 0.031  0.100  -0.081 364 ASP EEE N   
5368  C CA  . ASP E 35  ? 0.737 0.664 0.663 0.044  0.106  -0.095 364 ASP EEE CA  
5369  C C   . ASP E 35  ? 0.701 0.613 0.639 0.052  0.094  -0.092 364 ASP EEE C   
5370  O O   . ASP E 35  ? 0.697 0.590 0.621 0.049  0.088  -0.094 364 ASP EEE O   
5371  C CB  . ASP E 35  ? 0.784 0.706 0.694 0.045  0.116  -0.111 364 ASP EEE CB  
5372  C CG  . ASP E 35  ? 0.792 0.719 0.726 0.059  0.125  -0.124 364 ASP EEE CG  
5373  O OD1 . ASP E 35  ? 0.767 0.699 0.726 0.068  0.121  -0.117 364 ASP EEE OD1 
5374  O OD2 . ASP E 35  ? 0.851 0.781 0.779 0.060  0.137  -0.140 364 ASP EEE OD2 
5375  N N   . TYR E 36  ? 0.690 0.612 0.653 0.060  0.092  -0.088 365 TYR EEE N   
5376  C CA  . TYR E 36  ? 0.687 0.603 0.662 0.066  0.080  -0.082 365 TYR EEE CA  
5377  C C   . TYR E 36  ? 0.713 0.620 0.699 0.081  0.083  -0.088 365 TYR EEE C   
5378  O O   . TYR E 36  ? 0.707 0.609 0.702 0.087  0.075  -0.081 365 TYR EEE O   
5379  C CB  . TYR E 36  ? 0.663 0.599 0.658 0.066  0.076  -0.075 365 TYR EEE CB  
5380  C CG  . TYR E 36  ? 0.632 0.570 0.622 0.054  0.071  -0.068 365 TYR EEE CG  
5381  C CD1 . TYR E 36  ? 0.611 0.540 0.597 0.050  0.060  -0.062 365 TYR EEE CD1 
5382  C CD2 . TYR E 36  ? 0.603 0.552 0.594 0.046  0.079  -0.066 365 TYR EEE CD2 
5383  C CE1 . TYR E 36  ? 0.617 0.547 0.603 0.040  0.056  -0.056 365 TYR EEE CE1 
5384  C CE2 . TYR E 36  ? 0.590 0.538 0.580 0.035  0.075  -0.057 365 TYR EEE CE2 
5385  C CZ  . TYR E 36  ? 0.583 0.521 0.572 0.033  0.064  -0.053 365 TYR EEE CZ  
5386  O OH  . TYR E 36  ? 0.588 0.526 0.582 0.025  0.060  -0.045 365 TYR EEE OH  
5387  N N   . SER E 37  ? 0.737 0.643 0.723 0.086  0.095  -0.101 366 SER EEE N   
5388  C CA  . SER E 37  ? 0.758 0.656 0.762 0.101  0.099  -0.106 366 SER EEE CA  
5389  C C   . SER E 37  ? 0.771 0.638 0.767 0.102  0.093  -0.106 366 SER EEE C   
5390  O O   . SER E 37  ? 0.790 0.646 0.803 0.115  0.091  -0.101 366 SER EEE O   
5391  C CB  . SER E 37  ? 0.795 0.700 0.806 0.107  0.115  -0.122 366 SER EEE CB  
5392  O OG  . SER E 37  ? 0.825 0.734 0.813 0.094  0.123  -0.131 366 SER EEE OG  
5393  N N   . VAL E 38  ? 0.793 0.645 0.764 0.089  0.090  -0.107 367 VAL EEE N   
5394  C CA  . VAL E 38  ? 0.782 0.606 0.745 0.086  0.084  -0.106 367 VAL EEE CA  
5395  C C   . VAL E 38  ? 0.790 0.615 0.764 0.090  0.072  -0.088 367 VAL EEE C   
5396  O O   . VAL E 38  ? 0.853 0.661 0.838 0.098  0.070  -0.084 367 VAL EEE O   
5397  C CB  . VAL E 38  ? 0.800 0.617 0.735 0.070  0.082  -0.112 367 VAL EEE CB  
5398  C CG1 . VAL E 38  ? 0.800 0.633 0.726 0.060  0.072  -0.099 367 VAL EEE CG1 
5399  C CG2 . VAL E 38  ? 0.786 0.575 0.716 0.066  0.080  -0.118 367 VAL EEE CG2 
5400  N N   . LEU E 39  ? 0.737 0.585 0.712 0.086  0.065  -0.079 368 LEU EEE N   
5401  C CA  . LEU E 39  ? 0.694 0.551 0.680 0.088  0.054  -0.064 368 LEU EEE CA  
5402  C C   . LEU E 39  ? 0.701 0.572 0.711 0.104  0.055  -0.059 368 LEU EEE C   
5403  O O   . LEU E 39  ? 0.708 0.579 0.725 0.110  0.047  -0.046 368 LEU EEE O   
5404  C CB  . LEU E 39  ? 0.654 0.532 0.638 0.079  0.049  -0.060 368 LEU EEE CB  
5405  C CG  . LEU E 39  ? 0.665 0.534 0.629 0.065  0.046  -0.062 368 LEU EEE CG  
5406  C CD1 . LEU E 39  ? 0.651 0.540 0.621 0.058  0.042  -0.057 368 LEU EEE CD1 
5407  C CD2 . LEU E 39  ? 0.670 0.518 0.623 0.060  0.040  -0.059 368 LEU EEE CD2 
5408  N N   . TYR E 40  ? 0.702 0.587 0.724 0.112  0.063  -0.066 369 TYR EEE N   
5409  C CA  . TYR E 40  ? 0.696 0.602 0.745 0.128  0.063  -0.061 369 TYR EEE CA  
5410  C C   . TYR E 40  ? 0.709 0.590 0.768 0.142  0.064  -0.057 369 TYR EEE C   
5411  O O   . TYR E 40  ? 0.711 0.606 0.790 0.155  0.059  -0.044 369 TYR EEE O   
5412  C CB  . TYR E 40  ? 0.694 0.619 0.755 0.132  0.074  -0.073 369 TYR EEE CB  
5413  C CG  . TYR E 40  ? 0.667 0.620 0.727 0.121  0.075  -0.075 369 TYR EEE CG  
5414  C CD1 . TYR E 40  ? 0.645 0.613 0.705 0.114  0.064  -0.067 369 TYR EEE CD1 
5415  C CD2 . TYR E 40  ? 0.651 0.614 0.711 0.117  0.087  -0.086 369 TYR EEE CD2 
5416  C CE1 . TYR E 40  ? 0.647 0.635 0.710 0.103  0.066  -0.070 369 TYR EEE CE1 
5417  C CE2 . TYR E 40  ? 0.647 0.632 0.709 0.106  0.088  -0.087 369 TYR EEE CE2 
5418  C CZ  . TYR E 40  ? 0.650 0.646 0.715 0.099  0.078  -0.079 369 TYR EEE CZ  
5419  O OH  . TYR E 40  ? 0.643 0.656 0.714 0.088  0.080  -0.080 369 TYR EEE OH  
5420  N N   . ASN E 41  ? 0.735 0.583 0.782 0.138  0.071  -0.066 370 ASN EEE N   
5421  C CA  . ASN E 41  ? 0.770 0.588 0.830 0.150  0.075  -0.065 370 ASN EEE CA  
5422  C C   . ASN E 41  ? 0.742 0.537 0.794 0.145  0.066  -0.051 370 ASN EEE C   
5423  O O   . ASN E 41  ? 0.765 0.531 0.827 0.151  0.070  -0.049 370 ASN EEE O   
5424  C CB  . ASN E 41  ? 0.830 0.627 0.885 0.147  0.089  -0.088 370 ASN EEE CB  
5425  C CG  . ASN E 41  ? 0.875 0.696 0.942 0.154  0.099  -0.101 370 ASN EEE CG  
5426  O OD1 . ASN E 41  ? 0.880 0.719 0.972 0.169  0.099  -0.094 370 ASN EEE OD1 
5427  N ND2 . ASN E 41  ? 0.917 0.740 0.966 0.142  0.109  -0.119 370 ASN EEE ND2 
5428  N N   . SER E 42  ? 0.689 0.498 0.726 0.133  0.056  -0.041 371 SER EEE N   
5429  C CA  . SER E 42  ? 0.682 0.478 0.712 0.127  0.047  -0.026 371 SER EEE CA  
5430  C C   . SER E 42  ? 0.666 0.487 0.710 0.138  0.038  -0.005 371 SER EEE C   
5431  O O   . SER E 42  ? 0.648 0.505 0.697 0.140  0.035  -0.005 371 SER EEE O   
5432  C CB  . SER E 42  ? 0.664 0.465 0.670 0.108  0.042  -0.030 371 SER EEE CB  
5433  O OG  . SER E 42  ? 0.681 0.467 0.673 0.099  0.048  -0.048 371 SER EEE OG  
5434  N N   . ALA E 43  ? 0.690 0.433 0.701 0.085  0.026  -0.053 372 ALA EEE N   
5435  C CA  . ALA E 43  ? 0.676 0.427 0.705 0.088  0.014  -0.029 372 ALA EEE CA  
5436  C C   . ALA E 43  ? 0.672 0.417 0.680 0.070  0.002  -0.020 372 ALA EEE C   
5437  O O   . ALA E 43  ? 0.670 0.424 0.684 0.071  -0.008 -0.000 372 ALA EEE O   
5438  C CB  . ALA E 43  ? 0.702 0.428 0.757 0.106  0.016  -0.021 372 ALA EEE CB  
5439  N N   . SER E 44  ? 0.680 0.410 0.666 0.055  0.004  -0.033 373 SER EEE N   
5440  C CA  . SER E 44  ? 0.682 0.404 0.655 0.038  -0.004 -0.024 373 SER EEE CA  
5441  C C   . SER E 44  ? 0.663 0.418 0.623 0.027  -0.010 -0.021 373 SER EEE C   
5442  O O   . SER E 44  ? 0.683 0.439 0.634 0.016  -0.015 -0.012 373 SER EEE O   
5443  C CB  . SER E 44  ? 0.691 0.381 0.654 0.027  -0.001 -0.038 373 SER EEE CB  
5444  O OG  . SER E 44  ? 0.737 0.389 0.714 0.034  0.001  -0.033 373 SER EEE OG  
5445  N N   . PHE E 45  ? 0.669 0.450 0.628 0.030  -0.008 -0.027 374 PHE EEE N   
5446  C CA  . PHE E 45  ? 0.659 0.468 0.610 0.023  -0.014 -0.024 374 PHE EEE CA  
5447  C C   . PHE E 45  ? 0.634 0.455 0.590 0.025  -0.023 -0.007 374 PHE EEE C   
5448  O O   . PHE E 45  ? 0.642 0.465 0.612 0.037  -0.025 0.002  374 PHE EEE O   
5449  C CB  . PHE E 45  ? 0.658 0.489 0.614 0.028  -0.011 -0.031 374 PHE EEE CB  
5450  C CG  . PHE E 45  ? 0.689 0.514 0.633 0.025  -0.003 -0.046 374 PHE EEE CG  
5451  C CD1 . PHE E 45  ? 0.690 0.507 0.618 0.013  -0.004 -0.053 374 PHE EEE CD1 
5452  C CD2 . PHE E 45  ? 0.709 0.543 0.660 0.033  0.006  -0.052 374 PHE EEE CD2 
5453  C CE1 . PHE E 45  ? 0.718 0.533 0.632 0.009  0.001  -0.067 374 PHE EEE CE1 
5454  C CE2 . PHE E 45  ? 0.737 0.568 0.672 0.030  0.014  -0.065 374 PHE EEE CE2 
5455  C CZ  . PHE E 45  ? 0.735 0.556 0.650 0.018  0.010  -0.073 374 PHE EEE CZ  
5456  N N   . SER E 46  ? 0.636 0.466 0.579 0.015  -0.027 -0.002 375 SER EEE N   
5457  C CA  . SER E 46  ? 0.637 0.482 0.576 0.015  -0.035 0.013  375 SER EEE CA  
5458  C C   . SER E 46  ? 0.602 0.472 0.544 0.019  -0.040 0.010  375 SER EEE C   
5459  O O   . SER E 46  ? 0.585 0.466 0.528 0.023  -0.049 0.020  375 SER EEE O   
5460  C CB  . SER E 46  ? 0.636 0.485 0.560 0.003  -0.034 0.016  375 SER EEE CB  
5461  O OG  . SER E 46  ? 0.606 0.466 0.525 -0.004 -0.031 0.003  375 SER EEE OG  
5462  N N   . THR E 47  ? 0.572 0.451 0.518 0.018  -0.037 -0.003 376 THR EEE N   
5463  C CA  . THR E 47  ? 0.579 0.478 0.532 0.020  -0.042 -0.007 376 THR EEE CA  
5464  C C   . THR E 47  ? 0.575 0.474 0.538 0.021  -0.035 -0.017 376 THR EEE C   
5465  O O   . THR E 47  ? 0.546 0.435 0.501 0.017  -0.028 -0.023 376 THR EEE O   
5466  C CB  . THR E 47  ? 0.574 0.485 0.513 0.012  -0.046 -0.011 376 THR EEE CB  
5467  O OG1 . THR E 47  ? 0.550 0.477 0.497 0.014  -0.053 -0.014 376 THR EEE OG1 
5468  C CG2 . THR E 47  ? 0.556 0.465 0.490 0.006  -0.039 -0.020 376 THR EEE CG2 
5469  N N   . PHE E 48  ? 0.555 0.469 0.536 0.025  -0.037 -0.016 377 PHE EEE N   
5470  C CA  . PHE E 48  ? 0.549 0.468 0.540 0.026  -0.029 -0.022 377 PHE EEE CA  
5471  C C   . PHE E 48  ? 0.517 0.456 0.526 0.025  -0.035 -0.020 377 PHE EEE C   
5472  O O   . PHE E 48  ? 0.511 0.462 0.541 0.032  -0.038 -0.014 377 PHE EEE O   
5473  C CB  . PHE E 48  ? 0.561 0.471 0.559 0.035  -0.018 -0.023 377 PHE EEE CB  
5474  C CG  . PHE E 48  ? 0.566 0.483 0.569 0.036  -0.007 -0.028 377 PHE EEE CG  
5475  C CD1 . PHE E 48  ? 0.558 0.491 0.567 0.030  -0.008 -0.026 377 PHE EEE CD1 
5476  C CD2 . PHE E 48  ? 0.582 0.491 0.585 0.044  0.005  -0.033 377 PHE EEE CD2 
5477  C CE1 . PHE E 48  ? 0.570 0.513 0.584 0.031  0.003  -0.027 377 PHE EEE CE1 
5478  C CE2 . PHE E 48  ? 0.588 0.507 0.593 0.045  0.017  -0.037 377 PHE EEE CE2 
5479  C CZ  . PHE E 48  ? 0.566 0.503 0.575 0.038  0.016  -0.032 377 PHE EEE CZ  
5480  N N   . LYS E 49  ? 0.483 0.427 0.489 0.017  -0.040 -0.024 378 LYS EEE N   
5481  C CA  . LYS E 49  ? 0.487 0.446 0.511 0.013  -0.047 -0.024 378 LYS EEE CA  
5482  C C   . LYS E 49  ? 0.464 0.423 0.495 0.008  -0.041 -0.026 378 LYS EEE C   
5483  O O   . LYS E 49  ? 0.484 0.433 0.500 0.006  -0.037 -0.029 378 LYS EEE O   
5484  C CB  . LYS E 49  ? 0.501 0.461 0.514 0.008  -0.059 -0.029 378 LYS EEE CB  
5485  C CG  . LYS E 49  ? 0.513 0.474 0.513 0.012  -0.066 -0.025 378 LYS EEE CG  
5486  C CD  . LYS E 49  ? 0.506 0.469 0.487 0.007  -0.075 -0.032 378 LYS EEE CD  
5487  C CE  . LYS E 49  ? 0.526 0.495 0.493 0.009  -0.084 -0.024 378 LYS EEE CE  
5488  N NZ  . LYS E 49  ? 0.563 0.539 0.508 0.004  -0.092 -0.033 378 LYS EEE NZ  
5489  N N   . CYS E 50  ? 0.453 0.425 0.509 0.005  -0.042 -0.022 379 CYS EEE N   
5490  C CA  . CYS E 50  ? 0.458 0.431 0.525 -0.002 -0.039 -0.020 379 CYS EEE CA  
5491  C C   . CYS E 50  ? 0.460 0.436 0.543 -0.010 -0.052 -0.025 379 CYS EEE C   
5492  O O   . CYS E 50  ? 0.441 0.426 0.531 -0.011 -0.063 -0.028 379 CYS EEE O   
5493  C CB  . CYS E 50  ? 0.476 0.462 0.560 0.000  -0.026 -0.011 379 CYS EEE CB  
5494  S SG  . CYS E 50  ? 0.522 0.500 0.581 0.010  -0.011 -0.012 379 CYS EEE SG  
5495  N N   . TYR E 51  ? 0.475 0.441 0.563 -0.016 -0.051 -0.025 380 TYR EEE N   
5496  C CA  . TYR E 51  ? 0.489 0.449 0.592 -0.025 -0.062 -0.033 380 TYR EEE CA  
5497  C C   . TYR E 51  ? 0.506 0.468 0.636 -0.033 -0.056 -0.021 380 TYR EEE C   
5498  O O   . TYR E 51  ? 0.510 0.466 0.633 -0.031 -0.046 -0.012 380 TYR EEE O   
5499  C CB  . TYR E 51  ? 0.487 0.428 0.568 -0.023 -0.064 -0.044 380 TYR EEE CB  
5500  C CG  . TYR E 51  ? 0.483 0.427 0.538 -0.017 -0.066 -0.051 380 TYR EEE CG  
5501  C CD1 . TYR E 51  ? 0.475 0.417 0.510 -0.010 -0.057 -0.046 380 TYR EEE CD1 
5502  C CD2 . TYR E 51  ? 0.470 0.415 0.515 -0.019 -0.077 -0.063 380 TYR EEE CD2 
5503  C CE1 . TYR E 51  ? 0.476 0.418 0.489 -0.006 -0.058 -0.050 380 TYR EEE CE1 
5504  C CE2 . TYR E 51  ? 0.488 0.436 0.507 -0.014 -0.078 -0.066 380 TYR EEE CE2 
5505  C CZ  . TYR E 51  ? 0.479 0.425 0.484 -0.007 -0.068 -0.058 380 TYR EEE CZ  
5506  O OH  . TYR E 51  ? 0.470 0.417 0.452 -0.004 -0.068 -0.059 380 TYR EEE OH  
5507  N N   . GLY E 52  ? 0.485 0.458 0.646 -0.043 -0.064 -0.020 381 GLY EEE N   
5508  C CA  . GLY E 52  ? 0.477 0.453 0.668 -0.052 -0.058 -0.006 381 GLY EEE CA  
5509  C C   . GLY E 52  ? 0.495 0.494 0.696 -0.049 -0.043 0.010  381 GLY EEE C   
5510  O O   . GLY E 52  ? 0.536 0.542 0.763 -0.058 -0.037 0.024  381 GLY EEE O   
5511  N N   . VAL E 53  ? 0.521 0.530 0.703 -0.037 -0.036 0.009  382 VAL EEE N   
5512  C CA  . VAL E 53  ? 0.522 0.555 0.715 -0.032 -0.020 0.021  382 VAL EEE CA  
5513  C C   . VAL E 53  ? 0.494 0.536 0.681 -0.020 -0.023 0.014  382 VAL EEE C   
5514  O O   . VAL E 53  ? 0.487 0.514 0.647 -0.015 -0.030 0.004  382 VAL EEE O   
5515  C CB  . VAL E 53  ? 0.523 0.550 0.691 -0.027 -0.004 0.028  382 VAL EEE CB  
5516  C CG1 . VAL E 53  ? 0.551 0.571 0.728 -0.038 -0.001 0.041  382 VAL EEE CG1 
5517  C CG2 . VAL E 53  ? 0.523 0.529 0.652 -0.019 -0.006 0.018  382 VAL EEE CG2 
5518  N N   . SER E 54  ? 0.485 0.554 0.698 -0.016 -0.015 0.021  383 SER EEE N   
5519  C CA  . SER E 54  ? 0.503 0.580 0.715 -0.002 -0.015 0.017  383 SER EEE CA  
5520  C C   . SER E 54  ? 0.510 0.573 0.690 0.010  0.001  0.014  383 SER EEE C   
5521  O O   . SER E 54  ? 0.501 0.569 0.678 0.010  0.018  0.019  383 SER EEE O   
5522  C CB  . SER E 54  ? 0.506 0.618 0.763 0.001  -0.014 0.026  383 SER EEE CB  
5523  O OG  . SER E 54  ? 0.532 0.648 0.788 0.017  -0.012 0.025  383 SER EEE OG  
5524  N N   . PRO E 55  ? 0.496 0.542 0.652 0.020  -0.003 0.006  384 PRO EEE N   
5525  C CA  . PRO E 55  ? 0.534 0.567 0.665 0.030  0.012  0.001  384 PRO EEE CA  
5526  C C   . PRO E 55  ? 0.545 0.597 0.695 0.040  0.031  0.004  384 PRO EEE C   
5527  O O   . PRO E 55  ? 0.584 0.627 0.711 0.045  0.047  -0.001 384 PRO EEE O   
5528  C CB  . PRO E 55  ? 0.543 0.559 0.661 0.038  0.002  -0.004 384 PRO EEE CB  
5529  C CG  . PRO E 55  ? 0.548 0.564 0.666 0.028  -0.018 -0.004 384 PRO EEE CG  
5530  C CD  . PRO E 55  ? 0.525 0.565 0.677 0.020  -0.022 0.002  384 PRO EEE CD  
5531  N N   . THR E 56  ? 0.516 0.595 0.707 0.044  0.030  0.012  385 THR EEE N   
5532  C CA  . THR E 56  ? 0.533 0.637 0.751 0.055  0.050  0.016  385 THR EEE CA  
5533  C C   . THR E 56  ? 0.565 0.685 0.783 0.047  0.067  0.022  385 THR EEE C   
5534  O O   . THR E 56  ? 0.590 0.728 0.820 0.057  0.089  0.023  385 THR EEE O   
5535  C CB  . THR E 56  ? 0.513 0.649 0.782 0.060  0.041  0.025  385 THR EEE CB  
5536  O OG1 . THR E 56  ? 0.500 0.655 0.794 0.043  0.029  0.034  385 THR EEE OG1 
5537  C CG2 . THR E 56  ? 0.499 0.621 0.766 0.069  0.023  0.023  385 THR EEE CG2 
5538  N N   . LYS E 57  ? 0.581 0.695 0.790 0.031  0.060  0.027  386 LYS EEE N   
5539  C CA  . LYS E 57  ? 0.604 0.734 0.818 0.021  0.074  0.039  386 LYS EEE CA  
5540  C C   . LYS E 57  ? 0.584 0.691 0.750 0.018  0.081  0.035  386 LYS EEE C   
5541  O O   . LYS E 57  ? 0.591 0.710 0.755 0.010  0.092  0.047  386 LYS EEE O   
5542  C CB  . LYS E 57  ? 0.647 0.786 0.893 0.004  0.059  0.050  386 LYS EEE CB  
5543  C CG  . LYS E 57  ? 0.692 0.862 0.991 0.004  0.052  0.055  386 LYS EEE CG  
5544  C CD  . LYS E 57  ? 0.746 0.955 1.083 0.002  0.072  0.069  386 LYS EEE CD  
5545  C CE  . LYS E 57  ? 0.784 0.997 1.133 -0.018 0.074  0.084  386 LYS EEE CE  
5546  N NZ  . LYS E 57  ? 0.819 1.054 1.166 -0.017 0.103  0.097  386 LYS EEE NZ  
5547  N N   . LEU E 58  ? 0.566 0.644 0.695 0.023  0.073  0.022  387 LEU EEE N   
5548  C CA  . LEU E 58  ? 0.584 0.643 0.670 0.018  0.074  0.020  387 LEU EEE CA  
5549  C C   . LEU E 58  ? 0.603 0.676 0.669 0.021  0.097  0.022  387 LEU EEE C   
5550  O O   . LEU E 58  ? 0.643 0.715 0.686 0.013  0.099  0.031  387 LEU EEE O   
5551  C CB  . LEU E 58  ? 0.585 0.616 0.641 0.023  0.064  0.004  387 LEU EEE CB  
5552  C CG  . LEU E 58  ? 0.585 0.602 0.650 0.018  0.042  0.003  387 LEU EEE CG  
5553  C CD1 . LEU E 58  ? 0.603 0.595 0.639 0.022  0.035  -0.010 387 LEU EEE CD1 
5554  C CD2 . LEU E 58  ? 0.580 0.595 0.648 0.006  0.033  0.012  387 LEU EEE CD2 
5555  N N   . ASN E 59  ? 0.614 0.702 0.689 0.034  0.115  0.016  388 ASN EEE N   
5556  C CA  . ASN E 59  ? 0.631 0.733 0.683 0.038  0.139  0.014  388 ASN EEE CA  
5557  C C   . ASN E 59  ? 0.614 0.750 0.690 0.030  0.153  0.035  388 ASN EEE C   
5558  O O   . ASN E 59  ? 0.661 0.813 0.714 0.032  0.175  0.037  388 ASN EEE O   
5559  C CB  . ASN E 59  ? 0.675 0.777 0.726 0.057  0.155  -0.004 388 ASN EEE CB  
5560  C CG  . ASN E 59  ? 0.709 0.776 0.717 0.061  0.150  -0.026 388 ASN EEE CG  
5561  O OD1 . ASN E 59  ? 0.714 0.764 0.689 0.051  0.137  -0.027 388 ASN EEE OD1 
5562  N ND2 . ASN E 59  ? 0.750 0.807 0.762 0.077  0.159  -0.043 388 ASN EEE ND2 
5563  N N   . ASP E 60  ? 0.596 0.743 0.714 0.020  0.142  0.051  389 ASP EEE N   
5564  C CA  . ASP E 60  ? 0.605 0.785 0.757 0.010  0.155  0.074  389 ASP EEE CA  
5565  C C   . ASP E 60  ? 0.581 0.751 0.732 -0.008 0.141  0.092  389 ASP EEE C   
5566  O O   . ASP E 60  ? 0.583 0.776 0.765 -0.019 0.150  0.113  389 ASP EEE O   
5567  C CB  . ASP E 60  ? 0.626 0.831 0.838 0.012  0.152  0.078  389 ASP EEE CB  
5568  C CG  . ASP E 60  ? 0.665 0.884 0.890 0.032  0.165  0.064  389 ASP EEE CG  
5569  O OD1 . ASP E 60  ? 0.717 0.953 0.928 0.042  0.193  0.061  389 ASP EEE OD1 
5570  O OD2 . ASP E 60  ? 0.696 0.906 0.941 0.038  0.149  0.055  389 ASP EEE OD2 
5571  N N   . LEU E 61  ? 0.556 0.693 0.679 -0.011 0.122  0.086  390 LEU EEE N   
5572  C CA  . LEU E 61  ? 0.550 0.673 0.681 -0.026 0.107  0.102  390 LEU EEE CA  
5573  C C   . LEU E 61  ? 0.586 0.699 0.671 -0.029 0.111  0.111  390 LEU EEE C   
5574  O O   . LEU E 61  ? 0.609 0.715 0.652 -0.020 0.114  0.096  390 LEU EEE O   
5575  C CB  . LEU E 61  ? 0.532 0.628 0.672 -0.027 0.082  0.088  390 LEU EEE CB  
5576  C CG  . LEU E 61  ? 0.524 0.630 0.706 -0.027 0.074  0.081  390 LEU EEE CG  
5577  C CD1 . LEU E 61  ? 0.529 0.608 0.708 -0.027 0.050  0.067  390 LEU EEE CD1 
5578  C CD2 . LEU E 61  ? 0.524 0.653 0.754 -0.040 0.077  0.099  390 LEU EEE CD2 
5579  N N   . CYS E 62  ? 0.609 0.720 0.705 -0.041 0.107  0.134  391 CYS EEE N   
5580  C CA  . CYS E 62  ? 0.637 0.737 0.697 -0.044 0.104  0.148  391 CYS EEE CA  
5581  C C   . CYS E 62  ? 0.610 0.679 0.683 -0.049 0.080  0.150  391 CYS EEE C   
5582  O O   . CYS E 62  ? 0.572 0.633 0.686 -0.056 0.072  0.150  391 CYS EEE O   
5583  C CB  . CYS E 62  ? 0.685 0.809 0.748 -0.054 0.121  0.178  391 CYS EEE CB  
5584  S SG  . CYS E 62  ? 0.756 0.916 0.791 -0.045 0.153  0.173  391 CYS EEE SG  
5585  N N   . PHE E 63  ? 0.631 0.685 0.670 -0.046 0.070  0.149  392 PHE EEE N   
5586  C CA  . PHE E 63  ? 0.630 0.657 0.679 -0.047 0.050  0.150  392 PHE EEE CA  
5587  C C   . PHE E 63  ? 0.678 0.704 0.704 -0.049 0.047  0.174  392 PHE EEE C   
5588  O O   . PHE E 63  ? 0.721 0.766 0.709 -0.048 0.058  0.181  392 PHE EEE O   
5589  C CB  . PHE E 63  ? 0.599 0.610 0.635 -0.038 0.038  0.122  392 PHE EEE CB  
5590  C CG  . PHE E 63  ? 0.576 0.589 0.633 -0.036 0.038  0.102  392 PHE EEE CG  
5591  C CD1 . PHE E 63  ? 0.565 0.570 0.661 -0.042 0.030  0.101  392 PHE EEE CD1 
5592  C CD2 . PHE E 63  ? 0.574 0.597 0.613 -0.028 0.046  0.085  392 PHE EEE CD2 
5593  C CE1 . PHE E 63  ? 0.542 0.552 0.657 -0.040 0.028  0.085  392 PHE EEE CE1 
5594  C CE2 . PHE E 63  ? 0.560 0.585 0.619 -0.025 0.045  0.071  392 PHE EEE CE2 
5595  C CZ  . PHE E 63  ? 0.553 0.575 0.651 -0.031 0.036  0.072  392 PHE EEE CZ  
5596  N N   . THR E 64  ? 0.701 0.705 0.749 -0.052 0.034  0.187  393 THR EEE N   
5597  C CA  . THR E 64  ? 0.744 0.744 0.778 -0.052 0.027  0.213  393 THR EEE CA  
5598  C C   . THR E 64  ? 0.741 0.742 0.739 -0.043 0.016  0.198  393 THR EEE C   
5599  O O   . THR E 64  ? 0.794 0.807 0.763 -0.043 0.014  0.214  393 THR EEE O   
5600  C CB  . THR E 64  ? 0.761 0.733 0.837 -0.054 0.013  0.224  393 THR EEE CB  
5601  O OG1 . THR E 64  ? 0.726 0.689 0.843 -0.062 0.016  0.220  393 THR EEE OG1 
5602  C CG2 . THR E 64  ? 0.836 0.805 0.915 -0.057 0.011  0.262  393 THR EEE CG2 
5603  N N   . ASN E 65  ? 0.708 0.698 0.711 -0.037 0.009  0.168  394 ASN EEE N   
5604  C CA  . ASN E 65  ? 0.719 0.707 0.698 -0.030 -0.002 0.153  394 ASN EEE CA  
5605  C C   . ASN E 65  ? 0.641 0.624 0.619 -0.026 -0.002 0.121  394 ASN EEE C   
5606  O O   . ASN E 65  ? 0.612 0.586 0.619 -0.027 0.000  0.112  394 ASN EEE O   
5607  C CB  . ASN E 65  ? 0.784 0.756 0.784 -0.026 -0.018 0.163  394 ASN EEE CB  
5608  C CG  . ASN E 65  ? 0.855 0.834 0.833 -0.020 -0.029 0.157  394 ASN EEE CG  
5609  O OD1 . ASN E 65  ? 0.920 0.916 0.867 -0.022 -0.031 0.169  394 ASN EEE OD1 
5610  N ND2 . ASN E 65  ? 0.872 0.839 0.865 -0.014 -0.036 0.137  394 ASN EEE ND2 
5611  N N   . VAL E 66  ? 0.603 0.592 0.550 -0.023 -0.004 0.106  395 VAL EEE N   
5612  C CA  . VAL E 66  ? 0.581 0.561 0.529 -0.019 -0.006 0.078  395 VAL EEE CA  
5613  C C   . VAL E 66  ? 0.578 0.556 0.515 -0.017 -0.019 0.072  395 VAL EEE C   
5614  O O   . VAL E 66  ? 0.605 0.595 0.518 -0.019 -0.024 0.081  395 VAL EEE O   
5615  C CB  . VAL E 66  ? 0.594 0.581 0.520 -0.019 0.006  0.063  395 VAL EEE CB  
5616  C CG1 . VAL E 66  ? 0.560 0.536 0.488 -0.015 0.003  0.040  395 VAL EEE CG1 
5617  C CG2 . VAL E 66  ? 0.615 0.612 0.557 -0.020 0.020  0.072  395 VAL EEE CG2 
5618  N N   . TYR E 67  ? 0.572 0.539 0.526 -0.013 -0.025 0.058  396 TYR EEE N   
5619  C CA  . TYR E 67  ? 0.562 0.530 0.510 -0.011 -0.035 0.050  396 TYR EEE CA  
5620  C C   . TYR E 67  ? 0.548 0.511 0.488 -0.012 -0.032 0.028  396 TYR EEE C   
5621  O O   . TYR E 67  ? 0.514 0.469 0.467 -0.010 -0.027 0.020  396 TYR EEE O   
5622  C CB  . TYR E 67  ? 0.579 0.541 0.558 -0.006 -0.043 0.055  396 TYR EEE CB  
5623  C CG  . TYR E 67  ? 0.638 0.602 0.627 -0.005 -0.048 0.079  396 TYR EEE CG  
5624  C CD1 . TYR E 67  ? 0.675 0.656 0.646 -0.006 -0.055 0.092  396 TYR EEE CD1 
5625  C CD2 . TYR E 67  ? 0.688 0.638 0.708 -0.002 -0.048 0.088  396 TYR EEE CD2 
5626  C CE1 . TYR E 67  ? 0.723 0.708 0.704 -0.004 -0.062 0.118  396 TYR EEE CE1 
5627  C CE2 . TYR E 67  ? 0.733 0.682 0.767 0.001  -0.054 0.112  396 TYR EEE CE2 
5628  C CZ  . TYR E 67  ? 0.764 0.732 0.779 0.001  -0.061 0.129  396 TYR EEE CZ  
5629  O OH  . TYR E 67  ? 0.821 0.790 0.848 0.003  -0.067 0.157  396 TYR EEE OH  
5630  N N   . ALA E 68  ? 0.580 0.548 0.501 -0.014 -0.037 0.020  397 ALA EEE N   
5631  C CA  . ALA E 68  ? 0.560 0.521 0.475 -0.016 -0.036 0.002  397 ALA EEE CA  
5632  C C   . ALA E 68  ? 0.527 0.493 0.454 -0.016 -0.045 0.001  397 ALA EEE C   
5633  O O   . ALA E 68  ? 0.563 0.541 0.481 -0.020 -0.053 0.005  397 ALA EEE O   
5634  C CB  . ALA E 68  ? 0.582 0.542 0.467 -0.020 -0.032 -0.008 397 ALA EEE CB  
5635  N N   . ASP E 69  ? 0.510 0.470 0.455 -0.012 -0.043 -0.005 398 ASP EEE N   
5636  C CA  . ASP E 69  ? 0.519 0.485 0.477 -0.011 -0.048 -0.008 398 ASP EEE CA  
5637  C C   . ASP E 69  ? 0.539 0.501 0.487 -0.016 -0.045 -0.019 398 ASP EEE C   
5638  O O   . ASP E 69  ? 0.560 0.509 0.502 -0.015 -0.039 -0.025 398 ASP EEE O   
5639  C CB  . ASP E 69  ? 0.533 0.496 0.514 -0.004 -0.046 -0.008 398 ASP EEE CB  
5640  C CG  . ASP E 69  ? 0.525 0.487 0.522 0.001  -0.048 0.004  398 ASP EEE CG  
5641  O OD1 . ASP E 69  ? 0.507 0.479 0.500 -0.000 -0.054 0.017  398 ASP EEE OD1 
5642  O OD2 . ASP E 69  ? 0.545 0.496 0.556 0.006  -0.045 0.002  398 ASP EEE OD2 
5643  N N   . SER E 70  ? 0.552 0.522 0.499 -0.022 -0.049 -0.021 399 SER EEE N   
5644  C CA  . SER E 70  ? 0.555 0.518 0.494 -0.029 -0.047 -0.030 399 SER EEE CA  
5645  C C   . SER E 70  ? 0.568 0.546 0.523 -0.033 -0.050 -0.028 399 SER EEE C   
5646  O O   . SER E 70  ? 0.585 0.583 0.555 -0.033 -0.056 -0.022 399 SER EEE O   
5647  C CB  . SER E 70  ? 0.570 0.525 0.488 -0.037 -0.050 -0.036 399 SER EEE CB  
5648  O OG  . SER E 70  ? 0.620 0.591 0.534 -0.042 -0.059 -0.032 399 SER EEE OG  
5649  N N   . PHE E 71  ? 0.542 0.514 0.497 -0.037 -0.045 -0.032 400 PHE EEE N   
5650  C CA  . PHE E 71  ? 0.541 0.530 0.513 -0.041 -0.043 -0.029 400 PHE EEE CA  
5651  C C   . PHE E 71  ? 0.534 0.510 0.498 -0.047 -0.037 -0.031 400 PHE EEE C   
5652  O O   . PHE E 71  ? 0.533 0.487 0.482 -0.044 -0.035 -0.034 400 PHE EEE O   
5653  C CB  . PHE E 71  ? 0.547 0.550 0.535 -0.030 -0.039 -0.027 400 PHE EEE CB  
5654  C CG  . PHE E 71  ? 0.550 0.538 0.531 -0.020 -0.033 -0.031 400 PHE EEE CG  
5655  C CD1 . PHE E 71  ? 0.553 0.534 0.525 -0.020 -0.026 -0.034 400 PHE EEE CD1 
5656  C CD2 . PHE E 71  ? 0.545 0.527 0.528 -0.013 -0.036 -0.030 400 PHE EEE CD2 
5657  C CE1 . PHE E 71  ? 0.575 0.546 0.541 -0.013 -0.024 -0.038 400 PHE EEE CE1 
5658  C CE2 . PHE E 71  ? 0.557 0.526 0.537 -0.006 -0.032 -0.035 400 PHE EEE CE2 
5659  C CZ  . PHE E 71  ? 0.564 0.529 0.535 -0.007 -0.028 -0.040 400 PHE EEE CZ  
5660  N N   . VAL E 72  ? 0.513 0.504 0.490 -0.053 -0.033 -0.027 401 VAL EEE N   
5661  C CA  . VAL E 72  ? 0.526 0.508 0.498 -0.059 -0.027 -0.023 401 VAL EEE CA  
5662  C C   . VAL E 72  ? 0.503 0.500 0.479 -0.052 -0.017 -0.020 401 VAL EEE C   
5663  O O   . VAL E 72  ? 0.482 0.505 0.476 -0.048 -0.014 -0.019 401 VAL EEE O   
5664  C CB  . VAL E 72  ? 0.528 0.512 0.508 -0.076 -0.030 -0.020 401 VAL EEE CB  
5665  C CG1 . VAL E 72  ? 0.536 0.514 0.516 -0.083 -0.022 -0.011 401 VAL EEE CG1 
5666  C CG2 . VAL E 72  ? 0.560 0.520 0.528 -0.083 -0.039 -0.027 401 VAL EEE CG2 
5667  N N   . ILE E 73  ? 0.508 0.493 0.469 -0.049 -0.012 -0.017 402 ILE EEE N   
5668  C CA  . ILE E 73  ? 0.530 0.530 0.487 -0.045 -0.002 -0.015 402 ILE EEE CA  
5669  C C   . ILE E 73  ? 0.558 0.546 0.502 -0.052 0.001  -0.004 402 ILE EEE C   
5670  O O   . ILE E 73  ? 0.567 0.533 0.508 -0.059 -0.004 -0.000 402 ILE EEE O   
5671  C CB  . ILE E 73  ? 0.498 0.496 0.447 -0.031 -0.002 -0.024 402 ILE EEE CB  
5672  C CG1 . ILE E 73  ? 0.501 0.474 0.436 -0.027 -0.010 -0.026 402 ILE EEE CG1 
5673  C CG2 . ILE E 73  ? 0.479 0.490 0.446 -0.023 -0.003 -0.031 402 ILE EEE CG2 
5674  C CD1 . ILE E 73  ? 0.496 0.468 0.425 -0.017 -0.011 -0.034 402 ILE EEE CD1 
5675  N N   . ARG E 74  ? 0.598 0.600 0.532 -0.050 0.010  0.002  403 ARG EEE N   
5676  C CA  . ARG E 74  ? 0.639 0.631 0.556 -0.055 0.013  0.016  403 ARG EEE CA  
5677  C C   . ARG E 74  ? 0.657 0.627 0.557 -0.047 0.004  0.014  403 ARG EEE C   
5678  O O   . ARG E 74  ? 0.646 0.619 0.542 -0.036 0.001  0.001  403 ARG EEE O   
5679  C CB  . ARG E 74  ? 0.684 0.701 0.588 -0.054 0.025  0.022  403 ARG EEE CB  
5680  C CG  . ARG E 74  ? 0.730 0.773 0.651 -0.064 0.037  0.030  403 ARG EEE CG  
5681  C CD  . ARG E 74  ? 0.738 0.811 0.647 -0.058 0.052  0.028  403 ARG EEE CD  
5682  N NE  . ARG E 74  ? 0.773 0.840 0.649 -0.056 0.052  0.036  403 ARG EEE NE  
5683  C CZ  . ARG E 74  ? 0.832 0.922 0.685 -0.051 0.064  0.035  403 ARG EEE CZ  
5684  N NH1 . ARG E 74  ? 0.836 0.956 0.699 -0.047 0.079  0.026  403 ARG EEE NH1 
5685  N NH2 . ARG E 74  ? 0.870 0.954 0.689 -0.050 0.061  0.044  403 ARG EEE NH2 
5686  N N   . GLY E 75  ? 0.662 0.614 0.554 -0.050 0.001  0.028  404 GLY EEE N   
5687  C CA  . GLY E 75  ? 0.627 0.564 0.507 -0.042 -0.007 0.030  404 GLY EEE CA  
5688  C C   . GLY E 75  ? 0.629 0.584 0.492 -0.033 -0.008 0.023  404 GLY EEE C   
5689  O O   . GLY E 75  ? 0.599 0.548 0.462 -0.025 -0.016 0.013  404 GLY EEE O   
5690  N N   . ASP E 76  ? 0.665 0.641 0.512 -0.035 0.000  0.027  405 ASP EEE N   
5691  C CA  . ASP E 76  ? 0.711 0.701 0.536 -0.028 -0.002 0.019  405 ASP EEE CA  
5692  C C   . ASP E 76  ? 0.690 0.691 0.523 -0.021 0.001  -0.005 405 ASP EEE C   
5693  O O   . ASP E 76  ? 0.693 0.702 0.509 -0.016 -0.001 -0.017 405 ASP EEE O   
5694  C CB  . ASP E 76  ? 0.787 0.793 0.584 -0.031 0.004  0.034  405 ASP EEE CB  
5695  C CG  . ASP E 76  ? 0.878 0.903 0.678 -0.039 0.020  0.042  405 ASP EEE CG  
5696  O OD1 . ASP E 76  ? 0.897 0.930 0.717 -0.039 0.028  0.029  405 ASP EEE OD1 
5697  O OD2 . ASP E 76  ? 0.984 1.016 0.766 -0.045 0.026  0.063  405 ASP EEE OD2 
5698  N N   . GLU E 77  ? 0.650 0.647 0.507 -0.022 0.004  -0.011 406 GLU EEE N   
5699  C CA  . GLU E 77  ? 0.606 0.607 0.476 -0.015 0.004  -0.030 406 GLU EEE CA  
5700  C C   . GLU E 77  ? 0.613 0.595 0.493 -0.011 -0.008 -0.036 406 GLU EEE C   
5701  O O   . GLU E 77  ? 0.586 0.567 0.475 -0.006 -0.010 -0.049 406 GLU EEE O   
5702  C CB  . GLU E 77  ? 0.582 0.596 0.474 -0.017 0.013  -0.031 406 GLU EEE CB  
5703  C CG  . GLU E 77  ? 0.602 0.642 0.489 -0.017 0.028  -0.030 406 GLU EEE CG  
5704  C CD  . GLU E 77  ? 0.598 0.655 0.513 -0.021 0.036  -0.026 406 GLU EEE CD  
5705  O OE1 . GLU E 77  ? 0.559 0.606 0.492 -0.027 0.028  -0.021 406 GLU EEE OE1 
5706  O OE2 . GLU E 77  ? 0.610 0.693 0.529 -0.018 0.050  -0.029 406 GLU EEE OE2 
5707  N N   . VAL E 78  ? 0.622 0.589 0.503 -0.014 -0.015 -0.025 407 VAL EEE N   
5708  C CA  . VAL E 78  ? 0.578 0.531 0.471 -0.011 -0.023 -0.030 407 VAL EEE CA  
5709  C C   . VAL E 78  ? 0.585 0.540 0.473 -0.005 -0.030 -0.039 407 VAL EEE C   
5710  O O   . VAL E 78  ? 0.570 0.520 0.472 -0.003 -0.033 -0.047 407 VAL EEE O   
5711  C CB  . VAL E 78  ? 0.596 0.533 0.490 -0.012 -0.027 -0.018 407 VAL EEE CB  
5712  C CG1 . VAL E 78  ? 0.587 0.514 0.491 -0.007 -0.033 -0.022 407 VAL EEE CG1 
5713  C CG2 . VAL E 78  ? 0.639 0.568 0.540 -0.020 -0.022 -0.014 407 VAL EEE CG2 
5714  N N   . ARG E 79  ? 0.616 0.579 0.486 -0.005 -0.033 -0.039 408 ARG EEE N   
5715  C CA  . ARG E 79  ? 0.644 0.611 0.508 -0.002 -0.041 -0.051 408 ARG EEE CA  
5716  C C   . ARG E 79  ? 0.636 0.602 0.508 0.000  -0.038 -0.069 408 ARG EEE C   
5717  O O   . ARG E 79  ? 0.666 0.629 0.543 0.001  -0.046 -0.081 408 ARG EEE O   
5718  C CB  . ARG E 79  ? 0.723 0.702 0.558 -0.003 -0.044 -0.048 408 ARG EEE CB  
5719  C CG  . ARG E 79  ? 0.828 0.820 0.645 -0.004 -0.032 -0.054 408 ARG EEE CG  
5720  C CD  . ARG E 79  ? 0.937 0.944 0.720 -0.005 -0.034 -0.056 408 ARG EEE CD  
5721  N NE  . ARG E 79  ? 1.068 1.074 0.847 -0.003 -0.044 -0.078 408 ARG EEE NE  
5722  C CZ  . ARG E 79  ? 1.119 1.128 0.889 -0.005 -0.060 -0.079 408 ARG EEE CZ  
5723  N NH1 . ARG E 79  ? 1.107 1.120 0.869 -0.007 -0.070 -0.057 408 ARG EEE NH1 
5724  N NH2 . ARG E 79  ? 1.107 1.113 0.877 -0.006 -0.069 -0.101 408 ARG EEE NH2 
5725  N N   . GLN E 80  ? 0.615 0.585 0.494 0.002  -0.027 -0.072 409 GLN EEE N   
5726  C CA  . GLN E 80  ? 0.594 0.564 0.486 0.007  -0.022 -0.088 409 GLN EEE CA  
5727  C C   . GLN E 80  ? 0.566 0.523 0.484 0.008  -0.027 -0.085 409 GLN EEE C   
5728  O O   . GLN E 80  ? 0.537 0.488 0.469 0.012  -0.026 -0.096 409 GLN EEE O   
5729  C CB  . GLN E 80  ? 0.600 0.583 0.494 0.010  -0.009 -0.089 409 GLN EEE CB  
5730  C CG  . GLN E 80  ? 0.651 0.649 0.518 0.010  -0.001 -0.094 409 GLN EEE CG  
5731  C CD  . GLN E 80  ? 0.661 0.678 0.535 0.014  0.015  -0.096 409 GLN EEE CD  
5732  O OE1 . GLN E 80  ? 0.694 0.712 0.592 0.021  0.020  -0.105 409 GLN EEE OE1 
5733  N NE2 . GLN E 80  ? 0.654 0.687 0.510 0.009  0.024  -0.085 409 GLN EEE NE2 
5734  N N   . ILE E 81  ? 0.533 0.485 0.456 0.004  -0.030 -0.072 410 ILE EEE N   
5735  C CA  . ILE E 81  ? 0.530 0.474 0.473 0.004  -0.032 -0.068 410 ILE EEE CA  
5736  C C   . ILE E 81  ? 0.533 0.470 0.481 0.003  -0.040 -0.070 410 ILE EEE C   
5737  O O   . ILE E 81  ? 0.561 0.496 0.511 0.001  -0.043 -0.061 410 ILE EEE O   
5738  C CB  . ILE E 81  ? 0.523 0.466 0.467 0.001  -0.030 -0.056 410 ILE EEE CB  
5739  C CG1 . ILE E 81  ? 0.537 0.490 0.477 -0.001 -0.024 -0.054 410 ILE EEE CG1 
5740  C CG2 . ILE E 81  ? 0.533 0.472 0.491 0.001  -0.031 -0.053 410 ILE EEE CG2 
5741  C CD1 . ILE E 81  ? 0.558 0.521 0.510 0.004  -0.019 -0.060 410 ILE EEE CD1 
5742  N N   . ALA E 82  ? 0.559 0.493 0.510 0.004  -0.044 -0.082 411 ALA EEE N   
5743  C CA  . ALA E 82  ? 0.560 0.491 0.519 0.000  -0.054 -0.086 411 ALA EEE CA  
5744  C C   . ALA E 82  ? 0.569 0.490 0.537 0.001  -0.056 -0.102 411 ALA EEE C   
5745  O O   . ALA E 82  ? 0.583 0.504 0.542 0.005  -0.050 -0.114 411 ALA EEE O   
5746  C CB  . ALA E 82  ? 0.533 0.473 0.474 -0.002 -0.060 -0.086 411 ALA EEE CB  
5747  N N   . PRO E 83  ? 0.573 0.486 0.560 -0.004 -0.063 -0.104 412 PRO EEE N   
5748  C CA  . PRO E 83  ? 0.609 0.508 0.608 -0.005 -0.066 -0.121 412 PRO EEE CA  
5749  C C   . PRO E 83  ? 0.620 0.522 0.593 -0.005 -0.071 -0.141 412 PRO EEE C   
5750  O O   . PRO E 83  ? 0.650 0.565 0.607 -0.009 -0.077 -0.139 412 PRO EEE O   
5751  C CB  . PRO E 83  ? 0.609 0.504 0.632 -0.014 -0.075 -0.115 412 PRO EEE CB  
5752  C CG  . PRO E 83  ? 0.594 0.507 0.612 -0.016 -0.078 -0.101 412 PRO EEE CG  
5753  C CD  . PRO E 83  ? 0.569 0.486 0.572 -0.009 -0.067 -0.091 412 PRO EEE CD  
5754  N N   . GLY E 84  ? 0.634 0.524 0.606 -0.000 -0.066 -0.160 413 GLY EEE N   
5755  C CA  . GLY E 84  ? 0.666 0.555 0.614 -0.001 -0.069 -0.185 413 GLY EEE CA  
5756  C C   . GLY E 84  ? 0.701 0.609 0.616 0.005  -0.059 -0.187 413 GLY EEE C   
5757  O O   . GLY E 84  ? 0.750 0.664 0.638 0.004  -0.062 -0.205 413 GLY EEE O   
5758  N N   . GLN E 85  ? 0.706 0.625 0.623 0.010  -0.049 -0.168 414 GLN EEE N   
5759  C CA  . GLN E 85  ? 0.680 0.619 0.569 0.013  -0.039 -0.164 414 GLN EEE CA  
5760  C C   . GLN E 85  ? 0.683 0.624 0.574 0.024  -0.023 -0.177 414 GLN EEE C   
5761  O O   . GLN E 85  ? 0.683 0.610 0.603 0.030  -0.019 -0.180 414 GLN EEE O   
5762  C CB  . GLN E 85  ? 0.662 0.610 0.556 0.012  -0.036 -0.138 414 GLN EEE CB  
5763  C CG  . GLN E 85  ? 0.663 0.612 0.553 0.005  -0.049 -0.125 414 GLN EEE CG  
5764  C CD  . GLN E 85  ? 0.667 0.629 0.526 0.001  -0.056 -0.128 414 GLN EEE CD  
5765  O OE1 . GLN E 85  ? 0.729 0.702 0.563 0.003  -0.047 -0.129 414 GLN EEE OE1 
5766  N NE2 . GLN E 85  ? 0.694 0.656 0.555 -0.004 -0.071 -0.127 414 GLN EEE NE2 
5767  N N   . THR E 86  ? 0.701 0.660 0.563 0.026  -0.013 -0.183 415 THR EEE N   
5768  C CA  . THR E 86  ? 0.717 0.687 0.583 0.036  0.006  -0.191 415 THR EEE CA  
5769  C C   . THR E 86  ? 0.701 0.696 0.553 0.034  0.017  -0.171 415 THR EEE C   
5770  O O   . THR E 86  ? 0.714 0.715 0.547 0.025  0.008  -0.155 415 THR EEE O   
5771  C CB  . THR E 86  ? 0.761 0.729 0.607 0.043  0.013  -0.222 415 THR EEE CB  
5772  O OG1 . THR E 86  ? 0.754 0.733 0.556 0.035  0.007  -0.225 415 THR EEE OG1 
5773  C CG2 . THR E 86  ? 0.784 0.721 0.650 0.046  0.005  -0.243 415 THR EEE CG2 
5774  N N   . GLY E 87  ? 0.681 0.693 0.547 0.042  0.034  -0.171 416 GLY EEE N   
5775  C CA  . GLY E 87  ? 0.648 0.685 0.511 0.038  0.045  -0.151 416 GLY EEE CA  
5776  C C   . GLY E 87  ? 0.633 0.678 0.537 0.044  0.053  -0.143 416 GLY EEE C   
5777  O O   . GLY E 87  ? 0.594 0.622 0.524 0.051  0.047  -0.149 416 GLY EEE O   
5778  N N   . LYS E 88  ? 0.658 0.729 0.568 0.041  0.064  -0.127 417 LYS EEE N   
5779  C CA  . LYS E 88  ? 0.660 0.746 0.610 0.045  0.070  -0.118 417 LYS EEE CA  
5780  C C   . LYS E 88  ? 0.637 0.703 0.609 0.042  0.053  -0.108 417 LYS EEE C   
5781  O O   . LYS E 88  ? 0.655 0.721 0.660 0.051  0.052  -0.111 417 LYS EEE O   
5782  C CB  . LYS E 88  ? 0.703 0.818 0.657 0.035  0.079  -0.097 417 LYS EEE CB  
5783  C CG  . LYS E 88  ? 0.787 0.930 0.722 0.036  0.100  -0.100 417 LYS EEE CG  
5784  C CD  . LYS E 88  ? 0.845 1.003 0.798 0.054  0.116  -0.121 417 LYS EEE CD  
5785  C CE  . LYS E 88  ? 0.911 1.097 0.840 0.058  0.139  -0.130 417 LYS EEE CE  
5786  N NZ  . LYS E 88  ? 0.953 1.130 0.867 0.074  0.148  -0.162 417 LYS EEE NZ  
5787  N N   . ILE E 89  ? 0.597 0.646 0.552 0.031  0.039  -0.098 418 ILE EEE N   
5788  C CA  . ILE E 89  ? 0.576 0.611 0.549 0.026  0.025  -0.087 418 ILE EEE CA  
5789  C C   . ILE E 89  ? 0.568 0.580 0.550 0.034  0.017  -0.098 418 ILE EEE C   
5790  O O   . ILE E 89  ? 0.524 0.534 0.533 0.040  0.015  -0.095 418 ILE EEE O   
5791  C CB  . ILE E 89  ? 0.577 0.602 0.532 0.014  0.017  -0.073 418 ILE EEE CB  
5792  C CG1 . ILE E 89  ? 0.596 0.639 0.545 0.005  0.025  -0.061 418 ILE EEE CG1 
5793  C CG2 . ILE E 89  ? 0.551 0.564 0.521 0.010  0.006  -0.065 418 ILE EEE CG2 
5794  C CD1 . ILE E 89  ? 0.610 0.676 0.588 0.004  0.031  -0.054 418 ILE EEE CD1 
5795  N N   . ALA E 90  ? 0.592 0.588 0.553 0.034  0.013  -0.110 419 ALA EEE N   
5796  C CA  . ALA E 90  ? 0.603 0.576 0.574 0.038  0.005  -0.122 419 ALA EEE CA  
5797  C C   . ALA E 90  ? 0.619 0.591 0.614 0.051  0.013  -0.134 419 ALA EEE C   
5798  O O   . ALA E 90  ? 0.610 0.565 0.629 0.055  0.007  -0.132 419 ALA EEE O   
5799  C CB  . ALA E 90  ? 0.623 0.586 0.568 0.034  -0.000 -0.135 419 ALA EEE CB  
5800  N N   . ASP E 91  ? 0.623 0.613 0.615 0.059  0.028  -0.145 420 ASP EEE N   
5801  C CA  . ASP E 91  ? 0.645 0.632 0.660 0.075  0.038  -0.162 420 ASP EEE CA  
5802  C C   . ASP E 91  ? 0.633 0.636 0.687 0.083  0.041  -0.146 420 ASP EEE C   
5803  O O   . ASP E 91  ? 0.658 0.648 0.742 0.095  0.040  -0.150 420 ASP EEE O   
5804  C CB  . ASP E 91  ? 0.680 0.683 0.673 0.081  0.055  -0.182 420 ASP EEE CB  
5805  C CG  . ASP E 91  ? 0.731 0.720 0.684 0.075  0.050  -0.201 420 ASP EEE CG  
5806  O OD1 . ASP E 91  ? 0.741 0.706 0.691 0.067  0.033  -0.201 420 ASP EEE OD1 
5807  O OD2 . ASP E 91  ? 0.761 0.767 0.685 0.077  0.063  -0.213 420 ASP EEE OD2 
5808  N N   . TYR E 92  ? 0.600 0.630 0.656 0.076  0.044  -0.128 421 TYR EEE N   
5809  C CA  . TYR E 92  ? 0.576 0.632 0.669 0.083  0.049  -0.116 421 TYR EEE CA  
5810  C C   . TYR E 92  ? 0.529 0.590 0.632 0.072  0.034  -0.092 421 TYR EEE C   
5811  O O   . TYR E 92  ? 0.506 0.588 0.643 0.077  0.034  -0.081 421 TYR EEE O   
5812  C CB  . TYR E 92  ? 0.588 0.679 0.679 0.085  0.067  -0.118 421 TYR EEE CB  
5813  C CG  . TYR E 92  ? 0.629 0.723 0.710 0.098  0.085  -0.143 421 TYR EEE CG  
5814  C CD1 . TYR E 92  ? 0.661 0.728 0.748 0.111  0.086  -0.164 421 TYR EEE CD1 
5815  C CD2 . TYR E 92  ? 0.668 0.793 0.734 0.096  0.103  -0.145 421 TYR EEE CD2 
5816  C CE1 . TYR E 92  ? 0.699 0.769 0.775 0.124  0.103  -0.191 421 TYR EEE CE1 
5817  C CE2 . TYR E 92  ? 0.728 0.859 0.781 0.108  0.122  -0.169 421 TYR EEE CE2 
5818  C CZ  . TYR E 92  ? 0.734 0.837 0.790 0.123  0.122  -0.194 421 TYR EEE CZ  
5819  O OH  . TYR E 92  ? 0.790 0.897 0.831 0.135  0.141  -0.222 421 TYR EEE OH  
5820  N N   . ASN E 93  ? 0.521 0.566 0.599 0.058  0.023  -0.085 422 ASN EEE N   
5821  C CA  . ASN E 93  ? 0.505 0.555 0.586 0.047  0.011  -0.066 422 ASN EEE CA  
5822  C C   . ASN E 93  ? 0.501 0.525 0.575 0.043  -0.002 -0.061 422 ASN EEE C   
5823  O O   . ASN E 93  ? 0.493 0.521 0.585 0.044  -0.011 -0.049 422 ASN EEE O   
5824  C CB  . ASN E 93  ? 0.503 0.564 0.562 0.032  0.014  -0.061 422 ASN EEE CB  
5825  C CG  . ASN E 93  ? 0.524 0.617 0.595 0.033  0.027  -0.060 422 ASN EEE CG  
5826  O OD1 . ASN E 93  ? 0.513 0.627 0.606 0.027  0.025  -0.048 422 ASN EEE OD1 
5827  N ND2 . ASN E 93  ? 0.514 0.613 0.574 0.039  0.042  -0.072 422 ASN EEE ND2 
5828  N N   . TYR E 94  ? 0.511 0.515 0.561 0.039  -0.004 -0.068 423 TYR EEE N   
5829  C CA  . TYR E 94  ? 0.500 0.481 0.543 0.034  -0.015 -0.063 423 TYR EEE CA  
5830  C C   . TYR E 94  ? 0.510 0.471 0.542 0.035  -0.015 -0.077 423 TYR EEE C   
5831  O O   . TYR E 94  ? 0.516 0.478 0.526 0.030  -0.012 -0.084 423 TYR EEE O   
5832  C CB  . TYR E 94  ? 0.502 0.485 0.528 0.022  -0.020 -0.053 423 TYR EEE CB  
5833  C CG  . TYR E 94  ? 0.532 0.499 0.553 0.018  -0.027 -0.046 423 TYR EEE CG  
5834  C CD1 . TYR E 94  ? 0.563 0.533 0.594 0.018  -0.033 -0.034 423 TYR EEE CD1 
5835  C CD2 . TYR E 94  ? 0.546 0.499 0.554 0.015  -0.029 -0.051 423 TYR EEE CD2 
5836  C CE1 . TYR E 94  ? 0.571 0.531 0.596 0.014  -0.038 -0.027 423 TYR EEE CE1 
5837  C CE2 . TYR E 94  ? 0.534 0.477 0.541 0.012  -0.033 -0.044 423 TYR EEE CE2 
5838  C CZ  . TYR E 94  ? 0.546 0.492 0.560 0.011  -0.037 -0.032 423 TYR EEE CZ  
5839  O OH  . TYR E 94  ? 0.525 0.464 0.536 0.008  -0.039 -0.024 423 TYR EEE OH  
5840  N N   . LYS E 95  ? 0.513 0.457 0.562 0.041  -0.018 -0.079 424 LYS EEE N   
5841  C CA  . LYS E 95  ? 0.541 0.465 0.587 0.041  -0.020 -0.093 424 LYS EEE CA  
5842  C C   . LYS E 95  ? 0.535 0.444 0.584 0.033  -0.029 -0.083 424 LYS EEE C   
5843  O O   . LYS E 95  ? 0.530 0.434 0.598 0.035  -0.032 -0.070 424 LYS EEE O   
5844  C CB  . LYS E 95  ? 0.579 0.492 0.647 0.053  -0.016 -0.106 424 LYS EEE CB  
5845  C CG  . LYS E 95  ? 0.617 0.506 0.682 0.052  -0.019 -0.126 424 LYS EEE CG  
5846  C CD  . LYS E 95  ? 0.629 0.524 0.662 0.045  -0.019 -0.140 424 LYS EEE CD  
5847  C CE  . LYS E 95  ? 0.659 0.535 0.686 0.045  -0.021 -0.166 424 LYS EEE CE  
5848  N NZ  . LYS E 95  ? 0.670 0.556 0.665 0.036  -0.026 -0.173 424 LYS EEE NZ  
5849  N N   . LEU E 96  ? 0.574 0.479 0.607 0.025  -0.033 -0.088 425 LEU EEE N   
5850  C CA  . LEU E 96  ? 0.564 0.458 0.605 0.018  -0.040 -0.081 425 LEU EEE CA  
5851  C C   . LEU E 96  ? 0.572 0.447 0.628 0.018  -0.044 -0.094 425 LEU EEE C   
5852  O O   . LEU E 96  ? 0.602 0.474 0.649 0.020  -0.043 -0.114 425 LEU EEE O   
5853  C CB  . LEU E 96  ? 0.582 0.484 0.604 0.010  -0.043 -0.078 425 LEU EEE CB  
5854  C CG  . LEU E 96  ? 0.594 0.508 0.606 0.008  -0.040 -0.064 425 LEU EEE CG  
5855  C CD1 . LEU E 96  ? 0.600 0.518 0.600 0.003  -0.043 -0.064 425 LEU EEE CD1 
5856  C CD2 . LEU E 96  ? 0.616 0.529 0.640 0.008  -0.040 -0.049 425 LEU EEE CD2 
5857  N N   . PRO E 97  ? 0.582 0.443 0.660 0.014  -0.048 -0.084 426 PRO EEE N   
5858  C CA  . PRO E 97  ? 0.594 0.433 0.690 0.010  -0.053 -0.097 426 PRO EEE CA  
5859  C C   . PRO E 97  ? 0.585 0.427 0.669 -0.000 -0.061 -0.110 426 PRO EEE C   
5860  O O   . PRO E 97  ? 0.588 0.447 0.658 -0.004 -0.062 -0.101 426 PRO EEE O   
5861  C CB  . PRO E 97  ? 0.590 0.418 0.712 0.006  -0.055 -0.076 426 PRO EEE CB  
5862  C CG  . PRO E 97  ? 0.577 0.426 0.685 0.003  -0.052 -0.056 426 PRO EEE CG  
5863  C CD  . PRO E 97  ? 0.557 0.424 0.643 0.011  -0.048 -0.061 426 PRO EEE CD  
5864  N N   . ASP E 98  ? 0.631 0.456 0.722 -0.004 -0.067 -0.130 427 ASP EEE N   
5865  C CA  . ASP E 98  ? 0.665 0.497 0.746 -0.015 -0.077 -0.142 427 ASP EEE CA  
5866  C C   . ASP E 98  ? 0.632 0.469 0.733 -0.027 -0.083 -0.124 427 ASP EEE C   
5867  O O   . ASP E 98  ? 0.610 0.466 0.703 -0.033 -0.090 -0.124 427 ASP EEE O   
5868  C CB  . ASP E 98  ? 0.750 0.562 0.828 -0.018 -0.083 -0.173 427 ASP EEE CB  
5869  C CG  . ASP E 98  ? 0.834 0.660 0.892 -0.028 -0.096 -0.187 427 ASP EEE CG  
5870  O OD1 . ASP E 98  ? 0.858 0.703 0.882 -0.023 -0.094 -0.192 427 ASP EEE OD1 
5871  O OD2 . ASP E 98  ? 0.863 0.683 0.940 -0.042 -0.109 -0.192 427 ASP EEE OD2 
5872  N N   . ASP E 99  ? 0.608 0.433 0.737 -0.029 -0.080 -0.107 428 ASP EEE N   
5873  C CA  . ASP E 99  ? 0.614 0.447 0.766 -0.040 -0.082 -0.087 428 ASP EEE CA  
5874  C C   . ASP E 99  ? 0.595 0.447 0.739 -0.035 -0.072 -0.063 428 ASP EEE C   
5875  O O   . ASP E 99  ? 0.600 0.456 0.762 -0.040 -0.068 -0.042 428 ASP EEE O   
5876  C CB  . ASP E 99  ? 0.631 0.438 0.818 -0.049 -0.085 -0.083 428 ASP EEE CB  
5877  C CG  . ASP E 99  ? 0.654 0.446 0.852 -0.040 -0.077 -0.067 428 ASP EEE CG  
5878  O OD1 . ASP E 99  ? 0.658 0.457 0.836 -0.026 -0.070 -0.065 428 ASP EEE OD1 
5879  O OD2 . ASP E 99  ? 0.677 0.451 0.907 -0.047 -0.078 -0.053 428 ASP EEE OD2 
5880  N N   . PHE E 100 ? 0.570 0.434 0.686 -0.025 -0.067 -0.065 429 PHE EEE N   
5881  C CA  . PHE E 100 ? 0.580 0.460 0.683 -0.021 -0.059 -0.047 429 PHE EEE CA  
5882  C C   . PHE E 100 ? 0.538 0.433 0.651 -0.028 -0.057 -0.033 429 PHE EEE C   
5883  O O   . PHE E 100 ? 0.545 0.451 0.662 -0.032 -0.062 -0.039 429 PHE EEE O   
5884  C CB  . PHE E 100 ? 0.581 0.471 0.655 -0.014 -0.056 -0.055 429 PHE EEE CB  
5885  C CG  . PHE E 100 ? 0.568 0.471 0.627 -0.010 -0.049 -0.042 429 PHE EEE CG  
5886  C CD1 . PHE E 100 ? 0.570 0.472 0.631 -0.008 -0.045 -0.029 429 PHE EEE CD1 
5887  C CD2 . PHE E 100 ? 0.542 0.457 0.586 -0.010 -0.048 -0.043 429 PHE EEE CD2 
5888  C CE1 . PHE E 100 ? 0.555 0.467 0.599 -0.006 -0.039 -0.020 429 PHE EEE CE1 
5889  C CE2 . PHE E 100 ? 0.551 0.473 0.582 -0.007 -0.042 -0.034 429 PHE EEE CE2 
5890  C CZ  . PHE E 100 ? 0.571 0.491 0.599 -0.006 -0.038 -0.025 429 PHE EEE CZ  
5891  N N   . THR E 101 ? 0.523 0.423 0.638 -0.028 -0.049 -0.014 430 THR EEE N   
5892  C CA  . THR E 101 ? 0.540 0.459 0.658 -0.031 -0.041 -0.001 430 THR EEE CA  
5893  C C   . THR E 101 ? 0.532 0.461 0.623 -0.023 -0.033 0.003  430 THR EEE C   
5894  O O   . THR E 101 ? 0.525 0.449 0.606 -0.021 -0.030 0.013  430 THR EEE O   
5895  C CB  . THR E 101 ? 0.545 0.463 0.688 -0.039 -0.037 0.018  430 THR EEE CB  
5896  O OG1 . THR E 101 ? 0.556 0.460 0.727 -0.048 -0.046 0.012  430 THR EEE OG1 
5897  C CG2 . THR E 101 ? 0.544 0.486 0.693 -0.042 -0.027 0.030  430 THR EEE CG2 
5898  N N   . GLY E 102 ? 0.548 0.487 0.626 -0.020 -0.031 -0.003 431 GLY EEE N   
5899  C CA  . GLY E 102 ? 0.546 0.489 0.597 -0.013 -0.024 -0.002 431 GLY EEE CA  
5900  C C   . GLY E 102 ? 0.535 0.481 0.576 -0.009 -0.026 -0.013 431 GLY EEE C   
5901  O O   . GLY E 102 ? 0.536 0.487 0.591 -0.010 -0.032 -0.017 431 GLY EEE O   
5902  N N   . CYS E 103 ? 0.524 0.467 0.542 -0.004 -0.022 -0.016 432 CYS EEE N   
5903  C CA  . CYS E 103 ? 0.546 0.489 0.555 0.000  -0.023 -0.023 432 CYS EEE CA  
5904  C C   . CYS E 103 ? 0.524 0.457 0.513 0.001  -0.026 -0.028 432 CYS EEE C   
5905  O O   . CYS E 103 ? 0.524 0.455 0.505 -0.001 -0.025 -0.027 432 CYS EEE O   
5906  C CB  . CYS E 103 ? 0.557 0.504 0.563 0.005  -0.013 -0.021 432 CYS EEE CB  
5907  S SG  . CYS E 103 ? 0.587 0.552 0.619 0.004  -0.006 -0.012 432 CYS EEE SG  
5908  N N   . VAL E 104 ? 0.506 0.438 0.490 0.003  -0.030 -0.033 433 VAL EEE N   
5909  C CA  . VAL E 104 ? 0.512 0.437 0.480 0.002  -0.031 -0.036 433 VAL EEE CA  
5910  C C   . VAL E 104 ? 0.522 0.441 0.482 0.005  -0.029 -0.035 433 VAL EEE C   
5911  O O   . VAL E 104 ? 0.526 0.447 0.493 0.008  -0.031 -0.033 433 VAL EEE O   
5912  C CB  . VAL E 104 ? 0.534 0.461 0.501 0.001  -0.037 -0.041 433 VAL EEE CB  
5913  C CG1 . VAL E 104 ? 0.541 0.467 0.493 -0.000 -0.036 -0.042 433 VAL EEE CG1 
5914  C CG2 . VAL E 104 ? 0.535 0.463 0.513 -0.000 -0.039 -0.044 433 VAL EEE CG2 
5915  N N   . ILE E 105 ? 0.497 0.407 0.445 0.002  -0.025 -0.036 434 ILE EEE N   
5916  C CA  . ILE E 105 ? 0.525 0.423 0.467 0.004  -0.022 -0.037 434 ILE EEE CA  
5917  C C   . ILE E 105 ? 0.532 0.424 0.464 -0.002 -0.023 -0.037 434 ILE EEE C   
5918  O O   . ILE E 105 ? 0.558 0.456 0.486 -0.008 -0.024 -0.039 434 ILE EEE O   
5919  C CB  . ILE E 105 ? 0.538 0.430 0.476 0.007  -0.014 -0.041 434 ILE EEE CB  
5920  C CG1 . ILE E 105 ? 0.539 0.442 0.491 0.012  -0.010 -0.039 434 ILE EEE CG1 
5921  C CG2 . ILE E 105 ? 0.547 0.420 0.480 0.009  -0.011 -0.045 434 ILE EEE CG2 
5922  C CD1 . ILE E 105 ? 0.556 0.461 0.501 0.013  -0.000 -0.043 434 ILE EEE CD1 
5923  N N   . ALA E 106 ? 0.544 0.426 0.473 -0.002 -0.024 -0.033 435 ALA EEE N   
5924  C CA  . ALA E 106 ? 0.552 0.429 0.475 -0.010 -0.025 -0.030 435 ALA EEE CA  
5925  C C   . ALA E 106 ? 0.592 0.447 0.514 -0.009 -0.023 -0.027 435 ALA EEE C   
5926  O O   . ALA E 106 ? 0.632 0.481 0.561 -0.000 -0.023 -0.024 435 ALA EEE O   
5927  C CB  . ALA E 106 ? 0.535 0.426 0.456 -0.011 -0.027 -0.025 435 ALA EEE CB  
5928  N N   . TRP E 107 ? 0.584 0.429 0.503 -0.019 -0.022 -0.027 436 TRP EEE N   
5929  C CA  . TRP E 107 ? 0.589 0.407 0.510 -0.021 -0.021 -0.023 436 TRP EEE CA  
5930  C C   . TRP E 107 ? 0.580 0.397 0.501 -0.035 -0.022 -0.016 436 TRP EEE C   
5931  O O   . TRP E 107 ? 0.574 0.408 0.494 -0.044 -0.023 -0.020 436 TRP EEE O   
5932  C CB  . TRP E 107 ? 0.591 0.388 0.511 -0.019 -0.018 -0.036 436 TRP EEE CB  
5933  C CG  . TRP E 107 ? 0.597 0.396 0.509 -0.029 -0.019 -0.049 436 TRP EEE CG  
5934  C CD1 . TRP E 107 ? 0.609 0.391 0.518 -0.042 -0.021 -0.054 436 TRP EEE CD1 
5935  C CD2 . TRP E 107 ? 0.584 0.403 0.488 -0.029 -0.019 -0.056 436 TRP EEE CD2 
5936  N NE1 . TRP E 107 ? 0.622 0.416 0.522 -0.050 -0.024 -0.066 436 TRP EEE NE1 
5937  C CE2 . TRP E 107 ? 0.583 0.399 0.479 -0.042 -0.023 -0.066 436 TRP EEE CE2 
5938  C CE3 . TRP E 107 ? 0.578 0.417 0.484 -0.021 -0.018 -0.055 436 TRP EEE CE3 
5939  C CZ2 . TRP E 107 ? 0.601 0.435 0.488 -0.045 -0.026 -0.072 436 TRP EEE CZ2 
5940  C CZ3 . TRP E 107 ? 0.567 0.421 0.465 -0.024 -0.020 -0.060 436 TRP EEE CZ3 
5941  C CH2 . TRP E 107 ? 0.587 0.439 0.475 -0.035 -0.024 -0.067 436 TRP EEE CH2 
5942  N N   . ASN E 108 ? 0.596 0.396 0.520 -0.037 -0.021 -0.003 437 ASN EEE N   
5943  C CA  . ASN E 108 ? 0.616 0.410 0.542 -0.052 -0.021 0.006  437 ASN EEE CA  
5944  C C   . ASN E 108 ? 0.625 0.405 0.555 -0.064 -0.022 -0.008 437 ASN EEE C   
5945  O O   . ASN E 108 ? 0.627 0.380 0.556 -0.060 -0.022 -0.020 437 ASN EEE O   
5946  C CB  . ASN E 108 ? 0.638 0.410 0.568 -0.050 -0.020 0.024  437 ASN EEE CB  
5947  C CG  . ASN E 108 ? 0.681 0.452 0.615 -0.067 -0.018 0.039  437 ASN EEE CG  
5948  O OD1 . ASN E 108 ? 0.709 0.464 0.651 -0.080 -0.018 0.032  437 ASN EEE OD1 
5949  N ND2 . ASN E 108 ? 0.685 0.475 0.613 -0.066 -0.016 0.058  437 ASN EEE ND2 
5950  N N   . SER E 109 ? 0.610 0.409 0.544 -0.078 -0.023 -0.008 438 SER EEE N   
5951  C CA  . SER E 109 ? 0.623 0.414 0.561 -0.093 -0.027 -0.021 438 SER EEE CA  
5952  C C   . SER E 109 ? 0.656 0.446 0.608 -0.112 -0.027 -0.009 438 SER EEE C   
5953  O O   . SER E 109 ? 0.681 0.481 0.641 -0.128 -0.032 -0.015 438 SER EEE O   
5954  C CB  . SER E 109 ? 0.599 0.420 0.534 -0.093 -0.031 -0.031 438 SER EEE CB  
5955  O OG  . SER E 109 ? 0.574 0.429 0.517 -0.094 -0.029 -0.020 438 SER EEE OG  
5956  N N   . ASN E 110 ? 0.666 0.445 0.622 -0.112 -0.023 0.010  439 ASN EEE N   
5957  C CA  . ASN E 110 ? 0.686 0.464 0.657 -0.131 -0.020 0.027  439 ASN EEE CA  
5958  C C   . ASN E 110 ? 0.710 0.458 0.691 -0.149 -0.027 0.014  439 ASN EEE C   
5959  O O   . ASN E 110 ? 0.698 0.463 0.696 -0.168 -0.029 0.017  439 ASN EEE O   
5960  C CB  . ASN E 110 ? 0.704 0.466 0.673 -0.127 -0.015 0.051  439 ASN EEE CB  
5961  C CG  . ASN E 110 ? 0.718 0.494 0.699 -0.145 -0.009 0.073  439 ASN EEE CG  
5962  O OD1 . ASN E 110 ? 0.716 0.529 0.705 -0.154 -0.006 0.074  439 ASN EEE OD1 
5963  N ND2 . ASN E 110 ? 0.757 0.507 0.743 -0.149 -0.007 0.095  439 ASN EEE ND2 
5964  N N   . ASN E 111 ? 0.731 0.441 0.706 -0.142 -0.030 -0.002 440 ASN EEE N   
5965  C CA  . ASN E 111 ? 0.768 0.441 0.749 -0.159 -0.036 -0.017 440 ASN EEE CA  
5966  C C   . ASN E 111 ? 0.756 0.454 0.736 -0.173 -0.045 -0.036 440 ASN EEE C   
5967  O O   . ASN E 111 ? 0.775 0.457 0.766 -0.194 -0.052 -0.045 440 ASN EEE O   
5968  C CB  . ASN E 111 ? 0.806 0.434 0.778 -0.144 -0.035 -0.033 440 ASN EEE CB  
5969  C CG  . ASN E 111 ? 0.874 0.459 0.853 -0.161 -0.040 -0.052 440 ASN EEE CG  
5970  O OD1 . ASN E 111 ? 0.920 0.492 0.917 -0.182 -0.043 -0.041 440 ASN EEE OD1 
5971  N ND2 . ASN E 111 ? 0.893 0.455 0.856 -0.152 -0.041 -0.080 440 ASN EEE ND2 
5972  N N   . LEU E 112 ? 0.721 0.455 0.689 -0.161 -0.046 -0.042 441 LEU EEE N   
5973  C CA  . LEU E 112 ? 0.723 0.483 0.688 -0.171 -0.056 -0.058 441 LEU EEE CA  
5974  C C   . LEU E 112 ? 0.700 0.509 0.684 -0.179 -0.057 -0.043 441 LEU EEE C   
5975  O O   . LEU E 112 ? 0.715 0.542 0.711 -0.197 -0.067 -0.049 441 LEU EEE O   
5976  C CB  . LEU E 112 ? 0.718 0.486 0.660 -0.152 -0.056 -0.072 441 LEU EEE CB  
5977  C CG  . LEU E 112 ? 0.741 0.467 0.664 -0.144 -0.054 -0.092 441 LEU EEE CG  
5978  C CD1 . LEU E 112 ? 0.732 0.475 0.633 -0.128 -0.052 -0.103 441 LEU EEE CD1 
5979  C CD2 . LEU E 112 ? 0.779 0.475 0.700 -0.164 -0.062 -0.112 441 LEU EEE CD2 
5980  N N   . ASP E 113 ? 0.690 0.522 0.678 -0.167 -0.047 -0.025 442 ASP EEE N   
5981  C CA  . ASP E 113 ? 0.667 0.549 0.669 -0.166 -0.045 -0.015 442 ASP EEE CA  
5982  C C   . ASP E 113 ? 0.681 0.579 0.704 -0.177 -0.037 0.006  442 ASP EEE C   
5983  O O   . ASP E 113 ? 0.642 0.583 0.679 -0.175 -0.032 0.014  442 ASP EEE O   
5984  C CB  . ASP E 113 ? 0.634 0.531 0.622 -0.142 -0.039 -0.015 442 ASP EEE CB  
5985  C CG  . ASP E 113 ? 0.638 0.534 0.610 -0.133 -0.047 -0.031 442 ASP EEE CG  
5986  O OD1 . ASP E 113 ? 0.625 0.531 0.601 -0.144 -0.058 -0.040 442 ASP EEE OD1 
5987  O OD2 . ASP E 113 ? 0.607 0.496 0.565 -0.115 -0.042 -0.033 442 ASP EEE OD2 
5988  N N   . SER E 114 ? 0.733 0.601 0.761 -0.189 -0.034 0.016  443 SER EEE N   
5989  C CA  . SER E 114 ? 0.796 0.681 0.845 -0.203 -0.024 0.039  443 SER EEE CA  
5990  C C   . SER E 114 ? 0.873 0.744 0.946 -0.231 -0.032 0.039  443 SER EEE C   
5991  O O   . SER E 114 ? 0.923 0.754 0.988 -0.236 -0.042 0.021  443 SER EEE O   
5992  C CB  . SER E 114 ? 0.812 0.679 0.846 -0.192 -0.013 0.057  443 SER EEE CB  
5993  O OG  . SER E 114 ? 0.857 0.675 0.892 -0.201 -0.016 0.061  443 SER EEE OG  
5994  N N   . LYS E 115 ? 0.959 0.863 1.061 -0.249 -0.027 0.055  444 LYS EEE N   
5995  C CA  . LYS E 115 ? 1.023 0.917 1.154 -0.281 -0.036 0.056  444 LYS EEE CA  
5996  C C   . LYS E 115 ? 1.008 0.908 1.159 -0.295 -0.022 0.087  444 LYS EEE C   
5997  O O   . LYS E 115 ? 0.958 0.892 1.105 -0.283 -0.006 0.104  444 LYS EEE O   
5998  C CB  . LYS E 115 ? 1.068 1.009 1.224 -0.293 -0.047 0.047  444 LYS EEE CB  
5999  C CG  . LYS E 115 ? 1.142 1.063 1.286 -0.298 -0.067 0.018  444 LYS EEE CG  
6000  C CD  . LYS E 115 ? 1.180 1.150 1.332 -0.294 -0.078 0.008  444 LYS EEE CD  
6001  C CE  . LYS E 115 ? 1.241 1.192 1.358 -0.279 -0.089 -0.016 444 LYS EEE CE  
6002  N NZ  . LYS E 115 ? 1.242 1.237 1.357 -0.260 -0.091 -0.017 444 LYS EEE NZ  
6003  N N   . VAL E 116 ? 1.048 0.917 1.221 -0.322 -0.027 0.092  445 VAL EEE N   
6004  C CA  . VAL E 116 ? 1.075 0.956 1.277 -0.344 -0.016 0.124  445 VAL EEE CA  
6005  C C   . VAL E 116 ? 1.017 0.972 1.249 -0.352 -0.010 0.131  445 VAL EEE C   
6006  O O   . VAL E 116 ? 0.996 0.974 1.244 -0.359 -0.024 0.112  445 VAL EEE O   
6007  C CB  . VAL E 116 ? 1.154 0.985 1.378 -0.373 -0.025 0.125  445 VAL EEE CB  
6008  C CG1 . VAL E 116 ? 1.188 0.949 1.386 -0.360 -0.026 0.124  445 VAL EEE CG1 
6009  C CG2 . VAL E 116 ? 1.181 1.011 1.423 -0.393 -0.046 0.097  445 VAL EEE CG2 
6010  N N   . GLY E 117 ? 0.980 0.973 1.215 -0.346 0.011  0.157  446 GLY EEE N   
6011  C CA  . GLY E 117 ? 0.947 1.013 1.210 -0.347 0.021  0.165  446 GLY EEE CA  
6012  C C   . GLY E 117 ? 0.911 1.007 1.153 -0.316 0.022  0.147  446 GLY EEE C   
6013  O O   . GLY E 117 ? 0.885 1.040 1.150 -0.313 0.033  0.152  446 GLY EEE O   
6014  N N   . GLY E 118 ? 0.916 0.974 1.119 -0.294 0.014  0.128  447 GLY EEE N   
6015  C CA  . GLY E 118 ? 0.853 0.931 1.031 -0.263 0.019  0.116  447 GLY EEE CA  
6016  C C   . GLY E 118 ? 0.823 0.913 1.007 -0.257 0.002  0.092  447 GLY EEE C   
6017  O O   . GLY E 118 ? 0.799 0.921 1.019 -0.274 -0.006 0.091  447 GLY EEE O   
6018  N N   . ASN E 119 ? 0.780 0.847 0.931 -0.235 -0.004 0.074  448 ASN EEE N   
6019  C CA  . ASN E 119 ? 0.744 0.825 0.895 -0.225 -0.018 0.055  448 ASN EEE CA  
6020  C C   . ASN E 119 ? 0.713 0.839 0.870 -0.203 -0.007 0.057  448 ASN EEE C   
6021  O O   . ASN E 119 ? 0.742 0.857 0.872 -0.183 0.004  0.056  448 ASN EEE O   
6022  C CB  . ASN E 119 ? 0.735 0.769 0.851 -0.214 -0.030 0.037  448 ASN EEE CB  
6023  C CG  . ASN E 119 ? 0.698 0.746 0.810 -0.204 -0.043 0.020  448 ASN EEE CG  
6024  O OD1 . ASN E 119 ? 0.711 0.800 0.850 -0.209 -0.049 0.022  448 ASN EEE OD1 
6025  N ND2 . ASN E 119 ? 0.698 0.715 0.779 -0.190 -0.048 0.007  448 ASN EEE ND2 
6026  N N   . TYR E 120 ? 0.711 0.885 0.904 -0.207 -0.010 0.058  449 TYR EEE N   
6027  C CA  . TYR E 120 ? 0.690 0.909 0.898 -0.187 0.002  0.060  449 TYR EEE CA  
6028  C C   . TYR E 120 ? 0.655 0.878 0.861 -0.172 -0.013 0.046  449 TYR EEE C   
6029  O O   . TYR E 120 ? 0.646 0.904 0.870 -0.154 -0.007 0.046  449 TYR EEE O   
6030  C CB  . TYR E 120 ? 0.709 0.982 0.963 -0.199 0.015  0.076  449 TYR EEE CB  
6031  C CG  . TYR E 120 ? 0.771 1.039 1.019 -0.210 0.034  0.093  449 TYR EEE CG  
6032  C CD1 . TYR E 120 ? 0.808 1.079 1.031 -0.192 0.056  0.097  449 TYR EEE CD1 
6033  C CD2 . TYR E 120 ? 0.830 1.088 1.095 -0.240 0.030  0.106  449 TYR EEE CD2 
6034  C CE1 . TYR E 120 ? 0.834 1.102 1.046 -0.203 0.072  0.115  449 TYR EEE CE1 
6035  C CE2 . TYR E 120 ? 0.864 1.115 1.122 -0.250 0.048  0.125  449 TYR EEE CE2 
6036  C CZ  . TYR E 120 ? 0.875 1.132 1.106 -0.231 0.069  0.131  449 TYR EEE CZ  
6037  O OH  . TYR E 120 ? 0.890 1.143 1.110 -0.241 0.085  0.153  449 TYR EEE OH  
6038  N N   . ASN E 121 ? 0.629 0.818 0.814 -0.177 -0.032 0.034  450 ASN EEE N   
6039  C CA  . ASN E 121 ? 0.615 0.808 0.795 -0.165 -0.048 0.024  450 ASN EEE CA  
6040  C C   . ASN E 121 ? 0.565 0.746 0.722 -0.138 -0.040 0.018  450 ASN EEE C   
6041  O O   . ASN E 121 ? 0.543 0.742 0.709 -0.124 -0.046 0.017  450 ASN EEE O   
6042  C CB  . ASN E 121 ? 0.646 0.807 0.805 -0.180 -0.068 0.012  450 ASN EEE CB  
6043  C CG  . ASN E 121 ? 0.704 0.887 0.894 -0.207 -0.082 0.015  450 ASN EEE CG  
6044  O OD1 . ASN E 121 ? 0.676 0.907 0.908 -0.212 -0.081 0.026  450 ASN EEE OD1 
6045  N ND2 . ASN E 121 ? 0.774 0.923 0.944 -0.225 -0.096 0.003  450 ASN EEE ND2 
6046  N N   . TYR E 122 ? 0.544 0.694 0.672 -0.130 -0.027 0.017  451 TYR EEE N   
6047  C CA  . TYR E 122 ? 0.522 0.658 0.627 -0.106 -0.022 0.010  451 TYR EEE CA  
6048  C C   . TYR E 122 ? 0.509 0.675 0.630 -0.092 -0.004 0.014  451 TYR EEE C   
6049  O O   . TYR E 122 ? 0.501 0.677 0.625 -0.097 0.010  0.021  451 TYR EEE O   
6050  C CB  . TYR E 122 ? 0.522 0.614 0.591 -0.105 -0.020 0.006  451 TYR EEE CB  
6051  C CG  . TYR E 122 ? 0.538 0.599 0.590 -0.114 -0.034 -0.002 451 TYR EEE CG  
6052  C CD1 . TYR E 122 ? 0.538 0.593 0.579 -0.105 -0.044 -0.011 451 TYR EEE CD1 
6053  C CD2 . TYR E 122 ? 0.564 0.599 0.609 -0.131 -0.037 -0.002 451 TYR EEE CD2 
6054  C CE1 . TYR E 122 ? 0.544 0.572 0.565 -0.111 -0.055 -0.020 451 TYR EEE CE1 
6055  C CE2 . TYR E 122 ? 0.583 0.588 0.611 -0.137 -0.048 -0.013 451 TYR EEE CE2 
6056  C CZ  . TYR E 122 ? 0.562 0.565 0.576 -0.127 -0.056 -0.023 451 TYR EEE CZ  
6057  O OH  . TYR E 122 ? 0.585 0.561 0.579 -0.132 -0.065 -0.035 451 TYR EEE OH  
6058  N N   . LEU E 123 ? 0.476 0.654 0.607 -0.073 -0.005 0.008  452 LEU EEE N   
6059  C CA  . LEU E 123 ? 0.475 0.680 0.623 -0.056 0.011  0.007  452 LEU EEE CA  
6060  C C   . LEU E 123 ? 0.487 0.666 0.609 -0.038 0.015  -0.004 452 LEU EEE C   
6061  O O   . LEU E 123 ? 0.491 0.639 0.592 -0.037 0.003  -0.008 452 LEU EEE O   
6062  C CB  . LEU E 123 ? 0.472 0.714 0.662 -0.050 0.004  0.012  452 LEU EEE CB  
6063  C CG  . LEU E 123 ? 0.485 0.760 0.708 -0.070 -0.004 0.023  452 LEU EEE CG  
6064  C CD1 . LEU E 123 ? 0.471 0.786 0.738 -0.059 -0.011 0.028  452 LEU EEE CD1 
6065  C CD2 . LEU E 123 ? 0.498 0.794 0.733 -0.082 0.013  0.030  452 LEU EEE CD2 
6066  N N   . TYR E 124 ? 0.472 0.664 0.596 -0.024 0.032  -0.009 453 TYR EEE N   
6067  C CA  . TYR E 124 ? 0.472 0.644 0.579 -0.006 0.037  -0.023 453 TYR EEE CA  
6068  C C   . TYR E 124 ? 0.490 0.690 0.623 0.011  0.051  -0.030 453 TYR EEE C   
6069  O O   . TYR E 124 ? 0.478 0.713 0.632 0.009  0.065  -0.024 453 TYR EEE O   
6070  C CB  . TYR E 124 ? 0.488 0.636 0.554 -0.010 0.042  -0.027 453 TYR EEE CB  
6071  C CG  . TYR E 124 ? 0.502 0.673 0.563 -0.014 0.060  -0.023 453 TYR EEE CG  
6072  C CD1 . TYR E 124 ? 0.524 0.710 0.581 0.001  0.077  -0.035 453 TYR EEE CD1 
6073  C CD2 . TYR E 124 ? 0.516 0.693 0.575 -0.032 0.061  -0.008 453 TYR EEE CD2 
6074  C CE1 . TYR E 124 ? 0.543 0.753 0.590 -0.003 0.096  -0.030 453 TYR EEE CE1 
6075  C CE2 . TYR E 124 ? 0.526 0.725 0.579 -0.037 0.079  -0.001 453 TYR EEE CE2 
6076  C CZ  . TYR E 124 ? 0.548 0.766 0.593 -0.022 0.097  -0.011 453 TYR EEE CZ  
6077  O OH  . TYR E 124 ? 0.593 0.837 0.630 -0.027 0.116  -0.003 453 TYR EEE OH  
6078  N N   . ARG E 125 ? 0.488 0.673 0.625 0.029  0.050  -0.041 454 ARG EEE N   
6079  C CA  . ARG E 125 ? 0.506 0.709 0.667 0.049  0.065  -0.052 454 ARG EEE CA  
6080  C C   . ARG E 125 ? 0.546 0.747 0.677 0.053  0.084  -0.066 454 ARG EEE C   
6081  O O   . ARG E 125 ? 0.560 0.730 0.654 0.050  0.079  -0.075 454 ARG EEE O   
6082  C CB  . ARG E 125 ? 0.497 0.678 0.673 0.065  0.055  -0.058 454 ARG EEE CB  
6083  C CG  . ARG E 125 ? 0.509 0.706 0.719 0.088  0.070  -0.069 454 ARG EEE CG  
6084  C CD  . ARG E 125 ? 0.510 0.683 0.740 0.103  0.058  -0.070 454 ARG EEE CD  
6085  N NE  . ARG E 125 ? 0.496 0.676 0.747 0.096  0.039  -0.049 454 ARG EEE NE  
6086  C CZ  . ARG E 125 ? 0.501 0.719 0.794 0.100  0.036  -0.034 454 ARG EEE CZ  
6087  N NH1 . ARG E 125 ? 0.506 0.760 0.833 0.112  0.053  -0.038 454 ARG EEE NH1 
6088  N NH2 . ARG E 125 ? 0.501 0.724 0.803 0.091  0.015  -0.016 454 ARG EEE NH2 
6089  N N   . LEU E 126 ? 0.575 0.812 0.721 0.058  0.104  -0.067 455 LEU EEE N   
6090  C CA  . LEU E 126 ? 0.654 0.898 0.768 0.060  0.124  -0.079 455 LEU EEE CA  
6091  C C   . LEU E 126 ? 0.678 0.919 0.797 0.083  0.138  -0.104 455 LEU EEE C   
6092  O O   . LEU E 126 ? 0.695 0.923 0.773 0.086  0.147  -0.121 455 LEU EEE O   
6093  C CB  . LEU E 126 ? 0.677 0.966 0.806 0.050  0.141  -0.064 455 LEU EEE CB  
6094  C CG  . LEU E 126 ? 0.728 1.034 0.826 0.051  0.165  -0.071 455 LEU EEE CG  
6095  C CD1 . LEU E 126 ? 0.766 1.039 0.805 0.041  0.157  -0.074 455 LEU EEE CD1 
6096  C CD2 . LEU E 126 ? 0.728 1.081 0.848 0.039  0.181  -0.051 455 LEU EEE CD2 
6097  N N   . PHE E 127 ? 0.708 0.961 0.874 0.099  0.140  -0.106 456 PHE EEE N   
6098  C CA  . PHE E 127 ? 0.771 1.021 0.953 0.125  0.154  -0.130 456 PHE EEE CA  
6099  C C   . PHE E 127 ? 0.739 0.958 0.948 0.136  0.136  -0.130 456 PHE EEE C   
6100  O O   . PHE E 127 ? 0.735 0.964 0.976 0.131  0.120  -0.109 456 PHE EEE O   
6101  C CB  . PHE E 127 ? 0.791 1.092 1.015 0.138  0.178  -0.128 456 PHE EEE CB  
6102  C CG  . PHE E 127 ? 0.839 1.177 1.041 0.126  0.199  -0.123 456 PHE EEE CG  
6103  C CD1 . PHE E 127 ? 0.888 1.218 1.039 0.128  0.215  -0.143 456 PHE EEE CD1 
6104  C CD2 . PHE E 127 ? 0.838 1.218 1.069 0.112  0.201  -0.098 456 PHE EEE CD2 
6105  C CE1 . PHE E 127 ? 0.905 1.268 1.032 0.116  0.234  -0.134 456 PHE EEE CE1 
6106  C CE2 . PHE E 127 ? 0.852 1.264 1.064 0.100  0.221  -0.090 456 PHE EEE CE2 
6107  C CZ  . PHE E 127 ? 0.886 1.290 1.046 0.102  0.238  -0.107 456 PHE EEE CZ  
6108  N N   . ARG E 128 ? 0.732 0.916 0.929 0.150  0.138  -0.154 457 ARG EEE N   
6109  C CA  . ARG E 128 ? 0.727 0.884 0.959 0.164  0.125  -0.155 457 ARG EEE CA  
6110  C C   . ARG E 128 ? 0.781 0.912 1.011 0.184  0.139  -0.187 457 ARG EEE C   
6111  O O   . ARG E 128 ? 0.811 0.931 0.996 0.180  0.148  -0.209 457 ARG EEE O   
6112  C CB  . ARG E 128 ? 0.702 0.824 0.915 0.148  0.099  -0.142 457 ARG EEE CB  
6113  C CG  . ARG E 128 ? 0.706 0.808 0.957 0.159  0.085  -0.131 457 ARG EEE CG  
6114  C CD  . ARG E 128 ? 0.688 0.766 0.919 0.141  0.062  -0.115 457 ARG EEE CD  
6115  N NE  . ARG E 128 ? 0.683 0.752 0.949 0.148  0.047  -0.097 457 ARG EEE NE  
6116  C CZ  . ARG E 128 ? 0.682 0.715 0.961 0.158  0.041  -0.101 457 ARG EEE CZ  
6117  N NH1 . ARG E 128 ? 0.713 0.714 0.975 0.161  0.048  -0.127 457 ARG EEE NH1 
6118  N NH2 . ARG E 128 ? 0.673 0.703 0.983 0.163  0.028  -0.079 457 ARG EEE NH2 
6119  N N   . LYS E 129 ? 0.786 0.910 1.065 0.206  0.140  -0.189 458 LYS EEE N   
6120  C CA  . LYS E 129 ? 0.809 0.908 1.098 0.229  0.155  -0.222 458 LYS EEE CA  
6121  C C   . LYS E 129 ? 0.807 0.850 1.061 0.221  0.142  -0.240 458 LYS EEE C   
6122  O O   . LYS E 129 ? 0.857 0.878 1.096 0.232  0.154  -0.274 458 LYS EEE O   
6123  C CB  . LYS E 129 ? 0.840 0.946 1.198 0.255  0.158  -0.214 458 LYS EEE CB  
6124  C CG  . LYS E 129 ? 0.860 1.026 1.251 0.267  0.180  -0.207 458 LYS EEE CG  
6125  C CD  . LYS E 129 ? 0.876 1.063 1.340 0.293  0.184  -0.196 458 LYS EEE CD  
6126  C CE  . LYS E 129 ? 0.889 1.144 1.379 0.298  0.206  -0.190 458 LYS EEE CE  
6127  N NZ  . LYS E 129 ? 0.901 1.190 1.468 0.322  0.208  -0.173 458 LYS EEE NZ  
6128  N N   . SER E 130 ? 0.777 0.799 1.019 0.203  0.118  -0.220 459 SER EEE N   
6129  C CA  . SER E 130 ? 0.777 0.750 0.989 0.192  0.103  -0.234 459 SER EEE CA  
6130  C C   . SER E 130 ? 0.726 0.698 0.913 0.167  0.083  -0.208 459 SER EEE C   
6131  O O   . SER E 130 ? 0.686 0.687 0.886 0.161  0.078  -0.181 459 SER EEE O   
6132  C CB  . SER E 130 ? 0.808 0.741 1.060 0.207  0.098  -0.239 459 SER EEE CB  
6133  O OG  . SER E 130 ? 0.784 0.716 1.065 0.203  0.079  -0.204 459 SER EEE OG  
6134  N N   . ASN E 131 ? 0.712 0.655 0.867 0.153  0.072  -0.219 460 ASN EEE N   
6135  C CA  . ASN E 131 ? 0.675 0.617 0.804 0.131  0.055  -0.199 460 ASN EEE CA  
6136  C C   . ASN E 131 ? 0.646 0.575 0.805 0.129  0.039  -0.172 460 ASN EEE C   
6137  O O   . ASN E 131 ? 0.649 0.555 0.840 0.141  0.037  -0.174 460 ASN EEE O   
6138  C CB  . ASN E 131 ? 0.697 0.614 0.788 0.119  0.047  -0.218 460 ASN EEE CB  
6139  C CG  . ASN E 131 ? 0.716 0.649 0.765 0.117  0.060  -0.239 460 ASN EEE CG  
6140  O OD1 . ASN E 131 ? 0.734 0.700 0.783 0.124  0.075  -0.237 460 ASN EEE OD1 
6141  N ND2 . ASN E 131 ? 0.738 0.653 0.754 0.107  0.052  -0.257 460 ASN EEE ND2 
6142  N N   . LEU E 132 ? 0.621 0.565 0.768 0.114  0.029  -0.148 461 LEU EEE N   
6143  C CA  . LEU E 132 ? 0.610 0.543 0.774 0.109  0.014  -0.123 461 LEU EEE CA  
6144  C C   . LEU E 132 ? 0.641 0.537 0.801 0.103  0.005  -0.130 461 LEU EEE C   
6145  O O   . LEU E 132 ? 0.687 0.573 0.817 0.094  0.004  -0.147 461 LEU EEE O   
6146  C CB  . LEU E 132 ? 0.574 0.529 0.716 0.093  0.007  -0.104 461 LEU EEE CB  
6147  C CG  . LEU E 132 ? 0.567 0.559 0.719 0.094  0.012  -0.092 461 LEU EEE CG  
6148  C CD1 . LEU E 132 ? 0.542 0.545 0.673 0.077  0.003  -0.075 461 LEU EEE CD1 
6149  C CD2 . LEU E 132 ? 0.578 0.580 0.774 0.108  0.010  -0.078 461 LEU EEE CD2 
6150  N N   . LYS E 133 ? 0.660 0.536 0.848 0.107  -0.003 -0.115 462 LYS EEE N   
6151  C CA  . LYS E 133 ? 0.675 0.520 0.862 0.096  -0.014 -0.111 462 LYS EEE CA  
6152  C C   . LYS E 133 ? 0.632 0.492 0.796 0.079  -0.022 -0.092 462 LYS EEE C   
6153  O O   . LYS E 133 ? 0.598 0.486 0.753 0.077  -0.021 -0.079 462 LYS EEE O   
6154  C CB  . LYS E 133 ? 0.724 0.547 0.952 0.106  -0.019 -0.096 462 LYS EEE CB  
6155  C CG  . LYS E 133 ? 0.792 0.587 1.047 0.122  -0.011 -0.118 462 LYS EEE CG  
6156  C CD  . LYS E 133 ? 0.859 0.630 1.157 0.132  -0.017 -0.099 462 LYS EEE CD  
6157  C CE  . LYS E 133 ? 0.868 0.666 1.179 0.134  -0.024 -0.061 462 LYS EEE CE  
6158  N NZ  . LYS E 133 ? 0.914 0.688 1.266 0.144  -0.030 -0.038 462 LYS EEE NZ  
6159  N N   . PRO E 134 ? 0.644 0.487 0.797 0.066  -0.029 -0.091 463 PRO EEE N   
6160  C CA  . PRO E 134 ? 0.615 0.471 0.747 0.052  -0.034 -0.075 463 PRO EEE CA  
6161  C C   . PRO E 134 ? 0.573 0.444 0.714 0.053  -0.038 -0.047 463 PRO EEE C   
6162  O O   . PRO E 134 ? 0.588 0.448 0.754 0.059  -0.041 -0.034 463 PRO EEE O   
6163  C CB  . PRO E 134 ? 0.622 0.457 0.757 0.042  -0.041 -0.078 463 PRO EEE CB  
6164  C CG  . PRO E 134 ? 0.646 0.462 0.785 0.046  -0.039 -0.106 463 PRO EEE CG  
6165  C CD  . PRO E 134 ? 0.666 0.477 0.826 0.063  -0.032 -0.109 463 PRO EEE CD  
6166  N N   . PHE E 135 ? 0.565 0.460 0.684 0.048  -0.038 -0.040 464 PHE EEE N   
6167  C CA  . PHE E 135 ? 0.567 0.479 0.685 0.046  -0.042 -0.018 464 PHE EEE CA  
6168  C C   . PHE E 135 ? 0.559 0.484 0.702 0.058  -0.043 -0.010 464 PHE EEE C   
6169  O O   . PHE E 135 ? 0.581 0.518 0.726 0.057  -0.050 0.010  464 PHE EEE O   
6170  C CB  . PHE E 135 ? 0.570 0.470 0.689 0.039  -0.048 0.001  464 PHE EEE CB  
6171  C CG  . PHE E 135 ? 0.561 0.458 0.660 0.027  -0.046 -0.003 464 PHE EEE CG  
6172  C CD1 . PHE E 135 ? 0.555 0.467 0.628 0.021  -0.045 -0.008 464 PHE EEE CD1 
6173  C CD2 . PHE E 135 ? 0.599 0.478 0.709 0.022  -0.047 -0.002 464 PHE EEE CD2 
6174  C CE1 . PHE E 135 ? 0.560 0.470 0.619 0.013  -0.043 -0.011 464 PHE EEE CE1 
6175  C CE2 . PHE E 135 ? 0.617 0.498 0.714 0.012  -0.046 -0.005 464 PHE EEE CE2 
6176  C CZ  . PHE E 135 ? 0.582 0.478 0.653 0.009  -0.044 -0.009 464 PHE EEE CZ  
6177  N N   . GLU E 136 ? 0.584 0.508 0.743 0.069  -0.036 -0.025 465 GLU EEE N   
6178  C CA  . GLU E 136 ? 0.588 0.531 0.775 0.083  -0.035 -0.019 465 GLU EEE CA  
6179  C C   . GLU E 136 ? 0.554 0.530 0.727 0.077  -0.034 -0.017 465 GLU EEE C   
6180  O O   . GLU E 136 ? 0.526 0.505 0.670 0.067  -0.030 -0.028 465 GLU EEE O   
6181  C CB  . GLU E 136 ? 0.620 0.550 0.830 0.099  -0.025 -0.039 465 GLU EEE CB  
6182  C CG  . GLU E 136 ? 0.630 0.574 0.880 0.117  -0.024 -0.029 465 GLU EEE CG  
6183  C CD  . GLU E 136 ? 0.667 0.599 0.942 0.135  -0.011 -0.052 465 GLU EEE CD  
6184  O OE1 . GLU E 136 ? 0.691 0.600 0.948 0.132  -0.005 -0.077 465 GLU EEE OE1 
6185  O OE2 . GLU E 136 ? 0.703 0.648 1.015 0.152  -0.008 -0.046 465 GLU EEE OE2 
6186  N N   . ARG E 137 ? 0.555 0.555 0.750 0.083  -0.039 -0.002 466 ARG EEE N   
6187  C CA  . ARG E 137 ? 0.535 0.570 0.725 0.075  -0.041 0.003  466 ARG EEE CA  
6188  C C   . ARG E 137 ? 0.484 0.545 0.713 0.090  -0.037 0.005  466 ARG EEE C   
6189  O O   . ARG E 137 ? 0.481 0.542 0.740 0.102  -0.043 0.018  466 ARG EEE O   
6190  C CB  . ARG E 137 ? 0.547 0.591 0.723 0.064  -0.056 0.022  466 ARG EEE CB  
6191  C CG  . ARG E 137 ? 0.567 0.639 0.731 0.051  -0.060 0.024  466 ARG EEE CG  
6192  C CD  . ARG E 137 ? 0.557 0.625 0.694 0.038  -0.072 0.035  466 ARG EEE CD  
6193  N NE  . ARG E 137 ? 0.545 0.634 0.668 0.024  -0.079 0.035  466 ARG EEE NE  
6194  C CZ  . ARG E 137 ? 0.586 0.705 0.724 0.021  -0.091 0.047  466 ARG EEE CZ  
6195  N NH1 . ARG E 137 ? 0.586 0.720 0.756 0.034  -0.099 0.063  466 ARG EEE NH1 
6196  N NH2 . ARG E 137 ? 0.599 0.734 0.722 0.005  -0.098 0.044  466 ARG EEE NH2 
6197  N N   . ASP E 138 ? 0.463 0.548 0.695 0.089  -0.026 -0.006 467 ASP EEE N   
6198  C CA  . ASP E 138 ? 0.471 0.589 0.744 0.103  -0.020 -0.004 467 ASP EEE CA  
6199  C C   . ASP E 138 ? 0.459 0.614 0.730 0.088  -0.024 0.004  467 ASP EEE C   
6200  O O   . ASP E 138 ? 0.464 0.620 0.709 0.075  -0.016 -0.006 467 ASP EEE O   
6201  C CB  . ASP E 138 ? 0.481 0.592 0.760 0.116  0.000  -0.027 467 ASP EEE CB  
6202  C CG  . ASP E 138 ? 0.497 0.642 0.821 0.134  0.012  -0.028 467 ASP EEE CG  
6203  O OD1 . ASP E 138 ? 0.488 0.668 0.841 0.133  0.002  -0.009 467 ASP EEE OD1 
6204  O OD2 . ASP E 138 ? 0.538 0.674 0.867 0.148  0.030  -0.049 467 ASP EEE OD2 
6205  N N   . ILE E 139 ? 0.457 0.642 0.757 0.088  -0.038 0.023  468 ILE EEE N   
6206  C CA  . ILE E 139 ? 0.433 0.656 0.739 0.073  -0.045 0.032  468 ILE EEE CA  
6207  C C   . ILE E 139 ? 0.442 0.710 0.803 0.086  -0.040 0.038  468 ILE EEE C   
6208  O O   . ILE E 139 ? 0.443 0.750 0.823 0.075  -0.049 0.049  468 ILE EEE O   
6209  C CB  . ILE E 139 ? 0.426 0.650 0.713 0.057  -0.068 0.047  468 ILE EEE CB  
6210  C CG1 . ILE E 139 ? 0.432 0.663 0.745 0.070  -0.083 0.067  468 ILE EEE CG1 
6211  C CG2 . ILE E 139 ? 0.422 0.607 0.658 0.045  -0.069 0.039  468 ILE EEE CG2 
6212  C CD1 . ILE E 139 ? 0.442 0.689 0.740 0.055  -0.107 0.083  468 ILE EEE CD1 
6213  N N   . SER E 140 ? 0.451 0.714 0.840 0.110  -0.025 0.030  469 SER EEE N   
6214  C CA  . SER E 140 ? 0.452 0.759 0.897 0.127  -0.015 0.034  469 SER EEE CA  
6215  C C   . SER E 140 ? 0.434 0.770 0.877 0.116  0.003  0.024  469 SER EEE C   
6216  O O   . SER E 140 ? 0.412 0.725 0.811 0.103  0.012  0.010  469 SER EEE O   
6217  C CB  . SER E 140 ? 0.479 0.768 0.951 0.156  -0.001 0.024  469 SER EEE CB  
6218  O OG  . SER E 140 ? 0.506 0.766 0.946 0.157  0.020  -0.002 469 SER EEE OG  
6219  N N   . THR E 141 ? 0.440 0.830 0.933 0.119  0.005  0.034  470 THR EEE N   
6220  C CA  . THR E 141 ? 0.454 0.882 0.956 0.108  0.022  0.030  470 THR EEE CA  
6221  C C   . THR E 141 ? 0.476 0.948 1.040 0.132  0.040  0.031  470 THR EEE C   
6222  O O   . THR E 141 ? 0.463 0.987 1.062 0.124  0.044  0.041  470 THR EEE O   
6223  C CB  . THR E 141 ? 0.438 0.892 0.939 0.079  0.003  0.046  470 THR EEE CB  
6224  O OG1 . THR E 141 ? 0.433 0.913 0.971 0.082  -0.022 0.065  470 THR EEE OG1 
6225  C CG2 . THR E 141 ? 0.433 0.844 0.873 0.056  -0.010 0.042  470 THR EEE CG2 
6226  N N   . GLU E 142 ? 0.549 0.999 1.126 0.161  0.051  0.020  471 GLU EEE N   
6227  C CA  . GLU E 142 ? 0.595 1.079 1.225 0.188  0.076  0.012  471 GLU EEE CA  
6228  C C   . GLU E 142 ? 0.619 1.111 1.222 0.184  0.107  -0.009 471 GLU EEE C   
6229  O O   . GLU E 142 ? 0.624 1.073 1.165 0.172  0.111  -0.024 471 GLU EEE O   
6230  C CB  . GLU E 142 ? 0.649 1.097 1.295 0.219  0.078  0.004  471 GLU EEE CB  
6231  C CG  . GLU E 142 ? 0.692 1.148 1.378 0.226  0.049  0.031  471 GLU EEE CG  
6232  C CD  . GLU E 142 ? 0.771 1.188 1.478 0.256  0.050  0.027  471 GLU EEE CD  
6233  O OE1 . GLU E 142 ? 0.806 1.163 1.466 0.252  0.048  0.013  471 GLU EEE OE1 
6234  O OE2 . GLU E 142 ? 0.796 1.241 1.570 0.283  0.052  0.037  471 GLU EEE OE2 
6235  N N   . ILE E 143 ? 0.661 1.209 1.310 0.193  0.128  -0.007 472 ILE EEE N   
6236  C CA  . ILE E 143 ? 0.726 1.292 1.357 0.193  0.162  -0.024 472 ILE EEE CA  
6237  C C   . ILE E 143 ? 0.806 1.324 1.405 0.215  0.180  -0.055 472 ILE EEE C   
6238  O O   . ILE E 143 ? 0.827 1.335 1.462 0.243  0.181  -0.061 472 ILE EEE O   
6239  C CB  . ILE E 143 ? 0.739 1.379 1.439 0.203  0.182  -0.015 472 ILE EEE CB  
6240  C CG1 . ILE E 143 ? 0.713 1.402 1.450 0.179  0.161  0.015  472 ILE EEE CG1 
6241  C CG2 . ILE E 143 ? 0.773 1.432 1.450 0.204  0.219  -0.032 472 ILE EEE CG2 
6242  C CD1 . ILE E 143 ? 0.693 1.366 1.378 0.141  0.149  0.022  472 ILE EEE CD1 
6243  N N   . TYR E 144 ? 0.892 1.380 1.425 0.202  0.191  -0.071 473 TYR EEE N   
6244  C CA  . TYR E 144 ? 1.008 1.448 1.497 0.216  0.204  -0.103 473 TYR EEE CA  
6245  C C   . TYR E 144 ? 1.091 1.565 1.599 0.238  0.241  -0.123 473 TYR EEE C   
6246  O O   . TYR E 144 ? 1.110 1.633 1.618 0.228  0.262  -0.117 473 TYR EEE O   
6247  C CB  . TYR E 144 ? 1.048 1.451 1.463 0.191  0.196  -0.108 473 TYR EEE CB  
6248  C CG  . TYR E 144 ? 1.105 1.467 1.469 0.199  0.209  -0.140 473 TYR EEE CG  
6249  C CD1 . TYR E 144 ? 1.124 1.429 1.471 0.206  0.193  -0.153 473 TYR EEE CD1 
6250  C CD2 . TYR E 144 ? 1.130 1.512 1.462 0.199  0.236  -0.156 473 TYR EEE CD2 
6251  C CE1 . TYR E 144 ? 1.141 1.409 1.442 0.210  0.201  -0.183 473 TYR EEE CE1 
6252  C CE2 . TYR E 144 ? 1.137 1.483 1.418 0.206  0.246  -0.187 473 TYR EEE CE2 
6253  C CZ  . TYR E 144 ? 1.153 1.442 1.421 0.211  0.227  -0.201 473 TYR EEE CZ  
6254  O OH  . TYR E 144 ? 1.178 1.433 1.397 0.215  0.235  -0.232 473 TYR EEE OH  
6255  N N   . GLN E 145 ? 1.177 1.625 1.701 0.268  0.251  -0.147 474 GLN EEE N   
6256  C CA  . GLN E 145 ? 1.253 1.723 1.790 0.295  0.289  -0.174 474 GLN EEE CA  
6257  C C   . GLN E 145 ? 1.350 1.786 1.809 0.287  0.302  -0.204 474 GLN EEE C   
6258  O O   . GLN E 145 ? 1.361 1.738 1.790 0.293  0.292  -0.226 474 GLN EEE O   
6259  C CB  . GLN E 145 ? 1.219 1.669 1.808 0.331  0.293  -0.190 474 GLN EEE CB  
6260  C CG  . GLN E 145 ? 1.199 1.708 1.856 0.360  0.323  -0.193 474 GLN EEE CG  
6261  C CD  . GLN E 145 ? 1.135 1.692 1.861 0.357  0.304  -0.153 474 GLN EEE CD  
6262  O OE1 . GLN E 145 ? 1.052 1.616 1.762 0.326  0.279  -0.126 474 GLN EEE OE1 
6263  N NE2 . GLN E 145 ? 1.129 1.719 1.933 0.389  0.315  -0.150 474 GLN EEE NE2 
6264  N N   . ALA E 146 ? 1.372 1.847 1.800 0.273  0.323  -0.203 475 ALA EEE N   
6265  C CA  . ALA E 146 ? 1.384 1.842 1.739 0.269  0.343  -0.231 475 ALA EEE CA  
6266  C C   . ALA E 146 ? 1.440 1.920 1.810 0.301  0.381  -0.264 475 ALA EEE C   
6267  O O   . ALA E 146 ? 1.515 1.978 1.826 0.303  0.398  -0.295 475 ALA EEE O   
6268  C CB  . ALA E 146 ? 1.352 1.843 1.670 0.239  0.346  -0.209 475 ALA EEE CB  
6269  N N   . GLY E 147 ? 1.392 1.909 1.838 0.325  0.395  -0.259 476 GLY EEE N   
6270  C CA  . GLY E 147 ? 1.397 1.941 1.864 0.357  0.436  -0.290 476 GLY EEE CA  
6271  C C   . GLY E 147 ? 1.371 1.902 1.911 0.393  0.436  -0.300 476 GLY EEE C   
6272  O O   . GLY E 147 ? 1.315 1.828 1.896 0.390  0.404  -0.275 476 GLY EEE O   
6273  N N   . SER E 148 ? 1.381 1.925 1.937 0.425  0.472  -0.334 477 SER EEE N   
6274  C CA  . SER E 148 ? 1.375 1.919 2.011 0.466  0.483  -0.345 477 SER EEE CA  
6275  C C   . SER E 148 ? 1.341 1.944 2.067 0.469  0.474  -0.301 477 SER EEE C   
6276  O O   . SER E 148 ? 1.314 1.895 2.097 0.487  0.453  -0.291 477 SER EEE O   
6277  C CB  . SER E 148 ? 1.414 1.978 2.044 0.495  0.531  -0.388 477 SER EEE CB  
6278  O OG  . SER E 148 ? 1.417 1.982 2.126 0.537  0.546  -0.401 477 SER EEE OG  
6279  N N   . THR E 149 ? 1.344 2.022 2.083 0.453  0.488  -0.276 478 THR EEE N   
6280  C CA  . THR E 149 ? 1.319 2.068 2.149 0.458  0.486  -0.238 478 THR EEE CA  
6281  C C   . THR E 149 ? 1.309 2.038 2.161 0.438  0.436  -0.201 478 THR EEE C   
6282  O O   . THR E 149 ? 1.209 1.899 2.000 0.405  0.408  -0.191 478 THR EEE O   
6283  C CB  . THR E 149 ? 1.290 2.119 2.120 0.438  0.512  -0.221 478 THR EEE CB  
6284  O OG1 . THR E 149 ? 1.334 2.177 2.131 0.456  0.558  -0.258 478 THR EEE OG1 
6285  C CG2 . THR E 149 ? 1.253 2.164 2.185 0.447  0.517  -0.189 478 THR EEE CG2 
6286  N N   . PRO E 150 ? 1.323 2.081 2.265 0.458  0.424  -0.178 479 PRO EEE N   
6287  C CA  . PRO E 150 ? 1.274 2.029 2.241 0.439  0.378  -0.139 479 PRO EEE CA  
6288  C C   . PRO E 150 ? 1.222 2.032 2.183 0.399  0.369  -0.108 479 PRO EEE C   
6289  O O   . PRO E 150 ? 1.204 2.072 2.176 0.396  0.399  -0.108 479 PRO EEE O   
6290  C CB  . PRO E 150 ? 1.270 2.056 2.339 0.476  0.376  -0.125 479 PRO EEE CB  
6291  C CG  . PRO E 150 ? 1.275 2.118 2.387 0.504  0.425  -0.145 479 PRO EEE CG  
6292  C CD  . PRO E 150 ? 1.316 2.113 2.340 0.502  0.452  -0.188 479 PRO EEE CD  
6293  N N   . CYS E 151 ? 1.184 1.970 2.123 0.369  0.327  -0.083 480 CYS EEE N   
6294  C CA  . CYS E 151 ? 1.118 1.932 2.031 0.327  0.313  -0.058 480 CYS EEE CA  
6295  C C   . CYS E 151 ? 1.049 1.928 2.039 0.318  0.293  -0.021 480 CYS EEE C   
6296  O O   . CYS E 151 ? 0.993 1.910 1.979 0.285  0.286  -0.001 480 CYS EEE O   
6297  C CB  . CYS E 151 ? 1.109 1.853 1.945 0.300  0.282  -0.058 480 CYS EEE CB  
6298  S SG  . CYS E 151 ? 1.279 1.970 2.018 0.294  0.307  -0.095 480 CYS EEE SG  
6299  N N   . ASN E 152 ? 1.033 1.922 2.090 0.346  0.279  -0.011 481 ASN EEE N   
6300  C CA  . ASN E 152 ? 0.988 1.937 2.123 0.342  0.253  0.025  481 ASN EEE CA  
6301  C C   . ASN E 152 ? 0.919 1.860 2.016 0.297  0.214  0.048  481 ASN EEE C   
6302  O O   . ASN E 152 ? 0.869 1.875 2.015 0.279  0.202  0.073  481 ASN EEE O   
6303  C CB  . ASN E 152 ? 0.975 2.017 2.185 0.350  0.282  0.034  481 ASN EEE CB  
6304  C CG  . ASN E 152 ? 0.991 2.047 2.241 0.396  0.324  0.009  481 ASN EEE CG  
6305  O OD1 . ASN E 152 ? 1.015 2.009 2.222 0.417  0.338  -0.021 481 ASN EEE OD1 
6306  N ND2 . ASN E 152 ? 0.976 2.117 2.312 0.411  0.344  0.022  481 ASN EEE ND2 
6307  N N   . GLY E 153 ? 0.924 1.791 1.942 0.281  0.196  0.038  482 GLY EEE N   
6308  C CA  . GLY E 153 ? 0.857 1.702 1.830 0.241  0.161  0.055  482 GLY EEE CA  
6309  C C   . GLY E 153 ? 0.829 1.716 1.794 0.205  0.167  0.064  482 GLY EEE C   
6310  O O   . GLY E 153 ? 0.776 1.672 1.738 0.175  0.136  0.084  482 GLY EEE O   
6311  N N   . VAL E 154 ? 0.817 1.727 1.775 0.208  0.207  0.050  483 VAL EEE N   
6312  C CA  . VAL E 154 ? 0.738 1.680 1.681 0.173  0.218  0.059  483 VAL EEE CA  
6313  C C   . VAL E 154 ? 0.730 1.625 1.592 0.168  0.242  0.037  483 VAL EEE C   
6314  O O   . VAL E 154 ? 0.755 1.627 1.600 0.197  0.266  0.012  483 VAL EEE O   
6315  C CB  . VAL E 154 ? 0.722 1.756 1.745 0.176  0.241  0.074  483 VAL EEE CB  
6316  C CG1 . VAL E 154 ? 0.758 1.812 1.781 0.200  0.291  0.053  483 VAL EEE CG1 
6317  C CG2 . VAL E 154 ? 0.695 1.761 1.719 0.132  0.231  0.095  483 VAL EEE CG2 
6318  N N   . GLU E 155 ? 0.685 1.570 1.503 0.132  0.236  0.045  484 GLU EEE N   
6319  C CA  . GLU E 155 ? 0.686 1.533 1.428 0.121  0.256  0.031  484 GLU EEE CA  
6320  C C   . GLU E 155 ? 0.712 1.614 1.471 0.127  0.301  0.028  484 GLU EEE C   
6321  O O   . GLU E 155 ? 0.698 1.671 1.527 0.125  0.310  0.046  484 GLU EEE O   
6322  C CB  . GLU E 155 ? 0.656 1.478 1.358 0.080  0.233  0.046  484 GLU EEE CB  
6323  C CG  . GLU E 155 ? 0.681 1.446 1.298 0.070  0.239  0.033  484 GLU EEE CG  
6324  C CD  . GLU E 155 ? 0.664 1.381 1.240 0.041  0.206  0.042  484 GLU EEE CD  
6325  O OE1 . GLU E 155 ? 0.639 1.371 1.248 0.022  0.181  0.059  484 GLU EEE OE1 
6326  O OE2 . GLU E 155 ? 0.646 1.308 1.154 0.038  0.205  0.030  484 GLU EEE OE2 
6327  N N   . GLY E 156 ? 0.733 1.607 1.431 0.136  0.327  0.006  485 GLY EEE N   
6328  C CA  . GLY E 156 ? 0.765 1.687 1.466 0.145  0.372  -0.000 485 GLY EEE CA  
6329  C C   . GLY E 156 ? 0.817 1.698 1.452 0.167  0.395  -0.034 485 GLY EEE C   
6330  O O   . GLY E 156 ? 0.823 1.635 1.401 0.165  0.373  -0.047 485 GLY EEE O   
6331  N N   . PHE E 157 ? 0.890 1.813 1.530 0.185  0.438  -0.047 486 PHE EEE N   
6332  C CA  . PHE E 157 ? 0.977 1.871 1.554 0.206  0.464  -0.083 486 PHE EEE CA  
6333  C C   . PHE E 157 ? 1.005 1.836 1.574 0.232  0.445  -0.110 486 PHE EEE C   
6334  O O   . PHE E 157 ? 0.982 1.828 1.619 0.256  0.441  -0.112 486 PHE EEE O   
6335  C CB  . PHE E 157 ? 1.043 2.004 1.650 0.228  0.514  -0.093 486 PHE EEE CB  
6336  C CG  . PHE E 157 ? 1.135 2.076 1.682 0.252  0.546  -0.133 486 PHE EEE CG  
6337  C CD1 . PHE E 157 ? 1.167 2.078 1.622 0.233  0.551  -0.140 486 PHE EEE CD1 
6338  C CD2 . PHE E 157 ? 1.185 2.138 1.768 0.293  0.572  -0.164 486 PHE EEE CD2 
6339  C CE1 . PHE E 157 ? 1.237 2.132 1.633 0.254  0.578  -0.178 486 PHE EEE CE1 
6340  C CE2 . PHE E 157 ? 1.241 2.173 1.766 0.314  0.601  -0.205 486 PHE EEE CE2 
6341  C CZ  . PHE E 157 ? 1.272 2.177 1.701 0.293  0.604  -0.212 486 PHE EEE CZ  
6342  N N   . ASN E 158 ? 1.058 1.822 1.549 0.226  0.431  -0.129 487 ASN EEE N   
6343  C CA  . ASN E 158 ? 1.114 1.811 1.587 0.247  0.414  -0.157 487 ASN EEE CA  
6344  C C   . ASN E 158 ? 1.095 1.771 1.616 0.246  0.375  -0.139 487 ASN EEE C   
6345  O O   . ASN E 158 ? 1.144 1.775 1.672 0.267  0.363  -0.157 487 ASN EEE O   
6346  C CB  . ASN E 158 ? 1.146 1.851 1.638 0.287  0.446  -0.193 487 ASN EEE CB  
6347  C CG  . ASN E 158 ? 1.194 1.906 1.621 0.290  0.481  -0.220 487 ASN EEE CG  
6348  O OD1 . ASN E 158 ? 1.222 1.966 1.670 0.317  0.518  -0.242 487 ASN EEE OD1 
6349  N ND2 . ASN E 158 ? 1.199 1.883 1.549 0.263  0.471  -0.217 487 ASN EEE ND2 
6350  N N   . CYS E 159 ? 1.054 1.758 1.603 0.220  0.356  -0.104 488 CYS EEE N   
6351  C CA  . CYS E 159 ? 0.990 1.686 1.586 0.216  0.320  -0.083 488 CYS EEE CA  
6352  C C   . CYS E 159 ? 0.889 1.567 1.452 0.178  0.290  -0.060 488 CYS EEE C   
6353  O O   . CYS E 159 ? 0.845 1.569 1.442 0.158  0.287  -0.034 488 CYS EEE O   
6354  C CB  . CYS E 159 ? 1.022 1.788 1.708 0.229  0.328  -0.065 488 CYS EEE CB  
6355  S SG  . CYS E 159 ? 1.094 1.869 1.836 0.280  0.351  -0.090 488 CYS EEE SG  
6356  N N   . TYR E 160 ? 0.851 1.190 1.147 0.028  0.255  -0.245 489 TYR EEE N   
6357  C CA  . TYR E 160 ? 0.844 1.164 1.119 0.015  0.250  -0.223 489 TYR EEE CA  
6358  C C   . TYR E 160 ? 0.760 1.075 1.058 0.015  0.214  -0.224 489 TYR EEE C   
6359  O O   . TYR E 160 ? 0.729 1.039 1.023 0.027  0.188  -0.232 489 TYR EEE O   
6360  C CB  . TYR E 160 ? 0.916 1.206 1.117 0.015  0.253  -0.206 489 TYR EEE CB  
6361  C CG  . TYR E 160 ? 0.979 1.271 1.148 0.018  0.285  -0.208 489 TYR EEE CG  
6362  C CD1 . TYR E 160 ? 0.998 1.310 1.193 0.010  0.321  -0.209 489 TYR EEE CD1 
6363  C CD2 . TYR E 160 ? 1.028 1.303 1.144 0.031  0.279  -0.211 489 TYR EEE CD2 
6364  C CE1 . TYR E 160 ? 1.043 1.359 1.208 0.014  0.352  -0.212 489 TYR EEE CE1 
6365  C CE2 . TYR E 160 ? 1.094 1.370 1.177 0.035  0.308  -0.214 489 TYR EEE CE2 
6366  C CZ  . TYR E 160 ? 1.104 1.401 1.210 0.027  0.345  -0.215 489 TYR EEE CZ  
6367  O OH  . TYR E 160 ? 1.194 1.493 1.266 0.032  0.376  -0.218 489 TYR EEE OH  
6368  N N   . PHE E 161 ? 0.699 1.016 1.024 0.004  0.212  -0.215 490 PHE EEE N   
6369  C CA  . PHE E 161 ? 0.636 0.941 0.965 0.003  0.179  -0.210 490 PHE EEE CA  
6370  C C   . PHE E 161 ? 0.625 0.900 0.889 0.004  0.170  -0.195 490 PHE EEE C   
6371  O O   . PHE E 161 ? 0.645 0.909 0.874 -0.002 0.189  -0.182 490 PHE EEE O   
6372  C CB  . PHE E 161 ? 0.603 0.916 0.973 -0.009 0.183  -0.206 490 PHE EEE CB  
6373  C CG  . PHE E 161 ? 0.573 0.876 0.949 -0.009 0.150  -0.204 490 PHE EEE CG  
6374  C CD1 . PHE E 161 ? 0.554 0.867 0.967 -0.000 0.126  -0.219 490 PHE EEE CD1 
6375  C CD2 . PHE E 161 ? 0.572 0.854 0.916 -0.016 0.144  -0.187 490 PHE EEE CD2 
6376  C CE1 . PHE E 161 ? 0.554 0.854 0.965 0.001  0.097  -0.217 490 PHE EEE CE1 
6377  C CE2 . PHE E 161 ? 0.557 0.831 0.905 -0.014 0.116  -0.187 490 PHE EEE CE2 
6378  C CZ  . PHE E 161 ? 0.566 0.848 0.944 -0.006 0.093  -0.201 490 PHE EEE CZ  
6379  N N   . PRO E 162 ? 0.606 0.867 0.851 0.013  0.141  -0.195 491 PRO EEE N   
6380  C CA  . PRO E 162 ? 0.605 0.841 0.793 0.016  0.133  -0.184 491 PRO EEE CA  
6381  C C   . PRO E 162 ? 0.598 0.816 0.760 0.007  0.128  -0.167 491 PRO EEE C   
6382  O O   . PRO E 162 ? 0.619 0.817 0.736 0.008  0.124  -0.157 491 PRO EEE O   
6383  C CB  . PRO E 162 ? 0.594 0.826 0.784 0.027  0.104  -0.193 491 PRO EEE CB  
6384  C CG  . PRO E 162 ? 0.591 0.837 0.829 0.026  0.090  -0.200 491 PRO EEE CG  
6385  C CD  . PRO E 162 ? 0.597 0.865 0.875 0.020  0.114  -0.207 491 PRO EEE CD  
6386  N N   . LEU E 163 ? 0.557 0.782 0.750 -0.002 0.125  -0.164 492 LEU EEE N   
6387  C CA  . LEU E 163 ? 0.569 0.777 0.742 -0.010 0.120  -0.149 492 LEU EEE CA  
6388  C C   . LEU E 163 ? 0.569 0.777 0.743 -0.021 0.145  -0.140 492 LEU EEE C   
6389  O O   . LEU E 163 ? 0.583 0.809 0.792 -0.025 0.163  -0.146 492 LEU EEE O   
6390  C CB  . LEU E 163 ? 0.547 0.759 0.750 -0.011 0.098  -0.152 492 LEU EEE CB  
6391  C CG  . LEU E 163 ? 0.538 0.749 0.742 -0.001 0.072  -0.160 492 LEU EEE CG  
6392  C CD1 . LEU E 163 ? 0.518 0.729 0.741 -0.002 0.052  -0.161 492 LEU EEE CD1 
6393  C CD2 . LEU E 163 ? 0.542 0.734 0.698 0.005  0.064  -0.153 492 LEU EEE CD2 
6394  N N   . GLN E 164 ? 0.588 0.776 0.725 -0.027 0.146  -0.125 493 GLN EEE N   
6395  C CA  . GLN E 164 ? 0.615 0.795 0.746 -0.038 0.167  -0.112 493 GLN EEE CA  
6396  C C   . GLN E 164 ? 0.593 0.760 0.722 -0.044 0.151  -0.103 493 GLN EEE C   
6397  O O   . GLN E 164 ? 0.572 0.730 0.684 -0.039 0.129  -0.103 493 GLN EEE O   
6398  C CB  . GLN E 164 ? 0.680 0.845 0.760 -0.036 0.183  -0.104 493 GLN EEE CB  
6399  C CG  . GLN E 164 ? 0.732 0.885 0.797 -0.047 0.205  -0.089 493 GLN EEE CG  
6400  C CD  . GLN E 164 ? 0.781 0.956 0.889 -0.056 0.231  -0.092 493 GLN EEE CD  
6401  O OE1 . GLN E 164 ? 0.842 1.035 0.965 -0.051 0.244  -0.103 493 GLN EEE OE1 
6402  N NE2 . GLN E 164 ? 0.819 0.991 0.949 -0.069 0.239  -0.082 493 GLN EEE NE2 
6403  N N   . SER E 165 ? 0.598 0.765 0.747 -0.056 0.163  -0.096 494 SER EEE N   
6404  C CA  . SER E 165 ? 0.590 0.746 0.744 -0.062 0.150  -0.088 494 SER EEE CA  
6405  C C   . SER E 165 ? 0.596 0.725 0.700 -0.065 0.154  -0.072 494 SER EEE C   
6406  O O   . SER E 165 ? 0.619 0.741 0.698 -0.067 0.174  -0.065 494 SER EEE O   
6407  C CB  . SER E 165 ? 0.607 0.776 0.812 -0.073 0.159  -0.090 494 SER EEE CB  
6408  O OG  . SER E 165 ? 0.663 0.821 0.875 -0.079 0.146  -0.083 494 SER EEE OG  
6409  N N   . TYR E 166 ? 0.588 0.701 0.677 -0.065 0.134  -0.068 495 TYR EEE N   
6410  C CA  . TYR E 166 ? 0.622 0.708 0.669 -0.067 0.134  -0.054 495 TYR EEE CA  
6411  C C   . TYR E 166 ? 0.662 0.741 0.723 -0.080 0.149  -0.042 495 TYR EEE C   
6412  O O   . TYR E 166 ? 0.705 0.764 0.732 -0.084 0.161  -0.028 495 TYR EEE O   
6413  C CB  . TYR E 166 ? 0.608 0.683 0.641 -0.062 0.109  -0.055 495 TYR EEE CB  
6414  C CG  . TYR E 166 ? 0.621 0.691 0.622 -0.051 0.099  -0.058 495 TYR EEE CG  
6415  C CD1 . TYR E 166 ? 0.632 0.684 0.589 -0.048 0.104  -0.051 495 TYR EEE CD1 
6416  C CD2 . TYR E 166 ? 0.606 0.689 0.620 -0.044 0.083  -0.069 495 TYR EEE CD2 
6417  C CE1 . TYR E 166 ? 0.636 0.684 0.569 -0.038 0.093  -0.056 495 TYR EEE CE1 
6418  C CE2 . TYR E 166 ? 0.612 0.690 0.600 -0.035 0.074  -0.072 495 TYR EEE CE2 
6419  C CZ  . TYR E 166 ? 0.619 0.681 0.570 -0.032 0.078  -0.066 495 TYR EEE CZ  
6420  O OH  . TYR E 166 ? 0.583 0.640 0.513 -0.023 0.067  -0.069 495 TYR EEE OH  
6421  N N   . GLY E 167 ? 0.656 0.748 0.767 -0.087 0.146  -0.046 496 GLY EEE N   
6422  C CA  . GLY E 167 ? 0.702 0.785 0.829 -0.100 0.158  -0.034 496 GLY EEE CA  
6423  C C   . GLY E 167 ? 0.727 0.781 0.819 -0.102 0.147  -0.022 496 GLY EEE C   
6424  O O   . GLY E 167 ? 0.746 0.778 0.800 -0.106 0.161  -0.007 496 GLY EEE O   
6425  N N   . PHE E 168 ? 0.711 0.762 0.812 -0.098 0.123  -0.028 497 PHE EEE N   
6426  C CA  . PHE E 168 ? 0.730 0.755 0.802 -0.098 0.108  -0.020 497 PHE EEE CA  
6427  C C   . PHE E 168 ? 0.743 0.758 0.841 -0.110 0.110  -0.011 497 PHE EEE C   
6428  O O   . PHE E 168 ? 0.715 0.744 0.860 -0.112 0.101  -0.020 497 PHE EEE O   
6429  C CB  . PHE E 168 ? 0.695 0.724 0.766 -0.088 0.082  -0.032 497 PHE EEE CB  
6430  C CG  . PHE E 168 ? 0.691 0.724 0.732 -0.076 0.078  -0.038 497 PHE EEE CG  
6431  C CD1 . PHE E 168 ? 0.700 0.714 0.695 -0.073 0.081  -0.029 497 PHE EEE CD1 
6432  C CD2 . PHE E 168 ? 0.660 0.714 0.717 -0.069 0.069  -0.051 497 PHE EEE CD2 
6433  C CE1 . PHE E 168 ? 0.685 0.702 0.657 -0.063 0.075  -0.035 497 PHE EEE CE1 
6434  C CE2 . PHE E 168 ? 0.650 0.706 0.683 -0.060 0.064  -0.055 497 PHE EEE CE2 
6435  C CZ  . PHE E 168 ? 0.671 0.709 0.663 -0.057 0.067  -0.048 497 PHE EEE CZ  
6436  N N   . GLN E 169 ? 0.772 0.760 0.840 -0.116 0.119  0.006  498 GLN EEE N   
6437  C CA  . GLN E 169 ? 0.783 0.754 0.871 -0.128 0.119  0.017  498 GLN EEE CA  
6438  C C   . GLN E 169 ? 0.785 0.729 0.844 -0.123 0.098  0.022  498 GLN EEE C   
6439  O O   . GLN E 169 ? 0.818 0.747 0.830 -0.116 0.094  0.025  498 GLN EEE O   
6440  C CB  . GLN E 169 ? 0.821 0.783 0.901 -0.139 0.148  0.034  498 GLN EEE CB  
6441  C CG  . GLN E 169 ? 0.815 0.808 0.941 -0.144 0.166  0.026  498 GLN EEE CG  
6442  C CD  . GLN E 169 ? 0.844 0.838 0.968 -0.154 0.199  0.038  498 GLN EEE CD  
6443  O OE1 . GLN E 169 ? 0.874 0.868 0.959 -0.148 0.213  0.041  498 GLN EEE OE1 
6444  N NE2 . GLN E 169 ? 0.874 0.873 1.047 -0.168 0.210  0.044  498 GLN EEE NE2 
6445  N N   . PRO E 170 ? 0.773 0.710 0.862 -0.128 0.082  0.020  499 PRO EEE N   
6446  C CA  . PRO E 170 ? 0.771 0.685 0.839 -0.123 0.060  0.021  499 PRO EEE CA  
6447  C C   . PRO E 170 ? 0.797 0.676 0.816 -0.125 0.066  0.041  499 PRO EEE C   
6448  O O   . PRO E 170 ? 0.802 0.664 0.793 -0.118 0.049  0.040  499 PRO EEE O   
6449  C CB  . PRO E 170 ? 0.776 0.689 0.892 -0.129 0.047  0.017  499 PRO EEE CB  
6450  C CG  . PRO E 170 ? 0.785 0.714 0.943 -0.141 0.067  0.020  499 PRO EEE CG  
6451  C CD  . PRO E 170 ? 0.771 0.723 0.918 -0.137 0.085  0.016  499 PRO EEE CD  
6452  N N   . THR E 171 ? 0.826 0.697 0.837 -0.136 0.091  0.057  500 THR EEE N   
6453  C CA  . THR E 171 ? 0.873 0.708 0.832 -0.139 0.100  0.079  500 THR EEE CA  
6454  C C   . THR E 171 ? 0.860 0.692 0.766 -0.130 0.108  0.079  500 THR EEE C   
6455  O O   . THR E 171 ? 0.893 0.694 0.749 -0.129 0.110  0.095  500 THR EEE O   
6456  C CB  . THR E 171 ? 0.917 0.745 0.893 -0.156 0.126  0.097  500 THR EEE CB  
6457  O OG1 . THR E 171 ? 0.919 0.779 0.918 -0.159 0.149  0.090  500 THR EEE OG1 
6458  C CG2 . THR E 171 ? 0.909 0.733 0.936 -0.166 0.116  0.098  500 THR EEE CG2 
6459  N N   . ASN E 172 ? 0.804 0.666 0.717 -0.121 0.110  0.063  501 ASN EEE N   
6460  C CA  . ASN E 172 ? 0.797 0.657 0.663 -0.110 0.114  0.061  501 ASN EEE CA  
6461  C C   . ASN E 172 ? 0.800 0.630 0.623 -0.101 0.092  0.064  501 ASN EEE C   
6462  O O   . ASN E 172 ? 0.764 0.590 0.605 -0.099 0.069  0.058  501 ASN EEE O   
6463  C CB  . ASN E 172 ? 0.756 0.650 0.643 -0.101 0.109  0.041  501 ASN EEE CB  
6464  C CG  . ASN E 172 ? 0.738 0.661 0.661 -0.107 0.131  0.036  501 ASN EEE CG  
6465  O OD1 . ASN E 172 ? 0.756 0.676 0.688 -0.118 0.152  0.048  501 ASN EEE OD1 
6466  N ND2 . ASN E 172 ? 0.699 0.650 0.642 -0.100 0.126  0.020  501 ASN EEE ND2 
6467  N N   . GLY E 173 ? 0.836 0.647 0.605 -0.095 0.097  0.071  502 GLY EEE N   
6468  C CA  . GLY E 173 ? 0.856 0.643 0.587 -0.083 0.073  0.068  502 GLY EEE CA  
6469  C C   . GLY E 173 ? 0.813 0.625 0.568 -0.073 0.055  0.048  502 GLY EEE C   
6470  O O   . GLY E 173 ? 0.772 0.617 0.557 -0.073 0.064  0.037  502 GLY EEE O   
6471  N N   . VAL E 174 ? 0.831 0.628 0.573 -0.065 0.030  0.043  503 VAL EEE N   
6472  C CA  . VAL E 174 ? 0.812 0.631 0.580 -0.056 0.012  0.025  503 VAL EEE CA  
6473  C C   . VAL E 174 ? 0.791 0.634 0.557 -0.050 0.021  0.015  503 VAL EEE C   
6474  O O   . VAL E 174 ? 0.761 0.633 0.562 -0.049 0.018  0.003  503 VAL EEE O   
6475  C CB  . VAL E 174 ? 0.840 0.637 0.590 -0.047 -0.013 0.022  503 VAL EEE CB  
6476  C CG1 . VAL E 174 ? 0.832 0.653 0.611 -0.040 -0.028 0.005  503 VAL EEE CG1 
6477  C CG2 . VAL E 174 ? 0.876 0.645 0.625 -0.052 -0.024 0.032  503 VAL EEE CG2 
6478  N N   . GLY E 175 ? 0.808 0.639 0.534 -0.045 0.029  0.020  504 GLY EEE N   
6479  C CA  . GLY E 175 ? 0.803 0.652 0.524 -0.038 0.035  0.010  504 GLY EEE CA  
6480  C C   . GLY E 175 ? 0.789 0.668 0.543 -0.045 0.055  0.007  504 GLY EEE C   
6481  O O   . GLY E 175 ? 0.777 0.677 0.541 -0.039 0.055  -0.004 504 GLY EEE O   
6482  N N   . TYR E 176 ? 0.815 0.696 0.586 -0.056 0.069  0.015  505 TYR EEE N   
6483  C CA  . TYR E 176 ? 0.805 0.715 0.612 -0.062 0.088  0.011  505 TYR EEE CA  
6484  C C   . TYR E 176 ? 0.743 0.670 0.599 -0.067 0.078  0.004  505 TYR EEE C   
6485  O O   . TYR E 176 ? 0.737 0.687 0.629 -0.073 0.090  0.000  505 TYR EEE O   
6486  C CB  . TYR E 176 ? 0.869 0.770 0.665 -0.071 0.113  0.025  505 TYR EEE CB  
6487  C CG  . TYR E 176 ? 0.952 0.840 0.698 -0.065 0.126  0.030  505 TYR EEE CG  
6488  C CD1 . TYR E 176 ? 0.977 0.886 0.726 -0.061 0.140  0.020  505 TYR EEE CD1 
6489  C CD2 . TYR E 176 ? 1.036 0.887 0.731 -0.063 0.122  0.042  505 TYR EEE CD2 
6490  C CE1 . TYR E 176 ? 1.028 0.925 0.730 -0.054 0.151  0.023  505 TYR EEE CE1 
6491  C CE2 . TYR E 176 ? 1.093 0.930 0.739 -0.056 0.133  0.046  505 TYR EEE CE2 
6492  C CZ  . TYR E 176 ? 1.094 0.954 0.743 -0.051 0.147  0.035  505 TYR EEE CZ  
6493  O OH  . TYR E 176 ? 1.179 1.025 0.777 -0.043 0.157  0.037  505 TYR EEE OH  
6494  N N   . GLN E 177 ? 0.725 0.644 0.585 -0.064 0.057  0.002  506 GLN EEE N   
6495  C CA  . GLN E 177 ? 0.682 0.617 0.585 -0.067 0.046  -0.007 506 GLN EEE CA  
6496  C C   . GLN E 177 ? 0.635 0.595 0.552 -0.059 0.039  -0.022 506 GLN EEE C   
6497  O O   . GLN E 177 ? 0.624 0.583 0.519 -0.051 0.035  -0.025 506 GLN EEE O   
6498  C CB  . GLN E 177 ? 0.678 0.594 0.579 -0.066 0.028  -0.005 506 GLN EEE CB  
6499  C CG  . GLN E 177 ? 0.699 0.593 0.599 -0.076 0.034  0.009  506 GLN EEE CG  
6500  C CD  . GLN E 177 ? 0.691 0.562 0.585 -0.075 0.014  0.011  506 GLN EEE CD  
6501  O OE1 . GLN E 177 ? 0.680 0.558 0.587 -0.068 -0.004 -0.001 506 GLN EEE OE1 
6502  N NE2 . GLN E 177 ? 0.715 0.557 0.590 -0.081 0.017  0.026  506 GLN EEE NE2 
6503  N N   . PRO E 178 ? 0.627 0.607 0.581 -0.061 0.035  -0.031 507 PRO EEE N   
6504  C CA  . PRO E 178 ? 0.597 0.597 0.562 -0.053 0.028  -0.043 507 PRO EEE CA  
6505  C C   . PRO E 178 ? 0.587 0.581 0.540 -0.046 0.010  -0.048 507 PRO EEE C   
6506  O O   . PRO E 178 ? 0.604 0.587 0.560 -0.048 0.001  -0.046 507 PRO EEE O   
6507  C CB  . PRO E 178 ? 0.576 0.595 0.582 -0.057 0.027  -0.051 507 PRO EEE CB  
6508  C CG  . PRO E 178 ? 0.601 0.606 0.619 -0.065 0.024  -0.045 507 PRO EEE CG  
6509  C CD  . PRO E 178 ? 0.642 0.624 0.629 -0.069 0.036  -0.030 507 PRO EEE CD  
6510  N N   . TYR E 179 ? 0.558 0.560 0.501 -0.039 0.007  -0.053 508 TYR EEE N   
6511  C CA  . TYR E 179 ? 0.524 0.527 0.463 -0.033 -0.007 -0.059 508 TYR EEE CA  
6512  C C   . TYR E 179 ? 0.510 0.534 0.464 -0.029 -0.009 -0.067 508 TYR EEE C   
6513  O O   . TYR E 179 ? 0.485 0.517 0.438 -0.028 -0.002 -0.068 508 TYR EEE O   
6514  C CB  . TYR E 179 ? 0.535 0.522 0.446 -0.028 -0.011 -0.055 508 TYR EEE CB  
6515  C CG  . TYR E 179 ? 0.549 0.512 0.444 -0.029 -0.016 -0.049 508 TYR EEE CG  
6516  C CD1 . TYR E 179 ? 0.570 0.518 0.453 -0.035 -0.007 -0.039 508 TYR EEE CD1 
6517  C CD2 . TYR E 179 ? 0.545 0.499 0.436 -0.025 -0.030 -0.052 508 TYR EEE CD2 
6518  C CE1 . TYR E 179 ? 0.603 0.526 0.468 -0.036 -0.013 -0.031 508 TYR EEE CE1 
6519  C CE2 . TYR E 179 ? 0.570 0.500 0.447 -0.025 -0.038 -0.046 508 TYR EEE CE2 
6520  C CZ  . TYR E 179 ? 0.603 0.515 0.465 -0.031 -0.031 -0.035 508 TYR EEE CZ  
6521  O OH  . TYR E 179 ? 0.625 0.510 0.471 -0.031 -0.040 -0.029 508 TYR EEE OH  
6522  N N   . ARG E 180 ? 0.533 0.564 0.498 -0.027 -0.019 -0.074 509 ARG EEE N   
6523  C CA  . ARG E 180 ? 0.543 0.590 0.515 -0.023 -0.022 -0.081 509 ARG EEE CA  
6524  C C   . ARG E 180 ? 0.536 0.580 0.493 -0.018 -0.025 -0.080 509 ARG EEE C   
6525  O O   . ARG E 180 ? 0.563 0.596 0.512 -0.017 -0.030 -0.079 509 ARG EEE O   
6526  C CB  . ARG E 180 ? 0.538 0.593 0.526 -0.022 -0.030 -0.089 509 ARG EEE CB  
6527  C CG  . ARG E 180 ? 0.532 0.592 0.541 -0.026 -0.028 -0.091 509 ARG EEE CG  
6528  C CD  . ARG E 180 ? 0.510 0.576 0.533 -0.023 -0.037 -0.100 509 ARG EEE CD  
6529  N NE  . ARG E 180 ? 0.518 0.588 0.564 -0.027 -0.037 -0.103 509 ARG EEE NE  
6530  C CZ  . ARG E 180 ? 0.509 0.586 0.573 -0.025 -0.046 -0.113 509 ARG EEE CZ  
6531  N NH1 . ARG E 180 ? 0.502 0.584 0.559 -0.018 -0.055 -0.121 509 ARG EEE NH1 
6532  N NH2 . ARG E 180 ? 0.501 0.583 0.591 -0.029 -0.046 -0.115 509 ARG EEE NH2 
6533  N N   . VAL E 181 ? 0.529 0.582 0.484 -0.015 -0.024 -0.081 510 VAL EEE N   
6534  C CA  . VAL E 181 ? 0.532 0.584 0.478 -0.011 -0.027 -0.080 510 VAL EEE CA  
6535  C C   . VAL E 181 ? 0.535 0.600 0.487 -0.009 -0.029 -0.084 510 VAL EEE C   
6536  O O   . VAL E 181 ? 0.498 0.572 0.456 -0.009 -0.028 -0.086 510 VAL EEE O   
6537  C CB  . VAL E 181 ? 0.523 0.570 0.459 -0.010 -0.023 -0.077 510 VAL EEE CB  
6538  C CG1 . VAL E 181 ? 0.511 0.554 0.440 -0.006 -0.028 -0.076 510 VAL EEE CG1 
6539  C CG2 . VAL E 181 ? 0.545 0.579 0.470 -0.013 -0.018 -0.073 510 VAL EEE CG2 
6540  N N   . VAL E 182 ? 0.509 0.574 0.459 -0.007 -0.032 -0.084 511 VAL EEE N   
6541  C CA  . VAL E 182 ? 0.498 0.573 0.449 -0.005 -0.032 -0.084 511 VAL EEE CA  
6542  C C   . VAL E 182 ? 0.487 0.557 0.436 -0.005 -0.033 -0.080 511 VAL EEE C   
6543  O O   . VAL E 182 ? 0.442 0.505 0.392 -0.004 -0.035 -0.081 511 VAL EEE O   
6544  C CB  . VAL E 182 ? 0.506 0.587 0.460 -0.004 -0.033 -0.089 511 VAL EEE CB  
6545  C CG1 . VAL E 182 ? 0.498 0.587 0.449 -0.003 -0.031 -0.087 511 VAL EEE CG1 
6546  C CG2 . VAL E 182 ? 0.505 0.591 0.464 -0.004 -0.035 -0.094 511 VAL EEE CG2 
6547  N N   . VAL E 183 ? 0.481 0.553 0.427 -0.004 -0.033 -0.077 512 VAL EEE N   
6548  C CA  . VAL E 183 ? 0.460 0.529 0.408 -0.003 -0.034 -0.073 512 VAL EEE CA  
6549  C C   . VAL E 183 ? 0.450 0.527 0.400 -0.004 -0.032 -0.070 512 VAL EEE C   
6550  O O   . VAL E 183 ? 0.458 0.539 0.403 -0.003 -0.031 -0.069 512 VAL EEE O   
6551  C CB  . VAL E 183 ? 0.453 0.516 0.398 -0.001 -0.036 -0.072 512 VAL EEE CB  
6552  C CG1 . VAL E 183 ? 0.466 0.524 0.415 -0.001 -0.040 -0.069 512 VAL EEE CG1 
6553  C CG2 . VAL E 183 ? 0.462 0.518 0.401 -0.001 -0.036 -0.074 512 VAL EEE CG2 
6554  N N   . LEU E 184 ? 0.469 0.547 0.426 -0.005 -0.030 -0.069 513 LEU EEE N   
6555  C CA  . LEU E 184 ? 0.483 0.568 0.441 -0.007 -0.025 -0.065 513 LEU EEE CA  
6556  C C   . LEU E 184 ? 0.482 0.560 0.447 -0.008 -0.027 -0.058 513 LEU EEE C   
6557  O O   . LEU E 184 ? 0.516 0.591 0.494 -0.009 -0.030 -0.060 513 LEU EEE O   
6558  C CB  . LEU E 184 ? 0.480 0.572 0.446 -0.008 -0.019 -0.069 513 LEU EEE CB  
6559  C CG  . LEU E 184 ? 0.482 0.579 0.443 -0.005 -0.019 -0.076 513 LEU EEE CG  
6560  C CD1 . LEU E 184 ? 0.490 0.595 0.462 -0.005 -0.015 -0.082 513 LEU EEE CD1 
6561  C CD2 . LEU E 184 ? 0.492 0.593 0.437 -0.004 -0.017 -0.076 513 LEU EEE CD2 
6562  N N   . SER E 185 ? 0.493 0.569 0.451 -0.008 -0.027 -0.052 514 SER EEE N   
6563  C CA  . SER E 185 ? 0.513 0.584 0.480 -0.010 -0.030 -0.045 514 SER EEE CA  
6564  C C   . SER E 185 ? 0.511 0.585 0.480 -0.015 -0.021 -0.037 514 SER EEE C   
6565  O O   . SER E 185 ? 0.492 0.571 0.446 -0.014 -0.016 -0.034 514 SER EEE O   
6566  C CB  . SER E 185 ? 0.540 0.604 0.497 -0.008 -0.036 -0.042 514 SER EEE CB  
6567  O OG  . SER E 185 ? 0.580 0.639 0.541 -0.005 -0.042 -0.048 514 SER EEE OG  
6568  N N   . PHE E 186 ? 0.528 0.601 0.517 -0.018 -0.020 -0.034 515 PHE EEE N   
6569  C CA  . PHE E 186 ? 0.550 0.628 0.547 -0.024 -0.009 -0.025 515 PHE EEE CA  
6570  C C   . PHE E 186 ? 0.562 0.629 0.566 -0.027 -0.014 -0.014 515 PHE EEE C   
6571  O O   . PHE E 186 ? 0.584 0.645 0.606 -0.026 -0.024 -0.017 515 PHE EEE O   
6572  C CB  . PHE E 186 ? 0.545 0.632 0.567 -0.026 -0.004 -0.030 515 PHE EEE CB  
6573  C CG  . PHE E 186 ? 0.541 0.635 0.559 -0.023 -0.002 -0.041 515 PHE EEE CG  
6574  C CD1 . PHE E 186 ? 0.553 0.652 0.548 -0.020 0.002  -0.044 515 PHE EEE CD1 
6575  C CD2 . PHE E 186 ? 0.544 0.640 0.584 -0.022 -0.006 -0.050 515 PHE EEE CD2 
6576  C CE1 . PHE E 186 ? 0.578 0.685 0.574 -0.017 0.002  -0.054 515 PHE EEE CE1 
6577  C CE2 . PHE E 186 ? 0.547 0.649 0.585 -0.019 -0.006 -0.060 515 PHE EEE CE2 
6578  C CZ  . PHE E 186 ? 0.552 0.659 0.568 -0.017 -0.002 -0.062 515 PHE EEE CZ  
6579  N N   . GLU E 187 ? 0.602 0.666 0.591 -0.029 -0.008 -0.003 516 GLU EEE N   
6580  C CA  . GLU E 187 ? 0.617 0.669 0.613 -0.033 -0.012 0.010  516 GLU EEE CA  
6581  C C   . GLU E 187 ? 0.616 0.673 0.628 -0.042 0.003  0.020  516 GLU EEE C   
6582  O O   . GLU E 187 ? 0.609 0.676 0.609 -0.044 0.018  0.023  516 GLU EEE O   
6583  C CB  . GLU E 187 ? 0.665 0.709 0.633 -0.030 -0.016 0.017  516 GLU EEE CB  
6584  C CG  . GLU E 187 ? 0.699 0.734 0.665 -0.024 -0.032 0.011  516 GLU EEE CG  
6585  C CD  . GLU E 187 ? 0.774 0.799 0.717 -0.021 -0.039 0.017  516 GLU EEE CD  
6586  O OE1 . GLU E 187 ? 0.774 0.795 0.698 -0.024 -0.032 0.030  516 GLU EEE OE1 
6587  O OE2 . GLU E 187 ? 0.873 0.895 0.815 -0.015 -0.051 0.009  516 GLU EEE OE2 
6588  N N   . LEU E 188 ? 0.600 0.650 0.640 -0.047 -0.001 0.026  517 LEU EEE N   
6589  C CA  . LEU E 188 ? 0.600 0.653 0.661 -0.056 0.013  0.039  517 LEU EEE CA  
6590  C C   . LEU E 188 ? 0.605 0.640 0.670 -0.061 0.006  0.054  517 LEU EEE C   
6591  O O   . LEU E 188 ? 0.622 0.651 0.722 -0.065 -0.001 0.055  517 LEU EEE O   
6592  C CB  . LEU E 188 ? 0.605 0.665 0.707 -0.058 0.012  0.029  517 LEU EEE CB  
6593  C CG  . LEU E 188 ? 0.596 0.675 0.702 -0.057 0.022  0.017  517 LEU EEE CG  
6594  C CD1 . LEU E 188 ? 0.571 0.653 0.714 -0.055 0.012  0.003  517 LEU EEE CD1 
6595  C CD2 . LEU E 188 ? 0.600 0.691 0.702 -0.063 0.045  0.026  517 LEU EEE CD2 
6596  N N   . LEU E 189 ? 0.610 0.635 0.642 -0.060 0.007  0.066  518 LEU EEE N   
6597  C CA  . LEU E 189 ? 0.605 0.609 0.636 -0.064 -0.001 0.081  518 LEU EEE CA  
6598  C C   . LEU E 189 ? 0.635 0.638 0.669 -0.075 0.018  0.102  518 LEU EEE C   
6599  O O   . LEU E 189 ? 0.631 0.649 0.667 -0.079 0.038  0.101  518 LEU EEE O   
6600  C CB  . LEU E 189 ? 0.602 0.596 0.595 -0.056 -0.012 0.082  518 LEU EEE CB  
6601  C CG  . LEU E 189 ? 0.586 0.584 0.574 -0.045 -0.027 0.063  518 LEU EEE CG  
6602  C CD1 . LEU E 189 ? 0.601 0.589 0.558 -0.039 -0.038 0.065  518 LEU EEE CD1 
6603  C CD2 . LEU E 189 ? 0.559 0.554 0.580 -0.043 -0.041 0.053  518 LEU EEE CD2 
6604  N N   . HIS E 190 ? 0.658 0.641 0.691 -0.080 0.013  0.119  519 HIS EEE N   
6605  C CA  . HIS E 190 ? 0.703 0.678 0.733 -0.092 0.031  0.142  519 HIS EEE CA  
6606  C C   . HIS E 190 ? 0.757 0.726 0.730 -0.089 0.040  0.152  519 HIS EEE C   
6607  O O   . HIS E 190 ? 0.802 0.749 0.753 -0.089 0.032  0.168  519 HIS EEE O   
6608  C CB  . HIS E 190 ? 0.706 0.660 0.762 -0.097 0.017  0.154  519 HIS EEE CB  
6609  C CG  . HIS E 190 ? 0.675 0.636 0.784 -0.098 0.006  0.140  519 HIS EEE CG  
6610  N ND1 . HIS E 190 ? 0.659 0.637 0.804 -0.105 0.022  0.137  519 HIS EEE ND1 
6611  C CD2 . HIS E 190 ? 0.646 0.600 0.775 -0.090 -0.018 0.127  519 HIS EEE CD2 
6612  C CE1 . HIS E 190 ? 0.633 0.612 0.819 -0.102 0.005  0.122  519 HIS EEE CE1 
6613  N NE2 . HIS E 190 ? 0.625 0.590 0.800 -0.093 -0.019 0.116  519 HIS EEE NE2 
6614  N N   . ALA E 191 ? 0.771 0.758 0.724 -0.085 0.054  0.143  520 ALA EEE N   
6615  C CA  . ALA E 191 ? 0.812 0.796 0.709 -0.078 0.059  0.146  520 ALA EEE CA  
6616  C C   . ALA E 191 ? 0.818 0.826 0.710 -0.080 0.084  0.139  520 ALA EEE C   
6617  O O   . ALA E 191 ? 0.829 0.856 0.759 -0.082 0.091  0.128  520 ALA EEE O   
6618  C CB  . ALA E 191 ? 0.795 0.776 0.674 -0.066 0.037  0.130  520 ALA EEE CB  
6619  N N   . PRO E 192 ? 0.845 0.851 0.689 -0.077 0.097  0.147  521 PRO EEE N   
6620  C CA  . PRO E 192 ? 0.832 0.860 0.669 -0.076 0.119  0.137  521 PRO EEE CA  
6621  C C   . PRO E 192 ? 0.769 0.815 0.620 -0.067 0.108  0.111  521 PRO EEE C   
6622  O O   . PRO E 192 ? 0.758 0.797 0.599 -0.058 0.086  0.102  521 PRO EEE O   
6623  C CB  . PRO E 192 ? 0.879 0.896 0.654 -0.072 0.127  0.148  521 PRO EEE CB  
6624  C CG  . PRO E 192 ? 0.919 0.907 0.679 -0.077 0.120  0.172  521 PRO EEE CG  
6625  C CD  . PRO E 192 ? 0.891 0.872 0.686 -0.075 0.093  0.165  521 PRO EEE CD  
6626  N N   . ALA E 193 ? 0.744 0.813 0.622 -0.069 0.123  0.099  522 ALA EEE N   
6627  C CA  . ALA E 193 ? 0.738 0.824 0.625 -0.061 0.116  0.076  522 ALA EEE CA  
6628  C C   . ALA E 193 ? 0.785 0.870 0.623 -0.050 0.115  0.069  522 ALA EEE C   
6629  O O   . ALA E 193 ? 0.835 0.918 0.640 -0.051 0.131  0.079  522 ALA EEE O   
6630  C CB  . ALA E 193 ? 0.703 0.812 0.628 -0.065 0.134  0.067  522 ALA EEE CB  
6631  N N   . THR E 194 ? 0.793 0.879 0.626 -0.041 0.096  0.053  523 THR EEE N   
6632  C CA  . THR E 194 ? 0.824 0.910 0.617 -0.031 0.092  0.044  523 THR EEE CA  
6633  C C   . THR E 194 ? 0.809 0.914 0.620 -0.026 0.092  0.022  523 THR EEE C   
6634  O O   . THR E 194 ? 0.895 1.005 0.678 -0.018 0.094  0.013  523 THR EEE O   
6635  C CB  . THR E 194 ? 0.823 0.890 0.591 -0.024 0.069  0.046  523 THR EEE CB  
6636  O OG1 . THR E 194 ? 0.774 0.844 0.572 -0.022 0.052  0.033  523 THR EEE OG1 
6637  C CG2 . THR E 194 ? 0.843 0.889 0.601 -0.029 0.066  0.066  523 THR EEE CG2 
6638  N N   . VAL E 195 ? 0.750 0.864 0.604 -0.029 0.089  0.014  524 VAL EEE N   
6639  C CA  . VAL E 195 ? 0.724 0.854 0.597 -0.025 0.087  -0.005 524 VAL EEE CA  
6640  C C   . VAL E 195 ? 0.689 0.834 0.601 -0.031 0.102  -0.008 524 VAL EEE C   
6641  O O   . VAL E 195 ? 0.689 0.830 0.631 -0.037 0.097  -0.003 524 VAL EEE O   
6642  C CB  . VAL E 195 ? 0.706 0.831 0.593 -0.021 0.066  -0.015 524 VAL EEE CB  
6643  C CG1 . VAL E 195 ? 0.684 0.821 0.591 -0.018 0.063  -0.033 524 VAL EEE CG1 
6644  C CG2 . VAL E 195 ? 0.739 0.852 0.594 -0.015 0.052  -0.015 524 VAL EEE CG2 
6645  N N   . CYS E 196 ? 0.696 0.858 0.609 -0.029 0.116  -0.018 525 CYS EEE N   
6646  C CA  . CYS E 196 ? 0.687 0.867 0.643 -0.033 0.129  -0.025 525 CYS EEE CA  
6647  C C   . CYS E 196 ? 0.652 0.844 0.618 -0.026 0.124  -0.046 525 CYS EEE C   
6648  O O   . CYS E 196 ? 0.647 0.838 0.584 -0.018 0.118  -0.054 525 CYS EEE O   
6649  C CB  . CYS E 196 ? 0.730 0.919 0.682 -0.039 0.156  -0.015 525 CYS EEE CB  
6650  S SG  . CYS E 196 ? 0.787 0.961 0.739 -0.051 0.163  0.012  525 CYS EEE SG  
6651  N N   . GLY E 197 ? 0.654 0.856 0.663 -0.028 0.123  -0.056 526 GLY EEE N   
6652  C CA  . GLY E 197 ? 0.673 0.888 0.698 -0.021 0.120  -0.077 526 GLY EEE CA  
6653  C C   . GLY E 197 ? 0.726 0.961 0.748 -0.019 0.143  -0.082 526 GLY EEE C   
6654  O O   . GLY E 197 ? 0.752 0.990 0.762 -0.024 0.163  -0.070 526 GLY EEE O   
6655  N N   . PRO E 198 ? 0.792 1.039 0.823 -0.012 0.142  -0.102 527 PRO EEE N   
6656  C CA  . PRO E 198 ? 0.852 1.120 0.882 -0.008 0.164  -0.111 527 PRO EEE CA  
6657  C C   . PRO E 198 ? 0.948 1.232 1.013 -0.017 0.188  -0.106 527 PRO EEE C   
6658  O O   . PRO E 198 ? 0.974 1.274 1.027 -0.016 0.212  -0.107 527 PRO EEE O   
6659  C CB  . PRO E 198 ? 0.821 1.097 0.874 0.000  0.151  -0.135 527 PRO EEE CB  
6660  C CG  . PRO E 198 ? 0.782 1.036 0.818 0.004  0.124  -0.135 527 PRO EEE CG  
6661  C CD  . PRO E 198 ? 0.766 1.005 0.803 -0.005 0.118  -0.116 527 PRO EEE CD  
6671  N N   . GLN F 1   ? 0.682 1.021 1.093 0.157  -0.237 -0.273 1   GLN FFF N   
6672  C CA  . GLN F 1   ? 0.626 0.933 1.045 0.118  -0.203 -0.252 1   GLN FFF CA  
6673  C C   . GLN F 1   ? 0.588 0.842 0.901 0.118  -0.192 -0.217 1   GLN FFF C   
6674  O O   . GLN F 1   ? 0.600 0.827 0.856 0.127  -0.180 -0.192 1   GLN FFF O   
6675  C CB  . GLN F 1   ? 0.652 0.956 1.129 0.096  -0.165 -0.238 1   GLN FFF CB  
6676  C CG  . GLN F 1   ? 0.722 0.986 1.193 0.065  -0.126 -0.212 1   GLN FFF CG  
6677  C CD  . GLN F 1   ? 0.777 1.046 1.298 0.044  -0.124 -0.228 1   GLN FFF CD  
6678  O OE1 . GLN F 1   ? 0.816 1.123 1.400 0.046  -0.150 -0.267 1   GLN FFF OE1 
6679  N NE2 . GLN F 1   ? 0.795 1.022 1.286 0.026  -0.093 -0.201 1   GLN FFF NE2 
6680  N N   . VAL F 2   ? 0.553 0.794 0.851 0.106  -0.195 -0.217 2   VAL FFF N   
6681  C CA  . VAL F 2   ? 0.528 0.724 0.750 0.098  -0.180 -0.186 2   VAL FFF CA  
6682  C C   . VAL F 2   ? 0.471 0.651 0.720 0.066  -0.154 -0.173 2   VAL FFF C   
6683  O O   . VAL F 2   ? 0.463 0.658 0.769 0.053  -0.153 -0.191 2   VAL FFF O   
6684  C CB  . VAL F 2   ? 0.533 0.725 0.713 0.117  -0.202 -0.196 2   VAL FFF CB  
6685  C CG1 . VAL F 2   ? 0.528 0.681 0.650 0.107  -0.183 -0.165 2   VAL FFF CG1 
6686  C CG2 . VAL F 2   ? 0.572 0.773 0.711 0.159  -0.227 -0.208 2   VAL FFF CG2 
6687  N N   . GLN F 3   ? 0.440 0.586 0.645 0.056  -0.133 -0.144 3   GLN FFF N   
6688  C CA  . GLN F 3   ? 0.418 0.543 0.626 0.034  -0.112 -0.129 3   GLN FFF CA  
6689  C C   . GLN F 3   ? 0.412 0.521 0.576 0.033  -0.118 -0.119 3   GLN FFF C   
6690  O O   . GLN F 3   ? 0.422 0.523 0.542 0.045  -0.126 -0.112 3   GLN FFF O   
6691  C CB  . GLN F 3   ? 0.412 0.514 0.605 0.030  -0.089 -0.109 3   GLN FFF CB  
6692  C CG  . GLN F 3   ? 0.417 0.534 0.668 0.029  -0.073 -0.118 3   GLN FFF CG  
6693  C CD  . GLN F 3   ? 0.436 0.520 0.662 0.028  -0.044 -0.096 3   GLN FFF CD  
6694  O OE1 . GLN F 3   ? 0.427 0.485 0.634 0.022  -0.028 -0.082 3   GLN FFF OE1 
6695  N NE2 . GLN F 3   ? 0.436 0.520 0.659 0.039  -0.038 -0.093 3   GLN FFF NE2 
6696  N N   . LEU F 4   ? 0.399 0.503 0.577 0.020  -0.110 -0.117 4   LEU FFF N   
6697  C CA  . LEU F 4   ? 0.413 0.507 0.562 0.019  -0.113 -0.109 4   LEU FFF CA  
6698  C C   . LEU F 4   ? 0.419 0.494 0.561 0.008  -0.097 -0.092 4   LEU FFF C   
6699  O O   . LEU F 4   ? 0.430 0.500 0.601 0.002  -0.081 -0.093 4   LEU FFF O   
6700  C CB  . LEU F 4   ? 0.402 0.510 0.575 0.023  -0.125 -0.129 4   LEU FFF CB  
6701  C CG  . LEU F 4   ? 0.415 0.544 0.590 0.042  -0.149 -0.153 4   LEU FFF CG  
6702  C CD1 . LEU F 4   ? 0.414 0.556 0.619 0.045  -0.163 -0.180 4   LEU FFF CD1 
6703  C CD2 . LEU F 4   ? 0.433 0.548 0.546 0.061  -0.154 -0.140 4   LEU FFF CD2 
6704  N N   . VAL F 5   ? 0.427 0.490 0.535 0.007  -0.098 -0.078 5   VAL FFF N   
6705  C CA  . VAL F 5   ? 0.444 0.492 0.538 0.004  -0.090 -0.066 5   VAL FFF CA  
6706  C C   . VAL F 5   ? 0.460 0.513 0.547 0.003  -0.097 -0.062 5   VAL FFF C   
6707  O O   . VAL F 5   ? 0.465 0.522 0.542 0.003  -0.104 -0.060 5   VAL FFF O   
6708  C CB  . VAL F 5   ? 0.442 0.476 0.509 0.006  -0.090 -0.058 5   VAL FFF CB  
6709  C CG1 . VAL F 5   ? 0.452 0.473 0.497 0.010  -0.090 -0.050 5   VAL FFF CG1 
6710  C CG2 . VAL F 5   ? 0.449 0.475 0.523 0.009  -0.077 -0.059 5   VAL FFF CG2 
6711  N N   . GLU F 6   ? 0.469 0.521 0.566 0.004  -0.091 -0.060 6   GLU FFF N   
6712  C CA  . GLU F 6   ? 0.465 0.522 0.559 0.006  -0.094 -0.055 6   GLU FFF CA  
6713  C C   . GLU F 6   ? 0.471 0.525 0.548 0.010  -0.099 -0.046 6   GLU FFF C   
6714  O O   . GLU F 6   ? 0.492 0.531 0.552 0.016  -0.095 -0.042 6   GLU FFF O   
6715  C CB  . GLU F 6   ? 0.485 0.535 0.592 0.009  -0.083 -0.056 6   GLU FFF CB  
6716  C CG  . GLU F 6   ? 0.478 0.533 0.611 0.006  -0.083 -0.073 6   GLU FFF CG  
6717  C CD  . GLU F 6   ? 0.484 0.532 0.644 0.000  -0.070 -0.081 6   GLU FFF CD  
6718  O OE1 . GLU F 6   ? 0.482 0.519 0.632 0.001  -0.061 -0.070 6   GLU FFF OE1 
6719  O OE2 . GLU F 6   ? 0.498 0.551 0.694 -0.003 -0.070 -0.100 6   GLU FFF OE2 
6720  N N   . SER F 7   ? 0.460 0.528 0.544 0.010  -0.108 -0.044 7   SER FFF N   
6721  C CA  . SER F 7   ? 0.464 0.539 0.544 0.017  -0.120 -0.043 7   SER FFF CA  
6722  C C   . SER F 7   ? 0.463 0.558 0.567 0.019  -0.121 -0.040 7   SER FFF C   
6723  O O   . SER F 7   ? 0.400 0.496 0.514 0.015  -0.110 -0.038 7   SER FFF O   
6724  C CB  . SER F 7   ? 0.471 0.549 0.552 0.011  -0.133 -0.050 7   SER FFF CB  
6725  O OG  . SER F 7   ? 0.495 0.581 0.599 -0.002 -0.129 -0.052 7   SER FFF OG  
6726  N N   . GLY F 8   ? 0.505 0.614 0.615 0.028  -0.134 -0.042 8   GLY FFF N   
6727  C CA  . GLY F 8   ? 0.529 0.662 0.671 0.031  -0.136 -0.040 8   GLY FFF CA  
6728  C C   . GLY F 8   ? 0.565 0.692 0.692 0.048  -0.128 -0.031 8   GLY FFF C   
6729  O O   . GLY F 8   ? 0.615 0.762 0.768 0.054  -0.127 -0.028 8   GLY FFF O   
6730  N N   . GLY F 9   ? 0.580 0.677 0.672 0.057  -0.117 -0.025 9   GLY FFF N   
6731  C CA  . GLY F 9   ? 0.629 0.711 0.706 0.074  -0.103 -0.015 9   GLY FFF CA  
6732  C C   . GLY F 9   ? 0.637 0.724 0.693 0.102  -0.117 -0.011 9   GLY FFF C   
6733  O O   . GLY F 9   ? 0.674 0.784 0.737 0.105  -0.142 -0.021 9   GLY FFF O   
6734  N N   . GLY F 10  ? 0.650 0.713 0.681 0.124  -0.101 0.002  10  GLY FFF N   
6735  C CA  . GLY F 10  ? 0.697 0.759 0.694 0.161  -0.112 0.008  10  GLY FFF CA  
6736  C C   . GLY F 10  ? 0.726 0.795 0.732 0.178  -0.105 0.016  10  GLY FFF C   
6737  O O   . GLY F 10  ? 0.704 0.764 0.731 0.163  -0.083 0.020  10  GLY FFF O   
6738  N N   . LEU F 11  ? 0.786 0.868 0.771 0.215  -0.124 0.018  11  LEU FFF N   
6739  C CA  . LEU F 11  ? 0.820 0.906 0.802 0.243  -0.119 0.028  11  LEU FFF CA  
6740  C C   . LEU F 11  ? 0.777 0.924 0.830 0.228  -0.138 0.016  11  LEU FFF C   
6741  O O   . LEU F 11  ? 0.766 0.953 0.857 0.215  -0.168 -0.003 11  LEU FFF O   
6742  C CB  . LEU F 11  ? 0.891 0.968 0.815 0.295  -0.135 0.033  11  LEU FFF CB  
6743  C CG  . LEU F 11  ? 0.962 1.040 0.871 0.336  -0.132 0.045  11  LEU FFF CG  
6744  C CD1 . LEU F 11  ? 0.962 0.990 0.861 0.329  -0.083 0.067  11  LEU FFF CD1 
6745  C CD2 . LEU F 11  ? 1.051 1.108 0.883 0.396  -0.148 0.051  11  LEU FFF CD2 
6746  N N   . VAL F 12  ? 0.761 0.908 0.834 0.229  -0.119 0.025  12  VAL FFF N   
6747  C CA  . VAL F 12  ? 0.739 0.939 0.879 0.221  -0.129 0.018  12  VAL FFF CA  
6748  C C   . VAL F 12  ? 0.780 0.971 0.912 0.247  -0.110 0.033  12  VAL FFF C   
6749  O O   . VAL F 12  ? 0.798 0.935 0.884 0.254  -0.081 0.047  12  VAL FFF O   
6750  C CB  . VAL F 12  ? 0.733 0.939 0.912 0.180  -0.116 0.012  12  VAL FFF CB  
6751  C CG1 . VAL F 12  ? 0.765 0.926 0.918 0.169  -0.083 0.022  12  VAL FFF CG1 
6752  C CG2 . VAL F 12  ? 0.710 0.970 0.965 0.171  -0.123 0.005  12  VAL FFF CG2 
6753  N N   . GLN F 13  ? 0.794 1.038 0.976 0.263  -0.125 0.029  13  GLN FFF N   
6754  C CA  . GLN F 13  ? 0.829 1.070 1.009 0.291  -0.108 0.043  13  GLN FFF CA  
6755  C C   . GLN F 13  ? 0.766 0.990 0.966 0.266  -0.074 0.050  13  GLN FFF C   
6756  O O   . GLN F 13  ? 0.722 0.965 0.963 0.234  -0.073 0.041  13  GLN FFF O   
6757  C CB  . GLN F 13  ? 0.878 1.189 1.114 0.317  -0.139 0.033  13  GLN FFF CB  
6758  C CG  . GLN F 13  ? 0.971 1.285 1.161 0.361  -0.172 0.028  13  GLN FFF CG  
6759  C CD  . GLN F 13  ? 1.098 1.385 1.237 0.411  -0.158 0.048  13  GLN FFF CD  
6760  O OE1 . GLN F 13  ? 1.188 1.404 1.261 0.417  -0.120 0.070  13  GLN FFF OE1 
6761  N NE2 . GLN F 13  ? 1.140 1.484 1.314 0.448  -0.186 0.040  13  GLN FFF NE2 
6762  N N   . ALA F 14  ? 0.762 0.945 0.927 0.283  -0.046 0.065  14  ALA FFF N   
6763  C CA  . ALA F 14  ? 0.741 0.903 0.913 0.272  -0.015 0.069  14  ALA FFF CA  
6764  C C   . ALA F 14  ? 0.689 0.908 0.931 0.265  -0.018 0.066  14  ALA FFF C   
6765  O O   . ALA F 14  ? 0.696 0.970 0.985 0.282  -0.039 0.063  14  ALA FFF O   
6766  C CB  . ALA F 14  ? 0.785 0.907 0.919 0.302  0.009  0.084  14  ALA FFF CB  
6767  N N   . GLY F 15  ? 0.664 0.870 0.915 0.243  0.002  0.065  15  GLY FFF N   
6768  C CA  . GLY F 15  ? 0.632 0.880 0.947 0.235  0.011  0.065  15  GLY FFF CA  
6769  C C   . GLY F 15  ? 0.598 0.881 0.958 0.208  -0.009 0.053  15  GLY FFF C   
6770  O O   . GLY F 15  ? 0.588 0.893 0.999 0.197  0.007  0.054  15  GLY FFF O   
6771  N N   . GLY F 16  ? 0.594 0.876 0.933 0.200  -0.037 0.042  16  GLY FFF N   
6772  C CA  . GLY F 16  ? 0.559 0.867 0.934 0.176  -0.058 0.028  16  GLY FFF CA  
6773  C C   . GLY F 16  ? 0.552 0.825 0.900 0.149  -0.042 0.028  16  GLY FFF C   
6774  O O   . GLY F 16  ? 0.539 0.768 0.841 0.152  -0.018 0.036  16  GLY FFF O   
6775  N N   . SER F 17  ? 0.574 0.862 0.947 0.128  -0.057 0.016  17  SER FFF N   
6776  C CA  . SER F 17  ? 0.593 0.852 0.945 0.105  -0.045 0.015  17  SER FFF CA  
6777  C C   . SER F 17  ? 0.610 0.861 0.936 0.093  -0.071 0.003  17  SER FFF C   
6778  O O   . SER F 17  ? 0.651 0.927 0.992 0.099  -0.098 -0.007 17  SER FFF O   
6779  C CB  . SER F 17  ? 0.589 0.869 1.002 0.092  -0.026 0.016  17  SER FFF CB  
6780  O OG  . SER F 17  ? 0.660 0.931 1.079 0.105  0.008  0.031  17  SER FFF OG  
6781  N N   . LEU F 18  ? 0.616 0.831 0.901 0.080  -0.062 0.003  18  LEU FFF N   
6782  C CA  . LEU F 18  ? 0.595 0.798 0.857 0.066  -0.079 -0.006 18  LEU FFF CA  
6783  C C   . LEU F 18  ? 0.568 0.749 0.817 0.053  -0.063 -0.005 18  LEU FFF C   
6784  O O   . LEU F 18  ? 0.575 0.734 0.799 0.061  -0.044 0.001  18  LEU FFF O   
6785  C CB  . LEU F 18  ? 0.639 0.811 0.848 0.075  -0.084 -0.006 18  LEU FFF CB  
6786  C CG  . LEU F 18  ? 0.675 0.855 0.873 0.090  -0.103 -0.007 18  LEU FFF CG  
6787  C CD1 . LEU F 18  ? 0.740 0.878 0.887 0.095  -0.095 -0.004 18  LEU FFF CD1 
6788  C CD2 . LEU F 18  ? 0.655 0.862 0.877 0.084  -0.128 -0.020 18  LEU FFF CD2 
6789  N N   . ARG F 19  ? 0.552 0.736 0.813 0.038  -0.071 -0.012 19  ARG FFF N   
6790  C CA  . ARG F 19  ? 0.551 0.709 0.785 0.030  -0.060 -0.011 19  ARG FFF CA  
6791  C C   . ARG F 19  ? 0.549 0.692 0.748 0.025  -0.078 -0.020 19  ARG FFF C   
6792  O O   . ARG F 19  ? 0.551 0.704 0.763 0.016  -0.094 -0.028 19  ARG FFF O   
6793  C CB  . ARG F 19  ? 0.574 0.739 0.850 0.019  -0.046 -0.010 19  ARG FFF CB  
6794  C CG  . ARG F 19  ? 0.639 0.771 0.878 0.023  -0.024 -0.002 19  ARG FFF CG  
6795  C CD  . ARG F 19  ? 0.670 0.797 0.944 0.014  -0.001 0.004  19  ARG FFF CD  
6796  N NE  . ARG F 19  ? 0.678 0.814 0.974 -0.005 -0.022 -0.010 19  ARG FFF NE  
6797  C CZ  . ARG F 19  ? 0.722 0.845 1.037 -0.016 -0.008 -0.010 19  ARG FFF CZ  
6798  N NH1 . ARG F 19  ? 0.766 0.860 1.077 -0.009 0.031  0.006  19  ARG FFF NH1 
6799  N NH2 . ARG F 19  ? 0.704 0.835 1.036 -0.031 -0.032 -0.026 19  ARG FFF NH2 
6800  N N   . LEU F 20  ? 0.524 0.645 0.685 0.031  -0.075 -0.021 20  LEU FFF N   
6801  C CA  . LEU F 20  ? 0.509 0.614 0.645 0.025  -0.084 -0.029 20  LEU FFF CA  
6802  C C   . LEU F 20  ? 0.522 0.620 0.651 0.020  -0.081 -0.031 20  LEU FFF C   
6803  O O   . LEU F 20  ? 0.497 0.589 0.622 0.027  -0.066 -0.025 20  LEU FFF O   
6804  C CB  . LEU F 20  ? 0.503 0.592 0.620 0.032  -0.081 -0.035 20  LEU FFF CB  
6805  C CG  . LEU F 20  ? 0.533 0.618 0.652 0.039  -0.077 -0.032 20  LEU FFF CG  
6806  C CD1 . LEU F 20  ? 0.532 0.596 0.643 0.039  -0.072 -0.042 20  LEU FFF CD1 
6807  C CD2 . LEU F 20  ? 0.573 0.663 0.693 0.040  -0.085 -0.026 20  LEU FFF CD2 
6808  N N   . ALA F 21  ? 0.511 0.606 0.635 0.012  -0.091 -0.036 21  ALA FFF N   
6809  C CA  . ALA F 21  ? 0.520 0.602 0.629 0.010  -0.087 -0.037 21  ALA FFF CA  
6810  C C   . ALA F 21  ? 0.523 0.599 0.616 0.010  -0.096 -0.046 21  ALA FFF C   
6811  O O   . ALA F 21  ? 0.540 0.616 0.635 0.007  -0.101 -0.048 21  ALA FFF O   
6812  C CB  . ALA F 21  ? 0.498 0.584 0.628 -0.001 -0.087 -0.036 21  ALA FFF CB  
6813  N N   . CYS F 22  ? 0.520 0.587 0.595 0.017  -0.095 -0.050 22  CYS FFF N   
6814  C CA  . CYS F 22  ? 0.520 0.586 0.590 0.018  -0.103 -0.060 22  CYS FFF CA  
6815  C C   . CYS F 22  ? 0.499 0.555 0.551 0.024  -0.102 -0.059 22  CYS FFF C   
6816  O O   . CYS F 22  ? 0.515 0.563 0.546 0.040  -0.096 -0.056 22  CYS FFF O   
6817  C CB  . CYS F 22  ? 0.564 0.634 0.638 0.026  -0.109 -0.074 22  CYS FFF CB  
6818  S SG  . CYS F 22  ? 0.602 0.680 0.688 0.029  -0.119 -0.092 22  CYS FFF SG  
6819  N N   . ILE F 23  ? 0.465 0.519 0.518 0.017  -0.104 -0.059 23  ILE FFF N   
6820  C CA  . ILE F 23  ? 0.467 0.507 0.501 0.023  -0.101 -0.057 23  ILE FFF CA  
6821  C C   . ILE F 23  ? 0.460 0.508 0.495 0.032  -0.109 -0.068 23  ILE FFF C   
6822  O O   . ILE F 23  ? 0.454 0.512 0.512 0.024  -0.112 -0.075 23  ILE FFF O   
6823  C CB  . ILE F 23  ? 0.459 0.488 0.497 0.010  -0.097 -0.051 23  ILE FFF CB  
6824  C CG1 . ILE F 23  ? 0.480 0.487 0.499 0.016  -0.088 -0.047 23  ILE FFF CG1 
6825  C CG2 . ILE F 23  ? 0.450 0.482 0.493 0.002  -0.105 -0.056 23  ILE FFF CG2 
6826  C CD1 . ILE F 23  ? 0.474 0.466 0.501 0.001  -0.085 -0.047 23  ILE FFF CD1 
6827  N N   . ALA F 24  ? 0.463 0.506 0.476 0.051  -0.111 -0.071 24  ALA FFF N   
6828  C CA  . ALA F 24  ? 0.455 0.514 0.476 0.065  -0.123 -0.085 24  ALA FFF CA  
6829  C C   . ALA F 24  ? 0.462 0.505 0.466 0.068  -0.116 -0.077 24  ALA FFF C   
6830  O O   . ALA F 24  ? 0.499 0.516 0.476 0.069  -0.103 -0.063 24  ALA FFF O   
6831  C CB  . ALA F 24  ? 0.483 0.548 0.484 0.093  -0.136 -0.097 24  ALA FFF CB  
6832  N N   . SER F 25  ? 0.459 0.612 0.577 -0.055 0.037  0.004  25  SER FFF N   
6833  C CA  . SER F 25  ? 0.434 0.629 0.564 -0.041 0.052  0.008  25  SER FFF CA  
6834  C C   . SER F 25  ? 0.444 0.624 0.571 -0.041 0.064  0.012  25  SER FFF C   
6835  O O   . SER F 25  ? 0.467 0.615 0.590 -0.057 0.061  0.015  25  SER FFF O   
6836  C CB  . SER F 25  ? 0.425 0.678 0.542 -0.047 0.045  0.034  25  SER FFF CB  
6837  O OG  . SER F 25  ? 0.427 0.695 0.529 -0.077 0.038  0.060  25  SER FFF OG  
6838  N N   . GLY F 26  ? 0.474 0.671 0.595 -0.017 0.076  0.011  26  GLY FFF N   
6839  C CA  . GLY F 26  ? 0.512 0.698 0.614 -0.007 0.085  0.018  26  GLY FFF CA  
6840  C C   . GLY F 26  ? 0.547 0.655 0.634 -0.003 0.101  -0.004 26  GLY FFF C   
6841  O O   . GLY F 26  ? 0.545 0.623 0.646 -0.018 0.105  -0.025 26  GLY FFF O   
6842  N N   . ARG F 27  ? 0.616 0.696 0.669 0.015  0.110  0.001  27  ARG FFF N   
6843  C CA  . ARG F 27  ? 0.712 0.702 0.730 0.012  0.128  -0.016 27  ARG FFF CA  
6844  C C   . ARG F 27  ? 0.677 0.651 0.691 0.001  0.129  -0.005 27  ARG FFF C   
6845  O O   . ARG F 27  ? 0.760 0.659 0.730 0.004  0.145  -0.011 27  ARG FFF O   
6846  C CB  . ARG F 27  ? 0.850 0.792 0.803 0.050  0.136  -0.021 27  ARG FFF CB  
6847  C CG  . ARG F 27  ? 0.969 0.872 0.905 0.049  0.141  -0.042 27  ARG FFF CG  
6848  C CD  . ARG F 27  ? 1.183 1.015 1.028 0.096  0.145  -0.047 27  ARG FFF CD  
6849  N NE  . ARG F 27  ? 1.257 1.135 1.076 0.147  0.136  -0.028 27  ARG FFF NE  
6850  C CZ  . ARG F 27  ? 1.274 1.230 1.087 0.196  0.123  -0.020 27  ARG FFF CZ  
6851  N NH1 . ARG F 27  ? 1.299 1.279 1.121 0.205  0.118  -0.029 27  ARG FFF NH1 
6852  N NH2 . ARG F 27  ? 1.264 1.283 1.060 0.238  0.115  -0.007 27  ARG FFF NH2 
6853  N N   . THR F 28  ? 0.584 0.609 0.631 -0.016 0.113  0.011  28  THR FFF N   
6854  C CA  . THR F 28  ? 0.575 0.578 0.614 -0.026 0.112  0.020  28  THR FFF CA  
6855  C C   . THR F 28  ? 0.542 0.543 0.609 -0.056 0.101  0.017  28  THR FFF C   
6856  O O   . THR F 28  ? 0.542 0.543 0.603 -0.066 0.090  0.030  28  THR FFF O   
6857  C CB  . THR F 28  ? 0.562 0.618 0.589 -0.011 0.100  0.040  28  THR FFF CB  
6858  O OG1 . THR F 28  ? 0.527 0.663 0.580 -0.025 0.083  0.053  28  THR FFF OG1 
6859  C CG2 . THR F 28  ? 0.589 0.632 0.569 0.034  0.110  0.038  28  THR FFF CG2 
6860  N N   . PHE F 29  ? 0.510 0.504 0.597 -0.064 0.105  -0.003 29  PHE FFF N   
6861  C CA  . PHE F 29  ? 0.483 0.472 0.584 -0.077 0.093  -0.012 29  PHE FFF CA  
6862  C C   . PHE F 29  ? 0.494 0.447 0.582 -0.081 0.099  -0.014 29  PHE FFF C   
6863  O O   . PHE F 29  ? 0.497 0.441 0.575 -0.085 0.079  -0.009 29  PHE FFF O   
6864  C CB  . PHE F 29  ? 0.472 0.472 0.595 -0.077 0.101  -0.040 29  PHE FFF CB  
6865  C CG  . PHE F 29  ? 0.462 0.470 0.593 -0.074 0.086  -0.055 29  PHE FFF CG  
6866  C CD1 . PHE F 29  ? 0.459 0.472 0.578 -0.068 0.060  -0.045 29  PHE FFF CD1 
6867  C CD2 . PHE F 29  ? 0.452 0.462 0.592 -0.076 0.097  -0.079 29  PHE FFF CD2 
6868  C CE1 . PHE F 29  ? 0.472 0.475 0.577 -0.053 0.042  -0.059 29  PHE FFF CE1 
6869  C CE2 . PHE F 29  ? 0.457 0.482 0.595 -0.060 0.080  -0.096 29  PHE FFF CE2 
6870  C CZ  . PHE F 29  ? 0.466 0.480 0.582 -0.044 0.051  -0.086 29  PHE FFF CZ  
6871  N N   . HIS F 30  ? 0.505 0.427 0.578 -0.081 0.122  -0.021 30  HIS FFF N   
6872  C CA  . HIS F 30  ? 0.542 0.428 0.597 -0.085 0.132  -0.024 30  HIS FFF CA  
6873  C C   . HIS F 30  ? 0.544 0.423 0.581 -0.080 0.113  -0.000 30  HIS FFF C   
6874  O O   . HIS F 30  ? 0.568 0.421 0.591 -0.080 0.111  -0.002 30  HIS FFF O   
6875  C CB  . HIS F 30  ? 0.580 0.420 0.605 -0.090 0.162  -0.031 30  HIS FFF CB  
6876  C CG  . HIS F 30  ? 0.612 0.427 0.599 -0.068 0.161  -0.012 30  HIS FFF CG  
6877  N ND1 . HIS F 30  ? 0.630 0.459 0.611 -0.052 0.158  -0.009 30  HIS FFF ND1 
6878  C CD2 . HIS F 30  ? 0.638 0.431 0.592 -0.051 0.158  0.004  30  HIS FFF CD2 
6879  C CE1 . HIS F 30  ? 0.643 0.467 0.588 -0.023 0.153  0.007  30  HIS FFF CE1 
6880  N NE2 . HIS F 30  ? 0.652 0.456 0.582 -0.023 0.152  0.015  30  HIS FFF NE2 
6881  N N   . SER F 31  ? 0.541 0.449 0.575 -0.076 0.098  0.020  31  SER FFF N   
6882  C CA  . SER F 31  ? 0.552 0.469 0.569 -0.080 0.079  0.040  31  SER FFF CA  
6883  C C   . SER F 31  ? 0.561 0.478 0.573 -0.101 0.052  0.048  31  SER FFF C   
6884  O O   . SER F 31  ? 0.572 0.489 0.562 -0.116 0.034  0.064  31  SER FFF O   
6885  C CB  . SER F 31  ? 0.543 0.510 0.555 -0.067 0.078  0.054  31  SER FFF CB  
6886  O OG  . SER F 31  ? 0.536 0.560 0.568 -0.077 0.067  0.061  31  SER FFF OG  
6887  N N   . TYR F 32  ? 0.555 0.465 0.576 -0.103 0.047  0.036  32  TYR FFF N   
6888  C CA  . TYR F 32  ? 0.587 0.474 0.580 -0.118 0.018  0.043  32  TYR FFF CA  
6889  C C   . TYR F 32  ? 0.626 0.457 0.594 -0.103 0.010  0.026  32  TYR FFF C   
6890  O O   . TYR F 32  ? 0.575 0.417 0.566 -0.083 0.026  0.002  32  TYR FFF O   
6891  C CB  . TYR F 32  ? 0.575 0.491 0.580 -0.122 0.013  0.044  32  TYR FFF CB  
6892  C CG  . TYR F 32  ? 0.558 0.534 0.573 -0.139 0.014  0.064  32  TYR FFF CG  
6893  C CD1 . TYR F 32  ? 0.548 0.574 0.595 -0.121 0.035  0.060  32  TYR FFF CD1 
6894  C CD2 . TYR F 32  ? 0.593 0.578 0.576 -0.175 -0.007 0.087  32  TYR FFF CD2 
6895  C CE1 . TYR F 32  ? 0.534 0.631 0.588 -0.124 0.035  0.076  32  TYR FFF CE1 
6896  C CE2 . TYR F 32  ? 0.592 0.661 0.590 -0.191 -0.004 0.104  32  TYR FFF CE2 
6897  C CZ  . TYR F 32  ? 0.548 0.682 0.585 -0.160 0.016  0.097  32  TYR FFF CZ  
6898  O OH  . TYR F 32  ? 0.550 0.781 0.598 -0.164 0.018  0.110  32  TYR FFF OH  
6899  N N   . VAL F 33  ? 0.425 0.403 0.423 0.019  -0.012 -0.029 33  VAL FFF N   
6900  C CA  . VAL F 33  ? 0.480 0.463 0.479 0.021  -0.007 -0.033 33  VAL FFF CA  
6901  C C   . VAL F 33  ? 0.499 0.482 0.510 0.021  -0.007 -0.034 33  VAL FFF C   
6902  O O   . VAL F 33  ? 0.500 0.479 0.515 0.021  -0.010 -0.034 33  VAL FFF O   
6903  C CB  . VAL F 33  ? 0.519 0.498 0.509 0.023  -0.009 -0.041 33  VAL FFF CB  
6904  C CG1 . VAL F 33  ? 0.538 0.517 0.529 0.028  -0.004 -0.047 33  VAL FFF CG1 
6905  C CG2 . VAL F 33  ? 0.560 0.542 0.534 0.023  -0.011 -0.040 33  VAL FFF CG2 
6906  N N   . MET F 34  ? 0.520 0.510 0.536 0.022  -0.003 -0.032 34  MET FFF N   
6907  C CA  . MET F 34  ? 0.516 0.509 0.542 0.024  -0.003 -0.030 34  MET FFF CA  
6908  C C   . MET F 34  ? 0.504 0.499 0.535 0.030  0.000  -0.033 34  MET FFF C   
6909  O O   . MET F 34  ? 0.509 0.509 0.537 0.034  0.005  -0.035 34  MET FFF O   
6910  C CB  . MET F 34  ? 0.508 0.511 0.540 0.019  -0.004 -0.026 34  MET FFF CB  
6911  C CG  . MET F 34  ? 0.509 0.505 0.537 0.014  -0.008 -0.025 34  MET FFF CG  
6912  S SD  . MET F 34  ? 0.537 0.522 0.560 0.016  -0.012 -0.028 34  MET FFF SD  
6913  C CE  . MET F 34  ? 0.569 0.561 0.596 0.018  -0.014 -0.028 34  MET FFF CE  
6914  N N   . ALA F 35  ? 0.484 0.475 0.520 0.033  -0.002 -0.032 35  ALA FFF N   
6915  C CA  . ALA F 35  ? 0.483 0.469 0.523 0.041  0.001  -0.033 35  ALA FFF CA  
6916  C C   . ALA F 35  ? 0.481 0.471 0.531 0.044  -0.001 -0.026 35  ALA FFF C   
6917  O O   . ALA F 35  ? 0.488 0.480 0.536 0.040  -0.005 -0.022 35  ALA FFF O   
6918  C CB  . ALA F 35  ? 0.501 0.469 0.536 0.040  -0.000 -0.040 35  ALA FFF CB  
6919  N N   . TRP F 36  ? 0.498 0.488 0.555 0.053  0.001  -0.026 36  TRP FFF N   
6920  C CA  . TRP F 36  ? 0.506 0.497 0.572 0.060  -0.001 -0.018 36  TRP FFF CA  
6921  C C   . TRP F 36  ? 0.512 0.480 0.579 0.066  0.001  -0.019 36  TRP FFF C   
6922  O O   . TRP F 36  ? 0.522 0.482 0.588 0.071  0.005  -0.028 36  TRP FFF O   
6923  C CB  . TRP F 36  ? 0.538 0.550 0.615 0.066  -0.000 -0.014 36  TRP FFF CB  
6924  C CG  . TRP F 36  ? 0.505 0.537 0.583 0.058  -0.005 -0.011 36  TRP FFF CG  
6925  C CD1 . TRP F 36  ? 0.507 0.551 0.587 0.052  -0.002 -0.015 36  TRP FFF CD1 
6926  C CD2 . TRP F 36  ? 0.506 0.545 0.582 0.054  -0.012 -0.005 36  TRP FFF CD2 
6927  N NE1 . TRP F 36  ? 0.500 0.556 0.581 0.044  -0.009 -0.012 36  TRP FFF NE1 
6928  C CE2 . TRP F 36  ? 0.505 0.559 0.583 0.046  -0.015 -0.007 36  TRP FFF CE2 
6929  C CE3 . TRP F 36  ? 0.521 0.556 0.593 0.058  -0.017 0.002  36  TRP FFF CE3 
6930  C CZ2 . TRP F 36  ? 0.512 0.574 0.587 0.040  -0.024 -0.006 36  TRP FFF CZ2 
6931  C CZ3 . TRP F 36  ? 0.531 0.577 0.597 0.053  -0.024 0.005  36  TRP FFF CZ3 
6932  C CH2 . TRP F 36  ? 0.535 0.594 0.602 0.045  -0.028 -0.000 36  TRP FFF CH2 
6933  N N   . PHE F 37  ? 0.516 0.473 0.583 0.064  -0.002 -0.011 37  PHE FFF N   
6934  C CA  . PHE F 37  ? 0.531 0.465 0.604 0.070  -0.002 -0.008 37  PHE FFF CA  
6935  C C   . PHE F 37  ? 0.541 0.480 0.620 0.077  -0.004 0.007  37  PHE FFF C   
6936  O O   . PHE F 37  ? 0.529 0.489 0.605 0.075  -0.007 0.013  37  PHE FFF O   
6937  C CB  . PHE F 37  ? 0.543 0.460 0.612 0.059  -0.003 -0.008 37  PHE FFF CB  
6938  C CG  . PHE F 37  ? 0.512 0.421 0.577 0.052  -0.003 -0.022 37  PHE FFF CG  
6939  C CD1 . PHE F 37  ? 0.480 0.405 0.537 0.046  -0.004 -0.027 37  PHE FFF CD1 
6940  C CD2 . PHE F 37  ? 0.541 0.424 0.607 0.051  -0.004 -0.029 37  PHE FFF CD2 
6941  C CE1 . PHE F 37  ? 0.484 0.403 0.534 0.041  -0.005 -0.038 37  PHE FFF CE1 
6942  C CE2 . PHE F 37  ? 0.541 0.419 0.600 0.045  -0.007 -0.043 37  PHE FFF CE2 
6943  C CZ  . PHE F 37  ? 0.523 0.421 0.574 0.040  -0.007 -0.047 37  PHE FFF CZ  
6944  N N   . ARG F 38  ? 0.570 0.489 0.656 0.086  -0.004 0.012  38  ARG FFF N   
6945  C CA  . ARG F 38  ? 0.581 0.503 0.672 0.094  -0.007 0.029  38  ARG FFF CA  
6946  C C   . ARG F 38  ? 0.606 0.495 0.701 0.094  -0.007 0.038  38  ARG FFF C   
6947  O O   . ARG F 38  ? 0.615 0.477 0.711 0.091  -0.005 0.028  38  ARG FFF O   
6948  C CB  . ARG F 38  ? 0.573 0.509 0.676 0.110  -0.008 0.030  38  ARG FFF CB  
6949  C CG  . ARG F 38  ? 0.568 0.481 0.680 0.123  -0.003 0.023  38  ARG FFF CG  
6950  C CD  . ARG F 38  ? 0.557 0.493 0.681 0.139  -0.002 0.022  38  ARG FFF CD  
6951  N NE  . ARG F 38  ? 0.577 0.492 0.708 0.154  0.004  0.011  38  ARG FFF NE  
6952  C CZ  . ARG F 38  ? 0.566 0.497 0.711 0.172  0.008  0.009  38  ARG FFF CZ  
6953  N NH1 . ARG F 38  ? 0.560 0.531 0.718 0.176  0.006  0.018  38  ARG FFF NH1 
6954  N NH2 . ARG F 38  ? 0.589 0.495 0.737 0.186  0.015  -0.003 38  ARG FFF NH2 
6955  N N   . GLN F 39  ? 0.607 0.497 0.701 0.097  -0.009 0.057  39  GLN FFF N   
6956  C CA  . GLN F 39  ? 0.630 0.489 0.727 0.095  -0.009 0.071  39  GLN FFF CA  
6957  C C   . GLN F 39  ? 0.653 0.514 0.754 0.109  -0.012 0.091  39  GLN FFF C   
6958  O O   . GLN F 39  ? 0.626 0.512 0.717 0.109  -0.015 0.104  39  GLN FFF O   
6959  C CB  . GLN F 39  ? 0.637 0.499 0.727 0.078  -0.007 0.077  39  GLN FFF CB  
6960  C CG  . GLN F 39  ? 0.679 0.511 0.775 0.073  -0.005 0.094  39  GLN FFF CG  
6961  C CD  . GLN F 39  ? 0.685 0.523 0.780 0.055  -0.001 0.097  39  GLN FFF CD  
6962  O OE1 . GLN F 39  ? 0.644 0.510 0.728 0.050  0.001  0.096  39  GLN FFF OE1 
6963  N NE2 . GLN F 39  ? 0.751 0.560 0.857 0.044  -0.000 0.101  39  GLN FFF NE2 
6964  N N   . ALA F 40  ? 0.682 0.516 0.795 0.122  -0.012 0.092  40  ALA FFF N   
6965  C CA  . ALA F 40  ? 0.720 0.544 0.839 0.137  -0.016 0.114  40  ALA FFF CA  
6966  C C   . ALA F 40  ? 0.757 0.553 0.874 0.127  -0.014 0.133  40  ALA FFF C   
6967  O O   . ALA F 40  ? 0.728 0.503 0.846 0.111  -0.011 0.125  40  ALA FFF O   
6968  C CB  . ALA F 40  ? 0.751 0.556 0.885 0.156  -0.015 0.105  40  ALA FFF CB  
6969  N N   . PRO F 41  ? 0.815 0.612 0.928 0.133  -0.017 0.160  41  PRO FFF N   
6970  C CA  . PRO F 41  ? 0.856 0.630 0.967 0.122  -0.015 0.182  41  PRO FFF CA  
6971  C C   . PRO F 41  ? 0.892 0.613 1.019 0.121  -0.013 0.179  41  PRO FFF C   
6972  O O   . PRO F 41  ? 0.917 0.617 1.056 0.139  -0.015 0.174  41  PRO FFF O   
6973  C CB  . PRO F 41  ? 0.877 0.665 0.980 0.134  -0.019 0.211  41  PRO FFF CB  
6974  C CG  . PRO F 41  ? 0.868 0.681 0.976 0.155  -0.026 0.203  41  PRO FFF CG  
6975  C CD  . PRO F 41  ? 0.806 0.632 0.919 0.151  -0.024 0.171  41  PRO FFF CD  
6976  N N   . GLY F 42  ? 0.890 0.592 1.020 0.101  -0.009 0.181  42  GLY FFF N   
6977  C CA  . GLY F 42  ? 0.903 0.552 1.049 0.094  -0.009 0.177  42  GLY FFF CA  
6978  C C   . GLY F 42  ? 0.878 0.518 1.027 0.089  -0.009 0.142  42  GLY FFF C   
6979  O O   . GLY F 42  ? 0.883 0.483 1.044 0.077  -0.010 0.135  42  GLY FFF O   
6980  N N   . LYS F 43  ? 0.840 0.516 0.981 0.093  -0.009 0.122  43  LYS FFF N   
6981  C CA  . LYS F 43  ? 0.860 0.531 1.001 0.090  -0.009 0.090  43  LYS FFF CA  
6982  C C   . LYS F 43  ? 0.848 0.549 0.981 0.071  -0.008 0.081  43  LYS FFF C   
6983  O O   . LYS F 43  ? 0.823 0.554 0.949 0.065  -0.006 0.097  43  LYS FFF O   
6984  C CB  . LYS F 43  ? 0.862 0.549 1.000 0.111  -0.009 0.074  43  LYS FFF CB  
6985  C CG  . LYS F 43  ? 0.924 0.575 1.071 0.131  -0.010 0.069  43  LYS FFF CG  
6986  C CD  . LYS F 43  ? 0.902 0.576 1.047 0.150  -0.007 0.050  43  LYS FFF CD  
6987  C CE  . LYS F 43  ? 0.959 0.599 1.114 0.174  -0.006 0.043  43  LYS FFF CE  
6988  N NZ  . LYS F 43  ? 0.970 0.603 1.136 0.190  -0.008 0.070  43  LYS FFF NZ  
6989  N N   . GLU F 44  ? 0.879 0.572 1.011 0.063  -0.009 0.056  44  GLU FFF N   
6990  C CA  . GLU F 44  ? 0.875 0.597 1.001 0.048  -0.009 0.046  44  GLU FFF CA  
6991  C C   . GLU F 44  ? 0.800 0.558 0.914 0.059  -0.008 0.036  44  GLU FFF C   
6992  O O   . GLU F 44  ? 0.829 0.589 0.943 0.076  -0.007 0.035  44  GLU FFF O   
6993  C CB  . GLU F 44  ? 0.973 0.672 1.103 0.036  -0.014 0.025  44  GLU FFF CB  
6994  C CG  . GLU F 44  ? 1.139 0.797 1.284 0.023  -0.017 0.033  44  GLU FFF CG  
6995  C CD  . GLU F 44  ? 1.217 0.885 1.373 0.008  -0.014 0.060  44  GLU FFF CD  
6996  O OE1 . GLU F 44  ? 1.176 0.882 1.329 -0.001 -0.011 0.064  44  GLU FFF OE1 
6997  O OE2 . GLU F 44  ? 1.357 0.994 1.524 0.005  -0.014 0.078  44  GLU FFF OE2 
6998  N N   . ARG F 45  ? 0.735 0.522 0.843 0.049  -0.007 0.031  45  ARG FFF N   
6999  C CA  . ARG F 45  ? 0.700 0.518 0.798 0.055  -0.006 0.020  45  ARG FFF CA  
7000  C C   . ARG F 45  ? 0.724 0.530 0.818 0.062  -0.006 -0.002 45  ARG FFF C   
7001  O O   . ARG F 45  ? 0.770 0.559 0.864 0.054  -0.009 -0.015 45  ARG FFF O   
7002  C CB  . ARG F 45  ? 0.686 0.529 0.778 0.042  -0.006 0.017  45  ARG FFF CB  
7003  C CG  . ARG F 45  ? 0.676 0.543 0.763 0.042  -0.003 0.034  45  ARG FFF CG  
7004  C CD  . ARG F 45  ? 0.692 0.576 0.778 0.029  -0.002 0.034  45  ARG FFF CD  
7005  N NE  . ARG F 45  ? 0.713 0.610 0.796 0.027  0.002  0.053  45  ARG FFF NE  
7006  C CZ  . ARG F 45  ? 0.724 0.644 0.799 0.024  0.005  0.054  45  ARG FFF CZ  
7007  N NH1 . ARG F 45  ? 0.728 0.661 0.801 0.021  0.004  0.040  45  ARG FFF NH1 
7008  N NH2 . ARG F 45  ? 0.779 0.710 0.848 0.024  0.009  0.070  45  ARG FFF NH2 
7009  N N   . GLU F 46  ? 0.738 0.556 0.831 0.078  -0.004 -0.005 46  GLU FFF N   
7010  C CA  . GLU F 46  ? 0.737 0.549 0.827 0.090  -0.001 -0.023 46  GLU FFF CA  
7011  C C   . GLU F 46  ? 0.688 0.535 0.769 0.089  0.001  -0.030 46  GLU FFF C   
7012  O O   . GLU F 46  ? 0.671 0.546 0.755 0.088  0.001  -0.018 46  GLU FFF O   
7013  C CB  . GLU F 46  ? 0.817 0.618 0.917 0.109  0.001  -0.017 46  GLU FFF CB  
7014  C CG  . GLU F 46  ? 0.901 0.708 1.000 0.127  0.006  -0.031 46  GLU FFF CG  
7015  C CD  . GLU F 46  ? 0.954 0.759 1.067 0.148  0.008  -0.021 46  GLU FFF CD  
7016  O OE1 . GLU F 46  ? 1.024 0.806 1.145 0.150  0.004  -0.006 46  GLU FFF OE1 
7017  O OE2 . GLU F 46  ? 0.957 0.786 1.075 0.164  0.014  -0.027 46  GLU FFF OE2 
7018  N N   . PHE F 47  ? 0.665 0.510 0.736 0.086  0.003  -0.047 47  PHE FFF N   
7019  C CA  . PHE F 47  ? 0.646 0.521 0.708 0.085  0.006  -0.052 47  PHE FFF CA  
7020  C C   . PHE F 47  ? 0.621 0.517 0.691 0.100  0.012  -0.050 47  PHE FFF C   
7021  O O   . PHE F 47  ? 0.628 0.512 0.702 0.115  0.016  -0.056 47  PHE FFF O   
7022  C CB  . PHE F 47  ? 0.635 0.501 0.682 0.081  0.006  -0.071 47  PHE FFF CB  
7023  C CG  . PHE F 47  ? 0.618 0.512 0.656 0.081  0.010  -0.074 47  PHE FFF CG  
7024  C CD1 . PHE F 47  ? 0.596 0.507 0.631 0.069  0.007  -0.068 47  PHE FFF CD1 
7025  C CD2 . PHE F 47  ? 0.651 0.555 0.684 0.094  0.018  -0.082 47  PHE FFF CD2 
7026  C CE1 . PHE F 47  ? 0.605 0.537 0.631 0.068  0.011  -0.069 47  PHE FFF CE1 
7027  C CE2 . PHE F 47  ? 0.642 0.572 0.668 0.093  0.023  -0.082 47  PHE FFF CE2 
7028  C CZ  . PHE F 47  ? 0.624 0.567 0.646 0.079  0.019  -0.075 47  PHE FFF CZ  
7029  N N   . VAL F 48  ? 0.589 0.515 0.661 0.097  0.012  -0.042 48  VAL FFF N   
7030  C CA  . VAL F 48  ? 0.576 0.530 0.659 0.108  0.017  -0.038 48  VAL FFF CA  
7031  C C   . VAL F 48  ? 0.559 0.534 0.635 0.104  0.023  -0.046 48  VAL FFF C   
7032  O O   . VAL F 48  ? 0.545 0.530 0.623 0.116  0.032  -0.052 48  VAL FFF O   
7033  C CB  . VAL F 48  ? 0.553 0.528 0.648 0.105  0.012  -0.023 48  VAL FFF CB  
7034  C CG1 . VAL F 48  ? 0.565 0.573 0.674 0.114  0.015  -0.019 48  VAL FFF CG1 
7035  C CG2 . VAL F 48  ? 0.552 0.507 0.652 0.111  0.007  -0.013 48  VAL FFF CG2 
7036  N N   . ALA F 49  ? 0.532 0.514 0.599 0.089  0.020  -0.044 49  ALA FFF N   
7037  C CA  . ALA F 49  ? 0.531 0.533 0.592 0.085  0.025  -0.047 49  ALA FFF CA  
7038  C C   . ALA F 49  ? 0.531 0.528 0.579 0.070  0.019  -0.046 49  ALA FFF C   
7039  O O   . ALA F 49  ? 0.536 0.524 0.585 0.063  0.012  -0.042 49  ALA FFF O   
7040  C CB  . ALA F 49  ? 0.510 0.543 0.587 0.086  0.027  -0.038 49  ALA FFF CB  
7041  N N   . ALA F 50  ? 0.532 0.536 0.569 0.066  0.023  -0.050 50  ALA FFF N   
7042  C CA  . ALA F 50  ? 0.516 0.517 0.542 0.055  0.019  -0.049 50  ALA FFF CA  
7043  C C   . ALA F 50  ? 0.493 0.512 0.514 0.052  0.025  -0.045 50  ALA FFF C   
7044  O O   . ALA F 50  ? 0.483 0.514 0.502 0.060  0.034  -0.048 50  ALA FFF O   
7045  C CB  . ALA F 50  ? 0.527 0.507 0.539 0.053  0.014  -0.058 50  ALA FFF CB  
7046  N N   . ILE F 51  ? 0.469 0.488 0.487 0.041  0.020  -0.039 51  ILE FFF N   
7047  C CA  . ILE F 51  ? 0.496 0.529 0.510 0.036  0.025  -0.032 51  ILE FFF CA  
7048  C C   . ILE F 51  ? 0.494 0.514 0.494 0.029  0.019  -0.030 51  ILE FFF C   
7049  O O   . ILE F 51  ? 0.488 0.497 0.491 0.025  0.011  -0.030 51  ILE FFF O   
7050  C CB  . ILE F 51  ? 0.489 0.537 0.522 0.030  0.025  -0.022 51  ILE FFF CB  
7051  C CG1 . ILE F 51  ? 0.509 0.572 0.543 0.023  0.031  -0.013 51  ILE FFF CG1 
7052  C CG2 . ILE F 51  ? 0.504 0.541 0.542 0.024  0.015  -0.021 51  ILE FFF CG2 
7053  C CD1 . ILE F 51  ? 0.516 0.599 0.573 0.016  0.032  -0.005 51  ILE FFF CD1 
7054  N N   . SER F 52  ? 0.513 0.537 0.497 0.030  0.023  -0.029 52  SER FFF N   
7055  C CA  . SER F 52  ? 0.535 0.549 0.503 0.026  0.017  -0.026 52  SER FFF CA  
7056  C C   . SER F 52  ? 0.549 0.563 0.525 0.017  0.015  -0.013 52  SER FFF C   
7057  O O   . SER F 52  ? 0.520 0.543 0.513 0.013  0.019  -0.008 52  SER FFF O   
7058  C CB  . SER F 52  ? 0.560 0.579 0.506 0.030  0.021  -0.028 52  SER FFF CB  
7059  O OG  . SER F 52  ? 0.605 0.614 0.537 0.028  0.012  -0.028 52  SER FFF OG  
7060  N N   . TRP F 53  ? 0.548 0.553 0.515 0.015  0.009  -0.008 53  TRP FFF N   
7061  C CA  . TRP F 53  ? 0.534 0.530 0.508 0.008  0.006  0.002  53  TRP FFF CA  
7062  C C   . TRP F 53  ? 0.529 0.535 0.507 0.001  0.014  0.014  53  TRP FFF C   
7063  O O   . TRP F 53  ? 0.548 0.552 0.543 -0.006 0.013  0.016  53  TRP FFF O   
7064  C CB  . TRP F 53  ? 0.529 0.514 0.489 0.010  -0.001 0.007  53  TRP FFF CB  
7065  C CG  . TRP F 53  ? 0.512 0.494 0.468 0.015  -0.008 -0.004 53  TRP FFF CG  
7066  C CD1 . TRP F 53  ? 0.503 0.479 0.472 0.017  -0.014 -0.009 53  TRP FFF CD1 
7067  C CD2 . TRP F 53  ? 0.495 0.482 0.436 0.020  -0.011 -0.009 53  TRP FFF CD2 
7068  N NE1 . TRP F 53  ? 0.490 0.467 0.455 0.020  -0.019 -0.017 53  TRP FFF NE1 
7069  C CE2 . TRP F 53  ? 0.505 0.488 0.453 0.022  -0.019 -0.018 53  TRP FFF CE2 
7070  C CE3 . TRP F 53  ? 0.524 0.519 0.444 0.022  -0.007 -0.009 53  TRP FFF CE3 
7071  C CZ2 . TRP F 53  ? 0.506 0.491 0.443 0.024  -0.026 -0.026 53  TRP FFF CZ2 
7072  C CZ3 . TRP F 53  ? 0.540 0.535 0.445 0.026  -0.014 -0.019 53  TRP FFF CZ3 
7073  C CH2 . TRP F 53  ? 0.526 0.517 0.441 0.026  -0.024 -0.027 53  TRP FFF CH2 
7074  N N   . SER F 54  ? 0.545 0.563 0.510 0.003  0.022  0.019  54  SER FFF N   
7075  C CA  . SER F 54  ? 0.559 0.591 0.529 -0.005 0.032  0.033  54  SER FFF CA  
7076  C C   . SER F 54  ? 0.556 0.609 0.546 -0.005 0.040  0.030  54  SER FFF C   
7077  O O   . SER F 54  ? 0.537 0.607 0.537 -0.012 0.049  0.042  54  SER FFF O   
7078  C CB  . SER F 54  ? 0.585 0.627 0.530 -0.000 0.040  0.040  54  SER FFF CB  
7079  O OG  . SER F 54  ? 0.577 0.631 0.513 0.010  0.046  0.027  54  SER FFF OG  
7080  N N   . SER F 55  ? 0.564 0.618 0.561 0.002  0.037  0.016  55  SER FFF N   
7081  C CA  . SER F 55  ? 0.573 0.648 0.587 0.006  0.044  0.012  55  SER FFF CA  
7082  C C   . SER F 55  ? 0.614 0.704 0.614 0.018  0.056  0.007  55  SER FFF C   
7083  O O   . SER F 55  ? 0.622 0.728 0.636 0.024  0.063  0.003  55  SER FFF O   
7084  C CB  . SER F 55  ? 0.549 0.642 0.587 -0.005 0.048  0.023  55  SER FFF CB  
7085  O OG  . SER F 55  ? 0.537 0.615 0.586 -0.015 0.036  0.024  55  SER FFF OG  
7086  N N   . THR F 56  ? 0.692 0.776 0.665 0.022  0.058  0.007  56  THR FFF N   
7087  C CA  . THR F 56  ? 0.796 0.900 0.753 0.029  0.073  0.008  56  THR FFF CA  
7088  C C   . THR F 56  ? 0.806 0.906 0.748 0.044  0.076  -0.011 56  THR FFF C   
7089  O O   . THR F 56  ? 0.883 1.003 0.821 0.054  0.090  -0.013 56  THR FFF O   
7090  C CB  . THR F 56  ? 0.925 1.029 0.858 0.025  0.077  0.020  56  THR FFF CB  
7091  O OG1 . THR F 56  ? 1.041 1.160 0.992 0.013  0.084  0.039  56  THR FFF OG1 
7092  C CG2 . THR F 56  ? 0.959 1.075 0.862 0.037  0.088  0.013  56  THR FFF CG2 
7093  N N   . PRO F 57  ? 0.670 0.746 0.601 0.047  0.063  -0.024 57  PRO FFF N   
7094  C CA  . PRO F 57  ? 0.627 0.695 0.556 0.059  0.063  -0.042 57  PRO FFF CA  
7095  C C   . PRO F 57  ? 0.584 0.648 0.543 0.057  0.058  -0.042 57  PRO FFF C   
7096  O O   . PRO F 57  ? 0.548 0.600 0.516 0.048  0.047  -0.037 57  PRO FFF O   
7097  C CB  . PRO F 57  ? 0.628 0.674 0.531 0.060  0.052  -0.054 57  PRO FFF CB  
7098  C CG  . PRO F 57  ? 0.629 0.673 0.524 0.049  0.045  -0.041 57  PRO FFF CG  
7099  C CD  . PRO F 57  ? 0.605 0.662 0.522 0.041  0.050  -0.023 57  PRO FFF CD  
7100  N N   . THR F 58  ? 0.562 0.639 0.537 0.067  0.067  -0.044 58  THR FFF N   
7101  C CA  . THR F 58  ? 0.550 0.621 0.549 0.070  0.061  -0.047 58  THR FFF CA  
7102  C C   . THR F 58  ? 0.563 0.617 0.553 0.084  0.062  -0.063 58  THR FFF C   
7103  O O   . THR F 58  ? 0.606 0.661 0.577 0.093  0.071  -0.073 58  THR FFF O   
7104  C CB  . THR F 58  ? 0.521 0.619 0.548 0.070  0.067  -0.037 58  THR FFF CB  
7105  O OG1 . THR F 58  ? 0.523 0.645 0.552 0.082  0.082  -0.038 58  THR FFF OG1 
7106  C CG2 . THR F 58  ? 0.498 0.606 0.537 0.054  0.063  -0.022 58  THR FFF CG2 
7107  N N   . TYR F 59  ? 0.565 0.601 0.566 0.085  0.053  -0.067 59  TYR FFF N   
7108  C CA  . TYR F 59  ? 0.595 0.607 0.591 0.096  0.052  -0.081 59  TYR FFF CA  
7109  C C   . TYR F 59  ? 0.567 0.578 0.588 0.103  0.050  -0.075 59  TYR FFF C   
7110  O O   . TYR F 59  ? 0.563 0.583 0.600 0.094  0.044  -0.063 59  TYR FFF O   
7111  C CB  . TYR F 59  ? 0.620 0.603 0.602 0.088  0.040  -0.088 59  TYR FFF CB  
7112  C CG  . TYR F 59  ? 0.637 0.620 0.595 0.080  0.037  -0.092 59  TYR FFF CG  
7113  C CD1 . TYR F 59  ? 0.625 0.614 0.583 0.067  0.031  -0.081 59  TYR FFF CD1 
7114  C CD2 . TYR F 59  ? 0.683 0.655 0.616 0.087  0.038  -0.108 59  TYR FFF CD2 
7115  C CE1 . TYR F 59  ? 0.638 0.626 0.575 0.062  0.026  -0.083 59  TYR FFF CE1 
7116  C CE2 . TYR F 59  ? 0.693 0.665 0.602 0.080  0.033  -0.111 59  TYR FFF CE2 
7117  C CZ  . TYR F 59  ? 0.665 0.646 0.577 0.068  0.027  -0.097 59  TYR FFF CZ  
7118  O OH  . TYR F 59  ? 0.650 0.633 0.540 0.063  0.021  -0.097 59  TYR FFF OH  
7119  N N   . TYR F 60  ? 0.582 0.583 0.606 0.118  0.055  -0.085 60  TYR FFF N   
7120  C CA  . TYR F 60  ? 0.574 0.574 0.621 0.129  0.054  -0.079 60  TYR FFF CA  
7121  C C   . TYR F 60  ? 0.608 0.570 0.649 0.139  0.051  -0.092 60  TYR FFF C   
7122  O O   . TYR F 60  ? 0.633 0.579 0.655 0.145  0.055  -0.108 60  TYR FFF O   
7123  C CB  . TYR F 60  ? 0.570 0.605 0.634 0.142  0.066  -0.075 60  TYR FFF CB  
7124  C CG  . TYR F 60  ? 0.542 0.612 0.617 0.130  0.068  -0.061 60  TYR FFF CG  
7125  C CD1 . TYR F 60  ? 0.527 0.607 0.620 0.120  0.058  -0.047 60  TYR FFF CD1 
7126  C CD2 . TYR F 60  ? 0.531 0.623 0.597 0.126  0.078  -0.061 60  TYR FFF CD2 
7127  C CE1 . TYR F 60  ? 0.510 0.618 0.613 0.107  0.057  -0.036 60  TYR FFF CE1 
7128  C CE2 . TYR F 60  ? 0.500 0.620 0.578 0.113  0.078  -0.047 60  TYR FFF CE2 
7129  C CZ  . TYR F 60  ? 0.501 0.628 0.598 0.103  0.068  -0.036 60  TYR FFF CZ  
7130  O OH  . TYR F 60  ? 0.463 0.613 0.572 0.088  0.066  -0.024 60  TYR FFF OH  
7131  N N   . GLY F 61  ? 0.631 0.578 0.688 0.139  0.044  -0.084 61  GLY FFF N   
7132  C CA  . GLY F 61  ? 0.665 0.577 0.724 0.151  0.042  -0.091 61  GLY FFF CA  
7133  C C   . GLY F 61  ? 0.710 0.628 0.776 0.175  0.053  -0.098 61  GLY FFF C   
7134  O O   . GLY F 61  ? 0.711 0.666 0.792 0.181  0.060  -0.089 61  GLY FFF O   
7135  N N   . GLU F 62  ? 0.810 0.693 0.868 0.187  0.055  -0.113 62  GLU FFF N   
7136  C CA  . GLU F 62  ? 0.864 0.746 0.927 0.213  0.066  -0.124 62  GLU FFF CA  
7137  C C   . GLU F 62  ? 0.838 0.748 0.932 0.227  0.069  -0.106 62  GLU FFF C   
7138  O O   . GLU F 62  ? 0.820 0.764 0.924 0.243  0.081  -0.106 62  GLU FFF O   
7139  C CB  . GLU F 62  ? 0.968 0.795 1.021 0.221  0.062  -0.141 62  GLU FFF CB  
7140  C CG  . GLU F 62  ? 1.088 0.903 1.143 0.251  0.073  -0.155 62  GLU FFF CG  
7141  C CD  . GLU F 62  ? 1.161 1.001 1.197 0.261  0.087  -0.172 62  GLU FFF CD  
7142  O OE1 . GLU F 62  ? 1.194 1.051 1.209 0.245  0.087  -0.176 62  GLU FFF OE1 
7143  O OE2 . GLU F 62  ? 1.196 1.034 1.236 0.288  0.099  -0.183 62  GLU FFF OE2 
7144  N N   . SER F 63  ? 0.821 0.718 0.929 0.222  0.058  -0.090 63  SER FFF N   
7145  C CA  . SER F 63  ? 0.797 0.709 0.933 0.238  0.057  -0.073 63  SER FFF CA  
7146  C C   . SER F 63  ? 0.723 0.691 0.875 0.231  0.057  -0.057 63  SER FFF C   
7147  O O   . SER F 63  ? 0.710 0.701 0.887 0.245  0.057  -0.044 63  SER FFF O   
7148  C CB  . SER F 63  ? 0.808 0.685 0.949 0.234  0.046  -0.061 63  SER FFF CB  
7149  O OG  . SER F 63  ? 0.817 0.696 0.949 0.209  0.036  -0.051 63  SER FFF OG  
7150  N N   . VAL F 64  ? 0.695 0.683 0.837 0.210  0.056  -0.057 64  VAL FFF N   
7151  C CA  . VAL F 64  ? 0.656 0.693 0.813 0.201  0.055  -0.043 64  VAL FFF CA  
7152  C C   . VAL F 64  ? 0.657 0.725 0.812 0.201  0.068  -0.050 64  VAL FFF C   
7153  O O   . VAL F 64  ? 0.646 0.756 0.819 0.195  0.069  -0.039 64  VAL FFF O   
7154  C CB  . VAL F 64  ? 0.640 0.675 0.789 0.177  0.043  -0.033 64  VAL FFF CB  
7155  C CG1 . VAL F 64  ? 0.657 0.664 0.807 0.177  0.032  -0.024 64  VAL FFF CG1 
7156  C CG2 . VAL F 64  ? 0.650 0.669 0.773 0.160  0.044  -0.044 64  VAL FFF CG2 
7157  N N   . LYS F 65  ? 0.717 0.767 0.850 0.206  0.077  -0.068 65  LYS FFF N   
7158  C CA  . LYS F 65  ? 0.752 0.831 0.876 0.206  0.091  -0.074 65  LYS FFF CA  
7159  C C   . LYS F 65  ? 0.710 0.836 0.866 0.221  0.102  -0.065 65  LYS FFF C   
7160  O O   . LYS F 65  ? 0.715 0.837 0.887 0.243  0.105  -0.066 65  LYS FFF O   
7161  C CB  . LYS F 65  ? 0.860 0.910 0.955 0.215  0.100  -0.096 65  LYS FFF CB  
7162  C CG  . LYS F 65  ? 0.930 0.992 0.999 0.203  0.106  -0.101 65  LYS FFF CG  
7163  C CD  . LYS F 65  ? 1.021 1.072 1.063 0.218  0.119  -0.122 65  LYS FFF CD  
7164  C CE  . LYS F 65  ? 1.049 1.141 1.082 0.219  0.135  -0.120 65  LYS FFF CE  
7165  N NZ  . LYS F 65  ? 1.065 1.170 1.097 0.247  0.154  -0.132 65  LYS FFF NZ  
7166  N N   . GLY F 66  ? 0.664 0.833 0.831 0.209  0.107  -0.054 66  GLY FFF N   
7167  C CA  . GLY F 66  ? 0.639 0.861 0.840 0.219  0.117  -0.043 66  GLY FFF CA  
7168  C C   . GLY F 66  ? 0.616 0.863 0.849 0.211  0.102  -0.025 66  GLY FFF C   
7169  O O   . GLY F 66  ? 0.630 0.926 0.892 0.206  0.107  -0.014 66  GLY FFF O   
7170  N N   . ARG F 67  ? 0.584 0.800 0.814 0.208  0.086  -0.023 67  ARG FFF N   
7171  C CA  . ARG F 67  ? 0.575 0.812 0.831 0.203  0.071  -0.007 67  ARG FFF CA  
7172  C C   . ARG F 67  ? 0.538 0.772 0.783 0.174  0.058  -0.001 67  ARG FFF C   
7173  O O   . ARG F 67  ? 0.515 0.779 0.780 0.164  0.048  0.011  67  ARG FFF O   
7174  C CB  . ARG F 67  ? 0.584 0.793 0.842 0.219  0.062  -0.004 67  ARG FFF CB  
7175  C CG  . ARG F 67  ? 0.588 0.801 0.863 0.251  0.074  -0.009 67  ARG FFF CG  
7176  C CD  . ARG F 67  ? 0.594 0.778 0.875 0.268  0.064  -0.003 67  ARG FFF CD  
7177  N NE  . ARG F 67  ? 0.594 0.721 0.844 0.258  0.057  -0.009 67  ARG FFF NE  
7178  C CZ  . ARG F 67  ? 0.592 0.703 0.836 0.247  0.042  0.003  67  ARG FFF CZ  
7179  N NH1 . ARG F 67  ? 0.593 0.737 0.857 0.244  0.030  0.019  67  ARG FFF NH1 
7180  N NH2 . ARG F 67  ? 0.617 0.679 0.836 0.238  0.037  -0.002 67  ARG FFF NH2 
7181  N N   . PHE F 68  ? 0.541 0.737 0.753 0.162  0.057  -0.010 68  PHE FFF N   
7182  C CA  . PHE F 68  ? 0.520 0.703 0.717 0.138  0.045  -0.006 68  PHE FFF CA  
7183  C C   . PHE F 68  ? 0.535 0.724 0.719 0.123  0.052  -0.010 68  PHE FFF C   
7184  O O   . PHE F 68  ? 0.578 0.759 0.748 0.130  0.064  -0.019 68  PHE FFF O   
7185  C CB  . PHE F 68  ? 0.526 0.663 0.700 0.137  0.037  -0.011 68  PHE FFF CB  
7186  C CG  . PHE F 68  ? 0.508 0.635 0.690 0.147  0.027  -0.003 68  PHE FFF CG  
7187  C CD1 . PHE F 68  ? 0.525 0.680 0.734 0.162  0.026  0.006  68  PHE FFF CD1 
7188  C CD2 . PHE F 68  ? 0.510 0.602 0.675 0.142  0.020  -0.003 68  PHE FFF CD2 
7189  C CE1 . PHE F 68  ? 0.540 0.684 0.755 0.173  0.017  0.015  68  PHE FFF CE1 
7190  C CE2 . PHE F 68  ? 0.531 0.611 0.701 0.151  0.012  0.006  68  PHE FFF CE2 
7191  C CZ  . PHE F 68  ? 0.542 0.648 0.736 0.167  0.010  0.016  68  PHE FFF CZ  
7192  N N   . THR F 69  ? 0.523 0.724 0.711 0.103  0.044  -0.003 69  THR FFF N   
7193  C CA  . THR F 69  ? 0.497 0.699 0.672 0.087  0.049  -0.003 69  THR FFF CA  
7194  C C   . THR F 69  ? 0.503 0.678 0.661 0.070  0.036  -0.004 69  THR FFF C   
7195  O O   . THR F 69  ? 0.473 0.655 0.642 0.063  0.024  0.001  69  THR FFF O   
7196  C CB  . THR F 69  ? 0.503 0.748 0.705 0.078  0.054  0.007  69  THR FFF CB  
7197  O OG1 . THR F 69  ? 0.520 0.793 0.740 0.097  0.067  0.007  69  THR FFF OG1 
7198  C CG2 . THR F 69  ? 0.518 0.762 0.708 0.062  0.059  0.009  69  THR FFF CG2 
7199  N N   . ILE F 70  ? 0.484 0.632 0.617 0.066  0.038  -0.010 70  ILE FFF N   
7200  C CA  . ILE F 70  ? 0.467 0.593 0.584 0.052  0.028  -0.011 70  ILE FFF CA  
7201  C C   . ILE F 70  ? 0.469 0.605 0.586 0.037  0.031  -0.005 70  ILE FFF C   
7202  O O   . ILE F 70  ? 0.480 0.629 0.596 0.040  0.043  -0.004 70  ILE FFF O   
7203  C CB  . ILE F 70  ? 0.482 0.574 0.574 0.056  0.028  -0.020 70  ILE FFF CB  
7204  C CG1 . ILE F 70  ? 0.476 0.550 0.558 0.045  0.017  -0.019 70  ILE FFF CG1 
7205  C CG2 . ILE F 70  ? 0.502 0.590 0.578 0.059  0.038  -0.025 70  ILE FFF CG2 
7206  C CD1 . ILE F 70  ? 0.493 0.539 0.558 0.048  0.015  -0.026 70  ILE FFF CD1 
7207  N N   . SER F 71  ? 0.442 0.571 0.559 0.024  0.021  -0.003 71  SER FFF N   
7208  C CA  . SER F 71  ? 0.456 0.587 0.574 0.008  0.021  0.003  71  SER FFF CA  
7209  C C   . SER F 71  ? 0.490 0.594 0.595 -0.000 0.010  0.000  71  SER FFF C   
7210  O O   . SER F 71  ? 0.488 0.582 0.588 0.004  0.002  -0.005 71  SER FFF O   
7211  C CB  . SER F 71  ? 0.449 0.612 0.594 0.000  0.022  0.012  71  SER FFF CB  
7212  O OG  . SER F 71  ? 0.445 0.614 0.604 -0.003 0.009  0.011  71  SER FFF OG  
7213  N N   . ARG F 72  ? 0.490 0.583 0.589 -0.011 0.009  0.004  72  ARG FFF N   
7214  C CA  . ARG F 72  ? 0.509 0.575 0.595 -0.017 -0.001 -0.000 72  ARG FFF CA  
7215  C C   . ARG F 72  ? 0.513 0.577 0.609 -0.033 -0.005 0.006  72  ARG FFF C   
7216  O O   . ARG F 72  ? 0.479 0.558 0.585 -0.040 0.003  0.015  72  ARG FFF O   
7217  C CB  . ARG F 72  ? 0.529 0.574 0.594 -0.011 0.002  -0.003 72  ARG FFF CB  
7218  C CG  . ARG F 72  ? 0.550 0.595 0.608 -0.014 0.010  0.004  72  ARG FFF CG  
7219  C CD  . ARG F 72  ? 0.579 0.607 0.616 -0.006 0.010  0.001  72  ARG FFF CD  
7220  N NE  . ARG F 72  ? 0.569 0.576 0.599 -0.007 0.002  -0.003 72  ARG FFF NE  
7221  C CZ  . ARG F 72  ? 0.539 0.535 0.559 -0.000 -0.001 -0.009 72  ARG FFF CZ  
7222  N NH1 . ARG F 72  ? 0.535 0.535 0.548 0.007  0.002  -0.013 72  ARG FFF NH1 
7223  N NH2 . ARG F 72  ? 0.568 0.548 0.585 -0.001 -0.008 -0.011 72  ARG FFF NH2 
7224  N N   . ASP F 73  ? 0.535 0.583 0.628 -0.039 -0.016 0.000  73  ASP FFF N   
7225  C CA  . ASP F 73  ? 0.566 0.601 0.665 -0.054 -0.022 0.003  73  ASP FFF CA  
7226  C C   . ASP F 73  ? 0.568 0.569 0.647 -0.051 -0.027 -0.004 73  ASP FFF C   
7227  O O   . ASP F 73  ? 0.570 0.561 0.641 -0.047 -0.034 -0.015 73  ASP FFF O   
7228  C CB  . ASP F 73  ? 0.568 0.618 0.685 -0.065 -0.032 -0.001 73  ASP FFF CB  
7229  C CG  . ASP F 73  ? 0.602 0.637 0.728 -0.083 -0.040 0.001  73  ASP FFF CG  
7230  O OD1 . ASP F 73  ? 0.627 0.634 0.742 -0.085 -0.038 0.004  73  ASP FFF OD1 
7231  O OD2 . ASP F 73  ? 0.583 0.634 0.728 -0.095 -0.049 0.000  73  ASP FFF OD2 
7232  N N   . ASN F 74  ? 0.557 0.543 0.627 -0.050 -0.021 0.003  74  ASN FFF N   
7233  C CA  . ASN F 74  ? 0.574 0.531 0.628 -0.044 -0.024 -0.002 74  ASN FFF CA  
7234  C C   . ASN F 74  ? 0.611 0.544 0.666 -0.052 -0.035 -0.009 74  ASN FFF C   
7235  O O   . ASN F 74  ? 0.636 0.552 0.679 -0.044 -0.039 -0.019 74  ASN FFF O   
7236  C CB  . ASN F 74  ? 0.578 0.527 0.624 -0.043 -0.018 0.010  74  ASN FFF CB  
7237  C CG  . ASN F 74  ? 0.572 0.537 0.609 -0.031 -0.011 0.010  74  ASN FFF CG  
7238  O OD1 . ASN F 74  ? 0.538 0.517 0.576 -0.025 -0.010 0.003  74  ASN FFF OD1 
7239  N ND2 . ASN F 74  ? 0.587 0.546 0.613 -0.028 -0.007 0.019  74  ASN FFF ND2 
7240  N N   . ALA F 75  ? 0.602 0.536 0.672 -0.068 -0.039 -0.005 75  ALA FFF N   
7241  C CA  . ALA F 75  ? 0.619 0.527 0.690 -0.078 -0.050 -0.014 75  ALA FFF CA  
7242  C C   . ALA F 75  ? 0.610 0.522 0.673 -0.072 -0.059 -0.031 75  ALA FFF C   
7243  O O   . ALA F 75  ? 0.628 0.513 0.681 -0.073 -0.067 -0.043 75  ALA FFF O   
7244  C CB  . ALA F 75  ? 0.613 0.526 0.706 -0.099 -0.054 -0.005 75  ALA FFF CB  
7245  N N   . LYS F 76  ? 0.590 0.532 0.655 -0.065 -0.056 -0.031 76  LYS FFF N   
7246  C CA  . LYS F 76  ? 0.577 0.526 0.633 -0.060 -0.063 -0.044 76  LYS FFF CA  
7247  C C   . LYS F 76  ? 0.555 0.507 0.596 -0.042 -0.056 -0.046 76  LYS FFF C   
7248  O O   . LYS F 76  ? 0.537 0.500 0.570 -0.036 -0.060 -0.052 76  LYS FFF O   
7249  C CB  . LYS F 76  ? 0.576 0.558 0.650 -0.066 -0.067 -0.040 76  LYS FFF CB  
7250  C CG  . LYS F 76  ? 0.625 0.612 0.721 -0.086 -0.075 -0.037 76  LYS FFF CG  
7251  C CD  . LYS F 76  ? 0.608 0.629 0.721 -0.092 -0.083 -0.036 76  LYS FFF CD  
7252  C CE  . LYS F 76  ? 0.651 0.677 0.787 -0.114 -0.094 -0.036 76  LYS FFF CE  
7253  N NZ  . LYS F 76  ? 0.728 0.794 0.884 -0.118 -0.102 -0.034 76  LYS FFF NZ  
7254  N N   . ASN F 77  ? 0.539 0.485 0.576 -0.034 -0.047 -0.039 77  ASN FFF N   
7255  C CA  . ASN F 77  ? 0.530 0.479 0.556 -0.020 -0.041 -0.041 77  ASN FFF CA  
7256  C C   . ASN F 77  ? 0.513 0.488 0.545 -0.017 -0.039 -0.038 77  ASN FFF C   
7257  O O   . ASN F 77  ? 0.547 0.524 0.569 -0.008 -0.038 -0.041 77  ASN FFF O   
7258  C CB  . ASN F 77  ? 0.542 0.475 0.553 -0.012 -0.044 -0.051 77  ASN FFF CB  
7259  C CG  . ASN F 77  ? 0.566 0.477 0.571 -0.007 -0.041 -0.052 77  ASN FFF CG  
7260  O OD1 . ASN F 77  ? 0.546 0.444 0.557 -0.014 -0.042 -0.046 77  ASN FFF OD1 
7261  N ND2 . ASN F 77  ? 0.598 0.507 0.594 0.005  -0.037 -0.056 77  ASN FFF ND2 
7262  N N   . THR F 78  ? 0.461 0.454 0.508 -0.023 -0.039 -0.032 78  THR FFF N   
7263  C CA  . THR F 78  ? 0.455 0.472 0.510 -0.018 -0.039 -0.029 78  THR FFF CA  
7264  C C   . THR F 78  ? 0.453 0.484 0.517 -0.014 -0.029 -0.022 78  THR FFF C   
7265  O O   . THR F 78  ? 0.440 0.474 0.512 -0.020 -0.025 -0.016 78  THR FFF O   
7266  C CB  . THR F 78  ? 0.474 0.504 0.538 -0.027 -0.049 -0.031 78  THR FFF CB  
7267  O OG1 . THR F 78  ? 0.486 0.500 0.534 -0.028 -0.058 -0.042 78  THR FFF OG1 
7268  C CG2 . THR F 78  ? 0.470 0.526 0.544 -0.021 -0.051 -0.027 78  THR FFF CG2 
7269  N N   . VAL F 79  ? 0.461 0.498 0.523 -0.004 -0.026 -0.021 79  VAL FFF N   
7270  C CA  . VAL F 79  ? 0.451 0.503 0.523 0.003  -0.018 -0.017 79  VAL FFF CA  
7271  C C   . VAL F 79  ? 0.461 0.533 0.546 0.007  -0.022 -0.014 79  VAL FFF C   
7272  O O   . VAL F 79  ? 0.467 0.538 0.547 0.009  -0.029 -0.015 79  VAL FFF O   
7273  C CB  . VAL F 79  ? 0.436 0.474 0.496 0.012  -0.012 -0.019 79  VAL FFF CB  
7274  C CG1 . VAL F 79  ? 0.439 0.469 0.492 0.018  -0.016 -0.020 79  VAL FFF CG1 
7275  C CG2 . VAL F 79  ? 0.435 0.481 0.501 0.019  -0.004 -0.018 79  VAL FFF CG2 
7276  N N   . TYR F 80  ? 0.488 0.582 0.590 0.009  -0.017 -0.009 80  TYR FFF N   
7277  C CA  . TYR F 80  ? 0.484 0.603 0.605 0.014  -0.020 -0.005 80  TYR FFF CA  
7278  C C   . TYR F 80  ? 0.470 0.593 0.596 0.030  -0.011 -0.003 80  TYR FFF C   
7279  O O   . TYR F 80  ? 0.459 0.575 0.579 0.033  -0.001 -0.006 80  TYR FFF O   
7280  C CB  . TYR F 80  ? 0.465 0.610 0.608 0.004  -0.022 -0.000 80  TYR FFF CB  
7281  C CG  . TYR F 80  ? 0.453 0.591 0.594 -0.013 -0.033 -0.003 80  TYR FFF CG  
7282  C CD1 . TYR F 80  ? 0.479 0.621 0.618 -0.015 -0.047 -0.006 80  TYR FFF CD1 
7283  C CD2 . TYR F 80  ? 0.458 0.583 0.595 -0.024 -0.030 -0.003 80  TYR FFF CD2 
7284  C CE1 . TYR F 80  ? 0.475 0.607 0.610 -0.030 -0.058 -0.012 80  TYR FFF CE1 
7285  C CE2 . TYR F 80  ? 0.471 0.584 0.606 -0.039 -0.041 -0.007 80  TYR FFF CE2 
7286  C CZ  . TYR F 80  ? 0.472 0.588 0.605 -0.042 -0.055 -0.013 80  TYR FFF CZ  
7287  O OH  . TYR F 80  ? 0.502 0.603 0.632 -0.055 -0.066 -0.020 80  TYR FFF OH  
7288  N N   . LEU F 81  ? 0.487 0.621 0.622 0.040  -0.015 0.000  81  LEU FFF N   
7289  C CA  . LEU F 81  ? 0.508 0.647 0.652 0.057  -0.007 0.002  81  LEU FFF CA  
7290  C C   . LEU F 81  ? 0.499 0.674 0.670 0.062  -0.011 0.009  81  LEU FFF C   
7291  O O   . LEU F 81  ? 0.489 0.669 0.663 0.064  -0.022 0.014  81  LEU FFF O   
7292  C CB  . LEU F 81  ? 0.510 0.623 0.640 0.066  -0.008 0.001  81  LEU FFF CB  
7293  C CG  . LEU F 81  ? 0.513 0.620 0.649 0.083  0.001  -0.000 81  LEU FFF CG  
7294  C CD1 . LEU F 81  ? 0.525 0.621 0.651 0.083  0.012  -0.009 81  LEU FFF CD1 
7295  C CD2 . LEU F 81  ? 0.546 0.626 0.672 0.090  -0.003 0.002  81  LEU FFF CD2 
7296  N N   . GLN F 82  ? 0.488 0.689 0.679 0.063  -0.003 0.011  82  GLN FFF N   
7297  C CA  . GLN F 82  ? 0.497 0.738 0.720 0.071  -0.004 0.019  82  GLN FFF CA  
7298  C C   . GLN F 82  ? 0.522 0.757 0.748 0.095  0.003  0.019  82  GLN FFF C   
7299  O O   . GLN F 82  ? 0.549 0.768 0.765 0.103  0.016  0.012  82  GLN FFF O   
7300  C CB  . GLN F 82  ? 0.479 0.750 0.722 0.062  0.006  0.022  82  GLN FFF CB  
7301  C CG  . GLN F 82  ? 0.496 0.816 0.778 0.066  0.003  0.031  82  GLN FFF CG  
7302  C CD  . GLN F 82  ? 0.528 0.861 0.819 0.058  -0.017 0.035  82  GLN FFF CD  
7303  O OE1 . GLN F 82  ? 0.550 0.869 0.828 0.039  -0.028 0.032  82  GLN FFF OE1 
7304  N NE2 . GLN F 82  ? 0.539 0.896 0.851 0.073  -0.024 0.041  82  GLN FFF NE2 
7305  N N   . MET F 83  ? 0.542 0.783 0.777 0.105  -0.007 0.026  83  MET FFF N   
7306  C CA  . MET F 83  ? 0.572 0.803 0.812 0.128  -0.003 0.028  83  MET FFF CA  
7307  C C   . MET F 83  ? 0.552 0.828 0.828 0.141  -0.004 0.037  83  MET FFF C   
7308  O O   . MET F 83  ? 0.552 0.851 0.841 0.137  -0.019 0.045  83  MET FFF O   
7309  C CB  . MET F 83  ? 0.622 0.822 0.843 0.132  -0.013 0.032  83  MET FFF CB  
7310  C CG  . MET F 83  ? 0.641 0.805 0.831 0.118  -0.013 0.024  83  MET FFF CG  
7311  S SD  . MET F 83  ? 0.707 0.839 0.878 0.121  -0.022 0.032  83  MET FFF SD  
7312  C CE  . MET F 83  ? 0.701 0.864 0.876 0.114  -0.039 0.042  83  MET FFF CE  
7313  N N   . ASN F 84  ? 0.551 0.843 0.844 0.156  0.011  0.034  84  ASN FFF N   
7314  C CA  . ASN F 84  ? 0.537 0.876 0.869 0.172  0.013  0.043  84  ASN FFF CA  
7315  C C   . ASN F 84  ? 0.552 0.875 0.888 0.202  0.018  0.043  84  ASN FFF C   
7316  O O   . ASN F 84  ? 0.546 0.822 0.856 0.208  0.024  0.034  84  ASN FFF O   
7317  C CB  . ASN F 84  ? 0.536 0.911 0.887 0.168  0.028  0.040  84  ASN FFF CB  
7318  C CG  . ASN F 84  ? 0.531 0.922 0.882 0.138  0.022  0.043  84  ASN FFF CG  
7319  O OD1 . ASN F 84  ? 0.529 0.926 0.884 0.124  0.004  0.048  84  ASN FFF OD1 
7320  N ND2 . ASN F 84  ? 0.548 0.942 0.894 0.128  0.037  0.038  84  ASN FFF ND2 
7321  N N   . ARG F 85  ? 0.569 0.930 0.940 0.219  0.013  0.054  85  ARG FFF N   
7322  C CA  . ARG F 85  ? 0.616 0.968 1.000 0.251  0.019  0.056  85  ARG FFF CA  
7323  C C   . ARG F 85  ? 0.614 0.904 0.965 0.254  0.012  0.055  85  ARG FFF C   
7324  O O   . ARG F 85  ? 0.628 0.880 0.966 0.268  0.024  0.045  85  ARG FFF O   
7325  C CB  . ARG F 85  ? 0.652 1.011 1.043 0.266  0.042  0.045  85  ARG FFF CB  
7326  C CG  . ARG F 85  ? 0.688 1.112 1.115 0.264  0.050  0.050  85  ARG FFF CG  
7327  C CD  . ARG F 85  ? 0.749 1.186 1.185 0.285  0.075  0.040  85  ARG FFF CD  
7328  N NE  . ARG F 85  ? 0.780 1.177 1.176 0.276  0.088  0.023  85  ARG FFF NE  
7329  C CZ  . ARG F 85  ? 0.780 1.182 1.161 0.250  0.091  0.021  85  ARG FFF CZ  
7330  N NH1 . ARG F 85  ? 0.758 1.198 1.159 0.226  0.081  0.033  85  ARG FFF NH1 
7331  N NH2 . ARG F 85  ? 0.804 1.171 1.149 0.246  0.102  0.006  85  ARG FFF NH2 
7332  N N   . LEU F 86  ? 0.593 0.877 0.932 0.240  -0.006 0.065  86  LEU FFF N   
7333  C CA  . LEU F 86  ? 0.622 0.854 0.932 0.239  -0.012 0.067  86  LEU FFF CA  
7334  C C   . LEU F 86  ? 0.676 0.891 0.997 0.267  -0.013 0.077  86  LEU FFF C   
7335  O O   . LEU F 86  ? 0.679 0.933 1.031 0.284  -0.019 0.089  86  LEU FFF O   
7336  C CB  . LEU F 86  ? 0.605 0.844 0.900 0.218  -0.030 0.076  86  LEU FFF CB  
7337  C CG  . LEU F 86  ? 0.586 0.819 0.859 0.191  -0.028 0.065  86  LEU FFF CG  
7338  C CD1 . LEU F 86  ? 0.585 0.836 0.851 0.173  -0.046 0.072  86  LEU FFF CD1 
7339  C CD2 . LEU F 86  ? 0.599 0.780 0.842 0.185  -0.020 0.055  86  LEU FFF CD2 
7340  N N   . LYS F 87  ? 0.721 0.880 1.020 0.272  -0.008 0.073  87  LYS FFF N   
7341  C CA  . LYS F 87  ? 0.755 0.883 1.061 0.298  -0.009 0.081  87  LYS FFF CA  
7342  C C   . LYS F 87  ? 0.757 0.849 1.040 0.288  -0.020 0.094  87  LYS FFF C   
7343  O O   . LYS F 87  ? 0.744 0.825 1.003 0.263  -0.022 0.090  87  LYS FFF O   
7344  C CB  . LYS F 87  ? 0.800 0.891 1.102 0.312  0.008  0.063  87  LYS FFF CB  
7345  C CG  . LYS F 87  ? 0.805 0.929 1.118 0.314  0.023  0.046  87  LYS FFF CG  
7346  C CD  . LYS F 87  ? 0.854 0.950 1.167 0.338  0.039  0.028  87  LYS FFF CD  
7347  C CE  . LYS F 87  ? 0.857 0.925 1.141 0.324  0.050  0.005  87  LYS FFF CE  
7348  N NZ  . LYS F 87  ? 0.891 0.974 1.181 0.343  0.069  -0.012 87  LYS FFF NZ  
7349  N N   . PRO F 88  ? 0.761 0.835 1.051 0.306  -0.027 0.112  88  PRO FFF N   
7350  C CA  . PRO F 88  ? 0.768 0.805 1.034 0.297  -0.036 0.127  88  PRO FFF CA  
7351  C C   . PRO F 88  ? 0.766 0.753 1.007 0.279  -0.027 0.114  88  PRO FFF C   
7352  O O   . PRO F 88  ? 0.770 0.749 0.990 0.260  -0.033 0.122  88  PRO FFF O   
7353  C CB  . PRO F 88  ? 0.811 0.830 1.094 0.326  -0.039 0.145  88  PRO FFF CB  
7354  C CG  . PRO F 88  ? 0.788 0.864 1.104 0.344  -0.043 0.148  88  PRO FFF CG  
7355  C CD  . PRO F 88  ? 0.759 0.854 1.081 0.337  -0.028 0.123  88  PRO FFF CD  
7356  N N   . GLU F 89  ? 0.794 0.754 1.036 0.285  -0.015 0.094  89  GLU FFF N   
7357  C CA  . GLU F 89  ? 0.822 0.735 1.042 0.268  -0.008 0.079  89  GLU FFF CA  
7358  C C   . GLU F 89  ? 0.755 0.689 0.957 0.240  -0.008 0.069  89  GLU FFF C   
7359  O O   . GLU F 89  ? 0.755 0.658 0.940 0.225  -0.005 0.059  89  GLU FFF O   
7360  C CB  . GLU F 89  ? 0.883 0.769 1.105 0.280  0.004  0.056  89  GLU FFF CB  
7361  C CG  . GLU F 89  ? 1.015 0.882 1.257 0.312  0.006  0.059  89  GLU FFF CG  
7362  C CD  . GLU F 89  ? 1.047 0.966 1.315 0.333  0.011  0.058  89  GLU FFF CD  
7363  O OE1 . GLU F 89  ? 1.082 1.035 1.350 0.327  0.019  0.043  89  GLU FFF OE1 
7364  O OE2 . GLU F 89  ? 1.050 0.978 1.339 0.357  0.006  0.075  89  GLU FFF OE2 
7365  N N   . ASP F 90  ? 0.720 0.705 0.929 0.235  -0.012 0.071  90  ASP FFF N   
7366  C CA  . ASP F 90  ? 0.690 0.694 0.884 0.210  -0.012 0.062  90  ASP FFF CA  
7367  C C   . ASP F 90  ? 0.673 0.679 0.852 0.196  -0.023 0.078  90  ASP FFF C   
7368  O O   . ASP F 90  ? 0.677 0.690 0.839 0.176  -0.023 0.071  90  ASP FFF O   
7369  C CB  . ASP F 90  ? 0.670 0.723 0.878 0.209  -0.011 0.057  90  ASP FFF CB  
7370  C CG  . ASP F 90  ? 0.683 0.741 0.902 0.221  0.002  0.041  90  ASP FFF CG  
7371  O OD1 . ASP F 90  ? 0.664 0.689 0.868 0.217  0.011  0.026  90  ASP FFF OD1 
7372  O OD2 . ASP F 90  ? 0.694 0.789 0.937 0.234  0.004  0.043  90  ASP FFF OD2 
7373  N N   . THR F 91  ? 0.645 0.646 0.827 0.207  -0.030 0.098  91  THR FFF N   
7374  C CA  . THR F 91  ? 0.643 0.644 0.806 0.195  -0.039 0.114  91  THR FFF CA  
7375  C C   . THR F 91  ? 0.635 0.601 0.778 0.178  -0.033 0.109  91  THR FFF C   
7376  O O   . THR F 91  ? 0.656 0.583 0.802 0.182  -0.027 0.107  91  THR FFF O   
7377  C CB  . THR F 91  ? 0.669 0.665 0.837 0.213  -0.047 0.138  91  THR FFF CB  
7378  O OG1 . THR F 91  ? 0.692 0.731 0.881 0.226  -0.055 0.142  91  THR FFF OG1 
7379  C CG2 . THR F 91  ? 0.665 0.658 0.811 0.202  -0.053 0.156  91  THR FFF CG2 
7380  N N   . ALA F 92  ? 0.617 0.595 0.742 0.160  -0.035 0.106  92  ALA FFF N   
7381  C CA  . ALA F 92  ? 0.626 0.579 0.735 0.143  -0.029 0.102  92  ALA FFF CA  
7382  C C   . ALA F 92  ? 0.589 0.566 0.681 0.128  -0.031 0.098  92  ALA FFF C   
7383  O O   . ALA F 92  ? 0.598 0.608 0.691 0.129  -0.038 0.096  92  ALA FFF O   
7384  C CB  . ALA F 92  ? 0.636 0.568 0.751 0.139  -0.020 0.082  92  ALA FFF CB  
7385  N N   . VAL F 93  ? 0.559 0.521 0.639 0.114  -0.026 0.098  93  VAL FFF N   
7386  C CA  . VAL F 93  ? 0.529 0.508 0.594 0.100  -0.026 0.089  93  VAL FFF CA  
7387  C C   . VAL F 93  ? 0.548 0.525 0.619 0.094  -0.022 0.068  93  VAL FFF C   
7388  O O   . VAL F 93  ? 0.590 0.543 0.668 0.093  -0.016 0.062  93  VAL FFF O   
7389  C CB  . VAL F 93  ? 0.519 0.486 0.570 0.091  -0.021 0.098  93  VAL FFF CB  
7390  C CG1 . VAL F 93  ? 0.483 0.464 0.520 0.079  -0.019 0.087  93  VAL FFF CG1 
7391  C CG2 . VAL F 93  ? 0.528 0.497 0.570 0.097  -0.024 0.122  93  VAL FFF CG2 
7392  N N   . TYR F 94  ? 0.515 0.516 0.583 0.090  -0.025 0.058  94  TYR FFF N   
7393  C CA  . TYR F 94  ? 0.492 0.495 0.565 0.084  -0.021 0.041  94  TYR FFF CA  
7394  C C   . TYR F 94  ? 0.498 0.500 0.556 0.071  -0.020 0.034  94  TYR FFF C   
7395  O O   . TYR F 94  ? 0.460 0.477 0.507 0.068  -0.024 0.037  94  TYR FFF O   
7396  C CB  . TYR F 94  ? 0.491 0.519 0.575 0.088  -0.025 0.036  94  TYR FFF CB  
7397  C CG  . TYR F 94  ? 0.507 0.535 0.608 0.102  -0.023 0.038  94  TYR FFF CG  
7398  C CD1 . TYR F 94  ? 0.531 0.561 0.640 0.115  -0.027 0.052  94  TYR FFF CD1 
7399  C CD2 . TYR F 94  ? 0.506 0.533 0.617 0.105  -0.016 0.027  94  TYR FFF CD2 
7400  C CE1 . TYR F 94  ? 0.552 0.581 0.679 0.131  -0.025 0.054  94  TYR FFF CE1 
7401  C CE2 . TYR F 94  ? 0.536 0.563 0.662 0.121  -0.012 0.027  94  TYR FFF CE2 
7402  C CZ  . TYR F 94  ? 0.551 0.579 0.687 0.134  -0.016 0.040  94  TYR FFF CZ  
7403  O OH  . TYR F 94  ? 0.579 0.607 0.732 0.153  -0.012 0.040  94  TYR FFF OH  
7404  N N   . PHE F 95  ? 0.502 0.488 0.560 0.065  -0.014 0.026  95  PHE FFF N   
7405  C CA  . PHE F 95  ? 0.505 0.491 0.554 0.054  -0.012 0.020  95  PHE FFF CA  
7406  C C   . PHE F 95  ? 0.525 0.515 0.575 0.050  -0.011 0.007  95  PHE FFF C   
7407  O O   . PHE F 95  ? 0.540 0.524 0.597 0.052  -0.009 0.001  95  PHE FFF O   
7408  C CB  . PHE F 95  ? 0.516 0.483 0.567 0.050  -0.007 0.022  95  PHE FFF CB  
7409  C CG  . PHE F 95  ? 0.513 0.473 0.564 0.051  -0.006 0.038  95  PHE FFF CG  
7410  C CD1 . PHE F 95  ? 0.524 0.468 0.583 0.058  -0.007 0.046  95  PHE FFF CD1 
7411  C CD2 . PHE F 95  ? 0.535 0.504 0.575 0.047  -0.004 0.046  95  PHE FFF CD2 
7412  C CE1 . PHE F 95  ? 0.536 0.472 0.595 0.059  -0.005 0.064  95  PHE FFF CE1 
7413  C CE2 . PHE F 95  ? 0.558 0.522 0.597 0.048  -0.001 0.063  95  PHE FFF CE2 
7414  C CZ  . PHE F 95  ? 0.550 0.498 0.598 0.053  -0.003 0.073  95  PHE FFF CZ  
7415  N N   . CYS F 96  ? 0.524 0.524 0.566 0.045  -0.013 0.003  96  CYS FFF N   
7416  C CA  . CYS F 96  ? 0.544 0.544 0.584 0.039  -0.012 -0.007 96  CYS FFF CA  
7417  C C   . CYS F 96  ? 0.503 0.491 0.541 0.035  -0.009 -0.010 96  CYS FFF C   
7418  O O   . CYS F 96  ? 0.477 0.463 0.513 0.034  -0.008 -0.004 96  CYS FFF O   
7419  C CB  . CYS F 96  ? 0.574 0.584 0.606 0.035  -0.017 -0.009 96  CYS FFF CB  
7420  S SG  . CYS F 96  ? 0.708 0.716 0.740 0.028  -0.017 -0.018 96  CYS FFF SG  
7421  N N   . ALA F 97  ? 0.471 0.455 0.511 0.033  -0.008 -0.017 97  ALA FFF N   
7422  C CA  . ALA F 97  ? 0.480 0.457 0.519 0.028  -0.007 -0.020 97  ALA FFF CA  
7423  C C   . ALA F 97  ? 0.468 0.446 0.502 0.026  -0.008 -0.026 97  ALA FFF C   
7424  O O   . ALA F 97  ? 0.454 0.437 0.488 0.027  -0.008 -0.027 97  ALA FFF O   
7425  C CB  . ALA F 97  ? 0.492 0.457 0.537 0.028  -0.007 -0.020 97  ALA FFF CB  
7426  N N   . ALA F 98  ? 0.457 0.435 0.491 0.023  -0.009 -0.027 98  ALA FFF N   
7427  C CA  . ALA F 98  ? 0.448 0.426 0.477 0.022  -0.011 -0.030 98  ALA FFF CA  
7428  C C   . ALA F 98  ? 0.446 0.423 0.478 0.020  -0.014 -0.032 98  ALA FFF C   
7429  O O   . ALA F 98  ? 0.466 0.446 0.506 0.019  -0.013 -0.030 98  ALA FFF O   
7430  C CB  . ALA F 98  ? 0.444 0.424 0.469 0.022  -0.011 -0.029 98  ALA FFF CB  
7431  N N   . ASP F 99  ? 0.459 0.436 0.485 0.019  -0.016 -0.035 99  ASP FFF N   
7432  C CA  . ASP F 99  ? 0.452 0.431 0.479 0.018  -0.021 -0.036 99  ASP FFF CA  
7433  C C   . ASP F 99  ? 0.432 0.410 0.449 0.020  -0.024 -0.035 99  ASP FFF C   
7434  O O   . ASP F 99  ? 0.464 0.441 0.473 0.020  -0.021 -0.034 99  ASP FFF O   
7435  C CB  . ASP F 99  ? 0.482 0.456 0.510 0.015  -0.024 -0.042 99  ASP FFF CB  
7436  C CG  . ASP F 99  ? 0.515 0.495 0.551 0.011  -0.031 -0.042 99  ASP FFF CG  
7437  O OD1 . ASP F 99  ? 0.557 0.543 0.609 0.008  -0.030 -0.038 99  ASP FFF OD1 
7438  O OD2 . ASP F 99  ? 0.532 0.515 0.561 0.011  -0.038 -0.046 99  ASP FFF OD2 
7439  N N   . ARG F 100 ? 0.446 0.429 0.466 0.021  -0.029 -0.033 100 ARG FFF N   
7440  C CA  . ARG F 100 ? 0.509 0.492 0.519 0.023  -0.033 -0.029 100 ARG FFF CA  
7441  C C   . ARG F 100 ? 0.517 0.501 0.513 0.021  -0.036 -0.033 100 ARG FFF C   
7442  O O   . ARG F 100 ? 0.522 0.503 0.504 0.022  -0.034 -0.028 100 ARG FFF O   
7443  C CB  . ARG F 100 ? 0.535 0.526 0.554 0.026  -0.039 -0.026 100 ARG FFF CB  
7444  C CG  . ARG F 100 ? 0.544 0.534 0.573 0.031  -0.035 -0.023 100 ARG FFF CG  
7445  C CD  . ARG F 100 ? 0.580 0.556 0.600 0.035  -0.033 -0.019 100 ARG FFF CD  
7446  N NE  . ARG F 100 ? 0.617 0.590 0.626 0.035  -0.038 -0.013 100 ARG FFF NE  
7447  C CZ  . ARG F 100 ? 0.614 0.586 0.624 0.041  -0.044 -0.007 100 ARG FFF CZ  
7448  N NH1 . ARG F 100 ? 0.590 0.569 0.615 0.049  -0.045 -0.007 100 ARG FFF NH1 
7449  N NH2 . ARG F 100 ? 0.679 0.647 0.675 0.041  -0.047 0.000  100 ARG FFF NH2 
7450  N N   . GLY F 101 ? 0.470 0.454 0.468 0.018  -0.038 -0.041 101 GLY FFF N   
7451  C CA  . GLY F 101 ? 0.521 0.504 0.503 0.017  -0.042 -0.048 101 GLY FFF CA  
7452  C C   . GLY F 101 ? 0.517 0.493 0.492 0.019  -0.034 -0.054 101 GLY FFF C   
7453  O O   . GLY F 101 ? 0.472 0.443 0.459 0.018  -0.029 -0.054 101 GLY FFF O   
7454  N N   . GLU F 102 ? 0.518 0.494 0.473 0.021  -0.033 -0.058 102 GLU FFF N   
7455  C CA  . GLU F 102 ? 0.533 0.503 0.479 0.025  -0.026 -0.066 102 GLU FFF CA  
7456  C C   . GLU F 102 ? 0.554 0.515 0.493 0.024  -0.033 -0.081 102 GLU FFF C   
7457  O O   . GLU F 102 ? 0.537 0.502 0.459 0.023  -0.041 -0.085 102 GLU FFF O   
7458  C CB  . GLU F 102 ? 0.548 0.527 0.477 0.029  -0.017 -0.062 102 GLU FFF CB  
7459  C CG  . GLU F 102 ? 0.572 0.551 0.496 0.036  -0.007 -0.069 102 GLU FFF CG  
7460  C CD  . GLU F 102 ? 0.600 0.592 0.507 0.040  0.003  -0.064 102 GLU FFF CD  
7461  O OE1 . GLU F 102 ? 0.609 0.608 0.515 0.036  0.003  -0.050 102 GLU FFF OE1 
7462  O OE2 . GLU F 102 ? 0.641 0.635 0.536 0.047  0.011  -0.072 102 GLU FFF OE2 
7463  N N   . SER F 103 ? 0.540 0.489 0.490 0.024  -0.032 -0.088 103 SER FFF N   
7464  C CA  . SER F 103 ? 0.564 0.498 0.511 0.021  -0.040 -0.103 103 SER FFF CA  
7465  C C   . SER F 103 ? 0.577 0.502 0.502 0.029  -0.035 -0.117 103 SER FFF C   
7466  O O   . SER F 103 ? 0.598 0.523 0.522 0.038  -0.023 -0.116 103 SER FFF O   
7467  C CB  . SER F 103 ? 0.556 0.478 0.527 0.016  -0.041 -0.102 103 SER FFF CB  
7468  O OG  . SER F 103 ? 0.582 0.486 0.552 0.011  -0.049 -0.116 103 SER FFF OG  
7469  N N   . TYR F 104 ? 0.517 0.474 0.474 0.106  0.022  0.039  104 TYR FFF N   
7470  C CA  . TYR F 104 ? 0.542 0.502 0.495 0.113  0.028  0.038  104 TYR FFF CA  
7471  C C   . TYR F 104 ? 0.529 0.486 0.488 0.115  0.026  0.034  104 TYR FFF C   
7472  O O   . TYR F 104 ? 0.545 0.510 0.507 0.123  0.031  0.034  104 TYR FFF O   
7473  C CB  . TYR F 104 ? 0.564 0.517 0.499 0.118  0.027  0.031  104 TYR FFF CB  
7474  C CG  . TYR F 104 ? 0.580 0.533 0.507 0.127  0.033  0.028  104 TYR FFF CG  
7475  C CD1 . TYR F 104 ? 0.581 0.549 0.509 0.131  0.041  0.033  104 TYR FFF CD1 
7476  C CD2 . TYR F 104 ? 0.618 0.556 0.533 0.131  0.029  0.020  104 TYR FFF CD2 
7477  C CE1 . TYR F 104 ? 0.598 0.571 0.518 0.143  0.047  0.029  104 TYR FFF CE1 
7478  C CE2 . TYR F 104 ? 0.631 0.565 0.534 0.143  0.033  0.015  104 TYR FFF CE2 
7479  C CZ  . TYR F 104 ? 0.617 0.571 0.524 0.150  0.043  0.019  104 TYR FFF CZ  
7480  O OH  . TYR F 104 ? 0.628 0.584 0.524 0.165  0.047  0.013  104 TYR FFF OH  
7481  N N   . TYR F 105 ? 0.528 0.477 0.488 0.109  0.019  0.030  105 TYR FFF N   
7482  C CA  . TYR F 105 ? 0.537 0.476 0.496 0.108  0.015  0.028  105 TYR FFF CA  
7483  C C   . TYR F 105 ? 0.537 0.486 0.515 0.102  0.013  0.033  105 TYR FFF C   
7484  O O   . TYR F 105 ? 0.524 0.469 0.503 0.094  0.007  0.032  105 TYR FFF O   
7485  C CB  . TYR F 105 ? 0.550 0.474 0.493 0.099  0.008  0.021  105 TYR FFF CB  
7486  C CG  . TYR F 105 ? 0.537 0.454 0.462 0.101  0.008  0.015  105 TYR FFF CG  
7487  C CD1 . TYR F 105 ? 0.552 0.452 0.460 0.110  0.010  0.012  105 TYR FFF CD1 
7488  C CD2 . TYR F 105 ? 0.535 0.462 0.456 0.094  0.005  0.012  105 TYR FFF CD2 
7489  C CE1 . TYR F 105 ? 0.562 0.454 0.451 0.111  0.009  0.006  105 TYR FFF CE1 
7490  C CE2 . TYR F 105 ? 0.554 0.478 0.459 0.094  0.005  0.006  105 TYR FFF CE2 
7491  C CZ  . TYR F 105 ? 0.561 0.466 0.449 0.101  0.007  0.003  105 TYR FFF CZ  
7492  O OH  . TYR F 105 ? 0.592 0.494 0.462 0.101  0.006  -0.003 105 TYR FFF OH  
7493  N N   . TYR F 106 ? 0.541 0.507 0.531 0.105  0.019  0.039  106 TYR FFF N   
7494  C CA  . TYR F 106 ? 0.530 0.508 0.537 0.098  0.018  0.045  106 TYR FFF CA  
7495  C C   . TYR F 106 ? 0.521 0.497 0.533 0.099  0.013  0.045  106 TYR FFF C   
7496  O O   . TYR F 106 ? 0.506 0.491 0.531 0.090  0.011  0.048  106 TYR FFF O   
7497  C CB  . TYR F 106 ? 0.529 0.528 0.545 0.097  0.025  0.052  106 TYR FFF CB  
7498  C CG  . TYR F 106 ? 0.519 0.534 0.536 0.110  0.031  0.051  106 TYR FFF CG  
7499  C CD1 . TYR F 106 ? 0.516 0.546 0.544 0.117  0.030  0.050  106 TYR FFF CD1 
7500  C CD2 . TYR F 106 ? 0.534 0.552 0.540 0.117  0.037  0.049  106 TYR FFF CD2 
7501  C CE1 . TYR F 106 ? 0.529 0.577 0.557 0.134  0.034  0.047  106 TYR FFF CE1 
7502  C CE2 . TYR F 106 ? 0.538 0.574 0.544 0.131  0.042  0.046  106 TYR FFF CE2 
7503  C CZ  . TYR F 106 ? 0.548 0.600 0.565 0.141  0.040  0.044  106 TYR FFF CZ  
7504  O OH  . TYR F 106 ? 0.558 0.632 0.574 0.160  0.045  0.039  106 TYR FFF OH  
7505  N N   . THR F 107 ? 0.519 0.481 0.519 0.108  0.011  0.040  107 THR FFF N   
7506  C CA  . THR F 107 ? 0.522 0.475 0.521 0.111  0.004  0.040  107 THR FFF CA  
7507  C C   . THR F 107 ? 0.524 0.456 0.511 0.097  -0.004 0.038  107 THR FFF C   
7508  O O   . THR F 107 ? 0.536 0.458 0.520 0.095  -0.010 0.040  107 THR FFF O   
7509  C CB  . THR F 107 ? 0.535 0.476 0.520 0.130  0.003  0.037  107 THR FFF CB  
7510  O OG1 . THR F 107 ? 0.571 0.480 0.530 0.130  -0.001 0.031  107 THR FFF OG1 
7511  C CG2 . THR F 107 ? 0.521 0.491 0.517 0.144  0.011  0.037  107 THR FFF CG2 
7512  N N   . ARG F 108 ? 0.543 0.471 0.523 0.088  -0.003 0.034  108 ARG FFF N   
7513  C CA  . ARG F 108 ? 0.557 0.476 0.526 0.072  -0.010 0.031  108 ARG FFF CA  
7514  C C   . ARG F 108 ? 0.546 0.483 0.531 0.062  -0.011 0.033  108 ARG FFF C   
7515  O O   . ARG F 108 ? 0.551 0.505 0.549 0.063  -0.008 0.033  108 ARG FFF O   
7516  C CB  . ARG F 108 ? 0.560 0.480 0.517 0.067  -0.009 0.025  108 ARG FFF CB  
7517  C CG  . ARG F 108 ? 0.570 0.466 0.504 0.072  -0.010 0.021  108 ARG FFF CG  
7518  C CD  . ARG F 108 ? 0.578 0.481 0.502 0.062  -0.011 0.015  108 ARG FFF CD  
7519  N NE  . ARG F 108 ? 0.601 0.485 0.504 0.067  -0.010 0.011  108 ARG FFF NE  
7520  C CZ  . ARG F 108 ? 0.606 0.498 0.500 0.062  -0.010 0.006  108 ARG FFF CZ  
7521  N NH1 . ARG F 108 ? 0.614 0.535 0.519 0.054  -0.011 0.003  108 ARG FFF NH1 
7522  N NH2 . ARG F 108 ? 0.633 0.504 0.506 0.066  -0.010 0.002  108 ARG FFF NH2 
7523  N N   . PRO F 109 ? 0.553 0.485 0.535 0.053  -0.017 0.034  109 PRO FFF N   
7524  C CA  . PRO F 109 ? 0.531 0.481 0.525 0.042  -0.019 0.034  109 PRO FFF CA  
7525  C C   . PRO F 109 ? 0.520 0.488 0.515 0.036  -0.018 0.027  109 PRO FFF C   
7526  O O   . PRO F 109 ? 0.548 0.532 0.556 0.037  -0.017 0.026  109 PRO FFF O   
7527  C CB  . PRO F 109 ? 0.538 0.475 0.519 0.031  -0.026 0.036  109 PRO FFF CB  
7528  C CG  . PRO F 109 ? 0.566 0.477 0.536 0.043  -0.028 0.040  109 PRO FFF CG  
7529  C CD  . PRO F 109 ? 0.564 0.470 0.528 0.054  -0.023 0.037  109 PRO FFF CD  
7530  N N   . THR F 110 ? 0.495 0.461 0.475 0.030  -0.019 0.022  110 THR FFF N   
7531  C CA  . THR F 110 ? 0.480 0.470 0.459 0.026  -0.020 0.013  110 THR FFF CA  
7532  C C   . THR F 110 ? 0.460 0.459 0.449 0.042  -0.016 0.012  110 THR FFF C   
7533  O O   . THR F 110 ? 0.467 0.487 0.458 0.044  -0.018 0.005  110 THR FFF O   
7534  C CB  . THR F 110 ? 0.496 0.484 0.455 0.014  -0.022 0.008  110 THR FFF CB  
7535  O OG1 . THR F 110 ? 0.515 0.477 0.464 0.023  -0.020 0.011  110 THR FFF OG1 
7536  C CG2 . THR F 110 ? 0.497 0.476 0.439 -0.008 -0.027 0.009  110 THR FFF CG2 
7537  N N   . GLU F 111 ? 0.467 0.450 0.460 0.053  -0.012 0.018  111 GLU FFF N   
7538  C CA  . GLU F 111 ? 0.468 0.452 0.464 0.065  -0.009 0.019  111 GLU FFF CA  
7539  C C   . GLU F 111 ? 0.488 0.475 0.494 0.066  -0.010 0.022  111 GLU FFF C   
7540  O O   . GLU F 111 ? 0.509 0.489 0.512 0.074  -0.010 0.023  111 GLU FFF O   
7541  C CB  . GLU F 111 ? 0.473 0.444 0.465 0.073  -0.004 0.025  111 GLU FFF CB  
7542  C CG  . GLU F 111 ? 0.484 0.450 0.463 0.074  -0.003 0.021  111 GLU FFF CG  
7543  C CD  . GLU F 111 ? 0.483 0.459 0.454 0.078  -0.005 0.014  111 GLU FFF CD  
7544  O OE1 . GLU F 111 ? 0.457 0.450 0.428 0.072  -0.010 0.008  111 GLU FFF OE1 
7545  O OE2 . GLU F 111 ? 0.489 0.460 0.453 0.086  -0.002 0.016  111 GLU FFF OE2 
7546  N N   . TYR F 112 ? 0.486 0.477 0.500 0.058  -0.013 0.022  112 TYR FFF N   
7547  C CA  . TYR F 112 ? 0.496 0.486 0.516 0.058  -0.015 0.024  112 TYR FFF CA  
7548  C C   . TYR F 112 ? 0.485 0.491 0.506 0.054  -0.020 0.015  112 TYR FFF C   
7549  O O   . TYR F 112 ? 0.484 0.501 0.507 0.044  -0.021 0.013  112 TYR FFF O   
7550  C CB  . TYR F 112 ? 0.495 0.481 0.526 0.053  -0.012 0.033  112 TYR FFF CB  
7551  C CG  . TYR F 112 ? 0.509 0.489 0.540 0.057  -0.007 0.040  112 TYR FFF CG  
7552  C CD1 . TYR F 112 ? 0.535 0.513 0.563 0.061  -0.005 0.040  112 TYR FFF CD1 
7553  C CD2 . TYR F 112 ? 0.517 0.493 0.548 0.058  -0.004 0.045  112 TYR FFF CD2 
7554  C CE1 . TYR F 112 ? 0.548 0.526 0.576 0.068  0.001  0.045  112 TYR FFF CE1 
7555  C CE2 . TYR F 112 ? 0.535 0.513 0.567 0.060  0.002  0.051  112 TYR FFF CE2 
7556  C CZ  . TYR F 112 ? 0.535 0.518 0.568 0.068  0.005  0.050  112 TYR FFF CZ  
7557  O OH  . TYR F 112 ? 0.543 0.532 0.575 0.073  0.011  0.054  112 TYR FFF OH  
7558  N N   . GLU F 113 ? 0.482 0.489 0.498 0.063  -0.023 0.009  113 GLU FFF N   
7559  C CA  . GLU F 113 ? 0.495 0.524 0.511 0.065  -0.028 -0.003 113 GLU FFF CA  
7560  C C   . GLU F 113 ? 0.467 0.497 0.490 0.055  -0.030 -0.001 113 GLU FFF C   
7561  O O   . GLU F 113 ? 0.500 0.554 0.525 0.048  -0.031 -0.008 113 GLU FFF O   
7562  C CB  . GLU F 113 ? 0.556 0.583 0.561 0.083  -0.033 -0.011 113 GLU FFF CB  
7563  C CG  . GLU F 113 ? 0.599 0.656 0.604 0.089  -0.038 -0.026 113 GLU FFF CG  
7564  C CD  . GLU F 113 ? 0.681 0.737 0.672 0.113  -0.045 -0.037 113 GLU FFF CD  
7565  O OE1 . GLU F 113 ? 0.717 0.743 0.696 0.124  -0.047 -0.032 113 GLU FFF OE1 
7566  O OE2 . GLU F 113 ? 0.777 0.862 0.768 0.121  -0.050 -0.051 113 GLU FFF OE2 
7567  N N   . PHE F 114 ? 0.462 0.470 0.486 0.054  -0.029 0.006  114 PHE FFF N   
7568  C CA  . PHE F 114 ? 0.461 0.468 0.490 0.046  -0.032 0.007  114 PHE FFF CA  
7569  C C   . PHE F 114 ? 0.446 0.451 0.486 0.034  -0.029 0.018  114 PHE FFF C   
7570  O O   . PHE F 114 ? 0.466 0.462 0.509 0.034  -0.025 0.027  114 PHE FFF O   
7571  C CB  . PHE F 114 ? 0.487 0.468 0.504 0.053  -0.036 0.006  114 PHE FFF CB  
7572  C CG  . PHE F 114 ? 0.496 0.476 0.499 0.070  -0.042 -0.006 114 PHE FFF CG  
7573  C CD1 . PHE F 114 ? 0.489 0.495 0.492 0.076  -0.045 -0.020 114 PHE FFF CD1 
7574  C CD2 . PHE F 114 ? 0.520 0.475 0.507 0.083  -0.043 -0.005 114 PHE FFF CD2 
7575  C CE1 . PHE F 114 ? 0.516 0.526 0.505 0.096  -0.051 -0.033 114 PHE FFF CE1 
7576  C CE2 . PHE F 114 ? 0.537 0.488 0.507 0.103  -0.050 -0.017 114 PHE FFF CE2 
7577  C CZ  . PHE F 114 ? 0.521 0.503 0.494 0.112  -0.054 -0.032 114 PHE FFF CZ  
7578  N N   . TRP F 115 ? 0.447 0.465 0.492 0.024  -0.031 0.017  115 TRP FFF N   
7579  C CA  . TRP F 115 ? 0.432 0.451 0.485 0.015  -0.031 0.026  115 TRP FFF CA  
7580  C C   . TRP F 115 ? 0.442 0.466 0.499 0.007  -0.035 0.026  115 TRP FFF C   
7581  O O   . TRP F 115 ? 0.462 0.496 0.515 0.005  -0.038 0.017  115 TRP FFF O   
7582  C CB  . TRP F 115 ? 0.422 0.448 0.471 0.010  -0.031 0.026  115 TRP FFF CB  
7583  C CG  . TRP F 115 ? 0.422 0.440 0.466 0.016  -0.028 0.028  115 TRP FFF CG  
7584  C CD1 . TRP F 115 ? 0.415 0.438 0.452 0.021  -0.027 0.021  115 TRP FFF CD1 
7585  C CD2 . TRP F 115 ? 0.419 0.425 0.463 0.020  -0.026 0.036  115 TRP FFF CD2 
7586  N NE1 . TRP F 115 ? 0.420 0.431 0.452 0.025  -0.024 0.025  115 TRP FFF NE1 
7587  C CE2 . TRP F 115 ? 0.434 0.434 0.470 0.025  -0.023 0.033  115 TRP FFF CE2 
7588  C CE3 . TRP F 115 ? 0.452 0.453 0.501 0.021  -0.027 0.044  115 TRP FFF CE3 
7589  C CZ2 . TRP F 115 ? 0.453 0.440 0.484 0.032  -0.021 0.038  115 TRP FFF CZ2 
7590  C CZ3 . TRP F 115 ? 0.462 0.453 0.507 0.030  -0.026 0.048  115 TRP FFF CZ3 
7591  C CH2 . TRP F 115 ? 0.460 0.442 0.495 0.036  -0.022 0.045  115 TRP FFF CH2 
7592  N N   . GLY F 116 ? 0.430 0.451 0.495 0.002  -0.035 0.035  116 GLY FFF N   
7593  C CA  . GLY F 116 ? 0.424 0.452 0.493 -0.007 -0.039 0.036  116 GLY FFF CA  
7594  C C   . GLY F 116 ? 0.424 0.462 0.493 -0.013 -0.042 0.038  116 GLY FFF C   
7595  O O   . GLY F 116 ? 0.435 0.471 0.498 -0.010 -0.041 0.038  116 GLY FFF O   
7596  N N   . GLN F 117 ? 0.435 0.481 0.505 -0.021 -0.046 0.038  117 GLN FFF N   
7597  C CA  . GLN F 117 ? 0.457 0.509 0.522 -0.029 -0.051 0.041  117 GLN FFF CA  
7598  C C   . GLN F 117 ? 0.479 0.527 0.548 -0.025 -0.053 0.052  117 GLN FFF C   
7599  O O   . GLN F 117 ? 0.541 0.583 0.599 -0.027 -0.057 0.056  117 GLN FFF O   
7600  C CB  . GLN F 117 ? 0.446 0.509 0.510 -0.039 -0.055 0.037  117 GLN FFF CB  
7601  C CG  . GLN F 117 ? 0.450 0.520 0.508 -0.039 -0.054 0.024  117 GLN FFF CG  
7602  C CD  . GLN F 117 ? 0.465 0.545 0.513 -0.040 -0.052 0.018  117 GLN FFF CD  
7603  O OE1 . GLN F 117 ? 0.487 0.574 0.528 -0.051 -0.054 0.021  117 GLN FFF OE1 
7604  N NE2 . GLN F 117 ? 0.457 0.540 0.504 -0.030 -0.049 0.008  117 GLN FFF NE2 
7605  N N   . GLY F 118 ? 0.494 0.546 0.576 -0.018 -0.050 0.056  118 GLY FFF N   
7606  C CA  . GLY F 118 ? 0.493 0.551 0.581 -0.010 -0.052 0.065  118 GLY FFF CA  
7607  C C   . GLY F 118 ? 0.479 0.555 0.576 -0.015 -0.058 0.069  118 GLY FFF C   
7608  O O   . GLY F 118 ? 0.487 0.565 0.581 -0.026 -0.061 0.066  118 GLY FFF O   
7609  N N   . THR F 119 ? 0.515 0.608 0.624 -0.006 -0.059 0.074  119 THR FFF N   
7610  C CA  . THR F 119 ? 0.516 0.635 0.636 -0.008 -0.065 0.078  119 THR FFF CA  
7611  C C   . THR F 119 ? 0.525 0.650 0.644 0.012  -0.070 0.083  119 THR FFF C   
7612  O O   . THR F 119 ? 0.529 0.653 0.649 0.026  -0.065 0.083  119 THR FFF O   
7613  C CB  . THR F 119 ? 0.535 0.677 0.670 -0.020 -0.060 0.078  119 THR FFF CB  
7614  O OG1 . THR F 119 ? 0.569 0.736 0.711 -0.028 -0.067 0.080  119 THR FFF OG1 
7615  C CG2 . THR F 119 ? 0.531 0.691 0.676 -0.011 -0.053 0.080  119 THR FFF CG2 
7616  N N   . GLN F 120 ? 0.535 0.666 0.650 0.015  -0.079 0.087  120 GLN FFF N   
7617  C CA  . GLN F 120 ? 0.536 0.671 0.647 0.038  -0.088 0.091  120 GLN FFF CA  
7618  C C   . GLN F 120 ? 0.547 0.731 0.682 0.048  -0.085 0.091  120 GLN FFF C   
7619  O O   . GLN F 120 ? 0.540 0.759 0.692 0.033  -0.084 0.092  120 GLN FFF O   
7620  C CB  . GLN F 120 ? 0.548 0.674 0.644 0.036  -0.100 0.095  120 GLN FFF CB  
7621  C CG  . GLN F 120 ? 0.591 0.706 0.671 0.063  -0.112 0.099  120 GLN FFF CG  
7622  C CD  . GLN F 120 ? 0.640 0.706 0.693 0.075  -0.113 0.099  120 GLN FFF CD  
7623  O OE1 . GLN F 120 ? 0.637 0.667 0.670 0.058  -0.112 0.099  120 GLN FFF OE1 
7624  N NE2 . GLN F 120 ? 0.677 0.743 0.727 0.103  -0.115 0.098  120 GLN FFF NE2 
7625  N N   . VAL F 121 ? 0.547 0.736 0.682 0.072  -0.084 0.090  121 VAL FFF N   
7626  C CA  . VAL F 121 ? 0.529 0.771 0.684 0.090  -0.084 0.090  121 VAL FFF CA  
7627  C C   . VAL F 121 ? 0.551 0.780 0.688 0.121  -0.098 0.091  121 VAL FFF C   
7628  O O   . VAL F 121 ? 0.586 0.766 0.697 0.136  -0.101 0.090  121 VAL FFF O   
7629  C CB  . VAL F 121 ? 0.512 0.771 0.677 0.095  -0.072 0.087  121 VAL FFF CB  
7630  C CG1 . VAL F 121 ? 0.525 0.844 0.709 0.117  -0.072 0.084  121 VAL FFF CG1 
7631  C CG2 . VAL F 121 ? 0.484 0.747 0.659 0.065  -0.061 0.087  121 VAL FFF CG2 
7632  N N   . THR F 122 ? 0.546 0.816 0.694 0.131  -0.107 0.092  122 THR FFF N   
7633  C CA  . THR F 122 ? 0.592 0.853 0.722 0.167  -0.122 0.093  122 THR FFF CA  
7634  C C   . THR F 122 ? 0.592 0.926 0.748 0.192  -0.122 0.088  122 THR FFF C   
7635  O O   . THR F 122 ? 0.587 0.983 0.772 0.176  -0.119 0.089  122 THR FFF O   
7636  C CB  . THR F 122 ? 0.594 0.831 0.706 0.160  -0.137 0.099  122 THR FFF CB  
7637  O OG1 . THR F 122 ? 0.602 0.780 0.692 0.136  -0.134 0.102  122 THR FFF OG1 
7638  C CG2 . THR F 122 ? 0.637 0.852 0.722 0.197  -0.155 0.100  122 THR FFF CG2 
7639  N N   . VAL F 123 ? 0.620 0.947 0.764 0.229  -0.126 0.083  123 VAL FFF N   
7640  C CA  . VAL F 123 ? 0.644 1.045 0.810 0.261  -0.127 0.076  123 VAL FFF CA  
7641  C C   . VAL F 123 ? 0.709 1.094 0.849 0.303  -0.148 0.075  123 VAL FFF C   
7642  O O   . VAL F 123 ? 0.750 1.064 0.851 0.326  -0.156 0.074  123 VAL FFF O   
7643  C CB  . VAL F 123 ? 0.636 1.045 0.805 0.274  -0.114 0.069  123 VAL FFF CB  
7644  C CG1 . VAL F 123 ? 0.643 1.144 0.840 0.299  -0.111 0.061  123 VAL FFF CG1 
7645  C CG2 . VAL F 123 ? 0.599 0.999 0.780 0.233  -0.096 0.072  123 VAL FFF CG2 
7646  N N   . SER F 124 ? 0.749 1.198 0.908 0.313  -0.157 0.075  124 SER FFF N   
7647  C CA  . SER F 124 ? 0.804 1.249 0.942 0.357  -0.179 0.074  124 SER FFF CA  
7648  C C   . SER F 124 ? 0.799 1.333 0.961 0.398  -0.180 0.062  124 SER FFF C   
7649  O O   . SER F 124 ? 0.810 1.330 0.959 0.428  -0.178 0.054  124 SER FFF O   
7650  C CB  . SER F 124 ? 0.809 1.263 0.949 0.339  -0.189 0.081  124 SER FFF CB  
7651  O OG  . SER F 124 ? 0.818 1.376 1.003 0.328  -0.184 0.078  124 SER FFF OG  
7652  N N   . THR G 4   ? 1.115 1.301 0.893 -0.062 -0.140 0.146  333 THR GGG N   
7653  C CA  . THR G 4   ? 1.101 1.293 0.855 -0.055 -0.114 0.179  333 THR GGG CA  
7654  C C   . THR G 4   ? 1.036 1.224 0.805 -0.057 -0.073 0.172  333 THR GGG C   
7655  O O   . THR G 4   ? 1.016 1.196 0.818 -0.063 -0.058 0.200  333 THR GGG O   
7656  C CB  . THR G 4   ? 1.209 1.416 0.874 -0.047 -0.126 0.189  333 THR GGG CB  
7657  O OG1 . THR G 4   ? 1.206 1.436 0.841 -0.048 -0.096 0.225  333 THR GGG OG1 
7658  C CG2 . THR G 4   ? 1.249 1.449 0.845 -0.034 -0.138 0.142  333 THR GGG CG2 
7659  N N   . ASN G 5   ? 0.963 1.148 0.706 -0.052 -0.063 0.136  334 ASN GGG N   
7660  C CA  . ASN G 5   ? 0.860 1.049 0.617 -0.050 -0.028 0.125  334 ASN GGG CA  
7661  C C   . ASN G 5   ? 0.766 0.933 0.595 -0.062 -0.023 0.119  334 ASN GGG C   
7662  O O   . ASN G 5   ? 0.726 0.883 0.581 -0.067 -0.044 0.103  334 ASN GGG O   
7663  C CB  . ASN G 5   ? 0.895 1.080 0.596 -0.029 -0.029 0.082  334 ASN GGG CB  
7664  C CG  . ASN G 5   ? 0.885 1.024 0.583 -0.034 -0.072 0.048  334 ASN GGG CG  
7665  O OD1 . ASN G 5   ? 0.894 1.027 0.591 -0.044 -0.106 0.057  334 ASN GGG OD1 
7666  N ND2 . ASN G 5   ? 0.874 0.980 0.577 -0.030 -0.077 0.016  334 ASN GGG ND2 
7667  N N   . LEU G 6   ? 0.724 0.891 0.584 -0.067 0.000  0.133  335 LEU GGG N   
7668  C CA  . LEU G 6   ? 0.659 0.809 0.575 -0.071 0.006  0.125  335 LEU GGG CA  
7669  C C   . LEU G 6   ? 0.625 0.771 0.544 -0.071 0.013  0.094  335 LEU GGG C   
7670  O O   . LEU G 6   ? 0.652 0.802 0.534 -0.063 0.020  0.079  335 LEU GGG O   
7671  C CB  . LEU G 6   ? 0.666 0.802 0.601 -0.078 0.017  0.148  335 LEU GGG CB  
7672  C CG  . LEU G 6   ? 0.719 0.835 0.655 -0.079 -0.003 0.183  335 LEU GGG CG  
7673  C CD1 . LEU G 6   ? 0.737 0.821 0.690 -0.095 -0.005 0.207  335 LEU GGG CD1 
7674  C CD2 . LEU G 6   ? 0.732 0.835 0.693 -0.059 -0.024 0.173  335 LEU GGG CD2 
7675  N N   . CYS G 7   ? 0.612 0.754 0.570 -0.077 0.007  0.086  336 CYS GGG N   
7676  C CA  . CYS G 7   ? 0.616 0.746 0.581 -0.083 0.007  0.066  336 CYS GGG CA  
7677  C C   . CYS G 7   ? 0.599 0.723 0.566 -0.078 0.031  0.062  336 CYS GGG C   
7678  O O   . CYS G 7   ? 0.541 0.666 0.527 -0.078 0.043  0.075  336 CYS GGG O   
7679  C CB  . CYS G 7   ? 0.603 0.754 0.614 -0.094 -0.001 0.075  336 CYS GGG CB  
7680  S SG  . CYS G 7   ? 0.660 0.842 0.688 -0.109 -0.036 0.089  336 CYS GGG SG  
7681  N N   . PRO G 8   ? 0.647 0.759 0.594 -0.072 0.032  0.041  337 PRO GGG N   
7682  C CA  . PRO G 8   ? 0.636 0.760 0.588 -0.065 0.054  0.040  337 PRO GGG CA  
7683  C C   . PRO G 8   ? 0.598 0.708 0.585 -0.074 0.057  0.039  337 PRO GGG C   
7684  O O   . PRO G 8   ? 0.623 0.721 0.609 -0.069 0.054  0.025  337 PRO GGG O   
7685  C CB  . PRO G 8   ? 0.680 0.800 0.589 -0.040 0.048  0.013  337 PRO GGG CB  
7686  C CG  . PRO G 8   ? 0.713 0.782 0.610 -0.047 0.011  -0.005 337 PRO GGG CG  
7687  C CD  . PRO G 8   ? 0.689 0.769 0.607 -0.070 0.003  0.018  337 PRO GGG CD  
7688  N N   . PHE G 9   ? 0.592 0.703 0.604 -0.082 0.059  0.053  338 PHE GGG N   
7689  C CA  . PHE G 9   ? 0.586 0.689 0.618 -0.084 0.062  0.050  338 PHE GGG CA  
7690  C C   . PHE G 9   ? 0.576 0.676 0.615 -0.086 0.069  0.050  338 PHE GGG C   
7691  O O   . PHE G 9   ? 0.550 0.643 0.597 -0.086 0.068  0.042  338 PHE GGG O   
7692  C CB  . PHE G 9   ? 0.606 0.710 0.649 -0.076 0.059  0.056  338 PHE GGG CB  
7693  C CG  . PHE G 9   ? 0.634 0.767 0.685 -0.072 0.054  0.060  338 PHE GGG CG  
7694  C CD1 . PHE G 9   ? 0.621 0.776 0.681 -0.086 0.050  0.064  338 PHE GGG CD1 
7695  C CD2 . PHE G 9   ? 0.662 0.808 0.718 -0.057 0.048  0.067  338 PHE GGG CD2 
7696  C CE1 . PHE G 9   ? 0.618 0.821 0.699 -0.092 0.042  0.079  338 PHE GGG CE1 
7697  C CE2 . PHE G 9   ? 0.661 0.858 0.737 -0.052 0.044  0.076  338 PHE GGG CE2 
7698  C CZ  . PHE G 9   ? 0.642 0.875 0.734 -0.074 0.042  0.085  338 PHE GGG CZ  
7699  N N   . GLY G 10  ? 0.616 0.732 0.657 -0.090 0.075  0.066  339 GLY GGG N   
7700  C CA  . GLY G 10  ? 0.594 0.734 0.655 -0.098 0.080  0.077  339 GLY GGG CA  
7701  C C   . GLY G 10  ? 0.582 0.741 0.642 -0.082 0.087  0.059  339 GLY GGG C   
7702  O O   . GLY G 10  ? 0.564 0.726 0.647 -0.086 0.084  0.059  339 GLY GGG O   
7703  N N   . GLU G 11  ? 0.613 0.775 0.644 -0.062 0.089  0.041  340 GLU GGG N   
7704  C CA  . GLU G 11  ? 0.693 0.856 0.715 -0.036 0.085  0.016  340 GLU GGG CA  
7705  C C   . GLU G 11  ? 0.651 0.767 0.683 -0.045 0.067  0.008  340 GLU GGG C   
7706  O O   . GLU G 11  ? 0.670 0.782 0.705 -0.027 0.060  -0.005 340 GLU GGG O   
7707  C CB  . GLU G 11  ? 0.824 0.968 0.798 -0.011 0.073  -0.008 340 GLU GGG CB  
7708  C CG  . GLU G 11  ? 0.917 1.119 0.866 0.007  0.092  -0.003 340 GLU GGG CG  
7709  C CD  . GLU G 11  ? 1.028 1.202 0.915 0.041  0.073  -0.037 340 GLU GGG CD  
7710  O OE1 . GLU G 11  ? 1.083 1.182 0.952 0.048  0.039  -0.065 340 GLU GGG OE1 
7711  O OE2 . GLU G 11  ? 1.097 1.318 0.949 0.057  0.086  -0.032 340 GLU GGG OE2 
7712  N N   . VAL G 12  ? 0.613 0.702 0.647 -0.066 0.060  0.016  341 VAL GGG N   
7713  C CA  . VAL G 12  ? 0.617 0.680 0.657 -0.078 0.047  0.018  341 VAL GGG CA  
7714  C C   . VAL G 12  ? 0.563 0.637 0.620 -0.083 0.053  0.025  341 VAL GGG C   
7715  O O   . VAL G 12  ? 0.602 0.669 0.665 -0.080 0.045  0.022  341 VAL GGG O   
7716  C CB  . VAL G 12  ? 0.602 0.663 0.639 -0.094 0.040  0.029  341 VAL GGG CB  
7717  C CG1 . VAL G 12  ? 0.606 0.663 0.647 -0.109 0.030  0.043  341 VAL GGG CG1 
7718  C CG2 . VAL G 12  ? 0.619 0.662 0.639 -0.096 0.023  0.024  341 VAL GGG CG2 
7719  N N   . PHE G 13  ? 0.508 0.588 0.569 -0.088 0.060  0.031  342 PHE GGG N   
7720  C CA  . PHE G 13  ? 0.532 0.600 0.596 -0.091 0.053  0.031  342 PHE GGG CA  
7721  C C   . PHE G 13  ? 0.553 0.631 0.640 -0.098 0.047  0.037  342 PHE GGG C   
7722  O O   . PHE G 13  ? 0.516 0.581 0.605 -0.101 0.032  0.034  342 PHE GGG O   
7723  C CB  . PHE G 13  ? 0.526 0.580 0.581 -0.086 0.050  0.030  342 PHE GGG CB  
7724  C CG  . PHE G 13  ? 0.509 0.577 0.547 -0.072 0.055  0.026  342 PHE GGG CG  
7725  C CD1 . PHE G 13  ? 0.490 0.581 0.533 -0.075 0.063  0.034  342 PHE GGG CD1 
7726  C CD2 . PHE G 13  ? 0.532 0.602 0.550 -0.057 0.052  0.016  342 PHE GGG CD2 
7727  C CE1 . PHE G 13  ? 0.483 0.612 0.526 -0.067 0.067  0.040  342 PHE GGG CE1 
7728  C CE2 . PHE G 13  ? 0.526 0.641 0.534 -0.041 0.063  0.019  342 PHE GGG CE2 
7729  C CZ  . PHE G 13  ? 0.492 0.644 0.520 -0.048 0.071  0.035  342 PHE GGG CZ  
7730  N N   . ASN G 14  ? 0.569 0.681 0.674 -0.100 0.057  0.048  343 ASN GGG N   
7731  C CA  . ASN G 14  ? 0.563 0.718 0.705 -0.111 0.055  0.067  343 ASN GGG CA  
7732  C C   . ASN G 14  ? 0.518 0.727 0.672 -0.088 0.068  0.062  343 ASN GGG C   
7733  O O   . ASN G 14  ? 0.510 0.788 0.702 -0.092 0.074  0.083  343 ASN GGG O   
7734  C CB  . ASN G 14  ? 0.627 0.801 0.783 -0.132 0.055  0.097  343 ASN GGG CB  
7735  C CG  . ASN G 14  ? 0.744 0.849 0.888 -0.149 0.027  0.099  343 ASN GGG CG  
7736  O OD1 . ASN G 14  ? 0.792 0.852 0.927 -0.148 0.006  0.082  343 ASN GGG OD1 
7737  N ND2 . ASN G 14  ? 0.865 0.960 1.004 -0.159 0.024  0.119  343 ASN GGG ND2 
7738  N N   . ALA G 15  ? 0.498 0.678 0.624 -0.064 0.067  0.037  344 ALA GGG N   
7739  C CA  . ALA G 15  ? 0.497 0.701 0.626 -0.030 0.066  0.022  344 ALA GGG CA  
7740  C C   . ALA G 15  ? 0.511 0.750 0.682 -0.034 0.057  0.033  344 ALA GGG C   
7741  O O   . ALA G 15  ? 0.492 0.696 0.667 -0.059 0.041  0.040  344 ALA GGG O   
7742  C CB  . ALA G 15  ? 0.516 0.650 0.610 -0.018 0.047  -0.000 344 ALA GGG CB  
7743  N N   . THR G 16  ? 0.539 0.858 0.741 -0.008 0.067  0.037  345 THR GGG N   
7744  C CA  . THR G 16  ? 0.575 0.946 0.829 -0.014 0.055  0.054  345 THR GGG CA  
7745  C C   . THR G 16  ? 0.613 0.921 0.850 0.008  0.029  0.031  345 THR GGG C   
7746  O O   . THR G 16  ? 0.624 0.933 0.886 -0.008 0.009  0.042  345 THR GGG O   
7747  C CB  . THR G 16  ? 0.586 1.092 0.888 0.008  0.078  0.075  345 THR GGG CB  
7748  O OG1 . THR G 16  ? 0.646 1.160 0.908 0.068  0.092  0.041  345 THR GGG OG1 
7749  C CG2 . THR G 16  ? 0.555 1.122 0.887 -0.037 0.092  0.119  345 THR GGG CG2 
7750  N N   . ARG G 17  ? 0.641 0.886 0.831 0.037  0.022  0.004  346 ARG GGG N   
7751  C CA  . ARG G 17  ? 0.664 0.836 0.833 0.054  -0.011 -0.010 346 ARG GGG CA  
7752  C C   . ARG G 17  ? 0.630 0.710 0.754 0.023  -0.024 -0.009 346 ARG GGG C   
7753  O O   . ARG G 17  ? 0.605 0.669 0.706 0.015  -0.013 -0.014 346 ARG GGG O   
7754  C CB  . ARG G 17  ? 0.764 0.932 0.917 0.117  -0.022 -0.041 346 ARG GGG CB  
7755  C CG  . ARG G 17  ? 0.861 1.050 1.041 0.159  -0.044 -0.047 346 ARG GGG CG  
7756  C CD  . ARG G 17  ? 0.983 1.207 1.150 0.239  -0.043 -0.083 346 ARG GGG CD  
7757  N NE  . ARG G 17  ? 1.049 1.413 1.279 0.275  -0.024 -0.074 346 ARG GGG NE  
7758  C CZ  . ARG G 17  ? 1.128 1.588 1.363 0.351  -0.006 -0.098 346 ARG GGG CZ  
7759  N NH1 . ARG G 17  ? 1.209 1.621 1.376 0.404  -0.010 -0.141 346 ARG GGG NH1 
7760  N NH2 . ARG G 17  ? 1.093 1.706 1.400 0.378  0.013  -0.078 346 ARG GGG NH2 
7761  N N   . PHE G 18  ? 0.535 0.777 0.558 -0.062 0.040  0.105  347 PHE GGG N   
7762  C CA  . PHE G 18  ? 0.524 0.708 0.524 -0.062 0.040  0.072  347 PHE GGG CA  
7763  C C   . PHE G 18  ? 0.492 0.667 0.487 -0.049 0.045  0.058  347 PHE GGG C   
7764  O O   . PHE G 18  ? 0.487 0.681 0.496 -0.052 0.042  0.072  347 PHE GGG O   
7765  C CB  . PHE G 18  ? 0.538 0.677 0.529 -0.086 0.025  0.072  347 PHE GGG CB  
7766  C CG  . PHE G 18  ? 0.548 0.668 0.530 -0.092 0.022  0.070  347 PHE GGG CG  
7767  C CD1 . PHE G 18  ? 0.552 0.704 0.550 -0.097 0.019  0.092  347 PHE GGG CD1 
7768  C CD2 . PHE G 18  ? 0.562 0.636 0.523 -0.091 0.021  0.049  347 PHE GGG CD2 
7769  C CE1 . PHE G 18  ? 0.558 0.691 0.550 -0.102 0.014  0.090  347 PHE GGG CE1 
7770  C CE2 . PHE G 18  ? 0.577 0.633 0.531 -0.093 0.018  0.048  347 PHE GGG CE2 
7771  C CZ  . PHE G 18  ? 0.570 0.653 0.539 -0.100 0.014  0.067  347 PHE GGG CZ  
7772  N N   . ALA G 19  ? 0.488 0.634 0.469 -0.039 0.049  0.033  348 ALA GGG N   
7773  C CA  . ALA G 19  ? 0.493 0.623 0.471 -0.028 0.048  0.019  348 ALA GGG CA  
7774  C C   . ALA G 19  ? 0.510 0.616 0.488 -0.046 0.041  0.021  348 ALA GGG C   
7775  O O   . ALA G 19  ? 0.537 0.622 0.507 -0.062 0.036  0.023  348 ALA GGG O   
7776  C CB  . ALA G 19  ? 0.492 0.596 0.457 -0.018 0.048  -0.002 348 ALA GGG CB  
7777  N N   . SER G 20  ? 0.519 0.625 0.503 -0.040 0.039  0.019  349 SER GGG N   
7778  C CA  . SER G 20  ? 0.538 0.619 0.520 -0.051 0.034  0.016  349 SER GGG CA  
7779  C C   . SER G 20  ? 0.534 0.588 0.505 -0.051 0.034  0.003  349 SER GGG C   
7780  O O   . SER G 20  ? 0.569 0.621 0.540 -0.040 0.035  -0.007 349 SER GGG O   
7781  C CB  . SER G 20  ? 0.542 0.630 0.534 -0.042 0.031  0.018  349 SER GGG CB  
7782  O OG  . SER G 20  ? 0.582 0.699 0.587 -0.046 0.031  0.036  349 SER GGG OG  
7783  N N   . VAL G 21  ? 0.510 0.548 0.473 -0.062 0.032  0.004  350 VAL GGG N   
7784  C CA  . VAL G 21  ? 0.504 0.528 0.461 -0.061 0.034  -0.001 350 VAL GGG CA  
7785  C C   . VAL G 21  ? 0.489 0.511 0.461 -0.055 0.029  -0.003 350 VAL GGG C   
7786  O O   . VAL G 21  ? 0.471 0.489 0.445 -0.053 0.028  -0.005 350 VAL GGG O   
7787  C CB  . VAL G 21  ? 0.503 0.515 0.444 -0.067 0.035  0.003  350 VAL GGG CB  
7788  C CG1 . VAL G 21  ? 0.500 0.515 0.446 -0.071 0.030  0.009  350 VAL GGG CG1 
7789  C CG2 . VAL G 21  ? 0.508 0.516 0.442 -0.061 0.041  0.003  350 VAL GGG CG2 
7790  N N   . TYR G 22  ? 0.498 0.522 0.480 -0.054 0.023  -0.000 351 TYR GGG N   
7791  C CA  . TYR G 22  ? 0.526 0.539 0.521 -0.051 0.011  -0.001 351 TYR GGG CA  
7792  C C   . TYR G 22  ? 0.545 0.548 0.536 -0.038 0.005  -0.013 351 TYR GGG C   
7793  O O   . TYR G 22  ? 0.578 0.563 0.574 -0.038 -0.009 -0.014 351 TYR GGG O   
7794  C CB  . TYR G 22  ? 0.525 0.539 0.531 -0.052 0.004  0.005  351 TYR GGG CB  
7795  C CG  . TYR G 22  ? 0.532 0.548 0.538 -0.036 0.001  -0.002 351 TYR GGG CG  
7796  C CD1 . TYR G 22  ? 0.516 0.554 0.519 -0.034 0.011  0.002  351 TYR GGG CD1 
7797  C CD2 . TYR G 22  ? 0.559 0.555 0.567 -0.022 -0.013 -0.011 351 TYR GGG CD2 
7798  C CE1 . TYR G 22  ? 0.545 0.597 0.550 -0.015 0.013  -0.000 351 TYR GGG CE1 
7799  C CE2 . TYR G 22  ? 0.594 0.593 0.595 0.000  -0.013 -0.019 351 TYR GGG CE2 
7800  C CZ  . TYR G 22  ? 0.581 0.613 0.582 0.006  0.002  -0.013 351 TYR GGG CZ  
7801  O OH  . TYR G 22  ? 0.564 0.611 0.560 0.032  0.005  -0.016 351 TYR GGG OH  
7802  N N   . ALA G 23  ? 0.525 0.541 0.507 -0.027 0.013  -0.019 352 ALA GGG N   
7803  C CA  . ALA G 23  ? 0.564 0.576 0.534 -0.009 0.010  -0.032 352 ALA GGG CA  
7804  C C   . ALA G 23  ? 0.541 0.564 0.502 -0.011 0.020  -0.032 352 ALA GGG C   
7805  O O   . ALA G 23  ? 0.529 0.571 0.482 0.002  0.027  -0.035 352 ALA GGG O   
7806  C CB  . ALA G 23  ? 0.588 0.615 0.555 0.011  0.013  -0.034 352 ALA GGG CB  
7807  N N   . TRP G 24  ? 0.547 0.565 0.512 -0.026 0.022  -0.027 353 TRP GGG N   
7808  C CA  . TRP G 24  ? 0.541 0.567 0.500 -0.031 0.031  -0.025 353 TRP GGG CA  
7809  C C   . TRP G 24  ? 0.571 0.598 0.521 -0.018 0.029  -0.034 353 TRP GGG C   
7810  O O   . TRP G 24  ? 0.591 0.600 0.537 -0.011 0.016  -0.043 353 TRP GGG O   
7811  C CB  . TRP G 24  ? 0.515 0.533 0.476 -0.042 0.033  -0.019 353 TRP GGG CB  
7812  C CG  . TRP G 24  ? 0.507 0.515 0.479 -0.045 0.022  -0.015 353 TRP GGG CG  
7813  C CD1 . TRP G 24  ? 0.495 0.500 0.479 -0.050 0.015  -0.007 353 TRP GGG CD1 
7814  C CD2 . TRP G 24  ? 0.508 0.510 0.484 -0.045 0.015  -0.015 353 TRP GGG CD2 
7815  N NE1 . TRP G 24  ? 0.492 0.492 0.490 -0.056 0.003  0.002  353 TRP GGG NE1 
7816  C CE2 . TRP G 24  ? 0.510 0.507 0.502 -0.053 0.001  -0.003 353 TRP GGG CE2 
7817  C CE3 . TRP G 24  ? 0.542 0.545 0.509 -0.041 0.017  -0.020 353 TRP GGG CE3 
7818  C CZ2 . TRP G 24  ? 0.534 0.525 0.537 -0.059 -0.013 0.005  353 TRP GGG CZ2 
7819  C CZ3 . TRP G 24  ? 0.551 0.547 0.525 -0.045 0.004  -0.016 353 TRP GGG CZ3 
7820  C CH2 . TRP G 24  ? 0.527 0.516 0.519 -0.055 -0.011 -0.003 353 TRP GGG CH2 
7821  N N   . ASN G 25  ? 0.572 0.618 0.518 -0.017 0.038  -0.031 354 ASN GGG N   
7822  C CA  . ASN G 25  ? 0.570 0.625 0.504 -0.003 0.039  -0.037 354 ASN GGG CA  
7823  C C   . ASN G 25  ? 0.564 0.609 0.497 -0.012 0.037  -0.037 354 ASN GGG C   
7824  O O   . ASN G 25  ? 0.547 0.592 0.488 -0.025 0.043  -0.029 354 ASN GGG O   
7825  C CB  . ASN G 25  ? 0.565 0.657 0.501 0.002  0.049  -0.026 354 ASN GGG CB  
7826  C CG  . ASN G 25  ? 0.570 0.681 0.493 0.019  0.052  -0.029 354 ASN GGG CG  
7827  O OD1 . ASN G 25  ? 0.586 0.704 0.508 0.013  0.054  -0.025 354 ASN GGG OD1 
7828  N ND2 . ASN G 25  ? 0.600 0.718 0.508 0.044  0.050  -0.038 354 ASN GGG ND2 
7829  N N   . ARG G 26  ? 0.592 0.626 0.514 -0.002 0.027  -0.047 355 ARG GGG N   
7830  C CA  . ARG G 26  ? 0.601 0.630 0.522 -0.009 0.023  -0.045 355 ARG GGG CA  
7831  C C   . ARG G 26  ? 0.608 0.656 0.514 0.004  0.027  -0.049 355 ARG GGG C   
7832  O O   . ARG G 26  ? 0.582 0.625 0.467 0.024  0.020  -0.062 355 ARG GGG O   
7833  C CB  . ARG G 26  ? 0.630 0.629 0.544 -0.007 0.002  -0.054 355 ARG GGG CB  
7834  C CG  . ARG G 26  ? 0.630 0.618 0.565 -0.025 -0.007 -0.041 355 ARG GGG CG  
7835  C CD  . ARG G 26  ? 0.606 0.594 0.548 -0.034 -0.014 -0.032 355 ARG GGG CD  
7836  N NE  . ARG G 26  ? 0.622 0.623 0.587 -0.046 -0.004 -0.014 355 ARG GGG NE  
7837  C CZ  . ARG G 26  ? 0.596 0.596 0.582 -0.058 -0.015 0.003  355 ARG GGG CZ  
7838  N NH1 . ARG G 26  ? 0.645 0.627 0.635 -0.065 -0.041 0.007  355 ARG GGG NH1 
7839  N NH2 . ARG G 26  ? 0.593 0.612 0.594 -0.061 -0.001 0.019  355 ARG GGG NH2 
7840  N N   . LYS G 27  ? 0.581 0.645 0.494 -0.004 0.036  -0.039 356 LYS GGG N   
7841  C CA  . LYS G 27  ? 0.600 0.682 0.500 0.005  0.037  -0.039 356 LYS GGG CA  
7842  C C   . LYS G 27  ? 0.584 0.652 0.488 -0.006 0.030  -0.037 356 LYS GGG C   
7843  O O   . LYS G 27  ? 0.585 0.651 0.508 -0.020 0.035  -0.026 356 LYS GGG O   
7844  C CB  . LYS G 27  ? 0.600 0.720 0.509 0.004  0.051  -0.024 356 LYS GGG CB  
7845  C CG  . LYS G 27  ? 0.645 0.792 0.545 0.012  0.054  -0.018 356 LYS GGG CG  
7846  C CD  . LYS G 27  ? 0.690 0.884 0.601 0.013  0.065  0.002  356 LYS GGG CD  
7847  C CE  . LYS G 27  ? 0.737 0.963 0.642 0.020  0.067  0.011  356 LYS GGG CE  
7848  N NZ  . LYS G 27  ? 0.774 1.010 0.646 0.050  0.066  -0.004 356 LYS GGG NZ  
7849  N N   . ARG G 28  ? 0.579 0.638 0.465 0.004  0.017  -0.046 357 ARG GGG N   
7850  C CA  . ARG G 28  ? 0.607 0.659 0.497 -0.007 0.008  -0.041 357 ARG GGG CA  
7851  C C   . ARG G 28  ? 0.582 0.666 0.474 -0.006 0.021  -0.031 357 ARG GGG C   
7852  O O   . ARG G 28  ? 0.555 0.662 0.431 0.008  0.027  -0.033 357 ARG GGG O   
7853  C CB  . ARG G 28  ? 0.684 0.706 0.547 0.003  -0.017 -0.056 357 ARG GGG CB  
7854  C CG  . ARG G 28  ? 0.747 0.759 0.615 -0.010 -0.032 -0.048 357 ARG GGG CG  
7855  C CD  . ARG G 28  ? 0.842 0.812 0.687 -0.007 -0.066 -0.061 357 ARG GGG CD  
7856  N NE  . ARG G 28  ? 0.924 0.896 0.756 -0.009 -0.076 -0.058 357 ARG GGG NE  
7857  C CZ  . ARG G 28  ? 1.090 1.030 0.917 -0.020 -0.109 -0.056 357 ARG GGG CZ  
7858  N NH1 . ARG G 28  ? 1.179 1.081 1.013 -0.031 -0.136 -0.055 357 ARG GGG NH1 
7859  N NH2 . ARG G 28  ? 1.112 1.057 0.926 -0.022 -0.117 -0.053 357 ARG GGG NH2 
7860  N N   . ILE G 29  ? 0.580 0.668 0.492 -0.021 0.025  -0.017 358 ILE GGG N   
7861  C CA  . ILE G 29  ? 0.571 0.684 0.489 -0.024 0.033  -0.004 358 ILE GGG CA  
7862  C C   . ILE G 29  ? 0.579 0.684 0.498 -0.030 0.021  -0.000 358 ILE GGG C   
7863  O O   . ILE G 29  ? 0.562 0.652 0.498 -0.041 0.016  0.006  358 ILE GGG O   
7864  C CB  . ILE G 29  ? 0.549 0.666 0.488 -0.034 0.046  0.009  358 ILE GGG CB  
7865  C CG1 . ILE G 29  ? 0.551 0.678 0.489 -0.031 0.053  0.009  358 ILE GGG CG1 
7866  C CG2 . ILE G 29  ? 0.550 0.682 0.499 -0.040 0.050  0.024  358 ILE GGG CG2 
7867  C CD1 . ILE G 29  ? 0.565 0.678 0.514 -0.040 0.057  0.016  358 ILE GGG CD1 
7868  N N   . SER G 30  ? 0.573 0.693 0.476 -0.024 0.017  -0.001 359 SER GGG N   
7869  C CA  . SER G 30  ? 0.588 0.703 0.489 -0.030 0.003  0.004  359 SER GGG CA  
7870  C C   . SER G 30  ? 0.584 0.729 0.473 -0.024 0.007  0.009  359 SER GGG C   
7871  O O   . SER G 30  ? 0.575 0.744 0.452 -0.011 0.017  0.007  359 SER GGG O   
7872  C CB  . SER G 30  ? 0.621 0.703 0.503 -0.028 -0.022 -0.009 359 SER GGG CB  
7873  O OG  . SER G 30  ? 0.662 0.737 0.509 -0.007 -0.026 -0.030 359 SER GGG OG  
7874  N N   . ASN G 31  ? 0.600 0.748 0.495 -0.033 -0.002 0.019  360 ASN GGG N   
7875  C CA  . ASN G 31  ? 0.637 0.813 0.518 -0.027 -0.002 0.026  360 ASN GGG CA  
7876  C C   . ASN G 31  ? 0.606 0.820 0.503 -0.026 0.018  0.040  360 ASN GGG C   
7877  O O   . ASN G 31  ? 0.633 0.876 0.510 -0.010 0.023  0.039  360 ASN GGG O   
7878  C CB  . ASN G 31  ? 0.692 0.859 0.525 -0.007 -0.018 0.005  360 ASN GGG CB  
7879  C CG  . ASN G 31  ? 0.746 0.866 0.564 -0.013 -0.047 -0.007 360 ASN GGG CG  
7880  O OD1 . ASN G 31  ? 0.828 0.944 0.654 -0.027 -0.061 0.005  360 ASN GGG OD1 
7881  N ND2 . ASN G 31  ? 0.765 0.851 0.568 -0.006 -0.058 -0.024 360 ASN GGG ND2 
7882  N N   . CYS G 32  ? 0.574 0.785 0.504 -0.039 0.028  0.054  361 CYS GGG N   
7883  C CA  . CYS G 32  ? 0.565 0.800 0.514 -0.043 0.040  0.071  361 CYS GGG CA  
7884  C C   . CYS G 32  ? 0.539 0.758 0.517 -0.056 0.043  0.084  361 CYS GGG C   
7885  O O   . CYS G 32  ? 0.532 0.725 0.515 -0.058 0.041  0.080  361 CYS GGG O   
7886  C CB  . CYS G 32  ? 0.563 0.799 0.508 -0.037 0.047  0.064  361 CYS GGG CB  
7887  S SG  . CYS G 32  ? 0.610 0.801 0.557 -0.039 0.046  0.047  361 CYS GGG SG  
7888  N N   . VAL G 33  ? 0.533 0.767 0.527 -0.062 0.046  0.103  362 VAL GGG N   
7889  C CA  . VAL G 33  ? 0.545 0.756 0.560 -0.069 0.046  0.114  362 VAL GGG CA  
7890  C C   . VAL G 33  ? 0.557 0.741 0.570 -0.068 0.048  0.107  362 VAL GGG C   
7891  O O   . VAL G 33  ? 0.522 0.718 0.535 -0.072 0.046  0.111  362 VAL GGG O   
7892  C CB  . VAL G 33  ? 0.544 0.777 0.575 -0.077 0.042  0.138  362 VAL GGG CB  
7893  C CG1 . VAL G 33  ? 0.546 0.747 0.592 -0.080 0.039  0.146  362 VAL GGG CG1 
7894  C CG2 . VAL G 33  ? 0.540 0.807 0.570 -0.077 0.040  0.147  362 VAL GGG CG2 
7895  N N   . ALA G 34  ? 0.596 0.747 0.607 -0.063 0.051  0.098  363 ALA GGG N   
7896  C CA  . ALA G 34  ? 0.630 0.750 0.635 -0.060 0.052  0.089  363 ALA GGG CA  
7897  C C   . ALA G 34  ? 0.635 0.729 0.644 -0.061 0.045  0.099  363 ALA GGG C   
7898  O O   . ALA G 34  ? 0.672 0.745 0.680 -0.050 0.048  0.099  363 ALA GGG O   
7899  C CB  . ALA G 34  ? 0.592 0.695 0.590 -0.051 0.059  0.077  363 ALA GGG CB  
7900  N N   . ASP G 35  ? 0.639 0.734 0.652 -0.072 0.035  0.109  364 ASP GGG N   
7901  C CA  . ASP G 35  ? 0.661 0.717 0.674 -0.075 0.019  0.118  364 ASP GGG CA  
7902  C C   . ASP G 35  ? 0.673 0.690 0.667 -0.072 0.013  0.105  364 ASP GGG C   
7903  O O   . ASP G 35  ? 0.649 0.681 0.646 -0.084 0.008  0.108  364 ASP GGG O   
7904  C CB  . ASP G 35  ? 0.671 0.750 0.703 -0.093 0.005  0.144  364 ASP GGG CB  
7905  C CG  . ASP G 35  ? 0.707 0.739 0.741 -0.094 -0.015 0.153  364 ASP GGG CG  
7906  O OD1 . ASP G 35  ? 0.708 0.687 0.719 -0.078 -0.016 0.136  364 ASP GGG OD1 
7907  O OD2 . ASP G 35  ? 0.748 0.795 0.802 -0.109 -0.030 0.178  364 ASP GGG OD2 
7908  N N   . TYR G 36  ? 0.687 0.659 0.661 -0.055 0.014  0.092  365 TYR GGG N   
7909  C CA  . TYR G 36  ? 0.724 0.654 0.672 -0.048 0.009  0.076  365 TYR GGG CA  
7910  C C   . TYR G 36  ? 0.770 0.647 0.706 -0.054 -0.019 0.081  365 TYR GGG C   
7911  O O   . TYR G 36  ? 0.793 0.630 0.704 -0.051 -0.030 0.069  365 TYR GGG O   
7912  C CB  . TYR G 36  ? 0.730 0.644 0.658 -0.021 0.025  0.061  365 TYR GGG CB  
7913  C CG  . TYR G 36  ? 0.672 0.630 0.613 -0.020 0.045  0.057  365 TYR GGG CG  
7914  C CD1 . TYR G 36  ? 0.653 0.647 0.613 -0.020 0.055  0.066  365 TYR GGG CD1 
7915  C CD2 . TYR G 36  ? 0.693 0.653 0.625 -0.022 0.049  0.047  365 TYR GGG CD2 
7916  C CE1 . TYR G 36  ? 0.619 0.645 0.589 -0.022 0.066  0.065  365 TYR GGG CE1 
7917  C CE2 . TYR G 36  ? 0.672 0.667 0.616 -0.022 0.062  0.045  365 TYR GGG CE2 
7918  C CZ  . TYR G 36  ? 0.636 0.660 0.598 -0.023 0.068  0.053  365 TYR GGG CZ  
7919  O OH  . TYR G 36  ? 0.660 0.709 0.632 -0.025 0.073  0.053  365 TYR GGG OH  
7920  N N   . SER G 37  ? 0.774 0.649 0.726 -0.066 -0.035 0.100  366 SER GGG N   
7921  C CA  . SER G 37  ? 0.851 0.668 0.793 -0.075 -0.070 0.109  366 SER GGG CA  
7922  C C   . SER G 37  ? 0.850 0.674 0.800 -0.100 -0.088 0.120  366 SER GGG C   
7923  O O   . SER G 37  ? 0.930 0.694 0.861 -0.106 -0.119 0.119  366 SER GGG O   
7924  C CB  . SER G 37  ? 0.856 0.670 0.818 -0.084 -0.086 0.130  366 SER GGG CB  
7925  O OG  . SER G 37  ? 0.810 0.699 0.809 -0.100 -0.073 0.151  366 SER GGG OG  
7926  N N   . VAL G 38  ? 0.819 0.709 0.793 -0.112 -0.071 0.128  367 VAL GGG N   
7927  C CA  . VAL G 38  ? 0.825 0.729 0.807 -0.131 -0.084 0.140  367 VAL GGG CA  
7928  C C   . VAL G 38  ? 0.833 0.682 0.779 -0.120 -0.088 0.115  367 VAL GGG C   
7929  O O   . VAL G 38  ? 0.904 0.715 0.842 -0.135 -0.118 0.123  367 VAL GGG O   
7930  C CB  . VAL G 38  ? 0.801 0.788 0.810 -0.136 -0.060 0.151  367 VAL GGG CB  
7931  C CG1 . VAL G 38  ? 0.774 0.776 0.767 -0.116 -0.030 0.123  367 VAL GGG CG1 
7932  C CG2 . VAL G 38  ? 0.824 0.840 0.852 -0.157 -0.075 0.176  367 VAL GGG CG2 
7933  N N   . LEU G 39  ? 0.800 0.644 0.723 -0.095 -0.063 0.087  368 LEU GGG N   
7934  C CA  . LEU G 39  ? 0.802 0.600 0.688 -0.080 -0.063 0.063  368 LEU GGG CA  
7935  C C   . LEU G 39  ? 0.869 0.586 0.716 -0.065 -0.087 0.052  368 LEU GGG C   
7936  O O   . LEU G 39  ? 0.938 0.605 0.752 -0.063 -0.106 0.040  368 LEU GGG O   
7937  C CB  . LEU G 39  ? 0.762 0.590 0.644 -0.058 -0.029 0.046  368 LEU GGG CB  
7938  C CG  . LEU G 39  ? 0.712 0.607 0.623 -0.068 -0.009 0.052  368 LEU GGG CG  
7939  C CD1 . LEU G 39  ? 0.661 0.577 0.569 -0.051 0.016  0.038  368 LEU GGG CD1 
7940  C CD2 . LEU G 39  ? 0.711 0.615 0.628 -0.085 -0.020 0.058  368 LEU GGG CD2 
7941  N N   . TYR G 40  ? 0.893 0.593 0.738 -0.053 -0.089 0.054  369 TYR GGG N   
7942  C CA  . TYR G 40  ? 0.990 0.607 0.792 -0.031 -0.111 0.040  369 TYR GGG CA  
7943  C C   . TYR G 40  ? 1.056 0.612 0.847 -0.055 -0.160 0.051  369 TYR GGG C   
7944  O O   . TYR G 40  ? 1.135 0.607 0.875 -0.036 -0.186 0.033  369 TYR GGG O   
7945  C CB  . TYR G 40  ? 0.992 0.611 0.803 -0.016 -0.105 0.046  369 TYR GGG CB  
7946  C CG  . TYR G 40  ? 0.959 0.624 0.775 0.011  -0.064 0.038  369 TYR GGG CG  
7947  C CD1 . TYR G 40  ? 0.954 0.630 0.748 0.034  -0.040 0.021  369 TYR GGG CD1 
7948  C CD2 . TYR G 40  ? 0.948 0.648 0.793 0.011  -0.052 0.053  369 TYR GGG CD2 
7949  C CE1 . TYR G 40  ? 0.936 0.661 0.743 0.054  -0.007 0.021  369 TYR GGG CE1 
7950  C CE2 . TYR G 40  ? 0.920 0.665 0.775 0.032  -0.020 0.051  369 TYR GGG CE2 
7951  C CZ  . TYR G 40  ? 0.939 0.696 0.776 0.052  0.002  0.037  369 TYR GGG CZ  
7952  O OH  . TYR G 40  ? 0.908 0.712 0.759 0.069  0.030  0.042  369 TYR GGG OH  
7953  N N   . ASN G 41  ? 1.043 0.641 0.880 -0.093 -0.175 0.082  370 ASN GGG N   
7954  C CA  . ASN G 41  ? 1.126 0.679 0.969 -0.124 -0.226 0.105  370 ASN GGG CA  
7955  C C   . ASN G 41  ? 1.154 0.703 0.993 -0.144 -0.242 0.109  370 ASN GGG C   
7956  O O   . ASN G 41  ? 1.181 0.705 1.033 -0.175 -0.285 0.135  370 ASN GGG O   
7957  C CB  . ASN G 41  ? 1.073 0.685 0.975 -0.154 -0.233 0.146  370 ASN GGG CB  
7958  C CG  . ASN G 41  ? 1.080 0.682 0.984 -0.139 -0.228 0.146  370 ASN GGG CG  
7959  O OD1 . ASN G 41  ? 1.161 0.683 1.024 -0.115 -0.245 0.126  370 ASN GGG OD1 
7960  N ND2 . ASN G 41  ? 1.019 0.701 0.967 -0.148 -0.204 0.167  370 ASN GGG ND2 
7961  N N   . SER G 42  ? 1.157 0.730 0.980 -0.127 -0.210 0.087  371 SER GGG N   
7962  C CA  . SER G 42  ? 1.197 0.758 1.007 -0.139 -0.223 0.084  371 SER GGG CA  
7963  C C   . SER G 42  ? 1.302 0.765 1.042 -0.114 -0.244 0.051  371 SER GGG C   
7964  O O   . SER G 42  ? 1.336 0.784 1.042 -0.075 -0.218 0.023  371 SER GGG O   
7965  C CB  . SER G 42  ? 1.141 0.779 0.971 -0.134 -0.180 0.079  371 SER GGG CB  
7966  O OG  . SER G 42  ? 1.077 0.800 0.960 -0.147 -0.158 0.103  371 SER GGG OG  
7967  N N   . ALA G 43  ? 1.372 0.772 1.091 -0.134 -0.292 0.058  372 ALA GGG N   
7968  C CA  . ALA G 43  ? 1.414 0.714 1.058 -0.111 -0.320 0.026  372 ALA GGG CA  
7969  C C   . ALA G 43  ? 1.358 0.675 0.994 -0.119 -0.315 0.021  372 ALA GGG C   
7970  O O   . ALA G 43  ? 1.462 0.705 1.035 -0.102 -0.336 -0.004 372 ALA GGG O   
7971  C CB  . ALA G 43  ? 1.495 0.701 1.117 -0.130 -0.386 0.037  372 ALA GGG CB  
7972  N N   . SER G 44  ? 1.220 0.632 0.914 -0.141 -0.287 0.044  373 SER GGG N   
7973  C CA  . SER G 44  ? 1.181 0.621 0.880 -0.154 -0.281 0.046  373 SER GGG CA  
7974  C C   . SER G 44  ? 1.137 0.606 0.815 -0.119 -0.234 0.016  373 SER GGG C   
7975  O O   . SER G 44  ? 1.135 0.602 0.797 -0.122 -0.235 0.010  373 SER GGG O   
7976  C CB  . SER G 44  ? 1.114 0.641 0.883 -0.189 -0.275 0.086  373 SER GGG CB  
7977  O OG  . SER G 44  ? 1.162 0.659 0.946 -0.226 -0.328 0.119  373 SER GGG OG  
7978  N N   . PHE G 45  ? 0.656 0.549 0.513 -0.095 -0.009 -0.018 374 PHE GGG N   
7979  C CA  . PHE G 45  ? 0.638 0.545 0.498 -0.084 -0.005 -0.022 374 PHE GGG CA  
7980  C C   . PHE G 45  ? 0.670 0.553 0.506 -0.083 -0.009 -0.029 374 PHE GGG C   
7981  O O   . PHE G 45  ? 0.708 0.559 0.520 -0.081 -0.007 -0.032 374 PHE GGG O   
7982  C CB  . PHE G 45  ? 0.628 0.543 0.493 -0.070 0.005  -0.022 374 PHE GGG CB  
7983  C CG  . PHE G 45  ? 0.616 0.553 0.498 -0.070 0.008  -0.017 374 PHE GGG CG  
7984  C CD1 . PHE G 45  ? 0.578 0.540 0.480 -0.076 0.007  -0.014 374 PHE GGG CD1 
7985  C CD2 . PHE G 45  ? 0.613 0.546 0.491 -0.062 0.013  -0.014 374 PHE GGG CD2 
7986  C CE1 . PHE G 45  ? 0.561 0.540 0.473 -0.075 0.013  -0.011 374 PHE GGG CE1 
7987  C CE2 . PHE G 45  ? 0.590 0.542 0.478 -0.062 0.016  -0.010 374 PHE GGG CE2 
7988  C CZ  . PHE G 45  ? 0.558 0.532 0.461 -0.069 0.017  -0.009 374 PHE GGG CZ  
7989  N N   . SER G 46  ? 0.662 0.556 0.501 -0.084 -0.013 -0.030 375 SER GGG N   
7990  C CA  . SER G 46  ? 0.694 0.565 0.504 -0.083 -0.015 -0.036 375 SER GGG CA  
7991  C C   . SER G 46  ? 0.688 0.553 0.490 -0.067 -0.001 -0.039 375 SER GGG C   
7992  O O   . SER G 46  ? 0.721 0.557 0.493 -0.063 0.002  -0.045 375 SER GGG O   
7993  C CB  . SER G 46  ? 0.679 0.565 0.496 -0.089 -0.025 -0.033 375 SER GGG CB  
7994  O OG  . SER G 46  ? 0.651 0.569 0.496 -0.082 -0.020 -0.030 375 SER GGG OG  
7995  N N   . THR G 47  ? 0.643 0.533 0.469 -0.058 0.006  -0.036 376 THR GGG N   
7996  C CA  . THR G 47  ? 0.642 0.535 0.471 -0.043 0.019  -0.037 376 THR GGG CA  
7997  C C   . THR G 47  ? 0.621 0.535 0.474 -0.038 0.022  -0.034 376 THR GGG C   
7998  O O   . THR G 47  ? 0.600 0.533 0.470 -0.043 0.017  -0.031 376 THR GGG O   
7999  C CB  . THR G 47  ? 0.643 0.546 0.473 -0.041 0.020  -0.037 376 THR GGG CB  
8000  O OG1 . THR G 47  ? 0.705 0.605 0.533 -0.029 0.033  -0.038 376 THR GGG OG1 
8001  C CG2 . THR G 47  ? 0.609 0.543 0.467 -0.044 0.016  -0.033 376 THR GGG CG2 
8002  N N   . PHE G 48  ? 0.603 0.513 0.458 -0.026 0.031  -0.034 377 PHE GGG N   
8003  C CA  . PHE G 48  ? 0.584 0.511 0.459 -0.020 0.032  -0.030 377 PHE GGG CA  
8004  C C   . PHE G 48  ? 0.558 0.486 0.441 -0.007 0.042  -0.029 377 PHE GGG C   
8005  O O   . PHE G 48  ? 0.593 0.501 0.467 0.001  0.047  -0.029 377 PHE GGG O   
8006  C CB  . PHE G 48  ? 0.611 0.527 0.481 -0.024 0.028  -0.027 377 PHE GGG CB  
8007  C CG  . PHE G 48  ? 0.609 0.538 0.493 -0.018 0.027  -0.022 377 PHE GGG CG  
8008  C CD1 . PHE G 48  ? 0.605 0.554 0.508 -0.010 0.029  -0.020 377 PHE GGG CD1 
8009  C CD2 . PHE G 48  ? 0.626 0.547 0.504 -0.023 0.024  -0.017 377 PHE GGG CD2 
8010  C CE1 . PHE G 48  ? 0.611 0.571 0.523 -0.006 0.025  -0.016 377 PHE GGG CE1 
8011  C CE2 . PHE G 48  ? 0.629 0.560 0.514 -0.018 0.021  -0.012 377 PHE GGG CE2 
8012  C CZ  . PHE G 48  ? 0.626 0.576 0.527 -0.010 0.021  -0.011 377 PHE GGG CZ  
8013  N N   . LYS G 49  ? 0.563 0.511 0.462 -0.004 0.044  -0.029 378 LYS GGG N   
8014  C CA  . LYS G 49  ? 0.577 0.529 0.488 0.008  0.055  -0.027 378 LYS GGG CA  
8015  C C   . LYS G 49  ? 0.546 0.526 0.488 0.010  0.051  -0.023 378 LYS GGG C   
8016  O O   . LYS G 49  ? 0.549 0.544 0.498 0.002  0.044  -0.024 378 LYS GGG O   
8017  C CB  . LYS G 49  ? 0.586 0.535 0.490 0.008  0.062  -0.029 378 LYS GGG CB  
8018  C CG  . LYS G 49  ? 0.630 0.548 0.498 0.005  0.065  -0.033 378 LYS GGG CG  
8019  C CD  . LYS G 49  ? 0.621 0.539 0.481 0.005  0.072  -0.034 378 LYS GGG CD  
8020  C CE  . LYS G 49  ? 0.681 0.566 0.500 0.004  0.076  -0.039 378 LYS GGG CE  
8021  N NZ  . LYS G 49  ? 0.698 0.585 0.508 0.004  0.083  -0.037 378 LYS GGG NZ  
8022  N N   . CYS G 50  ? 0.525 0.511 0.484 0.020  0.055  -0.019 379 CYS GGG N   
8023  C CA  . CYS G 50  ? 0.501 0.514 0.491 0.022  0.050  -0.015 379 CYS GGG CA  
8024  C C   . CYS G 50  ? 0.489 0.512 0.500 0.028  0.061  -0.012 379 CYS GGG C   
8025  O O   . CYS G 50  ? 0.472 0.481 0.473 0.036  0.075  -0.012 379 CYS GGG O   
8026  C CB  . CYS G 50  ? 0.540 0.554 0.537 0.026  0.042  -0.011 379 CYS GGG CB  
8027  S SG  . CYS G 50  ? 0.601 0.603 0.572 0.016  0.032  -0.013 379 CYS GGG SG  
8028  N N   . TYR G 51  ? 0.476 0.522 0.513 0.025  0.056  -0.009 380 TYR GGG N   
8029  C CA  . TYR G 51  ? 0.467 0.530 0.532 0.029  0.065  -0.005 380 TYR GGG CA  
8030  C C   . TYR G 51  ? 0.459 0.544 0.558 0.031  0.054  0.001  380 TYR GGG C   
8031  O O   . TYR G 51  ? 0.504 0.596 0.604 0.023  0.039  -0.002 380 TYR GGG O   
8032  C CB  . TYR G 51  ? 0.461 0.526 0.521 0.020  0.066  -0.007 380 TYR GGG CB  
8033  C CG  . TYR G 51  ? 0.471 0.514 0.496 0.017  0.071  -0.012 380 TYR GGG CG  
8034  C CD1 . TYR G 51  ? 0.481 0.515 0.485 0.010  0.061  -0.017 380 TYR GGG CD1 
8035  C CD2 . TYR G 51  ? 0.485 0.516 0.497 0.022  0.086  -0.010 380 TYR GGG CD2 
8036  C CE1 . TYR G 51  ? 0.488 0.502 0.462 0.006  0.063  -0.020 380 TYR GGG CE1 
8037  C CE2 . TYR G 51  ? 0.496 0.505 0.473 0.018  0.088  -0.014 380 TYR GGG CE2 
8038  C CZ  . TYR G 51  ? 0.493 0.495 0.453 0.010  0.075  -0.019 380 TYR GGG CZ  
8039  O OH  . TYR G 51  ? 0.540 0.521 0.468 0.006  0.075  -0.022 380 TYR GGG OH  
8040  N N   . GLY G 52  ? 0.441 0.537 0.568 0.040  0.062  0.008  381 GLY GGG N   
8041  C CA  . GLY G 52  ? 0.445 0.565 0.609 0.041  0.049  0.015  381 GLY GGG CA  
8042  C C   . GLY G 52  ? 0.482 0.596 0.640 0.047  0.038  0.017  381 GLY GGG C   
8043  O O   . GLY G 52  ? 0.539 0.672 0.730 0.051  0.028  0.025  381 GLY GGG O   
8044  N N   . VAL G 53  ? 0.493 0.582 0.614 0.047  0.038  0.012  382 VAL GGG N   
8045  C CA  . VAL G 53  ? 0.522 0.602 0.636 0.053  0.029  0.015  382 VAL GGG CA  
8046  C C   . VAL G 53  ? 0.525 0.575 0.606 0.057  0.041  0.012  382 VAL GGG C   
8047  O O   . VAL G 53  ? 0.529 0.566 0.585 0.051  0.047  0.004  382 VAL GGG O   
8048  C CB  . VAL G 53  ? 0.537 0.619 0.637 0.042  0.010  0.014  382 VAL GGG CB  
8049  C CG1 . VAL G 53  ? 0.547 0.654 0.677 0.038  -0.005 0.018  382 VAL GGG CG1 
8050  C CG2 . VAL G 53  ? 0.533 0.603 0.601 0.031  0.011  0.004  382 VAL GGG CG2 
8051  N N   . SER G 54  ? 0.560 0.598 0.641 0.067  0.041  0.017  383 SER GGG N   
8052  C CA  . SER G 54  ? 0.608 0.614 0.657 0.071  0.050  0.013  383 SER GGG CA  
8053  C C   . SER G 54  ? 0.612 0.605 0.631 0.059  0.037  0.010  383 SER GGG C   
8054  O O   . SER G 54  ? 0.590 0.593 0.613 0.056  0.022  0.015  383 SER GGG O   
8055  C CB  . SER G 54  ? 0.650 0.645 0.711 0.087  0.055  0.020  383 SER GGG CB  
8056  O OG  . SER G 54  ? 0.764 0.724 0.791 0.088  0.061  0.015  383 SER GGG OG  
8057  N N   . PRO G 55  ? 0.651 0.622 0.639 0.051  0.042  0.003  384 PRO GGG N   
8058  C CA  . PRO G 55  ? 0.676 0.635 0.639 0.040  0.033  0.002  384 PRO GGG CA  
8059  C C   . PRO G 55  ? 0.715 0.661 0.674 0.045  0.026  0.010  384 PRO GGG C   
8060  O O   . PRO G 55  ? 0.711 0.656 0.657 0.037  0.016  0.012  384 PRO GGG O   
8061  C CB  . PRO G 55  ? 0.693 0.628 0.629 0.035  0.041  -0.006 384 PRO GGG CB  
8062  C CG  . PRO G 55  ? 0.673 0.615 0.617 0.038  0.052  -0.010 384 PRO GGG CG  
8063  C CD  . PRO G 55  ? 0.664 0.621 0.638 0.052  0.056  -0.004 384 PRO GGG CD  
8064  N N   . THR G 56  ? 0.719 0.654 0.688 0.060  0.032  0.014  385 THR GGG N   
8065  C CA  . THR G 56  ? 0.737 0.656 0.704 0.067  0.026  0.023  385 THR GGG CA  
8066  C C   . THR G 56  ? 0.700 0.643 0.686 0.068  0.011  0.033  385 THR GGG C   
8067  O O   . THR G 56  ? 0.730 0.662 0.711 0.072  0.002  0.042  385 THR GGG O   
8068  C CB  . THR G 56  ? 0.760 0.661 0.736 0.084  0.039  0.025  385 THR GGG CB  
8069  O OG1 . THR G 56  ? 0.740 0.668 0.753 0.096  0.043  0.028  385 THR GGG OG1 
8070  C CG2 . THR G 56  ? 0.747 0.618 0.696 0.083  0.053  0.014  385 THR GGG CG2 
8071  N N   . LYS G 57  ? 0.679 0.653 0.686 0.065  0.006  0.031  386 LYS GGG N   
8072  C CA  . LYS G 57  ? 0.684 0.680 0.711 0.067  -0.011 0.040  386 LYS GGG CA  
8073  C C   . LYS G 57  ? 0.610 0.615 0.619 0.051  -0.022 0.036  386 LYS GGG C   
8074  O O   . LYS G 57  ? 0.600 0.620 0.618 0.050  -0.037 0.041  386 LYS GGG O   
8075  C CB  . LYS G 57  ? 0.718 0.741 0.787 0.074  -0.008 0.042  386 LYS GGG CB  
8076  C CG  . LYS G 57  ? 0.798 0.816 0.890 0.092  0.004  0.048  386 LYS GGG CG  
8077  C CD  . LYS G 57  ? 0.863 0.897 0.987 0.101  -0.011 0.061  386 LYS GGG CD  
8078  C CE  . LYS G 57  ? 0.890 0.961 1.054 0.099  -0.018 0.064  386 LYS GGG CE  
8079  N NZ  . LYS G 57  ? 0.921 1.008 1.097 0.097  -0.044 0.074  386 LYS GGG NZ  
8080  N N   . LEU G 58  ? 0.570 0.566 0.554 0.041  -0.015 0.027  387 LEU GGG N   
8081  C CA  . LEU G 58  ? 0.570 0.577 0.542 0.028  -0.022 0.021  387 LEU GGG CA  
8082  C C   . LEU G 58  ? 0.573 0.577 0.527 0.025  -0.036 0.028  387 LEU GGG C   
8083  O O   . LEU G 58  ? 0.559 0.576 0.511 0.019  -0.046 0.026  387 LEU GGG O   
8084  C CB  . LEU G 58  ? 0.556 0.555 0.509 0.019  -0.011 0.013  387 LEU GGG CB  
8085  C CG  . LEU G 58  ? 0.544 0.546 0.508 0.020  -0.000 0.006  387 LEU GGG CG  
8086  C CD1 . LEU G 58  ? 0.532 0.526 0.478 0.010  0.007  -0.001 387 LEU GGG CD1 
8087  C CD2 . LEU G 58  ? 0.546 0.572 0.535 0.020  -0.003 0.003  387 LEU GGG CD2 
8088  N N   . ASN G 59  ? 0.608 0.593 0.547 0.028  -0.038 0.037  388 ASN GGG N   
8089  C CA  . ASN G 59  ? 0.671 0.650 0.588 0.025  -0.051 0.045  388 ASN GGG CA  
8090  C C   . ASN G 59  ? 0.676 0.668 0.611 0.032  -0.069 0.054  388 ASN GGG C   
8091  O O   . ASN G 59  ? 0.721 0.708 0.635 0.029  -0.082 0.061  388 ASN GGG O   
8092  C CB  . ASN G 59  ? 0.702 0.654 0.596 0.025  -0.046 0.053  388 ASN GGG CB  
8093  C CG  . ASN G 59  ? 0.733 0.676 0.602 0.012  -0.036 0.047  388 ASN GGG CG  
8094  O OD1 . ASN G 59  ? 0.726 0.683 0.591 0.004  -0.034 0.039  388 ASN GGG OD1 
8095  N ND2 . ASN G 59  ? 0.817 0.737 0.672 0.010  -0.029 0.051  388 ASN GGG ND2 
8096  N N   . ASP G 60  ? 0.690 0.699 0.663 0.041  -0.069 0.054  389 ASP GGG N   
8097  C CA  . ASP G 60  ? 0.718 0.744 0.718 0.048  -0.087 0.065  389 ASP GGG CA  
8098  C C   . ASP G 60  ? 0.657 0.709 0.682 0.043  -0.094 0.058  389 ASP GGG C   
8099  O O   . ASP G 60  ? 0.660 0.731 0.717 0.048  -0.107 0.066  389 ASP GGG O   
8100  C CB  . ASP G 60  ? 0.766 0.792 0.800 0.065  -0.081 0.073  389 ASP GGG CB  
8101  C CG  . ASP G 60  ? 0.857 0.852 0.870 0.071  -0.073 0.079  389 ASP GGG CG  
8102  O OD1 . ASP G 60  ? 0.929 0.912 0.919 0.069  -0.086 0.089  389 ASP GGG OD1 
8103  O OD2 . ASP G 60  ? 0.898 0.880 0.914 0.076  -0.055 0.074  389 ASP GGG OD2 
8104  N N   . LEU G 61  ? 0.620 0.674 0.632 0.033  -0.086 0.045  390 LEU GGG N   
8105  C CA  . LEU G 61  ? 0.604 0.680 0.639 0.027  -0.091 0.038  390 LEU GGG CA  
8106  C C   . LEU G 61  ? 0.594 0.667 0.599 0.015  -0.104 0.032  390 LEU GGG C   
8107  O O   . LEU G 61  ? 0.609 0.665 0.575 0.010  -0.100 0.029  390 LEU GGG O   
8108  C CB  . LEU G 61  ? 0.597 0.676 0.643 0.026  -0.071 0.029  390 LEU GGG CB  
8109  C CG  . LEU G 61  ? 0.637 0.714 0.704 0.038  -0.054 0.033  390 LEU GGG CG  
8110  C CD1 . LEU G 61  ? 0.611 0.686 0.676 0.034  -0.036 0.023  390 LEU GGG CD1 
8111  C CD2 . LEU G 61  ? 0.657 0.755 0.769 0.048  -0.059 0.043  390 LEU GGG CD2 
8112  N N   . CYS G 62  ? 0.577 0.667 0.601 0.010  -0.119 0.030  391 CYS GGG N   
8113  C CA  . CYS G 62  ? 0.587 0.673 0.584 -0.002 -0.131 0.020  391 CYS GGG CA  
8114  C C   . CYS G 62  ? 0.538 0.636 0.559 -0.008 -0.124 0.010  391 CYS GGG C   
8115  O O   . CYS G 62  ? 0.528 0.644 0.591 -0.004 -0.124 0.014  391 CYS GGG O   
8116  C CB  . CYS G 62  ? 0.634 0.723 0.628 -0.005 -0.159 0.027  391 CYS GGG CB  
8117  S SG  . CYS G 62  ? 0.726 0.797 0.683 -0.001 -0.169 0.040  391 CYS GGG SG  
8118  N N   . PHE G 63  ? 0.531 0.618 0.524 -0.016 -0.119 -0.003 392 PHE GGG N   
8119  C CA  . PHE G 63  ? 0.522 0.615 0.529 -0.023 -0.114 -0.014 392 PHE GGG CA  
8120  C C   . PHE G 63  ? 0.550 0.631 0.525 -0.032 -0.126 -0.025 392 PHE GGG C   
8121  O O   . PHE G 63  ? 0.571 0.637 0.507 -0.033 -0.133 -0.025 392 PHE GGG O   
8122  C CB  . PHE G 63  ? 0.503 0.593 0.510 -0.020 -0.090 -0.019 392 PHE GGG CB  
8123  C CG  . PHE G 63  ? 0.481 0.579 0.515 -0.011 -0.079 -0.010 392 PHE GGG CG  
8124  C CD1 . PHE G 63  ? 0.486 0.601 0.561 -0.008 -0.079 -0.005 392 PHE GGG CD1 
8125  C CD2 . PHE G 63  ? 0.461 0.547 0.478 -0.005 -0.067 -0.006 392 PHE GGG CD2 
8126  C CE1 . PHE G 63  ? 0.474 0.595 0.571 0.001  -0.065 0.002  392 PHE GGG CE1 
8127  C CE2 . PHE G 63  ? 0.479 0.568 0.516 0.003  -0.056 0.000  392 PHE GGG CE2 
8128  C CZ  . PHE G 63  ? 0.467 0.573 0.543 0.007  -0.054 0.004  392 PHE GGG CZ  
8129  N N   . THR G 64  ? 0.552 0.636 0.541 -0.039 -0.130 -0.034 393 THR GGG N   
8130  C CA  . THR G 64  ? 0.599 0.666 0.557 -0.048 -0.140 -0.047 393 THR GGG CA  
8131  C C   . THR G 64  ? 0.613 0.665 0.538 -0.047 -0.120 -0.057 393 THR GGG C   
8132  O O   . THR G 64  ? 0.651 0.684 0.533 -0.050 -0.122 -0.065 393 THR GGG O   
8133  C CB  . THR G 64  ? 0.592 0.666 0.579 -0.056 -0.148 -0.053 393 THR GGG CB  
8134  O OG1 . THR G 64  ? 0.568 0.665 0.603 -0.055 -0.155 -0.041 393 THR GGG OG1 
8135  C CG2 . THR G 64  ? 0.641 0.698 0.599 -0.066 -0.169 -0.064 393 THR GGG CG2 
8136  N N   . ASN G 65  ? 0.577 0.635 0.521 -0.042 -0.100 -0.055 394 ASN GGG N   
8137  C CA  . ASN G 65  ? 0.565 0.613 0.490 -0.040 -0.080 -0.063 394 ASN GGG CA  
8138  C C   . ASN G 65  ? 0.547 0.606 0.494 -0.034 -0.064 -0.055 394 ASN GGG C   
8139  O O   . ASN G 65  ? 0.544 0.615 0.523 -0.032 -0.065 -0.048 394 ASN GGG O   
8140  C CB  . ASN G 65  ? 0.583 0.625 0.511 -0.045 -0.077 -0.075 394 ASN GGG CB  
8141  C CG  . ASN G 65  ? 0.632 0.657 0.531 -0.051 -0.091 -0.086 394 ASN GGG CG  
8142  O OD1 . ASN G 65  ? 0.647 0.657 0.506 -0.050 -0.086 -0.091 394 ASN GGG OD1 
8143  N ND2 . ASN G 65  ? 0.646 0.673 0.563 -0.058 -0.107 -0.089 394 ASN GGG ND2 
8144  N N   . VAL G 66  ? 0.535 0.587 0.465 -0.032 -0.049 -0.057 395 VAL GGG N   
8145  C CA  . VAL G 66  ? 0.496 0.553 0.441 -0.029 -0.034 -0.053 395 VAL GGG CA  
8146  C C   . VAL G 66  ? 0.522 0.576 0.464 -0.030 -0.023 -0.061 395 VAL GGG C   
8147  O O   . VAL G 66  ? 0.545 0.590 0.464 -0.032 -0.021 -0.068 395 VAL GGG O   
8148  C CB  . VAL G 66  ? 0.496 0.549 0.426 -0.026 -0.030 -0.045 395 VAL GGG CB  
8149  C CG1 . VAL G 66  ? 0.480 0.536 0.422 -0.024 -0.017 -0.042 395 VAL GGG CG1 
8150  C CG2 . VAL G 66  ? 0.495 0.550 0.430 -0.023 -0.042 -0.036 395 VAL GGG CG2 
8151  N N   . TYR G 67  ? 0.518 0.578 0.482 -0.029 -0.016 -0.060 396 TYR GGG N   
8152  C CA  . TYR G 67  ? 0.540 0.599 0.508 -0.029 -0.005 -0.065 396 TYR GGG CA  
8153  C C   . TYR G 67  ? 0.524 0.587 0.496 -0.027 0.004  -0.059 396 TYR GGG C   
8154  O O   . TYR G 67  ? 0.505 0.571 0.486 -0.026 0.003  -0.052 396 TYR GGG O   
8155  C CB  . TYR G 67  ? 0.556 0.617 0.545 -0.030 -0.007 -0.069 396 TYR GGG CB  
8156  C CG  . TYR G 67  ? 0.579 0.634 0.564 -0.033 -0.017 -0.076 396 TYR GGG CG  
8157  C CD1 . TYR G 67  ? 0.601 0.643 0.564 -0.034 -0.016 -0.086 396 TYR GGG CD1 
8158  C CD2 . TYR G 67  ? 0.593 0.653 0.593 -0.036 -0.029 -0.073 396 TYR GGG CD2 
8159  C CE1 . TYR G 67  ? 0.648 0.680 0.601 -0.038 -0.028 -0.095 396 TYR GGG CE1 
8160  C CE2 . TYR G 67  ? 0.617 0.670 0.613 -0.041 -0.043 -0.079 396 TYR GGG CE2 
8161  C CZ  . TYR G 67  ? 0.648 0.686 0.618 -0.043 -0.043 -0.091 396 TYR GGG CZ  
8162  O OH  . TYR G 67  ? 0.719 0.747 0.681 -0.049 -0.058 -0.098 396 TYR GGG OH  
8163  N N   . ALA G 68  ? 0.527 0.588 0.490 -0.027 0.013  -0.060 397 ALA GGG N   
8164  C CA  . ALA G 68  ? 0.530 0.595 0.497 -0.028 0.020  -0.055 397 ALA GGG CA  
8165  C C   . ALA G 68  ? 0.534 0.604 0.518 -0.027 0.025  -0.057 397 ALA GGG C   
8166  O O   . ALA G 68  ? 0.552 0.622 0.534 -0.026 0.031  -0.062 397 ALA GGG O   
8167  C CB  . ALA G 68  ? 0.563 0.626 0.514 -0.030 0.025  -0.052 397 ALA GGG CB  
8168  N N   . ASP G 69  ? 0.536 0.608 0.534 -0.027 0.023  -0.053 398 ASP GGG N   
8169  C CA  . ASP G 69  ? 0.489 0.565 0.503 -0.026 0.026  -0.052 398 ASP GGG CA  
8170  C C   . ASP G 69  ? 0.469 0.548 0.483 -0.029 0.027  -0.046 398 ASP GGG C   
8171  O O   . ASP G 69  ? 0.493 0.568 0.498 -0.031 0.025  -0.042 398 ASP GGG O   
8172  C CB  . ASP G 69  ? 0.497 0.571 0.522 -0.025 0.022  -0.051 398 ASP GGG CB  
8173  C CG  . ASP G 69  ? 0.541 0.612 0.569 -0.025 0.018  -0.056 398 ASP GGG CG  
8174  O OD1 . ASP G 69  ? 0.521 0.589 0.543 -0.024 0.019  -0.063 398 ASP GGG OD1 
8175  O OD2 . ASP G 69  ? 0.556 0.627 0.592 -0.026 0.015  -0.053 398 ASP GGG OD2 
8176  N N   . SER G 70  ? 0.444 0.531 0.471 -0.029 0.031  -0.045 399 SER GGG N   
8177  C CA  . SER G 70  ? 0.411 0.503 0.442 -0.033 0.030  -0.038 399 SER GGG CA  
8178  C C   . SER G 70  ? 0.407 0.508 0.460 -0.032 0.029  -0.035 399 SER GGG C   
8179  O O   . SER G 70  ? 0.404 0.508 0.469 -0.027 0.033  -0.039 399 SER GGG O   
8180  C CB  . SER G 70  ? 0.400 0.496 0.426 -0.036 0.036  -0.037 399 SER GGG CB  
8181  O OG  . SER G 70  ? 0.389 0.490 0.420 -0.032 0.045  -0.042 399 SER GGG OG  
8182  N N   . PHE G 71  ? 0.439 0.541 0.495 -0.037 0.022  -0.028 400 PHE GGG N   
8183  C CA  . PHE G 71  ? 0.437 0.547 0.513 -0.037 0.016  -0.022 400 PHE GGG CA  
8184  C C   . PHE G 71  ? 0.437 0.545 0.508 -0.045 0.006  -0.015 400 PHE GGG C   
8185  O O   . PHE G 71  ? 0.422 0.519 0.472 -0.050 0.005  -0.016 400 PHE GGG O   
8186  C CB  . PHE G 71  ? 0.453 0.555 0.529 -0.032 0.013  -0.023 400 PHE GGG CB  
8187  C CG  . PHE G 71  ? 0.453 0.541 0.506 -0.034 0.011  -0.024 400 PHE GGG CG  
8188  C CD1 . PHE G 71  ? 0.490 0.570 0.530 -0.039 0.004  -0.018 400 PHE GGG CD1 
8189  C CD2 . PHE G 71  ? 0.441 0.524 0.488 -0.031 0.016  -0.029 400 PHE GGG CD2 
8190  C CE1 . PHE G 71  ? 0.498 0.565 0.518 -0.038 0.005  -0.019 400 PHE GGG CE1 
8191  C CE2 . PHE G 71  ? 0.442 0.515 0.475 -0.031 0.015  -0.029 400 PHE GGG CE2 
8192  C CZ  . PHE G 71  ? 0.463 0.528 0.482 -0.034 0.012  -0.024 400 PHE GGG CZ  
8193  N N   . VAL G 72  ? 0.463 0.578 0.550 -0.047 -0.002 -0.008 401 VAL GGG N   
8194  C CA  . VAL G 72  ? 0.473 0.585 0.554 -0.056 -0.016 -0.002 401 VAL GGG CA  
8195  C C   . VAL G 72  ? 0.501 0.602 0.571 -0.055 -0.025 0.002  401 VAL GGG C   
8196  O O   . VAL G 72  ? 0.462 0.568 0.548 -0.048 -0.024 0.004  401 VAL GGG O   
8197  C CB  . VAL G 72  ? 0.466 0.598 0.578 -0.061 -0.020 0.005  401 VAL GGG CB  
8198  C CG1 . VAL G 72  ? 0.473 0.602 0.582 -0.071 -0.039 0.013  401 VAL GGG CG1 
8199  C CG2 . VAL G 72  ? 0.487 0.627 0.605 -0.064 -0.010 0.003  401 VAL GGG CG2 
8200  N N   . ILE G 73  ? 0.567 0.650 0.608 -0.062 -0.033 0.002  402 ILE GGG N   
8201  C CA  . ILE G 73  ? 0.581 0.650 0.604 -0.063 -0.043 0.007  402 ILE GGG CA  
8202  C C   . ILE G 73  ? 0.610 0.667 0.612 -0.074 -0.058 0.010  402 ILE GGG C   
8203  O O   . ILE G 73  ? 0.585 0.645 0.591 -0.081 -0.059 0.008  402 ILE GGG O   
8204  C CB  . ILE G 73  ? 0.575 0.628 0.574 -0.057 -0.033 0.002  402 ILE GGG CB  
8205  C CG1 . ILE G 73  ? 0.613 0.654 0.590 -0.058 -0.025 -0.005 402 ILE GGG CG1 
8206  C CG2 . ILE G 73  ? 0.544 0.607 0.564 -0.048 -0.024 0.001  402 ILE GGG CG2 
8207  C CD1 . ILE G 73  ? 0.622 0.649 0.579 -0.053 -0.016 -0.008 402 ILE GGG CD1 
8208  N N   . ARG G 74  ? 0.641 0.682 0.619 -0.077 -0.069 0.014  403 ARG GGG N   
8209  C CA  . ARG G 74  ? 0.689 0.711 0.637 -0.089 -0.084 0.015  403 ARG GGG CA  
8210  C C   . ARG G 74  ? 0.689 0.685 0.599 -0.089 -0.074 0.005  403 ARG GGG C   
8211  O O   . ARG G 74  ? 0.651 0.643 0.554 -0.079 -0.058 0.001  403 ARG GGG O   
8212  C CB  . ARG G 74  ? 0.754 0.761 0.677 -0.090 -0.097 0.021  403 ARG GGG CB  
8213  C CG  . ARG G 74  ? 0.815 0.842 0.769 -0.092 -0.114 0.033  403 ARG GGG CG  
8214  C CD  . ARG G 74  ? 0.851 0.863 0.781 -0.090 -0.121 0.041  403 ARG GGG CD  
8215  N NE  . ARG G 74  ? 0.889 0.868 0.763 -0.097 -0.128 0.037  403 ARG GGG NE  
8216  C CZ  . ARG G 74  ? 0.958 0.916 0.796 -0.096 -0.131 0.042  403 ARG GGG CZ  
8217  N NH1 . ARG G 74  ? 0.987 0.954 0.841 -0.088 -0.128 0.051  403 ARG GGG NH1 
8218  N NH2 . ARG G 74  ? 1.031 0.957 0.815 -0.102 -0.136 0.038  403 ARG GGG NH2 
8219  N N   . GLY G 75  ? 0.694 0.672 0.581 -0.099 -0.084 0.003  404 GLY GGG N   
8220  C CA  . GLY G 75  ? 0.725 0.673 0.573 -0.099 -0.076 -0.007 404 GLY GGG CA  
8221  C C   . GLY G 75  ? 0.727 0.656 0.542 -0.091 -0.066 -0.009 404 GLY GGG C   
8222  O O   . GLY G 75  ? 0.712 0.635 0.522 -0.082 -0.048 -0.015 404 GLY GGG O   
8223  N N   . ASP G 76  ? 0.752 0.672 0.548 -0.092 -0.075 -0.004 405 ASP GGG N   
8224  C CA  . ASP G 76  ? 0.822 0.718 0.580 -0.085 -0.062 -0.006 405 ASP GGG CA  
8225  C C   . ASP G 76  ? 0.759 0.676 0.544 -0.074 -0.047 -0.002 405 ASP GGG C   
8226  O O   . ASP G 76  ? 0.805 0.708 0.567 -0.068 -0.034 -0.002 405 ASP GGG O   
8227  C CB  . ASP G 76  ? 0.903 0.772 0.615 -0.093 -0.076 -0.004 405 ASP GGG CB  
8228  C CG  . ASP G 76  ? 0.943 0.826 0.670 -0.099 -0.098 0.008  405 ASP GGG CG  
8229  O OD1 . ASP G 76  ? 0.939 0.853 0.712 -0.094 -0.096 0.015  405 ASP GGG OD1 
8230  O OD2 . ASP G 76  ? 0.975 0.838 0.669 -0.109 -0.117 0.010  405 ASP GGG OD2 
8231  N N   . GLU G 77  ? 0.678 0.625 0.510 -0.071 -0.046 0.001  406 GLU GGG N   
8232  C CA  . GLU G 77  ? 0.664 0.627 0.520 -0.062 -0.032 0.002  406 GLU GGG CA  
8233  C C   . GLU G 77  ? 0.633 0.601 0.500 -0.056 -0.017 -0.006 406 GLU GGG C   
8234  O O   . GLU G 77  ? 0.565 0.542 0.447 -0.049 -0.005 -0.005 406 GLU GGG O   
8235  C CB  . GLU G 77  ? 0.653 0.641 0.549 -0.061 -0.040 0.009  406 GLU GGG CB  
8236  C CG  . GLU G 77  ? 0.659 0.644 0.549 -0.064 -0.053 0.019  406 GLU GGG CG  
8237  C CD  . GLU G 77  ? 0.643 0.653 0.577 -0.062 -0.062 0.026  406 GLU GGG CD  
8238  O OE1 . GLU G 77  ? 0.609 0.637 0.573 -0.062 -0.060 0.022  406 GLU GGG OE1 
8239  O OE2 . GLU G 77  ? 0.637 0.646 0.573 -0.061 -0.071 0.035  406 GLU GGG OE2 
8240  N N   . VAL G 78  ? 0.675 0.636 0.534 -0.059 -0.018 -0.011 407 VAL GGG N   
8241  C CA  . VAL G 78  ? 0.644 0.609 0.514 -0.054 -0.006 -0.017 407 VAL GGG CA  
8242  C C   . VAL G 78  ? 0.626 0.581 0.482 -0.045 0.009  -0.019 407 VAL GGG C   
8243  O O   . VAL G 78  ? 0.586 0.555 0.464 -0.039 0.018  -0.020 407 VAL GGG O   
8244  C CB  . VAL G 78  ? 0.636 0.592 0.498 -0.060 -0.011 -0.021 407 VAL GGG CB  
8245  C CG1 . VAL G 78  ? 0.638 0.594 0.504 -0.053 0.001  -0.026 407 VAL GGG CG1 
8246  C CG2 . VAL G 78  ? 0.620 0.594 0.506 -0.068 -0.023 -0.018 407 VAL GGG CG2 
8247  N N   . ARG G 79  ? 0.650 0.582 0.473 -0.045 0.012  -0.019 408 ARG GGG N   
8248  C CA  . ARG G 79  ? 0.706 0.629 0.517 -0.036 0.030  -0.020 408 ARG GGG CA  
8249  C C   . ARG G 79  ? 0.647 0.592 0.488 -0.031 0.037  -0.014 408 ARG GGG C   
8250  O O   . ARG G 79  ? 0.661 0.607 0.507 -0.024 0.052  -0.013 408 ARG GGG O   
8251  C CB  . ARG G 79  ? 0.827 0.720 0.592 -0.037 0.032  -0.020 408 ARG GGG CB  
8252  C CG  . ARG G 79  ? 0.912 0.804 0.667 -0.042 0.023  -0.013 408 ARG GGG CG  
8253  C CD  . ARG G 79  ? 1.059 0.931 0.779 -0.039 0.035  -0.009 408 ARG GGG CD  
8254  N NE  . ARG G 79  ? 1.152 1.029 0.871 -0.043 0.026  0.001  408 ARG GGG NE  
8255  C CZ  . ARG G 79  ? 1.177 1.069 0.919 -0.039 0.033  0.010  408 ARG GGG CZ  
8256  N NH1 . ARG G 79  ? 1.228 1.136 0.999 -0.032 0.050  0.009  408 ARG GGG NH1 
8257  N NH2 . ARG G 79  ? 1.202 1.093 0.939 -0.044 0.023  0.019  408 ARG GGG NH2 
8258  N N   . GLN G 80  ? 0.593 0.552 0.453 -0.035 0.027  -0.009 409 GLN GGG N   
8259  C CA  . GLN G 80  ? 0.547 0.523 0.434 -0.032 0.032  -0.003 409 GLN GGG CA  
8260  C C   . GLN G 80  ? 0.503 0.499 0.424 -0.029 0.035  -0.007 409 GLN GGG C   
8261  O O   . GLN G 80  ? 0.475 0.482 0.418 -0.026 0.040  -0.004 409 GLN GGG O   
8262  C CB  . GLN G 80  ? 0.546 0.528 0.441 -0.036 0.020  0.003  409 GLN GGG CB  
8263  C CG  . GLN G 80  ? 0.583 0.545 0.445 -0.039 0.017  0.010  409 GLN GGG CG  
8264  C CD  . GLN G 80  ? 0.578 0.546 0.451 -0.042 0.003  0.018  409 GLN GGG CD  
8265  O OE1 . GLN G 80  ? 0.515 0.497 0.418 -0.040 0.005  0.022  409 GLN GGG OE1 
8266  N NE2 . GLN G 80  ? 0.597 0.551 0.443 -0.048 -0.010 0.022  409 GLN GGG NE2 
8267  N N   . ILE G 81  ? 0.495 0.494 0.419 -0.030 0.030  -0.013 410 ILE GGG N   
8268  C CA  . ILE G 81  ? 0.473 0.488 0.423 -0.027 0.032  -0.016 410 ILE GGG CA  
8269  C C   . ILE G 81  ? 0.494 0.505 0.441 -0.021 0.042  -0.018 410 ILE GGG C   
8270  O O   . ILE G 81  ? 0.503 0.510 0.444 -0.020 0.042  -0.022 410 ILE GGG O   
8271  C CB  . ILE G 81  ? 0.445 0.466 0.400 -0.031 0.023  -0.020 410 ILE GGG CB  
8272  C CG1 . ILE G 81  ? 0.447 0.471 0.404 -0.036 0.014  -0.017 410 ILE GGG CG1 
8273  C CG2 . ILE G 81  ? 0.417 0.452 0.393 -0.029 0.024  -0.023 410 ILE GGG CG2 
8274  C CD1 . ILE G 81  ? 0.443 0.476 0.419 -0.035 0.013  -0.013 410 ILE GGG CD1 
8275  N N   . ALA G 82  ? 0.519 0.533 0.474 -0.018 0.051  -0.014 411 ALA GGG N   
8276  C CA  . ALA G 82  ? 0.534 0.548 0.492 -0.011 0.063  -0.013 411 ALA GGG CA  
8277  C C   . ALA G 82  ? 0.540 0.565 0.520 -0.009 0.071  -0.007 411 ALA GGG C   
8278  O O   . ALA G 82  ? 0.571 0.594 0.549 -0.013 0.070  -0.003 411 ALA GGG O   
8279  C CB  . ALA G 82  ? 0.535 0.527 0.461 -0.007 0.071  -0.014 411 ALA GGG CB  
8280  N N   . PRO G 83  ? 0.542 0.579 0.546 -0.004 0.077  -0.005 412 PRO GGG N   
8281  C CA  . PRO G 83  ? 0.521 0.570 0.548 -0.004 0.086  0.002  412 PRO GGG CA  
8282  C C   . PRO G 83  ? 0.534 0.568 0.539 -0.002 0.101  0.007  412 PRO GGG C   
8283  O O   . PRO G 83  ? 0.603 0.623 0.582 0.003  0.108  0.005  412 PRO GGG O   
8284  C CB  . PRO G 83  ? 0.515 0.579 0.570 0.002  0.090  0.003  412 PRO GGG CB  
8285  C CG  . PRO G 83  ? 0.551 0.602 0.584 0.007  0.089  -0.002 412 PRO GGG CG  
8286  C CD  . PRO G 83  ? 0.541 0.583 0.554 0.001  0.076  -0.009 412 PRO GGG CD  
8287  N N   . GLY G 84  ? 0.531 0.569 0.545 -0.006 0.104  0.014  413 GLY GGG N   
8288  C CA  . GLY G 84  ? 0.555 0.582 0.550 -0.005 0.120  0.022  413 GLY GGG CA  
8289  C C   . GLY G 84  ? 0.591 0.595 0.544 -0.008 0.115  0.022  413 GLY GGG C   
8290  O O   . GLY G 84  ? 0.665 0.655 0.593 -0.007 0.128  0.028  413 GLY GGG O   
8291  N N   . GLN G 85  ? 0.589 0.589 0.533 -0.013 0.097  0.017  414 GLN GGG N   
8292  C CA  . GLN G 85  ? 0.621 0.602 0.528 -0.017 0.088  0.017  414 GLN GGG CA  
8293  C C   . GLN G 85  ? 0.606 0.589 0.521 -0.022 0.081  0.025  414 GLN GGG C   
8294  O O   . GLN G 85  ? 0.596 0.596 0.546 -0.023 0.078  0.027  414 GLN GGG O   
8295  C CB  . GLN G 85  ? 0.632 0.613 0.536 -0.019 0.072  0.008  414 GLN GGG CB  
8296  C CG  . GLN G 85  ? 0.672 0.643 0.560 -0.015 0.078  0.001  414 GLN GGG CG  
8297  C CD  . GLN G 85  ? 0.733 0.677 0.576 -0.013 0.086  0.000  414 GLN GGG CD  
8298  O OE1 . GLN G 85  ? 0.786 0.715 0.601 -0.018 0.079  0.003  414 GLN GGG OE1 
8299  N NE2 . GLN G 85  ? 0.763 0.698 0.596 -0.006 0.101  -0.003 414 GLN GGG NE2 
8300  N N   . THR G 86  ? 0.646 0.611 0.527 -0.025 0.077  0.030  415 THR GGG N   
8301  C CA  . THR G 86  ? 0.644 0.608 0.529 -0.030 0.065  0.039  415 THR GGG CA  
8302  C C   . THR G 86  ? 0.645 0.599 0.506 -0.033 0.047  0.038  415 THR GGG C   
8303  O O   . THR G 86  ? 0.671 0.614 0.506 -0.034 0.045  0.030  415 THR GGG O   
8304  C CB  . THR G 86  ? 0.687 0.640 0.557 -0.030 0.078  0.052  415 THR GGG CB  
8305  O OG1 . THR G 86  ? 0.736 0.667 0.558 -0.029 0.086  0.051  415 THR GGG OG1 
8306  C CG2 . THR G 86  ? 0.682 0.650 0.586 -0.028 0.093  0.056  415 THR GGG CG2 
8307  N N   . GLY G 87  ? 0.632 0.589 0.505 -0.036 0.034  0.045  416 GLY GGG N   
8308  C CA  . GLY G 87  ? 0.644 0.598 0.508 -0.040 0.013  0.046  416 GLY GGG CA  
8309  C C   . GLY G 87  ? 0.615 0.587 0.521 -0.039 0.003  0.047  416 GLY GGG C   
8310  O O   . GLY G 87  ? 0.585 0.569 0.521 -0.036 0.011  0.044  416 GLY GGG O   
8311  N N   . LYS G 88  ? 0.643 0.618 0.551 -0.042 -0.015 0.050  417 LYS GGG N   
8312  C CA  . LYS G 88  ? 0.629 0.620 0.577 -0.039 -0.024 0.052  417 LYS GGG CA  
8313  C C   . LYS G 88  ? 0.570 0.577 0.547 -0.036 -0.015 0.040  417 LYS GGG C   
8314  O O   . LYS G 88  ? 0.571 0.585 0.576 -0.032 -0.012 0.039  417 LYS GGG O   
8315  C CB  . LYS G 88  ? 0.667 0.663 0.619 -0.042 -0.043 0.056  417 LYS GGG CB  
8316  C CG  . LYS G 88  ? 0.758 0.739 0.685 -0.045 -0.056 0.070  417 LYS GGG CG  
8317  C CD  . LYS G 88  ? 0.808 0.782 0.741 -0.041 -0.052 0.082  417 LYS GGG CD  
8318  C CE  . LYS G 88  ? 0.890 0.839 0.776 -0.045 -0.054 0.093  417 LYS GGG CE  
8319  N NZ  . LYS G 88  ? 0.949 0.892 0.843 -0.043 -0.061 0.109  417 LYS GGG NZ  
8320  N N   . ILE G 89  ? 0.538 0.547 0.504 -0.038 -0.012 0.030  418 ILE GGG N   
8321  C CA  . ILE G 89  ? 0.498 0.521 0.487 -0.035 -0.007 0.020  418 ILE GGG CA  
8322  C C   . ILE G 89  ? 0.487 0.511 0.483 -0.033 0.006  0.016  418 ILE GGG C   
8323  O O   . ILE G 89  ? 0.475 0.508 0.498 -0.030 0.008  0.013  418 ILE GGG O   
8324  C CB  . ILE G 89  ? 0.509 0.533 0.485 -0.039 -0.010 0.013  418 ILE GGG CB  
8325  C CG1 . ILE G 89  ? 0.538 0.562 0.510 -0.044 -0.025 0.018  418 ILE GGG CG1 
8326  C CG2 . ILE G 89  ? 0.488 0.526 0.486 -0.037 -0.005 0.004  418 ILE GGG CG2 
8327  C CD1 . ILE G 89  ? 0.521 0.561 0.527 -0.041 -0.033 0.023  418 ILE GGG CD1 
8328  N N   . ALA G 90  ? 0.508 0.523 0.484 -0.033 0.016  0.017  419 ALA GGG N   
8329  C CA  . ALA G 90  ? 0.496 0.515 0.484 -0.031 0.028  0.015  419 ALA GGG CA  
8330  C C   . ALA G 90  ? 0.488 0.508 0.497 -0.031 0.029  0.022  419 ALA GGG C   
8331  O O   . ALA G 90  ? 0.476 0.505 0.509 -0.030 0.032  0.017  419 ALA GGG O   
8332  C CB  . ALA G 90  ? 0.514 0.522 0.478 -0.030 0.039  0.017  419 ALA GGG CB  
8333  N N   . ASP G 91  ? 0.469 0.480 0.470 -0.032 0.024  0.031  420 ASP GGG N   
8334  C CA  . ASP G 91  ? 0.500 0.508 0.517 -0.032 0.026  0.040  420 ASP GGG CA  
8335  C C   . ASP G 91  ? 0.496 0.510 0.541 -0.030 0.017  0.037  420 ASP GGG C   
8336  O O   . ASP G 91  ? 0.493 0.506 0.560 -0.031 0.021  0.036  420 ASP GGG O   
8337  C CB  . ASP G 91  ? 0.543 0.535 0.536 -0.034 0.025  0.054  420 ASP GGG CB  
8338  C CG  . ASP G 91  ? 0.573 0.555 0.534 -0.035 0.037  0.058  420 ASP GGG CG  
8339  O OD1 . ASP G 91  ? 0.574 0.563 0.540 -0.034 0.049  0.051  420 ASP GGG OD1 
8340  O OD2 . ASP G 91  ? 0.575 0.542 0.506 -0.037 0.035  0.067  420 ASP GGG OD2 
8341  N N   . TYR G 92  ? 0.473 0.490 0.519 -0.028 0.007  0.034  421 TYR GGG N   
8342  C CA  . TYR G 92  ? 0.504 0.525 0.576 -0.025 0.000  0.035  421 TYR GGG CA  
8343  C C   . TYR G 92  ? 0.458 0.492 0.545 -0.022 -0.001 0.022  421 TYR GGG C   
8344  O O   . TYR G 92  ? 0.465 0.501 0.574 -0.017 -0.003 0.020  421 TYR GGG O   
8345  C CB  . TYR G 92  ? 0.515 0.531 0.581 -0.024 -0.011 0.047  421 TYR GGG CB  
8346  C CG  . TYR G 92  ? 0.554 0.554 0.603 -0.026 -0.011 0.061  421 TYR GGG CG  
8347  C CD1 . TYR G 92  ? 0.559 0.551 0.610 -0.028 -0.001 0.064  421 TYR GGG CD1 
8348  C CD2 . TYR G 92  ? 0.601 0.594 0.635 -0.027 -0.024 0.073  421 TYR GGG CD2 
8349  C CE1 . TYR G 92  ? 0.583 0.561 0.618 -0.031 0.001  0.079  421 TYR GGG CE1 
8350  C CE2 . TYR G 92  ? 0.645 0.622 0.659 -0.029 -0.024 0.088  421 TYR GGG CE2 
8351  C CZ  . TYR G 92  ? 0.635 0.604 0.649 -0.031 -0.010 0.091  421 TYR GGG CZ  
8352  O OH  . TYR G 92  ? 0.681 0.633 0.675 -0.033 -0.009 0.107  421 TYR GGG OH  
8353  N N   . ASN G 93  ? 0.442 0.482 0.517 -0.024 0.002  0.015  422 ASN GGG N   
8354  C CA  . ASN G 93  ? 0.454 0.505 0.539 -0.022 0.001  0.005  422 ASN GGG CA  
8355  C C   . ASN G 93  ? 0.439 0.494 0.521 -0.023 0.008  -0.005 422 ASN GGG C   
8356  O O   . ASN G 93  ? 0.448 0.506 0.543 -0.020 0.011  -0.014 422 ASN GGG O   
8357  C CB  . ASN G 93  ? 0.496 0.553 0.571 -0.024 -0.006 0.009  422 ASN GGG CB  
8358  C CG  . ASN G 93  ? 0.503 0.560 0.587 -0.023 -0.016 0.019  422 ASN GGG CG  
8359  O OD1 . ASN G 93  ? 0.524 0.593 0.633 -0.019 -0.019 0.019  422 ASN GGG OD1 
8360  N ND2 . ASN G 93  ? 0.480 0.526 0.546 -0.026 -0.022 0.029  422 ASN GGG ND2 
8361  N N   . TYR G 94  ? 0.455 0.507 0.519 -0.025 0.011  -0.005 423 TYR GGG N   
8362  C CA  . TYR G 94  ? 0.466 0.522 0.527 -0.026 0.016  -0.014 423 TYR GGG CA  
8363  C C   . TYR G 94  ? 0.463 0.514 0.513 -0.027 0.022  -0.010 423 TYR GGG C   
8364  O O   . TYR G 94  ? 0.497 0.543 0.528 -0.028 0.023  -0.006 423 TYR GGG O   
8365  C CB  . TYR G 94  ? 0.446 0.508 0.498 -0.027 0.015  -0.018 423 TYR GGG CB  
8366  C CG  . TYR G 94  ? 0.467 0.531 0.516 -0.026 0.018  -0.025 423 TYR GGG CG  
8367  C CD1 . TYR G 94  ? 0.451 0.520 0.510 -0.025 0.018  -0.033 423 TYR GGG CD1 
8368  C CD2 . TYR G 94  ? 0.474 0.535 0.510 -0.027 0.021  -0.025 423 TYR GGG CD2 
8369  C CE1 . TYR G 94  ? 0.459 0.529 0.512 -0.025 0.019  -0.038 423 TYR GGG CE1 
8370  C CE2 . TYR G 94  ? 0.447 0.512 0.483 -0.026 0.022  -0.030 423 TYR GGG CE2 
8371  C CZ  . TYR G 94  ? 0.470 0.539 0.513 -0.026 0.020  -0.036 423 TYR GGG CZ  
8372  O OH  . TYR G 94  ? 0.449 0.519 0.487 -0.025 0.019  -0.040 423 TYR GGG OH  
8373  N N   . LYS G 95  ? 0.441 0.495 0.505 -0.028 0.025  -0.012 424 LYS GGG N   
8374  C CA  . LYS G 95  ? 0.458 0.511 0.521 -0.028 0.032  -0.006 424 LYS GGG CA  
8375  C C   . LYS G 95  ? 0.451 0.512 0.521 -0.027 0.033  -0.012 424 LYS GGG C   
8376  O O   . LYS G 95  ? 0.403 0.469 0.487 -0.029 0.028  -0.018 424 LYS GGG O   
8377  C CB  . LYS G 95  ? 0.489 0.540 0.569 -0.031 0.034  -0.000 424 LYS GGG CB  
8378  C CG  . LYS G 95  ? 0.529 0.582 0.615 -0.032 0.044  0.007  424 LYS GGG CG  
8379  C CD  . LYS G 95  ? 0.565 0.612 0.626 -0.029 0.052  0.012  424 LYS GGG CD  
8380  C CE  . LYS G 95  ? 0.612 0.658 0.677 -0.030 0.065  0.023  424 LYS GGG CE  
8381  N NZ  . LYS G 95  ? 0.640 0.674 0.672 -0.027 0.073  0.027  424 LYS GGG NZ  
8382  N N   . LEU G 96  ? 0.436 0.497 0.494 -0.025 0.039  -0.011 425 LEU GGG N   
8383  C CA  . LEU G 96  ? 0.438 0.507 0.506 -0.023 0.040  -0.013 425 LEU GGG CA  
8384  C C   . LEU G 96  ? 0.438 0.514 0.526 -0.024 0.048  -0.006 425 LEU GGG C   
8385  O O   . LEU G 96  ? 0.416 0.486 0.499 -0.023 0.057  0.001  425 LEU GGG O   
8386  C CB  . LEU G 96  ? 0.464 0.529 0.514 -0.019 0.044  -0.014 425 LEU GGG CB  
8387  C CG  . LEU G 96  ? 0.470 0.531 0.505 -0.020 0.037  -0.020 425 LEU GGG CG  
8388  C CD1 . LEU G 96  ? 0.490 0.543 0.507 -0.017 0.040  -0.020 425 LEU GGG CD1 
8389  C CD2 . LEU G 96  ? 0.478 0.547 0.524 -0.021 0.029  -0.026 425 LEU GGG CD2 
8390  N N   . PRO G 97  ? 0.444 0.531 0.556 -0.025 0.044  -0.007 426 PRO GGG N   
8391  C CA  . PRO G 97  ? 0.449 0.547 0.588 -0.026 0.050  0.001  426 PRO GGG CA  
8392  C C   . PRO G 97  ? 0.471 0.571 0.605 -0.019 0.064  0.006  426 PRO GGG C   
8393  O O   . PRO G 97  ? 0.490 0.585 0.605 -0.014 0.064  0.003  426 PRO GGG O   
8394  C CB  . PRO G 97  ? 0.425 0.535 0.586 -0.030 0.038  -0.004 426 PRO GGG CB  
8395  C CG  . PRO G 97  ? 0.423 0.529 0.563 -0.026 0.030  -0.012 426 PRO GGG CG  
8396  C CD  . PRO G 97  ? 0.434 0.526 0.548 -0.026 0.032  -0.015 426 PRO GGG CD  
8397  N N   . ASP G 98  ? 0.529 0.637 0.682 -0.019 0.076  0.016  427 ASP GGG N   
8398  C CA  . ASP G 98  ? 0.584 0.694 0.735 -0.010 0.093  0.021  427 ASP GGG CA  
8399  C C   . ASP G 98  ? 0.527 0.650 0.696 -0.005 0.089  0.020  427 ASP GGG C   
8400  O O   . ASP G 98  ? 0.512 0.628 0.668 0.004  0.099  0.020  427 ASP GGG O   
8401  C CB  . ASP G 98  ? 0.665 0.782 0.836 -0.012 0.109  0.033  427 ASP GGG CB  
8402  C CG  . ASP G 98  ? 0.815 0.913 0.951 -0.007 0.126  0.037  427 ASP GGG CG  
8403  O OD1 . ASP G 98  ? 0.809 0.899 0.924 0.002  0.136  0.034  427 ASP GGG OD1 
8404  O OD2 . ASP G 98  ? 0.946 1.036 1.072 -0.013 0.128  0.042  427 ASP GGG OD2 
8405  N N   . ASP G 99  ? 0.496 0.633 0.692 -0.010 0.073  0.018  428 ASP GGG N   
8406  C CA  . ASP G 99  ? 0.497 0.648 0.713 -0.005 0.066  0.018  428 ASP GGG CA  
8407  C C   . ASP G 99  ? 0.486 0.627 0.678 -0.006 0.050  0.008  428 ASP GGG C   
8408  O O   . ASP G 99  ? 0.463 0.613 0.668 -0.007 0.035  0.007  428 ASP GGG O   
8409  C CB  . ASP G 99  ? 0.487 0.661 0.750 -0.011 0.058  0.025  428 ASP GGG CB  
8410  C CG  . ASP G 99  ? 0.500 0.672 0.765 -0.023 0.039  0.018  428 ASP GGG CG  
8411  O OD1 . ASP G 99  ? 0.493 0.647 0.728 -0.026 0.036  0.010  428 ASP GGG OD1 
8412  O OD2 . ASP G 99  ? 0.526 0.714 0.826 -0.030 0.028  0.021  428 ASP GGG OD2 
8413  N N   . PHE G 100 ? 0.461 0.584 0.617 -0.006 0.051  0.002  429 PHE GGG N   
8414  C CA  . PHE G 100 ? 0.465 0.578 0.596 -0.007 0.040  -0.006 429 PHE GGG CA  
8415  C C   . PHE G 100 ? 0.443 0.559 0.577 -0.000 0.036  -0.005 429 PHE GGG C   
8416  O O   . PHE G 100 ? 0.411 0.525 0.545 0.008  0.047  -0.001 429 PHE GGG O   
8417  C CB  . PHE G 100 ? 0.472 0.567 0.570 -0.007 0.045  -0.010 429 PHE GGG CB  
8418  C CG  . PHE G 100 ? 0.480 0.567 0.556 -0.008 0.036  -0.017 429 PHE GGG CG  
8419  C CD1 . PHE G 100 ? 0.496 0.586 0.574 -0.014 0.025  -0.022 429 PHE GGG CD1 
8420  C CD2 . PHE G 100 ? 0.478 0.551 0.530 -0.005 0.041  -0.018 429 PHE GGG CD2 
8421  C CE1 . PHE G 100 ? 0.490 0.573 0.547 -0.015 0.020  -0.027 429 PHE GGG CE1 
8422  C CE2 . PHE G 100 ? 0.508 0.575 0.543 -0.007 0.033  -0.022 429 PHE GGG CE2 
8423  C CZ  . PHE G 100 ? 0.497 0.570 0.535 -0.012 0.024  -0.026 429 PHE GGG CZ  
8424  N N   . THR G 101 ? 0.453 0.571 0.584 -0.004 0.021  -0.009 430 THR GGG N   
8425  C CA  . THR G 101 ? 0.448 0.564 0.571 0.002  0.015  -0.008 430 THR GGG CA  
8426  C C   . THR G 101 ? 0.468 0.569 0.558 -0.002 0.010  -0.015 430 THR GGG C   
8427  O O   . THR G 101 ? 0.465 0.567 0.550 -0.008 0.000  -0.020 430 THR GGG O   
8428  C CB  . THR G 101 ? 0.438 0.571 0.588 0.000  -0.000 -0.004 430 THR GGG CB  
8429  O OG1 . THR G 101 ? 0.391 0.541 0.578 0.002  0.005  0.003  430 THR GGG OG1 
8430  C CG2 . THR G 101 ? 0.458 0.589 0.602 0.007  -0.007 -0.000 430 THR GGG CG2 
8431  N N   . GLY G 102 ? 0.492 0.580 0.561 0.003  0.017  -0.015 431 GLY GGG N   
8432  C CA  . GLY G 102 ? 0.498 0.573 0.539 -0.001 0.014  -0.020 431 GLY GGG CA  
8433  C C   . GLY G 102 ? 0.518 0.576 0.538 0.001  0.023  -0.020 431 GLY GGG C   
8434  O O   . GLY G 102 ? 0.516 0.571 0.541 0.008  0.032  -0.016 431 GLY GGG O   
8435  N N   . CYS G 103 ? 0.526 0.575 0.526 -0.004 0.022  -0.023 432 CYS GGG N   
8436  C CA  . CYS G 103 ? 0.525 0.558 0.505 -0.005 0.027  -0.023 432 CYS GGG CA  
8437  C C   . CYS G 103 ? 0.493 0.525 0.465 -0.012 0.027  -0.027 432 CYS GGG C   
8438  O O   . CYS G 103 ? 0.534 0.576 0.512 -0.016 0.023  -0.029 432 CYS GGG O   
8439  C CB  . CYS G 103 ? 0.563 0.585 0.529 -0.004 0.023  -0.021 432 CYS GGG CB  
8440  S SG  . CYS G 103 ? 0.621 0.646 0.600 0.006  0.020  -0.015 432 CYS GGG SG  
8441  N N   . VAL G 104 ? 0.502 0.521 0.461 -0.013 0.031  -0.027 433 VAL GGG N   
8442  C CA  . VAL G 104 ? 0.498 0.514 0.449 -0.021 0.029  -0.029 433 VAL GGG CA  
8443  C C   . VAL G 104 ? 0.518 0.519 0.451 -0.025 0.026  -0.029 433 VAL GGG C   
8444  O O   . VAL G 104 ? 0.520 0.502 0.437 -0.022 0.030  -0.029 433 VAL GGG O   
8445  C CB  . VAL G 104 ? 0.489 0.503 0.439 -0.020 0.033  -0.028 433 VAL GGG CB  
8446  C CG1 . VAL G 104 ? 0.470 0.480 0.411 -0.027 0.028  -0.028 433 VAL GGG CG1 
8447  C CG2 . VAL G 104 ? 0.495 0.524 0.466 -0.017 0.034  -0.027 433 VAL GGG CG2 
8448  N N   . ILE G 105 ? 0.526 0.532 0.460 -0.032 0.022  -0.029 434 ILE GGG N   
8449  C CA  . ILE G 105 ? 0.565 0.558 0.486 -0.040 0.019  -0.027 434 ILE GGG CA  
8450  C C   . ILE G 105 ? 0.531 0.532 0.458 -0.048 0.014  -0.027 434 ILE GGG C   
8451  O O   . ILE G 105 ? 0.542 0.562 0.487 -0.047 0.014  -0.027 434 ILE GGG O   
8452  C CB  . ILE G 105 ? 0.581 0.577 0.503 -0.041 0.019  -0.025 434 ILE GGG CB  
8453  C CG1 . ILE G 105 ? 0.623 0.613 0.541 -0.032 0.021  -0.024 434 ILE GGG CG1 
8454  C CG2 . ILE G 105 ? 0.602 0.586 0.514 -0.050 0.016  -0.023 434 ILE GGG CG2 
8455  C CD1 . ILE G 105 ? 0.649 0.643 0.567 -0.032 0.020  -0.021 434 ILE GGG CD1 
8456  N N   . ALA G 106 ? 0.516 0.502 0.429 -0.055 0.008  -0.026 435 ALA GGG N   
8457  C CA  . ALA G 106 ? 0.518 0.511 0.438 -0.064 0.000  -0.024 435 ALA GGG CA  
8458  C C   . ALA G 106 ? 0.539 0.518 0.450 -0.074 -0.006 -0.022 435 ALA GGG C   
8459  O O   . ALA G 106 ? 0.572 0.528 0.462 -0.074 -0.004 -0.024 435 ALA GGG O   
8460  C CB  . ALA G 106 ? 0.523 0.511 0.436 -0.062 -0.003 -0.024 435 ALA GGG CB  
8461  N N   . TRP G 107 ? 0.513 0.506 0.440 -0.084 -0.014 -0.018 436 TRP GGG N   
8462  C CA  . TRP G 107 ? 0.537 0.519 0.460 -0.097 -0.023 -0.016 436 TRP GGG CA  
8463  C C   . TRP G 107 ? 0.525 0.521 0.465 -0.106 -0.035 -0.011 436 TRP GGG C   
8464  O O   . TRP G 107 ? 0.502 0.524 0.467 -0.101 -0.032 -0.008 436 TRP GGG O   
8465  C CB  . TRP G 107 ? 0.525 0.510 0.456 -0.101 -0.017 -0.012 436 TRP GGG CB  
8466  C CG  . TRP G 107 ? 0.502 0.518 0.463 -0.100 -0.010 -0.007 436 TRP GGG CG  
8467  C CD1 . TRP G 107 ? 0.495 0.530 0.482 -0.109 -0.013 -0.001 436 TRP GGG CD1 
8468  C CD2 . TRP G 107 ? 0.490 0.521 0.458 -0.089 0.001  -0.009 436 TRP GGG CD2 
8469  N NE1 . TRP G 107 ? 0.497 0.556 0.504 -0.103 -0.002 0.001  436 TRP GGG NE1 
8470  C CE2 . TRP G 107 ? 0.474 0.529 0.468 -0.091 0.006  -0.005 436 TRP GGG CE2 
8471  C CE3 . TRP G 107 ? 0.490 0.516 0.447 -0.077 0.007  -0.014 436 TRP GGG CE3 
8472  C CZ2 . TRP G 107 ? 0.473 0.543 0.475 -0.082 0.017  -0.007 436 TRP GGG CZ2 
8473  C CZ3 . TRP G 107 ? 0.482 0.524 0.449 -0.070 0.014  -0.016 436 TRP GGG CZ3 
8474  C CH2 . TRP G 107 ? 0.471 0.532 0.457 -0.073 0.020  -0.013 436 TRP GGG CH2 
8475  N N   . ASN G 108 ? 0.522 0.500 0.448 -0.118 -0.048 -0.010 437 ASN GGG N   
8476  C CA  . ASN G 108 ? 0.540 0.532 0.485 -0.129 -0.064 -0.004 437 ASN GGG CA  
8477  C C   . ASN G 108 ? 0.542 0.565 0.528 -0.133 -0.060 0.003  437 ASN GGG C   
8478  O O   . ASN G 108 ? 0.561 0.581 0.549 -0.138 -0.054 0.005  437 ASN GGG O   
8479  C CB  . ASN G 108 ? 0.571 0.532 0.488 -0.143 -0.080 -0.006 437 ASN GGG CB  
8480  C CG  . ASN G 108 ? 0.590 0.564 0.524 -0.155 -0.100 0.000  437 ASN GGG CG  
8481  O OD1 . ASN G 108 ? 0.585 0.587 0.559 -0.162 -0.104 0.009  437 ASN GGG OD1 
8482  N ND2 . ASN G 108 ? 0.635 0.591 0.542 -0.156 -0.112 -0.002 437 ASN GGG ND2 
8483  N N   . SER G 109 ? 0.513 0.565 0.531 -0.131 -0.062 0.009  438 SER GGG N   
8484  C CA  . SER G 109 ? 0.479 0.565 0.541 -0.133 -0.056 0.017  438 SER GGG CA  
8485  C C   . SER G 109 ? 0.487 0.591 0.580 -0.143 -0.073 0.026  438 SER GGG C   
8486  O O   . SER G 109 ? 0.446 0.582 0.581 -0.141 -0.068 0.033  438 SER GGG O   
8487  C CB  . SER G 109 ? 0.461 0.565 0.538 -0.117 -0.039 0.015  438 SER GGG CB  
8488  O OG  . SER G 109 ? 0.494 0.601 0.572 -0.110 -0.045 0.014  438 SER GGG OG  
8489  N N   . ASN G 110 ? 0.511 0.594 0.582 -0.155 -0.094 0.026  439 ASN GGG N   
8490  C CA  . ASN G 110 ? 0.518 0.616 0.615 -0.167 -0.116 0.035  439 ASN GGG CA  
8491  C C   . ASN G 110 ? 0.515 0.643 0.660 -0.177 -0.113 0.045  439 ASN GGG C   
8492  O O   . ASN G 110 ? 0.499 0.660 0.690 -0.177 -0.118 0.055  439 ASN GGG O   
8493  C CB  . ASN G 110 ? 0.555 0.618 0.612 -0.180 -0.138 0.032  439 ASN GGG CB  
8494  C CG  . ASN G 110 ? 0.577 0.651 0.651 -0.189 -0.164 0.040  439 ASN GGG CG  
8495  O OD1 . ASN G 110 ? 0.571 0.670 0.672 -0.180 -0.165 0.046  439 ASN GGG OD1 
8496  N ND2 . ASN G 110 ? 0.615 0.668 0.670 -0.208 -0.187 0.040  439 ASN GGG ND2 
8497  N N   . ASN G 111 ? 0.536 0.654 0.674 -0.184 -0.103 0.044  440 ASN GGG N   
8498  C CA  . ASN G 111 ? 0.545 0.688 0.726 -0.195 -0.099 0.054  440 ASN GGG CA  
8499  C C   . ASN G 111 ? 0.530 0.712 0.754 -0.182 -0.078 0.060  440 ASN GGG C   
8500  O O   . ASN G 111 ? 0.552 0.765 0.823 -0.190 -0.076 0.071  440 ASN GGG O   
8501  C CB  . ASN G 111 ? 0.546 0.664 0.702 -0.204 -0.092 0.052  440 ASN GGG CB  
8502  C CG  . ASN G 111 ? 0.578 0.662 0.707 -0.222 -0.114 0.049  440 ASN GGG CG  
8503  O OD1 . ASN G 111 ? 0.608 0.696 0.748 -0.234 -0.138 0.054  440 ASN GGG OD1 
8504  N ND2 . ASN G 111 ? 0.601 0.651 0.694 -0.225 -0.108 0.043  440 ASN GGG ND2 
8505  N N   . LEU G 112 ? 0.539 0.720 0.748 -0.163 -0.061 0.052  441 LEU GGG N   
8506  C CA  . LEU G 112 ? 0.536 0.747 0.777 -0.150 -0.039 0.054  441 LEU GGG CA  
8507  C C   . LEU G 112 ? 0.503 0.731 0.765 -0.138 -0.043 0.055  441 LEU GGG C   
8508  O O   . LEU G 112 ? 0.495 0.753 0.800 -0.131 -0.032 0.062  441 LEU GGG O   
8509  C CB  . LEU G 112 ? 0.565 0.758 0.770 -0.138 -0.018 0.044  441 LEU GGG CB  
8510  C CG  . LEU G 112 ? 0.584 0.799 0.810 -0.128 0.007  0.046  441 LEU GGG CG  
8511  C CD1 . LEU G 112 ? 0.560 0.805 0.832 -0.139 0.013  0.059  441 LEU GGG CD1 
8512  C CD2 . LEU G 112 ? 0.616 0.810 0.804 -0.123 0.022  0.038  441 LEU GGG CD2 
8513  N N   . ASP G 113 ? 0.505 0.712 0.738 -0.134 -0.057 0.050  442 ASP GGG N   
8514  C CA  . ASP G 113 ? 0.484 0.700 0.728 -0.119 -0.058 0.049  442 ASP GGG CA  
8515  C C   . ASP G 113 ? 0.505 0.728 0.766 -0.125 -0.083 0.058  442 ASP GGG C   
8516  O O   . ASP G 113 ? 0.510 0.735 0.774 -0.114 -0.086 0.059  442 ASP GGG O   
8517  C CB  . ASP G 113 ? 0.454 0.641 0.651 -0.109 -0.052 0.037  442 ASP GGG CB  
8518  C CG  . ASP G 113 ? 0.452 0.638 0.640 -0.099 -0.028 0.029  442 ASP GGG CG  
8519  O OD1 . ASP G 113 ? 0.425 0.634 0.645 -0.092 -0.013 0.032  442 ASP GGG OD1 
8520  O OD2 . ASP G 113 ? 0.424 0.584 0.572 -0.097 -0.024 0.020  442 ASP GGG OD2 
8521  N N   . SER G 114 ? 0.553 0.777 0.821 -0.143 -0.103 0.065  443 SER GGG N   
8522  C CA  . SER G 114 ? 0.600 0.831 0.884 -0.150 -0.130 0.074  443 SER GGG CA  
8523  C C   . SER G 114 ? 0.623 0.892 0.968 -0.159 -0.137 0.089  443 SER GGG C   
8524  O O   . SER G 114 ? 0.646 0.924 1.006 -0.166 -0.124 0.090  443 SER GGG O   
8525  C CB  . SER G 114 ? 0.635 0.828 0.866 -0.163 -0.152 0.069  443 SER GGG CB  
8526  O OG  . SER G 114 ? 0.638 0.828 0.872 -0.182 -0.164 0.072  443 SER GGG OG  
8527  N N   . LYS G 115 ? 0.682 0.975 1.067 -0.158 -0.154 0.101  444 LYS GGG N   
8528  C CA  . LYS G 115 ? 0.697 1.032 1.152 -0.166 -0.160 0.116  444 LYS GGG CA  
8529  C C   . LYS G 115 ? 0.711 1.048 1.175 -0.180 -0.199 0.127  444 LYS GGG C   
8530  O O   . LYS G 115 ? 0.689 1.003 1.115 -0.177 -0.215 0.124  444 LYS GGG O   
8531  C CB  . LYS G 115 ? 0.723 1.094 1.232 -0.146 -0.141 0.123  444 LYS GGG CB  
8532  C CG  . LYS G 115 ? 0.785 1.172 1.313 -0.138 -0.105 0.119  444 LYS GGG CG  
8533  C CD  . LYS G 115 ? 0.837 1.235 1.380 -0.114 -0.079 0.115  444 LYS GGG CD  
8534  C CE  . LYS G 115 ? 0.859 1.240 1.368 -0.107 -0.048 0.101  444 LYS GGG CE  
8535  N NZ  . LYS G 115 ? 0.828 1.205 1.331 -0.084 -0.028 0.092  444 LYS GGG NZ  
8536  N N   . VAL G 116 ? 0.717 1.083 1.232 -0.197 -0.213 0.141  445 VAL GGG N   
8537  C CA  . VAL G 116 ? 0.733 1.111 1.272 -0.210 -0.253 0.154  445 VAL GGG CA  
8538  C C   . VAL G 116 ? 0.693 1.097 1.270 -0.191 -0.253 0.164  445 VAL GGG C   
8539  O O   . VAL G 116 ? 0.639 1.074 1.263 -0.174 -0.226 0.167  445 VAL GGG O   
8540  C CB  . VAL G 116 ? 0.785 1.191 1.377 -0.232 -0.267 0.168  445 VAL GGG CB  
8541  C CG1 . VAL G 116 ? 0.811 1.181 1.354 -0.253 -0.270 0.157  445 VAL GGG CG1 
8542  C CG2 . VAL G 116 ? 0.765 1.223 1.435 -0.223 -0.239 0.178  445 VAL GGG CG2 
8543  N N   . GLY G 117 ? 0.683 1.068 1.232 -0.190 -0.281 0.167  446 GLY GGG N   
8544  C CA  . GLY G 117 ? 0.662 1.064 1.239 -0.171 -0.282 0.176  446 GLY GGG CA  
8545  C C   . GLY G 117 ? 0.655 1.031 1.188 -0.150 -0.255 0.162  446 GLY GGG C   
8546  O O   . GLY G 117 ? 0.674 1.057 1.223 -0.134 -0.256 0.168  446 GLY GGG O   
8547  N N   . GLY G 118 ? 0.678 1.024 1.158 -0.151 -0.235 0.144  447 GLY GGG N   
8548  C CA  . GLY G 118 ? 0.675 0.988 1.101 -0.136 -0.216 0.130  447 GLY GGG CA  
8549  C C   . GLY G 118 ? 0.625 0.954 1.076 -0.117 -0.179 0.124  447 GLY GGG C   
8550  O O   . GLY G 118 ? 0.662 1.025 1.172 -0.106 -0.172 0.133  447 GLY GGG O   
8551  N N   . ASN G 119 ? 0.565 0.867 0.969 -0.113 -0.157 0.108  448 ASN GGG N   
8552  C CA  . ASN G 119 ? 0.527 0.835 0.940 -0.095 -0.124 0.099  448 ASN GGG CA  
8553  C C   . ASN G 119 ? 0.535 0.824 0.924 -0.080 -0.122 0.095  448 ASN GGG C   
8554  O O   . ASN G 119 ? 0.553 0.809 0.888 -0.083 -0.126 0.087  448 ASN GGG O   
8555  C CB  . ASN G 119 ? 0.507 0.799 0.887 -0.099 -0.104 0.086  448 ASN GGG CB  
8556  C CG  . ASN G 119 ? 0.495 0.788 0.875 -0.083 -0.073 0.076  448 ASN GGG CG  
8557  O OD1 . ASN G 119 ? 0.502 0.811 0.914 -0.068 -0.063 0.079  448 ASN GGG OD1 
8558  N ND2 . ASN G 119 ? 0.512 0.786 0.855 -0.084 -0.058 0.064  448 ASN GGG ND2 
8559  N N   . TYR G 120 ? 0.531 0.838 0.961 -0.065 -0.114 0.100  449 TYR GGG N   
8560  C CA  . TYR G 120 ? 0.554 0.845 0.970 -0.051 -0.114 0.099  449 TYR GGG CA  
8561  C C   . TYR G 120 ? 0.555 0.839 0.965 -0.036 -0.083 0.086  449 TYR GGG C   
8562  O O   . TYR G 120 ? 0.552 0.823 0.956 -0.024 -0.079 0.084  449 TYR GGG O   
8563  C CB  . TYR G 120 ? 0.557 0.868 1.019 -0.045 -0.132 0.116  449 TYR GGG CB  
8564  C CG  . TYR G 120 ? 0.594 0.904 1.048 -0.061 -0.167 0.129  449 TYR GGG CG  
8565  C CD1 . TYR G 120 ? 0.625 0.903 1.025 -0.066 -0.184 0.128  449 TYR GGG CD1 
8566  C CD2 . TYR G 120 ? 0.613 0.952 1.110 -0.072 -0.182 0.141  449 TYR GGG CD2 
8567  C CE1 . TYR G 120 ? 0.662 0.933 1.044 -0.082 -0.216 0.138  449 TYR GGG CE1 
8568  C CE2 . TYR G 120 ? 0.650 0.986 1.136 -0.088 -0.217 0.151  449 TYR GGG CE2 
8569  C CZ  . TYR G 120 ? 0.679 0.978 1.104 -0.093 -0.234 0.149  449 TYR GGG CZ  
8570  O OH  . TYR G 120 ? 0.682 0.973 1.089 -0.110 -0.269 0.158  449 TYR GGG OH  
8571  N N   . ASN G 121 ? 0.534 0.823 0.941 -0.038 -0.063 0.076  450 ASN GGG N   
8572  C CA  . ASN G 121 ? 0.517 0.800 0.919 -0.025 -0.035 0.063  450 ASN GGG CA  
8573  C C   . ASN G 121 ? 0.505 0.754 0.852 -0.024 -0.031 0.051  450 ASN GGG C   
8574  O O   . ASN G 121 ? 0.529 0.768 0.873 -0.012 -0.016 0.042  450 ASN GGG O   
8575  C CB  . ASN G 121 ? 0.530 0.828 0.943 -0.027 -0.015 0.059  450 ASN GGG CB  
8576  C CG  . ASN G 121 ? 0.579 0.913 1.054 -0.023 -0.010 0.071  450 ASN GGG CG  
8577  O OD1 . ASN G 121 ? 0.617 0.964 1.129 -0.012 -0.014 0.079  450 ASN GGG OD1 
8578  N ND2 . ASN G 121 ? 0.626 0.978 1.116 -0.030 0.001  0.072  450 ASN GGG ND2 
8579  N N   . TYR G 122 ? 0.483 0.714 0.791 -0.036 -0.045 0.049  451 TYR GGG N   
8580  C CA  . TYR G 122 ? 0.463 0.664 0.724 -0.035 -0.040 0.039  451 TYR GGG CA  
8581  C C   . TYR G 122 ? 0.475 0.662 0.726 -0.031 -0.052 0.044  451 TYR GGG C   
8582  O O   . TYR G 122 ? 0.468 0.655 0.719 -0.037 -0.072 0.055  451 TYR GGG O   
8583  C CB  . TYR G 122 ? 0.472 0.660 0.697 -0.048 -0.045 0.035  451 TYR GGG CB  
8584  C CG  . TYR G 122 ? 0.480 0.676 0.707 -0.052 -0.031 0.029  451 TYR GGG CG  
8585  C CD1 . TYR G 122 ? 0.474 0.663 0.688 -0.045 -0.012 0.019  451 TYR GGG CD1 
8586  C CD2 . TYR G 122 ? 0.487 0.695 0.727 -0.064 -0.039 0.036  451 TYR GGG CD2 
8587  C CE1 . TYR G 122 ? 0.451 0.644 0.661 -0.049 -0.000 0.015  451 TYR GGG CE1 
8588  C CE2 . TYR G 122 ? 0.469 0.682 0.708 -0.068 -0.026 0.032  451 TYR GGG CE2 
8589  C CZ  . TYR G 122 ? 0.450 0.656 0.674 -0.060 -0.006 0.022  451 TYR GGG CZ  
8590  O OH  . TYR G 122 ? 0.468 0.677 0.689 -0.064 0.006  0.020  451 TYR GGG OH  
8591  N N   . LEU G 123 ? 0.453 0.627 0.696 -0.021 -0.040 0.037  452 LEU GGG N   
8592  C CA  . LEU G 123 ? 0.469 0.628 0.705 -0.016 -0.047 0.042  452 LEU GGG CA  
8593  C C   . LEU G 123 ? 0.450 0.585 0.644 -0.019 -0.043 0.035  452 LEU GGG C   
8594  O O   . LEU G 123 ? 0.442 0.573 0.619 -0.021 -0.032 0.024  452 LEU GGG O   
8595  C CB  . LEU G 123 ? 0.452 0.616 0.720 -0.002 -0.036 0.041  452 LEU GGG CB  
8596  C CG  . LEU G 123 ? 0.441 0.631 0.757 0.005  -0.035 0.048  452 LEU GGG CG  
8597  C CD1 . LEU G 123 ? 0.422 0.609 0.764 0.021  -0.023 0.045  452 LEU GGG CD1 
8598  C CD2 . LEU G 123 ? 0.447 0.650 0.782 0.000  -0.058 0.064  452 LEU GGG CD2 
8599  N N   . TYR G 124 ? 0.445 0.564 0.623 -0.020 -0.052 0.042  453 TYR GGG N   
8600  C CA  . TYR G 124 ? 0.466 0.564 0.611 -0.021 -0.046 0.037  453 TYR GGG CA  
8601  C C   . TYR G 124 ? 0.478 0.566 0.630 -0.015 -0.049 0.045  453 TYR GGG C   
8602  O O   . TYR G 124 ? 0.491 0.584 0.662 -0.012 -0.061 0.057  453 TYR GGG O   
8603  C CB  . TYR G 124 ? 0.490 0.576 0.598 -0.031 -0.054 0.039  453 TYR GGG CB  
8604  C CG  . TYR G 124 ? 0.514 0.596 0.612 -0.036 -0.073 0.052  453 TYR GGG CG  
8605  C CD1 . TYR G 124 ? 0.523 0.617 0.632 -0.041 -0.087 0.057  453 TYR GGG CD1 
8606  C CD2 . TYR G 124 ? 0.522 0.586 0.599 -0.035 -0.077 0.060  453 TYR GGG CD2 
8607  C CE1 . TYR G 124 ? 0.524 0.613 0.624 -0.047 -0.108 0.070  453 TYR GGG CE1 
8608  C CE2 . TYR G 124 ? 0.528 0.586 0.592 -0.040 -0.096 0.073  453 TYR GGG CE2 
8609  C CZ  . TYR G 124 ? 0.543 0.612 0.617 -0.046 -0.112 0.077  453 TYR GGG CZ  
8610  O OH  . TYR G 124 ? 0.602 0.666 0.663 -0.051 -0.135 0.090  453 TYR GGG OH  
8611  N N   . ARG G 125 ? 0.471 0.545 0.612 -0.013 -0.039 0.040  454 ARG GGG N   
8612  C CA  . ARG G 125 ? 0.490 0.550 0.634 -0.009 -0.040 0.049  454 ARG GGG CA  
8613  C C   . ARG G 125 ? 0.520 0.567 0.632 -0.016 -0.050 0.060  454 ARG GGG C   
8614  O O   . ARG G 125 ? 0.563 0.603 0.645 -0.022 -0.045 0.056  454 ARG GGG O   
8615  C CB  . ARG G 125 ? 0.471 0.522 0.617 -0.007 -0.027 0.039  454 ARG GGG CB  
8616  C CG  . ARG G 125 ? 0.480 0.516 0.635 -0.003 -0.027 0.048  454 ARG GGG CG  
8617  C CD  . ARG G 125 ? 0.469 0.495 0.629 -0.002 -0.016 0.038  454 ARG GGG CD  
8618  N NE  . ARG G 125 ? 0.458 0.492 0.637 0.003  -0.010 0.025  454 ARG GGG NE  
8619  C CZ  . ARG G 125 ? 0.460 0.494 0.665 0.013  -0.009 0.024  454 ARG GGG CZ  
8620  N NH1 . ARG G 125 ? 0.459 0.485 0.678 0.018  -0.016 0.036  454 ARG GGG NH1 
8621  N NH2 . ARG G 125 ? 0.476 0.515 0.692 0.018  -0.001 0.010  454 ARG GGG NH2 
8622  N N   . LEU G 126 ? 0.555 0.599 0.673 -0.014 -0.063 0.075  455 LEU GGG N   
8623  C CA  . LEU G 126 ? 0.609 0.637 0.691 -0.021 -0.074 0.087  455 LEU GGG CA  
8624  C C   . LEU G 126 ? 0.639 0.648 0.709 -0.019 -0.068 0.095  455 LEU GGG C   
8625  O O   . LEU G 126 ? 0.689 0.683 0.721 -0.025 -0.067 0.100  455 LEU GGG O   
8626  C CB  . LEU G 126 ? 0.634 0.672 0.731 -0.020 -0.095 0.100  455 LEU GGG CB  
8627  C CG  . LEU G 126 ? 0.659 0.680 0.719 -0.026 -0.112 0.115  455 LEU GGG CG  
8628  C CD1 . LEU G 126 ? 0.658 0.666 0.670 -0.036 -0.110 0.108  455 LEU GGG CD1 
8629  C CD2 . LEU G 126 ? 0.672 0.705 0.754 -0.026 -0.135 0.128  455 LEU GGG CD2 
8630  N N   . PHE G 127 ? 0.660 0.669 0.762 -0.012 -0.063 0.096  456 PHE GGG N   
8631  C CA  . PHE G 127 ? 0.672 0.662 0.770 -0.011 -0.058 0.105  456 PHE GGG CA  
8632  C C   . PHE G 127 ? 0.617 0.606 0.735 -0.009 -0.042 0.092  456 PHE GGG C   
8633  O O   . PHE G 127 ? 0.588 0.588 0.733 -0.003 -0.039 0.081  456 PHE GGG O   
8634  C CB  . PHE G 127 ? 0.723 0.708 0.840 -0.005 -0.071 0.121  456 PHE GGG CB  
8635  C CG  . PHE G 127 ? 0.792 0.779 0.893 -0.007 -0.091 0.135  456 PHE GGG CG  
8636  C CD1 . PHE G 127 ? 0.838 0.809 0.893 -0.015 -0.096 0.145  456 PHE GGG CD1 
8637  C CD2 . PHE G 127 ? 0.825 0.829 0.957 -0.002 -0.105 0.139  456 PHE GGG CD2 
8638  C CE1 . PHE G 127 ? 0.860 0.829 0.897 -0.019 -0.117 0.158  456 PHE GGG CE1 
8639  C CE2 . PHE G 127 ? 0.847 0.853 0.967 -0.005 -0.127 0.152  456 PHE GGG CE2 
8640  C CZ  . PHE G 127 ? 0.864 0.852 0.934 -0.014 -0.134 0.161  456 PHE GGG CZ  
8641  N N   . ARG G 128 ? 0.603 0.579 0.707 -0.014 -0.032 0.095  457 ARG GGG N   
8642  C CA  . ARG G 128 ? 0.576 0.547 0.700 -0.013 -0.021 0.086  457 ARG GGG CA  
8643  C C   . ARG G 128 ? 0.604 0.559 0.719 -0.019 -0.015 0.098  457 ARG GGG C   
8644  O O   . ARG G 128 ? 0.579 0.530 0.664 -0.024 -0.013 0.107  457 ARG GGG O   
8645  C CB  . ARG G 128 ? 0.532 0.516 0.654 -0.016 -0.012 0.068  457 ARG GGG CB  
8646  C CG  . ARG G 128 ? 0.516 0.497 0.660 -0.015 -0.005 0.056  457 ARG GGG CG  
8647  C CD  . ARG G 128 ? 0.501 0.497 0.643 -0.017 0.000  0.040  457 ARG GGG CD  
8648  N NE  . ARG G 128 ? 0.486 0.479 0.646 -0.015 0.004  0.027  457 ARG GGG NE  
8649  C CZ  . ARG G 128 ? 0.486 0.471 0.650 -0.021 0.008  0.023  457 ARG GGG CZ  
8650  N NH1 . ARG G 128 ? 0.480 0.464 0.637 -0.028 0.012  0.032  457 ARG GGG NH1 
8651  N NH2 . ARG G 128 ? 0.495 0.475 0.672 -0.020 0.009  0.010  457 ARG GGG NH2 
8652  N N   . LYS G 129 ? 0.652 0.595 0.789 -0.018 -0.011 0.097  458 LYS GGG N   
8653  C CA  . LYS G 129 ? 0.690 0.616 0.824 -0.024 -0.005 0.111  458 LYS GGG CA  
8654  C C   . LYS G 129 ? 0.658 0.591 0.779 -0.033 0.008  0.107  458 LYS GGG C   
8655  O O   . LYS G 129 ? 0.679 0.603 0.787 -0.039 0.015  0.121  458 LYS GGG O   
8656  C CB  . LYS G 129 ? 0.724 0.636 0.888 -0.023 -0.004 0.108  458 LYS GGG CB  
8657  C CG  . LYS G 129 ? 0.766 0.666 0.949 -0.014 -0.014 0.114  458 LYS GGG CG  
8658  C CD  . LYS G 129 ? 0.791 0.675 1.000 -0.014 -0.010 0.104  458 LYS GGG CD  
8659  C CE  . LYS G 129 ? 0.888 0.751 1.117 -0.005 -0.017 0.114  458 LYS GGG CE  
8660  N NZ  . LYS G 129 ? 0.921 0.771 1.173 -0.002 -0.014 0.096  458 LYS GGG NZ  
8661  N N   . SER G 130 ? 0.602 0.550 0.727 -0.033 0.012  0.090  459 SER GGG N   
8662  C CA  . SER G 130 ? 0.583 0.541 0.703 -0.040 0.023  0.086  459 SER GGG CA  
8663  C C   . SER G 130 ? 0.563 0.538 0.677 -0.037 0.023  0.070  459 SER GGG C   
8664  O O   . SER G 130 ? 0.573 0.552 0.692 -0.032 0.015  0.061  459 SER GGG O   
8665  C CB  . SER G 130 ? 0.593 0.546 0.739 -0.046 0.028  0.084  459 SER GGG CB  
8666  O OG  . SER G 130 ? 0.587 0.545 0.751 -0.044 0.024  0.067  459 SER GGG OG  
8667  N N   . ASN G 131 ? 0.548 0.531 0.651 -0.041 0.033  0.068  460 ASN GGG N   
8668  C CA  . ASN G 131 ? 0.521 0.518 0.616 -0.039 0.033  0.055  460 ASN GGG CA  
8669  C C   . ASN G 131 ? 0.496 0.502 0.615 -0.038 0.030  0.041  460 ASN GGG C   
8670  O O   . ASN G 131 ? 0.499 0.501 0.639 -0.042 0.031  0.041  460 ASN GGG O   
8671  C CB  . ASN G 131 ? 0.514 0.515 0.593 -0.041 0.046  0.059  460 ASN GGG CB  
8672  C CG  . ASN G 131 ? 0.542 0.532 0.586 -0.040 0.049  0.070  460 ASN GGG CG  
8673  O OD1 . ASN G 131 ? 0.570 0.550 0.602 -0.039 0.039  0.076  460 ASN GGG OD1 
8674  N ND2 . ASN G 131 ? 0.554 0.544 0.582 -0.041 0.063  0.074  460 ASN GGG ND2 
8675  N N   . LEU G 132 ? 0.513 0.527 0.626 -0.035 0.026  0.029  461 LEU GGG N   
8676  C CA  . LEU G 132 ? 0.516 0.537 0.643 -0.035 0.024  0.015  461 LEU GGG CA  
8677  C C   . LEU G 132 ? 0.504 0.534 0.638 -0.040 0.030  0.014  461 LEU GGG C   
8678  O O   . LEU G 132 ? 0.521 0.555 0.642 -0.040 0.037  0.020  461 LEU GGG O   
8679  C CB  . LEU G 132 ? 0.536 0.566 0.650 -0.030 0.021  0.006  461 LEU GGG CB  
8680  C CG  . LEU G 132 ? 0.530 0.557 0.645 -0.026 0.015  0.006  461 LEU GGG CG  
8681  C CD1 . LEU G 132 ? 0.511 0.550 0.619 -0.023 0.014  -0.003 461 LEU GGG CD1 
8682  C CD2 . LEU G 132 ? 0.556 0.575 0.691 -0.023 0.013  0.001  461 LEU GGG CD2 
8683  N N   . LYS G 133 ? 0.528 0.558 0.680 -0.043 0.026  0.007  462 LYS GGG N   
8684  C CA  . LYS G 133 ? 0.522 0.564 0.685 -0.047 0.027  0.002  462 LYS GGG CA  
8685  C C   . LYS G 133 ? 0.478 0.529 0.625 -0.042 0.025  -0.006 462 LYS GGG C   
8686  O O   . LYS G 133 ? 0.460 0.507 0.593 -0.038 0.022  -0.012 462 LYS GGG O   
8687  C CB  . LYS G 133 ? 0.566 0.603 0.749 -0.053 0.019  -0.005 462 LYS GGG CB  
8688  C CG  . LYS G 133 ? 0.652 0.682 0.857 -0.061 0.020  0.004  462 LYS GGG CG  
8689  C CD  . LYS G 133 ? 0.732 0.750 0.935 -0.060 0.026  0.017  462 LYS GGG CD  
8690  C CE  . LYS G 133 ? 0.781 0.801 1.001 -0.068 0.033  0.031  462 LYS GGG CE  
8691  N NZ  . LYS G 133 ? 0.869 0.870 1.096 -0.071 0.033  0.040  462 LYS GGG NZ  
8692  N N   . PRO G 134 ? 0.480 0.543 0.630 -0.043 0.028  -0.006 463 PRO GGG N   
8693  C CA  . PRO G 134 ? 0.471 0.540 0.607 -0.039 0.026  -0.013 463 PRO GGG CA  
8694  C C   . PRO G 134 ? 0.462 0.527 0.594 -0.039 0.017  -0.026 463 PRO GGG C   
8695  O O   . PRO G 134 ? 0.453 0.515 0.598 -0.043 0.010  -0.031 463 PRO GGG O   
8696  C CB  . PRO G 134 ? 0.466 0.548 0.616 -0.040 0.028  -0.010 463 PRO GGG CB  
8697  C CG  . PRO G 134 ? 0.474 0.556 0.636 -0.042 0.038  0.002  463 PRO GGG CG  
8698  C CD  . PRO G 134 ? 0.469 0.541 0.640 -0.047 0.034  0.003  463 PRO GGG CD  
8699  N N   . PHE G 135 ? 0.454 0.518 0.568 -0.034 0.017  -0.030 464 PHE GGG N   
8700  C CA  . PHE G 135 ? 0.461 0.522 0.566 -0.033 0.012  -0.041 464 PHE GGG CA  
8701  C C   . PHE G 135 ? 0.460 0.511 0.573 -0.033 0.011  -0.045 464 PHE GGG C   
8702  O O   . PHE G 135 ? 0.452 0.497 0.559 -0.031 0.008  -0.056 464 PHE GGG O   
8703  C CB  . PHE G 135 ? 0.452 0.517 0.557 -0.036 0.006  -0.048 464 PHE GGG CB  
8704  C CG  . PHE G 135 ? 0.443 0.517 0.541 -0.034 0.007  -0.044 464 PHE GGG CG  
8705  C CD1 . PHE G 135 ? 0.460 0.534 0.540 -0.030 0.010  -0.044 464 PHE GGG CD1 
8706  C CD2 . PHE G 135 ? 0.432 0.515 0.544 -0.036 0.003  -0.040 464 PHE GGG CD2 
8707  C CE1 . PHE G 135 ? 0.481 0.560 0.554 -0.028 0.011  -0.041 464 PHE GGG CE1 
8708  C CE2 . PHE G 135 ? 0.441 0.530 0.547 -0.032 0.005  -0.037 464 PHE GGG CE2 
8709  C CZ  . PHE G 135 ? 0.463 0.548 0.548 -0.028 0.009  -0.037 464 PHE GGG CZ  
8710  N N   . GLU G 136 ? 0.477 0.523 0.600 -0.033 0.013  -0.037 465 GLU GGG N   
8711  C CA  . GLU G 136 ? 0.507 0.540 0.637 -0.031 0.012  -0.039 465 GLU GGG CA  
8712  C C   . GLU G 136 ? 0.496 0.533 0.619 -0.024 0.014  -0.039 465 GLU GGG C   
8713  O O   . GLU G 136 ? 0.467 0.512 0.580 -0.023 0.016  -0.034 465 GLU GGG O   
8714  C CB  . GLU G 136 ? 0.524 0.550 0.667 -0.034 0.013  -0.029 465 GLU GGG CB  
8715  C CG  . GLU G 136 ? 0.534 0.544 0.690 -0.032 0.011  -0.032 465 GLU GGG CG  
8716  C CD  . GLU G 136 ? 0.567 0.568 0.736 -0.035 0.011  -0.020 465 GLU GGG CD  
8717  O OE1 . GLU G 136 ? 0.526 0.532 0.695 -0.040 0.014  -0.008 465 GLU GGG OE1 
8718  O OE2 . GLU G 136 ? 0.657 0.642 0.835 -0.033 0.009  -0.021 465 GLU GGG OE2 
8719  N N   . ARG G 137 ? 0.510 0.538 0.639 -0.019 0.015  -0.046 466 ARG GGG N   
8720  C CA  . ARG G 137 ? 0.497 0.530 0.626 -0.012 0.018  -0.046 466 ARG GGG CA  
8721  C C   . ARG G 137 ? 0.509 0.532 0.656 -0.007 0.018  -0.043 466 ARG GGG C   
8722  O O   . ARG G 137 ? 0.517 0.524 0.668 -0.007 0.018  -0.051 466 ARG GGG O   
8723  C CB  . ARG G 137 ? 0.489 0.524 0.610 -0.010 0.022  -0.059 466 ARG GGG CB  
8724  C CG  . ARG G 137 ? 0.519 0.564 0.643 -0.004 0.027  -0.058 466 ARG GGG CG  
8725  C CD  . ARG G 137 ? 0.561 0.608 0.668 -0.004 0.032  -0.069 466 ARG GGG CD  
8726  N NE  . ARG G 137 ? 0.587 0.645 0.698 0.001  0.040  -0.068 466 ARG GGG NE  
8727  C CZ  . ARG G 137 ? 0.685 0.740 0.804 0.009  0.049  -0.074 466 ARG GGG CZ  
8728  N NH1 . ARG G 137 ? 0.722 0.760 0.845 0.013  0.051  -0.082 466 ARG GGG NH1 
8729  N NH2 . ARG G 137 ? 0.711 0.781 0.837 0.013  0.057  -0.072 466 ARG GGG NH2 
8730  N N   . ASP G 138 ? 0.492 0.520 0.647 -0.004 0.017  -0.032 467 ASP GGG N   
8731  C CA  . ASP G 138 ? 0.489 0.508 0.663 0.003  0.015  -0.026 467 ASP GGG CA  
8732  C C   . ASP G 138 ? 0.492 0.522 0.677 0.011  0.017  -0.025 467 ASP GGG C   
8733  O O   . ASP G 138 ? 0.492 0.536 0.675 0.009  0.013  -0.016 467 ASP GGG O   
8734  C CB  . ASP G 138 ? 0.492 0.504 0.666 -0.001 0.010  -0.011 467 ASP GGG CB  
8735  C CG  . ASP G 138 ? 0.501 0.501 0.694 0.004  0.007  -0.003 467 ASP GGG CG  
8736  O OD1 . ASP G 138 ? 0.492 0.490 0.700 0.013  0.010  -0.009 467 ASP GGG OD1 
8737  O OD2 . ASP G 138 ? 0.500 0.491 0.691 0.001  0.003  0.009  467 ASP GGG OD2 
8738  N N   . ILE G 139 ? 0.502 0.527 0.701 0.019  0.024  -0.033 468 ILE GGG N   
8739  C CA  . ILE G 139 ? 0.485 0.524 0.703 0.029  0.028  -0.032 468 ILE GGG CA  
8740  C C   . ILE G 139 ? 0.487 0.515 0.730 0.039  0.028  -0.025 468 ILE GGG C   
8741  O O   . ILE G 139 ? 0.510 0.549 0.776 0.049  0.033  -0.024 468 ILE GGG O   
8742  C CB  . ILE G 139 ? 0.520 0.561 0.730 0.032  0.041  -0.047 468 ILE GGG CB  
8743  C CG1 . ILE G 139 ? 0.541 0.557 0.742 0.036  0.047  -0.062 468 ILE GGG CG1 
8744  C CG2 . ILE G 139 ? 0.529 0.582 0.715 0.023  0.040  -0.050 468 ILE GGG CG2 
8745  C CD1 . ILE G 139 ? 0.578 0.592 0.772 0.042  0.060  -0.077 468 ILE GGG CD1 
8746  N N   . SER G 140 ? 0.483 0.493 0.726 0.036  0.021  -0.020 469 SER GGG N   
8747  C CA  . SER G 140 ? 0.485 0.481 0.751 0.046  0.019  -0.011 469 SER GGG CA  
8748  C C   . SER G 140 ? 0.483 0.498 0.766 0.049  0.010  0.007  469 SER GGG C   
8749  O O   . SER G 140 ? 0.490 0.520 0.759 0.040  0.002  0.014  469 SER GGG O   
8750  C CB  . SER G 140 ? 0.491 0.463 0.750 0.039  0.014  -0.008 469 SER GGG CB  
8751  O OG  . SER G 140 ? 0.501 0.479 0.747 0.030  0.006  0.006  469 SER GGG OG  
8752  N N   . THR G 141 ? 0.482 0.493 0.794 0.061  0.009  0.014  470 THR GGG N   
8753  C CA  . THR G 141 ? 0.499 0.527 0.832 0.065  -0.003 0.033  470 THR GGG CA  
8754  C C   . THR G 141 ? 0.522 0.531 0.871 0.072  -0.011 0.047  470 THR GGG C   
8755  O O   . THR G 141 ? 0.548 0.564 0.928 0.084  -0.014 0.057  470 THR GGG O   
8756  C CB  . THR G 141 ? 0.499 0.552 0.860 0.075  0.003  0.031  470 THR GGG CB  
8757  O OG1 . THR G 141 ? 0.495 0.536 0.874 0.089  0.019  0.019  470 THR GGG OG1 
8758  C CG2 . THR G 141 ? 0.485 0.558 0.829 0.066  0.008  0.022  470 THR GGG CG2 
8759  N N   . GLU G 142 ? 0.556 0.541 0.884 0.064  -0.012 0.048  471 GLU GGG N   
8760  C CA  . GLU G 142 ? 0.588 0.549 0.926 0.068  -0.019 0.061  471 GLU GGG CA  
8761  C C   . GLU G 142 ? 0.602 0.573 0.935 0.064  -0.036 0.084  471 GLU GGG C   
8762  O O   . GLU G 142 ? 0.626 0.610 0.933 0.052  -0.040 0.086  471 GLU GGG O   
8763  C CB  . GLU G 142 ? 0.625 0.558 0.942 0.058  -0.015 0.055  471 GLU GGG CB  
8764  C CG  . GLU G 142 ? 0.665 0.587 0.981 0.059  -0.001 0.032  471 GLU GGG CG  
8765  C CD  . GLU G 142 ? 0.715 0.621 1.056 0.075  0.006  0.023  471 GLU GGG CD  
8766  O OE1 . GLU G 142 ? 0.743 0.626 1.099 0.081  0.003  0.033  471 GLU GGG OE1 
8767  O OE2 . GLU G 142 ? 0.715 0.631 1.061 0.083  0.017  0.007  471 GLU GGG OE2 
8768  N N   . ILE G 143 ? 0.624 0.587 0.979 0.073  -0.045 0.101  472 ILE GGG N   
8769  C CA  . ILE G 143 ? 0.639 0.605 0.987 0.070  -0.064 0.125  472 ILE GGG CA  
8770  C C   . ILE G 143 ? 0.635 0.584 0.944 0.055  -0.065 0.131  472 ILE GGG C   
8771  O O   . ILE G 143 ? 0.634 0.558 0.940 0.054  -0.057 0.128  472 ILE GGG O   
8772  C CB  . ILE G 143 ? 0.676 0.634 1.058 0.084  -0.073 0.142  472 ILE GGG CB  
8773  C CG1 . ILE G 143 ? 0.674 0.654 1.100 0.100  -0.069 0.137  472 ILE GGG CG1 
8774  C CG2 . ILE G 143 ? 0.690 0.648 1.059 0.079  -0.095 0.168  472 ILE GGG CG2 
8775  C CD1 . ILE G 143 ? 0.663 0.679 1.091 0.095  -0.074 0.135  472 ILE GGG CD1 
8776  N N   . TYR G 144 ? 0.625 0.584 0.904 0.045  -0.073 0.138  473 TYR GGG N   
8777  C CA  . TYR G 144 ? 0.638 0.583 0.877 0.031  -0.072 0.144  473 TYR GGG CA  
8778  C C   . TYR G 144 ? 0.677 0.604 0.907 0.032  -0.085 0.169  473 TYR GGG C   
8779  O O   . TYR G 144 ? 0.710 0.647 0.945 0.035  -0.102 0.182  473 TYR GGG O   
8780  C CB  . TYR G 144 ? 0.631 0.592 0.839 0.021  -0.072 0.137  473 TYR GGG CB  
8781  C CG  . TYR G 144 ? 0.642 0.590 0.809 0.009  -0.069 0.143  473 TYR GGG CG  
8782  C CD1 . TYR G 144 ? 0.630 0.572 0.786 0.003  -0.053 0.132  473 TYR GGG CD1 
8783  C CD2 . TYR G 144 ? 0.652 0.595 0.789 0.005  -0.082 0.160  473 TYR GGG CD2 
8784  C CE1 . TYR G 144 ? 0.643 0.575 0.765 -0.007 -0.047 0.139  473 TYR GGG CE1 
8785  C CE2 . TYR G 144 ? 0.663 0.593 0.758 -0.005 -0.076 0.165  473 TYR GGG CE2 
8786  C CZ  . TYR G 144 ? 0.650 0.576 0.740 -0.010 -0.057 0.155  473 TYR GGG CZ  
8787  O OH  . TYR G 144 ? 0.696 0.610 0.749 -0.019 -0.049 0.161  473 TYR GGG OH  
8788  N N   . GLN G 145 ? 0.673 0.575 0.893 0.027  -0.078 0.175  474 GLN GGG N   
8789  C CA  . GLN G 145 ? 0.707 0.589 0.911 0.025  -0.089 0.201  474 GLN GGG CA  
8790  C C   . GLN G 145 ? 0.742 0.623 0.895 0.013  -0.090 0.208  474 GLN GGG C   
8791  O O   . GLN G 145 ? 0.747 0.619 0.881 0.003  -0.074 0.202  474 GLN GGG O   
8792  C CB  . GLN G 145 ? 0.711 0.564 0.925 0.026  -0.081 0.206  474 GLN GGG CB  
8793  C CG  . GLN G 145 ? 0.749 0.580 0.941 0.022  -0.090 0.234  474 GLN GGG CG  
8794  C CD  . GLN G 145 ? 0.766 0.568 0.975 0.023  -0.084 0.242  474 GLN GGG CD  
8795  O OE1 . GLN G 145 ? 0.773 0.570 1.016 0.030  -0.077 0.228  474 GLN GGG OE1 
8796  N NE2 . GLN G 145 ? 0.811 0.591 0.995 0.017  -0.086 0.264  474 GLN GGG NE2 
8797  N N   . ALA G 146 ? 0.785 0.674 0.920 0.012  -0.107 0.218  475 ALA GGG N   
8798  C CA  . ALA G 146 ? 0.819 0.706 0.901 0.001  -0.110 0.223  475 ALA GGG CA  
8799  C C   . ALA G 146 ? 0.892 0.752 0.941 -0.003 -0.116 0.248  475 ALA GGG C   
8800  O O   . ALA G 146 ? 0.939 0.789 0.939 -0.013 -0.112 0.253  475 ALA GGG O   
8801  C CB  . ALA G 146 ? 0.811 0.717 0.887 0.001  -0.127 0.221  475 ALA GGG CB  
8802  N N   . GLY G 147 ? 0.913 0.759 0.987 0.004  -0.124 0.264  476 GLY GGG N   
8803  C CA  . GLY G 147 ? 0.992 0.812 1.036 0.001  -0.133 0.291  476 GLY GGG CA  
8804  C C   . GLY G 147 ? 1.019 0.817 1.084 0.004  -0.123 0.301  476 GLY GGG C   
8805  O O   . GLY G 147 ? 1.016 0.816 1.115 0.006  -0.108 0.284  476 GLY GGG O   
8806  N N   . SER G 148 ? 1.070 0.843 1.111 0.002  -0.132 0.328  477 SER GGG N   
8807  C CA  . SER G 148 ? 1.100 0.845 1.154 0.003  -0.124 0.343  477 SER GGG CA  
8808  C C   . SER G 148 ? 1.080 0.826 1.196 0.017  -0.129 0.337  477 SER GGG C   
8809  O O   . SER G 148 ? 1.057 0.789 1.196 0.016  -0.114 0.331  477 SER GGG O   
8810  C CB  . SER G 148 ? 1.160 0.880 1.175 -0.000 -0.138 0.374  477 SER GGG CB  
8811  O OG  . SER G 148 ? 1.229 0.921 1.255 -0.001 -0.130 0.390  477 SER GGG OG  
8812  N N   . THR G 149 ? 1.064 0.824 1.205 0.029  -0.149 0.341  478 THR GGG N   
8813  C CA  . THR G 149 ? 1.042 0.799 1.239 0.046  -0.155 0.341  478 THR GGG CA  
8814  C C   . THR G 149 ? 0.974 0.746 1.207 0.049  -0.136 0.309  478 THR GGG C   
8815  O O   . THR G 149 ? 0.930 0.727 1.154 0.045  -0.131 0.290  478 THR GGG O   
8816  C CB  . THR G 149 ? 1.049 0.824 1.268 0.058  -0.180 0.353  478 THR GGG CB  
8817  O OG1 . THR G 149 ? 1.122 0.887 1.298 0.051  -0.200 0.379  478 THR GGG OG1 
8818  C CG2 . THR G 149 ? 1.059 0.823 1.332 0.076  -0.186 0.361  478 THR GGG CG2 
8819  N N   . PRO G 150 ? 0.985 0.738 1.253 0.057  -0.127 0.304  479 PRO GGG N   
8820  C CA  . PRO G 150 ? 0.956 0.720 1.256 0.063  -0.112 0.274  479 PRO GGG CA  
8821  C C   . PRO G 150 ? 0.950 0.742 1.283 0.078  -0.122 0.268  479 PRO GGG C   
8822  O O   . PRO G 150 ? 0.982 0.776 1.328 0.088  -0.140 0.288  479 PRO GGG O   
8823  C CB  . PRO G 150 ? 0.980 0.709 1.303 0.066  -0.103 0.274  479 PRO GGG CB  
8824  C CG  . PRO G 150 ? 1.021 0.726 1.344 0.072  -0.119 0.306  479 PRO GGG CG  
8825  C CD  . PRO G 150 ? 1.030 0.747 1.309 0.061  -0.130 0.325  479 PRO GGG CD  
8826  N N   . CYS G 151 ? 0.941 0.755 1.289 0.080  -0.109 0.241  480 CYS GGG N   
8827  C CA  . CYS G 151 ? 0.930 0.776 1.308 0.093  -0.115 0.234  480 CYS GGG CA  
8828  C C   . CYS G 151 ? 0.926 0.764 1.353 0.112  -0.108 0.226  480 CYS GGG C   
8829  O O   . CYS G 151 ? 0.901 0.762 1.360 0.125  -0.115 0.229  480 CYS GGG O   
8830  C CB  . CYS G 151 ? 0.924 0.796 1.285 0.084  -0.105 0.211  480 CYS GGG CB  
8831  S SG  . CYS G 151 ? 1.002 0.886 1.310 0.065  -0.116 0.222  480 CYS GGG SG  
8832  N N   . ASN G 152 ? 0.960 0.766 1.392 0.114  -0.095 0.217  481 ASN GGG N   
8833  C CA  . ASN G 152 ? 0.968 0.757 1.442 0.133  -0.086 0.208  481 ASN GGG CA  
8834  C C   . ASN G 152 ? 0.959 0.779 1.458 0.145  -0.076 0.188  481 ASN GGG C   
8835  O O   . ASN G 152 ? 0.958 0.781 1.500 0.165  -0.076 0.191  481 ASN GGG O   
8836  C CB  . ASN G 152 ? 0.976 0.748 1.477 0.148  -0.100 0.234  481 ASN GGG CB  
8837  C CG  . ASN G 152 ? 0.997 0.741 1.534 0.166  -0.088 0.224  481 ASN GGG CG  
8838  O OD1 . ASN G 152 ? 0.984 0.702 1.511 0.161  -0.072 0.204  481 ASN GGG OD1 
8839  N ND2 . ASN G 152 ? 1.013 0.759 1.593 0.187  -0.095 0.237  481 ASN GGG ND2 
8840  N N   . GLY G 153 ? 0.943 0.786 1.420 0.133  -0.069 0.170  482 GLY GGG N   
8841  C CA  . GLY G 153 ? 0.931 0.803 1.425 0.141  -0.057 0.150  482 GLY GGG CA  
8842  C C   . GLY G 153 ? 0.951 0.857 1.480 0.153  -0.069 0.165  482 GLY GGG C   
8843  O O   . GLY G 153 ? 0.965 0.889 1.526 0.166  -0.057 0.153  482 GLY GGG O   
8844  N N   . VAL G 154 ? 0.956 0.872 1.478 0.147  -0.091 0.190  483 VAL GGG N   
8845  C CA  . VAL G 154 ? 0.902 0.853 1.454 0.154  -0.108 0.206  483 VAL GGG CA  
8846  C C   . VAL G 154 ? 0.869 0.839 1.381 0.134  -0.123 0.213  483 VAL GGG C   
8847  O O   . VAL G 154 ? 0.870 0.819 1.338 0.120  -0.127 0.219  483 VAL GGG O   
8848  C CB  . VAL G 154 ? 0.952 0.892 1.535 0.168  -0.125 0.233  483 VAL GGG CB  
8849  C CG1 . VAL G 154 ? 0.964 0.939 1.570 0.170  -0.149 0.255  483 VAL GGG CG1 
8850  C CG2 . VAL G 154 ? 0.968 0.890 1.596 0.191  -0.109 0.227  483 VAL GGG CG2 
8851  N N   . GLU G 155 ? 0.857 0.864 1.384 0.133  -0.129 0.212  484 GLU GGG N   
8852  C CA  . GLU G 155 ? 0.852 0.877 1.344 0.115  -0.145 0.218  484 GLU GGG CA  
8853  C C   . GLU G 155 ? 0.870 0.894 1.361 0.114  -0.175 0.248  484 GLU GGG C   
8854  O O   . GLU G 155 ? 0.884 0.909 1.419 0.130  -0.184 0.263  484 GLU GGG O   
8855  C CB  . GLU G 155 ? 0.852 0.917 1.369 0.115  -0.143 0.208  484 GLU GGG CB  
8856  C CG  . GLU G 155 ? 0.843 0.913 1.372 0.120  -0.114 0.182  484 GLU GGG CG  
8857  C CD  . GLU G 155 ? 0.845 0.946 1.370 0.110  -0.111 0.170  484 GLU GGG CD  
8858  O OE1 . GLU G 155 ? 0.859 0.970 1.357 0.095  -0.129 0.178  484 GLU GGG OE1 
8859  O OE2 . GLU G 155 ? 0.804 0.917 1.348 0.117  -0.090 0.153  484 GLU GGG OE2 
8860  N N   . GLY G 156 ? 0.865 0.885 1.307 0.096  -0.190 0.255  485 GLY GGG N   
8861  C CA  . GLY G 156 ? 0.906 0.926 1.337 0.092  -0.221 0.282  485 GLY GGG CA  
8862  C C   . GLY G 156 ? 0.963 0.964 1.322 0.073  -0.229 0.286  485 GLY GGG C   
8863  O O   . GLY G 156 ? 1.015 1.015 1.343 0.062  -0.212 0.266  485 GLY GGG O   
8864  N N   . PHE G 157 ? 1.049 1.034 1.382 0.069  -0.253 0.310  486 PHE GGG N   
8865  C CA  . PHE G 157 ? 1.098 1.059 1.359 0.052  -0.259 0.317  486 PHE GGG CA  
8866  C C   . PHE G 157 ? 1.069 1.005 1.301 0.048  -0.229 0.302  486 PHE GGG C   
8867  O O   . PHE G 157 ? 1.053 0.972 1.307 0.057  -0.217 0.304  486 PHE GGG O   
8868  C CB  . PHE G 157 ? 1.178 1.121 1.423 0.053  -0.287 0.348  486 PHE GGG CB  
8869  C CG  . PHE G 157 ? 1.265 1.177 1.432 0.037  -0.293 0.357  486 PHE GGG CG  
8870  C CD1 . PHE G 157 ? 1.306 1.219 1.421 0.022  -0.287 0.343  486 PHE GGG CD1 
8871  C CD2 . PHE G 157 ? 1.353 1.236 1.497 0.039  -0.304 0.383  486 PHE GGG CD2 
8872  C CE1 . PHE G 157 ? 1.361 1.244 1.402 0.009  -0.290 0.351  486 PHE GGG CE1 
8873  C CE2 . PHE G 157 ? 1.414 1.268 1.483 0.025  -0.308 0.393  486 PHE GGG CE2 
8874  C CZ  . PHE G 157 ? 1.411 1.266 1.429 0.011  -0.300 0.377  486 PHE GGG CZ  
8875  N N   . ASN G 158 ? 1.048 0.983 1.235 0.034  -0.218 0.286  487 ASN GGG N   
8876  C CA  . ASN G 158 ? 1.051 0.966 1.207 0.027  -0.191 0.273  487 ASN GGG CA  
8877  C C   . ASN G 158 ? 0.989 0.912 1.190 0.036  -0.169 0.253  487 ASN GGG C   
8878  O O   . ASN G 158 ? 0.963 0.869 1.151 0.032  -0.149 0.246  487 ASN GGG O   
8879  C CB  . ASN G 158 ? 1.090 0.972 1.211 0.023  -0.191 0.292  487 ASN GGG CB  
8880  C CG  . ASN G 158 ? 1.137 1.006 1.198 0.012  -0.208 0.307  487 ASN GGG CG  
8881  O OD1 . ASN G 158 ? 1.161 1.038 1.189 0.002  -0.207 0.296  487 ASN GGG OD1 
8882  N ND2 . ASN G 158 ? 1.240 1.087 1.285 0.013  -0.222 0.333  487 ASN GGG ND2 
8883  N N   . CYS G 159 ? 0.934 0.881 1.184 0.047  -0.171 0.246  488 CYS GGG N   
8884  C CA  . CYS G 159 ? 0.888 0.840 1.179 0.057  -0.151 0.227  488 CYS GGG CA  
8885  C C   . CYS G 159 ? 0.847 0.832 1.158 0.058  -0.147 0.209  488 CYS GGG C   
8886  O O   . CYS G 159 ? 0.846 0.852 1.201 0.069  -0.154 0.213  488 CYS GGG O   
8887  C CB  . CYS G 159 ? 0.885 0.828 1.221 0.074  -0.154 0.239  488 CYS GGG CB  
8888  S SG  . CYS G 159 ? 0.901 0.801 1.218 0.072  -0.150 0.253  488 CYS GGG SG  
8889  N N   . TYR G 160 ? 0.812 0.802 1.092 0.046  -0.135 0.192  489 TYR GGG N   
8890  C CA  . TYR G 160 ? 0.741 0.759 1.025 0.042  -0.135 0.180  489 TYR GGG CA  
8891  C C   . TYR G 160 ? 0.691 0.717 0.998 0.048  -0.113 0.157  489 TYR GGG C   
8892  O O   . TYR G 160 ? 0.688 0.696 0.984 0.047  -0.096 0.146  489 TYR GGG O   
8893  C CB  . TYR G 160 ? 0.755 0.768 0.985 0.026  -0.139 0.178  489 TYR GGG CB  
8894  C CG  . TYR G 160 ? 0.825 0.825 1.024 0.020  -0.161 0.199  489 TYR GGG CG  
8895  C CD1 . TYR G 160 ? 0.866 0.877 1.089 0.025  -0.184 0.217  489 TYR GGG CD1 
8896  C CD2 . TYR G 160 ? 0.869 0.845 1.016 0.010  -0.157 0.203  489 TYR GGG CD2 
8897  C CE1 . TYR G 160 ? 0.916 0.913 1.106 0.018  -0.207 0.237  489 TYR GGG CE1 
8898  C CE2 . TYR G 160 ? 0.939 0.899 1.049 0.004  -0.176 0.222  489 TYR GGG CE2 
8899  C CZ  . TYR G 160 ? 0.953 0.923 1.083 0.008  -0.202 0.239  489 TYR GGG CZ  
8900  O OH  . TYR G 160 ? 1.002 0.954 1.091 0.002  -0.222 0.259  489 TYR GGG OH  
8901  N N   . PHE G 161 ? 0.647 0.700 0.985 0.053  -0.113 0.151  490 PHE GGG N   
8902  C CA  . PHE G 161 ? 0.606 0.672 0.954 0.054  -0.093 0.129  490 PHE GGG CA  
8903  C C   . PHE G 161 ? 0.582 0.645 0.884 0.039  -0.089 0.119  490 PHE GGG C   
8904  O O   . PHE G 161 ? 0.600 0.668 0.880 0.029  -0.104 0.127  490 PHE GGG O   
8905  C CB  . PHE G 161 ? 0.590 0.688 0.981 0.062  -0.095 0.130  490 PHE GGG CB  
8906  C CG  . PHE G 161 ? 0.556 0.666 0.958 0.065  -0.073 0.109  490 PHE GGG CG  
8907  C CD1 . PHE G 161 ? 0.567 0.667 0.990 0.078  -0.055 0.098  490 PHE GGG CD1 
8908  C CD2 . PHE G 161 ? 0.537 0.664 0.926 0.055  -0.071 0.101  490 PHE GGG CD2 
8909  C CE1 . PHE G 161 ? 0.568 0.675 0.995 0.081  -0.035 0.079  490 PHE GGG CE1 
8910  C CE2 . PHE G 161 ? 0.527 0.663 0.923 0.058  -0.051 0.083  490 PHE GGG CE2 
8911  C CZ  . PHE G 161 ? 0.541 0.667 0.954 0.071  -0.033 0.073  490 PHE GGG CZ  
8912  N N   . PRO G 162 ? 0.563 0.615 0.848 0.036  -0.071 0.102  491 PRO GGG N   
8913  C CA  . PRO G 162 ? 0.553 0.597 0.795 0.023  -0.068 0.096  491 PRO GGG CA  
8914  C C   . PRO G 162 ? 0.555 0.618 0.787 0.016  -0.066 0.086  491 PRO GGG C   
8915  O O   . PRO G 162 ? 0.574 0.630 0.770 0.006  -0.065 0.082  491 PRO GGG O   
8916  C CB  . PRO G 162 ? 0.548 0.575 0.787 0.024  -0.051 0.083  491 PRO GGG CB  
8917  C CG  . PRO G 162 ? 0.549 0.583 0.824 0.037  -0.042 0.074  491 PRO GGG CG  
8918  C CD  . PRO G 162 ? 0.560 0.604 0.866 0.046  -0.054 0.089  491 PRO GGG CD  
8919  N N   . LEU G 163 ? 0.553 0.638 0.816 0.022  -0.065 0.082  492 LEU GGG N   
8920  C CA  . LEU G 163 ? 0.537 0.639 0.793 0.014  -0.063 0.073  492 LEU GGG CA  
8921  C C   . LEU G 163 ? 0.517 0.634 0.779 0.009  -0.083 0.087  492 LEU GGG C   
8922  O O   . LEU G 163 ? 0.529 0.653 0.820 0.016  -0.094 0.100  492 LEU GGG O   
8923  C CB  . LEU G 163 ? 0.536 0.653 0.820 0.022  -0.047 0.061  492 LEU GGG CB  
8924  C CG  . LEU G 163 ? 0.554 0.656 0.831 0.027  -0.029 0.046  492 LEU GGG CG  
8925  C CD1 . LEU G 163 ? 0.543 0.659 0.838 0.033  -0.014 0.033  492 LEU GGG CD1 
8926  C CD2 . LEU G 163 ? 0.540 0.626 0.776 0.016  -0.027 0.039  492 LEU GGG CD2 
8927  N N   . GLN G 164 ? 0.760 0.595 0.886 0.039  -0.155 0.130  493 GLN GGG N   
8928  C CA  . GLN G 164 ? 0.751 0.619 0.891 0.033  -0.164 0.144  493 GLN GGG CA  
8929  C C   . GLN G 164 ? 0.696 0.609 0.853 0.037  -0.143 0.131  493 GLN GGG C   
8930  O O   . GLN G 164 ? 0.641 0.557 0.784 0.034  -0.122 0.115  493 GLN GGG O   
8931  C CB  . GLN G 164 ? 0.795 0.649 0.896 0.001  -0.175 0.159  493 GLN GGG CB  
8932  C CG  . GLN G 164 ? 0.798 0.679 0.904 -0.011 -0.186 0.174  493 GLN GGG CG  
8933  C CD  . GLN G 164 ? 0.844 0.725 0.981 0.005  -0.211 0.191  493 GLN GGG CD  
8934  O OE1 . GLN G 164 ? 0.854 0.770 1.030 0.023  -0.211 0.189  493 GLN GGG OE1 
8935  N NE2 . GLN G 164 ? 0.893 0.737 1.013 -0.002 -0.233 0.207  493 GLN GGG NE2 
8936  N N   . SER G 165 ? 0.675 0.623 0.861 0.043  -0.149 0.139  494 SER GGG N   
8937  C CA  . SER G 165 ? 0.633 0.626 0.837 0.044  -0.133 0.131  494 SER GGG CA  
8938  C C   . SER G 165 ? 0.603 0.603 0.778 0.015  -0.132 0.136  494 SER GGG C   
8939  O O   . SER G 165 ? 0.603 0.588 0.759 -0.001 -0.150 0.151  494 SER GGG O   
8940  C CB  . SER G 165 ? 0.649 0.678 0.901 0.065  -0.141 0.137  494 SER GGG CB  
8941  O OG  . SER G 165 ? 0.742 0.752 1.008 0.076  -0.165 0.151  494 SER GGG OG  
8942  N N   . TYR G 166 ? 0.585 0.605 0.755 0.009  -0.113 0.125  495 TYR GGG N   
8943  C CA  . TYR G 166 ? 0.596 0.621 0.740 -0.015 -0.112 0.127  495 TYR GGG CA  
8944  C C   . TYR G 166 ? 0.629 0.684 0.793 -0.022 -0.125 0.141  495 TYR GGG C   
8945  O O   . TYR G 166 ? 0.658 0.706 0.798 -0.044 -0.136 0.150  495 TYR GGG O   
8946  C CB  . TYR G 166 ? 0.567 0.599 0.700 -0.018 -0.090 0.112  495 TYR GGG CB  
8947  C CG  . TYR G 166 ? 0.564 0.567 0.664 -0.025 -0.079 0.101  495 TYR GGG CG  
8948  C CD1 . TYR G 166 ? 0.582 0.566 0.647 -0.045 -0.083 0.105  495 TYR GGG CD1 
8949  C CD2 . TYR G 166 ? 0.568 0.566 0.673 -0.011 -0.065 0.088  495 TYR GGG CD2 
8950  C CE1 . TYR G 166 ? 0.588 0.553 0.627 -0.051 -0.073 0.096  495 TYR GGG CE1 
8951  C CE2 . TYR G 166 ? 0.579 0.554 0.655 -0.018 -0.057 0.080  495 TYR GGG CE2 
8952  C CZ  . TYR G 166 ? 0.576 0.537 0.621 -0.037 -0.060 0.084  495 TYR GGG CZ  
8953  O OH  . TYR G 166 ? 0.557 0.504 0.580 -0.044 -0.051 0.076  495 TYR GGG OH  
8954  N N   . GLY G 167 ? 0.636 0.725 0.842 -0.005 -0.125 0.142  496 GLY GGG N   
8955  C CA  . GLY G 167 ? 0.662 0.786 0.889 -0.014 -0.138 0.156  496 GLY GGG CA  
8956  C C   . GLY G 167 ? 0.644 0.773 0.846 -0.039 -0.133 0.154  496 GLY GGG C   
8957  O O   . GLY G 167 ? 0.677 0.791 0.852 -0.060 -0.146 0.163  496 GLY GGG O   
8958  N N   . PHE G 168 ? 0.610 0.754 0.817 -0.037 -0.114 0.143  497 PHE GGG N   
8959  C CA  . PHE G 168 ? 0.583 0.725 0.765 -0.058 -0.107 0.139  497 PHE GGG CA  
8960  C C   . PHE G 168 ? 0.588 0.768 0.794 -0.069 -0.117 0.151  497 PHE GGG C   
8961  O O   . PHE G 168 ? 0.596 0.814 0.840 -0.056 -0.111 0.152  497 PHE GGG O   
8962  C CB  . PHE G 168 ? 0.548 0.688 0.726 -0.050 -0.084 0.123  497 PHE GGG CB  
8963  C CG  . PHE G 168 ? 0.529 0.634 0.679 -0.044 -0.074 0.111  497 PHE GGG CG  
8964  C CD1 . PHE G 168 ? 0.526 0.599 0.637 -0.060 -0.077 0.109  497 PHE GGG CD1 
8965  C CD2 . PHE G 168 ? 0.505 0.609 0.667 -0.025 -0.061 0.101  497 PHE GGG CD2 
8966  C CE1 . PHE G 168 ? 0.530 0.577 0.618 -0.057 -0.067 0.098  497 PHE GGG CE1 
8967  C CE2 . PHE G 168 ? 0.491 0.565 0.628 -0.023 -0.053 0.091  497 PHE GGG CE2 
8968  C CZ  . PHE G 168 ? 0.506 0.553 0.607 -0.039 -0.056 0.090  497 PHE GGG CZ  
8969  N N   . GLN G 169 ? 0.611 0.781 0.794 -0.093 -0.131 0.159  498 GLN GGG N   
8970  C CA  . GLN G 169 ? 0.605 0.807 0.804 -0.110 -0.142 0.170  498 GLN GGG CA  
8971  C C   . GLN G 169 ? 0.599 0.781 0.764 -0.131 -0.136 0.163  498 GLN GGG C   
8972  O O   . GLN G 169 ? 0.595 0.736 0.717 -0.139 -0.133 0.153  498 GLN GGG O   
8973  C CB  . GLN G 169 ? 0.659 0.865 0.858 -0.122 -0.168 0.187  498 GLN GGG CB  
8974  C CG  . GLN G 169 ? 0.699 0.924 0.936 -0.098 -0.176 0.195  498 GLN GGG CG  
8975  C CD  . GLN G 169 ? 0.739 0.969 0.979 -0.109 -0.203 0.214  498 GLN GGG CD  
8976  O OE1 . GLN G 169 ? 0.768 0.962 0.971 -0.120 -0.214 0.216  498 GLN GGG OE1 
8977  N NE2 . GLN G 169 ? 0.784 1.062 1.069 -0.105 -0.216 0.228  498 GLN GGG NE2 
8978  N N   . PRO G 170 ? 0.585 0.795 0.767 -0.141 -0.134 0.167  499 PRO GGG N   
8979  C CA  . PRO G 170 ? 0.601 0.789 0.752 -0.160 -0.128 0.160  499 PRO GGG CA  
8980  C C   . PRO G 170 ? 0.642 0.793 0.750 -0.184 -0.143 0.160  499 PRO GGG C   
8981  O O   . PRO G 170 ? 0.649 0.764 0.722 -0.192 -0.137 0.149  499 PRO GGG O   
8982  C CB  . PRO G 170 ? 0.585 0.817 0.767 -0.170 -0.129 0.171  499 PRO GGG CB  
8983  C CG  . PRO G 170 ? 0.579 0.861 0.809 -0.160 -0.139 0.185  499 PRO GGG CG  
8984  C CD  . PRO G 170 ? 0.581 0.848 0.814 -0.135 -0.137 0.179  499 PRO GGG CD  
8985  N N   . THR G 171 ? 0.633 0.791 0.743 -0.192 -0.163 0.172  500 THR GGG N   
8986  C CA  . THR G 171 ? 0.670 0.796 0.737 -0.217 -0.179 0.173  500 THR GGG CA  
8987  C C   . THR G 171 ? 0.675 0.762 0.704 -0.211 -0.175 0.162  500 THR GGG C   
8988  O O   . THR G 171 ? 0.701 0.759 0.689 -0.230 -0.184 0.158  500 THR GGG O   
8989  C CB  . THR G 171 ? 0.689 0.846 0.775 -0.231 -0.204 0.192  500 THR GGG CB  
8990  O OG1 . THR G 171 ? 0.702 0.884 0.824 -0.208 -0.207 0.201  500 THR GGG OG1 
8991  C CG2 . THR G 171 ? 0.687 0.881 0.801 -0.245 -0.211 0.203  500 THR GGG CG2 
8992  N N   . ASN G 172 ? 0.656 0.742 0.698 -0.187 -0.162 0.156  501 ASN GGG N   
8993  C CA  . ASN G 172 ? 0.667 0.719 0.674 -0.183 -0.155 0.146  501 ASN GGG CA  
8994  C C   . ASN G 172 ? 0.674 0.690 0.636 -0.195 -0.145 0.129  501 ASN GGG C   
8995  O O   . ASN G 172 ? 0.655 0.669 0.620 -0.195 -0.136 0.122  501 ASN GGG O   
8996  C CB  . ASN G 172 ? 0.661 0.715 0.687 -0.157 -0.139 0.140  501 ASN GGG CB  
8997  C CG  . ASN G 172 ? 0.662 0.740 0.725 -0.142 -0.148 0.153  501 ASN GGG CG  
8998  O OD1 . ASN G 172 ? 0.666 0.762 0.744 -0.150 -0.168 0.168  501 ASN GGG OD1 
8999  N ND2 . ASN G 172 ? 0.654 0.732 0.734 -0.120 -0.135 0.147  501 ASN GGG ND2 
9000  N N   . GLY G 173 ? 0.690 0.679 0.612 -0.204 -0.147 0.123  502 GLY GGG N   
9001  C CA  . GLY G 173 ? 0.711 0.667 0.592 -0.207 -0.133 0.103  502 GLY GGG CA  
9002  C C   . GLY G 173 ? 0.703 0.658 0.598 -0.185 -0.112 0.091  502 GLY GGG C   
9003  O O   . GLY G 173 ? 0.661 0.635 0.587 -0.169 -0.107 0.097  502 GLY GGG O   
9004  N N   . VAL G 174 ? 0.737 0.669 0.609 -0.185 -0.099 0.074  503 VAL GGG N   
9005  C CA  . VAL G 174 ? 0.739 0.670 0.624 -0.165 -0.081 0.064  503 VAL GGG CA  
9006  C C   . VAL G 174 ? 0.753 0.692 0.646 -0.151 -0.071 0.062  503 VAL GGG C   
9007  O O   . VAL G 174 ? 0.680 0.633 0.600 -0.135 -0.061 0.063  503 VAL GGG O   
9008  C CB  . VAL G 174 ? 0.756 0.659 0.614 -0.166 -0.071 0.047  503 VAL GGG CB  
9009  C CG1 . VAL G 174 ? 0.797 0.681 0.619 -0.168 -0.065 0.032  503 VAL GGG CG1 
9010  C CG2 . VAL G 174 ? 0.730 0.637 0.608 -0.148 -0.057 0.041  503 VAL GGG CG2 
9011  N N   . GLY G 175 ? 0.784 0.713 0.650 -0.159 -0.073 0.061  504 GLY GGG N   
9012  C CA  . GLY G 175 ? 0.774 0.706 0.641 -0.151 -0.067 0.061  504 GLY GGG CA  
9013  C C   . GLY G 175 ? 0.741 0.692 0.644 -0.141 -0.074 0.076  504 GLY GGG C   
9014  O O   . GLY G 175 ? 0.750 0.702 0.661 -0.130 -0.065 0.074  504 GLY GGG O   
9015  N N   . TYR G 176 ? 0.745 0.710 0.668 -0.145 -0.088 0.089  505 TYR GGG N   
9016  C CA  . TYR G 176 ? 0.737 0.721 0.697 -0.133 -0.096 0.103  505 TYR GGG CA  
9017  C C   . TYR G 176 ? 0.698 0.704 0.694 -0.120 -0.090 0.103  505 TYR GGG C   
9018  O O   . TYR G 176 ? 0.656 0.683 0.686 -0.109 -0.096 0.112  505 TYR GGG O   
9019  C CB  . TYR G 176 ? 0.776 0.765 0.735 -0.146 -0.119 0.120  505 TYR GGG CB  
9020  C CG  . TYR G 176 ? 0.879 0.848 0.803 -0.159 -0.126 0.123  505 TYR GGG CG  
9021  C CD1 . TYR G 176 ? 0.913 0.877 0.842 -0.152 -0.129 0.130  505 TYR GGG CD1 
9022  C CD2 . TYR G 176 ? 0.956 0.911 0.840 -0.180 -0.130 0.119  505 TYR GGG CD2 
9023  C CE1 . TYR G 176 ? 0.962 0.909 0.856 -0.167 -0.136 0.135  505 TYR GGG CE1 
9024  C CE2 . TYR G 176 ? 1.001 0.942 0.850 -0.194 -0.136 0.122  505 TYR GGG CE2 
9025  C CZ  . TYR G 176 ? 1.033 0.972 0.888 -0.189 -0.139 0.132  505 TYR GGG CZ  
9026  O OH  . TYR G 176 ? 1.137 1.062 0.956 -0.205 -0.144 0.137  505 TYR GGG OH  
9027  N N   . GLN G 177 ? 0.653 0.656 0.642 -0.121 -0.079 0.092  506 GLN GGG N   
9028  C CA  . GLN G 177 ? 0.629 0.652 0.648 -0.111 -0.071 0.092  506 GLN GGG CA  
9029  C C   . GLN G 177 ? 0.598 0.623 0.628 -0.092 -0.056 0.084  506 GLN GGG C   
9030  O O   . GLN G 177 ? 0.593 0.600 0.603 -0.089 -0.048 0.075  506 GLN GGG O   
9031  C CB  . GLN G 177 ? 0.627 0.642 0.632 -0.122 -0.069 0.087  506 GLN GGG CB  
9032  C CG  . GLN G 177 ? 0.640 0.662 0.643 -0.142 -0.086 0.098  506 GLN GGG CG  
9033  C CD  . GLN G 177 ? 0.655 0.659 0.638 -0.155 -0.086 0.093  506 GLN GGG CD  
9034  O OE1 . GLN G 177 ? 0.621 0.617 0.603 -0.149 -0.074 0.085  506 GLN GGG OE1 
9035  N NE2 . GLN G 177 ? 0.684 0.678 0.648 -0.176 -0.101 0.097  506 GLN GGG NE2 
9036  N N   . PRO G 178 ? 0.569 0.618 0.630 -0.080 -0.050 0.086  507 PRO GGG N   
9037  C CA  . PRO G 178 ? 0.546 0.597 0.615 -0.063 -0.035 0.077  507 PRO GGG CA  
9038  C C   . PRO G 178 ? 0.537 0.575 0.588 -0.065 -0.023 0.066  507 PRO GGG C   
9039  O O   . PRO G 178 ? 0.531 0.569 0.577 -0.074 -0.024 0.068  507 PRO GGG O   
9040  C CB  . PRO G 178 ? 0.533 0.616 0.639 -0.051 -0.033 0.081  507 PRO GGG CB  
9041  C CG  . PRO G 178 ? 0.547 0.649 0.661 -0.065 -0.041 0.091  507 PRO GGG CG  
9042  C CD  . PRO G 178 ? 0.566 0.646 0.656 -0.082 -0.056 0.096  507 PRO GGG CD  
9043  N N   . TYR G 179 ? 0.527 0.552 0.568 -0.056 -0.014 0.057  508 TYR GGG N   
9044  C CA  . TYR G 179 ? 0.540 0.557 0.569 -0.053 -0.002 0.047  508 TYR GGG CA  
9045  C C   . TYR G 179 ? 0.507 0.534 0.550 -0.039 0.008  0.042  508 TYR GGG C   
9046  O O   . TYR G 179 ? 0.480 0.504 0.527 -0.033 0.007  0.041  508 TYR GGG O   
9047  C CB  . TYR G 179 ? 0.560 0.555 0.562 -0.058 -0.000 0.039  508 TYR GGG CB  
9048  C CG  . TYR G 179 ? 0.562 0.543 0.545 -0.071 -0.006 0.039  508 TYR GGG CG  
9049  C CD1 . TYR G 179 ? 0.583 0.562 0.561 -0.083 -0.019 0.047  508 TYR GGG CD1 
9050  C CD2 . TYR G 179 ? 0.560 0.527 0.528 -0.071 -0.001 0.031  508 TYR GGG CD2 
9051  C CE1 . TYR G 179 ? 0.590 0.554 0.548 -0.096 -0.026 0.045  508 TYR GGG CE1 
9052  C CE2 . TYR G 179 ? 0.604 0.553 0.553 -0.082 -0.007 0.028  508 TYR GGG CE2 
9053  C CZ  . TYR G 179 ? 0.629 0.575 0.570 -0.096 -0.019 0.035  508 TYR GGG CZ  
9054  O OH  . TYR G 179 ? 0.620 0.546 0.539 -0.108 -0.026 0.032  508 TYR GGG OH  
9055  N N   . ARG G 180 ? 0.529 0.567 0.578 -0.036 0.015  0.040  509 ARG GGG N   
9056  C CA  . ARG G 180 ? 0.553 0.597 0.608 -0.024 0.026  0.033  509 ARG GGG CA  
9057  C C   . ARG G 180 ? 0.528 0.555 0.564 -0.024 0.031  0.025  509 ARG GGG C   
9058  O O   . ARG G 180 ? 0.537 0.554 0.560 -0.030 0.029  0.025  509 ARG GGG O   
9059  C CB  . ARG G 180 ? 0.536 0.601 0.603 -0.024 0.031  0.036  509 ARG GGG CB  
9060  C CG  . ARG G 180 ? 0.570 0.662 0.662 -0.021 0.029  0.043  509 ARG GGG CG  
9061  C CD  . ARG G 180 ? 0.539 0.658 0.643 -0.021 0.037  0.045  509 ARG GGG CD  
9062  N NE  . ARG G 180 ? 0.529 0.677 0.660 -0.016 0.035  0.050  509 ARG GGG NE  
9063  C CZ  . ARG G 180 ? 0.495 0.676 0.644 -0.011 0.044  0.050  509 ARG GGG CZ  
9064  N NH1 . ARG G 180 ? 0.499 0.687 0.639 -0.013 0.054  0.047  509 ARG GGG NH1 
9065  N NH2 . ARG G 180 ? 0.459 0.669 0.636 -0.004 0.042  0.054  509 ARG GGG NH2 
9066  N N   . VAL G 181 ? 0.507 0.533 0.542 -0.017 0.035  0.019  510 VAL GGG N   
9067  C CA  . VAL G 181 ? 0.482 0.498 0.503 -0.016 0.040  0.012  510 VAL GGG CA  
9068  C C   . VAL G 181 ? 0.478 0.502 0.503 -0.009 0.047  0.007  510 VAL GGG C   
9069  O O   . VAL G 181 ? 0.482 0.513 0.518 -0.003 0.048  0.006  510 VAL GGG O   
9070  C CB  . VAL G 181 ? 0.470 0.475 0.483 -0.020 0.036  0.011  510 VAL GGG CB  
9071  C CG1 . VAL G 181 ? 0.476 0.477 0.477 -0.022 0.041  0.005  510 VAL GGG CG1 
9072  C CG2 . VAL G 181 ? 0.487 0.485 0.495 -0.028 0.028  0.017  510 VAL GGG CG2 
9073  N N   . VAL G 182 ? 0.471 0.496 0.489 -0.009 0.050  0.004  511 VAL GGG N   
9074  C CA  . VAL G 182 ? 0.456 0.487 0.473 -0.005 0.055  -0.001 511 VAL GGG CA  
9075  C C   . VAL G 182 ? 0.459 0.485 0.467 -0.006 0.056  -0.006 511 VAL GGG C   
9076  O O   . VAL G 182 ? 0.471 0.494 0.474 -0.007 0.055  -0.005 511 VAL GGG O   
9077  C CB  . VAL G 182 ? 0.461 0.502 0.479 -0.003 0.058  0.002  511 VAL GGG CB  
9078  C CG1 . VAL G 182 ? 0.476 0.523 0.489 -0.001 0.062  -0.003 511 VAL GGG CG1 
9079  C CG2 . VAL G 182 ? 0.467 0.519 0.494 -0.004 0.059  0.006  511 VAL GGG CG2 
9080  N N   . VAL G 183 ? 0.454 0.480 0.460 -0.007 0.057  -0.010 512 VAL GGG N   
9081  C CA  . VAL G 183 ? 0.473 0.502 0.473 -0.010 0.058  -0.014 512 VAL GGG CA  
9082  C C   . VAL G 183 ? 0.473 0.512 0.473 -0.008 0.060  -0.017 512 VAL GGG C   
9083  O O   . VAL G 183 ? 0.479 0.516 0.478 -0.007 0.060  -0.019 512 VAL GGG O   
9084  C CB  . VAL G 183 ? 0.495 0.516 0.491 -0.017 0.055  -0.014 512 VAL GGG CB  
9085  C CG1 . VAL G 183 ? 0.493 0.523 0.484 -0.023 0.056  -0.017 512 VAL GGG CG1 
9086  C CG2 . VAL G 183 ? 0.519 0.531 0.513 -0.020 0.051  -0.010 512 VAL GGG CG2 
9087  N N   . LEU G 184 ? 0.466 0.515 0.467 -0.006 0.060  -0.016 513 LEU GGG N   
9088  C CA  . LEU G 184 ? 0.464 0.524 0.464 -0.005 0.060  -0.017 513 LEU GGG CA  
9089  C C   . LEU G 184 ? 0.483 0.552 0.483 -0.010 0.059  -0.020 513 LEU GGG C   
9090  O O   . LEU G 184 ? 0.470 0.546 0.474 -0.009 0.060  -0.020 513 LEU GGG O   
9091  C CB  . LEU G 184 ? 0.456 0.520 0.458 0.001  0.058  -0.012 513 LEU GGG CB  
9092  C CG  . LEU G 184 ? 0.457 0.514 0.459 0.002  0.058  -0.007 513 LEU GGG CG  
9093  C CD1 . LEU G 184 ? 0.469 0.525 0.471 0.006  0.055  -0.001 513 LEU GGG CD1 
9094  C CD2 . LEU G 184 ? 0.463 0.525 0.461 0.000  0.061  -0.008 513 LEU GGG CD2 
9095  N N   . SER G 185 ? 0.500 0.568 0.495 -0.016 0.058  -0.024 514 SER GGG N   
9096  C CA  . SER G 185 ? 0.518 0.597 0.512 -0.025 0.055  -0.026 514 SER GGG CA  
9097  C C   . SER G 185 ? 0.485 0.581 0.480 -0.024 0.053  -0.025 514 SER GGG C   
9098  O O   . SER G 185 ? 0.478 0.569 0.466 -0.023 0.052  -0.026 514 SER GGG O   
9099  C CB  . SER G 185 ? 0.525 0.588 0.509 -0.034 0.053  -0.029 514 SER GGG CB  
9100  O OG  . SER G 185 ? 0.586 0.636 0.569 -0.038 0.053  -0.027 514 SER GGG OG  
9101  N N   . PHE G 186 ? 0.481 0.598 0.484 -0.025 0.051  -0.023 515 PHE GGG N   
9102  C CA  . PHE G 186 ? 0.483 0.620 0.491 -0.025 0.046  -0.021 515 PHE GGG CA  
9103  C C   . PHE G 186 ? 0.478 0.628 0.484 -0.039 0.042  -0.023 515 PHE GGG C   
9104  O O   . PHE G 186 ? 0.477 0.638 0.489 -0.045 0.044  -0.023 515 PHE GGG O   
9105  C CB  . PHE G 186 ? 0.469 0.624 0.493 -0.013 0.046  -0.017 515 PHE GGG CB  
9106  C CG  . PHE G 186 ? 0.454 0.593 0.478 -0.002 0.048  -0.015 515 PHE GGG CG  
9107  C CD1 . PHE G 186 ? 0.479 0.598 0.491 -0.002 0.048  -0.013 515 PHE GGG CD1 
9108  C CD2 . PHE G 186 ? 0.453 0.596 0.488 0.009  0.050  -0.015 515 PHE GGG CD2 
9109  C CE1 . PHE G 186 ? 0.475 0.581 0.488 0.006  0.049  -0.009 515 PHE GGG CE1 
9110  C CE2 . PHE G 186 ? 0.451 0.575 0.484 0.018  0.050  -0.013 515 PHE GGG CE2 
9111  C CZ  . PHE G 186 ? 0.469 0.575 0.491 0.015  0.048  -0.009 515 PHE GGG CZ  
9112  N N   . GLU G 187 ? 0.523 0.668 0.516 -0.046 0.037  -0.025 516 GLU GGG N   
9113  C CA  . GLU G 187 ? 0.556 0.704 0.541 -0.063 0.031  -0.028 516 GLU GGG CA  
9114  C C   . GLU G 187 ? 0.539 0.717 0.531 -0.066 0.024  -0.023 516 GLU GGG C   
9115  O O   . GLU G 187 ? 0.504 0.685 0.493 -0.058 0.021  -0.020 516 GLU GGG O   
9116  C CB  . GLU G 187 ? 0.605 0.722 0.568 -0.067 0.031  -0.035 516 GLU GGG CB  
9117  C CG  . GLU G 187 ? 0.690 0.796 0.641 -0.085 0.025  -0.040 516 GLU GGG CG  
9118  C CD  . GLU G 187 ? 0.761 0.835 0.689 -0.088 0.023  -0.050 516 GLU GGG CD  
9119  O OE1 . GLU G 187 ? 0.757 0.829 0.675 -0.082 0.025  -0.054 516 GLU GGG OE1 
9120  O OE2 . GLU G 187 ? 0.861 0.908 0.779 -0.097 0.020  -0.055 516 GLU GGG OE2 
9121  N N   . LEU G 188 ? 0.553 0.754 0.553 -0.078 0.019  -0.021 517 LEU GGG N   
9122  C CA  . LEU G 188 ? 0.567 0.802 0.576 -0.084 0.010  -0.016 517 LEU GGG CA  
9123  C C   . LEU G 188 ? 0.584 0.818 0.580 -0.107 0.002  -0.019 517 LEU GGG C   
9124  O O   . LEU G 188 ? 0.606 0.850 0.608 -0.119 0.003  -0.017 517 LEU GGG O   
9125  C CB  . LEU G 188 ? 0.577 0.850 0.616 -0.076 0.013  -0.010 517 LEU GGG CB  
9126  C CG  . LEU G 188 ? 0.588 0.866 0.641 -0.052 0.015  -0.007 517 LEU GGG CG  
9127  C CD1 . LEU G 188 ? 0.590 0.901 0.672 -0.042 0.019  -0.005 517 LEU GGG CD1 
9128  C CD2 . LEU G 188 ? 0.606 0.891 0.657 -0.049 0.004  -0.001 517 LEU GGG CD2 
9129  N N   . LEU G 189 ? 0.600 0.814 0.572 -0.115 -0.004 -0.023 518 LEU GGG N   
9130  C CA  . LEU G 189 ? 0.623 0.832 0.577 -0.139 -0.014 -0.027 518 LEU GGG CA  
9131  C C   . LEU G 189 ? 0.612 0.858 0.574 -0.146 -0.025 -0.020 518 LEU GGG C   
9132  O O   . LEU G 189 ? 0.608 0.876 0.586 -0.130 -0.026 -0.013 518 LEU GGG O   
9133  C CB  . LEU G 189 ? 0.669 0.831 0.590 -0.142 -0.013 -0.039 518 LEU GGG CB  
9134  C CG  . LEU G 189 ? 0.695 0.822 0.612 -0.129 -0.002 -0.045 518 LEU GGG CG  
9135  C CD1 . LEU G 189 ? 0.717 0.805 0.606 -0.127 -0.001 -0.058 518 LEU GGG CD1 
9136  C CD2 . LEU G 189 ? 0.707 0.828 0.632 -0.139 -0.002 -0.043 518 LEU GGG CD2 
9137  N N   . HIS G 190 ? 0.640 0.891 0.591 -0.169 -0.036 -0.021 519 HIS GGG N   
9138  C CA  . HIS G 190 ? 0.644 0.925 0.594 -0.180 -0.051 -0.015 519 HIS GGG CA  
9139  C C   . HIS G 190 ? 0.680 0.931 0.596 -0.181 -0.054 -0.023 519 HIS GGG C   
9140  O O   . HIS G 190 ? 0.729 0.957 0.616 -0.200 -0.061 -0.032 519 HIS GGG O   
9141  C CB  . HIS G 190 ? 0.636 0.935 0.587 -0.208 -0.061 -0.013 519 HIS GGG CB  
9142  C CG  . HIS G 190 ? 0.654 0.987 0.607 -0.221 -0.077 -0.006 519 HIS GGG CG  
9143  N ND1 . HIS G 190 ? 0.642 1.022 0.625 -0.207 -0.081 0.006  519 HIS GGG ND1 
9144  C CD2 . HIS G 190 ? 0.689 1.016 0.618 -0.247 -0.092 -0.009 519 HIS GGG CD2 
9145  C CE1 . HIS G 190 ? 0.657 1.062 0.635 -0.224 -0.098 0.012  519 HIS GGG CE1 
9146  N NE2 . HIS G 190 ? 0.691 1.065 0.635 -0.250 -0.105 0.002  519 HIS GGG NE2 
9147  N N   . ALA G 191 ? 0.680 0.929 0.598 -0.160 -0.048 -0.021 520 ALA GGG N   
9148  C CA  . ALA G 191 ? 0.707 0.933 0.595 -0.156 -0.047 -0.027 520 ALA GGG CA  
9149  C C   . ALA G 191 ? 0.683 0.932 0.587 -0.139 -0.048 -0.014 520 ALA GGG C   
9150  O O   . ALA G 191 ? 0.676 0.946 0.611 -0.125 -0.045 -0.005 520 ALA GGG O   
9151  C CB  . ALA G 191 ? 0.707 0.889 0.577 -0.149 -0.034 -0.041 520 ALA GGG CB  
9152  N N   . PRO G 192 ? 0.711 0.954 0.591 -0.139 -0.051 -0.013 521 PRO GGG N   
9153  C CA  . PRO G 192 ? 0.690 0.945 0.582 -0.123 -0.051 -0.001 521 PRO GGG CA  
9154  C C   . PRO G 192 ? 0.649 0.885 0.554 -0.103 -0.036 -0.002 521 PRO GGG C   
9155  O O   . PRO G 192 ? 0.668 0.879 0.562 -0.103 -0.024 -0.015 521 PRO GGG O   
9156  C CB  . PRO G 192 ? 0.729 0.974 0.584 -0.131 -0.055 -0.003 521 PRO GGG CB  
9157  C CG  . PRO G 192 ? 0.757 1.000 0.588 -0.154 -0.064 -0.012 521 PRO GGG CG  
9158  C CD  . PRO G 192 ? 0.761 0.988 0.602 -0.157 -0.056 -0.024 521 PRO GGG CD  
9159  N N   . ALA G 193 ? 0.616 0.868 0.549 -0.087 -0.037 0.010  522 ALA GGG N   
9160  C CA  . ALA G 193 ? 0.576 0.812 0.520 -0.070 -0.025 0.010  522 ALA GGG CA  
9161  C C   . ALA G 193 ? 0.584 0.801 0.502 -0.070 -0.021 0.010  522 ALA GGG C   
9162  O O   . ALA G 193 ? 0.659 0.885 0.564 -0.075 -0.030 0.019  522 ALA GGG O   
9163  C CB  . ALA G 193 ? 0.552 0.807 0.527 -0.055 -0.030 0.022  522 ALA GGG CB  
9164  N N   . THR G 194 ? 0.576 0.770 0.487 -0.065 -0.007 0.002  523 THR GGG N   
9165  C CA  . THR G 194 ? 0.592 0.774 0.480 -0.066 -0.000 0.000  523 THR GGG CA  
9166  C C   . THR G 194 ? 0.553 0.726 0.454 -0.053 0.007  0.007  523 THR GGG C   
9167  O O   . THR G 194 ? 0.565 0.734 0.451 -0.054 0.010  0.011  523 THR GGG O   
9168  C CB  . THR G 194 ? 0.622 0.787 0.486 -0.074 0.009  -0.018 523 THR GGG CB  
9169  O OG1 . THR G 194 ? 0.642 0.790 0.519 -0.065 0.020  -0.026 523 THR GGG OG1 
9170  C CG2 . THR G 194 ? 0.626 0.794 0.476 -0.088 0.001  -0.026 523 THR GGG CG2 
9171  N N   . VAL G 195 ? 0.538 0.708 0.464 -0.043 0.008  0.008  524 VAL GGG N   
9172  C CA  . VAL G 195 ? 0.546 0.706 0.484 -0.031 0.013  0.015  524 VAL GGG CA  
9173  C C   . VAL G 195 ? 0.558 0.727 0.517 -0.021 0.003  0.026  524 VAL GGG C   
9174  O O   . VAL G 195 ? 0.557 0.736 0.534 -0.017 0.002  0.022  524 VAL GGG O   
9175  C CB  . VAL G 195 ? 0.548 0.694 0.495 -0.026 0.025  0.004  524 VAL GGG CB  
9176  C CG1 . VAL G 195 ? 0.546 0.681 0.502 -0.017 0.027  0.011  524 VAL GGG CG1 
9177  C CG2 . VAL G 195 ? 0.567 0.703 0.496 -0.032 0.034  -0.008 524 VAL GGG CG2 
9178  N N   . CYS G 196 ? 0.601 0.767 0.556 -0.018 -0.005 0.039  525 CYS GGG N   
9179  C CA  . CYS G 196 ? 0.628 0.798 0.603 -0.007 -0.017 0.051  525 CYS GGG CA  
9180  C C   . CYS G 196 ? 0.647 0.795 0.620 -0.001 -0.016 0.060  525 CYS GGG C   
9181  O O   . CYS G 196 ? 0.638 0.775 0.591 -0.010 -0.011 0.062  525 CYS GGG O   
9182  C CB  . CYS G 196 ? 0.656 0.843 0.626 -0.011 -0.032 0.063  525 CYS GGG CB  
9183  S SG  . CYS G 196 ? 0.694 0.911 0.672 -0.019 -0.036 0.055  525 CYS GGG SG  
9184  N N   . GLY G 197 ? 0.691 0.831 0.683 0.014  -0.022 0.064  526 GLY GGG N   
9185  C CA  . GLY G 197 ? 0.716 0.830 0.706 0.020  -0.027 0.074  526 GLY GGG CA  
9186  C C   . GLY G 197 ? 0.779 0.889 0.754 0.014  -0.042 0.092  526 GLY GGG C   
9187  O O   . GLY G 197 ? 0.792 0.921 0.762 0.008  -0.049 0.097  526 GLY GGG O   
9188  N N   . PRO G 198 ? 0.872 0.956 0.839 0.013  -0.047 0.104  527 PRO GGG N   
9189  C CA  . PRO G 198 ? 0.956 1.032 0.907 0.005  -0.063 0.125  527 PRO GGG CA  
9190  C C   . PRO G 198 ? 1.060 1.147 1.022 0.015  -0.082 0.135  527 PRO GGG C   
9191  O O   . PRO G 198 ? 1.049 1.137 0.994 0.005  -0.095 0.152  527 PRO GGG O   
9192  C CB  . PRO G 198 ? 0.952 0.992 0.901 0.008  -0.068 0.134  527 PRO GGG CB  
9193  C CG  . PRO G 198 ? 0.912 0.948 0.866 0.009  -0.050 0.117  527 PRO GGG CG  
9194  C CD  . PRO G 198 ? 0.863 0.921 0.836 0.019  -0.041 0.099  527 PRO GGG CD  
9204  N N   . GLN H 1   ? 0.930 0.667 0.898 0.148  0.423  0.057  1   GLN HHH N   
9205  C CA  . GLN H 1   ? 0.841 0.672 0.884 0.141  0.367  0.067  1   GLN HHH CA  
9206  C C   . GLN H 1   ? 0.792 0.634 0.758 0.121  0.319  0.036  1   GLN HHH C   
9207  O O   . GLN H 1   ? 0.785 0.623 0.703 0.110  0.296  0.020  1   GLN HHH O   
9208  C CB  . GLN H 1   ? 0.836 0.723 0.962 0.143  0.341  0.092  1   GLN HHH CB  
9209  C CG  . GLN H 1   ? 0.934 0.774 1.045 0.153  0.378  0.095  1   GLN HHH CG  
9210  C CD  . GLN H 1   ? 0.957 0.845 1.151 0.154  0.355  0.123  1   GLN HHH CD  
9211  O OE1 . GLN H 1   ? 0.898 0.833 1.089 0.136  0.297  0.118  1   GLN HHH OE1 
9212  N NE2 . GLN H 1   ? 1.012 0.879 1.277 0.175  0.403  0.154  1   GLN HHH NE2 
9213  N N   . VAL H 2   ? 0.764 0.615 0.724 0.117  0.309  0.029  2   VAL HHH N   
9214  C CA  . VAL H 2   ? 0.730 0.595 0.635 0.101  0.266  0.005  2   VAL HHH CA  
9215  C C   . VAL H 2   ? 0.651 0.583 0.616 0.098  0.228  0.013  2   VAL HHH C   
9216  O O   . VAL H 2   ? 0.636 0.585 0.657 0.104  0.235  0.032  2   VAL HHH O   
9217  C CB  . VAL H 2   ? 0.781 0.591 0.620 0.096  0.283  -0.008 2   VAL HHH CB  
9218  C CG1 . VAL H 2   ? 0.753 0.583 0.558 0.081  0.238  -0.025 2   VAL HHH CG1 
9219  C CG2 . VAL H 2   ? 0.877 0.596 0.632 0.092  0.322  -0.015 2   VAL HHH CG2 
9220  N N   . GLN H 3   ? 0.613 0.575 0.562 0.087  0.190  -0.000 3   GLN HHH N   
9221  C CA  . GLN H 3   ? 0.576 0.578 0.551 0.080  0.157  0.001  3   GLN HHH CA  
9222  C C   . GLN H 3   ? 0.606 0.600 0.538 0.076  0.146  -0.019 3   GLN HHH C   
9223  O O   . GLN H 3   ? 0.628 0.598 0.514 0.073  0.149  -0.033 3   GLN HHH O   
9224  C CB  . GLN H 3   ? 0.531 0.559 0.514 0.070  0.131  0.003  3   GLN HHH CB  
9225  C CG  . GLN H 3   ? 0.512 0.554 0.554 0.071  0.131  0.032  3   GLN HHH CG  
9226  C CD  . GLN H 3   ? 0.497 0.556 0.536 0.055  0.100  0.036  3   GLN HHH CD  
9227  O OE1 . GLN H 3   ? 0.482 0.548 0.504 0.041  0.073  0.032  3   GLN HHH OE1 
9228  N NE2 . GLN H 3   ? 0.493 0.549 0.537 0.056  0.106  0.042  3   GLN HHH NE2 
9229  N N   . LEU H 4   ? 0.619 0.628 0.570 0.074  0.132  -0.016 4   LEU HHH N   
9230  C CA  . LEU H 4   ? 0.613 0.616 0.538 0.072  0.122  -0.030 4   LEU HHH CA  
9231  C C   . LEU H 4   ? 0.598 0.621 0.529 0.065  0.097  -0.033 4   LEU HHH C   
9232  O O   . LEU H 4   ? 0.607 0.640 0.565 0.059  0.086  -0.017 4   LEU HHH O   
9233  C CB  . LEU H 4   ? 0.617 0.602 0.552 0.077  0.139  -0.021 4   LEU HHH CB  
9234  C CG  . LEU H 4   ? 0.649 0.593 0.564 0.082  0.175  -0.017 4   LEU HHH CG  
9235  C CD1 . LEU H 4   ? 0.657 0.586 0.591 0.087  0.197  -0.005 4   LEU HHH CD1 
9236  C CD2 . LEU H 4   ? 0.673 0.580 0.520 0.075  0.172  -0.035 4   LEU HHH CD2 
9237  N N   . VAL H 5   ? 0.584 0.605 0.490 0.065  0.089  -0.049 5   VAL HHH N   
9238  C CA  . VAL H 5   ? 0.595 0.616 0.490 0.059  0.076  -0.056 5   VAL HHH CA  
9239  C C   . VAL H 5   ? 0.615 0.627 0.501 0.065  0.076  -0.066 5   VAL HHH C   
9240  O O   . VAL H 5   ? 0.615 0.630 0.501 0.071  0.080  -0.073 5   VAL HHH O   
9241  C CB  . VAL H 5   ? 0.595 0.618 0.474 0.054  0.076  -0.063 5   VAL HHH CB  
9242  C CG1 . VAL H 5   ? 0.639 0.642 0.488 0.049  0.075  -0.073 5   VAL HHH CG1 
9243  C CG2 . VAL H 5   ? 0.591 0.621 0.478 0.046  0.071  -0.050 5   VAL HHH CG2 
9244  N N   . GLU H 6   ? 0.608 0.609 0.491 0.061  0.068  -0.064 6   GLU HHH N   
9245  C CA  . GLU H 6   ? 0.617 0.605 0.492 0.066  0.067  -0.072 6   GLU HHH CA  
9246  C C   . GLU H 6   ? 0.645 0.617 0.499 0.067  0.074  -0.085 6   GLU HHH C   
9247  O O   . GLU H 6   ? 0.653 0.613 0.484 0.057  0.073  -0.086 6   GLU HHH O   
9248  C CB  . GLU H 6   ? 0.624 0.601 0.499 0.059  0.057  -0.064 6   GLU HHH CB  
9249  C CG  . GLU H 6   ? 0.597 0.585 0.498 0.059  0.060  -0.048 6   GLU HHH CG  
9250  C CD  . GLU H 6   ? 0.590 0.591 0.518 0.050  0.055  -0.029 6   GLU HHH CD  
9251  O OE1 . GLU H 6   ? 0.588 0.591 0.507 0.043  0.047  -0.029 6   GLU HHH OE1 
9252  O OE2 . GLU H 6   ? 0.575 0.584 0.538 0.051  0.062  -0.011 6   GLU HHH OE2 
9253  N N   . SER H 7   ? 0.663 0.630 0.526 0.078  0.082  -0.091 7   SER HHH N   
9254  C CA  . SER H 7   ? 0.707 0.649 0.556 0.084  0.099  -0.101 7   SER HHH CA  
9255  C C   . SER H 7   ? 0.724 0.657 0.592 0.095  0.101  -0.101 7   SER HHH C   
9256  O O   . SER H 7   ? 0.678 0.626 0.565 0.096  0.085  -0.093 7   SER HHH O   
9257  C CB  . SER H 7   ? 0.706 0.663 0.575 0.091  0.117  -0.102 7   SER HHH CB  
9258  O OG  . SER H 7   ? 0.704 0.694 0.619 0.099  0.110  -0.092 7   SER HHH OG  
9259  N N   . GLY H 8   ? 0.779 0.678 0.635 0.103  0.124  -0.109 8   GLY HHH N   
9260  C CA  . GLY H 8   ? 0.794 0.681 0.675 0.117  0.130  -0.107 8   GLY HHH CA  
9261  C C   . GLY H 8   ? 0.853 0.699 0.688 0.109  0.121  -0.113 8   GLY HHH C   
9262  O O   . GLY H 8   ? 0.903 0.736 0.757 0.119  0.123  -0.111 8   GLY HHH O   
9263  N N   . GLY H 9   ? 0.893 0.718 0.675 0.088  0.107  -0.116 9   GLY HHH N   
9264  C CA  . GLY H 9   ? 0.969 0.754 0.707 0.074  0.091  -0.117 9   GLY HHH CA  
9265  C C   . GLY H 9   ? 1.083 0.792 0.758 0.072  0.115  -0.130 9   GLY HHH C   
9266  O O   . GLY H 9   ? 1.124 0.817 0.801 0.086  0.151  -0.138 9   GLY HHH O   
9267  N N   . GLY H 10  ? 1.136 0.795 0.755 0.054  0.099  -0.131 10  GLY HHH N   
9268  C CA  . GLY H 10  ? 1.238 0.800 0.768 0.044  0.121  -0.144 10  GLY HHH CA  
9269  C C   . GLY H 10  ? 1.288 0.811 0.802 0.046  0.118  -0.146 10  GLY HHH C   
9270  O O   . GLY H 10  ? 1.224 0.794 0.782 0.045  0.087  -0.134 10  GLY HHH O   
9271  N N   . LEU H 11  ? 1.402 0.834 0.846 0.048  0.153  -0.161 11  LEU HHH N   
9272  C CA  . LEU H 11  ? 1.455 0.822 0.856 0.046  0.155  -0.165 11  LEU HHH CA  
9273  C C   . LEU H 11  ? 1.411 0.818 0.905 0.086  0.180  -0.163 11  LEU HHH C   
9274  O O   . LEU H 11  ? 1.408 0.839 0.958 0.113  0.218  -0.164 11  LEU HHH O   
9275  C CB  . LEU H 11  ? 1.602 0.837 0.874 0.029  0.189  -0.183 11  LEU HHH CB  
9276  C CG  . LEU H 11  ? 1.707 0.846 0.904 0.022  0.196  -0.190 11  LEU HHH CG  
9277  C CD1 . LEU H 11  ? 1.751 0.860 0.986 0.064  0.260  -0.200 11  LEU HHH CD1 
9278  C CD2 . LEU H 11  ? 1.657 0.835 0.877 0.004  0.137  -0.174 11  LEU HHH CD2 
9279  N N   . VAL H 12  ? 1.401 0.815 0.915 0.088  0.157  -0.157 12  VAL HHH N   
9280  C CA  . VAL H 12  ? 1.372 0.809 0.967 0.121  0.176  -0.151 12  VAL HHH CA  
9281  C C   . VAL H 12  ? 1.382 0.767 0.936 0.113  0.161  -0.152 12  VAL HHH C   
9282  O O   . VAL H 12  ? 1.380 0.756 0.882 0.082  0.120  -0.149 12  VAL HHH O   
9283  C CB  . VAL H 12  ? 1.276 0.820 0.977 0.133  0.150  -0.134 12  VAL HHH CB  
9284  C CG1 . VAL H 12  ? 1.225 0.809 0.927 0.112  0.100  -0.124 12  VAL HHH CG1 
9285  C CG2 . VAL H 12  ? 1.264 0.832 1.057 0.165  0.170  -0.121 12  VAL HHH CG2 
9286  N N   . GLN H 13  ? 1.419 0.768 1.000 0.139  0.193  -0.152 13  GLN HHH N   
9287  C CA  . GLN H 13  ? 1.471 0.770 1.017 0.133  0.178  -0.152 13  GLN HHH CA  
9288  C C   . GLN H 13  ? 1.378 0.762 1.006 0.134  0.132  -0.133 13  GLN HHH C   
9289  O O   . GLN H 13  ? 1.283 0.745 1.004 0.151  0.128  -0.120 13  GLN HHH O   
9290  C CB  . GLN H 13  ? 1.573 0.784 1.103 0.159  0.234  -0.159 13  GLN HHH CB  
9291  C CG  . GLN H 13  ? 1.670 0.806 1.129 0.143  0.217  -0.164 13  GLN HHH CG  
9292  C CD  . GLN H 13  ? 1.859 0.849 1.191 0.136  0.263  -0.184 13  GLN HHH CD  
9293  O OE1 . GLN H 13  ? 1.947 0.881 1.296 0.168  0.324  -0.188 13  GLN HHH OE1 
9294  N NE2 . GLN H 13  ? 1.929 0.850 1.132 0.091  0.233  -0.193 13  GLN HHH NE2 
9295  N N   . ALA H 14  ? 1.377 0.741 0.963 0.113  0.097  -0.131 14  ALA HHH N   
9296  C CA  . ALA H 14  ? 1.290 0.708 0.929 0.110  0.058  -0.115 14  ALA HHH CA  
9297  C C   . ALA H 14  ? 1.251 0.698 0.983 0.142  0.072  -0.103 14  ALA HHH C   
9298  O O   . ALA H 14  ? 1.289 0.686 1.030 0.166  0.112  -0.106 14  ALA HHH O   
9299  C CB  . ALA H 14  ? 1.333 0.696 0.907 0.089  0.035  -0.116 14  ALA HHH CB  
9300  N N   . GLY H 15  ? 1.168 0.686 0.965 0.141  0.040  -0.086 15  GLY HHH N   
9301  C CA  . GLY H 15  ? 1.125 0.678 1.016 0.162  0.039  -0.065 15  GLY HHH CA  
9302  C C   . GLY H 15  ? 1.105 0.699 1.057 0.179  0.062  -0.059 15  GLY HHH C   
9303  O O   . GLY H 15  ? 1.089 0.723 1.127 0.190  0.050  -0.035 15  GLY HHH O   
9304  N N   . GLY H 16  ? 1.125 0.709 1.036 0.177  0.089  -0.077 16  GLY HHH N   
9305  C CA  . GLY H 16  ? 1.100 0.720 1.064 0.192  0.113  -0.072 16  GLY HHH CA  
9306  C C   . GLY H 16  ? 1.036 0.727 1.025 0.177  0.078  -0.062 16  GLY HHH C   
9307  O O   . GLY H 16  ? 0.979 0.684 0.943 0.156  0.041  -0.059 16  GLY HHH O   
9308  N N   . SER H 17  ? 1.031 0.756 1.063 0.186  0.095  -0.057 17  SER HHH N   
9309  C CA  . SER H 17  ? 0.983 0.766 1.035 0.172  0.068  -0.048 17  SER HHH CA  
9310  C C   . SER H 17  ? 0.976 0.765 0.996 0.170  0.091  -0.064 17  SER HHH C   
9311  O O   . SER H 17  ? 1.020 0.774 1.024 0.183  0.132  -0.075 17  SER HHH O   
9312  C CB  . SER H 17  ? 0.970 0.793 1.117 0.181  0.055  -0.018 17  SER HHH CB  
9313  O OG  . SER H 17  ? 1.021 0.842 1.188 0.173  0.018  0.000  17  SER HHH OG  
9314  N N   . LEU H 18  ? 0.936 0.761 0.942 0.153  0.067  -0.063 18  LEU HHH N   
9315  C CA  . LEU H 18  ? 0.911 0.753 0.898 0.148  0.080  -0.072 18  LEU HHH CA  
9316  C C   . LEU H 18  ? 0.866 0.751 0.875 0.136  0.052  -0.059 18  LEU HHH C   
9317  O O   . LEU H 18  ? 0.878 0.764 0.870 0.122  0.025  -0.053 18  LEU HHH O   
9318  C CB  . LEU H 18  ? 0.946 0.762 0.855 0.131  0.078  -0.089 18  LEU HHH CB  
9319  C CG  . LEU H 18  ? 1.023 0.786 0.880 0.133  0.107  -0.106 18  LEU HHH CG  
9320  C CD1 . LEU H 18  ? 1.041 0.791 0.835 0.108  0.090  -0.112 18  LEU HHH CD1 
9321  C CD2 . LEU H 18  ? 1.043 0.804 0.922 0.148  0.144  -0.108 18  LEU HHH CD2 
9322  N N   . ARG H 19  ? 0.838 0.751 0.874 0.139  0.062  -0.055 19  ARG HHH N   
9323  C CA  . ARG H 19  ? 0.792 0.732 0.825 0.124  0.040  -0.047 19  ARG HHH CA  
9324  C C   . ARG H 19  ? 0.773 0.716 0.764 0.119  0.055  -0.063 19  ARG HHH C   
9325  O O   . ARG H 19  ? 0.766 0.717 0.770 0.127  0.077  -0.067 19  ARG HHH O   
9326  C CB  . ARG H 19  ? 0.793 0.762 0.894 0.127  0.030  -0.023 19  ARG HHH CB  
9327  C CG  . ARG H 19  ? 0.801 0.775 0.881 0.103  -0.004 -0.011 19  ARG HHH CG  
9328  C CD  . ARG H 19  ? 0.824 0.823 0.966 0.097  -0.025 0.018  19  ARG HHH CD  
9329  N NE  . ARG H 19  ? 0.827 0.853 1.000 0.110  0.003  0.015  19  ARG HHH NE  
9330  C CZ  . ARG H 19  ? 0.845 0.896 1.059 0.102  -0.009 0.036  19  ARG HHH CZ  
9331  N NH1 . ARG H 19  ? 0.894 0.943 1.116 0.078  -0.055 0.063  19  ARG HHH NH1 
9332  N NH2 . ARG H 19  ? 0.805 0.877 1.044 0.115  0.022  0.030  19  ARG HHH NH2 
9333  N N   . LEU H 20  ? 0.746 0.682 0.693 0.105  0.044  -0.069 20  LEU HHH N   
9334  C CA  . LEU H 20  ? 0.732 0.677 0.652 0.098  0.050  -0.075 20  LEU HHH CA  
9335  C C   . LEU H 20  ? 0.710 0.674 0.643 0.093  0.044  -0.067 20  LEU HHH C   
9336  O O   . LEU H 20  ? 0.715 0.674 0.652 0.085  0.026  -0.055 20  LEU HHH O   
9337  C CB  . LEU H 20  ? 0.758 0.692 0.648 0.087  0.044  -0.076 20  LEU HHH CB  
9338  C CG  . LEU H 20  ? 0.794 0.705 0.665 0.085  0.042  -0.081 20  LEU HHH CG  
9339  C CD1 . LEU H 20  ? 0.794 0.705 0.654 0.073  0.035  -0.073 20  LEU HHH CD1 
9340  C CD2 . LEU H 20  ? 0.824 0.718 0.679 0.088  0.056  -0.091 20  LEU HHH CD2 
9341  N N   . ALA H 21  ? 0.691 0.669 0.622 0.093  0.055  -0.071 21  ALA HHH N   
9342  C CA  . ALA H 21  ? 0.674 0.663 0.603 0.085  0.050  -0.065 21  ALA HHH CA  
9343  C C   . ALA H 21  ? 0.683 0.672 0.586 0.081  0.059  -0.071 21  ALA HHH C   
9344  O O   . ALA H 21  ? 0.730 0.719 0.627 0.082  0.067  -0.077 21  ALA HHH O   
9345  C CB  . ALA H 21  ? 0.649 0.659 0.616 0.090  0.053  -0.058 21  ALA HHH CB  
9346  N N   . CYS H 22  ? 0.678 0.661 0.564 0.072  0.058  -0.066 22  CYS HHH N   
9347  C CA  . CYS H 22  ? 0.692 0.676 0.566 0.071  0.070  -0.067 22  CYS HHH CA  
9348  C C   . CYS H 22  ? 0.679 0.658 0.539 0.064  0.070  -0.063 22  CYS HHH C   
9349  O O   . CYS H 22  ? 0.706 0.658 0.541 0.054  0.062  -0.058 22  CYS HHH O   
9350  C CB  . CYS H 22  ? 0.749 0.714 0.611 0.068  0.079  -0.062 22  CYS HHH CB  
9351  S SG  . CYS H 22  ? 0.782 0.745 0.645 0.069  0.100  -0.055 22  CYS HHH SG  
9352  N N   . ILE H 23  ? 0.647 0.644 0.517 0.066  0.076  -0.066 23  ILE HHH N   
9353  C CA  . ILE H 23  ? 0.647 0.640 0.503 0.059  0.076  -0.062 23  ILE HHH CA  
9354  C C   . ILE H 23  ? 0.647 0.628 0.489 0.059  0.092  -0.061 23  ILE HHH C   
9355  O O   . ILE H 23  ? 0.627 0.624 0.489 0.065  0.098  -0.060 23  ILE HHH O   
9356  C CB  . ILE H 23  ? 0.638 0.662 0.523 0.062  0.072  -0.063 23  ILE HHH CB  
9357  C CG1 . ILE H 23  ? 0.669 0.689 0.544 0.051  0.065  -0.056 23  ILE HHH CG1 
9358  C CG2 . ILE H 23  ? 0.603 0.641 0.495 0.067  0.084  -0.070 23  ILE HHH CG2 
9359  C CD1 . ILE H 23  ? 0.659 0.711 0.572 0.053  0.065  -0.052 23  ILE HHH CD1 
9360  N N   . ALA H 24  ? 0.697 0.644 0.503 0.052  0.098  -0.058 24  ALA HHH N   
9361  C CA  . ALA H 24  ? 0.703 0.627 0.495 0.054  0.122  -0.055 24  ALA HHH CA  
9362  C C   . ALA H 24  ? 0.716 0.644 0.499 0.049  0.119  -0.055 24  ALA HHH C   
9363  O O   . ALA H 24  ? 0.695 0.625 0.466 0.038  0.099  -0.055 24  ALA HHH O   
9364  C CB  . ALA H 24  ? 0.723 0.584 0.463 0.047  0.140  -0.053 24  ALA HHH CB  
9365  N N   . SER H 25  ? 0.649 0.595 0.491 0.012  -0.031 -0.016 25  SER HHH N   
9366  C CA  . SER H 25  ? 0.660 0.585 0.490 -0.002 -0.025 -0.008 25  SER HHH CA  
9367  C C   . SER H 25  ? 0.654 0.588 0.515 -0.005 -0.026 -0.012 25  SER HHH C   
9368  O O   . SER H 25  ? 0.639 0.594 0.525 0.005  -0.033 -0.020 25  SER HHH O   
9369  C CB  . SER H 25  ? 0.684 0.568 0.480 0.000  -0.038 0.006  25  SER HHH CB  
9370  O OG  . SER H 25  ? 0.649 0.529 0.465 0.014  -0.057 0.006  25  SER HHH OG  
9371  N N   . GLY H 26  ? 0.680 0.596 0.535 -0.020 -0.018 -0.008 26  GLY HHH N   
9372  C CA  . GLY H 26  ? 0.689 0.602 0.566 -0.024 -0.021 -0.014 26  GLY HHH CA  
9373  C C   . GLY H 26  ? 0.650 0.600 0.554 -0.037 -0.012 -0.027 26  GLY HHH C   
9374  O O   . GLY H 26  ? 0.614 0.599 0.530 -0.037 -0.005 -0.032 26  GLY HHH O   
9375  N N   . ARG H 27  ? 0.665 0.605 0.579 -0.047 -0.012 -0.033 27  ARG HHH N   
9376  C CA  . ARG H 27  ? 0.702 0.677 0.642 -0.063 -0.006 -0.047 27  ARG HHH CA  
9377  C C   . ARG H 27  ? 0.659 0.650 0.615 -0.054 -0.019 -0.058 27  ARG HHH C   
9378  O O   . ARG H 27  ? 0.703 0.714 0.674 -0.067 -0.020 -0.070 27  ARG HHH O   
9379  C CB  . ARG H 27  ? 0.796 0.746 0.730 -0.089 0.007  -0.047 27  ARG HHH CB  
9380  C CG  . ARG H 27  ? 0.886 0.844 0.815 -0.107 0.026  -0.043 27  ARG HHH CG  
9381  C CD  . ARG H 27  ? 1.054 0.955 0.950 -0.128 0.038  -0.031 27  ARG HHH CD  
9382  N NE  . ARG H 27  ? 1.184 1.082 1.097 -0.151 0.043  -0.044 27  ARG HHH NE  
9383  C CZ  . ARG H 27  ? 1.257 1.158 1.177 -0.184 0.063  -0.049 27  ARG HHH CZ  
9384  N NH1 . ARG H 27  ? 1.306 1.212 1.215 -0.198 0.084  -0.041 27  ARG HHH NH1 
9385  N NH2 . ARG H 27  ? 1.244 1.142 1.181 -0.206 0.064  -0.063 27  ARG HHH NH2 
9386  N N   . THR H 28  ? 0.662 0.643 0.611 -0.034 -0.028 -0.055 28  THR HHH N   
9387  C CA  . THR H 28  ? 0.647 0.635 0.601 -0.026 -0.036 -0.065 28  THR HHH CA  
9388  C C   . THR H 28  ? 0.618 0.623 0.573 -0.007 -0.042 -0.061 28  THR HHH C   
9389  O O   . THR H 28  ? 0.632 0.626 0.582 0.003  -0.045 -0.063 28  THR HHH O   
9390  C CB  . THR H 28  ? 0.672 0.622 0.618 -0.024 -0.035 -0.067 28  THR HHH CB  
9391  O OG1 . THR H 28  ? 0.695 0.620 0.635 -0.012 -0.036 -0.055 28  THR HHH OG1 
9392  C CG2 . THR H 28  ? 0.709 0.637 0.653 -0.044 -0.029 -0.074 28  THR HHH CG2 
9393  N N   . PHE H 29  ? 0.590 0.620 0.550 -0.003 -0.041 -0.058 29  PHE HHH N   
9394  C CA  . PHE H 29  ? 0.571 0.611 0.529 0.014  -0.046 -0.055 29  PHE HHH CA  
9395  C C   . PHE H 29  ? 0.582 0.631 0.539 0.020  -0.054 -0.061 29  PHE HHH C   
9396  O O   . PHE H 29  ? 0.577 0.615 0.525 0.032  -0.056 -0.058 29  PHE HHH O   
9397  C CB  . PHE H 29  ? 0.559 0.626 0.527 0.017  -0.042 -0.055 29  PHE HHH CB  
9398  C CG  . PHE H 29  ? 0.538 0.609 0.503 0.035  -0.045 -0.053 29  PHE HHH CG  
9399  C CD1 . PHE H 29  ? 0.542 0.590 0.491 0.041  -0.043 -0.047 29  PHE HHH CD1 
9400  C CD2 . PHE H 29  ? 0.560 0.655 0.536 0.045  -0.052 -0.057 29  PHE HHH CD2 
9401  C CE1 . PHE H 29  ? 0.536 0.583 0.480 0.055  -0.045 -0.047 29  PHE HHH CE1 
9402  C CE2 . PHE H 29  ? 0.563 0.652 0.532 0.062  -0.054 -0.054 29  PHE HHH CE2 
9403  C CZ  . PHE H 29  ? 0.563 0.627 0.516 0.066  -0.049 -0.050 29  PHE HHH CZ  
9404  N N   . HIS H 30  ? 0.583 0.649 0.547 0.011  -0.059 -0.069 30  HIS HHH N   
9405  C CA  . HIS H 30  ? 0.595 0.666 0.548 0.014  -0.069 -0.075 30  HIS HHH CA  
9406  C C   . HIS H 30  ? 0.614 0.651 0.546 0.014  -0.064 -0.076 30  HIS HHH C   
9407  O O   . HIS H 30  ? 0.657 0.689 0.569 0.019  -0.069 -0.078 30  HIS HHH O   
9408  C CB  . HIS H 30  ? 0.585 0.681 0.549 -0.000 -0.077 -0.086 30  HIS HHH CB  
9409  C CG  . HIS H 30  ? 0.642 0.718 0.605 -0.019 -0.069 -0.093 30  HIS HHH CG  
9410  N ND1 . HIS H 30  ? 0.684 0.734 0.627 -0.026 -0.069 -0.101 30  HIS HHH ND1 
9411  C CD2 . HIS H 30  ? 0.642 0.713 0.618 -0.033 -0.059 -0.093 30  HIS HHH CD2 
9412  C CE1 . HIS H 30  ? 0.692 0.721 0.638 -0.041 -0.060 -0.106 30  HIS HHH CE1 
9413  N NE2 . HIS H 30  ? 0.687 0.725 0.651 -0.046 -0.054 -0.100 30  HIS HHH NE2 
9414  N N   . SER H 31  ? 0.614 0.628 0.549 0.011  -0.055 -0.076 31  SER HHH N   
9415  C CA  . SER H 31  ? 0.626 0.614 0.552 0.013  -0.047 -0.080 31  SER HHH CA  
9416  C C   . SER H 31  ? 0.586 0.568 0.513 0.025  -0.044 -0.072 31  SER HHH C   
9417  O O   . SER H 31  ? 0.567 0.535 0.494 0.027  -0.036 -0.077 31  SER HHH O   
9418  C CB  . SER H 31  ? 0.632 0.597 0.568 0.007  -0.041 -0.082 31  SER HHH CB  
9419  O OG  . SER H 31  ? 0.702 0.665 0.635 -0.009 -0.042 -0.090 31  SER HHH OG  
9420  N N   . TYR H 32  ? 0.577 0.572 0.508 0.032  -0.049 -0.064 32  TYR HHH N   
9421  C CA  . TYR H 32  ? 0.576 0.564 0.510 0.041  -0.046 -0.059 32  TYR HHH CA  
9422  C C   . TYR H 32  ? 0.569 0.558 0.487 0.046  -0.047 -0.056 32  TYR HHH C   
9423  O O   . TYR H 32  ? 0.638 0.639 0.549 0.050  -0.054 -0.054 32  TYR HHH O   
9424  C CB  . TYR H 32  ? 0.545 0.535 0.487 0.043  -0.049 -0.052 32  TYR HHH CB  
9425  C CG  . TYR H 32  ? 0.561 0.538 0.512 0.040  -0.050 -0.051 32  TYR HHH CG  
9426  C CD1 . TYR H 32  ? 0.606 0.574 0.570 0.045  -0.050 -0.052 32  TYR HHH CD1 
9427  C CD2 . TYR H 32  ? 0.591 0.565 0.540 0.032  -0.049 -0.051 32  TYR HHH CD2 
9428  C CE1 . TYR H 32  ? 0.628 0.582 0.601 0.047  -0.054 -0.049 32  TYR HHH CE1 
9429  C CE2 . TYR H 32  ? 0.626 0.579 0.577 0.030  -0.050 -0.048 32  TYR HHH CE2 
9430  C CZ  . TYR H 32  ? 0.632 0.574 0.595 0.040  -0.054 -0.047 32  TYR HHH CZ  
9431  O OH  . TYR H 32  ? 0.638 0.556 0.603 0.042  -0.057 -0.042 32  TYR HHH OH  
9432  N N   . VAL H 33  ? 0.586 0.560 0.498 0.047  -0.039 -0.057 33  VAL HHH N   
9433  C CA  . VAL H 33  ? 0.592 0.556 0.489 0.051  -0.037 -0.052 33  VAL HHH CA  
9434  C C   . VAL H 33  ? 0.592 0.559 0.502 0.056  -0.041 -0.048 33  VAL HHH C   
9435  O O   . VAL H 33  ? 0.562 0.531 0.490 0.053  -0.040 -0.051 33  VAL HHH O   
9436  C CB  . VAL H 33  ? 0.600 0.548 0.490 0.045  -0.023 -0.055 33  VAL HHH CB  
9437  C CG1 . VAL H 33  ? 0.618 0.547 0.489 0.046  -0.018 -0.049 33  VAL HHH CG1 
9438  C CG2 . VAL H 33  ? 0.638 0.579 0.506 0.040  -0.017 -0.061 33  VAL HHH CG2 
9439  N N   . MET H 34  ? 0.593 0.559 0.492 0.064  -0.045 -0.044 34  MET HHH N   
9440  C CA  . MET H 34  ? 0.578 0.542 0.482 0.068  -0.047 -0.043 34  MET HHH CA  
9441  C C   . MET H 34  ? 0.628 0.567 0.517 0.070  -0.042 -0.041 34  MET HHH C   
9442  O O   . MET H 34  ? 0.656 0.580 0.525 0.073  -0.040 -0.037 34  MET HHH O   
9443  C CB  . MET H 34  ? 0.587 0.567 0.493 0.077  -0.052 -0.042 34  MET HHH CB  
9444  C CG  . MET H 34  ? 0.564 0.566 0.483 0.071  -0.054 -0.044 34  MET HHH CG  
9445  S SD  . MET H 34  ? 0.580 0.576 0.507 0.061  -0.052 -0.044 34  MET HHH SD  
9446  C CE  . MET H 34  ? 0.561 0.551 0.479 0.065  -0.052 -0.044 34  MET HHH CE  
9447  N N   . ALA H 35  ? 0.636 0.569 0.532 0.066  -0.041 -0.044 35  ALA HHH N   
9448  C CA  . ALA H 35  ? 0.659 0.565 0.544 0.062  -0.034 -0.045 35  ALA HHH CA  
9449  C C   . ALA H 35  ? 0.664 0.563 0.546 0.063  -0.038 -0.050 35  ALA HHH C   
9450  O O   . ALA H 35  ? 0.626 0.542 0.517 0.063  -0.044 -0.053 35  ALA HHH O   
9451  C CB  . ALA H 35  ? 0.672 0.577 0.570 0.048  -0.026 -0.049 35  ALA HHH CB  
9452  N N   . TRP H 36  ? 0.710 0.579 0.576 0.063  -0.032 -0.051 36  TRP HHH N   
9453  C CA  . TRP H 36  ? 0.700 0.550 0.558 0.060  -0.032 -0.058 36  TRP HHH CA  
9454  C C   . TRP H 36  ? 0.732 0.563 0.593 0.042  -0.026 -0.064 36  TRP HHH C   
9455  O O   . TRP H 36  ? 0.720 0.531 0.572 0.037  -0.016 -0.059 36  TRP HHH O   
9456  C CB  . TRP H 36  ? 0.731 0.557 0.567 0.077  -0.029 -0.057 36  TRP HHH CB  
9457  C CG  . TRP H 36  ? 0.717 0.569 0.559 0.092  -0.032 -0.056 36  TRP HHH CG  
9458  C CD1 . TRP H 36  ? 0.705 0.575 0.554 0.105  -0.035 -0.048 36  TRP HHH CD1 
9459  C CD2 . TRP H 36  ? 0.723 0.588 0.566 0.093  -0.033 -0.064 36  TRP HHH CD2 
9460  N NE1 . TRP H 36  ? 0.695 0.591 0.555 0.113  -0.036 -0.052 36  TRP HHH NE1 
9461  C CE2 . TRP H 36  ? 0.708 0.599 0.561 0.106  -0.032 -0.061 36  TRP HHH CE2 
9462  C CE3 . TRP H 36  ? 0.746 0.602 0.579 0.082  -0.034 -0.073 36  TRP HHH CE3 
9463  C CZ2 . TRP H 36  ? 0.701 0.608 0.555 0.108  -0.028 -0.067 36  TRP HHH CZ2 
9464  C CZ3 . TRP H 36  ? 0.739 0.606 0.564 0.085  -0.032 -0.079 36  TRP HHH CZ3 
9465  C CH2 . TRP H 36  ? 0.717 0.609 0.552 0.097  -0.026 -0.075 36  TRP HHH CH2 
9466  N N   . PHE H 37  ? 0.734 0.573 0.608 0.030  -0.033 -0.074 37  PHE HHH N   
9467  C CA  . PHE H 37  ? 0.751 0.577 0.633 0.010  -0.029 -0.084 37  PHE HHH CA  
9468  C C   . PHE H 37  ? 0.767 0.571 0.630 0.008  -0.034 -0.095 37  PHE HHH C   
9469  O O   . PHE H 37  ? 0.765 0.574 0.613 0.020  -0.041 -0.095 37  PHE HHH O   
9470  C CB  . PHE H 37  ? 0.723 0.586 0.645 -0.003 -0.037 -0.090 37  PHE HHH CB  
9471  C CG  . PHE H 37  ? 0.709 0.589 0.652 -0.005 -0.027 -0.085 37  PHE HHH CG  
9472  C CD1 . PHE H 37  ? 0.687 0.582 0.628 0.010  -0.028 -0.075 37  PHE HHH CD1 
9473  C CD2 . PHE H 37  ? 0.718 0.598 0.682 -0.023 -0.013 -0.091 37  PHE HHH CD2 
9474  C CE1 . PHE H 37  ? 0.701 0.607 0.656 0.007  -0.017 -0.073 37  PHE HHH CE1 
9475  C CE2 . PHE H 37  ? 0.694 0.587 0.673 -0.025 0.001  -0.088 37  PHE HHH CE2 
9476  C CZ  . PHE H 37  ? 0.681 0.586 0.654 -0.009 -0.002 -0.080 37  PHE HHH CZ  
9477  N N   . ARG H 38  ? 0.792 0.571 0.653 -0.011 -0.030 -0.105 38  ARG HHH N   
9478  C CA  . ARG H 38  ? 0.834 0.591 0.675 -0.017 -0.036 -0.119 38  ARG HHH CA  
9479  C C   . ARG H 38  ? 0.844 0.608 0.708 -0.045 -0.042 -0.135 38  ARG HHH C   
9480  O O   . ARG H 38  ? 0.840 0.615 0.733 -0.060 -0.034 -0.134 38  ARG HHH O   
9481  C CB  . ARG H 38  ? 0.872 0.574 0.676 -0.007 -0.021 -0.119 38  ARG HHH CB  
9482  C CG  . ARG H 38  ? 0.898 0.558 0.696 -0.022 -0.006 -0.118 38  ARG HHH CG  
9483  C CD  . ARG H 38  ? 0.929 0.533 0.689 -0.003 0.007  -0.111 38  ARG HHH CD  
9484  N NE  . ARG H 38  ? 0.983 0.539 0.729 -0.018 0.023  -0.106 38  ARG HHH NE  
9485  C CZ  . ARG H 38  ? 1.043 0.536 0.753 -0.005 0.034  -0.098 38  ARG HHH CZ  
9486  N NH1 . ARG H 38  ? 1.069 0.547 0.761 0.025  0.030  -0.097 38  ARG HHH NH1 
9487  N NH2 . ARG H 38  ? 1.103 0.548 0.794 -0.021 0.049  -0.091 38  ARG HHH NH2 
9488  N N   . GLN H 39  ? 0.875 0.634 0.726 -0.054 -0.056 -0.150 39  GLN HHH N   
9489  C CA  . GLN H 39  ? 0.896 0.668 0.772 -0.082 -0.068 -0.167 39  GLN HHH CA  
9490  C C   . GLN H 39  ? 0.938 0.671 0.775 -0.092 -0.072 -0.185 39  GLN HHH C   
9491  O O   . GLN H 39  ? 0.929 0.660 0.735 -0.080 -0.084 -0.188 39  GLN HHH O   
9492  C CB  . GLN H 39  ? 0.858 0.688 0.769 -0.081 -0.094 -0.167 39  GLN HHH CB  
9493  C CG  . GLN H 39  ? 0.864 0.719 0.810 -0.107 -0.111 -0.186 39  GLN HHH CG  
9494  C CD  . GLN H 39  ? 0.835 0.749 0.827 -0.102 -0.136 -0.183 39  GLN HHH CD  
9495  O OE1 . GLN H 39  ? 0.824 0.749 0.801 -0.081 -0.149 -0.171 39  GLN HHH OE1 
9496  N NE2 . GLN H 39  ? 0.851 0.800 0.899 -0.122 -0.144 -0.196 39  GLN HHH NE2 
9497  N N   . ALA H 40  ? 0.996 0.692 0.830 -0.114 -0.061 -0.197 40  ALA HHH N   
9498  C CA  . ALA H 40  ? 1.082 0.739 0.885 -0.131 -0.065 -0.220 40  ALA HHH CA  
9499  C C   . ALA H 40  ? 1.106 0.808 0.942 -0.157 -0.093 -0.238 40  ALA HHH C   
9500  O O   . ALA H 40  ? 1.047 0.799 0.937 -0.165 -0.100 -0.234 40  ALA HHH O   
9501  C CB  . ALA H 40  ? 1.138 0.733 0.925 -0.145 -0.040 -0.224 40  ALA HHH CB  
9502  N N   . PRO H 41  ? 1.183 0.870 0.989 -0.171 -0.111 -0.259 41  PRO HHH N   
9503  C CA  . PRO H 41  ? 1.209 0.943 1.045 -0.192 -0.145 -0.275 41  PRO HHH CA  
9504  C C   . PRO H 41  ? 1.209 0.977 1.113 -0.223 -0.147 -0.286 41  PRO HHH C   
9505  O O   . PRO H 41  ? 1.189 1.018 1.136 -0.224 -0.174 -0.287 41  PRO HHH O   
9506  C CB  . PRO H 41  ? 1.279 0.975 1.057 -0.204 -0.159 -0.298 41  PRO HHH CB  
9507  C CG  . PRO H 41  ? 1.297 0.937 1.015 -0.178 -0.133 -0.290 41  PRO HHH CG  
9508  C CD  . PRO H 41  ? 1.262 0.887 1.003 -0.165 -0.101 -0.270 41  PRO HHH CD  
9509  N N   . GLY H 42  ? 1.250 0.983 1.164 -0.247 -0.120 -0.294 42  GLY HHH N   
9510  C CA  . GLY H 42  ? 1.280 1.053 1.265 -0.280 -0.118 -0.305 42  GLY HHH CA  
9511  C C   . GLY H 42  ? 1.276 1.086 1.311 -0.269 -0.098 -0.285 42  GLY HHH C   
9512  O O   . GLY H 42  ? 1.321 1.166 1.416 -0.295 -0.090 -0.294 42  GLY HHH O   
9513  N N   . LYS H 43  ? 1.277 1.077 1.284 -0.234 -0.087 -0.260 43  LYS HHH N   
9514  C CA  . LYS H 43  ? 1.274 1.072 1.297 -0.225 -0.056 -0.239 43  LYS HHH CA  
9515  C C   . LYS H 43  ? 1.199 1.059 1.257 -0.199 -0.070 -0.225 43  LYS HHH C   
9516  O O   . LYS H 43  ? 1.152 1.037 1.204 -0.182 -0.099 -0.225 43  LYS HHH O   
9517  C CB  . LYS H 43  ? 1.366 1.092 1.324 -0.205 -0.031 -0.222 43  LYS HHH CB  
9518  C CG  . LYS H 43  ? 1.489 1.145 1.418 -0.231 -0.007 -0.231 43  LYS HHH CG  
9519  C CD  . LYS H 43  ? 1.563 1.138 1.425 -0.210 0.013  -0.217 43  LYS HHH CD  
9520  C CE  . LYS H 43  ? 1.619 1.126 1.439 -0.225 0.016  -0.235 43  LYS HHH CE  
9521  N NZ  . LYS H 43  ? 1.660 1.086 1.446 -0.235 0.047  -0.228 43  LYS HHH NZ  
9522  N N   . GLU H 44  ? 1.157 1.034 1.246 -0.197 -0.047 -0.214 44  GLU HHH N   
9523  C CA  . GLU H 44  ? 1.051 0.974 1.166 -0.171 -0.053 -0.200 44  GLU HHH CA  
9524  C C   . GLU H 44  ? 0.974 0.858 1.031 -0.141 -0.045 -0.178 44  GLU HHH C   
9525  O O   . GLU H 44  ? 0.996 0.823 1.002 -0.141 -0.031 -0.174 44  GLU HHH O   
9526  C CB  . GLU H 44  ? 1.073 1.033 1.247 -0.184 -0.031 -0.201 44  GLU HHH CB  
9527  C CG  . GLU H 44  ? 1.125 1.135 1.370 -0.214 -0.041 -0.226 44  GLU HHH CG  
9528  C CD  . GLU H 44  ? 1.154 1.189 1.454 -0.238 -0.008 -0.233 44  GLU HHH CD  
9529  O OE1 . GLU H 44  ? 1.139 1.182 1.444 -0.222 0.012  -0.220 44  GLU HHH OE1 
9530  O OE2 . GLU H 44  ? 1.164 1.209 1.501 -0.274 -0.001 -0.253 44  GLU HHH OE2 
9531  N N   . ARG H 45  ? 0.869 0.785 0.936 -0.117 -0.054 -0.165 45  ARG HHH N   
9532  C CA  . ARG H 45  ? 0.868 0.759 0.891 -0.090 -0.046 -0.146 45  ARG HHH CA  
9533  C C   . ARG H 45  ? 0.882 0.739 0.888 -0.094 -0.014 -0.136 45  ARG HHH C   
9534  O O   . ARG H 45  ? 0.908 0.787 0.949 -0.106 0.001  -0.138 45  ARG HHH O   
9535  C CB  . ARG H 45  ? 0.821 0.754 0.867 -0.069 -0.059 -0.137 45  ARG HHH CB  
9536  C CG  . ARG H 45  ? 0.827 0.762 0.847 -0.054 -0.084 -0.134 45  ARG HHH CG  
9537  C CD  . ARG H 45  ? 0.830 0.803 0.875 -0.039 -0.102 -0.128 45  ARG HHH CD  
9538  N NE  . ARG H 45  ? 0.886 0.865 0.916 -0.036 -0.131 -0.131 45  ARG HHH NE  
9539  C CZ  . ARG H 45  ? 0.892 0.881 0.912 -0.020 -0.149 -0.121 45  ARG HHH CZ  
9540  N NH1 . ARG H 45  ? 0.924 0.922 0.953 -0.005 -0.141 -0.109 45  ARG HHH NH1 
9541  N NH2 . ARG H 45  ? 0.909 0.898 0.907 -0.020 -0.175 -0.124 45  ARG HHH NH2 
9542  N N   . GLU H 46  ? 0.885 0.691 0.839 -0.084 -0.005 -0.127 46  GLU HHH N   
9543  C CA  . GLU H 46  ? 0.907 0.668 0.829 -0.084 0.020  -0.115 46  GLU HHH CA  
9544  C C   . GLU H 46  ? 0.874 0.636 0.771 -0.055 0.017  -0.097 46  GLU HHH C   
9545  O O   . GLU H 46  ? 0.846 0.612 0.729 -0.035 0.001  -0.095 46  GLU HHH O   
9546  C CB  . GLU H 46  ? 0.969 0.669 0.854 -0.095 0.028  -0.119 46  GLU HHH CB  
9547  C CG  . GLU H 46  ? 1.042 0.682 0.883 -0.092 0.050  -0.104 46  GLU HHH CG  
9548  C CD  . GLU H 46  ? 1.137 0.707 0.934 -0.093 0.056  -0.106 46  GLU HHH CD  
9549  O OE1 . GLU H 46  ? 1.172 0.740 0.977 -0.105 0.047  -0.124 46  GLU HHH OE1 
9550  O OE2 . GLU H 46  ? 1.227 0.742 0.981 -0.083 0.069  -0.090 46  GLU HHH OE2 
9551  N N   . PHE H 47  ? 0.862 0.624 0.755 -0.053 0.031  -0.087 47  PHE HHH N   
9552  C CA  . PHE H 47  ? 0.825 0.585 0.692 -0.028 0.028  -0.071 47  PHE HHH CA  
9553  C C   . PHE H 47  ? 0.844 0.554 0.664 -0.012 0.028  -0.062 47  PHE HHH C   
9554  O O   . PHE H 47  ? 0.873 0.533 0.666 -0.023 0.041  -0.059 47  PHE HHH O   
9555  C CB  . PHE H 47  ? 0.832 0.594 0.696 -0.034 0.045  -0.065 47  PHE HHH CB  
9556  C CG  . PHE H 47  ? 0.841 0.597 0.674 -0.012 0.040  -0.050 47  PHE HHH CG  
9557  C CD1 . PHE H 47  ? 0.790 0.588 0.643 0.001  0.026  -0.051 47  PHE HHH CD1 
9558  C CD2 . PHE H 47  ? 0.861 0.569 0.643 -0.006 0.047  -0.036 47  PHE HHH CD2 
9559  C CE1 . PHE H 47  ? 0.781 0.577 0.609 0.018  0.020  -0.040 47  PHE HHH CE1 
9560  C CE2 . PHE H 47  ? 0.856 0.563 0.611 0.014  0.037  -0.024 47  PHE HHH CE2 
9561  C CZ  . PHE H 47  ? 0.818 0.572 0.599 0.024  0.024  -0.028 47  PHE HHH CZ  
9562  N N   . VAL H 48  ? 0.829 0.551 0.641 0.012  0.013  -0.056 48  VAL HHH N   
9563  C CA  . VAL H 48  ? 0.870 0.555 0.647 0.034  0.011  -0.047 48  VAL HHH CA  
9564  C C   . VAL H 48  ? 0.843 0.531 0.603 0.053  0.007  -0.032 48  VAL HHH C   
9565  O O   . VAL H 48  ? 0.876 0.519 0.600 0.061  0.011  -0.020 48  VAL HHH O   
9566  C CB  . VAL H 48  ? 0.874 0.571 0.658 0.048  -0.000 -0.057 48  VAL HHH CB  
9567  C CG1 . VAL H 48  ? 0.912 0.579 0.672 0.074  -0.001 -0.050 48  VAL HHH CG1 
9568  C CG2 . VAL H 48  ? 0.908 0.595 0.699 0.028  0.001  -0.073 48  VAL HHH CG2 
9569  N N   . ALA H 49  ? 0.789 0.526 0.572 0.059  -0.003 -0.033 49  ALA HHH N   
9570  C CA  . ALA H 49  ? 0.804 0.552 0.575 0.076  -0.011 -0.022 49  ALA HHH CA  
9571  C C   . ALA H 49  ? 0.753 0.551 0.551 0.071  -0.016 -0.026 49  ALA HHH C   
9572  O O   . ALA H 49  ? 0.751 0.576 0.579 0.064  -0.018 -0.035 49  ALA HHH O   
9573  C CB  . ALA H 49  ? 0.809 0.553 0.572 0.102  -0.022 -0.017 49  ALA HHH CB  
9574  N N   . ALA H 50  ? 0.728 0.531 0.512 0.076  -0.019 -0.019 50  ALA HHH N   
9575  C CA  . ALA H 50  ? 0.680 0.522 0.485 0.072  -0.024 -0.023 50  ALA HHH CA  
9576  C C   . ALA H 50  ? 0.688 0.537 0.474 0.085  -0.036 -0.016 50  ALA HHH C   
9577  O O   . ALA H 50  ? 0.749 0.565 0.498 0.093  -0.038 -0.006 50  ALA HHH O   
9578  C CB  . ALA H 50  ? 0.666 0.511 0.479 0.054  -0.010 -0.029 50  ALA HHH CB  
9579  N N   . ILE H 51  ? 0.633 0.519 0.442 0.086  -0.044 -0.022 51  ILE HHH N   
9580  C CA  . ILE H 51  ? 0.650 0.552 0.449 0.095  -0.059 -0.019 51  ILE HHH CA  
9581  C C   . ILE H 51  ? 0.631 0.555 0.442 0.082  -0.057 -0.027 51  ILE HHH C   
9582  O O   . ILE H 51  ? 0.581 0.524 0.422 0.075  -0.053 -0.034 51  ILE HHH O   
9583  C CB  . ILE H 51  ? 0.633 0.560 0.454 0.112  -0.071 -0.019 51  ILE HHH CB  
9584  C CG1 . ILE H 51  ? 0.665 0.613 0.483 0.122  -0.090 -0.017 51  ILE HHH CG1 
9585  C CG2 . ILE H 51  ? 0.578 0.533 0.435 0.106  -0.066 -0.028 51  ILE HHH CG2 
9586  C CD1 . ILE H 51  ? 0.659 0.631 0.502 0.143  -0.101 -0.017 51  ILE HHH CD1 
9587  N N   . SER H 52  ? 0.679 0.594 0.460 0.078  -0.060 -0.026 52  SER HHH N   
9588  C CA  . SER H 52  ? 0.677 0.604 0.460 0.065  -0.057 -0.036 52  SER HHH CA  
9589  C C   . SER H 52  ? 0.663 0.627 0.473 0.067  -0.072 -0.042 52  SER HHH C   
9590  O O   . SER H 52  ? 0.681 0.663 0.507 0.080  -0.084 -0.038 52  SER HHH O   
9591  C CB  . SER H 52  ? 0.717 0.620 0.453 0.059  -0.055 -0.035 52  SER HHH CB  
9592  O OG  . SER H 52  ? 0.741 0.646 0.480 0.045  -0.043 -0.048 52  SER HHH OG  
9593  N N   . TRP H 53  ? 0.686 0.659 0.502 0.055  -0.070 -0.052 53  TRP HHH N   
9594  C CA  . TRP H 53  ? 0.655 0.659 0.497 0.050  -0.080 -0.060 53  TRP HHH CA  
9595  C C   . TRP H 53  ? 0.628 0.655 0.468 0.058  -0.101 -0.058 53  TRP HHH C   
9596  O O   . TRP H 53  ? 0.630 0.687 0.503 0.063  -0.107 -0.059 53  TRP HHH O   
9597  C CB  . TRP H 53  ? 0.651 0.647 0.486 0.034  -0.073 -0.072 53  TRP HHH CB  
9598  C CG  . TRP H 53  ? 0.638 0.611 0.476 0.030  -0.053 -0.075 53  TRP HHH CG  
9599  C CD1 . TRP H 53  ? 0.615 0.590 0.484 0.030  -0.045 -0.075 53  TRP HHH CD1 
9600  C CD2 . TRP H 53  ? 0.640 0.588 0.451 0.025  -0.038 -0.079 53  TRP HHH CD2 
9601  N NE1 . TRP H 53  ? 0.585 0.543 0.456 0.028  -0.029 -0.079 53  TRP HHH NE1 
9602  C CE2 . TRP H 53  ? 0.630 0.572 0.468 0.024  -0.022 -0.083 53  TRP HHH CE2 
9603  C CE3 . TRP H 53  ? 0.671 0.600 0.435 0.022  -0.037 -0.080 53  TRP HHH CE3 
9604  C CZ2 . TRP H 53  ? 0.632 0.557 0.462 0.020  -0.002 -0.090 53  TRP HHH CZ2 
9605  C CZ3 . TRP H 53  ? 0.701 0.606 0.447 0.015  -0.014 -0.086 53  TRP HHH CZ3 
9606  C CH2 . TRP H 53  ? 0.683 0.589 0.466 0.014  0.005  -0.092 53  TRP HHH CH2 
9607  N N   . SER H 54  ? 0.665 0.680 0.467 0.061  -0.113 -0.056 54  SER HHH N   
9608  C CA  . SER H 54  ? 0.708 0.745 0.504 0.071  -0.140 -0.054 54  SER HHH CA  
9609  C C   . SER H 54  ? 0.722 0.762 0.526 0.095  -0.149 -0.041 54  SER HHH C   
9610  O O   . SER H 54  ? 0.739 0.801 0.546 0.108  -0.173 -0.039 54  SER HHH O   
9611  C CB  . SER H 54  ? 0.755 0.767 0.494 0.066  -0.149 -0.054 54  SER HHH CB  
9612  O OG  . SER H 54  ? 0.791 0.759 0.488 0.074  -0.139 -0.041 54  SER HHH OG  
9613  N N   . SER H 55  ? 0.723 0.738 0.528 0.100  -0.131 -0.034 55  SER HHH N   
9614  C CA  . SER H 55  ? 0.745 0.743 0.544 0.122  -0.134 -0.022 55  SER HHH CA  
9615  C C   . SER H 55  ? 0.800 0.749 0.539 0.128  -0.137 -0.009 55  SER HHH C   
9616  O O   . SER H 55  ? 0.799 0.723 0.527 0.145  -0.139 0.002  55  SER HHH O   
9617  C CB  . SER H 55  ? 0.729 0.767 0.562 0.142  -0.154 -0.022 55  SER HHH CB  
9618  O OG  . SER H 55  ? 0.692 0.772 0.578 0.135  -0.146 -0.033 55  SER HHH OG  
9619  N N   . THR H 56  ? 0.875 0.804 0.572 0.113  -0.136 -0.010 56  THR HHH N   
9620  C CA  . THR H 56  ? 1.031 0.924 0.665 0.122  -0.151 0.003  56  THR HHH CA  
9621  C C   . THR H 56  ? 1.088 0.920 0.672 0.115  -0.128 0.014  56  THR HHH C   
9622  O O   . THR H 56  ? 1.200 0.992 0.733 0.128  -0.139 0.030  56  THR HHH O   
9623  C CB  . THR H 56  ? 1.133 1.033 0.734 0.110  -0.166 -0.004 56  THR HHH CB  
9624  O OG1 . THR H 56  ? 1.142 1.087 0.773 0.126  -0.199 -0.006 56  THR HHH OG1 
9625  C CG2 . THR H 56  ? 1.207 1.050 0.723 0.108  -0.167 0.008  56  THR HHH CG2 
9626  N N   . PRO H 57  ? 0.997 0.818 0.589 0.095  -0.097 0.006  57  PRO HHH N   
9627  C CA  . PRO H 57  ? 0.961 0.738 0.533 0.090  -0.074 0.014  57  PRO HHH CA  
9628  C C   . PRO H 57  ? 0.875 0.672 0.503 0.099  -0.071 0.012  57  PRO HHH C   
9629  O O   . PRO H 57  ? 0.792 0.628 0.469 0.093  -0.068 -0.001 57  PRO HHH O   
9630  C CB  . PRO H 57  ? 0.941 0.707 0.501 0.065  -0.046 0.004  57  PRO HHH CB  
9631  C CG  . PRO H 57  ? 0.948 0.751 0.525 0.059  -0.054 -0.012 57  PRO HHH CG  
9632  C CD  . PRO H 57  ? 0.923 0.767 0.534 0.075  -0.085 -0.012 57  PRO HHH CD  
9633  N N   . THR H 58  ? 0.906 0.672 0.520 0.114  -0.075 0.024  58  THR HHH N   
9634  C CA  . THR H 58  ? 0.869 0.633 0.517 0.117  -0.065 0.021  58  THR HHH CA  
9635  C C   . THR H 58  ? 0.901 0.613 0.517 0.102  -0.041 0.027  58  THR HHH C   
9636  O O   . THR H 58  ? 0.944 0.614 0.506 0.097  -0.037 0.038  58  THR HHH O   
9637  C CB  . THR H 58  ? 0.869 0.636 0.530 0.144  -0.083 0.027  58  THR HHH CB  
9638  O OG1 . THR H 58  ? 0.930 0.651 0.541 0.161  -0.094 0.044  58  THR HHH OG1 
9639  C CG2 . THR H 58  ? 0.823 0.651 0.529 0.155  -0.101 0.018  58  THR HHH CG2 
9640  N N   . TYR H 59  ? 0.879 0.593 0.528 0.092  -0.026 0.018  59  TYR HHH N   
9641  C CA  . TYR H 59  ? 0.918 0.591 0.550 0.072  -0.002 0.019  59  TYR HHH CA  
9642  C C   . TYR H 59  ? 0.920 0.580 0.572 0.077  -0.001 0.016  59  TYR HHH C   
9643  O O   . TYR H 59  ? 0.906 0.605 0.599 0.087  -0.012 0.007  59  TYR HHH O   
9644  C CB  . TYR H 59  ? 0.887 0.587 0.549 0.047  0.017  0.005  59  TYR HHH CB  
9645  C CG  . TYR H 59  ? 0.888 0.604 0.538 0.040  0.021  0.002  59  TYR HHH CG  
9646  C CD1 . TYR H 59  ? 0.934 0.614 0.538 0.024  0.041  0.006  59  TYR HHH CD1 
9647  C CD2 . TYR H 59  ? 0.842 0.606 0.526 0.045  0.008  -0.007 59  TYR HHH CD2 
9648  C CE1 . TYR H 59  ? 0.953 0.645 0.542 0.017  0.047  0.001  59  TYR HHH CE1 
9649  C CE2 . TYR H 59  ? 0.841 0.616 0.514 0.037  0.014  -0.013 59  TYR HHH CE2 
9650  C CZ  . TYR H 59  ? 0.905 0.645 0.531 0.023  0.033  -0.010 59  TYR HHH CZ  
9651  O OH  . TYR H 59  ? 0.904 0.652 0.516 0.015  0.040  -0.019 59  TYR HHH OH  
9652  N N   . TYR H 60  ? 0.967 0.572 0.589 0.068  0.013  0.022  60  TYR HHH N   
9653  C CA  . TYR H 60  ? 0.991 0.569 0.620 0.071  0.016  0.018  60  TYR HHH CA  
9654  C C   . TYR H 60  ? 1.033 0.577 0.656 0.040  0.041  0.013  60  TYR HHH C   
9655  O O   . TYR H 60  ? 1.089 0.600 0.676 0.024  0.057  0.022  60  TYR HHH O   
9656  C CB  . TYR H 60  ? 1.050 0.581 0.640 0.099  0.003  0.034  60  TYR HHH CB  
9657  C CG  . TYR H 60  ? 1.019 0.594 0.630 0.129  -0.022 0.035  60  TYR HHH CG  
9658  C CD1 . TYR H 60  ? 0.947 0.562 0.604 0.140  -0.028 0.021  60  TYR HHH CD1 
9659  C CD2 . TYR H 60  ? 1.025 0.604 0.611 0.144  -0.038 0.048  60  TYR HHH CD2 
9660  C CE1 . TYR H 60  ? 0.923 0.582 0.604 0.163  -0.047 0.020  60  TYR HHH CE1 
9661  C CE2 . TYR H 60  ? 0.990 0.616 0.603 0.168  -0.061 0.046  60  TYR HHH CE2 
9662  C CZ  . TYR H 60  ? 0.938 0.605 0.602 0.177  -0.064 0.032  60  TYR HHH CZ  
9663  O OH  . TYR H 60  ? 0.955 0.673 0.651 0.198  -0.082 0.029  60  TYR HHH OH  
9664  N N   . GLY H 61  ? 1.042 0.595 0.698 0.029  0.045  -0.002 61  GLY HHH N   
9665  C CA  . GLY H 61  ? 1.079 0.596 0.732 -0.000 0.066  -0.008 61  GLY HHH CA  
9666  C C   . GLY H 61  ? 1.163 0.597 0.759 0.004  0.074  0.006  61  GLY HHH C   
9667  O O   . GLY H 61  ? 1.154 0.565 0.727 0.035  0.058  0.017  61  GLY HHH O   
9668  N N   . GLU H 62  ? 1.253 0.643 0.828 -0.026 0.099  0.007  62  GLU HHH N   
9669  C CA  . GLU H 62  ? 1.365 0.663 0.874 -0.027 0.111  0.025  62  GLU HHH CA  
9670  C C   . GLU H 62  ? 1.368 0.627 0.870 -0.006 0.099  0.023  62  GLU HHH C   
9671  O O   . GLU H 62  ? 1.439 0.640 0.892 0.021  0.091  0.042  62  GLU HHH O   
9672  C CB  . GLU H 62  ? 1.435 0.700 0.935 -0.071 0.145  0.021  62  GLU HHH CB  
9673  C CG  . GLU H 62  ? 1.610 0.774 1.031 -0.076 0.162  0.043  62  GLU HHH CG  
9674  C CD  . GLU H 62  ? 1.704 0.836 1.062 -0.046 0.148  0.071  62  GLU HHH CD  
9675  O OE1 . GLU H 62  ? 1.674 0.864 1.045 -0.036 0.137  0.071  62  GLU HHH OE1 
9676  O OE2 . GLU H 62  ? 1.798 0.845 1.093 -0.032 0.146  0.091  62  GLU HHH OE2 
9677  N N   . SER H 63  ? 1.287 0.577 0.834 -0.015 0.096  0.000  63  SER HHH N   
9678  C CA  . SER H 63  ? 1.308 0.548 0.843 -0.004 0.093  -0.007 63  SER HHH CA  
9679  C C   . SER H 63  ? 1.260 0.523 0.802 0.041  0.070  -0.004 63  SER HHH C   
9680  O O   . SER H 63  ? 1.324 0.541 0.850 0.058  0.068  -0.008 63  SER HHH O   
9681  C CB  . SER H 63  ? 1.287 0.545 0.859 -0.035 0.100  -0.033 63  SER HHH CB  
9682  O OG  . SER H 63  ? 1.233 0.578 0.858 -0.033 0.084  -0.048 63  SER HHH OG  
9683  N N   . VAL H 64  ? 1.187 0.516 0.753 0.058  0.054  0.000  64  VAL HHH N   
9684  C CA  . VAL H 64  ? 1.172 0.530 0.751 0.098  0.034  0.001  64  VAL HHH CA  
9685  C C   . VAL H 64  ? 1.196 0.546 0.748 0.126  0.021  0.024  64  VAL HHH C   
9686  O O   . VAL H 64  ? 1.151 0.519 0.715 0.161  0.004  0.026  64  VAL HHH O   
9687  C CB  . VAL H 64  ? 1.091 0.534 0.722 0.097  0.024  -0.015 64  VAL HHH CB  
9688  C CG1 . VAL H 64  ? 1.078 0.529 0.731 0.071  0.032  -0.037 64  VAL HHH CG1 
9689  C CG2 . VAL H 64  ? 1.046 0.544 0.694 0.087  0.020  -0.009 64  VAL HHH CG2 
9690  N N   . LYS H 65  ? 1.273 0.599 0.791 0.111  0.028  0.039  65  LYS HHH N   
9691  C CA  . LYS H 65  ? 1.345 0.658 0.826 0.134  0.013  0.062  65  LYS HHH CA  
9692  C C   . LYS H 65  ? 1.393 0.655 0.849 0.173  -0.002 0.075  65  LYS HHH C   
9693  O O   . LYS H 65  ? 1.462 0.652 0.891 0.171  0.011  0.076  65  LYS HHH O   
9694  C CB  . LYS H 65  ? 1.430 0.697 0.859 0.107  0.030  0.077  65  LYS HHH CB  
9695  C CG  . LYS H 65  ? 1.461 0.764 0.877 0.108  0.020  0.086  65  LYS HHH CG  
9696  C CD  . LYS H 65  ? 1.513 0.792 0.898 0.069  0.049  0.089  65  LYS HHH CD  
9697  C CE  . LYS H 65  ? 1.527 0.828 0.885 0.068  0.043  0.097  65  LYS HHH CE  
9698  N NZ  . LYS H 65  ? 1.654 0.876 0.928 0.054  0.059  0.118  65  LYS HHH NZ  
9699  N N   . GLY H 66  ? 1.373 0.674 0.844 0.209  -0.028 0.081  66  GLY HHH N   
9700  C CA  . GLY H 66  ? 1.437 0.702 0.896 0.253  -0.047 0.092  66  GLY HHH CA  
9701  C C   . GLY H 66  ? 1.416 0.717 0.930 0.275  -0.048 0.071  66  GLY HHH C   
9702  O O   . GLY H 66  ? 1.451 0.765 0.981 0.316  -0.068 0.076  66  GLY HHH O   
9703  N N   . ARG H 67  ? 1.374 0.693 0.916 0.249  -0.029 0.049  67  ARG HHH N   
9704  C CA  . ARG H 67  ? 1.346 0.686 0.928 0.265  -0.025 0.028  67  ARG HHH CA  
9705  C C   . ARG H 67  ? 1.253 0.690 0.890 0.262  -0.030 0.012  67  ARG HHH C   
9706  O O   . ARG H 67  ? 1.265 0.734 0.937 0.286  -0.032 -0.000 67  ARG HHH O   
9707  C CB  . ARG H 67  ? 1.375 0.666 0.943 0.238  -0.001 0.012  67  ARG HHH CB  
9708  C CG  . ARG H 67  ? 1.489 0.675 1.001 0.237  0.008  0.026  67  ARG HHH CG  
9709  C CD  . ARG H 67  ? 1.527 0.666 1.031 0.212  0.030  0.006  67  ARG HHH CD  
9710  N NE  . ARG H 67  ? 1.479 0.653 0.997 0.165  0.040  -0.007 67  ARG HHH NE  
9711  C CZ  . ARG H 67  ? 1.403 0.624 0.955 0.146  0.044  -0.032 67  ARG HHH CZ  
9712  N NH1 . ARG H 67  ? 1.393 0.626 0.962 0.168  0.042  -0.048 67  ARG HHH NH1 
9713  N NH2 . ARG H 67  ? 1.363 0.612 0.929 0.106  0.050  -0.041 67  ARG HHH NH2 
9714  N N   . PHE H 68  ? 1.169 0.650 0.815 0.232  -0.030 0.012  68  PHE HHH N   
9715  C CA  . PHE H 68  ? 1.057 0.620 0.749 0.222  -0.032 -0.001 68  PHE HHH CA  
9716  C C   . PHE H 68  ? 1.017 0.626 0.718 0.230  -0.050 0.010  68  PHE HHH C   
9717  O O   . PHE H 68  ? 1.066 0.649 0.733 0.225  -0.055 0.026  68  PHE HHH O   
9718  C CB  . PHE H 68  ? 1.039 0.610 0.734 0.183  -0.019 -0.012 68  PHE HHH CB  
9719  C CG  . PHE H 68  ? 1.058 0.601 0.751 0.170  -0.005 -0.029 68  PHE HHH CG  
9720  C CD1 . PHE H 68  ? 1.113 0.605 0.790 0.190  0.000  -0.034 68  PHE HHH CD1 
9721  C CD2 . PHE H 68  ? 1.029 0.594 0.735 0.139  0.001  -0.042 68  PHE HHH CD2 
9722  C CE1 . PHE H 68  ? 1.139 0.602 0.809 0.175  0.013  -0.052 68  PHE HHH CE1 
9723  C CE2 . PHE H 68  ? 1.070 0.609 0.770 0.124  0.010  -0.059 68  PHE HHH CE2 
9724  C CZ  . PHE H 68  ? 1.112 0.599 0.792 0.141  0.016  -0.065 68  PHE HHH CZ  
9725  N N   . THR H 69  ? 0.963 0.639 0.708 0.240  -0.058 0.001  69  THR HHH N   
9726  C CA  . THR H 69  ? 0.938 0.667 0.699 0.244  -0.076 0.007  69  THR HHH CA  
9727  C C   . THR H 69  ? 0.875 0.663 0.671 0.222  -0.069 -0.007 69  THR HHH C   
9728  O O   . THR H 69  ? 0.837 0.651 0.663 0.225  -0.061 -0.020 69  THR HHH O   
9729  C CB  . THR H 69  ? 0.937 0.691 0.722 0.281  -0.095 0.010  69  THR HHH CB  
9730  O OG1 . THR H 69  ? 0.993 0.681 0.740 0.303  -0.101 0.025  69  THR HHH OG1 
9731  C CG2 . THR H 69  ? 0.909 0.714 0.707 0.281  -0.115 0.015  69  THR HHH CG2 
9732  N N   . ILE H 70  ? 0.844 0.646 0.633 0.200  -0.071 -0.003 70  ILE HHH N   
9733  C CA  . ILE H 70  ? 0.805 0.659 0.625 0.181  -0.068 -0.013 70  ILE HHH CA  
9734  C C   . ILE H 70  ? 0.782 0.683 0.623 0.191  -0.085 -0.012 70  ILE HHH C   
9735  O O   . ILE H 70  ? 0.846 0.735 0.665 0.202  -0.099 -0.002 70  ILE HHH O   
9736  C CB  . ILE H 70  ? 0.802 0.644 0.607 0.153  -0.059 -0.013 70  ILE HHH CB  
9737  C CG1 . ILE H 70  ? 0.775 0.658 0.610 0.137  -0.055 -0.024 70  ILE HHH CG1 
9738  C CG2 . ILE H 70  ? 0.827 0.655 0.604 0.148  -0.065 -0.003 70  ILE HHH CG2 
9739  C CD1 . ILE H 70  ? 0.752 0.628 0.584 0.114  -0.047 -0.026 70  ILE HHH CD1 
9740  N N   . SER H 71  ? 0.718 0.668 0.595 0.186  -0.083 -0.023 71  SER HHH N   
9741  C CA  . SER H 71  ? 0.699 0.700 0.605 0.189  -0.096 -0.026 71  SER HHH CA  
9742  C C   . SER H 71  ? 0.665 0.700 0.596 0.167  -0.086 -0.036 71  SER HHH C   
9743  O O   . SER H 71  ? 0.700 0.721 0.627 0.157  -0.071 -0.040 71  SER HHH O   
9744  C CB  . SER H 71  ? 0.706 0.732 0.641 0.218  -0.106 -0.028 71  SER HHH CB  
9745  O OG  . SER H 71  ? 0.702 0.736 0.660 0.223  -0.089 -0.038 71  SER HHH OG  
9746  N N   . ARG H 72  ? 0.637 0.711 0.588 0.159  -0.094 -0.039 72  ARG HHH N   
9747  C CA  . ARG H 72  ? 0.607 0.706 0.577 0.137  -0.084 -0.047 72  ARG HHH CA  
9748  C C   . ARG H 72  ? 0.593 0.747 0.604 0.138  -0.090 -0.055 72  ARG HHH C   
9749  O O   . ARG H 72  ? 0.648 0.821 0.668 0.151  -0.108 -0.054 72  ARG HHH O   
9750  C CB  . ARG H 72  ? 0.610 0.691 0.558 0.117  -0.084 -0.045 72  ARG HHH CB  
9751  C CG  . ARG H 72  ? 0.621 0.708 0.559 0.116  -0.100 -0.043 72  ARG HHH CG  
9752  C CD  . ARG H 72  ? 0.634 0.696 0.547 0.098  -0.095 -0.043 72  ARG HHH CD  
9753  N NE  . ARG H 72  ? 0.617 0.688 0.547 0.081  -0.085 -0.050 72  ARG HHH NE  
9754  C CZ  . ARG H 72  ? 0.635 0.682 0.554 0.070  -0.075 -0.050 72  ARG HHH CZ  
9755  N NH1 . ARG H 72  ? 0.662 0.682 0.559 0.071  -0.071 -0.046 72  ARG HHH NH1 
9756  N NH2 . ARG H 72  ? 0.621 0.674 0.555 0.057  -0.068 -0.054 72  ARG HHH NH2 
9757  N N   . ASP H 73  ? 0.596 0.772 0.629 0.124  -0.075 -0.063 73  ASP HHH N   
9758  C CA  . ASP H 73  ? 0.576 0.805 0.652 0.116  -0.074 -0.073 73  ASP HHH CA  
9759  C C   . ASP H 73  ? 0.562 0.785 0.631 0.087  -0.064 -0.074 73  ASP HHH C   
9760  O O   . ASP H 73  ? 0.549 0.758 0.609 0.077  -0.045 -0.074 73  ASP HHH O   
9761  C CB  . ASP H 73  ? 0.590 0.848 0.699 0.129  -0.060 -0.081 73  ASP HHH CB  
9762  C CG  . ASP H 73  ? 0.603 0.921 0.764 0.118  -0.054 -0.093 73  ASP HHH CG  
9763  O OD1 . ASP H 73  ? 0.617 0.951 0.784 0.097  -0.061 -0.095 73  ASP HHH OD1 
9764  O OD2 . ASP H 73  ? 0.612 0.963 0.808 0.130  -0.041 -0.102 73  ASP HHH OD2 
9765  N N   . ASN H 74  ? 0.547 0.774 0.612 0.074  -0.076 -0.076 74  ASN HHH N   
9766  C CA  . ASN H 74  ? 0.518 0.728 0.572 0.048  -0.068 -0.077 74  ASN HHH CA  
9767  C C   . ASN H 74  ? 0.496 0.734 0.578 0.030  -0.051 -0.084 74  ASN HHH C   
9768  O O   . ASN H 74  ? 0.472 0.682 0.536 0.015  -0.038 -0.080 74  ASN HHH O   
9769  C CB  . ASN H 74  ? 0.521 0.727 0.564 0.040  -0.084 -0.080 74  ASN HHH CB  
9770  C CG  . ASN H 74  ? 0.556 0.721 0.560 0.050  -0.090 -0.072 74  ASN HHH CG  
9771  O OD1 . ASN H 74  ? 0.532 0.672 0.520 0.062  -0.084 -0.064 74  ASN HHH OD1 
9772  N ND2 . ASN H 74  ? 0.585 0.742 0.572 0.043  -0.101 -0.075 74  ASN HHH ND2 
9773  N N   . ALA H 75  ? 0.500 0.789 0.625 0.033  -0.052 -0.093 75  ALA HHH N   
9774  C CA  . ALA H 75  ? 0.502 0.822 0.658 0.013  -0.031 -0.102 75  ALA HHH CA  
9775  C C   . ALA H 75  ? 0.525 0.819 0.659 0.013  -0.006 -0.096 75  ALA HHH C   
9776  O O   . ALA H 75  ? 0.551 0.844 0.686 -0.010 0.015  -0.098 75  ALA HHH O   
9777  C CB  . ALA H 75  ? 0.482 0.870 0.697 0.020  -0.037 -0.115 75  ALA HHH CB  
9778  N N   . LYS H 76  ? 0.549 0.816 0.659 0.035  -0.008 -0.089 76  LYS HHH N   
9779  C CA  . LYS H 76  ? 0.574 0.814 0.657 0.036  0.012  -0.086 76  LYS HHH CA  
9780  C C   . LYS H 76  ? 0.569 0.752 0.602 0.037  0.006  -0.074 76  LYS HHH C   
9781  O O   . LYS H 76  ? 0.598 0.757 0.605 0.040  0.016  -0.071 76  LYS HHH O   
9782  C CB  . LYS H 76  ? 0.595 0.852 0.693 0.062  0.017  -0.092 76  LYS HHH CB  
9783  C CG  . LYS H 76  ? 0.622 0.943 0.781 0.067  0.023  -0.106 76  LYS HHH CG  
9784  C CD  . LYS H 76  ? 0.658 0.994 0.835 0.091  0.036  -0.115 76  LYS HHH CD  
9785  C CE  . LYS H 76  ? 0.702 1.110 0.948 0.093  0.044  -0.130 76  LYS HHH CE  
9786  N NZ  . LYS H 76  ? 0.748 1.178 1.025 0.125  0.051  -0.140 76  LYS HHH NZ  
9787  N N   . ASN H 77  ? 0.570 0.735 0.593 0.033  -0.010 -0.069 77  ASN HHH N   
9788  C CA  . ASN H 77  ? 0.576 0.694 0.562 0.034  -0.017 -0.059 77  ASN HHH CA  
9789  C C   . ASN H 77  ? 0.584 0.686 0.555 0.052  -0.019 -0.057 77  ASN HHH C   
9790  O O   . ASN H 77  ? 0.580 0.651 0.524 0.050  -0.018 -0.052 77  ASN HHH O   
9791  C CB  . ASN H 77  ? 0.571 0.663 0.534 0.017  -0.006 -0.053 77  ASN HHH CB  
9792  C CG  . ASN H 77  ? 0.562 0.643 0.526 -0.000 -0.008 -0.051 77  ASN HHH CG  
9793  O OD1 . ASN H 77  ? 0.524 0.631 0.513 -0.008 -0.010 -0.058 77  ASN HHH OD1 
9794  N ND2 . ASN H 77  ? 0.561 0.603 0.498 -0.005 -0.010 -0.042 77  ASN HHH ND2 
9795  N N   . THR H 78  ? 0.569 0.689 0.556 0.069  -0.023 -0.062 78  THR HHH N   
9796  C CA  . THR H 78  ? 0.567 0.669 0.541 0.086  -0.022 -0.062 78  THR HHH CA  
9797  C C   . THR H 78  ? 0.594 0.683 0.564 0.101  -0.036 -0.058 78  THR HHH C   
9798  O O   . THR H 78  ? 0.607 0.719 0.594 0.107  -0.047 -0.059 78  THR HHH O   
9799  C CB  . THR H 78  ? 0.558 0.682 0.548 0.095  -0.006 -0.071 78  THR HHH CB  
9800  O OG1 . THR H 78  ? 0.532 0.657 0.512 0.077  0.010  -0.073 78  THR HHH OG1 
9801  C CG2 . THR H 78  ? 0.577 0.677 0.551 0.112  -0.003 -0.074 78  THR HHH CG2 
9802  N N   . VAL H 79  ? 0.614 0.667 0.559 0.104  -0.037 -0.055 79  VAL HHH N   
9803  C CA  . VAL H 79  ? 0.624 0.655 0.558 0.117  -0.045 -0.051 79  VAL HHH CA  
9804  C C   . VAL H 79  ? 0.647 0.661 0.573 0.131  -0.037 -0.056 79  VAL HHH C   
9805  O O   . VAL H 79  ? 0.637 0.643 0.553 0.125  -0.027 -0.062 79  VAL HHH O   
9806  C CB  . VAL H 79  ? 0.628 0.631 0.543 0.105  -0.048 -0.047 79  VAL HHH CB  
9807  C CG1 . VAL H 79  ? 0.634 0.620 0.538 0.095  -0.043 -0.049 79  VAL HHH CG1 
9808  C CG2 . VAL H 79  ? 0.670 0.647 0.569 0.114  -0.052 -0.042 79  VAL HHH CG2 
9809  N N   . TYR H 80  ? 0.665 0.670 0.592 0.151  -0.042 -0.054 80  TYR HHH N   
9810  C CA  . TYR H 80  ? 0.693 0.676 0.614 0.169  -0.035 -0.059 80  TYR HHH CA  
9811  C C   . TYR H 80  ? 0.720 0.653 0.611 0.173  -0.039 -0.052 80  TYR HHH C   
9812  O O   . TYR H 80  ? 0.698 0.622 0.579 0.170  -0.049 -0.042 80  TYR HHH O   
9813  C CB  . TYR H 80  ? 0.692 0.707 0.644 0.193  -0.038 -0.062 80  TYR HHH CB  
9814  C CG  . TYR H 80  ? 0.678 0.746 0.665 0.187  -0.030 -0.071 80  TYR HHH CG  
9815  C CD1 . TYR H 80  ? 0.681 0.754 0.671 0.184  -0.009 -0.083 80  TYR HHH CD1 
9816  C CD2 . TYR H 80  ? 0.663 0.773 0.677 0.181  -0.040 -0.069 80  TYR HHH CD2 
9817  C CE1 . TYR H 80  ? 0.663 0.781 0.682 0.175  0.003  -0.091 80  TYR HHH CE1 
9818  C CE2 . TYR H 80  ? 0.632 0.790 0.680 0.172  -0.030 -0.078 80  TYR HHH CE2 
9819  C CZ  . TYR H 80  ? 0.654 0.815 0.704 0.168  -0.007 -0.088 80  TYR HHH CZ  
9820  O OH  . TYR H 80  ? 0.675 0.878 0.754 0.155  0.008  -0.097 80  TYR HHH OH  
9821  N N   . LEU H 81  ? 0.769 0.667 0.644 0.176  -0.029 -0.058 81  LEU HHH N   
9822  C CA  . LEU H 81  ? 0.818 0.661 0.664 0.182  -0.030 -0.053 81  LEU HHH CA  
9823  C C   . LEU H 81  ? 0.860 0.681 0.707 0.208  -0.023 -0.060 81  LEU HHH C   
9824  O O   . LEU H 81  ? 0.891 0.703 0.733 0.205  -0.010 -0.074 81  LEU HHH O   
9825  C CB  . LEU H 81  ? 0.809 0.625 0.636 0.156  -0.024 -0.058 81  LEU HHH CB  
9826  C CG  . LEU H 81  ? 0.855 0.616 0.654 0.152  -0.022 -0.052 81  LEU HHH CG  
9827  C CD1 . LEU H 81  ? 0.843 0.604 0.636 0.149  -0.029 -0.037 81  LEU HHH CD1 
9828  C CD2 . LEU H 81  ? 0.874 0.614 0.663 0.127  -0.016 -0.062 81  LEU HHH CD2 
9829  N N   . GLN H 82  ? 0.883 0.697 0.733 0.233  -0.033 -0.050 82  GLN HHH N   
9830  C CA  . GLN H 82  ? 0.933 0.716 0.782 0.264  -0.030 -0.053 82  GLN HHH CA  
9831  C C   . GLN H 82  ? 0.998 0.706 0.804 0.257  -0.024 -0.049 82  GLN HHH C   
9832  O O   . GLN H 82  ? 1.038 0.719 0.819 0.248  -0.032 -0.034 82  GLN HHH O   
9833  C CB  . GLN H 82  ? 0.928 0.735 0.800 0.294  -0.048 -0.043 82  GLN HHH CB  
9834  C CG  . GLN H 82  ? 0.981 0.769 0.865 0.333  -0.047 -0.047 82  GLN HHH CG  
9835  C CD  . GLN H 82  ? 0.975 0.788 0.888 0.337  -0.025 -0.070 82  GLN HHH CD  
9836  O OE1 . GLN H 82  ? 0.896 0.771 0.843 0.327  -0.020 -0.079 82  GLN HHH OE1 
9837  N NE2 . GLN H 82  ? 1.037 0.797 0.932 0.351  -0.011 -0.079 82  GLN HHH NE2 
9838  N N   . MET H 83  ? 1.014 0.687 0.808 0.255  -0.009 -0.064 83  MET HHH N   
9839  C CA  . MET H 83  ? 1.060 0.657 0.813 0.245  -0.001 -0.064 83  MET HHH CA  
9840  C C   . MET H 83  ? 1.088 0.638 0.834 0.279  0.004  -0.067 83  MET HHH C   
9841  O O   . MET H 83  ? 1.091 0.652 0.852 0.290  0.016  -0.086 83  MET HHH O   
9842  C CB  . MET H 83  ? 1.065 0.656 0.807 0.212  0.010  -0.081 83  MET HHH CB  
9843  C CG  . MET H 83  ? 1.017 0.658 0.772 0.184  0.004  -0.079 83  MET HHH CG  
9844  S SD  . MET H 83  ? 1.062 0.696 0.804 0.149  0.010  -0.098 83  MET HHH SD  
9845  C CE  . MET H 83  ? 1.092 0.746 0.837 0.164  0.020  -0.116 83  MET HHH CE  
9846  N N   . ASN H 84  ? 1.154 0.652 0.876 0.295  -0.004 -0.049 84  ASN HHH N   
9847  C CA  . ASN H 84  ? 1.233 0.674 0.944 0.332  -0.002 -0.049 84  ASN HHH CA  
9848  C C   . ASN H 84  ? 1.308 0.654 0.968 0.315  0.011  -0.048 84  ASN HHH C   
9849  O O   . ASN H 84  ? 1.262 0.593 0.898 0.278  0.013  -0.042 84  ASN HHH O   
9850  C CB  . ASN H 84  ? 1.242 0.691 0.962 0.369  -0.025 -0.027 84  ASN HHH CB  
9851  C CG  . ASN H 84  ? 1.190 0.735 0.968 0.384  -0.036 -0.032 84  ASN HHH CG  
9852  O OD1 . ASN H 84  ? 1.164 0.753 0.977 0.386  -0.022 -0.054 84  ASN HHH OD1 
9853  N ND2 . ASN H 84  ? 1.184 0.759 0.967 0.393  -0.060 -0.014 84  ASN HHH ND2 
9854  N N   . ARG H 85  ? 1.398 0.684 1.046 0.341  0.020  -0.057 85  ARG HHH N   
9855  C CA  . ARG H 85  ? 1.482 0.665 1.079 0.329  0.032  -0.056 85  ARG HHH CA  
9856  C C   . ARG H 85  ? 1.431 0.612 1.013 0.276  0.045  -0.070 85  ARG HHH C   
9857  O O   . ARG H 85  ? 1.435 0.574 0.986 0.247  0.047  -0.057 85  ARG HHH O   
9858  C CB  . ARG H 85  ? 1.566 0.695 1.129 0.345  0.019  -0.024 85  ARG HHH CB  
9859  C CG  . ARG H 85  ? 1.629 0.766 1.212 0.402  0.000  -0.011 85  ARG HHH CG  
9860  C CD  . ARG H 85  ? 1.750 0.810 1.288 0.427  -0.015 0.020  85  ARG HHH CD  
9861  N NE  . ARG H 85  ? 1.791 0.826 1.282 0.392  -0.018 0.042  85  ARG HHH NE  
9862  C CZ  . ARG H 85  ? 1.740 0.843 1.243 0.376  -0.031 0.052  85  ARG HHH CZ  
9863  N NH1 . ARG H 85  ? 1.674 0.876 1.233 0.390  -0.045 0.044  85  ARG HHH NH1 
9864  N NH2 . ARG H 85  ? 1.750 0.820 1.206 0.343  -0.028 0.070  85  ARG HHH NH2 
9865  N N   . LEU H 86  ? 1.371 0.601 0.976 0.263  0.052  -0.095 86  LEU HHH N   
9866  C CA  . LEU H 86  ? 1.340 0.582 0.939 0.215  0.058  -0.110 86  LEU HHH CA  
9867  C C   . LEU H 86  ? 1.422 0.575 0.980 0.194  0.072  -0.122 86  LEU HHH C   
9868  O O   . LEU H 86  ? 1.527 0.622 1.069 0.218  0.083  -0.133 86  LEU HHH O   
9869  C CB  . LEU H 86  ? 1.297 0.604 0.921 0.213  0.061  -0.131 86  LEU HHH CB  
9870  C CG  . LEU H 86  ? 1.211 0.607 0.871 0.215  0.048  -0.121 86  LEU HHH CG  
9871  C CD1 . LEU H 86  ? 1.176 0.624 0.856 0.222  0.054  -0.139 86  LEU HHH CD1 
9872  C CD2 . LEU H 86  ? 1.159 0.583 0.821 0.178  0.039  -0.113 86  LEU HHH CD2 
9873  N N   . LYS H 87  ? 1.406 0.552 0.954 0.150  0.073  -0.123 87  LYS HHH N   
9874  C CA  . LYS H 87  ? 1.479 0.549 0.995 0.118  0.087  -0.137 87  LYS HHH CA  
9875  C C   . LYS H 87  ? 1.439 0.550 0.967 0.080  0.084  -0.162 87  LYS HHH C   
9876  O O   . LYS H 87  ? 1.372 0.563 0.930 0.074  0.072  -0.161 87  LYS HHH O   
9877  C CB  . LYS H 87  ? 1.521 0.548 1.017 0.097  0.090  -0.115 87  LYS HHH CB  
9878  C CG  . LYS H 87  ? 1.546 0.557 1.031 0.133  0.084  -0.083 87  LYS HHH CG  
9879  C CD  . LYS H 87  ? 1.576 0.553 1.037 0.110  0.089  -0.059 87  LYS HHH CD  
9880  C CE  . LYS H 87  ? 1.634 0.573 1.067 0.151  0.081  -0.029 87  LYS HHH CE  
9881  N NZ  . LYS H 87  ? 1.694 0.588 1.089 0.129  0.087  -0.004 87  LYS HHH NZ  
9882  N N   . PRO H 88  ? 1.513 0.570 1.017 0.054  0.094  -0.187 88  PRO HHH N   
9883  C CA  . PRO H 88  ? 1.495 0.589 1.007 0.016  0.086  -0.211 88  PRO HHH CA  
9884  C C   . PRO H 88  ? 1.423 0.585 0.970 -0.015 0.073  -0.201 88  PRO HHH C   
9885  O O   . PRO H 88  ? 1.377 0.603 0.944 -0.026 0.059  -0.212 88  PRO HHH O   
9886  C CB  . PRO H 88  ? 1.580 0.587 1.058 -0.010 0.099  -0.233 88  PRO HHH CB  
9887  C CG  . PRO H 88  ? 1.646 0.581 1.095 0.032  0.114  -0.231 88  PRO HHH CG  
9888  C CD  . PRO H 88  ? 1.618 0.571 1.082 0.063  0.110  -0.195 88  PRO HHH CD  
9889  N N   . GLU H 89  ? 1.425 0.570 0.976 -0.025 0.079  -0.181 89  GLU HHH N   
9890  C CA  . GLU H 89  ? 1.368 0.573 0.955 -0.053 0.072  -0.172 89  GLU HHH CA  
9891  C C   . GLU H 89  ? 1.268 0.557 0.886 -0.030 0.057  -0.158 89  GLU HHH C   
9892  O O   . GLU H 89  ? 1.211 0.553 0.861 -0.049 0.051  -0.153 89  GLU HHH O   
9893  C CB  . GLU H 89  ? 1.430 0.590 1.004 -0.063 0.088  -0.150 89  GLU HHH CB  
9894  C CG  . GLU H 89  ? 1.572 0.635 1.109 -0.084 0.107  -0.158 89  GLU HHH CG  
9895  C CD  . GLU H 89  ? 1.679 0.659 1.171 -0.046 0.115  -0.147 89  GLU HHH CD  
9896  O OE1 . GLU H 89  ? 1.740 0.723 1.224 -0.010 0.111  -0.121 89  GLU HHH OE1 
9897  O OE2 . GLU H 89  ? 1.708 0.619 1.172 -0.051 0.124  -0.166 89  GLU HHH OE2 
9898  N N   . ASP H 90  ? 1.249 0.547 0.860 0.008  0.054  -0.152 90  ASP HHH N   
9899  C CA  . ASP H 90  ? 1.161 0.535 0.800 0.029  0.041  -0.141 90  ASP HHH CA  
9900  C C   . ASP H 90  ? 1.123 0.546 0.773 0.020  0.029  -0.160 90  ASP HHH C   
9901  O O   . ASP H 90  ? 1.063 0.548 0.736 0.028  0.019  -0.152 90  ASP HHH O   
9902  C CB  . ASP H 90  ? 1.164 0.531 0.796 0.072  0.043  -0.127 90  ASP HHH CB  
9903  C CG  . ASP H 90  ? 1.194 0.519 0.811 0.085  0.048  -0.103 90  ASP HHH CG  
9904  O OD1 . ASP H 90  ? 1.174 0.514 0.798 0.065  0.047  -0.091 90  ASP HHH OD1 
9905  O OD2 . ASP H 90  ? 1.225 0.503 0.822 0.115  0.052  -0.098 90  ASP HHH OD2 
9906  N N   . THR H 91  ? 1.160 0.550 0.789 0.003  0.031  -0.184 91  THR HHH N   
9907  C CA  . THR H 91  ? 1.149 0.576 0.776 -0.008 0.018  -0.203 91  THR HHH CA  
9908  C C   . THR H 91  ? 1.091 0.579 0.752 -0.031 -0.000 -0.198 91  THR HHH C   
9909  O O   . THR H 91  ? 1.102 0.584 0.779 -0.058 -0.001 -0.201 91  THR HHH O   
9910  C CB  . THR H 91  ? 1.225 0.598 0.817 -0.027 0.022  -0.230 91  THR HHH CB  
9911  O OG1 . THR H 91  ? 1.270 0.590 0.834 0.002  0.041  -0.234 91  THR HHH OG1 
9912  C CG2 . THR H 91  ? 1.222 0.627 0.803 -0.042 0.006  -0.249 91  THR HHH CG2 
9913  N N   . ALA H 92  ? 1.043 0.587 0.716 -0.021 -0.013 -0.193 92  ALA HHH N   
9914  C CA  . ALA H 92  ? 0.999 0.602 0.706 -0.037 -0.033 -0.188 92  ALA HHH CA  
9915  C C   . ALA H 92  ? 0.984 0.630 0.690 -0.019 -0.043 -0.180 92  ALA HHH C   
9916  O O   . ALA H 92  ? 1.046 0.681 0.731 0.003  -0.031 -0.177 92  ALA HHH O   
9917  C CB  . ALA H 92  ? 0.964 0.583 0.705 -0.040 -0.028 -0.171 92  ALA HHH CB  
9918  N N   . VAL H 93  ? 0.951 0.643 0.680 -0.029 -0.063 -0.176 93  VAL HHH N   
9919  C CA  . VAL H 93  ? 0.884 0.617 0.620 -0.015 -0.071 -0.162 93  VAL HHH CA  
9920  C C   . VAL H 93  ? 0.837 0.589 0.604 -0.002 -0.061 -0.143 93  VAL HHH C   
9921  O O   . VAL H 93  ? 0.836 0.595 0.633 -0.012 -0.061 -0.140 93  VAL HHH O   
9922  C CB  . VAL H 93  ? 0.871 0.637 0.616 -0.029 -0.098 -0.165 93  VAL HHH CB  
9923  C CG1 . VAL H 93  ? 0.840 0.640 0.592 -0.014 -0.106 -0.148 93  VAL HHH CG1 
9924  C CG2 . VAL H 93  ? 0.906 0.650 0.611 -0.043 -0.111 -0.184 93  VAL HHH CG2 
9925  N N   . TYR H 94  ? 0.833 0.592 0.594 0.020  -0.052 -0.133 94  TYR HHH N   
9926  C CA  . TYR H 94  ? 0.801 0.580 0.586 0.033  -0.045 -0.116 94  TYR HHH CA  
9927  C C   . TYR H 94  ? 0.781 0.600 0.581 0.035  -0.057 -0.106 94  TYR HHH C   
9928  O O   . TYR H 94  ? 0.781 0.607 0.563 0.039  -0.059 -0.108 94  TYR HHH O   
9929  C CB  . TYR H 94  ? 0.812 0.573 0.585 0.055  -0.030 -0.112 94  TYR HHH CB  
9930  C CG  . TYR H 94  ? 0.851 0.565 0.612 0.057  -0.019 -0.115 94  TYR HHH CG  
9931  C CD1 . TYR H 94  ? 0.918 0.592 0.655 0.048  -0.015 -0.131 94  TYR HHH CD1 
9932  C CD2 . TYR H 94  ? 0.848 0.553 0.617 0.065  -0.014 -0.101 94  TYR HHH CD2 
9933  C CE1 . TYR H 94  ? 0.974 0.597 0.697 0.048  -0.004 -0.133 94  TYR HHH CE1 
9934  C CE2 . TYR H 94  ? 0.900 0.554 0.651 0.067  -0.004 -0.101 94  TYR HHH CE2 
9935  C CZ  . TYR H 94  ? 0.976 0.587 0.706 0.059  0.002  -0.116 94  TYR HHH CZ  
9936  O OH  . TYR H 94  ? 1.048 0.601 0.758 0.060  0.012  -0.114 94  TYR HHH OH  
9937  N N   . PHE H 95  ? 0.743 0.585 0.575 0.030  -0.062 -0.098 95  PHE HHH N   
9938  C CA  . PHE H 95  ? 0.684 0.559 0.535 0.032  -0.072 -0.090 95  PHE HHH CA  
9939  C C   . PHE H 95  ? 0.671 0.558 0.533 0.043  -0.062 -0.078 95  PHE HHH C   
9940  O O   . PHE H 95  ? 0.652 0.533 0.524 0.044  -0.053 -0.075 95  PHE HHH O   
9941  C CB  . PHE H 95  ? 0.646 0.540 0.528 0.019  -0.085 -0.092 95  PHE HHH CB  
9942  C CG  . PHE H 95  ? 0.663 0.555 0.541 0.006  -0.101 -0.104 95  PHE HHH CG  
9943  C CD1 . PHE H 95  ? 0.682 0.556 0.561 -0.008 -0.097 -0.117 95  PHE HHH CD1 
9944  C CD2 . PHE H 95  ? 0.672 0.577 0.542 0.007  -0.122 -0.103 95  PHE HHH CD2 
9945  C CE1 . PHE H 95  ? 0.722 0.596 0.598 -0.023 -0.115 -0.131 95  PHE HHH CE1 
9946  C CE2 . PHE H 95  ? 0.706 0.610 0.568 -0.005 -0.142 -0.115 95  PHE HHH CE2 
9947  C CZ  . PHE H 95  ? 0.720 0.612 0.588 -0.021 -0.139 -0.130 95  PHE HHH CZ  
9948  N N   . CYS H 96  ? 0.664 0.567 0.524 0.050  -0.064 -0.072 96  CYS HHH N   
9949  C CA  . CYS H 96  ? 0.664 0.585 0.538 0.057  -0.060 -0.063 96  CYS HHH CA  
9950  C C   . CYS H 96  ? 0.618 0.554 0.517 0.051  -0.068 -0.060 96  CYS HHH C   
9951  O O   . CYS H 96  ? 0.617 0.557 0.520 0.045  -0.081 -0.062 96  CYS HHH O   
9952  C CB  . CYS H 96  ? 0.716 0.646 0.578 0.061  -0.058 -0.060 96  CYS HHH CB  
9953  S SG  . CYS H 96  ? 0.791 0.744 0.671 0.067  -0.052 -0.052 96  CYS HHH SG  
9954  N N   . ALA H 97  ? 0.585 0.528 0.499 0.052  -0.062 -0.056 97  ALA HHH N   
9955  C CA  . ALA H 97  ? 0.556 0.513 0.495 0.049  -0.065 -0.056 97  ALA HHH CA  
9956  C C   . ALA H 97  ? 0.547 0.510 0.488 0.053  -0.058 -0.051 97  ALA HHH C   
9957  O O   . ALA H 97  ? 0.551 0.510 0.477 0.057  -0.052 -0.049 97  ALA HHH O   
9958  C CB  . ALA H 97  ? 0.556 0.512 0.515 0.040  -0.061 -0.062 97  ALA HHH CB  
9959  N N   . ALA H 98  ? 0.522 0.493 0.481 0.052  -0.061 -0.051 98  ALA HHH N   
9960  C CA  . ALA H 98  ? 0.531 0.506 0.490 0.053  -0.056 -0.050 98  ALA HHH CA  
9961  C C   . ALA H 98  ? 0.547 0.525 0.530 0.052  -0.053 -0.054 98  ALA HHH C   
9962  O O   . ALA H 98  ? 0.569 0.552 0.574 0.054  -0.061 -0.056 98  ALA HHH O   
9963  C CB  . ALA H 98  ? 0.539 0.516 0.489 0.054  -0.061 -0.045 98  ALA HHH CB  
9964  N N   . ASP H 99  ? 0.538 0.514 0.517 0.050  -0.043 -0.057 99  ASP HHH N   
9965  C CA  . ASP H 99  ? 0.550 0.527 0.549 0.050  -0.035 -0.065 99  ASP HHH CA  
9966  C C   . ASP H 99  ? 0.536 0.506 0.517 0.047  -0.029 -0.068 99  ASP HHH C   
9967  O O   . ASP H 99  ? 0.521 0.490 0.477 0.044  -0.029 -0.065 99  ASP HHH O   
9968  C CB  . ASP H 99  ? 0.567 0.548 0.582 0.046  -0.023 -0.072 99  ASP HHH CB  
9969  C CG  . ASP H 99  ? 0.566 0.554 0.617 0.049  -0.017 -0.082 99  ASP HHH CG  
9970  O OD1 . ASP H 99  ? 0.553 0.553 0.634 0.056  -0.029 -0.081 99  ASP HHH OD1 
9971  O OD2 . ASP H 99  ? 0.576 0.558 0.623 0.047  -0.000 -0.090 99  ASP HHH OD2 
9972  N N   . ARG H 100 ? 0.580 0.554 0.514 -0.054 0.000  0.007  100 ARG HHH N   
9973  C CA  . ARG H 100 ? 0.548 0.539 0.528 -0.038 0.016  -0.009 100 ARG HHH CA  
9974  C C   . ARG H 100 ? 0.530 0.515 0.515 -0.018 0.022  -0.028 100 ARG HHH C   
9975  O O   . ARG H 100 ? 0.524 0.525 0.510 -0.011 0.032  -0.046 100 ARG HHH O   
9976  C CB  . ARG H 100 ? 0.555 0.546 0.599 -0.048 0.014  0.014  100 ARG HHH CB  
9977  C CG  . ARG H 100 ? 0.593 0.592 0.631 -0.072 0.005  0.040  100 ARG HHH CG  
9978  C CD  . ARG H 100 ? 0.612 0.630 0.640 -0.072 0.025  0.018  100 ARG HHH CD  
9979  N NE  . ARG H 100 ? 0.604 0.627 0.680 -0.062 0.041  -0.004 100 ARG HHH NE  
9980  C CZ  . ARG H 100 ? 0.596 0.609 0.733 -0.071 0.051  0.005  100 ARG HHH CZ  
9981  N NH1 . ARG H 100 ? 0.630 0.634 0.805 -0.086 0.039  0.046  100 ARG HHH NH1 
9982  N NH2 . ARG H 100 ? 0.582 0.592 0.742 -0.071 0.072  -0.026 100 ARG HHH NH2 
9983  N N   . GLY H 101 ? 0.557 0.523 0.543 -0.017 0.014  -0.019 101 GLY HHH N   
9984  C CA  . GLY H 101 ? 0.542 0.498 0.530 -0.006 0.022  -0.032 101 GLY HHH CA  
9985  C C   . GLY H 101 ? 0.581 0.527 0.522 0.005  0.016  -0.038 101 GLY HHH C   
9986  O O   . GLY H 101 ? 0.625 0.557 0.538 0.001  0.009  -0.033 101 GLY HHH O   
9987  N N   . GLU H 102 ? 0.585 0.533 0.516 0.014  0.021  -0.048 102 GLU HHH N   
9988  C CA  . GLU H 102 ? 0.589 0.522 0.493 0.026  0.016  -0.046 102 GLU HHH CA  
9989  C C   . GLU H 102 ? 0.576 0.486 0.480 0.019  0.017  -0.041 102 GLU HHH C   
9990  O O   . GLU H 102 ? 0.559 0.474 0.473 0.010  0.029  -0.047 102 GLU HHH O   
9991  C CB  . GLU H 102 ? 0.587 0.543 0.488 0.035  0.011  -0.047 102 GLU HHH CB  
9992  C CG  . GLU H 102 ? 0.608 0.550 0.501 0.051  0.004  -0.034 102 GLU HHH CG  
9993  C CD  . GLU H 102 ? 0.635 0.610 0.541 0.056  -0.011 -0.019 102 GLU HHH CD  
9994  O OE1 . GLU H 102 ? 0.653 0.667 0.575 0.049  -0.015 -0.022 102 GLU HHH OE1 
9995  O OE2 . GLU H 102 ? 0.697 0.661 0.601 0.063  -0.022 0.002  102 GLU HHH OE2 
9996  N N   . SER H 103 ? 0.606 0.489 0.497 0.019  0.011  -0.034 103 SER HHH N   
9997  C CA  . SER H 103 ? 0.620 0.484 0.520 0.010  0.011  -0.025 103 SER HHH CA  
9998  C C   . SER H 103 ? 0.662 0.509 0.534 0.016  0.014  -0.024 103 SER HHH C   
9999  O O   . SER H 103 ? 0.655 0.490 0.507 0.030  0.008  -0.022 103 SER HHH O   
10000 C CB  . SER H 103 ? 0.618 0.466 0.518 -0.003 -0.003 -0.015 103 SER HHH CB  
10001 O OG  . SER H 103 ? 0.597 0.435 0.519 -0.013 -0.003 -0.003 103 SER HHH OG  
10002 N N   . TYR H 104 ? 0.665 0.508 0.542 0.005  0.025  -0.022 104 TYR HHH N   
10003 C CA  . TYR H 104 ? 0.693 0.513 0.541 0.003  0.025  -0.013 104 TYR HHH CA  
10004 C C   . TYR H 104 ? 0.682 0.470 0.529 0.005  0.015  -0.005 104 TYR HHH C   
10005 O O   . TYR H 104 ? 0.712 0.475 0.537 0.013  0.011  0.003  104 TYR HHH O   
10006 C CB  . TYR H 104 ? 0.698 0.516 0.551 -0.018 0.049  -0.016 104 TYR HHH CB  
10007 C CG  . TYR H 104 ? 0.769 0.563 0.583 -0.027 0.049  -0.002 104 TYR HHH CG  
10008 C CD1 . TYR H 104 ? 0.829 0.624 0.595 -0.029 0.035  0.012  104 TYR HHH CD1 
10009 C CD2 . TYR H 104 ? 0.803 0.576 0.635 -0.037 0.058  0.005  104 TYR HHH CD2 
10010 C CE1 . TYR H 104 ? 0.906 0.678 0.638 -0.039 0.030  0.034  104 TYR HHH CE1 
10011 C CE2 . TYR H 104 ? 0.845 0.593 0.640 -0.047 0.059  0.020  104 TYR HHH CE2 
10012 C CZ  . TYR H 104 ? 0.904 0.649 0.647 -0.048 0.044  0.037  104 TYR HHH CZ  
10013 O OH  . TYR H 104 ? 0.984 0.703 0.692 -0.061 0.040  0.062  104 TYR HHH OH  
10014 N N   . TYR H 105 ? 0.657 0.447 0.529 -0.005 0.009  -0.005 105 TYR HHH N   
10015 C CA  . TYR H 105 ? 0.678 0.438 0.537 -0.018 -0.003 -0.002 105 TYR HHH CA  
10016 C C   . TYR H 105 ? 0.705 0.458 0.535 -0.017 -0.009 -0.014 105 TYR HHH C   
10017 O O   . TYR H 105 ? 0.735 0.491 0.558 -0.042 -0.023 -0.011 105 TYR HHH O   
10018 C CB  . TYR H 105 ? 0.671 0.445 0.575 -0.042 -0.012 0.014  105 TYR HHH CB  
10019 C CG  . TYR H 105 ? 0.676 0.463 0.627 -0.044 0.007  0.021  105 TYR HHH CG  
10020 C CD1 . TYR H 105 ? 0.697 0.458 0.626 -0.047 0.019  0.023  105 TYR HHH CD1 
10021 C CD2 . TYR H 105 ? 0.653 0.472 0.675 -0.045 0.020  0.027  105 TYR HHH CD2 
10022 C CE1 . TYR H 105 ? 0.707 0.478 0.671 -0.056 0.046  0.025  105 TYR HHH CE1 
10023 C CE2 . TYR H 105 ? 0.657 0.482 0.727 -0.050 0.053  0.025  105 TYR HHH CE2 
10024 C CZ  . TYR H 105 ? 0.692 0.494 0.726 -0.058 0.067  0.022  105 TYR HHH CZ  
10025 O OH  . TYR H 105 ? 0.760 0.566 0.835 -0.069 0.108  0.017  105 TYR HHH OH  
10026 N N   . TYR H 106 ? 0.717 0.464 0.532 0.005  0.002  -0.025 106 TYR HHH N   
10027 C CA  . TYR H 106 ? 0.736 0.480 0.535 0.010  0.011  -0.041 106 TYR HHH CA  
10028 C C   . TYR H 106 ? 0.813 0.509 0.568 -0.014 0.018  -0.058 106 TYR HHH C   
10029 O O   . TYR H 106 ? 0.815 0.507 0.545 -0.024 0.031  -0.076 106 TYR HHH O   
10030 C CB  . TYR H 106 ? 0.745 0.496 0.563 0.041  0.023  -0.043 106 TYR HHH CB  
10031 C CG  . TYR H 106 ? 0.797 0.513 0.624 0.057  0.028  -0.032 106 TYR HHH CG  
10032 C CD1 . TYR H 106 ? 0.865 0.528 0.688 0.059  0.049  -0.047 106 TYR HHH CD1 
10033 C CD2 . TYR H 106 ? 0.793 0.526 0.632 0.064  0.014  -0.008 106 TYR HHH CD2 
10034 C CE1 . TYR H 106 ? 0.903 0.529 0.748 0.075  0.054  -0.032 106 TYR HHH CE1 
10035 C CE2 . TYR H 106 ? 0.831 0.533 0.678 0.074  0.013  0.013  106 TYR HHH CE2 
10036 C CZ  . TYR H 106 ? 0.886 0.534 0.745 0.083  0.032  0.003  106 TYR HHH CZ  
10037 O OH  . TYR H 106 ? 0.939 0.551 0.821 0.095  0.032  0.028  106 TYR HHH OH  
10038 N N   . THR H 107 ? 0.743 0.581 0.586 -0.081 -0.018 -0.036 107 THR HHH N   
10039 C CA  . THR H 107 ? 0.736 0.566 0.580 -0.074 -0.027 -0.031 107 THR HHH CA  
10040 C C   . THR H 107 ? 0.711 0.556 0.570 -0.069 -0.016 -0.032 107 THR HHH C   
10041 O O   . THR H 107 ? 0.758 0.599 0.618 -0.066 -0.023 -0.030 107 THR HHH O   
10042 C CB  . THR H 107 ? 0.775 0.590 0.601 -0.088 -0.041 -0.023 107 THR HHH CB  
10043 O OG1 . THR H 107 ? 0.814 0.644 0.635 -0.103 -0.034 -0.021 107 THR HHH OG1 
10044 C CG2 . THR H 107 ? 0.784 0.586 0.596 -0.094 -0.053 -0.018 107 THR HHH CG2 
10045 N N   . ARG H 108 ? 0.700 0.563 0.571 -0.069 0.000  -0.035 108 ARG HHH N   
10046 C CA  . ARG H 108 ? 0.664 0.546 0.556 -0.063 0.010  -0.031 108 ARG HHH CA  
10047 C C   . ARG H 108 ? 0.650 0.532 0.557 -0.048 0.013  -0.033 108 ARG HHH C   
10048 O O   . ARG H 108 ? 0.635 0.513 0.546 -0.042 0.021  -0.040 108 ARG HHH O   
10049 C CB  . ARG H 108 ? 0.658 0.557 0.561 -0.065 0.029  -0.033 108 ARG HHH CB  
10050 C CG  . ARG H 108 ? 0.663 0.572 0.555 -0.081 0.029  -0.030 108 ARG HHH CG  
10051 C CD  . ARG H 108 ? 0.655 0.585 0.564 -0.078 0.052  -0.033 108 ARG HHH CD  
10052 N NE  . ARG H 108 ? 0.670 0.610 0.564 -0.097 0.055  -0.033 108 ARG HHH NE  
10053 C CZ  . ARG H 108 ? 0.684 0.642 0.586 -0.099 0.076  -0.038 108 ARG HHH CZ  
10054 N NH1 . ARG H 108 ? 0.697 0.659 0.622 -0.082 0.097  -0.044 108 ARG HHH NH1 
10055 N NH2 . ARG H 108 ? 0.719 0.686 0.603 -0.120 0.076  -0.039 108 ARG HHH NH2 
10056 N N   . PRO H 109 ? 0.633 0.522 0.546 -0.045 0.006  -0.028 109 PRO HHH N   
10057 C CA  . PRO H 109 ? 0.599 0.493 0.527 -0.034 0.009  -0.027 109 PRO HHH CA  
10058 C C   . PRO H 109 ? 0.562 0.468 0.512 -0.025 0.025  -0.026 109 PRO HHH C   
10059 O O   . PRO H 109 ? 0.529 0.429 0.483 -0.018 0.029  -0.030 109 PRO HHH O   
10060 C CB  . PRO H 109 ? 0.612 0.517 0.541 -0.039 0.000  -0.018 109 PRO HHH CB  
10061 C CG  . PRO H 109 ? 0.640 0.529 0.545 -0.051 -0.011 -0.020 109 PRO HHH CG  
10062 C CD  . PRO H 109 ? 0.641 0.529 0.543 -0.056 -0.006 -0.021 109 PRO HHH CD  
10063 N N   . THR H 110 ? 0.548 0.469 0.509 -0.026 0.035  -0.020 110 THR HHH N   
10064 C CA  . THR H 110 ? 0.540 0.470 0.526 -0.015 0.054  -0.018 110 THR HHH CA  
10065 C C   . THR H 110 ? 0.559 0.466 0.534 -0.013 0.066  -0.032 110 THR HHH C   
10066 O O   . THR H 110 ? 0.569 0.470 0.557 -0.003 0.081  -0.033 110 THR HHH O   
10067 C CB  . THR H 110 ? 0.527 0.483 0.530 -0.015 0.063  -0.009 110 THR HHH CB  
10068 O OG1 . THR H 110 ? 0.579 0.531 0.562 -0.028 0.064  -0.017 110 THR HHH OG1 
10069 C CG2 . THR H 110 ? 0.505 0.490 0.521 -0.019 0.051  0.008  110 THR HHH CG2 
10070 N N   . GLU H 111 ? 0.579 0.470 0.527 -0.024 0.060  -0.042 111 GLU HHH N   
10071 C CA  . GLU H 111 ? 0.605 0.476 0.538 -0.028 0.070  -0.054 111 GLU HHH CA  
10072 C C   . GLU H 111 ? 0.596 0.457 0.527 -0.024 0.064  -0.056 111 GLU HHH C   
10073 O O   . GLU H 111 ? 0.639 0.484 0.555 -0.030 0.071  -0.064 111 GLU HHH O   
10074 C CB  . GLU H 111 ? 0.629 0.494 0.537 -0.045 0.063  -0.059 111 GLU HHH CB  
10075 C CG  . GLU H 111 ? 0.647 0.523 0.554 -0.053 0.073  -0.059 111 GLU HHH CG  
10076 C CD  . GLU H 111 ? 0.668 0.539 0.577 -0.052 0.099  -0.069 111 GLU HHH CD  
10077 O OE1 . GLU H 111 ? 0.666 0.540 0.599 -0.036 0.112  -0.067 111 GLU HHH OE1 
10078 O OE2 . GLU H 111 ? 0.691 0.555 0.578 -0.068 0.106  -0.078 111 GLU HHH OE2 
10079 N N   . TYR H 112 ? 0.585 0.454 0.525 -0.017 0.052  -0.049 112 TYR HHH N   
10080 C CA  . TYR H 112 ? 0.593 0.459 0.532 -0.014 0.047  -0.050 112 TYR HHH CA  
10081 C C   . TYR H 112 ? 0.573 0.444 0.531 -0.005 0.051  -0.042 112 TYR HHH C   
10082 O O   . TYR H 112 ? 0.543 0.430 0.514 -0.002 0.045  -0.032 112 TYR HHH O   
10083 C CB  . TYR H 112 ? 0.575 0.446 0.505 -0.016 0.030  -0.051 112 TYR HHH CB  
10084 C CG  . TYR H 112 ? 0.568 0.432 0.482 -0.024 0.024  -0.055 112 TYR HHH CG  
10085 C CD1 . TYR H 112 ? 0.580 0.443 0.489 -0.029 0.019  -0.052 112 TYR HHH CD1 
10086 C CD2 . TYR H 112 ? 0.586 0.448 0.490 -0.029 0.021  -0.059 112 TYR HHH CD2 
10087 C CE1 . TYR H 112 ? 0.597 0.454 0.490 -0.038 0.012  -0.052 112 TYR HHH CE1 
10088 C CE2 . TYR H 112 ? 0.620 0.479 0.509 -0.037 0.013  -0.059 112 TYR HHH CE2 
10089 C CZ  . TYR H 112 ? 0.611 0.466 0.495 -0.042 0.009  -0.055 112 TYR HHH CZ  
10090 O OH  . TYR H 112 ? 0.610 0.462 0.481 -0.051 -0.001 -0.052 112 TYR HHH OH  
10091 N N   . GLU H 113 ? 0.586 0.445 0.544 -0.003 0.060  -0.045 113 GLU HHH N   
10092 C CA  . GLU H 113 ? 0.621 0.481 0.598 0.005  0.064  -0.034 113 GLU HHH CA  
10093 C C   . GLU H 113 ? 0.599 0.474 0.578 0.003  0.050  -0.028 113 GLU HHH C   
10094 O O   . GLU H 113 ? 0.611 0.500 0.607 0.007  0.046  -0.015 113 GLU HHH O   
10095 C CB  . GLU H 113 ? 0.677 0.511 0.649 0.005  0.078  -0.039 113 GLU HHH CB  
10096 C CG  . GLU H 113 ? 0.730 0.562 0.723 0.015  0.082  -0.026 113 GLU HHH CG  
10097 C CD  . GLU H 113 ? 0.789 0.586 0.775 0.017  0.098  -0.029 113 GLU HHH CD  
10098 O OE1 . GLU H 113 ? 0.843 0.617 0.806 0.008  0.109  -0.045 113 GLU HHH OE1 
10099 O OE2 . GLU H 113 ? 0.839 0.630 0.841 0.025  0.099  -0.016 113 GLU HHH OE2 
10100 N N   . PHE H 114 ? 0.597 0.472 0.559 -0.003 0.042  -0.037 114 PHE HHH N   
10101 C CA  . PHE H 114 ? 0.582 0.471 0.543 -0.006 0.032  -0.035 114 PHE HHH CA  
10102 C C   . PHE H 114 ? 0.586 0.487 0.540 -0.007 0.021  -0.039 114 PHE HHH C   
10103 O O   . PHE H 114 ? 0.564 0.460 0.509 -0.007 0.019  -0.047 114 PHE HHH O   
10104 C CB  . PHE H 114 ? 0.581 0.464 0.529 -0.013 0.033  -0.041 114 PHE HHH CB  
10105 C CG  . PHE H 114 ? 0.577 0.440 0.526 -0.014 0.044  -0.038 114 PHE HHH CG  
10106 C CD1 . PHE H 114 ? 0.572 0.434 0.535 -0.010 0.045  -0.025 114 PHE HHH CD1 
10107 C CD2 . PHE H 114 ? 0.591 0.432 0.524 -0.020 0.054  -0.047 114 PHE HHH CD2 
10108 C CE1 . PHE H 114 ? 0.606 0.442 0.570 -0.008 0.056  -0.021 114 PHE HHH CE1 
10109 C CE2 . PHE H 114 ? 0.607 0.421 0.537 -0.021 0.067  -0.046 114 PHE HHH CE2 
10110 C CZ  . PHE H 114 ? 0.627 0.435 0.573 -0.014 0.068  -0.033 114 PHE HHH CZ  
10111 N N   . TRP H 115 ? 0.583 0.497 0.541 -0.008 0.015  -0.034 115 TRP HHH N   
10112 C CA  . TRP H 115 ? 0.565 0.485 0.514 -0.010 0.007  -0.039 115 TRP HHH CA  
10113 C C   . TRP H 115 ? 0.557 0.490 0.501 -0.014 0.004  -0.042 115 TRP HHH C   
10114 O O   . TRP H 115 ? 0.548 0.491 0.499 -0.020 0.003  -0.033 115 TRP HHH O   
10115 C CB  . TRP H 115 ? 0.566 0.489 0.519 -0.013 0.004  -0.030 115 TRP HHH CB  
10116 C CG  . TRP H 115 ? 0.595 0.509 0.549 -0.011 0.007  -0.029 115 TRP HHH CG  
10117 C CD1 . TRP H 115 ? 0.599 0.511 0.566 -0.007 0.016  -0.024 115 TRP HHH CD1 
10118 C CD2 . TRP H 115 ? 0.603 0.506 0.545 -0.012 0.002  -0.035 115 TRP HHH CD2 
10119 N NE1 . TRP H 115 ? 0.610 0.516 0.573 -0.008 0.018  -0.027 115 TRP HHH NE1 
10120 C CE2 . TRP H 115 ? 0.589 0.489 0.535 -0.012 0.008  -0.033 115 TRP HHH CE2 
10121 C CE3 . TRP H 115 ? 0.611 0.505 0.537 -0.014 -0.005 -0.043 115 TRP HHH CE3 
10122 C CZ2 . TRP H 115 ? 0.603 0.493 0.538 -0.016 0.004  -0.036 115 TRP HHH CZ2 
10123 C CZ3 . TRP H 115 ? 0.625 0.503 0.540 -0.016 -0.009 -0.045 115 TRP HHH CZ3 
10124 C CH2 . TRP H 115 ? 0.618 0.496 0.537 -0.018 -0.006 -0.040 115 TRP HHH CH2 
10125 N N   . GLY H 116 ? 0.560 0.493 0.495 -0.012 0.002  -0.054 116 GLY HHH N   
10126 C CA  . GLY H 116 ? 0.570 0.515 0.497 -0.016 0.001  -0.060 116 GLY HHH CA  
10127 C C   . GLY H 116 ? 0.601 0.545 0.520 -0.024 -0.003 -0.057 116 GLY HHH C   
10128 O O   . GLY H 116 ? 0.585 0.520 0.505 -0.026 -0.005 -0.049 116 GLY HHH O   
10129 N N   . GLN H 117 ? 0.609 0.563 0.517 -0.033 -0.002 -0.062 117 GLN HHH N   
10130 C CA  . GLN H 117 ? 0.605 0.558 0.498 -0.047 -0.006 -0.061 117 GLN HHH CA  
10131 C C   . GLN H 117 ? 0.630 0.559 0.506 -0.043 -0.004 -0.076 117 GLN HHH C   
10132 O O   . GLN H 117 ? 0.669 0.589 0.528 -0.056 -0.007 -0.074 117 GLN HHH O   
10133 C CB  . GLN H 117 ? 0.601 0.575 0.485 -0.062 -0.005 -0.061 117 GLN HHH CB  
10134 C CG  . GLN H 117 ? 0.596 0.590 0.496 -0.067 -0.008 -0.044 117 GLN HHH CG  
10135 C CD  . GLN H 117 ? 0.612 0.607 0.526 -0.070 -0.014 -0.022 117 GLN HHH CD  
10136 O OE1 . GLN H 117 ? 0.614 0.609 0.547 -0.061 -0.014 -0.012 117 GLN HHH OE1 
10137 N NE2 . GLN H 117 ? 0.617 0.615 0.523 -0.082 -0.020 -0.016 117 GLN HHH NE2 
10138 N N   . GLY H 118 ? 0.646 0.564 0.525 -0.026 0.001  -0.088 118 GLY HHH N   
10139 C CA  . GLY H 118 ? 0.676 0.565 0.541 -0.018 0.002  -0.100 118 GLY HHH CA  
10140 C C   . GLY H 118 ? 0.716 0.603 0.568 -0.015 0.011  -0.118 118 GLY HHH C   
10141 O O   . GLY H 118 ? 0.689 0.596 0.536 -0.027 0.015  -0.120 118 GLY HHH O   
10142 N N   . THR H 119 ? 0.756 0.618 0.604 0.001  0.016  -0.130 119 THR HHH N   
10143 C CA  . THR H 119 ? 0.777 0.630 0.615 0.009  0.028  -0.150 119 THR HHH CA  
10144 C C   . THR H 119 ? 0.821 0.624 0.638 0.014  0.029  -0.159 119 THR HHH C   
10145 O O   . THR H 119 ? 0.798 0.582 0.621 0.022  0.020  -0.150 119 THR HHH O   
10146 C CB  . THR H 119 ? 0.780 0.659 0.644 0.030  0.034  -0.154 119 THR HHH CB  
10147 O OG1 . THR H 119 ? 0.833 0.714 0.691 0.038  0.049  -0.173 119 THR HHH OG1 
10148 C CG2 . THR H 119 ? 0.777 0.643 0.659 0.052  0.029  -0.148 119 THR HHH CG2 
10149 N N   . GLN H 120 ? 0.843 0.623 0.631 0.006  0.039  -0.176 120 GLN HHH N   
10150 C CA  . GLN H 120 ? 0.890 0.614 0.650 0.007  0.042  -0.187 120 GLN HHH CA  
10151 C C   . GLN H 120 ? 0.891 0.596 0.669 0.041  0.050  -0.195 120 GLN HHH C   
10152 O O   . GLN H 120 ? 0.867 0.595 0.663 0.058  0.062  -0.205 120 GLN HHH O   
10153 C CB  . GLN H 120 ? 0.952 0.657 0.673 -0.016 0.053  -0.204 120 GLN HHH CB  
10154 C CG  . GLN H 120 ? 1.026 0.667 0.708 -0.023 0.056  -0.216 120 GLN HHH CG  
10155 C CD  . GLN H 120 ? 1.050 0.676 0.720 -0.042 0.038  -0.197 120 GLN HHH CD  
10156 O OE1 . GLN H 120 ? 1.054 0.712 0.724 -0.066 0.027  -0.181 120 GLN HHH OE1 
10157 N NE2 . GLN H 120 ? 1.113 0.692 0.775 -0.031 0.034  -0.197 120 GLN HHH NE2 
10158 N N   . VAL H 121 ? 0.923 0.590 0.699 0.049  0.041  -0.188 121 VAL HHH N   
10159 C CA  . VAL H 121 ? 0.967 0.596 0.749 0.079  0.047  -0.195 121 VAL HHH CA  
10160 C C   . VAL H 121 ? 1.019 0.580 0.758 0.068  0.050  -0.207 121 VAL HHH C   
10161 O O   . VAL H 121 ? 1.005 0.548 0.722 0.044  0.037  -0.196 121 VAL HHH O   
10162 C CB  . VAL H 121 ? 0.958 0.597 0.771 0.096  0.032  -0.174 121 VAL HHH CB  
10163 C CG1 . VAL H 121 ? 0.991 0.591 0.813 0.125  0.035  -0.177 121 VAL HHH CG1 
10164 C CG2 . VAL H 121 ? 0.898 0.601 0.748 0.102  0.030  -0.164 121 VAL HHH CG2 
10165 N N   . THR H 122 ? 1.075 0.599 0.800 0.083  0.069  -0.229 122 THR HHH N   
10166 C CA  . THR H 122 ? 1.174 0.621 0.852 0.073  0.075  -0.243 122 THR HHH CA  
10167 C C   . THR H 122 ? 1.239 0.640 0.932 0.111  0.082  -0.247 122 THR HHH C   
10168 O O   . THR H 122 ? 1.267 0.687 0.989 0.142  0.099  -0.258 122 THR HHH O   
10169 C CB  . THR H 122 ? 1.210 0.644 0.847 0.049  0.092  -0.268 122 THR HHH CB  
10170 O OG1 . THR H 122 ? 1.173 0.657 0.805 0.015  0.081  -0.256 122 THR HHH OG1 
10171 C CG2 . THR H 122 ? 1.279 0.632 0.861 0.032  0.098  -0.283 122 THR HHH CG2 
10172 N N   . VAL H 123 ? 1.292 0.639 0.968 0.110  0.069  -0.237 123 VAL HHH N   
10173 C CA  . VAL H 123 ? 1.361 0.653 1.047 0.145  0.073  -0.237 123 VAL HHH CA  
10174 C C   . VAL H 123 ? 1.467 0.668 1.094 0.131  0.084  -0.258 123 VAL HHH C   
10175 O O   . VAL H 123 ? 1.469 0.638 1.057 0.098  0.069  -0.250 123 VAL HHH O   
10176 C CB  . VAL H 123 ? 1.333 0.633 1.043 0.151  0.048  -0.206 123 VAL HHH CB  
10177 C CG1 . VAL H 123 ? 1.385 0.644 1.118 0.191  0.049  -0.200 123 VAL HHH CG1 
10178 C CG2 . VAL H 123 ? 1.232 0.618 0.986 0.151  0.036  -0.187 123 VAL HHH CG2 
10179 N N   . SER H 124 ? 1.562 0.726 1.180 0.152  0.111  -0.284 124 SER HHH N   
10180 C CA  . SER H 124 ? 1.697 0.765 1.256 0.141  0.126  -0.308 124 SER HHH CA  
10181 C C   . SER H 124 ? 1.836 0.831 1.399 0.169  0.120  -0.298 124 SER HHH C   
10182 O O   . SER H 124 ? 1.784 0.812 1.402 0.205  0.110  -0.276 124 SER HHH O   
10183 C CB  . SER H 124 ? 1.724 0.781 1.271 0.151  0.160  -0.343 124 SER HHH CB  
10184 O OG  . SER H 124 ? 1.704 0.789 1.309 0.203  0.174  -0.344 124 SER HHH OG  
10207 N N   . THR I 4   ? 1.446 1.752 1.439 -0.023 -0.121 0.105  333 THR III N   
10208 C CA  . THR I 4   ? 1.297 1.645 1.294 -0.029 -0.070 0.148  333 THR III CA  
10209 C C   . THR I 4   ? 1.195 1.555 1.172 -0.023 -0.028 0.150  333 THR III C   
10210 O O   . THR I 4   ? 1.134 1.521 1.148 -0.037 0.007  0.182  333 THR III O   
10211 C CB  . THR I 4   ? 1.312 1.689 1.256 -0.004 -0.072 0.179  333 THR III CB  
10212 O OG1 . THR I 4   ? 1.403 1.766 1.242 0.040  -0.096 0.153  333 THR III OG1 
10213 C CG2 . THR I 4   ? 1.271 1.648 1.264 -0.021 -0.101 0.193  333 THR III CG2 
10214 N N   . ASN I 5   ? 1.128 1.465 1.062 -0.005 -0.038 0.115  334 ASN III N   
10215 C CA  . ASN I 5   ? 1.047 1.392 0.961 0.003  -0.002 0.114  334 ASN III CA  
10216 C C   . ASN I 5   ? 0.938 1.275 0.930 -0.033 0.016  0.115  334 ASN III C   
10217 O O   . ASN I 5   ? 0.893 1.204 0.933 -0.051 -0.006 0.097  334 ASN III O   
10218 C CB  . ASN I 5   ? 1.107 1.423 0.952 0.036  -0.025 0.072  334 ASN III CB  
10219 C CG  . ASN I 5   ? 1.112 1.382 0.997 0.023  -0.077 0.032  334 ASN III CG  
10220 O OD1 . ASN I 5   ? 1.099 1.358 1.015 0.012  -0.112 0.031  334 ASN III OD1 
10221 N ND2 . ASN I 5   ? 1.121 1.366 1.021 0.022  -0.082 0.005  334 ASN III ND2 
10222 N N   . LEU I 6   ? 0.893 1.251 0.900 -0.038 0.053  0.138  335 LEU III N   
10223 C CA  . LEU I 6   ? 0.797 1.148 0.865 -0.064 0.069  0.140  335 LEU III CA  
10224 C C   . LEU I 6   ? 0.776 1.102 0.837 -0.062 0.068  0.113  335 LEU III C   
10225 O O   . LEU I 6   ? 0.773 1.097 0.786 -0.041 0.067  0.098  335 LEU III O   
10226 C CB  . LEU I 6   ? 0.747 1.123 0.837 -0.067 0.096  0.171  335 LEU III CB  
10227 C CG  . LEU I 6   ? 0.751 1.149 0.870 -0.073 0.094  0.202  335 LEU III CG  
10228 C CD1 . LEU I 6   ? 0.734 1.154 0.898 -0.077 0.111  0.233  335 LEU III CD1 
10229 C CD2 . LEU I 6   ? 0.743 1.126 0.905 -0.091 0.077  0.194  335 LEU III CD2 
10230 N N   . CYS I 7   ? 0.756 1.067 0.865 -0.081 0.069  0.108  336 CYS III N   
10231 C CA  . CYS I 7   ? 0.759 1.050 0.879 -0.082 0.070  0.091  336 CYS III CA  
10232 C C   . CYS I 7   ? 0.770 1.069 0.866 -0.075 0.095  0.096  336 CYS III C   
10233 O O   . CYS I 7   ? 0.739 1.052 0.845 -0.079 0.111  0.114  336 CYS III O   
10234 C CB  . CYS I 7   ? 0.731 1.013 0.909 -0.098 0.076  0.100  336 CYS III CB  
10235 S SG  . CYS I 7   ? 0.766 1.039 1.003 -0.107 0.046  0.102  336 CYS III SG  
10236 N N   . PRO I 8   ? 0.834 1.121 0.905 -0.062 0.093  0.078  337 PRO III N   
10237 C CA  . PRO I 8   ? 0.825 1.125 0.878 -0.052 0.115  0.085  337 PRO III CA  
10238 C C   . PRO I 8   ? 0.771 1.060 0.856 -0.066 0.127  0.090  337 PRO III C   
10239 O O   . PRO I 8   ? 0.779 1.054 0.864 -0.062 0.127  0.078  337 PRO III O   
10240 C CB  . PRO I 8   ? 0.897 1.185 0.909 -0.028 0.104  0.059  337 PRO III CB  
10241 C CG  . PRO I 8   ? 0.917 1.173 0.956 -0.037 0.071  0.035  337 PRO III CG  
10242 C CD  . PRO I 8   ? 0.886 1.147 0.958 -0.056 0.064  0.050  337 PRO III CD  
10243 N N   . PHE I 9   ? 0.729 1.023 0.837 -0.077 0.133  0.105  338 PHE III N   
10244 C CA  . PHE I 9   ? 0.700 0.981 0.821 -0.080 0.141  0.109  338 PHE III CA  
10245 C C   . PHE I 9   ? 0.696 0.980 0.813 -0.074 0.147  0.112  338 PHE III C   
10246 O O   . PHE I 9   ? 0.727 0.997 0.845 -0.073 0.149  0.108  338 PHE III O   
10247 C CB  . PHE I 9   ? 0.685 0.967 0.821 -0.083 0.140  0.118  338 PHE III CB  
10248 C CG  . PHE I 9   ? 0.678 0.957 0.829 -0.087 0.140  0.120  338 PHE III CG  
10249 C CD1 . PHE I 9   ? 0.680 0.950 0.844 -0.086 0.146  0.120  338 PHE III CD1 
10250 C CD2 . PHE I 9   ? 0.672 0.959 0.838 -0.090 0.136  0.126  338 PHE III CD2 
10251 C CE1 . PHE I 9   ? 0.658 0.931 0.856 -0.088 0.150  0.132  338 PHE III CE1 
10252 C CE2 . PHE I 9   ? 0.674 0.961 0.865 -0.091 0.139  0.132  338 PHE III CE2 
10253 C CZ  . PHE I 9   ? 0.659 0.940 0.869 -0.090 0.148  0.137  338 PHE III CZ  
10254 N N   . GLY I 10  ? 0.687 0.993 0.806 -0.069 0.151  0.124  339 GLY III N   
10255 C CA  . GLY I 10  ? 0.669 0.986 0.800 -0.061 0.160  0.135  339 GLY III CA  
10256 C C   . GLY I 10  ? 0.673 0.978 0.786 -0.053 0.165  0.118  339 GLY III C   
10257 O O   . GLY I 10  ? 0.645 0.942 0.775 -0.053 0.165  0.121  339 GLY III O   
10258 N N   . GLU I 11  ? 0.711 1.010 0.794 -0.045 0.162  0.100  340 GLU III N   
10259 C CA  . GLU I 11  ? 0.747 1.030 0.820 -0.034 0.160  0.079  340 GLU III CA  
10260 C C   . GLU I 11  ? 0.735 0.995 0.833 -0.048 0.153  0.075  340 GLU III C   
10261 O O   . GLU I 11  ? 0.766 1.015 0.870 -0.043 0.154  0.067  340 GLU III O   
10262 C CB  . GLU I 11  ? 0.801 1.073 0.844 -0.021 0.144  0.053  340 GLU III CB  
10263 C CG  . GLU I 11  ? 0.890 1.186 0.889 0.004  0.152  0.056  340 GLU III CG  
10264 C CD  . GLU I 11  ? 0.987 1.264 0.942 0.026  0.126  0.022  340 GLU III CD  
10265 O OE1 . GLU I 11  ? 1.023 1.266 0.999 0.019  0.098  -0.004 340 GLU III OE1 
10266 O OE2 . GLU I 11  ? 1.040 1.336 0.944 0.053  0.130  0.025  340 GLU III OE2 
10267 N N   . VAL I 12  ? 0.697 0.950 0.807 -0.061 0.150  0.084  341 VAL III N   
10268 C CA  . VAL I 12  ? 0.681 0.917 0.806 -0.067 0.151  0.090  341 VAL III CA  
10269 C C   . VAL I 12  ? 0.672 0.905 0.792 -0.064 0.154  0.100  341 VAL III C   
10270 O O   . VAL I 12  ? 0.681 0.904 0.805 -0.060 0.154  0.101  341 VAL III O   
10271 C CB  . VAL I 12  ? 0.687 0.922 0.826 -0.073 0.151  0.098  341 VAL III CB  
10272 C CG1 . VAL I 12  ? 0.724 0.951 0.877 -0.070 0.160  0.115  341 VAL III CG1 
10273 C CG2 . VAL I 12  ? 0.691 0.925 0.848 -0.077 0.137  0.088  341 VAL III CG2 
10274 N N   . PHE I 13  ? 0.645 0.884 0.761 -0.064 0.150  0.106  342 PHE III N   
10275 C CA  . PHE I 13  ? 0.648 0.875 0.761 -0.057 0.139  0.109  342 PHE III CA  
10276 C C   . PHE I 13  ? 0.671 0.901 0.807 -0.056 0.132  0.113  342 PHE III C   
10277 O O   . PHE I 13  ? 0.695 0.907 0.831 -0.050 0.118  0.112  342 PHE III O   
10278 C CB  . PHE I 13  ? 0.628 0.855 0.741 -0.055 0.130  0.110  342 PHE III CB  
10279 C CG  . PHE I 13  ? 0.628 0.849 0.719 -0.048 0.138  0.109  342 PHE III CG  
10280 C CD1 . PHE I 13  ? 0.610 0.845 0.711 -0.057 0.150  0.113  342 PHE III CD1 
10281 C CD2 . PHE I 13  ? 0.651 0.852 0.710 -0.028 0.133  0.106  342 PHE III CD2 
10282 C CE1 . PHE I 13  ? 0.621 0.855 0.718 -0.050 0.161  0.120  342 PHE III CE1 
10283 C CE2 . PHE I 13  ? 0.670 0.872 0.710 -0.014 0.149  0.112  342 PHE III CE2 
10284 C CZ  . PHE I 13  ? 0.655 0.876 0.723 -0.027 0.165  0.122  342 PHE III CZ  
10285 N N   . ASN I 14  ? 0.687 0.940 0.841 -0.059 0.143  0.119  343 ASN III N   
10286 C CA  . ASN I 14  ? 0.700 0.969 0.891 -0.055 0.145  0.133  343 ASN III CA  
10287 C C   . ASN I 14  ? 0.681 0.959 0.863 -0.046 0.163  0.128  343 ASN III C   
10288 O O   . ASN I 14  ? 0.677 0.977 0.885 -0.037 0.175  0.143  343 ASN III O   
10289 C CB  . ASN I 14  ? 0.705 1.002 0.930 -0.056 0.148  0.156  343 ASN III CB  
10290 C CG  . ASN I 14  ? 0.755 1.038 1.011 -0.062 0.120  0.161  343 ASN III CG  
10291 O OD1 . ASN I 14  ? 0.751 1.005 1.009 -0.060 0.096  0.150  343 ASN III OD1 
10292 N ND2 . ASN I 14  ? 0.909 1.211 1.188 -0.066 0.120  0.177  343 ASN III ND2 
10293 N N   . ALA I 15  ? 0.686 0.946 0.840 -0.046 0.163  0.108  344 ALA III N   
10294 C CA  . ALA I 15  ? 0.692 0.949 0.844 -0.036 0.170  0.096  344 ALA III CA  
10295 C C   . ALA I 15  ? 0.682 0.940 0.867 -0.032 0.170  0.108  344 ALA III C   
10296 O O   . ALA I 15  ? 0.652 0.895 0.851 -0.040 0.154  0.116  344 ALA III O   
10297 C CB  . ALA I 15  ? 0.677 0.909 0.821 -0.041 0.160  0.081  344 ALA III CB  
10298 N N   . THR I 16  ? 0.694 0.967 0.891 -0.016 0.185  0.109  345 THR III N   
10299 C CA  . THR I 16  ? 0.701 0.979 0.945 -0.013 0.186  0.125  345 THR III CA  
10300 C C   . THR I 16  ? 0.718 0.965 0.962 -0.019 0.170  0.112  345 THR III C   
10301 O O   . THR I 16  ? 0.771 1.008 1.047 -0.023 0.157  0.124  345 THR III O   
10302 C CB  . THR I 16  ? 0.720 1.031 0.976 0.012  0.214  0.135  345 THR III CB  
10303 O OG1 . THR I 16  ? 0.771 1.073 0.976 0.029  0.219  0.104  345 THR III OG1 
10304 C CG2 . THR I 16  ? 0.707 1.057 0.983 0.019  0.232  0.167  345 THR III CG2 
10305 N N   . ARG I 17  ? 0.687 0.915 0.903 -0.020 0.167  0.091  346 ARG III N   
10306 C CA  . ARG I 17  ? 0.671 0.873 0.898 -0.025 0.154  0.087  346 ARG III CA  
10307 C C   . ARG I 17  ? 0.650 0.838 0.859 -0.037 0.146  0.090  346 ARG III C   
10308 O O   . ARG I 17  ? 0.639 0.832 0.831 -0.039 0.149  0.083  346 ARG III O   
10309 C CB  . ARG I 17  ? 0.698 0.893 0.935 -0.012 0.155  0.065  346 ARG III CB  
10310 C CG  . ARG I 17  ? 0.721 0.905 0.994 -0.008 0.150  0.069  346 ARG III CG  
10311 C CD  . ARG I 17  ? 0.758 0.923 1.046 0.001  0.141  0.044  346 ARG III CD  
10312 N NE  . ARG I 17  ? 0.806 0.983 1.076 0.029  0.152  0.019  346 ARG III NE  
10313 C CZ  . ARG I 17  ? 0.821 1.009 1.105 0.051  0.166  0.018  346 ARG III CZ  
10314 N NH1 . ARG I 17  ? 0.810 0.998 1.138 0.042  0.166  0.039  346 ARG III NH1 
10315 N NH2 . ARG I 17  ? 0.847 1.048 1.101 0.086  0.180  -0.003 346 ARG III NH2 
10316 N N   . PHE I 18  ? 0.602 1.077 0.675 0.004  0.118  0.083  347 PHE III N   
10317 C CA  . PHE I 18  ? 0.599 1.021 0.651 0.005  0.108  0.071  347 PHE III CA  
10318 C C   . PHE I 18  ? 0.590 1.007 0.634 0.031  0.110  0.061  347 PHE III C   
10319 O O   . PHE I 18  ? 0.596 1.050 0.654 0.042  0.111  0.064  347 PHE III O   
10320 C CB  . PHE I 18  ? 0.613 1.023 0.672 -0.015 0.091  0.071  347 PHE III CB  
10321 C CG  . PHE I 18  ? 0.632 1.012 0.685 -0.036 0.087  0.074  347 PHE III CG  
10322 C CD1 . PHE I 18  ? 0.626 1.027 0.693 -0.051 0.094  0.087  347 PHE III CD1 
10323 C CD2 . PHE I 18  ? 0.647 0.977 0.677 -0.037 0.079  0.066  347 PHE III CD2 
10324 C CE1 . PHE I 18  ? 0.633 1.004 0.692 -0.069 0.091  0.092  347 PHE III CE1 
10325 C CE2 . PHE I 18  ? 0.651 0.953 0.674 -0.054 0.076  0.069  347 PHE III CE2 
10326 C CZ  . PHE I 18  ? 0.645 0.966 0.682 -0.070 0.081  0.082  347 PHE III CZ  
10327 N N   . ALA I 19  ? 0.580 0.952 0.605 0.040  0.111  0.053  348 ALA III N   
10328 C CA  . ALA I 19  ? 0.562 0.920 0.581 0.063  0.115  0.046  348 ALA III CA  
10329 C C   . ALA I 19  ? 0.562 0.919 0.583 0.068  0.107  0.047  348 ALA III C   
10330 O O   . ALA I 19  ? 0.546 0.894 0.564 0.053  0.097  0.049  348 ALA III O   
10331 C CB  . ALA I 19  ? 0.572 0.885 0.580 0.068  0.117  0.040  348 ALA III CB  
10332 N N   . SER I 20  ? 0.568 0.930 0.589 0.090  0.112  0.046  349 SER III N   
10333 C CA  . SER I 20  ? 0.586 0.931 0.599 0.103  0.109  0.047  349 SER III CA  
10334 C C   . SER I 20  ? 0.601 0.896 0.602 0.102  0.112  0.048  349 SER III C   
10335 O O   . SER I 20  ? 0.582 0.856 0.587 0.100  0.118  0.045  349 SER III O   
10336 C CB  . SER I 20  ? 0.593 0.950 0.608 0.130  0.116  0.049  349 SER III CB  
10337 O OG  . SER I 20  ? 0.599 1.007 0.627 0.132  0.111  0.051  349 SER III OG  
10338 N N   . VAL I 21  ? 0.609 0.887 0.598 0.104  0.107  0.051  350 VAL III N   
10339 C CA  . VAL I 21  ? 0.629 0.864 0.609 0.105  0.112  0.054  350 VAL III CA  
10340 C C   . VAL I 21  ? 0.643 0.856 0.633 0.121  0.125  0.059  350 VAL III C   
10341 O O   . VAL I 21  ? 0.646 0.832 0.644 0.114  0.129  0.060  350 VAL III O   
10342 C CB  . VAL I 21  ? 0.662 0.886 0.620 0.114  0.106  0.057  350 VAL III CB  
10343 C CG1 . VAL I 21  ? 0.680 0.913 0.631 0.140  0.110  0.062  350 VAL III CG1 
10344 C CG2 . VAL I 21  ? 0.658 0.842 0.606 0.114  0.112  0.063  350 VAL III CG2 
10345 N N   . TYR I 22  ? 0.660 0.883 0.655 0.141  0.131  0.061  351 TYR III N   
10346 C CA  . TYR I 22  ? 0.688 0.883 0.696 0.155  0.143  0.067  351 TYR III CA  
10347 C C   . TYR I 22  ? 0.660 0.847 0.684 0.144  0.141  0.057  351 TYR III C   
10348 O O   . TYR I 22  ? 0.667 0.823 0.707 0.146  0.145  0.060  351 TYR III O   
10349 C CB  . TYR I 22  ? 0.689 0.895 0.696 0.180  0.149  0.072  351 TYR III CB  
10350 C CG  . TYR I 22  ? 0.684 0.913 0.698 0.184  0.147  0.063  351 TYR III CG  
10351 C CD1 . TYR I 22  ? 0.666 0.939 0.675 0.181  0.139  0.057  351 TYR III CD1 
10352 C CD2 . TYR I 22  ? 0.691 0.897 0.717 0.193  0.153  0.060  351 TYR III CD2 
10353 C CE1 . TYR I 22  ? 0.652 0.948 0.666 0.188  0.141  0.051  351 TYR III CE1 
10354 C CE2 . TYR I 22  ? 0.687 0.911 0.713 0.201  0.151  0.049  351 TYR III CE2 
10355 C CZ  . TYR I 22  ? 0.672 0.943 0.691 0.200  0.147  0.046  351 TYR III CZ  
10356 O OH  . TYR I 22  ? 0.687 0.978 0.705 0.212  0.149  0.039  351 TYR III OH  
10357 N N   . ALA I 23  ? 0.633 0.847 0.651 0.135  0.134  0.047  352 ALA III N   
10358 C CA  . ALA I 23  ? 0.640 0.851 0.662 0.129  0.131  0.036  352 ALA III CA  
10359 C C   . ALA I 23  ? 0.624 0.839 0.639 0.107  0.125  0.034  352 ALA III C   
10360 O O   . ALA I 23  ? 0.627 0.863 0.637 0.102  0.123  0.028  352 ALA III O   
10361 C CB  . ALA I 23  ? 0.654 0.894 0.672 0.143  0.133  0.030  352 ALA III CB  
10362 N N   . TRP I 24  ? 0.623 0.820 0.639 0.096  0.123  0.040  353 TRP III N   
10363 C CA  . TRP I 24  ? 0.617 0.815 0.626 0.076  0.118  0.040  353 TRP III CA  
10364 C C   . TRP I 24  ? 0.613 0.805 0.621 0.070  0.114  0.032  353 TRP III C   
10365 O O   . TRP I 24  ? 0.607 0.779 0.624 0.078  0.113  0.026  353 TRP III O   
10366 C CB  . TRP I 24  ? 0.613 0.784 0.619 0.072  0.118  0.047  353 TRP III CB  
10367 C CG  . TRP I 24  ? 0.609 0.750 0.632 0.081  0.124  0.052  353 TRP III CG  
10368 C CD1 . TRP I 24  ? 0.626 0.756 0.657 0.098  0.134  0.062  353 TRP III CD1 
10369 C CD2 . TRP I 24  ? 0.602 0.723 0.640 0.073  0.122  0.051  353 TRP III CD2 
10370 N NE1 . TRP I 24  ? 0.624 0.728 0.679 0.099  0.138  0.069  353 TRP III NE1 
10371 C CE2 . TRP I 24  ? 0.618 0.717 0.679 0.083  0.130  0.061  353 TRP III CE2 
10372 C CE3 . TRP I 24  ? 0.581 0.700 0.616 0.059  0.113  0.045  353 TRP III CE3 
10373 C CZ2 . TRP I 24  ? 0.618 0.697 0.706 0.078  0.127  0.064  353 TRP III CZ2 
10374 C CZ3 . TRP I 24  ? 0.583 0.680 0.638 0.056  0.110  0.045  353 TRP III CZ3 
10375 C CH2 . TRP I 24  ? 0.599 0.678 0.684 0.064  0.116  0.054  353 TRP III CH2 
10376 N N   . ASN I 25  ? 0.615 0.826 0.614 0.057  0.111  0.032  354 ASN III N   
10377 C CA  . ASN I 25  ? 0.611 0.822 0.601 0.054  0.108  0.026  354 ASN III CA  
10378 C C   . ASN I 25  ? 0.605 0.789 0.594 0.041  0.102  0.027  354 ASN III C   
10379 O O   . ASN I 25  ? 0.604 0.783 0.594 0.030  0.102  0.035  354 ASN III O   
10380 C CB  . ASN I 25  ? 0.626 0.875 0.609 0.048  0.112  0.031  354 ASN III CB  
10381 C CG  . ASN I 25  ? 0.648 0.902 0.617 0.049  0.112  0.028  354 ASN III CG  
10382 O OD1 . ASN I 25  ? 0.661 0.908 0.624 0.036  0.109  0.033  354 ASN III OD1 
10383 N ND2 . ASN I 25  ? 0.657 0.919 0.617 0.068  0.114  0.019  354 ASN III ND2 
10384 N N   . ARG I 26  ? 0.628 0.796 0.616 0.046  0.096  0.019  355 ARG III N   
10385 C CA  . ARG I 26  ? 0.639 0.786 0.627 0.037  0.089  0.019  355 ARG III CA  
10386 C C   . ARG I 26  ? 0.637 0.796 0.603 0.036  0.086  0.015  355 ARG III C   
10387 O O   . ARG I 26  ? 0.619 0.781 0.576 0.050  0.082  0.004  355 ARG III O   
10388 C CB  . ARG I 26  ? 0.658 0.780 0.662 0.044  0.079  0.009  355 ARG III CB  
10389 C CG  . ARG I 26  ? 0.658 0.759 0.690 0.041  0.080  0.016  355 ARG III CG  
10390 C CD  . ARG I 26  ? 0.653 0.737 0.698 0.034  0.071  0.018  355 ARG III CD  
10391 N NE  . ARG I 26  ? 0.663 0.741 0.720 0.030  0.082  0.034  355 ARG III NE  
10392 C CZ  . ARG I 26  ? 0.655 0.719 0.743 0.033  0.086  0.043  355 ARG III CZ  
10393 N NH1 . ARG I 26  ? 0.675 0.727 0.795 0.034  0.076  0.038  355 ARG III NH1 
10394 N NH2 . ARG I 26  ? 0.673 0.733 0.761 0.035  0.098  0.057  355 ARG III NH2 
10395 N N   . LYS I 27  ? 0.659 0.818 0.615 0.024  0.086  0.024  356 LYS III N   
10396 C CA  . LYS I 27  ? 0.701 0.864 0.636 0.026  0.082  0.023  356 LYS III CA  
10397 C C   . LYS I 27  ? 0.693 0.830 0.632 0.021  0.072  0.022  356 LYS III C   
10398 O O   . LYS I 27  ? 0.654 0.778 0.605 0.010  0.074  0.031  356 LYS III O   
10399 C CB  . LYS I 27  ? 0.740 0.928 0.663 0.016  0.093  0.037  356 LYS III CB  
10400 C CG  . LYS I 27  ? 0.792 1.012 0.721 0.019  0.102  0.040  356 LYS III CG  
10401 C CD  . LYS I 27  ? 0.837 1.088 0.764 0.010  0.113  0.057  356 LYS III CD  
10402 C CE  . LYS I 27  ? 0.810 1.098 0.751 0.013  0.121  0.061  356 LYS III CE  
10403 N NZ  . LYS I 27  ? 0.799 1.085 0.761 0.002  0.117  0.061  356 LYS III NZ  
10404 N N   . ARG I 28  ? 0.730 0.858 0.659 0.031  0.060  0.011  357 ARG III N   
10405 C CA  . ARG I 28  ? 0.750 0.859 0.683 0.028  0.048  0.011  357 ARG III CA  
10406 C C   . ARG I 28  ? 0.783 0.898 0.689 0.023  0.053  0.024  357 ARG III C   
10407 O O   . ARG I 28  ? 0.858 0.991 0.738 0.030  0.059  0.026  357 ARG III O   
10408 C CB  . ARG I 28  ? 0.789 0.886 0.721 0.042  0.029  -0.008 357 ARG III CB  
10409 C CG  . ARG I 28  ? 0.829 0.910 0.776 0.039  0.013  -0.009 357 ARG III CG  
10410 C CD  . ARG I 28  ? 0.880 0.945 0.847 0.047  -0.009 -0.028 357 ARG III CD  
10411 N NE  . ARG I 28  ? 0.941 0.999 0.915 0.044  -0.023 -0.025 357 ARG III NE  
10412 C CZ  . ARG I 28  ? 1.005 1.061 0.954 0.055  -0.041 -0.036 357 ARG III CZ  
10413 N NH1 . ARG I 28  ? 1.043 1.102 0.953 0.072  -0.047 -0.051 357 ARG III NH1 
10414 N NH2 . ARG I 28  ? 0.986 1.037 0.945 0.053  -0.053 -0.031 357 ARG III NH2 
10415 N N   . ILE I 29  ? 0.775 0.876 0.688 0.013  0.052  0.034  358 ILE III N   
10416 C CA  . ILE I 29  ? 0.767 0.867 0.657 0.009  0.055  0.047  358 ILE III CA  
10417 C C   . ILE I 29  ? 0.792 0.876 0.681 0.015  0.040  0.042  358 ILE III C   
10418 O O   . ILE I 29  ? 0.770 0.840 0.688 0.011  0.035  0.042  358 ILE III O   
10419 C CB  . ILE I 29  ? 0.752 0.846 0.646 -0.008 0.067  0.062  358 ILE III CB  
10420 C CG1 . ILE I 29  ? 0.741 0.856 0.638 -0.014 0.078  0.065  358 ILE III CG1 
10421 C CG2 . ILE I 29  ? 0.771 0.856 0.645 -0.012 0.069  0.076  358 ILE III CG2 
10422 C CD1 . ILE I 29  ? 0.745 0.851 0.650 -0.030 0.083  0.074  358 ILE III CD1 
10423 N N   . SER I 30  ? 0.831 0.919 0.692 0.027  0.033  0.040  359 SER III N   
10424 C CA  . SER I 30  ? 0.846 0.921 0.704 0.035  0.015  0.035  359 SER III CA  
10425 C C   . SER I 30  ? 0.898 0.978 0.713 0.048  0.014  0.042  359 SER III C   
10426 O O   . SER I 30  ? 0.906 1.001 0.695 0.052  0.028  0.048  359 SER III O   
10427 C CB  . SER I 30  ? 0.843 0.914 0.721 0.045  -0.006 0.014  359 SER III CB  
10428 O OG  . SER I 30  ? 0.879 0.960 0.737 0.056  -0.006 0.001  359 SER III OG  
10429 N N   . ASN I 31  ? 0.947 1.017 0.757 0.054  0.001  0.043  360 ASN III N   
10430 C CA  . ASN I 31  ? 0.971 1.042 0.737 0.071  -0.004 0.049  360 ASN III CA  
10431 C C   . ASN I 31  ? 0.944 1.021 0.686 0.064  0.022  0.073  360 ASN III C   
10432 O O   . ASN I 31  ? 0.995 1.087 0.703 0.078  0.030  0.077  360 ASN III O   
10433 C CB  . ASN I 31  ? 1.018 1.095 0.760 0.094  -0.022 0.026  360 ASN III CB  
10434 C CG  . ASN I 31  ? 1.027 1.094 0.805 0.095  -0.052 0.004  360 ASN III CG  
10435 O OD1 . ASN I 31  ? 1.000 1.066 0.793 0.097  -0.063 -0.016 360 ASN III OD1 
10436 N ND2 . ASN I 31  ? 1.035 1.094 0.830 0.092  -0.064 0.009  360 ASN III ND2 
10437 N N   . CYS I 32  ? 0.888 0.954 0.650 0.045  0.034  0.089  361 CYS III N   
10438 C CA  . CYS I 32  ? 0.884 0.951 0.636 0.032  0.056  0.113  361 CYS III CA  
10439 C C   . CYS I 32  ? 0.850 0.891 0.618 0.017  0.059  0.125  361 CYS III C   
10440 O O   . CYS I 32  ? 0.792 0.821 0.584 0.015  0.048  0.115  361 CYS III O   
10441 C CB  . CYS I 32  ? 0.886 0.973 0.651 0.022  0.070  0.112  361 CYS III CB  
10442 S SG  . CYS I 32  ? 0.879 0.961 0.687 0.008  0.064  0.096  361 CYS III SG  
10443 N N   . VAL I 33  ? 0.868 0.901 0.624 0.008  0.073  0.147  362 VAL III N   
10444 C CA  . VAL I 33  ? 0.877 0.879 0.642 -0.007 0.076  0.160  362 VAL III CA  
10445 C C   . VAL I 33  ? 0.861 0.863 0.650 -0.028 0.084  0.158  362 VAL III C   
10446 O O   . VAL I 33  ? 0.884 0.905 0.674 -0.037 0.095  0.166  362 VAL III O   
10447 C CB  . VAL I 33  ? 0.912 0.901 0.653 -0.007 0.086  0.185  362 VAL III CB  
10448 C CG1 . VAL I 33  ? 0.921 0.872 0.670 -0.021 0.088  0.195  362 VAL III CG1 
10449 C CG2 . VAL I 33  ? 0.930 0.921 0.641 0.017  0.079  0.187  362 VAL III CG2 
10450 N N   . ALA I 34  ? 0.847 0.832 0.655 -0.033 0.078  0.147  363 ALA III N   
10451 C CA  . ALA I 34  ? 0.846 0.827 0.671 -0.048 0.081  0.143  363 ALA III CA  
10452 C C   . ALA I 34  ? 0.886 0.834 0.704 -0.062 0.084  0.158  363 ALA III C   
10453 O O   . ALA I 34  ? 0.919 0.835 0.733 -0.059 0.079  0.157  363 ALA III O   
10454 C CB  . ALA I 34  ? 0.824 0.799 0.666 -0.043 0.075  0.128  363 ALA III CB  
10455 N N   . ASP I 35  ? 0.892 0.849 0.713 -0.077 0.092  0.171  364 ASP III N   
10456 C CA  . ASP I 35  ? 0.932 0.858 0.756 -0.096 0.092  0.183  364 ASP III CA  
10457 C C   . ASP I 35  ? 0.902 0.830 0.746 -0.110 0.087  0.171  364 ASP III C   
10458 O O   . ASP I 35  ? 0.884 0.847 0.746 -0.120 0.091  0.173  364 ASP III O   
10459 C CB  . ASP I 35  ? 0.956 0.888 0.779 -0.106 0.103  0.208  364 ASP III CB  
10460 C CG  . ASP I 35  ? 0.979 0.865 0.802 -0.122 0.100  0.221  364 ASP III CG  
10461 O OD1 . ASP I 35  ? 0.976 0.831 0.800 -0.125 0.089  0.206  364 ASP III OD1 
10462 O OD2 . ASP I 35  ? 1.009 0.890 0.829 -0.127 0.110  0.245  364 ASP III OD2 
10463 N N   . TYR I 36  ? 0.909 0.800 0.748 -0.110 0.077  0.160  365 TYR III N   
10464 C CA  . TYR I 36  ? 0.919 0.808 0.769 -0.118 0.069  0.146  365 TYR III CA  
10465 C C   . TYR I 36  ? 0.952 0.817 0.811 -0.141 0.061  0.153  365 TYR III C   
10466 O O   . TYR I 36  ? 0.947 0.808 0.815 -0.149 0.050  0.140  365 TYR III O   
10467 C CB  . TYR I 36  ? 0.916 0.778 0.751 -0.100 0.063  0.131  365 TYR III CB  
10468 C CG  . TYR I 36  ? 0.899 0.790 0.740 -0.082 0.068  0.123  365 TYR III CG  
10469 C CD1 . TYR I 36  ? 0.893 0.787 0.729 -0.068 0.072  0.128  365 TYR III CD1 
10470 C CD2 . TYR I 36  ? 0.909 0.824 0.762 -0.080 0.068  0.112  365 TYR III CD2 
10471 C CE1 . TYR I 36  ? 0.885 0.803 0.732 -0.054 0.073  0.120  365 TYR III CE1 
10472 C CE2 . TYR I 36  ? 0.877 0.814 0.739 -0.065 0.072  0.106  365 TYR III CE2 
10473 C CZ  . TYR I 36  ? 0.880 0.818 0.741 -0.053 0.074  0.110  365 TYR III CZ  
10474 O OH  . TYR I 36  ? 0.913 0.871 0.790 -0.041 0.075  0.103  365 TYR III OH  
10475 N N   . SER I 37  ? 0.997 0.845 0.856 -0.152 0.065  0.172  366 SER III N   
10476 C CA  . SER I 37  ? 1.050 0.868 0.923 -0.177 0.056  0.180  366 SER III CA  
10477 C C   . SER I 37  ? 1.033 0.893 0.943 -0.197 0.055  0.183  366 SER III C   
10478 O O   . SER I 37  ? 1.083 0.923 1.010 -0.217 0.039  0.178  366 SER III O   
10479 C CB  . SER I 37  ? 1.083 0.873 0.950 -0.183 0.063  0.204  366 SER III CB  
10480 O OG  . SER I 37  ? 1.071 0.899 0.937 -0.175 0.081  0.222  366 SER III OG  
10481 N N   . VAL I 38  ? 0.984 0.901 0.906 -0.191 0.068  0.187  367 VAL III N   
10482 C CA  . VAL I 38  ? 0.976 0.940 0.935 -0.206 0.068  0.189  367 VAL III CA  
10483 C C   . VAL I 38  ? 0.940 0.895 0.900 -0.206 0.049  0.163  367 VAL III C   
10484 O O   . VAL I 38  ? 0.950 0.910 0.940 -0.227 0.036  0.163  367 VAL III O   
10485 C CB  . VAL I 38  ? 0.965 0.986 0.927 -0.192 0.087  0.197  367 VAL III CB  
10486 C CG1 . VAL I 38  ? 0.940 0.969 0.879 -0.167 0.086  0.175  367 VAL III CG1 
10487 C CG2 . VAL I 38  ? 0.951 1.022 0.954 -0.208 0.092  0.209  367 VAL III CG2 
10488 N N   . LEU I 39  ? 0.903 0.843 0.834 -0.183 0.046  0.144  368 LEU III N   
10489 C CA  . LEU I 39  ? 0.896 0.826 0.821 -0.176 0.031  0.121  368 LEU III CA  
10490 C C   . LEU I 39  ? 0.920 0.793 0.831 -0.184 0.011  0.112  368 LEU III C   
10491 O O   . LEU I 39  ? 0.924 0.792 0.840 -0.189 -0.007 0.097  368 LEU III O   
10492 C CB  . LEU I 39  ? 0.863 0.795 0.764 -0.148 0.038  0.109  368 LEU III CB  
10493 C CG  . LEU I 39  ? 0.826 0.808 0.738 -0.138 0.054  0.114  368 LEU III CG  
10494 C CD1 . LEU I 39  ? 0.822 0.800 0.717 -0.114 0.058  0.103  368 LEU III CD1 
10495 C CD2 . LEU I 39  ? 0.801 0.829 0.741 -0.147 0.053  0.114  368 LEU III CD2 
10496 N N   . TYR I 40  ? 0.940 0.768 0.831 -0.182 0.013  0.119  369 TYR III N   
10497 C CA  . TYR I 40  ? 1.006 0.769 0.876 -0.185 -0.006 0.109  369 TYR III CA  
10498 C C   . TYR I 40  ? 1.064 0.820 0.967 -0.217 -0.024 0.111  369 TYR III C   
10499 O O   . TYR I 40  ? 1.127 0.839 1.017 -0.219 -0.048 0.094  369 TYR III O   
10500 C CB  . TYR I 40  ? 1.020 0.741 0.867 -0.178 0.002  0.121  369 TYR III CB  
10501 C CG  . TYR I 40  ? 1.004 0.722 0.821 -0.147 0.015  0.118  369 TYR III CG  
10502 C CD1 . TYR I 40  ? 0.982 0.707 0.784 -0.124 0.015  0.101  369 TYR III CD1 
10503 C CD2 . TYR I 40  ? 1.000 0.708 0.807 -0.139 0.028  0.134  369 TYR III CD2 
10504 C CE1 . TYR I 40  ? 0.962 0.686 0.745 -0.098 0.027  0.101  369 TYR III CE1 
10505 C CE2 . TYR I 40  ? 0.990 0.698 0.776 -0.112 0.037  0.132  369 TYR III CE2 
10506 C CZ  . TYR I 40  ? 0.970 0.686 0.748 -0.093 0.037  0.116  369 TYR III CZ  
10507 O OH  . TYR I 40  ? 0.960 0.679 0.728 -0.068 0.046  0.117  369 TYR III OH  
10508 N N   . ASN I 41  ? 1.075 0.875 1.020 -0.239 -0.014 0.133  370 ASN III N   
10509 C CA  . ASN I 41  ? 1.132 0.930 1.121 -0.274 -0.028 0.144  370 ASN III CA  
10510 C C   . ASN I 41  ? 1.109 0.958 1.135 -0.285 -0.039 0.136  370 ASN III C   
10511 O O   . ASN I 41  ? 1.129 0.995 1.206 -0.315 -0.048 0.149  370 ASN III O   
10512 C CB  . ASN I 41  ? 1.148 0.967 1.165 -0.289 -0.006 0.179  370 ASN III CB  
10513 C CG  . ASN I 41  ? 1.192 0.956 1.176 -0.281 0.001  0.189  370 ASN III CG  
10514 O OD1 . ASN I 41  ? 1.271 0.972 1.232 -0.280 -0.017 0.175  370 ASN III OD1 
10515 N ND2 . ASN I 41  ? 1.176 0.964 1.154 -0.272 0.026  0.212  370 ASN III ND2 
10516 N N   . SER I 42  ? 1.081 0.954 1.087 -0.262 -0.039 0.117  371 SER III N   
10517 C CA  . SER I 42  ? 1.084 1.003 1.117 -0.266 -0.051 0.106  371 SER III CA  
10518 C C   . SER I 42  ? 1.136 1.012 1.153 -0.266 -0.085 0.078  371 SER III C   
10519 O O   . SER I 42  ? 1.176 1.002 1.141 -0.242 -0.089 0.061  371 SER III O   
10520 C CB  . SER I 42  ? 1.047 1.010 1.066 -0.241 -0.032 0.102  371 SER III CB  
10521 O OG  . SER I 42  ? 1.052 1.054 1.086 -0.241 -0.005 0.126  371 SER III OG  
10522 N N   . ALA I 43  ? 0.827 1.012 1.301 -0.287 0.040  0.118  372 ALA III N   
10523 C CA  . ALA I 43  ? 0.830 1.014 1.337 -0.297 0.012  0.089  372 ALA III CA  
10524 C C   . ALA I 43  ? 0.801 1.036 1.317 -0.285 -0.002 0.068  372 ALA III C   
10525 O O   . ALA I 43  ? 0.817 1.057 1.352 -0.287 -0.028 0.041  372 ALA III O   
10526 C CB  . ALA I 43  ? 0.826 1.007 1.397 -0.329 0.016  0.093  372 ALA III CB  
10527 N N   . SER I 44  ? 0.780 1.048 1.277 -0.269 0.013  0.078  373 SER III N   
10528 C CA  . SER I 44  ? 0.758 1.075 1.265 -0.256 0.003  0.062  373 SER III CA  
10529 C C   . SER I 44  ? 0.743 1.046 1.196 -0.229 -0.014 0.046  373 SER III C   
10530 O O   . SER I 44  ? 0.741 1.072 1.202 -0.220 -0.030 0.028  373 SER III O   
10531 C CB  . SER I 44  ? 0.742 1.101 1.258 -0.252 0.029  0.080  373 SER III CB  
10532 O OG  . SER I 44  ? 0.748 1.083 1.220 -0.244 0.051  0.104  373 SER III OG  
10533 N N   . PHE I 45  ? 0.714 0.977 1.117 -0.218 -0.010 0.054  374 PHE III N   
10534 C CA  . PHE I 45  ? 0.661 0.918 1.015 -0.192 -0.018 0.044  374 PHE III CA  
10535 C C   . PHE I 45  ? 0.633 0.881 0.984 -0.187 -0.045 0.018  374 PHE III C   
10536 O O   . PHE I 45  ? 0.625 0.844 0.984 -0.198 -0.056 0.011  374 PHE III O   
10537 C CB  . PHE I 45  ? 0.690 0.912 0.998 -0.181 -0.008 0.057  374 PHE III CB  
10538 C CG  . PHE I 45  ? 0.716 0.948 1.015 -0.180 0.017  0.079  374 PHE III CG  
10539 C CD1 . PHE I 45  ? 0.688 0.960 0.998 -0.175 0.029  0.084  374 PHE III CD1 
10540 C CD2 . PHE I 45  ? 0.748 0.947 1.022 -0.180 0.027  0.095  374 PHE III CD2 
10541 C CE1 . PHE I 45  ? 0.682 0.963 0.978 -0.171 0.051  0.103  374 PHE III CE1 
10542 C CE2 . PHE I 45  ? 0.747 0.954 1.004 -0.174 0.048  0.115  374 PHE III CE2 
10543 C CZ  . PHE I 45  ? 0.709 0.957 0.976 -0.170 0.060  0.119  374 PHE III CZ  
10544 N N   . SER I 46  ? 0.603 0.874 0.942 -0.170 -0.055 0.006  375 SER III N   
10545 C CA  . SER I 46  ? 0.600 0.866 0.927 -0.159 -0.079 -0.017 375 SER III CA  
10546 C C   . SER I 46  ? 0.562 0.787 0.839 -0.145 -0.081 -0.020 375 SER III C   
10547 O O   . SER I 46  ? 0.557 0.764 0.823 -0.141 -0.098 -0.037 375 SER III O   
10548 C CB  . SER I 46  ? 0.604 0.906 0.931 -0.144 -0.087 -0.026 375 SER III CB  
10549 O OG  . SER I 46  ? 0.614 0.920 0.911 -0.127 -0.071 -0.014 375 SER III OG  
10550 N N   . THR I 47  ? 0.549 0.764 0.798 -0.137 -0.063 -0.004 376 THR III N   
10551 C CA  . THR I 47  ? 0.549 0.732 0.755 -0.123 -0.062 -0.005 376 THR III CA  
10552 C C   . THR I 47  ? 0.534 0.706 0.728 -0.124 -0.043 0.014  376 THR III C   
10553 O O   . THR I 47  ? 0.532 0.725 0.737 -0.128 -0.030 0.027  376 THR III O   
10554 C CB  . THR I 47  ? 0.524 0.717 0.702 -0.103 -0.066 -0.013 376 THR III CB  
10555 O OG1 . THR I 47  ? 0.530 0.694 0.674 -0.091 -0.066 -0.017 376 THR III OG1 
10556 C CG2 . THR I 47  ? 0.502 0.717 0.677 -0.096 -0.052 -0.002 376 THR III CG2 
10557 N N   . PHE I 48  ? 0.532 0.672 0.704 -0.121 -0.043 0.014  377 PHE III N   
10558 C CA  . PHE I 48  ? 0.542 0.669 0.698 -0.118 -0.029 0.030  377 PHE III CA  
10559 C C   . PHE I 48  ? 0.543 0.643 0.672 -0.106 -0.034 0.023  377 PHE III C   
10560 O O   . PHE I 48  ? 0.576 0.650 0.705 -0.110 -0.041 0.020  377 PHE III O   
10561 C CB  . PHE I 48  ? 0.567 0.684 0.744 -0.135 -0.022 0.045  377 PHE III CB  
10562 C CG  . PHE I 48  ? 0.573 0.676 0.731 -0.131 -0.009 0.062  377 PHE III CG  
10563 C CD1 . PHE I 48  ? 0.554 0.650 0.681 -0.114 -0.008 0.062  377 PHE III CD1 
10564 C CD2 . PHE I 48  ? 0.597 0.693 0.769 -0.144 0.001  0.080  377 PHE III CD2 
10565 C CE1 . PHE I 48  ? 0.566 0.652 0.675 -0.109 0.001  0.076  377 PHE III CE1 
10566 C CE2 . PHE I 48  ? 0.616 0.697 0.765 -0.137 0.012  0.098  377 PHE III CE2 
10567 C CZ  . PHE I 48  ? 0.592 0.669 0.709 -0.119 0.011  0.094  377 PHE III CZ  
10568 N N   . LYS I 49  ? 0.500 0.609 0.609 -0.092 -0.031 0.020  378 LYS III N   
10569 C CA  . LYS I 49  ? 0.531 0.622 0.618 -0.080 -0.032 0.013  378 LYS III CA  
10570 C C   . LYS I 49  ? 0.525 0.620 0.599 -0.072 -0.022 0.021  378 LYS III C   
10571 O O   . LYS I 49  ? 0.519 0.634 0.594 -0.071 -0.015 0.026  378 LYS III O   
10572 C CB  . LYS I 49  ? 0.555 0.650 0.629 -0.069 -0.037 -0.000 378 LYS III CB  
10573 C CG  . LYS I 49  ? 0.575 0.670 0.657 -0.072 -0.051 -0.012 378 LYS III CG  
10574 C CD  . LYS I 49  ? 0.573 0.676 0.636 -0.058 -0.054 -0.021 378 LYS III CD  
10575 C CE  . LYS I 49  ? 0.611 0.712 0.673 -0.057 -0.070 -0.037 378 LYS III CE  
10576 N NZ  . LYS I 49  ? 0.600 0.708 0.637 -0.040 -0.070 -0.042 378 LYS III NZ  
10577 N N   . CYS I 50  ? 0.529 0.607 0.593 -0.065 -0.022 0.019  379 CYS III N   
10578 C CA  . CYS I 50  ? 0.526 0.609 0.580 -0.057 -0.016 0.022  379 CYS III CA  
10579 C C   . CYS I 50  ? 0.504 0.585 0.551 -0.047 -0.016 0.011  379 CYS III C   
10580 O O   . CYS I 50  ? 0.511 0.580 0.554 -0.044 -0.021 0.003  379 CYS III O   
10581 C CB  . CYS I 50  ? 0.561 0.632 0.611 -0.056 -0.016 0.032  379 CYS III CB  
10582 S SG  . CYS I 50  ? 0.606 0.680 0.664 -0.069 -0.011 0.049  379 CYS III SG  
10583 N N   . TYR I 51  ? 0.471 0.564 0.516 -0.041 -0.010 0.011  380 TYR III N   
10584 C CA  . TYR I 51  ? 0.469 0.565 0.512 -0.033 -0.005 0.003  380 TYR III CA  
10585 C C   . TYR I 51  ? 0.452 0.551 0.500 -0.028 -0.005 0.002  380 TYR III C   
10586 O O   . TYR I 51  ? 0.481 0.590 0.530 -0.030 -0.004 0.006  380 TYR III O   
10587 C CB  . TYR I 51  ? 0.463 0.570 0.506 -0.033 0.002  0.002  380 TYR III CB  
10588 C CG  . TYR I 51  ? 0.465 0.571 0.502 -0.036 -0.001 0.003  380 TYR III CG  
10589 C CD1 . TYR I 51  ? 0.476 0.590 0.519 -0.043 -0.004 0.008  380 TYR III CD1 
10590 C CD2 . TYR I 51  ? 0.454 0.553 0.481 -0.030 -0.002 -0.003 380 TYR III CD2 
10591 C CE1 . TYR I 51  ? 0.474 0.593 0.519 -0.045 -0.010 0.006  380 TYR III CE1 
10592 C CE2 . TYR I 51  ? 0.483 0.584 0.505 -0.030 -0.009 -0.005 380 TYR III CE2 
10593 C CZ  . TYR I 51  ? 0.484 0.596 0.517 -0.038 -0.013 -0.001 380 TYR III CZ  
10594 O OH  . TYR I 51  ? 0.494 0.611 0.527 -0.038 -0.022 -0.005 380 TYR III OH  
10595 N N   . GLY I 52  ? 0.437 0.532 0.488 -0.021 -0.006 -0.004 381 GLY III N   
10596 C CA  . GLY I 52  ? 0.439 0.541 0.498 -0.014 -0.008 -0.007 381 GLY III CA  
10597 C C   . GLY I 52  ? 0.499 0.591 0.552 -0.011 -0.018 -0.000 381 GLY III C   
10598 O O   . GLY I 52  ? 0.495 0.592 0.552 -0.002 -0.022 -0.003 381 GLY III O   
10599 N N   . VAL I 53  ? 0.534 0.611 0.577 -0.018 -0.020 0.009  382 VAL III N   
10600 C CA  . VAL I 53  ? 0.543 0.602 0.578 -0.015 -0.027 0.019  382 VAL III CA  
10601 C C   . VAL I 53  ? 0.543 0.581 0.577 -0.023 -0.028 0.023  382 VAL III C   
10602 O O   . VAL I 53  ? 0.550 0.593 0.588 -0.033 -0.025 0.021  382 VAL III O   
10603 C CB  . VAL I 53  ? 0.554 0.623 0.581 -0.016 -0.025 0.029  382 VAL III CB  
10604 C CG1 . VAL I 53  ? 0.542 0.630 0.571 -0.006 -0.027 0.022  382 VAL III CG1 
10605 C CG2 . VAL I 53  ? 0.553 0.631 0.581 -0.027 -0.018 0.035  382 VAL III CG2 
10606 N N   . SER I 54  ? 0.550 0.562 0.580 -0.020 -0.034 0.028  383 SER III N   
10607 C CA  . SER I 54  ? 0.571 0.559 0.604 -0.030 -0.037 0.032  383 SER III CA  
10608 C C   . SER I 54  ? 0.610 0.598 0.644 -0.042 -0.032 0.048  383 SER III C   
10609 O O   . SER I 54  ? 0.638 0.628 0.661 -0.038 -0.028 0.061  383 SER III O   
10610 C CB  . SER I 54  ? 0.593 0.549 0.621 -0.021 -0.044 0.031  383 SER III CB  
10611 O OG  . SER I 54  ? 0.597 0.527 0.632 -0.033 -0.048 0.033  383 SER III OG  
10612 N N   . PRO I 55  ? 0.601 0.590 0.647 -0.057 -0.030 0.049  384 PRO III N   
10613 C CA  . PRO I 55  ? 0.623 0.614 0.676 -0.070 -0.023 0.065  384 PRO III CA  
10614 C C   . PRO I 55  ? 0.676 0.636 0.722 -0.071 -0.021 0.082  384 PRO III C   
10615 O O   . PRO I 55  ? 0.705 0.669 0.748 -0.075 -0.011 0.100  384 PRO III O   
10616 C CB  . PRO I 55  ? 0.622 0.614 0.696 -0.086 -0.026 0.057  384 PRO III CB  
10617 C CG  . PRO I 55  ? 0.596 0.600 0.666 -0.078 -0.033 0.037  384 PRO III CG  
10618 C CD  . PRO I 55  ? 0.598 0.591 0.653 -0.061 -0.035 0.032  384 PRO III CD  
10619 N N   . THR I 56  ? 0.701 0.632 0.745 -0.064 -0.030 0.077  385 THR III N   
10620 C CA  . THR I 56  ? 0.757 0.650 0.794 -0.062 -0.030 0.092  385 THR III CA  
10621 C C   . THR I 56  ? 0.770 0.667 0.782 -0.045 -0.027 0.106  385 THR III C   
10622 O O   . THR I 56  ? 0.827 0.696 0.828 -0.042 -0.024 0.124  385 THR III O   
10623 C CB  . THR I 56  ? 0.771 0.629 0.810 -0.056 -0.042 0.080  385 THR III CB  
10624 O OG1 . THR I 56  ? 0.754 0.621 0.781 -0.036 -0.048 0.066  385 THR III OG1 
10625 C CG2 . THR I 56  ? 0.762 0.616 0.823 -0.072 -0.048 0.064  385 THR III CG2 
10626 N N   . LYS I 57  ? 0.756 0.684 0.760 -0.033 -0.029 0.096  386 LYS III N   
10627 C CA  . LYS I 57  ? 0.790 0.724 0.773 -0.014 -0.031 0.102  386 LYS III CA  
10628 C C   . LYS I 57  ? 0.759 0.721 0.731 -0.015 -0.022 0.110  386 LYS III C   
10629 O O   . LYS I 57  ? 0.761 0.732 0.715 0.000  -0.026 0.113  386 LYS III O   
10630 C CB  . LYS I 57  ? 0.805 0.752 0.789 0.001  -0.041 0.082  386 LYS III CB  
10631 C CG  . LYS I 57  ? 0.859 0.781 0.851 0.007  -0.049 0.073  386 LYS III CG  
10632 C CD  . LYS I 57  ? 0.960 0.849 0.936 0.023  -0.055 0.084  386 LYS III CD  
10633 C CE  . LYS I 57  ? 1.046 0.956 1.013 0.044  -0.063 0.080  386 LYS III CE  
10634 N NZ  . LYS I 57  ? 1.101 0.991 1.043 0.058  -0.065 0.101  386 LYS III NZ  
10635 N N   . LEU I 58  ? 0.727 0.705 0.711 -0.032 -0.013 0.113  387 LEU III N   
10636 C CA  . LEU I 58  ? 0.729 0.737 0.704 -0.031 -0.004 0.117  387 LEU III CA  
10637 C C   . LEU I 58  ? 0.789 0.787 0.736 -0.021 0.002  0.139  387 LEU III C   
10638 O O   . LEU I 58  ? 0.835 0.854 0.764 -0.009 0.002  0.137  387 LEU III O   
10639 C CB  . LEU I 58  ? 0.707 0.730 0.703 -0.049 0.006  0.118  387 LEU III CB  
10640 C CG  . LEU I 58  ? 0.671 0.709 0.686 -0.055 -0.000 0.096  387 LEU III CG  
10641 C CD1 . LEU I 58  ? 0.653 0.709 0.687 -0.070 0.008  0.098  387 LEU III CD1 
10642 C CD2 . LEU I 58  ? 0.652 0.711 0.660 -0.042 -0.004 0.082  387 LEU III CD2 
10643 N N   . ASN I 59  ? 0.833 0.799 0.775 -0.023 0.006  0.158  388 ASN III N   
10644 C CA  . ASN I 59  ? 0.871 0.823 0.780 -0.012 0.014  0.183  388 ASN III CA  
10645 C C   . ASN I 59  ? 0.888 0.833 0.770 0.014  -0.001 0.179  388 ASN III C   
10646 O O   . ASN I 59  ? 0.920 0.858 0.769 0.029  0.003  0.198  388 ASN III O   
10647 C CB  . ASN I 59  ? 0.897 0.815 0.811 -0.025 0.026  0.208  388 ASN III CB  
10648 C CG  . ASN I 59  ? 0.892 0.829 0.822 -0.044 0.045  0.220  388 ASN III CG  
10649 O OD1 . ASN I 59  ? 0.888 0.861 0.816 -0.043 0.050  0.212  388 ASN III OD1 
10650 N ND2 . ASN I 59  ? 0.927 0.841 0.877 -0.063 0.057  0.236  388 ASN III ND2 
10651 N N   . ASP I 60  ? 0.867 0.818 0.762 0.022  -0.016 0.157  389 ASP III N   
10652 C CA  . ASP I 60  ? 0.868 0.815 0.745 0.046  -0.032 0.151  389 ASP III CA  
10653 C C   . ASP I 60  ? 0.807 0.794 0.690 0.055  -0.042 0.127  389 ASP III C   
10654 O O   . ASP I 60  ? 0.806 0.796 0.681 0.075  -0.056 0.119  389 ASP III O   
10655 C CB  . ASP I 60  ? 0.895 0.815 0.787 0.049  -0.042 0.144  389 ASP III CB  
10656 C CG  . ASP I 60  ? 0.987 0.862 0.878 0.040  -0.034 0.164  389 ASP III CG  
10657 O OD1 . ASP I 60  ? 1.058 0.910 0.921 0.050  -0.030 0.189  389 ASP III OD1 
10658 O OD2 . ASP I 60  ? 1.058 0.921 0.975 0.023  -0.033 0.156  389 ASP III OD2 
10659 N N   . LEU I 61  ? 0.766 0.779 0.663 0.042  -0.036 0.116  390 LEU III N   
10660 C CA  . LEU I 61  ? 0.726 0.773 0.636 0.047  -0.044 0.091  390 LEU III CA  
10661 C C   . LEU I 61  ? 0.721 0.791 0.611 0.054  -0.043 0.090  390 LEU III C   
10662 O O   . LEU I 61  ? 0.728 0.795 0.603 0.048  -0.030 0.106  390 LEU III O   
10663 C CB  . LEU I 61  ? 0.709 0.765 0.650 0.029  -0.039 0.077  390 LEU III CB  
10664 C CG  . LEU I 61  ? 0.735 0.773 0.695 0.026  -0.043 0.071  390 LEU III CG  
10665 C CD1 . LEU I 61  ? 0.705 0.754 0.689 0.011  -0.038 0.058  390 LEU III CD1 
10666 C CD2 . LEU I 61  ? 0.737 0.777 0.699 0.044  -0.056 0.061  390 LEU III CD2 
10667 N N   . CYS I 62  ? 0.714 0.807 0.608 0.065  -0.055 0.070  391 CYS III N   
10668 C CA  . CYS I 62  ? 0.717 0.834 0.596 0.073  -0.058 0.061  391 CYS III CA  
10669 C C   . CYS I 62  ? 0.657 0.796 0.567 0.062  -0.058 0.037  391 CYS III C   
10670 O O   . CYS I 62  ? 0.633 0.774 0.571 0.057  -0.063 0.025  391 CYS III O   
10671 C CB  . CYS I 62  ? 0.755 0.878 0.611 0.098  -0.076 0.055  391 CYS III CB  
10672 S SG  . CYS I 62  ? 0.854 0.948 0.662 0.115  -0.073 0.087  391 CYS III SG  
10673 N N   . PHE I 63  ? 0.635 0.788 0.539 0.058  -0.052 0.033  392 PHE III N   
10674 C CA  . PHE I 63  ? 0.590 0.759 0.519 0.048  -0.050 0.013  392 PHE III CA  
10675 C C   . PHE I 63  ? 0.595 0.780 0.507 0.060  -0.058 -0.001 392 PHE III C   
10676 O O   . PHE I 63  ? 0.647 0.832 0.524 0.073  -0.057 0.010  392 PHE III O   
10677 C CB  . PHE I 63  ? 0.550 0.714 0.491 0.031  -0.034 0.021  392 PHE III CB  
10678 C CG  . PHE I 63  ? 0.529 0.676 0.485 0.020  -0.029 0.032  392 PHE III CG  
10679 C CD1 . PHE I 63  ? 0.509 0.655 0.490 0.017  -0.034 0.020  392 PHE III CD1 
10680 C CD2 . PHE I 63  ? 0.540 0.671 0.486 0.015  -0.020 0.052  392 PHE III CD2 
10681 C CE1 . PHE I 63  ? 0.509 0.640 0.500 0.010  -0.031 0.027  392 PHE III CE1 
10682 C CE2 . PHE I 63  ? 0.526 0.640 0.486 0.006  -0.019 0.058  392 PHE III CE2 
10683 C CZ  . PHE I 63  ? 0.530 0.642 0.509 0.005  -0.025 0.045  392 PHE III CZ  
10684 N N   . THR I 64  ? 0.586 0.786 0.524 0.056  -0.064 -0.024 393 THR III N   
10685 C CA  . THR I 64  ? 0.614 0.828 0.543 0.065  -0.073 -0.044 393 THR III CA  
10686 C C   . THR I 64  ? 0.622 0.835 0.538 0.061  -0.058 -0.039 393 THR III C   
10687 O O   . THR I 64  ? 0.646 0.866 0.535 0.074  -0.062 -0.045 393 THR III O   
10688 C CB  . THR I 64  ? 0.590 0.817 0.558 0.061  -0.086 -0.070 393 THR III CB  
10689 O OG1 . THR I 64  ? 0.540 0.760 0.541 0.042  -0.073 -0.068 393 THR III OG1 
10690 C CG2 . THR I 64  ? 0.625 0.860 0.598 0.072  -0.103 -0.077 393 THR III CG2 
10691 N N   . ASN I 65  ? 0.620 0.825 0.552 0.045  -0.043 -0.028 394 ASN III N   
10692 C CA  . ASN I 65  ? 0.641 0.847 0.567 0.041  -0.028 -0.023 394 ASN III CA  
10693 C C   . ASN I 65  ? 0.588 0.786 0.528 0.027  -0.014 -0.005 394 ASN III C   
10694 O O   . ASN I 65  ? 0.555 0.745 0.516 0.018  -0.016 -0.004 394 ASN III O   
10695 C CB  . ASN I 65  ? 0.668 0.879 0.614 0.038  -0.030 -0.046 394 ASN III CB  
10696 C CG  . ASN I 65  ? 0.720 0.934 0.652 0.041  -0.019 -0.044 394 ASN III CG  
10697 O OD1 . ASN I 65  ? 0.758 0.979 0.658 0.056  -0.019 -0.044 394 ASN III OD1 
10698 N ND2 . ASN I 65  ? 0.705 0.915 0.658 0.030  -0.008 -0.042 394 ASN III ND2 
10699 N N   . VAL I 66  ? 0.591 0.792 0.520 0.025  -0.000 0.009  395 VAL III N   
10700 C CA  . VAL I 66  ? 0.605 0.802 0.551 0.011  0.011  0.022  395 VAL III CA  
10701 C C   . VAL I 66  ? 0.608 0.816 0.558 0.011  0.021  0.019  395 VAL III C   
10702 O O   . VAL I 66  ? 0.606 0.825 0.536 0.022  0.026  0.018  395 VAL III O   
10703 C CB  . VAL I 66  ? 0.620 0.812 0.557 0.008  0.019  0.045  395 VAL III CB  
10704 C CG1 . VAL I 66  ? 0.563 0.752 0.523 -0.008 0.027  0.055  395 VAL III CG1 
10705 C CG2 . VAL I 66  ? 0.620 0.797 0.548 0.012  0.008  0.049  395 VAL III CG2 
10706 N N   . TYR I 67  ? 0.577 0.784 0.551 0.001  0.024  0.016  396 TYR III N   
10707 C CA  . TYR I 67  ? 0.577 0.794 0.558 0.001  0.034  0.015  396 TYR III CA  
10708 C C   . TYR I 67  ? 0.579 0.801 0.576 -0.009 0.041  0.030  396 TYR III C   
10709 O O   . TYR I 67  ? 0.546 0.757 0.555 -0.019 0.036  0.033  396 TYR III O   
10710 C CB  . TYR I 67  ? 0.598 0.808 0.592 0.002  0.030  -0.001 396 TYR III CB  
10711 C CG  . TYR I 67  ? 0.659 0.867 0.643 0.012  0.023  -0.018 396 TYR III CG  
10712 C CD1 . TYR I 67  ? 0.674 0.892 0.638 0.024  0.026  -0.023 396 TYR III CD1 
10713 C CD2 . TYR I 67  ? 0.692 0.889 0.689 0.009  0.014  -0.032 396 TYR III CD2 
10714 C CE1 . TYR I 67  ? 0.738 0.954 0.693 0.034  0.017  -0.043 396 TYR III CE1 
10715 C CE2 . TYR I 67  ? 0.759 0.955 0.752 0.016  0.006  -0.051 396 TYR III CE2 
10716 C CZ  . TYR I 67  ? 0.772 0.977 0.743 0.029  0.006  -0.058 396 TYR III CZ  
10717 O OH  . TYR I 67  ? 0.867 1.071 0.833 0.038  -0.005 -0.079 396 TYR III OH  
10718 N N   . ALA I 68  ? 0.575 0.814 0.573 -0.007 0.051  0.037  397 ALA III N   
10719 C CA  . ALA I 68  ? 0.562 0.811 0.581 -0.017 0.057  0.048  397 ALA III CA  
10720 C C   . ALA I 68  ? 0.546 0.807 0.577 -0.012 0.060  0.039  397 ALA III C   
10721 O O   . ALA I 68  ? 0.578 0.854 0.602 -0.001 0.068  0.037  397 ALA III O   
10722 C CB  . ALA I 68  ? 0.573 0.837 0.590 -0.020 0.069  0.064  397 ALA III CB  
10723 N N   . ASP I 69  ? 0.489 0.742 0.534 -0.016 0.053  0.035  398 ASP III N   
10724 C CA  . ASP I 69  ? 0.494 0.756 0.551 -0.011 0.053  0.029  398 ASP III CA  
10725 C C   . ASP I 69  ? 0.484 0.764 0.562 -0.018 0.055  0.038  398 ASP III C   
10726 O O   . ASP I 69  ? 0.446 0.721 0.533 -0.030 0.049  0.043  398 ASP III O   
10727 C CB  . ASP I 69  ? 0.504 0.743 0.559 -0.009 0.046  0.021  398 ASP III CB  
10728 C CG  . ASP I 69  ? 0.511 0.732 0.552 -0.005 0.044  0.011  398 ASP III CG  
10729 O OD1 . ASP I 69  ? 0.533 0.760 0.564 0.002  0.047  0.007  398 ASP III OD1 
10730 O OD2 . ASP I 69  ? 0.546 0.749 0.588 -0.009 0.039  0.008  398 ASP III OD2 
10731 N N   . SER I 70  ? 0.515 0.820 0.606 -0.011 0.060  0.038  399 SER III N   
10732 C CA  . SER I 70  ? 0.533 0.863 0.652 -0.019 0.061  0.044  399 SER III CA  
10733 C C   . SER I 70  ? 0.537 0.883 0.668 -0.006 0.058  0.037  399 SER III C   
10734 O O   . SER I 70  ? 0.542 0.887 0.660 0.009  0.063  0.031  399 SER III O   
10735 C CB  . SER I 70  ? 0.530 0.883 0.660 -0.025 0.073  0.055  399 SER III CB  
10736 O OG  . SER I 70  ? 0.555 0.920 0.671 -0.011 0.085  0.054  399 SER III OG  
10737 N N   . PHE I 71  ? 0.528 0.891 0.683 -0.011 0.050  0.037  400 PHE III N   
10738 C CA  . PHE I 71  ? 0.527 0.906 0.694 0.003  0.044  0.031  400 PHE III CA  
10739 C C   . PHE I 71  ? 0.514 0.915 0.711 -0.006 0.033  0.031  400 PHE III C   
10740 O O   . PHE I 71  ? 0.495 0.891 0.701 -0.024 0.030  0.034  400 PHE III O   
10741 C CB  . PHE I 71  ? 0.536 0.883 0.677 0.015  0.038  0.025  400 PHE III CB  
10742 C CG  . PHE I 71  ? 0.536 0.852 0.661 0.006  0.029  0.025  400 PHE III CG  
10743 C CD1 . PHE I 71  ? 0.526 0.842 0.658 0.002  0.017  0.023  400 PHE III CD1 
10744 C CD2 . PHE I 71  ? 0.545 0.833 0.650 0.002  0.034  0.025  400 PHE III CD2 
10745 C CE1 . PHE I 71  ? 0.522 0.811 0.638 -0.004 0.011  0.022  400 PHE III CE1 
10746 C CE2 . PHE I 71  ? 0.530 0.793 0.623 -0.005 0.028  0.024  400 PHE III CE2 
10747 C CZ  . PHE I 71  ? 0.518 0.782 0.616 -0.008 0.018  0.024  400 PHE III CZ  
10748 N N   . VAL I 72  ? 0.506 0.927 0.717 0.007  0.025  0.025  401 VAL III N   
10749 C CA  . VAL I 72  ? 0.525 0.969 0.764 0.003  0.010  0.020  401 VAL III CA  
10750 C C   . VAL I 72  ? 0.521 0.944 0.737 0.018  -0.006 0.014  401 VAL III C   
10751 O O   . VAL I 72  ? 0.503 0.913 0.697 0.037  -0.004 0.014  401 VAL III O   
10752 C CB  . VAL I 72  ? 0.546 1.042 0.826 0.007  0.013  0.019  401 VAL III CB  
10753 C CG1 . VAL I 72  ? 0.565 1.087 0.875 0.007  -0.007 0.010  401 VAL III CG1 
10754 C CG2 . VAL I 72  ? 0.556 1.073 0.861 -0.011 0.031  0.028  401 VAL III CG2 
10755 N N   . ILE I 73  ? 0.513 0.932 0.733 0.010  -0.022 0.009  402 ILE III N   
10756 C CA  . ILE I 73  ? 0.533 0.937 0.731 0.025  -0.039 0.002  402 ILE III CA  
10757 C C   . ILE I 73  ? 0.566 0.998 0.793 0.018  -0.059 -0.008 402 ILE III C   
10758 O O   . ILE I 73  ? 0.567 1.025 0.833 -0.000 -0.058 -0.009 402 ILE III O   
10759 C CB  . ILE I 73  ? 0.517 0.874 0.673 0.024  -0.037 0.005  402 ILE III CB  
10760 C CG1 . ILE I 73  ? 0.486 0.832 0.649 0.001  -0.035 0.005  402 ILE III CG1 
10761 C CG2 . ILE I 73  ? 0.525 0.857 0.656 0.034  -0.021 0.012  402 ILE III CG2 
10762 C CD1 . ILE I 73  ? 0.500 0.806 0.628 0.002  -0.035 0.006  402 ILE III CD1 
10763 N N   . ARG I 74  ? 0.618 1.045 0.827 0.034  -0.078 -0.016 403 ARG III N   
10764 C CA  . ARG I 74  ? 0.656 1.103 0.886 0.029  -0.102 -0.030 403 ARG III CA  
10765 C C   . ARG I 74  ? 0.623 1.043 0.845 0.010  -0.105 -0.033 403 ARG III C   
10766 O O   . ARG I 74  ? 0.579 0.961 0.765 0.010  -0.093 -0.026 403 ARG III O   
10767 C CB  . ARG I 74  ? 0.732 1.172 0.929 0.056  -0.120 -0.036 403 ARG III CB  
10768 C CG  . ARG I 74  ? 0.770 1.241 0.978 0.080  -0.127 -0.037 403 ARG III CG  
10769 C CD  . ARG I 74  ? 0.820 1.267 0.978 0.109  -0.138 -0.036 403 ARG III CD  
10770 N NE  . ARG I 74  ? 0.843 1.282 0.983 0.111  -0.159 -0.048 403 ARG III NE  
10771 C CZ  . ARG I 74  ? 0.898 1.312 0.988 0.135  -0.168 -0.047 403 ARG III CZ  
10772 N NH1 . ARG I 74  ? 0.903 1.294 0.957 0.158  -0.157 -0.033 403 ARG III NH1 
10773 N NH2 . ARG I 74  ? 0.947 1.357 1.022 0.136  -0.188 -0.060 403 ARG III NH2 
10774 N N   . GLY I 75  ? 0.615 1.055 0.871 -0.004 -0.122 -0.046 404 GLY III N   
10775 C CA  . GLY I 75  ? 0.614 1.029 0.866 -0.021 -0.129 -0.053 404 GLY III CA  
10776 C C   . GLY I 75  ? 0.619 0.994 0.815 -0.006 -0.132 -0.055 404 GLY III C   
10777 O O   . GLY I 75  ? 0.612 0.955 0.790 -0.016 -0.121 -0.049 404 GLY III O   
10778 N N   . ASP I 76  ? 0.691 1.067 0.858 0.019  -0.146 -0.061 405 ASP III N   
10779 C CA  . ASP I 76  ? 0.749 1.088 0.863 0.033  -0.150 -0.063 405 ASP III CA  
10780 C C   . ASP I 76  ? 0.716 1.025 0.793 0.043  -0.125 -0.045 405 ASP III C   
10781 O O   . ASP I 76  ? 0.724 1.003 0.759 0.053  -0.122 -0.043 405 ASP III O   
10782 C CB  . ASP I 76  ? 0.807 1.155 0.901 0.055  -0.176 -0.078 405 ASP III CB  
10783 C CG  . ASP I 76  ? 0.869 1.246 0.966 0.077  -0.185 -0.077 405 ASP III CG  
10784 O OD1 . ASP I 76  ? 0.876 1.252 0.971 0.082  -0.166 -0.061 405 ASP III OD1 
10785 O OD2 . ASP I 76  ? 0.900 1.300 1.001 0.090  -0.212 -0.093 405 ASP III OD2 
10786 N N   . GLU I 77  ? 0.680 0.996 0.774 0.037  -0.107 -0.032 406 GLU III N   
10787 C CA  . GLU I 77  ? 0.646 0.933 0.712 0.042  -0.085 -0.017 406 GLU III CA  
10788 C C   . GLU I 77  ? 0.612 0.884 0.688 0.020  -0.071 -0.014 406 GLU III C   
10789 O O   . GLU I 77  ? 0.614 0.861 0.668 0.021  -0.055 -0.005 406 GLU III O   
10790 C CB  . GLU I 77  ? 0.630 0.932 0.705 0.052  -0.075 -0.009 406 GLU III CB  
10791 C CG  . GLU I 77  ? 0.634 0.941 0.690 0.079  -0.086 -0.009 406 GLU III CG  
10792 C CD  . GLU I 77  ? 0.619 0.944 0.689 0.091  -0.079 -0.004 406 GLU III CD  
10793 O OE1 . GLU I 77  ? 0.574 0.918 0.677 0.077  -0.070 -0.003 406 GLU III OE1 
10794 O OE2 . GLU I 77  ? 0.642 0.960 0.689 0.116  -0.083 0.001  406 GLU III OE2 
10795 N N   . VAL I 78  ? 0.588 0.873 0.695 0.001  -0.077 -0.019 407 VAL III N   
10796 C CA  . VAL I 78  ? 0.569 0.838 0.682 -0.018 -0.065 -0.014 407 VAL III CA  
10797 C C   . VAL I 78  ? 0.563 0.797 0.642 -0.014 -0.062 -0.015 407 VAL III C   
10798 O O   . VAL I 78  ? 0.533 0.752 0.605 -0.019 -0.047 -0.007 407 VAL III O   
10799 C CB  . VAL I 78  ? 0.576 0.861 0.728 -0.038 -0.072 -0.018 407 VAL III CB  
10800 C CG1 . VAL I 78  ? 0.557 0.818 0.707 -0.054 -0.062 -0.013 407 VAL III CG1 
10801 C CG2 . VAL I 78  ? 0.567 0.889 0.755 -0.043 -0.068 -0.014 407 VAL III CG2 
10802 N N   . ARG I 79  ? 0.594 0.818 0.652 -0.004 -0.074 -0.024 408 ARG III N   
10803 C CA  . ARG I 79  ? 0.610 0.804 0.635 0.002  -0.069 -0.025 408 ARG III CA  
10804 C C   . ARG I 79  ? 0.582 0.762 0.585 0.012  -0.050 -0.012 408 ARG III C   
10805 O O   . ARG I 79  ? 0.579 0.738 0.565 0.012  -0.041 -0.011 408 ARG III O   
10806 C CB  . ARG I 79  ? 0.672 0.863 0.675 0.015  -0.086 -0.038 408 ARG III CB  
10807 C CG  . ARG I 79  ? 0.757 0.953 0.735 0.038  -0.089 -0.035 408 ARG III CG  
10808 C CD  . ARG I 79  ? 0.869 1.062 0.820 0.053  -0.108 -0.049 408 ARG III CD  
10809 N NE  . ARG I 79  ? 0.958 1.180 0.929 0.057  -0.132 -0.062 408 ARG III NE  
10810 C CZ  . ARG I 79  ? 0.996 1.232 0.995 0.044  -0.153 -0.079 408 ARG III CZ  
10811 N NH1 . ARG I 79  ? 1.068 1.288 1.076 0.029  -0.153 -0.087 408 ARG III NH1 
10812 N NH2 . ARG I 79  ? 0.963 1.230 0.986 0.048  -0.173 -0.090 408 ARG III NH2 
10813 N N   . GLN I 80  ? 0.539 0.728 0.544 0.019  -0.044 -0.005 409 GLN III N   
10814 C CA  . GLN I 80  ? 0.542 0.714 0.529 0.027  -0.026 0.006  409 GLN III CA  
10815 C C   . GLN I 80  ? 0.507 0.677 0.512 0.013  -0.014 0.011  409 GLN III C   
10816 O O   . GLN I 80  ? 0.482 0.636 0.477 0.015  0.000  0.016  409 GLN III O   
10817 C CB  . GLN I 80  ? 0.565 0.745 0.547 0.042  -0.026 0.011  409 GLN III CB  
10818 C CG  . GLN I 80  ? 0.590 0.766 0.544 0.062  -0.036 0.010  409 GLN III CG  
10819 C CD  . GLN I 80  ? 0.626 0.805 0.571 0.080  -0.036 0.017  409 GLN III CD  
10820 O OE1 . GLN I 80  ? 0.620 0.784 0.562 0.083  -0.020 0.027  409 GLN III OE1 
10821 N NE2 . GLN I 80  ? 0.679 0.878 0.623 0.093  -0.054 0.011  409 GLN III NE2 
10822 N N   . ILE I 81  ? 0.525 0.710 0.555 -0.001 -0.018 0.008  410 ILE III N   
10823 C CA  . ILE I 81  ? 0.512 0.696 0.554 -0.012 -0.007 0.012  410 ILE III CA  
10824 C C   . ILE I 81  ? 0.521 0.689 0.558 -0.019 -0.007 0.010  410 ILE III C   
10825 O O   . ILE I 81  ? 0.509 0.679 0.558 -0.031 -0.011 0.009  410 ILE III O   
10826 C CB  . ILE I 81  ? 0.518 0.725 0.585 -0.021 -0.009 0.014  410 ILE III CB  
10827 C CG1 . ILE I 81  ? 0.529 0.758 0.604 -0.011 -0.012 0.014  410 ILE III CG1 
10828 C CG2 . ILE I 81  ? 0.530 0.735 0.599 -0.026 0.003  0.019  410 ILE III CG2 
10829 C CD1 . ILE I 81  ? 0.533 0.752 0.592 0.003  -0.004 0.017  410 ILE III CD1 
10830 N N   . ALA I 82  ? 0.545 0.695 0.564 -0.013 0.000  0.010  411 ALA III N   
10831 C CA  . ALA I 82  ? 0.549 0.685 0.562 -0.015 0.002  0.007  411 ALA III CA  
10832 C C   . ALA I 82  ? 0.575 0.697 0.575 -0.008 0.015  0.010  411 ALA III C   
10833 O O   . ALA I 82  ? 0.554 0.673 0.542 0.001  0.020  0.014  411 ALA III O   
10834 C CB  . ALA I 82  ? 0.530 0.661 0.534 -0.013 -0.011 -0.000 411 ALA III CB  
10835 N N   . PRO I 83  ? 0.603 0.718 0.606 -0.012 0.021  0.009  412 PRO III N   
10836 C CA  . PRO I 83  ? 0.587 0.692 0.585 -0.007 0.035  0.011  412 PRO III CA  
10837 C C   . PRO I 83  ? 0.571 0.667 0.545 0.005  0.039  0.013  412 PRO III C   
10838 O O   . PRO I 83  ? 0.568 0.664 0.531 0.008  0.028  0.007  412 PRO III O   
10839 C CB  . PRO I 83  ? 0.608 0.713 0.618 -0.013 0.037  0.006  412 PRO III CB  
10840 C CG  . PRO I 83  ? 0.610 0.717 0.621 -0.016 0.022  0.002  412 PRO III CG  
10841 C CD  . PRO I 83  ? 0.611 0.727 0.626 -0.020 0.016  0.005  412 PRO III CD  
10842 N N   . GLY I 84  ? 0.569 0.656 0.534 0.011  0.053  0.021  413 GLY III N   
10843 C CA  . GLY I 84  ? 0.595 0.670 0.532 0.024  0.062  0.026  413 GLY III CA  
10844 C C   . GLY I 84  ? 0.614 0.689 0.527 0.037  0.052  0.028  413 GLY III C   
10845 O O   . GLY I 84  ? 0.688 0.754 0.572 0.051  0.056  0.031  413 GLY III O   
10846 N N   . GLN I 85  ? 0.600 0.685 0.524 0.035  0.040  0.027  414 GLN III N   
10847 C CA  . GLN I 85  ? 0.621 0.711 0.527 0.047  0.027  0.027  414 GLN III CA  
10848 C C   . GLN I 85  ? 0.624 0.702 0.517 0.059  0.038  0.039  414 GLN III C   
10849 O O   . GLN I 85  ? 0.586 0.657 0.495 0.052  0.051  0.045  414 GLN III O   
10850 C CB  . GLN I 85  ? 0.625 0.737 0.556 0.038  0.010  0.019  414 GLN III CB  
10851 C CG  . GLN I 85  ? 0.626 0.744 0.566 0.029  -0.003 0.008  414 GLN III CG  
10852 C CD  . GLN I 85  ? 0.656 0.772 0.570 0.042  -0.015 0.000  414 GLN III CD  
10853 O OE1 . GLN I 85  ? 0.718 0.839 0.618 0.056  -0.023 0.001  414 GLN III OE1 
10854 N NE2 . GLN I 85  ? 0.704 0.812 0.611 0.041  -0.018 -0.008 414 GLN III NE2 
10855 N N   . THR I 86  ? 0.654 0.731 0.520 0.077  0.030  0.043  415 THR III N   
10856 C CA  . THR I 86  ? 0.701 0.767 0.553 0.092  0.035  0.054  415 THR III CA  
10857 C C   . THR I 86  ? 0.709 0.796 0.560 0.103  0.013  0.048  415 THR III C   
10858 O O   . THR I 86  ? 0.697 0.803 0.555 0.100  -0.005 0.035  415 THR III O   
10859 C CB  . THR I 86  ? 0.778 0.817 0.592 0.108  0.052  0.069  415 THR III CB  
10860 O OG1 . THR I 86  ? 0.826 0.870 0.610 0.121  0.041  0.063  415 THR III OG1 
10861 C CG2 . THR I 86  ? 0.799 0.821 0.622 0.096  0.077  0.077  415 THR III CG2 
10862 N N   . GLY I 87  ? 0.728 0.810 0.574 0.116  0.014  0.056  416 GLY III N   
10863 C CA  . GLY I 87  ? 0.728 0.834 0.581 0.128  -0.005 0.051  416 GLY III CA  
10864 C C   . GLY I 87  ? 0.721 0.829 0.597 0.127  0.001  0.055  416 GLY III C   
10865 O O   . GLY I 87  ? 0.692 0.784 0.580 0.114  0.018  0.059  416 GLY III O   
10866 N N   . LYS I 88  ? 0.730 0.859 0.614 0.140  -0.013 0.052  417 LYS III N   
10867 C CA  . LYS I 88  ? 0.719 0.851 0.622 0.144  -0.008 0.055  417 LYS III CA  
10868 C C   . LYS I 88  ? 0.669 0.810 0.604 0.120  0.000  0.048  417 LYS III C   
10869 O O   . LYS I 88  ? 0.657 0.780 0.597 0.118  0.014  0.052  417 LYS III O   
10870 C CB  . LYS I 88  ? 0.754 0.921 0.671 0.159  -0.027 0.048  417 LYS III CB  
10871 C CG  . LYS I 88  ? 0.835 0.998 0.719 0.189  -0.040 0.053  417 LYS III CG  
10872 C CD  . LYS I 88  ? 0.915 1.032 0.762 0.207  -0.024 0.071  417 LYS III CD  
10873 C CE  . LYS I 88  ? 0.984 1.095 0.792 0.239  -0.036 0.078  417 LYS III CE  
10874 N NZ  . LYS I 88  ? 1.050 1.110 0.815 0.252  -0.016 0.099  417 LYS III NZ  
10875 N N   . ILE I 89  ? 0.623 0.788 0.579 0.102  -0.008 0.038  418 ILE III N   
10876 C CA  . ILE I 89  ? 0.596 0.775 0.583 0.082  -0.002 0.033  418 ILE III CA  
10877 C C   . ILE I 89  ? 0.579 0.730 0.558 0.069  0.013  0.036  418 ILE III C   
10878 O O   . ILE I 89  ? 0.587 0.728 0.574 0.066  0.024  0.037  418 ILE III O   
10879 C CB  . ILE I 89  ? 0.588 0.800 0.600 0.068  -0.015 0.024  418 ILE III CB  
10880 C CG1 . ILE I 89  ? 0.604 0.847 0.629 0.080  -0.031 0.019  418 ILE III CG1 
10881 C CG2 . ILE I 89  ? 0.592 0.814 0.628 0.051  -0.006 0.022  418 ILE III CG2 
10882 C CD1 . ILE I 89  ? 0.617 0.873 0.653 0.093  -0.026 0.022  418 ILE III CD1 
10883 N N   . ALA I 90  ? 0.559 0.697 0.524 0.065  0.014  0.037  419 ALA III N   
10884 C CA  . ALA I 90  ? 0.576 0.691 0.538 0.053  0.028  0.039  419 ALA III CA  
10885 C C   . ALA I 90  ? 0.605 0.693 0.558 0.061  0.044  0.048  419 ALA III C   
10886 O O   . ALA I 90  ? 0.584 0.661 0.550 0.050  0.054  0.046  419 ALA III O   
10887 C CB  . ALA I 90  ? 0.601 0.709 0.546 0.053  0.027  0.039  419 ALA III CB  
10888 N N   . ASP I 91  ? 0.634 0.709 0.565 0.079  0.045  0.057  420 ASP III N   
10889 C CA  . ASP I 91  ? 0.699 0.739 0.618 0.087  0.061  0.068  420 ASP III CA  
10890 C C   . ASP I 91  ? 0.709 0.746 0.643 0.090  0.063  0.066  420 ASP III C   
10891 O O   . ASP I 91  ? 0.717 0.728 0.658 0.084  0.077  0.068  420 ASP III O   
10892 C CB  . ASP I 91  ? 0.771 0.793 0.654 0.109  0.063  0.081  420 ASP III CB  
10893 C CG  . ASP I 91  ? 0.781 0.801 0.641 0.110  0.064  0.084  420 ASP III CG  
10894 O OD1 . ASP I 91  ? 0.809 0.834 0.682 0.092  0.068  0.078  420 ASP III OD1 
10895 O OD2 . ASP I 91  ? 0.832 0.843 0.657 0.130  0.061  0.093  420 ASP III OD2 
10896 N N   . TYR I 92  ? 0.683 0.744 0.625 0.099  0.050  0.060  421 TYR III N   
10897 C CA  . TYR I 92  ? 0.693 0.749 0.642 0.110  0.052  0.059  421 TYR III CA  
10898 C C   . TYR I 92  ? 0.641 0.729 0.617 0.101  0.046  0.046  421 TYR III C   
10899 O O   . TYR I 92  ? 0.661 0.744 0.644 0.110  0.049  0.043  421 TYR III O   
10900 C CB  . TYR I 92  ? 0.733 0.791 0.664 0.136  0.043  0.066  421 TYR III CB  
10901 C CG  . TYR I 92  ? 0.781 0.805 0.678 0.151  0.050  0.082  421 TYR III CG  
10902 C CD1 . TYR I 92  ? 0.798 0.785 0.684 0.143  0.068  0.092  421 TYR III CD1 
10903 C CD2 . TYR I 92  ? 0.813 0.843 0.688 0.176  0.038  0.088  421 TYR III CD2 
10904 C CE1 . TYR I 92  ? 0.839 0.793 0.691 0.158  0.078  0.109  421 TYR III CE1 
10905 C CE2 . TYR I 92  ? 0.875 0.872 0.712 0.194  0.045  0.105  421 TYR III CE2 
10906 C CZ  . TYR I 92  ? 0.887 0.845 0.711 0.185  0.066  0.117  421 TYR III CZ  
10907 O OH  . TYR I 92  ? 0.896 0.821 0.680 0.204  0.075  0.136  421 TYR III OH  
10908 N N   . ASN I 93  ? 0.591 0.706 0.581 0.086  0.040  0.040  422 ASN III N   
10909 C CA  . ASN I 93  ? 0.558 0.706 0.571 0.080  0.036  0.031  422 ASN III CA  
10910 C C   . ASN I 93  ? 0.546 0.697 0.569 0.060  0.039  0.025  422 ASN III C   
10911 O O   . ASN I 93  ? 0.536 0.689 0.567 0.058  0.045  0.019  422 ASN III O   
10912 C CB  . ASN I 93  ? 0.535 0.720 0.558 0.084  0.022  0.030  422 ASN III CB  
10913 C CG  . ASN I 93  ? 0.537 0.728 0.556 0.107  0.016  0.032  422 ASN III CG  
10914 O OD1 . ASN I 93  ? 0.539 0.748 0.572 0.116  0.016  0.029  422 ASN III OD1 
10915 N ND2 . ASN I 93  ? 0.555 0.728 0.550 0.119  0.011  0.039  422 ASN III ND2 
10916 N N   . TYR I 94  ? 0.521 0.674 0.543 0.048  0.036  0.027  423 TYR III N   
10917 C CA  . TYR I 94  ? 0.516 0.673 0.546 0.031  0.038  0.022  423 TYR III CA  
10918 C C   . TYR I 94  ? 0.515 0.655 0.536 0.024  0.038  0.025  423 TYR III C   
10919 O O   . TYR I 94  ? 0.508 0.654 0.523 0.025  0.031  0.027  423 TYR III O   
10920 C CB  . TYR I 94  ? 0.492 0.681 0.537 0.024  0.031  0.020  423 TYR III CB  
10921 C CG  . TYR I 94  ? 0.474 0.665 0.524 0.010  0.033  0.018  423 TYR III CG  
10922 C CD1 . TYR I 94  ? 0.505 0.699 0.557 0.010  0.038  0.014  423 TYR III CD1 
10923 C CD2 . TYR I 94  ? 0.457 0.643 0.506 -0.000 0.029  0.019  423 TYR III CD2 
10924 C CE1 . TYR I 94  ? 0.493 0.689 0.546 0.000  0.039  0.012  423 TYR III CE1 
10925 C CE2 . TYR I 94  ? 0.455 0.642 0.507 -0.010 0.030  0.018  423 TYR III CE2 
10926 C CZ  . TYR I 94  ? 0.482 0.673 0.535 -0.010 0.035  0.015  423 TYR III CZ  
10927 O OH  . TYR I 94  ? 0.447 0.638 0.499 -0.017 0.034  0.015  423 TYR III OH  
10928 N N   . LYS I 95  ? 0.528 0.649 0.549 0.018  0.047  0.023  424 LYS III N   
10929 C CA  . LYS I 95  ? 0.532 0.638 0.547 0.012  0.052  0.025  424 LYS III CA  
10930 C C   . LYS I 95  ? 0.503 0.616 0.530 -0.001 0.050  0.019  424 LYS III C   
10931 O O   . LYS I 95  ? 0.483 0.596 0.521 -0.005 0.052  0.013  424 LYS III O   
10932 C CB  . LYS I 95  ? 0.573 0.651 0.584 0.016  0.064  0.029  424 LYS III CB  
10933 C CG  . LYS I 95  ? 0.600 0.666 0.608 0.011  0.074  0.033  424 LYS III CG  
10934 C CD  . LYS I 95  ? 0.614 0.684 0.603 0.017  0.069  0.038  424 LYS III CD  
10935 C CE  . LYS I 95  ? 0.635 0.686 0.613 0.019  0.083  0.046  424 LYS III CE  
10936 N NZ  . LYS I 95  ? 0.646 0.702 0.602 0.026  0.077  0.047  424 LYS III NZ  
10937 N N   . LEU I 96  ? 0.485 0.604 0.510 -0.005 0.045  0.019  425 LEU III N   
10938 C CA  . LEU I 96  ? 0.479 0.600 0.513 -0.015 0.043  0.014  425 LEU III CA  
10939 C C   . LEU I 96  ? 0.478 0.585 0.513 -0.016 0.053  0.014  425 LEU III C   
10940 O O   . LEU I 96  ? 0.504 0.601 0.527 -0.010 0.059  0.020  425 LEU III O   
10941 C CB  . LEU I 96  ? 0.473 0.605 0.506 -0.018 0.034  0.014  425 LEU III CB  
10942 C CG  . LEU I 96  ? 0.469 0.617 0.508 -0.021 0.027  0.015  425 LEU III CG  
10943 C CD1 . LEU I 96  ? 0.489 0.641 0.530 -0.027 0.018  0.015  425 LEU III CD1 
10944 C CD2 . LEU I 96  ? 0.469 0.622 0.514 -0.024 0.029  0.013  425 LEU III CD2 
10945 N N   . PRO I 97  ? 0.449 0.558 0.499 -0.023 0.055  0.008  426 PRO III N   
10946 C CA  . PRO I 97  ? 0.463 0.565 0.523 -0.026 0.065  0.007  426 PRO III CA  
10947 C C   . PRO I 97  ? 0.480 0.584 0.532 -0.024 0.064  0.009  426 PRO III C   
10948 O O   . PRO I 97  ? 0.446 0.556 0.490 -0.023 0.053  0.008  426 PRO III O   
10949 C CB  . PRO I 97  ? 0.456 0.567 0.537 -0.033 0.061  -0.003 426 PRO III CB  
10950 C CG  . PRO I 97  ? 0.418 0.541 0.492 -0.032 0.047  -0.005 426 PRO III CG  
10951 C CD  . PRO I 97  ? 0.444 0.565 0.504 -0.027 0.047  0.001  426 PRO III CD  
10952 N N   . ASP I 98  ? 0.516 0.613 0.570 -0.023 0.077  0.011  427 ASP III N   
10953 C CA  . ASP I 98  ? 0.560 0.658 0.603 -0.018 0.078  0.011  427 ASP III CA  
10954 C C   . ASP I 98  ? 0.515 0.625 0.573 -0.022 0.068  0.003  427 ASP III C   
10955 O O   . ASP I 98  ? 0.523 0.632 0.569 -0.017 0.062  0.001  427 ASP III O   
10956 C CB  . ASP I 98  ? 0.621 0.711 0.661 -0.014 0.097  0.017  427 ASP III CB  
10957 C CG  . ASP I 98  ? 0.701 0.787 0.713 -0.003 0.097  0.019  427 ASP III CG  
10958 O OD1 . ASP I 98  ? 0.758 0.837 0.746 0.005  0.090  0.023  427 ASP III OD1 
10959 O OD2 . ASP I 98  ? 0.768 0.859 0.784 -0.000 0.101  0.015  427 ASP III OD2 
10960 N N   . ASP I 99  ? 0.481 0.599 0.561 -0.028 0.065  -0.003 428 ASP III N   
10961 C CA  . ASP I 99  ? 0.470 0.600 0.564 -0.029 0.055  -0.011 428 ASP III CA  
10962 C C   . ASP I 99  ? 0.466 0.598 0.553 -0.030 0.041  -0.012 428 ASP III C   
10963 O O   . ASP I 99  ? 0.495 0.636 0.592 -0.031 0.033  -0.017 428 ASP III O   
10964 C CB  . ASP I 99  ? 0.454 0.594 0.577 -0.033 0.062  -0.019 428 ASP III CB  
10965 C CG  . ASP I 99  ? 0.447 0.590 0.585 -0.040 0.060  -0.024 428 ASP III CG  
10966 O OD1 . ASP I 99  ? 0.462 0.597 0.586 -0.040 0.058  -0.019 428 ASP III OD1 
10967 O OD2 . ASP I 99  ? 0.480 0.636 0.645 -0.044 0.058  -0.034 428 ASP III OD2 
10968 N N   . PHE I 100 ? 0.449 0.576 0.520 -0.030 0.038  -0.006 429 PHE III N   
10969 C CA  . PHE I 100 ? 0.454 0.586 0.519 -0.032 0.029  -0.004 429 PHE III CA  
10970 C C   . PHE I 100 ? 0.458 0.592 0.524 -0.031 0.019  -0.005 429 PHE III C   
10971 O O   . PHE I 100 ? 0.493 0.619 0.554 -0.029 0.017  -0.004 429 PHE III O   
10972 C CB  . PHE I 100 ? 0.476 0.605 0.528 -0.031 0.027  0.002  429 PHE III CB  
10973 C CG  . PHE I 100 ? 0.471 0.608 0.522 -0.034 0.021  0.006  429 PHE III CG  
10974 C CD1 . PHE I 100 ? 0.475 0.620 0.528 -0.034 0.022  0.005  429 PHE III CD1 
10975 C CD2 . PHE I 100 ? 0.514 0.650 0.561 -0.037 0.015  0.010  429 PHE III CD2 
10976 C CE1 . PHE I 100 ? 0.490 0.643 0.539 -0.035 0.019  0.010  429 PHE III CE1 
10977 C CE2 . PHE I 100 ? 0.508 0.652 0.556 -0.041 0.012  0.016  429 PHE III CE2 
10978 C CZ  . PHE I 100 ? 0.505 0.658 0.553 -0.039 0.015  0.017  429 PHE III CZ  
10979 N N   . THR I 101 ? 0.468 0.608 0.535 -0.031 0.014  -0.005 430 THR III N   
10980 C CA  . THR I 101 ? 0.450 0.588 0.510 -0.029 0.005  -0.002 430 THR III CA  
10981 C C   . THR I 101 ? 0.437 0.577 0.486 -0.032 0.004  0.007  430 THR III C   
10982 O O   . THR I 101 ? 0.453 0.602 0.500 -0.030 0.005  0.005  430 THR III O   
10983 C CB  . THR I 101 ? 0.448 0.594 0.516 -0.024 -0.001 -0.009 430 THR III CB  
10984 O OG1 . THR I 101 ? 0.440 0.589 0.525 -0.023 0.002  -0.017 430 THR III OG1 
10985 C CG2 . THR I 101 ? 0.467 0.608 0.525 -0.018 -0.010 -0.004 430 THR III CG2 
10986 N N   . GLY I 102 ? 0.444 0.576 0.489 -0.035 0.002  0.015  431 GLY III N   
10987 C CA  . GLY I 102 ? 0.497 0.634 0.538 -0.040 0.004  0.025  431 GLY III CA  
10988 C C   . GLY I 102 ? 0.491 0.621 0.536 -0.047 0.003  0.029  431 GLY III C   
10989 O O   . GLY I 102 ? 0.511 0.629 0.558 -0.047 -0.002 0.025  431 GLY III O   
10990 N N   . CYS I 103 ? 0.538 0.677 0.587 -0.053 0.006  0.037  432 CYS III N   
10991 C CA  . CYS I 103 ? 0.559 0.696 0.620 -0.062 0.003  0.040  432 CYS III CA  
10992 C C   . CYS I 103 ? 0.522 0.679 0.593 -0.065 0.007  0.040  432 CYS III C   
10993 O O   . CYS I 103 ? 0.542 0.713 0.610 -0.060 0.014  0.042  432 CYS III O   
10994 C CB  . CYS I 103 ? 0.612 0.740 0.675 -0.070 0.005  0.052  432 CYS III CB  
10995 S SG  . CYS I 103 ? 0.692 0.796 0.741 -0.063 0.000  0.055  432 CYS III SG  
10996 N N   . VAL I 104 ? 0.518 0.676 0.600 -0.069 0.000  0.035  433 VAL III N   
10997 C CA  . VAL I 104 ? 0.506 0.684 0.600 -0.070 -0.000 0.033  433 VAL III CA  
10998 C C   . VAL I 104 ? 0.511 0.696 0.628 -0.083 -0.004 0.036  433 VAL III C   
10999 O O   . VAL I 104 ? 0.508 0.676 0.629 -0.089 -0.014 0.031  433 VAL III O   
11000 C CB  . VAL I 104 ? 0.526 0.703 0.612 -0.061 -0.006 0.023  433 VAL III CB  
11001 C CG1 . VAL I 104 ? 0.526 0.724 0.623 -0.059 -0.009 0.021  433 VAL III CG1 
11002 C CG2 . VAL I 104 ? 0.522 0.692 0.591 -0.051 0.001  0.022  433 VAL III CG2 
11003 N N   . ILE I 105 ? 0.512 0.720 0.646 -0.088 0.003  0.044  434 ILE III N   
11004 C CA  . ILE I 105 ? 0.505 0.725 0.670 -0.103 0.002  0.048  434 ILE III CA  
11005 C C   . ILE I 105 ? 0.496 0.750 0.681 -0.101 0.001  0.043  434 ILE III C   
11006 O O   . ILE I 105 ? 0.482 0.750 0.658 -0.090 0.010  0.045  434 ILE III O   
11007 C CB  . ILE I 105 ? 0.514 0.732 0.683 -0.112 0.016  0.065  434 ILE III CB  
11008 C CG1 . ILE I 105 ? 0.538 0.721 0.684 -0.111 0.015  0.069  434 ILE III CG1 
11009 C CG2 . ILE I 105 ? 0.517 0.748 0.724 -0.130 0.019  0.071  434 ILE III CG2 
11010 C CD1 . ILE I 105 ? 0.569 0.747 0.705 -0.112 0.028  0.087  434 ILE III CD1 
11011 N N   . ALA I 106 ? 0.496 0.761 0.708 -0.110 -0.010 0.035  435 ALA III N   
11012 C CA  . ALA I 106 ? 0.493 0.795 0.732 -0.108 -0.014 0.030  435 ALA III CA  
11013 C C   . ALA I 106 ? 0.488 0.806 0.772 -0.128 -0.018 0.030  435 ALA III C   
11014 O O   . ALA I 106 ? 0.477 0.770 0.767 -0.141 -0.023 0.030  435 ALA III O   
11015 C CB  . ALA I 106 ? 0.500 0.801 0.723 -0.092 -0.029 0.016  435 ALA III CB  
11016 N N   . TRP I 107 ? 0.490 0.849 0.807 -0.129 -0.015 0.030  436 TRP III N   
11017 C CA  . TRP I 107 ? 0.493 0.877 0.863 -0.149 -0.020 0.027  436 TRP III CA  
11018 C C   . TRP I 107 ? 0.485 0.915 0.883 -0.140 -0.027 0.017  436 TRP III C   
11019 O O   . TRP I 107 ? 0.468 0.914 0.849 -0.122 -0.019 0.020  436 TRP III O   
11020 C CB  . TRP I 107 ? 0.500 0.887 0.893 -0.167 0.002  0.046  436 TRP III CB  
11021 C CG  . TRP I 107 ? 0.499 0.912 0.889 -0.159 0.025  0.061  436 TRP III CG  
11022 C CD1 . TRP I 107 ? 0.510 0.970 0.942 -0.163 0.036  0.065  436 TRP III CD1 
11023 C CD2 . TRP I 107 ? 0.495 0.891 0.839 -0.144 0.040  0.071  436 TRP III CD2 
11024 N NE1 . TRP I 107 ? 0.498 0.969 0.909 -0.151 0.057  0.077  436 TRP III NE1 
11025 C CE2 . TRP I 107 ? 0.486 0.920 0.844 -0.139 0.059  0.081  436 TRP III CE2 
11026 C CE3 . TRP I 107 ? 0.486 0.844 0.782 -0.133 0.038  0.072  436 TRP III CE3 
11027 C CZ2 . TRP I 107 ? 0.476 0.904 0.796 -0.123 0.075  0.090  436 TRP III CZ2 
11028 C CZ3 . TRP I 107 ? 0.501 0.856 0.765 -0.120 0.053  0.081  436 TRP III CZ3 
11029 C CH2 . TRP I 107 ? 0.499 0.888 0.773 -0.114 0.070  0.089  436 TRP III CH2 
11030 N N   . ASN I 108 ? 0.498 0.949 0.938 -0.151 -0.045 0.003  437 ASN III N   
11031 C CA  . ASN I 108 ? 0.490 0.991 0.969 -0.145 -0.055 -0.008 437 ASN III CA  
11032 C C   . ASN I 108 ? 0.476 1.016 0.988 -0.151 -0.030 0.008  437 ASN III C   
11033 O O   . ASN I 108 ? 0.452 0.991 0.991 -0.173 -0.013 0.021  437 ASN III O   
11034 C CB  . ASN I 108 ? 0.502 1.016 1.026 -0.162 -0.079 -0.027 437 ASN III CB  
11035 C CG  . ASN I 108 ? 0.504 1.071 1.065 -0.152 -0.095 -0.041 437 ASN III CG  
11036 O OD1 . ASN I 108 ? 0.513 1.124 1.116 -0.157 -0.081 -0.034 437 ASN III OD1 
11037 N ND2 . ASN I 108 ? 0.540 1.104 1.081 -0.135 -0.123 -0.061 437 ASN III ND2 
11038 N N   . SER I 109 ? 0.477 1.048 0.985 -0.130 -0.026 0.007  438 SER III N   
11039 C CA  . SER I 109 ? 0.498 1.109 1.034 -0.129 -0.002 0.020  438 SER III CA  
11040 C C   . SER I 109 ? 0.504 1.173 1.089 -0.122 -0.014 0.007  438 SER III C   
11041 O O   . SER I 109 ? 0.511 1.215 1.108 -0.109 0.002  0.013  438 SER III O   
11042 C CB  . SER I 109 ? 0.490 1.084 0.976 -0.109 0.016  0.031  438 SER III CB  
11043 O OG  . SER I 109 ? 0.500 1.086 0.952 -0.083 0.000  0.019  438 SER III OG  
11044 N N   . ASN I 110 ? 0.502 1.182 1.116 -0.129 -0.041 -0.012 439 ASN III N   
11045 C CA  . ASN I 110 ? 0.500 1.238 1.164 -0.120 -0.058 -0.027 439 ASN III CA  
11046 C C   . ASN I 110 ? 0.480 1.273 1.208 -0.134 -0.034 -0.017 439 ASN III C   
11047 O O   . ASN I 110 ? 0.442 1.280 1.189 -0.115 -0.032 -0.020 439 ASN III O   
11048 C CB  . ASN I 110 ? 0.507 1.249 1.198 -0.130 -0.092 -0.050 439 ASN III CB  
11049 C CG  . ASN I 110 ? 0.510 1.302 1.230 -0.110 -0.118 -0.070 439 ASN III CG  
11050 O OD1 . ASN I 110 ? 0.500 1.303 1.193 -0.080 -0.117 -0.068 439 ASN III OD1 
11051 N ND2 . ASN I 110 ? 0.514 1.334 1.288 -0.125 -0.142 -0.090 439 ASN III ND2 
11052 N N   . ASN I 111 ? 0.498 1.283 1.252 -0.164 -0.015 -0.003 440 ASN III N   
11053 C CA  . ASN I 111 ? 0.533 1.370 1.353 -0.182 0.011  0.009  440 ASN III CA  
11054 C C   . ASN I 111 ? 0.512 1.365 1.308 -0.161 0.041  0.026  440 ASN III C   
11055 O O   . ASN I 111 ? 0.513 1.423 1.362 -0.164 0.058  0.030  440 ASN III O   
11056 C CB  . ASN I 111 ? 0.572 1.389 1.424 -0.219 0.024  0.021  440 ASN III CB  
11057 C CG  . ASN I 111 ? 0.604 1.420 1.500 -0.239 -0.008 -0.001 440 ASN III CG  
11058 O OD1 . ASN I 111 ? 0.606 1.421 1.489 -0.224 -0.042 -0.025 440 ASN III OD1 
11059 N ND2 . ASN I 111 ? 0.655 1.471 1.603 -0.274 0.003  0.007  440 ASN III ND2 
11060 N N   . LEU I 112 ? 0.525 1.332 1.246 -0.142 0.048  0.033  441 LEU III N   
11061 C CA  . LEU I 112 ? 0.542 1.359 1.234 -0.121 0.075  0.046  441 LEU III CA  
11062 C C   . LEU I 112 ? 0.535 1.359 1.199 -0.086 0.060  0.033  441 LEU III C   
11063 O O   . LEU I 112 ? 0.535 1.395 1.208 -0.069 0.077  0.036  441 LEU III O   
11064 C CB  . LEU I 112 ? 0.558 1.318 1.187 -0.122 0.092  0.063  441 LEU III CB  
11065 C CG  . LEU I 112 ? 0.580 1.330 1.227 -0.151 0.114  0.083  441 LEU III CG  
11066 C CD1 . LEU I 112 ? 0.601 1.298 1.180 -0.145 0.128  0.098  441 LEU III CD1 
11067 C CD2 . LEU I 112 ? 0.593 1.401 1.297 -0.160 0.142  0.095  441 LEU III CD2 
11068 N N   . ASP I 113 ? 0.533 1.323 1.162 -0.075 0.032  0.019  442 ASP III N   
11069 C CA  . ASP I 113 ? 0.538 1.313 1.120 -0.041 0.022  0.012  442 ASP III CA  
11070 C C   . ASP I 113 ? 0.546 1.353 1.153 -0.024 -0.005 -0.006 442 ASP III C   
11071 O O   . ASP I 113 ? 0.519 1.309 1.087 0.004  -0.015 -0.011 442 ASP III O   
11072 C CB  . ASP I 113 ? 0.549 1.256 1.064 -0.038 0.015  0.013  442 ASP III CB  
11073 C CG  . ASP I 113 ? 0.568 1.242 1.046 -0.043 0.041  0.029  442 ASP III CG  
11074 O OD1 . ASP I 113 ? 0.537 1.234 1.017 -0.034 0.063  0.037  442 ASP III OD1 
11075 O OD2 . ASP I 113 ? 0.615 1.243 1.061 -0.054 0.037  0.033  442 ASP III OD2 
11076 N N   . SER I 114 ? 0.598 1.449 1.268 -0.039 -0.019 -0.016 443 SER III N   
11077 C CA  . SER I 114 ? 0.631 1.520 1.328 -0.021 -0.048 -0.035 443 SER III CA  
11078 C C   . SER I 114 ? 0.628 1.594 1.400 -0.022 -0.038 -0.037 443 SER III C   
11079 O O   . SER I 114 ? 0.633 1.620 1.445 -0.047 -0.014 -0.026 443 SER III O   
11080 C CB  . SER I 114 ? 0.657 1.531 1.360 -0.033 -0.079 -0.050 443 SER III CB  
11081 O OG  . SER I 114 ? 0.673 1.588 1.450 -0.063 -0.082 -0.056 443 SER III OG  
11082 N N   . LYS I 115 ? 0.624 1.629 1.413 0.007  -0.053 -0.049 444 LYS III N   
11083 C CA  . LYS I 115 ? 0.620 1.704 1.482 0.011  -0.044 -0.052 444 LYS III CA  
11084 C C   . LYS I 115 ? 0.619 1.748 1.523 0.024  -0.081 -0.075 444 LYS III C   
11085 O O   . LYS I 115 ? 0.612 1.707 1.468 0.044  -0.110 -0.085 444 LYS III O   
11086 C CB  . LYS I 115 ? 0.645 1.737 1.481 0.042  -0.022 -0.044 444 LYS III CB  
11087 C CG  . LYS I 115 ? 0.671 1.840 1.578 0.043  -0.001 -0.042 444 LYS III CG  
11088 C CD  . LYS I 115 ? 0.677 1.860 1.564 0.082  0.009  -0.042 444 LYS III CD  
11089 C CE  . LYS I 115 ? 0.670 1.780 1.469 0.097  0.025  -0.031 444 LYS III CE  
11090 N NZ  . LYS I 115 ? 0.680 1.804 1.464 0.134  0.036  -0.032 444 LYS III NZ  
11091 N N   . VAL I 116 ? 0.632 1.838 1.623 0.014  -0.081 -0.083 445 VAL III N   
11092 C CA  . VAL I 116 ? 0.632 1.898 1.672 0.033  -0.115 -0.106 445 VAL III CA  
11093 C C   . VAL I 116 ? 0.636 1.895 1.627 0.082  -0.120 -0.106 445 VAL III C   
11094 O O   . VAL I 116 ? 0.640 1.900 1.616 0.095  -0.088 -0.092 445 VAL III O   
11095 C CB  . VAL I 116 ? 0.633 1.987 1.783 0.012  -0.108 -0.113 445 VAL III CB  
11096 C CG1 . VAL I 116 ? 0.635 1.988 1.833 -0.036 -0.110 -0.116 445 VAL III CG1 
11097 C CG2 . VAL I 116 ? 0.620 2.012 1.796 0.016  -0.064 -0.096 445 VAL III CG2 
11098 N N   . GLY I 117 ? 0.629 1.873 1.586 0.109  -0.156 -0.120 446 GLY III N   
11099 C CA  . GLY I 117 ? 0.646 1.871 1.548 0.156  -0.163 -0.118 446 GLY III CA  
11100 C C   . GLY I 117 ? 0.666 1.801 1.472 0.164  -0.149 -0.101 446 GLY III C   
11101 O O   . GLY I 117 ? 0.701 1.808 1.455 0.202  -0.156 -0.099 446 GLY III O   
11102 N N   . GLY I 118 ? 0.643 1.732 1.425 0.131  -0.134 -0.092 447 GLY III N   
11103 C CA  . GLY I 118 ? 0.637 1.642 1.333 0.135  -0.127 -0.079 447 GLY III CA  
11104 C C   . GLY I 118 ? 0.627 1.605 1.295 0.134  -0.090 -0.062 447 GLY III C   
11105 O O   . GLY I 118 ? 0.605 1.612 1.286 0.157  -0.078 -0.061 447 GLY III O   
11106 N N   . ASN I 119 ? 0.619 1.544 1.249 0.111  -0.074 -0.051 448 ASN III N   
11107 C CA  . ASN I 119 ? 0.611 1.500 1.201 0.113  -0.043 -0.036 448 ASN III CA  
11108 C C   . ASN I 119 ? 0.617 1.441 1.133 0.138  -0.049 -0.033 448 ASN III C   
11109 O O   . ASN I 119 ? 0.583 1.360 1.060 0.130  -0.061 -0.032 448 ASN III O   
11110 C CB  . ASN I 119 ? 0.586 1.455 1.177 0.077  -0.024 -0.026 448 ASN III CB  
11111 C CG  . ASN I 119 ? 0.569 1.403 1.117 0.080  0.005  -0.013 448 ASN III CG  
11112 O OD1 . ASN I 119 ? 0.562 1.396 1.091 0.107  0.014  -0.013 448 ASN III OD1 
11113 N ND2 . ASN I 119 ? 0.585 1.388 1.116 0.054  0.018  -0.003 448 ASN III ND2 
11114 N N   . TYR I 120 ? 0.642 1.465 1.141 0.168  -0.040 -0.032 449 TYR III N   
11115 C CA  . TYR I 120 ? 0.663 1.426 1.098 0.194  -0.044 -0.028 449 TYR III CA  
11116 C C   . TYR I 120 ? 0.659 1.380 1.057 0.190  -0.018 -0.020 449 TYR III C   
11117 O O   . TYR I 120 ? 0.676 1.346 1.026 0.209  -0.017 -0.017 449 TYR III O   
11118 C CB  . TYR I 120 ? 0.696 1.482 1.137 0.233  -0.058 -0.035 449 TYR III CB  
11119 C CG  . TYR I 120 ? 0.733 1.552 1.198 0.240  -0.089 -0.045 449 TYR III CG  
11120 C CD1 . TYR I 120 ? 0.741 1.632 1.276 0.230  -0.098 -0.055 449 TYR III CD1 
11121 C CD2 . TYR I 120 ? 0.762 1.540 1.180 0.260  -0.111 -0.044 449 TYR III CD2 
11122 C CE1 . TYR I 120 ? 0.755 1.680 1.315 0.238  -0.130 -0.067 449 TYR III CE1 
11123 C CE2 . TYR I 120 ? 0.794 1.603 1.229 0.271  -0.142 -0.055 449 TYR III CE2 
11124 C CZ  . TYR I 120 ? 0.789 1.672 1.296 0.259  -0.154 -0.068 449 TYR III CZ  
11125 O OH  . TYR I 120 ? 0.773 1.689 1.299 0.270  -0.187 -0.082 449 TYR III OH  
11126 N N   . ASN I 121 ? 0.618 1.353 1.035 0.164  0.002  -0.015 450 ASN III N   
11127 C CA  . ASN I 121 ? 0.611 1.309 0.992 0.161  0.025  -0.009 450 ASN III CA  
11128 C C   . ASN I 121 ? 0.581 1.212 0.911 0.149  0.021  -0.004 450 ASN III C   
11129 O O   . ASN I 121 ? 0.586 1.178 0.879 0.156  0.032  -0.003 450 ASN III O   
11130 C CB  . ASN I 121 ? 0.616 1.348 1.026 0.140  0.048  -0.003 450 ASN III CB  
11131 C CG  . ASN I 121 ? 0.657 1.449 1.108 0.156  0.061  -0.006 450 ASN III CG  
11132 O OD1 . ASN I 121 ? 0.715 1.515 1.164 0.186  0.056  -0.013 450 ASN III OD1 
11133 N ND2 . ASN I 121 ? 0.643 1.477 1.133 0.136  0.079  -0.000 450 ASN III ND2 
11134 N N   . TYR I 122 ? 0.544 1.165 0.874 0.131  0.006  -0.004 451 TYR III N   
11135 C CA  . TYR I 122 ? 0.546 1.109 0.833 0.119  0.004  0.001  451 TYR III CA  
11136 C C   . TYR I 122 ? 0.540 1.065 0.790 0.140  -0.009 -0.000 451 TYR III C   
11137 O O   . TYR I 122 ? 0.537 1.078 0.796 0.152  -0.028 -0.004 451 TYR III O   
11138 C CB  . TYR I 122 ? 0.515 1.082 0.817 0.090  -0.002 0.002  451 TYR III CB  
11139 C CG  . TYR I 122 ? 0.485 1.076 0.814 0.067  0.016  0.008  451 TYR III CG  
11140 C CD1 . TYR I 122 ? 0.480 1.042 0.781 0.060  0.033  0.014  451 TYR III CD1 
11141 C CD2 . TYR I 122 ? 0.474 1.115 0.856 0.054  0.015  0.006  451 TYR III CD2 
11142 C CE1 . TYR I 122 ? 0.456 1.035 0.775 0.041  0.050  0.022  451 TYR III CE1 
11143 C CE2 . TYR I 122 ? 0.464 1.123 0.868 0.033  0.034  0.015  451 TYR III CE2 
11144 C CZ  . TYR I 122 ? 0.463 1.089 0.832 0.028  0.052  0.024  451 TYR III CZ  
11145 O OH  . TYR I 122 ? 0.461 1.102 0.847 0.009  0.071  0.034  451 TYR III OH  
11146 N N   . LEU I 123 ? 0.540 1.014 0.749 0.145  0.000  0.004  452 LEU III N   
11147 C CA  . LEU I 123 ? 0.558 0.987 0.729 0.165  -0.006 0.006  452 LEU III CA  
11148 C C   . LEU I 123 ? 0.609 0.992 0.749 0.148  -0.006 0.011  452 LEU III C   
11149 O O   . LEU I 123 ? 0.608 0.988 0.752 0.125  0.003  0.012  452 LEU III O   
11150 C CB  . LEU I 123 ? 0.561 0.969 0.718 0.184  0.007  0.005  452 LEU III CB  
11151 C CG  . LEU I 123 ? 0.557 1.010 0.743 0.204  0.009  -0.000 452 LEU III CG  
11152 C CD1 . LEU I 123 ? 0.570 0.993 0.736 0.224  0.021  -0.003 452 LEU III CD1 
11153 C CD2 . LEU I 123 ? 0.572 1.056 0.775 0.223  -0.009 -0.002 452 LEU III CD2 
11154 N N   . TYR I 124 ? 0.651 1.001 0.762 0.161  -0.014 0.015  453 TYR III N   
11155 C CA  . TYR I 124 ? 0.650 0.952 0.728 0.151  -0.010 0.021  453 TYR III CA  
11156 C C   . TYR I 124 ? 0.676 0.935 0.721 0.173  -0.006 0.028  453 TYR III C   
11157 O O   . TYR I 124 ? 0.701 0.968 0.745 0.198  -0.014 0.029  453 TYR III O   
11158 C CB  . TYR I 124 ? 0.652 0.961 0.727 0.141  -0.023 0.021  453 TYR III CB  
11159 C CG  . TYR I 124 ? 0.679 0.999 0.746 0.163  -0.041 0.020  453 TYR III CG  
11160 C CD1 . TYR I 124 ? 0.689 1.060 0.790 0.168  -0.056 0.012  453 TYR III CD1 
11161 C CD2 . TYR I 124 ? 0.711 0.993 0.738 0.179  -0.043 0.028  453 TYR III CD2 
11162 C CE1 . TYR I 124 ? 0.711 1.095 0.805 0.190  -0.076 0.009  453 TYR III CE1 
11163 C CE2 . TYR I 124 ? 0.759 1.051 0.772 0.202  -0.061 0.028  453 TYR III CE2 
11164 C CZ  . TYR I 124 ? 0.760 1.103 0.806 0.209  -0.079 0.017  453 TYR III CZ  
11165 O OH  . TYR I 124 ? 0.806 1.161 0.839 0.234  -0.100 0.015  453 TYR III OH  
11166 N N   . ARG I 125 ? 0.647 0.861 0.670 0.164  0.006  0.033  454 ARG III N   
11167 C CA  . ARG I 125 ? 0.681 0.848 0.675 0.181  0.013  0.043  454 ARG III CA  
11168 C C   . ARG I 125 ? 0.707 0.862 0.674 0.190  0.003  0.052  454 ARG III C   
11169 O O   . ARG I 125 ? 0.689 0.845 0.652 0.173  0.002  0.052  454 ARG III O   
11170 C CB  . ARG I 125 ? 0.660 0.786 0.646 0.166  0.029  0.044  454 ARG III CB  
11171 C CG  . ARG I 125 ? 0.704 0.780 0.667 0.181  0.039  0.053  454 ARG III CG  
11172 C CD  . ARG I 125 ? 0.716 0.758 0.682 0.164  0.053  0.050  454 ARG III CD  
11173 N NE  . ARG I 125 ? 0.701 0.762 0.688 0.160  0.054  0.035  454 ARG III NE  
11174 C CZ  . ARG I 125 ? 0.707 0.762 0.697 0.177  0.056  0.030  454 ARG III CZ  
11175 N NH1 . ARG I 125 ? 0.769 0.799 0.746 0.200  0.056  0.038  454 ARG III NH1 
11176 N NH2 . ARG I 125 ? 0.681 0.756 0.687 0.172  0.057  0.016  454 ARG III NH2 
11177 N N   . LEU I 126 ? 0.765 0.912 0.714 0.218  -0.003 0.059  455 LEU III N   
11178 C CA  . LEU I 126 ? 0.814 0.955 0.734 0.234  -0.015 0.066  455 LEU III CA  
11179 C C   . LEU I 126 ? 0.855 0.937 0.735 0.242  0.000  0.083  455 LEU III C   
11180 O O   . LEU I 126 ? 0.876 0.945 0.727 0.244  -0.001 0.091  455 LEU III O   
11181 C CB  . LEU I 126 ? 0.852 1.023 0.776 0.263  -0.033 0.064  455 LEU III CB  
11182 C CG  . LEU I 126 ? 0.903 1.069 0.792 0.286  -0.049 0.071  455 LEU III CG  
11183 C CD1 . LEU I 126 ? 0.878 1.061 0.763 0.270  -0.059 0.064  455 LEU III CD1 
11184 C CD2 . LEU I 126 ? 0.921 1.123 0.821 0.315  -0.069 0.065  455 LEU III CD2 
11185 N N   . PHE I 127 ? 0.859 0.907 0.738 0.246  0.016  0.089  456 PHE III N   
11186 C CA  . PHE I 127 ? 0.926 0.913 0.774 0.253  0.033  0.106  456 PHE III CA  
11187 C C   . PHE I 127 ? 0.879 0.842 0.748 0.228  0.052  0.102  456 PHE III C   
11188 O O   . PHE I 127 ? 0.830 0.809 0.726 0.222  0.051  0.088  456 PHE III O   
11189 C CB  . PHE I 127 ? 0.987 0.951 0.817 0.286  0.032  0.117  456 PHE III CB  
11190 C CG  . PHE I 127 ? 1.028 1.020 0.841 0.315  0.010  0.119  456 PHE III CG  
11191 C CD1 . PHE I 127 ? 1.063 1.045 0.837 0.325  0.006  0.130  456 PHE III CD1 
11192 C CD2 . PHE I 127 ? 1.046 1.077 0.881 0.333  -0.006 0.108  456 PHE III CD2 
11193 C CE1 . PHE I 127 ? 1.079 1.090 0.837 0.353  -0.018 0.129  456 PHE III CE1 
11194 C CE2 . PHE I 127 ? 1.079 1.141 0.903 0.359  -0.029 0.107  456 PHE III CE2 
11195 C CZ  . PHE I 127 ? 1.095 1.146 0.880 0.370  -0.036 0.118  456 PHE III CZ  
11196 N N   . ARG I 128 ? 0.905 0.830 0.759 0.216  0.068  0.113  457 ARG III N   
11197 C CA  . ARG I 128 ? 0.906 0.801 0.779 0.195  0.086  0.110  457 ARG III CA  
11198 C C   . ARG I 128 ? 0.966 0.811 0.816 0.193  0.106  0.130  457 ARG III C   
11199 O O   . ARG I 128 ? 0.992 0.839 0.816 0.197  0.106  0.141  457 ARG III O   
11200 C CB  . ARG I 128 ? 0.843 0.771 0.744 0.167  0.083  0.093  457 ARG III CB  
11201 C CG  . ARG I 128 ? 0.822 0.731 0.747 0.148  0.094  0.084  457 ARG III CG  
11202 C CD  . ARG I 128 ? 0.780 0.726 0.730 0.126  0.087  0.067  457 ARG III CD  
11203 N NE  . ARG I 128 ? 0.777 0.713 0.748 0.114  0.092  0.053  457 ARG III NE  
11204 C CZ  . ARG I 128 ? 0.807 0.721 0.791 0.096  0.103  0.050  457 ARG III CZ  
11205 N NH1 . ARG I 128 ? 0.836 0.733 0.813 0.087  0.113  0.063  457 ARG III NH1 
11206 N NH2 . ARG I 128 ? 0.806 0.714 0.809 0.087  0.103  0.034  457 ARG III NH2 
11207 N N   . LYS I 129 ? 1.017 0.820 0.878 0.187  0.121  0.133  458 LYS III N   
11208 C CA  . LYS I 129 ? 1.103 0.853 0.947 0.184  0.144  0.154  458 LYS III CA  
11209 C C   . LYS I 129 ? 1.062 0.822 0.917 0.158  0.155  0.154  458 LYS III C   
11210 O O   . LYS I 129 ? 1.095 0.825 0.928 0.160  0.173  0.174  458 LYS III O   
11211 C CB  . LYS I 129 ? 1.171 0.873 1.030 0.183  0.157  0.155  458 LYS III CB  
11212 C CG  . LYS I 129 ? 1.225 0.906 1.063 0.216  0.150  0.162  458 LYS III CG  
11213 C CD  . LYS I 129 ? 1.274 0.912 1.128 0.219  0.157  0.156  458 LYS III CD  
11214 C CE  . LYS I 129 ? 1.311 0.955 1.155 0.251  0.141  0.151  458 LYS III CE  
11215 N NZ  . LYS I 129 ? 1.391 0.973 1.229 0.267  0.151  0.160  458 LYS III NZ  
11216 N N   . SER I 130 ? 0.965 0.764 0.848 0.137  0.146  0.133  459 SER III N   
11217 C CA  . SER I 130 ? 0.924 0.736 0.819 0.114  0.154  0.131  459 SER III CA  
11218 C C   . SER I 130 ? 0.847 0.710 0.761 0.103  0.135  0.111  459 SER III C   
11219 O O   . SER I 130 ? 0.845 0.730 0.768 0.108  0.120  0.098  459 SER III O   
11220 C CB  . SER I 130 ? 0.919 0.701 0.843 0.093  0.173  0.130  459 SER III CB  
11221 O OG  . SER I 130 ? 0.877 0.676 0.836 0.079  0.163  0.107  459 SER III OG  
11222 N N   . ASN I 131 ? 0.805 0.686 0.722 0.089  0.138  0.109  460 ASN III N   
11223 C CA  . ASN I 131 ? 0.730 0.655 0.660 0.079  0.121  0.093  460 ASN III CA  
11224 C C   . ASN I 131 ? 0.683 0.619 0.648 0.061  0.118  0.075  460 ASN III C   
11225 O O   . ASN I 131 ? 0.676 0.589 0.659 0.050  0.130  0.074  460 ASN III O   
11226 C CB  . ASN I 131 ? 0.708 0.645 0.631 0.071  0.125  0.096  460 ASN III CB  
11227 C CG  . ASN I 131 ? 0.736 0.668 0.619 0.091  0.123  0.109  460 ASN III CG  
11228 O OD1 . ASN I 131 ? 0.787 0.713 0.649 0.111  0.116  0.116  460 ASN III OD1 
11229 N ND2 . ASN I 131 ? 0.721 0.658 0.591 0.089  0.129  0.113  460 ASN III ND2 
11230 N N   . LEU I 132 ? 0.641 0.611 0.616 0.059  0.102  0.062  461 LEU III N   
11231 C CA  . LEU I 132 ? 0.614 0.600 0.615 0.044  0.097  0.045  461 LEU III CA  
11232 C C   . LEU I 132 ? 0.592 0.579 0.607 0.026  0.103  0.042  461 LEU III C   
11233 O O   . LEU I 132 ? 0.593 0.589 0.597 0.025  0.103  0.049  461 LEU III O   
11234 C CB  . LEU I 132 ? 0.579 0.602 0.582 0.046  0.081  0.037  461 LEU III CB  
11235 C CG  . LEU I 132 ? 0.588 0.620 0.587 0.062  0.074  0.036  461 LEU III CG  
11236 C CD1 . LEU I 132 ? 0.575 0.646 0.582 0.059  0.063  0.028  461 LEU III CD1 
11237 C CD2 . LEU I 132 ? 0.613 0.622 0.618 0.067  0.080  0.030  461 LEU III CD2 
11238 N N   . LYS I 133 ? 0.593 0.576 0.632 0.013  0.105  0.030  462 LYS III N   
11239 C CA  . LYS I 133 ? 0.600 0.597 0.659 -0.003 0.104  0.021  462 LYS III CA  
11240 C C   . LYS I 133 ? 0.584 0.615 0.641 -0.004 0.089  0.014  462 LYS III C   
11241 O O   . LYS I 133 ? 0.561 0.604 0.609 0.005  0.080  0.012  462 LYS III O   
11242 C CB  . LYS I 133 ? 0.620 0.605 0.707 -0.014 0.108  0.008  462 LYS III CB  
11243 C CG  . LYS I 133 ? 0.709 0.661 0.807 -0.019 0.126  0.017  462 LYS III CG  
11244 C CD  . LYS I 133 ? 0.773 0.707 0.901 -0.030 0.128  0.002  462 LYS III CD  
11245 C CE  . LYS I 133 ? 0.880 0.779 1.019 -0.036 0.150  0.016  462 LYS III CE  
11246 N NZ  . LYS I 133 ? 0.934 0.814 1.111 -0.051 0.153  0.002  462 LYS III NZ  
11247 N N   . PRO I 134 ? 0.562 0.608 0.626 -0.013 0.086  0.010  463 PRO III N   
11248 C CA  . PRO I 134 ? 0.553 0.625 0.615 -0.014 0.073  0.005  463 PRO III CA  
11249 C C   . PRO I 134 ? 0.547 0.629 0.614 -0.013 0.065  -0.006 463 PRO III C   
11250 O O   . PRO I 134 ? 0.563 0.638 0.644 -0.017 0.066  -0.016 463 PRO III O   
11251 C CB  . PRO I 134 ? 0.533 0.612 0.607 -0.024 0.073  0.002  463 PRO III CB  
11252 C CG  . PRO I 134 ? 0.552 0.614 0.624 -0.024 0.088  0.011  463 PRO III CG  
11253 C CD  . PRO I 134 ? 0.562 0.601 0.637 -0.021 0.097  0.014  463 PRO III CD  
11254 N N   . PHE I 135 ? 0.526 0.626 0.583 -0.008 0.058  -0.004 464 PHE III N   
11255 C CA  . PHE I 135 ? 0.534 0.647 0.590 -0.004 0.052  -0.012 464 PHE III CA  
11256 C C   . PHE I 135 ? 0.564 0.663 0.620 0.005  0.056  -0.018 464 PHE III C   
11257 O O   . PHE I 135 ? 0.564 0.671 0.619 0.009  0.053  -0.028 464 PHE III O   
11258 C CB  . PHE I 135 ? 0.513 0.635 0.576 -0.011 0.046  -0.022 464 PHE III CB  
11259 C CG  . PHE I 135 ? 0.512 0.647 0.573 -0.016 0.042  -0.016 464 PHE III CG  
11260 C CD1 . PHE I 135 ? 0.508 0.658 0.561 -0.015 0.039  -0.008 464 PHE III CD1 
11261 C CD2 . PHE I 135 ? 0.516 0.649 0.586 -0.023 0.040  -0.020 464 PHE III CD2 
11262 C CE1 . PHE I 135 ? 0.505 0.661 0.556 -0.020 0.034  -0.003 464 PHE III CE1 
11263 C CE2 . PHE I 135 ? 0.507 0.649 0.574 -0.026 0.035  -0.016 464 PHE III CE2 
11264 C CZ  . PHE I 135 ? 0.507 0.657 0.563 -0.025 0.032  -0.007 464 PHE III CZ  
11265 N N   . GLU I 136 ? 0.597 0.674 0.652 0.009  0.063  -0.012 465 GLU III N   
11266 C CA  . GLU I 136 ? 0.625 0.684 0.678 0.020  0.067  -0.015 465 GLU III CA  
11267 C C   . GLU I 136 ? 0.639 0.717 0.682 0.033  0.064  -0.011 465 GLU III C   
11268 O O   . GLU I 136 ? 0.626 0.723 0.664 0.034  0.060  -0.002 465 GLU III O   
11269 C CB  . GLU I 136 ? 0.667 0.693 0.721 0.021  0.077  -0.006 465 GLU III CB  
11270 C CG  . GLU I 136 ? 0.685 0.683 0.740 0.029  0.082  -0.012 465 GLU III CG  
11271 C CD  . GLU I 136 ? 0.734 0.694 0.789 0.030  0.095  -0.001 465 GLU III CD  
11272 O OE1 . GLU I 136 ? 0.747 0.703 0.799 0.023  0.102  0.012  465 GLU III OE1 
11273 O OE2 . GLU I 136 ? 0.771 0.702 0.827 0.038  0.099  -0.004 465 GLU III OE2 
11274 N N   . ARG I 137 ? 0.659 0.734 0.701 0.045  0.064  -0.019 466 ARG III N   
11275 C CA  . ARG I 137 ? 0.628 0.724 0.665 0.060  0.062  -0.017 466 ARG III CA  
11276 C C   . ARG I 137 ? 0.645 0.715 0.678 0.076  0.066  -0.019 466 ARG III C   
11277 O O   . ARG I 137 ? 0.639 0.685 0.675 0.075  0.068  -0.030 466 ARG III O   
11278 C CB  . ARG I 137 ? 0.609 0.731 0.647 0.060  0.060  -0.028 466 ARG III CB  
11279 C CG  . ARG I 137 ? 0.601 0.754 0.639 0.073  0.060  -0.025 466 ARG III CG  
11280 C CD  . ARG I 137 ? 0.578 0.756 0.613 0.068  0.060  -0.030 466 ARG III CD  
11281 N NE  . ARG I 137 ? 0.588 0.800 0.626 0.077  0.064  -0.027 466 ARG III NE  
11282 C CZ  . ARG I 137 ? 0.614 0.835 0.649 0.094  0.069  -0.035 466 ARG III CZ  
11283 N NH1 . ARG I 137 ? 0.654 0.848 0.681 0.104  0.069  -0.049 466 ARG III NH1 
11284 N NH2 . ARG I 137 ? 0.623 0.880 0.664 0.101  0.075  -0.030 466 ARG III NH2 
11285 N N   . ASP I 138 ? 0.644 0.719 0.671 0.089  0.066  -0.008 467 ASP III N   
11286 C CA  . ASP I 138 ? 0.659 0.707 0.680 0.108  0.069  -0.007 467 ASP III CA  
11287 C C   . ASP I 138 ? 0.670 0.751 0.694 0.126  0.065  -0.008 467 ASP III C   
11288 O O   . ASP I 138 ? 0.676 0.785 0.701 0.129  0.060  0.001  467 ASP III O   
11289 C CB  . ASP I 138 ? 0.668 0.686 0.679 0.111  0.073  0.009  467 ASP III CB  
11290 C CG  . ASP I 138 ? 0.734 0.717 0.736 0.131  0.077  0.013  467 ASP III CG  
11291 O OD1 . ASP I 138 ? 0.763 0.748 0.768 0.145  0.076  0.003  467 ASP III OD1 
11292 O OD2 . ASP I 138 ? 0.769 0.720 0.758 0.133  0.083  0.027  467 ASP III OD2 
11293 N N   . ILE I 139 ? 0.675 0.755 0.700 0.139  0.067  -0.021 468 ILE III N   
11294 C CA  . ILE I 139 ? 0.688 0.802 0.718 0.158  0.066  -0.024 468 ILE III CA  
11295 C C   . ILE I 139 ? 0.716 0.800 0.739 0.182  0.067  -0.025 468 ILE III C   
11296 O O   . ILE I 139 ? 0.736 0.842 0.764 0.202  0.068  -0.031 468 ILE III O   
11297 C CB  . ILE I 139 ? 0.694 0.837 0.728 0.155  0.068  -0.037 468 ILE III CB  
11298 C CG1 . ILE I 139 ? 0.725 0.837 0.752 0.156  0.071  -0.054 468 ILE III CG1 
11299 C CG2 . ILE I 139 ? 0.652 0.824 0.692 0.134  0.067  -0.031 468 ILE III CG2 
11300 C CD1 . ILE I 139 ? 0.726 0.865 0.749 0.161  0.073  -0.068 468 ILE III CD1 
11301 N N   . SER I 140 ? 0.748 0.782 0.761 0.182  0.070  -0.019 469 SER III N   
11302 C CA  . SER I 140 ? 0.797 0.794 0.803 0.206  0.072  -0.017 469 SER III CA  
11303 C C   . SER I 140 ? 0.809 0.828 0.811 0.227  0.066  -0.004 469 SER III C   
11304 O O   . SER I 140 ? 0.765 0.814 0.768 0.218  0.061  0.006  469 SER III O   
11305 C CB  . SER I 140 ? 0.823 0.760 0.820 0.198  0.079  -0.011 469 SER III CB  
11306 O OG  . SER I 140 ? 0.818 0.752 0.807 0.189  0.079  0.008  469 SER III OG  
11307 N N   . THR I 141 ? 0.854 0.861 0.852 0.255  0.066  -0.006 470 THR III N   
11308 C CA  . THR I 141 ? 0.867 0.899 0.864 0.280  0.058  0.003  470 THR III CA  
11309 C C   . THR I 141 ? 0.934 0.911 0.912 0.304  0.060  0.013  470 THR III C   
11310 O O   . THR I 141 ? 0.995 0.983 0.974 0.334  0.055  0.011  470 THR III O   
11311 C CB  . THR I 141 ? 0.822 0.910 0.839 0.293  0.055  -0.010 470 THR III CB  
11312 O OG1 . THR I 141 ? 0.810 0.877 0.826 0.302  0.062  -0.026 470 THR III OG1 
11313 C CG2 . THR I 141 ? 0.768 0.911 0.804 0.270  0.054  -0.013 470 THR III CG2 
11314 N N   . GLU I 142 ? 0.967 0.885 0.930 0.293  0.068  0.021  471 GLU III N   
11315 C CA  . GLU I 142 ? 1.051 0.908 0.994 0.314  0.073  0.035  471 GLU III CA  
11316 C C   . GLU I 142 ? 1.050 0.916 0.974 0.330  0.065  0.056  471 GLU III C   
11317 O O   . GLU I 142 ? 1.021 0.915 0.944 0.312  0.062  0.062  471 GLU III O   
11318 C CB  . GLU I 142 ? 1.102 0.898 1.042 0.293  0.086  0.037  471 GLU III CB  
11319 C CG  . GLU I 142 ? 1.169 0.954 1.126 0.287  0.088  0.012  471 GLU III CG  
11320 C CD  . GLU I 142 ? 1.241 0.978 1.207 0.262  0.098  0.004  471 GLU III CD  
11321 O OE1 . GLU I 142 ? 1.231 0.961 1.199 0.237  0.104  0.015  471 GLU III OE1 
11322 O OE2 . GLU I 142 ? 1.301 1.010 1.274 0.268  0.099  -0.014 471 GLU III OE2 
11323 N N   . ILE I 143 ? 1.104 0.949 1.012 0.364  0.062  0.065  472 ILE III N   
11324 C CA  . ILE I 143 ? 1.132 0.984 1.016 0.386  0.052  0.085  472 ILE III CA  
11325 C C   . ILE I 143 ? 1.150 0.958 1.010 0.370  0.063  0.105  472 ILE III C   
11326 O O   . ILE I 143 ? 1.195 0.940 1.047 0.363  0.079  0.111  472 ILE III O   
11327 C CB  . ILE I 143 ? 1.194 1.021 1.064 0.429  0.047  0.092  472 ILE III CB  
11328 C CG1 . ILE I 143 ? 1.165 1.038 1.062 0.446  0.039  0.071  472 ILE III CG1 
11329 C CG2 . ILE I 143 ? 1.225 1.055 1.065 0.453  0.036  0.112  472 ILE III CG2 
11330 C CD1 . ILE I 143 ? 1.100 1.057 1.024 0.439  0.026  0.059  472 ILE III CD1 
11331 N N   . TYR I 144 ? 1.130 0.970 0.980 0.363  0.055  0.113  473 TYR III N   
11332 C CA  . TYR I 144 ? 1.183 0.989 1.007 0.349  0.066  0.132  473 TYR III CA  
11333 C C   . TYR I 144 ? 1.259 1.022 1.041 0.382  0.067  0.157  473 TYR III C   
11334 O O   . TYR I 144 ? 1.252 1.043 1.020 0.414  0.049  0.159  473 TYR III O   
11335 C CB  . TYR I 144 ? 1.156 1.015 0.984 0.331  0.056  0.127  473 TYR III CB  
11336 C CG  . TYR I 144 ? 1.192 1.025 0.992 0.320  0.066  0.145  473 TYR III CG  
11337 C CD1 . TYR I 144 ? 1.163 0.977 0.974 0.287  0.082  0.144  473 TYR III CD1 
11338 C CD2 . TYR I 144 ? 1.254 1.086 1.016 0.344  0.057  0.161  473 TYR III CD2 
11339 C CE1 . TYR I 144 ? 1.175 0.969 0.962 0.278  0.093  0.160  473 TYR III CE1 
11340 C CE2 . TYR I 144 ? 1.264 1.073 0.997 0.337  0.068  0.177  473 TYR III CE2 
11341 C CZ  . TYR I 144 ? 1.232 1.022 0.978 0.303  0.088  0.177  473 TYR III CZ  
11342 O OH  . TYR I 144 ? 1.249 1.020 0.968 0.297  0.100  0.193  473 TYR III OH  
11343 N N   . GLN I 145 ? 1.313 1.008 1.076 0.377  0.088  0.175  474 GLN III N   
11344 C CA  . GLN I 145 ? 1.391 1.033 1.109 0.407  0.095  0.204  474 GLN III CA  
11345 C C   . GLN I 145 ? 1.369 1.020 1.056 0.402  0.097  0.220  474 GLN III C   
11346 O O   . GLN I 145 ? 1.320 0.948 1.008 0.374  0.116  0.227  474 GLN III O   
11347 C CB  . GLN I 145 ? 1.463 1.027 1.180 0.400  0.119  0.216  474 GLN III CB  
11348 C CG  . GLN I 145 ? 1.574 1.080 1.242 0.430  0.129  0.249  474 GLN III CG  
11349 C CD  . GLN I 145 ? 1.669 1.095 1.340 0.429  0.151  0.260  474 GLN III CD  
11350 O OE1 . GLN I 145 ? 1.663 1.083 1.371 0.415  0.152  0.239  474 GLN III OE1 
11351 N NE2 . GLN I 145 ? 1.774 1.140 1.405 0.443  0.169  0.294  474 GLN III NE2 
11352 N N   . ALA I 146 ? 1.402 1.089 1.064 0.430  0.076  0.223  475 ALA III N   
11353 C CA  . ALA I 146 ? 1.426 1.130 1.054 0.432  0.071  0.233  475 ALA III CA  
11354 C C   . ALA I 146 ? 1.536 1.179 1.105 0.461  0.084  0.267  475 ALA III C   
11355 O O   . ALA I 146 ? 1.570 1.212 1.104 0.463  0.088  0.281  475 ALA III O   
11356 C CB  . ALA I 146 ? 1.384 1.160 1.021 0.446  0.039  0.215  475 ALA III CB  
11357 N N   . GLY I 147 ? 1.588 1.182 1.146 0.486  0.091  0.281  476 GLY III N   
11358 C CA  . GLY I 147 ? 1.673 1.207 1.172 0.519  0.102  0.316  476 GLY III CA  
11359 C C   . GLY I 147 ? 1.739 1.197 1.241 0.521  0.126  0.332  476 GLY III C   
11360 O O   . GLY I 147 ? 1.709 1.160 1.258 0.490  0.137  0.316  476 GLY III O   
11361 N N   . SER I 148 ? 1.830 1.230 1.280 0.557  0.134  0.364  477 SER III N   
11362 C CA  . SER I 148 ? 1.916 1.226 1.353 0.560  0.164  0.390  477 SER III CA  
11363 C C   . SER I 148 ? 1.917 1.211 1.400 0.557  0.160  0.370  477 SER III C   
11364 O O   . SER I 148 ? 1.936 1.184 1.449 0.527  0.184  0.370  477 SER III O   
11365 C CB  . SER I 148 ? 2.012 1.277 1.381 0.608  0.165  0.426  477 SER III CB  
11366 O OG  . SER I 148 ? 2.003 1.312 1.362 0.648  0.130  0.413  477 SER III OG  
11367 N N   . THR I 149 ? 1.898 1.227 1.385 0.590  0.132  0.354  478 THR III N   
11368 C CA  . THR I 149 ? 1.903 1.208 1.420 0.601  0.129  0.340  478 THR III CA  
11369 C C   . THR I 149 ? 1.852 1.194 1.432 0.559  0.129  0.304  478 THR III C   
11370 O O   . THR I 149 ? 1.753 1.167 1.355 0.537  0.116  0.283  478 THR III O   
11371 C CB  . THR I 149 ? 1.892 1.231 1.397 0.650  0.099  0.333  478 THR III CB  
11372 O OG1 . THR I 149 ? 1.963 1.276 1.404 0.690  0.096  0.365  478 THR III OG1 
11373 C CG2 . THR I 149 ? 1.919 1.216 1.440 0.671  0.100  0.325  478 THR III CG2 
11374 N N   . PRO I 150 ? 1.914 1.208 1.523 0.547  0.142  0.294  479 PRO III N   
11375 C CA  . PRO I 150 ? 1.842 1.175 1.505 0.516  0.137  0.257  479 PRO III CA  
11376 C C   . PRO I 150 ? 1.793 1.196 1.474 0.540  0.109  0.231  479 PRO III C   
11377 O O   . PRO I 150 ? 1.826 1.224 1.482 0.584  0.097  0.241  479 PRO III O   
11378 C CB  . PRO I 150 ? 1.903 1.157 1.583 0.506  0.156  0.255  479 PRO III CB  
11379 C CG  . PRO I 150 ? 1.999 1.182 1.636 0.547  0.162  0.287  479 PRO III CG  
11380 C CD  . PRO I 150 ? 2.013 1.212 1.603 0.562  0.161  0.317  479 PRO III CD  
11381 N N   . CYS I 151 ? 1.680 1.148 1.401 0.514  0.100  0.200  480 CYS III N   
11382 C CA  . CYS I 151 ? 1.625 1.175 1.365 0.531  0.076  0.179  480 CYS III CA  
11383 C C   . CYS I 151 ? 1.608 1.161 1.376 0.545  0.072  0.154  480 CYS III C   
11384 O O   . CYS I 151 ? 1.553 1.165 1.334 0.569  0.054  0.140  480 CYS III O   
11385 C CB  . CYS I 151 ? 1.564 1.183 1.328 0.496  0.070  0.163  480 CYS III CB  
11386 S SG  . CYS I 151 ? 1.608 1.246 1.338 0.492  0.066  0.186  480 CYS III SG  
11387 N N   . ASN I 152 ? 1.600 1.092 1.379 0.530  0.088  0.147  481 ASN III N   
11388 C CA  . ASN I 152 ? 1.569 1.052 1.370 0.544  0.086  0.122  481 ASN III CA  
11389 C C   . ASN I 152 ? 1.454 1.028 1.288 0.538  0.073  0.092  481 ASN III C   
11390 O O   . ASN I 152 ? 1.428 1.022 1.273 0.567  0.064  0.076  481 ASN III O   
11391 C CB  . ASN I 152 ? 1.650 1.094 1.429 0.594  0.081  0.132  481 ASN III CB  
11392 C CG  . ASN I 152 ? 1.730 1.083 1.473 0.606  0.095  0.165  481 ASN III CG  
11393 O OD1 . ASN I 152 ? 1.738 1.062 1.469 0.578  0.109  0.185  481 ASN III OD1 
11394 N ND2 . ASN I 152 ? 1.790 1.096 1.516 0.648  0.092  0.173  481 ASN III ND2 
11395 N N   . GLY I 153 ? 1.370 0.995 1.219 0.503  0.072  0.086  482 GLY III N   
11396 C CA  . GLY I 153 ? 1.297 1.003 1.176 0.490  0.063  0.062  482 GLY III CA  
11397 C C   . GLY I 153 ? 1.278 1.051 1.165 0.522  0.046  0.060  482 GLY III C   
11398 O O   . GLY I 153 ? 1.243 1.074 1.158 0.523  0.042  0.038  482 GLY III O   
11399 N N   . VAL I 154 ? 1.303 1.071 1.166 0.548  0.037  0.081  483 VAL III N   
11400 C CA  . VAL I 154 ? 1.259 1.094 1.131 0.579  0.018  0.079  483 VAL III CA  
11401 C C   . VAL I 154 ? 1.227 1.090 1.084 0.571  0.007  0.095  483 VAL III C   
11402 O O   . VAL I 154 ? 1.229 1.038 1.052 0.563  0.015  0.117  483 VAL III O   
11403 C CB  . VAL I 154 ? 1.316 1.117 1.171 0.629  0.012  0.087  483 VAL III CB  
11404 C CG1 . VAL I 154 ? 1.304 1.170 1.165 0.662  -0.010 0.088  483 VAL III CG1 
11405 C CG2 . VAL I 154 ? 1.332 1.119 1.206 0.642  0.019  0.065  483 VAL III CG2 
11406 N N   . GLU I 155 ? 1.175 1.120 1.057 0.571  -0.009 0.085  484 GLU III N   
11407 C CA  . GLU I 155 ? 1.150 1.134 1.024 0.567  -0.025 0.094  484 GLU III CA  
11408 C C   . GLU I 155 ? 1.212 1.179 1.052 0.613  -0.040 0.111  484 GLU III C   
11409 O O   . GLU I 155 ? 1.247 1.206 1.089 0.649  -0.044 0.109  484 GLU III O   
11410 C CB  . GLU I 155 ? 1.089 1.166 1.010 0.554  -0.037 0.073  484 GLU III CB  
11411 C CG  . GLU I 155 ? 1.075 1.193 0.998 0.535  -0.050 0.075  484 GLU III CG  
11412 C CD  . GLU I 155 ? 1.008 1.192 0.976 0.500  -0.050 0.057  484 GLU III CD  
11413 O OE1 . GLU I 155 ? 0.988 1.204 0.991 0.500  -0.044 0.042  484 GLU III OE1 
11414 O OE2 . GLU I 155 ? 0.989 1.189 0.956 0.475  -0.055 0.058  484 GLU III OE2 
11415 N N   . GLY I 156 ? 1.226 1.189 1.035 0.612  -0.049 0.126  485 GLY III N   
11416 C CA  . GLY I 156 ? 1.285 1.239 1.056 0.655  -0.066 0.143  485 GLY III CA  
11417 C C   . GLY I 156 ? 1.312 1.238 1.038 0.645  -0.066 0.163  485 GLY III C   
11418 O O   . GLY I 156 ? 1.274 1.211 1.009 0.605  -0.057 0.158  485 GLY III O   
11419 N N   . PHE I 157 ? 1.395 1.286 1.070 0.684  -0.074 0.184  486 PHE III N   
11420 C CA  . PHE I 157 ? 1.440 1.299 1.060 0.684  -0.072 0.207  486 PHE III CA  
11421 C C   . PHE I 157 ? 1.457 1.255 1.067 0.644  -0.039 0.219  486 PHE III C   
11422 O O   . PHE I 157 ? 1.482 1.218 1.090 0.643  -0.017 0.228  486 PHE III O   
11423 C CB  . PHE I 157 ? 1.526 1.344 1.090 0.738  -0.081 0.231  486 PHE III CB  
11424 C CG  . PHE I 157 ? 1.537 1.418 1.113 0.780  -0.117 0.218  486 PHE III CG  
11425 C CD1 . PHE I 157 ? 1.484 1.449 1.088 0.773  -0.144 0.195  486 PHE III CD1 
11426 C CD2 . PHE I 157 ? 1.606 1.460 1.165 0.828  -0.123 0.228  486 PHE III CD2 
11427 C CE1 . PHE I 157 ? 1.490 1.517 1.110 0.811  -0.178 0.182  486 PHE III CE1 
11428 C CE2 . PHE I 157 ? 1.616 1.531 1.188 0.869  -0.157 0.216  486 PHE III CE2 
11429 C CZ  . PHE I 157 ? 1.556 1.560 1.161 0.859  -0.184 0.192  486 PHE III CZ  
11430 N N   . ASN I 158 ? 1.455 1.272 1.063 0.612  -0.036 0.216  487 ASN III N   
11431 C CA  . ASN I 158 ? 1.475 1.245 1.075 0.574  -0.007 0.227  487 ASN III CA  
11432 C C   . ASN I 158 ? 1.446 1.211 1.095 0.540  0.010  0.211  487 ASN III C   
11433 O O   . ASN I 158 ? 1.443 1.162 1.091 0.511  0.035  0.219  487 ASN III O   
11434 C CB  . ASN I 158 ? 1.574 1.260 1.116 0.592  0.015  0.262  487 ASN III CB  
11435 C CG  . ASN I 158 ? 1.625 1.314 1.109 0.621  0.002  0.280  487 ASN III CG  
11436 O OD1 . ASN I 158 ? 1.607 1.344 1.090 0.610  -0.012 0.269  487 ASN III OD1 
11437 N ND2 . ASN I 158 ? 1.705 1.341 1.137 0.663  0.004  0.307  487 ASN III ND2 
11438 N N   . CYS I 159 ? 1.266 1.448 1.085 0.387  -0.081 0.189  488 CYS III N   
11439 C CA  . CYS I 159 ? 1.204 1.407 1.061 0.370  -0.055 0.183  488 CYS III CA  
11440 C C   . CYS I 159 ? 1.117 1.376 1.028 0.355  -0.064 0.172  488 CYS III C   
11441 O O   . CYS I 159 ? 1.080 1.372 1.036 0.363  -0.073 0.168  488 CYS III O   
11442 C CB  . CYS I 159 ? 1.233 1.428 1.103 0.388  -0.046 0.187  488 CYS III CB  
11443 S SG  . CYS I 159 ? 1.324 1.451 1.133 0.398  -0.021 0.199  488 CYS III SG  
11444 N N   . TYR I 160 ? 1.064 1.331 0.971 0.333  -0.061 0.168  489 TYR III N   
11445 C CA  . TYR I 160 ? 1.016 1.330 0.968 0.317  -0.071 0.158  489 TYR III CA  
11446 C C   . TYR I 160 ? 0.955 1.288 0.936 0.297  -0.045 0.152  489 TYR III C   
11447 O O   . TYR I 160 ? 0.979 1.287 0.936 0.287  -0.023 0.155  489 TYR III O   
11448 C CB  . TYR I 160 ? 1.031 1.341 0.959 0.307  -0.084 0.157  489 TYR III CB  
11449 C CG  . TYR I 160 ? 1.088 1.380 0.985 0.327  -0.110 0.161  489 TYR III CG  
11450 C CD1 . TYR I 160 ? 1.140 1.382 0.981 0.342  -0.109 0.171  489 TYR III CD1 
11451 C CD2 . TYR I 160 ? 1.082 1.404 0.998 0.326  -0.137 0.154  489 TYR III CD2 
11452 C CE1 . TYR I 160 ? 1.183 1.406 0.991 0.359  -0.134 0.175  489 TYR III CE1 
11453 C CE2 . TYR I 160 ? 1.125 1.432 1.012 0.343  -0.163 0.157  489 TYR III CE2 
11454 C CZ  . TYR I 160 ? 1.180 1.436 1.010 0.360  -0.162 0.168  489 TYR III CZ  
11455 O OH  . TYR I 160 ? 1.213 1.451 1.008 0.377  -0.188 0.171  489 TYR III OH  
11456 N N   . PHE I 161 ? 0.903 1.279 0.937 0.292  -0.048 0.144  490 PHE III N   
11457 C CA  . PHE I 161 ? 0.848 1.247 0.910 0.270  -0.029 0.138  490 PHE III CA  
11458 C C   . PHE I 161 ? 0.828 1.226 0.873 0.252  -0.031 0.136  490 PHE III C   
11459 O O   . PHE I 161 ? 0.823 1.231 0.867 0.254  -0.052 0.135  490 PHE III O   
11460 C CB  . PHE I 161 ? 0.820 1.263 0.939 0.271  -0.034 0.130  490 PHE III CB  
11461 C CG  . PHE I 161 ? 0.787 1.251 0.933 0.251  -0.013 0.123  490 PHE III CG  
11462 C CD1 . PHE I 161 ? 0.785 1.239 0.931 0.248  0.011  0.124  490 PHE III CD1 
11463 C CD2 . PHE I 161 ? 0.764 1.255 0.932 0.234  -0.017 0.117  490 PHE III CD2 
11464 C CE1 . PHE I 161 ? 0.764 1.235 0.931 0.230  0.029  0.118  490 PHE III CE1 
11465 C CE2 . PHE I 161 ? 0.747 1.255 0.936 0.216  0.003  0.112  490 PHE III CE2 
11466 C CZ  . PHE I 161 ? 0.757 1.254 0.944 0.214  0.025  0.113  490 PHE III CZ  
11467 N N   . PRO I 162 ? 0.800 1.186 0.829 0.235  -0.011 0.137  491 PRO III N   
11468 C CA  . PRO I 162 ? 0.788 1.163 0.792 0.221  -0.011 0.138  491 PRO III CA  
11469 C C   . PRO I 162 ? 0.739 1.148 0.772 0.205  -0.018 0.131  491 PRO III C   
11470 O O   . PRO I 162 ? 0.724 1.126 0.739 0.196  -0.023 0.131  491 PRO III O   
11471 C CB  . PRO I 162 ? 0.784 1.137 0.769 0.210  0.014  0.139  491 PRO III CB  
11472 C CG  . PRO I 162 ? 0.764 1.137 0.782 0.208  0.028  0.135  491 PRO III CG  
11473 C CD  . PRO I 162 ? 0.787 1.167 0.822 0.229  0.014  0.136  491 PRO III CD  
11474 N N   . LEU I 163 ? 0.707 1.151 0.785 0.203  -0.018 0.125  492 LEU III N   
11475 C CA  . LEU I 163 ? 0.679 1.156 0.788 0.189  -0.023 0.118  492 LEU III CA  
11476 C C   . LEU I 163 ? 0.689 1.187 0.821 0.200  -0.047 0.114  492 LEU III C   
11477 O O   . LEU I 163 ? 0.679 1.181 0.823 0.217  -0.055 0.114  492 LEU III O   
11478 C CB  . LEU I 163 ? 0.645 1.145 0.788 0.178  -0.005 0.113  492 LEU III CB  
11479 C CG  . LEU I 163 ? 0.633 1.114 0.756 0.167  0.018  0.116  492 LEU III CG  
11480 C CD1 . LEU I 163 ? 0.613 1.118 0.767 0.156  0.033  0.110  492 LEU III CD1 
11481 C CD2 . LEU I 163 ? 0.640 1.103 0.732 0.155  0.019  0.119  492 LEU III CD2 
11482 N N   . GLN I 164 ? 0.705 1.218 0.844 0.190  -0.058 0.109  493 GLN III N   
11483 C CA  . GLN I 164 ? 0.718 1.255 0.882 0.197  -0.082 0.103  493 GLN III CA  
11484 C C   . GLN I 164 ? 0.686 1.258 0.891 0.179  -0.078 0.094  493 GLN III C   
11485 O O   . GLN I 164 ? 0.672 1.239 0.869 0.162  -0.062 0.095  493 GLN III O   
11486 C CB  . GLN I 164 ? 0.772 1.286 0.896 0.203  -0.101 0.106  493 GLN III CB  
11487 C CG  . GLN I 164 ? 0.802 1.338 0.947 0.211  -0.128 0.099  493 GLN III CG  
11488 C CD  . GLN I 164 ? 0.830 1.376 0.994 0.233  -0.141 0.098  493 GLN III CD  
11489 O OE1 . GLN I 164 ? 0.869 1.387 1.004 0.248  -0.140 0.106  493 GLN III OE1 
11490 N NE2 . GLN I 164 ? 0.823 1.407 1.038 0.234  -0.154 0.087  493 GLN III NE2 
11491 N N   . SER I 165 ? 0.691 1.294 0.939 0.185  -0.091 0.085  494 SER III N   
11492 C CA  . SER I 165 ? 0.668 1.305 0.960 0.169  -0.087 0.075  494 SER III CA  
11493 C C   . SER I 165 ? 0.664 1.306 0.952 0.162  -0.103 0.070  494 SER III C   
11494 O O   . SER I 165 ? 0.684 1.316 0.951 0.174  -0.125 0.071  494 SER III O   
11495 C CB  . SER I 165 ? 0.666 1.334 1.010 0.179  -0.091 0.067  494 SER III CB  
11496 O OG  . SER I 165 ? 0.668 1.366 1.054 0.163  -0.085 0.057  494 SER III OG  
11497 N N   . TYR I 166 ? 0.644 1.299 0.947 0.143  -0.093 0.066  495 TYR III N   
11498 C CA  . TYR I 166 ? 0.641 1.302 0.943 0.133  -0.106 0.060  495 TYR III CA  
11499 C C   . TYR I 166 ? 0.662 1.358 1.011 0.139  -0.125 0.047  495 TYR III C   
11500 O O   . TYR I 166 ? 0.689 1.387 1.032 0.141  -0.147 0.042  495 TYR III O   
11501 C CB  . TYR I 166 ? 0.614 1.276 0.918 0.112  -0.087 0.060  495 TYR III CB  
11502 C CG  . TYR I 166 ? 0.612 1.241 0.867 0.105  -0.078 0.071  495 TYR III CG  
11503 C CD1 . TYR I 166 ? 0.619 1.229 0.840 0.106  -0.092 0.073  495 TYR III CD1 
11504 C CD2 . TYR I 166 ? 0.590 1.206 0.832 0.098  -0.056 0.078  495 TYR III CD2 
11505 C CE1 . TYR I 166 ? 0.629 1.208 0.809 0.100  -0.082 0.081  495 TYR III CE1 
11506 C CE2 . TYR I 166 ? 0.588 1.176 0.790 0.093  -0.048 0.086  495 TYR III CE2 
11507 C CZ  . TYR I 166 ? 0.615 1.185 0.787 0.093  -0.060 0.088  495 TYR III CZ  
11508 O OH  . TYR I 166 ? 0.622 1.164 0.757 0.087  -0.051 0.095  495 TYR III OH  
11509 N N   . GLY I 167 ? 0.667 1.391 1.065 0.139  -0.118 0.040  496 GLY III N   
11510 C CA  . GLY I 167 ? 0.689 1.450 1.139 0.143  -0.135 0.026  496 GLY III CA  
11511 C C   . GLY I 167 ? 0.698 1.471 1.160 0.127  -0.140 0.017  496 GLY III C   
11512 O O   . GLY I 167 ? 0.729 1.503 1.182 0.132  -0.164 0.012  496 GLY III O   
11513 N N   . PHE I 168 ? 0.684 1.465 1.164 0.107  -0.116 0.015  497 PHE III N   
11514 C CA  . PHE I 168 ? 0.676 1.465 1.166 0.089  -0.114 0.008  497 PHE III CA  
11515 C C   . PHE I 168 ? 0.657 1.487 1.211 0.086  -0.122 -0.010 497 PHE III C   
11516 O O   . PHE I 168 ? 0.628 1.476 1.222 0.083  -0.105 -0.015 497 PHE III O   
11517 C CB  . PHE I 168 ? 0.672 1.447 1.150 0.071  -0.085 0.014  497 PHE III CB  
11518 C CG  . PHE I 168 ? 0.691 1.430 1.110 0.070  -0.078 0.029  497 PHE III CG  
11519 C CD1 . PHE I 168 ? 0.695 1.416 1.079 0.069  -0.091 0.032  497 PHE III CD1 
11520 C CD2 . PHE I 168 ? 0.688 1.411 1.089 0.069  -0.057 0.039  497 PHE III CD2 
11521 C CE1 . PHE I 168 ? 0.702 1.389 1.035 0.068  -0.084 0.045  497 PHE III CE1 
11522 C CE2 . PHE I 168 ? 0.679 1.370 1.030 0.068  -0.051 0.051  497 PHE III CE2 
11523 C CZ  . PHE I 168 ? 0.706 1.379 1.025 0.067  -0.064 0.054  497 PHE III CZ  
11524 N N   . GLN I 169 ? 0.650 1.491 1.213 0.086  -0.145 -0.020 498 GLN III N   
11525 C CA  . GLN I 169 ? 0.640 1.521 1.266 0.081  -0.153 -0.040 498 GLN III CA  
11526 C C   . GLN I 169 ? 0.624 1.507 1.255 0.060  -0.145 -0.046 498 GLN III C   
11527 O O   . GLN I 169 ? 0.634 1.492 1.219 0.056  -0.151 -0.040 498 GLN III O   
11528 C CB  . GLN I 169 ? 0.654 1.550 1.292 0.100  -0.188 -0.048 498 GLN III CB  
11529 C CG  . GLN I 169 ? 0.660 1.554 1.297 0.121  -0.192 -0.041 498 GLN III CG  
11530 C CD  . GLN I 169 ? 0.680 1.590 1.329 0.141  -0.228 -0.049 498 GLN III CD  
11531 O OE1 . GLN I 169 ? 0.710 1.598 1.312 0.151  -0.249 -0.043 498 GLN III OE1 
11532 N NE2 . GLN I 169 ? 0.679 1.626 1.391 0.148  -0.235 -0.062 498 GLN III NE2 
11533 N N   . PRO I 170 ? 0.600 1.510 1.285 0.046  -0.131 -0.060 499 PRO III N   
11534 C CA  . PRO I 170 ? 0.589 1.500 1.282 0.025  -0.120 -0.066 499 PRO III CA  
11535 C C   . PRO I 170 ? 0.597 1.510 1.279 0.025  -0.147 -0.075 499 PRO III C   
11536 O O   . PRO I 170 ? 0.592 1.491 1.254 0.011  -0.139 -0.074 499 PRO III O   
11537 C CB  . PRO I 170 ? 0.576 1.520 1.337 0.014  -0.103 -0.082 499 PRO III CB  
11538 C CG  . PRO I 170 ? 0.583 1.551 1.381 0.032  -0.115 -0.088 499 PRO III CG  
11539 C CD  . PRO I 170 ? 0.589 1.531 1.335 0.050  -0.124 -0.070 499 PRO III CD  
11540 N N   . THR I 171 ? 0.609 1.536 1.299 0.042  -0.179 -0.082 500 THR III N   
11541 C CA  . THR I 171 ? 0.633 1.564 1.313 0.045  -0.209 -0.092 500 THR III CA  
11542 C C   . THR I 171 ? 0.648 1.539 1.253 0.054  -0.221 -0.076 500 THR III C   
11543 O O   . THR I 171 ? 0.668 1.554 1.254 0.053  -0.241 -0.083 500 THR III O   
11544 C CB  . THR I 171 ? 0.645 1.611 1.369 0.061  -0.239 -0.108 500 THR III CB  
11545 O OG1 . THR I 171 ? 0.650 1.608 1.359 0.082  -0.244 -0.096 500 THR III OG1 
11546 C CG2 . THR I 171 ? 0.632 1.640 1.435 0.051  -0.229 -0.127 500 THR III CG2 
11547 N N   . ASN I 172 ? 0.634 1.495 1.196 0.061  -0.207 -0.057 501 ASN III N   
11548 C CA  . ASN I 172 ? 0.651 1.471 1.142 0.067  -0.213 -0.042 501 ASN III CA  
11549 C C   . ASN I 172 ? 0.650 1.455 1.118 0.050  -0.209 -0.044 501 ASN III C   
11550 O O   . ASN I 172 ? 0.615 1.430 1.110 0.032  -0.188 -0.049 501 ASN III O   
11551 C CB  . ASN I 172 ? 0.640 1.433 1.098 0.070  -0.190 -0.024 501 ASN III CB  
11552 C CG  . ASN I 172 ? 0.650 1.448 1.116 0.089  -0.195 -0.019 501 ASN III CG  
11553 O OD1 . ASN I 172 ? 0.655 1.476 1.149 0.102  -0.217 -0.029 501 ASN III OD1 
11554 N ND2 . ASN I 172 ? 0.650 1.427 1.091 0.091  -0.175 -0.005 501 ASN III ND2 
11555 N N   . GLY I 173 ? 0.678 1.456 1.095 0.056  -0.225 -0.040 502 GLY III N   
11556 C CA  . GLY I 173 ? 0.692 1.446 1.075 0.041  -0.217 -0.037 502 GLY III CA  
11557 C C   . GLY I 173 ? 0.693 1.425 1.057 0.031  -0.185 -0.022 502 GLY III C   
11558 O O   . GLY I 173 ? 0.677 1.403 1.036 0.039  -0.174 -0.011 502 GLY III O   
11559 N N   . VAL I 174 ? 0.702 1.422 1.056 0.014  -0.171 -0.022 503 VAL III N   
11560 C CA  . VAL I 174 ? 0.698 1.401 1.041 0.002  -0.141 -0.009 503 VAL III CA  
11561 C C   . VAL I 174 ? 0.716 1.388 1.011 0.013  -0.136 0.008  503 VAL III C   
11562 O O   . VAL I 174 ? 0.711 1.380 1.009 0.011  -0.116 0.017  503 VAL III O   
11563 C CB  . VAL I 174 ? 0.687 1.378 1.022 -0.016 -0.130 -0.011 503 VAL III CB  
11564 C CG1 . VAL I 174 ? 0.707 1.367 0.990 -0.014 -0.140 -0.007 503 VAL III CG1 
11565 C CG2 . VAL I 174 ? 0.666 1.348 1.003 -0.027 -0.100 -0.001 503 VAL III CG2 
11566 N N   . GLY I 175 ? 0.736 1.385 0.989 0.023  -0.152 0.012  504 GLY III N   
11567 C CA  . GLY I 175 ? 0.729 1.346 0.936 0.034  -0.148 0.026  504 GLY III CA  
11568 C C   . GLY I 175 ? 0.729 1.355 0.948 0.048  -0.147 0.031  504 GLY III C   
11569 O O   . GLY I 175 ? 0.733 1.337 0.925 0.052  -0.134 0.044  504 GLY III O   
11570 N N   . TYR I 176 ? 0.727 1.385 0.987 0.055  -0.159 0.021  505 TYR III N   
11571 C CA  . TYR I 176 ? 0.721 1.389 0.997 0.069  -0.159 0.025  505 TYR III CA  
11572 C C   . TYR I 176 ? 0.673 1.368 0.997 0.059  -0.140 0.021  505 TYR III C   
11573 O O   . TYR I 176 ? 0.657 1.366 1.004 0.068  -0.137 0.021  505 TYR III O   
11574 C CB  . TYR I 176 ? 0.762 1.443 1.047 0.086  -0.188 0.017  505 TYR III CB  
11575 C CG  . TYR I 176 ? 0.839 1.488 1.068 0.099  -0.204 0.023  505 TYR III CG  
11576 C CD1 . TYR I 176 ? 0.891 1.528 1.096 0.094  -0.218 0.018  505 TYR III CD1 
11577 C CD2 . TYR I 176 ? 0.872 1.500 1.072 0.116  -0.206 0.034  505 TYR III CD2 
11578 C CE1 . TYR I 176 ? 0.929 1.534 1.081 0.106  -0.233 0.024  505 TYR III CE1 
11579 C CE2 . TYR I 176 ? 0.917 1.512 1.064 0.129  -0.220 0.040  505 TYR III CE2 
11580 C CZ  . TYR I 176 ? 0.948 1.531 1.070 0.124  -0.233 0.035  505 TYR III CZ  
11581 O OH  . TYR I 176 ? 0.995 1.543 1.062 0.136  -0.246 0.042  505 TYR III OH  
11582 N N   . GLN I 177 ? 0.646 1.346 0.985 0.040  -0.124 0.018  506 GLN III N   
11583 C CA  . GLN I 177 ? 0.624 1.344 1.003 0.030  -0.102 0.015  506 GLN III CA  
11584 C C   . GLN I 177 ? 0.621 1.318 0.972 0.028  -0.080 0.030  506 GLN III C   
11585 O O   . GLN I 177 ? 0.644 1.314 0.953 0.028  -0.078 0.040  506 GLN III O   
11586 C CB  . GLN I 177 ? 0.622 1.355 1.027 0.011  -0.094 0.006  506 GLN III CB  
11587 C CG  . GLN I 177 ? 0.635 1.400 1.085 0.012  -0.112 -0.012 506 GLN III CG  
11588 C CD  . GLN I 177 ? 0.625 1.399 1.097 -0.007 -0.104 -0.022 506 GLN III CD  
11589 O OE1 . GLN I 177 ? 0.596 1.361 1.066 -0.021 -0.081 -0.017 506 GLN III OE1 
11590 N NE2 . GLN I 177 ? 0.634 1.427 1.128 -0.007 -0.125 -0.037 506 GLN III NE2 
11591 N N   . PRO I 178 ? 0.597 1.307 0.974 0.025  -0.062 0.031  507 PRO III N   
11592 C CA  . PRO I 178 ? 0.573 1.263 0.925 0.023  -0.042 0.043  507 PRO III CA  
11593 C C   . PRO I 178 ? 0.547 1.223 0.884 0.007  -0.027 0.048  507 PRO III C   
11594 O O   . PRO I 178 ? 0.543 1.233 0.905 -0.005 -0.023 0.040  507 PRO III O   
11595 C CB  . PRO I 178 ? 0.573 1.283 0.960 0.024  -0.029 0.040  507 PRO III CB  
11596 C CG  . PRO I 178 ? 0.576 1.316 1.012 0.018  -0.033 0.025  507 PRO III CG  
11597 C CD  . PRO I 178 ? 0.593 1.336 1.024 0.024  -0.060 0.019  507 PRO III CD  
11598 N N   . TYR I 179 ? 0.531 1.181 0.829 0.007  -0.019 0.059  508 TYR III N   
11599 C CA  . TYR I 179 ? 0.518 1.153 0.799 -0.006 -0.003 0.066  508 TYR III CA  
11600 C C   . TYR I 179 ? 0.521 1.145 0.788 -0.005 0.013  0.075  508 TYR III C   
11601 O O   . TYR I 179 ? 0.514 1.129 0.762 0.006  0.009  0.080  508 TYR III O   
11602 C CB  . TYR I 179 ? 0.522 1.135 0.770 -0.008 -0.011 0.070  508 TYR III CB  
11603 C CG  . TYR I 179 ? 0.534 1.155 0.795 -0.015 -0.021 0.061  508 TYR III CG  
11604 C CD1 . TYR I 179 ? 0.545 1.182 0.824 -0.008 -0.040 0.051  508 TYR III CD1 
11605 C CD2 . TYR I 179 ? 0.528 1.140 0.785 -0.028 -0.012 0.062  508 TYR III CD2 
11606 C CE1 . TYR I 179 ? 0.561 1.207 0.853 -0.015 -0.050 0.041  508 TYR III CE1 
11607 C CE2 . TYR I 179 ? 0.539 1.159 0.809 -0.035 -0.020 0.053  508 TYR III CE2 
11608 C CZ  . TYR I 179 ? 0.557 1.194 0.845 -0.029 -0.039 0.041  508 TYR III CZ  
11609 O OH  . TYR I 179 ? 0.585 1.229 0.886 -0.037 -0.048 0.030  508 TYR III OH  
11610 N N   . ARG I 180 ? 0.528 1.154 0.803 -0.016 0.031  0.077  509 ARG III N   
11611 C CA  . ARG I 180 ? 0.524 1.136 0.780 -0.017 0.047  0.086  509 ARG III CA  
11612 C C   . ARG I 180 ? 0.528 1.116 0.749 -0.020 0.047  0.095  509 ARG III C   
11613 O O   . ARG I 180 ? 0.565 1.150 0.785 -0.028 0.045  0.094  509 ARG III O   
11614 C CB  . ARG I 180 ? 0.532 1.154 0.809 -0.026 0.065  0.084  509 ARG III CB  
11615 C CG  . ARG I 180 ? 0.530 1.174 0.840 -0.021 0.067  0.076  509 ARG III CG  
11616 C CD  . ARG I 180 ? 0.533 1.184 0.863 -0.031 0.087  0.074  509 ARG III CD  
11617 N NE  . ARG I 180 ? 0.537 1.208 0.901 -0.025 0.088  0.065  509 ARG III NE  
11618 C CZ  . ARG I 180 ? 0.527 1.205 0.909 -0.030 0.107  0.062  509 ARG III CZ  
11619 N NH1 . ARG I 180 ? 0.512 1.176 0.880 -0.040 0.126  0.068  509 ARG III NH1 
11620 N NH2 . ARG I 180 ? 0.535 1.233 0.951 -0.024 0.106  0.054  509 ARG III NH2 
11621 N N   . VAL I 181 ? 0.511 1.084 0.707 -0.015 0.051  0.102  510 VAL III N   
11622 C CA  . VAL I 181 ? 0.506 1.058 0.671 -0.017 0.051  0.110  510 VAL III CA  
11623 C C   . VAL I 181 ? 0.502 1.045 0.654 -0.020 0.065  0.116  510 VAL III C   
11624 O O   . VAL I 181 ? 0.505 1.054 0.660 -0.015 0.070  0.115  510 VAL III O   
11625 C CB  . VAL I 181 ? 0.517 1.056 0.661 -0.007 0.039  0.111  510 VAL III CB  
11626 C CG1 . VAL I 181 ? 0.522 1.040 0.640 -0.010 0.041  0.117  510 VAL III CG1 
11627 C CG2 . VAL I 181 ? 0.518 1.065 0.672 -0.003 0.024  0.104  510 VAL III CG2 
11628 N N   . VAL I 182 ? 0.487 1.019 0.626 -0.027 0.070  0.121  511 VAL III N   
11629 C CA  . VAL I 182 ? 0.474 0.995 0.594 -0.028 0.079  0.128  511 VAL III CA  
11630 C C   . VAL I 182 ? 0.469 0.972 0.567 -0.027 0.074  0.132  511 VAL III C   
11631 O O   . VAL I 182 ? 0.455 0.954 0.554 -0.031 0.071  0.133  511 VAL III O   
11632 C CB  . VAL I 182 ? 0.480 1.002 0.604 -0.036 0.092  0.131  511 VAL III CB  
11633 C CG1 . VAL I 182 ? 0.478 0.987 0.579 -0.036 0.098  0.138  511 VAL III CG1 
11634 C CG2 . VAL I 182 ? 0.470 1.008 0.617 -0.037 0.100  0.125  511 VAL III CG2 
11635 N N   . VAL I 183 ? 0.487 0.982 0.569 -0.022 0.074  0.134  512 VAL III N   
11636 C CA  . VAL I 183 ? 0.482 0.961 0.546 -0.021 0.072  0.138  512 VAL III CA  
11637 C C   . VAL I 183 ? 0.494 0.968 0.548 -0.023 0.079  0.142  512 VAL III C   
11638 O O   . VAL I 183 ? 0.529 1.007 0.580 -0.021 0.083  0.141  512 VAL III O   
11639 C CB  . VAL I 183 ? 0.482 0.953 0.536 -0.013 0.067  0.136  512 VAL III CB  
11640 C CG1 . VAL I 183 ? 0.495 0.950 0.535 -0.014 0.066  0.138  512 VAL III CG1 
11641 C CG2 . VAL I 183 ? 0.488 0.964 0.550 -0.009 0.058  0.131  512 VAL III CG2 
11642 N N   . LEU I 184 ? 0.500 0.968 0.550 -0.028 0.079  0.147  513 LEU III N   
11643 C CA  . LEU I 184 ? 0.527 0.988 0.564 -0.029 0.083  0.151  513 LEU III CA  
11644 C C   . LEU I 184 ? 0.521 0.972 0.550 -0.026 0.078  0.151  513 LEU III C   
11645 O O   . LEU I 184 ? 0.496 0.940 0.526 -0.028 0.075  0.152  513 LEU III O   
11646 C CB  . LEU I 184 ? 0.544 1.003 0.583 -0.035 0.087  0.157  513 LEU III CB  
11647 C CG  . LEU I 184 ? 0.540 1.008 0.591 -0.039 0.094  0.156  513 LEU III CG  
11648 C CD1 . LEU I 184 ? 0.558 1.020 0.610 -0.045 0.099  0.161  513 LEU III CD1 
11649 C CD2 . LEU I 184 ? 0.541 1.014 0.586 -0.038 0.101  0.156  513 LEU III CD2 
11650 N N   . SER I 185 ? 0.527 0.977 0.547 -0.023 0.078  0.149  514 SER III N   
11651 C CA  . SER I 185 ? 0.518 0.960 0.532 -0.020 0.076  0.147  514 SER III CA  
11652 C C   . SER I 185 ? 0.507 0.947 0.515 -0.022 0.075  0.151  514 SER III C   
11653 O O   . SER I 185 ? 0.511 0.955 0.512 -0.022 0.077  0.152  514 SER III O   
11654 C CB  . SER I 185 ? 0.518 0.960 0.529 -0.016 0.077  0.142  514 SER III CB  
11655 O OG  . SER I 185 ? 0.551 0.989 0.564 -0.013 0.076  0.139  514 SER III OG  
11656 N N   . PHE I 186 ? 0.506 0.939 0.515 -0.022 0.071  0.152  515 PHE III N   
11657 C CA  . PHE I 186 ? 0.530 0.961 0.535 -0.022 0.068  0.155  515 PHE III CA  
11658 C C   . PHE I 186 ? 0.516 0.944 0.522 -0.020 0.065  0.149  515 PHE III C   
11659 O O   . PHE I 186 ? 0.508 0.931 0.521 -0.020 0.065  0.145  515 PHE III O   
11660 C CB  . PHE I 186 ? 0.536 0.960 0.545 -0.024 0.067  0.161  515 PHE III CB  
11661 C CG  . PHE I 186 ? 0.536 0.962 0.548 -0.028 0.072  0.166  515 PHE III CG  
11662 C CD1 . PHE I 186 ? 0.542 0.975 0.549 -0.029 0.076  0.167  515 PHE III CD1 
11663 C CD2 . PHE I 186 ? 0.523 0.943 0.542 -0.031 0.072  0.168  515 PHE III CD2 
11664 C CE1 . PHE I 186 ? 0.540 0.973 0.551 -0.033 0.082  0.170  515 PHE III CE1 
11665 C CE2 . PHE I 186 ? 0.532 0.954 0.555 -0.035 0.077  0.171  515 PHE III CE2 
11666 C CZ  . PHE I 186 ? 0.527 0.956 0.547 -0.037 0.082  0.172  515 PHE III CZ  
11667 N N   . GLU I 187 ? 0.533 0.966 0.532 -0.018 0.062  0.147  516 GLU III N   
11668 C CA  . GLU I 187 ? 0.537 0.969 0.539 -0.016 0.058  0.140  516 GLU III CA  
11669 C C   . GLU I 187 ? 0.491 0.923 0.495 -0.015 0.051  0.144  516 GLU III C   
11670 O O   . GLU I 187 ? 0.486 0.918 0.478 -0.014 0.048  0.150  516 GLU III O   
11671 C CB  . GLU I 187 ? 0.594 1.031 0.587 -0.015 0.060  0.135  516 GLU III CB  
11672 C CG  . GLU I 187 ? 0.614 1.050 0.611 -0.015 0.066  0.128  516 GLU III CG  
11673 C CD  . GLU I 187 ? 0.689 1.129 0.678 -0.014 0.069  0.122  516 GLU III CD  
11674 O OE1 . GLU I 187 ? 0.716 1.160 0.695 -0.014 0.065  0.121  516 GLU III OE1 
11675 O OE2 . GLU I 187 ? 0.801 1.239 0.791 -0.013 0.075  0.119  516 GLU III OE2 
11676 N N   . LEU I 188 ? 0.464 0.894 0.482 -0.014 0.048  0.139  517 LEU III N   
11677 C CA  . LEU I 188 ? 0.472 0.903 0.495 -0.012 0.039  0.140  517 LEU III CA  
11678 C C   . LEU I 188 ? 0.464 0.901 0.496 -0.011 0.034  0.128  517 LEU III C   
11679 O O   . LEU I 188 ? 0.473 0.908 0.525 -0.011 0.034  0.123  517 LEU III O   
11680 C CB  . LEU I 188 ? 0.463 0.888 0.500 -0.013 0.040  0.143  517 LEU III CB  
11681 C CG  . LEU I 188 ? 0.480 0.900 0.509 -0.014 0.042  0.154  517 LEU III CG  
11682 C CD1 . LEU I 188 ? 0.480 0.892 0.523 -0.016 0.046  0.156  517 LEU III CD1 
11683 C CD2 . LEU I 188 ? 0.497 0.918 0.516 -0.010 0.034  0.161  517 LEU III CD2 
11684 N N   . LEU I 189 ? 0.453 0.896 0.474 -0.010 0.031  0.124  518 LEU III N   
11685 C CA  . LEU I 189 ? 0.447 0.896 0.477 -0.009 0.028  0.111  518 LEU III CA  
11686 C C   . LEU I 189 ? 0.458 0.915 0.491 -0.006 0.013  0.110  518 LEU III C   
11687 O O   . LEU I 189 ? 0.469 0.924 0.493 -0.002 0.007  0.121  518 LEU III O   
11688 C CB  . LEU I 189 ? 0.446 0.897 0.461 -0.011 0.032  0.107  518 LEU III CB  
11689 C CG  . LEU I 189 ? 0.435 0.880 0.447 -0.013 0.045  0.109  518 LEU III CG  
11690 C CD1 . LEU I 189 ? 0.447 0.894 0.446 -0.013 0.049  0.103  518 LEU III CD1 
11691 C CD2 . LEU I 189 ? 0.414 0.852 0.441 -0.015 0.052  0.104  518 LEU III CD2 
11692 N N   . HIS I 190 ? 0.453 0.917 0.498 -0.006 0.008  0.098  519 HIS III N   
11693 C CA  . HIS I 190 ? 0.477 0.950 0.525 -0.001 -0.008 0.094  519 HIS III CA  
11694 C C   . HIS I 190 ? 0.492 0.968 0.511 0.001  -0.014 0.095  519 HIS III C   
11695 O O   . HIS I 190 ? 0.492 0.974 0.512 -0.001 -0.017 0.082  519 HIS III O   
11696 C CB  . HIS I 190 ? 0.468 0.948 0.545 -0.003 -0.010 0.079  519 HIS III CB  
11697 C CG  . HIS I 190 ? 0.466 0.940 0.567 -0.005 -0.002 0.080  519 HIS III CG  
11698 N ND1 . HIS I 190 ? 0.451 0.917 0.564 -0.010 0.013  0.073  519 HIS III ND1 
11699 C CD2 . HIS I 190 ? 0.468 0.939 0.580 -0.002 -0.005 0.088  519 HIS III CD2 
11700 C CE1 . HIS I 190 ? 0.444 0.904 0.574 -0.011 0.019  0.075  519 HIS III CE1 
11701 N NE2 . HIS I 190 ? 0.463 0.926 0.594 -0.006 0.008  0.084  519 HIS III NE2 
11702 N N   . ALA I 191 ? 0.524 0.993 0.519 0.003  -0.014 0.108  520 ALA III N   
11703 C CA  . ALA I 191 ? 0.558 1.024 0.520 0.004  -0.015 0.112  520 ALA III CA  
11704 C C   . ALA I 191 ? 0.567 1.024 0.510 0.008  -0.019 0.128  520 ALA III C   
11705 O O   . ALA I 191 ? 0.561 1.013 0.515 0.009  -0.016 0.136  520 ALA III O   
11706 C CB  . ALA I 191 ? 0.545 1.007 0.498 -0.001 0.000  0.111  520 ALA III CB  
11707 N N   . PRO I 192 ? 0.608 1.059 0.519 0.011  -0.023 0.133  521 PRO III N   
11708 C CA  . PRO I 192 ? 0.617 1.056 0.506 0.014  -0.021 0.148  521 PRO III CA  
11709 C C   . PRO I 192 ? 0.603 1.035 0.496 0.009  -0.004 0.155  521 PRO III C   
11710 O O   . PRO I 192 ? 0.594 1.030 0.491 0.004  0.007  0.150  521 PRO III O   
11711 C CB  . PRO I 192 ? 0.647 1.080 0.499 0.016  -0.024 0.149  521 PRO III CB  
11712 C CG  . PRO I 192 ? 0.651 1.095 0.509 0.018  -0.038 0.135  521 PRO III CG  
11713 C CD  . PRO I 192 ? 0.630 1.085 0.522 0.012  -0.030 0.124  521 PRO III CD  
11714 N N   . ALA I 193 ? 0.608 1.033 0.503 0.010  -0.002 0.167  522 ALA III N   
11715 C CA  . ALA I 193 ? 0.606 1.025 0.502 0.006  0.014  0.175  522 ALA III CA  
11716 C C   . ALA I 193 ? 0.622 1.032 0.488 0.004  0.022  0.179  522 ALA III C   
11717 O O   . ALA I 193 ? 0.627 1.030 0.467 0.008  0.016  0.182  522 ALA III O   
11718 C CB  . ALA I 193 ? 0.622 1.031 0.522 0.008  0.013  0.185  522 ALA III CB  
11719 N N   . THR I 194 ? 0.646 1.058 0.517 -0.002 0.036  0.177  523 THR III N   
11720 C CA  . THR I 194 ? 0.698 1.103 0.546 -0.004 0.048  0.180  523 THR III CA  
11721 C C   . THR I 194 ? 0.687 1.086 0.540 -0.008 0.061  0.189  523 THR III C   
11722 O O   . THR I 194 ? 0.710 1.100 0.544 -0.010 0.071  0.194  523 THR III O   
11723 C CB  . THR I 194 ? 0.712 1.126 0.563 -0.008 0.053  0.170  523 THR III CB  
11724 O OG1 . THR I 194 ? 0.685 1.107 0.562 -0.012 0.061  0.166  523 THR III OG1 
11725 C CG2 . THR I 194 ? 0.705 1.126 0.556 -0.005 0.041  0.160  523 THR III CG2 
11726 N N   . VAL I 195 ? 0.679 1.082 0.557 -0.010 0.061  0.190  524 VAL III N   
11727 C CA  . VAL I 195 ? 0.677 1.075 0.563 -0.015 0.073  0.196  524 VAL III CA  
11728 C C   . VAL I 195 ? 0.668 1.059 0.560 -0.013 0.068  0.204  524 VAL III C   
11729 O O   . VAL I 195 ? 0.644 1.042 0.556 -0.012 0.060  0.199  524 VAL III O   
11730 C CB  . VAL I 195 ? 0.661 1.071 0.571 -0.020 0.080  0.189  524 VAL III CB  
11731 C CG1 . VAL I 195 ? 0.659 1.065 0.580 -0.025 0.090  0.194  524 VAL III CG1 
11732 C CG2 . VAL I 195 ? 0.663 1.078 0.567 -0.021 0.087  0.183  524 VAL III CG2 
11733 N N   . CYS I 196 ? 0.705 1.082 0.583 -0.012 0.074  0.214  525 CYS III N   
11734 C CA  . CYS I 196 ? 0.729 1.097 0.614 -0.010 0.072  0.222  525 CYS III CA  
11735 C C   . CYS I 196 ? 0.740 1.099 0.627 -0.017 0.088  0.227  525 CYS III C   
11736 O O   . CYS I 196 ? 0.762 1.118 0.638 -0.020 0.099  0.227  525 CYS III O   
11737 C CB  . CYS I 196 ? 0.759 1.114 0.620 -0.002 0.062  0.230  525 CYS III CB  
11738 S SG  . CYS I 196 ? 0.812 1.180 0.681 0.005  0.041  0.222  525 CYS III SG  
11739 N N   . GLY I 197 ? 0.748 1.104 0.652 -0.018 0.089  0.230  526 GLY III N   
11740 C CA  . GLY I 197 ? 0.800 1.145 0.706 -0.024 0.104  0.236  526 GLY III CA  
11741 C C   . GLY I 197 ? 0.875 1.199 0.753 -0.020 0.109  0.248  526 GLY III C   
11742 O O   . GLY I 197 ? 0.864 1.182 0.721 -0.012 0.098  0.252  526 GLY III O   
11743 N N   . PRO I 198 ? 0.972 1.283 0.847 -0.025 0.125  0.253  527 PRO III N   
11744 C CA  . PRO I 198 ? 1.044 1.329 0.890 -0.021 0.132  0.266  527 PRO III CA  
11745 C C   . PRO I 198 ? 1.125 1.398 0.963 -0.012 0.120  0.275  527 PRO III C   
11746 O O   . PRO I 198 ? 1.113 1.367 0.920 -0.004 0.119  0.285  527 PRO III O   
11747 C CB  . PRO I 198 ? 1.044 1.322 0.903 -0.031 0.152  0.267  527 PRO III CB  
11748 C CG  . PRO I 198 ? 1.008 1.308 0.893 -0.040 0.157  0.254  527 PRO III CG  
11749 C CD  . PRO I 198 ? 0.964 1.284 0.864 -0.036 0.138  0.247  527 PRO III CD  
11759 N N   . GLN J 1   ? 0.867 0.796 0.801 0.128  -0.148 -0.018 1   GLN JJJ N   
11760 C CA  . GLN J 1   ? 0.844 0.810 0.796 0.118  -0.145 -0.010 1   GLN JJJ CA  
11761 C C   . GLN J 1   ? 0.783 0.757 0.744 0.091  -0.142 -0.008 1   GLN JJJ C   
11762 O O   . GLN J 1   ? 0.831 0.777 0.779 0.077  -0.146 -0.004 1   GLN JJJ O   
11763 C CB  . GLN J 1   ? 0.952 0.902 0.895 0.124  -0.153 0.001  1   GLN JJJ CB  
11764 C CG  . GLN J 1   ? 1.081 0.971 0.995 0.134  -0.163 0.002  1   GLN JJJ CG  
11765 C CD  . GLN J 1   ? 1.171 1.030 1.067 0.138  -0.174 0.015  1   GLN JJJ CD  
11766 O OE1 . GLN J 1   ? 1.151 1.037 1.058 0.131  -0.174 0.026  1   GLN JJJ OE1 
11767 N NE2 . GLN J 1   ? 1.227 1.026 1.095 0.147  -0.184 0.014  1   GLN JJJ NE2 
11768 N N   . VAL J 2   ? 0.699 0.708 0.679 0.085  -0.134 -0.011 2   VAL JJJ N   
11769 C CA  . VAL J 2   ? 0.619 0.641 0.609 0.065  -0.130 -0.011 2   VAL JJJ CA  
11770 C C   . VAL J 2   ? 0.575 0.626 0.578 0.061  -0.128 -0.007 2   VAL JJJ C   
11771 O O   . VAL J 2   ? 0.619 0.694 0.631 0.069  -0.125 -0.008 2   VAL JJJ O   
11772 C CB  . VAL J 2   ? 0.595 0.629 0.594 0.063  -0.126 -0.017 2   VAL JJJ CB  
11773 C CG1 . VAL J 2   ? 0.572 0.619 0.582 0.048  -0.123 -0.016 2   VAL JJJ CG1 
11774 C CG2 . VAL J 2   ? 0.622 0.631 0.607 0.066  -0.128 -0.022 2   VAL JJJ CG2 
11775 N N   . GLN J 3   ? 0.521 0.576 0.526 0.048  -0.128 -0.004 3   GLN JJJ N   
11776 C CA  . GLN J 3   ? 0.467 0.550 0.483 0.041  -0.125 -0.004 3   GLN JJJ CA  
11777 C C   . GLN J 3   ? 0.458 0.549 0.484 0.033  -0.120 -0.011 3   GLN JJJ C   
11778 O O   . GLN J 3   ? 0.436 0.517 0.460 0.029  -0.120 -0.012 3   GLN JJJ O   
11779 C CB  . GLN J 3   ? 0.454 0.540 0.466 0.034  -0.128 0.003  3   GLN JJJ CB  
11780 C CG  . GLN J 3   ? 0.463 0.546 0.467 0.046  -0.133 0.010  3   GLN JJJ CG  
11781 C CD  . GLN J 3   ? 0.454 0.545 0.454 0.037  -0.137 0.019  3   GLN JJJ CD  
11782 O OE1 . GLN J 3   ? 0.408 0.527 0.416 0.028  -0.133 0.017  3   GLN JJJ OE1 
11783 N NE2 . GLN J 3   ? 0.474 0.539 0.458 0.039  -0.145 0.028  3   GLN JJJ NE2 
11784 N N   . LEU J 4   ? 0.463 0.573 0.498 0.031  -0.117 -0.014 4   LEU JJJ N   
11785 C CA  . LEU J 4   ? 0.468 0.581 0.511 0.026  -0.114 -0.020 4   LEU JJJ CA  
11786 C C   . LEU J 4   ? 0.488 0.614 0.533 0.019  -0.112 -0.024 4   LEU JJJ C   
11787 O O   . LEU J 4   ? 0.486 0.626 0.530 0.018  -0.112 -0.022 4   LEU JJJ O   
11788 C CB  . LEU J 4   ? 0.461 0.576 0.506 0.029  -0.113 -0.021 4   LEU JJJ CB  
11789 C CG  . LEU J 4   ? 0.466 0.573 0.509 0.037  -0.114 -0.019 4   LEU JJJ CG  
11790 C CD1 . LEU J 4   ? 0.468 0.589 0.514 0.037  -0.113 -0.018 4   LEU JJJ CD1 
11791 C CD2 . LEU J 4   ? 0.466 0.559 0.508 0.035  -0.114 -0.020 4   LEU JJJ CD2 
11792 N N   . VAL J 5   ? 0.498 0.624 0.545 0.016  -0.110 -0.031 5   VAL JJJ N   
11793 C CA  . VAL J 5   ? 0.508 0.645 0.555 0.011  -0.109 -0.038 5   VAL JJJ CA  
11794 C C   . VAL J 5   ? 0.510 0.636 0.560 0.014  -0.107 -0.047 5   VAL JJJ C   
11795 O O   . VAL J 5   ? 0.493 0.616 0.547 0.019  -0.107 -0.049 5   VAL JJJ O   
11796 C CB  . VAL J 5   ? 0.515 0.668 0.561 0.007  -0.108 -0.038 5   VAL JJJ CB  
11797 C CG1 . VAL J 5   ? 0.515 0.682 0.561 0.003  -0.105 -0.049 5   VAL JJJ CG1 
11798 C CG2 . VAL J 5   ? 0.515 0.674 0.556 0.004  -0.111 -0.027 5   VAL JJJ CG2 
11799 N N   . GLU J 6   ? 0.541 0.660 0.588 0.010  -0.108 -0.052 6   GLU JJJ N   
11800 C CA  . GLU J 6   ? 0.559 0.658 0.604 0.012  -0.109 -0.060 6   GLU JJJ CA  
11801 C C   . GLU J 6   ? 0.560 0.665 0.602 0.014  -0.106 -0.073 6   GLU JJJ C   
11802 O O   . GLU J 6   ? 0.588 0.715 0.629 0.007  -0.104 -0.075 6   GLU JJJ O   
11803 C CB  . GLU J 6   ? 0.572 0.659 0.609 0.001  -0.111 -0.059 6   GLU JJJ CB  
11804 C CG  . GLU J 6   ? 0.560 0.652 0.599 -0.002 -0.113 -0.047 6   GLU JJJ CG  
11805 C CD  . GLU J 6   ? 0.554 0.673 0.594 -0.006 -0.112 -0.041 6   GLU JJJ CD  
11806 O OE1 . GLU J 6   ? 0.522 0.655 0.562 -0.006 -0.110 -0.043 6   GLU JJJ OE1 
11807 O OE2 . GLU J 6   ? 0.553 0.681 0.592 -0.009 -0.114 -0.034 6   GLU JJJ OE2 
11808 N N   . SER J 7   ? 0.579 0.670 0.621 0.024  -0.107 -0.083 7   SER JJJ N   
11809 C CA  . SER J 7   ? 0.607 0.701 0.645 0.031  -0.105 -0.099 7   SER JJJ CA  
11810 C C   . SER J 7   ? 0.656 0.713 0.688 0.042  -0.108 -0.108 7   SER JJJ C   
11811 O O   . SER J 7   ? 0.674 0.709 0.706 0.042  -0.112 -0.098 7   SER JJJ O   
11812 C CB  . SER J 7   ? 0.576 0.703 0.622 0.038  -0.101 -0.101 7   SER JJJ CB  
11813 O OG  . SER J 7   ? 0.574 0.699 0.627 0.048  -0.102 -0.095 7   SER JJJ OG  
11814 N N   . GLY J 8   ? 0.705 0.753 0.729 0.050  -0.108 -0.125 8   GLY JJJ N   
11815 C CA  . GLY J 8   ? 0.779 0.785 0.793 0.064  -0.112 -0.135 8   GLY JJJ CA  
11816 C C   . GLY J 8   ? 0.829 0.791 0.824 0.050  -0.118 -0.138 8   GLY JJJ C   
11817 O O   . GLY J 8   ? 0.916 0.833 0.898 0.059  -0.124 -0.145 8   GLY JJJ O   
11818 N N   . GLY J 9   ? 0.813 0.787 0.803 0.027  -0.117 -0.133 9   GLY JJJ N   
11819 C CA  . GLY J 9   ? 0.830 0.770 0.800 0.008  -0.123 -0.135 9   GLY JJJ CA  
11820 C C   . GLY J 9   ? 0.837 0.761 0.790 0.008  -0.122 -0.157 9   GLY JJJ C   
11821 O O   . GLY J 9   ? 0.860 0.803 0.820 0.027  -0.117 -0.171 9   GLY JJJ O   
11822 N N   . GLY J 10  ? 0.832 0.725 0.763 -0.012 -0.127 -0.161 10  GLY JJJ N   
11823 C CA  . GLY J 10  ? 0.840 0.715 0.751 -0.016 -0.127 -0.184 10  GLY JJJ CA  
11824 C C   . GLY J 10  ? 0.900 0.702 0.781 -0.022 -0.138 -0.192 10  GLY JJJ C   
11825 O O   . GLY J 10  ? 0.900 0.675 0.776 -0.034 -0.145 -0.175 10  GLY JJJ O   
11826 N N   . LEU J 11  ? 0.943 0.716 0.805 -0.015 -0.139 -0.217 11  LEU JJJ N   
11827 C CA  . LEU J 11  ? 1.005 0.701 0.830 -0.024 -0.150 -0.229 11  LEU JJJ CA  
11828 C C   . LEU J 11  ? 1.042 0.684 0.863 0.008  -0.156 -0.233 11  LEU JJJ C   
11829 O O   . LEU J 11  ? 1.017 0.686 0.858 0.041  -0.150 -0.242 11  LEU JJJ O   
11830 C CB  . LEU J 11  ? 1.025 0.720 0.831 -0.028 -0.146 -0.257 11  LEU JJJ CB  
11831 C CG  . LEU J 11  ? 1.116 0.728 0.879 -0.039 -0.157 -0.275 11  LEU JJJ CG  
11832 C CD1 . LEU J 11  ? 1.143 0.724 0.887 -0.079 -0.167 -0.253 11  LEU JJJ CD1 
11833 C CD2 . LEU J 11  ? 1.137 0.757 0.882 -0.044 -0.152 -0.304 11  LEU JJJ CD2 
11834 N N   . VAL J 12  ? 1.104 0.677 0.901 -0.003 -0.169 -0.225 12  VAL JJJ N   
11835 C CA  . VAL J 12  ? 1.159 0.671 0.948 0.028  -0.178 -0.228 12  VAL JJJ CA  
11836 C C   . VAL J 12  ? 1.244 0.663 0.989 0.007  -0.194 -0.229 12  VAL JJJ C   
11837 O O   . VAL J 12  ? 1.222 0.640 0.955 -0.034 -0.199 -0.214 12  VAL JJJ O   
11838 C CB  . VAL J 12  ? 1.114 0.656 0.933 0.042  -0.177 -0.203 12  VAL JJJ CB  
11839 C CG1 . VAL J 12  ? 1.105 0.640 0.920 0.008  -0.184 -0.175 12  VAL JJJ CG1 
11840 C CG2 . VAL J 12  ? 1.172 0.675 0.990 0.082  -0.183 -0.209 12  VAL JJJ CG2 
11841 N N   . GLN J 13  ? 1.331 0.678 1.054 0.035  -0.203 -0.245 13  GLN JJJ N   
11842 C CA  . GLN J 13  ? 1.427 0.670 1.103 0.019  -0.222 -0.247 13  GLN JJJ CA  
11843 C C   . GLN J 13  ? 1.427 0.642 1.103 0.009  -0.233 -0.214 13  GLN JJJ C   
11844 O O   . GLN J 13  ? 1.375 0.630 1.085 0.035  -0.229 -0.201 13  GLN JJJ O   
11845 C CB  . GLN J 13  ? 1.510 0.684 1.160 0.058  -0.227 -0.278 13  GLN JJJ CB  
11846 C CG  . GLN J 13  ? 1.533 0.722 1.170 0.055  -0.218 -0.311 13  GLN JJJ CG  
11847 C CD  . GLN J 13  ? 1.649 0.763 1.254 0.090  -0.225 -0.346 13  GLN JJJ CD  
11848 O OE1 . GLN J 13  ? 1.749 0.759 1.309 0.084  -0.242 -0.352 13  GLN JJJ OE1 
11849 N NE2 . GLN J 13  ? 1.635 0.804 1.260 0.125  -0.211 -0.372 13  GLN JJJ NE2 
11850 N N   . ALA J 14  ? 1.477 0.634 1.119 -0.032 -0.248 -0.201 14  ALA JJJ N   
11851 C CA  . ALA J 14  ? 1.492 0.611 1.124 -0.048 -0.262 -0.170 14  ALA JJJ CA  
11852 C C   . ALA J 14  ? 1.517 0.589 1.152 -0.000 -0.269 -0.170 14  ALA JJJ C   
11853 O O   . ALA J 14  ? 1.549 0.573 1.168 0.034  -0.271 -0.197 14  ALA JJJ O   
11854 C CB  . ALA J 14  ? 1.560 0.603 1.142 -0.094 -0.279 -0.164 14  ALA JJJ CB  
11855 N N   . GLY J 15  ? 1.494 0.589 1.151 0.004  -0.272 -0.142 15  GLY JJJ N   
11856 C CA  . GLY J 15  ? 1.522 0.593 1.190 0.050  -0.278 -0.139 15  GLY JJJ CA  
11857 C C   . GLY J 15  ? 1.459 0.612 1.171 0.092  -0.259 -0.151 15  GLY JJJ C   
11858 O O   . GLY J 15  ? 1.467 0.622 1.195 0.127  -0.262 -0.145 15  GLY JJJ O   
11859 N N   . GLY J 16  ? 1.405 0.626 1.136 0.086  -0.243 -0.167 16  GLY JJJ N   
11860 C CA  . GLY J 16  ? 1.344 0.646 1.114 0.120  -0.226 -0.179 16  GLY JJJ CA  
11861 C C   . GLY J 16  ? 1.267 0.646 1.075 0.113  -0.217 -0.154 16  GLY JJJ C   
11862 O O   . GLY J 16  ? 1.271 0.642 1.075 0.084  -0.224 -0.129 16  GLY JJJ O   
11863 N N   . SER J 17  ? 1.209 0.662 1.050 0.137  -0.203 -0.162 17  SER JJJ N   
11864 C CA  . SER J 17  ? 1.116 0.645 0.993 0.134  -0.194 -0.143 17  SER JJJ CA  
11865 C C   . SER J 17  ? 1.054 0.658 0.953 0.126  -0.178 -0.151 17  SER JJJ C   
11866 O O   . SER J 17  ? 1.071 0.682 0.964 0.136  -0.172 -0.175 17  SER JJJ O   
11867 C CB  . SER J 17  ? 1.104 0.648 0.999 0.173  -0.194 -0.140 17  SER JJJ CB  
11868 O OG  . SER J 17  ? 1.150 0.634 1.030 0.176  -0.210 -0.123 17  SER JJJ OG  
11869 N N   . LEU J 18  ? 1.004 0.661 0.925 0.109  -0.172 -0.133 18  LEU JJJ N   
11870 C CA  . LEU J 18  ? 0.960 0.690 0.903 0.102  -0.158 -0.134 18  LEU JJJ CA  
11871 C C   . LEU J 18  ? 0.924 0.698 0.892 0.103  -0.155 -0.115 18  LEU JJJ C   
11872 O O   . LEU J 18  ? 0.951 0.706 0.916 0.091  -0.162 -0.096 18  LEU JJJ O   
11873 C CB  . LEU J 18  ? 0.956 0.692 0.890 0.067  -0.157 -0.131 18  LEU JJJ CB  
11874 C CG  . LEU J 18  ? 0.995 0.724 0.913 0.061  -0.154 -0.153 18  LEU JJJ CG  
11875 C CD1 . LEU J 18  ? 0.970 0.727 0.887 0.027  -0.151 -0.145 18  LEU JJJ CD1 
11876 C CD2 . LEU J 18  ? 0.981 0.752 0.914 0.086  -0.144 -0.171 18  LEU JJJ CD2 
11877 N N   . ARG J 19  ? 0.883 0.713 0.871 0.115  -0.145 -0.119 19  ARG JJJ N   
11878 C CA  . ARG J 19  ? 0.835 0.711 0.844 0.110  -0.141 -0.102 19  ARG JJJ CA  
11879 C C   . ARG J 19  ? 0.757 0.673 0.773 0.090  -0.132 -0.102 19  ARG JJJ C   
11880 O O   . ARG J 19  ? 0.673 0.624 0.696 0.097  -0.125 -0.113 19  ARG JJJ O   
11881 C CB  . ARG J 19  ? 0.871 0.778 0.896 0.136  -0.138 -0.103 19  ARG JJJ CB  
11882 C CG  . ARG J 19  ? 0.891 0.826 0.931 0.129  -0.137 -0.084 19  ARG JJJ CG  
11883 C CD  . ARG J 19  ? 0.956 0.928 1.010 0.151  -0.135 -0.084 19  ARG JJJ CD  
11884 N NE  . ARG J 19  ? 0.988 1.007 1.051 0.154  -0.126 -0.095 19  ARG JJJ NE  
11885 C CZ  . ARG J 19  ? 1.015 1.084 1.091 0.159  -0.122 -0.092 19  ARG JJJ CZ  
11886 N NH1 . ARG J 19  ? 0.999 1.080 1.084 0.164  -0.125 -0.079 19  ARG JJJ NH1 
11887 N NH2 . ARG J 19  ? 1.001 1.113 1.082 0.157  -0.115 -0.101 19  ARG JJJ NH2 
11888 N N   . LEU J 20  ? 0.735 0.651 0.750 0.068  -0.134 -0.088 20  LEU JJJ N   
11889 C CA  . LEU J 20  ? 0.708 0.663 0.731 0.053  -0.127 -0.083 20  LEU JJJ CA  
11890 C C   . LEU J 20  ? 0.691 0.680 0.730 0.060  -0.123 -0.075 20  LEU JJJ C   
11891 O O   . LEU J 20  ? 0.707 0.689 0.751 0.067  -0.127 -0.066 20  LEU JJJ O   
11892 C CB  . LEU J 20  ? 0.729 0.675 0.744 0.030  -0.131 -0.071 20  LEU JJJ CB  
11893 C CG  . LEU J 20  ? 0.789 0.702 0.784 0.016  -0.136 -0.077 20  LEU JJJ CG  
11894 C CD1 . LEU J 20  ? 0.797 0.720 0.787 -0.009 -0.138 -0.065 20  LEU JJJ CD1 
11895 C CD2 . LEU J 20  ? 0.790 0.709 0.780 0.018  -0.131 -0.095 20  LEU JJJ CD2 
11896 N N   . ALA J 21  ? 0.676 0.699 0.722 0.057  -0.117 -0.076 21  ALA JJJ N   
11897 C CA  . ALA J 21  ? 0.629 0.681 0.686 0.057  -0.114 -0.067 21  ALA JJJ CA  
11898 C C   . ALA J 21  ? 0.603 0.670 0.660 0.043  -0.112 -0.061 21  ALA JJJ C   
11899 O O   . ALA J 21  ? 0.647 0.716 0.698 0.036  -0.111 -0.066 21  ALA JJJ O   
11900 C CB  . ALA J 21  ? 0.618 0.698 0.681 0.069  -0.111 -0.075 21  ALA JJJ CB  
11901 N N   . CYS J 22  ? 0.566 0.643 0.627 0.041  -0.112 -0.051 22  CYS JJJ N   
11902 C CA  . CYS J 22  ? 0.545 0.634 0.604 0.032  -0.111 -0.045 22  CYS JJJ CA  
11903 C C   . CYS J 22  ? 0.549 0.650 0.610 0.033  -0.110 -0.041 22  CYS JJJ C   
11904 O O   . CYS J 22  ? 0.569 0.667 0.633 0.036  -0.111 -0.036 22  CYS JJJ O   
11905 C CB  . CYS J 22  ? 0.567 0.647 0.624 0.027  -0.113 -0.039 22  CYS JJJ CB  
11906 S SG  . CYS J 22  ? 0.606 0.699 0.661 0.024  -0.112 -0.032 22  CYS JJJ SG  
11907 N N   . ILE J 23  ? 0.529 0.643 0.588 0.028  -0.109 -0.040 23  ILE JJJ N   
11908 C CA  . ILE J 23  ? 0.497 0.619 0.553 0.024  -0.110 -0.035 23  ILE JJJ CA  
11909 C C   . ILE J 23  ? 0.509 0.621 0.558 0.020  -0.112 -0.028 23  ILE JJJ C   
11910 O O   . ILE J 23  ? 0.488 0.600 0.535 0.020  -0.112 -0.028 23  ILE JJJ O   
11911 C CB  . ILE J 23  ? 0.464 0.610 0.520 0.020  -0.108 -0.038 23  ILE JJJ CB  
11912 C CG1 . ILE J 23  ? 0.455 0.611 0.506 0.012  -0.110 -0.032 23  ILE JJJ CG1 
11913 C CG2 . ILE J 23  ? 0.469 0.621 0.521 0.015  -0.108 -0.039 23  ILE JJJ CG2 
11914 C CD1 . ILE J 23  ? 0.437 0.624 0.488 0.006  -0.110 -0.033 23  ILE JJJ CD1 
11915 N N   . ALA J 24  ? 0.500 0.602 0.543 0.019  -0.114 -0.023 24  ALA JJJ N   
11916 C CA  . ALA J 24  ? 0.503 0.588 0.535 0.019  -0.117 -0.019 24  ALA JJJ CA  
11917 C C   . ALA J 24  ? 0.512 0.591 0.532 0.010  -0.120 -0.014 24  ALA JJJ C   
11918 O O   . ALA J 24  ? 0.504 0.595 0.523 0.001  -0.120 -0.013 24  ALA JJJ O   
11919 C CB  . ALA J 24  ? 0.474 0.550 0.506 0.024  -0.117 -0.019 24  ALA JJJ CB  
11920 N N   . SER J 25  ? 0.509 0.573 0.519 0.011  -0.124 -0.009 25  SER JJJ N   
11921 C CA  . SER J 25  ? 0.510 0.553 0.501 0.002  -0.130 -0.002 25  SER JJJ CA  
11922 C C   . SER J 25  ? 0.520 0.542 0.501 0.001  -0.132 -0.004 25  SER JJJ C   
11923 O O   . SER J 25  ? 0.511 0.538 0.501 0.009  -0.129 -0.010 25  SER JJJ O   
11924 C CB  . SER J 25  ? 0.523 0.551 0.505 0.007  -0.135 0.003  25  SER JJJ CB  
11925 O OG  . SER J 25  ? 0.530 0.545 0.512 0.024  -0.135 -0.000 25  SER JJJ OG  
11926 N N   . GLY J 26  ? 0.555 0.552 0.516 -0.010 -0.139 0.001  26  GLY JJJ N   
11927 C CA  . GLY J 26  ? 0.594 0.562 0.538 -0.011 -0.142 -0.002 26  GLY JJJ CA  
11928 C C   . GLY J 26  ? 0.606 0.589 0.550 -0.027 -0.141 -0.003 26  GLY JJJ C   
11929 O O   . GLY J 26  ? 0.600 0.619 0.560 -0.032 -0.137 -0.002 26  GLY JJJ O   
11930 N N   . ARG J 27  ? 0.669 0.626 0.594 -0.034 -0.145 -0.005 27  ARG JJJ N   
11931 C CA  . ARG J 27  ? 0.697 0.671 0.619 -0.051 -0.145 -0.004 27  ARG JJJ CA  
11932 C C   . ARG J 27  ? 0.642 0.618 0.569 -0.042 -0.141 -0.012 27  ARG JJJ C   
11933 O O   . ARG J 27  ? 0.630 0.612 0.550 -0.056 -0.142 -0.012 27  ARG JJJ O   
11934 C CB  . ARG J 27  ? 0.836 0.777 0.726 -0.074 -0.154 0.001  27  ARG JJJ CB  
11935 C CG  . ARG J 27  ? 0.936 0.894 0.822 -0.095 -0.158 0.012  27  ARG JJJ CG  
11936 C CD  . ARG J 27  ? 1.119 1.030 0.967 -0.117 -0.170 0.020  27  ARG JJJ CD  
11937 N NE  . ARG J 27  ? 1.242 1.091 1.067 -0.106 -0.176 0.014  27  ARG JJJ NE  
11938 C CZ  . ARG J 27  ? 1.331 1.135 1.142 -0.093 -0.182 0.015  27  ARG JJJ CZ  
11939 N NH1 . ARG J 27  ? 1.417 1.228 1.232 -0.092 -0.184 0.025  27  ARG JJJ NH1 
11940 N NH2 . ARG J 27  ? 1.375 1.126 1.165 -0.080 -0.186 0.007  27  ARG JJJ NH2 
11941 N N   . THR J 28  ? 0.613 0.588 0.553 -0.021 -0.137 -0.018 28  THR JJJ N   
11942 C CA  . THR J 28  ? 0.600 0.579 0.543 -0.014 -0.134 -0.025 28  THR JJJ CA  
11943 C C   . THR J 28  ? 0.557 0.568 0.526 -0.001 -0.128 -0.025 28  THR JJJ C   
11944 O O   . THR J 28  ? 0.570 0.582 0.543 0.010  -0.125 -0.029 28  THR JJJ O   
11945 C CB  . THR J 28  ? 0.630 0.573 0.554 -0.003 -0.137 -0.033 28  THR JJJ CB  
11946 O OG1 . THR J 28  ? 0.592 0.525 0.519 0.013  -0.137 -0.032 28  THR JJJ OG1 
11947 C CG2 . THR J 28  ? 0.648 0.552 0.540 -0.018 -0.144 -0.034 28  THR JJJ CG2 
11948 N N   . PHE J 29  ? 0.506 0.541 0.492 -0.003 -0.126 -0.020 29  PHE JJJ N   
11949 C CA  . PHE J 29  ? 0.499 0.555 0.505 0.007  -0.121 -0.019 29  PHE JJJ CA  
11950 C C   . PHE J 29  ? 0.501 0.570 0.514 0.009  -0.120 -0.020 29  PHE JJJ C   
11951 O O   . PHE J 29  ? 0.542 0.617 0.563 0.017  -0.118 -0.020 29  PHE JJJ O   
11952 C CB  . PHE J 29  ? 0.503 0.580 0.521 0.004  -0.120 -0.016 29  PHE JJJ CB  
11953 C CG  . PHE J 29  ? 0.502 0.591 0.536 0.014  -0.117 -0.017 29  PHE JJJ CG  
11954 C CD1 . PHE J 29  ? 0.503 0.587 0.540 0.020  -0.116 -0.019 29  PHE JJJ CD1 
11955 C CD2 . PHE J 29  ? 0.496 0.601 0.540 0.016  -0.117 -0.015 29  PHE JJJ CD2 
11956 C CE1 . PHE J 29  ? 0.519 0.609 0.568 0.026  -0.115 -0.019 29  PHE JJJ CE1 
11957 C CE2 . PHE J 29  ? 0.506 0.613 0.561 0.025  -0.116 -0.015 29  PHE JJJ CE2 
11958 C CZ  . PHE J 29  ? 0.516 0.614 0.572 0.028  -0.115 -0.018 29  PHE JJJ CZ  
11959 N N   . HIS J 30  ? 0.486 0.561 0.492 -0.001 -0.121 -0.018 30  HIS JJJ N   
11960 C CA  . HIS J 30  ? 0.481 0.571 0.491 -0.003 -0.121 -0.017 30  HIS JJJ CA  
11961 C C   . HIS J 30  ? 0.475 0.556 0.479 0.004  -0.120 -0.023 30  HIS JJJ C   
11962 O O   . HIS J 30  ? 0.491 0.589 0.503 0.004  -0.119 -0.021 30  HIS JJJ O   
11963 C CB  . HIS J 30  ? 0.468 0.568 0.470 -0.017 -0.123 -0.015 30  HIS JJJ CB  
11964 C CG  . HIS J 30  ? 0.504 0.576 0.481 -0.027 -0.126 -0.021 30  HIS JJJ CG  
11965 N ND1 . HIS J 30  ? 0.524 0.589 0.490 -0.028 -0.126 -0.027 30  HIS JJJ ND1 
11966 C CD2 . HIS J 30  ? 0.540 0.586 0.499 -0.034 -0.129 -0.022 30  HIS JJJ CD2 
11967 C CE1 . HIS J 30  ? 0.568 0.600 0.508 -0.036 -0.129 -0.033 30  HIS JJJ CE1 
11968 N NE2 . HIS J 30  ? 0.573 0.590 0.509 -0.040 -0.132 -0.029 30  HIS JJJ NE2 
11969 N N   . SER J 31  ? 0.481 0.539 0.472 0.009  -0.121 -0.029 31  SER JJJ N   
11970 C CA  . SER J 31  ? 0.505 0.559 0.489 0.018  -0.120 -0.037 31  SER JJJ CA  
11971 C C   . SER J 31  ? 0.495 0.564 0.493 0.029  -0.117 -0.035 31  SER JJJ C   
11972 O O   . SER J 31  ? 0.499 0.577 0.494 0.038  -0.116 -0.041 31  SER JJJ O   
11973 C CB  . SER J 31  ? 0.542 0.562 0.504 0.022  -0.122 -0.045 31  SER JJJ CB  
11974 O OG  . SER J 31  ? 0.565 0.568 0.525 0.029  -0.124 -0.044 31  SER JJJ OG  
11975 N N   . TYR J 32  ? 0.485 0.561 0.497 0.029  -0.117 -0.029 32  TYR JJJ N   
11976 C CA  . TYR J 32  ? 0.477 0.565 0.499 0.035  -0.115 -0.027 32  TYR JJJ CA  
11977 C C   . TYR J 32  ? 0.471 0.578 0.505 0.030  -0.115 -0.020 32  TYR JJJ C   
11978 O O   . TYR J 32  ? 0.446 0.551 0.485 0.025  -0.116 -0.015 32  TYR JJJ O   
11979 C CB  . TYR J 32  ? 0.473 0.552 0.497 0.038  -0.115 -0.026 32  TYR JJJ CB  
11980 C CG  . TYR J 32  ? 0.489 0.549 0.499 0.046  -0.117 -0.030 32  TYR JJJ CG  
11981 C CD1 . TYR J 32  ? 0.504 0.540 0.501 0.042  -0.120 -0.031 32  TYR JJJ CD1 
11982 C CD2 . TYR J 32  ? 0.501 0.570 0.511 0.058  -0.116 -0.033 32  TYR JJJ CD2 
11983 C CE1 . TYR J 32  ? 0.518 0.530 0.500 0.049  -0.123 -0.035 32  TYR JJJ CE1 
11984 C CE2 . TYR J 32  ? 0.522 0.572 0.519 0.070  -0.119 -0.037 32  TYR JJJ CE2 
11985 C CZ  . TYR J 32  ? 0.531 0.547 0.512 0.066  -0.123 -0.037 32  TYR JJJ CZ  
11986 O OH  . TYR J 32  ? 0.567 0.555 0.532 0.077  -0.127 -0.040 32  TYR JJJ OH  
11987 N N   . VAL J 33  ? 0.544 0.591 0.527 -0.008 -0.059 -0.035 33  VAL JJJ N   
11988 C CA  . VAL J 33  ? 0.569 0.601 0.532 -0.010 -0.073 -0.025 33  VAL JJJ CA  
11989 C C   . VAL J 33  ? 0.564 0.596 0.542 -0.004 -0.078 -0.019 33  VAL JJJ C   
11990 O O   . VAL J 33  ? 0.609 0.652 0.606 -0.004 -0.067 -0.017 33  VAL JJJ O   
11991 C CB  . VAL J 33  ? 0.587 0.610 0.532 -0.023 -0.064 -0.019 33  VAL JJJ CB  
11992 C CG1 . VAL J 33  ? 0.611 0.613 0.535 -0.027 -0.074 -0.007 33  VAL JJJ CG1 
11993 C CG2 . VAL J 33  ? 0.611 0.631 0.534 -0.029 -0.060 -0.025 33  VAL JJJ CG2 
11994 N N   . MET J 34  ? 0.539 0.559 0.508 0.003  -0.094 -0.018 34  MET JJJ N   
11995 C CA  . MET J 34  ? 0.550 0.566 0.527 0.007  -0.099 -0.015 34  MET JJJ CA  
11996 C C   . MET J 34  ? 0.599 0.594 0.557 -0.000 -0.107 -0.008 34  MET JJJ C   
11997 O O   . MET J 34  ? 0.610 0.586 0.546 -0.003 -0.114 -0.004 34  MET JJJ O   
11998 C CB  . MET J 34  ? 0.549 0.566 0.531 0.020  -0.106 -0.023 34  MET JJJ CB  
11999 C CG  . MET J 34  ? 0.537 0.574 0.539 0.024  -0.096 -0.032 34  MET JJJ CG  
12000 S SD  . MET J 34  ? 0.513 0.560 0.529 0.022  -0.078 -0.029 34  MET JJJ SD  
12001 C CE  . MET J 34  ? 0.512 0.552 0.525 0.028  -0.085 -0.025 34  MET JJJ CE  
12002 N N   . ALA J 35  ? 0.631 0.629 0.599 -0.005 -0.106 -0.005 35  ALA JJJ N   
12003 C CA  . ALA J 35  ? 0.688 0.668 0.643 -0.017 -0.111 0.000  35  ALA JJJ CA  
12004 C C   . ALA J 35  ? 0.702 0.680 0.662 -0.016 -0.119 -0.003 35  ALA JJJ C   
12005 O O   . ALA J 35  ? 0.747 0.743 0.722 -0.008 -0.118 -0.007 35  ALA JJJ O   
12006 C CB  . ALA J 35  ? 0.693 0.685 0.657 -0.032 -0.099 0.005  35  ALA JJJ CB  
12007 N N   . TRP J 36  ? 0.717 0.669 0.662 -0.025 -0.125 -0.002 36  TRP JJJ N   
12008 C CA  . TRP J 36  ? 0.693 0.638 0.638 -0.030 -0.132 -0.007 36  TRP JJJ CA  
12009 C C   . TRP J 36  ? 0.701 0.647 0.651 -0.052 -0.129 -0.004 36  TRP JJJ C   
12010 O O   . TRP J 36  ? 0.753 0.677 0.688 -0.063 -0.123 0.002  36  TRP JJJ O   
12011 C CB  . TRP J 36  ? 0.707 0.615 0.631 -0.022 -0.141 -0.010 36  TRP JJJ CB  
12012 C CG  . TRP J 36  ? 0.671 0.585 0.598 -0.002 -0.144 -0.017 36  TRP JJJ CG  
12013 C CD1 . TRP J 36  ? 0.659 0.570 0.584 0.012  -0.145 -0.016 36  TRP JJJ CD1 
12014 C CD2 . TRP J 36  ? 0.623 0.550 0.556 0.005  -0.144 -0.025 36  TRP JJJ CD2 
12015 N NE1 . TRP J 36  ? 0.646 0.570 0.581 0.026  -0.144 -0.025 36  TRP JJJ NE1 
12016 C CE2 . TRP J 36  ? 0.611 0.542 0.549 0.022  -0.142 -0.030 36  TRP JJJ CE2 
12017 C CE3 . TRP J 36  ? 0.631 0.567 0.565 -0.001 -0.146 -0.030 36  TRP JJJ CE3 
12018 C CZ2 . TRP J 36  ? 0.599 0.538 0.540 0.031  -0.138 -0.039 36  TRP JJJ CZ2 
12019 C CZ3 . TRP J 36  ? 0.636 0.579 0.568 0.009  -0.145 -0.037 36  TRP JJJ CZ3 
12020 C CH2 . TRP J 36  ? 0.604 0.547 0.539 0.025  -0.139 -0.041 36  TRP JJJ CH2 
12021 N N   . PHE J 37  ? 0.666 0.637 0.636 -0.059 -0.132 -0.009 37  PHE JJJ N   
12022 C CA  . PHE J 37  ? 0.684 0.662 0.665 -0.082 -0.131 -0.011 37  PHE JJJ CA  
12023 C C   . PHE J 37  ? 0.699 0.669 0.674 -0.085 -0.144 -0.021 37  PHE JJJ C   
12024 O O   . PHE J 37  ? 0.672 0.641 0.638 -0.068 -0.152 -0.025 37  PHE JJJ O   
12025 C CB  . PHE J 37  ? 0.663 0.689 0.680 -0.086 -0.125 -0.009 37  PHE JJJ CB  
12026 C CG  . PHE J 37  ? 0.661 0.693 0.684 -0.088 -0.108 -0.002 37  PHE JJJ CG  
12027 C CD1 . PHE J 37  ? 0.647 0.678 0.663 -0.071 -0.103 0.002  37  PHE JJJ CD1 
12028 C CD2 . PHE J 37  ? 0.680 0.721 0.717 -0.109 -0.096 -0.002 37  PHE JJJ CD2 
12029 C CE1 . PHE J 37  ? 0.643 0.678 0.660 -0.075 -0.087 0.006  37  PHE JJJ CE1 
12030 C CE2 . PHE J 37  ? 0.674 0.719 0.713 -0.112 -0.078 0.003  37  PHE JJJ CE2 
12031 C CZ  . PHE J 37  ? 0.661 0.703 0.688 -0.095 -0.074 0.007  37  PHE JJJ CZ  
12032 N N   . ARG J 38  ? 0.711 0.677 0.691 -0.108 -0.146 -0.027 38  ARG JJJ N   
12033 C CA  . ARG J 38  ? 0.736 0.700 0.712 -0.115 -0.160 -0.040 38  ARG JJJ CA  
12034 C C   . ARG J 38  ? 0.747 0.746 0.754 -0.139 -0.163 -0.047 38  ARG JJJ C   
12035 O O   . ARG J 38  ? 0.744 0.755 0.770 -0.154 -0.150 -0.042 38  ARG JJJ O   
12036 C CB  . ARG J 38  ? 0.770 0.676 0.712 -0.119 -0.161 -0.045 38  ARG JJJ CB  
12037 C CG  . ARG J 38  ? 0.809 0.683 0.745 -0.144 -0.151 -0.043 38  ARG JJJ CG  
12038 C CD  . ARG J 38  ? 0.842 0.650 0.740 -0.140 -0.150 -0.044 38  ARG JJJ CD  
12039 N NE  . ARG J 38  ? 0.869 0.637 0.754 -0.162 -0.139 -0.038 38  ARG JJJ NE  
12040 C CZ  . ARG J 38  ? 0.915 0.618 0.767 -0.163 -0.137 -0.037 38  ARG JJJ CZ  
12041 N NH1 . ARG J 38  ? 0.913 0.586 0.746 -0.142 -0.145 -0.042 38  ARG JJJ NH1 
12042 N NH2 . ARG J 38  ? 0.971 0.636 0.808 -0.185 -0.124 -0.030 38  ARG JJJ NH2 
12043 N N   . GLN J 39  ? 0.762 0.779 0.772 -0.143 -0.178 -0.059 39  GLN JJJ N   
12044 C CA  . GLN J 39  ? 0.776 0.835 0.820 -0.165 -0.186 -0.068 39  GLN JJJ CA  
12045 C C   . GLN J 39  ? 0.808 0.850 0.834 -0.178 -0.201 -0.086 39  GLN JJJ C   
12046 O O   . GLN J 39  ? 0.822 0.866 0.828 -0.162 -0.214 -0.090 39  GLN JJJ O   
12047 C CB  . GLN J 39  ? 0.754 0.874 0.832 -0.149 -0.194 -0.063 39  GLN JJJ CB  
12048 C CG  . GLN J 39  ? 0.787 0.959 0.907 -0.169 -0.205 -0.074 39  GLN JJJ CG  
12049 C CD  . GLN J 39  ? 0.779 1.009 0.938 -0.151 -0.209 -0.066 39  GLN JJJ CD  
12050 O OE1 . GLN J 39  ? 0.815 1.047 0.962 -0.123 -0.212 -0.055 39  GLN JJJ OE1 
12051 N NE2 . GLN J 39  ? 0.772 1.050 0.982 -0.167 -0.208 -0.071 39  GLN JJJ NE2 
12052 N N   . ALA J 40  ? 0.849 0.871 0.877 -0.208 -0.196 -0.096 40  ALA JJJ N   
12053 C CA  . ALA J 40  ? 0.891 0.902 0.909 -0.230 -0.209 -0.117 40  ALA JJJ CA  
12054 C C   . ALA J 40  ? 0.878 0.961 0.940 -0.242 -0.226 -0.128 40  ALA JJJ C   
12055 O O   . ALA J 40  ? 0.839 0.969 0.944 -0.243 -0.221 -0.120 40  ALA JJJ O   
12056 C CB  . ALA J 40  ? 0.935 0.893 0.940 -0.258 -0.194 -0.123 40  ALA JJJ CB  
12057 N N   . PRO J 41  ? 0.928 1.023 0.980 -0.250 -0.248 -0.146 41  PRO JJJ N   
12058 C CA  . PRO J 41  ? 0.914 1.081 1.008 -0.261 -0.269 -0.157 41  PRO JJJ CA  
12059 C C   . PRO J 41  ? 0.903 1.092 1.044 -0.298 -0.258 -0.167 41  PRO JJJ C   
12060 O O   . PRO J 41  ? 0.888 1.027 1.013 -0.324 -0.244 -0.176 41  PRO JJJ O   
12061 C CB  . PRO J 41  ? 0.960 1.121 1.021 -0.266 -0.292 -0.177 41  PRO JJJ CB  
12062 C CG  . PRO J 41  ? 0.998 1.075 1.004 -0.265 -0.278 -0.181 41  PRO JJJ CG  
12063 C CD  . PRO J 41  ? 0.973 1.015 0.974 -0.247 -0.253 -0.158 41  PRO JJJ CD  
12064 N N   . GLY J 42  ? 0.886 1.146 1.084 -0.298 -0.262 -0.163 42  GLY JJJ N   
12065 C CA  . GLY J 42  ? 0.919 1.212 1.171 -0.331 -0.249 -0.172 42  GLY JJJ CA  
12066 C C   . GLY J 42  ? 0.936 1.204 1.194 -0.332 -0.215 -0.155 42  GLY JJJ C   
12067 O O   . GLY J 42  ? 0.957 1.257 1.263 -0.357 -0.201 -0.160 42  GLY JJJ O   
12068 N N   . LYS J 43  ? 0.961 1.177 1.175 -0.305 -0.203 -0.135 43  LYS JJJ N   
12069 C CA  . LYS J 43  ? 0.971 1.158 1.180 -0.304 -0.173 -0.118 43  LYS JJJ CA  
12070 C C   . LYS J 43  ? 0.923 1.143 1.146 -0.269 -0.171 -0.100 43  LYS JJJ C   
12071 O O   . LYS J 43  ? 0.921 1.164 1.141 -0.243 -0.191 -0.098 43  LYS JJJ O   
12072 C CB  . LYS J 43  ? 1.038 1.137 1.185 -0.303 -0.160 -0.111 43  LYS JJJ CB  
12073 C CG  . LYS J 43  ? 1.115 1.170 1.253 -0.342 -0.145 -0.121 43  LYS JJJ CG  
12074 C CD  . LYS J 43  ? 1.190 1.159 1.268 -0.342 -0.143 -0.120 43  LYS JJJ CD  
12075 C CE  . LYS J 43  ? 1.289 1.211 1.360 -0.382 -0.122 -0.127 43  LYS JJJ CE  
12076 N NZ  . LYS J 43  ? 1.348 1.225 1.394 -0.401 -0.131 -0.146 43  LYS JJJ NZ  
12077 N N   . GLU J 44  ? 0.932 1.143 1.161 -0.270 -0.145 -0.088 44  GLU JJJ N   
12078 C CA  . GLU J 44  ? 0.895 1.124 1.131 -0.240 -0.138 -0.072 44  GLU JJJ CA  
12079 C C   . GLU J 44  ? 0.880 1.049 1.057 -0.216 -0.137 -0.060 44  GLU JJJ C   
12080 O O   . GLU J 44  ? 0.892 1.005 1.027 -0.226 -0.138 -0.063 44  GLU JJJ O   
12081 C CB  . GLU J 44  ? 0.918 1.160 1.180 -0.253 -0.108 -0.067 44  GLU JJJ CB  
12082 C CG  . GLU J 44  ? 0.955 1.248 1.275 -0.284 -0.101 -0.082 44  GLU JJJ CG  
12083 C CD  . GLU J 44  ? 0.961 1.334 1.341 -0.273 -0.124 -0.092 44  GLU JJJ CD  
12084 O OE1 . GLU J 44  ? 0.932 1.330 1.320 -0.239 -0.132 -0.082 44  GLU JJJ OE1 
12085 O OE2 . GLU J 44  ? 0.988 1.400 1.408 -0.299 -0.134 -0.109 44  GLU JJJ OE2 
12086 N N   . ARG J 45  ? 0.848 1.028 1.024 -0.188 -0.135 -0.048 45  ARG JJJ N   
12087 C CA  . ARG J 45  ? 0.864 0.996 0.994 -0.167 -0.131 -0.037 45  ARG JJJ CA  
12088 C C   . ARG J 45  ? 0.882 0.967 0.985 -0.182 -0.110 -0.031 45  ARG JJJ C   
12089 O O   . ARG J 45  ? 0.935 1.036 1.057 -0.193 -0.092 -0.028 45  ARG JJJ O   
12090 C CB  . ARG J 45  ? 0.842 1.001 0.985 -0.139 -0.128 -0.028 45  ARG JJJ CB  
12091 C CG  . ARG J 45  ? 0.840 1.006 0.972 -0.116 -0.147 -0.028 45  ARG JJJ CG  
12092 C CD  . ARG J 45  ? 0.817 1.013 0.968 -0.092 -0.145 -0.020 45  ARG JJJ CD  
12093 N NE  . ARG J 45  ? 0.840 1.064 0.999 -0.079 -0.166 -0.022 45  ARG JJJ NE  
12094 C CZ  . ARG J 45  ? 0.827 1.057 0.981 -0.054 -0.170 -0.013 45  ARG JJJ CZ  
12095 N NH1 . ARG J 45  ? 0.817 1.030 0.963 -0.039 -0.153 -0.005 45  ARG JJJ NH1 
12096 N NH2 . ARG J 45  ? 0.790 1.043 0.945 -0.044 -0.190 -0.014 45  ARG JJJ NH2 
12097 N N   . GLU J 46  ? 0.843 0.872 0.901 -0.180 -0.114 -0.029 46  GLU JJJ N   
12098 C CA  . GLU J 46  ? 0.845 0.817 0.865 -0.189 -0.100 -0.020 46  GLU JJJ CA  
12099 C C   . GLU J 46  ? 0.796 0.746 0.786 -0.160 -0.102 -0.010 46  GLU JJJ C   
12100 O O   . GLU J 46  ? 0.779 0.728 0.761 -0.140 -0.116 -0.012 46  GLU JJJ O   
12101 C CB  . GLU J 46  ? 0.901 0.829 0.898 -0.207 -0.105 -0.028 46  GLU JJJ CB  
12102 C CG  . GLU J 46  ? 0.978 0.836 0.929 -0.212 -0.095 -0.018 46  GLU JJJ CG  
12103 C CD  . GLU J 46  ? 1.055 0.863 0.983 -0.229 -0.099 -0.026 46  GLU JJJ CD  
12104 O OE1 . GLU J 46  ? 1.088 0.917 1.037 -0.238 -0.110 -0.042 46  GLU JJJ OE1 
12105 O OE2 . GLU J 46  ? 1.113 0.857 1.001 -0.230 -0.092 -0.016 46  GLU JJJ OE2 
12106 N N   . PHE J 47  ? 0.764 0.701 0.739 -0.160 -0.087 0.001  47  PHE JJJ N   
12107 C CA  . PHE J 47  ? 0.740 0.655 0.685 -0.137 -0.089 0.009  47  PHE JJJ CA  
12108 C C   . PHE J 47  ? 0.762 0.622 0.669 -0.130 -0.100 0.012  47  PHE JJJ C   
12109 O O   . PHE J 47  ? 0.801 0.621 0.686 -0.147 -0.096 0.014  47  PHE JJJ O   
12110 C CB  . PHE J 47  ? 0.742 0.651 0.672 -0.143 -0.071 0.018  47  PHE JJJ CB  
12111 C CG  . PHE J 47  ? 0.734 0.619 0.631 -0.122 -0.077 0.026  47  PHE JJJ CG  
12112 C CD1 . PHE J 47  ? 0.693 0.609 0.606 -0.103 -0.080 0.023  47  PHE JJJ CD1 
12113 C CD2 . PHE J 47  ? 0.789 0.620 0.639 -0.122 -0.080 0.035  47  PHE JJJ CD2 
12114 C CE1 . PHE J 47  ? 0.697 0.597 0.584 -0.086 -0.086 0.026  47  PHE JJJ CE1 
12115 C CE2 . PHE J 47  ? 0.795 0.610 0.618 -0.102 -0.089 0.041  47  PHE JJJ CE2 
12116 C CZ  . PHE J 47  ? 0.753 0.607 0.597 -0.085 -0.092 0.035  47  PHE JJJ CZ  
12117 N N   . VAL J 48  ? 0.740 0.598 0.639 -0.105 -0.113 0.011  48  VAL JJJ N   
12118 C CA  . VAL J 48  ? 0.784 0.594 0.652 -0.092 -0.124 0.012  48  VAL JJJ CA  
12119 C C   . VAL J 48  ? 0.781 0.574 0.625 -0.074 -0.126 0.021  48  VAL JJJ C   
12120 O O   . VAL J 48  ? 0.824 0.569 0.633 -0.073 -0.128 0.030  48  VAL JJJ O   
12121 C CB  . VAL J 48  ? 0.761 0.581 0.641 -0.078 -0.136 -0.000 48  VAL JJJ CB  
12122 C CG1 . VAL J 48  ? 0.780 0.555 0.634 -0.061 -0.145 -0.001 48  VAL JJJ CG1 
12123 C CG2 . VAL J 48  ? 0.779 0.612 0.676 -0.098 -0.137 -0.011 48  VAL JJJ CG2 
12124 N N   . ALA J 49  ? 0.743 0.573 0.604 -0.059 -0.127 0.019  49  ALA JJJ N   
12125 C CA  . ALA J 49  ? 0.762 0.585 0.606 -0.041 -0.133 0.024  49  ALA JJJ CA  
12126 C C   . ALA J 49  ? 0.704 0.573 0.571 -0.035 -0.127 0.020  49  ALA JJJ C   
12127 O O   . ALA J 49  ? 0.631 0.533 0.528 -0.036 -0.122 0.013  49  ALA JJJ O   
12128 C CB  . ALA J 49  ? 0.773 0.576 0.610 -0.019 -0.148 0.020  49  ALA JJJ CB  
12129 N N   . ALA J 50  ? 0.739 0.606 0.590 -0.028 -0.128 0.023  50  ALA JJJ N   
12130 C CA  . ALA J 50  ? 0.699 0.602 0.568 -0.023 -0.122 0.017  50  ALA JJJ CA  
12131 C C   . ALA J 50  ? 0.693 0.589 0.543 -0.009 -0.135 0.017  50  ALA JJJ C   
12132 O O   . ALA J 50  ? 0.740 0.601 0.555 -0.006 -0.145 0.026  50  ALA JJJ O   
12133 C CB  . ALA J 50  ? 0.713 0.629 0.584 -0.040 -0.104 0.020  50  ALA JJJ CB  
12134 N N   . ILE J 51  ? 0.657 0.584 0.529 -0.000 -0.134 0.007  51  ILE JJJ N   
12135 C CA  . ILE J 51  ? 0.689 0.622 0.554 0.013  -0.147 0.002  51  ILE JJJ CA  
12136 C C   . ILE J 51  ? 0.668 0.630 0.544 0.007  -0.135 -0.007 51  ILE JJJ C   
12137 O O   . ILE J 51  ? 0.614 0.599 0.521 0.004  -0.121 -0.014 51  ILE JJJ O   
12138 C CB  . ILE J 51  ? 0.677 0.617 0.563 0.031  -0.159 -0.006 51  ILE JJJ CB  
12139 C CG1 . ILE J 51  ? 0.701 0.651 0.585 0.046  -0.176 -0.012 51  ILE JJJ CG1 
12140 C CG2 . ILE J 51  ? 0.642 0.609 0.564 0.031  -0.147 -0.016 51  ILE JJJ CG2 
12141 C CD1 . ILE J 51  ? 0.705 0.657 0.609 0.066  -0.189 -0.018 51  ILE JJJ CD1 
12142 N N   . SER J 52  ? 0.689 0.647 0.539 0.005  -0.140 -0.007 52  SER JJJ N   
12143 C CA  . SER J 52  ? 0.686 0.666 0.540 -0.003 -0.129 -0.018 52  SER JJJ CA  
12144 C C   . SER J 52  ? 0.670 0.679 0.555 0.008  -0.136 -0.033 52  SER JJJ C   
12145 O O   . SER J 52  ? 0.659 0.671 0.561 0.022  -0.150 -0.035 52  SER JJJ O   
12146 C CB  . SER J 52  ? 0.732 0.696 0.541 -0.010 -0.132 -0.014 52  SER JJJ CB  
12147 O OG  . SER J 52  ? 0.740 0.719 0.552 -0.023 -0.114 -0.024 52  SER JJJ OG  
12148 N N   . TRP J 53  ? 0.644 0.674 0.539 0.000  -0.125 -0.046 53  TRP JJJ N   
12149 C CA  . TRP J 53  ? 0.611 0.668 0.540 0.004  -0.124 -0.064 53  TRP JJJ CA  
12150 C C   . TRP J 53  ? 0.630 0.699 0.561 0.017  -0.151 -0.070 53  TRP JJJ C   
12151 O O   . TRP J 53  ? 0.607 0.692 0.572 0.027  -0.153 -0.077 53  TRP JJJ O   
12152 C CB  . TRP J 53  ? 0.584 0.653 0.513 -0.010 -0.108 -0.077 53  TRP JJJ CB  
12153 C CG  . TRP J 53  ? 0.577 0.634 0.502 -0.020 -0.083 -0.071 53  TRP JJJ CG  
12154 C CD1 . TRP J 53  ? 0.552 0.612 0.506 -0.020 -0.064 -0.069 53  TRP JJJ CD1 
12155 C CD2 . TRP J 53  ? 0.602 0.644 0.493 -0.031 -0.075 -0.066 53  TRP JJJ CD2 
12156 N NE1 . TRP J 53  ? 0.562 0.614 0.508 -0.028 -0.046 -0.063 53  TRP JJJ NE1 
12157 C CE2 . TRP J 53  ? 0.585 0.626 0.494 -0.037 -0.050 -0.063 53  TRP JJJ CE2 
12158 C CE3 . TRP J 53  ? 0.635 0.663 0.481 -0.037 -0.085 -0.064 53  TRP JJJ CE3 
12159 C CZ2 . TRP J 53  ? 0.591 0.621 0.480 -0.048 -0.033 -0.059 53  TRP JJJ CZ2 
12160 C CZ3 . TRP J 53  ? 0.661 0.674 0.480 -0.050 -0.067 -0.060 53  TRP JJJ CZ3 
12161 C CH2 . TRP J 53  ? 0.644 0.659 0.487 -0.056 -0.040 -0.058 53  TRP JJJ CH2 
12162 N N   . SER J 54  ? 0.655 0.715 0.550 0.019  -0.169 -0.067 54  SER JJJ N   
12163 C CA  . SER J 54  ? 0.690 0.763 0.584 0.034  -0.199 -0.071 54  SER JJJ CA  
12164 C C   . SER J 54  ? 0.716 0.770 0.609 0.053  -0.215 -0.058 54  SER JJJ C   
12165 O O   . SER J 54  ? 0.722 0.786 0.619 0.070  -0.240 -0.060 54  SER JJJ O   
12166 C CB  . SER J 54  ? 0.723 0.786 0.569 0.030  -0.215 -0.069 54  SER JJJ CB  
12167 O OG  . SER J 54  ? 0.761 0.782 0.561 0.029  -0.215 -0.046 54  SER JJJ OG  
12168 N N   . SER J 55  ? 0.730 0.756 0.617 0.049  -0.201 -0.044 55  SER JJJ N   
12169 C CA  . SER J 55  ? 0.776 0.771 0.650 0.063  -0.212 -0.029 55  SER JJJ CA  
12170 C C   . SER J 55  ? 0.840 0.794 0.657 0.062  -0.223 -0.011 55  SER JJJ C   
12171 O O   . SER J 55  ? 0.875 0.796 0.678 0.071  -0.231 0.002  55  SER JJJ O   
12172 C CB  . SER J 55  ? 0.779 0.790 0.682 0.085  -0.231 -0.038 55  SER JJJ CB  
12173 O OG  . SER J 55  ? 0.762 0.805 0.714 0.085  -0.216 -0.054 55  SER JJJ OG  
12174 N N   . THR J 56  ? 0.901 0.853 0.685 0.050  -0.223 -0.009 56  THR JJJ N   
12175 C CA  . THR J 56  ? 1.058 0.978 0.785 0.057  -0.244 0.006  56  THR JJJ CA  
12176 C C   . THR J 56  ? 1.118 0.989 0.797 0.043  -0.230 0.026  56  THR JJJ C   
12177 O O   . THR J 56  ? 1.266 1.097 0.899 0.052  -0.246 0.043  56  THR JJJ O   
12178 C CB  . THR J 56  ? 1.143 1.083 0.848 0.055  -0.257 -0.003 56  THR JJJ CB  
12179 O OG1 . THR J 56  ? 1.204 1.174 0.940 0.077  -0.285 -0.014 56  THR JJJ OG1 
12180 C CG2 . THR J 56  ? 1.213 1.112 0.844 0.051  -0.266 0.014  56  THR JJJ CG2 
12181 N N   . PRO J 57  ? 0.979 0.852 0.661 0.020  -0.201 0.024  57  PRO JJJ N   
12182 C CA  . PRO J 57  ? 0.941 0.774 0.599 0.007  -0.185 0.040  57  PRO JJJ CA  
12183 C C   . PRO J 57  ? 0.880 0.723 0.587 0.011  -0.179 0.036  57  PRO JJJ C   
12184 O O   . PRO J 57  ? 0.800 0.679 0.551 0.009  -0.169 0.022  57  PRO JJJ O   
12185 C CB  . PRO J 57  ? 0.941 0.779 0.584 -0.017 -0.159 0.038  57  PRO JJJ CB  
12186 C CG  . PRO J 57  ? 0.945 0.825 0.608 -0.016 -0.160 0.019  57  PRO JJJ CG  
12187 C CD  . PRO J 57  ? 0.915 0.822 0.616 0.005  -0.183 0.008  57  PRO JJJ CD  
12188 N N   . THR J 58  ? 0.881 0.687 0.575 0.018  -0.188 0.048  58  THR JJJ N   
12189 C CA  . THR J 58  ? 0.842 0.642 0.564 0.015  -0.179 0.047  58  THR JJJ CA  
12190 C C   . THR J 58  ? 0.876 0.638 0.569 -0.007 -0.163 0.060  58  THR JJJ C   
12191 O O   . THR J 58  ? 0.931 0.659 0.575 -0.012 -0.164 0.073  58  THR JJJ O   
12192 C CB  . THR J 58  ? 0.827 0.614 0.562 0.037  -0.197 0.046  58  THR JJJ CB  
12193 O OG1 . THR J 58  ? 0.865 0.603 0.554 0.048  -0.212 0.061  58  THR JJJ OG1 
12194 C CG2 . THR J 58  ? 0.786 0.616 0.560 0.055  -0.208 0.030  58  THR JJJ CG2 
12195 N N   . TYR J 59  ? 0.868 0.639 0.590 -0.020 -0.148 0.055  59  TYR JJJ N   
12196 C CA  . TYR J 59  ? 0.894 0.638 0.601 -0.044 -0.131 0.064  59  TYR JJJ CA  
12197 C C   . TYR J 59  ? 0.871 0.604 0.599 -0.045 -0.133 0.060  59  TYR JJJ C   
12198 O O   . TYR J 59  ? 0.818 0.582 0.583 -0.034 -0.139 0.048  59  TYR JJJ O   
12199 C CB  . TYR J 59  ? 0.887 0.669 0.617 -0.064 -0.108 0.057  59  TYR JJJ CB  
12200 C CG  . TYR J 59  ? 0.907 0.705 0.621 -0.065 -0.102 0.056  59  TYR JJJ CG  
12201 C CD1 . TYR J 59  ? 0.869 0.709 0.614 -0.053 -0.104 0.043  59  TYR JJJ CD1 
12202 C CD2 . TYR J 59  ? 0.979 0.749 0.648 -0.080 -0.089 0.066  59  TYR JJJ CD2 
12203 C CE1 . TYR J 59  ? 0.882 0.736 0.613 -0.057 -0.097 0.039  59  TYR JJJ CE1 
12204 C CE2 . TYR J 59  ? 0.996 0.780 0.647 -0.083 -0.082 0.062  59  TYR JJJ CE2 
12205 C CZ  . TYR J 59  ? 0.945 0.772 0.629 -0.072 -0.086 0.048  59  TYR JJJ CZ  
12206 O OH  . TYR J 59  ? 0.961 0.799 0.626 -0.076 -0.077 0.041  59  TYR JJJ OH  
12207 N N   . TYR J 60  ? 0.917 0.606 0.620 -0.061 -0.126 0.069  60  TYR JJJ N   
12208 C CA  . TYR J 60  ? 0.927 0.595 0.642 -0.066 -0.127 0.065  60  TYR JJJ CA  
12209 C C   . TYR J 60  ? 0.937 0.591 0.649 -0.099 -0.107 0.067  60  TYR JJJ C   
12210 O O   . TYR J 60  ? 0.943 0.568 0.620 -0.113 -0.095 0.079  60  TYR JJJ O   
12211 C CB  . TYR J 60  ? 0.972 0.586 0.654 -0.047 -0.143 0.073  60  TYR JJJ CB  
12212 C CG  . TYR J 60  ? 0.944 0.579 0.640 -0.015 -0.163 0.067  60  TYR JJJ CG  
12213 C CD1 . TYR J 60  ? 0.896 0.562 0.632 -0.005 -0.167 0.051  60  TYR JJJ CD1 
12214 C CD2 . TYR J 60  ? 0.948 0.577 0.619 0.003  -0.176 0.076  60  TYR JJJ CD2 
12215 C CE1 . TYR J 60  ? 0.871 0.557 0.624 0.022  -0.182 0.044  60  TYR JJJ CE1 
12216 C CE2 . TYR J 60  ? 0.925 0.579 0.617 0.031  -0.194 0.068  60  TYR JJJ CE2 
12217 C CZ  . TYR J 60  ? 0.889 0.573 0.624 0.040  -0.195 0.051  60  TYR JJJ CZ  
12218 O OH  . TYR J 60  ? 0.884 0.597 0.645 0.064  -0.208 0.041  60  TYR JJJ OH  
12219 N N   . GLY J 61  ? 0.933 0.606 0.680 -0.111 -0.104 0.055  61  GLY JJJ N   
12220 C CA  . GLY J 61  ? 0.966 0.624 0.716 -0.142 -0.088 0.053  61  GLY JJJ CA  
12221 C C   . GLY J 61  ? 1.051 0.633 0.755 -0.148 -0.088 0.064  61  GLY JJJ C   
12222 O O   . GLY J 61  ? 1.066 0.614 0.750 -0.123 -0.105 0.067  61  GLY JJJ O   
12223 N N   . GLU J 62  ? 1.114 0.668 0.803 -0.179 -0.069 0.069  62  GLU JJJ N   
12224 C CA  . GLU J 62  ? 1.223 0.693 0.857 -0.185 -0.064 0.084  62  GLU JJJ CA  
12225 C C   . GLU J 62  ? 1.215 0.650 0.851 -0.178 -0.077 0.075  62  GLU JJJ C   
12226 O O   . GLU J 62  ? 1.250 0.623 0.845 -0.159 -0.086 0.087  62  GLU JJJ O   
12227 C CB  . GLU J 62  ? 1.299 0.746 0.916 -0.223 -0.036 0.091  62  GLU JJJ CB  
12228 C CG  . GLU J 62  ? 1.432 0.787 0.978 -0.226 -0.029 0.113  62  GLU JJJ CG  
12229 C CD  . GLU J 62  ? 1.480 0.804 0.977 -0.190 -0.048 0.131  62  GLU JJJ CD  
12230 O OE1 . GLU J 62  ? 1.471 0.846 0.980 -0.174 -0.056 0.130  62  GLU JJJ OE1 
12231 O OE2 . GLU J 62  ? 1.566 0.819 1.019 -0.175 -0.058 0.145  62  GLU JJJ OE2 
12232 N N   . SER J 63  ? 1.175 0.651 0.856 -0.187 -0.079 0.055  63  SER JJJ N   
12233 C CA  . SER J 63  ? 1.229 0.669 0.910 -0.189 -0.086 0.042  63  SER JJJ CA  
12234 C C   . SER J 63  ? 1.207 0.649 0.890 -0.150 -0.108 0.038  63  SER JJJ C   
12235 O O   . SER J 63  ? 1.259 0.661 0.933 -0.145 -0.113 0.029  63  SER JJJ O   
12236 C CB  . SER J 63  ? 1.201 0.686 0.926 -0.217 -0.082 0.021  63  SER JJJ CB  
12237 O OG  . SER J 63  ? 1.144 0.708 0.912 -0.204 -0.092 0.011  63  SER JJJ OG  
12238 N N   . VAL J 64  ? 1.147 0.631 0.840 -0.123 -0.118 0.042  64  VAL JJJ N   
12239 C CA  . VAL J 64  ? 1.138 0.628 0.837 -0.087 -0.136 0.037  64  VAL JJJ CA  
12240 C C   . VAL J 64  ? 1.183 0.643 0.849 -0.060 -0.145 0.055  64  VAL JJJ C   
12241 O O   . VAL J 64  ? 1.176 0.631 0.846 -0.030 -0.159 0.051  64  VAL JJJ O   
12242 C CB  . VAL J 64  ? 1.055 0.622 0.797 -0.078 -0.141 0.024  64  VAL JJJ CB  
12243 C CG1 . VAL J 64  ? 1.013 0.610 0.784 -0.102 -0.137 0.007  64  VAL JJJ CG1 
12244 C CG2 . VAL J 64  ? 1.018 0.629 0.769 -0.075 -0.139 0.032  64  VAL JJJ CG2 
12245 N N   . LYS J 65  ? 1.247 0.689 0.883 -0.071 -0.137 0.073  65  LYS JJJ N   
12246 C CA  . LYS J 65  ? 1.283 0.696 0.881 -0.046 -0.149 0.091  65  LYS JJJ CA  
12247 C C   . LYS J 65  ? 1.298 0.648 0.872 -0.022 -0.162 0.096  65  LYS JJJ C   
12248 O O   . LYS J 65  ? 1.355 0.649 0.912 -0.037 -0.152 0.096  65  LYS JJJ O   
12249 C CB  . LYS J 65  ? 1.363 0.749 0.920 -0.067 -0.135 0.110  65  LYS JJJ CB  
12250 C CG  . LYS J 65  ? 1.401 0.810 0.940 -0.050 -0.145 0.120  65  LYS JJJ CG  
12251 C CD  . LYS J 65  ? 1.481 0.869 0.977 -0.072 -0.128 0.136  65  LYS JJJ CD  
12252 C CE  . LYS J 65  ? 1.526 0.916 0.986 -0.051 -0.144 0.148  65  LYS JJJ CE  
12253 N NZ  . LYS J 65  ? 1.637 0.953 1.022 -0.055 -0.140 0.174  65  LYS JJJ NZ  
12254 N N   . GLY J 66  ? 1.259 0.619 0.837 0.015  -0.182 0.097  66  GLY JJJ N   
12255 C CA  . GLY J 66  ? 1.318 0.624 0.880 0.045  -0.196 0.102  66  GLY JJJ CA  
12256 C C   . GLY J 66  ? 1.263 0.592 0.868 0.059  -0.199 0.078  66  GLY JJJ C   
12257 O O   . GLY J 66  ? 1.287 0.603 0.898 0.094  -0.214 0.077  66  GLY JJJ O   
12258 N N   . ARG J 67  ? 1.209 0.573 0.845 0.035  -0.186 0.060  67  ARG JJJ N   
12259 C CA  . ARG J 67  ? 1.170 0.549 0.838 0.043  -0.186 0.037  67  ARG JJJ CA  
12260 C C   . ARG J 67  ? 1.091 0.550 0.801 0.054  -0.191 0.023  67  ARG JJJ C   
12261 O O   . ARG J 67  ? 1.060 0.532 0.793 0.073  -0.195 0.008  67  ARG JJJ O   
12262 C CB  . ARG J 67  ? 1.175 0.535 0.841 0.009  -0.171 0.025  67  ARG JJJ CB  
12263 C CG  . ARG J 67  ? 1.260 0.535 0.885 -0.005 -0.163 0.035  67  ARG JJJ CG  
12264 C CD  . ARG J 67  ? 1.272 0.530 0.901 -0.038 -0.150 0.018  67  ARG JJJ CD  
12265 N NE  . ARG J 67  ? 1.217 0.532 0.868 -0.071 -0.142 0.013  67  ARG JJJ NE  
12266 C CZ  . ARG J 67  ? 1.165 0.535 0.850 -0.083 -0.142 -0.007 67  ARG JJJ CZ  
12267 N NH1 . ARG J 67  ? 1.160 0.533 0.856 -0.068 -0.148 -0.025 67  ARG JJJ NH1 
12268 N NH2 . ARG J 67  ? 1.122 0.543 0.828 -0.109 -0.136 -0.009 67  ARG JJJ NH2 
12269 N N   . PHE J 68  ? 1.066 0.574 0.787 0.039  -0.188 0.028  68  PHE JJJ N   
12270 C CA  . PHE J 68  ? 1.029 0.609 0.789 0.043  -0.187 0.015  68  PHE JJJ CA  
12271 C C   . PHE J 68  ? 1.016 0.627 0.780 0.061  -0.197 0.024  68  PHE JJJ C   
12272 O O   . PHE J 68  ? 1.046 0.637 0.781 0.056  -0.199 0.040  68  PHE JJJ O   
12273 C CB  . PHE J 68  ? 1.006 0.621 0.779 0.012  -0.175 0.011  68  PHE JJJ CB  
12274 C CG  . PHE J 68  ? 1.005 0.611 0.784 -0.006 -0.169 -0.002 68  PHE JJJ CG  
12275 C CD1 . PHE J 68  ? 1.053 0.609 0.817 -0.002 -0.170 -0.010 68  PHE JJJ CD1 
12276 C CD2 . PHE J 68  ? 0.993 0.641 0.792 -0.029 -0.162 -0.008 68  PHE JJJ CD2 
12277 C CE1 . PHE J 68  ? 1.064 0.613 0.830 -0.022 -0.165 -0.024 68  PHE JJJ CE1 
12278 C CE2 . PHE J 68  ? 1.008 0.652 0.811 -0.047 -0.159 -0.022 68  PHE JJJ CE2 
12279 C CZ  . PHE J 68  ? 1.033 0.627 0.818 -0.045 -0.161 -0.031 68  PHE JJJ CZ  
12280 N N   . THR J 69  ? 0.960 0.617 0.757 0.078  -0.202 0.011  69  THR JJJ N   
12281 C CA  . THR J 69  ? 0.928 0.622 0.736 0.092  -0.210 0.014  69  THR JJJ CA  
12282 C C   . THR J 69  ? 0.868 0.622 0.711 0.084  -0.200 0.002  69  THR JJJ C   
12283 O O   . THR J 69  ? 0.835 0.607 0.702 0.088  -0.195 -0.013 69  THR JJJ O   
12284 C CB  . THR J 69  ? 0.934 0.624 0.752 0.126  -0.227 0.010  69  THR JJJ CB  
12285 O OG1 . THR J 69  ? 1.006 0.633 0.789 0.135  -0.235 0.024  69  THR JJJ OG1 
12286 C CG2 . THR J 69  ? 0.892 0.624 0.724 0.138  -0.238 0.011  69  THR JJJ CG2 
12287 N N   . ILE J 70  ? 0.854 0.634 0.695 0.071  -0.196 0.007  70  ILE JJJ N   
12288 C CA  . ILE J 70  ? 0.807 0.640 0.679 0.066  -0.187 -0.003 70  ILE JJJ CA  
12289 C C   . ILE J 70  ? 0.791 0.652 0.679 0.084  -0.197 -0.009 70  ILE JJJ C   
12290 O O   . ILE J 70  ? 0.802 0.648 0.669 0.092  -0.210 -0.000 70  ILE JJJ O   
12291 C CB  . ILE J 70  ? 0.815 0.659 0.681 0.043  -0.174 0.004  70  ILE JJJ CB  
12292 C CG1 . ILE J 70  ? 0.762 0.650 0.658 0.038  -0.163 -0.006 70  ILE JJJ CG1 
12293 C CG2 . ILE J 70  ? 0.825 0.659 0.664 0.039  -0.178 0.015  70  ILE JJJ CG2 
12294 C CD1 . ILE J 70  ? 0.733 0.635 0.631 0.018  -0.150 -0.001 70  ILE JJJ CD1 
12295 N N   . SER J 71  ? 0.727 0.627 0.649 0.088  -0.190 -0.023 71  SER JJJ N   
12296 C CA  . SER J 71  ? 0.692 0.627 0.638 0.101  -0.196 -0.033 71  SER JJJ CA  
12297 C C   . SER J 71  ? 0.655 0.628 0.630 0.092  -0.178 -0.045 71  SER JJJ C   
12298 O O   . SER J 71  ? 0.613 0.581 0.588 0.081  -0.165 -0.044 71  SER JJJ O   
12299 C CB  . SER J 71  ? 0.697 0.630 0.659 0.125  -0.209 -0.041 71  SER JJJ CB  
12300 O OG  . SER J 71  ? 0.688 0.618 0.666 0.128  -0.197 -0.051 71  SER JJJ OG  
12301 N N   . ARG J 72  ? 0.639 0.646 0.636 0.094  -0.179 -0.055 72  ARG JJJ N   
12302 C CA  . ARG J 72  ? 0.614 0.651 0.637 0.084  -0.159 -0.065 72  ARG JJJ CA  
12303 C C   . ARG J 72  ? 0.580 0.650 0.639 0.094  -0.161 -0.083 72  ARG JJJ C   
12304 O O   . ARG J 72  ? 0.579 0.658 0.642 0.106  -0.179 -0.086 72  ARG JJJ O   
12305 C CB  . ARG J 72  ? 0.617 0.659 0.628 0.068  -0.152 -0.060 72  ARG JJJ CB  
12306 C CG  . ARG J 72  ? 0.621 0.673 0.623 0.068  -0.165 -0.062 72  ARG JJJ CG  
12307 C CD  . ARG J 72  ? 0.626 0.677 0.612 0.051  -0.154 -0.057 72  ARG JJJ CD  
12308 N NE  . ARG J 72  ? 0.599 0.667 0.607 0.041  -0.132 -0.065 72  ARG JJJ NE  
12309 C CZ  . ARG J 72  ? 0.599 0.662 0.601 0.029  -0.116 -0.059 72  ARG JJJ CZ  
12310 N NH1 . ARG J 72  ? 0.634 0.679 0.609 0.022  -0.117 -0.048 72  ARG JJJ NH1 
12311 N NH2 . ARG J 72  ? 0.571 0.646 0.593 0.024  -0.097 -0.066 72  ARG JJJ NH2 
12312 N N   . ASP J 73  ? 0.549 0.637 0.631 0.090  -0.141 -0.093 73  ASP JJJ N   
12313 C CA  . ASP J 73  ? 0.529 0.653 0.651 0.093  -0.135 -0.112 73  ASP JJJ CA  
12314 C C   . ASP J 73  ? 0.516 0.651 0.645 0.075  -0.112 -0.116 73  ASP JJJ C   
12315 O O   . ASP J 73  ? 0.530 0.655 0.656 0.070  -0.092 -0.114 73  ASP JJJ O   
12316 C CB  . ASP J 73  ? 0.545 0.670 0.686 0.106  -0.129 -0.122 73  ASP JJJ CB  
12317 C CG  . ASP J 73  ? 0.545 0.711 0.732 0.107  -0.118 -0.143 73  ASP JJJ CG  
12318 O OD1 . ASP J 73  ? 0.550 0.741 0.753 0.096  -0.114 -0.151 73  ASP JJJ OD1 
12319 O OD2 . ASP J 73  ? 0.524 0.695 0.731 0.119  -0.112 -0.154 73  ASP JJJ OD2 
12320 N N   . ASN J 74  ? 0.503 0.654 0.636 0.067  -0.116 -0.121 74  ASN JJJ N   
12321 C CA  . ASN J 74  ? 0.474 0.630 0.610 0.050  -0.095 -0.124 74  ASN JJJ CA  
12322 C C   . ASN J 74  ? 0.461 0.633 0.628 0.045  -0.071 -0.138 74  ASN JJJ C   
12323 O O   . ASN J 74  ? 0.430 0.588 0.590 0.035  -0.049 -0.134 74  ASN JJJ O   
12324 C CB  . ASN J 74  ? 0.466 0.636 0.600 0.042  -0.105 -0.130 74  ASN JJJ CB  
12325 C CG  . ASN J 74  ? 0.480 0.624 0.574 0.040  -0.115 -0.113 74  ASN JJJ CG  
12326 O OD1 . ASN J 74  ? 0.491 0.610 0.564 0.043  -0.115 -0.097 74  ASN JJJ OD1 
12327 N ND2 . ASN J 74  ? 0.484 0.635 0.566 0.032  -0.123 -0.117 74  ASN JJJ ND2 
12328 N N   . ALA J 75  ? 0.494 0.692 0.693 0.052  -0.076 -0.154 75  ALA JJJ N   
12329 C CA  . ALA J 75  ? 0.493 0.710 0.726 0.046  -0.051 -0.171 75  ALA JJJ CA  
12330 C C   . ALA J 75  ? 0.531 0.719 0.743 0.047  -0.031 -0.160 75  ALA JJJ C   
12331 O O   . ALA J 75  ? 0.573 0.761 0.795 0.037  -0.004 -0.166 75  ALA JJJ O   
12332 C CB  . ALA J 75  ? 0.484 0.739 0.759 0.057  -0.062 -0.190 75  ALA JJJ CB  
12333 N N   . LYS J 76  ? 0.544 0.706 0.726 0.058  -0.044 -0.144 76  LYS JJJ N   
12334 C CA  . LYS J 76  ? 0.555 0.691 0.713 0.060  -0.030 -0.135 76  LYS JJJ CA  
12335 C C   . LYS J 76  ? 0.530 0.638 0.652 0.056  -0.032 -0.114 76  LYS JJJ C   
12336 O O   . LYS J 76  ? 0.550 0.637 0.647 0.058  -0.028 -0.106 76  LYS JJJ O   
12337 C CB  . LYS J 76  ? 0.602 0.732 0.758 0.075  -0.042 -0.138 76  LYS JJJ CB  
12338 C CG  . LYS J 76  ? 0.647 0.808 0.845 0.084  -0.041 -0.159 76  LYS JJJ CG  
12339 C CD  . LYS J 76  ? 0.696 0.844 0.890 0.099  -0.044 -0.162 76  LYS JJJ CD  
12340 C CE  . LYS J 76  ? 0.742 0.925 0.984 0.110  -0.039 -0.185 76  LYS JJJ CE  
12341 N NZ  . LYS J 76  ? 0.810 0.976 1.047 0.128  -0.044 -0.188 76  LYS JJJ NZ  
12342 N N   . ASN J 77  ? 0.497 0.606 0.615 0.049  -0.038 -0.108 77  ASN JJJ N   
12343 C CA  . ASN J 77  ? 0.504 0.592 0.595 0.045  -0.038 -0.091 77  ASN JJJ CA  
12344 C C   . ASN J 77  ? 0.493 0.565 0.562 0.052  -0.055 -0.080 77  ASN JJJ C   
12345 O O   . ASN J 77  ? 0.467 0.524 0.517 0.050  -0.052 -0.068 77  ASN JJJ O   
12346 C CB  . ASN J 77  ? 0.487 0.564 0.572 0.040  -0.014 -0.085 77  ASN JJJ CB  
12347 C CG  . ASN J 77  ? 0.464 0.544 0.560 0.030  0.002  -0.089 77  ASN JJJ CG  
12348 O OD1 . ASN J 77  ? 0.438 0.537 0.557 0.024  0.002  -0.104 77  ASN JJJ OD1 
12349 N ND2 . ASN J 77  ? 0.465 0.527 0.548 0.028  0.014  -0.077 77  ASN JJJ ND2 
12350 N N   . THR J 78  ? 0.518 0.591 0.589 0.060  -0.072 -0.084 78  THR JJJ N   
12351 C CA  . THR J 78  ? 0.530 0.582 0.580 0.066  -0.084 -0.078 78  THR JJJ CA  
12352 C C   . THR J 78  ? 0.570 0.612 0.610 0.067  -0.105 -0.071 78  THR JJJ C   
12353 O O   . THR J 78  ? 0.568 0.622 0.619 0.072  -0.114 -0.076 78  THR JJJ O   
12354 C CB  . THR J 78  ? 0.526 0.577 0.583 0.075  -0.081 -0.089 78  THR JJJ CB  
12355 O OG1 . THR J 78  ? 0.484 0.537 0.541 0.071  -0.059 -0.092 78  THR JJJ OG1 
12356 C CG2 . THR J 78  ? 0.538 0.563 0.573 0.080  -0.092 -0.085 78  THR JJJ CG2 
12357 N N   . VAL J 79  ? 0.573 0.596 0.591 0.062  -0.111 -0.059 79  VAL JJJ N   
12358 C CA  . VAL J 79  ? 0.597 0.600 0.597 0.062  -0.127 -0.051 79  VAL JJJ CA  
12359 C C   . VAL J 79  ? 0.625 0.603 0.613 0.067  -0.133 -0.053 79  VAL JJJ C   
12360 O O   . VAL J 79  ? 0.654 0.631 0.638 0.065  -0.125 -0.055 79  VAL JJJ O   
12361 C CB  . VAL J 79  ? 0.606 0.605 0.593 0.048  -0.125 -0.039 79  VAL JJJ CB  
12362 C CG1 . VAL J 79  ? 0.607 0.606 0.592 0.041  -0.118 -0.035 79  VAL JJJ CG1 
12363 C CG2 . VAL J 79  ? 0.643 0.618 0.609 0.044  -0.137 -0.030 79  VAL JJJ CG2 
12364 N N   . TYR J 80  ? 0.665 0.623 0.644 0.076  -0.146 -0.052 80  TYR JJJ N   
12365 C CA  . TYR J 80  ? 0.707 0.635 0.674 0.082  -0.152 -0.055 80  TYR JJJ CA  
12366 C C   . TYR J 80  ? 0.737 0.631 0.677 0.073  -0.161 -0.043 80  TYR JJJ C   
12367 O O   . TYR J 80  ? 0.767 0.658 0.698 0.069  -0.166 -0.033 80  TYR JJJ O   
12368 C CB  . TYR J 80  ? 0.710 0.639 0.693 0.103  -0.158 -0.065 80  TYR JJJ CB  
12369 C CG  . TYR J 80  ? 0.698 0.661 0.710 0.110  -0.146 -0.079 80  TYR JJJ CG  
12370 C CD1 . TYR J 80  ? 0.711 0.673 0.725 0.110  -0.132 -0.090 80  TYR JJJ CD1 
12371 C CD2 . TYR J 80  ? 0.687 0.682 0.724 0.113  -0.147 -0.084 80  TYR JJJ CD2 
12372 C CE1 . TYR J 80  ? 0.679 0.668 0.718 0.114  -0.117 -0.103 80  TYR JJJ CE1 
12373 C CE2 . TYR J 80  ? 0.661 0.687 0.728 0.116  -0.132 -0.098 80  TYR JJJ CE2 
12374 C CZ  . TYR J 80  ? 0.647 0.669 0.714 0.116  -0.116 -0.107 80  TYR JJJ CZ  
12375 O OH  . TYR J 80  ? 0.603 0.652 0.697 0.116  -0.098 -0.121 80  TYR JJJ OH  
12376 N N   . LEU J 81  ? 0.771 0.638 0.697 0.068  -0.161 -0.045 81  LEU JJJ N   
12377 C CA  . LEU J 81  ? 0.787 0.614 0.688 0.060  -0.167 -0.037 81  LEU JJJ CA  
12378 C C   . LEU J 81  ? 0.813 0.604 0.706 0.073  -0.171 -0.046 81  LEU JJJ C   
12379 O O   . LEU J 81  ? 0.796 0.583 0.687 0.069  -0.166 -0.057 81  LEU JJJ O   
12380 C CB  . LEU J 81  ? 0.778 0.606 0.672 0.036  -0.162 -0.033 81  LEU JJJ CB  
12381 C CG  . LEU J 81  ? 0.806 0.596 0.677 0.021  -0.165 -0.024 81  LEU JJJ CG  
12382 C CD1 . LEU J 81  ? 0.804 0.592 0.666 0.019  -0.166 -0.010 81  LEU JJJ CD1 
12383 C CD2 . LEU J 81  ? 0.800 0.599 0.673 -0.003 -0.161 -0.026 81  LEU JJJ CD2 
12384 N N   . GLN J 82  ? 0.841 0.607 0.728 0.090  -0.181 -0.041 82  GLN JJJ N   
12385 C CA  . GLN J 82  ? 0.868 0.590 0.745 0.105  -0.185 -0.046 82  GLN JJJ CA  
12386 C C   . GLN J 82  ? 0.936 0.609 0.781 0.086  -0.185 -0.038 82  GLN JJJ C   
12387 O O   . GLN J 82  ? 0.953 0.612 0.780 0.077  -0.189 -0.022 82  GLN JJJ O   
12388 C CB  . GLN J 82  ? 0.851 0.569 0.735 0.132  -0.198 -0.042 82  GLN JJJ CB  
12389 C CG  . GLN J 82  ? 0.896 0.575 0.779 0.155  -0.202 -0.050 82  GLN JJJ CG  
12390 C CD  . GLN J 82  ? 0.888 0.579 0.790 0.158  -0.188 -0.072 82  GLN JJJ CD  
12391 O OE1 . GLN J 82  ? 0.823 0.563 0.753 0.161  -0.181 -0.082 82  GLN JJJ OE1 
12392 N NE2 . GLN J 82  ? 0.921 0.565 0.804 0.156  -0.183 -0.079 82  GLN JJJ NE2 
12393 N N   . MET J 83  ? 0.972 0.623 0.808 0.076  -0.179 -0.050 83  MET JJJ N   
12394 C CA  . MET J 83  ? 1.014 0.618 0.824 0.054  -0.176 -0.046 83  MET JJJ CA  
12395 C C   . MET J 83  ? 1.073 0.620 0.868 0.069  -0.177 -0.054 83  MET JJJ C   
12396 O O   . MET J 83  ? 1.097 0.645 0.899 0.076  -0.172 -0.072 83  MET JJJ O   
12397 C CB  . MET J 83  ? 0.992 0.619 0.805 0.027  -0.170 -0.057 83  MET JJJ CB  
12398 C CG  . MET J 83  ? 0.965 0.649 0.797 0.017  -0.169 -0.051 83  MET JJJ CG  
12399 S SD  . MET J 83  ? 0.971 0.684 0.808 -0.010 -0.166 -0.062 83  MET JJJ SD  
12400 C CE  . MET J 83  ? 0.981 0.698 0.817 0.005  -0.164 -0.082 83  MET JJJ CE  
12401 N N   . ASN J 84  ? 1.118 0.613 0.890 0.074  -0.182 -0.039 84  ASN JJJ N   
12402 C CA  . ASN J 84  ? 1.205 0.634 0.959 0.091  -0.183 -0.043 84  ASN JJJ CA  
12403 C C   . ASN J 84  ? 1.274 0.644 0.997 0.062  -0.175 -0.041 84  ASN JJJ C   
12404 O O   . ASN J 84  ? 1.287 0.667 1.002 0.034  -0.172 -0.031 84  ASN JJJ O   
12405 C CB  . ASN J 84  ? 1.208 0.618 0.959 0.124  -0.196 -0.027 84  ASN JJJ CB  
12406 C CG  . ASN J 84  ? 1.141 0.611 0.929 0.151  -0.203 -0.034 84  ASN JJJ CG  
12407 O OD1 . ASN J 84  ? 1.111 0.613 0.925 0.155  -0.195 -0.055 84  ASN JJJ OD1 
12408 N ND2 . ASN J 84  ? 1.139 0.626 0.930 0.168  -0.216 -0.019 84  ASN JJJ ND2 
12409 N N   . ARG J 85  ? 1.327 0.640 1.036 0.068  -0.170 -0.052 85  ARG JJJ N   
12410 C CA  . ARG J 85  ? 1.404 0.646 1.081 0.043  -0.162 -0.052 85  ARG JJJ CA  
12411 C C   . ARG J 85  ? 1.346 0.623 1.027 0.000  -0.155 -0.059 85  ARG JJJ C   
12412 O O   . ARG J 85  ? 1.333 0.591 0.999 -0.026 -0.151 -0.046 85  ARG JJJ O   
12413 C CB  . ARG J 85  ? 1.481 0.667 1.128 0.053  -0.166 -0.024 85  ARG JJJ CB  
12414 C CG  . ARG J 85  ? 1.544 0.701 1.191 0.099  -0.177 -0.018 85  ARG JJJ CG  
12415 C CD  . ARG J 85  ? 1.648 0.733 1.256 0.113  -0.182 0.010  85  ARG JJJ CD  
12416 N NE  . ARG J 85  ? 1.655 0.763 1.248 0.098  -0.186 0.033  85  ARG JJJ NE  
12417 C CZ  . ARG J 85  ? 1.719 0.787 1.276 0.066  -0.175 0.048  85  ARG JJJ CZ  
12418 N NH1 . ARG J 85  ? 1.784 0.783 1.317 0.042  -0.161 0.043  85  ARG JJJ NH1 
12419 N NH2 . ARG J 85  ? 1.712 0.806 1.257 0.056  -0.178 0.067  85  ARG JJJ NH2 
12420 N N   . LEU J 86  ? 1.296 0.623 0.999 -0.005 -0.155 -0.080 86  LEU JJJ N   
12421 C CA  . LEU J 86  ? 1.271 0.643 0.984 -0.040 -0.153 -0.088 86  LEU JJJ CA  
12422 C C   . LEU J 86  ? 1.337 0.658 1.030 -0.073 -0.146 -0.101 86  LEU JJJ C   
12423 O O   . LEU J 86  ? 1.361 0.626 1.036 -0.067 -0.141 -0.115 86  LEU JJJ O   
12424 C CB  . LEU J 86  ? 1.227 0.657 0.960 -0.033 -0.156 -0.106 86  LEU JJJ CB  
12425 C CG  . LEU J 86  ? 1.161 0.652 0.918 -0.012 -0.161 -0.094 86  LEU JJJ CG  
12426 C CD1 . LEU J 86  ? 1.134 0.663 0.903 0.001  -0.160 -0.111 86  LEU JJJ CD1 
12427 C CD2 . LEU J 86  ? 1.115 0.652 0.885 -0.034 -0.163 -0.081 86  LEU JJJ CD2 
12428 N N   . LYS J 87  ? 1.351 0.695 1.051 -0.107 -0.144 -0.097 87  LYS JJJ N   
12429 C CA  . LYS J 87  ? 1.386 0.695 1.075 -0.146 -0.136 -0.110 87  LYS JJJ CA  
12430 C C   . LYS J 87  ? 1.319 0.696 1.032 -0.170 -0.143 -0.128 87  LYS JJJ C   
12431 O O   . LYS J 87  ? 1.240 0.686 0.977 -0.160 -0.151 -0.123 87  LYS JJJ O   
12432 C CB  . LYS J 87  ? 1.439 0.717 1.117 -0.167 -0.126 -0.089 87  LYS JJJ CB  
12433 C CG  . LYS J 87  ? 1.492 0.723 1.147 -0.137 -0.125 -0.063 87  LYS JJJ CG  
12434 C CD  . LYS J 87  ? 1.543 0.752 1.182 -0.156 -0.115 -0.040 87  LYS JJJ CD  
12435 C CE  . LYS J 87  ? 1.608 0.754 1.211 -0.125 -0.117 -0.015 87  LYS JJJ CE  
12436 N NZ  . LYS J 87  ? 1.651 0.764 1.227 -0.143 -0.105 0.009  87  LYS JJJ NZ  
12437 N N   . PRO J 88  ? 1.352 0.712 1.060 -0.202 -0.141 -0.151 88  PRO JJJ N   
12438 C CA  . PRO J 88  ? 1.320 0.748 1.052 -0.225 -0.152 -0.168 88  PRO JJJ CA  
12439 C C   . PRO J 88  ? 1.265 0.761 1.030 -0.237 -0.155 -0.153 88  PRO JJJ C   
12440 O O   . PRO J 88  ? 1.245 0.808 1.031 -0.232 -0.167 -0.157 88  PRO JJJ O   
12441 C CB  . PRO J 88  ? 1.387 0.771 1.106 -0.263 -0.147 -0.192 88  PRO JJJ CB  
12442 C CG  . PRO J 88  ? 1.445 0.741 1.128 -0.246 -0.137 -0.196 88  PRO JJJ CG  
12443 C CD  . PRO J 88  ? 1.432 0.707 1.111 -0.214 -0.131 -0.164 88  PRO JJJ CD  
12444 N N   . GLU J 89  ? 1.290 0.767 1.058 -0.248 -0.143 -0.134 89  GLU JJJ N   
12445 C CA  . GLU J 89  ? 1.249 0.786 1.049 -0.260 -0.141 -0.120 89  GLU JJJ CA  
12446 C C   . GLU J 89  ? 1.161 0.746 0.973 -0.225 -0.147 -0.104 89  GLU JJJ C   
12447 O O   . GLU J 89  ? 1.118 0.755 0.958 -0.232 -0.146 -0.094 89  GLU JJJ O   
12448 C CB  . GLU J 89  ? 1.303 0.796 1.092 -0.277 -0.122 -0.103 89  GLU JJJ CB  
12449 C CG  . GLU J 89  ? 1.417 0.840 1.185 -0.309 -0.110 -0.113 89  GLU JJJ CG  
12450 C CD  . GLU J 89  ? 1.510 0.841 1.232 -0.289 -0.105 -0.109 89  GLU JJJ CD  
12451 O OE1 . GLU J 89  ? 1.544 0.852 1.246 -0.257 -0.105 -0.086 89  GLU JJJ OE1 
12452 O OE2 . GLU J 89  ? 1.569 0.853 1.275 -0.304 -0.103 -0.129 89  GLU JJJ OE2 
12453 N N   . ASP J 90  ? 1.126 0.693 0.920 -0.191 -0.152 -0.102 90  ASP JJJ N   
12454 C CA  . ASP J 90  ? 1.066 0.679 0.873 -0.160 -0.158 -0.090 90  ASP JJJ CA  
12455 C C   . ASP J 90  ? 0.996 0.666 0.820 -0.156 -0.169 -0.103 90  ASP JJJ C   
12456 O O   . ASP J 90  ? 0.902 0.613 0.739 -0.135 -0.172 -0.094 90  ASP JJJ O   
12457 C CB  . ASP J 90  ? 1.088 0.659 0.873 -0.127 -0.157 -0.082 90  ASP JJJ CB  
12458 C CG  . ASP J 90  ? 1.132 0.650 0.896 -0.124 -0.149 -0.064 90  ASP JJJ CG  
12459 O OD1 . ASP J 90  ? 1.108 0.642 0.878 -0.136 -0.143 -0.049 90  ASP JJJ OD1 
12460 O OD2 . ASP J 90  ? 1.173 0.631 0.912 -0.109 -0.148 -0.064 90  ASP JJJ OD2 
12461 N N   . THR J 91  ? 1.021 0.690 0.841 -0.175 -0.176 -0.124 91  THR JJJ N   
12462 C CA  . THR J 91  ? 0.987 0.708 0.815 -0.173 -0.189 -0.137 91  THR JJJ CA  
12463 C C   . THR J 91  ? 0.941 0.731 0.806 -0.178 -0.194 -0.126 91  THR JJJ C   
12464 O O   . THR J 91  ? 0.948 0.750 0.834 -0.203 -0.192 -0.126 91  THR JJJ O   
12465 C CB  . THR J 91  ? 1.018 0.722 0.832 -0.198 -0.197 -0.163 91  THR JJJ CB  
12466 O OG1 . THR J 91  ? 1.069 0.710 0.850 -0.186 -0.190 -0.173 91  THR JJJ OG1 
12467 C CG2 . THR J 91  ? 1.002 0.761 0.821 -0.198 -0.214 -0.175 91  THR JJJ CG2 
12468 N N   . ALA J 92  ? 0.896 0.725 0.767 -0.155 -0.200 -0.119 92  ALA JJJ N   
12469 C CA  . ALA J 92  ? 0.837 0.729 0.743 -0.153 -0.204 -0.107 92  ALA JJJ CA  
12470 C C   . ALA J 92  ? 0.797 0.714 0.698 -0.124 -0.207 -0.100 92  ALA JJJ C   
12471 O O   . ALA J 92  ? 0.806 0.692 0.681 -0.107 -0.203 -0.103 92  ALA JJJ O   
12472 C CB  . ALA J 92  ? 0.811 0.703 0.735 -0.157 -0.190 -0.091 92  ALA JJJ CB  
12473 N N   . VAL J 93  ? 0.758 0.728 0.686 -0.119 -0.212 -0.091 93  VAL JJJ N   
12474 C CA  . VAL J 93  ? 0.734 0.724 0.662 -0.093 -0.209 -0.079 93  VAL JJJ CA  
12475 C C   . VAL J 93  ? 0.712 0.691 0.652 -0.084 -0.193 -0.065 93  VAL JJJ C   
12476 O O   . VAL J 93  ? 0.690 0.679 0.651 -0.097 -0.188 -0.059 93  VAL JJJ O   
12477 C CB  . VAL J 93  ? 0.708 0.753 0.660 -0.090 -0.221 -0.074 93  VAL JJJ CB  
12478 C CG1 . VAL J 93  ? 0.690 0.748 0.642 -0.064 -0.215 -0.060 93  VAL JJJ CG1 
12479 C CG2 . VAL J 93  ? 0.738 0.793 0.671 -0.097 -0.241 -0.088 93  VAL JJJ CG2 
12480 N N   . TYR J 94  ? 0.723 0.681 0.646 -0.064 -0.185 -0.061 94  TYR JJJ N   
12481 C CA  . TYR J 94  ? 0.700 0.649 0.629 -0.053 -0.173 -0.049 94  TYR JJJ CA  
12482 C C   . TYR J 94  ? 0.658 0.641 0.603 -0.037 -0.169 -0.040 94  TYR JJJ C   
12483 O O   . TYR J 94  ? 0.675 0.661 0.607 -0.024 -0.170 -0.043 94  TYR JJJ O   
12484 C CB  . TYR J 94  ? 0.715 0.622 0.622 -0.042 -0.169 -0.053 94  TYR JJJ CB  
12485 C CG  . TYR J 94  ? 0.758 0.624 0.652 -0.056 -0.170 -0.057 94  TYR JJJ CG  
12486 C CD1 . TYR J 94  ? 0.804 0.652 0.686 -0.072 -0.176 -0.070 94  TYR JJJ CD1 
12487 C CD2 . TYR J 94  ? 0.766 0.608 0.657 -0.056 -0.164 -0.047 94  TYR JJJ CD2 
12488 C CE1 . TYR J 94  ? 0.852 0.656 0.720 -0.086 -0.174 -0.074 94  TYR JJJ CE1 
12489 C CE2 . TYR J 94  ? 0.819 0.616 0.692 -0.069 -0.163 -0.047 94  TYR JJJ CE2 
12490 C CZ  . TYR J 94  ? 0.848 0.625 0.712 -0.084 -0.167 -0.061 94  TYR JJJ CZ  
12491 O OH  . TYR J 94  ? 0.889 0.615 0.734 -0.098 -0.164 -0.062 94  TYR JJJ OH  
12492 N N   . PHE J 95  ? 0.645 0.649 0.612 -0.040 -0.162 -0.030 95  PHE JJJ N   
12493 C CA  . PHE J 95  ? 0.629 0.661 0.612 -0.027 -0.155 -0.022 95  PHE JJJ CA  
12494 C C   . PHE J 95  ? 0.618 0.637 0.600 -0.018 -0.143 -0.017 95  PHE JJJ C   
12495 O O   . PHE J 95  ? 0.598 0.604 0.578 -0.027 -0.139 -0.015 95  PHE JJJ O   
12496 C CB  . PHE J 95  ? 0.612 0.679 0.626 -0.035 -0.154 -0.017 95  PHE JJJ CB  
12497 C CG  . PHE J 95  ? 0.623 0.715 0.647 -0.042 -0.169 -0.021 95  PHE JJJ CG  
12498 C CD1 . PHE J 95  ? 0.633 0.748 0.659 -0.028 -0.177 -0.018 95  PHE JJJ CD1 
12499 C CD2 . PHE J 95  ? 0.642 0.736 0.674 -0.064 -0.175 -0.029 95  PHE JJJ CD2 
12500 C CE1 . PHE J 95  ? 0.623 0.765 0.658 -0.034 -0.195 -0.022 95  PHE JJJ CE1 
12501 C CE2 . PHE J 95  ? 0.638 0.763 0.686 -0.073 -0.190 -0.035 95  PHE JJJ CE2 
12502 C CZ  . PHE J 95  ? 0.638 0.788 0.686 -0.057 -0.202 -0.032 95  PHE JJJ CZ  
12503 N N   . CYS J 96  ? 0.643 0.667 0.624 -0.003 -0.137 -0.016 96  CYS JJJ N   
12504 C CA  . CYS J 96  ? 0.620 0.644 0.606 0.005  -0.125 -0.013 96  CYS JJJ CA  
12505 C C   . CYS J 96  ? 0.557 0.604 0.564 0.003  -0.117 -0.006 96  CYS JJJ C   
12506 O O   . CYS J 96  ? 0.568 0.635 0.588 0.005  -0.118 -0.003 96  CYS JJJ O   
12507 C CB  . CYS J 96  ? 0.632 0.653 0.612 0.019  -0.120 -0.017 96  CYS JJJ CB  
12508 S SG  . CYS J 96  ? 0.749 0.771 0.738 0.026  -0.108 -0.019 96  CYS JJJ SG  
12509 N N   . ALA J 97  ? 0.536 0.581 0.547 -0.000 -0.108 -0.005 97  ALA JJJ N   
12510 C CA  . ALA J 97  ? 0.568 0.633 0.598 -0.001 -0.096 -0.000 97  ALA JJJ CA  
12511 C C   . ALA J 97  ? 0.577 0.636 0.603 0.003  -0.085 -0.003 97  ALA JJJ C   
12512 O O   . ALA J 97  ? 0.641 0.683 0.651 0.003  -0.091 -0.007 97  ALA JJJ O   
12513 C CB  . ALA J 97  ? 0.587 0.661 0.628 -0.016 -0.094 0.002  97  ALA JJJ CB  
12514 N N   . ALA J 98  ? 0.528 0.600 0.570 0.006  -0.072 -0.002 98  ALA JJJ N   
12515 C CA  . ALA J 98  ? 0.500 0.568 0.539 0.008  -0.060 -0.007 98  ALA JJJ CA  
12516 C C   . ALA J 98  ? 0.489 0.568 0.543 0.004  -0.044 -0.007 98  ALA JJJ C   
12517 O O   . ALA J 98  ? 0.443 0.537 0.518 0.008  -0.039 -0.001 98  ALA JJJ O   
12518 C CB  . ALA J 98  ? 0.503 0.569 0.545 0.018  -0.056 -0.011 98  ALA JJJ CB  
12519 N N   . ASP J 99  ? 0.479 0.552 0.523 -0.002 -0.036 -0.013 99  ASP JJJ N   
12520 C CA  . ASP J 99  ? 0.494 0.573 0.547 -0.006 -0.017 -0.016 99  ASP JJJ CA  
12521 C C   . ASP J 99  ? 0.495 0.564 0.532 -0.010 -0.011 -0.027 99  ASP JJJ C   
12522 O O   . ASP J 99  ? 0.527 0.588 0.544 -0.013 -0.025 -0.029 99  ASP JJJ O   
12523 C CB  . ASP J 99  ? 0.502 0.586 0.555 -0.018 -0.013 -0.012 99  ASP JJJ CB  
12524 C CG  . ASP J 99  ? 0.517 0.615 0.593 -0.018 0.009  -0.015 99  ASP JJJ CG  
12525 O OD1 . ASP J 99  ? 0.480 0.595 0.587 -0.008 0.011  -0.010 99  ASP JJJ OD1 
12526 O OD2 . ASP J 99  ? 0.598 0.688 0.660 -0.026 0.023  -0.022 99  ASP JJJ OD2 
12527 N N   . ARG J 100 ? 0.537 0.623 0.642 -0.034 -0.022 0.089  100 ARG JJJ N   
12528 C CA  . ARG J 100 ? 0.501 0.609 0.663 -0.048 -0.019 0.089  100 ARG JJJ CA  
12529 C C   . ARG J 100 ? 0.473 0.599 0.645 -0.062 -0.042 0.076  100 ARG JJJ C   
12530 O O   . ARG J 100 ? 0.498 0.641 0.704 -0.067 -0.045 0.075  100 ARG JJJ O   
12531 C CB  . ARG J 100 ? 0.500 0.607 0.681 -0.054 -0.014 0.091  100 ARG JJJ CB  
12532 C CG  . ARG J 100 ? 0.537 0.620 0.714 -0.040 0.017  0.108  100 ARG JJJ CG  
12533 C CD  . ARG J 100 ? 0.555 0.644 0.780 -0.044 0.042  0.118  100 ARG JJJ CD  
12534 N NE  . ARG J 100 ? 0.530 0.651 0.817 -0.067 0.028  0.105  100 ARG JJJ NE  
12535 C CZ  . ARG J 100 ? 0.533 0.655 0.865 -0.083 0.034  0.101  100 ARG JJJ CZ  
12536 N NH1 . ARG J 100 ? 0.544 0.634 0.866 -0.079 0.059  0.112  100 ARG JJJ NH1 
12537 N NH2 . ARG J 100 ? 0.531 0.683 0.914 -0.102 0.014  0.086  100 ARG JJJ NH2 
12538 N N   . GLY J 101 ? 0.470 0.593 0.613 -0.066 -0.058 0.067  101 GLY JJJ N   
12539 C CA  . GLY J 101 ? 0.446 0.578 0.591 -0.077 -0.073 0.058  101 GLY JJJ CA  
12540 C C   . GLY J 101 ? 0.466 0.582 0.584 -0.075 -0.075 0.057  101 GLY JJJ C   
12541 O O   . GLY J 101 ? 0.493 0.591 0.583 -0.069 -0.072 0.057  101 GLY JJJ O   
12542 N N   . GLU J 102 ? 0.480 0.598 0.601 -0.078 -0.081 0.055  102 GLU JJJ N   
12543 C CA  . GLU J 102 ? 0.502 0.596 0.593 -0.076 -0.081 0.054  102 GLU JJJ CA  
12544 C C   . GLU J 102 ? 0.510 0.599 0.589 -0.091 -0.085 0.047  102 GLU JJJ C   
12545 O O   . GLU J 102 ? 0.487 0.588 0.576 -0.095 -0.089 0.046  102 GLU JJJ O   
12546 C CB  . GLU J 102 ? 0.507 0.604 0.605 -0.065 -0.083 0.060  102 GLU JJJ CB  
12547 C CG  . GLU J 102 ? 0.547 0.611 0.608 -0.058 -0.080 0.062  102 GLU JJJ CG  
12548 C CD  . GLU J 102 ? 0.559 0.629 0.624 -0.040 -0.086 0.069  102 GLU JJJ CD  
12549 O OE1 . GLU J 102 ? 0.544 0.649 0.650 -0.032 -0.093 0.070  102 GLU JJJ OE1 
12550 O OE2 . GLU J 102 ? 0.573 0.610 0.601 -0.033 -0.083 0.072  102 GLU JJJ OE2 
12551 N N   . SER J 103 ? 0.553 0.625 0.613 -0.100 -0.083 0.042  103 SER JJJ N   
12552 C CA  . SER J 103 ? 0.568 0.642 0.632 -0.117 -0.083 0.035  103 SER JJJ CA  
12553 C C   . SER J 103 ? 0.575 0.617 0.617 -0.122 -0.073 0.038  103 SER JJJ C   
12554 O O   . SER J 103 ? 0.577 0.587 0.593 -0.116 -0.069 0.040  103 SER JJJ O   
12555 C CB  . SER J 103 ? 0.608 0.686 0.674 -0.127 -0.090 0.024  103 SER JJJ CB  
12556 O OG  . SER J 103 ? 0.630 0.720 0.716 -0.146 -0.088 0.017  103 SER JJJ OG  
12557 N N   . TYR J 104 ? 0.588 0.634 0.634 -0.130 -0.066 0.039  104 TYR JJJ N   
12558 C CA  . TYR J 104 ? 0.626 0.636 0.649 -0.137 -0.049 0.043  104 TYR JJJ CA  
12559 C C   . TYR J 104 ? 0.645 0.639 0.674 -0.158 -0.045 0.033  104 TYR JJJ C   
12560 O O   . TYR J 104 ? 0.706 0.653 0.707 -0.161 -0.032 0.036  104 TYR JJJ O   
12561 C CB  . TYR J 104 ? 0.646 0.662 0.671 -0.141 -0.037 0.047  104 TYR JJJ CB  
12562 C CG  . TYR J 104 ? 0.701 0.672 0.697 -0.146 -0.012 0.055  104 TYR JJJ CG  
12563 C CD1 . TYR J 104 ? 0.744 0.672 0.690 -0.126 -0.008 0.066  104 TYR JJJ CD1 
12564 C CD2 . TYR J 104 ? 0.731 0.701 0.751 -0.170 0.008  0.052  104 TYR JJJ CD2 
12565 C CE1 . TYR J 104 ? 0.802 0.678 0.710 -0.127 0.019  0.077  104 TYR JJJ CE1 
12566 C CE2 . TYR J 104 ? 0.791 0.712 0.783 -0.176 0.039  0.063  104 TYR JJJ CE2 
12567 C CZ  . TYR J 104 ? 0.823 0.692 0.754 -0.153 0.045  0.076  104 TYR JJJ CZ  
12568 O OH  . TYR J 104 ? 0.880 0.690 0.773 -0.154 0.079  0.090  104 TYR JJJ OH  
12569 N N   . TYR J 105 ? 0.617 0.645 0.679 -0.170 -0.057 0.021  105 TYR JJJ N   
12570 C CA  . TYR J 105 ? 0.629 0.650 0.703 -0.191 -0.063 0.005  105 TYR JJJ CA  
12571 C C   . TYR J 105 ? 0.623 0.631 0.671 -0.178 -0.080 -0.001 105 TYR JJJ C   
12572 O O   . TYR J 105 ? 0.590 0.621 0.649 -0.179 -0.099 -0.014 105 TYR JJJ O   
12573 C CB  . TYR J 105 ? 0.619 0.690 0.746 -0.208 -0.070 -0.006 105 TYR JJJ CB  
12574 C CG  . TYR J 105 ? 0.634 0.725 0.788 -0.215 -0.050 0.003  105 TYR JJJ CG  
12575 C CD1 . TYR J 105 ? 0.663 0.721 0.813 -0.230 -0.022 0.009  105 TYR JJJ CD1 
12576 C CD2 . TYR J 105 ? 0.607 0.744 0.788 -0.204 -0.054 0.006  105 TYR JJJ CD2 
12577 C CE1 . TYR J 105 ? 0.671 0.742 0.838 -0.231 0.002  0.019  105 TYR JJJ CE1 
12578 C CE2 . TYR J 105 ? 0.592 0.743 0.792 -0.206 -0.033 0.014  105 TYR JJJ CE2 
12579 C CZ  . TYR J 105 ? 0.640 0.758 0.831 -0.219 -0.004 0.021  105 TYR JJJ CZ  
12580 O OH  . TYR J 105 ? 0.649 0.775 0.851 -0.218 0.023  0.030  105 TYR JJJ OH  
12581 N N   . TYR J 106 ? 0.639 0.608 0.648 -0.160 -0.071 0.008  106 TYR JJJ N   
12582 C CA  . TYR J 106 ? 0.658 0.613 0.639 -0.140 -0.078 0.008  106 TYR JJJ CA  
12583 C C   . TYR J 106 ? 0.692 0.618 0.650 -0.149 -0.088 -0.011 106 TYR JJJ C   
12584 O O   . TYR J 106 ? 0.756 0.673 0.687 -0.130 -0.094 -0.012 106 TYR JJJ O   
12585 C CB  . TYR J 106 ? 0.677 0.600 0.629 -0.118 -0.065 0.023  106 TYR JJJ CB  
12586 C CG  . TYR J 106 ? 0.740 0.609 0.663 -0.124 -0.050 0.024  106 TYR JJJ CG  
12587 C CD1 . TYR J 106 ? 0.740 0.605 0.667 -0.130 -0.038 0.034  106 TYR JJJ CD1 
12588 C CD2 . TYR J 106 ? 0.784 0.600 0.671 -0.127 -0.046 0.014  106 TYR JJJ CD2 
12589 C CE1 . TYR J 106 ? 0.803 0.609 0.698 -0.135 -0.019 0.037  106 TYR JJJ CE1 
12590 C CE2 . TYR J 106 ? 0.848 0.604 0.707 -0.134 -0.028 0.015  106 TYR JJJ CE2 
12591 C CZ  . TYR J 106 ? 0.849 0.600 0.712 -0.138 -0.013 0.029  106 TYR JJJ CZ  
12592 O OH  . TYR J 106 ? 0.936 0.621 0.767 -0.144 0.009  0.033  106 TYR JJJ OH  
12593 N N   . THR J 107 ? 0.614 0.652 0.659 -0.194 -0.097 -0.051 107 THR JJJ N   
12594 C CA  . THR J 107 ? 0.618 0.655 0.679 -0.181 -0.105 -0.049 107 THR JJJ CA  
12595 C C   . THR J 107 ? 0.590 0.653 0.681 -0.167 -0.091 -0.064 107 THR JJJ C   
12596 O O   . THR J 107 ? 0.586 0.651 0.691 -0.156 -0.098 -0.063 107 THR JJJ O   
12597 C CB  . THR J 107 ? 0.629 0.654 0.668 -0.204 -0.115 -0.042 107 THR JJJ CB  
12598 O OG1 . THR J 107 ? 0.621 0.672 0.660 -0.226 -0.098 -0.053 107 THR JJJ OG1 
12599 C CG2 . THR J 107 ? 0.662 0.659 0.671 -0.220 -0.132 -0.026 107 THR JJJ CG2 
12600 N N   . ARG J 108 ? 0.587 0.671 0.690 -0.169 -0.073 -0.077 108 ARG JJJ N   
12601 C CA  . ARG J 108 ? 0.587 0.696 0.726 -0.154 -0.062 -0.090 108 ARG JJJ CA  
12602 C C   . ARG J 108 ? 0.564 0.666 0.721 -0.126 -0.068 -0.088 108 ARG JJJ C   
12603 O O   . ARG J 108 ? 0.562 0.654 0.713 -0.120 -0.066 -0.088 108 ARG JJJ O   
12604 C CB  . ARG J 108 ? 0.602 0.733 0.752 -0.164 -0.040 -0.108 108 ARG JJJ CB  
12605 C CG  . ARG J 108 ? 0.619 0.767 0.756 -0.194 -0.029 -0.114 108 ARG JJJ CG  
12606 C CD  . ARG J 108 ? 0.631 0.808 0.788 -0.199 -0.004 -0.137 108 ARG JJJ CD  
12607 N NE  . ARG J 108 ? 0.670 0.861 0.804 -0.235 0.009  -0.144 108 ARG JJJ NE  
12608 C CZ  . ARG J 108 ? 0.710 0.925 0.852 -0.249 0.034  -0.167 108 ARG JJJ CZ  
12609 N NH1 . ARG J 108 ? 0.708 0.933 0.882 -0.226 0.049  -0.185 108 ARG JJJ NH1 
12610 N NH2 . ARG J 108 ? 0.753 0.981 0.867 -0.287 0.046  -0.173 108 ARG JJJ NH2 
12611 N N   . PRO J 109 ? 0.541 0.648 0.717 -0.112 -0.077 -0.086 109 PRO JJJ N   
12612 C CA  . PRO J 109 ? 0.516 0.619 0.707 -0.090 -0.083 -0.084 109 PRO JJJ CA  
12613 C C   . PRO J 109 ? 0.511 0.622 0.723 -0.080 -0.072 -0.094 109 PRO JJJ C   
12614 O O   . PRO J 109 ? 0.485 0.581 0.691 -0.069 -0.076 -0.091 109 PRO JJJ O   
12615 C CB  . PRO J 109 ? 0.531 0.646 0.742 -0.085 -0.092 -0.081 109 PRO JJJ CB  
12616 C CG  . PRO J 109 ? 0.547 0.658 0.739 -0.102 -0.096 -0.077 109 PRO JJJ CG  
12617 C CD  . PRO J 109 ? 0.555 0.671 0.735 -0.120 -0.083 -0.083 109 PRO JJJ CD  
12618 N N   . THR J 110 ? 0.515 0.648 0.748 -0.085 -0.057 -0.108 110 THR JJJ N   
12619 C CA  . THR J 110 ? 0.511 0.650 0.767 -0.075 -0.045 -0.122 110 THR JJJ CA  
12620 C C   . THR J 110 ? 0.529 0.647 0.757 -0.081 -0.037 -0.124 110 THR JJJ C   
12621 O O   . THR J 110 ? 0.537 0.649 0.778 -0.070 -0.031 -0.133 110 THR JJJ O   
12622 C CB  . THR J 110 ? 0.507 0.679 0.795 -0.080 -0.028 -0.140 110 THR JJJ CB  
12623 O OG1 . THR J 110 ? 0.510 0.689 0.772 -0.107 -0.018 -0.143 110 THR JJJ OG1 
12624 C CG2 . THR J 110 ? 0.489 0.687 0.817 -0.069 -0.036 -0.140 110 THR JJJ CG2 
12625 N N   . GLU J 111 ? 0.549 0.655 0.741 -0.098 -0.039 -0.116 111 GLU JJJ N   
12626 C CA  . GLU J 111 ? 0.575 0.663 0.739 -0.107 -0.034 -0.116 111 GLU JJJ CA  
12627 C C   . GLU J 111 ? 0.579 0.648 0.734 -0.094 -0.048 -0.103 111 GLU JJJ C   
12628 O O   . GLU J 111 ? 0.650 0.705 0.783 -0.100 -0.046 -0.101 111 GLU JJJ O   
12629 C CB  . GLU J 111 ? 0.594 0.679 0.725 -0.133 -0.033 -0.110 111 GLU JJJ CB  
12630 C CG  . GLU J 111 ? 0.609 0.713 0.740 -0.154 -0.016 -0.125 111 GLU JJJ CG  
12631 C CD  . GLU J 111 ? 0.616 0.723 0.748 -0.160 0.006  -0.144 111 GLU JJJ CD  
12632 O OE1 . GLU J 111 ? 0.609 0.722 0.774 -0.140 0.013  -0.157 111 GLU JJJ OE1 
12633 O OE2 . GLU J 111 ? 0.603 0.704 0.702 -0.187 0.015  -0.147 111 GLU JJJ OE2 
12634 N N   . TYR J 112 ? 0.580 0.648 0.748 -0.078 -0.062 -0.095 112 TYR JJJ N   
12635 C CA  . TYR J 112 ? 0.600 0.654 0.758 -0.068 -0.074 -0.084 112 TYR JJJ CA  
12636 C C   . TYR J 112 ? 0.582 0.633 0.761 -0.052 -0.078 -0.086 112 TYR JJJ C   
12637 O O   . TYR J 112 ? 0.575 0.637 0.776 -0.045 -0.084 -0.086 112 TYR JJJ O   
12638 C CB  . TYR J 112 ? 0.588 0.641 0.736 -0.068 -0.087 -0.073 112 TYR JJJ CB  
12639 C CG  . TYR J 112 ? 0.614 0.663 0.742 -0.083 -0.087 -0.069 112 TYR JJJ CG  
12640 C CD1 . TYR J 112 ? 0.614 0.670 0.743 -0.095 -0.084 -0.071 112 TYR JJJ CD1 
12641 C CD2 . TYR J 112 ? 0.623 0.664 0.733 -0.088 -0.091 -0.061 112 TYR JJJ CD2 
12642 C CE1 . TYR J 112 ? 0.606 0.655 0.714 -0.111 -0.088 -0.064 112 TYR JJJ CE1 
12643 C CE2 . TYR J 112 ? 0.619 0.655 0.712 -0.102 -0.096 -0.055 112 TYR JJJ CE2 
12644 C CZ  . TYR J 112 ? 0.609 0.646 0.699 -0.114 -0.095 -0.055 112 TYR JJJ CZ  
12645 O OH  . TYR J 112 ? 0.598 0.625 0.668 -0.131 -0.103 -0.046 112 TYR JJJ OH  
12646 N N   . GLU J 113 ? 0.584 0.621 0.756 -0.049 -0.078 -0.087 113 GLU JJJ N   
12647 C CA  . GLU J 113 ? 0.596 0.625 0.787 -0.035 -0.085 -0.087 113 GLU JJJ CA  
12648 C C   . GLU J 113 ? 0.575 0.601 0.760 -0.031 -0.102 -0.074 113 GLU JJJ C   
12649 O O   . GLU J 113 ? 0.549 0.577 0.755 -0.022 -0.112 -0.071 113 GLU JJJ O   
12650 C CB  . GLU J 113 ? 0.649 0.657 0.828 -0.036 -0.081 -0.091 113 GLU JJJ CB  
12651 C CG  . GLU J 113 ? 0.703 0.697 0.900 -0.022 -0.091 -0.090 113 GLU JJJ CG  
12652 C CD  . GLU J 113 ? 0.782 0.749 0.970 -0.022 -0.088 -0.096 113 GLU JJJ CD  
12653 O OE1 . GLU J 113 ? 0.829 0.791 0.994 -0.034 -0.075 -0.102 113 GLU JJJ OE1 
12654 O OE2 . GLU J 113 ? 0.827 0.776 1.027 -0.012 -0.100 -0.092 113 GLU JJJ OE2 
12655 N N   . PHE J 114 ? 0.584 0.609 0.745 -0.037 -0.106 -0.066 114 PHE JJJ N   
12656 C CA  . PHE J 114 ? 0.564 0.587 0.715 -0.037 -0.118 -0.057 114 PHE JJJ CA  
12657 C C   . PHE J 114 ? 0.562 0.596 0.711 -0.038 -0.121 -0.055 114 PHE JJJ C   
12658 O O   . PHE J 114 ? 0.580 0.619 0.723 -0.042 -0.115 -0.057 114 PHE JJJ O   
12659 C CB  . PHE J 114 ? 0.561 0.576 0.687 -0.044 -0.118 -0.053 114 PHE JJJ CB  
12660 C CG  . PHE J 114 ? 0.589 0.585 0.712 -0.044 -0.117 -0.055 114 PHE JJJ CG  
12661 C CD1 . PHE J 114 ? 0.596 0.579 0.728 -0.038 -0.128 -0.052 114 PHE JJJ CD1 
12662 C CD2 . PHE J 114 ? 0.580 0.569 0.689 -0.051 -0.107 -0.059 114 PHE JJJ CD2 
12663 C CE1 . PHE J 114 ? 0.622 0.582 0.752 -0.037 -0.128 -0.054 114 PHE JJJ CE1 
12664 C CE2 . PHE J 114 ? 0.610 0.579 0.715 -0.052 -0.106 -0.063 114 PHE JJJ CE2 
12665 C CZ  . PHE J 114 ? 0.628 0.581 0.744 -0.043 -0.116 -0.061 114 PHE JJJ CZ  
12666 N N   . TRP J 115 ? 0.550 0.587 0.703 -0.036 -0.131 -0.051 115 TRP JJJ N   
12667 C CA  . TRP J 115 ? 0.535 0.579 0.686 -0.038 -0.134 -0.051 115 TRP JJJ CA  
12668 C C   . TRP J 115 ? 0.534 0.576 0.669 -0.042 -0.142 -0.047 115 TRP JJJ C   
12669 O O   . TRP J 115 ? 0.529 0.566 0.664 -0.043 -0.151 -0.042 115 TRP JJJ O   
12670 C CB  . TRP J 115 ? 0.538 0.589 0.709 -0.036 -0.137 -0.052 115 TRP JJJ CB  
12671 C CG  . TRP J 115 ? 0.533 0.590 0.715 -0.036 -0.127 -0.058 115 TRP JJJ CG  
12672 C CD1 . TRP J 115 ? 0.532 0.592 0.728 -0.034 -0.119 -0.063 115 TRP JJJ CD1 
12673 C CD2 . TRP J 115 ? 0.541 0.602 0.719 -0.042 -0.123 -0.060 115 TRP JJJ CD2 
12674 N NE1 . TRP J 115 ? 0.539 0.606 0.738 -0.040 -0.109 -0.069 115 TRP JJJ NE1 
12675 C CE2 . TRP J 115 ? 0.551 0.619 0.738 -0.046 -0.113 -0.065 115 TRP JJJ CE2 
12676 C CE3 . TRP J 115 ? 0.559 0.616 0.725 -0.046 -0.128 -0.058 115 TRP JJJ CE3 
12677 C CZ2 . TRP J 115 ? 0.568 0.639 0.749 -0.057 -0.108 -0.067 115 TRP JJJ CZ2 
12678 C CZ3 . TRP J 115 ? 0.576 0.632 0.739 -0.054 -0.125 -0.059 115 TRP JJJ CZ3 
12679 C CH2 . TRP J 115 ? 0.569 0.632 0.738 -0.060 -0.116 -0.062 115 TRP JJJ CH2 
12680 N N   . GLY J 116 ? 0.518 0.564 0.642 -0.044 -0.139 -0.051 116 GLY JJJ N   
12681 C CA  . GLY J 116 ? 0.517 0.566 0.628 -0.050 -0.143 -0.052 116 GLY JJJ CA  
12682 C C   . GLY J 116 ? 0.520 0.568 0.634 -0.053 -0.151 -0.050 116 GLY JJJ C   
12683 O O   . GLY J 116 ? 0.525 0.573 0.656 -0.049 -0.152 -0.049 116 GLY JJJ O   
12684 N N   . GLN J 117 ? 0.541 0.590 0.639 -0.062 -0.155 -0.051 117 GLN JJJ N   
12685 C CA  . GLN J 117 ? 0.568 0.615 0.664 -0.069 -0.164 -0.049 117 GLN JJJ CA  
12686 C C   . GLN J 117 ? 0.606 0.651 0.701 -0.068 -0.158 -0.059 117 GLN JJJ C   
12687 O O   . GLN J 117 ? 0.648 0.691 0.743 -0.074 -0.165 -0.057 117 GLN JJJ O   
12688 C CB  . GLN J 117 ? 0.573 0.619 0.646 -0.085 -0.172 -0.046 117 GLN JJJ CB  
12689 C CG  . GLN J 117 ? 0.594 0.636 0.663 -0.089 -0.181 -0.035 117 GLN JJJ CG  
12690 C CD  . GLN J 117 ? 0.589 0.626 0.682 -0.082 -0.194 -0.024 117 GLN JJJ CD  
12691 O OE1 . GLN J 117 ? 0.612 0.643 0.716 -0.074 -0.195 -0.020 117 GLN JJJ OE1 
12692 N NE2 . GLN J 117 ? 0.593 0.633 0.696 -0.084 -0.203 -0.020 117 GLN JJJ NE2 
12693 N N   . GLY J 118 ? 0.607 0.652 0.701 -0.061 -0.148 -0.067 118 GLY JJJ N   
12694 C CA  . GLY J 118 ? 0.608 0.645 0.701 -0.058 -0.144 -0.077 118 GLY JJJ CA  
12695 C C   . GLY J 118 ? 0.631 0.667 0.708 -0.063 -0.139 -0.089 118 GLY JJJ C   
12696 O O   . GLY J 118 ? 0.618 0.660 0.680 -0.075 -0.141 -0.089 118 GLY JJJ O   
12697 N N   . THR J 119 ? 0.644 0.671 0.724 -0.056 -0.134 -0.100 119 THR JJJ N   
12698 C CA  . THR J 119 ? 0.670 0.695 0.740 -0.059 -0.127 -0.117 119 THR JJJ CA  
12699 C C   . THR J 119 ? 0.712 0.714 0.782 -0.056 -0.129 -0.124 119 THR JJJ C   
12700 O O   . THR J 119 ? 0.693 0.685 0.776 -0.047 -0.134 -0.117 119 THR JJJ O   
12701 C CB  . THR J 119 ? 0.691 0.730 0.771 -0.049 -0.117 -0.128 119 THR JJJ CB  
12702 O OG1 . THR J 119 ? 0.714 0.758 0.784 -0.055 -0.107 -0.147 119 THR JJJ OG1 
12703 C CG2 . THR J 119 ? 0.708 0.741 0.810 -0.032 -0.118 -0.128 119 THR JJJ CG2 
12704 N N   . GLN J 120 ? 0.753 0.745 0.804 -0.067 -0.127 -0.135 120 GLN JJJ N   
12705 C CA  . GLN J 120 ? 0.764 0.730 0.809 -0.067 -0.130 -0.142 120 GLN JJJ CA  
12706 C C   . GLN J 120 ? 0.743 0.697 0.803 -0.049 -0.123 -0.157 120 GLN JJJ C   
12707 O O   . GLN J 120 ? 0.754 0.721 0.819 -0.044 -0.112 -0.173 120 GLN JJJ O   
12708 C CB  . GLN J 120 ? 0.823 0.783 0.840 -0.087 -0.129 -0.151 120 GLN JJJ CB  
12709 C CG  . GLN J 120 ? 0.871 0.801 0.876 -0.092 -0.133 -0.157 120 GLN JJJ CG  
12710 C CD  . GLN J 120 ? 0.904 0.828 0.913 -0.096 -0.146 -0.138 120 GLN JJJ CD  
12711 O OE1 . GLN J 120 ? 0.995 0.937 1.006 -0.105 -0.153 -0.122 120 GLN JJJ OE1 
12712 N NE2 . GLN J 120 ? 0.930 0.829 0.943 -0.090 -0.150 -0.139 120 GLN JJJ NE2 
12713 N N   . VAL J 121 ? 0.738 0.669 0.806 -0.041 -0.132 -0.152 121 VAL JJJ N   
12714 C CA  . VAL J 121 ? 0.753 0.659 0.833 -0.026 -0.132 -0.166 121 VAL JJJ CA  
12715 C C   . VAL J 121 ? 0.775 0.645 0.833 -0.036 -0.137 -0.171 121 VAL JJJ C   
12716 O O   . VAL J 121 ? 0.757 0.619 0.805 -0.048 -0.148 -0.155 121 VAL JJJ O   
12717 C CB  . VAL J 121 ? 0.740 0.642 0.842 -0.012 -0.141 -0.153 121 VAL JJJ CB  
12718 C CG1 . VAL J 121 ? 0.772 0.642 0.886 0.004  -0.147 -0.163 121 VAL JJJ CG1 
12719 C CG2 . VAL J 121 ? 0.700 0.637 0.819 -0.004 -0.136 -0.148 121 VAL JJJ CG2 
12720 N N   . THR J 122 ? 0.807 0.660 0.861 -0.032 -0.130 -0.194 122 THR JJJ N   
12721 C CA  . THR J 122 ? 0.876 0.689 0.907 -0.042 -0.134 -0.202 122 THR JJJ CA  
12722 C C   . THR J 122 ? 0.928 0.706 0.976 -0.021 -0.137 -0.217 122 THR JJJ C   
12723 O O   . THR J 122 ? 0.941 0.731 1.009 -0.005 -0.124 -0.238 122 THR JJJ O   
12724 C CB  . THR J 122 ? 0.885 0.703 0.887 -0.062 -0.124 -0.216 122 THR JJJ CB  
12725 O OG1 . THR J 122 ? 0.870 0.718 0.862 -0.079 -0.128 -0.197 122 THR JJJ OG1 
12726 C CG2 . THR J 122 ? 0.932 0.709 0.905 -0.076 -0.128 -0.226 122 THR JJJ CG2 
12727 N N   . VAL J 123 ? 0.972 0.712 1.013 -0.022 -0.153 -0.206 123 VAL JJJ N   
12728 C CA  . VAL J 123 ? 1.043 0.740 1.099 -0.003 -0.161 -0.217 123 VAL JJJ CA  
12729 C C   . VAL J 123 ? 1.105 0.756 1.129 -0.018 -0.163 -0.230 123 VAL JJJ C   
12730 O O   . VAL J 123 ? 1.082 0.715 1.079 -0.039 -0.175 -0.213 123 VAL JJJ O   
12731 C CB  . VAL J 123 ? 1.055 0.738 1.124 0.003  -0.181 -0.193 123 VAL JJJ CB  
12732 C CG1 . VAL J 123 ? 1.118 0.759 1.209 0.025  -0.193 -0.201 123 VAL JJJ CG1 
12733 C CG2 . VAL J 123 ? 0.993 0.723 1.083 0.009  -0.179 -0.177 123 VAL JJJ CG2 
12734 N N   . SER J 124 ? 1.208 0.843 1.232 -0.009 -0.150 -0.261 124 SER JJJ N   
12735 C CA  . SER J 124 ? 1.323 0.909 1.316 -0.022 -0.149 -0.279 124 SER JJJ CA  
12736 C C   . SER J 124 ? 1.478 1.005 1.482 -0.005 -0.167 -0.280 124 SER JJJ C   
12737 O O   . SER J 124 ? 1.467 0.998 1.508 0.020  -0.175 -0.273 124 SER JJJ O   
12738 C CB  . SER J 124 ? 1.321 0.918 1.310 -0.021 -0.125 -0.314 124 SER JJJ CB  
12739 O OG  . SER J 124 ? 1.302 0.911 1.335 0.010  -0.115 -0.335 124 SER JJJ OG  
12754 N N   . THR K 4   ? 1.827 1.532 1.439 -0.154 0.308  -0.216 333 THR KKK N   
12755 C CA  . THR K 4   ? 1.696 1.388 1.236 -0.152 0.289  -0.193 333 THR KKK CA  
12756 C C   . THR K 4   ? 1.582 1.275 1.075 -0.118 0.237  -0.145 333 THR KKK C   
12757 O O   . THR K 4   ? 1.537 1.208 1.028 -0.102 0.229  -0.117 333 THR KKK O   
12758 C CB  . THR K 4   ? 1.723 1.426 1.168 -0.188 0.300  -0.222 333 THR KKK CB  
12759 O OG1 . THR K 4   ? 1.709 1.397 1.189 -0.222 0.354  -0.262 333 THR KKK OG1 
12760 C CG2 . THR K 4   ? 1.734 1.410 1.071 -0.174 0.277  -0.181 333 THR KKK CG2 
12761 N N   . ASN K 5   ? 1.475 1.201 0.939 -0.111 0.206  -0.146 334 ASN KKK N   
12762 C CA  . ASN K 5   ? 1.393 1.127 0.818 -0.077 0.159  -0.107 334 ASN KKK CA  
12763 C C   . ASN K 5   ? 1.268 0.991 0.769 -0.054 0.151  -0.083 334 ASN KKK C   
12764 O O   . ASN K 5   ? 1.212 0.942 0.783 -0.056 0.171  -0.099 334 ASN KKK O   
12765 C CB  . ASN K 5   ? 1.427 1.227 0.816 -0.077 0.132  -0.128 334 ASN KKK CB  
12766 C CG  . ASN K 5   ? 1.415 1.253 0.883 -0.105 0.157  -0.182 334 ASN KKK CG  
12767 O OD1 . ASN K 5   ? 1.405 1.227 0.917 -0.136 0.205  -0.218 334 ASN KKK OD1 
12768 N ND2 . ASN K 5   ? 1.406 1.285 0.899 -0.095 0.135  -0.190 334 ASN KKK ND2 
12769 N N   . LEU K 6   ? 1.210 0.915 0.694 -0.032 0.130  -0.048 335 LEU KKK N   
12770 C CA  . LEU K 6   ? 1.137 0.850 0.682 -0.010 0.120  -0.027 335 LEU KKK CA  
12771 C C   . LEU K 6   ? 1.092 0.825 0.646 0.004  0.095  -0.022 335 LEU KKK C   
12772 O O   . LEU K 6   ? 1.115 0.864 0.621 0.004  0.074  -0.028 335 LEU KKK O   
12773 C CB  . LEU K 6   ? 1.141 0.839 0.666 -0.005 0.115  -0.009 335 LEU KKK CB  
12774 C CG  . LEU K 6   ? 1.165 0.854 0.698 -0.025 0.148  -0.027 335 LEU KKK CG  
12775 C CD1 . LEU K 6   ? 1.160 0.838 0.682 -0.032 0.157  -0.026 335 LEU KKK CD1 
12776 C CD2 . LEU K 6   ? 1.128 0.857 0.744 -0.019 0.165  -0.040 335 LEU KKK CD2 
12777 N N   . CYS K 7   ? 1.053 0.794 0.667 0.017  0.102  -0.013 336 CYS KKK N   
12778 C CA  . CYS K 7   ? 1.037 0.790 0.667 0.025  0.090  -0.012 336 CYS KKK CA  
12779 C C   . CYS K 7   ? 1.051 0.815 0.646 0.039  0.051  0.007  336 CYS KKK C   
12780 O O   . CYS K 7   ? 1.088 0.846 0.676 0.048  0.045  0.026  336 CYS KKK O   
12781 C CB  . CYS K 7   ? 1.022 0.764 0.709 0.043  0.116  0.007  336 CYS KKK CB  
12782 S SG  . CYS K 7   ? 1.068 0.772 0.806 0.033  0.183  -0.014 336 CYS KKK SG  
12783 N N   . PRO K 8   ? 1.067 0.855 0.646 0.042  0.030  -0.005 337 PRO KKK N   
12784 C CA  . PRO K 8   ? 1.042 0.835 0.591 0.062  -0.000 0.013  337 PRO KKK CA  
12785 C C   . PRO K 8   ? 1.009 0.804 0.594 0.070  -0.005 0.027  337 PRO KKK C   
12786 O O   . PRO K 8   ? 1.016 0.834 0.612 0.077  -0.021 0.019  337 PRO KKK O   
12787 C CB  . PRO K 8   ? 1.071 0.915 0.600 0.066  -0.021 -0.012 337 PRO KKK CB  
12788 C CG  . PRO K 8   ? 1.059 0.930 0.643 0.039  0.003  -0.053 337 PRO KKK CG  
12789 C CD  . PRO K 8   ? 1.069 0.892 0.671 0.024  0.040  -0.046 337 PRO KKK CD  
12790 N N   . PHE K 9   ? 0.978 0.765 0.582 0.071  0.007  0.042  338 PHE KKK N   
12791 C CA  . PHE K 9   ? 0.936 0.742 0.563 0.078  0.002  0.054  338 PHE KKK CA  
12792 C C   . PHE K 9   ? 0.936 0.736 0.544 0.080  -0.012 0.054  338 PHE KKK C   
12793 O O   . PHE K 9   ? 0.947 0.765 0.573 0.083  -0.019 0.053  338 PHE KKK O   
12794 C CB  . PHE K 9   ? 0.930 0.762 0.576 0.081  0.014  0.063  338 PHE KKK CB  
12795 C CG  . PHE K 9   ? 0.948 0.786 0.621 0.096  0.034  0.076  338 PHE KKK CG  
12796 C CD1 . PHE K 9   ? 0.978 0.799 0.665 0.106  0.049  0.088  338 PHE KKK CD1 
12797 C CD2 . PHE K 9   ? 0.962 0.815 0.650 0.102  0.048  0.077  338 PHE KKK CD2 
12798 C CE1 . PHE K 9   ? 0.999 0.801 0.710 0.125  0.084  0.106  338 PHE KKK CE1 
12799 C CE2 . PHE K 9   ? 0.982 0.832 0.700 0.126  0.074  0.096  338 PHE KKK CE2 
12800 C CZ  . PHE K 9   ? 1.003 0.819 0.729 0.142  0.095  0.116  338 PHE KKK CZ  
12801 N N   . GLY K 10  ? 0.953 0.717 0.522 0.081  -0.007 0.056  339 GLY KKK N   
12802 C CA  . GLY K 10  ? 0.986 0.719 0.535 0.091  -0.004 0.062  339 GLY KKK CA  
12803 C C   . GLY K 10  ? 0.979 0.730 0.535 0.113  -0.027 0.064  339 GLY KKK C   
12804 O O   . GLY K 10  ? 0.951 0.701 0.526 0.117  -0.024 0.061  339 GLY KKK O   
12805 N N   . GLU K 11  ? 1.002 0.785 0.552 0.123  -0.047 0.057  340 GLU KKK N   
12806 C CA  . GLU K 11  ? 1.008 0.839 0.573 0.143  -0.071 0.044  340 GLU KKK CA  
12807 C C   . GLU K 11  ? 0.951 0.807 0.573 0.127  -0.068 0.026  340 GLU KKK C   
12808 O O   . GLU K 11  ? 0.938 0.825 0.582 0.142  -0.081 0.014  340 GLU KKK O   
12809 C CB  . GLU K 11  ? 1.042 0.930 0.602 0.142  -0.085 0.019  340 GLU KKK CB  
12810 C CG  . GLU K 11  ? 1.142 1.020 0.633 0.162  -0.090 0.037  340 GLU KKK CG  
12811 C CD  . GLU K 11  ? 1.193 1.154 0.676 0.156  -0.105 0.001  340 GLU KKK CD  
12812 O OE1 . GLU K 11  ? 1.176 1.203 0.717 0.134  -0.107 -0.046 340 GLU KKK OE1 
12813 O OE2 . GLU K 11  ? 1.257 1.217 0.677 0.167  -0.106 0.014  340 GLU KKK OE2 
12814 N N   . VAL K 12  ? 0.889 0.735 0.528 0.103  -0.050 0.027  341 VAL KKK N   
12815 C CA  . VAL K 12  ? 0.840 0.702 0.515 0.091  -0.040 0.020  341 VAL KKK CA  
12816 C C   . VAL K 12  ? 0.817 0.677 0.493 0.089  -0.037 0.029  341 VAL KKK C   
12817 O O   . VAL K 12  ? 0.794 0.669 0.490 0.088  -0.039 0.016  341 VAL KKK O   
12818 C CB  . VAL K 12  ? 0.835 0.687 0.518 0.080  -0.015 0.028  341 VAL KKK CB  
12819 C CG1 . VAL K 12  ? 0.835 0.692 0.535 0.077  0.004  0.035  341 VAL KKK CG1 
12820 C CG2 . VAL K 12  ? 0.855 0.705 0.546 0.070  -0.003 0.006  341 VAL KKK CG2 
12821 N N   . PHE K 13  ? 0.805 0.659 0.466 0.083  -0.028 0.039  342 PHE KKK N   
12822 C CA  . PHE K 13  ? 0.789 0.670 0.459 0.069  -0.018 0.031  342 PHE KKK CA  
12823 C C   . PHE K 13  ? 0.823 0.671 0.495 0.068  -0.008 0.018  342 PHE KKK C   
12824 O O   . PHE K 13  ? 0.814 0.686 0.506 0.052  0.004  -0.002 342 PHE KKK O   
12825 C CB  . PHE K 13  ? 0.767 0.675 0.433 0.061  -0.010 0.032  342 PHE KKK CB  
12826 C CG  . PHE K 13  ? 0.744 0.698 0.414 0.074  -0.012 0.051  342 PHE KKK CG  
12827 C CD1 . PHE K 13  ? 0.746 0.669 0.413 0.089  -0.009 0.070  342 PHE KKK CD1 
12828 C CD2 . PHE K 13  ? 0.732 0.762 0.406 0.076  -0.013 0.051  342 PHE KKK CD2 
12829 C CE1 . PHE K 13  ? 0.748 0.695 0.420 0.111  0.001  0.096  342 PHE KKK CE1 
12830 C CE2 . PHE K 13  ? 0.746 0.815 0.414 0.106  -0.012 0.084  342 PHE KKK CE2 
12831 C CZ  . PHE K 13  ? 0.754 0.771 0.423 0.126  -0.001 0.110  342 PHE KKK CZ  
12832 N N   . ASN K 14  ? 0.878 0.674 0.526 0.087  -0.008 0.030  343 ASN KKK N   
12833 C CA  . ASN K 14  ? 0.958 0.698 0.598 0.100  0.015  0.032  343 ASN KKK CA  
12834 C C   . ASN K 14  ? 0.942 0.679 0.581 0.142  -0.007 0.046  343 ASN KKK C   
12835 O O   . ASN K 14  ? 0.991 0.673 0.612 0.172  0.012  0.063  343 ASN KKK O   
12836 C CB  . ASN K 14  ? 1.067 0.743 0.669 0.097  0.046  0.043  343 ASN KKK CB  
12837 C CG  . ASN K 14  ? 1.142 0.838 0.761 0.052  0.076  0.012  343 ASN KKK CG  
12838 O OD1 . ASN K 14  ? 1.099 0.854 0.756 0.025  0.081  -0.019 343 ASN KKK OD1 
12839 N ND2 . ASN K 14  ? 1.350 1.008 0.941 0.044  0.098  0.015  343 ASN KKK ND2 
12840 N N   . ALA K 15  ? 0.889 0.685 0.550 0.145  -0.037 0.035  344 ALA KKK N   
12841 C CA  . ALA K 15  ? 0.894 0.728 0.578 0.178  -0.059 0.028  344 ALA KKK CA  
12842 C C   . ALA K 15  ? 0.912 0.720 0.625 0.188  -0.037 0.023  344 ALA KKK C   
12843 O O   . ALA K 15  ? 0.892 0.693 0.626 0.150  -0.014 0.005  344 ALA KKK O   
12844 C CB  . ALA K 15  ? 0.841 0.740 0.561 0.157  -0.075 -0.003 344 ALA KKK CB  
12845 N N   . THR K 16  ? 0.972 0.770 0.686 0.241  -0.039 0.039  345 THR KKK N   
12846 C CA  . THR K 16  ? 1.020 0.775 0.767 0.255  -0.004 0.036  345 THR KKK CA  
12847 C C   . THR K 16  ? 0.957 0.781 0.770 0.232  -0.015 -0.007 345 THR KKK C   
12848 O O   . THR K 16  ? 0.950 0.751 0.798 0.210  0.019  -0.028 345 THR KKK O   
12849 C CB  . THR K 16  ? 1.130 0.842 0.850 0.333  0.004  0.081  345 THR KKK CB  
12850 O OG1 . THR K 16  ? 1.141 0.953 0.858 0.375  -0.052 0.082  345 THR KKK OG1 
12851 C CG2 . THR K 16  ? 1.218 0.829 0.865 0.346  0.039  0.124  345 THR KKK CG2 
12852 N N   . ARG K 17  ? 0.907 0.815 0.737 0.229  -0.053 -0.027 346 ARG KKK N   
12853 C CA  . ARG K 17  ? 0.869 0.841 0.758 0.203  -0.056 -0.073 346 ARG KKK CA  
12854 C C   . ARG K 17  ? 0.815 0.805 0.694 0.150  -0.056 -0.088 346 ARG KKK C   
12855 O O   . ARG K 17  ? 0.795 0.785 0.641 0.147  -0.068 -0.075 346 ARG KKK O   
12856 C CB  . ARG K 17  ? 0.896 0.958 0.826 0.247  -0.088 -0.094 346 ARG KKK CB  
12857 C CG  . ARG K 17  ? 0.941 1.033 0.939 0.265  -0.076 -0.121 346 ARG KKK CG  
12858 C CD  . ARG K 17  ? 0.984 1.201 1.034 0.307  -0.112 -0.155 346 ARG KKK CD  
12859 N NE  . ARG K 17  ? 1.081 1.320 1.143 0.398  -0.126 -0.125 346 ARG KKK NE  
12860 C CZ  . ARG K 17  ? 1.169 1.436 1.181 0.468  -0.156 -0.081 346 ARG KKK CZ  
12861 N NH1 . ARG K 17  ? 1.151 1.425 1.101 0.447  -0.175 -0.071 346 ARG KKK NH1 
12862 N NH2 . ARG K 17  ? 1.248 1.533 1.267 0.563  -0.162 -0.044 346 ARG KKK NH2 
12863 N N   . PHE K 18  ? 0.668 0.520 0.509 -0.033 -0.008 0.095  347 PHE KKK N   
12864 C CA  . PHE K 18  ? 0.642 0.524 0.514 -0.050 -0.022 0.078  347 PHE KKK CA  
12865 C C   . PHE K 18  ? 0.615 0.519 0.497 -0.045 -0.041 0.068  347 PHE KKK C   
12866 O O   . PHE K 18  ? 0.644 0.539 0.521 -0.037 -0.043 0.072  347 PHE KKK O   
12867 C CB  . PHE K 18  ? 0.650 0.524 0.550 -0.072 -0.013 0.073  347 PHE KKK CB  
12868 C CG  . PHE K 18  ? 0.650 0.525 0.557 -0.083 -0.000 0.072  347 PHE KKK CG  
12869 C CD1 . PHE K 18  ? 0.698 0.551 0.585 -0.078 0.020  0.086  347 PHE KKK CD1 
12870 C CD2 . PHE K 18  ? 0.617 0.515 0.550 -0.097 -0.006 0.061  347 PHE KKK CD2 
12871 C CE1 . PHE K 18  ? 0.730 0.585 0.627 -0.089 0.034  0.085  347 PHE KKK CE1 
12872 C CE2 . PHE K 18  ? 0.633 0.536 0.575 -0.105 0.006  0.060  347 PHE KKK CE2 
12873 C CZ  . PHE K 18  ? 0.683 0.566 0.608 -0.102 0.026  0.071  347 PHE KKK CZ  
12874 N N   . ALA K 19  ? 0.590 0.521 0.489 -0.051 -0.053 0.055  348 ALA KKK N   
12875 C CA  . ALA K 19  ? 0.573 0.527 0.490 -0.050 -0.067 0.043  348 ALA KKK CA  
12876 C C   . ALA K 19  ? 0.568 0.517 0.507 -0.061 -0.067 0.043  348 ALA KKK C   
12877 O O   . ALA K 19  ? 0.613 0.552 0.560 -0.072 -0.059 0.045  348 ALA KKK O   
12878 C CB  . ALA K 19  ? 0.563 0.538 0.494 -0.055 -0.073 0.029  348 ALA KKK CB  
12879 N N   . SER K 20  ? 0.568 0.529 0.518 -0.057 -0.075 0.039  349 SER KKK N   
12880 C CA  . SER K 20  ? 0.561 0.528 0.533 -0.065 -0.075 0.036  349 SER KKK CA  
12881 C C   . SER K 20  ? 0.557 0.534 0.548 -0.074 -0.073 0.030  349 SER KKK C   
12882 O O   . SER K 20  ? 0.585 0.571 0.578 -0.074 -0.075 0.022  349 SER KKK O   
12883 C CB  . SER K 20  ? 0.559 0.538 0.539 -0.057 -0.082 0.032  349 SER KKK CB  
12884 O OG  . SER K 20  ? 0.567 0.534 0.531 -0.047 -0.082 0.040  349 SER KKK OG  
12885 N N   . VAL K 21  ? 0.534 0.509 0.535 -0.080 -0.068 0.033  350 VAL KKK N   
12886 C CA  . VAL K 21  ? 0.521 0.502 0.537 -0.084 -0.062 0.031  350 VAL KKK CA  
12887 C C   . VAL K 21  ? 0.534 0.523 0.568 -0.085 -0.061 0.024  350 VAL KKK C   
12888 O O   . VAL K 21  ? 0.566 0.555 0.608 -0.089 -0.056 0.019  350 VAL KKK O   
12889 C CB  . VAL K 21  ? 0.528 0.512 0.548 -0.083 -0.058 0.037  350 VAL KKK CB  
12890 C CG1 . VAL K 21  ? 0.533 0.520 0.558 -0.077 -0.059 0.039  350 VAL KKK CG1 
12891 C CG2 . VAL K 21  ? 0.544 0.533 0.572 -0.082 -0.051 0.039  350 VAL KKK CG2 
12892 N N   . TYR K 22  ? 0.505 0.501 0.550 -0.083 -0.063 0.022  351 TYR KKK N   
12893 C CA  . TYR K 22  ? 0.508 0.514 0.580 -0.087 -0.058 0.012  351 TYR KKK CA  
12894 C C   . TYR K 22  ? 0.515 0.533 0.590 -0.090 -0.065 -0.005 351 TYR KKK C   
12895 O O   . TYR K 22  ? 0.491 0.513 0.590 -0.098 -0.059 -0.019 351 TYR KKK O   
12896 C CB  . TYR K 22  ? 0.501 0.517 0.586 -0.084 -0.058 0.012  351 TYR KKK CB  
12897 C CG  . TYR K 22  ? 0.497 0.530 0.578 -0.079 -0.072 0.002  351 TYR KKK CG  
12898 C CD1 . TYR K 22  ? 0.528 0.554 0.581 -0.069 -0.080 0.010  351 TYR KKK CD1 
12899 C CD2 . TYR K 22  ? 0.506 0.563 0.612 -0.083 -0.075 -0.016 351 TYR KKK CD2 
12900 C CE1 . TYR K 22  ? 0.513 0.555 0.557 -0.058 -0.091 0.005  351 TYR KKK CE1 
12901 C CE2 . TYR K 22  ? 0.497 0.578 0.597 -0.073 -0.090 -0.026 351 TYR KKK CE2 
12902 C CZ  . TYR K 22  ? 0.505 0.577 0.571 -0.058 -0.097 -0.013 351 TYR KKK CZ  
12903 O OH  . TYR K 22  ? 0.522 0.616 0.578 -0.043 -0.110 -0.019 351 TYR KKK OH  
12904 N N   . ALA K 23  ? 0.535 0.556 0.584 -0.082 -0.077 -0.005 352 ALA KKK N   
12905 C CA  . ALA K 23  ? 0.535 0.572 0.576 -0.078 -0.086 -0.020 352 ALA KKK CA  
12906 C C   . ALA K 23  ? 0.555 0.578 0.571 -0.076 -0.083 -0.013 352 ALA KKK C   
12907 O O   . ALA K 23  ? 0.566 0.593 0.555 -0.065 -0.089 -0.011 352 ALA KKK O   
12908 C CB  . ALA K 23  ? 0.558 0.613 0.586 -0.064 -0.098 -0.021 352 ALA KKK CB  
12909 N N   . TRP K 24  ? 0.528 0.536 0.551 -0.084 -0.073 -0.007 353 TRP KKK N   
12910 C CA  . TRP K 24  ? 0.518 0.515 0.522 -0.084 -0.068 0.001  353 TRP KKK CA  
12911 C C   . TRP K 24  ? 0.554 0.560 0.545 -0.079 -0.072 -0.011 353 TRP KKK C   
12912 O O   . TRP K 24  ? 0.556 0.577 0.562 -0.081 -0.076 -0.030 353 TRP KKK O   
12913 C CB  . TRP K 24  ? 0.513 0.500 0.530 -0.090 -0.057 0.006  353 TRP KKK CB  
12914 C CG  . TRP K 24  ? 0.508 0.496 0.551 -0.095 -0.050 -0.004 353 TRP KKK CG  
12915 C CD1 . TRP K 24  ? 0.503 0.489 0.568 -0.097 -0.043 -0.002 353 TRP KKK CD1 
12916 C CD2 . TRP K 24  ? 0.515 0.501 0.564 -0.097 -0.044 -0.015 353 TRP KKK CD2 
12917 N NE1 . TRP K 24  ? 0.504 0.483 0.591 -0.102 -0.032 -0.012 353 TRP KKK NE1 
12918 C CE2 . TRP K 24  ? 0.505 0.484 0.582 -0.103 -0.033 -0.022 353 TRP KKK CE2 
12919 C CE3 . TRP K 24  ? 0.514 0.502 0.547 -0.095 -0.045 -0.021 353 TRP KKK CE3 
12920 C CZ2 . TRP K 24  ? 0.532 0.504 0.624 -0.107 -0.022 -0.035 353 TRP KKK CZ2 
12921 C CZ3 . TRP K 24  ? 0.526 0.511 0.571 -0.097 -0.038 -0.035 353 TRP KKK CZ3 
12922 C CH2 . TRP K 24  ? 0.543 0.518 0.618 -0.104 -0.026 -0.042 353 TRP KKK CH2 
12923 N N   . ASN K 25  ? 0.587 0.586 0.551 -0.073 -0.069 -0.001 354 ASN KKK N   
12924 C CA  . ASN K 25  ? 0.630 0.638 0.571 -0.062 -0.072 -0.008 354 ASN KKK CA  
12925 C C   . ASN K 25  ? 0.613 0.616 0.558 -0.068 -0.063 -0.013 354 ASN KKK C   
12926 O O   . ASN K 25  ? 0.603 0.592 0.554 -0.075 -0.053 -0.000 354 ASN KKK O   
12927 C CB  . ASN K 25  ? 0.700 0.697 0.606 -0.049 -0.069 0.009  354 ASN KKK CB  
12928 C CG  . ASN K 25  ? 0.771 0.779 0.647 -0.033 -0.070 0.004  354 ASN KKK CG  
12929 O OD1 . ASN K 25  ? 0.870 0.869 0.733 -0.032 -0.059 0.011  354 ASN KKK OD1 
12930 N ND2 . ASN K 25  ? 0.806 0.840 0.673 -0.018 -0.085 -0.008 354 ASN KKK ND2 
12931 N N   . ARG K 26  ? 0.601 0.619 0.543 -0.064 -0.066 -0.032 355 ARG KKK N   
12932 C CA  . ARG K 26  ? 0.637 0.651 0.576 -0.065 -0.058 -0.038 355 ARG KKK CA  
12933 C C   . ARG K 26  ? 0.672 0.695 0.574 -0.049 -0.058 -0.037 355 ARG KKK C   
12934 O O   . ARG K 26  ? 0.682 0.726 0.572 -0.038 -0.070 -0.054 355 ARG KKK O   
12935 C CB  . ARG K 26  ? 0.635 0.662 0.595 -0.069 -0.060 -0.066 355 ARG KKK CB  
12936 C CG  . ARG K 26  ? 0.638 0.649 0.631 -0.082 -0.049 -0.069 355 ARG KKK CG  
12937 C CD  . ARG K 26  ? 0.643 0.646 0.636 -0.081 -0.038 -0.077 355 ARG KKK CD  
12938 N NE  . ARG K 26  ? 0.636 0.620 0.648 -0.087 -0.026 -0.060 355 ARG KKK NE  
12939 C CZ  . ARG K 26  ? 0.614 0.583 0.653 -0.092 -0.013 -0.064 355 ARG KKK CZ  
12940 N NH1 . ARG K 26  ? 0.671 0.637 0.726 -0.096 -0.009 -0.090 355 ARG KKK NH1 
12941 N NH2 . ARG K 26  ? 0.589 0.547 0.635 -0.090 -0.004 -0.044 355 ARG KKK NH2 
12942 N N   . LYS K 27  ? 0.698 0.709 0.586 -0.048 -0.045 -0.024 356 LYS KKK N   
12943 C CA  . LYS K 27  ? 0.732 0.750 0.586 -0.032 -0.041 -0.025 356 LYS KKK CA  
12944 C C   . LYS K 27  ? 0.701 0.719 0.567 -0.038 -0.032 -0.037 356 LYS KKK C   
12945 O O   . LYS K 27  ? 0.661 0.667 0.550 -0.050 -0.023 -0.029 356 LYS KKK O   
12946 C CB  . LYS K 27  ? 0.777 0.780 0.605 -0.025 -0.027 0.002  356 LYS KKK CB  
12947 C CG  . LYS K 27  ? 0.869 0.875 0.658 -0.006 -0.017 0.008  356 LYS KKK CG  
12948 C CD  . LYS K 27  ? 0.959 0.949 0.711 0.010  -0.005 0.034  356 LYS KKK CD  
12949 C CE  . LYS K 27  ? 1.028 1.028 0.732 0.038  -0.000 0.037  356 LYS KKK CE  
12950 N NZ  . LYS K 27  ? 1.077 1.073 0.778 0.035  0.019  0.041  356 LYS KKK NZ  
12951 N N   . ARG K 28  ? 0.742 0.776 0.593 -0.027 -0.037 -0.058 357 ARG KKK N   
12952 C CA  . ARG K 28  ? 0.759 0.792 0.614 -0.027 -0.026 -0.069 357 ARG KKK CA  
12953 C C   . ARG K 28  ? 0.752 0.780 0.575 -0.016 -0.011 -0.047 357 ARG KKK C   
12954 O O   . ARG K 28  ? 0.763 0.797 0.550 0.000  -0.012 -0.038 357 ARG KKK O   
12955 C CB  . ARG K 28  ? 0.795 0.848 0.648 -0.021 -0.037 -0.104 357 ARG KKK CB  
12956 C CG  . ARG K 28  ? 0.854 0.901 0.713 -0.022 -0.025 -0.118 357 ARG KKK CG  
12957 C CD  . ARG K 28  ? 0.908 0.978 0.748 -0.009 -0.033 -0.152 357 ARG KKK CD  
12958 N NE  . ARG K 28  ? 0.924 1.009 0.793 -0.018 -0.047 -0.186 357 ARG KKK NE  
12959 C CZ  . ARG K 28  ? 0.944 1.012 0.858 -0.037 -0.040 -0.204 357 ARG KKK CZ  
12960 N NH1 . ARG K 28  ? 0.941 0.978 0.871 -0.044 -0.022 -0.188 357 ARG KKK NH1 
12961 N NH2 . ARG K 28  ? 0.954 1.036 0.898 -0.048 -0.051 -0.235 357 ARG KKK NH2 
12962 N N   . ILE K 29  ? 0.746 0.764 0.582 -0.023 0.004  -0.039 358 ILE KKK N   
12963 C CA  . ILE K 29  ? 0.759 0.777 0.573 -0.014 0.022  -0.024 358 ILE KKK CA  
12964 C C   . ILE K 29  ? 0.762 0.786 0.577 -0.009 0.027  -0.043 358 ILE KKK C   
12965 O O   . ILE K 29  ? 0.759 0.778 0.606 -0.019 0.028  -0.053 358 ILE KKK O   
12966 C CB  . ILE K 29  ? 0.736 0.743 0.573 -0.028 0.035  -0.001 358 ILE KKK CB  
12967 C CG1 . ILE K 29  ? 0.736 0.733 0.567 -0.031 0.033  0.015  358 ILE KKK CG1 
12968 C CG2 . ILE K 29  ? 0.750 0.759 0.582 -0.025 0.057  0.010  358 ILE KKK CG2 
12969 C CD1 . ILE K 29  ? 0.734 0.725 0.596 -0.048 0.039  0.028  358 ILE KKK CD1 
12970 N N   . SER K 30  ? 0.797 0.831 0.574 0.010  0.032  -0.047 359 SER KKK N   
12971 C CA  . SER K 30  ? 0.821 0.862 0.592 0.018  0.038  -0.067 359 SER KKK CA  
12972 C C   . SER K 30  ? 0.854 0.906 0.581 0.040  0.052  -0.058 359 SER KKK C   
12973 O O   . SER K 30  ? 0.884 0.936 0.580 0.051  0.054  -0.039 359 SER KKK O   
12974 C CB  . SER K 30  ? 0.819 0.870 0.598 0.018  0.021  -0.104 359 SER KKK CB  
12975 O OG  . SER K 30  ? 0.835 0.903 0.591 0.028  0.004  -0.111 359 SER KKK OG  
12976 N N   . ASN K 31  ? 0.879 0.935 0.600 0.047  0.062  -0.070 360 ASN KKK N   
12977 C CA  . ASN K 31  ? 0.929 0.996 0.604 0.071  0.077  -0.065 360 ASN KKK CA  
12978 C C   . ASN K 31  ? 0.928 0.985 0.589 0.072  0.097  -0.026 360 ASN KKK C   
12979 O O   . ASN K 31  ? 0.970 1.030 0.587 0.093  0.101  -0.013 360 ASN KKK O   
12980 C CB  . ASN K 31  ? 0.980 1.069 0.614 0.094  0.059  -0.089 360 ASN KKK CB  
12981 C CG  . ASN K 31  ? 0.991 1.090 0.646 0.088  0.043  -0.134 360 ASN KKK CG  
12982 O OD1 . ASN K 31  ? 0.985 1.094 0.650 0.084  0.021  -0.158 360 ASN KKK OD1 
12983 N ND2 . ASN K 31  ? 1.009 1.105 0.668 0.091  0.055  -0.146 360 ASN KKK ND2 
12984 N N   . CYS K 32  ? 0.892 0.939 0.593 0.052  0.111  -0.009 361 CYS KKK N   
12985 C CA  . CYS K 32  ? 0.908 0.945 0.613 0.046  0.134  0.023  361 CYS KKK CA  
12986 C C   . CYS K 32  ? 0.868 0.909 0.620 0.027  0.148  0.028  361 CYS KKK C   
12987 O O   . CYS K 32  ? 0.839 0.887 0.622 0.019  0.136  0.011  361 CYS KKK O   
12988 C CB  . CYS K 32  ? 0.907 0.930 0.614 0.038  0.124  0.036  361 CYS KKK CB  
12989 S SG  . CYS K 32  ? 0.872 0.893 0.629 0.013  0.098  0.020  361 CYS KKK SG  
12990 N N   . VAL K 33  ? 0.880 0.919 0.639 0.022  0.175  0.051  362 VAL KKK N   
12991 C CA  . VAL K 33  ? 0.875 0.928 0.685 0.003  0.190  0.055  362 VAL KKK CA  
12992 C C   . VAL K 33  ? 0.863 0.910 0.709 -0.020 0.180  0.060  362 VAL KKK C   
12993 O O   . VAL K 33  ? 0.861 0.889 0.695 -0.023 0.189  0.075  362 VAL KKK O   
12994 C CB  . VAL K 33  ? 0.918 0.974 0.724 0.005  0.226  0.073  362 VAL KKK CB  
12995 C CG1 . VAL K 33  ? 0.887 0.967 0.753 -0.015 0.239  0.072  362 VAL KKK CG1 
12996 C CG2 . VAL K 33  ? 0.952 1.013 0.715 0.031  0.237  0.071  362 VAL KKK CG2 
12997 N N   . ALA K 34  ? 0.871 0.931 0.755 -0.031 0.164  0.047  363 ALA KKK N   
12998 C CA  . ALA K 34  ? 0.853 0.915 0.773 -0.050 0.153  0.048  363 ALA KKK CA  
12999 C C   . ALA K 34  ? 0.874 0.959 0.836 -0.065 0.174  0.052  363 ALA KKK C   
13000 O O   . ALA K 34  ? 0.874 0.988 0.868 -0.066 0.172  0.043  363 ALA KKK O   
13001 C CB  . ALA K 34  ? 0.823 0.891 0.761 -0.050 0.129  0.034  363 ALA KKK CB  
13002 N N   . ASP K 35  ? 0.890 0.961 0.852 -0.076 0.194  0.066  364 ASP KKK N   
13003 C CA  . ASP K 35  ? 0.874 0.966 0.885 -0.097 0.214  0.065  364 ASP KKK CA  
13004 C C   . ASP K 35  ? 0.811 0.902 0.850 -0.115 0.198  0.058  364 ASP KKK C   
13005 O O   . ASP K 35  ? 0.806 0.864 0.826 -0.119 0.200  0.068  364 ASP KKK O   
13006 C CB  . ASP K 35  ? 0.936 1.008 0.937 -0.101 0.252  0.083  364 ASP KKK CB  
13007 C CG  . ASP K 35  ? 0.947 1.052 1.008 -0.123 0.275  0.075  364 ASP KKK CG  
13008 O OD1 . ASP K 35  ? 0.961 1.103 1.068 -0.134 0.257  0.056  364 ASP KKK OD1 
13009 O OD2 . ASP K 35  ? 0.975 1.071 1.037 -0.127 0.312  0.088  364 ASP KKK OD2 
13010 N N   . TYR K 36  ? 0.757 0.887 0.839 -0.123 0.184  0.042  365 TYR KKK N   
13011 C CA  . TYR K 36  ? 0.735 0.873 0.843 -0.136 0.165  0.032  365 TYR KKK CA  
13012 C C   . TYR K 36  ? 0.734 0.888 0.889 -0.161 0.186  0.024  365 TYR KKK C   
13013 O O   . TYR K 36  ? 0.711 0.872 0.888 -0.174 0.173  0.013  365 TYR KKK O   
13014 C CB  . TYR K 36  ? 0.704 0.879 0.831 -0.125 0.141  0.019  365 TYR KKK CB  
13015 C CG  . TYR K 36  ? 0.700 0.850 0.788 -0.106 0.122  0.023  365 TYR KKK CG  
13016 C CD1 . TYR K 36  ? 0.726 0.872 0.791 -0.089 0.126  0.026  365 TYR KKK CD1 
13017 C CD2 . TYR K 36  ? 0.700 0.831 0.775 -0.106 0.102  0.024  365 TYR KKK CD2 
13018 C CE1 . TYR K 36  ? 0.729 0.851 0.764 -0.075 0.112  0.025  365 TYR KKK CE1 
13019 C CE2 . TYR K 36  ? 0.703 0.812 0.750 -0.092 0.088  0.025  365 TYR KKK CE2 
13020 C CZ  . TYR K 36  ? 0.723 0.828 0.751 -0.077 0.093  0.025  365 TYR KKK CZ  
13021 O OH  . TYR K 36  ? 0.763 0.847 0.770 -0.066 0.081  0.021  365 TYR KKK OH  
13022 N N   . SER K 37  ? 0.750 0.909 0.921 -0.170 0.218  0.029  366 SER KKK N   
13023 C CA  . SER K 37  ? 0.773 0.948 0.998 -0.198 0.241  0.017  366 SER KKK CA  
13024 C C   . SER K 37  ? 0.807 0.934 1.022 -0.212 0.250  0.024  366 SER KKK C   
13025 O O   . SER K 37  ? 0.828 0.969 1.091 -0.236 0.256  0.007  366 SER KKK O   
13026 C CB  . SER K 37  ? 0.787 0.976 1.035 -0.205 0.278  0.020  366 SER KKK CB  
13027 O OG  . SER K 37  ? 0.816 0.963 1.008 -0.187 0.295  0.046  366 SER KKK OG  
13028 N N   . VAL K 38  ? 0.815 0.889 0.971 -0.195 0.247  0.047  367 VAL KKK N   
13029 C CA  . VAL K 38  ? 0.831 0.859 0.974 -0.203 0.252  0.055  367 VAL KKK CA  
13030 C C   . VAL K 38  ? 0.797 0.847 0.966 -0.213 0.220  0.033  367 VAL KKK C   
13031 O O   . VAL K 38  ? 0.785 0.827 0.986 -0.234 0.231  0.022  367 VAL KKK O   
13032 C CB  . VAL K 38  ? 0.881 0.861 0.954 -0.177 0.251  0.081  367 VAL KKK CB  
13033 C CG1 . VAL K 38  ? 0.849 0.839 0.890 -0.157 0.210  0.077  367 VAL KKK CG1 
13034 C CG2 . VAL K 38  ? 0.909 0.838 0.968 -0.182 0.269  0.095  367 VAL KKK CG2 
13035 N N   . LEU K 39  ? 0.743 0.822 0.903 -0.198 0.186  0.025  368 LEU KKK N   
13036 C CA  . LEU K 39  ? 0.706 0.809 0.886 -0.201 0.156  0.007  368 LEU KKK CA  
13037 C C   . LEU K 39  ? 0.716 0.877 0.959 -0.219 0.157  -0.021 368 LEU KKK C   
13038 O O   . LEU K 39  ? 0.733 0.908 1.001 -0.231 0.146  -0.039 368 LEU KKK O   
13039 C CB  . LEU K 39  ? 0.663 0.775 0.813 -0.177 0.127  0.010  368 LEU KKK CB  
13040 C CG  . LEU K 39  ? 0.680 0.748 0.775 -0.160 0.122  0.030  368 LEU KKK CG  
13041 C CD1 . LEU K 39  ? 0.665 0.742 0.742 -0.141 0.098  0.029  368 LEU KKK CD1 
13042 C CD2 . LEU K 39  ? 0.697 0.726 0.776 -0.165 0.122  0.037  368 LEU KKK CD2 
13043 N N   . TYR K 40  ? 0.955 0.783 0.767 -0.012 0.136  -0.021 369 TYR KKK N   
13044 C CA  . TYR K 40  ? 0.955 0.816 0.787 -0.038 0.144  -0.036 369 TYR KKK CA  
13045 C C   . TYR K 40  ? 0.979 0.810 0.795 -0.069 0.180  -0.039 369 TYR KKK C   
13046 O O   . TYR K 40  ? 0.975 0.835 0.810 -0.096 0.187  -0.055 369 TYR KKK O   
13047 C CB  . TYR K 40  ? 0.952 0.858 0.790 -0.033 0.140  -0.045 369 TYR KKK CB  
13048 C CG  . TYR K 40  ? 0.927 0.855 0.772 -0.006 0.112  -0.047 369 TYR KKK CG  
13049 C CD1 . TYR K 40  ? 0.933 0.854 0.786 0.001  0.093  -0.047 369 TYR KKK CD1 
13050 C CD2 . TYR K 40  ? 0.916 0.865 0.753 0.011  0.108  -0.049 369 TYR KKK CD2 
13051 C CE1 . TYR K 40  ? 0.949 0.871 0.794 0.024  0.076  -0.050 369 TYR KKK CE1 
13052 C CE2 . TYR K 40  ? 0.925 0.879 0.757 0.035  0.087  -0.052 369 TYR KKK CE2 
13053 C CZ  . TYR K 40  ? 0.939 0.874 0.772 0.041  0.073  -0.053 369 TYR KKK CZ  
13054 O OH  . TYR K 40  ? 0.966 0.887 0.781 0.064  0.061  -0.056 369 TYR KKK OH  
13055 N N   . ASN K 41  ? 1.019 0.795 0.797 -0.062 0.204  -0.024 370 ASN KKK N   
13056 C CA  . ASN K 41  ? 1.108 0.831 0.853 -0.092 0.249  -0.026 370 ASN KKK CA  
13057 C C   . ASN K 41  ? 1.157 0.814 0.875 -0.089 0.263  -0.015 370 ASN KKK C   
13058 O O   . ASN K 41  ? 1.253 0.841 0.927 -0.108 0.306  -0.013 370 ASN KKK O   
13059 C CB  . ASN K 41  ? 1.143 0.827 0.846 -0.082 0.276  -0.012 370 ASN KKK CB  
13060 C CG  . ASN K 41  ? 1.117 0.867 0.843 -0.091 0.269  -0.025 370 ASN KKK CG  
13061 O OD1 . ASN K 41  ? 1.092 0.904 0.853 -0.122 0.267  -0.049 370 ASN KKK OD1 
13062 N ND2 . ASN K 41  ? 1.124 0.869 0.831 -0.061 0.266  -0.011 370 ASN KKK ND2 
13063 N N   . SER K 42  ? 1.157 0.830 0.894 -0.066 0.231  -0.010 371 SER KKK N   
13064 C CA  . SER K 42  ? 1.194 0.822 0.914 -0.062 0.239  -0.004 371 SER KKK CA  
13065 C C   . SER K 42  ? 1.175 0.834 0.931 -0.099 0.235  -0.025 371 SER KKK C   
13066 O O   . SER K 42  ? 1.131 0.860 0.932 -0.102 0.205  -0.037 371 SER KKK O   
13067 C CB  . SER K 42  ? 1.188 0.831 0.911 -0.021 0.209  0.010  371 SER KKK CB  
13068 O OG  . SER K 42  ? 1.214 0.823 0.920 -0.014 0.215  0.016  371 SER KKK OG  
13069 N N   . ALA K 43  ? 1.210 0.815 0.939 -0.125 0.269  -0.031 372 ALA KKK N   
13070 C CA  . ALA K 43  ? 1.161 0.791 0.917 -0.159 0.270  -0.053 372 ALA KKK CA  
13071 C C   . ALA K 43  ? 1.146 0.737 0.887 -0.136 0.263  -0.040 372 ALA KKK C   
13072 O O   . ALA K 43  ? 1.197 0.802 0.956 -0.158 0.262  -0.055 372 ALA KKK O   
13073 C CB  . ALA K 43  ? 1.204 0.805 0.938 -0.210 0.316  -0.075 372 ALA KKK CB  
13074 N N   . SER K 44  ? 1.109 0.666 0.821 -0.091 0.256  -0.015 373 SER KKK N   
13075 C CA  . SER K 44  ? 1.085 0.618 0.780 -0.061 0.248  -0.002 373 SER KKK CA  
13076 C C   . SER K 44  ? 0.943 0.551 0.689 -0.049 0.203  -0.004 373 SER KKK C   
13077 O O   . SER K 44  ? 0.915 0.521 0.661 -0.039 0.196  -0.001 373 SER KKK O   
13078 C CB  . SER K 44  ? 1.167 0.644 0.802 -0.014 0.263  0.023  373 SER KKK CB  
13079 O OG  . SER K 44  ? 1.281 0.657 0.849 -0.019 0.313  0.029  373 SER KKK OG  
13080 N N   . PHE K 45  ? 0.866 0.531 0.648 -0.050 0.177  -0.008 374 PHE KKK N   
13081 C CA  . PHE K 45  ? 0.815 0.534 0.633 -0.040 0.141  -0.010 374 PHE KKK CA  
13082 C C   . PHE K 45  ? 0.777 0.517 0.623 -0.063 0.135  -0.022 374 PHE KKK C   
13083 O O   . PHE K 45  ? 0.776 0.529 0.635 -0.088 0.144  -0.036 374 PHE KKK O   
13084 C CB  . PHE K 45  ? 0.778 0.535 0.615 -0.036 0.122  -0.013 374 PHE KKK CB  
13085 C CG  . PHE K 45  ? 0.795 0.544 0.608 -0.010 0.123  -0.003 374 PHE KKK CG  
13086 C CD1 . PHE K 45  ? 0.822 0.563 0.608 0.019  0.125  0.008  374 PHE KKK CD1 
13087 C CD2 . PHE K 45  ? 0.802 0.565 0.618 -0.011 0.121  -0.006 374 PHE KKK CD2 
13088 C CE1 . PHE K 45  ? 0.855 0.604 0.618 0.048  0.125  0.015  374 PHE KKK CE1 
13089 C CE2 . PHE K 45  ? 0.839 0.602 0.633 0.014  0.122  0.002  374 PHE KKK CE2 
13090 C CZ  . PHE K 45  ? 0.856 0.615 0.624 0.044  0.123  0.012  374 PHE KKK CZ  
13091 N N   . SER K 46  ? 0.753 0.504 0.608 -0.054 0.120  -0.019 375 SER KKK N   
13092 C CA  . SER K 46  ? 0.717 0.491 0.597 -0.070 0.112  -0.029 375 SER KKK CA  
13093 C C   . SER K 46  ? 0.671 0.486 0.577 -0.073 0.092  -0.034 375 SER KKK C   
13094 O O   . SER K 46  ? 0.648 0.488 0.570 -0.084 0.090  -0.044 375 SER KKK O   
13095 C CB  . SER K 46  ? 0.721 0.492 0.597 -0.058 0.105  -0.022 375 SER KKK CB  
13096 O OG  . SER K 46  ? 0.725 0.518 0.604 -0.041 0.088  -0.016 375 SER KKK OG  
13097 N N   . THR K 47  ? 0.644 0.463 0.548 -0.061 0.080  -0.029 376 THR KKK N   
13098 C CA  . THR K 47  ? 0.632 0.469 0.545 -0.058 0.066  -0.032 376 THR KKK CA  
13099 C C   . THR K 47  ? 0.631 0.463 0.534 -0.049 0.063  -0.031 376 THR KKK C   
13100 O O   . THR K 47  ? 0.644 0.469 0.536 -0.042 0.064  -0.027 376 THR KKK O   
13101 C CB  . THR K 47  ? 0.629 0.467 0.546 -0.059 0.056  -0.030 376 THR KKK CB  
13102 O OG1 . THR K 47  ? 0.629 0.464 0.541 -0.056 0.050  -0.032 376 THR KKK OG1 
13103 C CG2 . THR K 47  ? 0.630 0.468 0.540 -0.056 0.051  -0.029 376 THR KKK CG2 
13104 N N   . PHE K 48  ? 0.632 0.471 0.533 -0.044 0.059  -0.035 377 PHE KKK N   
13105 C CA  . PHE K 48  ? 0.640 0.474 0.530 -0.034 0.056  -0.036 377 PHE KKK CA  
13106 C C   . PHE K 48  ? 0.649 0.478 0.528 -0.024 0.051  -0.038 377 PHE KKK C   
13107 O O   . PHE K 48  ? 0.652 0.505 0.532 -0.015 0.053  -0.041 377 PHE KKK O   
13108 C CB  . PHE K 48  ? 0.651 0.493 0.539 -0.034 0.066  -0.036 377 PHE KKK CB  
13109 C CG  . PHE K 48  ? 0.671 0.514 0.548 -0.022 0.063  -0.036 377 PHE KKK CG  
13110 C CD1 . PHE K 48  ? 0.692 0.525 0.558 -0.013 0.054  -0.040 377 PHE KKK CD1 
13111 C CD2 . PHE K 48  ? 0.705 0.550 0.576 -0.021 0.075  -0.034 377 PHE KKK CD2 
13112 C CE1 . PHE K 48  ? 0.717 0.549 0.571 -0.003 0.052  -0.043 377 PHE KKK CE1 
13113 C CE2 . PHE K 48  ? 0.718 0.568 0.579 -0.009 0.073  -0.035 377 PHE KKK CE2 
13114 C CZ  . PHE K 48  ? 0.724 0.570 0.578 0.001  0.060  -0.040 377 PHE KKK CZ  
13115 N N   . LYS K 49  ? 0.671 0.471 0.535 -0.026 0.048  -0.039 378 LYS KKK N   
13116 C CA  . LYS K 49  ? 0.718 0.488 0.554 -0.012 0.050  -0.038 378 LYS KKK CA  
13117 C C   . LYS K 49  ? 0.782 0.512 0.592 -0.015 0.053  -0.044 378 LYS KKK C   
13118 O O   . LYS K 49  ? 0.780 0.510 0.596 -0.036 0.052  -0.052 378 LYS KKK O   
13119 C CB  . LYS K 49  ? 0.719 0.469 0.548 -0.017 0.053  -0.034 378 LYS KKK CB  
13120 C CG  . LYS K 49  ? 0.690 0.478 0.543 -0.016 0.051  -0.031 378 LYS KKK CG  
13121 C CD  . LYS K 49  ? 0.719 0.480 0.553 -0.013 0.056  -0.025 378 LYS KKK CD  
13122 C CE  . LYS K 49  ? 0.684 0.479 0.543 -0.019 0.053  -0.024 378 LYS KKK CE  
13123 N NZ  . LYS K 49  ? 0.715 0.475 0.548 -0.014 0.059  -0.017 378 LYS KKK NZ  
13124 N N   . CYS K 50  ? 0.504 0.475 0.517 -0.032 -0.024 0.011  379 CYS KKK N   
13125 C CA  . CYS K 50  ? 0.522 0.485 0.542 -0.026 -0.017 0.000  379 CYS KKK CA  
13126 C C   . CYS K 50  ? 0.522 0.473 0.558 -0.022 -0.023 0.005  379 CYS KKK C   
13127 O O   . CYS K 50  ? 0.521 0.476 0.569 -0.021 -0.032 0.018  379 CYS KKK O   
13128 C CB  . CYS K 50  ? 0.564 0.541 0.596 -0.021 -0.006 -0.009 379 CYS KKK CB  
13129 S SG  . CYS K 50  ? 0.593 0.583 0.603 -0.029 0.000  -0.011 379 CYS KKK SG  
13130 N N   . TYR K 51  ? 0.536 0.472 0.572 -0.020 -0.021 -0.003 380 TYR KKK N   
13131 C CA  . TYR K 51  ? 0.555 0.475 0.606 -0.016 -0.026 0.001  380 TYR KKK CA  
13132 C C   . TYR K 51  ? 0.565 0.478 0.633 -0.008 -0.017 -0.014 380 TYR KKK C   
13133 O O   . TYR K 51  ? 0.571 0.483 0.625 -0.010 -0.010 -0.030 380 TYR KKK O   
13134 C CB  . TYR K 51  ? 0.544 0.452 0.576 -0.025 -0.031 0.005  380 TYR KKK CB  
13135 C CG  . TYR K 51  ? 0.534 0.451 0.548 -0.033 -0.037 0.016  380 TYR KKK CG  
13136 C CD1 . TYR K 51  ? 0.547 0.473 0.542 -0.037 -0.034 0.011  380 TYR KKK CD1 
13137 C CD2 . TYR K 51  ? 0.532 0.448 0.549 -0.036 -0.046 0.031  380 TYR KKK CD2 
13138 C CE1 . TYR K 51  ? 0.537 0.468 0.518 -0.043 -0.038 0.018  380 TYR KKK CE1 
13139 C CE2 . TYR K 51  ? 0.538 0.462 0.537 -0.043 -0.050 0.038  380 TYR KKK CE2 
13140 C CZ  . TYR K 51  ? 0.526 0.456 0.508 -0.046 -0.046 0.030  380 TYR KKK CZ  
13141 O OH  . TYR K 51  ? 0.497 0.434 0.465 -0.053 -0.050 0.035  380 TYR KKK OH  
13142 N N   . GLY K 52  ? 0.592 0.501 0.692 0.001  -0.019 -0.011 381 GLY KKK N   
13143 C CA  . GLY K 52  ? 0.615 0.515 0.737 0.011  -0.010 -0.027 381 GLY KKK CA  
13144 C C   . GLY K 52  ? 0.629 0.549 0.760 0.018  0.003  -0.040 381 GLY KKK C   
13145 O O   . GLY K 52  ? 0.682 0.597 0.836 0.027  0.011  -0.054 381 GLY KKK O   
13146 N N   . VAL K 53  ? 0.625 0.565 0.740 0.013  0.005  -0.036 382 VAL KKK N   
13147 C CA  . VAL K 53  ? 0.631 0.595 0.757 0.017  0.018  -0.045 382 VAL KKK CA  
13148 C C   . VAL K 53  ? 0.610 0.593 0.733 0.012  0.012  -0.028 382 VAL KKK C   
13149 O O   . VAL K 53  ? 0.562 0.541 0.662 0.002  0.003  -0.018 382 VAL KKK O   
13150 C CB  . VAL K 53  ? 0.653 0.622 0.753 0.013  0.031  -0.063 382 VAL KKK CB  
13151 C CG1 . VAL K 53  ? 0.700 0.650 0.804 0.018  0.037  -0.083 382 VAL KKK CG1 
13152 C CG2 . VAL K 53  ? 0.637 0.603 0.698 -0.000 0.024  -0.057 382 VAL KKK CG2 
13153 N N   . SER K 54  ? 0.632 0.637 0.781 0.018  0.018  -0.028 383 SER KKK N   
13154 C CA  . SER K 54  ? 0.630 0.656 0.780 0.012  0.013  -0.014 383 SER KKK CA  
13155 C C   . SER K 54  ? 0.623 0.660 0.744 0.002  0.022  -0.019 383 SER KKK C   
13156 O O   . SER K 54  ? 0.625 0.667 0.739 0.004  0.036  -0.034 383 SER KKK O   
13157 C CB  . SER K 54  ? 0.641 0.689 0.833 0.022  0.017  -0.011 383 SER KKK CB  
13158 O OG  . SER K 54  ? 0.659 0.728 0.852 0.014  0.013  0.001  383 SER KKK OG  
13159 N N   . PRO K 55  ? 0.634 0.674 0.736 -0.008 0.013  -0.007 384 PRO KKK N   
13160 C CA  . PRO K 55  ? 0.634 0.684 0.712 -0.018 0.019  -0.008 384 PRO KKK CA  
13161 C C   . PRO K 55  ? 0.644 0.719 0.738 -0.016 0.033  -0.013 384 PRO KKK C   
13162 O O   . PRO K 55  ? 0.639 0.722 0.712 -0.023 0.043  -0.018 384 PRO KKK O   
13163 C CB  . PRO K 55  ? 0.594 0.642 0.664 -0.027 0.006  0.007  384 PRO KKK CB  
13164 C CG  . PRO K 55  ? 0.598 0.628 0.667 -0.024 -0.006 0.011  384 PRO KKK CG  
13165 C CD  . PRO K 55  ? 0.610 0.641 0.710 -0.013 -0.003 0.008  384 PRO KKK CD  
13166 N N   . THR K 56  ? 0.658 0.748 0.788 -0.008 0.035  -0.010 385 THR KKK N   
13167 C CA  . THR K 56  ? 0.689 0.809 0.843 -0.006 0.049  -0.015 385 THR KKK CA  
13168 C C   . THR K 56  ? 0.737 0.860 0.889 0.001  0.067  -0.035 385 THR KKK C   
13169 O O   . THR K 56  ? 0.763 0.911 0.925 0.001  0.083  -0.041 385 THR KKK O   
13170 C CB  . THR K 56  ? 0.667 0.804 0.866 0.002  0.044  -0.006 385 THR KKK CB  
13171 O OG1 . THR K 56  ? 0.631 0.754 0.852 0.016  0.042  -0.012 385 THR KKK OG1 
13172 C CG2 . THR K 56  ? 0.642 0.779 0.842 -0.006 0.026  0.013  385 THR KKK CG2 
13173 N N   . LYS K 57  ? 0.769 0.867 0.909 0.006  0.066  -0.046 386 LYS KKK N   
13174 C CA  . LYS K 57  ? 0.793 0.891 0.934 0.013  0.083  -0.069 386 LYS KKK CA  
13175 C C   . LYS K 57  ? 0.784 0.871 0.879 0.003  0.086  -0.078 386 LYS KKK C   
13176 O O   . LYS K 57  ? 0.817 0.904 0.907 0.007  0.099  -0.098 386 LYS KKK O   
13177 C CB  . LYS K 57  ? 0.829 0.906 0.996 0.027  0.079  -0.076 386 LYS KKK CB  
13178 C CG  . LYS K 57  ? 0.863 0.951 1.079 0.038  0.074  -0.067 386 LYS KKK CG  
13179 C CD  . LYS K 57  ? 0.922 0.995 1.173 0.055  0.077  -0.079 386 LYS KKK CD  
13180 C CE  . LYS K 57  ? 0.977 1.031 1.249 0.060  0.057  -0.061 386 LYS KKK CE  
13181 N NZ  . LYS K 57  ? 0.996 1.065 1.324 0.074  0.056  -0.054 386 LYS KKK NZ  
13182 N N   . LEU K 58  ? 0.764 0.844 0.830 -0.008 0.075  -0.065 387 LEU KKK N   
13183 C CA  . LEU K 58  ? 0.768 0.836 0.794 -0.017 0.074  -0.071 387 LEU KKK CA  
13184 C C   . LEU K 58  ? 0.773 0.862 0.782 -0.022 0.092  -0.084 387 LEU KKK C   
13185 O O   . LEU K 58  ? 0.750 0.831 0.735 -0.024 0.096  -0.099 387 LEU KKK O   
13186 C CB  . LEU K 58  ? 0.763 0.823 0.767 -0.027 0.060  -0.054 387 LEU KKK CB  
13187 C CG  . LEU K 58  ? 0.747 0.787 0.760 -0.025 0.044  -0.044 387 LEU KKK CG  
13188 C CD1 . LEU K 58  ? 0.781 0.815 0.772 -0.035 0.033  -0.030 387 LEU KKK CD1 
13189 C CD2 . LEU K 58  ? 0.737 0.756 0.748 -0.020 0.041  -0.055 387 LEU KKK CD2 
13190 N N   . ASN K 59  ? 0.776 0.892 0.796 -0.024 0.102  -0.079 388 ASN KKK N   
13191 C CA  . ASN K 59  ? 0.808 0.946 0.808 -0.031 0.120  -0.089 388 ASN KKK CA  
13192 C C   . ASN K 59  ? 0.814 0.961 0.831 -0.020 0.138  -0.115 388 ASN KKK C   
13193 O O   . ASN K 59  ? 0.839 1.005 0.837 -0.025 0.154  -0.127 388 ASN KKK O   
13194 C CB  . ASN K 59  ? 0.818 0.984 0.823 -0.040 0.124  -0.073 388 ASN KKK CB  
13195 C CG  . ASN K 59  ? 0.867 1.026 0.838 -0.054 0.112  -0.055 388 ASN KKK CG  
13196 O OD1 . ASN K 59  ? 0.914 1.055 0.857 -0.058 0.104  -0.057 388 ASN KKK OD1 
13197 N ND2 . ASN K 59  ? 0.884 1.058 0.862 -0.063 0.110  -0.037 388 ASN KKK ND2 
13198 N N   . ASP K 60  ? 0.781 0.912 0.830 -0.006 0.135  -0.123 389 ASP KKK N   
13199 C CA  . ASP K 60  ? 0.802 0.939 0.875 0.007  0.153  -0.148 389 ASP KKK CA  
13200 C C   . ASP K 60  ? 0.794 0.899 0.859 0.012  0.149  -0.166 389 ASP KKK C   
13201 O O   . ASP K 60  ? 0.830 0.933 0.918 0.024  0.161  -0.188 389 ASP KKK O   
13202 C CB  . ASP K 60  ? 0.820 0.966 0.948 0.022  0.154  -0.144 389 ASP KKK CB  
13203 C CG  . ASP K 60  ? 0.879 1.058 1.023 0.017  0.158  -0.126 389 ASP KKK CG  
13204 O OD1 . ASP K 60  ? 0.950 1.157 1.084 0.011  0.176  -0.133 389 ASP KKK OD1 
13205 O OD2 . ASP K 60  ? 0.963 1.139 1.127 0.018  0.142  -0.106 389 ASP KKK OD2 
13206 N N   . LEU K 61  ? 0.764 0.845 0.801 0.004  0.132  -0.158 390 LEU KKK N   
13207 C CA  . LEU K 61  ? 0.771 0.821 0.804 0.008  0.125  -0.172 390 LEU KKK CA  
13208 C C   . LEU K 61  ? 0.774 0.821 0.761 -0.005 0.127  -0.185 390 LEU KKK C   
13209 O O   . LEU K 61  ? 0.775 0.836 0.729 -0.018 0.125  -0.174 390 LEU KKK O   
13210 C CB  . LEU K 61  ? 0.762 0.789 0.804 0.008  0.104  -0.151 390 LEU KKK CB  
13211 C CG  . LEU K 61  ? 0.753 0.781 0.840 0.020  0.098  -0.137 390 LEU KKK CG  
13212 C CD1 . LEU K 61  ? 0.739 0.745 0.825 0.017  0.078  -0.117 390 LEU KKK CD1 
13213 C CD2 . LEU K 61  ? 0.756 0.777 0.881 0.036  0.108  -0.156 390 LEU KKK CD2 
13214 N N   . CYS K 62  ? 0.795 0.822 0.780 -0.002 0.130  -0.208 391 CYS KKK N   
13215 C CA  . CYS K 62  ? 0.809 0.829 0.753 -0.014 0.130  -0.223 391 CYS KKK CA  
13216 C C   . CYS K 62  ? 0.769 0.756 0.714 -0.015 0.112  -0.221 391 CYS KKK C   
13217 O O   . CYS K 62  ? 0.739 0.706 0.719 -0.003 0.109  -0.222 391 CYS KKK O   
13218 C CB  . CYS K 62  ? 0.860 0.887 0.799 -0.011 0.150  -0.257 391 CYS KKK CB  
13219 S SG  . CYS K 62  ? 0.921 0.992 0.848 -0.015 0.172  -0.260 391 CYS KKK SG  
13220 N N   . PHE K 63  ? 0.769 0.752 0.679 -0.028 0.100  -0.216 392 PHE KKK N   
13221 C CA  . PHE K 63  ? 0.786 0.741 0.692 -0.032 0.084  -0.214 392 PHE KKK CA  
13222 C C   . PHE K 63  ? 0.810 0.765 0.679 -0.045 0.083  -0.231 392 PHE KKK C   
13223 O O   . PHE K 63  ? 0.828 0.805 0.668 -0.053 0.091  -0.238 392 PHE KKK O   
13224 C CB  . PHE K 63  ? 0.769 0.724 0.675 -0.036 0.068  -0.183 392 PHE KKK CB  
13225 C CG  . PHE K 63  ? 0.744 0.701 0.685 -0.025 0.067  -0.167 392 PHE KKK CG  
13226 C CD1 . PHE K 63  ? 0.737 0.673 0.711 -0.015 0.064  -0.168 392 PHE KKK CD1 
13227 C CD2 . PHE K 63  ? 0.720 0.697 0.659 -0.025 0.069  -0.150 392 PHE KKK CD2 
13228 C CE1 . PHE K 63  ? 0.719 0.658 0.723 -0.006 0.062  -0.152 392 PHE KKK CE1 
13229 C CE2 . PHE K 63  ? 0.703 0.683 0.674 -0.017 0.067  -0.136 392 PHE KKK CE2 
13230 C CZ  . PHE K 63  ? 0.704 0.666 0.706 -0.007 0.063  -0.136 392 PHE KKK CZ  
13231 N N   . THR K 64  ? 0.830 0.762 0.700 -0.049 0.072  -0.238 393 THR KKK N   
13232 C CA  . THR K 64  ? 0.888 0.816 0.723 -0.063 0.067  -0.254 393 THR KKK CA  
13233 C C   . THR K 64  ? 0.871 0.815 0.679 -0.075 0.053  -0.231 393 THR KKK C   
13234 O O   . THR K 64  ? 0.890 0.849 0.663 -0.087 0.052  -0.238 393 THR KKK O   
13235 C CB  . THR K 64  ? 0.908 0.806 0.757 -0.065 0.057  -0.264 393 THR KKK CB  
13236 O OG1 . THR K 64  ? 0.921 0.799 0.811 -0.050 0.061  -0.266 393 THR KKK OG1 
13237 C CG2 . THR K 64  ? 0.954 0.848 0.778 -0.075 0.060  -0.294 393 THR KKK CG2 
13238 N N   . ASN K 65  ? 0.845 0.787 0.670 -0.071 0.043  -0.205 394 ASN KKK N   
13239 C CA  . ASN K 65  ? 0.824 0.776 0.631 -0.080 0.029  -0.182 394 ASN KKK CA  
13240 C C   . ASN K 65  ? 0.789 0.742 0.620 -0.072 0.026  -0.158 394 ASN KKK C   
13241 O O   . ASN K 65  ? 0.748 0.688 0.608 -0.062 0.029  -0.157 394 ASN KKK O   
13242 C CB  . ASN K 65  ? 0.830 0.770 0.633 -0.088 0.014  -0.182 394 ASN KKK CB  
13243 C CG  . ASN K 65  ? 0.858 0.802 0.631 -0.100 0.013  -0.202 394 ASN KKK CG  
13244 O OD1 . ASN K 65  ? 0.882 0.846 0.626 -0.109 0.012  -0.199 394 ASN KKK OD1 
13245 N ND2 . ASN K 65  ? 0.880 0.805 0.660 -0.102 0.014  -0.224 394 ASN KKK ND2 
13246 N N   . VAL K 66  ? 0.772 0.739 0.590 -0.077 0.019  -0.138 395 VAL KKK N   
13247 C CA  . VAL K 66  ? 0.731 0.696 0.567 -0.072 0.013  -0.116 395 VAL KKK CA  
13248 C C   . VAL K 66  ? 0.729 0.693 0.555 -0.079 -0.002 -0.103 395 VAL KKK C   
13249 O O   . VAL K 66  ? 0.744 0.718 0.548 -0.088 -0.007 -0.105 395 VAL KKK O   
13250 C CB  . VAL K 66  ? 0.723 0.705 0.557 -0.070 0.020  -0.105 395 VAL KKK CB  
13251 C CG1 . VAL K 66  ? 0.732 0.711 0.582 -0.066 0.013  -0.084 395 VAL KKK CG1 
13252 C CG2 . VAL K 66  ? 0.719 0.705 0.567 -0.062 0.035  -0.118 395 VAL KKK CG2 
13253 N N   . TYR K 67  ? 0.704 0.658 0.549 -0.075 -0.009 -0.093 396 TYR KKK N   
13254 C CA  . TYR K 67  ? 0.717 0.672 0.560 -0.080 -0.022 -0.080 396 TYR KKK CA  
13255 C C   . TYR K 67  ? 0.672 0.631 0.524 -0.076 -0.023 -0.062 396 TYR KKK C   
13256 O O   . TYR K 67  ? 0.659 0.612 0.527 -0.069 -0.018 -0.059 396 TYR KKK O   
13257 C CB  . TYR K 67  ? 0.732 0.673 0.587 -0.081 -0.028 -0.083 396 TYR KKK CB  
13258 C CG  . TYR K 67  ? 0.769 0.705 0.617 -0.088 -0.028 -0.102 396 TYR KKK CG  
13259 C CD1 . TYR K 67  ? 0.788 0.734 0.614 -0.097 -0.035 -0.106 396 TYR KKK CD1 
13260 C CD2 . TYR K 67  ? 0.821 0.741 0.679 -0.084 -0.021 -0.116 396 TYR KKK CD2 
13261 C CE1 . TYR K 67  ? 0.858 0.799 0.673 -0.104 -0.035 -0.125 396 TYR KKK CE1 
13262 C CE2 . TYR K 67  ? 0.875 0.788 0.726 -0.090 -0.020 -0.136 396 TYR KKK CE2 
13263 C CZ  . TYR K 67  ? 0.875 0.799 0.703 -0.100 -0.027 -0.142 396 TYR KKK CZ  
13264 O OH  . TYR K 67  ? 0.900 0.816 0.718 -0.107 -0.027 -0.163 396 TYR KKK OH  
13265 N N   . ALA K 68  ? 0.670 0.638 0.512 -0.080 -0.031 -0.051 397 ALA KKK N   
13266 C CA  . ALA K 68  ? 0.664 0.634 0.515 -0.077 -0.033 -0.035 397 ALA KKK CA  
13267 C C   . ALA K 68  ? 0.630 0.598 0.489 -0.077 -0.043 -0.028 397 ALA KKK C   
13268 O O   . ALA K 68  ? 0.600 0.575 0.452 -0.082 -0.051 -0.025 397 ALA KKK O   
13269 C CB  . ALA K 68  ? 0.668 0.650 0.505 -0.080 -0.033 -0.027 397 ALA KKK CB  
13270 N N   . ASP K 69  ? 0.587 0.547 0.462 -0.073 -0.042 -0.027 398 ASP KKK N   
13271 C CA  . ASP K 69  ? 0.581 0.540 0.467 -0.072 -0.047 -0.021 398 ASP KKK CA  
13272 C C   . ASP K 69  ? 0.570 0.530 0.462 -0.069 -0.048 -0.011 398 ASP KKK C   
13273 O O   . ASP K 69  ? 0.562 0.519 0.455 -0.066 -0.043 -0.009 398 ASP KKK O   
13274 C CB  . ASP K 69  ? 0.568 0.519 0.466 -0.072 -0.045 -0.025 398 ASP KKK CB  
13275 C CG  . ASP K 69  ? 0.581 0.527 0.477 -0.076 -0.045 -0.036 398 ASP KKK CG  
13276 O OD1 . ASP K 69  ? 0.602 0.553 0.487 -0.081 -0.049 -0.041 398 ASP KKK OD1 
13277 O OD2 . ASP K 69  ? 0.551 0.487 0.456 -0.075 -0.041 -0.039 398 ASP KKK OD2 
13278 N N   . SER K 70  ? 0.581 0.545 0.478 -0.068 -0.054 -0.004 399 SER KKK N   
13279 C CA  . SER K 70  ? 0.581 0.543 0.484 -0.064 -0.055 0.004  399 SER KKK CA  
13280 C C   . SER K 70  ? 0.554 0.519 0.473 -0.062 -0.058 0.005  399 SER KKK C   
13281 O O   . SER K 70  ? 0.547 0.519 0.471 -0.063 -0.063 0.004  399 SER KKK O   
13282 C CB  . SER K 70  ? 0.625 0.591 0.520 -0.066 -0.058 0.012  399 SER KKK CB  
13283 O OG  . SER K 70  ? 0.669 0.643 0.560 -0.069 -0.067 0.015  399 SER KKK OG  
13284 N N   . PHE K 71  ? 0.523 0.483 0.450 -0.058 -0.055 0.007  400 PHE KKK N   
13285 C CA  . PHE K 71  ? 0.529 0.491 0.472 -0.054 -0.055 0.005  400 PHE KKK CA  
13286 C C   . PHE K 71  ? 0.548 0.501 0.494 -0.050 -0.051 0.005  400 PHE KKK C   
13287 O O   . PHE K 71  ? 0.534 0.482 0.471 -0.052 -0.049 0.006  400 PHE KKK O   
13288 C CB  . PHE K 71  ? 0.535 0.501 0.482 -0.056 -0.050 -0.001 400 PHE KKK CB  
13289 C CG  . PHE K 71  ? 0.542 0.502 0.479 -0.059 -0.045 -0.004 400 PHE KKK CG  
13290 C CD1 . PHE K 71  ? 0.558 0.513 0.493 -0.058 -0.040 -0.005 400 PHE KKK CD1 
13291 C CD2 . PHE K 71  ? 0.574 0.532 0.503 -0.062 -0.045 -0.006 400 PHE KKK CD2 
13292 C CE1 . PHE K 71  ? 0.570 0.521 0.498 -0.060 -0.037 -0.005 400 PHE KKK CE1 
13293 C CE2 . PHE K 71  ? 0.573 0.524 0.497 -0.063 -0.041 -0.007 400 PHE KKK CE2 
13294 C CZ  . PHE K 71  ? 0.567 0.515 0.491 -0.062 -0.037 -0.005 400 PHE KKK CZ  
13295 N N   . VAL K 72  ? 0.556 0.512 0.517 -0.046 -0.049 0.001  401 VAL KKK N   
13296 C CA  . VAL K 72  ? 0.565 0.512 0.529 -0.043 -0.045 -0.004 401 VAL KKK CA  
13297 C C   . VAL K 72  ? 0.559 0.511 0.523 -0.045 -0.036 -0.012 401 VAL KKK C   
13298 O O   . VAL K 72  ? 0.544 0.507 0.516 -0.044 -0.034 -0.014 401 VAL KKK O   
13299 C CB  . VAL K 72  ? 0.578 0.522 0.561 -0.037 -0.048 -0.002 401 VAL KKK CB  
13300 C CG1 . VAL K 72  ? 0.598 0.534 0.586 -0.034 -0.042 -0.011 401 VAL KKK CG1 
13301 C CG2 . VAL K 72  ? 0.598 0.536 0.578 -0.038 -0.057 0.009  401 VAL KKK CG2 
13302 N N   . ILE K 73  ? 0.574 0.520 0.527 -0.047 -0.032 -0.016 402 ILE KKK N   
13303 C CA  . ILE K 73  ? 0.603 0.552 0.550 -0.050 -0.024 -0.024 402 ILE KKK CA  
13304 C C   . ILE K 73  ? 0.608 0.549 0.551 -0.050 -0.022 -0.030 402 ILE KKK C   
13305 O O   . ILE K 73  ? 0.592 0.523 0.539 -0.048 -0.027 -0.028 402 ILE KKK O   
13306 C CB  . ILE K 73  ? 0.612 0.565 0.547 -0.056 -0.024 -0.019 402 ILE KKK CB  
13307 C CG1 . ILE K 73  ? 0.624 0.569 0.548 -0.058 -0.028 -0.014 402 ILE KKK CG1 
13308 C CG2 . ILE K 73  ? 0.601 0.561 0.542 -0.057 -0.024 -0.016 402 ILE KKK CG2 
13309 C CD1 . ILE K 73  ? 0.634 0.580 0.549 -0.063 -0.028 -0.010 402 ILE KKK CD1 
13310 N N   . ARG K 74  ? 0.633 0.578 0.569 -0.053 -0.015 -0.039 403 ARG KKK N   
13311 C CA  . ARG K 74  ? 0.646 0.583 0.572 -0.056 -0.013 -0.048 403 ARG KKK CA  
13312 C C   . ARG K 74  ? 0.640 0.573 0.550 -0.062 -0.020 -0.040 403 ARG KKK C   
13313 O O   . ARG K 74  ? 0.633 0.571 0.537 -0.065 -0.021 -0.032 403 ARG KKK O   
13314 C CB  . ARG K 74  ? 0.722 0.669 0.637 -0.060 -0.004 -0.058 403 ARG KKK CB  
13315 C CG  . ARG K 74  ? 0.797 0.750 0.729 -0.053 0.005  -0.070 403 ARG KKK CG  
13316 C CD  . ARG K 74  ? 0.866 0.835 0.786 -0.059 0.016  -0.076 403 ARG KKK CD  
13317 N NE  . ARG K 74  ? 0.952 0.919 0.847 -0.068 0.018  -0.081 403 ARG KKK NE  
13318 C CZ  . ARG K 74  ? 1.030 1.010 0.906 -0.076 0.025  -0.085 403 ARG KKK CZ  
13319 N NH1 . ARG K 74  ? 1.096 1.092 0.978 -0.078 0.033  -0.082 403 ARG KKK NH1 
13320 N NH2 . ARG K 74  ? 1.045 1.023 0.897 -0.085 0.024  -0.089 403 ARG KKK NH2 
13321 N N   . GLY K 75  ? 0.648 0.571 0.554 -0.065 -0.022 -0.045 404 GLY KKK N   
13322 C CA  . GLY K 75  ? 0.666 0.587 0.560 -0.072 -0.029 -0.039 404 GLY KKK CA  
13323 C C   . GLY K 75  ? 0.677 0.608 0.555 -0.078 -0.028 -0.035 404 GLY KKK C   
13324 O O   . GLY K 75  ? 0.650 0.584 0.528 -0.079 -0.033 -0.024 404 GLY KKK O   
13325 N N   . ASP K 76  ? 0.676 0.614 0.544 -0.081 -0.022 -0.043 405 ASP KKK N   
13326 C CA  . ASP K 76  ? 0.737 0.684 0.588 -0.090 -0.023 -0.037 405 ASP KKK CA  
13327 C C   . ASP K 76  ? 0.687 0.641 0.543 -0.088 -0.021 -0.027 405 ASP KKK C   
13328 O O   . ASP K 76  ? 0.698 0.659 0.543 -0.094 -0.022 -0.018 405 ASP KKK O   
13329 C CB  . ASP K 76  ? 0.812 0.764 0.643 -0.098 -0.019 -0.048 405 ASP KKK CB  
13330 C CG  . ASP K 76  ? 0.896 0.852 0.729 -0.094 -0.006 -0.063 405 ASP KKK CG  
13331 O OD1 . ASP K 76  ? 0.927 0.886 0.776 -0.088 -0.001 -0.061 405 ASP KKK OD1 
13332 O OD2 . ASP K 76  ? 1.028 0.984 0.848 -0.099 -0.002 -0.077 405 ASP KKK OD2 
13333 N N   . GLU K 77  ? 0.677 0.629 0.549 -0.081 -0.019 -0.026 406 GLU KKK N   
13334 C CA  . GLU K 77  ? 0.651 0.608 0.530 -0.080 -0.018 -0.017 406 GLU KKK CA  
13335 C C   . GLU K 77  ? 0.644 0.594 0.529 -0.077 -0.026 -0.008 406 GLU KKK C   
13336 O O   . GLU K 77  ? 0.610 0.561 0.500 -0.077 -0.027 -0.002 406 GLU KKK O   
13337 C CB  . GLU K 77  ? 0.681 0.643 0.574 -0.075 -0.013 -0.022 406 GLU KKK CB  
13338 C CG  . GLU K 77  ? 0.713 0.685 0.604 -0.077 -0.003 -0.031 406 GLU KKK CG  
13339 C CD  . GLU K 77  ? 0.720 0.699 0.631 -0.071 0.002  -0.037 406 GLU KKK CD  
13340 O OE1 . GLU K 77  ? 0.644 0.617 0.569 -0.064 -0.003 -0.036 406 GLU KKK OE1 
13341 O OE2 . GLU K 77  ? 0.748 0.740 0.662 -0.073 0.012  -0.042 406 GLU KKK OE2 
13342 N N   . VAL K 78  ? 0.628 0.572 0.515 -0.075 -0.030 -0.008 407 VAL KKK N   
13343 C CA  . VAL K 78  ? 0.618 0.559 0.512 -0.072 -0.035 -0.002 407 VAL KKK CA  
13344 C C   . VAL K 78  ? 0.596 0.539 0.488 -0.075 -0.038 0.007  407 VAL KKK C   
13345 O O   . VAL K 78  ? 0.573 0.514 0.473 -0.072 -0.039 0.010  407 VAL KKK O   
13346 C CB  . VAL K 78  ? 0.611 0.548 0.508 -0.072 -0.038 -0.002 407 VAL KKK CB  
13347 C CG1 . VAL K 78  ? 0.595 0.533 0.499 -0.070 -0.041 0.004  407 VAL KKK CG1 
13348 C CG2 . VAL K 78  ? 0.609 0.541 0.511 -0.068 -0.037 -0.008 407 VAL KKK CG2 
13349 N N   . ARG K 79  ? 0.607 0.553 0.490 -0.081 -0.041 0.010  408 ARG KKK N   
13350 C CA  . ARG K 79  ? 0.642 0.590 0.525 -0.084 -0.045 0.022  408 ARG KKK CA  
13351 C C   . ARG K 79  ? 0.636 0.582 0.524 -0.083 -0.042 0.025  408 ARG KKK C   
13352 O O   . ARG K 79  ? 0.665 0.608 0.560 -0.083 -0.047 0.034  408 ARG KKK O   
13353 C CB  . ARG K 79  ? 0.701 0.655 0.568 -0.092 -0.049 0.025  408 ARG KKK CB  
13354 C CG  . ARG K 79  ? 0.765 0.723 0.618 -0.098 -0.042 0.021  408 ARG KKK CG  
13355 C CD  . ARG K 79  ? 0.833 0.799 0.667 -0.107 -0.045 0.024  408 ARG KKK CD  
13356 N NE  . ARG K 79  ? 0.868 0.833 0.696 -0.107 -0.043 0.010  408 ARG KKK NE  
13357 C CZ  . ARG K 79  ? 0.937 0.906 0.748 -0.115 -0.046 0.005  408 ARG KKK CZ  
13358 N NH1 . ARG K 79  ? 0.949 0.927 0.742 -0.125 -0.051 0.013  408 ARG KKK NH1 
13359 N NH2 . ARG K 79  ? 0.928 0.891 0.738 -0.114 -0.044 -0.010 408 ARG KKK NH2 
13360 N N   . GLN K 80  ? 0.624 0.571 0.511 -0.083 -0.036 0.019  409 GLN KKK N   
13361 C CA  . GLN K 80  ? 0.623 0.570 0.517 -0.085 -0.034 0.022  409 GLN KKK CA  
13362 C C   . GLN K 80  ? 0.605 0.545 0.512 -0.079 -0.035 0.020  409 GLN KKK C   
13363 O O   . GLN K 80  ? 0.604 0.540 0.518 -0.080 -0.035 0.023  409 GLN KKK O   
13364 C CB  . GLN K 80  ? 0.635 0.589 0.526 -0.087 -0.026 0.016  409 GLN KKK CB  
13365 C CG  . GLN K 80  ? 0.650 0.613 0.527 -0.095 -0.023 0.018  409 GLN KKK CG  
13366 C CD  . GLN K 80  ? 0.655 0.629 0.534 -0.097 -0.014 0.011  409 GLN KKK CD  
13367 O OE1 . GLN K 80  ? 0.655 0.631 0.545 -0.098 -0.012 0.013  409 GLN KKK OE1 
13368 N NE2 . GLN K 80  ? 0.648 0.630 0.517 -0.099 -0.008 0.002  409 GLN KKK NE2 
13369 N N   . ILE K 81  ? 0.570 0.508 0.480 -0.073 -0.036 0.015  410 ILE KKK N   
13370 C CA  . ILE K 81  ? 0.576 0.510 0.495 -0.069 -0.036 0.012  410 ILE KKK CA  
13371 C C   . ILE K 81  ? 0.577 0.506 0.502 -0.066 -0.039 0.016  410 ILE KKK C   
13372 O O   . ILE K 81  ? 0.550 0.481 0.478 -0.062 -0.039 0.015  410 ILE KKK O   
13373 C CB  . ILE K 81  ? 0.589 0.525 0.506 -0.065 -0.035 0.006  410 ILE KKK CB  
13374 C CG1 . ILE K 81  ? 0.576 0.517 0.491 -0.066 -0.033 0.002  410 ILE KKK CG1 
13375 C CG2 . ILE K 81  ? 0.584 0.519 0.505 -0.063 -0.034 0.002  410 ILE KKK CG2 
13376 C CD1 . ILE K 81  ? 0.553 0.497 0.471 -0.069 -0.031 0.001  410 ILE KKK CD1 
13377 N N   . ALA K 82  ? 0.602 0.526 0.533 -0.068 -0.040 0.022  411 ALA KKK N   
13378 C CA  . ALA K 82  ? 0.613 0.532 0.555 -0.065 -0.044 0.029  411 ALA KKK CA  
13379 C C   . ALA K 82  ? 0.612 0.521 0.562 -0.068 -0.046 0.034  411 ALA KKK C   
13380 O O   . ALA K 82  ? 0.653 0.564 0.595 -0.075 -0.046 0.038  411 ALA KKK O   
13381 C CB  . ALA K 82  ? 0.596 0.522 0.535 -0.067 -0.049 0.037  411 ALA KKK CB  
13382 N N   . PRO K 83  ? 0.616 0.515 0.582 -0.063 -0.048 0.035  412 PRO KKK N   
13383 C CA  . PRO K 83  ? 0.617 0.503 0.593 -0.066 -0.051 0.042  412 PRO KKK CA  
13384 C C   . PRO K 83  ? 0.624 0.513 0.594 -0.073 -0.057 0.060  412 PRO KKK C   
13385 O O   . PRO K 83  ? 0.624 0.522 0.592 -0.071 -0.061 0.066  412 PRO KKK O   
13386 C CB  . PRO K 83  ? 0.640 0.516 0.637 -0.057 -0.052 0.039  412 PRO KKK CB  
13387 C CG  . PRO K 83  ? 0.625 0.513 0.622 -0.051 -0.050 0.036  412 PRO KKK CG  
13388 C CD  . PRO K 83  ? 0.611 0.510 0.588 -0.054 -0.046 0.028  412 PRO KKK CD  
13389 N N   . GLY K 84  ? 0.631 0.517 0.599 -0.082 -0.058 0.067  413 GLY KKK N   
13390 C CA  . GLY K 84  ? 0.625 0.512 0.587 -0.090 -0.064 0.086  413 GLY KKK CA  
13391 C C   . GLY K 84  ? 0.633 0.537 0.571 -0.098 -0.060 0.087  413 GLY KKK C   
13392 O O   . GLY K 84  ? 0.714 0.623 0.643 -0.106 -0.065 0.102  413 GLY KKK O   
13393 N N   . GLN K 85  ? 0.626 0.539 0.555 -0.096 -0.053 0.072  414 GLN KKK N   
13394 C CA  . GLN K 85  ? 0.617 0.545 0.526 -0.102 -0.048 0.069  414 GLN KKK CA  
13395 C C   . GLN K 85  ? 0.630 0.564 0.534 -0.110 -0.042 0.069  414 GLN KKK C   
13396 O O   . GLN K 85  ? 0.660 0.586 0.577 -0.110 -0.040 0.066  414 GLN KKK O   
13397 C CB  . GLN K 85  ? 0.596 0.528 0.502 -0.094 -0.044 0.053  414 GLN KKK CB  
13398 C CG  . GLN K 85  ? 0.605 0.537 0.513 -0.089 -0.049 0.054  414 GLN KKK CG  
13399 C CD  . GLN K 85  ? 0.613 0.554 0.507 -0.095 -0.054 0.062  414 GLN KKK CD  
13400 O OE1 . GLN K 85  ? 0.649 0.598 0.526 -0.102 -0.050 0.059  414 GLN KKK OE1 
13401 N NE2 . GLN K 85  ? 0.622 0.561 0.521 -0.094 -0.062 0.071  414 GLN KKK NE2 
13402 N N   . THR K 86  ? 0.636 0.583 0.523 -0.118 -0.037 0.071  415 THR KKK N   
13403 C CA  . THR K 86  ? 0.636 0.595 0.518 -0.125 -0.028 0.068  415 THR KKK CA  
13404 C C   . THR K 86  ? 0.625 0.599 0.496 -0.123 -0.020 0.054  415 THR KKK C   
13405 O O   . THR K 86  ? 0.649 0.621 0.511 -0.119 -0.023 0.049  415 THR KKK O   
13406 C CB  . THR K 86  ? 0.655 0.620 0.529 -0.139 -0.028 0.085  415 THR KKK CB  
13407 O OG1 . THR K 86  ? 0.645 0.615 0.500 -0.143 -0.032 0.092  415 THR KKK OG1 
13408 C CG2 . THR K 86  ? 0.675 0.623 0.566 -0.141 -0.035 0.098  415 THR KKK CG2 
13409 N N   . GLY K 87  ? 0.590 0.576 0.464 -0.126 -0.010 0.046  416 GLY KKK N   
13410 C CA  . GLY K 87  ? 0.591 0.589 0.461 -0.122 -0.001 0.031  416 GLY KKK CA  
13411 C C   . GLY K 87  ? 0.592 0.594 0.482 -0.117 0.003  0.022  416 GLY KKK C   
13412 O O   . GLY K 87  ? 0.574 0.569 0.478 -0.117 -0.002 0.027  416 GLY KKK O   
13413 N N   . LYS K 88  ? 0.620 0.634 0.513 -0.113 0.012  0.009  417 LYS KKK N   
13414 C CA  . LYS K 88  ? 0.611 0.634 0.527 -0.108 0.016  0.002  417 LYS KKK CA  
13415 C C   . LYS K 88  ? 0.567 0.575 0.494 -0.101 0.005  0.002  417 LYS KKK C   
13416 O O   . LYS K 88  ? 0.568 0.579 0.510 -0.102 0.003  0.004  417 LYS KKK O   
13417 C CB  . LYS K 88  ? 0.652 0.685 0.573 -0.100 0.024  -0.013 417 LYS KKK CB  
13418 C CG  . LYS K 88  ? 0.719 0.768 0.628 -0.107 0.037  -0.019 417 LYS KKK CG  
13419 C CD  . LYS K 88  ? 0.752 0.820 0.665 -0.117 0.045  -0.012 417 LYS KKK CD  
13420 C CE  . LYS K 88  ? 0.780 0.847 0.671 -0.131 0.044  0.003  417 LYS KKK CE  
13421 N NZ  . LYS K 88  ? 0.776 0.864 0.672 -0.142 0.054  0.009  417 LYS KKK NZ  
13422 N N   . ILE K 89  ? 0.538 0.533 0.458 -0.095 -0.001 0.001  418 ILE KKK N   
13423 C CA  . ILE K 89  ? 0.550 0.534 0.478 -0.088 -0.009 -0.000 418 ILE KKK CA  
13424 C C   . ILE K 89  ? 0.550 0.524 0.480 -0.091 -0.015 0.008  418 ILE KKK C   
13425 O O   . ILE K 89  ? 0.526 0.500 0.467 -0.092 -0.018 0.006  418 ILE KKK O   
13426 C CB  . ILE K 89  ? 0.560 0.535 0.481 -0.081 -0.012 -0.004 418 ILE KKK CB  
13427 C CG1 . ILE K 89  ? 0.568 0.550 0.490 -0.077 -0.007 -0.014 418 ILE KKK CG1 
13428 C CG2 . ILE K 89  ? 0.543 0.511 0.471 -0.075 -0.019 -0.005 418 ILE KKK CG2 
13429 C CD1 . ILE K 89  ? 0.593 0.585 0.533 -0.073 -0.003 -0.019 418 ILE KKK CD1 
13430 N N   . ALA K 90  ? 0.566 0.532 0.486 -0.095 -0.018 0.015  419 ALA KKK N   
13431 C CA  . ALA K 90  ? 0.596 0.549 0.520 -0.098 -0.023 0.023  419 ALA KKK CA  
13432 C C   . ALA K 90  ? 0.612 0.569 0.547 -0.106 -0.021 0.026  419 ALA KKK C   
13433 O O   . ALA K 90  ? 0.634 0.581 0.578 -0.106 -0.026 0.026  419 ALA KKK O   
13434 C CB  . ALA K 90  ? 0.580 0.527 0.495 -0.100 -0.026 0.033  419 ALA KKK CB  
13435 N N   . ASP K 91  ? 0.615 0.587 0.548 -0.112 -0.015 0.029  420 ASP KKK N   
13436 C CA  . ASP K 91  ? 0.628 0.605 0.570 -0.123 -0.012 0.035  420 ASP KKK CA  
13437 C C   . ASP K 91  ? 0.614 0.601 0.573 -0.121 -0.011 0.026  420 ASP KKK C   
13438 O O   . ASP K 91  ? 0.644 0.628 0.614 -0.128 -0.014 0.029  420 ASP KKK O   
13439 C CB  . ASP K 91  ? 0.674 0.666 0.607 -0.132 -0.004 0.043  420 ASP KKK CB  
13440 C CG  . ASP K 91  ? 0.698 0.682 0.613 -0.137 -0.007 0.055  420 ASP KKK CG  
13441 O OD1 . ASP K 91  ? 0.663 0.629 0.580 -0.133 -0.017 0.060  420 ASP KKK OD1 
13442 O OD2 . ASP K 91  ? 0.704 0.703 0.605 -0.144 -0.000 0.059  420 ASP KKK OD2 
13443 N N   . TYR K 92  ? 0.574 0.574 0.535 -0.114 -0.007 0.017  421 TYR KKK N   
13444 C CA  . TYR K 92  ? 0.564 0.581 0.544 -0.114 -0.005 0.011  421 TYR KKK CA  
13445 C C   . TYR K 92  ? 0.555 0.568 0.541 -0.104 -0.012 0.003  421 TYR KKK C   
13446 O O   . TYR K 92  ? 0.570 0.596 0.573 -0.104 -0.014 0.000  421 TYR KKK O   
13447 C CB  . TYR K 92  ? 0.567 0.605 0.549 -0.114 0.007  0.008  421 TYR KKK CB  
13448 C CG  . TYR K 92  ? 0.578 0.626 0.554 -0.126 0.015  0.016  421 TYR KKK CG  
13449 C CD1 . TYR K 92  ? 0.576 0.617 0.552 -0.137 0.012  0.028  421 TYR KKK CD1 
13450 C CD2 . TYR K 92  ? 0.603 0.669 0.575 -0.126 0.028  0.011  421 TYR KKK CD2 
13451 C CE1 . TYR K 92  ? 0.599 0.650 0.568 -0.149 0.020  0.037  421 TYR KKK CE1 
13452 C CE2 . TYR K 92  ? 0.607 0.687 0.572 -0.138 0.037  0.018  421 TYR KKK CE2 
13453 C CZ  . TYR K 92  ? 0.618 0.691 0.581 -0.151 0.033  0.033  421 TYR KKK CZ  
13454 O OH  . TYR K 92  ? 0.628 0.716 0.582 -0.164 0.042  0.043  421 TYR KKK OH  
13455 N N   . ASN K 93  ? 0.566 0.564 0.539 -0.097 -0.016 0.001  422 ASN KKK N   
13456 C CA  . ASN K 93  ? 0.566 0.563 0.542 -0.088 -0.022 -0.004 422 ASN KKK CA  
13457 C C   . ASN K 93  ? 0.581 0.562 0.549 -0.088 -0.030 -0.005 422 ASN KKK C   
13458 O O   . ASN K 93  ? 0.572 0.555 0.545 -0.088 -0.036 -0.008 422 ASN KKK O   
13459 C CB  . ASN K 93  ? 0.566 0.565 0.537 -0.081 -0.018 -0.008 422 ASN KKK CB  
13460 C CG  . ASN K 93  ? 0.558 0.574 0.542 -0.079 -0.010 -0.011 422 ASN KKK CG  
13461 O OD1 . ASN K 93  ? 0.520 0.545 0.521 -0.074 -0.012 -0.015 422 ASN KKK OD1 
13462 N ND2 . ASN K 93  ? 0.552 0.574 0.530 -0.085 -0.002 -0.011 422 ASN KKK ND2 
13463 N N   . TYR K 94  ? 0.573 0.541 0.528 -0.087 -0.029 -0.002 423 TYR KKK N   
13464 C CA  . TYR K 94  ? 0.585 0.539 0.534 -0.084 -0.034 -0.004 423 TYR KKK CA  
13465 C C   . TYR K 94  ? 0.583 0.526 0.529 -0.086 -0.033 0.001  423 TYR KKK C   
13466 O O   . TYR K 94  ? 0.612 0.555 0.551 -0.084 -0.031 0.005  423 TYR KKK O   
13467 C CB  . TYR K 94  ? 0.574 0.529 0.517 -0.077 -0.035 -0.007 423 TYR KKK CB  
13468 C CG  . TYR K 94  ? 0.567 0.512 0.503 -0.075 -0.038 -0.010 423 TYR KKK CG  
13469 C CD1 . TYR K 94  ? 0.563 0.510 0.498 -0.076 -0.042 -0.015 423 TYR KKK CD1 
13470 C CD2 . TYR K 94  ? 0.570 0.507 0.502 -0.072 -0.036 -0.008 423 TYR KKK CD2 
13471 C CE1 . TYR K 94  ? 0.560 0.501 0.488 -0.075 -0.042 -0.020 423 TYR KKK CE1 
13472 C CE2 . TYR K 94  ? 0.573 0.504 0.501 -0.070 -0.037 -0.012 423 TYR KKK CE2 
13473 C CZ  . TYR K 94  ? 0.558 0.491 0.484 -0.071 -0.039 -0.019 423 TYR KKK CZ  
13474 O OH  . TYR K 94  ? 0.550 0.479 0.471 -0.069 -0.037 -0.025 423 TYR KKK OH  
13475 N N   . LYS K 95  ? 0.602 0.535 0.553 -0.090 -0.036 0.000  424 LYS KKK N   
13476 C CA  . LYS K 95  ? 0.634 0.553 0.586 -0.092 -0.036 0.007  424 LYS KKK CA  
13477 C C   . LYS K 95  ? 0.638 0.545 0.592 -0.086 -0.038 0.001  424 LYS KKK C   
13478 O O   . LYS K 95  ? 0.743 0.644 0.699 -0.087 -0.040 -0.008 424 LYS KKK O   
13479 C CB  . LYS K 95  ? 0.669 0.585 0.630 -0.102 -0.037 0.012  424 LYS KKK CB  
13480 C CG  . LYS K 95  ? 0.714 0.615 0.682 -0.104 -0.039 0.021  424 LYS KKK CG  
13481 C CD  . LYS K 95  ? 0.765 0.671 0.730 -0.112 -0.038 0.037  424 LYS KKK CD  
13482 C CE  . LYS K 95  ? 0.847 0.742 0.809 -0.109 -0.041 0.047  424 LYS KKK CE  
13483 N NZ  . LYS K 95  ? 0.882 0.792 0.830 -0.112 -0.039 0.056  424 LYS KKK NZ  
13484 N N   . LEU K 96  ? 0.611 0.513 0.564 -0.081 -0.038 0.006  425 LEU KKK N   
13485 C CA  . LEU K 96  ? 0.596 0.486 0.555 -0.075 -0.039 0.001  425 LEU KKK CA  
13486 C C   . LEU K 96  ? 0.618 0.492 0.590 -0.077 -0.042 0.007  425 LEU KKK C   
13487 O O   . LEU K 96  ? 0.576 0.450 0.549 -0.082 -0.044 0.020  425 LEU KKK O   
13488 C CB  . LEU K 96  ? 0.573 0.468 0.530 -0.068 -0.038 0.003  425 LEU KKK CB  
13489 C CG  . LEU K 96  ? 0.565 0.472 0.511 -0.065 -0.036 -0.003 425 LEU KKK CG  
13490 C CD1 . LEU K 96  ? 0.589 0.500 0.533 -0.060 -0.035 0.001  425 LEU KKK CD1 
13491 C CD2 . LEU K 96  ? 0.581 0.486 0.525 -0.064 -0.034 -0.015 425 LEU KKK CD2 
13492 N N   . PRO K 97  ? 0.638 0.498 0.621 -0.075 -0.042 -0.003 426 PRO KKK N   
13493 C CA  . PRO K 97  ? 0.643 0.485 0.643 -0.076 -0.045 0.003  426 PRO KKK CA  
13494 C C   . PRO K 97  ? 0.672 0.512 0.682 -0.069 -0.047 0.015  426 PRO KKK C   
13495 O O   . PRO K 97  ? 0.725 0.576 0.729 -0.062 -0.045 0.013  426 PRO KKK O   
13496 C CB  . PRO K 97  ? 0.657 0.486 0.665 -0.072 -0.043 -0.016 426 PRO KKK CB  
13497 C CG  . PRO K 97  ? 0.657 0.500 0.651 -0.066 -0.038 -0.027 426 PRO KKK CG  
13498 C CD  . PRO K 97  ? 0.633 0.495 0.611 -0.070 -0.038 -0.019 426 PRO KKK CD  
13499 N N   . ASP K 98  ? 0.703 0.528 0.727 -0.071 -0.053 0.027  427 ASP KKK N   
13500 C CA  . ASP K 98  ? 0.738 0.562 0.773 -0.065 -0.058 0.042  427 ASP KKK CA  
13501 C C   . ASP K 98  ? 0.730 0.550 0.781 -0.052 -0.055 0.031  427 ASP KKK C   
13502 O O   . ASP K 98  ? 0.724 0.553 0.780 -0.046 -0.057 0.039  427 ASP KKK O   
13503 C CB  . ASP K 98  ? 0.785 0.594 0.833 -0.071 -0.065 0.060  427 ASP KKK CB  
13504 C CG  . ASP K 98  ? 0.859 0.673 0.911 -0.069 -0.073 0.081  427 ASP KKK CG  
13505 O OD1 . ASP K 98  ? 0.938 0.773 0.970 -0.072 -0.072 0.086  427 ASP KKK OD1 
13506 O OD2 . ASP K 98  ? 0.914 0.713 0.990 -0.064 -0.079 0.090  427 ASP KKK OD2 
13507 N N   . ASP K 99  ? 0.710 0.518 0.770 -0.048 -0.050 0.012  428 ASP KKK N   
13508 C CA  . ASP K 99  ? 0.713 0.518 0.790 -0.035 -0.044 -0.002 428 ASP KKK CA  
13509 C C   . ASP K 99  ? 0.693 0.514 0.751 -0.034 -0.036 -0.019 428 ASP KKK C   
13510 O O   . ASP K 99  ? 0.701 0.520 0.766 -0.027 -0.028 -0.037 428 ASP KKK O   
13511 C CB  . ASP K 99  ? 0.749 0.527 0.848 -0.033 -0.044 -0.012 428 ASP KKK CB  
13512 C CG  . ASP K 99  ? 0.784 0.554 0.870 -0.041 -0.041 -0.029 428 ASP KKK CG  
13513 O OD1 . ASP K 99  ? 0.805 0.591 0.866 -0.049 -0.040 -0.031 428 ASP KKK OD1 
13514 O OD2 . ASP K 99  ? 0.841 0.587 0.944 -0.041 -0.042 -0.039 428 ASP KKK OD2 
13515 N N   . PHE K 100 ? 0.648 0.487 0.683 -0.040 -0.036 -0.014 429 PHE KKK N   
13516 C CA  . PHE K 100 ? 0.633 0.487 0.649 -0.040 -0.029 -0.025 429 PHE KKK CA  
13517 C C   . PHE K 100 ? 0.628 0.490 0.656 -0.029 -0.023 -0.032 429 PHE KKK C   
13518 O O   . PHE K 100 ? 0.607 0.474 0.651 -0.024 -0.026 -0.021 429 PHE KKK O   
13519 C CB  . PHE K 100 ? 0.626 0.496 0.625 -0.045 -0.032 -0.014 429 PHE KKK CB  
13520 C CG  . PHE K 100 ? 0.593 0.479 0.576 -0.045 -0.028 -0.021 429 PHE KKK CG  
13521 C CD1 . PHE K 100 ? 0.597 0.484 0.568 -0.048 -0.024 -0.034 429 PHE KKK CD1 
13522 C CD2 . PHE K 100 ? 0.588 0.488 0.568 -0.043 -0.027 -0.014 429 PHE KKK CD2 
13523 C CE1 . PHE K 100 ? 0.602 0.503 0.558 -0.049 -0.022 -0.038 429 PHE KKK CE1 
13524 C CE2 . PHE K 100 ? 0.603 0.515 0.569 -0.043 -0.024 -0.019 429 PHE KKK CE2 
13525 C CZ  . PHE K 100 ? 0.591 0.503 0.545 -0.046 -0.021 -0.030 429 PHE KKK CZ  
13526 N N   . THR K 101 ? 0.622 0.489 0.642 -0.028 -0.015 -0.050 430 THR KKK N   
13527 C CA  . THR K 101 ? 0.627 0.508 0.651 -0.020 -0.006 -0.057 430 THR KKK CA  
13528 C C   . THR K 101 ? 0.609 0.508 0.607 -0.026 -0.003 -0.059 430 THR KKK C   
13529 O O   . THR K 101 ? 0.614 0.511 0.594 -0.032 -0.002 -0.070 430 THR KKK O   
13530 C CB  . THR K 101 ? 0.653 0.526 0.691 -0.014 0.003  -0.078 430 THR KKK CB  
13531 O OG1 . THR K 101 ? 0.663 0.516 0.729 -0.008 -0.002 -0.073 430 THR KKK OG1 
13532 C CG2 . THR K 101 ? 0.645 0.536 0.691 -0.006 0.014  -0.086 430 THR KKK CG2 
13533 N N   . GLY K 102 ? 0.605 0.520 0.603 -0.026 -0.004 -0.048 431 GLY KKK N   
13534 C CA  . GLY K 102 ? 0.597 0.526 0.572 -0.031 -0.002 -0.047 431 GLY KKK CA  
13535 C C   . GLY K 102 ? 0.584 0.523 0.560 -0.032 -0.007 -0.032 431 GLY KKK C   
13536 O O   . GLY K 102 ? 0.580 0.519 0.574 -0.028 -0.010 -0.023 431 GLY KKK O   
13537 N N   . CYS K 103 ? 0.599 0.546 0.557 -0.038 -0.008 -0.028 432 CYS KKK N   
13538 C CA  . CYS K 103 ? 0.567 0.522 0.525 -0.041 -0.012 -0.016 432 CYS KKK CA  
13539 C C   . CYS K 103 ? 0.553 0.504 0.495 -0.046 -0.018 -0.012 432 CYS KKK C   
13540 O O   . CYS K 103 ? 0.596 0.544 0.526 -0.049 -0.018 -0.017 432 CYS KKK O   
13541 C CB  . CYS K 103 ? 0.589 0.559 0.547 -0.041 -0.005 -0.016 432 CYS KKK CB  
13542 S SG  . CYS K 103 ? 0.628 0.607 0.607 -0.033 0.005  -0.025 432 CYS KKK SG  
13543 N N   . VAL K 104 ? 0.547 0.499 0.491 -0.048 -0.023 -0.003 433 VAL KKK N   
13544 C CA  . VAL K 104 ? 0.555 0.503 0.487 -0.053 -0.028 0.001  433 VAL KKK CA  
13545 C C   . VAL K 104 ? 0.564 0.518 0.495 -0.055 -0.029 0.006  433 VAL KKK C   
13546 O O   . VAL K 104 ? 0.547 0.505 0.487 -0.055 -0.030 0.011  433 VAL KKK O   
13547 C CB  . VAL K 104 ? 0.536 0.477 0.470 -0.054 -0.032 0.005  433 VAL KKK CB  
13548 C CG1 . VAL K 104 ? 0.534 0.474 0.459 -0.057 -0.035 0.006  433 VAL KKK CG1 
13549 C CG2 . VAL K 104 ? 0.559 0.493 0.498 -0.052 -0.031 0.001  433 VAL KKK CG2 
13550 N N   . ILE K 105 ? 0.563 0.517 0.485 -0.058 -0.029 0.006  434 ILE KKK N   
13551 C CA  . ILE K 105 ? 0.599 0.556 0.520 -0.061 -0.031 0.012  434 ILE KKK CA  
13552 C C   . ILE K 105 ? 0.582 0.531 0.498 -0.062 -0.035 0.013  434 ILE KKK C   
13553 O O   . ILE K 105 ? 0.579 0.526 0.491 -0.061 -0.036 0.010  434 ILE KKK O   
13554 C CB  . ILE K 105 ? 0.611 0.577 0.529 -0.063 -0.027 0.014  434 ILE KKK CB  
13555 C CG1 . ILE K 105 ? 0.633 0.608 0.559 -0.060 -0.020 0.010  434 ILE KKK CG1 
13556 C CG2 . ILE K 105 ? 0.586 0.552 0.505 -0.068 -0.030 0.021  434 ILE KKK CG2 
13557 C CD1 . ILE K 105 ? 0.692 0.677 0.611 -0.062 -0.013 0.009  434 ILE KKK CD1 
13558 N N   . ALA K 106 ? 0.560 0.506 0.479 -0.065 -0.038 0.015  435 ALA KKK N   
13559 C CA  . ALA K 106 ? 0.578 0.516 0.495 -0.065 -0.041 0.013  435 ALA KKK CA  
13560 C C   . ALA K 106 ? 0.565 0.499 0.486 -0.069 -0.044 0.017  435 ALA KKK C   
13561 O O   . ALA K 106 ? 0.585 0.524 0.509 -0.073 -0.044 0.020  435 ALA KKK O   
13562 C CB  . ALA K 106 ? 0.573 0.508 0.489 -0.065 -0.041 0.008  435 ALA KKK CB  
13563 N N   . TRP K 107 ? 0.559 0.483 0.481 -0.068 -0.047 0.016  436 TRP KKK N   
13564 C CA  . TRP K 107 ? 0.563 0.478 0.491 -0.072 -0.051 0.019  436 TRP KKK CA  
13565 C C   . TRP K 107 ? 0.559 0.463 0.492 -0.069 -0.052 0.012  436 TRP KKK C   
13566 O O   . TRP K 107 ? 0.589 0.494 0.523 -0.063 -0.051 0.010  436 TRP KKK O   
13567 C CB  . TRP K 107 ? 0.552 0.469 0.482 -0.076 -0.052 0.030  436 TRP KKK CB  
13568 C CG  . TRP K 107 ? 0.554 0.470 0.483 -0.073 -0.054 0.035  436 TRP KKK CG  
13569 C CD1 . TRP K 107 ? 0.563 0.469 0.500 -0.072 -0.059 0.040  436 TRP KKK CD1 
13570 C CD2 . TRP K 107 ? 0.535 0.463 0.457 -0.071 -0.052 0.036  436 TRP KKK CD2 
13571 N NE1 . TRP K 107 ? 0.555 0.466 0.488 -0.069 -0.061 0.046  436 TRP KKK NE1 
13572 C CE2 . TRP K 107 ? 0.549 0.473 0.471 -0.070 -0.057 0.043  436 TRP KKK CE2 
13573 C CE3 . TRP K 107 ? 0.544 0.483 0.459 -0.070 -0.046 0.032  436 TRP KKK CE3 
13574 C CZ2 . TRP K 107 ? 0.549 0.484 0.464 -0.069 -0.057 0.045  436 TRP KKK CZ2 
13575 C CZ3 . TRP K 107 ? 0.549 0.494 0.456 -0.069 -0.046 0.032  436 TRP KKK CZ3 
13576 C CH2 . TRP K 107 ? 0.559 0.503 0.464 -0.069 -0.051 0.038  436 TRP KKK CH2 
13577 N N   . ASN K 108 ? 0.557 0.450 0.493 -0.072 -0.054 0.007  437 ASN KKK N   
13578 C CA  . ASN K 108 ? 0.565 0.445 0.509 -0.068 -0.055 -0.001 437 ASN KKK CA  
13579 C C   . ASN K 108 ? 0.562 0.435 0.518 -0.064 -0.058 0.008  437 ASN KKK C   
13580 O O   . ASN K 108 ? 0.554 0.425 0.511 -0.069 -0.062 0.019  437 ASN KKK O   
13581 C CB  . ASN K 108 ? 0.580 0.449 0.524 -0.075 -0.057 -0.008 437 ASN KKK CB  
13582 C CG  . ASN K 108 ? 0.609 0.463 0.561 -0.070 -0.056 -0.021 437 ASN KKK CG  
13583 O OD1 . ASN K 108 ? 0.630 0.473 0.597 -0.066 -0.058 -0.018 437 ASN KKK OD1 
13584 N ND2 . ASN K 108 ? 0.630 0.487 0.573 -0.072 -0.051 -0.035 437 ASN KKK ND2 
13585 N N   . SER K 109 ? 0.565 0.438 0.529 -0.057 -0.057 0.004  438 SER KKK N   
13586 C CA  . SER K 109 ? 0.575 0.443 0.553 -0.052 -0.063 0.013  438 SER KKK CA  
13587 C C   . SER K 109 ? 0.581 0.434 0.578 -0.045 -0.063 0.004  438 SER KKK C   
13588 O O   . SER K 109 ? 0.595 0.447 0.608 -0.038 -0.066 0.008  438 SER KKK O   
13589 C CB  . SER K 109 ? 0.565 0.448 0.540 -0.048 -0.063 0.019  438 SER KKK CB  
13590 O OG  . SER K 109 ? 0.571 0.461 0.548 -0.044 -0.057 0.007  438 SER KKK OG  
13591 N N   . ASN K 110 ? 0.571 0.413 0.567 -0.047 -0.060 -0.009 439 ASN KKK N   
13592 C CA  . ASN K 110 ? 0.609 0.436 0.623 -0.041 -0.058 -0.023 439 ASN KKK CA  
13593 C C   . ASN K 110 ? 0.616 0.427 0.653 -0.037 -0.067 -0.010 439 ASN KKK C   
13594 O O   . ASN K 110 ? 0.619 0.426 0.678 -0.026 -0.067 -0.014 439 ASN KKK O   
13595 C CB  . ASN K 110 ? 0.628 0.444 0.633 -0.047 -0.055 -0.039 439 ASN KKK CB  
13596 C CG  . ASN K 110 ? 0.647 0.454 0.665 -0.040 -0.048 -0.059 439 ASN KKK CG  
13597 O OD1 . ASN K 110 ? 0.658 0.475 0.685 -0.031 -0.042 -0.065 439 ASN KKK OD1 
13598 N ND2 . ASN K 110 ? 0.675 0.464 0.693 -0.044 -0.048 -0.072 439 ASN KKK ND2 
13599 N N   . ASN K 111 ? 0.612 0.417 0.645 -0.045 -0.074 0.006  440 ASN KKK N   
13600 C CA  . ASN K 111 ? 0.642 0.431 0.694 -0.044 -0.084 0.022  440 ASN KKK CA  
13601 C C   . ASN K 111 ? 0.686 0.485 0.748 -0.036 -0.089 0.036  440 ASN KKK C   
13602 O O   . ASN K 111 ? 0.755 0.540 0.840 -0.031 -0.098 0.045  440 ASN KKK O   
13603 C CB  . ASN K 111 ? 0.615 0.400 0.657 -0.057 -0.089 0.037  440 ASN KKK CB  
13604 C CG  . ASN K 111 ? 0.636 0.404 0.680 -0.065 -0.089 0.027  440 ASN KKK CG  
13605 O OD1 . ASN K 111 ? 0.631 0.383 0.686 -0.060 -0.087 0.009  440 ASN KKK OD1 
13606 N ND2 . ASN K 111 ? 0.647 0.418 0.679 -0.077 -0.091 0.037  440 ASN KKK ND2 
13607 N N   . LEU K 112 ? 0.724 0.547 0.772 -0.036 -0.086 0.037  441 LEU KKK N   
13608 C CA  . LEU K 112 ? 0.754 0.590 0.808 -0.031 -0.093 0.051  441 LEU KKK CA  
13609 C C   . LEU K 112 ? 0.748 0.593 0.816 -0.020 -0.088 0.038  441 LEU KKK C   
13610 O O   . LEU K 112 ? 0.741 0.589 0.831 -0.012 -0.095 0.046  441 LEU KKK O   
13611 C CB  . LEU K 112 ? 0.821 0.677 0.849 -0.039 -0.092 0.060  441 LEU KKK CB  
13612 C CG  . LEU K 112 ? 0.904 0.758 0.915 -0.050 -0.095 0.073  441 LEU KKK CG  
13613 C CD1 . LEU K 112 ? 0.910 0.785 0.897 -0.056 -0.091 0.076  441 LEU KKK CD1 
13614 C CD2 . LEU K 112 ? 0.944 0.787 0.968 -0.052 -0.107 0.094  441 LEU KKK CD2 
13615 N N   . ASP K 113 ? 0.723 0.576 0.782 -0.020 -0.076 0.019  442 ASP KKK N   
13616 C CA  . ASP K 113 ? 0.710 0.580 0.774 -0.013 -0.070 0.009  442 ASP KKK CA  
13617 C C   . ASP K 113 ? 0.740 0.605 0.822 -0.005 -0.061 -0.011 442 ASP KKK C   
13618 O O   . ASP K 113 ? 0.699 0.579 0.786 -0.001 -0.054 -0.020 442 ASP KKK O   
13619 C CB  . ASP K 113 ? 0.663 0.549 0.701 -0.021 -0.064 0.005  442 ASP KKK CB  
13620 C CG  . ASP K 113 ? 0.627 0.524 0.650 -0.026 -0.070 0.021  442 ASP KKK CG  
13621 O OD1 . ASP K 113 ? 0.628 0.529 0.662 -0.023 -0.079 0.032  442 ASP KKK OD1 
13622 O OD2 . ASP K 113 ? 0.611 0.512 0.612 -0.034 -0.067 0.020  442 ASP KKK OD2 
13623 N N   . SER K 114 ? 0.788 0.631 0.880 -0.004 -0.061 -0.018 443 SER KKK N   
13624 C CA  . SER K 114 ? 0.841 0.678 0.950 0.004  -0.051 -0.040 443 SER KKK CA  
13625 C C   . SER K 114 ? 0.837 0.656 0.983 0.015  -0.058 -0.037 443 SER KKK C   
13626 O O   . SER K 114 ? 0.838 0.644 0.988 0.012  -0.070 -0.019 443 SER KKK O   
13627 C CB  . SER K 114 ? 0.873 0.701 0.960 -0.004 -0.043 -0.057 443 SER KKK CB  
13628 O OG  . SER K 114 ? 0.946 0.747 1.038 -0.007 -0.049 -0.056 443 SER KKK OG  
13629 N N   . LYS K 115 ? 0.842 0.663 1.015 0.027  -0.050 -0.053 444 LYS KKK N   
13630 C CA  . LYS K 115 ? 0.907 0.711 1.123 0.040  -0.056 -0.051 444 LYS KKK CA  
13631 C C   . LYS K 115 ? 0.919 0.709 1.150 0.048  -0.043 -0.080 444 LYS KKK C   
13632 O O   . LYS K 115 ? 0.902 0.707 1.114 0.045  -0.028 -0.100 444 LYS KKK O   
13633 C CB  . LYS K 115 ? 0.960 0.784 1.206 0.052  -0.061 -0.040 444 LYS KKK CB  
13634 C CG  . LYS K 115 ? 1.020 0.851 1.267 0.049  -0.078 -0.010 444 LYS KKK CG  
13635 C CD  . LYS K 115 ? 1.067 0.925 1.338 0.058  -0.080 -0.005 444 LYS KKK CD  
13636 C CE  . LYS K 115 ? 1.108 0.977 1.377 0.054  -0.098 0.023  444 LYS KKK CE  
13637 N NZ  . LYS K 115 ? 1.113 0.997 1.338 0.039  -0.097 0.029  444 LYS KKK NZ  
13638 N N   . VAL K 116 ? 0.950 0.712 1.213 0.056  -0.048 -0.082 445 VAL KKK N   
13639 C CA  . VAL K 116 ? 0.990 0.739 1.277 0.067  -0.036 -0.112 445 VAL KKK CA  
13640 C C   . VAL K 116 ? 0.934 0.713 1.246 0.080  -0.024 -0.122 445 VAL KKK C   
13641 O O   . VAL K 116 ? 0.915 0.708 1.251 0.088  -0.034 -0.102 445 VAL KKK O   
13642 C CB  . VAL K 116 ? 1.057 0.768 1.380 0.074  -0.045 -0.110 445 VAL KKK CB  
13643 C CG1 . VAL K 116 ? 1.070 0.755 1.367 0.059  -0.054 -0.103 445 VAL KKK CG1 
13644 C CG2 . VAL K 116 ? 1.068 0.779 1.430 0.086  -0.061 -0.083 445 VAL KKK CG2 
13645 N N   . GLY K 117 ? 0.894 0.686 1.195 0.080  -0.005 -0.150 446 GLY KKK N   
13646 C CA  . GLY K 117 ? 0.868 0.692 1.189 0.091  0.009  -0.161 446 GLY KKK CA  
13647 C C   . GLY K 117 ? 0.844 0.701 1.136 0.080  0.009  -0.147 446 GLY KKK C   
13648 O O   . GLY K 117 ? 0.843 0.729 1.151 0.086  0.020  -0.154 446 GLY KKK O   
13649 N N   . GLY K 118 ? 0.825 0.678 1.079 0.065  -0.001 -0.129 447 GLY KKK N   
13650 C CA  . GLY K 118 ? 0.783 0.661 1.003 0.054  0.001  -0.121 447 GLY KKK CA  
13651 C C   . GLY K 118 ? 0.744 0.637 0.973 0.054  -0.013 -0.094 447 GLY KKK C   
13652 O O   . GLY K 118 ? 0.750 0.652 1.019 0.067  -0.017 -0.089 447 GLY KKK O   
13653 N N   . ASN K 119 ? 0.705 0.601 0.900 0.041  -0.021 -0.078 448 ASN KKK N   
13654 C CA  . ASN K 119 ? 0.695 0.607 0.890 0.039  -0.033 -0.056 448 ASN KKK CA  
13655 C C   . ASN K 119 ? 0.668 0.609 0.853 0.035  -0.022 -0.061 448 ASN KKK C   
13656 O O   . ASN K 119 ? 0.736 0.680 0.888 0.024  -0.015 -0.067 448 ASN KKK O   
13657 C CB  . ASN K 119 ? 0.683 0.584 0.849 0.028  -0.045 -0.038 448 ASN KKK CB  
13658 C CG  . ASN K 119 ? 0.659 0.576 0.821 0.024  -0.056 -0.018 448 ASN KKK CG  
13659 O OD1 . ASN K 119 ? 0.656 0.591 0.842 0.030  -0.059 -0.014 448 ASN KKK OD1 
13660 N ND2 . ASN K 119 ? 0.661 0.573 0.794 0.013  -0.063 -0.006 448 ASN KKK ND2 
13661 N N   . TYR K 120 ? 0.682 0.645 0.899 0.042  -0.023 -0.059 449 TYR KKK N   
13662 C CA  . TYR K 120 ? 0.700 0.692 0.916 0.039  -0.013 -0.063 449 TYR KKK CA  
13663 C C   . TYR K 120 ? 0.693 0.698 0.902 0.032  -0.027 -0.043 449 TYR KKK C   
13664 O O   . TYR K 120 ? 0.716 0.744 0.927 0.028  -0.022 -0.044 449 TYR KKK O   
13665 C CB  . TYR K 120 ? 0.718 0.727 0.973 0.051  -0.001 -0.078 449 TYR KKK CB  
13666 C CG  . TYR K 120 ? 0.770 0.768 1.023 0.055  0.016  -0.102 449 TYR KKK CG  
13667 C CD1 . TYR K 120 ? 0.780 0.786 1.003 0.045  0.032  -0.116 449 TYR KKK CD1 
13668 C CD2 . TYR K 120 ? 0.806 0.784 1.087 0.068  0.015  -0.110 449 TYR KKK CD2 
13669 C CE1 . TYR K 120 ? 0.809 0.806 1.025 0.047  0.047  -0.140 449 TYR KKK CE1 
13670 C CE2 . TYR K 120 ? 0.835 0.801 1.112 0.070  0.030  -0.135 449 TYR KKK CE2 
13671 C CZ  . TYR K 120 ? 0.845 0.822 1.089 0.060  0.047  -0.151 449 TYR KKK CZ  
13672 O OH  . TYR K 120 ? 0.862 0.829 1.098 0.061  0.062  -0.177 449 TYR KKK OH  
13673 N N   . ASN K 121 ? 0.716 0.706 0.914 0.029  -0.043 -0.027 450 ASN KKK N   
13674 C CA  . ASN K 121 ? 0.712 0.714 0.900 0.021  -0.056 -0.009 450 ASN KKK CA  
13675 C C   . ASN K 121 ? 0.684 0.690 0.835 0.008  -0.051 -0.012 450 ASN KKK C   
13676 O O   . ASN K 121 ? 0.693 0.715 0.841 0.002  -0.056 -0.005 450 ASN KKK O   
13677 C CB  . ASN K 121 ? 0.737 0.724 0.921 0.021  -0.073 0.009  450 ASN KKK CB  
13678 C CG  . ASN K 121 ? 0.803 0.791 1.029 0.033  -0.083 0.017  450 ASN KKK CG  
13679 O OD1 . ASN K 121 ? 0.824 0.831 1.083 0.042  -0.080 0.012  450 ASN KKK OD1 
13680 N ND2 . ASN K 121 ? 0.866 0.835 1.093 0.035  -0.096 0.031  450 ASN KKK ND2 
13681 N N   . TYR K 122 ? 0.658 0.650 0.782 0.003  -0.042 -0.020 451 TYR KKK N   
13682 C CA  . TYR K 122 ? 0.613 0.607 0.705 -0.009 -0.038 -0.020 451 TYR KKK CA  
13683 C C   . TYR K 122 ? 0.605 0.615 0.698 -0.012 -0.025 -0.031 451 TYR KKK C   
13684 O O   . TYR K 122 ? 0.587 0.597 0.686 -0.008 -0.013 -0.044 451 TYR KKK O   
13685 C CB  . TYR K 122 ? 0.605 0.578 0.669 -0.013 -0.038 -0.021 451 TYR KKK CB  
13686 C CG  . TYR K 122 ? 0.608 0.569 0.666 -0.014 -0.050 -0.008 451 TYR KKK CG  
13687 C CD1 . TYR K 122 ? 0.583 0.550 0.627 -0.021 -0.058 0.002  451 TYR KKK CD1 
13688 C CD2 . TYR K 122 ? 0.607 0.551 0.673 -0.010 -0.053 -0.007 451 TYR KKK CD2 
13689 C CE1 . TYR K 122 ? 0.602 0.560 0.637 -0.023 -0.068 0.014  451 TYR KKK CE1 
13690 C CE2 . TYR K 122 ? 0.615 0.550 0.675 -0.012 -0.065 0.008  451 TYR KKK CE2 
13691 C CZ  . TYR K 122 ? 0.615 0.558 0.658 -0.019 -0.071 0.018  451 TYR KKK CZ  
13692 O OH  . TYR K 122 ? 0.632 0.567 0.666 -0.023 -0.080 0.032  451 TYR KKK OH  
13693 N N   . LEU K 123 ? 0.596 0.619 0.684 -0.019 -0.027 -0.026 452 LEU KKK N   
13694 C CA  . LEU K 123 ? 0.593 0.634 0.684 -0.024 -0.016 -0.032 452 LEU KKK CA  
13695 C C   . LEU K 123 ? 0.582 0.616 0.642 -0.036 -0.014 -0.030 452 LEU KKK C   
13696 O O   . LEU K 123 ? 0.589 0.610 0.631 -0.039 -0.023 -0.023 452 LEU KKK O   
13697 C CB  . LEU K 123 ? 0.591 0.653 0.708 -0.024 -0.021 -0.026 452 LEU KKK CB  
13698 C CG  . LEU K 123 ? 0.596 0.668 0.750 -0.012 -0.026 -0.026 452 LEU KKK CG  
13699 C CD1 . LEU K 123 ? 0.591 0.688 0.771 -0.014 -0.033 -0.019 452 LEU KKK CD1 
13700 C CD2 . LEU K 123 ? 0.594 0.670 0.766 -0.003 -0.011 -0.039 452 LEU KKK CD2 
13701 N N   . TYR K 124 ? 0.557 0.602 0.612 -0.042 -0.002 -0.035 453 TYR KKK N   
13702 C CA  . TYR K 124 ? 0.564 0.605 0.596 -0.053 -0.001 -0.031 453 TYR KKK CA  
13703 C C   . TYR K 124 ? 0.560 0.622 0.604 -0.059 0.007  -0.031 453 TYR KKK C   
13704 O O   . TYR K 124 ? 0.567 0.646 0.630 -0.055 0.017  -0.038 453 TYR KKK O   
13705 C CB  . TYR K 124 ? 0.572 0.600 0.579 -0.055 0.004  -0.034 453 TYR KKK CB  
13706 C CG  . TYR K 124 ? 0.591 0.628 0.599 -0.054 0.018  -0.045 453 TYR KKK CG  
13707 C CD1 . TYR K 124 ? 0.586 0.618 0.603 -0.045 0.020  -0.055 453 TYR KKK CD1 
13708 C CD2 . TYR K 124 ? 0.611 0.661 0.610 -0.063 0.028  -0.045 453 TYR KKK CD2 
13709 C CE1 . TYR K 124 ? 0.608 0.648 0.625 -0.044 0.034  -0.068 453 TYR KKK CE1 
13710 C CE2 . TYR K 124 ? 0.628 0.689 0.625 -0.063 0.042  -0.057 453 TYR KKK CE2 
13711 C CZ  . TYR K 124 ? 0.623 0.678 0.628 -0.053 0.045  -0.070 453 TYR KKK CZ  
13712 O OH  . TYR K 124 ? 0.641 0.707 0.643 -0.053 0.060  -0.084 453 TYR KKK OH  
13713 N N   . ARG K 125 ? 0.565 0.627 0.601 -0.070 0.004  -0.024 454 ARG KKK N   
13714 C CA  . ARG K 125 ? 0.575 0.655 0.620 -0.079 0.012  -0.022 454 ARG KKK CA  
13715 C C   . ARG K 125 ? 0.578 0.659 0.604 -0.084 0.024  -0.024 454 ARG KKK C   
13716 O O   . ARG K 125 ? 0.612 0.676 0.613 -0.088 0.021  -0.020 454 ARG KKK O   
13717 C CB  . ARG K 125 ? 0.550 0.625 0.593 -0.088 0.003  -0.013 454 ARG KKK CB  
13718 C CG  . ARG K 125 ? 0.562 0.656 0.619 -0.100 0.009  -0.009 454 ARG KKK CG  
13719 C CD  . ARG K 125 ? 0.560 0.646 0.619 -0.109 -0.002 -0.003 454 ARG KKK CD  
13720 N NE  . ARG K 125 ? 0.556 0.642 0.626 -0.103 -0.014 -0.005 454 ARG KKK NE  
13721 C CZ  . ARG K 125 ? 0.538 0.645 0.635 -0.102 -0.017 -0.006 454 ARG KKK CZ  
13722 N NH1 . ARG K 125 ? 0.547 0.679 0.665 -0.105 -0.007 -0.007 454 ARG KKK NH1 
13723 N NH2 . ARG K 125 ? 0.527 0.634 0.630 -0.098 -0.030 -0.007 454 ARG KKK NH2 
13724 N N   . LEU K 126 ? 0.614 0.717 0.651 -0.085 0.038  -0.029 455 LEU KKK N   
13725 C CA  . LEU K 126 ? 0.662 0.771 0.679 -0.091 0.051  -0.033 455 LEU KKK CA  
13726 C C   . LEU K 126 ? 0.668 0.788 0.680 -0.107 0.056  -0.022 455 LEU KKK C   
13727 O O   . LEU K 126 ? 0.680 0.797 0.666 -0.116 0.060  -0.018 455 LEU KKK O   
13728 C CB  . LEU K 126 ? 0.673 0.800 0.707 -0.083 0.065  -0.048 455 LEU KKK CB  
13729 C CG  . LEU K 126 ? 0.734 0.872 0.747 -0.090 0.081  -0.056 455 LEU KKK CG  
13730 C CD1 . LEU K 126 ? 0.742 0.858 0.719 -0.093 0.076  -0.054 455 LEU KKK CD1 
13731 C CD2 . LEU K 126 ? 0.735 0.889 0.768 -0.079 0.095  -0.074 455 LEU KKK CD2 
13732 N N   . PHE K 127 ? 0.649 0.784 0.686 -0.111 0.055  -0.018 456 PHE KKK N   
13733 C CA  . PHE K 127 ? 0.675 0.824 0.715 -0.126 0.060  -0.007 456 PHE KKK CA  
13734 C C   . PHE K 127 ? 0.643 0.780 0.694 -0.131 0.045  0.002  456 PHE KKK C   
13735 O O   . PHE K 127 ? 0.625 0.761 0.694 -0.123 0.036  -0.002 456 PHE KKK O   
13736 C CB  . PHE K 127 ? 0.684 0.867 0.749 -0.128 0.075  -0.013 456 PHE KKK CB  
13737 C CG  . PHE K 127 ? 0.702 0.900 0.760 -0.123 0.092  -0.026 456 PHE KKK CG  
13738 C CD1 . PHE K 127 ? 0.729 0.926 0.754 -0.132 0.101  -0.024 456 PHE KKK CD1 
13739 C CD2 . PHE K 127 ? 0.686 0.896 0.769 -0.108 0.098  -0.041 456 PHE KKK CD2 
13740 C CE1 . PHE K 127 ? 0.734 0.944 0.749 -0.128 0.117  -0.039 456 PHE KKK CE1 
13741 C CE2 . PHE K 127 ? 0.702 0.923 0.779 -0.103 0.114  -0.056 456 PHE KKK CE2 
13742 C CZ  . PHE K 127 ? 0.728 0.949 0.769 -0.113 0.124  -0.056 456 PHE KKK CZ  
13743 N N   . ARG K 128 ? 0.627 0.756 0.667 -0.145 0.042  0.015  457 ARG KKK N   
13744 C CA  . ARG K 128 ? 0.622 0.739 0.673 -0.152 0.030  0.022  457 ARG KKK CA  
13745 C C   . ARG K 128 ? 0.627 0.745 0.672 -0.170 0.034  0.036  457 ARG KKK C   
13746 O O   . ARG K 128 ? 0.595 0.708 0.618 -0.174 0.039  0.043  457 ARG KKK O   
13747 C CB  . ARG K 128 ? 0.574 0.662 0.613 -0.145 0.016  0.020  457 ARG KKK CB  
13748 C CG  . ARG K 128 ? 0.575 0.653 0.627 -0.150 0.004  0.022  457 ARG KKK CG  
13749 C CD  . ARG K 128 ? 0.590 0.644 0.630 -0.141 -0.008 0.017  457 ARG KKK CD  
13750 N NE  . ARG K 128 ? 0.598 0.648 0.651 -0.144 -0.019 0.013  457 ARG KKK NE  
13751 C CZ  . ARG K 128 ? 0.595 0.628 0.648 -0.154 -0.026 0.017  457 ARG KKK CZ  
13752 N NH1 . ARG K 128 ? 0.630 0.648 0.674 -0.160 -0.023 0.025  457 ARG KKK NH1 
13753 N NH2 . ARG K 128 ? 0.584 0.614 0.646 -0.157 -0.036 0.011  457 ARG KKK NH2 
13754 N N   . LYS K 129 ? 0.669 0.792 0.735 -0.181 0.029  0.042  458 LYS KKK N   
13755 C CA  . LYS K 129 ? 0.720 0.845 0.788 -0.200 0.032  0.057  458 LYS KKK CA  
13756 C C   . LYS K 129 ? 0.723 0.814 0.770 -0.203 0.023  0.068  458 LYS KKK C   
13757 O O   . LYS K 129 ? 0.758 0.847 0.796 -0.216 0.026  0.083  458 LYS KKK O   
13758 C CB  . LYS K 129 ? 0.738 0.874 0.836 -0.210 0.027  0.059  458 LYS KKK CB  
13759 C CG  . LYS K 129 ? 0.759 0.933 0.884 -0.208 0.036  0.051  458 LYS KKK CG  
13760 C CD  . LYS K 129 ? 0.799 0.997 0.954 -0.225 0.039  0.059  458 LYS KKK CD  
13761 C CE  . LYS K 129 ? 0.815 1.057 0.990 -0.223 0.056  0.055  458 LYS KKK CE  
13762 N NZ  . LYS K 129 ? 0.852 1.121 1.057 -0.242 0.061  0.064  458 LYS KKK NZ  
13763 N N   . SER K 130 ? 0.709 0.774 0.749 -0.192 0.011  0.060  459 SER KKK N   
13764 C CA  . SER K 130 ? 0.693 0.726 0.720 -0.192 0.002  0.068  459 SER KKK CA  
13765 C C   . SER K 130 ? 0.686 0.702 0.701 -0.175 -0.005 0.056  459 SER KKK C   
13766 O O   . SER K 130 ? 0.674 0.701 0.695 -0.166 -0.005 0.044  459 SER KKK O   
13767 C CB  . SER K 130 ? 0.689 0.705 0.731 -0.203 -0.007 0.074  459 SER KKK CB  
13768 O OG  . SER K 130 ? 0.691 0.699 0.744 -0.197 -0.016 0.060  459 SER KKK OG  
13769 N N   . ASN K 131 ? 0.676 0.668 0.678 -0.172 -0.011 0.062  460 ASN KKK N   
13770 C CA  . ASN K 131 ? 0.648 0.626 0.638 -0.157 -0.016 0.053  460 ASN KKK CA  
13771 C C   . ASN K 131 ? 0.621 0.587 0.623 -0.153 -0.024 0.041  460 ASN KKK C   
13772 O O   . ASN K 131 ? 0.616 0.572 0.629 -0.161 -0.029 0.043  460 ASN KKK O   
13773 C CB  . ASN K 131 ? 0.651 0.610 0.628 -0.156 -0.020 0.063  460 ASN KKK CB  
13774 C CG  . ASN K 131 ? 0.660 0.632 0.620 -0.161 -0.013 0.073  460 ASN KKK CG  
13775 O OD1 . ASN K 131 ? 0.642 0.638 0.599 -0.164 -0.003 0.070  460 ASN KKK OD1 
13776 N ND2 . ASN K 131 ? 0.699 0.658 0.649 -0.162 -0.018 0.085  460 ASN KKK ND2 
13777 N N   . LEU K 132 ? 0.621 0.586 0.616 -0.141 -0.026 0.030  461 LEU KKK N   
13778 C CA  . LEU K 132 ? 0.650 0.603 0.648 -0.136 -0.033 0.019  461 LEU KKK CA  
13779 C C   . LEU K 132 ? 0.696 0.622 0.693 -0.136 -0.039 0.021  461 LEU KKK C   
13780 O O   . LEU K 132 ? 0.705 0.622 0.695 -0.133 -0.037 0.029  461 LEU KKK O   
13781 C CB  . LEU K 132 ? 0.643 0.600 0.631 -0.123 -0.033 0.011  461 LEU KKK CB  
13782 C CG  . LEU K 132 ? 0.663 0.643 0.658 -0.120 -0.030 0.007  461 LEU KKK CG  
13783 C CD1 . LEU K 132 ? 0.666 0.645 0.652 -0.109 -0.033 0.001  461 LEU KKK CD1 
13784 C CD2 . LEU K 132 ? 0.668 0.660 0.680 -0.127 -0.035 0.004  461 LEU KKK CD2 
13785 N N   . LYS K 133 ? 0.724 0.637 0.729 -0.140 -0.044 0.013  462 LYS KKK N   
13786 C CA  . LYS K 133 ? 0.745 0.633 0.750 -0.136 -0.049 0.008  462 LYS KKK CA  
13787 C C   . LYS K 133 ? 0.712 0.600 0.705 -0.123 -0.048 -0.001 462 LYS KKK C   
13788 O O   . LYS K 133 ? 0.645 0.550 0.630 -0.118 -0.046 -0.006 462 LYS KKK O   
13789 C CB  . LYS K 133 ? 0.805 0.681 0.821 -0.144 -0.054 -0.002 462 LYS KKK CB  
13790 C CG  . LYS K 133 ? 0.886 0.755 0.918 -0.158 -0.056 0.009  462 LYS KKK CG  
13791 C CD  . LYS K 133 ? 1.009 0.857 1.053 -0.166 -0.063 -0.002 462 LYS KKK CD  
13792 C CE  . LYS K 133 ? 1.090 0.936 1.126 -0.161 -0.066 -0.023 462 LYS KKK CE  
13793 N NZ  . LYS K 133 ? 1.108 0.980 1.142 -0.166 -0.069 -0.028 462 LYS KKK NZ  
13794 N N   . PRO K 134 ? 0.698 0.568 0.690 -0.115 -0.048 -0.004 463 PRO KKK N   
13795 C CA  . PRO K 134 ? 0.670 0.543 0.652 -0.104 -0.046 -0.012 463 PRO KKK CA  
13796 C C   . PRO K 134 ? 0.630 0.511 0.605 -0.104 -0.048 -0.026 463 PRO KKK C   
13797 O O   . PRO K 134 ? 0.605 0.478 0.584 -0.110 -0.051 -0.035 463 PRO KKK O   
13798 C CB  . PRO K 134 ? 0.684 0.536 0.674 -0.099 -0.047 -0.013 463 PRO KKK CB  
13799 C CG  . PRO K 134 ? 0.681 0.524 0.682 -0.105 -0.049 0.003  463 PRO KKK CG  
13800 C CD  . PRO K 134 ? 0.693 0.542 0.697 -0.117 -0.050 0.004  463 PRO KKK CD  
13801 N N   . PHE K 135 ? 0.607 0.503 0.571 -0.099 -0.046 -0.027 464 PHE KKK N   
13802 C CA  . PHE K 135 ? 0.616 0.521 0.570 -0.098 -0.049 -0.037 464 PHE KKK CA  
13803 C C   . PHE K 135 ? 0.610 0.527 0.570 -0.107 -0.054 -0.037 464 PHE KKK C   
13804 O O   . PHE K 135 ? 0.610 0.534 0.564 -0.110 -0.059 -0.044 464 PHE KKK O   
13805 C CB  . PHE K 135 ? 0.610 0.505 0.558 -0.097 -0.049 -0.050 464 PHE KKK CB  
13806 C CG  . PHE K 135 ? 0.595 0.485 0.540 -0.087 -0.043 -0.051 464 PHE KKK CG  
13807 C CD1 . PHE K 135 ? 0.591 0.492 0.527 -0.081 -0.041 -0.044 464 PHE KKK CD1 
13808 C CD2 . PHE K 135 ? 0.595 0.467 0.548 -0.084 -0.040 -0.057 464 PHE KKK CD2 
13809 C CE1 . PHE K 135 ? 0.587 0.486 0.523 -0.073 -0.036 -0.044 464 PHE KKK CE1 
13810 C CE2 . PHE K 135 ? 0.601 0.472 0.555 -0.074 -0.035 -0.057 464 PHE KKK CE2 
13811 C CZ  . PHE K 135 ? 0.606 0.491 0.550 -0.070 -0.033 -0.050 464 PHE KKK CZ  
13812 N N   . GLU K 136 ? 0.612 0.534 0.585 -0.113 -0.053 -0.028 465 GLU KKK N   
13813 C CA  . GLU K 136 ? 0.616 0.554 0.599 -0.121 -0.057 -0.027 465 GLU KKK CA  
13814 C C   . GLU K 136 ? 0.615 0.574 0.597 -0.115 -0.056 -0.023 465 GLU KKK C   
13815 O O   . GLU K 136 ? 0.597 0.555 0.571 -0.106 -0.051 -0.019 465 GLU KKK O   
13816 C CB  . GLU K 136 ? 0.637 0.574 0.633 -0.130 -0.054 -0.018 465 GLU KKK CB  
13817 C CG  . GLU K 136 ? 0.648 0.601 0.660 -0.140 -0.059 -0.018 465 GLU KKK CG  
13818 C CD  . GLU K 136 ? 0.663 0.619 0.690 -0.151 -0.056 -0.008 465 GLU KKK CD  
13819 O OE1 . GLU K 136 ? 0.662 0.605 0.686 -0.151 -0.051 -0.000 465 GLU KKK OE1 
13820 O OE2 . GLU K 136 ? 0.691 0.663 0.733 -0.160 -0.058 -0.008 465 GLU KKK OE2 
13821 N N   . ARG K 137 ? 0.616 0.590 0.605 -0.118 -0.062 -0.025 466 ARG KKK N   
13822 C CA  . ARG K 137 ? 0.641 0.634 0.634 -0.112 -0.063 -0.021 466 ARG KKK CA  
13823 C C   . ARG K 137 ? 0.640 0.654 0.656 -0.118 -0.065 -0.017 466 ARG KKK C   
13824 O O   . ARG K 137 ? 0.671 0.688 0.693 -0.127 -0.072 -0.021 466 ARG KKK O   
13825 C CB  . ARG K 137 ? 0.650 0.644 0.631 -0.110 -0.071 -0.025 466 ARG KKK CB  
13826 C CG  . ARG K 137 ? 0.664 0.673 0.649 -0.102 -0.074 -0.020 466 ARG KKK CG  
13827 C CD  . ARG K 137 ? 0.686 0.692 0.653 -0.102 -0.082 -0.023 466 ARG KKK CD  
13828 N NE  . ARG K 137 ? 0.731 0.747 0.700 -0.095 -0.086 -0.015 466 ARG KKK NE  
13829 C CZ  . ARG K 137 ? 0.776 0.809 0.756 -0.096 -0.097 -0.010 466 ARG KKK CZ  
13830 N NH1 . ARG K 137 ? 0.791 0.835 0.782 -0.105 -0.104 -0.012 466 ARG KKK NH1 
13831 N NH2 . ARG K 137 ? 0.773 0.812 0.756 -0.089 -0.101 -0.002 466 ARG KKK NH2 
13832 N N   . ASP K 138 ? 0.600 0.627 0.627 -0.113 -0.058 -0.012 467 ASP KKK N   
13833 C CA  . ASP K 138 ? 0.578 0.629 0.631 -0.118 -0.056 -0.009 467 ASP KKK CA  
13834 C C   . ASP K 138 ? 0.575 0.643 0.640 -0.107 -0.057 -0.008 467 ASP KKK C   
13835 O O   . ASP K 138 ? 0.578 0.642 0.637 -0.098 -0.049 -0.007 467 ASP KKK O   
13836 C CB  . ASP K 138 ? 0.569 0.621 0.626 -0.123 -0.045 -0.005 467 ASP KKK CB  
13837 C CG  . ASP K 138 ? 0.578 0.656 0.661 -0.129 -0.041 -0.002 467 ASP KKK CG  
13838 O OD1 . ASP K 138 ? 0.521 0.619 0.624 -0.127 -0.047 -0.003 467 ASP KKK OD1 
13839 O OD2 . ASP K 138 ? 0.604 0.685 0.690 -0.136 -0.031 0.003  467 ASP KKK OD2 
13840 N N   . ILE K 139 ? 0.581 0.665 0.662 -0.109 -0.068 -0.007 468 ILE KKK N   
13841 C CA  . ILE K 139 ? 0.560 0.662 0.660 -0.098 -0.071 -0.004 468 ILE KKK CA  
13842 C C   . ILE K 139 ? 0.532 0.663 0.667 -0.100 -0.068 -0.002 468 ILE KKK C   
13843 O O   . ILE K 139 ? 0.537 0.685 0.695 -0.091 -0.072 0.001  468 ILE KKK O   
13844 C CB  . ILE K 139 ? 0.571 0.669 0.661 -0.096 -0.086 -0.002 468 ILE KKK CB  
13845 C CG1 . ILE K 139 ? 0.599 0.708 0.694 -0.108 -0.100 -0.002 468 ILE KKK CG1 
13846 C CG2 . ILE K 139 ? 0.579 0.653 0.637 -0.093 -0.085 -0.004 468 ILE KKK CG2 
13847 C CD1 . ILE K 139 ? 0.630 0.746 0.721 -0.106 -0.116 0.003  468 ILE KKK CD1 
13848 N N   . SER K 140 ? 0.530 0.666 0.672 -0.111 -0.062 -0.002 469 SER KKK N   
13849 C CA  . SER K 140 ? 0.528 0.695 0.705 -0.115 -0.057 -0.000 469 SER KKK CA  
13850 C C   . SER K 140 ? 0.499 0.679 0.690 -0.104 -0.041 -0.002 469 SER KKK C   
13851 O O   . SER K 140 ? 0.490 0.652 0.659 -0.098 -0.032 -0.005 469 SER KKK O   
13852 C CB  . SER K 140 ? 0.548 0.715 0.725 -0.132 -0.053 0.001  469 SER KKK CB  
13853 O OG  . SER K 140 ? 0.606 0.759 0.765 -0.132 -0.039 0.001  469 SER KKK OG  
13854 N N   . THR K 141 ? 0.488 0.699 0.717 -0.101 -0.039 -0.001 470 THR KKK N   
13855 C CA  . THR K 141 ? 0.494 0.722 0.743 -0.090 -0.023 -0.006 470 THR KKK CA  
13856 C C   . THR K 141 ? 0.503 0.763 0.781 -0.099 -0.011 -0.005 470 THR KKK C   
13857 O O   . THR K 141 ? 0.537 0.826 0.853 -0.091 -0.006 -0.007 470 THR KKK O   
13858 C CB  . THR K 141 ? 0.490 0.724 0.761 -0.074 -0.032 -0.006 470 THR KKK CB  
13859 O OG1 . THR K 141 ? 0.507 0.761 0.804 -0.077 -0.048 0.001  470 THR KKK OG1 
13860 C CG2 . THR K 141 ? 0.497 0.699 0.737 -0.066 -0.040 -0.005 470 THR KKK CG2 
13861 N N   . GLU K 142 ? 0.502 0.757 0.765 -0.115 -0.008 -0.002 471 GLU KKK N   
13862 C CA  . GLU K 142 ? 0.504 0.788 0.791 -0.128 0.004  0.001  471 GLU KKK CA  
13863 C C   . GLU K 142 ? 0.499 0.792 0.781 -0.123 0.027  -0.004 471 GLU KKK C   
13864 O O   . GLU K 142 ? 0.474 0.742 0.721 -0.119 0.032  -0.007 471 GLU KKK O   
13865 C CB  . GLU K 142 ? 0.510 0.780 0.779 -0.148 -0.001 0.008  471 GLU KKK CB  
13866 C CG  . GLU K 142 ? 0.518 0.775 0.785 -0.154 -0.023 0.010  471 GLU KKK CG  
13867 C CD  . GLU K 142 ? 0.533 0.823 0.842 -0.158 -0.033 0.012  471 GLU KKK CD  
13868 O OE1 . GLU K 142 ? 0.563 0.875 0.894 -0.172 -0.026 0.017  471 GLU KKK OE1 
13869 O OE2 . GLU K 142 ? 0.525 0.821 0.845 -0.149 -0.048 0.012  471 GLU KKK OE2 
13870 N N   . ILE K 143 ? 0.505 0.836 0.821 -0.124 0.041  -0.007 472 ILE KKK N   
13871 C CA  . ILE K 143 ? 0.522 0.867 0.834 -0.122 0.066  -0.014 472 ILE KKK CA  
13872 C C   . ILE K 143 ? 0.525 0.854 0.799 -0.139 0.072  -0.006 472 ILE KKK C   
13873 O O   . ILE K 143 ? 0.508 0.840 0.786 -0.156 0.067  0.004  472 ILE KKK O   
13874 C CB  . ILE K 143 ? 0.536 0.929 0.895 -0.122 0.081  -0.016 472 ILE KKK CB  
13875 C CG1 . ILE K 143 ? 0.545 0.956 0.949 -0.105 0.071  -0.021 472 ILE KKK CG1 
13876 C CG2 . ILE K 143 ? 0.551 0.959 0.900 -0.121 0.108  -0.026 472 ILE KKK CG2 
13877 C CD1 . ILE K 143 ? 0.552 0.941 0.946 -0.084 0.069  -0.030 472 ILE KKK CD1 
13878 N N   . TYR K 144 ? 0.528 0.838 0.767 -0.135 0.082  -0.011 473 TYR KKK N   
13879 C CA  . TYR K 144 ? 0.560 0.854 0.762 -0.150 0.086  -0.002 473 TYR KKK CA  
13880 C C   . TYR K 144 ? 0.579 0.907 0.788 -0.161 0.109  -0.002 473 TYR KKK C   
13881 O O   . TYR K 144 ? 0.574 0.922 0.790 -0.151 0.126  -0.015 473 TYR KKK O   
13882 C CB  . TYR K 144 ? 0.586 0.847 0.749 -0.142 0.083  -0.006 473 TYR KKK CB  
13883 C CG  . TYR K 144 ? 0.635 0.880 0.761 -0.156 0.087  0.003  473 TYR KKK CG  
13884 C CD1 . TYR K 144 ? 0.650 0.869 0.760 -0.165 0.073  0.016  473 TYR KKK CD1 
13885 C CD2 . TYR K 144 ? 0.687 0.945 0.794 -0.158 0.105  -0.001 473 TYR KKK CD2 
13886 C CE1 . TYR K 144 ? 0.686 0.891 0.766 -0.177 0.075  0.027  473 TYR KKK CE1 
13887 C CE2 . TYR K 144 ? 0.724 0.968 0.795 -0.171 0.107  0.010  473 TYR KKK CE2 
13888 C CZ  . TYR K 144 ? 0.718 0.936 0.777 -0.179 0.091  0.025  473 TYR KKK CZ  
13889 O OH  . TYR K 144 ? 0.777 0.982 0.806 -0.191 0.091  0.037  473 TYR KKK OH  
13890 N N   . GLN K 145 ? 0.607 0.941 0.814 -0.181 0.110  0.013  474 GLN KKK N   
13891 C CA  . GLN K 145 ? 0.650 1.014 0.854 -0.196 0.132  0.018  474 GLN KKK CA  
13892 C C   . GLN K 145 ? 0.689 1.033 0.845 -0.202 0.138  0.022  474 GLN KKK C   
13893 O O   . GLN K 145 ? 0.703 1.021 0.837 -0.214 0.126  0.037  474 GLN KKK O   
13894 C CB  . GLN K 145 ? 0.654 1.031 0.878 -0.217 0.128  0.034  474 GLN KKK CB  
13895 C CG  . GLN K 145 ? 0.692 1.100 0.912 -0.234 0.150  0.041  474 GLN KKK CG  
13896 C CD  . GLN K 145 ? 0.698 1.126 0.947 -0.255 0.149  0.056  474 GLN KKK CD  
13897 O OE1 . GLN K 145 ? 0.699 1.130 0.982 -0.253 0.135  0.056  474 GLN KKK OE1 
13898 N NE2 . GLN K 145 ? 0.745 1.188 0.982 -0.275 0.162  0.070  474 GLN KKK NE2 
13899 N N   . ALA K 146 ? 0.718 1.073 0.860 -0.193 0.154  0.008  475 ALA KKK N   
13900 C CA  . ALA K 146 ? 0.768 1.108 0.862 -0.198 0.160  0.009  475 ALA KKK CA  
13901 C C   . ALA K 146 ? 0.806 1.177 0.888 -0.218 0.180  0.018  475 ALA KKK C   
13902 O O   . ALA K 146 ? 0.846 1.206 0.887 -0.227 0.183  0.024  475 ALA KKK O   
13903 C CB  . ALA K 146 ? 0.763 1.100 0.848 -0.179 0.167  -0.013 475 ALA KKK CB  
13904 N N   . GLY K 147 ? 0.824 1.232 0.941 -0.226 0.192  0.019  476 GLY KKK N   
13905 C CA  . GLY K 147 ? 0.869 1.313 0.978 -0.245 0.215  0.026  476 GLY KKK CA  
13906 C C   . GLY K 147 ? 0.893 1.350 1.024 -0.266 0.211  0.049  476 GLY KKK C   
13907 O O   . GLY K 147 ? 0.927 1.365 1.081 -0.264 0.191  0.056  476 GLY KKK O   
13908 N N   . SER K 148 ? 0.918 1.408 1.042 -0.286 0.231  0.058  477 SER KKK N   
13909 C CA  . SER K 148 ? 0.915 1.428 1.065 -0.308 0.234  0.078  477 SER KKK CA  
13910 C C   . SER K 148 ? 0.895 1.434 1.105 -0.299 0.233  0.069  477 SER KKK C   
13911 O O   . SER K 148 ? 0.896 1.427 1.130 -0.310 0.218  0.083  477 SER KKK O   
13912 C CB  . SER K 148 ? 0.934 1.486 1.066 -0.329 0.260  0.086  477 SER KKK CB  
13913 O OG  . SER K 148 ? 0.936 1.503 1.039 -0.319 0.280  0.066  477 SER KKK OG  
13914 N N   . THR K 149 ? 0.869 1.438 1.103 -0.281 0.249  0.045  478 THR KKK N   
13915 C CA  . THR K 149 ? 0.822 1.424 1.118 -0.272 0.251  0.035  478 THR KKK CA  
13916 C C   . THR K 149 ? 0.788 1.357 1.104 -0.259 0.221  0.036  478 THR KKK C   
13917 O O   . THR K 149 ? 0.789 1.318 1.079 -0.244 0.207  0.029  478 THR KKK O   
13918 C CB  . THR K 149 ? 0.806 1.439 1.119 -0.251 0.273  0.008  478 THR KKK CB  
13919 O OG1 . THR K 149 ? 0.776 1.373 1.053 -0.233 0.268  -0.006 478 THR KKK OG1 
13920 C CG2 . THR K 149 ? 0.826 1.504 1.132 -0.264 0.307  0.004  478 THR KKK CG2 
13921 N N   . PRO K 150 ? 0.770 1.355 1.130 -0.267 0.211  0.044  479 PRO KKK N   
13922 C CA  . PRO K 150 ? 0.741 1.302 1.122 -0.254 0.183  0.041  479 PRO KKK CA  
13923 C C   . PRO K 150 ? 0.721 1.294 1.128 -0.226 0.186  0.020  479 PRO KKK C   
13924 O O   . PRO K 150 ? 0.725 1.337 1.153 -0.220 0.209  0.008  479 PRO KKK O   
13925 C CB  . PRO K 150 ? 0.732 1.315 1.153 -0.274 0.176  0.055  479 PRO KKK CB  
13926 C CG  . PRO K 150 ? 0.743 1.381 1.187 -0.286 0.205  0.057  479 PRO KKK CG  
13927 C CD  . PRO K 150 ? 0.770 1.401 1.164 -0.288 0.225  0.055  479 PRO KKK CD  
13928 N N   . CYS K 151 ? 0.697 1.238 1.103 -0.211 0.162  0.016  480 CYS KKK N   
13929 C CA  . CYS K 151 ? 0.691 1.234 1.115 -0.184 0.161  -0.001 480 CYS KKK CA  
13930 C C   . CYS K 151 ? 0.657 1.232 1.142 -0.177 0.151  -0.003 480 CYS KKK C   
13931 O O   . CYS K 151 ? 0.647 1.236 1.159 -0.155 0.156  -0.016 480 CYS KKK O   
13932 C CB  . CYS K 151 ? 0.717 1.208 1.104 -0.172 0.141  -0.004 480 CYS KKK CB  
13933 S SG  . CYS K 151 ? 0.831 1.294 1.157 -0.172 0.155  -0.009 480 CYS KKK SG  
13934 N N   . ASN K 152 ? 0.635 1.220 1.141 -0.194 0.138  0.011  481 ASN KKK N   
13935 C CA  . ASN K 152 ? 0.628 1.246 1.193 -0.192 0.127  0.013  481 ASN KKK CA  
13936 C C   . ASN K 152 ? 0.600 1.204 1.178 -0.167 0.108  0.005  481 ASN KKK C   
13937 O O   . ASN K 152 ? 0.563 1.203 1.193 -0.155 0.109  0.000  481 ASN KKK O   
13938 C CB  . ASN K 152 ? 0.643 1.320 1.255 -0.193 0.153  0.008  481 ASN KKK CB  
13939 C CG  . ASN K 152 ? 0.655 1.372 1.331 -0.195 0.141  0.014  481 ASN KKK CG  
13940 O OD1 . ASN K 152 ? 0.705 1.411 1.381 -0.211 0.119  0.026  481 ASN KKK OD1 
13941 N ND2 . ASN K 152 ? 0.664 1.426 1.392 -0.179 0.155  0.004  481 ASN KKK ND2 
13942 N N   . GLY K 153 ? 0.624 1.179 1.157 -0.161 0.093  0.004  482 GLY KKK N   
13943 C CA  . GLY K 153 ? 0.629 1.164 1.166 -0.140 0.073  -0.001 482 GLY KKK CA  
13944 C C   . GLY K 153 ? 0.633 1.183 1.194 -0.116 0.087  -0.014 482 GLY KKK C   
13945 O O   . GLY K 153 ? 0.652 1.205 1.242 -0.100 0.071  -0.015 482 GLY KKK O   
13946 N N   . VAL K 154 ? 0.636 1.198 1.189 -0.113 0.114  -0.025 483 VAL KKK N   
13947 C CA  . VAL K 154 ? 0.615 1.188 1.188 -0.090 0.131  -0.042 483 VAL KKK CA  
13948 C C   . VAL K 154 ? 0.620 1.158 1.137 -0.087 0.144  -0.051 483 VAL KKK C   
13949 O O   . VAL K 154 ? 0.638 1.168 1.115 -0.105 0.152  -0.046 483 VAL KKK O   
13950 C CB  . VAL K 154 ? 0.614 1.243 1.237 -0.090 0.157  -0.049 483 VAL KKK CB  
13951 C CG1 . VAL K 154 ? 0.618 1.256 1.252 -0.069 0.180  -0.070 483 VAL KKK CG1 
13952 C CG2 . VAL K 154 ? 0.596 1.263 1.283 -0.089 0.143  -0.040 483 VAL KKK CG2 
13953 N N   . GLU K 155 ? 0.623 1.141 1.137 -0.066 0.143  -0.064 484 GLU KKK N   
13954 C CA  . GLU K 155 ? 0.631 1.118 1.097 -0.062 0.154  -0.076 484 GLU KKK CA  
13955 C C   . GLU K 155 ? 0.635 1.154 1.109 -0.061 0.187  -0.092 484 GLU KKK C   
13956 O O   . GLU K 155 ? 0.633 1.192 1.160 -0.052 0.199  -0.099 484 GLU KKK O   
13957 C CB  . GLU K 155 ? 0.650 1.106 1.117 -0.040 0.142  -0.083 484 GLU KKK CB  
13958 C CG  . GLU K 155 ? 0.653 1.087 1.121 -0.038 0.111  -0.068 484 GLU KKK CG  
13959 C CD  . GLU K 155 ? 0.678 1.070 1.122 -0.024 0.098  -0.072 484 GLU KKK CD  
13960 O OE1 . GLU K 155 ? 0.690 1.066 1.110 -0.019 0.113  -0.086 484 GLU KKK OE1 
13961 O OE2 . GLU K 155 ? 0.685 1.062 1.135 -0.020 0.074  -0.061 484 GLU KKK OE2 
13962 N N   . GLY K 156 ? 0.650 1.153 1.073 -0.069 0.202  -0.099 485 GLY KKK N   
13963 C CA  . GLY K 156 ? 0.696 1.227 1.116 -0.070 0.234  -0.116 485 GLY KKK CA  
13964 C C   . GLY K 156 ? 0.759 1.270 1.114 -0.086 0.242  -0.116 485 GLY KKK C   
13965 O O   . GLY K 156 ? 0.782 1.252 1.098 -0.091 0.222  -0.105 485 GLY KKK O   
13966 N N   . PHE K 157 ? 0.873 1.413 1.216 -0.095 0.270  -0.126 486 PHE KKK N   
13967 C CA  . PHE K 157 ? 0.943 1.473 1.225 -0.114 0.280  -0.123 486 PHE KKK CA  
13968 C C   . PHE K 157 ? 0.898 1.412 1.156 -0.135 0.260  -0.094 486 PHE KKK C   
13969 O O   . PHE K 157 ? 0.861 1.397 1.150 -0.145 0.257  -0.079 486 PHE KKK O   
13970 C CB  . PHE K 157 ? 1.052 1.628 1.335 -0.123 0.314  -0.136 486 PHE KKK CB  
13971 C CG  . PHE K 157 ? 1.148 1.725 1.372 -0.145 0.326  -0.130 486 PHE KKK CG  
13972 C CD1 . PHE K 157 ? 1.154 1.690 1.321 -0.149 0.314  -0.128 486 PHE KKK CD1 
13973 C CD2 . PHE K 157 ? 1.232 1.854 1.456 -0.164 0.351  -0.127 486 PHE KKK CD2 
13974 C CE1 . PHE K 157 ? 1.203 1.742 1.316 -0.171 0.323  -0.120 486 PHE KKK CE1 
13975 C CE2 . PHE K 157 ? 1.255 1.880 1.422 -0.186 0.362  -0.120 486 PHE KKK CE2 
13976 C CZ  . PHE K 157 ? 1.263 1.845 1.374 -0.189 0.347  -0.116 486 PHE KKK CZ  
13977 N N   . ASN K 158 ? 0.889 1.361 1.097 -0.140 0.246  -0.086 487 ASN KKK N   
13978 C CA  . ASN K 158 ? 0.874 1.323 1.055 -0.158 0.227  -0.060 487 ASN KKK CA  
13979 C C   . ASN K 158 ? 0.809 1.246 1.023 -0.153 0.203  -0.049 487 ASN KKK C   
13980 O O   . ASN K 158 ? 0.782 1.206 0.984 -0.169 0.190  -0.029 487 ASN KKK O   
13981 C CB  . ASN K 158 ? 0.907 1.382 1.073 -0.183 0.241  -0.046 487 ASN KKK CB  
13982 C CG  . ASN K 158 ? 0.948 1.429 1.067 -0.192 0.260  -0.052 487 ASN KKK CG  
13983 O OD1 . ASN K 158 ? 0.943 1.392 1.024 -0.187 0.252  -0.057 487 ASN KKK OD1 
13984 N ND2 . ASN K 158 ? 1.004 1.527 1.126 -0.206 0.284  -0.053 487 ASN KKK ND2 
13985 N N   . CYS K 159 ? 0.779 1.218 1.031 -0.133 0.197  -0.060 488 CYS KKK N   
13986 C CA  . CYS K 159 ? 0.754 1.187 1.039 -0.129 0.175  -0.050 488 CYS KKK CA  
13987 C C   . CYS K 159 ? 0.728 1.132 1.016 -0.108 0.159  -0.059 488 CYS KKK C   
13988 O O   . CYS K 159 ? 0.747 1.166 1.073 -0.091 0.162  -0.070 488 CYS KKK O   
13989 C CB  . CYS K 159 ? 0.743 1.222 1.084 -0.129 0.183  -0.051 488 CYS KKK CB  
13990 S SG  . CYS K 159 ? 0.740 1.248 1.083 -0.159 0.192  -0.032 488 CYS KKK SG  
13991 N N   . TYR K 160 ? 0.718 1.081 0.966 -0.109 0.143  -0.053 489 TYR KKK N   
13992 C CA  . TYR K 160 ? 0.711 1.043 0.949 -0.091 0.132  -0.062 489 TYR KKK CA  
13993 C C   . TYR K 160 ? 0.677 0.991 0.927 -0.087 0.107  -0.051 489 TYR KKK C   
13994 O O   . TYR K 160 ? 0.673 0.979 0.914 -0.101 0.095  -0.037 489 TYR KKK O   
13995 C CB  . TYR K 160 ? 0.725 1.028 0.911 -0.096 0.134  -0.064 489 TYR KKK CB  
13996 C CG  . TYR K 160 ? 0.776 1.098 0.943 -0.103 0.158  -0.073 489 TYR KKK CG  
13997 C CD1 . TYR K 160 ? 0.798 1.146 0.990 -0.092 0.177  -0.092 489 TYR KKK CD1 
13998 C CD2 . TYR K 160 ? 0.829 1.145 0.956 -0.121 0.161  -0.063 489 TYR KKK CD2 
13999 C CE1 . TYR K 160 ? 0.833 1.201 1.005 -0.100 0.201  -0.103 489 TYR KKK CE1 
14000 C CE2 . TYR K 160 ? 0.836 1.172 0.942 -0.130 0.183  -0.070 489 TYR KKK CE2 
14001 C CZ  . TYR K 160 ? 0.857 1.220 0.984 -0.120 0.204  -0.091 489 TYR KKK CZ  
14002 O OH  . TYR K 160 ? 0.919 1.304 1.023 -0.129 0.227  -0.101 489 TYR KKK OH  
14003 N N   . PHE K 161 ? 0.649 0.957 0.921 -0.069 0.099  -0.058 490 PHE KKK N   
14004 C CA  . PHE K 161 ? 0.623 0.906 0.894 -0.063 0.075  -0.050 490 PHE KKK CA  
14005 C C   . PHE K 161 ? 0.628 0.874 0.849 -0.068 0.068  -0.047 490 PHE KKK C   
14006 O O   . PHE K 161 ? 0.609 0.844 0.808 -0.065 0.079  -0.056 490 PHE KKK O   
14007 C CB  . PHE K 161 ? 0.605 0.889 0.907 -0.043 0.070  -0.057 490 PHE KKK CB  
14008 C CG  . PHE K 161 ? 0.595 0.861 0.900 -0.038 0.045  -0.047 490 PHE KKK CG  
14009 C CD1 . PHE K 161 ? 0.586 0.869 0.917 -0.043 0.031  -0.036 490 PHE KKK CD1 
14010 C CD2 . PHE K 161 ? 0.592 0.825 0.872 -0.031 0.036  -0.048 490 PHE KKK CD2 
14011 C CE1 . PHE K 161 ? 0.583 0.850 0.912 -0.040 0.008  -0.027 490 PHE KKK CE1 
14012 C CE2 . PHE K 161 ? 0.581 0.798 0.860 -0.028 0.014  -0.037 490 PHE KKK CE2 
14013 C CZ  . PHE K 161 ? 0.572 0.808 0.876 -0.032 0.001  -0.028 490 PHE KKK CZ  
14014 N N   . PRO K 162 ? 0.617 0.845 0.820 -0.078 0.052  -0.035 491 PRO KKK N   
14015 C CA  . PRO K 162 ? 0.631 0.829 0.790 -0.085 0.049  -0.031 491 PRO KKK CA  
14016 C C   . PRO K 162 ? 0.625 0.793 0.764 -0.074 0.040  -0.035 491 PRO KKK C   
14017 O O   . PRO K 162 ? 0.635 0.783 0.741 -0.078 0.040  -0.033 491 PRO KKK O   
14018 C CB  . PRO K 162 ? 0.636 0.828 0.793 -0.098 0.036  -0.019 491 PRO KKK CB  
14019 C CG  . PRO K 162 ? 0.628 0.834 0.818 -0.092 0.024  -0.018 491 PRO KKK CG  
14020 C CD  . PRO K 162 ? 0.634 0.869 0.858 -0.082 0.036  -0.026 491 PRO KKK CD  
14021 N N   . LEU K 163 ? 0.596 0.765 0.758 -0.060 0.033  -0.038 492 LEU KKK N   
14022 C CA  . LEU K 163 ? 0.604 0.745 0.749 -0.051 0.024  -0.039 492 LEU KKK CA  
14023 C C   . LEU K 163 ? 0.621 0.763 0.772 -0.040 0.036  -0.053 492 LEU KKK C   
14024 O O   . LEU K 163 ? 0.646 0.810 0.828 -0.034 0.046  -0.060 492 LEU KKK O   
14025 C CB  . LEU K 163 ? 0.598 0.737 0.761 -0.045 0.006  -0.032 492 LEU KKK CB  
14026 C CG  . LEU K 163 ? 0.572 0.710 0.728 -0.055 -0.007 -0.022 492 LEU KKK CG  
14027 C CD1 . LEU K 163 ? 0.565 0.696 0.727 -0.050 -0.025 -0.016 492 LEU KKK CD1 
14028 C CD2 . LEU K 163 ? 0.570 0.686 0.689 -0.065 -0.007 -0.020 492 LEU KKK CD2 
14029 N N   . GLN K 164 ? 0.647 0.765 0.771 -0.038 0.036  -0.056 493 GLN KKK N   
14030 C CA  . GLN K 164 ? 0.675 0.786 0.798 -0.029 0.046  -0.070 493 GLN KKK CA  
14031 C C   . GLN K 164 ? 0.637 0.722 0.755 -0.021 0.032  -0.068 493 GLN KKK C   
14032 O O   . GLN K 164 ? 0.629 0.698 0.728 -0.026 0.020  -0.057 493 GLN KKK O   
14033 C CB  . GLN K 164 ? 0.734 0.846 0.827 -0.039 0.060  -0.077 493 GLN KKK CB  
14034 C CG  . GLN K 164 ? 0.818 0.924 0.907 -0.032 0.071  -0.095 493 GLN KKK CG  
14035 C CD  . GLN K 164 ? 0.875 1.003 1.001 -0.022 0.084  -0.109 493 GLN KKK CD  
14036 O OE1 . GLN K 164 ? 0.890 1.012 1.044 -0.008 0.081  -0.115 493 GLN KKK OE1 
14037 N NE2 . GLN K 164 ? 0.927 1.084 1.057 -0.029 0.099  -0.112 493 GLN KKK NE2 
14038 N N   . SER K 165 ? 0.646 0.726 0.782 -0.009 0.036  -0.078 494 SER KKK N   
14039 C CA  . SER K 165 ? 0.637 0.691 0.773 -0.002 0.024  -0.076 494 SER KKK CA  
14040 C C   . SER K 165 ? 0.656 0.690 0.759 -0.006 0.029  -0.084 494 SER KKK C   
14041 O O   . SER K 165 ? 0.692 0.733 0.785 -0.010 0.044  -0.097 494 SER KKK O   
14042 C CB  . SER K 165 ? 0.663 0.721 0.840 0.013  0.025  -0.082 494 SER KKK CB  
14043 O OG  . SER K 165 ? 0.725 0.758 0.902 0.019  0.013  -0.077 494 SER KKK OG  
14044 N N   . TYR K 166 ? 0.658 0.669 0.745 -0.008 0.017  -0.076 495 TYR KKK N   
14045 C CA  . TYR K 166 ? 0.644 0.636 0.703 -0.012 0.018  -0.083 495 TYR KKK CA  
14046 C C   . TYR K 166 ? 0.662 0.643 0.738 -0.003 0.024  -0.098 495 TYR KKK C   
14047 O O   . TYR K 166 ? 0.689 0.664 0.746 -0.007 0.032  -0.112 495 TYR KKK O   
14048 C CB  . TYR K 166 ? 0.634 0.609 0.676 -0.017 0.004  -0.069 495 TYR KKK CB  
14049 C CG  . TYR K 166 ? 0.604 0.583 0.620 -0.028 0.002  -0.060 495 TYR KKK CG  
14050 C CD1 . TYR K 166 ? 0.606 0.585 0.597 -0.036 0.009  -0.064 495 TYR KKK CD1 
14051 C CD2 . TYR K 166 ? 0.584 0.568 0.602 -0.030 -0.006 -0.046 495 TYR KKK CD2 
14052 C CE1 . TYR K 166 ? 0.605 0.586 0.577 -0.045 0.006  -0.055 495 TYR KKK CE1 
14053 C CE2 . TYR K 166 ? 0.591 0.576 0.589 -0.039 -0.008 -0.040 495 TYR KKK CE2 
14054 C CZ  . TYR K 166 ? 0.596 0.579 0.572 -0.046 -0.002 -0.043 495 TYR KKK CZ  
14055 O OH  . TYR K 166 ? 0.590 0.573 0.551 -0.054 -0.004 -0.035 495 TYR KKK OH  
14056 N N   . GLY K 167 ? 0.692 0.668 0.801 0.009  0.018  -0.096 496 GLY KKK N   
14057 C CA  . GLY K 167 ? 0.753 0.714 0.881 0.018  0.022  -0.111 496 GLY KKK CA  
14058 C C   . GLY K 167 ? 0.755 0.689 0.857 0.012  0.017  -0.113 496 GLY KKK C   
14059 O O   . GLY K 167 ? 0.795 0.725 0.879 0.007  0.027  -0.131 496 GLY KKK O   
14060 N N   . PHE K 168 ? 0.743 0.662 0.842 0.010  0.002  -0.096 497 PHE KKK N   
14061 C CA  . PHE K 168 ? 0.754 0.651 0.831 0.002  -0.005 -0.094 497 PHE KKK CA  
14062 C C   . PHE K 168 ? 0.782 0.655 0.882 0.010  -0.007 -0.103 497 PHE KKK C   
14063 O O   . PHE K 168 ? 0.772 0.638 0.900 0.019  -0.016 -0.092 497 PHE KKK O   
14064 C CB  . PHE K 168 ? 0.732 0.626 0.798 -0.003 -0.019 -0.071 497 PHE KKK CB  
14065 C CG  . PHE K 168 ? 0.699 0.609 0.740 -0.012 -0.018 -0.064 497 PHE KKK CG  
14066 C CD1 . PHE K 168 ? 0.709 0.621 0.723 -0.021 -0.012 -0.071 497 PHE KKK CD1 
14067 C CD2 . PHE K 168 ? 0.666 0.589 0.711 -0.012 -0.024 -0.050 497 PHE KKK CD2 
14068 C CE1 . PHE K 168 ? 0.674 0.598 0.668 -0.029 -0.012 -0.063 497 PHE KKK CE1 
14069 C CE2 . PHE K 168 ? 0.641 0.575 0.666 -0.020 -0.023 -0.044 497 PHE KKK CE2 
14070 C CZ  . PHE K 168 ? 0.667 0.601 0.668 -0.027 -0.017 -0.050 497 PHE KKK CZ  
14071 N N   . GLN K 169 ? 0.813 0.672 0.899 0.006  -0.000 -0.121 498 GLN KKK N   
14072 C CA  . GLN K 169 ? 0.859 0.691 0.965 0.011  -0.003 -0.132 498 GLN KKK CA  
14073 C C   . GLN K 169 ? 0.862 0.674 0.945 -0.001 -0.012 -0.126 498 GLN KKK C   
14074 O O   . GLN K 169 ? 0.852 0.672 0.903 -0.013 -0.010 -0.128 498 GLN KKK O   
14075 C CB  . GLN K 169 ? 0.905 0.737 1.018 0.017  0.013  -0.162 498 GLN KKK CB  
14076 C CG  . GLN K 169 ? 0.924 0.779 1.065 0.029  0.023  -0.165 498 GLN KKK CG  
14077 C CD  . GLN K 169 ? 0.958 0.825 1.096 0.031  0.043  -0.194 498 GLN KKK CD  
14078 O OE1 . GLN K 169 ? 1.003 0.854 1.161 0.039  0.050  -0.215 498 GLN KKK OE1 
14079 N NE2 . GLN K 169 ? 0.966 0.860 1.079 0.023  0.053  -0.196 498 GLN KKK NE2 
14080 N N   . PRO K 170 ? 0.885 0.672 0.987 0.001  -0.023 -0.119 499 PRO KKK N   
14081 C CA  . PRO K 170 ? 0.862 0.632 0.946 -0.011 -0.032 -0.111 499 PRO KKK CA  
14082 C C   . PRO K 170 ? 0.834 0.598 0.894 -0.021 -0.026 -0.133 499 PRO KKK C   
14083 O O   . PRO K 170 ? 0.802 0.565 0.840 -0.034 -0.032 -0.126 499 PRO KKK O   
14084 C CB  . PRO K 170 ? 0.886 0.629 1.002 -0.006 -0.043 -0.102 499 PRO KKK CB  
14085 C CG  . PRO K 170 ? 0.908 0.648 1.059 0.012  -0.037 -0.114 499 PRO KKK CG  
14086 C CD  . PRO K 170 ? 0.890 0.663 1.033 0.016  -0.026 -0.117 499 PRO KKK CD  
14087 N N   . THR K 171 ? 0.815 0.578 0.880 -0.016 -0.013 -0.160 500 THR KKK N   
14088 C CA  . THR K 171 ? 0.828 0.586 0.868 -0.026 -0.007 -0.184 500 THR KKK CA  
14089 C C   . THR K 171 ? 0.816 0.602 0.820 -0.035 0.001  -0.187 500 THR KKK C   
14090 O O   . THR K 171 ? 0.831 0.617 0.809 -0.046 0.004  -0.202 500 THR KKK O   
14091 C CB  . THR K 171 ? 0.835 0.576 0.894 -0.018 0.004  -0.213 500 THR KKK CB  
14092 O OG1 . THR K 171 ? 0.850 0.611 0.928 -0.004 0.015  -0.217 500 THR KKK OG1 
14093 C CG2 . THR K 171 ? 0.841 0.548 0.933 -0.013 -0.006 -0.211 500 THR KKK CG2 
14094 N N   . ASN K 172 ? 0.804 0.615 0.807 -0.031 0.004  -0.172 501 ASN KKK N   
14095 C CA  . ASN K 172 ? 0.805 0.641 0.776 -0.040 0.009  -0.169 501 ASN KKK CA  
14096 C C   . ASN K 172 ? 0.792 0.624 0.734 -0.055 -0.001 -0.163 501 ASN KKK C   
14097 O O   . ASN K 172 ? 0.829 0.648 0.779 -0.058 -0.012 -0.149 501 ASN KKK O   
14098 C CB  . ASN K 172 ? 0.809 0.664 0.785 -0.036 0.007  -0.148 501 ASN KKK CB  
14099 C CG  . ASN K 172 ? 0.835 0.703 0.836 -0.023 0.017  -0.153 501 ASN KKK CG  
14100 O OD1 . ASN K 172 ? 0.872 0.735 0.888 -0.017 0.027  -0.173 501 ASN KKK OD1 
14101 N ND2 . ASN K 172 ? 0.819 0.704 0.828 -0.020 0.014  -0.136 501 ASN KKK ND2 
14102 N N   . GLY K 173 ? 0.771 0.619 0.683 -0.066 0.004  -0.170 502 GLY KKK N   
14103 C CA  . GLY K 173 ? 0.733 0.585 0.620 -0.080 -0.006 -0.158 502 GLY KKK CA  
14104 C C   . GLY K 173 ? 0.719 0.580 0.611 -0.078 -0.014 -0.131 502 GLY KKK C   
14105 O O   . GLY K 173 ? 0.704 0.573 0.611 -0.068 -0.010 -0.123 502 GLY KKK O   
14106 N N   . VAL K 174 ? 0.714 0.574 0.596 -0.086 -0.025 -0.118 503 VAL KKK N   
14107 C CA  . VAL K 174 ? 0.673 0.539 0.564 -0.085 -0.032 -0.095 503 VAL KKK CA  
14108 C C   . VAL K 174 ? 0.663 0.548 0.548 -0.081 -0.027 -0.087 503 VAL KKK C   
14109 O O   . VAL K 174 ? 0.641 0.529 0.540 -0.074 -0.028 -0.074 503 VAL KKK O   
14110 C CB  . VAL K 174 ? 0.678 0.544 0.560 -0.095 -0.043 -0.085 503 VAL KKK CB  
14111 C CG1 . VAL K 174 ? 0.704 0.586 0.563 -0.104 -0.045 -0.084 503 VAL KKK CG1 
14112 C CG2 . VAL K 174 ? 0.664 0.534 0.558 -0.092 -0.048 -0.065 503 VAL KKK CG2 
14113 N N   . GLY K 175 ? 0.691 0.589 0.556 -0.087 -0.022 -0.093 504 GLY KKK N   
14114 C CA  . GLY K 175 ? 0.663 0.577 0.522 -0.086 -0.017 -0.085 504 GLY KKK CA  
14115 C C   . GLY K 175 ? 0.661 0.578 0.538 -0.076 -0.008 -0.088 504 GLY KKK C   
14116 O O   . GLY K 175 ? 0.632 0.560 0.512 -0.074 -0.007 -0.076 504 GLY KKK O   
14117 N N   . TYR K 176 ? 0.700 0.608 0.591 -0.069 -0.003 -0.102 505 TYR KKK N   
14118 C CA  . TYR K 176 ? 0.724 0.637 0.638 -0.058 0.004  -0.105 505 TYR KKK CA  
14119 C C   . TYR K 176 ? 0.679 0.579 0.619 -0.049 -0.004 -0.097 505 TYR KKK C   
14120 O O   . TYR K 176 ? 0.676 0.578 0.639 -0.040 -0.000 -0.098 505 TYR KKK O   
14121 C CB  . TYR K 176 ? 0.779 0.695 0.695 -0.056 0.017  -0.127 505 TYR KKK CB  
14122 C CG  . TYR K 176 ? 0.861 0.795 0.752 -0.065 0.026  -0.134 505 TYR KKK CG  
14123 C CD1 . TYR K 176 ? 0.884 0.838 0.777 -0.064 0.035  -0.129 505 TYR KKK CD1 
14124 C CD2 . TYR K 176 ? 0.897 0.829 0.760 -0.076 0.026  -0.144 505 TYR KKK CD2 
14125 C CE1 . TYR K 176 ? 0.904 0.875 0.774 -0.074 0.044  -0.134 505 TYR KKK CE1 
14126 C CE2 . TYR K 176 ? 0.933 0.882 0.769 -0.086 0.034  -0.148 505 TYR KKK CE2 
14127 C CZ  . TYR K 176 ? 0.968 0.937 0.808 -0.085 0.044  -0.143 505 TYR KKK CZ  
14128 O OH  . TYR K 176 ? 1.041 1.028 0.854 -0.096 0.052  -0.144 505 TYR KKK OH  
14129 N N   . GLN K 177 ? 0.659 0.547 0.595 -0.053 -0.014 -0.086 506 GLN KKK N   
14130 C CA  . GLN K 177 ? 0.619 0.496 0.575 -0.047 -0.022 -0.075 506 GLN KKK CA  
14131 C C   . GLN K 177 ? 0.579 0.469 0.536 -0.046 -0.026 -0.058 506 GLN KKK C   
14132 O O   . GLN K 177 ? 0.561 0.462 0.502 -0.051 -0.025 -0.053 506 GLN KKK O   
14133 C CB  . GLN K 177 ? 0.620 0.482 0.573 -0.054 -0.031 -0.070 506 GLN KKK CB  
14134 C CG  . GLN K 177 ? 0.640 0.483 0.600 -0.053 -0.029 -0.087 506 GLN KKK CG  
14135 C CD  . GLN K 177 ? 0.631 0.460 0.588 -0.062 -0.038 -0.083 506 GLN KKK CD  
14136 O OE1 . GLN K 177 ? 0.639 0.469 0.597 -0.065 -0.045 -0.066 506 GLN KKK OE1 
14137 N NE2 . GLN K 177 ? 0.622 0.438 0.575 -0.066 -0.037 -0.101 506 GLN KKK NE2 
14138 N N   . PRO K 178 ? 0.588 0.475 0.563 -0.040 -0.031 -0.049 507 PRO KKK N   
14139 C CA  . PRO K 178 ? 0.581 0.480 0.554 -0.039 -0.034 -0.035 507 PRO KKK CA  
14140 C C   . PRO K 178 ? 0.582 0.479 0.540 -0.047 -0.040 -0.024 507 PRO KKK C   
14141 O O   . PRO K 178 ? 0.596 0.482 0.555 -0.049 -0.044 -0.022 507 PRO KKK O   
14142 C CB  . PRO K 178 ? 0.599 0.495 0.595 -0.032 -0.039 -0.028 507 PRO KKK CB  
14143 C CG  . PRO K 178 ? 0.617 0.493 0.623 -0.030 -0.042 -0.032 507 PRO KKK CG  
14144 C CD  . PRO K 178 ? 0.614 0.487 0.611 -0.033 -0.034 -0.050 507 PRO KKK CD  
14145 N N   . TYR K 179 ? 0.582 0.491 0.531 -0.049 -0.039 -0.019 508 TYR KKK N   
14146 C CA  . TYR K 179 ? 0.585 0.495 0.523 -0.054 -0.043 -0.009 508 TYR KKK CA  
14147 C C   . TYR K 179 ? 0.576 0.495 0.516 -0.052 -0.044 -0.002 508 TYR KKK C   
14148 O O   . TYR K 179 ? 0.560 0.487 0.503 -0.050 -0.042 -0.005 508 TYR KKK O   
14149 C CB  . TYR K 179 ? 0.594 0.509 0.520 -0.059 -0.040 -0.011 508 TYR KKK CB  
14150 C CG  . TYR K 179 ? 0.625 0.533 0.547 -0.064 -0.042 -0.015 508 TYR KKK CG  
14151 C CD1 . TYR K 179 ? 0.608 0.509 0.530 -0.064 -0.039 -0.027 508 TYR KKK CD1 
14152 C CD2 . TYR K 179 ? 0.604 0.513 0.522 -0.069 -0.045 -0.009 508 TYR KKK CD2 
14153 C CE1 . TYR K 179 ? 0.607 0.501 0.524 -0.070 -0.042 -0.032 508 TYR KKK CE1 
14154 C CE2 . TYR K 179 ? 0.603 0.506 0.518 -0.075 -0.048 -0.012 508 TYR KKK CE2 
14155 C CZ  . TYR K 179 ? 0.606 0.501 0.520 -0.076 -0.047 -0.024 508 TYR KKK CZ  
14156 O OH  . TYR K 179 ? 0.631 0.520 0.540 -0.083 -0.051 -0.029 508 TYR KKK OH  
14157 N N   . ARG K 180 ? 0.576 0.494 0.515 -0.054 -0.049 0.007  509 ARG KKK N   
14158 C CA  . ARG K 180 ? 0.568 0.494 0.502 -0.054 -0.050 0.013  509 ARG KKK CA  
14159 C C   . ARG K 180 ? 0.570 0.502 0.494 -0.057 -0.047 0.011  509 ARG KKK C   
14160 O O   . ARG K 180 ? 0.613 0.543 0.534 -0.060 -0.045 0.012  509 ARG KKK O   
14161 C CB  . ARG K 180 ? 0.608 0.532 0.542 -0.056 -0.056 0.024  509 ARG KKK CB  
14162 C CG  . ARG K 180 ? 0.629 0.549 0.578 -0.051 -0.062 0.027  509 ARG KKK CG  
14163 C CD  . ARG K 180 ? 0.636 0.554 0.586 -0.053 -0.069 0.041  509 ARG KKK CD  
14164 N NE  . ARG K 180 ? 0.662 0.576 0.631 -0.047 -0.075 0.044  509 ARG KKK NE  
14165 C CZ  . ARG K 180 ? 0.697 0.612 0.671 -0.047 -0.085 0.058  509 ARG KKK CZ  
14166 N NH1 . ARG K 180 ? 0.711 0.632 0.670 -0.054 -0.088 0.069  509 ARG KKK NH1 
14167 N NH2 . ARG K 180 ? 0.677 0.589 0.674 -0.040 -0.091 0.060  509 ARG KKK NH2 
14168 N N   . VAL K 181 ? 0.537 0.475 0.457 -0.057 -0.045 0.009  510 VAL KKK N   
14169 C CA  . VAL K 181 ? 0.535 0.476 0.449 -0.059 -0.042 0.007  510 VAL KKK CA  
14170 C C   . VAL K 181 ? 0.540 0.487 0.448 -0.060 -0.042 0.007  510 VAL KKK C   
14171 O O   . VAL K 181 ? 0.579 0.529 0.487 -0.060 -0.046 0.008  510 VAL KKK O   
14172 C CB  . VAL K 181 ? 0.507 0.448 0.423 -0.058 -0.039 0.002  510 VAL KKK CB  
14173 C CG1 . VAL K 181 ? 0.520 0.462 0.434 -0.059 -0.037 0.001  510 VAL KKK CG1 
14174 C CG2 . VAL K 181 ? 0.520 0.459 0.439 -0.058 -0.038 -0.000 510 VAL KKK CG2 
14175 N N   . VAL K 182 ? 0.532 0.482 0.436 -0.061 -0.039 0.006  511 VAL KKK N   
14176 C CA  . VAL K 182 ? 0.546 0.501 0.442 -0.062 -0.037 0.002  511 VAL KKK CA  
14177 C C   . VAL K 182 ? 0.545 0.497 0.445 -0.060 -0.032 -0.004 511 VAL KKK C   
14178 O O   . VAL K 182 ? 0.541 0.493 0.447 -0.059 -0.029 -0.002 511 VAL KKK O   
14179 C CB  . VAL K 182 ? 0.551 0.513 0.439 -0.065 -0.035 0.007  511 VAL KKK CB  
14180 C CG1 . VAL K 182 ? 0.582 0.550 0.460 -0.067 -0.031 -0.001 511 VAL KKK CG1 
14181 C CG2 . VAL K 182 ? 0.556 0.518 0.441 -0.068 -0.042 0.016  511 VAL KKK CG2 
14182 N N   . VAL K 183 ? 0.533 0.483 0.433 -0.061 -0.032 -0.011 512 VAL KKK N   
14183 C CA  . VAL K 183 ? 0.551 0.496 0.457 -0.059 -0.028 -0.017 512 VAL KKK CA  
14184 C C   . VAL K 183 ? 0.577 0.526 0.476 -0.060 -0.024 -0.026 512 VAL KKK C   
14185 O O   . VAL K 183 ? 0.580 0.531 0.469 -0.064 -0.027 -0.030 512 VAL KKK O   
14186 C CB  . VAL K 183 ? 0.564 0.502 0.476 -0.060 -0.031 -0.018 512 VAL KKK CB  
14187 C CG1 . VAL K 183 ? 0.571 0.500 0.492 -0.058 -0.028 -0.022 512 VAL KKK CG1 
14188 C CG2 . VAL K 183 ? 0.578 0.516 0.493 -0.060 -0.033 -0.011 512 VAL KKK CG2 
14189 N N   . LEU K 184 ? 0.567 0.517 0.470 -0.056 -0.017 -0.030 513 LEU KKK N   
14190 C CA  . LEU K 184 ? 0.601 0.555 0.498 -0.056 -0.010 -0.042 513 LEU KKK CA  
14191 C C   . LEU K 184 ? 0.613 0.555 0.525 -0.052 -0.008 -0.051 513 LEU KKK C   
14192 O O   . LEU K 184 ? 0.608 0.547 0.537 -0.047 -0.007 -0.047 513 LEU KKK O   
14193 C CB  . LEU K 184 ? 0.577 0.544 0.475 -0.055 -0.003 -0.041 513 LEU KKK CB  
14194 C CG  . LEU K 184 ? 0.566 0.543 0.452 -0.060 -0.005 -0.029 513 LEU KKK CG  
14195 C CD1 . LEU K 184 ? 0.576 0.566 0.467 -0.060 0.002  -0.026 513 LEU KKK CD1 
14196 C CD2 . LEU K 184 ? 0.584 0.565 0.449 -0.067 -0.009 -0.031 513 LEU KKK CD2 
14197 N N   . SER K 185 ? 0.608 0.544 0.513 -0.056 -0.010 -0.062 514 SER KKK N   
14198 C CA  . SER K 185 ? 0.648 0.569 0.565 -0.053 -0.008 -0.073 514 SER KKK CA  
14199 C C   . SER K 185 ? 0.675 0.600 0.589 -0.051 0.002  -0.090 514 SER KKK C   
14200 O O   . SER K 185 ? 0.679 0.614 0.572 -0.056 0.004  -0.096 514 SER KKK O   
14201 C CB  . SER K 185 ? 0.663 0.575 0.575 -0.060 -0.015 -0.077 514 SER KKK CB  
14202 O OG  . SER K 185 ? 0.671 0.578 0.592 -0.061 -0.021 -0.064 514 SER KKK OG  
14203 N N   . PHE K 186 ? 0.677 0.594 0.612 -0.043 0.009  -0.096 515 PHE KKK N   
14204 C CA  . PHE K 186 ? 0.700 0.619 0.636 -0.039 0.021  -0.115 515 PHE KKK CA  
14205 C C   . PHE K 186 ? 0.735 0.634 0.679 -0.039 0.020  -0.132 515 PHE KKK C   
14206 O O   . PHE K 186 ? 0.771 0.653 0.737 -0.034 0.015  -0.126 515 PHE KKK O   
14207 C CB  . PHE K 186 ? 0.691 0.619 0.650 -0.028 0.028  -0.112 515 PHE KKK CB  
14208 C CG  . PHE K 186 ? 0.691 0.638 0.645 -0.030 0.028  -0.096 515 PHE KKK CG  
14209 C CD1 . PHE K 186 ? 0.729 0.689 0.656 -0.039 0.027  -0.092 515 PHE KKK CD1 
14210 C CD2 . PHE K 186 ? 0.683 0.635 0.660 -0.023 0.028  -0.085 515 PHE KKK CD2 
14211 C CE1 . PHE K 186 ? 0.703 0.677 0.627 -0.041 0.026  -0.077 515 PHE KKK CE1 
14212 C CE2 . PHE K 186 ? 0.675 0.644 0.648 -0.026 0.027  -0.071 515 PHE KKK CE2 
14213 C CZ  . PHE K 186 ? 0.679 0.658 0.626 -0.034 0.027  -0.068 515 PHE KKK CZ  
14214 N N   . GLU K 187 ? 0.793 0.693 0.717 -0.045 0.023  -0.150 516 GLU KKK N   
14215 C CA  . GLU K 187 ? 0.874 0.753 0.802 -0.048 0.022  -0.168 516 GLU KKK CA  
14216 C C   . GLU K 187 ? 0.936 0.811 0.873 -0.040 0.036  -0.192 516 GLU KKK C   
14217 O O   . GLU K 187 ? 0.954 0.848 0.875 -0.040 0.047  -0.201 516 GLU KKK O   
14218 C CB  . GLU K 187 ? 0.925 0.808 0.823 -0.061 0.015  -0.173 516 GLU KKK CB  
14219 C CG  . GLU K 187 ? 0.980 0.841 0.884 -0.067 0.007  -0.185 516 GLU KKK CG  
14220 C CD  . GLU K 187 ? 1.012 0.878 0.888 -0.082 0.001  -0.195 516 GLU KKK CD  
14221 O OE1 . GLU K 187 ? 1.044 0.925 0.895 -0.085 0.007  -0.208 516 GLU KKK OE1 
14222 O OE2 . GLU K 187 ? 0.996 0.854 0.875 -0.090 -0.011 -0.191 516 GLU KKK OE2 
14223 N N   . LEU K 188 ? 1.013 0.864 0.978 -0.033 0.036  -0.199 517 LEU KKK N   
14224 C CA  . LEU K 188 ? 1.088 0.930 1.070 -0.024 0.049  -0.225 517 LEU KKK CA  
14225 C C   . LEU K 188 ? 1.090 0.904 1.075 -0.030 0.044  -0.242 517 LEU KKK C   
14226 O O   . LEU K 188 ? 1.083 0.874 1.096 -0.026 0.037  -0.235 517 LEU KKK O   
14227 C CB  . LEU K 188 ? 1.155 0.995 1.176 -0.009 0.054  -0.215 517 LEU KKK CB  
14228 C CG  . LEU K 188 ? 1.219 1.088 1.240 -0.002 0.068  -0.217 517 LEU KKK CG  
14229 C CD1 . LEU K 188 ? 1.230 1.101 1.292 0.013  0.069  -0.203 517 LEU KKK CD1 
14230 C CD2 . LEU K 188 ? 1.230 1.104 1.243 0.000  0.086  -0.250 517 LEU KKK CD2 
14231 N N   . LEU K 189 ? 1.101 0.919 1.056 -0.040 0.048  -0.265 518 LEU KKK N   
14232 C CA  . LEU K 189 ? 1.132 0.924 1.089 -0.045 0.047  -0.291 518 LEU KKK CA  
14233 C C   . LEU K 189 ? 1.196 0.985 1.166 -0.034 0.066  -0.320 518 LEU KKK C   
14234 O O   . LEU K 189 ? 1.212 1.027 1.180 -0.026 0.079  -0.319 518 LEU KKK O   
14235 C CB  . LEU K 189 ? 1.130 0.931 1.046 -0.064 0.039  -0.299 518 LEU KKK CB  
14236 C CG  . LEU K 189 ? 1.083 0.901 0.983 -0.073 0.025  -0.269 518 LEU KKK CG  
14237 C CD1 . LEU K 189 ? 1.090 0.923 0.951 -0.089 0.018  -0.277 518 LEU KKK CD1 
14238 C CD2 . LEU K 189 ? 1.044 0.842 0.969 -0.073 0.012  -0.249 518 LEU KKK CD2 
14239 N N   . HIS K 190 ? 1.277 1.037 1.264 -0.032 0.069  -0.346 519 HIS KKK N   
14240 C CA  . HIS K 190 ? 1.314 1.073 1.307 -0.022 0.089  -0.381 519 HIS KKK CA  
14241 C C   . HIS K 190 ? 1.307 1.081 1.251 -0.038 0.093  -0.406 519 HIS KKK C   
14242 O O   . HIS K 190 ? 1.381 1.134 1.315 -0.048 0.091  -0.431 519 HIS KKK O   
14243 C CB  . HIS K 190 ? 1.368 1.091 1.408 -0.009 0.092  -0.397 519 HIS KKK CB  
14244 C CG  . HIS K 190 ? 1.389 1.121 1.460 0.011  0.111  -0.408 519 HIS KKK CG  
14245 N ND1 . HIS K 190 ? 1.455 1.178 1.537 0.019  0.129  -0.448 519 HIS KKK ND1 
14246 C CD2 . HIS K 190 ? 1.325 1.077 1.420 0.024  0.115  -0.385 519 HIS KKK CD2 
14247 C CE1 . HIS K 190 ? 1.403 1.141 1.518 0.038  0.144  -0.448 519 HIS KKK CE1 
14248 N NE2 . HIS K 190 ? 1.356 1.112 1.479 0.041  0.135  -0.409 519 HIS KKK NE2 
14249 N N   . ALA K 191 ? 1.244 1.055 1.157 -0.042 0.098  -0.395 520 ALA KKK N   
14250 C CA  . ALA K 191 ? 1.223 1.058 1.084 -0.058 0.103  -0.410 520 ALA KKK CA  
14251 C C   . ALA K 191 ? 1.168 1.039 1.019 -0.052 0.119  -0.404 520 ALA KKK C   
14252 O O   . ALA K 191 ? 1.099 0.977 0.981 -0.038 0.122  -0.384 520 ALA KKK O   
14253 C CB  . ALA K 191 ? 1.211 1.052 1.045 -0.074 0.082  -0.387 520 ALA KKK CB  
14254 N N   . PRO K 192 ? 1.165 1.063 0.974 -0.062 0.130  -0.421 521 PRO KKK N   
14255 C CA  . PRO K 192 ? 1.125 1.058 0.922 -0.059 0.144  -0.410 521 PRO KKK CA  
14256 C C   . PRO K 192 ? 1.045 0.993 0.844 -0.061 0.130  -0.367 521 PRO KKK C   
14257 O O   . PRO K 192 ? 1.034 0.975 0.816 -0.072 0.110  -0.349 521 PRO KKK O   
14258 C CB  . PRO K 192 ? 1.166 1.121 0.908 -0.076 0.152  -0.432 521 PRO KKK CB  
14259 C CG  . PRO K 192 ? 1.207 1.134 0.946 -0.080 0.152  -0.469 521 PRO KKK CG  
14260 C CD  . PRO K 192 ? 1.192 1.086 0.962 -0.077 0.130  -0.452 521 PRO KKK CD  
14261 N N   . ALA K 193 ? 1.006 0.971 0.826 -0.050 0.140  -0.353 522 ALA KKK N   
14262 C CA  . ALA K 193 ? 0.960 0.940 0.782 -0.051 0.130  -0.315 522 ALA KKK CA  
14263 C C   . ALA K 193 ? 0.954 0.961 0.726 -0.068 0.127  -0.307 522 ALA KKK C   
14264 O O   . ALA K 193 ? 0.986 1.011 0.732 -0.074 0.143  -0.327 522 ALA KKK O   
14265 C CB  . ALA K 193 ? 0.942 0.936 0.798 -0.037 0.143  -0.307 522 ALA KKK CB  
14266 N N   . THR K 194 ? 0.942 0.950 0.701 -0.077 0.109  -0.278 523 THR KKK N   
14267 C CA  . THR K 194 ? 0.942 0.975 0.659 -0.092 0.104  -0.265 523 THR KKK CA  
14268 C C   . THR K 194 ? 0.889 0.937 0.617 -0.090 0.102  -0.232 523 THR KKK C   
14269 O O   . THR K 194 ? 0.910 0.982 0.609 -0.100 0.103  -0.220 523 THR KKK O   
14270 C CB  . THR K 194 ? 0.953 0.977 0.643 -0.106 0.084  -0.262 523 THR KKK CB  
14271 O OG1 . THR K 194 ? 0.903 0.914 0.614 -0.103 0.066  -0.236 523 THR KKK OG1 
14272 C CG2 . THR K 194 ? 0.982 0.987 0.667 -0.108 0.086  -0.295 523 THR KKK CG2 
14273 N N   . VAL K 195 ? 0.831 0.867 0.598 -0.077 0.098  -0.219 524 VAL KKK N   
14274 C CA  . VAL K 195 ? 0.810 0.858 0.589 -0.075 0.095  -0.190 524 VAL KKK CA  
14275 C C   . VAL K 195 ? 0.832 0.887 0.647 -0.061 0.111  -0.195 524 VAL KKK C   
14276 O O   . VAL K 195 ? 0.836 0.871 0.684 -0.049 0.110  -0.201 524 VAL KKK O   
14277 C CB  . VAL K 195 ? 0.767 0.798 0.560 -0.073 0.075  -0.168 524 VAL KKK CB  
14278 C CG1 . VAL K 195 ? 0.737 0.778 0.543 -0.071 0.073  -0.142 524 VAL KKK CG1 
14279 C CG2 . VAL K 195 ? 0.782 0.809 0.546 -0.086 0.059  -0.162 524 VAL KKK CG2 
14280 N N   . CYS K 196 ? 0.864 0.946 0.675 -0.063 0.125  -0.191 525 CYS KKK N   
14281 C CA  . CYS K 196 ? 0.869 0.965 0.715 -0.052 0.140  -0.194 525 CYS KKK CA  
14282 C C   . CYS K 196 ? 0.859 0.975 0.708 -0.057 0.139  -0.167 525 CYS KKK C   
14283 O O   . CYS K 196 ? 0.845 0.970 0.662 -0.070 0.132  -0.152 525 CYS KKK O   
14284 C CB  . CYS K 196 ? 0.917 1.031 0.757 -0.050 0.164  -0.223 525 CYS KKK CB  
14285 S SG  . CYS K 196 ? 0.978 1.065 0.827 -0.041 0.169  -0.259 525 CYS KKK SG  
14286 N N   . GLY K 197 ? 0.894 1.017 0.782 -0.046 0.143  -0.159 526 GLY KKK N   
14287 C CA  . GLY K 197 ? 0.925 1.071 0.822 -0.051 0.145  -0.138 526 GLY KKK CA  
14288 C C   . GLY K 197 ? 1.015 1.194 0.894 -0.059 0.166  -0.145 526 GLY KKK C   
14289 O O   . GLY K 197 ? 1.046 1.232 0.913 -0.058 0.181  -0.171 526 GLY KKK O   
14290 N N   . PRO K 198 ? 1.089 1.291 0.969 -0.067 0.169  -0.125 527 PRO KKK N   
14291 C CA  . PRO K 198 ? 1.142 1.379 1.008 -0.076 0.190  -0.129 527 PRO KKK CA  
14292 C C   . PRO K 198 ? 1.255 1.512 1.149 -0.064 0.214  -0.155 527 PRO KKK C   
14293 O O   . PRO K 198 ? 1.262 1.546 1.136 -0.071 0.235  -0.168 527 PRO KKK O   
14294 C CB  . PRO K 198 ? 1.095 1.347 0.976 -0.083 0.185  -0.100 527 PRO KKK CB  
14295 C CG  . PRO K 198 ? 1.066 1.288 0.950 -0.083 0.159  -0.080 527 PRO KKK CG  
14296 C CD  . PRO K 198 ? 1.044 1.238 0.941 -0.069 0.151  -0.097 527 PRO KKK CD  
14306 N N   . GLN L 1   ? 0.651 0.962 0.935 -0.179 -0.165 0.268  1   GLN LLL N   
14307 C CA  . GLN L 1   ? 0.623 0.890 0.906 -0.141 -0.139 0.246  1   GLN LLL CA  
14308 C C   . GLN L 1   ? 0.582 0.792 0.768 -0.145 -0.125 0.212  1   GLN LLL C   
14309 O O   . GLN L 1   ? 0.574 0.761 0.713 -0.158 -0.112 0.189  1   GLN LLL O   
14310 C CB  . GLN L 1   ? 0.672 0.938 1.015 -0.116 -0.110 0.235  1   GLN LLL CB  
14311 C CG  . GLN L 1   ? 0.748 0.966 1.082 -0.084 -0.080 0.210  1   GLN LLL CG  
14312 C CD  . GLN L 1   ? 0.777 0.992 1.141 -0.062 -0.082 0.223  1   GLN LLL CD  
14313 O OE1 . GLN L 1   ? 0.854 1.104 1.262 -0.064 -0.105 0.256  1   GLN LLL OE1 
14314 N NE2 . GLN L 1   ? 0.800 0.973 1.140 -0.043 -0.057 0.197  1   GLN LLL NE2 
14315 N N   . VAL L 2   ? 0.541 0.729 0.702 -0.134 -0.126 0.208  2   VAL LLL N   
14316 C CA  . VAL L 2   ? 0.540 0.676 0.630 -0.128 -0.109 0.176  2   VAL LLL CA  
14317 C C   . VAL L 2   ? 0.500 0.614 0.612 -0.092 -0.089 0.163  2   VAL LLL C   
14318 O O   . VAL L 2   ? 0.468 0.597 0.626 -0.078 -0.094 0.178  2   VAL LLL O   
14319 C CB  . VAL L 2   ? 0.573 0.703 0.617 -0.147 -0.124 0.180  2   VAL LLL CB  
14320 C CG1 . VAL L 2   ? 0.590 0.673 0.578 -0.137 -0.103 0.150  2   VAL LLL CG1 
14321 C CG2 . VAL L 2   ? 0.609 0.760 0.623 -0.191 -0.143 0.194  2   VAL LLL CG2 
14322 N N   . GLN L 3   ? 0.494 0.571 0.570 -0.081 -0.069 0.136  3   GLN LLL N   
14323 C CA  . GLN L 3   ? 0.474 0.529 0.554 -0.055 -0.054 0.123  3   GLN LLL CA  
14324 C C   . GLN L 3   ? 0.485 0.515 0.515 -0.052 -0.054 0.110  3   GLN LLL C   
14325 O O   . GLN L 3   ? 0.531 0.548 0.518 -0.067 -0.055 0.102  3   GLN LLL O   
14326 C CB  . GLN L 3   ? 0.465 0.499 0.543 -0.047 -0.033 0.107  3   GLN LLL CB  
14327 C CG  . GLN L 3   ? 0.447 0.505 0.590 -0.044 -0.025 0.118  3   GLN LLL CG  
14328 C CD  . GLN L 3   ? 0.476 0.507 0.611 -0.038 0.000  0.098  3   GLN LLL CD  
14329 O OE1 . GLN L 3   ? 0.483 0.486 0.594 -0.028 0.012  0.084  3   GLN LLL OE1 
14330 N NE2 . GLN L 3   ? 0.466 0.503 0.613 -0.050 0.008  0.097  3   GLN LLL NE2 
14331 N N   . LEU L 4   ? 0.451 0.477 0.492 -0.036 -0.050 0.106  4   LEU LLL N   
14332 C CA  . LEU L 4   ? 0.463 0.474 0.471 -0.032 -0.050 0.096  4   LEU LLL CA  
14333 C C   . LEU L 4   ? 0.459 0.455 0.467 -0.013 -0.038 0.083  4   LEU LLL C   
14334 O O   . LEU L 4   ? 0.467 0.468 0.505 -0.006 -0.032 0.086  4   LEU LLL O   
14335 C CB  . LEU L 4   ? 0.459 0.488 0.482 -0.038 -0.063 0.110  4   LEU LLL CB  
14336 C CG  . LEU L 4   ? 0.472 0.521 0.495 -0.063 -0.080 0.129  4   LEU LLL CG  
14337 C CD1 . LEU L 4   ? 0.462 0.528 0.505 -0.067 -0.094 0.148  4   LEU LLL CD1 
14338 C CD2 . LEU L 4   ? 0.497 0.529 0.465 -0.083 -0.078 0.117  4   LEU LLL CD2 
14339 N N   . VAL L 5   ? 0.465 0.443 0.440 -0.008 -0.035 0.070  5   VAL LLL N   
14340 C CA  . VAL L 5   ? 0.469 0.437 0.439 0.005  -0.029 0.061  5   VAL LLL CA  
14341 C C   . VAL L 5   ? 0.492 0.463 0.452 0.011  -0.032 0.056  5   VAL LLL C   
14342 O O   . VAL L 5   ? 0.510 0.471 0.453 0.011  -0.031 0.052  5   VAL LLL O   
14343 C CB  . VAL L 5   ? 0.488 0.436 0.438 0.008  -0.023 0.056  5   VAL LLL CB  
14344 C CG1 . VAL L 5   ? 0.485 0.426 0.423 0.015  -0.023 0.051  5   VAL LLL CG1 
14345 C CG2 . VAL L 5   ? 0.500 0.446 0.465 0.001  -0.015 0.058  5   VAL LLL CG2 
14346 N N   . GLU L 6   ? 0.484 0.466 0.457 0.014  -0.033 0.055  6   GLU LLL N   
14347 C CA  . GLU L 6   ? 0.490 0.481 0.460 0.018  -0.035 0.049  6   GLU LLL CA  
14348 C C   . GLU L 6   ? 0.514 0.502 0.475 0.027  -0.036 0.045  6   GLU LLL C   
14349 O O   . GLU L 6   ? 0.531 0.510 0.485 0.025  -0.035 0.046  6   GLU LLL O   
14350 C CB  . GLU L 6   ? 0.493 0.496 0.477 0.014  -0.034 0.049  6   GLU LLL CB  
14351 C CG  . GLU L 6   ? 0.490 0.497 0.487 0.005  -0.036 0.059  6   GLU LLL CG  
14352 C CD  . GLU L 6   ? 0.497 0.502 0.517 0.005  -0.032 0.069  6   GLU LLL CD  
14353 O OE1 . GLU L 6   ? 0.489 0.485 0.508 0.009  -0.025 0.064  6   GLU LLL OE1 
14354 O OE2 . GLU L 6   ? 0.497 0.508 0.538 0.001  -0.035 0.081  6   GLU LLL OE2 
14355 N N   . SER L 7   ? 0.522 0.518 0.487 0.035  -0.038 0.043  7   SER LLL N   
14356 C CA  . SER L 7   ? 0.542 0.546 0.509 0.044  -0.045 0.046  7   SER LLL CA  
14357 C C   . SER L 7   ? 0.553 0.581 0.542 0.049  -0.046 0.042  7   SER LLL C   
14358 O O   . SER L 7   ? 0.572 0.602 0.567 0.044  -0.037 0.036  7   SER LLL O   
14359 C CB  . SER L 7   ? 0.554 0.539 0.511 0.053  -0.046 0.052  7   SER LLL CB  
14360 O OG  . SER L 7   ? 0.553 0.526 0.514 0.058  -0.037 0.049  7   SER LLL OG  
14361 N N   . GLY L 8   ? 0.593 0.641 0.594 0.055  -0.056 0.048  8   GLY LLL N   
14362 C CA  . GLY L 8   ? 0.611 0.689 0.644 0.061  -0.056 0.047  8   GLY LLL CA  
14363 C C   . GLY L 8   ? 0.622 0.725 0.657 0.047  -0.060 0.040  8   GLY LLL C   
14364 O O   . GLY L 8   ? 0.651 0.784 0.715 0.050  -0.059 0.038  8   GLY LLL O   
14365 N N   . GLY L 9   ? 0.625 0.717 0.635 0.032  -0.059 0.037  9   GLY LLL N   
14366 C CA  . GLY L 9   ? 0.672 0.781 0.681 0.016  -0.058 0.029  9   GLY LLL CA  
14367 C C   . GLY L 9   ? 0.674 0.809 0.681 0.007  -0.072 0.035  9   GLY LLL C   
14368 O O   . GLY L 9   ? 0.735 0.878 0.747 0.016  -0.086 0.047  9   GLY LLL O   
14369 N N   . GLY L 10  ? 0.652 0.800 0.650 -0.012 -0.069 0.026  10  GLY LLL N   
14370 C CA  . GLY L 10  ? 0.669 0.843 0.656 -0.031 -0.083 0.030  10  GLY LLL CA  
14371 C C   . GLY L 10  ? 0.660 0.870 0.665 -0.043 -0.083 0.023  10  GLY LLL C   
14372 O O   . GLY L 10  ? 0.644 0.847 0.658 -0.041 -0.068 0.011  10  GLY LLL O   
14373 N N   . LEU L 11  ? 0.675 0.922 0.680 -0.059 -0.102 0.030  11  LEU LLL N   
14374 C CA  . LEU L 11  ? 0.691 0.980 0.710 -0.079 -0.104 0.024  11  LEU LLL CA  
14375 C C   . LEU L 11  ? 0.674 1.006 0.754 -0.055 -0.112 0.031  11  LEU LLL C   
14376 O O   . LEU L 11  ? 0.697 1.042 0.806 -0.033 -0.126 0.049  11  LEU LLL O   
14377 C CB  . LEU L 11  ? 0.727 1.040 0.717 -0.111 -0.124 0.032  11  LEU LLL CB  
14378 C CG  . LEU L 11  ? 0.759 1.121 0.757 -0.139 -0.131 0.027  11  LEU LLL CG  
14379 C CD1 . LEU L 11  ? 0.754 1.091 0.736 -0.153 -0.101 0.001  11  LEU LLL CD1 
14380 C CD2 . LEU L 11  ? 0.791 1.170 0.746 -0.179 -0.151 0.036  11  LEU LLL CD2 
14381 N N   . VAL L 12  ? 0.660 1.011 0.761 -0.060 -0.098 0.017  12  VAL LLL N   
14382 C CA  . VAL L 12  ? 0.633 1.025 0.796 -0.042 -0.098 0.019  12  VAL LLL CA  
14383 C C   . VAL L 12  ? 0.606 1.032 0.778 -0.066 -0.090 0.004  12  VAL LLL C   
14384 O O   . VAL L 12  ? 0.583 0.977 0.708 -0.089 -0.076 -0.012 12  VAL LLL O   
14385 C CB  . VAL L 12  ? 0.624 0.980 0.799 -0.016 -0.077 0.013  12  VAL LLL CB  
14386 C CG1 . VAL L 12  ? 0.636 0.955 0.778 -0.029 -0.054 -0.008 12  VAL LLL CG1 
14387 C CG2 . VAL L 12  ? 0.618 1.008 0.859 0.005  -0.071 0.015  12  VAL LLL CG2 
14388 N N   . GLN L 13  ? 0.595 1.081 0.826 -0.061 -0.099 0.011  13  GLN LLL N   
14389 C CA  . GLN L 13  ? 0.592 1.118 0.837 -0.086 -0.092 -0.004 13  GLN LLL CA  
14390 C C   . GLN L 13  ? 0.546 1.046 0.799 -0.080 -0.060 -0.026 13  GLN LLL C   
14391 O O   . GLN L 13  ? 0.523 1.002 0.799 -0.053 -0.048 -0.025 13  GLN LLL O   
14392 C CB  . GLN L 13  ? 0.623 1.231 0.935 -0.087 -0.115 0.014  13  GLN LLL CB  
14393 C CG  . GLN L 13  ? 0.633 1.271 1.028 -0.048 -0.116 0.030  13  GLN LLL CG  
14394 C CD  . GLN L 13  ? 0.649 1.377 1.123 -0.050 -0.138 0.049  13  GLN LLL CD  
14395 O OE1 . GLN L 13  ? 0.655 1.425 1.162 -0.065 -0.128 0.035  13  GLN LLL OE1 
14396 N NE2 . GLN L 13  ? 0.651 1.410 1.163 -0.032 -0.170 0.084  13  GLN LLL NE2 
14397 N N   . ALA L 14  ? 0.532 1.026 0.755 -0.108 -0.044 -0.046 14  ALA LLL N   
14398 C CA  . ALA L 14  ? 0.513 0.988 0.737 -0.112 -0.015 -0.067 14  ALA LLL CA  
14399 C C   . ALA L 14  ? 0.489 1.002 0.786 -0.091 -0.006 -0.067 14  ALA LLL C   
14400 O O   . ALA L 14  ? 0.464 1.041 0.821 -0.084 -0.023 -0.054 14  ALA LLL O   
14401 C CB  . ALA L 14  ? 0.533 1.017 0.732 -0.148 -0.006 -0.084 14  ALA LLL CB  
14402 N N   . GLY L 15  ? 0.476 0.950 0.768 -0.082 0.020  -0.080 15  GLY LLL N   
14403 C CA  . GLY L 15  ? 0.469 0.963 0.825 -0.063 0.038  -0.085 15  GLY LLL CA  
14404 C C   . GLY L 15  ? 0.476 0.960 0.858 -0.029 0.030  -0.066 15  GLY LLL C   
14405 O O   . GLY L 15  ? 0.489 0.973 0.918 -0.011 0.052  -0.071 15  GLY LLL O   
14406 N N   . GLY L 16  ? 0.478 0.949 0.832 -0.021 0.002  -0.046 16  GLY LLL N   
14407 C CA  . GLY L 16  ? 0.480 0.939 0.853 0.009  -0.008 -0.027 16  GLY LLL CA  
14408 C C   . GLY L 16  ? 0.509 0.901 0.839 0.015  0.011  -0.035 16  GLY LLL C   
14409 O O   . GLY L 16  ? 0.508 0.865 0.793 -0.005 0.029  -0.054 16  GLY LLL O   
14410 N N   . SER L 17  ? 0.534 0.906 0.871 0.039  0.005  -0.020 17  SER LLL N   
14411 C CA  . SER L 17  ? 0.524 0.836 0.822 0.044  0.020  -0.025 17  SER LLL CA  
14412 C C   . SER L 17  ? 0.528 0.816 0.791 0.052  -0.003 -0.007 17  SER LLL C   
14413 O O   . SER L 17  ? 0.523 0.840 0.805 0.061  -0.028 0.012  17  SER LLL O   
14414 C CB  . SER L 17  ? 0.523 0.827 0.868 0.064  0.046  -0.029 17  SER LLL CB  
14415 O OG  . SER L 17  ? 0.537 0.846 0.899 0.051  0.076  -0.052 17  SER LLL OG  
14416 N N   . LEU L 18  ? 0.558 0.795 0.771 0.046  0.005  -0.013 18  LEU LLL N   
14417 C CA  . LEU L 18  ? 0.577 0.783 0.756 0.053  -0.009 -0.000 18  LEU LLL CA  
14418 C C   . LEU L 18  ? 0.561 0.722 0.713 0.051  0.010  -0.008 18  LEU LLL C   
14419 O O   . LEU L 18  ? 0.567 0.713 0.698 0.033  0.025  -0.022 18  LEU LLL O   
14420 C CB  . LEU L 18  ? 0.600 0.799 0.735 0.035  -0.023 0.001  18  LEU LLL CB  
14421 C CG  . LEU L 18  ? 0.608 0.834 0.746 0.033  -0.046 0.013  18  LEU LLL CG  
14422 C CD1 . LEU L 18  ? 0.614 0.814 0.705 0.015  -0.049 0.011  18  LEU LLL CD1 
14423 C CD2 . LEU L 18  ? 0.615 0.845 0.770 0.052  -0.060 0.032  18  LEU LLL CD2 
14424 N N   . ARG L 19  ? 0.558 0.695 0.705 0.065  0.008  0.002  19  ARG LLL N   
14425 C CA  . ARG L 19  ? 0.575 0.667 0.684 0.057  0.020  -0.004 19  ARG LLL CA  
14426 C C   . ARG L 19  ? 0.538 0.614 0.611 0.054  0.001  0.007  19  ARG LLL C   
14427 O O   . ARG L 19  ? 0.547 0.621 0.625 0.068  -0.010 0.020  19  ARG LLL O   
14428 C CB  . ARG L 19  ? 0.609 0.681 0.740 0.073  0.041  -0.005 19  ARG LLL CB  
14429 C CG  . ARG L 19  ? 0.650 0.678 0.740 0.054  0.062  -0.019 19  ARG LLL CG  
14430 C CD  . ARG L 19  ? 0.705 0.704 0.811 0.067  0.088  -0.023 19  ARG LLL CD  
14431 N NE  . ARG L 19  ? 0.729 0.719 0.833 0.085  0.070  -0.004 19  ARG LLL NE  
14432 C CZ  . ARG L 19  ? 0.799 0.751 0.897 0.093  0.086  -0.003 19  ARG LLL CZ  
14433 N NH1 . ARG L 19  ? 0.864 0.781 0.955 0.083  0.123  -0.021 19  ARG LLL NH1 
14434 N NH2 . ARG L 19  ? 0.769 0.714 0.863 0.108  0.068  0.015  19  ARG LLL NH2 
14435 N N   . LEU L 20  ? 0.540 0.606 0.583 0.035  -0.002 0.004  20  LEU LLL N   
14436 C CA  . LEU L 20  ? 0.573 0.621 0.588 0.030  -0.013 0.013  20  LEU LLL CA  
14437 C C   . LEU L 20  ? 0.595 0.613 0.591 0.028  -0.003 0.012  20  LEU LLL C   
14438 O O   . LEU L 20  ? 0.636 0.642 0.625 0.017  0.013  0.002  20  LEU LLL O   
14439 C CB  . LEU L 20  ? 0.560 0.609 0.560 0.013  -0.017 0.014  20  LEU LLL CB  
14440 C CG  . LEU L 20  ? 0.568 0.639 0.580 0.011  -0.021 0.012  20  LEU LLL CG  
14441 C CD1 . LEU L 20  ? 0.574 0.636 0.573 -0.003 -0.023 0.016  20  LEU LLL CD1 
14442 C CD2 . LEU L 20  ? 0.555 0.639 0.576 0.022  -0.032 0.017  20  LEU LLL CD2 
14443 N N   . ALA L 21  ? 0.594 0.599 0.580 0.033  -0.011 0.021  21  ALA LLL N   
14444 C CA  . ALA L 21  ? 0.628 0.605 0.590 0.025  -0.004 0.021  21  ALA LLL CA  
14445 C C   . ALA L 21  ? 0.606 0.581 0.554 0.016  -0.016 0.030  21  ALA LLL C   
14446 O O   . ALA L 21  ? 0.624 0.611 0.583 0.022  -0.026 0.036  21  ALA LLL O   
14447 C CB  . ALA L 21  ? 0.643 0.601 0.609 0.040  0.004  0.022  21  ALA LLL CB  
14448 N N   . CYS L 22  ? 0.612 0.575 0.541 -0.001 -0.014 0.031  22  CYS LLL N   
14449 C CA  . CYS L 22  ? 0.622 0.587 0.548 -0.010 -0.024 0.042  22  CYS LLL CA  
14450 C C   . CYS L 22  ? 0.636 0.580 0.537 -0.023 -0.018 0.041  22  CYS LLL C   
14451 O O   . CYS L 22  ? 0.666 0.600 0.545 -0.042 -0.011 0.035  22  CYS LLL O   
14452 C CB  . CYS L 22  ? 0.645 0.626 0.577 -0.024 -0.034 0.051  22  CYS LLL CB  
14453 S SG  . CYS L 22  ? 0.668 0.659 0.610 -0.035 -0.046 0.069  22  CYS LLL SG  
14454 N N   . ILE L 23  ? 0.592 0.529 0.493 -0.017 -0.020 0.045  23  ILE LLL N   
14455 C CA  . ILE L 23  ? 0.606 0.522 0.482 -0.030 -0.013 0.043  23  ILE LLL CA  
14456 C C   . ILE L 23  ? 0.602 0.537 0.488 -0.045 -0.025 0.055  23  ILE LLL C   
14457 O O   . ILE L 23  ? 0.545 0.497 0.459 -0.035 -0.032 0.063  23  ILE LLL O   
14458 C CB  . ILE L 23  ? 0.609 0.499 0.478 -0.013 -0.004 0.039  23  ILE LLL CB  
14459 C CG1 . ILE L 23  ? 0.628 0.488 0.465 -0.028 0.008  0.034  23  ILE LLL CG1 
14460 C CG2 . ILE L 23  ? 0.599 0.498 0.483 -0.000 -0.013 0.045  23  ILE LLL CG2 
14461 C CD1 . ILE L 23  ? 0.648 0.475 0.475 -0.011 0.019  0.032  23  ILE LLL CD1 
14462 N N   . ALA L 24  ? 0.533 0.503 0.521 -0.010 0.030  -0.006 24  ALA LLL N   
14463 C CA  . ALA L 24  ? 0.532 0.520 0.530 -0.022 0.036  -0.006 24  ALA LLL CA  
14464 C C   . ALA L 24  ? 0.552 0.530 0.543 -0.040 0.035  0.005  24  ALA LLL C   
14465 O O   . ALA L 24  ? 0.594 0.538 0.572 -0.042 0.026  0.011  24  ALA LLL O   
14466 C CB  . ALA L 24  ? 0.519 0.509 0.527 -0.020 0.032  -0.014 24  ALA LLL CB  
14467 N N   . SER L 25  ? 0.532 0.539 0.534 -0.052 0.043  0.009  25  SER LLL N   
14468 C CA  . SER L 25  ? 0.530 0.537 0.532 -0.074 0.043  0.020  25  SER LLL CA  
14469 C C   . SER L 25  ? 0.536 0.532 0.548 -0.081 0.034  0.015  25  SER LLL C   
14470 O O   . SER L 25  ? 0.540 0.534 0.557 -0.067 0.029  0.004  25  SER LLL O   
14471 C CB  . SER L 25  ? 0.491 0.543 0.508 -0.083 0.058  0.021  25  SER LLL CB  
14472 O OG  . SER L 25  ? 0.447 0.529 0.492 -0.074 0.060  0.010  25  SER LLL OG  
14473 N N   . GLY L 26  ? 0.563 0.554 0.577 -0.104 0.030  0.023  26  GLY LLL N   
14474 C CA  . GLY L 26  ? 0.589 0.578 0.614 -0.115 0.019  0.018  26  GLY LLL CA  
14475 C C   . GLY L 26  ? 0.636 0.568 0.637 -0.117 0.005  0.015  26  GLY LLL C   
14476 O O   . GLY L 26  ? 0.630 0.529 0.614 -0.103 0.004  0.013  26  GLY LLL O   
14477 N N   . ARG L 27  ? 0.715 0.637 0.719 -0.135 -0.005 0.012  27  ARG LLL N   
14478 C CA  . ARG L 27  ? 0.791 0.655 0.771 -0.139 -0.019 0.004  27  ARG LLL CA  
14479 C C   . ARG L 27  ? 0.761 0.625 0.738 -0.129 -0.026 -0.015 27  ARG LLL C   
14480 O O   . ARG L 27  ? 0.787 0.610 0.745 -0.135 -0.037 -0.025 27  ARG LLL O   
14481 C CB  . ARG L 27  ? 0.890 0.735 0.868 -0.172 -0.028 0.016  27  ARG LLL CB  
14482 C CG  . ARG L 27  ? 1.056 0.862 1.016 -0.178 -0.029 0.032  27  ARG LLL CG  
14483 C CD  . ARG L 27  ? 1.209 0.995 1.166 -0.217 -0.038 0.047  27  ARG LLL CD  
14484 N NE  . ARG L 27  ? 1.286 1.134 1.273 -0.238 -0.034 0.050  27  ARG LLL NE  
14485 C CZ  . ARG L 27  ? 1.371 1.271 1.378 -0.258 -0.022 0.067  27  ARG LLL CZ  
14486 N NH1 . ARG L 27  ? 1.385 1.280 1.379 -0.264 -0.013 0.085  27  ARG LLL NH1 
14487 N NH2 . ARG L 27  ? 1.393 1.352 1.435 -0.272 -0.020 0.066  27  ARG LLL NH2 
14488 N N   . THR L 28  ? 0.725 0.630 0.716 -0.115 -0.019 -0.019 28  THR LLL N   
14489 C CA  . THR L 28  ? 0.713 0.621 0.697 -0.108 -0.025 -0.034 28  THR LLL CA  
14490 C C   . THR L 28  ? 0.657 0.578 0.640 -0.082 -0.015 -0.039 28  THR LLL C   
14491 O O   . THR L 28  ? 0.675 0.622 0.663 -0.078 -0.017 -0.042 28  THR LLL O   
14492 C CB  . THR L 28  ? 0.697 0.644 0.700 -0.125 -0.034 -0.030 28  THR LLL CB  
14493 O OG1 . THR L 28  ? 0.672 0.666 0.707 -0.120 -0.024 -0.019 28  THR LLL OG1 
14494 C CG2 . THR L 28  ? 0.724 0.660 0.729 -0.154 -0.046 -0.027 28  THR LLL CG2 
14495 N N   . PHE L 29  ? 0.627 0.530 0.603 -0.067 -0.008 -0.039 29  PHE LLL N   
14496 C CA  . PHE L 29  ? 0.612 0.528 0.589 -0.045 0.001  -0.043 29  PHE LLL CA  
14497 C C   . PHE L 29  ? 0.646 0.559 0.608 -0.039 -0.000 -0.057 29  PHE LLL C   
14498 O O   . PHE L 29  ? 0.635 0.573 0.602 -0.031 0.004  -0.057 29  PHE LLL O   
14499 C CB  . PHE L 29  ? 0.602 0.495 0.573 -0.032 0.005  -0.041 29  PHE LLL CB  
14500 C CG  . PHE L 29  ? 0.590 0.501 0.566 -0.013 0.012  -0.044 29  PHE LLL CG  
14501 C CD1 . PHE L 29  ? 0.572 0.512 0.560 -0.010 0.018  -0.036 29  PHE LLL CD1 
14502 C CD2 . PHE L 29  ? 0.599 0.497 0.567 0.002  0.014  -0.056 29  PHE LLL CD2 
14503 C CE1 . PHE L 29  ? 0.559 0.513 0.551 0.004  0.023  -0.038 29  PHE LLL CE1 
14504 C CE2 . PHE L 29  ? 0.586 0.506 0.562 0.017  0.021  -0.058 29  PHE LLL CE2 
14505 C CZ  . PHE L 29  ? 0.558 0.504 0.546 0.016  0.024  -0.048 29  PHE LLL CZ  
14506 N N   . HIS L 30  ? 0.667 0.548 0.609 -0.044 -0.007 -0.070 30  HIS LLL N   
14507 C CA  . HIS L 30  ? 0.683 0.559 0.603 -0.040 -0.007 -0.087 30  HIS LLL CA  
14508 C C   . HIS L 30  ? 0.680 0.587 0.601 -0.053 -0.013 -0.081 30  HIS LLL C   
14509 O O   . HIS L 30  ? 0.673 0.588 0.576 -0.050 -0.012 -0.090 30  HIS LLL O   
14510 C CB  . HIS L 30  ? 0.738 0.568 0.634 -0.045 -0.014 -0.103 30  HIS LLL CB  
14511 C CG  . HIS L 30  ? 0.806 0.626 0.700 -0.071 -0.028 -0.098 30  HIS LLL CG  
14512 N ND1 . HIS L 30  ? 0.858 0.667 0.767 -0.084 -0.033 -0.084 30  HIS LLL ND1 
14513 C CD2 . HIS L 30  ? 0.863 0.690 0.745 -0.089 -0.040 -0.103 30  HIS LLL CD2 
14514 C CE1 . HIS L 30  ? 0.882 0.693 0.791 -0.109 -0.046 -0.081 30  HIS LLL CE1 
14515 N NE2 . HIS L 30  ? 0.893 0.715 0.787 -0.112 -0.052 -0.093 30  HIS LLL NE2 
14516 N N   . SER L 31  ? 0.656 0.584 0.598 -0.065 -0.020 -0.067 31  SER LLL N   
14517 C CA  . SER L 31  ? 0.649 0.610 0.600 -0.074 -0.029 -0.060 31  SER LLL CA  
14518 C C   . SER L 31  ? 0.576 0.564 0.542 -0.060 -0.022 -0.050 31  SER LLL C   
14519 O O   . SER L 31  ? 0.557 0.568 0.531 -0.063 -0.031 -0.043 31  SER LLL O   
14520 C CB  . SER L 31  ? 0.651 0.630 0.626 -0.091 -0.040 -0.049 31  SER LLL CB  
14521 O OG  . SER L 31  ? 0.768 0.721 0.730 -0.109 -0.049 -0.056 31  SER LLL OG  
14522 N N   . TYR L 32  ? 0.561 0.547 0.534 -0.045 -0.009 -0.050 32  TYR LLL N   
14523 C CA  . TYR L 32  ? 0.534 0.542 0.524 -0.034 -0.003 -0.041 32  TYR LLL CA  
14524 C C   . TYR L 32  ? 0.538 0.543 0.511 -0.026 0.003  -0.046 32  TYR LLL C   
14525 O O   . TYR L 32  ? 0.549 0.539 0.510 -0.019 0.011  -0.056 32  TYR LLL O   
14526 C CB  . TYR L 32  ? 0.510 0.522 0.519 -0.028 0.004  -0.036 32  TYR LLL CB  
14527 C CG  . TYR L 32  ? 0.500 0.530 0.532 -0.037 0.001  -0.029 32  TYR LLL CG  
14528 C CD1 . TYR L 32  ? 0.519 0.540 0.550 -0.051 -0.002 -0.029 32  TYR LLL CD1 
14529 C CD2 . TYR L 32  ? 0.492 0.549 0.548 -0.033 -0.001 -0.022 32  TYR LLL CD2 
14530 C CE1 . TYR L 32  ? 0.517 0.562 0.572 -0.062 -0.005 -0.021 32  TYR LLL CE1 
14531 C CE2 . TYR L 32  ? 0.487 0.570 0.570 -0.039 -0.003 -0.017 32  TYR LLL CE2 
14532 C CZ  . TYR L 32  ? 0.496 0.577 0.579 -0.055 -0.004 -0.016 32  TYR LLL CZ  
14533 O OH  . TYR L 32  ? 0.485 0.599 0.599 -0.064 -0.005 -0.010 32  TYR LLL OH  
14534 N N   . VAL L 33  ? 0.533 0.553 0.508 -0.026 0.000  -0.038 33  VAL LLL N   
14535 C CA  . VAL L 33  ? 0.520 0.545 0.488 -0.020 0.008  -0.037 33  VAL LLL CA  
14536 C C   . VAL L 33  ? 0.494 0.522 0.484 -0.010 0.014  -0.034 33  VAL LLL C   
14537 O O   . VAL L 33  ? 0.475 0.508 0.484 -0.009 0.011  -0.027 33  VAL LLL O   
14538 C CB  . VAL L 33  ? 0.527 0.561 0.489 -0.027 -0.001 -0.025 33  VAL LLL CB  
14539 C CG1 . VAL L 33  ? 0.523 0.562 0.481 -0.025 0.006  -0.020 33  VAL LLL CG1 
14540 C CG2 . VAL L 33  ? 0.561 0.594 0.497 -0.038 -0.010 -0.028 33  VAL LLL CG2 
14541 N N   . MET L 34  ? 0.495 0.522 0.482 -0.003 0.024  -0.039 34  MET LLL N   
14542 C CA  . MET L 34  ? 0.489 0.518 0.491 0.004  0.028  -0.037 34  MET LLL CA  
14543 C C   . MET L 34  ? 0.511 0.552 0.515 0.003  0.031  -0.032 34  MET LLL C   
14544 O O   . MET L 34  ? 0.490 0.538 0.483 -0.001 0.034  -0.034 34  MET LLL O   
14545 C CB  . MET L 34  ? 0.489 0.510 0.490 0.012  0.033  -0.043 34  MET LLL CB  
14546 C CG  . MET L 34  ? 0.496 0.501 0.494 0.009  0.029  -0.046 34  MET LLL CG  
14547 S SD  . MET L 34  ? 0.497 0.508 0.509 0.002  0.026  -0.037 34  MET LLL SD  
14548 C CE  . MET L 34  ? 0.475 0.490 0.493 0.009  0.031  -0.034 34  MET LLL CE  
14549 N N   . ALA L 35  ? 0.529 0.570 0.545 0.005  0.029  -0.028 35  ALA LLL N   
14550 C CA  . ALA L 35  ? 0.505 0.550 0.523 0.000  0.028  -0.023 35  ALA LLL CA  
14551 C C   . ALA L 35  ? 0.476 0.520 0.503 0.004  0.029  -0.025 35  ALA LLL C   
14552 O O   . ALA L 35  ? 0.458 0.497 0.489 0.010  0.029  -0.029 35  ALA LLL O   
14553 C CB  . ALA L 35  ? 0.514 0.551 0.531 -0.005 0.020  -0.014 35  ALA LLL CB  
14554 N N   . TRP L 36  ? 0.479 0.530 0.508 -0.002 0.029  -0.022 36  TRP LLL N   
14555 C CA  . TRP L 36  ? 0.464 0.514 0.500 -0.004 0.026  -0.024 36  TRP LLL CA  
14556 C C   . TRP L 36  ? 0.471 0.508 0.507 -0.013 0.019  -0.018 36  TRP LLL C   
14557 O O   . TRP L 36  ? 0.481 0.522 0.512 -0.023 0.018  -0.009 36  TRP LLL O   
14558 C CB  . TRP L 36  ? 0.457 0.529 0.499 -0.004 0.029  -0.025 36  TRP LLL CB  
14559 C CG  . TRP L 36  ? 0.437 0.513 0.481 0.008  0.032  -0.030 36  TRP LLL CG  
14560 C CD1 . TRP L 36  ? 0.447 0.530 0.490 0.015  0.037  -0.033 36  TRP LLL CD1 
14561 C CD2 . TRP L 36  ? 0.432 0.500 0.473 0.013  0.028  -0.032 36  TRP LLL CD2 
14562 N NE1 . TRP L 36  ? 0.418 0.494 0.462 0.025  0.035  -0.036 36  TRP LLL NE1 
14563 C CE2 . TRP L 36  ? 0.421 0.490 0.463 0.023  0.030  -0.034 36  TRP LLL CE2 
14564 C CE3 . TRP L 36  ? 0.438 0.498 0.474 0.010  0.023  -0.034 36  TRP LLL CE3 
14565 C CZ2 . TRP L 36  ? 0.437 0.499 0.474 0.028  0.025  -0.032 36  TRP LLL CZ2 
14566 C CZ3 . TRP L 36  ? 0.434 0.491 0.463 0.015  0.021  -0.035 36  TRP LLL CZ3 
14567 C CH2 . TRP L 36  ? 0.437 0.496 0.467 0.023  0.021  -0.032 36  TRP LLL CH2 
14568 N N   . PHE L 37  ? 0.494 0.512 0.530 -0.011 0.014  -0.022 37  PHE LLL N   
14569 C CA  . PHE L 37  ? 0.501 0.498 0.538 -0.019 0.005  -0.020 37  PHE LLL CA  
14570 C C   . PHE L 37  ? 0.530 0.523 0.564 -0.022 0.002  -0.028 37  PHE LLL C   
14571 O O   . PHE L 37  ? 0.567 0.574 0.600 -0.015 0.007  -0.036 37  PHE LLL O   
14572 C CB  . PHE L 37  ? 0.497 0.469 0.536 -0.009 0.000  -0.021 37  PHE LLL CB  
14573 C CG  . PHE L 37  ? 0.494 0.466 0.534 -0.009 -0.003 -0.010 37  PHE LLL CG  
14574 C CD1 . PHE L 37  ? 0.464 0.456 0.505 -0.004 0.002  -0.010 37  PHE LLL CD1 
14575 C CD2 . PHE L 37  ? 0.508 0.457 0.546 -0.016 -0.015 0.002  37  PHE LLL CD2 
14576 C CE1 . PHE L 37  ? 0.466 0.457 0.504 -0.005 -0.003 0.000  37  PHE LLL CE1 
14577 C CE2 . PHE L 37  ? 0.499 0.449 0.535 -0.016 -0.021 0.015  37  PHE LLL CE2 
14578 C CZ  . PHE L 37  ? 0.481 0.454 0.517 -0.012 -0.015 0.013  37  PHE LLL CZ  
14579 N N   . ARG L 38  ? 0.524 0.498 0.557 -0.034 -0.007 -0.027 38  ARG LLL N   
14580 C CA  . ARG L 38  ? 0.554 0.519 0.581 -0.039 -0.012 -0.038 38  ARG LLL CA  
14581 C C   . ARG L 38  ? 0.589 0.512 0.611 -0.043 -0.022 -0.043 38  ARG LLL C   
14582 O O   . ARG L 38  ? 0.576 0.478 0.601 -0.046 -0.027 -0.033 38  ARG LLL O   
14583 C CB  . ARG L 38  ? 0.576 0.570 0.609 -0.056 -0.015 -0.032 38  ARG LLL CB  
14584 C CG  . ARG L 38  ? 0.601 0.590 0.639 -0.077 -0.021 -0.019 38  ARG LLL CG  
14585 C CD  . ARG L 38  ? 0.594 0.626 0.645 -0.091 -0.019 -0.012 38  ARG LLL CD  
14586 N NE  . ARG L 38  ? 0.618 0.652 0.673 -0.115 -0.023 0.003  38  ARG LLL NE  
14587 C CZ  . ARG L 38  ? 0.624 0.700 0.695 -0.132 -0.020 0.011  38  ARG LLL CZ  
14588 N NH1 . ARG L 38  ? 0.608 0.726 0.696 -0.125 -0.017 0.005  38  ARG LLL NH1 
14589 N NH2 . ARG L 38  ? 0.654 0.731 0.726 -0.157 -0.022 0.026  38  ARG LLL NH2 
14590 N N   . GLN L 39  ? 0.605 0.512 0.616 -0.043 -0.026 -0.059 39  GLN LLL N   
14591 C CA  . GLN L 39  ? 0.671 0.532 0.674 -0.043 -0.035 -0.071 39  GLN LLL CA  
14592 C C   . GLN L 39  ? 0.703 0.555 0.691 -0.057 -0.043 -0.083 39  GLN LLL C   
14593 O O   . GLN L 39  ? 0.732 0.601 0.709 -0.051 -0.038 -0.096 39  GLN LLL O   
14594 C CB  . GLN L 39  ? 0.678 0.524 0.682 -0.018 -0.027 -0.085 39  GLN LLL CB  
14595 C CG  . GLN L 39  ? 0.746 0.542 0.744 -0.013 -0.035 -0.100 39  GLN LLL CG  
14596 C CD  . GLN L 39  ? 0.749 0.538 0.759 0.015  -0.027 -0.111 39  GLN LLL CD  
14597 O OE1 . GLN L 39  ? 0.782 0.605 0.796 0.027  -0.013 -0.116 39  GLN LLL OE1 
14598 N NE2 . GLN L 39  ? 0.779 0.524 0.796 0.024  -0.037 -0.114 39  GLN LLL NE2 
14599 N N   . ALA L 40  ? 0.735 0.564 0.722 -0.079 -0.057 -0.079 40  ALA LLL N   
14600 C CA  . ALA L 40  ? 0.783 0.590 0.753 -0.095 -0.070 -0.093 40  ALA LLL CA  
14601 C C   . ALA L 40  ? 0.838 0.589 0.792 -0.082 -0.073 -0.116 40  ALA LLL C   
14602 O O   . ALA L 40  ? 0.859 0.583 0.822 -0.067 -0.071 -0.114 40  ALA LLL O   
14603 C CB  . ALA L 40  ? 0.806 0.612 0.784 -0.127 -0.084 -0.077 40  ALA LLL CB  
14604 N N   . PRO L 41  ? 0.878 0.612 0.808 -0.085 -0.077 -0.140 41  PRO LLL N   
14605 C CA  . PRO L 41  ? 0.937 0.618 0.851 -0.069 -0.077 -0.167 41  PRO LLL CA  
14606 C C   . PRO L 41  ? 1.019 0.639 0.938 -0.078 -0.094 -0.164 41  PRO LLL C   
14607 O O   . PRO L 41  ? 1.022 0.631 0.940 -0.108 -0.110 -0.151 41  PRO LLL O   
14608 C CB  . PRO L 41  ? 0.953 0.629 0.833 -0.077 -0.080 -0.193 41  PRO LLL CB  
14609 C CG  . PRO L 41  ? 0.921 0.647 0.804 -0.100 -0.087 -0.175 41  PRO LLL CG  
14610 C CD  . PRO L 41  ? 0.869 0.633 0.785 -0.102 -0.083 -0.143 41  PRO LLL CD  
14611 N N   . GLY L 42  ? 1.075 0.658 1.002 -0.052 -0.090 -0.172 42  GLY LLL N   
14612 C CA  . GLY L 42  ? 1.150 0.667 1.082 -0.056 -0.108 -0.167 42  GLY LLL CA  
14613 C C   . GLY L 42  ? 1.160 0.687 1.116 -0.061 -0.112 -0.131 42  GLY LLL C   
14614 O O   . GLY L 42  ? 1.246 0.719 1.208 -0.059 -0.127 -0.123 42  GLY LLL O   
14615 N N   . LYS L 43  ? 1.093 0.685 1.060 -0.066 -0.101 -0.110 43  LYS LLL N   
14616 C CA  . LYS L 43  ? 1.078 0.687 1.062 -0.075 -0.103 -0.076 43  LYS LLL CA  
14617 C C   . LYS L 43  ? 1.015 0.658 1.015 -0.046 -0.089 -0.072 43  LYS LLL C   
14618 O O   . LYS L 43  ? 1.003 0.667 1.002 -0.025 -0.075 -0.093 43  LYS LLL O   
14619 C CB  . LYS L 43  ? 1.078 0.736 1.063 -0.105 -0.102 -0.057 43  LYS LLL CB  
14620 C CG  . LYS L 43  ? 1.155 0.786 1.132 -0.141 -0.119 -0.047 43  LYS LLL CG  
14621 C CD  . LYS L 43  ? 1.165 0.858 1.149 -0.167 -0.114 -0.033 43  LYS LLL CD  
14622 C CE  . LYS L 43  ? 1.250 0.922 1.229 -0.206 -0.132 -0.027 43  LYS LLL CE  
14623 N NZ  . LYS L 43  ? 1.252 0.972 1.234 -0.220 -0.130 -0.036 43  LYS LLL NZ  
14624 N N   . GLU L 44  ? 0.993 0.643 1.004 -0.048 -0.092 -0.046 44  GLU LLL N   
14625 C CA  . GLU L 44  ? 0.955 0.634 0.981 -0.024 -0.082 -0.041 44  GLU LLL CA  
14626 C C   . GLU L 44  ? 0.834 0.578 0.861 -0.030 -0.066 -0.036 44  GLU LLL C   
14627 O O   . GLU L 44  ? 0.774 0.536 0.792 -0.052 -0.065 -0.031 44  GLU LLL O   
14628 C CB  . GLU L 44  ? 1.027 0.685 1.060 -0.025 -0.096 -0.015 44  GLU LLL CB  
14629 C CG  . GLU L 44  ? 1.152 0.737 1.182 -0.026 -0.118 -0.012 44  GLU LLL CG  
14630 C CD  . GLU L 44  ? 1.247 0.797 1.289 0.006  -0.119 -0.041 44  GLU LLL CD  
14631 O OE1 . GLU L 44  ? 1.234 0.817 1.294 0.035  -0.106 -0.052 44  GLU LLL OE1 
14632 O OE2 . GLU L 44  ? 1.320 0.809 1.353 0.003  -0.132 -0.053 44  GLU LLL OE2 
14633 N N   . ARG L 45  ? 0.804 0.580 0.842 -0.010 -0.055 -0.037 45  ARG LLL N   
14634 C CA  . ARG L 45  ? 0.772 0.600 0.810 -0.014 -0.042 -0.030 45  ARG LLL CA  
14635 C C   . ARG L 45  ? 0.749 0.587 0.782 -0.035 -0.047 -0.006 45  ARG LLL C   
14636 O O   . ARG L 45  ? 0.760 0.579 0.795 -0.034 -0.057 0.010  45  ARG LLL O   
14637 C CB  . ARG L 45  ? 0.756 0.607 0.806 0.008  -0.032 -0.035 45  ARG LLL CB  
14638 C CG  . ARG L 45  ? 0.802 0.676 0.850 0.017  -0.018 -0.054 45  ARG LLL CG  
14639 C CD  . ARG L 45  ? 0.847 0.739 0.910 0.038  -0.009 -0.061 45  ARG LLL CD  
14640 N NE  . ARG L 45  ? 0.881 0.774 0.941 0.049  0.001  -0.083 45  ARG LLL NE  
14641 C CZ  . ARG L 45  ? 0.914 0.836 0.979 0.059  0.015  -0.092 45  ARG LLL CZ  
14642 N NH1 . ARG L 45  ? 0.921 0.872 0.999 0.060  0.019  -0.080 45  ARG LLL NH1 
14643 N NH2 . ARG L 45  ? 0.949 0.871 1.006 0.066  0.025  -0.112 45  ARG LLL NH2 
14644 N N   . GLU L 46  ? 0.728 0.596 0.756 -0.051 -0.040 -0.002 46  GLU LLL N   
14645 C CA  . GLU L 46  ? 0.714 0.603 0.737 -0.072 -0.039 0.018  46  GLU LLL CA  
14646 C C   . GLU L 46  ? 0.619 0.553 0.644 -0.064 -0.025 0.017  46  GLU LLL C   
14647 O O   . GLU L 46  ? 0.554 0.510 0.584 -0.054 -0.016 0.003  46  GLU LLL O   
14648 C CB  . GLU L 46  ? 0.768 0.659 0.790 -0.096 -0.043 0.019  46  GLU LLL CB  
14649 C CG  . GLU L 46  ? 0.833 0.757 0.854 -0.119 -0.038 0.037  46  GLU LLL CG  
14650 C CD  . GLU L 46  ? 0.896 0.834 0.923 -0.144 -0.042 0.038  46  GLU LLL CD  
14651 O OE1 . GLU L 46  ? 0.953 0.866 0.980 -0.144 -0.051 0.025  46  GLU LLL OE1 
14652 O OE2 . GLU L 46  ? 0.926 0.903 0.958 -0.162 -0.035 0.051  46  GLU LLL OE2 
14653 N N   . PHE L 47  ? 0.594 0.538 0.613 -0.069 -0.024 0.031  47  PHE LLL N   
14654 C CA  . PHE L 47  ? 0.565 0.547 0.581 -0.064 -0.011 0.029  47  PHE LLL CA  
14655 C C   . PHE L 47  ? 0.546 0.563 0.566 -0.074 0.000  0.026  47  PHE LLL C   
14656 O O   . PHE L 47  ? 0.551 0.574 0.570 -0.095 -0.002 0.037  47  PHE LLL O   
14657 C CB  . PHE L 47  ? 0.562 0.545 0.564 -0.070 -0.013 0.044  47  PHE LLL CB  
14658 C CG  . PHE L 47  ? 0.542 0.559 0.536 -0.068 -0.000 0.039  47  PHE LLL CG  
14659 C CD1 . PHE L 47  ? 0.520 0.540 0.517 -0.051 0.002  0.028  47  PHE LLL CD1 
14660 C CD2 . PHE L 47  ? 0.544 0.589 0.528 -0.083 0.010  0.044  47  PHE LLL CD2 
14661 C CE1 . PHE L 47  ? 0.518 0.561 0.505 -0.049 0.013  0.022  47  PHE LLL CE1 
14662 C CE2 . PHE L 47  ? 0.529 0.601 0.504 -0.078 0.023  0.036  47  PHE LLL CE2 
14663 C CZ  . PHE L 47  ? 0.508 0.575 0.483 -0.061 0.023  0.024  47  PHE LLL CZ  
14664 N N   . VAL L 48  ? 0.533 0.575 0.560 -0.061 0.011  0.014  48  VAL LLL N   
14665 C CA  . VAL L 48  ? 0.521 0.601 0.557 -0.064 0.021  0.010  48  VAL LLL CA  
14666 C C   . VAL L 48  ? 0.507 0.614 0.538 -0.059 0.033  0.008  48  VAL LLL C   
14667 O O   . VAL L 48  ? 0.516 0.653 0.547 -0.071 0.042  0.013  48  VAL LLL O   
14668 C CB  . VAL L 48  ? 0.498 0.583 0.546 -0.052 0.019  -0.002 48  VAL LLL CB  
14669 C CG1 . VAL L 48  ? 0.494 0.620 0.558 -0.051 0.027  -0.005 48  VAL LLL CG1 
14670 C CG2 . VAL L 48  ? 0.518 0.577 0.566 -0.060 0.008  -0.003 48  VAL LLL CG2 
14671 N N   . ALA L 49  ? 0.512 0.609 0.537 -0.043 0.035  0.000  49  ALA LLL N   
14672 C CA  . ALA L 49  ? 0.522 0.637 0.539 -0.037 0.046  -0.007 49  ALA LLL CA  
14673 C C   . ALA L 49  ? 0.498 0.591 0.505 -0.026 0.042  -0.011 49  ALA LLL C   
14674 O O   . ALA L 49  ? 0.479 0.552 0.492 -0.019 0.034  -0.012 49  ALA LLL O   
14675 C CB  . ALA L 49  ? 0.512 0.653 0.545 -0.026 0.055  -0.017 49  ALA LLL CB  
14676 N N   . ALA L 50  ? 0.509 0.607 0.499 -0.026 0.048  -0.015 50  ALA LLL N   
14677 C CA  . ALA L 50  ? 0.524 0.606 0.504 -0.020 0.043  -0.021 50  ALA LLL CA  
14678 C C   . ALA L 50  ? 0.539 0.630 0.504 -0.016 0.053  -0.034 50  ALA LLL C   
14679 O O   . ALA L 50  ? 0.549 0.663 0.506 -0.021 0.064  -0.036 50  ALA LLL O   
14680 C CB  . ALA L 50  ? 0.529 0.597 0.498 -0.030 0.031  -0.008 50  ALA LLL CB  
14681 N N   . ILE L 51  ? 0.538 0.613 0.499 -0.009 0.050  -0.043 51  ILE LLL N   
14682 C CA  . ILE L 51  ? 0.535 0.606 0.480 -0.003 0.057  -0.060 51  ILE LLL CA  
14683 C C   . ILE L 51  ? 0.534 0.584 0.463 -0.008 0.047  -0.061 51  ILE LLL C   
14684 O O   . ILE L 51  ? 0.516 0.552 0.458 -0.008 0.037  -0.056 51  ILE LLL O   
14685 C CB  . ILE L 51  ? 0.521 0.591 0.485 0.015  0.063  -0.070 51  ILE LLL CB  
14686 C CG1 . ILE L 51  ? 0.553 0.618 0.503 0.024  0.072  -0.090 51  ILE LLL CG1 
14687 C CG2 . ILE L 51  ? 0.495 0.544 0.472 0.019  0.054  -0.065 51  ILE LLL CG2 
14688 C CD1 . ILE L 51  ? 0.557 0.624 0.528 0.044  0.078  -0.100 51  ILE LLL CD1 
14689 N N   . SER L 52  ? 0.593 0.644 0.493 -0.016 0.049  -0.069 52  SER LLL N   
14690 C CA  . SER L 52  ? 0.621 0.654 0.501 -0.025 0.036  -0.072 52  SER LLL CA  
14691 C C   . SER L 52  ? 0.610 0.619 0.492 -0.017 0.036  -0.088 52  SER LLL C   
14692 O O   . SER L 52  ? 0.628 0.634 0.524 -0.002 0.046  -0.096 52  SER LLL O   
14693 C CB  . SER L 52  ? 0.650 0.691 0.494 -0.038 0.036  -0.074 52  SER LLL CB  
14694 O OG  . SER L 52  ? 0.703 0.733 0.535 -0.050 0.018  -0.068 52  SER LLL OG  
14695 N N   . TRP L 53  ? 0.616 0.608 0.484 -0.027 0.023  -0.091 53  TRP LLL N   
14696 C CA  . TRP L 53  ? 0.639 0.602 0.508 -0.025 0.018  -0.102 53  TRP LLL CA  
14697 C C   . TRP L 53  ? 0.669 0.614 0.523 -0.011 0.031  -0.125 53  TRP LLL C   
14698 O O   . TRP L 53  ? 0.647 0.574 0.518 0.001  0.033  -0.129 53  TRP LLL O   
14699 C CB  . TRP L 53  ? 0.641 0.593 0.493 -0.044 0.002  -0.102 53  TRP LLL CB  
14700 C CG  . TRP L 53  ? 0.612 0.587 0.480 -0.054 -0.011 -0.081 53  TRP LLL CG  
14701 C CD1 . TRP L 53  ? 0.579 0.563 0.481 -0.054 -0.016 -0.067 53  TRP LLL CD1 
14702 C CD2 . TRP L 53  ? 0.612 0.604 0.462 -0.065 -0.020 -0.072 53  TRP LLL CD2 
14703 N NE1 . TRP L 53  ? 0.563 0.569 0.476 -0.060 -0.028 -0.051 53  TRP LLL NE1 
14704 C CE2 . TRP L 53  ? 0.584 0.592 0.465 -0.067 -0.032 -0.052 53  TRP LLL CE2 
14705 C CE3 . TRP L 53  ? 0.629 0.624 0.440 -0.073 -0.019 -0.078 53  TRP LLL CE3 
14706 C CZ2 . TRP L 53  ? 0.590 0.615 0.466 -0.076 -0.046 -0.037 53  TRP LLL CZ2 
14707 C CZ3 . TRP L 53  ? 0.658 0.669 0.458 -0.085 -0.033 -0.061 53  TRP LLL CZ3 
14708 C CH2 . TRP L 53  ? 0.638 0.661 0.472 -0.085 -0.048 -0.040 53  TRP LLL CH2 
14709 N N   . SER L 54  ? 0.704 0.656 0.528 -0.013 0.039  -0.140 54  SER LLL N   
14710 C CA  . SER L 54  ? 0.741 0.680 0.549 0.002  0.053  -0.167 54  SER LLL CA  
14711 C C   . SER L 54  ? 0.713 0.677 0.547 0.022  0.070  -0.168 54  SER LLL C   
14712 O O   . SER L 54  ? 0.732 0.693 0.563 0.040  0.083  -0.190 54  SER LLL O   
14713 C CB  . SER L 54  ? 0.773 0.719 0.538 -0.009 0.058  -0.182 54  SER LLL CB  
14714 O OG  . SER L 54  ? 0.781 0.770 0.545 -0.014 0.067  -0.168 54  SER LLL OG  
14715 N N   . SER L 55  ? 0.676 0.667 0.537 0.020  0.070  -0.145 55  SER LLL N   
14716 C CA  . SER L 55  ? 0.670 0.696 0.557 0.033  0.084  -0.142 55  SER LLL CA  
14717 C C   . SER L 55  ? 0.724 0.788 0.592 0.023  0.097  -0.142 55  SER LLL C   
14718 O O   . SER L 55  ? 0.671 0.769 0.562 0.029  0.109  -0.137 55  SER LLL O   
14719 C CB  . SER L 55  ? 0.649 0.669 0.554 0.058  0.092  -0.158 55  SER LLL CB  
14720 O OG  . SER L 55  ? 0.608 0.593 0.528 0.065  0.079  -0.153 55  SER LLL OG  
14721 N N   . THR L 56  ? 0.837 0.897 0.666 0.006  0.095  -0.145 56  THR LLL N   
14722 C CA  . THR L 56  ? 0.958 1.048 0.759 0.002  0.114  -0.158 56  THR LLL CA  
14723 C C   . THR L 56  ? 0.967 1.090 0.761 -0.019 0.115  -0.134 56  THR LLL C   
14724 O O   . THR L 56  ? 1.135 1.294 0.920 -0.021 0.135  -0.139 56  THR LLL O   
14725 C CB  . THR L 56  ? 1.058 1.127 0.811 -0.005 0.114  -0.179 56  THR LLL CB  
14726 O OG1 . THR L 56  ? 1.114 1.168 0.874 0.019  0.125  -0.209 56  THR LLL OG1 
14727 C CG2 . THR L 56  ? 1.087 1.187 0.798 -0.023 0.126  -0.181 56  THR LLL CG2 
14728 N N   . PRO L 57  ? 0.814 0.925 0.607 -0.035 0.096  -0.109 57  PRO LLL N   
14729 C CA  . PRO L 57  ? 0.717 0.852 0.520 -0.048 0.095  -0.083 57  PRO LLL CA  
14730 C C   . PRO L 57  ? 0.657 0.789 0.508 -0.035 0.092  -0.076 57  PRO LLL C   
14731 O O   . PRO L 57  ? 0.609 0.715 0.475 -0.027 0.078  -0.075 57  PRO LLL O   
14732 C CB  . PRO L 57  ? 0.710 0.829 0.487 -0.068 0.074  -0.063 57  PRO LLL CB  
14733 C CG  . PRO L 57  ? 0.755 0.847 0.514 -0.066 0.063  -0.079 57  PRO LLL CG  
14734 C CD  . PRO L 57  ? 0.756 0.836 0.532 -0.044 0.074  -0.105 57  PRO LLL CD  
14735 N N   . THR L 58  ? 0.610 0.773 0.483 -0.032 0.105  -0.073 58  THR LLL N   
14736 C CA  . THR L 58  ? 0.551 0.716 0.462 -0.029 0.099  -0.060 58  THR LLL CA  
14737 C C   . THR L 58  ? 0.554 0.731 0.461 -0.051 0.095  -0.036 58  THR LLL C   
14738 O O   . THR L 58  ? 0.580 0.777 0.461 -0.066 0.104  -0.032 58  THR LLL O   
14739 C CB  . THR L 58  ? 0.534 0.723 0.477 -0.011 0.111  -0.072 58  THR LLL CB  
14740 O OG1 . THR L 58  ? 0.547 0.780 0.489 -0.015 0.131  -0.078 58  THR LLL OG1 
14741 C CG2 . THR L 58  ? 0.518 0.684 0.468 0.012  0.110  -0.091 58  THR LLL CG2 
14742 N N   . TYR L 59  ? 0.532 0.694 0.460 -0.052 0.082  -0.022 59  TYR LLL N   
14743 C CA  . TYR L 59  ? 0.543 0.705 0.470 -0.072 0.074  0.000  59  TYR LLL CA  
14744 C C   . TYR L 59  ? 0.512 0.680 0.472 -0.070 0.072  0.003  59  TYR LLL C   
14745 O O   . TYR L 59  ? 0.479 0.637 0.460 -0.052 0.069  -0.007 59  TYR LLL O   
14746 C CB  . TYR L 59  ? 0.554 0.680 0.469 -0.077 0.053  0.014  59  TYR LLL CB  
14747 C CG  . TYR L 59  ? 0.587 0.704 0.471 -0.081 0.048  0.014  59  TYR LLL CG  
14748 C CD1 . TYR L 59  ? 0.582 0.683 0.468 -0.067 0.043  0.000  59  TYR LLL CD1 
14749 C CD2 . TYR L 59  ? 0.621 0.742 0.471 -0.101 0.045  0.029  59  TYR LLL CD2 
14750 C CE1 . TYR L 59  ? 0.609 0.700 0.467 -0.072 0.034  0.000  59  TYR LLL CE1 
14751 C CE2 . TYR L 59  ? 0.655 0.766 0.475 -0.106 0.036  0.029  59  TYR LLL CE2 
14752 C CZ  . TYR L 59  ? 0.650 0.747 0.474 -0.091 0.030  0.014  59  TYR LLL CZ  
14753 O OH  . TYR L 59  ? 0.694 0.784 0.488 -0.098 0.019  0.014  59  TYR LLL OH  
14754 N N   . TYR L 60  ? 0.520 0.702 0.483 -0.090 0.073  0.018  60  TYR LLL N   
14755 C CA  . TYR L 60  ? 0.506 0.698 0.498 -0.094 0.070  0.022  60  TYR LLL CA  
14756 C C   . TYR L 60  ? 0.526 0.696 0.510 -0.118 0.057  0.044  60  TYR LLL C   
14757 O O   . TYR L 60  ? 0.524 0.696 0.484 -0.137 0.058  0.059  60  TYR LLL O   
14758 C CB  . TYR L 60  ? 0.513 0.758 0.524 -0.095 0.089  0.014  60  TYR LLL CB  
14759 C CG  . TYR L 60  ? 0.497 0.757 0.520 -0.067 0.099  -0.008 60  TYR LLL CG  
14760 C CD1 . TYR L 60  ? 0.458 0.706 0.504 -0.048 0.090  -0.016 60  TYR LLL CD1 
14761 C CD2 . TYR L 60  ? 0.490 0.770 0.498 -0.060 0.115  -0.021 60  TYR LLL CD2 
14762 C CE1 . TYR L 60  ? 0.464 0.717 0.520 -0.024 0.096  -0.033 60  TYR LLL CE1 
14763 C CE2 . TYR L 60  ? 0.494 0.778 0.513 -0.034 0.123  -0.042 60  TYR LLL CE2 
14764 C CZ  . TYR L 60  ? 0.481 0.750 0.525 -0.016 0.112  -0.047 60  TYR LLL CZ  
14765 O OH  . TYR L 60  ? 0.503 0.769 0.557 0.010  0.116  -0.065 60  TYR LLL OH  
14766 N N   . GLY L 61  ? 0.531 0.678 0.533 -0.117 0.044  0.045  61  GLY LLL N   
14767 C CA  . GLY L 61  ? 0.579 0.703 0.579 -0.140 0.031  0.063  61  GLY LLL CA  
14768 C C   . GLY L 61  ? 0.620 0.785 0.626 -0.166 0.041  0.073  61  GLY LLL C   
14769 O O   . GLY L 61  ? 0.611 0.823 0.638 -0.159 0.055  0.061  61  GLY LLL O   
14770 N N   . GLU L 62  ? 0.698 0.847 0.691 -0.194 0.033  0.095  62  GLU LLL N   
14771 C CA  . GLU L 62  ? 0.748 0.940 0.745 -0.226 0.043  0.109  62  GLU LLL CA  
14772 C C   . GLU L 62  ? 0.711 0.937 0.745 -0.226 0.046  0.098  62  GLU LLL C   
14773 O O   . GLU L 62  ? 0.724 1.015 0.776 -0.233 0.064  0.096  62  GLU LLL O   
14774 C CB  . GLU L 62  ? 0.876 1.028 0.852 -0.257 0.027  0.137  62  GLU LLL CB  
14775 C CG  . GLU L 62  ? 1.010 1.148 0.947 -0.263 0.027  0.153  62  GLU LLL CG  
14776 C CD  . GLU L 62  ? 1.064 1.263 0.989 -0.265 0.053  0.147  62  GLU LLL CD  
14777 O OE1 . GLU L 62  ? 1.052 1.308 0.994 -0.280 0.072  0.146  62  GLU LLL OE1 
14778 O OE2 . GLU L 62  ? 1.080 1.271 0.979 -0.249 0.055  0.141  62  GLU LLL OE2 
14779 N N   . SER L 63  ? 0.687 0.877 0.733 -0.217 0.029  0.090  63  SER LLL N   
14780 C CA  . SER L 63  ? 0.670 0.887 0.747 -0.227 0.025  0.085  63  SER LLL CA  
14781 C C   . SER L 63  ? 0.589 0.851 0.692 -0.198 0.036  0.065  63  SER LLL C   
14782 O O   . SER L 63  ? 0.551 0.850 0.683 -0.205 0.034  0.061  63  SER LLL O   
14783 C CB  . SER L 63  ? 0.704 0.862 0.777 -0.232 0.001  0.084  63  SER LLL CB  
14784 O OG  . SER L 63  ? 0.718 0.839 0.783 -0.200 -0.004 0.068  63  SER LLL OG  
14785 N N   . VAL L 64  ? 0.560 0.820 0.654 -0.169 0.045  0.052  64  VAL LLL N   
14786 C CA  . VAL L 64  ? 0.530 0.824 0.647 -0.141 0.054  0.034  64  VAL LLL CA  
14787 C C   . VAL L 64  ? 0.533 0.874 0.653 -0.133 0.077  0.029  64  VAL LLL C   
14788 O O   . VAL L 64  ? 0.500 0.875 0.643 -0.110 0.085  0.015  64  VAL LLL O   
14789 C CB  . VAL L 64  ? 0.500 0.750 0.606 -0.114 0.045  0.022  64  VAL LLL CB  
14790 C CG1 . VAL L 64  ? 0.499 0.707 0.600 -0.121 0.026  0.023  64  VAL LLL CG1 
14791 C CG2 . VAL L 64  ? 0.494 0.716 0.573 -0.103 0.050  0.020  64  VAL LLL CG2 
14792 N N   . LYS L 65  ? 0.583 0.924 0.677 -0.149 0.086  0.039  65  LYS LLL N   
14793 C CA  . LYS L 65  ? 0.633 1.019 0.722 -0.143 0.110  0.032  65  LYS LLL CA  
14794 C C   . LYS L 65  ? 0.603 1.062 0.735 -0.142 0.125  0.025  65  LYS LLL C   
14795 O O   . LYS L 65  ? 0.603 1.087 0.756 -0.166 0.120  0.038  65  LYS LLL O   
14796 C CB  . LYS L 65  ? 0.735 1.116 0.788 -0.171 0.116  0.050  65  LYS LLL CB  
14797 C CG  . LYS L 65  ? 0.813 1.192 0.833 -0.158 0.129  0.039  65  LYS LLL CG  
14798 C CD  . LYS L 65  ? 0.901 1.277 0.881 -0.188 0.133  0.059  65  LYS LLL CD  
14799 C CE  . LYS L 65  ? 0.945 1.346 0.896 -0.180 0.154  0.045  65  LYS LLL CE  
14800 N NZ  . LYS L 65  ? 0.991 1.435 0.920 -0.213 0.171  0.060  65  LYS LLL NZ  
14801 N N   . GLY L 66  ? 0.583 1.072 0.730 -0.112 0.140  0.004  66  GLY LLL N   
14802 C CA  . GLY L 66  ? 0.568 1.131 0.762 -0.102 0.155  -0.006 66  GLY LLL CA  
14803 C C   . GLY L 66  ? 0.554 1.114 0.783 -0.079 0.139  -0.013 66  GLY LLL C   
14804 O O   . GLY L 66  ? 0.579 1.185 0.844 -0.054 0.149  -0.027 66  GLY LLL O   
14805 N N   . ARG L 67  ? 0.519 1.030 0.740 -0.085 0.114  -0.004 67  ARG LLL N   
14806 C CA  . ARG L 67  ? 0.476 0.987 0.727 -0.070 0.096  -0.008 67  ARG LLL CA  
14807 C C   . ARG L 67  ? 0.458 0.916 0.690 -0.040 0.087  -0.019 67  ARG LLL C   
14808 O O   . ARG L 67  ? 0.445 0.912 0.701 -0.018 0.079  -0.025 67  ARG LLL O   
14809 C CB  . ARG L 67  ? 0.488 0.981 0.737 -0.099 0.075  0.007  67  ARG LLL CB  
14810 C CG  . ARG L 67  ? 0.511 1.055 0.782 -0.134 0.081  0.020  67  ARG LLL CG  
14811 C CD  . ARG L 67  ? 0.510 1.035 0.783 -0.162 0.057  0.032  67  ARG LLL CD  
14812 N NE  . ARG L 67  ? 0.527 0.973 0.756 -0.171 0.045  0.036  67  ARG LLL NE  
14813 C CZ  . ARG L 67  ? 0.514 0.909 0.729 -0.163 0.025  0.031  67  ARG LLL CZ  
14814 N NH1 . ARG L 67  ? 0.512 0.923 0.747 -0.149 0.014  0.023  67  ARG LLL NH1 
14815 N NH2 . ARG L 67  ? 0.524 0.852 0.703 -0.170 0.017  0.034  67  ARG LLL NH2 
14816 N N   . PHE L 68  ? 0.464 0.869 0.656 -0.041 0.087  -0.019 68  PHE LLL N   
14817 C CA  . PHE L 68  ? 0.457 0.808 0.628 -0.020 0.078  -0.026 68  PHE LLL CA  
14818 C C   . PHE L 68  ? 0.479 0.820 0.632 -0.003 0.092  -0.038 68  PHE LLL C   
14819 O O   . PHE L 68  ? 0.517 0.870 0.654 -0.015 0.106  -0.038 68  PHE LLL O   
14820 C CB  . PHE L 68  ? 0.444 0.741 0.585 -0.035 0.064  -0.017 68  PHE LLL CB  
14821 C CG  . PHE L 68  ? 0.436 0.726 0.586 -0.049 0.047  -0.010 68  PHE LLL CG  
14822 C CD1 . PHE L 68  ? 0.426 0.757 0.606 -0.055 0.042  -0.008 68  PHE LLL CD1 
14823 C CD2 . PHE L 68  ? 0.452 0.692 0.578 -0.056 0.035  -0.007 68  PHE LLL CD2 
14824 C CE1 . PHE L 68  ? 0.452 0.771 0.633 -0.070 0.025  -0.003 68  PHE LLL CE1 
14825 C CE2 . PHE L 68  ? 0.474 0.701 0.601 -0.068 0.020  -0.005 68  PHE LLL CE2 
14826 C CZ  . PHE L 68  ? 0.471 0.735 0.623 -0.077 0.014  -0.003 68  PHE LLL CZ  
14827 N N   . THR L 69  ? 0.477 0.796 0.631 0.022  0.088  -0.049 69  THR LLL N   
14828 C CA  . THR L 69  ? 0.513 0.814 0.649 0.039  0.099  -0.063 69  THR LLL CA  
14829 C C   . THR L 69  ? 0.515 0.759 0.628 0.045  0.085  -0.062 69  THR LLL C   
14830 O O   . THR L 69  ? 0.555 0.786 0.680 0.055  0.073  -0.059 69  THR LLL O   
14831 C CB  . THR L 69  ? 0.544 0.875 0.708 0.065  0.108  -0.078 69  THR LLL CB  
14832 O OG1 . THR L 69  ? 0.592 0.986 0.783 0.058  0.122  -0.078 69  THR LLL OG1 
14833 C CG2 . THR L 69  ? 0.563 0.869 0.704 0.081  0.119  -0.096 69  THR LLL CG2 
14834 N N   . ILE L 70  ? 0.504 0.719 0.586 0.037  0.087  -0.063 70  ILE LLL N   
14835 C CA  . ILE L 70  ? 0.508 0.676 0.571 0.041  0.077  -0.063 70  ILE LLL CA  
14836 C C   . ILE L 70  ? 0.530 0.684 0.585 0.058  0.083  -0.079 70  ILE LLL C   
14837 O O   . ILE L 70  ? 0.555 0.728 0.605 0.060  0.096  -0.090 70  ILE LLL O   
14838 C CB  . ILE L 70  ? 0.497 0.644 0.537 0.023  0.072  -0.054 70  ILE LLL CB  
14839 C CG1 . ILE L 70  ? 0.478 0.589 0.510 0.026  0.061  -0.052 70  ILE LLL CG1 
14840 C CG2 . ILE L 70  ? 0.507 0.660 0.525 0.014  0.081  -0.057 70  ILE LLL CG2 
14841 C CD1 . ILE L 70  ? 0.488 0.583 0.506 0.012  0.054  -0.042 70  ILE LLL CD1 
14842 N N   . SER L 71  ? 0.533 0.653 0.586 0.068  0.073  -0.080 71  SER LLL N   
14843 C CA  . SER L 71  ? 0.555 0.648 0.599 0.083  0.074  -0.095 71  SER LLL CA  
14844 C C   . SER L 71  ? 0.550 0.600 0.580 0.079  0.061  -0.087 71  SER LLL C   
14845 O O   . SER L 71  ? 0.528 0.577 0.562 0.070  0.053  -0.073 71  SER LLL O   
14846 C CB  . SER L 71  ? 0.549 0.656 0.618 0.107  0.077  -0.104 71  SER LLL CB  
14847 O OG  . SER L 71  ? 0.550 0.656 0.639 0.113  0.064  -0.091 71  SER LLL OG  
14848 N N   . ARG L 72  ? 0.555 0.572 0.569 0.083  0.059  -0.098 72  ARG LLL N   
14849 C CA  . ARG L 72  ? 0.544 0.523 0.546 0.074  0.047  -0.090 72  ARG LLL CA  
14850 C C   . ARG L 72  ? 0.585 0.527 0.584 0.089  0.043  -0.100 72  ARG LLL C   
14851 O O   . ARG L 72  ? 0.593 0.534 0.591 0.103  0.050  -0.118 72  ARG LLL O   
14852 C CB  . ARG L 72  ? 0.561 0.534 0.543 0.055  0.046  -0.090 72  ARG LLL CB  
14853 C CG  . ARG L 72  ? 0.579 0.544 0.540 0.055  0.052  -0.107 72  ARG LLL CG  
14854 C CD  . ARG L 72  ? 0.591 0.558 0.534 0.034  0.047  -0.103 72  ARG LLL CD  
14855 N NE  . ARG L 72  ? 0.590 0.535 0.534 0.023  0.035  -0.093 72  ARG LLL NE  
14856 C CZ  . ARG L 72  ? 0.583 0.540 0.529 0.008  0.029  -0.082 72  ARG LLL CZ  
14857 N NH1 . ARG L 72  ? 0.577 0.558 0.521 0.003  0.030  -0.077 72  ARG LLL NH1 
14858 N NH2 . ARG L 72  ? 0.585 0.530 0.537 -0.001 0.021  -0.074 72  ARG LLL NH2 
14859 N N   . ASP L 73  ? 0.604 0.516 0.601 0.086  0.031  -0.088 73  ASP LLL N   
14860 C CA  . ASP L 73  ? 0.649 0.514 0.640 0.094  0.022  -0.093 73  ASP LLL CA  
14861 C C   . ASP L 73  ? 0.673 0.509 0.646 0.071  0.014  -0.083 73  ASP LLL C   
14862 O O   . ASP L 73  ? 0.623 0.461 0.599 0.060  0.008  -0.064 73  ASP LLL O   
14863 C CB  . ASP L 73  ? 0.677 0.536 0.686 0.112  0.013  -0.082 73  ASP LLL CB  
14864 C CG  . ASP L 73  ? 0.748 0.551 0.750 0.123  0.001  -0.084 73  ASP LLL CG  
14865 O OD1 . ASP L 73  ? 0.779 0.546 0.761 0.112  -0.001 -0.092 73  ASP LLL OD1 
14866 O OD2 . ASP L 73  ? 0.812 0.608 0.830 0.141  -0.008 -0.076 73  ASP LLL OD2 
14867 N N   . ASN L 74  ? 0.709 0.526 0.664 0.061  0.014  -0.096 74  ASN LLL N   
14868 C CA  . ASN L 74  ? 0.704 0.505 0.647 0.036  0.006  -0.088 74  ASN LLL CA  
14869 C C   . ASN L 74  ? 0.743 0.500 0.682 0.031  -0.006 -0.076 74  ASN LLL C   
14870 O O   . ASN L 74  ? 0.726 0.487 0.665 0.010  -0.010 -0.059 74  ASN LLL O   
14871 C CB  . ASN L 74  ? 0.736 0.527 0.660 0.027  0.006  -0.106 74  ASN LLL CB  
14872 C CG  . ASN L 74  ? 0.717 0.551 0.640 0.023  0.015  -0.109 74  ASN LLL CG  
14873 O OD1 . ASN L 74  ? 0.651 0.522 0.590 0.026  0.021  -0.098 74  ASN LLL OD1 
14874 N ND2 . ASN L 74  ? 0.748 0.576 0.650 0.014  0.014  -0.124 74  ASN LLL ND2 
14875 N N   . ALA L 75  ? 0.759 0.479 0.697 0.050  -0.011 -0.082 75  ALA LLL N   
14876 C CA  . ALA L 75  ? 0.787 0.458 0.720 0.046  -0.026 -0.067 75  ALA LLL CA  
14877 C C   . ALA L 75  ? 0.772 0.467 0.713 0.038  -0.028 -0.040 75  ALA LLL C   
14878 O O   . ALA L 75  ? 0.847 0.512 0.777 0.021  -0.037 -0.022 75  ALA LLL O   
14879 C CB  . ALA L 75  ? 0.807 0.436 0.743 0.074  -0.033 -0.079 75  ALA LLL CB  
14880 N N   . LYS L 76  ? 0.730 0.474 0.685 0.047  -0.018 -0.038 76  LYS LLL N   
14881 C CA  . LYS L 76  ? 0.721 0.489 0.679 0.042  -0.019 -0.017 76  LYS LLL CA  
14882 C C   . LYS L 76  ? 0.664 0.477 0.626 0.026  -0.008 -0.014 76  LYS LLL C   
14883 O O   . LYS L 76  ? 0.650 0.487 0.614 0.023  -0.006 -0.003 76  LYS LLL O   
14884 C CB  . LYS L 76  ? 0.733 0.518 0.707 0.066  -0.021 -0.017 76  LYS LLL CB  
14885 C CG  . LYS L 76  ? 0.781 0.526 0.759 0.089  -0.034 -0.019 76  LYS LLL CG  
14886 C CD  . LYS L 76  ? 0.780 0.547 0.776 0.109  -0.040 -0.012 76  LYS LLL CD  
14887 C CE  . LYS L 76  ? 0.846 0.572 0.851 0.134  -0.055 -0.011 76  LYS LLL CE  
14888 N NZ  . LYS L 76  ? 0.860 0.606 0.879 0.146  -0.068 0.007  76  LYS LLL NZ  
14889 N N   . ASN L 77  ? 0.657 0.481 0.619 0.016  -0.002 -0.025 77  ASN LLL N   
14890 C CA  . ASN L 77  ? 0.617 0.482 0.586 0.004  0.007  -0.023 77  ASN LLL CA  
14891 C C   . ASN L 77  ? 0.578 0.477 0.558 0.017  0.013  -0.024 77  ASN LLL C   
14892 O O   . ASN L 77  ? 0.533 0.456 0.516 0.010  0.017  -0.018 77  ASN LLL O   
14893 C CB  . ASN L 77  ? 0.628 0.497 0.594 -0.016 0.007  -0.008 77  ASN LLL CB  
14894 C CG  . ASN L 77  ? 0.625 0.484 0.589 -0.036 0.003  -0.008 77  ASN LLL CG  
14895 O OD1 . ASN L 77  ? 0.650 0.475 0.605 -0.037 -0.004 -0.016 77  ASN LLL OD1 
14896 N ND2 . ASN L 77  ? 0.594 0.484 0.568 -0.052 0.009  -0.001 77  ASN LLL ND2 
14897 N N   . THR L 78  ? 0.556 0.456 0.541 0.035  0.013  -0.033 78  THR LLL N   
14898 C CA  . THR L 78  ? 0.526 0.456 0.523 0.044  0.016  -0.031 78  THR LLL CA  
14899 C C   . THR L 78  ? 0.525 0.478 0.531 0.052  0.023  -0.044 78  THR LLL C   
14900 O O   . THR L 78  ? 0.536 0.479 0.540 0.060  0.026  -0.056 78  THR LLL O   
14901 C CB  . THR L 78  ? 0.542 0.461 0.541 0.057  0.007  -0.023 78  THR LLL CB  
14902 O OG1 . THR L 78  ? 0.529 0.430 0.514 0.045  0.001  -0.008 78  THR LLL OG1 
14903 C CG2 . THR L 78  ? 0.504 0.456 0.516 0.064  0.007  -0.022 78  THR LLL CG2 
14904 N N   . VAL L 79  ? 0.514 0.495 0.526 0.047  0.028  -0.042 79  VAL LLL N   
14905 C CA  . VAL L 79  ? 0.515 0.522 0.535 0.050  0.034  -0.048 79  VAL LLL CA  
14906 C C   . VAL L 79  ? 0.515 0.544 0.550 0.057  0.032  -0.044 79  VAL LLL C   
14907 O O   . VAL L 79  ? 0.479 0.505 0.512 0.053  0.026  -0.036 79  VAL LLL O   
14908 C CB  . VAL L 79  ? 0.503 0.521 0.520 0.037  0.037  -0.047 79  VAL LLL CB  
14909 C CG1 . VAL L 79  ? 0.506 0.528 0.526 0.031  0.034  -0.039 79  VAL LLL CG1 
14910 C CG2 . VAL L 79  ? 0.491 0.531 0.511 0.036  0.043  -0.050 79  VAL LLL CG2 
14911 N N   . TYR L 80  ? 0.526 0.576 0.575 0.066  0.036  -0.050 80  TYR LLL N   
14912 C CA  . TYR L 80  ? 0.505 0.583 0.574 0.071  0.032  -0.046 80  TYR LLL CA  
14913 C C   . TYR L 80  ? 0.479 0.588 0.556 0.061  0.039  -0.047 80  TYR LLL C   
14914 O O   . TYR L 80  ? 0.485 0.599 0.555 0.056  0.049  -0.053 80  TYR LLL O   
14915 C CB  . TYR L 80  ? 0.520 0.602 0.606 0.092  0.031  -0.052 80  TYR LLL CB  
14916 C CG  . TYR L 80  ? 0.557 0.601 0.634 0.102  0.021  -0.049 80  TYR LLL CG  
14917 C CD1 . TYR L 80  ? 0.554 0.591 0.631 0.102  0.008  -0.035 80  TYR LLL CD1 
14918 C CD2 . TYR L 80  ? 0.589 0.602 0.655 0.109  0.024  -0.058 80  TYR LLL CD2 
14919 C CE1 . TYR L 80  ? 0.593 0.592 0.658 0.108  -0.003 -0.028 80  TYR LLL CE1 
14920 C CE2 . TYR L 80  ? 0.613 0.585 0.670 0.115  0.013  -0.053 80  TYR LLL CE2 
14921 C CZ  . TYR L 80  ? 0.621 0.587 0.679 0.114  -0.000 -0.036 80  TYR LLL CZ  
14922 O OH  . TYR L 80  ? 0.699 0.623 0.745 0.117  -0.012 -0.027 80  TYR LLL OH  
14923 N N   . LEU L 81  ? 0.476 0.605 0.565 0.055  0.033  -0.041 81  LEU LLL N   
14924 C CA  . LEU L 81  ? 0.475 0.637 0.577 0.044  0.037  -0.039 81  LEU LLL CA  
14925 C C   . LEU L 81  ? 0.455 0.652 0.586 0.051  0.032  -0.038 81  LEU LLL C   
14926 O O   . LEU L 81  ? 0.424 0.619 0.556 0.048  0.019  -0.032 81  LEU LLL O   
14927 C CB  . LEU L 81  ? 0.452 0.600 0.540 0.025  0.032  -0.033 81  LEU LLL CB  
14928 C CG  . LEU L 81  ? 0.463 0.632 0.558 0.009  0.036  -0.030 81  LEU LLL CG  
14929 C CD1 . LEU L 81  ? 0.475 0.648 0.561 0.005  0.047  -0.031 81  LEU LLL CD1 
14930 C CD2 . LEU L 81  ? 0.481 0.630 0.566 -0.006 0.027  -0.025 81  LEU LLL CD2 
14931 N N   . GLN L 82  ? 0.452 0.683 0.605 0.060  0.042  -0.044 82  GLN LLL N   
14932 C CA  . GLN L 82  ? 0.460 0.739 0.650 0.067  0.040  -0.043 82  GLN LLL CA  
14933 C C   . GLN L 82  ? 0.465 0.774 0.662 0.041  0.041  -0.036 82  GLN LLL C   
14934 O O   . GLN L 82  ? 0.501 0.816 0.689 0.029  0.054  -0.037 82  GLN LLL O   
14935 C CB  . GLN L 82  ? 0.465 0.769 0.676 0.089  0.053  -0.055 82  GLN LLL CB  
14936 C CG  . GLN L 82  ? 0.483 0.841 0.741 0.103  0.049  -0.055 82  GLN LLL CG  
14937 C CD  . GLN L 82  ? 0.499 0.843 0.765 0.112  0.026  -0.045 82  GLN LLL CD  
14938 O OE1 . GLN L 82  ? 0.518 0.816 0.765 0.125  0.016  -0.044 82  GLN LLL OE1 
14939 N NE2 . GLN L 82  ? 0.502 0.888 0.795 0.103  0.015  -0.037 82  GLN LLL NE2 
14940 N N   . MET L 83  ? 0.479 0.798 0.686 0.031  0.025  -0.028 83  MET LLL N   
14941 C CA  . MET L 83  ? 0.492 0.833 0.705 0.003  0.023  -0.021 83  MET LLL CA  
14942 C C   . MET L 83  ? 0.500 0.903 0.758 0.004  0.018  -0.019 83  MET LLL C   
14943 O O   . MET L 83  ? 0.507 0.914 0.777 0.012  0.001  -0.016 83  MET LLL O   
14944 C CB  . MET L 83  ? 0.520 0.820 0.707 -0.013 0.007  -0.017 83  MET LLL CB  
14945 C CG  . MET L 83  ? 0.525 0.771 0.675 -0.010 0.011  -0.020 83  MET LLL CG  
14946 S SD  . MET L 83  ? 0.589 0.795 0.712 -0.025 -0.004 -0.020 83  MET LLL SD  
14947 C CE  . MET L 83  ? 0.562 0.771 0.685 -0.013 -0.019 -0.020 83  MET LLL CE  
14948 N N   . ASN L 84  ? 0.508 0.959 0.790 -0.005 0.033  -0.019 84  ASN LLL N   
14949 C CA  . ASN L 84  ? 0.529 1.053 0.863 -0.006 0.032  -0.016 84  ASN LLL CA  
14950 C C   . ASN L 84  ? 0.548 1.094 0.887 -0.044 0.027  -0.005 84  ASN LLL C   
14951 O O   . ASN L 84  ? 0.542 1.050 0.847 -0.066 0.031  -0.001 84  ASN LLL O   
14952 C CB  . ASN L 84  ? 0.544 1.116 0.906 0.015  0.055  -0.027 84  ASN LLL CB  
14953 C CG  . ASN L 84  ? 0.554 1.098 0.912 0.053  0.056  -0.038 84  ASN LLL CG  
14954 O OD1 . ASN L 84  ? 0.543 1.061 0.901 0.068  0.036  -0.035 84  ASN LLL OD1 
14955 N ND2 . ASN L 84  ? 0.603 1.148 0.955 0.069  0.078  -0.052 84  ASN LLL ND2 
14956 N N   . ARG L 85  ? 0.546 1.149 0.928 -0.053 0.016  -0.000 85  ARG LLL N   
14957 C CA  . ARG L 85  ? 0.548 1.183 0.945 -0.092 0.011  0.011  85  ARG LLL CA  
14958 C C   . ARG L 85  ? 0.538 1.099 0.885 -0.117 -0.003 0.015  85  ARG LLL C   
14959 O O   . ARG L 85  ? 0.540 1.088 0.870 -0.144 0.004  0.022  85  ARG LLL O   
14960 C CB  . ARG L 85  ? 0.575 1.262 0.990 -0.104 0.039  0.013  85  ARG LLL CB  
14961 C CG  . ARG L 85  ? 0.608 1.372 1.076 -0.075 0.054  0.004  85  ARG LLL CG  
14962 C CD  . ARG L 85  ? 0.645 1.482 1.140 -0.093 0.081  0.007  85  ARG LLL CD  
14963 N NE  . ARG L 85  ? 0.705 1.503 1.152 -0.100 0.102  0.005  85  ARG LLL NE  
14964 C CZ  . ARG L 85  ? 0.732 1.519 1.151 -0.139 0.108  0.018  85  ARG LLL CZ  
14965 N NH1 . ARG L 85  ? 0.728 1.537 1.164 -0.178 0.096  0.035  85  ARG LLL NH1 
14966 N NH2 . ARG L 85  ? 0.708 1.460 1.083 -0.140 0.125  0.017  85  ARG LLL NH2 
14967 N N   . LEU L 86  ? 0.527 1.043 0.852 -0.107 -0.022 0.011  86  LEU LLL N   
14968 C CA  . LEU L 86  ? 0.541 0.986 0.819 -0.124 -0.035 0.010  86  LEU LLL CA  
14969 C C   . LEU L 86  ? 0.575 1.028 0.859 -0.163 -0.051 0.017  86  LEU LLL C   
14970 O O   . LEU L 86  ? 0.589 1.097 0.910 -0.172 -0.063 0.021  86  LEU LLL O   
14971 C CB  . LEU L 86  ? 0.550 0.958 0.805 -0.103 -0.050 0.003  86  LEU LLL CB  
14972 C CG  . LEU L 86  ? 0.530 0.906 0.765 -0.072 -0.036 -0.003 86  LEU LLL CG  
14973 C CD1 . LEU L 86  ? 0.540 0.899 0.764 -0.052 -0.050 -0.005 86  LEU LLL CD1 
14974 C CD2 . LEU L 86  ? 0.522 0.842 0.719 -0.079 -0.027 -0.005 86  LEU LLL CD2 
14975 N N   . LYS L 87  ? 0.582 0.982 0.833 -0.184 -0.052 0.019  87  LYS LLL N   
14976 C CA  . LYS L 87  ? 0.619 1.006 0.867 -0.224 -0.069 0.025  87  LYS LLL CA  
14977 C C   . LYS L 87  ? 0.645 0.954 0.848 -0.225 -0.085 0.013  87  LYS LLL C   
14978 O O   . LYS L 87  ? 0.638 0.907 0.814 -0.199 -0.078 0.005  87  LYS LLL O   
14979 C CB  . LYS L 87  ? 0.642 1.026 0.888 -0.249 -0.055 0.038  87  LYS LLL CB  
14980 C CG  . LYS L 87  ? 0.635 1.084 0.910 -0.240 -0.030 0.044  87  LYS LLL CG  
14981 C CD  . LYS L 87  ? 0.665 1.104 0.925 -0.262 -0.015 0.058  87  LYS LLL CD  
14982 C CE  . LYS L 87  ? 0.668 1.186 0.960 -0.258 0.010  0.063  87  LYS LLL CE  
14983 N NZ  . LYS L 87  ? 0.700 1.212 0.972 -0.284 0.025  0.078  87  LYS LLL NZ  
14984 N N   . PRO L 88  ? 0.683 0.974 0.879 -0.254 -0.107 0.011  88  PRO LLL N   
14985 C CA  . PRO L 88  ? 0.708 0.923 0.859 -0.255 -0.121 -0.004 88  PRO LLL CA  
14986 C C   . PRO L 88  ? 0.712 0.861 0.831 -0.243 -0.108 -0.007 88  PRO LLL C   
14987 O O   . PRO L 88  ? 0.714 0.820 0.804 -0.223 -0.109 -0.022 88  PRO LLL O   
14988 C CB  . PRO L 88  ? 0.748 0.953 0.899 -0.297 -0.143 -0.003 88  PRO LLL CB  
14989 C CG  . PRO L 88  ? 0.740 1.033 0.941 -0.312 -0.147 0.010  88  PRO LLL CG  
14990 C CD  . PRO L 88  ? 0.694 1.037 0.924 -0.288 -0.120 0.021  88  PRO LLL CD  
14991 N N   . GLU L 89  ? 0.717 0.866 0.844 -0.255 -0.097 0.008  89  GLU LLL N   
14992 C CA  . GLU L 89  ? 0.738 0.832 0.842 -0.246 -0.089 0.010  89  GLU LLL CA  
14993 C C   . GLU L 89  ? 0.654 0.749 0.750 -0.207 -0.072 0.003  89  GLU LLL C   
14994 O O   . GLU L 89  ? 0.641 0.692 0.719 -0.196 -0.067 0.003  89  GLU LLL O   
14995 C CB  . GLU L 89  ? 0.813 0.924 0.928 -0.268 -0.080 0.031  89  GLU LLL CB  
14996 C CG  . GLU L 89  ? 0.956 1.072 1.082 -0.312 -0.095 0.043  89  GLU LLL CG  
14997 C CD  . GLU L 89  ? 1.006 1.209 1.172 -0.328 -0.092 0.050  89  GLU LLL CD  
14998 O OE1 . GLU L 89  ? 1.075 1.337 1.264 -0.314 -0.072 0.057  89  GLU LLL OE1 
14999 O OE2 . GLU L 89  ? 1.005 1.216 1.182 -0.355 -0.111 0.049  89  GLU LLL OE2 
15000 N N   . ASP L 90  ? 0.599 0.743 0.712 -0.188 -0.065 -0.001 90  ASP LLL N   
15001 C CA  . ASP L 90  ? 0.583 0.727 0.689 -0.154 -0.051 -0.006 90  ASP LLL CA  
15002 C C   . ASP L 90  ? 0.568 0.677 0.650 -0.138 -0.059 -0.022 90  ASP LLL C   
15003 O O   . ASP L 90  ? 0.555 0.654 0.627 -0.114 -0.048 -0.027 90  ASP LLL O   
15004 C CB  . ASP L 90  ? 0.561 0.768 0.697 -0.141 -0.041 -0.002 90  ASP LLL CB  
15005 C CG  . ASP L 90  ? 0.562 0.809 0.719 -0.151 -0.027 0.010  90  ASP LLL CG  
15006 O OD1 . ASP L 90  ? 0.553 0.775 0.694 -0.155 -0.019 0.016  90  ASP LLL OD1 
15007 O OD2 . ASP L 90  ? 0.602 0.909 0.793 -0.155 -0.025 0.014  90  ASP LLL OD2 
15008 N N   . THR L 91  ? 0.567 0.658 0.637 -0.154 -0.075 -0.031 91  THR LLL N   
15009 C CA  . THR L 91  ? 0.578 0.635 0.618 -0.143 -0.081 -0.048 91  THR LLL CA  
15010 C C   . THR L 91  ? 0.588 0.594 0.606 -0.128 -0.072 -0.056 91  THR LLL C   
15011 O O   . THR L 91  ? 0.613 0.584 0.629 -0.140 -0.075 -0.054 91  THR LLL O   
15012 C CB  . THR L 91  ? 0.609 0.652 0.636 -0.166 -0.102 -0.057 91  THR LLL CB  
15013 O OG1 . THR L 91  ? 0.600 0.700 0.652 -0.176 -0.112 -0.048 91  THR LLL OG1 
15014 C CG2 . THR L 91  ? 0.646 0.650 0.634 -0.156 -0.106 -0.077 91  THR LLL CG2 
15015 N N   . ALA L 92  ? 0.574 0.576 0.581 -0.104 -0.061 -0.063 92  ALA LLL N   
15016 C CA  . ALA L 92  ? 0.616 0.581 0.609 -0.087 -0.051 -0.072 92  ALA LLL CA  
15017 C C   . ALA L 92  ? 0.595 0.572 0.579 -0.066 -0.040 -0.076 92  ALA LLL C   
15018 O O   . ALA L 92  ? 0.601 0.611 0.589 -0.064 -0.041 -0.070 92  ALA LLL O   
15019 C CB  . ALA L 92  ? 0.599 0.559 0.608 -0.086 -0.044 -0.058 92  ALA LLL CB  
15020 N N   . VAL L 93  ? 0.584 0.536 0.558 -0.051 -0.030 -0.086 93  VAL LLL N   
15021 C CA  . VAL L 93  ? 0.548 0.513 0.519 -0.033 -0.017 -0.086 93  VAL LLL CA  
15022 C C   . VAL L 93  ? 0.508 0.488 0.501 -0.027 -0.010 -0.071 93  VAL LLL C   
15023 O O   . VAL L 93  ? 0.521 0.485 0.524 -0.029 -0.011 -0.067 93  VAL LLL O   
15024 C CB  . VAL L 93  ? 0.567 0.507 0.525 -0.021 -0.008 -0.103 93  VAL LLL CB  
15025 C CG1 . VAL L 93  ? 0.544 0.503 0.503 -0.006 0.006  -0.101 93  VAL LLL CG1 
15026 C CG2 . VAL L 93  ? 0.586 0.509 0.515 -0.027 -0.014 -0.123 93  VAL LLL CG2 
15027 N N   . TYR L 94  ? 0.484 0.491 0.483 -0.021 -0.005 -0.063 94  TYR LLL N   
15028 C CA  . TYR L 94  ? 0.485 0.507 0.500 -0.015 0.002  -0.052 94  TYR LLL CA  
15029 C C   . TYR L 94  ? 0.485 0.503 0.496 -0.002 0.012  -0.054 94  TYR LLL C   
15030 O O   . TYR L 94  ? 0.461 0.483 0.459 0.001  0.014  -0.057 94  TYR LLL O   
15031 C CB  . TYR L 94  ? 0.488 0.539 0.514 -0.017 -0.000 -0.043 94  TYR LLL CB  
15032 C CG  . TYR L 94  ? 0.483 0.548 0.522 -0.031 -0.006 -0.038 94  TYR LLL CG  
15033 C CD1 . TYR L 94  ? 0.510 0.574 0.547 -0.044 -0.018 -0.042 94  TYR LLL CD1 
15034 C CD2 . TYR L 94  ? 0.473 0.555 0.527 -0.034 -0.001 -0.030 94  TYR LLL CD2 
15035 C CE1 . TYR L 94  ? 0.514 0.595 0.566 -0.061 -0.024 -0.035 94  TYR LLL CE1 
15036 C CE2 . TYR L 94  ? 0.480 0.582 0.548 -0.050 -0.004 -0.024 94  TYR LLL CE2 
15037 C CZ  . TYR L 94  ? 0.479 0.581 0.548 -0.064 -0.016 -0.025 94  TYR LLL CZ  
15038 O OH  . TYR L 94  ? 0.481 0.606 0.566 -0.084 -0.020 -0.018 94  TYR LLL OH  
15039 N N   . PHE L 95  ? 0.490 0.499 0.508 0.002  0.015  -0.052 95  PHE LLL N   
15040 C CA  . PHE L 95  ? 0.480 0.490 0.501 0.012  0.023  -0.053 95  PHE LLL CA  
15041 C C   . PHE L 95  ? 0.465 0.487 0.494 0.012  0.025  -0.044 95  PHE LLL C   
15042 O O   . PHE L 95  ? 0.479 0.502 0.512 0.008  0.023  -0.038 95  PHE LLL O   
15043 C CB  . PHE L 95  ? 0.486 0.480 0.515 0.017  0.023  -0.057 95  PHE LLL CB  
15044 C CG  . PHE L 95  ? 0.501 0.477 0.523 0.019  0.021  -0.071 95  PHE LLL CG  
15045 C CD1 . PHE L 95  ? 0.530 0.485 0.548 0.012  0.012  -0.073 95  PHE LLL CD1 
15046 C CD2 . PHE L 95  ? 0.506 0.486 0.524 0.029  0.031  -0.084 95  PHE LLL CD2 
15047 C CE1 . PHE L 95  ? 0.559 0.491 0.568 0.014  0.010  -0.089 95  PHE LLL CE1 
15048 C CE2 . PHE L 95  ? 0.533 0.496 0.541 0.032  0.032  -0.101 95  PHE LLL CE2 
15049 C CZ  . PHE L 95  ? 0.558 0.493 0.560 0.026  0.020  -0.105 95  PHE LLL CZ  
15050 N N   . CYS L 96  ? 0.470 0.498 0.495 0.016  0.031  -0.043 96  CYS LLL N   
15051 C CA  . CYS L 96  ? 0.480 0.512 0.509 0.017  0.033  -0.038 96  CYS LLL CA  
15052 C C   . CYS L 96  ? 0.466 0.497 0.504 0.019  0.033  -0.038 96  CYS LLL C   
15053 O O   . CYS L 96  ? 0.476 0.507 0.519 0.023  0.036  -0.043 96  CYS LLL O   
15054 C CB  . CYS L 96  ? 0.522 0.555 0.544 0.018  0.036  -0.037 96  CYS LLL CB  
15055 S SG  . CYS L 96  ? 0.663 0.693 0.686 0.018  0.036  -0.033 96  CYS LLL SG  
15056 N N   . ALA L 97  ? 0.456 0.488 0.497 0.017  0.030  -0.033 97  ALA LLL N   
15057 C CA  . ALA L 97  ? 0.445 0.481 0.498 0.018  0.027  -0.031 97  ALA LLL CA  
15058 C C   . ALA L 97  ? 0.435 0.475 0.484 0.013  0.025  -0.028 97  ALA LLL C   
15059 O O   . ALA L 97  ? 0.452 0.487 0.487 0.010  0.026  -0.028 97  ALA LLL O   
15060 C CB  . ALA L 97  ? 0.485 0.512 0.543 0.019  0.019  -0.027 97  ALA LLL CB  
15061 N N   . ALA L 98  ? 0.421 0.468 0.480 0.012  0.022  -0.026 98  ALA LLL N   
15062 C CA  . ALA L 98  ? 0.433 0.482 0.488 0.004  0.017  -0.024 98  ALA LLL CA  
15063 C C   . ALA L 98  ? 0.431 0.492 0.500 0.002  0.007  -0.018 98  ALA LLL C   
15064 O O   . ALA L 98  ? 0.465 0.538 0.558 0.010  0.007  -0.017 98  ALA LLL O   
15065 C CB  . ALA L 98  ? 0.430 0.479 0.483 -0.000 0.023  -0.026 98  ALA LLL CB  
15066 N N   . ASP L 99  ? 0.425 0.484 0.482 -0.006 -0.002 -0.016 99  ASP LLL N   
15067 C CA  . ASP L 99  ? 0.435 0.507 0.505 -0.011 -0.016 -0.009 99  ASP LLL CA  
15068 C C   . ASP L 99  ? 0.434 0.501 0.483 -0.025 -0.023 -0.011 99  ASP LLL C   
15069 O O   . ASP L 99  ? 0.453 0.503 0.474 -0.028 -0.017 -0.018 99  ASP LLL O   
15070 C CB  . ASP L 99  ? 0.434 0.503 0.504 -0.007 -0.026 0.000  99  ASP LLL CB  
15071 C CG  . ASP L 99  ? 0.448 0.535 0.545 -0.004 -0.041 0.009  99  ASP LLL CG  
15072 O OD1 . ASP L 99  ? 0.406 0.506 0.534 0.009  -0.038 0.008  99  ASP LLL OD1 
15073 O OD2 . ASP L 99  ? 0.523 0.614 0.609 -0.014 -0.056 0.016  99  ASP LLL OD2 
15074 N N   . ARG L 100 ? 0.583 0.516 0.546 -0.064 -0.057 -0.066 100 ARG LLL N   
15075 C CA  . ARG L 100 ? 0.595 0.516 0.588 -0.046 -0.084 -0.070 100 ARG LLL CA  
15076 C C   . ARG L 100 ? 0.578 0.495 0.561 -0.019 -0.088 -0.087 100 ARG LLL C   
15077 O O   . ARG L 100 ? 0.579 0.484 0.565 -0.003 -0.108 -0.095 100 ARG LLL O   
15078 C CB  . ARG L 100 ? 0.591 0.514 0.625 -0.051 -0.084 -0.068 100 ARG LLL CB  
15079 C CG  . ARG L 100 ? 0.613 0.541 0.663 -0.079 -0.077 -0.046 100 ARG LLL CG  
15080 C CD  . ARG L 100 ? 0.656 0.569 0.723 -0.083 -0.112 -0.030 100 ARG LLL CD  
15081 N NE  . ARG L 100 ? 0.695 0.590 0.798 -0.059 -0.145 -0.044 100 ARG LLL NE  
15082 C CZ  . ARG L 100 ? 0.701 0.590 0.858 -0.061 -0.162 -0.040 100 ARG LLL CZ  
15083 N NH1 . ARG L 100 ? 0.714 0.619 0.908 -0.084 -0.145 -0.018 100 ARG LLL NH1 
15084 N NH2 . ARG L 100 ? 0.714 0.578 0.888 -0.039 -0.198 -0.058 100 ARG LLL NH2 
15085 N N   . GLY L 101 ? 0.563 0.492 0.535 -0.016 -0.069 -0.094 101 GLY LLL N   
15086 C CA  . GLY L 101 ? 0.571 0.499 0.529 0.005  -0.070 -0.103 101 GLY LLL CA  
15087 C C   . GLY L 101 ? 0.568 0.505 0.507 0.011  -0.059 -0.100 101 GLY LLL C   
15088 O O   . GLY L 101 ? 0.550 0.494 0.488 -0.004 -0.049 -0.093 101 GLY LLL O   
15089 N N   . GLU L 102 ? 0.583 0.518 0.507 0.030  -0.060 -0.106 102 GLU LLL N   
15090 C CA  . GLU L 102 ? 0.599 0.547 0.517 0.039  -0.044 -0.101 102 GLU LLL CA  
15091 C C   . GLU L 102 ? 0.581 0.538 0.489 0.041  -0.034 -0.095 102 GLU LLL C   
15092 O O   . GLU L 102 ? 0.599 0.546 0.486 0.049  -0.042 -0.100 102 GLU LLL O   
15093 C CB  . GLU L 102 ? 0.632 0.575 0.542 0.058  -0.044 -0.112 102 GLU LLL CB  
15094 C CG  . GLU L 102 ? 0.635 0.598 0.557 0.066  -0.023 -0.104 102 GLU LLL CG  
15095 C CD  . GLU L 102 ? 0.677 0.639 0.601 0.088  -0.013 -0.120 102 GLU LLL CD  
15096 O OE1 . GLU L 102 ? 0.686 0.629 0.614 0.094  -0.030 -0.137 102 GLU LLL OE1 
15097 O OE2 . GLU L 102 ? 0.704 0.685 0.633 0.098  0.014  -0.116 102 GLU LLL OE2 
15098 N N   . SER L 103 ? 0.539 0.511 0.464 0.032  -0.022 -0.084 103 SER LLL N   
15099 C CA  . SER L 103 ? 0.523 0.503 0.455 0.031  -0.017 -0.075 103 SER LLL CA  
15100 C C   . SER L 103 ? 0.532 0.524 0.453 0.042  -0.005 -0.060 103 SER LLL C   
15101 O O   . SER L 103 ? 0.512 0.516 0.447 0.045  0.007  -0.056 103 SER LLL O   
15102 C CB  . SER L 103 ? 0.511 0.496 0.472 0.016  -0.014 -0.074 103 SER LLL CB  
15103 O OG  . SER L 103 ? 0.533 0.524 0.516 0.015  -0.014 -0.065 103 SER LLL OG  
15104 N N   . TYR L 104 ? 0.541 0.533 0.444 0.045  -0.007 -0.050 104 TYR LLL N   
15105 C CA  . TYR L 104 ? 0.552 0.561 0.451 0.049  0.009  -0.027 104 TYR LLL CA  
15106 C C   . TYR L 104 ? 0.532 0.557 0.487 0.039  0.013  -0.013 104 TYR LLL C   
15107 O O   . TYR L 104 ? 0.562 0.605 0.533 0.042  0.030  0.004  104 TYR LLL O   
15108 C CB  . TYR L 104 ? 0.597 0.598 0.465 0.047  -0.002 -0.012 104 TYR LLL CB  
15109 C CG  . TYR L 104 ? 0.644 0.664 0.501 0.047  0.016  0.018  104 TYR LLL CG  
15110 C CD1 . TYR L 104 ? 0.699 0.729 0.513 0.059  0.045  0.018  104 TYR LLL CD1 
15111 C CD2 . TYR L 104 ? 0.647 0.676 0.545 0.035  0.007  0.047  104 TYR LLL CD2 
15112 C CE1 . TYR L 104 ? 0.724 0.777 0.528 0.058  0.070  0.049  104 TYR LLL CE1 
15113 C CE2 . TYR L 104 ? 0.695 0.744 0.587 0.032  0.024  0.082  104 TYR LLL CE2 
15114 C CZ  . TYR L 104 ? 0.722 0.785 0.566 0.043  0.059  0.084  104 TYR LLL CZ  
15115 O OH  . TYR L 104 ? 0.751 0.839 0.592 0.039  0.083  0.122  104 TYR LLL OH  
15116 N N   . TYR L 105 ? 0.482 0.499 0.469 0.027  -0.001 -0.022 105 TYR LLL N   
15117 C CA  . TYR L 105 ? 0.475 0.498 0.510 0.017  -0.003 -0.018 105 TYR LLL CA  
15118 C C   . TYR L 105 ? 0.486 0.501 0.518 0.011  -0.004 -0.035 105 TYR LLL C   
15119 O O   . TYR L 105 ? 0.504 0.509 0.545 -0.001 -0.011 -0.052 105 TYR LLL O   
15120 C CB  . TYR L 105 ? 0.456 0.473 0.528 0.008  -0.016 -0.022 105 TYR LLL CB  
15121 C CG  . TYR L 105 ? 0.497 0.514 0.572 0.010  -0.025 -0.002 105 TYR LLL CG  
15122 C CD1 . TYR L 105 ? 0.510 0.541 0.593 0.010  -0.024 0.032  105 TYR LLL CD1 
15123 C CD2 . TYR L 105 ? 0.494 0.497 0.572 0.009  -0.039 -0.012 105 TYR LLL CD2 
15124 C CE1 . TYR L 105 ? 0.531 0.559 0.609 0.007  -0.038 0.057  105 TYR LLL CE1 
15125 C CE2 . TYR L 105 ? 0.521 0.519 0.604 0.007  -0.058 0.010  105 TYR LLL CE2 
15126 C CZ  . TYR L 105 ? 0.546 0.554 0.621 0.005  -0.059 0.045  105 TYR LLL CZ  
15127 O OH  . TYR L 105 ? 0.592 0.591 0.664 -0.000 -0.083 0.073  105 TYR LLL OH  
15128 N N   . TYR L 106 ? 0.504 0.524 0.526 0.017  0.002  -0.031 106 TYR LLL N   
15129 C CA  . TYR L 106 ? 0.509 0.519 0.525 0.011  -0.007 -0.041 106 TYR LLL CA  
15130 C C   . TYR L 106 ? 0.504 0.507 0.542 -0.005 -0.021 -0.039 106 TYR LLL C   
15131 O O   . TYR L 106 ? 0.517 0.504 0.536 -0.017 -0.034 -0.047 106 TYR LLL O   
15132 C CB  . TYR L 106 ? 0.529 0.546 0.551 0.023  -0.001 -0.036 106 TYR LLL CB  
15133 C CG  . TYR L 106 ? 0.521 0.560 0.583 0.031  0.013  -0.015 106 TYR LLL CG  
15134 C CD1 . TYR L 106 ? 0.521 0.563 0.633 0.023  0.002  -0.001 106 TYR LLL CD1 
15135 C CD2 . TYR L 106 ? 0.526 0.582 0.577 0.046  0.037  -0.008 106 TYR LLL CD2 
15136 C CE1 . TYR L 106 ? 0.508 0.574 0.673 0.029  0.017  0.021  106 TYR LLL CE1 
15137 C CE2 . TYR L 106 ? 0.531 0.612 0.621 0.052  0.058  0.015  106 TYR LLL CE2 
15138 C CZ  . TYR L 106 ? 0.521 0.610 0.677 0.044  0.049  0.030  106 TYR LLL CZ  
15139 O OH  . TYR L 106 ? 0.530 0.647 0.741 0.050  0.071  0.056  106 TYR LLL OH  
15140 N N   . THR L 107 ? 0.510 0.418 0.433 -0.048 0.022  0.005  107 THR LLL N   
15141 C CA  . THR L 107 ? 0.482 0.404 0.433 -0.039 0.025  0.000  107 THR LLL CA  
15142 C C   . THR L 107 ? 0.468 0.398 0.437 -0.034 0.017  0.005  107 THR LLL C   
15143 O O   . THR L 107 ? 0.471 0.409 0.457 -0.028 0.019  -0.000 107 THR LLL O   
15144 C CB  . THR L 107 ? 0.487 0.406 0.441 -0.043 0.032  -0.001 107 THR LLL CB  
15145 O OG1 . THR L 107 ? 0.505 0.416 0.456 -0.048 0.026  0.009  107 THR LLL OG1 
15146 C CG2 . THR L 107 ? 0.513 0.427 0.451 -0.048 0.044  -0.005 107 THR LLL CG2 
15147 N N   . ARG L 108 ? 0.486 0.416 0.452 -0.036 0.007  0.016  108 ARG LLL N   
15148 C CA  . ARG L 108 ? 0.506 0.445 0.493 -0.029 0.002  0.022  108 ARG LLL CA  
15149 C C   . ARG L 108 ? 0.479 0.431 0.475 -0.024 0.001  0.017  108 ARG LLL C   
15150 O O   . ARG L 108 ? 0.478 0.431 0.462 -0.029 -0.003 0.018  108 ARG LLL O   
15151 C CB  . ARG L 108 ? 0.521 0.461 0.507 -0.033 -0.009 0.038  108 ARG LLL CB  
15152 C CG  . ARG L 108 ? 0.532 0.459 0.511 -0.038 -0.010 0.047  108 ARG LLL CG  
15153 C CD  . ARG L 108 ? 0.573 0.506 0.559 -0.039 -0.022 0.066  108 ARG LLL CD  
15154 N NE  . ARG L 108 ? 0.597 0.516 0.568 -0.047 -0.025 0.076  108 ARG LLL NE  
15155 C CZ  . ARG L 108 ? 0.639 0.560 0.607 -0.052 -0.039 0.095  108 ARG LLL CZ  
15156 N NH1 . ARG L 108 ? 0.662 0.605 0.646 -0.049 -0.050 0.107  108 ARG LLL NH1 
15157 N NH2 . ARG L 108 ? 0.694 0.599 0.644 -0.060 -0.042 0.105  108 ARG LLL NH2 
15158 N N   . PRO L 109 ? 0.504 0.462 0.517 -0.015 0.006  0.010  109 PRO LLL N   
15159 C CA  . PRO L 109 ? 0.483 0.452 0.503 -0.011 0.006  0.007  109 PRO LLL CA  
15160 C C   . PRO L 109 ? 0.493 0.473 0.518 -0.013 -0.002 0.018  109 PRO LLL C   
15161 O O   . PRO L 109 ? 0.499 0.485 0.518 -0.016 -0.004 0.016  109 PRO LLL O   
15162 C CB  . PRO L 109 ? 0.466 0.435 0.501 -0.004 0.013  -0.000 109 PRO LLL CB  
15163 C CG  . PRO L 109 ? 0.465 0.422 0.495 -0.007 0.017  -0.005 109 PRO LLL CG  
15164 C CD  . PRO L 109 ? 0.487 0.438 0.509 -0.012 0.013  0.005  109 PRO LLL CD  
15165 N N   . THR L 110 ? 0.462 0.446 0.500 -0.011 -0.006 0.030  110 THR LLL N   
15166 C CA  . THR L 110 ? 0.454 0.456 0.504 -0.012 -0.014 0.044  110 THR LLL CA  
15167 C C   . THR L 110 ? 0.462 0.465 0.489 -0.027 -0.025 0.050  110 THR LLL C   
15168 O O   . THR L 110 ? 0.452 0.473 0.487 -0.032 -0.033 0.060  110 THR LLL O   
15169 C CB  . THR L 110 ? 0.478 0.485 0.549 -0.004 -0.017 0.059  110 THR LLL CB  
15170 O OG1 . THR L 110 ? 0.500 0.489 0.554 -0.011 -0.021 0.063  110 THR LLL OG1 
15171 C CG2 . THR L 110 ? 0.476 0.480 0.569 0.011  -0.004 0.053  110 THR LLL CG2 
15172 N N   . GLU L 111 ? 0.483 0.467 0.483 -0.035 -0.024 0.043  111 GLU LLL N   
15173 C CA  . GLU L 111 ? 0.534 0.509 0.504 -0.051 -0.031 0.046  111 GLU LLL CA  
15174 C C   . GLU L 111 ? 0.542 0.514 0.501 -0.053 -0.027 0.036  111 GLU LLL C   
15175 O O   . GLU L 111 ? 0.562 0.523 0.494 -0.067 -0.032 0.037  111 GLU LLL O   
15176 C CB  . GLU L 111 ? 0.544 0.496 0.487 -0.059 -0.028 0.043  111 GLU LLL CB  
15177 C CG  . GLU L 111 ? 0.565 0.517 0.510 -0.062 -0.034 0.056  111 GLU LLL CG  
15178 C CD  . GLU L 111 ? 0.596 0.559 0.536 -0.075 -0.050 0.073  111 GLU LLL CD  
15179 O OE1 . GLU L 111 ? 0.565 0.552 0.530 -0.071 -0.057 0.083  111 GLU LLL OE1 
15180 O OE2 . GLU L 111 ? 0.677 0.624 0.586 -0.090 -0.055 0.078  111 GLU LLL OE2 
15181 N N   . TYR L 112 ? 0.503 0.482 0.479 -0.042 -0.020 0.027  112 TYR LLL N   
15182 C CA  . TYR L 112 ? 0.478 0.452 0.442 -0.043 -0.017 0.020  112 TYR LLL CA  
15183 C C   . TYR L 112 ? 0.468 0.464 0.453 -0.040 -0.018 0.023  112 TYR LLL C   
15184 O O   . TYR L 112 ? 0.477 0.484 0.486 -0.029 -0.013 0.021  112 TYR LLL O   
15185 C CB  . TYR L 112 ? 0.511 0.474 0.472 -0.034 -0.008 0.007  112 TYR LLL CB  
15186 C CG  . TYR L 112 ? 0.518 0.463 0.462 -0.036 -0.003 0.004  112 TYR LLL CG  
15187 C CD1 . TYR L 112 ? 0.481 0.426 0.433 -0.033 -0.001 0.005  112 TYR LLL CD1 
15188 C CD2 . TYR L 112 ? 0.557 0.481 0.473 -0.041 0.000  0.000  112 TYR LLL CD2 
15189 C CE1 . TYR L 112 ? 0.502 0.433 0.439 -0.036 0.005  0.002  112 TYR LLL CE1 
15190 C CE2 . TYR L 112 ? 0.546 0.454 0.447 -0.042 0.008  -0.003 112 TYR LLL CE2 
15191 C CZ  . TYR L 112 ? 0.517 0.430 0.429 -0.040 0.010  -0.002 112 TYR LLL CZ  
15192 O OH  . TYR L 112 ? 0.490 0.388 0.385 -0.043 0.019  -0.005 112 TYR LLL OH  
15193 N N   . GLU L 113 ? 0.487 0.488 0.463 -0.051 -0.024 0.028  113 GLU LLL N   
15194 C CA  . GLU L 113 ? 0.484 0.510 0.482 -0.050 -0.025 0.033  113 GLU LLL CA  
15195 C C   . GLU L 113 ? 0.487 0.509 0.485 -0.043 -0.016 0.022  113 GLU LLL C   
15196 O O   . GLU L 113 ? 0.443 0.483 0.463 -0.036 -0.010 0.022  113 GLU LLL O   
15197 C CB  . GLU L 113 ? 0.519 0.553 0.505 -0.068 -0.034 0.042  113 GLU LLL CB  
15198 C CG  . GLU L 113 ? 0.546 0.610 0.558 -0.068 -0.034 0.049  113 GLU LLL CG  
15199 C CD  . GLU L 113 ? 0.600 0.680 0.606 -0.088 -0.045 0.061  113 GLU LLL CD  
15200 O OE1 . GLU L 113 ? 0.575 0.639 0.554 -0.104 -0.054 0.064  113 GLU LLL OE1 
15201 O OE2 . GLU L 113 ? 0.652 0.759 0.679 -0.091 -0.043 0.066  113 GLU LLL OE2 
15202 N N   . PHE L 114 ? 0.486 0.486 0.459 -0.044 -0.014 0.013  114 PHE LLL N   
15203 C CA  . PHE L 114 ? 0.475 0.471 0.443 -0.041 -0.009 0.006  114 PHE LLL CA  
15204 C C   . PHE L 114 ? 0.495 0.482 0.464 -0.029 -0.003 -0.003 114 PHE LLL C   
15205 O O   . PHE L 114 ? 0.535 0.508 0.495 -0.027 -0.003 -0.005 114 PHE LLL O   
15206 C CB  . PHE L 114 ? 0.485 0.462 0.424 -0.051 -0.012 0.007  114 PHE LLL CB  
15207 C CG  . PHE L 114 ? 0.476 0.464 0.412 -0.067 -0.018 0.016  114 PHE LLL CG  
15208 C CD1 . PHE L 114 ? 0.482 0.497 0.439 -0.068 -0.017 0.020  114 PHE LLL CD1 
15209 C CD2 . PHE L 114 ? 0.510 0.484 0.424 -0.081 -0.025 0.020  114 PHE LLL CD2 
15210 C CE1 . PHE L 114 ? 0.485 0.517 0.444 -0.083 -0.023 0.030  114 PHE LLL CE1 
15211 C CE2 . PHE L 114 ? 0.524 0.512 0.437 -0.098 -0.033 0.030  114 PHE LLL CE2 
15212 C CZ  . PHE L 114 ? 0.520 0.540 0.458 -0.099 -0.032 0.036  114 PHE LLL CZ  
15213 N N   . TRP L 115 ? 0.472 0.467 0.450 -0.024 0.001  -0.008 115 TRP LLL N   
15214 C CA  . TRP L 115 ? 0.460 0.452 0.442 -0.017 0.005  -0.016 115 TRP LLL CA  
15215 C C   . TRP L 115 ? 0.450 0.441 0.421 -0.017 0.005  -0.019 115 TRP LLL C   
15216 O O   . TRP L 115 ? 0.472 0.471 0.445 -0.021 0.007  -0.019 115 TRP LLL O   
15217 C CB  . TRP L 115 ? 0.464 0.466 0.465 -0.012 0.010  -0.018 115 TRP LLL CB  
15218 C CG  . TRP L 115 ? 0.463 0.462 0.471 -0.011 0.008  -0.014 115 TRP LLL CG  
15219 C CD1 . TRP L 115 ? 0.468 0.474 0.483 -0.013 0.005  -0.005 115 TRP LLL CD1 
15220 C CD2 . TRP L 115 ? 0.469 0.460 0.477 -0.008 0.009  -0.017 115 TRP LLL CD2 
15221 N NE1 . TRP L 115 ? 0.480 0.480 0.496 -0.013 0.003  -0.002 115 TRP LLL NE1 
15222 C CE2 . TRP L 115 ? 0.480 0.470 0.492 -0.010 0.007  -0.009 115 TRP LLL CE2 
15223 C CE3 . TRP L 115 ? 0.517 0.505 0.523 -0.006 0.011  -0.023 115 TRP LLL CE3 
15224 C CZ2 . TRP L 115 ? 0.486 0.469 0.498 -0.009 0.008  -0.010 115 TRP LLL CZ2 
15225 C CZ3 . TRP L 115 ? 0.524 0.508 0.533 -0.006 0.013  -0.024 115 TRP LLL CZ3 
15226 C CH2 . TRP L 115 ? 0.516 0.496 0.526 -0.007 0.012  -0.017 115 TRP LLL CH2 
15227 N N   . GLY L 116 ? 0.438 0.421 0.401 -0.014 0.003  -0.021 116 GLY LLL N   
15228 C CA  . GLY L 116 ? 0.493 0.479 0.450 -0.014 0.001  -0.024 116 GLY LLL CA  
15229 C C   . GLY L 116 ? 0.475 0.470 0.440 -0.015 0.005  -0.030 116 GLY LLL C   
15230 O O   . GLY L 116 ? 0.513 0.511 0.491 -0.014 0.009  -0.033 116 GLY LLL O   
15231 N N   . GLN L 117 ? 0.504 0.501 0.459 -0.019 0.003  -0.033 117 GLN LLL N   
15232 C CA  . GLN L 117 ? 0.526 0.527 0.480 -0.024 0.008  -0.041 117 GLN LLL CA  
15233 C C   . GLN L 117 ? 0.526 0.531 0.485 -0.024 0.003  -0.042 117 GLN LLL C   
15234 O O   . GLN L 117 ? 0.529 0.533 0.487 -0.029 0.006  -0.050 117 GLN LLL O   
15235 C CB  . GLN L 117 ? 0.512 0.512 0.447 -0.032 0.008  -0.042 117 GLN LLL CB  
15236 C CG  . GLN L 117 ? 0.559 0.558 0.489 -0.034 0.013  -0.040 117 GLN LLL CG  
15237 C CD  . GLN L 117 ? 0.576 0.580 0.523 -0.031 0.025  -0.043 117 GLN LLL CD  
15238 O OE1 . GLN L 117 ? 0.612 0.614 0.562 -0.031 0.034  -0.051 117 GLN LLL OE1 
15239 N NE2 . GLN L 117 ? 0.533 0.542 0.488 -0.030 0.025  -0.036 117 GLN LLL NE2 
15240 N N   . GLY L 118 ? 0.492 0.500 0.456 -0.018 -0.004 -0.036 118 GLY LLL N   
15241 C CA  . GLY L 118 ? 0.514 0.532 0.488 -0.017 -0.009 -0.035 118 GLY LLL CA  
15242 C C   . GLY L 118 ? 0.527 0.555 0.495 -0.021 -0.019 -0.031 118 GLY LLL C   
15243 O O   . GLY L 118 ? 0.517 0.542 0.469 -0.028 -0.021 -0.031 118 GLY LLL O   
15244 N N   . THR L 119 ? 0.516 0.560 0.499 -0.018 -0.024 -0.026 119 THR LLL N   
15245 C CA  . THR L 119 ? 0.520 0.582 0.504 -0.022 -0.036 -0.018 119 THR LLL CA  
15246 C C   . THR L 119 ? 0.503 0.584 0.503 -0.028 -0.039 -0.020 119 THR LLL C   
15247 O O   . THR L 119 ? 0.477 0.560 0.494 -0.022 -0.032 -0.021 119 THR LLL O   
15248 C CB  . THR L 119 ? 0.531 0.593 0.520 -0.008 -0.041 -0.006 119 THR LLL CB  
15249 O OG1 . THR L 119 ? 0.546 0.625 0.534 -0.011 -0.054 0.004  119 THR LLL OG1 
15250 C CG2 . THR L 119 ? 0.533 0.600 0.544 0.006  -0.035 -0.002 119 THR LLL CG2 
15251 N N   . GLN L 120 ? 0.511 0.605 0.504 -0.042 -0.049 -0.019 120 GLN LLL N   
15252 C CA  . GLN L 120 ? 0.520 0.635 0.526 -0.054 -0.053 -0.020 120 GLN LLL CA  
15253 C C   . GLN L 120 ? 0.517 0.663 0.554 -0.044 -0.060 -0.006 120 GLN LLL C   
15254 O O   . GLN L 120 ? 0.566 0.722 0.606 -0.036 -0.070 0.006  120 GLN LLL O   
15255 C CB  . GLN L 120 ? 0.547 0.664 0.529 -0.076 -0.063 -0.024 120 GLN LLL CB  
15256 C CG  . GLN L 120 ? 0.565 0.697 0.552 -0.095 -0.067 -0.027 120 GLN LLL CG  
15257 C CD  . GLN L 120 ? 0.593 0.704 0.578 -0.098 -0.052 -0.041 120 GLN LLL CD  
15258 O OE1 . GLN L 120 ? 0.574 0.653 0.539 -0.097 -0.040 -0.052 120 GLN LLL OE1 
15259 N NE2 . GLN L 120 ? 0.652 0.780 0.659 -0.100 -0.052 -0.038 120 GLN LLL NE2 
15260 N N   . VAL L 121 ? 0.489 0.646 0.546 -0.043 -0.055 -0.007 121 VAL LLL N   
15261 C CA  . VAL L 121 ? 0.486 0.681 0.577 -0.038 -0.060 0.005  121 VAL LLL CA  
15262 C C   . VAL L 121 ? 0.492 0.707 0.586 -0.061 -0.067 0.002  121 VAL LLL C   
15263 O O   . VAL L 121 ? 0.531 0.726 0.614 -0.071 -0.057 -0.011 121 VAL LLL O   
15264 C CB  . VAL L 121 ? 0.478 0.669 0.589 -0.020 -0.046 0.006  121 VAL LLL CB  
15265 C CG1 . VAL L 121 ? 0.493 0.725 0.641 -0.015 -0.047 0.018  121 VAL LLL CG1 
15266 C CG2 . VAL L 121 ? 0.476 0.643 0.578 -0.000 -0.039 0.008  121 VAL LLL CG2 
15267 N N   . THR L 122 ? 0.486 0.737 0.594 -0.071 -0.083 0.014  122 THR LLL N   
15268 C CA  . THR L 122 ? 0.515 0.789 0.625 -0.097 -0.091 0.012  122 THR LLL CA  
15269 C C   . THR L 122 ? 0.508 0.834 0.664 -0.091 -0.098 0.029  122 THR LLL C   
15270 O O   . THR L 122 ? 0.497 0.850 0.672 -0.078 -0.108 0.046  122 THR LLL O   
15271 C CB  . THR L 122 ? 0.547 0.816 0.624 -0.121 -0.106 0.010  122 THR LLL CB  
15272 O OG1 . THR L 122 ? 0.546 0.767 0.585 -0.122 -0.095 -0.006 122 THR LLL OG1 
15273 C CG2 . THR L 122 ? 0.552 0.840 0.624 -0.152 -0.116 0.008  122 THR LLL CG2 
15274 N N   . VAL L 123 ? 0.506 0.845 0.678 -0.100 -0.090 0.026  123 VAL LLL N   
15275 C CA  . VAL L 123 ? 0.538 0.931 0.757 -0.097 -0.093 0.041  123 VAL LLL CA  
15276 C C   . VAL L 123 ? 0.602 1.024 0.821 -0.132 -0.108 0.043  123 VAL LLL C   
15277 O O   . VAL L 123 ? 0.659 1.057 0.857 -0.151 -0.100 0.028  123 VAL LLL O   
15278 C CB  . VAL L 123 ? 0.500 0.884 0.737 -0.081 -0.071 0.036  123 VAL LLL CB  
15279 C CG1 . VAL L 123 ? 0.505 0.944 0.794 -0.072 -0.069 0.053  123 VAL LLL CG1 
15280 C CG2 . VAL L 123 ? 0.489 0.833 0.712 -0.055 -0.057 0.031  123 VAL LLL CG2 
15281 N N   . SER L 124 ? 0.653 1.121 0.889 -0.141 -0.129 0.060  124 SER LLL N   
15282 C CA  . SER L 124 ? 0.767 1.270 1.004 -0.177 -0.147 0.065  124 SER LLL CA  
15283 C C   . SER L 124 ? 0.851 1.405 1.139 -0.178 -0.142 0.075  124 SER LLL C   
15284 O O   . SER L 124 ? 0.808 1.381 1.135 -0.146 -0.129 0.084  124 SER LLL O   
15285 C CB  . SER L 124 ? 0.776 1.312 1.013 -0.188 -0.174 0.081  124 SER LLL CB  
15286 O OG  . SER L 124 ? 0.768 1.347 1.052 -0.158 -0.178 0.104  124 SER LLL OG  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   PRO 1   330 ?   ?   ?   AAA . n 
A 1 2   ASN 2   331 331 ASN ASN AAA . n 
A 1 3   ILE 3   332 332 ILE ILE AAA . n 
A 1 4   THR 4   333 333 THR THR AAA . n 
A 1 5   ASN 5   334 334 ASN ASN AAA . n 
A 1 6   LEU 6   335 335 LEU LEU AAA . n 
A 1 7   CYS 7   336 336 CYS CYS AAA . n 
A 1 8   PRO 8   337 337 PRO PRO AAA . n 
A 1 9   PHE 9   338 338 PHE PHE AAA . n 
A 1 10  GLY 10  339 339 GLY GLY AAA . n 
A 1 11  GLU 11  340 340 GLU GLU AAA . n 
A 1 12  VAL 12  341 341 VAL VAL AAA . n 
A 1 13  PHE 13  342 342 PHE PHE AAA . n 
A 1 14  ASN 14  343 343 ASN ASN AAA . n 
A 1 15  ALA 15  344 344 ALA ALA AAA . n 
A 1 16  THR 16  345 345 THR THR AAA . n 
A 1 17  ARG 17  346 346 ARG ARG AAA . n 
A 1 18  PHE 18  347 347 PHE PHE AAA . n 
A 1 19  ALA 19  348 348 ALA ALA AAA . n 
A 1 20  SER 20  349 349 SER SER AAA . n 
A 1 21  VAL 21  350 350 VAL VAL AAA . n 
A 1 22  TYR 22  351 351 TYR TYR AAA . n 
A 1 23  ALA 23  352 352 ALA ALA AAA . n 
A 1 24  TRP 24  353 353 TRP TRP AAA . n 
A 1 25  ASN 25  354 354 ASN ASN AAA . n 
A 1 26  ARG 26  355 355 ARG ARG AAA . n 
A 1 27  LYS 27  356 356 LYS LYS AAA . n 
A 1 28  ARG 28  357 357 ARG ARG AAA . n 
A 1 29  ILE 29  358 358 ILE ILE AAA . n 
A 1 30  SER 30  359 359 SER SER AAA . n 
A 1 31  ASN 31  360 360 ASN ASN AAA . n 
A 1 32  CYS 32  361 361 CYS CYS AAA . n 
A 1 33  VAL 33  362 362 VAL VAL AAA . n 
A 1 34  ALA 34  363 363 ALA ALA AAA . n 
A 1 35  ASP 35  364 364 ASP ASP AAA . n 
A 1 36  TYR 36  365 365 TYR TYR AAA . n 
A 1 37  SER 37  366 366 SER SER AAA . n 
A 1 38  VAL 38  367 367 VAL VAL AAA . n 
A 1 39  LEU 39  368 368 LEU LEU AAA . n 
A 1 40  TYR 40  369 369 TYR TYR AAA . n 
A 1 41  ASN 41  370 370 ASN ASN AAA . n 
A 1 42  SER 42  371 371 SER SER AAA . n 
A 1 43  ALA 43  372 372 ALA ALA AAA . n 
A 1 44  SER 44  373 373 SER SER AAA . n 
A 1 45  PHE 45  374 374 PHE PHE AAA . n 
A 1 46  SER 46  375 375 SER SER AAA . n 
A 1 47  THR 47  376 376 THR THR AAA . n 
A 1 48  PHE 48  377 377 PHE PHE AAA . n 
A 1 49  LYS 49  378 378 LYS LYS AAA . n 
A 1 50  CYS 50  379 379 CYS CYS AAA . n 
A 1 51  TYR 51  380 380 TYR TYR AAA . n 
A 1 52  GLY 52  381 381 GLY GLY AAA . n 
A 1 53  VAL 53  382 382 VAL VAL AAA . n 
A 1 54  SER 54  383 383 SER SER AAA . n 
A 1 55  PRO 55  384 384 PRO PRO AAA . n 
A 1 56  THR 56  385 385 THR THR AAA . n 
A 1 57  LYS 57  386 386 LYS LYS AAA . n 
A 1 58  LEU 58  387 387 LEU LEU AAA . n 
A 1 59  ASN 59  388 388 ASN ASN AAA . n 
A 1 60  ASP 60  389 389 ASP ASP AAA . n 
A 1 61  LEU 61  390 390 LEU LEU AAA . n 
A 1 62  CYS 62  391 391 CYS CYS AAA . n 
A 1 63  PHE 63  392 392 PHE PHE AAA . n 
A 1 64  THR 64  393 393 THR THR AAA . n 
A 1 65  ASN 65  394 394 ASN ASN AAA . n 
A 1 66  VAL 66  395 395 VAL VAL AAA . n 
A 1 67  TYR 67  396 396 TYR TYR AAA . n 
A 1 68  ALA 68  397 397 ALA ALA AAA . n 
A 1 69  ASP 69  398 398 ASP ASP AAA . n 
A 1 70  SER 70  399 399 SER SER AAA . n 
A 1 71  PHE 71  400 400 PHE PHE AAA . n 
A 1 72  VAL 72  401 401 VAL VAL AAA . n 
A 1 73  ILE 73  402 402 ILE ILE AAA . n 
A 1 74  ARG 74  403 403 ARG ARG AAA . n 
A 1 75  GLY 75  404 404 GLY GLY AAA . n 
A 1 76  ASP 76  405 405 ASP ASP AAA . n 
A 1 77  GLU 77  406 406 GLU GLU AAA . n 
A 1 78  VAL 78  407 407 VAL VAL AAA . n 
A 1 79  ARG 79  408 408 ARG ARG AAA . n 
A 1 80  GLN 80  409 409 GLN GLN AAA . n 
A 1 81  ILE 81  410 410 ILE ILE AAA . n 
A 1 82  ALA 82  411 411 ALA ALA AAA . n 
A 1 83  PRO 83  412 412 PRO PRO AAA . n 
A 1 84  GLY 84  413 413 GLY GLY AAA . n 
A 1 85  GLN 85  414 414 GLN GLN AAA . n 
A 1 86  THR 86  415 415 THR THR AAA . n 
A 1 87  GLY 87  416 416 GLY GLY AAA . n 
A 1 88  LYS 88  417 417 LYS LYS AAA . n 
A 1 89  ILE 89  418 418 ILE ILE AAA . n 
A 1 90  ALA 90  419 419 ALA ALA AAA . n 
A 1 91  ASP 91  420 420 ASP ASP AAA . n 
A 1 92  TYR 92  421 421 TYR TYR AAA . n 
A 1 93  ASN 93  422 422 ASN ASN AAA . n 
A 1 94  TYR 94  423 423 TYR TYR AAA . n 
A 1 95  LYS 95  424 424 LYS LYS AAA . n 
A 1 96  LEU 96  425 425 LEU LEU AAA . n 
A 1 97  PRO 97  426 426 PRO PRO AAA . n 
A 1 98  ASP 98  427 427 ASP ASP AAA . n 
A 1 99  ASP 99  428 428 ASP ASP AAA . n 
A 1 100 PHE 100 429 429 PHE PHE AAA . n 
A 1 101 THR 101 430 430 THR THR AAA . n 
A 1 102 GLY 102 431 431 GLY GLY AAA . n 
A 1 103 CYS 103 432 432 CYS CYS AAA . n 
A 1 104 VAL 104 433 433 VAL VAL AAA . n 
A 1 105 ILE 105 434 434 ILE ILE AAA . n 
A 1 106 ALA 106 435 435 ALA ALA AAA . n 
A 1 107 TRP 107 436 436 TRP TRP AAA . n 
A 1 108 ASN 108 437 437 ASN ASN AAA . n 
A 1 109 SER 109 438 438 SER SER AAA . n 
A 1 110 ASN 110 439 439 ASN ASN AAA . n 
A 1 111 ASN 111 440 440 ASN ASN AAA . n 
A 1 112 LEU 112 441 441 LEU LEU AAA . n 
A 1 113 ASP 113 442 442 ASP ASP AAA . n 
A 1 114 SER 114 443 443 SER SER AAA . n 
A 1 115 LYS 115 444 444 LYS LYS AAA . n 
A 1 116 VAL 116 445 445 VAL VAL AAA . n 
A 1 117 GLY 117 446 446 GLY GLY AAA . n 
A 1 118 GLY 118 447 447 GLY GLY AAA . n 
A 1 119 ASN 119 448 448 ASN ASN AAA . n 
A 1 120 TYR 120 449 449 TYR TYR AAA . n 
A 1 121 ASN 121 450 450 ASN ASN AAA . n 
A 1 122 TYR 122 451 451 TYR TYR AAA . n 
A 1 123 LEU 123 452 452 LEU LEU AAA . n 
A 1 124 TYR 124 453 453 TYR TYR AAA . n 
A 1 125 ARG 125 454 454 ARG ARG AAA . n 
A 1 126 LEU 126 455 455 LEU LEU AAA . n 
A 1 127 PHE 127 456 456 PHE PHE AAA . n 
A 1 128 ARG 128 457 457 ARG ARG AAA . n 
A 1 129 LYS 129 458 458 LYS LYS AAA . n 
A 1 130 SER 130 459 459 SER SER AAA . n 
A 1 131 ASN 131 460 460 ASN ASN AAA . n 
A 1 132 LEU 132 461 461 LEU LEU AAA . n 
A 1 133 LYS 133 462 462 LYS LYS AAA . n 
A 1 134 PRO 134 463 463 PRO PRO AAA . n 
A 1 135 PHE 135 464 464 PHE PHE AAA . n 
A 1 136 GLU 136 465 465 GLU GLU AAA . n 
A 1 137 ARG 137 466 466 ARG ARG AAA . n 
A 1 138 ASP 138 467 467 ASP ASP AAA . n 
A 1 139 ILE 139 468 468 ILE ILE AAA . n 
A 1 140 SER 140 469 469 SER SER AAA . n 
A 1 141 THR 141 470 470 THR THR AAA . n 
A 1 142 GLU 142 471 471 GLU GLU AAA . n 
A 1 143 ILE 143 472 472 ILE ILE AAA . n 
A 1 144 TYR 144 473 473 TYR TYR AAA . n 
A 1 145 GLN 145 474 474 GLN GLN AAA . n 
A 1 146 ALA 146 475 475 ALA ALA AAA . n 
A 1 147 GLY 147 476 476 GLY GLY AAA . n 
A 1 148 SER 148 477 477 SER SER AAA . n 
A 1 149 THR 149 478 478 THR THR AAA . n 
A 1 150 PRO 150 479 479 PRO PRO AAA . n 
A 1 151 CYS 151 480 480 CYS CYS AAA . n 
A 1 152 ASN 152 481 481 ASN ASN AAA . n 
A 1 153 GLY 153 482 482 GLY GLY AAA . n 
A 1 154 VAL 154 483 483 VAL VAL AAA . n 
A 1 155 GLU 155 484 484 GLU GLU AAA . n 
A 1 156 GLY 156 485 485 GLY GLY AAA . n 
A 1 157 PHE 157 486 486 PHE PHE AAA . n 
A 1 158 ASN 158 487 487 ASN ASN AAA . n 
A 1 159 CYS 159 488 488 CYS CYS AAA . n 
A 1 160 TYR 160 489 489 TYR TYR AAA . n 
A 1 161 PHE 161 490 490 PHE PHE AAA . n 
A 1 162 PRO 162 491 491 PRO PRO AAA . n 
A 1 163 LEU 163 492 492 LEU LEU AAA . n 
A 1 164 GLN 164 493 493 GLN GLN AAA . n 
A 1 165 SER 165 494 494 SER SER AAA . n 
A 1 166 TYR 166 495 495 TYR TYR AAA . n 
A 1 167 GLY 167 496 496 GLY GLY AAA . n 
A 1 168 PHE 168 497 497 PHE PHE AAA . n 
A 1 169 GLN 169 498 498 GLN GLN AAA . n 
A 1 170 PRO 170 499 499 PRO PRO AAA . n 
A 1 171 THR 171 500 500 THR THR AAA . n 
A 1 172 ASN 172 501 501 ASN ASN AAA . n 
A 1 173 GLY 173 502 502 GLY GLY AAA . n 
A 1 174 VAL 174 503 503 VAL VAL AAA . n 
A 1 175 GLY 175 504 504 GLY GLY AAA . n 
A 1 176 TYR 176 505 505 TYR TYR AAA . n 
A 1 177 GLN 177 506 506 GLN GLN AAA . n 
A 1 178 PRO 178 507 507 PRO PRO AAA . n 
A 1 179 TYR 179 508 508 TYR TYR AAA . n 
A 1 180 ARG 180 509 509 ARG ARG AAA . n 
A 1 181 VAL 181 510 510 VAL VAL AAA . n 
A 1 182 VAL 182 511 511 VAL VAL AAA . n 
A 1 183 VAL 183 512 512 VAL VAL AAA . n 
A 1 184 LEU 184 513 513 LEU LEU AAA . n 
A 1 185 SER 185 514 514 SER SER AAA . n 
A 1 186 PHE 186 515 515 PHE PHE AAA . n 
A 1 187 GLU 187 516 516 GLU GLU AAA . n 
A 1 188 LEU 188 517 517 LEU LEU AAA . n 
A 1 189 LEU 189 518 518 LEU LEU AAA . n 
A 1 190 HIS 190 519 519 HIS HIS AAA . n 
A 1 191 ALA 191 520 520 ALA ALA AAA . n 
A 1 192 PRO 192 521 521 PRO PRO AAA . n 
A 1 193 ALA 193 522 522 ALA ALA AAA . n 
A 1 194 THR 194 523 523 THR THR AAA . n 
A 1 195 VAL 195 524 524 VAL VAL AAA . n 
A 1 196 CYS 196 525 525 CYS CYS AAA . n 
A 1 197 GLY 197 526 526 GLY GLY AAA . n 
A 1 198 PRO 198 527 527 PRO PRO AAA . n 
A 1 199 LYS 199 528 528 LYS LYS AAA . n 
A 1 200 LYS 200 529 ?   ?   ?   AAA . n 
A 1 201 SER 201 530 ?   ?   ?   AAA . n 
A 1 202 THR 202 531 ?   ?   ?   AAA . n 
A 1 203 ASN 203 532 ?   ?   ?   AAA . n 
A 1 204 LYS 204 533 ?   ?   ?   AAA . n 
A 1 205 HIS 205 534 ?   ?   ?   AAA . n 
A 1 206 HIS 206 535 ?   ?   ?   AAA . n 
A 1 207 HIS 207 536 ?   ?   ?   AAA . n 
A 1 208 HIS 208 537 ?   ?   ?   AAA . n 
A 1 209 HIS 209 538 ?   ?   ?   AAA . n 
A 1 210 HIS 210 539 ?   ?   ?   AAA . n 
B 2 1   GLN 1   1   1   GLN GLN BBB . n 
B 2 2   VAL 2   2   2   VAL VAL BBB . n 
B 2 3   GLN 3   3   3   GLN GLN BBB . n 
B 2 4   LEU 4   4   4   LEU LEU BBB . n 
B 2 5   VAL 5   5   5   VAL VAL BBB . n 
B 2 6   GLU 6   6   6   GLU GLU BBB . n 
B 2 7   SER 7   7   7   SER SER BBB . n 
B 2 8   GLY 8   8   8   GLY GLY BBB . n 
B 2 9   GLY 9   9   9   GLY GLY BBB . n 
B 2 10  GLY 10  10  10  GLY GLY BBB . n 
B 2 11  LEU 11  11  11  LEU LEU BBB . n 
B 2 12  VAL 12  12  12  VAL VAL BBB . n 
B 2 13  GLN 13  13  13  GLN GLN BBB . n 
B 2 14  ALA 14  14  14  ALA ALA BBB . n 
B 2 15  GLY 15  15  15  GLY GLY BBB . n 
B 2 16  GLY 16  16  16  GLY GLY BBB . n 
B 2 17  SER 17  17  17  SER SER BBB . n 
B 2 18  LEU 18  18  18  LEU LEU BBB . n 
B 2 19  ARG 19  19  19  ARG ARG BBB . n 
B 2 20  LEU 20  20  20  LEU LEU BBB . n 
B 2 21  ALA 21  21  21  ALA ALA BBB . n 
B 2 22  CYS 22  22  22  CYS CYS BBB . n 
B 2 23  ILE 23  23  23  ILE ILE BBB . n 
B 2 24  ALA 24  24  24  ALA ALA BBB . n 
B 2 25  SER 25  25  25  SER SER BBB . n 
B 2 26  GLY 26  26  26  GLY GLY BBB . n 
B 2 27  ARG 27  27  27  ARG ARG BBB . n 
B 2 28  THR 28  28  28  THR THR BBB . n 
B 2 29  PHE 29  29  29  PHE PHE BBB . n 
B 2 30  HIS 30  30  30  HIS HIS BBB . n 
B 2 31  SER 31  31  31  SER SER BBB . n 
B 2 32  TYR 32  32  32  TYR TYR BBB . n 
B 2 33  VAL 33  33  33  VAL VAL BBB . n 
B 2 34  MET 34  34  34  MET MET BBB . n 
B 2 35  ALA 35  35  35  ALA ALA BBB . n 
B 2 36  TRP 36  36  36  TRP TRP BBB . n 
B 2 37  PHE 37  37  37  PHE PHE BBB . n 
B 2 38  ARG 38  38  38  ARG ARG BBB . n 
B 2 39  GLN 39  39  39  GLN GLN BBB . n 
B 2 40  ALA 40  40  40  ALA ALA BBB . n 
B 2 41  PRO 41  41  41  PRO PRO BBB . n 
B 2 42  GLY 42  42  42  GLY GLY BBB . n 
B 2 43  LYS 43  43  43  LYS LYS BBB . n 
B 2 44  GLU 44  44  44  GLU GLU BBB . n 
B 2 45  ARG 45  45  45  ARG ARG BBB . n 
B 2 46  GLU 46  46  46  GLU GLU BBB . n 
B 2 47  PHE 47  47  47  PHE PHE BBB . n 
B 2 48  VAL 48  48  48  VAL VAL BBB . n 
B 2 49  ALA 49  49  49  ALA ALA BBB . n 
B 2 50  ALA 50  50  50  ALA ALA BBB . n 
B 2 51  ILE 51  51  51  ILE ILE BBB . n 
B 2 52  SER 52  52  52  SER SER BBB . n 
B 2 53  TRP 53  53  53  TRP TRP BBB . n 
B 2 54  SER 54  54  54  SER SER BBB . n 
B 2 55  SER 55  55  55  SER SER BBB . n 
B 2 56  THR 56  56  56  THR THR BBB . n 
B 2 57  PRO 57  57  57  PRO PRO BBB . n 
B 2 58  THR 58  58  58  THR THR BBB . n 
B 2 59  TYR 59  59  59  TYR TYR BBB . n 
B 2 60  TYR 60  60  60  TYR TYR BBB . n 
B 2 61  GLY 61  61  61  GLY GLY BBB . n 
B 2 62  GLU 62  62  62  GLU GLU BBB . n 
B 2 63  SER 63  63  63  SER SER BBB . n 
B 2 64  VAL 64  64  64  VAL VAL BBB . n 
B 2 65  LYS 65  65  65  LYS LYS BBB . n 
B 2 66  GLY 66  66  66  GLY GLY BBB . n 
B 2 67  ARG 67  67  67  ARG ARG BBB . n 
B 2 68  PHE 68  68  68  PHE PHE BBB . n 
B 2 69  THR 69  69  69  THR THR BBB . n 
B 2 70  ILE 70  70  70  ILE ILE BBB . n 
B 2 71  SER 71  71  71  SER SER BBB . n 
B 2 72  ARG 72  72  72  ARG ARG BBB . n 
B 2 73  ASP 73  73  73  ASP ASP BBB . n 
B 2 74  ASN 74  74  74  ASN ASN BBB . n 
B 2 75  ALA 75  75  75  ALA ALA BBB . n 
B 2 76  LYS 76  76  76  LYS LYS BBB . n 
B 2 77  ASN 77  77  77  ASN ASN BBB . n 
B 2 78  THR 78  78  78  THR THR BBB . n 
B 2 79  VAL 79  79  79  VAL VAL BBB . n 
B 2 80  TYR 80  80  80  TYR TYR BBB . n 
B 2 81  LEU 81  81  81  LEU LEU BBB . n 
B 2 82  GLN 82  82  82  GLN GLN BBB . n 
B 2 83  MET 83  83  83  MET MET BBB . n 
B 2 84  ASN 84  84  84  ASN ASN BBB . n 
B 2 85  ARG 85  85  85  ARG ARG BBB . n 
B 2 86  LEU 86  86  86  LEU LEU BBB . n 
B 2 87  LYS 87  87  87  LYS LYS BBB . n 
B 2 88  PRO 88  88  88  PRO PRO BBB . n 
B 2 89  GLU 89  89  89  GLU GLU BBB . n 
B 2 90  ASP 90  90  90  ASP ASP BBB . n 
B 2 91  THR 91  91  91  THR THR BBB . n 
B 2 92  ALA 92  92  92  ALA ALA BBB . n 
B 2 93  VAL 93  93  93  VAL VAL BBB . n 
B 2 94  TYR 94  94  94  TYR TYR BBB . n 
B 2 95  PHE 95  95  95  PHE PHE BBB . n 
B 2 96  CYS 96  96  96  CYS CYS BBB . n 
B 2 97  ALA 97  97  97  ALA ALA BBB . n 
B 2 98  ALA 98  98  98  ALA ALA BBB . n 
B 2 99  ASP 99  99  99  ASP ASP BBB . n 
B 2 100 ARG 100 100 100 ARG ARG BBB . n 
B 2 101 GLY 101 101 101 GLY GLY BBB . n 
B 2 102 GLU 102 102 102 GLU GLU BBB . n 
B 2 103 SER 103 103 103 SER SER BBB . n 
B 2 104 TYR 104 104 104 TYR TYR BBB . n 
B 2 105 TYR 105 105 105 TYR TYR BBB . n 
B 2 106 TYR 106 106 106 TYR TYR BBB . n 
B 2 107 THR 107 107 107 THR THR BBB . n 
B 2 108 ARG 108 108 108 ARG ARG BBB . n 
B 2 109 PRO 109 109 109 PRO PRO BBB . n 
B 2 110 THR 110 110 110 THR THR BBB . n 
B 2 111 GLU 111 111 111 GLU GLU BBB . n 
B 2 112 TYR 112 112 112 TYR TYR BBB . n 
B 2 113 GLU 113 113 113 GLU GLU BBB . n 
B 2 114 PHE 114 114 114 PHE PHE BBB . n 
B 2 115 TRP 115 115 115 TRP TRP BBB . n 
B 2 116 GLY 116 116 116 GLY GLY BBB . n 
B 2 117 GLN 117 117 117 GLN GLN BBB . n 
B 2 118 GLY 118 118 118 GLY GLY BBB . n 
B 2 119 THR 119 119 119 THR THR BBB . n 
B 2 120 GLN 120 120 120 GLN GLN BBB . n 
B 2 121 VAL 121 121 121 VAL VAL BBB . n 
B 2 122 THR 122 122 122 THR THR BBB . n 
B 2 123 VAL 123 123 123 VAL VAL BBB . n 
B 2 124 SER 124 124 124 SER SER BBB . n 
B 2 125 SER 125 125 125 SER SER BBB . n 
B 2 126 LYS 126 126 ?   ?   ?   BBB . n 
B 2 127 HIS 127 127 ?   ?   ?   BBB . n 
B 2 128 HIS 128 128 ?   ?   ?   BBB . n 
B 2 129 HIS 129 129 ?   ?   ?   BBB . n 
B 2 130 HIS 130 130 ?   ?   ?   BBB . n 
B 2 131 HIS 131 131 ?   ?   ?   BBB . n 
B 2 132 HIS 132 132 ?   ?   ?   BBB . n 
C 1 1   PRO 1   330 ?   ?   ?   CCC . n 
C 1 2   ASN 2   331 331 ASN ASN CCC . n 
C 1 3   ILE 3   332 332 ILE ILE CCC . n 
C 1 4   THR 4   333 333 THR THR CCC . n 
C 1 5   ASN 5   334 334 ASN ASN CCC . n 
C 1 6   LEU 6   335 335 LEU LEU CCC . n 
C 1 7   CYS 7   336 336 CYS CYS CCC . n 
C 1 8   PRO 8   337 337 PRO PRO CCC . n 
C 1 9   PHE 9   338 338 PHE PHE CCC . n 
C 1 10  GLY 10  339 339 GLY GLY CCC . n 
C 1 11  GLU 11  340 340 GLU GLU CCC . n 
C 1 12  VAL 12  341 341 VAL VAL CCC . n 
C 1 13  PHE 13  342 342 PHE PHE CCC . n 
C 1 14  ASN 14  343 343 ASN ASN CCC . n 
C 1 15  ALA 15  344 344 ALA ALA CCC . n 
C 1 16  THR 16  345 345 THR THR CCC . n 
C 1 17  ARG 17  346 346 ARG ARG CCC . n 
C 1 18  PHE 18  347 347 PHE PHE CCC . n 
C 1 19  ALA 19  348 348 ALA ALA CCC . n 
C 1 20  SER 20  349 349 SER SER CCC . n 
C 1 21  VAL 21  350 350 VAL VAL CCC . n 
C 1 22  TYR 22  351 351 TYR TYR CCC . n 
C 1 23  ALA 23  352 352 ALA ALA CCC . n 
C 1 24  TRP 24  353 353 TRP TRP CCC . n 
C 1 25  ASN 25  354 354 ASN ASN CCC . n 
C 1 26  ARG 26  355 355 ARG ARG CCC . n 
C 1 27  LYS 27  356 356 LYS LYS CCC . n 
C 1 28  ARG 28  357 357 ARG ARG CCC . n 
C 1 29  ILE 29  358 358 ILE ILE CCC . n 
C 1 30  SER 30  359 359 SER SER CCC . n 
C 1 31  ASN 31  360 360 ASN ASN CCC . n 
C 1 32  CYS 32  361 361 CYS CYS CCC . n 
C 1 33  VAL 33  362 362 VAL VAL CCC . n 
C 1 34  ALA 34  363 363 ALA ALA CCC . n 
C 1 35  ASP 35  364 364 ASP ASP CCC . n 
C 1 36  TYR 36  365 365 TYR TYR CCC . n 
C 1 37  SER 37  366 366 SER SER CCC . n 
C 1 38  VAL 38  367 367 VAL VAL CCC . n 
C 1 39  LEU 39  368 368 LEU LEU CCC . n 
C 1 40  TYR 40  369 369 TYR TYR CCC . n 
C 1 41  ASN 41  370 370 ASN ASN CCC . n 
C 1 42  SER 42  371 371 SER SER CCC . n 
C 1 43  ALA 43  372 372 ALA ALA CCC . n 
C 1 44  SER 44  373 373 SER SER CCC . n 
C 1 45  PHE 45  374 374 PHE PHE CCC . n 
C 1 46  SER 46  375 375 SER SER CCC . n 
C 1 47  THR 47  376 376 THR THR CCC . n 
C 1 48  PHE 48  377 377 PHE PHE CCC . n 
C 1 49  LYS 49  378 378 LYS LYS CCC . n 
C 1 50  CYS 50  379 379 CYS CYS CCC . n 
C 1 51  TYR 51  380 380 TYR TYR CCC . n 
C 1 52  GLY 52  381 381 GLY GLY CCC . n 
C 1 53  VAL 53  382 382 VAL VAL CCC . n 
C 1 54  SER 54  383 383 SER SER CCC . n 
C 1 55  PRO 55  384 384 PRO PRO CCC . n 
C 1 56  THR 56  385 385 THR THR CCC . n 
C 1 57  LYS 57  386 386 LYS LYS CCC . n 
C 1 58  LEU 58  387 387 LEU LEU CCC . n 
C 1 59  ASN 59  388 388 ASN ASN CCC . n 
C 1 60  ASP 60  389 389 ASP ASP CCC . n 
C 1 61  LEU 61  390 390 LEU LEU CCC . n 
C 1 62  CYS 62  391 391 CYS CYS CCC . n 
C 1 63  PHE 63  392 392 PHE PHE CCC . n 
C 1 64  THR 64  393 393 THR THR CCC . n 
C 1 65  ASN 65  394 394 ASN ASN CCC . n 
C 1 66  VAL 66  395 395 VAL VAL CCC . n 
C 1 67  TYR 67  396 396 TYR TYR CCC . n 
C 1 68  ALA 68  397 397 ALA ALA CCC . n 
C 1 69  ASP 69  398 398 ASP ASP CCC . n 
C 1 70  SER 70  399 399 SER SER CCC . n 
C 1 71  PHE 71  400 400 PHE PHE CCC . n 
C 1 72  VAL 72  401 401 VAL VAL CCC . n 
C 1 73  ILE 73  402 402 ILE ILE CCC . n 
C 1 74  ARG 74  403 403 ARG ARG CCC . n 
C 1 75  GLY 75  404 404 GLY GLY CCC . n 
C 1 76  ASP 76  405 405 ASP ASP CCC . n 
C 1 77  GLU 77  406 406 GLU GLU CCC . n 
C 1 78  VAL 78  407 407 VAL VAL CCC . n 
C 1 79  ARG 79  408 408 ARG ARG CCC . n 
C 1 80  GLN 80  409 409 GLN GLN CCC . n 
C 1 81  ILE 81  410 410 ILE ILE CCC . n 
C 1 82  ALA 82  411 411 ALA ALA CCC . n 
C 1 83  PRO 83  412 412 PRO PRO CCC . n 
C 1 84  GLY 84  413 413 GLY GLY CCC . n 
C 1 85  GLN 85  414 414 GLN GLN CCC . n 
C 1 86  THR 86  415 415 THR THR CCC . n 
C 1 87  GLY 87  416 416 GLY GLY CCC . n 
C 1 88  LYS 88  417 417 LYS LYS CCC . n 
C 1 89  ILE 89  418 418 ILE ILE CCC . n 
C 1 90  ALA 90  419 419 ALA ALA CCC . n 
C 1 91  ASP 91  420 420 ASP ASP CCC . n 
C 1 92  TYR 92  421 421 TYR TYR CCC . n 
C 1 93  ASN 93  422 422 ASN ASN CCC . n 
C 1 94  TYR 94  423 423 TYR TYR CCC . n 
C 1 95  LYS 95  424 424 LYS LYS CCC . n 
C 1 96  LEU 96  425 425 LEU LEU CCC . n 
C 1 97  PRO 97  426 426 PRO PRO CCC . n 
C 1 98  ASP 98  427 427 ASP ASP CCC . n 
C 1 99  ASP 99  428 428 ASP ASP CCC . n 
C 1 100 PHE 100 429 429 PHE PHE CCC . n 
C 1 101 THR 101 430 430 THR THR CCC . n 
C 1 102 GLY 102 431 431 GLY GLY CCC . n 
C 1 103 CYS 103 432 432 CYS CYS CCC . n 
C 1 104 VAL 104 433 433 VAL VAL CCC . n 
C 1 105 ILE 105 434 434 ILE ILE CCC . n 
C 1 106 ALA 106 435 435 ALA ALA CCC . n 
C 1 107 TRP 107 436 436 TRP TRP CCC . n 
C 1 108 ASN 108 437 437 ASN ASN CCC . n 
C 1 109 SER 109 438 438 SER SER CCC . n 
C 1 110 ASN 110 439 439 ASN ASN CCC . n 
C 1 111 ASN 111 440 440 ASN ASN CCC . n 
C 1 112 LEU 112 441 441 LEU LEU CCC . n 
C 1 113 ASP 113 442 442 ASP ASP CCC . n 
C 1 114 SER 114 443 443 SER SER CCC . n 
C 1 115 LYS 115 444 444 LYS LYS CCC . n 
C 1 116 VAL 116 445 445 VAL VAL CCC . n 
C 1 117 GLY 117 446 446 GLY GLY CCC . n 
C 1 118 GLY 118 447 447 GLY GLY CCC . n 
C 1 119 ASN 119 448 448 ASN ASN CCC . n 
C 1 120 TYR 120 449 449 TYR TYR CCC . n 
C 1 121 ASN 121 450 450 ASN ASN CCC . n 
C 1 122 TYR 122 451 451 TYR TYR CCC . n 
C 1 123 LEU 123 452 452 LEU LEU CCC . n 
C 1 124 TYR 124 453 453 TYR TYR CCC . n 
C 1 125 ARG 125 454 454 ARG ARG CCC . n 
C 1 126 LEU 126 455 455 LEU LEU CCC . n 
C 1 127 PHE 127 456 456 PHE PHE CCC . n 
C 1 128 ARG 128 457 457 ARG ARG CCC . n 
C 1 129 LYS 129 458 458 LYS LYS CCC . n 
C 1 130 SER 130 459 459 SER SER CCC . n 
C 1 131 ASN 131 460 460 ASN ASN CCC . n 
C 1 132 LEU 132 461 461 LEU LEU CCC . n 
C 1 133 LYS 133 462 462 LYS LYS CCC . n 
C 1 134 PRO 134 463 463 PRO PRO CCC . n 
C 1 135 PHE 135 464 464 PHE PHE CCC . n 
C 1 136 GLU 136 465 465 GLU GLU CCC . n 
C 1 137 ARG 137 466 466 ARG ARG CCC . n 
C 1 138 ASP 138 467 467 ASP ASP CCC . n 
C 1 139 ILE 139 468 468 ILE ILE CCC . n 
C 1 140 SER 140 469 469 SER SER CCC . n 
C 1 141 THR 141 470 470 THR THR CCC . n 
C 1 142 GLU 142 471 471 GLU GLU CCC . n 
C 1 143 ILE 143 472 472 ILE ILE CCC . n 
C 1 144 TYR 144 473 473 TYR TYR CCC . n 
C 1 145 GLN 145 474 474 GLN GLN CCC . n 
C 1 146 ALA 146 475 475 ALA ALA CCC . n 
C 1 147 GLY 147 476 476 GLY GLY CCC . n 
C 1 148 SER 148 477 477 SER SER CCC . n 
C 1 149 THR 149 478 478 THR THR CCC . n 
C 1 150 PRO 150 479 479 PRO PRO CCC . n 
C 1 151 CYS 151 480 480 CYS CYS CCC . n 
C 1 152 ASN 152 481 481 ASN ASN CCC . n 
C 1 153 GLY 153 482 482 GLY GLY CCC . n 
C 1 154 VAL 154 483 483 VAL VAL CCC . n 
C 1 155 GLU 155 484 484 GLU GLU CCC . n 
C 1 156 GLY 156 485 485 GLY GLY CCC . n 
C 1 157 PHE 157 486 486 PHE PHE CCC . n 
C 1 158 ASN 158 487 487 ASN ASN CCC . n 
C 1 159 CYS 159 488 488 CYS CYS CCC . n 
C 1 160 TYR 160 489 489 TYR TYR CCC . n 
C 1 161 PHE 161 490 490 PHE PHE CCC . n 
C 1 162 PRO 162 491 491 PRO PRO CCC . n 
C 1 163 LEU 163 492 492 LEU LEU CCC . n 
C 1 164 GLN 164 493 493 GLN GLN CCC . n 
C 1 165 SER 165 494 494 SER SER CCC . n 
C 1 166 TYR 166 495 495 TYR TYR CCC . n 
C 1 167 GLY 167 496 496 GLY GLY CCC . n 
C 1 168 PHE 168 497 497 PHE PHE CCC . n 
C 1 169 GLN 169 498 498 GLN GLN CCC . n 
C 1 170 PRO 170 499 499 PRO PRO CCC . n 
C 1 171 THR 171 500 500 THR THR CCC . n 
C 1 172 ASN 172 501 501 ASN ASN CCC . n 
C 1 173 GLY 173 502 502 GLY GLY CCC . n 
C 1 174 VAL 174 503 503 VAL VAL CCC . n 
C 1 175 GLY 175 504 504 GLY GLY CCC . n 
C 1 176 TYR 176 505 505 TYR TYR CCC . n 
C 1 177 GLN 177 506 506 GLN GLN CCC . n 
C 1 178 PRO 178 507 507 PRO PRO CCC . n 
C 1 179 TYR 179 508 508 TYR TYR CCC . n 
C 1 180 ARG 180 509 509 ARG ARG CCC . n 
C 1 181 VAL 181 510 510 VAL VAL CCC . n 
C 1 182 VAL 182 511 511 VAL VAL CCC . n 
C 1 183 VAL 183 512 512 VAL VAL CCC . n 
C 1 184 LEU 184 513 513 LEU LEU CCC . n 
C 1 185 SER 185 514 514 SER SER CCC . n 
C 1 186 PHE 186 515 515 PHE PHE CCC . n 
C 1 187 GLU 187 516 516 GLU GLU CCC . n 
C 1 188 LEU 188 517 517 LEU LEU CCC . n 
C 1 189 LEU 189 518 518 LEU LEU CCC . n 
C 1 190 HIS 190 519 519 HIS HIS CCC . n 
C 1 191 ALA 191 520 520 ALA ALA CCC . n 
C 1 192 PRO 192 521 521 PRO PRO CCC . n 
C 1 193 ALA 193 522 522 ALA ALA CCC . n 
C 1 194 THR 194 523 523 THR THR CCC . n 
C 1 195 VAL 195 524 524 VAL VAL CCC . n 
C 1 196 CYS 196 525 525 CYS CYS CCC . n 
C 1 197 GLY 197 526 526 GLY GLY CCC . n 
C 1 198 PRO 198 527 527 PRO PRO CCC . n 
C 1 199 LYS 199 528 528 LYS LYS CCC . n 
C 1 200 LYS 200 529 ?   ?   ?   CCC . n 
C 1 201 SER 201 530 ?   ?   ?   CCC . n 
C 1 202 THR 202 531 ?   ?   ?   CCC . n 
C 1 203 ASN 203 532 ?   ?   ?   CCC . n 
C 1 204 LYS 204 533 ?   ?   ?   CCC . n 
C 1 205 HIS 205 534 ?   ?   ?   CCC . n 
C 1 206 HIS 206 535 ?   ?   ?   CCC . n 
C 1 207 HIS 207 536 ?   ?   ?   CCC . n 
C 1 208 HIS 208 537 ?   ?   ?   CCC . n 
C 1 209 HIS 209 538 ?   ?   ?   CCC . n 
C 1 210 HIS 210 539 ?   ?   ?   CCC . n 
D 2 1   GLN 1   1   1   GLN GLN DDD . n 
D 2 2   VAL 2   2   2   VAL VAL DDD . n 
D 2 3   GLN 3   3   3   GLN GLN DDD . n 
D 2 4   LEU 4   4   4   LEU LEU DDD . n 
D 2 5   VAL 5   5   5   VAL VAL DDD . n 
D 2 6   GLU 6   6   6   GLU GLU DDD . n 
D 2 7   SER 7   7   7   SER SER DDD . n 
D 2 8   GLY 8   8   8   GLY GLY DDD . n 
D 2 9   GLY 9   9   9   GLY GLY DDD . n 
D 2 10  GLY 10  10  10  GLY GLY DDD . n 
D 2 11  LEU 11  11  11  LEU LEU DDD . n 
D 2 12  VAL 12  12  12  VAL VAL DDD . n 
D 2 13  GLN 13  13  13  GLN GLN DDD . n 
D 2 14  ALA 14  14  14  ALA ALA DDD . n 
D 2 15  GLY 15  15  15  GLY GLY DDD . n 
D 2 16  GLY 16  16  16  GLY GLY DDD . n 
D 2 17  SER 17  17  17  SER SER DDD . n 
D 2 18  LEU 18  18  18  LEU LEU DDD . n 
D 2 19  ARG 19  19  19  ARG ARG DDD . n 
D 2 20  LEU 20  20  20  LEU LEU DDD . n 
D 2 21  ALA 21  21  21  ALA ALA DDD . n 
D 2 22  CYS 22  22  22  CYS CYS DDD . n 
D 2 23  ILE 23  23  23  ILE ILE DDD . n 
D 2 24  ALA 24  24  24  ALA ALA DDD . n 
D 2 25  SER 25  25  25  SER SER DDD . n 
D 2 26  GLY 26  26  26  GLY GLY DDD . n 
D 2 27  ARG 27  27  27  ARG ARG DDD . n 
D 2 28  THR 28  28  28  THR THR DDD . n 
D 2 29  PHE 29  29  29  PHE PHE DDD . n 
D 2 30  HIS 30  30  30  HIS HIS DDD . n 
D 2 31  SER 31  31  31  SER SER DDD . n 
D 2 32  TYR 32  32  32  TYR TYR DDD . n 
D 2 33  VAL 33  33  33  VAL VAL DDD . n 
D 2 34  MET 34  34  34  MET MET DDD . n 
D 2 35  ALA 35  35  35  ALA ALA DDD . n 
D 2 36  TRP 36  36  36  TRP TRP DDD . n 
D 2 37  PHE 37  37  37  PHE PHE DDD . n 
D 2 38  ARG 38  38  38  ARG ARG DDD . n 
D 2 39  GLN 39  39  39  GLN GLN DDD . n 
D 2 40  ALA 40  40  40  ALA ALA DDD . n 
D 2 41  PRO 41  41  41  PRO PRO DDD . n 
D 2 42  GLY 42  42  42  GLY GLY DDD . n 
D 2 43  LYS 43  43  43  LYS LYS DDD . n 
D 2 44  GLU 44  44  44  GLU GLU DDD . n 
D 2 45  ARG 45  45  45  ARG ARG DDD . n 
D 2 46  GLU 46  46  46  GLU GLU DDD . n 
D 2 47  PHE 47  47  47  PHE PHE DDD . n 
D 2 48  VAL 48  48  48  VAL VAL DDD . n 
D 2 49  ALA 49  49  49  ALA ALA DDD . n 
D 2 50  ALA 50  50  50  ALA ALA DDD . n 
D 2 51  ILE 51  51  51  ILE ILE DDD . n 
D 2 52  SER 52  52  52  SER SER DDD . n 
D 2 53  TRP 53  53  53  TRP TRP DDD . n 
D 2 54  SER 54  54  54  SER SER DDD . n 
D 2 55  SER 55  55  55  SER SER DDD . n 
D 2 56  THR 56  56  56  THR THR DDD . n 
D 2 57  PRO 57  57  57  PRO PRO DDD . n 
D 2 58  THR 58  58  58  THR THR DDD . n 
D 2 59  TYR 59  59  59  TYR TYR DDD . n 
D 2 60  TYR 60  60  60  TYR TYR DDD . n 
D 2 61  GLY 61  61  61  GLY GLY DDD . n 
D 2 62  GLU 62  62  62  GLU GLU DDD . n 
D 2 63  SER 63  63  63  SER SER DDD . n 
D 2 64  VAL 64  64  64  VAL VAL DDD . n 
D 2 65  LYS 65  65  65  LYS LYS DDD . n 
D 2 66  GLY 66  66  66  GLY GLY DDD . n 
D 2 67  ARG 67  67  67  ARG ARG DDD . n 
D 2 68  PHE 68  68  68  PHE PHE DDD . n 
D 2 69  THR 69  69  69  THR THR DDD . n 
D 2 70  ILE 70  70  70  ILE ILE DDD . n 
D 2 71  SER 71  71  71  SER SER DDD . n 
D 2 72  ARG 72  72  72  ARG ARG DDD . n 
D 2 73  ASP 73  73  73  ASP ASP DDD . n 
D 2 74  ASN 74  74  74  ASN ASN DDD . n 
D 2 75  ALA 75  75  75  ALA ALA DDD . n 
D 2 76  LYS 76  76  76  LYS LYS DDD . n 
D 2 77  ASN 77  77  77  ASN ASN DDD . n 
D 2 78  THR 78  78  78  THR THR DDD . n 
D 2 79  VAL 79  79  79  VAL VAL DDD . n 
D 2 80  TYR 80  80  80  TYR TYR DDD . n 
D 2 81  LEU 81  81  81  LEU LEU DDD . n 
D 2 82  GLN 82  82  82  GLN GLN DDD . n 
D 2 83  MET 83  83  83  MET MET DDD . n 
D 2 84  ASN 84  84  84  ASN ASN DDD . n 
D 2 85  ARG 85  85  85  ARG ARG DDD . n 
D 2 86  LEU 86  86  86  LEU LEU DDD . n 
D 2 87  LYS 87  87  87  LYS LYS DDD . n 
D 2 88  PRO 88  88  88  PRO PRO DDD . n 
D 2 89  GLU 89  89  89  GLU GLU DDD . n 
D 2 90  ASP 90  90  90  ASP ASP DDD . n 
D 2 91  THR 91  91  91  THR THR DDD . n 
D 2 92  ALA 92  92  92  ALA ALA DDD . n 
D 2 93  VAL 93  93  93  VAL VAL DDD . n 
D 2 94  TYR 94  94  94  TYR TYR DDD . n 
D 2 95  PHE 95  95  95  PHE PHE DDD . n 
D 2 96  CYS 96  96  96  CYS CYS DDD . n 
D 2 97  ALA 97  97  97  ALA ALA DDD . n 
D 2 98  ALA 98  98  98  ALA ALA DDD . n 
D 2 99  ASP 99  99  99  ASP ASP DDD . n 
D 2 100 ARG 100 100 100 ARG ARG DDD . n 
D 2 101 GLY 101 101 101 GLY GLY DDD . n 
D 2 102 GLU 102 102 102 GLU GLU DDD . n 
D 2 103 SER 103 103 103 SER SER DDD . n 
D 2 104 TYR 104 104 104 TYR TYR DDD . n 
D 2 105 TYR 105 105 105 TYR TYR DDD . n 
D 2 106 TYR 106 106 106 TYR TYR DDD . n 
D 2 107 THR 107 107 107 THR THR DDD . n 
D 2 108 ARG 108 108 108 ARG ARG DDD . n 
D 2 109 PRO 109 109 109 PRO PRO DDD . n 
D 2 110 THR 110 110 110 THR THR DDD . n 
D 2 111 GLU 111 111 111 GLU GLU DDD . n 
D 2 112 TYR 112 112 112 TYR TYR DDD . n 
D 2 113 GLU 113 113 113 GLU GLU DDD . n 
D 2 114 PHE 114 114 114 PHE PHE DDD . n 
D 2 115 TRP 115 115 115 TRP TRP DDD . n 
D 2 116 GLY 116 116 116 GLY GLY DDD . n 
D 2 117 GLN 117 117 117 GLN GLN DDD . n 
D 2 118 GLY 118 118 118 GLY GLY DDD . n 
D 2 119 THR 119 119 119 THR THR DDD . n 
D 2 120 GLN 120 120 120 GLN GLN DDD . n 
D 2 121 VAL 121 121 121 VAL VAL DDD . n 
D 2 122 THR 122 122 122 THR THR DDD . n 
D 2 123 VAL 123 123 123 VAL VAL DDD . n 
D 2 124 SER 124 124 124 SER SER DDD . n 
D 2 125 SER 125 125 125 SER SER DDD . n 
D 2 126 LYS 126 126 ?   ?   ?   DDD . n 
D 2 127 HIS 127 127 ?   ?   ?   DDD . n 
D 2 128 HIS 128 128 ?   ?   ?   DDD . n 
D 2 129 HIS 129 129 ?   ?   ?   DDD . n 
D 2 130 HIS 130 130 ?   ?   ?   DDD . n 
D 2 131 HIS 131 131 ?   ?   ?   DDD . n 
D 2 132 HIS 132 132 ?   ?   ?   DDD . n 
E 1 1   PRO 1   330 ?   ?   ?   EEE . n 
E 1 2   ASN 2   331 ?   ?   ?   EEE . n 
E 1 3   ILE 3   332 332 ILE ILE EEE . n 
E 1 4   THR 4   333 333 THR THR EEE . n 
E 1 5   ASN 5   334 334 ASN ASN EEE . n 
E 1 6   LEU 6   335 335 LEU LEU EEE . n 
E 1 7   CYS 7   336 336 CYS CYS EEE . n 
E 1 8   PRO 8   337 337 PRO PRO EEE . n 
E 1 9   PHE 9   338 338 PHE PHE EEE . n 
E 1 10  GLY 10  339 339 GLY GLY EEE . n 
E 1 11  GLU 11  340 340 GLU GLU EEE . n 
E 1 12  VAL 12  341 341 VAL VAL EEE . n 
E 1 13  PHE 13  342 342 PHE PHE EEE . n 
E 1 14  ASN 14  343 343 ASN ASN EEE . n 
E 1 15  ALA 15  344 344 ALA ALA EEE . n 
E 1 16  THR 16  345 345 THR THR EEE . n 
E 1 17  ARG 17  346 346 ARG ARG EEE . n 
E 1 18  PHE 18  347 347 PHE PHE EEE . n 
E 1 19  ALA 19  348 348 ALA ALA EEE . n 
E 1 20  SER 20  349 349 SER SER EEE . n 
E 1 21  VAL 21  350 350 VAL VAL EEE . n 
E 1 22  TYR 22  351 351 TYR TYR EEE . n 
E 1 23  ALA 23  352 352 ALA ALA EEE . n 
E 1 24  TRP 24  353 353 TRP TRP EEE . n 
E 1 25  ASN 25  354 354 ASN ASN EEE . n 
E 1 26  ARG 26  355 355 ARG ARG EEE . n 
E 1 27  LYS 27  356 356 LYS LYS EEE . n 
E 1 28  ARG 28  357 357 ARG ARG EEE . n 
E 1 29  ILE 29  358 358 ILE ILE EEE . n 
E 1 30  SER 30  359 359 SER SER EEE . n 
E 1 31  ASN 31  360 360 ASN ASN EEE . n 
E 1 32  CYS 32  361 361 CYS CYS EEE . n 
E 1 33  VAL 33  362 362 VAL VAL EEE . n 
E 1 34  ALA 34  363 363 ALA ALA EEE . n 
E 1 35  ASP 35  364 364 ASP ASP EEE . n 
E 1 36  TYR 36  365 365 TYR TYR EEE . n 
E 1 37  SER 37  366 366 SER SER EEE . n 
E 1 38  VAL 38  367 367 VAL VAL EEE . n 
E 1 39  LEU 39  368 368 LEU LEU EEE . n 
E 1 40  TYR 40  369 369 TYR TYR EEE . n 
E 1 41  ASN 41  370 370 ASN ASN EEE . n 
E 1 42  SER 42  371 371 SER SER EEE . n 
E 1 43  ALA 43  372 372 ALA ALA EEE . n 
E 1 44  SER 44  373 373 SER SER EEE . n 
E 1 45  PHE 45  374 374 PHE PHE EEE . n 
E 1 46  SER 46  375 375 SER SER EEE . n 
E 1 47  THR 47  376 376 THR THR EEE . n 
E 1 48  PHE 48  377 377 PHE PHE EEE . n 
E 1 49  LYS 49  378 378 LYS LYS EEE . n 
E 1 50  CYS 50  379 379 CYS CYS EEE . n 
E 1 51  TYR 51  380 380 TYR TYR EEE . n 
E 1 52  GLY 52  381 381 GLY GLY EEE . n 
E 1 53  VAL 53  382 382 VAL VAL EEE . n 
E 1 54  SER 54  383 383 SER SER EEE . n 
E 1 55  PRO 55  384 384 PRO PRO EEE . n 
E 1 56  THR 56  385 385 THR THR EEE . n 
E 1 57  LYS 57  386 386 LYS LYS EEE . n 
E 1 58  LEU 58  387 387 LEU LEU EEE . n 
E 1 59  ASN 59  388 388 ASN ASN EEE . n 
E 1 60  ASP 60  389 389 ASP ASP EEE . n 
E 1 61  LEU 61  390 390 LEU LEU EEE . n 
E 1 62  CYS 62  391 391 CYS CYS EEE . n 
E 1 63  PHE 63  392 392 PHE PHE EEE . n 
E 1 64  THR 64  393 393 THR THR EEE . n 
E 1 65  ASN 65  394 394 ASN ASN EEE . n 
E 1 66  VAL 66  395 395 VAL VAL EEE . n 
E 1 67  TYR 67  396 396 TYR TYR EEE . n 
E 1 68  ALA 68  397 397 ALA ALA EEE . n 
E 1 69  ASP 69  398 398 ASP ASP EEE . n 
E 1 70  SER 70  399 399 SER SER EEE . n 
E 1 71  PHE 71  400 400 PHE PHE EEE . n 
E 1 72  VAL 72  401 401 VAL VAL EEE . n 
E 1 73  ILE 73  402 402 ILE ILE EEE . n 
E 1 74  ARG 74  403 403 ARG ARG EEE . n 
E 1 75  GLY 75  404 404 GLY GLY EEE . n 
E 1 76  ASP 76  405 405 ASP ASP EEE . n 
E 1 77  GLU 77  406 406 GLU GLU EEE . n 
E 1 78  VAL 78  407 407 VAL VAL EEE . n 
E 1 79  ARG 79  408 408 ARG ARG EEE . n 
E 1 80  GLN 80  409 409 GLN GLN EEE . n 
E 1 81  ILE 81  410 410 ILE ILE EEE . n 
E 1 82  ALA 82  411 411 ALA ALA EEE . n 
E 1 83  PRO 83  412 412 PRO PRO EEE . n 
E 1 84  GLY 84  413 413 GLY GLY EEE . n 
E 1 85  GLN 85  414 414 GLN GLN EEE . n 
E 1 86  THR 86  415 415 THR THR EEE . n 
E 1 87  GLY 87  416 416 GLY GLY EEE . n 
E 1 88  LYS 88  417 417 LYS LYS EEE . n 
E 1 89  ILE 89  418 418 ILE ILE EEE . n 
E 1 90  ALA 90  419 419 ALA ALA EEE . n 
E 1 91  ASP 91  420 420 ASP ASP EEE . n 
E 1 92  TYR 92  421 421 TYR TYR EEE . n 
E 1 93  ASN 93  422 422 ASN ASN EEE . n 
E 1 94  TYR 94  423 423 TYR TYR EEE . n 
E 1 95  LYS 95  424 424 LYS LYS EEE . n 
E 1 96  LEU 96  425 425 LEU LEU EEE . n 
E 1 97  PRO 97  426 426 PRO PRO EEE . n 
E 1 98  ASP 98  427 427 ASP ASP EEE . n 
E 1 99  ASP 99  428 428 ASP ASP EEE . n 
E 1 100 PHE 100 429 429 PHE PHE EEE . n 
E 1 101 THR 101 430 430 THR THR EEE . n 
E 1 102 GLY 102 431 431 GLY GLY EEE . n 
E 1 103 CYS 103 432 432 CYS CYS EEE . n 
E 1 104 VAL 104 433 433 VAL VAL EEE . n 
E 1 105 ILE 105 434 434 ILE ILE EEE . n 
E 1 106 ALA 106 435 435 ALA ALA EEE . n 
E 1 107 TRP 107 436 436 TRP TRP EEE . n 
E 1 108 ASN 108 437 437 ASN ASN EEE . n 
E 1 109 SER 109 438 438 SER SER EEE . n 
E 1 110 ASN 110 439 439 ASN ASN EEE . n 
E 1 111 ASN 111 440 440 ASN ASN EEE . n 
E 1 112 LEU 112 441 441 LEU LEU EEE . n 
E 1 113 ASP 113 442 442 ASP ASP EEE . n 
E 1 114 SER 114 443 443 SER SER EEE . n 
E 1 115 LYS 115 444 444 LYS LYS EEE . n 
E 1 116 VAL 116 445 445 VAL VAL EEE . n 
E 1 117 GLY 117 446 446 GLY GLY EEE . n 
E 1 118 GLY 118 447 447 GLY GLY EEE . n 
E 1 119 ASN 119 448 448 ASN ASN EEE . n 
E 1 120 TYR 120 449 449 TYR TYR EEE . n 
E 1 121 ASN 121 450 450 ASN ASN EEE . n 
E 1 122 TYR 122 451 451 TYR TYR EEE . n 
E 1 123 LEU 123 452 452 LEU LEU EEE . n 
E 1 124 TYR 124 453 453 TYR TYR EEE . n 
E 1 125 ARG 125 454 454 ARG ARG EEE . n 
E 1 126 LEU 126 455 455 LEU LEU EEE . n 
E 1 127 PHE 127 456 456 PHE PHE EEE . n 
E 1 128 ARG 128 457 457 ARG ARG EEE . n 
E 1 129 LYS 129 458 458 LYS LYS EEE . n 
E 1 130 SER 130 459 459 SER SER EEE . n 
E 1 131 ASN 131 460 460 ASN ASN EEE . n 
E 1 132 LEU 132 461 461 LEU LEU EEE . n 
E 1 133 LYS 133 462 462 LYS LYS EEE . n 
E 1 134 PRO 134 463 463 PRO PRO EEE . n 
E 1 135 PHE 135 464 464 PHE PHE EEE . n 
E 1 136 GLU 136 465 465 GLU GLU EEE . n 
E 1 137 ARG 137 466 466 ARG ARG EEE . n 
E 1 138 ASP 138 467 467 ASP ASP EEE . n 
E 1 139 ILE 139 468 468 ILE ILE EEE . n 
E 1 140 SER 140 469 469 SER SER EEE . n 
E 1 141 THR 141 470 470 THR THR EEE . n 
E 1 142 GLU 142 471 471 GLU GLU EEE . n 
E 1 143 ILE 143 472 472 ILE ILE EEE . n 
E 1 144 TYR 144 473 473 TYR TYR EEE . n 
E 1 145 GLN 145 474 474 GLN GLN EEE . n 
E 1 146 ALA 146 475 475 ALA ALA EEE . n 
E 1 147 GLY 147 476 476 GLY GLY EEE . n 
E 1 148 SER 148 477 477 SER SER EEE . n 
E 1 149 THR 149 478 478 THR THR EEE . n 
E 1 150 PRO 150 479 479 PRO PRO EEE . n 
E 1 151 CYS 151 480 480 CYS CYS EEE . n 
E 1 152 ASN 152 481 481 ASN ASN EEE . n 
E 1 153 GLY 153 482 482 GLY GLY EEE . n 
E 1 154 VAL 154 483 483 VAL VAL EEE . n 
E 1 155 GLU 155 484 484 GLU GLU EEE . n 
E 1 156 GLY 156 485 485 GLY GLY EEE . n 
E 1 157 PHE 157 486 486 PHE PHE EEE . n 
E 1 158 ASN 158 487 487 ASN ASN EEE . n 
E 1 159 CYS 159 488 488 CYS CYS EEE . n 
E 1 160 TYR 160 489 489 TYR TYR EEE . n 
E 1 161 PHE 161 490 490 PHE PHE EEE . n 
E 1 162 PRO 162 491 491 PRO PRO EEE . n 
E 1 163 LEU 163 492 492 LEU LEU EEE . n 
E 1 164 GLN 164 493 493 GLN GLN EEE . n 
E 1 165 SER 165 494 494 SER SER EEE . n 
E 1 166 TYR 166 495 495 TYR TYR EEE . n 
E 1 167 GLY 167 496 496 GLY GLY EEE . n 
E 1 168 PHE 168 497 497 PHE PHE EEE . n 
E 1 169 GLN 169 498 498 GLN GLN EEE . n 
E 1 170 PRO 170 499 499 PRO PRO EEE . n 
E 1 171 THR 171 500 500 THR THR EEE . n 
E 1 172 ASN 172 501 501 ASN ASN EEE . n 
E 1 173 GLY 173 502 502 GLY GLY EEE . n 
E 1 174 VAL 174 503 503 VAL VAL EEE . n 
E 1 175 GLY 175 504 504 GLY GLY EEE . n 
E 1 176 TYR 176 505 505 TYR TYR EEE . n 
E 1 177 GLN 177 506 506 GLN GLN EEE . n 
E 1 178 PRO 178 507 507 PRO PRO EEE . n 
E 1 179 TYR 179 508 508 TYR TYR EEE . n 
E 1 180 ARG 180 509 509 ARG ARG EEE . n 
E 1 181 VAL 181 510 510 VAL VAL EEE . n 
E 1 182 VAL 182 511 511 VAL VAL EEE . n 
E 1 183 VAL 183 512 512 VAL VAL EEE . n 
E 1 184 LEU 184 513 513 LEU LEU EEE . n 
E 1 185 SER 185 514 514 SER SER EEE . n 
E 1 186 PHE 186 515 515 PHE PHE EEE . n 
E 1 187 GLU 187 516 516 GLU GLU EEE . n 
E 1 188 LEU 188 517 517 LEU LEU EEE . n 
E 1 189 LEU 189 518 518 LEU LEU EEE . n 
E 1 190 HIS 190 519 519 HIS HIS EEE . n 
E 1 191 ALA 191 520 520 ALA ALA EEE . n 
E 1 192 PRO 192 521 521 PRO PRO EEE . n 
E 1 193 ALA 193 522 522 ALA ALA EEE . n 
E 1 194 THR 194 523 523 THR THR EEE . n 
E 1 195 VAL 195 524 524 VAL VAL EEE . n 
E 1 196 CYS 196 525 525 CYS CYS EEE . n 
E 1 197 GLY 197 526 526 GLY GLY EEE . n 
E 1 198 PRO 198 527 527 PRO PRO EEE . n 
E 1 199 LYS 199 528 528 LYS LYS EEE . n 
E 1 200 LYS 200 529 ?   ?   ?   EEE . n 
E 1 201 SER 201 530 ?   ?   ?   EEE . n 
E 1 202 THR 202 531 ?   ?   ?   EEE . n 
E 1 203 ASN 203 532 ?   ?   ?   EEE . n 
E 1 204 LYS 204 533 ?   ?   ?   EEE . n 
E 1 205 HIS 205 534 ?   ?   ?   EEE . n 
E 1 206 HIS 206 535 ?   ?   ?   EEE . n 
E 1 207 HIS 207 536 ?   ?   ?   EEE . n 
E 1 208 HIS 208 537 ?   ?   ?   EEE . n 
E 1 209 HIS 209 538 ?   ?   ?   EEE . n 
E 1 210 HIS 210 539 ?   ?   ?   EEE . n 
F 2 1   GLN 1   1   1   GLN GLN FFF . n 
F 2 2   VAL 2   2   2   VAL VAL FFF . n 
F 2 3   GLN 3   3   3   GLN GLN FFF . n 
F 2 4   LEU 4   4   4   LEU LEU FFF . n 
F 2 5   VAL 5   5   5   VAL VAL FFF . n 
F 2 6   GLU 6   6   6   GLU GLU FFF . n 
F 2 7   SER 7   7   7   SER SER FFF . n 
F 2 8   GLY 8   8   8   GLY GLY FFF . n 
F 2 9   GLY 9   9   9   GLY GLY FFF . n 
F 2 10  GLY 10  10  10  GLY GLY FFF . n 
F 2 11  LEU 11  11  11  LEU LEU FFF . n 
F 2 12  VAL 12  12  12  VAL VAL FFF . n 
F 2 13  GLN 13  13  13  GLN GLN FFF . n 
F 2 14  ALA 14  14  14  ALA ALA FFF . n 
F 2 15  GLY 15  15  15  GLY GLY FFF . n 
F 2 16  GLY 16  16  16  GLY GLY FFF . n 
F 2 17  SER 17  17  17  SER SER FFF . n 
F 2 18  LEU 18  18  18  LEU LEU FFF . n 
F 2 19  ARG 19  19  19  ARG ARG FFF . n 
F 2 20  LEU 20  20  20  LEU LEU FFF . n 
F 2 21  ALA 21  21  21  ALA ALA FFF . n 
F 2 22  CYS 22  22  22  CYS CYS FFF . n 
F 2 23  ILE 23  23  23  ILE ILE FFF . n 
F 2 24  ALA 24  24  24  ALA ALA FFF . n 
F 2 25  SER 25  25  25  SER SER FFF . n 
F 2 26  GLY 26  26  26  GLY GLY FFF . n 
F 2 27  ARG 27  27  27  ARG ARG FFF . n 
F 2 28  THR 28  28  28  THR THR FFF . n 
F 2 29  PHE 29  29  29  PHE PHE FFF . n 
F 2 30  HIS 30  30  30  HIS HIS FFF . n 
F 2 31  SER 31  31  31  SER SER FFF . n 
F 2 32  TYR 32  32  32  TYR TYR FFF . n 
F 2 33  VAL 33  33  33  VAL VAL FFF . n 
F 2 34  MET 34  34  34  MET MET FFF . n 
F 2 35  ALA 35  35  35  ALA ALA FFF . n 
F 2 36  TRP 36  36  36  TRP TRP FFF . n 
F 2 37  PHE 37  37  37  PHE PHE FFF . n 
F 2 38  ARG 38  38  38  ARG ARG FFF . n 
F 2 39  GLN 39  39  39  GLN GLN FFF . n 
F 2 40  ALA 40  40  40  ALA ALA FFF . n 
F 2 41  PRO 41  41  41  PRO PRO FFF . n 
F 2 42  GLY 42  42  42  GLY GLY FFF . n 
F 2 43  LYS 43  43  43  LYS LYS FFF . n 
F 2 44  GLU 44  44  44  GLU GLU FFF . n 
F 2 45  ARG 45  45  45  ARG ARG FFF . n 
F 2 46  GLU 46  46  46  GLU GLU FFF . n 
F 2 47  PHE 47  47  47  PHE PHE FFF . n 
F 2 48  VAL 48  48  48  VAL VAL FFF . n 
F 2 49  ALA 49  49  49  ALA ALA FFF . n 
F 2 50  ALA 50  50  50  ALA ALA FFF . n 
F 2 51  ILE 51  51  51  ILE ILE FFF . n 
F 2 52  SER 52  52  52  SER SER FFF . n 
F 2 53  TRP 53  53  53  TRP TRP FFF . n 
F 2 54  SER 54  54  54  SER SER FFF . n 
F 2 55  SER 55  55  55  SER SER FFF . n 
F 2 56  THR 56  56  56  THR THR FFF . n 
F 2 57  PRO 57  57  57  PRO PRO FFF . n 
F 2 58  THR 58  58  58  THR THR FFF . n 
F 2 59  TYR 59  59  59  TYR TYR FFF . n 
F 2 60  TYR 60  60  60  TYR TYR FFF . n 
F 2 61  GLY 61  61  61  GLY GLY FFF . n 
F 2 62  GLU 62  62  62  GLU GLU FFF . n 
F 2 63  SER 63  63  63  SER SER FFF . n 
F 2 64  VAL 64  64  64  VAL VAL FFF . n 
F 2 65  LYS 65  65  65  LYS LYS FFF . n 
F 2 66  GLY 66  66  66  GLY GLY FFF . n 
F 2 67  ARG 67  67  67  ARG ARG FFF . n 
F 2 68  PHE 68  68  68  PHE PHE FFF . n 
F 2 69  THR 69  69  69  THR THR FFF . n 
F 2 70  ILE 70  70  70  ILE ILE FFF . n 
F 2 71  SER 71  71  71  SER SER FFF . n 
F 2 72  ARG 72  72  72  ARG ARG FFF . n 
F 2 73  ASP 73  73  73  ASP ASP FFF . n 
F 2 74  ASN 74  74  74  ASN ASN FFF . n 
F 2 75  ALA 75  75  75  ALA ALA FFF . n 
F 2 76  LYS 76  76  76  LYS LYS FFF . n 
F 2 77  ASN 77  77  77  ASN ASN FFF . n 
F 2 78  THR 78  78  78  THR THR FFF . n 
F 2 79  VAL 79  79  79  VAL VAL FFF . n 
F 2 80  TYR 80  80  80  TYR TYR FFF . n 
F 2 81  LEU 81  81  81  LEU LEU FFF . n 
F 2 82  GLN 82  82  82  GLN GLN FFF . n 
F 2 83  MET 83  83  83  MET MET FFF . n 
F 2 84  ASN 84  84  84  ASN ASN FFF . n 
F 2 85  ARG 85  85  85  ARG ARG FFF . n 
F 2 86  LEU 86  86  86  LEU LEU FFF . n 
F 2 87  LYS 87  87  87  LYS LYS FFF . n 
F 2 88  PRO 88  88  88  PRO PRO FFF . n 
F 2 89  GLU 89  89  89  GLU GLU FFF . n 
F 2 90  ASP 90  90  90  ASP ASP FFF . n 
F 2 91  THR 91  91  91  THR THR FFF . n 
F 2 92  ALA 92  92  92  ALA ALA FFF . n 
F 2 93  VAL 93  93  93  VAL VAL FFF . n 
F 2 94  TYR 94  94  94  TYR TYR FFF . n 
F 2 95  PHE 95  95  95  PHE PHE FFF . n 
F 2 96  CYS 96  96  96  CYS CYS FFF . n 
F 2 97  ALA 97  97  97  ALA ALA FFF . n 
F 2 98  ALA 98  98  98  ALA ALA FFF . n 
F 2 99  ASP 99  99  99  ASP ASP FFF . n 
F 2 100 ARG 100 100 100 ARG ARG FFF . n 
F 2 101 GLY 101 101 101 GLY GLY FFF . n 
F 2 102 GLU 102 102 102 GLU GLU FFF . n 
F 2 103 SER 103 103 103 SER SER FFF . n 
F 2 104 TYR 104 104 104 TYR TYR FFF . n 
F 2 105 TYR 105 105 105 TYR TYR FFF . n 
F 2 106 TYR 106 106 106 TYR TYR FFF . n 
F 2 107 THR 107 107 107 THR THR FFF . n 
F 2 108 ARG 108 108 108 ARG ARG FFF . n 
F 2 109 PRO 109 109 109 PRO PRO FFF . n 
F 2 110 THR 110 110 110 THR THR FFF . n 
F 2 111 GLU 111 111 111 GLU GLU FFF . n 
F 2 112 TYR 112 112 112 TYR TYR FFF . n 
F 2 113 GLU 113 113 113 GLU GLU FFF . n 
F 2 114 PHE 114 114 114 PHE PHE FFF . n 
F 2 115 TRP 115 115 115 TRP TRP FFF . n 
F 2 116 GLY 116 116 116 GLY GLY FFF . n 
F 2 117 GLN 117 117 117 GLN GLN FFF . n 
F 2 118 GLY 118 118 118 GLY GLY FFF . n 
F 2 119 THR 119 119 119 THR THR FFF . n 
F 2 120 GLN 120 120 120 GLN GLN FFF . n 
F 2 121 VAL 121 121 121 VAL VAL FFF . n 
F 2 122 THR 122 122 122 THR THR FFF . n 
F 2 123 VAL 123 123 123 VAL VAL FFF . n 
F 2 124 SER 124 124 124 SER SER FFF . n 
F 2 125 SER 125 125 ?   ?   ?   FFF . n 
F 2 126 LYS 126 126 ?   ?   ?   FFF . n 
F 2 127 HIS 127 127 ?   ?   ?   FFF . n 
F 2 128 HIS 128 128 ?   ?   ?   FFF . n 
F 2 129 HIS 129 129 ?   ?   ?   FFF . n 
F 2 130 HIS 130 130 ?   ?   ?   FFF . n 
F 2 131 HIS 131 131 ?   ?   ?   FFF . n 
F 2 132 HIS 132 132 ?   ?   ?   FFF . n 
G 1 1   PRO 1   330 ?   ?   ?   GGG . n 
G 1 2   ASN 2   331 ?   ?   ?   GGG . n 
G 1 3   ILE 3   332 ?   ?   ?   GGG . n 
G 1 4   THR 4   333 333 THR THR GGG . n 
G 1 5   ASN 5   334 334 ASN ASN GGG . n 
G 1 6   LEU 6   335 335 LEU LEU GGG . n 
G 1 7   CYS 7   336 336 CYS CYS GGG . n 
G 1 8   PRO 8   337 337 PRO PRO GGG . n 
G 1 9   PHE 9   338 338 PHE PHE GGG . n 
G 1 10  GLY 10  339 339 GLY GLY GGG . n 
G 1 11  GLU 11  340 340 GLU GLU GGG . n 
G 1 12  VAL 12  341 341 VAL VAL GGG . n 
G 1 13  PHE 13  342 342 PHE PHE GGG . n 
G 1 14  ASN 14  343 343 ASN ASN GGG . n 
G 1 15  ALA 15  344 344 ALA ALA GGG . n 
G 1 16  THR 16  345 345 THR THR GGG . n 
G 1 17  ARG 17  346 346 ARG ARG GGG . n 
G 1 18  PHE 18  347 347 PHE PHE GGG . n 
G 1 19  ALA 19  348 348 ALA ALA GGG . n 
G 1 20  SER 20  349 349 SER SER GGG . n 
G 1 21  VAL 21  350 350 VAL VAL GGG . n 
G 1 22  TYR 22  351 351 TYR TYR GGG . n 
G 1 23  ALA 23  352 352 ALA ALA GGG . n 
G 1 24  TRP 24  353 353 TRP TRP GGG . n 
G 1 25  ASN 25  354 354 ASN ASN GGG . n 
G 1 26  ARG 26  355 355 ARG ARG GGG . n 
G 1 27  LYS 27  356 356 LYS LYS GGG . n 
G 1 28  ARG 28  357 357 ARG ARG GGG . n 
G 1 29  ILE 29  358 358 ILE ILE GGG . n 
G 1 30  SER 30  359 359 SER SER GGG . n 
G 1 31  ASN 31  360 360 ASN ASN GGG . n 
G 1 32  CYS 32  361 361 CYS CYS GGG . n 
G 1 33  VAL 33  362 362 VAL VAL GGG . n 
G 1 34  ALA 34  363 363 ALA ALA GGG . n 
G 1 35  ASP 35  364 364 ASP ASP GGG . n 
G 1 36  TYR 36  365 365 TYR TYR GGG . n 
G 1 37  SER 37  366 366 SER SER GGG . n 
G 1 38  VAL 38  367 367 VAL VAL GGG . n 
G 1 39  LEU 39  368 368 LEU LEU GGG . n 
G 1 40  TYR 40  369 369 TYR TYR GGG . n 
G 1 41  ASN 41  370 370 ASN ASN GGG . n 
G 1 42  SER 42  371 371 SER SER GGG . n 
G 1 43  ALA 43  372 372 ALA ALA GGG . n 
G 1 44  SER 44  373 373 SER SER GGG . n 
G 1 45  PHE 45  374 374 PHE PHE GGG . n 
G 1 46  SER 46  375 375 SER SER GGG . n 
G 1 47  THR 47  376 376 THR THR GGG . n 
G 1 48  PHE 48  377 377 PHE PHE GGG . n 
G 1 49  LYS 49  378 378 LYS LYS GGG . n 
G 1 50  CYS 50  379 379 CYS CYS GGG . n 
G 1 51  TYR 51  380 380 TYR TYR GGG . n 
G 1 52  GLY 52  381 381 GLY GLY GGG . n 
G 1 53  VAL 53  382 382 VAL VAL GGG . n 
G 1 54  SER 54  383 383 SER SER GGG . n 
G 1 55  PRO 55  384 384 PRO PRO GGG . n 
G 1 56  THR 56  385 385 THR THR GGG . n 
G 1 57  LYS 57  386 386 LYS LYS GGG . n 
G 1 58  LEU 58  387 387 LEU LEU GGG . n 
G 1 59  ASN 59  388 388 ASN ASN GGG . n 
G 1 60  ASP 60  389 389 ASP ASP GGG . n 
G 1 61  LEU 61  390 390 LEU LEU GGG . n 
G 1 62  CYS 62  391 391 CYS CYS GGG . n 
G 1 63  PHE 63  392 392 PHE PHE GGG . n 
G 1 64  THR 64  393 393 THR THR GGG . n 
G 1 65  ASN 65  394 394 ASN ASN GGG . n 
G 1 66  VAL 66  395 395 VAL VAL GGG . n 
G 1 67  TYR 67  396 396 TYR TYR GGG . n 
G 1 68  ALA 68  397 397 ALA ALA GGG . n 
G 1 69  ASP 69  398 398 ASP ASP GGG . n 
G 1 70  SER 70  399 399 SER SER GGG . n 
G 1 71  PHE 71  400 400 PHE PHE GGG . n 
G 1 72  VAL 72  401 401 VAL VAL GGG . n 
G 1 73  ILE 73  402 402 ILE ILE GGG . n 
G 1 74  ARG 74  403 403 ARG ARG GGG . n 
G 1 75  GLY 75  404 404 GLY GLY GGG . n 
G 1 76  ASP 76  405 405 ASP ASP GGG . n 
G 1 77  GLU 77  406 406 GLU GLU GGG . n 
G 1 78  VAL 78  407 407 VAL VAL GGG . n 
G 1 79  ARG 79  408 408 ARG ARG GGG . n 
G 1 80  GLN 80  409 409 GLN GLN GGG . n 
G 1 81  ILE 81  410 410 ILE ILE GGG . n 
G 1 82  ALA 82  411 411 ALA ALA GGG . n 
G 1 83  PRO 83  412 412 PRO PRO GGG . n 
G 1 84  GLY 84  413 413 GLY GLY GGG . n 
G 1 85  GLN 85  414 414 GLN GLN GGG . n 
G 1 86  THR 86  415 415 THR THR GGG . n 
G 1 87  GLY 87  416 416 GLY GLY GGG . n 
G 1 88  LYS 88  417 417 LYS LYS GGG . n 
G 1 89  ILE 89  418 418 ILE ILE GGG . n 
G 1 90  ALA 90  419 419 ALA ALA GGG . n 
G 1 91  ASP 91  420 420 ASP ASP GGG . n 
G 1 92  TYR 92  421 421 TYR TYR GGG . n 
G 1 93  ASN 93  422 422 ASN ASN GGG . n 
G 1 94  TYR 94  423 423 TYR TYR GGG . n 
G 1 95  LYS 95  424 424 LYS LYS GGG . n 
G 1 96  LEU 96  425 425 LEU LEU GGG . n 
G 1 97  PRO 97  426 426 PRO PRO GGG . n 
G 1 98  ASP 98  427 427 ASP ASP GGG . n 
G 1 99  ASP 99  428 428 ASP ASP GGG . n 
G 1 100 PHE 100 429 429 PHE PHE GGG . n 
G 1 101 THR 101 430 430 THR THR GGG . n 
G 1 102 GLY 102 431 431 GLY GLY GGG . n 
G 1 103 CYS 103 432 432 CYS CYS GGG . n 
G 1 104 VAL 104 433 433 VAL VAL GGG . n 
G 1 105 ILE 105 434 434 ILE ILE GGG . n 
G 1 106 ALA 106 435 435 ALA ALA GGG . n 
G 1 107 TRP 107 436 436 TRP TRP GGG . n 
G 1 108 ASN 108 437 437 ASN ASN GGG . n 
G 1 109 SER 109 438 438 SER SER GGG . n 
G 1 110 ASN 110 439 439 ASN ASN GGG . n 
G 1 111 ASN 111 440 440 ASN ASN GGG . n 
G 1 112 LEU 112 441 441 LEU LEU GGG . n 
G 1 113 ASP 113 442 442 ASP ASP GGG . n 
G 1 114 SER 114 443 443 SER SER GGG . n 
G 1 115 LYS 115 444 444 LYS LYS GGG . n 
G 1 116 VAL 116 445 445 VAL VAL GGG . n 
G 1 117 GLY 117 446 446 GLY GLY GGG . n 
G 1 118 GLY 118 447 447 GLY GLY GGG . n 
G 1 119 ASN 119 448 448 ASN ASN GGG . n 
G 1 120 TYR 120 449 449 TYR TYR GGG . n 
G 1 121 ASN 121 450 450 ASN ASN GGG . n 
G 1 122 TYR 122 451 451 TYR TYR GGG . n 
G 1 123 LEU 123 452 452 LEU LEU GGG . n 
G 1 124 TYR 124 453 453 TYR TYR GGG . n 
G 1 125 ARG 125 454 454 ARG ARG GGG . n 
G 1 126 LEU 126 455 455 LEU LEU GGG . n 
G 1 127 PHE 127 456 456 PHE PHE GGG . n 
G 1 128 ARG 128 457 457 ARG ARG GGG . n 
G 1 129 LYS 129 458 458 LYS LYS GGG . n 
G 1 130 SER 130 459 459 SER SER GGG . n 
G 1 131 ASN 131 460 460 ASN ASN GGG . n 
G 1 132 LEU 132 461 461 LEU LEU GGG . n 
G 1 133 LYS 133 462 462 LYS LYS GGG . n 
G 1 134 PRO 134 463 463 PRO PRO GGG . n 
G 1 135 PHE 135 464 464 PHE PHE GGG . n 
G 1 136 GLU 136 465 465 GLU GLU GGG . n 
G 1 137 ARG 137 466 466 ARG ARG GGG . n 
G 1 138 ASP 138 467 467 ASP ASP GGG . n 
G 1 139 ILE 139 468 468 ILE ILE GGG . n 
G 1 140 SER 140 469 469 SER SER GGG . n 
G 1 141 THR 141 470 470 THR THR GGG . n 
G 1 142 GLU 142 471 471 GLU GLU GGG . n 
G 1 143 ILE 143 472 472 ILE ILE GGG . n 
G 1 144 TYR 144 473 473 TYR TYR GGG . n 
G 1 145 GLN 145 474 474 GLN GLN GGG . n 
G 1 146 ALA 146 475 475 ALA ALA GGG . n 
G 1 147 GLY 147 476 476 GLY GLY GGG . n 
G 1 148 SER 148 477 477 SER SER GGG . n 
G 1 149 THR 149 478 478 THR THR GGG . n 
G 1 150 PRO 150 479 479 PRO PRO GGG . n 
G 1 151 CYS 151 480 480 CYS CYS GGG . n 
G 1 152 ASN 152 481 481 ASN ASN GGG . n 
G 1 153 GLY 153 482 482 GLY GLY GGG . n 
G 1 154 VAL 154 483 483 VAL VAL GGG . n 
G 1 155 GLU 155 484 484 GLU GLU GGG . n 
G 1 156 GLY 156 485 485 GLY GLY GGG . n 
G 1 157 PHE 157 486 486 PHE PHE GGG . n 
G 1 158 ASN 158 487 487 ASN ASN GGG . n 
G 1 159 CYS 159 488 488 CYS CYS GGG . n 
G 1 160 TYR 160 489 489 TYR TYR GGG . n 
G 1 161 PHE 161 490 490 PHE PHE GGG . n 
G 1 162 PRO 162 491 491 PRO PRO GGG . n 
G 1 163 LEU 163 492 492 LEU LEU GGG . n 
G 1 164 GLN 164 493 493 GLN GLN GGG . n 
G 1 165 SER 165 494 494 SER SER GGG . n 
G 1 166 TYR 166 495 495 TYR TYR GGG . n 
G 1 167 GLY 167 496 496 GLY GLY GGG . n 
G 1 168 PHE 168 497 497 PHE PHE GGG . n 
G 1 169 GLN 169 498 498 GLN GLN GGG . n 
G 1 170 PRO 170 499 499 PRO PRO GGG . n 
G 1 171 THR 171 500 500 THR THR GGG . n 
G 1 172 ASN 172 501 501 ASN ASN GGG . n 
G 1 173 GLY 173 502 502 GLY GLY GGG . n 
G 1 174 VAL 174 503 503 VAL VAL GGG . n 
G 1 175 GLY 175 504 504 GLY GLY GGG . n 
G 1 176 TYR 176 505 505 TYR TYR GGG . n 
G 1 177 GLN 177 506 506 GLN GLN GGG . n 
G 1 178 PRO 178 507 507 PRO PRO GGG . n 
G 1 179 TYR 179 508 508 TYR TYR GGG . n 
G 1 180 ARG 180 509 509 ARG ARG GGG . n 
G 1 181 VAL 181 510 510 VAL VAL GGG . n 
G 1 182 VAL 182 511 511 VAL VAL GGG . n 
G 1 183 VAL 183 512 512 VAL VAL GGG . n 
G 1 184 LEU 184 513 513 LEU LEU GGG . n 
G 1 185 SER 185 514 514 SER SER GGG . n 
G 1 186 PHE 186 515 515 PHE PHE GGG . n 
G 1 187 GLU 187 516 516 GLU GLU GGG . n 
G 1 188 LEU 188 517 517 LEU LEU GGG . n 
G 1 189 LEU 189 518 518 LEU LEU GGG . n 
G 1 190 HIS 190 519 519 HIS HIS GGG . n 
G 1 191 ALA 191 520 520 ALA ALA GGG . n 
G 1 192 PRO 192 521 521 PRO PRO GGG . n 
G 1 193 ALA 193 522 522 ALA ALA GGG . n 
G 1 194 THR 194 523 523 THR THR GGG . n 
G 1 195 VAL 195 524 524 VAL VAL GGG . n 
G 1 196 CYS 196 525 525 CYS CYS GGG . n 
G 1 197 GLY 197 526 526 GLY GLY GGG . n 
G 1 198 PRO 198 527 527 PRO PRO GGG . n 
G 1 199 LYS 199 528 528 LYS LYS GGG . n 
G 1 200 LYS 200 529 ?   ?   ?   GGG . n 
G 1 201 SER 201 530 ?   ?   ?   GGG . n 
G 1 202 THR 202 531 ?   ?   ?   GGG . n 
G 1 203 ASN 203 532 ?   ?   ?   GGG . n 
G 1 204 LYS 204 533 ?   ?   ?   GGG . n 
G 1 205 HIS 205 534 ?   ?   ?   GGG . n 
G 1 206 HIS 206 535 ?   ?   ?   GGG . n 
G 1 207 HIS 207 536 ?   ?   ?   GGG . n 
G 1 208 HIS 208 537 ?   ?   ?   GGG . n 
G 1 209 HIS 209 538 ?   ?   ?   GGG . n 
G 1 210 HIS 210 539 ?   ?   ?   GGG . n 
H 2 1   GLN 1   1   1   GLN GLN HHH . n 
H 2 2   VAL 2   2   2   VAL VAL HHH . n 
H 2 3   GLN 3   3   3   GLN GLN HHH . n 
H 2 4   LEU 4   4   4   LEU LEU HHH . n 
H 2 5   VAL 5   5   5   VAL VAL HHH . n 
H 2 6   GLU 6   6   6   GLU GLU HHH . n 
H 2 7   SER 7   7   7   SER SER HHH . n 
H 2 8   GLY 8   8   8   GLY GLY HHH . n 
H 2 9   GLY 9   9   9   GLY GLY HHH . n 
H 2 10  GLY 10  10  10  GLY GLY HHH . n 
H 2 11  LEU 11  11  11  LEU LEU HHH . n 
H 2 12  VAL 12  12  12  VAL VAL HHH . n 
H 2 13  GLN 13  13  13  GLN GLN HHH . n 
H 2 14  ALA 14  14  14  ALA ALA HHH . n 
H 2 15  GLY 15  15  15  GLY GLY HHH . n 
H 2 16  GLY 16  16  16  GLY GLY HHH . n 
H 2 17  SER 17  17  17  SER SER HHH . n 
H 2 18  LEU 18  18  18  LEU LEU HHH . n 
H 2 19  ARG 19  19  19  ARG ARG HHH . n 
H 2 20  LEU 20  20  20  LEU LEU HHH . n 
H 2 21  ALA 21  21  21  ALA ALA HHH . n 
H 2 22  CYS 22  22  22  CYS CYS HHH . n 
H 2 23  ILE 23  23  23  ILE ILE HHH . n 
H 2 24  ALA 24  24  24  ALA ALA HHH . n 
H 2 25  SER 25  25  25  SER SER HHH . n 
H 2 26  GLY 26  26  26  GLY GLY HHH . n 
H 2 27  ARG 27  27  27  ARG ARG HHH . n 
H 2 28  THR 28  28  28  THR THR HHH . n 
H 2 29  PHE 29  29  29  PHE PHE HHH . n 
H 2 30  HIS 30  30  30  HIS HIS HHH . n 
H 2 31  SER 31  31  31  SER SER HHH . n 
H 2 32  TYR 32  32  32  TYR TYR HHH . n 
H 2 33  VAL 33  33  33  VAL VAL HHH . n 
H 2 34  MET 34  34  34  MET MET HHH . n 
H 2 35  ALA 35  35  35  ALA ALA HHH . n 
H 2 36  TRP 36  36  36  TRP TRP HHH . n 
H 2 37  PHE 37  37  37  PHE PHE HHH . n 
H 2 38  ARG 38  38  38  ARG ARG HHH . n 
H 2 39  GLN 39  39  39  GLN GLN HHH . n 
H 2 40  ALA 40  40  40  ALA ALA HHH . n 
H 2 41  PRO 41  41  41  PRO PRO HHH . n 
H 2 42  GLY 42  42  42  GLY GLY HHH . n 
H 2 43  LYS 43  43  43  LYS LYS HHH . n 
H 2 44  GLU 44  44  44  GLU GLU HHH . n 
H 2 45  ARG 45  45  45  ARG ARG HHH . n 
H 2 46  GLU 46  46  46  GLU GLU HHH . n 
H 2 47  PHE 47  47  47  PHE PHE HHH . n 
H 2 48  VAL 48  48  48  VAL VAL HHH . n 
H 2 49  ALA 49  49  49  ALA ALA HHH . n 
H 2 50  ALA 50  50  50  ALA ALA HHH . n 
H 2 51  ILE 51  51  51  ILE ILE HHH . n 
H 2 52  SER 52  52  52  SER SER HHH . n 
H 2 53  TRP 53  53  53  TRP TRP HHH . n 
H 2 54  SER 54  54  54  SER SER HHH . n 
H 2 55  SER 55  55  55  SER SER HHH . n 
H 2 56  THR 56  56  56  THR THR HHH . n 
H 2 57  PRO 57  57  57  PRO PRO HHH . n 
H 2 58  THR 58  58  58  THR THR HHH . n 
H 2 59  TYR 59  59  59  TYR TYR HHH . n 
H 2 60  TYR 60  60  60  TYR TYR HHH . n 
H 2 61  GLY 61  61  61  GLY GLY HHH . n 
H 2 62  GLU 62  62  62  GLU GLU HHH . n 
H 2 63  SER 63  63  63  SER SER HHH . n 
H 2 64  VAL 64  64  64  VAL VAL HHH . n 
H 2 65  LYS 65  65  65  LYS LYS HHH . n 
H 2 66  GLY 66  66  66  GLY GLY HHH . n 
H 2 67  ARG 67  67  67  ARG ARG HHH . n 
H 2 68  PHE 68  68  68  PHE PHE HHH . n 
H 2 69  THR 69  69  69  THR THR HHH . n 
H 2 70  ILE 70  70  70  ILE ILE HHH . n 
H 2 71  SER 71  71  71  SER SER HHH . n 
H 2 72  ARG 72  72  72  ARG ARG HHH . n 
H 2 73  ASP 73  73  73  ASP ASP HHH . n 
H 2 74  ASN 74  74  74  ASN ASN HHH . n 
H 2 75  ALA 75  75  75  ALA ALA HHH . n 
H 2 76  LYS 76  76  76  LYS LYS HHH . n 
H 2 77  ASN 77  77  77  ASN ASN HHH . n 
H 2 78  THR 78  78  78  THR THR HHH . n 
H 2 79  VAL 79  79  79  VAL VAL HHH . n 
H 2 80  TYR 80  80  80  TYR TYR HHH . n 
H 2 81  LEU 81  81  81  LEU LEU HHH . n 
H 2 82  GLN 82  82  82  GLN GLN HHH . n 
H 2 83  MET 83  83  83  MET MET HHH . n 
H 2 84  ASN 84  84  84  ASN ASN HHH . n 
H 2 85  ARG 85  85  85  ARG ARG HHH . n 
H 2 86  LEU 86  86  86  LEU LEU HHH . n 
H 2 87  LYS 87  87  87  LYS LYS HHH . n 
H 2 88  PRO 88  88  88  PRO PRO HHH . n 
H 2 89  GLU 89  89  89  GLU GLU HHH . n 
H 2 90  ASP 90  90  90  ASP ASP HHH . n 
H 2 91  THR 91  91  91  THR THR HHH . n 
H 2 92  ALA 92  92  92  ALA ALA HHH . n 
H 2 93  VAL 93  93  93  VAL VAL HHH . n 
H 2 94  TYR 94  94  94  TYR TYR HHH . n 
H 2 95  PHE 95  95  95  PHE PHE HHH . n 
H 2 96  CYS 96  96  96  CYS CYS HHH . n 
H 2 97  ALA 97  97  97  ALA ALA HHH . n 
H 2 98  ALA 98  98  98  ALA ALA HHH . n 
H 2 99  ASP 99  99  99  ASP ASP HHH . n 
H 2 100 ARG 100 100 100 ARG ARG HHH . n 
H 2 101 GLY 101 101 101 GLY GLY HHH . n 
H 2 102 GLU 102 102 102 GLU GLU HHH . n 
H 2 103 SER 103 103 103 SER SER HHH . n 
H 2 104 TYR 104 104 104 TYR TYR HHH . n 
H 2 105 TYR 105 105 105 TYR TYR HHH . n 
H 2 106 TYR 106 106 106 TYR TYR HHH . n 
H 2 107 THR 107 107 107 THR THR HHH . n 
H 2 108 ARG 108 108 108 ARG ARG HHH . n 
H 2 109 PRO 109 109 109 PRO PRO HHH . n 
H 2 110 THR 110 110 110 THR THR HHH . n 
H 2 111 GLU 111 111 111 GLU GLU HHH . n 
H 2 112 TYR 112 112 112 TYR TYR HHH . n 
H 2 113 GLU 113 113 113 GLU GLU HHH . n 
H 2 114 PHE 114 114 114 PHE PHE HHH . n 
H 2 115 TRP 115 115 115 TRP TRP HHH . n 
H 2 116 GLY 116 116 116 GLY GLY HHH . n 
H 2 117 GLN 117 117 117 GLN GLN HHH . n 
H 2 118 GLY 118 118 118 GLY GLY HHH . n 
H 2 119 THR 119 119 119 THR THR HHH . n 
H 2 120 GLN 120 120 120 GLN GLN HHH . n 
H 2 121 VAL 121 121 121 VAL VAL HHH . n 
H 2 122 THR 122 122 122 THR THR HHH . n 
H 2 123 VAL 123 123 123 VAL VAL HHH . n 
H 2 124 SER 124 124 124 SER SER HHH . n 
H 2 125 SER 125 125 125 SER SER HHH . n 
H 2 126 LYS 126 126 ?   ?   ?   HHH . n 
H 2 127 HIS 127 127 ?   ?   ?   HHH . n 
H 2 128 HIS 128 128 ?   ?   ?   HHH . n 
H 2 129 HIS 129 129 ?   ?   ?   HHH . n 
H 2 130 HIS 130 130 ?   ?   ?   HHH . n 
H 2 131 HIS 131 131 ?   ?   ?   HHH . n 
H 2 132 HIS 132 132 ?   ?   ?   HHH . n 
I 1 1   PRO 1   330 ?   ?   ?   III . n 
I 1 2   ASN 2   331 331 ASN ASN III . n 
I 1 3   ILE 3   332 332 ILE ILE III . n 
I 1 4   THR 4   333 333 THR THR III . n 
I 1 5   ASN 5   334 334 ASN ASN III . n 
I 1 6   LEU 6   335 335 LEU LEU III . n 
I 1 7   CYS 7   336 336 CYS CYS III . n 
I 1 8   PRO 8   337 337 PRO PRO III . n 
I 1 9   PHE 9   338 338 PHE PHE III . n 
I 1 10  GLY 10  339 339 GLY GLY III . n 
I 1 11  GLU 11  340 340 GLU GLU III . n 
I 1 12  VAL 12  341 341 VAL VAL III . n 
I 1 13  PHE 13  342 342 PHE PHE III . n 
I 1 14  ASN 14  343 343 ASN ASN III . n 
I 1 15  ALA 15  344 344 ALA ALA III . n 
I 1 16  THR 16  345 345 THR THR III . n 
I 1 17  ARG 17  346 346 ARG ARG III . n 
I 1 18  PHE 18  347 347 PHE PHE III . n 
I 1 19  ALA 19  348 348 ALA ALA III . n 
I 1 20  SER 20  349 349 SER SER III . n 
I 1 21  VAL 21  350 350 VAL VAL III . n 
I 1 22  TYR 22  351 351 TYR TYR III . n 
I 1 23  ALA 23  352 352 ALA ALA III . n 
I 1 24  TRP 24  353 353 TRP TRP III . n 
I 1 25  ASN 25  354 354 ASN ASN III . n 
I 1 26  ARG 26  355 355 ARG ARG III . n 
I 1 27  LYS 27  356 356 LYS LYS III . n 
I 1 28  ARG 28  357 357 ARG ARG III . n 
I 1 29  ILE 29  358 358 ILE ILE III . n 
I 1 30  SER 30  359 359 SER SER III . n 
I 1 31  ASN 31  360 360 ASN ASN III . n 
I 1 32  CYS 32  361 361 CYS CYS III . n 
I 1 33  VAL 33  362 362 VAL VAL III . n 
I 1 34  ALA 34  363 363 ALA ALA III . n 
I 1 35  ASP 35  364 364 ASP ASP III . n 
I 1 36  TYR 36  365 365 TYR TYR III . n 
I 1 37  SER 37  366 366 SER SER III . n 
I 1 38  VAL 38  367 367 VAL VAL III . n 
I 1 39  LEU 39  368 368 LEU LEU III . n 
I 1 40  TYR 40  369 369 TYR TYR III . n 
I 1 41  ASN 41  370 370 ASN ASN III . n 
I 1 42  SER 42  371 371 SER SER III . n 
I 1 43  ALA 43  372 372 ALA ALA III . n 
I 1 44  SER 44  373 373 SER SER III . n 
I 1 45  PHE 45  374 374 PHE PHE III . n 
I 1 46  SER 46  375 375 SER SER III . n 
I 1 47  THR 47  376 376 THR THR III . n 
I 1 48  PHE 48  377 377 PHE PHE III . n 
I 1 49  LYS 49  378 378 LYS LYS III . n 
I 1 50  CYS 50  379 379 CYS CYS III . n 
I 1 51  TYR 51  380 380 TYR TYR III . n 
I 1 52  GLY 52  381 381 GLY GLY III . n 
I 1 53  VAL 53  382 382 VAL VAL III . n 
I 1 54  SER 54  383 383 SER SER III . n 
I 1 55  PRO 55  384 384 PRO PRO III . n 
I 1 56  THR 56  385 385 THR THR III . n 
I 1 57  LYS 57  386 386 LYS LYS III . n 
I 1 58  LEU 58  387 387 LEU LEU III . n 
I 1 59  ASN 59  388 388 ASN ASN III . n 
I 1 60  ASP 60  389 389 ASP ASP III . n 
I 1 61  LEU 61  390 390 LEU LEU III . n 
I 1 62  CYS 62  391 391 CYS CYS III . n 
I 1 63  PHE 63  392 392 PHE PHE III . n 
I 1 64  THR 64  393 393 THR THR III . n 
I 1 65  ASN 65  394 394 ASN ASN III . n 
I 1 66  VAL 66  395 395 VAL VAL III . n 
I 1 67  TYR 67  396 396 TYR TYR III . n 
I 1 68  ALA 68  397 397 ALA ALA III . n 
I 1 69  ASP 69  398 398 ASP ASP III . n 
I 1 70  SER 70  399 399 SER SER III . n 
I 1 71  PHE 71  400 400 PHE PHE III . n 
I 1 72  VAL 72  401 401 VAL VAL III . n 
I 1 73  ILE 73  402 402 ILE ILE III . n 
I 1 74  ARG 74  403 403 ARG ARG III . n 
I 1 75  GLY 75  404 404 GLY GLY III . n 
I 1 76  ASP 76  405 405 ASP ASP III . n 
I 1 77  GLU 77  406 406 GLU GLU III . n 
I 1 78  VAL 78  407 407 VAL VAL III . n 
I 1 79  ARG 79  408 408 ARG ARG III . n 
I 1 80  GLN 80  409 409 GLN GLN III . n 
I 1 81  ILE 81  410 410 ILE ILE III . n 
I 1 82  ALA 82  411 411 ALA ALA III . n 
I 1 83  PRO 83  412 412 PRO PRO III . n 
I 1 84  GLY 84  413 413 GLY GLY III . n 
I 1 85  GLN 85  414 414 GLN GLN III . n 
I 1 86  THR 86  415 415 THR THR III . n 
I 1 87  GLY 87  416 416 GLY GLY III . n 
I 1 88  LYS 88  417 417 LYS LYS III . n 
I 1 89  ILE 89  418 418 ILE ILE III . n 
I 1 90  ALA 90  419 419 ALA ALA III . n 
I 1 91  ASP 91  420 420 ASP ASP III . n 
I 1 92  TYR 92  421 421 TYR TYR III . n 
I 1 93  ASN 93  422 422 ASN ASN III . n 
I 1 94  TYR 94  423 423 TYR TYR III . n 
I 1 95  LYS 95  424 424 LYS LYS III . n 
I 1 96  LEU 96  425 425 LEU LEU III . n 
I 1 97  PRO 97  426 426 PRO PRO III . n 
I 1 98  ASP 98  427 427 ASP ASP III . n 
I 1 99  ASP 99  428 428 ASP ASP III . n 
I 1 100 PHE 100 429 429 PHE PHE III . n 
I 1 101 THR 101 430 430 THR THR III . n 
I 1 102 GLY 102 431 431 GLY GLY III . n 
I 1 103 CYS 103 432 432 CYS CYS III . n 
I 1 104 VAL 104 433 433 VAL VAL III . n 
I 1 105 ILE 105 434 434 ILE ILE III . n 
I 1 106 ALA 106 435 435 ALA ALA III . n 
I 1 107 TRP 107 436 436 TRP TRP III . n 
I 1 108 ASN 108 437 437 ASN ASN III . n 
I 1 109 SER 109 438 438 SER SER III . n 
I 1 110 ASN 110 439 439 ASN ASN III . n 
I 1 111 ASN 111 440 440 ASN ASN III . n 
I 1 112 LEU 112 441 441 LEU LEU III . n 
I 1 113 ASP 113 442 442 ASP ASP III . n 
I 1 114 SER 114 443 443 SER SER III . n 
I 1 115 LYS 115 444 444 LYS LYS III . n 
I 1 116 VAL 116 445 445 VAL VAL III . n 
I 1 117 GLY 117 446 446 GLY GLY III . n 
I 1 118 GLY 118 447 447 GLY GLY III . n 
I 1 119 ASN 119 448 448 ASN ASN III . n 
I 1 120 TYR 120 449 449 TYR TYR III . n 
I 1 121 ASN 121 450 450 ASN ASN III . n 
I 1 122 TYR 122 451 451 TYR TYR III . n 
I 1 123 LEU 123 452 452 LEU LEU III . n 
I 1 124 TYR 124 453 453 TYR TYR III . n 
I 1 125 ARG 125 454 454 ARG ARG III . n 
I 1 126 LEU 126 455 455 LEU LEU III . n 
I 1 127 PHE 127 456 456 PHE PHE III . n 
I 1 128 ARG 128 457 457 ARG ARG III . n 
I 1 129 LYS 129 458 458 LYS LYS III . n 
I 1 130 SER 130 459 459 SER SER III . n 
I 1 131 ASN 131 460 460 ASN ASN III . n 
I 1 132 LEU 132 461 461 LEU LEU III . n 
I 1 133 LYS 133 462 462 LYS LYS III . n 
I 1 134 PRO 134 463 463 PRO PRO III . n 
I 1 135 PHE 135 464 464 PHE PHE III . n 
I 1 136 GLU 136 465 465 GLU GLU III . n 
I 1 137 ARG 137 466 466 ARG ARG III . n 
I 1 138 ASP 138 467 467 ASP ASP III . n 
I 1 139 ILE 139 468 468 ILE ILE III . n 
I 1 140 SER 140 469 469 SER SER III . n 
I 1 141 THR 141 470 470 THR THR III . n 
I 1 142 GLU 142 471 471 GLU GLU III . n 
I 1 143 ILE 143 472 472 ILE ILE III . n 
I 1 144 TYR 144 473 473 TYR TYR III . n 
I 1 145 GLN 145 474 474 GLN GLN III . n 
I 1 146 ALA 146 475 475 ALA ALA III . n 
I 1 147 GLY 147 476 476 GLY GLY III . n 
I 1 148 SER 148 477 477 SER SER III . n 
I 1 149 THR 149 478 478 THR THR III . n 
I 1 150 PRO 150 479 479 PRO PRO III . n 
I 1 151 CYS 151 480 480 CYS CYS III . n 
I 1 152 ASN 152 481 481 ASN ASN III . n 
I 1 153 GLY 153 482 482 GLY GLY III . n 
I 1 154 VAL 154 483 483 VAL VAL III . n 
I 1 155 GLU 155 484 484 GLU GLU III . n 
I 1 156 GLY 156 485 485 GLY GLY III . n 
I 1 157 PHE 157 486 486 PHE PHE III . n 
I 1 158 ASN 158 487 487 ASN ASN III . n 
I 1 159 CYS 159 488 488 CYS CYS III . n 
I 1 160 TYR 160 489 489 TYR TYR III . n 
I 1 161 PHE 161 490 490 PHE PHE III . n 
I 1 162 PRO 162 491 491 PRO PRO III . n 
I 1 163 LEU 163 492 492 LEU LEU III . n 
I 1 164 GLN 164 493 493 GLN GLN III . n 
I 1 165 SER 165 494 494 SER SER III . n 
I 1 166 TYR 166 495 495 TYR TYR III . n 
I 1 167 GLY 167 496 496 GLY GLY III . n 
I 1 168 PHE 168 497 497 PHE PHE III . n 
I 1 169 GLN 169 498 498 GLN GLN III . n 
I 1 170 PRO 170 499 499 PRO PRO III . n 
I 1 171 THR 171 500 500 THR THR III . n 
I 1 172 ASN 172 501 501 ASN ASN III . n 
I 1 173 GLY 173 502 502 GLY GLY III . n 
I 1 174 VAL 174 503 503 VAL VAL III . n 
I 1 175 GLY 175 504 504 GLY GLY III . n 
I 1 176 TYR 176 505 505 TYR TYR III . n 
I 1 177 GLN 177 506 506 GLN GLN III . n 
I 1 178 PRO 178 507 507 PRO PRO III . n 
I 1 179 TYR 179 508 508 TYR TYR III . n 
I 1 180 ARG 180 509 509 ARG ARG III . n 
I 1 181 VAL 181 510 510 VAL VAL III . n 
I 1 182 VAL 182 511 511 VAL VAL III . n 
I 1 183 VAL 183 512 512 VAL VAL III . n 
I 1 184 LEU 184 513 513 LEU LEU III . n 
I 1 185 SER 185 514 514 SER SER III . n 
I 1 186 PHE 186 515 515 PHE PHE III . n 
I 1 187 GLU 187 516 516 GLU GLU III . n 
I 1 188 LEU 188 517 517 LEU LEU III . n 
I 1 189 LEU 189 518 518 LEU LEU III . n 
I 1 190 HIS 190 519 519 HIS HIS III . n 
I 1 191 ALA 191 520 520 ALA ALA III . n 
I 1 192 PRO 192 521 521 PRO PRO III . n 
I 1 193 ALA 193 522 522 ALA ALA III . n 
I 1 194 THR 194 523 523 THR THR III . n 
I 1 195 VAL 195 524 524 VAL VAL III . n 
I 1 196 CYS 196 525 525 CYS CYS III . n 
I 1 197 GLY 197 526 526 GLY GLY III . n 
I 1 198 PRO 198 527 527 PRO PRO III . n 
I 1 199 LYS 199 528 528 LYS LYS III . n 
I 1 200 LYS 200 529 ?   ?   ?   III . n 
I 1 201 SER 201 530 ?   ?   ?   III . n 
I 1 202 THR 202 531 ?   ?   ?   III . n 
I 1 203 ASN 203 532 ?   ?   ?   III . n 
I 1 204 LYS 204 533 ?   ?   ?   III . n 
I 1 205 HIS 205 534 ?   ?   ?   III . n 
I 1 206 HIS 206 535 ?   ?   ?   III . n 
I 1 207 HIS 207 536 ?   ?   ?   III . n 
I 1 208 HIS 208 537 ?   ?   ?   III . n 
I 1 209 HIS 209 538 ?   ?   ?   III . n 
I 1 210 HIS 210 539 ?   ?   ?   III . n 
J 2 1   GLN 1   1   1   GLN GLN JJJ . n 
J 2 2   VAL 2   2   2   VAL VAL JJJ . n 
J 2 3   GLN 3   3   3   GLN GLN JJJ . n 
J 2 4   LEU 4   4   4   LEU LEU JJJ . n 
J 2 5   VAL 5   5   5   VAL VAL JJJ . n 
J 2 6   GLU 6   6   6   GLU GLU JJJ . n 
J 2 7   SER 7   7   7   SER SER JJJ . n 
J 2 8   GLY 8   8   8   GLY GLY JJJ . n 
J 2 9   GLY 9   9   9   GLY GLY JJJ . n 
J 2 10  GLY 10  10  10  GLY GLY JJJ . n 
J 2 11  LEU 11  11  11  LEU LEU JJJ . n 
J 2 12  VAL 12  12  12  VAL VAL JJJ . n 
J 2 13  GLN 13  13  13  GLN GLN JJJ . n 
J 2 14  ALA 14  14  14  ALA ALA JJJ . n 
J 2 15  GLY 15  15  15  GLY GLY JJJ . n 
J 2 16  GLY 16  16  16  GLY GLY JJJ . n 
J 2 17  SER 17  17  17  SER SER JJJ . n 
J 2 18  LEU 18  18  18  LEU LEU JJJ . n 
J 2 19  ARG 19  19  19  ARG ARG JJJ . n 
J 2 20  LEU 20  20  20  LEU LEU JJJ . n 
J 2 21  ALA 21  21  21  ALA ALA JJJ . n 
J 2 22  CYS 22  22  22  CYS CYS JJJ . n 
J 2 23  ILE 23  23  23  ILE ILE JJJ . n 
J 2 24  ALA 24  24  24  ALA ALA JJJ . n 
J 2 25  SER 25  25  25  SER SER JJJ . n 
J 2 26  GLY 26  26  26  GLY GLY JJJ . n 
J 2 27  ARG 27  27  27  ARG ARG JJJ . n 
J 2 28  THR 28  28  28  THR THR JJJ . n 
J 2 29  PHE 29  29  29  PHE PHE JJJ . n 
J 2 30  HIS 30  30  30  HIS HIS JJJ . n 
J 2 31  SER 31  31  31  SER SER JJJ . n 
J 2 32  TYR 32  32  32  TYR TYR JJJ . n 
J 2 33  VAL 33  33  33  VAL VAL JJJ . n 
J 2 34  MET 34  34  34  MET MET JJJ . n 
J 2 35  ALA 35  35  35  ALA ALA JJJ . n 
J 2 36  TRP 36  36  36  TRP TRP JJJ . n 
J 2 37  PHE 37  37  37  PHE PHE JJJ . n 
J 2 38  ARG 38  38  38  ARG ARG JJJ . n 
J 2 39  GLN 39  39  39  GLN GLN JJJ . n 
J 2 40  ALA 40  40  40  ALA ALA JJJ . n 
J 2 41  PRO 41  41  41  PRO PRO JJJ . n 
J 2 42  GLY 42  42  42  GLY GLY JJJ . n 
J 2 43  LYS 43  43  43  LYS LYS JJJ . n 
J 2 44  GLU 44  44  44  GLU GLU JJJ . n 
J 2 45  ARG 45  45  45  ARG ARG JJJ . n 
J 2 46  GLU 46  46  46  GLU GLU JJJ . n 
J 2 47  PHE 47  47  47  PHE PHE JJJ . n 
J 2 48  VAL 48  48  48  VAL VAL JJJ . n 
J 2 49  ALA 49  49  49  ALA ALA JJJ . n 
J 2 50  ALA 50  50  50  ALA ALA JJJ . n 
J 2 51  ILE 51  51  51  ILE ILE JJJ . n 
J 2 52  SER 52  52  52  SER SER JJJ . n 
J 2 53  TRP 53  53  53  TRP TRP JJJ . n 
J 2 54  SER 54  54  54  SER SER JJJ . n 
J 2 55  SER 55  55  55  SER SER JJJ . n 
J 2 56  THR 56  56  56  THR THR JJJ . n 
J 2 57  PRO 57  57  57  PRO PRO JJJ . n 
J 2 58  THR 58  58  58  THR THR JJJ . n 
J 2 59  TYR 59  59  59  TYR TYR JJJ . n 
J 2 60  TYR 60  60  60  TYR TYR JJJ . n 
J 2 61  GLY 61  61  61  GLY GLY JJJ . n 
J 2 62  GLU 62  62  62  GLU GLU JJJ . n 
J 2 63  SER 63  63  63  SER SER JJJ . n 
J 2 64  VAL 64  64  64  VAL VAL JJJ . n 
J 2 65  LYS 65  65  65  LYS LYS JJJ . n 
J 2 66  GLY 66  66  66  GLY GLY JJJ . n 
J 2 67  ARG 67  67  67  ARG ARG JJJ . n 
J 2 68  PHE 68  68  68  PHE PHE JJJ . n 
J 2 69  THR 69  69  69  THR THR JJJ . n 
J 2 70  ILE 70  70  70  ILE ILE JJJ . n 
J 2 71  SER 71  71  71  SER SER JJJ . n 
J 2 72  ARG 72  72  72  ARG ARG JJJ . n 
J 2 73  ASP 73  73  73  ASP ASP JJJ . n 
J 2 74  ASN 74  74  74  ASN ASN JJJ . n 
J 2 75  ALA 75  75  75  ALA ALA JJJ . n 
J 2 76  LYS 76  76  76  LYS LYS JJJ . n 
J 2 77  ASN 77  77  77  ASN ASN JJJ . n 
J 2 78  THR 78  78  78  THR THR JJJ . n 
J 2 79  VAL 79  79  79  VAL VAL JJJ . n 
J 2 80  TYR 80  80  80  TYR TYR JJJ . n 
J 2 81  LEU 81  81  81  LEU LEU JJJ . n 
J 2 82  GLN 82  82  82  GLN GLN JJJ . n 
J 2 83  MET 83  83  83  MET MET JJJ . n 
J 2 84  ASN 84  84  84  ASN ASN JJJ . n 
J 2 85  ARG 85  85  85  ARG ARG JJJ . n 
J 2 86  LEU 86  86  86  LEU LEU JJJ . n 
J 2 87  LYS 87  87  87  LYS LYS JJJ . n 
J 2 88  PRO 88  88  88  PRO PRO JJJ . n 
J 2 89  GLU 89  89  89  GLU GLU JJJ . n 
J 2 90  ASP 90  90  90  ASP ASP JJJ . n 
J 2 91  THR 91  91  91  THR THR JJJ . n 
J 2 92  ALA 92  92  92  ALA ALA JJJ . n 
J 2 93  VAL 93  93  93  VAL VAL JJJ . n 
J 2 94  TYR 94  94  94  TYR TYR JJJ . n 
J 2 95  PHE 95  95  95  PHE PHE JJJ . n 
J 2 96  CYS 96  96  96  CYS CYS JJJ . n 
J 2 97  ALA 97  97  97  ALA ALA JJJ . n 
J 2 98  ALA 98  98  98  ALA ALA JJJ . n 
J 2 99  ASP 99  99  99  ASP ASP JJJ . n 
J 2 100 ARG 100 100 100 ARG ARG JJJ . n 
J 2 101 GLY 101 101 101 GLY GLY JJJ . n 
J 2 102 GLU 102 102 102 GLU GLU JJJ . n 
J 2 103 SER 103 103 103 SER SER JJJ . n 
J 2 104 TYR 104 104 104 TYR TYR JJJ . n 
J 2 105 TYR 105 105 105 TYR TYR JJJ . n 
J 2 106 TYR 106 106 106 TYR TYR JJJ . n 
J 2 107 THR 107 107 107 THR THR JJJ . n 
J 2 108 ARG 108 108 108 ARG ARG JJJ . n 
J 2 109 PRO 109 109 109 PRO PRO JJJ . n 
J 2 110 THR 110 110 110 THR THR JJJ . n 
J 2 111 GLU 111 111 111 GLU GLU JJJ . n 
J 2 112 TYR 112 112 112 TYR TYR JJJ . n 
J 2 113 GLU 113 113 113 GLU GLU JJJ . n 
J 2 114 PHE 114 114 114 PHE PHE JJJ . n 
J 2 115 TRP 115 115 115 TRP TRP JJJ . n 
J 2 116 GLY 116 116 116 GLY GLY JJJ . n 
J 2 117 GLN 117 117 117 GLN GLN JJJ . n 
J 2 118 GLY 118 118 118 GLY GLY JJJ . n 
J 2 119 THR 119 119 119 THR THR JJJ . n 
J 2 120 GLN 120 120 120 GLN GLN JJJ . n 
J 2 121 VAL 121 121 121 VAL VAL JJJ . n 
J 2 122 THR 122 122 122 THR THR JJJ . n 
J 2 123 VAL 123 123 123 VAL VAL JJJ . n 
J 2 124 SER 124 124 124 SER SER JJJ . n 
J 2 125 SER 125 125 125 SER SER JJJ . n 
J 2 126 LYS 126 126 ?   ?   ?   JJJ . n 
J 2 127 HIS 127 127 ?   ?   ?   JJJ . n 
J 2 128 HIS 128 128 ?   ?   ?   JJJ . n 
J 2 129 HIS 129 129 ?   ?   ?   JJJ . n 
J 2 130 HIS 130 130 ?   ?   ?   JJJ . n 
J 2 131 HIS 131 131 ?   ?   ?   JJJ . n 
J 2 132 HIS 132 132 ?   ?   ?   JJJ . n 
K 1 1   PRO 1   330 ?   ?   ?   KKK . n 
K 1 2   ASN 2   331 ?   ?   ?   KKK . n 
K 1 3   ILE 3   332 332 ILE ILE KKK . n 
K 1 4   THR 4   333 333 THR THR KKK . n 
K 1 5   ASN 5   334 334 ASN ASN KKK . n 
K 1 6   LEU 6   335 335 LEU LEU KKK . n 
K 1 7   CYS 7   336 336 CYS CYS KKK . n 
K 1 8   PRO 8   337 337 PRO PRO KKK . n 
K 1 9   PHE 9   338 338 PHE PHE KKK . n 
K 1 10  GLY 10  339 339 GLY GLY KKK . n 
K 1 11  GLU 11  340 340 GLU GLU KKK . n 
K 1 12  VAL 12  341 341 VAL VAL KKK . n 
K 1 13  PHE 13  342 342 PHE PHE KKK . n 
K 1 14  ASN 14  343 343 ASN ASN KKK . n 
K 1 15  ALA 15  344 344 ALA ALA KKK . n 
K 1 16  THR 16  345 345 THR THR KKK . n 
K 1 17  ARG 17  346 346 ARG ARG KKK . n 
K 1 18  PHE 18  347 347 PHE PHE KKK . n 
K 1 19  ALA 19  348 348 ALA ALA KKK . n 
K 1 20  SER 20  349 349 SER SER KKK . n 
K 1 21  VAL 21  350 350 VAL VAL KKK . n 
K 1 22  TYR 22  351 351 TYR TYR KKK . n 
K 1 23  ALA 23  352 352 ALA ALA KKK . n 
K 1 24  TRP 24  353 353 TRP TRP KKK . n 
K 1 25  ASN 25  354 354 ASN ASN KKK . n 
K 1 26  ARG 26  355 355 ARG ARG KKK . n 
K 1 27  LYS 27  356 356 LYS LYS KKK . n 
K 1 28  ARG 28  357 357 ARG ARG KKK . n 
K 1 29  ILE 29  358 358 ILE ILE KKK . n 
K 1 30  SER 30  359 359 SER SER KKK . n 
K 1 31  ASN 31  360 360 ASN ASN KKK . n 
K 1 32  CYS 32  361 361 CYS CYS KKK . n 
K 1 33  VAL 33  362 362 VAL VAL KKK . n 
K 1 34  ALA 34  363 363 ALA ALA KKK . n 
K 1 35  ASP 35  364 364 ASP ASP KKK . n 
K 1 36  TYR 36  365 365 TYR TYR KKK . n 
K 1 37  SER 37  366 366 SER SER KKK . n 
K 1 38  VAL 38  367 367 VAL VAL KKK . n 
K 1 39  LEU 39  368 368 LEU LEU KKK . n 
K 1 40  TYR 40  369 369 TYR TYR KKK . n 
K 1 41  ASN 41  370 370 ASN ASN KKK . n 
K 1 42  SER 42  371 371 SER SER KKK . n 
K 1 43  ALA 43  372 372 ALA ALA KKK . n 
K 1 44  SER 44  373 373 SER SER KKK . n 
K 1 45  PHE 45  374 374 PHE PHE KKK . n 
K 1 46  SER 46  375 375 SER SER KKK . n 
K 1 47  THR 47  376 376 THR THR KKK . n 
K 1 48  PHE 48  377 377 PHE PHE KKK . n 
K 1 49  LYS 49  378 378 LYS LYS KKK . n 
K 1 50  CYS 50  379 379 CYS CYS KKK . n 
K 1 51  TYR 51  380 380 TYR TYR KKK . n 
K 1 52  GLY 52  381 381 GLY GLY KKK . n 
K 1 53  VAL 53  382 382 VAL VAL KKK . n 
K 1 54  SER 54  383 383 SER SER KKK . n 
K 1 55  PRO 55  384 384 PRO PRO KKK . n 
K 1 56  THR 56  385 385 THR THR KKK . n 
K 1 57  LYS 57  386 386 LYS LYS KKK . n 
K 1 58  LEU 58  387 387 LEU LEU KKK . n 
K 1 59  ASN 59  388 388 ASN ASN KKK . n 
K 1 60  ASP 60  389 389 ASP ASP KKK . n 
K 1 61  LEU 61  390 390 LEU LEU KKK . n 
K 1 62  CYS 62  391 391 CYS CYS KKK . n 
K 1 63  PHE 63  392 392 PHE PHE KKK . n 
K 1 64  THR 64  393 393 THR THR KKK . n 
K 1 65  ASN 65  394 394 ASN ASN KKK . n 
K 1 66  VAL 66  395 395 VAL VAL KKK . n 
K 1 67  TYR 67  396 396 TYR TYR KKK . n 
K 1 68  ALA 68  397 397 ALA ALA KKK . n 
K 1 69  ASP 69  398 398 ASP ASP KKK . n 
K 1 70  SER 70  399 399 SER SER KKK . n 
K 1 71  PHE 71  400 400 PHE PHE KKK . n 
K 1 72  VAL 72  401 401 VAL VAL KKK . n 
K 1 73  ILE 73  402 402 ILE ILE KKK . n 
K 1 74  ARG 74  403 403 ARG ARG KKK . n 
K 1 75  GLY 75  404 404 GLY GLY KKK . n 
K 1 76  ASP 76  405 405 ASP ASP KKK . n 
K 1 77  GLU 77  406 406 GLU GLU KKK . n 
K 1 78  VAL 78  407 407 VAL VAL KKK . n 
K 1 79  ARG 79  408 408 ARG ARG KKK . n 
K 1 80  GLN 80  409 409 GLN GLN KKK . n 
K 1 81  ILE 81  410 410 ILE ILE KKK . n 
K 1 82  ALA 82  411 411 ALA ALA KKK . n 
K 1 83  PRO 83  412 412 PRO PRO KKK . n 
K 1 84  GLY 84  413 413 GLY GLY KKK . n 
K 1 85  GLN 85  414 414 GLN GLN KKK . n 
K 1 86  THR 86  415 415 THR THR KKK . n 
K 1 87  GLY 87  416 416 GLY GLY KKK . n 
K 1 88  LYS 88  417 417 LYS LYS KKK . n 
K 1 89  ILE 89  418 418 ILE ILE KKK . n 
K 1 90  ALA 90  419 419 ALA ALA KKK . n 
K 1 91  ASP 91  420 420 ASP ASP KKK . n 
K 1 92  TYR 92  421 421 TYR TYR KKK . n 
K 1 93  ASN 93  422 422 ASN ASN KKK . n 
K 1 94  TYR 94  423 423 TYR TYR KKK . n 
K 1 95  LYS 95  424 424 LYS LYS KKK . n 
K 1 96  LEU 96  425 425 LEU LEU KKK . n 
K 1 97  PRO 97  426 426 PRO PRO KKK . n 
K 1 98  ASP 98  427 427 ASP ASP KKK . n 
K 1 99  ASP 99  428 428 ASP ASP KKK . n 
K 1 100 PHE 100 429 429 PHE PHE KKK . n 
K 1 101 THR 101 430 430 THR THR KKK . n 
K 1 102 GLY 102 431 431 GLY GLY KKK . n 
K 1 103 CYS 103 432 432 CYS CYS KKK . n 
K 1 104 VAL 104 433 433 VAL VAL KKK . n 
K 1 105 ILE 105 434 434 ILE ILE KKK . n 
K 1 106 ALA 106 435 435 ALA ALA KKK . n 
K 1 107 TRP 107 436 436 TRP TRP KKK . n 
K 1 108 ASN 108 437 437 ASN ASN KKK . n 
K 1 109 SER 109 438 438 SER SER KKK . n 
K 1 110 ASN 110 439 439 ASN ASN KKK . n 
K 1 111 ASN 111 440 440 ASN ASN KKK . n 
K 1 112 LEU 112 441 441 LEU LEU KKK . n 
K 1 113 ASP 113 442 442 ASP ASP KKK . n 
K 1 114 SER 114 443 443 SER SER KKK . n 
K 1 115 LYS 115 444 444 LYS LYS KKK . n 
K 1 116 VAL 116 445 445 VAL VAL KKK . n 
K 1 117 GLY 117 446 446 GLY GLY KKK . n 
K 1 118 GLY 118 447 447 GLY GLY KKK . n 
K 1 119 ASN 119 448 448 ASN ASN KKK . n 
K 1 120 TYR 120 449 449 TYR TYR KKK . n 
K 1 121 ASN 121 450 450 ASN ASN KKK . n 
K 1 122 TYR 122 451 451 TYR TYR KKK . n 
K 1 123 LEU 123 452 452 LEU LEU KKK . n 
K 1 124 TYR 124 453 453 TYR TYR KKK . n 
K 1 125 ARG 125 454 454 ARG ARG KKK . n 
K 1 126 LEU 126 455 455 LEU LEU KKK . n 
K 1 127 PHE 127 456 456 PHE PHE KKK . n 
K 1 128 ARG 128 457 457 ARG ARG KKK . n 
K 1 129 LYS 129 458 458 LYS LYS KKK . n 
K 1 130 SER 130 459 459 SER SER KKK . n 
K 1 131 ASN 131 460 460 ASN ASN KKK . n 
K 1 132 LEU 132 461 461 LEU LEU KKK . n 
K 1 133 LYS 133 462 462 LYS LYS KKK . n 
K 1 134 PRO 134 463 463 PRO PRO KKK . n 
K 1 135 PHE 135 464 464 PHE PHE KKK . n 
K 1 136 GLU 136 465 465 GLU GLU KKK . n 
K 1 137 ARG 137 466 466 ARG ARG KKK . n 
K 1 138 ASP 138 467 467 ASP ASP KKK . n 
K 1 139 ILE 139 468 468 ILE ILE KKK . n 
K 1 140 SER 140 469 469 SER SER KKK . n 
K 1 141 THR 141 470 470 THR THR KKK . n 
K 1 142 GLU 142 471 471 GLU GLU KKK . n 
K 1 143 ILE 143 472 472 ILE ILE KKK . n 
K 1 144 TYR 144 473 473 TYR TYR KKK . n 
K 1 145 GLN 145 474 474 GLN GLN KKK . n 
K 1 146 ALA 146 475 475 ALA ALA KKK . n 
K 1 147 GLY 147 476 476 GLY GLY KKK . n 
K 1 148 SER 148 477 477 SER SER KKK . n 
K 1 149 THR 149 478 478 THR THR KKK . n 
K 1 150 PRO 150 479 479 PRO PRO KKK . n 
K 1 151 CYS 151 480 480 CYS CYS KKK . n 
K 1 152 ASN 152 481 481 ASN ASN KKK . n 
K 1 153 GLY 153 482 482 GLY GLY KKK . n 
K 1 154 VAL 154 483 483 VAL VAL KKK . n 
K 1 155 GLU 155 484 484 GLU GLU KKK . n 
K 1 156 GLY 156 485 485 GLY GLY KKK . n 
K 1 157 PHE 157 486 486 PHE PHE KKK . n 
K 1 158 ASN 158 487 487 ASN ASN KKK . n 
K 1 159 CYS 159 488 488 CYS CYS KKK . n 
K 1 160 TYR 160 489 489 TYR TYR KKK . n 
K 1 161 PHE 161 490 490 PHE PHE KKK . n 
K 1 162 PRO 162 491 491 PRO PRO KKK . n 
K 1 163 LEU 163 492 492 LEU LEU KKK . n 
K 1 164 GLN 164 493 493 GLN GLN KKK . n 
K 1 165 SER 165 494 494 SER SER KKK . n 
K 1 166 TYR 166 495 495 TYR TYR KKK . n 
K 1 167 GLY 167 496 496 GLY GLY KKK . n 
K 1 168 PHE 168 497 497 PHE PHE KKK . n 
K 1 169 GLN 169 498 498 GLN GLN KKK . n 
K 1 170 PRO 170 499 499 PRO PRO KKK . n 
K 1 171 THR 171 500 500 THR THR KKK . n 
K 1 172 ASN 172 501 501 ASN ASN KKK . n 
K 1 173 GLY 173 502 502 GLY GLY KKK . n 
K 1 174 VAL 174 503 503 VAL VAL KKK . n 
K 1 175 GLY 175 504 504 GLY GLY KKK . n 
K 1 176 TYR 176 505 505 TYR TYR KKK . n 
K 1 177 GLN 177 506 506 GLN GLN KKK . n 
K 1 178 PRO 178 507 507 PRO PRO KKK . n 
K 1 179 TYR 179 508 508 TYR TYR KKK . n 
K 1 180 ARG 180 509 509 ARG ARG KKK . n 
K 1 181 VAL 181 510 510 VAL VAL KKK . n 
K 1 182 VAL 182 511 511 VAL VAL KKK . n 
K 1 183 VAL 183 512 512 VAL VAL KKK . n 
K 1 184 LEU 184 513 513 LEU LEU KKK . n 
K 1 185 SER 185 514 514 SER SER KKK . n 
K 1 186 PHE 186 515 515 PHE PHE KKK . n 
K 1 187 GLU 187 516 516 GLU GLU KKK . n 
K 1 188 LEU 188 517 517 LEU LEU KKK . n 
K 1 189 LEU 189 518 518 LEU LEU KKK . n 
K 1 190 HIS 190 519 519 HIS HIS KKK . n 
K 1 191 ALA 191 520 520 ALA ALA KKK . n 
K 1 192 PRO 192 521 521 PRO PRO KKK . n 
K 1 193 ALA 193 522 522 ALA ALA KKK . n 
K 1 194 THR 194 523 523 THR THR KKK . n 
K 1 195 VAL 195 524 524 VAL VAL KKK . n 
K 1 196 CYS 196 525 525 CYS CYS KKK . n 
K 1 197 GLY 197 526 526 GLY GLY KKK . n 
K 1 198 PRO 198 527 527 PRO PRO KKK . n 
K 1 199 LYS 199 528 528 LYS LYS KKK . n 
K 1 200 LYS 200 529 ?   ?   ?   KKK . n 
K 1 201 SER 201 530 ?   ?   ?   KKK . n 
K 1 202 THR 202 531 ?   ?   ?   KKK . n 
K 1 203 ASN 203 532 ?   ?   ?   KKK . n 
K 1 204 LYS 204 533 ?   ?   ?   KKK . n 
K 1 205 HIS 205 534 ?   ?   ?   KKK . n 
K 1 206 HIS 206 535 ?   ?   ?   KKK . n 
K 1 207 HIS 207 536 ?   ?   ?   KKK . n 
K 1 208 HIS 208 537 ?   ?   ?   KKK . n 
K 1 209 HIS 209 538 ?   ?   ?   KKK . n 
K 1 210 HIS 210 539 ?   ?   ?   KKK . n 
L 2 1   GLN 1   1   1   GLN GLN LLL . n 
L 2 2   VAL 2   2   2   VAL VAL LLL . n 
L 2 3   GLN 3   3   3   GLN GLN LLL . n 
L 2 4   LEU 4   4   4   LEU LEU LLL . n 
L 2 5   VAL 5   5   5   VAL VAL LLL . n 
L 2 6   GLU 6   6   6   GLU GLU LLL . n 
L 2 7   SER 7   7   7   SER SER LLL . n 
L 2 8   GLY 8   8   8   GLY GLY LLL . n 
L 2 9   GLY 9   9   9   GLY GLY LLL . n 
L 2 10  GLY 10  10  10  GLY GLY LLL . n 
L 2 11  LEU 11  11  11  LEU LEU LLL . n 
L 2 12  VAL 12  12  12  VAL VAL LLL . n 
L 2 13  GLN 13  13  13  GLN GLN LLL . n 
L 2 14  ALA 14  14  14  ALA ALA LLL . n 
L 2 15  GLY 15  15  15  GLY GLY LLL . n 
L 2 16  GLY 16  16  16  GLY GLY LLL . n 
L 2 17  SER 17  17  17  SER SER LLL . n 
L 2 18  LEU 18  18  18  LEU LEU LLL . n 
L 2 19  ARG 19  19  19  ARG ARG LLL . n 
L 2 20  LEU 20  20  20  LEU LEU LLL . n 
L 2 21  ALA 21  21  21  ALA ALA LLL . n 
L 2 22  CYS 22  22  22  CYS CYS LLL . n 
L 2 23  ILE 23  23  23  ILE ILE LLL . n 
L 2 24  ALA 24  24  24  ALA ALA LLL . n 
L 2 25  SER 25  25  25  SER SER LLL . n 
L 2 26  GLY 26  26  26  GLY GLY LLL . n 
L 2 27  ARG 27  27  27  ARG ARG LLL . n 
L 2 28  THR 28  28  28  THR THR LLL . n 
L 2 29  PHE 29  29  29  PHE PHE LLL . n 
L 2 30  HIS 30  30  30  HIS HIS LLL . n 
L 2 31  SER 31  31  31  SER SER LLL . n 
L 2 32  TYR 32  32  32  TYR TYR LLL . n 
L 2 33  VAL 33  33  33  VAL VAL LLL . n 
L 2 34  MET 34  34  34  MET MET LLL . n 
L 2 35  ALA 35  35  35  ALA ALA LLL . n 
L 2 36  TRP 36  36  36  TRP TRP LLL . n 
L 2 37  PHE 37  37  37  PHE PHE LLL . n 
L 2 38  ARG 38  38  38  ARG ARG LLL . n 
L 2 39  GLN 39  39  39  GLN GLN LLL . n 
L 2 40  ALA 40  40  40  ALA ALA LLL . n 
L 2 41  PRO 41  41  41  PRO PRO LLL . n 
L 2 42  GLY 42  42  42  GLY GLY LLL . n 
L 2 43  LYS 43  43  43  LYS LYS LLL . n 
L 2 44  GLU 44  44  44  GLU GLU LLL . n 
L 2 45  ARG 45  45  45  ARG ARG LLL . n 
L 2 46  GLU 46  46  46  GLU GLU LLL . n 
L 2 47  PHE 47  47  47  PHE PHE LLL . n 
L 2 48  VAL 48  48  48  VAL VAL LLL . n 
L 2 49  ALA 49  49  49  ALA ALA LLL . n 
L 2 50  ALA 50  50  50  ALA ALA LLL . n 
L 2 51  ILE 51  51  51  ILE ILE LLL . n 
L 2 52  SER 52  52  52  SER SER LLL . n 
L 2 53  TRP 53  53  53  TRP TRP LLL . n 
L 2 54  SER 54  54  54  SER SER LLL . n 
L 2 55  SER 55  55  55  SER SER LLL . n 
L 2 56  THR 56  56  56  THR THR LLL . n 
L 2 57  PRO 57  57  57  PRO PRO LLL . n 
L 2 58  THR 58  58  58  THR THR LLL . n 
L 2 59  TYR 59  59  59  TYR TYR LLL . n 
L 2 60  TYR 60  60  60  TYR TYR LLL . n 
L 2 61  GLY 61  61  61  GLY GLY LLL . n 
L 2 62  GLU 62  62  62  GLU GLU LLL . n 
L 2 63  SER 63  63  63  SER SER LLL . n 
L 2 64  VAL 64  64  64  VAL VAL LLL . n 
L 2 65  LYS 65  65  65  LYS LYS LLL . n 
L 2 66  GLY 66  66  66  GLY GLY LLL . n 
L 2 67  ARG 67  67  67  ARG ARG LLL . n 
L 2 68  PHE 68  68  68  PHE PHE LLL . n 
L 2 69  THR 69  69  69  THR THR LLL . n 
L 2 70  ILE 70  70  70  ILE ILE LLL . n 
L 2 71  SER 71  71  71  SER SER LLL . n 
L 2 72  ARG 72  72  72  ARG ARG LLL . n 
L 2 73  ASP 73  73  73  ASP ASP LLL . n 
L 2 74  ASN 74  74  74  ASN ASN LLL . n 
L 2 75  ALA 75  75  75  ALA ALA LLL . n 
L 2 76  LYS 76  76  76  LYS LYS LLL . n 
L 2 77  ASN 77  77  77  ASN ASN LLL . n 
L 2 78  THR 78  78  78  THR THR LLL . n 
L 2 79  VAL 79  79  79  VAL VAL LLL . n 
L 2 80  TYR 80  80  80  TYR TYR LLL . n 
L 2 81  LEU 81  81  81  LEU LEU LLL . n 
L 2 82  GLN 82  82  82  GLN GLN LLL . n 
L 2 83  MET 83  83  83  MET MET LLL . n 
L 2 84  ASN 84  84  84  ASN ASN LLL . n 
L 2 85  ARG 85  85  85  ARG ARG LLL . n 
L 2 86  LEU 86  86  86  LEU LEU LLL . n 
L 2 87  LYS 87  87  87  LYS LYS LLL . n 
L 2 88  PRO 88  88  88  PRO PRO LLL . n 
L 2 89  GLU 89  89  89  GLU GLU LLL . n 
L 2 90  ASP 90  90  90  ASP ASP LLL . n 
L 2 91  THR 91  91  91  THR THR LLL . n 
L 2 92  ALA 92  92  92  ALA ALA LLL . n 
L 2 93  VAL 93  93  93  VAL VAL LLL . n 
L 2 94  TYR 94  94  94  TYR TYR LLL . n 
L 2 95  PHE 95  95  95  PHE PHE LLL . n 
L 2 96  CYS 96  96  96  CYS CYS LLL . n 
L 2 97  ALA 97  97  97  ALA ALA LLL . n 
L 2 98  ALA 98  98  98  ALA ALA LLL . n 
L 2 99  ASP 99  99  99  ASP ASP LLL . n 
L 2 100 ARG 100 100 100 ARG ARG LLL . n 
L 2 101 GLY 101 101 101 GLY GLY LLL . n 
L 2 102 GLU 102 102 102 GLU GLU LLL . n 
L 2 103 SER 103 103 103 SER SER LLL . n 
L 2 104 TYR 104 104 104 TYR TYR LLL . n 
L 2 105 TYR 105 105 105 TYR TYR LLL . n 
L 2 106 TYR 106 106 106 TYR TYR LLL . n 
L 2 107 THR 107 107 107 THR THR LLL . n 
L 2 108 ARG 108 108 108 ARG ARG LLL . n 
L 2 109 PRO 109 109 109 PRO PRO LLL . n 
L 2 110 THR 110 110 110 THR THR LLL . n 
L 2 111 GLU 111 111 111 GLU GLU LLL . n 
L 2 112 TYR 112 112 112 TYR TYR LLL . n 
L 2 113 GLU 113 113 113 GLU GLU LLL . n 
L 2 114 PHE 114 114 114 PHE PHE LLL . n 
L 2 115 TRP 115 115 115 TRP TRP LLL . n 
L 2 116 GLY 116 116 116 GLY GLY LLL . n 
L 2 117 GLN 117 117 117 GLN GLN LLL . n 
L 2 118 GLY 118 118 118 GLY GLY LLL . n 
L 2 119 THR 119 119 119 THR THR LLL . n 
L 2 120 GLN 120 120 120 GLN GLN LLL . n 
L 2 121 VAL 121 121 121 VAL VAL LLL . n 
L 2 122 THR 122 122 122 THR THR LLL . n 
L 2 123 VAL 123 123 123 VAL VAL LLL . n 
L 2 124 SER 124 124 124 SER SER LLL . n 
L 2 125 SER 125 125 125 SER SER LLL . n 
L 2 126 LYS 126 126 ?   ?   ?   LLL . n 
L 2 127 HIS 127 127 ?   ?   ?   LLL . n 
L 2 128 HIS 128 128 ?   ?   ?   LLL . n 
L 2 129 HIS 129 129 ?   ?   ?   LLL . n 
L 2 130 HIS 130 130 ?   ?   ?   LLL . n 
L 2 131 HIS 131 131 ?   ?   ?   LLL . n 
L 2 132 HIS 132 132 ?   ?   ?   LLL . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  3 NAG 1  601 601 NAG NAG AAA . 
N  3 NAG 1  601 528 NAG NAG CCC . 
O  3 NAG 1  601 601 NAG NAG EEE . 
P  3 NAG 1  601 529 NAG NAG GGG . 
Q  3 NAG 1  601 601 NAG NAG III . 
R  3 NAG 1  601 529 NAG NAG KKK . 
S  4 HOH 1  701 21  HOH HOH AAA . 
S  4 HOH 2  702 105 HOH HOH AAA . 
S  4 HOH 3  703 250 HOH HOH AAA . 
S  4 HOH 4  704 289 HOH HOH AAA . 
S  4 HOH 5  705 108 HOH HOH AAA . 
S  4 HOH 6  706 296 HOH HOH AAA . 
S  4 HOH 7  707 142 HOH HOH AAA . 
S  4 HOH 8  708 324 HOH HOH AAA . 
S  4 HOH 9  709 136 HOH HOH AAA . 
S  4 HOH 10 710 152 HOH HOH AAA . 
S  4 HOH 11 711 235 HOH HOH AAA . 
S  4 HOH 12 712 78  HOH HOH AAA . 
S  4 HOH 13 713 53  HOH HOH AAA . 
S  4 HOH 14 714 145 HOH HOH AAA . 
S  4 HOH 15 715 320 HOH HOH AAA . 
S  4 HOH 16 716 319 HOH HOH AAA . 
S  4 HOH 17 717 64  HOH HOH AAA . 
S  4 HOH 18 718 83  HOH HOH AAA . 
S  4 HOH 19 719 42  HOH HOH AAA . 
S  4 HOH 20 720 262 HOH HOH AAA . 
S  4 HOH 21 721 195 HOH HOH AAA . 
S  4 HOH 22 722 11  HOH HOH AAA . 
S  4 HOH 23 723 172 HOH HOH AAA . 
S  4 HOH 24 724 99  HOH HOH AAA . 
S  4 HOH 25 725 189 HOH HOH AAA . 
S  4 HOH 26 726 4   HOH HOH AAA . 
S  4 HOH 27 727 32  HOH HOH AAA . 
S  4 HOH 28 728 12  HOH HOH AAA . 
S  4 HOH 29 729 19  HOH HOH AAA . 
S  4 HOH 30 730 93  HOH HOH AAA . 
S  4 HOH 31 731 281 HOH HOH AAA . 
S  4 HOH 32 732 77  HOH HOH AAA . 
S  4 HOH 33 733 282 HOH HOH AAA . 
S  4 HOH 34 734 213 HOH HOH AAA . 
S  4 HOH 35 735 268 HOH HOH AAA . 
S  4 HOH 36 736 212 HOH HOH AAA . 
S  4 HOH 37 737 163 HOH HOH AAA . 
S  4 HOH 38 738 199 HOH HOH AAA . 
S  4 HOH 39 739 146 HOH HOH AAA . 
S  4 HOH 40 740 300 HOH HOH AAA . 
S  4 HOH 41 741 301 HOH HOH AAA . 
S  4 HOH 42 742 187 HOH HOH AAA . 
T  4 HOH 1  201 259 HOH HOH BBB . 
T  4 HOH 2  202 270 HOH HOH BBB . 
T  4 HOH 3  203 67  HOH HOH BBB . 
T  4 HOH 4  204 242 HOH HOH BBB . 
T  4 HOH 5  205 190 HOH HOH BBB . 
T  4 HOH 6  206 15  HOH HOH BBB . 
T  4 HOH 7  207 49  HOH HOH BBB . 
T  4 HOH 8  208 52  HOH HOH BBB . 
T  4 HOH 9  209 216 HOH HOH BBB . 
T  4 HOH 10 210 263 HOH HOH BBB . 
T  4 HOH 11 211 13  HOH HOH BBB . 
T  4 HOH 12 212 227 HOH HOH BBB . 
T  4 HOH 13 213 260 HOH HOH BBB . 
T  4 HOH 14 214 275 HOH HOH BBB . 
T  4 HOH 15 215 137 HOH HOH BBB . 
T  4 HOH 16 216 39  HOH HOH BBB . 
T  4 HOH 17 217 88  HOH HOH BBB . 
T  4 HOH 18 218 120 HOH HOH BBB . 
T  4 HOH 19 219 244 HOH HOH BBB . 
T  4 HOH 20 220 200 HOH HOH BBB . 
U  4 HOH 1  701 159 HOH HOH CCC . 
U  4 HOH 2  702 85  HOH HOH CCC . 
U  4 HOH 3  703 272 HOH HOH CCC . 
U  4 HOH 4  704 127 HOH HOH CCC . 
U  4 HOH 5  705 89  HOH HOH CCC . 
U  4 HOH 6  706 74  HOH HOH CCC . 
U  4 HOH 7  707 96  HOH HOH CCC . 
U  4 HOH 8  708 130 HOH HOH CCC . 
U  4 HOH 9  709 73  HOH HOH CCC . 
U  4 HOH 10 710 210 HOH HOH CCC . 
U  4 HOH 11 711 104 HOH HOH CCC . 
U  4 HOH 12 712 202 HOH HOH CCC . 
U  4 HOH 13 713 179 HOH HOH CCC . 
U  4 HOH 14 714 60  HOH HOH CCC . 
U  4 HOH 15 715 91  HOH HOH CCC . 
U  4 HOH 16 716 37  HOH HOH CCC . 
U  4 HOH 17 717 183 HOH HOH CCC . 
U  4 HOH 18 718 287 HOH HOH CCC . 
U  4 HOH 19 719 291 HOH HOH CCC . 
U  4 HOH 20 720 14  HOH HOH CCC . 
U  4 HOH 21 721 47  HOH HOH CCC . 
U  4 HOH 22 722 294 HOH HOH CCC . 
U  4 HOH 23 723 306 HOH HOH CCC . 
U  4 HOH 24 724 125 HOH HOH CCC . 
U  4 HOH 25 725 186 HOH HOH CCC . 
U  4 HOH 26 726 198 HOH HOH CCC . 
U  4 HOH 27 727 277 HOH HOH CCC . 
U  4 HOH 28 728 170 HOH HOH CCC . 
U  4 HOH 29 729 27  HOH HOH CCC . 
U  4 HOH 30 730 285 HOH HOH CCC . 
U  4 HOH 31 731 56  HOH HOH CCC . 
U  4 HOH 32 732 168 HOH HOH CCC . 
U  4 HOH 33 733 252 HOH HOH CCC . 
U  4 HOH 34 734 110 HOH HOH CCC . 
U  4 HOH 35 735 176 HOH HOH CCC . 
U  4 HOH 36 736 284 HOH HOH CCC . 
U  4 HOH 37 737 249 HOH HOH CCC . 
V  4 HOH 1  201 147 HOH HOH DDD . 
V  4 HOH 2  202 46  HOH HOH DDD . 
V  4 HOH 3  203 158 HOH HOH DDD . 
V  4 HOH 4  204 50  HOH HOH DDD . 
V  4 HOH 5  205 167 HOH HOH DDD . 
V  4 HOH 6  206 84  HOH HOH DDD . 
V  4 HOH 7  207 230 HOH HOH DDD . 
V  4 HOH 8  208 139 HOH HOH DDD . 
V  4 HOH 9  209 8   HOH HOH DDD . 
V  4 HOH 10 210 161 HOH HOH DDD . 
V  4 HOH 11 211 246 HOH HOH DDD . 
W  4 HOH 1  701 41  HOH HOH EEE . 
W  4 HOH 2  702 297 HOH HOH EEE . 
W  4 HOH 3  703 58  HOH HOH EEE . 
W  4 HOH 4  704 94  HOH HOH EEE . 
W  4 HOH 5  705 316 HOH HOH EEE . 
W  4 HOH 6  706 87  HOH HOH EEE . 
W  4 HOH 7  707 113 HOH HOH EEE . 
W  4 HOH 8  708 188 HOH HOH EEE . 
W  4 HOH 9  709 251 HOH HOH EEE . 
W  4 HOH 10 710 241 HOH HOH EEE . 
W  4 HOH 11 711 237 HOH HOH EEE . 
W  4 HOH 12 712 20  HOH HOH EEE . 
W  4 HOH 13 713 315 HOH HOH EEE . 
W  4 HOH 14 714 219 HOH HOH EEE . 
W  4 HOH 15 715 150 HOH HOH EEE . 
W  4 HOH 16 716 40  HOH HOH EEE . 
W  4 HOH 17 717 141 HOH HOH EEE . 
W  4 HOH 18 718 102 HOH HOH EEE . 
W  4 HOH 19 719 232 HOH HOH EEE . 
W  4 HOH 20 720 45  HOH HOH EEE . 
W  4 HOH 21 721 31  HOH HOH EEE . 
W  4 HOH 22 722 295 HOH HOH EEE . 
W  4 HOH 23 723 257 HOH HOH EEE . 
W  4 HOH 24 724 34  HOH HOH EEE . 
W  4 HOH 25 725 303 HOH HOH EEE . 
W  4 HOH 26 726 211 HOH HOH EEE . 
W  4 HOH 27 727 30  HOH HOH EEE . 
W  4 HOH 28 728 222 HOH HOH EEE . 
W  4 HOH 29 729 254 HOH HOH EEE . 
W  4 HOH 30 730 223 HOH HOH EEE . 
W  4 HOH 31 731 224 HOH HOH EEE . 
W  4 HOH 32 732 256 HOH HOH EEE . 
W  4 HOH 33 733 226 HOH HOH EEE . 
W  4 HOH 34 734 331 HOH HOH EEE . 
W  4 HOH 35 735 253 HOH HOH EEE . 
W  4 HOH 36 736 312 HOH HOH EEE . 
X  4 HOH 1  201 66  HOH HOH FFF . 
X  4 HOH 2  202 266 HOH HOH FFF . 
X  4 HOH 3  203 325 HOH HOH FFF . 
X  4 HOH 4  204 228 HOH HOH FFF . 
X  4 HOH 5  205 59  HOH HOH FFF . 
X  4 HOH 6  206 245 HOH HOH FFF . 
X  4 HOH 7  207 273 HOH HOH FFF . 
X  4 HOH 8  208 43  HOH HOH FFF . 
X  4 HOH 9  209 80  HOH HOH FFF . 
X  4 HOH 10 210 149 HOH HOH FFF . 
X  4 HOH 11 211 217 HOH HOH FFF . 
X  4 HOH 12 212 28  HOH HOH FFF . 
X  4 HOH 13 213 44  HOH HOH FFF . 
X  4 HOH 14 214 229 HOH HOH FFF . 
X  4 HOH 15 215 153 HOH HOH FFF . 
X  4 HOH 16 216 160 HOH HOH FFF . 
X  4 HOH 17 217 18  HOH HOH FFF . 
X  4 HOH 18 218 2   HOH HOH FFF . 
X  4 HOH 19 219 131 HOH HOH FFF . 
X  4 HOH 20 220 240 HOH HOH FFF . 
X  4 HOH 21 221 114 HOH HOH FFF . 
X  4 HOH 22 222 24  HOH HOH FFF . 
X  4 HOH 23 223 308 HOH HOH FFF . 
X  4 HOH 24 224 81  HOH HOH FFF . 
X  4 HOH 25 225 258 HOH HOH FFF . 
X  4 HOH 26 226 267 HOH HOH FFF . 
X  4 HOH 27 227 72  HOH HOH FFF . 
Y  4 HOH 1  701 218 HOH HOH GGG . 
Y  4 HOH 2  702 117 HOH HOH GGG . 
Y  4 HOH 3  703 132 HOH HOH GGG . 
Y  4 HOH 4  704 97  HOH HOH GGG . 
Y  4 HOH 5  705 119 HOH HOH GGG . 
Y  4 HOH 6  706 298 HOH HOH GGG . 
Y  4 HOH 7  707 327 HOH HOH GGG . 
Y  4 HOH 8  708 154 HOH HOH GGG . 
Y  4 HOH 9  709 225 HOH HOH GGG . 
Y  4 HOH 10 710 26  HOH HOH GGG . 
Y  4 HOH 11 711 321 HOH HOH GGG . 
Y  4 HOH 12 712 70  HOH HOH GGG . 
Y  4 HOH 13 713 193 HOH HOH GGG . 
Y  4 HOH 14 714 328 HOH HOH GGG . 
Y  4 HOH 15 715 209 HOH HOH GGG . 
Y  4 HOH 16 716 326 HOH HOH GGG . 
Y  4 HOH 17 717 322 HOH HOH GGG . 
Y  4 HOH 18 718 215 HOH HOH GGG . 
Y  4 HOH 19 719 103 HOH HOH GGG . 
Y  4 HOH 20 720 17  HOH HOH GGG . 
Y  4 HOH 21 721 323 HOH HOH GGG . 
Y  4 HOH 22 722 63  HOH HOH GGG . 
Y  4 HOH 23 723 36  HOH HOH GGG . 
Y  4 HOH 24 724 191 HOH HOH GGG . 
Y  4 HOH 25 725 255 HOH HOH GGG . 
Y  4 HOH 26 726 286 HOH HOH GGG . 
Y  4 HOH 27 727 48  HOH HOH GGG . 
Y  4 HOH 28 728 290 HOH HOH GGG . 
Y  4 HOH 29 729 313 HOH HOH GGG . 
Y  4 HOH 30 730 243 HOH HOH GGG . 
Y  4 HOH 31 731 135 HOH HOH GGG . 
Y  4 HOH 32 732 51  HOH HOH GGG . 
Y  4 HOH 33 733 169 HOH HOH GGG . 
Y  4 HOH 34 734 121 HOH HOH GGG . 
Y  4 HOH 35 735 62  HOH HOH GGG . 
Y  4 HOH 36 736 204 HOH HOH GGG . 
Y  4 HOH 37 737 239 HOH HOH GGG . 
Z  4 HOH 1  201 330 HOH HOH HHH . 
Z  4 HOH 2  202 248 HOH HOH HHH . 
Z  4 HOH 3  203 122 HOH HOH HHH . 
Z  4 HOH 4  204 35  HOH HOH HHH . 
Z  4 HOH 5  205 71  HOH HOH HHH . 
Z  4 HOH 6  206 164 HOH HOH HHH . 
Z  4 HOH 7  207 128 HOH HOH HHH . 
Z  4 HOH 8  208 134 HOH HOH HHH . 
Z  4 HOH 9  209 6   HOH HOH HHH . 
Z  4 HOH 10 210 299 HOH HOH HHH . 
Z  4 HOH 11 211 305 HOH HOH HHH . 
Z  4 HOH 12 212 302 HOH HOH HHH . 
Z  4 HOH 13 213 280 HOH HOH HHH . 
Z  4 HOH 14 214 214 HOH HOH HHH . 
Z  4 HOH 15 215 123 HOH HOH HHH . 
Z  4 HOH 16 216 309 HOH HOH HHH . 
AA 4 HOH 1  701 57  HOH HOH III . 
AA 4 HOH 2  702 318 HOH HOH III . 
AA 4 HOH 3  703 197 HOH HOH III . 
AA 4 HOH 4  704 234 HOH HOH III . 
AA 4 HOH 5  705 98  HOH HOH III . 
AA 4 HOH 6  706 126 HOH HOH III . 
AA 4 HOH 7  707 116 HOH HOH III . 
AA 4 HOH 8  708 101 HOH HOH III . 
AA 4 HOH 9  709 100 HOH HOH III . 
AA 4 HOH 10 710 165 HOH HOH III . 
AA 4 HOH 11 711 317 HOH HOH III . 
AA 4 HOH 12 712 65  HOH HOH III . 
AA 4 HOH 13 713 115 HOH HOH III . 
AA 4 HOH 14 714 185 HOH HOH III . 
AA 4 HOH 15 715 265 HOH HOH III . 
AA 4 HOH 16 716 311 HOH HOH III . 
BA 4 HOH 1  201 276 HOH HOH JJJ . 
BA 4 HOH 2  202 90  HOH HOH JJJ . 
BA 4 HOH 3  203 171 HOH HOH JJJ . 
BA 4 HOH 4  204 82  HOH HOH JJJ . 
BA 4 HOH 5  205 157 HOH HOH JJJ . 
BA 4 HOH 6  206 23  HOH HOH JJJ . 
BA 4 HOH 7  207 118 HOH HOH JJJ . 
BA 4 HOH 8  208 177 HOH HOH JJJ . 
BA 4 HOH 9  209 279 HOH HOH JJJ . 
BA 4 HOH 10 210 264 HOH HOH JJJ . 
BA 4 HOH 11 211 238 HOH HOH JJJ . 
BA 4 HOH 12 212 236 HOH HOH JJJ . 
BA 4 HOH 13 213 304 HOH HOH JJJ . 
BA 4 HOH 14 214 148 HOH HOH JJJ . 
BA 4 HOH 15 215 111 HOH HOH JJJ . 
CA 4 HOH 1  701 173 HOH HOH KKK . 
CA 4 HOH 2  702 55  HOH HOH KKK . 
CA 4 HOH 3  703 22  HOH HOH KKK . 
CA 4 HOH 4  704 274 HOH HOH KKK . 
CA 4 HOH 5  705 68  HOH HOH KKK . 
CA 4 HOH 6  706 307 HOH HOH KKK . 
CA 4 HOH 7  707 140 HOH HOH KKK . 
CA 4 HOH 8  708 76  HOH HOH KKK . 
CA 4 HOH 9  709 201 HOH HOH KKK . 
CA 4 HOH 10 710 33  HOH HOH KKK . 
CA 4 HOH 11 711 143 HOH HOH KKK . 
CA 4 HOH 12 712 314 HOH HOH KKK . 
CA 4 HOH 13 713 107 HOH HOH KKK . 
CA 4 HOH 14 714 207 HOH HOH KKK . 
CA 4 HOH 15 715 95  HOH HOH KKK . 
CA 4 HOH 16 716 133 HOH HOH KKK . 
CA 4 HOH 17 717 233 HOH HOH KKK . 
CA 4 HOH 18 718 194 HOH HOH KKK . 
CA 4 HOH 19 719 292 HOH HOH KKK . 
CA 4 HOH 20 720 208 HOH HOH KKK . 
CA 4 HOH 21 721 178 HOH HOH KKK . 
CA 4 HOH 22 722 112 HOH HOH KKK . 
CA 4 HOH 23 723 106 HOH HOH KKK . 
CA 4 HOH 24 724 7   HOH HOH KKK . 
CA 4 HOH 25 725 221 HOH HOH KKK . 
CA 4 HOH 26 726 247 HOH HOH KKK . 
CA 4 HOH 27 727 206 HOH HOH KKK . 
CA 4 HOH 28 728 166 HOH HOH KKK . 
CA 4 HOH 29 729 129 HOH HOH KKK . 
CA 4 HOH 30 730 162 HOH HOH KKK . 
CA 4 HOH 31 731 5   HOH HOH KKK . 
CA 4 HOH 32 732 203 HOH HOH KKK . 
CA 4 HOH 33 733 293 HOH HOH KKK . 
CA 4 HOH 34 734 205 HOH HOH KKK . 
CA 4 HOH 35 735 151 HOH HOH KKK . 
CA 4 HOH 36 736 283 HOH HOH KKK . 
CA 4 HOH 37 737 156 HOH HOH KKK . 
CA 4 HOH 38 738 184 HOH HOH KKK . 
CA 4 HOH 39 739 278 HOH HOH KKK . 
DA 4 HOH 1  201 138 HOH HOH LLL . 
DA 4 HOH 2  202 182 HOH HOH LLL . 
DA 4 HOH 3  203 75  HOH HOH LLL . 
DA 4 HOH 4  204 29  HOH HOH LLL . 
DA 4 HOH 5  205 16  HOH HOH LLL . 
DA 4 HOH 6  206 54  HOH HOH LLL . 
DA 4 HOH 7  207 144 HOH HOH LLL . 
DA 4 HOH 8  208 38  HOH HOH LLL . 
DA 4 HOH 9  209 192 HOH HOH LLL . 
DA 4 HOH 10 210 220 HOH HOH LLL . 
DA 4 HOH 11 211 61  HOH HOH LLL . 
DA 4 HOH 12 212 9   HOH HOH LLL . 
DA 4 HOH 13 213 174 HOH HOH LLL . 
DA 4 HOH 14 214 69  HOH HOH LLL . 
DA 4 HOH 15 215 261 HOH HOH LLL . 
DA 4 HOH 16 216 231 HOH HOH LLL . 
DA 4 HOH 17 217 3   HOH HOH LLL . 
DA 4 HOH 18 218 25  HOH HOH LLL . 
DA 4 HOH 19 219 79  HOH HOH LLL . 
DA 4 HOH 20 220 269 HOH HOH LLL . 
DA 4 HOH 21 221 109 HOH HOH LLL . 
DA 4 HOH 22 222 155 HOH HOH LLL . 
DA 4 HOH 23 223 181 HOH HOH LLL . 
DA 4 HOH 24 224 124 HOH HOH LLL . 
DA 4 HOH 25 225 196 HOH HOH LLL . 
DA 4 HOH 26 226 175 HOH HOH LLL . 
DA 4 HOH 27 227 329 HOH HOH LLL . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
3 author_defined_assembly ? dimeric 2 
4 author_defined_assembly ? dimeric 2 
5 author_defined_assembly ? dimeric 2 
6 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,M,S,T   
2 1 C,D,N,U,V   
3 1 E,F,O,W,X   
4 1 G,H,P,Y,Z   
5 1 I,J,Q,AA,BA 
6 1 K,L,R,CA,DA 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2021-08-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 21.8030  -15.1950 -9.2980  0.1651 ? -0.0818 ? 0.0324  ? 0.1117 ? 0.0106  ? 0.1131 ? 5.7589  ? 
-0.1554 ? -2.6976 ? 0.9922  ? -1.2862 ? 3.4005  ? 0.0344  ? 0.1764  ? -0.2863 ? -0.2131 ? -0.0128 ? 0.0313  ? 0.1945  ? -0.0766 ? 
-0.0216 ? 
2  'X-RAY DIFFRACTION' ? refined 30.6680  -6.4940  -0.8750  0.0776 ? -0.0693 ? 0.0005  ? 0.1006 ? -0.0085 ? 0.0647 ? 3.6486  ? 
0.3751  ? -0.9404 ? 8.8785  ? -0.9922 ? 7.3282  ? 0.1420  ? 0.1363  ? 0.0495  ? -0.1399 ? -0.0386 ? -0.0549 ? -0.4119 ? 0.3818  ? 
-0.1035 ? 
3  'X-RAY DIFFRACTION' ? refined 15.7470  -16.1660 2.2420   0.0980 ? -0.0806 ? -0.0119 ? 0.1240 ? 0.0462  ? 0.0630 ? 2.0616  ? 
-0.2789 ? 0.0418  ? 2.1222  ? -0.3470 ? 2.6050  ? 0.0781  ? -0.1731 ? -0.0886 ? 0.0410  ? 0.1132  ? 0.3048  ? 0.1194  ? -0.4398 ? 
-0.1914 ? 
4  'X-RAY DIFFRACTION' ? refined 42.9120  -12.8840 16.6320  0.0412 ? -0.0298 ? -0.0108 ? 0.2020 ? -0.0789 ? 0.1133 ? 3.3467  ? 
1.0603  ? -0.2312 ? 3.7894  ? -0.0838 ? 4.4657  ? 0.0057  ? -0.1308 ? 0.2497  ? 0.1707  ? 0.0280  ? -0.2634 ? -0.2259 ? 0.6423  ? 
-0.0337 ? 
5  'X-RAY DIFFRACTION' ? refined 52.9840  -7.2530  11.3660  0.1460 ? -0.0665 ? 0.0478  ? 0.3918 ? -0.0463 ? 0.3531 ? 8.0822  ? 
3.3806  ? -1.5438 ? 8.8855  ? 3.1720  ? 2.2656  ? 0.2690  ? -0.0048 ? 0.1870  ? -0.6290 ? -0.0860 ? -0.3943 ? -0.4102 ? -0.1029 ? 
-0.1829 ? 
6  'X-RAY DIFFRACTION' ? refined 45.6640  -12.8760 15.8850  0.0991 ? -0.0452 ? 0.0108  ? 0.3143 ? -0.1095 ? 0.1665 ? 1.8062  ? 
0.0076  ? 0.3313  ? 0.7345  ? -0.4613 ? 3.9140  ? -0.0693 ? -0.1789 ? 0.2295  ? 0.0159  ? 0.0729  ? -0.2771 ? -0.1915 ? 0.9282  ? 
-0.0036 ? 
7  'X-RAY DIFFRACTION' ? refined 38.2640  -7.8010  16.1760  0.0818 ? -0.0264 ? -0.0254 ? 0.1315 ? -0.1588 ? 0.2638 ? 1.8929  ? 
1.2864  ? 0.5004  ? 1.5187  ? -0.1138 ? 5.8035  ? 0.1229  ? -0.1212 ? 0.2508  ? 0.2188  ? 0.0933  ? -0.1692 ? -0.3532 ? 0.3552  ? 
-0.2162 ? 
8  'X-RAY DIFFRACTION' ? refined 20.4820  -68.0230 -11.6610 0.3285 ? 0.0678  ? -0.1027 ? 0.2216 ? 0.0142  ? 0.1568 ? 7.0600  ? 
0.4973  ? -9.0441 ? 3.8960  ? 2.4990  ? 14.7008 ? 0.0674  ? 0.6669  ? -0.0765 ? -0.4098 ? -0.4585 ? 0.2791  ? -0.0948 ? -1.2139 ? 
0.3911  ? 
9  'X-RAY DIFFRACTION' ? refined 19.2250  -73.4970 -6.7660  0.1898 ? 0.0055  ? -0.0626 ? 0.1762 ? 0.0194  ? 0.1009 ? 5.2979  ? 
-1.4989 ? -4.1784 ? 1.3973  ? 0.3555  ? 4.5975  ? 0.1882  ? 0.1895  ? -0.0829 ? -0.3571 ? -0.2920 ? 0.0240  ? 0.0922  ? -0.0847 ? 
0.1037  ? 
10 'X-RAY DIFFRACTION' ? refined 29.5010  -65.9960 1.2370   0.1376 ? -0.0548 ? -0.0292 ? 0.1859 ? -0.0238 ? 0.1781 ? 5.1606  ? 
-1.3728 ? -2.1272 ? 5.5037  ? 1.6197  ? 9.5154  ? 0.4307  ? 0.3789  ? 0.1189  ? -0.3738 ? -0.0351 ? -0.4884 ? -0.5718 ? 0.6382  ? 
-0.3956 ? 
11 'X-RAY DIFFRACTION' ? refined 13.9260  -73.9440 5.2360   0.1631 ? -0.0730 ? -0.0333 ? 0.0747 ? -0.0126 ? 0.1014 ? 2.1865  ? 
0.4212  ? -0.2763 ? 2.3963  ? -0.0386 ? 1.3969  ? 0.1973  ? -0.1646 ? -0.0684 ? 0.3073  ? -0.1995 ? 0.3060  ? 0.0357  ? -0.1693 ? 
0.0022  ? 
12 'X-RAY DIFFRACTION' ? refined 46.7480  -75.8790 24.0150  0.1265 ? 0.0319  ? -0.1324 ? 0.3665 ? -0.0644 ? 0.1812 ? 1.7529  ? 
3.4462  ? -1.1623 ? 7.1595  ? -0.9015 ? 5.7888  ? 0.0769  ? -0.0267 ? -0.0816 ? 0.1510  ? 0.2235  ? -0.2391 ? 0.0309  ? 1.0226  ? 
-0.3004 ? 
13 'X-RAY DIFFRACTION' ? refined 44.2160  -73.5800 15.2760  0.0729 ? -0.0307 ? -0.0478 ? 0.2943 ? -0.0816 ? 0.1438 ? 4.1130  ? 
0.7146  ? 0.0661  ? 3.5098  ? 0.0911  ? 5.2431  ? 0.0648  ? 0.0291  ? 0.2691  ? -0.1049 ? 0.1110  ? -0.2249 ? -0.2460 ? 0.8109  ? 
-0.1758 ? 
14 'X-RAY DIFFRACTION' ? refined 33.5940  -72.3000 6.0430   0.0523 ? -0.0210 ? -0.0399 ? 0.1571 ? -0.0381 ? 0.0664 ? 9.0629  ? 
-1.8768 ? -0.7969 ? 8.6961  ? -3.8267 ? 4.6529  ? 0.2101  ? 0.0042  ? -0.1083 ? -0.2801 ? -0.1529 ? -0.0087 ? 0.0613  ? 0.2466  ? 
-0.0571 ? 
15 'X-RAY DIFFRACTION' ? refined 38.7410  -69.2180 19.4400  0.1469 ? -0.1004 ? 0.0730  ? 0.1696 ? -0.1280 ? 0.3381 ? 0.0990  ? 
0.1582  ? -0.5545 ? 1.9029  ? -0.0536 ? 5.1205  ? 0.0808  ? -0.0897 ? 0.1074  ? 0.0176  ? 0.1070  ? 0.0616  ? -0.2529 ? 0.5417  ? 
-0.1878 ? 
16 'X-RAY DIFFRACTION' ? refined 33.9190  -38.5870 13.1900  0.3447 ? -0.1048 ? -0.0020 ? 0.2643 ? -0.0552 ? 0.1520 ? 7.8389  ? 
1.6539  ? -4.4028 ? 2.6033  ? -0.6091 ? 6.8736  ? 0.1589  ? -1.2846 ? 0.0454  ? 0.6930  ? -0.3919 ? 0.1180  ? 0.1095  ? 0.4826  ? 
0.2329  ? 
17 'X-RAY DIFFRACTION' ? refined 33.3530  -43.0990 8.2130   0.1726 ? 0.0085  ? 0.0071  ? 0.0536 ? -0.0350 ? 0.1089 ? 4.1449  ? 
0.5582  ? -0.5813 ? 1.3720  ? 0.3873  ? 1.8116  ? 0.0551  ? -0.2834 ? -0.1046 ? 0.3548  ? -0.0709 ? 0.0830  ? -0.2117 ? -0.0529 ? 
0.0158  ? 
18 'X-RAY DIFFRACTION' ? refined 40.2790  -46.3720 -3.9480  0.1161 ? 0.0091  ? -0.0131 ? 0.1131 ? -0.0519 ? 0.1157 ? 4.2480  ? 
0.2297  ? 0.0434  ? 3.0188  ? -0.6177 ? 2.7012  ? 0.0337  ? 0.2520  ? -0.3493 ? -0.1890 ? -0.0765 ? -0.3312 ? 0.0541  ? 0.4267  ? 
0.0428  ? 
19 'X-RAY DIFFRACTION' ? refined 37.8700  -42.9850 -0.1720  0.1130 ? -0.0071 ? -0.0211 ? 0.1811 ? -0.0808 ? 0.0619 ? 1.9561  ? 
-0.5591 ? 0.8237  ? 2.9891  ? 0.7018  ? 0.8666  ? 0.0145  ? -0.0167 ? 0.0992  ? -0.1758 ? 0.0374  ? -0.1808 ? -0.0373 ? 0.1384  ? 
-0.0519 ? 
20 'X-RAY DIFFRACTION' ? refined 8.3410   -44.4160 -23.0020 0.0912 ? 0.0179  ? -0.0968 ? 0.1738 ? -0.0394 ? 0.1989 ? 4.1014  ? 
-4.3987 ? -2.2206 ? 7.3706  ? 1.3890  ? 3.4669  ? 0.1117  ? 0.0663  ? 0.1168  ? -0.1137 ? 0.0741  ? 0.2134  ? -0.1464 ? -0.2954 ? 
-0.1858 ? 
21 'X-RAY DIFFRACTION' ? refined 19.9850  -56.2340 -14.3240 0.2107 ? -0.0556 ? 0.0957  ? 0.2428 ? 0.0143  ? 0.2940 ? 1.3442  ? 
-1.3557 ? 1.3484  ? 2.2827  ? 2.1019  ? 14.7140 ? -0.2235 ? 0.4215  ? -0.1059 ? 0.3404  ? -0.3440 ? 0.2369  ? 0.3958  ? 0.8137  ? 
0.5676  ? 
22 'X-RAY DIFFRACTION' ? refined 10.0900  -40.6690 -13.8210 0.0828 ? 0.0760  ? 0.0108  ? 0.1064 ? -0.0236 ? 0.1661 ? 3.0871  ? 
-0.3992 ? 0.2631  ? 2.3818  ? -0.5065 ? 2.7746  ? -0.0013 ? -0.0721 ? 0.3716  ? 0.1261  ? 0.0748  ? 0.3055  ? -0.3190 ? -0.4779 ? 
-0.0735 ? 
23 'X-RAY DIFFRACTION' ? refined 17.1300  -38.0740 -15.4640 0.0930 ? 0.0543  ? -0.0163 ? 0.0851 ? 0.0538  ? 0.1451 ? 1.3083  ? 
0.3062  ? 1.0626  ? 0.8225  ? 0.6118  ? 5.4284  ? -0.1703 ? -0.0141 ? 0.0418  ? 0.0579  ? 0.1915  ? 0.2396  ? -0.2902 ? -0.2739 ? 
-0.0212 ? 
24 'X-RAY DIFFRACTION' ? refined 14.4710  -14.9520 63.3700  0.1353 ? -0.0680 ? 0.0755  ? 0.2611 ? 0.0355  ? 0.1477 ? 9.8026  ? 
-2.2053 ? 7.3497  ? 6.1018  ? -3.2923 ? 12.2269 ? -0.2703 ? -0.9420 ? -0.0372 ? 0.5031  ? 0.1636  ? 0.1873  ? -0.3191 ? -0.5578 ? 
0.1067  ? 
25 'X-RAY DIFFRACTION' ? refined 18.4450  -12.7920 58.4340  0.1403 ? -0.0532 ? 0.0563  ? 0.2035 ? 0.0169  ? 0.0878 ? 3.6258  ? 
-1.4686 ? 2.8644  ? 2.6417  ? -3.2866 ? 4.4791  ? 0.0399  ? -0.4145 ? -0.2123 ? -0.1464 ? 0.0894  ? 0.0504  ? 0.1920  ? -0.2742 ? 
-0.1292 ? 
26 'X-RAY DIFFRACTION' ? refined 16.9190  -4.3190  45.7520  0.0490 ? -0.0299 ? 0.0032  ? 0.1084 ? -0.0068 ? 0.0911 ? 1.7628  ? 
0.1329  ? 0.0616  ? 3.3436  ? -0.7805 ? 1.9020  ? -0.0283 ? 0.0999  ? 0.3320  ? -0.2867 ? 0.0643  ? 0.1853  ? 0.0338  ? -0.1396 ? 
-0.0359 ? 
27 'X-RAY DIFFRACTION' ? refined 17.3300  -11.4870 51.4440  0.0669 ? -0.0086 ? 0.0499  ? 0.0856 ? -0.0003 ? 0.0820 ? 2.4370  ? 
0.9608  ? 0.9762  ? 2.0012  ? -0.3034 ? 3.3534  ? -0.0905 ? -0.0966 ? 0.1131  ? -0.1005 ? 0.1433  ? 0.2015  ? -0.0712 ? -0.0631 ? 
-0.0528 ? 
28 'X-RAY DIFFRACTION' ? refined 38.4170  -30.0980 28.9990  0.3173 ? 0.0845  ? 0.0638  ? 0.2669 ? -0.0854 ? 0.1942 ? 1.2767  ? 
3.0396  ? -0.6067 ? 10.0909 ? -4.1693 ? 3.1864  ? 0.0073  ? 0.1368  ? -0.3049 ? -0.3505 ? 0.0670  ? -0.3766 ? 0.4467  ? 0.1137  ? 
-0.0744 ? 
29 'X-RAY DIFFRACTION' ? refined 34.8180  -29.8990 37.5520  0.2799 ? 0.0969  ? -0.0310 ? 0.1126 ? -0.0419 ? 0.1100 ? 2.9261  ? 
0.6736  ? -0.5139 ? 5.3904  ? 1.1733  ? 4.4277  ? -0.0983 ? -0.0173 ? -0.4054 ? 0.2067  ? -0.0168 ? 0.0036  ? 0.8329  ? 0.2359  ? 
0.1151  ? 
30 'X-RAY DIFFRACTION' ? refined 27.2620  -22.0680 46.5260  0.1757 ? 0.0155  ? 0.0098  ? 0.0501 ? -0.0303 ? 0.0688 ? 9.7736  ? 
7.0247  ? -2.5626 ? 10.9467 ? -2.6067 ? 4.4720  ? -0.0008 ? -0.0532 ? 0.1180  ? -0.0498 ? 0.1878  ? 0.3560  ? 0.5185  ? 0.2728  ? 
-0.1870 ? 
31 'X-RAY DIFFRACTION' ? refined 28.1930  -28.0570 33.1620  0.2069 ? -0.0092 ? -0.0175 ? 0.0602 ? -0.0592 ? 0.1014 ? 2.7179  ? 
2.1830  ? -0.3071 ? 1.9542  ? -1.1525 ? 4.1290  ? 0.0572  ? 0.1678  ? -0.1224 ? -0.0484 ? 0.1363  ? -0.0557 ? 0.4524  ? -0.0253 ? 
-0.1935 ? 
32 'X-RAY DIFFRACTION' ? refined 20.1290  -76.3750 66.6150  0.2206 ? -0.0574 ? 0.1469  ? 0.5070 ? 0.0913  ? 0.3057 ? 8.5286  ? 
-5.1940 ? 3.0659  ? 8.7831  ? -2.9940 ? 1.5919  ? -0.2503 ? -0.8050 ? 0.2062  ? 0.5316  ? 0.2844  ? -0.0721 ? -0.3626 ? -0.2222 ? 
-0.0342 ? 
33 'X-RAY DIFFRACTION' ? refined 23.9620  -74.0500 61.6040  0.2593 ? -0.0439 ? 0.0894  ? 0.3920 ? 0.0716  ? 0.1960 ? 3.3057  ? 
-2.5137 ? 0.4747  ? 3.7581  ? -1.1430 ? 2.8831  ? 0.0038  ? -0.3837 ? -0.1329 ? 0.1373  ? 0.0668  ? 0.1206  ? 0.2796  ? -0.5921 ? 
-0.0707 ? 
34 'X-RAY DIFFRACTION' ? refined 22.2130  -66.3600 49.5730  0.0824 ? 0.0284  ? 0.0136  ? 0.3128 ? 0.0215  ? 0.1446 ? 3.1008  ? 
-1.5478 ? -0.0478 ? 3.1599  ? 0.5253  ? 2.7105  ? 0.1817  ? 0.0493  ? 0.0300  ? -0.2496 ? -0.1102 ? 0.3306  ? -0.2563 ? -0.5993 ? 
-0.0715 ? 
35 'X-RAY DIFFRACTION' ? refined 20.8970  -69.8390 53.1090  0.1455 ? 0.0080  ? 0.0469  ? 0.6724 ? 0.1157  ? 0.2675 ? 0.9079  ? 
-0.1242 ? -0.7320 ? 2.3554  ? 0.6756  ? 0.9331  ? 0.0607  ? 0.0065  ? -0.0642 ? -0.1245 ? -0.1447 ? 0.5353  ? -0.0824 ? -0.4036 ? 
0.0840  ? 
36 'X-RAY DIFFRACTION' ? refined 38.4590  -87.7490 31.1620  0.1192 ? 0.0317  ? -0.1116 ? 0.1993 ? -0.0467 ? 0.1770 ? 2.5955  ? 
0.7427  ? 0.9087  ? 0.2738  ? -0.2672 ? 4.8739  ? 0.0037  ? 0.2250  ? -0.3035 ? -0.0376 ? 0.0691  ? -0.0922 ? 0.3491  ? 0.1007  ? 
-0.0727 ? 
37 'X-RAY DIFFRACTION' ? refined 34.1720  -94.2080 37.4840  0.3212 ? -0.0204 ? -0.1488 ? 0.1577 ? -0.0022 ? 0.2014 ? 2.7425  ? 
0.3047  ? -1.0226 ? 4.0617  ? 1.0741  ? 3.6178  ? 0.1026  ? -0.0466 ? -0.4554 ? 0.2940  ? -0.0043 ? 0.1064  ? 0.9177  ? -0.1710 ? 
-0.0983 ? 
38 'X-RAY DIFFRACTION' ? refined 29.4560  -84.4570 48.0420  0.1614 ? -0.1071 ? -0.0840 ? 0.2343 ? 0.0383  ? 0.2229 ? 3.4271  ? 
-2.6595 ? -1.7003 ? 7.3059  ? 0.2212  ? 5.4350  ? -0.0200 ? 0.0449  ? -0.1281 ? -0.0815 ? -0.1603 ? 0.1108  ? 0.6554  ? -0.1317 ? 
0.1804  ? 
39 'X-RAY DIFFRACTION' ? refined 28.1080  -89.2770 34.1620  0.1555 ? -0.0523 ? -0.1343 ? 0.1920 ? -0.0577 ? 0.2969 ? 2.5755  ? 
2.4950  ? 0.9025  ? 2.7318  ? 0.3035  ? 3.2424  ? 0.1258  ? 0.0088  ? -0.0638 ? 0.0005  ? -0.0629 ? 0.1804  ? 0.2285  ? -0.1511 ? 
-0.0630 ? 
40 'X-RAY DIFFRACTION' ? refined -31.2030 -37.8420 -9.0360  0.5526 ? 0.0983  ? -0.0357 ? 0.3495 ? 0.0448  ? 0.1266 ? 12.9191 ? 
-0.5378 ? -9.7659 ? 6.0180  ? 5.2622  ? 11.3570 ? 0.0233  ? 0.6429  ? -0.0534 ? -0.7897 ? -0.2262 ? 0.1738  ? -0.5267 ? -0.5996 ? 
0.2029  ? 
41 'X-RAY DIFFRACTION' ? refined -33.3790 -43.4560 -4.6870  0.2485 ? -0.0697 ? 0.0034  ? 0.2277 ? 0.0266  ? 0.1535 ? 4.4366  ? 
-2.2453 ? -2.3522 ? 2.5866  ? 1.2802  ? 3.6250  ? 0.2489  ? 0.5990  ? -0.0204 ? -0.6035 ? -0.2504 ? -0.1931 ? -0.2205 ? 0.0354  ? 
0.0015  ? 
42 'X-RAY DIFFRACTION' ? refined -22.5270 -37.9030 3.8200   0.3972 ? -0.0468 ? 0.1035  ? 0.2126 ? -0.0294 ? 0.2672 ? 3.3380  ? 
-1.6878 ? -3.8117 ? 0.9184  ? 2.3217  ? 10.5795 ? 0.4846  ? 0.1310  ? 0.2573  ? -0.3513 ? -0.0481 ? -0.1618 ? -0.5518 ? 0.3897  ? 
-0.4365 ? 
43 'X-RAY DIFFRACTION' ? refined -38.9540 -43.8610 7.3170   0.1304 ? -0.0679 ? -0.0329 ? 0.0900 ? -0.0068 ? 0.0687 ? 3.1065  ? 
0.8631  ? 0.3081  ? 2.1208  ? -0.2182 ? 1.6901  ? 0.0238  ? -0.0419 ? -0.0432 ? 0.0186  ? -0.0419 ? 0.2086  ? 0.0611  ? -0.1959 ? 
0.0181  ? 
44 'X-RAY DIFFRACTION' ? refined -8.4000  -50.0110 27.5060  0.1282 ? 0.0287  ? -0.0331 ? 0.1653 ? 0.0295  ? 0.1218 ? 3.4714  ? 
3.7501  ? -2.1351 ? 5.0836  ? -0.7805 ? 3.5793  ? -0.1291 ? -0.0469 ? -0.1883 ? -0.0342 ? 0.1732  ? -0.3123 ? 0.2184  ? 0.3938  ? 
-0.0441 ? 
45 'X-RAY DIFFRACTION' ? refined -9.9610  -47.5860 18.6080  0.0448 ? 0.0016  ? 0.0390  ? 0.1351 ? -0.0279 ? 0.0850 ? 3.9255  ? 
1.0933  ? 1.1303  ? 3.5025  ? -0.1467 ? 4.4373  ? -0.1332 ? 0.2871  ? 0.0638  ? -0.1429 ? 0.0728  ? -0.2200 ? -0.0653 ? 0.4988  ? 
0.0603  ? 
46 'X-RAY DIFFRACTION' ? refined -19.5340 -45.1040 8.5080   0.1599 ? 0.0311  ? -0.0199 ? 0.1344 ? -0.0810 ? 0.0871 ? 7.6169  ? 
1.5622  ? 2.6393  ? 9.8921  ? -1.0402 ? 1.1885  ? 0.3045  ? 0.4074  ? 0.0740  ? -0.4180 ? -0.3104 ? -0.0313 ? 0.2174  ? 0.2254  ? 
0.0059  ? 
47 'X-RAY DIFFRACTION' ? refined -14.9420 -42.3380 22.2440  0.0342 ? -0.0045 ? 0.0129  ? 0.0241 ? -0.0304 ? 0.0422 ? 1.6661  ? 
1.3216  ? -0.6673 ? 2.7522  ? -1.0036 ? 3.3448  ? 0.0402  ? -0.1166 ? 0.1528  ? -0.0267 ? 0.0240  ? -0.0735 ? 0.0306  ? 0.1058  ? 
-0.0641 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? AAA 347 ? ? ? AAA 368 ? ALL ? 
2  'X-RAY DIFFRACTION' 2  ? ? AAA 369 ? ? ? AAA 378 ? ALL ? 
3  'X-RAY DIFFRACTION' 3  ? ? AAA 379 ? ? ? AAA 527 ? ALL ? 
4  'X-RAY DIFFRACTION' 4  ? ? BBB 1   ? ? ? BBB 63  ? ALL ? 
5  'X-RAY DIFFRACTION' 5  ? ? BBB 64  ? ? ? BBB 69  ? ALL ? 
6  'X-RAY DIFFRACTION' 6  ? ? BBB 70  ? ? ? BBB 104 ? ALL ? 
7  'X-RAY DIFFRACTION' 7  ? ? BBB 105 ? ? ? BBB 124 ? ALL ? 
8  'X-RAY DIFFRACTION' 8  ? ? CCC 333 ? ? ? CCC 346 ? ALL ? 
9  'X-RAY DIFFRACTION' 9  ? ? CCC 347 ? ? ? CCC 368 ? ALL ? 
10 'X-RAY DIFFRACTION' 10 ? ? CCC 369 ? ? ? CCC 378 ? ALL ? 
11 'X-RAY DIFFRACTION' 11 ? ? CCC 379 ? ? ? CCC 527 ? ALL ? 
12 'X-RAY DIFFRACTION' 12 ? ? DDD 1   ? ? ? DDD 23  ? ALL ? 
13 'X-RAY DIFFRACTION' 13 ? ? DDD 24  ? ? ? DDD 99  ? ALL ? 
14 'X-RAY DIFFRACTION' 14 ? ? DDD 100 ? ? ? DDD 106 ? ALL ? 
15 'X-RAY DIFFRACTION' 15 ? ? DDD 107 ? ? ? DDD 124 ? ALL ? 
16 'X-RAY DIFFRACTION' 16 ? ? EEE 333 ? ? ? EEE 346 ? ALL ? 
17 'X-RAY DIFFRACTION' 17 ? ? EEE 347 ? ? ? EEE 371 ? ALL ? 
18 'X-RAY DIFFRACTION' 18 ? ? EEE 372 ? ? ? EEE 488 ? ALL ? 
19 'X-RAY DIFFRACTION' 19 ? ? EEE 489 ? ? ? EEE 527 ? ALL ? 
20 'X-RAY DIFFRACTION' 20 ? ? FFF 1   ? ? ? FFF 24  ? ALL ? 
21 'X-RAY DIFFRACTION' 21 ? ? FFF 25  ? ? ? FFF 32  ? ALL ? 
22 'X-RAY DIFFRACTION' 22 ? ? FFF 33  ? ? ? FFF 103 ? ALL ? 
23 'X-RAY DIFFRACTION' 23 ? ? FFF 104 ? ? ? FFF 124 ? ALL ? 
24 'X-RAY DIFFRACTION' 24 ? ? GGG 333 ? ? ? GGG 346 ? ALL ? 
25 'X-RAY DIFFRACTION' 25 ? ? GGG 347 ? ? ? GGG 373 ? ALL ? 
26 'X-RAY DIFFRACTION' 26 ? ? GGG 374 ? ? ? GGG 492 ? ALL ? 
27 'X-RAY DIFFRACTION' 27 ? ? GGG 493 ? ? ? GGG 527 ? ALL ? 
28 'X-RAY DIFFRACTION' 28 ? ? HHH 1   ? ? ? HHH 24  ? ALL ? 
29 'X-RAY DIFFRACTION' 29 ? ? HHH 25  ? ? ? HHH 99  ? ALL ? 
30 'X-RAY DIFFRACTION' 30 ? ? HHH 100 ? ? ? HHH 106 ? ALL ? 
31 'X-RAY DIFFRACTION' 31 ? ? HHH 107 ? ? ? HHH 124 ? ALL ? 
32 'X-RAY DIFFRACTION' 32 ? ? III 333 ? ? ? III 346 ? ALL ? 
33 'X-RAY DIFFRACTION' 33 ? ? III 347 ? ? ? III 371 ? ALL ? 
34 'X-RAY DIFFRACTION' 34 ? ? III 372 ? ? ? III 487 ? ALL ? 
35 'X-RAY DIFFRACTION' 35 ? ? III 488 ? ? ? III 527 ? ALL ? 
36 'X-RAY DIFFRACTION' 36 ? ? JJJ 1   ? ? ? JJJ 32  ? ALL ? 
37 'X-RAY DIFFRACTION' 37 ? ? JJJ 33  ? ? ? JJJ 99  ? ALL ? 
38 'X-RAY DIFFRACTION' 38 ? ? JJJ 100 ? ? ? JJJ 106 ? ALL ? 
39 'X-RAY DIFFRACTION' 39 ? ? JJJ 107 ? ? ? JJJ 124 ? ALL ? 
40 'X-RAY DIFFRACTION' 40 ? ? KKK 333 ? ? ? KKK 346 ? ALL ? 
41 'X-RAY DIFFRACTION' 41 ? ? KKK 347 ? ? ? KKK 368 ? ALL ? 
42 'X-RAY DIFFRACTION' 42 ? ? KKK 369 ? ? ? KKK 378 ? ALL ? 
43 'X-RAY DIFFRACTION' 43 ? ? KKK 379 ? ? ? KKK 527 ? ALL ? 
44 'X-RAY DIFFRACTION' 44 ? ? LLL 1   ? ? ? LLL 23  ? ALL ? 
45 'X-RAY DIFFRACTION' 45 ? ? LLL 24  ? ? ? LLL 99  ? ALL ? 
46 'X-RAY DIFFRACTION' 46 ? ? LLL 100 ? ? ? LLL 106 ? ALL ? 
47 'X-RAY DIFFRACTION' 47 ? ? LLL 107 ? ? ? LLL 124 ? ALL ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_pdbx_entry_details.entry_id                 7OAY 
_pdbx_entry_details.has_ligand_of_interest   N 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   EEE 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    481 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   EEE 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    701 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.99 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB AAA ARG 355 ? ? CA AAA ARG 355 ? ? C  AAA ARG 355 ? ? 94.66 110.40 -15.74 2.00 N 
2  1 CG AAA ARG 355 ? ? CD AAA ARG 355 ? ? NE AAA ARG 355 ? ? 98.12 111.80 -13.68 2.10 N 
3  1 CG AAA ARG 357 ? ? CD AAA ARG 357 ? ? NE AAA ARG 357 ? ? 98.92 111.80 -12.88 2.10 N 
4  1 CB CCC ARG 355 ? ? CA CCC ARG 355 ? ? C  CCC ARG 355 ? ? 93.47 110.40 -16.93 2.00 N 
5  1 CG CCC ARG 355 ? ? CD CCC ARG 355 ? ? NE CCC ARG 355 ? ? 96.08 111.80 -15.72 2.10 N 
6  1 CB EEE ARG 355 ? ? CA EEE ARG 355 ? ? C  EEE ARG 355 ? ? 94.56 110.40 -15.84 2.00 N 
7  1 CG EEE ARG 355 ? ? CD EEE ARG 355 ? ? NE EEE ARG 355 ? ? 97.99 111.80 -13.81 2.10 N 
8  1 CB GGG ARG 355 ? ? CA GGG ARG 355 ? ? C  GGG ARG 355 ? ? 95.07 110.40 -15.33 2.00 N 
9  1 CG GGG ARG 355 ? ? CD GGG ARG 355 ? ? NE GGG ARG 355 ? ? 95.57 111.80 -16.23 2.10 N 
10 1 CB III ARG 355 ? ? CA III ARG 355 ? ? C  III ARG 355 ? ? 95.04 110.40 -15.36 2.00 N 
11 1 CG III ARG 355 ? ? CD III ARG 355 ? ? NE III ARG 355 ? ? 99.12 111.80 -12.68 2.10 N 
12 1 CB KKK ARG 355 ? ? CA KKK ARG 355 ? ? C  KKK ARG 355 ? ? 94.60 110.40 -15.80 2.00 N 
13 1 CG KKK ARG 355 ? ? CD KKK ARG 355 ? ? NE KKK ARG 355 ? ? 95.70 111.80 -16.10 2.10 N 
14 1 CG KKK ARG 408 ? ? CD KKK ARG 408 ? ? NE KKK ARG 408 ? ? 98.72 111.80 -13.08 2.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR AAA 333 ? ? -141.11 -30.73 
2  1 ASN AAA 422 ? ? -126.53 -57.37 
3  1 SER BBB 55  ? ? 82.30   -2.41  
4  1 TYR BBB 105 ? ? -97.65  57.93  
5  1 ASN CCC 422 ? ? -127.24 -57.80 
6  1 SER DDD 55  ? ? 81.57   -0.80  
7  1 TYR DDD 105 ? ? -97.41  59.09  
8  1 THR EEE 333 ? ? 174.24  -44.16 
9  1 ASN EEE 422 ? ? -126.13 -57.92 
10 1 SER FFF 55  ? ? 81.57   -1.35  
11 1 TYR FFF 105 ? ? -98.45  59.53  
12 1 PHE GGG 377 ? ? -157.53 89.96  
13 1 ASN GGG 422 ? ? -126.70 -57.82 
14 1 SER HHH 55  ? ? 81.87   -2.21  
15 1 ALA HHH 92  ? ? 178.71  172.79 
16 1 TYR HHH 105 ? ? -98.31  59.82  
17 1 ASN III 422 ? ? -127.35 -59.57 
18 1 SER JJJ 55  ? ? 81.69   -1.48  
19 1 TYR JJJ 105 ? ? -95.73  58.38  
20 1 THR KKK 333 ? ? 162.24  -46.21 
21 1 ASN KKK 422 ? ? -126.38 -57.61 
22 1 SER LLL 55  ? ? 81.70   -1.05  
23 1 TYR LLL 105 ? ? -97.21  59.04  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 SER BBB 55 ? ? THR BBB 56 ? ? -147.38 
2 1 SER FFF 55 ? ? THR FFF 56 ? ? -149.32 
3 1 SER HHH 55 ? ? THR HHH 56 ? ? -147.84 
4 1 SER JJJ 55 ? ? THR JJJ 56 ? ? -148.89 
5 1 SER LLL 55 ? ? THR LLL 56 ? ? -148.04 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 AAA PRO 330 ? A PRO 1   
2   1 Y 1 AAA LYS 529 ? A LYS 200 
3   1 Y 1 AAA SER 530 ? A SER 201 
4   1 Y 1 AAA THR 531 ? A THR 202 
5   1 Y 1 AAA ASN 532 ? A ASN 203 
6   1 Y 1 AAA LYS 533 ? A LYS 204 
7   1 Y 1 AAA HIS 534 ? A HIS 205 
8   1 Y 1 AAA HIS 535 ? A HIS 206 
9   1 Y 1 AAA HIS 536 ? A HIS 207 
10  1 Y 1 AAA HIS 537 ? A HIS 208 
11  1 Y 1 AAA HIS 538 ? A HIS 209 
12  1 Y 1 AAA HIS 539 ? A HIS 210 
13  1 Y 1 BBB LYS 126 ? B LYS 126 
14  1 Y 1 BBB HIS 127 ? B HIS 127 
15  1 Y 1 BBB HIS 128 ? B HIS 128 
16  1 Y 1 BBB HIS 129 ? B HIS 129 
17  1 Y 1 BBB HIS 130 ? B HIS 130 
18  1 Y 1 BBB HIS 131 ? B HIS 131 
19  1 Y 1 BBB HIS 132 ? B HIS 132 
20  1 Y 1 CCC PRO 330 ? C PRO 1   
21  1 Y 1 CCC LYS 529 ? C LYS 200 
22  1 Y 1 CCC SER 530 ? C SER 201 
23  1 Y 1 CCC THR 531 ? C THR 202 
24  1 Y 1 CCC ASN 532 ? C ASN 203 
25  1 Y 1 CCC LYS 533 ? C LYS 204 
26  1 Y 1 CCC HIS 534 ? C HIS 205 
27  1 Y 1 CCC HIS 535 ? C HIS 206 
28  1 Y 1 CCC HIS 536 ? C HIS 207 
29  1 Y 1 CCC HIS 537 ? C HIS 208 
30  1 Y 1 CCC HIS 538 ? C HIS 209 
31  1 Y 1 CCC HIS 539 ? C HIS 210 
32  1 Y 1 DDD LYS 126 ? D LYS 126 
33  1 Y 1 DDD HIS 127 ? D HIS 127 
34  1 Y 1 DDD HIS 128 ? D HIS 128 
35  1 Y 1 DDD HIS 129 ? D HIS 129 
36  1 Y 1 DDD HIS 130 ? D HIS 130 
37  1 Y 1 DDD HIS 131 ? D HIS 131 
38  1 Y 1 DDD HIS 132 ? D HIS 132 
39  1 Y 1 EEE PRO 330 ? E PRO 1   
40  1 Y 1 EEE ASN 331 ? E ASN 2   
41  1 Y 1 EEE LYS 529 ? E LYS 200 
42  1 Y 1 EEE SER 530 ? E SER 201 
43  1 Y 1 EEE THR 531 ? E THR 202 
44  1 Y 1 EEE ASN 532 ? E ASN 203 
45  1 Y 1 EEE LYS 533 ? E LYS 204 
46  1 Y 1 EEE HIS 534 ? E HIS 205 
47  1 Y 1 EEE HIS 535 ? E HIS 206 
48  1 Y 1 EEE HIS 536 ? E HIS 207 
49  1 Y 1 EEE HIS 537 ? E HIS 208 
50  1 Y 1 EEE HIS 538 ? E HIS 209 
51  1 Y 1 EEE HIS 539 ? E HIS 210 
52  1 Y 1 FFF SER 125 ? F SER 125 
53  1 Y 1 FFF LYS 126 ? F LYS 126 
54  1 Y 1 FFF HIS 127 ? F HIS 127 
55  1 Y 1 FFF HIS 128 ? F HIS 128 
56  1 Y 1 FFF HIS 129 ? F HIS 129 
57  1 Y 1 FFF HIS 130 ? F HIS 130 
58  1 Y 1 FFF HIS 131 ? F HIS 131 
59  1 Y 1 FFF HIS 132 ? F HIS 132 
60  1 Y 1 GGG PRO 330 ? G PRO 1   
61  1 Y 1 GGG ASN 331 ? G ASN 2   
62  1 Y 1 GGG ILE 332 ? G ILE 3   
63  1 Y 1 GGG LYS 529 ? G LYS 200 
64  1 Y 1 GGG SER 530 ? G SER 201 
65  1 Y 1 GGG THR 531 ? G THR 202 
66  1 Y 1 GGG ASN 532 ? G ASN 203 
67  1 Y 1 GGG LYS 533 ? G LYS 204 
68  1 Y 1 GGG HIS 534 ? G HIS 205 
69  1 Y 1 GGG HIS 535 ? G HIS 206 
70  1 Y 1 GGG HIS 536 ? G HIS 207 
71  1 Y 1 GGG HIS 537 ? G HIS 208 
72  1 Y 1 GGG HIS 538 ? G HIS 209 
73  1 Y 1 GGG HIS 539 ? G HIS 210 
74  1 Y 1 HHH LYS 126 ? H LYS 126 
75  1 Y 1 HHH HIS 127 ? H HIS 127 
76  1 Y 1 HHH HIS 128 ? H HIS 128 
77  1 Y 1 HHH HIS 129 ? H HIS 129 
78  1 Y 1 HHH HIS 130 ? H HIS 130 
79  1 Y 1 HHH HIS 131 ? H HIS 131 
80  1 Y 1 HHH HIS 132 ? H HIS 132 
81  1 Y 1 III PRO 330 ? I PRO 1   
82  1 Y 1 III LYS 529 ? I LYS 200 
83  1 Y 1 III SER 530 ? I SER 201 
84  1 Y 1 III THR 531 ? I THR 202 
85  1 Y 1 III ASN 532 ? I ASN 203 
86  1 Y 1 III LYS 533 ? I LYS 204 
87  1 Y 1 III HIS 534 ? I HIS 205 
88  1 Y 1 III HIS 535 ? I HIS 206 
89  1 Y 1 III HIS 536 ? I HIS 207 
90  1 Y 1 III HIS 537 ? I HIS 208 
91  1 Y 1 III HIS 538 ? I HIS 209 
92  1 Y 1 III HIS 539 ? I HIS 210 
93  1 Y 1 JJJ LYS 126 ? J LYS 126 
94  1 Y 1 JJJ HIS 127 ? J HIS 127 
95  1 Y 1 JJJ HIS 128 ? J HIS 128 
96  1 Y 1 JJJ HIS 129 ? J HIS 129 
97  1 Y 1 JJJ HIS 130 ? J HIS 130 
98  1 Y 1 JJJ HIS 131 ? J HIS 131 
99  1 Y 1 JJJ HIS 132 ? J HIS 132 
100 1 Y 1 KKK PRO 330 ? K PRO 1   
101 1 Y 1 KKK ASN 331 ? K ASN 2   
102 1 Y 1 KKK LYS 529 ? K LYS 200 
103 1 Y 1 KKK SER 530 ? K SER 201 
104 1 Y 1 KKK THR 531 ? K THR 202 
105 1 Y 1 KKK ASN 532 ? K ASN 203 
106 1 Y 1 KKK LYS 533 ? K LYS 204 
107 1 Y 1 KKK HIS 534 ? K HIS 205 
108 1 Y 1 KKK HIS 535 ? K HIS 206 
109 1 Y 1 KKK HIS 536 ? K HIS 207 
110 1 Y 1 KKK HIS 537 ? K HIS 208 
111 1 Y 1 KKK HIS 538 ? K HIS 209 
112 1 Y 1 KKK HIS 539 ? K HIS 210 
113 1 Y 1 LLL LYS 126 ? L LYS 126 
114 1 Y 1 LLL HIS 127 ? L HIS 127 
115 1 Y 1 LLL HIS 128 ? L HIS 128 
116 1 Y 1 LLL HIS 129 ? L HIS 129 
117 1 Y 1 LLL HIS 130 ? L HIS 130 
118 1 Y 1 LLL HIS 131 ? L HIS 131 
119 1 Y 1 LLL HIS 132 ? L HIS 132 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Wellcome Trust'                                     'United Kingdom' '100209/Z/12/Z)' 1 
'Engineering and Physical Sciences Research Council' 'United Kingdom' EP/S025243/1     2 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
4 water                                    HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
