data_8OWT
# 
_entry.id   8OWT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.392 
_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   8OWT         pdb_00008owt 10.2210/pdb8owt/pdb 
WWPDB D_1292129660 ?            ?                   
# 
_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       2024-05-08 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8OWT 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-28 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ray.owens@rfi.ac.uk 
_pdbx_contact_author.name_first         Raymond 
_pdbx_contact_author.name_last          Owens 
_pdbx_contact_author.name_mi            J 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3705-2993 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mikolajek, H.'  1 ? 
'Naismith, J.H.' 2 ? 
'Owens, R.J.'    3 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Trimeric nanobodies potently neutralize Omicron variants of SARS-CoV-2' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_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 'Cornish, K.A.S.' 1 ? 
primary 'Mikolajek, H.'   2 ? 
primary 'Naismith, J.H.'  3 ? 
primary 'Owens, R.J.'     4 ? 
# 
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 'Nanobody A8'                            14481.021 2   ? ? ? ? 
2 polymer     man 'Spike protein S1'                       23716.580 2   ? ? ? ? 
3 polymer     man 'Nanobody H3'                            15134.849 2   ? ? ? ? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2   ? ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'   195.237   1   ? ? ? ? 
6 water       nat water                                    18.015    172 ? ? ? ? 
# 
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 
;QVQLVESGGGLVQAGGSLRLSCAASGGTFSTAAMGWFRQAPGEERECVASIGWRGVRTWYADSVKGRFTISRDNPQNTVY
LQMNNLKSGDTAVYYCAASVGNYGLPWAHFEYDFWGQGIQVTVSSKHHHHHH
;
;QVQLVESGGGLVQAGGSLRLSCAASGGTFSTAAMGWFRQAPGEERECVASIGWRGVRTWYADSVKGRFTISRDNPQNTVY
LQMNNLKSGDTAVYYCAASVGNYGLPWAHFEYDFWGQGIQVTVSSKHHHHHH
;
AAA,DDD ? 
2 'polypeptide(L)' no no 
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNKHHHHHH
;
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNKHHHHHH
;
BBB,EEE ? 
3 'polypeptide(L)' no no 
;MAQVQLVESGGGLVKTGGSLRLSCAASGRTFSTYSMGWFRQAPGKEREFVAGMRWTGSSTFYSDSVKGRFTVSRNNAKDT
VYLHMNSLKPEDTAVYYCAITTIVRAYYTEYTEADFGSWGQGTQVTVSSKHHHHHH
;
;MAQVQLVESGGGLVKTGGSLRLSCAASGRTFSTYSMGWFRQAPGKEREFVAGMRWTGSSTFYSDSVKGRFTVSRNNAKDT
VYLHMNSLKPEDTAVYYCAITTIVRAYYTEYTEADFGSWGQGTQVTVSSKHHHHHH
;
CCC,FFF ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'   MES 
6 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   VAL n 
1 3   GLN n 
1 4   LEU n 
1 5   VAL n 
1 6   GLU n 
1 7   SER n 
1 8   GLY n 
1 9   GLY n 
1 10  GLY n 
1 11  LEU n 
1 12  VAL n 
1 13  GLN n 
1 14  ALA n 
1 15  GLY n 
1 16  GLY n 
1 17  SER n 
1 18  LEU n 
1 19  ARG n 
1 20  LEU n 
1 21  SER n 
1 22  CYS n 
1 23  ALA n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  GLY n 
1 28  THR n 
1 29  PHE n 
1 30  SER n 
1 31  THR n 
1 32  ALA n 
1 33  ALA n 
1 34  MET n 
1 35  GLY n 
1 36  TRP n 
1 37  PHE n 
1 38  ARG n 
1 39  GLN n 
1 40  ALA n 
1 41  PRO n 
1 42  GLY n 
1 43  GLU n 
1 44  GLU n 
1 45  ARG n 
1 46  GLU n 
1 47  CYS n 
1 48  VAL n 
1 49  ALA n 
1 50  SER n 
1 51  ILE n 
1 52  GLY n 
1 53  TRP n 
1 54  ARG n 
1 55  GLY n 
1 56  VAL n 
1 57  ARG n 
1 58  THR n 
1 59  TRP n 
1 60  TYR n 
1 61  ALA n 
1 62  ASP n 
1 63  SER n 
1 64  VAL n 
1 65  LYS n 
1 66  GLY n 
1 67  ARG n 
1 68  PHE n 
1 69  THR n 
1 70  ILE n 
1 71  SER n 
1 72  ARG n 
1 73  ASP n 
1 74  ASN n 
1 75  PRO n 
1 76  GLN n 
1 77  ASN n 
1 78  THR n 
1 79  VAL n 
1 80  TYR n 
1 81  LEU n 
1 82  GLN n 
1 83  MET n 
1 84  ASN n 
1 85  ASN n 
1 86  LEU n 
1 87  LYS n 
1 88  SER n 
1 89  GLY n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  VAL n 
1 94  TYR n 
1 95  TYR n 
1 96  CYS n 
1 97  ALA n 
1 98  ALA n 
1 99  SER n 
1 100 VAL n 
1 101 GLY n 
1 102 ASN n 
1 103 TYR n 
1 104 GLY n 
1 105 LEU n 
1 106 PRO n 
1 107 TRP n 
1 108 ALA n 
1 109 HIS n 
1 110 PHE n 
1 111 GLU n 
1 112 TYR n 
1 113 ASP n 
1 114 PHE n 
1 115 TRP n 
1 116 GLY n 
1 117 GLN n 
1 118 GLY n 
1 119 ILE n 
1 120 GLN n 
1 121 VAL n 
1 122 THR n 
1 123 VAL n 
1 124 SER n 
1 125 SER n 
1 126 LYS n 
1 127 HIS n 
1 128 HIS n 
1 129 HIS n 
1 130 HIS n 
1 131 HIS n 
1 132 HIS n 
2 1   PRO n 
2 2   ASN n 
2 3   ILE n 
2 4   THR n 
2 5   ASN n 
2 6   LEU n 
2 7   CYS n 
2 8   PRO n 
2 9   PHE n 
2 10  GLY n 
2 11  GLU n 
2 12  VAL n 
2 13  PHE n 
2 14  ASN n 
2 15  ALA n 
2 16  THR n 
2 17  ARG n 
2 18  PHE n 
2 19  ALA n 
2 20  SER n 
2 21  VAL n 
2 22  TYR n 
2 23  ALA n 
2 24  TRP n 
2 25  ASN n 
2 26  ARG n 
2 27  LYS n 
2 28  ARG n 
2 29  ILE n 
2 30  SER n 
2 31  ASN n 
2 32  CYS n 
2 33  VAL n 
2 34  ALA n 
2 35  ASP n 
2 36  TYR n 
2 37  SER n 
2 38  VAL n 
2 39  LEU n 
2 40  TYR n 
2 41  ASN n 
2 42  SER n 
2 43  ALA n 
2 44  SER n 
2 45  PHE n 
2 46  SER n 
2 47  THR n 
2 48  PHE n 
2 49  LYS n 
2 50  CYS n 
2 51  TYR n 
2 52  GLY n 
2 53  VAL n 
2 54  SER n 
2 55  PRO n 
2 56  THR n 
2 57  LYS n 
2 58  LEU n 
2 59  ASN n 
2 60  ASP n 
2 61  LEU n 
2 62  CYS n 
2 63  PHE n 
2 64  THR n 
2 65  ASN n 
2 66  VAL n 
2 67  TYR n 
2 68  ALA n 
2 69  ASP n 
2 70  SER n 
2 71  PHE n 
2 72  VAL n 
2 73  ILE n 
2 74  ARG n 
2 75  GLY n 
2 76  ASP n 
2 77  GLU n 
2 78  VAL n 
2 79  ARG n 
2 80  GLN n 
2 81  ILE n 
2 82  ALA n 
2 83  PRO n 
2 84  GLY n 
2 85  GLN n 
2 86  THR n 
2 87  GLY n 
2 88  LYS n 
2 89  ILE n 
2 90  ALA n 
2 91  ASP n 
2 92  TYR n 
2 93  ASN n 
2 94  TYR n 
2 95  LYS n 
2 96  LEU n 
2 97  PRO n 
2 98  ASP n 
2 99  ASP n 
2 100 PHE n 
2 101 THR n 
2 102 GLY n 
2 103 CYS n 
2 104 VAL n 
2 105 ILE n 
2 106 ALA n 
2 107 TRP n 
2 108 ASN n 
2 109 SER n 
2 110 ASN n 
2 111 ASN n 
2 112 LEU n 
2 113 ASP n 
2 114 SER n 
2 115 LYS n 
2 116 VAL n 
2 117 GLY n 
2 118 GLY n 
2 119 ASN n 
2 120 TYR n 
2 121 ASN n 
2 122 TYR n 
2 123 LEU n 
2 124 TYR n 
2 125 ARG n 
2 126 LEU n 
2 127 PHE n 
2 128 ARG n 
2 129 LYS n 
2 130 SER n 
2 131 ASN n 
2 132 LEU n 
2 133 LYS n 
2 134 PRO n 
2 135 PHE n 
2 136 GLU n 
2 137 ARG n 
2 138 ASP n 
2 139 ILE n 
2 140 SER n 
2 141 THR n 
2 142 GLU n 
2 143 ILE n 
2 144 TYR n 
2 145 GLN n 
2 146 ALA n 
2 147 GLY n 
2 148 SER n 
2 149 THR n 
2 150 PRO n 
2 151 CYS n 
2 152 ASN n 
2 153 GLY n 
2 154 VAL n 
2 155 GLU n 
2 156 GLY n 
2 157 PHE n 
2 158 ASN n 
2 159 CYS n 
2 160 TYR n 
2 161 PHE n 
2 162 PRO n 
2 163 LEU n 
2 164 GLN n 
2 165 SER n 
2 166 TYR n 
2 167 GLY n 
2 168 PHE n 
2 169 GLN n 
2 170 PRO n 
2 171 THR n 
2 172 ASN n 
2 173 GLY n 
2 174 VAL n 
2 175 GLY n 
2 176 TYR n 
2 177 GLN n 
2 178 PRO n 
2 179 TYR n 
2 180 ARG n 
2 181 VAL n 
2 182 VAL n 
2 183 VAL n 
2 184 LEU n 
2 185 SER n 
2 186 PHE n 
2 187 GLU n 
2 188 LEU n 
2 189 LEU n 
2 190 HIS n 
2 191 ALA n 
2 192 PRO n 
2 193 ALA n 
2 194 THR n 
2 195 VAL n 
2 196 CYS n 
2 197 GLY n 
2 198 PRO n 
2 199 LYS n 
2 200 LYS n 
2 201 SER n 
2 202 THR n 
2 203 ASN n 
2 204 LYS n 
2 205 HIS n 
2 206 HIS n 
2 207 HIS n 
2 208 HIS n 
2 209 HIS n 
2 210 HIS n 
3 1   MET n 
3 2   ALA n 
3 3   GLN n 
3 4   VAL n 
3 5   GLN n 
3 6   LEU n 
3 7   VAL n 
3 8   GLU n 
3 9   SER n 
3 10  GLY n 
3 11  GLY n 
3 12  GLY n 
3 13  LEU n 
3 14  VAL n 
3 15  LYS n 
3 16  THR n 
3 17  GLY n 
3 18  GLY n 
3 19  SER n 
3 20  LEU n 
3 21  ARG n 
3 22  LEU n 
3 23  SER n 
3 24  CYS n 
3 25  ALA n 
3 26  ALA n 
3 27  SER n 
3 28  GLY n 
3 29  ARG n 
3 30  THR n 
3 31  PHE n 
3 32  SER n 
3 33  THR n 
3 34  TYR n 
3 35  SER n 
3 36  MET n 
3 37  GLY n 
3 38  TRP n 
3 39  PHE n 
3 40  ARG n 
3 41  GLN n 
3 42  ALA n 
3 43  PRO n 
3 44  GLY n 
3 45  LYS n 
3 46  GLU n 
3 47  ARG n 
3 48  GLU n 
3 49  PHE n 
3 50  VAL n 
3 51  ALA n 
3 52  GLY n 
3 53  MET n 
3 54  ARG n 
3 55  TRP n 
3 56  THR n 
3 57  GLY n 
3 58  SER n 
3 59  SER n 
3 60  THR n 
3 61  PHE n 
3 62  TYR n 
3 63  SER n 
3 64  ASP n 
3 65  SER n 
3 66  VAL n 
3 67  LYS n 
3 68  GLY n 
3 69  ARG n 
3 70  PHE n 
3 71  THR n 
3 72  VAL n 
3 73  SER n 
3 74  ARG n 
3 75  ASN n 
3 76  ASN n 
3 77  ALA n 
3 78  LYS n 
3 79  ASP n 
3 80  THR n 
3 81  VAL n 
3 82  TYR n 
3 83  LEU n 
3 84  HIS n 
3 85  MET n 
3 86  ASN n 
3 87  SER n 
3 88  LEU n 
3 89  LYS n 
3 90  PRO n 
3 91  GLU n 
3 92  ASP n 
3 93  THR n 
3 94  ALA n 
3 95  VAL n 
3 96  TYR n 
3 97  TYR n 
3 98  CYS n 
3 99  ALA n 
3 100 ILE n 
3 101 THR n 
3 102 THR n 
3 103 ILE n 
3 104 VAL n 
3 105 ARG n 
3 106 ALA n 
3 107 TYR n 
3 108 TYR n 
3 109 THR n 
3 110 GLU n 
3 111 TYR n 
3 112 THR n 
3 113 GLU n 
3 114 ALA n 
3 115 ASP n 
3 116 PHE n 
3 117 GLY n 
3 118 SER n 
3 119 TRP n 
3 120 GLY n 
3 121 GLN n 
3 122 GLY n 
3 123 THR n 
3 124 GLN n 
3 125 VAL n 
3 126 THR n 
3 127 VAL n 
3 128 SER n 
3 129 SER n 
3 130 LYS n 
3 131 HIS n 
3 132 HIS n 
3 133 HIS n 
3 134 HIS n 
3 135 HIS n 
3 136 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' 1 132 ? ? ?      ? ? ? ? ? ? 'Lama glama'                                      9844    ? ? ? ? ? 
? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 210 ? ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? 
? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 136 ? ? ?      ? ? ? ? ? ? 'Lama glama'                                      9844    ? ? ? ? ? 
? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
MES non-polymer                  . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'   ? 'C6 H13 N O4 S'  195.237 
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 
# 
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_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   GLN 1   3   3   GLN GLN AAA . n 
A 1 2   VAL 2   4   4   VAL VAL AAA . n 
A 1 3   GLN 3   5   5   GLN GLN AAA . n 
A 1 4   LEU 4   6   6   LEU LEU AAA . n 
A 1 5   VAL 5   7   7   VAL VAL AAA . n 
A 1 6   GLU 6   8   8   GLU GLU AAA . n 
A 1 7   SER 7   9   9   SER SER AAA . n 
A 1 8   GLY 8   10  10  GLY GLY AAA . n 
A 1 9   GLY 9   11  11  GLY GLY AAA . n 
A 1 10  GLY 10  12  12  GLY GLY AAA . n 
A 1 11  LEU 11  13  13  LEU LEU AAA . n 
A 1 12  VAL 12  14  14  VAL VAL AAA . n 
A 1 13  GLN 13  15  15  GLN GLN AAA . n 
A 1 14  ALA 14  16  16  ALA ALA AAA . n 
A 1 15  GLY 15  17  17  GLY GLY AAA . n 
A 1 16  GLY 16  18  18  GLY GLY AAA . n 
A 1 17  SER 17  19  19  SER SER AAA . n 
A 1 18  LEU 18  20  20  LEU LEU AAA . n 
A 1 19  ARG 19  21  21  ARG ARG AAA . n 
A 1 20  LEU 20  22  22  LEU LEU AAA . n 
A 1 21  SER 21  23  23  SER SER AAA . n 
A 1 22  CYS 22  24  24  CYS CYS AAA . n 
A 1 23  ALA 23  25  25  ALA ALA AAA . n 
A 1 24  ALA 24  26  26  ALA ALA AAA . n 
A 1 25  SER 25  27  27  SER SER AAA . n 
A 1 26  GLY 26  28  28  GLY GLY AAA . n 
A 1 27  GLY 27  29  29  GLY GLY AAA . n 
A 1 28  THR 28  30  30  THR THR AAA . n 
A 1 29  PHE 29  31  31  PHE PHE AAA . n 
A 1 30  SER 30  32  32  SER SER AAA . n 
A 1 31  THR 31  33  33  THR THR AAA . n 
A 1 32  ALA 32  34  34  ALA ALA AAA . n 
A 1 33  ALA 33  35  35  ALA ALA AAA . n 
A 1 34  MET 34  36  36  MET MET AAA . n 
A 1 35  GLY 35  37  37  GLY GLY AAA . n 
A 1 36  TRP 36  38  38  TRP TRP AAA . n 
A 1 37  PHE 37  39  39  PHE PHE AAA . n 
A 1 38  ARG 38  40  40  ARG ARG AAA . n 
A 1 39  GLN 39  41  41  GLN GLN AAA . n 
A 1 40  ALA 40  42  42  ALA ALA AAA . n 
A 1 41  PRO 41  43  43  PRO PRO AAA . n 
A 1 42  GLY 42  44  44  GLY GLY AAA . n 
A 1 43  GLU 43  45  45  GLU GLU AAA . n 
A 1 44  GLU 44  46  46  GLU GLU AAA . n 
A 1 45  ARG 45  47  47  ARG ARG AAA . n 
A 1 46  GLU 46  48  48  GLU GLU AAA . n 
A 1 47  CYS 47  49  49  CYS CYS AAA . n 
A 1 48  VAL 48  50  50  VAL VAL AAA . n 
A 1 49  ALA 49  51  51  ALA ALA AAA . n 
A 1 50  SER 50  52  52  SER SER AAA . n 
A 1 51  ILE 51  53  53  ILE ILE AAA . n 
A 1 52  GLY 52  54  54  GLY GLY AAA . n 
A 1 53  TRP 53  55  55  TRP TRP AAA . n 
A 1 54  ARG 54  56  56  ARG ARG AAA . n 
A 1 55  GLY 55  57  57  GLY GLY AAA . n 
A 1 56  VAL 56  58  58  VAL VAL AAA . n 
A 1 57  ARG 57  59  59  ARG ARG AAA . n 
A 1 58  THR 58  60  60  THR THR AAA . n 
A 1 59  TRP 59  61  61  TRP TRP AAA . n 
A 1 60  TYR 60  62  62  TYR TYR AAA . n 
A 1 61  ALA 61  63  63  ALA ALA AAA . n 
A 1 62  ASP 62  64  64  ASP ASP AAA . n 
A 1 63  SER 63  65  65  SER SER AAA . n 
A 1 64  VAL 64  66  66  VAL VAL AAA . n 
A 1 65  LYS 65  67  67  LYS LYS AAA . n 
A 1 66  GLY 66  68  68  GLY GLY AAA . n 
A 1 67  ARG 67  69  69  ARG ARG AAA . n 
A 1 68  PHE 68  70  70  PHE PHE AAA . n 
A 1 69  THR 69  71  71  THR THR AAA . n 
A 1 70  ILE 70  72  72  ILE ILE AAA . n 
A 1 71  SER 71  73  73  SER SER AAA . n 
A 1 72  ARG 72  74  74  ARG ARG AAA . n 
A 1 73  ASP 73  75  75  ASP ASP AAA . n 
A 1 74  ASN 74  76  76  ASN ASN AAA . n 
A 1 75  PRO 75  77  77  PRO PRO AAA . n 
A 1 76  GLN 76  78  78  GLN GLN AAA . n 
A 1 77  ASN 77  79  79  ASN ASN AAA . n 
A 1 78  THR 78  80  80  THR THR AAA . n 
A 1 79  VAL 79  81  81  VAL VAL AAA . n 
A 1 80  TYR 80  82  82  TYR TYR AAA . n 
A 1 81  LEU 81  83  83  LEU LEU AAA . n 
A 1 82  GLN 82  84  84  GLN GLN AAA . n 
A 1 83  MET 83  85  85  MET MET AAA . n 
A 1 84  ASN 84  86  86  ASN ASN AAA . n 
A 1 85  ASN 85  87  87  ASN ASN AAA . n 
A 1 86  LEU 86  88  88  LEU LEU AAA . n 
A 1 87  LYS 87  89  89  LYS LYS AAA . n 
A 1 88  SER 88  90  90  SER SER AAA . n 
A 1 89  GLY 89  91  91  GLY GLY AAA . n 
A 1 90  ASP 90  92  92  ASP ASP AAA . n 
A 1 91  THR 91  93  93  THR THR AAA . n 
A 1 92  ALA 92  94  94  ALA ALA AAA . n 
A 1 93  VAL 93  95  95  VAL VAL AAA . n 
A 1 94  TYR 94  96  96  TYR TYR AAA . n 
A 1 95  TYR 95  97  97  TYR TYR AAA . n 
A 1 96  CYS 96  98  98  CYS CYS AAA . n 
A 1 97  ALA 97  99  99  ALA ALA AAA . n 
A 1 98  ALA 98  100 100 ALA ALA AAA . n 
A 1 99  SER 99  101 101 SER SER AAA . n 
A 1 100 VAL 100 102 102 VAL VAL AAA . n 
A 1 101 GLY 101 103 103 GLY GLY AAA . n 
A 1 102 ASN 102 104 104 ASN ASN AAA . n 
A 1 103 TYR 103 105 105 TYR TYR AAA . n 
A 1 104 GLY 104 106 106 GLY GLY AAA . n 
A 1 105 LEU 105 107 107 LEU LEU AAA . n 
A 1 106 PRO 106 108 108 PRO PRO AAA . n 
A 1 107 TRP 107 109 109 TRP TRP AAA . n 
A 1 108 ALA 108 110 110 ALA ALA AAA . n 
A 1 109 HIS 109 111 111 HIS HIS AAA . n 
A 1 110 PHE 110 112 112 PHE PHE AAA . n 
A 1 111 GLU 111 113 113 GLU GLU AAA . n 
A 1 112 TYR 112 114 114 TYR TYR AAA . n 
A 1 113 ASP 113 115 115 ASP ASP AAA . n 
A 1 114 PHE 114 116 116 PHE PHE AAA . n 
A 1 115 TRP 115 117 117 TRP TRP AAA . n 
A 1 116 GLY 116 118 118 GLY GLY AAA . n 
A 1 117 GLN 117 119 119 GLN GLN AAA . n 
A 1 118 GLY 118 120 120 GLY GLY AAA . n 
A 1 119 ILE 119 121 121 ILE ILE AAA . n 
A 1 120 GLN 120 122 122 GLN GLN AAA . n 
A 1 121 VAL 121 123 123 VAL VAL AAA . n 
A 1 122 THR 122 124 124 THR THR AAA . n 
A 1 123 VAL 123 125 125 VAL VAL AAA . n 
A 1 124 SER 124 126 ?   ?   ?   AAA . n 
A 1 125 SER 125 127 ?   ?   ?   AAA . n 
A 1 126 LYS 126 128 ?   ?   ?   AAA . n 
A 1 127 HIS 127 129 ?   ?   ?   AAA . n 
A 1 128 HIS 128 130 ?   ?   ?   AAA . n 
A 1 129 HIS 129 131 ?   ?   ?   AAA . n 
A 1 130 HIS 130 132 ?   ?   ?   AAA . n 
A 1 131 HIS 131 133 ?   ?   ?   AAA . n 
A 1 132 HIS 132 134 ?   ?   ?   AAA . n 
B 2 1   PRO 1   330 ?   ?   ?   BBB . n 
B 2 2   ASN 2   331 331 ASN ASN BBB . n 
B 2 3   ILE 3   332 332 ILE ILE BBB . n 
B 2 4   THR 4   333 333 THR THR BBB . n 
B 2 5   ASN 5   334 334 ASN ASN BBB . n 
B 2 6   LEU 6   335 335 LEU LEU BBB . n 
B 2 7   CYS 7   336 336 CYS CYS BBB . n 
B 2 8   PRO 8   337 337 PRO PRO BBB . n 
B 2 9   PHE 9   338 338 PHE PHE BBB . n 
B 2 10  GLY 10  339 339 GLY GLY BBB . n 
B 2 11  GLU 11  340 340 GLU GLU BBB . n 
B 2 12  VAL 12  341 341 VAL VAL BBB . n 
B 2 13  PHE 13  342 342 PHE PHE BBB . n 
B 2 14  ASN 14  343 343 ASN ASN BBB . n 
B 2 15  ALA 15  344 344 ALA ALA BBB . n 
B 2 16  THR 16  345 345 THR THR BBB . n 
B 2 17  ARG 17  346 346 ARG ARG BBB . n 
B 2 18  PHE 18  347 347 PHE PHE BBB . n 
B 2 19  ALA 19  348 348 ALA ALA BBB . n 
B 2 20  SER 20  349 349 SER SER BBB . n 
B 2 21  VAL 21  350 350 VAL VAL BBB . n 
B 2 22  TYR 22  351 351 TYR TYR BBB . n 
B 2 23  ALA 23  352 352 ALA ALA BBB . n 
B 2 24  TRP 24  353 353 TRP TRP BBB . n 
B 2 25  ASN 25  354 354 ASN ASN BBB . n 
B 2 26  ARG 26  355 355 ARG ARG BBB . n 
B 2 27  LYS 27  356 356 LYS LYS BBB . n 
B 2 28  ARG 28  357 357 ARG ARG BBB . n 
B 2 29  ILE 29  358 358 ILE ILE BBB . n 
B 2 30  SER 30  359 359 SER SER BBB . n 
B 2 31  ASN 31  360 360 ASN ASN BBB . n 
B 2 32  CYS 32  361 361 CYS CYS BBB . n 
B 2 33  VAL 33  362 362 VAL VAL BBB . n 
B 2 34  ALA 34  363 363 ALA ALA BBB . n 
B 2 35  ASP 35  364 364 ASP ASP BBB . n 
B 2 36  TYR 36  365 365 TYR TYR BBB . n 
B 2 37  SER 37  366 366 SER SER BBB . n 
B 2 38  VAL 38  367 367 VAL VAL BBB . n 
B 2 39  LEU 39  368 368 LEU LEU BBB . n 
B 2 40  TYR 40  369 369 TYR TYR BBB . n 
B 2 41  ASN 41  370 370 ASN ASN BBB . n 
B 2 42  SER 42  371 371 SER SER BBB . n 
B 2 43  ALA 43  372 372 ALA ALA BBB . n 
B 2 44  SER 44  373 373 SER SER BBB . n 
B 2 45  PHE 45  374 374 PHE PHE BBB . n 
B 2 46  SER 46  375 375 SER SER BBB . n 
B 2 47  THR 47  376 376 THR THR BBB . n 
B 2 48  PHE 48  377 377 PHE PHE BBB . n 
B 2 49  LYS 49  378 378 LYS LYS BBB . n 
B 2 50  CYS 50  379 379 CYS CYS BBB . n 
B 2 51  TYR 51  380 380 TYR TYR BBB . n 
B 2 52  GLY 52  381 381 GLY GLY BBB . n 
B 2 53  VAL 53  382 382 VAL VAL BBB . n 
B 2 54  SER 54  383 383 SER SER BBB . n 
B 2 55  PRO 55  384 384 PRO PRO BBB . n 
B 2 56  THR 56  385 385 THR THR BBB . n 
B 2 57  LYS 57  386 386 LYS LYS BBB . n 
B 2 58  LEU 58  387 387 LEU LEU BBB . n 
B 2 59  ASN 59  388 388 ASN ASN BBB . n 
B 2 60  ASP 60  389 389 ASP ASP BBB . n 
B 2 61  LEU 61  390 390 LEU LEU BBB . n 
B 2 62  CYS 62  391 391 CYS CYS BBB . n 
B 2 63  PHE 63  392 392 PHE PHE BBB . n 
B 2 64  THR 64  393 393 THR THR BBB . n 
B 2 65  ASN 65  394 394 ASN ASN BBB . n 
B 2 66  VAL 66  395 395 VAL VAL BBB . n 
B 2 67  TYR 67  396 396 TYR TYR BBB . n 
B 2 68  ALA 68  397 397 ALA ALA BBB . n 
B 2 69  ASP 69  398 398 ASP ASP BBB . n 
B 2 70  SER 70  399 399 SER SER BBB . n 
B 2 71  PHE 71  400 400 PHE PHE BBB . n 
B 2 72  VAL 72  401 401 VAL VAL BBB . n 
B 2 73  ILE 73  402 402 ILE ILE BBB . n 
B 2 74  ARG 74  403 403 ARG ARG BBB . n 
B 2 75  GLY 75  404 404 GLY GLY BBB . n 
B 2 76  ASP 76  405 405 ASP ASP BBB . n 
B 2 77  GLU 77  406 406 GLU GLU BBB . n 
B 2 78  VAL 78  407 407 VAL VAL BBB . n 
B 2 79  ARG 79  408 408 ARG ARG BBB . n 
B 2 80  GLN 80  409 409 GLN GLN BBB . n 
B 2 81  ILE 81  410 410 ILE ILE BBB . n 
B 2 82  ALA 82  411 411 ALA ALA BBB . n 
B 2 83  PRO 83  412 412 PRO PRO BBB . n 
B 2 84  GLY 84  413 413 GLY GLY BBB . n 
B 2 85  GLN 85  414 414 GLN GLN BBB . n 
B 2 86  THR 86  415 415 THR THR BBB . n 
B 2 87  GLY 87  416 416 GLY GLY BBB . n 
B 2 88  LYS 88  417 417 LYS LYS BBB . n 
B 2 89  ILE 89  418 418 ILE ILE BBB . n 
B 2 90  ALA 90  419 419 ALA ALA BBB . n 
B 2 91  ASP 91  420 420 ASP ASP BBB . n 
B 2 92  TYR 92  421 421 TYR TYR BBB . n 
B 2 93  ASN 93  422 422 ASN ASN BBB . n 
B 2 94  TYR 94  423 423 TYR TYR BBB . n 
B 2 95  LYS 95  424 424 LYS LYS BBB . n 
B 2 96  LEU 96  425 425 LEU LEU BBB . n 
B 2 97  PRO 97  426 426 PRO PRO BBB . n 
B 2 98  ASP 98  427 427 ASP ASP BBB . n 
B 2 99  ASP 99  428 428 ASP ASP BBB . n 
B 2 100 PHE 100 429 429 PHE PHE BBB . n 
B 2 101 THR 101 430 430 THR THR BBB . n 
B 2 102 GLY 102 431 431 GLY GLY BBB . n 
B 2 103 CYS 103 432 432 CYS CYS BBB . n 
B 2 104 VAL 104 433 433 VAL VAL BBB . n 
B 2 105 ILE 105 434 434 ILE ILE BBB . n 
B 2 106 ALA 106 435 435 ALA ALA BBB . n 
B 2 107 TRP 107 436 436 TRP TRP BBB . n 
B 2 108 ASN 108 437 437 ASN ASN BBB . n 
B 2 109 SER 109 438 438 SER SER BBB . n 
B 2 110 ASN 110 439 439 ASN ASN BBB . n 
B 2 111 ASN 111 440 440 ASN ASN BBB . n 
B 2 112 LEU 112 441 441 LEU LEU BBB . n 
B 2 113 ASP 113 442 442 ASP ASP BBB . n 
B 2 114 SER 114 443 443 SER SER BBB . n 
B 2 115 LYS 115 444 444 LYS LYS BBB . n 
B 2 116 VAL 116 445 445 VAL VAL BBB . n 
B 2 117 GLY 117 446 446 GLY GLY BBB . n 
B 2 118 GLY 118 447 447 GLY GLY BBB . n 
B 2 119 ASN 119 448 448 ASN ASN BBB . n 
B 2 120 TYR 120 449 449 TYR TYR BBB . n 
B 2 121 ASN 121 450 450 ASN ASN BBB . n 
B 2 122 TYR 122 451 451 TYR TYR BBB . n 
B 2 123 LEU 123 452 452 LEU LEU BBB . n 
B 2 124 TYR 124 453 453 TYR TYR BBB . n 
B 2 125 ARG 125 454 454 ARG ARG BBB . n 
B 2 126 LEU 126 455 455 LEU LEU BBB . n 
B 2 127 PHE 127 456 456 PHE PHE BBB . n 
B 2 128 ARG 128 457 457 ARG ARG BBB . n 
B 2 129 LYS 129 458 458 LYS LYS BBB . n 
B 2 130 SER 130 459 459 SER SER BBB . n 
B 2 131 ASN 131 460 460 ASN ASN BBB . n 
B 2 132 LEU 132 461 461 LEU LEU BBB . n 
B 2 133 LYS 133 462 462 LYS LYS BBB . n 
B 2 134 PRO 134 463 463 PRO PRO BBB . n 
B 2 135 PHE 135 464 464 PHE PHE BBB . n 
B 2 136 GLU 136 465 465 GLU GLU BBB . n 
B 2 137 ARG 137 466 466 ARG ARG BBB . n 
B 2 138 ASP 138 467 467 ASP ASP BBB . n 
B 2 139 ILE 139 468 468 ILE ILE BBB . n 
B 2 140 SER 140 469 469 SER SER BBB . n 
B 2 141 THR 141 470 470 THR THR BBB . n 
B 2 142 GLU 142 471 471 GLU GLU BBB . n 
B 2 143 ILE 143 472 472 ILE ILE BBB . n 
B 2 144 TYR 144 473 473 TYR TYR BBB . n 
B 2 145 GLN 145 474 474 GLN GLN BBB . n 
B 2 146 ALA 146 475 475 ALA ALA BBB . n 
B 2 147 GLY 147 476 476 GLY GLY BBB . n 
B 2 148 SER 148 477 477 SER SER BBB . n 
B 2 149 THR 149 478 478 THR THR BBB . n 
B 2 150 PRO 150 479 479 PRO PRO BBB . n 
B 2 151 CYS 151 480 480 CYS CYS BBB . n 
B 2 152 ASN 152 481 481 ASN ASN BBB . n 
B 2 153 GLY 153 482 482 GLY GLY BBB . n 
B 2 154 VAL 154 483 483 VAL VAL BBB . n 
B 2 155 GLU 155 484 484 GLU GLU BBB . n 
B 2 156 GLY 156 485 485 GLY GLY BBB . n 
B 2 157 PHE 157 486 486 PHE PHE BBB . n 
B 2 158 ASN 158 487 487 ASN ASN BBB . n 
B 2 159 CYS 159 488 488 CYS CYS BBB . n 
B 2 160 TYR 160 489 489 TYR TYR BBB . n 
B 2 161 PHE 161 490 490 PHE PHE BBB . n 
B 2 162 PRO 162 491 491 PRO PRO BBB . n 
B 2 163 LEU 163 492 492 LEU LEU BBB . n 
B 2 164 GLN 164 493 493 GLN GLN BBB . n 
B 2 165 SER 165 494 494 SER SER BBB . n 
B 2 166 TYR 166 495 495 TYR TYR BBB . n 
B 2 167 GLY 167 496 496 GLY GLY BBB . n 
B 2 168 PHE 168 497 497 PHE PHE BBB . n 
B 2 169 GLN 169 498 498 GLN GLN BBB . n 
B 2 170 PRO 170 499 499 PRO PRO BBB . n 
B 2 171 THR 171 500 500 THR THR BBB . n 
B 2 172 ASN 172 501 501 ASN ASN BBB . n 
B 2 173 GLY 173 502 502 GLY GLY BBB . n 
B 2 174 VAL 174 503 503 VAL VAL BBB . n 
B 2 175 GLY 175 504 504 GLY GLY BBB . n 
B 2 176 TYR 176 505 505 TYR TYR BBB . n 
B 2 177 GLN 177 506 506 GLN GLN BBB . n 
B 2 178 PRO 178 507 507 PRO PRO BBB . n 
B 2 179 TYR 179 508 508 TYR TYR BBB . n 
B 2 180 ARG 180 509 509 ARG ARG BBB . n 
B 2 181 VAL 181 510 510 VAL VAL BBB . n 
B 2 182 VAL 182 511 511 VAL VAL BBB . n 
B 2 183 VAL 183 512 512 VAL VAL BBB . n 
B 2 184 LEU 184 513 513 LEU LEU BBB . n 
B 2 185 SER 185 514 514 SER SER BBB . n 
B 2 186 PHE 186 515 515 PHE PHE BBB . n 
B 2 187 GLU 187 516 516 GLU GLU BBB . n 
B 2 188 LEU 188 517 517 LEU LEU BBB . n 
B 2 189 LEU 189 518 518 LEU LEU BBB . n 
B 2 190 HIS 190 519 519 HIS HIS BBB . n 
B 2 191 ALA 191 520 520 ALA ALA BBB . n 
B 2 192 PRO 192 521 521 PRO PRO BBB . n 
B 2 193 ALA 193 522 522 ALA ALA BBB . n 
B 2 194 THR 194 523 523 THR THR BBB . n 
B 2 195 VAL 195 524 524 VAL VAL BBB . n 
B 2 196 CYS 196 525 525 CYS CYS BBB . n 
B 2 197 GLY 197 526 526 GLY GLY BBB . n 
B 2 198 PRO 198 527 527 PRO PRO BBB . n 
B 2 199 LYS 199 528 528 LYS LYS BBB . n 
B 2 200 LYS 200 529 529 LYS LYS BBB . n 
B 2 201 SER 201 530 ?   ?   ?   BBB . n 
B 2 202 THR 202 531 ?   ?   ?   BBB . n 
B 2 203 ASN 203 532 ?   ?   ?   BBB . n 
B 2 204 LYS 204 533 ?   ?   ?   BBB . n 
B 2 205 HIS 205 534 ?   ?   ?   BBB . n 
B 2 206 HIS 206 535 ?   ?   ?   BBB . n 
B 2 207 HIS 207 536 ?   ?   ?   BBB . n 
B 2 208 HIS 208 537 ?   ?   ?   BBB . n 
B 2 209 HIS 209 538 ?   ?   ?   BBB . n 
B 2 210 HIS 210 539 ?   ?   ?   BBB . n 
C 3 1   MET 1   1   ?   ?   ?   CCC . n 
C 3 2   ALA 2   2   ?   ?   ?   CCC . n 
C 3 3   GLN 3   3   ?   ?   ?   CCC . n 
C 3 4   VAL 4   4   4   VAL VAL CCC . n 
C 3 5   GLN 5   5   5   GLN GLN CCC . n 
C 3 6   LEU 6   6   6   LEU LEU CCC . n 
C 3 7   VAL 7   7   7   VAL VAL CCC . n 
C 3 8   GLU 8   8   8   GLU GLU CCC . n 
C 3 9   SER 9   9   9   SER SER CCC . n 
C 3 10  GLY 10  10  10  GLY GLY CCC . n 
C 3 11  GLY 11  11  11  GLY GLY CCC . n 
C 3 12  GLY 12  12  12  GLY GLY CCC . n 
C 3 13  LEU 13  13  13  LEU LEU CCC . n 
C 3 14  VAL 14  14  14  VAL VAL CCC . n 
C 3 15  LYS 15  15  15  LYS LYS CCC . n 
C 3 16  THR 16  16  16  THR THR CCC . n 
C 3 17  GLY 17  17  17  GLY GLY CCC . n 
C 3 18  GLY 18  18  18  GLY GLY CCC . n 
C 3 19  SER 19  19  19  SER SER CCC . n 
C 3 20  LEU 20  20  20  LEU LEU CCC . n 
C 3 21  ARG 21  21  21  ARG ARG CCC . n 
C 3 22  LEU 22  22  22  LEU LEU CCC . n 
C 3 23  SER 23  23  23  SER SER CCC . n 
C 3 24  CYS 24  24  24  CYS CYS CCC . n 
C 3 25  ALA 25  25  25  ALA ALA CCC . n 
C 3 26  ALA 26  26  26  ALA ALA CCC . n 
C 3 27  SER 27  27  27  SER SER CCC . n 
C 3 28  GLY 28  28  28  GLY GLY CCC . n 
C 3 29  ARG 29  29  29  ARG ARG CCC . n 
C 3 30  THR 30  30  30  THR THR CCC . n 
C 3 31  PHE 31  31  31  PHE PHE CCC . n 
C 3 32  SER 32  32  32  SER SER CCC . n 
C 3 33  THR 33  33  33  THR THR CCC . n 
C 3 34  TYR 34  34  34  TYR TYR CCC . n 
C 3 35  SER 35  35  35  SER SER CCC . n 
C 3 36  MET 36  36  36  MET MET CCC . n 
C 3 37  GLY 37  37  37  GLY GLY CCC . n 
C 3 38  TRP 38  38  38  TRP TRP CCC . n 
C 3 39  PHE 39  39  39  PHE PHE CCC . n 
C 3 40  ARG 40  40  40  ARG ARG CCC . n 
C 3 41  GLN 41  41  41  GLN GLN CCC . n 
C 3 42  ALA 42  42  42  ALA ALA CCC . n 
C 3 43  PRO 43  43  43  PRO PRO CCC . n 
C 3 44  GLY 44  44  44  GLY GLY CCC . n 
C 3 45  LYS 45  45  45  LYS LYS CCC . n 
C 3 46  GLU 46  46  46  GLU GLU CCC . n 
C 3 47  ARG 47  47  47  ARG ARG CCC . n 
C 3 48  GLU 48  48  48  GLU GLU CCC . n 
C 3 49  PHE 49  49  49  PHE PHE CCC . n 
C 3 50  VAL 50  50  50  VAL VAL CCC . n 
C 3 51  ALA 51  51  51  ALA ALA CCC . n 
C 3 52  GLY 52  52  52  GLY GLY CCC . n 
C 3 53  MET 53  53  53  MET MET CCC . n 
C 3 54  ARG 54  54  54  ARG ARG CCC . n 
C 3 55  TRP 55  55  55  TRP TRP CCC . n 
C 3 56  THR 56  56  56  THR THR CCC . n 
C 3 57  GLY 57  57  57  GLY GLY CCC . n 
C 3 58  SER 58  58  58  SER SER CCC . n 
C 3 59  SER 59  59  59  SER SER CCC . n 
C 3 60  THR 60  60  60  THR THR CCC . n 
C 3 61  PHE 61  61  61  PHE PHE CCC . n 
C 3 62  TYR 62  62  62  TYR TYR CCC . n 
C 3 63  SER 63  63  63  SER SER CCC . n 
C 3 64  ASP 64  64  64  ASP ASP CCC . n 
C 3 65  SER 65  65  65  SER SER CCC . n 
C 3 66  VAL 66  66  66  VAL VAL CCC . n 
C 3 67  LYS 67  67  67  LYS LYS CCC . n 
C 3 68  GLY 68  68  68  GLY GLY CCC . n 
C 3 69  ARG 69  69  69  ARG ARG CCC . n 
C 3 70  PHE 70  70  70  PHE PHE CCC . n 
C 3 71  THR 71  71  71  THR THR CCC . n 
C 3 72  VAL 72  72  72  VAL VAL CCC . n 
C 3 73  SER 73  73  73  SER SER CCC . n 
C 3 74  ARG 74  74  74  ARG ARG CCC . n 
C 3 75  ASN 75  75  75  ASN ASN CCC . n 
C 3 76  ASN 76  76  76  ASN ASN CCC . n 
C 3 77  ALA 77  77  77  ALA ALA CCC . n 
C 3 78  LYS 78  78  78  LYS LYS CCC . n 
C 3 79  ASP 79  79  79  ASP ASP CCC . n 
C 3 80  THR 80  80  80  THR THR CCC . n 
C 3 81  VAL 81  81  81  VAL VAL CCC . n 
C 3 82  TYR 82  82  82  TYR TYR CCC . n 
C 3 83  LEU 83  83  83  LEU LEU CCC . n 
C 3 84  HIS 84  84  84  HIS HIS CCC . n 
C 3 85  MET 85  85  85  MET MET CCC . n 
C 3 86  ASN 86  86  86  ASN ASN CCC . n 
C 3 87  SER 87  87  87  SER SER CCC . n 
C 3 88  LEU 88  88  88  LEU LEU CCC . n 
C 3 89  LYS 89  89  89  LYS LYS CCC . n 
C 3 90  PRO 90  90  90  PRO PRO CCC . n 
C 3 91  GLU 91  91  91  GLU GLU CCC . n 
C 3 92  ASP 92  92  92  ASP ASP CCC . n 
C 3 93  THR 93  93  93  THR THR CCC . n 
C 3 94  ALA 94  94  94  ALA ALA CCC . n 
C 3 95  VAL 95  95  95  VAL VAL CCC . n 
C 3 96  TYR 96  96  96  TYR TYR CCC . n 
C 3 97  TYR 97  97  97  TYR TYR CCC . n 
C 3 98  CYS 98  98  98  CYS CYS CCC . n 
C 3 99  ALA 99  99  99  ALA ALA CCC . n 
C 3 100 ILE 100 100 100 ILE ILE CCC . n 
C 3 101 THR 101 101 101 THR THR CCC . n 
C 3 102 THR 102 102 102 THR THR CCC . n 
C 3 103 ILE 103 103 103 ILE ILE CCC . n 
C 3 104 VAL 104 104 104 VAL VAL CCC . n 
C 3 105 ARG 105 105 105 ARG ARG CCC . n 
C 3 106 ALA 106 106 106 ALA ALA CCC . n 
C 3 107 TYR 107 107 107 TYR TYR CCC . n 
C 3 108 TYR 108 108 108 TYR TYR CCC . n 
C 3 109 THR 109 109 109 THR THR CCC . n 
C 3 110 GLU 110 110 110 GLU GLU CCC . n 
C 3 111 TYR 111 111 111 TYR TYR CCC . n 
C 3 112 THR 112 112 112 THR THR CCC . n 
C 3 113 GLU 113 113 113 GLU GLU CCC . n 
C 3 114 ALA 114 114 114 ALA ALA CCC . n 
C 3 115 ASP 115 115 115 ASP ASP CCC . n 
C 3 116 PHE 116 116 116 PHE PHE CCC . n 
C 3 117 GLY 117 117 117 GLY GLY CCC . n 
C 3 118 SER 118 118 118 SER SER CCC . n 
C 3 119 TRP 119 119 119 TRP TRP CCC . n 
C 3 120 GLY 120 120 120 GLY GLY CCC . n 
C 3 121 GLN 121 121 121 GLN GLN CCC . n 
C 3 122 GLY 122 122 122 GLY GLY CCC . n 
C 3 123 THR 123 123 123 THR THR CCC . n 
C 3 124 GLN 124 124 124 GLN GLN CCC . n 
C 3 125 VAL 125 125 125 VAL VAL CCC . n 
C 3 126 THR 126 126 126 THR THR CCC . n 
C 3 127 VAL 127 127 127 VAL VAL CCC . n 
C 3 128 SER 128 128 128 SER SER CCC . n 
C 3 129 SER 129 129 ?   ?   ?   CCC . n 
C 3 130 LYS 130 130 ?   ?   ?   CCC . n 
C 3 131 HIS 131 131 ?   ?   ?   CCC . n 
C 3 132 HIS 132 132 ?   ?   ?   CCC . n 
C 3 133 HIS 133 133 ?   ?   ?   CCC . n 
C 3 134 HIS 134 134 ?   ?   ?   CCC . n 
C 3 135 HIS 135 135 ?   ?   ?   CCC . n 
C 3 136 HIS 136 136 ?   ?   ?   CCC . n 
D 1 1   GLN 1   3   3   GLN GLN DDD . n 
D 1 2   VAL 2   4   4   VAL VAL DDD . n 
D 1 3   GLN 3   5   5   GLN GLN DDD . n 
D 1 4   LEU 4   6   6   LEU LEU DDD . n 
D 1 5   VAL 5   7   7   VAL VAL DDD . n 
D 1 6   GLU 6   8   8   GLU GLU DDD . n 
D 1 7   SER 7   9   9   SER SER DDD . n 
D 1 8   GLY 8   10  10  GLY GLY DDD . n 
D 1 9   GLY 9   11  11  GLY GLY DDD . n 
D 1 10  GLY 10  12  12  GLY GLY DDD . n 
D 1 11  LEU 11  13  13  LEU LEU DDD . n 
D 1 12  VAL 12  14  14  VAL VAL DDD . n 
D 1 13  GLN 13  15  15  GLN GLN DDD . n 
D 1 14  ALA 14  16  16  ALA ALA DDD . n 
D 1 15  GLY 15  17  17  GLY GLY DDD . n 
D 1 16  GLY 16  18  18  GLY GLY DDD . n 
D 1 17  SER 17  19  19  SER SER DDD . n 
D 1 18  LEU 18  20  20  LEU LEU DDD . n 
D 1 19  ARG 19  21  21  ARG ARG DDD . n 
D 1 20  LEU 20  22  22  LEU LEU DDD . n 
D 1 21  SER 21  23  23  SER SER DDD . n 
D 1 22  CYS 22  24  24  CYS CYS DDD . n 
D 1 23  ALA 23  25  25  ALA ALA DDD . n 
D 1 24  ALA 24  26  26  ALA ALA DDD . n 
D 1 25  SER 25  27  27  SER SER DDD . n 
D 1 26  GLY 26  28  28  GLY GLY DDD . n 
D 1 27  GLY 27  29  29  GLY GLY DDD . n 
D 1 28  THR 28  30  30  THR THR DDD . n 
D 1 29  PHE 29  31  31  PHE PHE DDD . n 
D 1 30  SER 30  32  32  SER SER DDD . n 
D 1 31  THR 31  33  33  THR THR DDD . n 
D 1 32  ALA 32  34  34  ALA ALA DDD . n 
D 1 33  ALA 33  35  35  ALA ALA DDD . n 
D 1 34  MET 34  36  36  MET MET DDD . n 
D 1 35  GLY 35  37  37  GLY GLY DDD . n 
D 1 36  TRP 36  38  38  TRP TRP DDD . n 
D 1 37  PHE 37  39  39  PHE PHE DDD . n 
D 1 38  ARG 38  40  40  ARG ARG DDD . n 
D 1 39  GLN 39  41  41  GLN GLN DDD . n 
D 1 40  ALA 40  42  42  ALA ALA DDD . n 
D 1 41  PRO 41  43  43  PRO PRO DDD . n 
D 1 42  GLY 42  44  44  GLY GLY DDD . n 
D 1 43  GLU 43  45  45  GLU GLU DDD . n 
D 1 44  GLU 44  46  46  GLU GLU DDD . n 
D 1 45  ARG 45  47  47  ARG ARG DDD . n 
D 1 46  GLU 46  48  48  GLU GLU DDD . n 
D 1 47  CYS 47  49  49  CYS CYS DDD . n 
D 1 48  VAL 48  50  50  VAL VAL DDD . n 
D 1 49  ALA 49  51  51  ALA ALA DDD . n 
D 1 50  SER 50  52  52  SER SER DDD . n 
D 1 51  ILE 51  53  53  ILE ILE DDD . n 
D 1 52  GLY 52  54  54  GLY GLY DDD . n 
D 1 53  TRP 53  55  55  TRP TRP DDD . n 
D 1 54  ARG 54  56  56  ARG ARG DDD . n 
D 1 55  GLY 55  57  57  GLY GLY DDD . n 
D 1 56  VAL 56  58  58  VAL VAL DDD . n 
D 1 57  ARG 57  59  59  ARG ARG DDD . n 
D 1 58  THR 58  60  60  THR THR DDD . n 
D 1 59  TRP 59  61  61  TRP TRP DDD . n 
D 1 60  TYR 60  62  62  TYR TYR DDD . n 
D 1 61  ALA 61  63  63  ALA ALA DDD . n 
D 1 62  ASP 62  64  64  ASP ASP DDD . n 
D 1 63  SER 63  65  65  SER SER DDD . n 
D 1 64  VAL 64  66  66  VAL VAL DDD . n 
D 1 65  LYS 65  67  67  LYS LYS DDD . n 
D 1 66  GLY 66  68  68  GLY GLY DDD . n 
D 1 67  ARG 67  69  69  ARG ARG DDD . n 
D 1 68  PHE 68  70  70  PHE PHE DDD . n 
D 1 69  THR 69  71  71  THR THR DDD . n 
D 1 70  ILE 70  72  72  ILE ILE DDD . n 
D 1 71  SER 71  73  73  SER SER DDD . n 
D 1 72  ARG 72  74  74  ARG ARG DDD . n 
D 1 73  ASP 73  75  75  ASP ASP DDD . n 
D 1 74  ASN 74  76  76  ASN ASN DDD . n 
D 1 75  PRO 75  77  77  PRO PRO DDD . n 
D 1 76  GLN 76  78  78  GLN GLN DDD . n 
D 1 77  ASN 77  79  79  ASN ASN DDD . n 
D 1 78  THR 78  80  80  THR THR DDD . n 
D 1 79  VAL 79  81  81  VAL VAL DDD . n 
D 1 80  TYR 80  82  82  TYR TYR DDD . n 
D 1 81  LEU 81  83  83  LEU LEU DDD . n 
D 1 82  GLN 82  84  84  GLN GLN DDD . n 
D 1 83  MET 83  85  85  MET MET DDD . n 
D 1 84  ASN 84  86  86  ASN ASN DDD . n 
D 1 85  ASN 85  87  87  ASN ASN DDD . n 
D 1 86  LEU 86  88  88  LEU LEU DDD . n 
D 1 87  LYS 87  89  89  LYS LYS DDD . n 
D 1 88  SER 88  90  90  SER SER DDD . n 
D 1 89  GLY 89  91  91  GLY GLY DDD . n 
D 1 90  ASP 90  92  92  ASP ASP DDD . n 
D 1 91  THR 91  93  93  THR THR DDD . n 
D 1 92  ALA 92  94  94  ALA ALA DDD . n 
D 1 93  VAL 93  95  95  VAL VAL DDD . n 
D 1 94  TYR 94  96  96  TYR TYR DDD . n 
D 1 95  TYR 95  97  97  TYR TYR DDD . n 
D 1 96  CYS 96  98  98  CYS CYS DDD . n 
D 1 97  ALA 97  99  99  ALA ALA DDD . n 
D 1 98  ALA 98  100 100 ALA ALA DDD . n 
D 1 99  SER 99  101 101 SER SER DDD . n 
D 1 100 VAL 100 102 102 VAL VAL DDD . n 
D 1 101 GLY 101 103 103 GLY GLY DDD . n 
D 1 102 ASN 102 104 104 ASN ASN DDD . n 
D 1 103 TYR 103 105 105 TYR TYR DDD . n 
D 1 104 GLY 104 106 106 GLY GLY DDD . n 
D 1 105 LEU 105 107 107 LEU LEU DDD . n 
D 1 106 PRO 106 108 108 PRO PRO DDD . n 
D 1 107 TRP 107 109 109 TRP TRP DDD . n 
D 1 108 ALA 108 110 110 ALA ALA DDD . n 
D 1 109 HIS 109 111 111 HIS HIS DDD . n 
D 1 110 PHE 110 112 112 PHE PHE DDD . n 
D 1 111 GLU 111 113 113 GLU GLU DDD . n 
D 1 112 TYR 112 114 114 TYR TYR DDD . n 
D 1 113 ASP 113 115 115 ASP ASP DDD . n 
D 1 114 PHE 114 116 116 PHE PHE DDD . n 
D 1 115 TRP 115 117 117 TRP TRP DDD . n 
D 1 116 GLY 116 118 118 GLY GLY DDD . n 
D 1 117 GLN 117 119 119 GLN GLN DDD . n 
D 1 118 GLY 118 120 120 GLY GLY DDD . n 
D 1 119 ILE 119 121 121 ILE ILE DDD . n 
D 1 120 GLN 120 122 122 GLN GLN DDD . n 
D 1 121 VAL 121 123 123 VAL VAL DDD . n 
D 1 122 THR 122 124 124 THR THR DDD . n 
D 1 123 VAL 123 125 125 VAL VAL DDD . n 
D 1 124 SER 124 126 ?   ?   ?   DDD . n 
D 1 125 SER 125 127 ?   ?   ?   DDD . n 
D 1 126 LYS 126 128 ?   ?   ?   DDD . n 
D 1 127 HIS 127 129 ?   ?   ?   DDD . n 
D 1 128 HIS 128 130 ?   ?   ?   DDD . n 
D 1 129 HIS 129 131 ?   ?   ?   DDD . n 
D 1 130 HIS 130 132 ?   ?   ?   DDD . n 
D 1 131 HIS 131 133 ?   ?   ?   DDD . n 
D 1 132 HIS 132 134 ?   ?   ?   DDD . n 
E 2 1   PRO 1   330 ?   ?   ?   EEE . n 
E 2 2   ASN 2   331 ?   ?   ?   EEE . n 
E 2 3   ILE 3   332 ?   ?   ?   EEE . n 
E 2 4   THR 4   333 ?   ?   ?   EEE . n 
E 2 5   ASN 5   334 334 ASN ASN EEE . n 
E 2 6   LEU 6   335 335 LEU LEU EEE . n 
E 2 7   CYS 7   336 336 CYS CYS EEE . n 
E 2 8   PRO 8   337 337 PRO PRO EEE . n 
E 2 9   PHE 9   338 338 PHE PHE EEE . n 
E 2 10  GLY 10  339 339 GLY GLY EEE . n 
E 2 11  GLU 11  340 340 GLU GLU EEE . n 
E 2 12  VAL 12  341 341 VAL VAL EEE . n 
E 2 13  PHE 13  342 342 PHE PHE EEE . n 
E 2 14  ASN 14  343 343 ASN ASN EEE . n 
E 2 15  ALA 15  344 344 ALA ALA EEE . n 
E 2 16  THR 16  345 345 THR THR EEE . n 
E 2 17  ARG 17  346 346 ARG ARG EEE . n 
E 2 18  PHE 18  347 347 PHE PHE EEE . n 
E 2 19  ALA 19  348 348 ALA ALA EEE . n 
E 2 20  SER 20  349 349 SER SER EEE . n 
E 2 21  VAL 21  350 350 VAL VAL EEE . n 
E 2 22  TYR 22  351 351 TYR TYR EEE . n 
E 2 23  ALA 23  352 352 ALA ALA EEE . n 
E 2 24  TRP 24  353 353 TRP TRP EEE . n 
E 2 25  ASN 25  354 354 ASN ASN EEE . n 
E 2 26  ARG 26  355 355 ARG ARG EEE . n 
E 2 27  LYS 27  356 356 LYS LYS EEE . n 
E 2 28  ARG 28  357 357 ARG ARG EEE . n 
E 2 29  ILE 29  358 358 ILE ILE EEE . n 
E 2 30  SER 30  359 359 SER SER EEE . n 
E 2 31  ASN 31  360 360 ASN ASN EEE . n 
E 2 32  CYS 32  361 361 CYS CYS EEE . n 
E 2 33  VAL 33  362 362 VAL VAL EEE . n 
E 2 34  ALA 34  363 363 ALA ALA EEE . n 
E 2 35  ASP 35  364 364 ASP ASP EEE . n 
E 2 36  TYR 36  365 365 TYR TYR EEE . n 
E 2 37  SER 37  366 366 SER SER EEE . n 
E 2 38  VAL 38  367 367 VAL VAL EEE . n 
E 2 39  LEU 39  368 368 LEU LEU EEE . n 
E 2 40  TYR 40  369 369 TYR TYR EEE . n 
E 2 41  ASN 41  370 370 ASN ASN EEE . n 
E 2 42  SER 42  371 371 SER SER EEE . n 
E 2 43  ALA 43  372 372 ALA ALA EEE . n 
E 2 44  SER 44  373 373 SER SER EEE . n 
E 2 45  PHE 45  374 374 PHE PHE EEE . n 
E 2 46  SER 46  375 375 SER SER EEE . n 
E 2 47  THR 47  376 376 THR THR EEE . n 
E 2 48  PHE 48  377 377 PHE PHE EEE . n 
E 2 49  LYS 49  378 378 LYS LYS EEE . n 
E 2 50  CYS 50  379 379 CYS CYS EEE . n 
E 2 51  TYR 51  380 380 TYR TYR EEE . n 
E 2 52  GLY 52  381 381 GLY GLY EEE . n 
E 2 53  VAL 53  382 382 VAL VAL EEE . n 
E 2 54  SER 54  383 383 SER SER EEE . n 
E 2 55  PRO 55  384 384 PRO PRO EEE . n 
E 2 56  THR 56  385 385 THR THR EEE . n 
E 2 57  LYS 57  386 386 LYS LYS EEE . n 
E 2 58  LEU 58  387 387 LEU LEU EEE . n 
E 2 59  ASN 59  388 388 ASN ASN EEE . n 
E 2 60  ASP 60  389 389 ASP ASP EEE . n 
E 2 61  LEU 61  390 390 LEU LEU EEE . n 
E 2 62  CYS 62  391 391 CYS CYS EEE . n 
E 2 63  PHE 63  392 392 PHE PHE EEE . n 
E 2 64  THR 64  393 393 THR THR EEE . n 
E 2 65  ASN 65  394 394 ASN ASN EEE . n 
E 2 66  VAL 66  395 395 VAL VAL EEE . n 
E 2 67  TYR 67  396 396 TYR TYR EEE . n 
E 2 68  ALA 68  397 397 ALA ALA EEE . n 
E 2 69  ASP 69  398 398 ASP ASP EEE . n 
E 2 70  SER 70  399 399 SER SER EEE . n 
E 2 71  PHE 71  400 400 PHE PHE EEE . n 
E 2 72  VAL 72  401 401 VAL VAL EEE . n 
E 2 73  ILE 73  402 402 ILE ILE EEE . n 
E 2 74  ARG 74  403 403 ARG ARG EEE . n 
E 2 75  GLY 75  404 404 GLY GLY EEE . n 
E 2 76  ASP 76  405 405 ASP ASP EEE . n 
E 2 77  GLU 77  406 406 GLU GLU EEE . n 
E 2 78  VAL 78  407 407 VAL VAL EEE . n 
E 2 79  ARG 79  408 408 ARG ARG EEE . n 
E 2 80  GLN 80  409 409 GLN GLN EEE . n 
E 2 81  ILE 81  410 410 ILE ILE EEE . n 
E 2 82  ALA 82  411 411 ALA ALA EEE . n 
E 2 83  PRO 83  412 412 PRO PRO EEE . n 
E 2 84  GLY 84  413 413 GLY GLY EEE . n 
E 2 85  GLN 85  414 414 GLN GLN EEE . n 
E 2 86  THR 86  415 415 THR THR EEE . n 
E 2 87  GLY 87  416 416 GLY GLY EEE . n 
E 2 88  LYS 88  417 417 LYS LYS EEE . n 
E 2 89  ILE 89  418 418 ILE ILE EEE . n 
E 2 90  ALA 90  419 419 ALA ALA EEE . n 
E 2 91  ASP 91  420 420 ASP ASP EEE . n 
E 2 92  TYR 92  421 421 TYR TYR EEE . n 
E 2 93  ASN 93  422 422 ASN ASN EEE . n 
E 2 94  TYR 94  423 423 TYR TYR EEE . n 
E 2 95  LYS 95  424 424 LYS LYS EEE . n 
E 2 96  LEU 96  425 425 LEU LEU EEE . n 
E 2 97  PRO 97  426 426 PRO PRO EEE . n 
E 2 98  ASP 98  427 427 ASP ASP EEE . n 
E 2 99  ASP 99  428 428 ASP ASP EEE . n 
E 2 100 PHE 100 429 429 PHE PHE EEE . n 
E 2 101 THR 101 430 430 THR THR EEE . n 
E 2 102 GLY 102 431 431 GLY GLY EEE . n 
E 2 103 CYS 103 432 432 CYS CYS EEE . n 
E 2 104 VAL 104 433 433 VAL VAL EEE . n 
E 2 105 ILE 105 434 434 ILE ILE EEE . n 
E 2 106 ALA 106 435 435 ALA ALA EEE . n 
E 2 107 TRP 107 436 436 TRP TRP EEE . n 
E 2 108 ASN 108 437 437 ASN ASN EEE . n 
E 2 109 SER 109 438 438 SER SER EEE . n 
E 2 110 ASN 110 439 439 ASN ASN EEE . n 
E 2 111 ASN 111 440 440 ASN ASN EEE . n 
E 2 112 LEU 112 441 441 LEU LEU EEE . n 
E 2 113 ASP 113 442 442 ASP ASP EEE . n 
E 2 114 SER 114 443 443 SER SER EEE . n 
E 2 115 LYS 115 444 444 LYS LYS EEE . n 
E 2 116 VAL 116 445 445 VAL VAL EEE . n 
E 2 117 GLY 117 446 446 GLY GLY EEE . n 
E 2 118 GLY 118 447 447 GLY GLY EEE . n 
E 2 119 ASN 119 448 448 ASN ASN EEE . n 
E 2 120 TYR 120 449 449 TYR TYR EEE . n 
E 2 121 ASN 121 450 450 ASN ASN EEE . n 
E 2 122 TYR 122 451 451 TYR TYR EEE . n 
E 2 123 LEU 123 452 452 LEU LEU EEE . n 
E 2 124 TYR 124 453 453 TYR TYR EEE . n 
E 2 125 ARG 125 454 454 ARG ARG EEE . n 
E 2 126 LEU 126 455 455 LEU LEU EEE . n 
E 2 127 PHE 127 456 456 PHE PHE EEE . n 
E 2 128 ARG 128 457 457 ARG ARG EEE . n 
E 2 129 LYS 129 458 458 LYS LYS EEE . n 
E 2 130 SER 130 459 459 SER SER EEE . n 
E 2 131 ASN 131 460 460 ASN ASN EEE . n 
E 2 132 LEU 132 461 461 LEU LEU EEE . n 
E 2 133 LYS 133 462 462 LYS LYS EEE . n 
E 2 134 PRO 134 463 463 PRO PRO EEE . n 
E 2 135 PHE 135 464 464 PHE PHE EEE . n 
E 2 136 GLU 136 465 465 GLU GLU EEE . n 
E 2 137 ARG 137 466 466 ARG ARG EEE . n 
E 2 138 ASP 138 467 467 ASP ASP EEE . n 
E 2 139 ILE 139 468 468 ILE ILE EEE . n 
E 2 140 SER 140 469 469 SER SER EEE . n 
E 2 141 THR 141 470 470 THR THR EEE . n 
E 2 142 GLU 142 471 471 GLU GLU EEE . n 
E 2 143 ILE 143 472 472 ILE ILE EEE . n 
E 2 144 TYR 144 473 473 TYR TYR EEE . n 
E 2 145 GLN 145 474 474 GLN GLN EEE . n 
E 2 146 ALA 146 475 475 ALA ALA EEE . n 
E 2 147 GLY 147 476 476 GLY GLY EEE . n 
E 2 148 SER 148 477 477 SER SER EEE . n 
E 2 149 THR 149 478 478 THR THR EEE . n 
E 2 150 PRO 150 479 479 PRO PRO EEE . n 
E 2 151 CYS 151 480 480 CYS CYS EEE . n 
E 2 152 ASN 152 481 481 ASN ASN EEE . n 
E 2 153 GLY 153 482 482 GLY GLY EEE . n 
E 2 154 VAL 154 483 483 VAL VAL EEE . n 
E 2 155 GLU 155 484 484 GLU GLU EEE . n 
E 2 156 GLY 156 485 485 GLY GLY EEE . n 
E 2 157 PHE 157 486 486 PHE PHE EEE . n 
E 2 158 ASN 158 487 487 ASN ASN EEE . n 
E 2 159 CYS 159 488 488 CYS CYS EEE . n 
E 2 160 TYR 160 489 489 TYR TYR EEE . n 
E 2 161 PHE 161 490 490 PHE PHE EEE . n 
E 2 162 PRO 162 491 491 PRO PRO EEE . n 
E 2 163 LEU 163 492 492 LEU LEU EEE . n 
E 2 164 GLN 164 493 493 GLN GLN EEE . n 
E 2 165 SER 165 494 494 SER SER EEE . n 
E 2 166 TYR 166 495 495 TYR TYR EEE . n 
E 2 167 GLY 167 496 496 GLY GLY EEE . n 
E 2 168 PHE 168 497 497 PHE PHE EEE . n 
E 2 169 GLN 169 498 498 GLN GLN EEE . n 
E 2 170 PRO 170 499 499 PRO PRO EEE . n 
E 2 171 THR 171 500 500 THR THR EEE . n 
E 2 172 ASN 172 501 501 ASN ASN EEE . n 
E 2 173 GLY 173 502 502 GLY GLY EEE . n 
E 2 174 VAL 174 503 503 VAL VAL EEE . n 
E 2 175 GLY 175 504 504 GLY GLY EEE . n 
E 2 176 TYR 176 505 505 TYR TYR EEE . n 
E 2 177 GLN 177 506 506 GLN GLN EEE . n 
E 2 178 PRO 178 507 507 PRO PRO EEE . n 
E 2 179 TYR 179 508 508 TYR TYR EEE . n 
E 2 180 ARG 180 509 509 ARG ARG EEE . n 
E 2 181 VAL 181 510 510 VAL VAL EEE . n 
E 2 182 VAL 182 511 511 VAL VAL EEE . n 
E 2 183 VAL 183 512 512 VAL VAL EEE . n 
E 2 184 LEU 184 513 513 LEU LEU EEE . n 
E 2 185 SER 185 514 514 SER SER EEE . n 
E 2 186 PHE 186 515 515 PHE PHE EEE . n 
E 2 187 GLU 187 516 516 GLU GLU EEE . n 
E 2 188 LEU 188 517 517 LEU LEU EEE . n 
E 2 189 LEU 189 518 518 LEU LEU EEE . n 
E 2 190 HIS 190 519 519 HIS HIS EEE . n 
E 2 191 ALA 191 520 520 ALA ALA EEE . n 
E 2 192 PRO 192 521 521 PRO PRO EEE . n 
E 2 193 ALA 193 522 522 ALA ALA EEE . n 
E 2 194 THR 194 523 523 THR THR EEE . n 
E 2 195 VAL 195 524 524 VAL VAL EEE . n 
E 2 196 CYS 196 525 525 CYS CYS EEE . n 
E 2 197 GLY 197 526 526 GLY GLY EEE . n 
E 2 198 PRO 198 527 527 PRO PRO EEE . n 
E 2 199 LYS 199 528 528 LYS LYS EEE . n 
E 2 200 LYS 200 529 529 LYS LYS EEE . n 
E 2 201 SER 201 530 ?   ?   ?   EEE . n 
E 2 202 THR 202 531 ?   ?   ?   EEE . n 
E 2 203 ASN 203 532 ?   ?   ?   EEE . n 
E 2 204 LYS 204 533 ?   ?   ?   EEE . n 
E 2 205 HIS 205 534 ?   ?   ?   EEE . n 
E 2 206 HIS 206 535 ?   ?   ?   EEE . n 
E 2 207 HIS 207 536 ?   ?   ?   EEE . n 
E 2 208 HIS 208 537 ?   ?   ?   EEE . n 
E 2 209 HIS 209 538 ?   ?   ?   EEE . n 
E 2 210 HIS 210 539 ?   ?   ?   EEE . n 
F 3 1   MET 1   1   ?   ?   ?   FFF . n 
F 3 2   ALA 2   2   ?   ?   ?   FFF . n 
F 3 3   GLN 3   3   3   GLN GLN FFF . n 
F 3 4   VAL 4   4   4   VAL VAL FFF . n 
F 3 5   GLN 5   5   5   GLN GLN FFF . n 
F 3 6   LEU 6   6   6   LEU LEU FFF . n 
F 3 7   VAL 7   7   7   VAL VAL FFF . n 
F 3 8   GLU 8   8   8   GLU GLU FFF . n 
F 3 9   SER 9   9   9   SER SER FFF . n 
F 3 10  GLY 10  10  10  GLY GLY FFF . n 
F 3 11  GLY 11  11  11  GLY GLY FFF . n 
F 3 12  GLY 12  12  12  GLY GLY FFF . n 
F 3 13  LEU 13  13  13  LEU LEU FFF . n 
F 3 14  VAL 14  14  14  VAL VAL FFF . n 
F 3 15  LYS 15  15  15  LYS LYS FFF . n 
F 3 16  THR 16  16  16  THR THR FFF . n 
F 3 17  GLY 17  17  17  GLY GLY FFF . n 
F 3 18  GLY 18  18  18  GLY GLY FFF . n 
F 3 19  SER 19  19  19  SER SER FFF . n 
F 3 20  LEU 20  20  20  LEU LEU FFF . n 
F 3 21  ARG 21  21  21  ARG ARG FFF . n 
F 3 22  LEU 22  22  22  LEU LEU FFF . n 
F 3 23  SER 23  23  23  SER SER FFF . n 
F 3 24  CYS 24  24  24  CYS CYS FFF . n 
F 3 25  ALA 25  25  25  ALA ALA FFF . n 
F 3 26  ALA 26  26  26  ALA ALA FFF . n 
F 3 27  SER 27  27  27  SER SER FFF . n 
F 3 28  GLY 28  28  28  GLY GLY FFF . n 
F 3 29  ARG 29  29  29  ARG ARG FFF . n 
F 3 30  THR 30  30  30  THR THR FFF . n 
F 3 31  PHE 31  31  31  PHE PHE FFF . n 
F 3 32  SER 32  32  32  SER SER FFF . n 
F 3 33  THR 33  33  33  THR THR FFF . n 
F 3 34  TYR 34  34  34  TYR TYR FFF . n 
F 3 35  SER 35  35  35  SER SER FFF . n 
F 3 36  MET 36  36  36  MET MET FFF . n 
F 3 37  GLY 37  37  37  GLY GLY FFF . n 
F 3 38  TRP 38  38  38  TRP TRP FFF . n 
F 3 39  PHE 39  39  39  PHE PHE FFF . n 
F 3 40  ARG 40  40  40  ARG ARG FFF . n 
F 3 41  GLN 41  41  41  GLN GLN FFF . n 
F 3 42  ALA 42  42  42  ALA ALA FFF . n 
F 3 43  PRO 43  43  43  PRO PRO FFF . n 
F 3 44  GLY 44  44  44  GLY GLY FFF . n 
F 3 45  LYS 45  45  45  LYS LYS FFF . n 
F 3 46  GLU 46  46  46  GLU GLU FFF . n 
F 3 47  ARG 47  47  47  ARG ARG FFF . n 
F 3 48  GLU 48  48  48  GLU GLU FFF . n 
F 3 49  PHE 49  49  49  PHE PHE FFF . n 
F 3 50  VAL 50  50  50  VAL VAL FFF . n 
F 3 51  ALA 51  51  51  ALA ALA FFF . n 
F 3 52  GLY 52  52  52  GLY GLY FFF . n 
F 3 53  MET 53  53  53  MET MET FFF . n 
F 3 54  ARG 54  54  54  ARG ARG FFF . n 
F 3 55  TRP 55  55  55  TRP TRP FFF . n 
F 3 56  THR 56  56  56  THR THR FFF . n 
F 3 57  GLY 57  57  57  GLY GLY FFF . n 
F 3 58  SER 58  58  58  SER SER FFF . n 
F 3 59  SER 59  59  59  SER SER FFF . n 
F 3 60  THR 60  60  60  THR THR FFF . n 
F 3 61  PHE 61  61  61  PHE PHE FFF . n 
F 3 62  TYR 62  62  62  TYR TYR FFF . n 
F 3 63  SER 63  63  63  SER SER FFF . n 
F 3 64  ASP 64  64  64  ASP ASP FFF . n 
F 3 65  SER 65  65  65  SER SER FFF . n 
F 3 66  VAL 66  66  66  VAL VAL FFF . n 
F 3 67  LYS 67  67  67  LYS LYS FFF . n 
F 3 68  GLY 68  68  68  GLY GLY FFF . n 
F 3 69  ARG 69  69  69  ARG ARG FFF . n 
F 3 70  PHE 70  70  70  PHE PHE FFF . n 
F 3 71  THR 71  71  71  THR THR FFF . n 
F 3 72  VAL 72  72  72  VAL VAL FFF . n 
F 3 73  SER 73  73  73  SER SER FFF . n 
F 3 74  ARG 74  74  74  ARG ARG FFF . n 
F 3 75  ASN 75  75  75  ASN ASN FFF . n 
F 3 76  ASN 76  76  76  ASN ASN FFF . n 
F 3 77  ALA 77  77  77  ALA ALA FFF . n 
F 3 78  LYS 78  78  78  LYS LYS FFF . n 
F 3 79  ASP 79  79  79  ASP ASP FFF . n 
F 3 80  THR 80  80  80  THR THR FFF . n 
F 3 81  VAL 81  81  81  VAL VAL FFF . n 
F 3 82  TYR 82  82  82  TYR TYR FFF . n 
F 3 83  LEU 83  83  83  LEU LEU FFF . n 
F 3 84  HIS 84  84  84  HIS HIS FFF . n 
F 3 85  MET 85  85  85  MET MET FFF . n 
F 3 86  ASN 86  86  86  ASN ASN FFF . n 
F 3 87  SER 87  87  87  SER SER FFF . n 
F 3 88  LEU 88  88  88  LEU LEU FFF . n 
F 3 89  LYS 89  89  89  LYS LYS FFF . n 
F 3 90  PRO 90  90  90  PRO PRO FFF . n 
F 3 91  GLU 91  91  91  GLU GLU FFF . n 
F 3 92  ASP 92  92  92  ASP ASP FFF . n 
F 3 93  THR 93  93  93  THR THR FFF . n 
F 3 94  ALA 94  94  94  ALA ALA FFF . n 
F 3 95  VAL 95  95  95  VAL VAL FFF . n 
F 3 96  TYR 96  96  96  TYR TYR FFF . n 
F 3 97  TYR 97  97  97  TYR TYR FFF . n 
F 3 98  CYS 98  98  98  CYS CYS FFF . n 
F 3 99  ALA 99  99  99  ALA ALA FFF . n 
F 3 100 ILE 100 100 100 ILE ILE FFF . n 
F 3 101 THR 101 101 101 THR THR FFF . n 
F 3 102 THR 102 102 102 THR THR FFF . n 
F 3 103 ILE 103 103 103 ILE ILE FFF . n 
F 3 104 VAL 104 104 104 VAL VAL FFF . n 
F 3 105 ARG 105 105 105 ARG ARG FFF . n 
F 3 106 ALA 106 106 106 ALA ALA FFF . n 
F 3 107 TYR 107 107 107 TYR TYR FFF . n 
F 3 108 TYR 108 108 108 TYR TYR FFF . n 
F 3 109 THR 109 109 109 THR THR FFF . n 
F 3 110 GLU 110 110 110 GLU GLU FFF . n 
F 3 111 TYR 111 111 111 TYR TYR FFF . n 
F 3 112 THR 112 112 112 THR THR FFF . n 
F 3 113 GLU 113 113 113 GLU GLU FFF . n 
F 3 114 ALA 114 114 114 ALA ALA FFF . n 
F 3 115 ASP 115 115 115 ASP ASP FFF . n 
F 3 116 PHE 116 116 116 PHE PHE FFF . n 
F 3 117 GLY 117 117 117 GLY GLY FFF . n 
F 3 118 SER 118 118 118 SER SER FFF . n 
F 3 119 TRP 119 119 119 TRP TRP FFF . n 
F 3 120 GLY 120 120 120 GLY GLY FFF . n 
F 3 121 GLN 121 121 121 GLN GLN FFF . n 
F 3 122 GLY 122 122 122 GLY GLY FFF . n 
F 3 123 THR 123 123 123 THR THR FFF . n 
F 3 124 GLN 124 124 124 GLN GLN FFF . n 
F 3 125 VAL 125 125 125 VAL VAL FFF . n 
F 3 126 THR 126 126 126 THR THR FFF . n 
F 3 127 VAL 127 127 127 VAL VAL FFF . n 
F 3 128 SER 128 128 128 SER SER FFF . n 
F 3 129 SER 129 129 129 SER SER FFF . n 
F 3 130 LYS 130 130 ?   ?   ?   FFF . n 
F 3 131 HIS 131 131 ?   ?   ?   FFF . n 
F 3 132 HIS 132 132 ?   ?   ?   FFF . n 
F 3 133 HIS 133 133 ?   ?   ?   FFF . n 
F 3 134 HIS 134 134 ?   ?   ?   FFF . n 
F 3 135 HIS 135 135 ?   ?   ?   FFF . n 
F 3 136 HIS 136 136 ?   ?   ?   FFF . 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 
G 4 NAG 1  601 530 NAG NAG BBB . 
H 4 NAG 1  601 635 NAG NAG EEE . 
I 5 MES 1  602 1   MES MES EEE . 
J 6 HOH 1  201 70  HOH HOH AAA . 
J 6 HOH 2  202 32  HOH HOH AAA . 
J 6 HOH 3  203 97  HOH HOH AAA . 
J 6 HOH 4  204 4   HOH HOH AAA . 
J 6 HOH 5  205 16  HOH HOH AAA . 
J 6 HOH 6  206 16  HOH HOH AAA . 
J 6 HOH 7  207 59  HOH HOH AAA . 
J 6 HOH 8  208 9   HOH HOH AAA . 
J 6 HOH 9  209 12  HOH HOH AAA . 
J 6 HOH 10 210 2   HOH HOH AAA . 
J 6 HOH 11 211 28  HOH HOH AAA . 
J 6 HOH 12 212 8   HOH HOH AAA . 
J 6 HOH 13 213 13  HOH HOH AAA . 
J 6 HOH 14 214 9   HOH HOH AAA . 
J 6 HOH 15 215 11  HOH HOH AAA . 
J 6 HOH 16 216 10  HOH HOH AAA . 
K 6 HOH 1  701 19  HOH HOH BBB . 
K 6 HOH 2  702 14  HOH HOH BBB . 
K 6 HOH 3  703 20  HOH HOH BBB . 
K 6 HOH 4  704 28  HOH HOH BBB . 
K 6 HOH 5  705 31  HOH HOH BBB . 
K 6 HOH 6  706 15  HOH HOH BBB . 
K 6 HOH 7  707 48  HOH HOH BBB . 
K 6 HOH 8  708 62  HOH HOH BBB . 
K 6 HOH 9  709 20  HOH HOH BBB . 
K 6 HOH 10 710 35  HOH HOH BBB . 
K 6 HOH 11 711 32  HOH HOH BBB . 
K 6 HOH 12 712 56  HOH HOH BBB . 
K 6 HOH 13 713 8   HOH HOH BBB . 
K 6 HOH 14 714 63  HOH HOH BBB . 
K 6 HOH 15 715 22  HOH HOH BBB . 
K 6 HOH 16 716 113 HOH HOH BBB . 
K 6 HOH 17 717 36  HOH HOH BBB . 
K 6 HOH 18 718 52  HOH HOH BBB . 
K 6 HOH 19 719 46  HOH HOH BBB . 
K 6 HOH 20 720 8   HOH HOH BBB . 
K 6 HOH 21 721 9   HOH HOH BBB . 
K 6 HOH 22 722 1   HOH HOH BBB . 
K 6 HOH 23 723 25  HOH HOH BBB . 
K 6 HOH 24 724 49  HOH HOH BBB . 
K 6 HOH 25 725 91  HOH HOH BBB . 
K 6 HOH 26 726 47  HOH HOH BBB . 
K 6 HOH 27 727 33  HOH HOH BBB . 
K 6 HOH 28 728 3   HOH HOH BBB . 
K 6 HOH 29 729 51  HOH HOH BBB . 
K 6 HOH 30 730 34  HOH HOH BBB . 
K 6 HOH 31 731 102 HOH HOH BBB . 
K 6 HOH 32 732 29  HOH HOH BBB . 
K 6 HOH 33 733 15  HOH HOH BBB . 
K 6 HOH 34 734 13  HOH HOH BBB . 
K 6 HOH 35 735 76  HOH HOH BBB . 
K 6 HOH 36 736 82  HOH HOH BBB . 
K 6 HOH 37 737 60  HOH HOH BBB . 
K 6 HOH 38 738 27  HOH HOH BBB . 
K 6 HOH 39 739 48  HOH HOH BBB . 
K 6 HOH 40 740 17  HOH HOH BBB . 
K 6 HOH 41 741 13  HOH HOH BBB . 
K 6 HOH 42 742 104 HOH HOH BBB . 
K 6 HOH 43 743 99  HOH HOH BBB . 
K 6 HOH 44 744 43  HOH HOH BBB . 
K 6 HOH 45 745 74  HOH HOH BBB . 
K 6 HOH 46 746 108 HOH HOH BBB . 
K 6 HOH 47 747 71  HOH HOH BBB . 
K 6 HOH 48 748 17  HOH HOH BBB . 
K 6 HOH 49 749 100 HOH HOH BBB . 
K 6 HOH 50 750 3   HOH HOH BBB . 
K 6 HOH 51 751 65  HOH HOH BBB . 
K 6 HOH 52 752 57  HOH HOH BBB . 
K 6 HOH 53 753 90  HOH HOH BBB . 
K 6 HOH 54 754 15  HOH HOH BBB . 
K 6 HOH 55 755 40  HOH HOH BBB . 
K 6 HOH 56 756 36  HOH HOH BBB . 
K 6 HOH 57 757 30  HOH HOH BBB . 
K 6 HOH 58 758 7   HOH HOH BBB . 
K 6 HOH 59 759 85  HOH HOH BBB . 
K 6 HOH 60 760 22  HOH HOH BBB . 
K 6 HOH 61 761 18  HOH HOH BBB . 
K 6 HOH 62 762 21  HOH HOH BBB . 
K 6 HOH 63 763 47  HOH HOH BBB . 
K 6 HOH 64 764 51  HOH HOH BBB . 
K 6 HOH 65 765 16  HOH HOH BBB . 
L 6 HOH 1  201 23  HOH HOH CCC . 
L 6 HOH 2  202 28  HOH HOH CCC . 
L 6 HOH 3  203 21  HOH HOH CCC . 
L 6 HOH 4  204 40  HOH HOH CCC . 
L 6 HOH 5  205 72  HOH HOH CCC . 
L 6 HOH 6  206 35  HOH HOH CCC . 
L 6 HOH 7  207 111 HOH HOH CCC . 
L 6 HOH 8  208 75  HOH HOH CCC . 
L 6 HOH 9  209 88  HOH HOH CCC . 
L 6 HOH 10 210 29  HOH HOH CCC . 
L 6 HOH 11 211 11  HOH HOH CCC . 
L 6 HOH 12 212 26  HOH HOH CCC . 
L 6 HOH 13 213 46  HOH HOH CCC . 
L 6 HOH 14 214 41  HOH HOH CCC . 
L 6 HOH 15 215 103 HOH HOH CCC . 
L 6 HOH 16 216 62  HOH HOH CCC . 
L 6 HOH 17 217 86  HOH HOH CCC . 
L 6 HOH 18 218 27  HOH HOH CCC . 
L 6 HOH 19 219 89  HOH HOH CCC . 
L 6 HOH 20 220 73  HOH HOH CCC . 
L 6 HOH 21 221 5   HOH HOH CCC . 
L 6 HOH 22 222 66  HOH HOH CCC . 
L 6 HOH 23 223 26  HOH HOH CCC . 
L 6 HOH 24 224 83  HOH HOH CCC . 
L 6 HOH 25 225 24  HOH HOH CCC . 
L 6 HOH 26 226 25  HOH HOH CCC . 
M 6 HOH 1  201 44  HOH HOH DDD . 
M 6 HOH 2  202 60  HOH HOH DDD . 
M 6 HOH 3  203 101 HOH HOH DDD . 
M 6 HOH 4  204 34  HOH HOH DDD . 
M 6 HOH 5  205 43  HOH HOH DDD . 
N 6 HOH 1  701 18  HOH HOH EEE . 
N 6 HOH 2  702 40  HOH HOH EEE . 
N 6 HOH 3  703 69  HOH HOH EEE . 
N 6 HOH 4  704 44  HOH HOH EEE . 
N 6 HOH 5  705 31  HOH HOH EEE . 
N 6 HOH 6  706 19  HOH HOH EEE . 
N 6 HOH 7  707 81  HOH HOH EEE . 
N 6 HOH 8  708 12  HOH HOH EEE . 
N 6 HOH 9  709 78  HOH HOH EEE . 
N 6 HOH 10 710 50  HOH HOH EEE . 
N 6 HOH 11 711 1   HOH HOH EEE . 
N 6 HOH 12 712 42  HOH HOH EEE . 
N 6 HOH 13 713 24  HOH HOH EEE . 
N 6 HOH 14 714 34  HOH HOH EEE . 
N 6 HOH 15 715 37  HOH HOH EEE . 
N 6 HOH 16 716 59  HOH HOH EEE . 
N 6 HOH 17 717 27  HOH HOH EEE . 
N 6 HOH 18 718 33  HOH HOH EEE . 
N 6 HOH 19 719 11  HOH HOH EEE . 
N 6 HOH 20 720 5   HOH HOH EEE . 
N 6 HOH 21 721 87  HOH HOH EEE . 
N 6 HOH 22 722 4   HOH HOH EEE . 
N 6 HOH 23 723 26  HOH HOH EEE . 
N 6 HOH 24 724 6   HOH HOH EEE . 
N 6 HOH 25 725 49  HOH HOH EEE . 
N 6 HOH 26 726 19  HOH HOH EEE . 
N 6 HOH 27 727 1   HOH HOH EEE . 
N 6 HOH 28 728 46  HOH HOH EEE . 
N 6 HOH 29 729 2   HOH HOH EEE . 
O 6 HOH 1  201 12  HOH HOH FFF . 
O 6 HOH 2  202 45  HOH HOH FFF . 
O 6 HOH 3  203 58  HOH HOH FFF . 
O 6 HOH 4  204 41  HOH HOH FFF . 
O 6 HOH 5  205 24  HOH HOH FFF . 
O 6 HOH 6  206 3   HOH HOH FFF . 
O 6 HOH 7  207 30  HOH HOH FFF . 
O 6 HOH 8  208 4   HOH HOH FFF . 
O 6 HOH 9  209 39  HOH HOH FFF . 
O 6 HOH 10 210 37  HOH HOH FFF . 
O 6 HOH 11 211 38  HOH HOH FFF . 
O 6 HOH 12 212 33  HOH HOH FFF . 
O 6 HOH 13 213 25  HOH HOH FFF . 
O 6 HOH 14 214 14  HOH HOH FFF . 
O 6 HOH 15 215 45  HOH HOH FFF . 
O 6 HOH 16 216 84  HOH HOH FFF . 
O 6 HOH 17 217 32  HOH HOH FFF . 
O 6 HOH 18 218 49  HOH HOH FFF . 
O 6 HOH 19 219 47  HOH HOH FFF . 
O 6 HOH 20 220 105 HOH HOH FFF . 
O 6 HOH 21 221 37  HOH HOH FFF . 
O 6 HOH 22 222 43  HOH HOH FFF . 
O 6 HOH 23 223 109 HOH HOH FFF . 
O 6 HOH 24 224 63  HOH HOH FFF . 
O 6 HOH 25 225 7   HOH HOH FFF . 
O 6 HOH 26 226 14  HOH HOH FFF . 
O 6 HOH 27 227 80  HOH HOH FFF . 
O 6 HOH 28 228 41  HOH HOH FFF . 
O 6 HOH 29 229 112 HOH HOH FFF . 
O 6 HOH 30 230 29  HOH HOH FFF . 
O 6 HOH 31 231 7   HOH HOH FFF . 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8OWT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.609 
_cell.length_a_esd                 ? 
_cell.length_b                     97.197 
_cell.length_b_esd                 ? 
_cell.length_c                     117.583 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8OWT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   8OWT 
_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             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.32 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'NaCl, potassium citrate pH 4.2, PEG 8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-03-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   0.9795 
_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 I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8OWT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.14 
_reflns.d_resolution_low                               58.78 
_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                                     57917 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_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                                0.088 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_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                                    2.14 
_reflns_shell.d_res_low                                     2.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2847 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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                               ? 
_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                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.324 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_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]                            -0.246 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            0.218 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.027 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               54.720 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.924 
_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                                 8OWT 
_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                            2.37 
_refine.ls_d_res_low                             58.78 
_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                     42863 
_refine.ls_number_reflns_R_free                  2056 
_refine.ls_number_reflns_R_work                  40807 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.991 
_refine.ls_percent_reflns_R_free                 4.797 
_refine.ls_R_factor_all                          0.214 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2490 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2126 
_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                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.396 
_refine.pdbx_overall_ESU_R_Free                  0.252 
_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                             22.968 
_refine.overall_SU_ML                            0.248 
_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        6960 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             172 
_refine_hist.number_atoms_total               7172 
_refine_hist.d_res_high                       2.37 
_refine_hist.d_res_low                        58.78 
# 
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' ? 0.003  0.012  7220  ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  6477  ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.241  1.651  9817  ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.119  1.583  14848 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 6.771  5.000  895   ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 29.027 21.538 390   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.613 15.000 1076  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.816 15.000 49    ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.042  0.200  901   ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  8396  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1898  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200  1037  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.164  0.200  6126  ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.200  3375  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.068  0.200  3425  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.121  0.200  209   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.139  0.200  35    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.188  0.200  121   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.127  0.200  15    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 1.142  2.656  3574  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.142  2.656  3573  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 1.850  3.982  4459  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 1.850  3.983  4460  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 1.382  2.779  3646  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.335  2.776  3644  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 2.249  4.117  5354  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 2.249  4.119  5355  ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 3.921  29.207 7541  ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.913  29.127 7522  ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.088  0.050  3656  ? r_ncsr_local_group_1           ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.050  6207  ? r_ncsr_local_group_2           ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.050  3844  ? r_ncsr_local_group_3           ? ? 
# 
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 ? ? 0.08753 ? 0.05010 1 'Local ncs' ? AAA ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.08753 ? 0.05010 2 'Local ncs' ? DDD ? ? ? 1 
'X-RAY DIFFRACTION' 3 ? ? 0.07307 ? 0.05010 3 'Local ncs' ? BBB ? ? ? 2 
'X-RAY DIFFRACTION' 4 ? ? 0.07307 ? 0.05010 4 'Local ncs' ? EEE ? ? ? 2 
'X-RAY DIFFRACTION' 5 ? ? 0.07140 ? 0.05011 5 'Local ncs' ? CCC ? ? ? 3 
'X-RAY DIFFRACTION' 6 ? ? 0.07140 ? 0.05011 6 'Local ncs' ? FFF ? ? ? 3 
# 
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_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 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.370  2.431  . . 139 2982 100.0000 . . . . 0.346 . . . . . . . . . . . 0.352 
'X-RAY DIFFRACTION' 2.431  2.498  . . 174 2874 100.0000 . . . . 0.336 . . . . . . . . . . . 0.339 
'X-RAY DIFFRACTION' 2.498  2.570  . . 125 2831 99.9662  . . . . 0.316 . . . . . . . . . . . 0.344 
'X-RAY DIFFRACTION' 2.570  2.649  . . 150 2721 100.0000 . . . . 0.310 . . . . . . . . . . . 0.328 
'X-RAY DIFFRACTION' 2.649  2.736  . . 128 2661 100.0000 . . . . 0.266 . . . . . . . . . . . 0.267 
'X-RAY DIFFRACTION' 2.736  2.832  . . 132 2579 100.0000 . . . . 0.260 . . . . . . . . . . . 0.362 
'X-RAY DIFFRACTION' 2.832  2.938  . . 103 2512 100.0000 . . . . 0.242 . . . . . . . . . . . 0.283 
'X-RAY DIFFRACTION' 2.938  3.058  . . 104 2402 100.0000 . . . . 0.231 . . . . . . . . . . . 0.262 
'X-RAY DIFFRACTION' 3.058  3.194  . . 103 2302 100.0000 . . . . 0.222 . . . . . . . . . . . 0.268 
'X-RAY DIFFRACTION' 3.194  3.349  . . 111 2240 100.0000 . . . . 0.225 . . . . . . . . . . . 0.232 
'X-RAY DIFFRACTION' 3.349  3.529  . . 125 2068 100.0000 . . . . 0.211 . . . . . . . . . . . 0.265 
'X-RAY DIFFRACTION' 3.529  3.743  . . 132 1964 100.0000 . . . . 0.208 . . . . . . . . . . . 0.214 
'X-RAY DIFFRACTION' 3.743  4.000  . . 99  1887 100.0000 . . . . 0.183 . . . . . . . . . . . 0.239 
'X-RAY DIFFRACTION' 4.000  4.319  . . 98  1749 100.0000 . . . . 0.160 . . . . . . . . . . . 0.182 
'X-RAY DIFFRACTION' 4.319  4.728  . . 83  1617 100.0000 . . . . 0.135 . . . . . . . . . . . 0.167 
'X-RAY DIFFRACTION' 4.728  5.282  . . 73  1496 100.0000 . . . . 0.161 . . . . . . . . . . . 0.209 
'X-RAY DIFFRACTION' 5.282  6.091  . . 73  1309 100.0000 . . . . 0.204 . . . . . . . . . . . 0.259 
'X-RAY DIFFRACTION' 6.091  7.440  . . 51  1140 100.0000 . . . . 0.193 . . . . . . . . . . . 0.295 
'X-RAY DIFFRACTION' 7.440  10.439 . . 28  910  100.0000 . . . . 0.186 . . . . . . . . . . . 0.192 
'X-RAY DIFFRACTION' 10.439 58.78  . . 25  552  100.0000 . . . . 0.258 . . . . . . . . . . . 0.345 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 AAA 
2 1 DDD 
3 2 BBB 
4 2 EEE 
5 3 CCC 
6 3 FFF 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_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.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A GLN 1 . A VAL 123 . AAA GLN 3   AAA VAL 125 ? ? 
1 2 1 D GLN 1 . D VAL 123 . DDD GLN 3   DDD VAL 125 ? ? 
2 3 2 B ASN 5 . B LYS 199 . BBB ASN 334 BBB LYS 528 ? ? 
2 4 2 E ASN 5 . E LYS 199 . EEE ASN 334 EEE LYS 528 ? ? 
3 5 3 C VAL 4 . C VAL 127 . CCC VAL 4   CCC VAL 127 ? ? 
3 6 3 F VAL 4 . F VAL 127 . FFF VAL 4   FFF VAL 127 ? ? 
# 
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' 
# 
_struct.entry_id                     8OWT 
_struct.title                        'SARS-CoV-2 spike RBD with A8 and H3 nanobodies bound' 
_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        8OWT 
_struct_keywords.text            'Nanobody, Complex, Receptor binding domain, SARS-CoV-2, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 3 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 6 ? 
# 
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 PDB 8OWT        8OWT   ? 1 ? 1   
2 UNP SPIKE_SARS2 P0DTC2 ? 2 
;PNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQ
IAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCY
FPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTN
;
330 
3 PDB 8OWT        8OWT   ? 3 ? 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 8OWT AAA 1 ? 132 ? 8OWT   3   ? 134 ? 3   134 
2 2 8OWT BBB 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
3 3 8OWT CCC 1 ? 136 ? 8OWT   1   ? 136 ? 1   136 
4 1 8OWT DDD 1 ? 132 ? 8OWT   3   ? 134 ? 3   134 
5 2 8OWT EEE 1 ? 203 ? P0DTC2 330 ? 532 ? 330 532 
6 3 8OWT FFF 1 ? 136 ? 8OWT   1   ? 136 ? 1   136 
# 
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 
2 8OWT LYS BBB 204 ? UNP P0DTC2 ? ? 'expression tag' 533 1  
2 8OWT HIS BBB 205 ? UNP P0DTC2 ? ? 'expression tag' 534 2  
2 8OWT HIS BBB 206 ? UNP P0DTC2 ? ? 'expression tag' 535 3  
2 8OWT HIS BBB 207 ? UNP P0DTC2 ? ? 'expression tag' 536 4  
2 8OWT HIS BBB 208 ? UNP P0DTC2 ? ? 'expression tag' 537 5  
2 8OWT HIS BBB 209 ? UNP P0DTC2 ? ? 'expression tag' 538 6  
2 8OWT HIS BBB 210 ? UNP P0DTC2 ? ? 'expression tag' 539 7  
5 8OWT LYS EEE 204 ? UNP P0DTC2 ? ? 'expression tag' 533 8  
5 8OWT HIS EEE 205 ? UNP P0DTC2 ? ? 'expression tag' 534 9  
5 8OWT HIS EEE 206 ? UNP P0DTC2 ? ? 'expression tag' 535 10 
5 8OWT HIS EEE 207 ? UNP P0DTC2 ? ? 'expression tag' 536 11 
5 8OWT HIS EEE 208 ? UNP P0DTC2 ? ? 'expression tag' 537 12 
5 8OWT HIS EEE 209 ? UNP P0DTC2 ? ? 'expression tag' 538 13 
5 8OWT HIS EEE 210 ? UNP P0DTC2 ? ? 'expression tag' 539 14 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7520  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  40400 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 
# 
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 THR A 28  ? ALA A 32  ? THR AAA 30  ALA AAA 34  5 ? 5 
HELX_P HELX_P2  AA2 ASP A 62  ? LYS A 65  ? ASP AAA 64  LYS AAA 67  5 ? 4 
HELX_P HELX_P3  AA3 ASN A 74  ? GLN A 76  ? ASN AAA 76  GLN AAA 78  5 ? 3 
HELX_P HELX_P4  AA4 LYS A 87  ? THR A 91  ? LYS AAA 89  THR AAA 93  5 ? 5 
HELX_P HELX_P5  AA5 ALA A 108 ? TYR A 112 ? ALA AAA 110 TYR AAA 114 5 ? 5 
HELX_P HELX_P6  AA6 PRO B 8   ? ASN B 14  ? PRO BBB 337 ASN BBB 343 1 ? 7 
HELX_P HELX_P7  AA7 SER B 20  ? TRP B 24  ? SER BBB 349 TRP BBB 353 5 ? 5 
HELX_P HELX_P8  AA8 TYR B 36  ? ASN B 41  ? TYR BBB 365 ASN BBB 370 1 ? 6 
HELX_P HELX_P9  AA9 SER B 54  ? ASP B 60  ? SER BBB 383 ASP BBB 389 5 ? 7 
HELX_P HELX_P10 AB1 ASP B 76  ? ILE B 81  ? ASP BBB 405 ILE BBB 410 5 ? 6 
HELX_P HELX_P11 AB2 GLY B 87  ? ASN B 93  ? GLY BBB 416 ASN BBB 422 1 ? 7 
HELX_P HELX_P12 AB3 SER B 109 ? SER B 114 ? SER BBB 438 SER BBB 443 1 ? 6 
HELX_P HELX_P13 AB4 GLY B 173 ? TYR B 176 ? GLY BBB 502 TYR BBB 505 5 ? 4 
HELX_P HELX_P14 AB5 ARG C 29  ? TYR C 34  ? ARG CCC 29  TYR CCC 34  1 ? 6 
HELX_P HELX_P15 AB6 LYS C 89  ? THR C 93  ? LYS CCC 89  THR CCC 93  5 ? 5 
HELX_P HELX_P16 AB7 TYR C 107 ? TYR C 111 ? TYR CCC 107 TYR CCC 111 5 ? 5 
HELX_P HELX_P17 AB8 THR C 112 ? PHE C 116 ? THR CCC 112 PHE CCC 116 5 ? 5 
HELX_P HELX_P18 AB9 THR D 28  ? ALA D 32  ? THR DDD 30  ALA DDD 34  5 ? 5 
HELX_P HELX_P19 AC1 ASP D 62  ? LYS D 65  ? ASP DDD 64  LYS DDD 67  5 ? 4 
HELX_P HELX_P20 AC2 ASN D 74  ? GLN D 76  ? ASN DDD 76  GLN DDD 78  5 ? 3 
HELX_P HELX_P21 AC3 LYS D 87  ? THR D 91  ? LYS DDD 89  THR DDD 93  5 ? 5 
HELX_P HELX_P22 AC4 ALA D 108 ? TYR D 112 ? ALA DDD 110 TYR DDD 114 5 ? 5 
HELX_P HELX_P23 AC5 PRO E 8   ? ASN E 14  ? PRO EEE 337 ASN EEE 343 1 ? 7 
HELX_P HELX_P24 AC6 SER E 20  ? TRP E 24  ? SER EEE 349 TRP EEE 353 5 ? 5 
HELX_P HELX_P25 AC7 TYR E 36  ? ASN E 41  ? TYR EEE 365 ASN EEE 370 1 ? 6 
HELX_P HELX_P26 AC8 SER E 54  ? ASP E 60  ? SER EEE 383 ASP EEE 389 5 ? 7 
HELX_P HELX_P27 AC9 ASP E 76  ? ILE E 81  ? ASP EEE 405 ILE EEE 410 5 ? 6 
HELX_P HELX_P28 AD1 GLY E 87  ? ASN E 93  ? GLY EEE 416 ASN EEE 422 1 ? 7 
HELX_P HELX_P29 AD2 SER E 109 ? SER E 114 ? SER EEE 438 SER EEE 443 1 ? 6 
HELX_P HELX_P30 AD3 GLY E 173 ? TYR E 176 ? GLY EEE 502 TYR EEE 505 5 ? 4 
HELX_P HELX_P31 AD4 ARG F 29  ? TYR F 34  ? ARG FFF 29  TYR FFF 34  1 ? 6 
HELX_P HELX_P32 AD5 LYS F 89  ? THR F 93  ? LYS FFF 89  THR FFF 93  5 ? 5 
HELX_P HELX_P33 AD6 TYR F 107 ? TYR F 111 ? TYR FFF 107 TYR FFF 111 5 ? 5 
HELX_P HELX_P34 AD7 THR F 112 ? PHE F 116 ? THR FFF 112 PHE FFF 116 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 22  SG  ? ? ? 1_555 A CYS 96  SG ? ? AAA CYS 24  AAA CYS 98  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf2  disulf ?   ? B CYS 7   SG  ? ? ? 1_555 B CYS 32  SG ? ? BBB CYS 336 BBB CYS 361 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf3  disulf ?   ? B CYS 50  SG  ? ? ? 1_555 B CYS 103 SG ? ? BBB CYS 379 BBB CYS 432 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
disulf4  disulf ?   ? B CYS 62  SG  ? ? ? 1_555 B CYS 196 SG ? ? BBB CYS 391 BBB CYS 525 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
disulf5  disulf ?   ? B CYS 151 SG  ? ? ? 1_555 B CYS 159 SG ? ? BBB CYS 480 BBB CYS 488 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf6  disulf ?   ? C CYS 24  SG  ? ? ? 1_555 C CYS 98  SG ? ? CCC CYS 24  CCC CYS 98  1_555 ? ? ? ? ? ? ? 2.061 ? ? 
disulf7  disulf ?   ? D CYS 22  SG  ? ? ? 1_555 D CYS 96  SG ? ? DDD CYS 24  DDD CYS 98  1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf8  disulf ?   ? E CYS 7   SG  ? ? ? 1_555 E CYS 32  SG ? ? EEE CYS 336 EEE CYS 361 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf9  disulf ?   ? E CYS 50  SG  ? ? ? 1_555 E CYS 103 SG ? ? EEE CYS 379 EEE CYS 432 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
disulf10 disulf ?   ? E CYS 62  SG  ? ? ? 1_555 E CYS 196 SG ? ? EEE CYS 391 EEE CYS 525 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf11 disulf ?   ? E CYS 151 SG  ? ? ? 1_555 E CYS 159 SG ? ? EEE CYS 480 EEE CYS 488 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf12 disulf ?   ? F CYS 24  SG  ? ? ? 1_555 F CYS 98  SG ? ? FFF CYS 24  FFF CYS 98  1_555 ? ? ? ? ? ? ? 2.056 ? ? 
covale1  covale one ? B ASN 14  ND2 ? ? ? 1_555 G NAG .   C1 ? ? BBB ASN 343 BBB NAG 601 1_555 ? ? ? ? ? ? ? 1.428 ? 
N-Glycosylation 
covale2  covale one ? E ASN 14  ND2 ? ? ? 1_555 H NAG .   C1 ? ? EEE ASN 343 EEE NAG 601 1_555 ? ? ? ? ? ? ? 1.448 ? 
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 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 6 ? 
AB1 ? 4 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
AB4 ? 5 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
AB7 ? 2 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB2 5 6 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? 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 GLN A 3   ? SER A 7   ? GLN AAA 5   SER AAA 9   
AA1 2 LEU A 18  ? SER A 25  ? LEU AAA 20  SER AAA 27  
AA1 3 THR A 78  ? MET A 83  ? THR AAA 80  MET AAA 85  
AA1 4 PHE A 68  ? ASP A 73  ? PHE AAA 70  ASP AAA 75  
AA2 1 GLY A 10  ? LEU A 11  ? GLY AAA 12  LEU AAA 13  
AA2 2 ILE A 119 ? THR A 122 ? ILE AAA 121 THR AAA 124 
AA2 3 ALA A 92  ? SER A 99  ? ALA AAA 94  SER AAA 101 
AA2 4 ALA A 33  ? GLN A 39  ? ALA AAA 35  GLN AAA 41  
AA2 5 GLU A 46  ? ILE A 51  ? GLU AAA 48  ILE AAA 53  
AA2 6 THR A 58  ? TYR A 60  ? THR AAA 60  TYR AAA 62  
AA3 1 GLY A 10  ? LEU A 11  ? GLY AAA 12  LEU AAA 13  
AA3 2 ILE A 119 ? THR A 122 ? ILE AAA 121 THR AAA 124 
AA3 3 ALA A 92  ? SER A 99  ? ALA AAA 94  SER AAA 101 
AA3 4 PHE A 114 ? TRP A 115 ? PHE AAA 116 TRP AAA 117 
AA4 1 ASN B 25  ? ILE B 29  ? ASN BBB 354 ILE BBB 358 
AA4 2 ASN B 65  ? ARG B 74  ? ASN BBB 394 ARG BBB 403 
AA4 3 PRO B 178 ? GLU B 187 ? PRO BBB 507 GLU BBB 516 
AA4 4 GLY B 102 ? ASN B 108 ? GLY BBB 431 ASN BBB 437 
AA4 5 THR B 47  ? TYR B 51  ? THR BBB 376 TYR BBB 380 
AA5 1 CYS B 32  ? VAL B 33  ? CYS BBB 361 VAL BBB 362 
AA5 2 VAL B 195 ? CYS B 196 ? VAL BBB 524 CYS BBB 525 
AA5 3 CYS B 62  ? PHE B 63  ? CYS BBB 391 PHE BBB 392 
AA6 1 LEU B 123 ? ARG B 125 ? LEU BBB 452 ARG BBB 454 
AA6 2 LEU B 163 ? SER B 165 ? LEU BBB 492 SER BBB 494 
AA7 1 TYR B 144 ? GLN B 145 ? TYR BBB 473 GLN BBB 474 
AA7 2 CYS B 159 ? TYR B 160 ? CYS BBB 488 TYR BBB 489 
AA8 1 VAL C 7   ? SER C 9   ? VAL CCC 7   SER CCC 9   
AA8 2 LEU C 20  ? ALA C 25  ? LEU CCC 20  ALA CCC 25  
AA8 3 THR C 80  ? MET C 85  ? THR CCC 80  MET CCC 85  
AA8 4 PHE C 70  ? ARG C 74  ? PHE CCC 70  ARG CCC 74  
AA9 1 GLY C 12  ? VAL C 14  ? GLY CCC 12  VAL CCC 14  
AA9 2 THR C 123 ? VAL C 127 ? THR CCC 123 VAL CCC 127 
AA9 3 ALA C 94  ? ILE C 100 ? ALA CCC 94  ILE CCC 100 
AA9 4 MET C 36  ? GLN C 41  ? MET CCC 36  GLN CCC 41  
AA9 5 GLU C 48  ? MET C 53  ? GLU CCC 48  MET CCC 53  
AA9 6 THR C 60  ? TYR C 62  ? THR CCC 60  TYR CCC 62  
AB1 1 GLN D 3   ? SER D 7   ? GLN DDD 5   SER DDD 9   
AB1 2 LEU D 18  ? SER D 25  ? LEU DDD 20  SER DDD 27  
AB1 3 THR D 78  ? MET D 83  ? THR DDD 80  MET DDD 85  
AB1 4 PHE D 68  ? ASP D 73  ? PHE DDD 70  ASP DDD 75  
AB2 1 GLY D 10  ? LEU D 11  ? GLY DDD 12  LEU DDD 13  
AB2 2 ILE D 119 ? THR D 122 ? ILE DDD 121 THR DDD 124 
AB2 3 ALA D 92  ? SER D 99  ? ALA DDD 94  SER DDD 101 
AB2 4 ALA D 33  ? GLN D 39  ? ALA DDD 35  GLN DDD 41  
AB2 5 GLU D 46  ? ILE D 51  ? GLU DDD 48  ILE DDD 53  
AB2 6 THR D 58  ? TYR D 60  ? THR DDD 60  TYR DDD 62  
AB3 1 GLY D 10  ? LEU D 11  ? GLY DDD 12  LEU DDD 13  
AB3 2 ILE D 119 ? THR D 122 ? ILE DDD 121 THR DDD 124 
AB3 3 ALA D 92  ? SER D 99  ? ALA DDD 94  SER DDD 101 
AB3 4 PHE D 114 ? TRP D 115 ? PHE DDD 116 TRP DDD 117 
AB4 1 ASN E 25  ? ILE E 29  ? ASN EEE 354 ILE EEE 358 
AB4 2 ASN E 65  ? ARG E 74  ? ASN EEE 394 ARG EEE 403 
AB4 3 PRO E 178 ? GLU E 187 ? PRO EEE 507 GLU EEE 516 
AB4 4 GLY E 102 ? ASN E 108 ? GLY EEE 431 ASN EEE 437 
AB4 5 THR E 47  ? TYR E 51  ? THR EEE 376 TYR EEE 380 
AB5 1 CYS E 32  ? VAL E 33  ? CYS EEE 361 VAL EEE 362 
AB5 2 VAL E 195 ? CYS E 196 ? VAL EEE 524 CYS EEE 525 
AB5 3 CYS E 62  ? PHE E 63  ? CYS EEE 391 PHE EEE 392 
AB6 1 LEU E 123 ? ARG E 125 ? LEU EEE 452 ARG EEE 454 
AB6 2 LEU E 163 ? SER E 165 ? LEU EEE 492 SER EEE 494 
AB7 1 TYR E 144 ? GLN E 145 ? TYR EEE 473 GLN EEE 474 
AB7 2 CYS E 159 ? TYR E 160 ? CYS EEE 488 TYR EEE 489 
AB8 1 VAL F 7   ? SER F 9   ? VAL FFF 7   SER FFF 9   
AB8 2 LEU F 20  ? ALA F 25  ? LEU FFF 20  ALA FFF 25  
AB8 3 THR F 80  ? MET F 85  ? THR FFF 80  MET FFF 85  
AB8 4 PHE F 70  ? ARG F 74  ? PHE FFF 70  ARG FFF 74  
AB9 1 GLY F 12  ? LYS F 15  ? GLY FFF 12  LYS FFF 15  
AB9 2 THR F 123 ? SER F 128 ? THR FFF 123 SER FFF 128 
AB9 3 ALA F 94  ? ILE F 100 ? ALA FFF 94  ILE FFF 100 
AB9 4 MET F 36  ? GLN F 41  ? MET FFF 36  GLN FFF 41  
AB9 5 GLU F 48  ? MET F 53  ? GLU FFF 48  MET FFF 53  
AB9 6 THR F 60  ? TYR F 62  ? THR FFF 60  TYR FFF 62  
# 
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 VAL A 5   ? N VAL AAA 7   O ALA A 23  ? O ALA AAA 25  
AA1 2 3 N LEU A 20  ? N LEU AAA 22  O LEU A 81  ? O LEU AAA 83  
AA1 3 4 O TYR A 80  ? O TYR AAA 82  N SER A 71  ? N SER AAA 73  
AA2 1 2 N GLY A 10  ? N GLY AAA 12  O GLN A 120 ? O GLN AAA 122 
AA2 2 3 O ILE A 119 ? O ILE AAA 121 N TYR A 94  ? N TYR AAA 96  
AA2 3 4 O TYR A 95  ? O TYR AAA 97  N PHE A 37  ? N PHE AAA 39  
AA2 4 5 N TRP A 36  ? N TRP AAA 38  O ALA A 49  ? O ALA AAA 51  
AA2 5 6 N SER A 50  ? N SER AAA 52  O TRP A 59  ? O TRP AAA 61  
AA3 1 2 N GLY A 10  ? N GLY AAA 12  O GLN A 120 ? O GLN AAA 122 
AA3 2 3 O ILE A 119 ? O ILE AAA 121 N TYR A 94  ? N TYR AAA 96  
AA3 3 4 N ALA A 98  ? N ALA AAA 100 O PHE A 114 ? O PHE AAA 116 
AA4 1 2 N ILE B 29  ? N ILE BBB 358 O VAL B 66  ? O VAL BBB 395 
AA4 2 3 N ILE B 73  ? N ILE BBB 402 O TYR B 179 ? O TYR BBB 508 
AA4 3 4 O VAL B 182 ? O VAL BBB 511 N ILE B 105 ? N ILE BBB 434 
AA4 4 5 O VAL B 104 ? O VAL BBB 433 N LYS B 49  ? N LYS BBB 378 
AA5 1 2 N CYS B 32  ? N CYS BBB 361 O CYS B 196 ? O CYS BBB 525 
AA5 2 3 O VAL B 195 ? O VAL BBB 524 N PHE B 63  ? N PHE BBB 392 
AA6 1 2 N TYR B 124 ? N TYR BBB 453 O GLN B 164 ? O GLN BBB 493 
AA7 1 2 N TYR B 144 ? N TYR BBB 473 O TYR B 160 ? O TYR BBB 489 
AA8 1 2 N SER C 9   ? N SER CCC 9   O SER C 23  ? O SER CCC 23  
AA8 2 3 N LEU C 20  ? N LEU CCC 20  O MET C 85  ? O MET CCC 85  
AA8 3 4 O HIS C 84  ? O HIS CCC 84  N THR C 71  ? N THR CCC 71  
AA9 1 2 N GLY C 12  ? N GLY CCC 12  O GLN C 124 ? O GLN CCC 124 
AA9 2 3 O THR C 123 ? O THR CCC 123 N TYR C 96  ? N TYR CCC 96  
AA9 3 4 O TYR C 97  ? O TYR CCC 97  N PHE C 39  ? N PHE CCC 39  
AA9 4 5 N TRP C 38  ? N TRP CCC 38  O ALA C 51  ? O ALA CCC 51  
AA9 5 6 N GLY C 52  ? N GLY CCC 52  O PHE C 61  ? O PHE CCC 61  
AB1 1 2 N VAL D 5   ? N VAL DDD 7   O ALA D 23  ? O ALA DDD 25  
AB1 2 3 N LEU D 20  ? N LEU DDD 22  O LEU D 81  ? O LEU DDD 83  
AB1 3 4 O TYR D 80  ? O TYR DDD 82  N SER D 71  ? N SER DDD 73  
AB2 1 2 N GLY D 10  ? N GLY DDD 12  O GLN D 120 ? O GLN DDD 122 
AB2 2 3 O ILE D 119 ? O ILE DDD 121 N TYR D 94  ? N TYR DDD 96  
AB2 3 4 O TYR D 95  ? O TYR DDD 97  N PHE D 37  ? N PHE DDD 39  
AB2 4 5 N TRP D 36  ? N TRP DDD 38  O ALA D 49  ? O ALA DDD 51  
AB2 5 6 N SER D 50  ? N SER DDD 52  O TRP D 59  ? O TRP DDD 61  
AB3 1 2 N GLY D 10  ? N GLY DDD 12  O GLN D 120 ? O GLN DDD 122 
AB3 2 3 O ILE D 119 ? O ILE DDD 121 N TYR D 94  ? N TYR DDD 96  
AB3 3 4 N ALA D 98  ? N ALA DDD 100 O PHE D 114 ? O PHE DDD 116 
AB4 1 2 N ILE E 29  ? N ILE EEE 358 O VAL E 66  ? O VAL EEE 395 
AB4 2 3 N ILE E 73  ? N ILE EEE 402 O TYR E 179 ? O TYR EEE 508 
AB4 3 4 O VAL E 182 ? O VAL EEE 511 N ILE E 105 ? N ILE EEE 434 
AB4 4 5 O VAL E 104 ? O VAL EEE 433 N LYS E 49  ? N LYS EEE 378 
AB5 1 2 N CYS E 32  ? N CYS EEE 361 O CYS E 196 ? O CYS EEE 525 
AB5 2 3 O VAL E 195 ? O VAL EEE 524 N PHE E 63  ? N PHE EEE 392 
AB6 1 2 N TYR E 124 ? N TYR EEE 453 O GLN E 164 ? O GLN EEE 493 
AB7 1 2 N TYR E 144 ? N TYR EEE 473 O TYR E 160 ? O TYR EEE 489 
AB8 1 2 N SER F 9   ? N SER FFF 9   O SER F 23  ? O SER FFF 23  
AB8 2 3 N LEU F 20  ? N LEU FFF 20  O MET F 85  ? O MET FFF 85  
AB8 3 4 O HIS F 84  ? O HIS FFF 84  N THR F 71  ? N THR FFF 71  
AB9 1 2 N GLY F 12  ? N GLY FFF 12  O GLN F 124 ? O GLN FFF 124 
AB9 2 3 O THR F 123 ? O THR FFF 123 N TYR F 96  ? N TYR FFF 96  
AB9 3 4 O TYR F 97  ? O TYR FFF 97  N PHE F 39  ? N PHE FFF 39  
AB9 4 5 N TRP F 38  ? N TRP FFF 38  O ALA F 51  ? O ALA FFF 51  
AB9 5 6 N GLY F 52  ? N GLY FFF 52  O PHE F 61  ? O PHE FFF 61  
# 
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 30  ? ? 37.42   66.55  
2  1 ASN BBB 334 ? ? 78.70   170.45 
3  1 ALA BBB 352 ? ? -106.15 45.32  
4  1 LEU BBB 368 ? ? -91.44  -60.74 
5  1 ASN BBB 422 ? ? -124.67 -62.34 
6  1 THR DDD 30  ? ? 36.39   66.20  
7  1 ALA EEE 352 ? ? -105.82 44.75  
8  1 LEU EEE 368 ? ? -90.55  -61.33 
9  1 ASN EEE 422 ? ? -123.76 -61.20 
10 1 HIS EEE 519 ? ? -68.68  73.13  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   SER 
_pdbx_validate_peptide_omega.auth_asym_id_1   BBB 
_pdbx_validate_peptide_omega.auth_seq_id_1    494 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   BBB 
_pdbx_validate_peptide_omega.auth_seq_id_2    495 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            150.00 
# 
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 3.0930   13.1920 -33.6730 0.4031 ? -0.0228 ? -0.0920 ? 0.6262 ? -0.0821 ? 0.1324 ? 10.3768 ? 
-3.5336 ? 1.6316  ? 4.2166  ? -0.9063 ? 1.2954  ? 0.4403  ? 0.3433  ? 0.2223  ? -0.8751 ? -0.3838 ? 0.2028  ? 0.0234  ? -0.1643 ? 
-0.0565 ? 
2  'X-RAY DIFFRACTION' ? refined 7.4160   14.3220 -24.8650 0.2106 ? -0.0235 ? -0.0727 ? 0.6694 ? -0.0293 ? 0.1890 ? 4.3846  ? 
-0.8697 ? -2.1479 ? 1.5767  ? 0.6639  ? 5.5010  ? 0.1071  ? 0.7120  ? 0.5677  ? -0.3463 ? -0.3077 ? -0.0596 ? -0.8702 ? -0.0009 ? 
0.2006  ? 
3  'X-RAY DIFFRACTION' ? refined -0.5280  11.5630 -21.9590 0.0884 ? -0.0153 ? -0.0457 ? 0.6038 ? -0.0794 ? 0.2032 ? 3.5881  ? 
-1.6121 ? -0.2633 ? 4.7815  ? -0.1408 ? 6.5224  ? -0.1799 ? 0.2657  ? 0.2184  ? -0.1988 ? 0.0384  ? 0.3887  ? -0.5675 ? -0.6422 ? 
0.1415  ? 
4  'X-RAY DIFFRACTION' ? refined 7.5200   17.0660 -23.4790 0.3323 ? -0.0866 ? -0.1253 ? 0.6388 ? -0.0049 ? 0.1849 ? 3.4055  ? 
-1.1644 ? -1.3647 ? 4.7648  ? -1.8088 ? 2.1861  ? 0.2180  ? 0.4992  ? 0.3455  ? -0.5546 ? -0.0636 ? 0.1707  ? -0.1630 ? 0.0260  ? 
-0.1544 ? 
5  'X-RAY DIFFRACTION' ? refined 12.9840  12.4060 8.6520   0.4297 ? -0.0238 ? 0.0666  ? 0.6045 ? -0.0569 ? 0.0996 ? 4.6888  ? 
3.8656  ? -0.8225 ? 7.8944  ? -3.0867 ? 2.1728  ? 0.0582  ? -0.2232 ? -0.2912 ? 0.8693  ? 0.0854  ? 0.1265  ? 0.0428  ? -0.2412 ? 
-0.1435 ? 
6  'X-RAY DIFFRACTION' ? refined 12.4940  5.0320  -0.3730  0.1355 ? -0.0612 ? 0.0142  ? 0.7139 ? 0.0053  ? 0.1197 ? 0.9711  ? 
0.8621  ? -0.0532 ? 1.3400  ? -0.1633 ? 1.2155  ? 0.0345  ? -0.0955 ? -0.1658 ? 0.0645  ? -0.0454 ? -0.0285 ? 0.3772  ? -0.2685 ? 
0.0109  ? 
7  'X-RAY DIFFRACTION' ? refined 21.3370  21.2920 -8.9020  0.1551 ? -0.0295 ? 0.0842  ? 0.4505 ? 0.0021  ? 0.1470 ? 5.8475  ? 
-1.6622 ? 1.3469  ? 1.8008  ? 1.3284  ? 5.6952  ? -0.0061 ? 0.4175  ? 0.3143  ? -0.3462 ? -0.0231 ? -0.0682 ? -0.4401 ? 0.1604  ? 
0.0292  ? 
8  'X-RAY DIFFRACTION' ? refined 21.7200  25.0690 0.3210   0.0024 ? 0.0088  ? -0.0029 ? 0.4841 ? -0.0009 ? 0.0151 ? 1.1415  ? 
1.5968  ? 0.2981  ? 3.0995  ? 0.7161  ? 0.9168  ? -0.0059 ? 0.0152  ? -0.0293 ? 0.0327  ? -0.0280 ? -0.1227 ? 0.0226  ? -0.0114 ? 
0.0340  ? 
9  'X-RAY DIFFRACTION' ? refined 13.0170  -5.8560 7.5610   0.4195 ? -0.0963 ? 0.0062  ? 0.4838 ? 0.0943  ? 0.3713 ? 4.9563  ? 
-5.1462 ? -3.2043 ? 7.8792  ? 0.8133  ? 4.5692  ? -0.3641 ? 0.2287  ? -0.3110 ? 0.0148  ? 0.2341  ? 0.3594  ? 0.5950  ? -0.6543 ? 
0.1300  ? 
10 'X-RAY DIFFRACTION' ? refined 9.6220   44.5920 19.7330  0.2221 ? -0.0023 ? -0.0854 ? 0.5341 ? 0.1846  ? 0.7405 ? 15.8281 ? 
8.5180  ? 7.1729  ? 15.0739 ? 0.5277  ? 14.2693 ? -0.4938 ? -0.4432 ? -0.8216 ? -0.7074 ? 0.2057  ? 0.9354  ? -0.4257 ? -0.1852 ? 
0.2881  ? 
11 'X-RAY DIFFRACTION' ? refined 18.9230  52.8030 16.8600  0.2269 ? 0.0045  ? -0.0566 ? 0.4747 ? -0.0116 ? 0.2117 ? 5.1255  ? 
0.6378  ? 0.0361  ? 6.1746  ? 0.7487  ? 4.0689  ? -0.0458 ? 0.0474  ? 0.9351  ? 0.3338  ? -0.0269 ? -0.2867 ? -0.8674 ? -0.0322 ? 
0.0728  ? 
12 'X-RAY DIFFRACTION' ? refined 25.3270  49.7370 14.2960  0.0867 ? -0.0529 ? -0.0352 ? 0.4688 ? 0.0048  ? 0.1519 ? 5.2579  ? 
-1.7277 ? -0.3629 ? 2.7024  ? 1.0516  ? 3.1773  ? -0.0487 ? 0.1686  ? 0.8499  ? 0.0293  ? -0.0312 ? -0.3366 ? -0.4414 ? 0.2561  ? 
0.0800  ? 
13 'X-RAY DIFFRACTION' ? refined 16.8810  50.1310 9.3680   0.0776 ? -0.0186 ? -0.0006 ? 0.4507 ? 0.0355  ? 0.1479 ? 3.4580  ? 
-0.5644 ? -0.8612 ? 4.9226  ? 0.9031  ? 4.3562  ? 0.0514  ? 0.1123  ? 0.5976  ? 0.1210  ? -0.1080 ? 0.3300  ? -0.5215 ? -0.2152 ? 
0.0565  ? 
14 'X-RAY DIFFRACTION' ? refined 14.0880  15.7910 63.0020  0.4261 ? 0.0262  ? -0.0271 ? 0.4478 ? -0.0284 ? 0.3544 ? 3.2710  ? 
-5.2532 ? -3.5589 ? 13.1459 ? 6.0371  ? 4.0023  ? -0.1463 ? -0.1420 ? -0.0450 ? 0.6538  ? 0.0304  ? 0.2322  ? 0.0016  ? 0.0434  ? 
0.1158  ? 
15 'X-RAY DIFFRACTION' ? refined 15.4300  12.9140 54.3410  0.3358 ? -0.0459 ? -0.0743 ? 0.4519 ? -0.0394 ? 0.3377 ? 6.8600  ? 
-1.7888 ? -0.6046 ? 3.0953  ? -1.0840 ? 4.2472  ? -0.0241 ? -0.3774 ? 0.7566  ? 0.4811  ? -0.1110 ? 0.3169  ? -0.7690 ? -0.3605 ? 
0.1352  ? 
16 'X-RAY DIFFRACTION' ? refined 16.5460  19.8270 51.1060  0.5271 ? -0.0373 ? -0.1290 ? 0.5171 ? 0.0279  ? 0.4394 ? 4.0524  ? 
-1.3769 ? -0.6588 ? 6.0980  ? 0.5301  ? 4.2943  ? 0.0899  ? -0.0820 ? 0.7973  ? 0.3780  ? -0.1006 ? 0.3904  ? -0.9328 ? -0.2229 ? 
0.0107  ? 
17 'X-RAY DIFFRACTION' ? refined 10.3710  13.5470 52.6400  0.3530 ? 0.0210  ? -0.0490 ? 0.5447 ? -0.0458 ? 0.3626 ? 2.5568  ? 
-0.3144 ? -1.9514 ? 4.2159  ? 0.6184  ? 4.7804  ? 0.0326  ? -0.2278 ? 0.5474  ? 0.6894  ? -0.1047 ? 0.6068  ? -0.7076 ? -0.2072 ? 
0.0720  ? 
18 'X-RAY DIFFRACTION' ? refined 18.4880  8.2590  26.2670  0.2600 ? -0.0405 ? -0.0575 ? 0.8127 ? 0.2861  ? 0.3041 ? 3.7065  ? 
-0.2536 ? 0.2961  ? 0.6689  ? 0.8842  ? 1.4630  ? -0.0440 ? 0.8086  ? 0.6484  ? -0.1590 ? 0.0009  ? -0.1632 ? -0.3873 ? 0.2709  ? 
0.0431  ? 
19 'X-RAY DIFFRACTION' ? refined 16.3510  3.5940  29.6940  0.1822 ? -0.0104 ? -0.0700 ? 0.3048 ? 0.0904  ? 0.1082 ? 8.4717  ? 
-1.2705 ? -0.8714 ? 2.6252  ? 0.4523  ? 1.8482  ? -0.0359 ? 0.2643  ? 0.0443  ? -0.0854 ? -0.1222 ? 0.0027  ? -0.0779 ? 0.0632  ? 
0.1580  ? 
20 'X-RAY DIFFRACTION' ? refined 4.6450   1.6240  31.1980  0.0949 ? 0.0540  ? 0.0044  ? 0.4728 ? 0.0396  ? 0.0141 ? 5.1137  ? 
-0.1061 ? 1.7608  ? 2.9737  ? 0.0487  ? 3.1557  ? -0.1164 ? 0.0586  ? 0.1406  ? 0.1474  ? -0.0201 ? -0.0985 ? -0.0353 ? -0.0254 ? 
0.1365  ? 
21 'X-RAY DIFFRACTION' ? refined -5.1790  -8.1250 25.8170  0.1859 ? 0.0932  ? 0.0439  ? 0.4612 ? 0.0256  ? 0.1248 ? 5.6837  ? 
2.3130  ? 2.0639  ? 0.9922  ? 0.5794  ? 2.3796  ? -0.1314 ? 0.0678  ? -0.4867 ? -0.0944 ? 0.0411  ? -0.2221 ? 0.2012  ? 0.1044  ? 
0.0903  ? 
22 'X-RAY DIFFRACTION' ? refined 17.8500  6.0140  28.0760  0.2435 ? -0.0162 ? -0.0545 ? 0.4935 ? 0.1388  ? 0.1401 ? 9.6263  ? 
-2.2615 ? -0.7640 ? 2.1964  ? 1.1532  ? 1.0883  ? -0.1978 ? 0.2472  ? 0.5146  ? -0.0062 ? 0.1325  ? -0.2069 ? -0.0778 ? 0.2679  ? 
0.0653  ? 
23 'X-RAY DIFFRACTION' ? refined -18.8500 12.3140 9.8250   0.4217 ? 0.1234  ? 0.0107  ? 0.4454 ? -0.0324 ? 0.2999 ? 20.3654 ? 
4.8554  ? 9.2133  ? 1.8173  ? 1.0069  ? 7.6107  ? -0.5599 ? 0.2940  ? 0.6895  ? -0.0293 ? 0.1710  ? 0.0410  ? -0.7494 ? 0.1497  ? 
0.3888  ? 
24 'X-RAY DIFFRACTION' ? refined -26.4550 2.3360  13.2570  0.0867 ? 0.0296  ? 0.0329  ? 0.5623 ? 0.0032  ? 0.1130 ? 5.5798  ? 
1.0361  ? 0.6525  ? 3.1578  ? -0.4614 ? 3.7430  ? -0.0064 ? 0.1104  ? 0.1217  ? 0.1023  ? -0.0363 ? 0.5668  ? -0.0374 ? -0.6009 ? 
0.0427  ? 
25 'X-RAY DIFFRACTION' ? refined -21.8160 -3.8150 15.2860  0.0567 ? 0.0005  ? 0.0465  ? 0.4711 ? -0.0085 ? 0.0916 ? 3.8722  ? 
0.0311  ? 0.0649  ? 2.1428  ? -0.3558 ? 3.7409  ? -0.0120 ? 0.2093  ? -0.1460 ? 0.1218  ? -0.0238 ? 0.2848  ? 0.3303  ? -0.3792 ? 
0.0359  ? 
26 'X-RAY DIFFRACTION' ? refined -25.1890 3.5640  20.1560  0.1225 ? 0.0049  ? 0.0489  ? 0.5174 ? 0.0022  ? 0.1406 ? 4.4003  ? 
-0.6457 ? 1.7216  ? 1.6064  ? -0.1281 ? 2.5181  ? -0.0817 ? 0.1180  ? 0.0309  ? 0.1411  ? 0.0211  ? 0.4513  ? -0.0244 ? -0.3408 ? 
0.0606  ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ALL '{ AAA|3-21 }'    
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ALL '{ AAA|22-46 }'   
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ALL '{ AAA|47-89 }'   
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ALL '{ AAA|90-125 }'  
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ALL '{ BBB|331-357 }' 
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ALL '{ BBB|358-402 }' 
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ALL '{ BBB|403-417 }' 
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ALL '{ BBB|418-519 }' 
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ALL '{ BBB|520-529 }' 
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ALL '{ CCC|4-7 }'     
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ALL '{ CCC|8-46 }'    
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ALL '{ CCC|47-92 }'   
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ALL '{ CCC|93-128 }'  
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ALL '{ DDD|3-20 }'    
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ALL '{ DDD|21-44 }'   
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ALL '{ DDD|45-88 }'   
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ALL '{ DDD|89-125 }'  
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ALL '{ EEE|334-386 }' 
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ALL '{ EEE|387-408 }' 
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ALL '{ EEE|409-458 }' 
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ALL '{ EEE|459-498 }' 
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ALL '{ EEE|499-529 }' 
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ALL '{ FFF|3-8 }'     
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ALL '{ FFF|9-46 }'    
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ALL '{ FFF|47-88 }'   
26 'X-RAY DIFFRACTION' 26 ? ? ? ? ? ? ? ? ? ? ALL '{ FFF|89-129 }'  
# 
_pdbx_entry_details.entry_id                 8OWT 
_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         ? 
# 
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 SER 126 ? A SER 124 
2  1 Y 1 AAA SER 127 ? A SER 125 
3  1 Y 1 AAA LYS 128 ? A LYS 126 
4  1 Y 1 AAA HIS 129 ? A HIS 127 
5  1 Y 1 AAA HIS 130 ? A HIS 128 
6  1 Y 1 AAA HIS 131 ? A HIS 129 
7  1 Y 1 AAA HIS 132 ? A HIS 130 
8  1 Y 1 AAA HIS 133 ? A HIS 131 
9  1 Y 1 AAA HIS 134 ? A HIS 132 
10 1 Y 1 BBB PRO 330 ? B PRO 1   
11 1 Y 1 BBB SER 530 ? B SER 201 
12 1 Y 1 BBB THR 531 ? B THR 202 
13 1 Y 1 BBB ASN 532 ? B ASN 203 
14 1 Y 1 BBB LYS 533 ? B LYS 204 
15 1 Y 1 BBB HIS 534 ? B HIS 205 
16 1 Y 1 BBB HIS 535 ? B HIS 206 
17 1 Y 1 BBB HIS 536 ? B HIS 207 
18 1 Y 1 BBB HIS 537 ? B HIS 208 
19 1 Y 1 BBB HIS 538 ? B HIS 209 
20 1 Y 1 BBB HIS 539 ? B HIS 210 
21 1 Y 1 CCC MET 1   ? C MET 1   
22 1 Y 1 CCC ALA 2   ? C ALA 2   
23 1 Y 1 CCC GLN 3   ? C GLN 3   
24 1 Y 1 CCC SER 129 ? C SER 129 
25 1 Y 1 CCC LYS 130 ? C LYS 130 
26 1 Y 1 CCC HIS 131 ? C HIS 131 
27 1 Y 1 CCC HIS 132 ? C HIS 132 
28 1 Y 1 CCC HIS 133 ? C HIS 133 
29 1 Y 1 CCC HIS 134 ? C HIS 134 
30 1 Y 1 CCC HIS 135 ? C HIS 135 
31 1 Y 1 CCC HIS 136 ? C HIS 136 
32 1 Y 1 DDD SER 126 ? D SER 124 
33 1 Y 1 DDD SER 127 ? D SER 125 
34 1 Y 1 DDD LYS 128 ? D LYS 126 
35 1 Y 1 DDD HIS 129 ? D HIS 127 
36 1 Y 1 DDD HIS 130 ? D HIS 128 
37 1 Y 1 DDD HIS 131 ? D HIS 129 
38 1 Y 1 DDD HIS 132 ? D HIS 130 
39 1 Y 1 DDD HIS 133 ? D HIS 131 
40 1 Y 1 DDD HIS 134 ? D HIS 132 
41 1 Y 1 EEE PRO 330 ? E PRO 1   
42 1 Y 1 EEE ASN 331 ? E ASN 2   
43 1 Y 1 EEE ILE 332 ? E ILE 3   
44 1 Y 1 EEE THR 333 ? E THR 4   
45 1 Y 1 EEE SER 530 ? E SER 201 
46 1 Y 1 EEE THR 531 ? E THR 202 
47 1 Y 1 EEE ASN 532 ? E ASN 203 
48 1 Y 1 EEE LYS 533 ? E LYS 204 
49 1 Y 1 EEE HIS 534 ? E HIS 205 
50 1 Y 1 EEE HIS 535 ? E HIS 206 
51 1 Y 1 EEE HIS 536 ? E HIS 207 
52 1 Y 1 EEE HIS 537 ? E HIS 208 
53 1 Y 1 EEE HIS 538 ? E HIS 209 
54 1 Y 1 EEE HIS 539 ? E HIS 210 
55 1 Y 1 FFF MET 1   ? F MET 1   
56 1 Y 1 FFF ALA 2   ? F ALA 2   
57 1 Y 1 FFF LYS 130 ? F LYS 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 FFF HIS 133 ? F HIS 133 
61 1 Y 1 FFF HIS 134 ? F HIS 134 
62 1 Y 1 FFF HIS 135 ? F HIS 135 
63 1 Y 1 FFF HIS 136 ? F HIS 136 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MES O1   O N N 230 
MES C2   C N N 231 
MES C3   C N N 232 
MES N4   N N N 233 
MES C5   C N N 234 
MES C6   C N N 235 
MES C7   C N N 236 
MES C8   C N N 237 
MES S    S N N 238 
MES O1S  O N N 239 
MES O2S  O N N 240 
MES O3S  O N N 241 
MES H21  H N N 242 
MES H22  H N N 243 
MES H31  H N N 244 
MES H32  H N N 245 
MES HN4  H N N 246 
MES H51  H N N 247 
MES H52  H N N 248 
MES H61  H N N 249 
MES H62  H N N 250 
MES H71  H N N 251 
MES H72  H N N 252 
MES H81  H N N 253 
MES H82  H N N 254 
MET N    N N N 255 
MET CA   C N S 256 
MET C    C N N 257 
MET O    O N N 258 
MET CB   C N N 259 
MET CG   C N N 260 
MET SD   S N N 261 
MET CE   C N N 262 
MET OXT  O N N 263 
MET H    H N N 264 
MET H2   H N N 265 
MET HA   H N N 266 
MET HB2  H N N 267 
MET HB3  H N N 268 
MET HG2  H N N 269 
MET HG3  H N N 270 
MET HE1  H N N 271 
MET HE2  H N N 272 
MET HE3  H N N 273 
MET HXT  H N N 274 
NAG C1   C N R 275 
NAG C2   C N R 276 
NAG C3   C N R 277 
NAG C4   C N S 278 
NAG C5   C N R 279 
NAG C6   C N N 280 
NAG C7   C N N 281 
NAG C8   C N N 282 
NAG N2   N N N 283 
NAG O1   O N N 284 
NAG O3   O N N 285 
NAG O4   O N N 286 
NAG O5   O N N 287 
NAG O6   O N N 288 
NAG O7   O N N 289 
NAG H1   H N N 290 
NAG H2   H N N 291 
NAG H3   H N N 292 
NAG H4   H N N 293 
NAG H5   H N N 294 
NAG H61  H N N 295 
NAG H62  H N N 296 
NAG H81  H N N 297 
NAG H82  H N N 298 
NAG H83  H N N 299 
NAG HN2  H N N 300 
NAG HO1  H N N 301 
NAG HO3  H N N 302 
NAG HO4  H N N 303 
NAG HO6  H N N 304 
PHE N    N N N 305 
PHE CA   C N S 306 
PHE C    C N N 307 
PHE O    O N N 308 
PHE CB   C N N 309 
PHE CG   C Y N 310 
PHE CD1  C Y N 311 
PHE CD2  C Y N 312 
PHE CE1  C Y N 313 
PHE CE2  C Y N 314 
PHE CZ   C Y N 315 
PHE OXT  O N N 316 
PHE H    H N N 317 
PHE H2   H N N 318 
PHE HA   H N N 319 
PHE HB2  H N N 320 
PHE HB3  H N N 321 
PHE HD1  H N N 322 
PHE HD2  H N N 323 
PHE HE1  H N N 324 
PHE HE2  H N N 325 
PHE HZ   H N N 326 
PHE HXT  H N N 327 
PRO N    N N N 328 
PRO CA   C N S 329 
PRO C    C N N 330 
PRO O    O N N 331 
PRO CB   C N N 332 
PRO CG   C N N 333 
PRO CD   C N N 334 
PRO OXT  O N N 335 
PRO H    H N N 336 
PRO HA   H N N 337 
PRO HB2  H N N 338 
PRO HB3  H N N 339 
PRO HG2  H N N 340 
PRO HG3  H N N 341 
PRO HD2  H N N 342 
PRO HD3  H N N 343 
PRO HXT  H N N 344 
SER N    N N N 345 
SER CA   C N S 346 
SER C    C N N 347 
SER O    O N N 348 
SER CB   C N N 349 
SER OG   O N N 350 
SER OXT  O N N 351 
SER H    H N N 352 
SER H2   H N N 353 
SER HA   H N N 354 
SER HB2  H N N 355 
SER HB3  H N N 356 
SER HG   H N N 357 
SER HXT  H N N 358 
THR N    N N N 359 
THR CA   C N S 360 
THR C    C N N 361 
THR O    O N N 362 
THR CB   C N R 363 
THR OG1  O N N 364 
THR CG2  C N N 365 
THR OXT  O N N 366 
THR H    H N N 367 
THR H2   H N N 368 
THR HA   H N N 369 
THR HB   H N N 370 
THR HG1  H N N 371 
THR HG21 H N N 372 
THR HG22 H N N 373 
THR HG23 H N N 374 
THR HXT  H N N 375 
TRP N    N N N 376 
TRP CA   C N S 377 
TRP C    C N N 378 
TRP O    O N N 379 
TRP CB   C N N 380 
TRP CG   C Y N 381 
TRP CD1  C Y N 382 
TRP CD2  C Y N 383 
TRP NE1  N Y N 384 
TRP CE2  C Y N 385 
TRP CE3  C Y N 386 
TRP CZ2  C Y N 387 
TRP CZ3  C Y N 388 
TRP CH2  C Y N 389 
TRP OXT  O N N 390 
TRP H    H N N 391 
TRP H2   H N N 392 
TRP HA   H N N 393 
TRP HB2  H N N 394 
TRP HB3  H N N 395 
TRP HD1  H N N 396 
TRP HE1  H N N 397 
TRP HE3  H N N 398 
TRP HZ2  H N N 399 
TRP HZ3  H N N 400 
TRP HH2  H N N 401 
TRP HXT  H N N 402 
TYR N    N N N 403 
TYR CA   C N S 404 
TYR C    C N N 405 
TYR O    O N N 406 
TYR CB   C N N 407 
TYR CG   C Y N 408 
TYR CD1  C Y N 409 
TYR CD2  C Y N 410 
TYR CE1  C Y N 411 
TYR CE2  C Y N 412 
TYR CZ   C Y N 413 
TYR OH   O N N 414 
TYR OXT  O N N 415 
TYR H    H N N 416 
TYR H2   H N N 417 
TYR HA   H N N 418 
TYR HB2  H N N 419 
TYR HB3  H N N 420 
TYR HD1  H N N 421 
TYR HD2  H N N 422 
TYR HE1  H N N 423 
TYR HE2  H N N 424 
TYR HH   H N N 425 
TYR HXT  H N N 426 
VAL N    N N N 427 
VAL CA   C N S 428 
VAL C    C N N 429 
VAL O    O N N 430 
VAL CB   C N N 431 
VAL CG1  C N N 432 
VAL CG2  C N N 433 
VAL OXT  O N N 434 
VAL H    H N N 435 
VAL H2   H N N 436 
VAL HA   H N N 437 
VAL HB   H N N 438 
VAL HG11 H N N 439 
VAL HG12 H N N 440 
VAL HG13 H N N 441 
VAL HG21 H N N 442 
VAL HG22 H N N 443 
VAL HG23 H N N 444 
VAL HXT  H N N 445 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MES O1  C2   sing N N 218 
MES O1  C6   sing N N 219 
MES C2  C3   sing N N 220 
MES C2  H21  sing N N 221 
MES C2  H22  sing N N 222 
MES C3  N4   sing N N 223 
MES C3  H31  sing N N 224 
MES C3  H32  sing N N 225 
MES N4  C5   sing N N 226 
MES N4  C7   sing N N 227 
MES N4  HN4  sing N N 228 
MES C5  C6   sing N N 229 
MES C5  H51  sing N N 230 
MES C5  H52  sing N N 231 
MES C6  H61  sing N N 232 
MES C6  H62  sing N N 233 
MES C7  C8   sing N N 234 
MES C7  H71  sing N N 235 
MES C7  H72  sing N N 236 
MES C8  S    sing N N 237 
MES C8  H81  sing N N 238 
MES C8  H82  sing N N 239 
MES S   O1S  doub N N 240 
MES S   O2S  doub N N 241 
MES S   O3S  sing N N 242 
MET N   CA   sing N N 243 
MET N   H    sing N N 244 
MET N   H2   sing N N 245 
MET CA  C    sing N N 246 
MET CA  CB   sing N N 247 
MET CA  HA   sing N N 248 
MET C   O    doub N N 249 
MET C   OXT  sing N N 250 
MET CB  CG   sing N N 251 
MET CB  HB2  sing N N 252 
MET CB  HB3  sing N N 253 
MET CG  SD   sing N N 254 
MET CG  HG2  sing N N 255 
MET CG  HG3  sing N N 256 
MET SD  CE   sing N N 257 
MET CE  HE1  sing N N 258 
MET CE  HE2  sing N N 259 
MET CE  HE3  sing N N 260 
MET OXT HXT  sing N N 261 
NAG C1  C2   sing N N 262 
NAG C1  O1   sing N N 263 
NAG C1  O5   sing N N 264 
NAG C1  H1   sing N N 265 
NAG C2  C3   sing N N 266 
NAG C2  N2   sing N N 267 
NAG C2  H2   sing N N 268 
NAG C3  C4   sing N N 269 
NAG C3  O3   sing N N 270 
NAG C3  H3   sing N N 271 
NAG C4  C5   sing N N 272 
NAG C4  O4   sing N N 273 
NAG C4  H4   sing N N 274 
NAG C5  C6   sing N N 275 
NAG C5  O5   sing N N 276 
NAG C5  H5   sing N N 277 
NAG C6  O6   sing N N 278 
NAG C6  H61  sing N N 279 
NAG C6  H62  sing N N 280 
NAG C7  C8   sing N N 281 
NAG C7  N2   sing N N 282 
NAG C7  O7   doub N N 283 
NAG C8  H81  sing N N 284 
NAG C8  H82  sing N N 285 
NAG C8  H83  sing N N 286 
NAG N2  HN2  sing N N 287 
NAG O1  HO1  sing N N 288 
NAG O3  HO3  sing N N 289 
NAG O4  HO4  sing N N 290 
NAG O6  HO6  sing N N 291 
PHE N   CA   sing N N 292 
PHE N   H    sing N N 293 
PHE N   H2   sing N N 294 
PHE CA  C    sing N N 295 
PHE CA  CB   sing N N 296 
PHE CA  HA   sing N N 297 
PHE C   O    doub N N 298 
PHE C   OXT  sing N N 299 
PHE CB  CG   sing N N 300 
PHE CB  HB2  sing N N 301 
PHE CB  HB3  sing N N 302 
PHE CG  CD1  doub Y N 303 
PHE CG  CD2  sing Y N 304 
PHE CD1 CE1  sing Y N 305 
PHE CD1 HD1  sing N N 306 
PHE CD2 CE2  doub Y N 307 
PHE CD2 HD2  sing N N 308 
PHE CE1 CZ   doub Y N 309 
PHE CE1 HE1  sing N N 310 
PHE CE2 CZ   sing Y N 311 
PHE CE2 HE2  sing N N 312 
PHE CZ  HZ   sing N N 313 
PHE OXT HXT  sing N N 314 
PRO N   CA   sing N N 315 
PRO N   CD   sing N N 316 
PRO N   H    sing N N 317 
PRO CA  C    sing N N 318 
PRO CA  CB   sing N N 319 
PRO CA  HA   sing N N 320 
PRO C   O    doub N N 321 
PRO C   OXT  sing N N 322 
PRO CB  CG   sing N N 323 
PRO CB  HB2  sing N N 324 
PRO CB  HB3  sing N N 325 
PRO CG  CD   sing N N 326 
PRO CG  HG2  sing N N 327 
PRO CG  HG3  sing N N 328 
PRO CD  HD2  sing N N 329 
PRO CD  HD3  sing N N 330 
PRO OXT HXT  sing N N 331 
SER N   CA   sing N N 332 
SER N   H    sing N N 333 
SER N   H2   sing N N 334 
SER CA  C    sing N N 335 
SER CA  CB   sing N N 336 
SER CA  HA   sing N N 337 
SER C   O    doub N N 338 
SER C   OXT  sing N N 339 
SER CB  OG   sing N N 340 
SER CB  HB2  sing N N 341 
SER CB  HB3  sing N N 342 
SER OG  HG   sing N N 343 
SER OXT HXT  sing N N 344 
THR N   CA   sing N N 345 
THR N   H    sing N N 346 
THR N   H2   sing N N 347 
THR CA  C    sing N N 348 
THR CA  CB   sing N N 349 
THR CA  HA   sing N N 350 
THR C   O    doub N N 351 
THR C   OXT  sing N N 352 
THR CB  OG1  sing N N 353 
THR CB  CG2  sing N N 354 
THR CB  HB   sing N N 355 
THR OG1 HG1  sing N N 356 
THR CG2 HG21 sing N N 357 
THR CG2 HG22 sing N N 358 
THR CG2 HG23 sing N N 359 
THR OXT HXT  sing N N 360 
TRP N   CA   sing N N 361 
TRP N   H    sing N N 362 
TRP N   H2   sing N N 363 
TRP CA  C    sing N N 364 
TRP CA  CB   sing N N 365 
TRP CA  HA   sing N N 366 
TRP C   O    doub N N 367 
TRP C   OXT  sing N N 368 
TRP CB  CG   sing N N 369 
TRP CB  HB2  sing N N 370 
TRP CB  HB3  sing N N 371 
TRP CG  CD1  doub Y N 372 
TRP CG  CD2  sing Y N 373 
TRP CD1 NE1  sing Y N 374 
TRP CD1 HD1  sing N N 375 
TRP CD2 CE2  doub Y N 376 
TRP CD2 CE3  sing Y N 377 
TRP NE1 CE2  sing Y N 378 
TRP NE1 HE1  sing N N 379 
TRP CE2 CZ2  sing Y N 380 
TRP CE3 CZ3  doub Y N 381 
TRP CE3 HE3  sing N N 382 
TRP CZ2 CH2  doub Y N 383 
TRP CZ2 HZ2  sing N N 384 
TRP CZ3 CH2  sing Y N 385 
TRP CZ3 HZ3  sing N N 386 
TRP CH2 HH2  sing N N 387 
TRP OXT HXT  sing N N 388 
TYR N   CA   sing N N 389 
TYR N   H    sing N N 390 
TYR N   H2   sing N N 391 
TYR CA  C    sing N N 392 
TYR CA  CB   sing N N 393 
TYR CA  HA   sing N N 394 
TYR C   O    doub N N 395 
TYR C   OXT  sing N N 396 
TYR CB  CG   sing N N 397 
TYR CB  HB2  sing N N 398 
TYR CB  HB3  sing N N 399 
TYR CG  CD1  doub Y N 400 
TYR CG  CD2  sing Y N 401 
TYR CD1 CE1  sing Y N 402 
TYR CD1 HD1  sing N N 403 
TYR CD2 CE2  doub Y N 404 
TYR CD2 HD2  sing N N 405 
TYR CE1 CZ   doub Y N 406 
TYR CE1 HE1  sing N N 407 
TYR CE2 CZ   sing Y N 408 
TYR CE2 HE2  sing N N 409 
TYR CZ  OH   sing N N 410 
TYR OH  HH   sing N N 411 
TYR OXT HXT  sing N N 412 
VAL N   CA   sing N N 413 
VAL N   H    sing N N 414 
VAL N   H2   sing N N 415 
VAL CA  C    sing N N 416 
VAL CA  CB   sing N N 417 
VAL CA  HA   sing N N 418 
VAL C   O    doub N N 419 
VAL C   OXT  sing N N 420 
VAL CB  CG1  sing N N 421 
VAL CB  CG2  sing N N 422 
VAL CB  HB   sing N N 423 
VAL CG1 HG11 sing N N 424 
VAL CG1 HG12 sing N N 425 
VAL CG1 HG13 sing N N 426 
VAL CG2 HG21 sing N N 427 
VAL CG2 HG22 sing N N 428 
VAL CG2 HG23 sing N N 429 
VAL OXT HXT  sing N N 430 
# 
_pdbx_audit_support.funding_organization   'Wellcome Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           223733/Z/21/Z 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7z1c 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8OWT 
_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]   0.011036 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.010288 
_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]   0.008505 
_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.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_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 6  6  2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H 1  1  0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N 7  7  12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O 8  8  3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S 16 16 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.050   
# 
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   . GLN A 1 1   ? 23.188  7.158   -28.105 1.000 68.009  0 3   GLN AAA N   1 ? 1  
ATOM   2    C CA  . GLN A 1 1   ? 22.438  8.222   -27.380 1.000 66.689  0 3   GLN AAA CA  1 ? 1  
ATOM   3    C C   . GLN A 1 1   ? 20.965  7.823   -27.254 1.000 62.864  0 3   GLN AAA C   1 ? 1  
ATOM   4    O O   . GLN A 1 1   ? 20.544  6.848   -27.904 1.000 60.999  0 3   GLN AAA O   1 ? 1  
ATOM   5    C CB  . GLN A 1 1   ? 22.570  9.578   -28.079 1.000 71.413  0 3   GLN AAA CB  1 ? 1  
ATOM   6    C CG  . GLN A 1 1   ? 21.656  9.770   -29.284 1.000 73.322  0 3   GLN AAA CG  1 ? 1  
ATOM   7    C CD  . GLN A 1 1   ? 22.060  10.967  -30.110 1.000 78.142  0 3   GLN AAA CD  1 ? 1  
ATOM   8    O OE1 . GLN A 1 1   ? 22.631  11.932  -29.605 1.000 79.811  0 3   GLN AAA OE1 1 ? 1  
ATOM   9    N NE2 . GLN A 1 1   ? 21.767  10.914  -31.401 1.000 81.789  0 3   GLN AAA NE2 1 ? 1  
ATOM   10   N N   . VAL A 1 2   ? 20.224  8.558   -26.424 1.000 60.314  0 4   VAL AAA N   1 ? 1  
ATOM   11   C CA  . VAL A 1 2   ? 18.749  8.414   -26.258 1.000 57.315  0 4   VAL AAA CA  1 ? 1  
ATOM   12   C C   . VAL A 1 2   ? 18.084  9.112   -27.446 1.000 54.680  0 4   VAL AAA C   1 ? 1  
ATOM   13   O O   . VAL A 1 2   ? 18.317  10.321  -27.626 1.000 53.484  0 4   VAL AAA O   1 ? 1  
ATOM   14   C CB  . VAL A 1 2   ? 18.253  8.994   -24.920 1.000 58.819  0 4   VAL AAA CB  1 ? 1  
ATOM   15   C CG1 . VAL A 1 2   ? 16.735  8.940   -24.812 1.000 58.328  0 4   VAL AAA CG1 1 ? 1  
ATOM   16   C CG2 . VAL A 1 2   ? 18.899  8.306   -23.728 1.000 59.988  0 4   VAL AAA CG2 1 ? 1  
ATOM   17   N N   . GLN A 1 3   ? 17.295  8.367   -28.220 1.000 52.135  0 5   GLN AAA N   1 ? 1  
ATOM   18   C CA  . GLN A 1 3   ? 16.589  8.866   -29.425 1.000 51.283  0 5   GLN AAA CA  1 ? 1  
ATOM   19   C C   . GLN A 1 3   ? 15.083  8.764   -29.181 1.000 49.348  0 5   GLN AAA C   1 ? 1  
ATOM   20   O O   . GLN A 1 3   ? 14.602  7.658   -28.877 1.000 48.348  0 5   GLN AAA O   1 ? 1  
ATOM   21   C CB  . GLN A 1 3   ? 17.027  8.068   -30.651 1.000 52.644  0 5   GLN AAA CB  1 ? 1  
ATOM   22   C CG  . GLN A 1 3   ? 18.490  8.287   -31.009 1.000 53.713  0 5   GLN AAA CG  1 ? 1  
ATOM   23   C CD  . GLN A 1 3   ? 18.937  7.390   -32.134 1.000 54.740  0 5   GLN AAA CD  1 ? 1  
ATOM   24   O OE1 . GLN A 1 3   ? 18.753  6.176   -32.094 1.000 53.805  0 5   GLN AAA OE1 1 ? 1  
ATOM   25   N NE2 . GLN A 1 3   ? 19.530  7.985   -33.154 1.000 57.892  0 5   GLN AAA NE2 1 ? 1  
ATOM   26   N N   . LEU A 1 4   ? 14.380  9.891   -29.286 1.000 48.949  0 6   LEU AAA N   1 ? 1  
ATOM   27   C CA  . LEU A 1 4   ? 12.903  9.972   -29.165 1.000 50.027  0 6   LEU AAA CA  1 ? 1  
ATOM   28   C C   . LEU A 1 4   ? 12.330  10.394  -30.525 1.000 51.263  0 6   LEU AAA C   1 ? 1  
ATOM   29   O O   . LEU A 1 4   ? 12.451  11.582  -30.874 1.000 52.556  0 6   LEU AAA O   1 ? 1  
ATOM   30   C CB  . LEU A 1 4   ? 12.562  10.967  -28.050 1.000 50.050  0 6   LEU AAA CB  1 ? 1  
ATOM   31   C CG  . LEU A 1 4   ? 13.113  10.609  -26.668 1.000 51.516  0 6   LEU AAA CG  1 ? 1  
ATOM   32   C CD1 . LEU A 1 4   ? 12.722  11.658  -25.634 1.000 52.862  0 6   LEU AAA CD1 1 ? 1  
ATOM   33   C CD2 . LEU A 1 4   ? 12.659  9.217   -26.238 1.000 51.681  0 6   LEU AAA CD2 1 ? 1  
ATOM   34   N N   . VAL A 1 5   ? 11.762  9.444   -31.271 1.000 51.565  0 7   VAL AAA N   1 ? 1  
ATOM   35   C CA  . VAL A 1 5   ? 11.239  9.654   -32.653 1.000 54.297  0 7   VAL AAA CA  1 ? 1  
ATOM   36   C C   . VAL A 1 5   ? 9.725   9.872   -32.568 1.000 54.439  0 7   VAL AAA C   1 ? 1  
ATOM   37   O O   . VAL A 1 5   ? 9.019   8.915   -32.190 1.000 54.033  0 7   VAL AAA O   1 ? 1  
ATOM   38   C CB  . VAL A 1 5   ? 11.586  8.468   -33.573 1.000 55.700  0 7   VAL AAA CB  1 ? 1  
ATOM   39   C CG1 . VAL A 1 5   ? 11.187  8.747   -35.010 1.000 57.329  0 7   VAL AAA CG1 1 ? 1  
ATOM   40   C CG2 . VAL A 1 5   ? 13.057  8.087   -33.485 1.000 56.268  0 7   VAL AAA CG2 1 ? 1  
ATOM   41   N N   . GLU A 1 6   ? 9.263   11.088  -32.889 1.000 56.177  0 8   GLU AAA N   1 ? 1  
ATOM   42   C CA  . GLU A 1 6   ? 7.830   11.486  -32.850 1.000 58.072  0 8   GLU AAA CA  1 ? 1  
ATOM   43   C C   . GLU A 1 6   ? 7.238   11.381  -34.256 1.000 59.559  0 8   GLU AAA C   1 ? 1  
ATOM   44   O O   . GLU A 1 6   ? 7.931   11.770  -35.212 1.000 60.127  0 8   GLU AAA O   1 ? 1  
ATOM   45   C CB  . GLU A 1 6   ? 7.664   12.924  -32.361 1.000 59.077  0 8   GLU AAA CB  1 ? 1  
ATOM   46   C CG  . GLU A 1 6   ? 8.279   13.184  -31.000 1.000 59.596  0 8   GLU AAA CG  1 ? 1  
ATOM   47   C CD  . GLU A 1 6   ? 9.335   14.273  -31.011 1.000 63.946  0 8   GLU AAA CD  1 ? 1  
ATOM   48   O OE1 . GLU A 1 6   ? 10.242  14.206  -31.873 1.000 68.437  0 8   GLU AAA OE1 1 ? 1  
ATOM   49   O OE2 . GLU A 1 6   ? 9.246   15.192  -30.167 1.000 65.340  0 8   GLU AAA OE2 1 ? 1  
ATOM   50   N N   . SER A 1 7   ? 6.002   10.891  -34.364 1.000 60.445  0 9   SER AAA N   1 ? 1  
ATOM   51   C CA  . SER A 1 7   ? 5.205   10.868  -35.620 1.000 64.170  0 9   SER AAA CA  1 ? 1  
ATOM   52   C C   . SER A 1 7   ? 3.716   11.027  -35.293 1.000 64.131  0 9   SER AAA C   1 ? 1  
ATOM   53   O O   . SER A 1 7   ? 3.363   10.977  -34.089 1.000 59.845  0 9   SER AAA O   1 ? 1  
ATOM   54   C CB  . SER A 1 7   ? 5.475   9.615   -36.418 1.000 66.077  0 9   SER AAA CB  1 ? 1  
ATOM   55   O OG  . SER A 1 7   ? 5.247   8.453   -35.637 1.000 66.224  0 9   SER AAA OG  1 ? 1  
ATOM   56   N N   . GLY A 1 8   ? 2.893   11.240  -36.327 1.000 64.894  0 10  GLY AAA N   1 ? 1  
ATOM   57   C CA  . GLY A 1 8   ? 1.424   11.335  -36.225 1.000 65.336  0 10  GLY AAA CA  1 ? 1  
ATOM   58   C C   . GLY A 1 8   ? 0.924   12.771  -36.184 1.000 65.651  0 10  GLY AAA C   1 ? 1  
ATOM   59   O O   . GLY A 1 8   ? -0.279  12.953  -35.927 1.000 69.875  0 10  GLY AAA O   1 ? 1  
ATOM   60   N N   . GLY A 1 9   ? 1.795   13.755  -36.436 1.000 64.581  0 11  GLY AAA N   1 ? 1  
ATOM   61   C CA  . GLY A 1 9   ? 1.434   15.187  -36.488 1.000 65.613  0 11  GLY AAA CA  1 ? 1  
ATOM   62   C C   . GLY A 1 9   ? 0.838   15.572  -37.835 1.000 70.083  0 11  GLY AAA C   1 ? 1  
ATOM   63   O O   . GLY A 1 9   ? 0.341   14.674  -38.544 1.000 68.986  0 11  GLY AAA O   1 ? 1  
ATOM   64   N N   . GLY A 1 10  ? 0.883   16.865  -38.173 1.000 73.059  0 12  GLY AAA N   1 ? 1  
ATOM   65   C CA  . GLY A 1 10  ? 0.463   17.407  -39.481 1.000 76.945  0 12  GLY AAA CA  1 ? 1  
ATOM   66   C C   . GLY A 1 10  ? -0.727  18.342  -39.355 1.000 79.452  0 12  GLY AAA C   1 ? 1  
ATOM   67   O O   . GLY A 1 10  ? -0.871  18.969  -38.286 1.000 79.729  0 12  GLY AAA O   1 ? 1  
ATOM   68   N N   . LEU A 1 11  ? -1.548  18.427  -40.410 1.000 83.174  0 13  LEU AAA N   1 ? 1  
ATOM   69   C CA  . LEU A 1 11  ? -2.721  19.338  -40.509 1.000 84.038  0 13  LEU AAA CA  1 ? 1  
ATOM   70   C C   . LEU A 1 11  ? -3.998  18.580  -40.122 1.000 83.226  0 13  LEU AAA C   1 ? 1  
ATOM   71   O O   . LEU A 1 11  ? -4.149  17.420  -40.549 1.000 82.018  0 13  LEU AAA O   1 ? 1  
ATOM   72   C CB  . LEU A 1 11  ? -2.819  19.883  -41.938 1.000 89.243  0 13  LEU AAA CB  1 ? 1  
ATOM   73   C CG  . LEU A 1 11  ? -3.712  21.113  -42.106 1.000 91.720  0 13  LEU AAA CG  1 ? 1  
ATOM   74   C CD1 . LEU A 1 11  ? -3.014  22.358  -41.587 1.000 91.997  0 13  LEU AAA CD1 1 ? 1  
ATOM   75   C CD2 . LEU A 1 11  ? -4.134  21.304  -43.556 1.000 95.820  0 13  LEU AAA CD2 1 ? 1  
ATOM   76   N N   . VAL A 1 12  ? -4.862  19.220  -39.325 1.000 83.794  0 14  VAL AAA N   1 ? 1  
ATOM   77   C CA  . VAL A 1 12  ? -6.254  18.776  -39.009 1.000 85.523  0 14  VAL AAA CA  1 ? 1  
ATOM   78   C C   . VAL A 1 12  ? -7.127  20.028  -38.857 1.000 87.617  0 14  VAL AAA C   1 ? 1  
ATOM   79   O O   . VAL A 1 12  ? -6.577  21.146  -38.932 1.000 90.677  0 14  VAL AAA O   1 ? 1  
ATOM   80   C CB  . VAL A 1 12  ? -6.317  17.890  -37.746 1.000 82.992  0 14  VAL AAA CB  1 ? 1  
ATOM   81   C CG1 . VAL A 1 12  ? -5.713  16.517  -37.985 1.000 82.959  0 14  VAL AAA CG1 1 ? 1  
ATOM   82   C CG2 . VAL A 1 12  ? -5.675  18.557  -36.540 1.000 80.545  0 14  VAL AAA CG2 1 ? 1  
ATOM   83   N N   . GLN A 1 13  ? -8.435  19.840  -38.660 1.000 86.879  0 15  GLN AAA N   1 ? 1  
ATOM   84   C CA  . GLN A 1 13  ? -9.414  20.935  -38.426 1.000 88.015  0 15  GLN AAA CA  1 ? 1  
ATOM   85   C C   . GLN A 1 13  ? -10.118 20.685  -37.088 1.000 84.691  0 15  GLN AAA C   1 ? 1  
ATOM   86   O O   . GLN A 1 13  ? -10.098 19.526  -36.622 1.000 81.228  0 15  GLN AAA O   1 ? 1  
ATOM   87   C CB  . GLN A 1 13  ? -10.413 21.018  -39.583 1.000 92.541  0 15  GLN AAA CB  1 ? 1  
ATOM   88   C CG  . GLN A 1 13  ? -9.765  21.043  -40.962 1.000 95.803  0 15  GLN AAA CG  1 ? 1  
ATOM   89   C CD  . GLN A 1 13  ? -10.657 21.652  -42.016 1.000 100.258 0 15  GLN AAA CD  1 ? 1  
ATOM   90   O OE1 . GLN A 1 13  ? -10.189 22.296  -42.951 1.000 103.803 0 15  GLN AAA OE1 1 ? 1  
ATOM   91   N NE2 . GLN A 1 13  ? -11.957 21.459  -41.865 1.000 101.316 0 15  GLN AAA NE2 1 ? 1  
ATOM   92   N N   . ALA A 1 14  ? -10.707 21.733  -36.503 1.000 84.279  0 16  ALA AAA N   1 ? 1  
ATOM   93   C CA  . ALA A 1 14  ? -11.357 21.712  -35.169 1.000 83.129  0 16  ALA AAA CA  1 ? 1  
ATOM   94   C C   . ALA A 1 14  ? -12.344 20.538  -35.084 1.000 82.863  0 16  ALA AAA C   1 ? 1  
ATOM   95   O O   . ALA A 1 14  ? -13.051 20.278  -36.081 1.000 85.513  0 16  ALA AAA O   1 ? 1  
ATOM   96   C CB  . ALA A 1 14  ? -12.035 23.032  -34.891 1.000 84.574  0 16  ALA AAA CB  1 ? 1  
ATOM   97   N N   . GLY A 1 15  ? -12.365 19.846  -33.939 1.000 80.558  0 17  GLY AAA N   1 ? 1  
ATOM   98   C CA  . GLY A 1 15  ? -13.208 18.661  -33.686 1.000 79.857  0 17  GLY AAA CA  1 ? 1  
ATOM   99   C C   . GLY A 1 15  ? -12.569 17.373  -34.184 1.000 79.047  0 17  GLY AAA C   1 ? 1  
ATOM   100  O O   . GLY A 1 15  ? -13.147 16.299  -33.920 1.000 79.741  0 17  GLY AAA O   1 ? 1  
ATOM   101  N N   . GLY A 1 16  ? -11.423 17.461  -34.869 1.000 78.636  0 18  GLY AAA N   1 ? 1  
ATOM   102  C CA  . GLY A 1 16  ? -10.718 16.314  -35.473 1.000 78.459  0 18  GLY AAA CA  1 ? 1  
ATOM   103  C C   . GLY A 1 16  ? -9.835  15.597  -34.465 1.000 76.060  0 18  GLY AAA C   1 ? 1  
ATOM   104  O O   . GLY A 1 16  ? -9.433  16.228  -33.477 1.000 71.489  0 18  GLY AAA O   1 ? 1  
ATOM   105  N N   . SER A 1 17  ? -9.552  14.317  -34.724 1.000 78.786  0 19  SER AAA N   1 ? 1  
ATOM   106  C CA  . SER A 1 17  ? -8.751  13.398  -33.873 1.000 77.611  0 19  SER AAA CA  1 ? 1  
ATOM   107  C C   . SER A 1 17  ? -7.367  13.182  -34.499 1.000 76.572  0 19  SER AAA C   1 ? 1  
ATOM   108  O O   . SER A 1 17  ? -7.302  12.764  -35.672 1.000 79.704  0 19  SER AAA O   1 ? 1  
ATOM   109  C CB  . SER A 1 17  ? -9.481  12.089  -33.667 1.000 80.333  0 19  SER AAA CB  1 ? 1  
ATOM   110  O OG  . SER A 1 17  ? -8.585  10.983  -33.692 1.000 81.818  0 19  SER AAA OG  1 ? 1  
ATOM   111  N N   . LEU A 1 18  ? -6.311  13.450  -33.726 1.000 73.990  0 20  LEU AAA N   1 ? 1  
ATOM   112  C CA  . LEU A 1 18  ? -4.886  13.246  -34.104 1.000 71.605  0 20  LEU AAA CA  1 ? 1  
ATOM   113  C C   . LEU A 1 18  ? -4.204  12.429  -32.998 1.000 68.460  0 20  LEU AAA C   1 ? 1  
ATOM   114  O O   . LEU A 1 18  ? -4.413  12.762  -31.817 1.000 68.211  0 20  LEU AAA O   1 ? 1  
ATOM   115  C CB  . LEU A 1 18  ? -4.238  14.625  -34.279 1.000 71.497  0 20  LEU AAA CB  1 ? 1  
ATOM   116  C CG  . LEU A 1 18  ? -3.042  14.700  -35.226 1.000 73.088  0 20  LEU AAA CG  1 ? 1  
ATOM   117  C CD1 . LEU A 1 18  ? -3.360  14.077  -36.581 1.000 74.423  0 20  LEU AAA CD1 1 ? 1  
ATOM   118  C CD2 . LEU A 1 18  ? -2.591  16.143  -35.397 1.000 73.454  0 20  LEU AAA CD2 1 ? 1  
ATOM   119  N N   . ARG A 1 19  ? -3.445  11.390  -33.362 1.000 67.107  0 21  ARG AAA N   1 ? 1  
ATOM   120  C CA  . ARG A 1 19  ? -2.753  10.484  -32.404 1.000 66.137  0 21  ARG AAA CA  1 ? 1  
ATOM   121  C C   . ARG A 1 19  ? -1.235  10.623  -32.575 1.000 63.526  0 21  ARG AAA C   1 ? 1  
ATOM   122  O O   . ARG A 1 19  ? -0.682  10.016  -33.518 1.000 63.040  0 21  ARG AAA O   1 ? 1  
ATOM   123  C CB  . ARG A 1 19  ? -3.187  9.028   -32.604 1.000 69.166  0 21  ARG AAA CB  1 ? 1  
ATOM   124  C CG  . ARG A 1 19  ? -2.654  8.079   -31.539 1.000 70.606  0 21  ARG AAA CG  1 ? 1  
ATOM   125  C CD  . ARG A 1 19  ? -2.835  6.615   -31.886 1.000 75.670  0 21  ARG AAA CD  1 ? 1  
ATOM   126  N NE  . ARG A 1 19  ? -2.508  5.753   -30.755 1.000 78.029  0 21  ARG AAA NE  1 ? 1  
ATOM   127  C CZ  . ARG A 1 19  ? -2.632  4.426   -30.736 1.000 83.417  0 21  ARG AAA CZ  1 ? 1  
ATOM   128  N NH1 . ARG A 1 19  ? -3.056  3.774   -31.808 1.000 85.998  0 21  ARG AAA NH1 1 ? 1  
ATOM   129  N NH2 . ARG A 1 19  ? -2.315  3.752   -29.640 1.000 83.451  0 21  ARG AAA NH2 1 ? 1  
ATOM   130  N N   . LEU A 1 20  ? -0.589  11.383  -31.686 1.000 68.174  0 22  LEU AAA N   1 ? 2  
ATOM   131  C CA  . LEU A 1 20  ? 0.890   11.493  -31.627 1.000 65.862  0 22  LEU AAA CA  1 ? 2  
ATOM   132  C C   . LEU A 1 20  ? 1.440   10.202  -31.018 1.000 62.424  0 22  LEU AAA C   1 ? 2  
ATOM   133  O O   . LEU A 1 20  ? 0.785   9.639   -30.125 1.000 62.766  0 22  LEU AAA O   1 ? 2  
ATOM   134  C CB  . LEU A 1 20  ? 1.309   12.717  -30.806 1.000 65.509  0 22  LEU AAA CB  1 ? 2  
ATOM   135  C CG  . LEU A 1 20  ? 0.710   14.058  -31.231 1.000 69.369  0 22  LEU AAA CG  1 ? 2  
ATOM   136  C CD1 . LEU A 1 20  ? 1.437   15.209  -30.549 1.000 69.800  0 22  LEU AAA CD1 1 ? 2  
ATOM   137  C CD2 . LEU A 1 20  ? 0.748   14.235  -32.741 1.000 73.221  0 22  LEU AAA CD2 1 ? 2  
ATOM   138  N N   . SER A 1 21  ? 2.582   9.740   -31.527 1.000 60.826  0 23  SER AAA N   1 ? 2  
ATOM   139  C CA  . SER A 1 21  ? 3.355   8.587   -31.006 1.000 58.251  0 23  SER AAA CA  1 ? 2  
ATOM   140  C C   . SER A 1 21  ? 4.817   9.012   -30.877 1.000 56.845  0 23  SER AAA C   1 ? 2  
ATOM   141  O O   . SER A 1 21  ? 5.272   9.836   -31.694 1.000 57.933  0 23  SER AAA O   1 ? 2  
ATOM   142  C CB  . SER A 1 21  ? 3.207   7.381   -31.892 1.000 59.774  0 23  SER AAA CB  1 ? 2  
ATOM   143  O OG  . SER A 1 21  ? 3.916   7.559   -33.106 1.000 61.526  0 23  SER AAA OG  1 ? 2  
ATOM   144  N N   . CYS A 1 22  ? 5.507   8.493   -29.866 1.000 54.814  0 24  CYS AAA N   1 ? 2  
ATOM   145  C CA  . CYS A 1 22  ? 6.943   8.750   -29.614 1.000 54.744  0 24  CYS AAA CA  1 ? 2  
ATOM   146  C C   . CYS A 1 22  ? 7.621   7.417   -29.281 1.000 53.641  0 24  CYS AAA C   1 ? 2  
ATOM   147  O O   . CYS A 1 22  ? 7.330   6.851   -28.205 1.000 51.767  0 24  CYS AAA O   1 ? 2  
ATOM   148  C CB  . CYS A 1 22  ? 7.130   9.786   -28.510 1.000 55.223  0 24  CYS AAA CB  1 ? 2  
ATOM   149  S SG  . CYS A 1 22  ? 8.822   9.817   -27.870 1.000 56.022  0 24  CYS AAA SG  1 ? 2  
ATOM   150  N N   . ALA A 1 23  ? 8.456   6.920   -30.199 1.000 53.314  0 25  ALA AAA N   1 ? 2  
ATOM   151  C CA  . ALA A 1 23  ? 9.259   5.684   -30.042 1.000 52.859  0 25  ALA AAA CA  1 ? 2  
ATOM   152  C C   . ALA A 1 23  ? 10.626  6.058   -29.457 1.000 52.404  0 25  ALA AAA C   1 ? 2  
ATOM   153  O O   . ALA A 1 23  ? 11.271  6.979   -29.999 1.000 53.523  0 25  ALA AAA O   1 ? 2  
ATOM   154  C CB  . ALA A 1 23  ? 9.393   4.978   -31.366 1.000 53.734  0 25  ALA AAA CB  1 ? 2  
ATOM   155  N N   . ALA A 1 24  ? 11.036  5.377   -28.385 1.000 51.204  0 26  ALA AAA N   1 ? 2  
ATOM   156  C CA  . ALA A 1 24  ? 12.268  5.661   -27.615 1.000 51.356  0 26  ALA AAA CA  1 ? 2  
ATOM   157  C C   . ALA A 1 24  ? 13.282  4.540   -27.848 1.000 52.264  0 26  ALA AAA C   1 ? 2  
ATOM   158  O O   . ALA A 1 24  ? 12.891  3.358   -27.821 1.000 54.009  0 26  ALA AAA O   1 ? 2  
ATOM   159  C CB  . ALA A 1 24  ? 11.943  5.802   -26.150 1.000 49.612  0 26  ALA AAA CB  1 ? 2  
ATOM   160  N N   . SER A 1 25  ? 14.542  4.910   -28.062 1.000 53.041  0 27  SER AAA N   1 ? 2  
ATOM   161  C CA  . SER A 1 25  ? 15.705  3.989   -28.046 1.000 55.055  0 27  SER AAA CA  1 ? 2  
ATOM   162  C C   . SER A 1 25  ? 16.700  4.452   -26.977 1.000 54.136  0 27  SER AAA C   1 ? 2  
ATOM   163  O O   . SER A 1 25  ? 17.189  5.590   -27.081 1.000 54.398  0 27  SER AAA O   1 ? 2  
ATOM   164  C CB  . SER A 1 25  ? 16.344  3.912   -29.402 1.000 57.168  0 27  SER AAA CB  1 ? 2  
ATOM   165  O OG  . SER A 1 25  ? 17.437  3.005   -29.389 1.000 60.183  0 27  SER AAA OG  1 ? 2  
ATOM   166  N N   . GLY A 1 26  ? 16.936  3.618   -25.963 1.000 53.969  0 28  GLY AAA N   1 ? 2  
ATOM   167  C CA  . GLY A 1 26  ? 18.111  3.716   -25.081 1.000 57.072  0 28  GLY AAA CA  1 ? 2  
ATOM   168  C C   . GLY A 1 26  ? 17.896  4.524   -23.813 1.000 57.760  0 28  GLY AAA C   1 ? 2  
ATOM   169  O O   . GLY A 1 26  ? 18.920  4.901   -23.197 1.000 65.168  0 28  GLY AAA O   1 ? 2  
ATOM   170  N N   . GLY A 1 27  ? 16.652  4.769   -23.403 1.000 53.561  0 29  GLY AAA N   1 ? 2  
ATOM   171  C CA  . GLY A 1 27  ? 16.363  5.510   -22.157 1.000 54.213  0 29  GLY AAA CA  1 ? 2  
ATOM   172  C C   . GLY A 1 27  ? 15.919  4.603   -21.019 1.000 51.823  0 29  GLY AAA C   1 ? 2  
ATOM   173  O O   . GLY A 1 27  ? 15.321  5.124   -20.059 1.000 52.155  0 29  GLY AAA O   1 ? 2  
ATOM   174  N N   . THR A 1 28  ? 16.206  3.299   -21.113 1.000 50.605  0 30  THR AAA N   1 ? 2  
ATOM   175  C CA  . THR A 1 28  ? 15.581  2.230   -20.286 1.000 48.759  0 30  THR AAA CA  1 ? 2  
ATOM   176  C C   . THR A 1 28  ? 14.109  2.603   -20.094 1.000 46.063  0 30  THR AAA C   1 ? 2  
ATOM   177  O O   . THR A 1 28  ? 13.717  2.925   -18.961 1.000 45.472  0 30  THR AAA O   1 ? 2  
ATOM   178  C CB  . THR A 1 28  ? 16.343  2.007   -18.974 1.000 48.213  0 30  THR AAA CB  1 ? 2  
ATOM   179  O OG1 . THR A 1 28  ? 17.726  1.849   -19.298 1.000 49.844  0 30  THR AAA OG1 1 ? 2  
ATOM   180  C CG2 . THR A 1 28  ? 15.862  0.789   -18.220 1.000 47.772  0 30  THR AAA CG2 1 ? 2  
ATOM   181  N N   . PHE A 1 29  ? 13.349  2.587   -21.192 1.000 45.660  0 31  PHE AAA N   1 ? 2  
ATOM   182  C CA  . PHE A 1 29  ? 11.953  3.087   -21.289 1.000 45.039  0 31  PHE AAA CA  1 ? 2  
ATOM   183  C C   . PHE A 1 29  ? 11.126  2.608   -20.091 1.000 44.008  0 31  PHE AAA C   1 ? 2  
ATOM   184  O O   . PHE A 1 29  ? 10.380  3.426   -19.524 1.000 44.203  0 31  PHE AAA O   1 ? 2  
ATOM   185  C CB  . PHE A 1 29  ? 11.297  2.630   -22.597 1.000 45.231  0 31  PHE AAA CB  1 ? 2  
ATOM   186  C CG  . PHE A 1 29  ? 9.979   3.303   -22.881 1.000 45.135  0 31  PHE AAA CG  1 ? 2  
ATOM   187  C CD1 . PHE A 1 29  ? 9.941   4.584   -23.411 1.000 45.617  0 31  PHE AAA CD1 1 ? 2  
ATOM   188  C CD2 . PHE A 1 29  ? 8.779   2.657   -22.620 1.000 44.368  0 31  PHE AAA CD2 1 ? 2  
ATOM   189  C CE1 . PHE A 1 29  ? 8.728   5.209   -23.665 1.000 47.095  0 31  PHE AAA CE1 1 ? 2  
ATOM   190  C CE2 . PHE A 1 29  ? 7.567   3.272   -22.904 1.000 45.421  0 31  PHE AAA CE2 1 ? 2  
ATOM   191  C CZ  . PHE A 1 29  ? 7.542   4.548   -23.422 1.000 46.529  0 31  PHE AAA CZ  1 ? 2  
ATOM   192  N N   . SER A 1 30  ? 11.275  1.333   -19.717 1.000 45.260  0 32  SER AAA N   1 ? 2  
ATOM   193  C CA  . SER A 1 30  ? 10.481  0.635   -18.670 1.000 45.684  0 32  SER AAA CA  1 ? 2  
ATOM   194  C C   . SER A 1 30  ? 10.523  1.375   -17.330 1.000 45.457  0 32  SER AAA C   1 ? 2  
ATOM   195  O O   . SER A 1 30  ? 9.512   1.302   -16.623 1.000 46.876  0 32  SER AAA O   1 ? 2  
ATOM   196  C CB  . SER A 1 30  ? 10.919  -0.794  -18.503 1.000 47.507  0 32  SER AAA CB  1 ? 2  
ATOM   197  O OG  . SER A 1 30  ? 10.125  -1.646  -19.315 1.000 49.910  0 32  SER AAA OG  1 ? 2  
ATOM   198  N N   . THR A 1 31  ? 11.638  2.032   -16.987 1.000 46.667  0 33  THR AAA N   1 ? 2  
ATOM   199  C CA  . THR A 1 31  ? 11.835  2.736   -15.686 1.000 45.621  0 33  THR AAA CA  1 ? 2  
ATOM   200  C C   . THR A 1 31  ? 11.827  4.257   -15.891 1.000 44.961  0 33  THR AAA C   1 ? 2  
ATOM   201  O O   . THR A 1 31  ? 12.241  4.974   -14.958 1.000 46.710  0 33  THR AAA O   1 ? 2  
ATOM   202  C CB  . THR A 1 31  ? 13.128  2.278   -14.996 1.000 46.476  0 33  THR AAA CB  1 ? 2  
ATOM   203  O OG1 . THR A 1 31  ? 14.227  2.664   -15.826 1.000 44.686  0 33  THR AAA OG1 1 ? 2  
ATOM   204  C CG2 . THR A 1 31  ? 13.157  0.787   -14.742 1.000 47.341  0 33  THR AAA CG2 1 ? 2  
ATOM   205  N N   . ALA A 1 32  ? 11.349  4.736   -17.044 1.000 43.993  0 34  ALA AAA N   1 ? 2  
ATOM   206  C CA  . ALA A 1 32  ? 11.306  6.174   -17.402 1.000 44.927  0 34  ALA AAA CA  1 ? 2  
ATOM   207  C C   . ALA A 1 32  ? 9.862   6.691   -17.365 1.000 44.422  0 34  ALA AAA C   1 ? 2  
ATOM   208  O O   . ALA A 1 32  ? 8.981   6.061   -17.973 1.000 44.756  0 34  ALA AAA O   1 ? 2  
ATOM   209  C CB  . ALA A 1 32  ? 11.926  6.386   -18.763 1.000 46.353  0 34  ALA AAA CB  1 ? 2  
ATOM   210  N N   . ALA A 1 33  ? 9.636   7.806   -16.670 1.000 43.645  0 35  ALA AAA N   1 ? 2  
ATOM   211  C CA  . ALA A 1 33  ? 8.408   8.620   -16.798 1.000 44.083  0 35  ALA AAA CA  1 ? 2  
ATOM   212  C C   . ALA A 1 33  ? 8.485   9.369   -18.131 1.000 44.199  0 35  ALA AAA C   1 ? 2  
ATOM   213  O O   . ALA A 1 33  ? 9.558   9.909   -18.440 1.000 45.517  0 35  ALA AAA O   1 ? 2  
ATOM   214  C CB  . ALA A 1 33  ? 8.264   9.563   -15.627 1.000 44.208  0 35  ALA AAA CB  1 ? 2  
ATOM   215  N N   . MET A 1 34  ? 7.391   9.381   -18.893 1.000 44.778  0 36  MET AAA N   1 ? 2  
ATOM   216  C CA  . MET A 1 34  ? 7.334   9.968   -20.256 1.000 44.753  0 36  MET AAA CA  1 ? 2  
ATOM   217  C C   . MET A 1 34  ? 6.330   11.122  -20.265 1.000 45.562  0 36  MET AAA C   1 ? 2  
ATOM   218  O O   . MET A 1 34  ? 5.314   11.029  -19.556 1.000 46.595  0 36  MET AAA O   1 ? 2  
ATOM   219  C CB  . MET A 1 34  ? 6.922   8.910   -21.279 1.000 45.490  0 36  MET AAA CB  1 ? 2  
ATOM   220  C CG  . MET A 1 34  ? 7.914   7.760   -21.412 1.000 46.032  0 36  MET AAA CG  1 ? 2  
ATOM   221  S SD  . MET A 1 34  ? 9.581   8.242   -21.917 1.000 46.638  0 36  MET AAA SD  1 ? 2  
ATOM   222  C CE  . MET A 1 34  ? 9.199   9.026   -23.482 1.000 47.946  0 36  MET AAA CE  1 ? 2  
ATOM   223  N N   . GLY A 1 35  ? 6.627   12.176  -21.027 1.000 46.544  0 37  GLY AAA N   1 ? 2  
ATOM   224  C CA  . GLY A 1 35  ? 5.830   13.416  -21.068 1.000 48.017  0 37  GLY AAA CA  1 ? 2  
ATOM   225  C C   . GLY A 1 35  ? 5.662   13.945  -22.482 1.000 49.578  0 37  GLY AAA C   1 ? 2  
ATOM   226  O O   . GLY A 1 35  ? 6.535   13.682  -23.332 1.000 48.517  0 37  GLY AAA O   1 ? 2  
ATOM   227  N N   . TRP A 1 36  ? 4.559   14.657  -22.718 1.000 49.688  0 38  TRP AAA N   1 ? 2  
ATOM   228  C CA  . TRP A 1 36  ? 4.304   15.454  -23.943 1.000 50.991  0 38  TRP AAA CA  1 ? 2  
ATOM   229  C C   . TRP A 1 36  ? 4.296   16.936  -23.567 1.000 52.893  0 38  TRP AAA C   1 ? 2  
ATOM   230  O O   . TRP A 1 36  ? 3.481   17.325  -22.710 1.000 52.762  0 38  TRP AAA O   1 ? 2  
ATOM   231  C CB  . TRP A 1 36  ? 2.996   15.016  -24.610 1.000 50.887  0 38  TRP AAA CB  1 ? 2  
ATOM   232  C CG  . TRP A 1 36  ? 3.120   13.711  -25.330 1.000 49.617  0 38  TRP AAA CG  1 ? 2  
ATOM   233  C CD1 . TRP A 1 36  ? 2.754   12.474  -24.881 1.000 47.624  0 38  TRP AAA CD1 1 ? 2  
ATOM   234  C CD2 . TRP A 1 36  ? 3.689   13.512  -26.633 1.000 50.294  0 38  TRP AAA CD2 1 ? 2  
ATOM   235  N NE1 . TRP A 1 36  ? 3.044   11.521  -25.819 1.000 47.321  0 38  TRP AAA NE1 1 ? 2  
ATOM   236  C CE2 . TRP A 1 36  ? 3.621   12.129  -26.903 1.000 49.283  0 38  TRP AAA CE2 1 ? 2  
ATOM   237  C CE3 . TRP A 1 36  ? 4.243   14.367  -27.593 1.000 52.450  0 38  TRP AAA CE3 1 ? 2  
ATOM   238  C CZ2 . TRP A 1 36  ? 4.085   11.588  -28.100 1.000 50.442  0 38  TRP AAA CZ2 1 ? 2  
ATOM   239  C CZ3 . TRP A 1 36  ? 4.704   13.831  -28.774 1.000 53.491  0 38  TRP AAA CZ3 1 ? 2  
ATOM   240  C CH2 . TRP A 1 36  ? 4.626   12.459  -29.020 1.000 52.823  0 38  TRP AAA CH2 1 ? 2  
ATOM   241  N N   . PHE A 1 37  ? 5.214   17.707  -24.148 1.000 55.297  0 39  PHE AAA N   1 ? 2  
ATOM   242  C CA  . PHE A 1 37  ? 5.285   19.185  -24.036 1.000 59.122  0 39  PHE AAA CA  1 ? 2  
ATOM   243  C C   . PHE A 1 37  ? 4.864   19.788  -25.376 1.000 62.649  0 39  PHE AAA C   1 ? 2  
ATOM   244  O O   . PHE A 1 37  ? 5.062   19.133  -26.415 1.000 63.156  0 39  PHE AAA O   1 ? 2  
ATOM   245  C CB  . PHE A 1 37  ? 6.695   19.630  -23.649 1.000 60.031  0 39  PHE AAA CB  1 ? 2  
ATOM   246  C CG  . PHE A 1 37  ? 7.068   19.378  -22.209 1.000 58.577  0 39  PHE AAA CG  1 ? 2  
ATOM   247  C CD1 . PHE A 1 37  ? 7.359   18.097  -21.766 1.000 56.443  0 39  PHE AAA CD1 1 ? 2  
ATOM   248  C CD2 . PHE A 1 37  ? 7.149   20.425  -21.303 1.000 60.289  0 39  PHE AAA CD2 1 ? 2  
ATOM   249  C CE1 . PHE A 1 37  ? 7.716   17.868  -20.445 1.000 55.305  0 39  PHE AAA CE1 1 ? 2  
ATOM   250  C CE2 . PHE A 1 37  ? 7.510   20.194  -19.984 1.000 59.250  0 39  PHE AAA CE2 1 ? 2  
ATOM   251  C CZ  . PHE A 1 37  ? 7.790   18.916  -19.556 1.000 56.375  0 39  PHE AAA CZ  1 ? 2  
ATOM   252  N N   . ARG A 1 38  ? 4.295   20.993  -25.350 1.000 66.185  0 40  ARG AAA N   1 ? 2  
ATOM   253  C CA  . ARG A 1 38  ? 3.942   21.758  -26.572 1.000 71.525  0 40  ARG AAA CA  1 ? 2  
ATOM   254  C C   . ARG A 1 38  ? 4.462   23.189  -26.427 1.000 75.563  0 40  ARG AAA C   1 ? 2  
ATOM   255  O O   . ARG A 1 38  ? 4.576   23.666  -25.280 1.000 75.320  0 40  ARG AAA O   1 ? 2  
ATOM   256  C CB  . ARG A 1 38  ? 2.431   21.715  -26.824 1.000 72.977  0 40  ARG AAA CB  1 ? 2  
ATOM   257  C CG  . ARG A 1 38  ? 1.605   22.623  -25.924 1.000 74.173  0 40  ARG AAA CG  1 ? 2  
ATOM   258  C CD  . ARG A 1 38  ? 0.132   22.540  -26.272 1.000 75.537  0 40  ARG AAA CD  1 ? 2  
ATOM   259  N NE  . ARG A 1 38  ? -0.707  23.168  -25.261 1.000 76.594  0 40  ARG AAA NE  1 ? 2  
ATOM   260  C CZ  . ARG A 1 38  ? -2.036  23.196  -25.287 1.000 77.962  0 40  ARG AAA CZ  1 ? 2  
ATOM   261  N NH1 . ARG A 1 38  ? -2.699  22.626  -26.281 1.000 79.027  0 40  ARG AAA NH1 1 ? 2  
ATOM   262  N NH2 . ARG A 1 38  ? -2.698  23.798  -24.314 1.000 78.637  0 40  ARG AAA NH2 1 ? 2  
ATOM   263  N N   . GLN A 1 39  ? 4.768   23.828  -27.557 1.000 80.127  0 41  GLN AAA N   1 ? 2  
ATOM   264  C CA  . GLN A 1 39  ? 5.229   25.237  -27.631 1.000 85.871  0 41  GLN AAA CA  1 ? 2  
ATOM   265  C C   . GLN A 1 39  ? 4.566   25.914  -28.834 1.000 90.494  0 41  GLN AAA C   1 ? 2  
ATOM   266  O O   . GLN A 1 39  ? 4.972   25.628  -29.977 1.000 91.942  0 41  GLN AAA O   1 ? 2  
ATOM   267  C CB  . GLN A 1 39  ? 6.754   25.296  -27.729 1.000 87.111  0 41  GLN AAA CB  1 ? 2  
ATOM   268  C CG  . GLN A 1 39  ? 7.312   26.702  -27.568 1.000 92.271  0 41  GLN AAA CG  1 ? 2  
ATOM   269  C CD  . GLN A 1 39  ? 8.818   26.714  -27.508 1.000 93.916  0 41  GLN AAA CD  1 ? 2  
ATOM   270  O OE1 . GLN A 1 39  ? 9.483   25.802  -27.997 1.000 93.952  0 41  GLN AAA OE1 1 ? 2  
ATOM   271  N NE2 . GLN A 1 39  ? 9.365   27.766  -26.921 1.000 97.098  0 41  GLN AAA NE2 1 ? 2  
ATOM   272  N N   . ALA A 1 40  ? 3.567   26.761  -28.572 1.000 94.223  0 42  ALA AAA N   1 ? 2  
ATOM   273  C CA  . ALA A 1 40  ? 2.957   27.685  -29.553 1.000 100.469 0 42  ALA AAA CA  1 ? 2  
ATOM   274  C C   . ALA A 1 40  ? 4.032   28.656  -30.032 1.000 105.685 0 42  ALA AAA C   1 ? 2  
ATOM   275  O O   . ALA A 1 40  ? 4.977   28.937  -29.300 1.000 103.936 0 42  ALA AAA O   1 ? 2  
ATOM   276  C CB  . ALA A 1 40  ? 1.785   28.400  -28.923 1.000 102.184 0 42  ALA AAA CB  1 ? 2  
ATOM   277  N N   . PRO A 1 41  ? 3.938   29.184  -31.272 1.000 111.938 0 43  PRO AAA N   1 ? 2  
ATOM   278  C CA  . PRO A 1 41  ? 4.994   30.038  -31.818 1.000 116.891 0 43  PRO AAA CA  1 ? 2  
ATOM   279  C C   . PRO A 1 41  ? 5.137   31.421  -31.159 1.000 122.138 0 43  PRO AAA C   1 ? 2  
ATOM   280  O O   . PRO A 1 41  ? 6.002   32.150  -31.607 1.000 127.092 0 43  PRO AAA O   1 ? 2  
ATOM   281  C CB  . PRO A 1 41  ? 4.587   30.204  -33.292 1.000 120.570 0 43  PRO AAA CB  1 ? 2  
ATOM   282  C CG  . PRO A 1 41  ? 3.081   30.049  -33.278 1.000 120.334 0 43  PRO AAA CG  1 ? 2  
ATOM   283  C CD  . PRO A 1 41  ? 2.821   29.006  -32.211 1.000 113.864 0 43  PRO AAA CD  1 ? 2  
ATOM   284  N N   . GLY A 1 42  ? 4.315   31.761  -30.156 1.000 121.552 0 44  GLY AAA N   1 ? 2  
ATOM   285  C CA  . GLY A 1 42  ? 4.444   33.004  -29.367 1.000 125.017 0 44  GLY AAA CA  1 ? 2  
ATOM   286  C C   . GLY A 1 42  ? 4.442   32.757  -27.866 1.000 121.955 0 44  GLY AAA C   1 ? 2  
ATOM   287  O O   . GLY A 1 42  ? 4.313   33.746  -27.117 1.000 125.718 0 44  GLY AAA O   1 ? 2  
ATOM   288  N N   . GLU A 1 43  ? 4.541   31.495  -27.431 1.000 115.663 0 45  GLU AAA N   1 ? 2  
ATOM   289  C CA  . GLU A 1 43  ? 4.501   31.075  -26.001 1.000 110.807 0 45  GLU AAA CA  1 ? 2  
ATOM   290  C C   . GLU A 1 43  ? 5.802   30.338  -25.660 1.000 106.528 0 45  GLU AAA C   1 ? 2  
ATOM   291  O O   . GLU A 1 43  ? 6.666   30.215  -26.549 1.000 106.541 0 45  GLU AAA O   1 ? 2  
ATOM   292  C CB  . GLU A 1 43  ? 3.287   30.178  -25.725 1.000 106.944 0 45  GLU AAA CB  1 ? 2  
ATOM   293  C CG  . GLU A 1 43  ? 1.950   30.778  -26.131 1.000 110.107 0 45  GLU AAA CG  1 ? 2  
ATOM   294  C CD  . GLU A 1 43  ? 1.659   32.158  -25.566 1.000 114.820 0 45  GLU AAA CD  1 ? 2  
ATOM   295  O OE1 . GLU A 1 43  ? 1.817   32.344  -24.344 1.000 114.141 0 45  GLU AAA OE1 1 ? 2  
ATOM   296  O OE2 . GLU A 1 43  ? 1.280   33.046  -26.354 1.000 119.287 0 45  GLU AAA OE2 1 ? 2  
ATOM   297  N N   . GLU A 1 44  ? 5.927   29.867  -24.413 1.000 103.231 0 46  GLU AAA N   1 ? 2  
ATOM   298  C CA  . GLU A 1 44  ? 7.052   29.026  -23.922 1.000 98.748  0 46  GLU AAA CA  1 ? 2  
ATOM   299  C C   . GLU A 1 44  ? 6.545   27.605  -23.649 1.000 92.435  0 46  GLU AAA C   1 ? 2  
ATOM   300  O O   . GLU A 1 44  ? 5.320   27.436  -23.462 1.000 89.337  0 46  GLU AAA O   1 ? 2  
ATOM   301  C CB  . GLU A 1 44  ? 7.671   29.654  -22.671 1.000 99.724  0 46  GLU AAA CB  1 ? 2  
ATOM   302  C CG  . GLU A 1 44  ? 8.206   31.053  -22.910 1.000 106.024 0 46  GLU AAA CG  1 ? 2  
ATOM   303  C CD  . GLU A 1 44  ? 8.885   31.713  -21.722 1.000 108.077 0 46  GLU AAA CD  1 ? 2  
ATOM   304  O OE1 . GLU A 1 44  ? 8.782   31.182  -20.595 1.000 105.529 0 46  GLU AAA OE1 1 ? 2  
ATOM   305  O OE2 . GLU A 1 44  ? 9.519   32.763  -21.930 1.000 112.085 0 46  GLU AAA OE2 1 ? 2  
ATOM   306  N N   . ARG A 1 45  ? 7.463   26.629  -23.647 1.000 89.728  0 47  ARG AAA N   1 ? 3  
ATOM   307  C CA  . ARG A 1 45  ? 7.198   25.183  -23.405 1.000 85.748  0 47  ARG AAA CA  1 ? 3  
ATOM   308  C C   . ARG A 1 45  ? 6.274   25.013  -22.193 1.000 82.814  0 47  ARG AAA C   1 ? 3  
ATOM   309  O O   . ARG A 1 45  ? 6.614   25.536  -21.114 1.000 85.071  0 47  ARG AAA O   1 ? 3  
ATOM   310  C CB  . ARG A 1 45  ? 8.503   24.420  -23.144 1.000 86.984  0 47  ARG AAA CB  1 ? 3  
ATOM   311  C CG  . ARG A 1 45  ? 9.302   24.075  -24.392 1.000 89.665  0 47  ARG AAA CG  1 ? 3  
ATOM   312  C CD  . ARG A 1 45  ? 10.759  23.766  -24.087 1.000 91.798  0 47  ARG AAA CD  1 ? 3  
ATOM   313  N NE  . ARG A 1 45  ? 11.516  23.582  -25.320 1.000 93.767  0 47  ARG AAA NE  1 ? 3  
ATOM   314  C CZ  . ARG A 1 45  ? 11.670  22.426  -25.965 1.000 90.827  0 47  ARG AAA CZ  1 ? 3  
ATOM   315  N NH1 . ARG A 1 45  ? 11.130  21.312  -25.496 1.000 86.207  0 47  ARG AAA NH1 1 ? 3  
ATOM   316  N NH2 . ARG A 1 45  ? 12.358  22.393  -27.093 1.000 92.636  0 47  ARG AAA NH2 1 ? 3  
ATOM   317  N N   . GLU A 1 46  ? 5.147   24.319  -22.375 1.000 78.680  0 48  GLU AAA N   1 ? 3  
ATOM   318  C CA  . GLU A 1 46  ? 4.265   23.838  -21.278 1.000 76.071  0 48  GLU AAA CA  1 ? 3  
ATOM   319  C C   . GLU A 1 46  ? 4.114   22.321  -21.414 1.000 68.936  0 48  GLU AAA C   1 ? 3  
ATOM   320  O O   . GLU A 1 46  ? 3.957   21.845  -22.551 1.000 69.008  0 48  GLU AAA O   1 ? 3  
ATOM   321  C CB  . GLU A 1 46  ? 2.897   24.522  -21.326 1.000 80.384  0 48  GLU AAA CB  1 ? 3  
ATOM   322  C CG  . GLU A 1 46  ? 2.904   25.963  -20.845 1.000 87.281  0 48  GLU AAA CG  1 ? 3  
ATOM   323  C CD  . GLU A 1 46  ? 1.529   26.601  -20.703 1.000 92.275  0 48  GLU AAA CD  1 ? 3  
ATOM   324  O OE1 . GLU A 1 46  ? 0.522   25.929  -21.024 1.000 92.654  0 48  GLU AAA OE1 1 ? 3  
ATOM   325  O OE2 . GLU A 1 46  ? 1.462   27.773  -20.268 1.000 96.798  0 48  GLU AAA OE2 1 ? 3  
ATOM   326  N N   . CYS A 1 47  ? 4.167   21.594  -20.297 1.000 63.852  0 49  CYS AAA N   1 ? 3  
ATOM   327  C CA  . CYS A 1 47  ? 3.795   20.158  -20.223 1.000 59.199  0 49  CYS AAA CA  1 ? 3  
ATOM   328  C C   . CYS A 1 47  ? 2.273   20.047  -20.361 1.000 58.427  0 49  CYS AAA C   1 ? 3  
ATOM   329  O O   . CYS A 1 47  ? 1.577   20.811  -19.672 1.000 59.352  0 49  CYS AAA O   1 ? 3  
ATOM   330  C CB  . CYS A 1 47  ? 4.251   19.529  -18.914 1.000 56.409  0 49  CYS AAA CB  1 ? 3  
ATOM   331  S SG  . CYS A 1 47  ? 4.130   17.722  -18.906 1.000 52.753  0 49  CYS AAA SG  1 ? 3  
ATOM   332  N N   . VAL A 1 48  ? 1.784   19.153  -21.226 1.000 57.233  0 50  VAL AAA N   1 ? 3  
ATOM   333  C CA  . VAL A 1 48  ? 0.324   18.954  -21.478 1.000 58.855  0 50  VAL AAA CA  1 ? 3  
ATOM   334  C C   . VAL A 1 48  ? -0.136  17.619  -20.879 1.000 56.221  0 50  VAL AAA C   1 ? 3  
ATOM   335  O O   . VAL A 1 48  ? -1.320  17.540  -20.484 1.000 57.073  0 50  VAL AAA O   1 ? 3  
ATOM   336  C CB  . VAL A 1 48  ? -0.023  19.061  -22.976 1.000 59.961  0 50  VAL AAA CB  1 ? 3  
ATOM   337  C CG1 . VAL A 1 48  ? 0.234   20.464  -23.495 1.000 63.908  0 50  VAL AAA CG1 1 ? 3  
ATOM   338  C CG2 . VAL A 1 48  ? 0.708   18.039  -23.831 1.000 58.158  0 50  VAL AAA CG2 1 ? 3  
ATOM   339  N N   . ALA A 1 49  ? 0.744   16.613  -20.825 1.000 52.135  0 51  ALA AAA N   1 ? 3  
ATOM   340  C CA  . ALA A 1 49  ? 0.453   15.292  -20.221 1.000 49.871  0 51  ALA AAA CA  1 ? 3  
ATOM   341  C C   . ALA A 1 49  ? 1.754   14.570  -19.860 1.000 48.197  0 51  ALA AAA C   1 ? 3  
ATOM   342  O O   . ALA A 1 49  ? 2.767   14.770  -20.561 1.000 48.150  0 51  ALA AAA O   1 ? 3  
ATOM   343  C CB  . ALA A 1 49  ? -0.387  14.462  -21.157 1.000 49.345  0 51  ALA AAA CB  1 ? 3  
ATOM   344  N N   . SER A 1 50  ? 1.709   13.768  -18.793 1.000 47.074  0 52  SER AAA N   1 ? 3  
ATOM   345  C CA  A SER A 1 50  ? 2.823   12.887  -18.354 0.500 46.596  0 52  SER AAA CA  1 ? 3  
ATOM   346  C CA  B SER A 1 50  ? 2.822   12.883  -18.361 0.500 45.852  0 52  SER AAA CA  1 ? 3  
ATOM   347  C C   . SER A 1 50  ? 2.248   11.575  -17.813 1.000 45.451  0 52  SER AAA C   1 ? 3  
ATOM   348  O O   . SER A 1 50  ? 1.066   11.571  -17.403 1.000 45.473  0 52  SER AAA O   1 ? 3  
ATOM   349  C CB  A SER A 1 50  ? 3.698   13.569  -17.333 0.500 47.862  0 52  SER AAA CB  1 ? 3  
ATOM   350  C CB  B SER A 1 50  ? 3.726   13.561  -17.357 0.500 46.275  0 52  SER AAA CB  1 ? 3  
ATOM   351  O OG  A SER A 1 50  ? 4.000   14.900  -17.731 0.500 50.791  0 52  SER AAA OG  1 ? 3  
ATOM   352  O OG  B SER A 1 50  ? 3.057   13.804  -16.132 0.500 46.253  0 52  SER AAA OG  1 ? 3  
ATOM   353  N N   . ILE A 1 51  ? 3.066   10.523  -17.821 1.000 44.552  0 53  ILE AAA N   1 ? 3  
ATOM   354  C CA  . ILE A 1 51  ? 2.661   9.141   -17.439 1.000 44.582  0 53  ILE AAA CA  1 ? 3  
ATOM   355  C C   . ILE A 1 51  ? 3.822   8.467   -16.694 1.000 43.959  0 53  ILE AAA C   1 ? 3  
ATOM   356  O O   . ILE A 1 51  ? 4.983   8.642   -17.108 1.000 44.640  0 53  ILE AAA O   1 ? 3  
ATOM   357  C CB  . ILE A 1 51  ? 2.213   8.353   -18.688 1.000 43.260  0 53  ILE AAA CB  1 ? 3  
ATOM   358  C CG1 . ILE A 1 51  ? 1.607   6.999   -18.314 1.000 44.077  0 53  ILE AAA CG1 1 ? 3  
ATOM   359  C CG2 . ILE A 1 51  ? 3.356   8.196   -19.684 1.000 42.539  0 53  ILE AAA CG2 1 ? 3  
ATOM   360  C CD1 . ILE A 1 51  ? 0.767   6.389   -19.409 1.000 45.615  0 53  ILE AAA CD1 1 ? 3  
ATOM   361  N N   . GLY A 1 52  ? 3.508   7.742   -15.620 1.000 45.363  0 54  GLY AAA N   1 ? 3  
ATOM   362  C CA  . GLY A 1 52  ? 4.485   6.991   -14.813 1.000 45.493  0 54  GLY AAA CA  1 ? 3  
ATOM   363  C C   . GLY A 1 52  ? 4.959   5.747   -15.540 1.000 45.246  0 54  GLY AAA C   1 ? 3  
ATOM   364  O O   . GLY A 1 52  ? 4.293   5.333   -16.514 1.000 45.851  0 54  GLY AAA O   1 ? 3  
ATOM   365  N N   . TRP A 1 53  ? 6.069   5.178   -15.072 1.000 46.344  0 55  TRP AAA N   1 ? 3  
ATOM   366  C CA  . TRP A 1 53  ? 6.776   4.012   -15.671 1.000 47.690  0 55  TRP AAA CA  1 ? 3  
ATOM   367  C C   . TRP A 1 53  ? 5.817   2.839   -15.919 1.000 48.372  0 55  TRP AAA C   1 ? 3  
ATOM   368  O O   . TRP A 1 53  ? 5.966   2.188   -16.973 1.000 48.482  0 55  TRP AAA O   1 ? 3  
ATOM   369  C CB  . TRP A 1 53  ? 7.965   3.602   -14.793 1.000 47.140  0 55  TRP AAA CB  1 ? 3  
ATOM   370  C CG  . TRP A 1 53  ? 7.601   3.076   -13.440 1.000 48.538  0 55  TRP AAA CG  1 ? 3  
ATOM   371  C CD1 . TRP A 1 53  ? 7.011   3.755   -12.413 1.000 48.310  0 55  TRP AAA CD1 1 ? 3  
ATOM   372  C CD2 . TRP A 1 53  ? 7.848   1.749   -12.949 1.000 50.072  0 55  TRP AAA CD2 1 ? 3  
ATOM   373  N NE1 . TRP A 1 53  ? 6.857   2.939   -11.326 1.000 49.727  0 55  TRP AAA NE1 1 ? 3  
ATOM   374  C CE2 . TRP A 1 53  ? 7.362   1.702   -11.623 1.000 50.665  0 55  TRP AAA CE2 1 ? 3  
ATOM   375  C CE3 . TRP A 1 53  ? 8.423   0.600   -13.502 1.000 51.894  0 55  TRP AAA CE3 1 ? 3  
ATOM   376  C CZ2 . TRP A 1 53  ? 7.433   0.549   -10.843 1.000 53.468  0 55  TRP AAA CZ2 1 ? 3  
ATOM   377  C CZ3 . TRP A 1 53  ? 8.503   -0.538  -12.727 1.000 55.575  0 55  TRP AAA CZ3 1 ? 3  
ATOM   378  C CH2 . TRP A 1 53  ? 8.009   -0.562  -11.418 1.000 55.991  0 55  TRP AAA CH2 1 ? 3  
ATOM   379  N N   . ARG A 1 54  ? 4.883   2.583   -14.996 1.000 49.486  0 56  ARG AAA N   1 ? 3  
ATOM   380  C CA  . ARG A 1 54  ? 3.901   1.462   -15.074 1.000 52.727  0 56  ARG AAA CA  1 ? 3  
ATOM   381  C C   . ARG A 1 54  ? 2.714   1.822   -15.977 1.000 51.972  0 56  ARG AAA C   1 ? 3  
ATOM   382  O O   . ARG A 1 54  ? 1.953   0.900   -16.318 1.000 54.926  0 56  ARG AAA O   1 ? 3  
ATOM   383  C CB  . ARG A 1 54  ? 3.319   1.127   -13.700 1.000 57.075  0 56  ARG AAA CB  1 ? 3  
ATOM   384  C CG  . ARG A 1 54  ? 4.201   0.260   -12.815 1.000 60.676  0 56  ARG AAA CG  1 ? 3  
ATOM   385  C CD  . ARG A 1 54  ? 3.682   0.353   -11.390 1.000 66.204  0 56  ARG AAA CD  1 ? 3  
ATOM   386  N NE  . ARG A 1 54  ? 3.993   -0.807  -10.566 1.000 70.022  0 56  ARG AAA NE  1 ? 3  
ATOM   387  C CZ  . ARG A 1 54  ? 3.805   -0.875  -9.254  1.000 69.084  0 56  ARG AAA CZ  1 ? 3  
ATOM   388  N NH1 . ARG A 1 54  ? 3.316   0.163   -8.594  1.000 68.684  0 56  ARG AAA NH1 1 ? 3  
ATOM   389  N NH2 . ARG A 1 54  ? 4.119   -1.984  -8.606  1.000 72.196  0 56  ARG AAA NH2 1 ? 3  
ATOM   390  N N   . GLY A 1 55  ? 2.533   3.107   -16.304 1.000 50.531  0 57  GLY AAA N   1 ? 3  
ATOM   391  C CA  . GLY A 1 55  ? 1.380   3.607   -17.082 1.000 51.326  0 57  GLY AAA CA  1 ? 3  
ATOM   392  C C   . GLY A 1 55  ? 0.093   3.634   -16.271 1.000 52.126  0 57  GLY AAA C   1 ? 3  
ATOM   393  O O   . GLY A 1 55  ? -0.992  3.665   -16.883 1.000 52.565  0 57  GLY AAA O   1 ? 3  
ATOM   394  N N   . VAL A 1 56  ? 0.205   3.643   -14.939 1.000 50.847  0 58  VAL AAA N   1 ? 3  
ATOM   395  C CA  . VAL A 1 56  ? -0.946  3.650   -13.991 1.000 51.470  0 58  VAL AAA CA  1 ? 3  
ATOM   396  C C   . VAL A 1 56  ? -1.324  5.104   -13.690 1.000 51.859  0 58  VAL AAA C   1 ? 3  
ATOM   397  O O   . VAL A 1 56  ? -2.520  5.443   -13.799 1.000 57.105  0 58  VAL AAA O   1 ? 3  
ATOM   398  C CB  . VAL A 1 56  ? -0.612  2.874   -12.702 1.000 52.201  0 58  VAL AAA CB  1 ? 3  
ATOM   399  C CG1 . VAL A 1 56  ? -1.662  3.097   -11.621 1.000 54.132  0 58  VAL AAA CG1 1 ? 3  
ATOM   400  C CG2 . VAL A 1 56  ? -0.418  1.389   -12.978 1.000 52.061  0 58  VAL AAA CG2 1 ? 3  
ATOM   401  N N   . ARG A 1 57  ? -0.345  5.921   -13.300 1.000 49.029  0 59  ARG AAA N   1 ? 3  
ATOM   402  C CA  . ARG A 1 57  ? -0.537  7.348   -12.936 1.000 47.618  0 59  ARG AAA CA  1 ? 3  
ATOM   403  C C   . ARG A 1 57  ? -0.345  8.210   -14.185 1.000 45.831  0 59  ARG AAA C   1 ? 3  
ATOM   404  O O   . ARG A 1 57  ? 0.617   7.967   -14.937 1.000 46.153  0 59  ARG AAA O   1 ? 3  
ATOM   405  C CB  . ARG A 1 57  ? 0.453   7.773   -11.848 1.000 47.442  0 59  ARG AAA CB  1 ? 3  
ATOM   406  C CG  . ARG A 1 57  ? 0.400   6.929   -10.584 1.000 48.456  0 59  ARG AAA CG  1 ? 3  
ATOM   407  C CD  . ARG A 1 57  ? 1.688   7.050   -9.798  1.000 47.819  0 59  ARG AAA CD  1 ? 3  
ATOM   408  N NE  . ARG A 1 57  ? 2.804   6.435   -10.504 1.000 45.416  0 59  ARG AAA NE  1 ? 3  
ATOM   409  C CZ  . ARG A 1 57  ? 4.090   6.625   -10.213 1.000 45.406  0 59  ARG AAA CZ  1 ? 3  
ATOM   410  N NH1 . ARG A 1 57  ? 4.448   7.424   -9.221  1.000 46.807  0 59  ARG AAA NH1 1 ? 3  
ATOM   411  N NH2 . ARG A 1 57  ? 5.018   6.009   -10.922 1.000 43.735  0 59  ARG AAA NH2 1 ? 3  
ATOM   412  N N   . THR A 1 58  ? -1.242  9.169   -14.393 1.000 45.778  0 60  THR AAA N   1 ? 3  
ATOM   413  C CA  . THR A 1 58  ? -1.208  10.155  -15.499 1.000 46.028  0 60  THR AAA CA  1 ? 3  
ATOM   414  C C   . THR A 1 58  ? -1.440  11.548  -14.912 1.000 47.842  0 60  THR AAA C   1 ? 3  
ATOM   415  O O   . THR A 1 58  ? -2.084  11.647  -13.863 1.000 48.516  0 60  THR AAA O   1 ? 3  
ATOM   416  C CB  . THR A 1 58  ? -2.240  9.821   -16.587 1.000 46.346  0 60  THR AAA CB  1 ? 3  
ATOM   417  O OG1 . THR A 1 58  ? -3.539  9.771   -15.994 1.000 47.492  0 60  THR AAA OG1 1 ? 3  
ATOM   418  C CG2 . THR A 1 58  ? -1.954  8.512   -17.293 1.000 44.673  0 60  THR AAA CG2 1 ? 3  
ATOM   419  N N   . TRP A 1 59  ? -0.894  12.571  -15.564 1.000 50.363  0 61  TRP AAA N   1 ? 3  
ATOM   420  C CA  . TRP A 1 59  ? -1.120  14.009  -15.269 1.000 52.417  0 61  TRP AAA CA  1 ? 3  
ATOM   421  C C   . TRP A 1 59  ? -1.455  14.707  -16.586 1.000 53.052  0 61  TRP AAA C   1 ? 3  
ATOM   422  O O   . TRP A 1 59  ? -0.805  14.385  -17.601 1.000 51.727  0 61  TRP AAA O   1 ? 3  
ATOM   423  C CB  . TRP A 1 59  ? 0.115   14.625  -14.600 1.000 54.080  0 61  TRP AAA CB  1 ? 3  
ATOM   424  C CG  . TRP A 1 59  ? 0.029   16.099  -14.349 1.000 58.326  0 61  TRP AAA CG  1 ? 3  
ATOM   425  C CD1 . TRP A 1 59  ? -0.363  16.711  -13.193 1.000 61.839  0 61  TRP AAA CD1 1 ? 3  
ATOM   426  C CD2 . TRP A 1 59  ? 0.373   17.156  -15.263 1.000 60.095  0 61  TRP AAA CD2 1 ? 3  
ATOM   427  N NE1 . TRP A 1 59  ? -0.296  18.072  -13.327 1.000 64.938  0 61  TRP AAA NE1 1 ? 3  
ATOM   428  C CE2 . TRP A 1 59  ? 0.147   18.376  -14.588 1.000 63.933  0 61  TRP AAA CE2 1 ? 3  
ATOM   429  C CE3 . TRP A 1 59  ? 0.837   17.196  -16.583 1.000 60.226  0 61  TRP AAA CE3 1 ? 3  
ATOM   430  C CZ2 . TRP A 1 59  ? 0.370   19.614  -15.191 1.000 65.751  0 61  TRP AAA CZ2 1 ? 3  
ATOM   431  C CZ3 . TRP A 1 59  ? 1.057   18.420  -17.178 1.000 61.638  0 61  TRP AAA CZ3 1 ? 3  
ATOM   432  C CH2 . TRP A 1 59  ? 0.825   19.611  -16.490 1.000 64.505  0 61  TRP AAA CH2 1 ? 3  
ATOM   433  N N   . TYR A 1 60  ? -2.442  15.602  -16.568 1.000 54.049  0 62  TYR AAA N   1 ? 3  
ATOM   434  C CA  . TYR A 1 60  ? -2.859  16.414  -17.738 1.000 54.237  0 62  TYR AAA CA  1 ? 3  
ATOM   435  C C   . TYR A 1 60  ? -2.913  17.885  -17.314 1.000 56.857  0 62  TYR AAA C   1 ? 3  
ATOM   436  O O   . TYR A 1 60  ? -3.345  18.163  -16.180 1.000 57.757  0 62  TYR AAA O   1 ? 3  
ATOM   437  C CB  . TYR A 1 60  ? -4.202  15.916  -18.280 1.000 54.563  0 62  TYR AAA CB  1 ? 3  
ATOM   438  C CG  . TYR A 1 60  ? -4.233  14.462  -18.685 1.000 51.420  0 62  TYR AAA CG  1 ? 3  
ATOM   439  C CD1 . TYR A 1 60  ? -3.866  14.065  -19.960 1.000 50.452  0 62  TYR AAA CD1 1 ? 3  
ATOM   440  C CD2 . TYR A 1 60  ? -4.645  13.478  -17.800 1.000 50.125  0 62  TYR AAA CD2 1 ? 3  
ATOM   441  C CE1 . TYR A 1 60  ? -3.905  12.733  -20.345 1.000 49.105  0 62  TYR AAA CE1 1 ? 3  
ATOM   442  C CE2 . TYR A 1 60  ? -4.687  12.141  -18.166 1.000 48.824  0 62  TYR AAA CE2 1 ? 3  
ATOM   443  C CZ  . TYR A 1 60  ? -4.317  11.764  -19.446 1.000 48.778  0 62  TYR AAA CZ  1 ? 3  
ATOM   444  O OH  . TYR A 1 60  ? -4.354  10.447  -19.811 1.000 47.593  0 62  TYR AAA OH  1 ? 3  
ATOM   445  N N   . ALA A 1 61  ? -2.460  18.789  -18.189 1.000 58.315  0 63  ALA AAA N   1 ? 3  
ATOM   446  C CA  . ALA A 1 61  ? -2.687  20.249  -18.079 1.000 61.722  0 63  ALA AAA CA  1 ? 3  
ATOM   447  C C   . ALA A 1 61  ? -4.192  20.506  -18.186 1.000 65.074  0 63  ALA AAA C   1 ? 3  
ATOM   448  O O   . ALA A 1 61  ? -4.859  19.761  -18.934 1.000 65.695  0 63  ALA AAA O   1 ? 3  
ATOM   449  C CB  . ALA A 1 61  ? -1.925  20.983  -19.152 1.000 62.225  0 63  ALA AAA CB  1 ? 3  
ATOM   450  N N   . ASP A 1 62  ? -4.702  21.509  -17.465 1.000 68.826  0 64  ASP AAA N   1 ? 3  
ATOM   451  C CA  . ASP A 1 62  ? -6.149  21.858  -17.422 1.000 72.680  0 64  ASP AAA CA  1 ? 3  
ATOM   452  C C   . ASP A 1 62  ? -6.658  22.123  -18.846 1.000 74.185  0 64  ASP AAA C   1 ? 3  
ATOM   453  O O   . ASP A 1 62  ? -7.787  21.703  -19.153 1.000 74.441  0 64  ASP AAA O   1 ? 3  
ATOM   454  C CB  . ASP A 1 62  ? -6.404  23.057  -16.503 1.000 77.012  0 64  ASP AAA CB  1 ? 3  
ATOM   455  C CG  . ASP A 1 62  ? -6.261  22.749  -15.020 1.000 78.391  0 64  ASP AAA CG  1 ? 3  
ATOM   456  O OD1 . ASP A 1 62  ? -6.319  21.553  -14.655 1.000 76.995  0 64  ASP AAA OD1 1 ? 3  
ATOM   457  O OD2 . ASP A 1 62  ? -6.095  23.709  -14.236 1.000 82.051  0 64  ASP AAA OD2 1 ? 3  
ATOM   458  N N   . SER A 1 63  ? -5.841  22.763  -19.689 1.000 75.327  0 65  SER AAA N   1 ? 3  
ATOM   459  C CA  . SER A 1 63  ? -6.201  23.232  -21.055 1.000 77.079  0 65  SER AAA CA  1 ? 3  
ATOM   460  C C   . SER A 1 63  ? -6.509  22.058  -21.995 1.000 76.225  0 65  SER AAA C   1 ? 3  
ATOM   461  O O   . SER A 1 63  ? -7.150  22.313  -23.034 1.000 79.065  0 65  SER AAA O   1 ? 3  
ATOM   462  C CB  . SER A 1 63  ? -5.110  24.102  -21.625 1.000 77.576  0 65  SER AAA CB  1 ? 3  
ATOM   463  O OG  . SER A 1 63  ? -3.891  23.380  -21.732 1.000 74.223  0 65  SER AAA OG  1 ? 3  
ATOM   464  N N   . VAL A 1 64  ? -6.066  20.834  -21.676 1.000 73.874  0 66  VAL AAA N   1 ? 3  
ATOM   465  C CA  . VAL A 1 64  ? -6.233  19.636  -22.558 1.000 73.192  0 66  VAL AAA CA  1 ? 3  
ATOM   466  C C   . VAL A 1 64  ? -6.960  18.498  -21.827 1.000 72.705  0 66  VAL AAA C   1 ? 3  
ATOM   467  O O   . VAL A 1 64  ? -7.175  17.453  -22.473 1.000 72.855  0 66  VAL AAA O   1 ? 3  
ATOM   468  C CB  . VAL A 1 64  ? -4.876  19.143  -23.098 1.000 70.875  0 66  VAL AAA CB  1 ? 3  
ATOM   469  C CG1 . VAL A 1 64  ? -4.103  20.257  -23.791 1.000 73.190  0 66  VAL AAA CG1 1 ? 3  
ATOM   470  C CG2 . VAL A 1 64  ? -4.031  18.492  -22.013 1.000 68.437  0 66  VAL AAA CG2 1 ? 3  
ATOM   471  N N   . LYS A 1 65  ? -7.320  18.674  -20.551 1.000 72.772  0 67  LYS AAA N   1 ? 3  
ATOM   472  C CA  . LYS A 1 65  ? -7.869  17.589  -19.692 1.000 73.524  0 67  LYS AAA CA  1 ? 3  
ATOM   473  C C   . LYS A 1 65  ? -9.245  17.174  -20.228 1.000 75.213  0 67  LYS AAA C   1 ? 3  
ATOM   474  O O   . LYS A 1 65  ? -10.035 18.072  -20.583 1.000 77.705  0 67  LYS AAA O   1 ? 3  
ATOM   475  C CB  . LYS A 1 65  ? -7.937  18.055  -18.234 1.000 78.120  0 67  LYS AAA CB  1 ? 3  
ATOM   476  C CG  . LYS A 1 65  ? -8.095  16.954  -17.194 1.000 79.653  0 67  LYS AAA CG  1 ? 3  
ATOM   477  C CD  . LYS A 1 65  ? -7.930  17.465  -15.773 1.000 82.138  0 67  LYS AAA CD  1 ? 3  
ATOM   478  C CE  . LYS A 1 65  ? -8.503  16.538  -14.722 1.000 84.526  0 67  LYS AAA CE  1 ? 3  
ATOM   479  N NZ  . LYS A 1 65  ? -7.696  15.302  -14.577 1.000 82.745  0 67  LYS AAA NZ  1 ? 3  
ATOM   480  N N   . GLY A 1 66  ? -9.496  15.862  -20.314 1.000 72.997  0 68  GLY AAA N   1 ? 3  
ATOM   481  C CA  . GLY A 1 66  ? -10.746 15.278  -20.840 1.000 74.596  0 68  GLY AAA CA  1 ? 3  
ATOM   482  C C   . GLY A 1 66  ? -10.730 15.109  -22.355 1.000 75.419  0 68  GLY AAA C   1 ? 3  
ATOM   483  O O   . GLY A 1 66  ? -11.579 14.350  -22.866 1.000 75.830  0 68  GLY AAA O   1 ? 3  
ATOM   484  N N   . ARG A 1 67  ? -9.802  15.779  -23.049 1.000 73.884  0 69  ARG AAA N   1 ? 3  
ATOM   485  C CA  . ARG A 1 67  ? -9.700  15.821  -24.535 1.000 73.397  0 69  ARG AAA CA  1 ? 3  
ATOM   486  C C   . ARG A 1 67  ? -8.487  15.010  -25.016 1.000 69.008  0 69  ARG AAA C   1 ? 3  
ATOM   487  O O   . ARG A 1 67  ? -8.583  14.412  -26.100 1.000 69.106  0 69  ARG AAA O   1 ? 3  
ATOM   488  C CB  . ARG A 1 67  ? -9.614  17.276  -25.004 1.000 75.285  0 69  ARG AAA CB  1 ? 3  
ATOM   489  C CG  . ARG A 1 67  ? -10.753 18.149  -24.498 1.000 79.796  0 69  ARG AAA CG  1 ? 3  
ATOM   490  C CD  . ARG A 1 67  ? -10.847 19.484  -25.214 1.000 83.067  0 69  ARG AAA CD  1 ? 3  
ATOM   491  N NE  . ARG A 1 67  ? -9.587  20.215  -25.169 1.000 82.004  0 69  ARG AAA NE  1 ? 3  
ATOM   492  C CZ  . ARG A 1 67  ? -8.721  20.336  -26.174 1.000 81.407  0 69  ARG AAA CZ  1 ? 3  
ATOM   493  N NH1 . ARG A 1 67  ? -8.961  19.779  -27.349 1.000 81.378  0 69  ARG AAA NH1 1 ? 3  
ATOM   494  N NH2 . ARG A 1 67  ? -7.605  21.021  -25.996 1.000 80.898  0 69  ARG AAA NH2 1 ? 3  
ATOM   495  N N   . PHE A 1 68  ? -7.385  15.012  -24.257 1.000 65.935  0 70  PHE AAA N   1 ? 3  
ATOM   496  C CA  . PHE A 1 68  ? -6.129  14.275  -24.561 1.000 62.768  0 70  PHE AAA CA  1 ? 3  
ATOM   497  C C   . PHE A 1 68  ? -5.995  13.074  -23.617 1.000 59.714  0 70  PHE AAA C   1 ? 3  
ATOM   498  O O   . PHE A 1 68  ? -6.287  13.215  -22.418 1.000 60.745  0 70  PHE AAA O   1 ? 3  
ATOM   499  C CB  . PHE A 1 68  ? -4.906  15.186  -24.407 1.000 62.449  0 70  PHE AAA CB  1 ? 3  
ATOM   500  C CG  . PHE A 1 68  ? -4.747  16.288  -25.427 1.000 64.598  0 70  PHE AAA CG  1 ? 3  
ATOM   501  C CD1 . PHE A 1 68  ? -5.794  16.692  -26.245 1.000 68.056  0 70  PHE AAA CD1 1 ? 3  
ATOM   502  C CD2 . PHE A 1 68  ? -3.541  16.967  -25.530 1.000 65.039  0 70  PHE AAA CD2 1 ? 3  
ATOM   503  C CE1 . PHE A 1 68  ? -5.628  17.718  -27.164 1.000 70.907  0 70  PHE AAA CE1 1 ? 3  
ATOM   504  C CE2 . PHE A 1 68  ? -3.378  17.997  -26.447 1.000 68.125  0 70  PHE AAA CE2 1 ? 3  
ATOM   505  C CZ  . PHE A 1 68  ? -4.422  18.372  -27.262 1.000 70.484  0 70  PHE AAA CZ  1 ? 3  
ATOM   506  N N   . THR A 1 69  ? -5.553  11.931  -24.145 1.000 58.366  0 71  THR AAA N   1 ? 3  
ATOM   507  C CA  . THR A 1 69  ? -5.180  10.722  -23.365 1.000 56.767  0 71  THR AAA CA  1 ? 3  
ATOM   508  C C   . THR A 1 69  ? -3.725  10.358  -23.675 1.000 55.030  0 71  THR AAA C   1 ? 3  
ATOM   509  O O   . THR A 1 69  ? -3.400  10.174  -24.867 1.000 54.698  0 71  THR AAA O   1 ? 3  
ATOM   510  C CB  . THR A 1 69  ? -6.119  9.546   -23.659 1.000 59.042  0 71  THR AAA CB  1 ? 3  
ATOM   511  O OG1 . THR A 1 69  ? -7.435  9.964   -23.303 1.000 63.827  0 71  THR AAA OG1 1 ? 3  
ATOM   512  C CG2 . THR A 1 69  ? -5.766  8.287   -22.897 1.000 57.474  0 71  THR AAA CG2 1 ? 3  
ATOM   513  N N   . ILE A 1 70  ? -2.892  10.270  -22.634 1.000 53.004  0 72  ILE AAA N   1 ? 3  
ATOM   514  C CA  . ILE A 1 70  ? -1.507  9.718   -22.710 1.000 49.996  0 72  ILE AAA CA  1 ? 3  
ATOM   515  C C   . ILE A 1 70  ? -1.591  8.245   -22.300 1.000 48.677  0 72  ILE AAA C   1 ? 3  
ATOM   516  O O   . ILE A 1 70  ? -2.346  7.937   -21.358 1.000 50.156  0 72  ILE AAA O   1 ? 3  
ATOM   517  C CB  . ILE A 1 70  ? -0.511  10.535  -21.853 1.000 49.173  0 72  ILE AAA CB  1 ? 3  
ATOM   518  C CG1 . ILE A 1 70  ? 0.941   10.156  -22.161 1.000 48.111  0 72  ILE AAA CG1 1 ? 3  
ATOM   519  C CG2 . ILE A 1 70  ? -0.812  10.412  -20.370 1.000 48.956  0 72  ILE AAA CG2 1 ? 3  
ATOM   520  C CD1 . ILE A 1 70  ? 1.964   11.067  -21.520 1.000 48.581  0 72  ILE AAA CD1 1 ? 3  
ATOM   521  N N   . SER A 1 71  ? -0.900  7.370   -23.031 1.000 47.545  0 73  SER AAA N   1 ? 3  
ATOM   522  C CA  . SER A 1 71  ? -0.761  5.918   -22.741 1.000 47.389  0 73  SER AAA CA  1 ? 3  
ATOM   523  C C   . SER A 1 71  ? 0.628   5.460   -23.191 1.000 45.477  0 73  SER AAA C   1 ? 3  
ATOM   524  O O   . SER A 1 71  ? 1.294   6.235   -23.906 1.000 46.626  0 73  SER AAA O   1 ? 3  
ATOM   525  C CB  . SER A 1 71  ? -1.848  5.124   -23.411 1.000 50.271  0 73  SER AAA CB  1 ? 3  
ATOM   526  O OG  . SER A 1 71  ? -1.845  5.353   -24.813 1.000 52.228  0 73  SER AAA OG  1 ? 3  
ATOM   527  N N   . ARG A 1 72  ? 1.053   4.263   -22.783 1.000 43.962  0 74  ARG AAA N   1 ? 3  
ATOM   528  C CA  . ARG A 1 72  ? 2.396   3.730   -23.127 1.000 44.345  0 74  ARG AAA CA  1 ? 3  
ATOM   529  C C   . ARG A 1 72  ? 2.323   2.216   -23.355 1.000 44.983  0 74  ARG AAA C   1 ? 3  
ATOM   530  O O   . ARG A 1 72  ? 1.482   1.549   -22.729 1.000 42.346  0 74  ARG AAA O   1 ? 3  
ATOM   531  C CB  . ARG A 1 72  ? 3.421   4.113   -22.052 1.000 43.243  0 74  ARG AAA CB  1 ? 3  
ATOM   532  C CG  . ARG A 1 72  ? 3.126   3.560   -20.670 1.000 42.991  0 74  ARG AAA CG  1 ? 3  
ATOM   533  C CD  . ARG A 1 72  ? 4.030   4.191   -19.633 1.000 43.448  0 74  ARG AAA CD  1 ? 3  
ATOM   534  N NE  . ARG A 1 72  ? 5.437   3.912   -19.890 1.000 43.433  0 74  ARG AAA NE  1 ? 3  
ATOM   535  C CZ  . ARG A 1 72  ? 6.453   4.633   -19.430 1.000 42.041  0 74  ARG AAA CZ  1 ? 3  
ATOM   536  N NH1 . ARG A 1 72  ? 6.242   5.690   -18.660 1.000 41.405  0 74  ARG AAA NH1 1 ? 3  
ATOM   537  N NH2 . ARG A 1 72  ? 7.690   4.287   -19.736 1.000 42.601  0 74  ARG AAA NH2 1 ? 3  
ATOM   538  N N   . ASP A 1 73  ? 3.189   1.724   -24.248 1.000 46.746  0 75  ASP AAA N   1 ? 3  
ATOM   539  C CA  . ASP A 1 73  ? 3.370   0.290   -24.593 1.000 49.258  0 75  ASP AAA CA  1 ? 3  
ATOM   540  C C   . ASP A 1 73  ? 4.823   -0.070  -24.256 1.000 49.969  0 75  ASP AAA C   1 ? 3  
ATOM   541  O O   . ASP A 1 73  ? 5.695   0.092   -25.135 1.000 51.253  0 75  ASP AAA O   1 ? 3  
ATOM   542  C CB  . ASP A 1 73  ? 2.990   0.056   -26.060 1.000 51.202  0 75  ASP AAA CB  1 ? 3  
ATOM   543  C CG  . ASP A 1 73  ? 2.942   -1.402  -26.487 1.000 54.163  0 75  ASP AAA CG  1 ? 3  
ATOM   544  O OD1 . ASP A 1 73  ? 3.201   -2.276  -25.633 1.000 55.274  0 75  ASP AAA OD1 1 ? 3  
ATOM   545  O OD2 . ASP A 1 73  ? 2.641   -1.654  -27.676 1.000 54.882  0 75  ASP AAA OD2 1 ? 3  
ATOM   546  N N   . ASN A 1 74  ? 5.073   -0.508  -23.018 1.000 49.595  0 76  ASN AAA N   1 ? 3  
ATOM   547  C CA  . ASN A 1 74  ? 6.438   -0.693  -22.455 1.000 50.704  0 76  ASN AAA CA  1 ? 3  
ATOM   548  C C   . ASN A 1 74  ? 7.220   -1.717  -23.276 1.000 52.272  0 76  ASN AAA C   1 ? 3  
ATOM   549  O O   . ASN A 1 74  ? 8.387   -1.479  -23.583 1.000 51.226  0 76  ASN AAA O   1 ? 3  
ATOM   550  C CB  . ASN A 1 74  ? 6.408   -1.028  -20.959 1.000 51.361  0 76  ASN AAA CB  1 ? 3  
ATOM   551  C CG  . ASN A 1 74  ? 6.386   0.212   -20.088 1.000 51.176  0 76  ASN AAA CG  1 ? 3  
ATOM   552  O OD1 . ASN A 1 74  ? 6.245   1.330   -20.580 1.000 50.843  0 76  ASN AAA OD1 1 ? 3  
ATOM   553  N ND2 . ASN A 1 74  ? 6.542   0.032   -18.789 1.000 55.334  0 76  ASN AAA ND2 1 ? 3  
ATOM   554  N N   . PRO A 1 75  ? 6.634   -2.874  -23.665 1.000 53.800  0 77  PRO AAA N   1 ? 3  
ATOM   555  C CA  . PRO A 1 75  ? 7.337   -3.824  -24.529 1.000 54.867  0 77  PRO AAA CA  1 ? 3  
ATOM   556  C C   . PRO A 1 75  ? 7.807   -3.223  -25.864 1.000 55.378  0 77  PRO AAA C   1 ? 3  
ATOM   557  O O   . PRO A 1 75  ? 8.762   -3.743  -26.411 1.000 56.989  0 77  PRO AAA O   1 ? 3  
ATOM   558  C CB  . PRO A 1 75  ? 6.301   -4.932  -24.770 1.000 56.828  0 77  PRO AAA CB  1 ? 3  
ATOM   559  C CG  . PRO A 1 75  ? 5.376   -4.845  -23.577 1.000 55.844  0 77  PRO AAA CG  1 ? 3  
ATOM   560  C CD  . PRO A 1 75  ? 5.307   -3.366  -23.256 1.000 53.949  0 77  PRO AAA CD  1 ? 3  
ATOM   561  N N   . GLN A 1 76  ? 7.146   -2.160  -26.345 1.000 54.402  0 78  GLN AAA N   1 ? 3  
ATOM   562  C CA  . GLN A 1 76  ? 7.422   -1.505  -27.656 1.000 55.889  0 78  GLN AAA CA  1 ? 3  
ATOM   563  C C   . GLN A 1 76  ? 8.148   -0.164  -27.472 1.000 52.810  0 78  GLN AAA C   1 ? 3  
ATOM   564  O O   . GLN A 1 76  ? 8.379   0.511   -28.492 1.000 55.235  0 78  GLN AAA O   1 ? 3  
ATOM   565  C CB  . GLN A 1 76  ? 6.112   -1.291  -28.421 1.000 57.175  0 78  GLN AAA CB  1 ? 3  
ATOM   566  C CG  . GLN A 1 76  ? 5.478   -2.583  -28.908 1.000 60.480  0 78  GLN AAA CG  1 ? 3  
ATOM   567  C CD  . GLN A 1 76  ? 6.359   -3.295  -29.904 1.000 65.103  0 78  GLN AAA CD  1 ? 3  
ATOM   568  O OE1 . GLN A 1 76  ? 6.766   -2.727  -30.916 1.000 70.836  0 78  GLN AAA OE1 1 ? 3  
ATOM   569  N NE2 . GLN A 1 76  ? 6.662   -4.552  -29.624 1.000 66.980  0 78  GLN AAA NE2 1 ? 3  
ATOM   570  N N   . ASN A 1 77  ? 8.498   0.209   -26.238 1.000 49.372  0 79  ASN AAA N   1 ? 3  
ATOM   571  C CA  . ASN A 1 77  ? 9.205   1.478   -25.908 1.000 48.162  0 79  ASN AAA CA  1 ? 3  
ATOM   572  C C   . ASN A 1 77  ? 8.543   2.645   -26.652 1.000 47.946  0 79  ASN AAA C   1 ? 3  
ATOM   573  O O   . ASN A 1 77  ? 9.266   3.422   -27.305 1.000 49.045  0 79  ASN AAA O   1 ? 3  
ATOM   574  C CB  . ASN A 1 77  ? 10.701  1.403   -26.232 1.000 49.113  0 79  ASN AAA CB  1 ? 3  
ATOM   575  C CG  . ASN A 1 77  ? 11.421  0.333   -25.441 1.000 49.468  0 79  ASN AAA CG  1 ? 3  
ATOM   576  O OD1 . ASN A 1 77  ? 10.988  -0.035  -24.351 1.000 48.087  0 79  ASN AAA OD1 1 ? 3  
ATOM   577  N ND2 . ASN A 1 77  ? 12.520  -0.174  -25.977 1.000 51.292  0 79  ASN AAA ND2 1 ? 3  
ATOM   578  N N   . THR A 1 78  ? 7.217   2.773   -26.551 1.000 49.614  0 80  THR AAA N   1 ? 3  
ATOM   579  C CA  . THR A 1 78  ? 6.419   3.824   -27.245 1.000 49.234  0 80  THR AAA CA  1 ? 3  
ATOM   580  C C   . THR A 1 78  ? 5.422   4.448   -26.263 1.000 48.462  0 80  THR AAA C   1 ? 3  
ATOM   581  O O   . THR A 1 78  ? 4.799   3.697   -25.487 1.000 49.526  0 80  THR AAA O   1 ? 3  
ATOM   582  C CB  . THR A 1 78  ? 5.745   3.258   -28.502 1.000 50.295  0 80  THR AAA CB  1 ? 3  
ATOM   583  O OG1 . THR A 1 78  ? 6.775   2.696   -29.315 1.000 51.316  0 80  THR AAA OG1 1 ? 3  
ATOM   584  C CG2 . THR A 1 78  ? 4.976   4.295   -29.291 1.000 50.700  0 80  THR AAA CG2 1 ? 3  
ATOM   585  N N   . VAL A 1 79  ? 5.300   5.778   -26.301 1.000 49.149  0 81  VAL AAA N   1 ? 3  
ATOM   586  C CA  . VAL A 1 79  ? 4.284   6.575   -25.551 1.000 49.782  0 81  VAL AAA CA  1 ? 3  
ATOM   587  C C   . VAL A 1 79  ? 3.396   7.279   -26.588 1.000 50.959  0 81  VAL AAA C   1 ? 3  
ATOM   588  O O   . VAL A 1 79  ? 3.933   7.763   -27.606 1.000 52.807  0 81  VAL AAA O   1 ? 3  
ATOM   589  C CB  . VAL A 1 79  ? 4.950   7.563   -24.569 1.000 49.286  0 81  VAL AAA CB  1 ? 3  
ATOM   590  C CG1 . VAL A 1 79  ? 5.849   8.569   -25.265 1.000 50.029  0 81  VAL AAA CG1 1 ? 3  
ATOM   591  C CG2 . VAL A 1 79  ? 3.928   8.296   -23.718 1.000 50.802  0 81  VAL AAA CG2 1 ? 3  
ATOM   592  N N   . TYR A 1 80  ? 2.084   7.310   -26.351 1.000 50.425  0 82  TYR AAA N   1 ? 3  
ATOM   593  C CA  . TYR A 1 80  ? 1.068   7.863   -27.287 1.000 52.268  0 82  TYR AAA CA  1 ? 3  
ATOM   594  C C   . TYR A 1 80  ? 0.362   9.058   -26.643 1.000 53.362  0 82  TYR AAA C   1 ? 3  
ATOM   595  O O   . TYR A 1 80  ? 0.208   9.067   -25.407 1.000 52.962  0 82  TYR AAA O   1 ? 3  
ATOM   596  C CB  . TYR A 1 80  ? 0.054   6.783   -27.666 1.000 52.305  0 82  TYR AAA CB  1 ? 3  
ATOM   597  C CG  . TYR A 1 80  ? 0.648   5.562   -28.323 1.000 52.288  0 82  TYR AAA CG  1 ? 3  
ATOM   598  C CD1 . TYR A 1 80  ? 0.838   5.512   -29.695 1.000 54.167  0 82  TYR AAA CD1 1 ? 3  
ATOM   599  C CD2 . TYR A 1 80  ? 1.024   4.458   -27.574 1.000 51.055  0 82  TYR AAA CD2 1 ? 3  
ATOM   600  C CE1 . TYR A 1 80  ? 1.364   4.388   -30.311 1.000 55.628  0 82  TYR AAA CE1 1 ? 3  
ATOM   601  C CE2 . TYR A 1 80  ? 1.561   3.329   -28.171 1.000 52.391  0 82  TYR AAA CE2 1 ? 3  
ATOM   602  C CZ  . TYR A 1 80  ? 1.734   3.294   -29.545 1.000 55.918  0 82  TYR AAA CZ  1 ? 3  
ATOM   603  O OH  . TYR A 1 80  ? 2.266   2.185   -30.142 1.000 58.303  0 82  TYR AAA OH  1 ? 3  
ATOM   604  N N   . LEU A 1 81  ? -0.039  10.037  -27.460 1.000 55.034  0 83  LEU AAA N   1 ? 3  
ATOM   605  C CA  . LEU A 1 81  ? -0.944  11.146  -27.055 1.000 56.487  0 83  LEU AAA CA  1 ? 3  
ATOM   606  C C   . LEU A 1 81  ? -2.133  11.183  -28.018 1.000 58.457  0 83  LEU AAA C   1 ? 3  
ATOM   607  O O   . LEU A 1 81  ? -2.033  11.854  -29.066 1.000 59.774  0 83  LEU AAA O   1 ? 3  
ATOM   608  C CB  . LEU A 1 81  ? -0.186  12.479  -27.043 1.000 56.781  0 83  LEU AAA CB  1 ? 3  
ATOM   609  C CG  . LEU A 1 81  ? -0.964  13.672  -26.485 1.000 58.370  0 83  LEU AAA CG  1 ? 3  
ATOM   610  C CD1 . LEU A 1 81  ? -1.356  13.442  -25.032 1.000 58.038  0 83  LEU AAA CD1 1 ? 3  
ATOM   611  C CD2 . LEU A 1 81  ? -0.171  14.965  -26.624 1.000 58.875  0 83  LEU AAA CD2 1 ? 3  
ATOM   612  N N   . GLN A 1 82  ? -3.204  10.463  -27.675 1.000 58.691  0 84  GLN AAA N   1 ? 3  
ATOM   613  C CA  . GLN A 1 82  ? -4.525  10.554  -28.350 1.000 62.266  0 84  GLN AAA CA  1 ? 3  
ATOM   614  C C   . GLN A 1 82  ? -5.102  11.942  -28.057 1.000 63.236  0 84  GLN AAA C   1 ? 3  
ATOM   615  O O   . GLN A 1 82  ? -5.360  12.219  -26.874 1.000 62.239  0 84  GLN AAA O   1 ? 3  
ATOM   616  C CB  . GLN A 1 82  ? -5.457  9.440   -27.863 1.000 62.894  0 84  GLN AAA CB  1 ? 3  
ATOM   617  C CG  . GLN A 1 82  ? -6.743  9.327   -28.665 1.000 66.595  0 84  GLN AAA CG  1 ? 3  
ATOM   618  C CD  . GLN A 1 82  ? -6.468  9.039   -30.121 1.000 68.869  0 84  GLN AAA CD  1 ? 3  
ATOM   619  O OE1 . GLN A 1 82  ? -5.772  8.086   -30.460 1.000 67.948  0 84  GLN AAA OE1 1 ? 3  
ATOM   620  N NE2 . GLN A 1 82  ? -7.004  9.871   -30.999 1.000 71.907  0 84  GLN AAA NE2 1 ? 3  
ATOM   621  N N   . MET A 1 83  ? -5.249  12.782  -29.086 1.000 65.282  0 85  MET AAA N   1 ? 3  
ATOM   622  C CA  . MET A 1 83  ? -5.779  14.167  -28.977 1.000 68.474  0 85  MET AAA CA  1 ? 3  
ATOM   623  C C   . MET A 1 83  ? -7.121  14.236  -29.712 1.000 73.806  0 85  MET AAA C   1 ? 3  
ATOM   624  O O   . MET A 1 83  ? -7.121  14.129  -30.953 1.000 75.010  0 85  MET AAA O   1 ? 3  
ATOM   625  C CB  . MET A 1 83  ? -4.806  15.185  -29.581 1.000 69.841  0 85  MET AAA CB  1 ? 3  
ATOM   626  C CG  . MET A 1 83  ? -3.436  15.179  -28.935 1.000 67.833  0 85  MET AAA CG  1 ? 3  
ATOM   627  S SD  . MET A 1 83  ? -2.149  15.943  -29.959 1.000 73.738  0 85  MET AAA SD  1 ? 3  
ATOM   628  C CE  . MET A 1 83  ? -2.750  17.627  -30.078 1.000 76.983  0 85  MET AAA CE  1 ? 3  
ATOM   629  N N   . ASN A 1 84  ? -8.217  14.380  -28.960 1.000 76.044  0 86  ASN AAA N   1 ? 3  
ATOM   630  C CA  . ASN A 1 84  ? -9.608  14.451  -29.482 1.000 79.041  0 86  ASN AAA CA  1 ? 3  
ATOM   631  C C   . ASN A 1 84  ? -10.160 15.857  -29.234 1.000 81.177  0 86  ASN AAA C   1 ? 3  
ATOM   632  O O   . ASN A 1 84  ? -9.713  16.500  -28.272 1.000 79.140  0 86  ASN AAA O   1 ? 3  
ATOM   633  C CB  . ASN A 1 84  ? -10.503 13.390  -28.837 1.000 80.338  0 86  ASN AAA CB  1 ? 3  
ATOM   634  C CG  . ASN A 1 84  ? -9.965  11.984  -29.002 1.000 79.852  0 86  ASN AAA CG  1 ? 3  
ATOM   635  O OD1 . ASN A 1 84  ? -9.148  11.728  -29.884 1.000 80.225  0 86  ASN AAA OD1 1 ? 3  
ATOM   636  N ND2 . ASN A 1 84  ? -10.417 11.067  -28.161 1.000 80.490  0 86  ASN AAA ND2 1 ? 3  
ATOM   637  N N   . ASN A 1 85  ? -11.086 16.310  -30.084 1.000 86.765  0 87  ASN AAA N   1 ? 3  
ATOM   638  C CA  . ASN A 1 85  ? -11.814 17.597  -29.923 1.000 91.276  0 87  ASN AAA CA  1 ? 3  
ATOM   639  C C   . ASN A 1 85  ? -10.811 18.756  -30.007 1.000 89.993  0 87  ASN AAA C   1 ? 3  
ATOM   640  O O   . ASN A 1 85  ? -10.932 19.703  -29.205 1.000 91.651  0 87  ASN AAA O   1 ? 3  
ATOM   641  C CB  . ASN A 1 85  ? -12.599 17.608  -28.606 1.000 92.198  0 87  ASN AAA CB  1 ? 3  
ATOM   642  C CG  . ASN A 1 85  ? -13.739 18.604  -28.571 1.000 97.586  0 87  ASN AAA CG  1 ? 3  
ATOM   643  O OD1 . ASN A 1 85  ? -14.169 19.109  -29.607 1.000 100.682 0 87  ASN AAA OD1 1 ? 3  
ATOM   644  N ND2 . ASN A 1 85  ? -14.239 18.886  -27.378 1.000 98.716  0 87  ASN AAA ND2 1 ? 3  
ATOM   645  N N   . LEU A 1 86  ? -9.854  18.679  -30.938 1.000 88.753  0 88  LEU AAA N   1 ? 3  
ATOM   646  C CA  . LEU A 1 86  ? -8.797  19.712  -31.128 1.000 89.401  0 88  LEU AAA CA  1 ? 3  
ATOM   647  C C   . LEU A 1 86  ? -9.457  21.061  -31.426 1.000 93.379  0 88  LEU AAA C   1 ? 3  
ATOM   648  O O   . LEU A 1 86  ? -10.324 21.099  -32.321 1.000 96.964  0 88  LEU AAA O   1 ? 3  
ATOM   649  C CB  . LEU A 1 86  ? -7.853  19.302  -32.265 1.000 89.698  0 88  LEU AAA CB  1 ? 3  
ATOM   650  C CG  . LEU A 1 86  ? -6.619  18.510  -31.832 1.000 86.602  0 88  LEU AAA CG  1 ? 3  
ATOM   651  C CD1 . LEU A 1 86  ? -6.920  17.024  -31.742 1.000 84.794  0 88  LEU AAA CD1 1 ? 3  
ATOM   652  C CD2 . LEU A 1 86  ? -5.458  18.754  -32.779 1.000 88.206  0 88  LEU AAA CD2 1 ? 3  
ATOM   653  N N   . LYS A 1 87  ? -9.073  22.113  -30.690 1.000 92.542  0 89  LYS AAA N   1 ? 3  
ATOM   654  C CA  . LYS A 1 87  ? -9.466  23.521  -30.982 1.000 97.165  0 89  LYS AAA CA  1 ? 3  
ATOM   655  C C   . LYS A 1 87  ? -8.225  24.274  -31.477 1.000 96.184  0 89  LYS AAA C   1 ? 3  
ATOM   656  O O   . LYS A 1 87  ? -7.111  23.767  -31.265 1.000 91.305  0 89  LYS AAA O   1 ? 3  
ATOM   657  C CB  . LYS A 1 87  ? -10.132 24.182  -29.769 1.000 99.400  0 89  LYS AAA CB  1 ? 3  
ATOM   658  C CG  . LYS A 1 87  ? -9.233  24.506  -28.583 1.000 97.773  0 89  LYS AAA CG  1 ? 3  
ATOM   659  C CD  . LYS A 1 87  ? -10.003 24.972  -27.358 1.000 99.916  0 89  LYS AAA CD  1 ? 3  
ATOM   660  C CE  . LYS A 1 87  ? -10.796 26.246  -27.576 1.000 106.053 0 89  LYS AAA CE  1 ? 3  
ATOM   661  N NZ  . LYS A 1 87  ? -9.915  27.415  -27.809 1.000 107.841 0 89  LYS AAA NZ  1 ? 3  
ATOM   662  N N   . SER A 1 88  ? -8.425  25.427  -32.124 1.000 95.345  0 90  SER AAA N   1 ? 4  
ATOM   663  C CA  . SER A 1 88  ? -7.390  26.200  -32.865 1.000 95.158  0 90  SER AAA CA  1 ? 4  
ATOM   664  C C   . SER A 1 88  ? -6.189  26.527  -31.965 1.000 91.263  0 90  SER AAA C   1 ? 4  
ATOM   665  O O   . SER A 1 88  ? -5.081  26.672  -32.512 1.000 91.826  0 90  SER AAA O   1 ? 4  
ATOM   666  C CB  . SER A 1 88  ? -7.978  27.450  -33.473 1.000 97.389  0 90  SER AAA CB  1 ? 4  
ATOM   667  O OG  . SER A 1 88  ? -8.328  28.390  -32.471 1.000 96.055  0 90  SER AAA OG  1 ? 4  
ATOM   668  N N   . GLY A 1 89  ? -6.399  26.639  -30.648 1.000 88.800  0 91  GLY AAA N   1 ? 4  
ATOM   669  C CA  . GLY A 1 89  ? -5.369  27.022  -29.660 1.000 85.149  0 91  GLY AAA CA  1 ? 4  
ATOM   670  C C   . GLY A 1 89  ? -4.465  25.868  -29.240 1.000 81.471  0 91  GLY AAA C   1 ? 4  
ATOM   671  O O   . GLY A 1 89  ? -3.594  26.104  -28.377 1.000 77.314  0 91  GLY AAA O   1 ? 4  
ATOM   672  N N   . ASP A 1 90  ? -4.655  24.670  -29.807 1.000 81.540  0 92  ASP AAA N   1 ? 4  
ATOM   673  C CA  . ASP A 1 90  ? -3.772  23.490  -29.591 1.000 78.734  0 92  ASP AAA CA  1 ? 4  
ATOM   674  C C   . ASP A 1 90  ? -2.584  23.540  -30.563 1.000 79.009  0 92  ASP AAA C   1 ? 4  
ATOM   675  O O   . ASP A 1 90  ? -1.593  22.831  -30.305 1.000 78.814  0 92  ASP AAA O   1 ? 4  
ATOM   676  C CB  . ASP A 1 90  ? -4.538  22.173  -29.749 1.000 79.092  0 92  ASP AAA CB  1 ? 4  
ATOM   677  C CG  . ASP A 1 90  ? -5.499  21.869  -28.611 1.000 78.416  0 92  ASP AAA CG  1 ? 4  
ATOM   678  O OD1 . ASP A 1 90  ? -5.178  22.213  -27.460 1.000 75.483  0 92  ASP AAA OD1 1 ? 4  
ATOM   679  O OD2 . ASP A 1 90  ? -6.563  21.280  -28.884 1.000 81.188  0 92  ASP AAA OD2 1 ? 4  
ATOM   680  N N   . THR A 1 91  ? -2.681  24.341  -31.631 1.000 81.133  0 93  THR AAA N   1 ? 4  
ATOM   681  C CA  . THR A 1 91  ? -1.634  24.502  -32.679 1.000 81.724  0 93  THR AAA CA  1 ? 4  
ATOM   682  C C   . THR A 1 91  ? -0.303  24.869  -32.010 1.000 78.887  0 93  THR AAA C   1 ? 4  
ATOM   683  O O   . THR A 1 91  ? -0.248  25.904  -31.307 1.000 78.356  0 93  THR AAA O   1 ? 4  
ATOM   684  C CB  . THR A 1 91  ? -2.051  25.527  -33.744 1.000 84.688  0 93  THR AAA CB  1 ? 4  
ATOM   685  O OG1 . THR A 1 91  ? -1.095  25.494  -34.802 1.000 85.598  0 93  THR AAA OG1 1 ? 4  
ATOM   686  C CG2 . THR A 1 91  ? -2.138  26.943  -33.219 1.000 84.747  0 93  THR AAA CG2 1 ? 4  
ATOM   687  N N   . ALA A 1 92  ? 0.719   24.032  -32.206 1.000 76.869  0 94  ALA AAA N   1 ? 4  
ATOM   688  C CA  . ALA A 1 92  ? 2.046   24.148  -31.560 1.000 74.919  0 94  ALA AAA CA  1 ? 4  
ATOM   689  C C   . ALA A 1 92  ? 2.962   23.015  -32.035 1.000 73.698  0 94  ALA AAA C   1 ? 4  
ATOM   690  O O   . ALA A 1 92  ? 2.458   22.059  -32.649 1.000 73.984  0 94  ALA AAA O   1 ? 4  
ATOM   691  C CB  . ALA A 1 92  ? 1.885   24.115  -30.058 1.000 72.624  0 94  ALA AAA CB  1 ? 4  
ATOM   692  N N   . VAL A 1 93  ? 4.260   23.135  -31.747 1.000 72.175  0 95  VAL AAA N   1 ? 4  
ATOM   693  C CA  . VAL A 1 93  ? 5.268   22.044  -31.890 1.000 71.868  0 95  VAL AAA CA  1 ? 4  
ATOM   694  C C   . VAL A 1 93  ? 5.180   21.173  -30.630 1.000 69.328  0 95  VAL AAA C   1 ? 4  
ATOM   695  O O   . VAL A 1 93  ? 5.449   21.701  -29.537 1.000 69.077  0 95  VAL AAA O   1 ? 4  
ATOM   696  C CB  . VAL A 1 93  ? 6.686   22.613  -32.097 1.000 71.779  0 95  VAL AAA CB  1 ? 4  
ATOM   697  C CG1 . VAL A 1 93  ? 7.736   21.517  -32.195 1.000 70.757  0 95  VAL AAA CG1 1 ? 4  
ATOM   698  C CG2 . VAL A 1 93  ? 6.747   23.517  -33.321 1.000 74.657  0 95  VAL AAA CG2 1 ? 4  
ATOM   699  N N   . TYR A 1 94  ? 4.796   19.902  -30.781 1.000 68.675  0 96  TYR AAA N   1 ? 4  
ATOM   700  C CA  . TYR A 1 94  ? 4.653   18.923  -29.671 1.000 66.810  0 96  TYR AAA CA  1 ? 4  
ATOM   701  C C   . TYR A 1 94  ? 5.947   18.109  -29.531 1.000 65.556  0 96  TYR AAA C   1 ? 4  
ATOM   702  O O   . TYR A 1 94  ? 6.338   17.426  -30.499 1.000 67.640  0 96  TYR AAA O   1 ? 4  
ATOM   703  C CB  . TYR A 1 94  ? 3.431   18.030  -29.896 1.000 67.925  0 96  TYR AAA CB  1 ? 4  
ATOM   704  C CG  . TYR A 1 94  ? 2.113   18.702  -29.602 1.000 68.916  0 96  TYR AAA CG  1 ? 4  
ATOM   705  C CD1 . TYR A 1 94  ? 1.609   19.678  -30.445 1.000 71.425  0 96  TYR AAA CD1 1 ? 4  
ATOM   706  C CD2 . TYR A 1 94  ? 1.366   18.370  -28.483 1.000 67.148  0 96  TYR AAA CD2 1 ? 4  
ATOM   707  C CE1 . TYR A 1 94  ? 0.399   20.304  -30.189 1.000 71.680  0 96  TYR AAA CE1 1 ? 4  
ATOM   708  C CE2 . TYR A 1 94  ? 0.154   18.984  -28.213 1.000 67.569  0 96  TYR AAA CE2 1 ? 4  
ATOM   709  C CZ  . TYR A 1 94  ? -0.331  19.959  -29.066 1.000 69.521  0 96  TYR AAA CZ  1 ? 4  
ATOM   710  O OH  . TYR A 1 94  ? -1.522  20.573  -28.803 1.000 69.929  0 96  TYR AAA OH  1 ? 4  
ATOM   711  N N   . TYR A 1 95  ? 6.584   18.192  -28.355 1.000 61.638  0 97  TYR AAA N   1 ? 4  
ATOM   712  C CA  . TYR A 1 95  ? 7.804   17.432  -27.978 1.000 59.645  0 97  TYR AAA CA  1 ? 4  
ATOM   713  C C   . TYR A 1 95  ? 7.426   16.306  -27.012 1.000 57.299  0 97  TYR AAA C   1 ? 4  
ATOM   714  O O   . TYR A 1 95  ? 6.724   16.583  -26.020 1.000 55.709  0 97  TYR AAA O   1 ? 4  
ATOM   715  C CB  . TYR A 1 95  ? 8.836   18.347  -27.313 1.000 58.867  0 97  TYR AAA CB  1 ? 4  
ATOM   716  C CG  . TYR A 1 95  ? 9.182   19.590  -28.091 1.000 61.178  0 97  TYR AAA CG  1 ? 4  
ATOM   717  C CD1 . TYR A 1 95  ? 8.395   20.727  -28.008 1.000 62.711  0 97  TYR AAA CD1 1 ? 4  
ATOM   718  C CD2 . TYR A 1 95  ? 10.298  19.635  -28.910 1.000 62.870  0 97  TYR AAA CD2 1 ? 4  
ATOM   719  C CE1 . TYR A 1 95  ? 8.705   21.874  -28.722 1.000 65.141  0 97  TYR AAA CE1 1 ? 4  
ATOM   720  C CE2 . TYR A 1 95  ? 10.625  20.775  -29.627 1.000 64.748  0 97  TYR AAA CE2 1 ? 4  
ATOM   721  C CZ  . TYR A 1 95  ? 9.823   21.899  -29.536 1.000 65.800  0 97  TYR AAA CZ  1 ? 4  
ATOM   722  O OH  . TYR A 1 95  ? 10.127  23.029  -30.236 1.000 67.356  0 97  TYR AAA OH  1 ? 4  
ATOM   723  N N   . CYS A 1 96  ? 7.878   15.079  -27.285 1.000 57.156  0 98  CYS AAA N   1 ? 4  
ATOM   724  C CA  . CYS A 1 96  ? 7.873   13.974  -26.294 1.000 56.802  0 98  CYS AAA CA  1 ? 4  
ATOM   725  C C   . CYS A 1 96  ? 9.173   14.093  -25.483 1.000 54.204  0 98  CYS AAA C   1 ? 4  
ATOM   726  O O   . CYS A 1 96  ? 10.182  14.541  -26.053 1.000 54.177  0 98  CYS AAA O   1 ? 4  
ATOM   727  C CB  . CYS A 1 96  ? 7.684   12.614  -26.965 1.000 59.898  0 98  CYS AAA CB  1 ? 4  
ATOM   728  S SG  . CYS A 1 96  ? 9.089   11.500  -26.739 1.000 62.720  0 98  CYS AAA SG  1 ? 4  
ATOM   729  N N   . ALA A 1 97  ? 9.137   13.774  -24.188 1.000 51.903  0 99  ALA AAA N   1 ? 4  
ATOM   730  C CA  . ALA A 1 97  ? 10.283  13.922  -23.260 1.000 49.838  0 99  ALA AAA CA  1 ? 4  
ATOM   731  C C   . ALA A 1 97  ? 10.370  12.700  -22.343 1.000 47.981  0 99  ALA AAA C   1 ? 4  
ATOM   732  O O   . ALA A 1 97  ? 9.315   12.146  -21.998 1.000 48.198  0 99  ALA AAA O   1 ? 4  
ATOM   733  C CB  . ALA A 1 97  ? 10.152  15.204  -22.473 1.000 49.236  0 99  ALA AAA CB  1 ? 4  
ATOM   734  N N   . ALA A 1 98  ? 11.592  12.313  -21.975 1.000 47.423  0 100 ALA AAA N   1 ? 4  
ATOM   735  C CA  . ALA A 1 98  ? 11.907  11.162  -21.098 1.000 46.135  0 100 ALA AAA CA  1 ? 4  
ATOM   736  C C   . ALA A 1 98  ? 12.574  11.664  -19.813 1.000 45.449  0 100 ALA AAA C   1 ? 4  
ATOM   737  O O   . ALA A 1 98  ? 13.583  12.399  -19.909 1.000 45.480  0 100 ALA AAA O   1 ? 4  
ATOM   738  C CB  . ALA A 1 98  ? 12.799  10.193  -21.832 1.000 47.571  0 100 ALA AAA CB  1 ? 4  
ATOM   739  N N   . SER A 1 99  ? 12.005  11.295  -18.661 1.000 44.146  0 101 SER AAA N   1 ? 4  
ATOM   740  C CA  . SER A 1 99  ? 12.624  11.403  -17.318 1.000 43.803  0 101 SER AAA CA  1 ? 4  
ATOM   741  C C   . SER A 1 99  ? 13.100  10.003  -16.919 1.000 43.463  0 101 SER AAA C   1 ? 4  
ATOM   742  O O   . SER A 1 99  ? 12.246  9.174   -16.542 1.000 43.239  0 101 SER AAA O   1 ? 4  
ATOM   743  C CB  . SER A 1 99  ? 11.660  11.995  -16.313 1.000 43.511  0 101 SER AAA CB  1 ? 4  
ATOM   744  O OG  . SER A 1 99  ? 12.333  12.360  -15.107 1.000 42.806  0 101 SER AAA OG  1 ? 4  
ATOM   745  N N   . VAL A 1 100 ? 14.405  9.741   -17.047 1.000 43.083  0 102 VAL AAA N   1 ? 4  
ATOM   746  C CA  . VAL A 1 100 ? 14.990  8.368   -16.962 1.000 42.653  0 102 VAL AAA CA  1 ? 4  
ATOM   747  C C   . VAL A 1 100 ? 15.143  7.970   -15.492 1.000 41.432  0 102 VAL AAA C   1 ? 4  
ATOM   748  O O   . VAL A 1 100 ? 15.431  8.856   -14.665 1.000 41.055  0 102 VAL AAA O   1 ? 4  
ATOM   749  C CB  . VAL A 1 100 ? 16.326  8.263   -17.726 1.000 43.931  0 102 VAL AAA CB  1 ? 4  
ATOM   750  C CG1 . VAL A 1 100 ? 16.141  8.610   -19.195 1.000 44.585  0 102 VAL AAA CG1 1 ? 4  
ATOM   751  C CG2 . VAL A 1 100 ? 17.434  9.103   -17.106 1.000 44.258  0 102 VAL AAA CG2 1 ? 4  
ATOM   752  N N   . GLY A 1 101 ? 14.949  6.680   -15.199 1.000 41.344  0 103 GLY AAA N   1 ? 4  
ATOM   753  C CA  . GLY A 1 101 ? 14.989  6.106   -13.840 1.000 42.209  0 103 GLY AAA CA  1 ? 4  
ATOM   754  C C   . GLY A 1 101 ? 14.145  6.905   -12.859 1.000 42.901  0 103 GLY AAA C   1 ? 4  
ATOM   755  O O   . GLY A 1 101 ? 14.563  7.036   -11.696 1.000 44.045  0 103 GLY AAA O   1 ? 4  
ATOM   756  N N   . ASN A 1 102 ? 13.000  7.428   -13.313 1.000 43.594  0 104 ASN AAA N   1 ? 4  
ATOM   757  C CA  . ASN A 1 102 ? 12.089  8.295   -12.519 1.000 43.368  0 104 ASN AAA CA  1 ? 4  
ATOM   758  C C   . ASN A 1 102 ? 10.774  7.546   -12.291 1.000 42.620  0 104 ASN AAA C   1 ? 4  
ATOM   759  O O   . ASN A 1 102 ? 10.043  7.315   -13.274 1.000 41.760  0 104 ASN AAA O   1 ? 4  
ATOM   760  C CB  . ASN A 1 102 ? 11.851  9.651   -13.187 1.000 43.394  0 104 ASN AAA CB  1 ? 4  
ATOM   761  C CG  . ASN A 1 102 ? 11.086  10.608  -12.294 1.000 44.552  0 104 ASN AAA CG  1 ? 4  
ATOM   762  O OD1 . ASN A 1 102 ? 10.719  10.261  -11.172 1.000 44.145  0 104 ASN AAA OD1 1 ? 4  
ATOM   763  N ND2 . ASN A 1 102 ? 10.844  11.816  -12.779 1.000 45.034  0 104 ASN AAA ND2 1 ? 4  
ATOM   764  N N   . TYR A 1 103 ? 10.498  7.205   -11.029 1.000 44.219  0 105 TYR AAA N   1 ? 4  
ATOM   765  C CA  . TYR A 1 103 ? 9.343   6.385   -10.575 1.000 44.683  0 105 TYR AAA CA  1 ? 4  
ATOM   766  C C   . TYR A 1 103 ? 8.208   7.306   -10.104 1.000 44.511  0 105 TYR AAA C   1 ? 4  
ATOM   767  O O   . TYR A 1 103 ? 7.253   6.807   -9.472  1.000 45.481  0 105 TYR AAA O   1 ? 4  
ATOM   768  C CB  . TYR A 1 103 ? 9.824   5.419   -9.486  1.000 45.255  0 105 TYR AAA CB  1 ? 4  
ATOM   769  C CG  . TYR A 1 103 ? 10.838  4.417   -9.978  1.000 45.828  0 105 TYR AAA CG  1 ? 4  
ATOM   770  C CD1 . TYR A 1 103 ? 12.198  4.685   -9.945  1.000 46.914  0 105 TYR AAA CD1 1 ? 4  
ATOM   771  C CD2 . TYR A 1 103 ? 10.433  3.202   -10.506 1.000 45.703  0 105 TYR AAA CD2 1 ? 4  
ATOM   772  C CE1 . TYR A 1 103 ? 13.129  3.770   -10.413 1.000 47.027  0 105 TYR AAA CE1 1 ? 4  
ATOM   773  C CE2 . TYR A 1 103 ? 11.348  2.274   -10.973 1.000 46.662  0 105 TYR AAA CE2 1 ? 4  
ATOM   774  C CZ  . TYR A 1 103 ? 12.702  2.562   -10.936 1.000 47.156  0 105 TYR AAA CZ  1 ? 4  
ATOM   775  O OH  . TYR A 1 103 ? 13.600  1.644   -11.394 1.000 47.448  0 105 TYR AAA OH  1 ? 4  
ATOM   776  N N   . GLY A 1 104 ? 8.314   8.603   -10.419 1.000 43.945  0 106 GLY AAA N   1 ? 4  
ATOM   777  C CA  . GLY A 1 104 ? 7.344   9.650   -10.055 1.000 44.338  0 106 GLY AAA CA  1 ? 4  
ATOM   778  C C   . GLY A 1 104 ? 6.519   10.082  -11.251 1.000 43.655  0 106 GLY AAA C   1 ? 4  
ATOM   779  O O   . GLY A 1 104 ? 6.418   9.305   -12.226 1.000 43.401  0 106 GLY AAA O   1 ? 4  
ATOM   780  N N   . LEU A 1 105 ? 5.933   11.278  -11.167 1.000 44.088  0 107 LEU AAA N   1 ? 4  
ATOM   781  C CA  . LEU A 1 105 ? 5.023   11.845  -12.197 1.000 44.528  0 107 LEU AAA CA  1 ? 4  
ATOM   782  C C   . LEU A 1 105 ? 5.463   13.274  -12.508 1.000 44.740  0 107 LEU AAA C   1 ? 4  
ATOM   783  O O   . LEU A 1 105 ? 4.836   14.235  -12.068 1.000 46.134  0 107 LEU AAA O   1 ? 4  
ATOM   784  C CB  . LEU A 1 105 ? 3.586   11.783  -11.671 1.000 44.884  0 107 LEU AAA CB  1 ? 4  
ATOM   785  C CG  . LEU A 1 105 ? 2.496   12.102  -12.691 1.000 45.670  0 107 LEU AAA CG  1 ? 4  
ATOM   786  C CD1 . LEU A 1 105 ? 2.593   11.184  -13.904 1.000 45.491  0 107 LEU AAA CD1 1 ? 4  
ATOM   787  C CD2 . LEU A 1 105 ? 1.120   12.003  -12.049 1.000 46.882  0 107 LEU AAA CD2 1 ? 4  
ATOM   788  N N   . PRO A 1 106 ? 6.568   13.452  -13.267 1.000 43.465  0 108 PRO AAA N   1 ? 4  
ATOM   789  C CA  . PRO A 1 106 ? 7.117   14.779  -13.544 1.000 43.598  0 108 PRO AAA CA  1 ? 4  
ATOM   790  C C   . PRO A 1 106 ? 6.241   15.593  -14.505 1.000 42.945  0 108 PRO AAA C   1 ? 4  
ATOM   791  O O   . PRO A 1 106 ? 5.626   14.996  -15.364 1.000 41.833  0 108 PRO AAA O   1 ? 4  
ATOM   792  C CB  . PRO A 1 106 ? 8.474   14.470  -14.194 1.000 44.031  0 108 PRO AAA CB  1 ? 4  
ATOM   793  C CG  . PRO A 1 106 ? 8.267   13.120  -14.843 1.000 43.477  0 108 PRO AAA CG  1 ? 4  
ATOM   794  C CD  . PRO A 1 106 ? 7.344   12.379  -13.902 1.000 43.360  0 108 PRO AAA CD  1 ? 4  
ATOM   795  N N   . TRP A 1 107 ? 6.203   16.917  -14.321 1.000 43.409  0 109 TRP AAA N   1 ? 4  
ATOM   796  C CA  . TRP A 1 107 ? 5.454   17.864  -15.192 1.000 44.034  0 109 TRP AAA CA  1 ? 4  
ATOM   797  C C   . TRP A 1 107 ? 6.238   19.157  -15.454 1.000 45.252  0 109 TRP AAA C   1 ? 4  
ATOM   798  O O   . TRP A 1 107 ? 5.757   19.959  -16.269 1.000 47.153  0 109 TRP AAA O   1 ? 4  
ATOM   799  C CB  . TRP A 1 107 ? 4.078   18.164  -14.590 1.000 44.446  0 109 TRP AAA CB  1 ? 4  
ATOM   800  C CG  . TRP A 1 107 ? 4.078   18.636  -13.169 1.000 44.420  0 109 TRP AAA CG  1 ? 4  
ATOM   801  C CD1 . TRP A 1 107 ? 3.881   17.875  -12.054 1.000 44.168  0 109 TRP AAA CD1 1 ? 4  
ATOM   802  C CD2 . TRP A 1 107 ? 4.233   19.991  -12.709 1.000 45.385  0 109 TRP AAA CD2 1 ? 4  
ATOM   803  N NE1 . TRP A 1 107 ? 3.924   18.657  -10.931 1.000 45.604  0 109 TRP AAA NE1 1 ? 4  
ATOM   804  C CE2 . TRP A 1 107 ? 4.136   19.960  -11.301 1.000 46.256  0 109 TRP AAA CE2 1 ? 4  
ATOM   805  C CE3 . TRP A 1 107 ? 4.444   21.221  -13.344 1.000 45.998  0 109 TRP AAA CE3 1 ? 4  
ATOM   806  C CZ2 . TRP A 1 107 ? 4.251   21.112  -10.523 1.000 47.907  0 109 TRP AAA CZ2 1 ? 4  
ATOM   807  C CZ3 . TRP A 1 107 ? 4.560   22.358  -12.575 1.000 47.628  0 109 TRP AAA CZ3 1 ? 4  
ATOM   808  C CH2 . TRP A 1 107 ? 4.460   22.302  -11.184 1.000 48.770  0 109 TRP AAA CH2 1 ? 4  
ATOM   809  N N   . ALA A 1 108 ? 7.382   19.370  -14.798 1.000 45.693  0 110 ALA AAA N   1 ? 4  
ATOM   810  C CA  . ALA A 1 108 ? 8.252   20.552  -15.006 1.000 47.497  0 110 ALA AAA CA  1 ? 4  
ATOM   811  C C   . ALA A 1 108 ? 9.363   20.172  -15.993 1.000 47.080  0 110 ALA AAA C   1 ? 4  
ATOM   812  O O   . ALA A 1 108 ? 9.847   19.026  -15.921 1.000 45.689  0 110 ALA AAA O   1 ? 4  
ATOM   813  C CB  . ALA A 1 108 ? 8.804   21.034  -13.684 1.000 49.027  0 110 ALA AAA CB  1 ? 4  
ATOM   814  N N   . HIS A 1 109 ? 9.738   21.091  -16.887 1.000 48.155  0 111 HIS AAA N   1 ? 4  
ATOM   815  C CA  . HIS A 1 109 ? 10.691  20.843  -18.004 1.000 48.037  0 111 HIS AAA CA  1 ? 4  
ATOM   816  C C   . HIS A 1 109 ? 12.039  20.350  -17.449 1.000 48.314  0 111 HIS AAA C   1 ? 4  
ATOM   817  O O   . HIS A 1 109 ? 12.604  19.408  -18.034 1.000 48.459  0 111 HIS AAA O   1 ? 4  
ATOM   818  C CB  . HIS A 1 109 ? 10.825  22.092  -18.888 1.000 48.839  0 111 HIS AAA CB  1 ? 4  
ATOM   819  C CG  . HIS A 1 109 ? 11.649  23.180  -18.283 1.000 50.154  0 111 HIS AAA CG  1 ? 4  
ATOM   820  N ND1 . HIS A 1 109 ? 13.023  23.249  -18.461 1.000 51.204  0 111 HIS AAA ND1 1 ? 4  
ATOM   821  C CD2 . HIS A 1 109 ? 11.316  24.222  -17.493 1.000 51.097  0 111 HIS AAA CD2 1 ? 4  
ATOM   822  C CE1 . HIS A 1 109 ? 13.495  24.294  -17.817 1.000 52.578  0 111 HIS AAA CE1 1 ? 4  
ATOM   823  N NE2 . HIS A 1 109 ? 12.471  24.901  -17.208 1.000 53.189  0 111 HIS AAA NE2 1 ? 4  
ATOM   824  N N   . PHE A 1 110 ? 12.516  20.937  -16.348 1.000 49.070  0 112 PHE AAA N   1 ? 4  
ATOM   825  C CA  . PHE A 1 110 ? 13.835  20.624  -15.731 1.000 50.351  0 112 PHE AAA CA  1 ? 4  
ATOM   826  C C   . PHE A 1 110 ? 13.861  19.202  -15.147 1.000 48.758  0 112 PHE AAA C   1 ? 4  
ATOM   827  O O   . PHE A 1 110 ? 14.969  18.712  -14.879 1.000 48.912  0 112 PHE AAA O   1 ? 4  
ATOM   828  C CB  . PHE A 1 110 ? 14.216  21.661  -14.669 1.000 52.592  0 112 PHE AAA CB  1 ? 4  
ATOM   829  C CG  . PHE A 1 110 ? 13.151  21.973  -13.648 1.000 53.141  0 112 PHE AAA CG  1 ? 4  
ATOM   830  C CD1 . PHE A 1 110 ? 12.824  21.063  -12.656 1.000 52.546  0 112 PHE AAA CD1 1 ? 4  
ATOM   831  C CD2 . PHE A 1 110 ? 12.495  23.194  -13.664 1.000 54.866  0 112 PHE AAA CD2 1 ? 4  
ATOM   832  C CE1 . PHE A 1 110 ? 11.854  21.363  -11.710 1.000 53.965  0 112 PHE AAA CE1 1 ? 4  
ATOM   833  C CE2 . PHE A 1 110 ? 11.524  23.492  -12.719 1.000 55.584  0 112 PHE AAA CE2 1 ? 4  
ATOM   834  C CZ  . PHE A 1 110 ? 11.203  22.575  -11.745 1.000 54.789  0 112 PHE AAA CZ  1 ? 4  
ATOM   835  N N   . GLU A 1 111 ? 12.704  18.563  -14.947 1.000 47.377  0 113 GLU AAA N   1 ? 4  
ATOM   836  C CA  . GLU A 1 111 ? 12.605  17.189  -14.385 1.000 46.922  0 113 GLU AAA CA  1 ? 4  
ATOM   837  C C   . GLU A 1 111 ? 12.806  16.143  -15.489 1.000 47.035  0 113 GLU AAA C   1 ? 4  
ATOM   838  O O   . GLU A 1 111 ? 12.887  14.946  -15.150 1.000 46.296  0 113 GLU AAA O   1 ? 4  
ATOM   839  C CB  . GLU A 1 111 ? 11.252  16.978  -13.704 1.000 47.007  0 113 GLU AAA CB  1 ? 4  
ATOM   840  C CG  . GLU A 1 111 ? 11.014  17.888  -12.513 1.000 48.718  0 113 GLU AAA CG  1 ? 4  
ATOM   841  C CD  . GLU A 1 111 ? 9.661   17.715  -11.839 1.000 49.003  0 113 GLU AAA CD  1 ? 4  
ATOM   842  O OE1 . GLU A 1 111 ? 8.640   17.618  -12.556 1.000 48.027  0 113 GLU AAA OE1 1 ? 4  
ATOM   843  O OE2 . GLU A 1 111 ? 9.634   17.644  -10.598 1.000 51.292  0 113 GLU AAA OE2 1 ? 4  
ATOM   844  N N   . TYR A 1 112 ? 12.847  16.565  -16.758 1.000 48.183  0 114 TYR AAA N   1 ? 4  
ATOM   845  C CA  . TYR A 1 112 ? 13.035  15.682  -17.939 1.000 48.758  0 114 TYR AAA CA  1 ? 4  
ATOM   846  C C   . TYR A 1 112 ? 14.486  15.786  -18.419 1.000 50.136  0 114 TYR AAA C   1 ? 4  
ATOM   847  O O   . TYR A 1 112 ? 15.116  16.835  -18.207 1.000 51.598  0 114 TYR AAA O   1 ? 4  
ATOM   848  C CB  . TYR A 1 112 ? 12.019  16.029  -19.031 1.000 49.038  0 114 TYR AAA CB  1 ? 4  
ATOM   849  C CG  . TYR A 1 112 ? 10.615  15.593  -18.705 1.000 48.369  0 114 TYR AAA CG  1 ? 4  
ATOM   850  C CD1 . TYR A 1 112 ? 9.820   16.332  -17.844 1.000 48.617  0 114 TYR AAA CD1 1 ? 4  
ATOM   851  C CD2 . TYR A 1 112 ? 10.082  14.433  -19.244 1.000 48.231  0 114 TYR AAA CD2 1 ? 4  
ATOM   852  C CE1 . TYR A 1 112 ? 8.526   15.938  -17.540 1.000 48.173  0 114 TYR AAA CE1 1 ? 4  
ATOM   853  C CE2 . TYR A 1 112 ? 8.791   14.023  -18.950 1.000 48.102  0 114 TYR AAA CE2 1 ? 4  
ATOM   854  C CZ  . TYR A 1 112 ? 8.009   14.777  -18.093 1.000 47.576  0 114 TYR AAA CZ  1 ? 4  
ATOM   855  O OH  . TYR A 1 112 ? 6.741   14.368  -17.801 1.000 46.220  0 114 TYR AAA OH  1 ? 4  
ATOM   856  N N   . ASP A 1 113 ? 14.982  14.722  -19.058 1.000 50.868  0 115 ASP AAA N   1 ? 4  
ATOM   857  C CA  . ASP A 1 113 ? 16.421  14.502  -19.360 1.000 51.588  0 115 ASP AAA CA  1 ? 4  
ATOM   858  C C   . ASP A 1 113 ? 16.664  14.515  -20.872 1.000 52.660  0 115 ASP AAA C   1 ? 4  
ATOM   859  O O   . ASP A 1 113 ? 17.696  15.061  -21.290 1.000 55.570  0 115 ASP AAA O   1 ? 4  
ATOM   860  C CB  . ASP A 1 113 ? 16.902  13.184  -18.753 1.000 51.396  0 115 ASP AAA CB  1 ? 4  
ATOM   861  C CG  . ASP A 1 113 ? 16.666  13.104  -17.257 1.000 50.477  0 115 ASP AAA CG  1 ? 4  
ATOM   862  O OD1 . ASP A 1 113 ? 17.225  13.952  -16.540 1.000 51.618  0 115 ASP AAA OD1 1 ? 4  
ATOM   863  O OD2 . ASP A 1 113 ? 15.899  12.215  -16.825 1.000 50.492  0 115 ASP AAA OD2 1 ? 4  
ATOM   864  N N   . PHE A 1 114 ? 15.777  13.906  -21.661 1.000 52.181  0 116 PHE AAA N   1 ? 4  
ATOM   865  C CA  . PHE A 1 114 ? 15.934  13.757  -23.130 1.000 52.518  0 116 PHE AAA CA  1 ? 4  
ATOM   866  C C   . PHE A 1 114 ? 14.658  14.223  -23.834 1.000 52.939  0 116 PHE AAA C   1 ? 4  
ATOM   867  O O   . PHE A 1 114 ? 13.561  14.011  -23.283 1.000 51.083  0 116 PHE AAA O   1 ? 4  
ATOM   868  C CB  . PHE A 1 114 ? 16.310  12.313  -23.450 1.000 52.499  0 116 PHE AAA CB  1 ? 4  
ATOM   869  C CG  . PHE A 1 114 ? 17.571  11.878  -22.755 1.000 52.575  0 116 PHE AAA CG  1 ? 4  
ATOM   870  C CD1 . PHE A 1 114 ? 18.812  12.268  -23.236 1.000 53.873  0 116 PHE AAA CD1 1 ? 4  
ATOM   871  C CD2 . PHE A 1 114 ? 17.516  11.129  -21.590 1.000 51.849  0 116 PHE AAA CD2 1 ? 4  
ATOM   872  C CE1 . PHE A 1 114 ? 19.974  11.886  -22.586 1.000 54.434  0 116 PHE AAA CE1 1 ? 4  
ATOM   873  C CE2 . PHE A 1 114 ? 18.681  10.755  -20.936 1.000 52.285  0 116 PHE AAA CE2 1 ? 4  
ATOM   874  C CZ  . PHE A 1 114 ? 19.907  11.129  -21.439 1.000 53.918  0 116 PHE AAA CZ  1 ? 4  
ATOM   875  N N   . TRP A 1 115 ? 14.824  14.850  -25.003 1.000 54.192  0 117 TRP AAA N   1 ? 4  
ATOM   876  C CA  . TRP A 1 115 ? 13.752  15.516  -25.789 1.000 55.538  0 117 TRP AAA CA  1 ? 4  
ATOM   877  C C   . TRP A 1 115 ? 13.802  15.048  -27.248 1.000 58.304  0 117 TRP AAA C   1 ? 4  
ATOM   878  O O   . TRP A 1 115 ? 14.916  14.897  -27.793 1.000 59.371  0 117 TRP AAA O   1 ? 4  
ATOM   879  C CB  . TRP A 1 115 ? 13.896  17.039  -25.699 1.000 56.259  0 117 TRP AAA CB  1 ? 4  
ATOM   880  C CG  . TRP A 1 115 ? 13.788  17.584  -24.309 1.000 55.355  0 117 TRP AAA CG  1 ? 4  
ATOM   881  C CD1 . TRP A 1 115 ? 14.774  17.644  -23.368 1.000 55.393  0 117 TRP AAA CD1 1 ? 4  
ATOM   882  C CD2 . TRP A 1 115 ? 12.619  18.155  -23.698 1.000 54.699  0 117 TRP AAA CD2 1 ? 4  
ATOM   883  N NE1 . TRP A 1 115 ? 14.300  18.211  -22.214 1.000 54.910  0 117 TRP AAA NE1 1 ? 4  
ATOM   884  C CE2 . TRP A 1 115 ? 12.981  18.537  -22.385 1.000 54.569  0 117 TRP AAA CE2 1 ? 4  
ATOM   885  C CE3 . TRP A 1 115 ? 11.308  18.385  -24.128 1.000 54.794  0 117 TRP AAA CE3 1 ? 4  
ATOM   886  C CZ2 . TRP A 1 115 ? 12.075  19.131  -21.504 1.000 53.700  0 117 TRP AAA CZ2 1 ? 4  
ATOM   887  C CZ3 . TRP A 1 115 ? 10.412  18.963  -23.255 1.000 54.781  0 117 TRP AAA CZ3 1 ? 4  
ATOM   888  C CH2 . TRP A 1 115 ? 10.792  19.336  -21.963 1.000 54.033  0 117 TRP AAA CH2 1 ? 4  
ATOM   889  N N   . GLY A 1 116 ? 12.633  14.840  -27.860 1.000 58.909  0 118 GLY AAA N   1 ? 4  
ATOM   890  C CA  . GLY A 1 116 ? 12.493  14.660  -29.315 1.000 61.670  0 118 GLY AAA CA  1 ? 4  
ATOM   891  C C   . GLY A 1 116 ? 12.707  15.980  -30.030 1.000 63.698  0 118 GLY AAA C   1 ? 4  
ATOM   892  O O   . GLY A 1 116 ? 12.755  17.022  -29.342 1.000 63.021  0 118 GLY AAA O   1 ? 4  
ATOM   893  N N   . GLN A 1 117 ? 12.844  15.948  -31.357 1.000 66.633  0 119 GLN AAA N   1 ? 4  
ATOM   894  C CA  . GLN A 1 117 ? 13.048  17.162  -32.191 1.000 70.289  0 119 GLN AAA CA  1 ? 4  
ATOM   895  C C   . GLN A 1 117 ? 11.765  17.998  -32.195 1.000 69.530  0 119 GLN AAA C   1 ? 4  
ATOM   896  O O   . GLN A 1 117 ? 11.866  19.223  -32.383 1.000 70.799  0 119 GLN AAA O   1 ? 4  
ATOM   897  C CB  . GLN A 1 117 ? 13.466  16.775  -33.607 1.000 74.968  0 119 GLN AAA CB  1 ? 4  
ATOM   898  C CG  . GLN A 1 117 ? 14.877  16.214  -33.680 1.000 77.206  0 119 GLN AAA CG  1 ? 4  
ATOM   899  C CD  . GLN A 1 117 ? 15.139  15.523  -34.997 1.000 83.130  0 119 GLN AAA CD  1 ? 4  
ATOM   900  O OE1 . GLN A 1 117 ? 15.025  16.113  -36.074 1.000 86.464  0 119 GLN AAA OE1 1 ? 4  
ATOM   901  N NE2 . GLN A 1 117 ? 15.487  14.249  -34.920 1.000 84.597  0 119 GLN AAA NE2 1 ? 4  
ATOM   902  N N   . GLY A 1 118 ? 10.614  17.351  -31.995 1.000 67.894  0 120 GLY AAA N   1 ? 4  
ATOM   903  C CA  . GLY A 1 118 ? 9.287   17.995  -31.944 1.000 68.085  0 120 GLY AAA CA  1 ? 4  
ATOM   904  C C   . GLY A 1 118 ? 8.604   17.941  -33.299 1.000 70.388  0 120 GLY AAA C   1 ? 4  
ATOM   905  O O   . GLY A 1 118 ? 9.305   18.112  -34.311 1.000 72.244  0 120 GLY AAA O   1 ? 4  
ATOM   906  N N   . ILE A 1 119 ? 7.287   17.716  -33.313 1.000 70.857  0 121 ILE AAA N   1 ? 4  
ATOM   907  C CA  . ILE A 1 119 ? 6.459   17.589  -34.550 1.000 74.827  0 121 ILE AAA CA  1 ? 4  
ATOM   908  C C   . ILE A 1 119 ? 5.376   18.672  -34.536 1.000 75.422  0 121 ILE AAA C   1 ? 4  
ATOM   909  O O   . ILE A 1 119 ? 4.781   18.910  -33.465 1.000 73.714  0 121 ILE AAA O   1 ? 4  
ATOM   910  C CB  . ILE A 1 119 ? 5.860   16.174  -34.694 1.000 76.398  0 121 ILE AAA CB  1 ? 4  
ATOM   911  C CG1 . ILE A 1 119 ? 5.292   15.641  -33.375 1.000 74.552  0 121 ILE AAA CG1 1 ? 4  
ATOM   912  C CG2 . ILE A 1 119 ? 6.889   15.224  -35.286 1.000 77.488  0 121 ILE AAA CG2 1 ? 4  
ATOM   913  C CD1 . ILE A 1 119 ? 4.422   14.413  -33.535 1.000 76.115  0 121 ILE AAA CD1 1 ? 4  
ATOM   914  N N   . GLN A 1 120 ? 5.143   19.297  -35.693 1.000 78.475  0 122 GLN AAA N   1 ? 4  
ATOM   915  C CA  . GLN A 1 120 ? 4.169   20.405  -35.875 1.000 79.417  0 122 GLN AAA CA  1 ? 4  
ATOM   916  C C   . GLN A 1 120 ? 2.759   19.809  -35.930 1.000 80.546  0 122 GLN AAA C   1 ? 4  
ATOM   917  O O   . GLN A 1 120 ? 2.535   18.889  -36.742 1.000 82.915  0 122 GLN AAA O   1 ? 4  
ATOM   918  C CB  . GLN A 1 120 ? 4.515   21.203  -37.137 1.000 82.208  0 122 GLN AAA CB  1 ? 4  
ATOM   919  C CG  . GLN A 1 120 ? 3.643   22.434  -37.358 1.000 84.029  0 122 GLN AAA CG  1 ? 4  
ATOM   920  C CD  . GLN A 1 120 ? 3.818   23.486  -36.288 1.000 81.800  0 122 GLN AAA CD  1 ? 4  
ATOM   921  O OE1 . GLN A 1 120 ? 4.901   24.037  -36.100 1.000 81.146  0 122 GLN AAA OE1 1 ? 4  
ATOM   922  N NE2 . GLN A 1 120 ? 2.745   23.775  -35.570 1.000 80.892  0 122 GLN AAA NE2 1 ? 4  
ATOM   923  N N   . VAL A 1 121 ? 1.865   20.294  -35.065 1.000 79.663  0 123 VAL AAA N   1 ? 4  
ATOM   924  C CA  . VAL A 1 121 ? 0.394   20.050  -35.127 1.000 82.374  0 123 VAL AAA CA  1 ? 4  
ATOM   925  C C   . VAL A 1 121 ? -0.275  21.405  -35.376 1.000 84.686  0 123 VAL AAA C   1 ? 4  
ATOM   926  O O   . VAL A 1 121 ? -0.157  22.283  -34.501 1.000 83.290  0 123 VAL AAA O   1 ? 4  
ATOM   927  C CB  . VAL A 1 121 ? -0.138  19.384  -33.842 1.000 79.916  0 123 VAL AAA CB  1 ? 4  
ATOM   928  C CG1 . VAL A 1 121 ? -1.649  19.209  -33.886 1.000 82.023  0 123 VAL AAA CG1 1 ? 4  
ATOM   929  C CG2 . VAL A 1 121 ? 0.549   18.055  -33.561 1.000 78.019  0 123 VAL AAA CG2 1 ? 4  
ATOM   930  N N   . THR A 1 122 ? -0.911  21.574  -36.539 1.000 88.935  0 124 THR AAA N   1 ? 4  
ATOM   931  C CA  . THR A 1 122 ? -1.668  22.794  -36.928 1.000 91.955  0 124 THR AAA CA  1 ? 4  
ATOM   932  C C   . THR A 1 122 ? -3.133  22.400  -37.148 1.000 95.013  0 124 THR AAA C   1 ? 4  
ATOM   933  O O   . THR A 1 122 ? -3.390  21.536  -38.009 1.000 99.083  0 124 THR AAA O   1 ? 4  
ATOM   934  C CB  . THR A 1 122 ? -1.035  23.477  -38.148 1.000 94.890  0 124 THR AAA CB  1 ? 4  
ATOM   935  O OG1 . THR A 1 122 ? -0.497  22.466  -38.999 1.000 97.515  0 124 THR AAA OG1 1 ? 4  
ATOM   936  C CG2 . THR A 1 122 ? 0.070   24.446  -37.785 1.000 92.431  0 124 THR AAA CG2 1 ? 4  
ATOM   937  N N   . VAL A 1 123 ? -4.047  23.000  -36.380 1.000 94.394  0 125 VAL AAA N   1 ? 4  
ATOM   938  C CA  . VAL A 1 123 ? -5.489  22.611  -36.329 1.000 96.794  0 125 VAL AAA CA  1 ? 4  
ATOM   939  C C   . VAL A 1 123 ? -6.303  23.620  -37.149 1.000 100.363 0 125 VAL AAA C   1 ? 4  
ATOM   940  O O   . VAL A 1 123 ? -6.440  24.795  -36.818 1.000 99.457  0 125 VAL AAA O   1 ? 4  
ATOM   941  C CB  . VAL A 1 123 ? -5.996  22.456  -34.879 1.000 93.459  0 125 VAL AAA CB  1 ? 4  
ATOM   942  C CG1 . VAL A 1 123 ? -5.302  23.403  -33.911 1.000 90.450  0 125 VAL AAA CG1 1 ? 4  
ATOM   943  C CG2 . VAL A 1 123 ? -7.510  22.573  -34.777 1.000 96.169  0 125 VAL AAA CG2 1 ? 4  
ATOM   944  N N   . ASN B 2 2   ? 11.715  -8.946  15.955  1.000 93.507  0 331 ASN BBB N   1 ? 5  
ATOM   945  C CA  . ASN B 2 2   ? 10.433  -8.244  16.274  1.000 90.536  0 331 ASN BBB CA  1 ? 5  
ATOM   946  C C   . ASN B 2 2   ? 10.667  -6.730  16.194  1.000 86.980  0 331 ASN BBB C   1 ? 5  
ATOM   947  O O   . ASN B 2 2   ? 10.433  -6.044  17.211  1.000 86.377  0 331 ASN BBB O   1 ? 5  
ATOM   948  C CB  . ASN B 2 2   ? 9.871   -8.668  17.637  1.000 93.060  0 331 ASN BBB CB  1 ? 5  
ATOM   949  C CG  . ASN B 2 2   ? 9.234   -10.043 17.628  1.000 95.722  0 331 ASN BBB CG  1 ? 5  
ATOM   950  O OD1 . ASN B 2 2   ? 8.141   -10.232 18.160  1.000 96.107  0 331 ASN BBB OD1 1 ? 5  
ATOM   951  N ND2 . ASN B 2 2   ? 9.904   -11.013 17.028  1.000 97.547  0 331 ASN BBB ND2 1 ? 5  
ATOM   952  N N   . ILE B 2 3   ? 11.110  -6.240  15.027  1.000 84.860  0 332 ILE BBB N   1 ? 5  
ATOM   953  C CA  . ILE B 2 3   ? 11.385  -4.794  14.750  1.000 81.674  0 332 ILE BBB CA  1 ? 5  
ATOM   954  C C   . ILE B 2 3   ? 10.141  -3.982  15.133  1.000 79.982  0 332 ILE BBB C   1 ? 5  
ATOM   955  O O   . ILE B 2 3   ? 9.016   -4.533  15.048  1.000 79.850  0 332 ILE BBB O   1 ? 5  
ATOM   956  C CB  . ILE B 2 3   ? 11.814  -4.553  13.286  1.000 79.334  0 332 ILE BBB CB  1 ? 5  
ATOM   957  C CG1 . ILE B 2 3   ? 10.696  -4.888  12.293  1.000 78.924  0 332 ILE BBB CG1 1 ? 5  
ATOM   958  C CG2 . ILE B 2 3   ? 13.103  -5.299  12.974  1.000 81.113  0 332 ILE BBB CG2 1 ? 5  
ATOM   959  C CD1 . ILE B 2 3   ? 11.163  -5.058  10.863  1.000 79.005  0 332 ILE BBB CD1 1 ? 5  
ATOM   960  N N   . THR B 2 4   ? 10.345  -2.720  15.526  1.000 78.493  0 333 THR BBB N   1 ? 5  
ATOM   961  C CA  . THR B 2 4   ? 9.411   -1.926  16.371  1.000 79.674  0 333 THR BBB CA  1 ? 5  
ATOM   962  C C   . THR B 2 4   ? 8.718   -0.845  15.531  1.000 77.839  0 333 THR BBB C   1 ? 5  
ATOM   963  O O   . THR B 2 4   ? 9.374   0.160   15.206  1.000 77.446  0 333 THR BBB O   1 ? 5  
ATOM   964  C CB  . THR B 2 4   ? 10.154  -1.373  17.600  1.000 80.719  0 333 THR BBB CB  1 ? 5  
ATOM   965  O OG1 . THR B 2 4   ? 9.938   -2.262  18.701  1.000 82.224  0 333 THR BBB OG1 1 ? 5  
ATOM   966  C CG2 . THR B 2 4   ? 9.716   0.017   18.004  1.000 79.593  0 333 THR BBB CG2 1 ? 5  
ATOM   967  N N   . ASN B 2 5   ? 7.438   -1.053  15.201  1.000 78.549  0 334 ASN BBB N   1 ? 5  
ATOM   968  C CA  . ASN B 2 5   ? 6.512   0.013   14.736  1.000 78.222  0 334 ASN BBB CA  1 ? 5  
ATOM   969  C C   . ASN B 2 5   ? 6.761   0.348   13.256  1.000 72.315  0 334 ASN BBB C   1 ? 5  
ATOM   970  O O   . ASN B 2 5   ? 7.771   -0.113  12.681  1.000 68.397  0 334 ASN BBB O   1 ? 5  
ATOM   971  C CB  . ASN B 2 5   ? 6.657   1.263   15.613  1.000 84.402  0 334 ASN BBB CB  1 ? 5  
ATOM   972  C CG  . ASN B 2 5   ? 5.408   2.119   15.685  1.000 92.371  0 334 ASN BBB CG  1 ? 5  
ATOM   973  O OD1 . ASN B 2 5   ? 4.312   1.670   15.349  1.000 98.883  0 334 ASN BBB OD1 1 ? 5  
ATOM   974  N ND2 . ASN B 2 5   ? 5.564   3.355   16.133  1.000 95.779  0 334 ASN BBB ND2 1 ? 5  
ATOM   975  N N   . LEU B 2 6   ? 5.862   1.148   12.672  1.000 68.698  0 335 LEU BBB N   1 ? 5  
ATOM   976  C CA  . LEU B 2 6   ? 5.974   1.703   11.297  1.000 65.420  0 335 LEU BBB CA  1 ? 5  
ATOM   977  C C   . LEU B 2 6   ? 7.079   2.767   11.276  1.000 61.344  0 335 LEU BBB C   1 ? 5  
ATOM   978  O O   . LEU B 2 6   ? 7.109   3.592   12.214  1.000 59.901  0 335 LEU BBB O   1 ? 5  
ATOM   979  C CB  . LEU B 2 6   ? 4.625   2.305   10.886  1.000 66.630  0 335 LEU BBB CB  1 ? 5  
ATOM   980  C CG  . LEU B 2 6   ? 4.381   2.401   9.380   1.000 66.978  0 335 LEU BBB CG  1 ? 5  
ATOM   981  C CD1 . LEU B 2 6   ? 4.002   1.039   8.811   1.000 68.703  0 335 LEU BBB CD1 1 ? 5  
ATOM   982  C CD2 . LEU B 2 6   ? 3.315   3.437   9.059   1.000 67.790  0 335 LEU BBB CD2 1 ? 5  
ATOM   983  N N   . CYS B 2 7   ? 7.935   2.758   10.245  1.000 57.550  0 336 CYS BBB N   1 ? 5  
ATOM   984  C CA  . CYS B 2 7   ? 9.021   3.754   10.039  1.000 55.980  0 336 CYS BBB CA  1 ? 5  
ATOM   985  C C   . CYS B 2 7   ? 8.401   5.139   9.904   1.000 55.020  0 336 CYS BBB C   1 ? 5  
ATOM   986  O O   . CYS B 2 7   ? 7.406   5.309   9.203   1.000 55.318  0 336 CYS BBB O   1 ? 5  
ATOM   987  C CB  . CYS B 2 7   ? 9.875   3.457   8.809   1.000 54.553  0 336 CYS BBB CB  1 ? 5  
ATOM   988  S SG  . CYS B 2 7   ? 10.877  1.952   8.947   1.000 56.147  0 336 CYS BBB SG  1 ? 5  
ATOM   989  N N   . PRO B 2 8   ? 8.972   6.171   10.567  1.000 54.784  0 337 PRO BBB N   1 ? 5  
ATOM   990  C CA  . PRO B 2 8   ? 8.378   7.507   10.571  1.000 54.634  0 337 PRO BBB CA  1 ? 5  
ATOM   991  C C   . PRO B 2 8   ? 8.685   8.351   9.321   1.000 52.641  0 337 PRO BBB C   1 ? 5  
ATOM   992  O O   . PRO B 2 8   ? 9.174   9.442   9.469   1.000 52.638  0 337 PRO BBB O   1 ? 5  
ATOM   993  C CB  . PRO B 2 8   ? 9.017   8.101   11.838  1.000 55.458  0 337 PRO BBB CB  1 ? 5  
ATOM   994  C CG  . PRO B 2 8   ? 10.414  7.524   11.831  1.000 54.773  0 337 PRO BBB CG  1 ? 5  
ATOM   995  C CD  . PRO B 2 8   ? 10.205  6.098   11.370  1.000 54.990  0 337 PRO BBB CD  1 ? 5  
ATOM   996  N N   . PHE B 2 9   ? 8.352   7.855   8.127   1.000 52.603  0 338 PHE BBB N   1 ? 5  
ATOM   997  C CA  . PHE B 2 9   ? 8.489   8.603   6.848   1.000 51.568  0 338 PHE BBB CA  1 ? 5  
ATOM   998  C C   . PHE B 2 9   ? 7.519   9.785   6.842   1.000 50.793  0 338 PHE BBB C   1 ? 5  
ATOM   999  O O   . PHE B 2 9   ? 7.878   10.838  6.277   1.000 49.131  0 338 PHE BBB O   1 ? 5  
ATOM   1000 C CB  . PHE B 2 9   ? 8.267   7.694   5.638   1.000 53.282  0 338 PHE BBB CB  1 ? 5  
ATOM   1001 C CG  . PHE B 2 9   ? 9.409   6.750   5.363   1.000 55.446  0 338 PHE BBB CG  1 ? 5  
ATOM   1002 C CD1 . PHE B 2 9   ? 10.713  7.218   5.282   1.000 55.657  0 338 PHE BBB CD1 1 ? 5  
ATOM   1003 C CD2 . PHE B 2 9   ? 9.185   5.395   5.171   1.000 58.447  0 338 PHE BBB CD2 1 ? 5  
ATOM   1004 C CE1 . PHE B 2 9   ? 11.764  6.353   5.026   1.000 56.825  0 338 PHE BBB CE1 1 ? 5  
ATOM   1005 C CE2 . PHE B 2 9   ? 10.240  4.531   4.922   1.000 59.338  0 338 PHE BBB CE2 1 ? 5  
ATOM   1006 C CZ  . PHE B 2 9   ? 11.527  5.010   4.856   1.000 58.759  0 338 PHE BBB CZ  1 ? 5  
ATOM   1007 N N   . GLY B 2 10  ? 6.347   9.616   7.463   1.000 51.435  0 339 GLY BBB N   1 ? 5  
ATOM   1008 C CA  . GLY B 2 10  ? 5.349   10.687  7.645   1.000 52.449  0 339 GLY BBB CA  1 ? 5  
ATOM   1009 C C   . GLY B 2 10  ? 5.984   11.937  8.224   1.000 51.921  0 339 GLY BBB C   1 ? 5  
ATOM   1010 O O   . GLY B 2 10  ? 5.756   13.024  7.668   1.000 50.877  0 339 GLY BBB O   1 ? 5  
ATOM   1011 N N   . GLU B 2 11  ? 6.773   11.784  9.293   1.000 53.106  0 340 GLU BBB N   1 ? 5  
ATOM   1012 C CA  . GLU B 2 11  ? 7.465   12.897  10.002  1.000 53.899  0 340 GLU BBB CA  1 ? 5  
ATOM   1013 C C   . GLU B 2 11  ? 8.388   13.629  9.023   1.000 50.830  0 340 GLU BBB C   1 ? 5  
ATOM   1014 O O   . GLU B 2 11  ? 8.490   14.861  9.123   1.000 51.328  0 340 GLU BBB O   1 ? 5  
ATOM   1015 C CB  . GLU B 2 11  ? 8.291   12.381  11.181  1.000 55.820  0 340 GLU BBB CB  1 ? 5  
ATOM   1016 C CG  . GLU B 2 11  ? 7.460   11.892  12.349  1.000 60.736  0 340 GLU BBB CG  1 ? 5  
ATOM   1017 C CD  . GLU B 2 11  ? 8.279   11.389  13.529  1.000 63.315  0 340 GLU BBB CD  1 ? 5  
ATOM   1018 O OE1 . GLU B 2 11  ? 9.504   11.676  13.575  1.000 63.137  0 340 GLU BBB OE1 1 ? 5  
ATOM   1019 O OE2 . GLU B 2 11  ? 7.699   10.686  14.381  1.000 66.037  0 340 GLU BBB OE2 1 ? 5  
ATOM   1020 N N   . VAL B 2 12  ? 9.039   12.894  8.122   1.000 48.306  0 341 VAL BBB N   1 ? 5  
ATOM   1021 C CA  . VAL B 2 12  ? 10.026  13.445  7.151   1.000 46.758  0 341 VAL BBB CA  1 ? 5  
ATOM   1022 C C   . VAL B 2 12  ? 9.266   14.148  6.019   1.000 46.350  0 341 VAL BBB C   1 ? 5  
ATOM   1023 O O   . VAL B 2 12  ? 9.475   15.360  5.835   1.000 45.657  0 341 VAL BBB O   1 ? 5  
ATOM   1024 C CB  . VAL B 2 12  ? 10.966  12.337  6.638   1.000 45.928  0 341 VAL BBB CB  1 ? 5  
ATOM   1025 C CG1 . VAL B 2 12  ? 11.936  12.843  5.578   1.000 44.573  0 341 VAL BBB CG1 1 ? 5  
ATOM   1026 C CG2 . VAL B 2 12  ? 11.732  11.702  7.789   1.000 46.471  0 341 VAL BBB CG2 1 ? 5  
ATOM   1027 N N   . PHE B 2 13  ? 8.402   13.417  5.312   1.000 46.724  0 342 PHE BBB N   1 ? 5  
ATOM   1028 C CA  . PHE B 2 13  ? 7.735   13.880  4.065   1.000 48.208  0 342 PHE BBB CA  1 ? 5  
ATOM   1029 C C   . PHE B 2 13  ? 6.681   14.946  4.383   1.000 50.473  0 342 PHE BBB C   1 ? 5  
ATOM   1030 O O   . PHE B 2 13  ? 6.514   15.860  3.555   1.000 49.683  0 342 PHE BBB O   1 ? 5  
ATOM   1031 C CB  . PHE B 2 13  ? 7.134   12.704  3.293   1.000 48.884  0 342 PHE BBB CB  1 ? 5  
ATOM   1032 C CG  . PHE B 2 13  ? 8.149   11.862  2.562   1.000 48.252  0 342 PHE BBB CG  1 ? 5  
ATOM   1033 C CD1 . PHE B 2 13  ? 8.546   12.181  1.272   1.000 48.593  0 342 PHE BBB CD1 1 ? 5  
ATOM   1034 C CD2 . PHE B 2 13  ? 8.722   10.758  3.172   1.000 48.265  0 342 PHE BBB CD2 1 ? 5  
ATOM   1035 C CE1 . PHE B 2 13  ? 9.482   11.404  0.603   1.000 48.845  0 342 PHE BBB CE1 1 ? 5  
ATOM   1036 C CE2 . PHE B 2 13  ? 9.659   9.982   2.505   1.000 48.667  0 342 PHE BBB CE2 1 ? 5  
ATOM   1037 C CZ  . PHE B 2 13  ? 10.036  10.305  1.219   1.000 48.813  0 342 PHE BBB CZ  1 ? 5  
ATOM   1038 N N   . ASN B 2 14  ? 6.011   14.843  5.539   1.000 53.774  0 343 ASN BBB N   1 ? 5  
ATOM   1039 C CA  . ASN B 2 14  ? 4.821   15.668  5.889   1.000 57.719  0 343 ASN BBB CA  1 ? 5  
ATOM   1040 C C   . ASN B 2 14  ? 5.140   16.650  7.026   1.000 57.455  0 343 ASN BBB C   1 ? 5  
ATOM   1041 O O   . ASN B 2 14  ? 4.188   17.255  7.555   1.000 59.784  0 343 ASN BBB O   1 ? 5  
ATOM   1042 C CB  . ASN B 2 14  ? 3.621   14.781  6.228   1.000 61.823  0 343 ASN BBB CB  1 ? 5  
ATOM   1043 C CG  . ASN B 2 14  ? 2.877   14.296  5.005   1.000 65.384  0 343 ASN BBB CG  1 ? 5  
ATOM   1044 O OD1 . ASN B 2 14  ? 2.779   15.006  4.008   1.000 64.829  0 343 ASN BBB OD1 1 ? 5  
ATOM   1045 N ND2 . ASN B 2 14  ? 2.345   13.091  5.082   1.000 73.083  0 343 ASN BBB ND2 1 ? 5  
ATOM   1046 N N   . ALA B 2 15  ? 6.419   16.832  7.371   1.000 54.563  0 344 ALA BBB N   1 ? 5  
ATOM   1047 C CA  . ALA B 2 15  ? 6.891   17.895  8.288   1.000 54.917  0 344 ALA BBB CA  1 ? 5  
ATOM   1048 C C   . ALA B 2 15  ? 6.296   19.233  7.833   1.000 56.227  0 344 ALA BBB C   1 ? 5  
ATOM   1049 O O   . ALA B 2 15  ? 6.283   19.481  6.617   1.000 55.998  0 344 ALA BBB O   1 ? 5  
ATOM   1050 C CB  . ALA B 2 15  ? 8.397   17.937  8.293   1.000 52.375  0 344 ALA BBB CB  1 ? 5  
ATOM   1051 N N   . THR B 2 16  ? 5.830   20.067  8.763   1.000 58.601  0 345 THR BBB N   1 ? 5  
ATOM   1052 C CA  . THR B 2 16  ? 5.132   21.341  8.437   1.000 61.235  0 345 THR BBB CA  1 ? 5  
ATOM   1053 C C   . THR B 2 16  ? 6.162   22.328  7.874   1.000 59.634  0 345 THR BBB C   1 ? 5  
ATOM   1054 O O   . THR B 2 16  ? 5.812   23.052  6.928   1.000 59.423  0 345 THR BBB O   1 ? 5  
ATOM   1055 C CB  . THR B 2 16  ? 4.332   21.879  9.633   1.000 64.983  0 345 THR BBB CB  1 ? 5  
ATOM   1056 O OG1 . THR B 2 16  ? 5.244   22.461  10.561  1.000 65.830  0 345 THR BBB OG1 1 ? 5  
ATOM   1057 C CG2 . THR B 2 16  ? 3.504   20.819  10.328  1.000 66.276  0 345 THR BBB CG2 1 ? 5  
ATOM   1058 N N   . ARG B 2 17  ? 7.384   22.336  8.423   1.000 59.337  0 346 ARG BBB N   1 ? 5  
ATOM   1059 C CA  . ARG B 2 17  ? 8.558   23.089  7.894   1.000 57.923  0 346 ARG BBB CA  1 ? 5  
ATOM   1060 C C   . ARG B 2 17  ? 9.672   22.103  7.524   1.000 52.429  0 346 ARG BBB C   1 ? 5  
ATOM   1061 O O   . ARG B 2 17  ? 9.829   21.092  8.222   1.000 52.532  0 346 ARG BBB O   1 ? 5  
ATOM   1062 C CB  . ARG B 2 17  ? 9.103   24.069  8.937   1.000 62.279  0 346 ARG BBB CB  1 ? 5  
ATOM   1063 C CG  . ARG B 2 17  ? 8.358   25.390  9.045   1.000 68.616  0 346 ARG BBB CG  1 ? 5  
ATOM   1064 C CD  . ARG B 2 17  ? 9.023   26.286  10.074  1.000 74.050  0 346 ARG BBB CD  1 ? 5  
ATOM   1065 N NE  . ARG B 2 17  ? 8.110   27.284  10.625  1.000 82.055  0 346 ARG BBB NE  1 ? 5  
ATOM   1066 C CZ  . ARG B 2 17  ? 8.415   28.157  11.587  1.000 87.378  0 346 ARG BBB CZ  1 ? 5  
ATOM   1067 N NH1 . ARG B 2 17  ? 9.625   28.173  12.126  1.000 87.521  0 346 ARG BBB NH1 1 ? 5  
ATOM   1068 N NH2 . ARG B 2 17  ? 7.504   29.019  12.008  1.000 92.551  0 346 ARG BBB NH2 1 ? 5  
ATOM   1069 N N   . PHE B 2 18  ? 10.435  22.412  6.479   1.000 48.640  0 347 PHE BBB N   1 ? 5  
ATOM   1070 C CA  . PHE B 2 18  ? 11.664  21.681  6.071   1.000 44.952  0 347 PHE BBB CA  1 ? 5  
ATOM   1071 C C   . PHE B 2 18  ? 12.889  22.516  6.458   1.000 43.688  0 347 PHE BBB C   1 ? 5  
ATOM   1072 O O   . PHE B 2 18  ? 12.743  23.728  6.730   1.000 44.692  0 347 PHE BBB O   1 ? 5  
ATOM   1073 C CB  . PHE B 2 18  ? 11.632  21.371  4.571   1.000 43.607  0 347 PHE BBB CB  1 ? 5  
ATOM   1074 C CG  . PHE B 2 18  ? 11.075  20.014  4.218   1.000 43.138  0 347 PHE BBB CG  1 ? 5  
ATOM   1075 C CD1 . PHE B 2 18  ? 9.914   19.545  4.818   1.000 44.321  0 347 PHE BBB CD1 1 ? 5  
ATOM   1076 C CD2 . PHE B 2 18  ? 11.711  19.209  3.283   1.000 41.618  0 347 PHE BBB CD2 1 ? 5  
ATOM   1077 C CE1 . PHE B 2 18  ? 9.414   18.295  4.502   1.000 44.292  0 347 PHE BBB CE1 1 ? 5  
ATOM   1078 C CE2 . PHE B 2 18  ? 11.206  17.958  2.966   1.000 41.752  0 347 PHE BBB CE2 1 ? 5  
ATOM   1079 C CZ  . PHE B 2 18  ? 10.056  17.506  3.572   1.000 42.989  0 347 PHE BBB CZ  1 ? 5  
ATOM   1080 N N   . ALA B 2 19  ? 14.060  21.878  6.481   1.000 41.481  0 348 ALA BBB N   1 ? 5  
ATOM   1081 C CA  . ALA B 2 19  ? 15.371  22.520  6.730   1.000 40.718  0 348 ALA BBB CA  1 ? 5  
ATOM   1082 C C   . ALA B 2 19  ? 15.760  23.374  5.525   1.000 38.831  0 348 ALA BBB C   1 ? 5  
ATOM   1083 O O   . ALA B 2 19  ? 15.409  22.999  4.395   1.000 38.318  0 348 ALA BBB O   1 ? 5  
ATOM   1084 C CB  . ALA B 2 19  ? 16.422  21.470  6.995   1.000 40.050  0 348 ALA BBB CB  1 ? 5  
ATOM   1085 N N   . SER B 2 20  ? 16.478  24.471  5.764   1.000 39.222  0 349 SER BBB N   1 ? 5  
ATOM   1086 C CA  . SER B 2 20  ? 17.297  25.165  4.737   1.000 38.397  0 349 SER BBB CA  1 ? 5  
ATOM   1087 C C   . SER B 2 20  ? 18.343  24.186  4.191   1.000 36.831  0 349 SER BBB C   1 ? 5  
ATOM   1088 O O   . SER B 2 20  ? 18.857  23.373  4.974   1.000 36.418  0 349 SER BBB O   1 ? 5  
ATOM   1089 C CB  . SER B 2 20  ? 17.937  26.395  5.293   1.000 39.403  0 349 SER BBB CB  1 ? 5  
ATOM   1090 O OG  . SER B 2 20  ? 17.037  27.484  5.246   1.000 40.426  0 349 SER BBB OG  1 ? 5  
ATOM   1091 N N   . VAL B 2 21  ? 18.631  24.247  2.891   1.000 36.705  0 350 VAL BBB N   1 ? 5  
ATOM   1092 C CA  . VAL B 2 21  ? 19.552  23.284  2.211   1.000 36.660  0 350 VAL BBB CA  1 ? 5  
ATOM   1093 C C   . VAL B 2 21  ? 20.952  23.339  2.856   1.000 37.372  0 350 VAL BBB C   1 ? 5  
ATOM   1094 O O   . VAL B 2 21  ? 21.561  22.260  3.002   1.000 37.519  0 350 VAL BBB O   1 ? 5  
ATOM   1095 C CB  . VAL B 2 21  ? 19.588  23.512  0.691   1.000 36.635  0 350 VAL BBB CB  1 ? 5  
ATOM   1096 C CG1 . VAL B 2 21  ? 20.193  24.858  0.323   1.000 37.097  0 350 VAL BBB CG1 1 ? 5  
ATOM   1097 C CG2 . VAL B 2 21  ? 20.295  22.376  -0.029  1.000 37.113  0 350 VAL BBB CG2 1 ? 5  
ATOM   1098 N N   . TYR B 2 22  ? 21.438  24.517  3.268   1.000 38.067  0 351 TYR BBB N   1 ? 5  
ATOM   1099 C CA  . TYR B 2 22  ? 22.791  24.684  3.870   1.000 39.633  0 351 TYR BBB CA  1 ? 5  
ATOM   1100 C C   . TYR B 2 22  ? 22.853  23.911  5.191   1.000 41.535  0 351 TYR BBB C   1 ? 5  
ATOM   1101 O O   . TYR B 2 22  ? 23.906  23.313  5.479   1.000 43.794  0 351 TYR BBB O   1 ? 5  
ATOM   1102 C CB  . TYR B 2 22  ? 23.166  26.157  4.060   1.000 39.822  0 351 TYR BBB CB  1 ? 5  
ATOM   1103 C CG  . TYR B 2 22  ? 22.695  26.778  5.350   1.000 41.538  0 351 TYR BBB CG  1 ? 5  
ATOM   1104 C CD1 . TYR B 2 22  ? 21.445  27.371  5.442   1.000 41.571  0 351 TYR BBB CD1 1 ? 5  
ATOM   1105 C CD2 . TYR B 2 22  ? 23.502  26.788  6.479   1.000 43.561  0 351 TYR BBB CD2 1 ? 5  
ATOM   1106 C CE1 . TYR B 2 22  ? 21.003  27.948  6.622   1.000 43.608  0 351 TYR BBB CE1 1 ? 5  
ATOM   1107 C CE2 . TYR B 2 22  ? 23.074  27.357  7.670   1.000 45.218  0 351 TYR BBB CE2 1 ? 5  
ATOM   1108 C CZ  . TYR B 2 22  ? 21.821  27.941  7.740   1.000 45.382  0 351 TYR BBB CZ  1 ? 5  
ATOM   1109 O OH  . TYR B 2 22  ? 21.387  28.512  8.900   1.000 47.654  0 351 TYR BBB OH  1 ? 5  
ATOM   1110 N N   . ALA B 2 23  ? 21.759  23.923  5.960   1.000 42.229  0 352 ALA BBB N   1 ? 5  
ATOM   1111 C CA  . ALA B 2 23  ? 21.616  23.203  7.247   1.000 43.567  0 352 ALA BBB CA  1 ? 5  
ATOM   1112 C C   . ALA B 2 23  ? 20.706  21.989  7.047   1.000 42.891  0 352 ALA BBB C   1 ? 5  
ATOM   1113 O O   . ALA B 2 23  ? 19.824  21.755  7.896   1.000 44.158  0 352 ALA BBB O   1 ? 5  
ATOM   1114 C CB  . ALA B 2 23  ? 21.083  24.139  8.303   1.000 45.450  0 352 ALA BBB CB  1 ? 5  
ATOM   1115 N N   . TRP B 2 24  ? 20.929  21.231  5.971   1.000 41.998  0 353 TRP BBB N   1 ? 5  
ATOM   1116 C CA  . TRP B 2 24  ? 20.063  20.090  5.571   1.000 41.736  0 353 TRP BBB CA  1 ? 5  
ATOM   1117 C C   . TRP B 2 24  ? 19.912  19.113  6.738   1.000 43.237  0 353 TRP BBB C   1 ? 5  
ATOM   1118 O O   . TRP B 2 24  ? 20.884  18.908  7.485   1.000 44.373  0 353 TRP BBB O   1 ? 5  
ATOM   1119 C CB  . TRP B 2 24  ? 20.572  19.386  4.308   1.000 41.085  0 353 TRP BBB CB  1 ? 5  
ATOM   1120 C CG  . TRP B 2 24  ? 21.991  18.909  4.345   1.000 41.179  0 353 TRP BBB CG  1 ? 5  
ATOM   1121 C CD1 . TRP B 2 24  ? 23.098  19.613  3.975   1.000 41.313  0 353 TRP BBB CD1 1 ? 5  
ATOM   1122 C CD2 . TRP B 2 24  ? 22.449  17.591  4.694   1.000 41.793  0 353 TRP BBB CD2 1 ? 5  
ATOM   1123 N NE1 . TRP B 2 24  ? 24.214  18.834  4.090   1.000 42.665  0 353 TRP BBB NE1 1 ? 5  
ATOM   1124 C CE2 . TRP B 2 24  ? 23.851  17.590  4.530   1.000 42.942  0 353 TRP BBB CE2 1 ? 5  
ATOM   1125 C CE3 . TRP B 2 24  ? 21.819  16.416  5.125   1.000 41.901  0 353 TRP BBB CE3 1 ? 5  
ATOM   1126 C CZ2 . TRP B 2 24  ? 24.632  16.464  4.790   1.000 44.395  0 353 TRP BBB CZ2 1 ? 5  
ATOM   1127 C CZ3 . TRP B 2 24  ? 22.590  15.302  5.385   1.000 43.495  0 353 TRP BBB CZ3 1 ? 5  
ATOM   1128 C CH2 . TRP B 2 24  ? 23.979  15.329  5.220   1.000 44.884  0 353 TRP BBB CH2 1 ? 5  
ATOM   1129 N N   . ASN B 2 25  ? 18.714  18.550  6.880   1.000 43.832  0 354 ASN BBB N   1 ? 5  
ATOM   1130 C CA  . ASN B 2 25  ? 18.367  17.621  7.980   1.000 44.954  0 354 ASN BBB CA  1 ? 5  
ATOM   1131 C C   . ASN B 2 25  ? 18.645  16.187  7.521   1.000 44.648  0 354 ASN BBB C   1 ? 5  
ATOM   1132 O O   . ASN B 2 25  ? 18.405  15.890  6.343   1.000 43.064  0 354 ASN BBB O   1 ? 5  
ATOM   1133 C CB  . ASN B 2 25  ? 16.921  17.807  8.437   1.000 45.857  0 354 ASN BBB CB  1 ? 5  
ATOM   1134 C CG  . ASN B 2 25  ? 16.651  17.068  9.727   1.000 48.339  0 354 ASN BBB CG  1 ? 5  
ATOM   1135 O OD1 . ASN B 2 25  ? 16.983  17.555  10.805  1.000 50.255  0 354 ASN BBB OD1 1 ? 5  
ATOM   1136 N ND2 . ASN B 2 25  ? 16.101  15.869  9.614   1.000 48.842  0 354 ASN BBB ND2 1 ? 5  
ATOM   1137 N N   . ARG B 2 26  ? 19.171  15.361  8.428   1.000 46.516  0 355 ARG BBB N   1 ? 5  
ATOM   1138 C CA  . ARG B 2 26  ? 19.309  13.890  8.282   1.000 47.141  0 355 ARG BBB CA  1 ? 5  
ATOM   1139 C C   . ARG B 2 26  ? 18.543  13.222  9.427   1.000 48.480  0 355 ARG BBB C   1 ? 5  
ATOM   1140 O O   . ARG B 2 26  ? 18.853  13.517  10.594  1.000 49.553  0 355 ARG BBB O   1 ? 5  
ATOM   1141 C CB  . ARG B 2 26  ? 20.781  13.478  8.323   1.000 48.894  0 355 ARG BBB CB  1 ? 5  
ATOM   1142 C CG  . ARG B 2 26  ? 21.013  11.981  8.164   1.000 51.038  0 355 ARG BBB CG  1 ? 5  
ATOM   1143 C CD  . ARG B 2 26  ? 22.475  11.580  8.289   1.000 54.503  0 355 ARG BBB CD  1 ? 5  
ATOM   1144 N NE  . ARG B 2 26  ? 23.309  11.972  7.152   1.000 55.200  0 355 ARG BBB NE  1 ? 5  
ATOM   1145 C CZ  . ARG B 2 26  ? 23.289  11.381  5.964   1.000 56.176  0 355 ARG BBB CZ  1 ? 5  
ATOM   1146 N NH1 . ARG B 2 26  ? 22.453  10.380  5.744   1.000 58.208  0 355 ARG BBB NH1 1 ? 5  
ATOM   1147 N NH2 . ARG B 2 26  ? 24.089  11.793  4.995   1.000 57.260  0 355 ARG BBB NH2 1 ? 5  
ATOM   1148 N N   . LYS B 2 27  ? 17.564  12.381  9.088   1.000 48.333  0 356 LYS BBB N   1 ? 5  
ATOM   1149 C CA  . LYS B 2 27  ? 16.885  11.447  10.022  1.000 49.985  0 356 LYS BBB CA  1 ? 5  
ATOM   1150 C C   . LYS B 2 27  ? 17.417  10.044  9.722   1.000 50.441  0 356 LYS BBB C   1 ? 5  
ATOM   1151 O O   . LYS B 2 27  ? 17.251  9.576   8.579   1.000 48.569  0 356 LYS BBB O   1 ? 5  
ATOM   1152 C CB  . LYS B 2 27  ? 15.362  11.553  9.868   1.000 50.249  0 356 LYS BBB CB  1 ? 5  
ATOM   1153 C CG  . LYS B 2 27  ? 14.525  10.505  10.597  1.000 52.439  0 356 LYS BBB CG  1 ? 5  
ATOM   1154 C CD  . LYS B 2 27  ? 14.147  10.853  12.026  1.000 55.314  0 356 LYS BBB CD  1 ? 5  
ATOM   1155 C CE  . LYS B 2 27  ? 13.307  9.769   12.672  1.000 57.181  0 356 LYS BBB CE  1 ? 5  
ATOM   1156 N NZ  . LYS B 2 27  ? 13.310  9.854   14.153  1.000 60.479  0 356 LYS BBB NZ  1 ? 5  
ATOM   1157 N N   . ARG B 2 28  ? 18.078  9.420   10.697  1.000 52.971  0 357 ARG BBB N   1 ? 5  
ATOM   1158 C CA  . ARG B 2 28  ? 18.488  7.997   10.607  1.000 55.764  0 357 ARG BBB CA  1 ? 5  
ATOM   1159 C C   . ARG B 2 28  ? 17.264  7.156   10.959  1.000 56.750  0 357 ARG BBB C   1 ? 5  
ATOM   1160 O O   . ARG B 2 28  ? 16.682  7.377   12.036  1.000 58.614  0 357 ARG BBB O   1 ? 5  
ATOM   1161 C CB  . ARG B 2 28  ? 19.670  7.683   11.524  1.000 59.413  0 357 ARG BBB CB  1 ? 5  
ATOM   1162 C CG  . ARG B 2 28  ? 20.089  6.220   11.505  1.000 63.135  0 357 ARG BBB CG  1 ? 5  
ATOM   1163 C CD  . ARG B 2 28  ? 21.545  6.053   11.889  1.000 67.594  0 357 ARG BBB CD  1 ? 5  
ATOM   1164 N NE  . ARG B 2 28  ? 21.745  5.030   12.899  1.000 71.676  0 357 ARG BBB NE  1 ? 5  
ATOM   1165 C CZ  . ARG B 2 28  ? 22.883  4.373   13.093  1.000 76.441  0 357 ARG BBB CZ  1 ? 5  
ATOM   1166 N NH1 . ARG B 2 28  ? 23.947  4.617   12.343  1.000 77.115  0 357 ARG BBB NH1 1 ? 5  
ATOM   1167 N NH2 . ARG B 2 28  ? 22.953  3.457   14.042  1.000 80.571  0 357 ARG BBB NH2 1 ? 5  
ATOM   1168 N N   . ILE B 2 29  ? 16.870  6.265   10.052  1.000 48.103  0 358 ILE BBB N   1 ? 6  
ATOM   1169 C CA  . ILE B 2 29  ? 15.686  5.377   10.208  1.000 48.467  0 358 ILE BBB CA  1 ? 6  
ATOM   1170 C C   . ILE B 2 29  ? 16.198  3.973   10.519  1.000 48.767  0 358 ILE BBB C   1 ? 6  
ATOM   1171 O O   . ILE B 2 29  ? 17.017  3.464   9.740   1.000 49.091  0 358 ILE BBB O   1 ? 6  
ATOM   1172 C CB  . ILE B 2 29  ? 14.805  5.439   8.946   1.000 48.184  0 358 ILE BBB CB  1 ? 6  
ATOM   1173 C CG1 . ILE B 2 29  ? 14.274  6.858   8.732   1.000 48.019  0 358 ILE BBB CG1 1 ? 6  
ATOM   1174 C CG2 . ILE B 2 29  ? 13.682  4.420   9.015   1.000 49.255  0 358 ILE BBB CG2 1 ? 6  
ATOM   1175 C CD1 . ILE B 2 29  ? 13.627  7.072   7.403   1.000 48.675  0 358 ILE BBB CD1 1 ? 6  
ATOM   1176 N N   . SER B 2 30  ? 15.730  3.397   11.627  1.000 49.047  0 359 SER BBB N   1 ? 6  
ATOM   1177 C CA  . SER B 2 30  ? 16.164  2.083   12.165  1.000 49.757  0 359 SER BBB CA  1 ? 6  
ATOM   1178 C C   . SER B 2 30  ? 15.015  1.441   12.949  1.000 49.601  0 359 SER BBB C   1 ? 6  
ATOM   1179 O O   . SER B 2 30  ? 14.105  2.181   13.373  1.000 48.423  0 359 SER BBB O   1 ? 6  
ATOM   1180 C CB  . SER B 2 30  ? 17.385  2.245   13.026  1.000 50.342  0 359 SER BBB CB  1 ? 6  
ATOM   1181 O OG  . SER B 2 30  ? 17.140  3.177   14.073  1.000 51.343  0 359 SER BBB OG  1 ? 6  
ATOM   1182 N N   . ASN B 2 31  ? 15.054  0.112   13.091  1.000 50.147  0 360 ASN BBB N   1 ? 6  
ATOM   1183 C CA  . ASN B 2 31  ? 14.176  -0.680  13.994  1.000 52.085  0 360 ASN BBB CA  1 ? 6  
ATOM   1184 C C   . ASN B 2 31  ? 12.709  -0.369  13.677  1.000 51.384  0 360 ASN BBB C   1 ? 6  
ATOM   1185 O O   . ASN B 2 31  ? 11.986  0.040   14.601  1.000 50.755  0 360 ASN BBB O   1 ? 6  
ATOM   1186 C CB  . ASN B 2 31  ? 14.466  -0.398  15.473  1.000 52.926  0 360 ASN BBB CB  1 ? 6  
ATOM   1187 C CG  . ASN B 2 31  ? 15.940  -0.246  15.773  1.000 53.881  0 360 ASN BBB CG  1 ? 6  
ATOM   1188 O OD1 . ASN B 2 31  ? 16.508  0.830   15.588  1.000 53.078  0 360 ASN BBB OD1 1 ? 6  
ATOM   1189 N ND2 . ASN B 2 31  ? 16.559  -1.310  16.254  1.000 55.879  0 360 ASN BBB ND2 1 ? 6  
ATOM   1190 N N   . CYS B 2 32  ? 12.285  -0.544  12.422  1.000 50.329  0 361 CYS BBB N   1 ? 6  
ATOM   1191 C CA  . CYS B 2 32  ? 10.904  -0.222  11.981  1.000 50.629  0 361 CYS BBB CA  1 ? 6  
ATOM   1192 C C   . CYS B 2 32  ? 10.562  -0.918  10.659  1.000 50.473  0 361 CYS BBB C   1 ? 6  
ATOM   1193 O O   . CYS B 2 32  ? 11.491  -1.262  9.915   1.000 50.423  0 361 CYS BBB O   1 ? 6  
ATOM   1194 C CB  . CYS B 2 32  ? 10.724  1.288   11.873  1.000 49.496  0 361 CYS BBB CB  1 ? 6  
ATOM   1195 S SG  . CYS B 2 32  ? 11.867  2.096   10.723  1.000 48.262  0 361 CYS BBB SG  1 ? 6  
ATOM   1196 N N   . VAL B 2 33  ? 9.263   -1.108  10.401  1.000 51.217  0 362 VAL BBB N   1 ? 6  
ATOM   1197 C CA  . VAL B 2 33  ? 8.707   -1.664  9.133   1.000 51.118  0 362 VAL BBB CA  1 ? 6  
ATOM   1198 C C   . VAL B 2 33  ? 8.460   -0.485  8.189   1.000 51.077  0 362 VAL BBB C   1 ? 6  
ATOM   1199 O O   . VAL B 2 33  ? 7.652   0.386   8.549   1.000 51.333  0 362 VAL BBB O   1 ? 6  
ATOM   1200 C CB  . VAL B 2 33  ? 7.411   -2.471  9.360   1.000 52.314  0 362 VAL BBB CB  1 ? 6  
ATOM   1201 C CG1 . VAL B 2 33  ? 6.919   -3.114  8.066   1.000 52.461  0 362 VAL BBB CG1 1 ? 6  
ATOM   1202 C CG2 . VAL B 2 33  ? 7.567   -3.520  10.449  1.000 53.272  0 362 VAL BBB CG2 1 ? 6  
ATOM   1203 N N   . ALA B 2 34  ? 9.144   -0.461  7.044   1.000 51.093  0 363 ALA BBB N   1 ? 6  
ATOM   1204 C CA  . ALA B 2 34  ? 9.094   0.630   6.044   1.000 52.013  0 363 ALA BBB CA  1 ? 6  
ATOM   1205 C C   . ALA B 2 34  ? 8.102   0.259   4.945   1.000 54.058  0 363 ALA BBB C   1 ? 6  
ATOM   1206 O O   . ALA B 2 34  ? 8.403   -0.681  4.192   1.000 57.079  0 363 ALA BBB O   1 ? 6  
ATOM   1207 C CB  . ALA B 2 34  ? 10.467  0.878   5.462   1.000 50.693  0 363 ALA BBB CB  1 ? 6  
ATOM   1208 N N   . ASP B 2 35  ? 6.978   0.973   4.858   1.000 54.717  0 364 ASP BBB N   1 ? 6  
ATOM   1209 C CA  . ASP B 2 35  ? 6.037   0.849   3.717   1.000 56.576  0 364 ASP BBB CA  1 ? 6  
ATOM   1210 C C   . ASP B 2 35  ? 6.443   1.865   2.645   1.000 54.551  0 364 ASP BBB C   1 ? 6  
ATOM   1211 O O   . ASP B 2 35  ? 6.068   3.040   2.775   1.000 55.767  0 364 ASP BBB O   1 ? 6  
ATOM   1212 C CB  . ASP B 2 35  ? 4.581   1.014   4.157   1.000 57.608  0 364 ASP BBB CB  1 ? 6  
ATOM   1213 C CG  . ASP B 2 35  ? 3.607   0.464   3.133   1.000 58.900  0 364 ASP BBB CG  1 ? 6  
ATOM   1214 O OD1 . ASP B 2 35  ? 3.990   0.349   1.945   1.000 57.445  0 364 ASP BBB OD1 1 ? 6  
ATOM   1215 O OD2 . ASP B 2 35  ? 2.476   0.120   3.538   1.000 65.227  0 364 ASP BBB OD2 1 ? 6  
ATOM   1216 N N   . TYR B 2 36  ? 7.188   1.424   1.630   1.000 52.300  0 365 TYR BBB N   1 ? 6  
ATOM   1217 C CA  . TYR B 2 36  ? 7.721   2.282   0.536   1.000 51.805  0 365 TYR BBB CA  1 ? 6  
ATOM   1218 C C   . TYR B 2 36  ? 6.653   2.507   -0.546  1.000 52.050  0 365 TYR BBB C   1 ? 6  
ATOM   1219 O O   . TYR B 2 36  ? 6.765   3.495   -1.289  1.000 52.219  0 365 TYR BBB O   1 ? 6  
ATOM   1220 C CB  . TYR B 2 36  ? 8.980   1.664   -0.076  1.000 50.598  0 365 TYR BBB CB  1 ? 6  
ATOM   1221 C CG  . TYR B 2 36  ? 10.127  1.451   0.884   1.000 49.537  0 365 TYR BBB CG  1 ? 6  
ATOM   1222 C CD1 . TYR B 2 36  ? 11.018  2.469   1.186   1.000 48.093  0 365 TYR BBB CD1 1 ? 6  
ATOM   1223 C CD2 . TYR B 2 36  ? 10.333  0.218   1.481   1.000 49.976  0 365 TYR BBB CD2 1 ? 6  
ATOM   1224 C CE1 . TYR B 2 36  ? 12.086  2.262   2.046   1.000 48.566  0 365 TYR BBB CE1 1 ? 6  
ATOM   1225 C CE2 . TYR B 2 36  ? 11.388  -0.001  2.352   1.000 50.145  0 365 TYR BBB CE2 1 ? 6  
ATOM   1226 C CZ  . TYR B 2 36  ? 12.274  1.023   2.634   1.000 49.512  0 365 TYR BBB CZ  1 ? 6  
ATOM   1227 O OH  . TYR B 2 36  ? 13.318  0.808   3.494   1.000 49.466  0 365 TYR BBB OH  1 ? 6  
ATOM   1228 N N   . SER B 2 37  ? 5.636   1.642   -0.620  1.000 53.859  0 366 SER BBB N   1 ? 6  
ATOM   1229 C CA  . SER B 2 37  ? 4.526   1.696   -1.612  1.000 55.196  0 366 SER BBB CA  1 ? 6  
ATOM   1230 C C   . SER B 2 37  ? 3.732   3.002   -1.476  1.000 55.536  0 366 SER BBB C   1 ? 6  
ATOM   1231 O O   . SER B 2 37  ? 3.238   3.484   -2.503  1.000 55.613  0 366 SER BBB O   1 ? 6  
ATOM   1232 C CB  . SER B 2 37  ? 3.626   0.490   -1.488  1.000 55.934  0 366 SER BBB CB  1 ? 6  
ATOM   1233 O OG  . SER B 2 37  ? 2.751   0.624   -0.380  1.000 56.681  0 366 SER BBB OG  1 ? 6  
ATOM   1234 N N   . VAL B 2 38  ? 3.632   3.558   -0.265  1.000 56.335  0 367 VAL BBB N   1 ? 6  
ATOM   1235 C CA  . VAL B 2 38  ? 2.979   4.871   0.023   1.000 57.580  0 367 VAL BBB CA  1 ? 6  
ATOM   1236 C C   . VAL B 2 38  ? 3.747   6.002   -0.678  1.000 57.345  0 367 VAL BBB C   1 ? 6  
ATOM   1237 O O   . VAL B 2 38  ? 3.172   7.096   -0.819  1.000 56.149  0 367 VAL BBB O   1 ? 6  
ATOM   1238 C CB  . VAL B 2 38  ? 2.881   5.127   1.541   1.000 59.663  0 367 VAL BBB CB  1 ? 6  
ATOM   1239 C CG1 . VAL B 2 38  ? 4.248   5.354   2.166   1.000 59.249  0 367 VAL BBB CG1 1 ? 6  
ATOM   1240 C CG2 . VAL B 2 38  ? 1.955   6.288   1.865   1.000 60.844  0 367 VAL BBB CG2 1 ? 6  
ATOM   1241 N N   . LEU B 2 39  ? 5.005   5.757   -1.069  1.000 58.829  0 368 LEU BBB N   1 ? 6  
ATOM   1242 C CA  . LEU B 2 39  ? 5.861   6.731   -1.793  1.000 58.270  0 368 LEU BBB CA  1 ? 6  
ATOM   1243 C C   . LEU B 2 39  ? 5.701   6.546   -3.307  1.000 58.640  0 368 LEU BBB C   1 ? 6  
ATOM   1244 O O   . LEU B 2 39  ? 5.270   7.511   -3.970  1.000 61.276  0 368 LEU BBB O   1 ? 6  
ATOM   1245 C CB  . LEU B 2 39  ? 7.323   6.561   -1.364  1.000 59.692  0 368 LEU BBB CB  1 ? 6  
ATOM   1246 C CG  . LEU B 2 39  ? 7.612   6.689   0.129   1.000 61.364  0 368 LEU BBB CG  1 ? 6  
ATOM   1247 C CD1 . LEU B 2 39  ? 9.105   6.557   0.393   1.000 60.767  0 368 LEU BBB CD1 1 ? 6  
ATOM   1248 C CD2 . LEU B 2 39  ? 7.077   8.005   0.671   1.000 61.111  0 368 LEU BBB CD2 1 ? 6  
ATOM   1249 N N   . TYR B 2 40  ? 6.031   5.366   -3.844  1.000 57.381  0 369 TYR BBB N   1 ? 6  
ATOM   1250 C CA  . TYR B 2 40  ? 6.179   5.155   -5.313  1.000 56.110  0 369 TYR BBB CA  1 ? 6  
ATOM   1251 C C   . TYR B 2 40  ? 4.808   4.989   -5.982  1.000 53.841  0 369 TYR BBB C   1 ? 6  
ATOM   1252 O O   . TYR B 2 40  ? 4.762   5.101   -7.217  1.000 55.250  0 369 TYR BBB O   1 ? 6  
ATOM   1253 C CB  . TYR B 2 40  ? 7.140   4.003   -5.640  1.000 57.675  0 369 TYR BBB CB  1 ? 6  
ATOM   1254 C CG  . TYR B 2 40  ? 6.782   2.634   -5.116  1.000 60.318  0 369 TYR BBB CG  1 ? 6  
ATOM   1255 C CD1 . TYR B 2 40  ? 5.719   1.914   -5.645  1.000 63.051  0 369 TYR BBB CD1 1 ? 6  
ATOM   1256 C CD2 . TYR B 2 40  ? 7.534   2.037   -4.118  1.000 60.785  0 369 TYR BBB CD2 1 ? 6  
ATOM   1257 C CE1 . TYR B 2 40  ? 5.394   0.651   -5.178  1.000 64.506  0 369 TYR BBB CE1 1 ? 6  
ATOM   1258 C CE2 . TYR B 2 40  ? 7.233   0.769   -3.646  1.000 62.108  0 369 TYR BBB CE2 1 ? 6  
ATOM   1259 C CZ  . TYR B 2 40  ? 6.159   0.073   -4.177  1.000 63.673  0 369 TYR BBB CZ  1 ? 6  
ATOM   1260 O OH  . TYR B 2 40  ? 5.851   -1.169  -3.700  1.000 63.892  0 369 TYR BBB OH  1 ? 6  
ATOM   1261 N N   . ASN B 2 41  ? 3.733   4.746   -5.224  1.000 52.010  0 370 ASN BBB N   1 ? 6  
ATOM   1262 C CA  . ASN B 2 41  ? 2.347   4.683   -5.772  1.000 51.280  0 370 ASN BBB CA  1 ? 6  
ATOM   1263 C C   . ASN B 2 41  ? 1.701   6.074   -5.746  1.000 49.581  0 370 ASN BBB C   1 ? 6  
ATOM   1264 O O   . ASN B 2 41  ? 0.608   6.216   -6.298  1.000 49.963  0 370 ASN BBB O   1 ? 6  
ATOM   1265 C CB  . ASN B 2 41  ? 1.466   3.673   -5.036  1.000 52.176  0 370 ASN BBB CB  1 ? 6  
ATOM   1266 C CG  . ASN B 2 41  ? 1.890   2.237   -5.264  1.000 53.568  0 370 ASN BBB CG  1 ? 6  
ATOM   1267 O OD1 . ASN B 2 41  ? 2.485   1.906   -6.287  1.000 54.001  0 370 ASN BBB OD1 1 ? 6  
ATOM   1268 N ND2 . ASN B 2 41  ? 1.571   1.369   -4.320  1.000 54.613  0 370 ASN BBB ND2 1 ? 6  
ATOM   1269 N N   . SER B 2 42  ? 2.351   7.063   -5.133  1.000 48.989  0 371 SER BBB N   1 ? 6  
ATOM   1270 C CA  . SER B 2 42  ? 1.863   8.464   -5.073  1.000 48.779  0 371 SER BBB CA  1 ? 6  
ATOM   1271 C C   . SER B 2 42  ? 2.027   9.121   -6.447  1.000 48.617  0 371 SER BBB C   1 ? 6  
ATOM   1272 O O   . SER B 2 42  ? 3.006   8.802   -7.139  1.000 49.634  0 371 SER BBB O   1 ? 6  
ATOM   1273 C CB  . SER B 2 42  ? 2.582   9.244   -4.000  1.000 47.461  0 371 SER BBB CB  1 ? 6  
ATOM   1274 O OG  . SER B 2 42  ? 2.133   10.589  -3.972  1.000 47.029  0 371 SER BBB OG  1 ? 6  
ATOM   1275 N N   . ALA B 2 43  ? 1.103   10.011  -6.817  1.000 49.274  0 372 ALA BBB N   1 ? 6  
ATOM   1276 C CA  . ALA B 2 43  ? 1.201   10.896  -8.005  1.000 49.325  0 372 ALA BBB CA  1 ? 6  
ATOM   1277 C C   . ALA B 2 43  ? 1.739   12.268  -7.579  1.000 48.515  0 372 ALA BBB C   1 ? 6  
ATOM   1278 O O   . ALA B 2 43  ? 1.926   13.122  -8.460  1.000 50.224  0 372 ALA BBB O   1 ? 6  
ATOM   1279 C CB  . ALA B 2 43  ? -0.140  11.020  -8.690  1.000 50.468  0 372 ALA BBB CB  1 ? 6  
ATOM   1280 N N   . SER B 2 44  ? 1.984   12.457  -6.281  1.000 48.016  0 373 SER BBB N   1 ? 6  
ATOM   1281 C CA  . SER B 2 44  ? 2.367   13.749  -5.651  1.000 48.418  0 373 SER BBB CA  1 ? 6  
ATOM   1282 C C   . SER B 2 44  ? 3.871   14.021  -5.788  1.000 47.433  0 373 SER BBB C   1 ? 6  
ATOM   1283 O O   . SER B 2 44  ? 4.249   15.191  -5.606  1.000 48.355  0 373 SER BBB O   1 ? 6  
ATOM   1284 C CB  . SER B 2 44  ? 1.942   13.779  -4.202  1.000 48.574  0 373 SER BBB CB  1 ? 6  
ATOM   1285 O OG  . SER B 2 44  ? 0.545   13.538  -4.086  1.000 49.522  0 373 SER BBB OG  1 ? 6  
ATOM   1286 N N   . PHE B 2 45  ? 4.695   13.004  -6.070  1.000 46.143  0 374 PHE BBB N   1 ? 6  
ATOM   1287 C CA  . PHE B 2 45  ? 6.165   13.150  -6.260  1.000 44.668  0 374 PHE BBB CA  1 ? 6  
ATOM   1288 C C   . PHE B 2 45  ? 6.473   13.209  -7.758  1.000 45.007  0 374 PHE BBB C   1 ? 6  
ATOM   1289 O O   . PHE B 2 45  ? 6.304   12.187  -8.453  1.000 46.551  0 374 PHE BBB O   1 ? 6  
ATOM   1290 C CB  . PHE B 2 45  ? 6.938   12.018  -5.580  1.000 43.925  0 374 PHE BBB CB  1 ? 6  
ATOM   1291 C CG  . PHE B 2 45  ? 6.616   11.845  -4.119  1.000 44.958  0 374 PHE BBB CG  1 ? 6  
ATOM   1292 C CD1 . PHE B 2 45  ? 6.771   12.900  -3.232  1.000 44.231  0 374 PHE BBB CD1 1 ? 6  
ATOM   1293 C CD2 . PHE B 2 45  ? 6.147   10.635  -3.626  1.000 45.598  0 374 PHE BBB CD2 1 ? 6  
ATOM   1294 C CE1 . PHE B 2 45  ? 6.473   12.748  -1.888  1.000 44.365  0 374 PHE BBB CE1 1 ? 6  
ATOM   1295 C CE2 . PHE B 2 45  ? 5.859   10.487  -2.276  1.000 45.325  0 374 PHE BBB CE2 1 ? 6  
ATOM   1296 C CZ  . PHE B 2 45  ? 6.010   11.544  -1.414  1.000 44.765  0 374 PHE BBB CZ  1 ? 6  
ATOM   1297 N N   . SER B 2 46  ? 6.898   14.383  -8.231  1.000 43.799  0 375 SER BBB N   1 ? 6  
ATOM   1298 C CA  . SER B 2 46  ? 7.223   14.668  -9.651  1.000 43.306  0 375 SER BBB CA  1 ? 6  
ATOM   1299 C C   . SER B 2 46  ? 8.624   14.131  -9.975  1.000 42.508  0 375 SER BBB C   1 ? 6  
ATOM   1300 O O   . SER B 2 46  ? 8.823   13.635  -11.087 1.000 42.428  0 375 SER BBB O   1 ? 6  
ATOM   1301 C CB  . SER B 2 46  ? 7.087   16.139  -9.936  1.000 43.156  0 375 SER BBB CB  1 ? 6  
ATOM   1302 O OG  . SER B 2 46  ? 7.780   16.910  -8.965  1.000 42.258  0 375 SER BBB OG  1 ? 6  
ATOM   1303 N N   . THR B 2 47  ? 9.551   14.202  -9.018  1.000 42.909  0 376 THR BBB N   1 ? 6  
ATOM   1304 C CA  . THR B 2 47  ? 10.888  13.551  -9.082  1.000 42.340  0 376 THR BBB CA  1 ? 6  
ATOM   1305 C C   . THR B 2 47  ? 10.936  12.401  -8.071  1.000 41.872  0 376 THR BBB C   1 ? 6  
ATOM   1306 O O   . THR B 2 47  ? 10.673  12.639  -6.890  1.000 43.431  0 376 THR BBB O   1 ? 6  
ATOM   1307 C CB  . THR B 2 47  ? 12.013  14.563  -8.839  1.000 42.090  0 376 THR BBB CB  1 ? 6  
ATOM   1308 O OG1 . THR B 2 47  ? 11.903  15.588  -9.829  1.000 43.397  0 376 THR BBB OG1 1 ? 6  
ATOM   1309 C CG2 . THR B 2 47  ? 13.389  13.934  -8.863  1.000 41.445  0 376 THR BBB CG2 1 ? 6  
ATOM   1310 N N   . PHE B 2 48  ? 11.234  11.195  -8.545  1.000 42.301  0 377 PHE BBB N   1 ? 6  
ATOM   1311 C CA  . PHE B 2 48  ? 11.523  9.985   -7.737  1.000 42.696  0 377 PHE BBB CA  1 ? 6  
ATOM   1312 C C   . PHE B 2 48  ? 12.583  9.190   -8.507  1.000 43.693  0 377 PHE BBB C   1 ? 6  
ATOM   1313 O O   . PHE B 2 48  ? 12.281  8.097   -9.040  1.000 43.936  0 377 PHE BBB O   1 ? 6  
ATOM   1314 C CB  . PHE B 2 48  ? 10.241  9.195   -7.471  1.000 43.492  0 377 PHE BBB CB  1 ? 6  
ATOM   1315 C CG  . PHE B 2 48  ? 10.286  8.249   -6.297  1.000 44.226  0 377 PHE BBB CG  1 ? 6  
ATOM   1316 C CD1 . PHE B 2 48  ? 11.430  7.527   -5.979  1.000 44.515  0 377 PHE BBB CD1 1 ? 6  
ATOM   1317 C CD2 . PHE B 2 48  ? 9.142   8.028   -5.548  1.000 45.705  0 377 PHE BBB CD2 1 ? 6  
ATOM   1318 C CE1 . PHE B 2 48  ? 11.445  6.658   -4.898  1.000 45.514  0 377 PHE BBB CE1 1 ? 6  
ATOM   1319 C CE2 . PHE B 2 48  ? 9.155   7.154   -4.472  1.000 46.347  0 377 PHE BBB CE2 1 ? 6  
ATOM   1320 C CZ  . PHE B 2 48  ? 10.305  6.469   -4.150  1.000 47.019  0 377 PHE BBB CZ  1 ? 6  
ATOM   1321 N N   . LYS B 2 49  ? 13.791  9.753   -8.582  1.000 43.674  0 378 LYS BBB N   1 ? 6  
ATOM   1322 C CA  . LYS B 2 49  ? 14.918  9.199   -9.372  1.000 45.419  0 378 LYS BBB CA  1 ? 6  
ATOM   1323 C C   . LYS B 2 49  ? 15.750  8.292   -8.468  1.000 46.127  0 378 LYS BBB C   1 ? 6  
ATOM   1324 O O   . LYS B 2 49  ? 16.334  8.799   -7.493  1.000 48.386  0 378 LYS BBB O   1 ? 6  
ATOM   1325 C CB  . LYS B 2 49  ? 15.762  10.319  -9.986  1.000 46.930  0 378 LYS BBB CB  1 ? 6  
ATOM   1326 C CG  . LYS B 2 49  ? 15.092  11.054  -11.141 1.000 47.493  0 378 LYS BBB CG  1 ? 6  
ATOM   1327 C CD  . LYS B 2 49  ? 16.043  11.856  -11.988 1.000 51.305  0 378 LYS BBB CD  1 ? 6  
ATOM   1328 C CE  . LYS B 2 49  ? 15.383  12.451  -13.214 1.000 54.051  0 378 LYS BBB CE  1 ? 6  
ATOM   1329 N NZ  . LYS B 2 49  ? 14.480  13.566  -12.838 1.000 57.681  0 378 LYS BBB NZ  1 ? 6  
ATOM   1330 N N   . CYS B 2 50  ? 15.789  6.997   -8.782  1.000 46.363  0 379 CYS BBB N   1 ? 6  
ATOM   1331 C CA  . CYS B 2 50  ? 16.609  5.999   -8.059  1.000 46.635  0 379 CYS BBB CA  1 ? 6  
ATOM   1332 C C   . CYS B 2 50  ? 17.827  5.636   -8.917  1.000 47.482  0 379 CYS BBB C   1 ? 6  
ATOM   1333 O O   . CYS B 2 50  ? 17.776  5.802   -10.152 1.000 49.660  0 379 CYS BBB O   1 ? 6  
ATOM   1334 C CB  . CYS B 2 50  ? 15.781  4.785   -7.668  1.000 47.982  0 379 CYS BBB CB  1 ? 6  
ATOM   1335 S SG  . CYS B 2 50  ? 14.394  5.195   -6.575  1.000 49.402  0 379 CYS BBB SG  1 ? 6  
ATOM   1336 N N   . TYR B 2 51  ? 18.910  5.248   -8.243  1.000 47.352  0 380 TYR BBB N   1 ? 6  
ATOM   1337 C CA  . TYR B 2 51  ? 20.220  4.837   -8.806  1.000 46.865  0 380 TYR BBB CA  1 ? 6  
ATOM   1338 C C   . TYR B 2 51  ? 20.619  3.537   -8.095  1.000 49.019  0 380 TYR BBB C   1 ? 6  
ATOM   1339 O O   . TYR B 2 51  ? 20.826  3.577   -6.853  1.000 52.691  0 380 TYR BBB O   1 ? 6  
ATOM   1340 C CB  . TYR B 2 51  ? 21.249  5.960   -8.622  1.000 45.965  0 380 TYR BBB CB  1 ? 6  
ATOM   1341 C CG  . TYR B 2 51  ? 20.795  7.334   -9.067  1.000 44.822  0 380 TYR BBB CG  1 ? 6  
ATOM   1342 C CD1 . TYR B 2 51  ? 19.919  8.095   -8.305  1.000 43.575  0 380 TYR BBB CD1 1 ? 6  
ATOM   1343 C CD2 . TYR B 2 51  ? 21.268  7.898   -10.239 1.000 44.132  0 380 TYR BBB CD2 1 ? 6  
ATOM   1344 C CE1 . TYR B 2 51  ? 19.494  9.349   -8.713  1.000 42.276  0 380 TYR BBB CE1 1 ? 6  
ATOM   1345 C CE2 . TYR B 2 51  ? 20.851  9.150   -10.666 1.000 42.817  0 380 TYR BBB CE2 1 ? 6  
ATOM   1346 C CZ  . TYR B 2 51  ? 19.973  9.886   -9.892  1.000 42.407  0 380 TYR BBB CZ  1 ? 6  
ATOM   1347 O OH  . TYR B 2 51  ? 19.554  11.120  -10.296 1.000 42.905  0 380 TYR BBB OH  1 ? 6  
ATOM   1348 N N   . GLY B 2 52  ? 20.604  2.414   -8.821  1.000 48.509  0 381 GLY BBB N   1 ? 6  
ATOM   1349 C CA  . GLY B 2 52  ? 21.056  1.098   -8.334  1.000 50.626  0 381 GLY BBB CA  1 ? 6  
ATOM   1350 C C   . GLY B 2 52  ? 20.005  0.343   -7.531  1.000 51.640  0 381 GLY BBB C   1 ? 6  
ATOM   1351 O O   . GLY B 2 52  ? 20.178  -0.877  -7.349  1.000 54.700  0 381 GLY BBB O   1 ? 6  
ATOM   1352 N N   . VAL B 2 53  ? 18.960  1.018   -7.052  1.000 52.173  0 382 VAL BBB N   1 ? 6  
ATOM   1353 C CA  . VAL B 2 53  ? 17.896  0.414   -6.190  1.000 53.730  0 382 VAL BBB CA  1 ? 6  
ATOM   1354 C C   . VAL B 2 53  ? 16.549  0.582   -6.900  1.000 54.029  0 382 VAL BBB C   1 ? 6  
ATOM   1355 O O   . VAL B 2 53  ? 16.290  1.685   -7.398  1.000 54.305  0 382 VAL BBB O   1 ? 6  
ATOM   1356 C CB  . VAL B 2 53  ? 17.886  1.043   -4.781  1.000 54.255  0 382 VAL BBB CB  1 ? 6  
ATOM   1357 C CG1 . VAL B 2 53  ? 17.762  2.557   -4.833  1.000 53.908  0 382 VAL BBB CG1 1 ? 6  
ATOM   1358 C CG2 . VAL B 2 53  ? 16.797  0.456   -3.883  1.000 55.926  0 382 VAL BBB CG2 1 ? 6  
ATOM   1359 N N   . SER B 2 54  ? 15.759  -0.489  -7.000  1.000 56.113  0 383 SER BBB N   1 ? 6  
ATOM   1360 C CA  . SER B 2 54  ? 14.373  -0.449  -7.534  1.000 56.923  0 383 SER BBB CA  1 ? 6  
ATOM   1361 C C   . SER B 2 54  ? 13.407  -0.309  -6.365  1.000 55.747  0 383 SER BBB C   1 ? 6  
ATOM   1362 O O   . SER B 2 54  ? 13.410  -1.149  -5.469  1.000 54.806  0 383 SER BBB O   1 ? 6  
ATOM   1363 C CB  . SER B 2 54  ? 14.056  -1.660  -8.364  1.000 59.067  0 383 SER BBB CB  1 ? 6  
ATOM   1364 O OG  . SER B 2 54  ? 14.518  -2.834  -7.721  1.000 61.393  0 383 SER BBB OG  1 ? 6  
ATOM   1365 N N   . PRO B 2 55  ? 12.563  0.749   -6.340  1.000 56.082  0 384 PRO BBB N   1 ? 6  
ATOM   1366 C CA  . PRO B 2 55  ? 11.576  0.933   -5.275  1.000 57.619  0 384 PRO BBB CA  1 ? 6  
ATOM   1367 C C   . PRO B 2 55  ? 10.691  -0.292  -5.004  1.000 59.161  0 384 PRO BBB C   1 ? 6  
ATOM   1368 O O   . PRO B 2 55  ? 10.376  -0.525  -3.855  1.000 61.624  0 384 PRO BBB O   1 ? 6  
ATOM   1369 C CB  . PRO B 2 55  ? 10.694  2.089   -5.767  1.000 57.052  0 384 PRO BBB CB  1 ? 6  
ATOM   1370 C CG  . PRO B 2 55  ? 11.592  2.861   -6.702  1.000 56.040  0 384 PRO BBB CG  1 ? 6  
ATOM   1371 C CD  . PRO B 2 55  ? 12.506  1.829   -7.335  1.000 56.250  0 384 PRO BBB CD  1 ? 6  
ATOM   1372 N N   . THR B 2 56  ? 10.324  -1.031  -6.055  1.000 59.978  0 385 THR BBB N   1 ? 6  
ATOM   1373 C CA  . THR B 2 56  ? 9.386   -2.186  -6.025  1.000 61.394  0 385 THR BBB CA  1 ? 6  
ATOM   1374 C C   . THR B 2 56  ? 9.935   -3.325  -5.155  1.000 61.966  0 385 THR BBB C   1 ? 6  
ATOM   1375 O O   . THR B 2 56  ? 9.111   -4.061  -4.574  1.000 65.654  0 385 THR BBB O   1 ? 6  
ATOM   1376 C CB  . THR B 2 56  ? 9.103   -2.669  -7.452  1.000 63.688  0 385 THR BBB CB  1 ? 6  
ATOM   1377 O OG1 . THR B 2 56  ? 8.222   -1.700  -8.018  1.000 65.970  0 385 THR BBB OG1 1 ? 6  
ATOM   1378 C CG2 . THR B 2 56  ? 8.499   -4.056  -7.526  1.000 66.104  0 385 THR BBB CG2 1 ? 6  
ATOM   1379 N N   . LYS B 2 57  ? 11.261  -3.486  -5.082  1.000 58.535  0 386 LYS BBB N   1 ? 6  
ATOM   1380 C CA  . LYS B 2 57  ? 11.917  -4.604  -4.351  1.000 56.860  0 386 LYS BBB CA  1 ? 6  
ATOM   1381 C C   . LYS B 2 57  ? 12.080  -4.243  -2.869  1.000 55.199  0 386 LYS BBB C   1 ? 6  
ATOM   1382 O O   . LYS B 2 57  ? 12.229  -5.181  -2.061  1.000 54.467  0 386 LYS BBB O   1 ? 6  
ATOM   1383 C CB  . LYS B 2 57  ? 13.267  -4.940  -4.990  1.000 56.766  0 386 LYS BBB CB  1 ? 6  
ATOM   1384 C CG  . LYS B 2 57  ? 13.180  -5.492  -6.405  1.000 57.531  0 386 LYS BBB CG  1 ? 6  
ATOM   1385 C CD  . LYS B 2 57  ? 14.529  -5.750  -7.046  1.000 57.936  0 386 LYS BBB CD  1 ? 6  
ATOM   1386 C CE  . LYS B 2 57  ? 15.233  -6.965  -6.478  1.000 59.329  0 386 LYS BBB CE  1 ? 6  
ATOM   1387 N NZ  . LYS B 2 57  ? 16.321  -7.430  -7.371  1.000 60.273  0 386 LYS BBB NZ  1 ? 6  
ATOM   1388 N N   . LEU B 2 58  ? 12.047  -2.947  -2.529  1.000 53.644  0 387 LEU BBB N   1 ? 6  
ATOM   1389 C CA  . LEU B 2 58  ? 12.318  -2.418  -1.160  1.000 54.145  0 387 LEU BBB CA  1 ? 6  
ATOM   1390 C C   . LEU B 2 58  ? 11.335  -3.019  -0.143  1.000 54.564  0 387 LEU BBB C   1 ? 6  
ATOM   1391 O O   . LEU B 2 58  ? 11.748  -3.229  1.013   1.000 54.416  0 387 LEU BBB O   1 ? 6  
ATOM   1392 C CB  . LEU B 2 58  ? 12.223  -0.889  -1.160  1.000 52.993  0 387 LEU BBB CB  1 ? 6  
ATOM   1393 C CG  . LEU B 2 58  ? 13.342  -0.130  -1.875  1.000 52.315  0 387 LEU BBB CG  1 ? 6  
ATOM   1394 C CD1 . LEU B 2 58  ? 13.073  1.364   -1.846  1.000 51.493  0 387 LEU BBB CD1 1 ? 6  
ATOM   1395 C CD2 . LEU B 2 58  ? 14.704  -0.430  -1.281  1.000 51.792  0 387 LEU BBB CD2 1 ? 6  
ATOM   1396 N N   . ASN B 2 59  ? 10.090  -3.284  -0.552  1.000 56.158  0 388 ASN BBB N   1 ? 6  
ATOM   1397 C CA  . ASN B 2 59  ? 9.014   -3.827  0.321   1.000 57.850  0 388 ASN BBB CA  1 ? 6  
ATOM   1398 C C   . ASN B 2 59  ? 9.324   -5.279  0.719   1.000 59.376  0 388 ASN BBB C   1 ? 6  
ATOM   1399 O O   . ASN B 2 59  ? 8.663   -5.776  1.653   1.000 60.064  0 388 ASN BBB O   1 ? 6  
ATOM   1400 C CB  . ASN B 2 59  ? 7.634   -3.698  -0.336  1.000 59.048  0 388 ASN BBB CB  1 ? 6  
ATOM   1401 C CG  . ASN B 2 59  ? 6.851   -2.481  0.123   1.000 59.989  0 388 ASN BBB CG  1 ? 6  
ATOM   1402 O OD1 . ASN B 2 59  ? 7.346   -1.654  0.882   1.000 59.212  0 388 ASN BBB OD1 1 ? 6  
ATOM   1403 N ND2 . ASN B 2 59  ? 5.606   -2.368  -0.309  1.000 62.440  0 388 ASN BBB ND2 1 ? 6  
ATOM   1404 N N   . ASP B 2 60  ? 10.286  -5.935  0.057   1.000 59.580  0 389 ASP BBB N   1 ? 6  
ATOM   1405 C CA  . ASP B 2 60  ? 10.701  -7.332  0.367   1.000 61.093  0 389 ASP BBB CA  1 ? 6  
ATOM   1406 C C   . ASP B 2 60  ? 12.170  -7.358  0.822   1.000 59.281  0 389 ASP BBB C   1 ? 6  
ATOM   1407 O O   . ASP B 2 60  ? 12.731  -8.464  0.927   1.000 60.278  0 389 ASP BBB O   1 ? 6  
ATOM   1408 C CB  . ASP B 2 60  ? 10.453  -8.249  -0.835  1.000 63.197  0 389 ASP BBB CB  1 ? 6  
ATOM   1409 C CG  . ASP B 2 60  ? 10.299  -9.724  -0.482  1.000 67.028  0 389 ASP BBB CG  1 ? 6  
ATOM   1410 O OD1 . ASP B 2 60  ? 9.688   -10.025 0.575   1.000 69.543  0 389 ASP BBB OD1 1 ? 6  
ATOM   1411 O OD2 . ASP B 2 60  ? 10.796  -10.567 -1.262  1.000 68.622  0 389 ASP BBB OD2 1 ? 6  
ATOM   1412 N N   . LEU B 2 61  ? 12.762  -6.197  1.117   1.000 56.644  0 390 LEU BBB N   1 ? 6  
ATOM   1413 C CA  . LEU B 2 61  ? 14.209  -6.067  1.427   1.000 56.013  0 390 LEU BBB CA  1 ? 6  
ATOM   1414 C C   . LEU B 2 61  ? 14.398  -5.521  2.848   1.000 56.008  0 390 LEU BBB C   1 ? 6  
ATOM   1415 O O   . LEU B 2 61  ? 13.503  -4.806  3.348   1.000 54.245  0 390 LEU BBB O   1 ? 6  
ATOM   1416 C CB  . LEU B 2 61  ? 14.866  -5.156  0.385   1.000 55.195  0 390 LEU BBB CB  1 ? 6  
ATOM   1417 C CG  . LEU B 2 61  ? 15.086  -5.774  -0.997  1.000 55.541  0 390 LEU BBB CG  1 ? 6  
ATOM   1418 C CD1 . LEU B 2 61  ? 15.538  -4.716  -1.994  1.000 53.865  0 390 LEU BBB CD1 1 ? 6  
ATOM   1419 C CD2 . LEU B 2 61  ? 16.092  -6.916  -0.943  1.000 57.000  0 390 LEU BBB CD2 1 ? 6  
ATOM   1420 N N   . CYS B 2 62  ? 15.536  -5.863  3.459   1.000 56.461  0 391 CYS BBB N   1 ? 6  
ATOM   1421 C CA  . CYS B 2 62  ? 15.941  -5.461  4.830   1.000 57.222  0 391 CYS BBB CA  1 ? 6  
ATOM   1422 C C   . CYS B 2 62  ? 17.286  -4.730  4.772   1.000 56.092  0 391 CYS BBB C   1 ? 6  
ATOM   1423 O O   . CYS B 2 62  ? 18.168  -5.179  4.025   1.000 56.928  0 391 CYS BBB O   1 ? 6  
ATOM   1424 C CB  . CYS B 2 62  ? 16.049  -6.673  5.747   1.000 59.282  0 391 CYS BBB CB  1 ? 6  
ATOM   1425 S SG  . CYS B 2 62  ? 14.448  -7.411  6.159   1.000 60.671  0 391 CYS BBB SG  1 ? 6  
ATOM   1426 N N   . PHE B 2 63  ? 17.426  -3.651  5.545   1.000 54.788  0 392 PHE BBB N   1 ? 6  
ATOM   1427 C CA  . PHE B 2 63  ? 18.655  -2.826  5.643   1.000 53.936  0 392 PHE BBB CA  1 ? 6  
ATOM   1428 C C   . PHE B 2 63  ? 19.016  -2.615  7.115   1.000 54.152  0 392 PHE BBB C   1 ? 6  
ATOM   1429 O O   . PHE B 2 63  ? 18.119  -2.636  7.977   1.000 54.622  0 392 PHE BBB O   1 ? 6  
ATOM   1430 C CB  . PHE B 2 63  ? 18.450  -1.499  4.912   1.000 52.887  0 392 PHE BBB CB  1 ? 6  
ATOM   1431 C CG  . PHE B 2 63  ? 18.181  -1.656  3.441   1.000 52.011  0 392 PHE BBB CG  1 ? 6  
ATOM   1432 C CD1 . PHE B 2 63  ? 19.222  -1.875  2.551   1.000 52.298  0 392 PHE BBB CD1 1 ? 6  
ATOM   1433 C CD2 . PHE B 2 63  ? 16.886  -1.610  2.950   1.000 51.347  0 392 PHE BBB CD2 1 ? 6  
ATOM   1434 C CE1 . PHE B 2 63  ? 18.974  -2.029  1.195   1.000 51.747  0 392 PHE BBB CE1 1 ? 6  
ATOM   1435 C CE2 . PHE B 2 63  ? 16.642  -1.763  1.593   1.000 51.925  0 392 PHE BBB CE2 1 ? 6  
ATOM   1436 C CZ  . PHE B 2 63  ? 17.685  -1.977  0.720   1.000 51.025  0 392 PHE BBB CZ  1 ? 6  
ATOM   1437 N N   . THR B 2 64  ? 20.308  -2.436  7.382   1.000 53.645  0 393 THR BBB N   1 ? 6  
ATOM   1438 C CA  . THR B 2 64  ? 20.864  -2.074  8.709   1.000 54.654  0 393 THR BBB CA  1 ? 6  
ATOM   1439 C C   . THR B 2 64  ? 20.286  -0.707  9.098   1.000 53.173  0 393 THR BBB C   1 ? 6  
ATOM   1440 O O   . THR B 2 64  ? 19.776  -0.566  10.223  1.000 55.120  0 393 THR BBB O   1 ? 6  
ATOM   1441 C CB  . THR B 2 64  ? 22.400  -2.067  8.663   1.000 55.172  0 393 THR BBB CB  1 ? 6  
ATOM   1442 O OG1 . THR B 2 64  ? 22.826  -3.194  7.892   1.000 55.931  0 393 THR BBB OG1 1 ? 6  
ATOM   1443 C CG2 . THR B 2 64  ? 23.036  -2.084  10.035  1.000 55.740  0 393 THR BBB CG2 1 ? 6  
ATOM   1444 N N   . ASN B 2 65  ? 20.350  0.250   8.172   1.000 51.879  0 394 ASN BBB N   1 ? 6  
ATOM   1445 C CA  . ASN B 2 65  ? 19.877  1.646   8.351   1.000 50.134  0 394 ASN BBB CA  1 ? 6  
ATOM   1446 C C   . ASN B 2 65  ? 19.392  2.205   7.013   1.000 47.878  0 394 ASN BBB C   1 ? 6  
ATOM   1447 O O   . ASN B 2 65  ? 19.985  1.871   5.974   1.000 46.515  0 394 ASN BBB O   1 ? 6  
ATOM   1448 C CB  . ASN B 2 65  ? 20.984  2.561   8.873   1.000 50.532  0 394 ASN BBB CB  1 ? 6  
ATOM   1449 C CG  . ASN B 2 65  ? 21.346  2.266   10.308  1.000 51.361  0 394 ASN BBB CG  1 ? 6  
ATOM   1450 O OD1 . ASN B 2 65  ? 20.518  2.439   11.194  1.000 50.316  0 394 ASN BBB OD1 1 ? 6  
ATOM   1451 N ND2 . ASN B 2 65  ? 22.573  1.823   10.538  1.000 52.368  0 394 ASN BBB ND2 1 ? 6  
ATOM   1452 N N   . VAL B 2 66  ? 18.357  3.038   7.068   1.000 46.689  0 395 VAL BBB N   1 ? 6  
ATOM   1453 C CA  . VAL B 2 66  ? 17.939  3.949   5.967   1.000 45.850  0 395 VAL BBB CA  1 ? 6  
ATOM   1454 C C   . VAL B 2 66  ? 18.150  5.379   6.464   1.000 45.479  0 395 VAL BBB C   1 ? 6  
ATOM   1455 O O   . VAL B 2 66  ? 17.840  5.647   7.639   1.000 46.247  0 395 VAL BBB O   1 ? 6  
ATOM   1456 C CB  . VAL B 2 66  ? 16.480  3.696   5.545   1.000 45.185  0 395 VAL BBB CB  1 ? 6  
ATOM   1457 C CG1 . VAL B 2 66  ? 16.016  4.703   4.505   1.000 44.550  0 395 VAL BBB CG1 1 ? 6  
ATOM   1458 C CG2 . VAL B 2 66  ? 16.284  2.269   5.056   1.000 45.765  0 395 VAL BBB CG2 1 ? 6  
ATOM   1459 N N   . TYR B 2 67  ? 18.680  6.250   5.605   1.000 45.667  0 396 TYR BBB N   1 ? 6  
ATOM   1460 C CA  . TYR B 2 67  ? 18.909  7.687   5.898   1.000 45.416  0 396 TYR BBB CA  1 ? 6  
ATOM   1461 C C   . TYR B 2 67  ? 18.017  8.529   4.987   1.000 43.642  0 396 TYR BBB C   1 ? 6  
ATOM   1462 O O   . TYR B 2 67  ? 18.059  8.344   3.756   1.000 43.701  0 396 TYR BBB O   1 ? 6  
ATOM   1463 C CB  . TYR B 2 67  ? 20.383  8.054   5.725   1.000 45.462  0 396 TYR BBB CB  1 ? 6  
ATOM   1464 C CG  . TYR B 2 67  ? 21.313  7.328   6.663   1.000 46.975  0 396 TYR BBB CG  1 ? 6  
ATOM   1465 C CD1 . TYR B 2 67  ? 21.551  7.791   7.949   1.000 47.959  0 396 TYR BBB CD1 1 ? 6  
ATOM   1466 C CD2 . TYR B 2 67  ? 21.941  6.155   6.267   1.000 47.746  0 396 TYR BBB CD2 1 ? 6  
ATOM   1467 C CE1 . TYR B 2 67  ? 22.393  7.107   8.813   1.000 48.953  0 396 TYR BBB CE1 1 ? 6  
ATOM   1468 C CE2 . TYR B 2 67  ? 22.780  5.458   7.119   1.000 48.824  0 396 TYR BBB CE2 1 ? 6  
ATOM   1469 C CZ  . TYR B 2 67  ? 23.010  5.938   8.396   1.000 49.785  0 396 TYR BBB CZ  1 ? 6  
ATOM   1470 O OH  . TYR B 2 67  ? 23.851  5.254   9.225   1.000 51.630  0 396 TYR BBB OH  1 ? 6  
ATOM   1471 N N   . ALA B 2 68  ? 17.226  9.412   5.595   1.000 43.005  0 397 ALA BBB N   1 ? 6  
ATOM   1472 C CA  . ALA B 2 68  ? 16.384  10.412  4.909   1.000 43.715  0 397 ALA BBB CA  1 ? 6  
ATOM   1473 C C   . ALA B 2 68  ? 16.998  11.794  5.142   1.000 43.428  0 397 ALA BBB C   1 ? 6  
ATOM   1474 O O   . ALA B 2 68  ? 16.930  12.284  6.284   1.000 45.206  0 397 ALA BBB O   1 ? 6  
ATOM   1475 C CB  . ALA B 2 68  ? 14.960  10.332  5.407   1.000 43.924  0 397 ALA BBB CB  1 ? 6  
ATOM   1476 N N   . ASP B 2 69  ? 17.607  12.369  4.101   1.000 41.985  0 398 ASP BBB N   1 ? 6  
ATOM   1477 C CA  . ASP B 2 69  ? 18.056  13.784  4.076   1.000 41.421  0 398 ASP BBB CA  1 ? 6  
ATOM   1478 C C   . ASP B 2 69  ? 16.929  14.622  3.465   1.000 41.567  0 398 ASP BBB C   1 ? 6  
ATOM   1479 O O   . ASP B 2 69  ? 16.438  14.241  2.392   1.000 41.933  0 398 ASP BBB O   1 ? 6  
ATOM   1480 C CB  . ASP B 2 69  ? 19.367  13.940  3.304   1.000 41.119  0 398 ASP BBB CB  1 ? 6  
ATOM   1481 C CG  . ASP B 2 69  ? 20.483  13.055  3.826   1.000 41.955  0 398 ASP BBB CG  1 ? 6  
ATOM   1482 O OD1 . ASP B 2 69  ? 20.408  12.657  5.009   1.000 43.390  0 398 ASP BBB OD1 1 ? 6  
ATOM   1483 O OD2 . ASP B 2 69  ? 21.416  12.766  3.048   1.000 40.610  0 398 ASP BBB OD2 1 ? 6  
ATOM   1484 N N   . SER B 2 70  ? 16.530  15.703  4.136   1.000 41.068  0 399 SER BBB N   1 ? 6  
ATOM   1485 C CA  . SER B 2 70  ? 15.418  16.594  3.720   1.000 40.408  0 399 SER BBB CA  1 ? 6  
ATOM   1486 C C   . SER B 2 70  ? 15.891  18.050  3.728   1.000 39.808  0 399 SER BBB C   1 ? 6  
ATOM   1487 O O   . SER B 2 70  ? 16.708  18.406  4.590   1.000 40.655  0 399 SER BBB O   1 ? 6  
ATOM   1488 C CB  . SER B 2 70  ? 14.208  16.396  4.597   1.000 40.668  0 399 SER BBB CB  1 ? 6  
ATOM   1489 O OG  . SER B 2 70  ? 14.554  16.517  5.967   1.000 40.894  0 399 SER BBB OG  1 ? 6  
ATOM   1490 N N   . PHE B 2 71  ? 15.384  18.847  2.787   1.000 39.701  0 400 PHE BBB N   1 ? 6  
ATOM   1491 C CA  . PHE B 2 71  ? 15.668  20.297  2.633   1.000 39.154  0 400 PHE BBB CA  1 ? 6  
ATOM   1492 C C   . PHE B 2 71  ? 14.790  20.869  1.514   1.000 38.459  0 400 PHE BBB C   1 ? 6  
ATOM   1493 O O   . PHE B 2 71  ? 14.143  20.087  0.791   1.000 36.335  0 400 PHE BBB O   1 ? 6  
ATOM   1494 C CB  . PHE B 2 71  ? 17.148  20.530  2.321   1.000 39.470  0 400 PHE BBB CB  1 ? 6  
ATOM   1495 C CG  . PHE B 2 71  ? 17.679  19.701  1.179   1.000 39.646  0 400 PHE BBB CG  1 ? 6  
ATOM   1496 C CD1 . PHE B 2 71  ? 17.430  20.061  -0.136  1.000 39.877  0 400 PHE BBB CD1 1 ? 6  
ATOM   1497 C CD2 . PHE B 2 71  ? 18.412  18.550  1.422   1.000 40.261  0 400 PHE BBB CD2 1 ? 6  
ATOM   1498 C CE1 . PHE B 2 71  ? 17.907  19.286  -1.182  1.000 40.745  0 400 PHE BBB CE1 1 ? 6  
ATOM   1499 C CE2 . PHE B 2 71  ? 18.884  17.773  0.379   1.000 40.222  0 400 PHE BBB CE2 1 ? 6  
ATOM   1500 C CZ  . PHE B 2 71  ? 18.637  18.146  -0.922  1.000 41.766  0 400 PHE BBB CZ  1 ? 6  
ATOM   1501 N N   . VAL B 2 72  ? 14.787  22.198  1.385   1.000 38.603  0 401 VAL BBB N   1 ? 6  
ATOM   1502 C CA  . VAL B 2 72  ? 14.084  22.948  0.305   1.000 38.790  0 401 VAL BBB CA  1 ? 6  
ATOM   1503 C C   . VAL B 2 72  ? 15.129  23.636  -0.588  1.000 38.192  0 401 VAL BBB C   1 ? 6  
ATOM   1504 O O   . VAL B 2 72  ? 16.070  24.247  -0.056  1.000 37.415  0 401 VAL BBB O   1 ? 6  
ATOM   1505 C CB  . VAL B 2 72  ? 13.077  23.950  0.899   1.000 39.417  0 401 VAL BBB CB  1 ? 6  
ATOM   1506 C CG1 . VAL B 2 72  ? 12.753  25.088  -0.052  1.000 40.003  0 401 VAL BBB CG1 1 ? 6  
ATOM   1507 C CG2 . VAL B 2 72  ? 11.799  23.257  1.331   1.000 40.990  0 401 VAL BBB CG2 1 ? 6  
ATOM   1508 N N   . ILE B 2 73  ? 14.947  23.526  -1.903  1.000 38.724  0 402 ILE BBB N   1 ? 6  
ATOM   1509 C CA  . ILE B 2 73  ? 15.693  24.284  -2.952  1.000 39.489  0 402 ILE BBB CA  1 ? 6  
ATOM   1510 C C   . ILE B 2 73  ? 14.658  24.799  -3.958  1.000 39.659  0 402 ILE BBB C   1 ? 6  
ATOM   1511 O O   . ILE B 2 73  ? 13.473  24.454  -3.784  1.000 42.485  0 402 ILE BBB O   1 ? 6  
ATOM   1512 C CB  . ILE B 2 73  ? 16.765  23.394  -3.611  1.000 39.709  0 402 ILE BBB CB  1 ? 6  
ATOM   1513 C CG1 . ILE B 2 73  ? 16.171  22.091  -4.155  1.000 39.784  0 402 ILE BBB CG1 1 ? 6  
ATOM   1514 C CG2 . ILE B 2 73  ? 17.910  23.136  -2.637  1.000 40.189  0 402 ILE BBB CG2 1 ? 6  
ATOM   1515 C CD1 . ILE B 2 73  ? 17.160  21.221  -4.890  1.000 39.380  0 402 ILE BBB CD1 1 ? 6  
ATOM   1516 N N   . ARG B 2 74  ? 15.061  25.609  -4.938  1.000 41.029  0 403 ARG BBB N   1 ? 7  
ATOM   1517 C CA  A ARG B 2 74  ? 14.149  26.061  -6.024  0.500 42.679  0 403 ARG BBB CA  1 ? 7  
ATOM   1518 C CA  B ARG B 2 74  ? 14.149  26.061  -6.024  0.500 42.515  0 403 ARG BBB CA  1 ? 7  
ATOM   1519 C C   . ARG B 2 74  ? 14.199  25.033  -7.164  1.000 41.454  0 403 ARG BBB C   1 ? 7  
ATOM   1520 O O   . ARG B 2 74  ? 15.181  24.267  -7.228  1.000 40.036  0 403 ARG BBB O   1 ? 7  
ATOM   1521 C CB  A ARG B 2 74  ? 14.461  27.499  -6.460  0.500 45.090  0 403 ARG BBB CB  1 ? 7  
ATOM   1522 C CB  B ARG B 2 74  ? 14.462  27.496  -6.466  0.500 44.700  0 403 ARG BBB CB  1 ? 7  
ATOM   1523 C CG  A ARG B 2 74  ? 15.814  27.724  -7.119  0.500 45.279  0 403 ARG BBB CG  1 ? 7  
ATOM   1524 C CG  B ARG B 2 74  ? 15.823  27.712  -7.112  0.500 44.647  0 403 ARG BBB CG  1 ? 7  
ATOM   1525 C CD  A ARG B 2 74  ? 16.020  29.205  -7.390  0.500 48.319  0 403 ARG BBB CD  1 ? 7  
ATOM   1526 C CD  B ARG B 2 74  ? 15.875  29.029  -7.861  0.500 47.441  0 403 ARG BBB CD  1 ? 7  
ATOM   1527 N NE  A ARG B 2 74  ? 17.160  29.481  -8.254  0.500 49.608  0 403 ARG BBB NE  1 ? 7  
ATOM   1528 N NE  B ARG B 2 74  ? 17.113  29.769  -7.654  0.500 48.785  0 403 ARG BBB NE  1 ? 7  
ATOM   1529 C CZ  A ARG B 2 74  ? 17.130  29.461  -9.584  0.500 50.860  0 403 ARG BBB CZ  1 ? 7  
ATOM   1530 C CZ  B ARG B 2 74  ? 17.222  30.874  -6.921  0.500 50.692  0 403 ARG BBB CZ  1 ? 7  
ATOM   1531 N NH1 A ARG B 2 74  ? 16.009  29.174  -10.223 0.500 51.018  0 403 ARG BBB NH1 1 ? 7  
ATOM   1532 N NH1 B ARG B 2 74  ? 16.158  31.386  -6.325  0.500 52.004  0 403 ARG BBB NH1 1 ? 7  
ATOM   1533 N NH2 A ARG B 2 74  ? 18.224  29.734  -10.272 0.500 52.114  0 403 ARG BBB NH2 1 ? 7  
ATOM   1534 N NH2 B ARG B 2 74  ? 18.397  31.460  -6.779  0.500 51.417  0 403 ARG BBB NH2 1 ? 7  
ATOM   1535 N N   . GLY B 2 75  ? 13.152  25.005  -7.994  1.000 42.191  0 404 GLY BBB N   1 ? 7  
ATOM   1536 C CA  . GLY B 2 75  ? 12.924  23.991  -9.043  1.000 41.892  0 404 GLY BBB CA  1 ? 7  
ATOM   1537 C C   . GLY B 2 75  ? 14.131  23.764  -9.938  1.000 40.600  0 404 GLY BBB C   1 ? 7  
ATOM   1538 O O   . GLY B 2 75  ? 14.467  22.590  -10.170 1.000 39.080  0 404 GLY BBB O   1 ? 7  
ATOM   1539 N N   . ASP B 2 76  ? 14.759  24.840  -10.421 1.000 42.285  0 405 ASP BBB N   1 ? 7  
ATOM   1540 C CA  . ASP B 2 76  ? 15.902  24.805  -11.378 1.000 44.349  0 405 ASP BBB CA  1 ? 7  
ATOM   1541 C C   . ASP B 2 76  ? 17.086  24.022  -10.794 1.000 42.566  0 405 ASP BBB C   1 ? 7  
ATOM   1542 O O   . ASP B 2 76  ? 17.917  23.557  -11.593 1.000 42.967  0 405 ASP BBB O   1 ? 7  
ATOM   1543 C CB  . ASP B 2 76  ? 16.357  26.216  -11.770 1.000 46.999  0 405 ASP BBB CB  1 ? 7  
ATOM   1544 C CG  . ASP B 2 76  ? 15.464  26.909  -12.789 1.000 50.457  0 405 ASP BBB CG  1 ? 7  
ATOM   1545 O OD1 . ASP B 2 76  ? 14.659  26.214  -13.442 1.000 51.761  0 405 ASP BBB OD1 1 ? 7  
ATOM   1546 O OD2 . ASP B 2 76  ? 15.590  28.140  -12.934 1.000 53.941  0 405 ASP BBB OD2 1 ? 7  
ATOM   1547 N N   . GLU B 2 77  ? 17.152  23.871  -9.466  1.000 41.379  0 406 GLU BBB N   1 ? 7  
ATOM   1548 C CA  . GLU B 2 77  ? 18.312  23.281  -8.746  1.000 40.309  0 406 GLU BBB CA  1 ? 7  
ATOM   1549 C C   . GLU B 2 77  ? 18.076  21.795  -8.436  1.000 39.665  0 406 GLU BBB C   1 ? 7  
ATOM   1550 O O   . GLU B 2 77  ? 19.028  21.150  -7.959  1.000 39.928  0 406 GLU BBB O   1 ? 7  
ATOM   1551 C CB  . GLU B 2 77  ? 18.578  24.063  -7.458  1.000 39.831  0 406 GLU BBB CB  1 ? 7  
ATOM   1552 C CG  . GLU B 2 77  ? 19.108  25.470  -7.690  1.000 40.880  0 406 GLU BBB CG  1 ? 7  
ATOM   1553 C CD  . GLU B 2 77  ? 19.122  26.367  -6.461  1.000 40.822  0 406 GLU BBB CD  1 ? 7  
ATOM   1554 O OE1 . GLU B 2 77  ? 18.409  26.058  -5.488  1.000 39.774  0 406 GLU BBB OE1 1 ? 7  
ATOM   1555 O OE2 . GLU B 2 77  ? 19.840  27.377  -6.482  1.000 41.337  0 406 GLU BBB OE2 1 ? 7  
ATOM   1556 N N   . VAL B 2 78  ? 16.880  21.257  -8.692  1.000 39.750  0 407 VAL BBB N   1 ? 7  
ATOM   1557 C CA  . VAL B 2 78  ? 16.539  19.837  -8.369  1.000 39.737  0 407 VAL BBB CA  1 ? 7  
ATOM   1558 C C   . VAL B 2 78  ? 17.440  18.897  -9.178  1.000 39.517  0 407 VAL BBB C   1 ? 7  
ATOM   1559 O O   . VAL B 2 78  ? 17.735  17.807  -8.678  1.000 39.159  0 407 VAL BBB O   1 ? 7  
ATOM   1560 C CB  . VAL B 2 78  ? 15.044  19.527  -8.588  1.000 40.534  0 407 VAL BBB CB  1 ? 7  
ATOM   1561 C CG1 . VAL B 2 78  ? 14.748  18.033  -8.515  1.000 39.766  0 407 VAL BBB CG1 1 ? 7  
ATOM   1562 C CG2 . VAL B 2 78  ? 14.183  20.289  -7.592  1.000 40.915  0 407 VAL BBB CG2 1 ? 7  
ATOM   1563 N N   . ARG B 2 79  ? 17.883  19.303  -10.368 1.000 42.930  0 408 ARG BBB N   1 ? 7  
ATOM   1564 C CA  . ARG B 2 79  ? 18.781  18.477  -11.223 1.000 45.292  0 408 ARG BBB CA  1 ? 7  
ATOM   1565 C C   . ARG B 2 79  ? 20.182  18.395  -10.590 1.000 43.206  0 408 ARG BBB C   1 ? 7  
ATOM   1566 O O   . ARG B 2 79  ? 20.907  17.450  -10.934 1.000 44.412  0 408 ARG BBB O   1 ? 7  
ATOM   1567 C CB  . ARG B 2 79  ? 18.797  19.004  -12.663 1.000 50.017  0 408 ARG BBB CB  1 ? 7  
ATOM   1568 C CG  . ARG B 2 79  ? 19.433  20.375  -12.843 1.000 55.609  0 408 ARG BBB CG  1 ? 7  
ATOM   1569 C CD  . ARG B 2 79  ? 20.880  20.310  -13.299 1.000 61.359  0 408 ARG BBB CD  1 ? 7  
ATOM   1570 N NE  . ARG B 2 79  ? 21.573  21.585  -13.134 1.000 65.781  0 408 ARG BBB NE  1 ? 7  
ATOM   1571 C CZ  . ARG B 2 79  ? 22.891  21.736  -13.002 1.000 68.327  0 408 ARG BBB CZ  1 ? 7  
ATOM   1572 N NH1 . ARG B 2 79  ? 23.697  20.685  -13.005 1.000 68.939  0 408 ARG BBB NH1 1 ? 7  
ATOM   1573 N NH2 . ARG B 2 79  ? 23.399  22.949  -12.854 1.000 70.568  0 408 ARG BBB NH2 1 ? 7  
ATOM   1574 N N   . GLN B 2 80  ? 20.544  19.324  -9.692  1.000 41.122  0 409 GLN BBB N   1 ? 7  
ATOM   1575 C CA  . GLN B 2 80  ? 21.859  19.345  -8.988  1.000 39.706  0 409 GLN BBB CA  1 ? 7  
ATOM   1576 C C   . GLN B 2 80  ? 21.906  18.260  -7.906  1.000 38.486  0 409 GLN BBB C   1 ? 7  
ATOM   1577 O O   . GLN B 2 80  ? 23.019  17.898  -7.498  1.000 38.549  0 409 GLN BBB O   1 ? 7  
ATOM   1578 C CB  . GLN B 2 80  ? 22.150  20.698  -8.338  1.000 39.560  0 409 GLN BBB CB  1 ? 7  
ATOM   1579 C CG  . GLN B 2 80  ? 22.548  21.784  -9.323  1.000 41.377  0 409 GLN BBB CG  1 ? 7  
ATOM   1580 C CD  . GLN B 2 80  ? 22.965  23.053  -8.621  1.000 42.726  0 409 GLN BBB CD  1 ? 7  
ATOM   1581 O OE1 . GLN B 2 80  ? 23.756  23.038  -7.680  1.000 44.412  0 409 GLN BBB OE1 1 ? 7  
ATOM   1582 N NE2 . GLN B 2 80  ? 22.445  24.178  -9.082  1.000 43.954  0 409 GLN BBB NE2 1 ? 7  
ATOM   1583 N N   . ILE B 2 81  ? 20.750  17.784  -7.433  1.000 38.784  0 410 ILE BBB N   1 ? 7  
ATOM   1584 C CA  . ILE B 2 81  ? 20.657  16.703  -6.406  1.000 37.979  0 410 ILE BBB CA  1 ? 7  
ATOM   1585 C C   . ILE B 2 81  ? 20.706  15.363  -7.143  1.000 38.500  0 410 ILE BBB C   1 ? 7  
ATOM   1586 O O   . ILE B 2 81  ? 19.685  14.650  -7.183  1.000 38.626  0 410 ILE BBB O   1 ? 7  
ATOM   1587 C CB  . ILE B 2 81  ? 19.412  16.856  -5.509  1.000 37.666  0 410 ILE BBB CB  1 ? 7  
ATOM   1588 C CG1 . ILE B 2 81  ? 19.237  18.295  -5.012  1.000 37.782  0 410 ILE BBB CG1 1 ? 7  
ATOM   1589 C CG2 . ILE B 2 81  ? 19.460  15.867  -4.356  1.000 38.159  0 410 ILE BBB CG2 1 ? 7  
ATOM   1590 C CD1 . ILE B 2 81  ? 20.447  18.873  -4.300  1.000 37.496  0 410 ILE BBB CD1 1 ? 7  
ATOM   1591 N N   . ALA B 2 82  ? 21.876  15.051  -7.701  1.000 39.303  0 411 ALA BBB N   1 ? 7  
ATOM   1592 C CA  . ALA B 2 82  ? 22.154  13.835  -8.497  1.000 41.161  0 411 ALA BBB CA  1 ? 7  
ATOM   1593 C C   . ALA B 2 82  ? 23.667  13.644  -8.577  1.000 41.681  0 411 ALA BBB C   1 ? 7  
ATOM   1594 O O   . ALA B 2 82  ? 24.417  14.598  -8.387  1.000 40.931  0 411 ALA BBB O   1 ? 7  
ATOM   1595 C CB  . ALA B 2 82  ? 21.530  13.973  -9.865  1.000 40.811  0 411 ALA BBB CB  1 ? 7  
ATOM   1596 N N   . PRO B 2 83  ? 24.165  12.420  -8.861  1.000 43.963  0 412 PRO BBB N   1 ? 7  
ATOM   1597 C CA  . PRO B 2 83  ? 25.606  12.186  -8.915  1.000 45.678  0 412 PRO BBB CA  1 ? 7  
ATOM   1598 C C   . PRO B 2 83  ? 26.295  13.010  -10.016 1.000 45.905  0 412 PRO BBB C   1 ? 7  
ATOM   1599 O O   . PRO B 2 83  ? 25.730  13.141  -11.076 1.000 47.777  0 412 PRO BBB O   1 ? 7  
ATOM   1600 C CB  . PRO B 2 83  ? 25.755  10.684  -9.206  1.000 47.771  0 412 PRO BBB CB  1 ? 7  
ATOM   1601 C CG  . PRO B 2 83  ? 24.368  10.076  -9.049  1.000 47.465  0 412 PRO BBB CG  1 ? 7  
ATOM   1602 C CD  . PRO B 2 83  ? 23.377  11.213  -9.157  1.000 45.642  0 412 PRO BBB CD  1 ? 7  
ATOM   1603 N N   . GLY B 2 84  ? 27.483  13.546  -9.726  1.000 46.104  0 413 GLY BBB N   1 ? 7  
ATOM   1604 C CA  . GLY B 2 84  ? 28.375  14.191  -10.712 1.000 46.728  0 413 GLY BBB CA  1 ? 7  
ATOM   1605 C C   . GLY B 2 84  ? 27.871  15.546  -11.179 1.000 46.023  0 413 GLY BBB C   1 ? 7  
ATOM   1606 O O   . GLY B 2 84  ? 28.283  15.966  -12.271 1.000 47.888  0 413 GLY BBB O   1 ? 7  
ATOM   1607 N N   . GLN B 2 85  ? 27.023  16.217  -10.394 1.000 44.161  0 414 GLN BBB N   1 ? 7  
ATOM   1608 C CA  . GLN B 2 85  ? 26.486  17.565  -10.726 1.000 44.617  0 414 GLN BBB CA  1 ? 7  
ATOM   1609 C C   . GLN B 2 85  ? 27.339  18.651  -10.068 1.000 45.749  0 414 GLN BBB C   1 ? 7  
ATOM   1610 O O   . GLN B 2 85  ? 28.017  18.344  -9.070  1.000 45.918  0 414 GLN BBB O   1 ? 7  
ATOM   1611 C CB  . GLN B 2 85  ? 25.038  17.691  -10.264 1.000 43.980  0 414 GLN BBB CB  1 ? 7  
ATOM   1612 C CG  . GLN B 2 85  ? 24.114  16.678  -10.916 1.000 45.170  0 414 GLN BBB CG  1 ? 7  
ATOM   1613 C CD  . GLN B 2 85  ? 24.092  16.841  -12.414 1.000 46.745  0 414 GLN BBB CD  1 ? 7  
ATOM   1614 O OE1 . GLN B 2 85  ? 23.812  17.917  -12.940 1.000 48.296  0 414 GLN BBB OE1 1 ? 7  
ATOM   1615 N NE2 . GLN B 2 85  ? 24.396  15.762  -13.112 1.000 48.290  0 414 GLN BBB NE2 1 ? 7  
ATOM   1616 N N   . THR B 2 86  ? 27.297  19.868  -10.620 1.000 47.559  0 415 THR BBB N   1 ? 7  
ATOM   1617 C CA  . THR B 2 86  ? 27.953  21.090  -10.077 1.000 49.008  0 415 THR BBB CA  1 ? 7  
ATOM   1618 C C   . THR B 2 86  ? 26.925  22.228  -10.072 1.000 48.237  0 415 THR BBB C   1 ? 7  
ATOM   1619 O O   . THR B 2 86  ? 25.849  22.039  -10.671 1.000 47.742  0 415 THR BBB O   1 ? 7  
ATOM   1620 C CB  . THR B 2 86  ? 29.229  21.434  -10.860 1.000 51.774  0 415 THR BBB CB  1 ? 7  
ATOM   1621 O OG1 . THR B 2 86  ? 28.861  21.809  -12.188 1.000 53.083  0 415 THR BBB OG1 1 ? 7  
ATOM   1622 C CG2 . THR B 2 86  ? 30.215  20.287  -10.905 1.000 51.912  0 415 THR BBB CG2 1 ? 7  
ATOM   1623 N N   . GLY B 2 87  ? 27.261  23.356  -9.433  1.000 48.421  0 416 GLY BBB N   1 ? 7  
ATOM   1624 C CA  . GLY B 2 87  ? 26.353  24.488  -9.154  1.000 47.814  0 416 GLY BBB CA  1 ? 7  
ATOM   1625 C C   . GLY B 2 87  ? 26.383  24.850  -7.681  1.000 46.963  0 416 GLY BBB C   1 ? 7  
ATOM   1626 O O   . GLY B 2 87  ? 27.005  24.095  -6.920  1.000 44.230  0 416 GLY BBB O   1 ? 7  
ATOM   1627 N N   . LYS B 2 88  ? 25.731  25.951  -7.285  1.000 48.727  0 417 LYS BBB N   1 ? 7  
ATOM   1628 C CA  . LYS B 2 88  ? 25.766  26.493  -5.898  1.000 49.325  0 417 LYS BBB CA  1 ? 7  
ATOM   1629 C C   . LYS B 2 88  ? 25.359  25.406  -4.899  1.000 46.906  0 417 LYS BBB C   1 ? 7  
ATOM   1630 O O   . LYS B 2 88  ? 25.968  25.359  -3.818  1.000 46.868  0 417 LYS BBB O   1 ? 7  
ATOM   1631 C CB  . LYS B 2 88  ? 24.855  27.714  -5.738  1.000 51.367  0 417 LYS BBB CB  1 ? 7  
ATOM   1632 C CG  . LYS B 2 88  ? 25.335  28.981  -6.429  1.000 56.532  0 417 LYS BBB CG  1 ? 7  
ATOM   1633 C CD  . LYS B 2 88  ? 26.654  29.528  -5.909  1.000 60.286  0 417 LYS BBB CD  1 ? 7  
ATOM   1634 C CE  . LYS B 2 88  ? 27.209  30.630  -6.789  1.000 64.769  0 417 LYS BBB CE  1 ? 7  
ATOM   1635 N NZ  . LYS B 2 88  ? 28.407  31.273  -6.199  1.000 68.264  0 417 LYS BBB NZ  1 ? 7  
ATOM   1636 N N   . ILE B 2 89  ? 24.378  24.570  -5.245  1.000 38.073  0 418 ILE BBB N   1 ? 8  
ATOM   1637 C CA  . ILE B 2 89  ? 23.778  23.582  -4.298  1.000 38.033  0 418 ILE BBB CA  1 ? 8  
ATOM   1638 C C   . ILE B 2 89  ? 24.738  22.403  -4.148  1.000 37.590  0 418 ILE BBB C   1 ? 8  
ATOM   1639 O O   . ILE B 2 89  ? 25.135  22.129  -3.007  1.000 40.064  0 418 ILE BBB O   1 ? 8  
ATOM   1640 C CB  . ILE B 2 89  ? 22.374  23.132  -4.750  1.000 37.914  0 418 ILE BBB CB  1 ? 8  
ATOM   1641 C CG1 . ILE B 2 89  ? 21.444  24.321  -4.995  1.000 38.006  0 418 ILE BBB CG1 1 ? 8  
ATOM   1642 C CG2 . ILE B 2 89  ? 21.785  22.143  -3.757  1.000 37.215  0 418 ILE BBB CG2 1 ? 8  
ATOM   1643 C CD1 . ILE B 2 89  ? 21.345  25.278  -3.826  1.000 39.838  0 418 ILE BBB CD1 1 ? 8  
ATOM   1644 N N   . ALA B 2 90  ? 25.075  21.734  -5.253  1.000 38.328  0 419 ALA BBB N   1 ? 8  
ATOM   1645 C CA  . ALA B 2 90  ? 25.990  20.568  -5.300  1.000 40.940  0 419 ALA BBB CA  1 ? 8  
ATOM   1646 C C   . ALA B 2 90  ? 27.350  20.945  -4.697  1.000 41.898  0 419 ALA BBB C   1 ? 8  
ATOM   1647 O O   . ALA B 2 90  ? 27.906  20.126  -3.956  1.000 45.210  0 419 ALA BBB O   1 ? 8  
ATOM   1648 C CB  . ALA B 2 90  ? 26.139  20.078  -6.723  1.000 42.483  0 419 ALA BBB CB  1 ? 8  
ATOM   1649 N N   . ASP B 2 91  ? 27.840  22.153  -4.988  1.000 41.171  0 420 ASP BBB N   1 ? 8  
ATOM   1650 C CA  . ASP B 2 91  ? 29.181  22.642  -4.580  1.000 41.295  0 420 ASP BBB CA  1 ? 8  
ATOM   1651 C C   . ASP B 2 91  ? 29.199  23.019  -3.093  1.000 42.367  0 420 ASP BBB C   1 ? 8  
ATOM   1652 O O   . ASP B 2 91  ? 30.145  22.592  -2.401  1.000 42.994  0 420 ASP BBB O   1 ? 8  
ATOM   1653 C CB  . ASP B 2 91  ? 29.618  23.839  -5.432  1.000 41.909  0 420 ASP BBB CB  1 ? 8  
ATOM   1654 C CG  . ASP B 2 91  ? 29.881  23.507  -6.900  1.000 41.821  0 420 ASP BBB CG  1 ? 8  
ATOM   1655 O OD1 . ASP B 2 91  ? 29.867  22.302  -7.262  1.000 39.914  0 420 ASP BBB OD1 1 ? 8  
ATOM   1656 O OD2 . ASP B 2 91  ? 30.087  24.459  -7.680  1.000 42.056  0 420 ASP BBB OD2 1 ? 8  
ATOM   1657 N N   . TYR B 2 92  ? 28.220  23.800  -2.620  1.000 41.770  0 421 TYR BBB N   1 ? 8  
ATOM   1658 C CA  . TYR B 2 92  ? 28.296  24.549  -1.334  1.000 40.166  0 421 TYR BBB CA  1 ? 8  
ATOM   1659 C C   . TYR B 2 92  ? 27.219  24.142  -0.318  1.000 37.746  0 421 TYR BBB C   1 ? 8  
ATOM   1660 O O   . TYR B 2 92  ? 27.342  24.601  0.839   1.000 37.243  0 421 TYR BBB O   1 ? 8  
ATOM   1661 C CB  . TYR B 2 92  ? 28.168  26.058  -1.560  1.000 40.861  0 421 TYR BBB CB  1 ? 8  
ATOM   1662 C CG  . TYR B 2 92  ? 29.210  26.695  -2.444  1.000 42.547  0 421 TYR BBB CG  1 ? 8  
ATOM   1663 C CD1 . TYR B 2 92  ? 30.444  26.103  -2.673  1.000 44.784  0 421 TYR BBB CD1 1 ? 8  
ATOM   1664 C CD2 . TYR B 2 92  ? 28.980  27.949  -2.994  1.000 44.421  0 421 TYR BBB CD2 1 ? 8  
ATOM   1665 C CE1 . TYR B 2 92  ? 31.401  26.710  -3.473  1.000 45.205  0 421 TYR BBB CE1 1 ? 8  
ATOM   1666 C CE2 . TYR B 2 92  ? 29.925  28.568  -3.799  1.000 46.534  0 421 TYR BBB CE2 1 ? 8  
ATOM   1667 C CZ  . TYR B 2 92  ? 31.144  27.952  -4.030  1.000 46.227  0 421 TYR BBB CZ  1 ? 8  
ATOM   1668 O OH  . TYR B 2 92  ? 32.071  28.568  -4.821  1.000 47.752  0 421 TYR BBB OH  1 ? 8  
ATOM   1669 N N   . ASN B 2 93  ? 26.214  23.339  -0.684  1.000 37.806  0 422 ASN BBB N   1 ? 8  
ATOM   1670 C CA  . ASN B 2 93  ? 25.033  23.113  0.198   1.000 37.899  0 422 ASN BBB CA  1 ? 8  
ATOM   1671 C C   . ASN B 2 93  ? 24.813  21.622  0.473   1.000 36.472  0 422 ASN BBB C   1 ? 8  
ATOM   1672 O O   . ASN B 2 93  ? 24.861  21.230  1.657   1.000 35.546  0 422 ASN BBB O   1 ? 8  
ATOM   1673 C CB  . ASN B 2 93  ? 23.791  23.798  -0.367  1.000 37.575  0 422 ASN BBB CB  1 ? 8  
ATOM   1674 C CG  . ASN B 2 93  ? 23.908  25.306  -0.300  1.000 38.474  0 422 ASN BBB CG  1 ? 8  
ATOM   1675 O OD1 . ASN B 2 93  ? 23.467  25.921  0.675   1.000 35.510  0 422 ASN BBB OD1 1 ? 8  
ATOM   1676 N ND2 . ASN B 2 93  ? 24.541  25.900  -1.304  1.000 38.993  0 422 ASN BBB ND2 1 ? 8  
ATOM   1677 N N   . TYR B 2 94  ? 24.543  20.830  -0.563  1.000 35.509  0 423 TYR BBB N   1 ? 8  
ATOM   1678 C CA  . TYR B 2 94  ? 24.297  19.369  -0.454  1.000 36.209  0 423 TYR BBB CA  1 ? 8  
ATOM   1679 C C   . TYR B 2 94  ? 24.913  18.674  -1.670  1.000 38.170  0 423 TYR BBB C   1 ? 8  
ATOM   1680 O O   . TYR B 2 94  ? 24.502  18.979  -2.803  1.000 39.952  0 423 TYR BBB O   1 ? 8  
ATOM   1681 C CB  . TYR B 2 94  ? 22.800  19.080  -0.313  1.000 34.996  0 423 TYR BBB CB  1 ? 8  
ATOM   1682 C CG  . TYR B 2 94  ? 22.469  17.631  -0.058  1.000 34.787  0 423 TYR BBB CG  1 ? 8  
ATOM   1683 C CD1 . TYR B 2 94  ? 22.471  17.114  1.226   1.000 34.574  0 423 TYR BBB CD1 1 ? 8  
ATOM   1684 C CD2 . TYR B 2 94  ? 22.183  16.767  -1.104  1.000 35.486  0 423 TYR BBB CD2 1 ? 8  
ATOM   1685 C CE1 . TYR B 2 94  ? 22.179  15.780  1.473   1.000 34.749  0 423 TYR BBB CE1 1 ? 8  
ATOM   1686 C CE2 . TYR B 2 94  ? 21.886  15.432  -0.876  1.000 35.523  0 423 TYR BBB CE2 1 ? 8  
ATOM   1687 C CZ  . TYR B 2 94  ? 21.879  14.937  0.416   1.000 34.685  0 423 TYR BBB CZ  1 ? 8  
ATOM   1688 O OH  . TYR B 2 94  ? 21.590  13.623  0.639   1.000 35.598  0 423 TYR BBB OH  1 ? 8  
ATOM   1689 N N   . LYS B 2 95  ? 25.869  17.776  -1.419  1.000 38.965  0 424 LYS BBB N   1 ? 8  
ATOM   1690 C CA  . LYS B 2 95  ? 26.660  17.053  -2.440  1.000 39.807  0 424 LYS BBB CA  1 ? 8  
ATOM   1691 C C   . LYS B 2 95  ? 26.402  15.549  -2.314  1.000 40.140  0 424 LYS BBB C   1 ? 8  
ATOM   1692 O O   . LYS B 2 95  ? 26.804  14.970  -1.295  1.000 39.881  0 424 LYS BBB O   1 ? 8  
ATOM   1693 C CB  . LYS B 2 95  ? 28.146  17.367  -2.247  1.000 42.261  0 424 LYS BBB CB  1 ? 8  
ATOM   1694 C CG  . LYS B 2 95  ? 29.093  16.692  -3.230  1.000 43.962  0 424 LYS BBB CG  1 ? 8  
ATOM   1695 C CD  . LYS B 2 95  ? 28.683  16.862  -4.680  1.000 44.069  0 424 LYS BBB CD  1 ? 8  
ATOM   1696 C CE  . LYS B 2 95  ? 29.745  16.379  -5.643  1.000 45.575  0 424 LYS BBB CE  1 ? 8  
ATOM   1697 N NZ  . LYS B 2 95  ? 29.326  16.565  -7.049  1.000 46.736  0 424 LYS BBB NZ  1 ? 8  
ATOM   1698 N N   . LEU B 2 96  ? 25.763  14.942  -3.319  1.000 41.374  0 425 LEU BBB N   1 ? 8  
ATOM   1699 C CA  . LEU B 2 96  ? 25.702  13.464  -3.487  1.000 43.185  0 425 LEU BBB CA  1 ? 8  
ATOM   1700 C C   . LEU B 2 96  ? 27.057  12.985  -3.999  1.000 43.437  0 425 LEU BBB C   1 ? 8  
ATOM   1701 O O   . LEU B 2 96  ? 27.729  13.707  -4.731  1.000 43.297  0 425 LEU BBB O   1 ? 8  
ATOM   1702 C CB  . LEU B 2 96  ? 24.585  13.093  -4.472  1.000 43.827  0 425 LEU BBB CB  1 ? 8  
ATOM   1703 C CG  . LEU B 2 96  ? 23.158  13.242  -3.952  1.000 44.913  0 425 LEU BBB CG  1 ? 8  
ATOM   1704 C CD1 . LEU B 2 96  ? 22.150  12.663  -4.935  1.000 45.380  0 425 LEU BBB CD1 1 ? 8  
ATOM   1705 C CD2 . LEU B 2 96  ? 23.003  12.580  -2.593  1.000 46.336  0 425 LEU BBB CD2 1 ? 8  
ATOM   1706 N N   . PRO B 2 97  ? 27.513  11.770  -3.623  1.000 44.456  0 426 PRO BBB N   1 ? 8  
ATOM   1707 C CA  . PRO B 2 97  ? 28.739  11.205  -4.188  1.000 46.129  0 426 PRO BBB CA  1 ? 8  
ATOM   1708 C C   . PRO B 2 97  ? 28.531  10.764  -5.644  1.000 46.700  0 426 PRO BBB C   1 ? 8  
ATOM   1709 O O   . PRO B 2 97  ? 27.411  10.436  -6.004  1.000 48.936  0 426 PRO BBB O   1 ? 8  
ATOM   1710 C CB  . PRO B 2 97  ? 29.041  10.000  -3.287  1.000 46.863  0 426 PRO BBB CB  1 ? 8  
ATOM   1711 C CG  . PRO B 2 97  ? 27.683  9.595   -2.740  1.000 46.444  0 426 PRO BBB CG  1 ? 8  
ATOM   1712 C CD  . PRO B 2 97  ? 26.892  10.884  -2.628  1.000 44.589  0 426 PRO BBB CD  1 ? 8  
ATOM   1713 N N   . ASP B 2 98  ? 29.605  10.768  -6.436  1.000 47.241  0 427 ASP BBB N   1 ? 8  
ATOM   1714 C CA  . ASP B 2 98  ? 29.614  10.275  -7.836  1.000 48.420  0 427 ASP BBB CA  1 ? 8  
ATOM   1715 C C   . ASP B 2 98  ? 28.954  8.891   -7.889  1.000 47.888  0 427 ASP BBB C   1 ? 8  
ATOM   1716 O O   . ASP B 2 98  ? 28.241  8.634   -8.875  1.000 49.018  0 427 ASP BBB O   1 ? 8  
ATOM   1717 C CB  . ASP B 2 98  ? 31.039  10.223  -8.402  1.000 50.086  0 427 ASP BBB CB  1 ? 8  
ATOM   1718 C CG  . ASP B 2 98  ? 31.633  11.569  -8.782  1.000 50.412  0 427 ASP BBB CG  1 ? 8  
ATOM   1719 O OD1 . ASP B 2 98  ? 30.959  12.598  -8.587  1.000 47.983  0 427 ASP BBB OD1 1 ? 8  
ATOM   1720 O OD2 . ASP B 2 98  ? 32.776  11.570  -9.285  1.000 55.496  0 427 ASP BBB OD2 1 ? 8  
ATOM   1721 N N   . ASP B 2 99  ? 29.167  8.047   -6.872  1.000 46.838  0 428 ASP BBB N   1 ? 8  
ATOM   1722 C CA  . ASP B 2 99  ? 28.699  6.634   -6.858  1.000 46.823  0 428 ASP BBB CA  1 ? 8  
ATOM   1723 C C   . ASP B 2 99  ? 27.437  6.501   -5.996  1.000 45.027  0 428 ASP BBB C   1 ? 8  
ATOM   1724 O O   . ASP B 2 99  ? 27.190  5.384   -5.508  1.000 43.094  0 428 ASP BBB O   1 ? 8  
ATOM   1725 C CB  . ASP B 2 99  ? 29.817  5.684   -6.409  1.000 49.018  0 428 ASP BBB CB  1 ? 8  
ATOM   1726 C CG  . ASP B 2 99  ? 30.255  5.828   -4.962  1.000 48.578  0 428 ASP BBB CG  1 ? 8  
ATOM   1727 O OD1 . ASP B 2 99  ? 29.902  6.845   -4.339  1.000 48.823  0 428 ASP BBB OD1 1 ? 8  
ATOM   1728 O OD2 . ASP B 2 99  ? 30.942  4.912   -4.469  1.000 49.629  0 428 ASP BBB OD2 1 ? 8  
ATOM   1729 N N   . PHE B 2 100 ? 26.648  7.574   -5.854  1.000 45.357  0 429 PHE BBB N   1 ? 8  
ATOM   1730 C CA  . PHE B 2 100 ? 25.392  7.575   -5.059  1.000 46.286  0 429 PHE BBB CA  1 ? 8  
ATOM   1731 C C   . PHE B 2 100 ? 24.497  6.421   -5.521  1.000 48.612  0 429 PHE BBB C   1 ? 8  
ATOM   1732 O O   . PHE B 2 100 ? 24.228  6.283   -6.726  1.000 51.213  0 429 PHE BBB O   1 ? 8  
ATOM   1733 C CB  . PHE B 2 100 ? 24.615  8.890   -5.163  1.000 45.005  0 429 PHE BBB CB  1 ? 8  
ATOM   1734 C CG  . PHE B 2 100 ? 23.270  8.863   -4.474  1.000 44.070  0 429 PHE BBB CG  1 ? 8  
ATOM   1735 C CD1 . PHE B 2 100 ? 23.196  8.861   -3.090  1.000 43.846  0 429 PHE BBB CD1 1 ? 8  
ATOM   1736 C CD2 . PHE B 2 100 ? 22.081  8.827   -5.197  1.000 44.268  0 429 PHE BBB CD2 1 ? 8  
ATOM   1737 C CE1 . PHE B 2 100 ? 21.972  8.840   -2.442  1.000 43.331  0 429 PHE BBB CE1 1 ? 8  
ATOM   1738 C CE2 . PHE B 2 100 ? 20.855  8.797   -4.547  1.000 44.649  0 429 PHE BBB CE2 1 ? 8  
ATOM   1739 C CZ  . PHE B 2 100 ? 20.803  8.807   -3.169  1.000 44.632  0 429 PHE BBB CZ  1 ? 8  
ATOM   1740 N N   . THR B 2 101 ? 24.084  5.605   -4.556  1.000 52.563  0 430 THR BBB N   1 ? 8  
ATOM   1741 C CA  . THR B 2 101 ? 23.056  4.548   -4.667  1.000 52.994  0 430 THR BBB CA  1 ? 8  
ATOM   1742 C C   . THR B 2 101 ? 21.935  4.932   -3.703  1.000 54.328  0 430 THR BBB C   1 ? 8  
ATOM   1743 O O   . THR B 2 101 ? 22.197  5.038   -2.477  1.000 59.191  0 430 THR BBB O   1 ? 8  
ATOM   1744 C CB  . THR B 2 101 ? 23.626  3.165   -4.333  1.000 55.977  0 430 THR BBB CB  1 ? 8  
ATOM   1745 O OG1 . THR B 2 101 ? 24.376  2.731   -5.468  1.000 56.713  0 430 THR BBB OG1 1 ? 8  
ATOM   1746 C CG2 . THR B 2 101 ? 22.555  2.155   -3.993  1.000 60.061  0 430 THR BBB CG2 1 ? 8  
ATOM   1747 N N   . GLY B 2 102 ? 20.730  5.121   -4.232  1.000 49.356  0 431 GLY BBB N   1 ? 8  
ATOM   1748 C CA  . GLY B 2 102 ? 19.543  5.481   -3.439  1.000 46.377  0 431 GLY BBB CA  1 ? 8  
ATOM   1749 C C   . GLY B 2 102 ? 18.527  6.173   -4.316  1.000 45.158  0 431 GLY BBB C   1 ? 8  
ATOM   1750 O O   . GLY B 2 102 ? 18.609  6.009   -5.557  1.000 44.711  0 431 GLY BBB O   1 ? 8  
ATOM   1751 N N   . CYS B 2 103 ? 17.596  6.901   -3.705  1.000 43.156  0 432 CYS BBB N   1 ? 8  
ATOM   1752 C CA  . CYS B 2 103 ? 16.494  7.594   -4.417  1.000 42.800  0 432 CYS BBB CA  1 ? 8  
ATOM   1753 C C   . CYS B 2 103 ? 16.495  9.070   -4.016  1.000 41.208  0 432 CYS BBB C   1 ? 8  
ATOM   1754 O O   . CYS B 2 103 ? 16.752  9.361   -2.838  1.000 41.156  0 432 CYS BBB O   1 ? 8  
ATOM   1755 C CB  . CYS B 2 103 ? 15.162  6.912   -4.134  1.000 42.423  0 432 CYS BBB CB  1 ? 8  
ATOM   1756 S SG  . CYS B 2 103 ? 15.152  5.173   -4.644  1.000 44.889  0 432 CYS BBB SG  1 ? 8  
ATOM   1757 N N   . VAL B 2 104 ? 16.313  9.955   -4.996  1.000 40.652  0 433 VAL BBB N   1 ? 8  
ATOM   1758 C CA  . VAL B 2 104 ? 16.086  11.411  -4.785  1.000 40.085  0 433 VAL BBB CA  1 ? 8  
ATOM   1759 C C   . VAL B 2 104 ? 14.603  11.672  -5.066  1.000 40.482  0 433 VAL BBB C   1 ? 8  
ATOM   1760 O O   . VAL B 2 104 ? 14.158  11.408  -6.200  1.000 38.692  0 433 VAL BBB O   1 ? 8  
ATOM   1761 C CB  . VAL B 2 104 ? 17.017  12.262  -5.666  1.000 40.222  0 433 VAL BBB CB  1 ? 8  
ATOM   1762 C CG1 . VAL B 2 104 ? 16.663  13.740  -5.599  1.000 40.553  0 433 VAL BBB CG1 1 ? 8  
ATOM   1763 C CG2 . VAL B 2 104 ? 18.481  12.044  -5.298  1.000 41.225  0 433 VAL BBB CG2 1 ? 8  
ATOM   1764 N N   . ILE B 2 105 ? 13.865  12.120  -4.049  1.000 40.202  0 434 ILE BBB N   1 ? 8  
ATOM   1765 C CA  . ILE B 2 105 ? 12.403  12.407  -4.135  1.000 41.640  0 434 ILE BBB CA  1 ? 8  
ATOM   1766 C C   . ILE B 2 105 ? 12.219  13.914  -3.951  1.000 41.252  0 434 ILE BBB C   1 ? 8  
ATOM   1767 O O   . ILE B 2 105 ? 12.756  14.453  -2.976  1.000 40.303  0 434 ILE BBB O   1 ? 8  
ATOM   1768 C CB  . ILE B 2 105 ? 11.608  11.581  -3.103  1.000 41.725  0 434 ILE BBB CB  1 ? 8  
ATOM   1769 C CG1 . ILE B 2 105 ? 11.960  10.093  -3.194  1.000 41.733  0 434 ILE BBB CG1 1 ? 8  
ATOM   1770 C CG2 . ILE B 2 105 ? 10.109  11.816  -3.264  1.000 42.848  0 434 ILE BBB CG2 1 ? 8  
ATOM   1771 C CD1 . ILE B 2 105 ? 11.561  9.285   -1.981  1.000 42.292  0 434 ILE BBB CD1 1 ? 8  
ATOM   1772 N N   . ALA B 2 106 ? 11.532  14.560  -4.893  1.000 41.833  0 435 ALA BBB N   1 ? 8  
ATOM   1773 C CA  . ALA B 2 106 ? 11.254  16.012  -4.895  1.000 41.382  0 435 ALA BBB CA  1 ? 8  
ATOM   1774 C C   . ALA B 2 106 ? 9.823   16.263  -5.385  1.000 42.550  0 435 ALA BBB C   1 ? 8  
ATOM   1775 O O   . ALA B 2 106 ? 9.330   15.525  -6.268  1.000 40.353  0 435 ALA BBB O   1 ? 8  
ATOM   1776 C CB  . ALA B 2 106 ? 12.269  16.738  -5.745  1.000 41.057  0 435 ALA BBB CB  1 ? 8  
ATOM   1777 N N   . TRP B 2 107 ? 9.180   17.277  -4.811  1.000 42.072  0 436 TRP BBB N   1 ? 8  
ATOM   1778 C CA  . TRP B 2 107 ? 7.844   17.757  -5.234  1.000 41.663  0 436 TRP BBB CA  1 ? 8  
ATOM   1779 C C   . TRP B 2 107 ? 7.777   19.270  -5.048  1.000 40.343  0 436 TRP BBB C   1 ? 8  
ATOM   1780 O O   . TRP B 2 107 ? 8.468   19.785  -4.139  1.000 37.893  0 436 TRP BBB O   1 ? 8  
ATOM   1781 C CB  . TRP B 2 107 ? 6.733   17.026  -4.475  1.000 43.044  0 436 TRP BBB CB  1 ? 8  
ATOM   1782 C CG  . TRP B 2 107 ? 6.720   17.239  -2.993  1.000 42.721  0 436 TRP BBB CG  1 ? 8  
ATOM   1783 C CD1 . TRP B 2 107 ? 5.894   18.069  -2.299  1.000 42.418  0 436 TRP BBB CD1 1 ? 8  
ATOM   1784 C CD2 . TRP B 2 107 ? 7.537   16.574  -2.012  1.000 43.326  0 436 TRP BBB CD2 1 ? 8  
ATOM   1785 N NE1 . TRP B 2 107 ? 6.142   17.972  -0.957  1.000 43.035  0 436 TRP BBB NE1 1 ? 8  
ATOM   1786 C CE2 . TRP B 2 107 ? 7.141   17.060  -0.748  1.000 43.314  0 436 TRP BBB CE2 1 ? 8  
ATOM   1787 C CE3 . TRP B 2 107 ? 8.561   15.618  -2.073  1.000 43.732  0 436 TRP BBB CE3 1 ? 8  
ATOM   1788 C CZ2 . TRP B 2 107 ? 7.742   16.631  0.436   1.000 43.622  0 436 TRP BBB CZ2 1 ? 8  
ATOM   1789 C CZ3 . TRP B 2 107 ? 9.153   15.195  -0.903  1.000 43.255  0 436 TRP BBB CZ3 1 ? 8  
ATOM   1790 C CH2 . TRP B 2 107 ? 8.745   15.694  0.335   1.000 43.494  0 436 TRP BBB CH2 1 ? 8  
ATOM   1791 N N   . ASN B 2 108 ? 6.996   19.933  -5.908  1.000 39.246  0 437 ASN BBB N   1 ? 8  
ATOM   1792 C CA  . ASN B 2 108 ? 6.697   21.385  -5.842  1.000 39.769  0 437 ASN BBB CA  1 ? 8  
ATOM   1793 C C   . ASN B 2 108 ? 5.959   21.650  -4.524  1.000 40.300  0 437 ASN BBB C   1 ? 8  
ATOM   1794 O O   . ASN B 2 108 ? 4.952   20.974  -4.271  1.000 41.105  0 437 ASN BBB O   1 ? 8  
ATOM   1795 C CB  . ASN B 2 108 ? 5.899   21.837  -7.069  1.000 40.433  0 437 ASN BBB CB  1 ? 8  
ATOM   1796 C CG  . ASN B 2 108 ? 5.740   23.340  -7.149  1.000 40.804  0 437 ASN BBB CG  1 ? 8  
ATOM   1797 O OD1 . ASN B 2 108 ? 5.153   23.947  -6.259  1.000 41.410  0 437 ASN BBB OD1 1 ? 8  
ATOM   1798 N ND2 . ASN B 2 108 ? 6.249   23.947  -8.208  1.000 40.126  0 437 ASN BBB ND2 1 ? 8  
ATOM   1799 N N   . SER B 2 109 ? 6.469   22.575  -3.706  1.000 40.148  0 438 SER BBB N   1 ? 8  
ATOM   1800 C CA  . SER B 2 109 ? 5.935   22.904  -2.362  1.000 41.173  0 438 SER BBB CA  1 ? 8  
ATOM   1801 C C   . SER B 2 109 ? 5.462   24.363  -2.330  1.000 43.209  0 438 SER BBB C   1 ? 8  
ATOM   1802 O O   . SER B 2 109 ? 5.388   24.932  -1.227  1.000 43.807  0 438 SER BBB O   1 ? 8  
ATOM   1803 C CB  . SER B 2 109 ? 6.966   22.617  -1.303  1.000 39.822  0 438 SER BBB CB  1 ? 8  
ATOM   1804 O OG  . SER B 2 109 ? 8.107   23.438  -1.484  1.000 38.811  0 438 SER BBB OG  1 ? 8  
ATOM   1805 N N   . ASN B 2 110 ? 5.125   24.926  -3.497  1.000 44.918  0 439 ASN BBB N   1 ? 8  
ATOM   1806 C CA  . ASN B 2 110 ? 4.686   26.338  -3.669  1.000 46.056  0 439 ASN BBB CA  1 ? 8  
ATOM   1807 C C   . ASN B 2 110 ? 3.511   26.618  -2.724  1.000 46.991  0 439 ASN BBB C   1 ? 8  
ATOM   1808 O O   . ASN B 2 110 ? 3.495   27.703  -2.123  1.000 48.123  0 439 ASN BBB O   1 ? 8  
ATOM   1809 C CB  . ASN B 2 110 ? 4.310   26.642  -5.123  1.000 46.842  0 439 ASN BBB CB  1 ? 8  
ATOM   1810 C CG  . ASN B 2 110 ? 4.318   28.119  -5.461  1.000 47.599  0 439 ASN BBB CG  1 ? 8  
ATOM   1811 O OD1 . ASN B 2 110 ? 5.179   28.863  -4.996  1.000 49.036  0 439 ASN BBB OD1 1 ? 8  
ATOM   1812 N ND2 . ASN B 2 110 ? 3.388   28.548  -6.297  1.000 48.465  0 439 ASN BBB ND2 1 ? 8  
ATOM   1813 N N   . ASN B 2 111 ? 2.592   25.660  -2.577  1.000 46.825  0 440 ASN BBB N   1 ? 8  
ATOM   1814 C CA  A ASN B 2 111 ? 1.355   25.809  -1.758  0.500 49.428  0 440 ASN BBB CA  1 ? 8  
ATOM   1815 C CA  B ASN B 2 111 ? 1.356   25.817  -1.760  0.500 48.887  0 440 ASN BBB CA  1 ? 8  
ATOM   1816 C C   . ASN B 2 111 ? 1.706   25.853  -0.265  1.000 49.285  0 440 ASN BBB C   1 ? 8  
ATOM   1817 O O   . ASN B 2 111 ? 0.904   26.414  0.495   1.000 50.855  0 440 ASN BBB O   1 ? 8  
ATOM   1818 C CB  A ASN B 2 111 ? 0.343   24.695  -2.040  0.500 49.996  0 440 ASN BBB CB  1 ? 8  
ATOM   1819 C CB  B ASN B 2 111 ? 0.331   24.721  -2.067  0.500 48.772  0 440 ASN BBB CB  1 ? 8  
ATOM   1820 C CG  A ASN B 2 111 ? 0.856   23.321  -1.667  0.500 48.957  0 440 ASN BBB CG  1 ? 8  
ATOM   1821 C CG  B ASN B 2 111 ? -0.159  24.760  -3.501  0.500 49.005  0 440 ASN BBB CG  1 ? 8  
ATOM   1822 O OD1 A ASN B 2 111 ? 1.962   22.941  -2.048  0.500 48.158  0 440 ASN BBB OD1 1 ? 8  
ATOM   1823 O OD1 B ASN B 2 111 ? -0.214  25.822  -4.118  0.500 48.711  0 440 ASN BBB OD1 1 ? 8  
ATOM   1824 N ND2 A ASN B 2 111 ? 0.058   22.569  -0.926  0.500 49.314  0 440 ASN BBB ND2 1 ? 8  
ATOM   1825 N ND2 B ASN B 2 111 ? -0.506  23.605  -4.044  0.500 48.902  0 440 ASN BBB ND2 1 ? 8  
ATOM   1826 N N   . LEU B 2 112 ? 2.853   25.281  0.129   1.000 48.076  0 441 LEU BBB N   1 ? 8  
ATOM   1827 C CA  . LEU B 2 112 ? 3.289   25.167  1.551   1.000 47.995  0 441 LEU BBB CA  1 ? 8  
ATOM   1828 C C   . LEU B 2 112 ? 4.313   26.253  1.901   1.000 47.485  0 441 LEU BBB C   1 ? 8  
ATOM   1829 O O   . LEU B 2 112 ? 4.208   26.824  2.998   1.000 49.827  0 441 LEU BBB O   1 ? 8  
ATOM   1830 C CB  . LEU B 2 112 ? 3.906   23.783  1.790   1.000 47.735  0 441 LEU BBB CB  1 ? 8  
ATOM   1831 C CG  . LEU B 2 112 ? 2.971   22.582  1.639   1.000 48.608  0 441 LEU BBB CG  1 ? 8  
ATOM   1832 C CD1 . LEU B 2 112 ? 3.768   21.284  1.583   1.000 47.877  0 441 LEU BBB CD1 1 ? 8  
ATOM   1833 C CD2 . LEU B 2 112 ? 1.962   22.536  2.773   1.000 49.311  0 441 LEU BBB CD2 1 ? 8  
ATOM   1834 N N   . ASP B 2 113 ? 5.278   26.507  1.015   1.000 46.443  0 442 ASP BBB N   1 ? 8  
ATOM   1835 C CA  . ASP B 2 113 ? 6.560   27.183  1.352   1.000 45.316  0 442 ASP BBB CA  1 ? 8  
ATOM   1836 C C   . ASP B 2 113 ? 6.645   28.577  0.720   1.000 47.829  0 442 ASP BBB C   1 ? 8  
ATOM   1837 O O   . ASP B 2 113 ? 7.658   29.262  0.984   1.000 48.519  0 442 ASP BBB O   1 ? 8  
ATOM   1838 C CB  . ASP B 2 113 ? 7.743   26.310  0.929   1.000 42.612  0 442 ASP BBB CB  1 ? 8  
ATOM   1839 C CG  . ASP B 2 113 ? 7.903   25.076  1.794   1.000 42.087  0 442 ASP BBB CG  1 ? 8  
ATOM   1840 O OD1 . ASP B 2 113 ? 7.818   25.215  3.045   1.000 41.624  0 442 ASP BBB OD1 1 ? 8  
ATOM   1841 O OD2 . ASP B 2 113 ? 8.107   23.988  1.221   1.000 40.806  0 442 ASP BBB OD2 1 ? 8  
ATOM   1842 N N   . SER B 2 114 ? 5.651   28.989  -0.074  1.000 49.150  0 443 SER BBB N   1 ? 8  
ATOM   1843 C CA  . SER B 2 114 ? 5.547   30.372  -0.608  1.000 49.581  0 443 SER BBB CA  1 ? 8  
ATOM   1844 C C   . SER B 2 114 ? 4.466   31.118  0.179   1.000 51.081  0 443 SER BBB C   1 ? 8  
ATOM   1845 O O   . SER B 2 114 ? 3.532   30.458  0.672   1.000 49.883  0 443 SER BBB O   1 ? 8  
ATOM   1846 C CB  . SER B 2 114 ? 5.288   30.383  -2.092  1.000 50.532  0 443 SER BBB CB  1 ? 8  
ATOM   1847 O OG  . SER B 2 114 ? 3.898   30.310  -2.376  1.000 53.871  0 443 SER BBB OG  1 ? 8  
ATOM   1848 N N   . LYS B 2 115 ? 4.625   32.435  0.318   1.000 53.454  0 444 LYS BBB N   1 ? 8  
ATOM   1849 C CA  . LYS B 2 115 ? 3.659   33.342  0.992   1.000 58.624  0 444 LYS BBB CA  1 ? 8  
ATOM   1850 C C   . LYS B 2 115 ? 3.590   34.654  0.207   1.000 58.195  0 444 LYS BBB C   1 ? 8  
ATOM   1851 O O   . LYS B 2 115 ? 4.636   35.076  -0.322  1.000 55.474  0 444 LYS BBB O   1 ? 8  
ATOM   1852 C CB  . LYS B 2 115 ? 4.077   33.588  2.447   1.000 62.994  0 444 LYS BBB CB  1 ? 8  
ATOM   1853 C CG  . LYS B 2 115 ? 3.843   32.407  3.387   1.000 67.732  0 444 LYS BBB CG  1 ? 8  
ATOM   1854 C CD  . LYS B 2 115 ? 4.789   32.343  4.579   1.000 71.991  0 444 LYS BBB CD  1 ? 8  
ATOM   1855 C CE  . LYS B 2 115 ? 5.134   30.926  4.995   1.000 72.057  0 444 LYS BBB CE  1 ? 8  
ATOM   1856 N NZ  . LYS B 2 115 ? 6.161   30.913  6.066   1.000 70.509  0 444 LYS BBB NZ  1 ? 8  
ATOM   1857 N N   . VAL B 2 116 ? 2.403   35.260  0.137   1.000 58.620  0 445 VAL BBB N   1 ? 8  
ATOM   1858 C CA  . VAL B 2 116 ? 2.197   36.636  -0.407  1.000 60.643  0 445 VAL BBB CA  1 ? 8  
ATOM   1859 C C   . VAL B 2 116 ? 3.141   37.572  0.361   1.000 60.082  0 445 VAL BBB C   1 ? 8  
ATOM   1860 O O   . VAL B 2 116 ? 3.157   37.497  1.607   1.000 61.119  0 445 VAL BBB O   1 ? 8  
ATOM   1861 C CB  . VAL B 2 116 ? 0.729   37.097  -0.294  1.000 62.854  0 445 VAL BBB CB  1 ? 8  
ATOM   1862 C CG1 . VAL B 2 116 ? 0.493   38.380  -1.077  1.000 64.086  0 445 VAL BBB CG1 1 ? 8  
ATOM   1863 C CG2 . VAL B 2 116 ? -0.260  36.020  -0.727  1.000 62.876  0 445 VAL BBB CG2 1 ? 8  
ATOM   1864 N N   . GLY B 2 117 ? 3.916   38.393  -0.355  1.000 58.708  0 446 GLY BBB N   1 ? 8  
ATOM   1865 C CA  . GLY B 2 117 ? 5.006   39.211  0.212   1.000 57.806  0 446 GLY BBB CA  1 ? 8  
ATOM   1866 C C   . GLY B 2 117 ? 6.341   38.482  0.161   1.000 54.903  0 446 GLY BBB C   1 ? 8  
ATOM   1867 O O   . GLY B 2 117 ? 7.382   39.161  0.243   1.000 55.067  0 446 GLY BBB O   1 ? 8  
ATOM   1868 N N   . GLY B 2 118 ? 6.312   37.150  0.036   1.000 53.222  0 447 GLY BBB N   1 ? 8  
ATOM   1869 C CA  . GLY B 2 118 ? 7.500   36.286  -0.084  1.000 51.659  0 447 GLY BBB CA  1 ? 8  
ATOM   1870 C C   . GLY B 2 118 ? 7.874   35.641  1.239   1.000 51.128  0 447 GLY BBB C   1 ? 8  
ATOM   1871 O O   . GLY B 2 118 ? 7.852   36.344  2.266   1.000 51.847  0 447 GLY BBB O   1 ? 8  
ATOM   1872 N N   . ASN B 2 119 ? 8.192   34.343  1.216   1.000 50.015  0 448 ASN BBB N   1 ? 8  
ATOM   1873 C CA  . ASN B 2 119 ? 8.838   33.611  2.337   1.000 48.194  0 448 ASN BBB CA  1 ? 8  
ATOM   1874 C C   . ASN B 2 119 ? 10.345  33.576  2.067   1.000 46.793  0 448 ASN BBB C   1 ? 8  
ATOM   1875 O O   . ASN B 2 119 ? 10.741  33.061  1.004   1.000 46.501  0 448 ASN BBB O   1 ? 8  
ATOM   1876 C CB  . ASN B 2 119 ? 8.263   32.203  2.499   1.000 48.684  0 448 ASN BBB CB  1 ? 8  
ATOM   1877 C CG  . ASN B 2 119 ? 8.965   31.389  3.567   1.000 47.964  0 448 ASN BBB CG  1 ? 8  
ATOM   1878 O OD1 . ASN B 2 119 ? 9.514   31.935  4.521   1.000 47.297  0 448 ASN BBB OD1 1 ? 8  
ATOM   1879 N ND2 . ASN B 2 119 ? 8.943   30.075  3.421   1.000 47.788  0 448 ASN BBB ND2 1 ? 8  
ATOM   1880 N N   . TYR B 2 120 ? 11.144  34.103  2.999   1.000 46.678  0 449 TYR BBB N   1 ? 8  
ATOM   1881 C CA  . TYR B 2 120 ? 12.615  34.264  2.874   1.000 44.051  0 449 TYR BBB CA  1 ? 8  
ATOM   1882 C C   . TYR B 2 120 ? 13.350  33.422  3.923   1.000 42.706  0 449 TYR BBB C   1 ? 8  
ATOM   1883 O O   . TYR B 2 120 ? 14.576  33.589  4.047   1.000 44.435  0 449 TYR BBB O   1 ? 8  
ATOM   1884 C CB  . TYR B 2 120 ? 12.981  35.744  3.006   1.000 45.167  0 449 TYR BBB CB  1 ? 8  
ATOM   1885 C CG  . TYR B 2 120 ? 12.342  36.636  1.975   1.000 47.414  0 449 TYR BBB CG  1 ? 8  
ATOM   1886 C CD1 . TYR B 2 120 ? 12.966  36.889  0.760   1.000 48.945  0 449 TYR BBB CD1 1 ? 8  
ATOM   1887 C CD2 . TYR B 2 120 ? 11.104  37.215  2.202   1.000 49.054  0 449 TYR BBB CD2 1 ? 8  
ATOM   1888 C CE1 . TYR B 2 120 ? 12.373  37.696  -0.200  1.000 50.006  0 449 TYR BBB CE1 1 ? 8  
ATOM   1889 C CE2 . TYR B 2 120 ? 10.501  38.026  1.255   1.000 50.066  0 449 TYR BBB CE2 1 ? 8  
ATOM   1890 C CZ  . TYR B 2 120 ? 11.138  38.268  0.052   1.000 49.657  0 449 TYR BBB CZ  1 ? 8  
ATOM   1891 O OH  . TYR B 2 120 ? 10.540  39.070  -0.873  1.000 55.623  0 449 TYR BBB OH  1 ? 8  
ATOM   1892 N N   . ASN B 2 121 ? 12.648  32.524  4.620   1.000 42.659  0 450 ASN BBB N   1 ? 8  
ATOM   1893 C CA  . ASN B 2 121 ? 13.202  31.757  5.770   1.000 43.366  0 450 ASN BBB CA  1 ? 8  
ATOM   1894 C C   . ASN B 2 121 ? 14.103  30.618  5.275   1.000 42.539  0 450 ASN BBB C   1 ? 8  
ATOM   1895 O O   . ASN B 2 121 ? 14.936  30.151  6.067   1.000 42.904  0 450 ASN BBB O   1 ? 8  
ATOM   1896 C CB  . ASN B 2 121 ? 12.098  31.223  6.682   1.000 44.559  0 450 ASN BBB CB  1 ? 8  
ATOM   1897 C CG  . ASN B 2 121 ? 11.470  32.309  7.529   1.000 46.677  0 450 ASN BBB CG  1 ? 8  
ATOM   1898 O OD1 . ASN B 2 121 ? 12.012  33.408  7.638   1.000 49.148  0 450 ASN BBB OD1 1 ? 8  
ATOM   1899 N ND2 . ASN B 2 121 ? 10.339  32.004  8.142   1.000 47.459  0 450 ASN BBB ND2 1 ? 8  
ATOM   1900 N N   . TYR B 2 122 ? 13.932  30.173  4.032   1.000 41.489  0 451 TYR BBB N   1 ? 8  
ATOM   1901 C CA  . TYR B 2 122 ? 14.790  29.141  3.396   1.000 40.577  0 451 TYR BBB CA  1 ? 8  
ATOM   1902 C C   . TYR B 2 122 ? 16.046  29.822  2.852   1.000 39.736  0 451 TYR BBB C   1 ? 8  
ATOM   1903 O O   . TYR B 2 122 ? 15.922  30.772  2.058   1.000 39.827  0 451 TYR BBB O   1 ? 8  
ATOM   1904 C CB  . TYR B 2 122 ? 14.016  28.373  2.321   1.000 41.027  0 451 TYR BBB CB  1 ? 8  
ATOM   1905 C CG  . TYR B 2 122 ? 12.964  27.455  2.884   1.000 41.779  0 451 TYR BBB CG  1 ? 8  
ATOM   1906 C CD1 . TYR B 2 122 ? 13.321  26.333  3.618   1.000 41.407  0 451 TYR BBB CD1 1 ? 8  
ATOM   1907 C CD2 . TYR B 2 122 ? 11.614  27.720  2.718   1.000 41.120  0 451 TYR BBB CD2 1 ? 8  
ATOM   1908 C CE1 . TYR B 2 122 ? 12.364  25.488  4.154   1.000 41.442  0 451 TYR BBB CE1 1 ? 8  
ATOM   1909 C CE2 . TYR B 2 122 ? 10.646  26.883  3.246   1.000 41.051  0 451 TYR BBB CE2 1 ? 8  
ATOM   1910 C CZ  . TYR B 2 122 ? 11.022  25.763  3.965   1.000 40.742  0 451 TYR BBB CZ  1 ? 8  
ATOM   1911 O OH  . TYR B 2 122 ? 10.071  24.941  4.482   1.000 42.136  0 451 TYR BBB OH  1 ? 8  
ATOM   1912 N N   . LEU B 2 123 ? 17.214  29.360  3.303   1.000 39.550  0 452 LEU BBB N   1 ? 8  
ATOM   1913 C CA  . LEU B 2 123 ? 18.541  29.944  2.972   1.000 38.984  0 452 LEU BBB CA  1 ? 8  
ATOM   1914 C C   . LEU B 2 123 ? 19.378  28.918  2.201   1.000 38.466  0 452 LEU BBB C   1 ? 8  
ATOM   1915 O O   . LEU B 2 123 ? 19.103  27.704  2.311   1.000 37.667  0 452 LEU BBB O   1 ? 8  
ATOM   1916 C CB  . LEU B 2 123 ? 19.258  30.351  4.264   1.000 39.223  0 452 LEU BBB CB  1 ? 8  
ATOM   1917 C CG  . LEU B 2 123 ? 18.460  31.198  5.257   1.000 39.294  0 452 LEU BBB CG  1 ? 8  
ATOM   1918 C CD1 . LEU B 2 123 ? 19.329  31.588  6.444   1.000 38.663  0 452 LEU BBB CD1 1 ? 8  
ATOM   1919 C CD2 . LEU B 2 123 ? 17.892  32.443  4.593   1.000 40.099  0 452 LEU BBB CD2 1 ? 8  
ATOM   1920 N N   . TYR B 2 124 ? 20.375  29.409  1.464   1.000 37.643  0 453 TYR BBB N   1 ? 8  
ATOM   1921 C CA  . TYR B 2 124 ? 21.463  28.601  0.854   1.000 37.459  0 453 TYR BBB CA  1 ? 8  
ATOM   1922 C C   . TYR B 2 124 ? 22.793  29.338  1.050   1.000 36.604  0 453 TYR BBB C   1 ? 8  
ATOM   1923 O O   . TYR B 2 124 ? 22.793  30.581  1.212   1.000 36.800  0 453 TYR BBB O   1 ? 8  
ATOM   1924 C CB  . TYR B 2 124 ? 21.173  28.327  -0.625  1.000 37.103  0 453 TYR BBB CB  1 ? 8  
ATOM   1925 C CG  . TYR B 2 124 ? 21.018  29.560  -1.474  1.000 37.176  0 453 TYR BBB CG  1 ? 8  
ATOM   1926 C CD1 . TYR B 2 124 ? 19.787  30.177  -1.613  1.000 37.713  0 453 TYR BBB CD1 1 ? 8  
ATOM   1927 C CD2 . TYR B 2 124 ? 22.104  30.121  -2.131  1.000 39.008  0 453 TYR BBB CD2 1 ? 8  
ATOM   1928 C CE1 . TYR B 2 124 ? 19.634  31.311  -2.396  1.000 39.530  0 453 TYR BBB CE1 1 ? 8  
ATOM   1929 C CE2 . TYR B 2 124 ? 21.972  31.259  -2.910  1.000 39.850  0 453 TYR BBB CE2 1 ? 8  
ATOM   1930 C CZ  . TYR B 2 124 ? 20.731  31.854  -3.045  1.000 41.135  0 453 TYR BBB CZ  1 ? 8  
ATOM   1931 O OH  . TYR B 2 124 ? 20.602  32.971  -3.816  1.000 43.144  0 453 TYR BBB OH  1 ? 8  
ATOM   1932 N N   . ARG B 2 125 ? 23.889  28.581  1.051   1.000 35.500  0 454 ARG BBB N   1 ? 8  
ATOM   1933 C CA  . ARG B 2 125 ? 25.269  29.122  1.069   1.000 37.734  0 454 ARG BBB CA  1 ? 8  
ATOM   1934 C C   . ARG B 2 125 ? 25.633  29.572  -0.352  1.000 37.741  0 454 ARG BBB C   1 ? 8  
ATOM   1935 O O   . ARG B 2 125 ? 25.575  28.730  -1.267  1.000 36.047  0 454 ARG BBB O   1 ? 8  
ATOM   1936 C CB  . ARG B 2 125 ? 26.237  28.068  1.614   1.000 38.362  0 454 ARG BBB CB  1 ? 8  
ATOM   1937 C CG  . ARG B 2 125 ? 27.636  28.600  1.890   1.000 39.089  0 454 ARG BBB CG  1 ? 8  
ATOM   1938 C CD  . ARG B 2 125 ? 28.482  27.595  2.653   1.000 39.655  0 454 ARG BBB CD  1 ? 8  
ATOM   1939 N NE  . ARG B 2 125 ? 27.847  27.205  3.906   1.000 39.641  0 454 ARG BBB NE  1 ? 8  
ATOM   1940 C CZ  . ARG B 2 125 ? 27.861  27.925  5.028   1.000 39.653  0 454 ARG BBB CZ  1 ? 8  
ATOM   1941 N NH1 . ARG B 2 125 ? 28.493  29.090  5.084   1.000 39.055  0 454 ARG BBB NH1 1 ? 8  
ATOM   1942 N NH2 . ARG B 2 125 ? 27.233  27.469  6.099   1.000 39.937  0 454 ARG BBB NH2 1 ? 8  
ATOM   1943 N N   . LEU B 2 126 ? 25.971  30.857  -0.507  1.000 38.118  0 455 LEU BBB N   1 ? 8  
ATOM   1944 C CA  . LEU B 2 126 ? 26.350  31.517  -1.785  1.000 38.520  0 455 LEU BBB CA  1 ? 8  
ATOM   1945 C C   . LEU B 2 126 ? 27.875  31.461  -1.971  1.000 40.157  0 455 LEU BBB C   1 ? 8  
ATOM   1946 O O   . LEU B 2 126 ? 28.321  31.387  -3.136  1.000 37.926  0 455 LEU BBB O   1 ? 8  
ATOM   1947 C CB  . LEU B 2 126 ? 25.854  32.966  -1.728  1.000 39.403  0 455 LEU BBB CB  1 ? 8  
ATOM   1948 C CG  . LEU B 2 126 ? 26.153  33.845  -2.941  1.000 42.106  0 455 LEU BBB CG  1 ? 8  
ATOM   1949 C CD1 . LEU B 2 126 ? 25.470  33.308  -4.190  1.000 42.790  0 455 LEU BBB CD1 1 ? 8  
ATOM   1950 C CD2 . LEU B 2 126 ? 25.720  35.281  -2.679  1.000 42.609  0 455 LEU BBB CD2 1 ? 8  
ATOM   1951 N N   . PHE B 2 127 ? 28.636  31.497  -0.867  1.000 40.731  0 456 PHE BBB N   1 ? 8  
ATOM   1952 C CA  . PHE B 2 127 ? 30.122  31.580  -0.850  1.000 41.199  0 456 PHE BBB CA  1 ? 8  
ATOM   1953 C C   . PHE B 2 127 ? 30.714  30.441  -0.015  1.000 42.775  0 456 PHE BBB C   1 ? 8  
ATOM   1954 O O   . PHE B 2 127 ? 30.208  30.148  1.082   1.000 44.954  0 456 PHE BBB O   1 ? 8  
ATOM   1955 C CB  . PHE B 2 127 ? 30.604  32.906  -0.257  1.000 41.481  0 456 PHE BBB CB  1 ? 8  
ATOM   1956 C CG  . PHE B 2 127 ? 30.229  34.141  -1.032  1.000 41.567  0 456 PHE BBB CG  1 ? 8  
ATOM   1957 C CD1 . PHE B 2 127 ? 30.908  34.484  -2.190  1.000 42.377  0 456 PHE BBB CD1 1 ? 8  
ATOM   1958 C CD2 . PHE B 2 127 ? 29.218  34.979  -0.586  1.000 41.484  0 456 PHE BBB CD2 1 ? 8  
ATOM   1959 C CE1 . PHE B 2 127 ? 30.570  35.629  -2.895  1.000 42.626  0 456 PHE BBB CE1 1 ? 8  
ATOM   1960 C CE2 . PHE B 2 127 ? 28.886  36.129  -1.288  1.000 41.766  0 456 PHE BBB CE2 1 ? 8  
ATOM   1961 C CZ  . PHE B 2 127 ? 29.560  36.448  -2.443  1.000 42.996  0 456 PHE BBB CZ  1 ? 8  
ATOM   1962 N N   . ARG B 2 128 ? 31.788  29.835  -0.520  1.000 44.626  0 457 ARG BBB N   1 ? 8  
ATOM   1963 C CA  . ARG B 2 128 ? 32.614  28.854  0.227   1.000 45.158  0 457 ARG BBB CA  1 ? 8  
ATOM   1964 C C   . ARG B 2 128 ? 34.003  28.770  -0.423  1.000 46.871  0 457 ARG BBB C   1 ? 8  
ATOM   1965 O O   . ARG B 2 128 ? 34.085  28.909  -1.646  1.000 45.781  0 457 ARG BBB O   1 ? 8  
ATOM   1966 C CB  . ARG B 2 128 ? 31.896  27.503  0.270   1.000 43.380  0 457 ARG BBB CB  1 ? 8  
ATOM   1967 C CG  . ARG B 2 128 ? 32.302  26.654  1.466   1.000 42.758  0 457 ARG BBB CG  1 ? 8  
ATOM   1968 C CD  . ARG B 2 128 ? 31.447  25.418  1.624   1.000 43.167  0 457 ARG BBB CD  1 ? 8  
ATOM   1969 N NE  . ARG B 2 128 ? 31.890  24.628  2.763   1.000 43.364  0 457 ARG BBB NE  1 ? 8  
ATOM   1970 C CZ  . ARG B 2 128 ? 32.787  23.650  2.711   1.000 44.711  0 457 ARG BBB CZ  1 ? 8  
ATOM   1971 N NH1 . ARG B 2 128 ? 33.352  23.314  1.564   1.000 45.444  0 457 ARG BBB NH1 1 ? 8  
ATOM   1972 N NH2 . ARG B 2 128 ? 33.110  22.998  3.813   1.000 45.660  0 457 ARG BBB NH2 1 ? 8  
ATOM   1973 N N   . LYS B 2 129 ? 35.043  28.525  0.380   1.000 51.136  0 458 LYS BBB N   1 ? 8  
ATOM   1974 C CA  . LYS B 2 129 ? 36.470  28.509  -0.047  1.000 53.951  0 458 LYS BBB CA  1 ? 8  
ATOM   1975 C C   . LYS B 2 129 ? 36.778  27.229  -0.837  1.000 54.142  0 458 LYS BBB C   1 ? 8  
ATOM   1976 O O   . LYS B 2 129 ? 37.834  27.194  -1.494  1.000 54.238  0 458 LYS BBB O   1 ? 8  
ATOM   1977 C CB  . LYS B 2 129 ? 37.393  28.609  1.169   1.000 56.209  0 458 LYS BBB CB  1 ? 8  
ATOM   1978 C CG  . LYS B 2 129 ? 37.209  29.861  2.012   1.000 59.234  0 458 LYS BBB CG  1 ? 8  
ATOM   1979 C CD  . LYS B 2 129 ? 37.758  31.121  1.368   1.000 61.795  0 458 LYS BBB CD  1 ? 8  
ATOM   1980 C CE  . LYS B 2 129 ? 37.593  32.344  2.248   1.000 63.390  0 458 LYS BBB CE  1 ? 8  
ATOM   1981 N NZ  . LYS B 2 129 ? 38.672  33.337  2.032   1.000 65.659  0 458 LYS BBB NZ  1 ? 8  
ATOM   1982 N N   . SER B 2 130 ? 35.917  26.209  -0.757  1.000 53.782  0 459 SER BBB N   1 ? 8  
ATOM   1983 C CA  . SER B 2 130 ? 36.052  24.943  -1.525  1.000 53.753  0 459 SER BBB CA  1 ? 8  
ATOM   1984 C C   . SER B 2 130 ? 34.706  24.215  -1.577  1.000 50.752  0 459 SER BBB C   1 ? 8  
ATOM   1985 O O   . SER B 2 130 ? 33.811  24.573  -0.799  1.000 49.779  0 459 SER BBB O   1 ? 8  
ATOM   1986 C CB  . SER B 2 130 ? 37.129  24.060  -0.943  1.000 54.989  0 459 SER BBB CB  1 ? 8  
ATOM   1987 O OG  . SER B 2 130 ? 36.725  23.527  0.308   1.000 55.121  0 459 SER BBB OG  1 ? 8  
ATOM   1988 N N   . ASN B 2 131 ? 34.587  23.228  -2.464  1.000 48.827  0 460 ASN BBB N   1 ? 8  
ATOM   1989 C CA  . ASN B 2 131 ? 33.357  22.417  -2.648  1.000 47.604  0 460 ASN BBB CA  1 ? 8  
ATOM   1990 C C   . ASN B 2 131 ? 33.216  21.434  -1.478  1.000 46.715  0 460 ASN BBB C   1 ? 8  
ATOM   1991 O O   . ASN B 2 131 ? 34.246  20.943  -0.987  1.000 46.926  0 460 ASN BBB O   1 ? 8  
ATOM   1992 C CB  . ASN B 2 131 ? 33.365  21.689  -3.994  1.000 48.683  0 460 ASN BBB CB  1 ? 8  
ATOM   1993 C CG  . ASN B 2 131 ? 33.345  22.634  -5.178  1.000 50.587  0 460 ASN BBB CG  1 ? 8  
ATOM   1994 O OD1 . ASN B 2 131 ? 32.999  23.807  -5.052  1.000 50.892  0 460 ASN BBB OD1 1 ? 8  
ATOM   1995 N ND2 . ASN B 2 131 ? 33.705  22.124  -6.342  1.000 53.691  0 460 ASN BBB ND2 1 ? 8  
ATOM   1996 N N   . LEU B 2 132 ? 31.981  21.174  -1.043  1.000 45.022  0 461 LEU BBB N   1 ? 8  
ATOM   1997 C CA  . LEU B 2 132 ? 31.655  20.127  -0.041  1.000 45.441  0 461 LEU BBB CA  1 ? 8  
ATOM   1998 C C   . LEU B 2 132 ? 32.114  18.772  -0.580  1.000 46.575  0 461 LEU BBB C   1 ? 8  
ATOM   1999 O O   . LEU B 2 132 ? 31.953  18.530  -1.787  1.000 49.630  0 461 LEU BBB O   1 ? 8  
ATOM   2000 C CB  . LEU B 2 132 ? 30.144  20.097  0.214   1.000 45.044  0 461 LEU BBB CB  1 ? 8  
ATOM   2001 C CG  . LEU B 2 132 ? 29.547  21.287  0.962   1.000 43.319  0 461 LEU BBB CG  1 ? 8  
ATOM   2002 C CD1 . LEU B 2 132 ? 28.032  21.157  1.027   1.000 41.774  0 461 LEU BBB CD1 1 ? 8  
ATOM   2003 C CD2 . LEU B 2 132 ? 30.126  21.412  2.361   1.000 44.586  0 461 LEU BBB CD2 1 ? 8  
ATOM   2004 N N   . LYS B 2 133 ? 32.640  17.917  0.295   1.000 47.662  0 462 LYS BBB N   1 ? 8  
ATOM   2005 C CA  . LYS B 2 133 ? 32.781  16.461  0.042   1.000 48.615  0 462 LYS BBB CA  1 ? 8  
ATOM   2006 C C   . LYS B 2 133 ? 31.384  15.846  0.093   1.000 46.795  0 462 LYS BBB C   1 ? 8  
ATOM   2007 O O   . LYS B 2 133 ? 30.469  16.439  0.663   1.000 44.928  0 462 LYS BBB O   1 ? 8  
ATOM   2008 C CB  . LYS B 2 133 ? 33.748  15.846  1.058   1.000 52.069  0 462 LYS BBB CB  1 ? 8  
ATOM   2009 C CG  . LYS B 2 133 ? 35.174  16.368  0.960   1.000 55.594  0 462 LYS BBB CG  1 ? 8  
ATOM   2010 C CD  . LYS B 2 133 ? 36.079  15.927  2.085   1.000 60.600  0 462 LYS BBB CD  1 ? 8  
ATOM   2011 C CE  . LYS B 2 133 ? 37.521  16.336  1.852   1.000 64.826  0 462 LYS BBB CE  1 ? 8  
ATOM   2012 N NZ  . LYS B 2 133 ? 38.415  15.858  2.935   1.000 68.659  0 462 LYS BBB NZ  1 ? 8  
ATOM   2013 N N   . PRO B 2 134 ? 31.155  14.662  -0.519  1.000 45.849  0 463 PRO BBB N   1 ? 8  
ATOM   2014 C CA  . PRO B 2 134 ? 29.843  14.018  -0.454  1.000 44.265  0 463 PRO BBB CA  1 ? 8  
ATOM   2015 C C   . PRO B 2 134 ? 29.305  13.927  0.983   1.000 43.295  0 463 PRO BBB C   1 ? 8  
ATOM   2016 O O   . PRO B 2 134 ? 30.031  13.519  1.860   1.000 42.877  0 463 PRO BBB O   1 ? 8  
ATOM   2017 C CB  . PRO B 2 134 ? 30.088  12.620  -1.044  1.000 44.933  0 463 PRO BBB CB  1 ? 8  
ATOM   2018 C CG  . PRO B 2 134 ? 31.281  12.808  -1.959  1.000 45.926  0 463 PRO BBB CG  1 ? 8  
ATOM   2019 C CD  . PRO B 2 134 ? 32.123  13.886  -1.309  1.000 46.176  0 463 PRO BBB CD  1 ? 8  
ATOM   2020 N N   . PHE B 2 135 ? 28.051  14.342  1.174   1.000 42.498  0 464 PHE BBB N   1 ? 8  
ATOM   2021 C CA  . PHE B 2 135 ? 27.270  14.250  2.436   1.000 42.328  0 464 PHE BBB CA  1 ? 8  
ATOM   2022 C C   . PHE B 2 135 ? 27.878  15.154  3.514   1.000 44.257  0 464 PHE BBB C   1 ? 8  
ATOM   2023 O O   . PHE B 2 135 ? 27.511  14.986  4.685   1.000 45.484  0 464 PHE BBB O   1 ? 8  
ATOM   2024 C CB  . PHE B 2 135 ? 27.151  12.796  2.905   1.000 42.033  0 464 PHE BBB CB  1 ? 8  
ATOM   2025 C CG  . PHE B 2 135 ? 26.316  11.903  2.017   1.000 41.894  0 464 PHE BBB CG  1 ? 8  
ATOM   2026 C CD1 . PHE B 2 135 ? 25.024  12.263  1.652   1.000 39.973  0 464 PHE BBB CD1 1 ? 8  
ATOM   2027 C CD2 . PHE B 2 135 ? 26.810  10.687  1.567   1.000 42.389  0 464 PHE BBB CD2 1 ? 8  
ATOM   2028 C CE1 . PHE B 2 135 ? 24.255  11.431  0.851   1.000 40.085  0 464 PHE BBB CE1 1 ? 8  
ATOM   2029 C CE2 . PHE B 2 135 ? 26.039  9.857   0.766   1.000 42.759  0 464 PHE BBB CE2 1 ? 8  
ATOM   2030 C CZ  . PHE B 2 135 ? 24.761  10.229  0.410   1.000 41.565  0 464 PHE BBB CZ  1 ? 8  
ATOM   2031 N N   . GLU B 2 136 ? 28.740  16.106  3.141   1.000 46.374  0 465 GLU BBB N   1 ? 8  
ATOM   2032 C CA  . GLU B 2 136 ? 29.302  17.109  4.088   1.000 47.747  0 465 GLU BBB CA  1 ? 8  
ATOM   2033 C C   . GLU B 2 136 ? 28.233  18.179  4.341   1.000 45.647  0 465 GLU BBB C   1 ? 8  
ATOM   2034 O O   . GLU B 2 136 ? 27.429  18.444  3.431   1.000 45.876  0 465 GLU BBB O   1 ? 8  
ATOM   2035 C CB  . GLU B 2 136 ? 30.604  17.703  3.543   1.000 49.120  0 465 GLU BBB CB  1 ? 8  
ATOM   2036 C CG  . GLU B 2 136 ? 31.445  18.426  4.581   1.000 49.813  0 465 GLU BBB CG  1 ? 8  
ATOM   2037 C CD  . GLU B 2 136 ? 32.696  19.101  4.031   1.000 52.762  0 465 GLU BBB CD  1 ? 8  
ATOM   2038 O OE1 . GLU B 2 136 ? 33.249  18.615  3.013   1.000 51.553  0 465 GLU BBB OE1 1 ? 8  
ATOM   2039 O OE2 . GLU B 2 136 ? 33.123  20.116  4.622   1.000 55.244  0 465 GLU BBB OE2 1 ? 8  
ATOM   2040 N N   . ARG B 2 137 ? 28.225  18.750  5.545   1.000 47.467  0 466 ARG BBB N   1 ? 8  
ATOM   2041 C CA  . ARG B 2 137 ? 27.256  19.778  6.010   1.000 46.298  0 466 ARG BBB CA  1 ? 8  
ATOM   2042 C C   . ARG B 2 137 ? 28.053  20.930  6.627   1.000 45.086  0 466 ARG BBB C   1 ? 8  
ATOM   2043 O O   . ARG B 2 137 ? 28.892  20.654  7.503   1.000 44.633  0 466 ARG BBB O   1 ? 8  
ATOM   2044 C CB  . ARG B 2 137 ? 26.298  19.155  7.026   1.000 47.089  0 466 ARG BBB CB  1 ? 8  
ATOM   2045 C CG  . ARG B 2 137 ? 25.151  20.049  7.470   1.000 49.307  0 466 ARG BBB CG  1 ? 8  
ATOM   2046 C CD  . ARG B 2 137 ? 24.165  19.195  8.252   1.000 52.002  0 466 ARG BBB CD  1 ? 8  
ATOM   2047 N NE  . ARG B 2 137 ? 23.060  19.929  8.852   1.000 54.004  0 466 ARG BBB NE  1 ? 8  
ATOM   2048 C CZ  . ARG B 2 137 ? 23.066  20.481  10.066  1.000 60.123  0 466 ARG BBB CZ  1 ? 8  
ATOM   2049 N NH1 . ARG B 2 137 ? 24.140  20.420  10.839  1.000 64.392  0 466 ARG BBB NH1 1 ? 8  
ATOM   2050 N NH2 . ARG B 2 137 ? 21.983  21.101  10.506  1.000 61.806  0 466 ARG BBB NH2 1 ? 8  
ATOM   2051 N N   . ASP B 2 138 ? 27.828  22.158  6.155   1.000 42.892  0 467 ASP BBB N   1 ? 8  
ATOM   2052 C CA  . ASP B 2 138 ? 28.520  23.383  6.636   1.000 41.977  0 467 ASP BBB CA  1 ? 8  
ATOM   2053 C C   . ASP B 2 138 ? 27.448  24.380  7.087   1.000 39.919  0 467 ASP BBB C   1 ? 8  
ATOM   2054 O O   . ASP B 2 138 ? 26.746  24.920  6.214   1.000 38.767  0 467 ASP BBB O   1 ? 8  
ATOM   2055 C CB  . ASP B 2 138 ? 29.438  23.947  5.546   1.000 41.910  0 467 ASP BBB CB  1 ? 8  
ATOM   2056 C CG  . ASP B 2 138 ? 30.189  25.212  5.932   1.000 41.298  0 467 ASP BBB CG  1 ? 8  
ATOM   2057 O OD1 . ASP B 2 138 ? 29.928  25.746  7.024   1.000 41.333  0 467 ASP BBB OD1 1 ? 8  
ATOM   2058 O OD2 . ASP B 2 138 ? 31.027  25.661  5.122   1.000 42.906  0 467 ASP BBB OD2 1 ? 8  
ATOM   2059 N N   . ILE B 2 139 ? 27.328  24.600  8.398   1.000 40.023  0 468 ILE BBB N   1 ? 8  
ATOM   2060 C CA  . ILE B 2 139 ? 26.341  25.543  9.007   1.000 40.764  0 468 ILE BBB CA  1 ? 8  
ATOM   2061 C C   . ILE B 2 139 ? 27.094  26.732  9.619   1.000 41.803  0 468 ILE BBB C   1 ? 8  
ATOM   2062 O O   . ILE B 2 139 ? 26.474  27.494  10.380  1.000 43.425  0 468 ILE BBB O   1 ? 8  
ATOM   2063 C CB  . ILE B 2 139 ? 25.449  24.831  10.043  1.000 40.255  0 468 ILE BBB CB  1 ? 8  
ATOM   2064 C CG1 . ILE B 2 139 ? 26.243  24.296  11.237  1.000 41.686  0 468 ILE BBB CG1 1 ? 8  
ATOM   2065 C CG2 . ILE B 2 139 ? 24.631  23.734  9.383   1.000 39.663  0 468 ILE BBB CG2 1 ? 8  
ATOM   2066 C CD1 . ILE B 2 139 ? 25.371  23.904  12.408  1.000 41.993  0 468 ILE BBB CD1 1 ? 8  
ATOM   2067 N N   . SER B 2 140 ? 28.379  26.898  9.294   1.000 41.996  0 469 SER BBB N   1 ? 8  
ATOM   2068 C CA  . SER B 2 140 ? 29.194  28.058  9.735   1.000 41.785  0 469 SER BBB CA  1 ? 8  
ATOM   2069 C C   . SER B 2 140 ? 28.586  29.333  9.140   1.000 40.904  0 469 SER BBB C   1 ? 8  
ATOM   2070 O O   . SER B 2 140 ? 28.004  29.259  8.042   1.000 38.240  0 469 SER BBB O   1 ? 8  
ATOM   2071 C CB  . SER B 2 140 ? 30.650  27.894  9.377   1.000 42.967  0 469 SER BBB CB  1 ? 8  
ATOM   2072 O OG  . SER B 2 140 ? 30.833  27.800  7.973   1.000 44.450  0 469 SER BBB OG  1 ? 8  
ATOM   2073 N N   . THR B 2 141 ? 28.685  30.443  9.872   1.000 41.947  0 470 THR BBB N   1 ? 8  
ATOM   2074 C CA  . THR B 2 141 ? 28.057  31.747  9.544   1.000 42.641  0 470 THR BBB CA  1 ? 8  
ATOM   2075 C C   . THR B 2 141 ? 29.102  32.861  9.667   1.000 44.360  0 470 THR BBB C   1 ? 8  
ATOM   2076 O O   . THR B 2 141 ? 28.706  34.021  9.893   1.000 45.982  0 470 THR BBB O   1 ? 8  
ATOM   2077 C CB  . THR B 2 141 ? 26.842  31.980  10.448  1.000 43.374  0 470 THR BBB CB  1 ? 8  
ATOM   2078 O OG1 . THR B 2 141 ? 27.284  31.907  11.807  1.000 46.709  0 470 THR BBB OG1 1 ? 8  
ATOM   2079 C CG2 . THR B 2 141 ? 25.734  30.979  10.209  1.000 42.663  0 470 THR BBB CG2 1 ? 8  
ATOM   2080 N N   . GLU B 2 142 ? 30.385  32.524  9.514   1.000 45.921  0 471 GLU BBB N   1 ? 8  
ATOM   2081 C CA  . GLU B 2 142 ? 31.500  33.503  9.548   1.000 47.908  0 471 GLU BBB CA  1 ? 8  
ATOM   2082 C C   . GLU B 2 142 ? 31.476  34.305  8.244   1.000 44.166  0 471 GLU BBB C   1 ? 8  
ATOM   2083 O O   . GLU B 2 142 ? 31.129  33.724  7.189   1.000 41.430  0 471 GLU BBB O   1 ? 8  
ATOM   2084 C CB  . GLU B 2 142 ? 32.842  32.800  9.756   1.000 53.848  0 471 GLU BBB CB  1 ? 8  
ATOM   2085 C CG  . GLU B 2 142 ? 32.946  32.067  11.085  1.000 64.326  0 471 GLU BBB CG  1 ? 8  
ATOM   2086 C CD  . GLU B 2 142 ? 33.088  32.931  12.333  1.000 71.894  0 471 GLU BBB CD  1 ? 8  
ATOM   2087 O OE1 . GLU B 2 142 ? 32.532  34.055  12.360  1.000 70.835  0 471 GLU BBB OE1 1 ? 8  
ATOM   2088 O OE2 . GLU B 2 142 ? 33.760  32.472  13.288  1.000 81.663  0 471 GLU BBB OE2 1 ? 8  
ATOM   2089 N N   . ILE B 2 143 ? 31.812  35.594  8.321   1.000 41.531  0 472 ILE BBB N   1 ? 8  
ATOM   2090 C CA  . ILE B 2 143 ? 31.947  36.483  7.133   1.000 40.128  0 472 ILE BBB CA  1 ? 8  
ATOM   2091 C C   . ILE B 2 143 ? 32.918  35.796  6.168   1.000 40.811  0 472 ILE BBB C   1 ? 8  
ATOM   2092 O O   . ILE B 2 143 ? 34.010  35.391  6.620   1.000 40.317  0 472 ILE BBB O   1 ? 8  
ATOM   2093 C CB  . ILE B 2 143 ? 32.423  37.899  7.513   1.000 38.928  0 472 ILE BBB CB  1 ? 8  
ATOM   2094 C CG1 . ILE B 2 143 ? 31.449  38.612  8.456   1.000 38.379  0 472 ILE BBB CG1 1 ? 8  
ATOM   2095 C CG2 . ILE B 2 143 ? 32.674  38.709  6.255   1.000 39.304  0 472 ILE BBB CG2 1 ? 8  
ATOM   2096 C CD1 . ILE B 2 143 ? 31.890  39.992  8.894   1.000 37.604  0 472 ILE BBB CD1 1 ? 8  
ATOM   2097 N N   . TYR B 2 144 ? 32.516  35.639  4.906   1.000 40.511  0 473 TYR BBB N   1 ? 8  
ATOM   2098 C CA  . TYR B 2 144 ? 33.379  35.133  3.812   1.000 42.260  0 473 TYR BBB CA  1 ? 8  
ATOM   2099 C C   . TYR B 2 144 ? 34.383  36.229  3.454   1.000 43.176  0 473 TYR BBB C   1 ? 8  
ATOM   2100 O O   . TYR B 2 144 ? 33.957  37.319  3.013   1.000 43.431  0 473 TYR BBB O   1 ? 8  
ATOM   2101 C CB  . TYR B 2 144 ? 32.559  34.733  2.587   1.000 42.586  0 473 TYR BBB CB  1 ? 8  
ATOM   2102 C CG  . TYR B 2 144 ? 33.368  34.080  1.499   1.000 44.143  0 473 TYR BBB CG  1 ? 8  
ATOM   2103 C CD1 . TYR B 2 144 ? 33.863  32.794  1.664   1.000 45.084  0 473 TYR BBB CD1 1 ? 8  
ATOM   2104 C CD2 . TYR B 2 144 ? 33.620  34.725  0.296   1.000 44.517  0 473 TYR BBB CD2 1 ? 8  
ATOM   2105 C CE1 . TYR B 2 144 ? 34.564  32.148  0.655   1.000 45.356  0 473 TYR BBB CE1 1 ? 8  
ATOM   2106 C CE2 . TYR B 2 144 ? 34.330  34.101  -0.716  1.000 43.581  0 473 TYR BBB CE2 1 ? 8  
ATOM   2107 C CZ  . TYR B 2 144 ? 34.808  32.813  -0.535  1.000 44.617  0 473 TYR BBB CZ  1 ? 8  
ATOM   2108 O OH  . TYR B 2 144 ? 35.532  32.219  -1.528  1.000 46.183  0 473 TYR BBB OH  1 ? 8  
ATOM   2109 N N   . GLN B 2 145 ? 35.669  35.957  3.691   1.000 44.335  0 474 GLN BBB N   1 ? 8  
ATOM   2110 C CA  . GLN B 2 145 ? 36.801  36.849  3.338   1.000 44.820  0 474 GLN BBB CA  1 ? 8  
ATOM   2111 C C   . GLN B 2 145 ? 37.233  36.505  1.907   1.000 46.157  0 474 GLN BBB C   1 ? 8  
ATOM   2112 O O   . GLN B 2 145 ? 37.951  35.502  1.732   1.000 45.856  0 474 GLN BBB O   1 ? 8  
ATOM   2113 C CB  . GLN B 2 145 ? 37.933  36.673  4.350   1.000 45.819  0 474 GLN BBB CB  1 ? 8  
ATOM   2114 C CG  . GLN B 2 145 ? 39.101  37.627  4.145   1.000 46.904  0 474 GLN BBB CG  1 ? 8  
ATOM   2115 C CD  . GLN B 2 145 ? 40.266  37.280  5.038   1.000 47.352  0 474 GLN BBB CD  1 ? 8  
ATOM   2116 O OE1 . GLN B 2 145 ? 40.093  36.697  6.104   1.000 46.050  0 474 GLN BBB OE1 1 ? 8  
ATOM   2117 N NE2 . GLN B 2 145 ? 41.468  37.618  4.596   1.000 48.456  0 474 GLN BBB NE2 1 ? 8  
ATOM   2118 N N   . ALA B 2 146 ? 36.785  37.296  0.927   1.000 45.701  0 475 ALA BBB N   1 ? 8  
ATOM   2119 C CA  . ALA B 2 146 ? 36.979  37.056  -0.521  1.000 47.766  0 475 ALA BBB CA  1 ? 8  
ATOM   2120 C C   . ALA B 2 146 ? 38.354  37.576  -0.964  1.000 49.704  0 475 ALA BBB C   1 ? 8  
ATOM   2121 O O   . ALA B 2 146 ? 38.828  37.128  -2.019  1.000 53.168  0 475 ALA BBB O   1 ? 8  
ATOM   2122 C CB  . ALA B 2 146 ? 35.862  37.716  -1.294  1.000 48.019  0 475 ALA BBB CB  1 ? 8  
ATOM   2123 N N   . GLY B 2 147 ? 38.956  38.488  -0.192  1.000 49.578  0 476 GLY BBB N   1 ? 8  
ATOM   2124 C CA  . GLY B 2 147 ? 40.266  39.109  -0.479  1.000 49.517  0 476 GLY BBB CA  1 ? 8  
ATOM   2125 C C   . GLY B 2 147 ? 41.309  38.744  0.564   1.000 48.678  0 476 GLY BBB C   1 ? 8  
ATOM   2126 O O   . GLY B 2 147 ? 41.073  37.792  1.322   1.000 49.841  0 476 GLY BBB O   1 ? 8  
ATOM   2127 N N   . SER B 2 148 ? 42.424  39.476  0.595   1.000 48.519  0 477 SER BBB N   1 ? 8  
ATOM   2128 C CA  . SER B 2 148 ? 43.611  39.205  1.451   1.000 50.076  0 477 SER BBB CA  1 ? 8  
ATOM   2129 C C   . SER B 2 148 ? 43.469  39.918  2.801   1.000 48.625  0 477 SER BBB C   1 ? 8  
ATOM   2130 O O   . SER B 2 148 ? 44.103  39.467  3.777   1.000 47.623  0 477 SER BBB O   1 ? 8  
ATOM   2131 C CB  . SER B 2 148 ? 44.880  39.623  0.754   1.000 51.995  0 477 SER BBB CB  1 ? 8  
ATOM   2132 O OG  . SER B 2 148 ? 44.776  40.958  0.274   1.000 51.653  0 477 SER BBB OG  1 ? 8  
ATOM   2133 N N   . THR B 2 149 ? 42.679  40.999  2.838   1.000 47.672  0 478 THR BBB N   1 ? 8  
ATOM   2134 C CA  . THR B 2 149 ? 42.412  41.833  4.039   1.000 47.117  0 478 THR BBB CA  1 ? 8  
ATOM   2135 C C   . THR B 2 149 ? 41.415  41.098  4.933   1.000 45.179  0 478 THR BBB C   1 ? 8  
ATOM   2136 O O   . THR B 2 149 ? 40.358  40.687  4.461   1.000 42.921  0 478 THR BBB O   1 ? 8  
ATOM   2137 C CB  . THR B 2 149 ? 41.926  43.227  3.624   1.000 47.360  0 478 THR BBB CB  1 ? 8  
ATOM   2138 O OG1 . THR B 2 149 ? 43.008  43.851  2.930   1.000 47.707  0 478 THR BBB OG1 1 ? 8  
ATOM   2139 C CG2 . THR B 2 149 ? 41.502  44.096  4.789   1.000 48.006  0 478 THR BBB CG2 1 ? 8  
ATOM   2140 N N   . PRO B 2 150 ? 41.721  40.895  6.239   1.000 44.823  0 479 PRO BBB N   1 ? 8  
ATOM   2141 C CA  . PRO B 2 150 ? 40.764  40.313  7.181   1.000 44.549  0 479 PRO BBB CA  1 ? 8  
ATOM   2142 C C   . PRO B 2 150 ? 39.536  41.213  7.366   1.000 42.677  0 479 PRO BBB C   1 ? 8  
ATOM   2143 O O   . PRO B 2 150 ? 39.676  42.418  7.257   1.000 41.988  0 479 PRO BBB O   1 ? 8  
ATOM   2144 C CB  . PRO B 2 150 ? 41.532  40.204  8.510   1.000 44.909  0 479 PRO BBB CB  1 ? 8  
ATOM   2145 C CG  . PRO B 2 150 ? 42.983  40.306  8.113   1.000 46.347  0 479 PRO BBB CG  1 ? 8  
ATOM   2146 C CD  . PRO B 2 150 ? 43.004  41.195  6.887   1.000 45.836  0 479 PRO BBB CD  1 ? 8  
ATOM   2147 N N   . CYS B 2 151 ? 38.387  40.604  7.663   1.000 42.996  0 480 CYS BBB N   1 ? 8  
ATOM   2148 C CA  . CYS B 2 151 ? 37.079  41.289  7.829   1.000 43.427  0 480 CYS BBB CA  1 ? 8  
ATOM   2149 C C   . CYS B 2 151 ? 36.899  41.784  9.275   1.000 43.976  0 480 CYS BBB C   1 ? 8  
ATOM   2150 O O   . CYS B 2 151 ? 36.278  42.848  9.447   1.000 43.549  0 480 CYS BBB O   1 ? 8  
ATOM   2151 C CB  . CYS B 2 151 ? 35.946  40.364  7.404   1.000 44.107  0 480 CYS BBB CB  1 ? 8  
ATOM   2152 S SG  . CYS B 2 151 ? 36.118  39.776  5.695   1.000 44.952  0 480 CYS BBB SG  1 ? 8  
ATOM   2153 N N   . ASN B 2 152 ? 37.436  41.067  10.270  1.000 45.026  0 481 ASN BBB N   1 ? 8  
ATOM   2154 C CA  . ASN B 2 152 ? 37.352  41.427  11.715  1.000 46.443  0 481 ASN BBB CA  1 ? 8  
ATOM   2155 C C   . ASN B 2 152 ? 35.895  41.727  12.106  1.000 43.524  0 481 ASN BBB C   1 ? 8  
ATOM   2156 O O   . ASN B 2 152 ? 35.657  42.741  12.791  1.000 41.914  0 481 ASN BBB O   1 ? 8  
ATOM   2157 C CB  . ASN B 2 152 ? 38.269  42.605  12.059  1.000 48.888  0 481 ASN BBB CB  1 ? 8  
ATOM   2158 C CG  . ASN B 2 152 ? 39.739  42.262  11.953  1.000 52.572  0 481 ASN BBB CG  1 ? 8  
ATOM   2159 O OD1 . ASN B 2 152 ? 40.150  41.140  12.238  1.000 56.599  0 481 ASN BBB OD1 1 ? 8  
ATOM   2160 N ND2 . ASN B 2 152 ? 40.545  43.227  11.545  1.000 54.531  0 481 ASN BBB ND2 1 ? 8  
ATOM   2161 N N   . GLY B 2 153 ? 34.958  40.878  11.675  1.000 42.854  0 482 GLY BBB N   1 ? 8  
ATOM   2162 C CA  . GLY B 2 153 ? 33.528  40.950  12.033  1.000 43.102  0 482 GLY BBB CA  1 ? 8  
ATOM   2163 C C   . GLY B 2 153 ? 32.787  42.100  11.363  1.000 42.767  0 482 GLY BBB C   1 ? 8  
ATOM   2164 O O   . GLY B 2 153 ? 31.664  42.389  11.790  1.000 42.951  0 482 GLY BBB O   1 ? 8  
ATOM   2165 N N   . VAL B 2 154 ? 33.365  42.734  10.340  1.000 42.987  0 483 VAL BBB N   1 ? 8  
ATOM   2166 C CA  . VAL B 2 154 ? 32.698  43.844  9.594   1.000 42.182  0 483 VAL BBB CA  1 ? 8  
ATOM   2167 C C   . VAL B 2 154 ? 32.590  43.462  8.115   1.000 41.714  0 483 VAL BBB C   1 ? 8  
ATOM   2168 O O   . VAL B 2 154 ? 33.619  43.121  7.503   1.000 43.636  0 483 VAL BBB O   1 ? 8  
ATOM   2169 C CB  . VAL B 2 154 ? 33.427  45.189  9.771   1.000 42.651  0 483 VAL BBB CB  1 ? 8  
ATOM   2170 C CG1 . VAL B 2 154 ? 32.721  46.296  8.992   1.000 41.809  0 483 VAL BBB CG1 1 ? 8  
ATOM   2171 C CG2 . VAL B 2 154 ? 33.578  45.563  11.246  1.000 42.511  0 483 VAL BBB CG2 1 ? 8  
ATOM   2172 N N   . GLU B 2 155 ? 31.377  43.517  7.564   1.000 41.197  0 484 GLU BBB N   1 ? 8  
ATOM   2173 C CA  . GLU B 2 155 ? 31.118  43.294  6.120   1.000 39.072  0 484 GLU BBB CA  1 ? 8  
ATOM   2174 C C   . GLU B 2 155 ? 31.492  44.574  5.370   1.000 38.086  0 484 GLU BBB C   1 ? 8  
ATOM   2175 O O   . GLU B 2 155 ? 31.379  45.663  5.963   1.000 37.514  0 484 GLU BBB O   1 ? 8  
ATOM   2176 C CB  . GLU B 2 155 ? 29.663  42.897  5.881   1.000 39.102  0 484 GLU BBB CB  1 ? 8  
ATOM   2177 C CG  . GLU B 2 155 ? 29.265  41.597  6.564   1.000 39.632  0 484 GLU BBB CG  1 ? 8  
ATOM   2178 C CD  . GLU B 2 155 ? 27.801  41.217  6.397   1.000 40.409  0 484 GLU BBB CD  1 ? 8  
ATOM   2179 O OE1 . GLU B 2 155 ? 27.179  41.657  5.400   1.000 39.233  0 484 GLU BBB OE1 1 ? 8  
ATOM   2180 O OE2 . GLU B 2 155 ? 27.279  40.497  7.272   1.000 40.763  0 484 GLU BBB OE2 1 ? 8  
ATOM   2181 N N   . GLY B 2 156 ? 31.923  44.422  4.117   1.000 37.822  0 485 GLY BBB N   1 ? 8  
ATOM   2182 C CA  . GLY B 2 156 ? 32.428  45.503  3.252   1.000 38.101  0 485 GLY BBB CA  1 ? 8  
ATOM   2183 C C   . GLY B 2 156 ? 33.023  44.919  1.991   1.000 38.519  0 485 GLY BBB C   1 ? 8  
ATOM   2184 O O   . GLY B 2 156 ? 32.665  43.775  1.651   1.000 38.868  0 485 GLY BBB O   1 ? 8  
ATOM   2185 N N   . PHE B 2 157 ? 33.917  45.649  1.328   1.000 41.325  0 486 PHE BBB N   1 ? 8  
ATOM   2186 C CA  . PHE B 2 157 ? 34.653  45.151  0.136   1.000 42.064  0 486 PHE BBB CA  1 ? 8  
ATOM   2187 C C   . PHE B 2 157 ? 35.269  43.790  0.472   1.000 41.444  0 486 PHE BBB C   1 ? 8  
ATOM   2188 O O   . PHE B 2 157 ? 35.940  43.687  1.509   1.000 42.456  0 486 PHE BBB O   1 ? 8  
ATOM   2189 C CB  . PHE B 2 157 ? 35.732  46.133  -0.319  1.000 43.130  0 486 PHE BBB CB  1 ? 8  
ATOM   2190 C CG  . PHE B 2 157 ? 36.423  45.710  -1.591  1.000 46.145  0 486 PHE BBB CG  1 ? 8  
ATOM   2191 C CD1 . PHE B 2 157 ? 35.745  45.728  -2.801  1.000 46.168  0 486 PHE BBB CD1 1 ? 8  
ATOM   2192 C CD2 . PHE B 2 157 ? 37.738  45.265  -1.577  1.000 46.953  0 486 PHE BBB CD2 1 ? 8  
ATOM   2193 C CE1 . PHE B 2 157 ? 36.374  45.333  -3.972  1.000 47.957  0 486 PHE BBB CE1 1 ? 8  
ATOM   2194 C CE2 . PHE B 2 157 ? 38.363  44.870  -2.749  1.000 47.914  0 486 PHE BBB CE2 1 ? 8  
ATOM   2195 C CZ  . PHE B 2 157 ? 37.680  44.899  -3.943  1.000 48.128  0 486 PHE BBB CZ  1 ? 8  
ATOM   2196 N N   . ASN B 2 158 ? 35.001  42.780  -0.361  1.000 42.309  0 487 ASN BBB N   1 ? 8  
ATOM   2197 C CA  . ASN B 2 158 ? 35.550  41.401  -0.254  1.000 42.971  0 487 ASN BBB CA  1 ? 8  
ATOM   2198 C C   . ASN B 2 158 ? 35.249  40.792  1.126   1.000 42.648  0 487 ASN BBB C   1 ? 8  
ATOM   2199 O O   . ASN B 2 158 ? 35.995  39.885  1.539   1.000 43.573  0 487 ASN BBB O   1 ? 8  
ATOM   2200 C CB  . ASN B 2 158 ? 37.051  41.396  -0.550  1.000 45.394  0 487 ASN BBB CB  1 ? 8  
ATOM   2201 C CG  . ASN B 2 158 ? 37.376  41.230  -2.017  1.000 47.142  0 487 ASN BBB CG  1 ? 8  
ATOM   2202 O OD1 . ASN B 2 158 ? 36.610  40.632  -2.773  1.000 46.457  0 487 ASN BBB OD1 1 ? 8  
ATOM   2203 N ND2 . ASN B 2 158 ? 38.529  41.733  -2.415  1.000 49.876  0 487 ASN BBB ND2 1 ? 8  
ATOM   2204 N N   . CYS B 2 159 ? 34.184  41.246  1.797   1.000 42.721  0 488 CYS BBB N   1 ? 8  
ATOM   2205 C CA  . CYS B 2 159 ? 33.750  40.769  3.139   1.000 42.050  0 488 CYS BBB CA  1 ? 8  
ATOM   2206 C C   . CYS B 2 159 ? 32.223  40.658  3.156   1.000 41.328  0 488 CYS BBB C   1 ? 8  
ATOM   2207 O O   . CYS B 2 159 ? 31.550  41.663  3.459   1.000 42.468  0 488 CYS BBB O   1 ? 8  
ATOM   2208 C CB  . CYS B 2 159 ? 34.263  41.690  4.240   1.000 42.785  0 488 CYS BBB CB  1 ? 8  
ATOM   2209 S SG  . CYS B 2 159 ? 36.031  41.481  4.569   1.000 43.425  0 488 CYS BBB SG  1 ? 8  
ATOM   2210 N N   . TYR B 2 160 ? 31.710  39.473  2.820   1.000 40.267  0 489 TYR BBB N   1 ? 8  
ATOM   2211 C CA  . TYR B 2 160 ? 30.282  39.219  2.504   1.000 38.526  0 489 TYR BBB CA  1 ? 8  
ATOM   2212 C C   . TYR B 2 160 ? 29.737  38.142  3.445   1.000 38.325  0 489 TYR BBB C   1 ? 8  
ATOM   2213 O O   . TYR B 2 160 ? 30.505  37.240  3.814   1.000 37.457  0 489 TYR BBB O   1 ? 8  
ATOM   2214 C CB  . TYR B 2 160 ? 30.149  38.819  1.032   1.000 37.413  0 489 TYR BBB CB  1 ? 8  
ATOM   2215 C CG  . TYR B 2 160 ? 30.779  39.812  0.089   1.000 37.063  0 489 TYR BBB CG  1 ? 8  
ATOM   2216 C CD1 . TYR B 2 160 ? 30.333  41.124  0.041   1.000 36.285  0 489 TYR BBB CD1 1 ? 8  
ATOM   2217 C CD2 . TYR B 2 160 ? 31.842  39.456  -0.728  1.000 37.851  0 489 TYR BBB CD2 1 ? 8  
ATOM   2218 C CE1 . TYR B 2 160 ? 30.919  42.056  -0.797  1.000 37.475  0 489 TYR BBB CE1 1 ? 8  
ATOM   2219 C CE2 . TYR B 2 160 ? 32.438  40.375  -1.579  1.000 38.144  0 489 TYR BBB CE2 1 ? 8  
ATOM   2220 C CZ  . TYR B 2 160 ? 31.972  41.679  -1.615  1.000 38.739  0 489 TYR BBB CZ  1 ? 8  
ATOM   2221 O OH  . TYR B 2 160 ? 32.546  42.596  -2.443  1.000 39.537  0 489 TYR BBB OH  1 ? 8  
ATOM   2222 N N   . PHE B 2 161 ? 28.457  38.244  3.820   1.000 38.078  0 490 PHE BBB N   1 ? 8  
ATOM   2223 C CA  . PHE B 2 161 ? 27.735  37.187  4.572   1.000 38.126  0 490 PHE BBB CA  1 ? 8  
ATOM   2224 C C   . PHE B 2 161 ? 27.600  35.980  3.648   1.000 37.717  0 490 PHE BBB C   1 ? 8  
ATOM   2225 O O   . PHE B 2 161 ? 27.249  36.137  2.483   1.000 36.208  0 490 PHE BBB O   1 ? 8  
ATOM   2226 C CB  . PHE B 2 161 ? 26.391  37.699  5.101   1.000 38.689  0 490 PHE BBB CB  1 ? 8  
ATOM   2227 C CG  . PHE B 2 161 ? 25.821  36.868  6.223   1.000 39.004  0 490 PHE BBB CG  1 ? 8  
ATOM   2228 C CD1 . PHE B 2 161 ? 26.455  36.810  7.456   1.000 39.630  0 490 PHE BBB CD1 1 ? 8  
ATOM   2229 C CD2 . PHE B 2 161 ? 24.666  36.126  6.043   1.000 38.725  0 490 PHE BBB CD2 1 ? 8  
ATOM   2230 C CE1 . PHE B 2 161 ? 25.937  36.042  8.488   1.000 40.457  0 490 PHE BBB CE1 1 ? 8  
ATOM   2231 C CE2 . PHE B 2 161 ? 24.144  35.363  7.077   1.000 38.846  0 490 PHE BBB CE2 1 ? 8  
ATOM   2232 C CZ  . PHE B 2 161 ? 24.782  35.319  8.295   1.000 40.779  0 490 PHE BBB CZ  1 ? 8  
ATOM   2233 N N   . PRO B 2 162 ? 27.927  34.751  4.108   1.000 38.030  0 491 PRO BBB N   1 ? 8  
ATOM   2234 C CA  . PRO B 2 162 ? 27.947  33.579  3.231   1.000 38.186  0 491 PRO BBB CA  1 ? 8  
ATOM   2235 C C   . PRO B 2 162 ? 26.566  33.010  2.870   1.000 39.132  0 491 PRO BBB C   1 ? 8  
ATOM   2236 O O   . PRO B 2 162 ? 26.501  32.190  1.967   1.000 42.120  0 491 PRO BBB O   1 ? 8  
ATOM   2237 C CB  . PRO B 2 162 ? 28.740  32.551  4.055   1.000 37.717  0 491 PRO BBB CB  1 ? 8  
ATOM   2238 C CG  . PRO B 2 162 ? 28.417  32.907  5.483   1.000 37.806  0 491 PRO BBB CG  1 ? 8  
ATOM   2239 C CD  . PRO B 2 162 ? 28.328  34.422  5.485   1.000 37.893  0 491 PRO BBB CD  1 ? 8  
ATOM   2240 N N   . LEU B 2 163 ? 25.506  33.422  3.573   1.000 40.118  0 492 LEU BBB N   1 ? 8  
ATOM   2241 C CA  . LEU B 2 163 ? 24.134  32.877  3.372   1.000 41.036  0 492 LEU BBB CA  1 ? 8  
ATOM   2242 C C   . LEU B 2 163 ? 23.253  33.907  2.660   1.000 40.836  0 492 LEU BBB C   1 ? 8  
ATOM   2243 O O   . LEU B 2 163 ? 23.544  35.116  2.738   1.000 41.165  0 492 LEU BBB O   1 ? 8  
ATOM   2244 C CB  . LEU B 2 163 ? 23.535  32.468  4.719   1.000 41.237  0 492 LEU BBB CB  1 ? 8  
ATOM   2245 C CG  . LEU B 2 163 ? 24.295  31.369  5.457   1.000 42.860  0 492 LEU BBB CG  1 ? 8  
ATOM   2246 C CD1 . LEU B 2 163 ? 23.568  30.978  6.732   1.000 43.880  0 492 LEU BBB CD1 1 ? 8  
ATOM   2247 C CD2 . LEU B 2 163 ? 24.510  30.159  4.561   1.000 42.870  0 492 LEU BBB CD2 1 ? 8  
ATOM   2248 N N   . GLN B 2 164 ? 22.211  33.417  1.990   1.000 40.689  0 493 GLN BBB N   1 ? 8  
ATOM   2249 C CA  . GLN B 2 164 ? 21.283  34.217  1.148   1.000 41.714  0 493 GLN BBB CA  1 ? 8  
ATOM   2250 C C   . GLN B 2 164 ? 19.908  33.538  1.191   1.000 39.568  0 493 GLN BBB C   1 ? 8  
ATOM   2251 O O   . GLN B 2 164 ? 19.866  32.293  1.107   1.000 37.598  0 493 GLN BBB O   1 ? 8  
ATOM   2252 C CB  . GLN B 2 164 ? 21.868  34.323  -0.264  1.000 43.329  0 493 GLN BBB CB  1 ? 8  
ATOM   2253 C CG  . GLN B 2 164 ? 20.952  34.970  -1.291  1.000 46.043  0 493 GLN BBB CG  1 ? 8  
ATOM   2254 C CD  . GLN B 2 164 ? 21.013  36.477  -1.322  1.000 48.938  0 493 GLN BBB CD  1 ? 8  
ATOM   2255 O OE1 . GLN B 2 164 ? 22.075  37.086  -1.243  1.000 44.213  0 493 GLN BBB OE1 1 ? 8  
ATOM   2256 N NE2 . GLN B 2 164 ? 19.853  37.095  -1.485  1.000 56.604  0 493 GLN BBB NE2 1 ? 8  
ATOM   2257 N N   . SER B 2 165 ? 18.836  34.324  1.342   1.000 39.367  0 494 SER BBB N   1 ? 8  
ATOM   2258 C CA  . SER B 2 165 ? 17.424  33.856  1.272   1.000 39.346  0 494 SER BBB CA  1 ? 8  
ATOM   2259 C C   . SER B 2 165 ? 17.073  33.513  -0.177  1.000 38.817  0 494 SER BBB C   1 ? 8  
ATOM   2260 O O   . SER B 2 165 ? 17.462  34.288  -1.063  1.000 40.869  0 494 SER BBB O   1 ? 8  
ATOM   2261 C CB  . SER B 2 165 ? 16.459  34.897  1.809   1.000 38.905  0 494 SER BBB CB  1 ? 8  
ATOM   2262 O OG  . SER B 2 165 ? 16.622  35.091  3.202   1.000 39.511  0 494 SER BBB OG  1 ? 8  
ATOM   2263 N N   . TYR B 2 166 ? 16.355  32.408  -0.398  1.000 39.334  0 495 TYR BBB N   1 ? 8  
ATOM   2264 C CA  . TYR B 2 166 ? 15.417  32.254  -1.540  1.000 40.271  0 495 TYR BBB CA  1 ? 8  
ATOM   2265 C C   . TYR B 2 166 ? 14.275  33.252  -1.334  1.000 41.703  0 495 TYR BBB C   1 ? 8  
ATOM   2266 O O   . TYR B 2 166 ? 13.914  33.515  -0.162  1.000 41.584  0 495 TYR BBB O   1 ? 8  
ATOM   2267 C CB  . TYR B 2 166 ? 14.826  30.844  -1.626  1.000 40.652  0 495 TYR BBB CB  1 ? 8  
ATOM   2268 C CG  . TYR B 2 166 ? 15.798  29.750  -1.981  1.000 40.835  0 495 TYR BBB CG  1 ? 8  
ATOM   2269 C CD1 . TYR B 2 166 ? 16.259  29.586  -3.280  1.000 40.424  0 495 TYR BBB CD1 1 ? 8  
ATOM   2270 C CD2 . TYR B 2 166 ? 16.240  28.860  -1.016  1.000 40.946  0 495 TYR BBB CD2 1 ? 8  
ATOM   2271 C CE1 . TYR B 2 166 ? 17.154  28.578  -3.607  1.000 40.650  0 495 TYR BBB CE1 1 ? 8  
ATOM   2272 C CE2 . TYR B 2 166 ? 17.137  27.850  -1.324  1.000 40.508  0 495 TYR BBB CE2 1 ? 8  
ATOM   2273 C CZ  . TYR B 2 166 ? 17.593  27.708  -2.623  1.000 40.403  0 495 TYR BBB CZ  1 ? 8  
ATOM   2274 O OH  . TYR B 2 166 ? 18.469  26.708  -2.920  1.000 42.114  0 495 TYR BBB OH  1 ? 8  
ATOM   2275 N N   . GLY B 2 167 ? 13.725  33.784  -2.427  1.000 43.271  0 496 GLY BBB N   1 ? 8  
ATOM   2276 C CA  . GLY B 2 167 ? 12.531  34.648  -2.408  1.000 43.951  0 496 GLY BBB CA  1 ? 8  
ATOM   2277 C C   . GLY B 2 167 ? 11.330  33.906  -2.956  1.000 44.357  0 496 GLY BBB C   1 ? 8  
ATOM   2278 O O   . GLY B 2 167 ? 10.986  34.130  -4.126  1.000 44.681  0 496 GLY BBB O   1 ? 8  
ATOM   2279 N N   . PHE B 2 168 ? 10.730  33.025  -2.153  1.000 44.809  0 497 PHE BBB N   1 ? 8  
ATOM   2280 C CA  . PHE B 2 168 ? 9.585   32.180  -2.576  1.000 45.580  0 497 PHE BBB CA  1 ? 8  
ATOM   2281 C C   . PHE B 2 168 ? 8.298   32.997  -2.481  1.000 49.282  0 497 PHE BBB C   1 ? 8  
ATOM   2282 O O   . PHE B 2 168 ? 7.810   33.240  -1.355  1.000 51.004  0 497 PHE BBB O   1 ? 8  
ATOM   2283 C CB  . PHE B 2 168 ? 9.519   30.889  -1.760  1.000 44.365  0 497 PHE BBB CB  1 ? 8  
ATOM   2284 C CG  . PHE B 2 168 ? 10.670  29.949  -2.006  1.000 43.064  0 497 PHE BBB CG  1 ? 8  
ATOM   2285 C CD1 . PHE B 2 168 ? 11.074  29.641  -3.299  1.000 44.138  0 497 PHE BBB CD1 1 ? 8  
ATOM   2286 C CD2 . PHE B 2 168 ? 11.340  29.361  -0.946  1.000 40.833  0 497 PHE BBB CD2 1 ? 8  
ATOM   2287 C CE1 . PHE B 2 168 ? 12.131  28.773  -3.527  1.000 43.022  0 497 PHE BBB CE1 1 ? 8  
ATOM   2288 C CE2 . PHE B 2 168 ? 12.392  28.490  -1.174  1.000 41.267  0 497 PHE BBB CE2 1 ? 8  
ATOM   2289 C CZ  . PHE B 2 168 ? 12.787  28.198  -2.462  1.000 42.372  0 497 PHE BBB CZ  1 ? 8  
ATOM   2290 N N   . GLN B 2 169 ? 7.785   33.411  -3.644  1.000 51.674  0 498 GLN BBB N   1 ? 8  
ATOM   2291 C CA  . GLN B 2 169 ? 6.468   34.079  -3.816  1.000 55.223  0 498 GLN BBB CA  1 ? 8  
ATOM   2292 C C   . GLN B 2 169 ? 5.594   33.181  -4.686  1.000 54.735  0 498 GLN BBB C   1 ? 8  
ATOM   2293 O O   . GLN B 2 169 ? 6.109   32.467  -5.546  1.000 54.150  0 498 GLN BBB O   1 ? 8  
ATOM   2294 C CB  . GLN B 2 169 ? 6.664   35.470  -4.422  1.000 58.067  0 498 GLN BBB CB  1 ? 8  
ATOM   2295 C CG  . GLN B 2 169 ? 7.699   36.293  -3.669  1.000 60.050  0 498 GLN BBB CG  1 ? 8  
ATOM   2296 C CD  . GLN B 2 169 ? 7.619   37.778  -3.910  1.000 64.187  0 498 GLN BBB CD  1 ? 8  
ATOM   2297 O OE1 . GLN B 2 169 ? 6.995   38.241  -4.862  1.000 69.601  0 498 GLN BBB OE1 1 ? 8  
ATOM   2298 N NE2 . GLN B 2 169 ? 8.265   38.536  -3.037  1.000 64.770  0 498 GLN BBB NE2 1 ? 8  
ATOM   2299 N N   . PRO B 2 170 ? 4.255   33.173  -4.485  1.000 54.823  0 499 PRO BBB N   1 ? 8  
ATOM   2300 C CA  . PRO B 2 170 ? 3.365   32.295  -5.251  1.000 55.359  0 499 PRO BBB CA  1 ? 8  
ATOM   2301 C C   . PRO B 2 170 ? 3.478   32.480  -6.773  1.000 54.871  0 499 PRO BBB C   1 ? 8  
ATOM   2302 O O   . PRO B 2 170 ? 3.387   31.499  -7.477  1.000 52.637  0 499 PRO BBB O   1 ? 8  
ATOM   2303 C CB  . PRO B 2 170 ? 1.952   32.692  -4.790  1.000 56.380  0 499 PRO BBB CB  1 ? 8  
ATOM   2304 C CG  . PRO B 2 170 ? 2.156   33.356  -3.445  1.000 56.491  0 499 PRO BBB CG  1 ? 8  
ATOM   2305 C CD  . PRO B 2 170 ? 3.527   33.997  -3.507  1.000 55.408  0 499 PRO BBB CD  1 ? 8  
ATOM   2306 N N   . THR B 2 171 ? 3.695   33.727  -7.213  1.000 56.964  0 500 THR BBB N   1 ? 8  
ATOM   2307 C CA  . THR B 2 171 ? 3.700   34.196  -8.625  1.000 59.704  0 500 THR BBB CA  1 ? 8  
ATOM   2308 C C   . THR B 2 171 ? 5.042   33.907  -9.317  1.000 58.690  0 500 THR BBB C   1 ? 8  
ATOM   2309 O O   . THR B 2 171 ? 5.153   34.226  -10.514 1.000 60.694  0 500 THR BBB O   1 ? 8  
ATOM   2310 C CB  . THR B 2 171 ? 3.363   35.695  -8.655  1.000 63.363  0 500 THR BBB CB  1 ? 8  
ATOM   2311 O OG1 . THR B 2 171 ? 2.028   35.820  -8.165  1.000 68.057  0 500 THR BBB OG1 1 ? 8  
ATOM   2312 C CG2 . THR B 2 171 ? 3.446   36.334  -10.024 1.000 66.713  0 500 THR BBB CG2 1 ? 8  
ATOM   2313 N N   . ASN B 2 172 ? 6.024   33.337  -8.607  1.000 55.557  0 501 ASN BBB N   1 ? 8  
ATOM   2314 C CA  . ASN B 2 172 ? 7.322   32.900  -9.187  1.000 52.753  0 501 ASN BBB CA  1 ? 8  
ATOM   2315 C C   . ASN B 2 172 ? 7.073   31.937  -10.358 1.000 51.119  0 501 ASN BBB C   1 ? 8  
ATOM   2316 O O   . ASN B 2 172 ? 6.087   31.176  -10.303 1.000 48.034  0 501 ASN BBB O   1 ? 8  
ATOM   2317 C CB  . ASN B 2 172 ? 8.212   32.206  -8.151  1.000 50.423  0 501 ASN BBB CB  1 ? 8  
ATOM   2318 C CG  . ASN B 2 172 ? 8.936   33.157  -7.219  1.000 51.240  0 501 ASN BBB CG  1 ? 8  
ATOM   2319 O OD1 . ASN B 2 172 ? 8.774   34.372  -7.295  1.000 53.307  0 501 ASN BBB OD1 1 ? 8  
ATOM   2320 N ND2 . ASN B 2 172 ? 9.743   32.609  -6.325  1.000 49.885  0 501 ASN BBB ND2 1 ? 8  
ATOM   2321 N N   . GLY B 2 173 ? 7.958   31.950  -11.360 1.000 50.435  0 502 GLY BBB N   1 ? 8  
ATOM   2322 C CA  . GLY B 2 173 ? 8.080   30.868  -12.357 1.000 50.712  0 502 GLY BBB CA  1 ? 8  
ATOM   2323 C C   . GLY B 2 173 ? 8.476   29.565  -11.682 1.000 49.413  0 502 GLY BBB C   1 ? 8  
ATOM   2324 O O   . GLY B 2 173 ? 9.131   29.630  -10.620 1.000 48.920  0 502 GLY BBB O   1 ? 8  
ATOM   2325 N N   . VAL B 2 174 ? 8.107   28.423  -12.270 1.000 49.713  0 503 VAL BBB N   1 ? 8  
ATOM   2326 C CA  . VAL B 2 174 ? 8.262   27.068  -11.659 1.000 49.074  0 503 VAL BBB CA  1 ? 8  
ATOM   2327 C C   . VAL B 2 174 ? 9.725   26.861  -11.248 1.000 48.771  0 503 VAL BBB C   1 ? 8  
ATOM   2328 O O   . VAL B 2 174 ? 9.945   26.273  -10.165 1.000 48.439  0 503 VAL BBB O   1 ? 8  
ATOM   2329 C CB  . VAL B 2 174 ? 7.781   25.951  -12.604 1.000 51.334  0 503 VAL BBB CB  1 ? 8  
ATOM   2330 C CG1 . VAL B 2 174 ? 8.001   24.567  -12.006 1.000 50.779  0 503 VAL BBB CG1 1 ? 8  
ATOM   2331 C CG2 . VAL B 2 174 ? 6.318   26.134  -12.987 1.000 54.516  0 503 VAL BBB CG2 1 ? 8  
ATOM   2332 N N   . GLY B 2 175 ? 10.677  27.325  -12.068 1.000 47.255  0 504 GLY BBB N   1 ? 8  
ATOM   2333 C CA  . GLY B 2 175 ? 12.124  27.235  -11.792 1.000 46.577  0 504 GLY BBB CA  1 ? 8  
ATOM   2334 C C   . GLY B 2 175 ? 12.505  27.876  -10.462 1.000 45.973  0 504 GLY BBB C   1 ? 8  
ATOM   2335 O O   . GLY B 2 175 ? 13.460  27.385  -9.820  1.000 42.321  0 504 GLY BBB O   1 ? 8  
ATOM   2336 N N   . TYR B 2 176 ? 11.791  28.936  -10.061 1.000 46.149  0 505 TYR BBB N   1 ? 8  
ATOM   2337 C CA  . TYR B 2 176 ? 12.063  29.746  -8.845  1.000 45.283  0 505 TYR BBB CA  1 ? 8  
ATOM   2338 C C   . TYR B 2 176 ? 11.040  29.436  -7.742  1.000 43.909  0 505 TYR BBB C   1 ? 8  
ATOM   2339 O O   . TYR B 2 176 ? 11.059  30.120  -6.698  1.000 43.650  0 505 TYR BBB O   1 ? 8  
ATOM   2340 C CB  . TYR B 2 176 ? 12.078  31.231  -9.212  1.000 47.631  0 505 TYR BBB CB  1 ? 8  
ATOM   2341 C CG  . TYR B 2 176 ? 13.323  31.657  -9.942  1.000 50.332  0 505 TYR BBB CG  1 ? 8  
ATOM   2342 C CD1 . TYR B 2 176 ? 13.401  31.604  -11.326 1.000 52.482  0 505 TYR BBB CD1 1 ? 8  
ATOM   2343 C CD2 . TYR B 2 176 ? 14.440  32.089  -9.241  1.000 52.057  0 505 TYR BBB CD2 1 ? 8  
ATOM   2344 C CE1 . TYR B 2 176 ? 14.554  31.978  -11.997 1.000 52.855  0 505 TYR BBB CE1 1 ? 8  
ATOM   2345 C CE2 . TYR B 2 176 ? 15.599  32.469  -9.897  1.000 54.344  0 505 TYR BBB CE2 1 ? 8  
ATOM   2346 C CZ  . TYR B 2 176 ? 15.656  32.414  -11.280 1.000 53.825  0 505 TYR BBB CZ  1 ? 8  
ATOM   2347 O OH  . TYR B 2 176 ? 16.800  32.794  -11.919 1.000 56.991  0 505 TYR BBB OH  1 ? 8  
ATOM   2348 N N   . GLN B 2 177 ? 10.181  28.436  -7.949  1.000 43.067  0 506 GLN BBB N   1 ? 8  
ATOM   2349 C CA  . GLN B 2 177 ? 9.229   27.952  -6.916  1.000 43.075  0 506 GLN BBB CA  1 ? 8  
ATOM   2350 C C   . GLN B 2 177 ? 9.961   26.973  -6.004  1.000 41.881  0 506 GLN BBB C   1 ? 8  
ATOM   2351 O O   . GLN B 2 177 ? 10.918  26.327  -6.422  1.000 39.173  0 506 GLN BBB O   1 ? 8  
ATOM   2352 C CB  . GLN B 2 177 ? 7.994   27.311  -7.548  1.000 43.593  0 506 GLN BBB CB  1 ? 8  
ATOM   2353 C CG  . GLN B 2 177 ? 6.981   28.339  -8.024  1.000 45.236  0 506 GLN BBB CG  1 ? 8  
ATOM   2354 C CD  . GLN B 2 177 ? 5.784   27.725  -8.705  1.000 44.963  0 506 GLN BBB CD  1 ? 8  
ATOM   2355 O OE1 . GLN B 2 177 ? 5.431   26.571  -8.478  1.000 43.931  0 506 GLN BBB OE1 1 ? 8  
ATOM   2356 N NE2 . GLN B 2 177 ? 5.145   28.513  -9.547  1.000 46.302  0 506 GLN BBB NE2 1 ? 8  
ATOM   2357 N N   . PRO B 2 178 ? 9.535   26.844  -4.728  1.000 41.619  0 507 PRO BBB N   1 ? 8  
ATOM   2358 C CA  . PRO B 2 178 ? 10.207  25.951  -3.790  1.000 40.132  0 507 PRO BBB CA  1 ? 8  
ATOM   2359 C C   . PRO B 2 178 ? 9.897   24.485  -4.110  1.000 38.212  0 507 PRO BBB C   1 ? 8  
ATOM   2360 O O   . PRO B 2 178 ? 8.773   24.188  -4.477  1.000 38.051  0 507 PRO BBB O   1 ? 8  
ATOM   2361 C CB  . PRO B 2 178 ? 9.629   26.369  -2.431  1.000 42.191  0 507 PRO BBB CB  1 ? 8  
ATOM   2362 C CG  . PRO B 2 178 ? 8.245   26.892  -2.764  1.000 43.501  0 507 PRO BBB CG  1 ? 8  
ATOM   2363 C CD  . PRO B 2 178 ? 8.386   27.541  -4.126  1.000 43.081  0 507 PRO BBB CD  1 ? 8  
ATOM   2364 N N   . TYR B 2 179 ? 10.906  23.622  -3.986  1.000 36.805  0 508 TYR BBB N   1 ? 8  
ATOM   2365 C CA  . TYR B 2 179 ? 10.775  22.148  -4.100  1.000 37.247  0 508 TYR BBB CA  1 ? 8  
ATOM   2366 C C   . TYR B 2 179 ? 11.300  21.515  -2.812  1.000 36.855  0 508 TYR BBB C   1 ? 8  
ATOM   2367 O O   . TYR B 2 179 ? 12.445  21.795  -2.426  1.000 37.522  0 508 TYR BBB O   1 ? 8  
ATOM   2368 C CB  . TYR B 2 179 ? 11.484  21.627  -5.355  1.000 36.343  0 508 TYR BBB CB  1 ? 8  
ATOM   2369 C CG  . TYR B 2 179 ? 10.625  21.691  -6.590  1.000 36.090  0 508 TYR BBB CG  1 ? 8  
ATOM   2370 C CD1 . TYR B 2 179 ? 10.257  22.911  -7.136  1.000 37.434  0 508 TYR BBB CD1 1 ? 8  
ATOM   2371 C CD2 . TYR B 2 179 ? 10.136  20.541  -7.187  1.000 36.876  0 508 TYR BBB CD2 1 ? 8  
ATOM   2372 C CE1 . TYR B 2 179 ? 9.438   22.990  -8.252  1.000 38.315  0 508 TYR BBB CE1 1 ? 8  
ATOM   2373 C CE2 . TYR B 2 179 ? 9.325   20.602  -8.309  1.000 37.778  0 508 TYR BBB CE2 1 ? 8  
ATOM   2374 C CZ  . TYR B 2 179 ? 8.973   21.830  -8.845  1.000 39.071  0 508 TYR BBB CZ  1 ? 8  
ATOM   2375 O OH  . TYR B 2 179 ? 8.167   21.904  -9.953  1.000 42.144  0 508 TYR BBB OH  1 ? 8  
ATOM   2376 N N   . ARG B 2 180 ? 10.458  20.718  -2.154  1.000 36.520  0 509 ARG BBB N   1 ? 8  
ATOM   2377 C CA  . ARG B 2 180 ? 10.865  19.851  -1.021  1.000 35.976  0 509 ARG BBB CA  1 ? 8  
ATOM   2378 C C   . ARG B 2 180 ? 11.566  18.615  -1.589  1.000 35.811  0 509 ARG BBB C   1 ? 8  
ATOM   2379 O O   . ARG B 2 180 ? 11.083  18.067  -2.588  1.000 39.278  0 509 ARG BBB O   1 ? 8  
ATOM   2380 C CB  . ARG B 2 180 ? 9.659   19.505  -0.145  1.000 35.861  0 509 ARG BBB CB  1 ? 8  
ATOM   2381 C CG  . ARG B 2 180 ? 9.213   20.678  0.713   1.000 36.356  0 509 ARG BBB CG  1 ? 8  
ATOM   2382 C CD  . ARG B 2 180 ? 7.991   20.417  1.568   1.000 36.100  0 509 ARG BBB CD  1 ? 8  
ATOM   2383 N NE  . ARG B 2 180 ? 7.735   21.594  2.380   1.000 36.033  0 509 ARG BBB NE  1 ? 8  
ATOM   2384 C CZ  . ARG B 2 180 ? 7.080   21.604  3.533   1.000 36.818  0 509 ARG BBB CZ  1 ? 8  
ATOM   2385 N NH1 . ARG B 2 180 ? 6.588   20.486  4.043   1.000 37.102  0 509 ARG BBB NH1 1 ? 8  
ATOM   2386 N NH2 . ARG B 2 180 ? 6.921   22.745  4.179   1.000 36.910  0 509 ARG BBB NH2 1 ? 8  
ATOM   2387 N N   . VAL B 2 181 ? 12.675  18.225  -0.968  1.000 34.847  0 510 VAL BBB N   1 ? 8  
ATOM   2388 C CA  . VAL B 2 181 ? 13.570  17.125  -1.415  1.000 34.552  0 510 VAL BBB CA  1 ? 8  
ATOM   2389 C C   . VAL B 2 181 ? 13.792  16.163  -0.241  1.000 35.510  0 510 VAL BBB C   1 ? 8  
ATOM   2390 O O   . VAL B 2 181 ? 14.039  16.645  0.887   1.000 35.049  0 510 VAL BBB O   1 ? 8  
ATOM   2391 C CB  . VAL B 2 181 ? 14.901  17.701  -1.928  1.000 34.074  0 510 VAL BBB CB  1 ? 8  
ATOM   2392 C CG1 . VAL B 2 181 ? 15.866  16.597  -2.332  1.000 34.821  0 510 VAL BBB CG1 1 ? 8  
ATOM   2393 C CG2 . VAL B 2 181 ? 14.681  18.689  -3.068  1.000 33.843  0 510 VAL BBB CG2 1 ? 8  
ATOM   2394 N N   . VAL B 2 182 ? 13.682  14.860  -0.501  1.000 34.879  0 511 VAL BBB N   1 ? 8  
ATOM   2395 C CA  . VAL B 2 182 ? 14.077  13.773  0.435   1.000 35.855  0 511 VAL BBB CA  1 ? 8  
ATOM   2396 C C   . VAL B 2 182 ? 15.012  12.826  -0.320  1.000 36.792  0 511 VAL BBB C   1 ? 8  
ATOM   2397 O O   . VAL B 2 182 ? 14.565  12.230  -1.315  1.000 37.213  0 511 VAL BBB O   1 ? 8  
ATOM   2398 C CB  . VAL B 2 182 ? 12.857  13.032  1.012   1.000 37.891  0 511 VAL BBB CB  1 ? 8  
ATOM   2399 C CG1 . VAL B 2 182 ? 13.279  11.944  1.990   1.000 39.446  0 511 VAL BBB CG1 1 ? 8  
ATOM   2400 C CG2 . VAL B 2 182 ? 11.873  13.992  1.672   1.000 38.761  0 511 VAL BBB CG2 1 ? 8  
ATOM   2401 N N   . VAL B 2 183 ? 16.264  12.719  0.133   1.000 37.439  0 512 VAL BBB N   1 ? 8  
ATOM   2402 C CA  . VAL B 2 183 ? 17.282  11.766  -0.393  1.000 38.021  0 512 VAL BBB CA  1 ? 8  
ATOM   2403 C C   . VAL B 2 183 ? 17.320  10.551  0.543   1.000 38.566  0 512 VAL BBB C   1 ? 8  
ATOM   2404 O O   . VAL B 2 183 ? 17.715  10.718  1.723   1.000 38.113  0 512 VAL BBB O   1 ? 8  
ATOM   2405 C CB  . VAL B 2 183 ? 18.668  12.429  -0.530  1.000 38.390  0 512 VAL BBB CB  1 ? 8  
ATOM   2406 C CG1 . VAL B 2 183 ? 19.678  11.484  -1.160  1.000 39.603  0 512 VAL BBB CG1 1 ? 8  
ATOM   2407 C CG2 . VAL B 2 183 ? 18.605  13.733  -1.313  1.000 37.653  0 512 VAL BBB CG2 1 ? 8  
ATOM   2408 N N   . LEU B 2 184 ? 16.892  9.389   0.044   1.000 38.239  0 513 LEU BBB N   1 ? 8  
ATOM   2409 C CA  . LEU B 2 184 ? 16.950  8.099   0.775   1.000 40.220  0 513 LEU BBB CA  1 ? 8  
ATOM   2410 C C   . LEU B 2 184 ? 18.252  7.378   0.414   1.000 40.943  0 513 LEU BBB C   1 ? 8  
ATOM   2411 O O   . LEU B 2 184 ? 18.438  7.047   -0.780  1.000 40.390  0 513 LEU BBB O   1 ? 8  
ATOM   2412 C CB  . LEU B 2 184 ? 15.727  7.252   0.408   1.000 41.105  0 513 LEU BBB CB  1 ? 8  
ATOM   2413 C CG  . LEU B 2 184 ? 14.372  7.790   0.867   1.000 40.055  0 513 LEU BBB CG  1 ? 8  
ATOM   2414 C CD1 . LEU B 2 184 ? 13.270  6.799   0.526   1.000 40.347  0 513 LEU BBB CD1 1 ? 8  
ATOM   2415 C CD2 . LEU B 2 184 ? 14.376  8.094   2.356   1.000 39.707  0 513 LEU BBB CD2 1 ? 8  
ATOM   2416 N N   . SER B 2 185 ? 19.123  7.170   1.407   1.000 41.616  0 514 SER BBB N   1 ? 8  
ATOM   2417 C CA  . SER B 2 185 ? 20.320  6.292   1.326   1.000 42.380  0 514 SER BBB CA  1 ? 8  
ATOM   2418 C C   . SER B 2 185 ? 20.019  4.979   2.050   1.000 42.915  0 514 SER BBB C   1 ? 8  
ATOM   2419 O O   . SER B 2 185 ? 19.400  5.033   3.124   1.000 44.078  0 514 SER BBB O   1 ? 8  
ATOM   2420 C CB  . SER B 2 185 ? 21.528  6.966   1.901   1.000 42.851  0 514 SER BBB CB  1 ? 8  
ATOM   2421 O OG  . SER B 2 185 ? 21.746  8.218   1.271   1.000 43.214  0 514 SER BBB OG  1 ? 8  
ATOM   2422 N N   . PHE B 2 186 ? 20.431  3.848   1.477   1.000 44.055  0 515 PHE BBB N   1 ? 8  
ATOM   2423 C CA  . PHE B 2 186 ? 20.195  2.490   2.030   1.000 46.029  0 515 PHE BBB CA  1 ? 8  
ATOM   2424 C C   . PHE B 2 186 ? 21.540  1.877   2.417   1.000 49.112  0 515 PHE BBB C   1 ? 8  
ATOM   2425 O O   . PHE B 2 186 ? 22.379  1.677   1.523   1.000 51.762  0 515 PHE BBB O   1 ? 8  
ATOM   2426 C CB  . PHE B 2 186 ? 19.428  1.635   1.022   1.000 45.842  0 515 PHE BBB CB  1 ? 8  
ATOM   2427 C CG  . PHE B 2 186 ? 18.085  2.207   0.652   1.000 44.911  0 515 PHE BBB CG  1 ? 8  
ATOM   2428 C CD1 . PHE B 2 186 ? 17.963  3.100   -0.402  1.000 44.307  0 515 PHE BBB CD1 1 ? 8  
ATOM   2429 C CD2 . PHE B 2 186 ? 16.953  1.873   1.378   1.000 45.438  0 515 PHE BBB CD2 1 ? 8  
ATOM   2430 C CE1 . PHE B 2 186 ? 16.728  3.626   -0.743  1.000 44.731  0 515 PHE BBB CE1 1 ? 8  
ATOM   2431 C CE2 . PHE B 2 186 ? 15.720  2.410   1.046   1.000 45.626  0 515 PHE BBB CE2 1 ? 8  
ATOM   2432 C CZ  . PHE B 2 186 ? 15.610  3.282   -0.017  1.000 45.908  0 515 PHE BBB CZ  1 ? 8  
ATOM   2433 N N   . GLU B 2 187 ? 21.720  1.604   3.712   1.000 49.887  0 516 GLU BBB N   1 ? 8  
ATOM   2434 C CA  . GLU B 2 187 ? 22.983  1.107   4.312   1.000 52.173  0 516 GLU BBB CA  1 ? 8  
ATOM   2435 C C   . GLU B 2 187 ? 22.837  -0.384  4.638   1.000 53.960  0 516 GLU BBB C   1 ? 8  
ATOM   2436 O O   . GLU B 2 187 ? 21.829  -0.766  5.266   1.000 53.888  0 516 GLU BBB O   1 ? 8  
ATOM   2437 C CB  . GLU B 2 187 ? 23.321  1.922   5.559   1.000 53.060  0 516 GLU BBB CB  1 ? 8  
ATOM   2438 C CG  . GLU B 2 187 ? 24.729  1.678   6.071   1.000 56.128  0 516 GLU BBB CG  1 ? 8  
ATOM   2439 C CD  . GLU B 2 187 ? 25.096  2.446   7.327   1.000 58.288  0 516 GLU BBB CD  1 ? 8  
ATOM   2440 O OE1 . GLU B 2 187 ? 24.322  2.391   8.302   1.000 60.150  0 516 GLU BBB OE1 1 ? 8  
ATOM   2441 O OE2 . GLU B 2 187 ? 26.155  3.099   7.326   1.000 60.705  0 516 GLU BBB OE2 1 ? 8  
ATOM   2442 N N   . LEU B 2 188 ? 23.818  -1.184  4.215   1.000 55.438  0 517 LEU BBB N   1 ? 8  
ATOM   2443 C CA  . LEU B 2 188 ? 23.916  -2.641  4.482   1.000 57.231  0 517 LEU BBB CA  1 ? 8  
ATOM   2444 C C   . LEU B 2 188 ? 25.317  -2.923  5.029   1.000 60.135  0 517 LEU BBB C   1 ? 8  
ATOM   2445 O O   . LEU B 2 188 ? 26.291  -2.776  4.266   1.000 62.836  0 517 LEU BBB O   1 ? 8  
ATOM   2446 C CB  . LEU B 2 188 ? 23.645  -3.392  3.172   1.000 56.928  0 517 LEU BBB CB  1 ? 8  
ATOM   2447 C CG  . LEU B 2 188 ? 23.130  -4.822  3.312   1.000 58.218  0 517 LEU BBB CG  1 ? 8  
ATOM   2448 C CD1 . LEU B 2 188 ? 21.764  -4.858  3.986   1.000 57.786  0 517 LEU BBB CD1 1 ? 8  
ATOM   2449 C CD2 . LEU B 2 188 ? 23.057  -5.494  1.951   1.000 58.085  0 517 LEU BBB CD2 1 ? 8  
ATOM   2450 N N   . LEU B 2 189 ? 25.408  -3.263  6.319   1.000 62.181  0 518 LEU BBB N   1 ? 8  
ATOM   2451 C CA  . LEU B 2 189 ? 26.674  -3.557  7.047   1.000 63.018  0 518 LEU BBB CA  1 ? 8  
ATOM   2452 C C   . LEU B 2 189 ? 26.636  -5.009  7.535   1.000 66.126  0 518 LEU BBB C   1 ? 8  
ATOM   2453 O O   . LEU B 2 189 ? 25.541  -5.610  7.503   1.000 64.849  0 518 LEU BBB O   1 ? 8  
ATOM   2454 C CB  . LEU B 2 189 ? 26.820  -2.594  8.231   1.000 62.589  0 518 LEU BBB CB  1 ? 8  
ATOM   2455 C CG  . LEU B 2 189 ? 26.705  -1.104  7.909   1.000 60.156  0 518 LEU BBB CG  1 ? 8  
ATOM   2456 C CD1 . LEU B 2 189 ? 26.749  -0.270  9.181   1.000 60.093  0 518 LEU BBB CD1 1 ? 8  
ATOM   2457 C CD2 . LEU B 2 189 ? 27.802  -0.668  6.952   1.000 60.141  0 518 LEU BBB CD2 1 ? 8  
ATOM   2458 N N   . HIS B 2 190 ? 27.782  -5.551  7.970   1.000 70.981  0 519 HIS BBB N   1 ? 8  
ATOM   2459 C CA  . HIS B 2 190 ? 27.858  -6.858  8.680   1.000 73.800  0 519 HIS BBB CA  1 ? 8  
ATOM   2460 C C   . HIS B 2 190 ? 27.297  -6.655  10.090  1.000 73.798  0 519 HIS BBB C   1 ? 8  
ATOM   2461 O O   . HIS B 2 190 ? 28.086  -6.544  11.053  1.000 75.047  0 519 HIS BBB O   1 ? 8  
ATOM   2462 C CB  . HIS B 2 190 ? 29.270  -7.463  8.667   1.000 76.825  0 519 HIS BBB CB  1 ? 8  
ATOM   2463 C CG  . HIS B 2 190 ? 29.262  -8.929  8.955   1.000 80.719  0 519 HIS BBB CG  1 ? 8  
ATOM   2464 N ND1 . HIS B 2 190 ? 29.718  -9.452  10.150  1.000 85.372  0 519 HIS BBB ND1 1 ? 8  
ATOM   2465 C CD2 . HIS B 2 190 ? 28.817  -9.980  8.229   1.000 82.115  0 519 HIS BBB CD2 1 ? 8  
ATOM   2466 C CE1 . HIS B 2 190 ? 29.574  -10.764 10.139  1.000 87.211  0 519 HIS BBB CE1 1 ? 8  
ATOM   2467 N NE2 . HIS B 2 190 ? 29.020  -11.112 8.973   1.000 85.606  0 519 HIS BBB NE2 1 ? 8  
ATOM   2468 N N   . ALA B 2 191 ? 25.967  -6.577  10.178  1.000 68.845  0 520 ALA BBB N   1 ? 9  
ATOM   2469 C CA  . ALA B 2 191 ? 25.198  -6.240  11.397  1.000 68.244  0 520 ALA BBB CA  1 ? 9  
ATOM   2470 C C   . ALA B 2 191 ? 23.749  -6.676  11.206  1.000 64.923  0 520 ALA BBB C   1 ? 9  
ATOM   2471 O O   . ALA B 2 191 ? 23.317  -6.920  10.083  1.000 62.665  0 520 ALA BBB O   1 ? 9  
ATOM   2472 C CB  . ALA B 2 191 ? 25.299  -4.760  11.665  1.000 68.499  0 520 ALA BBB CB  1 ? 9  
ATOM   2473 N N   . PRO B 2 192 ? 22.949  -6.793  12.288  1.000 65.408  0 521 PRO BBB N   1 ? 9  
ATOM   2474 C CA  . PRO B 2 192 ? 21.528  -7.107  12.148  1.000 63.650  0 521 PRO BBB CA  1 ? 9  
ATOM   2475 C C   . PRO B 2 192 ? 20.790  -6.017  11.355  1.000 61.577  0 521 PRO BBB C   1 ? 9  
ATOM   2476 O O   . PRO B 2 192 ? 21.021  -4.846  11.609  1.000 61.929  0 521 PRO BBB O   1 ? 9  
ATOM   2477 C CB  . PRO B 2 192 ? 21.013  -7.178  13.593  1.000 65.354  0 521 PRO BBB CB  1 ? 9  
ATOM   2478 C CG  . PRO B 2 192 ? 22.261  -7.382  14.434  1.000 68.004  0 521 PRO BBB CG  1 ? 9  
ATOM   2479 C CD  . PRO B 2 192 ? 23.359  -6.652  13.693  1.000 67.842  0 521 PRO BBB CD  1 ? 9  
ATOM   2480 N N   . ALA B 2 193 ? 19.947  -6.428  10.402  1.000 60.205  0 522 ALA BBB N   1 ? 9  
ATOM   2481 C CA  . ALA B 2 193 ? 19.022  -5.548  9.650   1.000 58.763  0 522 ALA BBB CA  1 ? 9  
ATOM   2482 C C   . ALA B 2 193 ? 17.871  -5.146  10.576  1.000 57.365  0 522 ALA BBB C   1 ? 9  
ATOM   2483 O O   . ALA B 2 193 ? 17.319  -6.031  11.240  1.000 59.031  0 522 ALA BBB O   1 ? 9  
ATOM   2484 C CB  . ALA B 2 193 ? 18.521  -6.256  8.416   1.000 59.278  0 522 ALA BBB CB  1 ? 9  
ATOM   2485 N N   . THR B 2 194 ? 17.544  -3.854  10.634  1.000 56.484  0 523 THR BBB N   1 ? 9  
ATOM   2486 C CA  . THR B 2 194 ? 16.515  -3.292  11.550  1.000 56.633  0 523 THR BBB CA  1 ? 9  
ATOM   2487 C C   . THR B 2 194 ? 15.406  -2.586  10.755  1.000 54.550  0 523 THR BBB C   1 ? 9  
ATOM   2488 O O   . THR B 2 194 ? 14.364  -2.305  11.367  1.000 54.577  0 523 THR BBB O   1 ? 9  
ATOM   2489 C CB  . THR B 2 194 ? 17.170  -2.386  12.604  1.000 57.568  0 523 THR BBB CB  1 ? 9  
ATOM   2490 O OG1 . THR B 2 194 ? 17.504  -1.129  12.011  1.000 57.018  0 523 THR BBB OG1 1 ? 9  
ATOM   2491 C CG2 . THR B 2 194 ? 18.410  -3.012  13.205  1.000 59.131  0 523 THR BBB CG2 1 ? 9  
ATOM   2492 N N   . VAL B 2 195 ? 15.608  -2.319  9.460   1.000 53.229  0 524 VAL BBB N   1 ? 9  
ATOM   2493 C CA  . VAL B 2 195 ? 14.599  -1.657  8.577   1.000 53.446  0 524 VAL BBB CA  1 ? 9  
ATOM   2494 C C   . VAL B 2 195 ? 14.200  -2.635  7.470   1.000 54.292  0 524 VAL BBB C   1 ? 9  
ATOM   2495 O O   . VAL B 2 195 ? 14.971  -2.772  6.506   1.000 56.013  0 524 VAL BBB O   1 ? 9  
ATOM   2496 C CB  . VAL B 2 195 ? 15.122  -0.336  7.988   1.000 53.337  0 524 VAL BBB CB  1 ? 9  
ATOM   2497 C CG1 . VAL B 2 195 ? 14.046  0.377   7.186   1.000 53.521  0 524 VAL BBB CG1 1 ? 9  
ATOM   2498 C CG2 . VAL B 2 195 ? 15.682  0.575   9.068   1.000 54.388  0 524 VAL BBB CG2 1 ? 9  
ATOM   2499 N N   . CYS B 2 196 ? 13.032  -3.268  7.607   1.000 55.250  0 525 CYS BBB N   1 ? 9  
ATOM   2500 C CA  . CYS B 2 196 ? 12.486  -4.269  6.652   1.000 56.762  0 525 CYS BBB CA  1 ? 9  
ATOM   2501 C C   . CYS B 2 196 ? 11.170  -3.759  6.059   1.000 58.134  0 525 CYS BBB C   1 ? 9  
ATOM   2502 O O   . CYS B 2 196 ? 10.472  -2.982  6.739   1.000 56.989  0 525 CYS BBB O   1 ? 9  
ATOM   2503 C CB  . CYS B 2 196 ? 12.284  -5.617  7.330   1.000 58.227  0 525 CYS BBB CB  1 ? 9  
ATOM   2504 S SG  . CYS B 2 196 ? 13.844  -6.391  7.832   1.000 59.478  0 525 CYS BBB SG  1 ? 9  
ATOM   2505 N N   . GLY B 2 197 ? 10.870  -4.157  4.819   1.000 60.217  0 526 GLY BBB N   1 ? 9  
ATOM   2506 C CA  . GLY B 2 197 ? 9.574   -3.906  4.164   1.000 61.806  0 526 GLY BBB CA  1 ? 9  
ATOM   2507 C C   . GLY B 2 197 ? 8.484   -4.781  4.778   1.000 63.428  0 526 GLY BBB C   1 ? 9  
ATOM   2508 O O   . GLY B 2 197 ? 8.790   -5.737  5.488   1.000 62.530  0 526 GLY BBB O   1 ? 9  
ATOM   2509 N N   . PRO B 2 198 ? 7.188   -4.493  4.517   1.000 66.167  0 527 PRO BBB N   1 ? 9  
ATOM   2510 C CA  . PRO B 2 198 ? 6.086   -5.232  5.135   1.000 68.895  0 527 PRO BBB CA  1 ? 9  
ATOM   2511 C C   . PRO B 2 198 ? 6.067   -6.731  4.784   1.000 72.394  0 527 PRO BBB C   1 ? 9  
ATOM   2512 O O   . PRO B 2 198 ? 5.469   -7.481  5.532   1.000 75.646  0 527 PRO BBB O   1 ? 9  
ATOM   2513 C CB  . PRO B 2 198 ? 4.814   -4.550  4.593   1.000 71.005  0 527 PRO BBB CB  1 ? 9  
ATOM   2514 C CG  . PRO B 2 198 ? 5.281   -3.220  4.033   1.000 69.246  0 527 PRO BBB CG  1 ? 9  
ATOM   2515 C CD  . PRO B 2 198 ? 6.709   -3.455  3.595   1.000 67.000  0 527 PRO BBB CD  1 ? 9  
ATOM   2516 N N   . LYS B 2 199 ? 6.724   -7.130  3.686   1.000 74.504  0 528 LYS BBB N   1 ? 9  
ATOM   2517 C CA  . LYS B 2 199 ? 6.794   -8.538  3.202   1.000 79.458  0 528 LYS BBB CA  1 ? 9  
ATOM   2518 C C   . LYS B 2 199 ? 8.007   -9.258  3.810   1.000 79.132  0 528 LYS BBB C   1 ? 9  
ATOM   2519 O O   . LYS B 2 199 ? 8.212   -10.436 3.458   1.000 81.163  0 528 LYS BBB O   1 ? 9  
ATOM   2520 C CB  . LYS B 2 199 ? 6.845   -8.578  1.671   1.000 81.699  0 528 LYS BBB CB  1 ? 9  
ATOM   2521 C CG  . LYS B 2 199 ? 5.570   -8.114  0.978   1.000 85.648  0 528 LYS BBB CG  1 ? 9  
ATOM   2522 C CD  . LYS B 2 199 ? 5.379   -6.611  0.938   1.000 84.052  0 528 LYS BBB CD  1 ? 9  
ATOM   2523 C CE  . LYS B 2 199 ? 4.447   -6.149  -0.164  1.000 88.868  0 528 LYS BBB CE  1 ? 9  
ATOM   2524 N NZ  . LYS B 2 199 ? 3.093   -6.738  -0.029  1.000 93.782  0 528 LYS BBB NZ  1 ? 9  
ATOM   2525 N N   . LYS B 2 200 ? 8.753   -8.591  4.704   1.000 79.076  0 529 LYS BBB N   1 ? 9  
ATOM   2526 C CA  . LYS B 2 200 ? 9.972   -9.115  5.385   1.000 78.360  0 529 LYS BBB CA  1 ? 9  
ATOM   2527 C C   . LYS B 2 200 ? 11.011  -9.522  4.331   1.000 77.092  0 529 LYS BBB C   1 ? 9  
ATOM   2528 O O   . LYS B 2 200 ? 12.213  -9.349  4.525   1.000 73.128  0 529 LYS BBB O   1 ? 9  
ATOM   2529 C CB  . LYS B 2 200 ? 9.621   -10.290 6.306   1.000 81.714  0 529 LYS BBB CB  1 ? 9  
ATOM   2530 C CG  . LYS B 2 200 ? 8.930   -9.911  7.609   1.000 82.412  0 529 LYS BBB CG  1 ? 9  
ATOM   2531 C CD  . LYS B 2 200 ? 8.419   -11.111 8.381   1.000 87.158  0 529 LYS BBB CD  1 ? 9  
ATOM   2532 C CE  . LYS B 2 200 ? 7.786   -10.749 9.708   1.000 88.190  0 529 LYS BBB CE  1 ? 9  
ATOM   2533 N NZ  . LYS B 2 200 ? 7.305   -11.952 10.430  1.000 92.279  0 529 LYS BBB NZ  1 ? 9  
ATOM   2534 N N   . VAL C 3 4   ? 6.381   40.531  16.684  1.000 68.602  0 4   VAL CCC N   1 ? 10 
ATOM   2535 C CA  . VAL C 3 4   ? 7.254   40.748  17.888  1.000 64.621  0 4   VAL CCC CA  1 ? 10 
ATOM   2536 C C   . VAL C 3 4   ? 7.424   42.257  18.095  1.000 61.342  0 4   VAL CCC C   1 ? 10 
ATOM   2537 O O   . VAL C 3 4   ? 7.474   42.984  17.081  1.000 60.856  0 4   VAL CCC O   1 ? 10 
ATOM   2538 C CB  . VAL C 3 4   ? 8.616   40.029  17.769  1.000 65.121  0 4   VAL CCC CB  1 ? 10 
ATOM   2539 C CG1 . VAL C 3 4   ? 8.457   38.524  17.597  1.000 69.476  0 4   VAL CCC CG1 1 ? 10 
ATOM   2540 C CG2 . VAL C 3 4   ? 9.503   40.598  16.667  1.000 65.101  0 4   VAL CCC CG2 1 ? 10 
ATOM   2541 N N   . GLN C 3 5   ? 7.492   42.700  19.356  1.000 59.746  0 5   GLN CCC N   1 ? 10 
ATOM   2542 C CA  A GLN C 3 5   ? 7.712   44.126  19.717  0.500 58.134  0 5   GLN CCC CA  1 ? 10 
ATOM   2543 C CA  B GLN C 3 5   ? 7.711   44.125  19.726  0.500 58.078  0 5   GLN CCC CA  1 ? 10 
ATOM   2544 C C   . GLN C 3 5   ? 9.210   44.350  19.945  1.000 55.686  0 5   GLN CCC C   1 ? 10 
ATOM   2545 O O   . GLN C 3 5   ? 9.808   43.599  20.738  1.000 55.859  0 5   GLN CCC O   1 ? 10 
ATOM   2546 C CB  A GLN C 3 5   ? 6.906   44.518  20.957  0.500 60.163  0 5   GLN CCC CB  1 ? 10 
ATOM   2547 C CB  B GLN C 3 5   ? 6.905   44.494  20.976  0.500 60.039  0 5   GLN CCC CB  1 ? 10 
ATOM   2548 C CG  A GLN C 3 5   ? 6.857   46.022  21.198  0.500 60.941  0 5   GLN CCC CG  1 ? 10 
ATOM   2549 C CG  B GLN C 3 5   ? 6.937   45.981  21.316  0.500 60.590  0 5   GLN CCC CG  1 ? 10 
ATOM   2550 C CD  A GLN C 3 5   ? 5.843   46.724  20.325  0.500 64.179  0 5   GLN CCC CD  1 ? 10 
ATOM   2551 C CD  B GLN C 3 5   ? 5.856   46.373  22.292  0.500 65.317  0 5   GLN CCC CD  1 ? 10 
ATOM   2552 O OE1 A GLN C 3 5   ? 4.830   46.152  19.924  0.500 66.445  0 5   GLN CCC OE1 1 ? 10 
ATOM   2553 O OE1 B GLN C 3 5   ? 4.700   45.973  22.161  0.500 69.036  0 5   GLN CCC OE1 1 ? 10 
ATOM   2554 N NE2 A GLN C 3 5   ? 6.106   47.987  20.026  0.500 65.104  0 5   GLN CCC NE2 1 ? 10 
ATOM   2555 N NE2 B GLN C 3 5   ? 6.222   47.179  23.276  0.500 66.484  0 5   GLN CCC NE2 1 ? 10 
ATOM   2556 N N   . LEU C 3 6   ? 9.778   45.325  19.236  1.000 54.854  0 6   LEU CCC N   1 ? 10 
ATOM   2557 C CA  . LEU C 3 6   ? 11.143  45.846  19.474  1.000 53.905  0 6   LEU CCC CA  1 ? 10 
ATOM   2558 C C   . LEU C 3 6   ? 10.976  47.077  20.365  1.000 54.390  0 6   LEU CCC C   1 ? 10 
ATOM   2559 O O   . LEU C 3 6   ? 10.215  48.000  19.976  1.000 55.690  0 6   LEU CCC O   1 ? 10 
ATOM   2560 C CB  . LEU C 3 6   ? 11.820  46.188  18.138  1.000 54.850  0 6   LEU CCC CB  1 ? 10 
ATOM   2561 C CG  . LEU C 3 6   ? 12.762  45.114  17.589  1.000 55.851  0 6   LEU CCC CG  1 ? 10 
ATOM   2562 C CD1 . LEU C 3 6   ? 12.076  43.763  17.487  1.000 56.328  0 6   LEU CCC CD1 1 ? 10 
ATOM   2563 C CD2 . LEU C 3 6   ? 13.326  45.517  16.235  1.000 59.105  0 6   LEU CCC CD2 1 ? 10 
ATOM   2564 N N   . VAL C 3 7   ? 11.611  47.066  21.536  1.000 54.089  0 7   VAL CCC N   1 ? 10 
ATOM   2565 C CA  . VAL C 3 7   ? 11.608  48.210  22.491  1.000 55.667  0 7   VAL CCC CA  1 ? 10 
ATOM   2566 C C   . VAL C 3 7   ? 12.926  48.966  22.311  1.000 55.841  0 7   VAL CCC C   1 ? 10 
ATOM   2567 O O   . VAL C 3 7   ? 13.988  48.337  22.430  1.000 53.626  0 7   VAL CCC O   1 ? 10 
ATOM   2568 C CB  . VAL C 3 7   ? 11.406  47.738  23.943  1.000 56.850  0 7   VAL CCC CB  1 ? 10 
ATOM   2569 C CG1 . VAL C 3 7   ? 11.351  48.917  24.902  1.000 59.719  0 7   VAL CCC CG1 1 ? 10 
ATOM   2570 C CG2 . VAL C 3 7   ? 10.168  46.861  24.079  1.000 57.742  0 7   VAL CCC CG2 1 ? 10 
ATOM   2571 N N   . GLU C 3 8   ? 12.827  50.263  22.022  1.000 43.680  0 8   GLU CCC N   1 ? 11 
ATOM   2572 C CA  . GLU C 3 8   ? 13.949  51.157  21.643  1.000 45.277  0 8   GLU CCC CA  1 ? 11 
ATOM   2573 C C   . GLU C 3 8   ? 14.063  52.276  22.688  1.000 49.723  0 8   GLU CCC C   1 ? 11 
ATOM   2574 O O   . GLU C 3 8   ? 13.012  52.771  23.136  1.000 51.775  0 8   GLU CCC O   1 ? 11 
ATOM   2575 C CB  . GLU C 3 8   ? 13.681  51.707  20.241  1.000 45.196  0 8   GLU CCC CB  1 ? 11 
ATOM   2576 C CG  . GLU C 3 8   ? 14.864  52.423  19.616  1.000 45.918  0 8   GLU CCC CG  1 ? 11 
ATOM   2577 C CD  . GLU C 3 8   ? 14.595  52.970  18.227  1.000 46.967  0 8   GLU CCC CD  1 ? 11 
ATOM   2578 O OE1 . GLU C 3 8   ? 13.641  52.494  17.590  1.000 47.579  0 8   GLU CCC OE1 1 ? 11 
ATOM   2579 O OE2 . GLU C 3 8   ? 15.342  53.863  17.784  1.000 49.356  0 8   GLU CCC OE2 1 ? 11 
ATOM   2580 N N   . SER C 3 9   ? 15.287  52.645  23.074  1.000 52.518  0 9   SER CCC N   1 ? 11 
ATOM   2581 C CA  . SER C 3 9   ? 15.576  53.784  23.985  1.000 57.058  0 9   SER CCC CA  1 ? 11 
ATOM   2582 C C   . SER C 3 9   ? 16.956  54.375  23.664  1.000 58.029  0 9   SER CCC C   1 ? 11 
ATOM   2583 O O   . SER C 3 9   ? 17.661  53.805  22.812  1.000 54.370  0 9   SER CCC O   1 ? 11 
ATOM   2584 C CB  . SER C 3 9   ? 15.461  53.367  25.434  1.000 60.346  0 9   SER CCC CB  1 ? 11 
ATOM   2585 O OG  . SER C 3 9   ? 16.450  52.405  25.774  1.000 60.715  0 9   SER CCC OG  1 ? 11 
ATOM   2586 N N   . GLY C 3 10  ? 17.315  55.466  24.345  1.000 62.858  0 10  GLY CCC N   1 ? 11 
ATOM   2587 C CA  . GLY C 3 10  ? 18.517  56.277  24.078  1.000 65.633  0 10  GLY CCC CA  1 ? 11 
ATOM   2588 C C   . GLY C 3 10  ? 18.137  57.589  23.421  1.000 69.358  0 10  GLY CCC C   1 ? 11 
ATOM   2589 O O   . GLY C 3 10  ? 16.976  58.002  23.558  1.000 71.727  0 10  GLY CCC O   1 ? 11 
ATOM   2590 N N   . GLY C 3 11  ? 19.081  58.232  22.733  1.000 73.034  0 11  GLY CCC N   1 ? 11 
ATOM   2591 C CA  . GLY C 3 11  ? 18.850  59.494  22.006  1.000 76.512  0 11  GLY CCC CA  1 ? 11 
ATOM   2592 C C   . GLY C 3 11  ? 19.180  60.700  22.867  1.000 81.325  0 11  GLY CCC C   1 ? 11 
ATOM   2593 O O   . GLY C 3 11  ? 20.163  60.621  23.627  1.000 84.476  0 11  GLY CCC O   1 ? 11 
ATOM   2594 N N   . GLY C 3 12  ? 18.397  61.777  22.746  1.000 84.160  0 12  GLY CCC N   1 ? 11 
ATOM   2595 C CA  . GLY C 3 12  ? 18.605  63.050  23.466  1.000 88.690  0 12  GLY CCC CA  1 ? 11 
ATOM   2596 C C   . GLY C 3 12  ? 19.487  64.010  22.685  1.000 90.264  0 12  GLY CCC C   1 ? 11 
ATOM   2597 O O   . GLY C 3 12  ? 19.818  63.695  21.522  1.000 88.005  0 12  GLY CCC O   1 ? 11 
ATOM   2598 N N   . LEU C 3 13  ? 19.858  65.136  23.306  1.000 94.840  0 13  LEU CCC N   1 ? 11 
ATOM   2599 C CA  . LEU C 3 13  ? 20.690  66.216  22.705  1.000 98.144  0 13  LEU CCC CA  1 ? 11 
ATOM   2600 C C   . LEU C 3 13  ? 22.153  65.998  23.102  1.000 97.847  0 13  LEU CCC C   1 ? 11 
ATOM   2601 O O   . LEU C 3 13  ? 22.388  65.561  24.244  1.000 97.442  0 13  LEU CCC O   1 ? 11 
ATOM   2602 C CB  . LEU C 3 13  ? 20.202  67.585  23.201  1.000 104.299 0 13  LEU CCC CB  1 ? 11 
ATOM   2603 C CG  . LEU C 3 13  ? 18.688  67.780  23.302  1.000 106.400 0 13  LEU CCC CG  1 ? 11 
ATOM   2604 C CD1 . LEU C 3 13  ? 18.359  69.205  23.728  1.000 112.431 0 13  LEU CCC CD1 1 ? 11 
ATOM   2605 C CD2 . LEU C 3 13  ? 17.989  67.441  21.990  1.000 104.432 0 13  LEU CCC CD2 1 ? 11 
ATOM   2606 N N   . VAL C 3 14  ? 23.091  66.305  22.199  1.000 98.061  0 14  VAL CCC N   1 ? 11 
ATOM   2607 C CA  . VAL C 3 14  ? 24.563  66.288  22.461  1.000 99.054  0 14  VAL CCC CA  1 ? 11 
ATOM   2608 C C   . VAL C 3 14  ? 25.247  67.323  21.557  1.000 101.885 0 14  VAL CCC C   1 ? 11 
ATOM   2609 O O   . VAL C 3 14  ? 24.690  67.633  20.485  1.000 102.685 0 14  VAL CCC O   1 ? 11 
ATOM   2610 C CB  . VAL C 3 14  ? 25.158  64.880  22.256  1.000 94.820  0 14  VAL CCC CB  1 ? 11 
ATOM   2611 C CG1 . VAL C 3 14  ? 24.769  63.932  23.379  1.000 92.982  0 14  VAL CCC CG1 1 ? 11 
ATOM   2612 C CG2 . VAL C 3 14  ? 24.780  64.292  20.904  1.000 91.357  0 14  VAL CCC CG2 1 ? 11 
ATOM   2613 N N   . LYS C 3 15  ? 26.412  67.829  21.975  1.000 103.656 0 15  LYS CCC N   1 ? 11 
ATOM   2614 C CA  . LYS C 3 15  ? 27.262  68.758  21.179  1.000 106.409 0 15  LYS CCC CA  1 ? 11 
ATOM   2615 C C   . LYS C 3 15  ? 27.938  67.976  20.046  1.000 102.970 0 15  LYS CCC C   1 ? 11 
ATOM   2616 O O   . LYS C 3 15  ? 28.087  66.747  20.188  1.000 98.748  0 15  LYS CCC O   1 ? 11 
ATOM   2617 C CB  . LYS C 3 15  ? 28.319  69.421  22.068  1.000 111.351 0 15  LYS CCC CB  1 ? 11 
ATOM   2618 C CG  . LYS C 3 15  ? 27.775  70.315  23.176  1.000 114.851 0 15  LYS CCC CG  1 ? 11 
ATOM   2619 C CD  . LYS C 3 15  ? 28.861  70.973  24.005  1.000 119.990 0 15  LYS CCC CD  1 ? 11 
ATOM   2620 C CE  . LYS C 3 15  ? 28.345  72.088  24.890  1.000 125.012 0 15  LYS CCC CE  1 ? 11 
ATOM   2621 N NZ  . LYS C 3 15  ? 29.446  72.945  25.392  1.000 131.104 0 15  LYS CCC NZ  1 ? 11 
ATOM   2622 N N   . THR C 3 16  ? 28.330  68.666  18.969  1.000 105.136 0 16  THR CCC N   1 ? 11 
ATOM   2623 C CA  . THR C 3 16  ? 29.132  68.111  17.843  1.000 104.028 0 16  THR CCC CA  1 ? 11 
ATOM   2624 C C   . THR C 3 16  ? 30.408  67.475  18.408  1.000 104.051 0 16  THR CCC C   1 ? 11 
ATOM   2625 O O   . THR C 3 16  ? 31.077  68.133  19.226  1.000 108.433 0 16  THR CCC O   1 ? 11 
ATOM   2626 C CB  . THR C 3 16  ? 29.467  69.197  16.810  1.000 108.932 0 16  THR CCC CB  1 ? 11 
ATOM   2627 O OG1 . THR C 3 16  ? 28.236  69.723  16.313  1.000 109.357 0 16  THR CCC OG1 1 ? 11 
ATOM   2628 C CG2 . THR C 3 16  ? 30.308  68.687  15.660  1.000 108.389 0 16  THR CCC CG2 1 ? 11 
ATOM   2629 N N   . GLY C 3 17  ? 30.716  66.242  17.994  1.000 100.558 0 17  GLY CCC N   1 ? 11 
ATOM   2630 C CA  . GLY C 3 17  ? 31.872  65.464  18.481  1.000 100.995 0 17  GLY CCC CA  1 ? 11 
ATOM   2631 C C   . GLY C 3 17  ? 31.525  64.596  19.682  1.000 98.718  0 17  GLY CCC C   1 ? 11 
ATOM   2632 O O   . GLY C 3 17  ? 32.389  63.795  20.086  1.000 99.060  0 17  GLY CCC O   1 ? 11 
ATOM   2633 N N   . GLY C 3 18  ? 30.309  64.734  20.227  1.000 97.507  0 18  GLY CCC N   1 ? 11 
ATOM   2634 C CA  . GLY C 3 18  ? 29.832  63.998  21.416  1.000 94.848  0 18  GLY CCC CA  1 ? 11 
ATOM   2635 C C   . GLY C 3 18  ? 29.427  62.571  21.083  1.000 89.899  0 18  GLY CCC C   1 ? 11 
ATOM   2636 O O   . GLY C 3 18  ? 29.512  62.188  19.894  1.000 88.569  0 18  GLY CCC O   1 ? 11 
ATOM   2637 N N   . SER C 3 19  ? 28.987  61.813  22.094  1.000 87.721  0 19  SER CCC N   1 ? 11 
ATOM   2638 C CA  . SER C 3 19  ? 28.646  60.370  21.991  1.000 82.811  0 19  SER CCC CA  1 ? 11 
ATOM   2639 C C   . SER C 3 19  ? 27.233  60.102  22.521  1.000 81.379  0 19  SER CCC C   1 ? 11 
ATOM   2640 O O   . SER C 3 19  ? 26.812  60.790  23.473  1.000 84.465  0 19  SER CCC O   1 ? 11 
ATOM   2641 C CB  . SER C 3 19  ? 29.659  59.528  22.715  1.000 82.551  0 19  SER CCC CB  1 ? 11 
ATOM   2642 O OG  . SER C 3 19  ? 30.791  59.296  21.893  1.000 83.306  0 19  SER CCC OG  1 ? 11 
ATOM   2643 N N   . LEU C 3 20  ? 26.547  59.124  21.921  1.000 77.330  0 20  LEU CCC N   1 ? 11 
ATOM   2644 C CA  . LEU C 3 20  ? 25.227  58.606  22.368  1.000 75.411  0 20  LEU CCC CA  1 ? 11 
ATOM   2645 C C   . LEU C 3 20  ? 25.172  57.092  22.141  1.000 70.865  0 20  LEU CCC C   1 ? 11 
ATOM   2646 O O   . LEU C 3 20  ? 25.984  56.575  21.353  1.000 70.088  0 20  LEU CCC O   1 ? 11 
ATOM   2647 C CB  . LEU C 3 20  ? 24.117  59.318  21.590  1.000 77.368  0 20  LEU CCC CB  1 ? 11 
ATOM   2648 C CG  . LEU C 3 20  ? 23.798  60.744  22.034  1.000 82.542  0 20  LEU CCC CG  1 ? 11 
ATOM   2649 C CD1 . LEU C 3 20  ? 22.791  61.390  21.093  1.000 83.122  0 20  LEU CCC CD1 1 ? 11 
ATOM   2650 C CD2 . LEU C 3 20  ? 23.287  60.766  23.467  1.000 84.441  0 20  LEU CCC CD2 1 ? 11 
ATOM   2651 N N   . ARG C 3 21  ? 24.243  56.420  22.821  1.000 68.702  0 21  ARG CCC N   1 ? 11 
ATOM   2652 C CA  . ARG C 3 21  ? 24.049  54.948  22.776  1.000 65.280  0 21  ARG CCC CA  1 ? 11 
ATOM   2653 C C   . ARG C 3 21  ? 22.547  54.665  22.710  1.000 62.123  0 21  ARG CCC C   1 ? 11 
ATOM   2654 O O   . ARG C 3 21  ? 21.879  54.745  23.761  1.000 63.235  0 21  ARG CCC O   1 ? 11 
ATOM   2655 C CB  . ARG C 3 21  ? 24.698  54.298  24.002  1.000 67.942  0 21  ARG CCC CB  1 ? 11 
ATOM   2656 C CG  . ARG C 3 21  ? 24.546  52.784  24.097  1.000 67.158  0 21  ARG CCC CG  1 ? 11 
ATOM   2657 C CD  . ARG C 3 21  ? 25.241  52.292  25.357  1.000 72.246  0 21  ARG CCC CD  1 ? 11 
ATOM   2658 N NE  . ARG C 3 21  ? 24.526  51.312  26.171  1.000 73.929  0 21  ARG CCC NE  1 ? 11 
ATOM   2659 C CZ  . ARG C 3 21  ? 23.324  51.485  26.722  1.000 75.776  0 21  ARG CCC CZ  1 ? 11 
ATOM   2660 N NH1 . ARG C 3 21  ? 22.632  52.592  26.512  1.000 77.145  0 21  ARG CCC NH1 1 ? 11 
ATOM   2661 N NH2 . ARG C 3 21  ? 22.800  50.531  27.474  1.000 77.741  0 21  ARG CCC NH2 1 ? 11 
ATOM   2662 N N   . LEU C 3 22  ? 22.039  54.377  21.512  1.000 57.917  0 22  LEU CCC N   1 ? 11 
ATOM   2663 C CA  . LEU C 3 22  ? 20.661  53.865  21.307  1.000 54.402  0 22  LEU CCC CA  1 ? 11 
ATOM   2664 C C   . LEU C 3 22  ? 20.635  52.399  21.748  1.000 51.108  0 22  LEU CCC C   1 ? 11 
ATOM   2665 O O   . LEU C 3 22  ? 21.688  51.740  21.682  1.000 49.669  0 22  LEU CCC O   1 ? 11 
ATOM   2666 C CB  . LEU C 3 22  ? 20.260  54.030  19.836  1.000 53.328  0 22  LEU CCC CB  1 ? 11 
ATOM   2667 C CG  . LEU C 3 22  ? 19.706  55.401  19.442  1.000 56.083  0 22  LEU CCC CG  1 ? 11 
ATOM   2668 C CD1 . LEU C 3 22  ? 20.519  56.537  20.047  1.000 60.292  0 22  LEU CCC CD1 1 ? 11 
ATOM   2669 C CD2 . LEU C 3 22  ? 19.650  55.544  17.932  1.000 55.636  0 22  LEU CCC CD2 1 ? 11 
ATOM   2670 N N   . SER C 3 23  ? 19.474  51.928  22.203  1.000 51.323  0 23  SER CCC N   1 ? 11 
ATOM   2671 C CA  . SER C 3 23  ? 19.218  50.531  22.636  1.000 50.517  0 23  SER CCC CA  1 ? 11 
ATOM   2672 C C   . SER C 3 23  ? 18.013  49.981  21.879  1.000 47.475  0 23  SER CCC C   1 ? 11 
ATOM   2673 O O   . SER C 3 23  ? 17.058  50.751  21.677  1.000 46.850  0 23  SER CCC O   1 ? 11 
ATOM   2674 C CB  . SER C 3 23  ? 18.989  50.464  24.120  1.000 52.388  0 23  SER CCC CB  1 ? 11 
ATOM   2675 O OG  . SER C 3 23  ? 20.220  50.308  24.791  1.000 56.712  0 23  SER CCC OG  1 ? 11 
ATOM   2676 N N   . CYS C 3 24  ? 18.080  48.704  21.492  1.000 46.454  0 24  CYS CCC N   1 ? 11 
ATOM   2677 C CA  . CYS C 3 24  ? 16.967  47.928  20.885  1.000 46.449  0 24  CYS CCC CA  1 ? 11 
ATOM   2678 C C   . CYS C 3 24  ? 16.905  46.545  21.540  1.000 44.681  0 24  CYS CCC C   1 ? 11 
ATOM   2679 O O   . CYS C 3 24  ? 17.906  45.810  21.477  1.000 43.203  0 24  CYS CCC O   1 ? 11 
ATOM   2680 C CB  . CYS C 3 24  ? 17.128  47.802  19.376  1.000 46.416  0 24  CYS CCC CB  1 ? 11 
ATOM   2681 S SG  . CYS C 3 24  ? 15.603  47.287  18.546  1.000 50.680  0 24  CYS CCC SG  1 ? 11 
ATOM   2682 N N   . ALA C 3 25  ? 15.769  46.215  22.153  1.000 45.987  0 25  ALA CCC N   1 ? 11 
ATOM   2683 C CA  . ALA C 3 25  ? 15.557  44.966  22.919  1.000 46.630  0 25  ALA CCC CA  1 ? 11 
ATOM   2684 C C   . ALA C 3 25  ? 14.390  44.187  22.306  1.000 45.561  0 25  ALA CCC C   1 ? 11 
ATOM   2685 O O   . ALA C 3 25  ? 13.414  44.822  21.859  1.000 46.470  0 25  ALA CCC O   1 ? 11 
ATOM   2686 C CB  . ALA C 3 25  ? 15.323  45.280  24.377  1.000 49.232  0 25  ALA CCC CB  1 ? 11 
ATOM   2687 N N   . ALA C 3 26  ? 14.521  42.861  22.264  1.000 43.999  0 26  ALA CCC N   1 ? 11 
ATOM   2688 C CA  . ALA C 3 26  ? 13.524  41.902  21.737  1.000 43.195  0 26  ALA CCC CA  1 ? 11 
ATOM   2689 C C   . ALA C 3 26  ? 13.696  40.582  22.493  1.000 43.554  0 26  ALA CCC C   1 ? 11 
ATOM   2690 O O   . ALA C 3 26  ? 14.852  40.174  22.690  1.000 44.256  0 26  ALA CCC O   1 ? 11 
ATOM   2691 C CB  . ALA C 3 26  ? 13.719  41.732  20.248  1.000 41.639  0 26  ALA CCC CB  1 ? 11 
ATOM   2692 N N   . SER C 3 27  ? 12.605  39.954  22.926  1.000 44.516  0 27  SER CCC N   1 ? 11 
ATOM   2693 C CA  . SER C 3 27  ? 12.655  38.822  23.886  1.000 47.753  0 27  SER CCC CA  1 ? 11 
ATOM   2694 C C   . SER C 3 27  ? 13.283  37.596  23.216  1.000 45.494  0 27  SER CCC C   1 ? 11 
ATOM   2695 O O   . SER C 3 27  ? 13.067  37.392  22.004  1.000 44.664  0 27  SER CCC O   1 ? 11 
ATOM   2696 C CB  . SER C 3 27  ? 11.299  38.513  24.473  1.000 50.344  0 27  SER CCC CB  1 ? 11 
ATOM   2697 O OG  . SER C 3 27  ? 10.451  37.935  23.501  1.000 52.387  0 27  SER CCC OG  1 ? 11 
ATOM   2698 N N   . GLY C 3 28  ? 14.070  36.848  23.991  1.000 46.968  0 28  GLY CCC N   1 ? 11 
ATOM   2699 C CA  . GLY C 3 28  ? 14.537  35.491  23.659  1.000 48.395  0 28  GLY CCC CA  1 ? 11 
ATOM   2700 C C   . GLY C 3 28  ? 15.376  35.464  22.398  1.000 46.920  0 28  GLY CCC C   1 ? 11 
ATOM   2701 O O   . GLY C 3 28  ? 16.288  36.310  22.264  1.000 44.991  0 28  GLY CCC O   1 ? 11 
ATOM   2702 N N   . ARG C 3 29  ? 15.045  34.543  21.490  1.000 48.621  0 29  ARG CCC N   1 ? 11 
ATOM   2703 C CA  . ARG C 3 29  ? 15.897  34.127  20.344  1.000 47.286  0 29  ARG CCC CA  1 ? 11 
ATOM   2704 C C   . ARG C 3 29  ? 15.658  35.026  19.123  1.000 42.803  0 29  ARG CCC C   1 ? 11 
ATOM   2705 O O   . ARG C 3 29  ? 16.245  34.732  18.067  1.000 40.789  0 29  ARG CCC O   1 ? 11 
ATOM   2706 C CB  . ARG C 3 29  ? 15.634  32.649  20.040  1.000 51.414  0 29  ARG CCC CB  1 ? 11 
ATOM   2707 C CG  . ARG C 3 29  ? 15.967  31.734  21.211  1.000 57.824  0 29  ARG CCC CG  1 ? 11 
ATOM   2708 C CD  . ARG C 3 29  ? 16.141  30.267  20.851  1.000 64.290  0 29  ARG CCC CD  1 ? 11 
ATOM   2709 N NE  . ARG C 3 29  ? 16.626  29.491  21.993  1.000 70.667  0 29  ARG CCC NE  1 ? 11 
ATOM   2710 C CZ  . ARG C 3 29  ? 17.901  29.378  22.369  1.000 74.740  0 29  ARG CCC CZ  1 ? 11 
ATOM   2711 N NH1 . ARG C 3 29  ? 18.864  29.993  21.698  1.000 76.030  0 29  ARG CCC NH1 1 ? 11 
ATOM   2712 N NH2 . ARG C 3 29  ? 18.212  28.646  23.427  1.000 77.877  0 29  ARG CCC NH2 1 ? 11 
ATOM   2713 N N   . THR C 3 30  ? 14.867  36.097  19.263  1.000 41.176  0 30  THR CCC N   1 ? 11 
ATOM   2714 C CA  . THR C 3 30  ? 14.517  37.031  18.156  1.000 39.376  0 30  THR CCC CA  1 ? 11 
ATOM   2715 C C   . THR C 3 30  ? 15.788  37.472  17.410  1.000 38.681  0 30  THR CCC C   1 ? 11 
ATOM   2716 O O   . THR C 3 30  ? 15.889  37.185  16.192  1.000 38.469  0 30  THR CCC O   1 ? 11 
ATOM   2717 C CB  . THR C 3 30  ? 13.726  38.245  18.658  1.000 38.274  0 30  THR CCC CB  1 ? 11 
ATOM   2718 O OG1 . THR C 3 30  ? 12.516  37.777  19.250  1.000 39.276  0 30  THR CCC OG1 1 ? 11 
ATOM   2719 C CG2 . THR C 3 30  ? 13.400  39.228  17.555  1.000 37.013  0 30  THR CCC CG2 1 ? 11 
ATOM   2720 N N   . PHE C 3 31  ? 16.717  38.148  18.100  1.000 38.186  0 31  PHE CCC N   1 ? 11 
ATOM   2721 C CA  . PHE C 3 31  ? 17.947  38.726  17.491  1.000 37.828  0 31  PHE CCC CA  1 ? 11 
ATOM   2722 C C   . PHE C 3 31  ? 18.906  37.610  17.063  1.000 37.319  0 31  PHE CCC C   1 ? 11 
ATOM   2723 O O   . PHE C 3 31  ? 19.754  37.871  16.196  1.000 36.221  0 31  PHE CCC O   1 ? 11 
ATOM   2724 C CB  . PHE C 3 31  ? 18.646  39.708  18.435  1.000 37.762  0 31  PHE CCC CB  1 ? 11 
ATOM   2725 C CG  . PHE C 3 31  ? 17.975  41.053  18.561  1.000 38.700  0 31  PHE CCC CG  1 ? 11 
ATOM   2726 C CD1 . PHE C 3 31  ? 17.420  41.695  17.459  1.000 38.864  0 31  PHE CCC CD1 1 ? 11 
ATOM   2727 C CD2 . PHE C 3 31  ? 17.906  41.682  19.793  1.000 40.490  0 31  PHE CCC CD2 1 ? 11 
ATOM   2728 C CE1 . PHE C 3 31  ? 16.808  42.933  17.593  1.000 39.304  0 31  PHE CCC CE1 1 ? 11 
ATOM   2729 C CE2 . PHE C 3 31  ? 17.293  42.920  19.925  1.000 41.099  0 31  PHE CCC CE2 1 ? 11 
ATOM   2730 C CZ  . PHE C 3 31  ? 16.751  43.546  18.824  1.000 41.212  0 31  PHE CCC CZ  1 ? 11 
ATOM   2731 N N   . SER C 3 32  ? 18.767  36.420  17.651  1.000 37.920  0 32  SER CCC N   1 ? 11 
ATOM   2732 C CA  . SER C 3 32  ? 19.538  35.197  17.309  1.000 38.958  0 32  SER CCC CA  1 ? 11 
ATOM   2733 C C   . SER C 3 32  ? 18.960  34.518  16.062  1.000 38.162  0 32  SER CCC C   1 ? 11 
ATOM   2734 O O   . SER C 3 32  ? 19.624  33.617  15.543  1.000 40.086  0 32  SER CCC O   1 ? 11 
ATOM   2735 C CB  . SER C 3 32  ? 19.588  34.245  18.475  1.000 41.281  0 32  SER CCC CB  1 ? 11 
ATOM   2736 O OG  . SER C 3 32  ? 20.577  34.658  19.407  1.000 43.529  0 32  SER CCC OG  1 ? 11 
ATOM   2737 N N   . THR C 3 33  ? 17.774  34.933  15.606  1.000 38.082  0 33  THR CCC N   1 ? 11 
ATOM   2738 C CA  . THR C 3 33  ? 17.040  34.343  14.456  1.000 38.117  0 33  THR CCC CA  1 ? 11 
ATOM   2739 C C   . THR C 3 33  ? 16.992  35.320  13.275  1.000 38.824  0 33  THR CCC C   1 ? 11 
ATOM   2740 O O   . THR C 3 33  ? 17.054  34.841  12.129  1.000 40.522  0 33  THR CCC O   1 ? 11 
ATOM   2741 C CB  . THR C 3 33  ? 15.614  33.961  14.860  1.000 38.477  0 33  THR CCC CB  1 ? 11 
ATOM   2742 O OG1 . THR C 3 33  ? 15.718  33.146  16.029  1.000 38.847  0 33  THR CCC OG1 1 ? 11 
ATOM   2743 C CG2 . THR C 3 33  ? 14.864  33.240  13.759  1.000 39.254  0 33  THR CCC CG2 1 ? 11 
ATOM   2744 N N   . TYR C 3 34  ? 16.850  36.623  13.536  1.000 38.346  0 34  TYR CCC N   1 ? 11 
ATOM   2745 C CA  . TYR C 3 34  ? 16.646  37.663  12.495  1.000 39.974  0 34  TYR CCC CA  1 ? 11 
ATOM   2746 C C   . TYR C 3 34  ? 17.675  38.779  12.669  1.000 40.020  0 34  TYR CCC C   1 ? 11 
ATOM   2747 O O   . TYR C 3 34  ? 17.715  39.391  13.750  1.000 43.792  0 34  TYR CCC O   1 ? 11 
ATOM   2748 C CB  . TYR C 3 34  ? 15.225  38.230  12.563  1.000 40.746  0 34  TYR CCC CB  1 ? 11 
ATOM   2749 C CG  . TYR C 3 34  ? 14.139  37.189  12.520  1.000 41.732  0 34  TYR CCC CG  1 ? 11 
ATOM   2750 C CD1 . TYR C 3 34  ? 13.954  36.404  11.391  1.000 42.314  0 34  TYR CCC CD1 1 ? 11 
ATOM   2751 C CD2 . TYR C 3 34  ? 13.295  36.984  13.603  1.000 42.003  0 34  TYR CCC CD2 1 ? 11 
ATOM   2752 C CE1 . TYR C 3 34  ? 12.956  35.443  11.338  1.000 42.945  0 34  TYR CCC CE1 1 ? 11 
ATOM   2753 C CE2 . TYR C 3 34  ? 12.294  36.025  13.566  1.000 42.564  0 34  TYR CCC CE2 1 ? 11 
ATOM   2754 C CZ  . TYR C 3 34  ? 12.126  35.253  12.429  1.000 43.672  0 34  TYR CCC CZ  1 ? 11 
ATOM   2755 O OH  . TYR C 3 34  ? 11.154  34.299  12.380  1.000 46.598  0 34  TYR CCC OH  1 ? 11 
ATOM   2756 N N   . SER C 3 35  ? 18.456  39.041  11.620  1.000 40.171  0 35  SER CCC N   1 ? 11 
ATOM   2757 C CA  . SER C 3 35  ? 19.375  40.199  11.522  1.000 39.729  0 35  SER CCC CA  1 ? 11 
ATOM   2758 C C   . SER C 3 35  ? 18.590  41.481  11.807  1.000 38.387  0 35  SER CCC C   1 ? 11 
ATOM   2759 O O   . SER C 3 35  ? 17.432  41.581  11.375  1.000 39.654  0 35  SER CCC O   1 ? 11 
ATOM   2760 C CB  . SER C 3 35  ? 20.050  40.251  10.177  1.000 41.818  0 35  SER CCC CB  1 ? 11 
ATOM   2761 O OG  . SER C 3 35  ? 20.878  39.112  9.979   1.000 42.379  0 35  SER CCC OG  1 ? 11 
ATOM   2762 N N   . MET C 3 36  ? 19.204  42.421  12.516  1.000 39.048  0 36  MET CCC N   1 ? 11 
ATOM   2763 C CA  . MET C 3 36  ? 18.571  43.705  12.908  1.000 39.289  0 36  MET CCC CA  1 ? 11 
ATOM   2764 C C   . MET C 3 36  ? 19.262  44.851  12.163  1.000 40.890  0 36  MET CCC C   1 ? 11 
ATOM   2765 O O   . MET C 3 36  ? 20.443  44.698  11.772  1.000 40.890  0 36  MET CCC O   1 ? 11 
ATOM   2766 C CB  . MET C 3 36  ? 18.650  43.914  14.427  1.000 40.335  0 36  MET CCC CB  1 ? 11 
ATOM   2767 C CG  . MET C 3 36  ? 20.044  44.253  14.942  1.000 39.943  0 36  MET CCC CG  1 ? 11 
ATOM   2768 S SD  . MET C 3 36  ? 20.500  45.996  14.732  1.000 40.953  0 36  MET CCC SD  1 ? 11 
ATOM   2769 C CE  . MET C 3 36  ? 19.043  46.838  15.346  1.000 42.073  0 36  MET CCC CE  1 ? 11 
ATOM   2770 N N   . GLY C 3 37  ? 18.541  45.953  11.966  1.000 41.606  0 37  GLY CCC N   1 ? 11 
ATOM   2771 C CA  . GLY C 3 37  ? 19.035  47.155  11.271  1.000 43.295  0 37  GLY CCC CA  1 ? 11 
ATOM   2772 C C   . GLY C 3 37  ? 18.658  48.423  12.015  1.000 43.143  0 37  GLY CCC C   1 ? 11 
ATOM   2773 O O   . GLY C 3 37  ? 17.526  48.506  12.520  1.000 41.816  0 37  GLY CCC O   1 ? 11 
ATOM   2774 N N   . TRP C 3 38  ? 19.589  49.372  12.092  1.000 44.784  0 38  TRP CCC N   1 ? 11 
ATOM   2775 C CA  . TRP C 3 38  ? 19.331  50.762  12.544  1.000 46.843  0 38  TRP CCC CA  1 ? 11 
ATOM   2776 C C   . TRP C 3 38  ? 19.098  51.636  11.312  1.000 47.620  0 38  TRP CCC C   1 ? 11 
ATOM   2777 O O   . TRP C 3 38  ? 19.923  51.569  10.375  1.000 50.820  0 38  TRP CCC O   1 ? 11 
ATOM   2778 C CB  . TRP C 3 38  ? 20.490  51.283  13.401  1.000 48.695  0 38  TRP CCC CB  1 ? 11 
ATOM   2779 C CG  . TRP C 3 38  ? 20.603  50.616  14.735  1.000 47.494  0 38  TRP CCC CG  1 ? 11 
ATOM   2780 C CD1 . TRP C 3 38  ? 21.451  49.607  15.087  1.000 47.223  0 38  TRP CCC CD1 1 ? 11 
ATOM   2781 C CD2 . TRP C 3 38  ? 19.826  50.917  15.907  1.000 48.483  0 38  TRP CCC CD2 1 ? 11 
ATOM   2782 N NE1 . TRP C 3 38  ? 21.267  49.268  16.403  1.000 47.457  0 38  TRP CCC NE1 1 ? 11 
ATOM   2783 C CE2 . TRP C 3 38  ? 20.276  50.055  16.932  1.000 48.100  0 38  TRP CCC CE2 1 ? 11 
ATOM   2784 C CE3 . TRP C 3 38  ? 18.818  51.844  16.197  1.000 48.978  0 38  TRP CCC CE3 1 ? 11 
ATOM   2785 C CZ2 . TRP C 3 38  ? 19.736  50.084  18.216  1.000 48.300  0 38  TRP CCC CZ2 1 ? 11 
ATOM   2786 C CZ3 . TRP C 3 38  ? 18.281  51.869  17.466  1.000 50.270  0 38  TRP CCC CZ3 1 ? 11 
ATOM   2787 C CH2 . TRP C 3 38  ? 18.735  50.997  18.459  1.000 49.673  0 38  TRP CCC CH2 1 ? 11 
ATOM   2788 N N   . PHE C 3 39  ? 17.992  52.380  11.303  1.000 47.776  0 39  PHE CCC N   1 ? 11 
ATOM   2789 C CA  . PHE C 3 39  ? 17.634  53.381  10.264  1.000 49.337  0 39  PHE CCC CA  1 ? 11 
ATOM   2790 C C   . PHE C 3 39  ? 17.442  54.743  10.934  1.000 51.518  0 39  PHE CCC C   1 ? 11 
ATOM   2791 O O   . PHE C 3 39  ? 17.273  54.794  12.170  1.000 51.398  0 39  PHE CCC O   1 ? 11 
ATOM   2792 C CB  . PHE C 3 39  ? 16.368  52.959  9.519   1.000 48.411  0 39  PHE CCC CB  1 ? 11 
ATOM   2793 C CG  . PHE C 3 39  ? 16.526  51.716  8.687   1.000 46.148  0 39  PHE CCC CG  1 ? 11 
ATOM   2794 C CD1 . PHE C 3 39  ? 16.548  50.463  9.279   1.000 42.567  0 39  PHE CCC CD1 1 ? 11 
ATOM   2795 C CD2 . PHE C 3 39  ? 16.646  51.800  7.307   1.000 48.124  0 39  PHE CCC CD2 1 ? 11 
ATOM   2796 C CE1 . PHE C 3 39  ? 16.706  49.321  8.508   1.000 42.688  0 39  PHE CCC CE1 1 ? 11 
ATOM   2797 C CE2 . PHE C 3 39  ? 16.793  50.655  6.538   1.000 46.716  0 39  PHE CCC CE2 1 ? 11 
ATOM   2798 C CZ  . PHE C 3 39  ? 16.819  49.419  7.137   1.000 44.173  0 39  PHE CCC CZ  1 ? 11 
ATOM   2799 N N   . ARG C 3 40  ? 17.481  55.811  10.139  1.000 54.601  0 40  ARG CCC N   1 ? 11 
ATOM   2800 C CA  . ARG C 3 40  ? 17.239  57.198  10.612  1.000 57.382  0 40  ARG CCC CA  1 ? 11 
ATOM   2801 C C   . ARG C 3 40  ? 16.432  57.950  9.552   1.000 60.741  0 40  ARG CCC C   1 ? 11 
ATOM   2802 O O   . ARG C 3 40  ? 16.585  57.636  8.359   1.000 61.431  0 40  ARG CCC O   1 ? 11 
ATOM   2803 C CB  . ARG C 3 40  ? 18.561  57.898  10.934  1.000 58.669  0 40  ARG CCC CB  1 ? 11 
ATOM   2804 C CG  . ARG C 3 40  ? 19.434  58.218  9.729   1.000 60.810  0 40  ARG CCC CG  1 ? 11 
ATOM   2805 C CD  . ARG C 3 40  ? 20.784  58.708  10.209  1.000 62.846  0 40  ARG CCC CD  1 ? 11 
ATOM   2806 N NE  . ARG C 3 40  ? 21.742  58.981  9.150   1.000 65.708  0 40  ARG CCC NE  1 ? 11 
ATOM   2807 C CZ  . ARG C 3 40  ? 22.999  59.375  9.352   1.000 67.643  0 40  ARG CCC CZ  1 ? 11 
ATOM   2808 N NH1 . ARG C 3 40  ? 23.464  59.550  10.579  1.000 66.869  0 40  ARG CCC NH1 1 ? 11 
ATOM   2809 N NH2 . ARG C 3 40  ? 23.788  59.602  8.317   1.000 70.712  0 40  ARG CCC NH2 1 ? 11 
ATOM   2810 N N   . GLN C 3 41  ? 15.597  58.893  9.996   1.000 62.855  0 41  GLN CCC N   1 ? 11 
ATOM   2811 C CA  . GLN C 3 41  ? 14.741  59.747  9.137   1.000 66.603  0 41  GLN CCC CA  1 ? 11 
ATOM   2812 C C   . GLN C 3 41  ? 14.837  61.190  9.640   1.000 70.994  0 41  GLN CCC C   1 ? 11 
ATOM   2813 O O   . GLN C 3 41  ? 14.374  61.449  10.763  1.000 71.012  0 41  GLN CCC O   1 ? 11 
ATOM   2814 C CB  . GLN C 3 41  ? 13.304  59.226  9.155   1.000 65.721  0 41  GLN CCC CB  1 ? 11 
ATOM   2815 C CG  . GLN C 3 41  ? 12.398  59.908  8.137   1.000 69.963  0 41  GLN CCC CG  1 ? 11 
ATOM   2816 C CD  . GLN C 3 41  ? 11.173  59.093  7.802   1.000 69.312  0 41  GLN CCC CD  1 ? 11 
ATOM   2817 O OE1 . GLN C 3 41  ? 10.777  58.198  8.547   1.000 66.084  0 41  GLN CCC OE1 1 ? 11 
ATOM   2818 N NE2 . GLN C 3 41  ? 10.564  59.392  6.666   1.000 72.857  0 41  GLN CCC NE2 1 ? 11 
ATOM   2819 N N   . ALA C 3 42  ? 15.453  62.072  8.846   1.000 75.849  0 42  ALA CCC N   1 ? 11 
ATOM   2820 C CA  . ALA C 3 42  ? 15.497  63.540  9.059   1.000 81.321  0 42  ALA CCC CA  1 ? 11 
ATOM   2821 C C   . ALA C 3 42  ? 14.206  64.144  8.507   1.000 85.513  0 42  ALA CCC C   1 ? 11 
ATOM   2822 O O   . ALA C 3 42  ? 13.605  63.560  7.612   1.000 84.929  0 42  ALA CCC O   1 ? 11 
ATOM   2823 C CB  . ALA C 3 42  ? 16.726  64.119  8.398   1.000 83.575  0 42  ALA CCC CB  1 ? 11 
ATOM   2824 N N   . PRO C 3 43  ? 13.760  65.325  8.999   1.000 90.558  0 43  PRO CCC N   1 ? 11 
ATOM   2825 C CA  . PRO C 3 43  ? 12.398  65.818  8.764   1.000 94.716  0 43  PRO CCC CA  1 ? 11 
ATOM   2826 C C   . PRO C 3 43  ? 11.782  65.561  7.379   1.000 97.366  0 43  PRO CCC C   1 ? 11 
ATOM   2827 O O   . PRO C 3 43  ? 10.747  64.917  7.331   1.000 96.618  0 43  PRO CCC O   1 ? 11 
ATOM   2828 C CB  . PRO C 3 43  ? 12.554  67.329  9.000   1.000 99.699  0 43  PRO CCC CB  1 ? 11 
ATOM   2829 C CG  . PRO C 3 43  ? 13.596  67.406  10.089  1.000 97.589  0 43  PRO CCC CG  1 ? 11 
ATOM   2830 C CD  . PRO C 3 43  ? 14.553  66.267  9.804   1.000 92.658  0 43  PRO CCC CD  1 ? 11 
ATOM   2831 N N   . GLY C 3 44  ? 12.400  66.070  6.306   1.000 101.628 0 44  GLY CCC N   1 ? 11 
ATOM   2832 C CA  . GLY C 3 44  ? 11.911  65.946  4.917   1.000 105.284 0 44  GLY CCC CA  1 ? 11 
ATOM   2833 C C   . GLY C 3 44  ? 12.813  65.051  4.082   1.000 104.162 0 44  GLY CCC C   1 ? 11 
ATOM   2834 O O   . GLY C 3 44  ? 13.347  65.542  3.060   1.000 107.952 0 44  GLY CCC O   1 ? 11 
ATOM   2835 N N   . LYS C 3 45  ? 12.986  63.789  4.492   1.000 99.968  0 45  LYS CCC N   1 ? 11 
ATOM   2836 C CA  . LYS C 3 45  ? 13.908  62.815  3.844   1.000 97.879  0 45  LYS CCC CA  1 ? 11 
ATOM   2837 C C   . LYS C 3 45  ? 13.384  61.385  4.013   1.000 93.528  0 45  LYS CCC C   1 ? 11 
ATOM   2838 O O   . LYS C 3 45  ? 12.487  61.166  4.855   1.000 90.897  0 45  LYS CCC O   1 ? 11 
ATOM   2839 C CB  . LYS C 3 45  ? 15.310  62.911  4.455   1.000 97.625  0 45  LYS CCC CB  1 ? 11 
ATOM   2840 C CG  . LYS C 3 45  ? 16.164  64.075  3.975   1.000 103.258 0 45  LYS CCC CG  1 ? 11 
ATOM   2841 C CD  . LYS C 3 45  ? 17.622  63.917  4.367   1.000 102.845 0 45  LYS CCC CD  1 ? 11 
ATOM   2842 C CE  . LYS C 3 45  ? 18.381  65.224  4.444   1.000 108.649 0 45  LYS CCC CE  1 ? 11 
ATOM   2843 N NZ  . LYS C 3 45  ? 19.613  65.082  5.257   1.000 107.494 0 45  LYS CCC NZ  1 ? 11 
ATOM   2844 N N   . GLU C 3 46  ? 13.961  60.454  3.249   1.000 93.116  0 46  GLU CCC N   1 ? 11 
ATOM   2845 C CA  . GLU C 3 46  ? 13.611  59.009  3.250   1.000 90.501  0 46  GLU CCC CA  1 ? 11 
ATOM   2846 C C   . GLU C 3 46  ? 14.313  58.322  4.431   1.000 84.168  0 46  GLU CCC C   1 ? 11 
ATOM   2847 O O   . GLU C 3 46  ? 15.346  58.842  4.900   1.000 82.873  0 46  GLU CCC O   1 ? 11 
ATOM   2848 C CB  . GLU C 3 46  ? 14.002  58.387  1.905   1.000 92.801  0 46  GLU CCC CB  1 ? 11 
ATOM   2849 C CG  . GLU C 3 46  ? 13.477  56.976  1.695   1.000 91.620  0 46  GLU CCC CG  1 ? 11 
ATOM   2850 C CD  . GLU C 3 46  ? 11.961  56.844  1.696   1.000 94.375  0 46  GLU CCC CD  1 ? 11 
ATOM   2851 O OE1 . GLU C 3 46  ? 11.317  57.375  0.761   1.000 99.032  0 46  GLU CCC OE1 1 ? 11 
ATOM   2852 O OE2 . GLU C 3 46  ? 11.427  56.216  2.637   1.000 89.967  0 46  GLU CCC OE2 1 ? 11 
ATOM   2853 N N   . ARG C 3 47  ? 13.752  57.205  4.900   1.000 72.783  0 47  ARG CCC N   1 ? 12 
ATOM   2854 C CA  . ARG C 3 47  ? 14.323  56.364  5.984   1.000 69.464  0 47  ARG CCC CA  1 ? 12 
ATOM   2855 C C   . ARG C 3 47  ? 15.558  55.640  5.430   1.000 68.420  0 47  ARG CCC C   1 ? 12 
ATOM   2856 O O   . ARG C 3 47  ? 15.386  54.610  4.756   1.000 67.429  0 47  ARG CCC O   1 ? 12 
ATOM   2857 C CB  . ARG C 3 47  ? 13.262  55.392  6.511   1.000 68.118  0 47  ARG CCC CB  1 ? 12 
ATOM   2858 C CG  . ARG C 3 47  ? 13.339  55.129  8.008   1.000 67.820  0 47  ARG CCC CG  1 ? 12 
ATOM   2859 C CD  . ARG C 3 47  ? 12.229  54.227  8.515   1.000 67.307  0 47  ARG CCC CD  1 ? 12 
ATOM   2860 N NE  . ARG C 3 47  ? 11.099  54.939  9.103   1.000 68.716  0 47  ARG CCC NE  1 ? 12 
ATOM   2861 C CZ  . ARG C 3 47  ? 10.066  54.352  9.704   1.000 68.407  0 47  ARG CCC CZ  1 ? 12 
ATOM   2862 N NH1 . ARG C 3 47  ? 10.013  53.035  9.824   1.000 67.708  0 47  ARG CCC NH1 1 ? 12 
ATOM   2863 N NH2 . ARG C 3 47  ? 9.090   55.085  10.212  1.000 70.372  0 47  ARG CCC NH2 1 ? 12 
ATOM   2864 N N   . GLU C 3 48  ? 16.756  56.166  5.702   1.000 66.792  0 48  GLU CCC N   1 ? 12 
ATOM   2865 C CA  . GLU C 3 48  ? 18.037  55.625  5.174   1.000 64.690  0 48  GLU CCC CA  1 ? 12 
ATOM   2866 C C   . GLU C 3 48  ? 18.647  54.663  6.201   1.000 59.669  0 48  GLU CCC C   1 ? 12 
ATOM   2867 O O   . GLU C 3 48  ? 18.533  54.923  7.422   1.000 59.199  0 48  GLU CCC O   1 ? 12 
ATOM   2868 C CB  . GLU C 3 48  ? 18.987  56.762  4.787   1.000 68.847  0 48  GLU CCC CB  1 ? 12 
ATOM   2869 C CG  . GLU C 3 48  ? 19.505  57.589  5.951   1.000 70.076  0 48  GLU CCC CG  1 ? 12 
ATOM   2870 C CD  . GLU C 3 48  ? 20.530  58.638  5.550   1.000 74.398  0 48  GLU CCC CD  1 ? 12 
ATOM   2871 O OE1 . GLU C 3 48  ? 20.488  59.095  4.384   1.000 76.737  0 48  GLU CCC OE1 1 ? 12 
ATOM   2872 O OE2 . GLU C 3 48  ? 21.374  58.990  6.397   1.000 73.905  0 48  GLU CCC OE2 1 ? 12 
ATOM   2873 N N   . PHE C 3 49  ? 19.260  53.583  5.710   1.000 55.972  0 49  PHE CCC N   1 ? 12 
ATOM   2874 C CA  . PHE C 3 49  ? 20.004  52.583  6.518   1.000 52.413  0 49  PHE CCC CA  1 ? 12 
ATOM   2875 C C   . PHE C 3 49  ? 21.206  53.256  7.191   1.000 52.324  0 49  PHE CCC C   1 ? 12 
ATOM   2876 O O   . PHE C 3 49  ? 21.868  54.087  6.539   1.000 53.604  0 49  PHE CCC O   1 ? 12 
ATOM   2877 C CB  . PHE C 3 49  ? 20.464  51.412  5.648   1.000 50.742  0 49  PHE CCC CB  1 ? 12 
ATOM   2878 C CG  . PHE C 3 49  ? 21.317  50.426  6.399   1.000 49.111  0 49  PHE CCC CG  1 ? 12 
ATOM   2879 C CD1 . PHE C 3 49  ? 20.749  49.560  7.317   1.000 47.014  0 49  PHE CCC CD1 1 ? 12 
ATOM   2880 C CD2 . PHE C 3 49  ? 22.691  50.403  6.232   1.000 50.900  0 49  PHE CCC CD2 1 ? 12 
ATOM   2881 C CE1 . PHE C 3 49  ? 21.532  48.669  8.030   1.000 46.703  0 49  PHE CCC CE1 1 ? 12 
ATOM   2882 C CE2 . PHE C 3 49  ? 23.475  49.510  6.946   1.000 49.219  0 49  PHE CCC CE2 1 ? 12 
ATOM   2883 C CZ  . PHE C 3 49  ? 22.894  48.647  7.844   1.000 46.880  0 49  PHE CCC CZ  1 ? 12 
ATOM   2884 N N   . VAL C 3 50  ? 21.489  52.889  8.446   1.000 49.982  0 50  VAL CCC N   1 ? 12 
ATOM   2885 C CA  . VAL C 3 50  ? 22.623  53.436  9.250   1.000 50.493  0 50  VAL CCC CA  1 ? 12 
ATOM   2886 C C   . VAL C 3 50  ? 23.635  52.316  9.509   1.000 48.828  0 50  VAL CCC C   1 ? 12 
ATOM   2887 O O   . VAL C 3 50  ? 24.782  52.417  9.020   1.000 51.227  0 50  VAL CCC O   1 ? 12 
ATOM   2888 C CB  . VAL C 3 50  ? 22.122  54.059  10.566  1.000 50.992  0 50  VAL CCC CB  1 ? 12 
ATOM   2889 C CG1 . VAL C 3 50  ? 23.271  54.541  11.435  1.000 52.305  0 50  VAL CCC CG1 1 ? 12 
ATOM   2890 C CG2 . VAL C 3 50  ? 21.136  55.189  10.316  1.000 53.224  0 50  VAL CCC CG2 1 ? 12 
ATOM   2891 N N   . ALA C 3 51  ? 23.224  51.293  10.259  1.000 45.947  0 51  ALA CCC N   1 ? 12 
ATOM   2892 C CA  . ALA C 3 51  ? 24.086  50.183  10.725  1.000 44.077  0 51  ALA CCC CA  1 ? 12 
ATOM   2893 C C   . ALA C 3 51  ? 23.207  48.987  11.096  1.000 42.242  0 51  ALA CCC C   1 ? 12 
ATOM   2894 O O   . ALA C 3 51  ? 22.014  49.201  11.399  1.000 42.575  0 51  ALA CCC O   1 ? 12 
ATOM   2895 C CB  . ALA C 3 51  ? 24.924  50.638  11.891  1.000 43.507  0 51  ALA CCC CB  1 ? 12 
ATOM   2896 N N   . GLY C 3 52  ? 23.771  47.777  11.060  1.000 41.415  0 52  GLY CCC N   1 ? 12 
ATOM   2897 C CA  . GLY C 3 52  ? 23.040  46.528  11.341  1.000 40.668  0 52  GLY CCC CA  1 ? 12 
ATOM   2898 C C   . GLY C 3 52  ? 23.945  45.461  11.920  1.000 40.075  0 52  GLY CCC C   1 ? 12 
ATOM   2899 O O   . GLY C 3 52  ? 25.185  45.653  11.909  1.000 39.281  0 52  GLY CCC O   1 ? 12 
ATOM   2900 N N   . MET C 3 53  ? 23.343  44.381  12.422  1.000 39.772  0 53  MET CCC N   1 ? 12 
ATOM   2901 C CA  . MET C 3 53  ? 24.066  43.186  12.934  1.000 40.312  0 53  MET CCC CA  1 ? 12 
ATOM   2902 C C   . MET C 3 53  ? 23.336  41.924  12.459  1.000 39.219  0 53  MET CCC C   1 ? 12 
ATOM   2903 O O   . MET C 3 53  ? 22.092  41.876  12.580  1.000 39.028  0 53  MET CCC O   1 ? 12 
ATOM   2904 C CB  . MET C 3 53  ? 24.145  43.200  14.466  1.000 39.362  0 53  MET CCC CB  1 ? 12 
ATOM   2905 C CG  . MET C 3 53  ? 24.952  42.053  15.043  1.000 40.273  0 53  MET CCC CG  1 ? 12 
ATOM   2906 S SD  . MET C 3 53  ? 24.961  42.050  16.857  1.000 42.514  0 53  MET CCC SD  1 ? 12 
ATOM   2907 C CE  . MET C 3 53  ? 26.499  42.908  17.190  1.000 43.365  0 53  MET CCC CE  1 ? 12 
ATOM   2908 N N   . ARG C 3 54  ? 24.092  40.951  11.942  1.000 39.092  0 54  ARG CCC N   1 ? 12 
ATOM   2909 C CA  . ARG C 3 54  ? 23.578  39.606  11.571  1.000 38.864  0 54  ARG CCC CA  1 ? 12 
ATOM   2910 C C   . ARG C 3 54  ? 23.142  38.876  12.847  1.000 39.323  0 54  ARG CCC C   1 ? 12 
ATOM   2911 O O   . ARG C 3 54  ? 23.716  39.160  13.921  1.000 40.050  0 54  ARG CCC O   1 ? 12 
ATOM   2912 C CB  . ARG C 3 54  ? 24.640  38.804  10.811  1.000 38.840  0 54  ARG CCC CB  1 ? 12 
ATOM   2913 C CG  . ARG C 3 54  ? 25.122  39.454  9.520   1.000 38.529  0 54  ARG CCC CG  1 ? 12 
ATOM   2914 C CD  . ARG C 3 54  ? 24.046  39.557  8.450   1.000 38.914  0 54  ARG CCC CD  1 ? 12 
ATOM   2915 N NE  . ARG C 3 54  ? 24.594  40.151  7.235   1.000 39.262  0 54  ARG CCC NE  1 ? 12 
ATOM   2916 C CZ  . ARG C 3 54  ? 23.993  40.191  6.050   1.000 39.097  0 54  ARG CCC CZ  1 ? 12 
ATOM   2917 N NH1 . ARG C 3 54  ? 22.787  39.667  5.891   1.000 39.920  0 54  ARG CCC NH1 1 ? 12 
ATOM   2918 N NH2 . ARG C 3 54  ? 24.601  40.764  5.022   1.000 38.914  0 54  ARG CCC NH2 1 ? 12 
ATOM   2919 N N   . TRP C 3 55  ? 22.196  37.943  12.722  1.000 40.165  0 55  TRP CCC N   1 ? 12 
ATOM   2920 C CA  . TRP C 3 55  ? 21.644  37.136  13.844  1.000 40.939  0 55  TRP CCC CA  1 ? 12 
ATOM   2921 C C   . TRP C 3 55  ? 22.777  36.408  14.578  1.000 40.500  0 55  TRP CCC C   1 ? 12 
ATOM   2922 O O   . TRP C 3 55  ? 22.560  35.997  15.728  1.000 41.676  0 55  TRP CCC O   1 ? 12 
ATOM   2923 C CB  . TRP C 3 55  ? 20.590  36.139  13.343  1.000 42.715  0 55  TRP CCC CB  1 ? 12 
ATOM   2924 C CG  . TRP C 3 55  ? 21.174  34.965  12.616  1.000 44.289  0 55  TRP CCC CG  1 ? 12 
ATOM   2925 C CD1 . TRP C 3 55  ? 21.807  33.884  13.161  1.000 44.238  0 55  TRP CCC CD1 1 ? 12 
ATOM   2926 C CD2 . TRP C 3 55  ? 21.174  34.751  11.196  1.000 44.383  0 55  TRP CCC CD2 1 ? 12 
ATOM   2927 N NE1 . TRP C 3 55  ? 22.207  33.019  12.181  1.000 45.552  0 55  TRP CCC NE1 1 ? 12 
ATOM   2928 C CE2 . TRP C 3 55  ? 21.822  33.518  10.965  1.000 45.014  0 55  TRP CCC CE2 1 ? 12 
ATOM   2929 C CE3 . TRP C 3 55  ? 20.682  35.474  10.106  1.000 43.229  0 55  TRP CCC CE3 1 ? 12 
ATOM   2930 C CZ2 . TRP C 3 55  ? 21.985  32.994  9.687   1.000 45.343  0 55  TRP CCC CZ2 1 ? 12 
ATOM   2931 C CZ3 . TRP C 3 55  ? 20.849  34.956  8.843   1.000 45.058  0 55  TRP CCC CZ3 1 ? 12 
ATOM   2932 C CH2 . TRP C 3 55  ? 21.493  33.736  8.639   1.000 46.018  0 55  TRP CCC CH2 1 ? 12 
ATOM   2933 N N   . THR C 3 56  ? 23.919  36.223  13.914  1.000 39.024  0 56  THR CCC N   1 ? 12 
ATOM   2934 C CA  . THR C 3 56  ? 25.100  35.474  14.417  1.000 40.984  0 56  THR CCC CA  1 ? 12 
ATOM   2935 C C   . THR C 3 56  ? 25.763  36.215  15.585  1.000 41.723  0 56  THR CCC C   1 ? 12 
ATOM   2936 O O   . THR C 3 56  ? 26.392  35.543  16.413  1.000 43.467  0 56  THR CCC O   1 ? 12 
ATOM   2937 C CB  . THR C 3 56  ? 26.129  35.273  13.301  1.000 39.743  0 56  THR CCC CB  1 ? 12 
ATOM   2938 O OG1 . THR C 3 56  ? 26.519  36.571  12.853  1.000 39.541  0 56  THR CCC OG1 1 ? 12 
ATOM   2939 C CG2 . THR C 3 56  ? 25.593  34.468  12.143  1.000 40.635  0 56  THR CCC CG2 1 ? 12 
ATOM   2940 N N   . GLY C 3 57  ? 25.666  37.548  15.610  1.000 41.558  0 57  GLY CCC N   1 ? 12 
ATOM   2941 C CA  . GLY C 3 57  ? 26.377  38.419  16.565  1.000 42.031  0 57  GLY CCC CA  1 ? 12 
ATOM   2942 C C   . GLY C 3 57  ? 27.832  38.657  16.172  1.000 42.410  0 57  GLY CCC C   1 ? 12 
ATOM   2943 O O   . GLY C 3 57  ? 28.485  39.480  16.850  1.000 42.547  0 57  GLY CCC O   1 ? 12 
ATOM   2944 N N   . SER C 3 58  ? 28.328  37.988  15.121  1.000 39.830  0 58  SER CCC N   1 ? 12 
ATOM   2945 C CA  . SER C 3 58  ? 29.766  37.963  14.736  1.000 41.090  0 58  SER CCC CA  1 ? 12 
ATOM   2946 C C   . SER C 3 58  ? 30.002  38.806  13.479  1.000 40.607  0 58  SER CCC C   1 ? 12 
ATOM   2947 O O   . SER C 3 58  ? 31.137  38.791  12.960  1.000 42.946  0 58  SER CCC O   1 ? 12 
ATOM   2948 C CB  . SER C 3 58  ? 30.245  36.548  14.541  1.000 42.426  0 58  SER CCC CB  1 ? 12 
ATOM   2949 O OG  . SER C 3 58  ? 29.563  35.922  13.463  1.000 43.657  0 58  SER CCC OG  1 ? 12 
ATOM   2950 N N   . SER C 3 59  ? 28.973  39.514  13.007  1.000 39.339  0 59  SER CCC N   1 ? 12 
ATOM   2951 C CA  . SER C 3 59  ? 29.030  40.356  11.788  1.000 39.114  0 59  SER CCC CA  1 ? 12 
ATOM   2952 C C   . SER C 3 59  ? 28.174  41.610  11.987  1.000 39.707  0 59  SER CCC C   1 ? 12 
ATOM   2953 O O   . SER C 3 59  ? 26.976  41.468  12.328  1.000 40.840  0 59  SER CCC O   1 ? 12 
ATOM   2954 C CB  . SER C 3 59  ? 28.606  39.569  10.569  1.000 39.281  0 59  SER CCC CB  1 ? 12 
ATOM   2955 O OG  . SER C 3 59  ? 28.634  40.378  9.402   1.000 38.212  0 59  SER CCC OG  1 ? 12 
ATOM   2956 N N   . THR C 3 60  ? 28.778  42.785  11.790  1.000 40.510  0 60  THR CCC N   1 ? 12 
ATOM   2957 C CA  . THR C 3 60  ? 28.088  44.100  11.714  1.000 41.618  0 60  THR CCC CA  1 ? 12 
ATOM   2958 C C   . THR C 3 60  ? 28.399  44.742  10.357  1.000 42.173  0 60  THR CCC C   1 ? 12 
ATOM   2959 O O   . THR C 3 60  ? 29.386  44.340  9.723   1.000 43.750  0 60  THR CCC O   1 ? 12 
ATOM   2960 C CB  . THR C 3 60  ? 28.471  44.988  12.906  1.000 42.676  0 60  THR CCC CB  1 ? 12 
ATOM   2961 O OG1 . THR C 3 60  ? 29.874  45.244  12.858  1.000 41.105  0 60  THR CCC OG1 1 ? 12 
ATOM   2962 C CG2 . THR C 3 60  ? 28.095  44.357  14.232  1.000 42.806  0 60  THR CCC CG2 1 ? 12 
ATOM   2963 N N   . PHE C 3 61  ? 27.567  45.691  9.928   1.000 42.823  0 61  PHE CCC N   1 ? 12 
ATOM   2964 C CA  . PHE C 3 61  ? 27.691  46.402  8.629   1.000 44.623  0 61  PHE CCC CA  1 ? 12 
ATOM   2965 C C   . PHE C 3 61  ? 27.131  47.816  8.798   1.000 44.107  0 61  PHE CCC C   1 ? 12 
ATOM   2966 O O   . PHE C 3 61  ? 26.238  47.994  9.637   1.000 42.281  0 61  PHE CCC O   1 ? 12 
ATOM   2967 C CB  . PHE C 3 61  ? 27.009  45.601  7.514   1.000 44.849  0 61  PHE CCC CB  1 ? 12 
ATOM   2968 C CG  . PHE C 3 61  ? 25.677  44.996  7.885   1.000 43.961  0 61  PHE CCC CG  1 ? 12 
ATOM   2969 C CD1 . PHE C 3 61  ? 25.600  43.760  8.517   1.000 43.292  0 61  PHE CCC CD1 1 ? 12 
ATOM   2970 C CD2 . PHE C 3 61  ? 24.498  45.657  7.583   1.000 44.555  0 61  PHE CCC CD2 1 ? 12 
ATOM   2971 C CE1 . PHE C 3 61  ? 24.374  43.211  8.865   1.000 43.976  0 61  PHE CCC CE1 1 ? 12 
ATOM   2972 C CE2 . PHE C 3 61  ? 23.271  45.106  7.919   1.000 45.152  0 61  PHE CCC CE2 1 ? 12 
ATOM   2973 C CZ  . PHE C 3 61  ? 23.211  43.885  8.559   1.000 45.361  0 61  PHE CCC CZ  1 ? 12 
ATOM   2974 N N   . TYR C 3 62  ? 27.665  48.774  8.038   1.000 46.269  0 62  TYR CCC N   1 ? 12 
ATOM   2975 C CA  . TYR C 3 62  ? 27.516  50.236  8.266   1.000 48.824  0 62  TYR CCC CA  1 ? 12 
ATOM   2976 C C   . TYR C 3 62  ? 27.366  50.945  6.917   1.000 50.678  0 62  TYR CCC C   1 ? 12 
ATOM   2977 O O   . TYR C 3 62  ? 28.005  50.518  5.942   1.000 52.091  0 62  TYR CCC O   1 ? 12 
ATOM   2978 C CB  . TYR C 3 62  ? 28.718  50.765  9.058   1.000 49.948  0 62  TYR CCC CB  1 ? 12 
ATOM   2979 C CG  . TYR C 3 62  ? 28.957  50.011  10.341  1.000 48.210  0 62  TYR CCC CG  1 ? 12 
ATOM   2980 C CD1 . TYR C 3 62  ? 29.745  48.872  10.369  1.000 47.893  0 62  TYR CCC CD1 1 ? 12 
ATOM   2981 C CD2 . TYR C 3 62  ? 28.354  50.412  11.522  1.000 47.637  0 62  TYR CCC CD2 1 ? 12 
ATOM   2982 C CE1 . TYR C 3 62  ? 29.942  48.161  11.542  1.000 47.099  0 62  TYR CCC CE1 1 ? 12 
ATOM   2983 C CE2 . TYR C 3 62  ? 28.536  49.710  12.702  1.000 46.993  0 62  TYR CCC CE2 1 ? 12 
ATOM   2984 C CZ  . TYR C 3 62  ? 29.336  48.582  12.714  1.000 46.545  0 62  TYR CCC CZ  1 ? 12 
ATOM   2985 O OH  . TYR C 3 62  ? 29.526  47.883  13.870  1.000 45.860  0 62  TYR CCC OH  1 ? 12 
ATOM   2986 N N   . SER C 3 63  ? 26.521  51.978  6.862   1.000 52.630  0 63  SER CCC N   1 ? 12 
ATOM   2987 C CA  . SER C 3 63  ? 26.406  52.885  5.693   1.000 56.957  0 63  SER CCC CA  1 ? 12 
ATOM   2988 C C   . SER C 3 63  ? 27.740  53.625  5.535   1.000 59.998  0 63  SER CCC C   1 ? 12 
ATOM   2989 O O   . SER C 3 63  ? 28.452  53.777  6.547   1.000 58.694  0 63  SER CCC O   1 ? 12 
ATOM   2990 C CB  . SER C 3 63  ? 25.240  53.834  5.830   1.000 57.495  0 63  SER CCC CB  1 ? 12 
ATOM   2991 O OG  . SER C 3 63  ? 25.510  54.834  6.799   1.000 59.228  0 63  SER CCC OG  1 ? 12 
ATOM   2992 N N   . ASP C 3 64  ? 28.061  54.062  4.314   1.000 62.707  0 64  ASP CCC N   1 ? 12 
ATOM   2993 C CA  . ASP C 3 64  ? 29.326  54.772  3.989   1.000 67.106  0 64  ASP CCC CA  1 ? 12 
ATOM   2994 C C   . ASP C 3 64  ? 29.504  55.964  4.941   1.000 68.266  0 64  ASP CCC C   1 ? 12 
ATOM   2995 O O   . ASP C 3 64  ? 30.663  56.289  5.257   1.000 71.020  0 64  ASP CCC O   1 ? 12 
ATOM   2996 C CB  . ASP C 3 64  ? 29.364  55.211  2.518   1.000 70.936  0 64  ASP CCC CB  1 ? 12 
ATOM   2997 C CG  . ASP C 3 64  ? 29.601  54.091  1.511   1.000 70.831  0 64  ASP CCC CG  1 ? 12 
ATOM   2998 O OD1 . ASP C 3 64  ? 29.665  52.923  1.926   1.000 68.336  0 64  ASP CCC OD1 1 ? 12 
ATOM   2999 O OD2 . ASP C 3 64  ? 29.729  54.401  0.306   1.000 76.668  0 64  ASP CCC OD2 1 ? 12 
ATOM   3000 N N   . SER C 3 65  ? 28.408  56.579  5.399   1.000 67.347  0 65  SER CCC N   1 ? 12 
ATOM   3001 C CA  . SER C 3 65  ? 28.416  57.880  6.121   1.000 69.634  0 65  SER CCC CA  1 ? 12 
ATOM   3002 C C   . SER C 3 65  ? 28.614  57.712  7.637   1.000 67.181  0 65  SER CCC C   1 ? 12 
ATOM   3003 O O   . SER C 3 65  ? 28.753  58.755  8.308   1.000 68.924  0 65  SER CCC O   1 ? 12 
ATOM   3004 C CB  . SER C 3 65  ? 27.161  58.654  5.826   1.000 70.990  0 65  SER CCC CB  1 ? 12 
ATOM   3005 O OG  . SER C 3 65  ? 26.033  57.995  6.377   1.000 69.690  0 65  SER CCC OG  1 ? 12 
ATOM   3006 N N   . VAL C 3 66  ? 28.618  56.485  8.176   1.000 63.306  0 66  VAL CCC N   1 ? 12 
ATOM   3007 C CA  . VAL C 3 66  ? 28.823  56.255  9.641   1.000 62.151  0 66  VAL CCC CA  1 ? 12 
ATOM   3008 C C   . VAL C 3 66  ? 29.934  55.233  9.909   1.000 61.689  0 66  VAL CCC C   1 ? 12 
ATOM   3009 O O   . VAL C 3 66  ? 30.432  55.245  11.048  1.000 61.094  0 66  VAL CCC O   1 ? 12 
ATOM   3010 C CB  . VAL C 3 66  ? 27.521  55.845  10.355  1.000 59.726  0 66  VAL CCC CB  1 ? 12 
ATOM   3011 C CG1 . VAL C 3 66  ? 26.424  56.886  10.168  1.000 61.573  0 66  VAL CCC CG1 1 ? 12 
ATOM   3012 C CG2 . VAL C 3 66  ? 27.049  54.456  9.938   1.000 56.765  0 66  VAL CCC CG2 1 ? 12 
ATOM   3013 N N   . LYS C 3 67  ? 30.306  54.383  8.943   1.000 62.670  0 67  LYS CCC N   1 ? 12 
ATOM   3014 C CA  . LYS C 3 67  ? 31.384  53.373  9.129   1.000 63.022  0 67  LYS CCC CA  1 ? 12 
ATOM   3015 C C   . LYS C 3 67  ? 32.626  54.073  9.697   1.000 64.580  0 67  LYS CCC C   1 ? 12 
ATOM   3016 O O   . LYS C 3 67  ? 33.066  55.068  9.094   1.000 67.586  0 67  LYS CCC O   1 ? 12 
ATOM   3017 C CB  . LYS C 3 67  ? 31.723  52.657  7.817   1.000 64.638  0 67  LYS CCC CB  1 ? 12 
ATOM   3018 C CG  . LYS C 3 67  ? 32.646  51.454  7.973   1.000 64.620  0 67  LYS CCC CG  1 ? 12 
ATOM   3019 C CD  . LYS C 3 67  ? 32.760  50.601  6.730   1.000 65.141  0 67  LYS CCC CD  1 ? 12 
ATOM   3020 C CE  . LYS C 3 67  ? 33.726  49.452  6.912   1.000 65.109  0 67  LYS CCC CE  1 ? 12 
ATOM   3021 N NZ  . LYS C 3 67  ? 33.666  48.494  5.786   1.000 64.143  0 67  LYS CCC NZ  1 ? 12 
ATOM   3022 N N   . GLY C 3 68  ? 33.142  53.590  10.831  1.000 63.903  0 68  GLY CCC N   1 ? 12 
ATOM   3023 C CA  . GLY C 3 68  ? 34.335  54.145  11.500  1.000 66.164  0 68  GLY CCC CA  1 ? 12 
ATOM   3024 C C   . GLY C 3 68  ? 33.983  55.085  12.643  1.000 67.634  0 68  GLY CCC C   1 ? 12 
ATOM   3025 O O   . GLY C 3 68  ? 34.875  55.345  13.476  1.000 70.618  0 68  GLY CCC O   1 ? 12 
ATOM   3026 N N   . ARG C 3 69  ? 32.742  55.585  12.689  1.000 66.195  0 69  ARG CCC N   1 ? 12 
ATOM   3027 C CA  . ARG C 3 69  ? 32.244  56.514  13.743  1.000 66.570  0 69  ARG CCC CA  1 ? 12 
ATOM   3028 C C   . ARG C 3 69  ? 31.242  55.786  14.647  1.000 62.757  0 69  ARG CCC C   1 ? 12 
ATOM   3029 O O   . ARG C 3 69  ? 31.316  55.978  15.878  1.000 62.733  0 69  ARG CCC O   1 ? 12 
ATOM   3030 C CB  . ARG C 3 69  ? 31.602  57.750  13.106  1.000 69.265  0 69  ARG CCC CB  1 ? 12 
ATOM   3031 C CG  . ARG C 3 69  ? 32.573  58.626  12.329  1.000 73.384  0 69  ARG CCC CG  1 ? 12 
ATOM   3032 C CD  . ARG C 3 69  ? 31.986  59.970  11.924  1.000 76.323  0 69  ARG CCC CD  1 ? 12 
ATOM   3033 N NE  . ARG C 3 69  ? 30.742  59.831  11.173  1.000 75.047  0 69  ARG CCC NE  1 ? 12 
ATOM   3034 C CZ  . ARG C 3 69  ? 29.531  60.208  11.589  1.000 74.305  0 69  ARG CCC CZ  1 ? 12 
ATOM   3035 N NH1 . ARG C 3 69  ? 29.358  60.781  12.770  1.000 74.775  0 69  ARG CCC NH1 1 ? 12 
ATOM   3036 N NH2 . ARG C 3 69  ? 28.484  60.007  10.806  1.000 73.136  0 69  ARG CCC NH2 1 ? 12 
ATOM   3037 N N   . PHE C 3 70  ? 30.334  55.005  14.053  1.000 59.894  0 70  PHE CCC N   1 ? 12 
ATOM   3038 C CA  . PHE C 3 70  ? 29.293  54.210  14.753  1.000 56.461  0 70  PHE CCC CA  1 ? 12 
ATOM   3039 C C   . PHE C 3 70  ? 29.725  52.741  14.797  1.000 55.280  0 70  PHE CCC C   1 ? 12 
ATOM   3040 O O   . PHE C 3 70  ? 30.358  52.253  13.830  1.000 55.927  0 70  PHE CCC O   1 ? 12 
ATOM   3041 C CB  . PHE C 3 70  ? 27.939  54.323  14.046  1.000 55.302  0 70  PHE CCC CB  1 ? 12 
ATOM   3042 C CG  . PHE C 3 70  ? 27.264  55.673  14.085  1.000 56.285  0 70  PHE CCC CG  1 ? 12 
ATOM   3043 C CD1 . PHE C 3 70  ? 27.909  56.807  14.565  1.000 58.702  0 70  PHE CCC CD1 1 ? 12 
ATOM   3044 C CD2 . PHE C 3 70  ? 25.981  55.815  13.579  1.000 53.990  0 70  PHE CCC CD2 1 ? 12 
ATOM   3045 C CE1 . PHE C 3 70  ? 27.266  58.036  14.579  1.000 60.380  0 70  PHE CCC CE1 1 ? 12 
ATOM   3046 C CE2 . PHE C 3 70  ? 25.348  57.048  13.580  1.000 55.993  0 70  PHE CCC CE2 1 ? 12 
ATOM   3047 C CZ  . PHE C 3 70  ? 25.989  58.155  14.083  1.000 58.573  0 70  PHE CCC CZ  1 ? 12 
ATOM   3048 N N   . THR C 3 71  ? 29.391  52.056  15.893  1.000 53.783  0 71  THR CCC N   1 ? 12 
ATOM   3049 C CA  . THR C 3 71  ? 29.615  50.598  16.086  1.000 52.480  0 71  THR CCC CA  1 ? 12 
ATOM   3050 C C   . THR C 3 71  ? 28.337  50.000  16.673  1.000 48.869  0 71  THR CCC C   1 ? 12 
ATOM   3051 O O   . THR C 3 71  ? 27.691  50.686  17.497  1.000 49.582  0 71  THR CCC O   1 ? 12 
ATOM   3052 C CB  . THR C 3 71  ? 30.860  50.331  16.949  1.000 55.018  0 71  THR CCC CB  1 ? 12 
ATOM   3053 O OG1 . THR C 3 71  ? 31.062  48.923  17.064  1.000 56.899  0 71  THR CCC OG1 1 ? 12 
ATOM   3054 C CG2 . THR C 3 71  ? 30.771  50.926  18.335  1.000 56.562  0 71  THR CCC CG2 1 ? 12 
ATOM   3055 N N   . VAL C 3 72  ? 27.970  48.800  16.223  1.000 45.868  0 72  VAL CCC N   1 ? 12 
ATOM   3056 C CA  . VAL C 3 72  ? 26.849  47.999  16.790  1.000 44.516  0 72  VAL CCC CA  1 ? 12 
ATOM   3057 C C   . VAL C 3 72  ? 27.463  46.877  17.628  1.000 44.405  0 72  VAL CCC C   1 ? 12 
ATOM   3058 O O   . VAL C 3 72  ? 28.422  46.238  17.148  1.000 42.306  0 72  VAL CCC O   1 ? 12 
ATOM   3059 C CB  . VAL C 3 72  ? 25.911  47.438  15.705  1.000 42.986  0 72  VAL CCC CB  1 ? 12 
ATOM   3060 C CG1 . VAL C 3 72  ? 24.746  46.675  16.320  1.000 42.715  0 72  VAL CCC CG1 1 ? 12 
ATOM   3061 C CG2 . VAL C 3 72  ? 25.401  48.529  14.776  1.000 44.641  0 72  VAL CCC CG2 1 ? 12 
ATOM   3062 N N   . SER C 3 73  ? 26.935  46.673  18.836  1.000 44.483  0 73  SER CCC N   1 ? 12 
ATOM   3063 C CA  . SER C 3 73  ? 27.297  45.562  19.751  1.000 45.446  0 73  SER CCC CA  1 ? 12 
ATOM   3064 C C   . SER C 3 73  ? 26.012  44.922  20.278  1.000 44.590  0 73  SER CCC C   1 ? 12 
ATOM   3065 O O   . SER C 3 73  ? 24.924  45.502  20.063  1.000 45.094  0 73  SER CCC O   1 ? 12 
ATOM   3066 C CB  . SER C 3 73  ? 28.174  46.043  20.878  1.000 47.536  0 73  SER CCC CB  1 ? 12 
ATOM   3067 O OG  . SER C 3 73  ? 27.419  46.808  21.810  1.000 49.656  0 73  SER CCC OG  1 ? 12 
ATOM   3068 N N   . ARG C 3 74  ? 26.149  43.775  20.942  1.000 44.149  0 74  ARG CCC N   1 ? 12 
ATOM   3069 C CA  . ARG C 3 74  ? 25.024  42.986  21.504  1.000 43.153  0 74  ARG CCC CA  1 ? 12 
ATOM   3070 C C   . ARG C 3 74  ? 25.459  42.458  22.867  1.000 43.549  0 74  ARG CCC C   1 ? 12 
ATOM   3071 O O   . ARG C 3 74  ? 26.664  42.197  23.029  1.000 44.297  0 74  ARG CCC O   1 ? 12 
ATOM   3072 C CB  . ARG C 3 74  ? 24.665  41.849  20.544  1.000 43.807  0 74  ARG CCC CB  1 ? 12 
ATOM   3073 C CG  . ARG C 3 74  ? 23.293  41.236  20.770  1.000 43.839  0 74  ARG CCC CG  1 ? 12 
ATOM   3074 C CD  . ARG C 3 74  ? 22.889  40.346  19.609  1.000 43.049  0 74  ARG CCC CD  1 ? 12 
ATOM   3075 N NE  . ARG C 3 74  ? 23.611  39.083  19.560  1.000 42.191  0 74  ARG CCC NE  1 ? 12 
ATOM   3076 C CZ  . ARG C 3 74  ? 23.400  38.125  18.661  1.000 41.805  0 74  ARG CCC CZ  1 ? 12 
ATOM   3077 N NH1 . ARG C 3 74  ? 22.490  38.280  17.711  1.000 41.313  0 74  ARG CCC NH1 1 ? 12 
ATOM   3078 N NH2 . ARG C 3 74  ? 24.104  37.009  18.716  1.000 42.616  0 74  ARG CCC NH2 1 ? 12 
ATOM   3079 N N   . ASN C 3 75  ? 24.519  42.329  23.808  1.000 43.703  0 75  ASN CCC N   1 ? 12 
ATOM   3080 C CA  . ASN C 3 75  ? 24.782  41.827  25.182  1.000 45.219  0 75  ASN CCC CA  1 ? 12 
ATOM   3081 C C   . ASN C 3 75  ? 24.958  40.302  25.144  1.000 45.368  0 75  ASN CCC C   1 ? 12 
ATOM   3082 O O   . ASN C 3 75  ? 24.609  39.687  24.119  1.000 42.001  0 75  ASN CCC O   1 ? 12 
ATOM   3083 C CB  . ASN C 3 75  ? 23.687  42.269  26.158  1.000 46.100  0 75  ASN CCC CB  1 ? 12 
ATOM   3084 C CG  . ASN C 3 75  ? 22.338  41.634  25.892  1.000 44.800  0 75  ASN CCC CG  1 ? 12 
ATOM   3085 O OD1 . ASN C 3 75  ? 22.119  41.032  24.841  1.000 42.061  0 75  ASN CCC OD1 1 ? 12 
ATOM   3086 N ND2 . ASN C 3 75  ? 21.423  41.771  26.839  1.000 45.048  0 75  ASN CCC ND2 1 ? 12 
ATOM   3087 N N   . ASN C 3 76  ? 25.471  39.722  26.232  1.000 48.800  0 76  ASN CCC N   1 ? 12 
ATOM   3088 C CA  . ASN C 3 76  ? 25.717  38.261  26.381  1.000 50.747  0 76  ASN CCC CA  1 ? 12 
ATOM   3089 C C   . ASN C 3 76  ? 24.405  37.485  26.212  1.000 49.612  0 76  ASN CCC C   1 ? 12 
ATOM   3090 O O   . ASN C 3 76  ? 24.453  36.383  25.644  1.000 48.939  0 76  ASN CCC O   1 ? 12 
ATOM   3091 C CB  . ASN C 3 76  ? 26.375  37.933  27.725  1.000 55.286  0 76  ASN CCC CB  1 ? 12 
ATOM   3092 C CG  . ASN C 3 76  ? 27.815  38.396  27.807  1.000 58.517  0 76  ASN CCC CG  1 ? 12 
ATOM   3093 O OD1 . ASN C 3 76  ? 28.378  38.901  26.836  1.000 60.355  0 76  ASN CCC OD1 1 ? 12 
ATOM   3094 N ND2 . ASN C 3 76  ? 28.428  38.209  28.964  1.000 61.844  0 76  ASN CCC ND2 1 ? 12 
ATOM   3095 N N   . ALA C 3 77  ? 23.285  38.039  26.690  1.000 49.157  0 77  ALA CCC N   1 ? 12 
ATOM   3096 C CA  . ALA C 3 77  ? 21.934  37.438  26.589  1.000 49.059  0 77  ALA CCC CA  1 ? 12 
ATOM   3097 C C   . ALA C 3 77  ? 21.507  37.353  25.118  1.000 46.906  0 77  ALA CCC C   1 ? 12 
ATOM   3098 O O   . ALA C 3 77  ? 20.719  36.451  24.798  1.000 47.706  0 77  ALA CCC O   1 ? 12 
ATOM   3099 C CB  . ALA C 3 77  ? 20.950  38.238  27.402  1.000 49.557  0 77  ALA CCC CB  1 ? 12 
ATOM   3100 N N   . LYS C 3 78  ? 22.008  38.260  24.270  1.000 45.512  0 78  LYS CCC N   1 ? 12 
ATOM   3101 C CA  . LYS C 3 78  ? 21.732  38.335  22.806  1.000 44.340  0 78  LYS CCC CA  1 ? 12 
ATOM   3102 C C   . LYS C 3 78  ? 20.308  38.851  22.557  1.000 43.507  0 78  LYS CCC C   1 ? 12 
ATOM   3103 O O   . LYS C 3 78  ? 19.773  38.586  21.460  1.000 40.394  0 78  LYS CCC O   1 ? 12 
ATOM   3104 C CB  . LYS C 3 78  ? 21.897  36.970  22.128  1.000 46.113  0 78  LYS CCC CB  1 ? 12 
ATOM   3105 C CG  . LYS C 3 78  ? 23.138  36.177  22.517  1.000 48.764  0 78  LYS CCC CG  1 ? 12 
ATOM   3106 C CD  . LYS C 3 78  ? 23.337  34.939  21.665  1.000 51.325  0 78  LYS CCC CD  1 ? 12 
ATOM   3107 C CE  . LYS C 3 78  ? 24.275  33.929  22.292  1.000 56.441  0 78  LYS CCC CE  1 ? 12 
ATOM   3108 N NZ  . LYS C 3 78  ? 24.561  32.813  21.361  1.000 60.082  0 78  LYS CCC NZ  1 ? 12 
ATOM   3109 N N   . ASP C 3 79  ? 19.714  39.547  23.533  1.000 43.011  0 79  ASP CCC N   1 ? 12 
ATOM   3110 C CA  . ASP C 3 79  ? 18.320  40.061  23.454  1.000 43.617  0 79  ASP CCC CA  1 ? 12 
ATOM   3111 C C   . ASP C 3 79  ? 18.330  41.591  23.356  1.000 43.001  0 79  ASP CCC C   1 ? 12 
ATOM   3112 O O   . ASP C 3 79  ? 17.251  42.164  23.104  1.000 43.729  0 79  ASP CCC O   1 ? 12 
ATOM   3113 C CB  . ASP C 3 79  ? 17.465  39.569  24.630  1.000 45.311  0 79  ASP CCC CB  1 ? 12 
ATOM   3114 C CG  . ASP C 3 79  ? 18.003  39.896  26.013  1.000 46.572  0 79  ASP CCC CG  1 ? 12 
ATOM   3115 O OD1 . ASP C 3 79  ? 18.869  40.789  26.125  1.000 43.691  0 79  ASP CCC OD1 1 ? 12 
ATOM   3116 O OD2 . ASP C 3 79  ? 17.543  39.250  26.976  1.000 49.505  0 79  ASP CCC OD2 1 ? 12 
ATOM   3117 N N   . THR C 3 80  ? 19.488  42.229  23.549  1.000 43.194  0 80  THR CCC N   1 ? 12 
ATOM   3118 C CA  . THR C 3 80  ? 19.644  43.706  23.484  1.000 43.762  0 80  THR CCC CA  1 ? 12 
ATOM   3119 C C   . THR C 3 80  ? 20.814  44.060  22.563  1.000 43.228  0 80  THR CCC C   1 ? 12 
ATOM   3120 O O   . THR C 3 80  ? 21.915  43.534  22.776  1.000 44.195  0 80  THR CCC O   1 ? 12 
ATOM   3121 C CB  . THR C 3 80  ? 19.832  44.319  24.874  1.000 46.445  0 80  THR CCC CB  1 ? 12 
ATOM   3122 O OG1 . THR C 3 80  ? 18.927  43.695  25.786  1.000 46.967  0 80  THR CCC OG1 1 ? 12 
ATOM   3123 C CG2 . THR C 3 80  ? 19.601  45.813  24.864  1.000 47.212  0 80  THR CCC CG2 1 ? 12 
ATOM   3124 N N   . VAL C 3 81  ? 20.555  44.905  21.566  1.000 43.501  0 81  VAL CCC N   1 ? 12 
ATOM   3125 C CA  . VAL C 3 81  ? 21.561  45.424  20.598  1.000 43.479  0 81  VAL CCC CA  1 ? 12 
ATOM   3126 C C   . VAL C 3 81  ? 21.733  46.921  20.861  1.000 43.145  0 81  VAL CCC C   1 ? 12 
ATOM   3127 O O   . VAL C 3 81  ? 20.719  47.602  21.102  1.000 46.591  0 81  VAL CCC O   1 ? 12 
ATOM   3128 C CB  . VAL C 3 81  ? 21.125  45.145  19.147  1.000 44.502  0 81  VAL CCC CB  1 ? 12 
ATOM   3129 C CG1 . VAL C 3 81  ? 22.025  45.851  18.143  1.000 46.979  0 81  VAL CCC CG1 1 ? 12 
ATOM   3130 C CG2 . VAL C 3 81  ? 21.063  43.650  18.863  1.000 44.357  0 81  VAL CCC CG2 1 ? 12 
ATOM   3131 N N   . TYR C 3 82  ? 22.972  47.407  20.819  1.000 43.205  0 82  TYR CCC N   1 ? 12 
ATOM   3132 C CA  . TYR C 3 82  ? 23.336  48.820  21.091  1.000 45.235  0 82  TYR CCC CA  1 ? 12 
ATOM   3133 C C   . TYR C 3 82  ? 23.934  49.438  19.821  1.000 46.766  0 82  TYR CCC C   1 ? 12 
ATOM   3134 O O   . TYR C 3 82  ? 24.760  48.778  19.160  1.000 44.639  0 82  TYR CCC O   1 ? 12 
ATOM   3135 C CB  . TYR C 3 82  ? 24.305  48.887  22.274  1.000 46.270  0 82  TYR CCC CB  1 ? 12 
ATOM   3136 C CG  . TYR C 3 82  ? 23.817  48.168  23.507  1.000 46.430  0 82  TYR CCC CG  1 ? 12 
ATOM   3137 C CD1 . TYR C 3 82  ? 22.922  48.774  24.374  1.000 48.105  0 82  TYR CCC CD1 1 ? 12 
ATOM   3138 C CD2 . TYR C 3 82  ? 24.228  46.876  23.797  1.000 44.939  0 82  TYR CCC CD2 1 ? 12 
ATOM   3139 C CE1 . TYR C 3 82  ? 22.458  48.122  25.504  1.000 48.784  0 82  TYR CCC CE1 1 ? 12 
ATOM   3140 C CE2 . TYR C 3 82  ? 23.764  46.203  24.916  1.000 46.209  0 82  TYR CCC CE2 1 ? 12 
ATOM   3141 C CZ  . TYR C 3 82  ? 22.883  46.834  25.779  1.000 48.465  0 82  TYR CCC CZ  1 ? 12 
ATOM   3142 O OH  . TYR C 3 82  ? 22.412  46.211  26.899  1.000 50.824  0 82  TYR CCC OH  1 ? 12 
ATOM   3143 N N   . LEU C 3 83  ? 23.502  50.656  19.482  1.000 48.105  0 83  LEU CCC N   1 ? 12 
ATOM   3144 C CA  . LEU C 3 83  ? 24.168  51.524  18.480  1.000 49.461  0 83  LEU CCC CA  1 ? 12 
ATOM   3145 C C   . LEU C 3 83  ? 24.987  52.567  19.242  1.000 52.389  0 83  LEU CCC C   1 ? 12 
ATOM   3146 O O   . LEU C 3 83  ? 24.378  53.505  19.805  1.000 53.848  0 83  LEU CCC O   1 ? 12 
ATOM   3147 C CB  . LEU C 3 83  ? 23.127  52.189  17.573  1.000 50.142  0 83  LEU CCC CB  1 ? 12 
ATOM   3148 C CG  . LEU C 3 83  ? 23.696  53.038  16.435  1.000 51.343  0 83  LEU CCC CG  1 ? 12 
ATOM   3149 C CD1 . LEU C 3 83  ? 24.466  52.168  15.447  1.000 50.619  0 83  LEU CCC CD1 1 ? 12 
ATOM   3150 C CD2 . LEU C 3 83  ? 22.594  53.818  15.733  1.000 51.275  0 83  LEU CCC CD2 1 ? 12 
ATOM   3151 N N   . HIS C 3 84  ? 26.311  52.380  19.289  1.000 52.737  0 84  HIS CCC N   1 ? 12 
ATOM   3152 C CA  . HIS C 3 84  ? 27.279  53.342  19.879  1.000 54.115  0 84  HIS CCC CA  1 ? 12 
ATOM   3153 C C   . HIS C 3 84  ? 27.584  54.422  18.837  1.000 57.306  0 84  HIS CCC C   1 ? 12 
ATOM   3154 O O   . HIS C 3 84  ? 28.264  54.103  17.843  1.000 56.439  0 84  HIS CCC O   1 ? 12 
ATOM   3155 C CB  . HIS C 3 84  ? 28.547  52.619  20.347  1.000 52.546  0 84  HIS CCC CB  1 ? 12 
ATOM   3156 C CG  . HIS C 3 84  ? 28.289  51.449  21.235  1.000 50.154  0 84  HIS CCC CG  1 ? 12 
ATOM   3157 N ND1 . HIS C 3 84  ? 28.187  51.573  22.610  1.000 49.792  0 84  HIS CCC ND1 1 ? 12 
ATOM   3158 C CD2 . HIS C 3 84  ? 28.118  50.138  20.956  1.000 46.995  0 84  HIS CCC CD2 1 ? 12 
ATOM   3159 C CE1 . HIS C 3 84  ? 27.959  50.389  23.137  1.000 47.840  0 84  HIS CCC CE1 1 ? 12 
ATOM   3160 N NE2 . HIS C 3 84  ? 27.915  49.492  22.146  1.000 45.393  0 84  HIS CCC NE2 1 ? 12 
ATOM   3161 N N   . MET C 3 85  ? 27.070  55.637  19.053  1.000 61.408  0 85  MET CCC N   1 ? 12 
ATOM   3162 C CA  . MET C 3 85  ? 27.207  56.792  18.125  1.000 64.719  0 85  MET CCC CA  1 ? 12 
ATOM   3163 C C   . MET C 3 85  ? 28.284  57.739  18.663  1.000 66.283  0 85  MET CCC C   1 ? 12 
ATOM   3164 O O   . MET C 3 85  ? 27.998  58.468  19.631  1.000 68.907  0 85  MET CCC O   1 ? 12 
ATOM   3165 C CB  . MET C 3 85  ? 25.874  57.538  17.984  1.000 67.596  0 85  MET CCC CB  1 ? 12 
ATOM   3166 C CG  . MET C 3 85  ? 24.699  56.622  17.664  1.000 65.603  0 85  MET CCC CG  1 ? 12 
ATOM   3167 S SD  . MET C 3 85  ? 23.220  57.530  17.140  1.000 68.124  0 85  MET CCC SD  1 ? 12 
ATOM   3168 C CE  . MET C 3 85  ? 22.865  58.458  18.628  1.000 70.735  0 85  MET CCC CE  1 ? 12 
ATOM   3169 N N   . ASN C 3 86  ? 29.480  57.707  18.065  1.000 66.716  0 86  ASN CCC N   1 ? 12 
ATOM   3170 C CA  . ASN C 3 86  ? 30.650  58.541  18.454  1.000 69.010  0 86  ASN CCC CA  1 ? 12 
ATOM   3171 C C   . ASN C 3 86  ? 30.961  59.532  17.329  1.000 71.727  0 86  ASN CCC C   1 ? 12 
ATOM   3172 O O   . ASN C 3 86  ? 30.547  59.270  16.181  1.000 70.404  0 86  ASN CCC O   1 ? 12 
ATOM   3173 C CB  . ASN C 3 86  ? 31.874  57.679  18.768  1.000 68.196  0 86  ASN CCC CB  1 ? 12 
ATOM   3174 C CG  . ASN C 3 86  ? 31.574  56.590  19.775  1.000 65.023  0 86  ASN CCC CG  1 ? 12 
ATOM   3175 O OD1 . ASN C 3 86  ? 31.270  56.879  20.929  1.000 66.042  0 86  ASN CCC OD1 1 ? 12 
ATOM   3176 N ND2 . ASN C 3 86  ? 31.633  55.340  19.345  1.000 62.392  0 86  ASN CCC ND2 1 ? 12 
ATOM   3177 N N   . SER C 3 87  ? 31.669  60.619  17.655  1.000 77.066  0 87  SER CCC N   1 ? 12 
ATOM   3178 C CA  . SER C 3 87  ? 32.112  61.672  16.704  1.000 82.081  0 87  SER CCC CA  1 ? 12 
ATOM   3179 C C   . SER C 3 87  ? 30.902  62.174  15.908  1.000 83.576  0 87  SER CCC C   1 ? 12 
ATOM   3180 O O   . SER C 3 87  ? 30.958  62.175  14.658  1.000 84.508  0 87  SER CCC O   1 ? 12 
ATOM   3181 C CB  . SER C 3 87  ? 33.197  61.149  15.800  1.000 82.187  0 87  SER CCC CB  1 ? 12 
ATOM   3182 O OG  . SER C 3 87  ? 34.242  60.559  16.557  1.000 82.168  0 87  SER CCC OG  1 ? 12 
ATOM   3183 N N   . LEU C 3 88  ? 29.843  62.571  16.619  1.000 84.738  0 88  LEU CCC N   1 ? 12 
ATOM   3184 C CA  . LEU C 3 88  ? 28.521  62.907  16.028  1.000 85.610  0 88  LEU CCC CA  1 ? 12 
ATOM   3185 C C   . LEU C 3 88  ? 28.599  64.266  15.319  1.000 91.083  0 88  LEU CCC C   1 ? 12 
ATOM   3186 O O   . LEU C 3 88  ? 29.173  65.211  15.898  1.000 93.947  0 88  LEU CCC O   1 ? 12 
ATOM   3187 C CB  . LEU C 3 88  ? 27.456  62.895  17.130  1.000 83.900  0 88  LEU CCC CB  1 ? 12 
ATOM   3188 C CG  . LEU C 3 88  ? 26.886  61.514  17.463  1.000 79.077  0 88  LEU CCC CG  1 ? 12 
ATOM   3189 C CD1 . LEU C 3 88  ? 26.226  61.501  18.834  1.000 78.282  0 88  LEU CCC CD1 1 ? 12 
ATOM   3190 C CD2 . LEU C 3 88  ? 25.904  61.058  16.393  1.000 77.273  0 88  LEU CCC CD2 1 ? 12 
ATOM   3191 N N   . LYS C 3 89  ? 28.046  64.333  14.103  1.000 93.267  0 89  LYS CCC N   1 ? 12 
ATOM   3192 C CA  . LYS C 3 89  ? 27.926  65.554  13.260  1.000 98.786  0 89  LYS CCC CA  1 ? 12 
ATOM   3193 C C   . LYS C 3 89  ? 26.500  66.091  13.369  1.000 99.004  0 89  LYS CCC C   1 ? 12 
ATOM   3194 O O   . LYS C 3 89  ? 25.603  65.366  13.797  1.000 94.418  0 89  LYS CCC O   1 ? 12 
ATOM   3195 C CB  . LYS C 3 89  ? 28.234  65.217  11.794  1.000 99.554  0 89  LYS CCC CB  1 ? 12 
ATOM   3196 C CG  . LYS C 3 89  ? 29.609  64.634  11.503  1.000 99.406  0 89  LYS CCC CG  1 ? 12 
ATOM   3197 C CD  . LYS C 3 89  ? 29.656  63.911  10.171  1.000 98.137  0 89  LYS CCC CD  1 ? 12 
ATOM   3198 C CE  . LYS C 3 89  ? 31.026  63.360  9.850   1.000 98.793  0 89  LYS CCC CE  1 ? 12 
ATOM   3199 N NZ  . LYS C 3 89  ? 32.011  64.444  9.621   1.000 104.195 0 89  LYS CCC NZ  1 ? 12 
ATOM   3200 N N   . PRO C 3 90  ? 26.235  67.363  12.983  1.000 103.116 0 90  PRO CCC N   1 ? 12 
ATOM   3201 C CA  . PRO C 3 90  ? 24.861  67.849  12.826  1.000 102.624 0 90  PRO CCC CA  1 ? 12 
ATOM   3202 C C   . PRO C 3 90  ? 24.082  67.062  11.759  1.000 98.965  0 90  PRO CCC C   1 ? 12 
ATOM   3203 O O   . PRO C 3 90  ? 22.883  66.915  11.903  1.000 96.667  0 90  PRO CCC O   1 ? 12 
ATOM   3204 C CB  . PRO C 3 90  ? 25.032  69.321  12.410  1.000 108.469 0 90  PRO CCC CB  1 ? 12 
ATOM   3205 C CG  . PRO C 3 90  ? 26.442  69.396  11.860  1.000 110.640 0 90  PRO CCC CG  1 ? 12 
ATOM   3206 C CD  . PRO C 3 90  ? 27.230  68.408  12.693  1.000 107.595 0 90  PRO CCC CD  1 ? 12 
ATOM   3207 N N   . GLU C 3 91  ? 24.789  66.566  10.738  1.000 98.181  0 91  GLU CCC N   1 ? 12 
ATOM   3208 C CA  . GLU C 3 91  ? 24.248  65.734  9.628   1.000 95.259  0 91  GLU CCC CA  1 ? 12 
ATOM   3209 C C   . GLU C 3 91  ? 23.634  64.436  10.178  1.000 86.939  0 91  GLU CCC C   1 ? 12 
ATOM   3210 O O   . GLU C 3 91  ? 22.828  63.822  9.454   1.000 83.741  0 91  GLU CCC O   1 ? 12 
ATOM   3211 C CB  . GLU C 3 91  ? 25.362  65.443  8.618   1.000 98.957  0 91  GLU CCC CB  1 ? 12 
ATOM   3212 C CG  . GLU C 3 91  ? 24.867  64.804  7.330   1.000 99.719  0 91  GLU CCC CG  1 ? 12 
ATOM   3213 C CD  . GLU C 3 91  ? 25.901  64.703  6.218   1.000 102.992 0 91  GLU CCC CD  1 ? 12 
ATOM   3214 O OE1 . GLU C 3 91  ? 26.706  65.648  6.055   1.000 106.216 0 91  GLU CCC OE1 1 ? 12 
ATOM   3215 O OE2 . GLU C 3 91  ? 25.900  63.674  5.515   1.000 101.858 0 91  GLU CCC OE2 1 ? 12 
ATOM   3216 N N   . ASP C 3 92  ? 23.989  64.033  11.406  1.000 83.773  0 92  ASP CCC N   1 ? 12 
ATOM   3217 C CA  . ASP C 3 92  ? 23.491  62.795  12.069  1.000 78.267  0 92  ASP CCC CA  1 ? 12 
ATOM   3218 C C   . ASP C 3 92  ? 22.122  63.032  12.722  1.000 76.537  0 92  ASP CCC C   1 ? 12 
ATOM   3219 O O   . ASP C 3 92  ? 21.495  62.033  13.128  1.000 72.597  0 92  ASP CCC O   1 ? 12 
ATOM   3220 C CB  . ASP C 3 92  ? 24.478  62.289  13.124  1.000 77.147  0 92  ASP CCC CB  1 ? 12 
ATOM   3221 C CG  . ASP C 3 92  ? 25.782  61.774  12.546  1.000 77.979  0 92  ASP CCC CG  1 ? 12 
ATOM   3222 O OD1 . ASP C 3 92  ? 25.726  61.071  11.514  1.000 77.022  0 92  ASP CCC OD1 1 ? 12 
ATOM   3223 O OD2 . ASP C 3 92  ? 26.841  62.072  13.137  1.000 80.324  0 92  ASP CCC OD2 1 ? 12 
ATOM   3224 N N   . THR C 3 93  ? 21.684  64.290  12.844  1.000 75.899  0 93  THR CCC N   1 ? 13 
ATOM   3225 C CA  . THR C 3 93  ? 20.392  64.673  13.475  1.000 75.934  0 93  THR CCC CA  1 ? 13 
ATOM   3226 C C   . THR C 3 93  ? 19.237  64.029  12.698  1.000 72.949  0 93  THR CCC C   1 ? 13 
ATOM   3227 O O   . THR C 3 93  ? 19.106  64.317  11.492  1.000 73.423  0 93  THR CCC O   1 ? 13 
ATOM   3228 C CB  . THR C 3 93  ? 20.249  66.197  13.558  1.000 80.409  0 93  THR CCC CB  1 ? 13 
ATOM   3229 O OG1 . THR C 3 93  ? 21.289  66.661  14.419  1.000 82.504  0 93  THR CCC OG1 1 ? 13 
ATOM   3230 C CG2 . THR C 3 93  ? 18.900  66.645  14.078  1.000 81.904  0 93  THR CCC CG2 1 ? 13 
ATOM   3231 N N   . ALA C 3 94  ? 18.444  63.188  13.370  1.000 69.685  0 94  ALA CCC N   1 ? 13 
ATOM   3232 C CA  . ALA C 3 94  ? 17.310  62.435  12.784  1.000 66.915  0 94  ALA CCC CA  1 ? 13 
ATOM   3233 C C   . ALA C 3 94  ? 16.558  61.672  13.879  1.000 65.282  0 94  ALA CCC C   1 ? 13 
ATOM   3234 O O   . ALA C 3 94  ? 17.060  61.601  15.016  1.000 66.422  0 94  ALA CCC O   1 ? 13 
ATOM   3235 C CB  . ALA C 3 94  ? 17.818  61.488  11.723  1.000 64.069  0 94  ALA CCC CB  1 ? 13 
ATOM   3236 N N   . VAL C 3 95  ? 15.390  61.129  13.535  1.000 62.949  0 95  VAL CCC N   1 ? 13 
ATOM   3237 C CA  . VAL C 3 95  ? 14.681  60.091  14.337  1.000 60.428  0 95  VAL CCC CA  1 ? 13 
ATOM   3238 C C   . VAL C 3 95  ? 15.268  58.736  13.935  1.000 56.800  0 95  VAL CCC C   1 ? 13 
ATOM   3239 O O   . VAL C 3 95  ? 15.186  58.396  12.744  1.000 55.887  0 95  VAL CCC O   1 ? 13 
ATOM   3240 C CB  . VAL C 3 95  ? 13.158  60.131  14.119  1.000 61.045  0 95  VAL CCC CB  1 ? 13 
ATOM   3241 C CG1 . VAL C 3 95  ? 12.459  59.021  14.888  1.000 59.839  0 95  VAL CCC CG1 1 ? 13 
ATOM   3242 C CG2 . VAL C 3 95  ? 12.572  61.488  14.480  1.000 64.602  0 95  VAL CCC CG2 1 ? 13 
ATOM   3243 N N   . TYR C 3 96  ? 15.846  58.009  14.892  1.000 55.522  0 96  TYR CCC N   1 ? 13 
ATOM   3244 C CA  . TYR C 3 96  ? 16.505  56.696  14.676  1.000 51.885  0 96  TYR CCC CA  1 ? 13 
ATOM   3245 C C   . TYR C 3 96  ? 15.530  55.578  15.055  1.000 49.851  0 96  TYR CCC C   1 ? 13 
ATOM   3246 O O   . TYR C 3 96  ? 14.856  55.687  16.092  1.000 51.310  0 96  TYR CCC O   1 ? 13 
ATOM   3247 C CB  . TYR C 3 96  ? 17.820  56.624  15.455  1.000 52.172  0 96  TYR CCC CB  1 ? 13 
ATOM   3248 C CG  . TYR C 3 96  ? 18.950  57.395  14.823  1.000 53.598  0 96  TYR CCC CG  1 ? 13 
ATOM   3249 C CD1 . TYR C 3 96  ? 18.975  58.779  14.857  1.000 56.983  0 96  TYR CCC CD1 1 ? 13 
ATOM   3250 C CD2 . TYR C 3 96  ? 19.986  56.746  14.170  1.000 52.629  0 96  TYR CCC CD2 1 ? 13 
ATOM   3251 C CE1 . TYR C 3 96  ? 20.001  59.500  14.267  1.000 59.185  0 96  TYR CCC CE1 1 ? 13 
ATOM   3252 C CE2 . TYR C 3 96  ? 21.023  57.450  13.579  1.000 54.478  0 96  TYR CCC CE2 1 ? 13 
ATOM   3253 C CZ  . TYR C 3 96  ? 21.029  58.833  13.625  1.000 57.715  0 96  TYR CCC CZ  1 ? 13 
ATOM   3254 O OH  . TYR C 3 96  ? 22.042  59.538  13.041  1.000 60.481  0 96  TYR CCC OH  1 ? 13 
ATOM   3255 N N   . TYR C 3 97  ? 15.448  54.554  14.205  1.000 47.350  0 97  TYR CCC N   1 ? 13 
ATOM   3256 C CA  . TYR C 3 97  ? 14.593  53.351  14.367  1.000 46.577  0 97  TYR CCC CA  1 ? 13 
ATOM   3257 C C   . TYR C 3 97  ? 15.471  52.098  14.286  1.000 45.362  0 97  TYR CCC C   1 ? 13 
ATOM   3258 O O   . TYR C 3 97  ? 16.431  52.087  13.483  1.000 46.800  0 97  TYR CCC O   1 ? 13 
ATOM   3259 C CB  . TYR C 3 97  ? 13.536  53.264  13.259  1.000 46.265  0 97  TYR CCC CB  1 ? 13 
ATOM   3260 C CG  . TYR C 3 97  ? 12.628  54.459  13.116  1.000 47.483  0 97  TYR CCC CG  1 ? 13 
ATOM   3261 C CD1 . TYR C 3 97  ? 12.994  55.551  12.345  1.000 48.549  0 97  TYR CCC CD1 1 ? 13 
ATOM   3262 C CD2 . TYR C 3 97  ? 11.383  54.484  13.720  1.000 48.815  0 97  TYR CCC CD2 1 ? 13 
ATOM   3263 C CE1 . TYR C 3 97  ? 12.160  56.646  12.197  1.000 50.698  0 97  TYR CCC CE1 1 ? 13 
ATOM   3264 C CE2 . TYR C 3 97  ? 10.535  55.573  13.586  1.000 51.090  0 97  TYR CCC CE2 1 ? 13 
ATOM   3265 C CZ  . TYR C 3 97  ? 10.925  56.657  12.820  1.000 52.057  0 97  TYR CCC CZ  1 ? 13 
ATOM   3266 O OH  . TYR C 3 97  ? 10.103  57.736  12.680  1.000 54.572  0 97  TYR CCC OH  1 ? 13 
ATOM   3267 N N   . CYS C 3 98  ? 15.142  51.064  15.064  1.000 45.193  0 98  CYS CCC N   1 ? 13 
ATOM   3268 C CA  . CYS C 3 98  ? 15.674  49.690  14.868  1.000 43.952  0 98  CYS CCC CA  1 ? 13 
ATOM   3269 C C   . CYS C 3 98  ? 14.566  48.802  14.299  1.000 42.191  0 98  CYS CCC C   1 ? 13 
ATOM   3270 O O   . CYS C 3 98  ? 13.374  49.154  14.442  1.000 43.039  0 98  CYS CCC O   1 ? 13 
ATOM   3271 C CB  . CYS C 3 98  ? 16.232  49.093  16.152  1.000 46.176  0 98  CYS CCC CB  1 ? 13 
ATOM   3272 S SG  . CYS C 3 98  ? 15.013  48.949  17.479  1.000 51.053  0 98  CYS CCC SG  1 ? 13 
ATOM   3273 N N   . ALA C 3 99  ? 14.955  47.699  13.661  1.000 38.968  0 99  ALA CCC N   1 ? 13 
ATOM   3274 C CA  . ALA C 3 99  ? 14.035  46.756  12.993  1.000 39.544  0 99  ALA CCC CA  1 ? 13 
ATOM   3275 C C   . ALA C 3 99  ? 14.763  45.441  12.733  1.000 37.491  0 99  ALA CCC C   1 ? 13 
ATOM   3276 O O   . ALA C 3 99  ? 15.986  45.411  12.917  1.000 36.704  0 99  ALA CCC O   1 ? 13 
ATOM   3277 C CB  . ALA C 3 99  ? 13.516  47.360  11.711  1.000 40.016  0 99  ALA CCC CB  1 ? 13 
ATOM   3278 N N   . ILE C 3 100 ? 14.015  44.410  12.337  1.000 38.820  0 100 ILE CCC N   1 ? 13 
ATOM   3279 C CA  . ILE C 3 100 ? 14.542  43.061  11.982  1.000 38.979  0 100 ILE CCC CA  1 ? 13 
ATOM   3280 C C   . ILE C 3 100 ? 14.058  42.725  10.573  1.000 39.718  0 100 ILE CCC C   1 ? 13 
ATOM   3281 O O   . ILE C 3 100 ? 13.069  43.339  10.129  1.000 42.166  0 100 ILE CCC O   1 ? 13 
ATOM   3282 C CB  . ILE C 3 100 ? 14.125  41.994  13.015  1.000 40.437  0 100 ILE CCC CB  1 ? 13 
ATOM   3283 C CG1 . ILE C 3 100 ? 12.616  42.000  13.284  1.000 42.018  0 100 ILE CCC CG1 1 ? 13 
ATOM   3284 C CG2 . ILE C 3 100 ? 14.925  42.165  14.301  1.000 41.007  0 100 ILE CCC CG2 1 ? 13 
ATOM   3285 C CD1 . ILE C 3 100 ? 12.124  40.777  14.029  1.000 42.696  0 100 ILE CCC CD1 1 ? 13 
ATOM   3286 N N   . THR C 3 101 ? 14.757  41.813  9.898   1.000 39.113  0 101 THR CCC N   1 ? 13 
ATOM   3287 C CA  . THR C 3 101 ? 14.399  41.306  8.551   1.000 39.646  0 101 THR CCC CA  1 ? 13 
ATOM   3288 C C   . THR C 3 101 ? 14.457  39.773  8.552   1.000 40.157  0 101 THR CCC C   1 ? 13 
ATOM   3289 O O   . THR C 3 101 ? 15.354  39.211  9.225   1.000 41.762  0 101 THR CCC O   1 ? 13 
ATOM   3290 C CB  . THR C 3 101 ? 15.298  41.936  7.482   1.000 38.879  0 101 THR CCC CB  1 ? 13 
ATOM   3291 O OG1 . THR C 3 101 ? 14.817  41.448  6.232   1.000 40.285  0 101 THR CCC OG1 1 ? 13 
ATOM   3292 C CG2 . THR C 3 101 ? 16.768  41.616  7.653   1.000 38.022  0 101 THR CCC CG2 1 ? 13 
ATOM   3293 N N   . THR C 3 102 ? 13.511  39.132  7.856   1.000 40.525  0 102 THR CCC N   1 ? 13 
ATOM   3294 C CA  . THR C 3 102 ? 13.547  37.690  7.494   1.000 41.340  0 102 THR CCC CA  1 ? 13 
ATOM   3295 C C   . THR C 3 102 ? 14.384  37.508  6.221   1.000 41.163  0 102 THR CCC C   1 ? 13 
ATOM   3296 O O   . THR C 3 102 ? 14.748  36.358  5.922   1.000 41.016  0 102 THR CCC O   1 ? 13 
ATOM   3297 C CB  . THR C 3 102 ? 12.141  37.111  7.279   1.000 42.495  0 102 THR CCC CB  1 ? 13 
ATOM   3298 O OG1 . THR C 3 102 ? 11.515  37.817  6.206   1.000 43.094  0 102 THR CCC OG1 1 ? 13 
ATOM   3299 C CG2 . THR C 3 102 ? 11.278  37.180  8.517   1.000 42.563  0 102 THR CCC CG2 1 ? 13 
ATOM   3300 N N   . ILE C 3 103 ? 14.646  38.598  5.489   1.000 40.723  0 103 ILE CCC N   1 ? 13 
ATOM   3301 C CA  . ILE C 3 103 ? 15.353  38.579  4.175   1.000 40.085  0 103 ILE CCC CA  1 ? 13 
ATOM   3302 C C   . ILE C 3 103 ? 16.856  38.573  4.448   1.000 38.869  0 103 ILE CCC C   1 ? 13 
ATOM   3303 O O   . ILE C 3 103 ? 17.372  39.584  4.974   1.000 38.273  0 103 ILE CCC O   1 ? 13 
ATOM   3304 C CB  . ILE C 3 103 ? 14.935  39.766  3.282   1.000 42.045  0 103 ILE CCC CB  1 ? 13 
ATOM   3305 C CG1 . ILE C 3 103 ? 13.414  39.829  3.095   1.000 44.066  0 103 ILE CCC CG1 1 ? 13 
ATOM   3306 C CG2 . ILE C 3 103 ? 15.667  39.711  1.946   1.000 43.006  0 103 ILE CCC CG2 1 ? 13 
ATOM   3307 C CD1 . ILE C 3 103 ? 12.944  40.945  2.194   1.000 45.317  0 103 ILE CCC CD1 1 ? 13 
ATOM   3308 N N   . VAL C 3 104 ? 17.522  37.468  4.112   1.000 38.459  0 104 VAL CCC N   1 ? 13 
ATOM   3309 C CA  . VAL C 3 104 ? 18.998  37.302  4.257   1.000 36.753  0 104 VAL CCC CA  1 ? 13 
ATOM   3310 C C   . VAL C 3 104 ? 19.642  37.649  2.914   1.000 37.666  0 104 VAL CCC C   1 ? 13 
ATOM   3311 O O   . VAL C 3 104 ? 19.553  36.834  1.973   1.000 39.268  0 104 VAL CCC O   1 ? 13 
ATOM   3312 C CB  . VAL C 3 104 ? 19.373  35.885  4.722   1.000 37.141  0 104 VAL CCC CB  1 ? 13 
ATOM   3313 C CG1 . VAL C 3 104 ? 20.867  35.780  4.992   1.000 35.807  0 104 VAL CCC CG1 1 ? 13 
ATOM   3314 C CG2 . VAL C 3 104 ? 18.565  35.463  5.949   1.000 37.715  0 104 VAL CCC CG2 1 ? 13 
ATOM   3315 N N   . ARG C 3 105 ? 20.220  38.846  2.829   1.000 37.895  0 105 ARG CCC N   1 ? 13 
ATOM   3316 C CA  . ARG C 3 105 ? 20.990  39.340  1.662   1.000 39.231  0 105 ARG CCC CA  1 ? 13 
ATOM   3317 C C   . ARG C 3 105 ? 22.482  39.220  1.991   1.000 40.015  0 105 ARG CCC C   1 ? 13 
ATOM   3318 O O   . ARG C 3 105 ? 22.928  39.902  2.940   1.000 39.492  0 105 ARG CCC O   1 ? 13 
ATOM   3319 C CB  . ARG C 3 105 ? 20.605  40.790  1.359   1.000 38.728  0 105 ARG CCC CB  1 ? 13 
ATOM   3320 C CG  . ARG C 3 105 ? 19.113  41.019  1.171   1.000 38.691  0 105 ARG CCC CG  1 ? 13 
ATOM   3321 C CD  . ARG C 3 105 ? 18.883  42.398  0.585   1.000 40.381  0 105 ARG CCC CD  1 ? 13 
ATOM   3322 N NE  . ARG C 3 105 ? 17.488  42.734  0.348   1.000 41.465  0 105 ARG CCC NE  1 ? 13 
ATOM   3323 C CZ  . ARG C 3 105 ? 16.736  42.247  -0.636  1.000 40.787  0 105 ARG CCC CZ  1 ? 13 
ATOM   3324 N NH1 . ARG C 3 105 ? 17.217  41.351  -1.479  1.000 40.179  0 105 ARG CCC NH1 1 ? 13 
ATOM   3325 N NH2 . ARG C 3 105 ? 15.478  42.634  -0.747  1.000 42.760  0 105 ARG CCC NH2 1 ? 13 
ATOM   3326 N N   . ALA C 3 106 ? 23.208  38.374  1.249   1.000 40.587  0 106 ALA CCC N   1 ? 13 
ATOM   3327 C CA  . ALA C 3 106 ? 24.666  38.151  1.392   1.000 39.089  0 106 ALA CCC CA  1 ? 13 
ATOM   3328 C C   . ALA C 3 106 ? 25.393  39.495  1.289   1.000 40.316  0 106 ALA CCC C   1 ? 13 
ATOM   3329 O O   . ALA C 3 106 ? 26.375  39.705  2.039   1.000 44.994  0 106 ALA CCC O   1 ? 13 
ATOM   3330 C CB  . ALA C 3 106 ? 25.151  37.182  0.348   1.000 39.605  0 106 ALA CCC CB  1 ? 13 
ATOM   3331 N N   . TYR C 3 107 ? 24.936  40.356  0.378   1.000 39.321  0 107 TYR CCC N   1 ? 13 
ATOM   3332 C CA  . TYR C 3 107 ? 25.420  41.748  0.202   1.000 39.168  0 107 TYR CCC CA  1 ? 13 
ATOM   3333 C C   . TYR C 3 107 ? 24.493  42.693  0.975   1.000 37.170  0 107 TYR CCC C   1 ? 13 
ATOM   3334 O O   . TYR C 3 107 ? 23.371  42.936  0.495   1.000 37.257  0 107 TYR CCC O   1 ? 13 
ATOM   3335 C CB  . TYR C 3 107 ? 25.463  42.126  -1.279  1.000 41.202  0 107 TYR CCC CB  1 ? 13 
ATOM   3336 C CG  . TYR C 3 107 ? 26.381  41.287  -2.134  1.000 43.074  0 107 TYR CCC CG  1 ? 13 
ATOM   3337 C CD1 . TYR C 3 107 ? 25.936  40.113  -2.723  1.000 42.828  0 107 TYR CCC CD1 1 ? 13 
ATOM   3338 C CD2 . TYR C 3 107 ? 27.687  41.679  -2.376  1.000 43.678  0 107 TYR CCC CD2 1 ? 13 
ATOM   3339 C CE1 . TYR C 3 107 ? 26.768  39.343  -3.519  1.000 44.243  0 107 TYR CCC CE1 1 ? 13 
ATOM   3340 C CE2 . TYR C 3 107 ? 28.533  40.918  -3.163  1.000 46.052  0 107 TYR CCC CE2 1 ? 13 
ATOM   3341 C CZ  . TYR C 3 107 ? 28.071  39.749  -3.742  1.000 46.581  0 107 TYR CCC CZ  1 ? 13 
ATOM   3342 O OH  . TYR C 3 107 ? 28.906  39.010  -4.529  1.000 49.668  0 107 TYR CCC OH  1 ? 13 
ATOM   3343 N N   . TYR C 3 108 ? 24.950  43.200  2.127   1.000 35.968  0 108 TYR CCC N   1 ? 13 
ATOM   3344 C CA  . TYR C 3 108 ? 24.190  44.124  3.012   1.000 36.258  0 108 TYR CCC CA  1 ? 13 
ATOM   3345 C C   . TYR C 3 108 ? 23.875  45.412  2.238   1.000 37.009  0 108 TYR CCC C   1 ? 13 
ATOM   3346 O O   . TYR C 3 108 ? 22.868  46.076  2.561   1.000 36.120  0 108 TYR CCC O   1 ? 13 
ATOM   3347 C CB  . TYR C 3 108 ? 24.959  44.424  4.307   1.000 35.979  0 108 TYR CCC CB  1 ? 13 
ATOM   3348 C CG  . TYR C 3 108 ? 25.958  45.544  4.171   1.000 37.061  0 108 TYR CCC CG  1 ? 13 
ATOM   3349 C CD1 . TYR C 3 108 ? 25.561  46.863  4.302   1.000 37.791  0 108 TYR CCC CD1 1 ? 13 
ATOM   3350 C CD2 . TYR C 3 108 ? 27.285  45.293  3.865   1.000 38.723  0 108 TYR CCC CD2 1 ? 13 
ATOM   3351 C CE1 . TYR C 3 108 ? 26.458  47.907  4.153   1.000 41.240  0 108 TYR CCC CE1 1 ? 13 
ATOM   3352 C CE2 . TYR C 3 108 ? 28.199  46.326  3.710   1.000 41.399  0 108 TYR CCC CE2 1 ? 13 
ATOM   3353 C CZ  . TYR C 3 108 ? 27.782  47.641  3.849   1.000 42.565  0 108 TYR CCC CZ  1 ? 13 
ATOM   3354 O OH  . TYR C 3 108 ? 28.651  48.683  3.698   1.000 43.164  0 108 TYR CCC OH  1 ? 13 
ATOM   3355 N N   . THR C 3 109 ? 24.705  45.736  1.241   1.000 38.304  0 109 THR CCC N   1 ? 13 
ATOM   3356 C CA  . THR C 3 109 ? 24.599  46.940  0.371   1.000 40.346  0 109 THR CCC CA  1 ? 13 
ATOM   3357 C C   . THR C 3 109 ? 23.272  46.953  -0.407  1.000 40.399  0 109 THR CCC C   1 ? 13 
ATOM   3358 O O   . THR C 3 109 ? 22.952  48.005  -1.002  1.000 41.580  0 109 THR CCC O   1 ? 13 
ATOM   3359 C CB  . THR C 3 109 ? 25.785  47.004  -0.597  1.000 43.342  0 109 THR CCC CB  1 ? 13 
ATOM   3360 O OG1 . THR C 3 109 ? 25.753  45.821  -1.400  1.000 45.477  0 109 THR CCC OG1 1 ? 13 
ATOM   3361 C CG2 . THR C 3 109 ? 27.113  47.128  0.122   1.000 43.988  0 109 THR CCC CG2 1 ? 13 
ATOM   3362 N N   . GLU C 3 110 ? 22.536  45.838  -0.411  1.000 39.313  0 110 GLU CCC N   1 ? 13 
ATOM   3363 C CA  . GLU C 3 110 ? 21.240  45.697  -1.125  1.000 42.511  0 110 GLU CCC CA  1 ? 13 
ATOM   3364 C C   . GLU C 3 110 ? 20.063  45.843  -0.148  1.000 42.514  0 110 GLU CCC C   1 ? 13 
ATOM   3365 O O   . GLU C 3 110 ? 18.915  45.799  -0.621  1.000 45.184  0 110 GLU CCC O   1 ? 13 
ATOM   3366 C CB  . GLU C 3 110 ? 21.195  44.365  -1.883  1.000 43.573  0 110 GLU CCC CB  1 ? 13 
ATOM   3367 C CG  . GLU C 3 110 ? 22.223  44.278  -3.006  1.000 45.974  0 110 GLU CCC CG  1 ? 13 
ATOM   3368 C CD  . GLU C 3 110 ? 21.868  43.360  -4.169  1.000 47.763  0 110 GLU CCC CD  1 ? 13 
ATOM   3369 O OE1 . GLU C 3 110 ? 21.192  42.335  -3.947  1.000 49.754  0 110 GLU CCC OE1 1 ? 13 
ATOM   3370 O OE2 . GLU C 3 110 ? 22.267  43.675  -5.300  1.000 48.875  0 110 GLU CCC OE2 1 ? 13 
ATOM   3371 N N   . TYR C 3 111 ? 20.311  46.028  1.153   1.000 40.510  0 111 TYR CCC N   1 ? 13 
ATOM   3372 C CA  . TYR C 3 111 ? 19.229  46.213  2.156   1.000 40.318  0 111 TYR CCC CA  1 ? 13 
ATOM   3373 C C   . TYR C 3 111 ? 18.624  47.611  1.980   1.000 41.512  0 111 TYR CCC C   1 ? 13 
ATOM   3374 O O   . TYR C 3 111 ? 19.381  48.580  1.796   1.000 39.262  0 111 TYR CCC O   1 ? 13 
ATOM   3375 C CB  . TYR C 3 111 ? 19.716  45.985  3.593   1.000 38.953  0 111 TYR CCC CB  1 ? 13 
ATOM   3376 C CG  . TYR C 3 111 ? 19.710  44.547  4.049   1.000 38.508  0 111 TYR CCC CG  1 ? 13 
ATOM   3377 C CD1 . TYR C 3 111 ? 18.571  43.769  3.936   1.000 39.656  0 111 TYR CCC CD1 1 ? 13 
ATOM   3378 C CD2 . TYR C 3 111 ? 20.832  43.961  4.614   1.000 37.725  0 111 TYR CCC CD2 1 ? 13 
ATOM   3379 C CE1 . TYR C 3 111 ? 18.542  42.449  4.359   1.000 39.095  0 111 TYR CCC CE1 1 ? 13 
ATOM   3380 C CE2 . TYR C 3 111 ? 20.826  42.640  5.035   1.000 36.846  0 111 TYR CCC CE2 1 ? 13 
ATOM   3381 C CZ  . TYR C 3 111 ? 19.676  41.880  4.910   1.000 37.404  0 111 TYR CCC CZ  1 ? 13 
ATOM   3382 O OH  . TYR C 3 111 ? 19.652  40.576  5.312   1.000 37.776  0 111 TYR CCC OH  1 ? 13 
ATOM   3383 N N   . THR C 3 112 ? 17.287  47.684  1.995   1.000 43.431  0 112 THR CCC N   1 ? 13 
ATOM   3384 C CA  . THR C 3 112 ? 16.486  48.933  2.120   1.000 44.595  0 112 THR CCC CA  1 ? 13 
ATOM   3385 C C   . THR C 3 112 ? 15.473  48.755  3.255   1.000 44.853  0 112 THR CCC C   1 ? 13 
ATOM   3386 O O   . THR C 3 112 ? 15.258  47.599  3.683   1.000 43.636  0 112 THR CCC O   1 ? 13 
ATOM   3387 C CB  . THR C 3 112 ? 15.773  49.291  0.810   1.000 46.839  0 112 THR CCC CB  1 ? 13 
ATOM   3388 O OG1 . THR C 3 112 ? 14.563  48.538  0.734   1.000 46.871  0 112 THR CCC OG1 1 ? 13 
ATOM   3389 C CG2 . THR C 3 112 ? 16.609  49.021  -0.424  1.000 47.160  0 112 THR CCC CG2 1 ? 13 
ATOM   3390 N N   . GLU C 3 113 ? 14.850  49.852  3.691   1.000 48.030  0 113 GLU CCC N   1 ? 13 
ATOM   3391 C CA  . GLU C 3 113 ? 13.857  49.865  4.802   1.000 50.664  0 113 GLU CCC CA  1 ? 13 
ATOM   3392 C C   . GLU C 3 113 ? 12.699  48.915  4.465   1.000 48.880  0 113 GLU CCC C   1 ? 13 
ATOM   3393 O O   . GLU C 3 113 ? 12.143  48.315  5.409   1.000 48.869  0 113 GLU CCC O   1 ? 13 
ATOM   3394 C CB  . GLU C 3 113 ? 13.429  51.303  5.113   1.000 56.285  0 113 GLU CCC CB  1 ? 13 
ATOM   3395 C CG  . GLU C 3 113 ? 11.936  51.525  5.209   1.000 61.418  0 113 GLU CCC CG  1 ? 13 
ATOM   3396 C CD  . GLU C 3 113 ? 11.322  51.949  3.893   1.000 66.876  0 113 GLU CCC CD  1 ? 13 
ATOM   3397 O OE1 . GLU C 3 113 ? 11.665  53.054  3.431   1.000 70.688  0 113 GLU CCC OE1 1 ? 13 
ATOM   3398 O OE2 . GLU C 3 113 ? 10.514  51.173  3.336   1.000 74.057  0 113 GLU CCC OE2 1 ? 13 
ATOM   3399 N N   . ALA C 3 114 ? 12.383  48.744  3.178   1.000 47.609  0 114 ALA CCC N   1 ? 13 
ATOM   3400 C CA  . ALA C 3 114 ? 11.301  47.858  2.679   1.000 47.682  0 114 ALA CCC CA  1 ? 13 
ATOM   3401 C C   . ALA C 3 114 ? 11.536  46.402  3.112   1.000 45.129  0 114 ALA CCC C   1 ? 13 
ATOM   3402 O O   . ALA C 3 114 ? 10.556  45.654  3.186   1.000 46.089  0 114 ALA CCC O   1 ? 13 
ATOM   3403 C CB  . ALA C 3 114 ? 11.185  47.970  1.179   1.000 47.823  0 114 ALA CCC CB  1 ? 13 
ATOM   3404 N N   . ASP C 3 115 ? 12.782  46.009  3.388   1.000 43.659  0 115 ASP CCC N   1 ? 13 
ATOM   3405 C CA  . ASP C 3 115 ? 13.143  44.622  3.792   1.000 42.700  0 115 ASP CCC CA  1 ? 13 
ATOM   3406 C C   . ASP C 3 115 ? 12.811  44.375  5.268   1.000 41.210  0 115 ASP CCC C   1 ? 13 
ATOM   3407 O O   . ASP C 3 115 ? 12.741  43.192  5.663   1.000 40.573  0 115 ASP CCC O   1 ? 13 
ATOM   3408 C CB  . ASP C 3 115 ? 14.624  44.346  3.538   1.000 42.515  0 115 ASP CCC CB  1 ? 13 
ATOM   3409 C CG  . ASP C 3 115 ? 15.029  44.485  2.079   1.000 44.893  0 115 ASP CCC CG  1 ? 13 
ATOM   3410 O OD1 . ASP C 3 115 ? 14.215  44.108  1.200   1.000 46.017  0 115 ASP CCC OD1 1 ? 13 
ATOM   3411 O OD2 . ASP C 3 115 ? 16.160  44.958  1.827   1.000 45.099  0 115 ASP CCC OD2 1 ? 13 
ATOM   3412 N N   . PHE C 3 116 ? 12.615  45.437  6.055   1.000 41.499  0 116 PHE CCC N   1 ? 13 
ATOM   3413 C CA  . PHE C 3 116 ? 12.560  45.367  7.540   1.000 42.362  0 116 PHE CCC CA  1 ? 13 
ATOM   3414 C C   . PHE C 3 116 ? 11.129  45.583  8.031   1.000 44.212  0 116 PHE CCC C   1 ? 13 
ATOM   3415 O O   . PHE C 3 116 ? 10.329  46.233  7.331   1.000 45.889  0 116 PHE CCC O   1 ? 13 
ATOM   3416 C CB  . PHE C 3 116 ? 13.541  46.365  8.161   1.000 41.236  0 116 PHE CCC CB  1 ? 13 
ATOM   3417 C CG  . PHE C 3 116 ? 14.987  46.001  7.945   1.000 40.520  0 116 PHE CCC CG  1 ? 13 
ATOM   3418 C CD1 . PHE C 3 116 ? 15.592  46.228  6.715   1.000 40.113  0 116 PHE CCC CD1 1 ? 13 
ATOM   3419 C CD2 . PHE C 3 116 ? 15.739  45.418  8.960   1.000 41.087  0 116 PHE CCC CD2 1 ? 13 
ATOM   3420 C CE1 . PHE C 3 116 ? 16.918  45.886  6.502   1.000 39.748  0 116 PHE CCC CE1 1 ? 13 
ATOM   3421 C CE2 . PHE C 3 116 ? 17.069  45.081  8.745   1.000 39.245  0 116 PHE CCC CE2 1 ? 13 
ATOM   3422 C CZ  . PHE C 3 116 ? 17.651  45.306  7.514   1.000 39.045  0 116 PHE CCC CZ  1 ? 13 
ATOM   3423 N N   . GLY C 3 117 ? 10.841  45.023  9.209   1.000 44.684  0 117 GLY CCC N   1 ? 13 
ATOM   3424 C CA  . GLY C 3 117 ? 9.543   45.095  9.903   1.000 45.461  0 117 GLY CCC CA  1 ? 13 
ATOM   3425 C C   . GLY C 3 117 ? 9.740   45.096  11.407  1.000 45.370  0 117 GLY CCC C   1 ? 13 
ATOM   3426 O O   . GLY C 3 117 ? 10.901  45.204  11.854  1.000 43.712  0 117 GLY CCC O   1 ? 13 
ATOM   3427 N N   . SER C 3 118 ? 8.649   44.979  12.165  1.000 47.425  0 118 SER CCC N   1 ? 13 
ATOM   3428 C CA  . SER C 3 118 ? 8.641   45.061  13.647  1.000 48.249  0 118 SER CCC CA  1 ? 13 
ATOM   3429 C C   . SER C 3 118 ? 9.412   46.312  14.082  1.000 47.981  0 118 SER CCC C   1 ? 13 
ATOM   3430 O O   . SER C 3 118 ? 10.238  46.203  15.004  1.000 48.588  0 118 SER CCC O   1 ? 13 
ATOM   3431 C CB  . SER C 3 118 ? 9.214   43.807  14.254  1.000 46.917  0 118 SER CCC CB  1 ? 13 
ATOM   3432 O OG  . SER C 3 118 ? 8.392   42.686  13.967  1.000 48.309  0 118 SER CCC OG  1 ? 13 
ATOM   3433 N N   . TRP C 3 119 ? 9.148   47.448  13.426  1.000 49.534  0 119 TRP CCC N   1 ? 13 
ATOM   3434 C CA  . TRP C 3 119 ? 9.821   48.747  13.683  1.000 50.114  0 119 TRP CCC CA  1 ? 13 
ATOM   3435 C C   . TRP C 3 119 ? 9.625   49.136  15.150  1.000 53.165  0 119 TRP CCC C   1 ? 13 
ATOM   3436 O O   . TRP C 3 119 ? 8.468   49.158  15.603  1.000 55.858  0 119 TRP CCC O   1 ? 13 
ATOM   3437 C CB  . TRP C 3 119 ? 9.294   49.840  12.748  1.000 50.958  0 119 TRP CCC CB  1 ? 13 
ATOM   3438 C CG  . TRP C 3 119 ? 9.661   49.638  11.311  1.000 50.865  0 119 TRP CCC CG  1 ? 13 
ATOM   3439 C CD1 . TRP C 3 119 ? 8.895   49.067  10.338  1.000 51.951  0 119 TRP CCC CD1 1 ? 13 
ATOM   3440 C CD2 . TRP C 3 119 ? 10.900  49.997  10.679  1.000 49.010  0 119 TRP CCC CD2 1 ? 13 
ATOM   3441 N NE1 . TRP C 3 119 ? 9.567   49.051  9.145   1.000 51.117  0 119 TRP CCC NE1 1 ? 13 
ATOM   3442 C CE2 . TRP C 3 119 ? 10.799  49.623  9.320   1.000 49.163  0 119 TRP CCC CE2 1 ? 13 
ATOM   3443 C CE3 . TRP C 3 119 ? 12.072  50.614  11.123  1.000 48.699  0 119 TRP CCC CE3 1 ? 13 
ATOM   3444 C CZ2 . TRP C 3 119 ? 11.832  49.836  8.408   1.000 48.232  0 119 TRP CCC CZ2 1 ? 13 
ATOM   3445 C CZ3 . TRP C 3 119 ? 13.094  50.822  10.224  1.000 48.137  0 119 TRP CCC CZ3 1 ? 13 
ATOM   3446 C CH2 . TRP C 3 119 ? 12.978  50.432  8.887   1.000 48.663  0 119 TRP CCC CH2 1 ? 13 
ATOM   3447 N N   . GLY C 3 120 ? 10.723  49.420  15.857  1.000 54.844  0 120 GLY CCC N   1 ? 13 
ATOM   3448 C CA  . GLY C 3 120 ? 10.701  50.086  17.170  1.000 57.646  0 120 GLY CCC CA  1 ? 13 
ATOM   3449 C C   . GLY C 3 120 ? 10.142  51.493  17.043  1.000 60.580  0 120 GLY CCC C   1 ? 13 
ATOM   3450 O O   . GLY C 3 120 ? 10.153  52.036  15.911  1.000 61.487  0 120 GLY CCC O   1 ? 13 
ATOM   3451 N N   . GLN C 3 121 ? 9.633   52.051  18.145  1.000 62.265  0 121 GLN CCC N   1 ? 13 
ATOM   3452 C CA  . GLN C 3 121 ? 9.220   53.474  18.235  1.000 63.814  0 121 GLN CCC CA  1 ? 13 
ATOM   3453 C C   . GLN C 3 121 ? 10.471  54.326  18.008  1.000 62.580  0 121 GLN CCC C   1 ? 13 
ATOM   3454 O O   . GLN C 3 121 ? 11.495  54.009  18.632  1.000 63.142  0 121 GLN CCC O   1 ? 13 
ATOM   3455 C CB  . GLN C 3 121 ? 8.575   53.752  19.596  1.000 66.614  0 121 GLN CCC CB  1 ? 13 
ATOM   3456 C CG  . GLN C 3 121 ? 8.789   55.176  20.098  1.000 69.268  0 121 GLN CCC CG  1 ? 13 
ATOM   3457 C CD  . GLN C 3 121 ? 8.215   55.412  21.475  1.000 73.130  0 121 GLN CCC CD  1 ? 13 
ATOM   3458 O OE1 . GLN C 3 121 ? 8.012   54.480  22.253  1.000 74.061  0 121 GLN CCC OE1 1 ? 13 
ATOM   3459 N NE2 . GLN C 3 121 ? 7.955   56.672  21.791  1.000 76.012  0 121 GLN CCC NE2 1 ? 13 
ATOM   3460 N N   . GLY C 3 122 ? 10.402  55.343  17.146  1.000 62.026  0 122 GLY CCC N   1 ? 13 
ATOM   3461 C CA  . GLY C 3 122 ? 11.545  56.225  16.848  1.000 61.831  0 122 GLY CCC CA  1 ? 13 
ATOM   3462 C C   . GLY C 3 122 ? 12.050  56.927  18.098  1.000 63.398  0 122 GLY CCC C   1 ? 13 
ATOM   3463 O O   . GLY C 3 122 ? 11.217  57.246  18.964  1.000 66.734  0 122 GLY CCC O   1 ? 13 
ATOM   3464 N N   . THR C 3 123 ? 13.366  57.143  18.198  1.000 62.432  0 123 THR CCC N   1 ? 13 
ATOM   3465 C CA  . THR C 3 123 ? 14.018  57.943  19.269  1.000 63.940  0 123 THR CCC CA  1 ? 13 
ATOM   3466 C C   . THR C 3 123 ? 14.797  59.085  18.603  1.000 64.897  0 123 THR CCC C   1 ? 13 
ATOM   3467 O O   . THR C 3 123 ? 15.556  58.813  17.655  1.000 63.553  0 123 THR CCC O   1 ? 13 
ATOM   3468 C CB  . THR C 3 123 ? 14.865  57.049  20.186  1.000 62.645  0 123 THR CCC CB  1 ? 13 
ATOM   3469 O OG1 . THR C 3 123 ? 15.262  57.844  21.303  1.000 65.851  0 123 THR CCC OG1 1 ? 13 
ATOM   3470 C CG2 . THR C 3 123 ? 16.093  56.470  19.517  1.000 61.353  0 123 THR CCC CG2 1 ? 13 
ATOM   3471 N N   . GLN C 3 124 ? 14.583  60.321  19.063  1.000 68.459  0 124 GLN CCC N   1 ? 13 
ATOM   3472 C CA  . GLN C 3 124 ? 15.161  61.555  18.466  1.000 70.055  0 124 GLN CCC CA  1 ? 13 
ATOM   3473 C C   . GLN C 3 124 ? 16.628  61.677  18.891  1.000 70.842  0 124 GLN CCC C   1 ? 13 
ATOM   3474 O O   . GLN C 3 124 ? 16.916  61.520  20.090  1.000 71.825  0 124 GLN CCC O   1 ? 13 
ATOM   3475 C CB  . GLN C 3 124 ? 14.341  62.780  18.884  1.000 73.619  0 124 GLN CCC CB  1 ? 13 
ATOM   3476 C CG  . GLN C 3 124 ? 14.846  64.101  18.314  1.000 76.177  0 124 GLN CCC CG  1 ? 13 
ATOM   3477 C CD  . GLN C 3 124 ? 14.755  64.186  16.808  1.000 74.963  0 124 GLN CCC CD  1 ? 13 
ATOM   3478 O OE1 . GLN C 3 124 ? 13.684  64.060  16.216  1.000 75.159  0 124 GLN CCC OE1 1 ? 13 
ATOM   3479 N NE2 . GLN C 3 124 ? 15.893  64.415  16.171  1.000 74.199  0 124 GLN CCC NE2 1 ? 13 
ATOM   3480 N N   . VAL C 3 125 ? 17.513  61.934  17.925  1.000 71.290  0 125 VAL CCC N   1 ? 13 
ATOM   3481 C CA  . VAL C 3 125 ? 18.954  62.261  18.134  1.000 73.572  0 125 VAL CCC CA  1 ? 13 
ATOM   3482 C C   . VAL C 3 125 ? 19.200  63.644  17.522  1.000 76.317  0 125 VAL CCC C   1 ? 13 
ATOM   3483 O O   . VAL C 3 125 ? 18.901  63.806  16.320  1.000 76.535  0 125 VAL CCC O   1 ? 13 
ATOM   3484 C CB  . VAL C 3 125 ? 19.869  61.193  17.502  1.000 72.413  0 125 VAL CCC CB  1 ? 13 
ATOM   3485 C CG1 . VAL C 3 125 ? 21.344  61.520  17.691  1.000 73.792  0 125 VAL CCC CG1 1 ? 13 
ATOM   3486 C CG2 . VAL C 3 125 ? 19.557  59.798  18.027  1.000 70.474  0 125 VAL CCC CG2 1 ? 13 
ATOM   3487 N N   . THR C 3 126 ? 19.700  64.594  18.319  1.000 79.298  0 126 THR CCC N   1 ? 13 
ATOM   3488 C CA  . THR C 3 126 ? 19.953  66.004  17.913  1.000 83.271  0 126 THR CCC CA  1 ? 13 
ATOM   3489 C C   . THR C 3 126 ? 21.403  66.377  18.238  1.000 85.837  0 126 THR CCC C   1 ? 13 
ATOM   3490 O O   . THR C 3 126 ? 21.807  66.212  19.408  1.000 86.678  0 126 THR CCC O   1 ? 13 
ATOM   3491 C CB  . THR C 3 126 ? 18.960  66.956  18.591  1.000 86.185  0 126 THR CCC CB  1 ? 13 
ATOM   3492 O OG1 . THR C 3 126 ? 17.646  66.456  18.348  1.000 84.095  0 126 THR CCC OG1 1 ? 13 
ATOM   3493 C CG2 . THR C 3 126 ? 19.065  68.382  18.095  1.000 89.719  0 126 THR CCC CG2 1 ? 13 
ATOM   3494 N N   . VAL C 3 127 ? 22.140  66.866  17.233  1.000 87.212  0 127 VAL CCC N   1 ? 13 
ATOM   3495 C CA  . VAL C 3 127 ? 23.567  67.296  17.337  1.000 89.337  0 127 VAL CCC CA  1 ? 13 
ATOM   3496 C C   . VAL C 3 127 ? 23.672  68.753  16.868  1.000 93.102  0 127 VAL CCC C   1 ? 13 
ATOM   3497 O O   . VAL C 3 127 ? 23.220  69.034  15.743  1.000 92.637  0 127 VAL CCC O   1 ? 13 
ATOM   3498 C CB  . VAL C 3 127 ? 24.478  66.374  16.505  1.000 87.146  0 127 VAL CCC CB  1 ? 13 
ATOM   3499 C CG1 . VAL C 3 127 ? 25.952  66.677  16.735  1.000 89.951  0 127 VAL CCC CG1 1 ? 13 
ATOM   3500 C CG2 . VAL C 3 127 ? 24.186  64.902  16.761  1.000 83.052  0 127 VAL CCC CG2 1 ? 13 
ATOM   3501 N N   . SER C 3 128 ? 24.255  69.636  17.688  1.000 97.186  0 128 SER CCC N   1 ? 13 
ATOM   3502 C CA  . SER C 3 128 ? 24.475  71.077  17.381  1.000 101.693 0 128 SER CCC CA  1 ? 13 
ATOM   3503 C C   . SER C 3 128 ? 25.792  71.557  18.002  1.000 104.949 0 128 SER CCC C   1 ? 13 
ATOM   3504 O O   . SER C 3 128 ? 26.164  72.726  17.867  1.000 109.110 0 128 SER CCC O   1 ? 13 
ATOM   3505 C CB  . SER C 3 128 ? 23.313  71.914  17.852  1.000 104.499 0 128 SER CCC CB  1 ? 13 
ATOM   3506 O OG  . SER C 3 128 ? 23.187  71.862  19.264  1.000 105.511 0 128 SER CCC OG  1 ? 13 
ATOM   3507 N N   . GLN D 1 1   ? 18.917  -4.231  55.635  1.000 61.586  0 3   GLN DDD N   1 ? 14 
ATOM   3508 C CA  . GLN D 1 1   ? 17.832  -3.243  55.812  1.000 61.447  0 3   GLN DDD CA  1 ? 14 
ATOM   3509 C C   . GLN D 1 1   ? 18.402  -1.824  55.686  1.000 57.299  0 3   GLN DDD C   1 ? 14 
ATOM   3510 O O   . GLN D 1 1   ? 19.406  -1.540  56.358  1.000 57.555  0 3   GLN DDD O   1 ? 14 
ATOM   3511 C CB  . GLN D 1 1   ? 17.164  -3.505  57.164  1.000 65.792  0 3   GLN DDD CB  1 ? 14 
ATOM   3512 C CG  . GLN D 1 1   ? 16.340  -2.341  57.686  1.000 67.571  0 3   GLN DDD CG  1 ? 14 
ATOM   3513 C CD  . GLN D 1 1   ? 15.325  -2.763  58.720  1.000 72.812  0 3   GLN DDD CD  1 ? 14 
ATOM   3514 O OE1 . GLN D 1 1   ? 14.906  -3.920  58.778  1.000 76.565  0 3   GLN DDD OE1 1 ? 14 
ATOM   3515 N NE2 . GLN D 1 1   ? 14.910  -1.812  59.542  1.000 73.598  0 3   GLN DDD NE2 1 ? 14 
ATOM   3516 N N   . VAL D 1 2   ? 17.780  -0.974  54.860  1.000 54.939  0 4   VAL DDD N   1 ? 14 
ATOM   3517 C CA  . VAL D 1 2   ? 18.078  0.487   54.776  1.000 52.910  0 4   VAL DDD CA  1 ? 14 
ATOM   3518 C C   . VAL D 1 2   ? 17.436  1.163   55.991  1.000 53.420  0 4   VAL DDD C   1 ? 14 
ATOM   3519 O O   . VAL D 1 2   ? 16.208  1.039   56.157  1.000 55.663  0 4   VAL DDD O   1 ? 14 
ATOM   3520 C CB  . VAL D 1 2   ? 17.575  1.117   53.461  1.000 52.238  0 4   VAL DDD CB  1 ? 14 
ATOM   3521 C CG1 . VAL D 1 2   ? 17.777  2.626   53.448  1.000 51.321  0 4   VAL DDD CG1 1 ? 14 
ATOM   3522 C CG2 . VAL D 1 2   ? 18.235  0.488   52.246  1.000 52.465  0 4   VAL DDD CG2 1 ? 14 
ATOM   3523 N N   . GLN D 1 3   ? 18.240  1.846   56.803  1.000 53.084  0 5   GLN DDD N   1 ? 14 
ATOM   3524 C CA  . GLN D 1 3   ? 17.784  2.566   58.018  1.000 54.593  0 5   GLN DDD CA  1 ? 14 
ATOM   3525 C C   . GLN D 1 3   ? 18.012  4.066   57.816  1.000 53.452  0 5   GLN DDD C   1 ? 14 
ATOM   3526 O O   . GLN D 1 3   ? 19.158  4.456   57.534  1.000 53.375  0 5   GLN DDD O   1 ? 14 
ATOM   3527 C CB  . GLN D 1 3   ? 18.521  2.033   59.248  1.000 56.488  0 5   GLN DDD CB  1 ? 14 
ATOM   3528 C CG  . GLN D 1 3   ? 18.225  0.567   59.538  1.000 59.046  0 5   GLN DDD CG  1 ? 14 
ATOM   3529 C CD  . GLN D 1 3   ? 19.308  -0.092  60.357  1.000 61.744  0 5   GLN DDD CD  1 ? 14 
ATOM   3530 O OE1 . GLN D 1 3   ? 19.074  -0.551  61.472  1.000 64.218  0 5   GLN DDD OE1 1 ? 14 
ATOM   3531 N NE2 . GLN D 1 3   ? 20.510  -0.149  59.802  1.000 61.666  0 5   GLN DDD NE2 1 ? 14 
ATOM   3532 N N   . LEU D 1 4   ? 16.951  4.861   57.943  1.000 53.912  0 6   LEU DDD N   1 ? 14 
ATOM   3533 C CA  . LEU D 1 4   ? 17.008  6.341   57.890  1.000 53.948  0 6   LEU DDD CA  1 ? 14 
ATOM   3534 C C   . LEU D 1 4   ? 16.618  6.892   59.267  1.000 54.268  0 6   LEU DDD C   1 ? 14 
ATOM   3535 O O   . LEU D 1 4   ? 15.420  6.869   59.605  1.000 55.320  0 6   LEU DDD O   1 ? 14 
ATOM   3536 C CB  . LEU D 1 4   ? 16.073  6.835   56.782  1.000 54.423  0 6   LEU DDD CB  1 ? 14 
ATOM   3537 C CG  . LEU D 1 4   ? 16.386  6.334   55.371  1.000 54.966  0 6   LEU DDD CG  1 ? 14 
ATOM   3538 C CD1 . LEU D 1 4   ? 15.437  6.955   54.358  1.000 56.861  0 6   LEU DDD CD1 1 ? 14 
ATOM   3539 C CD2 . LEU D 1 4   ? 17.822  6.628   54.971  1.000 54.533  0 6   LEU DDD CD2 1 ? 14 
ATOM   3540 N N   . VAL D 1 5   ? 17.606  7.355   60.037  1.000 54.698  0 7   VAL DDD N   1 ? 14 
ATOM   3541 C CA  . VAL D 1 5   ? 17.417  7.880   61.419  1.000 57.068  0 7   VAL DDD CA  1 ? 14 
ATOM   3542 C C   . VAL D 1 5   ? 17.361  9.410   61.358  1.000 58.298  0 7   VAL DDD C   1 ? 14 
ATOM   3543 O O   . VAL D 1 5   ? 18.375  10.018  61.004  1.000 57.843  0 7   VAL DDD O   1 ? 14 
ATOM   3544 C CB  . VAL D 1 5   ? 18.527  7.367   62.357  1.000 58.098  0 7   VAL DDD CB  1 ? 14 
ATOM   3545 C CG1 . VAL D 1 5   ? 18.335  7.847   63.790  1.000 59.913  0 7   VAL DDD CG1 1 ? 14 
ATOM   3546 C CG2 . VAL D 1 5   ? 18.617  5.847   62.319  1.000 58.447  0 7   VAL DDD CG2 1 ? 14 
ATOM   3547 N N   . GLU D 1 6   ? 16.211  9.997   61.696  1.000 62.097  0 8   GLU DDD N   1 ? 14 
ATOM   3548 C CA  . GLU D 1 6   ? 15.987  11.468  61.735  1.000 65.152  0 8   GLU DDD CA  1 ? 14 
ATOM   3549 C C   . GLU D 1 6   ? 16.132  11.972  63.172  1.000 68.170  0 8   GLU DDD C   1 ? 14 
ATOM   3550 O O   . GLU D 1 6   ? 15.666  11.267  64.085  1.000 70.386  0 8   GLU DDD O   1 ? 14 
ATOM   3551 C CB  . GLU D 1 6   ? 14.588  11.839  61.239  1.000 67.386  0 8   GLU DDD CB  1 ? 14 
ATOM   3552 C CG  . GLU D 1 6   ? 14.262  11.322  59.853  1.000 68.622  0 8   GLU DDD CG  1 ? 14 
ATOM   3553 C CD  . GLU D 1 6   ? 13.084  10.367  59.804  1.000 71.950  0 8   GLU DDD CD  1 ? 14 
ATOM   3554 O OE1 . GLU D 1 6   ? 13.060  9.413   60.614  1.000 73.551  0 8   GLU DDD OE1 1 ? 14 
ATOM   3555 O OE2 . GLU D 1 6   ? 12.189  10.585  58.963  1.000 74.311  0 8   GLU DDD OE2 1 ? 14 
ATOM   3556 N N   . SER D 1 7   ? 16.727  13.157  63.350  1.000 70.615  0 9   SER DDD N   1 ? 14 
ATOM   3557 C CA  . SER D 1 7   ? 16.810  13.886  64.644  1.000 73.775  0 9   SER DDD CA  1 ? 14 
ATOM   3558 C C   . SER D 1 7   ? 16.817  15.398  64.388  1.000 74.990  0 9   SER DDD C   1 ? 14 
ATOM   3559 O O   . SER D 1 7   ? 16.925  15.801  63.209  1.000 71.156  0 9   SER DDD O   1 ? 14 
ATOM   3560 C CB  . SER D 1 7   ? 18.014  13.444  65.444  1.000 75.336  0 9   SER DDD CB  1 ? 14 
ATOM   3561 O OG  . SER D 1 7   ? 19.210  13.591  64.692  1.000 75.027  0 9   SER DDD OG  1 ? 14 
ATOM   3562 N N   . GLY D 1 8   ? 16.676  16.195  65.456  1.000 79.532  0 10  GLY DDD N   1 ? 14 
ATOM   3563 C CA  . GLY D 1 8   ? 16.743  17.670  65.423  1.000 81.208  0 10  GLY DDD CA  1 ? 14 
ATOM   3564 C C   . GLY D 1 8   ? 15.370  18.324  65.404  1.000 81.409  0 10  GLY DDD C   1 ? 14 
ATOM   3565 O O   . GLY D 1 8   ? 15.311  19.559  65.209  1.000 83.245  0 10  GLY DDD O   1 ? 14 
ATOM   3566 N N   . GLY D 1 9   ? 14.302  17.545  65.605  1.000 83.150  0 11  GLY DDD N   1 ? 14 
ATOM   3567 C CA  . GLY D 1 9   ? 12.915  18.046  65.666  1.000 85.686  0 11  GLY DDD CA  1 ? 14 
ATOM   3568 C C   . GLY D 1 9   ? 12.573  18.596  67.042  1.000 88.956  0 11  GLY DDD C   1 ? 14 
ATOM   3569 O O   . GLY D 1 9   ? 13.505  18.975  67.782  1.000 87.726  0 11  GLY DDD O   1 ? 14 
ATOM   3570 N N   . GLY D 1 10  ? 11.277  18.647  67.366  1.000 93.254  0 12  GLY DDD N   1 ? 14 
ATOM   3571 C CA  . GLY D 1 10  ? 10.757  19.050  68.688  1.000 98.764  0 12  GLY DDD CA  1 ? 14 
ATOM   3572 C C   . GLY D 1 10  ? 9.946   20.333  68.620  1.000 100.713 0 12  GLY DDD C   1 ? 14 
ATOM   3573 O O   . GLY D 1 10  ? 9.361   20.618  67.549  1.000 98.650  0 12  GLY DDD O   1 ? 14 
ATOM   3574 N N   . LEU D 1 11  ? 9.916   21.078  69.731  1.000 102.227 0 13  LEU DDD N   1 ? 14 
ATOM   3575 C CA  . LEU D 1 11  ? 9.111   22.315  69.915  1.000 102.304 0 13  LEU DDD CA  1 ? 14 
ATOM   3576 C C   . LEU D 1 11  ? 9.988   23.544  69.644  1.000 103.253 0 13  LEU DDD C   1 ? 14 
ATOM   3577 O O   . LEU D 1 11  ? 11.148  23.555  70.100  1.000 104.063 0 13  LEU DDD O   1 ? 14 
ATOM   3578 C CB  . LEU D 1 11  ? 8.557   22.331  71.344  1.000 104.799 0 13  LEU DDD CB  1 ? 14 
ATOM   3579 C CG  . LEU D 1 11  ? 7.426   23.323  71.613  1.000 104.586 0 13  LEU DDD CG  1 ? 14 
ATOM   3580 C CD1 . LEU D 1 11  ? 6.126   22.864  70.962  1.000 104.412 0 13  LEU DDD CD1 1 ? 14 
ATOM   3581 C CD2 . LEU D 1 11  ? 7.230   23.519  73.110  1.000 106.247 0 13  LEU DDD CD2 1 ? 14 
ATOM   3582 N N   . VAL D 1 12  ? 9.444   24.522  68.910  1.000 105.918 0 14  VAL DDD N   1 ? 14 
ATOM   3583 C CA  . VAL D 1 12  ? 10.039  25.874  68.662  1.000 107.330 0 14  VAL DDD CA  1 ? 14 
ATOM   3584 C C   . VAL D 1 12  ? 8.883   26.878  68.545  1.000 108.495 0 14  VAL DDD C   1 ? 14 
ATOM   3585 O O   . VAL D 1 12  ? 7.718   26.436  68.606  1.000 108.326 0 14  VAL DDD O   1 ? 14 
ATOM   3586 C CB  . VAL D 1 12  ? 10.938  25.899  67.406  1.000 106.820 0 14  VAL DDD CB  1 ? 14 
ATOM   3587 C CG1 . VAL D 1 12  ? 12.233  25.124  67.611  1.000 105.342 0 14  VAL DDD CG1 1 ? 14 
ATOM   3588 C CG2 . VAL D 1 12  ? 10.213  25.406  66.158  1.000 106.826 0 14  VAL DDD CG2 1 ? 14 
ATOM   3589 N N   . GLN D 1 13  ? 9.188   28.170  68.390  1.000 109.576 0 15  GLN DDD N   1 ? 14 
ATOM   3590 C CA  . GLN D 1 13  ? 8.184   29.237  68.122  1.000 110.737 0 15  GLN DDD CA  1 ? 14 
ATOM   3591 C C   . GLN D 1 13  ? 8.570   29.965  66.830  1.000 110.393 0 15  GLN DDD C   1 ? 14 
ATOM   3592 O O   . GLN D 1 13  ? 9.751   29.873  66.430  1.000 112.290 0 15  GLN DDD O   1 ? 14 
ATOM   3593 C CB  . GLN D 1 13  ? 8.063   30.202  69.304  1.000 111.707 0 15  GLN DDD CB  1 ? 14 
ATOM   3594 C CG  . GLN D 1 13  ? 9.392   30.748  69.805  1.000 111.629 0 15  GLN DDD CG  1 ? 14 
ATOM   3595 C CD  . GLN D 1 13  ? 9.218   31.622  71.023  1.000 112.732 0 15  GLN DDD CD  1 ? 14 
ATOM   3596 O OE1 . GLN D 1 13  ? 10.053  31.634  71.927  1.000 113.880 0 15  GLN DDD OE1 1 ? 14 
ATOM   3597 N NE2 . GLN D 1 13  ? 8.122   32.363  71.062  1.000 113.255 0 15  GLN DDD NE2 1 ? 14 
ATOM   3598 N N   . ALA D 1 14  ? 7.603   30.655  66.211  1.000 106.561 0 16  ALA DDD N   1 ? 14 
ATOM   3599 C CA  . ALA D 1 14  ? 7.741   31.371  64.919  1.000 104.872 0 16  ALA DDD CA  1 ? 14 
ATOM   3600 C C   . ALA D 1 14  ? 8.996   32.255  64.939  1.000 104.287 0 16  ALA DDD C   1 ? 14 
ATOM   3601 O O   . ALA D 1 14  ? 9.262   32.888  65.983  1.000 105.013 0 16  ALA DDD O   1 ? 14 
ATOM   3602 C CB  . ALA D 1 14  ? 6.495   32.180  64.643  1.000 104.627 0 16  ALA DDD CB  1 ? 14 
ATOM   3603 N N   . GLY D 1 15  ? 9.743   32.276  63.830  1.000 102.462 0 17  GLY DDD N   1 ? 14 
ATOM   3604 C CA  . GLY D 1 15  ? 11.008  33.027  63.689  1.000 105.802 0 17  GLY DDD CA  1 ? 14 
ATOM   3605 C C   . GLY D 1 15  ? 12.206  32.258  64.229  1.000 106.801 0 17  GLY DDD C   1 ? 14 
ATOM   3606 O O   . GLY D 1 15  ? 13.329  32.792  64.145  1.000 109.478 0 17  GLY DDD O   1 ? 14 
ATOM   3607 N N   . GLY D 1 16  ? 11.984  31.048  64.762  1.000 104.583 0 18  GLY DDD N   1 ? 14 
ATOM   3608 C CA  . GLY D 1 16  ? 13.040  30.164  65.295  1.000 102.639 0 18  GLY DDD CA  1 ? 14 
ATOM   3609 C C   . GLY D 1 16  ? 13.743  29.385  64.192  1.000 101.326 0 18  GLY DDD C   1 ? 14 
ATOM   3610 O O   . GLY D 1 16  ? 13.124  29.178  63.126  1.000 101.244 0 18  GLY DDD O   1 ? 14 
ATOM   3611 N N   . SER D 1 17  ? 14.990  28.971  64.443  1.000 99.852  0 19  SER DDD N   1 ? 14 
ATOM   3612 C CA  . SER D 1 17  ? 15.833  28.137  63.543  1.000 97.334  0 19  SER DDD CA  1 ? 14 
ATOM   3613 C C   . SER D 1 17  ? 15.907  26.706  64.089  1.000 93.393  0 19  SER DDD C   1 ? 14 
ATOM   3614 O O   . SER D 1 17  ? 16.322  26.537  65.256  1.000 91.952  0 19  SER DDD O   1 ? 14 
ATOM   3615 C CB  . SER D 1 17  ? 17.214  28.729  63.373  1.000 101.381 0 19  SER DDD CB  1 ? 14 
ATOM   3616 O OG  . SER D 1 17  ? 17.200  29.805  62.446  1.000 105.130 0 19  SER DDD OG  1 ? 14 
ATOM   3617 N N   . LEU D 1 18  ? 15.528  25.722  63.266  1.000 90.281  0 20  LEU DDD N   1 ? 14 
ATOM   3618 C CA  . LEU D 1 18  ? 15.558  24.269  63.583  1.000 86.535  0 20  LEU DDD CA  1 ? 14 
ATOM   3619 C C   . LEU D 1 18  ? 16.302  23.547  62.453  1.000 82.894  0 20  LEU DDD C   1 ? 14 
ATOM   3620 O O   . LEU D 1 18  ? 16.019  23.850  61.281  1.000 83.685  0 20  LEU DDD O   1 ? 14 
ATOM   3621 C CB  . LEU D 1 18  ? 14.113  23.776  63.724  1.000 86.387  0 20  LEU DDD CB  1 ? 14 
ATOM   3622 C CG  . LEU D 1 18  ? 13.893  22.546  64.607  1.000 87.071  0 20  LEU DDD CG  1 ? 14 
ATOM   3623 C CD1 . LEU D 1 18  ? 14.522  22.730  65.981  1.000 88.152  0 20  LEU DDD CD1 1 ? 14 
ATOM   3624 C CD2 . LEU D 1 18  ? 12.406  22.246  64.739  1.000 86.908  0 20  LEU DDD CD2 1 ? 14 
ATOM   3625 N N   . ARG D 1 19  ? 17.244  22.661  62.793  1.000 108.485 0 21  ARG DDD N   1 ? 15 
ATOM   3626 C CA  . ARG D 1 19  ? 18.089  21.921  61.816  1.000 102.312 0 21  ARG DDD CA  1 ? 15 
ATOM   3627 C C   . ARG D 1 19  ? 17.786  20.423  61.917  1.000 95.505  0 21  ARG DDD C   1 ? 15 
ATOM   3628 O O   . ARG D 1 19  ? 18.307  19.771  62.845  1.000 94.859  0 21  ARG DDD O   1 ? 15 
ATOM   3629 C CB  . ARG D 1 19  ? 19.575  22.199  62.066  1.000 104.599 0 21  ARG DDD CB  1 ? 15 
ATOM   3630 C CG  . ARG D 1 19  ? 20.506  21.595  61.023  1.000 102.068 0 21  ARG DDD CG  1 ? 15 
ATOM   3631 C CD  . ARG D 1 19  ? 21.955  21.679  61.458  1.000 106.009 0 21  ARG DDD CD  1 ? 15 
ATOM   3632 N NE  . ARG D 1 19  ? 22.875  21.182  60.443  1.000 105.234 0 21  ARG DDD NE  1 ? 15 
ATOM   3633 C CZ  . ARG D 1 19  ? 23.388  21.894  59.441  1.000 106.682 0 21  ARG DDD CZ  1 ? 15 
ATOM   3634 N NH1 . ARG D 1 19  ? 23.072  23.170  59.282  1.000 111.103 0 21  ARG DDD NH1 1 ? 15 
ATOM   3635 N NH2 . ARG D 1 19  ? 24.226  21.319  58.595  1.000 102.940 0 21  ARG DDD NH2 1 ? 15 
ATOM   3636 N N   . LEU D 1 20  ? 16.979  19.900  60.990  1.000 89.887  0 22  LEU DDD N   1 ? 15 
ATOM   3637 C CA  . LEU D 1 20  ? 16.714  18.443  60.867  1.000 83.801  0 22  LEU DDD CA  1 ? 15 
ATOM   3638 C C   . LEU D 1 20  ? 17.948  17.787  60.246  1.000 78.532  0 22  LEU DDD C   1 ? 15 
ATOM   3639 O O   . LEU D 1 20  ? 18.587  18.424  59.388  1.000 76.900  0 22  LEU DDD O   1 ? 15 
ATOM   3640 C CB  . LEU D 1 20  ? 15.468  18.191  60.012  1.000 82.044  0 22  LEU DDD CB  1 ? 15 
ATOM   3641 C CG  . LEU D 1 20  ? 14.189  18.905  60.451  1.000 85.518  0 22  LEU DDD CG  1 ? 15 
ATOM   3642 C CD1 . LEU D 1 20  ? 12.980  18.341  59.717  1.000 83.196  0 22  LEU DDD CD1 1 ? 15 
ATOM   3643 C CD2 . LEU D 1 20  ? 13.989  18.810  61.958  1.000 88.401  0 22  LEU DDD CD2 1 ? 15 
ATOM   3644 N N   . SER D 1 21  ? 18.281  16.581  60.707  1.000 75.430  0 23  SER DDD N   1 ? 15 
ATOM   3645 C CA  . SER D 1 21  ? 19.352  15.714  60.158  1.000 71.482  0 23  SER DDD CA  1 ? 15 
ATOM   3646 C C   . SER D 1 21  ? 18.782  14.309  59.955  1.000 67.450  0 23  SER DDD C   1 ? 15 
ATOM   3647 O O   . SER D 1 21  ? 17.913  13.902  60.743  1.000 67.975  0 23  SER DDD O   1 ? 15 
ATOM   3648 C CB  . SER D 1 21  ? 20.557  15.695  61.059  1.000 73.014  0 23  SER DDD CB  1 ? 15 
ATOM   3649 O OG  . SER D 1 21  ? 20.287  14.949  62.237  1.000 74.670  0 23  SER DDD OG  1 ? 15 
ATOM   3650 N N   . CYS D 1 22  ? 19.240  13.612  58.919  1.000 63.810  0 24  CYS DDD N   1 ? 15 
ATOM   3651 C CA  . CYS D 1 22  ? 18.843  12.219  58.605  1.000 61.674  0 24  CYS DDD CA  1 ? 15 
ATOM   3652 C C   . CYS D 1 22  ? 20.099  11.416  58.247  1.000 58.342  0 24  CYS DDD C   1 ? 15 
ATOM   3653 O O   . CYS D 1 22  ? 20.698  11.699  57.199  1.000 56.290  0 24  CYS DDD O   1 ? 15 
ATOM   3654 C CB  . CYS D 1 22  ? 17.798  12.176  57.494  1.000 62.388  0 24  CYS DDD CB  1 ? 15 
ATOM   3655 S SG  . CYS D 1 22  ? 17.577  10.502  56.839  1.000 60.255  0 24  CYS DDD SG  1 ? 15 
ATOM   3656 N N   . ALA D 1 23  ? 20.484  10.478  59.117  1.000 57.870  0 25  ALA DDD N   1 ? 15 
ATOM   3657 C CA  . ALA D 1 23  ? 21.614  9.539   58.935  1.000 56.196  0 25  ALA DDD CA  1 ? 15 
ATOM   3658 C C   . ALA D 1 23  ? 21.095  8.259   58.274  1.000 53.089  0 25  ALA DDD C   1 ? 15 
ATOM   3659 O O   . ALA D 1 23  ? 20.114  7.687   58.777  1.000 55.532  0 25  ALA DDD O   1 ? 15 
ATOM   3660 C CB  . ALA D 1 23  ? 22.271  9.252   60.266  1.000 57.946  0 25  ALA DDD CB  1 ? 15 
ATOM   3661 N N   . ALA D 1 24  ? 21.746  7.833   57.191  1.000 51.618  0 26  ALA DDD N   1 ? 15 
ATOM   3662 C CA  . ALA D 1 24  ? 21.359  6.674   56.356  1.000 50.034  0 26  ALA DDD CA  1 ? 15 
ATOM   3663 C C   . ALA D 1 24  ? 22.370  5.544   56.533  1.000 48.383  0 26  ALA DDD C   1 ? 15 
ATOM   3664 O O   . ALA D 1 24  ? 23.568  5.828   56.516  1.000 51.106  0 26  ALA DDD O   1 ? 15 
ATOM   3665 C CB  . ALA D 1 24  ? 21.281  7.096   54.913  1.000 50.098  0 26  ALA DDD CB  1 ? 15 
ATOM   3666 N N   . SER D 1 25  ? 21.895  4.312   56.690  1.000 47.573  0 27  SER DDD N   1 ? 15 
ATOM   3667 C CA  . SER D 1 25  ? 22.726  3.084   56.686  1.000 47.609  0 27  SER DDD CA  1 ? 15 
ATOM   3668 C C   . SER D 1 25  ? 22.206  2.129   55.612  1.000 46.149  0 27  SER DDD C   1 ? 15 
ATOM   3669 O O   . SER D 1 25  ? 21.035  1.721   55.698  1.000 45.525  0 27  SER DDD O   1 ? 15 
ATOM   3670 C CB  . SER D 1 25  ? 22.748  2.425   58.038  1.000 51.163  0 27  SER DDD CB  1 ? 15 
ATOM   3671 O OG  . SER D 1 25  ? 23.627  1.309   58.027  1.000 53.090  0 27  SER DDD OG  1 ? 15 
ATOM   3672 N N   . GLY D 1 26  ? 23.040  1.823   54.616  1.000 45.830  0 28  GLY DDD N   1 ? 15 
ATOM   3673 C CA  . GLY D 1 26  ? 22.831  0.702   53.683  1.000 45.660  0 28  GLY DDD CA  1 ? 15 
ATOM   3674 C C   . GLY D 1 26  ? 22.117  1.081   52.400  1.000 45.040  0 28  GLY DDD C   1 ? 15 
ATOM   3675 O O   . GLY D 1 26  ? 21.664  0.160   51.713  1.000 47.883  0 28  GLY DDD O   1 ? 15 
ATOM   3676 N N   . GLY D 1 27  ? 22.018  2.369   52.070  1.000 45.207  0 29  GLY DDD N   1 ? 15 
ATOM   3677 C CA  . GLY D 1 27  ? 21.321  2.838   50.857  1.000 46.039  0 29  GLY DDD CA  1 ? 15 
ATOM   3678 C C   . GLY D 1 27  ? 22.286  3.294   49.777  1.000 45.972  0 29  GLY DDD C   1 ? 15 
ATOM   3679 O O   . GLY D 1 27  ? 21.829  4.000   48.855  1.000 47.449  0 29  GLY DDD O   1 ? 15 
ATOM   3680 N N   . THR D 1 28  ? 23.556  2.876   49.856  1.000 45.887  0 30  THR DDD N   1 ? 15 
ATOM   3681 C CA  . THR D 1 28  ? 24.686  3.431   49.066  1.000 45.904  0 30  THR DDD CA  1 ? 15 
ATOM   3682 C C   . THR D 1 28  ? 24.454  4.939   48.924  1.000 46.960  0 30  THR DDD C   1 ? 15 
ATOM   3683 O O   . THR D 1 28  ? 24.190  5.409   47.797  1.000 49.006  0 30  THR DDD O   1 ? 15 
ATOM   3684 C CB  . THR D 1 28  ? 24.840  2.716   47.717  1.000 46.718  0 30  THR DDD CB  1 ? 15 
ATOM   3685 O OG1 . THR D 1 28  ? 24.816  1.305   47.936  1.000 47.968  0 30  THR DDD OG1 1 ? 15 
ATOM   3686 C CG2 . THR D 1 28  ? 26.123  3.091   47.008  1.000 47.434  0 30  THR DDD CG2 1 ? 15 
ATOM   3687 N N   . PHE D 1 29  ? 24.517  5.656   50.048  1.000 46.412  0 31  PHE DDD N   1 ? 15 
ATOM   3688 C CA  . PHE D 1 29  ? 24.119  7.081   50.178  1.000 47.243  0 31  PHE DDD CA  1 ? 15 
ATOM   3689 C C   . PHE D 1 29  ? 24.712  7.916   49.038  1.000 50.703  0 31  PHE DDD C   1 ? 15 
ATOM   3690 O O   . PHE D 1 29  ? 23.982  8.763   48.489  1.000 53.797  0 31  PHE DDD O   1 ? 15 
ATOM   3691 C CB  . PHE D 1 29  ? 24.556  7.627   51.531  1.000 46.695  0 31  PHE DDD CB  1 ? 15 
ATOM   3692 C CG  . PHE D 1 29  ? 24.012  8.993   51.851  1.000 47.129  0 31  PHE DDD CG  1 ? 15 
ATOM   3693 C CD1 . PHE D 1 29  ? 22.722  9.145   52.337  1.000 46.620  0 31  PHE DDD CD1 1 ? 15 
ATOM   3694 C CD2 . PHE D 1 29  ? 24.790  10.125  51.663  1.000 48.001  0 31  PHE DDD CD2 1 ? 15 
ATOM   3695 C CE1 . PHE D 1 29  ? 22.230  10.402  52.647  1.000 48.028  0 31  PHE DDD CE1 1 ? 15 
ATOM   3696 C CE2 . PHE D 1 29  ? 24.293  11.381  51.964  1.000 49.700  0 31  PHE DDD CE2 1 ? 15 
ATOM   3697 C CZ  . PHE D 1 29  ? 23.013  11.516  52.450  1.000 50.098  0 31  PHE DDD CZ  1 ? 15 
ATOM   3698 N N   . SER D 1 30  ? 25.980  7.670   48.688  1.000 52.533  0 32  SER DDD N   1 ? 15 
ATOM   3699 C CA  . SER D 1 30  ? 26.768  8.440   47.686  1.000 54.584  0 32  SER DDD CA  1 ? 15 
ATOM   3700 C C   . SER D 1 30  ? 26.046  8.533   46.337  1.000 56.422  0 32  SER DDD C   1 ? 15 
ATOM   3701 O O   . SER D 1 30  ? 26.217  9.565   45.670  1.000 60.439  0 32  SER DDD O   1 ? 15 
ATOM   3702 C CB  . SER D 1 30  ? 28.139  7.860   47.503  1.000 55.298  0 32  SER DDD CB  1 ? 15 
ATOM   3703 O OG  . SER D 1 30  ? 29.067  8.538   48.325  1.000 60.781  0 32  SER DDD OG  1 ? 15 
ATOM   3704 N N   . THR D 1 31  ? 25.305  7.492   45.935  1.000 55.358  0 33  THR DDD N   1 ? 15 
ATOM   3705 C CA  . THR D 1 31  ? 24.619  7.407   44.616  1.000 53.502  0 33  THR DDD CA  1 ? 15 
ATOM   3706 C C   . THR D 1 31  ? 23.100  7.545   44.792  1.000 52.749  0 33  THR DDD C   1 ? 15 
ATOM   3707 O O   . THR D 1 31  ? 22.375  7.231   43.831  1.000 54.714  0 33  THR DDD O   1 ? 15 
ATOM   3708 C CB  . THR D 1 31  ? 24.986  6.102   43.900  1.000 53.158  0 33  THR DDD CB  1 ? 15 
ATOM   3709 O OG1 . THR D 1 31  ? 24.472  5.009   44.659  1.000 52.118  0 33  THR DDD OG1 1 ? 15 
ATOM   3710 C CG2 . THR D 1 31  ? 26.477  5.931   43.705  1.000 53.411  0 33  THR DDD CG2 1 ? 15 
ATOM   3711 N N   . ALA D 1 32  ? 22.636  8.017   45.955  1.000 50.543  0 34  ALA DDD N   1 ? 15 
ATOM   3712 C CA  . ALA D 1 32  ? 21.201  8.180   46.289  1.000 49.984  0 34  ALA DDD CA  1 ? 15 
ATOM   3713 C C   . ALA D 1 32  ? 20.821  9.664   46.308  1.000 51.086  0 34  ALA DDD C   1 ? 15 
ATOM   3714 O O   . ALA D 1 32  ? 21.509  10.450  46.981  1.000 51.905  0 34  ALA DDD O   1 ? 15 
ATOM   3715 C CB  . ALA D 1 32  ? 20.906  7.533   47.617  1.000 48.939  0 34  ALA DDD CB  1 ? 15 
ATOM   3716 N N   . ALA D 1 33  ? 19.759  10.035  45.590  1.000 53.197  0 35  ALA DDD N   1 ? 15 
ATOM   3717 C CA  . ALA D 1 33  ? 19.065  11.333  45.746  1.000 54.962  0 35  ALA DDD CA  1 ? 15 
ATOM   3718 C C   . ALA D 1 33  ? 18.272  11.282  47.056  1.000 54.240  0 35  ALA DDD C   1 ? 15 
ATOM   3719 O O   . ALA D 1 33  ? 17.629  10.251  47.321  1.000 51.941  0 35  ALA DDD O   1 ? 15 
ATOM   3720 C CB  . ALA D 1 33  ? 18.176  11.616  44.557  1.000 56.591  0 35  ALA DDD CB  1 ? 15 
ATOM   3721 N N   . MET D 1 34  ? 18.349  12.344  47.858  1.000 56.125  0 36  MET DDD N   1 ? 15 
ATOM   3722 C CA  . MET D 1 34  ? 17.751  12.414  49.214  1.000 55.673  0 36  MET DDD CA  1 ? 15 
ATOM   3723 C C   . MET D 1 34  ? 16.703  13.526  49.247  1.000 56.075  0 36  MET DDD C   1 ? 15 
ATOM   3724 O O   . MET D 1 34  ? 16.907  14.553  48.578  1.000 55.581  0 36  MET DDD O   1 ? 15 
ATOM   3725 C CB  . MET D 1 34  ? 18.840  12.676  50.258  1.000 58.209  0 36  MET DDD CB  1 ? 15 
ATOM   3726 C CG  . MET D 1 34  ? 19.776  11.495  50.434  1.000 57.499  0 36  MET DDD CG  1 ? 15 
ATOM   3727 S SD  . MET D 1 34  ? 18.913  10.139  51.280  1.000 57.167  0 36  MET DDD SD  1 ? 15 
ATOM   3728 C CE  . MET D 1 34  ? 19.715  8.717   50.542  1.000 57.915  0 36  MET DDD CE  1 ? 15 
ATOM   3729 N N   . GLY D 1 35  ? 15.617  13.303  49.989  1.000 56.397  0 37  GLY DDD N   1 ? 15 
ATOM   3730 C CA  . GLY D 1 35  ? 14.461  14.215  50.048  1.000 58.694  0 37  GLY DDD CA  1 ? 15 
ATOM   3731 C C   . GLY D 1 35  ? 13.926  14.370  51.460  1.000 59.623  0 37  GLY DDD C   1 ? 15 
ATOM   3732 O O   . GLY D 1 35  ? 14.076  13.430  52.270  1.000 58.656  0 37  GLY DDD O   1 ? 15 
ATOM   3733 N N   . TRP D 1 36  ? 13.328  15.530  51.740  1.000 61.802  0 38  TRP DDD N   1 ? 15 
ATOM   3734 C CA  . TRP D 1 36  ? 12.543  15.807  52.969  1.000 64.770  0 38  TRP DDD CA  1 ? 15 
ATOM   3735 C C   . TRP D 1 36  ? 11.076  15.986  52.577  1.000 66.562  0 38  TRP DDD C   1 ? 15 
ATOM   3736 O O   . TRP D 1 36  ? 10.784  16.875  51.755  1.000 69.325  0 38  TRP DDD O   1 ? 15 
ATOM   3737 C CB  . TRP D 1 36  ? 13.100  17.030  53.706  1.000 68.229  0 38  TRP DDD CB  1 ? 15 
ATOM   3738 C CG  . TRP D 1 36  ? 14.373  16.735  54.436  1.000 67.051  0 38  TRP DDD CG  1 ? 15 
ATOM   3739 C CD1 . TRP D 1 36  ? 15.648  16.987  54.018  1.000 66.547  0 38  TRP DDD CD1 1 ? 15 
ATOM   3740 C CD2 . TRP D 1 36  ? 14.491  16.093  55.716  1.000 66.839  0 38  TRP DDD CD2 1 ? 15 
ATOM   3741 N NE1 . TRP D 1 36  ? 16.549  16.560  54.956  1.000 66.493  0 38  TRP DDD NE1 1 ? 15 
ATOM   3742 C CE2 . TRP D 1 36  ? 15.869  16.003  56.007  1.000 66.829  0 38  TRP DDD CE2 1 ? 15 
ATOM   3743 C CE3 . TRP D 1 36  ? 13.568  15.592  56.641  1.000 67.703  0 38  TRP DDD CE3 1 ? 15 
ATOM   3744 C CZ2 . TRP D 1 36  ? 16.341  15.432  57.189  1.000 66.744  0 38  TRP DDD CZ2 1 ? 15 
ATOM   3745 C CZ3 . TRP D 1 36  ? 14.036  15.025  57.806  1.000 67.549  0 38  TRP DDD CZ3 1 ? 15 
ATOM   3746 C CH2 . TRP D 1 36  ? 15.404  14.947  58.073  1.000 67.566  0 38  TRP DDD CH2 1 ? 15 
ATOM   3747 N N   . PHE D 1 37  ? 10.209  15.123  53.105  1.000 66.560  0 39  PHE DDD N   1 ? 15 
ATOM   3748 C CA  . PHE D 1 37  ? 8.733   15.202  52.971  1.000 68.332  0 39  PHE DDD CA  1 ? 15 
ATOM   3749 C C   . PHE D 1 37  ? 8.151   15.628  54.320  1.000 70.381  0 39  PHE DDD C   1 ? 15 
ATOM   3750 O O   . PHE D 1 37  ? 8.767   15.320  55.354  1.000 70.013  0 39  PHE DDD O   1 ? 15 
ATOM   3751 C CB  . PHE D 1 37  ? 8.165   13.857  52.516  1.000 67.080  0 39  PHE DDD CB  1 ? 15 
ATOM   3752 C CG  . PHE D 1 37  ? 8.413   13.520  51.067  1.000 66.308  0 39  PHE DDD CG  1 ? 15 
ATOM   3753 C CD1 . PHE D 1 37  ? 9.669   13.125  50.631  1.000 63.874  0 39  PHE DDD CD1 1 ? 15 
ATOM   3754 C CD2 . PHE D 1 37  ? 7.384   13.577  50.139  1.000 67.478  0 39  PHE DDD CD2 1 ? 15 
ATOM   3755 C CE1 . PHE D 1 37  ? 9.891   12.806  49.300  1.000 63.237  0 39  PHE DDD CE1 1 ? 15 
ATOM   3756 C CE2 . PHE D 1 37  ? 7.607   13.255  48.809  1.000 66.748  0 39  PHE DDD CE2 1 ? 15 
ATOM   3757 C CZ  . PHE D 1 37  ? 8.860   12.873  48.391  1.000 65.346  0 39  PHE DDD CZ  1 ? 15 
ATOM   3758 N N   . ARG D 1 38  ? 7.018   16.331  54.305  1.000 74.066  0 40  ARG DDD N   1 ? 15 
ATOM   3759 C CA  . ARG D 1 38  ? 6.277   16.716  55.535  1.000 77.441  0 40  ARG DDD CA  1 ? 15 
ATOM   3760 C C   . ARG D 1 38  ? 4.798   16.372  55.348  1.000 79.392  0 40  ARG DDD C   1 ? 15 
ATOM   3761 O O   . ARG D 1 38  ? 4.326   16.371  54.189  1.000 78.403  0 40  ARG DDD O   1 ? 15 
ATOM   3762 C CB  . ARG D 1 38  ? 6.486   18.197  55.870  1.000 80.192  0 40  ARG DDD CB  1 ? 15 
ATOM   3763 C CG  . ARG D 1 38  ? 5.678   19.166  55.020  1.000 82.277  0 40  ARG DDD CG  1 ? 15 
ATOM   3764 C CD  . ARG D 1 38  ? 5.912   20.602  55.445  1.000 85.746  0 40  ARG DDD CD  1 ? 15 
ATOM   3765 N NE  . ARG D 1 38  ? 5.377   21.550  54.479  1.000 88.675  0 40  ARG DDD NE  1 ? 15 
ATOM   3766 C CZ  . ARG D 1 38  ? 5.498   22.872  54.565  1.000 92.566  0 40  ARG DDD CZ  1 ? 15 
ATOM   3767 N NH1 . ARG D 1 38  ? 6.148   23.421  55.578  1.000 94.287  0 40  ARG DDD NH1 1 ? 15 
ATOM   3768 N NH2 . ARG D 1 38  ? 4.971   23.643  53.628  1.000 94.818  0 40  ARG DDD NH2 1 ? 15 
ATOM   3769 N N   . GLN D 1 39  ? 4.109   16.085  56.454  1.000 81.567  0 41  GLN DDD N   1 ? 15 
ATOM   3770 C CA  . GLN D 1 39  ? 2.656   15.782  56.487  1.000 84.417  0 41  GLN DDD CA  1 ? 15 
ATOM   3771 C C   . GLN D 1 39  ? 2.036   16.464  57.707  1.000 89.061  0 41  GLN DDD C   1 ? 15 
ATOM   3772 O O   . GLN D 1 39  ? 2.257   15.977  58.835  1.000 88.910  0 41  GLN DDD O   1 ? 15 
ATOM   3773 C CB  . GLN D 1 39  ? 2.438   14.270  56.519  1.000 82.925  0 41  GLN DDD CB  1 ? 15 
ATOM   3774 C CG  . GLN D 1 39  ? 0.986   13.863  56.323  1.000 85.272  0 41  GLN DDD CG  1 ? 15 
ATOM   3775 C CD  . GLN D 1 39  ? 0.839   12.365  56.204  1.000 84.188  0 41  GLN DDD CD  1 ? 15 
ATOM   3776 O OE1 . GLN D 1 39  ? 1.708   11.597  56.612  1.000 81.268  0 41  GLN DDD OE1 1 ? 15 
ATOM   3777 N NE2 . GLN D 1 39  ? -0.266  11.935  55.619  1.000 86.832  0 41  GLN DDD NE2 1 ? 15 
ATOM   3778 N N   . ALA D 1 40  ? 1.316   17.565  57.487  1.000 93.891  0 42  ALA DDD N   1 ? 15 
ATOM   3779 C CA  . ALA D 1 40  ? 0.449   18.205  58.504  1.000 98.516  0 42  ALA DDD CA  1 ? 15 
ATOM   3780 C C   . ALA D 1 40  ? -0.687  17.238  58.824  1.000 100.810 0 42  ALA DDD C   1 ? 15 
ATOM   3781 O O   . ALA D 1 40  ? -1.102  16.462  57.963  1.000 98.162  0 42  ALA DDD O   1 ? 15 
ATOM   3782 C CB  . ALA D 1 40  ? -0.074  19.532  58.013  1.000 101.009 0 42  ALA DDD CB  1 ? 15 
ATOM   3783 N N   . PRO D 1 41  ? -1.213  17.241  60.071  1.000 106.166 0 43  PRO DDD N   1 ? 15 
ATOM   3784 C CA  . PRO D 1 41  ? -2.370  16.414  60.412  1.000 107.751 0 43  PRO DDD CA  1 ? 15 
ATOM   3785 C C   . PRO D 1 41  ? -3.642  17.000  59.780  1.000 110.692 0 43  PRO DDD C   1 ? 15 
ATOM   3786 O O   . PRO D 1 41  ? -4.120  18.012  60.262  1.000 114.729 0 43  PRO DDD O   1 ? 15 
ATOM   3787 C CB  . PRO D 1 41  ? -2.390  16.447  61.947  1.000 111.237 0 43  PRO DDD CB  1 ? 15 
ATOM   3788 C CG  . PRO D 1 41  ? -1.735  17.772  62.299  1.000 112.847 0 43  PRO DDD CG  1 ? 15 
ATOM   3789 C CD  . PRO D 1 41  ? -0.705  18.017  61.214  1.000 108.837 0 43  PRO DDD CD  1 ? 15 
ATOM   3790 N N   . GLY D 1 42  ? -4.115  16.386  58.690  1.000 109.317 0 44  GLY DDD N   1 ? 15 
ATOM   3791 C CA  . GLY D 1 42  ? -5.288  16.844  57.914  1.000 112.258 0 44  GLY DDD CA  1 ? 15 
ATOM   3792 C C   . GLY D 1 42  ? -4.992  16.985  56.427  1.000 109.960 0 44  GLY DDD C   1 ? 15 
ATOM   3793 O O   . GLY D 1 42  ? -5.962  17.109  55.649  1.000 112.396 0 44  GLY DDD O   1 ? 15 
ATOM   3794 N N   . GLU D 1 43  ? -3.708  16.949  56.045  1.000 121.599 0 45  GLU DDD N   1 ? 16 
ATOM   3795 C CA  . GLU D 1 43  ? -3.235  16.998  54.635  1.000 118.143 0 45  GLU DDD CA  1 ? 16 
ATOM   3796 C C   . GLU D 1 43  ? -2.490  15.699  54.305  1.000 113.721 0 45  GLU DDD C   1 ? 16 
ATOM   3797 O O   . GLU D 1 43  ? -2.415  14.826  55.192  1.000 113.118 0 45  GLU DDD O   1 ? 16 
ATOM   3798 C CB  . GLU D 1 43  ? -2.348  18.224  54.418  1.000 115.777 0 45  GLU DDD CB  1 ? 16 
ATOM   3799 C CG  . GLU D 1 43  ? -3.071  19.541  54.648  1.000 120.221 0 45  GLU DDD CG  1 ? 16 
ATOM   3800 C CD  . GLU D 1 43  ? -2.875  20.160  56.022  1.000 121.169 0 45  GLU DDD CD  1 ? 16 
ATOM   3801 O OE1 . GLU D 1 43  ? -3.078  19.448  57.024  1.000 121.958 0 45  GLU DDD OE1 1 ? 16 
ATOM   3802 O OE2 . GLU D 1 43  ? -2.505  21.350  56.087  1.000 120.983 0 45  GLU DDD OE2 1 ? 16 
ATOM   3803 N N   . GLU D 1 44  ? -1.982  15.579  53.076  1.000 111.362 0 46  GLU DDD N   1 ? 16 
ATOM   3804 C CA  . GLU D 1 44  ? -1.239  14.383  52.587  1.000 107.892 0 46  GLU DDD CA  1 ? 16 
ATOM   3805 C C   . GLU D 1 44  ? 0.229   14.760  52.359  1.000 101.855 0 46  GLU DDD C   1 ? 16 
ATOM   3806 O O   . GLU D 1 44  ? 0.512   15.955  52.155  1.000 101.196 0 46  GLU DDD O   1 ? 16 
ATOM   3807 C CB  . GLU D 1 44  ? -1.879  13.799  51.322  1.000 110.026 0 46  GLU DDD CB  1 ? 16 
ATOM   3808 C CG  . GLU D 1 44  ? -2.179  14.817  50.230  1.000 112.012 0 46  GLU DDD CG  1 ? 16 
ATOM   3809 C CD  . GLU D 1 44  ? -2.757  14.216  48.959  1.000 114.254 0 46  GLU DDD CD  1 ? 16 
ATOM   3810 O OE1 . GLU D 1 44  ? -2.344  13.094  48.608  1.000 112.266 0 46  GLU DDD OE1 1 ? 16 
ATOM   3811 O OE2 . GLU D 1 44  ? -3.625  14.866  48.326  1.000 116.683 0 46  GLU DDD OE2 1 ? 16 
ATOM   3812 N N   . ARG D 1 45  ? 1.111   13.758  52.402  1.000 97.884  0 47  ARG DDD N   1 ? 16 
ATOM   3813 C CA  . ARG D 1 45  ? 2.588   13.901  52.295  1.000 93.784  0 47  ARG DDD CA  1 ? 16 
ATOM   3814 C C   . ARG D 1 45  ? 2.930   14.755  51.070  1.000 92.267  0 47  ARG DDD C   1 ? 16 
ATOM   3815 O O   . ARG D 1 45  ? 2.455   14.414  49.971  1.000 93.812  0 47  ARG DDD O   1 ? 16 
ATOM   3816 C CB  . ARG D 1 45  ? 3.239   12.518  52.191  1.000 91.624  0 47  ARG DDD CB  1 ? 16 
ATOM   3817 C CG  . ARG D 1 45  ? 4.584   12.410  52.890  1.000 88.892  0 47  ARG DDD CG  1 ? 16 
ATOM   3818 C CD  . ARG D 1 45  ? 5.081   10.979  52.972  1.000 87.994  0 47  ARG DDD CD  1 ? 16 
ATOM   3819 N NE  . ARG D 1 45  ? 4.662   10.273  54.178  1.000 90.413  0 47  ARG DDD NE  1 ? 16 
ATOM   3820 C CZ  . ARG D 1 45  ? 5.096   9.064   54.535  1.000 89.963  0 47  ARG DDD CZ  1 ? 16 
ATOM   3821 N NH1 . ARG D 1 45  ? 5.959   8.409   53.774  1.000 86.756  0 47  ARG DDD NH1 1 ? 16 
ATOM   3822 N NH2 . ARG D 1 45  ? 4.659   8.500   55.650  1.000 91.994  0 47  ARG DDD NH2 1 ? 16 
ATOM   3823 N N   . GLU D 1 46  ? 3.701   15.829  51.265  1.000 89.294  0 48  GLU DDD N   1 ? 16 
ATOM   3824 C CA  . GLU D 1 46  ? 4.265   16.675  50.179  1.000 86.911  0 48  GLU DDD CA  1 ? 16 
ATOM   3825 C C   . GLU D 1 46  ? 5.784   16.750  50.353  1.000 82.459  0 48  GLU DDD C   1 ? 16 
ATOM   3826 O O   . GLU D 1 46  ? 6.244   16.839  51.505  1.000 81.765  0 48  GLU DDD O   1 ? 16 
ATOM   3827 C CB  . GLU D 1 46  ? 3.643   18.076  50.177  1.000 90.414  0 48  GLU DDD CB  1 ? 16 
ATOM   3828 C CG  . GLU D 1 46  ? 4.098   18.979  51.314  1.000 91.078  0 48  GLU DDD CG  1 ? 16 
ATOM   3829 C CD  . GLU D 1 46  ? 3.804   20.459  51.117  1.000 95.036  0 48  GLU DDD CD  1 ? 16 
ATOM   3830 O OE1 . GLU D 1 46  ? 3.042   20.795  50.187  1.000 99.009  0 48  GLU DDD OE1 1 ? 16 
ATOM   3831 O OE2 . GLU D 1 46  ? 4.344   21.276  51.893  1.000 95.600  0 48  GLU DDD OE2 1 ? 16 
ATOM   3832 N N   . CYS D 1 47  ? 6.527   16.695  49.248  1.000 79.612  0 49  CYS DDD N   1 ? 16 
ATOM   3833 C CA  . CYS D 1 47  ? 7.991   16.938  49.211  1.000 75.937  0 49  CYS DDD CA  1 ? 16 
ATOM   3834 C C   . CYS D 1 47  ? 8.238   18.436  49.423  1.000 76.285  0 49  CYS DDD C   1 ? 16 
ATOM   3835 O O   . CYS D 1 47  ? 7.554   19.233  48.757  1.000 78.995  0 49  CYS DDD O   1 ? 16 
ATOM   3836 C CB  . CYS D 1 47  ? 8.590   16.481  47.887  1.000 74.515  0 49  CYS DDD CB  1 ? 16 
ATOM   3837 S SG  . CYS D 1 47  ? 10.400  16.429  47.905  1.000 73.063  0 49  CYS DDD SG  1 ? 16 
ATOM   3838 N N   . VAL D 1 48  ? 9.157   18.800  50.324  1.000 74.579  0 50  VAL DDD N   1 ? 16 
ATOM   3839 C CA  . VAL D 1 48  ? 9.489   20.224  50.644  1.000 75.815  0 50  VAL DDD CA  1 ? 16 
ATOM   3840 C C   . VAL D 1 48  ? 10.875  20.581  50.092  1.000 72.787  0 50  VAL DDD C   1 ? 16 
ATOM   3841 O O   . VAL D 1 48  ? 11.078  21.767  49.764  1.000 73.450  0 50  VAL DDD O   1 ? 16 
ATOM   3842 C CB  . VAL D 1 48  ? 9.387   20.517  52.154  1.000 77.906  0 50  VAL DDD CB  1 ? 16 
ATOM   3843 C CG1 . VAL D 1 48  ? 7.949   20.398  52.631  1.000 81.325  0 50  VAL DDD CG1 1 ? 16 
ATOM   3844 C CG2 . VAL D 1 48  ? 10.309  19.644  52.996  1.000 75.680  0 50  VAL DDD CG2 1 ? 16 
ATOM   3845 N N   . ALA D 1 49  ? 11.789  19.610  50.003  1.000 69.269  0 51  ALA DDD N   1 ? 16 
ATOM   3846 C CA  . ALA D 1 49  ? 13.143  19.791  49.428  1.000 67.211  0 51  ALA DDD CA  1 ? 16 
ATOM   3847 C C   . ALA D 1 49  ? 13.732  18.440  49.013  1.000 63.913  0 51  ALA DDD C   1 ? 16 
ATOM   3848 O O   . ALA D 1 49  ? 13.424  17.423  49.668  1.000 64.320  0 51  ALA DDD O   1 ? 16 
ATOM   3849 C CB  . ALA D 1 49  ? 14.036  20.490  50.421  1.000 67.863  0 51  ALA DDD CB  1 ? 16 
ATOM   3850 N N   . SER D 1 50  ? 14.546  18.441  47.956  1.000 62.409  0 52  SER DDD N   1 ? 16 
ATOM   3851 C CA  . SER D 1 50  ? 15.322  17.267  47.481  1.000 60.257  0 52  SER DDD CA  1 ? 16 
ATOM   3852 C C   . SER D 1 50  ? 16.686  17.732  46.967  1.000 59.751  0 52  SER DDD C   1 ? 16 
ATOM   3853 O O   . SER D 1 50  ? 16.819  18.922  46.601  1.000 59.914  0 52  SER DDD O   1 ? 16 
ATOM   3854 C CB  . SER D 1 50  ? 14.569  16.486  46.432  1.000 60.056  0 52  SER DDD CB  1 ? 16 
ATOM   3855 O OG  . SER D 1 50  ? 14.413  17.232  45.236  1.000 61.953  0 52  SER DDD OG  1 ? 16 
ATOM   3856 N N   . ILE D 1 51  ? 17.653  16.815  46.948  1.000 58.608  0 53  ILE DDD N   1 ? 16 
ATOM   3857 C CA  . ILE D 1 51  ? 19.075  17.099  46.599  1.000 59.733  0 53  ILE DDD CA  1 ? 16 
ATOM   3858 C C   . ILE D 1 51  ? 19.639  15.910  45.812  1.000 59.053  0 53  ILE DDD C   1 ? 16 
ATOM   3859 O O   . ILE D 1 51  ? 19.341  14.750  46.177  1.000 57.829  0 53  ILE DDD O   1 ? 16 
ATOM   3860 C CB  . ILE D 1 51  ? 19.888  17.412  47.873  1.000 59.836  0 53  ILE DDD CB  1 ? 16 
ATOM   3861 C CG1 . ILE D 1 51  ? 21.297  17.904  47.538  1.000 60.810  0 53  ILE DDD CG1 1 ? 16 
ATOM   3862 C CG2 . ILE D 1 51  ? 19.915  16.221  48.825  1.000 58.497  0 53  ILE DDD CG2 1 ? 16 
ATOM   3863 C CD1 . ILE D 1 51  ? 21.993  18.610  48.690  1.000 63.053  0 53  ILE DDD CD1 1 ? 16 
ATOM   3864 N N   . GLY D 1 52  ? 20.405  16.200  44.758  1.000 61.139  0 54  GLY DDD N   1 ? 16 
ATOM   3865 C CA  . GLY D 1 52  ? 21.091  15.194  43.925  1.000 60.777  0 54  GLY DDD CA  1 ? 16 
ATOM   3866 C C   . GLY D 1 52  ? 22.251  14.555  44.670  1.000 59.679  0 54  GLY DDD C   1 ? 16 
ATOM   3867 O O   . GLY D 1 52  ? 22.706  15.130  45.682  1.000 58.298  0 54  GLY DDD O   1 ? 16 
ATOM   3868 N N   . TRP D 1 53  ? 22.709  13.405  44.176  1.000 59.424  0 55  TRP DDD N   1 ? 16 
ATOM   3869 C CA  . TRP D 1 53  ? 23.780  12.562  44.769  1.000 59.476  0 55  TRP DDD CA  1 ? 16 
ATOM   3870 C C   . TRP D 1 53  ? 25.040  13.389  45.073  1.000 61.609  0 55  TRP DDD C   1 ? 16 
ATOM   3871 O O   . TRP D 1 53  ? 25.642  13.141  46.134  1.000 61.471  0 55  TRP DDD O   1 ? 16 
ATOM   3872 C CB  . TRP D 1 53  ? 24.081  11.375  43.845  1.000 59.512  0 55  TRP DDD CB  1 ? 16 
ATOM   3873 C CG  . TRP D 1 53  ? 24.680  11.738  42.520  1.000 61.535  0 55  TRP DDD CG  1 ? 16 
ATOM   3874 C CD1 . TRP D 1 53  ? 24.109  12.457  41.506  1.000 63.262  0 55  TRP DDD CD1 1 ? 16 
ATOM   3875 C CD2 . TRP D 1 53  ? 25.981  11.353  42.048  1.000 63.580  0 55  TRP DDD CD2 1 ? 16 
ATOM   3876 N NE1 . TRP D 1 53  ? 24.970  12.555  40.445  1.000 64.982  0 55  TRP DDD NE1 1 ? 16 
ATOM   3877 C CE2 . TRP D 1 53  ? 26.125  11.884  40.747  1.000 65.032  0 55  TRP DDD CE2 1 ? 16 
ATOM   3878 C CE3 . TRP D 1 53  ? 27.029  10.607  42.597  1.000 62.517  0 55  TRP DDD CE3 1 ? 16 
ATOM   3879 C CZ2 . TRP D 1 53  ? 27.281  11.693  39.994  1.000 67.196  0 55  TRP DDD CZ2 1 ? 16 
ATOM   3880 C CZ3 . TRP D 1 53  ? 28.172  10.421  41.852  1.000 66.455  0 55  TRP DDD CZ3 1 ? 16 
ATOM   3881 C CH2 . TRP D 1 53  ? 28.294  10.960  40.570  1.000 67.828  0 55  TRP DDD CH2 1 ? 16 
ATOM   3882 N N   . ARG D 1 54  ? 25.416  14.320  44.185  1.000 62.327  0 56  ARG DDD N   1 ? 16 
ATOM   3883 C CA  . ARG D 1 54  ? 26.630  15.176  44.301  1.000 63.323  0 56  ARG DDD CA  1 ? 16 
ATOM   3884 C C   . ARG D 1 54  ? 26.363  16.385  45.203  1.000 63.911  0 56  ARG DDD C   1 ? 16 
ATOM   3885 O O   . ARG D 1 54  ? 27.342  17.071  45.549  1.000 68.042  0 56  ARG DDD O   1 ? 16 
ATOM   3886 C CB  . ARG D 1 54  ? 27.060  15.728  42.939  1.000 66.790  0 56  ARG DDD CB  1 ? 16 
ATOM   3887 C CG  . ARG D 1 54  ? 27.910  14.790  42.098  1.000 68.049  0 56  ARG DDD CG  1 ? 16 
ATOM   3888 C CD  . ARG D 1 54  ? 27.977  15.350  40.692  1.000 71.032  0 56  ARG DDD CD  1 ? 16 
ATOM   3889 N NE  . ARG D 1 54  ? 28.962  14.699  39.841  1.000 72.988  0 56  ARG DDD NE  1 ? 16 
ATOM   3890 C CZ  . ARG D 1 54  ? 29.069  14.884  38.527  1.000 74.844  0 56  ARG DDD CZ  1 ? 16 
ATOM   3891 N NH1 . ARG D 1 54  ? 28.248  15.711  37.900  1.000 75.594  0 56  ARG DDD NH1 1 ? 16 
ATOM   3892 N NH2 . ARG D 1 54  ? 29.999  14.242  37.840  1.000 77.051  0 56  ARG DDD NH2 1 ? 16 
ATOM   3893 N N   . GLY D 1 55  ? 25.099  16.672  45.522  1.000 62.992  0 57  GLY DDD N   1 ? 16 
ATOM   3894 C CA  . GLY D 1 55  ? 24.694  17.852  46.313  1.000 63.298  0 57  GLY DDD CA  1 ? 16 
ATOM   3895 C C   . GLY D 1 55  ? 24.777  19.142  45.506  1.000 64.440  0 57  GLY DDD C   1 ? 16 
ATOM   3896 O O   . GLY D 1 55  ? 24.819  20.216  46.132  1.000 65.106  0 57  GLY DDD O   1 ? 16 
ATOM   3897 N N   . VAL D 1 56  ? 24.772  19.045  44.171  1.000 64.945  0 58  VAL DDD N   1 ? 16 
ATOM   3898 C CA  . VAL D 1 56  ? 24.902  20.198  43.231  1.000 68.226  0 58  VAL DDD CA  1 ? 16 
ATOM   3899 C C   . VAL D 1 56  ? 23.507  20.750  42.927  1.000 68.869  0 58  VAL DDD C   1 ? 16 
ATOM   3900 O O   . VAL D 1 56  ? 23.319  21.975  43.044  1.000 71.836  0 58  VAL DDD O   1 ? 16 
ATOM   3901 C CB  . VAL D 1 56  ? 25.638  19.786  41.941  1.000 69.791  0 58  VAL DDD CB  1 ? 16 
ATOM   3902 C CG1 . VAL D 1 56  ? 25.522  20.838  40.844  1.000 72.235  0 58  VAL DDD CG1 1 ? 16 
ATOM   3903 C CG2 . VAL D 1 56  ? 27.098  19.465  42.219  1.000 70.597  0 58  VAL DDD CG2 1 ? 16 
ATOM   3904 N N   . ARG D 1 57  ? 22.576  19.878  42.532  1.000 67.533  0 59  ARG DDD N   1 ? 16 
ATOM   3905 C CA  . ARG D 1 57  ? 21.173  20.251  42.205  1.000 67.146  0 59  ARG DDD CA  1 ? 16 
ATOM   3906 C C   . ARG D 1 57  ? 20.324  20.136  43.472  1.000 65.282  0 59  ARG DDD C   1 ? 16 
ATOM   3907 O O   . ARG D 1 57  ? 20.463  19.123  44.186  1.000 63.696  0 59  ARG DDD O   1 ? 16 
ATOM   3908 C CB  . ARG D 1 57  ? 20.610  19.349  41.104  1.000 65.766  0 59  ARG DDD CB  1 ? 16 
ATOM   3909 C CG  . ARG D 1 57  ? 21.407  19.380  39.809  1.000 66.590  0 59  ARG DDD CG  1 ? 16 
ATOM   3910 C CD  . ARG D 1 57  ? 21.193  18.115  39.007  1.000 65.373  0 59  ARG DDD CD  1 ? 16 
ATOM   3911 N NE  . ARG D 1 57  ? 21.742  16.951  39.689  1.000 62.454  0 59  ARG DDD NE  1 ? 16 
ATOM   3912 C CZ  . ARG D 1 57  ? 21.544  15.690  39.320  1.000 61.352  0 59  ARG DDD CZ  1 ? 16 
ATOM   3913 N NH1 . ARG D 1 57  ? 20.794  15.409  38.267  1.000 63.036  0 59  ARG DDD NH1 1 ? 16 
ATOM   3914 N NH2 . ARG D 1 57  ? 22.088  14.706  40.017  1.000 59.979  0 59  ARG DDD NH2 1 ? 16 
ATOM   3915 N N   . THR D 1 58  ? 19.485  21.140  43.726  1.000 66.802  0 60  THR DDD N   1 ? 16 
ATOM   3916 C CA  . THR D 1 58  ? 18.483  21.149  44.821  1.000 66.548  0 60  THR DDD CA  1 ? 16 
ATOM   3917 C C   . THR D 1 58  ? 17.126  21.540  44.235  1.000 68.865  0 60  THR DDD C   1 ? 16 
ATOM   3918 O O   . THR D 1 58  ? 17.103  22.247  43.212  1.000 70.109  0 60  THR DDD O   1 ? 16 
ATOM   3919 C CB  . THR D 1 58  ? 18.901  22.079  45.967  1.000 67.922  0 60  THR DDD CB  1 ? 16 
ATOM   3920 O OG1 . THR D 1 58  ? 19.083  23.393  45.439  1.000 70.146  0 60  THR DDD OG1 1 ? 16 
ATOM   3921 C CG2 . THR D 1 58  ? 20.166  21.628  46.666  1.000 66.682  0 60  THR DDD CG2 1 ? 16 
ATOM   3922 N N   . TRP D 1 59  ? 16.050  21.061  44.858  1.000 69.366  0 61  TRP DDD N   1 ? 16 
ATOM   3923 C CA  . TRP D 1 59  ? 14.646  21.451  44.573  1.000 71.316  0 61  TRP DDD CA  1 ? 16 
ATOM   3924 C C   . TRP D 1 59  ? 13.972  21.792  45.902  1.000 71.455  0 61  TRP DDD C   1 ? 16 
ATOM   3925 O O   . TRP D 1 59  ? 14.212  21.064  46.882  1.000 69.483  0 61  TRP DDD O   1 ? 16 
ATOM   3926 C CB  . TRP D 1 59  ? 13.918  20.322  43.832  1.000 71.042  0 61  TRP DDD CB  1 ? 16 
ATOM   3927 C CG  . TRP D 1 59  ? 12.465  20.578  43.573  1.000 73.242  0 61  TRP DDD CG  1 ? 16 
ATOM   3928 C CD1 . TRP D 1 59  ? 11.913  21.098  42.439  1.000 76.892  0 61  TRP DDD CD1 1 ? 16 
ATOM   3929 C CD2 . TRP D 1 59  ? 11.367  20.299  44.461  1.000 73.897  0 61  TRP DDD CD2 1 ? 16 
ATOM   3930 N NE1 . TRP D 1 59  ? 10.551  21.172  42.562  1.000 79.364  0 61  TRP DDD NE1 1 ? 16 
ATOM   3931 C CE2 . TRP D 1 59  ? 10.187  20.686  43.790  1.000 77.300  0 61  TRP DDD CE2 1 ? 16 
ATOM   3932 C CE3 . TRP D 1 59  ? 11.265  19.769  45.752  1.000 72.572  0 61  TRP DDD CE3 1 ? 16 
ATOM   3933 C CZ2 . TRP D 1 59  ? 8.926   20.558  44.371  1.000 78.560  0 61  TRP DDD CZ2 1 ? 16 
ATOM   3934 C CZ3 . TRP D 1 59  ? 10.018  19.644  46.325  1.000 74.408  0 61  TRP DDD CZ3 1 ? 16 
ATOM   3935 C CH2 . TRP D 1 59  ? 8.867   20.035  45.642  1.000 77.042  0 61  TRP DDD CH2 1 ? 16 
ATOM   3936 N N   . TYR D 1 60  ? 13.182  22.864  45.931  1.000 73.684  0 62  TYR DDD N   1 ? 16 
ATOM   3937 C CA  . TYR D 1 60  ? 12.401  23.306  47.114  1.000 75.072  0 62  TYR DDD CA  1 ? 16 
ATOM   3938 C C   . TYR D 1 60  ? 10.951  23.535  46.678  1.000 77.986  0 62  TYR DDD C   1 ? 16 
ATOM   3939 O O   . TYR D 1 60  ? 10.741  24.056  45.566  1.000 80.643  0 62  TYR DDD O   1 ? 16 
ATOM   3940 C CB  . TYR D 1 60  ? 13.020  24.566  47.728  1.000 76.606  0 62  TYR DDD CB  1 ? 16 
ATOM   3941 C CG  . TYR D 1 60  ? 14.464  24.434  48.146  1.000 74.669  0 62  TYR DDD CG  1 ? 16 
ATOM   3942 C CD1 . TYR D 1 60  ? 14.805  23.969  49.406  1.000 73.499  0 62  TYR DDD CD1 1 ? 16 
ATOM   3943 C CD2 . TYR D 1 60  ? 15.495  24.785  47.287  1.000 74.680  0 62  TYR DDD CD2 1 ? 16 
ATOM   3944 C CE1 . TYR D 1 60  ? 16.129  23.847  49.798  1.000 72.666  0 62  TYR DDD CE1 1 ? 16 
ATOM   3945 C CE2 . TYR D 1 60  ? 16.825  24.669  47.662  1.000 73.757  0 62  TYR DDD CE2 1 ? 16 
ATOM   3946 C CZ  . TYR D 1 60  ? 17.146  24.195  48.923  1.000 73.184  0 62  TYR DDD CZ  1 ? 16 
ATOM   3947 O OH  . TYR D 1 60  ? 18.456  24.075  49.296  1.000 72.619  0 62  TYR DDD OH  1 ? 16 
ATOM   3948 N N   . ALA D 1 61  ? 9.990   23.136  47.515  1.000 78.387  0 63  ALA DDD N   1 ? 16 
ATOM   3949 C CA  . ALA D 1 61  ? 8.566   23.528  47.403  1.000 81.500  0 63  ALA DDD CA  1 ? 16 
ATOM   3950 C C   . ALA D 1 61  ? 8.471   25.049  47.586  1.000 85.120  0 63  ALA DDD C   1 ? 16 
ATOM   3951 O O   . ALA D 1 61  ? 9.267   25.593  48.376  1.000 85.814  0 63  ALA DDD O   1 ? 16 
ATOM   3952 C CB  . ALA D 1 61  ? 7.739   22.786  48.423  1.000 81.014  0 63  ALA DDD CB  1 ? 16 
ATOM   3953 N N   . ASP D 1 62  ? 7.549   25.706  46.874  1.000 88.635  0 64  ASP DDD N   1 ? 16 
ATOM   3954 C CA  . ASP D 1 62  ? 7.352   27.182  46.910  1.000 92.165  0 64  ASP DDD CA  1 ? 16 
ATOM   3955 C C   . ASP D 1 62  ? 7.111   27.642  48.356  1.000 93.495  0 64  ASP DDD C   1 ? 16 
ATOM   3956 O O   . ASP D 1 62  ? 7.638   28.705  48.725  1.000 94.803  0 64  ASP DDD O   1 ? 16 
ATOM   3957 C CB  . ASP D 1 62  ? 6.208   27.613  45.987  1.000 95.749  0 64  ASP DDD CB  1 ? 16 
ATOM   3958 C CG  . ASP D 1 62  ? 6.547   27.546  44.506  1.000 95.635  0 64  ASP DDD CG  1 ? 16 
ATOM   3959 O OD1 . ASP D 1 62  ? 7.749   27.523  44.177  1.000 93.361  0 64  ASP DDD OD1 1 ? 16 
ATOM   3960 O OD2 . ASP D 1 62  ? 5.605   27.519  43.691  1.000 98.021  0 64  ASP DDD OD2 1 ? 16 
ATOM   3961 N N   . SER D 1 63  ? 6.375   26.852  49.146  1.000 93.258  0 65  SER DDD N   1 ? 16 
ATOM   3962 C CA  . SER D 1 63  ? 5.932   27.185  50.526  1.000 95.575  0 65  SER DDD CA  1 ? 16 
ATOM   3963 C C   . SER D 1 63  ? 7.119   27.323  51.494  1.000 94.238  0 65  SER DDD C   1 ? 16 
ATOM   3964 O O   . SER D 1 63  ? 6.914   27.935  52.560  1.000 96.806  0 65  SER DDD O   1 ? 16 
ATOM   3965 C CB  . SER D 1 63  ? 4.944   26.163  51.030  1.000 95.432  0 65  SER DDD CB  1 ? 16 
ATOM   3966 O OG  . SER D 1 63  ? 5.536   24.874  51.087  1.000 91.462  0 65  SER DDD OG  1 ? 16 
ATOM   3967 N N   . VAL D 1 64  ? 8.296   26.774  51.163  1.000 90.861  0 66  VAL DDD N   1 ? 16 
ATOM   3968 C CA  . VAL D 1 64  ? 9.495   26.776  52.061  1.000 89.313  0 66  VAL DDD CA  1 ? 16 
ATOM   3969 C C   . VAL D 1 64  ? 10.709  27.420  51.376  1.000 89.081  0 66  VAL DDD C   1 ? 16 
ATOM   3970 O O   . VAL D 1 64  ? 11.759  27.510  52.042  1.000 87.684  0 66  VAL DDD O   1 ? 16 
ATOM   3971 C CB  . VAL D 1 64  ? 9.845   25.352  52.536  1.000 85.787  0 66  VAL DDD CB  1 ? 16 
ATOM   3972 C CG1 . VAL D 1 64  ? 8.653   24.667  53.183  1.000 86.813  0 66  VAL DDD CG1 1 ? 16 
ATOM   3973 C CG2 . VAL D 1 64  ? 10.415  24.492  51.418  1.000 82.558  0 66  VAL DDD CG2 1 ? 16 
ATOM   3974 N N   . LYS D 1 65  ? 10.588  27.847  50.114  1.000 89.793  0 67  LYS DDD N   1 ? 16 
ATOM   3975 C CA  . LYS D 1 65  ? 11.731  28.332  49.293  1.000 89.457  0 67  LYS DDD CA  1 ? 16 
ATOM   3976 C C   . LYS D 1 65  ? 12.258  29.641  49.893  1.000 91.908  0 67  LYS DDD C   1 ? 16 
ATOM   3977 O O   . LYS D 1 65  ? 11.433  30.489  50.278  1.000 94.828  0 67  LYS DDD O   1 ? 16 
ATOM   3978 C CB  . LYS D 1 65  ? 11.301  28.499  47.832  1.000 91.506  0 67  LYS DDD CB  1 ? 16 
ATOM   3979 C CG  . LYS D 1 65  ? 12.440  28.598  46.824  1.000 91.442  0 67  LYS DDD CG  1 ? 16 
ATOM   3980 C CD  . LYS D 1 65  ? 11.972  28.483  45.386  1.000 92.704  0 67  LYS DDD CD  1 ? 16 
ATOM   3981 C CE  . LYS D 1 65  ? 12.904  29.142  44.389  1.000 94.470  0 67  LYS DDD CE  1 ? 16 
ATOM   3982 N NZ  . LYS D 1 65  ? 12.178  29.583  43.174  1.000 97.652  0 67  LYS DDD NZ  1 ? 16 
ATOM   3983 N N   . GLY D 1 66  ? 13.584  29.776  49.998  1.000 91.331  0 68  GLY DDD N   1 ? 16 
ATOM   3984 C CA  . GLY D 1 66  ? 14.267  30.947  50.584  1.000 94.124  0 68  GLY DDD CA  1 ? 16 
ATOM   3985 C C   . GLY D 1 66  ? 14.450  30.819  52.089  1.000 94.097  0 68  GLY DDD C   1 ? 16 
ATOM   3986 O O   . GLY D 1 66  ? 15.302  31.549  52.636  1.000 95.382  0 68  GLY DDD O   1 ? 16 
ATOM   3987 N N   . ARG D 1 67  ? 13.690  29.925  52.736  1.000 92.974  0 69  ARG DDD N   1 ? 16 
ATOM   3988 C CA  . ARG D 1 67  ? 13.631  29.760  54.216  1.000 93.818  0 69  ARG DDD CA  1 ? 16 
ATOM   3989 C C   . ARG D 1 67  ? 14.307  28.449  54.644  1.000 90.586  0 69  ARG DDD C   1 ? 16 
ATOM   3990 O O   . ARG D 1 67  ? 14.903  28.433  55.741  1.000 91.099  0 69  ARG DDD O   1 ? 16 
ATOM   3991 C CB  . ARG D 1 67  ? 12.170  29.806  54.674  1.000 95.348  0 69  ARG DDD CB  1 ? 16 
ATOM   3992 C CG  . ARG D 1 67  ? 11.426  31.053  54.220  1.000 99.041  0 69  ARG DDD CG  1 ? 16 
ATOM   3993 C CD  . ARG D 1 67  ? 10.086  31.233  54.904  1.000 101.717 0 69  ARG DDD CD  1 ? 16 
ATOM   3994 N NE  . ARG D 1 67  ? 9.240   30.050  54.797  1.000 99.002  0 69  ARG DDD NE  1 ? 16 
ATOM   3995 C CZ  . ARG D 1 67  ? 9.023   29.159  55.766  1.000 97.818  0 69  ARG DDD CZ  1 ? 16 
ATOM   3996 N NH1 . ARG D 1 67  ? 9.585   29.292  56.958  1.000 99.111  0 69  ARG DDD NH1 1 ? 16 
ATOM   3997 N NH2 . ARG D 1 67  ? 8.230   28.129  55.534  1.000 95.912  0 69  ARG DDD NH2 1 ? 16 
ATOM   3998 N N   . PHE D 1 68  ? 14.198  27.389  53.832  1.000 88.072  0 70  PHE DDD N   1 ? 16 
ATOM   3999 C CA  . PHE D 1 68  ? 14.793  26.049  54.087  1.000 84.162  0 70  PHE DDD CA  1 ? 16 
ATOM   4000 C C   . PHE D 1 68  ? 15.986  25.827  53.150  1.000 81.888  0 70  PHE DDD C   1 ? 16 
ATOM   4001 O O   . PHE D 1 68  ? 15.904  26.194  51.963  1.000 81.597  0 70  PHE DDD O   1 ? 16 
ATOM   4002 C CB  . PHE D 1 68  ? 13.765  24.935  53.866  1.000 82.622  0 70  PHE DDD CB  1 ? 16 
ATOM   4003 C CG  . PHE D 1 68  ? 12.644  24.842  54.874  1.000 84.460  0 70  PHE DDD CG  1 ? 16 
ATOM   4004 C CD1 . PHE D 1 68  ? 12.345  25.885  55.740  1.000 88.058  0 70  PHE DDD CD1 1 ? 16 
ATOM   4005 C CD2 . PHE D 1 68  ? 11.848  23.707  54.919  1.000 83.387  0 70  PHE DDD CD2 1 ? 16 
ATOM   4006 C CE1 . PHE D 1 68  ? 11.298  25.780  56.644  1.000 90.241  0 70  PHE DDD CE1 1 ? 16 
ATOM   4007 C CE2 . PHE D 1 68  ? 10.800  23.606  55.821  1.000 85.912  0 70  PHE DDD CE2 1 ? 16 
ATOM   4008 C CZ  . PHE D 1 68  ? 10.527  24.642  56.682  1.000 88.840  0 70  PHE DDD CZ  1 ? 16 
ATOM   4009 N N   . THR D 1 69  ? 17.057  25.226  53.670  1.000 80.265  0 71  THR DDD N   1 ? 16 
ATOM   4010 C CA  . THR D 1 69  ? 18.234  24.762  52.888  1.000 77.961  0 71  THR DDD CA  1 ? 16 
ATOM   4011 C C   . THR D 1 69  ? 18.426  23.264  53.129  1.000 74.530  0 71  THR DDD C   1 ? 16 
ATOM   4012 O O   . THR D 1 69  ? 18.549  22.865  54.307  1.000 74.224  0 71  THR DDD O   1 ? 16 
ATOM   4013 C CB  . THR D 1 69  ? 19.501  25.542  53.260  1.000 79.906  0 71  THR DDD CB  1 ? 16 
ATOM   4014 O OG1 . THR D 1 69  ? 19.240  26.925  53.025  1.000 83.881  0 71  THR DDD OG1 1 ? 16 
ATOM   4015 C CG2 . THR D 1 69  ? 20.716  25.104  52.472  1.000 78.056  0 71  THR DDD CG2 1 ? 16 
ATOM   4016 N N   . ILE D 1 70  ? 18.441  22.476  52.051  1.000 71.924  0 72  ILE DDD N   1 ? 16 
ATOM   4017 C CA  . ILE D 1 70  ? 18.839  21.038  52.068  1.000 68.878  0 72  ILE DDD CA  1 ? 16 
ATOM   4018 C C   . ILE D 1 70  ? 20.319  20.981  51.678  1.000 68.461  0 72  ILE DDD C   1 ? 16 
ATOM   4019 O O   . ILE D 1 70  ? 20.718  21.740  50.768  1.000 71.665  0 72  ILE DDD O   1 ? 16 
ATOM   4020 C CB  . ILE D 1 70  ? 17.940  20.175  51.153  1.000 67.222  0 72  ILE DDD CB  1 ? 16 
ATOM   4021 C CG1 . ILE D 1 70  ? 18.159  18.680  51.403  1.000 65.063  0 72  ILE DDD CG1 1 ? 16 
ATOM   4022 C CG2 . ILE D 1 70  ? 18.120  20.530  49.680  1.000 67.704  0 72  ILE DDD CG2 1 ? 16 
ATOM   4023 C CD1 . ILE D 1 70  ? 17.168  17.784  50.698  1.000 63.733  0 72  ILE DDD CD1 1 ? 16 
ATOM   4024 N N   . SER D 1 71  ? 21.103  20.167  52.388  1.000 65.872  0 73  SER DDD N   1 ? 16 
ATOM   4025 C CA  . SER D 1 71  ? 22.540  19.901  52.119  1.000 65.188  0 73  SER DDD CA  1 ? 16 
ATOM   4026 C C   . SER D 1 71  ? 22.850  18.458  52.518  1.000 63.314  0 73  SER DDD C   1 ? 16 
ATOM   4027 O O   . SER D 1 71  ? 22.006  17.844  53.196  1.000 62.935  0 73  SER DDD O   1 ? 16 
ATOM   4028 C CB  . SER D 1 71  ? 23.421  20.880  52.847  1.000 67.571  0 73  SER DDD CB  1 ? 16 
ATOM   4029 O OG  . SER D 1 71  ? 23.169  20.844  54.242  1.000 68.340  0 73  SER DDD OG  1 ? 16 
ATOM   4030 N N   . ARG D 1 72  ? 24.007  17.934  52.111  1.000 63.516  0 74  ARG DDD N   1 ? 16 
ATOM   4031 C CA  . ARG D 1 72  ? 24.404  16.532  52.410  1.000 62.002  0 74  ARG DDD CA  1 ? 16 
ATOM   4032 C C   . ARG D 1 72  ? 25.912  16.438  52.674  1.000 62.206  0 74  ARG DDD C   1 ? 16 
ATOM   4033 O O   . ARG D 1 72  ? 26.678  17.232  52.108  1.000 62.217  0 74  ARG DDD O   1 ? 16 
ATOM   4034 C CB  . ARG D 1 72  ? 23.958  15.608  51.272  1.000 59.694  0 74  ARG DDD CB  1 ? 16 
ATOM   4035 C CG  . ARG D 1 72  ? 24.550  15.933  49.906  1.000 59.688  0 74  ARG DDD CG  1 ? 16 
ATOM   4036 C CD  . ARG D 1 72  ? 23.836  15.158  48.810  1.000 57.398  0 74  ARG DDD CD  1 ? 16 
ATOM   4037 N NE  . ARG D 1 72  ? 23.931  13.715  49.027  1.000 55.250  0 74  ARG DDD NE  1 ? 16 
ATOM   4038 C CZ  . ARG D 1 72  ? 23.103  12.798  48.531  1.000 54.064  0 74  ARG DDD CZ  1 ? 16 
ATOM   4039 N NH1 . ARG D 1 72  ? 23.304  11.522  48.809  1.000 53.351  0 74  ARG DDD NH1 1 ? 16 
ATOM   4040 N NH2 . ARG D 1 72  ? 22.069  13.142  47.782  1.000 54.877  0 74  ARG DDD NH2 1 ? 16 
ATOM   4041 N N   . ASP D 1 73  ? 26.291  15.489  53.530  1.000 62.724  0 75  ASP DDD N   1 ? 16 
ATOM   4042 C CA  . ASP D 1 73  ? 27.689  15.131  53.886  1.000 65.323  0 75  ASP DDD CA  1 ? 16 
ATOM   4043 C C   . ASP D 1 73  ? 27.892  13.662  53.490  1.000 63.685  0 75  ASP DDD C   1 ? 16 
ATOM   4044 O O   . ASP D 1 73  ? 27.624  12.774  54.328  1.000 64.933  0 75  ASP DDD O   1 ? 16 
ATOM   4045 C CB  . ASP D 1 73  ? 27.944  15.411  55.372  1.000 67.522  0 75  ASP DDD CB  1 ? 16 
ATOM   4046 C CG  . ASP D 1 73  ? 29.391  15.276  55.815  1.000 71.073  0 75  ASP DDD CG  1 ? 16 
ATOM   4047 O OD1 . ASP D 1 73  ? 30.242  14.962  54.959  1.000 72.274  0 75  ASP DDD OD1 1 ? 16 
ATOM   4048 O OD2 . ASP D 1 73  ? 29.656  15.492  57.019  1.000 73.193  0 75  ASP DDD OD2 1 ? 16 
ATOM   4049 N N   . ASN D 1 74  ? 28.315  13.422  52.245  1.000 61.427  0 76  ASN DDD N   1 ? 16 
ATOM   4050 C CA  . ASN D 1 74  ? 28.362  12.073  51.620  1.000 59.035  0 76  ASN DDD CA  1 ? 16 
ATOM   4051 C C   . ASN D 1 74  ? 29.283  11.146  52.413  1.000 59.466  0 76  ASN DDD C   1 ? 16 
ATOM   4052 O O   . ASN D 1 74  ? 28.919  10.002  52.662  1.000 58.694  0 76  ASN DDD O   1 ? 16 
ATOM   4053 C CB  . ASN D 1 74  ? 28.722  12.149  50.134  1.000 58.776  0 76  ASN DDD CB  1 ? 16 
ATOM   4054 C CG  . ASN D 1 74  ? 27.511  12.368  49.249  1.000 57.880  0 76  ASN DDD CG  1 ? 16 
ATOM   4055 O OD1 . ASN D 1 74  ? 26.402  12.589  49.735  1.000 56.909  0 76  ASN DDD OD1 1 ? 16 
ATOM   4056 N ND2 . ASN D 1 74  ? 27.712  12.305  47.944  1.000 57.937  0 76  ASN DDD ND2 1 ? 16 
ATOM   4057 N N   . PRO D 1 75  ? 30.492  11.580  52.841  1.000 61.401  0 77  PRO DDD N   1 ? 16 
ATOM   4058 C CA  . PRO D 1 75  ? 31.343  10.736  53.683  1.000 62.570  0 77  PRO DDD CA  1 ? 16 
ATOM   4059 C C   . PRO D 1 75  ? 30.678  10.278  54.993  1.000 62.472  0 77  PRO DDD C   1 ? 16 
ATOM   4060 O O   . PRO D 1 75  ? 31.074  9.246   55.493  1.000 63.315  0 77  PRO DDD O   1 ? 16 
ATOM   4061 C CB  . PRO D 1 75  ? 32.555  11.632  53.979  1.000 66.074  0 77  PRO DDD CB  1 ? 16 
ATOM   4062 C CG  . PRO D 1 75  ? 32.590  12.599  52.817  1.000 65.760  0 77  PRO DDD CG  1 ? 16 
ATOM   4063 C CD  . PRO D 1 75  ? 31.134  12.857  52.497  1.000 62.779  0 77  PRO DDD CD  1 ? 16 
ATOM   4064 N N   . GLN D 1 76  ? 29.692  11.033  55.495  1.000 62.727  0 78  GLN DDD N   1 ? 16 
ATOM   4065 C CA  . GLN D 1 76  ? 28.984  10.770  56.782  1.000 63.728  0 78  GLN DDD CA  1 ? 16 
ATOM   4066 C C   . GLN D 1 76  ? 27.576  10.202  56.548  1.000 60.437  0 78  GLN DDD C   1 ? 16 
ATOM   4067 O O   . GLN D 1 76  ? 26.863  9.992   57.545  1.000 60.430  0 78  GLN DDD O   1 ? 16 
ATOM   4068 C CB  . GLN D 1 76  ? 28.895  12.059  57.601  1.000 66.859  0 78  GLN DDD CB  1 ? 16 
ATOM   4069 C CG  . GLN D 1 76  ? 30.237  12.520  58.142  1.000 71.453  0 78  GLN DDD CG  1 ? 16 
ATOM   4070 C CD  . GLN D 1 76  ? 30.810  11.521  59.118  1.000 74.777  0 78  GLN DDD CD  1 ? 16 
ATOM   4071 O OE1 . GLN D 1 76  ? 30.168  11.154  60.100  1.000 76.827  0 78  GLN DDD OE1 1 ? 16 
ATOM   4072 N NE2 . GLN D 1 76  ? 32.024  11.062  58.850  1.000 76.386  0 78  GLN DDD NE2 1 ? 16 
ATOM   4073 N N   . ASN D 1 77  ? 27.190  9.955   55.294  1.000 58.408  0 79  ASN DDD N   1 ? 16 
ATOM   4074 C CA  . ASN D 1 77  ? 25.866  9.391   54.917  1.000 55.959  0 79  ASN DDD CA  1 ? 16 
ATOM   4075 C C   . ASN D 1 77  ? 24.757  10.137  55.666  1.000 57.218  0 79  ASN DDD C   1 ? 16 
ATOM   4076 O O   . ASN D 1 77  ? 23.902  9.464   56.260  1.000 57.541  0 79  ASN DDD O   1 ? 16 
ATOM   4077 C CB  . ASN D 1 77  ? 25.798  7.883   55.180  1.000 54.323  0 79  ASN DDD CB  1 ? 16 
ATOM   4078 C CG  . ASN D 1 77  ? 26.792  7.100   54.353  1.000 53.270  0 79  ASN DDD CG  1 ? 16 
ATOM   4079 O OD1 . ASN D 1 77  ? 27.213  7.555   53.297  1.000 54.088  0 79  ASN DDD OD1 1 ? 16 
ATOM   4080 N ND2 . ASN D 1 77  ? 27.164  5.919   54.812  1.000 53.809  0 79  ASN DDD ND2 1 ? 16 
ATOM   4081 N N   . THR D 1 78  ? 24.772  11.472  55.623  1.000 59.142  0 80  THR DDD N   1 ? 16 
ATOM   4082 C CA  . THR D 1 78  ? 23.802  12.345  56.334  1.000 60.888  0 80  THR DDD CA  1 ? 16 
ATOM   4083 C C   . THR D 1 78  ? 23.307  13.451  55.391  1.000 61.084  0 80  THR DDD C   1 ? 16 
ATOM   4084 O O   . THR D 1 78  ? 24.134  14.033  54.660  1.000 60.996  0 80  THR DDD O   1 ? 16 
ATOM   4085 C CB  . THR D 1 78  ? 24.416  12.895  57.628  1.000 62.645  0 80  THR DDD CB  1 ? 16 
ATOM   4086 O OG1 . THR D 1 78  ? 24.831  11.769  58.401  1.000 63.383  0 80  THR DDD OG1 1 ? 16 
ATOM   4087 C CG2 . THR D 1 78  ? 23.458  13.741  58.436  1.000 63.868  0 80  THR DDD CG2 1 ? 16 
ATOM   4088 N N   . VAL D 1 79  ? 21.996  13.707  55.415  1.000 61.540  0 81  VAL DDD N   1 ? 16 
ATOM   4089 C CA  . VAL D 1 79  ? 21.321  14.832  54.702  1.000 62.046  0 81  VAL DDD CA  1 ? 16 
ATOM   4090 C C   . VAL D 1 79  ? 20.699  15.739  55.769  1.000 64.954  0 81  VAL DDD C   1 ? 16 
ATOM   4091 O O   . VAL D 1 79  ? 20.149  15.207  56.754  1.000 64.155  0 81  VAL DDD O   1 ? 16 
ATOM   4092 C CB  . VAL D 1 79  ? 20.282  14.322  53.681  1.000 60.865  0 81  VAL DDD CB  1 ? 16 
ATOM   4093 C CG1 . VAL D 1 79  ? 19.180  13.487  54.324  1.000 61.130  0 81  VAL DDD CG1 1 ? 16 
ATOM   4094 C CG2 . VAL D 1 79  ? 19.686  15.456  52.858  1.000 61.155  0 81  VAL DDD CG2 1 ? 16 
ATOM   4095 N N   . TYR D 1 80  ? 20.813  17.057  55.594  1.000 67.304  0 82  TYR DDD N   1 ? 16 
ATOM   4096 C CA  . TYR D 1 80  ? 20.355  18.085  56.564  1.000 70.243  0 82  TYR DDD CA  1 ? 16 
ATOM   4097 C C   . TYR D 1 80  ? 19.251  18.936  55.931  1.000 70.263  0 82  TYR DDD C   1 ? 16 
ATOM   4098 O O   . TYR D 1 80  ? 19.281  19.147  54.703  1.000 70.365  0 82  TYR DDD O   1 ? 16 
ATOM   4099 C CB  . TYR D 1 80  ? 21.528  18.966  57.000  1.000 72.829  0 82  TYR DDD CB  1 ? 16 
ATOM   4100 C CG  . TYR D 1 80  ? 22.672  18.220  57.637  1.000 73.190  0 82  TYR DDD CG  1 ? 16 
ATOM   4101 C CD1 . TYR D 1 80  ? 22.702  17.989  59.002  1.000 75.950  0 82  TYR DDD CD1 1 ? 16 
ATOM   4102 C CD2 . TYR D 1 80  ? 23.735  17.757  56.877  1.000 71.718  0 82  TYR DDD CD2 1 ? 16 
ATOM   4103 C CE1 . TYR D 1 80  ? 23.748  17.298  59.596  1.000 77.056  0 82  TYR DDD CE1 1 ? 16 
ATOM   4104 C CE2 . TYR D 1 80  ? 24.790  17.070  57.455  1.000 73.210  0 82  TYR DDD CE2 1 ? 16 
ATOM   4105 C CZ  . TYR D 1 80  ? 24.801  16.843  58.820  1.000 75.763  0 82  TYR DDD CZ  1 ? 16 
ATOM   4106 O OH  . TYR D 1 80  ? 25.839  16.171  59.400  1.000 75.865  0 82  TYR DDD OH  1 ? 16 
ATOM   4107 N N   . LEU D 1 81  ? 18.305  19.398  56.753  1.000 72.278  0 83  LEU DDD N   1 ? 16 
ATOM   4108 C CA  . LEU D 1 81  ? 17.308  20.435  56.376  1.000 74.476  0 83  LEU DDD CA  1 ? 16 
ATOM   4109 C C   . LEU D 1 81  ? 17.385  21.578  57.392  1.000 78.991  0 83  LEU DDD C   1 ? 16 
ATOM   4110 O O   . LEU D 1 81  ? 16.703  21.500  58.433  1.000 80.532  0 83  LEU DDD O   1 ? 16 
ATOM   4111 C CB  . LEU D 1 81  ? 15.904  19.822  56.317  1.000 73.883  0 83  LEU DDD CB  1 ? 16 
ATOM   4112 C CG  . LEU D 1 81  ? 14.808  20.747  55.786  1.000 75.053  0 83  LEU DDD CG  1 ? 16 
ATOM   4113 C CD1 . LEU D 1 81  ? 15.094  21.169  54.352  1.000 73.595  0 83  LEU DDD CD1 1 ? 16 
ATOM   4114 C CD2 . LEU D 1 81  ? 13.443  20.085  55.880  1.000 75.085  0 83  LEU DDD CD2 1 ? 16 
ATOM   4115 N N   . GLN D 1 82  ? 18.218  22.581  57.101  1.000 81.846  0 84  GLN DDD N   1 ? 16 
ATOM   4116 C CA  . GLN D 1 82  ? 18.266  23.871  57.836  1.000 86.529  0 84  GLN DDD CA  1 ? 16 
ATOM   4117 C C   . GLN D 1 82  ? 16.955  24.611  57.561  1.000 88.574  0 84  GLN DDD C   1 ? 16 
ATOM   4118 O O   . GLN D 1 82  ? 16.719  24.954  56.389  1.000 88.224  0 84  GLN DDD O   1 ? 16 
ATOM   4119 C CB  . GLN D 1 82  ? 19.477  24.699  57.398  1.000 87.956  0 84  GLN DDD CB  1 ? 16 
ATOM   4120 C CG  . GLN D 1 82  ? 19.724  25.927  58.263  1.000 91.997  0 84  GLN DDD CG  1 ? 16 
ATOM   4121 C CD  . GLN D 1 82  ? 19.971  25.550  59.703  1.000 93.908  0 84  GLN DDD CD  1 ? 16 
ATOM   4122 O OE1 . GLN D 1 82  ? 20.837  24.731  60.009  1.000 92.621  0 84  GLN DDD OE1 1 ? 16 
ATOM   4123 N NE2 . GLN D 1 82  ? 19.196  26.137  60.601  1.000 97.760  0 84  GLN DDD NE2 1 ? 16 
ATOM   4124 N N   . MET D 1 83  ? 16.126  24.803  58.592  1.000 92.460  0 85  MET DDD N   1 ? 16 
ATOM   4125 C CA  . MET D 1 83  ? 14.807  25.486  58.499  1.000 95.926  0 85  MET DDD CA  1 ? 16 
ATOM   4126 C C   . MET D 1 83  ? 14.877  26.796  59.292  1.000 99.622  0 85  MET DDD C   1 ? 16 
ATOM   4127 O O   . MET D 1 83  ? 14.972  26.730  60.532  1.000 101.623 0 85  MET DDD O   1 ? 16 
ATOM   4128 C CB  . MET D 1 83  ? 13.684  24.604  59.053  1.000 97.211  0 85  MET DDD CB  1 ? 16 
ATOM   4129 C CG  . MET D 1 83  ? 13.554  23.261  58.348  1.000 95.523  0 85  MET DDD CG  1 ? 16 
ATOM   4130 S SD  . MET D 1 83  ? 12.180  22.258  58.985  1.000 97.971  0 85  MET DDD SD  1 ? 16 
ATOM   4131 C CE  . MET D 1 83  ? 12.690  22.010  60.685  1.000 100.071 0 85  MET DDD CE  1 ? 16 
ATOM   4132 N N   . ASN D 1 84  ? 14.860  27.933  58.588  1.000 100.581 0 86  ASN DDD N   1 ? 16 
ATOM   4133 C CA  . ASN D 1 84  ? 14.928  29.301  59.169  1.000 104.403 0 86  ASN DDD CA  1 ? 16 
ATOM   4134 C C   . ASN D 1 84  ? 13.591  30.009  58.922  1.000 107.319 0 86  ASN DDD C   1 ? 16 
ATOM   4135 O O   . ASN D 1 84  ? 12.914  29.657  57.941  1.000 105.490 0 86  ASN DDD O   1 ? 16 
ATOM   4136 C CB  . ASN D 1 84  ? 16.093  30.101  58.579  1.000 104.817 0 86  ASN DDD CB  1 ? 16 
ATOM   4137 C CG  . ASN D 1 84  ? 17.432  29.410  58.738  1.000 102.310 0 86  ASN DDD CG  1 ? 16 
ATOM   4138 O OD1 . ASN D 1 84  ? 17.587  28.528  59.581  1.000 102.565 0 86  ASN DDD OD1 1 ? 16 
ATOM   4139 N ND2 . ASN D 1 84  ? 18.409  29.804  57.936  1.000 100.990 0 86  ASN DDD ND2 1 ? 16 
ATOM   4140 N N   . ASN D 1 85  ? 13.226  30.959  59.787  1.000 112.216 0 87  ASN DDD N   1 ? 16 
ATOM   4141 C CA  . ASN D 1 85  ? 12.008  31.802  59.646  1.000 115.828 0 87  ASN DDD CA  1 ? 16 
ATOM   4142 C C   . ASN D 1 85  ? 10.759  30.911  59.701  1.000 114.609 0 87  ASN DDD C   1 ? 16 
ATOM   4143 O O   . ASN D 1 85  ? 9.833   31.146  58.900  1.000 114.300 0 87  ASN DDD O   1 ? 16 
ATOM   4144 C CB  . ASN D 1 85  ? 12.038  32.621  58.349  1.000 116.207 0 87  ASN DDD CB  1 ? 16 
ATOM   4145 C CG  . ASN D 1 85  ? 13.281  33.471  58.189  1.000 117.653 0 87  ASN DDD CG  1 ? 16 
ATOM   4146 O OD1 . ASN D 1 85  ? 14.182  33.440  59.024  1.000 118.818 0 87  ASN DDD OD1 1 ? 16 
ATOM   4147 N ND2 . ASN D 1 85  ? 13.335  34.239  57.114  1.000 118.631 0 87  ASN DDD ND2 1 ? 16 
ATOM   4148 N N   . LEU D 1 86  ? 10.737  29.925  60.604  1.000 114.279 0 88  LEU DDD N   1 ? 16 
ATOM   4149 C CA  . LEU D 1 86  ? 9.610   28.962  60.750  1.000 114.366 0 88  LEU DDD CA  1 ? 16 
ATOM   4150 C C   . LEU D 1 86  ? 8.322   29.733  61.057  1.000 118.737 0 88  LEU DDD C   1 ? 16 
ATOM   4151 O O   . LEU D 1 86  ? 8.345   30.573  61.971  1.000 123.371 0 88  LEU DDD O   1 ? 16 
ATOM   4152 C CB  . LEU D 1 86  ? 9.914   27.955  61.864  1.000 114.683 0 88  LEU DDD CB  1 ? 16 
ATOM   4153 C CG  . LEU D 1 86  ? 10.567  26.649  61.415  1.000 110.958 0 88  LEU DDD CG  1 ? 16 
ATOM   4154 C CD1 . LEU D 1 86  ? 12.074  26.807  61.307  1.000 109.653 0 88  LEU DDD CD1 1 ? 16 
ATOM   4155 C CD2 . LEU D 1 86  ? 10.223  25.513  62.370  1.000 111.725 0 88  LEU DDD CD2 1 ? 16 
ATOM   4156 N N   . LYS D 1 87  ? 7.254   29.459  60.303  1.000 115.208 0 89  LYS DDD N   1 ? 17 
ATOM   4157 C CA  . LYS D 1 87  ? 5.879   29.960  60.558  1.000 118.372 0 89  LYS DDD CA  1 ? 17 
ATOM   4158 C C   . LYS D 1 87  ? 5.024   28.790  61.062  1.000 116.573 0 89  LYS DDD C   1 ? 17 
ATOM   4159 O O   . LYS D 1 87  ? 5.419   27.625  60.836  1.000 111.135 0 89  LYS DDD O   1 ? 17 
ATOM   4160 C CB  . LYS D 1 87  ? 5.310   30.597  59.285  1.000 119.086 0 89  LYS DDD CB  1 ? 17 
ATOM   4161 C CG  . LYS D 1 87  ? 3.897   31.153  59.411  1.000 123.052 0 89  LYS DDD CG  1 ? 17 
ATOM   4162 C CD  . LYS D 1 87  ? 3.458   31.992  58.230  1.000 125.350 0 89  LYS DDD CD  1 ? 17 
ATOM   4163 C CE  . LYS D 1 87  ? 2.151   32.714  58.481  1.000 129.862 0 89  LYS DDD CE  1 ? 17 
ATOM   4164 N NZ  . LYS D 1 87  ? 1.728   33.511  57.306  1.000 132.034 0 89  LYS DDD NZ  1 ? 17 
ATOM   4165 N N   . SER D 1 88  ? 3.891   29.096  61.702  1.000 120.805 0 90  SER DDD N   1 ? 17 
ATOM   4166 C CA  . SER D 1 88  ? 2.960   28.127  62.342  1.000 119.957 0 90  SER DDD CA  1 ? 17 
ATOM   4167 C C   . SER D 1 88  ? 2.524   27.036  61.352  1.000 115.689 0 90  SER DDD C   1 ? 17 
ATOM   4168 O O   . SER D 1 88  ? 2.219   25.919  61.815  1.000 113.700 0 90  SER DDD O   1 ? 17 
ATOM   4169 C CB  . SER D 1 88  ? 1.765   28.844  62.923  1.000 124.709 0 90  SER DDD CB  1 ? 17 
ATOM   4170 O OG  . SER D 1 88  ? 0.890   27.930  63.564  1.000 125.059 0 90  SER DDD OG  1 ? 17 
ATOM   4171 N N   . GLY D 1 89  ? 2.500   27.343  60.048  1.000 114.313 0 91  GLY DDD N   1 ? 17 
ATOM   4172 C CA  . GLY D 1 89  ? 2.031   26.438  58.978  1.000 110.788 0 91  GLY DDD CA  1 ? 17 
ATOM   4173 C C   . GLY D 1 89  ? 3.071   25.410  58.552  1.000 105.266 0 91  GLY DDD C   1 ? 17 
ATOM   4174 O O   . GLY D 1 89  ? 2.757   24.613  57.648  1.000 101.917 0 91  GLY DDD O   1 ? 17 
ATOM   4175 N N   . ASP D 1 90  ? 4.266   25.426  59.155  1.000 103.672 0 92  ASP DDD N   1 ? 17 
ATOM   4176 C CA  . ASP D 1 90  ? 5.346   24.429  58.913  1.000 98.622  0 92  ASP DDD CA  1 ? 17 
ATOM   4177 C C   . ASP D 1 90  ? 5.149   23.212  59.825  1.000 96.583  0 92  ASP DDD C   1 ? 17 
ATOM   4178 O O   . ASP D 1 90  ? 5.757   22.164  59.535  1.000 92.768  0 92  ASP DDD O   1 ? 17 
ATOM   4179 C CB  . ASP D 1 90  ? 6.736   25.036  59.131  1.000 98.572  0 92  ASP DDD CB  1 ? 17 
ATOM   4180 C CG  . ASP D 1 90  ? 7.161   26.017  58.053  1.000 98.643  0 92  ASP DDD CG  1 ? 17 
ATOM   4181 O OD1 . ASP D 1 90  ? 6.800   25.797  56.878  1.000 96.532  0 92  ASP DDD OD1 1 ? 17 
ATOM   4182 O OD2 . ASP D 1 90  ? 7.859   26.993  58.397  1.000 100.490 0 92  ASP DDD OD2 1 ? 17 
ATOM   4183 N N   . THR D 1 91  ? 4.346   23.348  60.888  1.000 98.899  0 93  THR DDD N   1 ? 17 
ATOM   4184 C CA  . THR D 1 91  ? 4.065   22.278  61.886  1.000 97.595  0 93  THR DDD CA  1 ? 17 
ATOM   4185 C C   . THR D 1 91  ? 3.564   21.031  61.148  1.000 93.848  0 93  THR DDD C   1 ? 17 
ATOM   4186 O O   . THR D 1 91  ? 2.537   21.124  60.456  1.000 93.571  0 93  THR DDD O   1 ? 17 
ATOM   4187 C CB  . THR D 1 91  ? 3.101   22.771  62.975  1.000 101.399 0 93  THR DDD CB  1 ? 17 
ATOM   4188 O OG1 . THR D 1 91  ? 3.846   23.682  63.783  1.000 103.735 0 93  THR DDD OG1 1 ? 17 
ATOM   4189 C CG2 . THR D 1 91  ? 2.543   21.671  63.853  1.000 101.478 0 93  THR DDD CG2 1 ? 17 
ATOM   4190 N N   . ALA D 1 92  ? 4.278   19.913  61.300  1.000 90.833  0 94  ALA DDD N   1 ? 17 
ATOM   4191 C CA  . ALA D 1 92  ? 4.026   18.641  60.584  1.000 88.315  0 94  ALA DDD CA  1 ? 17 
ATOM   4192 C C   . ALA D 1 92  ? 5.042   17.585  61.025  1.000 85.407  0 94  ALA DDD C   1 ? 17 
ATOM   4193 O O   . ALA D 1 92  ? 6.033   17.949  61.689  1.000 86.222  0 94  ALA DDD O   1 ? 17 
ATOM   4194 C CB  . ALA D 1 92  ? 4.102   18.871  59.092  1.000 86.504  0 94  ALA DDD CB  1 ? 17 
ATOM   4195 N N   . VAL D 1 93  ? 4.786   16.326  60.662  1.000 82.784  0 95  VAL DDD N   1 ? 17 
ATOM   4196 C CA  . VAL D 1 93  ? 5.756   15.198  60.776  1.000 80.377  0 95  VAL DDD CA  1 ? 17 
ATOM   4197 C C   . VAL D 1 93  ? 6.655   15.248  59.535  1.000 77.870  0 95  VAL DDD C   1 ? 17 
ATOM   4198 O O   . VAL D 1 93  ? 6.121   15.082  58.423  1.000 77.939  0 95  VAL DDD O   1 ? 17 
ATOM   4199 C CB  . VAL D 1 93  ? 5.032   13.843  60.904  1.000 79.731  0 95  VAL DDD CB  1 ? 17 
ATOM   4200 C CG1 . VAL D 1 93  ? 6.016   12.684  60.996  1.000 78.103  0 95  VAL DDD CG1 1 ? 17 
ATOM   4201 C CG2 . VAL D 1 93  ? 4.065   13.820  62.078  1.000 82.032  0 95  VAL DDD CG2 1 ? 17 
ATOM   4202 N N   . TYR D 1 94  ? 7.958   15.481  59.719  1.000 77.041  0 96  TYR DDD N   1 ? 17 
ATOM   4203 C CA  . TYR D 1 94  ? 8.966   15.567  58.629  1.000 73.666  0 96  TYR DDD CA  1 ? 17 
ATOM   4204 C C   . TYR D 1 94  ? 9.644   14.204  58.444  1.000 70.283  0 96  TYR DDD C   1 ? 17 
ATOM   4205 O O   . TYR D 1 94  ? 10.267  13.702  59.399  1.000 70.679  0 96  TYR DDD O   1 ? 17 
ATOM   4206 C CB  . TYR D 1 94  ? 9.984   16.672  58.921  1.000 74.808  0 96  TYR DDD CB  1 ? 17 
ATOM   4207 C CG  . TYR D 1 94  ? 9.463   18.068  58.693  1.000 76.810  0 96  TYR DDD CG  1 ? 17 
ATOM   4208 C CD1 . TYR D 1 94  ? 8.543   18.636  59.557  1.000 79.915  0 96  TYR DDD CD1 1 ? 17 
ATOM   4209 C CD2 . TYR D 1 94  ? 9.885   18.822  57.611  1.000 76.584  0 96  TYR DDD CD2 1 ? 17 
ATOM   4210 C CE1 . TYR D 1 94  ? 8.054   19.916  59.352  1.000 82.167  0 96  TYR DDD CE1 1 ? 17 
ATOM   4211 C CE2 . TYR D 1 94  ? 9.413   20.106  57.394  1.000 78.810  0 96  TYR DDD CE2 1 ? 17 
ATOM   4212 C CZ  . TYR D 1 94  ? 8.494   20.656  58.270  1.000 81.446  0 96  TYR DDD CZ  1 ? 17 
ATOM   4213 O OH  . TYR D 1 94  ? 8.022   21.920  58.065  1.000 84.444  0 96  TYR DDD OH  1 ? 17 
ATOM   4214 N N   . TYR D 1 95  ? 9.512   13.627  57.245  1.000 67.981  0 97  TYR DDD N   1 ? 17 
ATOM   4215 C CA  . TYR D 1 95  ? 10.149  12.352  56.822  1.000 65.764  0 97  TYR DDD CA  1 ? 17 
ATOM   4216 C C   . TYR D 1 95  ? 11.321  12.655  55.883  1.000 64.128  0 97  TYR DDD C   1 ? 17 
ATOM   4217 O O   . TYR D 1 95  ? 11.140  13.428  54.926  1.000 62.914  0 97  TYR DDD O   1 ? 17 
ATOM   4218 C CB  . TYR D 1 95  ? 9.143   11.448  56.105  1.000 64.735  0 97  TYR DDD CB  1 ? 17 
ATOM   4219 C CG  . TYR D 1 95  ? 7.859   11.204  56.856  1.000 67.267  0 97  TYR DDD CG  1 ? 17 
ATOM   4220 C CD1 . TYR D 1 95  ? 6.815   12.114  56.793  1.000 68.800  0 97  TYR DDD CD1 1 ? 17 
ATOM   4221 C CD2 . TYR D 1 95  ? 7.679   10.061  57.622  1.000 67.438  0 97  TYR DDD CD2 1 ? 17 
ATOM   4222 C CE1 . TYR D 1 95  ? 5.631   11.903  57.478  1.000 71.201  0 97  TYR DDD CE1 1 ? 17 
ATOM   4223 C CE2 . TYR D 1 95  ? 6.503   9.837   58.318  1.000 69.356  0 97  TYR DDD CE2 1 ? 17 
ATOM   4224 C CZ  . TYR D 1 95  ? 5.473   10.759  58.240  1.000 71.618  0 97  TYR DDD CZ  1 ? 17 
ATOM   4225 O OH  . TYR D 1 95  ? 4.308   10.547  58.920  1.000 75.485  0 97  TYR DDD OH  1 ? 17 
ATOM   4226 N N   . CYS D 1 96  ? 12.488  12.071  56.151  1.000 63.862  0 98  CYS DDD N   1 ? 17 
ATOM   4227 C CA  . CYS D 1 96  ? 13.609  12.004  55.177  1.000 64.043  0 98  CYS DDD CA  1 ? 17 
ATOM   4228 C C   . CYS D 1 96  ? 13.372  10.757  54.312  1.000 59.845  0 98  CYS DDD C   1 ? 17 
ATOM   4229 O O   . CYS D 1 96  ? 12.801  9.769   54.830  1.000 58.499  0 98  CYS DDD O   1 ? 17 
ATOM   4230 C CB  . CYS D 1 96  ? 14.975  12.017  55.865  1.000 66.134  0 98  CYS DDD CB  1 ? 17 
ATOM   4231 S SG  . CYS D 1 96  ? 15.816  10.414  55.806  1.000 68.391  0 98  CYS DDD SG  1 ? 17 
ATOM   4232 N N   . ALA D 1 97  ? 13.732  10.816  53.031  1.000 57.419  0 99  ALA DDD N   1 ? 17 
ATOM   4233 C CA  . ALA D 1 97  ? 13.491  9.729   52.052  1.000 55.650  0 99  ALA DDD CA  1 ? 17 
ATOM   4234 C C   . ALA D 1 97  ? 14.712  9.563   51.148  1.000 53.219  0 99  ALA DDD C   1 ? 17 
ATOM   4235 O O   . ALA D 1 97  ? 15.370  10.578  50.839  1.000 53.221  0 99  ALA DDD O   1 ? 17 
ATOM   4236 C CB  . ALA D 1 97  ? 12.251  10.023  51.246  1.000 56.164  0 99  ALA DDD CB  1 ? 17 
ATOM   4237 N N   . ALA D 1 98  ? 14.983  8.320   50.742  1.000 51.577  0 100 ALA DDD N   1 ? 17 
ATOM   4238 C CA  . ALA D 1 98  ? 16.121  7.928   49.883  1.000 50.012  0 100 ALA DDD CA  1 ? 17 
ATOM   4239 C C   . ALA D 1 98  ? 15.591  7.359   48.566  1.000 49.181  0 100 ALA DDD C   1 ? 17 
ATOM   4240 O O   . ALA D 1 98  ? 14.771  6.424   48.617  1.000 48.334  0 100 ALA DDD O   1 ? 17 
ATOM   4241 C CB  . ALA D 1 98  ? 16.990  6.926   50.605  1.000 49.109  0 100 ALA DDD CB  1 ? 17 
ATOM   4242 N N   . SER D 1 99  ? 16.031  7.935   47.442  1.000 50.459  0 101 SER DDD N   1 ? 17 
ATOM   4243 C CA  . SER D 1 99  ? 15.892  7.385   46.069  1.000 48.539  0 101 SER DDD CA  1 ? 17 
ATOM   4244 C C   . SER D 1 99  ? 17.249  6.797   45.673  1.000 47.284  0 101 SER DDD C   1 ? 17 
ATOM   4245 O O   . SER D 1 99  ? 18.146  7.579   45.325  1.000 47.427  0 101 SER DDD O   1 ? 17 
ATOM   4246 C CB  . SER D 1 99  ? 15.411  8.440   45.098  1.000 49.199  0 101 SER DDD CB  1 ? 17 
ATOM   4247 O OG  . SER D 1 99  ? 15.011  7.859   43.861  1.000 49.433  0 101 SER DDD OG  1 ? 17 
ATOM   4248 N N   . VAL D 1 100 ? 17.398  5.475   45.781  1.000 47.008  0 102 VAL DDD N   1 ? 17 
ATOM   4249 C CA  . VAL D 1 100 ? 18.709  4.763   45.692  1.000 47.009  0 102 VAL DDD CA  1 ? 17 
ATOM   4250 C C   . VAL D 1 100 ? 19.115  4.620   44.222  1.000 45.176  0 102 VAL DDD C   1 ? 17 
ATOM   4251 O O   . VAL D 1 100 ? 18.223  4.447   43.372  1.000 47.892  0 102 VAL DDD O   1 ? 17 
ATOM   4252 C CB  . VAL D 1 100 ? 18.675  3.402   46.417  1.000 47.568  0 102 VAL DDD CB  1 ? 17 
ATOM   4253 C CG1 . VAL D 1 100 ? 18.309  3.568   47.885  1.000 49.132  0 102 VAL DDD CG1 1 ? 17 
ATOM   4254 C CG2 . VAL D 1 100 ? 17.750  2.396   45.746  1.000 46.769  0 102 VAL DDD CG2 1 ? 17 
ATOM   4255 N N   . GLY D 1 101 ? 20.419  4.701   43.952  1.000 44.761  0 103 GLY DDD N   1 ? 17 
ATOM   4256 C CA  . GLY D 1 101 ? 21.013  4.646   42.603  1.000 46.254  0 103 GLY DDD CA  1 ? 17 
ATOM   4257 C C   . GLY D 1 101 ? 20.326  5.597   41.637  1.000 47.395  0 103 GLY DDD C   1 ? 17 
ATOM   4258 O O   . GLY D 1 101 ? 20.198  5.227   40.466  1.000 47.671  0 103 GLY DDD O   1 ? 17 
ATOM   4259 N N   . ASN D 1 102 ? 19.901  6.773   42.115  1.000 48.660  0 104 ASN DDD N   1 ? 17 
ATOM   4260 C CA  . ASN D 1 102 ? 19.138  7.784   41.336  1.000 49.156  0 104 ASN DDD CA  1 ? 17 
ATOM   4261 C C   . ASN D 1 102 ? 20.008  9.034   41.175  1.000 50.264  0 104 ASN DDD C   1 ? 17 
ATOM   4262 O O   . ASN D 1 102 ? 20.290  9.701   42.194  1.000 50.144  0 104 ASN DDD O   1 ? 17 
ATOM   4263 C CB  . ASN D 1 102 ? 17.792  8.121   41.985  1.000 49.478  0 104 ASN DDD CB  1 ? 17 
ATOM   4264 C CG  . ASN D 1 102 ? 16.937  9.036   41.132  1.000 51.273  0 104 ASN DDD CG  1 ? 17 
ATOM   4265 O OD1 . ASN D 1 102 ? 17.328  9.413   40.031  1.000 51.866  0 104 ASN DDD OD1 1 ? 17 
ATOM   4266 N ND2 . ASN D 1 102 ? 15.770  9.409   41.631  1.000 52.407  0 104 ASN DDD ND2 1 ? 17 
ATOM   4267 N N   . TYR D 1 103 ? 20.393  9.337   39.932  1.000 50.721  0 105 TYR DDD N   1 ? 17 
ATOM   4268 C CA  . TYR D 1 103 ? 21.318  10.439  39.558  1.000 52.712  0 105 TYR DDD CA  1 ? 17 
ATOM   4269 C C   . TYR D 1 103 ? 20.511  11.659  39.094  1.000 52.905  0 105 TYR DDD C   1 ? 17 
ATOM   4270 O O   . TYR D 1 103 ? 21.105  12.575  38.492  1.000 52.389  0 105 TYR DDD O   1 ? 17 
ATOM   4271 C CB  . TYR D 1 103 ? 22.310  9.937   38.505  1.000 53.438  0 105 TYR DDD CB  1 ? 17 
ATOM   4272 C CG  . TYR D 1 103 ? 23.186  8.805   38.984  1.000 53.038  0 105 TYR DDD CG  1 ? 17 
ATOM   4273 C CD1 . TYR D 1 103 ? 24.410  9.049   39.588  1.000 54.890  0 105 TYR DDD CD1 1 ? 17 
ATOM   4274 C CD2 . TYR D 1 103 ? 22.780  7.486   38.863  1.000 51.473  0 105 TYR DDD CD2 1 ? 17 
ATOM   4275 C CE1 . TYR D 1 103 ? 25.215  8.014   40.039  1.000 54.549  0 105 TYR DDD CE1 1 ? 17 
ATOM   4276 C CE2 . TYR D 1 103 ? 23.571  6.439   39.306  1.000 51.427  0 105 TYR DDD CE2 1 ? 17 
ATOM   4277 C CZ  . TYR D 1 103 ? 24.793  6.703   39.897  1.000 53.039  0 105 TYR DDD CZ  1 ? 17 
ATOM   4278 O OH  . TYR D 1 103 ? 25.573  5.674   40.337  1.000 51.974  0 105 TYR DDD OH  1 ? 17 
ATOM   4279 N N   . GLY D 1 104 ? 19.207  11.677  39.396  1.000 53.098  0 106 GLY DDD N   1 ? 17 
ATOM   4280 C CA  . GLY D 1 104 ? 18.267  12.759  39.038  1.000 54.089  0 106 GLY DDD CA  1 ? 17 
ATOM   4281 C C   . GLY D 1 104 ? 17.900  13.618  40.238  1.000 54.721  0 106 GLY DDD C   1 ? 17 
ATOM   4282 O O   . GLY D 1 104 ? 18.656  13.604  41.232  1.000 54.481  0 106 GLY DDD O   1 ? 17 
ATOM   4283 N N   . LEU D 1 105 ? 16.773  14.331  40.152  1.000 54.777  0 107 LEU DDD N   1 ? 17 
ATOM   4284 C CA  . LEU D 1 105 ? 16.262  15.241  41.212  1.000 54.594  0 107 LEU DDD CA  1 ? 17 
ATOM   4285 C C   . LEU D 1 105 ? 14.794  14.916  41.485  1.000 53.909  0 107 LEU DDD C   1 ? 17 
ATOM   4286 O O   . LEU D 1 105 ? 13.899  15.632  41.044  1.000 55.411  0 107 LEU DDD O   1 ? 17 
ATOM   4287 C CB  . LEU D 1 105 ? 16.456  16.691  40.756  1.000 56.460  0 107 LEU DDD CB  1 ? 17 
ATOM   4288 C CG  . LEU D 1 105 ? 16.207  17.758  41.821  1.000 58.472  0 107 LEU DDD CG  1 ? 17 
ATOM   4289 C CD1 . LEU D 1 105 ? 17.091  17.527  43.044  1.000 58.363  0 107 LEU DDD CD1 1 ? 17 
ATOM   4290 C CD2 . LEU D 1 105 ? 16.436  19.151  41.253  1.000 61.037  0 107 LEU DDD CD2 1 ? 17 
ATOM   4291 N N   . PRO D 1 106 ? 14.507  13.816  42.215  1.000 52.462  0 108 PRO DDD N   1 ? 17 
ATOM   4292 C CA  . PRO D 1 106 ? 13.131  13.386  42.458  1.000 53.526  0 108 PRO DDD CA  1 ? 17 
ATOM   4293 C C   . PRO D 1 106 ? 12.386  14.301  43.439  1.000 56.179  0 108 PRO DDD C   1 ? 17 
ATOM   4294 O O   . PRO D 1 106 ? 13.024  14.821  44.330  1.000 57.245  0 108 PRO DDD O   1 ? 17 
ATOM   4295 C CB  . PRO D 1 106 ? 13.303  11.980  43.051  1.000 51.906  0 108 PRO DDD CB  1 ? 17 
ATOM   4296 C CG  . PRO D 1 106 ? 14.657  12.027  43.728  1.000 50.868  0 108 PRO DDD CG  1 ? 17 
ATOM   4297 C CD  . PRO D 1 106 ? 15.496  12.922  42.840  1.000 51.258  0 108 PRO DDD CD  1 ? 17 
ATOM   4298 N N   . TRP D 1 107 ? 11.076  14.481  43.235  1.000 59.316  0 109 TRP DDD N   1 ? 17 
ATOM   4299 C CA  . TRP D 1 107 ? 10.190  15.286  44.123  1.000 61.801  0 109 TRP DDD CA  1 ? 17 
ATOM   4300 C C   . TRP D 1 107 ? 8.824   14.613  44.331  1.000 62.441  0 109 TRP DDD C   1 ? 17 
ATOM   4301 O O   . TRP D 1 107 ? 8.061   15.128  45.168  1.000 67.354  0 109 TRP DDD O   1 ? 17 
ATOM   4302 C CB  . TRP D 1 107 ? 10.037  16.722  43.594  1.000 65.041  0 109 TRP DDD CB  1 ? 17 
ATOM   4303 C CG  . TRP D 1 107 ? 9.589   16.824  42.168  1.000 67.856  0 109 TRP DDD CG  1 ? 17 
ATOM   4304 C CD1 . TRP D 1 107 ? 10.380  16.969  41.063  1.000 68.120  0 109 TRP DDD CD1 1 ? 17 
ATOM   4305 C CD2 . TRP D 1 107 ? 8.231   16.826  41.688  1.000 70.454  0 109 TRP DDD CD2 1 ? 17 
ATOM   4306 N NE1 . TRP D 1 107 ? 9.611   17.047  39.931  1.000 69.888  0 109 TRP DDD NE1 1 ? 17 
ATOM   4307 C CE2 . TRP D 1 107 ? 8.290   16.963  40.282  1.000 71.579  0 109 TRP DDD CE2 1 ? 17 
ATOM   4308 C CE3 . TRP D 1 107 ? 6.978   16.717  42.303  1.000 71.470  0 109 TRP DDD CE3 1 ? 17 
ATOM   4309 C CZ2 . TRP D 1 107 ? 7.143   16.994  39.489  1.000 74.146  0 109 TRP DDD CZ2 1 ? 17 
ATOM   4310 C CZ3 . TRP D 1 107 ? 5.845   16.750  41.518  1.000 74.242  0 109 TRP DDD CZ3 1 ? 17 
ATOM   4311 C CH2 . TRP D 1 107 ? 5.929   16.886  40.131  1.000 75.541  0 109 TRP DDD CH2 1 ? 17 
ATOM   4312 N N   . ALA D 1 108 ? 8.516   13.522  43.623  1.000 60.165  0 110 ALA DDD N   1 ? 17 
ATOM   4313 C CA  . ALA D 1 108 ? 7.266   12.741  43.790  1.000 60.720  0 110 ALA DDD CA  1 ? 17 
ATOM   4314 C C   . ALA D 1 108 ? 7.527   11.564  44.739  1.000 58.531  0 110 ALA DDD C   1 ? 17 
ATOM   4315 O O   . ALA D 1 108 ? 8.612   10.969  44.651  1.000 56.465  0 110 ALA DDD O   1 ? 17 
ATOM   4316 C CB  . ALA D 1 108 ? 6.756   12.278  42.446  1.000 61.408  0 110 ALA DDD CB  1 ? 17 
ATOM   4317 N N   . HIS D 1 109 ? 6.565   11.245  45.611  1.000 59.945  0 111 HIS DDD N   1 ? 17 
ATOM   4318 C CA  . HIS D 1 109 ? 6.706   10.226  46.689  1.000 59.242  0 111 HIS DDD CA  1 ? 17 
ATOM   4319 C C   . HIS D 1 109 ? 7.070   8.858   46.091  1.000 56.872  0 111 HIS DDD C   1 ? 17 
ATOM   4320 O O   . HIS D 1 109 ? 7.941   8.181   46.670  1.000 54.994  0 111 HIS DDD O   1 ? 17 
ATOM   4321 C CB  . HIS D 1 109 ? 5.447   10.177  47.564  1.000 61.462  0 111 HIS DDD CB  1 ? 17 
ATOM   4322 C CG  . HIS D 1 109 ? 4.271   9.535   46.917  1.000 63.936  0 111 HIS DDD CG  1 ? 17 
ATOM   4323 N ND1 . HIS D 1 109 ? 3.349   10.263  46.184  1.000 68.798  0 111 HIS DDD ND1 1 ? 17 
ATOM   4324 C CD2 . HIS D 1 109 ? 3.835   8.258   46.919  1.000 64.981  0 111 HIS DDD CD2 1 ? 17 
ATOM   4325 C CE1 . HIS D 1 109 ? 2.399   9.458   45.747  1.000 69.602  0 111 HIS DDD CE1 1 ? 17 
ATOM   4326 N NE2 . HIS D 1 109 ? 2.670   8.222   46.190  1.000 69.233  0 111 HIS DDD NE2 1 ? 17 
ATOM   4327 N N   . PHE D 1 110 ? 6.461   8.479   44.964  1.000 56.489  0 112 PHE DDD N   1 ? 17 
ATOM   4328 C CA  . PHE D 1 110 ? 6.654   7.156   44.306  1.000 55.252  0 112 PHE DDD CA  1 ? 17 
ATOM   4329 C C   . PHE D 1 110 ? 8.076   7.016   43.736  1.000 53.064  0 112 PHE DDD C   1 ? 17 
ATOM   4330 O O   . PHE D 1 110 ? 8.467   5.873   43.435  1.000 51.271  0 112 PHE DDD O   1 ? 17 
ATOM   4331 C CB  . PHE D 1 110 ? 5.605   6.906   43.216  1.000 55.916  0 112 PHE DDD CB  1 ? 17 
ATOM   4332 C CG  . PHE D 1 110 ? 5.412   8.027   42.227  1.000 57.130  0 112 PHE DDD CG  1 ? 17 
ATOM   4333 C CD1 . PHE D 1 110 ? 6.365   8.295   41.255  1.000 56.550  0 112 PHE DDD CD1 1 ? 17 
ATOM   4334 C CD2 . PHE D 1 110 ? 4.268   8.810   42.261  1.000 59.713  0 112 PHE DDD CD2 1 ? 17 
ATOM   4335 C CE1 . PHE D 1 110 ? 6.185   9.329   40.349  1.000 57.368  0 112 PHE DDD CE1 1 ? 17 
ATOM   4336 C CE2 . PHE D 1 110 ? 4.089   9.843   41.356  1.000 61.394  0 112 PHE DDD CE2 1 ? 17 
ATOM   4337 C CZ  . PHE D 1 110 ? 5.049   10.100  40.402  1.000 60.603  0 112 PHE DDD CZ  1 ? 17 
ATOM   4338 N N   . GLU D 1 111 ? 8.824   8.116   43.588  1.000 53.409  0 113 GLU DDD N   1 ? 17 
ATOM   4339 C CA  . GLU D 1 111 ? 10.214  8.106   43.052  1.000 52.318  0 113 GLU DDD CA  1 ? 17 
ATOM   4340 C C   . GLU D 1 111 ? 11.211  7.749   44.160  1.000 51.171  0 113 GLU DDD C   1 ? 17 
ATOM   4341 O O   . GLU D 1 111 ? 12.382  7.503   43.824  1.000 52.825  0 113 GLU DDD O   1 ? 17 
ATOM   4342 C CB  . GLU D 1 111 ? 10.572  9.457   42.431  1.000 54.152  0 113 GLU DDD CB  1 ? 17 
ATOM   4343 C CG  . GLU D 1 111 ? 9.708   9.820   41.237  1.000 57.660  0 113 GLU DDD CG  1 ? 17 
ATOM   4344 C CD  . GLU D 1 111 ? 9.982   11.184  40.625  1.000 60.810  0 113 GLU DDD CD  1 ? 17 
ATOM   4345 O OE1 . GLU D 1 111 ? 10.199  12.153  41.385  1.000 62.066  0 113 GLU DDD OE1 1 ? 17 
ATOM   4346 O OE2 . GLU D 1 111 ? 9.942   11.280  39.388  1.000 65.048  0 113 GLU DDD OE2 1 ? 17 
ATOM   4347 N N   . TYR D 1 112 ? 10.772  7.716   45.422  1.000 50.790  0 114 TYR DDD N   1 ? 17 
ATOM   4348 C CA  . TYR D 1 112 ? 11.612  7.386   46.605  1.000 50.534  0 114 TYR DDD CA  1 ? 17 
ATOM   4349 C C   . TYR D 1 112 ? 11.354  5.934   47.027  1.000 48.651  0 114 TYR DDD C   1 ? 17 
ATOM   4350 O O   . TYR D 1 112 ? 10.260  5.423   46.763  1.000 51.029  0 114 TYR DDD O   1 ? 17 
ATOM   4351 C CB  . TYR D 1 112 ? 11.346  8.388   47.730  1.000 53.280  0 114 TYR DDD CB  1 ? 17 
ATOM   4352 C CG  . TYR D 1 112 ? 11.904  9.764   47.465  1.000 53.766  0 114 TYR DDD CG  1 ? 17 
ATOM   4353 C CD1 . TYR D 1 112 ? 11.252  10.661  46.632  1.000 54.551  0 114 TYR DDD CD1 1 ? 17 
ATOM   4354 C CD2 . TYR D 1 112 ? 13.103  10.160  48.029  1.000 54.417  0 114 TYR DDD CD2 1 ? 17 
ATOM   4355 C CE1 . TYR D 1 112 ? 11.769  11.920  46.374  1.000 55.057  0 114 TYR DDD CE1 1 ? 17 
ATOM   4356 C CE2 . TYR D 1 112 ? 13.631  11.418  47.789  1.000 55.381  0 114 TYR DDD CE2 1 ? 17 
ATOM   4357 C CZ  . TYR D 1 112 ? 12.963  12.302  46.959  1.000 55.584  0 114 TYR DDD CZ  1 ? 17 
ATOM   4358 O OH  . TYR D 1 112 ? 13.487  13.540  46.723  1.000 56.951  0 114 TYR DDD OH  1 ? 17 
ATOM   4359 N N   . ASP D 1 113 ? 12.344  5.305   47.662  1.000 47.189  0 115 ASP DDD N   1 ? 17 
ATOM   4360 C CA  . ASP D 1 113 ? 12.413  3.837   47.901  1.000 46.278  0 115 ASP DDD CA  1 ? 17 
ATOM   4361 C C   . ASP D 1 113 ? 12.344  3.526   49.399  1.000 45.907  0 115 ASP DDD C   1 ? 17 
ATOM   4362 O O   . ASP D 1 113 ? 11.695  2.530   49.752  1.000 45.956  0 115 ASP DDD O   1 ? 17 
ATOM   4363 C CB  . ASP D 1 113 ? 13.693  3.250   47.302  1.000 45.242  0 115 ASP DDD CB  1 ? 17 
ATOM   4364 C CG  . ASP D 1 113 ? 13.838  3.543   45.823  1.000 44.548  0 115 ASP DDD CG  1 ? 17 
ATOM   4365 O OD1 . ASP D 1 113 ? 12.965  3.109   45.054  1.000 46.951  0 115 ASP DDD OD1 1 ? 17 
ATOM   4366 O OD2 . ASP D 1 113 ? 14.802  4.227   45.459  1.000 44.392  0 115 ASP DDD OD2 1 ? 17 
ATOM   4367 N N   . PHE D 1 114 ? 13.015  4.317   50.239  1.000 45.949  0 116 PHE DDD N   1 ? 17 
ATOM   4368 C CA  . PHE D 1 114 ? 13.112  4.081   51.705  1.000 46.884  0 116 PHE DDD CA  1 ? 17 
ATOM   4369 C C   . PHE D 1 114 ? 12.749  5.368   52.445  1.000 47.932  0 116 PHE DDD C   1 ? 17 
ATOM   4370 O O   . PHE D 1 114 ? 13.078  6.468   51.946  1.000 47.437  0 116 PHE DDD O   1 ? 17 
ATOM   4371 C CB  . PHE D 1 114 ? 14.501  3.538   52.050  1.000 46.279  0 116 PHE DDD CB  1 ? 17 
ATOM   4372 C CG  . PHE D 1 114 ? 14.829  2.275   51.296  1.000 45.352  0 116 PHE DDD CG  1 ? 17 
ATOM   4373 C CD1 . PHE D 1 114 ? 14.302  1.058   51.698  1.000 45.601  0 116 PHE DDD CD1 1 ? 17 
ATOM   4374 C CD2 . PHE D 1 114 ? 15.608  2.315   50.150  1.000 44.377  0 116 PHE DDD CD2 1 ? 17 
ATOM   4375 C CE1 . PHE D 1 114 ? 14.575  -0.101  50.987  1.000 45.598  0 116 PHE DDD CE1 1 ? 17 
ATOM   4376 C CE2 . PHE D 1 114 ? 15.879  1.156   49.439  1.000 44.056  0 116 PHE DDD CE2 1 ? 17 
ATOM   4377 C CZ  . PHE D 1 114 ? 15.361  -0.049  49.859  1.000 44.728  0 116 PHE DDD CZ  1 ? 17 
ATOM   4378 N N   . TRP D 1 115 ? 12.078  5.213   53.593  1.000 50.273  0 117 TRP DDD N   1 ? 17 
ATOM   4379 C CA  . TRP D 1 115 ? 11.504  6.314   54.412  1.000 52.679  0 117 TRP DDD CA  1 ? 17 
ATOM   4380 C C   . TRP D 1 115 ? 11.933  6.163   55.872  1.000 55.346  0 117 TRP DDD C   1 ? 17 
ATOM   4381 O O   . TRP D 1 115 ? 11.967  5.023   56.368  1.000 55.944  0 117 TRP DDD O   1 ? 17 
ATOM   4382 C CB  . TRP D 1 115 ? 9.976   6.328   54.297  1.000 53.141  0 117 TRP DDD CB  1 ? 17 
ATOM   4383 C CG  . TRP D 1 115 ? 9.479   6.559   52.905  1.000 52.984  0 117 TRP DDD CG  1 ? 17 
ATOM   4384 C CD1 . TRP D 1 115 ? 9.347   5.630   51.914  1.000 51.482  0 117 TRP DDD CD1 1 ? 17 
ATOM   4385 C CD2 . TRP D 1 115 ? 9.058   7.813   52.341  1.000 53.924  0 117 TRP DDD CD2 1 ? 17 
ATOM   4386 N NE1 . TRP D 1 115 ? 8.870   6.219   50.775  1.000 52.028  0 117 TRP DDD NE1 1 ? 17 
ATOM   4387 C CE2 . TRP D 1 115 ? 8.681   7.556   51.006  1.000 52.737  0 117 TRP DDD CE2 1 ? 17 
ATOM   4388 C CE3 . TRP D 1 115 ? 8.961   9.122   52.829  1.000 55.527  0 117 TRP DDD CE3 1 ? 17 
ATOM   4389 C CZ2 . TRP D 1 115 ? 8.213   8.559   50.159  1.000 53.689  0 117 TRP DDD CZ2 1 ? 17 
ATOM   4390 C CZ3 . TRP D 1 115 ? 8.492   10.111  51.992  1.000 56.325  0 117 TRP DDD CZ3 1 ? 17 
ATOM   4391 C CH2 . TRP D 1 115 ? 8.129   9.832   50.673  1.000 54.982  0 117 TRP DDD CH2 1 ? 17 
ATOM   4392 N N   . GLY D 1 116 ? 12.232  7.283   56.531  1.000 58.736  0 118 GLY DDD N   1 ? 17 
ATOM   4393 C CA  . GLY D 1 116 ? 12.397  7.339   57.993  1.000 62.381  0 118 GLY DDD CA  1 ? 17 
ATOM   4394 C C   . GLY D 1 116 ? 11.052  7.226   58.684  1.000 65.970  0 118 GLY DDD C   1 ? 17 
ATOM   4395 O O   . GLY D 1 116 ? 10.024  7.312   57.984  1.000 65.170  0 118 GLY DDD O   1 ? 17 
ATOM   4396 N N   . GLN D 1 117 ? 11.062  7.040   60.006  1.000 71.481  0 119 GLN DDD N   1 ? 17 
ATOM   4397 C CA  . GLN D 1 117 ? 9.849   6.942   60.864  1.000 75.058  0 119 GLN DDD CA  1 ? 17 
ATOM   4398 C C   . GLN D 1 117 ? 9.125   8.293   60.862  1.000 74.116  0 119 GLN DDD C   1 ? 17 
ATOM   4399 O O   . GLN D 1 117 ? 7.887   8.302   61.025  1.000 76.005  0 119 GLN DDD O   1 ? 17 
ATOM   4400 C CB  . GLN D 1 117 ? 10.224  6.560   62.301  1.000 80.630  0 119 GLN DDD CB  1 ? 17 
ATOM   4401 C CG  . GLN D 1 117 ? 10.867  5.186   62.442  1.000 83.802  0 119 GLN DDD CG  1 ? 17 
ATOM   4402 C CD  . GLN D 1 117 ? 9.864   4.069   62.290  1.000 87.256  0 119 GLN DDD CD  1 ? 17 
ATOM   4403 O OE1 . GLN D 1 117 ? 8.937   3.935   63.087  1.000 91.982  0 119 GLN DDD OE1 1 ? 17 
ATOM   4404 N NE2 . GLN D 1 117 ? 10.045  3.253   61.262  1.000 86.462  0 119 GLN DDD NE2 1 ? 17 
ATOM   4405 N N   . GLY D 1 118 ? 9.881   9.385   60.704  1.000 71.566  0 120 GLY DDD N   1 ? 17 
ATOM   4406 C CA  . GLY D 1 118 ? 9.373   10.769  60.706  1.000 72.259  0 120 GLY DDD CA  1 ? 17 
ATOM   4407 C C   . GLY D 1 118 ? 9.465   11.384  62.089  1.000 74.541  0 120 GLY DDD C   1 ? 17 
ATOM   4408 O O   . GLY D 1 118 ? 9.195   10.667  63.070  1.000 75.654  0 120 GLY DDD O   1 ? 17 
ATOM   4409 N N   . ILE D 1 119 ? 9.833   12.665  62.162  1.000 75.241  0 121 ILE DDD N   1 ? 17 
ATOM   4410 C CA  . ILE D 1 119 ? 10.027  13.419  63.436  1.000 78.393  0 121 ILE DDD CA  1 ? 17 
ATOM   4411 C C   . ILE D 1 119 ? 9.064   14.609  63.457  1.000 79.377  0 121 ILE DDD C   1 ? 17 
ATOM   4412 O O   . ILE D 1 119 ? 8.909   15.276  62.415  1.000 77.405  0 121 ILE DDD O   1 ? 17 
ATOM   4413 C CB  . ILE D 1 119 ? 11.498  13.849  63.623  1.000 78.988  0 121 ILE DDD CB  1 ? 17 
ATOM   4414 C CG1 . ILE D 1 119 ? 12.105  14.423  62.339  1.000 77.331  0 121 ILE DDD CG1 1 ? 17 
ATOM   4415 C CG2 . ILE D 1 119 ? 12.328  12.694  64.165  1.000 78.952  0 121 ILE DDD CG2 1 ? 17 
ATOM   4416 C CD1 . ILE D 1 119 ? 13.411  15.150  62.553  1.000 79.345  0 121 ILE DDD CD1 1 ? 17 
ATOM   4417 N N   . GLN D 1 120 ? 8.435   14.842  64.611  1.000 82.332  0 122 GLN DDD N   1 ? 17 
ATOM   4418 C CA  . GLN D 1 120 ? 7.443   15.924  64.837  1.000 85.452  0 122 GLN DDD CA  1 ? 17 
ATOM   4419 C C   . GLN D 1 120 ? 8.193   17.256  64.968  1.000 86.847  0 122 GLN DDD C   1 ? 17 
ATOM   4420 O O   . GLN D 1 120 ? 9.120   17.337  65.797  1.000 88.557  0 122 GLN DDD O   1 ? 17 
ATOM   4421 C CB  . GLN D 1 120 ? 6.605   15.608  66.081  1.000 89.107  0 122 GLN DDD CB  1 ? 17 
ATOM   4422 C CG  . GLN D 1 120 ? 5.480   16.599  66.356  1.000 91.961  0 122 GLN DDD CG  1 ? 17 
ATOM   4423 C CD  . GLN D 1 120 ? 4.422   16.606  65.280  1.000 90.981  0 122 GLN DDD CD  1 ? 17 
ATOM   4424 O OE1 . GLN D 1 120 ? 4.142   17.637  64.674  1.000 91.381  0 122 GLN DDD OE1 1 ? 17 
ATOM   4425 N NE2 . GLN D 1 120 ? 3.813   15.455  65.045  1.000 90.082  0 122 GLN DDD NE2 1 ? 17 
ATOM   4426 N N   . VAL D 1 121 ? 7.818   18.241  64.149  1.000 86.536  0 123 VAL DDD N   1 ? 17 
ATOM   4427 C CA  . VAL D 1 121 ? 8.206   19.674  64.296  1.000 88.705  0 123 VAL DDD CA  1 ? 17 
ATOM   4428 C C   . VAL D 1 121 ? 6.920   20.459  64.575  1.000 91.469  0 123 VAL DDD C   1 ? 17 
ATOM   4429 O O   . VAL D 1 121 ? 6.044   20.471  63.690  1.000 90.481  0 123 VAL DDD O   1 ? 17 
ATOM   4430 C CB  . VAL D 1 121 ? 8.939   20.205  63.046  1.000 86.649  0 123 VAL DDD CB  1 ? 17 
ATOM   4431 C CG1 . VAL D 1 121 ? 9.264   21.689  63.170  1.000 89.661  0 123 VAL DDD CG1 1 ? 17 
ATOM   4432 C CG2 . VAL D 1 121 ? 10.199  19.406  62.744  1.000 83.627  0 123 VAL DDD CG2 1 ? 17 
ATOM   4433 N N   . THR D 1 122 ? 6.800   21.042  65.771  1.000 94.912  0 124 THR DDD N   1 ? 17 
ATOM   4434 C CA  . THR D 1 122 ? 5.653   21.885  66.201  1.000 98.767  0 124 THR DDD CA  1 ? 17 
ATOM   4435 C C   . THR D 1 122 ? 6.180   23.284  66.538  1.000 101.719 0 124 THR DDD C   1 ? 17 
ATOM   4436 O O   . THR D 1 122 ? 7.043   23.382  67.428  1.000 103.802 0 124 THR DDD O   1 ? 17 
ATOM   4437 C CB  . THR D 1 122 ? 4.894   21.244  67.373  1.000 100.926 0 124 THR DDD CB  1 ? 17 
ATOM   4438 O OG1 . THR D 1 122 ? 5.828   20.529  68.183  1.000 100.825 0 124 THR DDD OG1 1 ? 17 
ATOM   4439 C CG2 . THR D 1 122 ? 3.793   20.312  66.918  1.000 99.328  0 124 THR DDD CG2 1 ? 17 
ATOM   4440 N N   . VAL D 1 123 ? 5.654   24.312  65.864  1.000 102.483 0 125 VAL DDD N   1 ? 17 
ATOM   4441 C CA  . VAL D 1 123 ? 6.109   25.732  65.948  1.000 105.166 0 125 VAL DDD CA  1 ? 17 
ATOM   4442 C C   . VAL D 1 123 ? 5.191   26.496  66.914  1.000 109.034 0 125 VAL DDD C   1 ? 17 
ATOM   4443 O O   . VAL D 1 123 ? 4.011   26.739  66.661  1.000 109.806 0 125 VAL DDD O   1 ? 17 
ATOM   4444 C CB  . VAL D 1 123 ? 6.118   26.376  64.546  1.000 104.076 0 125 VAL DDD CB  1 ? 17 
ATOM   4445 C CG1 . VAL D 1 123 ? 6.528   27.840  64.586  1.000 107.823 0 125 VAL DDD CG1 1 ? 17 
ATOM   4446 C CG2 . VAL D 1 123 ? 6.991   25.601  63.573  1.000 99.655  0 125 VAL DDD CG2 1 ? 17 
ATOM   4447 N N   . ASN E 2 5   ? 27.938  13.908  13.918  1.000 98.311  0 334 ASN EEE N   1 ? 18 
ATOM   4448 C CA  . ASN E 2 5   ? 28.818  12.946  14.646  1.000 95.924  0 334 ASN EEE CA  1 ? 18 
ATOM   4449 C C   . ASN E 2 5   ? 28.248  12.668  16.046  1.000 91.503  0 334 ASN EEE C   1 ? 18 
ATOM   4450 O O   . ASN E 2 5   ? 28.520  11.578  16.578  1.000 88.484  0 334 ASN EEE O   1 ? 18 
ATOM   4451 C CB  . ASN E 2 5   ? 30.261  13.459  14.719  1.000 99.152  0 334 ASN EEE CB  1 ? 18 
ATOM   4452 C CG  . ASN E 2 5   ? 31.291  12.353  14.837  1.000 99.951  0 334 ASN EEE CG  1 ? 18 
ATOM   4453 O OD1 . ASN E 2 5   ? 31.018  11.202  14.503  1.000 101.657 0 334 ASN EEE OD1 1 ? 18 
ATOM   4454 N ND2 . ASN E 2 5   ? 32.485  12.688  15.302  1.000 100.801 0 334 ASN EEE ND2 1 ? 18 
ATOM   4455 N N   . LEU E 2 6   ? 27.515  13.627  16.621  1.000 90.417  0 335 LEU EEE N   1 ? 18 
ATOM   4456 C CA  . LEU E 2 6   ? 26.859  13.540  17.954  1.000 87.284  0 335 LEU EEE CA  1 ? 18 
ATOM   4457 C C   . LEU E 2 6   ? 25.689  12.550  17.889  1.000 83.971  0 335 LEU EEE C   1 ? 18 
ATOM   4458 O O   . LEU E 2 6   ? 24.920  12.624  16.913  1.000 85.590  0 335 LEU EEE O   1 ? 18 
ATOM   4459 C CB  . LEU E 2 6   ? 26.369  14.943  18.336  1.000 89.145  0 335 LEU EEE CB  1 ? 18 
ATOM   4460 C CG  . LEU E 2 6   ? 26.165  15.208  19.826  1.000 87.926  0 335 LEU EEE CG  1 ? 18 
ATOM   4461 C CD1 . LEU E 2 6   ? 26.288  16.698  20.120  1.000 90.360  0 335 LEU EEE CD1 1 ? 18 
ATOM   4462 C CD2 . LEU E 2 6   ? 24.822  14.679  20.308  1.000 85.807  0 335 LEU EEE CD2 1 ? 18 
ATOM   4463 N N   . CYS E 2 7   ? 25.556  11.670  18.890  1.000 80.678  0 336 CYS EEE N   1 ? 18 
ATOM   4464 C CA  . CYS E 2 7   ? 24.444  10.682  19.002  1.000 78.106  0 336 CYS EEE CA  1 ? 18 
ATOM   4465 C C   . CYS E 2 7   ? 23.113  11.426  19.090  1.000 78.391  0 336 CYS EEE C   1 ? 18 
ATOM   4466 O O   . CYS E 2 7   ? 22.998  12.398  19.829  1.000 76.533  0 336 CYS EEE O   1 ? 18 
ATOM   4467 C CB  . CYS E 2 7   ? 24.602  9.767   20.213  1.000 74.115  0 336 CYS EEE CB  1 ? 18 
ATOM   4468 S SG  . CYS E 2 7   ? 26.009  8.626   20.117  1.000 73.415  0 336 CYS EEE SG  1 ? 18 
ATOM   4469 N N   . PRO E 2 8   ? 22.071  10.999  18.339  1.000 81.050  0 337 PRO EEE N   1 ? 18 
ATOM   4470 C CA  . PRO E 2 8   ? 20.797  11.727  18.287  1.000 82.336  0 337 PRO EEE CA  1 ? 18 
ATOM   4471 C C   . PRO E 2 8   ? 19.829  11.435  19.452  1.000 79.121  0 337 PRO EEE C   1 ? 18 
ATOM   4472 O O   . PRO E 2 8   ? 18.701  11.014  19.211  1.000 77.669  0 337 PRO EEE O   1 ? 18 
ATOM   4473 C CB  . PRO E 2 8   ? 20.228  11.245  16.943  1.000 82.909  0 337 PRO EEE CB  1 ? 18 
ATOM   4474 C CG  . PRO E 2 8   ? 20.684  9.805   16.865  1.000 81.318  0 337 PRO EEE CG  1 ? 18 
ATOM   4475 C CD  . PRO E 2 8   ? 22.072  9.806   17.474  1.000 80.694  0 337 PRO EEE CD  1 ? 18 
ATOM   4476 N N   . PHE E 2 9   ? 20.275  11.688  20.686  1.000 79.100  0 338 PHE EEE N   1 ? 18 
ATOM   4477 C CA  . PHE E 2 9   ? 19.463  11.557  21.925  1.000 78.022  0 338 PHE EEE CA  1 ? 18 
ATOM   4478 C C   . PHE E 2 9   ? 18.311  12.570  21.893  1.000 78.237  0 338 PHE EEE C   1 ? 18 
ATOM   4479 O O   . PHE E 2 9   ? 17.230  12.260  22.422  1.000 79.645  0 338 PHE EEE O   1 ? 18 
ATOM   4480 C CB  . PHE E 2 9   ? 20.317  11.765  23.180  1.000 78.966  0 338 PHE EEE CB  1 ? 18 
ATOM   4481 C CG  . PHE E 2 9   ? 21.283  10.653  23.498  1.000 79.598  0 338 PHE EEE CG  1 ? 18 
ATOM   4482 C CD1 . PHE E 2 9   ? 20.863  9.332   23.548  1.000 78.896  0 338 PHE EEE CD1 1 ? 18 
ATOM   4483 C CD2 . PHE E 2 9   ? 22.612  10.934  23.778  1.000 82.710  0 338 PHE EEE CD2 1 ? 18 
ATOM   4484 C CE1 . PHE E 2 9   ? 21.755  8.315   23.855  1.000 79.570  0 338 PHE EEE CE1 1 ? 18 
ATOM   4485 C CE2 . PHE E 2 9   ? 23.503  9.917   24.090  1.000 83.475  0 338 PHE EEE CE2 1 ? 18 
ATOM   4486 C CZ  . PHE E 2 9   ? 23.073  8.609   24.127  1.000 82.908  0 338 PHE EEE CZ  1 ? 18 
ATOM   4487 N N   . GLY E 2 10  ? 18.549  13.751  21.312  1.000 79.608  0 339 GLY EEE N   1 ? 18 
ATOM   4488 C CA  . GLY E 2 10  ? 17.538  14.806  21.118  1.000 80.575  0 339 GLY EEE CA  1 ? 18 
ATOM   4489 C C   . GLY E 2 10  ? 16.263  14.253  20.507  1.000 79.520  0 339 GLY EEE C   1 ? 18 
ATOM   4490 O O   . GLY E 2 10  ? 15.179  14.562  21.040  1.000 77.277  0 339 GLY EEE O   1 ? 18 
ATOM   4491 N N   . GLU E 2 11  ? 16.388  13.447  19.445  1.000 81.130  0 340 GLU EEE N   1 ? 18 
ATOM   4492 C CA  . GLU E 2 11  ? 15.244  12.825  18.719  1.000 82.571  0 340 GLU EEE CA  1 ? 18 
ATOM   4493 C C   . GLU E 2 11  ? 14.422  11.965  19.686  1.000 77.435  0 340 GLU EEE C   1 ? 18 
ATOM   4494 O O   . GLU E 2 11  ? 13.186  11.957  19.569  1.000 75.638  0 340 GLU EEE O   1 ? 18 
ATOM   4495 C CB  . GLU E 2 11  ? 15.734  11.977  17.543  1.000 85.776  0 340 GLU EEE CB  1 ? 18 
ATOM   4496 C CG  . GLU E 2 11  ? 16.263  12.801  16.382  1.000 92.321  0 340 GLU EEE CG  1 ? 18 
ATOM   4497 C CD  . GLU E 2 11  ? 16.898  11.989  15.264  1.000 96.500  0 340 GLU EEE CD  1 ? 18 
ATOM   4498 O OE1 . GLU E 2 11  ? 16.642  10.767  15.209  1.000 97.470  0 340 GLU EEE OE1 1 ? 18 
ATOM   4499 O OE2 . GLU E 2 11  ? 17.641  12.582  14.448  1.000 98.450  0 340 GLU EEE OE2 1 ? 18 
ATOM   4500 N N   . VAL E 2 12  ? 15.096  11.269  20.600  1.000 75.185  0 341 VAL EEE N   1 ? 18 
ATOM   4501 C CA  . VAL E 2 12  ? 14.465  10.328  21.572  1.000 71.630  0 341 VAL EEE CA  1 ? 18 
ATOM   4502 C C   . VAL E 2 12  ? 13.809  11.145  22.692  1.000 70.476  0 341 VAL EEE C   1 ? 18 
ATOM   4503 O O   . VAL E 2 12  ? 12.575  11.020  22.877  1.000 69.818  0 341 VAL EEE O   1 ? 18 
ATOM   4504 C CB  . VAL E 2 12  ? 15.495  9.327   22.130  1.000 70.474  0 341 VAL EEE CB  1 ? 18 
ATOM   4505 C CG1 . VAL E 2 12  ? 14.853  8.367   23.120  1.000 68.173  0 341 VAL EEE CG1 1 ? 18 
ATOM   4506 C CG2 . VAL E 2 12  ? 16.215  8.571   21.022  1.000 71.185  0 341 VAL EEE CG2 1 ? 18 
ATOM   4507 N N   . PHE E 2 13  ? 14.603  11.956  23.398  1.000 70.911  0 342 PHE EEE N   1 ? 18 
ATOM   4508 C CA  . PHE E 2 13  ? 14.198  12.672  24.638  1.000 71.343  0 342 PHE EEE CA  1 ? 18 
ATOM   4509 C C   . PHE E 2 13  ? 13.195  13.787  24.320  1.000 73.742  0 342 PHE EEE C   1 ? 18 
ATOM   4510 O O   . PHE E 2 13  ? 12.297  14.010  25.154  1.000 72.319  0 342 PHE EEE O   1 ? 18 
ATOM   4511 C CB  . PHE E 2 13  ? 15.426  13.211  25.380  1.000 71.202  0 342 PHE EEE CB  1 ? 18 
ATOM   4512 C CG  . PHE E 2 13  ? 16.182  12.161  26.156  1.000 68.961  0 342 PHE EEE CG  1 ? 18 
ATOM   4513 C CD1 . PHE E 2 13  ? 17.215  11.449  25.567  1.000 68.948  0 342 PHE EEE CD1 1 ? 18 
ATOM   4514 C CD2 . PHE E 2 13  ? 15.843  11.866  27.469  1.000 66.751  0 342 PHE EEE CD2 1 ? 18 
ATOM   4515 C CE1 . PHE E 2 13  ? 17.897  10.472  26.276  1.000 66.915  0 342 PHE EEE CE1 1 ? 18 
ATOM   4516 C CE2 . PHE E 2 13  ? 16.526  10.886  28.174  1.000 65.054  0 342 PHE EEE CE2 1 ? 18 
ATOM   4517 C CZ  . PHE E 2 13  ? 17.550  10.190  27.575  1.000 64.701  0 342 PHE EEE CZ  1 ? 18 
ATOM   4518 N N   . ASN E 2 14  ? 13.331  14.444  23.161  1.000 78.067  0 343 ASN EEE N   1 ? 18 
ATOM   4519 C CA  . ASN E 2 14  ? 12.575  15.678  22.806  1.000 81.053  0 343 ASN EEE CA  1 ? 18 
ATOM   4520 C C   . ASN E 2 14  ? 11.574  15.410  21.672  1.000 77.619  0 343 ASN EEE C   1 ? 18 
ATOM   4521 O O   . ASN E 2 14  ? 11.026  16.396  21.142  1.000 78.081  0 343 ASN EEE O   1 ? 18 
ATOM   4522 C CB  . ASN E 2 14  ? 13.530  16.827  22.465  1.000 87.896  0 343 ASN EEE CB  1 ? 18 
ATOM   4523 C CG  . ASN E 2 14  ? 14.057  17.542  23.691  1.000 93.777  0 343 ASN EEE CG  1 ? 18 
ATOM   4524 O OD1 . ASN E 2 14  ? 13.338  17.696  24.678  1.000 91.002  0 343 ASN EEE OD1 1 ? 18 
ATOM   4525 N ND2 . ASN E 2 14  ? 15.304  17.987  23.634  1.000 107.123 0 343 ASN EEE ND2 1 ? 18 
ATOM   4526 N N   . ALA E 2 15  ? 11.319  14.142  21.329  1.000 73.311  0 344 ALA EEE N   1 ? 18 
ATOM   4527 C CA  . ALA E 2 15  ? 10.240  13.729  20.399  1.000 72.621  0 344 ALA EEE CA  1 ? 18 
ATOM   4528 C C   . ALA E 2 15  ? 8.933   14.410  20.820  1.000 73.298  0 344 ALA EEE C   1 ? 18 
ATOM   4529 O O   . ALA E 2 15  ? 8.658   14.473  22.033  1.000 71.135  0 344 ALA EEE O   1 ? 18 
ATOM   4530 C CB  . ALA E 2 15  ? 10.093  12.228  20.391  1.000 69.874  0 344 ALA EEE CB  1 ? 18 
ATOM   4531 N N   . THR E 2 16  ? 8.153   14.910  19.860  1.000 76.974  0 345 THR EEE N   1 ? 18 
ATOM   4532 C CA  . THR E 2 16  ? 6.922   15.700  20.133  1.000 78.456  0 345 THR EEE CA  1 ? 18 
ATOM   4533 C C   . THR E 2 16  ? 5.855   14.759  20.710  1.000 76.262  0 345 THR EEE C   1 ? 18 
ATOM   4534 O O   . THR E 2 16  ? 5.143   15.191  21.638  1.000 76.715  0 345 THR EEE O   1 ? 18 
ATOM   4535 C CB  . THR E 2 16  ? 6.461   16.483  18.895  1.000 81.035  0 345 THR EEE CB  1 ? 18 
ATOM   4536 O OG1 . THR E 2 16  ? 5.851   15.568  17.985  1.000 82.325  0 345 THR EEE OG1 1 ? 18 
ATOM   4537 C CG2 . THR E 2 16  ? 7.588   17.225  18.209  1.000 83.088  0 345 THR EEE CG2 1 ? 18 
ATOM   4538 N N   . ARG E 2 17  ? 5.766   13.526  20.188  1.000 74.790  0 346 ARG EEE N   1 ? 18 
ATOM   4539 C CA  . ARG E 2 17  ? 4.906   12.435  20.729  1.000 72.600  0 346 ARG EEE CA  1 ? 18 
ATOM   4540 C C   . ARG E 2 17  ? 5.780   11.240  21.118  1.000 66.640  0 346 ARG EEE C   1 ? 18 
ATOM   4541 O O   . ARG E 2 17  ? 6.792   11.005  20.437  1.000 66.656  0 346 ARG EEE O   1 ? 18 
ATOM   4542 C CB  . ARG E 2 17  ? 3.844   11.995  19.716  1.000 76.632  0 346 ARG EEE CB  1 ? 18 
ATOM   4543 C CG  . ARG E 2 17  ? 2.599   11.398  20.360  1.000 79.140  0 346 ARG EEE CG  1 ? 18 
ATOM   4544 C CD  . ARG E 2 17  ? 1.360   11.449  19.478  1.000 83.968  0 346 ARG EEE CD  1 ? 18 
ATOM   4545 N NE  . ARG E 2 17  ? 1.244   10.274  18.622  1.000 87.802  0 346 ARG EEE NE  1 ? 18 
ATOM   4546 C CZ  . ARG E 2 17  ? 1.814   10.125  17.425  1.000 91.693  0 346 ARG EEE CZ  1 ? 18 
ATOM   4547 N NH1 . ARG E 2 17  ? 2.564   11.082  16.900  1.000 94.484  0 346 ARG EEE NH1 1 ? 18 
ATOM   4548 N NH2 . ARG E 2 17  ? 1.632   9.001   16.752  1.000 92.756  0 346 ARG EEE NH2 1 ? 18 
ATOM   4549 N N   . PHE E 2 18  ? 5.399   10.525  22.179  1.000 61.079  0 347 PHE EEE N   1 ? 18 
ATOM   4550 C CA  . PHE E 2 18  ? 6.033   9.254   22.618  1.000 57.943  0 347 PHE EEE CA  1 ? 18 
ATOM   4551 C C   . PHE E 2 18  ? 5.112   8.083   22.252  1.000 55.791  0 347 PHE EEE C   1 ? 18 
ATOM   4552 O O   . PHE E 2 18  ? 3.922   8.299   21.985  1.000 57.365  0 347 PHE EEE O   1 ? 18 
ATOM   4553 C CB  . PHE E 2 18  ? 6.352   9.297   24.116  1.000 55.822  0 347 PHE EEE CB  1 ? 18 
ATOM   4554 C CG  . PHE E 2 18  ? 7.746   9.768   24.460  1.000 55.939  0 347 PHE EEE CG  1 ? 18 
ATOM   4555 C CD1 . PHE E 2 18  ? 8.301   10.882  23.846  1.000 57.502  0 347 PHE EEE CD1 1 ? 18 
ATOM   4556 C CD2 . PHE E 2 18  ? 8.503   9.106   25.418  1.000 54.287  0 347 PHE EEE CD2 1 ? 18 
ATOM   4557 C CE1 . PHE E 2 18  ? 9.582   11.311  24.171  1.000 58.114  0 347 PHE EEE CE1 1 ? 18 
ATOM   4558 C CE2 . PHE E 2 18  ? 9.783   9.534   25.741  1.000 54.244  0 347 PHE EEE CE2 1 ? 18 
ATOM   4559 C CZ  . PHE E 2 18  ? 10.318  10.640  25.121  1.000 56.369  0 347 PHE EEE CZ  1 ? 18 
ATOM   4560 N N   . ALA E 2 19  ? 5.662   6.870   22.236  1.000 53.636  0 348 ALA EEE N   1 ? 18 
ATOM   4561 C CA  . ALA E 2 19  ? 4.931   5.606   21.995  1.000 52.258  0 348 ALA EEE CA  1 ? 18 
ATOM   4562 C C   . ALA E 2 19  ? 4.066   5.276   23.215  1.000 50.531  0 348 ALA EEE C   1 ? 18 
ATOM   4563 O O   . ALA E 2 19  ? 4.476   5.615   24.341  1.000 51.008  0 348 ALA EEE O   1 ? 18 
ATOM   4564 C CB  . ALA E 2 19  ? 5.911   4.491   21.718  1.000 51.499  0 348 ALA EEE CB  1 ? 18 
ATOM   4565 N N   . SER E 2 20  ? 2.927   4.618   22.996  1.000 49.200  0 349 SER EEE N   1 ? 18 
ATOM   4566 C CA  . SER E 2 20  ? 2.200   3.846   24.036  1.000 47.714  0 349 SER EEE CA  1 ? 18 
ATOM   4567 C C   . SER E 2 20  ? 3.128   2.750   24.567  1.000 46.591  0 349 SER EEE C   1 ? 18 
ATOM   4568 O O   . SER E 2 20  ? 3.891   2.181   23.764  1.000 46.599  0 349 SER EEE O   1 ? 18 
ATOM   4569 C CB  . SER E 2 20  ? 0.918   3.261   23.514  1.000 48.015  0 349 SER EEE CB  1 ? 18 
ATOM   4570 O OG  . SER E 2 20  ? -0.127  4.216   23.562  1.000 48.941  0 349 SER EEE OG  1 ? 18 
ATOM   4571 N N   . VAL E 2 21  ? 3.066   2.469   25.869  1.000 45.323  0 350 VAL EEE N   1 ? 18 
ATOM   4572 C CA  . VAL E 2 21  ? 3.987   1.513   26.551  1.000 44.553  0 350 VAL EEE CA  1 ? 18 
ATOM   4573 C C   . VAL E 2 21  ? 3.854   0.115   25.921  1.000 44.689  0 350 VAL EEE C   1 ? 18 
ATOM   4574 O O   . VAL E 2 21  ? 4.893   -0.557  25.781  1.000 44.814  0 350 VAL EEE O   1 ? 18 
ATOM   4575 C CB  . VAL E 2 21  ? 3.764   1.503   28.077  1.000 43.554  0 350 VAL EEE CB  1 ? 18 
ATOM   4576 C CG1 . VAL E 2 21  ? 2.388   0.973   28.461  1.000 43.440  0 350 VAL EEE CG1 1 ? 18 
ATOM   4577 C CG2 . VAL E 2 21  ? 4.863   0.737   28.801  1.000 42.434  0 350 VAL EEE CG2 1 ? 18 
ATOM   4578 N N   . TYR E 2 22  ? 2.649   -0.317  25.537  1.000 44.933  0 351 TYR EEE N   1 ? 18 
ATOM   4579 C CA  . TYR E 2 22  ? 2.414   -1.671  24.961  1.000 45.848  0 351 TYR EEE CA  1 ? 18 
ATOM   4580 C C   . TYR E 2 22  ? 3.162   -1.789  23.624  1.000 47.125  0 351 TYR EEE C   1 ? 18 
ATOM   4581 O O   . TYR E 2 22  ? 3.701   -2.875  23.336  1.000 47.550  0 351 TYR EEE O   1 ? 18 
ATOM   4582 C CB  . TYR E 2 22  ? 0.922   -1.975  24.803  1.000 45.955  0 351 TYR EEE CB  1 ? 18 
ATOM   4583 C CG  . TYR E 2 22  ? 0.299   -1.489  23.521  1.000 47.503  0 351 TYR EEE CG  1 ? 18 
ATOM   4584 C CD1 . TYR E 2 22  ? -0.228  -0.211  23.420  1.000 48.040  0 351 TYR EEE CD1 1 ? 18 
ATOM   4585 C CD2 . TYR E 2 22  ? 0.230   -2.309  22.408  1.000 48.561  0 351 TYR EEE CD2 1 ? 18 
ATOM   4586 C CE1 . TYR E 2 22  ? -0.798  0.245   22.244  1.000 49.532  0 351 TYR EEE CE1 1 ? 18 
ATOM   4587 C CE2 . TYR E 2 22  ? -0.340  -1.869  21.224  1.000 50.298  0 351 TYR EEE CE2 1 ? 18 
ATOM   4588 C CZ  . TYR E 2 22  ? -0.856  -0.588  21.141  1.000 50.691  0 351 TYR EEE CZ  1 ? 18 
ATOM   4589 O OH  . TYR E 2 22  ? -1.428  -0.151  19.980  1.000 52.424  0 351 TYR EEE OH  1 ? 18 
ATOM   4590 N N   . ALA E 2 23  ? 3.193   -0.707  22.842  1.000 48.003  0 352 ALA EEE N   1 ? 18 
ATOM   4591 C CA  . ALA E 2 23  ? 3.904   -0.618  21.544  1.000 49.681  0 352 ALA EEE CA  1 ? 18 
ATOM   4592 C C   . ALA E 2 23  ? 5.172   0.228   21.714  1.000 49.382  0 352 ALA EEE C   1 ? 18 
ATOM   4593 O O   . ALA E 2 23  ? 5.444   1.084   20.856  1.000 50.026  0 352 ALA EEE O   1 ? 18 
ATOM   4594 C CB  . ALA E 2 23  ? 2.974   -0.053  20.495  1.000 50.927  0 352 ALA EEE CB  1 ? 18 
ATOM   4595 N N   . TRP E 2 24  ? 5.925   -0.015  22.787  1.000 49.009  0 353 TRP EEE N   1 ? 18 
ATOM   4596 C CA  . TRP E 2 24  ? 7.115   0.792   23.168  1.000 49.487  0 353 TRP EEE CA  1 ? 18 
ATOM   4597 C C   . TRP E 2 24  ? 8.096   0.872   21.996  1.000 50.513  0 353 TRP EEE C   1 ? 18 
ATOM   4598 O O   . TRP E 2 24  ? 8.252   -0.125  21.259  1.000 49.832  0 353 TRP EEE O   1 ? 18 
ATOM   4599 C CB  . TRP E 2 24  ? 7.793   0.259   24.436  1.000 48.844  0 353 TRP EEE CB  1 ? 18 
ATOM   4600 C CG  . TRP E 2 24  ? 8.184   -1.186  24.423  1.000 49.387  0 353 TRP EEE CG  1 ? 18 
ATOM   4601 C CD1 . TRP E 2 24  ? 7.422   -2.249  24.814  1.000 49.418  0 353 TRP EEE CD1 1 ? 18 
ATOM   4602 C CD2 . TRP E 2 24  ? 9.469   -1.727  24.073  1.000 51.002  0 353 TRP EEE CD2 1 ? 18 
ATOM   4603 N NE1 . TRP E 2 24  ? 8.132   -3.414  24.708  1.000 50.041  0 353 TRP EEE NE1 1 ? 18 
ATOM   4604 C CE2 . TRP E 2 24  ? 9.393   -3.125  24.258  1.000 51.318  0 353 TRP EEE CE2 1 ? 18 
ATOM   4605 C CE3 . TRP E 2 24  ? 10.672  -1.171  23.627  1.000 52.140  0 353 TRP EEE CE3 1 ? 18 
ATOM   4606 C CZ2 . TRP E 2 24  ? 10.473  -3.970  24.009  1.000 51.749  0 353 TRP EEE CZ2 1 ? 18 
ATOM   4607 C CZ3 . TRP E 2 24  ? 11.737  -2.010  23.377  1.000 53.167  0 353 TRP EEE CZ3 1 ? 18 
ATOM   4608 C CH2 . TRP E 2 24  ? 11.636  -3.388  23.569  1.000 52.580  0 353 TRP EEE CH2 1 ? 18 
ATOM   4609 N N   . ASN E 2 25  ? 8.718   2.039   21.837  1.000 51.560  0 354 ASN EEE N   1 ? 18 
ATOM   4610 C CA  . ASN E 2 25  ? 9.660   2.341   20.734  1.000 53.887  0 354 ASN EEE CA  1 ? 18 
ATOM   4611 C C   . ASN E 2 25  ? 11.079  1.980   21.181  1.000 53.780  0 354 ASN EEE C   1 ? 18 
ATOM   4612 O O   . ASN E 2 25  ? 11.391  2.204   22.362  1.000 52.257  0 354 ASN EEE O   1 ? 18 
ATOM   4613 C CB  . ASN E 2 25  ? 9.541   3.799   20.294  1.000 55.513  0 354 ASN EEE CB  1 ? 18 
ATOM   4614 C CG  . ASN E 2 25  ? 10.276  4.061   18.999  1.000 57.978  0 354 ASN EEE CG  1 ? 18 
ATOM   4615 O OD1 . ASN E 2 25  ? 11.479  4.308   19.008  1.000 59.020  0 354 ASN EEE OD1 1 ? 18 
ATOM   4616 N ND2 . ASN E 2 25  ? 9.563   4.007   17.885  1.000 58.818  0 354 ASN EEE ND2 1 ? 18 
ATOM   4617 N N   . ARG E 2 26  ? 11.883  1.431   20.266  1.000 56.301  0 355 ARG EEE N   1 ? 18 
ATOM   4618 C CA  . ARG E 2 26  ? 13.335  1.159   20.439  1.000 57.880  0 355 ARG EEE CA  1 ? 18 
ATOM   4619 C C   . ARG E 2 26  ? 14.093  1.855   19.305  1.000 60.678  0 355 ARG EEE C   1 ? 18 
ATOM   4620 O O   . ARG E 2 26  ? 13.797  1.548   18.136  1.000 60.168  0 355 ARG EEE O   1 ? 18 
ATOM   4621 C CB  . ARG E 2 26  ? 13.636  -0.345  20.413  1.000 58.735  0 355 ARG EEE CB  1 ? 18 
ATOM   4622 C CG  . ARG E 2 26  ? 15.109  -0.688  20.593  1.000 59.638  0 355 ARG EEE CG  1 ? 18 
ATOM   4623 C CD  . ARG E 2 26  ? 15.405  -2.172  20.463  1.000 61.325  0 355 ARG EEE CD  1 ? 18 
ATOM   4624 N NE  . ARG E 2 26  ? 14.989  -2.974  21.607  1.000 61.367  0 355 ARG EEE NE  1 ? 18 
ATOM   4625 C CZ  . ARG E 2 26  ? 15.583  -2.980  22.792  1.000 61.930  0 355 ARG EEE CZ  1 ? 18 
ATOM   4626 N NH1 . ARG E 2 26  ? 16.615  -2.198  23.013  1.000 64.290  0 355 ARG EEE NH1 1 ? 18 
ATOM   4627 N NH2 . ARG E 2 26  ? 15.137  -3.741  23.773  1.000 63.436  0 355 ARG EEE NH2 1 ? 18 
ATOM   4628 N N   . LYS E 2 27  ? 15.009  2.764   19.648  1.000 62.665  0 356 LYS EEE N   1 ? 18 
ATOM   4629 C CA  . LYS E 2 27  ? 15.998  3.351   18.709  1.000 65.069  0 356 LYS EEE CA  1 ? 18 
ATOM   4630 C C   . LYS E 2 27  ? 17.365  2.745   19.034  1.000 65.221  0 356 LYS EEE C   1 ? 18 
ATOM   4631 O O   . LYS E 2 27  ? 17.828  2.931   20.177  1.000 62.631  0 356 LYS EEE O   1 ? 18 
ATOM   4632 C CB  . LYS E 2 27  ? 16.029  4.879   18.818  1.000 67.344  0 356 LYS EEE CB  1 ? 18 
ATOM   4633 C CG  . LYS E 2 27  ? 16.988  5.552   17.843  1.000 70.606  0 356 LYS EEE CG  1 ? 18 
ATOM   4634 C CD  . LYS E 2 27  ? 17.087  7.055   17.983  1.000 73.791  0 356 LYS EEE CD  1 ? 18 
ATOM   4635 C CE  . LYS E 2 27  ? 15.778  7.775   17.732  1.000 76.739  0 356 LYS EEE CE  1 ? 18 
ATOM   4636 N NZ  . LYS E 2 27  ? 15.234  7.497   16.381  1.000 79.444  0 356 LYS EEE NZ  1 ? 18 
ATOM   4637 N N   . ARG E 2 28  ? 17.960  2.014   18.088  1.000 65.558  0 357 ARG EEE N   1 ? 18 
ATOM   4638 C CA  . ARG E 2 28  ? 19.358  1.531   18.196  1.000 64.567  0 357 ARG EEE CA  1 ? 18 
ATOM   4639 C C   . ARG E 2 28  ? 20.289  2.698   17.862  1.000 65.342  0 357 ARG EEE C   1 ? 18 
ATOM   4640 O O   . ARG E 2 28  ? 20.146  3.275   16.783  1.000 67.311  0 357 ARG EEE O   1 ? 18 
ATOM   4641 C CB  . ARG E 2 28  ? 19.626  0.333   17.283  1.000 64.922  0 357 ARG EEE CB  1 ? 18 
ATOM   4642 C CG  . ARG E 2 28  ? 21.047  -0.205  17.398  1.000 65.076  0 357 ARG EEE CG  1 ? 18 
ATOM   4643 C CD  . ARG E 2 28  ? 21.562  -0.839  16.124  1.000 68.036  0 357 ARG EEE CD  1 ? 18 
ATOM   4644 N NE  . ARG E 2 28  ? 21.360  0.060   14.997  1.000 70.871  0 357 ARG EEE NE  1 ? 18 
ATOM   4645 C CZ  . ARG E 2 28  ? 21.232  -0.317  13.734  1.000 73.858  0 357 ARG EEE CZ  1 ? 18 
ATOM   4646 N NH1 . ARG E 2 28  ? 21.309  -1.595  13.398  1.000 75.763  0 357 ARG EEE NH1 1 ? 18 
ATOM   4647 N NH2 . ARG E 2 28  ? 21.027  0.595   12.805  1.000 76.040  0 357 ARG EEE NH2 1 ? 18 
ATOM   4648 N N   . ILE E 2 29  ? 21.188  3.031   18.784  1.000 66.043  0 358 ILE EEE N   1 ? 18 
ATOM   4649 C CA  . ILE E 2 29  ? 22.181  4.132   18.646  1.000 67.121  0 358 ILE EEE CA  1 ? 18 
ATOM   4650 C C   . ILE E 2 29  ? 23.542  3.494   18.367  1.000 68.019  0 358 ILE EEE C   1 ? 18 
ATOM   4651 O O   . ILE E 2 29  ? 23.954  2.602   19.142  1.000 66.392  0 358 ILE EEE O   1 ? 18 
ATOM   4652 C CB  . ILE E 2 29  ? 22.175  5.021   19.900  1.000 66.492  0 358 ILE EEE CB  1 ? 18 
ATOM   4653 C CG1 . ILE E 2 29  ? 20.800  5.664   20.105  1.000 66.857  0 358 ILE EEE CG1 1 ? 18 
ATOM   4654 C CG2 . ILE E 2 29  ? 23.280  6.062   19.829  1.000 68.270  0 358 ILE EEE CG2 1 ? 18 
ATOM   4655 C CD1 . ILE E 2 29  ? 20.642  6.384   21.427  1.000 66.275  0 358 ILE EEE CD1 1 ? 18 
ATOM   4656 N N   . SER E 2 30  ? 24.182  3.921   17.276  1.000 70.778  0 359 SER EEE N   1 ? 18 
ATOM   4657 C CA  . SER E 2 30  ? 25.470  3.389   16.772  1.000 72.226  0 359 SER EEE CA  1 ? 18 
ATOM   4658 C C   . SER E 2 30  ? 26.247  4.496   16.052  1.000 74.244  0 359 SER EEE C   1 ? 18 
ATOM   4659 O O   . SER E 2 30  ? 25.619  5.485   15.639  1.000 74.452  0 359 SER EEE O   1 ? 18 
ATOM   4660 C CB  . SER E 2 30  ? 25.236  2.197   15.884  1.000 73.758  0 359 SER EEE CB  1 ? 18 
ATOM   4661 O OG  . SER E 2 30  ? 25.682  1.011   16.516  1.000 75.998  0 359 SER EEE OG  1 ? 18 
ATOM   4662 N N   . ASN E 2 31  ? 27.569  4.328   15.954  1.000 74.801  0 360 ASN EEE N   1 ? 18 
ATOM   4663 C CA  . ASN E 2 31  ? 28.481  5.142   15.108  1.000 77.135  0 360 ASN EEE CA  1 ? 18 
ATOM   4664 C C   . ASN E 2 31  ? 28.300  6.625   15.433  1.000 77.023  0 360 ASN EEE C   1 ? 18 
ATOM   4665 O O   . ASN E 2 31  ? 28.000  7.389   14.504  1.000 79.847  0 360 ASN EEE O   1 ? 18 
ATOM   4666 C CB  . ASN E 2 31  ? 28.246  4.865   13.621  1.000 79.939  0 360 ASN EEE CB  1 ? 18 
ATOM   4667 C CG  . ASN E 2 31  ? 28.829  3.540   13.173  1.000 80.319  0 360 ASN EEE CG  1 ? 18 
ATOM   4668 O OD1 . ASN E 2 31  ? 30.024  3.446   12.894  1.000 81.873  0 360 ASN EEE OD1 1 ? 18 
ATOM   4669 N ND2 . ASN E 2 31  ? 28.001  2.508   13.108  1.000 78.697  0 360 ASN EEE ND2 1 ? 18 
ATOM   4670 N N   . CYS E 2 32  ? 28.480  7.016   16.695  1.000 74.784  0 361 CYS EEE N   1 ? 18 
ATOM   4671 C CA  . CYS E 2 32  ? 28.289  8.420   17.151  1.000 75.891  0 361 CYS EEE CA  1 ? 18 
ATOM   4672 C C   . CYS E 2 32  ? 28.956  8.655   18.514  1.000 73.780  0 361 CYS EEE C   1 ? 18 
ATOM   4673 O O   . CYS E 2 32  ? 29.176  7.677   19.248  1.000 70.576  0 361 CYS EEE O   1 ? 18 
ATOM   4674 C CB  . CYS E 2 32  ? 26.804  8.771   17.204  1.000 75.716  0 361 CYS EEE CB  1 ? 18 
ATOM   4675 S SG  . CYS E 2 32  ? 25.836  7.703   18.302  1.000 74.044  0 361 CYS EEE SG  1 ? 18 
ATOM   4676 N N   . VAL E 2 33  ? 29.271  9.918   18.818  1.000 75.533  0 362 VAL EEE N   1 ? 18 
ATOM   4677 C CA  . VAL E 2 33  ? 29.838  10.375  20.122  1.000 75.605  0 362 VAL EEE CA  1 ? 18 
ATOM   4678 C C   . VAL E 2 33  ? 28.664  10.736  21.036  1.000 74.315  0 362 VAL EEE C   1 ? 18 
ATOM   4679 O O   . VAL E 2 33  ? 27.894  11.647  20.678  1.000 74.594  0 362 VAL EEE O   1 ? 18 
ATOM   4680 C CB  . VAL E 2 33  ? 30.804  11.565  19.949  1.000 78.278  0 362 VAL EEE CB  1 ? 18 
ATOM   4681 C CG1 . VAL E 2 33  ? 31.441  11.966  21.270  1.000 77.027  0 362 VAL EEE CG1 1 ? 18 
ATOM   4682 C CG2 . VAL E 2 33  ? 31.876  11.288  18.903  1.000 80.011  0 362 VAL EEE CG2 1 ? 18 
ATOM   4683 N N   . ALA E 2 34  ? 28.533  10.032  22.163  1.000 73.289  0 363 ALA EEE N   1 ? 18 
ATOM   4684 C CA  . ALA E 2 34  ? 27.441  10.197  23.148  1.000 71.928  0 363 ALA EEE CA  1 ? 18 
ATOM   4685 C C   . ALA E 2 34  ? 27.922  11.106  24.284  1.000 73.594  0 363 ALA EEE C   1 ? 18 
ATOM   4686 O O   . ALA E 2 34  ? 28.815  10.675  25.037  1.000 74.769  0 363 ALA EEE O   1 ? 18 
ATOM   4687 C CB  . ALA E 2 34  ? 27.033  8.844   23.673  1.000 69.448  0 363 ALA EEE CB  1 ? 18 
ATOM   4688 N N   . ASP E 2 35  ? 27.363  12.314  24.411  1.000 76.023  0 364 ASP EEE N   1 ? 18 
ATOM   4689 C CA  . ASP E 2 35  ? 27.577  13.186  25.601  1.000 76.687  0 364 ASP EEE CA  1 ? 18 
ATOM   4690 C C   . ASP E 2 35  ? 26.499  12.845  26.637  1.000 72.845  0 364 ASP EEE C   1 ? 18 
ATOM   4691 O O   . ASP E 2 35  ? 25.369  13.357  26.503  1.000 72.268  0 364 ASP EEE O   1 ? 18 
ATOM   4692 C CB  . ASP E 2 35  ? 27.584  14.675  25.242  1.000 80.948  0 364 ASP EEE CB  1 ? 18 
ATOM   4693 C CG  . ASP E 2 35  ? 28.033  15.586  26.379  1.000 82.670  0 364 ASP EEE CG  1 ? 18 
ATOM   4694 O OD1 . ASP E 2 35  ? 28.262  15.070  27.494  1.000 80.469  0 364 ASP EEE OD1 1 ? 18 
ATOM   4695 O OD2 . ASP E 2 35  ? 28.127  16.803  26.148  1.000 85.924  0 364 ASP EEE OD2 1 ? 18 
ATOM   4696 N N   . TYR E 2 36  ? 26.840  12.008  27.622  1.000 69.277  0 365 TYR EEE N   1 ? 18 
ATOM   4697 C CA  . TYR E 2 36  ? 25.895  11.513  28.655  1.000 66.092  0 365 TYR EEE CA  1 ? 18 
ATOM   4698 C C   . TYR E 2 36  ? 25.712  12.564  29.757  1.000 66.436  0 365 TYR EEE C   1 ? 18 
ATOM   4699 O O   . TYR E 2 36  ? 24.629  12.560  30.366  1.000 65.128  0 365 TYR EEE O   1 ? 18 
ATOM   4700 C CB  . TYR E 2 36  ? 26.370  10.180  29.236  1.000 63.276  0 365 TYR EEE CB  1 ? 18 
ATOM   4701 C CG  . TYR E 2 36  ? 26.508  9.056   28.241  1.000 61.307  0 365 TYR EEE CG  1 ? 18 
ATOM   4702 C CD1 . TYR E 2 36  ? 25.420  8.276   27.892  1.000 59.121  0 365 TYR EEE CD1 1 ? 18 
ATOM   4703 C CD2 . TYR E 2 36  ? 27.736  8.748   27.674  1.000 61.779  0 365 TYR EEE CD2 1 ? 18 
ATOM   4704 C CE1 . TYR E 2 36  ? 25.537  7.240   26.979  1.000 59.190  0 365 TYR EEE CE1 1 ? 18 
ATOM   4705 C CE2 . TYR E 2 36  ? 27.876  7.703   26.775  1.000 61.023  0 365 TYR EEE CE2 1 ? 18 
ATOM   4706 C CZ  . TYR E 2 36  ? 26.772  6.947   26.422  1.000 59.812  0 365 TYR EEE CZ  1 ? 18 
ATOM   4707 O OH  . TYR E 2 36  ? 26.901  5.916   25.538  1.000 59.207  0 365 TYR EEE OH  1 ? 18 
ATOM   4708 N N   . SER E 2 37  ? 26.715  13.418  30.002  1.000 67.887  0 366 SER EEE N   1 ? 18 
ATOM   4709 C CA  . SER E 2 37  ? 26.746  14.367  31.152  1.000 68.718  0 366 SER EEE CA  1 ? 18 
ATOM   4710 C C   . SER E 2 37  ? 25.613  15.394  31.032  1.000 68.532  0 366 SER EEE C   1 ? 18 
ATOM   4711 O O   . SER E 2 37  ? 25.097  15.820  32.083  1.000 67.772  0 366 SER EEE O   1 ? 18 
ATOM   4712 C CB  . SER E 2 37  ? 28.085  15.041  31.301  1.000 71.006  0 366 SER EEE CB  1 ? 18 
ATOM   4713 O OG  . SER E 2 37  ? 28.573  15.490  30.040  1.000 74.321  0 366 SER EEE OG  1 ? 18 
ATOM   4714 N N   . VAL E 2 38  ? 25.225  15.760  29.807  1.000 69.143  0 367 VAL EEE N   1 ? 18 
ATOM   4715 C CA  . VAL E 2 38  ? 24.106  16.720  29.552  1.000 69.947  0 367 VAL EEE CA  1 ? 18 
ATOM   4716 C C   . VAL E 2 38  ? 22.777  16.068  29.961  1.000 67.347  0 367 VAL EEE C   1 ? 18 
ATOM   4717 O O   . VAL E 2 38  ? 21.784  16.806  30.087  1.000 67.672  0 367 VAL EEE O   1 ? 18 
ATOM   4718 C CB  . VAL E 2 38  ? 24.078  17.220  28.092  1.000 72.065  0 367 VAL EEE CB  1 ? 18 
ATOM   4719 C CG1 . VAL E 2 38  ? 25.319  18.035  27.760  1.000 74.626  0 367 VAL EEE CG1 1 ? 18 
ATOM   4720 C CG2 . VAL E 2 38  ? 23.889  16.100  27.078  1.000 70.989  0 367 VAL EEE CG2 1 ? 18 
ATOM   4721 N N   . LEU E 2 39  ? 22.754  14.742  30.147  1.000 65.498  0 368 LEU EEE N   1 ? 18 
ATOM   4722 C CA  . LEU E 2 39  ? 21.562  13.984  30.624  1.000 64.365  0 368 LEU EEE CA  1 ? 18 
ATOM   4723 C C   . LEU E 2 39  ? 21.585  13.893  32.157  1.000 63.399  0 368 LEU EEE C   1 ? 18 
ATOM   4724 O O   . LEU E 2 39  ? 20.645  14.413  32.779  1.000 64.238  0 368 LEU EEE O   1 ? 18 
ATOM   4725 C CB  . LEU E 2 39  ? 21.532  12.589  29.985  1.000 63.458  0 368 LEU EEE CB  1 ? 18 
ATOM   4726 C CG  . LEU E 2 39  ? 21.571  12.548  28.451  1.000 64.528  0 368 LEU EEE CG  1 ? 18 
ATOM   4727 C CD1 . LEU E 2 39  ? 21.406  11.123  27.938  1.000 62.924  0 368 LEU EEE CD1 1 ? 18 
ATOM   4728 C CD2 . LEU E 2 39  ? 20.501  13.441  27.830  1.000 64.970  0 368 LEU EEE CD2 1 ? 18 
ATOM   4729 N N   . TYR E 2 40  ? 22.610  13.269  32.751  1.000 63.230  0 369 TYR EEE N   1 ? 18 
ATOM   4730 C CA  . TYR E 2 40  ? 22.616  12.894  34.194  1.000 61.996  0 369 TYR EEE CA  1 ? 18 
ATOM   4731 C C   . TYR E 2 40  ? 22.896  14.111  35.088  1.000 62.487  0 369 TYR EEE C   1 ? 18 
ATOM   4732 O O   . TYR E 2 40  ? 22.601  14.010  36.284  1.000 63.507  0 369 TYR EEE O   1 ? 18 
ATOM   4733 C CB  . TYR E 2 40  ? 23.546  11.706  34.472  1.000 61.278  0 369 TYR EEE CB  1 ? 18 
ATOM   4734 C CG  . TYR E 2 40  ? 25.013  11.901  34.178  1.000 63.654  0 369 TYR EEE CG  1 ? 18 
ATOM   4735 C CD1 . TYR E 2 40  ? 25.807  12.730  34.955  1.000 65.038  0 369 TYR EEE CD1 1 ? 18 
ATOM   4736 C CD2 . TYR E 2 40  ? 25.629  11.195  33.156  1.000 64.210  0 369 TYR EEE CD2 1 ? 18 
ATOM   4737 C CE1 . TYR E 2 40  ? 27.160  12.887  34.694  1.000 66.330  0 369 TYR EEE CE1 1 ? 18 
ATOM   4738 C CE2 . TYR E 2 40  ? 26.976  11.351  32.877  1.000 65.440  0 369 TYR EEE CE2 1 ? 18 
ATOM   4739 C CZ  . TYR E 2 40  ? 27.748  12.196  33.653  1.000 66.406  0 369 TYR EEE CZ  1 ? 18 
ATOM   4740 O OH  . TYR E 2 40  ? 29.077  12.349  33.397  1.000 66.857  0 369 TYR EEE OH  1 ? 18 
ATOM   4741 N N   . ASN E 2 41  ? 23.408  15.218  34.543  1.000 64.851  0 370 ASN EEE N   1 ? 18 
ATOM   4742 C CA  . ASN E 2 41  ? 23.630  16.481  35.303  1.000 66.329  0 370 ASN EEE CA  1 ? 18 
ATOM   4743 C C   . ASN E 2 41  ? 22.387  17.376  35.224  1.000 66.313  0 370 ASN EEE C   1 ? 18 
ATOM   4744 O O   . ASN E 2 41  ? 22.384  18.417  35.906  1.000 68.180  0 370 ASN EEE O   1 ? 18 
ATOM   4745 C CB  . ASN E 2 41  ? 24.865  17.247  34.815  1.000 68.504  0 370 ASN EEE CB  1 ? 18 
ATOM   4746 C CG  . ASN E 2 41  ? 26.165  16.544  35.139  1.000 68.521  0 370 ASN EEE CG  1 ? 18 
ATOM   4747 O OD1 . ASN E 2 41  ? 26.239  15.782  36.099  1.000 67.749  0 370 ASN EEE OD1 1 ? 18 
ATOM   4748 N ND2 . ASN E 2 41  ? 27.195  16.786  34.344  1.000 70.639  0 370 ASN EEE ND2 1 ? 18 
ATOM   4749 N N   . SER E 2 42  ? 21.385  17.009  34.419  1.000 64.206  0 371 SER EEE N   1 ? 18 
ATOM   4750 C CA  . SER E 2 42  ? 20.113  17.763  34.267  1.000 64.633  0 371 SER EEE CA  1 ? 18 
ATOM   4751 C C   . SER E 2 42  ? 19.281  17.630  35.549  1.000 64.031  0 371 SER EEE C   1 ? 18 
ATOM   4752 O O   . SER E 2 42  ? 19.325  16.544  36.178  1.000 62.398  0 371 SER EEE O   1 ? 18 
ATOM   4753 C CB  . SER E 2 42  ? 19.334  17.294  33.055  1.000 63.532  0 371 SER EEE CB  1 ? 18 
ATOM   4754 O OG  . SER E 2 42  ? 18.081  17.953  32.954  1.000 62.552  0 371 SER EEE OG  1 ? 18 
ATOM   4755 N N   . ALA E 2 43  ? 18.549  18.696  35.897  1.000 65.729  0 372 ALA EEE N   1 ? 18 
ATOM   4756 C CA  . ALA E 2 43  ? 17.550  18.752  36.988  1.000 64.919  0 372 ALA EEE CA  1 ? 18 
ATOM   4757 C C   . ALA E 2 43  ? 16.154  18.454  36.429  1.000 64.069  0 372 ALA EEE C   1 ? 18 
ATOM   4758 O O   . ALA E 2 43  ? 15.205  18.392  37.233  1.000 63.918  0 372 ALA EEE O   1 ? 18 
ATOM   4759 C CB  . ALA E 2 43  ? 17.592  20.107  37.651  1.000 66.813  0 372 ALA EEE CB  1 ? 18 
ATOM   4760 N N   . SER E 2 44  ? 16.042  18.265  35.108  1.000 64.367  0 373 SER EEE N   1 ? 18 
ATOM   4761 C CA  . SER E 2 44  ? 14.768  18.041  34.373  1.000 63.988  0 373 SER EEE CA  1 ? 18 
ATOM   4762 C C   . SER E 2 44  ? 14.319  16.575  34.475  1.000 61.994  0 373 SER EEE C   1 ? 18 
ATOM   4763 O O   . SER E 2 44  ? 13.120  16.312  34.249  1.000 62.743  0 373 SER EEE O   1 ? 18 
ATOM   4764 C CB  . SER E 2 44  ? 14.901  18.466  32.938  1.000 65.492  0 373 SER EEE CB  1 ? 18 
ATOM   4765 O OG  . SER E 2 44  ? 15.330  19.816  32.852  1.000 68.770  0 373 SER EEE OG  1 ? 18 
ATOM   4766 N N   . PHE E 2 45  ? 15.239  15.655  34.786  1.000 60.287  0 374 PHE EEE N   1 ? 18 
ATOM   4767 C CA  . PHE E 2 45  ? 14.957  14.211  34.991  1.000 58.341  0 374 PHE EEE CA  1 ? 18 
ATOM   4768 C C   . PHE E 2 45  ? 14.849  13.940  36.494  1.000 58.356  0 374 PHE EEE C   1 ? 18 
ATOM   4769 O O   . PHE E 2 45  ? 15.871  14.045  37.210  1.000 59.336  0 374 PHE EEE O   1 ? 18 
ATOM   4770 C CB  . PHE E 2 45  ? 16.035  13.348  34.334  1.000 57.557  0 374 PHE EEE CB  1 ? 18 
ATOM   4771 C CG  . PHE E 2 45  ? 16.243  13.634  32.869  1.000 59.385  0 374 PHE EEE CG  1 ? 18 
ATOM   4772 C CD1 . PHE E 2 45  ? 15.190  13.545  31.970  1.000 59.199  0 374 PHE EEE CD1 1 ? 18 
ATOM   4773 C CD2 . PHE E 2 45  ? 17.489  14.009  32.393  1.000 60.679  0 374 PHE EEE CD2 1 ? 18 
ATOM   4774 C CE1 . PHE E 2 45  ? 15.385  13.819  30.626  1.000 60.847  0 374 PHE EEE CE1 1 ? 18 
ATOM   4775 C CE2 . PHE E 2 45  ? 17.681  14.291  31.050  1.000 62.061  0 374 PHE EEE CE2 1 ? 18 
ATOM   4776 C CZ  . PHE E 2 45  ? 16.631  14.184  30.167  1.000 62.013  0 374 PHE EEE CZ  1 ? 18 
ATOM   4777 N N   . SER E 2 46  ? 13.641  13.609  36.954  1.000 57.210  0 375 SER EEE N   1 ? 18 
ATOM   4778 C CA  . SER E 2 46  ? 13.324  13.299  38.372  1.000 56.346  0 375 SER EEE CA  1 ? 18 
ATOM   4779 C C   . SER E 2 46  ? 13.764  11.866  38.698  1.000 54.891  0 375 SER EEE C   1 ? 18 
ATOM   4780 O O   . SER E 2 46  ? 14.241  11.641  39.826  1.000 54.346  0 375 SER EEE O   1 ? 18 
ATOM   4781 C CB  . SER E 2 46  ? 11.865  13.527  38.654  1.000 56.033  0 375 SER EEE CB  1 ? 18 
ATOM   4782 O OG  . SER E 2 46  ? 11.055  12.893  37.675  1.000 55.649  0 375 SER EEE OG  1 ? 18 
ATOM   4783 N N   . THR E 2 47  ? 13.630  10.940  37.741  1.000 53.559  0 376 THR EEE N   1 ? 18 
ATOM   4784 C CA  . THR E 2 47  ? 14.190  9.565   37.824  1.000 52.507  0 376 THR EEE CA  1 ? 18 
ATOM   4785 C C   . THR E 2 47  ? 15.344  9.423   36.823  1.000 52.854  0 376 THR EEE C   1 ? 18 
ATOM   4786 O O   . THR E 2 47  ? 15.125  9.696   35.629  1.000 53.606  0 376 THR EEE O   1 ? 18 
ATOM   4787 C CB  . THR E 2 47  ? 13.111  8.503   37.600  1.000 51.584  0 376 THR EEE CB  1 ? 18 
ATOM   4788 O OG1 . THR E 2 47  ? 12.146  8.653   38.642  1.000 51.297  0 376 THR EEE OG1 1 ? 18 
ATOM   4789 C CG2 . THR E 2 47  ? 13.659  7.093   37.635  1.000 51.198  0 376 THR EEE CG2 1 ? 18 
ATOM   4790 N N   . PHE E 2 48  ? 16.525  9.038   37.313  1.000 51.656  0 377 PHE EEE N   1 ? 18 
ATOM   4791 C CA  . PHE E 2 48  ? 17.709  8.656   36.503  1.000 52.104  0 377 PHE EEE CA  1 ? 18 
ATOM   4792 C C   . PHE E 2 48  ? 18.440  7.537   37.249  1.000 51.386  0 377 PHE EEE C   1 ? 18 
ATOM   4793 O O   . PHE E 2 48  ? 19.560  7.751   37.755  1.000 51.556  0 377 PHE EEE O   1 ? 18 
ATOM   4794 C CB  . PHE E 2 48  ? 18.589  9.877   36.215  1.000 53.982  0 377 PHE EEE CB  1 ? 18 
ATOM   4795 C CG  . PHE E 2 48  ? 19.430  9.755   34.968  1.000 54.529  0 377 PHE EEE CG  1 ? 18 
ATOM   4796 C CD1 . PHE E 2 48  ? 20.275  8.672   34.784  1.000 54.389  0 377 PHE EEE CD1 1 ? 18 
ATOM   4797 C CD2 . PHE E 2 48  ? 19.349  10.703  33.957  1.000 56.328  0 377 PHE EEE CD2 1 ? 18 
ATOM   4798 C CE1 . PHE E 2 48  ? 21.048  8.555   33.639  1.000 55.359  0 377 PHE EEE CE1 1 ? 18 
ATOM   4799 C CE2 . PHE E 2 48  ? 20.114  10.581  32.807  1.000 57.567  0 377 PHE EEE CE2 1 ? 18 
ATOM   4800 C CZ  . PHE E 2 48  ? 20.962  9.508   32.650  1.000 57.451  0 377 PHE EEE CZ  1 ? 18 
ATOM   4801 N N   . LYS E 2 49  ? 17.789  6.377   37.334  1.000 50.644  0 378 LYS EEE N   1 ? 18 
ATOM   4802 C CA  . LYS E 2 49  ? 18.264  5.207   38.115  1.000 50.363  0 378 LYS EEE CA  1 ? 18 
ATOM   4803 C C   . LYS E 2 49  ? 19.104  4.307   37.208  1.000 51.057  0 378 LYS EEE C   1 ? 18 
ATOM   4804 O O   . LYS E 2 49  ? 18.557  3.767   36.227  1.000 50.995  0 378 LYS EEE O   1 ? 18 
ATOM   4805 C CB  . LYS E 2 49  ? 17.077  4.445   38.706  1.000 49.575  0 378 LYS EEE CB  1 ? 18 
ATOM   4806 C CG  . LYS E 2 49  ? 16.393  5.126   39.881  1.000 50.267  0 378 LYS EEE CG  1 ? 18 
ATOM   4807 C CD  . LYS E 2 49  ? 15.084  4.470   40.254  1.000 50.280  0 378 LYS EEE CD  1 ? 18 
ATOM   4808 C CE  . LYS E 2 49  ? 14.573  4.878   41.619  1.000 51.259  0 378 LYS EEE CE  1 ? 18 
ATOM   4809 N NZ  . LYS E 2 49  ? 15.387  4.269   42.698  1.000 52.560  0 378 LYS EEE NZ  1 ? 18 
ATOM   4810 N N   . CYS E 2 50  ? 20.389  4.150   37.523  1.000 52.730  0 379 CYS EEE N   1 ? 18 
ATOM   4811 C CA  . CYS E 2 50  ? 21.317  3.259   36.778  1.000 53.983  0 379 CYS EEE CA  1 ? 18 
ATOM   4812 C C   . CYS E 2 50  ? 21.571  1.989   37.600  1.000 53.265  0 379 CYS EEE C   1 ? 18 
ATOM   4813 O O   . CYS E 2 50  ? 21.438  2.051   38.836  1.000 53.843  0 379 CYS EEE O   1 ? 18 
ATOM   4814 C CB  . CYS E 2 50  ? 22.597  3.998   36.400  1.000 55.005  0 379 CYS EEE CB  1 ? 18 
ATOM   4815 S SG  . CYS E 2 50  ? 22.288  5.454   35.359  1.000 56.421  0 379 CYS EEE SG  1 ? 18 
ATOM   4816 N N   . TYR E 2 51  ? 21.856  0.881   36.905  1.000 53.311  0 380 TYR EEE N   1 ? 18 
ATOM   4817 C CA  . TYR E 2 51  ? 22.119  -0.475  37.452  1.000 52.074  0 380 TYR EEE CA  1 ? 18 
ATOM   4818 C C   . TYR E 2 51  ? 23.309  -1.096  36.707  1.000 52.908  0 380 TYR EEE C   1 ? 18 
ATOM   4819 O O   . TYR E 2 51  ? 23.227  -1.269  35.465  1.000 52.842  0 380 TYR EEE O   1 ? 18 
ATOM   4820 C CB  . TYR E 2 51  ? 20.883  -1.364  37.298  1.000 50.320  0 380 TYR EEE CB  1 ? 18 
ATOM   4821 C CG  . TYR E 2 51  ? 19.594  -0.782  37.819  1.000 49.071  0 380 TYR EEE CG  1 ? 18 
ATOM   4822 C CD1 . TYR E 2 51  ? 18.889  0.153   37.079  1.000 48.159  0 380 TYR EEE CD1 1 ? 18 
ATOM   4823 C CD2 . TYR E 2 51  ? 19.069  -1.172  39.043  1.000 47.995  0 380 TYR EEE CD2 1 ? 18 
ATOM   4824 C CE1 . TYR E 2 51  ? 17.690  0.681   37.532  1.000 47.115  0 380 TYR EEE CE1 1 ? 18 
ATOM   4825 C CE2 . TYR E 2 51  ? 17.869  -0.660  39.508  1.000 46.855  0 380 TYR EEE CE2 1 ? 18 
ATOM   4826 C CZ  . TYR E 2 51  ? 17.183  0.277   38.755  1.000 47.196  0 380 TYR EEE CZ  1 ? 18 
ATOM   4827 O OH  . TYR E 2 51  ? 16.004  0.781   39.216  1.000 47.322  0 380 TYR EEE OH  1 ? 18 
ATOM   4828 N N   . GLY E 2 52  ? 24.395  -1.394  37.430  1.000 52.753  0 381 GLY EEE N   1 ? 18 
ATOM   4829 C CA  . GLY E 2 52  ? 25.591  -2.075  36.890  1.000 54.059  0 381 GLY EEE CA  1 ? 18 
ATOM   4830 C C   . GLY E 2 52  ? 26.546  -1.119  36.187  1.000 54.557  0 381 GLY EEE C   1 ? 18 
ATOM   4831 O O   . GLY E 2 52  ? 27.710  -1.500  35.954  1.000 55.768  0 381 GLY EEE O   1 ? 18 
ATOM   4832 N N   . VAL E 2 53  ? 26.077  0.083   35.858  1.000 54.632  0 382 VAL EEE N   1 ? 18 
ATOM   4833 C CA  . VAL E 2 53  ? 26.834  1.125   35.113  1.000 56.018  0 382 VAL EEE CA  1 ? 18 
ATOM   4834 C C   . VAL E 2 53  ? 26.799  2.401   35.955  1.000 56.908  0 382 VAL EEE C   1 ? 18 
ATOM   4835 O O   . VAL E 2 53  ? 25.709  2.750   36.442  1.000 58.669  0 382 VAL EEE O   1 ? 18 
ATOM   4836 C CB  . VAL E 2 53  ? 26.237  1.338   33.706  1.000 57.037  0 382 VAL EEE CB  1 ? 18 
ATOM   4837 C CG1 . VAL E 2 53  ? 24.773  1.748   33.736  1.000 56.810  0 382 VAL EEE CG1 1 ? 18 
ATOM   4838 C CG2 . VAL E 2 53  ? 27.041  2.340   32.908  1.000 59.268  0 382 VAL EEE CG2 1 ? 18 
ATOM   4839 N N   . SER E 2 54  ? 27.942  3.066   36.136  1.000 58.949  0 383 SER EEE N   1 ? 18 
ATOM   4840 C CA  . SER E 2 54  ? 28.030  4.415   36.755  1.000 60.295  0 383 SER EEE CA  1 ? 18 
ATOM   4841 C C   . SER E 2 54  ? 27.998  5.465   35.649  1.000 60.805  0 383 SER EEE C   1 ? 18 
ATOM   4842 O O   . SER E 2 54  ? 28.823  5.422   34.742  1.000 60.757  0 383 SER EEE O   1 ? 18 
ATOM   4843 C CB  . SER E 2 54  ? 29.255  4.551   37.609  1.000 61.876  0 383 SER EEE CB  1 ? 18 
ATOM   4844 O OG  . SER E 2 54  ? 30.385  4.041   36.933  1.000 65.569  0 383 SER EEE OG  1 ? 18 
ATOM   4845 N N   . PRO E 2 55  ? 27.027  6.406   35.669  1.000 60.792  0 384 PRO EEE N   1 ? 18 
ATOM   4846 C CA  . PRO E 2 55  ? 26.900  7.403   34.606  1.000 63.297  0 384 PRO EEE CA  1 ? 18 
ATOM   4847 C C   . PRO E 2 55  ? 28.196  8.183   34.315  1.000 65.458  0 384 PRO EEE C   1 ? 18 
ATOM   4848 O O   . PRO E 2 55  ? 28.430  8.505   33.169  1.000 69.251  0 384 PRO EEE O   1 ? 18 
ATOM   4849 C CB  . PRO E 2 55  ? 25.833  8.379   35.131  1.000 63.321  0 384 PRO EEE CB  1 ? 18 
ATOM   4850 C CG  . PRO E 2 55  ? 25.074  7.633   36.206  1.000 60.849  0 384 PRO EEE CG  1 ? 18 
ATOM   4851 C CD  . PRO E 2 55  ? 25.985  6.532   36.698  1.000 59.731  0 384 PRO EEE CD  1 ? 18 
ATOM   4852 N N   . THR E 2 56  ? 28.998  8.472   35.344  1.000 64.356  0 385 THR EEE N   1 ? 18 
ATOM   4853 C CA  . THR E 2 56  ? 30.199  9.346   35.248  1.000 66.185  0 385 THR EEE CA  1 ? 18 
ATOM   4854 C C   . THR E 2 56  ? 31.296  8.675   34.408  1.000 66.863  0 385 THR EEE C   1 ? 18 
ATOM   4855 O O   . THR E 2 56  ? 32.106  9.420   33.828  1.000 69.408  0 385 THR EEE O   1 ? 18 
ATOM   4856 C CB  . THR E 2 56  ? 30.701  9.754   36.637  1.000 66.321  0 385 THR EEE CB  1 ? 18 
ATOM   4857 O OG1 . THR E 2 56  ? 31.157  8.593   37.330  1.000 65.307  0 385 THR EEE OG1 1 ? 18 
ATOM   4858 C CG2 . THR E 2 56  ? 29.631  10.455  37.444  1.000 66.618  0 385 THR EEE CG2 1 ? 18 
ATOM   4859 N N   . LYS E 2 57  ? 31.326  7.341   34.334  1.000 65.788  0 386 LYS EEE N   1 ? 18 
ATOM   4860 C CA  . LYS E 2 57  ? 32.353  6.576   33.568  1.000 66.332  0 386 LYS EEE CA  1 ? 18 
ATOM   4861 C C   . LYS E 2 57  ? 31.955  6.474   32.087  1.000 67.673  0 386 LYS EEE C   1 ? 18 
ATOM   4862 O O   . LYS E 2 57  ? 32.868  6.244   31.270  1.000 66.398  0 386 LYS EEE O   1 ? 18 
ATOM   4863 C CB  . LYS E 2 57  ? 32.560  5.186   34.178  1.000 64.435  0 386 LYS EEE CB  1 ? 18 
ATOM   4864 C CG  . LYS E 2 57  ? 33.148  5.191   35.582  1.000 64.347  0 386 LYS EEE CG  1 ? 18 
ATOM   4865 C CD  . LYS E 2 57  ? 33.242  3.825   36.225  1.000 62.990  0 386 LYS EEE CD  1 ? 18 
ATOM   4866 C CE  . LYS E 2 57  ? 34.298  2.930   35.623  1.000 63.349  0 386 LYS EEE CE  1 ? 18 
ATOM   4867 N NZ  . LYS E 2 57  ? 34.452  1.692   36.420  1.000 62.991  0 386 LYS EEE NZ  1 ? 18 
ATOM   4868 N N   . LEU E 2 58  ? 30.664  6.646   31.758  1.000 55.691  0 387 LEU EEE N   1 ? 19 
ATOM   4869 C CA  . LEU E 2 58  ? 30.107  6.480   30.380  1.000 55.721  0 387 LEU EEE CA  1 ? 19 
ATOM   4870 C C   . LEU E 2 58  ? 30.821  7.402   29.380  1.000 59.206  0 387 LEU EEE C   1 ? 19 
ATOM   4871 O O   . LEU E 2 58  ? 30.993  6.986   28.217  1.000 61.005  0 387 LEU EEE O   1 ? 19 
ATOM   4872 C CB  . LEU E 2 58  ? 28.602  6.782   30.380  1.000 53.579  0 387 LEU EEE CB  1 ? 19 
ATOM   4873 C CG  . LEU E 2 58  ? 27.712  5.727   31.034  1.000 51.160  0 387 LEU EEE CG  1 ? 19 
ATOM   4874 C CD1 . LEU E 2 58  ? 26.255  6.174   31.031  1.000 49.744  0 387 LEU EEE CD1 1 ? 19 
ATOM   4875 C CD2 . LEU E 2 58  ? 27.865  4.385   30.315  1.000 50.739  0 387 LEU EEE CD2 1 ? 19 
ATOM   4876 N N   . ASN E 2 59  ? 31.210  8.604   29.814  1.000 62.690  0 388 ASN EEE N   1 ? 19 
ATOM   4877 C CA  . ASN E 2 59  ? 31.860  9.635   28.957  1.000 67.066  0 388 ASN EEE CA  1 ? 19 
ATOM   4878 C C   . ASN E 2 59  ? 33.275  9.190   28.558  1.000 68.041  0 388 ASN EEE C   1 ? 19 
ATOM   4879 O O   . ASN E 2 59  ? 33.840  9.826   27.653  1.000 69.590  0 388 ASN EEE O   1 ? 19 
ATOM   4880 C CB  . ASN E 2 59  ? 31.883  11.010  29.635  1.000 71.769  0 388 ASN EEE CB  1 ? 19 
ATOM   4881 C CG  . ASN E 2 59  ? 30.732  11.906  29.223  1.000 75.246  0 388 ASN EEE CG  1 ? 19 
ATOM   4882 O OD1 . ASN E 2 59  ? 29.865  11.513  28.439  1.000 80.450  0 388 ASN EEE OD1 1 ? 19 
ATOM   4883 N ND2 . ASN E 2 59  ? 30.720  13.118  29.750  1.000 78.133  0 388 ASN EEE ND2 1 ? 19 
ATOM   4884 N N   . ASP E 2 60  ? 33.824  8.147   29.191  1.000 66.434  0 389 ASP EEE N   1 ? 19 
ATOM   4885 C CA  . ASP E 2 60  ? 35.174  7.602   28.886  1.000 67.118  0 389 ASP EEE CA  1 ? 19 
ATOM   4886 C C   . ASP E 2 60  ? 35.054  6.147   28.407  1.000 62.010  0 389 ASP EEE C   1 ? 19 
ATOM   4887 O O   . ASP E 2 60  ? 36.095  5.472   28.320  1.000 62.350  0 389 ASP EEE O   1 ? 19 
ATOM   4888 C CB  . ASP E 2 60  ? 36.085  7.739   30.111  1.000 71.551  0 389 ASP EEE CB  1 ? 19 
ATOM   4889 C CG  . ASP E 2 60  ? 37.571  7.747   29.798  1.000 78.461  0 389 ASP EEE CG  1 ? 19 
ATOM   4890 O OD1 . ASP E 2 60  ? 37.960  8.327   28.753  1.000 81.994  0 389 ASP EEE OD1 1 ? 19 
ATOM   4891 O OD2 . ASP E 2 60  ? 38.332  7.174   30.604  1.000 81.990  0 389 ASP EEE OD2 1 ? 19 
ATOM   4892 N N   . LEU E 2 61  ? 33.842  5.685   28.086  1.000 57.874  0 390 LEU EEE N   1 ? 19 
ATOM   4893 C CA  . LEU E 2 61  ? 33.559  4.263   27.743  1.000 56.503  0 390 LEU EEE CA  1 ? 19 
ATOM   4894 C C   . LEU E 2 61  ? 33.000  4.168   26.319  1.000 56.078  0 390 LEU EEE C   1 ? 19 
ATOM   4895 O O   . LEU E 2 61  ? 32.387  5.148   25.841  1.000 55.080  0 390 LEU EEE O   1 ? 19 
ATOM   4896 C CB  . LEU E 2 61  ? 32.577  3.677   28.766  1.000 54.590  0 390 LEU EEE CB  1 ? 19 
ATOM   4897 C CG  . LEU E 2 61  ? 33.161  3.364   30.144  1.000 54.730  0 390 LEU EEE CG  1 ? 19 
ATOM   4898 C CD1 . LEU E 2 61  ? 32.062  3.011   31.130  1.000 53.754  0 390 LEU EEE CD1 1 ? 19 
ATOM   4899 C CD2 . LEU E 2 61  ? 34.183  2.238   30.072  1.000 55.931  0 390 LEU EEE CD2 1 ? 19 
ATOM   4900 N N   . CYS E 2 62  ? 33.210  3.013   25.681  1.000 56.048  0 391 CYS EEE N   1 ? 19 
ATOM   4901 C CA  . CYS E 2 62  ? 32.794  2.694   24.291  1.000 56.197  0 391 CYS EEE CA  1 ? 19 
ATOM   4902 C C   . CYS E 2 62  ? 31.942  1.425   24.298  1.000 54.025  0 391 CYS EEE C   1 ? 19 
ATOM   4903 O O   . CYS E 2 62  ? 32.303  0.477   25.019  1.000 52.483  0 391 CYS EEE O   1 ? 19 
ATOM   4904 C CB  . CYS E 2 62  ? 34.003  2.487   23.383  1.000 60.336  0 391 CYS EEE CB  1 ? 19 
ATOM   4905 S SG  . CYS E 2 62  ? 34.908  4.014   23.022  1.000 64.720  0 391 CYS EEE SG  1 ? 19 
ATOM   4906 N N   . PHE E 2 63  ? 30.865  1.412   23.506  1.000 54.100  0 392 PHE EEE N   1 ? 19 
ATOM   4907 C CA  . PHE E 2 63  ? 29.928  0.267   23.365  1.000 52.246  0 392 PHE EEE CA  1 ? 19 
ATOM   4908 C C   . PHE E 2 63  ? 29.709  -0.041  21.883  1.000 55.312  0 392 PHE EEE C   1 ? 19 
ATOM   4909 O O   . PHE E 2 63  ? 29.823  0.880   21.043  1.000 55.470  0 392 PHE EEE O   1 ? 19 
ATOM   4910 C CB  . PHE E 2 63  ? 28.618  0.575   24.088  1.000 49.208  0 392 PHE EEE CB  1 ? 19 
ATOM   4911 C CG  . PHE E 2 63  ? 28.786  0.790   25.570  1.000 46.991  0 392 PHE EEE CG  1 ? 19 
ATOM   4912 C CD1 . PHE E 2 63  ? 28.894  -0.288  26.433  1.000 45.613  0 392 PHE EEE CD1 1 ? 19 
ATOM   4913 C CD2 . PHE E 2 63  ? 28.872  2.071   26.096  1.000 46.756  0 392 PHE EEE CD2 1 ? 19 
ATOM   4914 C CE1 . PHE E 2 63  ? 29.059  -0.088  27.795  1.000 44.531  0 392 PHE EEE CE1 1 ? 19 
ATOM   4915 C CE2 . PHE E 2 63  ? 29.040  2.269   27.457  1.000 45.683  0 392 PHE EEE CE2 1 ? 19 
ATOM   4916 C CZ  . PHE E 2 63  ? 29.129  1.190   28.305  1.000 44.715  0 392 PHE EEE CZ  1 ? 19 
ATOM   4917 N N   . THR E 2 64  ? 29.429  -1.312  21.582  1.000 57.433  0 393 THR EEE N   1 ? 19 
ATOM   4918 C CA  . THR E 2 64  ? 29.065  -1.795  20.227  1.000 62.266  0 393 THR EEE CA  1 ? 19 
ATOM   4919 C C   . THR E 2 64  ? 27.754  -1.117  19.824  1.000 62.277  0 393 THR EEE C   1 ? 19 
ATOM   4920 O O   . THR E 2 64  ? 27.692  -0.568  18.702  1.000 62.696  0 393 THR EEE O   1 ? 19 
ATOM   4921 C CB  . THR E 2 64  ? 29.033  -3.327  20.184  1.000 66.003  0 393 THR EEE CB  1 ? 19 
ATOM   4922 O OG1 . THR E 2 64  ? 28.191  -3.816  21.223  1.000 71.701  0 393 THR EEE OG1 1 ? 19 
ATOM   4923 C CG2 . THR E 2 64  ? 30.406  -3.941  20.348  1.000 69.074  0 393 THR EEE CG2 1 ? 19 
ATOM   4924 N N   . ASN E 2 65  ? 26.772  -1.119  20.731  1.000 62.308  0 394 ASN EEE N   1 ? 19 
ATOM   4925 C CA  . ASN E 2 65  ? 25.440  -0.484  20.537  1.000 61.324  0 394 ASN EEE CA  1 ? 19 
ATOM   4926 C C   . ASN E 2 65  ? 24.909  0.054   21.865  1.000 58.862  0 394 ASN EEE C   1 ? 19 
ATOM   4927 O O   . ASN E 2 65  ? 25.138  -0.596  22.900  1.000 61.312  0 394 ASN EEE O   1 ? 19 
ATOM   4928 C CB  . ASN E 2 65  ? 24.418  -1.468  19.971  1.000 62.826  0 394 ASN EEE CB  1 ? 19 
ATOM   4929 C CG  . ASN E 2 65  ? 24.712  -1.842  18.538  1.000 66.460  0 394 ASN EEE CG  1 ? 19 
ATOM   4930 O OD1 . ASN E 2 65  ? 24.688  -0.986  17.653  1.000 68.589  0 394 ASN EEE OD1 1 ? 19 
ATOM   4931 N ND2 . ASN E 2 65  ? 25.010  -3.110  18.308  1.000 67.804  0 394 ASN EEE ND2 1 ? 19 
ATOM   4932 N N   . VAL E 2 66  ? 24.216  1.191   21.812  1.000 56.958  0 395 VAL EEE N   1 ? 19 
ATOM   4933 C CA  . VAL E 2 66  ? 23.335  1.695   22.900  1.000 53.894  0 395 VAL EEE CA  1 ? 19 
ATOM   4934 C C   . VAL E 2 66  ? 21.898  1.657   22.374  1.000 54.478  0 395 VAL EEE C   1 ? 19 
ATOM   4935 O O   . VAL E 2 66  ? 21.683  2.010   21.202  1.000 56.619  0 395 VAL EEE O   1 ? 19 
ATOM   4936 C CB  . VAL E 2 66  ? 23.745  3.107   23.355  1.000 55.216  0 395 VAL EEE CB  1 ? 19 
ATOM   4937 C CG1 . VAL E 2 66  ? 22.758  3.689   24.363  1.000 54.122  0 395 VAL EEE CG1 1 ? 19 
ATOM   4938 C CG2 . VAL E 2 66  ? 25.157  3.109   23.919  1.000 55.015  0 395 VAL EEE CG2 1 ? 19 
ATOM   4939 N N   . TYR E 2 67  ? 20.960  1.208   23.205  1.000 51.824  0 396 TYR EEE N   1 ? 19 
ATOM   4940 C CA  . TYR E 2 67  ? 19.517  1.119   22.876  1.000 49.502  0 396 TYR EEE CA  1 ? 19 
ATOM   4941 C C   . TYR E 2 67  ? 18.740  2.080   23.773  1.000 47.816  0 396 TYR EEE C   1 ? 19 
ATOM   4942 O O   . TYR E 2 67  ? 18.907  2.022   25.002  1.000 47.368  0 396 TYR EEE O   1 ? 19 
ATOM   4943 C CB  . TYR E 2 67  ? 19.016  -0.312  23.037  1.000 48.551  0 396 TYR EEE CB  1 ? 19 
ATOM   4944 C CG  . TYR E 2 67  ? 19.667  -1.310  22.116  1.000 50.705  0 396 TYR EEE CG  1 ? 19 
ATOM   4945 C CD1 . TYR E 2 67  ? 19.187  -1.513  20.831  1.000 53.651  0 396 TYR EEE CD1 1 ? 19 
ATOM   4946 C CD2 . TYR E 2 67  ? 20.760  -2.054  22.524  1.000 51.003  0 396 TYR EEE CD2 1 ? 19 
ATOM   4947 C CE1 . TYR E 2 67  ? 19.766  -2.439  19.978  1.000 55.867  0 396 TYR EEE CE1 1 ? 19 
ATOM   4948 C CE2 . TYR E 2 67  ? 21.357  -2.979  21.682  1.000 53.910  0 396 TYR EEE CE2 1 ? 19 
ATOM   4949 C CZ  . TYR E 2 67  ? 20.862  -3.169  20.403  1.000 56.384  0 396 TYR EEE CZ  1 ? 19 
ATOM   4950 O OH  . TYR E 2 67  ? 21.456  -4.070  19.571  1.000 59.167  0 396 TYR EEE OH  1 ? 19 
ATOM   4951 N N   . ALA E 2 68  ? 17.936  2.946   23.157  1.000 47.668  0 397 ALA EEE N   1 ? 19 
ATOM   4952 C CA  . ALA E 2 68  ? 16.995  3.865   23.831  1.000 46.480  0 397 ALA EEE CA  1 ? 19 
ATOM   4953 C C   . ALA E 2 68  ? 15.568  3.367   23.582  1.000 46.465  0 397 ALA EEE C   1 ? 19 
ATOM   4954 O O   . ALA E 2 68  ? 15.091  3.457   22.429  1.000 49.790  0 397 ALA EEE O   1 ? 19 
ATOM   4955 C CB  . ALA E 2 68  ? 17.207  5.271   23.329  1.000 47.950  0 397 ALA EEE CB  1 ? 19 
ATOM   4956 N N   . ASP E 2 69  ? 14.943  2.801   24.616  1.000 44.274  0 398 ASP EEE N   1 ? 19 
ATOM   4957 C CA  . ASP E 2 69  ? 13.505  2.433   24.639  1.000 42.363  0 398 ASP EEE CA  1 ? 19 
ATOM   4958 C C   . ASP E 2 69  ? 12.739  3.609   25.246  1.000 41.431  0 398 ASP EEE C   1 ? 19 
ATOM   4959 O O   . ASP E 2 69  ? 13.145  4.079   26.329  1.000 41.631  0 398 ASP EEE O   1 ? 19 
ATOM   4960 C CB  . ASP E 2 69  ? 13.278  1.137   25.419  1.000 41.413  0 398 ASP EEE CB  1 ? 19 
ATOM   4961 C CG  . ASP E 2 69  ? 14.094  -0.035  24.900  1.000 41.847  0 398 ASP EEE CG  1 ? 19 
ATOM   4962 O OD1 . ASP E 2 69  ? 14.499  0.009   23.719  1.000 42.863  0 398 ASP EEE OD1 1 ? 19 
ATOM   4963 O OD2 . ASP E 2 69  ? 14.321  -0.981  25.680  1.000 41.362  0 398 ASP EEE OD2 1 ? 19 
ATOM   4964 N N   . SER E 2 70  ? 11.688  4.074   24.569  1.000 41.744  0 399 SER EEE N   1 ? 19 
ATOM   4965 C CA  . SER E 2 70  ? 10.875  5.248   24.979  1.000 41.946  0 399 SER EEE CA  1 ? 19 
ATOM   4966 C C   . SER E 2 70  ? 9.391   4.873   24.973  1.000 43.396  0 399 SER EEE C   1 ? 19 
ATOM   4967 O O   . SER E 2 70  ? 8.984   4.061   24.116  1.000 44.336  0 399 SER EEE O   1 ? 19 
ATOM   4968 C CB  . SER E 2 70  ? 11.150  6.441   24.103  1.000 43.216  0 399 SER EEE CB  1 ? 19 
ATOM   4969 O OG  . SER E 2 70  ? 11.018  6.104   22.730  1.000 44.988  0 399 SER EEE OG  1 ? 19 
ATOM   4970 N N   . PHE E 2 71  ? 8.631   5.434   25.917  1.000 44.011  0 400 PHE EEE N   1 ? 19 
ATOM   4971 C CA  . PHE E 2 71  ? 7.170   5.225   26.086  1.000 44.587  0 400 PHE EEE CA  1 ? 19 
ATOM   4972 C C   . PHE E 2 71  ? 6.644   6.134   27.200  1.000 43.691  0 400 PHE EEE C   1 ? 19 
ATOM   4973 O O   . PHE E 2 71  ? 7.454   6.754   27.907  1.000 42.952  0 400 PHE EEE O   1 ? 19 
ATOM   4974 C CB  . PHE E 2 71  ? 6.866   3.762   26.402  1.000 44.518  0 400 PHE EEE CB  1 ? 19 
ATOM   4975 C CG  . PHE E 2 71  ? 7.669   3.195   27.543  1.000 44.518  0 400 PHE EEE CG  1 ? 19 
ATOM   4976 C CD1 . PHE E 2 71  ? 7.323   3.466   28.858  1.000 44.054  0 400 PHE EEE CD1 1 ? 19 
ATOM   4977 C CD2 . PHE E 2 71  ? 8.773   2.392   27.301  1.000 44.860  0 400 PHE EEE CD2 1 ? 19 
ATOM   4978 C CE1 . PHE E 2 71  ? 8.064   2.943   29.906  1.000 43.332  0 400 PHE EEE CE1 1 ? 19 
ATOM   4979 C CE2 . PHE E 2 71  ? 9.508   1.863   28.352  1.000 43.404  0 400 PHE EEE CE2 1 ? 19 
ATOM   4980 C CZ  . PHE E 2 71  ? 9.152   2.141   29.651  1.000 42.645  0 400 PHE EEE CZ  1 ? 19 
ATOM   4981 N N   . VAL E 2 72  ? 5.317   6.202   27.332  1.000 46.457  0 401 VAL EEE N   1 ? 19 
ATOM   4982 C CA  . VAL E 2 72  ? 4.597   6.967   28.392  1.000 46.582  0 401 VAL EEE CA  1 ? 19 
ATOM   4983 C C   . VAL E 2 72  ? 3.853   5.977   29.298  1.000 45.818  0 401 VAL EEE C   1 ? 19 
ATOM   4984 O O   . VAL E 2 72  ? 3.188   5.064   28.776  1.000 47.192  0 401 VAL EEE O   1 ? 19 
ATOM   4985 C CB  . VAL E 2 72  ? 3.648   8.016   27.781  1.000 48.446  0 401 VAL EEE CB  1 ? 19 
ATOM   4986 C CG1 . VAL E 2 72  ? 2.536   8.415   28.741  1.000 50.773  0 401 VAL EEE CG1 1 ? 19 
ATOM   4987 C CG2 . VAL E 2 72  ? 4.410   9.246   27.321  1.000 49.353  0 401 VAL EEE CG2 1 ? 19 
ATOM   4988 N N   . ILE E 2 73  ? 3.978   6.171   30.611  1.000 45.355  0 402 ILE EEE N   1 ? 19 
ATOM   4989 C CA  . ILE E 2 73  ? 3.187   5.479   31.672  1.000 45.536  0 402 ILE EEE CA  1 ? 19 
ATOM   4990 C C   . ILE E 2 73  ? 2.734   6.555   32.665  1.000 46.601  0 402 ILE EEE C   1 ? 19 
ATOM   4991 O O   . ILE E 2 73  ? 3.147   7.717   32.482  1.000 47.416  0 402 ILE EEE O   1 ? 19 
ATOM   4992 C CB  . ILE E 2 73  ? 4.019   4.363   32.338  1.000 43.635  0 402 ILE EEE CB  1 ? 19 
ATOM   4993 C CG1 . ILE E 2 73  ? 5.355   4.885   32.876  1.000 42.580  0 402 ILE EEE CG1 1 ? 19 
ATOM   4994 C CG2 . ILE E 2 73  ? 4.218   3.201   31.376  1.000 43.363  0 402 ILE EEE CG2 1 ? 19 
ATOM   4995 C CD1 . ILE E 2 73  ? 6.156   3.849   33.630  1.000 42.829  0 402 ILE EEE CD1 1 ? 19 
ATOM   4996 N N   . ARG E 2 74  ? 1.913   6.203   33.659  1.000 48.722  0 403 ARG EEE N   1 ? 19 
ATOM   4997 C CA  . ARG E 2 74  ? 1.521   7.151   34.738  1.000 51.894  0 403 ARG EEE CA  1 ? 19 
ATOM   4998 C C   . ARG E 2 74  ? 2.553   7.053   35.870  1.000 51.714  0 403 ARG EEE C   1 ? 19 
ATOM   4999 O O   . ARG E 2 74  ? 3.263   6.025   35.941  1.000 48.558  0 403 ARG EEE O   1 ? 19 
ATOM   5000 C CB  . ARG E 2 74  ? 0.072   6.933   35.189  1.000 54.942  0 403 ARG EEE CB  1 ? 19 
ATOM   5001 C CG  . ARG E 2 74  ? -0.232  5.601   35.858  1.000 57.365  0 403 ARG EEE CG  1 ? 19 
ATOM   5002 C CD  . ARG E 2 74  ? -1.733  5.501   36.125  1.000 61.562  0 403 ARG EEE CD  1 ? 19 
ATOM   5003 N NE  . ARG E 2 74  ? -2.076  4.388   36.996  1.000 65.916  0 403 ARG EEE NE  1 ? 19 
ATOM   5004 C CZ  . ARG E 2 74  ? -2.042  4.428   38.329  1.000 72.083  0 403 ARG EEE CZ  1 ? 19 
ATOM   5005 N NH1 . ARG E 2 74  ? -1.684  5.536   38.960  1.000 74.726  0 403 ARG EEE NH1 1 ? 19 
ATOM   5006 N NH2 . ARG E 2 74  ? -2.382  3.360   39.031  1.000 73.712  0 403 ARG EEE NH2 1 ? 19 
ATOM   5007 N N   . GLY E 2 75  ? 2.650   8.107   36.688  1.000 54.091  0 404 GLY EEE N   1 ? 19 
ATOM   5008 C CA  . GLY E 2 75  ? 3.679   8.287   37.733  1.000 55.294  0 404 GLY EEE CA  1 ? 19 
ATOM   5009 C C   . GLY E 2 75  ? 3.836   7.071   38.636  1.000 55.651  0 404 GLY EEE C   1 ? 19 
ATOM   5010 O O   . GLY E 2 75  ? 4.989   6.658   38.865  1.000 58.141  0 404 GLY EEE O   1 ? 19 
ATOM   5011 N N   . ASP E 2 76  ? 2.723   6.518   39.130  1.000 56.226  0 405 ASP EEE N   1 ? 19 
ATOM   5012 C CA  . ASP E 2 76  ? 2.689   5.393   40.105  1.000 57.207  0 405 ASP EEE CA  1 ? 19 
ATOM   5013 C C   . ASP E 2 76  ? 3.392   4.153   39.534  1.000 54.289  0 405 ASP EEE C   1 ? 19 
ATOM   5014 O O   . ASP E 2 76  ? 3.788   3.287   40.336  1.000 57.184  0 405 ASP EEE O   1 ? 19 
ATOM   5015 C CB  . ASP E 2 76  ? 1.252   5.036   40.504  1.000 60.236  0 405 ASP EEE CB  1 ? 19 
ATOM   5016 C CG  . ASP E 2 76  ? 0.618   5.990   41.505  1.000 64.317  0 405 ASP EEE CG  1 ? 19 
ATOM   5017 O OD1 . ASP E 2 76  ? 1.365   6.764   42.144  1.000 67.889  0 405 ASP EEE OD1 1 ? 19 
ATOM   5018 O OD2 . ASP E 2 76  ? -0.620  5.944   41.648  1.000 67.793  0 405 ASP EEE OD2 1 ? 19 
ATOM   5019 N N   . GLU E 2 77  ? 3.539   4.062   38.210  1.000 49.482  0 406 GLU EEE N   1 ? 19 
ATOM   5020 C CA  . GLU E 2 77  ? 4.046   2.850   37.512  1.000 48.277  0 406 GLU EEE CA  1 ? 19 
ATOM   5021 C C   . GLU E 2 77  ? 5.541   2.981   37.187  1.000 46.515  0 406 GLU EEE C   1 ? 19 
ATOM   5022 O O   . GLU E 2 77  ? 6.116   1.983   36.721  1.000 46.211  0 406 GLU EEE O   1 ? 19 
ATOM   5023 C CB  . GLU E 2 77  ? 3.245   2.618   36.230  1.000 47.844  0 406 GLU EEE CB  1 ? 19 
ATOM   5024 C CG  . GLU E 2 77  ? 1.813   2.180   36.476  1.000 48.555  0 406 GLU EEE CG  1 ? 19 
ATOM   5025 C CD  . GLU E 2 77  ? 0.922   2.208   35.245  1.000 47.998  0 406 GLU EEE CD  1 ? 19 
ATOM   5026 O OE1 . GLU E 2 77  ? 1.280   2.893   34.261  1.000 45.356  0 406 GLU EEE OE1 1 ? 19 
ATOM   5027 O OE2 . GLU E 2 77  ? -0.138  1.555   35.280  1.000 49.534  0 406 GLU EEE OE2 1 ? 19 
ATOM   5028 N N   . VAL E 2 78  ? 6.155   4.146   37.415  1.000 46.704  0 407 VAL EEE N   1 ? 19 
ATOM   5029 C CA  . VAL E 2 78  ? 7.597   4.383   37.092  1.000 46.953  0 407 VAL EEE CA  1 ? 19 
ATOM   5030 C C   . VAL E 2 78  ? 8.471   3.425   37.915  1.000 47.305  0 407 VAL EEE C   1 ? 19 
ATOM   5031 O O   . VAL E 2 78  ? 9.534   3.041   37.410  1.000 47.942  0 407 VAL EEE O   1 ? 19 
ATOM   5032 C CB  . VAL E 2 78  ? 8.008   5.855   37.293  1.000 47.193  0 407 VAL EEE CB  1 ? 19 
ATOM   5033 C CG1 . VAL E 2 78  ? 9.518   6.037   37.203  1.000 46.052  0 407 VAL EEE CG1 1 ? 19 
ATOM   5034 C CG2 . VAL E 2 78  ? 7.302   6.777   36.303  1.000 47.417  0 407 VAL EEE CG2 1 ? 19 
ATOM   5035 N N   . ARG E 2 79  ? 8.036   3.025   39.114  1.000 49.518  0 408 ARG EEE N   1 ? 19 
ATOM   5036 C CA  . ARG E 2 79  ? 8.788   2.080   39.984  1.000 52.251  0 408 ARG EEE CA  1 ? 19 
ATOM   5037 C C   . ARG E 2 79  ? 8.781   0.672   39.366  1.000 51.254  0 408 ARG EEE C   1 ? 19 
ATOM   5038 O O   . ARG E 2 79  ? 9.672   -0.116  39.720  1.000 54.987  0 408 ARG EEE O   1 ? 19 
ATOM   5039 C CB  . ARG E 2 79  ? 8.245   2.112   41.420  1.000 57.695  0 408 ARG EEE CB  1 ? 19 
ATOM   5040 C CG  . ARG E 2 79  ? 6.842   1.548   41.606  1.000 62.297  0 408 ARG EEE CG  1 ? 19 
ATOM   5041 C CD  . ARG E 2 79  ? 6.838   0.107   42.094  1.000 68.150  0 408 ARG EEE CD  1 ? 19 
ATOM   5042 N NE  . ARG E 2 79  ? 5.527   -0.520  41.938  1.000 72.700  0 408 ARG EEE NE  1 ? 19 
ATOM   5043 C CZ  . ARG E 2 79  ? 5.304   -1.831  41.810  1.000 75.153  0 408 ARG EEE CZ  1 ? 19 
ATOM   5044 N NH1 . ARG E 2 79  ? 6.307   -2.694  41.819  1.000 76.800  0 408 ARG EEE NH1 1 ? 19 
ATOM   5045 N NH2 . ARG E 2 79  ? 4.067   -2.276  41.661  1.000 76.747  0 408 ARG EEE NH2 1 ? 19 
ATOM   5046 N N   . GLN E 2 80  ? 7.831   0.364   38.474  1.000 47.549  0 409 GLN EEE N   1 ? 20 
ATOM   5047 C CA  . GLN E 2 80  ? 7.724   -0.957  37.790  1.000 46.343  0 409 GLN EEE CA  1 ? 20 
ATOM   5048 C C   . GLN E 2 80  ? 8.789   -1.092  36.698  1.000 43.986  0 409 GLN EEE C   1 ? 20 
ATOM   5049 O O   . GLN E 2 80  ? 9.069   -2.236  36.321  1.000 43.195  0 409 GLN EEE O   1 ? 20 
ATOM   5050 C CB  . GLN E 2 80  ? 6.350   -1.157  37.147  1.000 46.426  0 409 GLN EEE CB  1 ? 20 
ATOM   5051 C CG  . GLN E 2 80  ? 5.247   -1.475  38.141  1.000 47.102  0 409 GLN EEE CG  1 ? 20 
ATOM   5052 C CD  . GLN E 2 80  ? 3.966   -1.847  37.441  1.000 47.473  0 409 GLN EEE CD  1 ? 20 
ATOM   5053 O OE1 . GLN E 2 80  ? 3.961   -2.650  36.509  1.000 46.757  0 409 GLN EEE OE1 1 ? 20 
ATOM   5054 N NE2 . GLN E 2 80  ? 2.866   -1.261  37.891  1.000 49.520  0 409 GLN EEE NE2 1 ? 20 
ATOM   5055 N N   . ILE E 2 81  ? 9.336   0.021   36.197  1.000 43.155  0 410 ILE EEE N   1 ? 20 
ATOM   5056 C CA  . ILE E 2 81  ? 10.423  0.019   35.171  1.000 42.576  0 410 ILE EEE CA  1 ? 20 
ATOM   5057 C C   . ILE E 2 81  ? 11.760  -0.119  35.911  1.000 44.743  0 410 ILE EEE C   1 ? 20 
ATOM   5058 O O   . ILE E 2 81  ? 12.537  0.855   35.961  1.000 45.115  0 410 ILE EEE O   1 ? 20 
ATOM   5059 C CB  . ILE E 2 81  ? 10.366  1.264   34.261  1.000 42.408  0 410 ILE EEE CB  1 ? 20 
ATOM   5060 C CG1 . ILE E 2 81  ? 8.948   1.563   33.759  1.000 41.422  0 410 ILE EEE CG1 1 ? 20 
ATOM   5061 C CG2 . ILE E 2 81  ? 11.342  1.113   33.102  1.000 43.317  0 410 ILE EEE CG2 1 ? 20 
ATOM   5062 C CD1 . ILE E 2 81  ? 8.278   0.403   33.052  1.000 39.879  0 410 ILE EEE CD1 1 ? 20 
ATOM   5063 N N   . ALA E 2 82  ? 11.988  -1.300  36.484  1.000 44.702  0 411 ALA EEE N   1 ? 20 
ATOM   5064 C CA  . ALA E 2 82  ? 13.179  -1.658  37.281  1.000 47.465  0 411 ALA EEE CA  1 ? 20 
ATOM   5065 C C   . ALA E 2 82  ? 13.273  -3.178  37.352  1.000 48.307  0 411 ALA EEE C   1 ? 20 
ATOM   5066 O O   . ALA E 2 82  ? 12.270  -3.863  37.165  1.000 48.074  0 411 ALA EEE O   1 ? 20 
ATOM   5067 C CB  . ALA E 2 82  ? 13.091  -1.036  38.650  1.000 47.618  0 411 ALA EEE CB  1 ? 20 
ATOM   5068 N N   . PRO E 2 83  ? 14.472  -3.750  37.610  1.000 48.757  0 412 PRO EEE N   1 ? 20 
ATOM   5069 C CA  . PRO E 2 83  ? 14.632  -5.201  37.691  1.000 50.073  0 412 PRO EEE CA  1 ? 20 
ATOM   5070 C C   . PRO E 2 83  ? 13.774  -5.812  38.810  1.000 50.650  0 412 PRO EEE C   1 ? 20 
ATOM   5071 O O   . PRO E 2 83  ? 13.683  -5.213  39.865  1.000 52.935  0 412 PRO EEE O   1 ? 20 
ATOM   5072 C CB  . PRO E 2 83  ? 16.123  -5.431  38.010  1.000 51.426  0 412 PRO EEE CB  1 ? 20 
ATOM   5073 C CG  . PRO E 2 83  ? 16.799  -4.094  37.751  1.000 50.971  0 412 PRO EEE CG  1 ? 20 
ATOM   5074 C CD  . PRO E 2 83  ? 15.727  -3.029  37.859  1.000 49.898  0 412 PRO EEE CD  1 ? 20 
ATOM   5075 N N   . GLY E 2 84  ? 13.161  -6.969  38.543  1.000 50.525  0 413 GLY EEE N   1 ? 20 
ATOM   5076 C CA  . GLY E 2 84  ? 12.471  -7.813  39.538  1.000 51.611  0 413 GLY EEE CA  1 ? 20 
ATOM   5077 C C   . GLY E 2 84  ? 11.167  -7.208  40.035  1.000 50.586  0 413 GLY EEE C   1 ? 20 
ATOM   5078 O O   . GLY E 2 84  ? 10.725  -7.594  41.134  1.000 51.950  0 413 GLY EEE O   1 ? 20 
ATOM   5079 N N   . GLN E 2 85  ? 10.552  -6.317  39.254  1.000 48.532  0 414 GLN EEE N   1 ? 20 
ATOM   5080 C CA  . GLN E 2 85  ? 9.241   -5.694  39.579  1.000 48.329  0 414 GLN EEE CA  1 ? 20 
ATOM   5081 C C   . GLN E 2 85  ? 8.125   -6.496  38.907  1.000 48.097  0 414 GLN EEE C   1 ? 20 
ATOM   5082 O O   . GLN E 2 85  ? 8.397   -7.190  37.907  1.000 46.713  0 414 GLN EEE O   1 ? 20 
ATOM   5083 C CB  . GLN E 2 85  ? 9.184   -4.240  39.113  1.000 47.375  0 414 GLN EEE CB  1 ? 20 
ATOM   5084 C CG  . GLN E 2 85  ? 10.252  -3.371  39.749  1.000 48.930  0 414 GLN EEE CG  1 ? 20 
ATOM   5085 C CD  . GLN E 2 85  ? 10.110  -3.328  41.248  1.000 52.052  0 414 GLN EEE CD  1 ? 20 
ATOM   5086 O OE1 . GLN E 2 85  ? 9.062   -2.976  41.783  1.000 54.299  0 414 GLN EEE OE1 1 ? 20 
ATOM   5087 N NE2 . GLN E 2 85  ? 11.166  -3.710  41.944  1.000 55.378  0 414 GLN EEE NE2 1 ? 20 
ATOM   5088 N N   . THR E 2 86  ? 6.918   -6.393  39.465  1.000 49.199  0 415 THR EEE N   1 ? 20 
ATOM   5089 C CA  . THR E 2 86  ? 5.660   -6.969  38.926  1.000 48.374  0 415 THR EEE CA  1 ? 20 
ATOM   5090 C C   . THR E 2 86  ? 4.598   -5.864  38.909  1.000 47.546  0 415 THR EEE C   1 ? 20 
ATOM   5091 O O   . THR E 2 86  ? 4.859   -4.785  39.487  1.000 47.538  0 415 THR EEE O   1 ? 20 
ATOM   5092 C CB  . THR E 2 86  ? 5.246   -8.212  39.725  1.000 50.090  0 415 THR EEE CB  1 ? 20 
ATOM   5093 O OG1 . THR E 2 86  ? 4.897   -7.808  41.049  1.000 50.089  0 415 THR EEE OG1 1 ? 20 
ATOM   5094 C CG2 . THR E 2 86  ? 6.337   -9.260  39.785  1.000 50.761  0 415 THR EEE CG2 1 ? 20 
ATOM   5095 N N   . GLY E 2 87  ? 3.456   -6.138  38.270  1.000 47.721  0 416 GLY EEE N   1 ? 20 
ATOM   5096 C CA  . GLY E 2 87  ? 2.381   -5.168  37.978  1.000 46.572  0 416 GLY EEE CA  1 ? 20 
ATOM   5097 C C   . GLY E 2 87  ? 2.036   -5.187  36.501  1.000 45.923  0 416 GLY EEE C   1 ? 20 
ATOM   5098 O O   . GLY E 2 87  ? 2.764   -5.847  35.746  1.000 46.869  0 416 GLY EEE O   1 ? 20 
ATOM   5099 N N   . LYS E 2 88  ? 0.984   -4.472  36.097  1.000 47.445  0 417 LYS EEE N   1 ? 20 
ATOM   5100 C CA  . LYS E 2 88  ? 0.442   -4.496  34.710  1.000 47.881  0 417 LYS EEE CA  1 ? 20 
ATOM   5101 C C   . LYS E 2 88  ? 1.551   -4.138  33.715  1.000 46.182  0 417 LYS EEE C   1 ? 20 
ATOM   5102 O O   . LYS E 2 88  ? 1.584   -4.753  32.635  1.000 48.219  0 417 LYS EEE O   1 ? 20 
ATOM   5103 C CB  . LYS E 2 88  ? -0.738  -3.533  34.545  1.000 49.340  0 417 LYS EEE CB  1 ? 20 
ATOM   5104 C CG  . LYS E 2 88  ? -2.005  -3.913  35.297  1.000 53.878  0 417 LYS EEE CG  1 ? 20 
ATOM   5105 C CD  . LYS E 2 88  ? -2.634  -5.220  34.842  1.000 56.616  0 417 LYS EEE CD  1 ? 20 
ATOM   5106 C CE  . LYS E 2 88  ? -3.571  -5.831  35.865  1.000 59.212  0 417 LYS EEE CE  1 ? 20 
ATOM   5107 N NZ  . LYS E 2 88  ? -4.337  -6.955  35.274  1.000 61.821  0 417 LYS EEE NZ  1 ? 20 
ATOM   5108 N N   . ILE E 2 89  ? 2.427   -3.191  34.063  1.000 43.225  0 418 ILE EEE N   1 ? 20 
ATOM   5109 C CA  . ILE E 2 89  ? 3.449   -2.643  33.123  1.000 42.234  0 418 ILE EEE CA  1 ? 20 
ATOM   5110 C C   . ILE E 2 89  ? 4.588   -3.657  32.976  1.000 42.234  0 418 ILE EEE C   1 ? 20 
ATOM   5111 O O   . ILE E 2 89  ? 4.855   -4.073  31.830  1.000 42.466  0 418 ILE EEE O   1 ? 20 
ATOM   5112 C CB  . ILE E 2 89  ? 3.954   -1.258  33.567  1.000 41.236  0 418 ILE EEE CB  1 ? 20 
ATOM   5113 C CG1 . ILE E 2 89  ? 2.802   -0.276  33.812  1.000 41.509  0 418 ILE EEE CG1 1 ? 20 
ATOM   5114 C CG2 . ILE E 2 89  ? 4.944   -0.717  32.548  1.000 41.122  0 418 ILE EEE CG2 1 ? 20 
ATOM   5115 C CD1 . ILE E 2 89  ? 1.841   -0.127  32.645  1.000 41.055  0 418 ILE EEE CD1 1 ? 20 
ATOM   5116 N N   . ALA E 2 90  ? 5.228   -4.027  34.090  1.000 41.230  0 419 ALA EEE N   1 ? 20 
ATOM   5117 C CA  . ALA E 2 90  ? 6.343   -5.003  34.145  1.000 42.164  0 419 ALA EEE CA  1 ? 20 
ATOM   5118 C C   . ALA E 2 90  ? 5.904   -6.337  33.531  1.000 42.689  0 419 ALA EEE C   1 ? 20 
ATOM   5119 O O   . ALA E 2 90  ? 6.705   -6.946  32.797  1.000 41.642  0 419 ALA EEE O   1 ? 20 
ATOM   5120 C CB  . ALA E 2 90  ? 6.801   -5.194  35.569  1.000 43.573  0 419 ALA EEE CB  1 ? 20 
ATOM   5121 N N   . ASP E 2 91  ? 4.674   -6.767  33.817  1.000 42.751  0 420 ASP EEE N   1 ? 20 
ATOM   5122 C CA  . ASP E 2 91  ? 4.142   -8.098  33.425  1.000 45.773  0 420 ASP EEE CA  1 ? 20 
ATOM   5123 C C   . ASP E 2 91  ? 3.772   -8.109  31.937  1.000 46.469  0 420 ASP EEE C   1 ? 20 
ATOM   5124 O O   . ASP E 2 91  ? 4.151   -9.084  31.254  1.000 47.744  0 420 ASP EEE O   1 ? 20 
ATOM   5125 C CB  . ASP E 2 91  ? 2.931   -8.485  34.277  1.000 47.637  0 420 ASP EEE CB  1 ? 20 
ATOM   5126 C CG  . ASP E 2 91  ? 3.236   -8.749  35.741  1.000 49.530  0 420 ASP EEE CG  1 ? 20 
ATOM   5127 O OD1 . ASP E 2 91  ? 4.431   -8.784  36.101  1.000 49.927  0 420 ASP EEE OD1 1 ? 20 
ATOM   5128 O OD2 . ASP E 2 91  ? 2.268   -8.910  36.508  1.000 52.543  0 420 ASP EEE OD2 1 ? 20 
ATOM   5129 N N   . TYR E 2 92  ? 3.036   -7.095  31.460  1.000 45.961  0 421 TYR EEE N   1 ? 20 
ATOM   5130 C CA  . TYR E 2 92  ? 2.284   -7.148  30.175  1.000 46.228  0 421 TYR EEE CA  1 ? 20 
ATOM   5131 C C   . TYR E 2 92  ? 2.745   -6.096  29.154  1.000 46.901  0 421 TYR EEE C   1 ? 20 
ATOM   5132 O O   . TYR E 2 92  ? 2.287   -6.205  28.003  1.000 47.210  0 421 TYR EEE O   1 ? 20 
ATOM   5133 C CB  . TYR E 2 92  ? 0.782   -6.960  30.414  1.000 44.856  0 421 TYR EEE CB  1 ? 20 
ATOM   5134 C CG  . TYR E 2 92  ? 0.126   -7.963  31.332  1.000 45.357  0 421 TYR EEE CG  1 ? 20 
ATOM   5135 C CD1 . TYR E 2 92  ? 0.648   -9.234  31.527  1.000 46.010  0 421 TYR EEE CD1 1 ? 20 
ATOM   5136 C CD2 . TYR E 2 92  ? -1.043  -7.643  32.003  1.000 45.294  0 421 TYR EEE CD2 1 ? 20 
ATOM   5137 C CE1 . TYR E 2 92  ? 0.032   -10.148 32.368  1.000 47.149  0 421 TYR EEE CE1 1 ? 20 
ATOM   5138 C CE2 . TYR E 2 92  ? -1.681  -8.550  32.834  1.000 45.930  0 421 TYR EEE CE2 1 ? 20 
ATOM   5139 C CZ  . TYR E 2 92  ? -1.136  -9.806  33.025  1.000 47.061  0 421 TYR EEE CZ  1 ? 20 
ATOM   5140 O OH  . TYR E 2 92  ? -1.756  -10.702 33.846  1.000 48.194  0 421 TYR EEE OH  1 ? 20 
ATOM   5141 N N   . ASN E 2 93  ? 3.597   -5.129  29.515  1.000 45.586  0 422 ASN EEE N   1 ? 20 
ATOM   5142 C CA  . ASN E 2 93  ? 3.889   -3.974  28.619  1.000 44.562  0 422 ASN EEE CA  1 ? 20 
ATOM   5143 C C   . ASN E 2 93  ? 5.390   -3.856  28.340  1.000 45.041  0 422 ASN EEE C   1 ? 20 
ATOM   5144 O O   . ASN E 2 93  ? 5.768   -3.926  27.154  1.000 46.687  0 422 ASN EEE O   1 ? 20 
ATOM   5145 C CB  . ASN E 2 93  ? 3.291   -2.682  29.171  1.000 42.896  0 422 ASN EEE CB  1 ? 20 
ATOM   5146 C CG  . ASN E 2 93  ? 1.779   -2.713  29.120  1.000 43.424  0 422 ASN EEE CG  1 ? 20 
ATOM   5147 O OD1 . ASN E 2 93  ? 1.174   -2.245  28.160  1.000 40.289  0 422 ASN EEE OD1 1 ? 20 
ATOM   5148 N ND2 . ASN E 2 93  ? 1.163   -3.307  30.128  1.000 43.972  0 422 ASN EEE ND2 1 ? 20 
ATOM   5149 N N   . TYR E 2 94  ? 6.197   -3.650  29.379  1.000 44.037  0 423 TYR EEE N   1 ? 20 
ATOM   5150 C CA  . TYR E 2 94  ? 7.664   -3.460  29.271  1.000 42.917  0 423 TYR EEE CA  1 ? 20 
ATOM   5151 C C   . TYR E 2 94  ? 8.334   -4.090  30.496  1.000 42.582  0 423 TYR EEE C   1 ? 20 
ATOM   5152 O O   . TYR E 2 94  ? 8.044   -3.655  31.623  1.000 43.778  0 423 TYR EEE O   1 ? 20 
ATOM   5153 C CB  . TYR E 2 94  ? 8.002   -1.974  29.113  1.000 42.136  0 423 TYR EEE CB  1 ? 20 
ATOM   5154 C CG  . TYR E 2 94  ? 9.458   -1.715  28.837  1.000 42.705  0 423 TYR EEE CG  1 ? 20 
ATOM   5155 C CD1 . TYR E 2 94  ? 9.962   -1.768  27.548  1.000 43.933  0 423 TYR EEE CD1 1 ? 20 
ATOM   5156 C CD2 . TYR E 2 94  ? 10.341  -1.461  29.872  1.000 42.620  0 423 TYR EEE CD2 1 ? 20 
ATOM   5157 C CE1 . TYR E 2 94  ? 11.304  -1.548  27.290  1.000 44.774  0 423 TYR EEE CE1 1 ? 20 
ATOM   5158 C CE2 . TYR E 2 94  ? 11.688  -1.251  29.635  1.000 44.231  0 423 TYR EEE CE2 1 ? 20 
ATOM   5159 C CZ  . TYR E 2 94  ? 12.171  -1.291  28.339  1.000 45.767  0 423 TYR EEE CZ  1 ? 20 
ATOM   5160 O OH  . TYR E 2 94  ? 13.497  -1.074  28.105  1.000 45.360  0 423 TYR EEE OH  1 ? 20 
ATOM   5161 N N   . LYS E 2 95  ? 9.188   -5.088  30.259  1.000 41.623  0 424 LYS EEE N   1 ? 20 
ATOM   5162 C CA  . LYS E 2 95  ? 9.847   -5.924  31.290  1.000 43.132  0 424 LYS EEE CA  1 ? 20 
ATOM   5163 C C   . LYS E 2 95  ? 11.366  -5.768  31.179  1.000 43.679  0 424 LYS EEE C   1 ? 20 
ATOM   5164 O O   . LYS E 2 95  ? 11.926  -6.204  30.160  1.000 43.845  0 424 LYS EEE O   1 ? 20 
ATOM   5165 C CB  . LYS E 2 95  ? 9.447   -7.390  31.095  1.000 45.055  0 424 LYS EEE CB  1 ? 20 
ATOM   5166 C CG  . LYS E 2 95  ? 10.067  -8.379  32.075  1.000 46.763  0 424 LYS EEE CG  1 ? 20 
ATOM   5167 C CD  . LYS E 2 95  ? 9.912   -7.968  33.520  1.000 47.272  0 424 LYS EEE CD  1 ? 20 
ATOM   5168 C CE  . LYS E 2 95  ? 10.343  -9.035  34.500  1.000 49.451  0 424 LYS EEE CE  1 ? 20 
ATOM   5169 N NZ  . LYS E 2 95  ? 10.135  -8.579  35.893  1.000 51.163  0 424 LYS EEE NZ  1 ? 20 
ATOM   5170 N N   . LEU E 2 96  ? 12.002  -5.169  32.189  1.000 44.209  0 425 LEU EEE N   1 ? 20 
ATOM   5171 C CA  . LEU E 2 96  ? 13.482  -5.188  32.350  1.000 47.316  0 425 LEU EEE CA  1 ? 20 
ATOM   5172 C C   . LEU E 2 96  ? 13.892  -6.560  32.873  1.000 48.827  0 425 LEU EEE C   1 ? 20 
ATOM   5173 O O   . LEU E 2 96  ? 13.144  -7.184  33.624  1.000 50.267  0 425 LEU EEE O   1 ? 20 
ATOM   5174 C CB  . LEU E 2 96  ? 13.931  -4.086  33.316  1.000 46.775  0 425 LEU EEE CB  1 ? 20 
ATOM   5175 C CG  . LEU E 2 96  ? 13.805  -2.653  32.805  1.000 46.836  0 425 LEU EEE CG  1 ? 20 
ATOM   5176 C CD1 . LEU E 2 96  ? 14.481  -1.699  33.776  1.000 47.515  0 425 LEU EEE CD1 1 ? 20 
ATOM   5177 C CD2 . LEU E 2 96  ? 14.398  -2.508  31.411  1.000 48.622  0 425 LEU EEE CD2 1 ? 20 
ATOM   5178 N N   . PRO E 2 97  ? 15.070  -7.087  32.470  1.000 51.329  0 426 PRO EEE N   1 ? 20 
ATOM   5179 C CA  . PRO E 2 97  ? 15.573  -8.340  33.027  1.000 53.137  0 426 PRO EEE CA  1 ? 20 
ATOM   5180 C C   . PRO E 2 97  ? 16.063  -8.150  34.469  1.000 54.091  0 426 PRO EEE C   1 ? 20 
ATOM   5181 O O   . PRO E 2 97  ? 16.461  -7.050  34.824  1.000 50.879  0 426 PRO EEE O   1 ? 20 
ATOM   5182 C CB  . PRO E 2 97  ? 16.737  -8.718  32.100  1.000 54.738  0 426 PRO EEE CB  1 ? 20 
ATOM   5183 C CG  . PRO E 2 97  ? 17.201  -7.401  31.520  1.000 54.291  0 426 PRO EEE CG  1 ? 20 
ATOM   5184 C CD  . PRO E 2 97  ? 15.968  -6.521  31.449  1.000 52.620  0 426 PRO EEE CD  1 ? 20 
ATOM   5185 N N   . ASP E 2 98  ? 16.034  -9.228  35.254  1.000 56.227  0 427 ASP EEE N   1 ? 20 
ATOM   5186 C CA  . ASP E 2 98  ? 16.533  -9.249  36.655  1.000 59.206  0 427 ASP EEE CA  1 ? 20 
ATOM   5187 C C   . ASP E 2 98  ? 17.957  -8.676  36.681  1.000 60.524  0 427 ASP EEE C   1 ? 20 
ATOM   5188 O O   . ASP E 2 98  ? 18.287  -7.953  37.640  1.000 59.987  0 427 ASP EEE O   1 ? 20 
ATOM   5189 C CB  . ASP E 2 98  ? 16.465  -10.657 37.254  1.000 62.073  0 427 ASP EEE CB  1 ? 20 
ATOM   5190 C CG  . ASP E 2 98  ? 15.056  -11.180 37.502  1.000 61.779  0 427 ASP EEE CG  1 ? 20 
ATOM   5191 O OD1 . ASP E 2 98  ? 14.097  -10.395 37.378  1.000 61.923  0 427 ASP EEE OD1 1 ? 20 
ATOM   5192 O OD2 . ASP E 2 98  ? 14.925  -12.377 37.807  1.000 64.545  0 427 ASP EEE OD2 1 ? 20 
ATOM   5193 N N   . ASP E 2 99  ? 18.757  -8.965  35.648  1.000 62.407  0 428 ASP EEE N   1 ? 20 
ATOM   5194 C CA  . ASP E 2 99  ? 20.198  -8.593  35.567  1.000 63.988  0 428 ASP EEE CA  1 ? 20 
ATOM   5195 C C   . ASP E 2 99  ? 20.382  -7.374  34.652  1.000 60.891  0 428 ASP EEE C   1 ? 20 
ATOM   5196 O O   . ASP E 2 99  ? 21.468  -7.241  34.058  1.000 63.823  0 428 ASP EEE O   1 ? 20 
ATOM   5197 C CB  . ASP E 2 99  ? 21.050  -9.787  35.115  1.000 67.747  0 428 ASP EEE CB  1 ? 20 
ATOM   5198 C CG  . ASP E 2 99  ? 20.793  -10.272 33.694  1.000 69.928  0 428 ASP EEE CG  1 ? 20 
ATOM   5199 O OD1 . ASP E 2 99  ? 19.778  -9.858  33.093  1.000 67.779  0 428 ASP EEE OD1 1 ? 20 
ATOM   5200 O OD2 . ASP E 2 99  ? 21.611  -11.071 33.200  1.000 73.126  0 428 ASP EEE OD2 1 ? 20 
ATOM   5201 N N   . PHE E 2 100 ? 19.381  -6.495  34.569  1.000 57.054  0 429 PHE EEE N   1 ? 20 
ATOM   5202 C CA  . PHE E 2 100 ? 19.410  -5.276  33.718  1.000 56.250  0 429 PHE EEE CA  1 ? 20 
ATOM   5203 C C   . PHE E 2 100 ? 20.681  -4.469  33.990  1.000 59.131  0 429 PHE EEE C   1 ? 20 
ATOM   5204 O O   . PHE E 2 100 ? 20.999  -4.178  35.152  1.000 60.737  0 429 PHE EEE O   1 ? 20 
ATOM   5205 C CB  . PHE E 2 100 ? 18.174  -4.404  33.935  1.000 52.142  0 429 PHE EEE CB  1 ? 20 
ATOM   5206 C CG  . PHE E 2 100 ? 18.211  -3.080  33.215  1.000 50.006  0 429 PHE EEE CG  1 ? 20 
ATOM   5207 C CD1 . PHE E 2 100 ? 18.097  -3.006  31.835  1.000 49.889  0 429 PHE EEE CD1 1 ? 20 
ATOM   5208 C CD2 . PHE E 2 100 ? 18.357  -1.903  33.924  1.000 48.870  0 429 PHE EEE CD2 1 ? 20 
ATOM   5209 C CE1 . PHE E 2 100 ? 18.133  -1.782  31.183  1.000 48.592  0 429 PHE EEE CE1 1 ? 20 
ATOM   5210 C CE2 . PHE E 2 100 ? 18.376  -0.679  33.274  1.000 48.066  0 429 PHE EEE CE2 1 ? 20 
ATOM   5211 C CZ  . PHE E 2 100 ? 18.273  -0.619  31.906  1.000 48.282  0 429 PHE EEE CZ  1 ? 20 
ATOM   5212 N N   . THR E 2 101 ? 21.386  -4.134  32.911  1.000 62.241  0 430 THR EEE N   1 ? 20 
ATOM   5213 C CA  . THR E 2 101 ? 22.532  -3.191  32.875  1.000 63.143  0 430 THR EEE CA  1 ? 20 
ATOM   5214 C C   . THR E 2 101 ? 22.116  -1.958  32.072  1.000 61.955  0 430 THR EEE C   1 ? 20 
ATOM   5215 O O   . THR E 2 101 ? 21.872  -2.115  30.855  1.000 64.067  0 430 THR EEE O   1 ? 20 
ATOM   5216 C CB  . THR E 2 101 ? 23.759  -3.851  32.240  1.000 66.212  0 430 THR EEE CB  1 ? 20 
ATOM   5217 O OG1 . THR E 2 101 ? 24.280  -4.788  33.181  1.000 69.594  0 430 THR EEE OG1 1 ? 20 
ATOM   5218 C CG2 . THR E 2 101 ? 24.820  -2.852  31.827  1.000 67.682  0 430 THR EEE CG2 1 ? 20 
ATOM   5219 N N   . GLY E 2 102 ? 22.038  -0.799  32.720  1.000 59.117  0 431 GLY EEE N   1 ? 20 
ATOM   5220 C CA  . GLY E 2 102 ? 21.732  0.473   32.051  1.000 57.072  0 431 GLY EEE CA  1 ? 20 
ATOM   5221 C C   . GLY E 2 102 ? 21.092  1.472   32.986  1.000 55.352  0 431 GLY EEE C   1 ? 20 
ATOM   5222 O O   . GLY E 2 102 ? 21.218  1.314   34.214  1.000 54.365  0 431 GLY EEE O   1 ? 20 
ATOM   5223 N N   . CYS E 2 103 ? 20.403  2.458   32.414  1.000 54.241  0 432 CYS EEE N   1 ? 20 
ATOM   5224 C CA  . CYS E 2 103 ? 19.771  3.576   33.153  1.000 53.047  0 432 CYS EEE CA  1 ? 20 
ATOM   5225 C C   . CYS E 2 103 ? 18.301  3.677   32.750  1.000 51.082  0 432 CYS EEE C   1 ? 20 
ATOM   5226 O O   . CYS E 2 103 ? 17.995  3.467   31.568  1.000 52.629  0 432 CYS EEE O   1 ? 20 
ATOM   5227 C CB  . CYS E 2 103 ? 20.535  4.872   32.910  1.000 55.119  0 432 CYS EEE CB  1 ? 20 
ATOM   5228 S SG  . CYS E 2 103 ? 22.270  4.758   33.425  1.000 58.642  0 432 CYS EEE SG  1 ? 20 
ATOM   5229 N N   . VAL E 2 104 ? 17.427  3.916   33.728  1.000 49.003  0 433 VAL EEE N   1 ? 20 
ATOM   5230 C CA  . VAL E 2 104 ? 15.986  4.223   33.516  1.000 45.800  0 433 VAL EEE CA  1 ? 20 
ATOM   5231 C C   . VAL E 2 104 ? 15.808  5.712   33.814  1.000 46.896  0 433 VAL EEE C   1 ? 20 
ATOM   5232 O O   . VAL E 2 104 ? 16.097  6.129   34.956  1.000 48.890  0 433 VAL EEE O   1 ? 20 
ATOM   5233 C CB  . VAL E 2 104 ? 15.081  3.338   34.394  1.000 44.306  0 433 VAL EEE CB  1 ? 20 
ATOM   5234 C CG1 . VAL E 2 104 ? 13.625  3.774   34.317  1.000 43.458  0 433 VAL EEE CG1 1 ? 20 
ATOM   5235 C CG2 . VAL E 2 104 ? 15.223  1.869   34.034  1.000 43.286  0 433 VAL EEE CG2 1 ? 20 
ATOM   5236 N N   . ILE E 2 105 ? 15.403  6.481   32.802  1.000 46.928  0 434 ILE EEE N   1 ? 20 
ATOM   5237 C CA  . ILE E 2 105 ? 15.248  7.961   32.879  1.000 48.142  0 434 ILE EEE CA  1 ? 20 
ATOM   5238 C C   . ILE E 2 105 ? 13.764  8.276   32.677  1.000 47.694  0 434 ILE EEE C   1 ? 20 
ATOM   5239 O O   . ILE E 2 105 ? 13.187  7.791   31.688  1.000 46.269  0 434 ILE EEE O   1 ? 20 
ATOM   5240 C CB  . ILE E 2 105 ? 16.154  8.665   31.849  1.000 49.785  0 434 ILE EEE CB  1 ? 20 
ATOM   5241 C CG1 . ILE E 2 105 ? 17.602  8.168   31.927  1.000 51.541  0 434 ILE EEE CG1 1 ? 20 
ATOM   5242 C CG2 . ILE E 2 105 ? 16.071  10.168  32.017  1.000 51.561  0 434 ILE EEE CG2 1 ? 20 
ATOM   5243 C CD1 . ILE E 2 105 ? 18.437  8.483   30.705  1.000 54.178  0 434 ILE EEE CD1 1 ? 20 
ATOM   5244 N N   . ALA E 2 106 ? 13.166  9.018   33.612  1.000 48.824  0 435 ALA EEE N   1 ? 20 
ATOM   5245 C CA  . ALA E 2 106 ? 11.733  9.389   33.604  1.000 48.372  0 435 ALA EEE CA  1 ? 20 
ATOM   5246 C C   . ALA E 2 106 ? 11.567  10.827  34.096  1.000 50.731  0 435 ALA EEE C   1 ? 20 
ATOM   5247 O O   . ALA E 2 106 ? 12.335  11.254  34.986  1.000 52.153  0 435 ALA EEE O   1 ? 20 
ATOM   5248 C CB  . ALA E 2 106 ? 10.939  8.422   34.446  1.000 47.826  0 435 ALA EEE CB  1 ? 20 
ATOM   5249 N N   . TRP E 2 107 ? 10.598  11.540  33.521  1.000 52.336  0 436 TRP EEE N   1 ? 20 
ATOM   5250 C CA  . TRP E 2 107 ? 10.204  12.912  33.927  1.000 55.207  0 436 TRP EEE CA  1 ? 20 
ATOM   5251 C C   . TRP E 2 107 ? 8.699   13.086  33.706  1.000 54.780  0 436 TRP EEE C   1 ? 20 
ATOM   5252 O O   . TRP E 2 107 ? 8.150   12.419  32.810  1.000 54.756  0 436 TRP EEE O   1 ? 20 
ATOM   5253 C CB  . TRP E 2 107 ? 11.033  13.961  33.171  1.000 58.577  0 436 TRP EEE CB  1 ? 20 
ATOM   5254 C CG  . TRP E 2 107 ? 10.829  13.982  31.685  1.000 58.241  0 436 TRP EEE CG  1 ? 20 
ATOM   5255 C CD1 . TRP E 2 107 ? 10.049  14.852  30.979  1.000 59.108  0 436 TRP EEE CD1 1 ? 20 
ATOM   5256 C CD2 . TRP E 2 107 ? 11.437  13.112  30.712  1.000 56.913  0 436 TRP EEE CD2 1 ? 20 
ATOM   5257 N NE1 . TRP E 2 107 ? 10.112  14.573  29.642  1.000 59.723  0 436 TRP EEE NE1 1 ? 20 
ATOM   5258 C CE2 . TRP E 2 107 ? 10.956  13.513  29.445  1.000 58.344  0 436 TRP EEE CE2 1 ? 20 
ATOM   5259 C CE3 . TRP E 2 107 ? 12.319  12.028  30.784  1.000 55.628  0 436 TRP EEE CE3 1 ? 20 
ATOM   5260 C CZ2 . TRP E 2 107 ? 11.336  12.873  28.266  1.000 58.176  0 436 TRP EEE CZ2 1 ? 20 
ATOM   5261 C CZ3 . TRP E 2 107 ? 12.695  11.395  29.619  1.000 56.327  0 436 TRP EEE CZ3 1 ? 20 
ATOM   5262 C CH2 . TRP E 2 107 ? 12.207  11.812  28.378  1.000 57.208  0 436 TRP EEE CH2 1 ? 20 
ATOM   5263 N N   . ASN E 2 108 ? 8.069   13.922  34.532  1.000 57.039  0 437 ASN EEE N   1 ? 20 
ATOM   5264 C CA  . ASN E 2 108 ? 6.635   14.304  34.446  1.000 56.797  0 437 ASN EEE CA  1 ? 20 
ATOM   5265 C C   . ASN E 2 108 ? 6.418   15.037  33.117  1.000 57.799  0 437 ASN EEE C   1 ? 20 
ATOM   5266 O O   . ASN E 2 108 ? 7.154   16.000  32.854  1.000 60.783  0 437 ASN EEE O   1 ? 20 
ATOM   5267 C CB  . ASN E 2 108 ? 6.230   15.146  35.659  1.000 59.262  0 437 ASN EEE CB  1 ? 20 
ATOM   5268 C CG  . ASN E 2 108 ? 4.743   15.409  35.732  1.000 60.164  0 437 ASN EEE CG  1 ? 20 
ATOM   5269 O OD1 . ASN E 2 108 ? 4.180   16.035  34.837  1.000 60.862  0 437 ASN EEE OD1 1 ? 20 
ATOM   5270 N ND2 . ASN E 2 108 ? 4.105   14.948  36.797  1.000 60.084  0 437 ASN EEE ND2 1 ? 20 
ATOM   5271 N N   . SER E 2 109 ? 5.462   14.581  32.305  1.000 57.080  0 438 SER EEE N   1 ? 20 
ATOM   5272 C CA  . SER E 2 109 ? 5.157   15.127  30.954  1.000 57.018  0 438 SER EEE CA  1 ? 20 
ATOM   5273 C C   . SER E 2 109 ? 3.727   15.683  30.908  1.000 57.713  0 438 SER EEE C   1 ? 20 
ATOM   5274 O O   . SER E 2 109 ? 3.152   15.764  29.796  1.000 58.678  0 438 SER EEE O   1 ? 20 
ATOM   5275 C CB  . SER E 2 109 ? 5.371   14.068  29.910  1.000 54.644  0 438 SER EEE CB  1 ? 20 
ATOM   5276 O OG  . SER E 2 109 ? 4.485   12.976  30.109  1.000 52.992  0 438 SER EEE OG  1 ? 20 
ATOM   5277 N N   . ASN E 2 110 ? 3.190   16.076  32.067  1.000 57.838  0 439 ASN EEE N   1 ? 20 
ATOM   5278 C CA  . ASN E 2 110 ? 1.798   16.578  32.230  1.000 59.015  0 439 ASN EEE CA  1 ? 20 
ATOM   5279 C C   . ASN E 2 110 ? 1.559   17.739  31.256  1.000 61.706  0 439 ASN EEE C   1 ? 20 
ATOM   5280 O O   . ASN E 2 110 ? 0.471   17.789  30.658  1.000 62.124  0 439 ASN EEE O   1 ? 20 
ATOM   5281 C CB  . ASN E 2 110 ? 1.518   16.987  33.678  1.000 60.288  0 439 ASN EEE CB  1 ? 20 
ATOM   5282 C CG  . ASN E 2 110 ? 0.046   17.067  34.018  1.000 60.870  0 439 ASN EEE CG  1 ? 20 
ATOM   5283 O OD1 . ASN E 2 110 ? -0.753  16.245  33.573  1.000 58.516  0 439 ASN EEE OD1 1 ? 20 
ATOM   5284 N ND2 . ASN E 2 110 ? -0.313  18.035  34.844  1.000 64.335  0 439 ASN EEE ND2 1 ? 20 
ATOM   5285 N N   . ASN E 2 111 ? 2.550   18.619  31.088  1.000 64.772  0 440 ASN EEE N   1 ? 20 
ATOM   5286 C CA  . ASN E 2 111 ? 2.454   19.842  30.245  1.000 69.550  0 440 ASN EEE CA  1 ? 20 
ATOM   5287 C C   . ASN E 2 111 ? 2.380   19.460  28.759  1.000 68.760  0 440 ASN EEE C   1 ? 20 
ATOM   5288 O O   . ASN E 2 111 ? 1.855   20.274  27.979  1.000 70.257  0 440 ASN EEE O   1 ? 20 
ATOM   5289 C CB  . ASN E 2 111 ? 3.617   20.802  30.503  1.000 74.055  0 440 ASN EEE CB  1 ? 20 
ATOM   5290 C CG  . ASN E 2 111 ? 4.963   20.220  30.114  1.000 76.227  0 440 ASN EEE CG  1 ? 20 
ATOM   5291 O OD1 . ASN E 2 111 ? 5.301   19.103  30.505  1.000 77.342  0 440 ASN EEE OD1 1 ? 20 
ATOM   5292 N ND2 . ASN E 2 111 ? 5.745   20.966  29.349  1.000 79.955  0 440 ASN EEE ND2 1 ? 20 
ATOM   5293 N N   . LEU E 2 112 ? 2.890   18.282  28.380  1.000 66.081  0 441 LEU EEE N   1 ? 20 
ATOM   5294 C CA  . LEU E 2 112 ? 2.965   17.815  26.967  1.000 66.500  0 441 LEU EEE CA  1 ? 20 
ATOM   5295 C C   . LEU E 2 112 ? 1.827   16.834  26.656  1.000 64.726  0 441 LEU EEE C   1 ? 20 
ATOM   5296 O O   . LEU E 2 112 ? 1.249   16.941  25.558  1.000 64.514  0 441 LEU EEE O   1 ? 20 
ATOM   5297 C CB  . LEU E 2 112 ? 4.320   17.136  26.729  1.000 65.794  0 441 LEU EEE CB  1 ? 20 
ATOM   5298 C CG  . LEU E 2 112 ? 5.552   18.037  26.820  1.000 68.001  0 441 LEU EEE CG  1 ? 20 
ATOM   5299 C CD1 . LEU E 2 112 ? 6.821   17.204  26.869  1.000 66.858  0 441 LEU EEE CD1 1 ? 20 
ATOM   5300 C CD2 . LEU E 2 112 ? 5.604   19.017  25.659  1.000 70.844  0 441 LEU EEE CD2 1 ? 20 
ATOM   5301 N N   . ASP E 2 113 ? 1.543   15.897  27.568  1.000 63.000  0 442 ASP EEE N   1 ? 20 
ATOM   5302 C CA  . ASP E 2 113 ? 0.802   14.642  27.266  1.000 60.760  0 442 ASP EEE CA  1 ? 20 
ATOM   5303 C C   . ASP E 2 113 ? -0.602  14.641  27.893  1.000 61.290  0 442 ASP EEE C   1 ? 20 
ATOM   5304 O O   . ASP E 2 113 ? -1.349  13.673  27.639  1.000 60.531  0 442 ASP EEE O   1 ? 20 
ATOM   5305 C CB  . ASP E 2 113 ? 1.629   13.432  27.703  1.000 57.155  0 442 ASP EEE CB  1 ? 20 
ATOM   5306 C CG  . ASP E 2 113 ? 2.858   13.202  26.838  1.000 56.244  0 442 ASP EEE CG  1 ? 20 
ATOM   5307 O OD1 . ASP E 2 113 ? 2.730   13.272  25.601  1.000 58.299  0 442 ASP EEE OD1 1 ? 20 
ATOM   5308 O OD2 . ASP E 2 113 ? 3.934   12.960  27.403  1.000 53.808  0 442 ASP EEE OD2 1 ? 20 
ATOM   5309 N N   . SER E 2 114 ? -0.960  15.669  28.669  1.000 62.012  0 443 SER EEE N   1 ? 20 
ATOM   5310 C CA  . SER E 2 114 ? -2.332  15.864  29.205  1.000 62.666  0 443 SER EEE CA  1 ? 20 
ATOM   5311 C C   . SER E 2 114 ? -3.035  16.966  28.402  1.000 66.356  0 443 SER EEE C   1 ? 20 
ATOM   5312 O O   . SER E 2 114 ? -2.331  17.843  27.864  1.000 66.560  0 443 SER EEE O   1 ? 20 
ATOM   5313 C CB  . SER E 2 114 ? -2.309  16.162  30.683  1.000 62.653  0 443 SER EEE CB  1 ? 20 
ATOM   5314 O OG  . SER E 2 114 ? -2.150  17.552  30.929  1.000 65.474  0 443 SER EEE OG  1 ? 20 
ATOM   5315 N N   . LYS E 2 115 ? -4.366  16.892  28.304  1.000 68.394  0 444 LYS EEE N   1 ? 20 
ATOM   5316 C CA  . LYS E 2 115 ? -5.228  17.881  27.602  1.000 72.554  0 444 LYS EEE CA  1 ? 20 
ATOM   5317 C C   . LYS E 2 115 ? -6.523  18.061  28.400  1.000 72.961  0 444 LYS EEE C   1 ? 20 
ATOM   5318 O O   . LYS E 2 115 ? -7.007  17.063  28.961  1.000 70.024  0 444 LYS EEE O   1 ? 20 
ATOM   5319 C CB  . LYS E 2 115 ? -5.547  17.413  26.178  1.000 74.601  0 444 LYS EEE CB  1 ? 20 
ATOM   5320 C CG  . LYS E 2 115 ? -4.380  17.412  25.200  1.000 77.856  0 444 LYS EEE CG  1 ? 20 
ATOM   5321 C CD  . LYS E 2 115 ? -4.705  16.712  23.892  1.000 79.722  0 444 LYS EEE CD  1 ? 20 
ATOM   5322 C CE  . LYS E 2 115 ? -3.492  16.096  23.221  1.000 79.254  0 444 LYS EEE CE  1 ? 20 
ATOM   5323 N NZ  . LYS E 2 115 ? -3.879  15.150  22.146  1.000 77.080  0 444 LYS EEE NZ  1 ? 20 
ATOM   5324 N N   . VAL E 2 116 ? -7.051  19.288  28.454  1.000 77.027  0 445 VAL EEE N   1 ? 20 
ATOM   5325 C CA  . VAL E 2 116 ? -8.416  19.593  28.981  1.000 78.803  0 445 VAL EEE CA  1 ? 20 
ATOM   5326 C C   . VAL E 2 116 ? -9.415  18.691  28.244  1.000 76.636  0 445 VAL EEE C   1 ? 20 
ATOM   5327 O O   . VAL E 2 116 ? -9.353  18.640  27.002  1.000 75.939  0 445 VAL EEE O   1 ? 20 
ATOM   5328 C CB  . VAL E 2 116 ? -8.779  21.086  28.839  1.000 83.383  0 445 VAL EEE CB  1 ? 20 
ATOM   5329 C CG1 . VAL E 2 116 ? -8.127  21.924  29.928  1.000 85.443  0 445 VAL EEE CG1 1 ? 20 
ATOM   5330 C CG2 . VAL E 2 116 ? -8.445  21.648  27.462  1.000 84.597  0 445 VAL EEE CG2 1 ? 20 
ATOM   5331 N N   . GLY E 2 117 ? -10.272 17.985  28.988  1.000 74.118  0 446 GLY EEE N   1 ? 20 
ATOM   5332 C CA  . GLY E 2 117 ? -11.158 16.928  28.461  1.000 71.469  0 446 GLY EEE CA  1 ? 20 
ATOM   5333 C C   . GLY E 2 117 ? -10.512 15.555  28.563  1.000 67.248  0 446 GLY EEE C   1 ? 20 
ATOM   5334 O O   . GLY E 2 117 ? -11.250 14.552  28.565  1.000 67.280  0 446 GLY EEE O   1 ? 20 
ATOM   5335 N N   . GLY E 2 118 ? -9.179  15.509  28.645  1.000 64.982  0 447 GLY EEE N   1 ? 20 
ATOM   5336 C CA  . GLY E 2 118 ? -8.385  14.276  28.805  1.000 60.963  0 447 GLY EEE CA  1 ? 20 
ATOM   5337 C C   . GLY E 2 118 ? -7.789  13.818  27.488  1.000 58.677  0 447 GLY EEE C   1 ? 20 
ATOM   5338 O O   . GLY E 2 118 ? -8.515  13.842  26.474  1.000 60.797  0 447 GLY EEE O   1 ? 20 
ATOM   5339 N N   . ASN E 2 119 ? -6.511  13.428  27.502  1.000 54.834  0 448 ASN EEE N   1 ? 20 
ATOM   5340 C CA  . ASN E 2 119 ? -5.827  12.720  26.387  1.000 51.937  0 448 ASN EEE CA  1 ? 20 
ATOM   5341 C C   . ASN E 2 119 ? -5.877  11.219  26.683  1.000 49.226  0 448 ASN EEE C   1 ? 20 
ATOM   5342 O O   . ASN E 2 119 ? -5.371  10.817  27.744  1.000 48.893  0 448 ASN EEE O   1 ? 20 
ATOM   5343 C CB  . ASN E 2 119 ? -4.389  13.213  26.202  1.000 51.685  0 448 ASN EEE CB  1 ? 20 
ATOM   5344 C CG  . ASN E 2 119 ? -3.634  12.459  25.127  1.000 50.565  0 448 ASN EEE CG  1 ? 20 
ATOM   5345 O OD1 . ASN E 2 119 ? -4.233  11.939  24.185  1.000 51.311  0 448 ASN EEE OD1 1 ? 20 
ATOM   5346 N ND2 . ASN E 2 119 ? -2.318  12.392  25.262  1.000 49.483  0 448 ASN EEE ND2 1 ? 20 
ATOM   5347 N N   . TYR E 2 120 ? -6.460  10.430  25.776  1.000 48.658  0 449 TYR EEE N   1 ? 20 
ATOM   5348 C CA  . TYR E 2 120 ? -6.697  8.970   25.931  1.000 47.763  0 449 TYR EEE CA  1 ? 20 
ATOM   5349 C C   . TYR E 2 120 ? -5.906  8.176   24.880  1.000 48.060  0 449 TYR EEE C   1 ? 20 
ATOM   5350 O O   . TYR E 2 120 ? -6.141  6.958   24.752  1.000 47.388  0 449 TYR EEE O   1 ? 20 
ATOM   5351 C CB  . TYR E 2 120 ? -8.194  8.674   25.825  1.000 49.551  0 449 TYR EEE CB  1 ? 20 
ATOM   5352 C CG  . TYR E 2 120 ? -9.049  9.395   26.838  1.000 51.408  0 449 TYR EEE CG  1 ? 20 
ATOM   5353 C CD1 . TYR E 2 120 ? -9.582  10.645  26.565  1.000 52.838  0 449 TYR EEE CD1 1 ? 20 
ATOM   5354 C CD2 . TYR E 2 120 ? -9.339  8.824   28.069  1.000 50.966  0 449 TYR EEE CD2 1 ? 20 
ATOM   5355 C CE1 . TYR E 2 120 ? -10.367 11.313  27.490  1.000 54.592  0 449 TYR EEE CE1 1 ? 20 
ATOM   5356 C CE2 . TYR E 2 120 ? -10.131 9.474   29.002  1.000 52.034  0 449 TYR EEE CE2 1 ? 20 
ATOM   5357 C CZ  . TYR E 2 120 ? -10.643 10.726  28.712  1.000 54.329  0 449 TYR EEE CZ  1 ? 20 
ATOM   5358 O OH  . TYR E 2 120 ? -11.420 11.376  29.623  1.000 56.908  0 449 TYR EEE OH  1 ? 20 
ATOM   5359 N N   . ASN E 2 121 ? -4.984  8.826   24.163  1.000 49.912  0 450 ASN EEE N   1 ? 20 
ATOM   5360 C CA  . ASN E 2 121 ? -4.255  8.227   23.012  1.000 50.031  0 450 ASN EEE CA  1 ? 20 
ATOM   5361 C C   . ASN E 2 121 ? -3.147  7.294   23.509  1.000 49.074  0 450 ASN EEE C   1 ? 20 
ATOM   5362 O O   . ASN E 2 121 ? -2.733  6.421   22.722  1.000 51.930  0 450 ASN EEE O   1 ? 20 
ATOM   5363 C CB  . ASN E 2 121 ? -3.687  9.294   22.076  1.000 51.312  0 450 ASN EEE CB  1 ? 20 
ATOM   5364 C CG  . ASN E 2 121 ? -4.754  9.960   21.237  1.000 54.182  0 450 ASN EEE CG  1 ? 20 
ATOM   5365 O OD1 . ASN E 2 121 ? -5.904  9.526   21.211  1.000 54.030  0 450 ASN EEE OD1 1 ? 20 
ATOM   5366 N ND2 . ASN E 2 121 ? -4.379  11.023  20.548  1.000 57.230  0 450 ASN EEE ND2 1 ? 20 
ATOM   5367 N N   . TYR E 2 122 ? -2.672  7.467   24.746  1.000 47.489  0 451 TYR EEE N   1 ? 20 
ATOM   5368 C CA  . TYR E 2 122 ? -1.677  6.560   25.371  1.000 45.817  0 451 TYR EEE CA  1 ? 20 
ATOM   5369 C C   . TYR E 2 122 ? -2.419  5.346   25.941  1.000 44.510  0 451 TYR EEE C   1 ? 20 
ATOM   5370 O O   . TYR E 2 122 ? -3.350  5.528   26.743  1.000 43.739  0 451 TYR EEE O   1 ? 20 
ATOM   5371 C CB  . TYR E 2 122 ? -0.832  7.300   26.409  1.000 46.155  0 451 TYR EEE CB  1 ? 20 
ATOM   5372 C CG  . TYR E 2 122 ? 0.137   8.290   25.813  1.000 47.321  0 451 TYR EEE CG  1 ? 20 
ATOM   5373 C CD1 . TYR E 2 122 ? 1.229   7.863   25.072  1.000 46.532  0 451 TYR EEE CD1 1 ? 20 
ATOM   5374 C CD2 . TYR E 2 122 ? -0.038  9.655   25.979  1.000 48.968  0 451 TYR EEE CD2 1 ? 20 
ATOM   5375 C CE1 . TYR E 2 122 ? 2.125   8.765   24.520  1.000 47.405  0 451 TYR EEE CE1 1 ? 20 
ATOM   5376 C CE2 . TYR E 2 122 ? 0.849   10.570  25.434  1.000 49.716  0 451 TYR EEE CE2 1 ? 20 
ATOM   5377 C CZ  . TYR E 2 122 ? 1.934   10.124  24.698  1.000 48.715  0 451 TYR EEE CZ  1 ? 20 
ATOM   5378 O OH  . TYR E 2 122 ? 2.815   11.018  24.158  1.000 48.939  0 451 TYR EEE OH  1 ? 20 
ATOM   5379 N N   . LEU E 2 123 ? -2.022  4.149   25.502  1.000 44.718  0 452 LEU EEE N   1 ? 20 
ATOM   5380 C CA  . LEU E 2 123 ? -2.655  2.853   25.860  1.000 44.766  0 452 LEU EEE CA  1 ? 20 
ATOM   5381 C C   . LEU E 2 123 ? -1.660  1.977   26.632  1.000 44.474  0 452 LEU EEE C   1 ? 20 
ATOM   5382 O O   . LEU E 2 123 ? -0.424  2.196   26.506  1.000 43.239  0 452 LEU EEE O   1 ? 20 
ATOM   5383 C CB  . LEU E 2 123 ? -3.100  2.141   24.577  1.000 45.445  0 452 LEU EEE CB  1 ? 20 
ATOM   5384 C CG  . LEU E 2 123 ? -3.923  2.965   23.585  1.000 46.013  0 452 LEU EEE CG  1 ? 20 
ATOM   5385 C CD1 . LEU E 2 123 ? -4.344  2.108   22.397  1.000 46.170  0 452 LEU EEE CD1 1 ? 20 
ATOM   5386 C CD2 . LEU E 2 123 ? -5.144  3.587   24.250  1.000 45.052  0 452 LEU EEE CD2 1 ? 20 
ATOM   5387 N N   . TYR E 2 124 ? -2.188  1.005   27.381  1.000 44.229  0 453 TYR EEE N   1 ? 20 
ATOM   5388 C CA  . TYR E 2 124 ? -1.424  -0.111  27.997  1.000 44.341  0 453 TYR EEE CA  1 ? 20 
ATOM   5389 C C   . TYR E 2 124 ? -2.224  -1.407  27.839  1.000 43.567  0 453 TYR EEE C   1 ? 20 
ATOM   5390 O O   . TYR E 2 124 ? -3.461  -1.350  27.710  1.000 43.743  0 453 TYR EEE O   1 ? 20 
ATOM   5391 C CB  . TYR E 2 124 ? -1.109  0.176   29.469  1.000 43.636  0 453 TYR EEE CB  1 ? 20 
ATOM   5392 C CG  . TYR E 2 124 ? -2.318  0.404   30.339  1.000 43.546  0 453 TYR EEE CG  1 ? 20 
ATOM   5393 C CD1 . TYR E 2 124 ? -2.888  1.662   30.459  1.000 44.278  0 453 TYR EEE CD1 1 ? 20 
ATOM   5394 C CD2 . TYR E 2 124 ? -2.887  -0.638  31.052  1.000 44.286  0 453 TYR EEE CD2 1 ? 20 
ATOM   5395 C CE1 . TYR E 2 124 ? -4.002  1.881   31.254  1.000 46.123  0 453 TYR EEE CE1 1 ? 20 
ATOM   5396 C CE2 . TYR E 2 124 ? -3.993  -0.435  31.864  1.000 46.289  0 453 TYR EEE CE2 1 ? 20 
ATOM   5397 C CZ  . TYR E 2 124 ? -4.554  0.828   31.964  1.000 46.481  0 453 TYR EEE CZ  1 ? 20 
ATOM   5398 O OH  . TYR E 2 124 ? -5.647  1.045   32.750  1.000 46.202  0 453 TYR EEE OH  1 ? 20 
ATOM   5399 N N   . ARG E 2 125 ? -1.517  -2.539  27.825  1.000 42.693  0 454 ARG EEE N   1 ? 20 
ATOM   5400 C CA  . ARG E 2 125 ? -2.112  -3.899  27.844  1.000 43.342  0 454 ARG EEE CA  1 ? 20 
ATOM   5401 C C   . ARG E 2 125 ? -2.532  -4.212  29.285  1.000 41.748  0 454 ARG EEE C   1 ? 20 
ATOM   5402 O O   . ARG E 2 125 ? -1.667  -4.183  30.168  1.000 40.958  0 454 ARG EEE O   1 ? 20 
ATOM   5403 C CB  . ARG E 2 125 ? -1.118  -4.926  27.290  1.000 43.032  0 454 ARG EEE CB  1 ? 20 
ATOM   5404 C CG  . ARG E 2 125 ? -1.717  -6.306  27.049  1.000 44.657  0 454 ARG EEE CG  1 ? 20 
ATOM   5405 C CD  . ARG E 2 125 ? -0.780  -7.221  26.275  1.000 46.162  0 454 ARG EEE CD  1 ? 20 
ATOM   5406 N NE  . ARG E 2 125 ? -0.372  -6.614  25.011  1.000 46.041  0 454 ARG EEE NE  1 ? 20 
ATOM   5407 C CZ  . ARG E 2 125 ? -1.100  -6.600  23.901  1.000 46.438  0 454 ARG EEE CZ  1 ? 20 
ATOM   5408 N NH1 . ARG E 2 125 ? -2.286  -7.184  23.867  1.000 49.068  0 454 ARG EEE NH1 1 ? 20 
ATOM   5409 N NH2 . ARG E 2 125 ? -0.638  -5.999  22.822  1.000 45.529  0 454 ARG EEE NH2 1 ? 20 
ATOM   5410 N N   . LEU E 2 126 ? -3.818  -4.492  29.492  1.000 42.508  0 455 LEU EEE N   1 ? 20 
ATOM   5411 C CA  . LEU E 2 126 ? -4.445  -4.802  30.804  1.000 43.950  0 455 LEU EEE CA  1 ? 20 
ATOM   5412 C C   . LEU E 2 126 ? -4.452  -6.320  31.033  1.000 45.112  0 455 LEU EEE C   1 ? 20 
ATOM   5413 O O   . LEU E 2 126 ? -4.370  -6.735  32.204  1.000 47.330  0 455 LEU EEE O   1 ? 20 
ATOM   5414 C CB  . LEU E 2 126 ? -5.865  -4.227  30.800  1.000 44.797  0 455 LEU EEE CB  1 ? 20 
ATOM   5415 C CG  . LEU E 2 126 ? -6.690  -4.447  32.067  1.000 47.340  0 455 LEU EEE CG  1 ? 20 
ATOM   5416 C CD1 . LEU E 2 126 ? -6.051  -3.773  33.278  1.000 47.540  0 455 LEU EEE CD1 1 ? 20 
ATOM   5417 C CD2 . LEU E 2 126 ? -8.112  -3.945  31.868  1.000 49.205  0 455 LEU EEE CD2 1 ? 20 
ATOM   5418 N N   . PHE E 2 127 ? -4.537  -7.112  29.957  1.000 45.415  0 456 PHE EEE N   1 ? 20 
ATOM   5419 C CA  . PHE E 2 127 ? -4.685  -8.593  29.980  1.000 47.282  0 456 PHE EEE CA  1 ? 20 
ATOM   5420 C C   . PHE E 2 127 ? -3.610  -9.270  29.115  1.000 46.614  0 456 PHE EEE C   1 ? 20 
ATOM   5421 O O   . PHE E 2 127 ? -3.328  -8.771  28.011  1.000 45.266  0 456 PHE EEE O   1 ? 20 
ATOM   5422 C CB  . PHE E 2 127 ? -6.060  -8.989  29.439  1.000 49.492  0 456 PHE EEE CB  1 ? 20 
ATOM   5423 C CG  . PHE E 2 127 ? -7.250  -8.531  30.246  1.000 50.600  0 456 PHE EEE CG  1 ? 20 
ATOM   5424 C CD1 . PHE E 2 127 ? -7.590  -9.166  31.432  1.000 51.923  0 456 PHE EEE CD1 1 ? 20 
ATOM   5425 C CD2 . PHE E 2 127 ? -8.052  -7.489  29.804  1.000 49.979  0 456 PHE EEE CD2 1 ? 20 
ATOM   5426 C CE1 . PHE E 2 127 ? -8.689  -8.752  32.167  1.000 52.482  0 456 PHE EEE CE1 1 ? 20 
ATOM   5427 C CE2 . PHE E 2 127 ? -9.146  -7.071  30.547  1.000 49.975  0 456 PHE EEE CE2 1 ? 20 
ATOM   5428 C CZ  . PHE E 2 127 ? -9.463  -7.705  31.724  1.000 51.479  0 456 PHE EEE CZ  1 ? 20 
ATOM   5429 N N   . ARG E 2 128 ? -3.077  -10.410 29.570  1.000 47.294  0 457 ARG EEE N   1 ? 20 
ATOM   5430 C CA  . ARG E 2 128 ? -2.169  -11.287 28.783  1.000 48.167  0 457 ARG EEE CA  1 ? 20 
ATOM   5431 C C   . ARG E 2 128 ? -2.079  -12.674 29.437  1.000 50.323  0 457 ARG EEE C   1 ? 20 
ATOM   5432 O O   . ARG E 2 128 ? -2.142  -12.739 30.666  1.000 50.320  0 457 ARG EEE O   1 ? 20 
ATOM   5433 C CB  . ARG E 2 128 ? -0.789  -10.636 28.659  1.000 47.212  0 457 ARG EEE CB  1 ? 20 
ATOM   5434 C CG  . ARG E 2 128 ? 0.002   -11.092 27.445  1.000 47.140  0 457 ARG EEE CG  1 ? 20 
ATOM   5435 C CD  . ARG E 2 128 ? 1.277   -10.304 27.269  1.000 46.244  0 457 ARG EEE CD  1 ? 20 
ATOM   5436 N NE  . ARG E 2 128 ? 2.023   -10.801 26.124  1.000 47.643  0 457 ARG EEE NE  1 ? 20 
ATOM   5437 C CZ  . ARG E 2 128 ? 2.945   -11.757 26.162  1.000 50.135  0 457 ARG EEE CZ  1 ? 20 
ATOM   5438 N NH1 . ARG E 2 128 ? 3.276   -12.338 27.306  1.000 51.310  0 457 ARG EEE NH1 1 ? 20 
ATOM   5439 N NH2 . ARG E 2 128 ? 3.557   -12.113 25.046  1.000 51.985  0 457 ARG EEE NH2 1 ? 20 
ATOM   5440 N N   . LYS E 2 129 ? -1.931  -13.733 28.628  1.000 53.703  0 458 LYS EEE N   1 ? 20 
ATOM   5441 C CA  . LYS E 2 129 ? -1.991  -15.164 29.050  1.000 57.778  0 458 LYS EEE CA  1 ? 20 
ATOM   5442 C C   . LYS E 2 129 ? -0.717  -15.565 29.805  1.000 57.147  0 458 LYS EEE C   1 ? 20 
ATOM   5443 O O   . LYS E 2 129 ? -0.727  -16.615 30.467  1.000 58.845  0 458 LYS EEE O   1 ? 20 
ATOM   5444 C CB  . LYS E 2 129 ? -2.207  -16.072 27.835  1.000 62.429  0 458 LYS EEE CB  1 ? 20 
ATOM   5445 C CG  . LYS E 2 129 ? -3.502  -15.808 27.079  1.000 66.805  0 458 LYS EEE CG  1 ? 20 
ATOM   5446 C CD  . LYS E 2 129 ? -3.820  -16.763 25.952  1.000 72.084  0 458 LYS EEE CD  1 ? 20 
ATOM   5447 C CE  . LYS E 2 129 ? -5.188  -16.485 25.358  1.000 74.457  0 458 LYS EEE CE  1 ? 20 
ATOM   5448 N NZ  . LYS E 2 129 ? -5.577  -17.506 24.357  1.000 78.431  0 458 LYS EEE NZ  1 ? 20 
ATOM   5449 N N   . SER E 2 130 ? 0.351   -14.777 29.689  1.000 54.005  0 459 SER EEE N   1 ? 21 
ATOM   5450 C CA  . SER E 2 130 ? 1.609   -14.950 30.461  1.000 54.641  0 459 SER EEE CA  1 ? 21 
ATOM   5451 C C   . SER E 2 130 ? 2.376   -13.627 30.481  1.000 51.914  0 459 SER EEE C   1 ? 21 
ATOM   5452 O O   . SER E 2 130 ? 2.037   -12.724 29.684  1.000 49.604  0 459 SER EEE O   1 ? 21 
ATOM   5453 C CB  . SER E 2 130 ? 2.445   -16.065 29.900  1.000 57.661  0 459 SER EEE CB  1 ? 21 
ATOM   5454 O OG  . SER E 2 130 ? 2.990   -15.703 28.639  1.000 58.527  0 459 SER EEE OG  1 ? 21 
ATOM   5455 N N   . ASN E 2 131 ? 3.362   -13.522 31.370  1.000 52.135  0 460 ASN EEE N   1 ? 21 
ATOM   5456 C CA  . ASN E 2 131 ? 4.200   -12.307 31.538  1.000 51.207  0 460 ASN EEE CA  1 ? 21 
ATOM   5457 C C   . ASN E 2 131 ? 5.171   -12.215 30.356  1.000 51.330  0 460 ASN EEE C   1 ? 21 
ATOM   5458 O O   . ASN E 2 131 ? 5.625   -13.274 29.873  1.000 52.785  0 460 ASN EEE O   1 ? 21 
ATOM   5459 C CB  . ASN E 2 131 ? 4.933   -12.321 32.882  1.000 52.901  0 460 ASN EEE CB  1 ? 21 
ATOM   5460 C CG  . ASN E 2 131 ? 3.994   -12.259 34.069  1.000 52.873  0 460 ASN EEE CG  1 ? 21 
ATOM   5461 O OD1 . ASN E 2 131 ? 2.835   -11.872 33.934  1.000 53.356  0 460 ASN EEE OD1 1 ? 21 
ATOM   5462 N ND2 . ASN E 2 131 ? 4.481   -12.638 35.237  1.000 53.574  0 460 ASN EEE ND2 1 ? 21 
ATOM   5463 N N   . LEU E 2 132 ? 5.471   -10.995 29.907  1.000 49.301  0 461 LEU EEE N   1 ? 21 
ATOM   5464 C CA  . LEU E 2 132 ? 6.522   -10.728 28.895  1.000 49.998  0 461 LEU EEE CA  1 ? 21 
ATOM   5465 C C   . LEU E 2 132 ? 7.856   -11.252 29.426  1.000 52.063  0 461 LEU EEE C   1 ? 21 
ATOM   5466 O O   . LEU E 2 132 ? 8.110   -11.101 30.633  1.000 51.782  0 461 LEU EEE O   1 ? 21 
ATOM   5467 C CB  . LEU E 2 132 ? 6.628   -9.225  28.621  1.000 47.866  0 461 LEU EEE CB  1 ? 21 
ATOM   5468 C CG  . LEU E 2 132 ? 5.465   -8.587  27.866  1.000 46.011  0 461 LEU EEE CG  1 ? 21 
ATOM   5469 C CD1 . LEU E 2 132 ? 5.664   -7.085  27.776  1.000 44.478  0 461 LEU EEE CD1 1 ? 21 
ATOM   5470 C CD2 . LEU E 2 132 ? 5.307   -9.184  26.475  1.000 47.478  0 461 LEU EEE CD2 1 ? 21 
ATOM   5471 N N   . LYS E 2 133 ? 8.665   -11.841 28.543  1.000 54.583  0 462 LYS EEE N   1 ? 21 
ATOM   5472 C CA  . LYS E 2 133 ? 10.110  -12.073 28.778  1.000 55.717  0 462 LYS EEE CA  1 ? 21 
ATOM   5473 C C   . LYS E 2 133 ? 10.797  -10.712 28.734  1.000 52.383  0 462 LYS EEE C   1 ? 21 
ATOM   5474 O O   . LYS E 2 133 ? 10.259  -9.761  28.175  1.000 49.394  0 462 LYS EEE O   1 ? 21 
ATOM   5475 C CB  . LYS E 2 133 ? 10.659  -13.061 27.745  1.000 60.247  0 462 LYS EEE CB  1 ? 21 
ATOM   5476 C CG  . LYS E 2 133 ? 10.058  -14.457 27.834  1.000 63.703  0 462 LYS EEE CG  1 ? 21 
ATOM   5477 C CD  . LYS E 2 133 ? 10.466  -15.376 26.704  1.000 68.353  0 462 LYS EEE CD  1 ? 21 
ATOM   5478 C CE  . LYS E 2 133 ? 9.729   -16.700 26.723  1.000 71.504  0 462 LYS EEE CE  1 ? 21 
ATOM   5479 N NZ  . LYS E 2 133 ? 10.464  -17.757 25.981  1.000 76.367  0 462 LYS EEE NZ  1 ? 21 
ATOM   5480 N N   . PRO E 2 134 ? 11.986  -10.549 29.350  1.000 52.880  0 463 PRO EEE N   1 ? 21 
ATOM   5481 C CA  . PRO E 2 134 ? 12.695  -9.273  29.290  1.000 51.947  0 463 PRO EEE CA  1 ? 21 
ATOM   5482 C C   . PRO E 2 134 ? 12.813  -8.739  27.852  1.000 51.591  0 463 PRO EEE C   1 ? 21 
ATOM   5483 O O   . PRO E 2 134 ? 13.187  -9.495  26.966  1.000 52.378  0 463 PRO EEE O   1 ? 21 
ATOM   5484 C CB  . PRO E 2 134 ? 14.075  -9.608  29.878  1.000 53.439  0 463 PRO EEE CB  1 ? 21 
ATOM   5485 C CG  . PRO E 2 134 ? 13.808  -10.775 30.803  1.000 54.545  0 463 PRO EEE CG  1 ? 21 
ATOM   5486 C CD  . PRO E 2 134 ? 12.701  -11.565 30.138  1.000 54.725  0 463 PRO EEE CD  1 ? 21 
ATOM   5487 N N   . PHE E 2 135 ? 12.463  -7.463  27.663  1.000 49.693  0 464 PHE EEE N   1 ? 21 
ATOM   5488 C CA  . PHE E 2 135 ? 12.587  -6.692  26.397  1.000 50.931  0 464 PHE EEE CA  1 ? 21 
ATOM   5489 C C   . PHE E 2 135 ? 11.659  -7.258  25.310  1.000 52.361  0 464 PHE EEE C   1 ? 21 
ATOM   5490 O O   . PHE E 2 135 ? 11.842  -6.894  24.142  1.000 53.066  0 464 PHE EEE O   1 ? 21 
ATOM   5491 C CB  . PHE E 2 135 ? 14.044  -6.658  25.922  1.000 52.500  0 464 PHE EEE CB  1 ? 21 
ATOM   5492 C CG  . PHE E 2 135 ? 14.985  -5.870  26.800  1.000 52.066  0 464 PHE EEE CG  1 ? 21 
ATOM   5493 C CD1 . PHE E 2 135 ? 14.685  -4.567  27.179  1.000 50.375  0 464 PHE EEE CD1 1 ? 21 
ATOM   5494 C CD2 . PHE E 2 135 ? 16.182  -6.420  27.233  1.000 53.207  0 464 PHE EEE CD2 1 ? 21 
ATOM   5495 C CE1 . PHE E 2 135 ? 15.553  -3.844  27.984  1.000 49.453  0 464 PHE EEE CE1 1 ? 21 
ATOM   5496 C CE2 . PHE E 2 135 ? 17.045  -5.695  28.040  1.000 52.526  0 464 PHE EEE CE2 1 ? 21 
ATOM   5497 C CZ  . PHE E 2 135 ? 16.733  -4.408  28.406  1.000 50.327  0 464 PHE EEE CZ  1 ? 21 
ATOM   5498 N N   . GLU E 2 136 ? 10.674  -8.084  25.672  1.000 53.948  0 465 GLU EEE N   1 ? 21 
ATOM   5499 C CA  . GLU E 2 136 ? 9.640   -8.592  24.732  1.000 56.116  0 465 GLU EEE CA  1 ? 21 
ATOM   5500 C C   . GLU E 2 136 ? 8.621   -7.473  24.484  1.000 53.932  0 465 GLU EEE C   1 ? 21 
ATOM   5501 O O   . GLU E 2 136 ? 8.400   -6.649  25.397  1.000 52.937  0 465 GLU EEE O   1 ? 21 
ATOM   5502 C CB  . GLU E 2 136 ? 8.983   -9.857  25.287  1.000 59.337  0 465 GLU EEE CB  1 ? 21 
ATOM   5503 C CG  . GLU E 2 136 ? 8.223   -10.670 24.252  1.000 62.551  0 465 GLU EEE CG  1 ? 21 
ATOM   5504 C CD  . GLU E 2 136 ? 7.458   -11.864 24.809  1.000 65.960  0 465 GLU EEE CD  1 ? 21 
ATOM   5505 O OE1 . GLU E 2 136 ? 7.881   -12.418 25.844  1.000 67.811  0 465 GLU EEE OE1 1 ? 21 
ATOM   5506 O OE2 . GLU E 2 136 ? 6.429   -12.233 24.210  1.000 68.837  0 465 GLU EEE OE2 1 ? 21 
ATOM   5507 N N   . ARG E 2 137 ? 8.046   -7.440  23.281  1.000 55.024  0 466 ARG EEE N   1 ? 21 
ATOM   5508 C CA  . ARG E 2 137 ? 7.055   -6.429  22.823  1.000 53.769  0 466 ARG EEE CA  1 ? 21 
ATOM   5509 C C   . ARG E 2 137 ? 5.853   -7.169  22.232  1.000 52.418  0 466 ARG EEE C   1 ? 21 
ATOM   5510 O O   . ARG E 2 137 ? 6.074   -8.034  21.372  1.000 52.745  0 466 ARG EEE O   1 ? 21 
ATOM   5511 C CB  . ARG E 2 137 ? 7.711   -5.512  21.787  1.000 55.438  0 466 ARG EEE CB  1 ? 21 
ATOM   5512 C CG  . ARG E 2 137 ? 6.872   -4.323  21.343  1.000 54.999  0 466 ARG EEE CG  1 ? 21 
ATOM   5513 C CD  . ARG E 2 137 ? 7.759   -3.388  20.548  1.000 57.541  0 466 ARG EEE CD  1 ? 21 
ATOM   5514 N NE  . ARG E 2 137 ? 7.076   -2.258  19.936  1.000 60.588  0 466 ARG EEE NE  1 ? 21 
ATOM   5515 C CZ  . ARG E 2 137 ? 6.516   -2.249  18.718  1.000 64.926  0 466 ARG EEE CZ  1 ? 21 
ATOM   5516 N NH1 . ARG E 2 137 ? 6.519   -3.335  17.955  1.000 65.148  0 466 ARG EEE NH1 1 ? 21 
ATOM   5517 N NH2 . ARG E 2 137 ? 5.949   -1.140  18.265  1.000 64.099  0 466 ARG EEE NH2 1 ? 21 
ATOM   5518 N N   . ASP E 2 138 ? 4.644   -6.868  22.713  1.000 50.650  0 467 ASP EEE N   1 ? 21 
ATOM   5519 C CA  . ASP E 2 138 ? 3.376   -7.489  22.249  1.000 50.538  0 467 ASP EEE CA  1 ? 21 
ATOM   5520 C C   . ASP E 2 138 ? 2.434   -6.368  21.802  1.000 48.194  0 467 ASP EEE C   1 ? 21 
ATOM   5521 O O   . ASP E 2 138 ? 1.950   -5.629  22.673  1.000 45.913  0 467 ASP EEE O   1 ? 21 
ATOM   5522 C CB  . ASP E 2 138 ? 2.770   -8.367  23.349  1.000 51.768  0 467 ASP EEE CB  1 ? 21 
ATOM   5523 C CG  . ASP E 2 138 ? 1.470   -9.062  22.970  1.000 53.279  0 467 ASP EEE CG  1 ? 21 
ATOM   5524 O OD1 . ASP E 2 138 ? 0.942   -8.777  21.871  1.000 52.779  0 467 ASP EEE OD1 1 ? 21 
ATOM   5525 O OD2 . ASP E 2 138 ? 0.989   -9.880  23.785  1.000 53.321  0 467 ASP EEE OD2 1 ? 21 
ATOM   5526 N N   . ILE E 2 139 ? 2.193   -6.248  20.494  1.000 48.821  0 468 ILE EEE N   1 ? 21 
ATOM   5527 C CA  . ILE E 2 139 ? 1.300   -5.209  19.895  1.000 47.659  0 468 ILE EEE CA  1 ? 21 
ATOM   5528 C C   . ILE E 2 139 ? 0.037   -5.874  19.336  1.000 47.854  0 468 ILE EEE C   1 ? 21 
ATOM   5529 O O   . ILE E 2 139 ? -0.721  -5.181  18.641  1.000 49.429  0 468 ILE EEE O   1 ? 21 
ATOM   5530 C CB  . ILE E 2 139 ? 2.042   -4.386  18.822  1.000 48.662  0 468 ILE EEE CB  1 ? 21 
ATOM   5531 C CG1 . ILE E 2 139 ? 2.497   -5.243  17.637  1.000 49.869  0 468 ILE EEE CG1 1 ? 21 
ATOM   5532 C CG2 . ILE E 2 139 ? 3.202   -3.628  19.445  1.000 48.810  0 468 ILE EEE CG2 1 ? 21 
ATOM   5533 C CD1 . ILE E 2 139 ? 2.959   -4.433  16.454  1.000 51.631  0 468 ILE EEE CD1 1 ? 21 
ATOM   5534 N N   . SER E 2 140 ? -0.184  -7.155  19.640  1.000 48.024  0 469 SER EEE N   1 ? 21 
ATOM   5535 C CA  . SER E 2 140 ? -1.376  -7.916  19.194  1.000 48.886  0 469 SER EEE CA  1 ? 21 
ATOM   5536 C C   . SER E 2 140 ? -2.625  -7.275  19.809  1.000 48.090  0 469 SER EEE C   1 ? 21 
ATOM   5537 O O   . SER E 2 140 ? -2.522  -6.716  20.923  1.000 47.188  0 469 SER EEE O   1 ? 21 
ATOM   5538 C CB  . SER E 2 140 ? -1.258  -9.381  19.529  1.000 49.612  0 469 SER EEE CB  1 ? 21 
ATOM   5539 O OG  . SER E 2 140 ? -1.135  -9.576  20.926  1.000 49.333  0 469 SER EEE OG  1 ? 21 
ATOM   5540 N N   . THR E 2 141 ? -3.746  -7.329  19.085  1.000 48.714  0 470 THR EEE N   1 ? 21 
ATOM   5541 C CA  . THR E 2 141 ? -5.028  -6.665  19.442  1.000 48.351  0 470 THR EEE CA  1 ? 21 
ATOM   5542 C C   . THR E 2 141 ? -6.183  -7.671  19.357  1.000 49.780  0 470 THR EEE C   1 ? 21 
ATOM   5543 O O   . THR E 2 141 ? -7.331  -7.238  19.183  1.000 50.348  0 470 THR EEE O   1 ? 21 
ATOM   5544 C CB  . THR E 2 141 ? -5.246  -5.439  18.550  1.000 47.973  0 470 THR EEE CB  1 ? 21 
ATOM   5545 O OG1 . THR E 2 141 ? -5.242  -5.883  17.191  1.000 49.090  0 470 THR EEE OG1 1 ? 21 
ATOM   5546 C CG2 . THR E 2 141 ? -4.190  -4.375  18.764  1.000 47.529  0 470 THR EEE CG2 1 ? 21 
ATOM   5547 N N   . GLU E 2 142 ? -5.879  -8.961  19.508  1.000 53.692  0 471 GLU EEE N   1 ? 21 
ATOM   5548 C CA  . GLU E 2 142 ? -6.872  -10.063 19.556  1.000 56.855  0 471 GLU EEE CA  1 ? 21 
ATOM   5549 C C   . GLU E 2 142 ? -7.632  -9.971  20.886  1.000 55.192  0 471 GLU EEE C   1 ? 21 
ATOM   5550 O O   . GLU E 2 142 ? -7.010  -9.589  21.901  1.000 53.834  0 471 GLU EEE O   1 ? 21 
ATOM   5551 C CB  . GLU E 2 142 ? -6.161  -11.412 19.401  1.000 62.786  0 471 GLU EEE CB  1 ? 21 
ATOM   5552 C CG  . GLU E 2 142 ? -7.037  -12.505 18.808  1.000 70.696  0 471 GLU EEE CG  1 ? 21 
ATOM   5553 C CD  . GLU E 2 142 ? -6.401  -13.884 18.679  1.000 76.733  0 471 GLU EEE CD  1 ? 21 
ATOM   5554 O OE1 . GLU E 2 142 ? -5.166  -13.961 18.481  1.000 80.330  0 471 GLU EEE OE1 1 ? 21 
ATOM   5555 O OE2 . GLU E 2 142 ? -7.149  -14.887 18.770  1.000 77.767  0 471 GLU EEE OE2 1 ? 21 
ATOM   5556 N N   . ILE E 2 143 ? -8.925  -10.301 20.887  1.000 53.752  0 472 ILE EEE N   1 ? 21 
ATOM   5557 C CA  . ILE E 2 143 ? -9.738  -10.388 22.137  1.000 51.805  0 472 ILE EEE CA  1 ? 21 
ATOM   5558 C C   . ILE E 2 143 ? -9.012  -11.349 23.083  1.000 51.003  0 472 ILE EEE C   1 ? 21 
ATOM   5559 O O   . ILE E 2 143 ? -8.643  -12.453 22.638  1.000 49.377  0 472 ILE EEE O   1 ? 21 
ATOM   5560 C CB  . ILE E 2 143 ? -11.190 -10.839 21.866  1.000 52.260  0 472 ILE EEE CB  1 ? 21 
ATOM   5561 C CG1 . ILE E 2 143 ? -11.947 -9.829  21.000  1.000 51.526  0 472 ILE EEE CG1 1 ? 21 
ATOM   5562 C CG2 . ILE E 2 143 ? -11.932 -11.118 23.174  1.000 52.542  0 472 ILE EEE CG2 1 ? 21 
ATOM   5563 C CD1 . ILE E 2 143 ? -13.356 -10.257 20.664  1.000 51.937  0 472 ILE EEE CD1 1 ? 21 
ATOM   5564 N N   . TYR E 2 144 ? -8.786  -10.919 24.325  1.000 50.140  0 473 TYR EEE N   1 ? 21 
ATOM   5565 C CA  . TYR E 2 144 ? -8.243  -11.764 25.414  1.000 49.569  0 473 TYR EEE CA  1 ? 21 
ATOM   5566 C C   . TYR E 2 144 ? -9.333  -12.745 25.851  1.000 50.070  0 473 TYR EEE C   1 ? 21 
ATOM   5567 O O   . TYR E 2 144 ? -10.385 -12.301 26.338  1.000 48.271  0 473 TYR EEE O   1 ? 21 
ATOM   5568 C CB  . TYR E 2 144 ? -7.746  -10.911 26.583  1.000 50.052  0 473 TYR EEE CB  1 ? 21 
ATOM   5569 C CG  . TYR E 2 144 ? -7.150  -11.722 27.706  1.000 51.375  0 473 TYR EEE CG  1 ? 21 
ATOM   5570 C CD1 . TYR E 2 144 ? -5.980  -12.435 27.525  1.000 52.082  0 473 TYR EEE CD1 1 ? 21 
ATOM   5571 C CD2 . TYR E 2 144 ? -7.783  -11.822 28.934  1.000 52.661  0 473 TYR EEE CD2 1 ? 21 
ATOM   5572 C CE1 . TYR E 2 144 ? -5.459  -13.224 28.533  1.000 55.084  0 473 TYR EEE CE1 1 ? 21 
ATOM   5573 C CE2 . TYR E 2 144 ? -7.269  -12.601 29.959  1.000 53.543  0 473 TYR EEE CE2 1 ? 21 
ATOM   5574 C CZ  . TYR E 2 144 ? -6.094  -13.299 29.758  1.000 54.899  0 473 TYR EEE CZ  1 ? 21 
ATOM   5575 O OH  . TYR E 2 144 ? -5.535  -14.057 30.742  1.000 57.268  0 473 TYR EEE OH  1 ? 21 
ATOM   5576 N N   . GLN E 2 145 ? -9.075  -14.036 25.649  1.000 51.175  0 474 GLN EEE N   1 ? 21 
ATOM   5577 C CA  . GLN E 2 145 ? -9.912  -15.156 26.141  1.000 52.842  0 474 GLN EEE CA  1 ? 21 
ATOM   5578 C C   . GLN E 2 145 ? -9.476  -15.499 27.571  1.000 54.292  0 474 GLN EEE C   1 ? 21 
ATOM   5579 O O   . GLN E 2 145 ? -8.444  -16.187 27.728  1.000 54.978  0 474 GLN EEE O   1 ? 21 
ATOM   5580 C CB  . GLN E 2 145 ? -9.761  -16.332 25.178  1.000 54.581  0 474 GLN EEE CB  1 ? 21 
ATOM   5581 C CG  . GLN E 2 145 ? -10.677 -17.500 25.490  1.000 56.133  0 474 GLN EEE CG  1 ? 21 
ATOM   5582 C CD  . GLN E 2 145 ? -10.354 -18.699 24.635  1.000 58.556  0 474 GLN EEE CD  1 ? 21 
ATOM   5583 O OE1 . GLN E 2 145 ? -9.846  -18.578 23.522  1.000 58.297  0 474 GLN EEE OE1 1 ? 21 
ATOM   5584 N NE2 . GLN E 2 145 ? -10.664 -19.876 25.149  1.000 61.508  0 474 GLN EEE NE2 1 ? 21 
ATOM   5585 N N   . ALA E 2 146 ? -10.227 -15.023 28.570  1.000 53.843  0 475 ALA EEE N   1 ? 21 
ATOM   5586 C CA  . ALA E 2 146 ? -9.904  -15.151 30.013  1.000 53.786  0 475 ALA EEE CA  1 ? 21 
ATOM   5587 C C   . ALA E 2 146 ? -10.379 -16.503 30.546  1.000 55.510  0 475 ALA EEE C   1 ? 21 
ATOM   5588 O O   . ALA E 2 146 ? -9.857  -16.925 31.599  1.000 58.134  0 475 ALA EEE O   1 ? 21 
ATOM   5589 C CB  . ALA E 2 146 ? -10.515 -14.015 30.796  1.000 51.914  0 475 ALA EEE CB  1 ? 21 
ATOM   5590 N N   . GLY E 2 147 ? -11.327 -17.141 29.849  1.000 55.258  0 476 GLY EEE N   1 ? 21 
ATOM   5591 C CA  . GLY E 2 147 ? -11.919 -18.439 30.222  1.000 57.930  0 476 GLY EEE CA  1 ? 21 
ATOM   5592 C C   . GLY E 2 147 ? -11.551 -19.535 29.236  1.000 60.303  0 476 GLY EEE C   1 ? 21 
ATOM   5593 O O   . GLY E 2 147 ? -10.639 -19.324 28.420  1.000 60.332  0 476 GLY EEE O   1 ? 21 
ATOM   5594 N N   . SER E 2 148 ? -12.252 -20.668 29.307  1.000 64.322  0 477 SER EEE N   1 ? 21 
ATOM   5595 C CA  . SER E 2 148 ? -12.032 -21.875 28.467  1.000 67.442  0 477 SER EEE CA  1 ? 21 
ATOM   5596 C C   . SER E 2 148 ? -12.846 -21.778 27.170  1.000 66.852  0 477 SER EEE C   1 ? 21 
ATOM   5597 O O   . SER E 2 148 ? -12.460 -22.446 26.193  1.000 68.883  0 477 SER EEE O   1 ? 21 
ATOM   5598 C CB  . SER E 2 148 ? -12.370 -23.123 29.236  1.000 71.366  0 477 SER EEE CB  1 ? 21 
ATOM   5599 O OG  . SER E 2 148 ? -13.661 -23.019 29.819  1.000 72.891  0 477 SER EEE OG  1 ? 21 
ATOM   5600 N N   . THR E 2 149 ? -13.923 -20.984 27.174  1.000 65.827  0 478 THR EEE N   1 ? 21 
ATOM   5601 C CA  . THR E 2 149 ? -14.831 -20.751 26.016  1.000 63.955  0 478 THR EEE CA  1 ? 21 
ATOM   5602 C C   . THR E 2 149 ? -14.162 -19.791 25.034  1.000 61.713  0 478 THR EEE C   1 ? 21 
ATOM   5603 O O   . THR E 2 149 ? -13.731 -18.715 25.435  1.000 58.480  0 478 THR EEE O   1 ? 21 
ATOM   5604 C CB  . THR E 2 149 ? -16.187 -20.203 26.482  1.000 62.628  0 478 THR EEE CB  1 ? 21 
ATOM   5605 O OG1 . THR E 2 149 ? -16.760 -21.138 27.396  1.000 65.033  0 478 THR EEE OG1 1 ? 21 
ATOM   5606 C CG2 . THR E 2 149 ? -17.149 -19.951 25.342  1.000 61.580  0 478 THR EEE CG2 1 ? 21 
ATOM   5607 N N   . PRO E 2 150 ? -14.035 -20.147 23.731  1.000 63.196  0 479 PRO EEE N   1 ? 21 
ATOM   5608 C CA  . PRO E 2 150 ? -13.530 -19.216 22.720  1.000 60.538  0 479 PRO EEE CA  1 ? 21 
ATOM   5609 C C   . PRO E 2 150 ? -14.476 -18.025 22.515  1.000 57.071  0 479 PRO EEE C   1 ? 21 
ATOM   5610 O O   . PRO E 2 150 ? -15.656 -18.184 22.697  1.000 57.277  0 479 PRO EEE O   1 ? 21 
ATOM   5611 C CB  . PRO E 2 150 ? -13.447 -20.049 21.432  1.000 62.395  0 479 PRO EEE CB  1 ? 21 
ATOM   5612 C CG  . PRO E 2 150 ? -13.481 -21.486 21.902  1.000 65.335  0 479 PRO EEE CG  1 ? 21 
ATOM   5613 C CD  . PRO E 2 150 ? -14.325 -21.470 23.158  1.000 65.660  0 479 PRO EEE CD  1 ? 21 
ATOM   5614 N N   . CYS E 2 151 ? -13.922 -16.872 22.141  1.000 55.554  0 480 CYS EEE N   1 ? 21 
ATOM   5615 C CA  . CYS E 2 151 ? -14.629 -15.570 21.995  1.000 54.279  0 480 CYS EEE CA  1 ? 21 
ATOM   5616 C C   . CYS E 2 151 ? -15.196 -15.409 20.576  1.000 53.270  0 480 CYS EEE C   1 ? 21 
ATOM   5617 O O   . CYS E 2 151 ? -16.248 -14.762 20.438  1.000 53.308  0 480 CYS EEE O   1 ? 21 
ATOM   5618 C CB  . CYS E 2 151 ? -13.682 -14.424 22.330  1.000 54.973  0 480 CYS EEE CB  1 ? 21 
ATOM   5619 S SG  . CYS E 2 151 ? -12.979 -14.558 23.996  1.000 60.466  0 480 CYS EEE SG  1 ? 21 
ATOM   5620 N N   . ASN E 2 152 ? -14.521 -15.963 19.562  1.000 53.269  0 481 ASN EEE N   1 ? 21 
ATOM   5621 C CA  . ASN E 2 152 ? -14.937 -15.910 18.134  1.000 53.163  0 481 ASN EEE CA  1 ? 21 
ATOM   5622 C C   . ASN E 2 152 ? -15.251 -14.463 17.724  1.000 51.825  0 481 ASN EEE C   1 ? 21 
ATOM   5623 O O   . ASN E 2 152 ? -16.289 -14.241 17.078  1.000 52.245  0 481 ASN EEE O   1 ? 21 
ATOM   5624 C CB  . ASN E 2 152 ? -16.121 -16.841 17.873  1.000 54.119  0 481 ASN EEE CB  1 ? 21 
ATOM   5625 C CG  . ASN E 2 152 ? -15.730 -18.300 17.943  1.000 56.590  0 481 ASN EEE CG  1 ? 21 
ATOM   5626 O OD1 . ASN E 2 152 ? -16.285 -19.058 18.730  1.000 58.469  0 481 ASN EEE OD1 1 ? 21 
ATOM   5627 N ND2 . ASN E 2 152 ? -14.780 -18.704 17.119  1.000 58.546  0 481 ASN EEE ND2 1 ? 21 
ATOM   5628 N N   . GLY E 2 153 ? -14.380 -13.520 18.093  1.000 51.173  0 482 GLY EEE N   1 ? 21 
ATOM   5629 C CA  . GLY E 2 153 ? -14.445 -12.106 17.675  1.000 48.674  0 482 GLY EEE CA  1 ? 21 
ATOM   5630 C C   . GLY E 2 153 ? -15.552 -11.331 18.371  1.000 46.578  0 482 GLY EEE C   1 ? 21 
ATOM   5631 O O   . GLY E 2 153 ? -15.855 -10.215 17.911  1.000 48.296  0 482 GLY EEE O   1 ? 21 
ATOM   5632 N N   . VAL E 2 154 ? -16.135 -11.868 19.445  1.000 45.118  0 483 VAL EEE N   1 ? 21 
ATOM   5633 C CA  . VAL E 2 154 ? -17.212 -11.171 20.213  1.000 45.310  0 483 VAL EEE CA  1 ? 21 
ATOM   5634 C C   . VAL E 2 154 ? -16.762 -11.000 21.667  1.000 44.139  0 483 VAL EEE C   1 ? 21 
ATOM   5635 O O   . VAL E 2 154 ? -16.377 -12.010 22.290  1.000 45.625  0 483 VAL EEE O   1 ? 21 
ATOM   5636 C CB  . VAL E 2 154 ? -18.565 -11.903 20.126  1.000 44.917  0 483 VAL EEE CB  1 ? 21 
ATOM   5637 C CG1 . VAL E 2 154 ? -19.635 -11.176 20.930  1.000 44.189  0 483 VAL EEE CG1 1 ? 21 
ATOM   5638 C CG2 . VAL E 2 154 ? -19.010 -12.090 18.683  1.000 45.425  0 483 VAL EEE CG2 1 ? 21 
ATOM   5639 N N   . GLU E 2 155 ? -16.810 -9.766  22.172  1.000 43.840  0 484 GLU EEE N   1 ? 21 
ATOM   5640 C CA  . GLU E 2 155 ? -16.502 -9.443  23.590  1.000 44.310  0 484 GLU EEE CA  1 ? 21 
ATOM   5641 C C   . GLU E 2 155 ? -17.728 -9.801  24.433  1.000 45.019  0 484 GLU EEE C   1 ? 21 
ATOM   5642 O O   . GLU E 2 155 ? -18.850 -9.760  23.898  1.000 46.657  0 484 GLU EEE O   1 ? 21 
ATOM   5643 C CB  . GLU E 2 155 ? -16.105 -7.973  23.757  1.000 44.323  0 484 GLU EEE CB  1 ? 21 
ATOM   5644 C CG  . GLU E 2 155 ? -14.858 -7.584  22.973  1.000 45.166  0 484 GLU EEE CG  1 ? 21 
ATOM   5645 C CD  . GLU E 2 155 ? -14.442 -6.123  23.083  1.000 45.230  0 484 GLU EEE CD  1 ? 21 
ATOM   5646 O OE1 . GLU E 2 155 ? -14.799 -5.478  24.089  1.000 46.426  0 484 GLU EEE OE1 1 ? 21 
ATOM   5647 O OE2 . GLU E 2 155 ? -13.750 -5.628  22.168  1.000 44.414  0 484 GLU EEE OE2 1 ? 21 
ATOM   5648 N N   . GLY E 2 156 ? -17.495 -10.154 25.697  1.000 44.818  0 485 GLY EEE N   1 ? 21 
ATOM   5649 C CA  . GLY E 2 156 ? -18.512 -10.563 26.681  1.000 44.779  0 485 GLY EEE CA  1 ? 21 
ATOM   5650 C C   . GLY E 2 156 ? -17.839 -11.153 27.907  1.000 46.077  0 485 GLY EEE C   1 ? 21 
ATOM   5651 O O   . GLY E 2 156 ? -16.663 -10.818 28.141  1.000 44.278  0 485 GLY EEE O   1 ? 21 
ATOM   5652 N N   . PHE E 2 157 ? -18.540 -12.003 28.662  1.000 46.891  0 486 PHE EEE N   1 ? 21 
ATOM   5653 C CA  . PHE E 2 157 ? -17.967 -12.725 29.826  1.000 47.748  0 486 PHE EEE CA  1 ? 21 
ATOM   5654 C C   . PHE E 2 157 ? -16.652 -13.385 29.401  1.000 47.420  0 486 PHE EEE C   1 ? 21 
ATOM   5655 O O   . PHE E 2 157 ? -16.641 -14.093 28.379  1.000 48.332  0 486 PHE EEE O   1 ? 21 
ATOM   5656 C CB  . PHE E 2 157 ? -18.934 -13.773 30.380  1.000 49.387  0 486 PHE EEE CB  1 ? 21 
ATOM   5657 C CG  . PHE E 2 157 ? -18.430 -14.450 31.629  1.000 51.715  0 486 PHE EEE CG  1 ? 21 
ATOM   5658 C CD1 . PHE E 2 157 ? -18.335 -13.747 32.822  1.000 52.321  0 486 PHE EEE CD1 1 ? 21 
ATOM   5659 C CD2 . PHE E 2 157 ? -18.018 -15.774 31.610  1.000 53.262  0 486 PHE EEE CD2 1 ? 21 
ATOM   5660 C CE1 . PHE E 2 157 ? -17.864 -14.357 33.975  1.000 54.119  0 486 PHE EEE CE1 1 ? 21 
ATOM   5661 C CE2 . PHE E 2 157 ? -17.549 -16.384 32.765  1.000 56.111  0 486 PHE EEE CE2 1 ? 21 
ATOM   5662 C CZ  . PHE E 2 157 ? -17.477 -15.676 33.947  1.000 55.880  0 486 PHE EEE CZ  1 ? 21 
ATOM   5663 N N   . ASN E 2 158 ? -15.579 -13.122 30.149  1.000 47.755  0 487 ASN EEE N   1 ? 21 
ATOM   5664 C CA  . ASN E 2 158 ? -14.226 -13.714 29.960  1.000 49.463  0 487 ASN EEE CA  1 ? 21 
ATOM   5665 C C   . ASN E 2 158 ? -13.709 -13.467 28.533  1.000 48.560  0 487 ASN EEE C   1 ? 21 
ATOM   5666 O O   . ASN E 2 158 ? -12.841 -14.240 28.091  1.000 49.344  0 487 ASN EEE O   1 ? 21 
ATOM   5667 C CB  . ASN E 2 158 ? -14.220 -15.208 30.302  1.000 51.387  0 487 ASN EEE CB  1 ? 21 
ATOM   5668 C CG  . ASN E 2 158 ? -13.966 -15.487 31.769  1.000 53.024  0 487 ASN EEE CG  1 ? 21 
ATOM   5669 O OD1 . ASN E 2 158 ? -13.348 -14.690 32.470  1.000 51.503  0 487 ASN EEE OD1 1 ? 21 
ATOM   5670 N ND2 . ASN E 2 158 ? -14.438 -16.628 32.242  1.000 56.052  0 487 ASN EEE ND2 1 ? 21 
ATOM   5671 N N   . CYS E 2 159 ? -14.191 -12.418 27.858  1.000 48.168  0 488 CYS EEE N   1 ? 21 
ATOM   5672 C CA  . CYS E 2 159 ? -13.812 -12.042 26.469  1.000 49.148  0 488 CYS EEE CA  1 ? 21 
ATOM   5673 C C   . CYS E 2 159 ? -13.685 -10.519 26.389  1.000 48.669  0 488 CYS EEE C   1 ? 21 
ATOM   5674 O O   . CYS E 2 159 ? -14.692 -9.835  26.126  1.000 49.533  0 488 CYS EEE O   1 ? 21 
ATOM   5675 C CB  . CYS E 2 159 ? -14.817 -12.582 25.459  1.000 49.919  0 488 CYS EEE CB  1 ? 21 
ATOM   5676 S SG  . CYS E 2 159 ? -14.648 -14.369 25.192  1.000 51.812  0 488 CYS EEE SG  1 ? 21 
ATOM   5677 N N   . TYR E 2 160 ? -12.475 -10.015 26.627  1.000 48.006  0 489 TYR EEE N   1 ? 21 
ATOM   5678 C CA  . TYR E 2 160 ? -12.194 -8.579  26.877  1.000 46.567  0 489 TYR EEE CA  1 ? 21 
ATOM   5679 C C   . TYR E 2 160 ? -11.188 -8.085  25.844  1.000 44.735  0 489 TYR EEE C   1 ? 21 
ATOM   5680 O O   . TYR E 2 160 ? -10.317 -8.876  25.459  1.000 46.378  0 489 TYR EEE O   1 ? 21 
ATOM   5681 C CB  . TYR E 2 160 ? -11.686 -8.389  28.308  1.000 45.070  0 489 TYR EEE CB  1 ? 21 
ATOM   5682 C CG  . TYR E 2 160 ? -12.598 -8.986  29.346  1.000 45.172  0 489 TYR EEE CG  1 ? 21 
ATOM   5683 C CD1 . TYR E 2 160 ? -13.891 -8.516  29.492  1.000 44.567  0 489 TYR EEE CD1 1 ? 21 
ATOM   5684 C CD2 . TYR E 2 160 ? -12.190 -10.034 30.157  1.000 45.834  0 489 TYR EEE CD2 1 ? 21 
ATOM   5685 C CE1 . TYR E 2 160 ? -14.753 -9.056  30.429  1.000 45.003  0 489 TYR EEE CE1 1 ? 21 
ATOM   5686 C CE2 . TYR E 2 160 ? -13.041 -10.586 31.102  1.000 46.363  0 489 TYR EEE CE2 1 ? 21 
ATOM   5687 C CZ  . TYR E 2 160 ? -14.329 -10.098 31.234  1.000 46.005  0 489 TYR EEE CZ  1 ? 21 
ATOM   5688 O OH  . TYR E 2 160 ? -15.174 -10.636 32.159  1.000 48.841  0 489 TYR EEE OH  1 ? 21 
ATOM   5689 N N   . PHE E 2 161 ? -11.318 -6.824  25.423  1.000 43.713  0 490 PHE EEE N   1 ? 21 
ATOM   5690 C CA  . PHE E 2 161 ? -10.293 -6.117  24.618  1.000 43.481  0 490 PHE EEE CA  1 ? 21 
ATOM   5691 C C   . PHE E 2 161 ? -9.056  -5.982  25.500  1.000 42.489  0 490 PHE EEE C   1 ? 21 
ATOM   5692 O O   . PHE E 2 161 ? -9.171  -5.598  26.666  1.000 42.404  0 490 PHE EEE O   1 ? 21 
ATOM   5693 C CB  . PHE E 2 161 ? -10.806 -4.771  24.096  1.000 43.728  0 490 PHE EEE CB  1 ? 21 
ATOM   5694 C CG  . PHE E 2 161 ? -10.007 -4.235  22.934  1.000 44.639  0 490 PHE EEE CG  1 ? 21 
ATOM   5695 C CD1 . PHE E 2 161 ? -10.017 -4.888  21.711  1.000 45.274  0 490 PHE EEE CD1 1 ? 21 
ATOM   5696 C CD2 . PHE E 2 161 ? -9.215  -3.102  23.068  1.000 45.372  0 490 PHE EEE CD2 1 ? 21 
ATOM   5697 C CE1 . PHE E 2 161 ? -9.266  -4.413  20.647  1.000 46.517  0 490 PHE EEE CE1 1 ? 21 
ATOM   5698 C CE2 . PHE E 2 161 ? -8.460  -2.633  22.006  1.000 45.246  0 490 PHE EEE CE2 1 ? 21 
ATOM   5699 C CZ  . PHE E 2 161 ? -8.492  -3.285  20.796  1.000 46.677  0 490 PHE EEE CZ  1 ? 21 
ATOM   5700 N N   . PRO E 2 162 ? -7.853  -6.354  25.001  1.000 41.757  0 491 PRO EEE N   1 ? 21 
ATOM   5701 C CA  . PRO E 2 162 ? -6.664  -6.412  25.852  1.000 42.045  0 491 PRO EEE CA  1 ? 21 
ATOM   5702 C C   . PRO E 2 162 ? -6.046  -5.044  26.177  1.000 41.140  0 491 PRO EEE C   1 ? 21 
ATOM   5703 O O   . PRO E 2 162 ? -5.232  -5.000  27.076  1.000 41.551  0 491 PRO EEE O   1 ? 21 
ATOM   5704 C CB  . PRO E 2 162 ? -5.697  -7.263  25.018  1.000 43.276  0 491 PRO EEE CB  1 ? 21 
ATOM   5705 C CG  . PRO E 2 162 ? -6.075  -6.934  23.589  1.000 43.844  0 491 PRO EEE CG  1 ? 21 
ATOM   5706 C CD  . PRO E 2 162 ? -7.580  -6.783  23.620  1.000 42.590  0 491 PRO EEE CD  1 ? 21 
ATOM   5707 N N   . LEU E 2 163 ? -6.439  -3.981  25.467  1.000 40.719  0 492 LEU EEE N   1 ? 21 
ATOM   5708 C CA  . LEU E 2 163 ? -5.839  -2.629  25.622  1.000 40.769  0 492 LEU EEE CA  1 ? 21 
ATOM   5709 C C   . LEU E 2 163 ? -6.816  -1.694  26.341  1.000 41.099  0 492 LEU EEE C   1 ? 21 
ATOM   5710 O O   . LEU E 2 163 ? -8.036  -1.942  26.297  1.000 40.340  0 492 LEU EEE O   1 ? 21 
ATOM   5711 C CB  . LEU E 2 163 ? -5.456  -2.082  24.245  1.000 41.162  0 492 LEU EEE CB  1 ? 21 
ATOM   5712 C CG  . LEU E 2 163 ? -4.393  -2.881  23.493  1.000 41.494  0 492 LEU EEE CG  1 ? 21 
ATOM   5713 C CD1 . LEU E 2 163 ? -3.980  -2.159  22.214  1.000 42.603  0 492 LEU EEE CD1 1 ? 21 
ATOM   5714 C CD2 . LEU E 2 163 ? -3.175  -3.141  24.367  1.000 40.674  0 492 LEU EEE CD2 1 ? 21 
ATOM   5715 N N   . GLN E 2 164 ? -6.268  -0.653  26.972  1.000 41.928  0 493 GLN EEE N   1 ? 21 
ATOM   5716 C CA  . GLN E 2 164 ? -7.006  0.336   27.798  1.000 43.125  0 493 GLN EEE CA  1 ? 21 
ATOM   5717 C C   . GLN E 2 164 ? -6.275  1.682   27.707  1.000 43.071  0 493 GLN EEE C   1 ? 21 
ATOM   5718 O O   . GLN E 2 164 ? -5.037  1.674   27.768  1.000 45.024  0 493 GLN EEE O   1 ? 21 
ATOM   5719 C CB  . GLN E 2 164 ? -7.105  -0.202  29.232  1.000 43.731  0 493 GLN EEE CB  1 ? 21 
ATOM   5720 C CG  . GLN E 2 164 ? -7.716  0.764   30.240  1.000 45.175  0 493 GLN EEE CG  1 ? 21 
ATOM   5721 C CD  . GLN E 2 164 ? -9.225  0.755   30.265  1.000 46.450  0 493 GLN EEE CD  1 ? 21 
ATOM   5722 O OE1 . GLN E 2 164 ? -9.870  -0.291  30.197  1.000 47.420  0 493 GLN EEE OE1 1 ? 21 
ATOM   5723 N NE2 . GLN E 2 164 ? -9.806  1.936   30.392  1.000 48.707  0 493 GLN EEE NE2 1 ? 21 
ATOM   5724 N N   . SER E 2 165 ? -7.013  2.784   27.541  1.000 43.420  0 494 SER EEE N   1 ? 21 
ATOM   5725 C CA  . SER E 2 165 ? -6.490  4.175   27.585  1.000 44.165  0 494 SER EEE CA  1 ? 21 
ATOM   5726 C C   . SER E 2 165 ? -6.121  4.538   29.027  1.000 45.059  0 494 SER EEE C   1 ? 21 
ATOM   5727 O O   . SER E 2 165 ? -6.909  4.204   29.932  1.000 45.632  0 494 SER EEE O   1 ? 21 
ATOM   5728 C CB  . SER E 2 165 ? -7.498  5.169   27.049  1.000 44.872  0 494 SER EEE CB  1 ? 21 
ATOM   5729 O OG  . SER E 2 165 ? -7.725  4.988   25.659  1.000 44.893  0 494 SER EEE OG  1 ? 21 
ATOM   5730 N N   . TYR E 2 166 ? -4.982  5.207   29.227  1.000 44.450  0 495 TYR EEE N   1 ? 21 
ATOM   5731 C CA  . TYR E 2 166 ? -4.772  6.151   30.354  1.000 45.104  0 495 TYR EEE CA  1 ? 21 
ATOM   5732 C C   . TYR E 2 166 ? -5.714  7.340   30.142  1.000 47.366  0 495 TYR EEE C   1 ? 21 
ATOM   5733 O O   . TYR E 2 166 ? -5.980  7.686   28.974  1.000 48.709  0 495 TYR EEE O   1 ? 21 
ATOM   5734 C CB  . TYR E 2 166 ? -3.335  6.673   30.424  1.000 45.123  0 495 TYR EEE CB  1 ? 21 
ATOM   5735 C CG  . TYR E 2 166 ? -2.288  5.644   30.764  1.000 43.818  0 495 TYR EEE CG  1 ? 21 
ATOM   5736 C CD1 . TYR E 2 166 ? -2.127  5.189   32.062  1.000 42.949  0 495 TYR EEE CD1 1 ? 21 
ATOM   5737 C CD2 . TYR E 2 166 ? -1.436  5.145   29.790  1.000 42.522  0 495 TYR EEE CD2 1 ? 21 
ATOM   5738 C CE1 . TYR E 2 166 ? -1.162  4.250   32.382  1.000 41.650  0 495 TYR EEE CE1 1 ? 21 
ATOM   5739 C CE2 . TYR E 2 166 ? -0.462  4.208   30.094  1.000 41.868  0 495 TYR EEE CE2 1 ? 21 
ATOM   5740 C CZ  . TYR E 2 166 ? -0.324  3.760   31.395  1.000 41.324  0 495 TYR EEE CZ  1 ? 21 
ATOM   5741 O OH  . TYR E 2 166 ? 0.632   2.833   31.687  1.000 41.251  0 495 TYR EEE OH  1 ? 21 
ATOM   5742 N N   . GLY E 2 167 ? -6.193  7.944   31.230  1.000 48.656  0 496 GLY EEE N   1 ? 21 
ATOM   5743 C CA  . GLY E 2 167 ? -6.990  9.185   31.202  1.000 51.274  0 496 GLY EEE CA  1 ? 21 
ATOM   5744 C C   . GLY E 2 167 ? -6.179  10.360  31.709  1.000 53.638  0 496 GLY EEE C   1 ? 21 
ATOM   5745 O O   . GLY E 2 167 ? -6.397  10.763  32.858  1.000 57.487  0 496 GLY EEE O   1 ? 21 
ATOM   5746 N N   . PHE E 2 168 ? -5.266  10.890  30.894  1.000 54.107  0 497 PHE EEE N   1 ? 21 
ATOM   5747 C CA  . PHE E 2 168 ? -4.361  12.003  31.283  1.000 56.269  0 497 PHE EEE CA  1 ? 21 
ATOM   5748 C C   . PHE E 2 168 ? -5.111  13.334  31.168  1.000 60.478  0 497 PHE EEE C   1 ? 21 
ATOM   5749 O O   . PHE E 2 168 ? -5.342  13.813  30.045  1.000 61.739  0 497 PHE EEE O   1 ? 21 
ATOM   5750 C CB  . PHE E 2 168 ? -3.074  11.983  30.453  1.000 54.813  0 497 PHE EEE CB  1 ? 21 
ATOM   5751 C CG  . PHE E 2 168 ? -2.191  10.787  30.706  1.000 52.095  0 497 PHE EEE CG  1 ? 21 
ATOM   5752 C CD1 . PHE E 2 168 ? -1.885  10.391  32.001  1.000 51.372  0 497 PHE EEE CD1 1 ? 21 
ATOM   5753 C CD2 . PHE E 2 168 ? -1.660  10.058  29.651  1.000 50.372  0 497 PHE EEE CD2 1 ? 21 
ATOM   5754 C CE1 . PHE E 2 168 ? -1.078  9.289   32.235  1.000 48.880  0 497 PHE EEE CE1 1 ? 21 
ATOM   5755 C CE2 . PHE E 2 168 ? -0.848  8.960   29.887  1.000 48.309  0 497 PHE EEE CE2 1 ? 21 
ATOM   5756 C CZ  . PHE E 2 168 ? -0.561  8.576   31.179  1.000 48.154  0 497 PHE EEE CZ  1 ? 21 
ATOM   5757 N N   . GLN E 2 169 ? -5.487  13.892  32.320  1.000 64.447  0 498 GLN EEE N   1 ? 21 
ATOM   5758 C CA  . GLN E 2 169 ? -6.060  15.254  32.478  1.000 70.069  0 498 GLN EEE CA  1 ? 21 
ATOM   5759 C C   . GLN E 2 169 ? -5.092  16.088  33.314  1.000 71.364  0 498 GLN EEE C   1 ? 21 
ATOM   5760 O O   . GLN E 2 169 ? -4.403  15.547  34.177  1.000 69.728  0 498 GLN EEE O   1 ? 21 
ATOM   5761 C CB  . GLN E 2 169 ? -7.444  15.160  33.119  1.000 72.875  0 498 GLN EEE CB  1 ? 21 
ATOM   5762 C CG  . GLN E 2 169 ? -8.364  14.195  32.387  1.000 73.629  0 498 GLN EEE CG  1 ? 21 
ATOM   5763 C CD  . GLN E 2 169 ? -9.752  14.162  32.975  1.000 76.638  0 498 GLN EEE CD  1 ? 21 
ATOM   5764 O OE1 . GLN E 2 169 ? -10.737 14.473  32.309  1.000 78.108  0 498 GLN EEE OE1 1 ? 21 
ATOM   5765 N NE2 . GLN E 2 169 ? -9.836  13.787  34.241  1.000 78.415  0 498 GLN EEE NE2 1 ? 21 
ATOM   5766 N N   . PRO E 2 170 ? -5.000  17.418  33.082  1.000 61.939  0 499 PRO EEE N   1 ? 22 
ATOM   5767 C CA  . PRO E 2 170 ? -4.060  18.267  33.816  1.000 63.238  0 499 PRO EEE CA  1 ? 22 
ATOM   5768 C C   . PRO E 2 170 ? -4.232  18.199  35.342  1.000 63.575  0 499 PRO EEE C   1 ? 22 
ATOM   5769 O O   . PRO E 2 170 ? -3.241  18.248  36.039  1.000 64.527  0 499 PRO EEE O   1 ? 22 
ATOM   5770 C CB  . PRO E 2 170 ? -4.380  19.691  33.331  1.000 66.244  0 499 PRO EEE CB  1 ? 22 
ATOM   5771 C CG  . PRO E 2 170 ? -5.067  19.498  31.994  1.000 65.858  0 499 PRO EEE CG  1 ? 22 
ATOM   5772 C CD  . PRO E 2 170 ? -5.796  18.176  32.103  1.000 63.605  0 499 PRO EEE CD  1 ? 22 
ATOM   5773 N N   . THR E 2 171 ? -5.478  18.072  35.811  1.000 63.504  0 500 THR EEE N   1 ? 22 
ATOM   5774 C CA  . THR E 2 171 ? -5.880  18.155  37.245  1.000 63.413  0 500 THR EEE CA  1 ? 22 
ATOM   5775 C C   . THR E 2 171 ? -5.753  16.788  37.936  1.000 61.896  0 500 THR EEE C   1 ? 22 
ATOM   5776 O O   . THR E 2 171 ? -6.089  16.710  39.130  1.000 62.328  0 500 THR EEE O   1 ? 22 
ATOM   5777 C CB  . THR E 2 171 ? -7.289  18.746  37.366  1.000 64.081  0 500 THR EEE CB  1 ? 22 
ATOM   5778 O OG1 . THR E 2 171 ? -8.165  18.009  36.510  1.000 62.167  0 500 THR EEE OG1 1 ? 22 
ATOM   5779 C CG2 . THR E 2 171 ? -7.320  20.216  37.005  1.000 65.651  0 500 THR EEE CG2 1 ? 22 
ATOM   5780 N N   . ASN E 2 172 ? -5.269  15.755  37.237  1.000 60.745  0 501 ASN EEE N   1 ? 22 
ATOM   5781 C CA  . ASN E 2 172 ? -4.913  14.436  37.832  1.000 60.614  0 501 ASN EEE CA  1 ? 22 
ATOM   5782 C C   . ASN E 2 172 ? -3.921  14.629  38.987  1.000 62.650  0 501 ASN EEE C   1 ? 22 
ATOM   5783 O O   . ASN E 2 172 ? -3.092  15.561  38.910  1.000 63.651  0 501 ASN EEE O   1 ? 22 
ATOM   5784 C CB  . ASN E 2 172 ? -4.275  13.486  36.810  1.000 58.780  0 501 ASN EEE CB  1 ? 22 
ATOM   5785 C CG  . ASN E 2 172 ? -5.274  12.798  35.905  1.000 57.573  0 501 ASN EEE CG  1 ? 22 
ATOM   5786 O OD1 . ASN E 2 172 ? -6.477  13.032  35.997  1.000 56.835  0 501 ASN EEE OD1 1 ? 22 
ATOM   5787 N ND2 . ASN E 2 172 ? -4.778  11.939  35.028  1.000 56.024  0 501 ASN EEE ND2 1 ? 22 
ATOM   5788 N N   . GLY E 2 173 ? -3.991  13.757  40.000  1.000 62.690  0 502 GLY EEE N   1 ? 22 
ATOM   5789 C CA  . GLY E 2 173 ? -2.918  13.569  40.996  1.000 63.681  0 502 GLY EEE CA  1 ? 22 
ATOM   5790 C C   . GLY E 2 173 ? -1.637  13.104  40.322  1.000 63.054  0 502 GLY EEE C   1 ? 22 
ATOM   5791 O O   . GLY E 2 173 ? -1.734  12.444  39.266  1.000 60.626  0 502 GLY EEE O   1 ? 22 
ATOM   5792 N N   . VAL E 2 174 ? -0.478  13.411  40.912  1.000 64.356  0 503 VAL EEE N   1 ? 22 
ATOM   5793 C CA  . VAL E 2 174 ? 0.866   13.180  40.295  1.000 62.304  0 503 VAL EEE CA  1 ? 22 
ATOM   5794 C C   . VAL E 2 174 ? 0.995   11.703  39.895  1.000 58.999  0 503 VAL EEE C   1 ? 22 
ATOM   5795 O O   . VAL E 2 174 ? 1.568   11.433  38.826  1.000 57.209  0 503 VAL EEE O   1 ? 22 
ATOM   5796 C CB  . VAL E 2 174 ? 2.010   13.612  41.233  1.000 64.910  0 503 VAL EEE CB  1 ? 22 
ATOM   5797 C CG1 . VAL E 2 174 ? 3.371   13.364  40.601  1.000 63.379  0 503 VAL EEE CG1 1 ? 22 
ATOM   5798 C CG2 . VAL E 2 174 ? 1.882   15.069  41.649  1.000 68.342  0 503 VAL EEE CG2 1 ? 22 
ATOM   5799 N N   . GLY E 2 175 ? 0.485   10.785  40.722  1.000 59.473  0 504 GLY EEE N   1 ? 22 
ATOM   5800 C CA  . GLY E 2 175 ? 0.498   9.331   40.464  1.000 58.196  0 504 GLY EEE CA  1 ? 22 
ATOM   5801 C C   . GLY E 2 175 ? -0.174  8.970   39.147  1.000 56.633  0 504 GLY EEE C   1 ? 22 
ATOM   5802 O O   . GLY E 2 175 ? 0.256   7.981   38.519  1.000 54.705  0 504 GLY EEE O   1 ? 22 
ATOM   5803 N N   . TYR E 2 176 ? -1.193  9.738   38.745  1.000 56.905  0 505 TYR EEE N   1 ? 22 
ATOM   5804 C CA  . TYR E 2 176 ? -2.025  9.499   37.536  1.000 55.592  0 505 TYR EEE CA  1 ? 22 
ATOM   5805 C C   . TYR E 2 176 ? -1.662  10.489  36.421  1.000 53.674  0 505 TYR EEE C   1 ? 22 
ATOM   5806 O O   . TYR E 2 176 ? -2.355  10.501  35.389  1.000 52.871  0 505 TYR EEE O   1 ? 22 
ATOM   5807 C CB  . TYR E 2 176 ? -3.506  9.576   37.913  1.000 57.351  0 505 TYR EEE CB  1 ? 22 
ATOM   5808 C CG  . TYR E 2 176 ? -4.002  8.363   38.654  1.000 60.218  0 505 TYR EEE CG  1 ? 22 
ATOM   5809 C CD1 . TYR E 2 176 ? -3.947  8.295   40.037  1.000 62.734  0 505 TYR EEE CD1 1 ? 22 
ATOM   5810 C CD2 . TYR E 2 176 ? -4.504  7.268   37.968  1.000 60.912  0 505 TYR EEE CD2 1 ? 22 
ATOM   5811 C CE1 . TYR E 2 176 ? -4.393  7.177   40.723  1.000 64.671  0 505 TYR EEE CE1 1 ? 22 
ATOM   5812 C CE2 . TYR E 2 176 ? -4.955  6.142   38.638  1.000 62.921  0 505 TYR EEE CE2 1 ? 22 
ATOM   5813 C CZ  . TYR E 2 176 ? -4.895  6.095   40.021  1.000 64.693  0 505 TYR EEE CZ  1 ? 22 
ATOM   5814 O OH  . TYR E 2 176 ? -5.335  4.988   40.686  1.000 66.756  0 505 TYR EEE OH  1 ? 22 
ATOM   5815 N N   . GLN E 2 177 ? -0.613  11.292  36.614  1.000 53.397  0 506 GLN EEE N   1 ? 22 
ATOM   5816 C CA  . GLN E 2 177 ? -0.072  12.198  35.566  1.000 52.978  0 506 GLN EEE CA  1 ? 22 
ATOM   5817 C C   . GLN E 2 177 ? 0.861   11.396  34.668  1.000 51.378  0 506 GLN EEE C   1 ? 22 
ATOM   5818 O O   . GLN E 2 177 ? 1.448   10.405  35.098  1.000 50.250  0 506 GLN EEE O   1 ? 22 
ATOM   5819 C CB  . GLN E 2 177 ? 0.640   13.403  36.178  1.000 54.649  0 506 GLN EEE CB  1 ? 22 
ATOM   5820 C CG  . GLN E 2 177 ? -0.327  14.481  36.640  1.000 56.497  0 506 GLN EEE CG  1 ? 22 
ATOM   5821 C CD  . GLN E 2 177 ? 0.363   15.650  37.295  1.000 58.364  0 506 GLN EEE CD  1 ? 22 
ATOM   5822 O OE1 . GLN E 2 177 ? 1.536   15.932  37.051  1.000 57.345  0 506 GLN EEE OE1 1 ? 22 
ATOM   5823 N NE2 . GLN E 2 177 ? -0.377  16.348  38.140  1.000 60.924  0 506 GLN EEE NE2 1 ? 22 
ATOM   5824 N N   . PRO E 2 178 ? 1.005   11.789  33.384  1.000 51.800  0 507 PRO EEE N   1 ? 22 
ATOM   5825 C CA  . PRO E 2 178 ? 1.852   11.052  32.451  1.000 50.771  0 507 PRO EEE CA  1 ? 22 
ATOM   5826 C C   . PRO E 2 178 ? 3.335   11.287  32.761  1.000 51.441  0 507 PRO EEE C   1 ? 22 
ATOM   5827 O O   . PRO E 2 178 ? 3.699   12.400  33.112  1.000 53.588  0 507 PRO EEE O   1 ? 22 
ATOM   5828 C CB  . PRO E 2 178 ? 1.453   11.630  31.086  1.000 51.367  0 507 PRO EEE CB  1 ? 22 
ATOM   5829 C CG  . PRO E 2 178 ? 1.027   13.050  31.397  1.000 52.402  0 507 PRO EEE CG  1 ? 22 
ATOM   5830 C CD  . PRO E 2 178 ? 0.375   12.966  32.762  1.000 53.404  0 507 PRO EEE CD  1 ? 22 
ATOM   5831 N N   . TYR E 2 179 ? 4.140   10.229  32.650  1.000 50.730  0 508 TYR EEE N   1 ? 22 
ATOM   5832 C CA  . TYR E 2 179 ? 5.619   10.274  32.766  1.000 50.609  0 508 TYR EEE CA  1 ? 22 
ATOM   5833 C C   . TYR E 2 179 ? 6.218   9.703   31.483  1.000 48.750  0 508 TYR EEE C   1 ? 22 
ATOM   5834 O O   . TYR E 2 179 ? 5.859   8.575   31.092  1.000 47.106  0 508 TYR EEE O   1 ? 22 
ATOM   5835 C CB  . TYR E 2 179 ? 6.089   9.543   34.029  1.000 51.563  0 508 TYR EEE CB  1 ? 22 
ATOM   5836 C CG  . TYR E 2 179 ? 6.080   10.420  35.255  1.000 53.821  0 508 TYR EEE CG  1 ? 22 
ATOM   5837 C CD1 . TYR E 2 179 ? 4.887   10.876  35.792  1.000 54.537  0 508 TYR EEE CD1 1 ? 22 
ATOM   5838 C CD2 . TYR E 2 179 ? 7.257   10.837  35.857  1.000 53.846  0 508 TYR EEE CD2 1 ? 22 
ATOM   5839 C CE1 . TYR E 2 179 ? 4.860   11.707  36.901  1.000 56.431  0 508 TYR EEE CE1 1 ? 22 
ATOM   5840 C CE2 . TYR E 2 179 ? 7.247   11.669  36.966  1.000 55.906  0 508 TYR EEE CE2 1 ? 22 
ATOM   5841 C CZ  . TYR E 2 179 ? 6.044   12.106  37.491  1.000 56.377  0 508 TYR EEE CZ  1 ? 22 
ATOM   5842 O OH  . TYR E 2 179 ? 6.015   12.927  38.580  1.000 59.279  0 508 TYR EEE OH  1 ? 22 
ATOM   5843 N N   . ARG E 2 180 ? 7.069   10.491  30.827  1.000 49.300  0 509 ARG EEE N   1 ? 22 
ATOM   5844 C CA  . ARG E 2 180 ? 7.908   10.030  29.694  1.000 49.441  0 509 ARG EEE CA  1 ? 22 
ATOM   5845 C C   . ARG E 2 180 ? 9.101   9.257   30.265  1.000 48.952  0 509 ARG EEE C   1 ? 22 
ATOM   5846 O O   . ARG E 2 180 ? 9.679   9.703   31.276  1.000 47.744  0 509 ARG EEE O   1 ? 22 
ATOM   5847 C CB  . ARG E 2 180 ? 8.323   11.212  28.818  1.000 50.519  0 509 ARG EEE CB  1 ? 22 
ATOM   5848 C CG  . ARG E 2 180 ? 7.184   11.703  27.940  1.000 51.479  0 509 ARG EEE CG  1 ? 22 
ATOM   5849 C CD  . ARG E 2 180 ? 7.520   12.897  27.072  1.000 53.296  0 509 ARG EEE CD  1 ? 22 
ATOM   5850 N NE  . ARG E 2 180 ? 6.356   13.206  26.250  1.000 54.389  0 509 ARG EEE NE  1 ? 22 
ATOM   5851 C CZ  . ARG E 2 180 ? 6.382   13.832  25.080  1.000 57.094  0 509 ARG EEE CZ  1 ? 22 
ATOM   5852 N NH1 . ARG E 2 180 ? 7.531   14.245  24.569  1.000 58.826  0 509 ARG EEE NH1 1 ? 22 
ATOM   5853 N NH2 . ARG E 2 180 ? 5.252   14.042  24.423  1.000 57.594  0 509 ARG EEE NH2 1 ? 22 
ATOM   5854 N N   . VAL E 2 181 ? 9.418   8.122   29.644  1.000 48.620  0 510 VAL EEE N   1 ? 22 
ATOM   5855 C CA  . VAL E 2 181 ? 10.455  7.159   30.106  1.000 47.466  0 510 VAL EEE CA  1 ? 22 
ATOM   5856 C C   . VAL E 2 181 ? 11.402  6.875   28.937  1.000 48.525  0 510 VAL EEE C   1 ? 22 
ATOM   5857 O O   . VAL E 2 181 ? 10.909  6.644   27.814  1.000 47.636  0 510 VAL EEE O   1 ? 22 
ATOM   5858 C CB  . VAL E 2 181 ? 9.800   5.869   30.631  1.000 46.885  0 510 VAL EEE CB  1 ? 22 
ATOM   5859 C CG1 . VAL E 2 181 ? 10.841  4.842   31.049  1.000 47.389  0 510 VAL EEE CG1 1 ? 22 
ATOM   5860 C CG2 . VAL E 2 181 ? 8.826   6.160   31.765  1.000 46.868  0 510 VAL EEE CG2 1 ? 22 
ATOM   5861 N N   . VAL E 2 182 ? 12.709  6.909   29.202  1.000 48.990  0 511 VAL EEE N   1 ? 22 
ATOM   5862 C CA  . VAL E 2 182 ? 13.769  6.424   28.273  1.000 48.957  0 511 VAL EEE CA  1 ? 22 
ATOM   5863 C C   . VAL E 2 182 ? 14.638  5.427   29.046  1.000 48.801  0 511 VAL EEE C   1 ? 22 
ATOM   5864 O O   . VAL E 2 182 ? 15.251  5.827   30.048  1.000 47.391  0 511 VAL EEE O   1 ? 22 
ATOM   5865 C CB  . VAL E 2 182 ? 14.604  7.581   27.697  1.000 51.198  0 511 VAL EEE CB  1 ? 22 
ATOM   5866 C CG1 . VAL E 2 182 ? 15.675  7.077   26.736  1.000 51.962  0 511 VAL EEE CG1 1 ? 22 
ATOM   5867 C CG2 . VAL E 2 182 ? 13.727  8.628   27.029  1.000 51.851  0 511 VAL EEE CG2 1 ? 22 
ATOM   5868 N N   . VAL E 2 183 ? 14.654  4.169   28.603  1.000 48.740  0 512 VAL EEE N   1 ? 22 
ATOM   5869 C CA  . VAL E 2 183 ? 15.546  3.100   29.135  1.000 47.952  0 512 VAL EEE CA  1 ? 22 
ATOM   5870 C C   . VAL E 2 183 ? 16.747  2.978   28.191  1.000 48.790  0 512 VAL EEE C   1 ? 22 
ATOM   5871 O O   . VAL E 2 183 ? 16.551  2.579   27.020  1.000 48.235  0 512 VAL EEE O   1 ? 22 
ATOM   5872 C CB  . VAL E 2 183 ? 14.798  1.763   29.285  1.000 48.364  0 512 VAL EEE CB  1 ? 22 
ATOM   5873 C CG1 . VAL E 2 183 ? 15.681  0.694   29.910  1.000 48.961  0 512 VAL EEE CG1 1 ? 22 
ATOM   5874 C CG2 . VAL E 2 183 ? 13.508  1.923   30.076  1.000 47.744  0 512 VAL EEE CG2 1 ? 22 
ATOM   5875 N N   . LEU E 2 184 ? 17.943  3.319   28.683  1.000 48.557  0 513 LEU EEE N   1 ? 22 
ATOM   5876 C CA  . LEU E 2 184 ? 19.226  3.117   27.962  1.000 49.115  0 513 LEU EEE CA  1 ? 22 
ATOM   5877 C C   . LEU E 2 184 ? 19.794  1.745   28.339  1.000 50.305  0 513 LEU EEE C   1 ? 22 
ATOM   5878 O O   . LEU E 2 184 ? 20.072  1.537   29.522  1.000 52.179  0 513 LEU EEE O   1 ? 22 
ATOM   5879 C CB  . LEU E 2 184 ? 20.201  4.244   28.317  1.000 50.411  0 513 LEU EEE CB  1 ? 22 
ATOM   5880 C CG  . LEU E 2 184 ? 19.777  5.649   27.881  1.000 50.960  0 513 LEU EEE CG  1 ? 22 
ATOM   5881 C CD1 . LEU E 2 184 ? 20.857  6.667   28.216  1.000 52.006  0 513 LEU EEE CD1 1 ? 22 
ATOM   5882 C CD2 . LEU E 2 184 ? 19.443  5.697   26.395  1.000 50.787  0 513 LEU EEE CD2 1 ? 22 
ATOM   5883 N N   . SER E 2 185 ? 19.920  0.844   27.363  1.000 52.378  0 514 SER EEE N   1 ? 22 
ATOM   5884 C CA  . SER E 2 185 ? 20.655  -0.444  27.463  1.000 53.545  0 514 SER EEE CA  1 ? 22 
ATOM   5885 C C   . SER E 2 185 ? 22.009  -0.289  26.765  1.000 53.636  0 514 SER EEE C   1 ? 22 
ATOM   5886 O O   . SER E 2 185 ? 22.053  0.348   25.703  1.000 56.627  0 514 SER EEE O   1 ? 22 
ATOM   5887 C CB  . SER E 2 185 ? 19.867  -1.574  26.867  1.000 54.215  0 514 SER EEE CB  1 ? 22 
ATOM   5888 O OG  . SER E 2 185 ? 18.566  -1.614  27.417  1.000 57.676  0 514 SER EEE OG  1 ? 22 
ATOM   5889 N N   . PHE E 2 186 ? 23.067  -0.847  27.347  1.000 52.798  0 515 PHE EEE N   1 ? 22 
ATOM   5890 C CA  . PHE E 2 186 ? 24.456  -0.764  26.830  1.000 53.215  0 515 PHE EEE CA  1 ? 22 
ATOM   5891 C C   . PHE E 2 186 ? 24.906  -2.169  26.430  1.000 54.435  0 515 PHE EEE C   1 ? 22 
ATOM   5892 O O   . PHE E 2 186 ? 24.965  -3.048  27.308  1.000 58.989  0 515 PHE EEE O   1 ? 22 
ATOM   5893 C CB  . PHE E 2 186 ? 25.366  -0.119  27.876  1.000 52.472  0 515 PHE EEE CB  1 ? 22 
ATOM   5894 C CG  . PHE E 2 186 ? 24.942  1.273   28.269  1.000 51.897  0 515 PHE EEE CG  1 ? 22 
ATOM   5895 C CD1 . PHE E 2 186 ? 24.055  1.474   29.316  1.000 51.035  0 515 PHE EEE CD1 1 ? 22 
ATOM   5896 C CD2 . PHE E 2 186 ? 25.407  2.380   27.576  1.000 51.468  0 515 PHE EEE CD2 1 ? 22 
ATOM   5897 C CE1 . PHE E 2 186 ? 23.655  2.754   29.671  1.000 51.013  0 515 PHE EEE CE1 1 ? 22 
ATOM   5898 C CE2 . PHE E 2 186 ? 25.004  3.658   27.931  1.000 52.151  0 515 PHE EEE CE2 1 ? 22 
ATOM   5899 C CZ  . PHE E 2 186 ? 24.130  3.845   28.979  1.000 51.976  0 515 PHE EEE CZ  1 ? 22 
ATOM   5900 N N   . GLU E 2 187 ? 25.192  -2.361  25.141  1.000 54.554  0 516 GLU EEE N   1 ? 22 
ATOM   5901 C CA  . GLU E 2 187 ? 25.583  -3.664  24.544  1.000 56.436  0 516 GLU EEE CA  1 ? 22 
ATOM   5902 C C   . GLU E 2 187 ? 27.091  -3.665  24.258  1.000 56.482  0 516 GLU EEE C   1 ? 22 
ATOM   5903 O O   . GLU E 2 187 ? 27.582  -2.703  23.632  1.000 53.940  0 516 GLU EEE O   1 ? 22 
ATOM   5904 C CB  . GLU E 2 187 ? 24.780  -3.907  23.267  1.000 57.972  0 516 GLU EEE CB  1 ? 22 
ATOM   5905 C CG  . GLU E 2 187 ? 24.873  -5.332  22.763  1.000 61.528  0 516 GLU EEE CG  1 ? 22 
ATOM   5906 C CD  . GLU E 2 187 ? 24.096  -5.602  21.484  1.000 63.544  0 516 GLU EEE CD  1 ? 22 
ATOM   5907 O OE1 . GLU E 2 187 ? 24.253  -4.825  20.509  1.000 62.327  0 516 GLU EEE OE1 1 ? 22 
ATOM   5908 O OE2 . GLU E 2 187 ? 23.333  -6.591  21.468  1.000 65.793  0 516 GLU EEE OE2 1 ? 22 
ATOM   5909 N N   . LEU E 2 188 ? 27.786  -4.715  24.705  1.000 56.843  0 517 LEU EEE N   1 ? 22 
ATOM   5910 C CA  . LEU E 2 188 ? 29.224  -4.967  24.431  1.000 58.394  0 517 LEU EEE CA  1 ? 22 
ATOM   5911 C C   . LEU E 2 188 ? 29.358  -6.385  23.864  1.000 60.504  0 517 LEU EEE C   1 ? 22 
ATOM   5912 O O   . LEU E 2 188 ? 29.105  -7.347  24.620  1.000 58.900  0 517 LEU EEE O   1 ? 22 
ATOM   5913 C CB  . LEU E 2 188 ? 30.027  -4.784  25.723  1.000 58.779  0 517 LEU EEE CB  1 ? 22 
ATOM   5914 C CG  . LEU E 2 188 ? 31.506  -4.441  25.533  1.000 60.158  0 517 LEU EEE CG  1 ? 22 
ATOM   5915 C CD1 . LEU E 2 188 ? 31.662  -3.051  24.936  1.000 59.787  0 517 LEU EEE CD1 1 ? 22 
ATOM   5916 C CD2 . LEU E 2 188 ? 32.274  -4.555  26.843  1.000 60.016  0 517 LEU EEE CD2 1 ? 22 
ATOM   5917 N N   . LEU E 2 189 ? 29.693  -6.493  22.572  1.000 63.544  0 518 LEU EEE N   1 ? 22 
ATOM   5918 C CA  . LEU E 2 189 ? 29.882  -7.775  21.839  1.000 67.031  0 518 LEU EEE CA  1 ? 22 
ATOM   5919 C C   . LEU E 2 189 ? 31.336  -7.883  21.370  1.000 68.135  0 518 LEU EEE C   1 ? 22 
ATOM   5920 O O   . LEU E 2 189 ? 32.044  -6.864  21.429  1.000 64.352  0 518 LEU EEE O   1 ? 22 
ATOM   5921 C CB  . LEU E 2 189 ? 28.926  -7.805  20.641  1.000 68.851  0 518 LEU EEE CB  1 ? 22 
ATOM   5922 C CG  . LEU E 2 189 ? 27.448  -7.571  20.949  1.000 67.615  0 518 LEU EEE CG  1 ? 22 
ATOM   5923 C CD1 . LEU E 2 189 ? 26.637  -7.534  19.661  1.000 68.993  0 518 LEU EEE CD1 1 ? 22 
ATOM   5924 C CD2 . LEU E 2 189 ? 26.901  -8.631  21.894  1.000 67.569  0 518 LEU EEE CD2 1 ? 22 
ATOM   5925 N N   . HIS E 2 190 ? 31.753  -9.072  20.918  1.000 73.186  0 519 HIS EEE N   1 ? 22 
ATOM   5926 C CA  . HIS E 2 190 ? 33.022  -9.304  20.175  1.000 78.502  0 519 HIS EEE CA  1 ? 22 
ATOM   5927 C C   . HIS E 2 190 ? 32.898  -8.643  18.795  1.000 79.038  0 519 HIS EEE C   1 ? 22 
ATOM   5928 O O   . HIS E 2 190 ? 32.712  -9.373  17.800  1.000 82.877  0 519 HIS EEE O   1 ? 22 
ATOM   5929 C CB  . HIS E 2 190 ? 33.328  -10.806 20.044  1.000 84.884  0 519 HIS EEE CB  1 ? 22 
ATOM   5930 C CG  . HIS E 2 190 ? 33.540  -11.526 21.333  1.000 88.930  0 519 HIS EEE CG  1 ? 22 
ATOM   5931 N ND1 . HIS E 2 190 ? 32.561  -12.317 21.912  1.000 92.277  0 519 HIS EEE ND1 1 ? 22 
ATOM   5932 C CD2 . HIS E 2 190 ? 34.620  -11.608 22.137  1.000 92.100  0 519 HIS EEE CD2 1 ? 22 
ATOM   5933 C CE1 . HIS E 2 190 ? 33.026  -12.840 23.030  1.000 94.383  0 519 HIS EEE CE1 1 ? 22 
ATOM   5934 N NE2 . HIS E 2 190 ? 34.289  -12.420 23.192  1.000 94.427  0 519 HIS EEE NE2 1 ? 22 
ATOM   5935 N N   . ALA E 2 191 ? 32.955  -7.309  18.749  1.000 76.590  0 520 ALA EEE N   1 ? 22 
ATOM   5936 C CA  . ALA E 2 191 ? 32.732  -6.481  17.541  1.000 77.421  0 520 ALA EEE CA  1 ? 22 
ATOM   5937 C C   . ALA E 2 191 ? 33.288  -5.082  17.777  1.000 75.756  0 520 ALA EEE C   1 ? 22 
ATOM   5938 O O   . ALA E 2 191 ? 33.505  -4.690  18.920  1.000 72.435  0 520 ALA EEE O   1 ? 22 
ATOM   5939 C CB  . ALA E 2 191 ? 31.260  -6.433  17.213  1.000 76.940  0 520 ALA EEE CB  1 ? 22 
ATOM   5940 N N   . PRO E 2 192 ? 33.541  -4.282  16.717  1.000 78.705  0 521 PRO EEE N   1 ? 22 
ATOM   5941 C CA  . PRO E 2 192 ? 34.014  -2.911  16.899  1.000 78.000  0 521 PRO EEE CA  1 ? 22 
ATOM   5942 C C   . PRO E 2 192 ? 32.989  -2.059  17.666  1.000 75.556  0 521 PRO EEE C   1 ? 22 
ATOM   5943 O O   . PRO E 2 192 ? 31.811  -2.140  17.359  1.000 76.071  0 521 PRO EEE O   1 ? 22 
ATOM   5944 C CB  . PRO E 2 192 ? 34.208  -2.383  15.469  1.000 80.332  0 521 PRO EEE CB  1 ? 22 
ATOM   5945 C CG  . PRO E 2 192 ? 34.282  -3.629  14.606  1.000 82.908  0 521 PRO EEE CG  1 ? 22 
ATOM   5946 C CD  . PRO E 2 192 ? 33.402  -4.647  15.299  1.000 80.801  0 521 PRO EEE CD  1 ? 22 
ATOM   5947 N N   . ALA E 2 193 ? 33.461  -1.293  18.653  1.000 74.407  0 522 ALA EEE N   1 ? 22 
ATOM   5948 C CA  . ALA E 2 193 ? 32.676  -0.290  19.408  1.000 71.845  0 522 ALA EEE CA  1 ? 22 
ATOM   5949 C C   . ALA E 2 193 ? 32.423  0.918   18.502  1.000 73.500  0 522 ALA EEE C   1 ? 22 
ATOM   5950 O O   . ALA E 2 193 ? 33.380  1.379   17.854  1.000 80.402  0 522 ALA EEE O   1 ? 22 
ATOM   5951 C CB  . ALA E 2 193 ? 33.402  0.108   20.665  1.000 70.612  0 522 ALA EEE CB  1 ? 22 
ATOM   5952 N N   . THR E 2 194 ? 31.178  1.390   18.436  1.000 70.362  0 523 THR EEE N   1 ? 22 
ATOM   5953 C CA  . THR E 2 194 ? 30.755  2.495   17.539  1.000 71.751  0 523 THR EEE CA  1 ? 22 
ATOM   5954 C C   . THR E 2 194 ? 30.158  3.657   18.349  1.000 69.359  0 523 THR EEE C   1 ? 22 
ATOM   5955 O O   . THR E 2 194 ? 29.999  4.742   17.756  1.000 71.513  0 523 THR EEE O   1 ? 22 
ATOM   5956 C CB  . THR E 2 194 ? 29.801  1.964   16.460  1.000 74.180  0 523 THR EEE CB  1 ? 22 
ATOM   5957 O OG1 . THR E 2 194 ? 28.513  1.731   17.032  1.000 71.363  0 523 THR EEE OG1 1 ? 22 
ATOM   5958 C CG2 . THR E 2 194 ? 30.302  0.695   15.807  1.000 75.642  0 523 THR EEE CG2 1 ? 22 
ATOM   5959 N N   . VAL E 2 195 ? 29.836  3.455   19.634  1.000 66.472  0 524 VAL EEE N   1 ? 22 
ATOM   5960 C CA  . VAL E 2 195 ? 29.240  4.504   20.516  1.000 65.002  0 524 VAL EEE CA  1 ? 22 
ATOM   5961 C C   . VAL E 2 195 ? 30.206  4.774   21.668  1.000 64.133  0 524 VAL EEE C   1 ? 22 
ATOM   5962 O O   . VAL E 2 195 ? 30.236  3.966   22.618  1.000 63.835  0 524 VAL EEE O   1 ? 22 
ATOM   5963 C CB  . VAL E 2 195 ? 27.850  4.110   21.050  1.000 62.777  0 524 VAL EEE CB  1 ? 22 
ATOM   5964 C CG1 . VAL E 2 195 ? 27.221  5.246   21.849  1.000 61.651  0 524 VAL EEE CG1 1 ? 22 
ATOM   5965 C CG2 . VAL E 2 195 ? 26.925  3.669   19.930  1.000 64.019  0 524 VAL EEE CG2 1 ? 22 
ATOM   5966 N N   . CYS E 2 196 ? 30.947  5.881   21.583  1.000 66.388  0 525 CYS EEE N   1 ? 22 
ATOM   5967 C CA  . CYS E 2 196 ? 31.979  6.293   22.568  1.000 66.814  0 525 CYS EEE CA  1 ? 22 
ATOM   5968 C C   . CYS E 2 196 ? 31.591  7.637   23.189  1.000 67.544  0 525 CYS EEE C   1 ? 22 
ATOM   5969 O O   . CYS E 2 196 ? 30.897  8.424   22.516  1.000 67.419  0 525 CYS EEE O   1 ? 22 
ATOM   5970 C CB  . CYS E 2 196 ? 33.351  6.374   21.910  1.000 68.858  0 525 CYS EEE CB  1 ? 22 
ATOM   5971 S SG  . CYS E 2 196 ? 33.969  4.760   21.367  1.000 69.154  0 525 CYS EEE SG  1 ? 22 
ATOM   5972 N N   . GLY E 2 197 ? 32.015  7.867   24.434  1.000 68.306  0 526 GLY EEE N   1 ? 22 
ATOM   5973 C CA  . GLY E 2 197 ? 31.896  9.170   25.113  1.000 69.922  0 526 GLY EEE CA  1 ? 22 
ATOM   5974 C C   . GLY E 2 197 ? 32.892  10.167  24.530  1.000 73.272  0 526 GLY EEE C   1 ? 22 
ATOM   5975 O O   . GLY E 2 197 ? 33.819  9.766   23.831  1.000 73.509  0 526 GLY EEE O   1 ? 22 
ATOM   5976 N N   . PRO E 2 198 ? 32.747  11.484  24.809  1.000 77.318  0 527 PRO EEE N   1 ? 22 
ATOM   5977 C CA  . PRO E 2 198 ? 33.610  12.496  24.196  1.000 84.072  0 527 PRO EEE CA  1 ? 22 
ATOM   5978 C C   . PRO E 2 198 ? 35.099  12.352  24.560  1.000 88.487  0 527 PRO EEE C   1 ? 22 
ATOM   5979 O O   . PRO E 2 198 ? 35.916  12.859  23.811  1.000 93.123  0 527 PRO EEE O   1 ? 22 
ATOM   5980 C CB  . PRO E 2 198 ? 33.043  13.830  24.708  1.000 85.180  0 527 PRO EEE CB  1 ? 22 
ATOM   5981 C CG  . PRO E 2 198 ? 32.299  13.466  25.973  1.000 81.419  0 527 PRO EEE CG  1 ? 22 
ATOM   5982 C CD  . PRO E 2 198 ? 31.767  12.065  25.740  1.000 77.011  0 527 PRO EEE CD  1 ? 22 
ATOM   5983 N N   . LYS E 2 199 ? 35.408  11.668  25.671  1.000 90.185  0 528 LYS EEE N   1 ? 22 
ATOM   5984 C CA  . LYS E 2 199 ? 36.791  11.437  26.179  1.000 94.353  0 528 LYS EEE CA  1 ? 22 
ATOM   5985 C C   . LYS E 2 199 ? 37.388  10.159  25.569  1.000 93.342  0 528 LYS EEE C   1 ? 22 
ATOM   5986 O O   . LYS E 2 199 ? 38.547  9.840   25.910  1.000 95.703  0 528 LYS EEE O   1 ? 22 
ATOM   5987 C CB  . LYS E 2 199 ? 36.811  11.313  27.709  1.000 95.808  0 528 LYS EEE CB  1 ? 22 
ATOM   5988 C CG  . LYS E 2 199 ? 35.990  12.327  28.499  1.000 99.016  0 528 LYS EEE CG  1 ? 22 
ATOM   5989 C CD  . LYS E 2 199 ? 36.160  13.757  28.039  1.000 105.568 0 528 LYS EEE CD  1 ? 22 
ATOM   5990 C CE  . LYS E 2 199 ? 35.444  14.742  28.937  1.000 108.954 0 528 LYS EEE CE  1 ? 22 
ATOM   5991 N NZ  . LYS E 2 199 ? 35.630  16.138  28.476  1.000 114.353 0 528 LYS EEE NZ  1 ? 22 
ATOM   5992 N N   . LYS E 2 200 ? 36.627  9.443   24.730  1.000 91.749  0 529 LYS EEE N   1 ? 22 
ATOM   5993 C CA  . LYS E 2 200 ? 37.048  8.180   24.063  1.000 90.642  0 529 LYS EEE CA  1 ? 22 
ATOM   5994 C C   . LYS E 2 200 ? 37.416  7.143   25.131  1.000 87.361  0 529 LYS EEE C   1 ? 22 
ATOM   5995 O O   . LYS E 2 200 ? 37.444  5.932   24.865  1.000 84.187  0 529 LYS EEE O   1 ? 22 
ATOM   5996 C CB  . LYS E 2 200 ? 38.219  8.439   23.108  1.000 95.199  0 529 LYS EEE CB  1 ? 22 
ATOM   5997 C CG  . LYS E 2 200 ? 37.948  9.464   22.014  1.000 99.108  0 529 LYS EEE CG  1 ? 22 
ATOM   5998 C CD  . LYS E 2 200 ? 39.173  9.807   21.198  1.000 103.058 0 529 LYS EEE CD  1 ? 22 
ATOM   5999 C CE  . LYS E 2 200 ? 38.876  10.725  20.032  1.000 106.941 0 529 LYS EEE CE  1 ? 22 
ATOM   6000 N NZ  . LYS E 2 200 ? 40.091  10.977  19.221  1.000 111.085 0 529 LYS EEE NZ  1 ? 22 
ATOM   6001 N N   . GLN F 3 3   ? -12.789 17.083  12.888  1.000 90.211  0 3   GLN FFF N   1 ? 23 
ATOM   6002 C CA  . GLN F 3 3   ? -14.133 17.514  12.392  1.000 90.345  0 3   GLN FFF CA  1 ? 23 
ATOM   6003 C C   . GLN F 3 3   ? -14.597 16.558  11.282  1.000 86.012  0 3   GLN FFF C   1 ? 23 
ATOM   6004 O O   . GLN F 3 3   ? -15.298 17.022  10.358  1.000 89.517  0 3   GLN FFF O   1 ? 23 
ATOM   6005 C CB  . GLN F 3 3   ? -14.082 18.966  11.898  1.000 96.552  0 3   GLN FFF CB  1 ? 23 
ATOM   6006 C CG  . GLN F 3 3   ? -14.081 20.010  13.010  1.000 101.578 0 3   GLN FFF CG  1 ? 23 
ATOM   6007 C CD  . GLN F 3 3   ? -12.698 20.330  13.529  1.000 104.071 0 3   GLN FFF CD  1 ? 23 
ATOM   6008 O OE1 . GLN F 3 3   ? -12.080 19.539  14.239  1.000 100.490 0 3   GLN FFF OE1 1 ? 23 
ATOM   6009 N NE2 . GLN F 3 3   ? -12.201 21.508  13.187  1.000 109.100 0 3   GLN FFF NE2 1 ? 23 
ATOM   6010 N N   . VAL F 3 4   ? -14.236 15.270  11.370  1.000 79.015  0 4   VAL FFF N   1 ? 23 
ATOM   6011 C CA  . VAL F 3 4   ? -14.614 14.240  10.357  1.000 73.551  0 4   VAL FFF CA  1 ? 23 
ATOM   6012 C C   . VAL F 3 4   ? -16.117 13.960  10.482  1.000 71.253  0 4   VAL FFF C   1 ? 23 
ATOM   6013 O O   . VAL F 3 4   ? -16.626 13.872  11.623  1.000 70.159  0 4   VAL FFF O   1 ? 23 
ATOM   6014 C CB  . VAL F 3 4   ? -13.794 12.941  10.485  1.000 69.641  0 4   VAL FFF CB  1 ? 23 
ATOM   6015 C CG1 . VAL F 3 4   ? -14.056 12.224  11.802  1.000 67.297  0 4   VAL FFF CG1 1 ? 23 
ATOM   6016 C CG2 . VAL F 3 4   ? -14.059 12.011  9.311   1.000 69.701  0 4   VAL FFF CG2 1 ? 23 
ATOM   6017 N N   . GLN F 3 5   ? -16.793 13.839  9.338   1.000 70.309  0 5   GLN FFF N   1 ? 23 
ATOM   6018 C CA  . GLN F 3 5   ? -18.249 13.564  9.239   1.000 67.108  0 5   GLN FFF CA  1 ? 23 
ATOM   6019 C C   . GLN F 3 5   ? -18.451 12.053  9.095   1.000 61.090  0 5   GLN FFF C   1 ? 23 
ATOM   6020 O O   . GLN F 3 5   ? -17.804 11.452  8.209   1.000 61.830  0 5   GLN FFF O   1 ? 23 
ATOM   6021 C CB  . GLN F 3 5   ? -18.843 14.317  8.047   1.000 71.262  0 5   GLN FFF CB  1 ? 23 
ATOM   6022 C CG  . GLN F 3 5   ? -20.365 14.281  7.985   1.000 73.223  0 5   GLN FFF CG  1 ? 23 
ATOM   6023 C CD  . GLN F 3 5   ? -21.023 15.299  8.885   1.000 76.200  0 5   GLN FFF CD  1 ? 23 
ATOM   6024 O OE1 . GLN F 3 5   ? -21.856 14.965  9.726   1.000 77.419  0 5   GLN FFF OE1 1 ? 23 
ATOM   6025 N NE2 . GLN F 3 5   ? -20.659 16.559  8.712   1.000 79.950  0 5   GLN FFF NE2 1 ? 23 
ATOM   6026 N N   . LEU F 3 6   ? -19.290 11.468  9.950   1.000 56.172  0 6   LEU FFF N   1 ? 23 
ATOM   6027 C CA  . LEU F 3 6   ? -19.825 10.093  9.767   1.000 52.857  0 6   LEU FFF CA  1 ? 23 
ATOM   6028 C C   . LEU F 3 6   ? -21.152 10.199  9.010   1.000 50.800  0 6   LEU FFF C   1 ? 23 
ATOM   6029 O O   . LEU F 3 6   ? -22.051 10.909  9.490   1.000 51.527  0 6   LEU FFF O   1 ? 23 
ATOM   6030 C CB  . LEU F 3 6   ? -20.004 9.399   11.119  1.000 52.613  0 6   LEU FFF CB  1 ? 23 
ATOM   6031 C CG  . LEU F 3 6   ? -18.867 8.477   11.558  1.000 54.245  0 6   LEU FFF CG  1 ? 23 
ATOM   6032 C CD1 . LEU F 3 6   ? -17.524 9.195   11.504  1.000 55.002  0 6   LEU FFF CD1 1 ? 23 
ATOM   6033 C CD2 . LEU F 3 6   ? -19.132 7.936   12.957  1.000 55.155  0 6   LEU FFF CD2 1 ? 23 
ATOM   6034 N N   . VAL F 3 7   ? -21.238 9.553   7.846   1.000 48.433  0 7   VAL FFF N   1 ? 23 
ATOM   6035 C CA  . VAL F 3 7   ? -22.458 9.536   6.994   1.000 47.516  0 7   VAL FFF CA  1 ? 23 
ATOM   6036 C C   . VAL F 3 7   ? -23.170 8.206   7.233   1.000 45.828  0 7   VAL FFF C   1 ? 23 
ATOM   6037 O O   . VAL F 3 7   ? -22.534 7.148   7.118   1.000 45.508  0 7   VAL FFF O   1 ? 23 
ATOM   6038 C CB  . VAL F 3 7   ? -22.127 9.777   5.511   1.000 49.118  0 7   VAL FFF CB  1 ? 23 
ATOM   6039 C CG1 . VAL F 3 7   ? -23.374 9.724   4.638   1.000 49.863  0 7   VAL FFF CG1 1 ? 23 
ATOM   6040 C CG2 . VAL F 3 7   ? -21.403 11.102  5.329   1.000 50.541  0 7   VAL FFF CG2 1 ? 23 
ATOM   6041 N N   . GLU F 3 8   ? -24.452 8.295   7.571   1.000 46.010  0 8   GLU FFF N   1 ? 23 
ATOM   6042 C CA  . GLU F 3 8   ? -25.304 7.171   8.026   1.000 46.746  0 8   GLU FFF CA  1 ? 23 
ATOM   6043 C C   . GLU F 3 8   ? -26.478 7.000   7.057   1.000 47.755  0 8   GLU FFF C   1 ? 23 
ATOM   6044 O O   . GLU F 3 8   ? -27.014 8.026   6.603   1.000 47.237  0 8   GLU FFF O   1 ? 23 
ATOM   6045 C CB  . GLU F 3 8   ? -25.766 7.516   9.438   1.000 47.161  0 8   GLU FFF CB  1 ? 23 
ATOM   6046 C CG  . GLU F 3 8   ? -26.355 6.358   10.194  1.000 48.514  0 8   GLU FFF CG  1 ? 23 
ATOM   6047 C CD  . GLU F 3 8   ? -26.735 6.714   11.619  1.000 50.553  0 8   GLU FFF CD  1 ? 23 
ATOM   6048 O OE1 . GLU F 3 8   ? -26.207 7.715   12.172  1.000 49.894  0 8   GLU FFF OE1 1 ? 23 
ATOM   6049 O OE2 . GLU F 3 8   ? -27.564 5.984   12.168  1.000 53.872  0 8   GLU FFF OE2 1 ? 23 
ATOM   6050 N N   . SER F 3 9   ? -26.858 5.760   6.749   1.000 45.135  0 9   SER FFF N   1 ? 24 
ATOM   6051 C CA  . SER F 3 9   ? -28.044 5.429   5.911   1.000 50.044  0 9   SER FFF CA  1 ? 24 
ATOM   6052 C C   . SER F 3 9   ? -28.597 4.055   6.304   1.000 49.767  0 9   SER FFF C   1 ? 24 
ATOM   6053 O O   . SER F 3 9   ? -27.988 3.397   7.173   1.000 47.768  0 9   SER FFF O   1 ? 24 
ATOM   6054 C CB  . SER F 3 9   ? -27.720 5.504   4.434   1.000 53.675  0 9   SER FFF CB  1 ? 24 
ATOM   6055 O OG  . SER F 3 9   ? -26.775 4.508   4.069   1.000 57.042  0 9   SER FFF OG  1 ? 24 
ATOM   6056 N N   . GLY F 3 10  ? -29.717 3.655   5.687   1.000 52.720  0 10  GLY FFF N   1 ? 24 
ATOM   6057 C CA  . GLY F 3 10  ? -30.511 2.462   6.041   1.000 53.951  0 10  GLY FFF CA  1 ? 24 
ATOM   6058 C C   . GLY F 3 10  ? -31.731 2.857   6.853   1.000 56.312  0 10  GLY FFF C   1 ? 24 
ATOM   6059 O O   . GLY F 3 10  ? -32.145 4.023   6.754   1.000 59.780  0 10  GLY FFF O   1 ? 24 
ATOM   6060 N N   . GLY F 3 11  ? -32.276 1.935   7.644   1.000 57.682  0 11  GLY FFF N   1 ? 24 
ATOM   6061 C CA  . GLY F 3 11  ? -33.460 2.190   8.490   1.000 61.430  0 11  GLY FFF CA  1 ? 24 
ATOM   6062 C C   . GLY F 3 11  ? -34.740 1.825   7.765   1.000 64.769  0 11  GLY FFF C   1 ? 24 
ATOM   6063 O O   . GLY F 3 11  ? -34.729 0.803   7.059   1.000 67.350  0 11  GLY FFF O   1 ? 24 
ATOM   6064 N N   . GLY F 3 12  ? -35.796 2.630   7.930   1.000 67.646  0 12  GLY FFF N   1 ? 24 
ATOM   6065 C CA  . GLY F 3 12  ? -37.120 2.408   7.316   1.000 70.561  0 12  GLY FFF CA  1 ? 24 
ATOM   6066 C C   . GLY F 3 12  ? -38.023 1.585   8.219   1.000 72.166  0 12  GLY FFF C   1 ? 24 
ATOM   6067 O O   . GLY F 3 12  ? -37.618 1.317   9.369   1.000 67.873  0 12  GLY FFF O   1 ? 24 
ATOM   6068 N N   . LEU F 3 13  ? -39.199 1.195   7.712   1.000 77.312  0 13  LEU FFF N   1 ? 24 
ATOM   6069 C CA  . LEU F 3 13  ? -40.222 0.401   8.448   1.000 79.039  0 13  LEU FFF CA  1 ? 24 
ATOM   6070 C C   . LEU F 3 13  ? -40.040 -1.082  8.104   1.000 78.047  0 13  LEU FFF C   1 ? 24 
ATOM   6071 O O   . LEU F 3 13  ? -39.725 -1.372  6.938   1.000 78.966  0 13  LEU FFF O   1 ? 24 
ATOM   6072 C CB  . LEU F 3 13  ? -41.629 0.872   8.062   1.000 86.399  0 13  LEU FFF CB  1 ? 24 
ATOM   6073 C CG  . LEU F 3 13  ? -41.831 2.376   7.856   1.000 89.906  0 13  LEU FFF CG  1 ? 24 
ATOM   6074 C CD1 . LEU F 3 13  ? -43.297 2.680   7.566   1.000 94.583  0 13  LEU FFF CD1 1 ? 24 
ATOM   6075 C CD2 . LEU F 3 13  ? -41.359 3.183   9.057   1.000 88.612  0 13  LEU FFF CD2 1 ? 24 
ATOM   6076 N N   . VAL F 3 14  ? -40.233 -1.977  9.080   1.000 78.454  0 14  VAL FFF N   1 ? 24 
ATOM   6077 C CA  . VAL F 3 14  ? -40.250 -3.460  8.876   1.000 80.652  0 14  VAL FFF CA  1 ? 24 
ATOM   6078 C C   . VAL F 3 14  ? -41.200 -4.106  9.896   1.000 83.957  0 14  VAL FFF C   1 ? 24 
ATOM   6079 O O   . VAL F 3 14  ? -41.442 -3.492  10.950  1.000 84.798  0 14  VAL FFF O   1 ? 24 
ATOM   6080 C CB  . VAL F 3 14  ? -38.833 -4.063  8.954   1.000 77.544  0 14  VAL FFF CB  1 ? 24 
ATOM   6081 C CG1 . VAL F 3 14  ? -38.265 -4.036  10.363  1.000 76.677  0 14  VAL FFF CG1 1 ? 24 
ATOM   6082 C CG2 . VAL F 3 14  ? -38.789 -5.473  8.386   1.000 78.402  0 14  VAL FFF CG2 1 ? 24 
ATOM   6083 N N   . LYS F 3 15  ? -41.732 -5.290  9.573   1.000 85.744  0 15  LYS FFF N   1 ? 24 
ATOM   6084 C CA  . LYS F 3 15  ? -42.611 -6.097  10.463  1.000 89.165  0 15  LYS FFF CA  1 ? 24 
ATOM   6085 C C   . LYS F 3 15  ? -41.772 -6.701  11.596  1.000 86.119  0 15  LYS FFF C   1 ? 24 
ATOM   6086 O O   . LYS F 3 15  ? -40.554 -6.865  11.396  1.000 86.034  0 15  LYS FFF O   1 ? 24 
ATOM   6087 C CB  . LYS F 3 15  ? -43.300 -7.211  9.667   1.000 93.677  0 15  LYS FFF CB  1 ? 24 
ATOM   6088 C CG  . LYS F 3 15  ? -44.239 -6.747  8.560   1.000 97.359  0 15  LYS FFF CG  1 ? 24 
ATOM   6089 C CD  . LYS F 3 15  ? -44.968 -7.887  7.878   1.000 101.140 0 15  LYS FFF CD  1 ? 24 
ATOM   6090 C CE  . LYS F 3 15  ? -45.930 -7.420  6.808   1.000 103.538 0 15  LYS FFF CE  1 ? 24 
ATOM   6091 N NZ  . LYS F 3 15  ? -46.501 -8.561  6.054   1.000 106.832 0 15  LYS FFF NZ  1 ? 24 
ATOM   6092 N N   . THR F 3 16  ? -42.399 -7.021  12.733  1.000 86.132  0 16  THR FFF N   1 ? 24 
ATOM   6093 C CA  . THR F 3 16  ? -41.780 -7.761  13.868  1.000 84.455  0 16  THR FFF CA  1 ? 24 
ATOM   6094 C C   . THR F 3 16  ? -41.206 -9.083  13.344  1.000 83.021  0 16  THR FFF C   1 ? 24 
ATOM   6095 O O   . THR F 3 16  ? -41.932 -9.788  12.622  1.000 87.164  0 16  THR FFF O   1 ? 24 
ATOM   6096 C CB  . THR F 3 16  ? -42.791 -8.011  14.995  1.000 88.384  0 16  THR FFF CB  1 ? 24 
ATOM   6097 O OG1 . THR F 3 16  ? -43.284 -6.748  15.443  1.000 89.749  0 16  THR FFF OG1 1 ? 24 
ATOM   6098 C CG2 . THR F 3 16  ? -42.201 -8.770  16.164  1.000 87.631  0 16  THR FFF CG2 1 ? 24 
ATOM   6099 N N   . GLY F 3 17  ? -39.951 -9.392  13.687  1.000 78.725  0 17  GLY FFF N   1 ? 24 
ATOM   6100 C CA  . GLY F 3 17  ? -39.222 -10.587 13.218  1.000 77.436  0 17  GLY FFF CA  1 ? 24 
ATOM   6101 C C   . GLY F 3 17  ? -38.442 -10.326 11.936  1.000 74.420  0 17  GLY FFF C   1 ? 24 
ATOM   6102 O O   . GLY F 3 17  ? -37.685 -11.219 11.522  1.000 73.384  0 17  GLY FFF O   1 ? 24 
ATOM   6103 N N   . GLY F 3 18  ? -38.614 -9.149  11.327  1.000 73.006  0 18  GLY FFF N   1 ? 24 
ATOM   6104 C CA  . GLY F 3 18  ? -37.985 -8.766  10.048  1.000 72.163  0 18  GLY FFF CA  1 ? 24 
ATOM   6105 C C   . GLY F 3 18  ? -36.551 -8.306  10.243  1.000 68.898  0 18  GLY FFF C   1 ? 24 
ATOM   6106 O O   . GLY F 3 18  ? -36.072 -8.325  11.396  1.000 68.065  0 18  GLY FFF O   1 ? 24 
ATOM   6107 N N   . SER F 3 19  ? -35.890 -7.904  9.153   1.000 67.872  0 19  SER FFF N   1 ? 24 
ATOM   6108 C CA  . SER F 3 19  ? -34.441 -7.573  9.106   1.000 64.262  0 19  SER FFF CA  1 ? 24 
ATOM   6109 C C   . SER F 3 19  ? -34.218 -6.194  8.476   1.000 62.532  0 19  SER FFF C   1 ? 24 
ATOM   6110 O O   . SER F 3 19  ? -34.984 -5.823  7.568   1.000 64.419  0 19  SER FFF O   1 ? 24 
ATOM   6111 C CB  . SER F 3 19  ? -33.674 -8.634  8.366   1.000 64.828  0 19  SER FFF CB  1 ? 24 
ATOM   6112 O OG  . SER F 3 19  ? -33.379 -9.726  9.222   1.000 65.368  0 19  SER FFF OG  1 ? 24 
ATOM   6113 N N   . LEU F 3 20  ? -33.191 -5.481  8.948   1.000 59.947  0 20  LEU FFF N   1 ? 24 
ATOM   6114 C CA  . LEU F 3 20  ? -32.714 -4.188  8.386   1.000 58.785  0 20  LEU FFF CA  1 ? 24 
ATOM   6115 C C   . LEU F 3 20  ? -31.184 -4.126  8.473   1.000 55.452  0 20  LEU FFF C   1 ? 24 
ATOM   6116 O O   . LEU F 3 20  ? -30.602 -4.912  9.241   1.000 52.908  0 20  LEU FFF O   1 ? 24 
ATOM   6117 C CB  . LEU F 3 20  ? -33.351 -3.038  9.170   1.000 59.241  0 20  LEU FFF CB  1 ? 24 
ATOM   6118 C CG  . LEU F 3 20  ? -34.811 -2.735  8.845   1.000 63.987  0 20  LEU FFF CG  1 ? 24 
ATOM   6119 C CD1 . LEU F 3 20  ? -35.350 -1.668  9.784   1.000 65.313  0 20  LEU FFF CD1 1 ? 24 
ATOM   6120 C CD2 . LEU F 3 20  ? -34.976 -2.305  7.394   1.000 65.633  0 20  LEU FFF CD2 1 ? 24 
ATOM   6121 N N   . ARG F 3 21  ? -30.577 -3.211  7.713   1.000 55.691  0 21  ARG FFF N   1 ? 24 
ATOM   6122 C CA  . ARG F 3 21  ? -29.108 -3.009  7.614   1.000 54.496  0 21  ARG FFF CA  1 ? 24 
ATOM   6123 C C   . ARG F 3 21  ? -28.830 -1.503  7.593   1.000 54.724  0 21  ARG FFF C   1 ? 24 
ATOM   6124 O O   . ARG F 3 21  ? -28.999 -0.887  6.530   1.000 60.346  0 21  ARG FFF O   1 ? 24 
ATOM   6125 C CB  . ARG F 3 21  ? -28.560 -3.707  6.364   1.000 55.982  0 21  ARG FFF CB  1 ? 24 
ATOM   6126 C CG  . ARG F 3 21  ? -27.061 -3.554  6.126   1.000 55.224  0 21  ARG FFF CG  1 ? 24 
ATOM   6127 C CD  . ARG F 3 21  ? -26.667 -4.308  4.865   1.000 58.999  0 21  ARG FFF CD  1 ? 24 
ATOM   6128 N NE  . ARG F 3 21  ? -25.774 -3.629  3.928   1.000 61.250  0 21  ARG FFF NE  1 ? 24 
ATOM   6129 C CZ  . ARG F 3 21  ? -26.004 -2.449  3.343   1.000 62.233  0 21  ARG FFF CZ  1 ? 24 
ATOM   6130 N NH1 . ARG F 3 21  ? -27.091 -1.747  3.621   1.000 66.039  0 21  ARG FFF NH1 1 ? 24 
ATOM   6131 N NH2 . ARG F 3 21  ? -25.124 -1.953  2.493   1.000 61.595  0 21  ARG FFF NH2 1 ? 24 
ATOM   6132 N N   . LEU F 3 22  ? -28.435 -0.936  8.734   1.000 53.500  0 22  LEU FFF N   1 ? 24 
ATOM   6133 C CA  . LEU F 3 22  ? -27.923 0.456   8.830   1.000 52.022  0 22  LEU FFF CA  1 ? 24 
ATOM   6134 C C   . LEU F 3 22  ? -26.501 0.470   8.265   1.000 50.904  0 22  LEU FFF C   1 ? 24 
ATOM   6135 O O   . LEU F 3 22  ? -25.841 -0.583  8.321   1.000 49.175  0 22  LEU FFF O   1 ? 24 
ATOM   6136 C CB  . LEU F 3 22  ? -27.952 0.933   10.287  1.000 51.787  0 22  LEU FFF CB  1 ? 24 
ATOM   6137 C CG  . LEU F 3 22  ? -29.286 1.490   10.787  1.000 53.968  0 22  LEU FFF CG  1 ? 24 
ATOM   6138 C CD1 . LEU F 3 22  ? -30.449 0.632   10.325  1.000 56.223  0 22  LEU FFF CD1 1 ? 24 
ATOM   6139 C CD2 . LEU F 3 22  ? -29.295 1.614   12.303  1.000 53.895  0 22  LEU FFF CD2 1 ? 24 
ATOM   6140 N N   . SER F 3 23  ? -26.073 1.613   7.725   1.000 50.108  0 23  SER FFF N   1 ? 24 
ATOM   6141 C CA  . SER F 3 23  ? -24.715 1.860   7.182   1.000 48.384  0 23  SER FFF CA  1 ? 24 
ATOM   6142 C C   . SER F 3 23  ? -24.123 3.100   7.853   1.000 46.777  0 23  SER FFF C   1 ? 24 
ATOM   6143 O O   . SER F 3 23  ? -24.883 4.059   8.085   1.000 44.928  0 23  SER FFF O   1 ? 24 
ATOM   6144 C CB  . SER F 3 23  ? -24.747 2.017   5.692   1.000 50.603  0 23  SER FFF CB  1 ? 24 
ATOM   6145 O OG  . SER F 3 23  ? -24.669 0.752   5.062   1.000 54.847  0 23  SER FFF OG  1 ? 24 
ATOM   6146 N N   . CYS F 3 24  ? -22.820 3.058   8.152   1.000 46.985  0 24  CYS FFF N   1 ? 24 
ATOM   6147 C CA  . CYS F 3 24  ? -22.011 4.193   8.672   1.000 46.071  0 24  CYS FFF CA  1 ? 24 
ATOM   6148 C C   . CYS F 3 24  ? -20.678 4.238   7.916   1.000 43.717  0 24  CYS FFF C   1 ? 24 
ATOM   6149 O O   . CYS F 3 24  ? -19.943 3.239   7.939   1.000 41.187  0 24  CYS FFF O   1 ? 24 
ATOM   6150 C CB  . CYS F 3 24  ? -21.760 4.076   10.170  1.000 44.865  0 24  CYS FFF CB  1 ? 24 
ATOM   6151 S SG  . CYS F 3 24  ? -21.137 5.606   10.919  1.000 49.284  0 24  CYS FFF SG  1 ? 24 
ATOM   6152 N N   . ALA F 3 25  ? -20.396 5.366   7.270   1.000 43.651  0 25  ALA FFF N   1 ? 24 
ATOM   6153 C CA  . ALA F 3 25  ? -19.204 5.576   6.426   1.000 44.779  0 25  ALA FFF CA  1 ? 24 
ATOM   6154 C C   . ALA F 3 25  ? -18.391 6.747   6.983   1.000 44.292  0 25  ALA FFF C   1 ? 24 
ATOM   6155 O O   . ALA F 3 25  ? -18.996 7.725   7.462   1.000 43.961  0 25  ALA FFF O   1 ? 24 
ATOM   6156 C CB  . ALA F 3 25  ? -19.623 5.802   4.993   1.000 46.244  0 25  ALA FFF CB  1 ? 24 
ATOM   6157 N N   . ALA F 3 26  ? -17.065 6.617   6.922   1.000 44.060  0 26  ALA FFF N   1 ? 24 
ATOM   6158 C CA  . ALA F 3 26  ? -16.071 7.618   7.369   1.000 45.725  0 26  ALA FFF CA  1 ? 24 
ATOM   6159 C C   . ALA F 3 26  ? -14.812 7.448   6.516   1.000 46.259  0 26  ALA FFF C   1 ? 24 
ATOM   6160 O O   . ALA F 3 26  ? -14.440 6.286   6.252   1.000 46.117  0 26  ALA FFF O   1 ? 24 
ATOM   6161 C CB  . ALA F 3 26  ? -15.781 7.429   8.839   1.000 44.706  0 26  ALA FFF CB  1 ? 24 
ATOM   6162 N N   . SER F 3 27  ? -14.192 8.551   6.088   1.000 46.931  0 27  SER FFF N   1 ? 24 
ATOM   6163 C CA  . SER F 3 27  ? -13.119 8.538   5.061   1.000 49.915  0 27  SER FFF CA  1 ? 24 
ATOM   6164 C C   . SER F 3 27  ? -11.878 7.826   5.609   1.000 48.183  0 27  SER FFF C   1 ? 24 
ATOM   6165 O O   . SER F 3 27  ? -11.580 8.000   6.803   1.000 44.864  0 27  SER FFF O   1 ? 24 
ATOM   6166 C CB  . SER F 3 27  ? -12.790 9.925   4.573   1.000 52.845  0 27  SER FFF CB  1 ? 24 
ATOM   6167 O OG  . SER F 3 27  ? -12.126 10.673  5.578   1.000 54.215  0 27  SER FFF OG  1 ? 24 
ATOM   6168 N N   . GLY F 3 28  ? -11.227 7.028   4.758   1.000 48.697  0 28  GLY FFF N   1 ? 24 
ATOM   6169 C CA  . GLY F 3 28  ? -9.881  6.463   4.966   1.000 49.713  0 28  GLY FFF CA  1 ? 24 
ATOM   6170 C C   . GLY F 3 28  ? -9.756  5.667   6.254   1.000 48.126  0 28  GLY FFF C   1 ? 24 
ATOM   6171 O O   . GLY F 3 28  ? -10.596 4.780   6.485   1.000 43.402  0 28  GLY FFF O   1 ? 24 
ATOM   6172 N N   . ARG F 3 29  ? -8.751  6.015   7.067   1.000 49.195  0 29  ARG FFF N   1 ? 24 
ATOM   6173 C CA  . ARG F 3 29  ? -8.225  5.197   8.188   1.000 50.213  0 29  ARG FFF CA  1 ? 24 
ATOM   6174 C C   . ARG F 3 29  ? -9.027  5.456   9.475   1.000 46.575  0 29  ARG FFF C   1 ? 24 
ATOM   6175 O O   . ARG F 3 29  ? -8.640  4.897   10.515  1.000 46.638  0 29  ARG FFF O   1 ? 24 
ATOM   6176 C CB  . ARG F 3 29  ? -6.730  5.499   8.359   1.000 54.623  0 29  ARG FFF CB  1 ? 24 
ATOM   6177 C CG  . ARG F 3 29  ? -5.899  5.230   7.111   1.000 61.315  0 29  ARG FFF CG  1 ? 24 
ATOM   6178 C CD  . ARG F 3 29  ? -4.482  5.775   7.170   1.000 67.349  0 29  ARG FFF CD  1 ? 24 
ATOM   6179 N NE  . ARG F 3 29  ? -3.776  5.634   5.893   1.000 76.171  0 29  ARG FFF NE  1 ? 24 
ATOM   6180 C CZ  . ARG F 3 29  ? -3.878  6.464   4.847   1.000 80.041  0 29  ARG FFF CZ  1 ? 24 
ATOM   6181 N NH1 . ARG F 3 29  ? -4.666  7.528   4.897   1.000 80.217  0 29  ARG FFF NH1 1 ? 24 
ATOM   6182 N NH2 . ARG F 3 29  ? -3.186  6.228   3.742   1.000 84.163  0 29  ARG FFF NH2 1 ? 24 
ATOM   6183 N N   . THR F 3 30  ? -10.105 6.247   9.420   1.000 44.295  0 30  THR FFF N   1 ? 24 
ATOM   6184 C CA  . THR F 3 30  ? -10.934 6.634   10.596  1.000 42.236  0 30  THR FFF CA  1 ? 24 
ATOM   6185 C C   . THR F 3 30  ? -11.316 5.386   11.399  1.000 40.910  0 30  THR FFF C   1 ? 24 
ATOM   6186 O O   . THR F 3 30  ? -10.923 5.312   12.584  1.000 38.901  0 30  THR FFF O   1 ? 24 
ATOM   6187 C CB  . THR F 3 30  ? -12.182 7.426   10.182  1.000 41.917  0 30  THR FFF CB  1 ? 24 
ATOM   6188 O OG1 . THR F 3 30  ? -11.751 8.635   9.560   1.000 43.397  0 30  THR FFF OG1 1 ? 24 
ATOM   6189 C CG2 . THR F 3 30  ? -13.087 7.768   11.345  1.000 40.356  0 30  THR FFF CG2 1 ? 24 
ATOM   6190 N N   . PHE F 3 31  ? -12.045 4.448   10.786  1.000 39.848  0 31  PHE FFF N   1 ? 24 
ATOM   6191 C CA  . PHE F 3 31  ? -12.575 3.230   11.456  1.000 39.547  0 31  PHE FFF CA  1 ? 24 
ATOM   6192 C C   . PHE F 3 31  ? -11.424 2.281   11.813  1.000 40.052  0 31  PHE FFF C   1 ? 24 
ATOM   6193 O O   . PHE F 3 31  ? -11.609 1.458   12.724  1.000 39.487  0 31  PHE FFF O   1 ? 24 
ATOM   6194 C CB  . PHE F 3 31  ? -13.621 2.525   10.589  1.000 38.716  0 31  PHE FFF CB  1 ? 24 
ATOM   6195 C CG  . PHE F 3 31  ? -14.966 3.204   10.524  1.000 39.777  0 31  PHE FFF CG  1 ? 24 
ATOM   6196 C CD1 . PHE F 3 31  ? -15.546 3.747   11.664  1.000 39.363  0 31  PHE FFF CD1 1 ? 24 
ATOM   6197 C CD2 . PHE F 3 31  ? -15.681 3.258   9.330   1.000 40.226  0 31  PHE FFF CD2 1 ? 24 
ATOM   6198 C CE1 . PHE F 3 31  ? -16.794 4.353   11.606  1.000 38.699  0 31  PHE FFF CE1 1 ? 24 
ATOM   6199 C CE2 . PHE F 3 31  ? -16.927 3.864   9.275   1.000 39.972  0 31  PHE FFF CE2 1 ? 24 
ATOM   6200 C CZ  . PHE F 3 31  ? -17.481 4.407   10.414  1.000 39.583  0 31  PHE FFF CZ  1 ? 24 
ATOM   6201 N N   . SER F 3 32  ? -10.282 2.402   11.128  1.000 41.473  0 32  SER FFF N   1 ? 24 
ATOM   6202 C CA  . SER F 3 32  ? -9.034  1.634   11.394  1.000 43.205  0 32  SER FFF CA  1 ? 24 
ATOM   6203 C C   . SER F 3 32  ? -8.260  2.232   12.578  1.000 41.839  0 32  SER FFF C   1 ? 24 
ATOM   6204 O O   . SER F 3 32  ? -7.326  1.572   13.044  1.000 41.776  0 32  SER FFF O   1 ? 24 
ATOM   6205 C CB  . SER F 3 32  ? -8.160  1.564   10.164  1.000 45.148  0 32  SER FFF CB  1 ? 24 
ATOM   6206 O OG  . SER F 3 32  ? -8.649  0.595   9.257   1.000 48.037  0 32  SER FFF OG  1 ? 24 
ATOM   6207 N N   . THR F 3 33  ? -8.626  3.435   13.028  1.000 40.925  0 33  THR FFF N   1 ? 24 
ATOM   6208 C CA  . THR F 3 33  ? -7.931  4.196   14.098  1.000 41.586  0 33  THR FFF CA  1 ? 24 
ATOM   6209 C C   . THR F 3 33  ? -8.798  4.294   15.359  1.000 42.042  0 33  THR FFF C   1 ? 24 
ATOM   6210 O O   . THR F 3 33  ? -8.222  4.263   16.465  1.000 42.584  0 33  THR FFF O   1 ? 24 
ATOM   6211 C CB  . THR F 3 33  ? -7.574  5.606   13.623  1.000 42.506  0 33  THR FFF CB  1 ? 24 
ATOM   6212 O OG1 . THR F 3 33  ? -6.890  5.479   12.377  1.000 42.996  0 33  THR FFF OG1 1 ? 24 
ATOM   6213 C CG2 . THR F 3 33  ? -6.724  6.357   14.625  1.000 43.493  0 33  THR FFF CG2 1 ? 24 
ATOM   6214 N N   . TYR F 3 34  ? -10.117 4.447   15.205  1.000 40.085  0 34  TYR FFF N   1 ? 24 
ATOM   6215 C CA  . TYR F 3 34  ? -11.061 4.714   16.318  1.000 40.499  0 34  TYR FFF CA  1 ? 24 
ATOM   6216 C C   . TYR F 3 34  ? -12.198 3.693   16.279  1.000 40.961  0 34  TYR FFF C   1 ? 24 
ATOM   6217 O O   . TYR F 3 34  ? -12.895 3.589   15.236  1.000 39.961  0 34  TYR FFF O   1 ? 24 
ATOM   6218 C CB  . TYR F 3 34  ? -11.608 6.140   16.230  1.000 41.137  0 34  TYR FFF CB  1 ? 24 
ATOM   6219 C CG  . TYR F 3 34  ? -10.544 7.207   16.150  1.000 42.787  0 34  TYR FFF CG  1 ? 24 
ATOM   6220 C CD1 . TYR F 3 34  ? -9.660  7.414   17.199  1.000 43.933  0 34  TYR FFF CD1 1 ? 24 
ATOM   6221 C CD2 . TYR F 3 34  ? -10.422 8.012   15.030  1.000 43.040  0 34  TYR FFF CD2 1 ? 24 
ATOM   6222 C CE1 . TYR F 3 34  ? -8.679  8.389   17.134  1.000 46.060  0 34  TYR FFF CE1 1 ? 24 
ATOM   6223 C CE2 . TYR F 3 34  ? -9.449  8.995   14.950  1.000 44.931  0 34  TYR FFF CE2 1 ? 24 
ATOM   6224 C CZ  . TYR F 3 34  ? -8.572  9.181   16.004  1.000 47.499  0 34  TYR FFF CZ  1 ? 24 
ATOM   6225 O OH  . TYR F 3 34  ? -7.604  10.139  15.926  1.000 51.142  0 34  TYR FFF OH  1 ? 24 
ATOM   6226 N N   . SER F 3 35  ? -12.385 2.970   17.388  1.000 40.666  0 35  SER FFF N   1 ? 24 
ATOM   6227 C CA  . SER F 3 35  ? -13.543 2.067   17.604  1.000 41.581  0 35  SER FFF CA  1 ? 24 
ATOM   6228 C C   . SER F 3 35  ? -14.841 2.851   17.365  1.000 40.796  0 35  SER FFF C   1 ? 24 
ATOM   6229 O O   . SER F 3 35  ? -14.903 4.045   17.734  1.000 41.062  0 35  SER FFF O   1 ? 24 
ATOM   6230 C CB  . SER F 3 35  ? -13.507 1.444   18.966  1.000 41.939  0 35  SER FFF CB  1 ? 24 
ATOM   6231 O OG  . SER F 3 35  ? -12.377 0.597   19.096  1.000 44.024  0 35  SER FFF OG  1 ? 24 
ATOM   6232 N N   . MET F 3 36  ? -15.824 2.210   16.736  1.000 38.687  0 36  MET FFF N   1 ? 24 
ATOM   6233 C CA  . MET F 3 36  ? -17.126 2.842   16.408  1.000 39.678  0 36  MET FFF CA  1 ? 24 
ATOM   6234 C C   . MET F 3 36  ? -18.220 2.201   17.268  1.000 38.618  0 36  MET FFF C   1 ? 24 
ATOM   6235 O O   . MET F 3 36  ? -18.051 1.033   17.697  1.000 37.099  0 36  MET FFF O   1 ? 24 
ATOM   6236 C CB  . MET F 3 36  ? -17.455 2.700   14.917  1.000 38.643  0 36  MET FFF CB  1 ? 24 
ATOM   6237 C CG  . MET F 3 36  ? -17.847 1.300   14.475  1.000 39.909  0 36  MET FFF CG  1 ? 24 
ATOM   6238 S SD  . MET F 3 36  ? -19.569 0.867   14.859  1.000 45.236  0 36  MET FFF SD  1 ? 24 
ATOM   6239 C CE  . MET F 3 36  ? -20.426 2.303   14.213  1.000 46.677  0 36  MET FFF CE  1 ? 24 
ATOM   6240 N N   . GLY F 3 37  ? -19.288 2.958   17.514  1.000 38.645  0 37  GLY FFF N   1 ? 24 
ATOM   6241 C CA  . GLY F 3 37  ? -20.450 2.516   18.304  1.000 40.824  0 37  GLY FFF CA  1 ? 24 
ATOM   6242 C C   . GLY F 3 37  ? -21.755 2.872   17.614  1.000 40.377  0 37  GLY FFF C   1 ? 24 
ATOM   6243 O O   . GLY F 3 37  ? -21.856 3.984   17.068  1.000 40.009  0 37  GLY FFF O   1 ? 24 
ATOM   6244 N N   . TRP F 3 38  ? -22.709 1.942   17.616  1.000 40.655  0 38  TRP FFF N   1 ? 24 
ATOM   6245 C CA  . TRP F 3 38  ? -24.129 2.205   17.279  1.000 42.574  0 38  TRP FFF CA  1 ? 24 
ATOM   6246 C C   . TRP F 3 38  ? -24.885 2.505   18.577  1.000 43.326  0 38  TRP FFF C   1 ? 24 
ATOM   6247 O O   . TRP F 3 38  ? -24.751 1.727   19.536  1.000 44.225  0 38  TRP FFF O   1 ? 24 
ATOM   6248 C CB  . TRP F 3 38  ? -24.734 1.022   16.518  1.000 44.335  0 38  TRP FFF CB  1 ? 24 
ATOM   6249 C CG  . TRP F 3 38  ? -24.177 0.835   15.140  1.000 43.553  0 38  TRP FFF CG  1 ? 24 
ATOM   6250 C CD1 . TRP F 3 38  ? -23.214 -0.048  14.747  1.000 44.222  0 38  TRP FFF CD1 1 ? 24 
ATOM   6251 C CD2 . TRP F 3 38  ? -24.566 1.551   13.959  1.000 44.464  0 38  TRP FFF CD2 1 ? 24 
ATOM   6252 N NE1 . TRP F 3 38  ? -22.970 0.073   13.406  1.000 45.044  0 38  TRP FFF NE1 1 ? 24 
ATOM   6253 C CE2 . TRP F 3 38  ? -23.785 1.048   12.894  1.000 46.026  0 38  TRP FFF CE2 1 ? 24 
ATOM   6254 C CE3 . TRP F 3 38  ? -25.487 2.573   13.702  1.000 45.886  0 38  TRP FFF CE3 1 ? 24 
ATOM   6255 C CZ2 . TRP F 3 38  ? -23.914 1.524   11.590  1.000 46.448  0 38  TRP FFF CZ2 1 ? 24 
ATOM   6256 C CZ3 . TRP F 3 38  ? -25.612 3.041   12.414  1.000 47.140  0 38  TRP FFF CZ3 1 ? 24 
ATOM   6257 C CH2 . TRP F 3 38  ? -24.839 2.521   11.374  1.000 46.493  0 38  TRP FFF CH2 1 ? 24 
ATOM   6258 N N   . PHE F 3 39  ? -25.615 3.619   18.602  1.000 44.267  0 39  PHE FFF N   1 ? 24 
ATOM   6259 C CA  . PHE F 3 39  ? -26.534 4.031   19.692  1.000 46.349  0 39  PHE FFF CA  1 ? 24 
ATOM   6260 C C   . PHE F 3 39  ? -27.940 4.187   19.114  1.000 48.316  0 39  PHE FFF C   1 ? 24 
ATOM   6261 O O   . PHE F 3 39  ? -28.087 4.287   17.873  1.000 47.779  0 39  PHE FFF O   1 ? 24 
ATOM   6262 C CB  . PHE F 3 39  ? -26.063 5.339   20.329  1.000 47.327  0 39  PHE FFF CB  1 ? 24 
ATOM   6263 C CG  . PHE F 3 39  ? -24.754 5.222   21.065  1.000 47.949  0 39  PHE FFF CG  1 ? 24 
ATOM   6264 C CD1 . PHE F 3 39  ? -23.554 5.177   20.372  1.000 45.991  0 39  PHE FFF CD1 1 ? 24 
ATOM   6265 C CD2 . PHE F 3 39  ? -24.726 5.133   22.449  1.000 49.987  0 39  PHE FFF CD2 1 ? 24 
ATOM   6266 C CE1 . PHE F 3 39  ? -22.353 5.063   21.054  1.000 46.970  0 39  PHE FFF CE1 1 ? 24 
ATOM   6267 C CE2 . PHE F 3 39  ? -23.524 5.019   23.129  1.000 50.623  0 39  PHE FFF CE2 1 ? 24 
ATOM   6268 C CZ  . PHE F 3 39  ? -22.339 4.973   22.428  1.000 48.344  0 39  PHE FFF CZ  1 ? 24 
ATOM   6269 N N   . ARG F 3 40  ? -28.944 4.196   19.990  1.000 51.023  0 40  ARG FFF N   1 ? 24 
ATOM   6270 C CA  . ARG F 3 40  ? -30.359 4.432   19.614  1.000 53.588  0 40  ARG FFF CA  1 ? 24 
ATOM   6271 C C   . ARG F 3 40  ? -31.012 5.302   20.686  1.000 55.917  0 40  ARG FFF C   1 ? 24 
ATOM   6272 O O   . ARG F 3 40  ? -30.598 5.206   21.857  1.000 55.938  0 40  ARG FFF O   1 ? 24 
ATOM   6273 C CB  . ARG F 3 40  ? -31.089 3.102   19.404  1.000 54.590  0 40  ARG FFF CB  1 ? 24 
ATOM   6274 C CG  . ARG F 3 40  ? -31.323 2.292   20.671  1.000 56.558  0 40  ARG FFF CG  1 ? 24 
ATOM   6275 C CD  . ARG F 3 40  ? -31.852 0.921   20.295  1.000 57.792  0 40  ARG FFF CD  1 ? 24 
ATOM   6276 N NE  . ARG F 3 40  ? -32.060 0.028   21.427  1.000 59.281  0 40  ARG FFF NE  1 ? 24 
ATOM   6277 C CZ  . ARG F 3 40  ? -32.464 -1.237  21.324  1.000 61.012  0 40  ARG FFF CZ  1 ? 24 
ATOM   6278 N NH1 . ARG F 3 40  ? -32.705 -1.773  20.137  1.000 60.338  0 40  ARG FFF NH1 1 ? 24 
ATOM   6279 N NH2 . ARG F 3 40  ? -32.622 -1.966  22.414  1.000 63.368  0 40  ARG FFF NH2 1 ? 24 
ATOM   6280 N N   . GLN F 3 41  ? -31.974 6.127   20.272  1.000 59.530  0 41  GLN FFF N   1 ? 24 
ATOM   6281 C CA  . GLN F 3 41  ? -32.753 7.038   21.148  1.000 63.718  0 41  GLN FFF CA  1 ? 24 
ATOM   6282 C C   . GLN F 3 41  ? -34.231 6.939   20.760  1.000 67.575  0 41  GLN FFF C   1 ? 24 
ATOM   6283 O O   . GLN F 3 41  ? -34.578 7.345   19.635  1.000 68.545  0 41  GLN FFF O   1 ? 24 
ATOM   6284 C CB  . GLN F 3 41  ? -32.223 8.465   21.016  1.000 64.353  0 41  GLN FFF CB  1 ? 24 
ATOM   6285 C CG  . GLN F 3 41  ? -32.805 9.430   22.037  1.000 67.902  0 41  GLN FFF CG  1 ? 24 
ATOM   6286 C CD  . GLN F 3 41  ? -31.974 10.681  22.202  1.000 67.980  0 41  GLN FFF CD  1 ? 24 
ATOM   6287 O OE1 . GLN F 3 41  ? -30.868 10.806  21.686  1.000 65.659  0 41  GLN FFF OE1 1 ? 24 
ATOM   6288 N NE2 . GLN F 3 41  ? -32.504 11.628  22.955  1.000 73.118  0 41  GLN FFF NE2 1 ? 24 
ATOM   6289 N N   . ALA F 3 42  ? -35.051 6.376   21.650  1.000 71.437  0 42  ALA FFF N   1 ? 24 
ATOM   6290 C CA  . ALA F 3 42  ? -36.526 6.338   21.539  1.000 75.615  0 42  ALA FFF CA  1 ? 24 
ATOM   6291 C C   . ALA F 3 42  ? -37.090 7.646   22.090  1.000 79.882  0 42  ALA FFF C   1 ? 24 
ATOM   6292 O O   . ALA F 3 42  ? -36.446 8.299   22.913  1.000 78.606  0 42  ALA FFF O   1 ? 24 
ATOM   6293 C CB  . ALA F 3 42  ? -37.068 5.136   22.274  1.000 77.752  0 42  ALA FFF CB  1 ? 24 
ATOM   6294 N N   . PRO F 3 43  ? -38.316 8.054   21.677  1.000 83.109  0 43  PRO FFF N   1 ? 24 
ATOM   6295 C CA  . PRO F 3 43  ? -38.900 9.321   22.118  1.000 87.267  0 43  PRO FFF CA  1 ? 24 
ATOM   6296 C C   . PRO F 3 43  ? -38.836 9.484   23.647  1.000 89.930  0 43  PRO FFF C   1 ? 24 
ATOM   6297 O O   . PRO F 3 43  ? -39.355 8.630   24.343  1.000 88.465  0 43  PRO FFF O   1 ? 24 
ATOM   6298 C CB  . PRO F 3 43  ? -40.356 9.256   21.624  1.000 90.844  0 43  PRO FFF CB  1 ? 24 
ATOM   6299 C CG  . PRO F 3 43  ? -40.587 7.804   21.240  1.000 88.498  0 43  PRO FFF CG  1 ? 24 
ATOM   6300 C CD  . PRO F 3 43  ? -39.227 7.303   20.799  1.000 83.146  0 43  PRO FFF CD  1 ? 24 
ATOM   6301 N N   . GLY F 3 44  ? -38.160 10.540  24.113  1.000 92.133  0 44  GLY FFF N   1 ? 24 
ATOM   6302 C CA  . GLY F 3 44  ? -38.046 10.916  25.536  1.000 97.031  0 44  GLY FFF CA  1 ? 24 
ATOM   6303 C C   . GLY F 3 44  ? -37.275 9.894   26.355  1.000 96.443  0 44  GLY FFF C   1 ? 24 
ATOM   6304 O O   . GLY F 3 44  ? -37.806 9.457   27.390  1.000 100.437 0 44  GLY FFF O   1 ? 24 
ATOM   6305 N N   . LYS F 3 45  ? -36.064 9.542   25.910  1.000 92.998  0 45  LYS FFF N   1 ? 24 
ATOM   6306 C CA  . LYS F 3 45  ? -35.137 8.604   26.600  1.000 91.706  0 45  LYS FFF CA  1 ? 24 
ATOM   6307 C C   . LYS F 3 45  ? -33.686 9.007   26.314  1.000 90.382  0 45  LYS FFF C   1 ? 24 
ATOM   6308 O O   . LYS F 3 45  ? -33.471 9.884   25.456  1.000 89.398  0 45  LYS FFF O   1 ? 24 
ATOM   6309 C CB  . LYS F 3 45  ? -35.380 7.165   26.141  1.000 89.837  0 45  LYS FFF CB  1 ? 24 
ATOM   6310 C CG  . LYS F 3 45  ? -36.584 6.474   26.764  1.000 94.844  0 45  LYS FFF CG  1 ? 24 
ATOM   6311 C CD  . LYS F 3 45  ? -36.702 5.012   26.388  1.000 93.922  0 45  LYS FFF CD  1 ? 24 
ATOM   6312 C CE  . LYS F 3 45  ? -35.595 4.152   26.964  1.000 92.921  0 45  LYS FFF CE  1 ? 24 
ATOM   6313 N NZ  . LYS F 3 45  ? -35.506 2.841   26.279  1.000 90.763  0 45  LYS FFF NZ  1 ? 24 
ATOM   6314 N N   . GLU F 3 46  ? -32.732 8.377   27.004  1.000 92.201  0 46  GLU FFF N   1 ? 24 
ATOM   6315 C CA  . GLU F 3 46  ? -31.274 8.612   26.827  1.000 92.991  0 46  GLU FFF CA  1 ? 24 
ATOM   6316 C C   . GLU F 3 46  ? -30.781 7.821   25.608  1.000 84.559  0 46  GLU FFF C   1 ? 24 
ATOM   6317 O O   . GLU F 3 46  ? -31.417 6.812   25.254  1.000 82.524  0 46  GLU FFF O   1 ? 24 
ATOM   6318 C CB  . GLU F 3 46  ? -30.524 8.225   28.105  1.000 101.512 0 46  GLU FFF CB  1 ? 24 
ATOM   6319 C CG  . GLU F 3 46  ? -29.066 8.661   28.124  1.000 106.805 0 46  GLU FFF CG  1 ? 24 
ATOM   6320 C CD  . GLU F 3 46  ? -28.841 10.163  28.045  1.000 112.108 0 46  GLU FFF CD  1 ? 24 
ATOM   6321 O OE1 . GLU F 3 46  ? -29.226 10.876  29.002  1.000 116.999 0 46  GLU FFF OE1 1 ? 24 
ATOM   6322 O OE2 . GLU F 3 46  ? -28.290 10.618  27.022  1.000 109.513 0 46  GLU FFF OE2 1 ? 24 
ATOM   6323 N N   . ARG F 3 47  ? -29.692 8.278   24.987  1.000 73.504  0 47  ARG FFF N   1 ? 25 
ATOM   6324 C CA  . ARG F 3 47  ? -28.959 7.538   23.924  1.000 70.909  0 47  ARG FFF CA  1 ? 25 
ATOM   6325 C C   . ARG F 3 47  ? -28.294 6.309   24.551  1.000 66.462  0 47  ARG FFF C   1 ? 25 
ATOM   6326 O O   . ARG F 3 47  ? -27.231 6.478   25.190  1.000 65.119  0 47  ARG FFF O   1 ? 25 
ATOM   6327 C CB  . ARG F 3 47  ? -27.901 8.426   23.255  1.000 72.293  0 47  ARG FFF CB  1 ? 25 
ATOM   6328 C CG  . ARG F 3 47  ? -28.179 8.714   21.791  1.000 73.094  0 47  ARG FFF CG  1 ? 25 
ATOM   6329 C CD  . ARG F 3 47  ? -27.209 9.726   21.215  1.000 74.400  0 47  ARG FFF CD  1 ? 25 
ATOM   6330 N NE  . ARG F 3 47  ? -27.929 10.802  20.552  1.000 79.720  0 47  ARG FFF NE  1 ? 25 
ATOM   6331 C CZ  . ARG F 3 47  ? -27.369 11.769  19.838  1.000 84.026  0 47  ARG FFF CZ  1 ? 25 
ATOM   6332 N NH1 . ARG F 3 47  ? -26.054 11.812  19.694  1.000 84.916  0 47  ARG FFF NH1 1 ? 25 
ATOM   6333 N NH2 . ARG F 3 47  ? -28.128 12.699  19.285  1.000 89.481  0 47  ARG FFF NH2 1 ? 25 
ATOM   6334 N N   . GLU F 3 48  ? -28.902 5.128   24.397  1.000 62.921  0 48  GLU FFF N   1 ? 25 
ATOM   6335 C CA  . GLU F 3 48  ? -28.348 3.854   24.935  1.000 59.985  0 48  GLU FFF CA  1 ? 25 
ATOM   6336 C C   . GLU F 3 48  ? -27.482 3.180   23.862  1.000 56.637  0 48  GLU FFF C   1 ? 25 
ATOM   6337 O O   . GLU F 3 48  ? -27.839 3.246   22.663  1.000 54.014  0 48  GLU FFF O   1 ? 25 
ATOM   6338 C CB  . GLU F 3 48  ? -29.460 2.940   25.454  1.000 61.668  0 48  GLU FFF CB  1 ? 25 
ATOM   6339 C CG  . GLU F 3 48  ? -30.388 2.399   24.381  1.000 62.282  0 48  GLU FFF CG  1 ? 25 
ATOM   6340 C CD  . GLU F 3 48  ? -31.452 1.456   24.906  1.000 64.037  0 48  GLU FFF CD  1 ? 25 
ATOM   6341 O OE1 . GLU F 3 48  ? -31.857 1.626   26.073  1.000 71.547  0 48  GLU FFF OE1 1 ? 25 
ATOM   6342 O OE2 . GLU F 3 48  ? -31.867 0.552   24.152  1.000 63.748  0 48  GLU FFF OE2 1 ? 25 
ATOM   6343 N N   . PHE F 3 49  ? -26.368 2.579   24.291  1.000 52.135  0 49  PHE FFF N   1 ? 25 
ATOM   6344 C CA  . PHE F 3 49  ? -25.437 1.798   23.441  1.000 48.985  0 49  PHE FFF CA  1 ? 25 
ATOM   6345 C C   . PHE F 3 49  ? -26.174 0.574   22.877  1.000 48.803  0 49  PHE FFF C   1 ? 25 
ATOM   6346 O O   . PHE F 3 49  ? -26.945 -0.050  23.617  1.000 47.550  0 49  PHE FFF O   1 ? 25 
ATOM   6347 C CB  . PHE F 3 49  ? -24.196 1.370   24.231  1.000 46.188  0 49  PHE FFF CB  1 ? 25 
ATOM   6348 C CG  . PHE F 3 49  ? -23.284 0.472   23.441  1.000 44.100  0 49  PHE FFF CG  1 ? 25 
ATOM   6349 C CD1 . PHE F 3 49  ? -22.496 0.994   22.427  1.000 42.890  0 49  PHE FFF CD1 1 ? 25 
ATOM   6350 C CD2 . PHE F 3 49  ? -23.260 -0.895  23.665  1.000 43.622  0 49  PHE FFF CD2 1 ? 25 
ATOM   6351 C CE1 . PHE F 3 49  ? -21.679 0.169   21.669  1.000 42.383  0 49  PHE FFF CE1 1 ? 25 
ATOM   6352 C CE2 . PHE F 3 49  ? -22.440 -1.719  22.908  1.000 44.425  0 49  PHE FFF CE2 1 ? 25 
ATOM   6353 C CZ  . PHE F 3 49  ? -21.653 -1.185  21.909  1.000 43.044  0 49  PHE FFF CZ  1 ? 25 
ATOM   6354 N N   . VAL F 3 50  ? -25.916 0.235   21.609  1.000 48.676  0 50  VAL FFF N   1 ? 25 
ATOM   6355 C CA  . VAL F 3 50  ? -26.538 -0.921  20.898  1.000 49.544  0 50  VAL FFF CA  1 ? 25 
ATOM   6356 C C   . VAL F 3 50  ? -25.449 -1.954  20.592  1.000 47.977  0 50  VAL FFF C   1 ? 25 
ATOM   6357 O O   . VAL F 3 50  ? -25.518 -3.074  21.122  1.000 49.973  0 50  VAL FFF O   1 ? 25 
ATOM   6358 C CB  . VAL F 3 50  ? -27.254 -0.466  19.612  1.000 49.882  0 50  VAL FFF CB  1 ? 25 
ATOM   6359 C CG1 . VAL F 3 50  ? -27.777 -1.647  18.797  1.000 49.838  0 50  VAL FFF CG1 1 ? 25 
ATOM   6360 C CG2 . VAL F 3 50  ? -28.363 0.527   19.928  1.000 51.658  0 50  VAL FFF CG2 1 ? 25 
ATOM   6361 N N   . ALA F 3 51  ? -24.490 -1.581  19.750  1.000 46.453  0 51  ALA FFF N   1 ? 25 
ATOM   6362 C CA  . ALA F 3 51  ? -23.443 -2.478  19.217  1.000 44.953  0 51  ALA FFF CA  1 ? 25 
ATOM   6363 C C   . ALA F 3 51  ? -22.279 -1.629  18.714  1.000 44.751  0 51  ALA FFF C   1 ? 25 
ATOM   6364 O O   . ALA F 3 51  ? -22.502 -0.448  18.391  1.000 48.525  0 51  ALA FFF O   1 ? 25 
ATOM   6365 C CB  . ALA F 3 51  ? -24.012 -3.344  18.119  1.000 44.538  0 51  ALA FFF CB  1 ? 25 
ATOM   6366 N N   . GLY F 3 52  ? -21.088 -2.216  18.651  1.000 42.406  0 52  GLY FFF N   1 ? 25 
ATOM   6367 C CA  . GLY F 3 52  ? -19.866 -1.519  18.222  1.000 40.354  0 52  GLY FFF CA  1 ? 25 
ATOM   6368 C C   . GLY F 3 52  ? -18.857 -2.468  17.615  1.000 38.921  0 52  GLY FFF C   1 ? 25 
ATOM   6369 O O   . GLY F 3 52  ? -19.056 -3.698  17.686  1.000 38.671  0 52  GLY FFF O   1 ? 25 
ATOM   6370 N N   . MET F 3 53  ? -17.800 -1.899  17.048  1.000 38.703  0 53  MET FFF N   1 ? 25 
ATOM   6371 C CA  . MET F 3 53  ? -16.648 -2.643  16.486  1.000 40.203  0 53  MET FFF CA  1 ? 25 
ATOM   6372 C C   . MET F 3 53  ? -15.356 -1.908  16.861  1.000 39.640  0 53  MET FFF C   1 ? 25 
ATOM   6373 O O   . MET F 3 53  ? -15.311 -0.665  16.723  1.000 37.108  0 53  MET FFF O   1 ? 25 
ATOM   6374 C CB  . MET F 3 53  ? -16.762 -2.758  14.964  1.000 40.097  0 53  MET FFF CB  1 ? 25 
ATOM   6375 C CG  . MET F 3 53  ? -15.668 -3.598  14.343  1.000 41.607  0 53  MET FFF CG  1 ? 25 
ATOM   6376 S SD  . MET F 3 53  ? -15.774 -3.653  12.540  1.000 42.190  0 53  MET FFF SD  1 ? 25 
ATOM   6377 C CE  . MET F 3 53  ? -16.677 -5.185  12.313  1.000 42.348  0 53  MET FFF CE  1 ? 25 
ATOM   6378 N N   . ARG F 3 54  ? -14.357 -2.654  17.342  1.000 39.866  0 54  ARG FFF N   1 ? 25 
ATOM   6379 C CA  . ARG F 3 54  ? -12.988 -2.138  17.609  1.000 40.159  0 54  ARG FFF CA  1 ? 25 
ATOM   6380 C C   . ARG F 3 54  ? -12.350 -1.766  16.268  1.000 39.044  0 54  ARG FFF C   1 ? 25 
ATOM   6381 O O   . ARG F 3 54  ? -12.715 -2.378  15.239  1.000 37.738  0 54  ARG FFF O   1 ? 25 
ATOM   6382 C CB  . ARG F 3 54  ? -12.129 -3.177  18.340  1.000 41.581  0 54  ARG FFF CB  1 ? 25 
ATOM   6383 C CG  . ARG F 3 54  ? -12.678 -3.622  19.689  1.000 41.324  0 54  ARG FFF CG  1 ? 25 
ATOM   6384 C CD  . ARG F 3 54  ? -12.702 -2.513  20.722  1.000 41.021  0 54  ARG FFF CD  1 ? 25 
ATOM   6385 N NE  . ARG F 3 54  ? -13.215 -3.001  21.995  1.000 41.052  0 54  ARG FFF NE  1 ? 25 
ATOM   6386 C CZ  . ARG F 3 54  ? -13.180 -2.329  23.145  1.000 42.876  0 54  ARG FFF CZ  1 ? 25 
ATOM   6387 N NH1 . ARG F 3 54  ? -12.650 -1.117  23.212  1.000 42.256  0 54  ARG FFF NH1 1 ? 25 
ATOM   6388 N NH2 . ARG F 3 54  ? -13.675 -2.883  24.237  1.000 44.429  0 54  ARG FFF NH2 1 ? 25 
ATOM   6389 N N   . TRP F 3 55  ? -11.419 -0.812  16.286  1.000 38.781  0 55  TRP FFF N   1 ? 25 
ATOM   6390 C CA  . TRP F 3 55  ? -10.686 -0.328  15.085  1.000 40.130  0 55  TRP FFF CA  1 ? 25 
ATOM   6391 C C   . TRP F 3 55  ? -10.023 -1.496  14.344  1.000 39.840  0 55  TRP FFF C   1 ? 25 
ATOM   6392 O O   . TRP F 3 55  ? -9.717  -1.332  13.158  1.000 41.481  0 55  TRP FFF O   1 ? 25 
ATOM   6393 C CB  . TRP F 3 55  ? -9.654  0.726   15.490  1.000 41.208  0 55  TRP FFF CB  1 ? 25 
ATOM   6394 C CG  . TRP F 3 55  ? -8.440  0.160   16.160  1.000 41.283  0 55  TRP FFF CG  1 ? 25 
ATOM   6395 C CD1 . TRP F 3 55  ? -7.399  -0.491  15.563  1.000 41.972  0 55  TRP FFF CD1 1 ? 25 
ATOM   6396 C CD2 . TRP F 3 55  ? -8.137  0.199   17.565  1.000 40.754  0 55  TRP FFF CD2 1 ? 25 
ATOM   6397 N NE1 . TRP F 3 55  ? -6.474  -0.866  16.502  1.000 43.159  0 55  TRP FFF NE1 1 ? 25 
ATOM   6398 C CE2 . TRP F 3 55  ? -6.894  -0.449  17.736  1.000 41.412  0 55  TRP FFF CE2 1 ? 25 
ATOM   6399 C CE3 . TRP F 3 55  ? -8.787  0.720   18.690  1.000 39.891  0 55  TRP FFF CE3 1 ? 25 
ATOM   6400 C CZ2 . TRP F 3 55  ? -6.294  -0.589  18.986  1.000 42.108  0 55  TRP FFF CZ2 1 ? 25 
ATOM   6401 C CZ3 . TRP F 3 55  ? -8.196  0.577   19.926  1.000 40.507  0 55  TRP FFF CZ3 1 ? 25 
ATOM   6402 C CH2 . TRP F 3 55  ? -6.967  -0.071  20.069  1.000 41.856  0 55  TRP FFF CH2 1 ? 25 
ATOM   6403 N N   . THR F 3 56  ? -9.791  -2.615  15.034  1.000 40.459  0 56  THR FFF N   1 ? 25 
ATOM   6404 C CA  . THR F 3 56  ? -9.094  -3.822  14.520  1.000 41.215  0 56  THR FFF CA  1 ? 25 
ATOM   6405 C C   . THR F 3 56  ? -9.923  -4.517  13.431  1.000 41.689  0 56  THR FFF C   1 ? 25 
ATOM   6406 O O   . THR F 3 56  ? -9.320  -5.184  12.580  1.000 40.885  0 56  THR FFF O   1 ? 25 
ATOM   6407 C CB  . THR F 3 56  ? -8.821  -4.814  15.657  1.000 41.490  0 56  THR FFF CB  1 ? 25 
ATOM   6408 O OG1 . THR F 3 56  ? -10.087 -5.181  16.208  1.000 40.366  0 56  THR FFF OG1 1 ? 25 
ATOM   6409 C CG2 . THR F 3 56  ? -7.918  -4.249  16.732  1.000 41.388  0 56  THR FFF CG2 1 ? 25 
ATOM   6410 N N   . GLY F 3 57  ? -11.253 -4.413  13.498  1.000 43.975  0 57  GLY FFF N   1 ? 25 
ATOM   6411 C CA  . GLY F 3 57  ? -12.190 -5.152  12.630  1.000 44.125  0 57  GLY FFF CA  1 ? 25 
ATOM   6412 C C   . GLY F 3 57  ? -12.409 -6.590  13.090  1.000 45.855  0 57  GLY FFF C   1 ? 25 
ATOM   6413 O O   . GLY F 3 57  ? -13.290 -7.255  12.508  1.000 48.194  0 57  GLY FFF O   1 ? 25 
ATOM   6414 N N   . SER F 3 58  ? -11.661 -7.062  14.098  1.000 44.871  0 58  SER FFF N   1 ? 25 
ATOM   6415 C CA  . SER F 3 58  ? -11.619 -8.484  14.536  1.000 45.942  0 58  SER FFF CA  1 ? 25 
ATOM   6416 C C   . SER F 3 58  ? -12.362 -8.664  15.870  1.000 45.295  0 58  SER FFF C   1 ? 25 
ATOM   6417 O O   . SER F 3 58  ? -12.309 -9.771  16.444  1.000 45.419  0 58  SER FFF O   1 ? 25 
ATOM   6418 C CB  . SER F 3 58  ? -10.195 -8.968  14.632  1.000 47.104  0 58  SER FFF CB  1 ? 25 
ATOM   6419 O OG  . SER F 3 58  ? -9.479  -8.249  15.626  1.000 50.364  0 58  SER FFF OG  1 ? 25 
ATOM   6420 N N   . SER F 3 59  ? -13.025 -7.611  16.347  1.000 43.196  0 59  SER FFF N   1 ? 25 
ATOM   6421 C CA  . SER F 3 59  ? -13.771 -7.595  17.628  1.000 43.856  0 59  SER FFF CA  1 ? 25 
ATOM   6422 C C   . SER F 3 59  ? -15.020 -6.722  17.479  1.000 43.297  0 59  SER FFF C   1 ? 25 
ATOM   6423 O O   . SER F 3 59  ? -14.892 -5.546  17.069  1.000 42.692  0 59  SER FFF O   1 ? 25 
ATOM   6424 C CB  . SER F 3 59  ? -12.898 -7.128  18.761  1.000 43.837  0 59  SER FFF CB  1 ? 25 
ATOM   6425 O OG  . SER F 3 59  ? -13.624 -7.105  19.979  1.000 45.535  0 59  SER FFF OG  1 ? 25 
ATOM   6426 N N   . THR F 3 60  ? -16.184 -7.302  17.770  1.000 43.649  0 60  THR FFF N   1 ? 25 
ATOM   6427 C CA  . THR F 3 60  ? -17.488 -6.602  17.883  1.000 44.334  0 60  THR FFF CA  1 ? 25 
ATOM   6428 C C   . THR F 3 60  ? -18.054 -6.873  19.280  1.000 46.743  0 60  THR FFF C   1 ? 25 
ATOM   6429 O O   . THR F 3 60  ? -17.619 -7.857  19.922  1.000 47.897  0 60  THR FFF O   1 ? 25 
ATOM   6430 C CB  . THR F 3 60  ? -18.442 -7.028  16.763  1.000 43.580  0 60  THR FFF CB  1 ? 25 
ATOM   6431 O OG1 . THR F 3 60  ? -18.674 -8.435  16.856  1.000 44.086  0 60  THR FFF OG1 1 ? 25 
ATOM   6432 C CG2 . THR F 3 60  ? -17.898 -6.698  15.393  1.000 43.261  0 60  THR FFF CG2 1 ? 25 
ATOM   6433 N N   . PHE F 3 61  ? -18.965 -6.017  19.740  1.000 45.688  0 61  PHE FFF N   1 ? 25 
ATOM   6434 C CA  . PHE F 3 61  ? -19.561 -6.075  21.096  1.000 45.041  0 61  PHE FFF CA  1 ? 25 
ATOM   6435 C C   . PHE F 3 61  ? -20.971 -5.494  21.019  1.000 45.673  0 61  PHE FFF C   1 ? 25 
ATOM   6436 O O   . PHE F 3 61  ? -21.211 -4.614  20.186  1.000 45.701  0 61  PHE FFF O   1 ? 25 
ATOM   6437 C CB  . PHE F 3 61  ? -18.657 -5.364  22.105  1.000 44.174  0 61  PHE FFF CB  1 ? 25 
ATOM   6438 C CG  . PHE F 3 61  ? -18.078 -4.051  21.644  1.000 43.481  0 61  PHE FFF CG  1 ? 25 
ATOM   6439 C CD1 . PHE F 3 61  ? -16.890 -4.013  20.934  1.000 44.272  0 61  PHE FFF CD1 1 ? 25 
ATOM   6440 C CD2 . PHE F 3 61  ? -18.706 -2.851  21.938  1.000 43.327  0 61  PHE FFF CD2 1 ? 25 
ATOM   6441 C CE1 . PHE F 3 61  ? -16.356 -2.802  20.518  1.000 42.777  0 61  PHE FFF CE1 1 ? 25 
ATOM   6442 C CE2 . PHE F 3 61  ? -18.170 -1.642  21.519  1.000 42.860  0 61  PHE FFF CE2 1 ? 25 
ATOM   6443 C CZ  . PHE F 3 61  ? -16.997 -1.620  20.804  1.000 42.164  0 61  PHE FFF CZ  1 ? 25 
ATOM   6444 N N   . TYR F 3 62  ? -21.869 -6.002  21.862  1.000 47.782  0 62  TYR FFF N   1 ? 25 
ATOM   6445 C CA  . TYR F 3 62  ? -23.340 -5.824  21.762  1.000 48.002  0 62  TYR FFF CA  1 ? 25 
ATOM   6446 C C   . TYR F 3 62  ? -23.915 -5.618  23.162  1.000 49.255  0 62  TYR FFF C   1 ? 25 
ATOM   6447 O O   . TYR F 3 62  ? -23.433 -6.280  24.093  1.000 50.108  0 62  TYR FFF O   1 ? 25 
ATOM   6448 C CB  . TYR F 3 62  ? -23.948 -7.039  21.055  1.000 49.109  0 62  TYR FFF CB  1 ? 25 
ATOM   6449 C CG  . TYR F 3 62  ? -23.286 -7.354  19.737  1.000 48.233  0 62  TYR FFF CG  1 ? 25 
ATOM   6450 C CD1 . TYR F 3 62  ? -23.704 -6.749  18.564  1.000 48.374  0 62  TYR FFF CD1 1 ? 25 
ATOM   6451 C CD2 . TYR F 3 62  ? -22.189 -8.198  19.676  1.000 48.244  0 62  TYR FFF CD2 1 ? 25 
ATOM   6452 C CE1 . TYR F 3 62  ? -23.073 -7.002  17.357  1.000 48.129  0 62  TYR FFF CE1 1 ? 25 
ATOM   6453 C CE2 . TYR F 3 62  ? -21.550 -8.467  18.478  1.000 48.798  0 62  TYR FFF CE2 1 ? 25 
ATOM   6454 C CZ  . TYR F 3 62  ? -21.989 -7.859  17.314  1.000 47.725  0 62  TYR FFF CZ  1 ? 25 
ATOM   6455 O OH  . TYR F 3 62  ? -21.379 -8.101  16.118  1.000 45.684  0 62  TYR FFF OH  1 ? 25 
ATOM   6456 N N   . SER F 3 63  ? -24.901 -4.729  23.295  1.000 50.744  0 63  SER FFF N   1 ? 25 
ATOM   6457 C CA  . SER F 3 63  ? -25.688 -4.531  24.539  1.000 53.633  0 63  SER FFF CA  1 ? 25 
ATOM   6458 C C   . SER F 3 63  ? -26.424 -5.835  24.854  1.000 54.379  0 63  SER FFF C   1 ? 25 
ATOM   6459 O O   . SER F 3 63  ? -26.668 -6.616  23.910  1.000 55.992  0 63  SER FFF O   1 ? 25 
ATOM   6460 C CB  . SER F 3 63  ? -26.640 -3.368  24.422  1.000 54.652  0 63  SER FFF CB  1 ? 25 
ATOM   6461 O OG  . SER F 3 63  ? -27.731 -3.683  23.572  1.000 58.454  0 63  SER FFF OG  1 ? 25 
ATOM   6462 N N   . ASP F 3 64  ? -26.750 -6.061  26.128  1.000 54.693  0 64  ASP FFF N   1 ? 25 
ATOM   6463 C CA  . ASP F 3 64  ? -27.430 -7.292  26.613  1.000 56.298  0 64  ASP FFF CA  1 ? 25 
ATOM   6464 C C   . ASP F 3 64  ? -28.703 -7.525  25.783  1.000 56.031  0 64  ASP FFF C   1 ? 25 
ATOM   6465 O O   . ASP F 3 64  ? -29.059 -8.695  25.573  1.000 58.224  0 64  ASP FFF O   1 ? 25 
ATOM   6466 C CB  . ASP F 3 64  ? -27.740 -7.210  28.114  1.000 57.960  0 64  ASP FFF CB  1 ? 25 
ATOM   6467 C CG  . ASP F 3 64  ? -26.538 -7.262  29.053  1.000 57.986  0 64  ASP FFF CG  1 ? 25 
ATOM   6468 O OD1 . ASP F 3 64  ? -25.405 -7.374  28.565  1.000 56.044  0 64  ASP FFF OD1 1 ? 25 
ATOM   6469 O OD2 . ASP F 3 64  ? -26.751 -7.191  30.284  1.000 62.878  0 64  ASP FFF OD2 1 ? 25 
ATOM   6470 N N   . SER F 3 65  ? -29.351 -6.459  25.301  1.000 54.590  0 65  SER FFF N   1 ? 25 
ATOM   6471 C CA  . SER F 3 65  ? -30.703 -6.500  24.687  1.000 56.501  0 65  SER FFF CA  1 ? 25 
ATOM   6472 C C   . SER F 3 65  ? -30.664 -6.802  23.180  1.000 54.231  0 65  SER FFF C   1 ? 25 
ATOM   6473 O O   . SER F 3 65  ? -31.757 -6.984  22.618  1.000 54.354  0 65  SER FFF O   1 ? 25 
ATOM   6474 C CB  . SER F 3 65  ? -31.441 -5.216  24.959  1.000 58.192  0 65  SER FFF CB  1 ? 25 
ATOM   6475 O OG  . SER F 3 65  ? -30.832 -4.134  24.277  1.000 60.181  0 65  SER FFF OG  1 ? 25 
ATOM   6476 N N   . VAL F 3 66  ? -29.493 -6.848  22.532  1.000 52.131  0 66  VAL FFF N   1 ? 25 
ATOM   6477 C CA  . VAL F 3 66  ? -29.393 -7.137  21.061  1.000 52.178  0 66  VAL FFF CA  1 ? 25 
ATOM   6478 C C   . VAL F 3 66  ? -28.392 -8.265  20.764  1.000 52.823  0 66  VAL FFF C   1 ? 25 
ATOM   6479 O O   . VAL F 3 66  ? -28.452 -8.807  19.642  1.000 57.121  0 66  VAL FFF O   1 ? 25 
ATOM   6480 C CB  . VAL F 3 66  ? -29.050 -5.881  20.236  1.000 49.852  0 66  VAL FFF CB  1 ? 25 
ATOM   6481 C CG1 . VAL F 3 66  ? -30.071 -4.776  20.446  1.000 50.135  0 66  VAL FFF CG1 1 ? 25 
ATOM   6482 C CG2 . VAL F 3 66  ? -27.642 -5.373  20.511  1.000 48.539  0 66  VAL FFF CG2 1 ? 25 
ATOM   6483 N N   . LYS F 3 67  ? -27.489 -8.601  21.689  1.000 52.545  0 67  LYS FFF N   1 ? 25 
ATOM   6484 C CA  . LYS F 3 67  ? -26.496 -9.689  21.476  1.000 53.363  0 67  LYS FFF CA  1 ? 25 
ATOM   6485 C C   . LYS F 3 67  ? -27.239 -10.953 21.028  1.000 54.769  0 67  LYS FFF C   1 ? 25 
ATOM   6486 O O   . LYS F 3 67  ? -28.183 -11.353 21.722  1.000 57.714  0 67  LYS FFF O   1 ? 25 
ATOM   6487 C CB  . LYS F 3 67  ? -25.666 -9.959  22.735  1.000 54.559  0 67  LYS FFF CB  1 ? 25 
ATOM   6488 C CG  . LYS F 3 67  ? -24.468 -10.873 22.505  1.000 55.003  0 67  LYS FFF CG  1 ? 25 
ATOM   6489 C CD  . LYS F 3 67  ? -23.542 -11.008 23.699  1.000 56.220  0 67  LYS FFF CD  1 ? 25 
ATOM   6490 C CE  . LYS F 3 67  ? -22.173 -11.539 23.324  1.000 55.329  0 67  LYS FFF CE  1 ? 25 
ATOM   6491 N NZ  . LYS F 3 67  ? -21.521 -12.242 24.453  1.000 57.083  0 67  LYS FFF NZ  1 ? 25 
ATOM   6492 N N   . GLY F 3 68  ? -26.841 -11.532 19.892  1.000 55.054  0 68  GLY FFF N   1 ? 25 
ATOM   6493 C CA  . GLY F 3 68  ? -27.442 -12.758 19.331  1.000 57.222  0 68  GLY FFF CA  1 ? 25 
ATOM   6494 C C   . GLY F 3 68  ? -28.463 -12.458 18.247  1.000 58.566  0 68  GLY FFF C   1 ? 25 
ATOM   6495 O O   . GLY F 3 68  ? -28.825 -13.399 17.516  1.000 62.513  0 68  GLY FFF O   1 ? 25 
ATOM   6496 N N   . ARG F 3 69  ? -28.928 -11.207 18.154  1.000 57.076  0 69  ARG FFF N   1 ? 25 
ATOM   6497 C CA  . ARG F 3 69  ? -29.941 -10.749 17.166  1.000 57.850  0 69  ARG FFF CA  1 ? 25 
ATOM   6498 C C   . ARG F 3 69  ? -29.270 -9.816  16.150  1.000 56.974  0 69  ARG FFF C   1 ? 25 
ATOM   6499 O O   . ARG F 3 69  ? -29.562 -9.952  14.942  1.000 55.873  0 69  ARG FFF O   1 ? 25 
ATOM   6500 C CB  . ARG F 3 69  ? -31.114 -10.057 17.874  1.000 57.948  0 69  ARG FFF CB  1 ? 25 
ATOM   6501 C CG  . ARG F 3 69  ? -31.931 -10.982 18.766  1.000 59.947  0 69  ARG FFF CG  1 ? 25 
ATOM   6502 C CD  . ARG F 3 69  ? -33.230 -10.376 19.266  1.000 60.897  0 69  ARG FFF CD  1 ? 25 
ATOM   6503 N NE  . ARG F 3 69  ? -33.047 -9.100  19.953  1.000 58.315  0 69  ARG FFF NE  1 ? 25 
ATOM   6504 C CZ  . ARG F 3 69  ? -33.460 -7.909  19.512  1.000 57.001  0 69  ARG FFF CZ  1 ? 25 
ATOM   6505 N NH1 . ARG F 3 69  ? -34.103 -7.785  18.362  1.000 56.711  0 69  ARG FFF NH1 1 ? 25 
ATOM   6506 N NH2 . ARG F 3 69  ? -33.234 -6.832  20.243  1.000 55.998  0 69  ARG FFF NH2 1 ? 25 
ATOM   6507 N N   . PHE F 3 70  ? -28.428 -8.890  16.626  1.000 55.277  0 70  PHE FFF N   1 ? 25 
ATOM   6508 C CA  . PHE F 3 70  ? -27.697 -7.891  15.800  1.000 53.650  0 70  PHE FFF CA  1 ? 25 
ATOM   6509 C C   . PHE F 3 70  ? -26.241 -8.345  15.623  1.000 52.309  0 70  PHE FFF C   1 ? 25 
ATOM   6510 O O   . PHE F 3 70  ? -25.671 -8.939  16.565  1.000 50.817  0 70  PHE FFF O   1 ? 25 
ATOM   6511 C CB  . PHE F 3 70  ? -27.744 -6.501  16.448  1.000 52.812  0 70  PHE FFF CB  1 ? 25 
ATOM   6512 C CG  . PHE F 3 70  ? -29.092 -5.818  16.489  1.000 54.318  0 70  PHE FFF CG  1 ? 25 
ATOM   6513 C CD1 . PHE F 3 70  ? -30.262 -6.478  16.140  1.000 55.590  0 70  PHE FFF CD1 1 ? 25 
ATOM   6514 C CD2 . PHE F 3 70  ? -29.193 -4.506  16.930  1.000 53.847  0 70  PHE FFF CD2 1 ? 25 
ATOM   6515 C CE1 . PHE F 3 70  ? -31.490 -5.836  16.205  1.000 56.930  0 70  PHE FFF CE1 1 ? 25 
ATOM   6516 C CE2 . PHE F 3 70  ? -30.422 -3.867  16.996  1.000 54.590  0 70  PHE FFF CE2 1 ? 25 
ATOM   6517 C CZ  . PHE F 3 70  ? -31.569 -4.533  16.634  1.000 56.439  0 70  PHE FFF CZ  1 ? 25 
ATOM   6518 N N   . THR F 3 71  ? -25.668 -8.083  14.444  1.000 50.403  0 71  THR FFF N   1 ? 25 
ATOM   6519 C CA  . THR F 3 71  ? -24.228 -8.289  14.133  1.000 48.538  0 71  THR FFF CA  1 ? 25 
ATOM   6520 C C   . THR F 3 71  ? -23.698 -7.021  13.456  1.000 46.778  0 71  THR FFF C   1 ? 25 
ATOM   6521 O O   . THR F 3 71  ? -24.447 -6.414  12.669  1.000 47.319  0 71  THR FFF O   1 ? 25 
ATOM   6522 C CB  . THR F 3 71  ? -23.981 -9.550  13.289  1.000 49.182  0 71  THR FFF CB  1 ? 25 
ATOM   6523 O OG1 . THR F 3 71  ? -24.593 -9.403  12.007  1.000 49.276  0 71  THR FFF OG1 1 ? 25 
ATOM   6524 C CG2 . THR F 3 71  ? -24.478 -10.814 13.954  1.000 51.201  0 71  THR FFF CG2 1 ? 25 
ATOM   6525 N N   . VAL F 3 72  ? -22.469 -6.624  13.793  1.000 44.745  0 72  VAL FFF N   1 ? 25 
ATOM   6526 C CA  . VAL F 3 72  ? -21.727 -5.522  13.117  1.000 43.558  0 72  VAL FFF CA  1 ? 25 
ATOM   6527 C C   . VAL F 3 72  ? -20.666 -6.165  12.223  1.000 43.607  0 72  VAL FFF C   1 ? 25 
ATOM   6528 O O   . VAL F 3 72  ? -19.996 -7.102  12.677  1.000 44.596  0 72  VAL FFF O   1 ? 25 
ATOM   6529 C CB  . VAL F 3 72  ? -21.097 -4.536  14.119  1.000 42.947  0 72  VAL FFF CB  1 ? 25 
ATOM   6530 C CG1 . VAL F 3 72  ? -20.391 -3.393  13.406  1.000 42.972  0 72  VAL FFF CG1 1 ? 25 
ATOM   6531 C CG2 . VAL F 3 72  ? -22.123 -3.991  15.098  1.000 42.844  0 72  VAL FFF CG2 1 ? 25 
ATOM   6532 N N   . SER F 3 73  ? -20.558 -5.687  10.986  1.000 43.998  0 73  SER FFF N   1 ? 25 
ATOM   6533 C CA  . SER F 3 73  ? -19.522 -6.077  9.998   1.000 44.599  0 73  SER FFF CA  1 ? 25 
ATOM   6534 C C   . SER F 3 73  ? -18.937 -4.806  9.383   1.000 44.419  0 73  SER FFF C   1 ? 25 
ATOM   6535 O O   . SER F 3 73  ? -19.508 -3.713  9.602   1.000 45.942  0 73  SER FFF O   1 ? 25 
ATOM   6536 C CB  . SER F 3 73  ? -20.084 -6.991  8.942   1.000 46.162  0 73  SER FFF CB  1 ? 25 
ATOM   6537 O OG  . SER F 3 73  ? -20.928 -6.278  8.049   1.000 46.446  0 73  SER FFF OG  1 ? 25 
ATOM   6538 N N   . ARG F 3 74  ? -17.845 -4.956  8.640   1.000 44.237  0 74  ARG FFF N   1 ? 25 
ATOM   6539 C CA  . ARG F 3 74  ? -17.125 -3.848  7.970   1.000 45.735  0 74  ARG FFF CA  1 ? 25 
ATOM   6540 C C   . ARG F 3 74  ? -16.723 -4.326  6.574   1.000 45.293  0 74  ARG FFF C   1 ? 25 
ATOM   6541 O O   . ARG F 3 74  ? -16.492 -5.540  6.425   1.000 45.292  0 74  ARG FFF O   1 ? 25 
ATOM   6542 C CB  . ARG F 3 74  ? -15.916 -3.465  8.827   1.000 47.750  0 74  ARG FFF CB  1 ? 25 
ATOM   6543 C CG  . ARG F 3 74  ? -15.318 -2.103  8.512   1.000 48.712  0 74  ARG FFF CG  1 ? 25 
ATOM   6544 C CD  . ARG F 3 74  ? -14.317 -1.681  9.579   1.000 47.955  0 74  ARG FFF CD  1 ? 25 
ATOM   6545 N NE  . ARG F 3 74  ? -13.078 -2.451  9.562   1.000 47.269  0 74  ARG FFF NE  1 ? 25 
ATOM   6546 C CZ  . ARG F 3 74  ? -12.052 -2.260  10.388  1.000 47.601  0 74  ARG FFF CZ  1 ? 25 
ATOM   6547 N NH1 . ARG F 3 74  ? -12.104 -1.323  11.321  1.000 46.790  0 74  ARG FFF NH1 1 ? 25 
ATOM   6548 N NH2 . ARG F 3 74  ? -10.965 -3.004  10.268  1.000 49.215  0 74  ARG FFF NH2 1 ? 25 
ATOM   6549 N N   . ASN F 3 75  ? -16.661 -3.414  5.599   1.000 45.139  0 75  ASN FFF N   1 ? 25 
ATOM   6550 C CA  . ASN F 3 75  ? -16.274 -3.727  4.196   1.000 45.585  0 75  ASN FFF CA  1 ? 25 
ATOM   6551 C C   . ASN F 3 75  ? -14.751 -3.902  4.122   1.000 45.418  0 75  ASN FFF C   1 ? 25 
ATOM   6552 O O   . ASN F 3 75  ? -14.062 -3.517  5.079   1.000 42.833  0 75  ASN FFF O   1 ? 25 
ATOM   6553 C CB  . ASN F 3 75  ? -16.784 -2.668  3.212   1.000 46.552  0 75  ASN FFF CB  1 ? 25 
ATOM   6554 C CG  . ASN F 3 75  ? -16.128 -1.312  3.373   1.000 46.129  0 75  ASN FFF CG  1 ? 25 
ATOM   6555 O OD1 . ASN F 3 75  ? -15.450 -1.057  4.372   1.000 45.087  0 75  ASN FFF OD1 1 ? 25 
ATOM   6556 N ND2 . ASN F 3 75  ? -16.333 -0.435  2.401   1.000 45.555  0 75  ASN FFF ND2 1 ? 25 
ATOM   6557 N N   . ASN F 3 76  ? -14.251 -4.448  3.009   1.000 48.705  0 76  ASN FFF N   1 ? 25 
ATOM   6558 C CA  . ASN F 3 76  ? -12.808 -4.714  2.769   1.000 50.361  0 76  ASN FFF CA  1 ? 25 
ATOM   6559 C C   . ASN F 3 76  ? -12.022 -3.397  2.817   1.000 48.884  0 76  ASN FFF C   1 ? 25 
ATOM   6560 O O   . ASN F 3 76  ? -10.881 -3.424  3.313   1.000 49.268  0 76  ASN FFF O   1 ? 25 
ATOM   6561 C CB  . ASN F 3 76  ? -12.579 -5.456  1.449   1.000 55.839  0 76  ASN FFF CB  1 ? 25 
ATOM   6562 C CG  . ASN F 3 76  ? -13.185 -6.847  1.439   1.000 59.202  0 76  ASN FFF CG  1 ? 25 
ATOM   6563 O OD1 . ASN F 3 76  ? -13.521 -7.393  2.490   1.000 57.203  0 76  ASN FFF OD1 1 ? 25 
ATOM   6564 N ND2 . ASN F 3 76  ? -13.336 -7.427  0.258   1.000 63.069  0 76  ASN FFF ND2 1 ? 25 
ATOM   6565 N N   . ALA F 3 77  ? -12.608 -2.295  2.337   1.000 48.066  0 77  ALA FFF N   1 ? 25 
ATOM   6566 C CA  . ALA F 3 77  ? -12.006 -0.938  2.355   1.000 48.350  0 77  ALA FFF CA  1 ? 25 
ATOM   6567 C C   . ALA F 3 77  ? -11.808 -0.461  3.802   1.000 46.655  0 77  ALA FFF C   1 ? 25 
ATOM   6568 O O   . ALA F 3 77  ? -10.894 0.340   4.027   1.000 45.567  0 77  ALA FFF O   1 ? 25 
ATOM   6569 C CB  . ALA F 3 77  ? -12.864 0.027   1.570   1.000 48.623  0 77  ALA FFF CB  1 ? 25 
ATOM   6570 N N   . LYS F 3 78  ? -12.648 -0.932  4.732   1.000 49.211  0 78  LYS FFF N   1 ? 25 
ATOM   6571 C CA  . LYS F 3 78  ? -12.622 -0.606  6.192   1.000 49.463  0 78  LYS FFF CA  1 ? 25 
ATOM   6572 C C   . LYS F 3 78  ? -13.114 0.831   6.422   1.000 45.936  0 78  LYS FFF C   1 ? 25 
ATOM   6573 O O   . LYS F 3 78  ? -12.764 1.402   7.468   1.000 44.742  0 78  LYS FFF O   1 ? 25 
ATOM   6574 C CB  . LYS F 3 78  ? -11.222 -0.773  6.795   1.000 52.130  0 78  LYS FFF CB  1 ? 25 
ATOM   6575 C CG  . LYS F 3 78  ? -10.458 -2.019  6.371   1.000 57.049  0 78  LYS FFF CG  1 ? 25 
ATOM   6576 C CD  . LYS F 3 78  ? -9.180  -2.234  7.156   1.000 58.845  0 78  LYS FFF CD  1 ? 25 
ATOM   6577 C CE  . LYS F 3 78  ? -8.344  -3.374  6.619   1.000 62.306  0 78  LYS FFF CE  1 ? 25 
ATOM   6578 N NZ  . LYS F 3 78  ? -7.014  -3.424  7.270   1.000 65.762  0 78  LYS FFF NZ  1 ? 25 
ATOM   6579 N N   . ASP F 3 79  ? -13.877 1.395   5.479   1.000 44.243  0 79  ASP FFF N   1 ? 25 
ATOM   6580 C CA  . ASP F 3 79  ? -14.392 2.790   5.550   1.000 44.120  0 79  ASP FFF CA  1 ? 25 
ATOM   6581 C C   . ASP F 3 79  ? -15.912 2.783   5.764   1.000 43.017  0 79  ASP FFF C   1 ? 25 
ATOM   6582 O O   . ASP F 3 79  ? -16.457 3.869   6.037   1.000 41.399  0 79  ASP FFF O   1 ? 25 
ATOM   6583 C CB  . ASP F 3 79  ? -13.999 3.611   4.318   1.000 45.402  0 79  ASP FFF CB  1 ? 25 
ATOM   6584 C CG  . ASP F 3 79  ? -14.434 3.031   2.982   1.000 46.720  0 79  ASP FFF CG  1 ? 25 
ATOM   6585 O OD1 . ASP F 3 79  ? -15.323 2.153   2.968   1.000 45.521  0 79  ASP FFF OD1 1 ? 25 
ATOM   6586 O OD2 . ASP F 3 79  ? -13.875 3.467   1.960   1.000 50.035  0 79  ASP FFF OD2 1 ? 25 
ATOM   6587 N N   . THR F 3 80  ? -16.559 1.617   5.657   1.000 42.616  0 80  THR FFF N   1 ? 25 
ATOM   6588 C CA  . THR F 3 80  ? -18.023 1.447   5.841   1.000 44.808  0 80  THR FFF CA  1 ? 25 
ATOM   6589 C C   . THR F 3 80  ? -18.287 0.310   6.835   1.000 45.441  0 80  THR FFF C   1 ? 25 
ATOM   6590 O O   . THR F 3 80  ? -17.784 -0.801  6.615   1.000 48.889  0 80  THR FFF O   1 ? 25 
ATOM   6591 C CB  . THR F 3 80  ? -18.738 1.194   4.509   1.000 45.516  0 80  THR FFF CB  1 ? 25 
ATOM   6592 O OG1 . THR F 3 80  ? -18.198 2.085   3.529   1.000 45.930  0 80  THR FFF OG1 1 ? 25 
ATOM   6593 C CG2 . THR F 3 80  ? -20.235 1.380   4.625   1.000 46.845  0 80  THR FFF CG2 1 ? 25 
ATOM   6594 N N   . VAL F 3 81  ? -19.057 0.598   7.883   1.000 45.423  0 81  VAL FFF N   1 ? 25 
ATOM   6595 C CA  . VAL F 3 81  ? -19.497 -0.377  8.922   1.000 46.270  0 81  VAL FFF CA  1 ? 25 
ATOM   6596 C C   . VAL F 3 81  ? -21.007 -0.572  8.765   1.000 46.535  0 81  VAL FFF C   1 ? 25 
ATOM   6597 O O   . VAL F 3 81  ? -21.709 0.425   8.517   1.000 45.629  0 81  VAL FFF O   1 ? 25 
ATOM   6598 C CB  . VAL F 3 81  ? -19.116 0.115   10.332  1.000 48.038  0 81  VAL FFF CB  1 ? 25 
ATOM   6599 C CG1 . VAL F 3 81  ? -19.753 -0.725  11.427  1.000 50.028  0 81  VAL FFF CG1 1 ? 25 
ATOM   6600 C CG2 . VAL F 3 81  ? -17.603 0.156   10.515  1.000 49.104  0 81  VAL FFF CG2 1 ? 25 
ATOM   6601 N N   . TYR F 3 82  ? -21.474 -1.813  8.891   1.000 46.728  0 82  TYR FFF N   1 ? 25 
ATOM   6602 C CA  . TYR F 3 82  ? -22.901 -2.199  8.747   1.000 48.951  0 82  TYR FFF CA  1 ? 25 
ATOM   6603 C C   . TYR F 3 82  ? -23.410 -2.747  10.084  1.000 49.136  0 82  TYR FFF C   1 ? 25 
ATOM   6604 O O   . TYR F 3 82  ? -22.698 -3.546  10.719  1.000 52.624  0 82  TYR FFF O   1 ? 25 
ATOM   6605 C CB  . TYR F 3 82  ? -23.060 -3.215  7.613   1.000 50.425  0 82  TYR FFF CB  1 ? 25 
ATOM   6606 C CG  . TYR F 3 82  ? -22.440 -2.780  6.309   1.000 50.883  0 82  TYR FFF CG  1 ? 25 
ATOM   6607 C CD1 . TYR F 3 82  ? -23.121 -1.937  5.445   1.000 50.945  0 82  TYR FFF CD1 1 ? 25 
ATOM   6608 C CD2 . TYR F 3 82  ? -21.164 -3.187  5.947   1.000 49.832  0 82  TYR FFF CD2 1 ? 25 
ATOM   6609 C CE1 . TYR F 3 82  ? -22.561 -1.521  4.247   1.000 52.595  0 82  TYR FFF CE1 1 ? 25 
ATOM   6610 C CE2 . TYR F 3 82  ? -20.588 -2.776  4.755   1.000 51.464  0 82  TYR FFF CE2 1 ? 25 
ATOM   6611 C CZ  . TYR F 3 82  ? -21.287 -1.940  3.902   1.000 52.932  0 82  TYR FFF CZ  1 ? 25 
ATOM   6612 O OH  . TYR F 3 82  ? -20.722 -1.529  2.733   1.000 53.046  0 82  TYR FFF OH  1 ? 25 
ATOM   6613 N N   . LEU F 3 83  ? -24.590 -2.291  10.516  1.000 49.529  0 83  LEU FFF N   1 ? 25 
ATOM   6614 C CA  . LEU F 3 83  ? -25.371 -2.920  11.612  1.000 47.247  0 83  LEU FFF CA  1 ? 25 
ATOM   6615 C C   . LEU F 3 83  ? -26.464 -3.780  10.972  1.000 49.638  0 83  LEU FFF C   1 ? 25 
ATOM   6616 O O   . LEU F 3 83  ? -27.436 -3.201  10.455  1.000 50.584  0 83  LEU FFF O   1 ? 25 
ATOM   6617 C CB  . LEU F 3 83  ? -25.955 -1.836  12.527  1.000 45.656  0 83  LEU FFF CB  1 ? 25 
ATOM   6618 C CG  . LEU F 3 83  ? -26.715 -2.355  13.750  1.000 46.567  0 83  LEU FFF CG  1 ? 25 
ATOM   6619 C CD1 . LEU F 3 83  ? -25.782 -3.098  14.689  1.000 44.979  0 83  LEU FFF CD1 1 ? 25 
ATOM   6620 C CD2 . LEU F 3 83  ? -27.421 -1.227  14.491  1.000 46.249  0 83  LEU FFF CD2 1 ? 25 
ATOM   6621 N N   . HIS F 3 84  ? -26.276 -5.102  10.970  1.000 50.837  0 84  HIS FFF N   1 ? 25 
ATOM   6622 C CA  . HIS F 3 84  ? -27.277 -6.103  10.510  1.000 53.701  0 84  HIS FFF CA  1 ? 25 
ATOM   6623 C C   . HIS F 3 84  ? -28.260 -6.362  11.659  1.000 54.734  0 84  HIS FFF C   1 ? 25 
ATOM   6624 O O   . HIS F 3 84  ? -27.858 -6.991  12.659  1.000 53.977  0 84  HIS FFF O   1 ? 25 
ATOM   6625 C CB  . HIS F 3 84  ? -26.594 -7.392  10.031  1.000 54.765  0 84  HIS FFF CB  1 ? 25 
ATOM   6626 C CG  . HIS F 3 84  ? -25.504 -7.168  9.037   1.000 54.265  0 84  HIS FFF CG  1 ? 25 
ATOM   6627 N ND1 . HIS F 3 84  ? -25.741 -7.137  7.677   1.000 55.656  0 84  HIS FFF ND1 1 ? 25 
ATOM   6628 C CD2 . HIS F 3 84  ? -24.179 -6.965  9.199   1.000 52.780  0 84  HIS FFF CD2 1 ? 25 
ATOM   6629 C CE1 . HIS F 3 84  ? -24.605 -6.920  7.045   1.000 55.792  0 84  HIS FFF CE1 1 ? 25 
ATOM   6630 N NE2 . HIS F 3 84  ? -23.634 -6.808  7.957   1.000 53.537  0 84  HIS FFF NE2 1 ? 25 
ATOM   6631 N N   . MET F 3 85  ? -29.488 -5.858  11.529  1.000 55.420  0 85  MET FFF N   1 ? 25 
ATOM   6632 C CA  . MET F 3 85  ? -30.555 -5.952  12.558  1.000 56.489  0 85  MET FFF CA  1 ? 25 
ATOM   6633 C C   . MET F 3 85  ? -31.538 -7.058  12.156  1.000 58.841  0 85  MET FFF C   1 ? 25 
ATOM   6634 O O   . MET F 3 85  ? -32.342 -6.823  11.238  1.000 62.219  0 85  MET FFF O   1 ? 25 
ATOM   6635 C CB  . MET F 3 85  ? -31.287 -4.612  12.693  1.000 56.852  0 85  MET FFF CB  1 ? 25 
ATOM   6636 C CG  . MET F 3 85  ? -30.359 -3.425  12.863  1.000 55.541  0 85  MET FFF CG  1 ? 25 
ATOM   6637 S SD  . MET F 3 85  ? -31.209 -1.926  13.406  1.000 55.571  0 85  MET FFF SD  1 ? 25 
ATOM   6638 C CE  . MET F 3 85  ? -32.242 -1.624  11.980  1.000 59.444  0 85  MET FFF CE  1 ? 25 
ATOM   6639 N N   . ASN F 3 86  ? -31.454 -8.222  12.809  1.000 59.754  0 86  ASN FFF N   1 ? 25 
ATOM   6640 C CA  . ASN F 3 86  ? -32.329 -9.402  12.570  1.000 62.543  0 86  ASN FFF CA  1 ? 25 
ATOM   6641 C C   . ASN F 3 86  ? -33.216 -9.639  13.796  1.000 64.627  0 86  ASN FFF C   1 ? 25 
ATOM   6642 O O   . ASN F 3 86  ? -32.862 -9.153  14.886  1.000 62.931  0 86  ASN FFF O   1 ? 25 
ATOM   6643 C CB  . ASN F 3 86  ? -31.511 -10.655 12.254  1.000 62.775  0 86  ASN FFF CB  1 ? 25 
ATOM   6644 C CG  . ASN F 3 86  ? -30.513 -10.435 11.139  1.000 61.964  0 86  ASN FFF CG  1 ? 25 
ATOM   6645 O OD1 . ASN F 3 86  ? -29.308 -10.551 11.349  1.000 61.603  0 86  ASN FFF OD1 1 ? 25 
ATOM   6646 N ND2 . ASN F 3 86  ? -31.004 -10.109 9.955   1.000 62.906  0 86  ASN FFF ND2 1 ? 25 
ATOM   6647 N N   . SER F 3 87  ? -34.322 -10.368 13.616  1.000 69.853  0 87  SER FFF N   1 ? 25 
ATOM   6648 C CA  . SER F 3 87  ? -35.286 -10.744 14.685  1.000 71.716  0 87  SER FFF CA  1 ? 25 
ATOM   6649 C C   . SER F 3 87  ? -35.726 -9.483  15.437  1.000 71.724  0 87  SER FFF C   1 ? 25 
ATOM   6650 O O   . SER F 3 87  ? -35.630 -9.464  16.676  1.000 74.003  0 87  SER FFF O   1 ? 25 
ATOM   6651 C CB  . SER F 3 87  ? -34.675 -11.763 15.615  1.000 71.590  0 87  SER FFF CB  1 ? 25 
ATOM   6652 O OG  . SER F 3 87  ? -34.154 -12.862 14.883  1.000 73.024  0 87  SER FFF OG  1 ? 25 
ATOM   6653 N N   . LEU F 3 88  ? -36.176 -8.463  14.701  1.000 71.529  0 88  LEU FFF N   1 ? 25 
ATOM   6654 C CA  . LEU F 3 88  ? -36.460 -7.106  15.241  1.000 69.990  0 88  LEU FFF CA  1 ? 25 
ATOM   6655 C C   . LEU F 3 88  ? -37.762 -7.130  16.051  1.000 72.465  0 88  LEU FFF C   1 ? 25 
ATOM   6656 O O   . LEU F 3 88  ? -38.746 -7.727  15.581  1.000 72.538  0 88  LEU FFF O   1 ? 25 
ATOM   6657 C CB  . LEU F 3 88  ? -36.528 -6.104  14.084  1.000 69.399  0 88  LEU FFF CB  1 ? 25 
ATOM   6658 C CG  . LEU F 3 88  ? -35.178 -5.567  13.610  1.000 66.411  0 88  LEU FFF CG  1 ? 25 
ATOM   6659 C CD1 . LEU F 3 88  ? -35.283 -4.990  12.209  1.000 66.599  0 88  LEU FFF CD1 1 ? 25 
ATOM   6660 C CD2 . LEU F 3 88  ? -34.639 -4.521  14.577  1.000 64.319  0 88  LEU FFF CD2 1 ? 25 
ATOM   6661 N N   . LYS F 3 89  ? -37.735 -6.513  17.237  1.000 74.262  0 89  LYS FFF N   1 ? 26 
ATOM   6662 C CA  . LYS F 3 89  ? -38.885 -6.342  18.166  1.000 75.341  0 89  LYS FFF CA  1 ? 26 
ATOM   6663 C C   . LYS F 3 89  ? -39.419 -4.919  18.025  1.000 74.015  0 89  LYS FFF C   1 ? 26 
ATOM   6664 O O   . LYS F 3 89  ? -38.728 -4.053  17.494  1.000 72.728  0 89  LYS FFF O   1 ? 26 
ATOM   6665 C CB  . LYS F 3 89  ? -38.434 -6.580  19.610  1.000 75.994  0 89  LYS FFF CB  1 ? 26 
ATOM   6666 C CG  . LYS F 3 89  ? -37.869 -7.968  19.906  1.000 77.902  0 89  LYS FFF CG  1 ? 26 
ATOM   6667 C CD  . LYS F 3 89  ? -37.047 -8.049  21.188  1.000 77.819  0 89  LYS FFF CD  1 ? 26 
ATOM   6668 C CE  . LYS F 3 89  ? -37.273 -9.317  21.995  1.000 80.919  0 89  LYS FFF CE  1 ? 26 
ATOM   6669 N NZ  . LYS F 3 89  ? -36.944 -10.543 21.229  1.000 81.630  0 89  LYS FFF NZ  1 ? 26 
ATOM   6670 N N   . PRO F 3 90  ? -40.655 -4.621  18.490  1.000 75.047  0 90  PRO FFF N   1 ? 26 
ATOM   6671 C CA  . PRO F 3 90  ? -41.123 -3.236  18.598  1.000 73.830  0 90  PRO FFF CA  1 ? 26 
ATOM   6672 C C   . PRO F 3 90  ? -40.254 -2.405  19.558  1.000 70.754  0 90  PRO FFF C   1 ? 26 
ATOM   6673 O O   . PRO F 3 90  ? -40.115 -1.219  19.339  1.000 66.863  0 90  PRO FFF O   1 ? 26 
ATOM   6674 C CB  . PRO F 3 90  ? -42.562 -3.373  19.123  1.000 76.390  0 90  PRO FFF CB  1 ? 26 
ATOM   6675 C CG  . PRO F 3 90  ? -42.962 -4.787  18.755  1.000 78.338  0 90  PRO FFF CG  1 ? 26 
ATOM   6676 C CD  . PRO F 3 90  ? -41.686 -5.590  18.893  1.000 77.354  0 90  PRO FFF CD  1 ? 26 
ATOM   6677 N N   . GLU F 3 91  ? -39.688 -3.060  20.580  1.000 73.194  0 91  GLU FFF N   1 ? 26 
ATOM   6678 C CA  . GLU F 3 91  ? -38.753 -2.482  21.587  1.000 75.375  0 91  GLU FFF CA  1 ? 26 
ATOM   6679 C C   . GLU F 3 91  ? -37.509 -1.893  20.892  1.000 70.018  0 91  GLU FFF C   1 ? 26 
ATOM   6680 O O   . GLU F 3 91  ? -36.833 -1.056  21.516  1.000 69.681  0 91  GLU FFF O   1 ? 26 
ATOM   6681 C CB  . GLU F 3 91  ? -38.390 -3.578  22.599  1.000 80.808  0 91  GLU FFF CB  1 ? 26 
ATOM   6682 C CG  . GLU F 3 91  ? -37.434 -3.154  23.708  1.000 83.528  0 91  GLU FFF CG  1 ? 26 
ATOM   6683 C CD  . GLU F 3 91  ? -36.768 -4.308  24.446  1.000 87.594  0 91  GLU FFF CD  1 ? 26 
ATOM   6684 O OE1 . GLU F 3 91  ? -37.492 -5.266  24.805  1.000 92.102  0 91  GLU FFF OE1 1 ? 26 
ATOM   6685 O OE2 . GLU F 3 91  ? -35.524 -4.255  24.655  1.000 82.692  0 91  GLU FFF OE2 1 ? 26 
ATOM   6686 N N   . ASP F 3 92  ? -37.208 -2.315  19.659  1.000 65.619  0 92  ASP FFF N   1 ? 26 
ATOM   6687 C CA  . ASP F 3 92  ? -36.029 -1.859  18.871  1.000 61.404  0 92  ASP FFF CA  1 ? 26 
ATOM   6688 C C   . ASP F 3 92  ? -36.317 -0.522  18.172  1.000 58.937  0 92  ASP FFF C   1 ? 26 
ATOM   6689 O O   . ASP F 3 92  ? -35.357 0.083   17.670  1.000 57.515  0 92  ASP FFF O   1 ? 26 
ATOM   6690 C CB  . ASP F 3 92  ? -35.605 -2.912  17.841  1.000 60.676  0 92  ASP FFF CB  1 ? 26 
ATOM   6691 C CG  . ASP F 3 92  ? -35.050 -4.188  18.456  1.000 61.313  0 92  ASP FFF CG  1 ? 26 
ATOM   6692 O OD1 . ASP F 3 92  ? -34.271 -4.086  19.430  1.000 59.839  0 92  ASP FFF OD1 1 ? 26 
ATOM   6693 O OD2 . ASP F 3 92  ? -35.401 -5.278  17.958  1.000 62.521  0 92  ASP FFF OD2 1 ? 26 
ATOM   6694 N N   . THR F 3 93  ? -37.577 -0.083  18.124  1.000 58.493  0 93  THR FFF N   1 ? 26 
ATOM   6695 C CA  . THR F 3 93  ? -38.005 1.182   17.465  1.000 57.317  0 93  THR FFF CA  1 ? 26 
ATOM   6696 C C   . THR F 3 93  ? -37.303 2.371   18.133  1.000 54.987  0 93  THR FFF C   1 ? 26 
ATOM   6697 O O   . THR F 3 93  ? -37.498 2.566   19.347  1.000 55.861  0 93  THR FFF O   1 ? 26 
ATOM   6698 C CB  . THR F 3 93  ? -39.532 1.328   17.496  1.000 59.438  0 93  THR FFF CB  1 ? 26 
ATOM   6699 O OG1 . THR F 3 93  ? -40.067 0.247   16.732  1.000 61.115  0 93  THR FFF OG1 1 ? 26 
ATOM   6700 C CG2 . THR F 3 93  ? -40.019 2.649   16.945  1.000 59.608  0 93  THR FFF CG2 1 ? 26 
ATOM   6701 N N   . ALA F 3 94  ? -36.520 3.133   17.365  1.000 53.424  0 94  ALA FFF N   1 ? 26 
ATOM   6702 C CA  . ALA F 3 94  ? -35.736 4.301   17.833  1.000 52.056  0 94  ALA FFF CA  1 ? 26 
ATOM   6703 C C   . ALA F 3 94  ? -35.058 4.995   16.648  1.000 51.396  0 94  ALA FFF C   1 ? 26 
ATOM   6704 O O   . ALA F 3 94  ? -35.068 4.431   15.529  1.000 50.915  0 94  ALA FFF O   1 ? 26 
ATOM   6705 C CB  . ALA F 3 94  ? -34.710 3.855   18.848  1.000 51.034  0 94  ALA FFF CB  1 ? 26 
ATOM   6706 N N   . VAL F 3 95  ? -34.492 6.178   16.895  1.000 51.244  0 95  VAL FFF N   1 ? 26 
ATOM   6707 C CA  . VAL F 3 95  ? -33.508 6.835   15.986  1.000 50.702  0 95  VAL FFF CA  1 ? 26 
ATOM   6708 C C   . VAL F 3 95  ? -32.131 6.254   16.318  1.000 48.676  0 95  VAL FFF C   1 ? 26 
ATOM   6709 O O   . VAL F 3 95  ? -31.699 6.396   17.475  1.000 47.214  0 95  VAL FFF O   1 ? 26 
ATOM   6710 C CB  . VAL F 3 95  ? -33.517 8.369   16.124  1.000 51.472  0 95  VAL FFF CB  1 ? 26 
ATOM   6711 C CG1 . VAL F 3 95  ? -32.469 9.010   15.228  1.000 51.352  0 95  VAL FFF CG1 1 ? 26 
ATOM   6712 C CG2 . VAL F 3 95  ? -34.889 8.953   15.836  1.000 53.595  0 95  VAL FFF CG2 1 ? 26 
ATOM   6713 N N   . TYR F 3 96  ? -31.485 5.619   15.336  1.000 47.705  0 96  TYR FFF N   1 ? 26 
ATOM   6714 C CA  . TYR F 3 96  ? -30.165 4.957   15.484  1.000 46.564  0 96  TYR FFF CA  1 ? 26 
ATOM   6715 C C   . TYR F 3 96  ? -29.074 5.911   14.991  1.000 45.926  0 96  TYR FFF C   1 ? 26 
ATOM   6716 O O   . TYR F 3 96  ? -29.263 6.539   13.937  1.000 45.598  0 96  TYR FFF O   1 ? 26 
ATOM   6717 C CB  . TYR F 3 96  ? -30.159 3.611   14.760  1.000 46.706  0 96  TYR FFF CB  1 ? 26 
ATOM   6718 C CG  . TYR F 3 96  ? -30.880 2.518   15.508  1.000 47.653  0 96  TYR FFF CG  1 ? 26 
ATOM   6719 C CD1 . TYR F 3 96  ? -32.263 2.501   15.589  1.000 49.955  0 96  TYR FFF CD1 1 ? 26 
ATOM   6720 C CD2 . TYR F 3 96  ? -30.186 1.508   16.153  1.000 47.324  0 96  TYR FFF CD2 1 ? 26 
ATOM   6721 C CE1 . TYR F 3 96  ? -32.937 1.507   16.281  1.000 50.562  0 96  TYR FFF CE1 1 ? 26 
ATOM   6722 C CE2 . TYR F 3 96  ? -30.842 0.505   16.847  1.000 48.127  0 96  TYR FFF CE2 1 ? 26 
ATOM   6723 C CZ  . TYR F 3 96  ? -32.224 0.502   16.911  1.000 49.990  0 96  TYR FFF CZ  1 ? 26 
ATOM   6724 O OH  . TYR F 3 96  ? -32.871 -0.483  17.598  1.000 50.277  0 96  TYR FFF OH  1 ? 26 
ATOM   6725 N N   . TYR F 3 97  ? -27.995 6.030   15.771  1.000 45.038  0 97  TYR FFF N   1 ? 26 
ATOM   6726 C CA  . TYR F 3 97  ? -26.806 6.871   15.487  1.000 46.928  0 97  TYR FFF CA  1 ? 26 
ATOM   6727 C C   . TYR F 3 97  ? -25.551 5.997   15.516  1.000 46.007  0 97  TYR FFF C   1 ? 26 
ATOM   6728 O O   . TYR F 3 97  ? -25.481 5.079   16.346  1.000 45.259  0 97  TYR FFF O   1 ? 26 
ATOM   6729 C CB  . TYR F 3 97  ? -26.640 7.977   16.531  1.000 47.934  0 97  TYR FFF CB  1 ? 26 
ATOM   6730 C CG  . TYR F 3 97  ? -27.812 8.908   16.695  1.000 49.969  0 97  TYR FFF CG  1 ? 26 
ATOM   6731 C CD1 . TYR F 3 97  ? -28.840 8.610   17.575  1.000 51.882  0 97  TYR FFF CD1 1 ? 26 
ATOM   6732 C CD2 . TYR F 3 97  ? -27.875 10.107  16.006  1.000 51.520  0 97  TYR FFF CD2 1 ? 26 
ATOM   6733 C CE1 . TYR F 3 97  ? -29.915 9.469   17.745  1.000 53.732  0 97  TYR FFF CE1 1 ? 26 
ATOM   6734 C CE2 . TYR F 3 97  ? -28.945 10.973  16.159  1.000 54.234  0 97  TYR FFF CE2 1 ? 26 
ATOM   6735 C CZ  . TYR F 3 97  ? -29.968 10.654  17.032  1.000 55.106  0 97  TYR FFF CZ  1 ? 26 
ATOM   6736 O OH  . TYR F 3 97  ? -31.023 11.503  17.187  1.000 61.017  0 97  TYR FFF OH  1 ? 26 
ATOM   6737 N N   . CYS F 3 98  ? -24.584 6.281   14.648  1.000 45.620  0 98  CYS FFF N   1 ? 26 
ATOM   6738 C CA  . CYS F 3 98  ? -23.203 5.745   14.761  1.000 45.928  0 98  CYS FFF CA  1 ? 26 
ATOM   6739 C C   . CYS F 3 98  ? -22.271 6.876   15.208  1.000 43.599  0 98  CYS FFF C   1 ? 26 
ATOM   6740 O O   . CYS F 3 98  ? -22.625 8.060   15.028  1.000 43.472  0 98  CYS FFF O   1 ? 26 
ATOM   6741 C CB  . CYS F 3 98  ? -22.725 5.114   13.458  1.000 47.615  0 98  CYS FFF CB  1 ? 26 
ATOM   6742 S SG  . CYS F 3 98  ? -22.695 6.280   12.079  1.000 52.484  0 98  CYS FFF SG  1 ? 26 
ATOM   6743 N N   . ALA F 3 99  ? -21.133 6.512   15.791  1.000 42.505  0 99  ALA FFF N   1 ? 26 
ATOM   6744 C CA  . ALA F 3 99  ? -20.123 7.455   16.319  1.000 43.055  0 99  ALA FFF CA  1 ? 26 
ATOM   6745 C C   . ALA F 3 99  ? -18.801 6.714   16.526  1.000 42.717  0 99  ALA FFF C   1 ? 26 
ATOM   6746 O O   . ALA F 3 99  ? -18.801 5.468   16.421  1.000 41.650  0 99  ALA FFF O   1 ? 26 
ATOM   6747 C CB  . ALA F 3 99  ? -20.619 8.075   17.598  1.000 42.283  0 99  ALA FFF CB  1 ? 26 
ATOM   6748 N N   . ILE F 3 100 ? -17.727 7.464   16.788  1.000 43.207  0 100 ILE FFF N   1 ? 26 
ATOM   6749 C CA  . ILE F 3 100 ? -16.364 6.924   17.064  1.000 43.793  0 100 ILE FFF CA  1 ? 26 
ATOM   6750 C C   . ILE F 3 100 ? -15.900 7.480   18.413  1.000 45.420  0 100 ILE FFF C   1 ? 26 
ATOM   6751 O O   . ILE F 3 100 ? -16.450 8.513   18.842  1.000 49.502  0 100 ILE FFF O   1 ? 26 
ATOM   6752 C CB  . ILE F 3 100 ? -15.383 7.261   15.920  1.000 44.355  0 100 ILE FFF CB  1 ? 26 
ATOM   6753 C CG1 . ILE F 3 100 ? -15.397 8.750   15.562  1.000 45.147  0 100 ILE FFF CG1 1 ? 26 
ATOM   6754 C CG2 . ILE F 3 100 ? -15.662 6.391   14.706  1.000 43.580  0 100 ILE FFF CG2 1 ? 26 
ATOM   6755 C CD1 . ILE F 3 100 ? -14.224 9.187   14.717  1.000 45.755  0 100 ILE FFF CD1 1 ? 26 
ATOM   6756 N N   . THR F 3 101 ? -14.948 6.806   19.058  1.000 43.745  0 101 THR FFF N   1 ? 26 
ATOM   6757 C CA  . THR F 3 101 ? -14.353 7.219   20.355  1.000 43.266  0 101 THR FFF CA  1 ? 26 
ATOM   6758 C C   . THR F 3 101 ? -12.825 7.139   20.265  1.000 44.226  0 101 THR FFF C   1 ? 26 
ATOM   6759 O O   . THR F 3 101 ? -12.318 6.192   19.616  1.000 43.049  0 101 THR FFF O   1 ? 26 
ATOM   6760 C CB  . THR F 3 101 ? -14.914 6.379   21.511  1.000 42.205  0 101 THR FFF CB  1 ? 26 
ATOM   6761 O OG1 . THR F 3 101 ? -14.332 6.875   22.714  1.000 41.262  0 101 THR FFF OG1 1 ? 26 
ATOM   6762 C CG2 . THR F 3 101 ? -14.633 4.899   21.383  1.000 41.198  0 101 THR FFF CG2 1 ? 26 
ATOM   6763 N N   . THR F 3 102 ? -12.129 8.108   20.873  1.000 45.813  0 102 THR FFF N   1 ? 26 
ATOM   6764 C CA  . THR F 3 102 ? -10.664 8.058   21.137  1.000 46.475  0 102 THR FFF CA  1 ? 26 
ATOM   6765 C C   . THR F 3 102 ? -10.406 7.276   22.429  1.000 45.076  0 102 THR FFF C   1 ? 26 
ATOM   6766 O O   . THR F 3 102 ? -9.250  6.872   22.628  1.000 45.543  0 102 THR FFF O   1 ? 26 
ATOM   6767 C CB  . THR F 3 102 ? -10.037 9.454   21.230  1.000 48.298  0 102 THR FFF CB  1 ? 26 
ATOM   6768 O OG1 . THR F 3 102 ? -10.656 10.150  22.309  1.000 50.231  0 102 THR FFF OG1 1 ? 26 
ATOM   6769 C CG2 . THR F 3 102 ? -10.187 10.257  19.958  1.000 50.438  0 102 THR FFF CG2 1 ? 26 
ATOM   6770 N N   . ILE F 3 103 ? -11.442 7.066   23.254  1.000 44.180  0 103 ILE FFF N   1 ? 26 
ATOM   6771 C CA  . ILE F 3 103 ? -11.330 6.388   24.581  1.000 45.026  0 103 ILE FFF CA  1 ? 26 
ATOM   6772 C C   . ILE F 3 103 ? -11.357 4.873   24.359  1.000 44.236  0 103 ILE FFF C   1 ? 26 
ATOM   6773 O O   . ILE F 3 103 ? -12.395 4.356   23.910  1.000 43.693  0 103 ILE FFF O   1 ? 26 
ATOM   6774 C CB  . ILE F 3 103 ? -12.435 6.841   25.556  1.000 46.065  0 103 ILE FFF CB  1 ? 26 
ATOM   6775 C CG1 . ILE F 3 103 ? -12.470 8.365   25.706  1.000 47.946  0 103 ILE FFF CG1 1 ? 26 
ATOM   6776 C CG2 . ILE F 3 103 ? -12.278 6.146   26.902  1.000 45.603  0 103 ILE FFF CG2 1 ? 26 
ATOM   6777 C CD1 . ILE F 3 103 ? -13.501 8.866   26.701  1.000 48.155  0 103 ILE FFF CD1 1 ? 26 
ATOM   6778 N N   . VAL F 3 104 ? -10.242 4.203   24.659  1.000 44.690  0 104 VAL FFF N   1 ? 26 
ATOM   6779 C CA  . VAL F 3 104 ? -10.105 2.720   24.571  1.000 43.518  0 104 VAL FFF CA  1 ? 26 
ATOM   6780 C C   . VAL F 3 104 ? -10.387 2.133   25.957  1.000 42.828  0 104 VAL FFF C   1 ? 26 
ATOM   6781 O O   . VAL F 3 104 ? -9.520  2.251   26.855  1.000 40.948  0 104 VAL FFF O   1 ? 26 
ATOM   6782 C CB  . VAL F 3 104 ? -8.724  2.307   24.032  1.000 43.573  0 104 VAL FFF CB  1 ? 26 
ATOM   6783 C CG1 . VAL F 3 104 ? -8.628  0.799   23.854  1.000 43.976  0 104 VAL FFF CG1 1 ? 26 
ATOM   6784 C CG2 . VAL F 3 104 ? -8.412  3.025   22.726  1.000 43.934  0 104 VAL FFF CG2 1 ? 26 
ATOM   6785 N N   . ARG F 3 105 ? -11.582 1.562   26.118  1.000 41.775  0 105 ARG FFF N   1 ? 26 
ATOM   6786 C CA  . ARG F 3 105 ? -12.020 0.849   27.341  1.000 40.325  0 105 ARG FFF CA  1 ? 26 
ATOM   6787 C C   . ARG F 3 105 ? -11.942 -0.654  27.066  1.000 40.391  0 105 ARG FFF C   1 ? 26 
ATOM   6788 O O   . ARG F 3 105 ? -12.685 -1.124  26.179  1.000 43.339  0 105 ARG FFF O   1 ? 26 
ATOM   6789 C CB  . ARG F 3 105 ? -13.442 1.269   27.716  1.000 40.322  0 105 ARG FFF CB  1 ? 26 
ATOM   6790 C CG  . ARG F 3 105 ? -13.636 2.769   27.882  1.000 40.863  0 105 ARG FFF CG  1 ? 26 
ATOM   6791 C CD  . ARG F 3 105 ? -14.986 3.040   28.524  1.000 43.314  0 105 ARG FFF CD  1 ? 26 
ATOM   6792 N NE  . ARG F 3 105 ? -15.262 4.460   28.710  1.000 44.729  0 105 ARG FFF NE  1 ? 26 
ATOM   6793 C CZ  . ARG F 3 105 ? -14.728 5.229   29.655  1.000 46.248  0 105 ARG FFF CZ  1 ? 26 
ATOM   6794 N NH1 . ARG F 3 105 ? -13.875 4.729   30.534  1.000 46.742  0 105 ARG FFF NH1 1 ? 26 
ATOM   6795 N NH2 . ARG F 3 105 ? -15.060 6.505   29.725  1.000 47.873  0 105 ARG FFF NH2 1 ? 26 
ATOM   6796 N N   . ALA F 3 106 ? -11.062 -1.364  27.777  1.000 39.715  0 106 ALA FFF N   1 ? 26 
ATOM   6797 C CA  . ALA F 3 106 ? -10.879 -2.833  27.697  1.000 40.752  0 106 ALA FFF CA  1 ? 26 
ATOM   6798 C C   . ALA F 3 106 ? -12.227 -3.528  27.913  1.000 41.245  0 106 ALA FFF C   1 ? 26 
ATOM   6799 O O   . ALA F 3 106 ? -12.492 -4.541  27.237  1.000 42.124  0 106 ALA FFF O   1 ? 26 
ATOM   6800 C CB  . ALA F 3 106 ? -9.862  -3.282  28.718  1.000 42.617  0 106 ALA FFF CB  1 ? 26 
ATOM   6801 N N   . TYR F 3 107 ? -13.031 -3.007  28.843  1.000 42.119  0 107 TYR FFF N   1 ? 26 
ATOM   6802 C CA  . TYR F 3 107 ? -14.419 -3.456  29.116  1.000 42.670  0 107 TYR FFF CA  1 ? 26 
ATOM   6803 C C   . TYR F 3 107 ? -15.388 -2.554  28.345  1.000 42.098  0 107 TYR FFF C   1 ? 26 
ATOM   6804 O O   . TYR F 3 107 ? -15.592 -1.400  28.774  1.000 41.952  0 107 TYR FFF O   1 ? 26 
ATOM   6805 C CB  . TYR F 3 107 ? -14.712 -3.401  30.614  1.000 44.238  0 107 TYR FFF CB  1 ? 26 
ATOM   6806 C CG  . TYR F 3 107 ? -13.845 -4.271  31.486  1.000 45.368  0 107 TYR FFF CG  1 ? 26 
ATOM   6807 C CD1 . TYR F 3 107 ? -14.178 -5.594  31.730  1.000 46.781  0 107 TYR FFF CD1 1 ? 26 
ATOM   6808 C CD2 . TYR F 3 107 ? -12.724 -3.758  32.120  1.000 44.472  0 107 TYR FFF CD2 1 ? 26 
ATOM   6809 C CE1 . TYR F 3 107 ? -13.405 -6.393  32.556  1.000 47.543  0 107 TYR FFF CE1 1 ? 26 
ATOM   6810 C CE2 . TYR F 3 107 ? -11.946 -4.541  32.957  1.000 44.579  0 107 TYR FFF CE2 1 ? 26 
ATOM   6811 C CZ  . TYR F 3 107 ? -12.287 -5.864  33.175  1.000 46.242  0 107 TYR FFF CZ  1 ? 26 
ATOM   6812 O OH  . TYR F 3 107 ? -11.531 -6.653  33.993  1.000 47.222  0 107 TYR FFF OH  1 ? 26 
ATOM   6813 N N   . TYR F 3 108 ? -15.962 -3.059  27.247  1.000 41.080  0 108 TYR FFF N   1 ? 26 
ATOM   6814 C CA  . TYR F 3 108 ? -16.915 -2.321  26.370  1.000 39.951  0 108 TYR FFF CA  1 ? 26 
ATOM   6815 C C   . TYR F 3 108 ? -18.164 -1.960  27.179  1.000 40.522  0 108 TYR FFF C   1 ? 26 
ATOM   6816 O O   . TYR F 3 108 ? -18.824 -0.956  26.850  1.000 40.672  0 108 TYR FFF O   1 ? 26 
ATOM   6817 C CB  . TYR F 3 108 ? -17.295 -3.139  25.131  1.000 39.686  0 108 TYR FFF CB  1 ? 26 
ATOM   6818 C CG  . TYR F 3 108 ? -18.392 -4.141  25.374  1.000 40.061  0 108 TYR FFF CG  1 ? 26 
ATOM   6819 C CD1 . TYR F 3 108 ? -19.726 -3.771  25.308  1.000 39.696  0 108 TYR FFF CD1 1 ? 26 
ATOM   6820 C CD2 . TYR F 3 108 ? -18.094 -5.453  25.708  1.000 41.236  0 108 TYR FFF CD2 1 ? 26 
ATOM   6821 C CE1 . TYR F 3 108 ? -20.737 -4.681  25.568  1.000 40.931  0 108 TYR FFF CE1 1 ? 26 
ATOM   6822 C CE2 . TYR F 3 108 ? -19.093 -6.375  25.969  1.000 42.513  0 108 TYR FFF CE2 1 ? 26 
ATOM   6823 C CZ  . TYR F 3 108 ? -20.418 -5.988  25.891  1.000 42.350  0 108 TYR FFF CZ  1 ? 26 
ATOM   6824 O OH  . TYR F 3 108 ? -21.395 -6.904  26.143  1.000 44.868  0 108 TYR FFF OH  1 ? 26 
ATOM   6825 N N   . THR F 3 109 ? -18.445 -2.746  28.226  1.000 41.622  0 109 THR FFF N   1 ? 26 
ATOM   6826 C CA  . THR F 3 109 ? -19.604 -2.606  29.145  1.000 42.530  0 109 THR FFF CA  1 ? 26 
ATOM   6827 C C   . THR F 3 109 ? -19.575 -1.245  29.855  1.000 42.869  0 109 THR FFF C   1 ? 26 
ATOM   6828 O O   . THR F 3 109 ? -20.605 -0.889  30.474  1.000 44.243  0 109 THR FFF O   1 ? 26 
ATOM   6829 C CB  . THR F 3 109 ? -19.611 -3.749  30.167  1.000 44.633  0 109 THR FFF CB  1 ? 26 
ATOM   6830 O OG1 . THR F 3 109 ? -18.383 -3.697  30.894  1.000 43.108  0 109 THR FFF OG1 1 ? 26 
ATOM   6831 C CG2 . THR F 3 109 ? -19.757 -5.117  29.537  1.000 45.214  0 109 THR FFF CG2 1 ? 26 
ATOM   6832 N N   . GLU F 3 110 ? -18.453 -0.521  29.788  1.000 41.647  0 110 GLU FFF N   1 ? 26 
ATOM   6833 C CA  . GLU F 3 110 ? -18.261 0.791   30.462  1.000 43.838  0 110 GLU FFF CA  1 ? 26 
ATOM   6834 C C   . GLU F 3 110 ? -18.415 1.944   29.461  1.000 42.678  0 110 GLU FFF C   1 ? 26 
ATOM   6835 O O   . GLU F 3 110 ? -18.305 3.107   29.893  1.000 45.368  0 110 GLU FFF O   1 ? 26 
ATOM   6836 C CB  . GLU F 3 110 ? -16.895 0.828   31.152  1.000 44.022  0 110 GLU FFF CB  1 ? 26 
ATOM   6837 C CG  . GLU F 3 110 ? -16.784 -0.154  32.303  1.000 46.523  0 110 GLU FFF CG  1 ? 26 
ATOM   6838 C CD  . GLU F 3 110 ? -15.650 0.120   33.273  1.000 48.755  0 110 GLU FFF CD  1 ? 26 
ATOM   6839 O OE1 . GLU F 3 110 ? -14.545 0.437   32.790  1.000 49.086  0 110 GLU FFF OE1 1 ? 26 
ATOM   6840 O OE2 . GLU F 3 110 ? -15.875 0.012   34.509  1.000 51.302  0 110 GLU FFF OE2 1 ? 26 
ATOM   6841 N N   . TYR F 3 111 ? -18.668 1.664   28.183  1.000 43.276  0 111 TYR FFF N   1 ? 26 
ATOM   6842 C CA  . TYR F 3 111 ? -18.879 2.722   27.159  1.000 43.037  0 111 TYR FFF CA  1 ? 26 
ATOM   6843 C C   . TYR F 3 111 ? -20.248 3.374   27.390  1.000 43.987  0 111 TYR FFF C   1 ? 26 
ATOM   6844 O O   . TYR F 3 111 ? -21.226 2.647   27.636  1.000 45.970  0 111 TYR FFF O   1 ? 26 
ATOM   6845 C CB  . TYR F 3 111 ? -18.738 2.175   25.735  1.000 42.441  0 111 TYR FFF CB  1 ? 26 
ATOM   6846 C CG  . TYR F 3 111 ? -17.326 2.137   25.204  1.000 40.153  0 111 TYR FFF CG  1 ? 26 
ATOM   6847 C CD1 . TYR F 3 111 ? -16.525 3.267   25.235  1.000 40.150  0 111 TYR FFF CD1 1 ? 26 
ATOM   6848 C CD2 . TYR F 3 111 ? -16.797 0.984   24.643  1.000 39.605  0 111 TYR FFF CD2 1 ? 26 
ATOM   6849 C CE1 . TYR F 3 111 ? -15.229 3.249   24.746  1.000 39.724  0 111 TYR FFF CE1 1 ? 26 
ATOM   6850 C CE2 . TYR F 3 111 ? -15.503 0.950   24.150  1.000 39.447  0 111 TYR FFF CE2 1 ? 26 
ATOM   6851 C CZ  . TYR F 3 111 ? -14.714 2.087   24.204  1.000 39.192  0 111 TYR FFF CZ  1 ? 26 
ATOM   6852 O OH  . TYR F 3 111 ? -13.436 2.073   23.726  1.000 39.196  0 111 TYR FFF OH  1 ? 26 
ATOM   6853 N N   . THR F 3 112 ? -20.288 4.708   27.358  1.000 44.878  0 112 THR FFF N   1 ? 26 
ATOM   6854 C CA  . THR F 3 112 ? -21.521 5.537   27.304  1.000 46.979  0 112 THR FFF CA  1 ? 26 
ATOM   6855 C C   . THR F 3 112 ? -21.397 6.523   26.141  1.000 48.291  0 112 THR FFF C   1 ? 26 
ATOM   6856 O O   . THR F 3 112 ? -20.277 6.701   25.624  1.000 46.803  0 112 THR FFF O   1 ? 26 
ATOM   6857 C CB  . THR F 3 112 ? -21.776 6.300   28.608  1.000 47.865  0 112 THR FFF CB  1 ? 26 
ATOM   6858 O OG1 . THR F 3 112 ? -21.002 7.501   28.593  1.000 47.146  0 112 THR FFF OG1 1 ? 26 
ATOM   6859 C CG2 . THR F 3 112 ? -21.453 5.482   29.837  1.000 48.918  0 112 THR FFF CG2 1 ? 26 
ATOM   6860 N N   . GLU F 3 113 ? -22.513 7.144   25.762  1.000 51.870  0 113 GLU FFF N   1 ? 26 
ATOM   6861 C CA  . GLU F 3 113 ? -22.592 8.087   24.618  1.000 54.907  0 113 GLU FFF CA  1 ? 26 
ATOM   6862 C C   . GLU F 3 113 ? -21.597 9.240   24.842  1.000 52.160  0 113 GLU FFF C   1 ? 26 
ATOM   6863 O O   . GLU F 3 113 ? -21.058 9.749   23.837  1.000 51.556  0 113 GLU FFF O   1 ? 26 
ATOM   6864 C CB  . GLU F 3 113 ? -24.049 8.517   24.415  1.000 59.965  0 113 GLU FFF CB  1 ? 26 
ATOM   6865 C CG  . GLU F 3 113 ? -24.254 10.016  24.278  1.000 64.965  0 113 GLU FFF CG  1 ? 26 
ATOM   6866 C CD  . GLU F 3 113 ? -24.551 10.698  25.601  1.000 69.146  0 113 GLU FFF CD  1 ? 26 
ATOM   6867 O OE1 . GLU F 3 113 ? -25.608 10.393  26.182  1.000 73.573  0 113 GLU FFF OE1 1 ? 26 
ATOM   6868 O OE2 . GLU F 3 113 ? -23.725 11.516  26.048  1.000 67.993  0 113 GLU FFF OE2 1 ? 26 
ATOM   6869 N N   . ALA F 3 114 ? -21.330 9.607   26.102  1.000 47.966  0 114 ALA FFF N   1 ? 26 
ATOM   6870 C CA  . ALA F 3 114 ? -20.403 10.696  26.495  1.000 46.466  0 114 ALA FFF CA  1 ? 26 
ATOM   6871 C C   . ALA F 3 114 ? -18.983 10.427  25.975  1.000 44.488  0 114 ALA FFF C   1 ? 26 
ATOM   6872 O O   . ALA F 3 114 ? -18.236 11.401  25.804  1.000 44.162  0 114 ALA FFF O   1 ? 26 
ATOM   6873 C CB  . ALA F 3 114 ? -20.405 10.861  27.994  1.000 47.028  0 114 ALA FFF CB  1 ? 26 
ATOM   6874 N N   . ASP F 3 115 ? -18.622 9.163   25.737  1.000 42.880  0 115 ASP FFF N   1 ? 26 
ATOM   6875 C CA  . ASP F 3 115 ? -17.271 8.758   25.268  1.000 42.090  0 115 ASP FFF CA  1 ? 26 
ATOM   6876 C C   . ASP F 3 115 ? -17.120 9.024   23.761  1.000 42.772  0 115 ASP FFF C   1 ? 26 
ATOM   6877 O O   . ASP F 3 115 ? -15.966 9.047   23.285  1.000 42.065  0 115 ASP FFF O   1 ? 26 
ATOM   6878 C CB  . ASP F 3 115 ? -17.018 7.277   25.556  1.000 41.798  0 115 ASP FFF CB  1 ? 26 
ATOM   6879 C CG  . ASP F 3 115 ? -17.088 6.908   27.024  1.000 42.806  0 115 ASP FFF CG  1 ? 26 
ATOM   6880 O OD1 . ASP F 3 115 ? -16.672 7.735   27.866  1.000 43.793  0 115 ASP FFF OD1 1 ? 26 
ATOM   6881 O OD2 . ASP F 3 115 ? -17.538 5.785   27.313  1.000 45.029  0 115 ASP FFF OD2 1 ? 26 
ATOM   6882 N N   . PHE F 3 116 ? -18.229 9.201   23.033  1.000 42.117  0 116 PHE FFF N   1 ? 26 
ATOM   6883 C CA  . PHE F 3 116 ? -18.255 9.193   21.549  1.000 41.705  0 116 PHE FFF CA  1 ? 26 
ATOM   6884 C C   . PHE F 3 116 ? -18.473 10.610  21.011  1.000 43.373  0 116 PHE FFF C   1 ? 26 
ATOM   6885 O O   . PHE F 3 116 ? -19.085 11.443  21.698  1.000 45.619  0 116 PHE FFF O   1 ? 26 
ATOM   6886 C CB  . PHE F 3 116 ? -19.316 8.214   21.044  1.000 40.019  0 116 PHE FFF CB  1 ? 26 
ATOM   6887 C CG  . PHE F 3 116 ? -18.981 6.767   21.303  1.000 38.661  0 116 PHE FFF CG  1 ? 26 
ATOM   6888 C CD1 . PHE F 3 116 ? -19.119 6.219   22.565  1.000 38.859  0 116 PHE FFF CD1 1 ? 26 
ATOM   6889 C CD2 . PHE F 3 116 ? -18.496 5.958   20.291  1.000 37.702  0 116 PHE FFF CD2 1 ? 26 
ATOM   6890 C CE1 . PHE F 3 116 ? -18.791 4.892   22.801  1.000 38.472  0 116 PHE FFF CE1 1 ? 26 
ATOM   6891 C CE2 . PHE F 3 116 ? -18.176 4.631   20.524  1.000 37.065  0 116 PHE FFF CE2 1 ? 26 
ATOM   6892 C CZ  . PHE F 3 116 ? -18.330 4.097   21.777  1.000 37.438  0 116 PHE FFF CZ  1 ? 26 
ATOM   6893 N N   . GLY F 3 117 ? -17.959 10.851  19.801  1.000 44.583  0 117 GLY FFF N   1 ? 26 
ATOM   6894 C CA  . GLY F 3 117 ? -18.099 12.103  19.036  1.000 45.926  0 117 GLY FFF CA  1 ? 26 
ATOM   6895 C C   . GLY F 3 117 ? -18.248 11.816  17.552  1.000 46.474  0 117 GLY FFF C   1 ? 26 
ATOM   6896 O O   . GLY F 3 117 ? -18.422 10.628  17.192  1.000 46.196  0 117 GLY FFF O   1 ? 26 
ATOM   6897 N N   . SER F 3 118 ? -18.183 12.857  16.717  1.000 47.581  0 118 SER FFF N   1 ? 26 
ATOM   6898 C CA  . SER F 3 118 ? -18.408 12.774  15.252  1.000 48.804  0 118 SER FFF CA  1 ? 26 
ATOM   6899 C C   . SER F 3 118 ? -19.702 11.993  14.984  1.000 47.514  0 118 SER FFF C   1 ? 26 
ATOM   6900 O O   . SER F 3 118 ? -19.688 11.078  14.142  1.000 47.848  0 118 SER FFF O   1 ? 26 
ATOM   6901 C CB  . SER F 3 118 ? -17.224 12.145  14.562  1.000 49.756  0 118 SER FFF CB  1 ? 26 
ATOM   6902 O OG  . SER F 3 118 ? -16.069 12.953  14.700  1.000 51.362  0 118 SER FFF OG  1 ? 26 
ATOM   6903 N N   . TRP F 3 119 ? -20.775 12.335  15.697  1.000 45.755  0 119 TRP FFF N   1 ? 26 
ATOM   6904 C CA  . TRP F 3 119 ? -22.101 11.673  15.577  1.000 45.390  0 119 TRP FFF CA  1 ? 26 
ATOM   6905 C C   . TRP F 3 119 ? -22.608 11.788  14.139  1.000 46.254  0 119 TRP FFF C   1 ? 26 
ATOM   6906 O O   . TRP F 3 119 ? -22.635 12.912  13.615  1.000 45.525  0 119 TRP FFF O   1 ? 26 
ATOM   6907 C CB  . TRP F 3 119 ? -23.106 12.281  16.561  1.000 45.600  0 119 TRP FFF CB  1 ? 26 
ATOM   6908 C CG  . TRP F 3 119 ? -22.796 11.961  17.987  1.000 44.977  0 119 TRP FFF CG  1 ? 26 
ATOM   6909 C CD1 . TRP F 3 119 ? -22.107 12.737  18.874  1.000 45.859  0 119 TRP FFF CD1 1 ? 26 
ATOM   6910 C CD2 . TRP F 3 119 ? -23.142 10.755  18.687  1.000 43.485  0 119 TRP FFF CD2 1 ? 26 
ATOM   6911 N NE1 . TRP F 3 119 ? -22.011 12.102  20.080  1.000 45.289  0 119 TRP FFF NE1 1 ? 26 
ATOM   6912 C CE2 . TRP F 3 119 ? -22.636 10.887  19.997  1.000 43.936  0 119 TRP FFF CE2 1 ? 26 
ATOM   6913 C CE3 . TRP F 3 119 ? -23.827 9.585   18.343  1.000 42.942  0 119 TRP FFF CE3 1 ? 26 
ATOM   6914 C CZ2 . TRP F 3 119 ? -22.803 9.897   20.960  1.000 42.808  0 119 TRP FFF CZ2 1 ? 26 
ATOM   6915 C CZ3 . TRP F 3 119 ? -23.986 8.601   19.296  1.000 43.457  0 119 TRP FFF CZ3 1 ? 26 
ATOM   6916 C CH2 . TRP F 3 119 ? -23.485 8.761   20.589  1.000 42.837  0 119 TRP FFF CH2 1 ? 26 
ATOM   6917 N N   . GLY F 3 120 ? -22.994 10.662  13.542  1.000 46.484  0 120 GLY FFF N   1 ? 26 
ATOM   6918 C CA  . GLY F 3 120 ? -23.784 10.633  12.299  1.000 50.544  0 120 GLY FFF CA  1 ? 26 
ATOM   6919 C C   . GLY F 3 120 ? -25.158 11.240  12.512  1.000 52.607  0 120 GLY FFF C   1 ? 26 
ATOM   6920 O O   . GLY F 3 120 ? -25.600 11.308  13.666  1.000 53.122  0 120 GLY FFF O   1 ? 26 
ATOM   6921 N N   . GLN F 3 121 ? -25.798 11.701  11.438  1.000 56.501  0 121 GLN FFF N   1 ? 26 
ATOM   6922 C CA  . GLN F 3 121 ? -27.218 12.139  11.461  1.000 58.800  0 121 GLN FFF CA  1 ? 26 
ATOM   6923 C C   . GLN F 3 121 ? -28.057 10.881  11.724  1.000 59.126  0 121 GLN FFF C   1 ? 26 
ATOM   6924 O O   . GLN F 3 121 ? -27.748 9.825   11.148  1.000 64.037  0 121 GLN FFF O   1 ? 26 
ATOM   6925 C CB  . GLN F 3 121 ? -27.564 12.929  10.192  1.000 62.489  0 121 GLN FFF CB  1 ? 26 
ATOM   6926 C CG  . GLN F 3 121 ? -27.950 12.104  8.968   1.000 65.132  0 121 GLN FFF CG  1 ? 26 
ATOM   6927 C CD  . GLN F 3 121 ? -26.810 11.318  8.360   1.000 66.364  0 121 GLN FFF CD  1 ? 26 
ATOM   6928 O OE1 . GLN F 3 121 ? -25.638 11.468  8.718   1.000 65.294  0 121 GLN FFF OE1 1 ? 26 
ATOM   6929 N NE2 . GLN F 3 121 ? -27.154 10.462  7.412   1.000 66.470  0 121 GLN FFF NE2 1 ? 26 
ATOM   6930 N N   . GLY F 3 122 ? -29.029 10.961  12.630  1.000 57.492  0 122 GLY FFF N   1 ? 26 
ATOM   6931 C CA  . GLY F 3 122 ? -29.853 9.802   13.024  1.000 57.788  0 122 GLY FFF CA  1 ? 26 
ATOM   6932 C C   . GLY F 3 122 ? -30.622 9.227   11.842  1.000 58.336  0 122 GLY FFF C   1 ? 26 
ATOM   6933 O O   . GLY F 3 122 ? -30.995 10.005  10.951  1.000 62.421  0 122 GLY FFF O   1 ? 26 
ATOM   6934 N N   . THR F 3 123 ? -30.841 7.911   11.829  1.000 55.640  0 123 THR FFF N   1 ? 26 
ATOM   6935 C CA  . THR F 3 123 ? -31.717 7.200   10.859  1.000 56.186  0 123 THR FFF CA  1 ? 26 
ATOM   6936 C C   . THR F 3 123 ? -32.818 6.470   11.646  1.000 56.403  0 123 THR FFF C   1 ? 26 
ATOM   6937 O O   . THR F 3 123 ? -32.484 5.771   12.622  1.000 55.779  0 123 THR FFF O   1 ? 26 
ATOM   6938 C CB  . THR F 3 123 ? -30.897 6.288   9.936   1.000 56.203  0 123 THR FFF CB  1 ? 26 
ATOM   6939 O OG1 . THR F 3 123 ? -31.762 5.800   8.912   1.000 58.450  0 123 THR FFF OG1 1 ? 26 
ATOM   6940 C CG2 . THR F 3 123 ? -30.272 5.106   10.641  1.000 55.741  0 123 THR FFF CG2 1 ? 26 
ATOM   6941 N N   . GLN F 3 124 ? -34.084 6.661   11.255  1.000 56.844  0 124 GLN FFF N   1 ? 26 
ATOM   6942 C CA  . GLN F 3 124 ? -35.273 6.119   11.966  1.000 56.529  0 124 GLN FFF CA  1 ? 26 
ATOM   6943 C C   . GLN F 3 124 ? -35.421 4.628   11.642  1.000 56.085  0 124 GLN FFF C   1 ? 26 
ATOM   6944 O O   . GLN F 3 124 ? -35.334 4.265   10.458  1.000 55.911  0 124 GLN FFF O   1 ? 26 
ATOM   6945 C CB  . GLN F 3 124 ? -36.531 6.905   11.585  1.000 58.249  0 124 GLN FFF CB  1 ? 26 
ATOM   6946 C CG  . GLN F 3 124 ? -37.803 6.434   12.283  1.000 59.241  0 124 GLN FFF CG  1 ? 26 
ATOM   6947 C CD  . GLN F 3 124 ? -37.780 6.642   13.778  1.000 59.027  0 124 GLN FFF CD  1 ? 26 
ATOM   6948 O OE1 . GLN F 3 124 ? -37.858 5.692   14.556  1.000 59.069  0 124 GLN FFF OE1 1 ? 26 
ATOM   6949 N NE2 . GLN F 3 124 ? -37.682 7.894   14.195  1.000 59.132  0 124 GLN FFF NE2 1 ? 26 
ATOM   6950 N N   . VAL F 3 125 ? -35.610 3.805   12.676  1.000 56.527  0 125 VAL FFF N   1 ? 26 
ATOM   6951 C CA  . VAL F 3 125 ? -35.955 2.357   12.579  1.000 56.788  0 125 VAL FFF CA  1 ? 26 
ATOM   6952 C C   . VAL F 3 125 ? -37.286 2.160   13.308  1.000 58.653  0 125 VAL FFF C   1 ? 26 
ATOM   6953 O O   . VAL F 3 125 ? -37.364 2.533   14.496  1.000 57.581  0 125 VAL FFF O   1 ? 26 
ATOM   6954 C CB  . VAL F 3 125 ? -34.847 1.469   13.178  1.000 56.031  0 125 VAL FFF CB  1 ? 26 
ATOM   6955 C CG1 . VAL F 3 125 ? -35.192 -0.009  13.089  1.000 56.810  0 125 VAL FFF CG1 1 ? 26 
ATOM   6956 C CG2 . VAL F 3 125 ? -33.496 1.741   12.533  1.000 55.267  0 125 VAL FFF CG2 1 ? 26 
ATOM   6957 N N   . THR F 3 126 ? -38.291 1.617   12.613  1.000 61.010  0 126 THR FFF N   1 ? 26 
ATOM   6958 C CA  . THR F 3 126 ? -39.667 1.387   13.128  1.000 62.567  0 126 THR FFF CA  1 ? 26 
ATOM   6959 C C   . THR F 3 126 ? -40.050 -0.081  12.915  1.000 63.892  0 126 THR FFF C   1 ? 26 
ATOM   6960 O O   . THR F 3 126 ? -39.961 -0.551  11.768  1.000 62.321  0 126 THR FFF O   1 ? 26 
ATOM   6961 C CB  . THR F 3 126 ? -40.662 2.336   12.453  1.000 64.713  0 126 THR FFF CB  1 ? 26 
ATOM   6962 O OG1 . THR F 3 126 ? -40.142 3.659   12.594  1.000 64.334  0 126 THR FFF OG1 1 ? 26 
ATOM   6963 C CG2 . THR F 3 126 ? -42.058 2.256   13.036  1.000 66.411  0 126 THR FFF CG2 1 ? 26 
ATOM   6964 N N   . VAL F 3 127 ? -40.464 -0.760  13.991  1.000 65.903  0 127 VAL FFF N   1 ? 26 
ATOM   6965 C CA  . VAL F 3 127 ? -40.897 -2.189  13.997  1.000 68.724  0 127 VAL FFF CA  1 ? 26 
ATOM   6966 C C   . VAL F 3 127 ? -42.324 -2.252  14.556  1.000 72.877  0 127 VAL FFF C   1 ? 26 
ATOM   6967 O O   . VAL F 3 127 ? -42.528 -1.754  15.684  1.000 72.566  0 127 VAL FFF O   1 ? 26 
ATOM   6968 C CB  . VAL F 3 127 ? -39.926 -3.058  14.817  1.000 66.803  0 127 VAL FFF CB  1 ? 26 
ATOM   6969 C CG1 . VAL F 3 127 ? -40.254 -4.537  14.692  1.000 68.735  0 127 VAL FFF CG1 1 ? 26 
ATOM   6970 C CG2 . VAL F 3 127 ? -38.477 -2.794  14.438  1.000 64.235  0 127 VAL FFF CG2 1 ? 26 
ATOM   6971 N N   . SER F 3 128 ? -43.257 -2.837  13.791  1.000 76.892  0 128 SER FFF N   1 ? 26 
ATOM   6972 C CA  . SER F 3 128 ? -44.725 -2.820  14.045  1.000 81.064  0 128 SER FFF CA  1 ? 26 
ATOM   6973 C C   . SER F 3 128 ? -45.309 -4.237  13.975  1.000 84.601  0 128 SER FFF C   1 ? 26 
ATOM   6974 O O   . SER F 3 128 ? -44.541 -5.182  13.711  1.000 85.061  0 128 SER FFF O   1 ? 26 
ATOM   6975 C CB  . SER F 3 128 ? -45.419 -1.908  13.065  1.000 81.983  0 128 SER FFF CB  1 ? 26 
ATOM   6976 O OG  . SER F 3 128 ? -44.839 -0.613  13.082  1.000 81.580  0 128 SER FFF OG  1 ? 26 
ATOM   6977 N N   . SER F 3 129 ? -46.623 -4.361  14.208  1.000 89.271  0 129 SER FFF N   1 ? 26 
ATOM   6978 C CA  . SER F 3 129 ? -47.423 -5.609  14.073  1.000 91.470  0 129 SER FFF CA  1 ? 26 
ATOM   6979 C C   . SER F 3 129 ? -48.807 -5.279  13.502  1.000 93.967  0 129 SER FFF C   1 ? 26 
ATOM   6980 O O   . SER F 3 129 ? -48.935 -4.922  12.331  1.000 94.390  0 129 SER FFF O   1 ? 26 
ATOM   6981 C CB  . SER F 3 129 ? -47.533 -6.328  15.392  1.000 92.499  0 129 SER FFF CB  1 ? 26 
ATOM   6982 O OG  . SER F 3 129 ? -46.248 -6.684  15.883  1.000 90.767  0 129 SER FFF OG  1 ? 26 
HETATM 6983 C C1  . NAG G 4 .   ? 1.585   12.551  4.001   1.000 42.331  0 601 NAG BBB C1  1 ? ?  
HETATM 6984 C C2  . NAG G 4 .   ? 1.701   11.038  3.894   1.000 47.570  0 601 NAG BBB C2  1 ? ?  
HETATM 6985 C C3  . NAG G 4 .   ? 0.754   10.533  2.802   1.000 48.879  0 601 NAG BBB C3  1 ? ?  
HETATM 6986 C C4  . NAG G 4 .   ? -0.668  11.038  3.062   1.000 48.783  0 601 NAG BBB C4  1 ? ?  
HETATM 6987 C C5  . NAG G 4 .   ? -0.645  12.559  3.157   1.000 50.977  0 601 NAG BBB C5  1 ? ?  
HETATM 6988 C C6  . NAG G 4 .   ? -2.019  13.182  3.391   1.000 51.089  0 601 NAG BBB C6  1 ? ?  
HETATM 6989 C C7  . NAG G 4 .   ? 3.753   9.716   4.211   1.000 50.208  0 601 NAG BBB C7  1 ? ?  
HETATM 6990 C C8  . NAG G 4 .   ? 5.159   9.491   3.729   1.000 53.514  0 601 NAG BBB C8  1 ? ?  
HETATM 6991 N N2  . NAG G 4 .   ? 3.083   10.696  3.600   1.000 47.876  0 601 NAG BBB N2  1 ? ?  
HETATM 6992 O O3  . NAG G 4 .   ? 0.784   9.101   2.741   1.000 50.753  0 601 NAG BBB O3  1 ? ?  
HETATM 6993 O O4  . NAG G 4 .   ? -1.550  10.634  2.012   1.000 48.129  0 601 NAG BBB O4  1 ? ?  
HETATM 6994 O O5  . NAG G 4 .   ? 0.225   12.923  4.227   1.000 47.299  0 601 NAG BBB O5  1 ? ?  
HETATM 6995 O O6  . NAG G 4 .   ? -2.558  12.724  4.633   1.000 51.796  0 601 NAG BBB O6  1 ? ?  
HETATM 6996 O O7  . NAG G 4 .   ? 3.277   9.025   5.097   1.000 50.453  0 601 NAG BBB O7  1 ? ?  
HETATM 6997 C C1  . NAG H 4 .   ? 15.957  18.699  24.713  1.000 73.695  0 601 NAG EEE C1  1 ? ?  
HETATM 6998 C C2  . NAG H 4 .   ? 17.445  18.369  24.798  1.000 81.302  0 601 NAG EEE C2  1 ? ?  
HETATM 6999 C C3  . NAG H 4 .   ? 18.113  19.140  25.933  1.000 82.391  0 601 NAG EEE C3  1 ? ?  
HETATM 7000 C C4  . NAG H 4 .   ? 17.804  20.626  25.840  1.000 81.148  0 601 NAG EEE C4  1 ? ?  
HETATM 7001 C C5  . NAG H 4 .   ? 16.306  20.861  25.684  1.000 81.705  0 601 NAG EEE C5  1 ? ?  
HETATM 7002 C C6  . NAG H 4 .   ? 16.019  22.352  25.523  1.000 81.165  0 601 NAG EEE C6  1 ? ?  
HETATM 7003 C C7  . NAG H 4 .   ? 18.593  16.254  24.351  1.000 89.963  0 601 NAG EEE C7  1 ? ?  
HETATM 7004 C C8  . NAG H 4 .   ? 18.727  14.808  24.731  1.000 90.675  0 601 NAG EEE C8  1 ? ?  
HETATM 7005 N N2  . NAG H 4 .   ? 17.653  16.945  25.004  1.000 86.342  0 601 NAG EEE N2  1 ? ?  
HETATM 7006 O O3  . NAG H 4 .   ? 19.532  18.953  25.888  1.000 78.304  0 601 NAG EEE O3  1 ? ?  
HETATM 7007 O O4  . NAG H 4 .   ? 18.279  21.279  27.021  1.000 82.219  0 601 NAG EEE O4  1 ? ?  
HETATM 7008 O O5  . NAG H 4 .   ? 15.822  20.118  24.559  1.000 77.359  0 601 NAG EEE O5  1 ? ?  
HETATM 7009 O O6  . NAG H 4 .   ? 14.705  22.559  24.997  1.000 86.507  0 601 NAG EEE O6  1 ? ?  
HETATM 7010 O O7  . NAG H 4 .   ? 19.317  16.752  23.503  1.000 97.224  0 601 NAG EEE O7  1 ? ?  
HETATM 7011 O O1  . MES I 5 .   ? 17.798  -9.641  23.993  1.000 85.552  0 602 MES EEE O1  1 ? ?  
HETATM 7012 C C2  . MES I 5 .   ? 16.632  -10.450 24.055  1.000 84.773  0 602 MES EEE C2  1 ? ?  
HETATM 7013 C C3  . MES I 5 .   ? 15.730  -10.204 22.872  1.000 85.550  0 602 MES EEE C3  1 ? ?  
HETATM 7014 N N4  . MES I 5 .   ? 15.341  -8.760  22.802  1.000 82.496  0 602 MES EEE N4  1 ? ?  
HETATM 7015 C C5  . MES I 5 .   ? 16.575  -7.912  22.813  1.000 80.620  0 602 MES EEE C5  1 ? ?  
HETATM 7016 C C6  . MES I 5 .   ? 17.443  -8.265  23.996  1.000 86.062  0 602 MES EEE C6  1 ? ?  
HETATM 7017 C C7  . MES I 5 .   ? 14.480  -8.483  21.602  1.000 85.136  0 602 MES EEE C7  1 ? ?  
HETATM 7018 C C8  . MES I 5 .   ? 14.006  -7.044  21.518  1.000 87.408  0 602 MES EEE C8  1 ? ?  
HETATM 7019 S S   . MES I 5 .   ? 12.537  -6.851  20.530  1.000 96.008  0 602 MES EEE S   1 ? ?  
HETATM 7020 O O1S . MES I 5 .   ? 12.913  -7.175  19.182  1.000 85.411  0 602 MES EEE O1S 1 ? ?  
HETATM 7021 O O2S . MES I 5 .   ? 12.136  -5.480  20.681  1.000 80.380  0 602 MES EEE O2S 1 ? ?  
HETATM 7022 O O3S . MES I 5 .   ? 11.570  -7.767  21.065  1.000 106.449 0 602 MES EEE O3S 1 ? ?  
HETATM 7023 O O   . HOH J 6 .   ? 19.192  5.220   -29.673 1.000 47.688  0 201 HOH AAA O   1 ? ?  
HETATM 7024 O O   . HOH J 6 .   ? 24.985  5.227   -28.462 1.000 53.037  0 202 HOH AAA O   1 ? ?  
HETATM 7025 O O   . HOH J 6 .   ? 0.938   8.046   -34.321 1.000 52.005  0 203 HOH AAA O   1 ? ?  
HETATM 7026 O O   . HOH J 6 .   ? 7.394   6.936   -13.158 1.000 36.454  0 204 HOH AAA O   1 ? ?  
HETATM 7027 O O   . HOH J 6 .   ? 14.678  4.944   -17.257 1.000 40.862  0 205 HOH AAA O   1 ? ?  
HETATM 7028 O O   . HOH J 6 .   ? 2.724   -0.489  -21.216 1.000 43.248  0 206 HOH AAA O   1 ? ?  
HETATM 7029 O O   . HOH J 6 .   ? 13.316  -0.456  -20.998 1.000 54.754  0 207 HOH AAA O   1 ? ?  
HETATM 7030 O O   . HOH J 6 .   ? -8.506  24.420  -38.971 1.000 55.992  0 208 HOH AAA O   1 ? ?  
HETATM 7031 O O   . HOH J 6 .   ? 7.062   18.783  -38.082 1.000 57.066  0 209 HOH AAA O   1 ? ?  
HETATM 7032 O O   . HOH J 6 .   ? 2.700   4.579   -13.200 1.000 15.879  0 210 HOH AAA O   1 ? ?  
HETATM 7033 O O   . HOH J 6 .   ? 7.885   23.656  -17.368 1.000 37.634  0 211 HOH AAA O   1 ? ?  
HETATM 7034 O O   . HOH J 6 .   ? 4.551   11.317  -39.145 1.000 50.865  0 212 HOH AAA O   1 ? ?  
HETATM 7035 O O   . HOH J 6 .   ? 20.447  5.867   -20.430 1.000 43.711  0 213 HOH AAA O   1 ? ?  
HETATM 7036 O O   . HOH J 6 .   ? -2.700  20.592  -13.173 1.000 58.674  0 214 HOH AAA O   1 ? ?  
HETATM 7037 O O   . HOH J 6 .   ? 10.289  18.382  -37.704 1.000 61.532  0 215 HOH AAA O   1 ? ?  
HETATM 7038 O O   . HOH J 6 .   ? 10.753  22.167  -35.220 1.000 55.761  0 216 HOH AAA O   1 ? ?  
HETATM 7039 O O   . HOH K 6 .   ? 21.944  3.078   -1.214  1.000 35.255  0 701 HOH BBB O   1 ? ?  
HETATM 7040 O O   . HOH K 6 .   ? 7.214   19.859  -10.699 1.000 34.220  0 702 HOH BBB O   1 ? ?  
HETATM 7041 O O   . HOH K 6 .   ? 18.425  22.838  9.675   1.000 44.379  0 703 HOH BBB O   1 ? ?  
HETATM 7042 O O   . HOH K 6 .   ? 15.286  14.313  7.118   1.000 33.653  0 704 HOH BBB O   1 ? ?  
HETATM 7043 O O   . HOH K 6 .   ? 30.159  19.742  -6.821  1.000 42.945  0 705 HOH BBB O   1 ? ?  
HETATM 7044 O O   . HOH K 6 .   ? 27.557  41.955  2.816   1.000 32.225  0 706 HOH BBB O   1 ? ?  
HETATM 7045 O O   . HOH K 6 .   ? 28.447  36.403  10.987  1.000 36.445  0 707 HOH BBB O   1 ? ?  
HETATM 7046 O O   . HOH K 6 .   ? 3.773   14.572  -9.665  1.000 35.161  0 708 HOH BBB O   1 ? ?  
HETATM 7047 O O   . HOH K 6 .   ? 18.128  12.938  -9.020  1.000 35.856  0 709 HOH BBB O   1 ? ?  
HETATM 7048 O O   . HOH K 6 .   ? 26.408  25.036  3.281   1.000 29.687  0 710 HOH BBB O   1 ? ?  
HETATM 7049 O O   . HOH K 6 .   ? 20.445  10.204  2.455   1.000 34.448  0 711 HOH BBB O   1 ? ?  
HETATM 7050 O O   . HOH K 6 .   ? 38.981  40.273  2.231   1.000 33.674  0 712 HOH BBB O   1 ? ?  
HETATM 7051 O O   . HOH K 6 .   ? 5.907   18.647  -8.230  1.000 38.366  0 713 HOH BBB O   1 ? ?  
HETATM 7052 O O   . HOH K 6 .   ? 44.222  37.275  5.276   1.000 39.507  0 714 HOH BBB O   1 ? ?  
HETATM 7053 O O   . HOH K 6 .   ? 15.105  33.449  -5.016  1.000 30.349  0 715 HOH BBB O   1 ? ?  
HETATM 7054 O O   . HOH K 6 .   ? 36.238  38.815  -4.700  1.000 43.352  0 716 HOH BBB O   1 ? ?  
HETATM 7055 O O   . HOH K 6 .   ? 25.949  22.456  3.980   1.000 30.263  0 717 HOH BBB O   1 ? ?  
HETATM 7056 O O   . HOH K 6 .   ? 35.711  36.550  8.329   1.000 35.190  0 718 HOH BBB O   1 ? ?  
HETATM 7057 O O   . HOH K 6 .   ? 18.704  28.569  9.083   1.000 48.253  0 719 HOH BBB O   1 ? ?  
HETATM 7058 O O   . HOH K 6 .   ? 13.492  -1.834  3.980   1.000 51.635  0 720 HOH BBB O   1 ? ?  
HETATM 7059 O O   . HOH K 6 .   ? 5.634   18.285  2.782   1.000 43.876  0 721 HOH BBB O   1 ? ?  
HETATM 7060 O O   . HOH K 6 .   ? 12.774  31.369  1.515   1.000 34.534  0 722 HOH BBB O   1 ? ?  
HETATM 7061 O O   . HOH K 6 .   ? 22.593  39.743  -1.424  1.000 32.285  0 723 HOH BBB O   1 ? ?  
HETATM 7062 O O   . HOH K 6 .   ? 18.926  -5.812  1.498   1.000 46.735  0 724 HOH BBB O   1 ? ?  
HETATM 7063 O O   . HOH K 6 .   ? 38.093  37.718  7.628   1.000 35.697  0 725 HOH BBB O   1 ? ?  
HETATM 7064 O O   . HOH K 6 .   ? 31.043  30.131  3.674   1.000 34.088  0 726 HOH BBB O   1 ? ?  
HETATM 7065 O O   . HOH K 6 .   ? 14.065  19.142  6.508   1.000 37.015  0 727 HOH BBB O   1 ? ?  
HETATM 7066 O O   . HOH K 6 .   ? 16.717  26.257  1.707   1.000 35.173  0 728 HOH BBB O   1 ? ?  
HETATM 7067 O O   . HOH K 6 .   ? 26.250  17.133  1.314   1.000 41.779  0 729 HOH BBB O   1 ? ?  
HETATM 7068 O O   . HOH K 6 .   ? 17.338  22.736  -14.163 1.000 37.736  0 730 HOH BBB O   1 ? ?  
HETATM 7069 O O   . HOH K 6 .   ? 3.543   4.096   14.258  1.000 54.211  0 731 HOH BBB O   1 ? ?  
HETATM 7070 O O   . HOH K 6 .   ? 32.099  32.176  5.096   1.000 35.627  0 732 HOH BBB O   1 ? ?  
HETATM 7071 O O   . HOH K 6 .   ? 16.294  21.316  -11.918 1.000 36.732  0 733 HOH BBB O   1 ? ?  
HETATM 7072 O O   . HOH K 6 .   ? 31.260  15.360  -8.856  1.000 46.389  0 734 HOH BBB O   1 ? ?  
HETATM 7073 O O   . HOH K 6 .   ? 2.946   9.701   0.207   1.000 47.365  0 735 HOH BBB O   1 ? ?  
HETATM 7074 O O   . HOH K 6 .   ? 1.238   27.082  -7.359  1.000 52.414  0 736 HOH BBB O   1 ? ?  
HETATM 7075 O O   . HOH K 6 .   ? 18.323  -3.425  16.864  1.000 38.945  0 737 HOH BBB O   1 ? ?  
HETATM 7076 O O   . HOH K 6 .   ? 29.960  48.091  6.334   1.000 35.501  0 738 HOH BBB O   1 ? ?  
HETATM 7077 O O   . HOH K 6 .   ? 12.041  26.464  7.083   1.000 52.848  0 739 HOH BBB O   1 ? ?  
HETATM 7078 O O   . HOH K 6 .   ? 6.849   3.638   6.959   1.000 43.414  0 740 HOH BBB O   1 ? ?  
HETATM 7079 O O   . HOH K 6 .   ? 19.093  -3.225  -6.136  1.000 41.384  0 741 HOH BBB O   1 ? ?  
HETATM 7080 O O   . HOH K 6 .   ? 34.653  28.303  3.203   1.000 52.218  0 742 HOH BBB O   1 ? ?  
HETATM 7081 O O   . HOH K 6 .   ? 8.443   21.120  10.817  1.000 38.188  0 743 HOH BBB O   1 ? ?  
HETATM 7082 O O   . HOH K 6 .   ? 8.838   -9.260  20.794  1.000 39.774  0 744 HOH BBB O   1 ? ?  
HETATM 7083 O O   . HOH K 6 .   ? 29.452  -13.952 9.462   1.000 61.733  0 745 HOH BBB O   1 ? ?  
HETATM 7084 O O   . HOH K 6 .   ? 0.338   16.329  4.985   1.000 63.162  0 746 HOH BBB O   1 ? ?  
HETATM 7085 O O   . HOH K 6 .   ? 6.590   19.300  11.517  1.000 49.624  0 747 HOH BBB O   1 ? ?  
HETATM 7086 O O   . HOH K 6 .   ? 29.702  43.722  1.807   1.000 31.677  0 748 HOH BBB O   1 ? ?  
HETATM 7087 O O   . HOH K 6 .   ? 16.957  24.909  8.680   1.000 38.542  0 749 HOH BBB O   1 ? ?  
HETATM 7088 O O   . HOH K 6 .   ? 24.101  0.863   13.018  1.000 45.229  0 750 HOH BBB O   1 ? ?  
HETATM 7089 O O   . HOH K 6 .   ? 24.081  6.935   -0.171  1.000 55.328  0 751 HOH BBB O   1 ? ?  
HETATM 7090 O O   . HOH K 6 .   ? 5.684   -9.932  7.327   1.000 65.734  0 752 HOH BBB O   1 ? ?  
HETATM 7091 O O   . HOH K 6 .   ? 0.240   33.753  1.680   1.000 57.991  0 753 HOH BBB O   1 ? ?  
HETATM 7092 O O   . HOH K 6 .   ? 6.616   29.136  -14.884 1.000 55.347  0 754 HOH BBB O   1 ? ?  
HETATM 7093 O O   . HOH K 6 .   ? 34.973  38.071  10.329  1.000 39.757  0 755 HOH BBB O   1 ? ?  
HETATM 7094 O O   . HOH K 6 .   ? 3.386   36.598  -5.440  1.000 49.991  0 756 HOH BBB O   1 ? ?  
HETATM 7095 O O   . HOH K 6 .   ? 5.653   9.329   10.908  1.000 55.118  0 757 HOH BBB O   1 ? ?  
HETATM 7096 O O   . HOH K 6 .   ? 19.520  -7.711  5.434   1.000 56.636  0 758 HOH BBB O   1 ? ?  
HETATM 7097 O O   . HOH K 6 .   ? 20.058  16.765  11.382  1.000 48.668  0 759 HOH BBB O   1 ? ?  
HETATM 7098 O O   . HOH K 6 .   ? 22.224  27.573  -8.682  1.000 49.651  0 760 HOH BBB O   1 ? ?  
HETATM 7099 O O   . HOH K 6 .   ? 10.677  29.538  -14.459 1.000 38.885  0 761 HOH BBB O   1 ? ?  
HETATM 7100 O O   . HOH K 6 .   ? 16.748  -3.027  -5.134  1.000 35.207  0 762 HOH BBB O   1 ? ?  
HETATM 7101 O O   . HOH K 6 .   ? 23.809  16.314  9.350   1.000 55.174  0 763 HOH BBB O   1 ? ?  
HETATM 7102 O O   . HOH K 6 .   ? 36.492  37.535  12.431  1.000 49.882  0 764 HOH BBB O   1 ? ?  
HETATM 7103 O O   . HOH K 6 .   ? 14.898  37.607  -3.546  1.000 47.951  0 765 HOH BBB O   1 ? ?  
HETATM 7104 O O   . HOH L 6 .   ? 20.475  53.382  25.238  1.000 43.402  0 201 HOH CCC O   1 ? ?  
HETATM 7105 O O   . HOH L 6 .   ? 14.826  34.707  7.824   1.000 34.950  0 202 HOH CCC O   1 ? ?  
HETATM 7106 O O   . HOH L 6 .   ? 16.246  38.729  21.029  1.000 35.198  0 203 HOH CCC O   1 ? ?  
HETATM 7107 O O   . HOH L 6 .   ? 19.612  40.424  15.283  1.000 46.340  0 204 HOH CCC O   1 ? ?  
HETATM 7108 O O   . HOH L 6 .   ? 18.689  36.276  20.702  1.000 47.411  0 205 HOH CCC O   1 ? ?  
HETATM 7109 O O   . HOH L 6 .   ? 18.235  53.764  27.208  1.000 35.960  0 206 HOH CCC O   1 ? ?  
HETATM 7110 O O   . HOH L 6 .   ? 18.791  40.064  29.223  1.000 41.964  0 207 HOH CCC O   1 ? ?  
HETATM 7111 O O   . HOH L 6 .   ? 20.042  38.841  7.415   1.000 29.822  0 208 HOH CCC O   1 ? ?  
HETATM 7112 O O   . HOH L 6 .   ? 17.747  38.104  8.565   1.000 33.895  0 209 HOH CCC O   1 ? ?  
HETATM 7113 O O   . HOH L 6 .   ? 19.891  40.618  -2.286  1.000 30.521  0 210 HOH CCC O   1 ? ?  
HETATM 7114 O O   . HOH L 6 .   ? 9.947   50.777  20.576  1.000 53.952  0 211 HOH CCC O   1 ? ?  
HETATM 7115 O O   . HOH L 6 .   ? 28.473  42.313  20.556  1.000 47.485  0 212 HOH CCC O   1 ? ?  
HETATM 7116 O O   . HOH L 6 .   ? 32.140  50.745  12.246  1.000 44.702  0 213 HOH CCC O   1 ? ?  
HETATM 7117 O O   . HOH L 6 .   ? 26.373  54.236  1.978   1.000 47.181  0 214 HOH CCC O   1 ? ?  
HETATM 7118 O O   . HOH L 6 .   ? 16.417  52.160  2.927   1.000 47.665  0 215 HOH CCC O   1 ? ?  
HETATM 7119 O O   . HOH L 6 .   ? 28.452  54.309  23.521  1.000 50.742  0 216 HOH CCC O   1 ? ?  
HETATM 7120 O O   . HOH L 6 .   ? 17.031  35.685  9.346   1.000 30.339  0 217 HOH CCC O   1 ? ?  
HETATM 7121 O O   . HOH L 6 .   ? 23.735  34.137  17.737  1.000 42.277  0 218 HOH CCC O   1 ? ?  
HETATM 7122 O O   . HOH L 6 .   ? 30.186  51.067  -0.348  1.000 49.952  0 219 HOH CCC O   1 ? ?  
HETATM 7123 O O   . HOH L 6 .   ? 26.975  51.638  1.973   1.000 55.308  0 220 HOH CCC O   1 ? ?  
HETATM 7124 O O   . HOH L 6 .   ? 30.339  48.353  1.232   1.000 38.616  0 221 HOH CCC O   1 ? ?  
HETATM 7125 O O   . HOH L 6 .   ? 9.165   48.890  5.733   1.000 46.990  0 222 HOH CCC O   1 ? ?  
HETATM 7126 O O   . HOH L 6 .   ? 19.051  53.119  2.583   1.000 42.351  0 223 HOH CCC O   1 ? ?  
HETATM 7127 O O   . HOH L 6 .   ? 26.107  56.721  3.085   1.000 47.710  0 224 HOH CCC O   1 ? ?  
HETATM 7128 O O   . HOH L 6 .   ? 12.898  32.149  22.746  1.000 39.765  0 225 HOH CCC O   1 ? ?  
HETATM 7129 O O   . HOH L 6 .   ? 12.226  33.725  17.251  1.000 47.737  0 226 HOH CCC O   1 ? ?  
HETATM 7130 O O   . HOH M 6 .   ? 20.791  12.249  42.198  1.000 46.273  0 201 HOH DDD O   1 ? ?  
HETATM 7131 O O   . HOH M 6 .   ? 22.264  4.603   46.221  1.000 43.090  0 202 HOH DDD O   1 ? ?  
HETATM 7132 O O   . HOH M 6 .   ? 32.792  15.546  55.451  1.000 57.393  0 203 HOH DDD O   1 ? ?  
HETATM 7133 O O   . HOH M 6 .   ? 4.651   13.151  45.993  1.000 49.531  0 204 HOH DDD O   1 ? ?  
HETATM 7134 O O   . HOH M 6 .   ? 23.561  16.734  42.304  1.000 31.932  0 205 HOH DDD O   1 ? ?  
HETATM 7135 O O   . HOH N 6 .   ? 16.950  0.050   26.420  1.000 37.145  0 701 HOH EEE O   1 ? ?  
HETATM 7136 O O   . HOH N 6 .   ? 14.061  -5.730  17.408  1.000 47.648  0 702 HOH EEE O   1 ? ?  
HETATM 7137 O O   . HOH N 6 .   ? -14.630 -6.060  26.611  1.000 41.602  0 703 HOH EEE O   1 ? ?  
HETATM 7138 O O   . HOH N 6 .   ? 7.030   -9.537  32.477  1.000 39.132  0 704 HOH EEE O   1 ? ?  
HETATM 7139 O O   . HOH N 6 .   ? 1.872   -5.214  25.598  1.000 34.962  0 705 HOH EEE O   1 ? ?  
HETATM 7140 O O   . HOH N 6 .   ? -3.426  -9.498  25.468  1.000 38.353  0 706 HOH EEE O   1 ? ?  
HETATM 7141 O O   . HOH N 6 .   ? -12.492 -0.606  30.542  1.000 36.206  0 707 HOH EEE O   1 ? ?  
HETATM 7142 O O   . HOH N 6 .   ? 14.274  2.186   37.732  1.000 47.939  0 708 HOH EEE O   1 ? ?  
HETATM 7143 O O   . HOH N 6 .   ? 28.591  -9.995  24.853  1.000 45.641  0 709 HOH EEE O   1 ? ?  
HETATM 7144 O O   . HOH N 6 .   ? 4.631   -4.925  24.844  1.000 36.433  0 710 HOH EEE O   1 ? ?  
HETATM 7145 O O   . HOH N 6 .   ? 1.154   4.453   27.069  1.000 46.028  0 711 HOH EEE O   1 ? ?  
HETATM 7146 O O   . HOH N 6 .   ? -3.683  8.684   27.332  1.000 39.984  0 712 HOH EEE O   1 ? ?  
HETATM 7147 O O   . HOH N 6 .   ? -10.824 -16.538 21.856  1.000 44.497  0 713 HOH EEE O   1 ? ?  
HETATM 7148 O O   . HOH N 6 .   ? -3.345  -8.363  16.408  1.000 50.034  0 714 HOH EEE O   1 ? ?  
HETATM 7149 O O   . HOH N 6 .   ? 30.486  -0.678  35.640  1.000 43.517  0 715 HOH EEE O   1 ? ?  
HETATM 7150 O O   . HOH N 6 .   ? 3.088   -8.574  18.956  1.000 44.156  0 716 HOH EEE O   1 ? ?  
HETATM 7151 O O   . HOH N 6 .   ? -7.997  11.131  23.332  1.000 41.182  0 717 HOH EEE O   1 ? ?  
HETATM 7152 O O   . HOH N 6 .   ? -5.564  6.641   33.871  1.000 42.018  0 718 HOH EEE O   1 ? ?  
HETATM 7153 O O   . HOH N 6 .   ? -1.252  10.866  43.194  1.000 50.322  0 719 HOH EEE O   1 ? ?  
HETATM 7154 O O   . HOH N 6 .   ? -0.992  -0.239  37.592  1.000 50.989  0 720 HOH EEE O   1 ? ?  
HETATM 7155 O O   . HOH N 6 .   ? 30.631  1.589   35.087  1.000 39.223  0 721 HOH EEE O   1 ? ?  
HETATM 7156 O O   . HOH N 6 .   ? -0.300  -2.570  38.160  1.000 50.723  0 722 HOH EEE O   1 ? ?  
HETATM 7157 O O   . HOH N 6 .   ? -16.603 -7.734  27.771  1.000 43.566  0 723 HOH EEE O   1 ? ?  
HETATM 7158 O O   . HOH N 6 .   ? -13.615 -21.036 32.424  1.000 45.448  0 724 HOH EEE O   1 ? ?  
HETATM 7159 O O   . HOH N 6 .   ? 13.485  21.067  38.327  1.000 50.835  0 725 HOH EEE O   1 ? ?  
HETATM 7160 O O   . HOH N 6 .   ? -0.188  8.956   21.994  1.000 48.704  0 726 HOH EEE O   1 ? ?  
HETATM 7161 O O   . HOH N 6 .   ? 13.165  16.456  28.844  1.000 47.393  0 727 HOH EEE O   1 ? ?  
HETATM 7162 O O   . HOH N 6 .   ? 17.760  24.876  26.369  1.000 57.259  0 728 HOH EEE O   1 ? ?  
HETATM 7163 O O   . HOH N 6 .   ? 12.211  18.063  30.570  1.000 35.879  0 729 HOH EEE O   1 ? ?  
HETATM 7164 O O   . HOH O 6 .   ? -14.888 2.489   -0.142  1.000 33.972  0 201 HOH FFF O   1 ? ?  
HETATM 7165 O O   . HOH O 6 .   ? -10.539 2.741   8.066   1.000 37.503  0 202 HOH FFF O   1 ? ?  
HETATM 7166 O O   . HOH O 6 .   ? -27.753 0.601   4.585   1.000 41.999  0 203 HOH FFF O   1 ? ?  
HETATM 7167 O O   . HOH O 6 .   ? -11.433 1.392   21.424  1.000 39.629  0 204 HOH FFF O   1 ? ?  
HETATM 7168 O O   . HOH O 6 .   ? -12.893 4.870   7.907   1.000 32.095  0 205 HOH FFF O   1 ? ?  
HETATM 7169 O O   . HOH O 6 .   ? -20.990 -8.287  28.404  1.000 32.713  0 206 HOH FFF O   1 ? ?  
HETATM 7170 O O   . HOH O 6 .   ? -46.283 -11.095 5.199   1.000 59.468  0 207 HOH FFF O   1 ? ?  
HETATM 7171 O O   . HOH O 6 .   ? -23.341 -8.544  29.819  1.000 38.524  0 208 HOH FFF O   1 ? ?  
HETATM 7172 O O   . HOH O 6 .   ? -13.985 1.434   14.062  1.000 37.042  0 209 HOH FFF O   1 ? ?  
HETATM 7173 O O   . HOH O 6 .   ? -39.205 1.975   5.114   1.000 54.575  0 210 HOH FFF O   1 ? ?  
HETATM 7174 O O   . HOH O 6 .   ? -16.776 -7.413  9.063   1.000 42.495  0 211 HOH FFF O   1 ? ?  
HETATM 7175 O O   . HOH O 6 .   ? -6.744  -8.316  15.840  1.000 45.029  0 212 HOH FFF O   1 ? ?  
HETATM 7176 O O   . HOH O 6 .   ? -18.473 7.345   29.929  1.000 39.995  0 213 HOH FFF O   1 ? ?  
HETATM 7177 O O   . HOH O 6 .   ? -8.649  4.499   19.201  1.000 41.628  0 214 HOH FFF O   1 ? ?  
HETATM 7178 O O   . HOH O 6 .   ? -7.209  8.177   6.213   1.000 42.272  0 215 HOH FFF O   1 ? ?  
HETATM 7179 O O   . HOH O 6 .   ? -24.459 -10.867 18.250  1.000 44.358  0 216 HOH FFF O   1 ? ?  
HETATM 7180 O O   . HOH O 6 .   ? -10.418 -11.074 18.113  1.000 44.224  0 217 HOH FFF O   1 ? ?  
HETATM 7181 O O   . HOH O 6 .   ? -21.253 -8.187  23.572  1.000 39.286  0 218 HOH FFF O   1 ? ?  
HETATM 7182 O O   . HOH O 6 .   ? -32.926 12.034  11.674  1.000 50.518  0 219 HOH FFF O   1 ? ?  
HETATM 7183 O O   . HOH O 6 .   ? -15.548 14.031  6.733   1.000 48.972  0 220 HOH FFF O   1 ? ?  
HETATM 7184 O O   . HOH O 6 .   ? -20.739 15.011  16.816  1.000 47.646  0 221 HOH FFF O   1 ? ?  
HETATM 7185 O O   . HOH O 6 .   ? -11.074 3.562   20.000  1.000 37.744  0 222 HOH FFF O   1 ? ?  
HETATM 7186 O O   . HOH O 6 .   ? -18.379 15.583  17.844  1.000 51.921  0 223 HOH FFF O   1 ? ?  
HETATM 7187 O O   . HOH O 6 .   ? -13.861 10.602  21.298  1.000 49.830  0 224 HOH FFF O   1 ? ?  
HETATM 7188 O O   . HOH O 6 .   ? -13.328 7.359   32.232  1.000 45.571  0 225 HOH FFF O   1 ? ?  
HETATM 7189 O O   . HOH O 6 .   ? -25.441 -3.933  28.192  1.000 52.425  0 226 HOH FFF O   1 ? ?  
HETATM 7190 O O   . HOH O 6 .   ? -13.057 12.110  23.394  1.000 51.592  0 227 HOH FFF O   1 ? ?  
HETATM 7191 O O   . HOH O 6 .   ? -5.670  -0.264  7.643   1.000 52.427  0 228 HOH FFF O   1 ? ?  
HETATM 7192 O O   . HOH O 6 .   ? -13.894 11.435  18.714  1.000 44.439  0 229 HOH FFF O   1 ? ?  
HETATM 7193 O O   . HOH O 6 .   ? -50.407 -9.726  5.166   1.000 49.987  0 230 HOH FFF O   1 ? ?  
HETATM 7194 O O   . HOH O 6 .   ? -31.843 -6.416  4.652   1.000 41.863  0 231 HOH FFF 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 
1    N N   . GLN A 1   ? 0.742 1.058 0.784 -0.078 0.090  0.012  3   GLN AAA N   
2    C CA  . GLN A 1   ? 0.717 1.050 0.767 -0.088 0.074  -0.002 3   GLN AAA CA  
3    C C   . GLN A 1   ? 0.685 1.017 0.687 -0.090 0.059  -0.011 3   GLN AAA C   
4    O O   . GLN A 1   ? 0.679 0.991 0.648 -0.083 0.061  -0.006 3   GLN AAA O   
5    C CB  . GLN A 1   ? 0.774 1.092 0.848 -0.084 0.089  0.002  3   GLN AAA CB  
6    C CG  . GLN A 1   ? 0.824 1.114 0.848 -0.072 0.101  0.010  3   GLN AAA CG  
7    C CD  . GLN A 1   ? 0.877 1.157 0.935 -0.065 0.122  0.030  3   GLN AAA CD  
8    O OE1 . GLN A 1   ? 0.871 1.162 0.999 -0.074 0.119  0.030  3   GLN AAA OE1 
9    N NE2 . GLN A 1   ? 0.944 1.206 0.958 -0.046 0.142  0.048  3   GLN AAA NE2 
10   N N   . VAL A 2   ? 0.643 1.000 0.649 -0.096 0.043  -0.026 4   VAL AAA N   
11   C CA  . VAL A 2   ? 0.615 0.977 0.585 -0.098 0.030  -0.033 4   VAL AAA CA  
12   C C   . VAL A 2   ? 0.602 0.928 0.548 -0.090 0.040  -0.034 4   VAL AAA C   
13   O O   . VAL A 2   ? 0.580 0.901 0.551 -0.089 0.045  -0.038 4   VAL AAA O   
14   C CB  . VAL A 2   ? 0.614 1.025 0.596 -0.102 0.012  -0.049 4   VAL AAA CB  
15   C CG1 . VAL A 2   ? 0.615 1.035 0.566 -0.102 0.003  -0.052 4   VAL AAA CG1 
16   C CG2 . VAL A 2   ? 0.607 1.065 0.607 -0.104 0.002  -0.045 4   VAL AAA CG2 
17   N N   . GLN A 3   ? 0.591 0.893 0.497 -0.085 0.039  -0.030 5   GLN AAA N   
18   C CA  . GLN A 3   ? 0.601 0.873 0.474 -0.073 0.045  -0.030 5   GLN AAA CA  
19   C C   . GLN A 3   ? 0.581 0.859 0.434 -0.077 0.026  -0.039 5   GLN AAA C   
20   O O   . GLN A 3   ? 0.568 0.852 0.417 -0.081 0.013  -0.039 5   GLN AAA O   
21   C CB  . GLN A 3   ? 0.637 0.882 0.481 -0.057 0.056  -0.023 5   GLN AAA CB  
22   C CG  . GLN A 3   ? 0.644 0.888 0.510 -0.049 0.080  -0.009 5   GLN AAA CG  
23   C CD  . GLN A 3   ? 0.673 0.900 0.507 -0.027 0.092  -0.007 5   GLN AAA CD  
24   O OE1 . GLN A 3   ? 0.667 0.887 0.491 -0.025 0.078  -0.019 5   GLN AAA OE1 
25   N NE2 . GLN A 3   ? 0.718 0.941 0.541 -0.008 0.118  0.010  5   GLN AAA NE2 
26   N N   . LEU A 4   ? 0.577 0.855 0.429 -0.076 0.024  -0.045 6   LEU AAA N   
27   C CA  . LEU A 4   ? 0.594 0.878 0.430 -0.078 0.008  -0.054 6   LEU AAA CA  
28   C C   . LEU A 4   ? 0.631 0.882 0.435 -0.064 0.011  -0.051 6   LEU AAA C   
29   O O   . LEU A 4   ? 0.646 0.891 0.460 -0.059 0.021  -0.046 6   LEU AAA O   
30   C CB  . LEU A 4   ? 0.573 0.891 0.438 -0.085 0.002  -0.067 6   LEU AAA CB  
31   C CG  . LEU A 4   ? 0.569 0.931 0.457 -0.092 -0.003 -0.071 6   LEU AAA CG  
32   C CD1 . LEU A 4   ? 0.565 0.968 0.476 -0.091 -0.013 -0.094 6   LEU AAA CD1 
33   C CD2 . LEU A 4   ? 0.567 0.950 0.447 -0.097 -0.011 -0.057 6   LEU AAA CD2 
34   N N   . VAL A 5   ? 0.651 0.885 0.423 -0.056 0.001  -0.054 7   VAL AAA N   
35   C CA  . VAL A 5   ? 0.708 0.917 0.439 -0.036 0.000  -0.054 7   VAL AAA CA  
36   C C   . VAL A 5   ? 0.709 0.922 0.437 -0.039 -0.020 -0.063 7   VAL AAA C   
37   O O   . VAL A 5   ? 0.699 0.918 0.437 -0.047 -0.040 -0.072 7   VAL AAA O   
38   C CB  . VAL A 5   ? 0.742 0.933 0.442 -0.019 -0.004 -0.062 7   VAL AAA CB  
39   C CG1 . VAL A 5   ? 0.784 0.961 0.433 0.009  -0.004 -0.064 7   VAL AAA CG1 
40   C CG2 . VAL A 5   ? 0.745 0.937 0.456 -0.017 0.016  -0.053 7   VAL AAA CG2 
41   N N   . GLU A 6   ? 0.733 0.944 0.458 -0.034 -0.016 -0.058 8   GLU AAA N   
42   C CA  . GLU A 6   ? 0.755 0.971 0.481 -0.035 -0.034 -0.066 8   GLU AAA CA  
43   C C   . GLU A 6   ? 0.796 0.991 0.476 -0.013 -0.044 -0.067 8   GLU AAA C   
44   O O   . GLU A 6   ? 0.816 1.000 0.468 0.006  -0.028 -0.053 8   GLU AAA O   
45   C CB  . GLU A 6   ? 0.754 0.980 0.511 -0.040 -0.027 -0.063 8   GLU AAA CB  
46   C CG  . GLU A 6   ? 0.737 0.990 0.537 -0.055 -0.021 -0.070 8   GLU AAA CG  
47   C CD  . GLU A 6   ? 0.783 1.031 0.616 -0.054 -0.005 -0.063 8   GLU AAA CD  
48   O OE1 . GLU A 6   ? 0.850 1.079 0.672 -0.045 0.011  -0.044 8   GLU AAA OE1 
49   O OE2 . GLU A 6   ? 0.780 1.046 0.657 -0.059 -0.009 -0.077 8   GLU AAA OE2 
50   N N   . SER A 7   ? 0.808 1.003 0.486 -0.014 -0.070 -0.080 9   SER AAA N   
51   C CA  . SER A 7   ? 0.873 1.054 0.511 0.009  -0.088 -0.087 9   SER AAA CA  
52   C C   . SER A 7   ? 0.862 1.052 0.524 -0.000 -0.111 -0.096 9   SER AAA C   
53   O O   . SER A 7   ? 0.785 0.996 0.493 -0.022 -0.112 -0.095 9   SER AAA O   
54   C CB  . SER A 7   ? 0.912 1.080 0.519 0.026  -0.103 -0.106 9   SER AAA CB  
55   O OG  . SER A 7   ? 0.899 1.069 0.549 0.007  -0.120 -0.119 9   SER AAA OG  
56   N N   . GLY A 8   ? 0.884 1.066 0.516 0.020  -0.130 -0.101 10  GLY AAA N   
57   C CA  . GLY A 8   ? 0.879 1.068 0.535 0.015  -0.156 -0.110 10  GLY AAA CA  
58   C C   . GLY A 8   ? 0.878 1.074 0.542 0.017  -0.146 -0.095 10  GLY AAA C   
59   O O   . GLY A 8   ? 0.919 1.125 0.611 0.011  -0.164 -0.100 10  GLY AAA O   
60   N N   . GLY A 9   ? 0.870 1.062 0.522 0.025  -0.120 -0.074 11  GLY AAA N   
61   C CA  . GLY A 9   ? 0.875 1.070 0.548 0.029  -0.111 -0.057 11  GLY AAA CA  
62   C C   . GLY A 9   ? 0.947 1.136 0.580 0.056  -0.123 -0.045 11  GLY AAA C   
63   O O   . GLY A 9   ? 0.947 1.134 0.540 0.070  -0.148 -0.062 11  GLY AAA O   
64   N N   . GLY A 10  ? 0.980 1.169 0.628 0.066  -0.109 -0.016 12  GLY AAA N   
65   C CA  . GLY A 10  ? 1.040 1.232 0.652 0.096  -0.115 0.008  12  GLY AAA CA  
66   C C   . GLY A 10  ? 1.058 1.252 0.709 0.094  -0.130 0.012  12  GLY AAA C   
67   O O   . GLY A 10  ? 1.039 1.234 0.756 0.072  -0.124 0.005  12  GLY AAA O   
68   N N   . LEU A 11  ? 1.115 1.316 0.729 0.120  -0.150 0.021  13  LEU AAA N   
69   C CA  . LEU A 11  ? 1.113 1.318 0.762 0.123  -0.166 0.030  13  LEU AAA CA  
70   C C   . LEU A 11  ? 1.099 1.307 0.756 0.113  -0.202 -0.010 13  LEU AAA C   
71   O O   . LEU A 11  ? 1.098 1.307 0.711 0.120  -0.223 -0.034 13  LEU AAA O   
72   C CB  . LEU A 11  ? 1.191 1.406 0.793 0.161  -0.168 0.069  13  LEU AAA CB  
73   C CG  . LEU A 11  ? 1.205 1.424 0.856 0.167  -0.175 0.095  13  LEU AAA CG  
74   C CD1 . LEU A 11  ? 1.186 1.395 0.914 0.155  -0.144 0.128  13  LEU AAA CD1 
75   C CD2 . LEU A 11  ? 1.271 1.510 0.861 0.208  -0.189 0.125  13  LEU AAA CD2 
76   N N   . VAL A 12  ? 1.083 1.297 0.804 0.097  -0.207 -0.017 14  VAL AAA N   
77   C CA  . VAL A 12  ? 1.093 1.317 0.839 0.089  -0.238 -0.043 14  VAL AAA CA  
78   C C   . VAL A 12  ? 1.099 1.330 0.899 0.091  -0.241 -0.030 14  VAL AAA C   
79   O O   . VAL A 12  ? 1.133 1.357 0.955 0.097  -0.220 -0.004 14  VAL AAA O   
80   C CB  . VAL A 12  ? 1.046 1.281 0.827 0.061  -0.237 -0.070 14  VAL AAA CB  
81   C CG1 . VAL A 12  ? 1.062 1.289 0.801 0.059  -0.244 -0.084 14  VAL AAA CG1 
82   C CG2 . VAL A 12  ? 0.998 1.240 0.823 0.043  -0.207 -0.069 14  VAL AAA CG2 
83   N N   . GLN A 13  ? 1.075 1.320 0.905 0.088  -0.267 -0.047 15  GLN AAA N   
84   C CA  . GLN A 13  ? 1.067 1.322 0.956 0.091  -0.273 -0.041 15  GLN AAA CA  
85   C C   . GLN A 13  ? 0.997 1.276 0.945 0.069  -0.272 -0.068 15  GLN AAA C   
86   O O   . GLN A 13  ? 0.952 1.242 0.893 0.055  -0.276 -0.084 15  GLN AAA O   
87   C CB  . GLN A 13  ? 1.130 1.387 0.999 0.113  -0.305 -0.031 15  GLN AAA CB  
88   C CG  . GLN A 13  ? 1.200 1.447 0.994 0.142  -0.308 -0.005 15  GLN AAA CG  
89   C CD  . GLN A 13  ? 1.256 1.512 1.041 0.170  -0.333 0.016  15  GLN AAA CD  
90   O OE1 . GLN A 13  ? 1.312 1.570 1.062 0.196  -0.324 0.056  15  GLN AAA OE1 
91   N NE2 . GLN A 13  ? 1.254 1.521 1.074 0.166  -0.364 -0.005 15  GLN AAA NE2 
92   N N   . ALA A 14  ? 0.967 1.259 0.976 0.069  -0.267 -0.070 16  ALA AAA N   
93   C CA  . ALA A 14  ? 0.921 1.250 0.988 0.056  -0.260 -0.094 16  ALA AAA CA  
94   C C   . ALA A 14  ? 0.908 1.260 0.981 0.048  -0.281 -0.102 16  ALA AAA C   
95   O O   . ALA A 14  ? 0.949 1.291 1.009 0.058  -0.311 -0.095 16  ALA AAA O   
96   C CB  . ALA A 14  ? 0.915 1.254 1.045 0.066  -0.260 -0.098 16  ALA AAA CB  
97   N N   . GLY A 15  ? 0.859 1.245 0.956 0.032  -0.268 -0.113 17  GLY AAA N   
98   C CA  . GLY A 15  ? 0.832 1.246 0.956 0.022  -0.284 -0.113 17  GLY AAA CA  
99   C C   . GLY A 15  ? 0.843 1.234 0.927 0.013  -0.295 -0.111 17  GLY AAA C   
100  O O   . GLY A 15  ? 0.833 1.244 0.953 0.002  -0.309 -0.109 17  GLY AAA O   
101  N N   . GLY A 16  ? 0.872 1.224 0.893 0.019  -0.290 -0.110 18  GLY AAA N   
102  C CA  . GLY A 16  ? 0.892 1.220 0.869 0.017  -0.301 -0.113 18  GLY AAA CA  
103  C C   . GLY A 16  ? 0.856 1.196 0.837 -0.001 -0.277 -0.113 18  GLY AAA C   
104  O O   . GLY A 16  ? 0.787 1.148 0.781 -0.006 -0.248 -0.111 18  GLY AAA O   
105  N N   . SER A 17  ? 0.897 1.226 0.871 -0.007 -0.292 -0.117 19  SER AAA N   
106  C CA  . SER A 17  ? 0.875 1.215 0.859 -0.024 -0.274 -0.113 19  SER AAA CA  
107  C C   . SER A 17  ? 0.896 1.200 0.814 -0.017 -0.266 -0.118 19  SER AAA C   
108  O O   . SER A 17  ? 0.958 1.232 0.839 -0.002 -0.291 -0.129 19  SER AAA O   
109  C CB  . SER A 17  ? 0.883 1.240 0.929 -0.037 -0.298 -0.110 19  SER AAA CB  
110  O OG  . SER A 17  ? 0.911 1.250 0.947 -0.044 -0.299 -0.112 19  SER AAA OG  
111  N N   . LEU A 18  ? 0.865 1.176 0.770 -0.024 -0.234 -0.111 20  LEU AAA N   
112  C CA  . LEU A 18  ? 0.861 1.144 0.715 -0.020 -0.219 -0.112 20  LEU AAA CA  
113  C C   . LEU A 18  ? 0.807 1.111 0.684 -0.038 -0.203 -0.107 20  LEU AAA C   
114  O O   . LEU A 18  ? 0.779 1.122 0.690 -0.048 -0.186 -0.100 20  LEU AAA O   
115  C CB  . LEU A 18  ? 0.872 1.145 0.700 -0.010 -0.197 -0.105 20  LEU AAA CB  
116  C CG  . LEU A 18  ? 0.922 1.163 0.693 0.004  -0.186 -0.099 20  LEU AAA CG  
117  C CD1 . LEU A 18  ? 0.959 1.181 0.687 0.024  -0.213 -0.106 20  LEU AAA CD1 
118  C CD2 . LEU A 18  ? 0.929 1.163 0.699 0.013  -0.166 -0.084 20  LEU AAA CD2 
119  N N   . ARG A 19  ? 0.803 1.086 0.662 -0.039 -0.208 -0.110 21  ARG AAA N   
120  C CA  . ARG A 19  ? 0.776 1.077 0.660 -0.055 -0.195 -0.100 21  ARG AAA CA  
121  C C   . ARG A 19  ? 0.765 1.045 0.603 -0.051 -0.174 -0.102 21  ARG AAA C   
122  O O   . ARG A 19  ? 0.781 1.028 0.586 -0.040 -0.184 -0.111 21  ARG AAA O   
123  C CB  . ARG A 19  ? 0.802 1.097 0.729 -0.062 -0.223 -0.102 21  ARG AAA CB  
124  C CG  . ARG A 19  ? 0.797 1.118 0.767 -0.079 -0.210 -0.082 21  ARG AAA CG  
125  C CD  . ARG A 19  ? 0.850 1.155 0.871 -0.085 -0.239 -0.085 21  ARG AAA CD  
126  N NE  . ARG A 19  ? 0.849 1.187 0.928 -0.102 -0.226 -0.054 21  ARG AAA NE  
127  C CZ  . ARG A 19  ? 0.895 1.228 1.046 -0.111 -0.248 -0.045 21  ARG AAA CZ  
128  N NH1 . ARG A 19  ? 0.934 1.227 1.107 -0.104 -0.287 -0.074 21  ARG AAA NH1 
129  N NH2 . ARG A 19  ? 0.865 1.236 1.069 -0.126 -0.232 -0.008 21  ARG AAA NH2 
130  N N   . LEU A 20  ? 0.602 1.450 0.538 0.118  -0.130 -0.139 22  LEU AAA N   
131  C CA  . LEU A 20  ? 0.594 1.388 0.520 0.102  -0.118 -0.113 22  LEU AAA CA  
132  C C   . LEU A 20  ? 0.545 1.330 0.497 0.071  -0.104 -0.140 22  LEU AAA C   
133  O O   . LEU A 20  ? 0.541 1.326 0.518 0.061  -0.102 -0.166 22  LEU AAA O   
134  C CB  . LEU A 20  ? 0.615 1.339 0.535 0.106  -0.117 -0.081 22  LEU AAA CB  
135  C CG  . LEU A 20  ? 0.676 1.390 0.570 0.140  -0.127 -0.053 22  LEU AAA CG  
136  C CD1 . LEU A 20  ? 0.711 1.345 0.596 0.136  -0.120 -0.021 22  LEU AAA CD1 
137  C CD2 . LEU A 20  ? 0.720 1.479 0.583 0.160  -0.130 -0.036 22  LEU AAA CD2 
138  N N   . SER A 21  ? 0.529 1.309 0.473 0.059  -0.093 -0.132 23  SER AAA N   
139  C CA  . SER A 21  ? 0.496 1.259 0.458 0.036  -0.077 -0.148 23  SER AAA CA  
140  C C   . SER A 21  ? 0.494 1.219 0.447 0.028  -0.068 -0.116 23  SER AAA C   
141  O O   . SER A 21  ? 0.515 1.242 0.444 0.038  -0.071 -0.088 23  SER AAA O   
142  C CB  . SER A 21  ? 0.500 1.309 0.462 0.029  -0.069 -0.179 23  SER AAA CB  
143  O OG  . SER A 21  ? 0.523 1.355 0.459 0.037  -0.068 -0.163 23  SER AAA OG  
144  N N   . CYS A 22  ? 0.472 1.167 0.444 0.012  -0.057 -0.119 24  CYS AAA N   
145  C CA  . CYS A 22  ? 0.480 1.150 0.450 0.003  -0.049 -0.093 24  CYS AAA CA  
146  C C   . CYS A 22  ? 0.460 1.133 0.445 -0.007 -0.032 -0.109 24  CYS AAA C   
147  O O   . CYS A 22  ? 0.436 1.091 0.439 -0.012 -0.028 -0.124 24  CYS AAA O   
148  C CB  . CYS A 22  ? 0.498 1.126 0.474 -0.002 -0.054 -0.075 24  CYS AAA CB  
149  S SG  . CYS A 22  ? 0.511 1.122 0.495 -0.020 -0.043 -0.056 24  CYS AAA SG  
150  N N   . ALA A 23  ? 0.452 1.147 0.427 -0.007 -0.022 -0.106 25  ALA AAA N   
151  C CA  . ALA A 23  ? 0.443 1.139 0.427 -0.012 -0.004 -0.116 25  ALA AAA CA  
152  C C   . ALA A 23  ? 0.439 1.124 0.428 -0.017 0.001  -0.090 25  ALA AAA C   
153  O O   . ALA A 23  ? 0.454 1.148 0.432 -0.019 -0.003 -0.065 25  ALA AAA O   
154  C CB  . ALA A 23  ? 0.448 1.177 0.417 -0.007 0.005  -0.130 25  ALA AAA CB  
155  N N   . ALA A 24  ? 0.423 1.093 0.430 -0.019 0.011  -0.094 26  ALA AAA N   
156  C CA  . ALA A 24  ? 0.422 1.091 0.438 -0.023 0.014  -0.072 26  ALA AAA CA  
157  C C   . ALA A 24  ? 0.426 1.114 0.445 -0.015 0.033  -0.073 26  ALA AAA C   
158  O O   . ALA A 24  ? 0.451 1.129 0.472 -0.007 0.047  -0.094 26  ALA AAA O   
159  C CB  . ALA A 24  ? 0.403 1.048 0.434 -0.026 0.009  -0.074 26  ALA AAA CB  
160  N N   . SER A 25  ? 0.427 1.140 0.447 -0.018 0.036  -0.052 27  SER AAA N   
161  C CA  . SER A 25  ? 0.443 1.180 0.469 -0.007 0.054  -0.047 27  SER AAA CA  
162  C C   . SER A 25  ? 0.420 1.174 0.463 -0.012 0.051  -0.029 27  SER AAA C   
163  O O   . SER A 25  ? 0.418 1.186 0.463 -0.029 0.041  -0.013 27  SER AAA O   
164  C CB  . SER A 25  ? 0.463 1.232 0.477 -0.004 0.062  -0.042 27  SER AAA CB  
165  O OG  . SER A 25  ? 0.492 1.284 0.511 0.010  0.080  -0.039 27  SER AAA OG  
166  N N   . GLY A 26  ? 0.416 1.166 0.469 0.001  0.060  -0.032 28  GLY AAA N   
167  C CA  . GLY A 26  ? 0.439 1.223 0.506 0.004  0.061  -0.015 28  GLY AAA CA  
168  C C   . GLY A 26  ? 0.447 1.224 0.524 -0.009 0.045  -0.013 28  GLY AAA C   
169  O O   . GLY A 26  ? 0.523 1.340 0.613 -0.014 0.042  -0.001 28  GLY AAA O   
170  N N   . GLY A 27  ? 0.410 1.143 0.482 -0.014 0.036  -0.025 29  GLY AAA N   
171  C CA  . GLY A 27  ? 0.419 1.143 0.499 -0.025 0.022  -0.025 29  GLY AAA CA  
172  C C   . GLY A 27  ? 0.393 1.101 0.475 -0.007 0.030  -0.032 29  GLY AAA C   
173  O O   . GLY A 27  ? 0.402 1.093 0.486 -0.014 0.019  -0.037 29  GLY AAA O   
174  N N   . THR A 28  ? 0.378 1.088 0.457 0.016  0.049  -0.031 30  THR AAA N   
175  C CA  . THR A 28  ? 0.366 1.045 0.442 0.034  0.064  -0.037 30  THR AAA CA  
176  C C   . THR A 28  ? 0.347 0.984 0.420 0.021  0.055  -0.054 30  THR AAA C   
177  O O   . THR A 28  ? 0.341 0.970 0.417 0.019  0.048  -0.055 30  THR AAA O   
178  C CB  . THR A 28  ? 0.348 1.054 0.429 0.050  0.066  -0.023 30  THR AAA CB  
179  O OG1 . THR A 28  ? 0.350 1.107 0.436 0.060  0.071  -0.008 30  THR AAA OG1 
180  C CG2 . THR A 28  ? 0.357 1.029 0.430 0.073  0.087  -0.023 30  THR AAA CG2 
181  N N   . PHE A 29  ? 0.349 0.968 0.418 0.012  0.055  -0.069 31  PHE AAA N   
182  C CA  . PHE A 29  ? 0.350 0.943 0.418 -0.000 0.044  -0.086 31  PHE AAA CA  
183  C C   . PHE A 29  ? 0.345 0.912 0.416 0.004  0.051  -0.094 31  PHE AAA C   
184  O O   . PHE A 29  ? 0.349 0.908 0.423 -0.004 0.036  -0.098 31  PHE AAA O   
185  C CB  . PHE A 29  ? 0.357 0.943 0.418 -0.002 0.050  -0.103 31  PHE AAA CB  
186  C CG  . PHE A 29  ? 0.359 0.936 0.420 -0.013 0.036  -0.118 31  PHE AAA CG  
187  C CD1 . PHE A 29  ? 0.363 0.952 0.418 -0.021 0.016  -0.110 31  PHE AAA CD1 
188  C CD2 . PHE A 29  ? 0.355 0.912 0.419 -0.015 0.043  -0.140 31  PHE AAA CD2 
189  C CE1 . PHE A 29  ? 0.385 0.967 0.438 -0.024 0.003  -0.121 31  PHE AAA CE1 
190  C CE2 . PHE A 29  ? 0.367 0.926 0.433 -0.022 0.029  -0.155 31  PHE AAA CE2 
191  C CZ  . PHE A 29  ? 0.378 0.952 0.438 -0.024 0.008  -0.144 31  PHE AAA CZ  
192  N N   . SER A 30  ? 0.366 0.918 0.436 0.019  0.075  -0.094 32  SER AAA N   
193  C CA  . SER A 30  ? 0.382 0.902 0.452 0.025  0.089  -0.100 32  SER AAA CA  
194  C C   . SER A 30  ? 0.375 0.905 0.447 0.026  0.075  -0.089 32  SER AAA C   
195  O O   . SER A 30  ? 0.399 0.909 0.473 0.022  0.078  -0.098 32  SER AAA O   
196  C CB  . SER A 30  ? 0.414 0.913 0.478 0.044  0.120  -0.094 32  SER AAA CB  
197  O OG  . SER A 30  ? 0.455 0.923 0.518 0.037  0.138  -0.118 32  SER AAA OG  
198  N N   . THR A 31  ? 0.378 0.944 0.451 0.029  0.063  -0.072 33  THR AAA N   
199  C CA  . THR A 31  ? 0.359 0.942 0.433 0.029  0.049  -0.064 33  THR AAA CA  
200  C C   . THR A 31  ? 0.344 0.941 0.423 0.007  0.023  -0.069 33  THR AAA C   
201  O O   . THR A 31  ? 0.359 0.977 0.439 0.003  0.011  -0.065 33  THR AAA O   
202  C CB  . THR A 31  ? 0.358 0.977 0.430 0.048  0.057  -0.044 33  THR AAA CB  
203  O OG1 . THR A 31  ? 0.322 0.977 0.399 0.044  0.049  -0.036 33  THR AAA OG1 
204  C CG2 . THR A 31  ? 0.379 0.976 0.443 0.075  0.086  -0.035 33  THR AAA CG2 
205  N N   . ALA A 32  ? 0.336 0.920 0.415 -0.005 0.016  -0.078 34  ALA AAA N   
206  C CA  . ALA A 32  ? 0.347 0.933 0.427 -0.023 -0.005 -0.079 34  ALA AAA CA  
207  C C   . ALA A 32  ? 0.351 0.907 0.429 -0.028 -0.013 -0.094 34  ALA AAA C   
208  O O   . ALA A 32  ? 0.360 0.903 0.437 -0.024 -0.005 -0.105 34  ALA AAA O   
209  C CB  . ALA A 32  ? 0.362 0.960 0.439 -0.029 -0.005 -0.072 34  ALA AAA CB  
210  N N   . ALA A 33  ? 0.344 0.893 0.421 -0.036 -0.027 -0.097 35  ALA AAA N   
211  C CA  . ALA A 33  ? 0.359 0.883 0.434 -0.039 -0.037 -0.108 35  ALA AAA CA  
212  C C   . ALA A 33  ? 0.364 0.883 0.433 -0.044 -0.045 -0.102 35  ALA AAA C   
213  O O   . ALA A 33  ? 0.378 0.906 0.445 -0.054 -0.048 -0.089 35  ALA AAA O   
214  C CB  . ALA A 33  ? 0.364 0.878 0.438 -0.044 -0.048 -0.113 35  ALA AAA CB  
215  N N   . MET A 34  ? 0.375 0.885 0.441 -0.038 -0.047 -0.111 36  MET AAA N   
216  C CA  . MET A 34  ? 0.378 0.888 0.434 -0.038 -0.053 -0.103 36  MET AAA CA  
217  C C   . MET A 34  ? 0.398 0.886 0.447 -0.032 -0.065 -0.106 36  MET AAA C   
218  O O   . MET A 34  ? 0.411 0.894 0.466 -0.025 -0.067 -0.121 36  MET AAA O   
219  C CB  . MET A 34  ? 0.381 0.911 0.437 -0.031 -0.045 -0.112 36  MET AAA CB  
220  C CG  . MET A 34  ? 0.381 0.927 0.441 -0.032 -0.030 -0.109 36  MET AAA CG  
221  S SD  . MET A 34  ? 0.386 0.946 0.440 -0.040 -0.030 -0.085 36  MET AAA SD  
222  C CE  . MET A 34  ? 0.407 0.969 0.445 -0.039 -0.038 -0.078 36  MET AAA CE  
223  N N   . GLY A 35  ? 0.420 0.894 0.455 -0.033 -0.071 -0.090 37  GLY AAA N   
224  C CA  . GLY A 35  ? 0.452 0.896 0.476 -0.024 -0.080 -0.088 37  GLY AAA CA  
225  C C   . GLY A 35  ? 0.478 0.922 0.484 -0.014 -0.083 -0.072 37  GLY AAA C   
226  O O   . GLY A 35  ? 0.461 0.920 0.462 -0.021 -0.077 -0.059 37  GLY AAA O   
227  N N   . TRP A 36  ? 0.487 0.918 0.483 0.005  -0.090 -0.072 38  TRP AAA N   
228  C CA  . TRP A 36  ? 0.513 0.937 0.487 0.022  -0.093 -0.052 38  TRP AAA CA  
229  C C   . TRP A 36  ? 0.562 0.927 0.521 0.026  -0.093 -0.037 38  TRP AAA C   
230  O O   . TRP A 36  ? 0.565 0.912 0.528 0.036  -0.098 -0.050 38  TRP AAA O   
231  C CB  . TRP A 36  ? 0.499 0.964 0.471 0.047  -0.101 -0.064 38  TRP AAA CB  
232  C CG  . TRP A 36  ? 0.463 0.979 0.443 0.041  -0.097 -0.077 38  TRP AAA CG  
233  C CD1 . TRP A 36  ? 0.421 0.967 0.422 0.033  -0.094 -0.104 38  TRP AAA CD1 
234  C CD2 . TRP A 36  ? 0.469 1.009 0.434 0.042  -0.095 -0.063 38  TRP AAA CD2 
235  N NE1 . TRP A 36  ? 0.405 0.987 0.406 0.029  -0.089 -0.110 38  TRP AAA NE1 
236  C CE2 . TRP A 36  ? 0.437 1.020 0.415 0.035  -0.090 -0.086 38  TRP AAA CE2 
237  C CE3 . TRP A 36  ? 0.509 1.036 0.448 0.049  -0.093 -0.034 38  TRP AAA CE3 
238  C CZ2 . TRP A 36  ? 0.444 1.060 0.412 0.034  -0.086 -0.084 38  TRP AAA CZ2 
239  C CZ3 . TRP A 36  ? 0.514 1.077 0.442 0.049  -0.089 -0.028 38  TRP AAA CZ3 
240  C CH2 . TRP A 36  ? 0.485 1.094 0.428 0.042  -0.087 -0.054 38  TRP AAA CH2 
241  N N   . PHE A 37  ? 0.608 0.943 0.550 0.016  -0.086 -0.013 39  PHE AAA N   
242  C CA  . PHE A 37  ? 0.685 0.954 0.608 0.018  -0.081 0.005  39  PHE AAA CA  
243  C C   . PHE A 37  ? 0.742 1.003 0.635 0.045  -0.080 0.032  39  PHE AAA C   
244  O O   . PHE A 37  ? 0.735 1.042 0.623 0.049  -0.080 0.040  39  PHE AAA O   
245  C CB  . PHE A 37  ? 0.705 0.944 0.632 -0.019 -0.071 0.012  39  PHE AAA CB  
246  C CG  . PHE A 37  ? 0.679 0.918 0.628 -0.041 -0.073 -0.012 39  PHE AAA CG  
247  C CD1 . PHE A 37  ? 0.627 0.920 0.598 -0.050 -0.076 -0.029 39  PHE AAA CD1 
248  C CD2 . PHE A 37  ? 0.720 0.904 0.666 -0.053 -0.069 -0.019 39  PHE AAA CD2 
249  C CE1 . PHE A 37  ? 0.605 0.903 0.593 -0.067 -0.078 -0.048 39  PHE AAA CE1 
250  C CE2 . PHE A 37  ? 0.698 0.891 0.662 -0.073 -0.072 -0.043 39  PHE AAA CE2 
251  C CZ  . PHE A 37  ? 0.635 0.888 0.620 -0.078 -0.077 -0.056 39  PHE AAA CZ  
252  N N   . ARG A 38  ? 0.812 1.017 0.685 0.065  -0.077 0.046  40  ARG AAA N   
253  C CA  . ARG A 38  ? 0.897 1.085 0.736 0.095  -0.073 0.079  40  ARG AAA CA  
254  C C   . ARG A 38  ? 0.987 1.081 0.803 0.087  -0.056 0.103  40  ARG AAA C   
255  O O   . ARG A 38  ? 0.996 1.043 0.823 0.070  -0.052 0.086  40  ARG AAA O   
256  C CB  . ARG A 38  ? 0.907 1.127 0.739 0.141  -0.085 0.074  40  ARG AAA CB  
257  C CG  . ARG A 38  ? 0.941 1.108 0.770 0.161  -0.086 0.068  40  ARG AAA CG  
258  C CD  . ARG A 38  ? 0.944 1.157 0.769 0.208  -0.098 0.063  40  ARG AAA CD  
259  N NE  . ARG A 38  ? 0.968 1.146 0.797 0.226  -0.100 0.050  40  ARG AAA NE  
260  C CZ  . ARG A 38  ? 0.972 1.188 0.802 0.267  -0.110 0.042  40  ARG AAA CZ  
261  N NH1 . ARG A 38  ? 0.959 1.256 0.787 0.292  -0.122 0.044  40  ARG AAA NH1 
262  N NH2 . ARG A 38  ? 0.991 1.172 0.825 0.282  -0.109 0.030  40  ARG AAA NH2 
263  N N   . GLN A 39  ? 1.063 1.133 0.848 0.099  -0.044 0.139  41  GLN AAA N   
264  C CA  . GLN A 39  ? 1.177 1.150 0.935 0.093  -0.023 0.168  41  GLN AAA CA  
265  C C   . GLN A 39  ? 1.255 1.211 0.972 0.141  -0.017 0.207  41  GLN AAA C   
266  O O   . GLN A 39  ? 1.267 1.259 0.968 0.144  -0.013 0.231  41  GLN AAA O   
267  C CB  . GLN A 39  ? 1.196 1.153 0.961 0.043  -0.007 0.176  41  GLN AAA CB  
268  C CG  . GLN A 39  ? 1.302 1.156 1.047 0.024  0.018  0.196  41  GLN AAA CG  
269  C CD  . GLN A 39  ? 1.320 1.169 1.079 -0.032 0.033  0.196  41  GLN AAA CD  
270  O OE1 . GLN A 39  ? 1.291 1.213 1.065 -0.047 0.028  0.196  41  GLN AAA OE1 
271  N NE2 . GLN A 39  ? 1.388 1.156 1.145 -0.063 0.052  0.195  41  GLN AAA NE2 
272  N N   . ALA A 40  ? 1.325 1.231 1.024 0.179  -0.016 0.214  42  ALA AAA N   
273  C CA  . ALA A 40  ? 1.432 1.300 1.085 0.229  -0.005 0.257  42  ALA AAA CA  
274  C C   . ALA A 40  ? 1.537 1.317 1.162 0.206  0.025  0.294  42  ALA AAA C   
275  O O   . ALA A 40  ? 1.527 1.255 1.168 0.155  0.038  0.280  42  ALA AAA O   
276  C CB  . ALA A 40  ? 1.471 1.296 1.115 0.271  -0.008 0.252  42  ALA AAA CB  
277  N N   . PRO A 41  ? 1.635 1.400 1.217 0.240  0.037  0.341  43  PRO AAA N   
278  C CA  . PRO A 41  ? 1.734 1.419 1.288 0.215  0.069  0.379  43  PRO AAA CA  
279  C C   . PRO A 41  ? 1.852 1.400 1.389 0.206  0.097  0.390  43  PRO AAA C   
280  O O   . PRO A 41  ? 1.946 1.423 1.461 0.182  0.127  0.421  43  PRO AAA O   
281  C CB  . PRO A 41  ? 1.787 1.499 1.295 0.267  0.073  0.427  43  PRO AAA CB  
282  C CG  . PRO A 41  ? 1.770 1.530 1.272 0.330  0.050  0.419  43  PRO AAA CG  
283  C CD  . PRO A 41  ? 1.647 1.475 1.204 0.305  0.023  0.360  43  PRO AAA CD  
284  N N   . GLY A 42  ? 1.854 1.365 1.399 0.224  0.090  0.365  44  GLY AAA N   
285  C CA  . GLY A 42  ? 1.946 1.326 1.479 0.211  0.116  0.364  44  GLY AAA CA  
286  C C   . GLY A 42  ? 1.893 1.273 1.467 0.176  0.104  0.309  44  GLY AAA C   
287  O O   . GLY A 42  ? 1.979 1.256 1.542 0.173  0.122  0.301  44  GLY AAA O   
288  N N   . GLU A 43  ? 1.764 1.251 1.380 0.154  0.076  0.272  45  GLU AAA N   
289  C CA  . GLU A 43  ? 1.683 1.189 1.339 0.125  0.061  0.219  45  GLU AAA CA  
290  C C   . GLU A 43  ? 1.601 1.155 1.292 0.059  0.058  0.196  45  GLU AAA C   
291  O O   . GLU A 43  ? 1.598 1.167 1.283 0.039  0.068  0.221  45  GLU AAA O   
292  C CB  . GLU A 43  ? 1.598 1.193 1.272 0.165  0.030  0.196  45  GLU AAA CB  
293  C CG  . GLU A 43  ? 1.656 1.229 1.299 0.235  0.030  0.218  45  GLU AAA CG  
294  C CD  . GLU A 43  ? 1.765 1.214 1.383 0.251  0.053  0.224  45  GLU AAA CD  
295  O OE1 . GLU A 43  ? 1.762 1.175 1.400 0.221  0.054  0.188  45  GLU AAA OE1 
296  O OE2 . GLU A 43  ? 1.856 1.244 1.432 0.294  0.070  0.266  45  GLU AAA OE2 
297  N N   . GLU A 44  ? 1.538 1.120 1.264 0.030  0.044  0.152  46  GLU AAA N   
298  C CA  . GLU A 44  ? 1.448 1.092 1.211 -0.024 0.037  0.126  46  GLU AAA CA  
299  C C   . GLU A 44  ? 1.323 1.075 1.114 -0.010 0.008  0.102  46  GLU AAA C   
300  O O   . GLU A 44  ? 1.280 1.047 1.068 0.032  -0.005 0.094  46  GLU AAA O   
301  C CB  . GLU A 44  ? 1.474 1.064 1.251 -0.070 0.047  0.094  46  GLU AAA CB  
302  C CG  . GLU A 44  ? 1.601 1.077 1.351 -0.092 0.079  0.113  46  GLU AAA CG  
303  C CD  . GLU A 44  ? 1.639 1.063 1.404 -0.143 0.091  0.077  46  GLU AAA CD  
304  O OE1 . GLU A 44  ? 1.582 1.053 1.374 -0.155 0.072  0.037  46  GLU AAA OE1 
305  O OE2 . GLU A 44  ? 1.725 1.061 1.473 -0.173 0.120  0.089  46  GLU AAA OE2 
306  N N   . ARG A 45  ? 1.292 1.008 1.109 -0.167 -0.069 0.039  47  ARG AAA N   
307  C CA  . ARG A 45  ? 1.192 1.017 1.049 -0.151 -0.069 0.024  47  ARG AAA CA  
308  C C   . ARG A 45  ? 1.155 0.984 1.008 -0.114 -0.085 -0.005 47  ARG AAA C   
309  O O   . ARG A 45  ? 1.198 0.987 1.047 -0.125 -0.097 -0.027 47  ARG AAA O   
310  C CB  . ARG A 45  ? 1.166 1.060 1.078 -0.193 -0.063 0.017  47  ARG AAA CB  
311  C CG  . ARG A 45  ? 1.183 1.113 1.111 -0.220 -0.041 0.045  47  ARG AAA CG  
312  C CD  . ARG A 45  ? 1.176 1.155 1.157 -0.267 -0.036 0.040  47  ARG AAA CD  
313  N NE  . ARG A 45  ? 1.187 1.196 1.180 -0.290 -0.010 0.069  47  ARG AAA NE  
314  C CZ  . ARG A 45  ? 1.118 1.205 1.128 -0.279 0.005  0.076  47  ARG AAA CZ  
315  N NH1 . ARG A 45  ? 1.037 1.179 1.060 -0.250 -0.004 0.055  47  ARG AAA NH1 
316  N NH2 . ARG A 45  ? 1.134 1.239 1.147 -0.298 0.030  0.103  47  ARG AAA NH2 
317  N N   . GLU A 46  ? 1.087 0.964 0.939 -0.073 -0.084 -0.006 48  GLU AAA N   
318  C CA  . GLU A 46  ? 1.040 0.949 0.900 -0.040 -0.093 -0.031 48  GLU AAA CA  
319  C C   . GLU A 46  ? 0.903 0.913 0.804 -0.038 -0.086 -0.034 48  GLU AAA C   
320  O O   . GLU A 46  ? 0.892 0.934 0.796 -0.038 -0.079 -0.016 48  GLU AAA O   
321  C CB  . GLU A 46  ? 1.120 0.990 0.944 0.010  -0.098 -0.029 48  GLU AAA CB  
322  C CG  . GLU A 46  ? 1.259 1.020 1.037 0.017  -0.106 -0.034 48  GLU AAA CG  
323  C CD  . GLU A 46  ? 1.346 1.072 1.089 0.075  -0.111 -0.035 48  GLU AAA CD  
324  O OE1 . GLU A 46  ? 1.321 1.117 1.083 0.108  -0.108 -0.031 48  GLU AAA OE1 
325  O OE2 . GLU A 46  ? 1.450 1.079 1.148 0.088  -0.117 -0.041 48  GLU AAA OE2 
326  N N   . CYS A 47  ? 0.817 0.868 0.741 -0.037 -0.088 -0.056 49  CYS AAA N   
327  C CA  . CYS A 47  ? 0.720 0.854 0.676 -0.029 -0.081 -0.061 49  CYS AAA CA  
328  C C   . CYS A 47  ? 0.706 0.858 0.656 0.011  -0.081 -0.060 49  CYS AAA C   
329  O O   . CYS A 47  ? 0.737 0.852 0.666 0.038  -0.086 -0.068 49  CYS AAA O   
330  C CB  . CYS A 47  ? 0.670 0.830 0.643 -0.035 -0.083 -0.081 49  CYS AAA CB  
331  S SG  . CYS A 47  ? 0.583 0.830 0.591 -0.035 -0.072 -0.083 49  CYS AAA SG  
332  N N   . VAL A 48  ? 0.666 0.874 0.635 0.015  -0.077 -0.051 50  VAL AAA N   
333  C CA  . VAL A 48  ? 0.674 0.915 0.648 0.048  -0.079 -0.050 50  VAL AAA CA  
334  C C   . VAL A 48  ? 0.605 0.916 0.616 0.048  -0.072 -0.062 50  VAL AAA C   
335  O O   . VAL A 48  ? 0.602 0.942 0.625 0.075  -0.072 -0.067 50  VAL AAA O   
336  C CB  . VAL A 48  ? 0.690 0.937 0.652 0.054  -0.084 -0.032 50  VAL AAA CB  
337  C CG1 . VAL A 48  ? 0.780 0.949 0.699 0.060  -0.089 -0.016 50  VAL AAA CG1 
338  C CG2 . VAL A 48  ? 0.651 0.934 0.625 0.025  -0.078 -0.026 50  VAL AAA CG2 
339  N N   . ALA A 49  ? 0.539 0.875 0.567 0.020  -0.065 -0.065 51  ALA AAA N   
340  C CA  . ALA A 49  ? 0.484 0.872 0.539 0.017  -0.056 -0.075 51  ALA AAA CA  
341  C C   . ALA A 49  ? 0.460 0.851 0.521 -0.008 -0.050 -0.079 51  ALA AAA C   
342  O O   . ALA A 49  ? 0.466 0.842 0.521 -0.027 -0.051 -0.071 51  ALA AAA O   
343  C CB  . ALA A 49  ? 0.455 0.891 0.530 0.018  -0.057 -0.071 51  ALA AAA CB  
344  N N   . SER A 50  ? 0.435 0.846 0.507 -0.006 -0.042 -0.088 52  SER AAA N   
345  C CA  A SER A 50  ? 0.424 0.845 0.502 -0.023 -0.037 -0.092 52  SER AAA CA  
346  C CA  B SER A 50  ? 0.414 0.836 0.492 -0.023 -0.037 -0.092 52  SER AAA CA  
347  C C   . SER A 50  ? 0.394 0.848 0.486 -0.019 -0.025 -0.096 52  SER AAA C   
348  O O   . SER A 50  ? 0.387 0.855 0.486 -0.004 -0.020 -0.097 52  SER AAA O   
349  C CB  A SER A 50  ? 0.454 0.846 0.518 -0.025 -0.044 -0.100 52  SER AAA CB  
350  C CB  B SER A 50  ? 0.434 0.826 0.498 -0.026 -0.044 -0.100 52  SER AAA CB  
351  O OG  A SER A 50  ? 0.509 0.861 0.559 -0.030 -0.055 -0.097 52  SER AAA OG  
352  O OG  B SER A 50  ? 0.441 0.824 0.492 -0.005 -0.043 -0.109 52  SER AAA OG  
353  N N   . ILE A 51  ? 0.377 0.842 0.474 -0.031 -0.019 -0.095 53  ILE AAA N   
354  C CA  . ILE A 51  ? 0.368 0.853 0.473 -0.031 -0.005 -0.096 53  ILE AAA CA  
355  C C   . ILE A 51  ? 0.364 0.845 0.461 -0.032 -0.002 -0.098 53  ILE AAA C   
356  O O   . ILE A 51  ? 0.373 0.852 0.470 -0.041 -0.008 -0.097 53  ILE AAA O   
357  C CB  . ILE A 51  ? 0.341 0.844 0.459 -0.043 -0.003 -0.094 53  ILE AAA CB  
358  C CG1 . ILE A 51  ? 0.344 0.859 0.471 -0.047 0.011  -0.095 53  ILE AAA CG1 
359  C CG2 . ILE A 51  ? 0.336 0.833 0.447 -0.054 -0.006 -0.091 53  ILE AAA CG2 
360  C CD1 . ILE A 51  ? 0.353 0.885 0.495 -0.059 0.009  -0.097 53  ILE AAA CD1 
361  N N   . GLY A 52  ? 0.384 0.865 0.474 -0.023 0.009  -0.098 54  GLY AAA N   
362  C CA  . GLY A 52  ? 0.392 0.868 0.468 -0.017 0.012  -0.098 54  GLY AAA CA  
363  C C   . GLY A 52  ? 0.386 0.865 0.468 -0.025 0.021  -0.094 54  GLY AAA C   
364  O O   . GLY A 52  ? 0.389 0.872 0.481 -0.036 0.026  -0.093 54  GLY AAA O   
365  N N   . TRP A 53  ? 0.404 0.881 0.475 -0.017 0.020  -0.092 55  TRP AAA N   
366  C CA  . TRP A 53  ? 0.422 0.898 0.492 -0.017 0.028  -0.089 55  TRP AAA CA  
367  C C   . TRP A 53  ? 0.438 0.896 0.503 -0.022 0.045  -0.087 55  TRP AAA C   
368  O O   . TRP A 53  ? 0.441 0.894 0.507 -0.030 0.049  -0.088 55  TRP AAA O   
369  C CB  . TRP A 53  ? 0.418 0.897 0.476 0.000  0.024  -0.087 55  TRP AAA CB  
370  C CG  . TRP A 53  ? 0.451 0.911 0.482 0.017  0.031  -0.083 55  TRP AAA CG  
371  C CD1 . TRP A 53  ? 0.454 0.909 0.472 0.024  0.028  -0.085 55  TRP AAA CD1 
372  C CD2 . TRP A 53  ? 0.485 0.924 0.493 0.033  0.044  -0.075 55  TRP AAA CD2 
373  N NE1 . TRP A 53  ? 0.489 0.925 0.476 0.041  0.040  -0.078 55  TRP AAA NE1 
374  C CE2 . TRP A 53  ? 0.507 0.930 0.487 0.047  0.049  -0.070 55  TRP AAA CE2 
375  C CE3 . TRP A 53  ? 0.514 0.941 0.517 0.040  0.053  -0.071 55  TRP AAA CE3 
376  C CZ2 . TRP A 53  ? 0.564 0.958 0.510 0.066  0.064  -0.058 55  TRP AAA CZ2 
377  C CZ3 . TRP A 53  ? 0.583 0.977 0.552 0.059  0.066  -0.061 55  TRP AAA CZ3 
378  C CH2 . TRP A 53  ? 0.603 0.980 0.545 0.071  0.071  -0.054 55  TRP AAA CH2 
379  N N   . ARG A 54  ? 0.459 0.906 0.515 -0.019 0.055  -0.083 56  ARG AAA N   
380  C CA  . ARG A 54  ? 0.506 0.936 0.562 -0.030 0.073  -0.079 56  ARG AAA CA  
381  C C   . ARG A 54  ? 0.481 0.930 0.564 -0.050 0.070  -0.084 56  ARG AAA C   
382  O O   . ARG A 54  ? 0.519 0.959 0.609 -0.065 0.080  -0.085 56  ARG AAA O   
383  C CB  . ARG A 54  ? 0.570 0.988 0.610 -0.020 0.089  -0.070 56  ARG AAA CB  
384  C CG  . ARG A 54  ? 0.638 1.026 0.642 -0.000 0.096  -0.061 56  ARG AAA CG  
385  C CD  . ARG A 54  ? 0.718 1.098 0.700 0.014  0.109  -0.052 56  ARG AAA CD  
386  N NE  . ARG A 54  ? 0.791 1.134 0.736 0.029  0.125  -0.038 56  ARG AAA NE  
387  C CZ  . ARG A 54  ? 0.795 1.124 0.706 0.047  0.137  -0.027 56  ARG AAA CZ  
388  N NH1 . ARG A 54  ? 0.783 1.134 0.692 0.055  0.134  -0.031 56  ARG AAA NH1 
389  N NH2 . ARG A 54  ? 0.862 1.149 0.733 0.062  0.153  -0.012 56  ARG AAA NH2 
390  N N   . GLY A 55  ? 0.450 0.923 0.547 -0.049 0.056  -0.088 57  GLY AAA N   
391  C CA  . GLY A 55  ? 0.444 0.940 0.566 -0.060 0.050  -0.092 57  GLY AAA CA  
392  C C   . GLY A 55  ? 0.443 0.956 0.581 -0.059 0.062  -0.089 57  GLY AAA C   
393  O O   . GLY A 55  ? 0.430 0.971 0.597 -0.071 0.059  -0.092 57  GLY AAA O   
394  N N   . VAL A 56  ? 0.435 0.939 0.558 -0.045 0.074  -0.083 58  VAL AAA N   
395  C CA  . VAL A 56  ? 0.434 0.955 0.567 -0.040 0.092  -0.077 58  VAL AAA CA  
396  C C   . VAL A 56  ? 0.432 0.971 0.567 -0.020 0.083  -0.081 58  VAL AAA C   
397  O O   . VAL A 56  ? 0.477 1.050 0.642 -0.020 0.088  -0.081 58  VAL AAA O   
398  C CB  . VAL A 56  ? 0.463 0.956 0.564 -0.029 0.112  -0.067 58  VAL AAA CB  
399  C CG1 . VAL A 56  ? 0.480 0.992 0.585 -0.019 0.133  -0.059 58  VAL AAA CG1 
400  C CG2 . VAL A 56  ? 0.472 0.938 0.568 -0.047 0.124  -0.061 58  VAL AAA CG2 
401  N N   . ARG A 57  ? 0.413 0.930 0.520 -0.005 0.070  -0.086 59  ARG AAA N   
402  C CA  . ARG A 57  ? 0.398 0.915 0.496 0.015  0.059  -0.092 59  ARG AAA CA  
403  C C   . ARG A 57  ? 0.371 0.889 0.482 0.008  0.038  -0.096 59  ARG AAA C   
404  O O   . ARG A 57  ? 0.379 0.886 0.488 -0.006 0.028  -0.097 59  ARG AAA O   
405  C CB  . ARG A 57  ? 0.420 0.906 0.477 0.031  0.053  -0.096 59  ARG AAA CB  
406  C CG  . ARG A 57  ? 0.444 0.922 0.475 0.043  0.073  -0.090 59  ARG AAA CG  
407  C CD  . ARG A 57  ? 0.458 0.909 0.450 0.054  0.060  -0.095 59  ARG AAA CD  
408  N NE  . ARG A 57  ? 0.425 0.874 0.427 0.039  0.048  -0.094 59  ARG AAA NE  
409  C CZ  . ARG A 57  ? 0.434 0.873 0.418 0.044  0.030  -0.099 59  ARG AAA CZ  
410  N NH1 . ARG A 57  ? 0.466 0.893 0.420 0.060  0.017  -0.109 59  ARG AAA NH1 
411  N NH2 . ARG A 57  ? 0.406 0.852 0.404 0.033  0.024  -0.097 59  ARG AAA NH2 
412  N N   . THR A 58  ? 0.362 0.893 0.484 0.020  0.034  -0.098 60  THR AAA N   
413  C CA  . THR A 58  ? 0.366 0.891 0.492 0.020  0.015  -0.100 60  THR AAA CA  
414  C C   . THR A 58  ? 0.403 0.906 0.509 0.045  0.008  -0.105 60  THR AAA C   
415  O O   . THR A 58  ? 0.412 0.921 0.511 0.065  0.021  -0.107 60  THR AAA O   
416  C CB  . THR A 58  ? 0.346 0.910 0.505 0.012  0.013  -0.096 60  THR AAA CB  
417  O OG1 . THR A 58  ? 0.340 0.941 0.524 0.026  0.026  -0.095 60  THR AAA OG1 
418  C CG2 . THR A 58  ? 0.317 0.892 0.489 -0.014 0.015  -0.095 60  THR AAA CG2 
419  N N   . TRP A 59  ? 0.451 0.922 0.541 0.044  -0.009 -0.106 61  TRP AAA N   
420  C CA  . TRP A 59  ? 0.497 0.932 0.563 0.067  -0.018 -0.110 61  TRP AAA CA  
421  C C   . TRP A 59  ? 0.504 0.935 0.577 0.068  -0.030 -0.103 61  TRP AAA C   
422  O O   . TRP A 59  ? 0.485 0.917 0.563 0.046  -0.037 -0.096 61  TRP AAA O   
423  C CB  . TRP A 59  ? 0.546 0.930 0.579 0.061  -0.028 -0.119 61  TRP AAA CB  
424  C CG  . TRP A 59  ? 0.627 0.959 0.630 0.080  -0.039 -0.126 61  TRP AAA CG  
425  C CD1 . TRP A 59  ? 0.691 0.996 0.663 0.107  -0.037 -0.139 61  TRP AAA CD1 
426  C CD2 . TRP A 59  ? 0.668 0.957 0.658 0.073  -0.053 -0.122 61  TRP AAA CD2 
427  N NE1 . TRP A 59  ? 0.760 1.005 0.702 0.117  -0.050 -0.144 61  TRP AAA NE1 
428  C CE2 . TRP A 59  ? 0.747 0.981 0.701 0.096  -0.060 -0.132 61  TRP AAA CE2 
429  C CE3 . TRP A 59  ? 0.666 0.955 0.668 0.051  -0.059 -0.109 61  TRP AAA CE3 
430  C CZ2 . TRP A 59  ? 0.798 0.971 0.729 0.095  -0.073 -0.129 61  TRP AAA CZ2 
431  C CZ3 . TRP A 59  ? 0.709 0.944 0.689 0.051  -0.070 -0.103 61  TRP AAA CZ3 
432  C CH2 . TRP A 59  ? 0.777 0.952 0.722 0.072  -0.077 -0.113 61  TRP AAA CH2 
433  N N   . TYR A 60  ? 0.520 0.946 0.588 0.098  -0.032 -0.103 62  TYR AAA N   
434  C CA  . TYR A 60  ? 0.527 0.943 0.591 0.108  -0.046 -0.094 62  TYR AAA CA  
435  C C   . TYR A 60  ? 0.594 0.946 0.620 0.136  -0.052 -0.097 62  TYR AAA C   
436  O O   . TYR A 60  ? 0.611 0.957 0.626 0.160  -0.044 -0.108 62  TYR AAA O   
437  C CB  . TYR A 60  ? 0.495 0.979 0.599 0.122  -0.044 -0.089 62  TYR AAA CB  
438  C CG  . TYR A 60  ? 0.426 0.963 0.564 0.093  -0.039 -0.088 62  TYR AAA CG  
439  C CD1 . TYR A 60  ? 0.412 0.954 0.551 0.072  -0.050 -0.082 62  TYR AAA CD1 
440  C CD2 . TYR A 60  ? 0.388 0.965 0.552 0.087  -0.021 -0.093 62  TYR AAA CD2 
441  C CE1 . TYR A 60  ? 0.373 0.955 0.538 0.047  -0.046 -0.085 62  TYR AAA CE1 
442  C CE2 . TYR A 60  ? 0.350 0.964 0.542 0.059  -0.016 -0.092 62  TYR AAA CE2 
443  C CZ  . TYR A 60  ? 0.349 0.964 0.541 0.039  -0.029 -0.090 62  TYR AAA CZ  
444  O OH  . TYR A 60  ? 0.318 0.960 0.531 0.013  -0.025 -0.093 62  TYR AAA OH  
445  N N   . ALA A 61  ? 0.638 0.939 0.639 0.132  -0.065 -0.089 63  ALA AAA N   
446  C CA  . ALA A 61  ? 0.717 0.950 0.678 0.161  -0.073 -0.089 63  ALA AAA CA  
447  C C   . ALA A 61  ? 0.743 1.012 0.717 0.206  -0.072 -0.086 63  ALA AAA C   
448  O O   . ALA A 61  ? 0.715 1.054 0.727 0.205  -0.072 -0.078 63  ALA AAA O   
449  C CB  . ALA A 61  ? 0.751 0.927 0.687 0.143  -0.084 -0.075 63  ALA AAA CB  
450  N N   . ASP A 62  ? 0.815 1.040 0.760 0.244  -0.070 -0.093 64  ASP AAA N   
451  C CA  . ASP A 62  ? 0.847 1.110 0.804 0.296  -0.067 -0.092 64  ASP AAA CA  
452  C C   . ASP A 62  ? 0.858 1.138 0.823 0.307  -0.082 -0.073 64  ASP AAA C   
453  O O   . ASP A 62  ? 0.819 1.182 0.827 0.330  -0.082 -0.069 64  ASP AAA O   
454  C CB  . ASP A 62  ? 0.942 1.133 0.851 0.338  -0.064 -0.103 64  ASP AAA CB  
455  C CG  . ASP A 62  ? 0.962 1.154 0.863 0.340  -0.049 -0.123 64  ASP AAA CG  
456  O OD1 . ASP A 62  ? 0.906 1.172 0.847 0.319  -0.036 -0.124 64  ASP AAA OD1 
457  O OD2 . ASP A 62  ? 1.052 1.166 0.900 0.363  -0.050 -0.137 64  ASP AAA OD2 
458  N N   . SER A 63  ? 0.909 1.117 0.836 0.291  -0.094 -0.062 65  SER AAA N   
459  C CA  . SER A 63  ? 0.938 1.139 0.852 0.306  -0.109 -0.041 65  SER AAA CA  
460  C C   . SER A 63  ? 0.881 1.175 0.841 0.286  -0.114 -0.034 65  SER AAA C   
461  O O   . SER A 63  ? 0.912 1.224 0.868 0.309  -0.129 -0.021 65  SER AAA O   
462  C CB  . SER A 63  ? 0.997 1.094 0.856 0.286  -0.114 -0.029 65  SER AAA CB  
463  O OG  . SER A 63  ? 0.950 1.050 0.820 0.230  -0.109 -0.030 65  SER AAA OG  
464  N N   . VAL A 64  ? 0.822 1.167 0.818 0.246  -0.105 -0.044 66  VAL AAA N   
465  C CA  . VAL A 64  ? 0.776 1.196 0.809 0.221  -0.110 -0.041 66  VAL AAA CA  
466  C C   . VAL A 64  ? 0.721 1.229 0.813 0.215  -0.100 -0.055 66  VAL AAA C   
467  O O   . VAL A 64  ? 0.692 1.260 0.816 0.193  -0.104 -0.055 66  VAL AAA O   
468  C CB  . VAL A 64  ? 0.762 1.152 0.779 0.175  -0.108 -0.037 66  VAL AAA CB  
469  C CG1 . VAL A 64  ? 0.838 1.142 0.800 0.175  -0.114 -0.021 66  VAL AAA CG1 
470  C CG2 . VAL A 64  ? 0.729 1.114 0.757 0.145  -0.092 -0.051 66  VAL AAA CG2 
471  N N   . LYS A 65  ? 0.717 1.229 0.818 0.234  -0.085 -0.064 67  LYS AAA N   
472  C CA  . LYS A 65  ? 0.686 1.271 0.837 0.224  -0.067 -0.074 67  LYS AAA CA  
473  C C   . LYS A 65  ? 0.657 1.337 0.863 0.239  -0.074 -0.072 67  LYS AAA C   
474  O O   . LYS A 65  ? 0.687 1.375 0.890 0.281  -0.085 -0.066 67  LYS AAA O   
475  C CB  . LYS A 65  ? 0.758 1.316 0.893 0.247  -0.049 -0.083 67  LYS AAA CB  
476  C CG  . LYS A 65  ? 0.751 1.358 0.918 0.230  -0.026 -0.091 67  LYS AAA CG  
477  C CD  . LYS A 65  ? 0.807 1.373 0.941 0.252  -0.009 -0.100 67  LYS AAA CD  
478  C CE  . LYS A 65  ? 0.807 1.432 0.972 0.251  0.018  -0.103 67  LYS AAA CE  
479  N NZ  . LYS A 65  ? 0.781 1.410 0.953 0.206  0.024  -0.103 67  LYS AAA NZ  
480  N N   . GLY A 66  ? 0.591 1.338 0.845 0.206  -0.069 -0.076 68  GLY AAA N   
481  C CA  . GLY A 66  ? 0.557 1.403 0.874 0.208  -0.077 -0.076 68  GLY AAA CA  
482  C C   . GLY A 66  ? 0.565 1.423 0.877 0.196  -0.106 -0.073 68  GLY AAA C   
483  O O   . GLY A 66  ? 0.526 1.465 0.890 0.183  -0.117 -0.077 68  GLY AAA O   
484  N N   . ARG A 67  ? 0.592 1.372 0.844 0.198  -0.118 -0.065 69  ARG AAA N   
485  C CA  . ARG A 67  ? 0.595 1.371 0.823 0.194  -0.145 -0.059 69  ARG AAA CA  
486  C C   . ARG A 67  ? 0.561 1.298 0.763 0.149  -0.142 -0.062 69  ARG AAA C   
487  O O   . ARG A 67  ? 0.554 1.316 0.755 0.134  -0.159 -0.064 69  ARG AAA O   
488  C CB  . ARG A 67  ? 0.657 1.372 0.832 0.235  -0.157 -0.045 69  ARG AAA CB  
489  C CG  . ARG A 67  ? 0.697 1.442 0.892 0.287  -0.159 -0.042 69  ARG AAA CG  
490  C CD  . ARG A 67  ? 0.776 1.464 0.917 0.332  -0.176 -0.026 69  ARG AAA CD  
491  N NE  . ARG A 67  ? 0.823 1.396 0.897 0.321  -0.167 -0.017 69  ARG AAA NE  
492  C CZ  . ARG A 67  ? 0.850 1.368 0.875 0.301  -0.175 -0.005 69  ARG AAA CZ  
493  N NH1 . ARG A 67  ? 0.834 1.396 0.862 0.293  -0.194 -0.001 69  ARG AAA NH1 
494  N NH2 . ARG A 67  ? 0.893 1.313 0.868 0.288  -0.164 0.002  69  ARG AAA NH2 
495  N N   . PHE A 68  ? 0.550 1.227 0.728 0.132  -0.122 -0.062 70  PHE AAA N   
496  C CA  . PHE A 68  ? 0.530 1.171 0.684 0.094  -0.115 -0.064 70  PHE AAA CA  
497  C C   . PHE A 68  ? 0.471 1.138 0.660 0.067  -0.096 -0.076 70  PHE AAA C   
498  O O   . PHE A 68  ? 0.476 1.150 0.682 0.078  -0.081 -0.079 70  PHE AAA O   
499  C CB  . PHE A 68  ? 0.569 1.129 0.675 0.094  -0.107 -0.055 70  PHE AAA CB  
500  C CG  . PHE A 68  ? 0.626 1.141 0.687 0.112  -0.121 -0.039 70  PHE AAA CG  
501  C CD1 . PHE A 68  ? 0.661 1.204 0.720 0.142  -0.141 -0.032 70  PHE AAA CD1 
502  C CD2 . PHE A 68  ? 0.670 1.113 0.689 0.101  -0.114 -0.029 70  PHE AAA CD2 
503  C CE1 . PHE A 68  ? 0.730 1.224 0.740 0.162  -0.152 -0.015 70  PHE AAA CE1 
504  C CE2 . PHE A 68  ? 0.740 1.134 0.714 0.116  -0.123 -0.010 70  PHE AAA CE2 
505  C CZ  . PHE A 68  ? 0.766 1.181 0.731 0.148  -0.141 -0.002 70  PHE AAA CZ  
506  N N   . THR A 69  ? 0.450 1.126 0.641 0.036  -0.096 -0.082 71  THR AAA N   
507  C CA  . THR A 69  ? 0.422 1.103 0.632 0.009  -0.077 -0.090 71  THR AAA CA  
508  C C   . THR A 69  ? 0.428 1.060 0.602 -0.010 -0.071 -0.089 71  THR AAA C   
509  O O   . THR A 69  ? 0.434 1.058 0.586 -0.018 -0.082 -0.088 71  THR AAA O   
510  C CB  . THR A 69  ? 0.418 1.156 0.669 -0.011 -0.081 -0.100 71  THR AAA CB  
511  O OG1 . THR A 69  ? 0.445 1.241 0.739 0.008  -0.085 -0.100 71  THR AAA OG1 
512  C CG2 . THR A 69  ? 0.395 1.128 0.660 -0.038 -0.060 -0.106 71  THR AAA CG2 
513  N N   . ILE A 70  ? 0.415 1.018 0.581 -0.015 -0.054 -0.089 72  ILE AAA N   
514  C CA  . ILE A 70  ? 0.395 0.965 0.539 -0.033 -0.045 -0.089 72  ILE AAA CA  
515  C C   . ILE A 70  ? 0.367 0.953 0.529 -0.050 -0.033 -0.097 72  ILE AAA C   
516  O O   . ILE A 70  ? 0.371 0.977 0.558 -0.048 -0.024 -0.099 72  ILE AAA O   
517  C CB  . ILE A 70  ? 0.403 0.936 0.530 -0.027 -0.039 -0.084 72  ILE AAA CB  
518  C CG1 . ILE A 70  ? 0.402 0.913 0.512 -0.042 -0.034 -0.082 72  ILE AAA CG1 
519  C CG2 . ILE A 70  ? 0.394 0.932 0.534 -0.019 -0.028 -0.089 72  ILE AAA CG2 
520  C CD1 . ILE A 70  ? 0.423 0.903 0.520 -0.041 -0.033 -0.079 72  ILE AAA CD1 
521  N N   . SER A 71  ? 0.362 0.936 0.509 -0.066 -0.032 -0.101 73  SER AAA N   
522  C CA  . SER A 71  ? 0.359 0.930 0.512 -0.082 -0.020 -0.108 73  SER AAA CA  
523  C C   . SER A 71  ? 0.355 0.895 0.478 -0.086 -0.014 -0.108 73  SER AAA C   
524  O O   . SER A 71  ? 0.378 0.910 0.483 -0.080 -0.020 -0.102 73  SER AAA O   
525  C CB  . SER A 71  ? 0.381 0.977 0.552 -0.097 -0.028 -0.118 73  SER AAA CB  
526  O OG  . SER A 71  ? 0.412 1.009 0.563 -0.097 -0.046 -0.121 73  SER AAA OG  
527  N N   . ARG A 72  ? 0.342 0.867 0.462 -0.093 -0.001 -0.112 74  ARG AAA N   
528  C CA  . ARG A 72  ? 0.363 0.864 0.458 -0.091 0.007  -0.112 74  ARG AAA CA  
529  C C   . ARG A 72  ? 0.382 0.862 0.466 -0.101 0.015  -0.122 74  ARG AAA C   
530  O O   . ARG A 72  ? 0.344 0.822 0.443 -0.111 0.020  -0.125 74  ARG AAA O   
531  C CB  . ARG A 72  ? 0.351 0.846 0.446 -0.080 0.015  -0.104 74  ARG AAA CB  
532  C CG  . ARG A 72  ? 0.347 0.836 0.450 -0.077 0.025  -0.103 74  ARG AAA CG  
533  C CD  . ARG A 72  ? 0.354 0.842 0.455 -0.064 0.026  -0.097 74  ARG AAA CD  
534  N NE  . ARG A 72  ? 0.358 0.843 0.449 -0.059 0.028  -0.096 74  ARG AAA NE  
535  C CZ  . ARG A 72  ? 0.336 0.830 0.431 -0.053 0.023  -0.092 74  ARG AAA CZ  
536  N NH1 . ARG A 72  ? 0.326 0.822 0.426 -0.051 0.015  -0.092 74  ARG AAA NH1 
537  N NH2 . ARG A 72  ? 0.341 0.843 0.435 -0.048 0.027  -0.090 74  ARG AAA NH2 
538  N N   . ASP A 73  ? 0.419 0.881 0.476 -0.097 0.017  -0.127 75  ASP AAA N   
539  C CA  . ASP A 73  ? 0.470 0.898 0.504 -0.101 0.026  -0.138 75  ASP AAA CA  
540  C C   . ASP A 73  ? 0.489 0.902 0.507 -0.083 0.041  -0.132 75  ASP AAA C   
541  O O   . ASP A 73  ? 0.511 0.927 0.510 -0.073 0.043  -0.132 75  ASP AAA O   
542  C CB  . ASP A 73  ? 0.504 0.927 0.514 -0.109 0.013  -0.152 75  ASP AAA CB  
543  C CG  . ASP A 73  ? 0.565 0.945 0.548 -0.117 0.018  -0.168 75  ASP AAA CG  
544  O OD1 . ASP A 73  ? 0.589 0.940 0.571 -0.116 0.032  -0.167 75  ASP AAA OD1 
545  O OD2 . ASP A 73  ? 0.586 0.957 0.542 -0.123 0.006  -0.183 75  ASP AAA OD2 
546  N N   . ASN A 74  ? 0.486 0.888 0.511 -0.076 0.051  -0.126 76  ASN AAA N   
547  C CA  . ASN A 74  ? 0.503 0.903 0.521 -0.054 0.062  -0.118 76  ASN AAA CA  
548  C C   . ASN A 74  ? 0.542 0.915 0.529 -0.042 0.072  -0.125 76  ASN AAA C   
549  O O   . ASN A 74  ? 0.523 0.915 0.508 -0.025 0.077  -0.121 76  ASN AAA O   
550  C CB  . ASN A 74  ? 0.513 0.902 0.536 -0.047 0.068  -0.110 76  ASN AAA CB  
551  C CG  . ASN A 74  ? 0.492 0.914 0.538 -0.045 0.060  -0.102 76  ASN AAA CG  
552  O OD1 . ASN A 74  ? 0.474 0.922 0.535 -0.052 0.049  -0.102 76  ASN AAA OD1 
553  N ND2 . ASN A 74  ? 0.547 0.964 0.591 -0.034 0.064  -0.095 76  ASN AAA ND2 
554  N N   . PRO A 75  ? 0.585 0.912 0.547 -0.049 0.075  -0.137 77  PRO AAA N   
555  C CA  . PRO A 75  ? 0.622 0.916 0.547 -0.034 0.085  -0.148 77  PRO AAA CA  
556  C C   . PRO A 75  ? 0.624 0.943 0.537 -0.029 0.082  -0.152 77  PRO AAA C   
557  O O   . PRO A 75  ? 0.657 0.964 0.544 -0.007 0.094  -0.156 77  PRO AAA O   
558  C CB  . PRO A 75  ? 0.673 0.911 0.575 -0.054 0.083  -0.163 77  PRO AAA CB  
559  C CG  . PRO A 75  ? 0.649 0.891 0.582 -0.072 0.082  -0.154 77  PRO AAA CG  
560  C CD  . PRO A 75  ? 0.592 0.897 0.561 -0.073 0.073  -0.142 77  PRO AAA CD  
561  N N   . GLN A 76  ? 0.596 0.947 0.524 -0.046 0.067  -0.151 78  GLN AAA N   
562  C CA  . GLN A 76  ? 0.614 0.985 0.525 -0.044 0.064  -0.152 78  GLN AAA CA  
563  C C   . GLN A 76  ? 0.550 0.968 0.489 -0.040 0.066  -0.133 78  GLN AAA C   
564  O O   . GLN A 76  ? 0.580 1.014 0.505 -0.039 0.066  -0.129 78  GLN AAA O   
565  C CB  . GLN A 76  ? 0.635 1.001 0.536 -0.064 0.044  -0.163 78  GLN AAA CB  
566  C CG  . GLN A 76  ? 0.703 1.022 0.572 -0.073 0.040  -0.186 78  GLN AAA CG  
567  C CD  . GLN A 76  ? 0.790 1.077 0.606 -0.053 0.051  -0.198 78  GLN AAA CD  
568  O OE1 . GLN A 76  ? 0.865 1.170 0.657 -0.043 0.052  -0.196 78  GLN AAA OE1 
569  N NE2 . GLN A 76  ? 0.838 1.075 0.632 -0.045 0.063  -0.208 78  GLN AAA NE2 
570  N N   . ASN A 77  ? 0.489 0.925 0.462 -0.038 0.067  -0.122 79  ASN AAA N   
571  C CA  . ASN A 77  ? 0.450 0.927 0.453 -0.039 0.067  -0.106 79  ASN AAA CA  
572  C C   . ASN A 77  ? 0.444 0.931 0.446 -0.053 0.055  -0.101 79  ASN AAA C   
573  O O   . ASN A 77  ? 0.452 0.958 0.453 -0.053 0.061  -0.090 79  ASN AAA O   
574  C CB  . ASN A 77  ? 0.453 0.955 0.458 -0.022 0.083  -0.099 79  ASN AAA CB  
575  C CG  . ASN A 77  ? 0.458 0.955 0.466 -0.002 0.092  -0.102 79  ASN AAA CG  
576  O OD1 . ASN A 77  ? 0.444 0.924 0.459 -0.001 0.086  -0.104 79  ASN AAA OD1 
577  N ND2 . ASN A 77  ? 0.479 0.990 0.479 0.019  0.109  -0.101 79  ASN AAA ND2 
578  N N   . THR A 78  ? 0.469 0.945 0.471 -0.064 0.040  -0.107 80  THR AAA N   
579  C CA  . THR A 78  ? 0.463 0.946 0.461 -0.072 0.026  -0.103 80  THR AAA CA  
580  C C   . THR A 78  ? 0.442 0.931 0.468 -0.078 0.014  -0.101 80  THR AAA C   
581  O O   . THR A 78  ? 0.453 0.937 0.492 -0.082 0.013  -0.109 80  THR AAA O   
582  C CB  . THR A 78  ? 0.493 0.962 0.456 -0.073 0.019  -0.115 80  THR AAA CB  
583  O OG1 . THR A 78  ? 0.519 0.979 0.451 -0.063 0.035  -0.117 80  THR AAA OG1 
584  C CG2 . THR A 78  ? 0.499 0.976 0.451 -0.076 0.003  -0.109 80  THR AAA CG2 
585  N N   . VAL A 79  ? 0.446 0.943 0.479 -0.079 0.006  -0.090 81  VAL AAA N   
586  C CA  . VAL A 79  ? 0.445 0.948 0.498 -0.079 -0.006 -0.088 81  VAL AAA CA  
587  C C   . VAL A 79  ? 0.464 0.969 0.503 -0.077 -0.021 -0.085 81  VAL AAA C   
588  O O   . VAL A 79  ? 0.499 0.996 0.511 -0.075 -0.019 -0.076 81  VAL AAA O   
589  C CB  . VAL A 79  ? 0.435 0.935 0.503 -0.078 -0.004 -0.079 81  VAL AAA CB  
590  C CG1 . VAL A 79  ? 0.450 0.944 0.507 -0.081 -0.002 -0.066 81  VAL AAA CG1 
591  C CG2 . VAL A 79  ? 0.449 0.949 0.532 -0.072 -0.014 -0.080 81  VAL AAA CG2 
592  N N   . TYR A 80  ? 0.448 0.966 0.502 -0.075 -0.033 -0.091 82  TYR AAA N   
593  C CA  . TYR A 80  ? 0.471 1.001 0.515 -0.068 -0.052 -0.090 82  TYR AAA CA  
594  C C   . TYR A 80  ? 0.477 1.012 0.538 -0.056 -0.059 -0.082 82  TYR AAA C   
595  O O   . TYR A 80  ? 0.462 1.002 0.549 -0.055 -0.053 -0.084 82  TYR AAA O   
596  C CB  . TYR A 80  ? 0.461 1.012 0.514 -0.077 -0.062 -0.107 82  TYR AAA CB  
597  C CG  . TYR A 80  ? 0.474 1.009 0.503 -0.087 -0.056 -0.118 82  TYR AAA CG  
598  C CD1 . TYR A 80  ? 0.515 1.041 0.502 -0.084 -0.064 -0.121 82  TYR AAA CD1 
599  C CD2 . TYR A 80  ? 0.459 0.982 0.499 -0.097 -0.041 -0.126 82  TYR AAA CD2 
600  C CE1 . TYR A 80  ? 0.550 1.056 0.508 -0.089 -0.057 -0.134 82  TYR AAA CE1 
601  C CE2 . TYR A 80  ? 0.493 0.993 0.505 -0.102 -0.034 -0.138 82  TYR AAA CE2 
602  C CZ  . TYR A 80  ? 0.554 1.046 0.525 -0.098 -0.043 -0.143 82  TYR AAA CZ  
603  O OH  . TYR A 80  ? 0.605 1.069 0.542 -0.099 -0.035 -0.157 82  TYR AAA OH  
604  N N   . LEU A 81  ? 0.506 1.037 0.548 -0.042 -0.073 -0.072 83  LEU AAA N   
605  C CA  . LEU A 81  ? 0.519 1.055 0.572 -0.023 -0.084 -0.066 83  LEU AAA CA  
606  C C   . LEU A 81  ? 0.535 1.101 0.585 -0.010 -0.106 -0.068 83  LEU AAA C   
607  O O   . LEU A 81  ? 0.571 1.118 0.582 0.001  -0.115 -0.057 83  LEU AAA O   
608  C CB  . LEU A 81  ? 0.547 1.038 0.573 -0.015 -0.079 -0.049 83  LEU AAA CB  
609  C CG  . LEU A 81  ? 0.570 1.049 0.600 0.008  -0.088 -0.044 83  LEU AAA CG  
610  C CD1 . LEU A 81  ? 0.548 1.044 0.613 0.010  -0.081 -0.055 83  LEU AAA CD1 
611  C CD2 . LEU A 81  ? 0.606 1.028 0.603 0.011  -0.084 -0.027 83  LEU AAA CD2 
612  N N   . GLN A 82  ? 0.510 1.122 0.599 -0.014 -0.113 -0.082 84  GLN AAA N   
613  C CA  . GLN A 82  ? 0.535 1.193 0.638 -0.001 -0.138 -0.086 84  GLN AAA CA  
614  C C   . GLN A 82  ? 0.547 1.204 0.652 0.032  -0.145 -0.073 84  GLN AAA C   
615  O O   . GLN A 82  ? 0.523 1.186 0.657 0.039  -0.132 -0.073 84  GLN AAA O   
616  C CB  . GLN A 82  ? 0.507 1.219 0.664 -0.019 -0.140 -0.103 84  GLN AAA CB  
617  C CG  . GLN A 82  ? 0.527 1.298 0.706 -0.013 -0.169 -0.112 84  GLN AAA CG  
618  C CD  . GLN A 82  ? 0.576 1.333 0.707 -0.017 -0.188 -0.117 84  GLN AAA CD  
619  O OE1 . GLN A 82  ? 0.581 1.311 0.689 -0.040 -0.181 -0.127 84  GLN AAA OE1 
620  N NE2 . GLN A 82  ? 0.617 1.388 0.727 0.010  -0.213 -0.109 84  GLN AAA NE2 
621  N N   . MET A 83  ? 0.590 1.233 0.657 0.054  -0.162 -0.061 85  MET AAA N   
622  C CA  . MET A 83  ? 0.639 1.268 0.695 0.090  -0.170 -0.046 85  MET AAA CA  
623  C C   . MET A 83  ? 0.681 1.370 0.753 0.114  -0.199 -0.048 85  MET AAA C   
624  O O   . MET A 83  ? 0.709 1.397 0.744 0.117  -0.218 -0.046 85  MET AAA O   
625  C CB  . MET A 83  ? 0.702 1.256 0.695 0.099  -0.165 -0.025 85  MET AAA CB  
626  C CG  . MET A 83  ? 0.697 1.201 0.680 0.073  -0.139 -0.022 85  MET AAA CG  
627  S SD  . MET A 83  ? 0.817 1.250 0.735 0.067  -0.130 0.001  85  MET AAA SD  
628  C CE  . MET A 83  ? 0.886 1.270 0.770 0.106  -0.141 0.022  85  MET AAA CE  
629  N N   . ASN A 84  ? 0.674 1.417 0.798 0.132  -0.203 -0.054 86  ASN AAA N   
630  C CA  . ASN A 84  ? 0.676 1.495 0.833 0.157  -0.232 -0.058 86  ASN AAA CA  
631  C C   . ASN A 84  ? 0.711 1.516 0.857 0.208  -0.236 -0.042 86  ASN AAA C   
632  O O   . ASN A 84  ? 0.705 1.460 0.842 0.217  -0.213 -0.036 86  ASN AAA O   
633  C CB  . ASN A 84  ? 0.637 1.542 0.873 0.135  -0.230 -0.077 86  ASN AAA CB  
634  C CG  . ASN A 84  ? 0.629 1.534 0.871 0.086  -0.224 -0.093 86  ASN AAA CG  
635  O OD1 . ASN A 84  ? 0.666 1.526 0.856 0.073  -0.229 -0.093 86  ASN AAA OD1 
636  N ND2 . ASN A 84  ? 0.602 1.552 0.904 0.060  -0.210 -0.106 86  ASN AAA ND2 
637  N N   . ASN A 85  ? 0.769 1.615 0.913 0.243  -0.266 -0.037 87  ASN AAA N   
638  C CA  . ASN A 85  ? 0.829 1.673 0.966 0.300  -0.274 -0.022 87  ASN AAA CA  
639  C C   . ASN A 85  ? 0.880 1.604 0.936 0.316  -0.261 -0.001 87  ASN AAA C   
640  O O   . ASN A 85  ? 0.915 1.601 0.966 0.347  -0.249 0.006  87  ASN AAA O   
641  C CB  . ASN A 85  ? 0.799 1.698 1.005 0.313  -0.258 -0.031 87  ASN AAA CB  
642  C CG  . ASN A 85  ? 0.850 1.787 1.071 0.376  -0.272 -0.022 87  ASN AAA CG  
643  O OD1 . ASN A 85  ? 0.895 1.842 1.089 0.409  -0.302 -0.012 87  ASN AAA OD1 
644  N ND2 . ASN A 85  ? 0.842 1.804 1.104 0.396  -0.251 -0.026 87  ASN AAA ND2 
645  N N   . LEU A 86  ? 0.903 1.569 0.900 0.296  -0.263 0.009  88  LEU AAA N   
646  C CA  . LEU A 86  ? 0.974 1.527 0.896 0.301  -0.248 0.031  88  LEU AAA CA  
647  C C   . LEU A 86  ? 1.049 1.566 0.933 0.360  -0.262 0.052  88  LEU AAA C   
648  O O   . LEU A 86  ? 1.080 1.646 0.958 0.391  -0.292 0.056  88  LEU AAA O   
649  C CB  . LEU A 86  ? 1.007 1.525 0.876 0.273  -0.248 0.040  88  LEU AAA CB  
650  C CG  . LEU A 86  ? 0.973 1.468 0.850 0.220  -0.221 0.030  88  LEU AAA CG  
651  C CD1 . LEU A 86  ? 0.905 1.480 0.836 0.190  -0.226 0.004  88  LEU AAA CD1 
652  C CD2 . LEU A 86  ? 1.038 1.465 0.848 0.205  -0.210 0.049  88  LEU AAA CD2 
653  N N   . LYS A 87  ? 1.075 1.509 0.932 0.375  -0.244 0.062  89  LYS AAA N   
654  C CA  . LYS A 87  ? 1.174 1.541 0.976 0.430  -0.253 0.085  89  LYS AAA CA  
655  C C   . LYS A 87  ? 1.229 1.474 0.952 0.413  -0.238 0.109  89  LYS AAA C   
656  O O   . LYS A 87  ? 1.174 1.395 0.900 0.360  -0.218 0.103  89  LYS AAA O   
657  C CB  . LYS A 87  ? 1.194 1.558 1.024 0.467  -0.246 0.076  89  LYS AAA CB  
658  C CG  . LYS A 87  ? 1.201 1.489 1.024 0.441  -0.217 0.068  89  LYS AAA CG  
659  C CD  . LYS A 87  ? 1.215 1.515 1.067 0.479  -0.210 0.054  89  LYS AAA CD  
660  C CE  . LYS A 87  ? 1.322 1.576 1.132 0.549  -0.222 0.070  89  LYS AAA CE  
661  N NZ  . LYS A 87  ? 1.423 1.528 1.147 0.551  -0.215 0.090  89  LYS AAA NZ  
662  N N   . SER A 88  ? 1.001 1.515 1.106 0.067  -0.323 0.367  90  SER AAA N   
663  C CA  . SER A 88  ? 1.028 1.518 1.070 0.078  -0.301 0.373  90  SER AAA CA  
664  C C   . SER A 88  ? 0.998 1.443 1.026 0.071  -0.253 0.350  90  SER AAA C   
665  O O   . SER A 88  ? 1.032 1.455 1.002 0.072  -0.241 0.341  90  SER AAA O   
666  C CB  . SER A 88  ? 1.045 1.549 1.106 0.102  -0.292 0.422  90  SER AAA CB  
667  O OG  . SER A 88  ? 1.012 1.501 1.137 0.110  -0.250 0.441  90  SER AAA OG  
668  N N   . GLY A 89  ? 0.954 1.385 1.034 0.064  -0.228 0.342  91  GLY AAA N   
669  C CA  . GLY A 89  ? 0.925 1.314 0.997 0.057  -0.186 0.320  91  GLY AAA CA  
670  C C   . GLY A 89  ? 0.893 1.271 0.932 0.037  -0.193 0.277  91  GLY AAA C   
671  O O   . GLY A 89  ? 0.852 1.200 0.886 0.029  -0.163 0.257  91  GLY AAA O   
672  N N   . ASP A 90  ? 0.893 1.294 0.910 0.029  -0.232 0.262  92  ASP AAA N   
673  C CA  . ASP A 90  ? 0.873 1.264 0.854 0.012  -0.240 0.222  92  ASP AAA CA  
674  C C   . ASP A 90  ? 0.905 1.281 0.817 0.015  -0.236 0.216  92  ASP AAA C   
675  O O   . ASP A 90  ? 0.917 1.278 0.800 0.004  -0.230 0.187  92  ASP AAA O   
676  C CB  . ASP A 90  ? 0.866 1.282 0.857 0.003  -0.281 0.209  92  ASP AAA CB  
677  C CG  . ASP A 90  ? 0.831 1.257 0.891 -0.002 -0.280 0.210  92  ASP AAA CG  
678  O OD1 . ASP A 90  ? 0.794 1.200 0.875 -0.003 -0.246 0.203  92  ASP AAA OD1 
679  O OD2 . ASP A 90  ? 0.845 1.301 0.939 -0.005 -0.313 0.217  92  ASP AAA OD2 
680  N N   . THR A 91  ? 0.938 1.319 0.826 0.031  -0.238 0.244  93  THR AAA N   
681  C CA  . THR A 91  ? 0.972 1.339 0.794 0.039  -0.230 0.245  93  THR AAA CA  
682  C C   . THR A 91  ? 0.947 1.284 0.766 0.031  -0.190 0.231  93  THR AAA C   
683  O O   . THR A 91  ? 0.932 1.255 0.790 0.033  -0.160 0.244  93  THR AAA O   
684  C CB  . THR A 91  ? 1.010 1.387 0.820 0.060  -0.231 0.285  93  THR AAA CB  
685  O OG1 . THR A 91  ? 1.049 1.414 0.789 0.069  -0.226 0.286  93  THR AAA OG1 
686  C CG2 . THR A 91  ? 0.999 1.364 0.856 0.070  -0.193 0.313  93  THR AAA CG2 
687  N N   . ALA A 92  ? 0.939 1.266 0.716 0.024  -0.190 0.206  94  ALA AAA N   
688  C CA  . ALA A 92  ? 0.922 1.227 0.698 0.014  -0.158 0.191  94  ALA AAA CA  
689  C C   . ALA A 92  ? 0.925 1.225 0.651 0.009  -0.165 0.167  94  ALA AAA C   
690  O O   . ALA A 92  ? 0.935 1.246 0.630 0.011  -0.196 0.158  94  ALA AAA O   
691  C CB  . ALA A 92  ? 0.877 1.177 0.705 -0.001 -0.148 0.174  94  ALA AAA CB  
692  N N   . VAL A 93  ? 0.912 1.197 0.634 0.004  -0.137 0.160  95  VAL AAA N   
693  C CA  . VAL A 93  ? 0.921 1.201 0.608 -0.002 -0.136 0.137  95  VAL AAA CA  
694  C C   . VAL A 93  ? 0.877 1.161 0.596 -0.019 -0.144 0.109  95  VAL AAA C   
695  O O   . VAL A 93  ? 0.860 1.142 0.623 -0.029 -0.127 0.106  95  VAL AAA O   
696  C CB  . VAL A 93  ? 0.927 1.193 0.607 0.001  -0.101 0.146  95  VAL AAA CB  
697  C CG1 . VAL A 93  ? 0.925 1.186 0.577 -0.003 -0.096 0.127  95  VAL AAA CG1 
698  C CG2 . VAL A 93  ? 0.976 1.235 0.626 0.021  -0.089 0.177  95  VAL AAA CG2 
699  N N   . TYR A 94  ? 0.873 1.164 0.572 -0.023 -0.169 0.090  96  TYR AAA N   
700  C CA  . TYR A 94  ? 0.838 1.134 0.566 -0.037 -0.177 0.066  96  TYR AAA CA  
701  C C   . TYR A 94  ? 0.832 1.120 0.540 -0.041 -0.162 0.048  96  TYR AAA C   
702  O O   . TYR A 94  ? 0.877 1.157 0.536 -0.035 -0.166 0.043  96  TYR AAA O   
703  C CB  . TYR A 94  ? 0.849 1.156 0.576 -0.039 -0.211 0.057  96  TYR AAA CB  
704  C CG  . TYR A 94  ? 0.842 1.163 0.613 -0.037 -0.224 0.073  96  TYR AAA CG  
705  C CD1 . TYR A 94  ? 0.875 1.201 0.637 -0.024 -0.228 0.099  96  TYR AAA CD1 
706  C CD2 . TYR A 94  ? 0.800 1.130 0.621 -0.045 -0.229 0.066  96  TYR AAA CD2 
707  C CE1 . TYR A 94  ? 0.859 1.200 0.665 -0.021 -0.238 0.118  96  TYR AAA CE1 
708  C CE2 . TYR A 94  ? 0.786 1.130 0.651 -0.041 -0.236 0.085  96  TYR AAA CE2 
709  C CZ  . TYR A 94  ? 0.811 1.160 0.670 -0.029 -0.241 0.111  96  TYR AAA CZ  
710  O OH  . TYR A 94  ? 0.796 1.159 0.702 -0.024 -0.247 0.133  96  TYR AAA OH  
711  N N   . TYR A 95  ? 0.770 1.059 0.513 -0.052 -0.145 0.041  97  TYR AAA N   
712  C CA  . TYR A 95  ? 0.746 1.035 0.485 -0.057 -0.131 0.027  97  TYR AAA CA  
713  C C   . TYR A 95  ? 0.707 1.003 0.467 -0.066 -0.143 0.007  97  TYR AAA C   
714  O O   . TYR A 95  ? 0.673 0.975 0.469 -0.071 -0.147 0.006  97  TYR AAA O   
715  C CB  . TYR A 95  ? 0.727 1.015 0.494 -0.063 -0.107 0.034  97  TYR AAA CB  
716  C CG  . TYR A 95  ? 0.761 1.041 0.522 -0.056 -0.091 0.057  97  TYR AAA CG  
717  C CD1 . TYR A 95  ? 0.776 1.051 0.556 -0.054 -0.091 0.071  97  TYR AAA CD1 
718  C CD2 . TYR A 95  ? 0.792 1.067 0.530 -0.049 -0.072 0.067  97  TYR AAA CD2 
719  C CE1 . TYR A 95  ? 0.810 1.077 0.588 -0.047 -0.074 0.094  97  TYR AAA CE1 
720  C CE2 . TYR A 95  ? 0.819 1.086 0.555 -0.041 -0.054 0.091  97  TYR AAA CE2 
721  C CZ  . TYR A 95  ? 0.827 1.090 0.583 -0.040 -0.055 0.104  97  TYR AAA CZ  
722  O OH  . TYR A 95  ? 0.850 1.103 0.606 -0.031 -0.035 0.129  97  TYR AAA OH  
723  N N   . CYS A 96  ? 0.714 1.007 0.450 -0.065 -0.145 -0.007 98  CYS AAA N   
724  C CA  . CYS A 96  ? 0.700 0.999 0.459 -0.072 -0.147 -0.024 98  CYS AAA CA  
725  C C   . CYS A 96  ? 0.659 0.965 0.435 -0.076 -0.126 -0.023 98  CYS AAA C   
726  O O   . CYS A 96  ? 0.664 0.968 0.426 -0.072 -0.110 -0.013 98  CYS AAA O   
727  C CB  . CYS A 96  ? 0.753 1.042 0.481 -0.069 -0.159 -0.039 98  CYS AAA CB  
728  S SG  . CYS A 96  ? 0.793 1.079 0.511 -0.068 -0.137 -0.048 98  CYS AAA SG  
729  N N   . ALA A 97  ? 0.616 0.932 0.425 -0.083 -0.125 -0.030 99  ALA AAA N   
730  C CA  . ALA A 97  ? 0.579 0.906 0.409 -0.088 -0.110 -0.030 99  ALA AAA CA  
731  C C   . ALA A 97  ? 0.548 0.884 0.391 -0.089 -0.111 -0.041 99  ALA AAA C   
732  O O   . ALA A 97  ? 0.548 0.883 0.400 -0.089 -0.122 -0.047 99  ALA AAA O   
733  C CB  . ALA A 97  ? 0.563 0.891 0.416 -0.095 -0.108 -0.025 99  ALA AAA CB  
734  N N   . ALA A 98  ? 0.534 0.883 0.385 -0.090 -0.099 -0.039 100 ALA AAA N   
735  C CA  . ALA A 98  ? 0.509 0.870 0.374 -0.089 -0.096 -0.045 100 ALA AAA CA  
736  C C   . ALA A 98  ? 0.486 0.864 0.376 -0.096 -0.093 -0.043 100 ALA AAA C   
737  O O   . ALA A 98  ? 0.481 0.868 0.379 -0.101 -0.087 -0.035 100 ALA AAA O   
738  C CB  . ALA A 98  ? 0.533 0.892 0.383 -0.082 -0.083 -0.044 100 ALA AAA CB  
739  N N   . SER A 99  ? 0.464 0.847 0.366 -0.095 -0.098 -0.048 101 SER AAA N   
740  C CA  . SER A 99  ? 0.449 0.849 0.367 -0.099 -0.098 -0.048 101 SER AAA CA  
741  C C   . SER A 99  ? 0.437 0.852 0.362 -0.091 -0.092 -0.046 101 SER AAA C   
742  O O   . SER A 99  ? 0.435 0.845 0.363 -0.084 -0.092 -0.050 101 SER AAA O   
743  C CB  . SER A 99  ? 0.448 0.838 0.367 -0.100 -0.105 -0.054 101 SER AAA CB  
744  O OG  . SER A 99  ? 0.433 0.836 0.357 -0.105 -0.107 -0.055 101 SER AAA OG  
745  N N   . VAL A 100 ? 0.423 0.857 0.357 -0.091 -0.085 -0.038 102 VAL AAA N   
746  C CA  . VAL A 100 ? 0.410 0.858 0.353 -0.081 -0.073 -0.033 102 VAL AAA CA  
747  C C   . VAL A 100 ? 0.383 0.851 0.340 -0.078 -0.077 -0.030 102 VAL AAA C   
748  O O   . VAL A 100 ? 0.373 0.853 0.334 -0.086 -0.088 -0.030 102 VAL AAA O   
749  C CB  . VAL A 100 ? 0.420 0.880 0.369 -0.079 -0.061 -0.021 102 VAL AAA CB  
750  C CG1 . VAL A 100 ? 0.444 0.880 0.370 -0.079 -0.055 -0.022 102 VAL AAA CG1 
751  C CG2 . VAL A 100 ? 0.407 0.895 0.380 -0.089 -0.066 -0.011 102 VAL AAA CG2 
752  N N   . GLY A 101 ? 0.379 0.850 0.342 -0.066 -0.068 -0.027 103 GLY AAA N   
753  C CA  . GLY A 101 ? 0.380 0.869 0.354 -0.059 -0.068 -0.022 103 GLY AAA CA  
754  C C   . GLY A 101 ? 0.395 0.877 0.358 -0.062 -0.079 -0.029 103 GLY AAA C   
755  O O   . GLY A 101 ? 0.403 0.904 0.366 -0.060 -0.085 -0.025 103 GLY AAA O   
756  N N   . ASN A 102 ? 0.416 0.871 0.370 -0.066 -0.083 -0.038 104 ASN AAA N   
757  C CA  . ASN A 102 ? 0.421 0.863 0.364 -0.068 -0.090 -0.045 104 ASN AAA CA  
758  C C   . ASN A 102 ? 0.413 0.841 0.365 -0.057 -0.083 -0.044 104 ASN AAA C   
759  O O   . ASN A 102 ? 0.405 0.818 0.364 -0.059 -0.083 -0.048 104 ASN AAA O   
760  C CB  . ASN A 102 ? 0.430 0.855 0.364 -0.080 -0.098 -0.051 104 ASN AAA CB  
761  C CG  . ASN A 102 ? 0.454 0.863 0.376 -0.081 -0.102 -0.057 104 ASN AAA CG  
762  O OD1 . ASN A 102 ? 0.450 0.860 0.367 -0.072 -0.098 -0.056 104 ASN AAA OD1 
763  N ND2 . ASN A 102 ? 0.467 0.860 0.383 -0.090 -0.106 -0.061 104 ASN AAA ND2 
764  N N   . TYR A 103 ? 0.432 0.865 0.384 -0.047 -0.077 -0.039 105 TYR AAA N   
765  C CA  . TYR A 103 ? 0.436 0.859 0.403 -0.034 -0.066 -0.034 105 TYR AAA CA  
766  C C   . TYR A 103 ? 0.443 0.845 0.403 -0.033 -0.066 -0.036 105 TYR AAA C   
767  O O   . TYR A 103 ? 0.453 0.848 0.427 -0.021 -0.054 -0.029 105 TYR AAA O   
768  C CB  . TYR A 103 ? 0.436 0.877 0.406 -0.019 -0.055 -0.023 105 TYR AAA CB  
769  C CG  . TYR A 103 ? 0.433 0.892 0.416 -0.018 -0.050 -0.017 105 TYR AAA CG  
770  C CD1 . TYR A 103 ? 0.442 0.924 0.417 -0.023 -0.057 -0.014 105 TYR AAA CD1 
771  C CD2 . TYR A 103 ? 0.426 0.877 0.433 -0.012 -0.037 -0.014 105 TYR AAA CD2 
772  C CE1 . TYR A 103 ? 0.433 0.931 0.423 -0.019 -0.049 -0.006 105 TYR AAA CE1 
773  C CE2 . TYR A 103 ? 0.432 0.893 0.448 -0.009 -0.029 -0.009 105 TYR AAA CE2 
774  C CZ  . TYR A 103 ? 0.433 0.918 0.441 -0.011 -0.033 -0.003 105 TYR AAA CZ  
775  O OH  . TYR A 103 ? 0.429 0.924 0.450 -0.005 -0.021 0.005  105 TYR AAA OH  
776  N N   . GLY A 104 ? 0.444 0.837 0.388 -0.044 -0.076 -0.045 106 GLY AAA N   
777  C CA  . GLY A 104 ? 0.459 0.830 0.395 -0.043 -0.074 -0.047 106 GLY AAA CA  
778  C C   . GLY A 104 ? 0.449 0.808 0.401 -0.050 -0.079 -0.047 106 GLY AAA C   
779  O O   . GLY A 104 ? 0.438 0.803 0.408 -0.053 -0.084 -0.047 106 GLY AAA O   
780  N N   . LEU A 105 ? 0.463 0.804 0.408 -0.052 -0.079 -0.049 107 LEU AAA N   
781  C CA  . LEU A 105 ? 0.467 0.797 0.428 -0.056 -0.084 -0.045 107 LEU AAA CA  
782  C C   . LEU A 105 ? 0.480 0.798 0.421 -0.066 -0.088 -0.051 107 LEU AAA C   
783  O O   . LEU A 105 ? 0.506 0.804 0.443 -0.062 -0.081 -0.049 107 LEU AAA O   
784  C CB  . LEU A 105 ? 0.467 0.787 0.452 -0.044 -0.073 -0.035 107 LEU AAA CB  
785  C CG  . LEU A 105 ? 0.468 0.785 0.482 -0.046 -0.080 -0.027 107 LEU AAA CG  
786  C CD1 . LEU A 105 ? 0.456 0.788 0.484 -0.054 -0.096 -0.030 107 LEU AAA CD1 
787  C CD2 . LEU A 105 ? 0.475 0.786 0.521 -0.033 -0.067 -0.013 107 LEU AAA CD2 
788  N N   . PRO A 106 ? 0.464 0.792 0.395 -0.077 -0.097 -0.056 108 PRO AAA N   
789  C CA  . PRO A 106 ? 0.474 0.790 0.392 -0.087 -0.099 -0.059 108 PRO AAA CA  
790  C C   . PRO A 106 ? 0.468 0.770 0.394 -0.087 -0.099 -0.052 108 PRO AAA C   
791  O O   . PRO A 106 ? 0.446 0.757 0.387 -0.084 -0.105 -0.046 108 PRO AAA O   
792  C CB  . PRO A 106 ? 0.475 0.809 0.389 -0.096 -0.105 -0.062 108 PRO AAA CB  
793  C CG  . PRO A 106 ? 0.460 0.808 0.384 -0.090 -0.107 -0.058 108 PRO AAA CG  
794  C CD  . PRO A 106 ? 0.455 0.802 0.390 -0.080 -0.102 -0.056 108 PRO AAA CD  
795  N N   . TRP A 107 ? 0.483 0.765 0.402 -0.091 -0.094 -0.053 109 TRP AAA N   
796  C CA  . TRP A 107 ? 0.492 0.761 0.421 -0.090 -0.092 -0.042 109 TRP AAA CA  
797  C C   . TRP A 107 ? 0.516 0.769 0.435 -0.100 -0.088 -0.045 109 TRP AAA C   
798  O O   . TRP A 107 ? 0.540 0.784 0.467 -0.098 -0.085 -0.034 109 TRP AAA O   
799  C CB  . TRP A 107 ? 0.498 0.751 0.440 -0.078 -0.081 -0.035 109 TRP AAA CB  
800  C CG  . TRP A 107 ? 0.511 0.740 0.436 -0.074 -0.068 -0.043 109 TRP AAA CG  
801  C CD1 . TRP A 107 ? 0.510 0.740 0.428 -0.065 -0.062 -0.047 109 TRP AAA CD1 
802  C CD2 . TRP A 107 ? 0.540 0.737 0.448 -0.078 -0.057 -0.049 109 TRP AAA CD2 
803  N NE1 . TRP A 107 ? 0.547 0.747 0.439 -0.063 -0.050 -0.056 109 TRP AAA NE1 
804  C CE2 . TRP A 107 ? 0.565 0.743 0.450 -0.071 -0.047 -0.059 109 TRP AAA CE2 
805  C CE3 . TRP A 107 ? 0.553 0.733 0.462 -0.085 -0.053 -0.047 109 TRP AAA CE3 
806  C CZ2 . TRP A 107 ? 0.607 0.746 0.467 -0.073 -0.035 -0.071 109 TRP AAA CZ2 
807  C CZ3 . TRP A 107 ? 0.592 0.734 0.483 -0.088 -0.040 -0.057 109 TRP AAA CZ3 
808  C CH2 . TRP A 107 ? 0.623 0.744 0.487 -0.082 -0.032 -0.070 109 TRP AAA CH2 
809  N N   . ALA A 108 ? 0.526 0.778 0.432 -0.111 -0.089 -0.057 110 ALA AAA N   
810  C CA  . ALA A 108 ? 0.554 0.793 0.458 -0.124 -0.086 -0.060 110 ALA AAA CA  
811  C C   . ALA A 108 ? 0.538 0.801 0.450 -0.131 -0.092 -0.055 110 ALA AAA C   
812  O O   . ALA A 108 ? 0.512 0.800 0.423 -0.130 -0.099 -0.058 110 ALA AAA O   
813  C CB  . ALA A 108 ? 0.584 0.806 0.473 -0.133 -0.086 -0.077 110 ALA AAA CB  
814  N N   . HIS A 109 ? 0.551 0.807 0.471 -0.137 -0.087 -0.047 111 HIS AAA N   
815  C CA  . HIS A 109 ? 0.541 0.816 0.467 -0.140 -0.087 -0.037 111 HIS AAA CA  
816  C C   . HIS A 109 ? 0.536 0.831 0.469 -0.151 -0.093 -0.045 111 HIS AAA C   
817  O O   . HIS A 109 ? 0.530 0.848 0.463 -0.147 -0.094 -0.039 111 HIS AAA O   
818  C CB  . HIS A 109 ? 0.554 0.813 0.489 -0.142 -0.076 -0.024 111 HIS AAA CB  
819  C CG  . HIS A 109 ? 0.571 0.814 0.521 -0.159 -0.071 -0.031 111 HIS AAA CG  
820  N ND1 . HIS A 109 ? 0.573 0.832 0.541 -0.172 -0.071 -0.029 111 HIS AAA ND1 
821  C CD2 . HIS A 109 ? 0.592 0.805 0.544 -0.166 -0.066 -0.041 111 HIS AAA CD2 
822  C CE1 . HIS A 109 ? 0.591 0.832 0.574 -0.188 -0.069 -0.038 111 HIS AAA CE1 
823  N NE2 . HIS A 109 ? 0.614 0.824 0.583 -0.185 -0.066 -0.047 111 HIS AAA NE2 
824  N N   . PHE A 110 ? 0.547 0.834 0.483 -0.164 -0.096 -0.058 112 PHE AAA N   
825  C CA  . PHE A 110 ? 0.551 0.862 0.500 -0.176 -0.106 -0.064 112 PHE AAA CA  
826  C C   . PHE A 110 ? 0.526 0.862 0.465 -0.167 -0.114 -0.067 112 PHE AAA C   
827  O O   . PHE A 110 ? 0.514 0.877 0.467 -0.174 -0.121 -0.066 112 PHE AAA O   
828  C CB  . PHE A 110 ? 0.586 0.877 0.536 -0.193 -0.113 -0.080 112 PHE AAA CB  
829  C CG  . PHE A 110 ? 0.612 0.873 0.534 -0.188 -0.112 -0.094 112 PHE AAA CG  
830  C CD1 . PHE A 110 ? 0.609 0.878 0.509 -0.179 -0.119 -0.102 112 PHE AAA CD1 
831  C CD2 . PHE A 110 ? 0.649 0.870 0.566 -0.190 -0.101 -0.097 112 PHE AAA CD2 
832  C CE1 . PHE A 110 ? 0.647 0.885 0.519 -0.171 -0.115 -0.113 112 PHE AAA CE1 
833  C CE2 . PHE A 110 ? 0.677 0.867 0.568 -0.182 -0.097 -0.109 112 PHE AAA CE2 
834  C CZ  . PHE A 110 ? 0.672 0.870 0.539 -0.173 -0.103 -0.117 112 PHE AAA CZ  
835  N N   . GLU A 111 ? 0.517 0.845 0.439 -0.153 -0.112 -0.069 113 GLU AAA N   
836  C CA  . GLU A 111 ? 0.506 0.854 0.422 -0.143 -0.116 -0.070 113 GLU AAA CA  
837  C C   . GLU A 111 ? 0.499 0.866 0.422 -0.135 -0.112 -0.059 113 GLU AAA C   
838  O O   . GLU A 111 ? 0.484 0.868 0.407 -0.127 -0.113 -0.059 113 GLU AAA O   
839  C CB  . GLU A 111 ? 0.518 0.848 0.419 -0.131 -0.113 -0.075 113 GLU AAA CB  
840  C CG  . GLU A 111 ? 0.553 0.859 0.438 -0.135 -0.114 -0.087 113 GLU AAA CG  
841  C CD  . GLU A 111 ? 0.568 0.854 0.440 -0.120 -0.105 -0.088 113 GLU AAA CD  
842  O OE1 . GLU A 111 ? 0.554 0.834 0.437 -0.111 -0.098 -0.078 113 GLU AAA OE1 
843  O OE2 . GLU A 111 ? 0.606 0.885 0.458 -0.116 -0.105 -0.096 113 GLU AAA OE2 
844  N N   . TYR A 112 ? 0.515 0.876 0.440 -0.135 -0.106 -0.051 114 TYR AAA N   
845  C CA  . TYR A 112 ? 0.520 0.891 0.442 -0.127 -0.101 -0.042 114 TYR AAA CA  
846  C C   . TYR A 112 ? 0.527 0.914 0.463 -0.132 -0.094 -0.033 114 TYR AAA C   
847  O O   . TYR A 112 ? 0.541 0.927 0.492 -0.145 -0.094 -0.031 114 TYR AAA O   
848  C CB  . TYR A 112 ? 0.535 0.886 0.443 -0.120 -0.100 -0.037 114 TYR AAA CB  
849  C CG  . TYR A 112 ? 0.531 0.873 0.434 -0.112 -0.106 -0.042 114 TYR AAA CG  
850  C CD1 . TYR A 112 ? 0.537 0.866 0.445 -0.114 -0.107 -0.046 114 TYR AAA CD1 
851  C CD2 . TYR A 112 ? 0.530 0.876 0.426 -0.104 -0.110 -0.043 114 TYR AAA CD2 
852  C CE1 . TYR A 112 ? 0.532 0.855 0.444 -0.105 -0.110 -0.046 114 TYR AAA CE1 
853  C CE2 . TYR A 112 ? 0.529 0.869 0.430 -0.099 -0.117 -0.046 114 TYR AAA CE2 
854  C CZ  . TYR A 112 ? 0.521 0.852 0.434 -0.099 -0.116 -0.046 114 TYR AAA CZ  
855  O OH  . TYR A 112 ? 0.501 0.829 0.426 -0.092 -0.120 -0.044 114 TYR AAA OH  
856  N N   . ASP A 113 ? 0.534 0.933 0.466 -0.124 -0.087 -0.027 115 ASP AAA N   
857  C CA  . ASP A 113 ? 0.529 0.950 0.481 -0.126 -0.078 -0.015 115 ASP AAA CA  
858  C C   . ASP A 113 ? 0.551 0.961 0.488 -0.117 -0.062 -0.003 115 ASP AAA C   
859  O O   . ASP A 113 ? 0.579 0.998 0.535 -0.121 -0.051 0.010  115 ASP AAA O   
860  C CB  . ASP A 113 ? 0.517 0.960 0.476 -0.119 -0.077 -0.015 115 ASP AAA CB  
861  C CG  . ASP A 113 ? 0.500 0.953 0.465 -0.125 -0.091 -0.025 115 ASP AAA CG  
862  O OD1 . ASP A 113 ? 0.506 0.968 0.488 -0.138 -0.100 -0.026 115 ASP AAA OD1 
863  O OD2 . ASP A 113 ? 0.505 0.954 0.459 -0.115 -0.093 -0.031 115 ASP AAA OD2 
864  N N   . PHE A 114 ? 0.562 0.954 0.466 -0.105 -0.062 -0.007 116 PHE AAA N   
865  C CA  . PHE A 114 ? 0.581 0.958 0.457 -0.093 -0.048 0.002  116 PHE AAA CA  
866  C C   . PHE A 114 ? 0.604 0.958 0.450 -0.089 -0.058 -0.002 116 PHE AAA C   
867  O O   . PHE A 114 ? 0.582 0.932 0.427 -0.091 -0.074 -0.014 116 PHE AAA O   
868  C CB  . PHE A 114 ? 0.585 0.963 0.446 -0.082 -0.039 -0.000 116 PHE AAA CB  
869  C CG  . PHE A 114 ? 0.565 0.971 0.462 -0.084 -0.029 0.008  116 PHE AAA CG  
870  C CD1 . PHE A 114 ? 0.571 0.989 0.487 -0.083 -0.011 0.027  116 PHE AAA CD1 
871  C CD2 . PHE A 114 ? 0.544 0.967 0.459 -0.087 -0.038 0.001  116 PHE AAA CD2 
872  C CE1 . PHE A 114 ? 0.555 1.003 0.511 -0.085 -0.004 0.038  116 PHE AAA CE1 
873  C CE2 . PHE A 114 ? 0.528 0.981 0.477 -0.088 -0.031 0.012  116 PHE AAA CE2 
874  C CZ  . PHE A 114 ? 0.537 1.004 0.508 -0.088 -0.015 0.030  116 PHE AAA CZ  
875  N N   . TRP A 115 ? 0.631 0.972 0.457 -0.083 -0.048 0.010  117 TRP AAA N   
876  C CA  . TRP A 115 ? 0.663 0.985 0.462 -0.078 -0.056 0.012  117 TRP AAA CA  
877  C C   . TRP A 115 ? 0.720 1.026 0.470 -0.062 -0.049 0.018  117 TRP AAA C   
878  O O   . TRP A 115 ? 0.735 1.041 0.479 -0.054 -0.027 0.029  117 TRP AAA O   
879  C CB  . TRP A 115 ? 0.664 0.986 0.487 -0.084 -0.050 0.026  117 TRP AAA CB  
880  C CG  . TRP A 115 ? 0.637 0.967 0.499 -0.099 -0.058 0.017  117 TRP AAA CG  
881  C CD1 . TRP A 115 ? 0.622 0.967 0.516 -0.111 -0.054 0.015  117 TRP AAA CD1 
882  C CD2 . TRP A 115 ? 0.630 0.951 0.497 -0.104 -0.070 0.010  117 TRP AAA CD2 
883  N NE1 . TRP A 115 ? 0.610 0.953 0.523 -0.123 -0.065 0.004  117 TRP AAA NE1 
884  C CE2 . TRP A 115 ? 0.617 0.943 0.514 -0.117 -0.072 0.002  117 TRP AAA CE2 
885  C CE3 . TRP A 115 ? 0.641 0.949 0.492 -0.096 -0.080 0.012  117 TRP AAA CE3 
886  C CZ2 . TRP A 115 ? 0.607 0.922 0.512 -0.122 -0.080 -0.006 117 TRP AAA CZ2 
887  C CZ3 . TRP A 115 ? 0.637 0.939 0.506 -0.101 -0.087 0.007  117 TRP AAA CZ3 
888  C CH2 . TRP A 115 ? 0.619 0.922 0.512 -0.113 -0.085 -0.002 117 TRP AAA CH2 
889  N N   . GLY A 116 ? 0.743 1.035 0.460 -0.056 -0.066 0.011  118 GLY AAA N   
890  C CA  . GLY A 116 ? 0.804 1.076 0.463 -0.041 -0.064 0.016  118 GLY AAA CA  
891  C C   . GLY A 116 ? 0.833 1.101 0.486 -0.034 -0.051 0.039  118 GLY AAA C   
892  O O   . GLY A 116 ? 0.806 1.085 0.503 -0.044 -0.048 0.048  118 GLY AAA O   
893  N N   . GLN A 117 ? 0.894 1.144 0.493 -0.017 -0.043 0.048  119 GLN AAA N   
894  C CA  . GLN A 117 ? 0.946 1.191 0.534 -0.006 -0.027 0.074  119 GLN AAA CA  
895  C C   . GLN A 117 ? 0.934 1.181 0.527 -0.008 -0.049 0.079  119 GLN AAA C   
896  O O   . GLN A 117 ? 0.944 1.191 0.554 -0.005 -0.036 0.101  119 GLN AAA O   
897  C CB  . GLN A 117 ? 1.036 1.258 0.554 0.016  -0.012 0.083  119 GLN AAA CB  
898  C CG  . GLN A 117 ? 1.065 1.284 0.585 0.022  0.020  0.088  119 GLN AAA CG  
899  C CD  . GLN A 117 ? 1.177 1.366 0.616 0.045  0.033  0.089  119 GLN AAA CD  
900  O OE1 . GLN A 117 ? 1.240 1.414 0.632 0.062  0.041  0.106  119 GLN AAA OE1 
901  N NE2 . GLN A 117 ? 1.205 1.384 0.625 0.046  0.036  0.070  119 GLN AAA NE2 
902  N N   . GLY A 118 ? 0.916 1.164 0.499 -0.013 -0.080 0.061  120 GLY AAA N   
903  C CA  . GLY A 118 ? 0.913 1.167 0.507 -0.015 -0.103 0.066  120 GLY AAA CA  
904  C C   . GLY A 118 ? 0.965 1.210 0.499 0.001  -0.120 0.073  120 GLY AAA C   
905  O O   . GLY A 118 ? 1.009 1.239 0.496 0.017  -0.102 0.086  120 GLY AAA O   
906  N N   . ILE A 119 ? 0.968 1.221 0.503 -0.002 -0.153 0.066  121 ILE AAA N   
907  C CA  . ILE A 119 ? 1.039 1.287 0.517 0.010  -0.180 0.071  121 ILE AAA CA  
908  C C   . ILE A 119 ? 1.031 1.295 0.540 0.013  -0.194 0.093  121 ILE AAA C   
909  O O   . ILE A 119 ? 0.983 1.262 0.555 0.001  -0.199 0.091  121 ILE AAA O   
910  C CB  . ILE A 119 ? 1.070 1.312 0.521 0.003  -0.212 0.042  121 ILE AAA CB  
911  C CG1 . ILE A 119 ? 1.019 1.277 0.537 -0.016 -0.224 0.025  121 ILE AAA CG1 
912  C CG2 . ILE A 119 ? 1.112 1.328 0.504 0.010  -0.196 0.026  121 ILE AAA CG2 
913  C CD1 . ILE A 119 ? 1.044 1.299 0.549 -0.025 -0.259 0.001  121 ILE AAA CD1 
914  N N   . GLN A 120 ? 1.085 1.346 0.550 0.031  -0.198 0.115  122 GLN AAA N   
915  C CA  . GLN A 120 ? 1.084 1.361 0.573 0.039  -0.208 0.143  122 GLN AAA CA  
916  C C   . GLN A 120 ? 1.089 1.385 0.586 0.032  -0.254 0.134  122 GLN AAA C   
917  O O   . GLN A 120 ? 1.141 1.430 0.580 0.034  -0.282 0.118  122 GLN AAA O   
918  C CB  . GLN A 120 ? 1.140 1.408 0.575 0.063  -0.194 0.172  122 GLN AAA CB  
919  C CG  . GLN A 120 ? 1.149 1.433 0.611 0.074  -0.198 0.207  122 GLN AAA CG  
920  C CD  . GLN A 120 ? 1.095 1.380 0.633 0.066  -0.167 0.220  122 GLN AAA CD  
921  O OE1 . GLN A 120 ? 1.088 1.359 0.637 0.067  -0.129 0.227  122 GLN AAA OE1 
922  N NE2 . GLN A 120 ? 1.059 1.362 0.653 0.058  -0.183 0.224  122 GLN AAA NE2 
923  N N   . VAL A 121 ? 1.048 1.364 0.615 0.024  -0.261 0.143  123 VAL AAA N   
924  C CA  . VAL A 121 ? 1.066 1.406 0.658 0.021  -0.302 0.146  123 VAL AAA CA  
925  C C   . VAL A 121 ? 1.081 1.436 0.700 0.035  -0.298 0.185  123 VAL AAA C   
926  O O   . VAL A 121 ? 1.046 1.399 0.719 0.034  -0.268 0.198  123 VAL AAA O   
927  C CB  . VAL A 121 ? 1.010 1.360 0.667 0.001  -0.310 0.126  123 VAL AAA CB  
928  C CG1 . VAL A 121 ? 1.014 1.392 0.711 -0.002 -0.349 0.135  123 VAL AAA CG1 
929  C CG2 . VAL A 121 ? 0.998 1.333 0.633 -0.012 -0.311 0.091  123 VAL AAA CG2 
930  N N   . THR A 122 ? 1.144 1.512 0.724 0.049  -0.326 0.203  124 THR AAA N   
931  C CA  . THR A 122 ? 1.168 1.555 0.771 0.066  -0.326 0.245  124 THR AAA CA  
932  C C   . THR A 122 ? 1.187 1.607 0.816 0.063  -0.377 0.251  124 THR AAA C   
933  O O   . THR A 122 ? 1.255 1.680 0.830 0.061  -0.417 0.236  124 THR AAA O   
934  C CB  . THR A 122 ? 1.232 1.606 0.767 0.090  -0.312 0.269  124 THR AAA CB  
935  O OG1 . THR A 122 ? 1.299 1.657 0.749 0.091  -0.329 0.245  124 THR AAA OG1 
936  C CG2 . THR A 122 ? 1.204 1.555 0.752 0.096  -0.256 0.283  124 THR AAA CG2 
937  N N   . VAL A 123 ? 1.144 1.587 0.855 0.061  -0.374 0.272  125 VAL AAA N   
938  C CA  . VAL A 123 ? 1.146 1.625 0.907 0.055  -0.418 0.279  125 VAL AAA CA  
939  C C   . VAL A 123 ? 1.179 1.687 0.948 0.077  -0.432 0.325  125 VAL AAA C   
940  O O   . VAL A 123 ? 1.153 1.662 0.964 0.090  -0.399 0.358  125 VAL AAA O   
941  C CB  . VAL A 123 ? 1.072 1.558 0.922 0.041  -0.405 0.272  125 VAL AAA CB  
942  C CG1 . VAL A 123 ? 1.033 1.493 0.911 0.045  -0.349 0.279  125 VAL AAA CG1 
943  C CG2 . VAL A 123 ? 1.068 1.595 0.991 0.042  -0.435 0.298  125 VAL AAA CG2 
944  N N   . ASN B 2   ? 1.178 1.103 1.272 -0.144 -0.046 0.275  331 ASN BBB N   
945  C CA  . ASN B 2   ? 1.164 1.109 1.167 -0.155 -0.032 0.267  331 ASN BBB CA  
946  C C   . ASN B 2   ? 1.133 1.097 1.074 -0.146 -0.027 0.245  331 ASN BBB C   
947  O O   . ASN B 2   ? 1.148 1.117 1.016 -0.157 -0.033 0.263  331 ASN BBB O   
948  C CB  . ASN B 2   ? 1.209 1.152 1.174 -0.175 -0.047 0.314  331 ASN BBB CB  
949  C CG  . ASN B 2   ? 1.231 1.160 1.246 -0.185 -0.045 0.332  331 ASN BBB CG  
950  O OD1 . ASN B 2   ? 1.246 1.183 1.223 -0.200 -0.036 0.347  331 ASN BBB OD1 
951  N ND2 . ASN B 2   ? 1.231 1.139 1.337 -0.178 -0.050 0.330  331 ASN BBB ND2 
952  N N   . ILE B 3   ? 1.097 1.066 1.062 -0.131 -0.014 0.206  332 ILE BBB N   
953  C CA  . ILE B 3   ? 1.066 1.053 0.983 -0.121 -0.008 0.181  332 ILE BBB CA  
954  C C   . ILE B 3   ? 1.064 1.069 0.906 -0.128 0.009  0.177  332 ILE BBB C   
955  O O   . ILE B 3   ? 1.060 1.070 0.905 -0.137 0.023  0.180  332 ILE BBB O   
956  C CB  . ILE B 3   ? 1.023 1.013 0.978 -0.108 0.009  0.140  332 ILE BBB CB  
957  C CG1 . ILE B 3   ? 1.017 1.010 0.972 -0.115 0.032  0.113  332 ILE BBB CG1 
958  C CG2 . ILE B 3   ? 1.026 0.994 1.062 -0.098 0.001  0.144  332 ILE BBB CG2 
959  C CD1 . ILE B 3   ? 1.010 0.991 1.000 -0.111 0.048  0.075  332 ILE BBB CD1 
960  N N   . THR B 4   ? 1.062 1.075 0.846 -0.125 0.010  0.171  333 THR BBB N   
961  C CA  . THR B 4   ? 1.100 1.118 0.808 -0.134 0.027  0.177  333 THR BBB CA  
962  C C   . THR B 4   ? 1.073 1.115 0.770 -0.122 0.054  0.145  333 THR BBB C   
963  O O   . THR B 4   ? 1.071 1.117 0.754 -0.112 0.051  0.127  333 THR BBB O   
964  C CB  . THR B 4   ? 1.142 1.139 0.785 -0.145 0.007  0.198  333 THR BBB CB  
965  O OG1 . THR B 4   ? 1.174 1.153 0.796 -0.166 -0.005 0.236  333 THR BBB OG1 
966  C CG2 . THR B 4   ? 1.155 1.151 0.719 -0.146 0.031  0.181  333 THR BBB CG2 
967  N N   . ASN B 5   ? 1.071 1.131 0.783 -0.125 0.077  0.144  334 ASN BBB N   
968  C CA  . ASN B 5   ? 1.061 1.147 0.765 -0.119 0.104  0.129  334 ASN BBB CA  
969  C C   . ASN B 5   ? 0.967 1.071 0.710 -0.111 0.098  0.102  334 ASN BBB C   
970  O O   . ASN B 5   ? 0.913 1.005 0.680 -0.108 0.080  0.090  334 ASN BBB O   
971  C CB  . ASN B 5   ? 1.165 1.240 0.803 -0.115 0.118  0.126  334 ASN BBB CB  
972  C CG  . ASN B 5   ? 1.261 1.355 0.893 -0.111 0.157  0.124  334 ASN BBB CG  
973  O OD1 . ASN B 5   ? 1.322 1.438 0.997 -0.114 0.171  0.135  334 ASN BBB OD1 
974  N ND2 . ASN B 5   ? 1.324 1.407 0.908 -0.105 0.175  0.112  334 ASN BBB ND2 
975  N N   . LEU B 6   ? 0.908 1.040 0.662 -0.108 0.116  0.094  335 LEU BBB N   
976  C CA  . LEU B 6   ? 0.852 1.004 0.631 -0.106 0.111  0.072  335 LEU BBB CA  
977  C C   . LEU B 6   ? 0.811 0.957 0.563 -0.092 0.105  0.054  335 LEU BBB C   
978  O O   . LEU B 6   ? 0.808 0.946 0.521 -0.085 0.117  0.059  335 LEU BBB O   
979  C CB  . LEU B 6   ? 0.847 1.034 0.651 -0.110 0.127  0.082  335 LEU BBB CB  
980  C CG  . LEU B 6   ? 0.833 1.042 0.670 -0.122 0.114  0.071  335 LEU BBB CG  
981  C CD1 . LEU B 6   ? 0.850 1.051 0.709 -0.144 0.101  0.075  335 LEU BBB CD1 
982  C CD2 . LEU B 6   ? 0.821 1.068 0.687 -0.122 0.126  0.086  335 LEU BBB CD2 
983  N N   . CYS B 7   ? 0.758 0.903 0.526 -0.091 0.092  0.033  336 CYS BBB N   
984  C CA  . CYS B 7   ? 0.744 0.887 0.497 -0.079 0.085  0.017  336 CYS BBB CA  
985  C C   . CYS B 7   ? 0.728 0.894 0.469 -0.073 0.098  0.014  336 CYS BBB C   
986  O O   . CYS B 7   ? 0.715 0.906 0.481 -0.080 0.106  0.017  336 CYS BBB O   
987  C CB  . CYS B 7   ? 0.718 0.858 0.496 -0.081 0.076  -0.005 336 CYS BBB CB  
988  S SG  . CYS B 7   ? 0.739 0.846 0.548 -0.083 0.067  -0.004 336 CYS BBB SG  
989  N N   . PRO B 8   ? 0.740 0.896 0.446 -0.063 0.100  0.010  337 PRO BBB N   
990  C CA  . PRO B 8   ? 0.735 0.906 0.435 -0.056 0.118  0.008  337 PRO BBB CA  
991  C C   . PRO B 8   ? 0.694 0.888 0.418 -0.052 0.110  -0.007 337 PRO BBB C   
992  O O   . PRO B 8   ? 0.701 0.892 0.407 -0.043 0.112  -0.015 337 PRO BBB O   
993  C CB  . PRO B 8   ? 0.776 0.914 0.417 -0.051 0.121  0.007  337 PRO BBB CB  
994  C CG  . PRO B 8   ? 0.774 0.896 0.411 -0.053 0.091  0.004  337 PRO BBB CG  
995  C CD  . PRO B 8   ? 0.762 0.889 0.438 -0.060 0.084  0.011  337 PRO BBB CD  
996  N N   . PHE B 9   ? 0.675 0.891 0.433 -0.064 0.102  -0.009 338 PHE BBB N   
997  C CA  . PHE B 9   ? 0.648 0.887 0.424 -0.069 0.094  -0.019 338 PHE BBB CA  
998  C C   . PHE B 9   ? 0.622 0.888 0.420 -0.064 0.106  -0.005 338 PHE BBB C   
999  O O   . PHE B 9   ? 0.595 0.873 0.398 -0.060 0.102  -0.011 338 PHE BBB O   
1000 C CB  . PHE B 9   ? 0.662 0.909 0.454 -0.091 0.082  -0.023 338 PHE BBB CB  
1001 C CG  . PHE B 9   ? 0.702 0.921 0.484 -0.094 0.076  -0.043 338 PHE BBB CG  
1002 C CD1 . PHE B 9   ? 0.712 0.919 0.484 -0.082 0.073  -0.059 338 PHE BBB CD1 
1003 C CD2 . PHE B 9   ? 0.744 0.945 0.532 -0.108 0.076  -0.044 338 PHE BBB CD2 
1004 C CE1 . PHE B 9   ? 0.732 0.915 0.512 -0.082 0.073  -0.073 338 PHE BBB CE1 
1005 C CE2 . PHE B 9   ? 0.765 0.935 0.554 -0.108 0.077  -0.062 338 PHE BBB CE2 
1006 C CZ  . PHE B 9   ? 0.760 0.923 0.550 -0.094 0.078  -0.076 338 PHE BBB CZ  
1007 N N   . GLY B 10  ? 0.621 0.895 0.439 -0.063 0.124  0.016  339 GLY BBB N   
1008 C CA  . GLY B 10  ? 0.614 0.910 0.469 -0.055 0.146  0.033  339 GLY BBB CA  
1009 C C   . GLY B 10  ? 0.623 0.899 0.450 -0.036 0.160  0.019  339 GLY BBB C   
1010 O O   . GLY B 10  ? 0.592 0.888 0.453 -0.032 0.163  0.024  339 GLY BBB O   
1011 N N   . GLU B 11  ? 0.672 0.907 0.439 -0.030 0.166  0.005  340 GLU BBB N   
1012 C CA  . GLU B 11  ? 0.707 0.911 0.430 -0.019 0.176  -0.010 340 GLU BBB CA  
1013 C C   . GLU B 11  ? 0.660 0.878 0.393 -0.017 0.152  -0.023 340 GLU BBB C   
1014 O O   . GLU B 11  ? 0.669 0.881 0.400 -0.008 0.163  -0.028 340 GLU BBB O   
1015 C CB  . GLU B 11  ? 0.770 0.930 0.421 -0.023 0.172  -0.018 340 GLU BBB CB  
1016 C CG  . GLU B 11  ? 0.849 0.986 0.473 -0.027 0.201  -0.007 340 GLU BBB CG  
1017 C CD  . GLU B 11  ? 0.923 1.014 0.469 -0.038 0.190  -0.010 340 GLU BBB CD  
1018 O OE1 . GLU B 11  ? 0.937 1.011 0.451 -0.040 0.162  -0.019 340 GLU BBB OE1 
1019 O OE2 . GLU B 11  ? 0.971 1.046 0.493 -0.046 0.207  0.002  340 GLU BBB OE2 
1020 N N   . VAL B 12  ? 0.621 0.853 0.362 -0.026 0.124  -0.028 341 VAL BBB N   
1021 C CA  . VAL B 12  ? 0.596 0.839 0.342 -0.027 0.102  -0.040 341 VAL BBB CA  
1022 C C   . VAL B 12  ? 0.562 0.844 0.356 -0.032 0.101  -0.029 341 VAL BBB C   
1023 O O   . VAL B 12  ? 0.548 0.836 0.351 -0.025 0.102  -0.031 341 VAL BBB O   
1024 C CB  . VAL B 12  ? 0.589 0.827 0.329 -0.035 0.083  -0.050 341 VAL BBB CB  
1025 C CG1 . VAL B 12  ? 0.566 0.815 0.313 -0.038 0.068  -0.063 341 VAL BBB CG1 
1026 C CG2 . VAL B 12  ? 0.619 0.822 0.325 -0.031 0.079  -0.052 341 VAL BBB CG2 
1027 N N   . PHE B 13  ? 0.548 0.855 0.373 -0.048 0.096  -0.016 342 PHE BBB N   
1028 C CA  . PHE B 13  ? 0.539 0.885 0.407 -0.064 0.083  0.001  342 PHE BBB CA  
1029 C C   . PHE B 13  ? 0.544 0.910 0.464 -0.053 0.101  0.025  342 PHE BBB C   
1030 O O   . PHE B 13  ? 0.513 0.906 0.469 -0.059 0.090  0.039  342 PHE BBB O   
1031 C CB  . PHE B 13  ? 0.541 0.899 0.417 -0.091 0.069  0.010  342 PHE BBB CB  
1032 C CG  . PHE B 13  ? 0.553 0.892 0.388 -0.107 0.055  -0.015 342 PHE BBB CG  
1033 C CD1 . PHE B 13  ? 0.556 0.908 0.383 -0.128 0.039  -0.021 342 PHE BBB CD1 
1034 C CD2 . PHE B 13  ? 0.572 0.880 0.382 -0.101 0.062  -0.031 342 PHE BBB CD2 
1035 C CE1 . PHE B 13  ? 0.580 0.907 0.369 -0.142 0.037  -0.048 342 PHE BBB CE1 
1036 C CE2 . PHE B 13  ? 0.592 0.879 0.378 -0.112 0.057  -0.054 342 PHE BBB CE2 
1037 C CZ  . PHE B 13  ? 0.595 0.890 0.369 -0.132 0.049  -0.065 342 PHE BBB CZ  
1038 N N   . ASN B 14  ? 0.588 0.940 0.515 -0.039 0.130  0.032  343 ASN BBB N   
1039 C CA  . ASN B 14  ? 0.611 0.980 0.602 -0.028 0.159  0.058  343 ASN BBB CA  
1040 C C   . ASN B 14  ? 0.630 0.959 0.594 -0.004 0.194  0.041  343 ASN BBB C   
1041 O O   . ASN B 14  ? 0.643 0.973 0.655 0.009  0.231  0.056  343 ASN BBB O   
1042 C CB  . ASN B 14  ? 0.646 1.029 0.674 -0.034 0.173  0.082  343 ASN BBB CB  
1043 C CG  . ASN B 14  ? 0.658 1.086 0.741 -0.061 0.141  0.112  343 ASN BBB CG  
1044 O OD1 . ASN B 14  ? 0.627 1.086 0.750 -0.072 0.119  0.128  343 ASN BBB OD1 
1045 N ND2 . ASN B 14  ? 0.754 1.186 0.837 -0.076 0.135  0.121  343 ASN BBB ND2 
1046 N N   . ALA B 15  ? 0.629 0.923 0.522 0.000  0.184  0.011  344 ALA BBB N   
1047 C CA  . ALA B 15  ? 0.660 0.912 0.515 0.015  0.209  -0.007 344 ALA BBB CA  
1048 C C   . ALA B 15  ? 0.647 0.918 0.572 0.025  0.225  0.007  344 ALA BBB C   
1049 O O   . ALA B 15  ? 0.613 0.927 0.588 0.017  0.196  0.023  344 ALA BBB O   
1050 C CB  . ALA B 15  ? 0.657 0.885 0.448 0.011  0.180  -0.031 344 ALA BBB CB  
1051 N N   . THR B 16  ? 0.687 0.924 0.615 0.040  0.272  0.002  345 THR BBB N   
1052 C CA  . THR B 16  ? 0.688 0.939 0.700 0.053  0.296  0.019  345 THR BBB CA  
1053 C C   . THR B 16  ? 0.674 0.921 0.671 0.054  0.270  0.006  345 THR BBB C   
1054 O O   . THR B 16  ? 0.631 0.917 0.710 0.055  0.258  0.030  345 THR BBB O   
1055 C CB  . THR B 16  ? 0.748 0.955 0.766 0.069  0.364  0.013  345 THR BBB CB  
1056 O OG1 . THR B 16  ? 0.815 0.953 0.734 0.070  0.380  -0.024 345 THR BBB OG1 
1057 C CG2 . THR B 16  ? 0.767 0.972 0.780 0.066  0.391  0.022  345 THR BBB CG2 
1058 N N   . ARG B 17  ? 0.717 0.919 0.618 0.050  0.257  -0.026 346 ARG BBB N   
1059 C CA  . ARG B 17  ? 0.707 0.906 0.587 0.047  0.225  -0.039 346 ARG BBB CA  
1060 C C   . ARG B 17  ? 0.652 0.861 0.479 0.033  0.180  -0.049 346 ARG BBB C   
1061 O O   . ARG B 17  ? 0.678 0.866 0.452 0.028  0.181  -0.057 346 ARG BBB O   
1062 C CB  . ARG B 17  ? 0.806 0.937 0.623 0.053  0.250  -0.066 346 ARG BBB CB  
1063 C CG  . ARG B 17  ? 0.871 0.987 0.749 0.068  0.292  -0.061 346 ARG BBB CG  
1064 C CD  . ARG B 17  ? 0.993 1.031 0.790 0.067  0.315  -0.094 346 ARG BBB CD  
1065 N NE  . ARG B 17  ? 1.094 1.093 0.930 0.081  0.379  -0.098 346 ARG BBB NE  
1066 C CZ  . ARG B 17  ? 1.212 1.130 0.978 0.079  0.414  -0.129 346 ARG BBB CZ  
1067 N NH1 . ARG B 17  ? 1.267 1.138 0.920 0.060  0.385  -0.155 346 ARG BBB NH1 
1068 N NH2 . ARG B 17  ? 1.273 1.156 1.088 0.094  0.480  -0.133 346 ARG BBB NH2 
1069 N N   . PHE B 18  ? 0.590 0.827 0.432 0.027  0.146  -0.047 347 PHE BBB N   
1070 C CA  . PHE B 18  ? 0.555 0.797 0.356 0.016  0.110  -0.058 347 PHE BBB CA  
1071 C C   . PHE B 18  ? 0.563 0.773 0.323 0.018  0.099  -0.075 347 PHE BBB C   
1072 O O   . PHE B 18  ? 0.580 0.770 0.348 0.025  0.114  -0.077 347 PHE BBB O   
1073 C CB  . PHE B 18  ? 0.506 0.801 0.351 0.003  0.085  -0.044 347 PHE BBB CB  
1074 C CG  . PHE B 18  ? 0.491 0.806 0.342 -0.008 0.081  -0.036 347 PHE BBB CG  
1075 C CD1 . PHE B 18  ? 0.501 0.814 0.368 -0.005 0.103  -0.025 347 PHE BBB CD1 
1076 C CD2 . PHE B 18  ? 0.471 0.802 0.309 -0.024 0.058  -0.042 347 PHE BBB CD2 
1077 C CE1 . PHE B 18  ? 0.494 0.823 0.366 -0.018 0.096  -0.017 347 PHE BBB CE1 
1078 C CE2 . PHE B 18  ? 0.469 0.810 0.307 -0.038 0.056  -0.038 347 PHE BBB CE2 
1079 C CZ  . PHE B 18  ? 0.479 0.820 0.334 -0.035 0.072  -0.025 347 PHE BBB CZ  
1080 N N   . ALA B 19  ? 0.550 0.753 0.273 0.011  0.073  -0.084 348 ALA BBB N   
1081 C CA  . ALA B 19  ? 0.558 0.738 0.251 0.008  0.053  -0.094 348 ALA BBB CA  
1082 C C   . ALA B 19  ? 0.508 0.722 0.245 0.008  0.038  -0.088 348 ALA BBB C   
1083 O O   . ALA B 19  ? 0.474 0.731 0.251 0.003  0.033  -0.078 348 ALA BBB O   
1084 C CB  . ALA B 19  ? 0.561 0.734 0.227 0.001  0.030  -0.096 348 ALA BBB CB  
1085 N N   . SER B 20  ? 0.524 0.717 0.249 0.009  0.030  -0.094 349 SER BBB N   
1086 C CA  . SER B 20  ? 0.494 0.715 0.250 0.005  0.008  -0.089 349 SER BBB CA  
1087 C C   . SER B 20  ? 0.467 0.709 0.224 -0.002 -0.012 -0.089 349 SER BBB C   
1088 O O   . SER B 20  ? 0.479 0.699 0.206 -0.003 -0.018 -0.093 349 SER BBB O   
1089 C CB  . SER B 20  ? 0.525 0.711 0.261 0.005  0.002  -0.095 349 SER BBB CB  
1090 O OG  . SER B 20  ? 0.531 0.710 0.294 0.013  0.023  -0.092 349 SER BBB OG  
1091 N N   . VAL B 21  ? 0.440 0.723 0.232 -0.008 -0.020 -0.082 350 VAL BBB N   
1092 C CA  . VAL B 21  ? 0.430 0.732 0.231 -0.015 -0.027 -0.085 350 VAL BBB CA  
1093 C C   . VAL B 21  ? 0.449 0.729 0.242 -0.013 -0.044 -0.087 350 VAL BBB C   
1094 O O   . VAL B 21  ? 0.450 0.728 0.248 -0.013 -0.045 -0.088 350 VAL BBB O   
1095 C CB  . VAL B 21  ? 0.408 0.749 0.235 -0.028 -0.028 -0.080 350 VAL BBB CB  
1096 C CG1 . VAL B 21  ? 0.406 0.755 0.249 -0.029 -0.041 -0.073 350 VAL BBB CG1 
1097 C CG2 . VAL B 21  ? 0.410 0.761 0.239 -0.036 -0.021 -0.088 350 VAL BBB CG2 
1098 N N   . TYR B 22  ? 0.465 0.730 0.252 -0.012 -0.058 -0.084 351 TYR BBB N   
1099 C CA  . TYR B 22  ? 0.492 0.739 0.276 -0.015 -0.081 -0.079 351 TYR BBB CA  
1100 C C   . TYR B 22  ? 0.541 0.751 0.287 -0.017 -0.089 -0.079 351 TYR BBB C   
1101 O O   . TYR B 22  ? 0.564 0.773 0.326 -0.021 -0.107 -0.068 351 TYR BBB O   
1102 C CB  . TYR B 22  ? 0.501 0.733 0.279 -0.018 -0.096 -0.077 351 TYR BBB CB  
1103 C CG  . TYR B 22  ? 0.560 0.737 0.282 -0.021 -0.096 -0.085 351 TYR BBB CG  
1104 C CD1 . TYR B 22  ? 0.568 0.732 0.279 -0.014 -0.070 -0.093 351 TYR BBB CD1 
1105 C CD2 . TYR B 22  ? 0.613 0.749 0.293 -0.033 -0.119 -0.082 351 TYR BBB CD2 
1106 C CE1 . TYR B 22  ? 0.631 0.737 0.288 -0.018 -0.060 -0.105 351 TYR BBB CE1 
1107 C CE2 . TYR B 22  ? 0.677 0.752 0.289 -0.042 -0.115 -0.093 351 TYR BBB CE2 
1108 C CZ  . TYR B 22  ? 0.689 0.747 0.287 -0.033 -0.081 -0.108 351 TYR BBB CZ  
1109 O OH  . TYR B 22  ? 0.764 0.755 0.292 -0.042 -0.066 -0.123 351 TYR BBB OH  
1110 N N   . ALA B 23  ? 0.573 0.755 0.276 -0.016 -0.073 -0.087 352 ALA BBB N   
1111 C CA  . ALA B 23  ? 0.620 0.762 0.273 -0.021 -0.077 -0.086 352 ALA BBB CA  
1112 C C   . ALA B 23  ? 0.602 0.761 0.266 -0.015 -0.055 -0.088 352 ALA BBB C   
1113 O O   . ALA B 23  ? 0.641 0.773 0.264 -0.016 -0.040 -0.092 352 ALA BBB O   
1114 C CB  . ALA B 23  ? 0.682 0.773 0.272 -0.028 -0.069 -0.096 352 ALA BBB CB  
1115 N N   . TRP B 24  ? 0.561 0.760 0.275 -0.011 -0.052 -0.086 353 TRP BBB N   
1116 C CA  . TRP B 24  ? 0.549 0.763 0.274 -0.008 -0.032 -0.089 353 TRP BBB CA  
1117 C C   . TRP B 24  ? 0.587 0.773 0.282 -0.011 -0.035 -0.084 353 TRP BBB C   
1118 O O   . TRP B 24  ? 0.611 0.777 0.298 -0.016 -0.057 -0.074 353 TRP BBB O   
1119 C CB  . TRP B 24  ? 0.514 0.762 0.285 -0.010 -0.028 -0.091 353 TRP BBB CB  
1120 C CG  . TRP B 24  ? 0.505 0.752 0.307 -0.009 -0.041 -0.084 353 TRP BBB CG  
1121 C CD1 . TRP B 24  ? 0.494 0.752 0.324 -0.009 -0.053 -0.079 353 TRP BBB CD1 
1122 C CD2 . TRP B 24  ? 0.508 0.747 0.333 -0.007 -0.041 -0.078 353 TRP BBB CD2 
1123 N NE1 . TRP B 24  ? 0.497 0.755 0.370 -0.007 -0.060 -0.068 353 TRP BBB NE1 
1124 C CE2 . TRP B 24  ? 0.504 0.750 0.378 -0.006 -0.053 -0.067 353 TRP BBB CE2 
1125 C CE3 . TRP B 24  ? 0.517 0.742 0.333 -0.007 -0.032 -0.078 353 TRP BBB CE3 
1126 C CZ2 . TRP B 24  ? 0.508 0.749 0.430 -0.003 -0.055 -0.054 353 TRP BBB CZ2 
1127 C CZ3 . TRP B 24  ? 0.526 0.745 0.382 -0.005 -0.036 -0.067 353 TRP BBB CZ3 
1128 C CH2 . TRP B 24  ? 0.522 0.749 0.434 -0.002 -0.047 -0.054 353 TRP BBB CH2 
1129 N N   . ASN B 25  ? 0.599 0.784 0.282 -0.009 -0.015 -0.087 354 ASN BBB N   
1130 C CA  . ASN B 25  ? 0.633 0.791 0.284 -0.013 -0.013 -0.081 354 ASN BBB CA  
1131 C C   . ASN B 25  ? 0.611 0.785 0.300 -0.013 -0.015 -0.077 354 ASN BBB C   
1132 O O   . ASN B 25  ? 0.570 0.772 0.294 -0.011 -0.003 -0.084 354 ASN BBB O   
1133 C CB  . ASN B 25  ? 0.657 0.804 0.281 -0.011 0.013  -0.085 354 ASN BBB CB  
1134 C CG  . ASN B 25  ? 0.716 0.828 0.293 -0.019 0.016  -0.078 354 ASN BBB CG  
1135 O OD1 . ASN B 25  ? 0.772 0.844 0.293 -0.028 0.008  -0.078 354 ASN BBB OD1 
1136 N ND2 . ASN B 25  ? 0.712 0.837 0.307 -0.018 0.023  -0.073 354 ASN BBB ND2 
1137 N N   . ARG B 26  ? 0.645 0.797 0.325 -0.018 -0.030 -0.063 355 ARG BBB N   
1138 C CA  . ARG B 26  ? 0.639 0.796 0.356 -0.017 -0.028 -0.056 355 ARG BBB CA  
1139 C C   . ARG B 26  ? 0.678 0.810 0.354 -0.024 -0.027 -0.046 355 ARG BBB C   
1140 O O   . ARG B 26  ? 0.716 0.820 0.347 -0.034 -0.045 -0.034 355 ARG BBB O   
1141 C CB  . ARG B 26  ? 0.646 0.803 0.410 -0.017 -0.050 -0.041 355 ARG BBB CB  
1142 C CG  . ARG B 26  ? 0.655 0.813 0.471 -0.014 -0.045 -0.033 355 ARG BBB CG  
1143 C CD  . ARG B 26  ? 0.677 0.836 0.558 -0.012 -0.065 -0.011 355 ARG BBB CD  
1144 N NE  . ARG B 26  ? 0.661 0.841 0.595 -0.004 -0.053 -0.022 355 ARG BBB NE  
1145 C CZ  . ARG B 26  ? 0.657 0.847 0.630 0.002  -0.019 -0.042 355 ARG BBB CZ  
1146 N NH1 . ARG B 26  ? 0.688 0.869 0.654 0.000  0.002  -0.053 355 ARG BBB NH1 
1147 N NH2 . ARG B 26  ? 0.652 0.858 0.665 0.007  -0.005 -0.051 355 ARG BBB NH2 
1148 N N   . LYS B 27  ? 0.669 0.811 0.356 -0.022 -0.007 -0.051 356 LYS BBB N   
1149 C CA  . LYS B 27  ? 0.704 0.827 0.368 -0.029 -0.004 -0.038 356 LYS BBB CA  
1150 C C   . LYS B 27  ? 0.692 0.817 0.408 -0.028 -0.010 -0.030 356 LYS BBB C   
1151 O O   . LYS B 27  ? 0.649 0.792 0.405 -0.024 0.006  -0.044 356 LYS BBB O   
1152 C CB  . LYS B 27  ? 0.710 0.842 0.357 -0.028 0.024  -0.046 356 LYS BBB CB  
1153 C CG  . LYS B 27  ? 0.747 0.866 0.380 -0.034 0.033  -0.034 356 LYS BBB CG  
1154 C CD  . LYS B 27  ? 0.816 0.902 0.383 -0.042 0.038  -0.024 356 LYS BBB CD  
1155 C CE  . LYS B 27  ? 0.846 0.923 0.404 -0.050 0.048  -0.010 356 LYS BBB CE  
1156 N NZ  . LYS B 27  ? 0.925 0.963 0.410 -0.065 0.046  0.002  356 LYS BBB NZ  
1157 N N   . ARG B 28  ? 0.730 0.835 0.448 -0.035 -0.032 -0.006 357 ARG BBB N   
1158 C CA  . ARG B 28  ? 0.746 0.849 0.523 -0.034 -0.036 0.008  357 ARG BBB CA  
1159 C C   . ARG B 28  ? 0.769 0.864 0.523 -0.039 -0.022 0.010  357 ARG BBB C   
1160 O O   . ARG B 28  ? 0.818 0.897 0.513 -0.049 -0.026 0.022  357 ARG BBB O   
1161 C CB  . ARG B 28  ? 0.790 0.879 0.589 -0.041 -0.072 0.041  357 ARG BBB CB  
1162 C CG  . ARG B 28  ? 0.813 0.898 0.687 -0.038 -0.075 0.061  357 ARG BBB CG  
1163 C CD  . ARG B 28  ? 0.849 0.933 0.786 -0.040 -0.108 0.095  357 ARG BBB CD  
1164 N NE  . ARG B 28  ? 0.898 0.967 0.858 -0.052 -0.135 0.135  357 ARG BBB NE  
1165 C CZ  . ARG B 28  ? 0.927 0.998 0.980 -0.051 -0.159 0.172  357 ARG BBB CZ  
1166 N NH1 . ARG B 28  ? 0.902 0.990 1.037 -0.037 -0.155 0.172  357 ARG BBB NH1 
1167 N NH2 . ARG B 28  ? 0.977 1.035 1.049 -0.065 -0.186 0.214  357 ARG BBB NH2 
1168 N N   . ILE B 29  ? 0.445 1.004 0.378 -0.074 -0.011 0.047  358 ILE BBB N   
1169 C CA  . ILE B 29  ? 0.454 1.010 0.377 -0.085 -0.007 0.047  358 ILE BBB CA  
1170 C C   . ILE B 29  ? 0.467 1.003 0.383 -0.088 -0.015 0.057  358 ILE BBB C   
1171 O O   . ILE B 29  ? 0.472 0.996 0.398 -0.079 -0.019 0.059  358 ILE BBB O   
1172 C CB  . ILE B 29  ? 0.444 1.009 0.378 -0.081 -0.001 0.039  358 ILE BBB CB  
1173 C CG1 . ILE B 29  ? 0.432 1.017 0.375 -0.078 0.006  0.030  358 ILE BBB CG1 
1174 C CG2 . ILE B 29  ? 0.462 1.023 0.387 -0.093 0.002  0.039  358 ILE BBB CG2 
1175 C CD1 . ILE B 29  ? 0.433 1.027 0.389 -0.072 0.010  0.023  358 ILE BBB CD1 
1176 N N   . SER B 30  ? 0.479 1.008 0.377 -0.102 -0.017 0.063  359 SER BBB N   
1177 C CA  . SER B 30  ? 0.498 1.006 0.386 -0.107 -0.025 0.074  359 SER BBB CA  
1178 C C   . SER B 30  ? 0.503 1.009 0.372 -0.124 -0.022 0.076  359 SER BBB C   
1179 O O   . SER B 30  ? 0.485 1.007 0.348 -0.131 -0.015 0.069  359 SER BBB O   
1180 C CB  . SER B 30  ? 0.509 1.011 0.394 -0.105 -0.035 0.083  359 SER BBB CB  
1181 O OG  . SER B 30  ? 0.521 1.035 0.394 -0.114 -0.033 0.082  359 SER BBB OG  
1182 N N   . ASN B 31  ? 0.520 1.005 0.380 -0.130 -0.028 0.084  360 ASN BBB N   
1183 C CA  . ASN B 31  ? 0.554 1.032 0.393 -0.147 -0.028 0.089  360 ASN BBB CA  
1184 C C   . ASN B 31  ? 0.540 1.035 0.378 -0.155 -0.016 0.078  360 ASN BBB C   
1185 O O   . ASN B 31  ? 0.532 1.038 0.358 -0.167 -0.011 0.077  360 ASN BBB O   
1186 C CB  . ASN B 31  ? 0.571 1.048 0.392 -0.158 -0.032 0.096  360 ASN BBB CB  
1187 C CG  . ASN B 31  ? 0.584 1.053 0.411 -0.149 -0.044 0.105  360 ASN BBB CG  
1188 O OD1 . ASN B 31  ? 0.565 1.048 0.404 -0.139 -0.043 0.100  360 ASN BBB OD1 
1189 N ND2 . ASN B 31  ? 0.619 1.066 0.438 -0.152 -0.055 0.118  360 ASN BBB ND2 
1190 N N   . CYS B 32  ? 0.521 1.019 0.372 -0.149 -0.011 0.072  361 CYS BBB N   
1191 C CA  . CYS B 32  ? 0.517 1.034 0.372 -0.155 -0.001 0.062  361 CYS BBB CA  
1192 C C   . CYS B 32  ? 0.515 1.025 0.378 -0.151 -0.000 0.059  361 CYS BBB C   
1193 O O   . CYS B 32  ? 0.516 1.012 0.387 -0.140 -0.005 0.061  361 CYS BBB O   
1194 C CB  . CYS B 32  ? 0.490 1.032 0.358 -0.147 0.005  0.053  361 CYS BBB CB  
1195 S SG  . CYS B 32  ? 0.467 1.011 0.356 -0.127 0.003  0.049  361 CYS BBB SG  
1196 N N   . VAL B 33  ? 0.521 1.043 0.383 -0.161 0.006  0.054  362 VAL BBB N   
1197 C CA  . VAL B 33  ? 0.518 1.038 0.386 -0.161 0.008  0.050  362 VAL BBB CA  
1198 C C   . VAL B 33  ? 0.503 1.046 0.391 -0.151 0.013  0.041  362 VAL BBB C   
1199 O O   . VAL B 33  ? 0.497 1.064 0.390 -0.154 0.019  0.036  362 VAL BBB O   
1200 C CB  . VAL B 33  ? 0.536 1.058 0.393 -0.179 0.012  0.050  362 VAL BBB CB  
1201 C CG1 . VAL B 33  ? 0.538 1.055 0.400 -0.180 0.013  0.047  362 VAL BBB CG1 
1202 C CG2 . VAL B 33  ? 0.563 1.063 0.398 -0.191 0.007  0.060  362 VAL BBB CG2 
1203 N N   . ALA B 34  ? 0.503 1.038 0.401 -0.139 0.011  0.038  363 ALA BBB N   
1204 C CA  . ALA B 34  ? 0.502 1.056 0.418 -0.128 0.014  0.031  363 ALA BBB CA  
1205 C C   . ALA B 34  ? 0.525 1.085 0.444 -0.133 0.017  0.026  363 ALA BBB C   
1206 O O   . ALA B 34  ? 0.572 1.112 0.485 -0.134 0.014  0.027  363 ALA BBB O   
1207 C CB  . ALA B 34  ? 0.487 1.029 0.410 -0.113 0.010  0.031  363 ALA BBB CB  
1208 N N   . ASP B 35  ? 0.522 1.108 0.449 -0.137 0.021  0.022  364 ASP BBB N   
1209 C CA  . ASP B 35  ? 0.540 1.136 0.474 -0.142 0.023  0.018  364 ASP BBB CA  
1210 C C   . ASP B 35  ? 0.506 1.112 0.455 -0.128 0.022  0.013  364 ASP BBB C   
1211 O O   . ASP B 35  ? 0.509 1.138 0.472 -0.123 0.025  0.010  364 ASP BBB O   
1212 C CB  . ASP B 35  ? 0.544 1.164 0.481 -0.154 0.028  0.016  364 ASP BBB CB  
1213 C CG  . ASP B 35  ? 0.557 1.183 0.497 -0.162 0.027  0.014  364 ASP BBB CG  
1214 O OD1 . ASP B 35  ? 0.541 1.159 0.483 -0.157 0.024  0.012  364 ASP BBB OD1 
1215 O OD2 . ASP B 35  ? 0.634 1.273 0.572 -0.176 0.030  0.015  364 ASP BBB OD2 
1216 N N   . TYR B 36  ? 0.484 1.072 0.431 -0.123 0.019  0.012  365 TYR BBB N   
1217 C CA  . TYR B 36  ? 0.472 1.066 0.431 -0.112 0.019  0.008  365 TYR BBB CA  
1218 C C   . TYR B 36  ? 0.467 1.077 0.433 -0.117 0.019  0.005  365 TYR BBB C   
1219 O O   . TYR B 36  ? 0.462 1.084 0.439 -0.109 0.018  0.002  365 TYR BBB O   
1220 C CB  . TYR B 36  ? 0.467 1.035 0.420 -0.105 0.016  0.009  365 TYR BBB CB  
1221 C CG  . TYR B 36  ? 0.460 1.012 0.409 -0.099 0.015  0.013  365 TYR BBB CG  
1222 C CD1 . TYR B 36  ? 0.437 0.995 0.395 -0.087 0.014  0.013  365 TYR BBB CD1 
1223 C CD2 . TYR B 36  ? 0.477 1.008 0.414 -0.105 0.013  0.018  365 TYR BBB CD2 
1224 C CE1 . TYR B 36  ? 0.448 0.994 0.403 -0.082 0.011  0.018  365 TYR BBB CE1 
1225 C CE2 . TYR B 36  ? 0.485 1.002 0.419 -0.099 0.010  0.024  365 TYR BBB CE2 
1226 C CZ  . TYR B 36  ? 0.471 0.996 0.414 -0.088 0.009  0.024  365 TYR BBB CZ  
1227 O OH  . TYR B 36  ? 0.475 0.988 0.416 -0.083 0.004  0.030  365 TYR BBB OH  
1228 N N   . SER B 37  ? 0.492 1.103 0.451 -0.131 0.019  0.006  366 SER BBB N   
1229 C CA  . SER B 37  ? 0.502 1.129 0.466 -0.138 0.018  0.004  366 SER BBB CA  
1230 C C   . SER B 37  ? 0.489 1.148 0.473 -0.134 0.020  0.002  366 SER BBB C   
1231 O O   . SER B 37  ? 0.482 1.155 0.476 -0.134 0.017  0.001  366 SER BBB O   
1232 C CB  . SER B 37  ? 0.517 1.139 0.470 -0.155 0.018  0.005  366 SER BBB CB  
1233 O OG  . SER B 37  ? 0.519 1.159 0.476 -0.162 0.021  0.007  366 SER BBB OG  
1234 N N   . VAL B 38  ? 0.494 1.164 0.483 -0.131 0.023  0.003  367 VAL BBB N   
1235 C CA  . VAL B 38  ? 0.493 1.193 0.502 -0.126 0.026  0.001  367 VAL BBB CA  
1236 C C   . VAL B 38  ? 0.486 1.187 0.505 -0.111 0.024  -0.001 367 VAL BBB C   
1237 O O   . VAL B 38  ? 0.458 1.181 0.494 -0.105 0.025  -0.003 367 VAL BBB O   
1238 C CB  . VAL B 38  ? 0.518 1.223 0.526 -0.126 0.032  0.001  367 VAL BBB CB  
1239 C CG1 . VAL B 38  ? 0.522 1.208 0.521 -0.117 0.031  0.002  367 VAL BBB CG1 
1240 C CG2 . VAL B 38  ? 0.516 1.251 0.544 -0.123 0.036  -0.002 367 VAL BBB CG2 
1241 N N   . LEU B 39  ? 0.516 1.194 0.525 -0.104 0.021  -0.001 368 LEU BBB N   
1242 C CA  . LEU B 39  ? 0.507 1.184 0.523 -0.092 0.019  -0.003 368 LEU BBB CA  
1243 C C   . LEU B 39  ? 0.512 1.187 0.528 -0.094 0.015  -0.003 368 LEU BBB C   
1244 O O   . LEU B 39  ? 0.536 1.228 0.565 -0.090 0.013  -0.004 368 LEU BBB O   
1245 C CB  . LEU B 39  ? 0.535 1.190 0.542 -0.084 0.019  -0.002 368 LEU BBB CB  
1246 C CG  . LEU B 39  ? 0.558 1.212 0.562 -0.083 0.022  -0.000 368 LEU BBB CG  
1247 C CD1 . LEU B 39  ? 0.559 1.193 0.556 -0.076 0.020  0.001  368 LEU BBB CD1 
1248 C CD2 . LEU B 39  ? 0.543 1.219 0.560 -0.078 0.025  -0.003 368 LEU BBB CD2 
1249 N N   . TYR B 40  ? 0.508 1.163 0.510 -0.101 0.014  -0.003 369 TYR BBB N   
1250 C CA  . TYR B 40  ? 0.496 1.143 0.493 -0.103 0.011  -0.005 369 TYR BBB CA  
1251 C C   . TYR B 40  ? 0.461 1.124 0.461 -0.115 0.008  -0.004 369 TYR BBB C   
1252 O O   . TYR B 40  ? 0.479 1.142 0.477 -0.117 0.005  -0.005 369 TYR BBB O   
1253 C CB  . TYR B 40  ? 0.532 1.148 0.512 -0.105 0.012  -0.006 369 TYR BBB CB  
1254 C CG  . TYR B 40  ? 0.574 1.177 0.541 -0.116 0.013  -0.005 369 TYR BBB CG  
1255 C CD1 . TYR B 40  ? 0.610 1.215 0.570 -0.130 0.012  -0.005 369 TYR BBB CD1 
1256 C CD2 . TYR B 40  ? 0.588 1.173 0.548 -0.113 0.015  -0.003 369 TYR BBB CD2 
1257 C CE1 . TYR B 40  ? 0.638 1.228 0.585 -0.141 0.013  -0.004 369 TYR BBB CE1 
1258 C CE2 . TYR B 40  ? 0.614 1.184 0.562 -0.123 0.016  -0.001 369 TYR BBB CE2 
1259 C CZ  . TYR B 40  ? 0.636 1.207 0.576 -0.138 0.015  -0.001 369 TYR BBB CZ  
1260 O OH  . TYR B 40  ? 0.649 1.204 0.575 -0.149 0.016  0.001  369 TYR BBB OH  
1261 N N   . ASN B 41  ? 0.431 1.110 0.436 -0.123 0.009  -0.002 370 ASN BBB N   
1262 C CA  . ASN B 41  ? 0.412 1.112 0.424 -0.134 0.006  -0.001 370 ASN BBB CA  
1263 C C   . ASN B 41  ? 0.373 1.102 0.408 -0.126 0.005  0.000  370 ASN BBB C   
1264 O O   . ASN B 41  ? 0.368 1.117 0.413 -0.133 0.001  0.002  370 ASN BBB O   
1265 C CB  . ASN B 41  ? 0.425 1.127 0.431 -0.148 0.008  0.001  370 ASN BBB CB  
1266 C CG  . ASN B 41  ? 0.460 1.132 0.443 -0.157 0.008  0.000  370 ASN BBB CG  
1267 O OD1 . ASN B 41  ? 0.475 1.129 0.447 -0.157 0.006  -0.002 370 ASN BBB OD1 
1268 N ND2 . ASN B 41  ? 0.478 1.144 0.453 -0.166 0.011  0.002  370 ASN BBB ND2 
1269 N N   . SER B 42  ? 0.362 1.094 0.406 -0.112 0.008  -0.001 371 SER BBB N   
1270 C CA  . SER B 42  ? 0.343 1.100 0.410 -0.103 0.007  -0.000 371 SER BBB CA  
1271 C C   . SER B 42  ? 0.339 1.098 0.410 -0.099 0.001  0.001  371 SER BBB C   
1272 O O   . SER B 42  ? 0.364 1.101 0.420 -0.098 -0.001 -0.000 371 SER BBB O   
1273 C CB  . SER B 42  ? 0.326 1.080 0.397 -0.091 0.013  -0.002 371 SER BBB CB  
1274 O OG  . SER B 42  ? 0.307 1.082 0.398 -0.082 0.013  -0.003 371 SER BBB OG  
1275 N N   . ALA B 43  ? 0.332 1.116 0.424 -0.097 -0.003 0.003  372 ALA BBB N   
1276 C CA  . ALA B 43  ? 0.329 1.117 0.428 -0.092 -0.010 0.006  372 ALA BBB CA  
1277 C C   . ALA B 43  ? 0.313 1.105 0.425 -0.076 -0.008 0.005  372 ALA BBB C   
1278 O O   . ALA B 43  ? 0.332 1.127 0.449 -0.070 -0.013 0.007  372 ALA BBB O   
1279 C CB  . ALA B 43  ? 0.330 1.143 0.444 -0.099 -0.017 0.010  372 ALA BBB CB  
1280 N N   . SER B 44  ? 0.306 1.098 0.420 -0.070 -0.000 0.002  373 SER BBB N   
1281 C CA  . SER B 44  ? 0.306 1.101 0.432 -0.056 0.004  -0.000 373 SER BBB CA  
1282 C C   . SER B 44  ? 0.306 1.078 0.418 -0.049 0.004  -0.002 373 SER BBB C   
1283 O O   . SER B 44  ? 0.314 1.088 0.435 -0.038 0.005  -0.003 373 SER BBB O   
1284 C CB  . SER B 44  ? 0.303 1.107 0.435 -0.055 0.012  -0.003 373 SER BBB CB  
1285 O OG  . SER B 44  ? 0.302 1.130 0.450 -0.062 0.013  -0.002 373 SER BBB OG  
1286 N N   . PHE B 45  ? 0.303 1.055 0.395 -0.054 0.003  -0.003 374 PHE BBB N   
1287 C CA  . PHE B 45  ? 0.295 1.026 0.376 -0.048 0.003  -0.005 374 PHE BBB CA  
1288 C C   . PHE B 45  ? 0.304 1.028 0.378 -0.050 -0.002 -0.003 374 PHE BBB C   
1289 O O   . PHE B 45  ? 0.329 1.047 0.393 -0.059 -0.004 -0.003 374 PHE BBB O   
1290 C CB  . PHE B 45  ? 0.298 1.009 0.362 -0.051 0.007  -0.006 374 PHE BBB CB  
1291 C CG  . PHE B 45  ? 0.309 1.025 0.374 -0.052 0.013  -0.007 374 PHE BBB CG  
1292 C CD1 . PHE B 45  ? 0.294 1.018 0.369 -0.044 0.016  -0.008 374 PHE BBB CD1 
1293 C CD2 . PHE B 45  ? 0.321 1.034 0.378 -0.063 0.014  -0.006 374 PHE BBB CD2 
1294 C CE1 . PHE B 45  ? 0.295 1.022 0.368 -0.046 0.021  -0.009 374 PHE BBB CE1 
1295 C CE2 . PHE B 45  ? 0.316 1.033 0.373 -0.065 0.019  -0.007 374 PHE BBB CE2 
1296 C CZ  . PHE B 45  ? 0.304 1.028 0.369 -0.057 0.023  -0.008 374 PHE BBB CZ  
1297 N N   . SER B 46  ? 0.286 1.012 0.367 -0.041 -0.005 -0.003 375 SER BBB N   
1298 C CA  . SER B 46  ? 0.283 1.004 0.359 -0.043 -0.011 -0.001 375 SER BBB CA  
1299 C C   . SER B 46  ? 0.286 0.984 0.345 -0.042 -0.008 -0.005 375 SER BBB C   
1300 O O   . SER B 46  ? 0.292 0.981 0.339 -0.049 -0.010 -0.005 375 SER BBB O   
1301 C CB  . SER B 46  ? 0.273 1.005 0.362 -0.034 -0.014 0.001  375 SER BBB CB  
1302 O OG  . SER B 46  ? 0.261 0.990 0.355 -0.024 -0.010 -0.001 375 SER BBB OG  
1303 N N   . THR B 47  ? 0.294 0.984 0.352 -0.035 -0.003 -0.007 376 THR BBB N   
1304 C CA  . THR B 47  ? 0.298 0.968 0.343 -0.034 0.000  -0.010 376 THR BBB CA  
1305 C C   . THR B 47  ? 0.297 0.959 0.336 -0.037 0.004  -0.011 376 THR BBB C   
1306 O O   . THR B 47  ? 0.312 0.981 0.357 -0.034 0.006  -0.010 376 THR BBB O   
1307 C CB  . THR B 47  ? 0.295 0.961 0.343 -0.024 0.002  -0.011 376 THR BBB CB  
1308 O OG1 . THR B 47  ? 0.309 0.980 0.360 -0.022 -0.002 -0.009 376 THR BBB OG1 
1309 C CG2 . THR B 47  ? 0.296 0.944 0.334 -0.022 0.005  -0.013 376 THR BBB CG2 
1310 N N   . PHE B 48  ? 0.311 0.958 0.338 -0.044 0.006  -0.012 377 PHE BBB N   
1311 C CA  . PHE B 48  ? 0.323 0.957 0.342 -0.046 0.009  -0.012 377 PHE BBB CA  
1312 C C   . PHE B 48  ? 0.346 0.959 0.354 -0.047 0.012  -0.015 377 PHE BBB C   
1313 O O   . PHE B 48  ? 0.356 0.959 0.354 -0.055 0.012  -0.017 377 PHE BBB O   
1314 C CB  . PHE B 48  ? 0.332 0.972 0.349 -0.057 0.008  -0.011 377 PHE BBB CB  
1315 C CG  . PHE B 48  ? 0.346 0.977 0.357 -0.059 0.011  -0.010 377 PHE BBB CG  
1316 C CD1 . PHE B 48  ? 0.359 0.970 0.363 -0.056 0.013  -0.010 377 PHE BBB CD1 
1317 C CD2 . PHE B 48  ? 0.360 1.003 0.374 -0.066 0.011  -0.008 377 PHE BBB CD2 
1318 C CE1 . PHE B 48  ? 0.376 0.979 0.375 -0.059 0.015  -0.008 377 PHE BBB CE1 
1319 C CE2 . PHE B 48  ? 0.373 1.008 0.380 -0.070 0.013  -0.007 377 PHE BBB CE2 
1320 C CZ  . PHE B 48  ? 0.391 1.005 0.390 -0.066 0.015  -0.006 377 PHE BBB CZ  
1321 N N   . LYS B 49  ? 0.347 0.955 0.358 -0.038 0.013  -0.016 378 LYS BBB N   
1322 C CA  . LYS B 49  ? 0.377 0.968 0.381 -0.036 0.016  -0.020 378 LYS BBB CA  
1323 C C   . LYS B 49  ? 0.391 0.967 0.394 -0.033 0.019  -0.019 378 LYS BBB C   
1324 O O   . LYS B 49  ? 0.416 0.996 0.427 -0.025 0.019  -0.017 378 LYS BBB O   
1325 C CB  . LYS B 49  ? 0.393 0.988 0.402 -0.030 0.017  -0.021 378 LYS BBB CB  
1326 C CG  . LYS B 49  ? 0.398 1.002 0.405 -0.035 0.013  -0.021 378 LYS BBB CG  
1327 C CD  . LYS B 49  ? 0.447 1.049 0.453 -0.031 0.014  -0.023 378 LYS BBB CD  
1328 C CE  . LYS B 49  ? 0.482 1.089 0.483 -0.037 0.010  -0.023 378 LYS BBB CE  
1329 N NZ  . LYS B 49  ? 0.518 1.144 0.530 -0.035 0.004  -0.018 378 LYS BBB NZ  
1330 N N   . CYS B 50  ? 0.403 0.962 0.397 -0.038 0.022  -0.021 379 CYS BBB N   
1331 C CA  . CYS B 50  ? 0.412 0.955 0.406 -0.034 0.025  -0.020 379 CYS BBB CA  
1332 C C   . CYS B 50  ? 0.427 0.956 0.421 -0.029 0.030  -0.024 379 CYS BBB C   
1333 O O   . CYS B 50  ? 0.457 0.984 0.445 -0.033 0.032  -0.029 379 CYS BBB O   
1334 C CB  . CYS B 50  ? 0.435 0.968 0.420 -0.043 0.024  -0.018 379 CYS BBB CB  
1335 S SG  . CYS B 50  ? 0.446 0.999 0.433 -0.049 0.020  -0.014 379 CYS BBB SG  
1336 N N   . TYR B 51  ? 0.426 0.946 0.427 -0.021 0.031  -0.022 380 TYR BBB N   
1337 C CA  . TYR B 51  ? 0.423 0.929 0.428 -0.014 0.037  -0.026 380 TYR BBB CA  
1338 C C   . TYR B 51  ? 0.456 0.944 0.462 -0.012 0.038  -0.023 380 TYR BBB C   
1339 O O   . TYR B 51  ? 0.499 0.991 0.512 -0.008 0.033  -0.016 380 TYR BBB O   
1340 C CB  . TYR B 51  ? 0.403 0.922 0.422 -0.005 0.036  -0.025 380 TYR BBB CB  
1341 C CG  . TYR B 51  ? 0.383 0.919 0.401 -0.007 0.033  -0.025 380 TYR BBB CG  
1342 C CD1 . TYR B 51  ? 0.362 0.913 0.381 -0.008 0.028  -0.021 380 TYR BBB CD1 
1343 C CD2 . TYR B 51  ? 0.374 0.912 0.391 -0.006 0.037  -0.030 380 TYR BBB CD2 
1344 C CE1 . TYR B 51  ? 0.340 0.906 0.360 -0.009 0.025  -0.022 380 TYR BBB CE1 
1345 C CE2 . TYR B 51  ? 0.353 0.905 0.369 -0.008 0.034  -0.030 380 TYR BBB CE2 
1346 C CZ  . TYR B 51  ? 0.342 0.908 0.361 -0.009 0.028  -0.026 380 TYR BBB CZ  
1347 O OH  . TYR B 51  ? 0.344 0.923 0.363 -0.010 0.025  -0.025 380 TYR BBB OH  
1348 N N   . GLY B 52  ? 0.459 0.927 0.457 -0.016 0.043  -0.028 381 GLY BBB N   
1349 C CA  . GLY B 52  ? 0.493 0.939 0.492 -0.013 0.045  -0.026 381 GLY BBB CA  
1350 C C   . GLY B 52  ? 0.511 0.951 0.500 -0.022 0.040  -0.021 381 GLY BBB C   
1351 O O   . GLY B 52  ? 0.558 0.977 0.543 -0.023 0.042  -0.020 381 GLY BBB O   
1352 N N   . VAL B 53  ? 0.513 0.971 0.498 -0.028 0.035  -0.018 382 VAL BBB N   
1353 C CA  . VAL B 53  ? 0.537 0.993 0.512 -0.038 0.031  -0.013 382 VAL BBB CA  
1354 C C   . VAL B 53  ? 0.541 1.006 0.506 -0.050 0.031  -0.017 382 VAL BBB C   
1355 O O   . VAL B 53  ? 0.537 1.021 0.505 -0.049 0.030  -0.019 382 VAL BBB O   
1356 C CB  . VAL B 53  ? 0.536 1.007 0.518 -0.034 0.024  -0.005 382 VAL BBB CB  
1357 C CG1 . VAL B 53  ? 0.521 1.017 0.511 -0.031 0.023  -0.006 382 VAL BBB CG1 
1358 C CG2 . VAL B 53  ? 0.561 1.031 0.533 -0.045 0.021  -0.001 382 VAL BBB CG2 
1359 N N   . SER B 54  ? 0.576 1.028 0.528 -0.061 0.031  -0.017 383 SER BBB N   
1360 C CA  . SER B 54  ? 0.587 1.048 0.528 -0.074 0.030  -0.019 383 SER BBB CA  
1361 C C   . SER B 54  ? 0.567 1.042 0.509 -0.080 0.025  -0.013 383 SER BBB C   
1362 O O   . SER B 54  ? 0.561 1.023 0.498 -0.082 0.024  -0.009 383 SER BBB O   
1363 C CB  . SER B 54  ? 0.627 1.065 0.553 -0.084 0.034  -0.024 383 SER BBB CB  
1364 O OG  . SER B 54  ? 0.665 1.080 0.588 -0.083 0.035  -0.021 383 SER BBB OG  
1365 N N   . PRO B 55  ? 0.561 1.062 0.508 -0.082 0.022  -0.012 384 PRO BBB N   
1366 C CA  . PRO B 55  ? 0.574 1.091 0.524 -0.088 0.019  -0.008 384 PRO BBB CA  
1367 C C   . PRO B 55  ? 0.602 1.108 0.538 -0.102 0.019  -0.006 384 PRO BBB C   
1368 O O   . PRO B 55  ? 0.633 1.141 0.568 -0.105 0.018  -0.001 384 PRO BBB O   
1369 C CB  . PRO B 55  ? 0.555 1.100 0.513 -0.090 0.018  -0.009 384 PRO BBB CB  
1370 C CG  . PRO B 55  ? 0.541 1.085 0.504 -0.080 0.019  -0.013 384 PRO BBB CG  
1371 C CD  . PRO B 55  ? 0.556 1.073 0.509 -0.079 0.022  -0.016 384 PRO BBB CD  
1372 N N   . THR B 56  ? 0.620 1.114 0.545 -0.110 0.021  -0.010 385 THR BBB N   
1373 C CA  . THR B 56  ? 0.646 1.129 0.558 -0.126 0.021  -0.009 385 THR BBB CA  
1374 C C   . THR B 56  ? 0.664 1.122 0.568 -0.126 0.022  -0.006 385 THR BBB C   
1375 O O   . THR B 56  ? 0.715 1.169 0.610 -0.138 0.020  -0.003 385 THR BBB O   
1376 C CB  . THR B 56  ? 0.682 1.155 0.583 -0.135 0.023  -0.015 385 THR BBB CB  
1377 O OG1 . THR B 56  ? 0.699 1.200 0.607 -0.139 0.019  -0.016 385 THR BBB OG1 
1378 C CG2 . THR B 56  ? 0.725 1.178 0.609 -0.149 0.023  -0.016 385 THR BBB CG2 
1379 N N   . LYS B 57  ? 0.626 1.066 0.533 -0.113 0.023  -0.006 386 LYS BBB N   
1380 C CA  . LYS B 57  ? 0.615 1.028 0.517 -0.112 0.023  -0.002 386 LYS BBB CA  
1381 C C   . LYS B 57  ? 0.589 1.012 0.497 -0.107 0.019  0.006  386 LYS BBB C   
1382 O O   . LYS B 57  ? 0.588 0.992 0.489 -0.110 0.017  0.012  386 LYS BBB O   
1383 C CB  . LYS B 57  ? 0.620 1.011 0.525 -0.100 0.027  -0.005 386 LYS BBB CB  
1384 C CG  . LYS B 57  ? 0.638 1.014 0.534 -0.105 0.033  -0.014 386 LYS BBB CG  
1385 C CD  . LYS B 57  ? 0.648 1.004 0.549 -0.093 0.038  -0.018 386 LYS BBB CD  
1386 C CE  . LYS B 57  ? 0.676 1.002 0.576 -0.089 0.039  -0.015 386 LYS BBB CE  
1387 N NZ  . LYS B 57  ? 0.695 0.998 0.597 -0.080 0.047  -0.022 386 LYS BBB NZ  
1388 N N   . LEU B 58  ? 0.556 1.006 0.476 -0.101 0.017  0.007  387 LEU BBB N   
1389 C CA  . LEU B 58  ? 0.557 1.017 0.483 -0.097 0.014  0.014  387 LEU BBB CA  
1390 C C   . LEU B 58  ? 0.566 1.026 0.480 -0.110 0.012  0.019  387 LEU BBB C   
1391 O O   . LEU B 58  ? 0.567 1.021 0.479 -0.109 0.009  0.025  387 LEU BBB O   
1392 C CB  . LEU B 58  ? 0.529 1.018 0.467 -0.090 0.014  0.011  387 LEU BBB CB  
1393 C CG  . LEU B 58  ? 0.516 1.006 0.465 -0.077 0.015  0.008  387 LEU BBB CG  
1394 C CD1 . LEU B 58  ? 0.493 1.010 0.453 -0.072 0.015  0.006  387 LEU BBB CD1 
1395 C CD2 . LEU B 58  ? 0.513 0.988 0.467 -0.067 0.013  0.012  387 LEU BBB CD2 
1396 N N   . ASN B 59  ? 0.586 1.054 0.494 -0.123 0.014  0.016  388 ASN BBB N   
1397 C CA  . ASN B 59  ? 0.610 1.081 0.507 -0.138 0.013  0.020  388 ASN BBB CA  
1398 C C   . ASN B 59  ? 0.645 1.084 0.527 -0.144 0.012  0.025  388 ASN BBB C   
1399 O O   . ASN B 59  ? 0.657 1.095 0.530 -0.156 0.010  0.030  388 ASN BBB O   
1400 C CB  . ASN B 59  ? 0.619 1.109 0.516 -0.150 0.015  0.016  388 ASN BBB CB  
1401 C CG  . ASN B 59  ? 0.615 1.140 0.524 -0.150 0.016  0.015  388 ASN BBB CG  
1402 O OD1 . ASN B 59  ? 0.600 1.134 0.516 -0.141 0.016  0.017  388 ASN BBB OD1 
1403 N ND2 . ASN B 59  ? 0.639 1.182 0.551 -0.160 0.017  0.013  388 ASN BBB ND2 
1404 N N   . ASP B 60  ? 0.657 1.070 0.538 -0.137 0.012  0.024  389 ASP BBB N   
1405 C CA  . ASP B 60  ? 0.691 1.070 0.560 -0.140 0.010  0.028  389 ASP BBB CA  
1406 C C   . ASP B 60  ? 0.670 1.034 0.548 -0.125 0.007  0.033  389 ASP BBB C   
1407 O O   . ASP B 60  ? 0.695 1.029 0.566 -0.124 0.006  0.037  389 ASP BBB O   
1408 C CB  . ASP B 60  ? 0.728 1.086 0.587 -0.146 0.014  0.022  389 ASP BBB CB  
1409 C CG  . ASP B 60  ? 0.793 1.119 0.635 -0.157 0.013  0.027  389 ASP BBB CG  
1410 O OD1 . ASP B 60  ? 0.827 1.155 0.660 -0.167 0.010  0.034  389 ASP BBB OD1 
1411 O OD2 . ASP B 60  ? 0.824 1.122 0.661 -0.155 0.016  0.023  389 ASP BBB OD2 
1412 N N   . LEU B 61  ? 0.626 1.010 0.517 -0.113 0.006  0.034  390 LEU BBB N   
1413 C CA  . LEU B 61  ? 0.617 0.992 0.519 -0.098 0.003  0.038  390 LEU BBB CA  
1414 C C   . LEU B 61  ? 0.612 1.000 0.516 -0.098 -0.003 0.046  390 LEU BBB C   
1415 O O   . LEU B 61  ? 0.583 0.994 0.484 -0.105 -0.002 0.045  390 LEU BBB O   
1416 C CB  . LEU B 61  ? 0.597 0.985 0.515 -0.086 0.007  0.030  390 LEU BBB CB  
1417 C CG  . LEU B 61  ? 0.608 0.978 0.524 -0.084 0.013  0.022  390 LEU BBB CG  
1418 C CD1 . LEU B 61  ? 0.577 0.963 0.506 -0.074 0.017  0.015  390 LEU BBB CD1 
1419 C CD2 . LEU B 61  ? 0.637 0.975 0.554 -0.077 0.013  0.026  390 LEU BBB CD2 
1420 N N   . CYS B 62  ? 0.621 0.994 0.530 -0.089 -0.008 0.054  391 CYS BBB N   
1421 C CA  . CYS B 62  ? 0.629 1.009 0.537 -0.089 -0.015 0.063  391 CYS BBB CA  
1422 C C   . CYS B 62  ? 0.606 0.993 0.532 -0.073 -0.017 0.064  391 CYS BBB C   
1423 O O   . CYS B 62  ? 0.618 0.990 0.555 -0.062 -0.016 0.063  391 CYS BBB O   
1424 C CB  . CYS B 62  ? 0.667 1.022 0.563 -0.096 -0.021 0.074  391 CYS BBB CB  
1425 S SG  . CYS B 62  ? 0.694 1.045 0.567 -0.117 -0.019 0.075  391 CYS BBB SG  
1426 N N   . PHE B 63  ? 0.582 0.989 0.511 -0.072 -0.020 0.066  392 PHE BBB N   
1427 C CA  . PHE B 63  ? 0.563 0.979 0.508 -0.058 -0.023 0.068  392 PHE BBB CA  
1428 C C   . PHE B 63  ? 0.566 0.986 0.506 -0.062 -0.032 0.079  392 PHE BBB C   
1429 O O   . PHE B 63  ? 0.576 1.000 0.500 -0.075 -0.032 0.081  392 PHE BBB O   
1430 C CB  . PHE B 63  ? 0.538 0.979 0.492 -0.054 -0.017 0.058  392 PHE BBB CB  
1431 C CG  . PHE B 63  ? 0.527 0.965 0.485 -0.051 -0.010 0.049  392 PHE BBB CG  
1432 C CD1 . PHE B 63  ? 0.529 0.958 0.500 -0.039 -0.008 0.046  392 PHE BBB CD1 
1433 C CD2 . PHE B 63  ? 0.519 0.964 0.468 -0.060 -0.005 0.042  392 PHE BBB CD2 
1434 C CE1 . PHE B 63  ? 0.523 0.948 0.496 -0.038 -0.001 0.037  392 PHE BBB CE1 
1435 C CE2 . PHE B 63  ? 0.526 0.969 0.478 -0.059 0.001  0.034  392 PHE BBB CE2 
1436 C CZ  . PHE B 63  ? 0.515 0.946 0.477 -0.048 0.003  0.031  392 PHE BBB CZ  
1437 N N   . THR B 64  ? 0.556 0.974 0.508 -0.052 -0.038 0.085  393 THR BBB N   
1438 C CA  . THR B 64  ? 0.568 0.991 0.517 -0.054 -0.047 0.095  393 THR BBB CA  
1439 C C   . THR B 64  ? 0.543 0.991 0.486 -0.060 -0.043 0.089  393 THR BBB C   
1440 O O   . THR B 64  ? 0.572 1.024 0.499 -0.072 -0.046 0.094  393 THR BBB O   
1441 C CB  . THR B 64  ? 0.570 0.989 0.537 -0.041 -0.053 0.101  393 THR BBB CB  
1442 O OG1 . THR B 64  ? 0.583 0.982 0.560 -0.033 -0.052 0.102  393 THR BBB OG1 
1443 C CG2 . THR B 64  ? 0.579 0.997 0.542 -0.045 -0.065 0.115  393 THR BBB CG2 
1444 N N   . ASN B 65  ? 0.518 0.981 0.473 -0.052 -0.037 0.079  394 ASN BBB N   
1445 C CA  . ASN B 65  ? 0.488 0.975 0.442 -0.054 -0.032 0.072  394 ASN BBB CA  
1446 C C   . ASN B 65  ? 0.453 0.950 0.416 -0.049 -0.024 0.060  394 ASN BBB C   
1447 O O   . ASN B 65  ? 0.435 0.924 0.409 -0.039 -0.022 0.058  394 ASN BBB O   
1448 C CB  . ASN B 65  ? 0.488 0.984 0.449 -0.048 -0.038 0.076  394 ASN BBB CB  
1449 C CG  . ASN B 65  ? 0.504 0.994 0.453 -0.056 -0.047 0.087  394 ASN BBB CG  
1450 O OD1 . ASN B 65  ? 0.495 0.989 0.427 -0.068 -0.046 0.088  394 ASN BBB OD1 
1451 N ND2 . ASN B 65  ? 0.517 0.998 0.475 -0.049 -0.056 0.097  394 ASN BBB ND2 
1452 N N   . VAL B 66  ? 0.435 0.948 0.392 -0.054 -0.018 0.054  395 VAL BBB N   
1453 C CA  . VAL B 66  ? 0.416 0.944 0.383 -0.049 -0.011 0.043  395 VAL BBB CA  
1454 C C   . VAL B 66  ? 0.404 0.949 0.374 -0.047 -0.011 0.041  395 VAL BBB C   
1455 O O   . VAL B 66  ? 0.416 0.965 0.375 -0.055 -0.012 0.044  395 VAL BBB O   
1456 C CB  . VAL B 66  ? 0.408 0.941 0.368 -0.058 -0.005 0.038  395 VAL BBB CB  
1457 C CG1 . VAL B 66  ? 0.391 0.940 0.362 -0.053 0.000  0.029  395 VAL BBB CG1 
1458 C CG2 . VAL B 66  ? 0.423 0.937 0.379 -0.061 -0.006 0.040  395 VAL BBB CG2 
1459 N N   . TYR B 67  ? 0.400 0.953 0.382 -0.037 -0.009 0.036  396 TYR BBB N   
1460 C CA  . TYR B 67  ? 0.391 0.959 0.376 -0.034 -0.008 0.033  396 TYR BBB CA  
1461 C C   . TYR B 67  ? 0.362 0.943 0.353 -0.032 -0.001 0.024  396 TYR BBB C   
1462 O O   . TYR B 67  ? 0.361 0.940 0.360 -0.027 0.001  0.020  396 TYR BBB O   
1463 C CB  . TYR B 67  ? 0.388 0.955 0.384 -0.025 -0.012 0.036  396 TYR BBB CB  
1464 C CG  . TYR B 67  ? 0.412 0.967 0.405 -0.026 -0.020 0.046  396 TYR BBB CG  
1465 C CD1 . TYR B 67  ? 0.426 0.985 0.411 -0.032 -0.025 0.050  396 TYR BBB CD1 
1466 C CD2 . TYR B 67  ? 0.425 0.966 0.424 -0.022 -0.023 0.050  396 TYR BBB CD2 
1467 C CE1 . TYR B 67  ? 0.443 0.992 0.424 -0.034 -0.034 0.061  396 TYR BBB CE1 
1468 C CE2 . TYR B 67  ? 0.442 0.973 0.440 -0.022 -0.032 0.061  396 TYR BBB CE2 
1469 C CZ  . TYR B 67  ? 0.456 0.991 0.445 -0.028 -0.038 0.067  396 TYR BBB CZ  
1470 O OH  . TYR B 67  ? 0.482 1.008 0.471 -0.029 -0.047 0.078  396 TYR BBB OH  
1471 N N   . ALA B 68  ? 0.351 0.945 0.338 -0.037 0.002  0.020  397 ALA BBB N   
1472 C CA  . ALA B 68  ? 0.353 0.961 0.347 -0.034 0.008  0.013  397 ALA BBB CA  
1473 C C   . ALA B 68  ? 0.345 0.961 0.344 -0.029 0.008  0.010  397 ALA BBB C   
1474 O O   . ALA B 68  ? 0.369 0.988 0.361 -0.033 0.009  0.011  397 ALA BBB O   
1475 C CB  . ALA B 68  ? 0.354 0.971 0.344 -0.043 0.013  0.010  397 ALA BBB CB  
1476 N N   . ASP B 69  ? 0.323 0.940 0.332 -0.020 0.008  0.008  398 ASP BBB N   
1477 C CA  . ASP B 69  ? 0.312 0.936 0.326 -0.015 0.008  0.005  398 ASP BBB CA  
1478 C C   . ASP B 69  ? 0.308 0.944 0.328 -0.013 0.013  -0.001 398 ASP BBB C   
1479 O O   . ASP B 69  ? 0.310 0.947 0.336 -0.012 0.014  -0.003 398 ASP BBB O   
1480 C CB  . ASP B 69  ? 0.307 0.927 0.328 -0.007 0.005  0.006  398 ASP BBB CB  
1481 C CG  . ASP B 69  ? 0.322 0.931 0.341 -0.007 -0.001 0.013  398 ASP BBB CG  
1482 O OD1 . ASP B 69  ? 0.344 0.950 0.354 -0.014 -0.003 0.017  398 ASP BBB OD1 
1483 O OD2 . ASP B 69  ? 0.304 0.908 0.331 -0.002 -0.002 0.014  398 ASP BBB OD2 
1484 N N   . SER B 70  ? 0.299 0.943 0.319 -0.014 0.017  -0.005 399 SER BBB N   
1485 C CA  . SER B 70  ? 0.284 0.939 0.312 -0.012 0.022  -0.010 399 SER BBB CA  
1486 C C   . SER B 70  ? 0.275 0.932 0.306 -0.006 0.023  -0.013 399 SER BBB C   
1487 O O   . SER B 70  ? 0.290 0.942 0.313 -0.007 0.021  -0.013 399 SER BBB O   
1488 C CB  . SER B 70  ? 0.286 0.949 0.310 -0.019 0.027  -0.012 399 SER BBB CB  
1489 O OG  . SER B 70  ? 0.294 0.953 0.307 -0.024 0.028  -0.012 399 SER BBB OG  
1490 N N   . PHE B 71  ? 0.268 0.931 0.309 -0.000 0.024  -0.017 400 PHE BBB N   
1491 C CA  . PHE B 71  ? 0.259 0.924 0.305 0.006  0.025  -0.020 400 PHE BBB CA  
1492 C C   . PHE B 71  ? 0.243 0.916 0.302 0.010  0.026  -0.021 400 PHE BBB C   
1493 O O   . PHE B 71  ? 0.213 0.891 0.276 0.009  0.024  -0.020 400 PHE BBB O   
1494 C CB  . PHE B 71  ? 0.267 0.923 0.310 0.008  0.020  -0.017 400 PHE BBB CB  
1495 C CG  . PHE B 71  ? 0.269 0.922 0.315 0.010  0.016  -0.014 400 PHE BBB CG  
1496 C CD1 . PHE B 71  ? 0.269 0.924 0.322 0.014  0.015  -0.015 400 PHE BBB CD1 
1497 C CD2 . PHE B 71  ? 0.281 0.927 0.322 0.007  0.013  -0.010 400 PHE BBB CD2 
1498 C CE1 . PHE B 71  ? 0.281 0.932 0.335 0.014  0.013  -0.013 400 PHE BBB CE1 
1499 C CE2 . PHE B 71  ? 0.281 0.922 0.325 0.009  0.011  -0.008 400 PHE BBB CE2 
1500 C CZ  . PHE B 71  ? 0.298 0.942 0.347 0.012  0.011  -0.010 400 PHE BBB CZ  
1501 N N   . VAL B 72  ? 0.243 0.917 0.307 0.016  0.027  -0.024 401 VAL BBB N   
1502 C CA  . VAL B 72  ? 0.239 0.920 0.316 0.021  0.026  -0.025 401 VAL BBB CA  
1503 C C   . VAL B 72  ? 0.234 0.907 0.310 0.026  0.021  -0.023 401 VAL BBB C   
1504 O O   . VAL B 72  ? 0.229 0.894 0.299 0.026  0.022  -0.024 401 VAL BBB O   
1505 C CB  . VAL B 72  ? 0.241 0.929 0.327 0.025  0.032  -0.029 401 VAL BBB CB  
1506 C CG1 . VAL B 72  ? 0.244 0.934 0.342 0.032  0.030  -0.029 401 VAL BBB CG1 
1507 C CG2 . VAL B 72  ? 0.255 0.955 0.347 0.021  0.036  -0.030 401 VAL BBB CG2 
1508 N N   . ILE B 73  ? 0.238 0.913 0.320 0.027  0.017  -0.021 402 ILE BBB N   
1509 C CA  . ILE B 73  ? 0.250 0.919 0.331 0.030  0.013  -0.019 402 ILE BBB CA  
1510 C C   . ILE B 73  ? 0.246 0.923 0.338 0.033  0.010  -0.017 402 ILE BBB C   
1511 O O   . ILE B 73  ? 0.276 0.963 0.376 0.032  0.012  -0.018 402 ILE BBB O   
1512 C CB  . ILE B 73  ? 0.257 0.920 0.331 0.027  0.010  -0.017 402 ILE BBB CB  
1513 C CG1 . ILE B 73  ? 0.257 0.923 0.331 0.023  0.009  -0.015 402 ILE BBB CG1 
1514 C CG2 . ILE B 73  ? 0.268 0.924 0.334 0.026  0.011  -0.017 402 ILE BBB CG2 
1515 C CD1 . ILE B 73  ? 0.257 0.915 0.324 0.021  0.008  -0.014 402 ILE BBB CD1 
1516 N N   . ARG B 74  ? 0.426 0.700 0.433 0.057  0.025  -0.039 403 ARG BBB N   
1517 C CA  A ARG B 74  ? 0.456 0.719 0.446 0.072  0.016  -0.034 403 ARG BBB CA  
1518 C CA  B ARG B 74  ? 0.454 0.717 0.444 0.072  0.016  -0.034 403 ARG BBB CA  
1519 C C   . ARG B 74  ? 0.438 0.715 0.423 0.060  0.024  -0.024 403 ARG BBB C   
1520 O O   . ARG B 74  ? 0.418 0.695 0.408 0.040  0.035  -0.018 403 ARG BBB O   
1521 C CB  A ARG B 74  ? 0.513 0.717 0.484 0.082  0.004  -0.027 403 ARG BBB CB  
1522 C CB  B ARG B 74  ? 0.508 0.712 0.479 0.082  0.004  -0.027 403 ARG BBB CB  
1523 C CG  A ARG B 74  ? 0.532 0.695 0.494 0.058  0.013  -0.008 403 ARG BBB CG  
1524 C CG  B ARG B 74  ? 0.523 0.687 0.486 0.058  0.013  -0.008 403 ARG BBB CG  
1525 C CD  A ARG B 74  ? 0.596 0.696 0.543 0.064  0.001  0.001  403 ARG BBB CD  
1526 C CD  B ARG B 74  ? 0.586 0.690 0.526 0.065  0.003  0.007  403 ARG BBB CD  
1527 N NE  A ARG B 74  ? 0.628 0.693 0.564 0.040  0.011  0.025  403 ARG BBB NE  
1528 N NE  B ARG B 74  ? 0.617 0.676 0.561 0.044  0.006  0.015  403 ARG BBB NE  
1529 C CZ  A ARG B 74  ? 0.655 0.712 0.566 0.039  0.015  0.049  403 ARG BBB CZ  
1530 C CZ  B ARG B 74  ? 0.653 0.670 0.604 0.050  -0.008 0.005  403 ARG BBB CZ  
1531 N NH1 A ARG B 74  ? 0.655 0.733 0.551 0.062  0.008  0.048  403 ARG BBB NH1 
1532 N NH1 B ARG B 74  ? 0.670 0.685 0.621 0.081  -0.025 -0.015 403 ARG BBB NH1 
1533 N NH2 A ARG B 74  ? 0.681 0.715 0.584 0.015  0.025  0.072  403 ARG BBB NH2 
1534 N NH2 B ARG B 74  ? 0.671 0.652 0.631 0.024  -0.004 0.011  403 ARG BBB NH2 
1535 N N   . GLY B 75  ? 0.445 0.737 0.421 0.074  0.016  -0.025 404 GLY BBB N   
1536 C CA  . GLY B 75  ? 0.434 0.750 0.408 0.067  0.019  -0.023 404 GLY BBB CA  
1537 C C   . GLY B 75  ? 0.430 0.723 0.390 0.053  0.028  -0.008 404 GLY BBB C   
1538 O O   . GLY B 75  ? 0.401 0.714 0.370 0.039  0.035  -0.012 404 GLY BBB O   
1539 N N   . ASP B 76  ? 0.473 0.724 0.410 0.055  0.027  0.008  405 ASP BBB N   
1540 C CA  . ASP B 76  ? 0.509 0.746 0.430 0.041  0.036  0.025  405 ASP BBB CA  
1541 C C   . ASP B 76  ? 0.477 0.724 0.417 0.019  0.050  0.022  405 ASP BBB C   
1542 O O   . ASP B 76  ? 0.482 0.738 0.413 0.010  0.058  0.029  405 ASP BBB O   
1543 C CB  . ASP B 76  ? 0.567 0.754 0.465 0.042  0.034  0.047  405 ASP BBB CB  
1544 C CG  . ASP B 76  ? 0.626 0.799 0.493 0.066  0.022  0.059  405 ASP BBB CG  
1545 O OD1 . ASP B 76  ? 0.631 0.842 0.493 0.080  0.018  0.050  405 ASP BBB OD1 
1546 O OD2 . ASP B 76  ? 0.693 0.815 0.541 0.071  0.016  0.077  405 ASP BBB OD2 
1547 N N   . GLU B 77  ? 0.454 0.703 0.415 0.015  0.050  0.010  406 GLU BBB N   
1548 C CA  . GLU B 77  ? 0.432 0.690 0.410 -0.002 0.061  0.006  406 GLU BBB CA  
1549 C C   . GLU B 77  ? 0.409 0.697 0.401 -0.004 0.064  -0.004 406 GLU BBB C   
1550 O O   . GLU B 77  ? 0.407 0.701 0.408 -0.013 0.071  -0.007 406 GLU BBB O   
1551 C CB  . GLU B 77  ? 0.427 0.670 0.417 -0.002 0.058  0.001  406 GLU BBB CB  
1552 C CG  . GLU B 77  ? 0.457 0.659 0.437 -0.007 0.055  0.010  406 GLU BBB CG  
1553 C CD  . GLU B 77  ? 0.458 0.642 0.451 -0.002 0.046  -0.002 406 GLU BBB CD  
1554 O OE1 . GLU B 77  ? 0.433 0.641 0.437 0.011  0.042  -0.018 406 GLU BBB OE1 
1555 O OE2 . GLU B 77  ? 0.476 0.625 0.469 -0.012 0.044  0.003  406 GLU BBB OE2 
1556 N N   . VAL B 78  ? 0.403 0.709 0.398 0.004  0.058  -0.011 407 VAL BBB N   
1557 C CA  . VAL B 78  ? 0.390 0.718 0.402 -0.002 0.059  -0.020 407 VAL BBB CA  
1558 C C   . VAL B 78  ? 0.389 0.716 0.397 -0.008 0.063  -0.021 407 VAL BBB C   
1559 O O   . VAL B 78  ? 0.379 0.709 0.400 -0.015 0.065  -0.026 407 VAL BBB O   
1560 C CB  . VAL B 78  ? 0.389 0.740 0.410 0.003  0.051  -0.028 407 VAL BBB CB  
1561 C CG1 . VAL B 78  ? 0.368 0.734 0.408 -0.009 0.052  -0.035 407 VAL BBB CG1 
1562 C CG2 . VAL B 78  ? 0.388 0.751 0.416 0.012  0.048  -0.030 407 VAL BBB CG2 
1563 N N   . ARG B 79  ? 0.439 0.764 0.428 -0.005 0.063  -0.017 408 ARG BBB N   
1564 C CA  . ARG B 79  ? 0.467 0.802 0.451 -0.006 0.066  -0.022 408 ARG BBB CA  
1565 C C   . ARG B 79  ? 0.441 0.772 0.429 -0.014 0.075  -0.020 408 ARG BBB C   
1566 O O   . ARG B 79  ? 0.452 0.794 0.441 -0.012 0.077  -0.029 408 ARG BBB O   
1567 C CB  . ARG B 79  ? 0.532 0.877 0.492 0.002  0.065  -0.017 408 ARG BBB CB  
1568 C CG  . ARG B 79  ? 0.614 0.943 0.556 -0.002 0.072  0.004  408 ARG BBB CG  
1569 C CD  . ARG B 79  ? 0.684 1.027 0.620 -0.010 0.084  0.010  408 ARG BBB CD  
1570 N NE  . ARG B 79  ? 0.749 1.073 0.678 -0.023 0.092  0.030  408 ARG BBB NE  
1571 C CZ  . ARG B 79  ? 0.775 1.111 0.710 -0.038 0.103  0.035  408 ARG BBB CZ  
1572 N NH1 . ARG B 79  ? 0.769 1.137 0.714 -0.037 0.107  0.020  408 ARG BBB NH1 
1573 N NH2 . ARG B 79  ? 0.811 1.126 0.745 -0.053 0.108  0.053  408 ARG BBB NH2 
1574 N N   . GLN B 80  ? 0.417 0.736 0.409 -0.019 0.079  -0.011 409 GLN BBB N   
1575 C CA  . GLN B 80  ? 0.395 0.718 0.395 -0.026 0.087  -0.012 409 GLN BBB CA  
1576 C C   . GLN B 80  ? 0.374 0.700 0.389 -0.023 0.085  -0.021 409 GLN BBB C   
1577 O O   . GLN B 80  ? 0.370 0.705 0.389 -0.023 0.089  -0.025 409 GLN BBB O   
1578 C CB  . GLN B 80  ? 0.398 0.705 0.400 -0.033 0.088  -0.005 409 GLN BBB CB  
1579 C CG  . GLN B 80  ? 0.428 0.727 0.417 -0.041 0.092  0.009  409 GLN BBB CG  
1580 C CD  . GLN B 80  ? 0.450 0.726 0.447 -0.052 0.092  0.014  409 GLN BBB CD  
1581 O OE1 . GLN B 80  ? 0.463 0.748 0.476 -0.058 0.094  0.004  409 GLN BBB OE1 
1582 N NE2 . GLN B 80  ? 0.480 0.726 0.464 -0.052 0.088  0.027  409 GLN BBB NE2 
1583 N N   . ILE B 81  ? 0.377 0.698 0.398 -0.021 0.080  -0.022 410 ILE BBB N   
1584 C CA  . ILE B 81  ? 0.364 0.684 0.396 -0.020 0.079  -0.023 410 ILE BBB CA  
1585 C C   . ILE B 81  ? 0.372 0.686 0.405 -0.018 0.075  -0.031 410 ILE BBB C   
1586 O O   . ILE B 81  ? 0.372 0.681 0.414 -0.022 0.070  -0.032 410 ILE BBB O   
1587 C CB  . ILE B 81  ? 0.355 0.679 0.396 -0.021 0.078  -0.018 410 ILE BBB CB  
1588 C CG1 . ILE B 81  ? 0.356 0.684 0.395 -0.018 0.078  -0.017 410 ILE BBB CG1 
1589 C CG2 . ILE B 81  ? 0.359 0.683 0.407 -0.022 0.080  -0.013 410 ILE BBB CG2 
1590 C CD1 . ILE B 81  ? 0.353 0.681 0.391 -0.017 0.081  -0.019 410 ILE BBB CD1 
1591 N N   . ALA B 82  ? 0.382 0.702 0.409 -0.013 0.076  -0.038 411 ALA BBB N   
1592 C CA  . ALA B 82  ? 0.408 0.723 0.433 -0.006 0.069  -0.051 411 ALA BBB CA  
1593 C C   . ALA B 82  ? 0.411 0.741 0.431 0.004  0.072  -0.059 411 ALA BBB C   
1594 O O   . ALA B 82  ? 0.396 0.745 0.414 0.001  0.080  -0.054 411 ALA BBB O   
1595 C CB  . ALA B 82  ? 0.402 0.727 0.421 -0.005 0.065  -0.059 411 ALA BBB CB  
1596 N N   . PRO B 83  ? 0.442 0.766 0.462 0.017  0.064  -0.073 412 PRO BBB N   
1597 C CA  . PRO B 83  ? 0.457 0.804 0.474 0.031  0.066  -0.084 412 PRO BBB CA  
1598 C C   . PRO B 83  ? 0.448 0.839 0.457 0.029  0.074  -0.088 412 PRO BBB C   
1599 O O   . PRO B 83  ? 0.472 0.869 0.474 0.028  0.073  -0.091 412 PRO BBB O   
1600 C CB  . PRO B 83  ? 0.491 0.817 0.507 0.048  0.052  -0.102 412 PRO BBB CB  
1601 C CG  . PRO B 83  ? 0.498 0.783 0.523 0.038  0.044  -0.096 412 PRO BBB CG  
1602 C CD  . PRO B 83  ? 0.471 0.767 0.497 0.020  0.052  -0.083 412 PRO BBB CD  
1603 N N   . GLY B 84  ? 0.440 0.862 0.450 0.029  0.083  -0.088 413 GLY BBB N   
1604 C CA  . GLY B 84  ? 0.433 0.904 0.438 0.025  0.093  -0.090 413 GLY BBB CA  
1605 C C   . GLY B 84  ? 0.426 0.898 0.425 0.004  0.103  -0.070 413 GLY BBB C   
1606 O O   . GLY B 84  ? 0.441 0.948 0.431 0.001  0.111  -0.067 413 GLY BBB O   
1607 N N   . GLN B 85  ? 0.412 0.849 0.417 -0.008 0.102  -0.056 414 GLN BBB N   
1608 C CA  . GLN B 85  ? 0.424 0.849 0.422 -0.024 0.108  -0.036 414 GLN BBB CA  
1609 C C   . GLN B 85  ? 0.432 0.865 0.441 -0.041 0.116  -0.028 414 GLN BBB C   
1610 O O   . GLN B 85  ? 0.426 0.868 0.450 -0.039 0.115  -0.039 414 GLN BBB O   
1611 C CB  . GLN B 85  ? 0.429 0.815 0.427 -0.023 0.100  -0.030 414 GLN BBB CB  
1612 C CG  . GLN B 85  ? 0.448 0.828 0.440 -0.012 0.091  -0.040 414 GLN BBB CG  
1613 C CD  . GLN B 85  ? 0.466 0.869 0.441 -0.007 0.092  -0.040 414 GLN BBB CD  
1614 O OE1 . GLN B 85  ? 0.491 0.892 0.452 -0.014 0.097  -0.023 414 GLN BBB OE1 
1615 N NE2 . GLN B 85  ? 0.480 0.903 0.452 0.006  0.087  -0.058 414 GLN BBB NE2 
1616 N N   . THR B 86  ? 0.459 0.886 0.462 -0.058 0.123  -0.010 415 THR BBB N   
1617 C CA  . THR B 86  ? 0.474 0.897 0.491 -0.079 0.129  -0.002 415 THR BBB CA  
1618 C C   . THR B 86  ? 0.484 0.858 0.491 -0.086 0.125  0.015  415 THR BBB C   
1619 O O   . THR B 86  ? 0.489 0.846 0.479 -0.074 0.119  0.021  415 THR BBB O   
1620 C CB  . THR B 86  ? 0.493 0.961 0.513 -0.096 0.143  0.005  415 THR BBB CB  
1621 O OG1 . THR B 86  ? 0.518 0.986 0.513 -0.100 0.149  0.025  415 THR BBB OG1 
1622 C CG2 . THR B 86  ? 0.475 0.996 0.502 -0.083 0.146  -0.016 415 THR BBB CG2 
1623 N N   . GLY B 87  ? 0.488 0.842 0.510 -0.103 0.125  0.020  416 GLY BBB N   
1624 C CA  . GLY B 87  ? 0.500 0.801 0.516 -0.106 0.116  0.030  416 GLY BBB CA  
1625 C C   . GLY B 87  ? 0.486 0.774 0.524 -0.105 0.108  0.012  416 GLY BBB C   
1626 O O   . GLY B 87  ? 0.435 0.757 0.489 -0.100 0.109  -0.005 416 GLY BBB O   
1627 N N   . LYS B 88  ? 0.523 0.767 0.562 -0.105 0.098  0.015  417 LYS BBB N   
1628 C CA  . LYS B 88  ? 0.527 0.760 0.586 -0.103 0.087  -0.005 417 LYS BBB CA  
1629 C C   . LYS B 88  ? 0.485 0.749 0.548 -0.080 0.084  -0.023 417 LYS BBB C   
1630 O O   . LYS B 88  ? 0.472 0.756 0.553 -0.080 0.081  -0.042 417 LYS BBB O   
1631 C CB  . LYS B 88  ? 0.574 0.752 0.626 -0.097 0.074  -0.003 417 LYS BBB CB  
1632 C CG  . LYS B 88  ? 0.654 0.788 0.706 -0.121 0.074  0.015  417 LYS BBB CG  
1633 C CD  . LYS B 88  ? 0.689 0.830 0.772 -0.149 0.076  0.005  417 LYS BBB CD  
1634 C CE  . LYS B 88  ? 0.760 0.859 0.842 -0.181 0.081  0.031  417 LYS BBB CE  
1635 N NZ  . LYS B 88  ? 0.790 0.894 0.909 -0.213 0.081  0.017  417 LYS BBB NZ  
1636 N N   . ILE B 89  ? 0.320 0.797 0.330 -0.006 0.023  -0.011 418 ILE BBB N   
1637 C CA  . ILE B 89  ? 0.316 0.796 0.333 0.000  0.018  -0.010 418 ILE BBB CA  
1638 C C   . ILE B 89  ? 0.304 0.786 0.338 0.002  0.023  -0.014 418 ILE BBB C   
1639 O O   . ILE B 89  ? 0.330 0.814 0.377 0.007  0.017  -0.012 418 ILE BBB O   
1640 C CB  . ILE B 89  ? 0.320 0.797 0.324 -0.001 0.016  -0.009 418 ILE BBB CB  
1641 C CG1 . ILE B 89  ? 0.326 0.800 0.318 -0.003 0.010  -0.005 418 ILE BBB CG1 
1642 C CG2 . ILE B 89  ? 0.309 0.788 0.317 0.003  0.013  -0.008 418 ILE BBB CG2 
1643 C CD1 . ILE B 89  ? 0.345 0.823 0.345 0.002  0.004  -0.002 418 ILE BBB CD1 
1644 N N   . ALA B 90  ? 0.314 0.794 0.349 -0.003 0.033  -0.020 419 ALA BBB N   
1645 C CA  . ALA B 90  ? 0.339 0.821 0.396 -0.001 0.039  -0.027 419 ALA BBB CA  
1646 C C   . ALA B 90  ? 0.341 0.828 0.423 0.002  0.038  -0.028 419 ALA BBB C   
1647 O O   . ALA B 90  ? 0.375 0.864 0.479 0.008  0.033  -0.029 419 ALA BBB O   
1648 C CB  . ALA B 90  ? 0.362 0.839 0.413 -0.009 0.053  -0.035 419 ALA BBB CB  
1649 N N   . ASP B 91  ? 0.332 0.822 0.411 -0.002 0.041  -0.029 420 ASP BBB N   
1650 C CA  . ASP B 91  ? 0.323 0.819 0.427 -0.000 0.041  -0.032 420 ASP BBB CA  
1651 C C   . ASP B 91  ? 0.334 0.832 0.443 0.006  0.025  -0.024 420 ASP BBB C   
1652 O O   . ASP B 91  ? 0.332 0.834 0.468 0.010  0.020  -0.025 420 ASP BBB O   
1653 C CB  . ASP B 91  ? 0.334 0.830 0.428 -0.009 0.050  -0.035 420 ASP BBB CB  
1654 C CG  . ASP B 91  ? 0.337 0.828 0.424 -0.019 0.067  -0.044 420 ASP BBB CG  
1655 O OD1 . ASP B 91  ? 0.309 0.801 0.406 -0.019 0.074  -0.051 420 ASP BBB OD1 
1656 O OD2 . ASP B 91  ? 0.347 0.834 0.417 -0.029 0.074  -0.046 420 ASP BBB OD2 
1657 N N   . TYR B 92  ? 0.336 0.830 0.421 0.006  0.018  -0.016 421 TYR BBB N   
1658 C CA  . TYR B 92  ? 0.316 0.810 0.401 0.009  0.007  -0.010 421 TYR BBB CA  
1659 C C   . TYR B 92  ? 0.292 0.780 0.362 0.011  -0.002 -0.005 421 TYR BBB C   
1660 O O   . TYR B 92  ? 0.287 0.773 0.355 0.012  -0.010 -0.000 421 TYR BBB O   
1661 C CB  . TYR B 92  ? 0.329 0.823 0.400 0.006  0.009  -0.008 421 TYR BBB CB  
1662 C CG  . TYR B 92  ? 0.347 0.843 0.426 0.001  0.017  -0.013 421 TYR BBB CG  
1663 C CD1 . TYR B 92  ? 0.364 0.867 0.471 0.001  0.023  -0.020 421 TYR BBB CD1 
1664 C CD2 . TYR B 92  ? 0.378 0.870 0.440 -0.004 0.020  -0.012 421 TYR BBB CD2 
1665 C CE1 . TYR B 92  ? 0.365 0.872 0.480 -0.006 0.033  -0.027 421 TYR BBB CE1 
1666 C CE2 . TYR B 92  ? 0.403 0.896 0.469 -0.011 0.029  -0.017 421 TYR BBB CE2 
1667 C CZ  . TYR B 92  ? 0.388 0.889 0.480 -0.012 0.037  -0.025 421 TYR BBB CZ  
1668 O OH  . TYR B 92  ? 0.406 0.907 0.502 -0.021 0.048  -0.031 421 TYR BBB OH  
1669 N N   . ASN B 93  ? 0.297 0.783 0.357 0.011  0.001  -0.005 422 ASN BBB N   
1670 C CA  . ASN B 93  ? 0.305 0.786 0.349 0.011  -0.004 -0.001 422 ASN BBB CA  
1671 C C   . ASN B 93  ? 0.288 0.764 0.334 0.012  -0.007 -0.001 422 ASN BBB C   
1672 O O   . ASN B 93  ? 0.279 0.749 0.323 0.012  -0.015 0.003  422 ASN BBB O   
1673 C CB  . ASN B 93  ? 0.305 0.788 0.335 0.010  -0.001 -0.002 422 ASN BBB CB  
1674 C CG  . ASN B 93  ? 0.317 0.801 0.344 0.009  -0.002 -0.000 422 ASN BBB CG  
1675 O OD1 . ASN B 93  ? 0.282 0.764 0.303 0.009  -0.005 0.001  422 ASN BBB OD1 
1676 N ND2 . ASN B 93  ? 0.323 0.807 0.351 0.008  0.003  -0.002 422 ASN BBB ND2 
1677 N N   . TYR B 94  ? 0.274 0.752 0.323 0.012  0.000  -0.005 423 TYR BBB N   
1678 C CA  . TYR B 94  ? 0.284 0.757 0.335 0.013  -0.001 -0.005 423 TYR BBB CA  
1679 C C   . TYR B 94  ? 0.304 0.778 0.368 0.013  0.008  -0.012 423 TYR BBB C   
1680 O O   . TYR B 94  ? 0.329 0.806 0.384 0.010  0.017  -0.015 423 TYR BBB O   
1681 C CB  . TYR B 94  ? 0.277 0.746 0.307 0.010  -0.000 -0.004 423 TYR BBB CB  
1682 C CG  . TYR B 94  ? 0.277 0.739 0.306 0.009  -0.002 -0.004 423 TYR BBB CG  
1683 C CD1 . TYR B 94  ? 0.279 0.732 0.303 0.008  -0.011 0.000  423 TYR BBB CD1 
1684 C CD2 . TYR B 94  ? 0.285 0.748 0.316 0.009  0.005  -0.008 423 TYR BBB CD2 
1685 C CE1 . TYR B 94  ? 0.286 0.729 0.306 0.006  -0.014 0.001  423 TYR BBB CE1 
1686 C CE2 . TYR B 94  ? 0.289 0.743 0.318 0.008  0.003  -0.008 423 TYR BBB CE2 
1687 C CZ  . TYR B 94  ? 0.283 0.728 0.307 0.007  -0.006 -0.003 423 TYR BBB CZ  
1688 O OH  . TYR B 94  ? 0.299 0.733 0.320 0.006  -0.009 -0.003 423 TYR BBB OH  
1689 N N   . LYS B 95  ? 0.307 0.780 0.394 0.016  0.005  -0.014 424 LYS BBB N   
1690 C CA  . LYS B 95  ? 0.310 0.785 0.418 0.017  0.015  -0.022 424 LYS BBB CA  
1691 C C   . LYS B 95  ? 0.315 0.782 0.428 0.018  0.013  -0.023 424 LYS BBB C   
1692 O O   . LYS B 95  ? 0.310 0.770 0.435 0.022  -0.000 -0.019 424 LYS BBB O   
1693 C CB  . LYS B 95  ? 0.329 0.809 0.468 0.020  0.013  -0.026 424 LYS BBB CB  
1694 C CG  . LYS B 95  ? 0.340 0.823 0.507 0.019  0.026  -0.038 424 LYS BBB CG  
1695 C CD  . LYS B 95  ? 0.346 0.831 0.497 0.012  0.044  -0.045 424 LYS BBB CD  
1696 C CE  . LYS B 95  ? 0.355 0.843 0.534 0.009  0.060  -0.059 424 LYS BBB CE  
1697 N NZ  . LYS B 95  ? 0.379 0.864 0.533 -0.002 0.077  -0.066 424 LYS BBB NZ  
1698 N N   . LEU B 96  ? 0.335 0.800 0.437 0.015  0.023  -0.028 425 LEU BBB N   
1699 C CA  . LEU B 96  ? 0.357 0.815 0.469 0.016  0.025  -0.032 425 LEU BBB CA  
1700 C C   . LEU B 96  ? 0.347 0.808 0.495 0.019  0.032  -0.042 425 LEU BBB C   
1701 O O   . LEU B 96  ? 0.340 0.808 0.497 0.016  0.042  -0.049 425 LEU BBB O   
1702 C CB  . LEU B 96  ? 0.374 0.829 0.462 0.010  0.034  -0.035 425 LEU BBB CB  
1703 C CG  . LEU B 96  ? 0.398 0.851 0.458 0.008  0.028  -0.027 425 LEU BBB CG  
1704 C CD1 . LEU B 96  ? 0.411 0.861 0.453 0.002  0.035  -0.031 425 LEU BBB CD1 
1705 C CD2 . LEU B 96  ? 0.419 0.863 0.479 0.011  0.015  -0.021 425 LEU BBB CD2 
1706 N N   . PRO B 97  ? 0.355 0.808 0.527 0.024  0.026  -0.044 426 PRO BBB N   
1707 C CA  . PRO B 97  ? 0.361 0.817 0.574 0.027  0.034  -0.056 426 PRO BBB CA  
1708 C C   . PRO B 97  ? 0.370 0.827 0.578 0.020  0.056  -0.069 426 PRO BBB C   
1709 O O   . PRO B 97  ? 0.411 0.861 0.587 0.015  0.059  -0.066 426 PRO BBB O   
1710 C CB  . PRO B 97  ? 0.366 0.811 0.603 0.034  0.018  -0.052 426 PRO BBB CB  
1711 C CG  . PRO B 97  ? 0.378 0.812 0.575 0.031  0.009  -0.042 426 PRO BBB CG  
1712 C CD  . PRO B 97  ? 0.364 0.804 0.526 0.026  0.011  -0.035 426 PRO BBB CD  
1713 N N   . ASP B 98  ? 0.364 0.828 0.603 0.018  0.071  -0.083 427 ASP BBB N   
1714 C CA  . ASP B 98  ? 0.381 0.842 0.617 0.009  0.095  -0.098 427 ASP BBB CA  
1715 C C   . ASP B 98  ? 0.379 0.829 0.611 0.011  0.093  -0.099 427 ASP BBB C   
1716 O O   . ASP B 98  ? 0.405 0.849 0.609 0.001  0.107  -0.104 427 ASP BBB O   
1717 C CB  . ASP B 98  ? 0.384 0.853 0.666 0.009  0.110  -0.115 427 ASP BBB CB  
1718 C CG  . ASP B 98  ? 0.385 0.865 0.665 0.002  0.120  -0.119 427 ASP BBB CG  
1719 O OD1 . ASP B 98  ? 0.367 0.847 0.609 -0.001 0.112  -0.107 427 ASP BBB OD1 
1720 O OD2 . ASP B 98  ? 0.435 0.922 0.752 -0.000 0.135  -0.134 427 ASP BBB OD2 
1721 N N   . ASP B 99  ? 0.360 0.804 0.616 0.021  0.076  -0.093 428 ASP BBB N   
1722 C CA  . ASP B 99  ? 0.363 0.794 0.622 0.023  0.074  -0.095 428 ASP BBB CA  
1723 C C   . ASP B 99  ? 0.356 0.778 0.576 0.023  0.057  -0.078 428 ASP BBB C   
1724 O O   . ASP B 99  ? 0.334 0.744 0.559 0.026  0.047  -0.075 428 ASP BBB O   
1725 C CB  . ASP B 99  ? 0.374 0.801 0.688 0.032  0.067  -0.101 428 ASP BBB CB  
1726 C CG  . ASP B 99  ? 0.363 0.788 0.695 0.042  0.040  -0.088 428 ASP BBB CG  
1727 O OD1 . ASP B 99  ? 0.374 0.803 0.679 0.041  0.030  -0.075 428 ASP BBB OD1 
1728 O OD2 . ASP B 99  ? 0.366 0.783 0.737 0.050  0.027  -0.089 428 ASP BBB OD2 
1729 N N   . PHE B 100 ? 0.371 0.798 0.555 0.018  0.054  -0.069 429 PHE BBB N   
1730 C CA  . PHE B 100 ? 0.396 0.817 0.545 0.017  0.041  -0.055 429 PHE BBB CA  
1731 C C   . PHE B 100 ? 0.435 0.845 0.567 0.013  0.046  -0.058 429 PHE BBB C   
1732 O O   . PHE B 100 ? 0.470 0.882 0.593 0.006  0.063  -0.067 429 PHE BBB O   
1733 C CB  . PHE B 100 ? 0.388 0.818 0.505 0.012  0.043  -0.050 429 PHE BBB CB  
1734 C CG  . PHE B 100 ? 0.388 0.813 0.473 0.009  0.033  -0.039 429 PHE BBB CG  
1735 C CD1 . PHE B 100 ? 0.388 0.807 0.471 0.012  0.017  -0.030 429 PHE BBB CD1 
1736 C CD2 . PHE B 100 ? 0.399 0.825 0.458 0.002  0.040  -0.040 429 PHE BBB CD2 
1737 C CE1 . PHE B 100 ? 0.392 0.807 0.447 0.008  0.012  -0.023 429 PHE BBB CE1 
1738 C CE2 . PHE B 100 ? 0.412 0.836 0.448 -0.000 0.033  -0.033 429 PHE BBB CE2 
1739 C CZ  . PHE B 100 ? 0.414 0.833 0.449 0.002  0.020  -0.025 429 PHE BBB CZ  
1740 N N   . THR B 101 ? 0.490 0.889 0.618 0.015  0.032  -0.050 430 THR BBB N   
1741 C CA  . THR B 101 ? 0.506 0.894 0.614 0.011  0.033  -0.049 430 THR BBB CA  
1742 C C   . THR B 101 ? 0.535 0.920 0.610 0.007  0.022  -0.037 430 THR BBB C   
1743 O O   . THR B 101 ? 0.598 0.976 0.675 0.010  0.007  -0.028 430 THR BBB O   
1744 C CB  . THR B 101 ? 0.541 0.913 0.673 0.015  0.027  -0.051 430 THR BBB CB  
1745 O OG1 . THR B 101 ? 0.540 0.915 0.700 0.016  0.043  -0.066 430 THR BBB OG1 
1746 C CG2 . THR B 101 ? 0.606 0.963 0.713 0.011  0.021  -0.046 430 THR BBB CG2 
1747 N N   . GLY B 102 ? 0.479 0.869 0.527 -0.000 0.029  -0.037 431 GLY BBB N   
1748 C CA  . GLY B 102 ? 0.451 0.840 0.471 -0.005 0.023  -0.029 431 GLY BBB CA  
1749 C C   . GLY B 102 ? 0.437 0.839 0.439 -0.011 0.031  -0.032 431 GLY BBB C   
1750 O O   . GLY B 102 ? 0.431 0.834 0.434 -0.013 0.042  -0.039 431 GLY BBB O   
1751 N N   . CYS B 103 ? 0.415 0.823 0.402 -0.013 0.027  -0.027 432 CYS BBB N   
1752 C CA  . CYS B 103 ? 0.412 0.830 0.384 -0.018 0.031  -0.028 432 CYS BBB CA  
1753 C C   . CYS B 103 ? 0.388 0.817 0.361 -0.016 0.028  -0.024 432 CYS BBB C   
1754 O O   . CYS B 103 ? 0.387 0.814 0.362 -0.014 0.022  -0.020 432 CYS BBB O   
1755 C CB  . CYS B 103 ? 0.413 0.828 0.371 -0.025 0.031  -0.028 432 CYS BBB CB  
1756 S SG  . CYS B 103 ? 0.450 0.851 0.405 -0.028 0.035  -0.032 432 CYS BBB SG  
1757 N N   . VAL B 104 ? 0.378 0.817 0.350 -0.017 0.031  -0.026 433 VAL BBB N   
1758 C CA  . VAL B 104 ? 0.368 0.816 0.339 -0.016 0.027  -0.023 433 VAL BBB CA  
1759 C C   . VAL B 104 ? 0.374 0.828 0.337 -0.020 0.025  -0.024 433 VAL BBB C   
1760 O O   . VAL B 104 ? 0.354 0.807 0.310 -0.025 0.027  -0.026 433 VAL BBB O   
1761 C CB  . VAL B 104 ? 0.367 0.818 0.343 -0.014 0.030  -0.025 433 VAL BBB CB  
1762 C CG1 . VAL B 104 ? 0.369 0.828 0.343 -0.014 0.026  -0.022 433 VAL BBB CG1 
1763 C CG2 . VAL B 104 ? 0.376 0.823 0.367 -0.009 0.032  -0.026 433 VAL BBB CG2 
1764 N N   . ILE B 105 ? 0.368 0.827 0.332 -0.020 0.022  -0.022 434 ILE BBB N   
1765 C CA  . ILE B 105 ? 0.383 0.851 0.348 -0.024 0.020  -0.024 434 ILE BBB CA  
1766 C C   . ILE B 105 ? 0.372 0.849 0.346 -0.021 0.016  -0.023 434 ILE BBB C   
1767 O O   . ILE B 105 ? 0.359 0.836 0.336 -0.018 0.016  -0.022 434 ILE BBB O   
1768 C CB  . ILE B 105 ? 0.386 0.851 0.348 -0.029 0.023  -0.026 434 ILE BBB CB  
1769 C CG1 . ILE B 105 ? 0.393 0.846 0.346 -0.031 0.025  -0.026 434 ILE BBB CG1 
1770 C CG2 . ILE B 105 ? 0.395 0.870 0.363 -0.033 0.022  -0.031 434 ILE BBB CG2 
1771 C CD1 . ILE B 105 ? 0.406 0.851 0.351 -0.036 0.027  -0.026 434 ILE BBB CD1 
1772 N N   . ALA B 106 ? 0.377 0.859 0.354 -0.022 0.011  -0.024 435 ALA BBB N   
1773 C CA  . ALA B 106 ? 0.365 0.855 0.353 -0.019 0.005  -0.022 435 ALA BBB CA  
1774 C C   . ALA B 106 ? 0.374 0.871 0.372 -0.021 -0.002 -0.025 435 ALA BBB C   
1775 O O   . ALA B 106 ? 0.349 0.843 0.341 -0.026 -0.004 -0.025 435 ALA BBB O   
1776 C CB  . ALA B 106 ? 0.365 0.849 0.346 -0.017 0.003  -0.018 435 ALA BBB CB  
1777 N N   . TRP B 107 ? 0.359 0.865 0.375 -0.018 -0.005 -0.027 436 TRP BBB N   
1778 C CA  . TRP B 107 ? 0.344 0.859 0.381 -0.019 -0.014 -0.030 436 TRP BBB CA  
1779 C C   . TRP B 107 ? 0.320 0.839 0.374 -0.013 -0.020 -0.030 436 TRP BBB C   
1780 O O   . TRP B 107 ? 0.289 0.808 0.342 -0.010 -0.014 -0.030 436 TRP BBB O   
1781 C CB  . TRP B 107 ? 0.354 0.878 0.404 -0.023 -0.007 -0.038 436 TRP BBB CB  
1782 C CG  . TRP B 107 ? 0.346 0.874 0.403 -0.022 0.004  -0.044 436 TRP BBB CG  
1783 C CD1 . TRP B 107 ? 0.330 0.869 0.413 -0.021 0.006  -0.052 436 TRP BBB CD1 
1784 C CD2 . TRP B 107 ? 0.363 0.883 0.401 -0.025 0.014  -0.043 436 TRP BBB CD2 
1785 N NE1 . TRP B 107 ? 0.340 0.878 0.417 -0.025 0.019  -0.057 436 TRP BBB NE1 
1786 C CE2 . TRP B 107 ? 0.358 0.882 0.405 -0.027 0.022  -0.051 436 TRP BBB CE2 
1787 C CE3 . TRP B 107 ? 0.380 0.887 0.394 -0.026 0.017  -0.038 436 TRP BBB CE3 
1788 C CZ2 . TRP B 107 ? 0.371 0.886 0.400 -0.032 0.031  -0.051 436 TRP BBB CZ2 
1789 C CZ3 . TRP B 107 ? 0.381 0.880 0.382 -0.029 0.023  -0.038 436 TRP BBB CZ3 
1790 C CH2 . TRP B 107 ? 0.382 0.883 0.388 -0.032 0.030  -0.043 436 TRP BBB CH2 
1791 N N   . ASN B 108 ? 0.301 0.822 0.369 -0.013 -0.035 -0.028 437 ASN BBB N   
1792 C CA  . ASN B 108 ? 0.299 0.823 0.389 -0.007 -0.044 -0.028 437 ASN BBB CA  
1793 C C   . ASN B 108 ? 0.291 0.830 0.411 -0.005 -0.034 -0.039 437 ASN BBB C   
1794 O O   . ASN B 108 ? 0.293 0.841 0.428 -0.008 -0.031 -0.047 437 ASN BBB O   
1795 C CB  . ASN B 108 ? 0.305 0.826 0.405 -0.008 -0.064 -0.024 437 ASN BBB CB  
1796 C CG  . ASN B 108 ? 0.303 0.823 0.424 -0.003 -0.077 -0.022 437 ASN BBB CG  
1797 O OD1 . ASN B 108 ? 0.296 0.828 0.449 0.003  -0.074 -0.030 437 ASN BBB OD1 
1798 N ND2 . ASN B 108 ? 0.306 0.811 0.407 -0.005 -0.091 -0.012 437 ASN BBB ND2 
1799 N N   . SER B 109 ? 0.287 0.826 0.412 -0.000 -0.029 -0.041 438 SER BBB N   
1800 C CA  . SER B 109 ? 0.289 0.839 0.436 -0.000 -0.017 -0.053 438 SER BBB CA  
1801 C C   . SER B 109 ? 0.303 0.857 0.482 0.006  -0.025 -0.056 438 SER BBB C   
1802 O O   . SER B 109 ? 0.304 0.864 0.496 0.007  -0.013 -0.065 438 SER BBB O   
1803 C CB  . SER B 109 ? 0.283 0.826 0.405 -0.003 -0.003 -0.052 438 SER BBB CB  
1804 O OG  . SER B 109 ? 0.277 0.812 0.386 0.002  -0.007 -0.044 438 SER BBB OG  
1805 N N   . ASN B 110 ? 0.322 0.873 0.512 0.010  -0.044 -0.050 439 ASN BBB N   
1806 C CA  . ASN B 110 ? 0.325 0.878 0.547 0.016  -0.057 -0.051 439 ASN BBB CA  
1807 C C   . ASN B 110 ? 0.316 0.886 0.584 0.018  -0.048 -0.068 439 ASN BBB C   
1808 O O   . ASN B 110 ? 0.323 0.894 0.612 0.023  -0.045 -0.074 439 ASN BBB O   
1809 C CB  . ASN B 110 ? 0.337 0.881 0.562 0.017  -0.082 -0.042 439 ASN BBB CB  
1810 C CG  . ASN B 110 ? 0.343 0.880 0.586 0.024  -0.099 -0.038 439 ASN BBB CG  
1811 O OD1 . ASN B 110 ? 0.367 0.898 0.599 0.026  -0.093 -0.036 439 ASN BBB OD1 
1812 N ND2 . ASN B 110 ? 0.346 0.881 0.615 0.026  -0.121 -0.035 439 ASN BBB ND2 
1813 N N   . ASN B 111 ? 0.305 0.886 0.587 0.013  -0.042 -0.076 440 ASN BBB N   
1814 C CA  A ASN B 111 ? 0.317 0.915 0.646 0.013  -0.031 -0.095 440 ASN BBB CA  
1815 C CA  B ASN B 111 ? 0.310 0.908 0.639 0.013  -0.031 -0.095 440 ASN BBB CA  
1816 C C   . ASN B 111 ? 0.317 0.918 0.638 0.008  -0.006 -0.106 440 ASN BBB C   
1817 O O   . ASN B 111 ? 0.320 0.932 0.680 0.008  0.005  -0.122 440 ASN BBB O   
1818 C CB  A ASN B 111 ? 0.316 0.925 0.659 0.007  -0.031 -0.100 440 ASN BBB CB  
1819 C CB  B ASN B 111 ? 0.300 0.909 0.644 0.008  -0.032 -0.100 440 ASN BBB CB  
1820 C CG  A ASN B 111 ? 0.319 0.923 0.618 -0.002 -0.015 -0.098 440 ASN BBB CG  
1821 C CG  B ASN B 111 ? 0.300 0.907 0.655 0.011  -0.059 -0.090 440 ASN BBB CG  
1822 O OD1 A ASN B 111 ? 0.328 0.918 0.584 -0.002 -0.018 -0.084 440 ASN BBB OD1 
1823 O OD1 B ASN B 111 ? 0.292 0.893 0.666 0.018  -0.079 -0.085 440 ASN BBB OD1 
1824 N ND2 A ASN B 111 ? 0.315 0.931 0.628 -0.010 0.001  -0.111 440 ASN BBB ND2 
1825 N ND2 B ASN B 111 ? 0.303 0.910 0.645 0.005  -0.061 -0.087 440 ASN BBB ND2 
1826 N N   . LEU B 112 ? 0.322 0.910 0.594 0.003  0.004  -0.098 441 LEU BBB N   
1827 C CA  . LEU B 112 ? 0.328 0.913 0.582 -0.004 0.026  -0.106 441 LEU BBB CA  
1828 C C   . LEU B 112 ? 0.329 0.905 0.570 0.000  0.025  -0.101 441 LEU BBB C   
1829 O O   . LEU B 112 ? 0.356 0.932 0.605 -0.004 0.040  -0.112 441 LEU BBB O   
1830 C CB  . LEU B 112 ? 0.343 0.919 0.552 -0.012 0.034  -0.099 441 LEU BBB CB  
1831 C CG  . LEU B 112 ? 0.349 0.933 0.565 -0.019 0.038  -0.105 441 LEU BBB CG  
1832 C CD1 . LEU B 112 ? 0.359 0.930 0.530 -0.025 0.040  -0.094 441 LEU BBB CD1 
1833 C CD2 . LEU B 112 ? 0.348 0.941 0.585 -0.029 0.058  -0.124 441 LEU BBB CD2 
1834 N N   . ASP B 113 ? 0.327 0.892 0.546 0.006  0.010  -0.085 442 ASP BBB N   
1835 C CA  . ASP B 113 ? 0.324 0.878 0.519 0.008  0.011  -0.078 442 ASP BBB CA  
1836 C C   . ASP B 113 ? 0.351 0.902 0.565 0.017  -0.004 -0.074 442 ASP BBB C   
1837 O O   . ASP B 113 ? 0.368 0.911 0.565 0.018  -0.004 -0.069 442 ASP BBB O   
1838 C CB  . ASP B 113 ? 0.308 0.851 0.461 0.006  0.007  -0.064 442 ASP BBB CB  
1839 C CG  . ASP B 113 ? 0.309 0.850 0.440 -0.003 0.021  -0.067 442 ASP BBB CG  
1840 O OD1 . ASP B 113 ? 0.305 0.844 0.433 -0.009 0.035  -0.075 442 ASP BBB OD1 
1841 O OD2 . ASP B 113 ? 0.300 0.837 0.413 -0.004 0.018  -0.060 442 ASP BBB OD2 
1842 N N   . SER B 114 ? 0.354 0.911 0.602 0.022  -0.017 -0.076 443 SER BBB N   
1843 C CA  . SER B 114 ? 0.353 0.906 0.625 0.030  -0.033 -0.073 443 SER BBB CA  
1844 C C   . SER B 114 ? 0.351 0.917 0.673 0.033  -0.026 -0.091 443 SER BBB C   
1845 O O   . SER B 114 ? 0.324 0.903 0.668 0.029  -0.014 -0.104 443 SER BBB O   
1846 C CB  . SER B 114 ? 0.366 0.914 0.641 0.033  -0.057 -0.062 443 SER BBB CB  
1847 O OG  . SER B 114 ? 0.390 0.949 0.708 0.036  -0.066 -0.070 443 SER BBB OG  
1848 N N   . LYS B 115 ? 0.377 0.938 0.717 0.039  -0.031 -0.093 444 LYS BBB N   
1849 C CA  . LYS B 115 ? 0.421 0.992 0.814 0.042  -0.024 -0.110 444 LYS BBB CA  
1850 C C   . LYS B 115 ? 0.410 0.972 0.829 0.052  -0.048 -0.104 444 LYS BBB C   
1851 O O   . LYS B 115 ? 0.393 0.939 0.776 0.054  -0.059 -0.089 444 LYS BBB O   
1852 C CB  . LYS B 115 ? 0.480 1.051 0.862 0.036  0.002  -0.123 444 LYS BBB CB  
1853 C CG  . LYS B 115 ? 0.544 1.121 0.909 0.024  0.025  -0.133 444 LYS BBB CG  
1854 C CD  . LYS B 115 ? 0.614 1.182 0.939 0.015  0.044  -0.135 444 LYS BBB CD  
1855 C CE  . LYS B 115 ? 0.630 1.195 0.913 0.004  0.055  -0.131 444 LYS BBB CE  
1856 N NZ  . LYS B 115 ? 0.629 1.181 0.870 -0.006 0.067  -0.129 444 LYS BBB NZ  
1857 N N   . VAL B 116 ? 0.393 0.964 0.871 0.059  -0.055 -0.116 445 VAL BBB N   
1858 C CA  . VAL B 116 ? 0.410 0.972 0.922 0.069  -0.077 -0.113 445 VAL BBB CA  
1859 C C   . VAL B 116 ? 0.413 0.965 0.906 0.069  -0.065 -0.115 445 VAL BBB C   
1860 O O   . VAL B 116 ? 0.422 0.983 0.917 0.063  -0.038 -0.130 445 VAL BBB O   
1861 C CB  . VAL B 116 ? 0.407 0.985 0.996 0.076  -0.082 -0.131 445 VAL BBB CB  
1862 C CG1 . VAL B 116 ? 0.416 0.980 1.039 0.086  -0.112 -0.124 445 VAL BBB CG1 
1863 C CG2 . VAL B 116 ? 0.396 0.988 1.005 0.073  -0.086 -0.134 445 VAL BBB CG2 
1864 N N   . GLY B 117 ? 0.409 0.942 0.881 0.072  -0.084 -0.099 446 GLY BBB N   
1865 C CA  . GLY B 117 ? 0.410 0.931 0.855 0.071  -0.075 -0.096 446 GLY BBB CA  
1866 C C   . GLY B 117 ? 0.398 0.911 0.777 0.063  -0.068 -0.082 446 GLY BBB C   
1867 O O   . GLY B 117 ? 0.413 0.913 0.765 0.062  -0.068 -0.075 446 GLY BBB O   
1868 N N   . GLY B 118 ? 0.381 0.902 0.739 0.058  -0.062 -0.080 447 GLY BBB N   
1869 C CA  . GLY B 118 ? 0.382 0.897 0.684 0.051  -0.056 -0.068 447 GLY BBB CA  
1870 C C   . GLY B 118 ? 0.379 0.901 0.663 0.044  -0.030 -0.077 447 GLY BBB C   
1871 O O   . GLY B 118 ? 0.383 0.907 0.680 0.043  -0.016 -0.089 447 GLY BBB O   
1872 N N   . ASN B 119 ? 0.373 0.899 0.629 0.038  -0.023 -0.073 448 ASN BBB N   
1873 C CA  . ASN B 119 ? 0.360 0.886 0.586 0.029  -0.004 -0.076 448 ASN BBB CA  
1874 C C   . ASN B 119 ? 0.360 0.874 0.545 0.028  -0.008 -0.062 448 ASN BBB C   
1875 O O   . ASN B 119 ? 0.363 0.873 0.531 0.029  -0.019 -0.050 448 ASN BBB O   
1876 C CB  . ASN B 119 ? 0.365 0.899 0.586 0.024  0.005  -0.080 448 ASN BBB CB  
1877 C CG  . ASN B 119 ? 0.368 0.899 0.555 0.014  0.021  -0.081 448 ASN BBB CG  
1878 O OD1 . ASN B 119 ? 0.366 0.890 0.541 0.010  0.030  -0.085 448 ASN BBB OD1 
1879 N ND2 . ASN B 119 ? 0.371 0.904 0.541 0.009  0.023  -0.078 448 ASN BBB ND2 
1880 N N   . TYR B 120 ? 0.365 0.873 0.535 0.025  0.001  -0.064 449 TYR BBB N   
1881 C CA  . TYR B 120 ? 0.346 0.844 0.484 0.023  -0.002 -0.052 449 TYR BBB CA  
1882 C C   . TYR B 120 ? 0.338 0.835 0.449 0.015  0.010  -0.053 449 TYR BBB C   
1883 O O   . TYR B 120 ? 0.370 0.859 0.459 0.014  0.008  -0.045 449 TYR BBB O   
1884 C CB  . TYR B 120 ? 0.360 0.851 0.506 0.026  -0.006 -0.053 449 TYR BBB CB  
1885 C CG  . TYR B 120 ? 0.381 0.869 0.552 0.034  -0.021 -0.050 449 TYR BBB CG  
1886 C CD1 . TYR B 120 ? 0.408 0.887 0.565 0.036  -0.036 -0.037 449 TYR BBB CD1 
1887 C CD2 . TYR B 120 ? 0.386 0.880 0.597 0.038  -0.021 -0.062 449 TYR BBB CD2 
1888 C CE1 . TYR B 120 ? 0.417 0.890 0.593 0.041  -0.053 -0.033 449 TYR BBB CE1 
1889 C CE2 . TYR B 120 ? 0.392 0.882 0.629 0.046  -0.039 -0.059 449 TYR BBB CE2 
1890 C CZ  . TYR B 120 ? 0.398 0.875 0.614 0.047  -0.056 -0.043 449 TYR BBB CZ  
1891 O OH  . TYR B 120 ? 0.469 0.938 0.707 0.052  -0.076 -0.039 449 TYR BBB OH  
1892 N N   . ASN B 121 ? 0.336 0.838 0.447 0.009  0.021  -0.061 450 ASN BBB N   
1893 C CA  . ASN B 121 ? 0.356 0.852 0.440 -0.001 0.031  -0.062 450 ASN BBB CA  
1894 C C   . ASN B 121 ? 0.355 0.847 0.415 -0.001 0.024  -0.050 450 ASN BBB C   
1895 O O   . ASN B 121 ? 0.370 0.854 0.406 -0.007 0.026  -0.046 450 ASN BBB O   
1896 C CB  . ASN B 121 ? 0.368 0.867 0.458 -0.009 0.045  -0.075 450 ASN BBB CB  
1897 C CG  . ASN B 121 ? 0.389 0.888 0.496 -0.013 0.057  -0.090 450 ASN BBB CG  
1898 O OD1 . ASN B 121 ? 0.421 0.916 0.531 -0.010 0.054  -0.089 450 ASN BBB OD1 
1899 N ND2 . ASN B 121 ? 0.392 0.897 0.514 -0.020 0.071  -0.105 450 ASN BBB ND2 
1900 N N   . TYR B 122 ? 0.337 0.835 0.404 0.005  0.016  -0.044 451 TYR BBB N   
1901 C CA  . TYR B 122 ? 0.333 0.828 0.382 0.005  0.010  -0.034 451 TYR BBB CA  
1902 C C   . TYR B 122 ? 0.326 0.816 0.368 0.009  0.003  -0.025 451 TYR BBB C   
1903 O O   . TYR B 122 ? 0.324 0.814 0.376 0.013  -0.003 -0.023 451 TYR BBB O   
1904 C CB  . TYR B 122 ? 0.334 0.834 0.391 0.008  0.006  -0.032 451 TYR BBB CB  
1905 C CG  . TYR B 122 ? 0.340 0.846 0.402 0.003  0.014  -0.040 451 TYR BBB CG  
1906 C CD1 . TYR B 122 ? 0.344 0.844 0.385 -0.004 0.020  -0.039 451 TYR BBB CD1 
1907 C CD2 . TYR B 122 ? 0.321 0.835 0.407 0.004  0.015  -0.049 451 TYR BBB CD2 
1908 C CE1 . TYR B 122 ? 0.344 0.846 0.385 -0.010 0.028  -0.046 451 TYR BBB CE1 
1909 C CE2 . TYR B 122 ? 0.316 0.835 0.408 -0.002 0.024  -0.057 451 TYR BBB CE2 
1910 C CZ  . TYR B 122 ? 0.323 0.835 0.390 -0.009 0.031  -0.056 451 TYR BBB CZ  
1911 O OH  . TYR B 122 ? 0.339 0.855 0.407 -0.017 0.041  -0.064 451 TYR BBB OH  
1912 N N   . LEU B 123 ? 0.331 0.816 0.356 0.006  0.003  -0.020 452 LEU BBB N   
1913 C CA  . LEU B 123 ? 0.326 0.808 0.347 0.008  -0.001 -0.014 452 LEU BBB CA  
1914 C C   . LEU B 123 ? 0.322 0.804 0.336 0.008  -0.004 -0.008 452 LEU BBB C   
1915 O O   . LEU B 123 ? 0.313 0.795 0.324 0.007  -0.002 -0.009 452 LEU BBB O   
1916 C CB  . LEU B 123 ? 0.334 0.810 0.346 0.003  0.000  -0.015 452 LEU BBB CB  
1917 C CG  . LEU B 123 ? 0.335 0.809 0.349 -0.000 0.006  -0.023 452 LEU BBB CG  
1918 C CD1 . LEU B 123 ? 0.335 0.800 0.334 -0.007 0.007  -0.022 452 LEU BBB CD1 
1919 C CD2 . LEU B 123 ? 0.339 0.815 0.370 0.005  0.005  -0.026 452 LEU BBB CD2 
1920 N N   . TYR B 124 ? 0.312 0.792 0.326 0.010  -0.007 -0.004 453 TYR BBB N   
1921 C CA  . TYR B 124 ? 0.310 0.791 0.323 0.009  -0.007 -0.001 453 TYR BBB CA  
1922 C C   . TYR B 124 ? 0.299 0.779 0.313 0.009  -0.008 0.001  453 TYR BBB C   
1923 O O   . TYR B 124 ? 0.302 0.780 0.316 0.009  -0.009 0.001  453 TYR BBB O   
1924 C CB  . TYR B 124 ? 0.306 0.787 0.317 0.009  -0.006 -0.000 453 TYR BBB CB  
1925 C CG  . TYR B 124 ? 0.309 0.786 0.318 0.009  -0.009 0.002  453 TYR BBB CG  
1926 C CD1 . TYR B 124 ? 0.315 0.791 0.327 0.011  -0.014 0.001  453 TYR BBB CD1 
1927 C CD2 . TYR B 124 ? 0.334 0.808 0.339 0.006  -0.008 0.004  453 TYR BBB CD2 
1928 C CE1 . TYR B 124 ? 0.341 0.810 0.351 0.010  -0.020 0.004  453 TYR BBB CE1 
1929 C CE2 . TYR B 124 ? 0.350 0.816 0.348 0.004  -0.013 0.006  453 TYR BBB CE2 
1930 C CZ  . TYR B 124 ? 0.366 0.830 0.367 0.006  -0.020 0.007  453 TYR BBB CZ  
1931 O OH  . TYR B 124 ? 0.397 0.850 0.392 0.004  -0.027 0.010  453 TYR BBB OH  
1932 N N   . ARG B 125 ? 0.283 0.764 0.302 0.008  -0.008 0.002  454 ARG BBB N   
1933 C CA  . ARG B 125 ? 0.309 0.790 0.335 0.007  -0.009 0.003  454 ARG BBB CA  
1934 C C   . ARG B 125 ? 0.308 0.791 0.335 0.005  -0.004 0.002  454 ARG BBB C   
1935 O O   . ARG B 125 ? 0.287 0.770 0.313 0.005  0.001  0.000  454 ARG BBB O   
1936 C CB  . ARG B 125 ? 0.313 0.796 0.349 0.008  -0.012 0.004  454 ARG BBB CB  
1937 C CG  . ARG B 125 ? 0.317 0.802 0.366 0.007  -0.015 0.004  454 ARG BBB CG  
1938 C CD  . ARG B 125 ? 0.320 0.804 0.383 0.008  -0.022 0.005  454 ARG BBB CD  
1939 N NE  . ARG B 125 ? 0.327 0.803 0.376 0.006  -0.030 0.009  454 ARG BBB NE  
1940 C CZ  . ARG B 125 ? 0.333 0.803 0.370 0.002  -0.036 0.012  454 ARG BBB CZ  
1941 N NH1 . ARG B 125 ? 0.324 0.796 0.364 0.001  -0.036 0.011  454 ARG BBB NH1 
1942 N NH2 . ARG B 125 ? 0.346 0.805 0.366 -0.003 -0.041 0.014  454 ARG BBB NH2 
1943 N N   . LEU B 126 ? 0.315 0.795 0.338 0.003  -0.004 0.003  455 LEU BBB N   
1944 C CA  . LEU B 126 ? 0.323 0.799 0.341 -0.001 -0.000 0.003  455 LEU BBB CA  
1945 C C   . LEU B 126 ? 0.339 0.819 0.368 -0.005 0.005  -0.000 455 LEU BBB C   
1946 O O   . LEU B 126 ? 0.312 0.791 0.338 -0.010 0.013  -0.003 455 LEU BBB O   
1947 C CB  . LEU B 126 ? 0.340 0.809 0.348 -0.002 -0.005 0.005  455 LEU BBB CB  
1948 C CG  . LEU B 126 ? 0.381 0.841 0.378 -0.008 -0.003 0.007  455 LEU BBB CG  
1949 C CD1 . LEU B 126 ? 0.396 0.850 0.380 -0.012 -0.003 0.007  455 LEU BBB CD1 
1950 C CD2 . LEU B 126 ? 0.392 0.844 0.383 -0.008 -0.010 0.010  455 LEU BBB CD2 
1951 N N   . PHE B 127 ? 0.340 0.825 0.382 -0.002 0.001  -0.000 456 PHE BBB N   
1952 C CA  . PHE B 127 ? 0.338 0.829 0.398 -0.005 0.004  -0.003 456 PHE BBB CA  
1953 C C   . PHE B 127 ? 0.349 0.846 0.430 -0.001 -0.001 -0.004 456 PHE BBB C   
1954 O O   . PHE B 127 ? 0.379 0.873 0.455 0.002  -0.010 -0.000 456 PHE BBB O   
1955 C CB  . PHE B 127 ? 0.343 0.832 0.401 -0.007 0.000  -0.001 456 PHE BBB CB  
1956 C CG  . PHE B 127 ? 0.353 0.833 0.393 -0.012 0.003  -0.000 456 PHE BBB CG  
1957 C CD1 . PHE B 127 ? 0.364 0.843 0.403 -0.019 0.012  -0.003 456 PHE BBB CD1 
1958 C CD2 . PHE B 127 ? 0.359 0.832 0.385 -0.009 -0.003 0.004  456 PHE BBB CD2 
1959 C CE1 . PHE B 127 ? 0.378 0.845 0.396 -0.025 0.012  -0.001 456 PHE BBB CE1 
1960 C CE2 . PHE B 127 ? 0.370 0.834 0.383 -0.013 -0.003 0.006  456 PHE BBB CE2 
1961 C CZ  . PHE B 127 ? 0.390 0.848 0.396 -0.021 0.003  0.004  456 PHE BBB CZ  
1962 N N   . ARG B 128 ? 0.362 0.867 0.466 -0.002 0.004  -0.010 457 ARG BBB N   
1963 C CA  . ARG B 128 ? 0.358 0.868 0.490 0.002  -0.003 -0.011 457 ARG BBB CA  
1964 C C   . ARG B 128 ? 0.366 0.886 0.529 -0.001 0.005  -0.019 457 ARG BBB C   
1965 O O   . ARG B 128 ? 0.353 0.874 0.513 -0.006 0.020  -0.026 457 ARG BBB O   
1966 C CB  . ARG B 128 ? 0.337 0.844 0.467 0.006  -0.005 -0.010 457 ARG BBB CB  
1967 C CG  . ARG B 128 ? 0.325 0.830 0.470 0.010  -0.020 -0.006 457 ARG BBB CG  
1968 C CD  . ARG B 128 ? 0.334 0.834 0.472 0.013  -0.022 -0.004 457 ARG BBB CD  
1969 N NE  . ARG B 128 ? 0.335 0.828 0.484 0.015  -0.039 0.001  457 ARG BBB NE  
1970 C CZ  . ARG B 128 ? 0.340 0.836 0.522 0.019  -0.044 -0.002 457 ARG BBB CZ  
1971 N NH1 . ARG B 128 ? 0.338 0.844 0.545 0.020  -0.030 -0.012 457 ARG BBB NH1 
1972 N NH2 . ARG B 128 ? 0.353 0.840 0.542 0.020  -0.062 0.004  457 ARG BBB NH2 
1973 N N   . LYS B 129 ? 0.408 0.934 0.601 0.002  -0.005 -0.020 458 LYS BBB N   
1974 C CA  . LYS B 129 ? 0.427 0.964 0.659 -0.000 0.002  -0.029 458 LYS BBB CA  
1975 C C   . LYS B 129 ? 0.419 0.961 0.677 0.002  0.011  -0.039 458 LYS BBB C   
1976 O O   . LYS B 129 ? 0.406 0.959 0.696 -0.002 0.023  -0.050 458 LYS BBB O   
1977 C CB  . LYS B 129 ? 0.446 0.986 0.703 0.003  -0.016 -0.026 458 LYS BBB CB  
1978 C CG  . LYS B 129 ? 0.495 1.029 0.727 -0.001 -0.025 -0.018 458 LYS BBB CG  
1979 C CD  . LYS B 129 ? 0.526 1.065 0.757 -0.008 -0.013 -0.023 458 LYS BBB CD  
1980 C CE  . LYS B 129 ? 0.556 1.088 0.765 -0.010 -0.023 -0.015 458 LYS BBB CE  
1981 N NZ  . LYS B 129 ? 0.577 1.116 0.802 -0.017 -0.018 -0.020 458 LYS BBB NZ  
1982 N N   . SER B 130 ? 0.420 0.956 0.667 0.006  0.008  -0.035 459 SER BBB N   
1983 C CA  . SER B 130 ? 0.411 0.951 0.680 0.008  0.018  -0.044 459 SER BBB CA  
1984 C C   . SER B 130 ? 0.387 0.916 0.625 0.011  0.016  -0.038 459 SER BBB C   
1985 O O   . SER B 130 ? 0.387 0.908 0.596 0.012  0.005  -0.028 459 SER BBB O   
1986 C CB  . SER B 130 ? 0.408 0.954 0.727 0.015  0.007  -0.048 459 SER BBB CB  
1987 O OG  . SER B 130 ? 0.415 0.952 0.728 0.021  -0.015 -0.036 459 SER BBB OG  
1988 N N   . ASN B 131 ? 0.360 0.889 0.606 0.010  0.028  -0.046 460 ASN BBB N   
1989 C CA  . ASN B 131 ? 0.356 0.876 0.576 0.011  0.028  -0.042 460 ASN BBB CA  
1990 C C   . ASN B 131 ? 0.343 0.858 0.574 0.019  0.009  -0.035 460 ASN BBB C   
1991 O O   . ASN B 131 ? 0.332 0.851 0.601 0.024  0.001  -0.038 460 ASN BBB O   
1992 C CB  . ASN B 131 ? 0.368 0.889 0.593 0.007  0.047  -0.054 460 ASN BBB CB  
1993 C CG  . ASN B 131 ? 0.400 0.920 0.602 -0.005 0.064  -0.060 460 ASN BBB CG  
1994 O OD1 . ASN B 131 ? 0.413 0.930 0.590 -0.008 0.060  -0.053 460 ASN BBB OD1 
1995 N ND2 . ASN B 131 ? 0.437 0.957 0.646 -0.012 0.083  -0.072 460 ASN BBB ND2 
1996 N N   . LEU B 132 ? 0.335 0.841 0.534 0.020  0.003  -0.027 461 LEU BBB N   
1997 C CA  . LEU B 132 ? 0.343 0.840 0.543 0.025  -0.013 -0.020 461 LEU BBB CA  
1998 C C   . LEU B 132 ? 0.348 0.845 0.578 0.028  -0.009 -0.028 461 LEU BBB C   
1999 O O   . LEU B 132 ? 0.385 0.886 0.615 0.025  0.009  -0.037 461 LEU BBB O   
2000 C CB  . LEU B 132 ? 0.355 0.842 0.514 0.023  -0.014 -0.013 461 LEU BBB CB  
2001 C CG  . LEU B 132 ? 0.343 0.828 0.475 0.020  -0.020 -0.006 461 LEU BBB CG  
2002 C CD1 . LEU B 132 ? 0.336 0.815 0.437 0.018  -0.018 -0.003 461 LEU BBB CD1 
2003 C CD2 . LEU B 132 ? 0.359 0.838 0.497 0.020  -0.037 0.001  461 LEU BBB CD2 
2004 N N   . LYS B 133 ? 0.356 0.846 0.609 0.033  -0.025 -0.024 462 LYS BBB N   
2005 C CA  . LYS B 133 ? 0.361 0.848 0.638 0.038  -0.026 -0.029 462 LYS BBB CA  
2006 C C   . LYS B 133 ? 0.355 0.830 0.593 0.035  -0.026 -0.023 462 LYS BBB C   
2007 O O   . LYS B 133 ? 0.345 0.815 0.547 0.032  -0.030 -0.015 462 LYS BBB O   
2008 C CB  . LYS B 133 ? 0.395 0.875 0.708 0.043  -0.049 -0.025 462 LYS BBB CB  
2009 C CG  . LYS B 133 ? 0.420 0.914 0.779 0.046  -0.049 -0.032 462 LYS BBB CG  
2010 C CD  . LYS B 133 ? 0.474 0.961 0.867 0.051  -0.076 -0.026 462 LYS BBB CD  
2011 C CE  . LYS B 133 ? 0.504 1.007 0.952 0.054  -0.075 -0.036 462 LYS BBB CE  
2012 N NZ  . LYS B 133 ? 0.543 1.038 1.028 0.059  -0.106 -0.029 462 LYS BBB NZ  
2013 N N   . PRO B 134 ? 0.342 0.812 0.588 0.037  -0.019 -0.029 463 PRO BBB N   
2014 C CA  . PRO B 134 ? 0.337 0.796 0.549 0.034  -0.019 -0.024 463 PRO BBB CA  
2015 C C   . PRO B 134 ? 0.337 0.783 0.525 0.033  -0.039 -0.011 463 PRO BBB C   
2016 O O   . PRO B 134 ? 0.328 0.766 0.535 0.036  -0.057 -0.006 463 PRO BBB O   
2017 C CB  . PRO B 134 ? 0.338 0.794 0.575 0.037  -0.014 -0.032 463 PRO BBB CB  
2018 C CG  . PRO B 134 ? 0.333 0.802 0.610 0.039  0.000  -0.046 463 PRO BBB CG  
2019 C CD  . PRO B 134 ? 0.329 0.805 0.620 0.040  -0.009 -0.042 463 PRO BBB CD  
2020 N N   . PHE B 135 ? 0.341 0.784 0.490 0.028  -0.036 -0.006 464 PHE BBB N   
2021 C CA  . PHE B 135 ? 0.354 0.782 0.472 0.023  -0.049 0.005  464 PHE BBB CA  
2022 C C   . PHE B 135 ? 0.380 0.806 0.496 0.021  -0.063 0.012  464 PHE BBB C   
2023 O O   . PHE B 135 ? 0.408 0.818 0.502 0.016  -0.076 0.020  464 PHE BBB O   
2024 C CB  . PHE B 135 ? 0.356 0.767 0.474 0.023  -0.060 0.008  464 PHE BBB CB  
2025 C CG  . PHE B 135 ? 0.356 0.767 0.468 0.022  -0.047 0.003  464 PHE BBB CG  
2026 C CD1 . PHE B 135 ? 0.340 0.756 0.422 0.017  -0.035 0.002  464 PHE BBB CD1 
2027 C CD2 . PHE B 135 ? 0.356 0.762 0.493 0.027  -0.048 -0.002 464 PHE BBB CD2 
2028 C CE1 . PHE B 135 ? 0.344 0.759 0.419 0.016  -0.025 -0.003 464 PHE BBB CE1 
2029 C CE2 . PHE B 135 ? 0.364 0.768 0.492 0.025  -0.036 -0.007 464 PHE BBB CE2 
2030 C CZ  . PHE B 135 ? 0.358 0.767 0.454 0.020  -0.025 -0.007 464 PHE BBB CZ  
2031 N N   . GLU B 136 ? 0.396 0.835 0.532 0.024  -0.059 0.008  465 GLU BBB N   
2032 C CA  . GLU B 136 ? 0.414 0.852 0.548 0.022  -0.070 0.013  465 GLU BBB CA  
2033 C C   . GLU B 136 ? 0.399 0.838 0.497 0.016  -0.063 0.015  465 GLU BBB C   
2034 O O   . GLU B 136 ? 0.403 0.850 0.490 0.016  -0.047 0.010  465 GLU BBB O   
2035 C CB  . GLU B 136 ? 0.415 0.867 0.585 0.027  -0.068 0.007  465 GLU BBB CB  
2036 C CG  . GLU B 136 ? 0.422 0.871 0.599 0.025  -0.084 0.014  465 GLU BBB CG  
2037 C CD  . GLU B 136 ? 0.442 0.907 0.656 0.029  -0.080 0.007  465 GLU BBB CD  
2038 O OE1 . GLU B 136 ? 0.412 0.888 0.659 0.033  -0.069 -0.003 465 GLU BBB OE1 
2039 O OE2 . GLU B 136 ? 0.474 0.940 0.685 0.026  -0.086 0.010  465 GLU BBB OE2 
2040 N N   . ARG B 137 ? 0.432 0.861 0.511 0.011  -0.074 0.022  466 ARG BBB N   
2041 C CA  . ARG B 137 ? 0.428 0.856 0.475 0.004  -0.068 0.023  466 ARG BBB CA  
2042 C C   . ARG B 137 ? 0.411 0.841 0.461 0.002  -0.075 0.025  466 ARG BBB C   
2043 O O   . ARG B 137 ? 0.408 0.826 0.462 0.000  -0.092 0.031  466 ARG BBB O   
2044 C CB  . ARG B 137 ? 0.455 0.865 0.469 -0.004 -0.073 0.028  466 ARG BBB CB  
2045 C CG  . ARG B 137 ? 0.492 0.902 0.479 -0.012 -0.063 0.025  466 ARG BBB CG  
2046 C CD  . ARG B 137 ? 0.542 0.935 0.499 -0.021 -0.064 0.027  466 ARG BBB CD  
2047 N NE  . ARG B 137 ? 0.576 0.967 0.508 -0.030 -0.054 0.023  466 ARG BBB NE  
2048 C CZ  . ARG B 137 ? 0.666 1.044 0.575 -0.041 -0.059 0.025  466 ARG BBB CZ  
2049 N NH1 . ARG B 137 ? 0.726 1.090 0.631 -0.045 -0.076 0.033  466 ARG BBB NH1 
2050 N NH2 . ARG B 137 ? 0.694 1.071 0.584 -0.049 -0.046 0.019  466 ARG BBB NH2 
2051 N N   . ASP B 138 ? 0.381 0.822 0.427 0.003  -0.063 0.021  467 ASP BBB N   
2052 C CA  . ASP B 138 ? 0.368 0.811 0.416 0.001  -0.068 0.023  467 ASP BBB CA  
2053 C C   . ASP B 138 ? 0.352 0.793 0.372 -0.005 -0.060 0.022  467 ASP BBB C   
2054 O O   . ASP B 138 ? 0.335 0.785 0.354 -0.002 -0.047 0.017  467 ASP BBB O   
2055 C CB  . ASP B 138 ? 0.352 0.811 0.429 0.007  -0.061 0.018  467 ASP BBB CB  
2056 C CG  . ASP B 138 ? 0.342 0.804 0.422 0.005  -0.064 0.018  467 ASP BBB CG  
2057 O OD1 . ASP B 138 ? 0.354 0.805 0.412 -0.001 -0.071 0.023  467 ASP BBB OD1 
2058 O OD2 . ASP B 138 ? 0.351 0.825 0.454 0.008  -0.059 0.014  467 ASP BBB OD2 
2059 N N   . ILE B 139 ? 0.366 0.792 0.363 -0.014 -0.068 0.025  468 ILE BBB N   
2060 C CA  . ILE B 139 ? 0.386 0.807 0.357 -0.021 -0.060 0.022  468 ILE BBB CA  
2061 C C   . ILE B 139 ? 0.400 0.819 0.369 -0.025 -0.065 0.024  468 ILE BBB C   
2062 O O   . ILE B 139 ? 0.431 0.842 0.377 -0.033 -0.060 0.021  468 ILE BBB O   
2063 C CB  . ILE B 139 ? 0.395 0.798 0.336 -0.032 -0.061 0.023  468 ILE BBB CB  
2064 C CG1 . ILE B 139 ? 0.425 0.808 0.351 -0.041 -0.080 0.032  468 ILE BBB CG1 
2065 C CG2 . ILE B 139 ? 0.385 0.792 0.329 -0.028 -0.055 0.021  468 ILE BBB CG2 
2066 C CD1 . ILE B 139 ? 0.449 0.810 0.337 -0.056 -0.080 0.032  468 ILE BBB CD1 
2067 N N   . SER B 140 ? 0.393 0.818 0.385 -0.020 -0.073 0.026  469 SER BBB N   
2068 C CA  . SER B 140 ? 0.390 0.815 0.383 -0.023 -0.078 0.027  469 SER BBB CA  
2069 C C   . SER B 140 ? 0.376 0.811 0.367 -0.020 -0.063 0.021  469 SER BBB C   
2070 O O   . SER B 140 ? 0.336 0.781 0.336 -0.014 -0.052 0.017  469 SER BBB O   
2071 C CB  . SER B 140 ? 0.392 0.824 0.417 -0.018 -0.088 0.029  469 SER BBB CB  
2072 O OG  . SER B 140 ? 0.396 0.846 0.447 -0.008 -0.077 0.024  469 SER BBB OG  
2073 N N   . THR B 141 ? 0.396 0.824 0.374 -0.027 -0.063 0.020  470 THR BBB N   
2074 C CA  . THR B 141 ? 0.404 0.838 0.378 -0.026 -0.051 0.015  470 THR BBB CA  
2075 C C   . THR B 141 ? 0.423 0.858 0.404 -0.027 -0.055 0.015  470 THR BBB C   
2076 O O   . THR B 141 ? 0.448 0.880 0.419 -0.030 -0.049 0.012  470 THR BBB O   
2077 C CB  . THR B 141 ? 0.426 0.848 0.375 -0.034 -0.044 0.010  470 THR BBB CB  
2078 O OG1 . THR B 141 ? 0.481 0.886 0.408 -0.046 -0.054 0.013  470 THR BBB OG1 
2079 C CG2 . THR B 141 ? 0.418 0.841 0.363 -0.033 -0.038 0.008  470 THR BBB CG2 
2080 N N   . GLU B 142 ? 0.435 0.875 0.435 -0.025 -0.066 0.020  471 GLU BBB N   
2081 C CA  . GLU B 142 ? 0.456 0.898 0.466 -0.027 -0.070 0.020  471 GLU BBB CA  
2082 C C   . GLU B 142 ? 0.400 0.855 0.424 -0.021 -0.057 0.016  471 GLU BBB C   
2083 O O   . GLU B 142 ? 0.359 0.822 0.393 -0.015 -0.050 0.014  471 GLU BBB O   
2084 C CB  . GLU B 142 ? 0.523 0.968 0.555 -0.027 -0.085 0.024  471 GLU BBB CB  
2085 C CG  . GLU B 142 ? 0.667 1.095 0.683 -0.035 -0.102 0.031  471 GLU BBB CG  
2086 C CD  . GLU B 142 ? 0.776 1.189 0.766 -0.047 -0.110 0.033  471 GLU BBB CD  
2087 O OE1 . GLU B 142 ? 0.768 1.180 0.743 -0.049 -0.098 0.028  471 GLU BBB OE1 
2088 O OE2 . GLU B 142 ? 0.906 1.306 0.891 -0.054 -0.129 0.040  471 GLU BBB OE2 
2089 N N   . ILE B 143 ? 0.368 0.822 0.389 -0.024 -0.055 0.014  472 ILE BBB N   
2090 C CA  . ILE B 143 ? 0.344 0.806 0.375 -0.020 -0.046 0.011  472 ILE BBB CA  
2091 C C   . ILE B 143 ? 0.340 0.814 0.396 -0.017 -0.045 0.011  472 ILE BBB C   
2092 O O   . ILE B 143 ? 0.327 0.805 0.400 -0.019 -0.054 0.012  472 ILE BBB O   
2093 C CB  . ILE B 143 ? 0.332 0.789 0.357 -0.026 -0.046 0.011  472 ILE BBB CB  
2094 C CG1 . ILE B 143 ? 0.338 0.782 0.339 -0.030 -0.044 0.009  472 ILE BBB CG1 
2095 C CG2 . ILE B 143 ? 0.333 0.795 0.365 -0.024 -0.038 0.008  472 ILE BBB CG2 
2096 C CD1 . ILE B 143 ? 0.332 0.770 0.327 -0.035 -0.045 0.008  472 ILE BBB CD1 
2097 N N   . TYR B 144 ? 0.334 0.813 0.393 -0.014 -0.035 0.008  473 TYR BBB N   
2098 C CA  . TYR B 144 ? 0.345 0.834 0.426 -0.013 -0.029 0.005  473 TYR BBB CA  
2099 C C   . TYR B 144 ? 0.353 0.845 0.442 -0.018 -0.026 0.002  473 TYR BBB C   
2100 O O   . TYR B 144 ? 0.364 0.850 0.436 -0.020 -0.020 0.002  473 TYR BBB O   
2101 C CB  . TYR B 144 ? 0.351 0.841 0.426 -0.010 -0.019 0.003  473 TYR BBB CB  
2102 C CG  . TYR B 144 ? 0.361 0.860 0.456 -0.011 -0.011 -0.002 473 TYR BBB CG  
2103 C CD1 . TYR B 144 ? 0.364 0.869 0.480 -0.008 -0.013 -0.004 473 TYR BBB CD1 
2104 C CD2 . TYR B 144 ? 0.368 0.866 0.458 -0.017 0.000  -0.006 473 TYR BBB CD2 
2105 C CE1 . TYR B 144 ? 0.357 0.871 0.495 -0.009 -0.003 -0.011 473 TYR BBB CE1 
2106 C CE2 . TYR B 144 ? 0.348 0.853 0.454 -0.020 0.011  -0.013 473 TYR BBB CE2 
2107 C CZ  . TYR B 144 ? 0.350 0.864 0.482 -0.016 0.010  -0.016 473 TYR BBB CZ  
2108 O OH  . TYR B 144 ? 0.361 0.882 0.512 -0.020 0.023  -0.025 473 TYR BBB OH  
2109 N N   . GLN B 145 ? 0.356 0.857 0.471 -0.019 -0.030 0.000  474 GLN BBB N   
2110 C CA  . GLN B 145 ? 0.356 0.862 0.485 -0.025 -0.026 -0.004 474 GLN BBB CA  
2111 C C   . GLN B 145 ? 0.365 0.880 0.509 -0.027 -0.011 -0.011 474 GLN BBB C   
2112 O O   . GLN B 145 ? 0.348 0.873 0.522 -0.025 -0.010 -0.016 474 GLN BBB O   
2113 C CB  . GLN B 145 ? 0.358 0.870 0.512 -0.026 -0.039 -0.003 474 GLN BBB CB  
2114 C CG  . GLN B 145 ? 0.364 0.883 0.535 -0.033 -0.036 -0.007 474 GLN BBB CG  
2115 C CD  . GLN B 145 ? 0.357 0.883 0.559 -0.033 -0.051 -0.007 474 GLN BBB CD  
2116 O OE1 . GLN B 145 ? 0.343 0.864 0.543 -0.031 -0.067 -0.001 474 GLN BBB OE1 
2117 N NE2 . GLN B 145 ? 0.356 0.895 0.590 -0.037 -0.046 -0.014 474 GLN BBB NE2 
2118 N N   . ALA B 146 ? 0.369 0.876 0.491 -0.032 0.000  -0.012 475 ALA BBB N   
2119 C CA  . ALA B 146 ? 0.394 0.903 0.517 -0.038 0.016  -0.019 475 ALA BBB CA  
2120 C C   . ALA B 146 ? 0.409 0.926 0.553 -0.047 0.025  -0.027 475 ALA BBB C   
2121 O O   . ALA B 146 ? 0.448 0.969 0.602 -0.053 0.040  -0.035 475 ALA BBB O   
2122 C CB  . ALA B 146 ? 0.415 0.908 0.501 -0.041 0.020  -0.014 475 ALA BBB CB  
2123 N N   . GLY B 147 ? 0.406 0.923 0.554 -0.049 0.018  -0.025 476 GLY BBB N   
2124 C CA  . GLY B 147 ? 0.396 0.921 0.565 -0.058 0.026  -0.032 476 GLY BBB CA  
2125 C C   . GLY B 147 ? 0.367 0.907 0.576 -0.054 0.014  -0.034 476 GLY BBB C   
2126 O O   . GLY B 147 ? 0.376 0.920 0.598 -0.045 0.002  -0.030 476 GLY BBB O   
2127 N N   . SER B 148 ? 0.356 0.903 0.584 -0.062 0.017  -0.040 477 SER BBB N   
2128 C CA  . SER B 148 ? 0.356 0.918 0.629 -0.060 0.006  -0.043 477 SER BBB CA  
2129 C C   . SER B 148 ? 0.345 0.899 0.603 -0.059 -0.014 -0.033 477 SER BBB C   
2130 O O   . SER B 148 ? 0.321 0.882 0.606 -0.055 -0.030 -0.031 477 SER BBB O   
2131 C CB  . SER B 148 ? 0.366 0.940 0.669 -0.071 0.021  -0.055 477 SER BBB CB  
2132 O OG  . SER B 148 ? 0.376 0.939 0.647 -0.082 0.031  -0.055 477 SER BBB OG  
2133 N N   . THR B 149 ? 0.353 0.891 0.568 -0.062 -0.012 -0.027 478 THR BBB N   
2134 C CA  . THR B 149 ? 0.357 0.883 0.550 -0.062 -0.027 -0.018 478 THR BBB CA  
2135 C C   . THR B 149 ? 0.340 0.859 0.517 -0.054 -0.039 -0.010 478 THR BBB C   
2136 O O   . THR B 149 ? 0.320 0.833 0.478 -0.049 -0.033 -0.009 478 THR BBB O   
2137 C CB  . THR B 149 ? 0.376 0.888 0.535 -0.069 -0.018 -0.017 478 THR BBB CB  
2138 O OG1 . THR B 149 ? 0.373 0.892 0.548 -0.079 -0.007 -0.024 478 THR BBB OG1 
2139 C CG2 . THR B 149 ? 0.397 0.896 0.531 -0.069 -0.030 -0.010 478 THR BBB CG2 
2140 N N   . PRO B 150 ? 0.335 0.851 0.517 -0.054 -0.058 -0.006 479 PRO BBB N   
2141 C CA  . PRO B 150 ? 0.343 0.847 0.503 -0.049 -0.069 0.002  479 PRO BBB CA  
2142 C C   . PRO B 150 ? 0.338 0.827 0.456 -0.050 -0.064 0.005  479 PRO BBB C   
2143 O O   . PRO B 150 ? 0.335 0.819 0.442 -0.056 -0.059 0.003  479 PRO BBB O   
2144 C CB  . PRO B 150 ? 0.345 0.847 0.515 -0.053 -0.091 0.006  479 PRO BBB CB  
2145 C CG  . PRO B 150 ? 0.343 0.862 0.556 -0.056 -0.091 0.000  479 PRO BBB CG  
2146 C CD  . PRO B 150 ? 0.336 0.860 0.546 -0.059 -0.070 -0.007 479 PRO BBB CD  
2147 N N   . CYS B 151 ? 0.352 0.832 0.450 -0.046 -0.064 0.008  480 CYS BBB N   
2148 C CA  . CYS B 151 ? 0.373 0.840 0.437 -0.046 -0.058 0.009  480 CYS BBB CA  
2149 C C   . CYS B 151 ? 0.392 0.845 0.435 -0.052 -0.068 0.011  480 CYS BBB C   
2150 O O   . CYS B 151 ? 0.396 0.839 0.419 -0.055 -0.062 0.010  480 CYS BBB O   
2151 C CB  . CYS B 151 ? 0.384 0.851 0.441 -0.039 -0.053 0.009  480 CYS BBB CB  
2152 S SG  . CYS B 151 ? 0.384 0.863 0.461 -0.034 -0.041 0.005  480 CYS BBB SG  
2153 N N   . ASN B 152 ? 0.404 0.855 0.451 -0.056 -0.083 0.015  481 ASN BBB N   
2154 C CA  . ASN B 152 ? 0.436 0.871 0.458 -0.065 -0.094 0.018  481 ASN BBB CA  
2155 C C   . ASN B 152 ? 0.414 0.835 0.404 -0.066 -0.084 0.015  481 ASN BBB C   
2156 O O   . ASN B 152 ? 0.405 0.813 0.374 -0.074 -0.081 0.013  481 ASN BBB O   
2157 C CB  . ASN B 152 ? 0.467 0.900 0.491 -0.073 -0.098 0.017  481 ASN BBB CB  
2158 C CG  . ASN B 152 ? 0.498 0.944 0.556 -0.074 -0.110 0.019  481 ASN BBB CG  
2159 O OD1 . ASN B 152 ? 0.543 0.991 0.617 -0.072 -0.123 0.022  481 ASN BBB OD1 
2160 N ND2 . ASN B 152 ? 0.516 0.968 0.587 -0.077 -0.106 0.016  481 ASN BBB ND2 
2161 N N   . GLY B 153 ? 0.406 0.829 0.394 -0.059 -0.077 0.015  482 GLY BBB N   
2162 C CA  . GLY B 153 ? 0.420 0.833 0.385 -0.060 -0.068 0.011  482 GLY BBB CA  
2163 C C   . GLY B 153 ? 0.417 0.829 0.379 -0.056 -0.054 0.006  482 GLY BBB C   
2164 O O   . GLY B 153 ? 0.427 0.831 0.374 -0.057 -0.046 0.001  482 GLY BBB O   
2165 N N   . VAL B 154 ? 0.411 0.832 0.390 -0.052 -0.051 0.006  483 VAL BBB N   
2166 C CA  . VAL B 154 ? 0.403 0.821 0.380 -0.048 -0.041 0.002  483 VAL BBB CA  
2167 C C   . VAL B 154 ? 0.388 0.817 0.380 -0.040 -0.036 0.003  483 VAL BBB C   
2168 O O   . VAL B 154 ? 0.405 0.843 0.411 -0.040 -0.038 0.006  483 VAL BBB O   
2169 C CB  . VAL B 154 ? 0.412 0.823 0.386 -0.054 -0.041 0.001  483 VAL BBB CB  
2170 C CG1 . VAL B 154 ? 0.404 0.809 0.376 -0.050 -0.033 -0.002 483 VAL BBB CG1 
2171 C CG2 . VAL B 154 ? 0.420 0.820 0.376 -0.064 -0.046 -0.001 483 VAL BBB CG2 
2172 N N   . GLU B 155 ? 0.384 0.809 0.372 -0.034 -0.030 0.002  484 GLU BBB N   
2173 C CA  . GLU B 155 ? 0.353 0.783 0.349 -0.029 -0.026 0.003  484 GLU BBB CA  
2174 C C   . GLU B 155 ? 0.343 0.767 0.337 -0.031 -0.025 0.004  484 GLU BBB C   
2175 O O   . GLU B 155 ? 0.341 0.755 0.328 -0.034 -0.025 0.002  484 GLU BBB O   
2176 C CB  . GLU B 155 ? 0.354 0.783 0.348 -0.023 -0.023 0.001  484 GLU BBB CB  
2177 C CG  . GLU B 155 ? 0.359 0.794 0.353 -0.022 -0.024 0.001  484 GLU BBB CG  
2178 C CD  . GLU B 155 ? 0.370 0.803 0.363 -0.016 -0.020 -0.002 484 GLU BBB CD  
2179 O OE1 . GLU B 155 ? 0.354 0.786 0.351 -0.012 -0.019 -0.002 484 GLU BBB OE1 
2180 O OE2 . GLU B 155 ? 0.376 0.809 0.364 -0.018 -0.019 -0.005 484 GLU BBB OE2 
2181 N N   . GLY B 156 ? 0.337 0.765 0.335 -0.032 -0.022 0.006  485 GLY BBB N   
2182 C CA  . GLY B 156 ? 0.345 0.765 0.338 -0.037 -0.020 0.007  485 GLY BBB CA  
2183 C C   . GLY B 156 ? 0.348 0.773 0.343 -0.040 -0.015 0.008  485 GLY BBB C   
2184 O O   . GLY B 156 ? 0.348 0.781 0.349 -0.036 -0.014 0.007  485 GLY BBB O   
2185 N N   . PHE B 157 ? 0.386 0.807 0.378 -0.049 -0.012 0.007  486 PHE BBB N   
2186 C CA  . PHE B 157 ? 0.393 0.818 0.387 -0.055 -0.003 0.006  486 PHE BBB CA  
2187 C C   . PHE B 157 ? 0.371 0.816 0.389 -0.052 -0.001 0.002  486 PHE BBB C   
2188 O O   . PHE B 157 ? 0.375 0.829 0.409 -0.051 -0.005 0.000  486 PHE BBB O   
2189 C CB  . PHE B 157 ? 0.409 0.829 0.400 -0.067 0.002  0.004  486 PHE BBB CB  
2190 C CG  . PHE B 157 ? 0.447 0.869 0.437 -0.077 0.013  -0.000 486 PHE BBB CG  
2191 C CD1 . PHE B 157 ? 0.460 0.867 0.427 -0.081 0.016  0.003  486 PHE BBB CD1 
2192 C CD2 . PHE B 157 ? 0.444 0.883 0.458 -0.082 0.022  -0.007 486 PHE BBB CD2 
2193 C CE1 . PHE B 157 ? 0.484 0.891 0.447 -0.093 0.028  -0.002 486 PHE BBB CE1 
2194 C CE2 . PHE B 157 ? 0.455 0.896 0.470 -0.093 0.035  -0.013 486 PHE BBB CE2 
2195 C CZ  . PHE B 157 ? 0.473 0.897 0.459 -0.099 0.040  -0.011 486 PHE BBB CZ  
2196 N N   . ASN B 158 ? 0.379 0.829 0.399 -0.051 0.004  0.000  487 ASN BBB N   
2197 C CA  . ASN B 158 ? 0.374 0.840 0.418 -0.048 0.007  -0.004 487 ASN BBB CA  
2198 C C   . ASN B 158 ? 0.365 0.837 0.418 -0.039 -0.003 -0.001 487 ASN BBB C   
2199 O O   . ASN B 158 ? 0.364 0.850 0.442 -0.037 -0.005 -0.004 487 ASN BBB O   
2200 C CB  . ASN B 158 ? 0.394 0.871 0.460 -0.056 0.015  -0.011 487 ASN BBB CB  
2201 C CG  . ASN B 158 ? 0.419 0.893 0.479 -0.066 0.030  -0.016 487 ASN BBB CG  
2202 O OD1 . ASN B 158 ? 0.416 0.886 0.463 -0.065 0.033  -0.015 487 ASN BBB OD1 
2203 N ND2 . ASN B 158 ? 0.449 0.927 0.519 -0.076 0.039  -0.022 487 ASN BBB ND2 
2204 N N   . CYS B 159 ? 0.374 0.837 0.412 -0.035 -0.010 0.003  488 CYS BBB N   
2205 C CA  . CYS B 159 ? 0.365 0.829 0.404 -0.030 -0.018 0.004  488 CYS BBB CA  
2206 C C   . CYS B 159 ? 0.363 0.820 0.387 -0.024 -0.019 0.006  488 CYS BBB C   
2207 O O   . CYS B 159 ? 0.385 0.832 0.397 -0.024 -0.020 0.006  488 CYS BBB O   
2208 C CB  . CYS B 159 ? 0.376 0.837 0.413 -0.034 -0.024 0.005  488 CYS BBB CB  
2209 S SG  . CYS B 159 ? 0.372 0.844 0.434 -0.039 -0.028 0.003  488 CYS BBB SG  
2210 N N   . TYR B 160 ? 0.347 0.809 0.374 -0.020 -0.017 0.006  489 TYR BBB N   
2211 C CA  . TYR B 160 ? 0.330 0.787 0.347 -0.015 -0.017 0.007  489 TYR BBB CA  
2212 C C   . TYR B 160 ? 0.325 0.786 0.345 -0.012 -0.020 0.006  489 TYR BBB C   
2213 O O   . TYR B 160 ? 0.309 0.776 0.338 -0.012 -0.022 0.007  489 TYR BBB O   
2214 C CB  . TYR B 160 ? 0.316 0.774 0.332 -0.016 -0.012 0.007  489 TYR BBB CB  
2215 C CG  . TYR B 160 ? 0.316 0.767 0.325 -0.023 -0.008 0.007  489 TYR BBB CG  
2216 C CD1 . TYR B 160 ? 0.314 0.753 0.312 -0.024 -0.012 0.009  489 TYR BBB CD1 
2217 C CD2 . TYR B 160 ? 0.322 0.778 0.338 -0.029 -0.001 0.004  489 TYR BBB CD2 
2218 C CE1 . TYR B 160 ? 0.336 0.765 0.323 -0.032 -0.009 0.010  489 TYR BBB CE1 
2219 C CE2 . TYR B 160 ? 0.332 0.780 0.338 -0.038 0.004  0.004  489 TYR BBB CE2 
2220 C CZ  . TYR B 160 ? 0.349 0.783 0.339 -0.040 -0.001 0.008  489 TYR BBB CZ  
2221 O OH  . TYR B 160 ? 0.368 0.790 0.345 -0.050 0.003  0.008  489 TYR BBB OH  
2222 N N   . PHE B 161 ? 0.326 0.783 0.338 -0.009 -0.020 0.005  490 PHE BBB N   
2223 C CA  . PHE B 161 ? 0.327 0.785 0.337 -0.007 -0.020 0.004  490 PHE BBB CA  
2224 C C   . PHE B 161 ? 0.318 0.782 0.333 -0.004 -0.019 0.005  490 PHE BBB C   
2225 O O   . PHE B 161 ? 0.299 0.763 0.314 -0.002 -0.016 0.005  490 PHE BBB O   
2226 C CB  . PHE B 161 ? 0.338 0.790 0.341 -0.006 -0.018 0.000  490 PHE BBB CB  
2227 C CG  . PHE B 161 ? 0.345 0.795 0.342 -0.008 -0.017 -0.002 490 PHE BBB CG  
2228 C CD1 . PHE B 161 ? 0.358 0.803 0.345 -0.015 -0.021 -0.002 490 PHE BBB CD1 
2229 C CD2 . PHE B 161 ? 0.340 0.793 0.338 -0.006 -0.014 -0.005 490 PHE BBB CD2 
2230 C CE1 . PHE B 161 ? 0.374 0.814 0.349 -0.020 -0.020 -0.003 490 PHE BBB CE1 
2231 C CE2 . PHE B 161 ? 0.346 0.796 0.335 -0.010 -0.012 -0.007 490 PHE BBB CE2 
2232 C CZ  . PHE B 161 ? 0.377 0.819 0.353 -0.018 -0.015 -0.007 490 PHE BBB CZ  
2233 N N   . PRO B 162 ? 0.319 0.787 0.339 -0.004 -0.021 0.006  491 PRO BBB N   
2234 C CA  . PRO B 162 ? 0.317 0.791 0.344 -0.001 -0.019 0.006  491 PRO BBB CA  
2235 C C   . PRO B 162 ? 0.331 0.804 0.351 0.002  -0.016 0.005  491 PRO BBB C   
2236 O O   . PRO B 162 ? 0.366 0.843 0.391 0.003  -0.013 0.005  491 PRO BBB O   
2237 C CB  . PRO B 162 ? 0.307 0.783 0.342 -0.002 -0.025 0.008  491 PRO BBB CB  
2238 C CG  . PRO B 162 ? 0.316 0.783 0.337 -0.005 -0.030 0.009  491 PRO BBB CG  
2239 C CD  . PRO B 162 ? 0.320 0.784 0.336 -0.007 -0.027 0.007  491 PRO BBB CD  
2240 N N   . LEU B 163 ? 0.347 0.817 0.360 0.002  -0.016 0.003  492 LEU BBB N   
2241 C CA  . LEU B 163 ? 0.360 0.829 0.370 0.004  -0.013 0.001  492 LEU BBB CA  
2242 C C   . LEU B 163 ? 0.357 0.825 0.370 0.006  -0.012 -0.000 492 LEU BBB C   
2243 O O   . LEU B 163 ? 0.362 0.826 0.375 0.006  -0.014 -0.000 492 LEU BBB O   
2244 C CB  . LEU B 163 ? 0.366 0.832 0.369 0.001  -0.012 -0.002 492 LEU BBB CB  
2245 C CG  . LEU B 163 ? 0.389 0.852 0.387 -0.003 -0.017 0.001  492 LEU BBB CG  
2246 C CD1 . LEU B 163 ? 0.409 0.865 0.394 -0.009 -0.015 -0.001 492 LEU BBB CD1 
2247 C CD2 . LEU B 163 ? 0.384 0.853 0.391 0.001  -0.017 0.003  492 LEU BBB CD2 
2248 N N   . GLN B 164 ? 0.353 0.824 0.369 0.009  -0.012 -0.001 493 GLN BBB N   
2249 C CA  . GLN B 164 ? 0.366 0.833 0.386 0.011  -0.015 -0.002 493 GLN BBB CA  
2250 C C   . GLN B 164 ? 0.335 0.806 0.362 0.014  -0.014 -0.006 493 GLN BBB C   
2251 O O   . GLN B 164 ? 0.310 0.785 0.334 0.013  -0.012 -0.005 493 GLN BBB O   
2252 C CB  . GLN B 164 ? 0.390 0.853 0.403 0.010  -0.018 0.003  493 GLN BBB CB  
2253 C CG  . GLN B 164 ? 0.426 0.883 0.440 0.011  -0.025 0.005  493 GLN BBB CG  
2254 C CD  . GLN B 164 ? 0.465 0.913 0.481 0.011  -0.031 0.007  493 GLN BBB CD  
2255 O OE1 . GLN B 164 ? 0.409 0.853 0.418 0.008  -0.029 0.008  493 GLN BBB OE1 
2256 N NE2 . GLN B 164 ? 0.560 1.004 0.587 0.015  -0.038 0.006  493 GLN BBB NE2 
2257 N N   . SER B 165 ? 0.328 0.799 0.368 0.016  -0.016 -0.010 494 SER BBB N   
2258 C CA  . SER B 165 ? 0.322 0.798 0.375 0.018  -0.016 -0.015 494 SER BBB CA  
2259 C C   . SER B 165 ? 0.316 0.791 0.369 0.020  -0.024 -0.010 494 SER BBB C   
2260 O O   . SER B 165 ? 0.346 0.813 0.394 0.020  -0.032 -0.004 494 SER BBB O   
2261 C CB  . SER B 165 ? 0.309 0.786 0.383 0.021  -0.015 -0.023 494 SER BBB CB  
2262 O OG  . SER B 165 ? 0.318 0.794 0.389 0.017  -0.005 -0.030 494 SER BBB OG  
2263 N N   . TYR B 166 ? 0.320 0.800 0.375 0.019  -0.023 -0.011 495 TYR BBB N   
2264 C CA  . TYR B 166 ? 0.329 0.809 0.392 0.021  -0.032 -0.009 495 TYR BBB CA  
2265 C C   . TYR B 166 ? 0.338 0.819 0.427 0.025  -0.038 -0.015 495 TYR BBB C   
2266 O O   . TYR B 166 ? 0.330 0.817 0.433 0.026  -0.030 -0.023 495 TYR BBB O   
2267 C CB  . TYR B 166 ? 0.332 0.819 0.394 0.019  -0.029 -0.011 495 TYR BBB CB  
2268 C CG  . TYR B 166 ? 0.342 0.827 0.383 0.015  -0.024 -0.007 495 TYR BBB CG  
2269 C CD1 . TYR B 166 ? 0.344 0.822 0.371 0.012  -0.029 -0.001 495 TYR BBB CD1 
2270 C CD2 . TYR B 166 ? 0.344 0.833 0.379 0.014  -0.015 -0.010 495 TYR BBB CD2 
2271 C CE1 . TYR B 166 ? 0.352 0.829 0.364 0.009  -0.023 0.001  495 TYR BBB CE1 
2272 C CE2 . TYR B 166 ? 0.343 0.830 0.366 0.012  -0.012 -0.006 495 TYR BBB CE2 
2273 C CZ  . TYR B 166 ? 0.346 0.829 0.360 0.010  -0.014 -0.002 495 TYR BBB CZ  
2274 O OH  . TYR B 166 ? 0.371 0.853 0.376 0.007  -0.009 -0.001 495 TYR BBB OH  
2275 N N   . GLY B 167 ? 0.358 0.832 0.454 0.027  -0.053 -0.010 496 GLY BBB N   
2276 C CA  . GLY B 167 ? 0.356 0.831 0.483 0.032  -0.062 -0.015 496 GLY BBB CA  
2277 C C   . GLY B 167 ? 0.353 0.835 0.497 0.033  -0.069 -0.017 496 GLY BBB C   
2278 O O   . GLY B 167 ? 0.361 0.833 0.504 0.032  -0.087 -0.009 496 GLY BBB O   
2279 N N   . PHE B 168 ? 0.350 0.846 0.506 0.033  -0.057 -0.026 497 PHE BBB N   
2280 C CA  . PHE B 168 ? 0.352 0.856 0.524 0.032  -0.061 -0.029 497 PHE BBB CA  
2281 C C   . PHE B 168 ? 0.382 0.891 0.599 0.038  -0.070 -0.038 497 PHE BBB C   
2282 O O   . PHE B 168 ? 0.392 0.912 0.634 0.040  -0.057 -0.051 497 PHE BBB O   
2283 C CB  . PHE B 168 ? 0.336 0.850 0.500 0.028  -0.044 -0.036 497 PHE BBB CB  
2284 C CG  . PHE B 168 ? 0.334 0.842 0.460 0.023  -0.039 -0.028 497 PHE BBB CG  
2285 C CD1 . PHE B 168 ? 0.357 0.856 0.464 0.021  -0.049 -0.018 497 PHE BBB CD1 
2286 C CD2 . PHE B 168 ? 0.310 0.820 0.421 0.020  -0.024 -0.031 497 PHE BBB CD2 
2287 C CE1 . PHE B 168 ? 0.354 0.849 0.431 0.017  -0.043 -0.013 497 PHE BBB CE1 
2288 C CE2 . PHE B 168 ? 0.326 0.832 0.410 0.017  -0.020 -0.024 497 PHE BBB CE2 
2289 C CZ  . PHE B 168 ? 0.347 0.846 0.416 0.016  -0.029 -0.016 497 PHE BBB CZ  
2290 N N   . GLN B 169 ? 0.411 0.913 0.639 0.040  -0.092 -0.030 498 GLN BBB N   
2291 C CA  . GLN B 169 ? 0.439 0.945 0.715 0.047  -0.107 -0.037 498 GLN BBB CA  
2292 C C   . GLN B 169 ? 0.429 0.939 0.712 0.044  -0.119 -0.034 498 GLN BBB C   
2293 O O   . GLN B 169 ? 0.437 0.937 0.683 0.038  -0.124 -0.023 498 GLN BBB O   
2294 C CB  . GLN B 169 ? 0.478 0.967 0.761 0.051  -0.127 -0.029 498 GLN BBB CB  
2295 C CG  . GLN B 169 ? 0.510 0.994 0.778 0.051  -0.115 -0.030 498 GLN BBB CG  
2296 C CD  . GLN B 169 ? 0.561 1.031 0.848 0.057  -0.131 -0.027 498 GLN BBB CD  
2297 O OE1 . GLN B 169 ? 0.628 1.087 0.930 0.059  -0.156 -0.020 498 GLN BBB OE1 
2298 N NE2 . GLN B 169 ? 0.569 1.038 0.854 0.058  -0.118 -0.032 498 GLN BBB NE2 
2299 N N   . PRO B 170 ? 0.409 0.933 0.742 0.048  -0.123 -0.045 499 PRO BBB N   
2300 C CA  . PRO B 170 ? 0.411 0.939 0.753 0.046  -0.135 -0.043 499 PRO BBB CA  
2301 C C   . PRO B 170 ? 0.419 0.927 0.739 0.042  -0.165 -0.026 499 PRO BBB C   
2302 O O   . PRO B 170 ? 0.399 0.904 0.696 0.036  -0.169 -0.020 499 PRO BBB O   
2303 C CB  . PRO B 170 ? 0.395 0.941 0.805 0.052  -0.138 -0.059 499 PRO BBB CB  
2304 C CG  . PRO B 170 ? 0.388 0.942 0.816 0.056  -0.116 -0.073 499 PRO BBB CG  
2305 C CD  . PRO B 170 ? 0.395 0.931 0.779 0.055  -0.116 -0.061 499 PRO BBB CD  
2306 N N   . THR B 171 ? 0.450 0.941 0.774 0.046  -0.183 -0.018 500 THR BBB N   
2307 C CA  . THR B 171 ? 0.499 0.965 0.804 0.042  -0.215 -0.002 500 THR BBB CA  
2308 C C   . THR B 171 ? 0.516 0.961 0.753 0.031  -0.211 0.012  500 THR BBB C   
2309 O O   . THR B 171 ? 0.558 0.979 0.769 0.024  -0.235 0.026  500 THR BBB O   
2310 C CB  . THR B 171 ? 0.537 0.993 0.877 0.050  -0.235 -0.000 500 THR BBB CB  
2311 O OG1 . THR B 171 ? 0.568 1.043 0.975 0.059  -0.240 -0.015 500 THR BBB OG1 
2312 C CG2 . THR B 171 ? 0.598 1.022 0.914 0.044  -0.270 0.018  500 THR BBB CG2 
2313 N N   . ASN B 172 ? 0.482 0.936 0.692 0.029  -0.183 0.008  501 ASN BBB N   
2314 C CA  . ASN B 172 ? 0.471 0.910 0.623 0.019  -0.175 0.018  501 ASN BBB CA  
2315 C C   . ASN B 172 ? 0.463 0.892 0.587 0.009  -0.186 0.025  501 ASN BBB C   
2316 O O   . ASN B 172 ? 0.412 0.854 0.559 0.010  -0.188 0.020  501 ASN BBB O   
2317 C CB  . ASN B 172 ? 0.441 0.895 0.580 0.020  -0.145 0.010  501 ASN BBB CB  
2318 C CG  . ASN B 172 ? 0.449 0.904 0.593 0.025  -0.134 0.007  501 ASN BBB CG  
2319 O OD1 . ASN B 172 ? 0.473 0.919 0.633 0.029  -0.147 0.009  501 ASN BBB OD1 
2320 N ND2 . ASN B 172 ? 0.433 0.898 0.564 0.025  -0.111 0.001  501 ASN BBB ND2 
2321 N N   . GLY B 173 ? 0.478 0.884 0.554 -0.003 -0.191 0.036  502 GLY BBB N   
2322 C CA  . GLY B 173 ? 0.497 0.893 0.536 -0.016 -0.191 0.041  502 GLY BBB CA  
2323 C C   . GLY B 173 ? 0.476 0.892 0.510 -0.015 -0.164 0.032  502 GLY BBB C   
2324 O O   . GLY B 173 ? 0.462 0.891 0.505 -0.008 -0.144 0.026  502 GLY BBB O   
2325 N N   . VAL B 174 ? 0.484 0.900 0.505 -0.022 -0.164 0.032  503 VAL BBB N   
2326 C CA  . VAL B 174 ? 0.471 0.903 0.490 -0.021 -0.141 0.024  503 VAL BBB CA  
2327 C C   . VAL B 174 ? 0.475 0.907 0.471 -0.022 -0.119 0.022  503 VAL BBB C   
2328 O O   . VAL B 174 ? 0.460 0.910 0.470 -0.015 -0.100 0.014  503 VAL BBB O   
2329 C CB  . VAL B 174 ? 0.508 0.934 0.508 -0.031 -0.146 0.026  503 VAL BBB CB  
2330 C CG1 . VAL B 174 ? 0.497 0.938 0.495 -0.030 -0.124 0.017  503 VAL BBB CG1 
2331 C CG2 . VAL B 174 ? 0.538 0.966 0.567 -0.030 -0.170 0.027  503 VAL BBB CG2 
2332 N N   . GLY B 175 ? 0.474 0.886 0.435 -0.031 -0.120 0.029  504 GLY BBB N   
2333 C CA  . GLY B 175 ? 0.472 0.884 0.414 -0.033 -0.100 0.027  504 GLY BBB CA  
2334 C C   . GLY B 175 ? 0.451 0.877 0.419 -0.021 -0.091 0.022  504 GLY BBB C   
2335 O O   . GLY B 175 ? 0.403 0.838 0.367 -0.019 -0.073 0.018  504 GLY BBB O   
2336 N N   . TYR B 176 ? 0.444 0.873 0.437 -0.013 -0.104 0.023  505 TYR BBB N   
2337 C CA  . TYR B 176 ? 0.422 0.861 0.438 -0.003 -0.097 0.019  505 TYR BBB CA  
2338 C C   . TYR B 176 ? 0.385 0.845 0.438 0.006  -0.093 0.010  505 TYR BBB C   
2339 O O   . TYR B 176 ? 0.372 0.840 0.446 0.012  -0.087 0.004  505 TYR BBB O   
2340 C CB  . TYR B 176 ? 0.456 0.881 0.473 -0.003 -0.113 0.025  505 TYR BBB CB  
2341 C CG  . TYR B 176 ? 0.508 0.915 0.489 -0.012 -0.111 0.032  505 TYR BBB CG  
2342 C CD1 . TYR B 176 ? 0.553 0.939 0.502 -0.025 -0.122 0.039  505 TYR BBB CD1 
2343 C CD2 . TYR B 176 ? 0.530 0.940 0.508 -0.010 -0.097 0.029  505 TYR BBB CD2 
2344 C CE1 . TYR B 176 ? 0.575 0.943 0.489 -0.036 -0.117 0.044  505 TYR BBB CE1 
2345 C CE2 . TYR B 176 ? 0.574 0.969 0.522 -0.020 -0.093 0.034  505 TYR BBB CE2 
2346 C CZ  . TYR B 176 ? 0.585 0.959 0.501 -0.033 -0.102 0.040  505 TYR BBB CZ  
2347 O OH  . TYR B 176 ? 0.641 0.999 0.526 -0.045 -0.096 0.043  505 TYR BBB OH  
2348 N N   . GLN B 177 ? 0.370 0.837 0.430 0.004  -0.094 0.007  506 GLN BBB N   
2349 C CA  . GLN B 177 ? 0.353 0.839 0.445 0.010  -0.086 -0.003 506 GLN BBB CA  
2350 C C   . GLN B 177 ? 0.340 0.833 0.418 0.009  -0.065 -0.008 506 GLN BBB C   
2351 O O   . GLN B 177 ? 0.317 0.803 0.368 0.004  -0.059 -0.004 506 GLN BBB O   
2352 C CB  . GLN B 177 ? 0.354 0.843 0.459 0.007  -0.097 -0.004 506 GLN BBB CB  
2353 C CG  . GLN B 177 ? 0.366 0.852 0.500 0.011  -0.120 -0.003 506 GLN BBB CG  
2354 C CD  . GLN B 177 ? 0.357 0.846 0.505 0.008  -0.134 -0.003 506 GLN BBB CD  
2355 O OE1 . GLN B 177 ? 0.340 0.840 0.489 0.005  -0.123 -0.008 506 GLN BBB OE1 
2356 N NE2 . GLN B 177 ? 0.373 0.852 0.534 0.008  -0.159 0.003  506 GLN BBB NE2 
2357 N N   . PRO B 178 ? 0.325 0.832 0.424 0.012  -0.054 -0.018 507 PRO BBB N   
2358 C CA  . PRO B 178 ? 0.310 0.820 0.395 0.011  -0.037 -0.021 507 PRO BBB CA  
2359 C C   . PRO B 178 ? 0.288 0.800 0.363 0.006  -0.033 -0.021 507 PRO BBB C   
2360 O O   . PRO B 178 ? 0.279 0.797 0.370 0.005  -0.039 -0.024 507 PRO BBB O   
2361 C CB  . PRO B 178 ? 0.325 0.845 0.433 0.013  -0.028 -0.031 507 PRO BBB CB  
2362 C CG  . PRO B 178 ? 0.328 0.855 0.470 0.016  -0.037 -0.036 507 PRO BBB CG  
2363 C CD  . PRO B 178 ? 0.328 0.845 0.465 0.017  -0.057 -0.026 507 PRO BBB CD  
2364 N N   . TYR B 179 ? 0.280 0.787 0.332 0.003  -0.024 -0.019 508 TYR BBB N   
2365 C CA  . TYR B 179 ? 0.289 0.796 0.330 -0.001 -0.018 -0.020 508 TYR BBB CA  
2366 C C   . TYR B 179 ? 0.286 0.794 0.321 -0.002 -0.006 -0.023 508 TYR BBB C   
2367 O O   . TYR B 179 ? 0.299 0.802 0.325 -0.000 -0.003 -0.020 508 TYR BBB O   
2368 C CB  . TYR B 179 ? 0.288 0.785 0.308 -0.005 -0.021 -0.014 508 TYR BBB CB  
2369 C CG  . TYR B 179 ? 0.286 0.780 0.305 -0.008 -0.033 -0.012 508 TYR BBB CG  
2370 C CD1 . TYR B 179 ? 0.301 0.792 0.329 -0.007 -0.047 -0.008 508 TYR BBB CD1 
2371 C CD2 . TYR B 179 ? 0.299 0.792 0.311 -0.014 -0.033 -0.013 508 TYR BBB CD2 
2372 C CE1 . TYR B 179 ? 0.315 0.800 0.341 -0.011 -0.062 -0.005 508 TYR BBB CE1 
2373 C CE2 . TYR B 179 ? 0.313 0.800 0.322 -0.019 -0.046 -0.010 508 TYR BBB CE2 
2374 C CZ  . TYR B 179 ? 0.328 0.812 0.345 -0.018 -0.062 -0.005 508 TYR BBB CZ  
2375 O OH  . TYR B 179 ? 0.370 0.847 0.384 -0.023 -0.078 -0.001 508 TYR BBB OH  
2376 N N   . ARG B 180 ? 0.278 0.791 0.319 -0.005 -0.000 -0.029 509 ARG BBB N   
2377 C CA  . ARG B 180 ? 0.277 0.785 0.305 -0.009 0.009  -0.031 509 ARG BBB CA  
2378 C C   . ARG B 180 ? 0.283 0.784 0.294 -0.011 0.010  -0.026 509 ARG BBB C   
2379 O O   . ARG B 180 ? 0.327 0.828 0.338 -0.012 0.007  -0.026 509 ARG BBB O   
2380 C CB  . ARG B 180 ? 0.270 0.785 0.308 -0.014 0.017  -0.039 509 ARG BBB CB  
2381 C CG  . ARG B 180 ? 0.269 0.790 0.323 -0.014 0.020  -0.046 509 ARG BBB CG  
2382 C CD  . ARG B 180 ? 0.259 0.787 0.326 -0.021 0.031  -0.058 509 ARG BBB CD  
2383 N NE  . ARG B 180 ? 0.252 0.783 0.334 -0.021 0.036  -0.066 509 ARG BBB NE  
2384 C CZ  . ARG B 180 ? 0.260 0.793 0.346 -0.029 0.050  -0.077 509 ARG BBB CZ  
2385 N NH1 . ARG B 180 ? 0.268 0.799 0.343 -0.040 0.059  -0.082 509 ARG BBB NH1 
2386 N NH2 . ARG B 180 ? 0.255 0.791 0.356 -0.029 0.055  -0.085 509 ARG BBB NH2 
2387 N N   . VAL B 181 ? 0.277 0.770 0.277 -0.010 0.012  -0.023 510 VAL BBB N   
2388 C CA  . VAL B 181 ? 0.280 0.764 0.269 -0.011 0.013  -0.019 510 VAL BBB CA  
2389 C C   . VAL B 181 ? 0.298 0.773 0.278 -0.014 0.015  -0.019 510 VAL BBB C   
2390 O O   . VAL B 181 ? 0.294 0.767 0.271 -0.016 0.016  -0.019 510 VAL BBB O   
2391 C CB  . VAL B 181 ? 0.275 0.756 0.264 -0.006 0.011  -0.015 510 VAL BBB CB  
2392 C CG1 . VAL B 181 ? 0.288 0.762 0.273 -0.006 0.013  -0.014 510 VAL BBB CG1 
2393 C CG2 . VAL B 181 ? 0.269 0.755 0.262 -0.005 0.007  -0.015 510 VAL BBB CG2 
2394 N N   . VAL B 182 ? 0.294 0.764 0.267 -0.017 0.017  -0.019 511 VAL BBB N   
2395 C CA  . VAL B 182 ? 0.315 0.771 0.277 -0.021 0.017  -0.017 511 VAL BBB CA  
2396 C C   . VAL B 182 ? 0.329 0.777 0.292 -0.018 0.015  -0.015 511 VAL BBB C   
2397 O O   . VAL B 182 ? 0.333 0.784 0.297 -0.018 0.018  -0.017 511 VAL BBB O   
2398 C CB  . VAL B 182 ? 0.344 0.798 0.298 -0.030 0.021  -0.021 511 VAL BBB CB  
2399 C CG1 . VAL B 182 ? 0.376 0.811 0.312 -0.035 0.019  -0.017 511 VAL BBB CG1 
2400 C CG2 . VAL B 182 ? 0.351 0.813 0.308 -0.033 0.025  -0.026 511 VAL BBB CG2 
2401 N N   . VAL B 183 ? 0.338 0.779 0.305 -0.014 0.010  -0.011 512 VAL BBB N   
2402 C CA  . VAL B 183 ? 0.346 0.779 0.320 -0.011 0.009  -0.010 512 VAL BBB CA  
2403 C C   . VAL B 183 ? 0.361 0.778 0.327 -0.014 0.003  -0.007 512 VAL BBB C   
2404 O O   . VAL B 183 ? 0.360 0.768 0.320 -0.016 -0.004 -0.002 512 VAL BBB O   
2405 C CB  . VAL B 183 ? 0.344 0.780 0.334 -0.004 0.006  -0.009 512 VAL BBB CB  
2406 C CG1 . VAL B 183 ? 0.356 0.787 0.361 -0.001 0.007  -0.011 512 VAL BBB CG1 
2407 C CG2 . VAL B 183 ? 0.329 0.779 0.323 -0.002 0.011  -0.011 512 VAL BBB CG2 
2408 N N   . LEU B 184 ? 0.360 0.771 0.323 -0.017 0.006  -0.009 513 LEU BBB N   
2409 C CA  . LEU B 184 ? 0.394 0.786 0.348 -0.021 0.000  -0.006 513 LEU BBB CA  
2410 C C   . LEU B 184 ? 0.399 0.783 0.373 -0.014 -0.004 -0.006 513 LEU BBB C   
2411 O O   . LEU B 184 ? 0.386 0.776 0.373 -0.010 0.004  -0.012 513 LEU BBB O   
2412 C CB  . LEU B 184 ? 0.410 0.800 0.352 -0.027 0.007  -0.010 513 LEU BBB CB  
2413 C CG  . LEU B 184 ? 0.398 0.797 0.327 -0.035 0.012  -0.012 513 LEU BBB CG  
2414 C CD1 . LEU B 184 ? 0.406 0.802 0.325 -0.042 0.017  -0.016 513 LEU BBB CD1 
2415 C CD2 . LEU B 184 ? 0.403 0.790 0.316 -0.042 0.007  -0.008 513 LEU BBB CD2 
2416 N N   . SER B 185 ? 0.411 0.781 0.389 -0.012 -0.017 0.000  514 SER BBB N   
2417 C CA  . SER B 185 ? 0.417 0.776 0.418 -0.006 -0.025 0.001  514 SER BBB CA  
2418 C C   . SER B 185 ? 0.436 0.771 0.423 -0.011 -0.035 0.006  514 SER BBB C   
2419 O O   . SER B 185 ? 0.464 0.787 0.424 -0.021 -0.041 0.012  514 SER BBB O   
2420 C CB  . SER B 185 ? 0.417 0.776 0.435 -0.000 -0.036 0.005  514 SER BBB CB  
2421 O OG  . SER B 185 ? 0.411 0.791 0.439 0.003  -0.027 0.001  514 SER BBB OG  
2422 N N   . PHE B 186 ? 0.447 0.774 0.452 -0.007 -0.035 0.003  515 PHE BBB N   
2423 C CA  . PHE B 186 ? 0.485 0.786 0.478 -0.012 -0.045 0.007  515 PHE BBB CA  
2424 C C   . PHE B 186 ? 0.519 0.805 0.542 -0.005 -0.062 0.011  515 PHE BBB C   
2425 O O   . PHE B 186 ? 0.538 0.833 0.597 0.005  -0.057 0.003  515 PHE BBB O   
2426 C CB  . PHE B 186 ? 0.483 0.786 0.473 -0.014 -0.031 -0.001 515 PHE BBB CB  
2427 C CG  . PHE B 186 ? 0.474 0.793 0.440 -0.022 -0.017 -0.004 515 PHE BBB CG  
2428 C CD1 . PHE B 186 ? 0.455 0.798 0.430 -0.018 -0.005 -0.011 515 PHE BBB CD1 
2429 C CD2 . PHE B 186 ? 0.494 0.803 0.429 -0.033 -0.018 -0.001 515 PHE BBB CD2 
2430 C CE1 . PHE B 186 ? 0.462 0.818 0.420 -0.024 0.005  -0.014 515 PHE BBB CE1 
2431 C CE2 . PHE B 186 ? 0.496 0.821 0.417 -0.039 -0.006 -0.005 515 PHE BBB CE2 
2432 C CZ  . PHE B 186 ? 0.488 0.836 0.421 -0.034 0.004  -0.011 515 PHE BBB CZ  
2433 N N   . GLU B 187 ? 0.542 0.804 0.549 -0.010 -0.083 0.022  516 GLU BBB N   
2434 C CA  . GLU B 187 ? 0.569 0.812 0.601 -0.004 -0.105 0.029  516 GLU BBB CA  
2435 C C   . GLU B 187 ? 0.604 0.817 0.630 -0.008 -0.118 0.033  516 GLU BBB C   
2436 O O   . GLU B 187 ? 0.623 0.819 0.606 -0.021 -0.119 0.039  516 GLU BBB O   
2437 C CB  . GLU B 187 ? 0.589 0.823 0.604 -0.009 -0.123 0.040  516 GLU BBB CB  
2438 C CG  . GLU B 187 ? 0.621 0.842 0.670 -0.002 -0.147 0.046  516 GLU BBB CG  
2439 C CD  . GLU B 187 ? 0.659 0.867 0.688 -0.009 -0.167 0.058  516 GLU BBB CD  
2440 O OE1 . GLU B 187 ? 0.706 0.893 0.686 -0.024 -0.173 0.066  516 GLU BBB OE1 
2441 O OE2 . GLU B 187 ? 0.675 0.895 0.737 -0.000 -0.174 0.057  516 GLU BBB OE2 
2442 N N   . LEU B 188 ? 0.610 0.817 0.679 0.003  -0.126 0.030  517 LEU BBB N   
2443 C CA  . LEU B 188 ? 0.641 0.818 0.715 0.003  -0.141 0.034  517 LEU BBB CA  
2444 C C   . LEU B 188 ? 0.670 0.831 0.784 0.012  -0.169 0.040  517 LEU BBB C   
2445 O O   . LEU B 188 ? 0.680 0.860 0.848 0.025  -0.163 0.030  517 LEU BBB O   
2446 C CB  . LEU B 188 ? 0.627 0.815 0.721 0.008  -0.120 0.020  517 LEU BBB CB  
2447 C CG  . LEU B 188 ? 0.658 0.817 0.737 0.002  -0.127 0.023  517 LEU BBB CG  
2448 C CD1 . LEU B 188 ? 0.677 0.823 0.695 -0.015 -0.125 0.031  517 LEU BBB CD1 
2449 C CD2 . LEU B 188 ? 0.644 0.814 0.749 0.009  -0.106 0.008  517 LEU BBB CD2 
2450 N N   . LEU B 189 ? 0.715 0.843 0.805 0.003  -0.197 0.056  518 LEU BBB N   
2451 C CA  . LEU B 189 ? 0.721 0.828 0.845 0.010  -0.231 0.065  518 LEU BBB CA  
2452 C C   . LEU B 189 ? 0.776 0.842 0.894 0.006  -0.254 0.074  518 LEU BBB C   
2453 O O   . LEU B 189 ? 0.778 0.832 0.854 -0.005 -0.243 0.075  518 LEU BBB O   
2454 C CB  . LEU B 189 ? 0.729 0.828 0.821 0.000  -0.248 0.079  518 LEU BBB CB  
2455 C CG  . LEU B 189 ? 0.688 0.822 0.776 0.001  -0.227 0.072  518 LEU BBB CG  
2456 C CD1 . LEU B 189 ? 0.705 0.824 0.754 -0.011 -0.244 0.085  518 LEU BBB CD1 
2457 C CD2 . LEU B 189 ? 0.655 0.821 0.809 0.019  -0.218 0.059  518 LEU BBB CD2 
2458 N N   . HIS B 190 ? 0.831 0.876 0.990 0.014  -0.285 0.081  519 HIS BBB N   
2459 C CA  . HIS B 190 ? 0.885 0.883 1.036 0.009  -0.316 0.093  519 HIS BBB CA  
2460 C C   . HIS B 190 ? 0.921 0.884 0.999 -0.012 -0.337 0.113  519 HIS BBB C   
2461 O O   . HIS B 190 ? 0.944 0.883 1.025 -0.015 -0.372 0.127  519 HIS BBB O   
2462 C CB  . HIS B 190 ? 0.902 0.890 1.126 0.026  -0.344 0.093  519 HIS BBB CB  
2463 C CG  . HIS B 190 ? 0.965 0.911 1.192 0.025  -0.367 0.101  519 HIS BBB CG  
2464 N ND1 . HIS B 190 ? 1.043 0.943 1.258 0.018  -0.412 0.121  519 HIS BBB ND1 
2465 C CD2 . HIS B 190 ? 0.981 0.922 1.217 0.028  -0.353 0.092  519 HIS BBB CD2 
2466 C CE1 . HIS B 190 ? 1.076 0.943 1.295 0.018  -0.425 0.124  519 HIS BBB CE1 
2467 N NE2 . HIS B 190 ? 1.043 0.935 1.275 0.024  -0.389 0.106  519 HIS BBB NE2 
2468 N N   . ALA B 191 ? 0.819 0.842 0.955 0.091  -0.055 -0.001 520 ALA BBB N   
2469 C CA  . ALA B 191 ? 0.822 0.851 0.920 0.109  -0.080 -0.012 520 ALA BBB CA  
2470 C C   . ALA B 191 ? 0.817 0.810 0.840 0.090  -0.057 0.015  520 ALA BBB C   
2471 O O   . ALA B 191 ? 0.797 0.772 0.812 0.059  -0.031 0.033  520 ALA BBB O   
2472 C CB  . ALA B 191 ? 0.788 0.854 0.961 0.102  -0.104 -0.038 520 ALA BBB CB  
2473 N N   . PRO B 192 ? 0.845 0.828 0.812 0.109  -0.066 0.016  521 PRO BBB N   
2474 C CA  . PRO B 192 ? 0.848 0.806 0.765 0.089  -0.042 0.039  521 PRO BBB CA  
2475 C C   . PRO B 192 ? 0.801 0.781 0.758 0.054  -0.041 0.041  521 PRO BBB C   
2476 O O   . PRO B 192 ? 0.782 0.788 0.783 0.059  -0.060 0.025  521 PRO BBB O   
2477 C CB  . PRO B 192 ? 0.890 0.838 0.755 0.126  -0.051 0.038  521 PRO BBB CB  
2478 C CG  . PRO B 192 ? 0.923 0.878 0.783 0.174  -0.077 0.018  521 PRO BBB CG  
2479 C CD  . PRO B 192 ? 0.878 0.873 0.827 0.157  -0.097 -0.005 521 PRO BBB CD  
2480 N N   . ALA B 193 ? 0.793 0.760 0.734 0.023  -0.018 0.058  522 ALA BBB N   
2481 C CA  . ALA B 193 ? 0.762 0.749 0.722 -0.002 -0.015 0.065  522 ALA BBB CA  
2482 C C   . ALA B 193 ? 0.747 0.743 0.690 0.005  -0.019 0.069  522 ALA BBB C   
2483 O O   . ALA B 193 ? 0.788 0.763 0.691 0.012  -0.007 0.078  522 ALA BBB O   
2484 C CB  . ALA B 193 ? 0.779 0.752 0.721 -0.029 0.002  0.075  522 ALA BBB CB  
2485 N N   . THR B 194 ? 0.718 0.739 0.690 0.005  -0.030 0.066  523 THR BBB N   
2486 C CA  . THR B 194 ? 0.722 0.752 0.678 0.017  -0.033 0.071  523 THR BBB CA  
2487 C C   . THR B 194 ? 0.682 0.736 0.655 -0.004 -0.025 0.084  523 THR BBB C   
2488 O O   . THR B 194 ? 0.683 0.747 0.644 0.002  -0.021 0.093  523 THR BBB O   
2489 C CB  . THR B 194 ? 0.729 0.762 0.696 0.047  -0.056 0.050  523 THR BBB CB  
2490 O OG1 . THR B 194 ? 0.698 0.749 0.719 0.037  -0.062 0.040  523 THR BBB OG1 
2491 C CG2 . THR B 194 ? 0.755 0.776 0.715 0.072  -0.071 0.032  523 THR BBB CG2 
2492 N N   . VAL B 195 ? 0.655 0.719 0.649 -0.022 -0.021 0.086  524 VAL BBB N   
2493 C CA  . VAL B 195 ? 0.646 0.736 0.648 -0.033 -0.016 0.098  524 VAL BBB CA  
2494 C C   . VAL B 195 ? 0.662 0.754 0.647 -0.053 -0.011 0.101  524 VAL BBB C   
2495 O O   . VAL B 195 ? 0.689 0.767 0.672 -0.056 -0.007 0.099  524 VAL BBB O   
2496 C CB  . VAL B 195 ? 0.634 0.728 0.665 -0.025 -0.012 0.097  524 VAL BBB CB  
2497 C CG1 . VAL B 195 ? 0.629 0.748 0.656 -0.025 -0.006 0.113  524 VAL BBB CG1 
2498 C CG2 . VAL B 195 ? 0.641 0.728 0.697 -0.008 -0.021 0.084  524 VAL BBB CG2 
2499 N N   . CYS B 196 ? 0.671 0.779 0.649 -0.066 -0.009 0.105  525 CYS BBB N   
2500 C CA  . CYS B 196 ? 0.691 0.804 0.661 -0.089 -0.010 0.099  525 CYS BBB CA  
2501 C C   . CYS B 196 ? 0.686 0.850 0.673 -0.094 -0.019 0.101  525 CYS BBB C   
2502 O O   . CYS B 196 ? 0.658 0.847 0.661 -0.084 -0.018 0.112  525 CYS BBB O   
2503 C CB  . CYS B 196 ? 0.720 0.809 0.684 -0.103 0.003  0.095  525 CYS BBB CB  
2504 S SG  . CYS B 196 ? 0.764 0.797 0.700 -0.090 0.012  0.092  525 CYS BBB SG  
2505 N N   . GLY B 197 ? 0.711 0.888 0.688 -0.105 -0.030 0.090  526 GLY BBB N   
2506 C CA  . GLY B 197 ? 0.708 0.940 0.701 -0.108 -0.047 0.085  526 GLY BBB CA  
2507 C C   . GLY B 197 ? 0.706 0.963 0.741 -0.135 -0.045 0.076  526 GLY BBB C   
2508 O O   . GLY B 197 ? 0.706 0.925 0.744 -0.151 -0.027 0.074  526 GLY BBB O   
2509 N N   . PRO B 198 ? 0.707 1.028 0.780 -0.139 -0.059 0.072  527 PRO BBB N   
2510 C CA  . PRO B 198 ? 0.712 1.061 0.845 -0.166 -0.051 0.064  527 PRO BBB CA  
2511 C C   . PRO B 198 ? 0.758 1.085 0.908 -0.201 -0.050 0.037  527 PRO BBB C   
2512 O O   . PRO B 198 ? 0.784 1.108 0.983 -0.224 -0.027 0.035  527 PRO BBB O   
2513 C CB  . PRO B 198 ? 0.697 1.130 0.871 -0.159 -0.075 0.060  527 PRO BBB CB  
2514 C CG  . PRO B 198 ? 0.690 1.127 0.813 -0.120 -0.086 0.076  527 PRO BBB CG  
2515 C CD  . PRO B 198 ? 0.704 1.074 0.767 -0.115 -0.081 0.074  527 PRO BBB CD  
2516 N N   . LYS B 199 ? 0.807 1.111 0.914 -0.203 -0.068 0.016  528 LYS BBB N   
2517 C CA  . LYS B 199 ? 0.878 1.151 0.990 -0.235 -0.069 -0.015 528 LYS BBB CA  
2518 C C   . LYS B 199 ? 0.916 1.105 0.986 -0.236 -0.036 -0.002 528 LYS BBB C   
2519 O O   . LYS B 199 ? 0.957 1.106 1.021 -0.259 -0.030 -0.024 528 LYS BBB O   
2520 C CB  . LYS B 199 ? 0.913 1.203 0.988 -0.229 -0.107 -0.044 528 LYS BBB CB  
2521 C CG  . LYS B 199 ? 0.920 1.298 1.036 -0.226 -0.146 -0.066 528 LYS BBB CG  
2522 C CD  . LYS B 199 ? 0.891 1.313 0.990 -0.185 -0.154 -0.038 528 LYS BBB CD  
2523 C CE  . LYS B 199 ? 0.925 1.424 1.028 -0.165 -0.199 -0.061 528 LYS BBB CE  
2524 N NZ  . LYS B 199 ? 0.930 1.502 1.131 -0.198 -0.220 -0.093 528 LYS BBB NZ  
2525 N N   . LYS B 200 ? 0.932 1.096 0.977 -0.210 -0.018 0.029  529 LYS BBB N   
2526 C CA  . LYS B 200 ? 0.959 1.054 0.965 -0.199 0.007  0.042  529 LYS BBB CA  
2527 C C   . LYS B 200 ? 0.971 1.029 0.929 -0.197 -0.001 0.030  529 LYS BBB C   
2528 O O   . LYS B 200 ? 0.944 0.966 0.868 -0.175 0.008  0.043  529 LYS BBB O   
2529 C CB  . LYS B 200 ? 1.006 1.065 1.034 -0.218 0.041  0.043  529 LYS BBB CB  
2530 C CG  . LYS B 200 ? 1.001 1.073 1.057 -0.207 0.063  0.066  529 LYS BBB CG  
2531 C CD  . LYS B 200 ? 1.065 1.099 1.148 -0.225 0.107  0.070  529 LYS BBB CD  
2532 C CE  . LYS B 200 ? 1.071 1.108 1.171 -0.205 0.136  0.098  529 LYS BBB CE  
2533 N NZ  . LYS B 200 ? 1.131 1.120 1.256 -0.218 0.190  0.106  529 LYS BBB NZ  
2534 N N   . VAL C 4   ? 0.575 0.782 1.249 -0.081 -0.167 0.161  4   VAL CCC N   
2535 C CA  . VAL C 4   ? 0.504 0.758 1.193 -0.052 -0.125 0.181  4   VAL CCC CA  
2536 C C   . VAL C 4   ? 0.471 0.750 1.110 -0.034 -0.125 0.177  4   VAL CCC C   
2537 O O   . VAL C 4   ? 0.505 0.735 1.072 -0.047 -0.153 0.157  4   VAL CCC O   
2538 C CB  . VAL C 4   ? 0.527 0.743 1.204 -0.044 -0.098 0.162  4   VAL CCC CB  
2539 C CG1 . VAL C 4   ? 0.579 0.743 1.317 -0.053 -0.109 0.158  4   VAL CCC CG1 
2540 C CG2 . VAL C 4   ? 0.568 0.752 1.154 -0.051 -0.087 0.114  4   VAL CCC CG2 
2541 N N   . GLN C 5   ? 0.423 0.762 1.085 -0.013 -0.101 0.198  5   GLN CCC N   
2542 C CA  A GLN C 5   ? 0.417 0.762 1.030 0.006  -0.103 0.187  5   GLN CCC CA  
2543 C CA  B GLN C 5   ? 0.416 0.762 1.029 0.006  -0.103 0.187  5   GLN CCC CA  
2544 C C   . GLN C 5   ? 0.413 0.741 0.961 0.002  -0.084 0.189  5   GLN CCC C   
2545 O O   . GLN C 5   ? 0.395 0.756 0.972 0.001  -0.059 0.212  5   GLN CCC O   
2546 C CB  A GLN C 5   ? 0.398 0.824 1.064 0.027  -0.083 0.190  5   GLN CCC CB  
2547 C CB  B GLN C 5   ? 0.395 0.823 1.063 0.027  -0.082 0.191  5   GLN CCC CB  
2548 C CG  A GLN C 5   ? 0.425 0.836 1.055 0.056  -0.096 0.160  5   GLN CCC CG  
2549 C CG  B GLN C 5   ? 0.420 0.835 1.047 0.055  -0.091 0.162  5   GLN CCC CG  
2550 C CD  A GLN C 5   ? 0.462 0.843 1.134 0.076  -0.149 0.139  5   GLN CCC CD  
2551 C CD  B GLN C 5   ? 0.425 0.931 1.125 0.083  -0.066 0.138  5   GLN CCC CD  
2552 O OE1 A GLN C 5   ? 0.449 0.870 1.206 0.074  -0.164 0.145  5   GLN CCC OE1 
2553 O OE1 B GLN C 5   ? 0.417 0.989 1.217 0.088  -0.067 0.136  5   GLN CCC OE1 
2554 N NE2 A GLN C 5   ? 0.517 0.822 1.134 0.092  -0.190 0.122  5   GLN CCC NE2 
2555 N NE2 B GLN C 5   ? 0.452 0.970 1.104 0.098  -0.042 0.114  5   GLN CCC NE2 
2556 N N   . LEU C 6   ? 0.446 0.724 0.914 -0.009 -0.103 0.174  6   LEU CCC N   
2557 C CA  . LEU C 6   ? 0.454 0.732 0.863 -0.022 -0.090 0.178  6   LEU CCC CA  
2558 C C   . LEU C 6   ? 0.474 0.744 0.848 -0.009 -0.105 0.178  6   LEU CCC C   
2559 O O   . LEU C 6   ? 0.515 0.733 0.868 0.000  -0.144 0.163  6   LEU CCC O   
2560 C CB  . LEU C 6   ? 0.506 0.741 0.837 -0.061 -0.102 0.163  6   LEU CCC CB  
2561 C CG  . LEU C 6   ? 0.499 0.769 0.855 -0.073 -0.061 0.144  6   LEU CCC CG  
2562 C CD1 . LEU C 6   ? 0.479 0.747 0.914 -0.052 -0.052 0.134  6   LEU CCC CD1 
2563 C CD2 . LEU C 6   ? 0.579 0.828 0.839 -0.125 -0.060 0.120  6   LEU CCC CD2 
2564 N N   . VAL C 7   ? 0.457 0.769 0.829 -0.007 -0.083 0.192  7   VAL CCC N   
2565 C CA  . VAL C 7   ? 0.499 0.797 0.819 -0.000 -0.092 0.180  7   VAL CCC CA  
2566 C C   . VAL C 7   ? 0.540 0.801 0.781 -0.035 -0.112 0.190  7   VAL CCC C   
2567 O O   . VAL C 7   ? 0.489 0.801 0.748 -0.056 -0.094 0.215  7   VAL CCC O   
2568 C CB  . VAL C 7   ? 0.484 0.853 0.824 0.006  -0.058 0.191  7   VAL CCC CB  
2569 C CG1 . VAL C 7   ? 0.550 0.900 0.819 0.010  -0.061 0.159  7   VAL CCC CG1 
2570 C CG2 . VAL C 7   ? 0.449 0.874 0.872 0.022  -0.035 0.191  7   VAL CCC CG2 
2571 N N   . GLU C 8   ? 0.502 0.789 0.369 0.065  0.018  -0.102 8   GLU CCC N   
2572 C CA  . GLU C 8   ? 0.530 0.787 0.403 0.060  -0.003 -0.098 8   GLU CCC CA  
2573 C C   . GLU C 8   ? 0.612 0.821 0.457 0.063  -0.003 -0.122 8   GLU CCC C   
2574 O O   . GLU C 8   ? 0.640 0.843 0.484 0.080  0.016  -0.139 8   GLU CCC O   
2575 C CB  . GLU C 8   ? 0.510 0.780 0.427 0.071  -0.007 -0.081 8   GLU CCC CB  
2576 C CG  . GLU C 8   ? 0.524 0.769 0.451 0.061  -0.025 -0.068 8   GLU CCC CG  
2577 C CD  . GLU C 8   ? 0.525 0.777 0.483 0.070  -0.028 -0.047 8   GLU CCC CD  
2578 O OE1 . GLU C 8   ? 0.516 0.803 0.489 0.082  -0.021 -0.040 8   GLU CCC OE1 
2579 O OE2 . GLU C 8   ? 0.563 0.785 0.528 0.063  -0.037 -0.037 8   GLU CCC OE2 
2580 N N   . SER C 9   ? 0.663 0.841 0.491 0.048  -0.024 -0.125 9   SER CCC N   
2581 C CA  . SER C 9   ? 0.747 0.874 0.548 0.047  -0.029 -0.151 9   SER CCC CA  
2582 C C   . SER C 9   ? 0.761 0.865 0.578 0.029  -0.056 -0.145 9   SER CCC C   
2583 O O   . SER C 9   ? 0.696 0.828 0.541 0.019  -0.066 -0.121 9   SER CCC O   
2584 C CB  . SER C 9   ? 0.813 0.928 0.552 0.042  -0.024 -0.173 9   SER CCC CB  
2585 O OG  . SER C 9   ? 0.822 0.947 0.538 0.023  -0.045 -0.162 9   SER CCC OG  
2586 N N   . GLY C 10  ? 0.844 0.900 0.645 0.025  -0.065 -0.168 10  GLY CCC N   
2587 C CA  . GLY C 10  ? 0.881 0.908 0.704 0.006  -0.088 -0.167 10  GLY CCC CA  
2588 C C   . GLY C 10  ? 0.930 0.920 0.785 0.017  -0.080 -0.166 10  GLY CCC C   
2589 O O   . GLY C 10  ? 0.966 0.942 0.817 0.040  -0.061 -0.178 10  GLY CCC O   
2590 N N   . GLY C 11  ? 0.971 0.943 0.861 -0.000 -0.094 -0.152 11  GLY CCC N   
2591 C CA  . GLY C 11  ? 1.019 0.948 0.940 0.007  -0.089 -0.144 11  GLY CCC CA  
2592 C C   . GLY C 11  ? 1.106 0.968 1.016 -0.002 -0.098 -0.176 11  GLY CCC C   
2593 O O   . GLY C 11  ? 1.154 1.009 1.047 -0.026 -0.118 -0.195 11  GLY CCC O   
2594 N N   . GLY C 12  ? 1.155 0.967 1.075 0.018  -0.087 -0.184 12  GLY CCC N   
2595 C CA  . GLY C 12  ? 1.240 0.977 1.153 0.013  -0.094 -0.218 12  GLY CCC CA  
2596 C C   . GLY C 12  ? 1.261 0.955 1.214 -0.009 -0.106 -0.198 12  GLY CCC C   
2597 O O   . GLY C 12  ? 1.212 0.937 1.195 -0.016 -0.105 -0.156 12  GLY CCC O   
2598 N N   . LEU C 13  ? 1.343 0.966 1.295 -0.021 -0.115 -0.228 13  LEU CCC N   
2599 C CA  . LEU C 13  ? 1.390 0.957 1.382 -0.046 -0.125 -0.214 13  LEU CCC CA  
2600 C C   . LEU C 13  ? 1.378 0.962 1.377 -0.090 -0.148 -0.223 13  LEU CCC C   
2601 O O   . LEU C 13  ? 1.381 0.979 1.343 -0.097 -0.162 -0.260 13  LEU CCC O   
2602 C CB  . LEU C 13  ? 1.499 0.974 1.490 -0.033 -0.122 -0.246 13  LEU CCC CB  
2603 C CG  . LEU C 13  ? 1.533 0.995 1.515 0.016  -0.100 -0.256 13  LEU CCC CG  
2604 C CD1 . LEU C 13  ? 1.639 1.003 1.630 0.027  -0.098 -0.288 13  LEU CCC CD1 
2605 C CD2 . LEU C 13  ? 1.486 0.985 1.497 0.040  -0.089 -0.203 13  LEU CCC CD2 
2606 N N   . VAL C 14  ? 1.366 0.948 1.411 -0.119 -0.153 -0.192 14  VAL CCC N   
2607 C CA  . VAL C 14  ? 1.365 0.961 1.437 -0.164 -0.175 -0.200 14  VAL CCC CA  
2608 C C   . VAL C 14  ? 1.399 0.949 1.523 -0.192 -0.171 -0.174 14  VAL CCC C   
2609 O O   . VAL C 14  ? 1.411 0.944 1.547 -0.176 -0.151 -0.135 14  VAL CCC O   
2610 C CB  . VAL C 14  ? 1.278 0.968 1.357 -0.172 -0.180 -0.182 14  VAL CCC CB  
2611 C CG1 . VAL C 14  ? 1.261 0.986 1.286 -0.155 -0.190 -0.212 14  VAL CCC CG1 
2612 C CG2 . VAL C 14  ? 1.214 0.948 1.309 -0.157 -0.156 -0.133 14  VAL CCC CG2 
2613 N N   . LYS C 15  ? 1.417 0.949 1.573 -0.234 -0.191 -0.194 15  LYS CCC N   
2614 C CA  . LYS C 15  ? 1.446 0.939 1.659 -0.271 -0.187 -0.169 15  LYS CCC CA  
2615 C C   . LYS C 15  ? 1.364 0.934 1.615 -0.287 -0.172 -0.122 15  LYS CCC C   
2616 O O   . LYS C 15  ? 1.286 0.937 1.528 -0.278 -0.177 -0.123 15  LYS CCC O   
2617 C CB  . LYS C 15  ? 1.510 0.971 1.750 -0.313 -0.214 -0.211 15  LYS CCC CB  
2618 C CG  . LYS C 15  ? 1.595 0.972 1.797 -0.304 -0.228 -0.263 15  LYS CCC CG  
2619 C CD  . LYS C 15  ? 1.661 1.007 1.890 -0.349 -0.259 -0.305 15  LYS CCC CD  
2620 C CE  . LYS C 15  ? 1.770 1.014 1.966 -0.343 -0.266 -0.356 15  LYS CCC CE  
2621 N NZ  . LYS C 15  ? 1.848 1.048 2.085 -0.395 -0.294 -0.390 15  LYS CCC NZ  
2622 N N   . THR C 16  ? 1.389 0.929 1.677 -0.309 -0.154 -0.083 16  THR CCC N   
2623 C CA  . THR C 16  ? 1.340 0.945 1.668 -0.333 -0.136 -0.041 16  THR CCC CA  
2624 C C   . THR C 16  ? 1.301 0.977 1.675 -0.366 -0.155 -0.065 16  THR CCC C   
2625 O O   . THR C 16  ? 1.358 1.002 1.760 -0.395 -0.178 -0.099 16  THR CCC O   
2626 C CB  . THR C 16  ? 1.412 0.957 1.770 -0.360 -0.114 -0.001 16  THR CCC CB  
2627 O OG1 . THR C 16  ? 1.454 0.934 1.767 -0.324 -0.103 0.023  16  THR CCC OG1 
2628 C CG2 . THR C 16  ? 1.372 0.981 1.765 -0.387 -0.089 0.041  16  THR CCC CG2 
2629 N N   . GLY C 17  ? 1.223 0.990 1.607 -0.360 -0.147 -0.050 17  GLY CCC N   
2630 C CA  . GLY C 17  ? 1.186 1.032 1.619 -0.383 -0.166 -0.069 17  GLY CCC CA  
2631 C C   . GLY C 17  ? 1.161 1.037 1.553 -0.356 -0.197 -0.106 17  GLY CCC C   
2632 O O   . GLY C 17  ? 1.131 1.075 1.558 -0.367 -0.216 -0.118 17  GLY CCC O   
2633 N N   . GLY C 18  ? 1.185 1.012 1.507 -0.321 -0.199 -0.120 18  GLY CCC N   
2634 C CA  . GLY C 18  ? 1.164 1.008 1.432 -0.296 -0.223 -0.153 18  GLY CCC CA  
2635 C C   . GLY C 18  ? 1.085 0.999 1.332 -0.268 -0.212 -0.134 18  GLY CCC C   
2636 O O   . GLY C 18  ? 1.047 0.997 1.321 -0.267 -0.186 -0.098 18  GLY CCC O   
2637 N N   . SER C 19  ? 1.068 0.999 1.266 -0.246 -0.230 -0.158 19  SER CCC N   
2638 C CA  . SER C 19  ? 0.992 0.986 1.168 -0.221 -0.225 -0.144 19  SER CCC CA  
2639 C C   . SER C 19  ? 1.007 0.976 1.108 -0.186 -0.216 -0.154 19  SER CCC C   
2640 O O   . SER C 19  ? 1.078 0.994 1.138 -0.182 -0.226 -0.185 19  SER CCC O   
2641 C CB  . SER C 19  ? 0.964 1.011 1.161 -0.234 -0.257 -0.158 19  SER CCC CB  
2642 O OG  . SER C 19  ? 0.930 1.029 1.206 -0.256 -0.253 -0.138 19  SER CCC OG  
2643 N N   . LEU C 20  ? 0.948 0.956 1.035 -0.161 -0.195 -0.131 20  LEU CCC N   
2644 C CA  . LEU C 20  ? 0.945 0.949 0.972 -0.129 -0.184 -0.138 20  LEU CCC CA  
2645 C C   . LEU C 20  ? 0.868 0.935 0.890 -0.117 -0.180 -0.121 20  LEU CCC C   
2646 O O   . LEU C 20  ? 0.828 0.938 0.897 -0.128 -0.178 -0.101 20  LEU CCC O   
2647 C CB  . LEU C 20  ? 0.983 0.952 1.004 -0.109 -0.157 -0.123 20  LEU CCC CB  
2648 C CG  . LEU C 20  ? 1.077 0.971 1.088 -0.110 -0.159 -0.145 20  LEU CCC CG  
2649 C CD1 . LEU C 20  ? 1.092 0.957 1.109 -0.088 -0.135 -0.123 20  LEU CCC CD1 
2650 C CD2 . LEU C 20  ? 1.128 0.997 1.083 -0.099 -0.168 -0.186 20  LEU CCC CD2 
2651 N N   . ARG C 21  ? 0.857 0.927 0.827 -0.095 -0.176 -0.130 21  ARG CCC N   
2652 C CA  . ARG C 21  ? 0.801 0.920 0.760 -0.083 -0.173 -0.117 21  ARG CCC CA  
2653 C C   . ARG C 21  ? 0.775 0.890 0.696 -0.057 -0.147 -0.115 21  ARG CCC C   
2654 O O   . ARG C 21  ? 0.814 0.904 0.684 -0.048 -0.147 -0.136 21  ARG CCC O   
2655 C CB  . ARG C 21  ? 0.841 0.968 0.773 -0.091 -0.203 -0.133 21  ARG CCC CB  
2656 C CG  . ARG C 21  ? 0.822 0.990 0.740 -0.079 -0.202 -0.119 21  ARG CCC CG  
2657 C CD  . ARG C 21  ? 0.897 1.064 0.784 -0.086 -0.237 -0.132 21  ARG CCC CD  
2658 N NE  . ARG C 21  ? 0.941 1.105 0.763 -0.073 -0.235 -0.130 21  ARG CCC NE  
2659 C CZ  . ARG C 21  ? 0.994 1.130 0.755 -0.062 -0.214 -0.142 21  ARG CCC CZ  
2660 N NH1 . ARG C 21  ? 1.022 1.129 0.781 -0.058 -0.194 -0.156 21  ARG CCC NH1 
2661 N NH2 . ARG C 21  ? 1.038 1.173 0.743 -0.054 -0.212 -0.138 21  ARG CCC NH2 
2662 N N   . LEU C 22  ? 0.705 0.845 0.650 -0.047 -0.126 -0.092 22  LEU CCC N   
2663 C CA  . LEU C 22  ? 0.664 0.816 0.587 -0.024 -0.104 -0.087 22  LEU CCC CA  
2664 C C   . LEU C 22  ? 0.617 0.804 0.521 -0.022 -0.106 -0.085 22  LEU CCC C   
2665 O O   . LEU C 22  ? 0.584 0.795 0.508 -0.034 -0.121 -0.078 22  LEU CCC O   
2666 C CB  . LEU C 22  ? 0.634 0.803 0.589 -0.017 -0.088 -0.062 22  LEU CCC CB  
2667 C CG  . LEU C 22  ? 0.681 0.808 0.642 -0.008 -0.082 -0.060 22  LEU CCC CG  
2668 C CD1 . LEU C 22  ? 0.749 0.827 0.715 -0.025 -0.096 -0.076 22  LEU CCC CD1 
2669 C CD2 . LEU C 22  ? 0.661 0.803 0.649 -0.007 -0.072 -0.030 22  LEU CCC CD2 
2670 N N   . SER C 23  ? 0.629 0.820 0.501 -0.007 -0.091 -0.091 23  SER CCC N   
2671 C CA  . SER C 23  ? 0.618 0.835 0.467 -0.005 -0.088 -0.086 23  SER CCC CA  
2672 C C   . SER C 23  ? 0.567 0.811 0.426 0.009  -0.064 -0.076 23  SER CCC C   
2673 O O   . SER C 23  ? 0.560 0.796 0.424 0.022  -0.050 -0.082 23  SER CCC O   
2674 C CB  . SER C 23  ? 0.670 0.860 0.460 -0.006 -0.093 -0.105 23  SER CCC CB  
2675 O OG  . SER C 23  ? 0.732 0.913 0.510 -0.020 -0.123 -0.108 23  SER CCC OG  
2676 N N   . CYS C 24  ? 0.540 0.816 0.409 0.007  -0.062 -0.063 24  CYS CCC N   
2677 C CA  . CYS C 24  ? 0.527 0.832 0.406 0.016  -0.042 -0.056 24  CYS CCC CA  
2678 C C   . CYS C 24  ? 0.509 0.823 0.365 0.011  -0.041 -0.054 24  CYS CCC C   
2679 O O   . CYS C 24  ? 0.486 0.805 0.351 0.003  -0.056 -0.045 24  CYS CCC O   
2680 C CB  . CYS C 24  ? 0.504 0.837 0.423 0.016  -0.041 -0.042 24  CYS CCC CB  
2681 S SG  . CYS C 24  ? 0.542 0.909 0.475 0.028  -0.022 -0.038 24  CYS CCC SG  
2682 N N   . ALA C 25  ? 0.534 0.848 0.366 0.015  -0.022 -0.060 25  ALA CCC N   
2683 C CA  . ALA C 25  ? 0.552 0.865 0.354 0.008  -0.017 -0.055 25  ALA CCC CA  
2684 C C   . ALA C 25  ? 0.520 0.865 0.346 0.010  0.006  -0.051 25  ALA CCC C   
2685 O O   . ALA C 25  ? 0.519 0.881 0.366 0.019  0.020  -0.059 25  ALA CCC O   
2686 C CB  . ALA C 25  ? 0.615 0.897 0.358 0.006  -0.012 -0.066 25  ALA CCC CB  
2687 N N   . ALA C 26  ? 0.499 0.849 0.325 0.001  0.006  -0.040 26  ALA CCC N   
2688 C CA  . ALA C 26  ? 0.472 0.848 0.321 -0.002 0.024  -0.038 26  ALA CCC CA  
2689 C C   . ALA C 26  ? 0.492 0.849 0.314 -0.014 0.026  -0.026 26  ALA CCC C   
2690 O O   . ALA C 26  ? 0.511 0.848 0.323 -0.016 0.004  -0.017 26  ALA CCC O   
2691 C CB  . ALA C 26  ? 0.427 0.832 0.323 0.000  0.017  -0.035 26  ALA CCC CB  
2692 N N   . SER C 27  ? 0.506 0.867 0.318 -0.022 0.050  -0.026 27  SER CCC N   
2693 C CA  . SER C 27  ? 0.570 0.902 0.342 -0.035 0.055  -0.012 27  SER CCC CA  
2694 C C   . SER C 27  ? 0.534 0.861 0.333 -0.040 0.042  -0.000 27  SER CCC C   
2695 O O   . SER C 27  ? 0.497 0.854 0.347 -0.039 0.043  -0.007 27  SER CCC O   
2696 C CB  . SER C 27  ? 0.604 0.944 0.364 -0.046 0.090  -0.014 27  SER CCC CB  
2697 O OG  . SER C 27  ? 0.599 0.975 0.416 -0.052 0.103  -0.019 27  SER CCC OG  
2698 N N   . GLY C 28  ? 0.578 0.865 0.342 -0.044 0.027  0.017  28  GLY CCC N   
2699 C CA  . GLY C 28  ? 0.595 0.866 0.378 -0.048 0.018  0.030  28  GLY CCC CA  
2700 C C   . GLY C 28  ? 0.550 0.843 0.389 -0.037 0.001  0.021  28  GLY CCC C   
2701 O O   . GLY C 28  ? 0.522 0.822 0.366 -0.027 -0.018 0.017  28  GLY CCC O   
2702 N N   . ARG C 29  ? 0.555 0.859 0.433 -0.042 0.010  0.017  29  ARG CCC N   
2703 C CA  . ARG C 29  ? 0.519 0.835 0.443 -0.035 -0.001 0.009  29  ARG CCC CA  
2704 C C   . ARG C 29  ? 0.437 0.798 0.392 -0.030 0.004  -0.009 29  ARG CCC C   
2705 O O   . ARG C 29  ? 0.395 0.771 0.384 -0.026 -0.000 -0.019 29  ARG CCC O   
2706 C CB  . ARG C 29  ? 0.571 0.868 0.515 -0.043 0.006  0.010  29  ARG CCC CB  
2707 C CG  . ARG C 29  ? 0.680 0.924 0.593 -0.046 -0.002 0.034  29  ARG CCC CG  
2708 C CD  . ARG C 29  ? 0.763 0.977 0.703 -0.049 -0.002 0.037  29  ARG CCC CD  
2709 N NE  . ARG C 29  ? 0.873 1.032 0.780 -0.048 -0.015 0.065  29  ARG CCC NE  
2710 C CZ  . ARG C 29  ? 0.931 1.069 0.840 -0.030 -0.045 0.078  29  ARG CCC CZ  
2711 N NH1 . ARG C 29  ? 0.924 1.095 0.870 -0.013 -0.060 0.063  29  ARG CCC NH1 
2712 N NH2 . ARG C 29  ? 1.001 1.085 0.873 -0.029 -0.060 0.107  29  ARG CCC NH2 
2713 N N   . THR C 30  ? 0.414 0.795 0.356 -0.030 0.013  -0.014 30  THR CCC N   
2714 C CA  . THR C 30  ? 0.371 0.790 0.336 -0.025 0.015  -0.026 30  THR CCC CA  
2715 C C   . THR C 30  ? 0.354 0.779 0.336 -0.017 0.001  -0.028 30  THR CCC C   
2716 O O   . THR C 30  ? 0.336 0.783 0.343 -0.017 0.003  -0.036 30  THR CCC O   
2717 C CB  . THR C 30  ? 0.359 0.787 0.308 -0.021 0.022  -0.028 30  THR CCC CB  
2718 O OG1 . THR C 30  ? 0.373 0.804 0.315 -0.030 0.041  -0.029 30  THR CCC OG1 
2719 C CG2 . THR C 30  ? 0.325 0.785 0.296 -0.013 0.021  -0.036 30  THR CCC CG2 
2720 N N   . PHE C 31  ? 0.358 0.767 0.326 -0.011 -0.013 -0.021 31  PHE CCC N   
2721 C CA  . PHE C 31  ? 0.343 0.761 0.333 -0.006 -0.025 -0.022 31  PHE CCC CA  
2722 C C   . PHE C 31  ? 0.327 0.745 0.346 -0.004 -0.029 -0.023 31  PHE CCC C   
2723 O O   . PHE C 31  ? 0.297 0.734 0.345 -0.001 -0.030 -0.027 31  PHE CCC O   
2724 C CB  . PHE C 31  ? 0.354 0.755 0.326 -0.003 -0.040 -0.016 31  PHE CCC CB  
2725 C CG  . PHE C 31  ? 0.371 0.773 0.326 -0.002 -0.035 -0.020 31  PHE CCC CG  
2726 C CD1 . PHE C 31  ? 0.361 0.785 0.331 0.000  -0.025 -0.023 31  PHE CCC CD1 
2727 C CD2 . PHE C 31  ? 0.414 0.791 0.334 -0.002 -0.042 -0.020 31  PHE CCC CD2 
2728 C CE1 . PHE C 31  ? 0.371 0.792 0.330 0.005  -0.022 -0.025 31  PHE CCC CE1 
2729 C CE2 . PHE C 31  ? 0.427 0.800 0.335 0.001  -0.036 -0.027 31  PHE CCC CE2 
2730 C CZ  . PHE C 31  ? 0.413 0.808 0.345 0.006  -0.026 -0.028 31  PHE CCC CZ  
2731 N N   . SER C 32  ? 0.344 0.739 0.358 -0.006 -0.030 -0.018 32  SER CCC N   
2732 C CA  . SER C 32  ? 0.350 0.736 0.394 -0.001 -0.034 -0.020 32  SER CCC CA  
2733 C C   . SER C 32  ? 0.327 0.731 0.392 -0.006 -0.016 -0.036 32  SER CCC C   
2734 O O   . SER C 32  ? 0.342 0.743 0.437 -0.001 -0.015 -0.045 32  SER CCC O   
2735 C CB  . SER C 32  ? 0.398 0.745 0.425 -0.001 -0.045 -0.005 32  SER CCC CB  
2736 O OG  . SER C 32  ? 0.434 0.768 0.452 0.007  -0.069 0.007  32  SER CCC OG  
2737 N N   . THR C 33  ? 0.325 0.747 0.375 -0.014 -0.004 -0.043 33  THR CCC N   
2738 C CA  . THR C 33  ? 0.315 0.756 0.377 -0.021 0.009  -0.060 33  THR CCC CA  
2739 C C   . THR C 33  ? 0.312 0.789 0.374 -0.019 0.012  -0.068 33  THR CCC C   
2740 O O   . THR C 33  ? 0.325 0.817 0.398 -0.022 0.019  -0.084 33  THR CCC O   
2741 C CB  . THR C 33  ? 0.324 0.762 0.375 -0.033 0.017  -0.060 33  THR CCC CB  
2742 O OG1 . THR C 33  ? 0.345 0.744 0.387 -0.036 0.015  -0.046 33  THR CCC OG1 
2743 C CG2 . THR C 33  ? 0.323 0.779 0.390 -0.043 0.025  -0.079 33  THR CCC CG2 
2744 N N   . TYR C 34  ? 0.308 0.794 0.355 -0.016 0.008  -0.058 34  TYR CCC N   
2745 C CA  . TYR C 34  ? 0.321 0.834 0.363 -0.014 0.009  -0.059 34  TYR CCC CA  
2746 C C   . TYR C 34  ? 0.323 0.832 0.365 -0.009 0.004  -0.048 34  TYR CCC C   
2747 O O   . TYR C 34  ? 0.380 0.871 0.412 -0.006 -0.003 -0.039 34  TYR CCC O   
2748 C CB  . TYR C 34  ? 0.330 0.857 0.361 -0.015 0.009  -0.057 34  TYR CCC CB  
2749 C CG  . TYR C 34  ? 0.338 0.872 0.376 -0.024 0.014  -0.068 34  TYR CCC CG  
2750 C CD1 . TYR C 34  ? 0.337 0.888 0.383 -0.031 0.016  -0.084 34  TYR CCC CD1 
2751 C CD2 . TYR C 34  ? 0.344 0.869 0.382 -0.028 0.018  -0.064 34  TYR CCC CD2 
2752 C CE1 . TYR C 34  ? 0.339 0.896 0.397 -0.042 0.019  -0.096 34  TYR CCC CE1 
2753 C CE2 . TYR C 34  ? 0.344 0.878 0.396 -0.040 0.025  -0.074 34  TYR CCC CE2 
2754 C CZ  . TYR C 34  ? 0.348 0.898 0.413 -0.048 0.024  -0.090 34  TYR CCC CZ  
2755 O OH  . TYR C 34  ? 0.376 0.934 0.460 -0.063 0.029  -0.102 34  TYR CCC OH  
2756 N N   . SER C 35  ? 0.318 0.842 0.367 -0.010 0.010  -0.050 35  SER CCC N   
2757 C CA  . SER C 35  ? 0.311 0.836 0.363 -0.009 0.008  -0.040 35  SER CCC CA  
2758 C C   . SER C 35  ? 0.303 0.821 0.335 -0.007 0.001  -0.028 35  SER CCC C   
2759 O O   . SER C 35  ? 0.321 0.848 0.338 -0.005 0.002  -0.029 35  SER CCC O   
2760 C CB  . SER C 35  ? 0.329 0.875 0.386 -0.014 0.022  -0.044 35  SER CCC CB  
2761 O OG  . SER C 35  ? 0.325 0.877 0.409 -0.013 0.030  -0.058 35  SER CCC OG  
2762 N N   . MET C 36  ? 0.316 0.817 0.351 -0.007 -0.006 -0.019 36  MET CCC N   
2763 C CA  . MET C 36  ? 0.330 0.815 0.348 -0.003 -0.012 -0.011 36  MET CCC CA  
2764 C C   . MET C 36  ? 0.350 0.832 0.371 -0.008 -0.010 0.000  36  MET CCC C   
2765 O O   . MET C 36  ? 0.341 0.832 0.381 -0.016 -0.004 0.001  36  MET CCC O   
2766 C CB  . MET C 36  ? 0.353 0.813 0.366 -0.001 -0.022 -0.013 36  MET CCC CB  
2767 C CG  . MET C 36  ? 0.347 0.795 0.375 -0.007 -0.032 -0.012 36  MET CCC CG  
2768 S SD  . MET C 36  ? 0.364 0.796 0.396 -0.012 -0.035 -0.004 36  MET CCC SD  
2769 C CE  . MET C 36  ? 0.397 0.804 0.398 -0.001 -0.036 -0.006 36  MET CCC CE  
2770 N N   . GLY C 37  ? 0.368 0.838 0.374 -0.002 -0.013 0.010  37  GLY CCC N   
2771 C CA  . GLY C 37  ? 0.394 0.852 0.398 -0.007 -0.011 0.026  37  GLY CCC CA  
2772 C C   . GLY C 37  ? 0.405 0.829 0.405 -0.001 -0.020 0.031  37  GLY CCC C   
2773 O O   . GLY C 37  ? 0.393 0.812 0.384 0.012  -0.024 0.025  37  GLY CCC O   
2774 N N   . TRP C 38  ? 0.431 0.831 0.440 -0.011 -0.021 0.038  38  TRP CCC N   
2775 C CA  . TRP C 38  ? 0.472 0.831 0.477 -0.007 -0.028 0.044  38  TRP CCC CA  
2776 C C   . TRP C 38  ? 0.489 0.837 0.483 -0.006 -0.024 0.068  38  TRP CCC C   
2777 O O   . TRP C 38  ? 0.525 0.885 0.520 -0.021 -0.014 0.081  38  TRP CCC O   
2778 C CB  . TRP C 38  ? 0.497 0.834 0.520 -0.022 -0.035 0.037  38  TRP CCC CB  
2779 C CG  . TRP C 38  ? 0.481 0.820 0.504 -0.020 -0.044 0.016  38  TRP CCC CG  
2780 C CD1 . TRP C 38  ? 0.465 0.827 0.503 -0.028 -0.048 0.008  38  TRP CCC CD1 
2781 C CD2 . TRP C 38  ? 0.508 0.822 0.511 -0.009 -0.052 0.001  38  TRP CCC CD2 
2782 N NE1 . TRP C 38  ? 0.477 0.827 0.500 -0.023 -0.060 -0.007 38  TRP CCC NE1 
2783 C CE2 . TRP C 38  ? 0.503 0.824 0.501 -0.013 -0.060 -0.013 38  TRP CCC CE2 
2784 C CE3 . TRP C 38  ? 0.529 0.814 0.518 0.005  -0.051 -0.003 38  TRP CCC CE3 
2785 C CZ2 . TRP C 38  ? 0.522 0.822 0.492 -0.006 -0.066 -0.029 38  TRP CCC CZ2 
2786 C CZ3 . TRP C 38  ? 0.558 0.826 0.527 0.013  -0.053 -0.023 38  TRP CCC CZ3 
2787 C CH2 . TRP C 38  ? 0.552 0.828 0.507 0.006  -0.060 -0.035 38  TRP CCC CH2 
2788 N N   . PHE C 39  ? 0.501 0.829 0.485 0.011  -0.032 0.074  39  PHE CCC N   
2789 C CA  . PHE C 39  ? 0.533 0.838 0.503 0.017  -0.034 0.102  39  PHE CCC CA  
2790 C C   . PHE C 39  ? 0.576 0.827 0.555 0.025  -0.042 0.103  39  PHE CCC C   
2791 O O   . PHE C 39  ? 0.575 0.814 0.565 0.031  -0.045 0.079  39  PHE CCC O   
2792 C CB  . PHE C 39  ? 0.517 0.850 0.472 0.035  -0.041 0.108  39  PHE CCC CB  
2793 C CG  . PHE C 39  ? 0.477 0.857 0.419 0.026  -0.034 0.105  39  PHE CCC CG  
2794 C CD1 . PHE C 39  ? 0.417 0.829 0.371 0.023  -0.029 0.081  39  PHE CCC CD1 
2795 C CD2 . PHE C 39  ? 0.509 0.897 0.422 0.020  -0.032 0.128  39  PHE CCC CD2 
2796 C CE1 . PHE C 39  ? 0.410 0.858 0.354 0.015  -0.022 0.075  39  PHE CCC CE1 
2797 C CE2 . PHE C 39  ? 0.483 0.912 0.380 0.011  -0.024 0.120  39  PHE CCC CE2 
2798 C CZ  . PHE C 39  ? 0.435 0.893 0.351 0.009  -0.019 0.092  39  PHE CCC CZ  
2799 N N   . ARG C 40  ? 0.630 0.845 0.600 0.024  -0.044 0.131  40  ARG CCC N   
2800 C CA  . ARG C 40  ? 0.682 0.836 0.662 0.034  -0.052 0.135  40  ARG CCC CA  
2801 C C   . ARG C 40  ? 0.737 0.869 0.702 0.052  -0.061 0.168  40  ARG CCC C   
2802 O O   . ARG C 40  ? 0.747 0.900 0.687 0.044  -0.059 0.194  40  ARG CCC O   
2803 C CB  . ARG C 40  ? 0.707 0.823 0.699 0.007  -0.046 0.136  40  ARG CCC CB  
2804 C CG  . ARG C 40  ? 0.740 0.849 0.722 -0.017 -0.035 0.170  40  ARG CCC CG  
2805 C CD  . ARG C 40  ? 0.765 0.850 0.773 -0.048 -0.029 0.163  40  ARG CCC CD  
2806 N NE  . ARG C 40  ? 0.803 0.886 0.808 -0.076 -0.012 0.193  40  ARG CCC NE  
2807 C CZ  . ARG C 40  ? 0.821 0.893 0.856 -0.108 -0.003 0.191  40  ARG CCC CZ  
2808 N NH1 . ARG C 40  ? 0.804 0.864 0.872 -0.115 -0.014 0.161  40  ARG CCC NH1 
2809 N NH2 . ARG C 40  ? 0.860 0.934 0.892 -0.133 0.018  0.220  40  ARG CCC NH2 
2810 N N   . GLN C 41  ? 0.773 0.864 0.751 0.077  -0.072 0.167  41  GLN CCC N   
2811 C CA  . GLN C 41  ? 0.832 0.895 0.804 0.100  -0.086 0.199  41  GLN CCC CA  
2812 C C   . GLN C 41  ? 0.908 0.891 0.898 0.107  -0.090 0.202  41  GLN CCC C   
2813 O O   . GLN C 41  ? 0.905 0.874 0.920 0.124  -0.090 0.170  41  GLN CCC O   
2814 C CB  . GLN C 41  ? 0.801 0.909 0.787 0.133  -0.098 0.188  41  GLN CCC CB  
2815 C CG  . GLN C 41  ? 0.862 0.954 0.843 0.159  -0.120 0.223  41  GLN CCC CG  
2816 C CD  . GLN C 41  ? 0.828 0.986 0.820 0.182  -0.134 0.216  41  GLN CCC CD  
2817 O OE1 . GLN C 41  ? 0.764 0.970 0.777 0.184  -0.125 0.182  41  GLN CCC OE1 
2818 N NE2 . GLN C 41  ? 0.877 1.038 0.853 0.198  -0.157 0.251  41  GLN CCC NE2 
2819 N N   . ALA C 42  ? 0.992 0.924 0.966 0.093  -0.090 0.239  42  ALA CCC N   
2820 C CA  . ALA C 42  ? 1.086 0.930 1.074 0.099  -0.096 0.252  42  ALA CCC CA  
2821 C C   . ALA C 42  ? 1.145 0.968 1.136 0.140  -0.117 0.276  42  ALA CCC C   
2822 O O   . ALA C 42  ? 1.129 0.998 1.100 0.152  -0.128 0.297  42  ALA CCC O   
2823 C CB  . ALA C 42  ? 1.135 0.936 1.105 0.061  -0.086 0.284  42  ALA CCC CB  
2824 N N   . PRO C 43  ? 1.223 0.975 1.242 0.163  -0.125 0.273  43  PRO CCC N   
2825 C CA  . PRO C 43  ? 1.272 1.014 1.313 0.211  -0.146 0.284  43  PRO CCC CA  
2826 C C   . PRO C 43  ? 1.305 1.077 1.318 0.226  -0.167 0.331  43  PRO CCC C   
2827 O O   . PRO C 43  ? 1.269 1.103 1.299 0.254  -0.180 0.319  43  PRO CCC O   
2828 C CB  . PRO C 43  ? 1.365 1.000 1.423 0.219  -0.150 0.295  43  PRO CCC CB  
2829 C CG  . PRO C 43  ? 1.343 0.955 1.409 0.186  -0.129 0.256  43  PRO CCC CG  
2830 C CD  . PRO C 43  ? 1.269 0.947 1.304 0.145  -0.116 0.256  43  PRO CCC CD  
2831 N N   . GLY C 44  ? 1.388 1.115 1.359 0.207  -0.172 0.382  44  GLY CCC N   
2832 C CA  . GLY C 44  ? 1.442 1.187 1.371 0.218  -0.194 0.431  44  GLY CCC CA  
2833 C C   . GLY C 44  ? 1.433 1.222 1.303 0.177  -0.178 0.447  44  GLY CCC C   
2834 O O   . GLY C 44  ? 1.512 1.258 1.332 0.158  -0.178 0.496  44  GLY CCC O   
2835 N N   . LYS C 45  ? 1.351 1.219 1.228 0.163  -0.164 0.407  45  LYS CCC N   
2836 C CA  . LYS C 45  ? 1.324 1.240 1.155 0.125  -0.144 0.410  45  LYS CCC CA  
2837 C C   . LYS C 45  ? 1.236 1.243 1.074 0.131  -0.145 0.374  45  LYS CCC C   
2838 O O   . LYS C 45  ? 1.179 1.212 1.063 0.158  -0.154 0.342  45  LYS CCC O   
2839 C CB  . LYS C 45  ? 1.325 1.218 1.167 0.085  -0.113 0.394  45  LYS CCC CB  
2840 C CG  . LYS C 45  ? 1.429 1.242 1.252 0.061  -0.103 0.435  45  LYS CCC CG  
2841 C CD  . LYS C 45  ? 1.419 1.234 1.255 0.016  -0.072 0.419  45  LYS CCC CD  
2842 C CE  . LYS C 45  ? 1.518 1.245 1.364 -0.006 -0.063 0.442  45  LYS CCC CE  
2843 N NZ  . LYS C 45  ? 1.488 1.224 1.372 -0.043 -0.040 0.410  45  LYS CCC NZ  
2844 N N   . GLU C 46  ? 1.230 1.282 1.026 0.105  -0.132 0.378  46  GLU CCC N   
2845 C CA  . GLU C 46  ? 1.169 1.304 0.965 0.104  -0.131 0.346  46  GLU CCC CA  
2846 C C   . GLU C 46  ? 1.069 1.227 0.903 0.087  -0.106 0.301  46  GLU CCC C   
2847 O O   . GLU C 46  ? 1.062 1.181 0.906 0.066  -0.088 0.300  46  GLU CCC O   
2848 C CB  . GLU C 46  ? 1.211 1.374 0.941 0.084  -0.126 0.367  46  GLU CCC CB  
2849 C CG  . GLU C 46  ? 1.172 1.412 0.897 0.086  -0.131 0.338  46  GLU CCC CG  
2850 C CD  . GLU C 46  ? 1.189 1.460 0.937 0.121  -0.166 0.332  46  GLU CCC CD  
2851 O OE1 . GLU C 46  ? 1.263 1.522 0.978 0.137  -0.194 0.367  46  GLU CCC OE1 
2852 O OE2 . GLU C 46  ? 1.103 1.411 0.904 0.131  -0.165 0.294  46  GLU CCC OE2 
2853 N N   . ARG C 47  ? 0.810 1.162 0.793 0.173  -0.065 0.165  47  ARG CCC N   
2854 C CA  . ARG C 47  ? 0.763 1.116 0.761 0.142  -0.060 0.136  47  ARG CCC CA  
2855 C C   . ARG C 47  ? 0.748 1.118 0.733 0.124  -0.050 0.149  47  ARG CCC C   
2856 O O   . ARG C 47  ? 0.725 1.144 0.693 0.129  -0.052 0.140  47  ARG CCC O   
2857 C CB  . ARG C 47  ? 0.732 1.122 0.734 0.145  -0.068 0.096  47  ARG CCC CB  
2858 C CG  . ARG C 47  ? 0.728 1.100 0.750 0.125  -0.066 0.066  47  ARG CCC CG  
2859 C CD  . ARG C 47  ? 0.707 1.115 0.736 0.128  -0.070 0.032  47  ARG CCC CD  
2860 N NE  . ARG C 47  ? 0.722 1.123 0.766 0.144  -0.076 0.017  47  ARG CCC NE  
2861 C CZ  . ARG C 47  ? 0.704 1.134 0.761 0.147  -0.078 -0.013 47  ARG CCC CZ  
2862 N NH1 . ARG C 47  ? 0.684 1.147 0.742 0.132  -0.072 -0.031 47  ARG CCC NH1 
2863 N NH2 . ARG C 47  ? 0.726 1.150 0.797 0.163  -0.083 -0.025 47  ARG CCC NH2 
2864 N N   . GLU C 48  ? 0.735 1.070 0.732 0.104  -0.039 0.167  48  GLU CCC N   
2865 C CA  . GLU C 48  ? 0.705 1.057 0.696 0.087  -0.028 0.182  48  GLU CCC CA  
2866 C C   . GLU C 48  ? 0.635 0.994 0.638 0.062  -0.027 0.151  48  GLU CCC C   
2867 O O   . GLU C 48  ? 0.632 0.963 0.654 0.052  -0.031 0.130  48  GLU CCC O   
2868 C CB  . GLU C 48  ? 0.767 1.082 0.768 0.079  -0.015 0.222  48  GLU CCC CB  
2869 C CG  . GLU C 48  ? 0.788 1.050 0.824 0.058  -0.014 0.214  48  GLU CCC CG  
2870 C CD  . GLU C 48  ? 0.848 1.075 0.904 0.045  0.000  0.251  48  GLU CCC CD  
2871 O OE1 . GLU C 48  ? 0.883 1.111 0.921 0.061  0.009  0.291  48  GLU CCC OE1 
2872 O OE2 . GLU C 48  ? 0.840 1.039 0.929 0.020  0.003  0.241  48  GLU CCC OE2 
2873 N N   . PHE C 49  ? 0.580 0.977 0.570 0.056  -0.022 0.148  49  PHE CCC N   
2874 C CA  . PHE C 49  ? 0.529 0.935 0.528 0.035  -0.020 0.124  49  PHE CCC CA  
2875 C C   . PHE C 49  ? 0.530 0.904 0.553 0.014  -0.013 0.133  49  PHE CCC C   
2876 O O   . PHE C 49  ? 0.548 0.911 0.578 0.010  -0.005 0.164  49  PHE CCC O   
2877 C CB  . PHE C 49  ? 0.498 0.949 0.481 0.037  -0.015 0.123  49  PHE CCC CB  
2878 C CG  . PHE C 49  ? 0.472 0.930 0.464 0.019  -0.012 0.103  49  PHE CCC CG  
2879 C CD1 . PHE C 49  ? 0.444 0.903 0.439 0.016  -0.018 0.073  49  PHE CCC CD1 
2880 C CD2 . PHE C 49  ? 0.491 0.953 0.490 0.005  -0.003 0.117  49  PHE CCC CD2 
2881 C CE1 . PHE C 49  ? 0.438 0.899 0.438 0.003  -0.016 0.059  49  PHE CCC CE1 
2882 C CE2 . PHE C 49  ? 0.464 0.934 0.472 -0.008 -0.003 0.099  49  PHE CCC CE2 
2883 C CZ  . PHE C 49  ? 0.436 0.903 0.442 -0.008 -0.009 0.071  49  PHE CCC CZ  
2884 N N   . VAL C 50  ? 0.499 0.863 0.536 -0.000 -0.018 0.108  50  VAL CCC N   
2885 C CA  . VAL C 50  ? 0.505 0.846 0.568 -0.021 -0.016 0.107  50  VAL CCC CA  
2886 C C   . VAL C 50  ? 0.475 0.843 0.537 -0.033 -0.013 0.095  50  VAL CCC C   
2887 O O   . VAL C 50  ? 0.498 0.877 0.572 -0.044 -0.005 0.111  50  VAL CCC O   
2888 C CB  . VAL C 50  ? 0.518 0.825 0.595 -0.022 -0.025 0.084  50  VAL CCC CB  
2889 C CG1 . VAL C 50  ? 0.531 0.821 0.636 -0.042 -0.026 0.076  50  VAL CCC CG1 
2890 C CG2 . VAL C 50  ? 0.555 0.833 0.635 -0.008 -0.028 0.095  50  VAL CCC CG2 
2891 N N   . ALA C 51  ? 0.438 0.818 0.489 -0.030 -0.018 0.070  51  ALA CCC N   
2892 C CA  . ALA C 51  ? 0.408 0.808 0.458 -0.038 -0.018 0.056  51  ALA CCC CA  
2893 C C   . ALA C 51  ? 0.387 0.799 0.419 -0.028 -0.020 0.037  51  ALA CCC C   
2894 O O   . ALA C 51  ? 0.397 0.797 0.423 -0.020 -0.023 0.029  51  ALA CCC O   
2895 C CB  . ALA C 51  ? 0.400 0.784 0.470 -0.051 -0.023 0.045  51  ALA CCC CB  
2896 N N   . GLY C 52  ? 0.372 0.805 0.397 -0.030 -0.017 0.030  52  GLY CCC N   
2897 C CA  . GLY C 52  ? 0.364 0.805 0.377 -0.023 -0.017 0.014  52  GLY CCC CA  
2898 C C   . GLY C 52  ? 0.354 0.802 0.366 -0.027 -0.015 0.006  52  GLY CCC C   
2899 O O   . GLY C 52  ? 0.339 0.794 0.360 -0.033 -0.015 0.012  52  GLY CCC O   
2900 N N   . MET C 53  ? 0.354 0.800 0.357 -0.023 -0.013 -0.007 53  MET CCC N   
2901 C CA  . MET C 53  ? 0.361 0.810 0.361 -0.022 -0.011 -0.013 53  MET CCC CA  
2902 C C   . MET C 53  ? 0.346 0.801 0.343 -0.017 -0.005 -0.023 53  MET CCC C   
2903 O O   . MET C 53  ? 0.346 0.794 0.343 -0.016 -0.003 -0.030 53  MET CCC O   
2904 C CB  . MET C 53  ? 0.357 0.788 0.351 -0.022 -0.013 -0.019 53  MET CCC CB  
2905 C CG  . MET C 53  ? 0.371 0.802 0.357 -0.017 -0.011 -0.021 53  MET CCC CG  
2906 S SD  . MET C 53  ? 0.410 0.825 0.381 -0.012 -0.014 -0.025 53  MET CCC SD  
2907 C CE  . MET C 53  ? 0.413 0.841 0.394 -0.015 -0.027 -0.026 53  MET CCC CE  
2908 N N   . ARG C 54  ? 0.340 0.807 0.338 -0.014 -0.002 -0.025 54  ARG CCC N   
2909 C CA  . ARG C 54  ? 0.335 0.805 0.336 -0.010 0.003  -0.038 54  ARG CCC CA  
2910 C C   . ARG C 54  ? 0.351 0.794 0.349 -0.011 0.009  -0.041 54  ARG CCC C   
2911 O O   . ARG C 54  ? 0.367 0.798 0.357 -0.010 0.007  -0.033 54  ARG CCC O   
2912 C CB  . ARG C 54  ? 0.328 0.816 0.332 -0.004 0.004  -0.040 54  ARG CCC CB  
2913 C CG  . ARG C 54  ? 0.314 0.833 0.317 -0.002 0.002  -0.034 54  ARG CCC CG  
2914 C CD  . ARG C 54  ? 0.314 0.849 0.315 0.002  0.001  -0.042 54  ARG CCC CD  
2915 N NE  . ARG C 54  ? 0.310 0.877 0.305 0.007  0.001  -0.032 54  ARG CCC NE  
2916 C CZ  . ARG C 54  ? 0.301 0.895 0.290 0.016  -0.001 -0.037 54  ARG CCC CZ  
2917 N NH1 . ARG C 54  ? 0.310 0.904 0.303 0.019  -0.005 -0.057 54  ARG CCC NH1 
2918 N NH2 . ARG C 54  ? 0.292 0.915 0.271 0.022  0.001  -0.023 54  ARG CCC NH2 
2919 N N   . TRP C 55  ? 0.361 0.797 0.368 -0.011 0.015  -0.052 55  TRP CCC N   
2920 C CA  . TRP C 55  ? 0.380 0.790 0.386 -0.013 0.026  -0.052 55  TRP CCC CA  
2921 C C   . TRP C 55  ? 0.383 0.777 0.379 -0.006 0.027  -0.043 55  TRP CCC C   
2922 O O   . TRP C 55  ? 0.408 0.780 0.395 -0.005 0.035  -0.035 55  TRP CCC O   
2923 C CB  . TRP C 55  ? 0.396 0.804 0.423 -0.018 0.034  -0.068 55  TRP CCC CB  
2924 C CG  . TRP C 55  ? 0.412 0.821 0.450 -0.014 0.035  -0.078 55  TRP CCC CG  
2925 C CD1 . TRP C 55  ? 0.419 0.804 0.457 -0.009 0.042  -0.073 55  TRP CCC CD1 
2926 C CD2 . TRP C 55  ? 0.400 0.837 0.450 -0.011 0.028  -0.095 55  TRP CCC CD2 
2927 N NE1 . TRP C 55  ? 0.429 0.822 0.480 -0.005 0.040  -0.088 55  TRP CCC NE1 
2928 C CE2 . TRP C 55  ? 0.408 0.835 0.467 -0.006 0.032  -0.103 55  TRP CCC CE2 
2929 C CE3 . TRP C 55  ? 0.374 0.843 0.426 -0.010 0.020  -0.104 55  TRP CCC CE3 
2930 C CZ2 . TRP C 55  ? 0.401 0.852 0.470 -0.000 0.027  -0.124 55  TRP CCC CZ2 
2931 C CZ3 . TRP C 55  ? 0.386 0.881 0.445 -0.004 0.015  -0.122 55  TRP CCC CZ3 
2932 C CH2 . TRP C 55  ? 0.398 0.885 0.466 0.001  0.018  -0.134 55  TRP CCC CH2 
2933 N N   . THR C 56  ? 0.359 0.768 0.356 -0.001 0.021  -0.043 56  THR CCC N   
2934 C CA  . THR C 56  ? 0.389 0.790 0.379 0.010  0.021  -0.037 56  THR CCC CA  
2935 C C   . THR C 56  ? 0.404 0.803 0.378 0.013  0.014  -0.025 56  THR CCC C   
2936 O O   . THR C 56  ? 0.434 0.821 0.397 0.024  0.015  -0.018 56  THR CCC O   
2937 C CB  . THR C 56  ? 0.362 0.788 0.360 0.015  0.015  -0.043 56  THR CCC CB  
2938 O OG1 . THR C 56  ? 0.351 0.803 0.349 0.010  0.008  -0.038 56  THR CCC OG1 
2939 C CG2 . THR C 56  ? 0.366 0.799 0.379 0.015  0.019  -0.060 56  THR CCC CG2 
2940 N N   . GLY C 57  ? 0.399 0.810 0.371 0.006  0.007  -0.024 57  GLY CCC N   
2941 C CA  . GLY C 57  ? 0.406 0.822 0.369 0.008  -0.002 -0.019 57  GLY CCC CA  
2942 C C   . GLY C 57  ? 0.400 0.840 0.372 0.010  -0.011 -0.019 57  GLY CCC C   
2943 O O   . GLY C 57  ? 0.399 0.847 0.371 0.010  -0.020 -0.019 57  GLY CCC O   
2944 N N   . SER C 58  ? 0.359 0.813 0.342 0.013  -0.008 -0.021 58  SER CCC N   
2945 C CA  . SER C 58  ? 0.361 0.844 0.356 0.018  -0.014 -0.021 58  SER CCC CA  
2946 C C   . SER C 58  ? 0.341 0.850 0.351 0.007  -0.013 -0.020 58  SER CCC C   
2947 O O   . SER C 58  ? 0.357 0.895 0.380 0.009  -0.014 -0.019 58  SER CCC O   
2948 C CB  . SER C 58  ? 0.379 0.860 0.373 0.032  -0.010 -0.024 58  SER CCC CB  
2949 O OG  . SER C 58  ? 0.394 0.872 0.393 0.031  -0.002 -0.031 58  SER CCC OG  
2950 N N   . SER C 59  ? 0.328 0.830 0.337 -0.002 -0.010 -0.018 59  SER CCC N   
2951 C CA  . SER C 59  ? 0.315 0.838 0.333 -0.009 -0.007 -0.012 59  SER CCC CA  
2952 C C   . SER C 59  ? 0.328 0.835 0.345 -0.018 -0.009 -0.006 59  SER CCC C   
2953 O O   . SER C 59  ? 0.353 0.840 0.360 -0.017 -0.009 -0.011 59  SER CCC O   
2954 C CB  . SER C 59  ? 0.314 0.850 0.328 -0.002 -0.001 -0.018 59  SER CCC CB  
2955 O OG  . SER C 59  ? 0.292 0.851 0.309 -0.006 0.002  -0.009 59  SER CCC OG  
2956 N N   . THR C 60  ? 0.331 0.847 0.361 -0.027 -0.011 0.004  60  THR CCC N   
2957 C CA  . THR C 60  ? 0.349 0.850 0.383 -0.035 -0.012 0.012  60  THR CCC CA  
2958 C C   . THR C 60  ? 0.347 0.867 0.388 -0.038 -0.005 0.028  60  THR CCC C   
2959 O O   . THR C 60  ? 0.355 0.904 0.403 -0.038 0.000  0.032  60  THR CCC O   
2960 C CB  . THR C 60  ? 0.364 0.849 0.409 -0.043 -0.020 0.008  60  THR CCC CB  
2961 O OG1 . THR C 60  ? 0.329 0.836 0.396 -0.050 -0.021 0.010  60  THR CCC OG1 
2962 C CG2 . THR C 60  ? 0.376 0.845 0.406 -0.036 -0.026 -0.006 60  THR CCC CG2 
2963 N N   . PHE C 61  ? 0.360 0.868 0.399 -0.040 -0.004 0.038  61  PHE CCC N   
2964 C CA  . PHE C 61  ? 0.378 0.900 0.418 -0.040 0.004  0.059  61  PHE CCC CA  
2965 C C   . PHE C 61  ? 0.378 0.872 0.426 -0.045 0.002  0.072  61  PHE CCC C   
2966 O O   . PHE C 61  ? 0.365 0.833 0.409 -0.043 -0.005 0.060  61  PHE CCC O   
2967 C CB  . PHE C 61  ? 0.380 0.925 0.399 -0.025 0.007  0.057  61  PHE CCC CB  
2968 C CG  . PHE C 61  ? 0.377 0.909 0.384 -0.017 0.001  0.039  61  PHE CCC CG  
2969 C CD1 . PHE C 61  ? 0.370 0.900 0.375 -0.015 -0.001 0.019  61  PHE CCC CD1 
2970 C CD2 . PHE C 61  ? 0.390 0.913 0.390 -0.011 -0.002 0.043  61  PHE CCC CD2 
2971 C CE1 . PHE C 61  ? 0.385 0.903 0.384 -0.011 -0.004 0.004  61  PHE CCC CE1 
2972 C CE2 . PHE C 61  ? 0.402 0.918 0.396 -0.005 -0.007 0.025  61  PHE CCC CE2 
2973 C CZ  . PHE C 61  ? 0.405 0.919 0.400 -0.007 -0.007 0.006  61  PHE CCC CZ  
2974 N N   . TYR C 62  ? 0.401 0.897 0.460 -0.051 0.011  0.096  62  TYR CCC N   
2975 C CA  . TYR C 62  ? 0.438 0.901 0.516 -0.060 0.011  0.110  62  TYR CCC CA  
2976 C C   . TYR C 62  ? 0.462 0.931 0.533 -0.054 0.022  0.142  62  TYR CCC C   
2977 O O   . TYR C 62  ? 0.471 0.974 0.534 -0.051 0.033  0.156  62  TYR CCC O   
2978 C CB  . TYR C 62  ? 0.443 0.900 0.556 -0.079 0.010  0.106  62  TYR CCC CB  
2979 C CG  . TYR C 62  ? 0.420 0.878 0.534 -0.081 -0.002 0.076  62  TYR CCC CG  
2980 C CD1 . TYR C 62  ? 0.406 0.897 0.517 -0.078 -0.001 0.067  62  TYR CCC CD1 
2981 C CD2 . TYR C 62  ? 0.422 0.851 0.537 -0.080 -0.013 0.058  62  TYR CCC CD2 
2982 C CE1 . TYR C 62  ? 0.397 0.888 0.505 -0.076 -0.012 0.044  62  TYR CCC CE1 
2983 C CE2 . TYR C 62  ? 0.414 0.847 0.524 -0.078 -0.023 0.034  62  TYR CCC CE2 
2984 C CZ  . TYR C 62  ? 0.400 0.863 0.506 -0.076 -0.022 0.028  62  TYR CCC CZ  
2985 O OH  . TYR C 62  ? 0.393 0.858 0.491 -0.070 -0.032 0.009  62  TYR CCC OH  
2986 N N   . SER C 63  ? 0.498 0.934 0.568 -0.049 0.020  0.155  63  SER CCC N   
2987 C CA  . SER C 63  ? 0.556 0.988 0.620 -0.042 0.032  0.191  63  SER CCC CA  
2988 C C   . SER C 63  ? 0.585 1.013 0.682 -0.063 0.046  0.214  63  SER CCC C   
2989 O O   . SER C 63  ? 0.561 0.978 0.691 -0.082 0.042  0.196  63  SER CCC O   
2990 C CB  . SER C 63  ? 0.577 0.971 0.637 -0.031 0.025  0.197  63  SER CCC CB  
2991 O OG  . SER C 63  ? 0.602 0.953 0.696 -0.047 0.022  0.193  63  SER CCC OG  
2992 N N   . ASP C 64  ? 0.617 1.059 0.707 -0.059 0.063  0.251  64  ASP CCC N   
2993 C CA  . ASP C 64  ? 0.661 1.104 0.785 -0.080 0.082  0.278  64  ASP CCC CA  
2994 C C   . ASP C 64  ? 0.678 1.068 0.848 -0.101 0.079  0.275  64  ASP CCC C   
2995 O O   . ASP C 64  ? 0.698 1.090 0.911 -0.126 0.087  0.276  64  ASP CCC O   
2996 C CB  . ASP C 64  ? 0.711 1.170 0.814 -0.069 0.103  0.324  64  ASP CCC CB  
2997 C CG  . ASP C 64  ? 0.701 1.222 0.768 -0.053 0.110  0.326  64  ASP CCC CG  
2998 O OD1 . ASP C 64  ? 0.663 1.211 0.723 -0.050 0.099  0.290  64  ASP CCC OD1 
2999 O OD2 . ASP C 64  ? 0.775 1.316 0.822 -0.041 0.128  0.363  64  ASP CCC OD2 
3000 N N   . SER C 65  ? 0.683 1.029 0.847 -0.091 0.067  0.269  65  SER CCC N   
3001 C CA  . SER C 65  ? 0.717 1.007 0.922 -0.105 0.064  0.270  65  SER CCC CA  
3002 C C   . SER C 65  ? 0.681 0.960 0.912 -0.119 0.046  0.224  65  SER CCC C   
3003 O O   . SER C 65  ? 0.704 0.941 0.974 -0.133 0.042  0.217  65  SER CCC O   
3004 C CB  . SER C 65  ? 0.754 1.004 0.939 -0.084 0.060  0.286  65  SER CCC CB  
3005 O OG  . SER C 65  ? 0.745 1.001 0.901 -0.065 0.041  0.255  65  SER CCC OG  
3006 N N   . VAL C 66  ? 0.627 0.941 0.837 -0.114 0.034  0.193  66  VAL CCC N   
3007 C CA  . VAL C 66  ? 0.608 0.918 0.836 -0.123 0.017  0.151  66  VAL CCC CA  
3008 C C   . VAL C 66  ? 0.585 0.940 0.819 -0.132 0.017  0.135  66  VAL CCC C   
3009 O O   . VAL C 66  ? 0.570 0.924 0.827 -0.143 0.004  0.105  66  VAL CCC O   
3010 C CB  . VAL C 66  ? 0.592 0.890 0.787 -0.103 0.001  0.126  66  VAL CCC CB  
3011 C CG1 . VAL C 66  ? 0.630 0.886 0.823 -0.091 -0.000 0.138  66  VAL CCC CG1 
3012 C CG2 . VAL C 66  ? 0.556 0.892 0.709 -0.087 0.001  0.122  66  VAL CCC CG2 
3013 N N   . LYS C 67  ? 0.590 0.986 0.805 -0.127 0.028  0.151  67  LYS CCC N   
3014 C CA  . LYS C 67  ? 0.578 1.018 0.799 -0.133 0.028  0.136  67  LYS CCC CA  
3015 C C   . LYS C 67  ? 0.578 1.020 0.855 -0.158 0.029  0.129  67  LYS CCC C   
3016 O O   . LYS C 67  ? 0.610 1.040 0.918 -0.173 0.043  0.155  67  LYS CCC O   
3017 C CB  . LYS C 67  ? 0.591 1.073 0.792 -0.124 0.044  0.159  67  LYS CCC CB  
3018 C CG  . LYS C 67  ? 0.575 1.103 0.777 -0.124 0.042  0.141  67  LYS CCC CG  
3019 C CD  . LYS C 67  ? 0.578 1.146 0.752 -0.110 0.055  0.156  67  LYS CCC CD  
3020 C CE  . LYS C 67  ? 0.561 1.172 0.741 -0.108 0.054  0.137  67  LYS CCC CE  
3021 N NZ  . LYS C 67  ? 0.547 1.195 0.696 -0.090 0.063  0.143  67  LYS CCC NZ  
3022 N N   . GLY C 68  ? 0.561 1.017 0.850 -0.161 0.013  0.095  68  GLY CCC N   
3023 C CA  . GLY C 68  ? 0.568 1.034 0.911 -0.184 0.009  0.079  68  GLY CCC CA  
3024 C C   . GLY C 68  ? 0.593 1.019 0.958 -0.191 -0.008 0.054  68  GLY CCC C   
3025 O O   . GLY C 68  ? 0.612 1.053 1.018 -0.205 -0.018 0.028  68  GLY CCC O   
3026 N N   . ARG C 69  ? 0.597 0.980 0.939 -0.180 -0.010 0.059  69  ARG CCC N   
3027 C CA  . ARG C 69  ? 0.609 0.952 0.968 -0.183 -0.026 0.034  69  ARG CCC CA  
3028 C C   . ARG C 69  ? 0.578 0.917 0.889 -0.160 -0.041 0.009  69  ARG CCC C   
3029 O O   . ARG C 69  ? 0.576 0.912 0.896 -0.159 -0.058 -0.025 69  ARG CCC O   
3030 C CB  . ARG C 69  ? 0.655 0.948 1.029 -0.187 -0.015 0.059  69  ARG CCC CB  
3031 C CG  . ARG C 69  ? 0.692 0.978 1.118 -0.212 0.003  0.086  69  ARG CCC CG  
3032 C CD  . ARG C 69  ? 0.742 0.969 1.188 -0.216 0.011  0.108  69  ARG CCC CD  
3033 N NE  . ARG C 69  ? 0.749 0.959 1.143 -0.190 0.017  0.135  69  ARG CCC NE  
3034 C CZ  . ARG C 69  ? 0.759 0.932 1.132 -0.172 0.006  0.125  69  ARG CCC CZ  
3035 N NH1 . ARG C 69  ? 0.766 0.912 1.163 -0.176 -0.011 0.088  69  ARG CCC NH1 
3036 N NH2 . ARG C 69  ? 0.761 0.929 1.089 -0.149 0.011  0.149  69  ARG CCC NH2 
3037 N N   . PHE C 70  ? 0.556 0.899 0.820 -0.141 -0.035 0.025  70  PHE CCC N   
3038 C CA  . PHE C 70  ? 0.527 0.870 0.748 -0.120 -0.045 0.008  70  PHE CCC CA  
3039 C C   . PHE C 70  ? 0.507 0.890 0.703 -0.112 -0.045 0.004  70  PHE CCC C   
3040 O O   . PHE C 70  ? 0.506 0.915 0.704 -0.116 -0.033 0.022  70  PHE CCC O   
3041 C CB  . PHE C 70  ? 0.529 0.851 0.721 -0.105 -0.038 0.026  70  PHE CCC CB  
3042 C CG  . PHE C 70  ? 0.550 0.828 0.760 -0.106 -0.040 0.029  70  PHE CCC CG  
3043 C CD1 . PHE C 70  ? 0.574 0.828 0.828 -0.122 -0.044 0.019  70  PHE CCC CD1 
3044 C CD2 . PHE C 70  ? 0.535 0.796 0.720 -0.089 -0.037 0.041  70  PHE CCC CD2 
3045 C CE1 . PHE C 70  ? 0.605 0.813 0.876 -0.120 -0.045 0.022  70  PHE CCC CE1 
3046 C CE2 . PHE C 70  ? 0.569 0.789 0.770 -0.085 -0.039 0.045  70  PHE CCC CE2 
3047 C CZ  . PHE C 70  ? 0.597 0.788 0.840 -0.101 -0.043 0.036  70  PHE CCC CZ  
3048 N N   . THR C 71  ? 0.495 0.883 0.666 -0.100 -0.056 -0.020 71  THR CCC N   
3049 C CA  . THR C 71  ? 0.478 0.895 0.622 -0.089 -0.056 -0.024 71  THR CCC CA  
3050 C C   . THR C 71  ? 0.449 0.853 0.555 -0.072 -0.057 -0.032 71  THR CCC C   
3051 O O   . THR C 71  ? 0.466 0.848 0.570 -0.069 -0.064 -0.046 71  THR CCC O   
3052 C CB  . THR C 71  ? 0.496 0.939 0.656 -0.092 -0.067 -0.042 71  THR CCC CB  
3053 O OG1 . THR C 71  ? 0.521 0.987 0.654 -0.079 -0.066 -0.042 71  THR CCC OG1 
3054 C CG2 . THR C 71  ? 0.518 0.950 0.681 -0.090 -0.083 -0.071 71  THR CCC CG2 
3055 N N   . VAL C 72  ? 0.416 0.831 0.496 -0.062 -0.050 -0.023 72  VAL CCC N   
3056 C CA  . VAL C 72  ? 0.412 0.819 0.461 -0.049 -0.048 -0.030 72  VAL CCC CA  
3057 C C   . VAL C 72  ? 0.410 0.833 0.444 -0.040 -0.051 -0.038 72  VAL CCC C   
3058 O O   . VAL C 72  ? 0.375 0.818 0.415 -0.042 -0.050 -0.032 72  VAL CCC O   
3059 C CB  . VAL C 72  ? 0.396 0.804 0.433 -0.044 -0.037 -0.017 72  VAL CCC CB  
3060 C CG1 . VAL C 72  ? 0.403 0.803 0.416 -0.033 -0.034 -0.025 72  VAL CCC CG1 
3061 C CG2 . VAL C 72  ? 0.417 0.813 0.466 -0.048 -0.035 -0.005 72  VAL CCC CG2 
3062 N N   . SER C 73  ? 0.421 0.835 0.434 -0.031 -0.055 -0.050 73  SER CCC N   
3063 C CA  . SER C 73  ? 0.438 0.862 0.427 -0.018 -0.056 -0.054 73  SER CCC CA  
3064 C C   . SER C 73  ? 0.441 0.850 0.403 -0.008 -0.047 -0.053 73  SER CCC C   
3065 O O   . SER C 73  ? 0.451 0.847 0.415 -0.011 -0.042 -0.054 73  SER CCC O   
3066 C CB  . SER C 73  ? 0.459 0.895 0.452 -0.015 -0.072 -0.071 73  SER CCC CB  
3067 O OG  . SER C 73  ? 0.494 0.917 0.476 -0.011 -0.076 -0.085 73  SER CCC OG  
3068 N N   . ARG C 74  ? 0.442 0.854 0.381 0.004  -0.043 -0.049 74  ARG CCC N   
3069 C CA  . ARG C 74  ? 0.442 0.840 0.357 0.012  -0.029 -0.044 74  ARG CCC CA  
3070 C C   . ARG C 74  ? 0.455 0.858 0.342 0.028  -0.032 -0.044 74  ARG CCC C   
3071 O O   . ARG C 74  ? 0.460 0.876 0.346 0.034  -0.042 -0.044 74  ARG CCC O   
3072 C CB  . ARG C 74  ? 0.451 0.843 0.371 0.009  -0.016 -0.032 74  ARG CCC CB  
3073 C CG  . ARG C 74  ? 0.459 0.837 0.370 0.010  0.000  -0.028 74  ARG CCC CG  
3074 C CD  . ARG C 74  ? 0.444 0.820 0.371 0.004  0.010  -0.024 74  ARG CCC CD  
3075 N NE  . ARG C 74  ? 0.436 0.808 0.359 0.010  0.014  -0.016 74  ARG CCC NE  
3076 C CZ  . ARG C 74  ? 0.428 0.795 0.365 0.006  0.022  -0.016 74  ARG CCC CZ  
3077 N NH1 . ARG C 74  ? 0.414 0.787 0.369 -0.003 0.025  -0.023 74  ARG CCC NH1 
3078 N NH2 . ARG C 74  ? 0.442 0.802 0.375 0.014  0.025  -0.010 74  ARG CCC NH2 
3079 N N   . ASN C 75  ? 0.468 0.862 0.330 0.036  -0.023 -0.044 75  ASN CCC N   
3080 C CA  . ASN C 75  ? 0.497 0.897 0.324 0.056  -0.023 -0.041 75  ASN CCC CA  
3081 C C   . ASN C 75  ? 0.508 0.896 0.320 0.064  -0.009 -0.019 75  ASN CCC C   
3082 O O   . ASN C 75  ? 0.462 0.838 0.295 0.053  0.001  -0.011 75  ASN CCC O   
3083 C CB  . ASN C 75  ? 0.516 0.914 0.321 0.062  -0.015 -0.046 75  ASN CCC CB  
3084 C CG  . ASN C 75  ? 0.505 0.887 0.311 0.056  0.009  -0.034 75  ASN CCC CG  
3085 O OD1 . ASN C 75  ? 0.466 0.838 0.294 0.045  0.017  -0.025 75  ASN CCC OD1 
3086 N ND2 . ASN C 75  ? 0.514 0.898 0.299 0.065  0.021  -0.035 75  ASN CCC ND2 
3087 N N   . ASN C 76  ? 0.560 0.953 0.340 0.085  -0.011 -0.011 76  ASN CCC N   
3088 C CA  . ASN C 76  ? 0.596 0.973 0.359 0.097  0.002  0.013  76  ASN CCC CA  
3089 C C   . ASN C 76  ? 0.590 0.940 0.355 0.089  0.029  0.028  76  ASN CCC C   
3090 O O   . ASN C 76  ? 0.584 0.915 0.360 0.087  0.040  0.042  76  ASN CCC O   
3091 C CB  . ASN C 76  ? 0.663 1.052 0.385 0.125  -0.005 0.020  76  ASN CCC CB  
3092 C CG  . ASN C 76  ? 0.693 1.111 0.420 0.134  -0.032 0.005  76  ASN CCC CG  
3093 O OD1 . ASN C 76  ? 0.700 1.129 0.464 0.118  -0.044 -0.009 76  ASN CCC OD1 
3094 N ND2 . ASN C 76  ? 0.741 1.177 0.432 0.160  -0.042 0.007  76  ASN CCC ND2 
3095 N N   . ALA C 77  ? 0.586 0.937 0.344 0.085  0.039  0.024  77  ALA CCC N   
3096 C CA  . ALA C 77  ? 0.589 0.921 0.354 0.074  0.066  0.035  77  ALA CCC CA  
3097 C C   . ALA C 77  ? 0.549 0.875 0.358 0.053  0.068  0.027  77  ALA CCC C   
3098 O O   . ALA C 77  ? 0.560 0.868 0.384 0.044  0.088  0.036  77  ALA CCC O   
3099 C CB  . ALA C 77  ? 0.596 0.940 0.347 0.076  0.073  0.028  77  ALA CCC CB  
3100 N N   . LYS C 78  ? 0.520 0.860 0.349 0.045  0.048  0.010  78  LYS CCC N   
3101 C CA  . LYS C 78  ? 0.493 0.834 0.359 0.028  0.046  0.001  78  LYS CCC CA  
3102 C C   . LYS C 78  ? 0.476 0.820 0.358 0.017  0.055  -0.008 78  LYS CCC C   
3103 O O   . LYS C 78  ? 0.427 0.771 0.337 0.005  0.059  -0.013 78  LYS CCC O   
3104 C CB  . LYS C 78  ? 0.516 0.841 0.395 0.025  0.056  0.010  78  LYS CCC CB  
3105 C CG  . LYS C 78  ? 0.557 0.876 0.420 0.040  0.051  0.022  78  LYS CCC CG  
3106 C CD  . LYS C 78  ? 0.589 0.891 0.470 0.038  0.059  0.026  78  LYS CCC CD  
3107 C CE  . LYS C 78  ? 0.665 0.952 0.527 0.057  0.060  0.042  78  LYS CCC CE  
3108 N NZ  . LYS C 78  ? 0.709 0.980 0.594 0.056  0.065  0.041  78  LYS CCC NZ  
3109 N N   . ASP C 79  ? 0.473 0.823 0.339 0.022  0.058  -0.011 79  ASP CCC N   
3110 C CA  . ASP C 79  ? 0.473 0.830 0.354 0.015  0.068  -0.021 79  ASP CCC CA  
3111 C C   . ASP C 79  ? 0.460 0.828 0.345 0.016  0.050  -0.038 79  ASP CCC C   
3112 O O   . ASP C 79  ? 0.462 0.837 0.363 0.012  0.054  -0.047 79  ASP CCC O   
3113 C CB  . ASP C 79  ? 0.501 0.856 0.364 0.021  0.090  -0.011 79  ASP CCC CB  
3114 C CG  . ASP C 79  ? 0.530 0.889 0.351 0.039  0.087  -0.007 79  ASP CCC CG  
3115 O OD1 . ASP C 79  ? 0.493 0.861 0.306 0.045  0.065  -0.020 79  ASP CCC OD1 
3116 O OD2 . ASP C 79  ? 0.575 0.932 0.374 0.046  0.107  0.007  79  ASP CCC OD2 
3117 N N   . THR C 80  ? 0.465 0.836 0.340 0.021  0.032  -0.042 80  THR CCC N   
3118 C CA  . THR C 80  ? 0.468 0.843 0.352 0.021  0.014  -0.058 80  THR CCC CA  
3119 C C   . THR C 80  ? 0.455 0.831 0.356 0.014  -0.002 -0.058 80  THR CCC C   
3120 O O   . THR C 80  ? 0.470 0.848 0.361 0.018  -0.007 -0.052 80  THR CCC O   
3121 C CB  . THR C 80  ? 0.508 0.890 0.367 0.035  0.008  -0.069 80  THR CCC CB  
3122 O OG1 . THR C 80  ? 0.521 0.906 0.358 0.043  0.028  -0.063 80  THR CCC OG1 
3123 C CG2 . THR C 80  ? 0.513 0.895 0.386 0.034  -0.005 -0.089 80  THR CCC CG2 
3124 N N   . VAL C 81  ? 0.451 0.825 0.376 0.006  -0.008 -0.062 81  VAL CCC N   
3125 C CA  . VAL C 81  ? 0.444 0.820 0.388 -0.002 -0.020 -0.059 81  VAL CCC CA  
3126 C C   . VAL C 81  ? 0.438 0.808 0.393 -0.003 -0.032 -0.071 81  VAL CCC C   
3127 O O   . VAL C 81  ? 0.484 0.846 0.440 0.001  -0.031 -0.079 81  VAL CCC O   
3128 C CB  . VAL C 81  ? 0.451 0.829 0.411 -0.009 -0.014 -0.050 81  VAL CCC CB  
3129 C CG1 . VAL C 81  ? 0.476 0.856 0.453 -0.016 -0.023 -0.044 81  VAL CCC CG1 
3130 C CG2 . VAL C 81  ? 0.450 0.832 0.404 -0.009 -0.003 -0.043 81  VAL CCC CG2 
3131 N N   . TYR C 82  ? 0.434 0.806 0.401 -0.009 -0.044 -0.073 82  TYR CCC N   
3132 C CA  . TYR C 82  ? 0.457 0.820 0.442 -0.012 -0.057 -0.087 82  TYR CCC CA  
3133 C C   . TYR C 82  ? 0.468 0.827 0.483 -0.026 -0.059 -0.075 82  TYR CCC C   
3134 O O   . TYR C 82  ? 0.435 0.807 0.454 -0.031 -0.056 -0.063 82  TYR CCC O   
3135 C CB  . TYR C 82  ? 0.468 0.843 0.447 -0.008 -0.069 -0.103 82  TYR CCC CB  
3136 C CG  . TYR C 82  ? 0.480 0.862 0.422 0.008  -0.065 -0.110 82  TYR CCC CG  
3137 C CD1 . TYR C 82  ? 0.506 0.884 0.437 0.018  -0.065 -0.126 82  TYR CCC CD1 
3138 C CD2 . TYR C 82  ? 0.465 0.859 0.384 0.015  -0.059 -0.098 82  TYR CCC CD2 
3139 C CE1 . TYR C 82  ? 0.523 0.912 0.419 0.033  -0.058 -0.129 82  TYR CCC CE1 
3140 C CE2 . TYR C 82  ? 0.491 0.890 0.375 0.031  -0.052 -0.099 82  TYR CCC CE2 
3141 C CZ  . TYR C 82  ? 0.524 0.922 0.395 0.040  -0.051 -0.113 82  TYR CCC CZ  
3142 O OH  . TYR C 82  ? 0.563 0.970 0.398 0.056  -0.042 -0.112 82  TYR CCC OH  
3143 N N   . LEU C 83  ? 0.485 0.825 0.519 -0.029 -0.062 -0.077 83  LEU CCC N   
3144 C CA  . LEU C 83  ? 0.495 0.826 0.559 -0.042 -0.063 -0.064 83  LEU CCC CA  
3145 C C   . LEU C 83  ? 0.527 0.848 0.616 -0.050 -0.076 -0.082 83  LEU CCC C   
3146 O O   . LEU C 83  ? 0.550 0.850 0.646 -0.045 -0.082 -0.098 83  LEU CCC O   
3147 C CB  . LEU C 83  ? 0.508 0.820 0.577 -0.038 -0.058 -0.051 83  LEU CCC CB  
3148 C CG  . LEU C 83  ? 0.518 0.819 0.613 -0.049 -0.056 -0.030 83  LEU CCC CG  
3149 C CD1 . LEU C 83  ? 0.502 0.828 0.593 -0.055 -0.048 -0.011 83  LEU CCC CD1 
3150 C CD2 . LEU C 83  ? 0.524 0.804 0.620 -0.040 -0.053 -0.018 83  LEU CCC CD2 
3151 N N   . HIS C 84  ? 0.520 0.859 0.625 -0.060 -0.080 -0.084 84  HIS CCC N   
3152 C CA  . HIS C 84  ? 0.527 0.863 0.667 -0.071 -0.093 -0.104 84  HIS CCC CA  
3153 C C   . HIS C 84  ? 0.561 0.875 0.741 -0.088 -0.087 -0.087 84  HIS CCC C   
3154 O O   . HIS C 84  ? 0.542 0.870 0.732 -0.098 -0.078 -0.064 84  HIS CCC O   
3155 C CB  . HIS C 84  ? 0.494 0.865 0.637 -0.074 -0.100 -0.113 84  HIS CCC CB  
3156 C CG  . HIS C 84  ? 0.472 0.862 0.572 -0.056 -0.103 -0.121 84  HIS CCC CG  
3157 N ND1 . HIS C 84  ? 0.471 0.866 0.555 -0.043 -0.115 -0.148 84  HIS CCC ND1 
3158 C CD2 . HIS C 84  ? 0.438 0.840 0.508 -0.046 -0.093 -0.104 84  HIS CCC CD2 
3159 C CE1 . HIS C 84  ? 0.455 0.865 0.498 -0.027 -0.112 -0.143 84  HIS CCC CE1 
3160 N NE2 . HIS C 84  ? 0.425 0.838 0.462 -0.030 -0.098 -0.117 84  HIS CCC NE2 
3161 N N   . MET C 85  ? 0.618 0.898 0.817 -0.090 -0.092 -0.096 85  MET CCC N   
3162 C CA  . MET C 85  ? 0.657 0.907 0.895 -0.104 -0.085 -0.077 85  MET CCC CA  
3163 C C   . MET C 85  ? 0.663 0.904 0.952 -0.123 -0.095 -0.099 85  MET CCC C   
3164 O O   . MET C 85  ? 0.698 0.921 0.999 -0.119 -0.108 -0.130 85  MET CCC O   
3165 C CB  . MET C 85  ? 0.709 0.921 0.938 -0.090 -0.083 -0.074 85  MET CCC CB  
3166 C CG  . MET C 85  ? 0.695 0.919 0.879 -0.071 -0.077 -0.062 85  MET CCC CG  
3167 S SD  . MET C 85  ? 0.740 0.928 0.921 -0.055 -0.074 -0.050 85  MET CCC SD  
3168 C CE  . MET C 85  ? 0.776 0.940 0.971 -0.049 -0.089 -0.093 85  MET CCC CE  
3169 N N   . ASN C 86  ? 0.652 0.911 0.972 -0.142 -0.088 -0.085 86  ASN CCC N   
3170 C CA  . ASN C 86  ? 0.661 0.920 1.041 -0.165 -0.096 -0.105 86  ASN CCC CA  
3171 C C   . ASN C 86  ? 0.691 0.919 1.115 -0.186 -0.079 -0.073 86  ASN CCC C   
3172 O O   . ASN C 86  ? 0.683 0.907 1.085 -0.180 -0.062 -0.033 86  ASN CCC O   
3173 C CB  . ASN C 86  ? 0.631 0.943 1.018 -0.172 -0.102 -0.117 86  ASN CCC CB  
3174 C CG  . ASN C 86  ? 0.597 0.939 0.934 -0.149 -0.115 -0.140 86  ASN CCC CG  
3175 O OD1 . ASN C 86  ? 0.614 0.951 0.944 -0.139 -0.131 -0.174 86  ASN CCC OD1 
3176 N ND2 . ASN C 86  ? 0.566 0.937 0.867 -0.139 -0.107 -0.120 86  ASN CCC ND2 
3177 N N   . SER C 87  ? 0.744 0.953 1.231 -0.207 -0.084 -0.091 87  SER CCC N   
3178 C CA  . SER C 87  ? 0.801 0.977 1.341 -0.231 -0.067 -0.061 87  SER CCC CA  
3179 C C   . SER C 87  ? 0.845 0.972 1.359 -0.216 -0.054 -0.026 87  SER CCC C   
3180 O O   . SER C 87  ? 0.860 0.982 1.369 -0.219 -0.033 0.021  87  SER CCC O   
3181 C CB  . SER C 87  ? 0.784 0.999 1.340 -0.248 -0.049 -0.032 87  SER CCC CB  
3182 O OG  . SER C 87  ? 0.760 1.027 1.335 -0.256 -0.063 -0.066 87  SER CCC OG  
3183 N N   . LEU C 88  ? 0.876 0.971 1.372 -0.198 -0.068 -0.049 88  LEU CCC N   
3184 C CA  . LEU C 88  ? 0.911 0.967 1.375 -0.176 -0.061 -0.023 88  LEU CCC CA  
3185 C C   . LEU C 88  ? 0.984 0.982 1.495 -0.189 -0.048 0.004  88  LEU CCC C   
3186 O O   . LEU C 88  ? 1.010 0.979 1.580 -0.208 -0.054 -0.020 88  LEU CCC O   
3187 C CB  . LEU C 88  ? 0.902 0.949 1.337 -0.152 -0.079 -0.062 88  LEU CCC CB  
3188 C CG  . LEU C 88  ? 0.846 0.940 1.219 -0.132 -0.084 -0.070 88  LEU CCC CG  
3189 C CD1 . LEU C 88  ? 0.841 0.937 1.197 -0.115 -0.102 -0.115 88  LEU CCC CD1 
3190 C CD2 . LEU C 88  ? 0.837 0.931 1.168 -0.114 -0.071 -0.031 88  LEU CCC CD2 
3191 N N   . LYS C 89  ? 1.025 1.007 1.512 -0.177 -0.030 0.054  89  LYS CCC N   
3192 C CA  . LYS C 89  ? 1.104 1.027 1.622 -0.182 -0.014 0.093  89  LYS CCC CA  
3193 C C   . LYS C 89  ? 1.129 1.009 1.623 -0.152 -0.023 0.091  89  LYS CCC C   
3194 O O   . LYS C 89  ? 1.078 0.984 1.524 -0.128 -0.035 0.071  89  LYS CCC O   
3195 C CB  . LYS C 89  ? 1.114 1.056 1.613 -0.184 0.010  0.151  89  LYS CCC CB  
3196 C CG  . LYS C 89  ? 1.089 1.079 1.609 -0.210 0.022  0.158  89  LYS CCC CG  
3197 C CD  . LYS C 89  ? 1.075 1.101 1.553 -0.201 0.042  0.206  89  LYS CCC CD  
3198 C CE  . LYS C 89  ? 1.058 1.135 1.560 -0.225 0.056  0.213  89  LYS CCC CE  
3199 N NZ  . LYS C 89  ? 1.113 1.160 1.686 -0.258 0.073  0.232  89  LYS CCC NZ  
3200 N N   . PRO C 90  ? 1.192 1.006 1.719 -0.151 -0.015 0.114  90  PRO CCC N   
3201 C CA  . PRO C 90  ? 1.208 0.984 1.708 -0.118 -0.020 0.122  90  PRO CCC CA  
3202 C C   . PRO C 90  ? 1.172 0.982 1.607 -0.091 -0.012 0.162  90  PRO CCC C   
3203 O O   . PRO C 90  ? 1.154 0.965 1.554 -0.062 -0.022 0.152  90  PRO CCC O   
3204 C CB  . PRO C 90  ? 1.290 0.989 1.843 -0.127 -0.008 0.149  90  PRO CCC CB  
3205 C CG  . PRO C 90  ? 1.301 1.007 1.896 -0.164 0.012  0.176  90  PRO CCC CG  
3206 C CD  . PRO C 90  ? 1.241 1.011 1.836 -0.182 -0.001 0.132  90  PRO CCC CD  
3207 N N   . GLU C 91  ? 1.155 0.996 1.579 -0.102 0.006  0.202  91  GLU CCC N   
3208 C CA  . GLU C 91  ? 1.124 1.006 1.489 -0.079 0.015  0.237  91  GLU CCC CA  
3209 C C   . GLU C 91  ? 1.015 0.954 1.335 -0.065 -0.001 0.201  91  GLU CCC C   
3210 O O   . GLU C 91  ? 0.981 0.948 1.253 -0.040 -0.001 0.218  91  GLU CCC O   
3211 C CB  . GLU C 91  ? 1.161 1.070 1.529 -0.099 0.037  0.278  91  GLU CCC CB  
3212 C CG  . GLU C 91  ? 1.177 1.123 1.489 -0.074 0.048  0.319  91  GLU CCC CG  
3213 C CD  . GLU C 91  ? 1.210 1.179 1.524 -0.089 0.073  0.365  91  GLU CCC CD  
3214 O OE1 . GLU C 91  ? 1.248 1.178 1.610 -0.112 0.090  0.389  91  GLU CCC OE1 
3215 O OE2 . GLU C 91  ? 1.192 1.217 1.461 -0.078 0.077  0.375  91  GLU CCC OE2 
3216 N N   . ASP C 92  ? 0.965 0.919 1.299 -0.079 -0.015 0.153  92  ASP CCC N   
3217 C CA  . ASP C 92  ? 0.892 0.896 1.187 -0.067 -0.027 0.119  92  ASP CCC CA  
3218 C C   . ASP C 92  ? 0.880 0.868 1.159 -0.042 -0.041 0.093  92  ASP CCC C   
3219 O O   . ASP C 92  ? 0.829 0.856 1.074 -0.029 -0.049 0.072  92  ASP CCC O   
3220 C CB  . ASP C 92  ? 0.863 0.892 1.177 -0.090 -0.035 0.081  92  ASP CCC CB  
3221 C CG  . ASP C 92  ? 0.859 0.920 1.184 -0.112 -0.023 0.101  92  ASP CCC CG  
3222 O OD1 . ASP C 92  ? 0.847 0.939 1.141 -0.105 -0.011 0.131  92  ASP CCC OD1 
3223 O OD2 . ASP C 92  ? 0.875 0.935 1.242 -0.136 -0.025 0.082  92  ASP CCC OD2 
3224 N N   . THR C 93  ? 0.996 0.842 1.046 -0.115 0.046  -0.038 93  THR CCC N   
3225 C CA  . THR C 93  ? 1.010 0.828 1.047 -0.084 0.052  -0.051 93  THR CCC CA  
3226 C C   . THR C 93  ? 0.960 0.811 1.001 -0.049 0.052  -0.025 93  THR CCC C   
3227 O O   . THR C 93  ? 0.969 0.806 1.015 -0.039 0.055  0.005  93  THR CCC O   
3228 C CB  . THR C 93  ? 1.098 0.828 1.130 -0.083 0.065  -0.058 93  THR CCC CB  
3229 O OG1 . THR C 93  ? 1.133 0.840 1.162 -0.119 0.062  -0.088 93  THR CCC OG1 
3230 C CG2 . THR C 93  ? 1.129 0.830 1.153 -0.046 0.074  -0.069 93  THR CCC CG2 
3231 N N   . ALA C 94  ? 0.905 0.798 0.944 -0.031 0.050  -0.038 94  ALA CCC N   
3232 C CA  . ALA C 94  ? 0.852 0.788 0.902 -0.001 0.049  -0.021 94  ALA CCC CA  
3233 C C   . ALA C 94  ? 0.821 0.792 0.867 0.010  0.052  -0.044 94  ALA CCC C   
3234 O O   . ALA C 94  ? 0.844 0.808 0.871 -0.007 0.053  -0.069 94  ALA CCC O   
3235 C CB  . ALA C 94  ? 0.798 0.782 0.854 -0.011 0.039  0.004  94  ALA CCC CB  
3236 N N   . VAL C 95  ? 0.774 0.781 0.837 0.036  0.054  -0.034 95  VAL CCC N   
3237 C CA  . VAL C 95  ? 0.726 0.779 0.790 0.042  0.060  -0.049 95  VAL CCC CA  
3238 C C   . VAL C 95  ? 0.664 0.769 0.725 0.025  0.048  -0.037 95  VAL CCC C   
3239 O O   . VAL C 95  ? 0.640 0.768 0.716 0.030  0.040  -0.014 95  VAL CCC O   
3240 C CB  . VAL C 95  ? 0.718 0.791 0.811 0.076  0.068  -0.046 95  VAL CCC CB  
3241 C CG1 . VAL C 95  ? 0.685 0.806 0.782 0.078  0.078  -0.060 95  VAL CCC CG1 
3242 C CG2 . VAL C 95  ? 0.779 0.799 0.876 0.097  0.080  -0.058 95  VAL CCC CG2 
3243 N N   . TYR C 96  ? 0.650 0.769 0.690 0.008  0.048  -0.053 96  TYR CCC N   
3244 C CA  . TYR C 96  ? 0.592 0.754 0.626 -0.007 0.038  -0.044 96  TYR CCC CA  
3245 C C   . TYR C 96  ? 0.553 0.752 0.590 0.003  0.046  -0.047 96  TYR CCC C   
3246 O O   . TYR C 96  ? 0.578 0.768 0.604 0.011  0.061  -0.065 96  TYR CCC O   
3247 C CB  . TYR C 96  ? 0.607 0.759 0.616 -0.030 0.029  -0.057 96  TYR CCC CB  
3248 C CG  . TYR C 96  ? 0.629 0.760 0.647 -0.047 0.020  -0.050 96  TYR CCC CG  
3249 C CD1 . TYR C 96  ? 0.688 0.769 0.708 -0.049 0.025  -0.057 96  TYR CCC CD1 
3250 C CD2 . TYR C 96  ? 0.605 0.765 0.629 -0.063 0.009  -0.037 96  TYR CCC CD2 
3251 C CE1 . TYR C 96  ? 0.721 0.779 0.749 -0.068 0.020  -0.050 96  TYR CCC CE1 
3252 C CE2 . TYR C 96  ? 0.630 0.774 0.666 -0.081 0.005  -0.030 96  TYR CCC CE2 
3253 C CZ  . TYR C 96  ? 0.687 0.780 0.726 -0.085 0.011  -0.036 96  TYR CCC CZ  
3254 O OH  . TYR C 96  ? 0.724 0.798 0.776 -0.106 0.011  -0.029 96  TYR CCC OH  
3255 N N   . TYR C 97  ? 0.503 0.742 0.554 0.003  0.040  -0.031 97  TYR CCC N   
3256 C CA  . TYR C 97  ? 0.479 0.755 0.537 0.007  0.048  -0.031 97  TYR CCC CA  
3257 C C   . TYR C 97  ? 0.462 0.758 0.503 -0.009 0.040  -0.025 97  TYR CCC C   
3258 O O   . TYR C 97  ? 0.479 0.778 0.521 -0.017 0.026  -0.013 97  TYR CCC O   
3259 C CB  . TYR C 97  ? 0.453 0.757 0.548 0.023  0.046  -0.019 97  TYR CCC CB  
3260 C CG  . TYR C 97  ? 0.465 0.755 0.584 0.044  0.051  -0.022 97  TYR CCC CG  
3261 C CD1 . TYR C 97  ? 0.488 0.748 0.608 0.051  0.041  -0.010 97  TYR CCC CD1 
3262 C CD2 . TYR C 97  ? 0.470 0.774 0.611 0.059  0.067  -0.035 97  TYR CCC CD2 
3263 C CE1 . TYR C 97  ? 0.516 0.755 0.655 0.075  0.045  -0.010 97  TYR CCC CE1 
3264 C CE2 . TYR C 97  ? 0.494 0.786 0.661 0.083  0.071  -0.038 97  TYR CCC CE2 
3265 C CZ  . TYR C 97  ? 0.519 0.776 0.683 0.093  0.059  -0.025 97  TYR CCC CZ  
3266 O OH  . TYR C 97  ? 0.549 0.789 0.736 0.120  0.062  -0.025 97  TYR CCC OH  
3267 N N   . CYS C 98  ? 0.460 0.769 0.487 -0.011 0.050  -0.031 98  CYS CCC N   
3268 C CA  . CYS C 98  ? 0.442 0.771 0.457 -0.021 0.044  -0.023 98  CYS CCC CA  
3269 C C   . CYS C 98  ? 0.401 0.760 0.442 -0.018 0.052  -0.019 98  CYS CCC C   
3270 O O   . CYS C 98  ? 0.401 0.768 0.466 -0.008 0.065  -0.025 98  CYS CCC O   
3271 C CB  . CYS C 98  ? 0.489 0.803 0.463 -0.028 0.048  -0.031 98  CYS CCC CB  
3272 S SG  . CYS C 98  ? 0.560 0.863 0.516 -0.022 0.076  -0.046 98  CYS CCC SG  
3273 N N   . ALA C 99  ? 0.355 0.731 0.395 -0.025 0.045  -0.009 99  ALA CCC N   
3274 C CA  . ALA C 99  ? 0.345 0.749 0.409 -0.026 0.050  -0.007 99  ALA CCC CA  
3275 C C   . ALA C 99  ? 0.324 0.730 0.370 -0.035 0.046  -0.001 99  ALA CCC C   
3276 O O   . ALA C 99  ? 0.327 0.719 0.349 -0.038 0.037  0.004  99  ALA CCC O   
3277 C CB  . ALA C 99  ? 0.333 0.757 0.431 -0.017 0.038  -0.001 99  ALA CCC CB  
3278 N N   . ILE C 100 ? 0.330 0.754 0.392 -0.040 0.052  -0.002 100 ILE CCC N   
3279 C CA  . ILE C 100 ? 0.337 0.760 0.384 -0.049 0.050  0.002  100 ILE CCC CA  
3280 C C   . ILE C 100 ? 0.328 0.778 0.403 -0.050 0.040  0.003  100 ILE CCC C   
3281 O O   . ILE C 100 ? 0.341 0.813 0.448 -0.045 0.037  -0.002 100 ILE CCC O   
3282 C CB  . ILE C 100 ? 0.367 0.774 0.396 -0.057 0.071  -0.001 100 ILE CCC CB  
3283 C CG1 . ILE C 100 ? 0.370 0.795 0.432 -0.061 0.089  -0.011 100 ILE CCC CG1 
3284 C CG2 . ILE C 100 ? 0.399 0.775 0.385 -0.053 0.075  0.001  100 ILE CCC CG2 
3285 C CD1 . ILE C 100 ? 0.388 0.798 0.437 -0.073 0.113  -0.013 100 ILE CCC CD1 
3286 N N   . THR C 101 ? 0.326 0.773 0.387 -0.055 0.033  0.007  101 THR CCC N   
3287 C CA  . THR C 101 ? 0.320 0.789 0.397 -0.057 0.023  0.004  101 THR CCC CA  
3288 C C   . THR C 101 ? 0.334 0.792 0.400 -0.068 0.031  -0.001 101 THR CCC C   
3289 O O   . THR C 101 ? 0.373 0.804 0.410 -0.068 0.038  0.004  101 THR CCC O   
3290 C CB  . THR C 101 ? 0.312 0.785 0.380 -0.050 0.007  0.014  101 THR CCC CB  
3291 O OG1 . THR C 101 ? 0.321 0.813 0.397 -0.051 -0.003 0.010  101 THR CCC OG1 
3292 C CG2 . THR C 101 ? 0.317 0.770 0.357 -0.049 0.007  0.021  101 THR CCC CG2 
3293 N N   . THR C 102 ? 0.325 0.801 0.414 -0.077 0.030  -0.011 102 THR CCC N   
3294 C CA  . THR C 102 ? 0.342 0.806 0.422 -0.089 0.035  -0.018 102 THR CCC CA  
3295 C C   . THR C 102 ? 0.345 0.811 0.408 -0.083 0.020  -0.017 102 THR CCC C   
3296 O O   . THR C 102 ? 0.355 0.802 0.401 -0.089 0.024  -0.022 102 THR CCC O   
3297 C CB  . THR C 102 ? 0.338 0.823 0.454 -0.104 0.040  -0.035 102 THR CCC CB  
3298 O OG1 . THR C 102 ? 0.323 0.849 0.466 -0.099 0.019  -0.040 102 THR CCC OG1 
3299 C CG2 . THR C 102 ? 0.332 0.818 0.467 -0.112 0.062  -0.037 102 THR CCC CG2 
3300 N N   . ILE C 103 ? 0.333 0.817 0.397 -0.072 0.004  -0.010 103 ILE CCC N   
3301 C CA  . ILE C 103 ? 0.330 0.818 0.375 -0.066 -0.009 -0.007 103 ILE CCC CA  
3302 C C   . ILE C 103 ? 0.330 0.797 0.349 -0.059 -0.003 0.004  103 ILE CCC C   
3303 O O   . ILE C 103 ? 0.323 0.789 0.343 -0.053 -0.003 0.015  103 ILE CCC O   
3304 C CB  . ILE C 103 ? 0.344 0.857 0.397 -0.057 -0.025 -0.002 103 ILE CCC CB  
3305 C CG1 . ILE C 103 ? 0.348 0.891 0.435 -0.060 -0.035 -0.014 103 ILE CCC CG1 
3306 C CG2 . ILE C 103 ? 0.365 0.878 0.390 -0.051 -0.035 0.002  103 ILE CCC CG2 
3307 C CD1 . ILE C 103 ? 0.355 0.920 0.448 -0.046 -0.054 -0.007 103 ILE CCC CD1 
3308 N N   . VAL C 104 ? 0.336 0.788 0.337 -0.060 0.002  -0.000 104 VAL CCC N   
3309 C CA  . VAL C 104 ? 0.325 0.764 0.308 -0.051 0.007  0.008  104 VAL CCC CA  
3310 C C   . VAL C 104 ? 0.336 0.788 0.307 -0.046 0.002  0.011  104 VAL CCC C   
3311 O O   . VAL C 104 ? 0.362 0.811 0.319 -0.047 0.002  0.001  104 VAL CCC O   
3312 C CB  . VAL C 104 ? 0.344 0.755 0.313 -0.052 0.018  0.003  104 VAL CCC CB  
3313 C CG1 . VAL C 104 ? 0.332 0.737 0.291 -0.039 0.021  0.012  104 VAL CCC CG1 
3314 C CG2 . VAL C 104 ? 0.356 0.749 0.329 -0.059 0.027  0.001  104 VAL CCC CG2 
3315 N N   . ARG C 105 ? 0.334 0.797 0.309 -0.041 -0.001 0.024  105 ARG CCC N   
3316 C CA  . ARG C 105 ? 0.352 0.824 0.314 -0.037 -0.001 0.031  105 ARG CCC CA  
3317 C C   . ARG C 105 ? 0.362 0.833 0.326 -0.032 0.009  0.037  105 ARG CCC C   
3318 O O   . ARG C 105 ? 0.349 0.822 0.329 -0.033 0.008  0.043  105 ARG CCC O   
3319 C CB  . ARG C 105 ? 0.342 0.822 0.308 -0.036 -0.009 0.043  105 ARG CCC CB  
3320 C CG  . ARG C 105 ? 0.337 0.824 0.310 -0.036 -0.021 0.038  105 ARG CCC CG  
3321 C CD  . ARG C 105 ? 0.358 0.848 0.328 -0.030 -0.029 0.052  105 ARG CCC CD  
3322 N NE  . ARG C 105 ? 0.364 0.866 0.345 -0.026 -0.043 0.049  105 ARG CCC NE  
3323 C CZ  . ARG C 105 ? 0.354 0.871 0.324 -0.024 -0.056 0.040  105 ARG CCC CZ  
3324 N NH1 . ARG C 105 ? 0.356 0.871 0.299 -0.026 -0.054 0.033  105 ARG CCC NH1 
3325 N NH2 . ARG C 105 ? 0.367 0.901 0.356 -0.018 -0.072 0.037  105 ARG CCC NH2 
3326 N N   . ALA C 106 ? 0.373 0.845 0.324 -0.027 0.017  0.032  106 ALA CCC N   
3327 C CA  . ALA C 106 ? 0.349 0.828 0.308 -0.020 0.027  0.035  106 ALA CCC CA  
3328 C C   . ALA C 106 ? 0.354 0.850 0.328 -0.024 0.029  0.048  106 ALA CCC C   
3329 O O   . ALA C 106 ? 0.401 0.910 0.398 -0.022 0.031  0.051  106 ALA CCC O   
3330 C CB  . ALA C 106 ? 0.362 0.839 0.303 -0.012 0.037  0.027  106 ALA CCC CB  
3331 N N   . TYR C 107 ? 0.345 0.843 0.306 -0.028 0.028  0.056  107 TYR CCC N   
3332 C CA  . TYR C 107 ? 0.338 0.842 0.308 -0.035 0.032  0.070  107 TYR CCC CA  
3333 C C   . TYR C 107 ? 0.313 0.806 0.293 -0.039 0.020  0.074  107 TYR CCC C   
3334 O O   . TYR C 107 ? 0.322 0.807 0.286 -0.037 0.011  0.076  107 TYR CCC O   
3335 C CB  . TYR C 107 ? 0.374 0.876 0.315 -0.034 0.041  0.079  107 TYR CCC CB  
3336 C CG  . TYR C 107 ? 0.399 0.911 0.327 -0.029 0.058  0.074  107 TYR CCC CG  
3337 C CD1 . TYR C 107 ? 0.407 0.912 0.309 -0.021 0.056  0.060  107 TYR CCC CD1 
3338 C CD2 . TYR C 107 ? 0.396 0.924 0.340 -0.032 0.077  0.082  107 TYR CCC CD2 
3339 C CE1 . TYR C 107 ? 0.427 0.938 0.315 -0.015 0.074  0.054  107 TYR CCC CE1 
3340 C CE2 . TYR C 107 ? 0.425 0.964 0.361 -0.025 0.095  0.076  107 TYR CCC CE2 
3341 C CZ  . TYR C 107 ? 0.445 0.975 0.350 -0.015 0.094  0.062  107 TYR CCC CZ  
3342 O OH  . TYR C 107 ? 0.485 1.023 0.379 -0.007 0.115  0.054  107 TYR CCC OH  
3343 N N   . TYR C 108 ? 0.290 0.784 0.293 -0.044 0.017  0.075  108 TYR CCC N   
3344 C CA  . TYR C 108 ? 0.295 0.776 0.307 -0.048 0.008  0.076  108 TYR CCC CA  
3345 C C   . TYR C 108 ? 0.310 0.780 0.316 -0.050 0.010  0.089  108 TYR CCC C   
3346 O O   . TYR C 108 ? 0.303 0.760 0.309 -0.048 0.002  0.090  108 TYR CCC O   
3347 C CB  . TYR C 108 ? 0.283 0.767 0.317 -0.053 0.006  0.071  108 TYR CCC CB  
3348 C CG  . TYR C 108 ? 0.289 0.778 0.341 -0.063 0.011  0.078  108 TYR CCC CG  
3349 C CD1 . TYR C 108 ? 0.304 0.773 0.358 -0.070 0.010  0.084  108 TYR CCC CD1 
3350 C CD2 . TYR C 108 ? 0.297 0.809 0.366 -0.067 0.020  0.079  108 TYR CCC CD2 
3351 C CE1 . TYR C 108 ? 0.343 0.810 0.414 -0.083 0.018  0.090  108 TYR CCC CE1 
3352 C CE2 . TYR C 108 ? 0.321 0.839 0.412 -0.081 0.028  0.084  108 TYR CCC CE2 
3353 C CZ  . TYR C 108 ? 0.344 0.838 0.435 -0.091 0.027  0.090  108 TYR CCC CZ  
3354 O OH  . TYR C 108 ? 0.345 0.838 0.457 -0.108 0.037  0.095  108 TYR CCC OH  
3355 N N   . THR C 109 ? 0.328 0.801 0.326 -0.054 0.021  0.100  109 THR CCC N   
3356 C CA  . THR C 109 ? 0.365 0.820 0.348 -0.056 0.027  0.117  109 THR CCC CA  
3357 C C   . THR C 109 ? 0.378 0.823 0.333 -0.043 0.015  0.122  109 THR CCC C   
3358 O O   . THR C 109 ? 0.405 0.830 0.344 -0.040 0.015  0.138  109 THR CCC O   
3359 C CB  . THR C 109 ? 0.403 0.865 0.379 -0.062 0.046  0.127  109 THR CCC CB  
3360 O OG1 . THR C 109 ? 0.433 0.909 0.386 -0.053 0.049  0.121  109 THR CCC OG1 
3361 C CG2 . THR C 109 ? 0.392 0.873 0.407 -0.075 0.056  0.122  109 THR CCC CG2 
3362 N N   . GLU C 110 ? 0.362 0.820 0.311 -0.037 0.005  0.108  110 GLU CCC N   
3363 C CA  . GLU C 110 ? 0.409 0.867 0.339 -0.026 -0.009 0.107  110 GLU CCC CA  
3364 C C   . GLU C 110 ? 0.400 0.860 0.355 -0.023 -0.022 0.099  110 GLU CCC C   
3365 O O   . GLU C 110 ? 0.433 0.901 0.383 -0.014 -0.037 0.096  110 GLU CCC O   
3366 C CB  . GLU C 110 ? 0.425 0.897 0.334 -0.024 -0.010 0.095  110 GLU CCC CB  
3367 C CG  . GLU C 110 ? 0.466 0.936 0.345 -0.024 0.004  0.104  110 GLU CCC CG  
3368 C CD  . GLU C 110 ? 0.500 0.974 0.341 -0.018 -0.000 0.095  110 GLU CCC CD  
3369 O OE1 . GLU C 110 ? 0.520 1.003 0.367 -0.018 -0.011 0.076  110 GLU CCC OE1 
3370 O OE2 . GLU C 110 ? 0.529 0.996 0.332 -0.014 0.008  0.106  110 GLU CCC OE2 
3371 N N   . TYR C 111 ? 0.368 0.824 0.348 -0.029 -0.018 0.093  111 TYR CCC N   
3372 C CA  . TYR C 111 ? 0.358 0.814 0.360 -0.026 -0.025 0.084  111 TYR CCC CA  
3373 C C   . TYR C 111 ? 0.377 0.818 0.382 -0.017 -0.030 0.096  111 TYR CCC C   
3374 O O   . TYR C 111 ? 0.358 0.778 0.355 -0.019 -0.023 0.109  111 TYR CCC O   
3375 C CB  . TYR C 111 ? 0.337 0.789 0.354 -0.033 -0.018 0.074  111 TYR CCC CB  
3376 C CG  . TYR C 111 ? 0.328 0.790 0.345 -0.037 -0.015 0.061  111 TYR CCC CG  
3377 C CD1 . TYR C 111 ? 0.338 0.810 0.359 -0.035 -0.019 0.052  111 TYR CCC CD1 
3378 C CD2 . TYR C 111 ? 0.319 0.780 0.334 -0.041 -0.009 0.059  111 TYR CCC CD2 
3379 C CE1 . TYR C 111 ? 0.331 0.804 0.350 -0.040 -0.014 0.041  111 TYR CCC CE1 
3380 C CE2 . TYR C 111 ? 0.309 0.771 0.320 -0.041 -0.007 0.050  111 TYR CCC CE2 
3381 C CZ  . TYR C 111 ? 0.316 0.779 0.326 -0.042 -0.008 0.041  111 TYR CCC CZ  
3382 O OH  . TYR C 111 ? 0.325 0.781 0.329 -0.044 -0.002 0.033  111 TYR CCC OH  
3383 N N   . THR C 112 ? 0.394 0.845 0.411 -0.006 -0.041 0.090  112 THR CCC N   
3384 C CA  . THR C 112 ? 0.409 0.847 0.438 0.008  -0.047 0.098  112 THR CCC CA  
3385 C C   . THR C 112 ? 0.398 0.849 0.458 0.010  -0.046 0.081  112 THR CCC C   
3386 O O   . THR C 112 ? 0.373 0.844 0.442 0.001  -0.043 0.067  112 THR CCC O   
3387 C CB  . THR C 112 ? 0.441 0.884 0.454 0.024  -0.062 0.110  112 THR CCC CB  
3388 O OG1 . THR C 112 ? 0.423 0.901 0.457 0.030  -0.076 0.095  112 THR CCC OG1 
3389 C CG2 . THR C 112 ? 0.460 0.898 0.434 0.021  -0.062 0.123  112 THR CCC CG2 
3390 N N   . GLU C 113 ? 0.437 0.875 0.513 0.022  -0.046 0.083  113 GLU CCC N   
3391 C CA  . GLU C 113 ? 0.456 0.905 0.564 0.027  -0.041 0.068  113 GLU CCC CA  
3392 C C   . GLU C 113 ? 0.412 0.903 0.543 0.030  -0.050 0.056  113 GLU CCC C   
3393 O O   . GLU C 113 ? 0.399 0.905 0.552 0.023  -0.039 0.040  113 GLU CCC O   
3394 C CB  . GLU C 113 ? 0.533 0.956 0.650 0.043  -0.040 0.073  113 GLU CCC CB  
3395 C CG  . GLU C 113 ? 0.577 1.026 0.730 0.063  -0.045 0.065  113 GLU CCC CG  
3396 C CD  . GLU C 113 ? 0.642 1.102 0.796 0.084  -0.066 0.080  113 GLU CCC CD  
3397 O OE1 . GLU C 113 ? 0.710 1.133 0.844 0.096  -0.069 0.098  113 GLU CCC OE1 
3398 O OE2 . GLU C 113 ? 0.713 1.217 0.885 0.087  -0.080 0.073  113 GLU CCC OE2 
3399 N N   . ALA C 114 ? 0.392 0.901 0.516 0.038  -0.068 0.063  114 ALA CCC N   
3400 C CA  . ALA C 114 ? 0.370 0.924 0.518 0.039  -0.081 0.050  114 ALA CCC CA  
3401 C C   . ALA C 114 ? 0.334 0.898 0.482 0.017  -0.070 0.035  114 ALA CCC C   
3402 O O   . ALA C 114 ? 0.325 0.922 0.504 0.012  -0.073 0.019  114 ALA CCC O   
3403 C CB  . ALA C 114 ? 0.376 0.939 0.502 0.051  -0.104 0.062  114 ALA CCC CB  
3404 N N   . ASP C 115 ? 0.334 0.872 0.452 0.004  -0.058 0.039  115 ASP CCC N   
3405 C CA  . ASP C 115 ? 0.324 0.863 0.436 -0.014 -0.047 0.027  115 ASP CCC CA  
3406 C C   . ASP C 115 ? 0.300 0.834 0.431 -0.022 -0.029 0.017  115 ASP CCC C   
3407 O O   . ASP C 115 ? 0.292 0.827 0.423 -0.035 -0.019 0.007  115 ASP CCC O   
3408 C CB  . ASP C 115 ? 0.341 0.857 0.417 -0.020 -0.042 0.036  115 ASP CCC CB  
3409 C CG  . ASP C 115 ? 0.379 0.897 0.430 -0.014 -0.054 0.046  115 ASP CCC CG  
3410 O OD1 . ASP C 115 ? 0.385 0.925 0.438 -0.011 -0.069 0.039  115 ASP CCC OD1 
3411 O OD2 . ASP C 115 ? 0.396 0.894 0.424 -0.014 -0.049 0.059  115 ASP CCC OD2 
3412 N N   . PHE C 116 ? 0.304 0.828 0.445 -0.013 -0.023 0.020  116 PHE CCC N   
3413 C CA  . PHE C 116 ? 0.319 0.828 0.463 -0.019 -0.003 0.012  116 PHE CCC CA  
3414 C C   . PHE C 116 ? 0.321 0.854 0.505 -0.013 0.004  0.000  116 PHE CCC C   
3415 O O   . PHE C 116 ? 0.325 0.882 0.537 0.000  -0.008 0.001  116 PHE CCC O   
3416 C CB  . PHE C 116 ? 0.323 0.800 0.444 -0.015 0.000  0.019  116 PHE CCC CB  
3417 C CG  . PHE C 116 ? 0.330 0.790 0.420 -0.024 -0.003 0.027  116 PHE CCC CG  
3418 C CD1 . PHE C 116 ? 0.327 0.789 0.408 -0.021 -0.014 0.039  116 PHE CCC CD1 
3419 C CD2 . PHE C 116 ? 0.349 0.793 0.420 -0.032 0.006  0.023  116 PHE CCC CD2 
3420 C CE1 . PHE C 116 ? 0.333 0.785 0.393 -0.028 -0.014 0.044  116 PHE CCC CE1 
3421 C CE2 . PHE C 116 ? 0.334 0.771 0.386 -0.037 0.002  0.030  116 PHE CCC CE2 
3422 C CZ  . PHE C 116 ? 0.330 0.773 0.380 -0.036 -0.007 0.039  116 PHE CCC CZ  
3423 N N   . GLY C 117 ? 0.328 0.856 0.514 -0.023 0.025  -0.009 117 GLY CCC N   
3424 C CA  . GLY C 117 ? 0.318 0.868 0.542 -0.022 0.042  -0.022 117 GLY CCC CA  
3425 C C   . GLY C 117 ? 0.334 0.855 0.535 -0.026 0.067  -0.026 117 GLY CCC C   
3426 O O   . GLY C 117 ? 0.340 0.825 0.496 -0.028 0.066  -0.019 117 GLY CCC O   
3427 N N   . SER C 118 ? 0.345 0.882 0.574 -0.028 0.089  -0.038 118 SER CCC N   
3428 C CA  . SER C 118 ? 0.373 0.883 0.577 -0.031 0.117  -0.043 118 SER CCC CA  
3429 C C   . SER C 118 ? 0.391 0.868 0.564 -0.017 0.110  -0.040 118 SER CCC C   
3430 O O   . SER C 118 ? 0.427 0.868 0.551 -0.022 0.117  -0.039 118 SER CCC O   
3431 C CB  . SER C 118 ? 0.379 0.863 0.541 -0.049 0.130  -0.040 118 SER CCC CB  
3432 O OG  . SER C 118 ? 0.378 0.886 0.571 -0.064 0.141  -0.045 118 SER CCC OG  
3433 N N   . TRP C 119 ? 0.399 0.886 0.598 -0.000 0.096  -0.039 119 TRP CCC N   
3434 C CA  . TRP C 119 ? 0.425 0.877 0.601 0.012  0.089  -0.037 119 TRP CCC CA  
3435 C C   . TRP C 119 ? 0.479 0.907 0.634 0.014  0.114  -0.051 119 TRP CCC C   
3436 O O   . TRP C 119 ? 0.496 0.944 0.682 0.020  0.135  -0.062 119 TRP CCC O   
3437 C CB  . TRP C 119 ? 0.420 0.885 0.632 0.032  0.074  -0.033 119 TRP CCC CB  
3438 C CG  . TRP C 119 ? 0.412 0.892 0.629 0.032  0.048  -0.018 119 TRP CCC CG  
3439 C CD1 . TRP C 119 ? 0.400 0.923 0.652 0.034  0.036  -0.017 119 TRP CCC CD1 
3440 C CD2 . TRP C 119 ? 0.408 0.861 0.593 0.029  0.032  -0.004 119 TRP CCC CD2 
3441 N NE1 . TRP C 119 ? 0.396 0.916 0.631 0.034  0.014  -0.003 119 TRP CCC NE1 
3442 C CE2 . TRP C 119 ? 0.398 0.876 0.594 0.031  0.013  0.006  119 TRP CCC CE2 
3443 C CE3 . TRP C 119 ? 0.430 0.841 0.579 0.023  0.032  -0.001 119 TRP CCC CE3 
3444 C CZ2 . TRP C 119 ? 0.401 0.861 0.570 0.028  -0.002 0.022  119 TRP CCC CZ2 
3445 C CZ3 . TRP C 119 ? 0.433 0.832 0.565 0.019  0.016  0.014  119 TRP CCC CZ3 
3446 C CH2 . TRP C 119 ? 0.429 0.851 0.569 0.022  0.002  0.026  119 TRP CCC CH2 
3447 N N   . GLY C 120 ? 0.531 0.918 0.635 0.008  0.112  -0.051 120 GLY CCC N   
3448 C CA  . GLY C 120 ? 0.587 0.942 0.661 0.013  0.130  -0.066 120 GLY CCC CA  
3449 C C   . GLY C 120 ? 0.618 0.965 0.719 0.032  0.131  -0.073 120 GLY CCC C   
3450 O O   . GLY C 120 ? 0.617 0.972 0.747 0.041  0.112  -0.063 120 GLY CCC O   
3451 N N   . GLN C 121 ? 0.650 0.977 0.738 0.040  0.155  -0.091 121 GLN CCC N   
3452 C CA  . GLN C 121 ? 0.671 0.978 0.776 0.060  0.159  -0.101 121 GLN CCC CA  
3453 C C   . GLN C 121 ? 0.680 0.943 0.754 0.055  0.136  -0.098 121 GLN CCC C   
3454 O O   . GLN C 121 ? 0.710 0.952 0.737 0.039  0.131  -0.101 121 GLN CCC O   
3455 C CB  . GLN C 121 ? 0.719 1.008 0.804 0.067  0.192  -0.123 121 GLN CCC CB  
3456 C CG  . GLN C 121 ? 0.775 1.016 0.841 0.080  0.194  -0.139 121 GLN CCC CG  
3457 C CD  . GLN C 121 ? 0.840 1.061 0.878 0.087  0.228  -0.163 121 GLN CCC CD  
3458 O OE1 . GLN C 121 ? 0.857 1.089 0.868 0.076  0.248  -0.167 121 GLN CCC OE1 
3459 N NE2 . GLN C 121 ? 0.888 1.074 0.927 0.105  0.237  -0.180 121 GLN CCC NE2 
3460 N N   . GLY C 122 ? 0.668 0.920 0.769 0.069  0.124  -0.091 122 GLY CCC N   
3461 C CA  . GLY C 122 ? 0.687 0.896 0.766 0.062  0.106  -0.086 122 GLY CCC CA  
3462 C C   . GLY C 122 ? 0.737 0.898 0.774 0.056  0.115  -0.109 122 GLY CCC C   
3463 O O   . GLY C 122 ? 0.783 0.935 0.817 0.069  0.138  -0.128 122 GLY CCC O   
3464 N N   . THR C 123 ? 0.744 0.878 0.750 0.037  0.099  -0.110 123 THR CCC N   
3465 C CA  . THR C 123 ? 0.793 0.878 0.758 0.028  0.101  -0.134 123 THR CCC CA  
3466 C C   . THR C 123 ? 0.815 0.862 0.789 0.021  0.087  -0.129 123 THR CCC C   
3467 O O   . THR C 123 ? 0.788 0.851 0.776 0.008  0.070  -0.109 123 THR CCC O   
3468 C CB  . THR C 123 ? 0.789 0.882 0.709 0.009  0.094  -0.142 123 THR CCC CB  
3469 O OG1 . THR C 123 ? 0.858 0.907 0.737 0.004  0.096  -0.170 123 THR CCC OG1 
3470 C CG2 . THR C 123 ? 0.765 0.879 0.687 -0.011 0.069  -0.125 123 THR CCC CG2 
3471 N N   . GLN C 124 ? 0.879 0.875 0.847 0.029  0.096  -0.148 124 GLN CCC N   
3472 C CA  . GLN C 124 ? 0.913 0.859 0.890 0.023  0.089  -0.144 124 GLN CCC CA  
3473 C C   . GLN C 124 ? 0.937 0.866 0.888 -0.009 0.073  -0.157 124 GLN CCC C   
3474 O O   . GLN C 124 ? 0.964 0.886 0.878 -0.019 0.073  -0.183 124 GLN CCC O   
3475 C CB  . GLN C 124 ? 0.975 0.869 0.953 0.046  0.107  -0.162 124 GLN CCC CB  
3476 C CG  . GLN C 124 ? 1.026 0.857 1.011 0.041  0.103  -0.158 124 GLN CCC CG  
3477 C CD  . GLN C 124 ? 0.997 0.838 1.014 0.050  0.095  -0.122 124 GLN CCC CD  
3478 O OE1 . GLN C 124 ? 0.982 0.846 1.027 0.080  0.099  -0.106 124 GLN CCC OE1 
3479 N NE2 . GLN C 124 ? 0.993 0.818 1.009 0.024  0.082  -0.108 124 GLN CCC NE2 
3480 N N   . VAL C 125 ? 0.938 0.863 0.907 -0.026 0.059  -0.138 125 VAL CCC N   
3481 C CA  . VAL C 125 ? 0.975 0.885 0.935 -0.059 0.044  -0.149 125 VAL CCC CA  
3482 C C   . VAL C 125 ? 1.025 0.874 1.000 -0.065 0.050  -0.145 125 VAL CCC C   
3483 O O   . VAL C 125 ? 1.021 0.868 1.019 -0.054 0.053  -0.115 125 VAL CCC O   
3484 C CB  . VAL C 125 ? 0.938 0.903 0.910 -0.076 0.028  -0.129 125 VAL CCC CB  
3485 C CG1 . VAL C 125 ? 0.957 0.916 0.931 -0.110 0.013  -0.141 125 VAL CCC CG1 
3486 C CG2 . VAL C 125 ? 0.902 0.918 0.858 -0.068 0.025  -0.129 125 VAL CCC CG2 
3487 N N   . THR C 126 ? 1.086 0.883 1.044 -0.082 0.050  -0.175 126 THR CCC N   
3488 C CA  . THR C 126 ? 1.157 0.882 1.125 -0.091 0.058  -0.176 126 THR CCC CA  
3489 C C   . THR C 126 ? 1.193 0.906 1.162 -0.134 0.044  -0.196 126 THR CCC C   
3490 O O   . THR C 126 ? 1.209 0.930 1.154 -0.147 0.033  -0.230 126 THR CCC O   
3491 C CB  . THR C 126 ? 1.220 0.884 1.171 -0.067 0.075  -0.199 126 THR CCC CB  
3492 O OG1 . THR C 126 ? 1.181 0.874 1.140 -0.028 0.086  -0.183 126 THR CCC OG1 
3493 C CG2 . THR C 126 ? 1.289 0.871 1.249 -0.071 0.086  -0.196 126 THR CCC CG2 
3494 N N   . VAL C 127 ? 1.207 0.904 1.203 -0.155 0.045  -0.175 127 VAL CCC N   
3495 C CA  . VAL C 127 ? 1.231 0.920 1.243 -0.200 0.035  -0.190 127 VAL CCC CA  
3496 C C   . VAL C 127 ? 1.305 0.907 1.325 -0.212 0.052  -0.188 127 VAL CCC C   
3497 O O   . VAL C 127 ? 1.304 0.882 1.334 -0.196 0.066  -0.152 127 VAL CCC O   
3498 C CB  . VAL C 127 ? 1.171 0.929 1.211 -0.217 0.025  -0.165 127 VAL CCC CB  
3499 C CG1 . VAL C 127 ? 1.195 0.963 1.260 -0.263 0.013  -0.185 127 VAL CCC CG1 
3500 C CG2 . VAL C 127 ? 1.097 0.932 1.127 -0.198 0.012  -0.159 127 VAL CCC CG2 
3501 N N   . SER C 128 ? 1.375 0.928 1.390 -0.240 0.049  -0.226 128 SER CCC N   
3502 C CA  . SER C 128 ? 1.461 0.920 1.483 -0.259 0.066  -0.230 128 SER CCC CA  
3503 C C   . SER C 128 ? 1.500 0.951 1.537 -0.311 0.054  -0.267 128 SER CCC C   
3504 O O   . SER C 128 ? 1.575 0.949 1.621 -0.336 0.067  -0.277 128 SER CCC O   
3505 C CB  . SER C 128 ? 1.532 0.914 1.524 -0.226 0.082  -0.244 128 SER CCC CB  
3506 O OG  . SER C 128 ? 1.554 0.937 1.517 -0.226 0.072  -0.291 128 SER CCC OG  
3507 N N   . GLN D 1   ? 0.744 0.745 0.851 -0.002 0.143  -0.005 3   GLN DDD N   
3508 C CA  . GLN D 1   ? 0.727 0.747 0.861 -0.010 0.139  -0.023 3   GLN DDD CA  
3509 C C   . GLN D 1   ? 0.674 0.721 0.783 -0.002 0.091  -0.014 3   GLN DDD C   
3510 O O   . GLN D 1   ? 0.699 0.729 0.760 0.012  0.078  0.007  3   GLN DDD O   
3511 C CB  . GLN D 1   ? 0.810 0.770 0.919 -0.005 0.189  -0.017 3   GLN DDD CB  
3512 C CG  . GLN D 1   ? 0.828 0.796 0.944 -0.008 0.184  -0.026 3   GLN DDD CG  
3513 C CD  . GLN D 1   ? 0.914 0.820 1.032 -0.011 0.251  -0.033 3   GLN DDD CD  
3514 O OE1 . GLN D 1   ? 0.964 0.834 1.111 -0.020 0.309  -0.043 3   GLN DDD OE1 
3515 N NE2 . GLN D 1   ? 0.939 0.828 1.030 -0.006 0.253  -0.028 3   GLN DDD NE2 
3516 N N   . VAL D 2   ? 0.621 0.705 0.761 -0.008 0.067  -0.034 4   VAL DDD N   
3517 C CA  . VAL D 2   ? 0.600 0.696 0.715 -0.002 0.036  -0.027 4   VAL DDD CA  
3518 C C   . VAL D 2   ? 0.614 0.697 0.719 -0.000 0.045  -0.025 4   VAL DDD C   
3519 O O   . VAL D 2   ? 0.629 0.714 0.772 -0.007 0.063  -0.046 4   VAL DDD O   
3520 C CB  . VAL D 2   ? 0.580 0.698 0.707 0.003  0.010  -0.047 4   VAL DDD CB  
3521 C CG1 . VAL D 2   ? 0.581 0.695 0.675 0.011  -0.009 -0.039 4   VAL DDD CG1 
3522 C CG2 . VAL D 2   ? 0.586 0.702 0.705 0.007  0.004  -0.048 4   VAL DDD CG2 
3523 N N   . GLN D 3   ? 0.629 0.697 0.691 0.009  0.033  -0.006 5   GLN DDD N   
3524 C CA  . GLN D 3   ? 0.664 0.711 0.699 0.015  0.039  -0.002 5   GLN DDD CA  
3525 C C   . GLN D 3   ? 0.643 0.713 0.675 0.015  0.009  -0.004 5   GLN DDD C   
3526 O O   . GLN D 3   ? 0.640 0.719 0.668 0.018  -0.010 0.001  5   GLN DDD O   
3527 C CB  . GLN D 3   ? 0.724 0.724 0.698 0.035  0.047  0.015  5   GLN DDD CB  
3528 C CG  . GLN D 3   ? 0.777 0.731 0.735 0.040  0.090  0.020  5   GLN DDD CG  
3529 C CD  . GLN D 3   ? 0.852 0.757 0.737 0.072  0.084  0.037  5   GLN DDD CD  
3530 O OE1 . GLN D 3   ? 0.934 0.763 0.743 0.096  0.115  0.048  5   GLN DDD OE1 
3531 N NE2 . GLN D 3   ? 0.834 0.774 0.735 0.077  0.047  0.035  5   GLN DDD NE2 
3532 N N   . LEU D 4   ? 0.643 0.718 0.687 0.012  0.011  -0.014 6   LEU DDD N   
3533 C CA  . LEU D 4   ? 0.643 0.729 0.678 0.013  -0.009 -0.015 6   LEU DDD CA  
3534 C C   . LEU D 4   ? 0.663 0.726 0.672 0.018  -0.001 -0.011 6   LEU DDD C   
3535 O O   . LEU D 4   ? 0.674 0.730 0.699 0.014  0.019  -0.020 6   LEU DDD O   
3536 C CB  . LEU D 4   ? 0.635 0.739 0.694 0.014  -0.019 -0.032 6   LEU DDD CB  
3537 C CG  . LEU D 4   ? 0.639 0.749 0.701 0.019  -0.029 -0.038 6   LEU DDD CG  
3538 C CD1 . LEU D 4   ? 0.661 0.777 0.723 0.036  -0.050 -0.059 6   LEU DDD CD1 
3539 C CD2 . LEU D 4   ? 0.647 0.743 0.682 0.018  -0.030 -0.020 6   LEU DDD CD2 
3540 N N   . VAL D 5   ? 0.684 0.735 0.660 0.028  -0.016 -0.003 7   VAL DDD N   
3541 C CA  . VAL D 5   ? 0.739 0.758 0.671 0.040  -0.015 -0.001 7   VAL DDD CA  
3542 C C   . VAL D 5   ? 0.744 0.782 0.688 0.035  -0.031 -0.008 7   VAL DDD C   
3543 O O   . VAL D 5   ? 0.726 0.784 0.688 0.033  -0.051 -0.014 7   VAL DDD O   
3544 C CB  . VAL D 5   ? 0.779 0.768 0.660 0.066  -0.031 0.002  7   VAL DDD CB  
3545 C CG1 . VAL D 5   ? 0.841 0.782 0.654 0.090  -0.033 0.003  7   VAL DDD CG1 
3546 C CG2 . VAL D 5   ? 0.799 0.761 0.661 0.074  -0.010 0.012  7   VAL DDD CG2 
3547 N N   . GLU D 6   ? 0.796 0.825 0.738 0.031  -0.017 -0.010 8   GLU DDD N   
3548 C CA  . GLU D 6   ? 0.830 0.869 0.776 0.028  -0.028 -0.015 8   GLU DDD CA  
3549 C C   . GLU D 6   ? 0.894 0.902 0.794 0.041  -0.031 -0.015 8   GLU DDD C   
3550 O O   . GLU D 6   ? 0.951 0.915 0.808 0.052  -0.010 -0.009 8   GLU DDD O   
3551 C CB  . GLU D 6   ? 0.845 0.895 0.820 0.022  -0.016 -0.023 8   GLU DDD CB  
3552 C CG  . GLU D 6   ? 0.841 0.915 0.851 0.020  -0.021 -0.032 8   GLU DDD CG  
3553 C CD  . GLU D 6   ? 0.865 0.948 0.921 0.017  -0.002 -0.049 8   GLU DDD CD  
3554 O OE1 . GLU D 6   ? 0.895 0.954 0.945 0.013  0.026  -0.044 8   GLU DDD OE1 
3555 O OE2 . GLU D 6   ? 0.874 0.981 0.969 0.023  -0.015 -0.072 8   GLU DDD OE2 
3556 N N   . SER D 7   ? 0.921 0.938 0.824 0.041  -0.051 -0.023 9   SER DDD N   
3557 C CA  . SER D 7   ? 0.983 0.975 0.845 0.055  -0.061 -0.030 9   SER DDD CA  
3558 C C   . SER D 7   ? 0.982 0.993 0.874 0.043  -0.067 -0.040 9   SER DDD C   
3559 O O   . SER D 7   ? 0.913 0.946 0.845 0.028  -0.061 -0.040 9   SER DDD O   
3560 C CB  . SER D 7   ? 1.018 0.996 0.848 0.080  -0.091 -0.043 9   SER DDD CB  
3561 O OG  . SER D 7   ? 0.978 1.000 0.873 0.071  -0.113 -0.060 9   SER DDD OG  
3562 N N   . GLY D 8   ? 1.057 1.047 0.918 0.053  -0.073 -0.048 10  GLY DDD N   
3563 C CA  . GLY D 8   ? 1.067 1.067 0.952 0.043  -0.076 -0.060 10  GLY DDD CA  
3564 C C   . GLY D 8   ? 1.077 1.064 0.952 0.036  -0.053 -0.048 10  GLY DDD C   
3565 O O   . GLY D 8   ? 1.094 1.084 0.985 0.028  -0.050 -0.055 10  GLY DDD O   
3566 N N   . GLY D 9   ? 1.112 1.081 0.966 0.039  -0.033 -0.036 11  GLY DDD N   
3567 C CA  . GLY D 9   ? 1.144 1.105 1.007 0.035  -0.010 -0.034 11  GLY DDD CA  
3568 C C   . GLY D 9   ? 1.215 1.135 1.030 0.044  0.001  -0.036 11  GLY DDD C   
3569 O O   . GLY D 9   ? 1.217 1.122 0.994 0.056  -0.021 -0.043 11  GLY DDD O   
3570 N N   . GLY D 10  ? 1.274 1.175 1.095 0.042  0.033  -0.035 12  GLY DDD N   
3571 C CA  . GLY D 10  ? 1.380 1.226 1.147 0.051  0.057  -0.034 12  GLY DDD CA  
3572 C C   . GLY D 10  ? 1.390 1.249 1.188 0.043  0.062  -0.041 12  GLY DDD C   
3573 O O   . GLY D 10  ? 1.326 1.231 1.191 0.034  0.057  -0.048 12  GLY DDD O   
3574 N N   . LEU D 11  ? 1.442 1.258 1.185 0.052  0.069  -0.041 13  LEU DDD N   
3575 C CA  . LEU D 11  ? 1.436 1.253 1.198 0.046  0.080  -0.047 13  LEU DDD CA  
3576 C C   . LEU D 11  ? 1.439 1.281 1.202 0.044  0.045  -0.053 13  LEU DDD C   
3577 O O   . LEU D 11  ? 1.464 1.298 1.192 0.052  0.018  -0.059 13  LEU DDD O   
3578 C CB  . LEU D 11  ? 1.516 1.257 1.208 0.058  0.117  -0.044 13  LEU DDD CB  
3579 C CG  . LEU D 11  ? 1.506 1.241 1.227 0.051  0.145  -0.050 13  LEU DDD CG  
3580 C CD1 . LEU D 11  ? 1.463 1.226 1.279 0.038  0.178  -0.062 13  LEU DDD CD1 
3581 C CD2 . LEU D 11  ? 1.589 1.234 1.214 0.067  0.177  -0.046 13  LEU DDD CD2 
3582 N N   . VAL D 12  ? 1.450 1.318 1.257 0.037  0.045  -0.056 14  VAL DDD N   
3583 C CA  . VAL D 12  ? 1.464 1.339 1.275 0.033  0.032  -0.061 14  VAL DDD CA  
3584 C C   . VAL D 12  ? 1.475 1.345 1.302 0.035  0.048  -0.062 14  VAL DDD C   
3585 O O   . VAL D 12  ? 1.465 1.336 1.315 0.038  0.065  -0.063 14  VAL DDD O   
3586 C CB  . VAL D 12  ? 1.439 1.341 1.278 0.028  0.017  -0.061 14  VAL DDD CB  
3587 C CG1 . VAL D 12  ? 1.418 1.329 1.255 0.026  -0.002 -0.067 14  VAL DDD CG1 
3588 C CG2 . VAL D 12  ? 1.424 1.345 1.289 0.035  0.018  -0.053 14  VAL DDD CG2 
3589 N N   . GLN D 13  ? 1.493 1.355 1.316 0.033  0.048  -0.065 15  GLN DDD N   
3590 C CA  . GLN D 13  ? 1.507 1.360 1.340 0.040  0.060  -0.065 15  GLN DDD CA  
3591 C C   . GLN D 13  ? 1.505 1.353 1.337 0.048  0.058  -0.060 15  GLN DDD C   
3592 O O   . GLN D 13  ? 1.530 1.376 1.360 0.040  0.057  -0.060 15  GLN DDD O   
3593 C CB  . GLN D 13  ? 1.537 1.362 1.345 0.036  0.073  -0.070 15  GLN DDD CB  
3594 C CG  . GLN D 13  ? 1.545 1.359 1.337 0.026  0.064  -0.082 15  GLN DDD CG  
3595 C CD  . GLN D 13  ? 1.579 1.363 1.341 0.026  0.072  -0.093 15  GLN DDD CD  
3596 O OE1 . GLN D 13  ? 1.605 1.378 1.344 0.028  0.055  -0.111 15  GLN DDD OE1 
3597 N NE2 . GLN D 13  ? 1.590 1.360 1.354 0.030  0.093  -0.086 15  GLN DDD NE2 
3598 N N   . ALA D 14  ? 1.461 1.297 1.291 0.069  0.061  -0.059 16  ALA DDD N   
3599 C CA  . ALA D 14  ? 1.461 1.265 1.259 0.092  0.064  -0.052 16  ALA DDD CA  
3600 C C   . ALA D 14  ? 1.473 1.239 1.251 0.075  0.092  -0.048 16  ALA DDD C   
3601 O O   . ALA D 14  ? 1.479 1.243 1.268 0.055  0.103  -0.057 16  ALA DDD O   
3602 C CB  . ALA D 14  ? 1.466 1.255 1.255 0.123  0.060  -0.057 16  ALA DDD CB  
3603 N N   . GLY D 15  ? 1.469 1.202 1.222 0.083  0.106  -0.040 17  GLY DDD N   
3604 C CA  . GLY D 15  ? 1.524 1.217 1.279 0.064  0.146  -0.043 17  GLY DDD CA  
3605 C C   . GLY D 15  ? 1.503 1.239 1.316 0.032  0.138  -0.060 17  GLY DDD C   
3606 O O   . GLY D 15  ? 1.533 1.248 1.379 0.012  0.170  -0.076 17  GLY DDD O   
3607 N N   . GLY D 16  ? 1.450 1.241 1.282 0.028  0.099  -0.062 18  GLY DDD N   
3608 C CA  . GLY D 16  ? 1.399 1.229 1.272 0.009  0.082  -0.078 18  GLY DDD CA  
3609 C C   . GLY D 16  ? 1.380 1.209 1.261 0.009  0.087  -0.072 18  GLY DDD C   
3610 O O   . GLY D 16  ? 1.399 1.207 1.241 0.030  0.092  -0.052 18  GLY DDD O   
3611 N N   . SER D 17  ? 1.336 1.190 1.268 -0.009 0.083  -0.094 19  SER DDD N   
3612 C CA  . SER D 17  ? 1.295 1.154 1.249 -0.013 0.089  -0.093 19  SER DDD CA  
3613 C C   . SER D 17  ? 1.226 1.135 1.187 -0.010 0.045  -0.094 19  SER DDD C   
3614 O O   . SER D 17  ? 1.192 1.127 1.174 -0.013 0.018  -0.117 19  SER DDD O   
3615 C CB  . SER D 17  ? 1.327 1.175 1.350 -0.035 0.123  -0.124 19  SER DDD CB  
3616 O OG  . SER D 17  ? 1.406 1.183 1.406 -0.033 0.184  -0.113 19  SER DDD OG  
3617 N N   . LEU D 18  ? 1.194 1.106 1.131 0.000  0.040  -0.073 20  LEU DDD N   
3618 C CA  . LEU D 18  ? 1.133 1.081 1.073 0.003  0.009  -0.071 20  LEU DDD CA  
3619 C C   . LEU D 18  ? 1.082 1.031 1.037 0.001  0.018  -0.066 20  LEU DDD C   
3620 O O   . LEU D 18  ? 1.113 1.027 1.040 0.010  0.042  -0.051 20  LEU DDD O   
3621 C CB  . LEU D 18  ? 1.142 1.093 1.047 0.017  -0.001 -0.054 20  LEU DDD CB  
3622 C CG  . LEU D 18  ? 1.147 1.116 1.045 0.019  -0.018 -0.053 20  LEU DDD CG  
3623 C CD1 . LEU D 18  ? 1.167 1.130 1.053 0.021  -0.032 -0.069 20  LEU DDD CD1 
3624 C CD2 . LEU D 18  ? 1.149 1.116 1.038 0.027  -0.011 -0.045 20  LEU DDD CD2 
3625 N N   . ARG D 19  ? 1.532 1.247 1.343 -0.026 -0.118 -0.390 21  ARG DDD N   
3626 C CA  . ARG D 19  ? 1.433 1.178 1.276 -0.056 -0.129 -0.340 21  ARG DDD CA  
3627 C C   . ARG D 19  ? 1.326 1.153 1.149 -0.050 -0.116 -0.309 21  ARG DDD C   
3628 O O   . ARG D 19  ? 1.317 1.186 1.101 -0.059 -0.123 -0.321 21  ARG DDD O   
3629 C CB  . ARG D 19  ? 1.466 1.196 1.312 -0.096 -0.158 -0.354 21  ARG DDD CB  
3630 C CG  . ARG D 19  ? 1.413 1.170 1.295 -0.124 -0.168 -0.302 21  ARG DDD CG  
3631 C CD  . ARG D 19  ? 1.461 1.224 1.342 -0.162 -0.197 -0.315 21  ARG DDD CD  
3632 N NE  . ARG D 19  ? 1.431 1.218 1.349 -0.187 -0.204 -0.266 21  ARG DDD NE  
3633 C CZ  . ARG D 19  ? 1.444 1.193 1.416 -0.204 -0.210 -0.242 21  ARG DDD CZ  
3634 N NH1 . ARG D 19  ? 1.516 1.191 1.514 -0.201 -0.209 -0.261 21  ARG DDD NH1 
3635 N NH2 . ARG D 19  ? 1.376 1.160 1.375 -0.222 -0.214 -0.196 21  ARG DDD NH2 
3636 N N   . LEU D 20  ? 1.239 1.087 1.089 -0.035 -0.100 -0.270 22  LEU DDD N   
3637 C CA  . LEU D 20  ? 1.140 1.059 0.985 -0.034 -0.089 -0.237 22  LEU DDD CA  
3638 C C   . LEU D 20  ? 1.063 0.999 0.922 -0.065 -0.106 -0.207 22  LEU DDD C   
3639 O O   . LEU D 20  ? 1.044 0.944 0.934 -0.080 -0.119 -0.196 22  LEU DDD O   
3640 C CB  . LEU D 20  ? 1.102 1.037 0.978 -0.010 -0.069 -0.212 22  LEU DDD CB  
3641 C CG  . LEU D 20  ? 1.152 1.072 1.025 0.025  -0.050 -0.235 22  LEU DDD CG  
3642 C CD1 . LEU D 20  ? 1.099 1.059 1.003 0.045  -0.033 -0.206 22  LEU DDD CD1 
3643 C CD2 . LEU D 20  ? 1.199 1.138 1.022 0.037  -0.041 -0.271 22  LEU DDD CD2 
3644 N N   . SER D 21  ? 1.013 1.002 0.851 -0.072 -0.104 -0.193 23  SER DDD N   
3645 C CA  . SER D 21  ? 0.950 0.967 0.799 -0.096 -0.115 -0.161 23  SER DDD CA  
3646 C C   . SER D 21  ? 0.881 0.948 0.734 -0.087 -0.098 -0.132 23  SER DDD C   
3647 O O   . SER D 21  ? 0.886 0.977 0.719 -0.070 -0.082 -0.140 23  SER DDD O   
3648 C CB  . SER D 21  ? 0.974 1.003 0.797 -0.116 -0.134 -0.176 23  SER DDD CB  
3649 O OG  . SER D 21  ? 0.995 1.066 0.776 -0.105 -0.124 -0.185 23  SER DDD OG  
3650 N N   . CYS D 22  ? 0.823 0.902 0.700 -0.098 -0.102 -0.100 24  CYS DDD N   
3651 C CA  . CYS D 22  ? 0.779 0.898 0.666 -0.094 -0.089 -0.074 24  CYS DDD CA  
3652 C C   . CYS D 22  ? 0.730 0.867 0.620 -0.111 -0.099 -0.050 24  CYS DDD C   
3653 O O   . CYS D 22  ? 0.701 0.825 0.613 -0.120 -0.109 -0.037 24  CYS DDD O   
3654 C CB  . CYS D 22  ? 0.778 0.895 0.697 -0.081 -0.080 -0.063 24  CYS DDD CB  
3655 S SG  . CYS D 22  ? 0.731 0.888 0.670 -0.084 -0.071 -0.035 24  CYS DDD SG  
3656 N N   . ALA D 23  ? 0.721 0.889 0.589 -0.114 -0.095 -0.043 25  ALA DDD N   
3657 C CA  . ALA D 23  ? 0.691 0.883 0.561 -0.125 -0.101 -0.018 25  ALA DDD CA  
3658 C C   . ALA D 23  ? 0.640 0.847 0.531 -0.119 -0.086 0.005  25  ALA DDD C   
3659 O O   . ALA D 23  ? 0.667 0.887 0.557 -0.109 -0.068 0.005  25  ALA DDD O   
3660 C CB  . ALA D 23  ? 0.715 0.935 0.552 -0.128 -0.104 -0.021 25  ALA DDD CB  
3661 N N   . ALA D 24  ? 0.614 0.821 0.526 -0.124 -0.091 0.023  26  ALA DDD N   
3662 C CA  . ALA D 24  ? 0.584 0.799 0.518 -0.119 -0.081 0.039  26  ALA DDD CA  
3663 C C   . ALA D 24  ? 0.558 0.791 0.489 -0.122 -0.079 0.061  26  ALA DDD C   
3664 O O   . ALA D 24  ? 0.593 0.832 0.517 -0.129 -0.091 0.069  26  ALA DDD O   
3665 C CB  . ALA D 24  ? 0.583 0.784 0.537 -0.118 -0.088 0.039  26  ALA DDD CB  
3666 N N   . SER D 25  ? 0.542 0.783 0.483 -0.117 -0.063 0.072  27  SER DDD N   
3667 C CA  . SER D 25  ? 0.538 0.789 0.483 -0.115 -0.057 0.095  27  SER DDD CA  
3668 C C   . SER D 25  ? 0.514 0.752 0.488 -0.112 -0.049 0.097  27  SER DDD C   
3669 O O   . SER D 25  ? 0.501 0.736 0.492 -0.111 -0.038 0.090  27  SER DDD O   
3670 C CB  . SER D 25  ? 0.581 0.851 0.512 -0.111 -0.045 0.110  27  SER DDD CB  
3671 O OG  . SER D 25  ? 0.601 0.879 0.537 -0.106 -0.039 0.136  27  SER DDD OG  
3672 N N   . GLY D 26  ? 0.508 0.744 0.489 -0.109 -0.056 0.103  28  GLY DDD N   
3673 C CA  . GLY D 26  ? 0.503 0.727 0.505 -0.104 -0.049 0.102  28  GLY DDD CA  
3674 C C   . GLY D 26  ? 0.493 0.711 0.507 -0.103 -0.057 0.081  28  GLY DDD C   
3675 O O   . GLY D 26  ? 0.526 0.735 0.559 -0.100 -0.052 0.072  28  GLY DDD O   
3676 N N   . GLY D 27  ? 0.497 0.719 0.502 -0.104 -0.068 0.074  29  GLY DDD N   
3677 C CA  . GLY D 27  ? 0.505 0.726 0.518 -0.099 -0.076 0.058  29  GLY DDD CA  
3678 C C   . GLY D 27  ? 0.504 0.733 0.509 -0.093 -0.086 0.067  29  GLY DDD C   
3679 O O   . GLY D 27  ? 0.521 0.755 0.527 -0.087 -0.094 0.060  29  GLY DDD O   
3680 N N   . THR D 28  ? 0.504 0.739 0.501 -0.091 -0.084 0.083  30  THR DDD N   
3681 C CA  . THR D 28  ? 0.502 0.751 0.492 -0.086 -0.091 0.099  30  THR DDD CA  
3682 C C   . THR D 28  ? 0.516 0.763 0.505 -0.092 -0.100 0.100  30  THR DDD C   
3683 O O   . THR D 28  ? 0.539 0.792 0.530 -0.082 -0.104 0.100  30  THR DDD O   
3684 C CB  . THR D 28  ? 0.509 0.767 0.498 -0.070 -0.089 0.095  30  THR DDD CB  
3685 O OG1 . THR D 28  ? 0.527 0.775 0.521 -0.066 -0.079 0.088  30  THR DDD OG1 
3686 C CG2 . THR D 28  ? 0.513 0.793 0.496 -0.062 -0.090 0.117  30  THR DDD CG2 
3687 N N   . PHE D 29  ? 0.513 0.750 0.500 -0.105 -0.103 0.100  31  PHE DDD N   
3688 C CA  . PHE D 29  ? 0.528 0.750 0.517 -0.110 -0.110 0.095  31  PHE DDD CA  
3689 C C   . PHE D 29  ? 0.567 0.795 0.564 -0.107 -0.116 0.112  31  PHE DDD C   
3690 O O   . PHE D 29  ? 0.608 0.826 0.611 -0.101 -0.118 0.109  31  PHE DDD O   
3691 C CB  . PHE D 29  ? 0.526 0.741 0.507 -0.125 -0.115 0.091  31  PHE DDD CB  
3692 C CG  . PHE D 29  ? 0.539 0.730 0.522 -0.130 -0.120 0.078  31  PHE DDD CG  
3693 C CD1 . PHE D 29  ? 0.538 0.716 0.517 -0.123 -0.115 0.058  31  PHE DDD CD1 
3694 C CD2 . PHE D 29  ? 0.550 0.730 0.543 -0.140 -0.130 0.086  31  PHE DDD CD2 
3695 C CE1 . PHE D 29  ? 0.564 0.716 0.545 -0.124 -0.118 0.044  31  PHE DDD CE1 
3696 C CE2 . PHE D 29  ? 0.580 0.730 0.578 -0.144 -0.135 0.072  31  PHE DDD CE2 
3697 C CZ  . PHE D 29  ? 0.593 0.727 0.583 -0.134 -0.129 0.051  31  PHE DDD CZ  
3698 N N   . SER D 30  ? 0.583 0.831 0.582 -0.109 -0.116 0.133  32  SER DDD N   
3699 C CA  . SER D 30  ? 0.601 0.862 0.611 -0.107 -0.119 0.157  32  SER DDD CA  
3700 C C   . SER D 30  ? 0.622 0.891 0.630 -0.087 -0.116 0.160  32  SER DDD C   
3701 O O   . SER D 30  ? 0.669 0.939 0.688 -0.085 -0.117 0.179  32  SER DDD O   
3702 C CB  . SER D 30  ? 0.599 0.890 0.613 -0.107 -0.116 0.179  32  SER DDD CB  
3703 O OG  . SER D 30  ? 0.663 0.956 0.691 -0.128 -0.124 0.190  32  SER DDD OG  
3704 N N   . THR D 31  ? 0.610 0.887 0.607 -0.073 -0.112 0.142  33  THR DDD N   
3705 C CA  . THR D 31  ? 0.583 0.877 0.573 -0.052 -0.113 0.139  33  THR DDD CA  
3706 C C   . THR D 31  ? 0.577 0.857 0.570 -0.050 -0.117 0.115  33  THR DDD C   
3707 O O   . THR D 31  ? 0.597 0.897 0.585 -0.035 -0.120 0.105  33  THR DDD O   
3708 C CB  . THR D 31  ? 0.576 0.892 0.552 -0.038 -0.108 0.132  33  THR DDD CB  
3709 O OG1 . THR D 31  ? 0.568 0.867 0.546 -0.044 -0.106 0.107  33  THR DDD OG1 
3710 C CG2 . THR D 31  ? 0.573 0.908 0.548 -0.035 -0.102 0.158  33  THR DDD CG2 
3711 N N   . ALA D 32  ? 0.555 0.809 0.556 -0.064 -0.117 0.105  34  ALA DDD N   
3712 C CA  . ALA D 32  ? 0.548 0.794 0.557 -0.062 -0.118 0.085  34  ALA DDD CA  
3713 C C   . ALA D 32  ? 0.565 0.794 0.582 -0.059 -0.121 0.093  34  ALA DDD C   
3714 O O   . ALA D 32  ? 0.582 0.788 0.602 -0.072 -0.121 0.102  34  ALA DDD O   
3715 C CB  . ALA D 32  ? 0.540 0.771 0.549 -0.075 -0.112 0.068  34  ALA DDD CB  
3716 N N   . ALA D 33  ? 0.585 0.827 0.609 -0.043 -0.123 0.090  35  ALA DDD N   
3717 C CA  . ALA D 33  ? 0.610 0.832 0.646 -0.036 -0.124 0.094  35  ALA DDD CA  
3718 C C   . ALA D 33  ? 0.606 0.809 0.646 -0.044 -0.119 0.070  35  ALA DDD C   
3719 O O   . ALA D 33  ? 0.570 0.791 0.612 -0.045 -0.117 0.052  35  ALA DDD O   
3720 C CB  . ALA D 33  ? 0.619 0.870 0.661 -0.013 -0.128 0.101  35  ALA DDD CB  
3721 N N   . MET D 34  ? 0.641 0.808 0.684 -0.048 -0.117 0.068  36  MET DDD N   
3722 C CA  . MET D 34  ? 0.642 0.791 0.682 -0.053 -0.111 0.045  36  MET DDD CA  
3723 C C   . MET D 34  ? 0.648 0.781 0.701 -0.036 -0.107 0.040  36  MET DDD C   
3724 O O   . MET D 34  ? 0.645 0.759 0.708 -0.027 -0.110 0.057  36  MET DDD O   
3725 C CB  . MET D 34  ? 0.687 0.810 0.714 -0.072 -0.112 0.040  36  MET DDD CB  
3726 C CG  . MET D 34  ? 0.676 0.819 0.690 -0.086 -0.113 0.045  36  MET DDD CG  
3727 S SD  . MET D 34  ? 0.666 0.831 0.675 -0.086 -0.103 0.028  36  MET DDD SD  
3728 C CE  . MET D 34  ? 0.668 0.857 0.675 -0.090 -0.104 0.042  36  MET DDD CE  
3729 N N   . GLY D 35  ? 0.648 0.790 0.705 -0.029 -0.099 0.020  37  GLY DDD N   
3730 C CA  . GLY D 35  ? 0.675 0.809 0.746 -0.007 -0.094 0.014  37  GLY DDD CA  
3731 C C   . GLY D 35  ? 0.694 0.815 0.757 -0.005 -0.082 -0.010 37  GLY DDD C   
3732 O O   . GLY D 35  ? 0.681 0.817 0.731 -0.019 -0.078 -0.020 37  GLY DDD O   
3733 N N   . TRP D 36  ? 0.729 0.822 0.798 0.013  -0.077 -0.018 38  TRP DDD N   
3734 C CA  . TRP D 36  ? 0.771 0.857 0.833 0.024  -0.063 -0.042 38  TRP DDD CA  
3735 C C   . TRP D 36  ? 0.774 0.891 0.864 0.052  -0.054 -0.039 38  TRP DDD C   
3736 O O   . TRP D 36  ? 0.807 0.911 0.915 0.071  -0.057 -0.026 38  TRP DDD O   
3737 C CB  . TRP D 36  ? 0.840 0.866 0.886 0.025  -0.063 -0.060 38  TRP DDD CB  
3738 C CG  . TRP D 36  ? 0.840 0.849 0.859 -0.003 -0.072 -0.070 38  TRP DDD CG  
3739 C CD1 . TRP D 36  ? 0.842 0.827 0.860 -0.024 -0.086 -0.058 38  TRP DDD CD1 
3740 C CD2 . TRP D 36  ? 0.842 0.867 0.831 -0.011 -0.066 -0.090 38  TRP DDD CD2 
3741 N NE1 . TRP D 36  ? 0.850 0.835 0.842 -0.045 -0.091 -0.072 38  TRP DDD NE1 
3742 C CE2 . TRP D 36  ? 0.853 0.862 0.824 -0.036 -0.080 -0.091 38  TRP DDD CE2 
3743 C CE3 . TRP D 36  ? 0.847 0.902 0.824 0.002  -0.050 -0.104 38  TRP DDD CE3 
3744 C CZ2 . TRP D 36  ? 0.857 0.882 0.796 -0.047 -0.079 -0.106 38  TRP DDD CZ2 
3745 C CZ3 . TRP D 36  ? 0.851 0.920 0.796 -0.009 -0.047 -0.117 38  TRP DDD CZ3 
3746 C CH2 . TRP D 36  ? 0.863 0.917 0.787 -0.032 -0.062 -0.118 38  TRP DDD CH2 
3747 N N   . PHE D 37  ? 0.757 0.919 0.854 0.054  -0.043 -0.047 39  PHE DDD N   
3748 C CA  . PHE D 37  ? 0.755 0.958 0.883 0.079  -0.033 -0.046 39  PHE DDD CA  
3749 C C   . PHE D 37  ? 0.788 0.982 0.904 0.094  -0.013 -0.067 39  PHE DDD C   
3750 O O   . PHE D 37  ? 0.799 0.978 0.883 0.080  -0.008 -0.081 39  PHE DDD O   
3751 C CB  . PHE D 37  ? 0.710 0.976 0.863 0.067  -0.035 -0.038 39  PHE DDD CB  
3752 C CG  . PHE D 37  ? 0.689 0.974 0.856 0.061  -0.054 -0.022 39  PHE DDD CG  
3753 C CD1 . PHE D 37  ? 0.673 0.936 0.818 0.041  -0.066 -0.015 39  PHE DDD CD1 
3754 C CD2 . PHE D 37  ? 0.676 1.009 0.878 0.078  -0.060 -0.013 39  PHE DDD CD2 
3755 C CE1 . PHE D 37  ? 0.655 0.940 0.808 0.039  -0.082 -0.002 39  PHE DDD CE1 
3756 C CE2 . PHE D 37  ? 0.657 1.014 0.865 0.076  -0.079 -0.001 39  PHE DDD CE2 
3757 C CZ  . PHE D 37  ? 0.656 0.988 0.838 0.057  -0.089 0.004  39  PHE DDD CZ  
3758 N N   . ARG D 38  ? 0.823 1.030 0.962 0.126  -0.002 -0.069 40  ARG DDD N   
3759 C CA  . ARG D 38  ? 0.868 1.077 0.998 0.148  0.021  -0.089 40  ARG DDD CA  
3760 C C   . ARG D 38  ? 0.855 1.134 1.028 0.168  0.033  -0.079 40  ARG DDD C   
3761 O O   . ARG D 38  ? 0.820 1.129 1.030 0.174  0.022  -0.060 40  ARG DDD O   
3762 C CB  . ARG D 38  ? 0.931 1.073 1.043 0.170  0.024  -0.107 40  ARG DDD CB  
3763 C CG  . ARG D 38  ? 0.948 1.084 1.094 0.204  0.025  -0.094 40  ARG DDD CG  
3764 C CD  . ARG D 38  ? 1.023 1.081 1.154 0.226  0.031  -0.114 40  ARG DDD CD  
3765 N NE  . ARG D 38  ? 1.053 1.096 1.220 0.256  0.030  -0.094 40  ARG DDD NE  
3766 C CZ  . ARG D 38  ? 1.127 1.097 1.293 0.278  0.034  -0.103 40  ARG DDD CZ  
3767 N NH1 . ARG D 38  ? 1.182 1.086 1.314 0.271  0.038  -0.139 40  ARG DDD NH1 
3768 N NH2 . ARG D 38  ? 1.146 1.109 1.348 0.307  0.035  -0.077 40  ARG DDD NH2 
3769 N N   . GLN D 39  ? 0.872 1.183 1.044 0.178  0.056  -0.089 41  GLN DDD N   
3770 C CA  . GLN D 39  ? 0.869 1.252 1.087 0.198  0.073  -0.079 41  GLN DDD CA  
3771 C C   . GLN D 39  ? 0.934 1.315 1.135 0.231  0.101  -0.097 41  GLN DDD C   
3772 O O   . GLN D 39  ? 0.940 1.328 1.110 0.224  0.116  -0.107 41  GLN DDD O   
3773 C CB  . GLN D 39  ? 0.821 1.265 1.064 0.168  0.074  -0.065 41  GLN DDD CB  
3774 C CG  . GLN D 39  ? 0.803 1.329 1.108 0.180  0.086  -0.051 41  GLN DDD CG  
3775 C CD  . GLN D 39  ? 0.761 1.338 1.100 0.144  0.084  -0.037 41  GLN DDD CD  
3776 O OE1 . GLN D 39  ? 0.741 1.294 1.053 0.117  0.082  -0.038 41  GLN DDD OE1 
3777 N NE2 . GLN D 39  ? 0.749 1.397 1.153 0.145  0.082  -0.025 41  GLN DDD NE2 
3778 N N   . ALA D 40  ? 0.992 1.365 1.210 0.270  0.108  -0.101 42  ALA DDD N   
3779 C CA  . ALA D 40  ? 1.049 1.433 1.261 0.311  0.138  -0.117 42  ALA DDD CA  
3780 C C   . ALA D 40  ? 1.031 1.513 1.286 0.312  0.158  -0.099 42  ALA DDD C   
3781 O O   . ALA D 40  ? 0.962 1.500 1.268 0.293  0.146  -0.075 42  ALA DDD O   
3782 C CB  . ALA D 40  ? 1.085 1.438 1.315 0.353  0.140  -0.120 42  ALA DDD CB  
3783 N N   . PRO D 41  ? 1.096 1.605 1.334 0.334  0.189  -0.110 43  PRO DDD N   
3784 C CA  . PRO D 41  ? 1.067 1.673 1.354 0.338  0.212  -0.089 43  PRO DDD CA  
3785 C C   . PRO D 41  ? 1.067 1.724 1.415 0.375  0.219  -0.076 43  PRO DDD C   
3786 O O   . PRO D 41  ? 1.127 1.769 1.463 0.420  0.239  -0.091 43  PRO DDD O   
3787 C CB  . PRO D 41  ? 1.126 1.737 1.364 0.357  0.244  -0.106 43  PRO DDD CB  
3788 C CG  . PRO D 41  ? 1.197 1.717 1.373 0.383  0.240  -0.144 43  PRO DDD CG  
3789 C CD  . PRO D 41  ? 1.171 1.622 1.343 0.355  0.202  -0.145 43  PRO DDD CD  
3790 N N   . GLY D 42  ? 1.010 1.722 1.422 0.355  0.201  -0.050 44  GLY DDD N   
3791 C CA  . GLY D 42  ? 1.006 1.778 1.482 0.386  0.200  -0.034 44  GLY DDD CA  
3792 C C   . GLY D 42  ? 0.974 1.732 1.471 0.373  0.163  -0.023 44  GLY DDD C   
3793 O O   . GLY D 42  ? 0.963 1.788 1.520 0.391  0.157  -0.005 44  GLY DDD O   
3794 N N   . GLU D 43  ? 1.022 1.678 1.919 0.186  0.237  -0.095 45  GLU DDD N   
3795 C CA  . GLU D 43  ? 0.977 1.639 1.873 0.185  0.166  -0.088 45  GLU DDD CA  
3796 C C   . GLU D 43  ? 0.934 1.590 1.797 0.140  0.147  -0.080 45  GLU DDD C   
3797 O O   . GLU D 43  ? 0.934 1.582 1.782 0.113  0.190  -0.078 45  GLU DDD O   
3798 C CB  . GLU D 43  ? 1.005 1.590 1.805 0.209  0.140  -0.084 45  GLU DDD CB  
3799 C CG  . GLU D 43  ? 1.052 1.634 1.882 0.256  0.155  -0.092 45  GLU DDD CG  
3800 C CD  . GLU D 43  ? 1.108 1.627 1.869 0.267  0.209  -0.100 45  GLU DDD CD  
3801 O OE1 . GLU D 43  ? 1.115 1.644 1.875 0.248  0.258  -0.104 45  GLU DDD OE1 
3802 O OE2 . GLU D 43  ? 1.145 1.602 1.850 0.294  0.202  -0.103 45  GLU DDD OE2 
3803 N N   . GLU D 44  ? 0.907 1.565 1.759 0.136  0.088  -0.075 46  GLU DDD N   
3804 C CA  . GLU D 44  ? 0.876 1.527 1.697 0.098  0.065  -0.069 46  GLU DDD CA  
3805 C C   . GLU D 44  ? 0.866 1.439 1.565 0.095  0.039  -0.057 46  GLU DDD C   
3806 O O   . GLU D 44  ? 0.882 1.420 1.543 0.123  0.025  -0.054 46  GLU DDD O   
3807 C CB  . GLU D 44  ? 0.850 1.572 1.759 0.093  0.019  -0.076 46  GLU DDD CB  
3808 C CG  . GLU D 44  ? 0.861 1.602 1.792 0.130  -0.030 -0.077 46  GLU DDD CG  
3809 C CD  . GLU D 44  ? 0.842 1.651 1.848 0.127  -0.082 -0.086 46  GLU DDD CD  
3810 O OE1 . GLU D 44  ? 0.820 1.630 1.815 0.093  -0.096 -0.088 46  GLU DDD OE1 
3811 O OE2 . GLU D 44  ? 0.833 1.692 1.908 0.160  -0.111 -0.092 46  GLU DDD OE2 
3812 N N   . ARG D 45  ? 0.842 1.388 1.489 0.063  0.036  -0.051 47  ARG DDD N   
3813 C CA  . ARG D 45  ? 0.849 1.327 1.387 0.054  0.017  -0.040 47  ARG DDD CA  
3814 C C   . ARG D 45  ? 0.837 1.308 1.360 0.075  -0.031 -0.035 47  ARG DDD C   
3815 O O   . ARG D 45  ? 0.824 1.341 1.399 0.077  -0.065 -0.038 47  ARG DDD O   
3816 C CB  . ARG D 45  ? 0.831 1.304 1.347 0.020  0.013  -0.035 47  ARG DDD CB  
3817 C CG  . ARG D 45  ? 0.853 1.259 1.266 0.007  0.022  -0.025 47  ARG DDD CG  
3818 C CD  . ARG D 45  ? 0.848 1.250 1.246 -0.023 0.026  -0.020 47  ARG DDD CD  
3819 N NE  . ARG D 45  ? 0.878 1.276 1.281 -0.036 0.074  -0.018 47  ARG DDD NE  
3820 C CZ  . ARG D 45  ? 0.887 1.266 1.265 -0.059 0.087  -0.011 47  ARG DDD CZ  
3821 N NH1 . ARG D 45  ? 0.859 1.226 1.211 -0.072 0.054  -0.006 47  ARG DDD NH1 
3822 N NH2 . ARG D 45  ? 0.915 1.286 1.294 -0.069 0.134  -0.006 47  ARG DDD NH2 
3823 N N   . GLU D 46  ? 0.843 1.255 1.295 0.088  -0.033 -0.029 48  GLU DDD N   
3824 C CA  . GLU D 46  ? 0.832 1.219 1.250 0.104  -0.073 -0.019 48  GLU DDD CA  
3825 C C   . GLU D 46  ? 0.828 1.152 1.153 0.086  -0.076 -0.010 48  GLU DDD C   
3826 O O   . GLU D 46  ? 0.845 1.133 1.128 0.077  -0.048 -0.014 48  GLU DDD O   
3827 C CB  . GLU D 46  ? 0.875 1.250 1.310 0.142  -0.071 -0.020 48  GLU DDD CB  
3828 C CG  . GLU D 46  ? 0.923 1.236 1.302 0.147  -0.040 -0.024 48  GLU DDD CG  
3829 C CD  . GLU D 46  ? 0.984 1.265 1.362 0.183  -0.045 -0.022 48  GLU DDD CD  
3830 O OE1 . GLU D 46  ? 1.006 1.320 1.436 0.209  -0.069 -0.018 48  GLU DDD OE1 
3831 O OE2 . GLU D 46  ? 1.031 1.249 1.353 0.186  -0.026 -0.027 48  GLU DDD OE2 
3832 N N   . CYS D 47  ? 0.805 1.120 1.101 0.082  -0.110 0.001  49  CYS DDD N   
3833 C CA  . CYS D 47  ? 0.802 1.063 1.021 0.068  -0.116 0.011  49  CYS DDD CA  
3834 C C   . CYS D 47  ? 0.834 1.043 1.021 0.086  -0.112 0.015  49  CYS DDD C   
3835 O O   . CYS D 47  ? 0.858 1.072 1.071 0.113  -0.125 0.019  49  CYS DDD O   
3836 C CB  . CYS D 47  ? 0.786 1.056 0.989 0.061  -0.149 0.022  49  CYS DDD CB  
3837 S SG  . CYS D 47  ? 0.810 1.031 0.936 0.038  -0.150 0.033  49  CYS DDD SG  
3838 N N   . VAL D 48  ? 0.846 1.007 0.981 0.073  -0.097 0.012  50  VAL DDD N   
3839 C CA  . VAL D 48  ? 0.892 0.995 0.994 0.085  -0.091 0.011  50  VAL DDD CA  
3840 C C   . VAL D 48  ? 0.883 0.946 0.937 0.068  -0.108 0.024  50  VAL DDD C   
3841 O O   . VAL D 48  ? 0.912 0.930 0.949 0.080  -0.113 0.031  50  VAL DDD O   
3842 C CB  . VAL D 48  ? 0.934 1.010 1.016 0.084  -0.061 -0.007 50  VAL DDD CB  
3843 C CG1 . VAL D 48  ? 0.947 1.060 1.083 0.105  -0.038 -0.017 50  VAL DDD CG1 
3844 C CG2 . VAL D 48  ? 0.922 0.991 0.962 0.055  -0.053 -0.011 50  VAL DDD CG2 
3845 N N   . ALA D 49  ? 0.841 0.917 0.874 0.043  -0.115 0.028  51  ALA DDD N   
3846 C CA  . ALA D 49  ? 0.835 0.886 0.833 0.026  -0.129 0.040  51  ALA DDD CA  
3847 C C   . ALA D 49  ? 0.782 0.869 0.777 0.007  -0.138 0.045  51  ALA DDD C   
3848 O O   . ALA D 49  ? 0.774 0.889 0.781 0.000  -0.129 0.036  51  ALA DDD O   
3849 C CB  . ALA D 49  ? 0.871 0.874 0.833 0.011  -0.119 0.031  51  ALA DDD CB  
3850 N N   . SER D 50  ? 0.769 0.853 0.749 0.001  -0.152 0.061  52  SER DDD N   
3851 C CA  . SER D 50  ? 0.736 0.846 0.708 -0.015 -0.160 0.065  52  SER DDD CA  
3852 C C   . SER D 50  ? 0.746 0.832 0.692 -0.028 -0.163 0.078  52  SER DDD C   
3853 O O   . SER D 50  ? 0.763 0.814 0.699 -0.022 -0.162 0.088  52  SER DDD O   
3854 C CB  . SER D 50  ? 0.714 0.862 0.707 -0.004 -0.173 0.069  52  SER DDD CB  
3855 O OG  . SER D 50  ? 0.744 0.881 0.729 0.013  -0.186 0.083  52  SER DDD OG  
3856 N N   . ILE D 51  ? 0.729 0.832 0.666 -0.045 -0.164 0.079  53  ILE DDD N   
3857 C CA  . ILE D 51  ? 0.752 0.843 0.674 -0.061 -0.164 0.089  53  ILE DDD CA  
3858 C C   . ILE D 51  ? 0.734 0.857 0.653 -0.064 -0.168 0.095  53  ILE DDD C   
3859 O O   . ILE D 51  ? 0.707 0.856 0.634 -0.065 -0.170 0.086  53  ILE DDD O   
3860 C CB  . ILE D 51  ? 0.760 0.835 0.678 -0.079 -0.160 0.078  53  ILE DDD CB  
3861 C CG1 . ILE D 51  ? 0.777 0.841 0.693 -0.097 -0.159 0.086  53  ILE DDD CG1 
3862 C CG2 . ILE D 51  ? 0.736 0.835 0.652 -0.083 -0.160 0.065  53  ILE DDD CG2 
3863 C CD1 . ILE D 51  ? 0.813 0.854 0.728 -0.114 -0.161 0.072  53  ILE DDD CD1 
3864 N N   . GLY D 52  ? 0.765 0.884 0.674 -0.066 -0.167 0.111  54  GLY DDD N   
3865 C CA  . GLY D 52  ? 0.755 0.899 0.656 -0.068 -0.167 0.117  54  GLY DDD CA  
3866 C C   . GLY D 52  ? 0.732 0.892 0.643 -0.085 -0.163 0.110  54  GLY DDD C   
3867 O O   . GLY D 52  ? 0.715 0.864 0.636 -0.098 -0.162 0.104  54  GLY DDD O   
3868 N N   . TRP D 53  ? 0.721 0.907 0.630 -0.083 -0.163 0.110  55  TRP DDD N   
3869 C CA  . TRP D 53  ? 0.711 0.917 0.632 -0.093 -0.162 0.105  55  TRP DDD CA  
3870 C C   . TRP D 53  ? 0.733 0.938 0.670 -0.110 -0.157 0.110  55  TRP DDD C   
3871 O O   . TRP D 53  ? 0.724 0.939 0.673 -0.119 -0.163 0.101  55  TRP DDD O   
3872 C CB  . TRP D 53  ? 0.707 0.934 0.621 -0.084 -0.160 0.106  55  TRP DDD CB  
3873 C CG  . TRP D 53  ? 0.736 0.964 0.638 -0.081 -0.149 0.121  55  TRP DDD CG  
3874 C CD1 . TRP D 53  ? 0.772 0.982 0.650 -0.071 -0.147 0.132  55  TRP DDD CD1 
3875 C CD2 . TRP D 53  ? 0.753 1.001 0.662 -0.084 -0.137 0.127  55  TRP DDD CD2 
3876 N NE1 . TRP D 53  ? 0.798 1.011 0.661 -0.070 -0.132 0.146  55  TRP DDD NE1 
3877 C CE2 . TRP D 53  ? 0.782 1.021 0.668 -0.078 -0.124 0.142  55  TRP DDD CE2 
3878 C CE3 . TRP D 53  ? 0.723 0.996 0.656 -0.089 -0.135 0.122  55  TRP DDD CE3 
3879 C CZ2 . TRP D 53  ? 0.804 1.059 0.691 -0.078 -0.104 0.152  55  TRP DDD CZ2 
3880 C CZ3 . TRP D 53  ? 0.763 1.057 0.705 -0.088 -0.118 0.130  55  TRP DDD CZ3 
3881 C CH2 . TRP D 53  ? 0.791 1.076 0.711 -0.084 -0.101 0.145  55  TRP DDD CH2 
3882 N N   . ARG D 54  ? 0.747 0.940 0.682 -0.114 -0.146 0.125  56  ARG DDD N   
3883 C CA  . ARG D 54  ? 0.752 0.944 0.711 -0.134 -0.137 0.132  56  ARG DDD CA  
3884 C C   . ARG D 54  ? 0.768 0.927 0.733 -0.145 -0.143 0.124  56  ARG DDD C   
3885 O O   . ARG D 54  ? 0.813 0.970 0.803 -0.166 -0.140 0.124  56  ARG DDD O   
3886 C CB  . ARG D 54  ? 0.801 0.984 0.752 -0.133 -0.118 0.153  56  ARG DDD CB  
3887 C CG  . ARG D 54  ? 0.805 1.022 0.759 -0.129 -0.105 0.160  56  ARG DDD CG  
3888 C CD  . ARG D 54  ? 0.858 1.056 0.785 -0.122 -0.084 0.183  56  ARG DDD CD  
3889 N NE  . ARG D 54  ? 0.872 1.099 0.802 -0.120 -0.064 0.191  56  ARG DDD NE  
3890 C CZ  . ARG D 54  ? 0.911 1.126 0.806 -0.109 -0.043 0.211  56  ARG DDD CZ  
3891 N NH1 . ARG D 54  ? 0.949 1.122 0.802 -0.100 -0.042 0.226  56  ARG DDD NH1 
3892 N NH2 . ARG D 54  ? 0.929 1.172 0.827 -0.105 -0.021 0.216  56  ARG DDD NH2 
3893 N N   . GLY D 55  ? 0.772 0.905 0.716 -0.133 -0.149 0.119  57  GLY DDD N   
3894 C CA  . GLY D 55  ? 0.789 0.884 0.732 -0.139 -0.151 0.110  57  GLY DDD CA  
3895 C C   . GLY D 55  ? 0.817 0.874 0.758 -0.143 -0.139 0.128  57  GLY DDD C   
3896 O O   . GLY D 55  ? 0.835 0.856 0.782 -0.154 -0.139 0.121  57  GLY DDD O   
3897 N N   . VAL D 56  ? 0.827 0.886 0.755 -0.133 -0.129 0.149  58  VAL DDD N   
3898 C CA  . VAL D 56  ? 0.885 0.905 0.802 -0.134 -0.113 0.172  58  VAL DDD CA  
3899 C C   . VAL D 56  ? 0.914 0.899 0.803 -0.108 -0.119 0.178  58  VAL DDD C   
3900 O O   . VAL D 56  ? 0.969 0.905 0.856 -0.109 -0.114 0.184  58  VAL DDD O   
3901 C CB  . VAL D 56  ? 0.902 0.940 0.809 -0.133 -0.097 0.194  58  VAL DDD CB  
3902 C CG1 . VAL D 56  ? 0.958 0.949 0.837 -0.126 -0.080 0.223  58  VAL DDD CG1 
3903 C CG2 . VAL D 56  ? 0.889 0.960 0.834 -0.159 -0.087 0.191  58  VAL DDD CG2 
3904 N N   . ARG D 57  ? 0.894 0.904 0.768 -0.085 -0.131 0.175  59  ARG DDD N   
3905 C CA  . ARG D 57  ? 0.900 0.893 0.758 -0.057 -0.141 0.178  59  ARG DDD CA  
3906 C C   . ARG D 57  ? 0.868 0.867 0.746 -0.053 -0.151 0.153  59  ARG DDD C   
3907 O O   . ARG D 57  ? 0.831 0.865 0.724 -0.062 -0.155 0.136  59  ARG DDD O   
3908 C CB  . ARG D 57  ? 0.880 0.902 0.716 -0.035 -0.151 0.184  59  ARG DDD CB  
3909 C CG  . ARG D 57  ? 0.904 0.918 0.708 -0.034 -0.139 0.209  59  ARG DDD CG  
3910 C CD  . ARG D 57  ? 0.882 0.934 0.667 -0.021 -0.149 0.204  59  ARG DDD CD  
3911 N NE  . ARG D 57  ? 0.824 0.915 0.635 -0.037 -0.149 0.184  59  ARG DDD NE  
3912 C CZ  . ARG D 57  ? 0.801 0.924 0.606 -0.030 -0.159 0.172  59  ARG DDD CZ  
3913 N NH1 . ARG D 57  ? 0.832 0.957 0.605 -0.007 -0.172 0.175  59  ARG DDD NH1 
3914 N NH2 . ARG D 57  ? 0.766 0.918 0.595 -0.043 -0.157 0.157  59  ARG DDD NH2 
3915 N N   . THR D 58  ? 0.899 0.863 0.777 -0.039 -0.152 0.153  60  THR DDD N   
3916 C CA  . THR D 58  ? 0.889 0.856 0.784 -0.030 -0.156 0.131  60  THR DDD CA  
3917 C C   . THR D 58  ? 0.919 0.882 0.816 0.003  -0.164 0.138  60  THR DDD C   
3918 O O   . THR D 58  ? 0.951 0.885 0.828 0.017  -0.166 0.160  60  THR DDD O   
3919 C CB  . THR D 58  ? 0.918 0.845 0.817 -0.045 -0.147 0.118  60  THR DDD CB  
3920 O OG1 . THR D 58  ? 0.968 0.840 0.856 -0.042 -0.140 0.135  60  THR DDD OG1 
3921 C CG2 . THR D 58  ? 0.897 0.837 0.800 -0.076 -0.146 0.107  60  THR DDD CG2 
3922 N N   . TRP D 59  ? 0.908 0.899 0.829 0.016  -0.169 0.120  61  TRP DDD N   
3923 C CA  . TRP D 59  ? 0.925 0.921 0.863 0.048  -0.177 0.121  61  TRP DDD CA  
3924 C C   . TRP D 59  ? 0.922 0.910 0.883 0.052  -0.165 0.099  61  TRP DDD C   
3925 O O   . TRP D 59  ? 0.889 0.896 0.855 0.033  -0.157 0.082  61  TRP DDD O   
3926 C CB  . TRP D 59  ? 0.898 0.950 0.852 0.059  -0.195 0.119  61  TRP DDD CB  
3927 C CG  . TRP D 59  ? 0.909 0.980 0.894 0.091  -0.208 0.116  61  TRP DDD CG  
3928 C CD1 . TRP D 59  ? 0.960 1.026 0.936 0.120  -0.226 0.132  61  TRP DDD CD1 
3929 C CD2 . TRP D 59  ? 0.890 0.994 0.923 0.099  -0.202 0.095  61  TRP DDD CD2 
3930 N NE1 . TRP D 59  ? 0.966 1.063 0.987 0.146  -0.237 0.122  61  TRP DDD NE1 
3931 C CE2 . TRP D 59  ? 0.918 1.040 0.979 0.132  -0.220 0.099  61  TRP DDD CE2 
3932 C CE3 . TRP D 59  ? 0.862 0.980 0.916 0.082  -0.183 0.075  61  TRP DDD CE3 
3933 C CZ2 . TRP D 59  ? 0.902 1.063 1.021 0.148  -0.218 0.082  61  TRP DDD CZ2 
3934 C CZ3 . TRP D 59  ? 0.858 1.008 0.961 0.097  -0.177 0.061  61  TRP DDD CZ3 
3935 C CH2 . TRP D 59  ? 0.871 1.045 1.011 0.128  -0.193 0.063  61  TRP DDD CH2 
3936 N N   . TYR D 60  ? 0.957 0.916 0.926 0.077  -0.163 0.101  62  TYR DDD N   
3937 C CA  . TYR D 60  ? 0.971 0.920 0.961 0.088  -0.149 0.081  62  TYR DDD CA  
3938 C C   . TYR D 60  ? 0.987 0.961 1.015 0.126  -0.157 0.082  62  TYR DDD C   
3939 O O   . TYR D 60  ? 1.027 0.989 1.048 0.147  -0.173 0.103  62  TYR DDD O   
3940 C CB  . TYR D 60  ? 1.023 0.901 0.987 0.082  -0.136 0.077  62  TYR DDD CB  
3941 C CG  . TYR D 60  ? 1.015 0.872 0.950 0.044  -0.132 0.074  62  TYR DDD CG  
3942 C CD1 . TYR D 60  ? 0.999 0.864 0.929 0.025  -0.124 0.051  62  TYR DDD CD1 
3943 C CD2 . TYR D 60  ? 1.030 0.862 0.946 0.029  -0.137 0.094  62  TYR DDD CD2 
3944 C CE1 . TYR D 60  ? 1.000 0.852 0.909 -0.006 -0.125 0.046  62  TYR DDD CE1 
3945 C CE2 . TYR D 60  ? 1.026 0.848 0.929 -0.005 -0.134 0.090  62  TYR DDD CE2 
3946 C CZ  . TYR D 60  ? 1.015 0.849 0.917 -0.022 -0.131 0.065  62  TYR DDD CZ  
3947 O OH  . TYR D 60  ? 1.012 0.842 0.905 -0.054 -0.134 0.059  62  TYR DDD OH  
3948 N N   . ALA D 61  ? 0.967 0.977 1.034 0.134  -0.146 0.063  63  ALA DDD N   
3949 C CA  . ALA D 61  ? 0.983 1.017 1.098 0.171  -0.148 0.059  63  ALA DDD CA  
3950 C C   . ALA D 61  ? 1.056 1.023 1.155 0.195  -0.139 0.062  63  ALA DDD C   
3951 O O   . ALA D 61  ? 1.096 1.007 1.158 0.177  -0.122 0.054  63  ALA DDD O   
3952 C CB  . ALA D 61  ? 0.945 1.028 1.105 0.169  -0.128 0.036  63  ALA DDD CB  
3953 N N   . ASP D 62  ? 1.091 1.060 1.216 0.234  -0.152 0.073  64  ASP DDD N   
3954 C CA  . ASP D 62  ? 1.163 1.063 1.275 0.263  -0.146 0.080  64  ASP DDD CA  
3955 C C   . ASP D 62  ? 1.187 1.060 1.305 0.264  -0.114 0.053  64  ASP DDD C   
3956 O O   . ASP D 62  ? 1.242 1.036 1.323 0.264  -0.102 0.051  64  ASP DDD O   
3957 C CB  . ASP D 62  ? 1.189 1.111 1.338 0.311  -0.167 0.094  64  ASP DDD CB  
3958 C CG  . ASP D 62  ? 1.198 1.119 1.317 0.318  -0.199 0.124  64  ASP DDD CG  
3959 O OD1 . ASP D 62  ? 1.201 1.082 1.265 0.288  -0.197 0.138  64  ASP DDD OD1 
3960 O OD2 . ASP D 62  ? 1.205 1.165 1.354 0.353  -0.225 0.133  64  ASP DDD OD2 
3961 N N   . SER D 63  ? 1.150 1.083 1.311 0.263  -0.098 0.032  65  SER DDD N   
3962 C CA  . SER D 63  ? 1.182 1.099 1.350 0.270  -0.064 0.005  65  SER DDD CA  
3963 C C   . SER D 63  ? 1.207 1.064 1.309 0.235  -0.048 -0.009 65  SER DDD C   
3964 O O   . SER D 63  ? 1.257 1.075 1.345 0.245  -0.023 -0.031 65  SER DDD O   
3965 C CB  . SER D 63  ? 1.134 1.132 1.360 0.273  -0.049 -0.009 65  SER DDD CB  
3966 O OG  . SER D 63  ? 1.074 1.111 1.290 0.234  -0.054 -0.009 65  SER DDD OG  
3967 N N   . VAL D 64  ? 1.178 1.031 1.244 0.199  -0.063 0.001  66  VAL DDD N   
3968 C CA  . VAL D 64  ? 1.191 1.000 1.202 0.163  -0.055 -0.013 66  VAL DDD CA  
3969 C C   . VAL D 64  ? 1.218 0.973 1.193 0.144  -0.072 0.003  66  VAL DDD C   
3970 O O   . VAL D 64  ? 1.225 0.945 1.162 0.114  -0.069 -0.009 66  VAL DDD O   
3971 C CB  . VAL D 64  ? 1.129 0.993 1.137 0.135  -0.053 -0.019 66  VAL DDD CB  
3972 C CG1 . VAL D 64  ? 1.112 1.029 1.158 0.150  -0.031 -0.031 66  VAL DDD CG1 
3973 C CG2 . VAL D 64  ? 1.073 0.976 1.087 0.117  -0.077 0.004  66  VAL DDD CG2 
3974 N N   . LYS D 65  ? 1.226 0.973 1.212 0.160  -0.088 0.030  67  LYS DDD N   
3975 C CA  . LYS D 65  ? 1.248 0.949 1.202 0.140  -0.100 0.051  67  LYS DDD CA  
3976 C C   . LYS D 65  ? 1.318 0.930 1.244 0.134  -0.088 0.040  67  LYS DDD C   
3977 O O   . LYS D 65  ? 1.365 0.940 1.298 0.164  -0.076 0.030  67  LYS DDD O   
3978 C CB  . LYS D 65  ? 1.267 0.978 1.232 0.165  -0.117 0.083  67  LYS DDD CB  
3979 C CG  . LYS D 65  ? 1.285 0.971 1.218 0.143  -0.126 0.110  67  LYS DDD CG  
3980 C CD  . LYS D 65  ? 1.294 1.001 1.227 0.170  -0.145 0.141  67  LYS DDD CD  
3981 C CE  . LYS D 65  ? 1.349 0.999 1.241 0.160  -0.145 0.173  67  LYS DDD CE  
3982 N NZ  . LYS D 65  ? 1.397 1.035 1.278 0.201  -0.160 0.202  67  LYS DDD NZ  
3983 N N   . GLY D 66  ? 1.331 0.910 1.229 0.095  -0.090 0.040  68  GLY DDD N   
3984 C CA  . GLY D 66  ? 1.402 0.897 1.277 0.079  -0.081 0.026  68  GLY DDD CA  
3985 C C   . GLY D 66  ? 1.410 0.898 1.267 0.064  -0.073 -0.014 68  GLY DDD C   
3986 O O   . GLY D 66  ? 1.454 0.882 1.289 0.040  -0.073 -0.031 68  GLY DDD O   
3987 N N   . ARG D 67  ? 1.374 0.919 1.240 0.078  -0.068 -0.029 69  ARG DDD N   
3988 C CA  . ARG D 67  ? 1.395 0.934 1.235 0.073  -0.056 -0.065 69  ARG DDD CA  
3989 C C   . ARG D 67  ? 1.338 0.936 1.168 0.044  -0.065 -0.069 69  ARG DDD C   
3990 O O   . ARG D 67  ? 1.363 0.941 1.157 0.026  -0.065 -0.096 69  ARG DDD O   
3991 C CB  . ARG D 67  ? 1.404 0.958 1.261 0.114  -0.035 -0.076 69  ARG DDD CB  
3992 C CG  . ARG D 67  ? 1.463 0.964 1.336 0.149  -0.028 -0.071 69  ARG DDD CG  
3993 C CD  . ARG D 67  ? 1.489 0.998 1.378 0.189  -0.003 -0.089 69  ARG DDD CD  
3994 N NE  . ARG D 67  ? 1.410 1.012 1.340 0.201  0.002  -0.081 69  ARG DDD NE  
3995 C CZ  . ARG D 67  ? 1.384 1.027 1.306 0.193  0.018  -0.099 69  ARG DDD CZ  
3996 N NH1 . ARG D 67  ? 1.432 1.034 1.300 0.176  0.030  -0.127 69  ARG DDD NH1 
3997 N NH2 . ARG D 67  ? 1.317 1.041 1.286 0.201  0.023  -0.089 69  ARG DDD NH2 
3998 N N   . PHE D 68  ? 1.275 0.940 1.131 0.043  -0.073 -0.046 70  PHE DDD N   
3999 C CA  . PHE D 68  ? 1.208 0.930 1.059 0.019  -0.081 -0.045 70  PHE DDD CA  
4000 C C   . PHE D 68  ? 1.174 0.907 1.030 -0.008 -0.099 -0.024 70  PHE DDD C   
4001 O O   . PHE D 68  ? 1.166 0.894 1.041 -0.000 -0.104 -0.000 70  PHE DDD O   
4002 C CB  . PHE D 68  ? 1.156 0.946 1.037 0.036  -0.074 -0.036 70  PHE DDD CB  
4003 C CG  . PHE D 68  ? 1.177 0.973 1.059 0.059  -0.049 -0.055 70  PHE DDD CG  
4004 C CD1 . PHE D 68  ? 1.249 0.990 1.107 0.073  -0.034 -0.078 70  PHE DDD CD1 
4005 C CD2 . PHE D 68  ? 1.133 0.992 1.043 0.066  -0.040 -0.051 70  PHE DDD CD2 
4006 C CE1 . PHE D 68  ? 1.274 1.023 1.132 0.095  -0.006 -0.095 70  PHE DDD CE1 
4007 C CE2 . PHE D 68  ? 1.160 1.028 1.077 0.085  -0.012 -0.066 70  PHE DDD CE2 
4008 C CZ  . PHE D 68  ? 1.223 1.039 1.114 0.101  0.006  -0.087 70  PHE DDD CZ  
4009 N N   . THR D 69  ? 1.155 0.901 0.994 -0.037 -0.109 -0.033 71  THR DDD N   
4010 C CA  . THR D 69  ? 1.114 0.885 0.963 -0.062 -0.124 -0.015 71  THR DDD CA  
4011 C C   . THR D 69  ? 1.050 0.883 0.899 -0.069 -0.129 -0.014 71  THR DDD C   
4012 O O   . THR D 69  ? 1.054 0.889 0.878 -0.073 -0.129 -0.034 71  THR DDD O   
4013 C CB  . THR D 69  ? 1.155 0.886 0.995 -0.092 -0.134 -0.027 71  THR DDD CB  
4014 O OG1 . THR D 69  ? 1.227 0.893 1.067 -0.085 -0.126 -0.028 71  THR DDD OG1 
4015 C CG2 . THR D 69  ? 1.115 0.876 0.975 -0.118 -0.144 -0.009 71  THR DDD CG2 
4016 N N   . ILE D 70  ? 0.995 0.871 0.866 -0.067 -0.134 0.009  72  ILE DDD N   
4017 C CA  . ILE D 70  ? 0.938 0.867 0.812 -0.076 -0.140 0.013  72  ILE DDD CA  
4018 C C   . ILE D 70  ? 0.930 0.864 0.807 -0.101 -0.152 0.021  72  ILE DDD C   
4019 O O   . ILE D 70  ? 0.973 0.888 0.862 -0.107 -0.151 0.035  72  ILE DDD O   
4020 C CB  . ILE D 70  ? 0.896 0.866 0.792 -0.059 -0.137 0.029  72  ILE DDD CB  
4021 C CG1 . ILE D 70  ? 0.855 0.868 0.749 -0.066 -0.140 0.029  72  ILE DDD CG1 
4022 C CG2 . ILE D 70  ? 0.898 0.868 0.806 -0.056 -0.143 0.051  72  ILE DDD CG2 
4023 C CD1 . ILE D 70  ? 0.817 0.868 0.736 -0.052 -0.138 0.037  72  ILE DDD CD1 
4024 N N   . SER D 71  ? 0.892 0.851 0.760 -0.115 -0.161 0.012  73  SER DDD N   
4025 C CA  . SER D 71  ? 0.872 0.851 0.754 -0.137 -0.173 0.017  73  SER DDD CA  
4026 C C   . SER D 71  ? 0.836 0.858 0.712 -0.136 -0.180 0.016  73  SER DDD C   
4027 O O   . SER D 71  ? 0.837 0.862 0.693 -0.122 -0.174 0.010  73  SER DDD O   
4028 C CB  . SER D 71  ? 0.913 0.861 0.793 -0.158 -0.183 -0.001 73  SER DDD CB  
4029 O OG  . SER D 71  ? 0.940 0.872 0.785 -0.154 -0.189 -0.025 73  SER DDD OG  
4030 N N   . ARG D 72  ? 0.822 0.875 0.717 -0.149 -0.189 0.024  74  ARG DDD N   
4031 C CA  . ARG D 72  ? 0.791 0.882 0.682 -0.145 -0.196 0.026  74  ARG DDD CA  
4032 C C   . ARG D 72  ? 0.780 0.894 0.689 -0.162 -0.213 0.022  74  ARG DDD C   
4033 O O   . ARG D 72  ? 0.771 0.884 0.709 -0.179 -0.213 0.025  74  ARG DDD O   
4034 C CB  . ARG D 72  ? 0.749 0.866 0.653 -0.134 -0.186 0.044  74  ARG DDD CB  
4035 C CG  . ARG D 72  ? 0.737 0.865 0.665 -0.140 -0.182 0.060  74  ARG DDD CG  
4036 C CD  . ARG D 72  ? 0.703 0.847 0.631 -0.125 -0.174 0.073  74  ARG DDD CD  
4037 N NE  . ARG D 72  ? 0.668 0.839 0.593 -0.119 -0.177 0.071  74  ARG DDD NE  
4038 C CZ  . ARG D 72  ? 0.651 0.832 0.572 -0.106 -0.173 0.074  74  ARG DDD CZ  
4039 N NH1 . ARG D 72  ? 0.637 0.835 0.556 -0.103 -0.175 0.072  74  ARG DDD NH1 
4040 N NH2 . ARG D 72  ? 0.663 0.837 0.585 -0.097 -0.170 0.077  74  ARG DDD NH2 
4041 N N   . ASP D 73  ? 0.786 0.918 0.679 -0.157 -0.225 0.015  75  ASP DDD N   
4042 C CA  . ASP D 73  ? 0.802 0.966 0.714 -0.167 -0.246 0.011  75  ASP DDD CA  
4043 C C   . ASP D 73  ? 0.768 0.967 0.685 -0.153 -0.244 0.026  75  ASP DDD C   
4044 O O   . ASP D 73  ? 0.796 0.992 0.680 -0.139 -0.249 0.024  75  ASP DDD O   
4045 C CB  . ASP D 73  ? 0.846 0.994 0.726 -0.169 -0.268 -0.011 75  ASP DDD CB  
4046 C CG  . ASP D 73  ? 0.871 1.053 0.776 -0.180 -0.297 -0.020 75  ASP DDD CG  
4047 O OD1 . ASP D 73  ? 0.856 1.079 0.811 -0.186 -0.296 -0.008 75  ASP DDD OD1 
4048 O OD2 . ASP D 73  ? 0.913 1.082 0.786 -0.181 -0.320 -0.040 75  ASP DDD OD2 
4049 N N   . ASN D 74  ? 0.719 0.943 0.672 -0.155 -0.234 0.040  76  ASN DDD N   
4050 C CA  . ASN D 74  ? 0.678 0.929 0.636 -0.140 -0.227 0.053  76  ASN DDD CA  
4051 C C   . ASN D 74  ? 0.675 0.951 0.634 -0.132 -0.245 0.050  76  ASN DDD C   
4052 O O   . ASN D 74  ? 0.674 0.947 0.609 -0.116 -0.243 0.055  76  ASN DDD O   
4053 C CB  . ASN D 74  ? 0.658 0.928 0.647 -0.143 -0.211 0.067  76  ASN DDD CB  
4054 C CG  . ASN D 74  ? 0.661 0.906 0.632 -0.136 -0.194 0.074  76  ASN DDD CG  
4055 O OD1 . ASN D 74  ? 0.666 0.884 0.613 -0.131 -0.193 0.069  76  ASN DDD OD1 
4056 N ND2 . ASN D 74  ? 0.654 0.911 0.637 -0.134 -0.181 0.086  76  ASN DDD ND2 
4057 N N   . PRO D 75  ? 0.681 0.982 0.669 -0.144 -0.264 0.042  77  PRO DDD N   
4058 C CA  . PRO D 75  ? 0.688 1.014 0.675 -0.132 -0.288 0.038  77  PRO DDD CA  
4059 C C   . PRO D 75  ? 0.719 1.012 0.643 -0.118 -0.299 0.033  77  PRO DDD C   
4060 O O   . PRO D 75  ? 0.730 1.035 0.641 -0.101 -0.311 0.038  77  PRO DDD O   
4061 C CB  . PRO D 75  ? 0.707 1.063 0.740 -0.152 -0.310 0.025  77  PRO DDD CB  
4062 C CG  . PRO D 75  ? 0.690 1.046 0.763 -0.172 -0.287 0.031  77  PRO DDD CG  
4063 C CD  . PRO D 75  ? 0.683 0.991 0.711 -0.167 -0.266 0.036  77  PRO DDD CD  
4064 N N   . GLN D 76  ? 0.748 1.000 0.635 -0.124 -0.292 0.024  78  GLN DDD N   
4065 C CA  . GLN D 76  ? 0.795 1.011 0.616 -0.111 -0.296 0.017  78  GLN DDD CA  
4066 C C   . GLN D 76  ? 0.771 0.959 0.565 -0.101 -0.266 0.028  78  GLN DDD C   
4067 O O   . GLN D 76  ? 0.799 0.956 0.541 -0.091 -0.261 0.026  78  GLN DDD O   
4068 C CB  . GLN D 76  ? 0.851 1.040 0.649 -0.124 -0.308 -0.004 78  GLN DDD CB  
4069 C CG  . GLN D 76  ? 0.893 1.109 0.713 -0.134 -0.344 -0.020 78  GLN DDD CG  
4070 C CD  . GLN D 76  ? 0.943 1.170 0.728 -0.115 -0.370 -0.019 78  GLN DDD CD  
4071 O OE1 . GLN D 76  ? 1.005 1.196 0.718 -0.099 -0.368 -0.020 78  GLN DDD OE1 
4072 N NE2 . GLN D 76  ? 0.931 1.208 0.764 -0.114 -0.391 -0.015 78  GLN DDD NE2 
4073 N N   . ASN D 77  ? 0.731 0.930 0.558 -0.103 -0.247 0.040  79  ASN DDD N   
4074 C CA  . ASN D 77  ? 0.710 0.891 0.526 -0.095 -0.222 0.048  79  ASN DDD CA  
4075 C C   . ASN D 77  ? 0.747 0.895 0.532 -0.096 -0.211 0.038  79  ASN DDD C   
4076 O O   . ASN D 77  ? 0.768 0.896 0.523 -0.087 -0.196 0.042  79  ASN DDD O   
4077 C CB  . ASN D 77  ? 0.696 0.875 0.494 -0.081 -0.218 0.059  79  ASN DDD CB  
4078 C CG  . ASN D 77  ? 0.661 0.871 0.492 -0.076 -0.225 0.067  79  ASN DDD CG  
4079 O OD1 . ASN D 77  ? 0.651 0.884 0.520 -0.084 -0.224 0.067  79  ASN DDD OD1 
4080 N ND2 . ASN D 77  ? 0.675 0.882 0.488 -0.061 -0.230 0.075  79  ASN DDD ND2 
4081 N N   . THR D 78  ? 0.772 0.910 0.565 -0.107 -0.214 0.027  80  THR DDD N   
4082 C CA  . THR D 78  ? 0.815 0.919 0.579 -0.105 -0.203 0.015  80  THR DDD CA  
4083 C C   . THR D 78  ? 0.809 0.907 0.605 -0.112 -0.194 0.013  80  THR DDD C   
4084 O O   . THR D 78  ? 0.793 0.904 0.620 -0.124 -0.205 0.015  80  THR DDD O   
4085 C CB  . THR D 78  ? 0.857 0.942 0.581 -0.107 -0.222 -0.002 80  THR DDD CB  
4086 O OG1 . THR D 78  ? 0.876 0.966 0.566 -0.097 -0.230 0.004  80  THR DDD OG1 
4087 C CG2 . THR D 78  ? 0.898 0.943 0.585 -0.103 -0.208 -0.017 80  THR DDD CG2 
4088 N N   . VAL D 79  ? 0.822 0.903 0.613 -0.104 -0.175 0.012  81  VAL DDD N   
4089 C CA  . VAL D 79  ? 0.825 0.893 0.639 -0.103 -0.166 0.010  81  VAL DDD CA  
4090 C C   . VAL D 79  ? 0.884 0.916 0.668 -0.098 -0.158 -0.007 81  VAL DDD C   
4091 O O   . VAL D 79  ? 0.888 0.911 0.639 -0.089 -0.146 -0.012 81  VAL DDD O   
4092 C CB  . VAL D 79  ? 0.794 0.881 0.637 -0.094 -0.153 0.023  81  VAL DDD CB  
4093 C CG1 . VAL D 79  ? 0.800 0.889 0.634 -0.084 -0.135 0.021  81  VAL DDD CG1 
4094 C CG2 . VAL D 79  ? 0.795 0.870 0.659 -0.090 -0.149 0.024  81  VAL DDD CG2 
4095 N N   . TYR D 80  ? 0.921 0.926 0.711 -0.103 -0.161 -0.016 82  TYR DDD N   
4096 C CA  . TYR D 80  ? 0.982 0.945 0.742 -0.098 -0.154 -0.036 82  TYR DDD CA  
4097 C C   . TYR D 80  ? 0.980 0.926 0.763 -0.085 -0.138 -0.034 82  TYR DDD C   
4098 O O   . TYR D 80  ? 0.966 0.924 0.784 -0.086 -0.141 -0.018 82  TYR DDD O   
4099 C CB  . TYR D 80  ? 1.027 0.966 0.774 -0.115 -0.176 -0.052 82  TYR DDD CB  
4100 C CG  . TYR D 80  ? 1.031 0.990 0.760 -0.126 -0.198 -0.057 82  TYR DDD CG  
4101 C CD1 . TYR D 80  ? 1.090 1.032 0.763 -0.119 -0.204 -0.074 82  TYR DDD CD1 
4102 C CD2 . TYR D 80  ? 0.988 0.984 0.753 -0.139 -0.214 -0.044 82  TYR DDD CD2 
4103 C CE1 . TYR D 80  ? 1.104 1.065 0.758 -0.124 -0.228 -0.077 82  TYR DDD CE1 
4104 C CE2 . TYR D 80  ? 1.002 1.022 0.758 -0.145 -0.236 -0.047 82  TYR DDD CE2 
4105 C CZ  . TYR D 80  ? 1.059 1.061 0.759 -0.137 -0.246 -0.064 82  TYR DDD CZ  
4106 O OH  . TYR D 80  ? 1.057 1.082 0.744 -0.139 -0.272 -0.066 82  TYR DDD OH  
4107 N N   . LEU D 81  ? 1.022 0.941 0.783 -0.070 -0.120 -0.048 83  LEU DDD N   
4108 C CA  . LEU D 81  ? 1.051 0.947 0.832 -0.054 -0.106 -0.051 83  LEU DDD CA  
4109 C C   . LEU D 81  ? 1.140 0.979 0.882 -0.052 -0.103 -0.077 83  LEU DDD C   
4110 O O   . LEU D 81  ? 1.175 1.001 0.885 -0.038 -0.084 -0.092 83  LEU DDD O   
4111 C CB  . LEU D 81  ? 1.027 0.951 0.830 -0.033 -0.083 -0.045 83  LEU DDD CB  
4112 C CG  . LEU D 81  ? 1.035 0.947 0.870 -0.012 -0.071 -0.044 83  LEU DDD CG  
4113 C CD1 . LEU D 81  ? 1.004 0.921 0.871 -0.014 -0.088 -0.025 83  LEU DDD CD1 
4114 C CD2 . LEU D 81  ? 1.013 0.962 0.878 0.006  -0.049 -0.042 83  LEU DDD CD2 
4115 N N   . GLN D 82  ? 1.186 0.992 0.931 -0.066 -0.119 -0.082 84  GLN DDD N   
4116 C CA  . GLN D 82  ? 1.276 1.019 0.992 -0.066 -0.117 -0.109 84  GLN DDD CA  
4117 C C   . GLN D 82  ? 1.305 1.024 1.036 -0.038 -0.094 -0.108 84  GLN DDD C   
4118 O O   . GLN D 82  ? 1.285 1.010 1.057 -0.032 -0.095 -0.087 84  GLN DDD O   
4119 C CB  . GLN D 82  ? 1.299 1.015 1.028 -0.092 -0.139 -0.111 84  GLN DDD CB  
4120 C CG  . GLN D 82  ? 1.383 1.032 1.080 -0.098 -0.143 -0.143 84  GLN DDD CG  
4121 C CD  . GLN D 82  ? 1.429 1.071 1.068 -0.099 -0.151 -0.172 84  GLN DDD CD  
4122 O OE1 . GLN D 82  ? 1.404 1.081 1.034 -0.115 -0.171 -0.172 84  GLN DDD OE1 
4123 N NE2 . GLN D 82  ? 1.507 1.103 1.104 -0.079 -0.134 -0.197 84  GLN DDD NE2 
4124 N N   . MET D 83  ? 1.372 1.069 1.072 -0.018 -0.074 -0.129 85  MET DDD N   
4125 C CA  . MET D 83  ? 1.416 1.095 1.134 0.014  -0.048 -0.131 85  MET DDD CA  
4126 C C   . MET D 83  ? 1.501 1.104 1.181 0.019  -0.043 -0.162 85  MET DDD C   
4127 O O   . MET D 83  ? 1.552 1.133 1.177 0.020  -0.037 -0.189 85  MET DDD O   
4128 C CB  . MET D 83  ? 1.418 1.137 1.139 0.035  -0.021 -0.131 85  MET DDD CB  
4129 C CG  . MET D 83  ? 1.360 1.150 1.119 0.028  -0.025 -0.105 85  MET DDD CG  
4130 S SD  . MET D 83  ? 1.372 1.206 1.145 0.048  0.012  -0.104 85  MET DDD SD  
4131 C CE  . MET D 83  ? 1.440 1.238 1.125 0.042  0.024  -0.127 85  MET DDD CE  
4132 N N   . ASN D 84  ? 1.520 1.079 1.223 0.024  -0.047 -0.158 86  ASN DDD N   
4133 C CA  . ASN D 84  ? 1.606 1.082 1.279 0.029  -0.043 -0.187 86  ASN DDD CA  
4134 C C   . ASN D 84  ? 1.642 1.097 1.339 0.070  -0.017 -0.185 86  ASN DDD C   
4135 O O   . ASN D 84  ? 1.587 1.088 1.334 0.086  -0.013 -0.156 86  ASN DDD O   
4136 C CB  . ASN D 84  ? 1.623 1.056 1.304 -0.001 -0.066 -0.184 86  ASN DDD CB  
4137 C CG  . ASN D 84  ? 1.584 1.047 1.256 -0.040 -0.093 -0.185 86  ASN DDD CG  
4138 O OD1 . ASN D 84  ? 1.587 1.083 1.227 -0.044 -0.097 -0.197 86  ASN DDD OD1 
4139 N ND2 . ASN D 84  ? 1.562 1.014 1.261 -0.068 -0.110 -0.172 86  ASN DDD ND2 
4140 N N   . ASN D 85  ? 1.738 1.126 1.400 0.087  -0.001 -0.217 87  ASN DDD N   
4141 C CA  . ASN D 85  ? 1.786 1.144 1.470 0.130  0.025  -0.219 87  ASN DDD CA  
4142 C C   . ASN D 85  ? 1.734 1.168 1.453 0.159  0.050  -0.208 87  ASN DDD C   
4143 O O   . ASN D 85  ? 1.705 1.159 1.479 0.189  0.058  -0.189 87  ASN DDD O   
4144 C CB  . ASN D 85  ? 1.786 1.116 1.513 0.135  0.013  -0.192 87  ASN DDD CB  
4145 C CG  . ASN D 85  ? 1.835 1.094 1.541 0.102  -0.008 -0.199 87  ASN DDD CG  
4146 O OD1 . ASN D 85  ? 1.871 1.108 1.535 0.072  -0.019 -0.226 87  ASN DDD OD1 
4147 N ND2 . ASN D 85  ? 1.850 1.073 1.584 0.106  -0.013 -0.174 87  ASN DDD ND2 
4148 N N   . LEU D 86  ? 1.728 1.199 1.415 0.151  0.061  -0.219 88  LEU DDD N   
4149 C CA  . LEU D 86  ? 1.693 1.237 1.415 0.173  0.089  -0.209 88  LEU DDD CA  
4150 C C   . LEU D 86  ? 1.747 1.273 1.491 0.217  0.124  -0.223 88  LEU DDD C   
4151 O O   . LEU D 86  ? 1.847 1.304 1.537 0.229  0.139  -0.255 88  LEU DDD O   
4152 C CB  . LEU D 86  ? 1.709 1.273 1.376 0.157  0.100  -0.221 88  LEU DDD CB  
4153 C CG  . LEU D 86  ? 1.637 1.262 1.316 0.126  0.078  -0.196 88  LEU DDD CG  
4154 C CD1 . LEU D 86  ? 1.643 1.237 1.286 0.092  0.039  -0.198 88  LEU DDD CD1 
4155 C CD2 . LEU D 86  ? 1.645 1.306 1.295 0.126  0.103  -0.198 88  LEU DDD CD2 
4156 N N   . LYS D 87  ? 1.814 1.145 1.418 0.100  0.219  -0.257 89  LYS DDD N   
4157 C CA  . LYS D 87  ? 1.858 1.161 1.478 0.146  0.257  -0.258 89  LYS DDD CA  
4158 C C   . LYS D 87  ? 1.798 1.178 1.454 0.163  0.262  -0.256 89  LYS DDD C   
4159 O O   . LYS D 87  ? 1.696 1.152 1.375 0.145  0.233  -0.244 89  LYS DDD O   
4160 C CB  . LYS D 87  ? 1.854 1.149 1.521 0.185  0.259  -0.231 89  LYS DDD CB  
4161 C CG  . LYS D 87  ? 1.903 1.177 1.596 0.240  0.296  -0.229 89  LYS DDD CG  
4162 C CD  . LYS D 87  ? 1.931 1.178 1.654 0.280  0.299  -0.204 89  LYS DDD CD  
4163 C CE  . LYS D 87  ? 1.992 1.207 1.734 0.335  0.338  -0.205 89  LYS DDD CE  
4164 N NZ  . LYS D 87  ? 2.019 1.210 1.788 0.379  0.338  -0.177 89  LYS DDD NZ  
4165 N N   . SER D 88  ? 1.857 1.216 1.517 0.195  0.301  -0.266 90  SER DDD N   
4166 C CA  . SER D 88  ? 1.816 1.236 1.506 0.211  0.318  -0.269 90  SER DDD CA  
4167 C C   . SER D 88  ? 1.699 1.224 1.473 0.224  0.293  -0.240 90  SER DDD C   
4168 O O   . SER D 88  ? 1.649 1.232 1.439 0.218  0.295  -0.242 90  SER DDD O   
4169 C CB  . SER D 88  ? 1.889 1.267 1.583 0.250  0.366  -0.281 90  SER DDD CB  
4170 O OG  . SER D 88  ? 1.865 1.299 1.587 0.261  0.386  -0.285 90  SER DDD OG  
4171 N N   . GLY D 89  ? 1.660 1.204 1.479 0.242  0.272  -0.217 91  GLY DDD N   
4172 C CA  . GLY D 89  ? 1.558 1.196 1.455 0.257  0.248  -0.191 91  GLY DDD CA  
4173 C C   . GLY D 89  ? 1.473 1.160 1.367 0.220  0.209  -0.181 91  GLY DDD C   
4174 O O   . GLY D 89  ? 1.386 1.148 1.339 0.228  0.189  -0.161 91  GLY DDD O   
4175 N N   . ASP D 90  ? 1.488 1.135 1.317 0.180  0.199  -0.194 92  ASP DDD N   
4176 C CA  . ASP D 90  ? 1.412 1.103 1.233 0.144  0.164  -0.187 92  ASP DDD CA  
4177 C C   . ASP D 90  ? 1.373 1.108 1.189 0.133  0.171  -0.195 92  ASP DDD C   
4178 O O   . ASP D 90  ? 1.305 1.090 1.129 0.114  0.145  -0.184 92  ASP DDD O   
4179 C CB  . ASP D 90  ? 1.450 1.086 1.210 0.108  0.149  -0.198 92  ASP DDD CB  
4180 C CG  . ASP D 90  ? 1.461 1.060 1.227 0.110  0.139  -0.186 92  ASP DDD CG  
4181 O OD1 . ASP D 90  ? 1.404 1.043 1.221 0.131  0.126  -0.161 92  ASP DDD OD1 
4182 O OD2 . ASP D 90  ? 1.526 1.052 1.241 0.090  0.145  -0.202 92  ASP DDD OD2 
4183 N N   . THR D 91  ? 1.417 1.127 1.214 0.146  0.206  -0.212 93  THR DDD N   
4184 C CA  . THR D 91  ? 1.396 1.134 1.178 0.138  0.221  -0.220 93  THR DDD CA  
4185 C C   . THR D 91  ? 1.297 1.121 1.147 0.144  0.210  -0.200 93  THR DDD C   
4186 O O   . THR D 91  ? 1.259 1.119 1.177 0.172  0.219  -0.191 93  THR DDD O   
4187 C CB  . THR D 91  ? 1.466 1.162 1.225 0.156  0.267  -0.241 93  THR DDD CB  
4188 O OG1 . THR D 91  ? 1.549 1.164 1.228 0.139  0.272  -0.262 93  THR DDD OG1 
4189 C CG2 . THR D 91  ? 1.458 1.185 1.213 0.154  0.290  -0.246 93  THR DDD CG2 
4190 N N   . ALA D 92  ? 1.255 1.109 1.087 0.119  0.191  -0.194 94  ALA DDD N   
4191 C CA  . ALA D 92  ? 1.180 1.108 1.067 0.118  0.178  -0.177 94  ALA DDD CA  
4192 C C   . ALA D 92  ? 1.155 1.093 0.997 0.091  0.161  -0.173 94  ALA DDD C   
4193 O O   . ALA D 92  ? 1.202 1.096 0.978 0.073  0.151  -0.183 94  ALA DDD O   
4194 C CB  . ALA D 92  ? 1.128 1.089 1.070 0.127  0.150  -0.158 94  ALA DDD CB  
4195 N N   . VAL D 93  ? 1.092 1.084 0.969 0.088  0.158  -0.160 95  VAL DDD N   
4196 C CA  . VAL D 93  ? 1.067 1.074 0.913 0.067  0.139  -0.151 95  VAL DDD CA  
4197 C C   . VAL D 93  ? 1.019 1.050 0.890 0.058  0.100  -0.135 95  VAL DDD C   
4198 O O   . VAL D 93  ? 0.986 1.057 0.918 0.068  0.093  -0.124 95  VAL DDD O   
4199 C CB  . VAL D 93  ? 1.038 1.083 0.909 0.067  0.159  -0.144 95  VAL DDD CB  
4200 C CG1 . VAL D 93  ? 1.025 1.080 0.863 0.050  0.141  -0.132 95  VAL DDD CG1 
4201 C CG2 . VAL D 93  ? 1.081 1.103 0.933 0.076  0.203  -0.159 95  VAL DDD CG2 
4202 N N   . TYR D 94  ? 1.031 1.041 0.855 0.041  0.076  -0.136 96  TYR DDD N   
4203 C CA  . TYR D 94  ? 0.976 1.005 0.818 0.030  0.042  -0.123 96  TYR DDD CA  
4204 C C   . TYR D 94  ? 0.921 0.988 0.761 0.019  0.026  -0.108 96  TYR DDD C   
4205 O O   . TYR D 94  ? 0.946 1.003 0.736 0.010  0.025  -0.112 96  TYR DDD O   
4206 C CB  . TYR D 94  ? 1.019 1.006 0.818 0.015  0.027  -0.134 96  TYR DDD CB  
4207 C CG  . TYR D 94  ? 1.055 1.001 0.863 0.026  0.039  -0.143 96  TYR DDD CG  
4208 C CD1 . TYR D 94  ? 1.112 1.021 0.903 0.040  0.069  -0.159 96  TYR DDD CD1 
4209 C CD2 . TYR D 94  ? 1.047 0.986 0.877 0.024  0.023  -0.134 96  TYR DDD CD2 
4210 C CE1 . TYR D 94  ? 1.153 1.020 0.949 0.054  0.083  -0.166 96  TYR DDD CE1 
4211 C CE2 . TYR D 94  ? 1.089 0.983 0.922 0.037  0.036  -0.140 96  TYR DDD CE2 
4212 C CZ  . TYR D 94  ? 1.140 0.997 0.957 0.053  0.066  -0.156 96  TYR DDD CZ  
4213 O OH  . TYR D 94  ? 1.195 1.002 1.012 0.069  0.081  -0.162 96  TYR DDD OH  
4214 N N   . TYR D 95  ? 0.862 0.969 0.752 0.022  0.015  -0.093 97  TYR DDD N   
4215 C CA  . TYR D 95  ? 0.821 0.962 0.716 0.013  0.001  -0.078 97  TYR DDD CA  
4216 C C   . TYR D 95  ? 0.794 0.946 0.696 0.003  -0.029 -0.068 97  TYR DDD C   
4217 O O   . TYR D 95  ? 0.768 0.921 0.701 0.007  -0.036 -0.065 97  TYR DDD O   
4218 C CB  . TYR D 95  ? 0.779 0.957 0.724 0.021  0.013  -0.070 97  TYR DDD CB  
4219 C CG  . TYR D 95  ? 0.809 0.985 0.762 0.030  0.046  -0.080 97  TYR DDD CG  
4220 C CD1 . TYR D 95  ? 0.819 0.992 0.803 0.045  0.060  -0.090 97  TYR DDD CD1 
4221 C CD2 . TYR D 95  ? 0.819 0.994 0.750 0.026  0.066  -0.080 97  TYR DDD CD2 
4222 C CE1 . TYR D 95  ? 0.844 1.019 0.842 0.053  0.094  -0.101 97  TYR DDD CE1 
4223 C CE2 . TYR D 95  ? 0.842 1.013 0.781 0.032  0.101  -0.090 97  TYR DDD CE2 
4224 C CZ  . TYR D 95  ? 0.857 1.032 0.833 0.045  0.115  -0.101 97  TYR DDD CZ  
4225 O OH  . TYR D 95  ? 0.900 1.077 0.891 0.051  0.152  -0.112 97  TYR DDD OH  
4226 N N   . CYS D 96  ? 0.797 0.958 0.672 -0.009 -0.045 -0.063 98  CYS DDD N   
4227 C CA  . CYS D 96  ? 0.787 0.969 0.677 -0.019 -0.070 -0.051 98  CYS DDD CA  
4228 C C   . CYS D 96  ? 0.712 0.929 0.633 -0.014 -0.068 -0.035 98  CYS DDD C   
4229 O O   . CYS D 96  ? 0.696 0.917 0.610 -0.008 -0.052 -0.034 98  CYS DDD O   
4230 C CB  . CYS D 96  ? 0.826 1.008 0.678 -0.032 -0.088 -0.054 98  CYS DDD CB  
4231 S SG  . CYS D 96  ? 0.844 1.063 0.691 -0.030 -0.097 -0.036 98  CYS DDD SG  
4232 N N   . ALA D 97  ? 0.665 0.900 0.616 -0.017 -0.082 -0.024 99  ALA DDD N   
4233 C CA  . ALA D 97  ? 0.623 0.888 0.603 -0.014 -0.082 -0.012 99  ALA DDD CA  
4234 C C   . ALA D 97  ? 0.585 0.866 0.571 -0.023 -0.100 0.000  99  ALA DDD C   
4235 O O   . ALA D 97  ? 0.589 0.860 0.574 -0.030 -0.113 -0.001 99  ALA DDD O   
4236 C CB  . ALA D 97  ? 0.615 0.887 0.632 -0.005 -0.075 -0.013 99  ALA DDD CB  
4237 N N   . ALA D 98  ? 0.556 0.857 0.546 -0.022 -0.099 0.011  100 ALA DDD N   
4238 C CA  . ALA D 98  ? 0.528 0.847 0.525 -0.028 -0.112 0.023  100 ALA DDD CA  
4239 C C   . ALA D 98  ? 0.505 0.837 0.527 -0.026 -0.109 0.030  100 ALA DDD C   
4240 O O   . ALA D 98  ? 0.491 0.827 0.518 -0.023 -0.095 0.029  100 ALA DDD O   
4241 C CB  . ALA D 98  ? 0.522 0.849 0.495 -0.026 -0.112 0.029  100 ALA DDD CB  
4242 N N   . SER D 99  ? 0.515 0.851 0.551 -0.031 -0.121 0.037  101 SER DDD N   
4243 C CA  . SER D 99  ? 0.481 0.830 0.533 -0.031 -0.122 0.045  101 SER DDD CA  
4244 C C   . SER D 99  ? 0.464 0.823 0.509 -0.036 -0.125 0.055  101 SER DDD C   
4245 O O   . SER D 99  ? 0.466 0.824 0.512 -0.043 -0.135 0.059  101 SER DDD O   
4246 C CB  . SER D 99  ? 0.487 0.830 0.552 -0.029 -0.130 0.046  101 SER DDD CB  
4247 O OG  . SER D 99  ? 0.482 0.838 0.557 -0.027 -0.132 0.052  101 SER DDD OG  
4248 N N   . VAL D 100 ? 0.460 0.827 0.499 -0.033 -0.116 0.059  102 VAL DDD N   
4249 C CA  . VAL D 100 ? 0.458 0.837 0.491 -0.033 -0.116 0.070  102 VAL DDD CA  
4250 C C   . VAL D 100 ? 0.429 0.814 0.473 -0.037 -0.117 0.078  102 VAL DDD C   
4251 O O   . VAL D 100 ? 0.464 0.844 0.512 -0.038 -0.114 0.075  102 VAL DDD O   
4252 C CB  . VAL D 100 ? 0.472 0.847 0.488 -0.024 -0.102 0.072  102 VAL DDD CB  
4253 C CG1 . VAL D 100 ? 0.501 0.867 0.500 -0.020 -0.100 0.066  102 VAL DDD CG1 
4254 C CG2 . VAL D 100 ? 0.463 0.831 0.483 -0.025 -0.087 0.071  102 VAL DDD CG2 
4255 N N   . GLY D 101 ? 0.419 0.816 0.466 -0.040 -0.121 0.086  103 GLY DDD N   
4256 C CA  . GLY D 101 ? 0.434 0.836 0.488 -0.044 -0.119 0.094  103 GLY DDD CA  
4257 C C   . GLY D 101 ? 0.453 0.840 0.508 -0.050 -0.125 0.092  103 GLY DDD C   
4258 O O   . GLY D 101 ? 0.459 0.842 0.510 -0.051 -0.121 0.097  103 GLY DDD O   
4259 N N   . ASN D 102 ? 0.472 0.849 0.528 -0.053 -0.133 0.086  104 ASN DDD N   
4260 C CA  . ASN D 102 ? 0.485 0.843 0.540 -0.053 -0.139 0.086  104 ASN DDD CA  
4261 C C   . ASN D 102 ? 0.503 0.849 0.558 -0.063 -0.142 0.090  104 ASN DDD C   
4262 O O   . ASN D 102 ? 0.502 0.844 0.559 -0.068 -0.145 0.083  104 ASN DDD O   
4263 C CB  . ASN D 102 ? 0.490 0.842 0.548 -0.044 -0.141 0.077  104 ASN DDD CB  
4264 C CG  . ASN D 102 ? 0.518 0.855 0.576 -0.038 -0.148 0.079  104 ASN DDD CG  
4265 O OD1 . ASN D 102 ? 0.531 0.859 0.581 -0.040 -0.151 0.088  104 ASN DDD OD1 
4266 N ND2 . ASN D 102 ? 0.530 0.865 0.596 -0.028 -0.150 0.071  104 ASN DDD ND2 
4267 N N   . TYR D 103 ? 0.514 0.850 0.563 -0.066 -0.140 0.100  105 TYR DDD N   
4268 C CA  . TYR D 103 ? 0.546 0.865 0.592 -0.079 -0.138 0.105  105 TYR DDD CA  
4269 C C   . TYR D 103 ? 0.566 0.847 0.597 -0.074 -0.141 0.108  105 TYR DDD C   
4270 O O   . TYR D 103 ? 0.571 0.827 0.593 -0.084 -0.135 0.115  105 TYR DDD O   
4271 C CB  . TYR D 103 ? 0.552 0.881 0.598 -0.086 -0.128 0.116  105 TYR DDD CB  
4272 C CG  . TYR D 103 ? 0.529 0.894 0.592 -0.087 -0.124 0.115  105 TYR DDD CG  
4273 C CD1 . TYR D 103 ? 0.539 0.926 0.621 -0.099 -0.123 0.112  105 TYR DDD CD1 
4274 C CD2 . TYR D 103 ? 0.507 0.884 0.565 -0.075 -0.121 0.115  105 TYR DDD CD2 
4275 C CE1 . TYR D 103 ? 0.517 0.941 0.615 -0.094 -0.121 0.113  105 TYR DDD CE1 
4276 C CE2 . TYR D 103 ? 0.494 0.897 0.563 -0.072 -0.115 0.117  105 TYR DDD CE2 
4277 C CZ  . TYR D 103 ? 0.499 0.928 0.589 -0.078 -0.116 0.117  105 TYR DDD CZ  
4278 O OH  . TYR D 103 ? 0.472 0.930 0.573 -0.070 -0.112 0.120  105 TYR DDD OH  
4279 N N   . GLY D 104 ? 0.570 0.847 0.600 -0.059 -0.147 0.102  106 GLY DDD N   
4280 C CA  . GLY D 104 ? 0.597 0.843 0.616 -0.047 -0.151 0.106  106 GLY DDD CA  
4281 C C   . GLY D 104 ? 0.609 0.838 0.632 -0.045 -0.151 0.094  106 GLY DDD C   
4282 O O   . GLY D 104 ? 0.602 0.838 0.631 -0.059 -0.148 0.085  106 GLY DDD O   
4283 N N   . LEU D 105 ? 0.618 0.826 0.637 -0.027 -0.154 0.095  107 LEU DDD N   
4284 C CA  . LEU D 105 ? 0.623 0.808 0.643 -0.021 -0.150 0.084  107 LEU DDD CA  
4285 C C   . LEU D 105 ? 0.603 0.807 0.639 0.001  -0.154 0.078  107 LEU DDD C   
4286 O O   . LEU D 105 ? 0.628 0.815 0.663 0.022  -0.157 0.084  107 LEU DDD O   
4287 C CB  . LEU D 105 ? 0.672 0.802 0.671 -0.020 -0.144 0.092  107 LEU DDD CB  
4288 C CG  . LEU D 105 ? 0.713 0.805 0.704 -0.019 -0.136 0.079  107 LEU DDD CG  
4289 C CD1 . LEU D 105 ? 0.706 0.810 0.701 -0.044 -0.133 0.062  107 LEU DDD CD1 
4290 C CD2 . LEU D 105 ? 0.775 0.804 0.741 -0.019 -0.127 0.089  107 LEU DDD CD2 
4291 N N   . PRO D 106 ? 0.567 0.807 0.619 -0.002 -0.153 0.068  108 PRO DDD N   
4292 C CA  . PRO D 106 ? 0.565 0.830 0.639 0.015  -0.154 0.061  108 PRO DDD CA  
4293 C C   . PRO D 106 ? 0.604 0.849 0.682 0.027  -0.146 0.051  108 PRO DDD C   
4294 O O   . PRO D 106 ? 0.632 0.850 0.694 0.017  -0.139 0.044  108 PRO DDD O   
4295 C CB  . PRO D 106 ? 0.530 0.829 0.613 0.003  -0.149 0.053  108 PRO DDD CB  
4296 C CG  . PRO D 106 ? 0.527 0.812 0.593 -0.014 -0.146 0.052  108 PRO DDD CG  
4297 C CD  . PRO D 106 ? 0.545 0.805 0.597 -0.020 -0.150 0.063  108 PRO DDD CD  
4298 N N   . TRP D 107 ? 0.632 0.891 0.731 0.050  -0.148 0.050  109 TRP DDD N   
4299 C CA  . TRP D 107 ? 0.666 0.908 0.774 0.066  -0.137 0.040  109 TRP DDD CA  
4300 C C   . TRP D 107 ? 0.646 0.935 0.792 0.081  -0.134 0.031  109 TRP DDD C   
4301 O O   . TRP D 107 ? 0.706 0.988 0.864 0.094  -0.122 0.021  109 TRP DDD O   
4302 C CB  . TRP D 107 ? 0.726 0.925 0.820 0.085  -0.138 0.050  109 TRP DDD CB  
4303 C CG  . TRP D 107 ? 0.756 0.968 0.855 0.104  -0.154 0.066  109 TRP DDD CG  
4304 C CD1 . TRP D 107 ? 0.773 0.967 0.847 0.097  -0.163 0.082  109 TRP DDD CD1 
4305 C CD2 . TRP D 107 ? 0.767 1.014 0.896 0.133  -0.163 0.068  109 TRP DDD CD2 
4306 N NE1 . TRP D 107 ? 0.788 1.000 0.868 0.121  -0.178 0.095  109 TRP DDD NE1 
4307 C CE2 . TRP D 107 ? 0.785 1.033 0.901 0.144  -0.181 0.086  109 TRP DDD CE2 
4308 C CE3 . TRP D 107 ? 0.755 1.037 0.924 0.151  -0.158 0.056  109 TRP DDD CE3 
4309 C CZ2 . TRP D 107 ? 0.797 1.083 0.937 0.173  -0.197 0.092  109 TRP DDD CZ2 
4310 C CZ3 . TRP D 107 ? 0.766 1.089 0.965 0.179  -0.172 0.061  109 TRP DDD CZ3 
4311 C CH2 . TRP D 107 ? 0.786 1.113 0.971 0.190  -0.194 0.079  109 TRP DDD CH2 
4312 N N   . ALA D 108 ? 0.595 0.930 0.761 0.076  -0.144 0.032  110 ALA DDD N   
4313 C CA  . ALA D 108 ? 0.571 0.957 0.779 0.082  -0.140 0.021  110 ALA DDD CA  
4314 C C   . ALA D 108 ? 0.541 0.937 0.746 0.061  -0.124 0.010  110 ALA DDD C   
4315 O O   . ALA D 108 ? 0.527 0.911 0.707 0.042  -0.126 0.015  110 ALA DDD O   
4316 C CB  . ALA D 108 ? 0.560 0.986 0.787 0.088  -0.159 0.027  110 ALA DDD CB  
4317 N N   . HIS D 109 ? 0.543 0.959 0.775 0.064  -0.107 -0.004 111 HIS DDD N   
4318 C CA  . HIS D 109 ? 0.538 0.953 0.761 0.047  -0.087 -0.014 111 HIS DDD CA  
4319 C C   . HIS D 109 ? 0.501 0.937 0.723 0.028  -0.090 -0.012 111 HIS DDD C   
4320 O O   . HIS D 109 ? 0.494 0.910 0.686 0.014  -0.081 -0.010 111 HIS DDD O   
4321 C CB  . HIS D 109 ? 0.549 0.983 0.804 0.055  -0.065 -0.029 111 HIS DDD CB  
4322 C CG  . HIS D 109 ? 0.544 1.035 0.851 0.056  -0.066 -0.037 111 HIS DDD CG  
4323 N ND1 . HIS D 109 ? 0.581 1.105 0.928 0.078  -0.080 -0.037 111 HIS DDD ND1 
4324 C CD2 . HIS D 109 ? 0.540 1.062 0.867 0.038  -0.055 -0.046 111 HIS DDD CD2 
4325 C CE1 . HIS D 109 ? 0.557 1.138 0.950 0.072  -0.080 -0.047 111 HIS DDD CE1 
4326 N NE2 . HIS D 109 ? 0.557 1.135 0.939 0.046  -0.063 -0.054 111 HIS DDD NE2 
4327 N N   . PHE D 110 ? 0.474 0.948 0.724 0.029  -0.103 -0.012 112 PHE DDD N   
4328 C CA  . PHE D 110 ? 0.452 0.945 0.702 0.010  -0.104 -0.013 112 PHE DDD CA  
4329 C C   . PHE D 110 ? 0.447 0.912 0.657 0.002  -0.115 0.001  112 PHE DDD C   
4330 O O   . PHE D 110 ? 0.427 0.894 0.627 -0.013 -0.110 0.001  112 PHE DDD O   
4331 C CB  . PHE D 110 ? 0.431 0.974 0.720 0.012  -0.118 -0.020 112 PHE DDD CB  
4332 C CG  . PHE D 110 ? 0.442 0.993 0.736 0.033  -0.144 -0.010 112 PHE DDD CG  
4333 C CD1 . PHE D 110 ? 0.453 0.982 0.713 0.034  -0.162 0.005  112 PHE DDD CD1 
4334 C CD2 . PHE D 110 ? 0.451 1.033 0.785 0.055  -0.149 -0.015 112 PHE DDD CD2 
4335 C CE1 . PHE D 110 ? 0.465 0.993 0.722 0.055  -0.183 0.016  112 PHE DDD CE1 
4336 C CE2 . PHE D 110 ? 0.472 1.056 0.805 0.079  -0.173 -0.003 112 PHE DDD CE2 
4337 C CZ  . PHE D 110 ? 0.486 1.040 0.777 0.078  -0.189 0.013  112 PHE DDD CZ  
4338 N N   . GLU D 111 ? 0.468 0.905 0.656 0.011  -0.126 0.012  113 GLU DDD N   
4339 C CA  . GLU D 111 ? 0.473 0.886 0.629 0.003  -0.134 0.026  113 GLU DDD CA  
4340 C C   . GLU D 111 ? 0.474 0.865 0.605 -0.007 -0.121 0.026  113 GLU DDD C   
4341 O O   . GLU D 111 ? 0.505 0.886 0.616 -0.014 -0.125 0.035  113 GLU DDD O   
4342 C CB  . GLU D 111 ? 0.507 0.899 0.651 0.014  -0.148 0.037  113 GLU DDD CB  
4343 C CG  . GLU D 111 ? 0.540 0.952 0.699 0.028  -0.164 0.041  113 GLU DDD CG  
4344 C CD  . GLU D 111 ? 0.595 0.977 0.738 0.043  -0.175 0.054  113 GLU DDD CD  
4345 O OE1 . GLU D 111 ? 0.625 0.975 0.759 0.048  -0.168 0.054  113 GLU DDD OE1 
4346 O OE2 . GLU D 111 ? 0.651 1.037 0.784 0.048  -0.190 0.064  113 GLU DDD OE2 
4347 N N   . TYR D 112 ? 0.470 0.856 0.603 -0.005 -0.107 0.016  114 TYR DDD N   
4348 C CA  . TYR D 112 ? 0.483 0.849 0.588 -0.011 -0.096 0.016  114 TYR DDD CA  
4349 C C   . TYR D 112 ? 0.457 0.831 0.560 -0.018 -0.079 0.013  114 TYR DDD C   
4350 O O   . TYR D 112 ? 0.473 0.866 0.601 -0.019 -0.070 0.005  114 TYR DDD O   
4351 C CB  . TYR D 112 ? 0.527 0.873 0.624 -0.004 -0.091 0.008  114 TYR DDD CB  
4352 C CG  . TYR D 112 ? 0.543 0.868 0.631 -0.001 -0.104 0.012  114 TYR DDD CG  
4353 C CD1 . TYR D 112 ? 0.547 0.872 0.654 0.010  -0.112 0.014  114 TYR DDD CD1 
4354 C CD2 . TYR D 112 ? 0.568 0.872 0.628 -0.010 -0.109 0.013  114 TYR DDD CD2 
4355 C CE1 . TYR D 112 ? 0.568 0.863 0.661 0.012  -0.120 0.019  114 TYR DDD CE1 
4356 C CE2 . TYR D 112 ? 0.590 0.871 0.642 -0.012 -0.117 0.015  114 TYR DDD CE2 
4357 C CZ  . TYR D 112 ? 0.591 0.863 0.658 -0.001 -0.121 0.018  114 TYR DDD CZ  
4358 O OH  . TYR D 112 ? 0.624 0.863 0.677 -0.003 -0.125 0.020  114 TYR DDD OH  
4359 N N   . ASP D 113 ? 0.453 0.813 0.527 -0.021 -0.074 0.019  115 ASP DDD N   
4360 C CA  . ASP D 113 ? 0.447 0.803 0.508 -0.026 -0.057 0.020  115 ASP DDD CA  
4361 C C   . ASP D 113 ? 0.458 0.794 0.492 -0.023 -0.039 0.017  115 ASP DDD C   
4362 O O   . ASP D 113 ? 0.462 0.792 0.493 -0.026 -0.017 0.014  115 ASP DDD O   
4363 C CB  . ASP D 113 ? 0.440 0.795 0.485 -0.028 -0.064 0.034  115 ASP DDD CB  
4364 C CG  . ASP D 113 ? 0.420 0.789 0.483 -0.032 -0.079 0.037  115 ASP DDD CG  
4365 O OD1 . ASP D 113 ? 0.440 0.822 0.522 -0.036 -0.076 0.031  115 ASP DDD OD1 
4366 O OD2 . ASP D 113 ? 0.420 0.789 0.478 -0.031 -0.094 0.045  115 ASP DDD OD2 
4367 N N   . PHE D 114 ? 0.471 0.794 0.481 -0.018 -0.048 0.019  116 PHE DDD N   
4368 C CA  . PHE D 114 ? 0.502 0.803 0.476 -0.013 -0.035 0.017  116 PHE DDD CA  
4369 C C   . PHE D 114 ? 0.521 0.811 0.489 -0.010 -0.037 0.005  116 PHE DDD C   
4370 O O   . PHE D 114 ? 0.508 0.804 0.490 -0.012 -0.056 0.004  116 PHE DDD O   
4371 C CB  . PHE D 114 ? 0.507 0.804 0.447 -0.009 -0.044 0.029  116 PHE DDD CB  
4372 C CG  . PHE D 114 ? 0.493 0.794 0.437 -0.008 -0.037 0.041  116 PHE DDD CG  
4373 C CD1 . PHE D 114 ? 0.508 0.790 0.435 -0.007 -0.011 0.042  116 PHE DDD CD1 
4374 C CD2 . PHE D 114 ? 0.468 0.788 0.431 -0.011 -0.053 0.048  116 PHE DDD CD2 
4375 C CE1 . PHE D 114 ? 0.509 0.787 0.436 -0.007 -0.001 0.051  116 PHE DDD CE1 
4376 C CE2 . PHE D 114 ? 0.464 0.783 0.427 -0.011 -0.043 0.057  116 PHE DDD CE2 
4377 C CZ  . PHE D 114 ? 0.486 0.783 0.431 -0.009 -0.018 0.058  116 PHE DDD CZ  
4378 N N   . TRP D 115 ? 0.564 0.835 0.511 -0.007 -0.016 -0.003 117 TRP DDD N   
4379 C CA  . TRP D 115 ? 0.602 0.858 0.542 -0.003 -0.011 -0.016 117 TRP DDD CA  
4380 C C   . TRP D 115 ? 0.665 0.892 0.546 0.000  -0.002 -0.018 117 TRP DDD C   
4381 O O   . TRP D 115 ? 0.685 0.901 0.540 0.003  0.013  -0.011 117 TRP DDD O   
4382 C CB  . TRP D 115 ? 0.593 0.857 0.569 -0.001 0.012  -0.026 117 TRP DDD CB  
4383 C CG  . TRP D 115 ? 0.563 0.858 0.592 -0.002 0.000  -0.026 117 TRP DDD CG  
4384 C CD1 . TRP D 115 ? 0.527 0.847 0.582 -0.008 -0.002 -0.020 117 TRP DDD CD1 
4385 C CD2 . TRP D 115 ? 0.562 0.866 0.621 0.005  -0.012 -0.030 117 TRP DDD CD2 
4386 N NE1 . TRP D 115 ? 0.512 0.857 0.608 -0.006 -0.017 -0.021 117 TRP DDD NE1 
4387 C CE2 . TRP D 115 ? 0.523 0.859 0.623 0.004  -0.023 -0.026 117 TRP DDD CE2 
4388 C CE3 . TRP D 115 ? 0.593 0.875 0.642 0.013  -0.014 -0.038 117 TRP DDD CE3 
4389 C CZ2 . TRP D 115 ? 0.520 0.869 0.651 0.014  -0.037 -0.026 117 TRP DDD CZ2 
4390 C CZ3 . TRP D 115 ? 0.589 0.880 0.671 0.023  -0.024 -0.038 117 TRP DDD CZ3 
4391 C CH2 . TRP D 115 ? 0.548 0.872 0.669 0.025  -0.037 -0.031 117 TRP DDD CH2 
4392 N N   . GLY D 116 ? 0.721 0.931 0.580 0.000  -0.012 -0.028 118 GLY DDD N   
4393 C CA  . GLY D 116 ? 0.797 0.977 0.597 0.004  -0.003 -0.034 118 GLY DDD CA  
4394 C C   . GLY D 116 ? 0.850 1.010 0.646 0.009  0.032  -0.044 118 GLY DDD C   
4395 O O   . GLY D 116 ? 0.817 0.994 0.665 0.009  0.045  -0.048 118 GLY DDD O   
4396 N N   . GLN D 117 ? 0.950 1.078 0.687 0.012  0.048  -0.049 119 GLN DDD N   
4397 C CA  . GLN D 117 ? 1.008 1.112 0.732 0.017  0.086  -0.059 119 GLN DDD CA  
4398 C C   . GLN D 117 ? 0.990 1.087 0.739 0.018  0.092  -0.077 119 GLN DDD C   
4399 O O   . GLN D 117 ? 1.006 1.102 0.780 0.023  0.123  -0.085 119 GLN DDD O   
4400 C CB  . GLN D 117 ? 1.119 1.184 0.761 0.022  0.097  -0.059 119 GLN DDD CB  
4401 C CG  . GLN D 117 ? 1.172 1.233 0.779 0.026  0.097  -0.039 119 GLN DDD CG  
4402 C CD  . GLN D 117 ? 1.211 1.267 0.838 0.025  0.135  -0.033 119 GLN DDD CD  
4403 O OE1 . GLN D 117 ? 1.286 1.315 0.893 0.026  0.172  -0.041 119 GLN DDD OE1 
4404 N NE2 . GLN D 117 ? 1.179 1.260 0.846 0.022  0.129  -0.021 119 GLN DDD NE2 
4405 N N   . GLY D 118 ? 0.961 1.054 0.703 0.015  0.064  -0.083 120 GLY DDD N   
4406 C CA  . GLY D 118 ? 0.971 1.048 0.727 0.018  0.068  -0.098 120 GLY DDD CA  
4407 C C   . GLY D 118 ? 1.037 1.068 0.727 0.018  0.080  -0.115 120 GLY DDD C   
4408 O O   . GLY D 118 ? 1.072 1.085 0.718 0.021  0.102  -0.115 120 GLY DDD O   
4409 N N   . ILE D 119 ? 1.058 1.066 0.735 0.014  0.067  -0.128 121 ILE DDD N   
4410 C CA  . ILE D 119 ? 1.137 1.097 0.745 0.010  0.075  -0.148 121 ILE DDD CA  
4411 C C   . ILE D 119 ? 1.153 1.083 0.780 0.019  0.098  -0.164 121 ILE DDD C   
4412 O O   . ILE D 119 ? 1.106 1.048 0.786 0.022  0.089  -0.161 121 ILE DDD O   
4413 C CB  . ILE D 119 ? 1.159 1.115 0.727 -0.007 0.037  -0.153 121 ILE DDD CB  
4414 C CG1 . ILE D 119 ? 1.112 1.093 0.733 -0.016 0.011  -0.146 121 ILE DDD CG1 
4415 C CG2 . ILE D 119 ? 1.167 1.140 0.692 -0.009 0.022  -0.141 121 ILE DDD CG2 
4416 C CD1 . ILE D 119 ? 1.151 1.124 0.740 -0.036 -0.019 -0.157 121 ILE DDD CD1 
4417 N N   . GLN D 120 ? 1.219 1.109 0.800 0.025  0.129  -0.180 122 GLN DDD N   
4418 C CA  . GLN D 120 ? 1.267 1.122 0.858 0.037  0.159  -0.197 122 GLN DDD CA  
4419 C C   . GLN D 120 ? 1.311 1.123 0.866 0.026  0.142  -0.214 122 GLN DDD C   
4420 O O   . GLN D 120 ? 1.363 1.152 0.850 0.009  0.127  -0.225 122 GLN DDD O   
4421 C CB  . GLN D 120 ? 1.338 1.163 0.885 0.045  0.201  -0.209 122 GLN DDD CB  
4422 C CG  . GLN D 120 ? 1.380 1.173 0.942 0.062  0.238  -0.226 122 GLN DDD CG  
4423 C CD  . GLN D 120 ? 1.320 1.158 0.979 0.080  0.249  -0.216 122 GLN DDD CD  
4424 O OE1 . GLN D 120 ? 1.315 1.146 1.011 0.091  0.247  -0.220 122 GLN DDD OE1 
4425 N NE2 . GLN D 120 ? 1.279 1.163 0.980 0.083  0.262  -0.203 122 GLN DDD NE2 
4426 N N   . VAL D 121 ? 1.294 1.099 0.896 0.034  0.144  -0.216 123 VAL DDD N   
4427 C CA  . VAL D 121 ? 1.350 1.099 0.921 0.027  0.142  -0.234 123 VAL DDD CA  
4428 C C   . VAL D 121 ? 1.393 1.105 0.977 0.052  0.183  -0.246 123 VAL DDD C   
4429 O O   . VAL D 121 ? 1.347 1.089 1.002 0.074  0.192  -0.233 123 VAL DDD O   
4430 C CB  . VAL D 121 ? 1.307 1.069 0.917 0.018  0.111  -0.223 123 VAL DDD CB  
4431 C CG1 . VAL D 121 ? 1.377 1.074 0.956 0.009  0.115  -0.243 123 VAL DDD CG1 
4432 C CG2 . VAL D 121 ? 1.256 1.060 0.861 -0.004 0.073  -0.211 123 VAL DDD CG2 
4433 N N   . THR D 122 ? 1.479 1.131 0.996 0.049  0.207  -0.271 124 THR DDD N   
4434 C CA  . THR D 122 ? 1.543 1.149 1.060 0.073  0.251  -0.286 124 THR DDD CA  
4435 C C   . THR D 122 ? 1.624 1.154 1.087 0.061  0.252  -0.309 124 THR DDD C   
4436 O O   . THR D 122 ? 1.688 1.183 1.073 0.035  0.242  -0.328 124 THR DDD O   
4437 C CB  . THR D 122 ? 1.585 1.183 1.067 0.081  0.288  -0.295 124 THR DDD CB  
4438 O OG1 . THR D 122 ? 1.608 1.204 1.019 0.057  0.269  -0.299 124 THR DDD OG1 
4439 C CG2 . THR D 122 ? 1.519 1.179 1.077 0.102  0.307  -0.277 124 THR DDD CG2 
4440 N N   . VAL D 123 ? 1.631 1.132 1.131 0.081  0.266  -0.308 125 VAL DDD N   
4441 C CA  . VAL D 123 ? 1.705 1.127 1.163 0.071  0.271  -0.328 125 VAL DDD CA  
4442 C C   . VAL D 123 ? 1.790 1.143 1.210 0.091  0.320  -0.352 125 VAL DDD C   
4443 O O   . VAL D 123 ? 1.783 1.138 1.251 0.128  0.351  -0.345 125 VAL DDD O   
4444 C CB  . VAL D 123 ? 1.670 1.096 1.188 0.084  0.257  -0.309 125 VAL DDD CB  
4445 C CG1 . VAL D 123 ? 1.762 1.098 1.237 0.075  0.268  -0.327 125 VAL DDD CG1 
4446 C CG2 . VAL D 123 ? 1.579 1.072 1.135 0.066  0.213  -0.286 125 VAL DDD CG2 
4447 N N   . ASN E 5   ? 0.893 1.889 0.953 -0.191 0.036  0.581  334 ASN EEE N   
4448 C CA  . ASN E 5   ? 0.857 1.862 0.925 -0.190 0.037  0.538  334 ASN EEE CA  
4449 C C   . ASN E 5   ? 0.819 1.761 0.896 -0.177 0.026  0.508  334 ASN EEE C   
4450 O O   . ASN E 5   ? 0.779 1.729 0.854 -0.168 0.023  0.470  334 ASN EEE O   
4451 C CB  . ASN E 5   ? 0.885 1.906 0.976 -0.213 0.047  0.545  334 ASN EEE CB  
4452 C CG  . ASN E 5   ? 0.880 1.945 0.972 -0.212 0.050  0.507  334 ASN EEE CG  
4453 O OD1 . ASN E 5   ? 0.896 1.996 0.970 -0.197 0.048  0.482  334 ASN EEE OD1 
4454 N ND2 . ASN E 5   ? 0.883 1.948 0.999 -0.229 0.056  0.503  334 ASN EEE ND2 
4455 N N   . LEU E 6   ? 0.822 1.704 0.910 -0.177 0.019  0.525  335 LEU EEE N   
4456 C CA  . LEU E 6   ? 0.800 1.621 0.896 -0.166 0.008  0.501  335 LEU EEE CA  
4457 C C   . LEU E 6   ? 0.765 1.589 0.837 -0.144 0.002  0.481  335 LEU EEE C   
4458 O O   . LEU E 6   ? 0.784 1.630 0.838 -0.138 0.002  0.500  335 LEU EEE O   
4459 C CB  . LEU E 6   ? 0.835 1.601 0.951 -0.172 0.004  0.529  335 LEU EEE CB  
4460 C CG  . LEU E 6   ? 0.833 1.539 0.969 -0.168 -0.005 0.506  335 LEU EEE CG  
4461 C CD1 . LEU E 6   ? 0.868 1.531 1.035 -0.182 -0.006 0.532  335 LEU EEE CD1 
4462 C CD2 . LEU E 6   ? 0.820 1.500 0.940 -0.147 -0.015 0.488  335 LEU EEE CD2 
4463 N N   . CYS E 7   ? 0.730 1.534 0.802 -0.133 -0.004 0.444  336 CYS EEE N   
4464 C CA  . CYS E 7   ? 0.704 1.506 0.757 -0.114 -0.010 0.422  336 CYS EEE CA  
4465 C C   . CYS E 7   ? 0.722 1.485 0.772 -0.106 -0.017 0.439  336 CYS EEE C   
4466 O O   . CYS E 7   ? 0.708 1.424 0.776 -0.111 -0.021 0.449  336 CYS EEE O   
4467 C CB  . CYS E 7   ? 0.660 1.439 0.717 -0.106 -0.015 0.384  336 CYS EEE CB  
4468 S SG  . CYS E 7   ? 0.635 1.461 0.694 -0.109 -0.009 0.358  336 CYS EEE SG  
4469 N N   . PRO E 8   ? 0.755 1.539 0.786 -0.093 -0.020 0.441  337 PRO EEE N   
4470 C CA  . PRO E 8   ? 0.783 1.536 0.810 -0.085 -0.027 0.459  337 PRO EEE CA  
4471 C C   . PRO E 8   ? 0.757 1.463 0.786 -0.073 -0.035 0.434  337 PRO EEE C   
4472 O O   . PRO E 8   ? 0.742 1.452 0.758 -0.059 -0.040 0.427  337 PRO EEE O   
4473 C CB  . PRO E 8   ? 0.780 1.586 0.784 -0.076 -0.025 0.467  337 PRO EEE CB  
4474 C CG  . PRO E 8   ? 0.750 1.594 0.746 -0.072 -0.021 0.433  337 PRO EEE CG  
4475 C CD  . PRO E 8   ? 0.738 1.578 0.750 -0.085 -0.016 0.425  337 PRO EEE CD  
4476 N N   . PHE E 9   ? 0.764 1.430 0.811 -0.078 -0.038 0.421  338 PHE EEE N   
4477 C CA  . PHE E 9   ? 0.763 1.385 0.816 -0.069 -0.046 0.399  338 PHE EEE CA  
4478 C C   . PHE E 9   ? 0.775 1.366 0.832 -0.063 -0.053 0.417  338 PHE EEE C   
4479 O O   . PHE E 9   ? 0.801 1.373 0.852 -0.051 -0.059 0.401  338 PHE EEE O   
4480 C CB  . PHE E 9   ? 0.779 1.371 0.850 -0.077 -0.046 0.384  338 PHE EEE CB  
4481 C CG  . PHE E 9   ? 0.780 1.396 0.848 -0.078 -0.042 0.360  338 PHE EEE CG  
4482 C CD1 . PHE E 9   ? 0.772 1.403 0.823 -0.066 -0.043 0.336  338 PHE EEE CD1 
4483 C CD2 . PHE E 9   ? 0.813 1.433 0.896 -0.091 -0.038 0.360  338 PHE EEE CD2 
4484 C CE1 . PHE E 9   ? 0.774 1.424 0.825 -0.067 -0.040 0.315  338 PHE EEE CE1 
4485 C CE2 . PHE E 9   ? 0.816 1.458 0.897 -0.091 -0.035 0.337  338 PHE EEE CE2 
4486 C CZ  . PHE E 9   ? 0.810 1.465 0.875 -0.078 -0.037 0.315  338 PHE EEE CZ  
4487 N N   . GLY E 10  ? 0.790 1.376 0.858 -0.072 -0.052 0.451  339 GLY EEE N   
4488 C CA  . GLY E 10  ? 0.809 1.368 0.884 -0.066 -0.059 0.473  339 GLY EEE CA  
4489 C C   . GLY E 10  ? 0.797 1.375 0.850 -0.049 -0.063 0.470  339 GLY EEE C   
4490 O O   . GLY E 10  ? 0.778 1.324 0.834 -0.039 -0.072 0.463  339 GLY EEE O   
4491 N N   . GLU E 11  ? 0.808 1.437 0.838 -0.047 -0.057 0.472  340 GLU EEE N   
4492 C CA  . GLU E 11  ? 0.824 1.480 0.833 -0.032 -0.060 0.466  340 GLU EEE CA  
4493 C C   . GLU E 11  ? 0.766 1.403 0.773 -0.021 -0.065 0.430  340 GLU EEE C   
4494 O O   . GLU E 11  ? 0.747 1.380 0.747 -0.008 -0.071 0.426  340 GLU EEE O   
4495 C CB  . GLU E 11  ? 0.850 1.570 0.840 -0.032 -0.052 0.467  340 GLU EEE CB  
4496 C CG  . GLU E 11  ? 0.924 1.673 0.911 -0.041 -0.048 0.507  340 GLU EEE CG  
4497 C CD  . GLU E 11  ? 0.959 1.778 0.930 -0.043 -0.039 0.506  340 GLU EEE CD  
4498 O OE1 . GLU E 11  ? 0.966 1.812 0.926 -0.034 -0.039 0.474  340 GLU EEE OE1 
4499 O OE2 . GLU E 11  ? 0.975 1.821 0.944 -0.054 -0.034 0.537  340 GLU EEE OE2 
4500 N N   . VAL E 12  ? 0.739 1.366 0.751 -0.026 -0.061 0.404  341 VAL EEE N   
4501 C CA  . VAL E 12  ? 0.701 1.311 0.710 -0.017 -0.064 0.370  341 VAL EEE CA  
4502 C C   . VAL E 12  ? 0.698 1.258 0.722 -0.015 -0.072 0.367  341 VAL EEE C   
4503 O O   . VAL E 12  ? 0.694 1.245 0.714 -0.004 -0.077 0.357  341 VAL EEE O   
4504 C CB  . VAL E 12  ? 0.683 1.302 0.693 -0.023 -0.059 0.347  341 VAL EEE CB  
4505 C CG1 . VAL E 12  ? 0.661 1.262 0.668 -0.015 -0.061 0.316  341 VAL EEE CG1 
4506 C CG2 . VAL E 12  ? 0.678 1.349 0.678 -0.025 -0.052 0.348  341 VAL EEE CG2 
4507 N N   . PHE E 13  ? 0.707 1.238 0.749 -0.025 -0.072 0.374  342 PHE EEE N   
4508 C CA  . PHE E 13  ? 0.721 1.208 0.782 -0.024 -0.079 0.365  342 PHE EEE CA  
4509 C C   . PHE E 13  ? 0.755 1.222 0.824 -0.017 -0.087 0.383  342 PHE EEE C   
4510 O O   . PHE E 13  ? 0.744 1.184 0.820 -0.009 -0.094 0.368  342 PHE EEE O   
4511 C CB  . PHE E 13  ? 0.719 1.187 0.800 -0.037 -0.077 0.365  342 PHE EEE CB  
4512 C CG  . PHE E 13  ? 0.689 1.166 0.765 -0.039 -0.073 0.339  342 PHE EEE CG  
4513 C CD1 . PHE E 13  ? 0.681 1.190 0.749 -0.046 -0.066 0.340  342 PHE EEE CD1 
4514 C CD2 . PHE E 13  ? 0.668 1.121 0.747 -0.035 -0.077 0.314  342 PHE EEE CD2 
4515 C CE1 . PHE E 13  ? 0.654 1.169 0.719 -0.046 -0.063 0.317  342 PHE EEE CE1 
4516 C CE2 . PHE E 13  ? 0.646 1.106 0.720 -0.036 -0.074 0.293  342 PHE EEE CE2 
4517 C CZ  . PHE E 13  ? 0.634 1.124 0.701 -0.041 -0.068 0.295  342 PHE EEE CZ  
4518 N N   . ASN E 14  ? 0.806 1.287 0.874 -0.020 -0.086 0.415  343 ASN EEE N   
4519 C CA  . ASN E 14  ? 0.846 1.306 0.927 -0.015 -0.094 0.440  343 ASN EEE CA  
4520 C C   . ASN E 14  ? 0.800 1.290 0.859 -0.002 -0.096 0.451  343 ASN EEE C   
4521 O O   . ASN E 14  ? 0.807 1.286 0.874 0.003  -0.103 0.477  343 ASN EEE O   
4522 C CB  . ASN E 14  ? 0.931 1.378 1.032 -0.028 -0.093 0.471  343 ASN EEE CB  
4523 C CG  . ASN E 14  ? 1.009 1.414 1.140 -0.037 -0.096 0.460  343 ASN EEE CG  
4524 O OD1 . ASN E 14  ? 0.979 1.357 1.122 -0.029 -0.103 0.438  343 ASN EEE OD1 
4525 N ND2 . ASN E 14  ? 1.173 1.577 1.320 -0.053 -0.090 0.474  343 ASN EEE ND2 
4526 N N   . ALA E 15  ? 0.741 1.267 0.778 0.004  -0.092 0.432  344 ALA EEE N   
4527 C CA  . ALA E 15  ? 0.728 1.285 0.746 0.018  -0.094 0.434  344 ALA EEE CA  
4528 C C   . ALA E 15  ? 0.744 1.270 0.771 0.030  -0.105 0.431  344 ALA EEE C   
4529 O O   . ALA E 15  ? 0.723 1.216 0.763 0.031  -0.109 0.409  344 ALA EEE O   
4530 C CB  . ALA E 15  ? 0.689 1.277 0.689 0.022  -0.089 0.403  344 ALA EEE CB  
4531 N N   . THR E 16  ? 0.788 1.329 0.808 0.041  -0.111 0.453  345 THR EEE N   
4532 C CA  . THR E 16  ? 0.812 1.326 0.843 0.054  -0.123 0.454  345 THR EEE CA  
4533 C C   . THR E 16  ? 0.785 1.305 0.808 0.064  -0.124 0.416  345 THR EEE C   
4534 O O   . THR E 16  ? 0.796 1.283 0.835 0.070  -0.131 0.402  345 THR EEE O   
4535 C CB  . THR E 16  ? 0.841 1.372 0.867 0.063  -0.128 0.490  345 THR EEE CB  
4536 O OG1 . THR E 16  ? 0.848 1.430 0.849 0.073  -0.126 0.483  345 THR EEE OG1 
4537 C CG2 . THR E 16  ? 0.864 1.398 0.895 0.050  -0.124 0.530  345 THR EEE CG2 
4538 N N   . ARG E 17  ? 0.759 1.321 0.762 0.066  -0.117 0.400  346 ARG EEE N   
4539 C CA  . ARG E 17  ? 0.731 1.301 0.727 0.073  -0.116 0.363  346 ARG EEE CA  
4540 C C   . ARG E 17  ? 0.654 1.235 0.643 0.062  -0.106 0.342  346 ARG EEE C   
4541 O O   . ARG E 17  ? 0.648 1.254 0.631 0.055  -0.099 0.355  346 ARG EEE O   
4542 C CB  . ARG E 17  ? 0.773 1.384 0.754 0.087  -0.119 0.360  346 ARG EEE CB  
4543 C CG  . ARG E 17  ? 0.806 1.413 0.788 0.096  -0.122 0.327  346 ARG EEE CG  
4544 C CD  . ARG E 17  ? 0.859 1.497 0.834 0.112  -0.128 0.327  346 ARG EEE CD  
4545 N NE  . ARG E 17  ? 0.896 1.585 0.856 0.115  -0.122 0.312  346 ARG EEE NE  
4546 C CZ  . ARG E 17  ? 0.936 1.666 0.882 0.115  -0.119 0.330  346 ARG EEE CZ  
4547 N NH1 . ARG E 17  ? 0.973 1.699 0.918 0.111  -0.120 0.366  346 ARG EEE NH1 
4548 N NH2 . ARG E 17  ? 0.937 1.714 0.873 0.118  -0.114 0.310  346 ARG EEE NH2 
4549 N N   . PHE E 18  ? 0.587 1.153 0.580 0.062  -0.104 0.312  347 PHE EEE N   
4550 C CA  . PHE E 18  ? 0.546 1.121 0.534 0.055  -0.096 0.290  347 PHE EEE CA  
4551 C C   . PHE E 18  ? 0.512 1.117 0.490 0.062  -0.093 0.266  347 PHE EEE C   
4552 O O   . PHE E 18  ? 0.530 1.142 0.507 0.073  -0.099 0.263  347 PHE EEE O   
4553 C CB  . PHE E 18  ? 0.529 1.065 0.528 0.048  -0.095 0.276  347 PHE EEE CB  
4554 C CG  . PHE E 18  ? 0.533 1.053 0.540 0.036  -0.093 0.289  347 PHE EEE CG  
4555 C CD1 . PHE E 18  ? 0.552 1.068 0.565 0.032  -0.095 0.318  347 PHE EEE CD1 
4556 C CD2 . PHE E 18  ? 0.515 1.024 0.524 0.028  -0.088 0.273  347 PHE EEE CD2 
4557 C CE1 . PHE E 18  ? 0.560 1.064 0.584 0.021  -0.092 0.328  347 PHE EEE CE1 
4558 C CE2 . PHE E 18  ? 0.515 1.013 0.533 0.018  -0.086 0.283  347 PHE EEE CE2 
4559 C CZ  . PHE E 18  ? 0.541 1.035 0.566 0.014  -0.088 0.309  347 PHE EEE CZ  
4560 N N   . ALA E 19  ? 0.481 1.103 0.454 0.057  -0.086 0.250  348 ALA EEE N   
4561 C CA  . ALA E 19  ? 0.456 1.105 0.425 0.062  -0.083 0.224  348 ALA EEE CA  
4562 C C   . ALA E 19  ? 0.441 1.062 0.417 0.063  -0.083 0.202  348 ALA EEE C   
4563 O O   . ALA E 19  ? 0.457 1.042 0.439 0.057  -0.083 0.203  348 ALA EEE O   
4564 C CB  . ALA E 19  ? 0.440 1.110 0.407 0.056  -0.075 0.213  348 ALA EEE CB  
4565 N N   . SER E 20  ? 0.419 1.057 0.394 0.070  -0.083 0.183  349 SER EEE N   
4566 C CA  . SER E 20  ? 0.403 1.025 0.385 0.068  -0.080 0.158  349 SER EEE CA  
4567 C C   . SER E 20  ? 0.391 1.006 0.374 0.058  -0.073 0.148  349 SER EEE C   
4568 O O   . SER E 20  ? 0.383 1.023 0.364 0.057  -0.070 0.149  349 SER EEE O   
4569 C CB  . SER E 20  ? 0.398 1.046 0.380 0.075  -0.080 0.139  349 SER EEE CB  
4570 O OG  . SER E 20  ? 0.411 1.054 0.395 0.084  -0.088 0.143  349 SER EEE OG  
4571 N N   . VAL E 21  ? 0.383 0.969 0.371 0.053  -0.071 0.138  350 VAL EEE N   
4572 C CA  . VAL E 21  ? 0.377 0.950 0.366 0.045  -0.065 0.132  350 VAL EEE CA  
4573 C C   . VAL E 21  ? 0.369 0.967 0.362 0.045  -0.060 0.114  350 VAL EEE C   
4574 O O   . VAL E 21  ? 0.368 0.972 0.363 0.041  -0.057 0.113  350 VAL EEE O   
4575 C CB  . VAL E 21  ? 0.374 0.915 0.366 0.040  -0.064 0.126  350 VAL EEE CB  
4576 C CG1 . VAL E 21  ? 0.370 0.914 0.366 0.042  -0.062 0.108  350 VAL EEE CG1 
4577 C CG2 . VAL E 21  ? 0.364 0.892 0.357 0.033  -0.060 0.125  350 VAL EEE CG2 
4578 N N   . TYR E 22  ? 0.365 0.981 0.362 0.050  -0.059 0.098  351 TYR EEE N   
4579 C CA  . TYR E 22  ? 0.365 1.006 0.371 0.050  -0.054 0.077  351 TYR EEE CA  
4580 C C   . TYR E 22  ? 0.370 1.047 0.374 0.054  -0.055 0.080  351 TYR EEE C   
4581 O O   . TYR E 22  ? 0.368 1.058 0.381 0.052  -0.051 0.067  351 TYR EEE O   
4582 C CB  . TYR E 22  ? 0.360 1.014 0.372 0.054  -0.054 0.060  351 TYR EEE CB  
4583 C CG  . TYR E 22  ? 0.368 1.060 0.377 0.064  -0.058 0.059  351 TYR EEE CG  
4584 C CD1 . TYR E 22  ? 0.378 1.068 0.379 0.070  -0.065 0.074  351 TYR EEE CD1 
4585 C CD2 . TYR E 22  ? 0.366 1.098 0.381 0.068  -0.057 0.043  351 TYR EEE CD2 
4586 C CE1 . TYR E 22  ? 0.387 1.112 0.383 0.081  -0.070 0.076  351 TYR EEE CE1 
4587 C CE2 . TYR E 22  ? 0.376 1.148 0.387 0.078  -0.061 0.043  351 TYR EEE CE2 
4588 C CZ  . TYR E 22  ? 0.386 1.154 0.386 0.085  -0.068 0.061  351 TYR EEE CZ  
4589 O OH  . TYR E 22  ? 0.396 1.205 0.391 0.096  -0.073 0.063  351 TYR EEE OH  
4590 N N   . ALA E 23  ? 0.379 1.072 0.373 0.059  -0.060 0.098  352 ALA EEE N   
4591 C CA  . ALA E 23  ? 0.389 1.121 0.378 0.063  -0.061 0.105  352 ALA EEE CA  
4592 C C   . ALA E 23  ? 0.392 1.109 0.374 0.057  -0.061 0.130  352 ALA EEE C   
4593 O O   . ALA E 23  ? 0.397 1.134 0.370 0.060  -0.064 0.150  352 ALA EEE O   
4594 C CB  . ALA E 23  ? 0.395 1.161 0.378 0.073  -0.065 0.108  352 ALA EEE CB  
4595 N N   . TRP E 24  ? 0.398 1.081 0.383 0.050  -0.059 0.130  353 TRP EEE N   
4596 C CA  . TRP E 24  ? 0.411 1.076 0.393 0.044  -0.060 0.151  353 TRP EEE CA  
4597 C C   . TRP E 24  ? 0.413 1.114 0.392 0.043  -0.059 0.161  353 TRP EEE C   
4598 O O   . TRP E 24  ? 0.392 1.127 0.374 0.046  -0.056 0.145  353 TRP EEE O   
4599 C CB  . TRP E 24  ? 0.412 1.044 0.400 0.037  -0.058 0.145  353 TRP EEE CB  
4600 C CG  . TRP E 24  ? 0.413 1.055 0.409 0.036  -0.054 0.125  353 TRP EEE CG  
4601 C CD1 . TRP E 24  ? 0.413 1.049 0.416 0.037  -0.051 0.105  353 TRP EEE CD1 
4602 C CD2 . TRP E 24  ? 0.427 1.084 0.426 0.033  -0.052 0.123  353 TRP EEE CD2 
4603 N NE1 . TRP E 24  ? 0.415 1.059 0.428 0.036  -0.048 0.092  353 TRP EEE NE1 
4604 C CE2 . TRP E 24  ? 0.427 1.085 0.437 0.034  -0.049 0.101  353 TRP EEE CE2 
4605 C CE3 . TRP E 24  ? 0.439 1.108 0.434 0.030  -0.052 0.138  353 TRP EEE CE3 
4606 C CZ2 . TRP E 24  ? 0.425 1.097 0.444 0.034  -0.048 0.092  353 TRP EEE CZ2 
4607 C CZ3 . TRP E 24  ? 0.444 1.130 0.446 0.029  -0.049 0.128  353 TRP EEE CZ3 
4608 C CH2 . TRP E 24  ? 0.432 1.120 0.446 0.032  -0.048 0.105  353 TRP EEE CH2 
4609 N N   . ASN E 25  ? 0.430 1.126 0.403 0.040  -0.061 0.187  354 ASN EEE N   
4610 C CA  . ASN E 25  ? 0.449 1.180 0.418 0.038  -0.059 0.202  354 ASN EEE CA  
4611 C C   . ASN E 25  ? 0.449 1.173 0.422 0.030  -0.055 0.200  354 ASN EEE C   
4612 O O   . ASN E 25  ? 0.441 1.125 0.419 0.025  -0.056 0.201  354 ASN EEE O   
4613 C CB  . ASN E 25  ? 0.473 1.201 0.435 0.038  -0.063 0.232  354 ASN EEE CB  
4614 C CG  . ASN E 25  ? 0.491 1.265 0.447 0.037  -0.060 0.249  354 ASN EEE CG  
4615 O OD1 . ASN E 25  ? 0.503 1.278 0.461 0.028  -0.057 0.260  354 ASN EEE OD1 
4616 N ND2 . ASN E 25  ? 0.491 1.305 0.438 0.045  -0.061 0.250  354 ASN EEE ND2 
4617 N N   . ARG E 26  ? 0.467 1.232 0.440 0.029  -0.052 0.196  355 ARG EEE N   
4618 C CA  . ARG E 26  ? 0.484 1.253 0.462 0.021  -0.048 0.195  355 ARG EEE CA  
4619 C C   . ARG E 26  ? 0.508 1.317 0.480 0.017  -0.046 0.216  355 ARG EEE C   
4620 O O   . ARG E 26  ? 0.487 1.344 0.454 0.023  -0.045 0.212  355 ARG EEE O   
4621 C CB  . ARG E 26  ? 0.486 1.273 0.473 0.025  -0.046 0.166  355 ARG EEE CB  
4622 C CG  . ARG E 26  ? 0.493 1.286 0.487 0.019  -0.044 0.162  355 ARG EEE CG  
4623 C CD  . ARG E 26  ? 0.504 1.316 0.510 0.024  -0.043 0.133  355 ARG EEE CD  
4624 N NE  . ARG E 26  ? 0.515 1.287 0.530 0.026  -0.045 0.118  355 ARG EEE NE  
4625 C CZ  . ARG E 26  ? 0.534 1.268 0.551 0.022  -0.046 0.120  355 ARG EEE CZ  
4626 N NH1 . ARG E 26  ? 0.566 1.296 0.581 0.016  -0.046 0.136  355 ARG EEE NH1 
4627 N NH2 . ARG E 26  ? 0.562 1.263 0.585 0.024  -0.048 0.109  355 ARG EEE NH2 
4628 N N   . LYS E 27  ? 0.538 1.330 0.512 0.008  -0.045 0.237  356 LYS EEE N   
4629 C CA  . LYS E 27  ? 0.558 1.386 0.529 0.001  -0.041 0.257  356 LYS EEE CA  
4630 C C   . LYS E 27  ? 0.554 1.390 0.534 -0.005 -0.037 0.244  356 LYS EEE C   
4631 O O   . LYS E 27  ? 0.532 1.327 0.520 -0.010 -0.039 0.243  356 LYS EEE O   
4632 C CB  . LYS E 27  ? 0.595 1.398 0.565 -0.006 -0.042 0.290  356 LYS EEE CB  
4633 C CG  . LYS E 27  ? 0.625 1.465 0.593 -0.015 -0.037 0.315  356 LYS EEE CG  
4634 C CD  . LYS E 27  ? 0.674 1.484 0.646 -0.023 -0.039 0.349  356 LYS EEE CD  
4635 C CE  . LYS E 27  ? 0.718 1.514 0.684 -0.015 -0.045 0.366  356 LYS EEE CE  
4636 N NZ  . LYS E 27  ? 0.739 1.589 0.690 -0.007 -0.044 0.371  356 LYS EEE NZ  
4637 N N   . ARG E 28  ? 0.541 1.430 0.521 -0.004 -0.034 0.232  357 ARG EEE N   
4638 C CA  . ARG E 28  ? 0.519 1.425 0.509 -0.010 -0.030 0.222  357 ARG EEE CA  
4639 C C   . ARG E 28  ? 0.526 1.443 0.514 -0.023 -0.026 0.251  357 ARG EEE C   
4640 O O   . ARG E 28  ? 0.542 1.495 0.521 -0.025 -0.023 0.271  357 ARG EEE O   
4641 C CB  . ARG E 28  ? 0.504 1.466 0.496 -0.004 -0.028 0.196  357 ARG EEE CB  
4642 C CG  . ARG E 28  ? 0.496 1.477 0.500 -0.008 -0.026 0.182  357 ARG EEE CG  
4643 C CD  . ARG E 28  ? 0.509 1.562 0.514 -0.006 -0.022 0.168  357 ARG EEE CD  
4644 N NE  . ARG E 28  ? 0.536 1.629 0.527 -0.010 -0.018 0.194  357 ARG EEE NE  
4645 C CZ  . ARG E 28  ? 0.554 1.713 0.540 -0.005 -0.015 0.186  357 ARG EEE CZ  
4646 N NH1 . ARG E 28  ? 0.563 1.756 0.560 0.004  -0.017 0.150  357 ARG EEE NH1 
4647 N NH2 . ARG E 28  ? 0.575 1.767 0.547 -0.009 -0.012 0.215  357 ARG EEE NH2 
4648 N N   . ILE E 29  ? 0.542 1.428 0.540 -0.031 -0.026 0.253  358 ILE EEE N   
4649 C CA  . ILE E 29  ? 0.552 1.443 0.555 -0.045 -0.022 0.278  358 ILE EEE CA  
4650 C C   . ILE E 29  ? 0.548 1.478 0.558 -0.050 -0.017 0.264  358 ILE EEE C   
4651 O O   . ILE E 29  ? 0.529 1.446 0.548 -0.045 -0.020 0.238  358 ILE EEE O   
4652 C CB  . ILE E 29  ? 0.562 1.392 0.573 -0.051 -0.025 0.289  358 ILE EEE CB  
4653 C CG1 . ILE E 29  ? 0.580 1.375 0.585 -0.045 -0.030 0.302  358 ILE EEE CG1 
4654 C CG2 . ILE E 29  ? 0.580 1.413 0.601 -0.067 -0.021 0.311  358 ILE EEE CG2 
4655 C CD1 . ILE E 29  ? 0.589 1.326 0.604 -0.048 -0.035 0.305  358 ILE EEE CD1 
4656 N N   . SER E 30  ? 0.567 1.547 0.575 -0.059 -0.010 0.280  359 SER EEE N   
4657 C CA  . SER E 30  ? 0.566 1.598 0.580 -0.064 -0.005 0.267  359 SER EEE CA  
4658 C C   . SER E 30  ? 0.582 1.643 0.596 -0.080 0.003  0.298  359 SER EEE C   
4659 O O   . SER E 30  ? 0.590 1.642 0.596 -0.084 0.004  0.330  359 SER EEE O   
4660 C CB  . SER E 30  ? 0.570 1.654 0.579 -0.052 -0.005 0.241  359 SER EEE CB  
4661 O OG  . SER E 30  ? 0.596 1.674 0.618 -0.044 -0.009 0.206  359 SER EEE OG  
4662 N N   . ASN E 31  ? 0.575 1.668 0.600 -0.089 0.008  0.290  360 ASN EEE N   
4663 C CA  . ASN E 31  ? 0.589 1.726 0.616 -0.105 0.018  0.315  360 ASN EEE CA  
4664 C C   . ASN E 31  ? 0.602 1.694 0.631 -0.118 0.019  0.354  360 ASN EEE C   
4665 O O   . ASN E 31  ? 0.633 1.748 0.653 -0.125 0.023  0.386  360 ASN EEE O   
4666 C CB  . ASN E 31  ? 0.606 1.814 0.617 -0.103 0.023  0.321  360 ASN EEE CB  
4667 C CG  . ASN E 31  ? 0.590 1.856 0.606 -0.094 0.023  0.283  360 ASN EEE CG  
4668 O OD1 . ASN E 31  ? 0.593 1.900 0.617 -0.103 0.029  0.276  360 ASN EEE OD1 
4669 N ND2 . ASN E 31  ? 0.570 1.838 0.581 -0.077 0.017  0.256  360 ASN EEE ND2 
4670 N N   . CYS E 32  ? 0.588 1.621 0.632 -0.122 0.014  0.350  361 CYS EEE N   
4671 C CA  . CYS E 32  ? 0.615 1.600 0.668 -0.133 0.014  0.382  361 CYS EEE CA  
4672 C C   . CYS E 32  ? 0.597 1.536 0.670 -0.139 0.011  0.368  361 CYS EEE C   
4673 O O   . CYS E 32  ? 0.558 1.491 0.633 -0.129 0.006  0.335  361 CYS EEE O   
4674 C CB  . CYS E 32  ? 0.629 1.577 0.671 -0.123 0.007  0.395  361 CYS EEE CB  
4675 S SG  . CYS E 32  ? 0.624 1.530 0.660 -0.102 -0.003 0.358  361 CYS EEE SG  
4676 N N   . VAL E 33  ? 0.623 1.534 0.713 -0.154 0.013  0.392  362 VAL EEE N   
4677 C CA  . VAL E 33  ? 0.631 1.498 0.743 -0.160 0.010  0.381  362 VAL EEE CA  
4678 C C   . VAL E 33  ? 0.635 1.441 0.748 -0.150 -0.000 0.381  362 VAL EEE C   
4679 O O   . VAL E 33  ? 0.646 1.431 0.758 -0.152 -0.001 0.409  362 VAL EEE O   
4680 C CB  . VAL E 33  ? 0.656 1.527 0.791 -0.182 0.017  0.406  362 VAL EEE CB  
4681 C CG1 . VAL E 33  ? 0.645 1.477 0.805 -0.188 0.013  0.390  362 VAL EEE CG1 
4682 C CG2 . VAL E 33  ? 0.657 1.594 0.790 -0.194 0.028  0.410  362 VAL EEE CG2 
4683 N N   . ALA E 34  ? 0.631 1.410 0.744 -0.138 -0.007 0.351  363 ALA EEE N   
4684 C CA  . ALA E 34  ? 0.631 1.358 0.743 -0.128 -0.016 0.344  363 ALA EEE CA  
4685 C C   . ALA E 34  ? 0.657 1.345 0.794 -0.137 -0.019 0.342  363 ALA EEE C   
4686 O O   . ALA E 34  ? 0.667 1.360 0.813 -0.137 -0.020 0.320  363 ALA EEE O   
4687 C CB  . ALA E 34  ? 0.605 1.331 0.702 -0.111 -0.021 0.314  363 ALA EEE CB  
4688 N N   . ASP E 35  ? 0.695 1.349 0.844 -0.142 -0.022 0.363  364 ASP EEE N   
4689 C CA  . ASP E 35  ? 0.708 1.321 0.884 -0.148 -0.026 0.356  364 ASP EEE CA  
4690 C C   . ASP E 35  ? 0.674 1.252 0.842 -0.131 -0.036 0.336  364 ASP EEE C   
4691 O O   . ASP E 35  ? 0.676 1.229 0.840 -0.126 -0.040 0.349  364 ASP EEE O   
4692 C CB  . ASP E 35  ? 0.761 1.354 0.960 -0.162 -0.025 0.386  364 ASP EEE CB  
4693 C CG  . ASP E 35  ? 0.783 1.342 1.016 -0.170 -0.029 0.376  364 ASP EEE CG  
4694 O OD1 . ASP E 35  ? 0.757 1.308 0.992 -0.163 -0.034 0.345  364 ASP EEE OD1 
4695 O OD2 . ASP E 35  ? 0.823 1.362 1.080 -0.183 -0.027 0.399  364 ASP EEE OD2 
4696 N N   . TYR E 36  ? 0.630 1.208 0.794 -0.124 -0.039 0.307  365 TYR EEE N   
4697 C CA  . TYR E 36  ? 0.602 1.153 0.756 -0.109 -0.047 0.288  365 TYR EEE CA  
4698 C C   . TYR E 36  ? 0.611 1.125 0.789 -0.112 -0.054 0.283  365 TYR EEE C   
4699 O O   . TYR E 36  ? 0.605 1.094 0.776 -0.101 -0.060 0.275  365 TYR EEE O   
4700 C CB  . TYR E 36  ? 0.565 1.132 0.707 -0.100 -0.048 0.262  365 TYR EEE CB  
4701 C CG  . TYR E 36  ? 0.535 1.138 0.657 -0.095 -0.044 0.261  365 TYR EEE CG  
4702 C CD1 . TYR E 36  ? 0.514 1.117 0.616 -0.083 -0.045 0.259  365 TYR EEE CD1 
4703 C CD2 . TYR E 36  ? 0.527 1.166 0.654 -0.103 -0.038 0.260  365 TYR EEE CD2 
4704 C CE1 . TYR E 36  ? 0.508 1.146 0.596 -0.078 -0.041 0.255  365 TYR EEE CE1 
4705 C CE2 . TYR E 36  ? 0.510 1.186 0.623 -0.097 -0.034 0.255  365 TYR EEE CE2 
4706 C CZ  . TYR E 36  ? 0.501 1.176 0.595 -0.085 -0.036 0.253  365 TYR EEE CZ  
4707 O OH  . TYR E 36  ? 0.485 1.197 0.568 -0.080 -0.033 0.245  365 TYR EEE OH  
4708 N N   . SER E 37  ? 0.621 1.133 0.826 -0.125 -0.052 0.284  366 SER EEE N   
4709 C CA  . SER E 37  ? 0.632 1.114 0.864 -0.128 -0.058 0.273  366 SER EEE CA  
4710 C C   . SER E 37  ? 0.637 1.086 0.880 -0.127 -0.063 0.288  366 SER EEE C   
4711 O O   . SER E 37  ? 0.632 1.055 0.888 -0.122 -0.070 0.272  366 SER EEE O   
4712 C CB  . SER E 37  ? 0.648 1.140 0.910 -0.144 -0.055 0.271  366 SER EEE CB  
4713 O OG  . SER E 37  ? 0.683 1.191 0.951 -0.159 -0.046 0.298  366 SER EEE OG  
4714 N N   . VAL E 38  ? 0.646 1.097 0.884 -0.132 -0.059 0.317  367 VAL EEE N   
4715 C CA  . VAL E 38  ? 0.663 1.084 0.910 -0.129 -0.064 0.335  367 VAL EEE CA  
4716 C C   . VAL E 38  ? 0.642 1.052 0.865 -0.111 -0.070 0.322  367 VAL EEE C   
4717 O O   . VAL E 38  ? 0.652 1.035 0.885 -0.105 -0.076 0.328  367 VAL EEE O   
4718 C CB  . VAL E 38  ? 0.687 1.119 0.932 -0.137 -0.058 0.373  367 VAL EEE CB  
4719 C CG1 . VAL E 38  ? 0.708 1.146 0.981 -0.157 -0.051 0.388  367 VAL EEE CG1 
4720 C CG2 . VAL E 38  ? 0.673 1.142 0.882 -0.131 -0.052 0.380  367 VAL EEE CG2 
4721 N N   . LEU E 39  ? 0.620 1.052 0.817 -0.101 -0.068 0.305  368 LEU EEE N   
4722 C CA  . LEU E 39  ? 0.616 1.040 0.790 -0.085 -0.073 0.290  368 LEU EEE CA  
4723 C C   . LEU E 39  ? 0.606 1.015 0.789 -0.081 -0.079 0.261  368 LEU EEE C   
4724 O O   . LEU E 39  ? 0.622 1.007 0.812 -0.074 -0.085 0.254  368 LEU EEE O   
4725 C CB  . LEU E 39  ? 0.604 1.058 0.748 -0.079 -0.068 0.287  368 LEU EEE CB  
4726 C CG  . LEU E 39  ? 0.613 1.092 0.747 -0.083 -0.062 0.312  368 LEU EEE CG  
4727 C CD1 . LEU E 39  ? 0.592 1.100 0.699 -0.074 -0.058 0.302  368 LEU EEE CD1 
4728 C CD2 . LEU E 39  ? 0.623 1.086 0.760 -0.080 -0.065 0.334  368 LEU EEE CD2 
4729 N N   . TYR E 40  ? 0.599 1.023 0.780 -0.083 -0.077 0.245  369 TYR EEE N   
4730 C CA  . TYR E 40  ? 0.585 1.004 0.767 -0.076 -0.082 0.218  369 TYR EEE CA  
4731 C C   . TYR E 40  ? 0.586 0.987 0.801 -0.081 -0.087 0.208  369 TYR EEE C   
4732 O O   . TYR E 40  ? 0.600 0.996 0.816 -0.074 -0.093 0.186  369 TYR EEE O   
4733 C CB  . TYR E 40  ? 0.572 1.016 0.740 -0.073 -0.079 0.205  369 TYR EEE CB  
4734 C CG  . TYR E 40  ? 0.591 1.054 0.774 -0.085 -0.075 0.207  369 TYR EEE CG  
4735 C CD1 . TYR E 40  ? 0.601 1.060 0.811 -0.092 -0.078 0.196  369 TYR EEE CD1 
4736 C CD2 . TYR E 40  ? 0.593 1.083 0.764 -0.088 -0.068 0.216  369 TYR EEE CD2 
4737 C CE1 . TYR E 40  ? 0.605 1.084 0.831 -0.104 -0.073 0.196  369 TYR EEE CE1 
4738 C CE2 . TYR E 40  ? 0.597 1.108 0.782 -0.099 -0.064 0.217  369 TYR EEE CE2 
4739 C CZ  . TYR E 40  ? 0.602 1.107 0.814 -0.107 -0.067 0.207  369 TYR EEE CZ  
4740 O OH  . TYR E 40  ? 0.595 1.123 0.823 -0.118 -0.062 0.206  369 TYR EEE OH  
4741 N N   . ASN E 41  ? 0.609 1.003 0.851 -0.094 -0.086 0.223  370 ASN EEE N   
4742 C CA  . ASN E 41  ? 0.622 0.996 0.902 -0.100 -0.091 0.213  370 ASN EEE CA  
4743 C C   . ASN E 41  ? 0.628 0.972 0.920 -0.096 -0.097 0.221  370 ASN EEE C   
4744 O O   . ASN E 41  ? 0.646 0.973 0.972 -0.099 -0.103 0.209  370 ASN EEE O   
4745 C CB  . ASN E 41  ? 0.638 1.017 0.947 -0.118 -0.087 0.224  370 ASN EEE CB  
4746 C CG  . ASN E 41  ? 0.630 1.038 0.935 -0.122 -0.083 0.210  370 ASN EEE CG  
4747 O OD1 . ASN E 41  ? 0.621 1.040 0.913 -0.112 -0.086 0.186  370 ASN EEE OD1 
4748 N ND2 . ASN E 41  ? 0.648 1.071 0.965 -0.136 -0.076 0.225  370 ASN EEE ND2 
4749 N N   . SER E 42  ? 0.610 0.952 0.878 -0.088 -0.096 0.237  371 SER EEE N   
4750 C CA  . SER E 42  ? 0.621 0.938 0.898 -0.082 -0.103 0.245  371 SER EEE CA  
4751 C C   . SER E 42  ? 0.616 0.925 0.892 -0.070 -0.110 0.216  371 SER EEE C   
4752 O O   . SER E 42  ? 0.597 0.925 0.849 -0.063 -0.108 0.199  371 SER EEE O   
4753 C CB  . SER E 42  ? 0.614 0.937 0.863 -0.076 -0.099 0.268  371 SER EEE CB  
4754 O OG  . SER E 42  ? 0.606 0.907 0.863 -0.068 -0.106 0.274  371 SER EEE OG  
4755 N N   . ALA E 43  ? 0.636 0.922 0.939 -0.067 -0.118 0.211  372 ALA EEE N   
4756 C CA  . ALA E 43  ? 0.628 0.907 0.932 -0.055 -0.126 0.185  372 ALA EEE CA  
4757 C C   . ALA E 43  ? 0.626 0.900 0.909 -0.043 -0.127 0.195  372 ALA EEE C   
4758 O O   . ALA E 43  ? 0.625 0.898 0.906 -0.033 -0.133 0.174  372 ALA EEE O   
4759 C CB  . ALA E 43  ? 0.643 0.901 0.994 -0.057 -0.134 0.171  372 ALA EEE CB  
4760 N N   . SER E 44  ? 0.634 0.910 0.902 -0.045 -0.123 0.223  373 SER EEE N   
4761 C CA  . SER E 44  ? 0.636 0.910 0.885 -0.035 -0.124 0.235  373 SER EEE CA  
4762 C C   . SER E 44  ? 0.616 0.913 0.826 -0.028 -0.119 0.225  373 SER EEE C   
4763 O O   . SER E 44  ? 0.630 0.927 0.826 -0.018 -0.121 0.225  373 SER EEE O   
4764 C CB  . SER E 44  ? 0.656 0.927 0.905 -0.040 -0.122 0.270  373 SER EEE CB  
4765 O OG  . SER E 44  ? 0.693 0.940 0.980 -0.048 -0.126 0.282  373 SER EEE OG  
4766 N N   . PHE E 45  ? 0.593 0.909 0.789 -0.032 -0.113 0.218  374 PHE EEE N   
4767 C CA  . PHE E 45  ? 0.573 0.908 0.736 -0.026 -0.108 0.207  374 PHE EEE CA  
4768 C C   . PHE E 45  ? 0.573 0.909 0.736 -0.022 -0.111 0.180  374 PHE EEE C   
4769 O O   . PHE E 45  ? 0.580 0.920 0.754 -0.028 -0.111 0.170  374 PHE EEE O   
4770 C CB  . PHE E 45  ? 0.562 0.917 0.709 -0.033 -0.100 0.217  374 PHE EEE CB  
4771 C CG  . PHE E 45  ? 0.583 0.944 0.729 -0.038 -0.096 0.244  374 PHE EEE CG  
4772 C CD1 . PHE E 45  ? 0.584 0.947 0.718 -0.031 -0.097 0.257  374 PHE EEE CD1 
4773 C CD2 . PHE E 45  ? 0.593 0.961 0.751 -0.049 -0.092 0.257  374 PHE EEE CD2 
4774 C CE1 . PHE E 45  ? 0.603 0.976 0.734 -0.035 -0.094 0.283  374 PHE EEE CE1 
4775 C CE2 . PHE E 45  ? 0.608 0.985 0.765 -0.054 -0.089 0.284  374 PHE EEE CE2 
4776 C CZ  . PHE E 45  ? 0.611 0.992 0.753 -0.047 -0.089 0.297  374 PHE EEE CZ  
4777 N N   . SER E 46  ? 0.562 0.898 0.714 -0.013 -0.113 0.168  375 SER EEE N   
4778 C CA  . SER E 46  ? 0.550 0.892 0.699 -0.008 -0.115 0.143  375 SER EEE CA  
4779 C C   . SER E 46  ? 0.535 0.894 0.657 -0.008 -0.109 0.139  375 SER EEE C   
4780 O O   . SER E 46  ? 0.525 0.893 0.647 -0.008 -0.110 0.124  375 SER EEE O   
4781 C CB  . SER E 46  ? 0.547 0.885 0.697 0.000  -0.119 0.133  375 SER EEE CB  
4782 O OG  . SER E 46  ? 0.548 0.888 0.678 0.004  -0.116 0.146  375 SER EEE OG  
4783 N N   . THR E 47  ? 0.522 0.888 0.624 -0.008 -0.103 0.153  376 THR EEE N   
4784 C CA  . THR E 47  ? 0.511 0.892 0.592 -0.008 -0.097 0.152  376 THR EEE CA  
4785 C C   . THR E 47  ? 0.513 0.900 0.595 -0.014 -0.093 0.166  376 THR EEE C   
4786 O O   . THR E 47  ? 0.522 0.910 0.605 -0.016 -0.092 0.182  376 THR EEE O   
4787 C CB  . THR E 47  ? 0.505 0.891 0.564 -0.002 -0.093 0.151  376 THR EEE CB  
4788 O OG1 . THR E 47  ? 0.502 0.885 0.562 0.002  -0.096 0.136  376 THR EEE OG1 
4789 C CG2 . THR E 47  ? 0.502 0.899 0.544 -0.002 -0.088 0.151  376 THR EEE CG2 
4790 N N   . PHE E 48  ? 0.495 0.891 0.577 -0.017 -0.092 0.161  377 PHE EEE N   
4791 C CA  . PHE E 48  ? 0.497 0.905 0.578 -0.023 -0.088 0.171  377 PHE EEE CA  
4792 C C   . PHE E 48  ? 0.487 0.908 0.557 -0.020 -0.087 0.161  377 PHE EEE C   
4793 O O   . PHE E 48  ? 0.484 0.911 0.564 -0.023 -0.089 0.155  377 PHE EEE O   
4794 C CB  . PHE E 48  ? 0.514 0.919 0.619 -0.032 -0.090 0.178  377 PHE EEE CB  
4795 C CG  . PHE E 48  ? 0.516 0.935 0.621 -0.039 -0.084 0.194  377 PHE EEE CG  
4796 C CD1 . PHE E 48  ? 0.512 0.950 0.605 -0.038 -0.081 0.191  377 PHE EEE CD1 
4797 C CD2 . PHE E 48  ? 0.536 0.951 0.653 -0.045 -0.083 0.212  377 PHE EEE CD2 
4798 C CE1 . PHE E 48  ? 0.518 0.974 0.611 -0.044 -0.076 0.203  377 PHE EEE CE1 
4799 C CE2 . PHE E 48  ? 0.546 0.979 0.661 -0.052 -0.078 0.228  377 PHE EEE CE2 
4800 C CZ  . PHE E 48  ? 0.541 0.997 0.645 -0.051 -0.074 0.222  377 PHE EEE CZ  
4801 N N   . LYS E 49  ? 0.483 0.906 0.534 -0.013 -0.085 0.158  378 LYS EEE N   
4802 C CA  . LYS E 49  ? 0.481 0.911 0.521 -0.009 -0.085 0.150  378 LYS EEE CA  
4803 C C   . LYS E 49  ? 0.487 0.931 0.522 -0.009 -0.081 0.155  378 LYS EEE C   
4804 O O   . LYS E 49  ? 0.487 0.934 0.516 -0.008 -0.077 0.160  378 LYS EEE O   
4805 C CB  . LYS E 49  ? 0.478 0.902 0.503 -0.003 -0.084 0.145  378 LYS EEE CB  
4806 C CG  . LYS E 49  ? 0.488 0.906 0.515 -0.001 -0.087 0.136  378 LYS EEE CG  
4807 C CD  . LYS E 49  ? 0.494 0.909 0.508 0.003  -0.085 0.133  378 LYS EEE CD  
4808 C CE  . LYS E 49  ? 0.506 0.922 0.519 0.005  -0.088 0.122  378 LYS EEE CE  
4809 N NZ  . LYS E 49  ? 0.522 0.948 0.528 0.008  -0.089 0.118  378 LYS EEE NZ  
4810 N N   . CYS E 50  ? 0.503 0.957 0.543 -0.010 -0.082 0.151  379 CYS EEE N   
4811 C CA  . CYS E 50  ? 0.514 0.984 0.553 -0.010 -0.080 0.152  379 CYS EEE CA  
4812 C C   . CYS E 50  ? 0.508 0.979 0.537 -0.001 -0.082 0.145  379 CYS EEE C   
4813 O O   . CYS E 50  ? 0.519 0.983 0.544 0.002  -0.086 0.140  379 CYS EEE O   
4814 C CB  . CYS E 50  ? 0.518 1.001 0.572 -0.017 -0.080 0.154  379 CYS EEE CB  
4815 S SG  . CYS E 50  ? 0.532 1.012 0.599 -0.028 -0.077 0.168  379 CYS EEE SG  
4816 N N   . TYR E 51  ? 0.507 0.987 0.532 0.002  -0.080 0.145  380 TYR EEE N   
4817 C CA  . TYR E 51  ? 0.493 0.973 0.512 0.011  -0.082 0.140  380 TYR EEE CA  
4818 C C   . TYR E 51  ? 0.495 0.994 0.522 0.013  -0.082 0.136  380 TYR EEE C   
4819 O O   . TYR E 51  ? 0.489 0.999 0.519 0.010  -0.079 0.137  380 TYR EEE O   
4820 C CB  . TYR E 51  ? 0.478 0.945 0.488 0.015  -0.079 0.141  380 TYR EEE CB  
4821 C CG  . TYR E 51  ? 0.470 0.922 0.473 0.013  -0.078 0.144  380 TYR EEE CG  
4822 C CD1 . TYR E 51  ? 0.457 0.909 0.463 0.007  -0.076 0.148  380 TYR EEE CD1 
4823 C CD2 . TYR E 51  ? 0.463 0.904 0.457 0.016  -0.080 0.144  380 TYR EEE CD2 
4824 C CE1 . TYR E 51  ? 0.450 0.890 0.451 0.007  -0.075 0.149  380 TYR EEE CE1 
4825 C CE2 . TYR E 51  ? 0.453 0.885 0.442 0.014  -0.078 0.144  380 TYR EEE CE2 
4826 C CZ  . TYR E 51  ? 0.456 0.887 0.450 0.010  -0.076 0.145  380 TYR EEE CZ  
4827 O OH  . TYR E 51  ? 0.462 0.885 0.451 0.009  -0.076 0.144  380 TYR EEE OH  
4828 N N   . GLY E 52  ? 0.490 0.995 0.520 0.017  -0.087 0.130  381 GLY EEE N   
4829 C CA  . GLY E 52  ? 0.496 1.022 0.536 0.020  -0.089 0.123  381 GLY EEE CA  
4830 C C   . GLY E 52  ? 0.492 1.039 0.543 0.012  -0.087 0.122  381 GLY EEE C   
4831 O O   . GLY E 52  ? 0.497 1.065 0.557 0.014  -0.088 0.114  381 GLY EEE O   
4832 N N   . VAL E 53  ? 0.493 1.036 0.546 0.002  -0.083 0.130  382 VAL EEE N   
4833 C CA  . VAL E 53  ? 0.501 1.062 0.566 -0.010 -0.079 0.133  382 VAL EEE CA  
4834 C C   . VAL E 53  ? 0.514 1.062 0.586 -0.016 -0.081 0.135  382 VAL EEE C   
4835 O O   . VAL E 53  ? 0.546 1.073 0.611 -0.015 -0.082 0.139  382 VAL EEE O   
4836 C CB  . VAL E 53  ? 0.511 1.081 0.575 -0.015 -0.073 0.143  382 VAL EEE CB  
4837 C CG1 . VAL E 53  ? 0.519 1.065 0.574 -0.016 -0.072 0.151  382 VAL EEE CG1 
4838 C CG2 . VAL E 53  ? 0.529 1.118 0.605 -0.027 -0.069 0.149  382 VAL EEE CG2 
4839 N N   . SER E 54  ? 0.530 1.092 0.617 -0.022 -0.082 0.130  383 SER EEE N   
4840 C CA  . SER E 54  ? 0.546 1.099 0.646 -0.030 -0.084 0.130  383 SER EEE CA  
4841 C C   . SER E 54  ? 0.547 1.103 0.660 -0.044 -0.078 0.143  383 SER EEE C   
4842 O O   . SER E 54  ? 0.537 1.115 0.656 -0.050 -0.073 0.147  383 SER EEE O   
4843 C CB  . SER E 54  ? 0.557 1.124 0.670 -0.030 -0.088 0.117  383 SER EEE CB  
4844 O OG  . SER E 54  ? 0.593 1.187 0.711 -0.031 -0.086 0.113  383 SER EEE OG  
4845 N N   . PRO E 55  ? 0.553 1.088 0.669 -0.048 -0.077 0.152  384 PRO EEE N   
4846 C CA  . PRO E 55  ? 0.582 1.115 0.708 -0.060 -0.072 0.169  384 PRO EEE CA  
4847 C C   . PRO E 55  ? 0.596 1.146 0.745 -0.073 -0.069 0.170  384 PRO EEE C   
4848 O O   . PRO E 55  ? 0.638 1.202 0.791 -0.082 -0.063 0.185  384 PRO EEE O   
4849 C CB  . PRO E 55  ? 0.590 1.095 0.722 -0.061 -0.076 0.172  384 PRO EEE CB  
4850 C CG  . PRO E 55  ? 0.567 1.061 0.684 -0.048 -0.081 0.160  384 PRO EEE CG  
4851 C CD  . PRO E 55  ? 0.550 1.061 0.659 -0.041 -0.082 0.147  384 PRO EEE CD  
4852 N N   . THR E 56  ? 0.576 1.129 0.740 -0.074 -0.073 0.155  385 THR EEE N   
4853 C CA  . THR E 56  ? 0.586 1.153 0.776 -0.088 -0.071 0.154  385 THR EEE CA  
4854 C C   . THR E 56  ? 0.584 1.185 0.772 -0.092 -0.066 0.154  385 THR EEE C   
4855 O O   . THR E 56  ? 0.604 1.220 0.813 -0.106 -0.061 0.161  385 THR EEE O   
4856 C CB  . THR E 56  ? 0.583 1.147 0.790 -0.086 -0.078 0.133  385 THR EEE CB  
4857 O OG1 . THR E 56  ? 0.570 1.149 0.762 -0.073 -0.082 0.117  385 THR EEE OG1 
4858 C CG2 . THR E 56  ? 0.596 1.130 0.805 -0.083 -0.083 0.130  385 THR EEE CG2 
4859 N N   . LYS E 57  ? 0.572 1.187 0.741 -0.079 -0.067 0.146  386 LYS EEE N   
4860 C CA  . LYS E 57  ? 0.567 1.217 0.736 -0.080 -0.063 0.142  386 LYS EEE CA  
4861 C C   . LYS E 57  ? 0.583 1.246 0.742 -0.085 -0.056 0.160  386 LYS EEE C   
4862 O O   . LYS E 57  ? 0.553 1.251 0.719 -0.091 -0.051 0.159  386 LYS EEE O   
4863 C CB  . LYS E 57  ? 0.546 1.202 0.700 -0.063 -0.070 0.125  386 LYS EEE CB  
4864 C CG  . LYS E 57  ? 0.543 1.197 0.705 -0.057 -0.077 0.108  386 LYS EEE CG  
4865 C CD  . LYS E 57  ? 0.530 1.186 0.677 -0.039 -0.084 0.096  386 LYS EEE CD  
4866 C CE  . LYS E 57  ? 0.523 1.211 0.673 -0.035 -0.084 0.087  386 LYS EEE CE  
4867 N NZ  . LYS E 57  ? 0.522 1.209 0.662 -0.017 -0.092 0.075  386 LYS EEE NZ  
4868 N N   . LEU E 58  ? 0.569 0.837 0.711 -0.057 -0.076 0.105  387 LEU EEE N   
4869 C CA  . LEU E 58  ? 0.582 0.831 0.704 -0.055 -0.060 0.125  387 LEU EEE CA  
4870 C C   . LEU E 58  ? 0.613 0.866 0.771 -0.065 -0.046 0.140  387 LEU EEE C   
4871 O O   . LEU E 58  ? 0.637 0.897 0.783 -0.061 -0.031 0.157  387 LEU EEE O   
4872 C CB  . LEU E 58  ? 0.573 0.795 0.668 -0.053 -0.062 0.124  387 LEU EEE CB  
4873 C CG  . LEU E 58  ? 0.557 0.773 0.614 -0.042 -0.069 0.117  387 LEU EEE CG  
4874 C CD1 . LEU E 58  ? 0.554 0.745 0.591 -0.042 -0.071 0.115  387 LEU EEE CD1 
4875 C CD2 . LEU E 58  ? 0.556 0.777 0.596 -0.032 -0.060 0.125  387 LEU EEE CD2 
4876 N N   . ASN E 59  ? 0.642 0.894 0.846 -0.078 -0.050 0.134  388 ASN EEE N   
4877 C CA  . ASN E 59  ? 0.681 0.934 0.933 -0.090 -0.034 0.153  388 ASN EEE CA  
4878 C C   . ASN E 59  ? 0.674 0.960 0.951 -0.092 -0.025 0.159  388 ASN EEE C   
4879 O O   . ASN E 59  ? 0.680 0.972 0.991 -0.099 -0.006 0.182  388 ASN EEE O   
4880 C CB  . ASN E 59  ? 0.726 0.967 1.034 -0.105 -0.041 0.138  388 ASN EEE CB  
4881 C CG  . ASN E 59  ? 0.781 0.988 1.090 -0.106 -0.035 0.152  388 ASN EEE CG  
4882 O OD1 . ASN E 59  ? 0.866 1.063 1.128 -0.095 -0.028 0.173  388 ASN EEE OD1 
4883 N ND2 . ASN E 59  ? 0.802 0.996 1.170 -0.118 -0.039 0.138  388 ASN EEE ND2 
4884 N N   . ASP E 60  ? 0.651 0.958 0.915 -0.084 -0.035 0.143  389 ASP EEE N   
4885 C CA  . ASP E 60  ? 0.640 0.981 0.930 -0.083 -0.028 0.147  389 ASP EEE CA  
4886 C C   . ASP E 60  ? 0.588 0.935 0.833 -0.065 -0.022 0.152  389 ASP EEE C   
4887 O O   . ASP E 60  ? 0.577 0.952 0.840 -0.060 -0.018 0.150  389 ASP EEE O   
4888 C CB  . ASP E 60  ? 0.674 1.041 1.004 -0.088 -0.046 0.123  389 ASP EEE CB  
4889 C CG  . ASP E 60  ? 0.732 1.135 1.115 -0.093 -0.038 0.126  389 ASP EEE CG  
4890 O OD1 . ASP E 60  ? 0.767 1.170 1.178 -0.102 -0.016 0.146  389 ASP EEE OD1 
4891 O OD2 . ASP E 60  ? 0.762 1.195 1.158 -0.088 -0.052 0.110  389 ASP EEE OD2 
4892 N N   . LEU E 61  ? 0.560 0.884 0.756 -0.057 -0.021 0.154  390 LEU EEE N   
4893 C CA  . LEU E 61  ? 0.553 0.879 0.714 -0.041 -0.018 0.152  390 LEU EEE CA  
4894 C C   . LEU E 61  ? 0.557 0.882 0.691 -0.037 -0.000 0.163  390 LEU EEE C   
4895 O O   . LEU E 61  ? 0.551 0.864 0.678 -0.043 0.004  0.176  390 LEU EEE O   
4896 C CB  . LEU E 61  ? 0.545 0.851 0.678 -0.034 -0.034 0.140  390 LEU EEE CB  
4897 C CG  . LEU E 61  ? 0.537 0.857 0.685 -0.030 -0.051 0.131  390 LEU EEE CG  
4898 C CD1 . LEU E 61  ? 0.540 0.844 0.658 -0.024 -0.063 0.125  390 LEU EEE CD1 
4899 C CD2 . LEU E 61  ? 0.538 0.883 0.704 -0.019 -0.047 0.132  390 LEU EEE CD2 
4900 N N   . CYS E 62  ? 0.556 0.896 0.677 -0.025 0.009  0.157  391 CYS EEE N   
4901 C CA  . CYS E 62  ? 0.563 0.916 0.657 -0.018 0.025  0.159  391 CYS EEE CA  
4902 C C   . CYS E 62  ? 0.548 0.889 0.616 -0.006 0.020  0.139  391 CYS EEE C   
4903 O O   . CYS E 62  ? 0.524 0.861 0.609 0.001  0.014  0.127  391 CYS EEE O   
4904 C CB  . CYS E 62  ? 0.596 0.988 0.709 -0.015 0.044  0.164  391 CYS EEE CB  
4905 S SG  . CYS E 62  ? 0.633 1.044 0.782 -0.030 0.057  0.194  391 CYS EEE SG  
4906 N N   . PHE E 63  ? 0.560 0.900 0.596 -0.002 0.022  0.135  392 PHE EEE N   
4907 C CA  . PHE E 63  ? 0.546 0.876 0.564 0.008  0.018  0.112  392 PHE EEE CA  
4908 C C   . PHE E 63  ? 0.580 0.945 0.577 0.016  0.031  0.100  392 PHE EEE C   
4909 O O   . PHE E 63  ? 0.579 0.969 0.560 0.015  0.040  0.120  392 PHE EEE O   
4910 C CB  . PHE E 63  ? 0.524 0.821 0.525 0.004  0.004  0.113  392 PHE EEE CB  
4911 C CG  . PHE E 63  ? 0.498 0.771 0.516 -0.002 -0.008 0.119  392 PHE EEE CG  
4912 C CD1 . PHE E 63  ? 0.479 0.741 0.512 0.004  -0.013 0.111  392 PHE EEE CD1 
4913 C CD2 . PHE E 63  ? 0.497 0.761 0.519 -0.012 -0.014 0.134  392 PHE EEE CD2 
4914 C CE1 . PHE E 63  ? 0.466 0.717 0.509 0.002  -0.025 0.118  392 PHE EEE CE1 
4915 C CE2 . PHE E 63  ? 0.483 0.735 0.518 -0.016 -0.027 0.134  392 PHE EEE CE2 
4916 C CZ  . PHE E 63  ? 0.469 0.719 0.511 -0.008 -0.033 0.127  392 PHE EEE CZ  
4917 N N   . THR E 64  ? 0.604 0.974 0.604 0.026  0.033  0.070  393 THR EEE N   
4918 C CA  . THR E 64  ? 0.659 1.068 0.639 0.036  0.041  0.046  393 THR EEE CA  
4919 C C   . THR E 64  ? 0.671 1.081 0.614 0.034  0.033  0.052  393 THR EEE C   
4920 O O   . THR E 64  ? 0.672 1.124 0.586 0.039  0.041  0.060  393 THR EEE O   
4921 C CB  . THR E 64  ? 0.698 1.105 0.705 0.045  0.043  0.006  393 THR EEE CB  
4922 O OG1 . THR E 64  ? 0.780 1.141 0.803 0.041  0.031  0.001  393 THR EEE OG1 
4923 C CG2 . THR E 64  ? 0.721 1.138 0.766 0.049  0.054  0.002  393 THR EEE CG2 
4924 N N   . ASN E 65  ? 0.685 1.053 0.630 0.029  0.019  0.052  394 ASN EEE N   
4925 C CA  . ASN E 65  ? 0.683 1.047 0.600 0.027  0.008  0.057  394 ASN EEE CA  
4926 C C   . ASN E 65  ? 0.665 0.981 0.590 0.018  -0.004 0.074  394 ASN EEE C   
4927 O O   . ASN E 65  ? 0.698 0.985 0.647 0.015  -0.007 0.068  394 ASN EEE O   
4928 C CB  . ASN E 65  ? 0.699 1.077 0.611 0.035  0.004  0.019  394 ASN EEE CB  
4929 C CG  . ASN E 65  ? 0.731 1.168 0.627 0.046  0.013  -0.003 394 ASN EEE CG  
4930 O OD1 . ASN E 65  ? 0.756 1.232 0.618 0.051  0.017  0.016  394 ASN EEE OD1 
4931 N ND2 . ASN E 65  ? 0.736 1.183 0.658 0.051  0.018  -0.043 394 ASN EEE ND2 
4932 N N   . VAL E 66  ? 0.649 0.959 0.556 0.015  -0.009 0.095  395 VAL EEE N   
4933 C CA  . VAL E 66  ? 0.622 0.894 0.532 0.008  -0.021 0.103  395 VAL EEE CA  
4934 C C   . VAL E 66  ? 0.633 0.912 0.524 0.013  -0.029 0.092  395 VAL EEE C   
4935 O O   . VAL E 66  ? 0.656 0.970 0.525 0.020  -0.027 0.097  395 VAL EEE O   
4936 C CB  . VAL E 66  ? 0.641 0.899 0.558 -0.000 -0.022 0.133  395 VAL EEE CB  
4937 C CG1 . VAL E 66  ? 0.637 0.862 0.557 -0.005 -0.033 0.135  395 VAL EEE CG1 
4938 C CG2 . VAL E 66  ? 0.631 0.887 0.573 -0.006 -0.016 0.139  395 VAL EEE CG2 
4939 N N   . TYR E 67  ? 0.606 0.858 0.505 0.010  -0.037 0.079  396 TYR EEE N   
4940 C CA  . TYR E 67  ? 0.578 0.835 0.468 0.013  -0.046 0.065  396 TYR EEE CA  
4941 C C   . TYR E 67  ? 0.566 0.794 0.457 0.008  -0.054 0.082  396 TYR EEE C   
4942 O O   . TYR E 67  ? 0.565 0.764 0.470 0.002  -0.054 0.085  396 TYR EEE O   
4943 C CB  . TYR E 67  ? 0.560 0.813 0.471 0.014  -0.046 0.032  396 TYR EEE CB  
4944 C CG  . TYR E 67  ? 0.575 0.858 0.493 0.020  -0.039 0.006  396 TYR EEE CG  
4945 C CD1 . TYR E 67  ? 0.603 0.930 0.506 0.028  -0.041 -0.017 396 TYR EEE CD1 
4946 C CD2 . TYR E 67  ? 0.575 0.846 0.516 0.019  -0.030 0.003  396 TYR EEE CD2 
4947 C CE1 . TYR E 67  ? 0.617 0.977 0.528 0.034  -0.034 -0.048 396 TYR EEE CE1 
4948 C CE2 . TYR E 67  ? 0.598 0.897 0.553 0.026  -0.022 -0.024 396 TYR EEE CE2 
4949 C CZ  . TYR E 67  ? 0.620 0.963 0.559 0.033  -0.024 -0.052 396 TYR EEE CZ  
4950 O OH  . TYR E 67  ? 0.640 1.016 0.593 0.040  -0.015 -0.086 396 TYR EEE OH  
4951 N N   . ALA E 68  ? 0.564 0.806 0.441 0.013  -0.059 0.093  397 ALA EEE N   
4952 C CA  . ALA E 68  ? 0.555 0.774 0.436 0.010  -0.067 0.105  397 ALA EEE CA  
4953 C C   . ALA E 68  ? 0.552 0.782 0.432 0.015  -0.075 0.085  397 ALA EEE C   
4954 O O   . ALA E 68  ? 0.587 0.853 0.451 0.024  -0.079 0.083  397 ALA EEE O   
4955 C CB  . ALA E 68  ? 0.573 0.798 0.450 0.013  -0.065 0.136  397 ALA EEE CB  
4956 N N   . ASP E 69  ? 0.527 0.732 0.423 0.009  -0.077 0.070  398 ASP EEE N   
4957 C CA  . ASP E 69  ? 0.498 0.708 0.404 0.011  -0.084 0.052  398 ASP EEE CA  
4958 C C   . ASP E 69  ? 0.491 0.684 0.399 0.011  -0.088 0.068  398 ASP EEE C   
4959 O O   . ASP E 69  ? 0.501 0.667 0.414 0.006  -0.085 0.079  398 ASP EEE O   
4960 C CB  . ASP E 69  ? 0.483 0.677 0.413 0.005  -0.078 0.032  398 ASP EEE CB  
4961 C CG  . ASP E 69  ? 0.482 0.686 0.422 0.005  -0.072 0.014  398 ASP EEE CG  
4962 O OD1 . ASP E 69  ? 0.490 0.725 0.413 0.011  -0.074 0.008  398 ASP EEE OD1 
4963 O OD2 . ASP E 69  ? 0.474 0.659 0.439 0.001  -0.065 0.009  398 ASP EEE OD2 
4964 N N   . SER E 70  ? 0.489 0.703 0.394 0.018  -0.097 0.068  399 SER EEE N   
4965 C CA  . SER E 70  ? 0.493 0.695 0.406 0.022  -0.102 0.083  399 SER EEE CA  
4966 C C   . SER E 70  ? 0.502 0.717 0.429 0.025  -0.110 0.064  399 SER EEE C   
4967 O O   . SER E 70  ? 0.504 0.751 0.429 0.028  -0.115 0.045  399 SER EEE O   
4968 C CB  . SER E 70  ? 0.508 0.723 0.411 0.031  -0.105 0.112  399 SER EEE CB  
4969 O OG  . SER E 70  ? 0.521 0.782 0.406 0.041  -0.110 0.112  399 SER EEE OG  
4970 N N   . PHE E 71  ? 0.511 0.706 0.455 0.023  -0.110 0.066  400 PHE EEE N   
4971 C CA  . PHE E 71  ? 0.508 0.714 0.472 0.025  -0.115 0.050  400 PHE EEE CA  
4972 C C   . PHE E 71  ? 0.500 0.681 0.479 0.025  -0.112 0.057  400 PHE EEE C   
4973 O O   . PHE E 71  ? 0.500 0.657 0.475 0.022  -0.106 0.068  400 PHE EEE O   
4974 C CB  . PHE E 71  ? 0.502 0.710 0.480 0.017  -0.110 0.025  400 PHE EEE CB  
4975 C CG  . PHE E 71  ? 0.511 0.689 0.491 0.007  -0.096 0.027  400 PHE EEE CG  
4976 C CD1 . PHE E 71  ? 0.508 0.668 0.498 0.004  -0.089 0.032  400 PHE EEE CD1 
4977 C CD2 . PHE E 71  ? 0.518 0.695 0.491 0.004  -0.091 0.025  400 PHE EEE CD2 
4978 C CE1 . PHE E 71  ? 0.505 0.648 0.493 -0.002 -0.078 0.037  400 PHE EEE CE1 
4979 C CE2 . PHE E 71  ? 0.506 0.660 0.483 -0.003 -0.080 0.031  400 PHE EEE CE2 
4980 C CZ  . PHE E 71  ? 0.500 0.639 0.482 -0.005 -0.074 0.038  400 PHE EEE CZ  
4981 N N   . VAL E 72  ? 0.524 0.717 0.524 0.029  -0.116 0.047  401 VAL EEE N   
4982 C CA  . VAL E 72  ? 0.525 0.701 0.544 0.030  -0.112 0.046  401 VAL EEE CA  
4983 C C   . VAL E 72  ? 0.509 0.687 0.545 0.022  -0.103 0.027  401 VAL EEE C   
4984 O O   . VAL E 72  ? 0.515 0.714 0.564 0.020  -0.106 0.014  401 VAL EEE O   
4985 C CB  . VAL E 72  ? 0.538 0.729 0.574 0.043  -0.123 0.055  401 VAL EEE CB  
4986 C CG1 . VAL E 72  ? 0.559 0.746 0.624 0.045  -0.119 0.044  401 VAL EEE CG1 
4987 C CG2 . VAL E 72  ? 0.555 0.734 0.586 0.051  -0.125 0.082  401 VAL EEE CG2 
4988 N N   . ILE E 73  ? 0.508 0.669 0.546 0.018  -0.092 0.027  402 ILE EEE N   
4989 C CA  . ILE E 73  ? 0.503 0.669 0.558 0.013  -0.079 0.016  402 ILE EEE CA  
4990 C C   . ILE E 73  ? 0.515 0.677 0.578 0.019  -0.074 0.013  402 ILE EEE C   
4991 O O   . ILE E 73  ? 0.531 0.681 0.590 0.024  -0.082 0.018  402 ILE EEE O   
4992 C CB  . ILE E 73  ? 0.485 0.643 0.530 0.005  -0.067 0.020  402 ILE EEE CB  
4993 C CG1 . ILE E 73  ? 0.486 0.629 0.503 0.004  -0.066 0.030  402 ILE EEE CG1 
4994 C CG2 . ILE E 73  ? 0.478 0.641 0.529 -0.000 -0.069 0.016  402 ILE EEE CG2 
4995 C CD1 . ILE E 73  ? 0.493 0.633 0.501 -0.001 -0.055 0.038  402 ILE EEE CD1 
4996 N N   . ARG E 74  ? 0.534 0.706 0.611 0.017  -0.062 0.005  403 ARG EEE N   
4997 C CA  . ARG E 74  ? 0.571 0.747 0.654 0.023  -0.055 -0.003 403 ARG EEE CA  
4998 C C   . ARG E 74  ? 0.578 0.752 0.635 0.019  -0.046 -0.002 403 ARG EEE C   
4999 O O   . ARG E 74  ? 0.544 0.716 0.585 0.013  -0.041 0.010  403 ARG EEE O   
5000 C CB  . ARG E 74  ? 0.592 0.790 0.705 0.025  -0.045 -0.013 403 ARG EEE CB  
5001 C CG  . ARG E 74  ? 0.616 0.828 0.735 0.017  -0.028 -0.008 403 ARG EEE CG  
5002 C CD  . ARG E 74  ? 0.649 0.884 0.806 0.019  -0.019 -0.017 403 ARG EEE CD  
5003 N NE  . ARG E 74  ? 0.695 0.945 0.864 0.012  0.004  -0.008 403 ARG EEE NE  
5004 C CZ  . ARG E 74  ? 0.773 1.039 0.927 0.014  0.022  -0.002 403 ARG EEE CZ  
5005 N NH1 . ARG E 74  ? 0.813 1.083 0.943 0.023  0.020  -0.013 403 ARG EEE NH1 
5006 N NH2 . ARG E 74  ? 0.783 1.066 0.952 0.009  0.045  0.014  403 ARG EEE NH2 
5007 N N   . GLY E 75  ? 0.608 0.784 0.664 0.025  -0.044 -0.015 404 GLY EEE N   
5008 C CA  . GLY E 75  ? 0.630 0.811 0.661 0.024  -0.040 -0.020 404 GLY EEE CA  
5009 C C   . GLY E 75  ? 0.634 0.836 0.644 0.021  -0.025 -0.009 404 GLY EEE C   
5010 O O   . GLY E 75  ? 0.674 0.875 0.660 0.018  -0.027 0.001  404 GLY EEE O   
5011 N N   . ASP E 76  ? 0.630 0.853 0.653 0.023  -0.011 -0.007 405 ASP EEE N   
5012 C CA  . ASP E 76  ? 0.638 0.886 0.649 0.022  0.008  0.011  405 ASP EEE CA  
5013 C C   . ASP E 76  ? 0.607 0.839 0.617 0.014  0.008  0.036  405 ASP EEE C   
5014 O O   . ASP E 76  ? 0.643 0.890 0.640 0.015  0.022  0.057  405 ASP EEE O   
5015 C CB  . ASP E 76  ? 0.660 0.931 0.698 0.023  0.025  0.012  405 ASP EEE CB  
5016 C CG  . ASP E 76  ? 0.702 1.003 0.738 0.033  0.033  -0.010 405 ASP EEE CG  
5017 O OD1 . ASP E 76  ? 0.752 1.064 0.763 0.038  0.028  -0.026 405 ASP EEE OD1 
5018 O OD2 . ASP E 76  ? 0.731 1.049 0.796 0.034  0.045  -0.014 405 ASP EEE OD2 
5019 N N   . GLU E 77  ? 0.551 0.756 0.573 0.009  -0.005 0.034  406 GLU EEE N   
5020 C CA  . GLU E 77  ? 0.538 0.728 0.568 0.002  -0.005 0.050  406 GLU EEE CA  
5021 C C   . GLU E 77  ? 0.530 0.705 0.533 0.002  -0.016 0.054  406 GLU EEE C   
5022 O O   . GLU E 77  ? 0.527 0.692 0.536 -0.002 -0.015 0.066  406 GLU EEE O   
5023 C CB  . GLU E 77  ? 0.525 0.706 0.586 -0.002 -0.013 0.039  406 GLU EEE CB  
5024 C CG  . GLU E 77  ? 0.516 0.713 0.615 -0.004 -0.001 0.036  406 GLU EEE CG  
5025 C CD  . GLU E 77  ? 0.499 0.697 0.628 -0.006 -0.013 0.019  406 GLU EEE CD  
5026 O OE1 . GLU E 77  ? 0.473 0.663 0.588 -0.003 -0.032 0.011  406 GLU EEE OE1 
5027 O OE2 . GLU E 77  ? 0.500 0.711 0.670 -0.011 -0.004 0.015  406 GLU EEE OE2 
5028 N N   . VAL E 78  ? 0.539 0.714 0.522 0.005  -0.026 0.044  407 VAL EEE N   
5029 C CA  . VAL E 78  ? 0.553 0.715 0.516 0.004  -0.037 0.047  407 VAL EEE CA  
5030 C C   . VAL E 78  ? 0.558 0.733 0.506 0.005  -0.028 0.064  407 VAL EEE C   
5031 O O   . VAL E 78  ? 0.572 0.736 0.514 0.003  -0.034 0.072  407 VAL EEE O   
5032 C CB  . VAL E 78  ? 0.559 0.719 0.515 0.007  -0.047 0.030  407 VAL EEE CB  
5033 C CG1 . VAL E 78  ? 0.551 0.706 0.493 0.004  -0.055 0.033  407 VAL EEE CG1 
5034 C CG2 . VAL E 78  ? 0.560 0.705 0.537 0.008  -0.056 0.021  407 VAL EEE CG2 
5035 N N   . ARG E 79  ? 0.579 0.780 0.522 0.010  -0.015 0.073  408 ARG EEE N   
5036 C CA  . ARG E 79  ? 0.612 0.832 0.541 0.014  -0.005 0.098  408 ARG EEE CA  
5037 C C   . ARG E 79  ? 0.597 0.798 0.553 0.010  0.004  0.120  408 ARG EEE C   
5038 O O   . ARG E 79  ? 0.644 0.849 0.596 0.013  0.008  0.142  408 ARG EEE O   
5039 C CB  . ARG E 79  ? 0.672 0.933 0.587 0.023  0.008  0.104  408 ARG EEE CB  
5040 C CG  . ARG E 79  ? 0.720 0.987 0.660 0.022  0.027  0.114  408 ARG EEE CG  
5041 C CD  . ARG E 79  ? 0.786 1.063 0.741 0.024  0.047  0.154  408 ARG EEE CD  
5042 N NE  . ARG E 79  ? 0.831 1.104 0.828 0.018  0.064  0.162  408 ARG EEE NE  
5043 C CZ  . ARG E 79  ? 0.852 1.114 0.889 0.014  0.081  0.191  408 ARG EEE CZ  
5044 N NH1 . ARG E 79  ? 0.875 1.127 0.916 0.017  0.083  0.216  408 ARG EEE NH1 
5045 N NH2 . ARG E 79  ? 0.858 1.118 0.940 0.008  0.096  0.192  408 ARG EEE NH2 
5046 N N   . GLN E 80  ? 0.538 0.880 0.388 0.065  -0.032 0.040  409 GLN EEE N   
5047 C CA  . GLN E 80  ? 0.521 0.861 0.379 0.062  -0.025 0.051  409 GLN EEE CA  
5048 C C   . GLN E 80  ? 0.481 0.823 0.367 0.064  -0.028 0.051  409 GLN EEE C   
5049 O O   . GLN E 80  ? 0.469 0.808 0.364 0.065  -0.027 0.056  409 GLN EEE O   
5050 C CB  . GLN E 80  ? 0.520 0.865 0.379 0.059  -0.011 0.050  409 GLN EEE CB  
5051 C CG  . GLN E 80  ? 0.535 0.884 0.371 0.056  -0.004 0.053  409 GLN EEE CG  
5052 C CD  . GLN E 80  ? 0.535 0.891 0.378 0.051  0.009  0.054  409 GLN EEE CD  
5053 O OE1 . GLN E 80  ? 0.522 0.873 0.382 0.047  0.010  0.057  409 GLN EEE OE1 
5054 N NE2 . GLN E 80  ? 0.558 0.930 0.393 0.051  0.017  0.049  409 GLN EEE NE2 
5055 N N   . ILE E 81  ? 0.463 0.812 0.365 0.063  -0.032 0.046  410 ILE EEE N   
5056 C CA  . ILE E 81  ? 0.442 0.804 0.372 0.063  -0.032 0.048  410 ILE EEE CA  
5057 C C   . ILE E 81  ? 0.466 0.829 0.405 0.065  -0.046 0.050  410 ILE EEE C   
5058 O O   . ILE E 81  ? 0.463 0.834 0.417 0.062  -0.055 0.049  410 ILE EEE O   
5059 C CB  . ILE E 81  ? 0.433 0.803 0.376 0.057  -0.030 0.047  410 ILE EEE CB  
5060 C CG1 . ILE E 81  ? 0.425 0.791 0.357 0.056  -0.021 0.044  410 ILE EEE CG1 
5061 C CG2 . ILE E 81  ? 0.429 0.820 0.397 0.056  -0.026 0.051  410 ILE EEE CG2 
5062 C CD1 . ILE E 81  ? 0.406 0.775 0.333 0.058  -0.010 0.044  410 ILE EEE CD1 
5063 N N   . ALA E 82  ? 0.469 0.826 0.403 0.071  -0.050 0.054  411 ALA EEE N   
5064 C CA  . ALA E 82  ? 0.501 0.859 0.443 0.076  -0.066 0.058  411 ALA EEE CA  
5065 C C   . ALA E 82  ? 0.515 0.863 0.458 0.083  -0.067 0.064  411 ALA EEE C   
5066 O O   . ALA E 82  ? 0.521 0.856 0.450 0.081  -0.058 0.066  411 ALA EEE O   
5067 C CB  . ALA E 82  ? 0.514 0.864 0.431 0.074  -0.079 0.057  411 ALA EEE CB  
5068 N N   . PRO E 83  ? 0.512 0.865 0.475 0.091  -0.080 0.067  412 PRO EEE N   
5069 C CA  . PRO E 83  ? 0.532 0.870 0.501 0.100  -0.086 0.073  412 PRO EEE CA  
5070 C C   . PRO E 83  ? 0.559 0.872 0.493 0.096  -0.091 0.087  412 PRO EEE C   
5071 O O   . PRO E 83  ? 0.597 0.909 0.505 0.091  -0.099 0.091  412 PRO EEE O   
5072 C CB  . PRO E 83  ? 0.535 0.886 0.533 0.110  -0.103 0.074  412 PRO EEE CB  
5073 C CG  . PRO E 83  ? 0.514 0.893 0.529 0.104  -0.102 0.067  412 PRO EEE CG  
5074 C CD  . PRO E 83  ? 0.513 0.885 0.498 0.092  -0.093 0.065  412 PRO EEE CD  
5075 N N   . GLY E 84  ? 0.564 0.858 0.498 0.096  -0.088 0.092  413 GLY EEE N   
5076 C CA  . GLY E 84  ? 0.595 0.864 0.502 0.091  -0.094 0.111  413 GLY EEE CA  
5077 C C   . GLY E 84  ? 0.593 0.865 0.465 0.078  -0.081 0.115  413 GLY EEE C   
5078 O O   . GLY E 84  ? 0.622 0.886 0.466 0.072  -0.086 0.132  413 GLY EEE O   
5079 N N   . GLN E 85  ? 0.561 0.848 0.435 0.074  -0.065 0.100  414 GLN EEE N   
5080 C CA  . GLN E 85  ? 0.565 0.859 0.413 0.064  -0.052 0.100  414 GLN EEE CA  
5081 C C   . GLN E 85  ? 0.562 0.848 0.417 0.057  -0.040 0.103  414 GLN EEE C   
5082 O O   . GLN E 85  ? 0.540 0.816 0.419 0.061  -0.041 0.098  414 GLN EEE O   
5083 C CB  . GLN E 85  ? 0.545 0.857 0.397 0.065  -0.045 0.083  414 GLN EEE CB  
5084 C CG  . GLN E 85  ? 0.563 0.882 0.414 0.070  -0.059 0.078  414 GLN EEE CG  
5085 C CD  . GLN E 85  ? 0.615 0.933 0.430 0.069  -0.067 0.086  414 GLN EEE CD  
5086 O OE1 . GLN E 85  ? 0.650 0.974 0.439 0.065  -0.057 0.084  414 GLN EEE OE1 
5087 N NE2 . GLN E 85  ? 0.659 0.972 0.473 0.073  -0.085 0.093  414 GLN EEE NE2 
5088 N N   . THR E 86  ? 0.581 0.873 0.414 0.047  -0.030 0.110  415 THR EEE N   
5089 C CA  . THR E 86  ? 0.569 0.860 0.409 0.037  -0.018 0.113  415 THR EEE CA  
5090 C C   . THR E 86  ? 0.554 0.869 0.384 0.034  -0.004 0.103  415 THR EEE C   
5091 O O   . THR E 86  ? 0.555 0.883 0.369 0.040  -0.004 0.095  415 THR EEE O   
5092 C CB  . THR E 86  ? 0.599 0.874 0.430 0.027  -0.022 0.138  415 THR EEE CB  
5093 O OG1 . THR E 86  ? 0.605 0.896 0.402 0.022  -0.019 0.150  415 THR EEE OG1 
5094 C CG2 . THR E 86  ? 0.613 0.860 0.456 0.033  -0.041 0.147  415 THR EEE CG2 
5095 N N   . GLY E 87  ? 0.550 0.871 0.391 0.026  0.007  0.102  416 GLY EEE N   
5096 C CA  . GLY E 87  ? 0.528 0.873 0.369 0.026  0.019  0.090  416 GLY EEE CA  
5097 C C   . GLY E 87  ? 0.511 0.856 0.378 0.026  0.021  0.079  416 GLY EEE C   
5098 O O   . GLY E 87  ? 0.525 0.852 0.404 0.028  0.014  0.076  416 GLY EEE O   
5099 N N   . LYS E 88  ? 0.522 0.887 0.394 0.025  0.030  0.070  417 LYS EEE N   
5100 C CA  . LYS E 88  ? 0.520 0.888 0.412 0.024  0.031  0.061  417 LYS EEE CA  
5101 C C   . LYS E 88  ? 0.499 0.858 0.397 0.033  0.023  0.051  417 LYS EEE C   
5102 O O   . LYS E 88  ? 0.523 0.877 0.433 0.032  0.021  0.046  417 LYS EEE O   
5103 C CB  . LYS E 88  ? 0.528 0.921 0.426 0.025  0.038  0.053  417 LYS EEE CB  
5104 C CG  . LYS E 88  ? 0.578 0.992 0.478 0.015  0.048  0.061  417 LYS EEE CG  
5105 C CD  . LYS E 88  ? 0.609 1.017 0.525 0.000  0.048  0.069  417 LYS EEE CD  
5106 C CE  . LYS E 88  ? 0.635 1.062 0.552 -0.014 0.057  0.085  417 LYS EEE CE  
5107 N NZ  . LYS E 88  ? 0.661 1.084 0.603 -0.030 0.054  0.092  417 LYS EEE NZ  
5108 N N   . ILE E 89  ? 0.464 0.824 0.355 0.041  0.020  0.049  418 ILE EEE N   
5109 C CA  . ILE E 89  ? 0.449 0.808 0.348 0.047  0.016  0.043  418 ILE EEE CA  
5110 C C   . ILE E 89  ? 0.451 0.798 0.355 0.049  0.010  0.044  418 ILE EEE C   
5111 O O   . ILE E 89  ? 0.450 0.799 0.365 0.052  0.011  0.038  418 ILE EEE O   
5112 C CB  . ILE E 89  ? 0.437 0.799 0.331 0.052  0.012  0.041  418 ILE EEE CB  
5113 C CG1 . ILE E 89  ? 0.438 0.810 0.329 0.053  0.016  0.036  418 ILE EEE CG1 
5114 C CG2 . ILE E 89  ? 0.430 0.796 0.336 0.054  0.008  0.039  418 ILE EEE CG2 
5115 C CD1 . ILE E 89  ? 0.425 0.807 0.328 0.051  0.019  0.033  418 ILE EEE CD1 
5116 N N   . ALA E 90  ? 0.445 0.781 0.341 0.051  0.005  0.052  419 ALA EEE N   
5117 C CA  . ALA E 90  ? 0.458 0.781 0.363 0.056  -0.003 0.054  419 ALA EEE CA  
5118 C C   . ALA E 90  ? 0.465 0.776 0.381 0.053  -0.004 0.053  419 ALA EEE C   
5119 O O   . ALA E 90  ? 0.448 0.755 0.379 0.061  -0.008 0.044  419 ALA EEE O   
5120 C CB  . ALA E 90  ? 0.483 0.797 0.375 0.056  -0.011 0.066  419 ALA EEE CB  
5121 N N   . ASP E 91  ? 0.470 0.775 0.380 0.043  -0.000 0.059  420 ASP EEE N   
5122 C CA  . ASP E 91  ? 0.510 0.797 0.432 0.038  -0.004 0.059  420 ASP EEE CA  
5123 C C   . ASP E 91  ? 0.512 0.808 0.446 0.039  -0.002 0.041  420 ASP EEE C   
5124 O O   . ASP E 91  ? 0.529 0.810 0.475 0.044  -0.009 0.031  420 ASP EEE O   
5125 C CB  . ASP E 91  ? 0.536 0.822 0.452 0.023  -0.001 0.075  420 ASP EEE CB  
5126 C CG  . ASP E 91  ? 0.569 0.845 0.468 0.019  -0.004 0.095  420 ASP EEE CG  
5127 O OD1 . ASP E 91  ? 0.578 0.845 0.474 0.029  -0.013 0.097  420 ASP EEE OD1 
5128 O OD2 . ASP E 91  ? 0.607 0.891 0.498 0.006  0.002  0.110  420 ASP EEE OD2 
5129 N N   . TYR E 92  ? 0.500 0.818 0.429 0.037  0.006  0.037  421 TYR EEE N   
5130 C CA  . TYR E 92  ? 0.498 0.826 0.433 0.035  0.008  0.024  421 TYR EEE CA  
5131 C C   . TYR E 92  ? 0.501 0.850 0.432 0.043  0.011  0.015  421 TYR EEE C   
5132 O O   . TYR E 92  ? 0.501 0.859 0.434 0.043  0.010  0.004  421 TYR EEE O   
5133 C CB  . TYR E 92  ? 0.476 0.815 0.414 0.023  0.012  0.029  421 TYR EEE CB  
5134 C CG  . TYR E 92  ? 0.485 0.810 0.429 0.010  0.010  0.042  421 TYR EEE CG  
5135 C CD1 . TYR E 92  ? 0.500 0.796 0.452 0.009  0.001  0.045  421 TYR EEE CD1 
5136 C CD2 . TYR E 92  ? 0.478 0.820 0.423 0.000  0.018  0.052  421 TYR EEE CD2 
5137 C CE1 . TYR E 92  ? 0.517 0.799 0.475 -0.006 -0.002 0.062  421 TYR EEE CE1 
5138 C CE2 . TYR E 92  ? 0.486 0.822 0.437 -0.015 0.018  0.068  421 TYR EEE CE2 
5139 C CZ  . TYR E 92  ? 0.509 0.813 0.466 -0.019 0.008  0.075  421 TYR EEE CZ  
5140 O OH  . TYR E 92  ? 0.524 0.819 0.488 -0.036 0.007  0.096  421 TYR EEE OH  
5141 N N   . ASN E 93  ? 0.483 0.840 0.409 0.048  0.013  0.020  422 ASN EEE N   
5142 C CA  . ASN E 93  ? 0.464 0.841 0.387 0.052  0.017  0.018  422 ASN EEE CA  
5143 C C   . ASN E 93  ? 0.466 0.851 0.394 0.059  0.017  0.016  422 ASN EEE C   
5144 O O   . ASN E 93  ? 0.482 0.882 0.410 0.063  0.020  0.009  422 ASN EEE O   
5145 C CB  . ASN E 93  ? 0.443 0.826 0.362 0.049  0.018  0.026  422 ASN EEE CB  
5146 C CG  . ASN E 93  ? 0.448 0.835 0.368 0.043  0.019  0.025  422 ASN EEE CG  
5147 O OD1 . ASN E 93  ? 0.403 0.803 0.325 0.043  0.018  0.022  422 ASN EEE OD1 
5148 N ND2 . ASN E 93  ? 0.457 0.837 0.377 0.039  0.021  0.028  422 ASN EEE ND2 
5149 N N   . TYR E 94  ? 0.455 0.833 0.385 0.061  0.014  0.024  423 TYR EEE N   
5150 C CA  . TYR E 94  ? 0.434 0.822 0.374 0.067  0.013  0.024  423 TYR EEE CA  
5151 C C   . TYR E 94  ? 0.434 0.806 0.379 0.070  0.006  0.028  423 TYR EEE C   
5152 O O   . TYR E 94  ? 0.456 0.817 0.391 0.066  0.002  0.036  423 TYR EEE O   
5153 C CB  . TYR E 94  ? 0.419 0.822 0.360 0.062  0.014  0.032  423 TYR EEE CB  
5154 C CG  . TYR E 94  ? 0.414 0.837 0.372 0.065  0.015  0.034  423 TYR EEE CG  
5155 C CD1 . TYR E 94  ? 0.419 0.868 0.382 0.067  0.023  0.031  423 TYR EEE CD1 
5156 C CD2 . TYR E 94  ? 0.412 0.829 0.378 0.066  0.007  0.039  423 TYR EEE CD2 
5157 C CE1 . TYR E 94  ? 0.415 0.890 0.397 0.069  0.025  0.034  423 TYR EEE CE1 
5158 C CE2 . TYR E 94  ? 0.418 0.858 0.405 0.068  0.007  0.041  423 TYR EEE CE2 
5159 C CZ  . TYR E 94  ? 0.424 0.894 0.421 0.069  0.017  0.039  423 TYR EEE CZ  
5160 O OH  . TYR E 94  ? 0.401 0.901 0.422 0.069  0.019  0.043  423 TYR EEE OH  
5161 N N   . LYS E 95  ? 0.418 0.788 0.376 0.079  0.003  0.021  424 LYS EEE N   
5162 C CA  . LYS E 95  ? 0.440 0.793 0.405 0.085  -0.007 0.025  424 LYS EEE CA  
5163 C C   . LYS E 95  ? 0.434 0.806 0.419 0.094  -0.010 0.023  424 LYS EEE C   
5164 O O   . LYS E 95  ? 0.425 0.815 0.426 0.103  -0.005 0.010  424 LYS EEE O   
5165 C CB  . LYS E 95  ? 0.471 0.801 0.440 0.089  -0.012 0.019  424 LYS EEE CB  
5166 C CG  . LYS E 95  ? 0.497 0.804 0.476 0.095  -0.025 0.026  424 LYS EEE CG  
5167 C CD  . LYS E 95  ? 0.513 0.809 0.474 0.087  -0.031 0.045  424 LYS EEE CD  
5168 C CE  . LYS E 95  ? 0.548 0.818 0.513 0.091  -0.047 0.057  424 LYS EEE CE  
5169 N NZ  . LYS E 95  ? 0.579 0.845 0.520 0.083  -0.051 0.076  424 LYS EEE NZ  
5170 N N   . LEU E 96  ? 0.440 0.813 0.427 0.093  -0.018 0.033  425 LEU EEE N   
5171 C CA  . LEU E 96  ? 0.465 0.856 0.477 0.101  -0.025 0.032  425 LEU EEE CA  
5172 C C   . LEU E 96  ? 0.488 0.858 0.510 0.113  -0.037 0.031  425 LEU EEE C   
5173 O O   . LEU E 96  ? 0.522 0.862 0.526 0.110  -0.043 0.039  425 LEU EEE O   
5174 C CB  . LEU E 96  ? 0.458 0.852 0.467 0.094  -0.034 0.042  425 LEU EEE CB  
5175 C CG  . LEU E 96  ? 0.453 0.865 0.461 0.083  -0.027 0.044  425 LEU EEE CG  
5176 C CD1 . LEU E 96  ? 0.459 0.873 0.473 0.078  -0.040 0.050  425 LEU EEE CD1 
5177 C CD2 . LEU E 96  ? 0.457 0.903 0.487 0.085  -0.014 0.040  425 LEU EEE CD2 
5178 N N   . PRO E 97  ? 0.503 0.891 0.556 0.127  -0.040 0.023  426 PRO EEE N   
5179 C CA  . PRO E 97  ? 0.528 0.895 0.596 0.141  -0.055 0.022  426 PRO EEE CA  
5180 C C   . PRO E 97  ? 0.545 0.901 0.608 0.139  -0.073 0.040  426 PRO EEE C   
5181 O O   . PRO E 97  ? 0.499 0.874 0.560 0.132  -0.074 0.045  426 PRO EEE O   
5182 C CB  . PRO E 97  ? 0.525 0.925 0.630 0.159  -0.051 0.005  426 PRO EEE CB  
5183 C CG  . PRO E 97  ? 0.502 0.947 0.614 0.150  -0.038 0.005  426 PRO EEE CG  
5184 C CD  . PRO E 97  ? 0.497 0.929 0.573 0.131  -0.029 0.013  426 PRO EEE CD  
5185 N N   . ASP E 98  ? 0.584 0.907 0.645 0.145  -0.089 0.049  427 ASP EEE N   
5186 C CA  . ASP E 98  ? 0.628 0.940 0.682 0.145  -0.110 0.066  427 ASP EEE CA  
5187 C C   . ASP E 98  ? 0.622 0.970 0.707 0.154  -0.117 0.061  427 ASP EEE C   
5188 O O   . ASP E 98  ? 0.618 0.971 0.691 0.147  -0.128 0.072  427 ASP EEE O   
5189 C CB  . ASP E 98  ? 0.677 0.950 0.732 0.153  -0.128 0.078  427 ASP EEE CB  
5190 C CG  . ASP E 98  ? 0.695 0.934 0.719 0.140  -0.123 0.090  427 ASP EEE CG  
5191 O OD1 . ASP E 98  ? 0.702 0.949 0.701 0.125  -0.107 0.090  427 ASP EEE OD1 
5192 O OD2 . ASP E 98  ? 0.739 0.944 0.769 0.144  -0.137 0.100  427 ASP EEE OD2 
5193 N N   . ASP E 99  ? 0.624 0.999 0.748 0.168  -0.111 0.045  428 ASP EEE N   
5194 C CA  . ASP E 99  ? 0.617 1.033 0.782 0.178  -0.116 0.039  428 ASP EEE CA  
5195 C C   . ASP E 99  ? 0.560 1.019 0.734 0.167  -0.096 0.032  428 ASP EEE C   
5196 O O   . ASP E 99  ? 0.569 1.072 0.784 0.175  -0.092 0.023  428 ASP EEE O   
5197 C CB  . ASP E 99  ? 0.648 1.071 0.856 0.203  -0.124 0.026  428 ASP EEE CB  
5198 C CG  . ASP E 99  ? 0.667 1.102 0.887 0.212  -0.103 0.003  428 ASP EEE CG  
5199 O OD1 . ASP E 99  ? 0.652 1.081 0.842 0.199  -0.086 0.001  428 ASP EEE OD1 
5200 O OD2 . ASP E 99  ? 0.689 1.141 0.948 0.235  -0.106 -0.013 428 ASP EEE OD2 
5201 N N   . PHE E 100 ? 0.526 0.976 0.666 0.148  -0.085 0.037  429 PHE EEE N   
5202 C CA  . PHE E 100 ? 0.503 0.986 0.648 0.135  -0.068 0.035  429 PHE EEE CA  
5203 C C   . PHE E 100 ? 0.516 1.035 0.695 0.132  -0.076 0.039  429 PHE EEE C   
5204 O O   . PHE E 100 ? 0.542 1.049 0.717 0.128  -0.096 0.047  429 PHE EEE O   
5205 C CB  . PHE E 100 ? 0.472 0.932 0.577 0.118  -0.062 0.042  429 PHE EEE CB  
5206 C CG  . PHE E 100 ? 0.435 0.921 0.545 0.104  -0.050 0.044  429 PHE EEE CG  
5207 C CD1 . PHE E 100 ? 0.422 0.934 0.540 0.103  -0.031 0.038  429 PHE EEE CD1 
5208 C CD2 . PHE E 100 ? 0.422 0.906 0.529 0.091  -0.061 0.052  429 PHE EEE CD2 
5209 C CE1 . PHE E 100 ? 0.397 0.931 0.519 0.088  -0.022 0.046  429 PHE EEE CE1 
5210 C CE2 . PHE E 100 ? 0.403 0.905 0.518 0.076  -0.053 0.056  429 PHE EEE CE2 
5211 C CZ  . PHE E 100 ? 0.395 0.922 0.518 0.074  -0.034 0.056  429 PHE EEE CZ  
5212 N N   . THR E 101 ? 0.529 1.095 0.740 0.132  -0.061 0.034  430 THR EEE N   
5213 C CA  . THR E 101 ? 0.513 1.124 0.763 0.123  -0.064 0.040  430 THR EEE CA  
5214 C C   . THR E 101 ? 0.496 1.121 0.737 0.102  -0.048 0.048  430 THR EEE C   
5215 O O   . THR E 101 ? 0.516 1.164 0.755 0.104  -0.026 0.043  430 THR EEE O   
5216 C CB  . THR E 101 ? 0.518 1.180 0.818 0.139  -0.058 0.030  430 THR EEE CB  
5217 O OG1 . THR E 101 ? 0.561 1.207 0.876 0.157  -0.080 0.027  430 THR EEE OG1 
5218 C CG2 . THR E 101 ? 0.503 1.223 0.846 0.126  -0.052 0.038  430 THR EEE CG2 
5219 N N   . GLY E 102 ? 0.466 1.079 0.701 0.084  -0.060 0.059  431 GLY EEE N   
5220 C CA  . GLY E 102 ? 0.438 1.060 0.670 0.063  -0.050 0.069  431 GLY EEE CA  
5221 C C   . GLY E 102 ? 0.438 1.019 0.646 0.050  -0.067 0.074  431 GLY EEE C   
5222 O O   . GLY E 102 ? 0.436 0.994 0.636 0.054  -0.087 0.070  431 GLY EEE O   
5223 N N   . CYS E 103 ? 0.431 1.004 0.626 0.035  -0.059 0.082  432 CYS EEE N   
5224 C CA  . CYS E 103 ? 0.435 0.970 0.611 0.023  -0.075 0.084  432 CYS EEE CA  
5225 C C   . CYS E 103 ? 0.433 0.939 0.569 0.024  -0.064 0.082  432 CYS EEE C   
5226 O O   . CYS E 103 ? 0.447 0.971 0.582 0.024  -0.045 0.086  432 CYS EEE O   
5227 C CB  . CYS E 103 ? 0.443 0.996 0.656 0.002  -0.083 0.097  432 CYS EEE CB  
5228 S SG  . CYS E 103 ? 0.456 1.049 0.723 -0.000 -0.099 0.098  432 CYS EEE SG  
5229 N N   . VAL E 104 ? 0.430 0.897 0.536 0.027  -0.075 0.074  433 VAL EEE N   
5230 C CA  . VAL E 104 ? 0.409 0.849 0.482 0.028  -0.067 0.071  433 VAL EEE CA  
5231 C C   . VAL E 104 ? 0.427 0.848 0.506 0.016  -0.082 0.073  433 VAL EEE C   
5232 O O   . VAL E 104 ? 0.458 0.863 0.536 0.016  -0.101 0.064  433 VAL EEE O   
5233 C CB  . VAL E 104 ? 0.410 0.826 0.447 0.040  -0.067 0.060  433 VAL EEE CB  
5234 C CG1 . VAL E 104 ? 0.415 0.810 0.426 0.040  -0.061 0.056  433 VAL EEE CG1 
5235 C CG2 . VAL E 104 ? 0.393 0.822 0.430 0.051  -0.056 0.059  433 VAL EEE CG2 
5236 N N   . ILE E 105 ? 0.425 0.848 0.511 0.006  -0.075 0.084  434 ILE EEE N   
5237 C CA  . ILE E 105 ? 0.443 0.844 0.541 -0.005 -0.091 0.088  434 ILE EEE CA  
5238 C C   . ILE E 105 ? 0.455 0.831 0.526 0.001  -0.086 0.083  434 ILE EEE C   
5239 O O   . ILE E 105 ? 0.436 0.825 0.497 0.003  -0.069 0.090  434 ILE EEE O   
5240 C CB  . ILE E 105 ? 0.443 0.870 0.579 -0.024 -0.090 0.111  434 ILE EEE CB  
5241 C CG1 . ILE E 105 ? 0.443 0.906 0.609 -0.029 -0.089 0.115  434 ILE EEE CG1 
5242 C CG2 . ILE E 105 ? 0.469 0.867 0.623 -0.038 -0.111 0.117  434 ILE EEE CG2 
5243 C CD1 . ILE E 105 ? 0.451 0.957 0.651 -0.045 -0.078 0.139  434 ILE EEE CD1 
5244 N N   . ALA E 106 ? 0.484 0.827 0.545 0.006  -0.102 0.069  435 ALA EEE N   
5245 C CA  . ALA E 106 ? 0.492 0.813 0.532 0.015  -0.100 0.060  435 ALA EEE CA  
5246 C C   . ALA E 106 ? 0.528 0.817 0.582 0.012  -0.123 0.052  435 ALA EEE C   
5247 O O   . ALA E 106 ? 0.546 0.825 0.610 0.009  -0.141 0.042  435 ALA EEE O   
5248 C CB  . ALA E 106 ? 0.497 0.817 0.503 0.030  -0.091 0.043  435 ALA EEE CB  
5249 N N   . TRP E 107 ? 0.554 0.826 0.608 0.015  -0.124 0.055  436 TRP EEE N   
5250 C CA  . TRP E 107 ? 0.598 0.834 0.666 0.017  -0.147 0.044  436 TRP EEE CA  
5251 C C   . TRP E 107 ? 0.601 0.826 0.654 0.032  -0.141 0.036  436 TRP EEE C   
5252 O O   . TRP E 107 ? 0.597 0.843 0.641 0.032  -0.123 0.049  436 TRP EEE O   
5253 C CB  . TRP E 107 ? 0.631 0.857 0.738 -0.004 -0.163 0.068  436 TRP EEE CB  
5254 C CG  . TRP E 107 ? 0.619 0.860 0.733 -0.014 -0.151 0.099  436 TRP EEE CG  
5255 C CD1 . TRP E 107 ? 0.634 0.854 0.757 -0.014 -0.159 0.111  436 TRP EEE CD1 
5256 C CD2 . TRP E 107 ? 0.589 0.872 0.702 -0.024 -0.129 0.121  436 TRP EEE CD2 
5257 N NE1 . TRP E 107 ? 0.634 0.880 0.756 -0.025 -0.145 0.141  436 TRP EEE NE1 
5258 C CE2 . TRP E 107 ? 0.605 0.891 0.721 -0.031 -0.125 0.146  436 TRP EEE CE2 
5259 C CE3 . TRP E 107 ? 0.563 0.880 0.671 -0.026 -0.114 0.121  436 TRP EEE CE3 
5260 C CZ2 . TRP E 107 ? 0.591 0.917 0.702 -0.040 -0.105 0.168  436 TRP EEE CZ2 
5261 C CZ3 . TRP E 107 ? 0.559 0.914 0.668 -0.033 -0.095 0.141  436 TRP EEE CZ3 
5262 C CH2 . TRP E 107 ? 0.568 0.930 0.676 -0.040 -0.089 0.164  436 TRP EEE CH2 
5263 N N   . ASN E 108 ? 0.639 0.836 0.692 0.045  -0.157 0.011  437 ASN EEE N   
5264 C CA  . ASN E 108 ? 0.641 0.828 0.689 0.062  -0.155 -0.001 437 ASN EEE CA  
5265 C C   . ASN E 108 ? 0.649 0.824 0.723 0.053  -0.163 0.026  437 ASN EEE C   
5266 O O   . ASN E 108 ? 0.685 0.837 0.787 0.040  -0.183 0.039  437 ASN EEE O   
5267 C CB  . ASN E 108 ? 0.681 0.842 0.729 0.079  -0.173 -0.036 437 ASN EEE CB  
5268 C CG  . ASN E 108 ? 0.694 0.854 0.738 0.101  -0.169 -0.054 437 ASN EEE CG  
5269 O OD1 . ASN E 108 ? 0.700 0.847 0.765 0.102  -0.176 -0.041 437 ASN EEE OD1 
5270 N ND2 . ASN E 108 ? 0.696 0.873 0.713 0.118  -0.158 -0.082 437 ASN EEE ND2 
5271 N N   . SER E 109 ? 0.637 0.830 0.702 0.059  -0.148 0.036  438 SER EEE N   
5272 C CA  . SER E 109 ? 0.633 0.820 0.714 0.051  -0.154 0.064  438 SER EEE CA  
5273 C C   . SER E 109 ? 0.644 0.818 0.731 0.071  -0.161 0.052  438 SER EEE C   
5274 O O   . SER E 109 ? 0.653 0.833 0.744 0.069  -0.161 0.073  438 SER EEE O   
5275 C CB  . SER E 109 ? 0.595 0.820 0.661 0.040  -0.132 0.087  438 SER EEE CB  
5276 O OG  . SER E 109 ? 0.575 0.823 0.616 0.052  -0.112 0.072  438 SER EEE OG  
5277 N N   . ASN E 110 ? 0.650 0.809 0.738 0.090  -0.169 0.017  439 ASN EEE N   
5278 C CA  . ASN E 110 ? 0.665 0.816 0.761 0.113  -0.174 -0.002 439 ASN EEE CA  
5279 C C   . ASN E 110 ? 0.699 0.819 0.827 0.111  -0.199 0.019  439 ASN EEE C   
5280 O O   . ASN E 110 ? 0.699 0.828 0.833 0.123  -0.198 0.023  439 ASN EEE O   
5281 C CB  . ASN E 110 ? 0.685 0.825 0.780 0.134  -0.181 -0.044 439 ASN EEE CB  
5282 C CG  . ASN E 110 ? 0.687 0.842 0.784 0.160  -0.175 -0.070 439 ASN EEE CG  
5283 O OD1 . ASN E 110 ? 0.649 0.838 0.736 0.162  -0.156 -0.062 439 ASN EEE OD1 
5284 N ND2 . ASN E 110 ? 0.734 0.865 0.845 0.181  -0.193 -0.103 439 ASN EEE ND2 
5285 N N   . ASN E 111 ? 0.742 0.828 0.891 0.096  -0.221 0.035  440 ASN EEE N   
5286 C CA  . ASN E 111 ? 0.804 0.852 0.986 0.091  -0.249 0.060  440 ASN EEE CA  
5287 C C   . ASN E 111 ? 0.789 0.860 0.964 0.075  -0.239 0.103  440 ASN EEE C   
5288 O O   . ASN E 111 ? 0.809 0.858 1.003 0.077  -0.259 0.124  440 ASN EEE O   
5289 C CB  . ASN E 111 ? 0.866 0.873 1.074 0.074  -0.274 0.068  440 ASN EEE CB  
5290 C CG  . ASN E 111 ? 0.889 0.919 1.088 0.044  -0.261 0.097  440 ASN EEE CG  
5291 O OD1 . ASN E 111 ? 0.900 0.968 1.071 0.043  -0.236 0.086  440 ASN EEE OD1 
5292 N ND2 . ASN E 111 ? 0.934 0.945 1.159 0.019  -0.278 0.134  440 ASN EEE ND2 
5293 N N   . LEU E 112 ? 0.750 0.864 0.897 0.061  -0.212 0.116  441 LEU EEE N   
5294 C CA  . LEU E 112 ? 0.750 0.893 0.884 0.045  -0.201 0.154  441 LEU EEE CA  
5295 C C   . LEU E 112 ? 0.724 0.901 0.834 0.060  -0.182 0.143  441 LEU EEE C   
5296 O O   . LEU E 112 ? 0.719 0.905 0.827 0.058  -0.186 0.166  441 LEU EEE O   
5297 C CB  . LEU E 112 ? 0.736 0.906 0.858 0.022  -0.184 0.171  441 LEU EEE CB  
5298 C CG  . LEU E 112 ? 0.764 0.908 0.912 0.001  -0.201 0.190  441 LEU EEE CG  
5299 C CD1 . LEU E 112 ? 0.741 0.920 0.879 -0.016 -0.182 0.196  441 LEU EEE CD1 
5300 C CD2 . LEU E 112 ? 0.799 0.927 0.966 -0.015 -0.219 0.233  441 LEU EEE CD2 
5301 N N   . ASP E 113 ? 0.701 0.898 0.794 0.071  -0.163 0.111  442 ASP EEE N   
5302 C CA  . ASP E 113 ? 0.667 0.904 0.737 0.077  -0.140 0.104  442 ASP EEE CA  
5303 C C   . ASP E 113 ? 0.670 0.912 0.747 0.101  -0.140 0.076  442 ASP EEE C   
5304 O O   . ASP E 113 ? 0.655 0.928 0.718 0.104  -0.124 0.071  442 ASP EEE O   
5305 C CB  . ASP E 113 ? 0.621 0.882 0.668 0.068  -0.117 0.097  442 ASP EEE CB  
5306 C CG  . ASP E 113 ? 0.608 0.881 0.648 0.046  -0.112 0.124  442 ASP EEE CG  
5307 O OD1 . ASP E 113 ? 0.631 0.917 0.668 0.039  -0.113 0.149  442 ASP EEE OD1 
5308 O OD2 . ASP E 113 ? 0.577 0.851 0.617 0.038  -0.107 0.121  442 ASP EEE OD2 
5309 N N   . SER E 114 ? 0.682 0.894 0.780 0.116  -0.157 0.057  443 SER EEE N   
5310 C CA  . SER E 114 ? 0.683 0.903 0.795 0.142  -0.159 0.030  443 SER EEE CA  
5311 C C   . SER E 114 ? 0.728 0.925 0.869 0.152  -0.185 0.043  443 SER EEE C   
5312 O O   . SER E 114 ? 0.737 0.900 0.891 0.140  -0.206 0.067  443 SER EEE O   
5313 C CB  . SER E 114 ? 0.686 0.895 0.800 0.157  -0.159 -0.007 443 SER EEE CB  
5314 O OG  . SER E 114 ? 0.727 0.892 0.869 0.167  -0.187 -0.014 443 SER EEE OG  
5315 N N   . LYS E 115 ? 0.742 0.960 0.896 0.171  -0.184 0.031  444 LYS EEE N   
5316 C CA  . LYS E 115 ? 0.790 0.991 0.976 0.185  -0.210 0.040  444 LYS EEE CA  
5317 C C   . LYS E 115 ? 0.782 1.000 0.991 0.216  -0.209 0.003  444 LYS EEE C   
5318 O O   . LYS E 115 ? 0.735 0.996 0.930 0.219  -0.183 -0.017 444 LYS EEE O   
5319 C CB  . LYS E 115 ? 0.812 1.035 0.987 0.173  -0.210 0.074  444 LYS EEE CB  
5320 C CG  . LYS E 115 ? 0.864 1.075 1.019 0.145  -0.214 0.114  444 LYS EEE CG  
5321 C CD  . LYS E 115 ? 0.884 1.127 1.018 0.133  -0.208 0.140  444 LYS EEE CD  
5322 C CE  . LYS E 115 ? 0.885 1.140 0.986 0.106  -0.194 0.165  444 LYS EEE CE  
5323 N NZ  . LYS E 115 ? 0.853 1.148 0.929 0.099  -0.184 0.178  444 LYS EEE NZ  
5324 N N   . VAL E 116 ? 0.831 1.018 1.078 0.238  -0.237 -0.006 445 VAL EEE N   
5325 C CA  . VAL E 116 ? 0.836 1.044 1.114 0.271  -0.239 -0.040 445 VAL EEE CA  
5326 C C   . VAL E 116 ? 0.792 1.052 1.068 0.270  -0.225 -0.029 445 VAL EEE C   
5327 O O   . VAL E 116 ? 0.786 1.042 1.058 0.255  -0.237 0.008  445 VAL EEE O   
5328 C CB  . VAL E 116 ? 0.895 1.055 1.218 0.294  -0.277 -0.044 445 VAL EEE CB  
5329 C CG1 . VAL E 116 ? 0.933 1.050 1.264 0.304  -0.289 -0.073 445 VAL EEE CG1 
5330 C CG2 . VAL E 116 ? 0.920 1.045 1.249 0.278  -0.305 0.005  445 VAL EEE CG2 
5331 N N   . GLY E 117 ? 0.742 1.052 1.022 0.283  -0.202 -0.058 446 GLY EEE N   
5332 C CA  . GLY E 117 ? 0.691 1.056 0.969 0.277  -0.185 -0.051 446 GLY EEE CA  
5333 C C   . GLY E 117 ? 0.644 1.032 0.879 0.249  -0.156 -0.042 446 GLY EEE C   
5334 O O   . GLY E 117 ? 0.629 1.065 0.863 0.245  -0.137 -0.046 446 GLY EEE O   
5335 N N   . GLY E 118 ? 0.636 0.992 0.841 0.231  -0.154 -0.029 447 GLY EEE N   
5336 C CA  . GLY E 118 ? 0.594 0.963 0.759 0.206  -0.129 -0.022 447 GLY EEE CA  
5337 C C   . GLY E 118 ? 0.573 0.938 0.719 0.183  -0.133 0.013  447 GLY EEE C   
5338 O O   . GLY E 118 ? 0.592 0.970 0.749 0.185  -0.144 0.027  447 GLY EEE O   
5339 N N   . ASN E 119 ? 0.539 0.888 0.656 0.164  -0.125 0.024  448 ASN EEE N   
5340 C CA  . ASN E 119 ? 0.509 0.864 0.601 0.142  -0.121 0.052  448 ASN EEE CA  
5341 C C   . ASN E 119 ? 0.471 0.858 0.541 0.132  -0.096 0.042  448 ASN EEE C   
5342 O O   . ASN E 119 ? 0.471 0.856 0.531 0.131  -0.081 0.028  448 ASN EEE O   
5343 C CB  . ASN E 119 ? 0.520 0.844 0.600 0.127  -0.128 0.070  448 ASN EEE CB  
5344 C CG  . ASN E 119 ? 0.511 0.847 0.563 0.107  -0.119 0.095  448 ASN EEE CG  
5345 O OD1 . ASN E 119 ? 0.515 0.875 0.560 0.104  -0.119 0.103  448 ASN EEE OD1 
5346 N ND2 . ASN E 119 ? 0.505 0.830 0.545 0.093  -0.114 0.103  448 ASN EEE ND2 
5347 N N   . TYR E 120 ? 0.457 0.870 0.522 0.126  -0.093 0.050  449 TYR EEE N   
5348 C CA  . TYR E 120 ? 0.441 0.882 0.492 0.116  -0.073 0.041  449 TYR EEE CA  
5349 C C   . TYR E 120 ? 0.453 0.896 0.477 0.099  -0.070 0.057  449 TYR EEE C   
5350 O O   . TYR E 120 ? 0.441 0.904 0.456 0.091  -0.058 0.050  449 TYR EEE O   
5351 C CB  . TYR E 120 ? 0.445 0.919 0.519 0.125  -0.074 0.031  449 TYR EEE CB  
5352 C CG  . TYR E 120 ? 0.456 0.937 0.560 0.144  -0.074 0.012  449 TYR EEE CG  
5353 C CD1 . TYR E 120 ? 0.469 0.940 0.599 0.162  -0.095 0.012  449 TYR EEE CD1 
5354 C CD2 . TYR E 120 ? 0.443 0.944 0.549 0.146  -0.054 -0.007 449 TYR EEE CD2 
5355 C CE1 . TYR E 120 ? 0.478 0.959 0.638 0.183  -0.095 -0.010 449 TYR EEE CE1 
5356 C CE2 . TYR E 120 ? 0.444 0.959 0.574 0.166  -0.052 -0.027 449 TYR EEE CE2 
5357 C CZ  . TYR E 120 ? 0.467 0.972 0.625 0.186  -0.072 -0.031 449 TYR EEE CZ  
5358 O OH  . TYR E 120 ? 0.485 1.007 0.670 0.208  -0.070 -0.055 449 TYR EEE OH  
5359 N N   . ASN E 121 ? 0.486 0.912 0.499 0.093  -0.079 0.076  450 ASN EEE N   
5360 C CA  . ASN E 121 ? 0.493 0.928 0.480 0.079  -0.076 0.091  450 ASN EEE CA  
5361 C C   . ASN E 121 ? 0.487 0.921 0.457 0.070  -0.058 0.084  450 ASN EEE C   
5362 O O   . ASN E 121 ? 0.525 0.973 0.475 0.062  -0.051 0.087  450 ASN EEE O   
5363 C CB  . ASN E 121 ? 0.515 0.937 0.497 0.075  -0.091 0.118  450 ASN EEE CB  
5364 C CG  . ASN E 121 ? 0.546 0.974 0.539 0.082  -0.112 0.130  450 ASN EEE CG  
5365 O OD1 . ASN E 121 ? 0.534 0.981 0.538 0.090  -0.114 0.116  450 ASN EEE OD1 
5366 N ND2 . ASN E 121 ? 0.590 1.002 0.583 0.079  -0.128 0.157  450 ASN EEE ND2 
5367 N N   . TYR E 122 ? 0.470 0.888 0.446 0.073  -0.052 0.075  451 TYR EEE N   
5368 C CA  . TYR E 122 ? 0.454 0.870 0.417 0.066  -0.037 0.068  451 TYR EEE CA  
5369 C C   . TYR E 122 ? 0.433 0.863 0.395 0.067  -0.026 0.051  451 TYR EEE C   
5370 O O   . TYR E 122 ? 0.418 0.851 0.393 0.075  -0.025 0.041  451 TYR EEE O   
5371 C CB  . TYR E 122 ? 0.464 0.858 0.432 0.068  -0.039 0.067  451 TYR EEE CB  
5372 C CG  . TYR E 122 ? 0.482 0.863 0.453 0.062  -0.049 0.086  451 TYR EEE CG  
5373 C CD1 . TYR E 122 ? 0.472 0.864 0.431 0.050  -0.043 0.099  451 TYR EEE CD1 
5374 C CD2 . TYR E 122 ? 0.504 0.863 0.493 0.067  -0.066 0.092  451 TYR EEE CD2 
5375 C CE1 . TYR E 122 ? 0.484 0.870 0.448 0.041  -0.050 0.120  451 TYR EEE CE1 
5376 C CE2 . TYR E 122 ? 0.516 0.861 0.512 0.057  -0.077 0.114  451 TYR EEE CE2 
5377 C CZ  . TYR E 122 ? 0.502 0.863 0.485 0.043  -0.068 0.130  451 TYR EEE CZ  
5378 O OH  . TYR E 122 ? 0.505 0.858 0.496 0.030  -0.077 0.155  451 TYR EEE OH  
5379 N N   . LEU E 123 ? 0.438 0.876 0.386 0.060  -0.017 0.049  452 LEU EEE N   
5380 C CA  . LEU E 123 ? 0.435 0.882 0.384 0.057  -0.009 0.037  452 LEU EEE CA  
5381 C C   . LEU E 123 ? 0.438 0.875 0.377 0.053  0.001  0.034  452 LEU EEE C   
5382 O O   . LEU E 123 ? 0.428 0.856 0.359 0.052  0.001  0.039  452 LEU EEE O   
5383 C CB  . LEU E 123 ? 0.440 0.903 0.383 0.052  -0.013 0.036  452 LEU EEE CB  
5384 C CG  . LEU E 123 ? 0.442 0.917 0.390 0.055  -0.026 0.043  452 LEU EEE CG  
5385 C CD1 . LEU E 123 ? 0.441 0.933 0.380 0.051  -0.031 0.038  452 LEU EEE CD1 
5386 C CD2 . LEU E 123 ? 0.420 0.900 0.392 0.063  -0.031 0.039  452 LEU EEE CD2 
5387 N N   . TYR E 124 ? 0.433 0.871 0.376 0.050  0.007  0.027  453 TYR EEE N   
5388 C CA  . TYR E 124 ? 0.441 0.868 0.376 0.045  0.014  0.025  453 TYR EEE CA  
5389 C C   . TYR E 124 ? 0.428 0.859 0.369 0.037  0.015  0.020  453 TYR EEE C   
5390 O O   . TYR E 124 ? 0.421 0.867 0.375 0.035  0.014  0.018  453 TYR EEE O   
5391 C CB  . TYR E 124 ? 0.436 0.854 0.368 0.048  0.018  0.026  453 TYR EEE CB  
5392 C CG  . TYR E 124 ? 0.428 0.859 0.368 0.049  0.023  0.023  453 TYR EEE CG  
5393 C CD1 . TYR E 124 ? 0.432 0.871 0.380 0.058  0.020  0.020  453 TYR EEE CD1 
5394 C CD2 . TYR E 124 ? 0.435 0.872 0.376 0.041  0.031  0.025  453 TYR EEE CD2 
5395 C CE1 . TYR E 124 ? 0.446 0.903 0.404 0.062  0.026  0.014  453 TYR EEE CE1 
5396 C CE2 . TYR E 124 ? 0.451 0.908 0.400 0.042  0.038  0.023  453 TYR EEE CE2 
5397 C CZ  . TYR E 124 ? 0.446 0.916 0.404 0.053  0.036  0.016  453 TYR EEE CZ  
5398 O OH  . TYR E 124 ? 0.430 0.927 0.398 0.056  0.045  0.011  453 TYR EEE OH  
5399 N N   . ARG E 125 ? 0.422 0.841 0.359 0.034  0.016  0.017  454 ARG EEE N   
5400 C CA  . ARG E 125 ? 0.430 0.842 0.375 0.025  0.015  0.013  454 ARG EEE CA  
5401 C C   . ARG E 125 ? 0.409 0.819 0.359 0.019  0.021  0.023  454 ARG EEE C   
5402 O O   . ARG E 125 ? 0.406 0.804 0.346 0.022  0.024  0.028  454 ARG EEE O   
5403 C CB  . ARG E 125 ? 0.433 0.829 0.373 0.026  0.011  0.006  454 ARG EEE CB  
5404 C CG  . ARG E 125 ? 0.453 0.838 0.405 0.018  0.005  -0.001 454 ARG EEE CG  
5405 C CD  . ARG E 125 ? 0.478 0.849 0.427 0.024  -0.001 -0.016 454 ARG EEE CD  
5406 N NE  . ARG E 125 ? 0.475 0.864 0.411 0.032  -0.001 -0.026 454 ARG EEE NE  
5407 C CZ  . ARG E 125 ? 0.476 0.880 0.409 0.031  -0.007 -0.037 454 ARG EEE CZ  
5408 N NH1 . ARG E 125 ? 0.505 0.907 0.453 0.020  -0.015 -0.041 454 ARG EEE NH1 
5409 N NH2 . ARG E 125 ? 0.463 0.887 0.380 0.038  -0.007 -0.042 454 ARG EEE NH2 
5410 N N   . LEU E 126 ? 0.409 0.833 0.373 0.010  0.023  0.024  455 LEU EEE N   
5411 C CA  . LEU E 126 ? 0.422 0.855 0.392 0.001  0.032  0.035  455 LEU EEE CA  
5412 C C   . LEU E 126 ? 0.441 0.855 0.418 -0.013 0.029  0.042  455 LEU EEE C   
5413 O O   . LEU E 126 ? 0.472 0.882 0.444 -0.020 0.035  0.057  455 LEU EEE O   
5414 C CB  . LEU E 126 ? 0.416 0.882 0.404 -0.001 0.037  0.033  455 LEU EEE CB  
5415 C CG  . LEU E 126 ? 0.438 0.927 0.434 -0.009 0.049  0.044  455 LEU EEE CG  
5416 C CD1 . LEU E 126 ? 0.449 0.936 0.421 -0.000 0.058  0.047  455 LEU EEE CD1 
5417 C CD2 . LEU E 126 ? 0.440 0.968 0.462 -0.010 0.053  0.039  455 LEU EEE CD2 
5418 N N   . PHE E 127 ? 0.445 0.848 0.433 -0.017 0.018  0.033  456 PHE EEE N   
5419 C CA  . PHE E 127 ? 0.471 0.851 0.474 -0.032 0.010  0.037  456 PHE EEE CA  
5420 C C   . PHE E 127 ? 0.475 0.825 0.471 -0.023 -0.001 0.022  456 PHE EEE C   
5421 O O   . PHE E 127 ? 0.457 0.816 0.447 -0.012 -0.005 0.006  456 PHE EEE O   
5422 C CB  . PHE E 127 ? 0.485 0.882 0.513 -0.046 0.005  0.033  456 PHE EEE CB  
5423 C CG  . PHE E 127 ? 0.482 0.916 0.525 -0.056 0.017  0.046  456 PHE EEE CG  
5424 C CD1 . PHE E 127 ? 0.496 0.931 0.546 -0.071 0.025  0.067  456 PHE EEE CD1 
5425 C CD2 . PHE E 127 ? 0.460 0.928 0.511 -0.049 0.020  0.038  456 PHE EEE CD2 
5426 C CE1 . PHE E 127 ? 0.485 0.962 0.548 -0.079 0.039  0.078  456 PHE EEE CE1 
5427 C CE2 . PHE E 127 ? 0.441 0.948 0.510 -0.055 0.032  0.047  456 PHE EEE CE2 
5428 C CZ  . PHE E 127 ? 0.456 0.970 0.530 -0.070 0.043  0.066  456 PHE EEE CZ  
5429 N N   . ARG E 128 ? 0.492 0.811 0.494 -0.028 -0.008 0.028  457 ARG EEE N   
5430 C CA  . ARG E 128 ? 0.513 0.801 0.516 -0.019 -0.021 0.011  457 ARG EEE CA  
5431 C C   . ARG E 128 ? 0.547 0.798 0.567 -0.030 -0.032 0.022  457 ARG EEE C   
5432 O O   . ARG E 128 ? 0.549 0.797 0.566 -0.039 -0.027 0.047  457 ARG EEE O   
5433 C CB  . ARG E 128 ? 0.506 0.797 0.491 0.001  -0.016 0.005  457 ARG EEE CB  
5434 C CG  . ARG E 128 ? 0.508 0.790 0.493 0.014  -0.024 -0.020 457 ARG EEE CG  
5435 C CD  . ARG E 128 ? 0.498 0.793 0.467 0.031  -0.017 -0.024 457 ARG EEE CD  
5436 N NE  . ARG E 128 ? 0.515 0.810 0.485 0.045  -0.022 -0.049 457 ARG EEE NE  
5437 C CZ  . ARG E 128 ? 0.551 0.823 0.531 0.056  -0.029 -0.059 457 ARG EEE CZ  
5438 N NH1 . ARG E 128 ? 0.572 0.816 0.562 0.053  -0.035 -0.043 457 ARG EEE NH1 
5439 N NH2 . ARG E 128 ? 0.572 0.852 0.551 0.071  -0.031 -0.086 457 ARG EEE NH2 
5440 N N   . LYS E 129 ? 0.594 0.817 0.629 -0.029 -0.048 0.004  458 LYS EEE N   
5441 C CA  . LYS E 129 ? 0.652 0.833 0.710 -0.040 -0.064 0.012  458 LYS EEE CA  
5442 C C   . LYS E 129 ? 0.656 0.807 0.708 -0.028 -0.068 0.022  458 LYS EEE C   
5443 O O   . LYS E 129 ? 0.684 0.799 0.752 -0.039 -0.081 0.039  458 LYS EEE O   
5444 C CB  . LYS E 129 ? 0.712 0.871 0.789 -0.039 -0.083 -0.018 458 LYS EEE CB  
5445 C CG  . LYS E 129 ? 0.756 0.941 0.841 -0.053 -0.084 -0.028 458 LYS EEE CG  
5446 C CD  . LYS E 129 ? 0.824 0.987 0.928 -0.054 -0.106 -0.059 458 LYS EEE CD  
5447 C CE  . LYS E 129 ? 0.840 1.033 0.956 -0.070 -0.109 -0.064 458 LYS EEE CE  
5448 N NZ  . LYS E 129 ? 0.892 1.060 1.028 -0.075 -0.134 -0.094 458 LYS EEE NZ  
5449 N N   . SER E 130 ? 0.557 0.785 0.710 0.140  0.005  0.087  459 SER EEE N   
5450 C CA  . SER E 130 ? 0.552 0.788 0.736 0.147  -0.006 0.103  459 SER EEE CA  
5451 C C   . SER E 130 ? 0.516 0.782 0.675 0.149  0.004  0.098  459 SER EEE C   
5452 O O   . SER E 130 ? 0.494 0.770 0.621 0.146  0.018  0.080  459 SER EEE O   
5453 C CB  . SER E 130 ? 0.577 0.797 0.817 0.164  -0.011 0.087  459 SER EEE CB  
5454 O OG  . SER E 130 ? 0.582 0.818 0.824 0.174  0.007  0.050  459 SER EEE OG  
5455 N N   . ASN E 131 ? 0.509 0.789 0.683 0.151  -0.005 0.117  460 ASN EEE N   
5456 C CA  . ASN E 131 ? 0.495 0.802 0.648 0.151  0.002  0.116  460 ASN EEE CA  
5457 C C   . ASN E 131 ? 0.487 0.805 0.658 0.163  0.014  0.088  460 ASN EEE C   
5458 O O   . ASN E 131 ? 0.494 0.803 0.709 0.176  0.011  0.075  460 ASN EEE O   
5459 C CB  . ASN E 131 ? 0.508 0.829 0.673 0.147  -0.012 0.146  460 ASN EEE CB  
5460 C CG  . ASN E 131 ? 0.514 0.840 0.656 0.129  -0.021 0.172  460 ASN EEE CG  
5461 O OD1 . ASN E 131 ? 0.531 0.855 0.641 0.120  -0.015 0.165  460 ASN EEE OD1 
5462 N ND2 . ASN E 131 ? 0.513 0.851 0.671 0.122  -0.037 0.202  460 ASN EEE ND2 
5463 N N   . LEU E 132 ? 0.465 0.804 0.605 0.159  0.025  0.078  461 LEU EEE N   
5464 C CA  . LEU E 132 ? 0.462 0.824 0.613 0.165  0.035  0.055  461 LEU EEE CA  
5465 C C   . LEU E 132 ? 0.470 0.845 0.663 0.177  0.028  0.061  461 LEU EEE C   
5466 O O   . LEU E 132 ? 0.466 0.842 0.659 0.174  0.017  0.088  461 LEU EEE O   
5467 C CB  . LEU E 132 ? 0.443 0.825 0.551 0.153  0.041  0.054  461 LEU EEE CB  
5468 C CG  . LEU E 132 ? 0.434 0.807 0.507 0.141  0.047  0.045  461 LEU EEE CG  
5469 C CD1 . LEU E 132 ? 0.421 0.809 0.460 0.129  0.046  0.051  461 LEU EEE CD1 
5470 C CD2 . LEU E 132 ? 0.448 0.825 0.531 0.142  0.057  0.019  461 LEU EEE CD2 
5471 N N   . LYS E 133 ? 0.484 0.875 0.715 0.189  0.034  0.034  462 LYS EEE N   
5472 C CA  . LYS E 133 ? 0.477 0.892 0.748 0.201  0.030  0.032  462 LYS EEE CA  
5473 C C   . LYS E 133 ? 0.435 0.885 0.670 0.190  0.038  0.036  462 LYS EEE C   
5474 O O   . LYS E 133 ? 0.411 0.865 0.601 0.176  0.047  0.031  462 LYS EEE O   
5475 C CB  . LYS E 133 ? 0.513 0.941 0.836 0.217  0.037  -0.006 462 LYS EEE CB  
5476 C CG  . LYS E 133 ? 0.554 0.944 0.922 0.229  0.025  -0.010 462 LYS EEE CG  
5477 C CD  . LYS E 133 ? 0.591 0.994 1.011 0.244  0.032  -0.056 462 LYS EEE CD  
5478 C CE  . LYS E 133 ? 0.632 0.992 1.093 0.253  0.020  -0.061 462 LYS EEE CE  
5479 N NZ  . LYS E 133 ? 0.665 1.036 1.201 0.275  0.019  -0.104 462 LYS EEE NZ  
5480 N N   . PRO E 134 ? 0.428 0.900 0.682 0.195  0.032  0.047  463 PRO EEE N   
5481 C CA  . PRO E 134 ? 0.416 0.920 0.638 0.183  0.038  0.050  463 PRO EEE CA  
5482 C C   . PRO E 134 ? 0.408 0.941 0.612 0.174  0.054  0.021  463 PRO EEE C   
5483 O O   . PRO E 134 ? 0.400 0.952 0.638 0.184  0.062  -0.008 463 PRO EEE O   
5484 C CB  . PRO E 134 ? 0.413 0.942 0.676 0.195  0.031  0.057  463 PRO EEE CB  
5485 C CG  . PRO E 134 ? 0.423 0.922 0.727 0.207  0.015  0.075  463 PRO EEE CG  
5486 C CD  . PRO E 134 ? 0.434 0.902 0.744 0.211  0.018  0.059  463 PRO EEE CD  
5487 N N   . PHE E 135 ? 0.400 0.936 0.553 0.155  0.056  0.030  464 PHE EEE N   
5488 C CA  . PHE E 135 ? 0.414 0.980 0.540 0.138  0.066  0.014  464 PHE EEE CA  
5489 C C   . PHE E 135 ? 0.435 0.994 0.560 0.137  0.075  -0.009 464 PHE EEE C   
5490 O O   . PHE E 135 ? 0.438 1.030 0.549 0.122  0.084  -0.027 464 PHE EEE O   
5491 C CB  . PHE E 135 ? 0.409 1.029 0.557 0.138  0.073  -0.002 464 PHE EEE CB  
5492 C CG  . PHE E 135 ? 0.401 1.035 0.542 0.134  0.065  0.021  464 PHE EEE CG  
5493 C CD1 . PHE E 135 ? 0.399 1.020 0.495 0.116  0.057  0.044  464 PHE EEE CD1 
5494 C CD2 . PHE E 135 ? 0.393 1.054 0.575 0.148  0.064  0.017  464 PHE EEE CD2 
5495 C CE1 . PHE E 135 ? 0.385 1.020 0.474 0.111  0.050  0.062  464 PHE EEE CE1 
5496 C CE2 . PHE E 135 ? 0.382 1.058 0.556 0.143  0.057  0.039  464 PHE EEE CE2 
5497 C CZ  . PHE E 135 ? 0.374 1.038 0.500 0.123  0.051  0.061  464 PHE EEE CZ  
5498 N N   . GLU E 136 ? 0.465 0.984 0.601 0.147  0.071  -0.008 465 GLU EEE N   
5499 C CA  . GLU E 136 ? 0.498 1.004 0.629 0.144  0.078  -0.027 465 GLU EEE CA  
5500 C C   . GLU E 136 ? 0.493 0.985 0.572 0.125  0.076  -0.013 465 GLU EEE C   
5501 O O   . GLU E 136 ? 0.493 0.967 0.551 0.121  0.066  0.013  465 GLU EEE O   
5502 C CB  . GLU E 136 ? 0.541 1.009 0.704 0.161  0.073  -0.027 465 GLU EEE CB  
5503 C CG  . GLU E 136 ? 0.581 1.042 0.753 0.162  0.081  -0.054 465 GLU EEE CG  
5504 C CD  . GLU E 136 ? 0.629 1.048 0.830 0.175  0.072  -0.050 465 GLU EEE CD  
5505 O OE1 . GLU E 136 ? 0.647 1.050 0.879 0.188  0.060  -0.033 465 GLU EEE OE1 
5506 O OE2 . GLU E 136 ? 0.674 1.076 0.865 0.170  0.076  -0.061 465 GLU EEE OE2 
5507 N N   . ARG E 137 ? 0.508 1.011 0.572 0.113  0.083  -0.030 466 ARG EEE N   
5508 C CA  . ARG E 137 ? 0.510 1.002 0.531 0.093  0.078  -0.018 466 ARG EEE CA  
5509 C C   . ARG E 137 ? 0.499 0.973 0.520 0.094  0.083  -0.031 466 ARG EEE C   
5510 O O   . ARG E 137 ? 0.489 0.985 0.530 0.095  0.094  -0.059 466 ARG EEE O   
5511 C CB  . ARG E 137 ? 0.523 1.060 0.523 0.070  0.081  -0.021 466 ARG EEE CB  
5512 C CG  . ARG E 137 ? 0.534 1.061 0.495 0.048  0.070  -0.003 466 ARG EEE CG  
5513 C CD  . ARG E 137 ? 0.556 1.129 0.501 0.022  0.067  0.002  466 ARG EEE CD  
5514 N NE  . ARG E 137 ? 0.607 1.175 0.520 -0.003 0.053  0.021  466 ARG EEE NE  
5515 C CZ  . ARG E 137 ? 0.660 1.249 0.557 -0.024 0.054  0.015  466 ARG EEE CZ  
5516 N NH1 . ARG E 137 ? 0.649 1.267 0.559 -0.022 0.072  -0.014 466 ARG EEE NH1 
5517 N NH2 . ARG E 137 ? 0.661 1.242 0.533 -0.048 0.036  0.038  466 ARG EEE NH2 
5518 N N   . ASP E 138 ? 0.495 0.932 0.497 0.092  0.075  -0.015 467 ASP EEE N   
5519 C CA  . ASP E 138 ? 0.502 0.918 0.500 0.092  0.078  -0.024 467 ASP EEE CA  
5520 C C   . ASP E 138 ? 0.486 0.897 0.448 0.074  0.070  -0.011 467 ASP EEE C   
5521 O O   . ASP E 138 ? 0.469 0.857 0.419 0.075  0.059  0.008  467 ASP EEE O   
5522 C CB  . ASP E 138 ? 0.524 0.904 0.539 0.108  0.073  -0.016 467 ASP EEE CB  
5523 C CG  . ASP E 138 ? 0.551 0.910 0.563 0.107  0.075  -0.024 467 ASP EEE CG  
5524 O OD1 . ASP E 138 ? 0.547 0.917 0.541 0.093  0.080  -0.034 467 ASP EEE OD1 
5525 O OD2 . ASP E 138 ? 0.556 0.887 0.583 0.117  0.071  -0.017 467 ASP EEE OD2 
5526 N N   . ILE E 139 ? 0.491 0.925 0.439 0.056  0.074  -0.022 468 ILE EEE N   
5527 C CA  . ILE E 139 ? 0.487 0.918 0.406 0.037  0.064  -0.008 468 ILE EEE CA  
5528 C C   . ILE E 139 ? 0.495 0.913 0.410 0.035  0.068  -0.018 468 ILE EEE C   
5529 O O   . ILE E 139 ? 0.521 0.942 0.415 0.017  0.059  -0.009 468 ILE EEE O   
5530 C CB  . ILE E 139 ? 0.491 0.964 0.393 0.011  0.061  -0.006 468 ILE EEE CB  
5531 C CG1 . ILE E 139 ? 0.489 1.008 0.398 0.001  0.078  -0.034 468 ILE EEE CG1 
5532 C CG2 . ILE E 139 ? 0.489 0.972 0.393 0.012  0.055  0.007  468 ILE EEE CG2 
5533 C CD1 . ILE E 139 ? 0.502 1.071 0.389 -0.032 0.075  -0.029 468 ILE EEE CD1 
5534 N N   . SER E 140 ? 0.495 0.899 0.431 0.051  0.078  -0.034 469 SER EEE N   
5535 C CA  . SER E 140 ? 0.512 0.900 0.446 0.049  0.082  -0.045 469 SER EEE CA  
5536 C C   . SER E 140 ? 0.517 0.875 0.435 0.050  0.069  -0.024 469 SER EEE C   
5537 O O   . SER E 140 ? 0.511 0.853 0.429 0.059  0.060  -0.008 469 SER EEE O   
5538 C CB  . SER E 140 ? 0.515 0.890 0.480 0.067  0.091  -0.063 469 SER EEE CB  
5539 O OG  . SER E 140 ? 0.516 0.863 0.495 0.084  0.084  -0.047 469 SER EEE OG  
5540 N N   . THR E 141 ? 0.530 0.886 0.434 0.039  0.068  -0.027 470 THR EEE N   
5541 C CA  . THR E 141 ? 0.537 0.872 0.428 0.037  0.056  -0.011 470 THR EEE CA  
5542 C C   . THR E 141 ? 0.560 0.879 0.452 0.040  0.061  -0.020 470 THR EEE C   
5543 O O   . THR E 141 ? 0.573 0.886 0.454 0.033  0.053  -0.013 470 THR EEE O   
5544 C CB  . THR E 141 ? 0.533 0.883 0.406 0.017  0.043  0.001  470 THR EEE CB  
5545 O OG1 . THR E 141 ? 0.541 0.919 0.405 -0.001 0.052  -0.011 470 THR EEE OG1 
5546 C CG2 . THR E 141 ? 0.525 0.885 0.396 0.013  0.034  0.014  470 THR EEE CG2 
5547 N N   . GLU E 142 ? 0.605 0.919 0.516 0.049  0.072  -0.035 471 GLU EEE N   
5548 C CA  . GLU E 142 ? 0.649 0.945 0.566 0.051  0.076  -0.043 471 GLU EEE CA  
5549 C C   . GLU E 142 ? 0.636 0.909 0.552 0.061  0.068  -0.026 471 GLU EEE C   
5550 O O   . GLU E 142 ? 0.617 0.888 0.540 0.070  0.063  -0.015 471 GLU EEE O   
5551 C CB  . GLU E 142 ? 0.716 1.010 0.660 0.059  0.087  -0.064 471 GLU EEE CB  
5552 C CG  . GLU E 142 ? 0.817 1.102 0.767 0.055  0.092  -0.080 471 GLU EEE CG  
5553 C CD  . GLU E 142 ? 0.884 1.161 0.870 0.064  0.099  -0.104 471 GLU EEE CD  
5554 O OE1 . GLU E 142 ? 0.917 1.212 0.923 0.071  0.104  -0.118 471 GLU EEE OE1 
5555 O OE2 . GLU E 142 ? 0.901 1.155 0.899 0.065  0.097  -0.109 471 GLU EEE OE2 
5556 N N   . ILE E 143 ? 0.623 0.887 0.532 0.056  0.066  -0.025 472 ILE EEE N   
5557 C CA  . ILE E 143 ? 0.602 0.854 0.512 0.061  0.059  -0.012 472 ILE EEE CA  
5558 C C   . ILE E 143 ? 0.589 0.829 0.520 0.071  0.059  -0.007 472 ILE EEE C   
5559 O O   . ILE E 143 ? 0.566 0.796 0.514 0.072  0.064  -0.018 472 ILE EEE O   
5560 C CB  . ILE E 143 ? 0.612 0.860 0.513 0.053  0.058  -0.014 472 ILE EEE CB  
5561 C CG1 . ILE E 143 ? 0.604 0.865 0.488 0.044  0.054  -0.015 472 ILE EEE CG1 
5562 C CG2 . ILE E 143 ? 0.617 0.861 0.519 0.055  0.053  -0.003 472 ILE EEE CG2 
5563 C CD1 . ILE E 143 ? 0.613 0.872 0.488 0.036  0.054  -0.018 472 ILE EEE CD1 
5564 N N   . TYR E 144 ? 0.577 0.820 0.509 0.076  0.053  0.007  473 TYR EEE N   
5565 C CA  . TYR E 144 ? 0.566 0.801 0.517 0.081  0.049  0.019  473 TYR EEE CA  
5566 C C   . TYR E 144 ? 0.575 0.800 0.527 0.073  0.045  0.026  473 TYR EEE C   
5567 O O   . TYR E 144 ? 0.553 0.791 0.490 0.066  0.042  0.031  473 TYR EEE O   
5568 C CB  . TYR E 144 ? 0.568 0.817 0.516 0.084  0.043  0.032  473 TYR EEE CB  
5569 C CG  . TYR E 144 ? 0.580 0.826 0.546 0.086  0.037  0.049  473 TYR EEE CG  
5570 C CD1 . TYR E 144 ? 0.584 0.818 0.576 0.094  0.037  0.048  473 TYR EEE CD1 
5571 C CD2 . TYR E 144 ? 0.594 0.852 0.555 0.078  0.029  0.065  473 TYR EEE CD2 
5572 C CE1 . TYR E 144 ? 0.617 0.846 0.630 0.095  0.027  0.067  473 TYR EEE CE1 
5573 C CE2 . TYR E 144 ? 0.600 0.857 0.577 0.074  0.020  0.085  473 TYR EEE CE2 
5574 C CZ  . TYR E 144 ? 0.614 0.854 0.619 0.083  0.018  0.088  473 TYR EEE CZ  
5575 O OH  . TYR E 144 ? 0.637 0.875 0.664 0.080  0.005  0.111  473 TYR EEE OH  
5576 N N   . GLN E 145 ? 0.588 0.793 0.563 0.074  0.044  0.024  474 GLN EEE N   
5577 C CA  . GLN E 145 ? 0.612 0.802 0.594 0.064  0.036  0.036  474 GLN EEE CA  
5578 C C   . GLN E 145 ? 0.625 0.818 0.620 0.062  0.023  0.062  474 GLN EEE C   
5579 O O   . GLN E 145 ? 0.629 0.806 0.654 0.070  0.017  0.066  474 GLN EEE O   
5580 C CB  . GLN E 145 ? 0.634 0.800 0.640 0.066  0.038  0.019  474 GLN EEE CB  
5581 C CG  . GLN E 145 ? 0.657 0.804 0.672 0.055  0.028  0.030  474 GLN EEE CG  
5582 C CD  . GLN E 145 ? 0.686 0.804 0.734 0.059  0.027  0.011  474 GLN EEE CD  
5583 O OE1 . GLN E 145 ? 0.680 0.802 0.734 0.067  0.039  -0.017 474 GLN EEE OE1 
5584 N NE2 . GLN E 145 ? 0.724 0.817 0.796 0.052  0.012  0.025  474 GLN EEE NE2 
5585 N N   . ALA E 146 ? 0.618 0.835 0.593 0.051  0.019  0.077  475 ALA EEE N   
5586 C CA  . ALA E 146 ? 0.610 0.843 0.590 0.044  0.007  0.103  475 ALA EEE CA  
5587 C C   . ALA E 146 ? 0.632 0.851 0.626 0.028  -0.008 0.125  475 ALA EEE C   
5588 O O   . ALA E 146 ? 0.659 0.884 0.666 0.020  -0.021 0.151  475 ALA EEE O   
5589 C CB  . ALA E 146 ? 0.582 0.855 0.536 0.037  0.010  0.103  475 ALA EEE CB  
5590 N N   . GLY E 147 ? 0.635 0.838 0.627 0.021  -0.006 0.118  476 GLY EEE N   
5591 C CA  . GLY E 147 ? 0.670 0.857 0.675 0.004  -0.022 0.138  476 GLY EEE CA  
5592 C C   . GLY E 147 ? 0.704 0.845 0.742 0.013  -0.026 0.126  476 GLY EEE C   
5593 O O   . GLY E 147 ? 0.704 0.831 0.757 0.032  -0.016 0.103  476 GLY EEE O   
5594 N N   . SER E 148 ? 0.758 0.878 0.808 -0.003 -0.039 0.140  477 SER EEE N   
5595 C CA  . SER E 148 ? 0.800 0.874 0.889 0.003  -0.047 0.127  477 SER EEE CA  
5596 C C   . SER E 148 ? 0.800 0.869 0.871 0.005  -0.030 0.094  477 SER EEE C   
5597 O O   . SER E 148 ? 0.826 0.866 0.926 0.015  -0.028 0.069  477 SER EEE O   
5598 C CB  . SER E 148 ? 0.849 0.900 0.962 -0.017 -0.074 0.161  477 SER EEE CB  
5599 O OG  . SER E 148 ? 0.871 0.951 0.947 -0.044 -0.077 0.181  477 SER EEE OG  
5600 N N   . THR E 149 ? 0.791 0.892 0.819 -0.006 -0.019 0.093  478 THR EEE N   
5601 C CA  . THR E 149 ? 0.773 0.878 0.779 -0.007 -0.004 0.067  478 THR EEE CA  
5602 C C   . THR E 149 ? 0.743 0.858 0.743 0.011  0.014  0.038  478 THR EEE C   
5603 O O   . THR E 149 ? 0.699 0.838 0.685 0.019  0.020  0.042  478 THR EEE O   
5604 C CB  . THR E 149 ? 0.757 0.897 0.726 -0.025 -0.002 0.078  478 THR EEE CB  
5605 O OG1 . THR E 149 ? 0.786 0.923 0.761 -0.046 -0.020 0.107  478 THR EEE OG1 
5606 C CG2 . THR E 149 ? 0.748 0.894 0.697 -0.027 0.011  0.055  478 THR EEE CG2 
5607 N N   . PRO E 150 ? 0.764 0.864 0.773 0.016  0.024  0.009  479 PRO EEE N   
5608 C CA  . PRO E 150 ? 0.728 0.847 0.726 0.027  0.040  -0.016 479 PRO EEE CA  
5609 C C   . PRO E 150 ? 0.687 0.836 0.645 0.020  0.048  -0.015 479 PRO EEE C   
5610 O O   . PRO E 150 ? 0.693 0.847 0.636 0.008  0.045  -0.006 479 PRO EEE O   
5611 C CB  . PRO E 150 ? 0.750 0.854 0.767 0.027  0.047  -0.048 479 PRO EEE CB  
5612 C CG  . PRO E 150 ? 0.787 0.855 0.840 0.024  0.031  -0.041 479 PRO EEE CG  
5613 C CD  . PRO E 150 ? 0.797 0.866 0.832 0.011  0.018  -0.003 479 PRO EEE CD  
5614 N N   . CYS E 151 ? 0.665 0.834 0.611 0.028  0.056  -0.022 480 CYS EEE N   
5615 C CA  . CYS E 151 ? 0.650 0.845 0.567 0.025  0.059  -0.019 480 CYS EEE CA  
5616 C C   . CYS E 151 ? 0.639 0.843 0.542 0.017  0.066  -0.037 480 CYS EEE C   
5617 O O   . CYS E 151 ? 0.641 0.860 0.524 0.010  0.065  -0.033 480 CYS EEE O   
5618 C CB  . CYS E 151 ? 0.655 0.864 0.570 0.036  0.059  -0.015 480 CYS EEE CB  
5619 S SG  . CYS E 151 ? 0.721 0.926 0.650 0.043  0.050  0.006  480 CYS EEE SG  
5620 N N   . ASN E 152 ? 0.637 0.836 0.551 0.016  0.074  -0.058 481 ASN EEE N   
5621 C CA  . ASN E 152 ? 0.635 0.849 0.536 0.004  0.083  -0.077 481 ASN EEE CA  
5622 C C   . ASN E 152 ? 0.617 0.858 0.494 -0.001 0.081  -0.068 481 ASN EEE C   
5623 O O   . ASN E 152 ? 0.624 0.876 0.484 -0.013 0.080  -0.069 481 ASN EEE O   
5624 C CB  . ASN E 152 ? 0.651 0.855 0.550 -0.008 0.082  -0.081 481 ASN EEE CB  
5625 C CG  . ASN E 152 ? 0.682 0.858 0.610 -0.006 0.082  -0.095 481 ASN EEE CG  
5626 O OD1 . ASN E 152 ? 0.710 0.864 0.647 -0.008 0.072  -0.081 481 ASN EEE OD1 
5627 N ND2 . ASN E 152 ? 0.699 0.878 0.647 -0.002 0.090  -0.122 481 ASN EEE ND2 
5628 N N   . GLY E 153 ? 0.606 0.854 0.484 0.008  0.078  -0.060 482 GLY EEE N   
5629 C CA  . GLY E 153 ? 0.573 0.841 0.435 0.004  0.072  -0.051 482 GLY EEE CA  
5630 C C   . GLY E 153 ? 0.549 0.818 0.403 0.006  0.061  -0.035 482 GLY EEE C   
5631 O O   . GLY E 153 ? 0.569 0.852 0.414 0.001  0.052  -0.028 482 GLY EEE O   
5632 N N   . VAL E 154 ? 0.532 0.791 0.391 0.011  0.059  -0.030 483 VAL EEE N   
5633 C CA  . VAL E 154 ? 0.532 0.802 0.388 0.014  0.050  -0.021 483 VAL EEE CA  
5634 C C   . VAL E 154 ? 0.514 0.783 0.379 0.025  0.047  -0.013 483 VAL EEE C   
5635 O O   . VAL E 154 ? 0.535 0.792 0.407 0.026  0.050  -0.009 483 VAL EEE O   
5636 C CB  . VAL E 154 ? 0.528 0.801 0.377 0.003  0.051  -0.022 483 VAL EEE CB  
5637 C CG1 . VAL E 154 ? 0.512 0.804 0.362 0.006  0.042  -0.017 483 VAL EEE CG1 
5638 C CG2 . VAL E 154 ? 0.537 0.813 0.376 -0.010 0.054  -0.030 483 VAL EEE CG2 
5639 N N   . GLU E 155 ? 0.505 0.787 0.373 0.032  0.038  -0.010 484 GLU EEE N   
5640 C CA  . GLU E 155 ? 0.506 0.796 0.382 0.041  0.035  -0.005 484 GLU EEE CA  
5641 C C   . GLU E 155 ? 0.508 0.819 0.383 0.036  0.033  -0.005 484 GLU EEE C   
5642 O O   . GLU E 155 ? 0.528 0.847 0.398 0.030  0.032  -0.010 484 GLU EEE O   
5643 C CB  . GLU E 155 ? 0.501 0.800 0.384 0.050  0.026  -0.007 484 GLU EEE CB  
5644 C CG  . GLU E 155 ? 0.516 0.802 0.398 0.052  0.026  -0.004 484 GLU EEE CG  
5645 C CD  . GLU E 155 ? 0.513 0.802 0.403 0.058  0.014  -0.003 484 GLU EEE CD  
5646 O OE1 . GLU E 155 ? 0.521 0.822 0.421 0.066  0.007  -0.007 484 GLU EEE OE1 
5647 O OE2 . GLU E 155 ? 0.506 0.789 0.393 0.053  0.011  0.002  484 GLU EEE OE2 
5648 N N   . GLY E 156 ? 0.501 0.822 0.379 0.036  0.033  0.001  485 GLY EEE N   
5649 C CA  . GLY E 156 ? 0.492 0.842 0.368 0.026  0.032  0.003  485 GLY EEE CA  
5650 C C   . GLY E 156 ? 0.505 0.862 0.383 0.021  0.031  0.017  485 GLY EEE C   
5651 O O   . GLY E 156 ? 0.484 0.830 0.368 0.030  0.031  0.020  485 GLY EEE O   
5652 N N   . PHE E 157 ? 0.511 0.887 0.384 0.005  0.029  0.027  486 PHE EEE N   
5653 C CA  . PHE E 157 ? 0.518 0.902 0.394 -0.006 0.025  0.047  486 PHE EEE CA  
5654 C C   . PHE E 157 ? 0.526 0.864 0.412 0.001  0.024  0.058  486 PHE EEE C   
5655 O O   . PHE E 157 ? 0.547 0.852 0.437 0.002  0.026  0.056  486 PHE EEE O   
5656 C CB  . PHE E 157 ? 0.535 0.938 0.403 -0.029 0.020  0.062  486 PHE EEE CB  
5657 C CG  . PHE E 157 ? 0.559 0.977 0.429 -0.046 0.011  0.087  486 PHE EEE CG  
5658 C CD1 . PHE E 157 ? 0.551 1.020 0.418 -0.051 0.010  0.086  486 PHE EEE CD1 
5659 C CD2 . PHE E 157 ? 0.587 0.970 0.466 -0.056 0.002  0.112  486 PHE EEE CD2 
5660 C CE1 . PHE E 157 ? 0.567 1.055 0.434 -0.070 0.000  0.113  486 PHE EEE CE1 
5661 C CE2 . PHE E 157 ? 0.617 1.014 0.501 -0.074 -0.011 0.140  486 PHE EEE CE2 
5662 C CZ  . PHE E 157 ? 0.598 1.050 0.475 -0.082 -0.011 0.143  486 PHE EEE CZ  
5663 N N   . ASN E 158 ? 0.526 0.869 0.420 0.006  0.021  0.067  487 ASN EEE N   
5664 C CA  . ASN E 158 ? 0.554 0.861 0.464 0.014  0.019  0.077  487 ASN EEE CA  
5665 C C   . ASN E 158 ? 0.552 0.828 0.466 0.030  0.027  0.060  487 ASN EEE C   
5666 O O   . ASN E 158 ? 0.566 0.812 0.497 0.035  0.026  0.062  487 ASN EEE O   
5667 C CB  . ASN E 158 ? 0.581 0.869 0.503 0.000  0.009  0.100  487 ASN EEE CB  
5668 C CG  . ASN E 158 ? 0.592 0.907 0.516 -0.015 -0.003 0.126  487 ASN EEE CG  
5669 O OD1 . ASN E 158 ? 0.565 0.904 0.487 -0.011 -0.002 0.127  487 ASN EEE OD1 
5670 N ND2 . ASN E 158 ? 0.630 0.942 0.559 -0.036 -0.015 0.149  487 ASN EEE ND2 
5671 N N   . CYS E 159 ? 0.547 0.833 0.450 0.036  0.032  0.042  488 CYS EEE N   
5672 C CA  . CYS E 159 ? 0.566 0.833 0.469 0.045  0.039  0.028  488 CYS EEE CA  
5673 C C   . CYS E 159 ? 0.557 0.839 0.454 0.053  0.037  0.019  488 CYS EEE C   
5674 O O   . CYS E 159 ? 0.565 0.861 0.456 0.051  0.035  0.011  488 CYS EEE O   
5675 C CB  . CYS E 159 ? 0.581 0.839 0.477 0.037  0.042  0.019  488 CYS EEE CB  
5676 S SG  . CYS E 159 ? 0.610 0.838 0.520 0.030  0.042  0.023  488 CYS EEE SG  
5677 N N   . TYR E 160 ? 0.547 0.827 0.450 0.061  0.037  0.022  489 TYR EEE N   
5678 C CA  . TYR E 160 ? 0.524 0.818 0.427 0.068  0.032  0.017  489 TYR EEE CA  
5679 C C   . TYR E 160 ? 0.505 0.786 0.409 0.072  0.034  0.014  489 TYR EEE C   
5680 O O   . TYR E 160 ? 0.529 0.796 0.437 0.073  0.040  0.016  489 TYR EEE O   
5681 C CB  . TYR E 160 ? 0.498 0.809 0.405 0.069  0.029  0.024  489 TYR EEE CB  
5682 C CG  . TYR E 160 ? 0.492 0.827 0.397 0.059  0.028  0.029  489 TYR EEE CG  
5683 C CD1 . TYR E 160 ? 0.478 0.836 0.379 0.056  0.026  0.018  489 TYR EEE CD1 
5684 C CD2 . TYR E 160 ? 0.499 0.835 0.408 0.052  0.026  0.047  489 TYR EEE CD2 
5685 C CE1 . TYR E 160 ? 0.475 0.863 0.372 0.043  0.025  0.021  489 TYR EEE CE1 
5686 C CE2 . TYR E 160 ? 0.498 0.861 0.403 0.037  0.023  0.055  489 TYR EEE CE2 
5687 C CZ  . TYR E 160 ? 0.487 0.878 0.383 0.032  0.024  0.042  489 TYR EEE CZ  
5688 O OH  . TYR E 160 ? 0.513 0.939 0.404 0.014  0.021  0.049  489 TYR EEE OH  
5689 N N   . PHE E 161 ? 0.492 0.776 0.393 0.074  0.027  0.009  490 PHE EEE N   
5690 C CA  . PHE E 161 ? 0.491 0.770 0.391 0.074  0.024  0.011  490 PHE EEE CA  
5691 C C   . PHE E 161 ? 0.475 0.757 0.382 0.080  0.025  0.016  490 PHE EEE C   
5692 O O   . PHE E 161 ? 0.469 0.761 0.381 0.085  0.021  0.017  490 PHE EEE O   
5693 C CB  . PHE E 161 ? 0.493 0.775 0.394 0.072  0.011  0.009  490 PHE EEE CB  
5694 C CG  . PHE E 161 ? 0.507 0.786 0.403 0.064  0.007  0.015  490 PHE EEE CG  
5695 C CD1 . PHE E 161 ? 0.518 0.799 0.404 0.053  0.015  0.013  490 PHE EEE CD1 
5696 C CD2 . PHE E 161 ? 0.515 0.794 0.415 0.064  -0.004 0.021  490 PHE EEE CD2 
5697 C CE1 . PHE E 161 ? 0.533 0.822 0.412 0.040  0.012  0.018  490 PHE EEE CE1 
5698 C CE2 . PHE E 161 ? 0.515 0.797 0.408 0.052  -0.009 0.029  490 PHE EEE CE2 
5699 C CZ  . PHE E 161 ? 0.534 0.824 0.416 0.039  -0.001 0.028  490 PHE EEE CZ  
5700 N N   . PRO E 162 ? 0.467 0.744 0.376 0.081  0.031  0.018  491 PRO EEE N   
5701 C CA  . PRO E 162 ? 0.466 0.748 0.384 0.087  0.032  0.024  491 PRO EEE CA  
5702 C C   . PRO E 162 ? 0.453 0.741 0.369 0.088  0.024  0.028  491 PRO EEE C   
5703 O O   . PRO E 162 ? 0.454 0.749 0.376 0.093  0.023  0.033  491 PRO EEE O   
5704 C CB  . PRO E 162 ? 0.480 0.759 0.405 0.087  0.042  0.021  491 PRO EEE CB  
5705 C CG  . PRO E 162 ? 0.490 0.772 0.404 0.077  0.043  0.012  491 PRO EEE CG  
5706 C CD  . PRO E 162 ? 0.479 0.755 0.384 0.074  0.038  0.012  491 PRO EEE CD  
5707 N N   . LEU E 163 ? 0.450 0.737 0.361 0.083  0.014  0.026  492 LEU EEE N   
5708 C CA  . LEU E 163 ? 0.449 0.738 0.362 0.082  0.002  0.029  492 LEU EEE CA  
5709 C C   . LEU E 163 ? 0.450 0.740 0.372 0.087  -0.011 0.023  492 LEU EEE C   
5710 O O   . LEU E 163 ? 0.440 0.730 0.363 0.088  -0.011 0.016  492 LEU EEE O   
5711 C CB  . LEU E 163 ? 0.456 0.745 0.363 0.070  -0.004 0.035  492 LEU EEE CB  
5712 C CG  . LEU E 163 ? 0.459 0.758 0.360 0.065  0.009  0.035  492 LEU EEE CG  
5713 C CD1 . LEU E 163 ? 0.472 0.782 0.364 0.047  0.002  0.041  492 LEU EEE CD1 
5714 C CD2 . LEU E 163 ? 0.444 0.749 0.353 0.073  0.015  0.037  492 LEU EEE CD2 
5715 N N   . GLN E 164 ? 0.457 0.749 0.387 0.089  -0.021 0.022  493 GLN EEE N   
5716 C CA  . GLN E 164 ? 0.465 0.762 0.412 0.096  -0.034 0.009  493 GLN EEE CA  
5717 C C   . GLN E 164 ? 0.464 0.752 0.421 0.094  -0.052 0.012  493 GLN EEE C   
5718 O O   . GLN E 164 ? 0.491 0.780 0.440 0.090  -0.048 0.022  493 GLN EEE O   
5719 C CB  . GLN E 164 ? 0.465 0.784 0.413 0.101  -0.024 0.001  493 GLN EEE CB  
5720 C CG  . GLN E 164 ? 0.471 0.807 0.438 0.107  -0.034 -0.020 493 GLN EEE CG  
5721 C CD  . GLN E 164 ? 0.481 0.827 0.457 0.110  -0.037 -0.036 493 GLN EEE CD  
5722 O OE1 . GLN E 164 ? 0.494 0.848 0.459 0.107  -0.026 -0.033 493 GLN EEE OE1 
5723 N NE2 . GLN E 164 ? 0.500 0.848 0.502 0.117  -0.053 -0.055 493 GLN EEE NE2 
5724 N N   . SER E 165 ? 0.465 0.743 0.442 0.096  -0.072 0.004  494 SER EEE N   
5725 C CA  . SER E 165 ? 0.473 0.738 0.467 0.094  -0.095 0.004  494 SER EEE CA  
5726 C C   . SER E 165 ? 0.475 0.756 0.481 0.103  -0.092 -0.013 494 SER EEE C   
5727 O O   . SER E 165 ? 0.473 0.775 0.486 0.111  -0.084 -0.033 494 SER EEE O   
5728 C CB  . SER E 165 ? 0.478 0.727 0.499 0.096  -0.120 -0.001 494 SER EEE CB  
5729 O OG  . SER E 165 ? 0.487 0.723 0.496 0.083  -0.126 0.019  494 SER EEE OG  
5730 N N   . TYR E 166 ? 0.469 0.745 0.475 0.098  -0.100 -0.006 495 TYR EEE N   
5731 C CA  . TYR E 166 ? 0.467 0.751 0.496 0.105  -0.110 -0.026 495 TYR EEE CA  
5732 C C   . TYR E 166 ? 0.489 0.756 0.555 0.111  -0.138 -0.043 495 TYR EEE C   
5733 O O   . TYR E 166 ? 0.513 0.754 0.583 0.104  -0.154 -0.026 495 TYR EEE O   
5734 C CB  . TYR E 166 ? 0.472 0.749 0.493 0.096  -0.116 -0.012 495 TYR EEE CB  
5735 C CG  . TYR E 166 ? 0.458 0.755 0.452 0.092  -0.092 0.002  495 TYR EEE CG  
5736 C CD1 . TYR E 166 ? 0.438 0.763 0.430 0.097  -0.078 -0.010 495 TYR EEE CD1 
5737 C CD2 . TYR E 166 ? 0.450 0.741 0.424 0.083  -0.086 0.026  495 TYR EEE CD2 
5738 C CE1 . TYR E 166 ? 0.423 0.764 0.396 0.094  -0.061 0.006  495 TYR EEE CE1 
5739 C CE2 . TYR E 166 ? 0.442 0.750 0.399 0.082  -0.067 0.036  495 TYR EEE CE2 
5740 C CZ  . TYR E 166 ? 0.427 0.757 0.386 0.088  -0.056 0.028  495 TYR EEE CZ  
5741 O OH  . TYR E 166 ? 0.425 0.770 0.372 0.087  -0.041 0.040  495 TYR EEE OH  
5742 N N   . GLY E 167 ? 0.491 0.773 0.585 0.121  -0.143 -0.075 496 GLY EEE N   
5743 C CA  . GLY E 167 ? 0.513 0.780 0.654 0.131  -0.172 -0.098 496 GLY EEE CA  
5744 C C   . GLY E 167 ? 0.539 0.795 0.704 0.130  -0.192 -0.108 496 GLY EEE C   
5745 O O   . GLY E 167 ? 0.572 0.853 0.760 0.139  -0.191 -0.144 496 GLY EEE O   
5746 N N   . PHE E 168 ? 0.558 0.781 0.716 0.117  -0.209 -0.077 497 PHE EEE N   
5747 C CA  . PHE E 168 ? 0.584 0.792 0.762 0.113  -0.229 -0.081 497 PHE EEE CA  
5748 C C   . PHE E 168 ? 0.628 0.806 0.864 0.121  -0.268 -0.101 497 PHE EEE C   
5749 O O   . PHE E 168 ? 0.651 0.794 0.901 0.114  -0.295 -0.076 497 PHE EEE O   
5750 C CB  . PHE E 168 ? 0.582 0.772 0.728 0.092  -0.232 -0.038 497 PHE EEE CB  
5751 C CG  . PHE E 168 ? 0.554 0.773 0.652 0.087  -0.197 -0.024 497 PHE EEE CG  
5752 C CD1 . PHE E 168 ? 0.536 0.788 0.628 0.094  -0.177 -0.045 497 PHE EEE CD1 
5753 C CD2 . PHE E 168 ? 0.544 0.762 0.608 0.073  -0.187 0.010  497 PHE EEE CD2 
5754 C CE1 . PHE E 168 ? 0.509 0.785 0.564 0.089  -0.149 -0.029 497 PHE EEE CE1 
5755 C CE2 . PHE E 168 ? 0.521 0.764 0.551 0.071  -0.158 0.019  497 PHE EEE CE2 
5756 C CZ  . PHE E 168 ? 0.511 0.780 0.538 0.080  -0.140 0.002  497 PHE EEE CZ  
5757 N N   . GLN E 169 ? 0.659 0.856 0.933 0.136  -0.271 -0.147 498 GLN EEE N   
5758 C CA  . GLN E 169 ? 0.716 0.889 1.058 0.148  -0.310 -0.178 498 GLN EEE CA  
5759 C C   . GLN E 169 ? 0.728 0.899 1.085 0.145  -0.319 -0.195 498 GLN EEE C   
5760 O O   . GLN E 169 ? 0.706 0.914 1.029 0.141  -0.290 -0.201 498 GLN EEE O   
5761 C CB  . GLN E 169 ? 0.728 0.933 1.107 0.169  -0.304 -0.227 498 GLN EEE CB  
5762 C CG  . GLN E 169 ? 0.743 0.955 1.100 0.171  -0.289 -0.210 498 GLN EEE CG  
5763 C CD  . GLN E 169 ? 0.756 1.004 1.152 0.190  -0.286 -0.258 498 GLN EEE CD  
5764 O OE1 . GLN E 169 ? 0.769 0.998 1.200 0.199  -0.307 -0.261 498 GLN EEE OE1 
5765 N NE2 . GLN E 169 ? 0.762 1.066 1.152 0.195  -0.259 -0.296 498 GLN EEE NE2 
5766 N N   . PRO E 170 ? 0.653 0.790 0.911 0.041  -0.151 -0.042 499 PRO EEE N   
5767 C CA  . PRO E 170 ? 0.656 0.795 0.952 0.040  -0.158 -0.060 499 PRO EEE CA  
5768 C C   . PRO E 170 ? 0.651 0.820 0.944 0.047  -0.153 -0.106 499 PRO EEE C   
5769 O O   . PRO E 170 ? 0.659 0.843 0.949 0.049  -0.152 -0.121 499 PRO EEE O   
5770 C CB  . PRO E 170 ? 0.673 0.794 1.049 0.042  -0.173 -0.056 499 PRO EEE CB  
5771 C CG  . PRO E 170 ? 0.676 0.786 1.039 0.044  -0.176 -0.017 499 PRO EEE CG  
5772 C CD  . PRO E 170 ? 0.664 0.790 0.963 0.044  -0.164 -0.025 499 PRO EEE CD  
5773 N N   . THR E 171 ? 0.645 0.828 0.939 0.053  -0.149 -0.126 500 THR EEE N   
5774 C CA  . THR E 171 ? 0.630 0.853 0.927 0.063  -0.144 -0.171 500 THR EEE CA  
5775 C C   . THR E 171 ? 0.625 0.875 0.852 0.067  -0.122 -0.163 500 THR EEE C   
5776 O O   . THR E 171 ? 0.619 0.912 0.838 0.079  -0.114 -0.192 500 THR EEE O   
5777 C CB  . THR E 171 ? 0.622 0.850 0.962 0.068  -0.149 -0.194 500 THR EEE CB  
5778 O OG1 . THR E 171 ? 0.613 0.823 0.927 0.063  -0.142 -0.165 500 THR EEE OG1 
5779 C CG2 . THR E 171 ? 0.620 0.829 1.045 0.068  -0.170 -0.207 500 THR EEE CG2 
5780 N N   . ASN E 172 ? 0.632 0.862 0.813 0.060  -0.112 -0.125 501 ASN EEE N   
5781 C CA  . ASN E 172 ? 0.643 0.893 0.767 0.064  -0.090 -0.111 501 ASN EEE CA  
5782 C C   . ASN E 172 ? 0.660 0.949 0.771 0.075  -0.090 -0.131 501 ASN EEE C   
5783 O O   . ASN E 172 ? 0.664 0.949 0.806 0.073  -0.108 -0.147 501 ASN EEE O   
5784 C CB  . ASN E 172 ? 0.640 0.861 0.732 0.054  -0.083 -0.073 501 ASN EEE CB  
5785 C CG  . ASN E 172 ? 0.631 0.834 0.723 0.047  -0.076 -0.057 501 ASN EEE CG  
5786 O OD1 . ASN E 172 ? 0.612 0.820 0.728 0.049  -0.076 -0.072 501 ASN EEE OD1 
5787 N ND2 . ASN E 172 ? 0.624 0.811 0.694 0.040  -0.071 -0.033 501 ASN EEE ND2 
5788 N N   . GLY E 173 ? 0.661 0.989 0.732 0.087  -0.070 -0.129 502 GLY EEE N   
5789 C CA  . GLY E 173 ? 0.668 1.040 0.711 0.101  -0.068 -0.137 502 GLY EEE CA  
5790 C C   . GLY E 173 ? 0.677 1.021 0.698 0.093  -0.070 -0.109 502 GLY EEE C   
5791 O O   . GLY E 173 ? 0.663 0.964 0.676 0.079  -0.064 -0.076 502 GLY EEE O   
5792 N N   . VAL E 174 ? 0.685 1.059 0.702 0.102  -0.080 -0.126 503 VAL EEE N   
5793 C CA  . VAL E 174 ? 0.670 1.021 0.677 0.094  -0.086 -0.107 503 VAL EEE CA  
5794 C C   . VAL E 174 ? 0.650 0.982 0.610 0.091  -0.064 -0.060 503 VAL EEE C   
5795 O O   . VAL E 174 ? 0.641 0.932 0.601 0.076  -0.067 -0.038 503 VAL EEE O   
5796 C CB  . VAL E 174 ? 0.686 1.086 0.694 0.108  -0.097 -0.138 503 VAL EEE CB  
5797 C CG1 . VAL E 174 ? 0.677 1.053 0.678 0.099  -0.102 -0.119 503 VAL EEE CG1 
5798 C CG2 . VAL E 174 ? 0.702 1.123 0.772 0.111  -0.118 -0.192 503 VAL EEE CG2 
5799 N N   . GLY E 175 ? 0.656 1.019 0.585 0.104  -0.042 -0.046 504 GLY EEE N   
5800 C CA  . GLY E 175 ? 0.654 1.001 0.556 0.103  -0.018 -0.003 504 GLY EEE CA  
5801 C C   . GLY E 175 ? 0.646 0.938 0.567 0.083  -0.016 0.013  504 GLY EEE C   
5802 O O   . GLY E 175 ? 0.632 0.901 0.545 0.076  -0.006 0.040  504 GLY EEE O   
5803 N N   . TYR E 176 ? 0.644 0.923 0.595 0.075  -0.025 -0.006 505 TYR EEE N   
5804 C CA  . TYR E 176 ? 0.633 0.874 0.605 0.060  -0.025 0.002  505 TYR EEE CA  
5805 C C   . TYR E 176 ? 0.612 0.824 0.603 0.048  -0.050 -0.005 505 TYR EEE C   
5806 O O   . TYR E 176 ? 0.603 0.794 0.612 0.040  -0.055 -0.001 505 TYR EEE O   
5807 C CB  . TYR E 176 ? 0.645 0.896 0.638 0.063  -0.016 -0.010 505 TYR EEE CB  
5808 C CG  . TYR E 176 ? 0.679 0.948 0.661 0.071  0.015  0.010  505 TYR EEE CG  
5809 C CD1 . TYR E 176 ? 0.701 1.018 0.664 0.089  0.029  0.011  505 TYR EEE CD1 
5810 C CD2 . TYR E 176 ? 0.689 0.936 0.689 0.061  0.032  0.029  505 TYR EEE CD2 
5811 C CE1 . TYR E 176 ? 0.720 1.058 0.679 0.098  0.061  0.039  505 TYR EEE CE1 
5812 C CE2 . TYR E 176 ? 0.708 0.969 0.714 0.068  0.064  0.051  505 TYR EEE CE2 
5813 C CZ  . TYR E 176 ? 0.723 1.028 0.708 0.086  0.080  0.062  505 TYR EEE CZ  
5814 O OH  . TYR E 176 ? 0.739 1.062 0.735 0.095  0.115  0.093  505 TYR EEE OH  
5815 N N   . GLN E 177 ? 0.605 0.824 0.600 0.050  -0.065 -0.014 506 GLN EEE N   
5816 C CA  . GLN E 177 ? 0.600 0.793 0.620 0.040  -0.084 -0.011 506 GLN EEE CA  
5817 C C   . GLN E 177 ? 0.593 0.771 0.588 0.032  -0.080 0.016  506 GLN EEE C   
5818 O O   . GLN E 177 ? 0.585 0.773 0.551 0.036  -0.067 0.025  506 GLN EEE O   
5819 C CB  . GLN E 177 ? 0.607 0.813 0.657 0.044  -0.099 -0.036 506 GLN EEE CB  
5820 C CG  . GLN E 177 ? 0.613 0.828 0.706 0.048  -0.109 -0.066 506 GLN EEE CG  
5821 C CD  . GLN E 177 ? 0.615 0.848 0.754 0.053  -0.125 -0.100 506 GLN EEE CD  
5822 O OE1 . GLN E 177 ? 0.600 0.827 0.752 0.048  -0.132 -0.096 506 GLN EEE OE1 
5823 N NE2 . GLN E 177 ? 0.629 0.887 0.799 0.062  -0.130 -0.137 506 GLN EEE NE2 
5824 N N   . PRO E 178 ? 0.600 0.759 0.609 0.023  -0.090 0.030  507 PRO EEE N   
5825 C CA  . PRO E 178 ? 0.596 0.749 0.584 0.017  -0.086 0.052  507 PRO EEE CA  
5826 C C   . PRO E 178 ? 0.605 0.761 0.588 0.017  -0.089 0.055  507 PRO EEE C   
5827 O O   . PRO E 178 ? 0.621 0.779 0.636 0.017  -0.100 0.043  507 PRO EEE O   
5828 C CB  . PRO E 178 ? 0.601 0.745 0.606 0.013  -0.097 0.067  507 PRO EEE CB  
5829 C CG  . PRO E 178 ? 0.602 0.740 0.649 0.015  -0.109 0.057  507 PRO EEE CG  
5830 C CD  . PRO E 178 ? 0.611 0.759 0.659 0.021  -0.104 0.029  507 PRO EEE CD  
5831 N N   . TYR E 179 ? 0.604 0.764 0.559 0.016  -0.079 0.066  508 TYR EEE N   
5832 C CA  . TYR E 179 ? 0.603 0.768 0.552 0.015  -0.082 0.070  508 TYR EEE CA  
5833 C C   . TYR E 179 ? 0.585 0.745 0.523 0.007  -0.079 0.091  508 TYR EEE C   
5834 O O   . TYR E 179 ? 0.570 0.730 0.490 0.007  -0.069 0.096  508 TYR EEE O   
5835 C CB  . TYR E 179 ? 0.616 0.801 0.542 0.026  -0.073 0.062  508 TYR EEE CB  
5836 C CG  . TYR E 179 ? 0.633 0.839 0.573 0.036  -0.081 0.036  508 TYR EEE CG  
5837 C CD1 . TYR E 179 ? 0.636 0.849 0.588 0.041  -0.082 0.020  508 TYR EEE CD1 
5838 C CD2 . TYR E 179 ? 0.624 0.851 0.571 0.041  -0.089 0.021  508 TYR EEE CD2 
5839 C CE1 . TYR E 179 ? 0.644 0.886 0.614 0.052  -0.090 -0.011 508 TYR EEE CE1 
5840 C CE2 . TYR E 179 ? 0.633 0.891 0.600 0.052  -0.099 -0.012 508 TYR EEE CE2 
5841 C CZ  . TYR E 179 ? 0.632 0.899 0.610 0.058  -0.100 -0.029 508 TYR EEE CZ  
5842 O OH  . TYR E 179 ? 0.648 0.954 0.650 0.071  -0.110 -0.069 508 TYR EEE OH  
5843 N N   . ARG E 180 ? 0.587 0.745 0.542 0.001  -0.087 0.101  509 ARG EEE N   
5844 C CA  . ARG E 180 ? 0.591 0.754 0.533 -0.004 -0.084 0.120  509 ARG EEE CA  
5845 C C   . ARG E 180 ? 0.589 0.758 0.513 -0.003 -0.078 0.115  509 ARG EEE C   
5846 O O   . ARG E 180 ? 0.569 0.742 0.503 0.001  -0.082 0.103  509 ARG EEE O   
5847 C CB  . ARG E 180 ? 0.595 0.757 0.567 -0.010 -0.091 0.139  509 ARG EEE CB  
5848 C CG  . ARG E 180 ? 0.603 0.767 0.586 -0.008 -0.095 0.152  509 ARG EEE CG  
5849 C CD  . ARG E 180 ? 0.614 0.779 0.632 -0.011 -0.100 0.182  509 ARG EEE CD  
5850 N NE  . ARG E 180 ? 0.624 0.797 0.645 -0.005 -0.104 0.197  509 ARG EEE NE  
5851 C CZ  . ARG E 180 ? 0.649 0.839 0.682 -0.001 -0.105 0.233  509 ARG EEE CZ  
5852 N NH1 . ARG E 180 ? 0.663 0.861 0.712 -0.005 -0.099 0.260  509 ARG EEE NH1 
5853 N NH2 . ARG E 180 ? 0.651 0.854 0.683 0.008  -0.111 0.243  509 ARG EEE NH2 
5854 N N   . VAL E 181 ? 0.589 0.765 0.493 -0.003 -0.069 0.122  510 VAL EEE N   
5855 C CA  . VAL E 181 ? 0.578 0.760 0.466 0.000  -0.062 0.120  510 VAL EEE CA  
5856 C C   . VAL E 181 ? 0.588 0.782 0.474 -0.006 -0.061 0.131  510 VAL EEE C   
5857 O O   . VAL E 181 ? 0.575 0.777 0.458 -0.009 -0.060 0.135  510 VAL EEE O   
5858 C CB  . VAL E 181 ? 0.575 0.755 0.452 0.007  -0.049 0.117  510 VAL EEE CB  
5859 C CG1 . VAL E 181 ? 0.582 0.768 0.450 0.013  -0.041 0.121  510 VAL EEE CG1 
5860 C CG2 . VAL E 181 ? 0.575 0.752 0.454 0.015  -0.048 0.110  510 VAL EEE CG2 
5861 N N   . VAL E 182 ? 0.592 0.791 0.478 -0.007 -0.061 0.131  511 VAL EEE N   
5862 C CA  . VAL E 182 ? 0.588 0.802 0.470 -0.011 -0.058 0.138  511 VAL EEE CA  
5863 C C   . VAL E 182 ? 0.588 0.805 0.462 -0.004 -0.052 0.131  511 VAL EEE C   
5864 O O   . VAL E 182 ? 0.568 0.786 0.446 0.000  -0.057 0.125  511 VAL EEE O   
5865 C CB  . VAL E 182 ? 0.607 0.829 0.510 -0.019 -0.062 0.151  511 VAL EEE CB  
5866 C CG1 . VAL E 182 ? 0.611 0.855 0.509 -0.023 -0.056 0.159  511 VAL EEE CG1 
5867 C CG2 . VAL E 182 ? 0.611 0.830 0.529 -0.022 -0.066 0.166  511 VAL EEE CG2 
5868 N N   . VAL E 183 ? 0.587 0.809 0.456 -0.002 -0.044 0.129  512 VAL EEE N   
5869 C CA  . VAL E 183 ? 0.576 0.802 0.444 0.005  -0.037 0.127  512 VAL EEE CA  
5870 C C   . VAL E 183 ? 0.579 0.823 0.451 -0.001 -0.037 0.126  512 VAL EEE C   
5871 O O   . VAL E 183 ? 0.567 0.825 0.441 -0.006 -0.034 0.122  512 VAL EEE O   
5872 C CB  . VAL E 183 ? 0.581 0.799 0.458 0.011  -0.025 0.124  512 VAL EEE CB  
5873 C CG1 . VAL E 183 ? 0.586 0.805 0.469 0.022  -0.017 0.129  512 VAL EEE CG1 
5874 C CG2 . VAL E 183 ? 0.578 0.782 0.454 0.016  -0.022 0.127  512 VAL EEE CG2 
5875 N N   . LEU E 184 ? 0.574 0.824 0.447 0.000  -0.042 0.126  513 LEU EEE N   
5876 C CA  . LEU E 184 ? 0.572 0.842 0.452 -0.004 -0.040 0.125  513 LEU EEE CA  
5877 C C   . LEU E 184 ? 0.585 0.858 0.469 0.006  -0.034 0.119  513 LEU EEE C   
5878 O O   . LEU E 184 ? 0.612 0.879 0.492 0.017  -0.035 0.121  513 LEU EEE O   
5879 C CB  . LEU E 184 ? 0.582 0.858 0.475 -0.008 -0.048 0.126  513 LEU EEE CB  
5880 C CG  . LEU E 184 ? 0.586 0.858 0.493 -0.018 -0.052 0.136  513 LEU EEE CG  
5881 C CD1 . LEU E 184 ? 0.586 0.865 0.525 -0.023 -0.057 0.133  513 LEU EEE CD1 
5882 C CD2 . LEU E 184 ? 0.580 0.866 0.483 -0.026 -0.046 0.150  513 LEU EEE CD2 
5883 N N   . SER E 185 ? 0.604 0.889 0.497 0.004  -0.027 0.112  514 SER EEE N   
5884 C CA  . SER E 185 ? 0.611 0.902 0.521 0.011  -0.021 0.104  514 SER EEE CA  
5885 C C   . SER E 185 ? 0.602 0.919 0.516 0.006  -0.022 0.098  514 SER EEE C   
5886 O O   . SER E 185 ? 0.635 0.973 0.544 -0.004 -0.023 0.097  514 SER EEE O   
5887 C CB  . SER E 185 ? 0.612 0.903 0.545 0.013  -0.012 0.091  514 SER EEE CB  
5888 O OG  . SER E 185 ? 0.664 0.932 0.596 0.015  -0.009 0.098  514 SER EEE OG  
5889 N N   . PHE E 186 ? 0.587 0.907 0.511 0.014  -0.022 0.096  515 PHE EEE N   
5890 C CA  . PHE E 186 ? 0.581 0.927 0.514 0.010  -0.024 0.089  515 PHE EEE CA  
5891 C C   . PHE E 186 ? 0.585 0.941 0.543 0.017  -0.016 0.074  515 PHE EEE C   
5892 O O   . PHE E 186 ? 0.643 0.983 0.615 0.030  -0.014 0.079  515 PHE EEE O   
5893 C CB  . PHE E 186 ? 0.573 0.918 0.503 0.016  -0.032 0.094  515 PHE EEE CB  
5894 C CG  . PHE E 186 ? 0.571 0.908 0.492 0.009  -0.040 0.100  515 PHE EEE CG  
5895 C CD1 . PHE E 186 ? 0.571 0.890 0.479 0.018  -0.044 0.105  515 PHE EEE CD1 
5896 C CD2 . PHE E 186 ? 0.558 0.908 0.490 -0.005 -0.040 0.102  515 PHE EEE CD2 
5897 C CE1 . PHE E 186 ? 0.572 0.886 0.480 0.013  -0.051 0.105  515 PHE EEE CE1 
5898 C CE2 . PHE E 186 ? 0.568 0.907 0.506 -0.011 -0.047 0.107  515 PHE EEE CE2 
5899 C CZ  . PHE E 186 ? 0.575 0.897 0.502 -0.002 -0.053 0.105  515 PHE EEE CZ  
5900 N N   . GLU E 187 ? 0.573 0.960 0.540 0.009  -0.012 0.059  516 GLU EEE N   
5901 C CA  . GLU E 187 ? 0.579 0.986 0.579 0.014  -0.006 0.035  516 GLU EEE CA  
5902 C C   . GLU E 187 ? 0.568 1.002 0.576 0.013  -0.007 0.027  516 GLU EEE C   
5903 O O   . GLU E 187 ? 0.533 0.993 0.524 0.003  -0.007 0.032  516 GLU EEE O   
5904 C CB  . GLU E 187 ? 0.587 1.023 0.593 0.009  -0.003 0.013  516 GLU EEE CB  
5905 C CG  . GLU E 187 ? 0.610 1.064 0.665 0.015  0.003  -0.021 516 GLU EEE CG  
5906 C CD  . GLU E 187 ? 0.618 1.114 0.683 0.013  0.004  -0.052 516 GLU EEE CD  
5907 O OE1 . GLU E 187 ? 0.598 1.140 0.630 0.008  0.002  -0.053 516 GLU EEE OE1 
5908 O OE2 . GLU E 187 ? 0.634 1.123 0.744 0.018  0.007  -0.076 516 GLU EEE OE2 
5909 N N   . LEU E 188 ? 0.563 0.993 0.603 0.024  -0.005 0.018  517 LEU EEE N   
5910 C CA  . LEU E 188 ? 0.567 1.026 0.625 0.025  -0.005 0.006  517 LEU EEE CA  
5911 C C   . LEU E 188 ? 0.573 1.047 0.679 0.032  0.001  -0.023 517 LEU EEE C   
5912 O O   . LEU E 188 ? 0.551 0.996 0.691 0.045  0.003  -0.019 517 LEU EEE O   
5913 C CB  . LEU E 188 ? 0.579 1.020 0.634 0.036  -0.013 0.023  517 LEU EEE CB  
5914 C CG  . LEU E 188 ? 0.584 1.055 0.647 0.033  -0.016 0.014  517 LEU EEE CG  
5915 C CD1 . LEU E 188 ? 0.581 1.070 0.621 0.016  -0.016 0.020  517 LEU EEE CD1 
5916 C CD2 . LEU E 188 ? 0.584 1.044 0.652 0.049  -0.025 0.024  517 LEU EEE CD2 
5917 N N   . LEU E 189 ? 0.592 1.115 0.707 0.026  0.005  -0.051 518 LEU EEE N   
5918 C CA  . LEU E 189 ? 0.609 1.160 0.778 0.031  0.010  -0.092 518 LEU EEE CA  
5919 C C   . LEU E 189 ? 0.605 1.197 0.787 0.031  0.010  -0.108 518 LEU EEE C   
5920 O O   . LEU E 189 ? 0.566 1.167 0.712 0.024  0.009  -0.088 518 LEU EEE O   
5921 C CB  . LEU E 189 ? 0.620 1.210 0.787 0.026  0.012  -0.119 518 LEU EEE CB  
5922 C CG  . LEU E 189 ? 0.620 1.177 0.773 0.025  0.011  -0.106 518 LEU EEE CG  
5923 C CD1 . LEU E 189 ? 0.620 1.231 0.770 0.022  0.011  -0.137 518 LEU EEE CD1 
5924 C CD2 . LEU E 189 ? 0.618 1.125 0.824 0.034  0.014  -0.104 518 LEU EEE CD2 
5925 N N   . HIS E 190 ? 0.642 1.257 0.881 0.039  0.014  -0.146 519 HIS EEE N   
5926 C CA  . HIS E 190 ? 0.685 1.354 0.943 0.039  0.016  -0.173 519 HIS EEE CA  
5927 C C   . HIS E 190 ? 0.680 1.418 0.904 0.030  0.020  -0.190 519 HIS EEE C   
5928 O O   . HIS E 190 ? 0.701 1.492 0.957 0.034  0.023  -0.236 519 HIS EEE O   
5929 C CB  . HIS E 190 ? 0.736 1.413 1.076 0.051  0.018  -0.214 519 HIS EEE CB  
5930 C CG  . HIS E 190 ? 0.794 1.411 1.173 0.063  0.016  -0.191 519 HIS EEE CG  
5931 N ND1 . HIS E 190 ? 0.837 1.409 1.260 0.071  0.020  -0.184 519 HIS EEE ND1 
5932 C CD2 . HIS E 190 ? 0.837 1.439 1.223 0.072  0.013  -0.172 519 HIS EEE CD2 
5933 C CE1 . HIS E 190 ? 0.867 1.400 1.319 0.086  0.020  -0.156 519 HIS EEE CE1 
5934 N NE2 . HIS E 190 ? 0.869 1.421 1.297 0.087  0.014  -0.149 519 HIS EEE NE2 
5935 N N   . ALA E 191 ? 0.667 1.409 0.834 0.020  0.021  -0.153 520 ALA EEE N   
5936 C CA  . ALA E 191 ? 0.670 1.474 0.798 0.014  0.028  -0.151 520 ALA EEE CA  
5937 C C   . ALA E 191 ? 0.664 1.460 0.754 0.003  0.031  -0.104 520 ALA EEE C   
5938 O O   . ALA E 191 ? 0.642 1.380 0.730 -0.000 0.026  -0.079 520 ALA EEE O   
5939 C CB  . ALA E 191 ? 0.670 1.473 0.781 0.015  0.025  -0.154 520 ALA EEE CB  
5940 N N   . PRO E 192 ? 0.689 1.547 0.754 -0.002 0.042  -0.091 521 PRO EEE N   
5941 C CA  . PRO E 192 ? 0.690 1.539 0.735 -0.014 0.049  -0.045 521 PRO EEE CA  
5942 C C   . PRO E 192 ? 0.688 1.474 0.709 -0.019 0.042  -0.010 521 PRO EEE C   
5943 O O   . PRO E 192 ? 0.700 1.488 0.702 -0.015 0.039  -0.012 521 PRO EEE O   
5944 C CB  . PRO E 192 ? 0.697 1.633 0.722 -0.014 0.065  -0.034 521 PRO EEE CB  
5945 C CG  . PRO E 192 ? 0.703 1.704 0.743 -0.002 0.065  -0.088 521 PRO EEE CG  
5946 C CD  . PRO E 192 ? 0.688 1.635 0.747 0.005  0.050  -0.120 521 PRO EEE CD  
5947 N N   . ALA E 193 ? 0.686 1.425 0.716 -0.026 0.038  0.014  522 ALA EEE N   
5948 C CA  . ALA E 193 ? 0.676 1.363 0.691 -0.032 0.032  0.045  522 ALA EEE CA  
5949 C C   . ALA E 193 ? 0.690 1.410 0.693 -0.040 0.045  0.081  522 ALA EEE C   
5950 O O   . ALA E 193 ? 0.758 1.521 0.776 -0.045 0.059  0.095  522 ALA EEE O   
5951 C CB  . ALA E 193 ? 0.667 1.311 0.705 -0.035 0.024  0.049  522 ALA EEE CB  
5952 N N   . THR E 194 ? 0.664 1.366 0.643 -0.039 0.042  0.100  523 THR EEE N   
5953 C CA  . THR E 194 ? 0.675 1.409 0.642 -0.043 0.053  0.140  523 THR EEE CA  
5954 C C   . THR E 194 ? 0.661 1.337 0.637 -0.051 0.048  0.170  523 THR EEE C   
5955 O O   . THR E 194 ? 0.680 1.374 0.663 -0.055 0.060  0.211  523 THR EEE O   
5956 C CB  . THR E 194 ? 0.700 1.486 0.633 -0.031 0.055  0.130  523 THR EEE CB  
5957 O OG1 . THR E 194 ? 0.684 1.425 0.603 -0.028 0.041  0.120  523 THR EEE OG1 
5958 C CG2 . THR E 194 ? 0.699 1.541 0.634 -0.022 0.056  0.086  523 THR EEE CG2 
5959 N N   . VAL E 195 ? 0.643 1.258 0.624 -0.050 0.033  0.153  524 VAL EEE N   
5960 C CA  . VAL E 195 ? 0.638 1.201 0.631 -0.056 0.025  0.171  524 VAL EEE CA  
5961 C C   . VAL E 195 ? 0.624 1.159 0.653 -0.060 0.018  0.158  524 VAL EEE C   
5962 O O   . VAL E 195 ? 0.632 1.142 0.652 -0.052 0.006  0.130  524 VAL EEE O   
5963 C CB  . VAL E 195 ? 0.631 1.159 0.596 -0.049 0.013  0.160  524 VAL EEE CB  
5964 C CG1 . VAL E 195 ? 0.626 1.111 0.605 -0.054 0.006  0.177  524 VAL EEE CG1 
5965 C CG2 . VAL E 195 ? 0.645 1.209 0.579 -0.042 0.017  0.162  524 VAL EEE CG2 
5966 N N   . CYS E 196 ? 0.636 1.177 0.709 -0.071 0.027  0.177  525 CYS EEE N   
5967 C CA  . CYS E 196 ? 0.631 1.156 0.751 -0.076 0.020  0.160  525 CYS EEE CA  
5968 C C   . CYS E 196 ? 0.637 1.131 0.799 -0.083 0.016  0.172  525 CYS EEE C   
5969 O O   . CYS E 196 ? 0.633 1.127 0.802 -0.089 0.026  0.206  525 CYS EEE O   
5970 C CB  . CYS E 196 ? 0.632 1.198 0.787 -0.083 0.035  0.164  525 CYS EEE CB  
5971 S SG  . CYS E 196 ? 0.635 1.239 0.754 -0.073 0.037  0.138  525 CYS EEE SG  
5972 N N   . GLY E 197 ? 0.643 1.118 0.835 -0.081 0.001  0.142  526 GLY EEE N   
5973 C CA  . GLY E 197 ? 0.650 1.104 0.902 -0.088 -0.005 0.139  526 GLY EEE CA  
5974 C C   . GLY E 197 ? 0.660 1.132 0.992 -0.104 0.013  0.157  526 GLY EEE C   
5975 O O   . GLY E 197 ? 0.652 1.155 0.987 -0.107 0.026  0.164  526 GLY EEE O   
5976 N N   . PRO E 198 ? 0.692 1.147 1.098 -0.113 0.014  0.163  527 PRO EEE N   
5977 C CA  . PRO E 198 ? 0.743 1.212 1.240 -0.129 0.035  0.188  527 PRO EEE CA  
5978 C C   . PRO E 198 ? 0.774 1.267 1.321 -0.133 0.035  0.155  527 PRO EEE C   
5979 O O   . PRO E 198 ? 0.805 1.319 1.414 -0.146 0.057  0.181  527 PRO EEE O   
5980 C CB  . PRO E 198 ? 0.741 1.179 1.316 -0.136 0.032  0.189  527 PRO EEE CB  
5981 C CG  . PRO E 198 ? 0.714 1.132 1.247 -0.122 0.002  0.141  527 PRO EEE CG  
5982 C CD  . PRO E 198 ? 0.696 1.118 1.112 -0.109 -0.003 0.146  527 PRO EEE CD  
5983 N N   . LYS E 199 ? 0.803 1.298 1.325 -0.121 0.010  0.102  528 LYS EEE N   
5984 C CA  . LYS E 199 ? 0.833 1.355 1.397 -0.120 0.004  0.062  528 LYS EEE CA  
5985 C C   . LYS E 199 ? 0.833 1.380 1.333 -0.114 0.010  0.068  528 LYS EEE C   
5986 O O   . LYS E 199 ? 0.845 1.417 1.374 -0.112 0.005  0.037  528 LYS EEE O   
5987 C CB  . LYS E 199 ? 0.851 1.373 1.416 -0.104 -0.028 0.004  528 LYS EEE CB  
5988 C CG  . LYS E 199 ? 0.885 1.385 1.492 -0.104 -0.041 -0.014 528 LYS EEE CG  
5989 C CD  . LYS E 199 ? 0.933 1.424 1.655 -0.125 -0.024 0.002  528 LYS EEE CD  
5990 C CE  . LYS E 199 ? 0.962 1.437 1.741 -0.123 -0.039 -0.029 528 LYS EEE CE  
5991 N NZ  . LYS E 199 ? 0.991 1.454 1.900 -0.143 -0.021 -0.012 528 LYS EEE NZ  
5992 N N   . LYS E 200 ? 0.839 1.384 1.263 -0.110 0.019  0.100  529 LYS EEE N   
5993 C CA  . LYS E 200 ? 0.835 1.407 1.202 -0.103 0.025  0.101  529 LYS EEE CA  
5994 C C   . LYS E 200 ? 0.804 1.375 1.140 -0.086 0.002  0.057  529 LYS EEE C   
5995 O O   . LYS E 200 ? 0.778 1.360 1.062 -0.075 0.001  0.052  529 LYS EEE O   
5996 C CB  . LYS E 200 ? 0.863 1.475 1.279 -0.116 0.049  0.118  529 LYS EEE CB  
5997 C CG  . LYS E 200 ? 0.898 1.519 1.348 -0.130 0.077  0.172  529 LYS EEE CG  
5998 C CD  . LYS E 200 ? 0.914 1.577 1.424 -0.142 0.103  0.191  529 LYS EEE CD  
5999 C CE  . LYS E 200 ? 0.948 1.629 1.486 -0.152 0.134  0.256  529 LYS EEE CE  
6000 N NZ  . LYS E 200 ? 0.965 1.695 1.560 -0.162 0.164  0.279  529 LYS EEE NZ  
6001 N N   . GLN F 3   ? 1.215 1.108 1.105 0.037  -0.107 -0.015 3   GLN FFF N   
6002 C CA  . GLN F 3   ? 1.222 1.077 1.134 0.055  -0.126 -0.022 3   GLN FFF CA  
6003 C C   . GLN F 3   ? 1.157 1.060 1.051 0.050  -0.096 0.004  3   GLN FFF C   
6004 O O   . GLN F 3   ? 1.203 1.087 1.111 0.040  -0.119 0.029  3   GLN FFF O   
6005 C CB  . GLN F 3   ? 1.310 1.093 1.266 0.032  -0.195 0.006  3   GLN FFF CB  
6006 C CG  . GLN F 3   ? 1.379 1.099 1.381 0.055  -0.239 -0.047 3   GLN FFF CG  
6007 C CD  . GLN F 3   ? 1.415 1.133 1.406 0.025  -0.250 -0.036 3   GLN FFF CD  
6008 O OE1 . GLN F 3   ? 1.364 1.140 1.314 0.029  -0.203 -0.053 3   GLN FFF OE1 
6009 N NE2 . GLN F 3   ? 1.486 1.136 1.523 -0.010 -0.321 -0.001 3   GLN FFF NE2 
6010 N N   . VAL F 4   ? 1.056 1.017 0.929 0.055  -0.052 -0.004 4   VAL FFF N   
6011 C CA  . VAL F 4   ? 0.971 0.984 0.840 0.054  -0.026 0.002  4   VAL FFF CA  
6012 C C   . VAL F 4   ? 0.947 0.940 0.820 0.084  -0.020 -0.015 4   VAL FFF C   
6013 O O   . VAL F 4   ? 0.936 0.918 0.812 0.109  -0.016 -0.041 4   VAL FFF O   
6014 C CB  . VAL F 4   ? 0.900 0.970 0.776 0.058  0.002  -0.014 4   VAL FFF CB  
6015 C CG1 . VAL F 4   ? 0.872 0.927 0.758 0.084  0.010  -0.032 4   VAL FFF CG1 
6016 C CG2 . VAL F 4   ? 0.877 1.006 0.765 0.058  0.019  -0.025 4   VAL FFF CG2 
6017 N N   . GLN F 5   ? 0.929 0.939 0.803 0.076  -0.020 -0.000 5   GLN FFF N   
6018 C CA  . GLN F 5   ? 0.891 0.891 0.768 0.100  -0.015 -0.011 5   GLN FFF CA  
6019 C C   . GLN F 5   ? 0.800 0.844 0.678 0.109  0.015  -0.025 5   GLN FFF C   
6020 O O   . GLN F 5   ? 0.791 0.884 0.674 0.093  0.025  -0.027 5   GLN FFF O   
6021 C CB  . GLN F 5   ? 0.943 0.937 0.827 0.081  -0.040 0.021  5   GLN FFF CB  
6022 C CG  . GLN F 5   ? 0.969 0.948 0.865 0.107  -0.043 0.012  5   GLN FFF CG  
6023 C CD  . GLN F 5   ? 1.014 0.939 0.942 0.139  -0.073 -0.013 5   GLN FFF CD  
6024 O OE1 . GLN F 5   ? 1.022 0.965 0.955 0.172  -0.058 -0.052 5   GLN FFF OE1 
6025 N NE2 . GLN F 5   ? 1.068 0.940 1.030 0.125  -0.122 0.006  5   GLN FFF NE2 
6026 N N   . LEU F 6   ? 0.737 0.778 0.619 0.132  0.023  -0.038 6   LEU FFF N   
6027 C CA  . LEU F 6   ? 0.681 0.749 0.579 0.137  0.034  -0.042 6   LEU FFF CA  
6028 C C   . LEU F 6   ? 0.656 0.727 0.548 0.142  0.034  -0.038 6   LEU FFF C   
6029 O O   . LEU F 6   ? 0.670 0.731 0.556 0.156  0.028  -0.040 6   LEU FFF O   
6030 C CB  . LEU F 6   ? 0.670 0.751 0.578 0.141  0.032  -0.037 6   LEU FFF CB  
6031 C CG  . LEU F 6   ? 0.678 0.765 0.618 0.133  0.024  -0.032 6   LEU FFF CG  
6032 C CD1 . LEU F 6   ? 0.694 0.772 0.624 0.127  0.027  -0.040 6   LEU FFF CD1 
6033 C CD2 . LEU F 6   ? 0.677 0.793 0.625 0.122  0.012  -0.006 6   LEU FFF CD2 
6034 N N   . VAL F 7   ? 0.615 0.711 0.515 0.132  0.040  -0.042 7   VAL FFF N   
6035 C CA  . VAL F 7   ? 0.601 0.710 0.495 0.132  0.040  -0.036 7   VAL FFF CA  
6036 C C   . VAL F 7   ? 0.569 0.687 0.485 0.140  0.042  -0.044 7   VAL FFF C   
6037 O O   . VAL F 7   ? 0.550 0.678 0.501 0.138  0.039  -0.063 7   VAL FFF O   
6038 C CB  . VAL F 7   ? 0.608 0.763 0.495 0.106  0.041  -0.033 7   VAL FFF CB  
6039 C CG1 . VAL F 7   ? 0.613 0.789 0.493 0.101  0.039  -0.023 7   VAL FFF CG1 
6040 C CG2 . VAL F 7   ? 0.633 0.782 0.505 0.084  0.025  -0.004 7   VAL FFF CG2 
6041 N N   . GLU F 8   ? 0.574 0.693 0.482 0.148  0.041  -0.031 8   GLU FFF N   
6042 C CA  . GLU F 8   ? 0.571 0.706 0.499 0.146  0.034  -0.022 8   GLU FFF CA  
6043 C C   . GLU F 8   ? 0.580 0.731 0.504 0.144  0.036  -0.019 8   GLU FFF C   
6044 O O   . GLU F 8   ? 0.579 0.733 0.482 0.151  0.040  -0.016 8   GLU FFF O   
6045 C CB  . GLU F 8   ? 0.571 0.733 0.488 0.150  0.033  -0.008 8   GLU FFF CB  
6046 C CG  . GLU F 8   ? 0.569 0.769 0.506 0.131  0.018  0.022  8   GLU FFF CG  
6047 C CD  . GLU F 8   ? 0.575 0.850 0.496 0.124  0.019  0.034  8   GLU FFF CD  
6048 O OE1 . GLU F 8   ? 0.570 0.852 0.473 0.139  0.029  0.008  8   GLU FFF OE1 
6049 O OE2 . GLU F 8   ? 0.592 0.934 0.521 0.100  0.007  0.067  8   GLU FFF OE2 
6050 N N   . SER F 9   ? 0.374 0.926 0.415 0.053  -0.045 0.062  9   SER FFF N   
6051 C CA  . SER F 9   ? 0.417 1.010 0.475 0.049  -0.059 0.064  9   SER FFF CA  
6052 C C   . SER F 9   ? 0.407 1.012 0.471 0.037  -0.052 0.043  9   SER FFF C   
6053 O O   . SER F 9   ? 0.395 0.973 0.447 0.032  -0.036 0.030  9   SER FFF O   
6054 C CB  . SER F 9   ? 0.463 1.078 0.498 0.041  -0.076 0.077  9   SER FFF CB  
6055 O OG  . SER F 9   ? 0.520 1.129 0.519 0.027  -0.069 0.061  9   SER FFF OG  
6056 N N   . GLY F 10  ? 0.425 1.069 0.509 0.031  -0.064 0.043  10  GLY FFF N   
6057 C CA  . GLY F 10  ? 0.430 1.090 0.529 0.017  -0.060 0.026  10  GLY FFF CA  
6058 C C   . GLY F 10  ? 0.437 1.120 0.583 0.027  -0.055 0.030  10  GLY FFF C   
6059 O O   . GLY F 10  ? 0.470 1.164 0.638 0.045  -0.061 0.045  10  GLY FFF O   
6060 N N   . GLY F 11  ? 0.448 1.136 0.608 0.015  -0.043 0.018  11  GLY FFF N   
6061 C CA  . GLY F 11  ? 0.470 1.188 0.676 0.022  -0.034 0.020  11  GLY FFF CA  
6062 C C   . GLY F 11  ? 0.482 1.254 0.724 0.012  -0.050 0.023  11  GLY FFF C   
6063 O O   . GLY F 11  ? 0.518 1.296 0.745 -0.010 -0.061 0.014  11  GLY FFF O   
6064 N N   . GLY F 12  ? 0.490 1.301 0.779 0.028  -0.051 0.032  12  GLY FFF N   
6065 C CA  . GLY F 12  ? 0.491 1.365 0.826 0.021  -0.068 0.038  12  GLY FFF CA  
6066 C C   . GLY F 12  ? 0.490 1.393 0.859 0.007  -0.052 0.029  12  GLY FFF C   
6067 O O   . GLY F 12  ? 0.450 1.323 0.806 0.005  -0.027 0.021  12  GLY FFF O   
6068 N N   . LEU F 13  ? 0.521 1.483 0.933 -0.006 -0.067 0.033  13  LEU FFF N   
6069 C CA  . LEU F 13  ? 0.516 1.518 0.969 -0.024 -0.054 0.028  13  LEU FFF CA  
6070 C C   . LEU F 13  ? 0.517 1.504 0.945 -0.062 -0.062 0.016  13  LEU FFF C   
6071 O O   . LEU F 13  ? 0.539 1.520 0.941 -0.073 -0.086 0.012  13  LEU FFF O   
6072 C CB  . LEU F 13  ? 0.560 1.641 1.081 -0.017 -0.067 0.039  13  LEU FFF CB  
6073 C CG  . LEU F 13  ? 0.590 1.686 1.140 0.023  -0.073 0.053  13  LEU FFF CG  
6074 C CD1 . LEU F 13  ? 0.596 1.776 1.222 0.030  -0.086 0.065  13  LEU FFF CD1 
6075 C CD2 . LEU F 13  ? 0.587 1.647 1.132 0.050  -0.042 0.048  13  LEU FFF CD2 
6076 N N   . VAL F 14  ? 0.522 1.503 0.956 -0.082 -0.042 0.011  14  VAL FFF N   
6077 C CA  . VAL F 14  ? 0.558 1.525 0.982 -0.121 -0.049 0.001  14  VAL FFF CA  
6078 C C   . VAL F 14  ? 0.574 1.575 1.041 -0.141 -0.031 0.006  14  VAL FFF C   
6079 O O   . VAL F 14  ? 0.573 1.591 1.058 -0.124 -0.006 0.013  14  VAL FFF O   
6080 C CB  . VAL F 14  ? 0.565 1.453 0.928 -0.125 -0.044 -0.010 14  VAL FFF CB  
6081 C CG1 . VAL F 14  ? 0.571 1.424 0.918 -0.118 -0.015 -0.005 14  VAL FFF CG1 
6082 C CG2 . VAL F 14  ? 0.587 1.454 0.938 -0.160 -0.058 -0.024 14  VAL FFF CG2 
6083 N N   . LYS F 15  ? 0.588 1.601 1.070 -0.178 -0.043 0.001  15  LYS FFF N   
6084 C CA  . LYS F 15  ? 0.607 1.651 1.129 -0.206 -0.028 0.009  15  LYS FFF CA  
6085 C C   . LYS F 15  ? 0.601 1.584 1.087 -0.214 -0.004 0.011  15  LYS FFF C   
6086 O O   . LYS F 15  ? 0.640 1.555 1.074 -0.206 -0.007 0.003  15  LYS FFF O   
6087 C CB  . LYS F 15  ? 0.650 1.714 1.195 -0.247 -0.052 0.002  15  LYS FFF CB  
6088 C CG  . LYS F 15  ? 0.661 1.794 1.244 -0.246 -0.080 0.002  15  LYS FFF CG  
6089 C CD  . LYS F 15  ? 0.694 1.849 1.301 -0.291 -0.104 -0.007 15  LYS FFF CD  
6090 C CE  . LYS F 15  ? 0.685 1.917 1.332 -0.292 -0.134 -0.005 15  LYS FFF CE  
6091 N NZ  . LYS F 15  ? 0.718 1.963 1.378 -0.338 -0.162 -0.018 15  LYS FFF NZ  
6092 N N   . THR F 16  ? 0.582 1.594 1.096 -0.228 0.019  0.024  16  THR FFF N   
6093 C CA  . THR F 16  ? 0.587 1.550 1.071 -0.243 0.040  0.033  16  THR FFF CA  
6094 C C   . THR F 16  ? 0.598 1.498 1.059 -0.273 0.021  0.026  16  THR FFF C   
6095 O O   . THR F 16  ? 0.634 1.554 1.124 -0.301 0.002  0.021  16  THR FFF O   
6096 C CB  . THR F 16  ? 0.605 1.624 1.129 -0.262 0.065  0.050  16  THR FFF CB  
6097 O OG1 . THR F 16  ? 0.595 1.672 1.143 -0.230 0.084  0.050  16  THR FFF OG1 
6098 C CG2 . THR F 16  ? 0.621 1.595 1.114 -0.280 0.084  0.064  16  THR FFF CG2 
6099 N N   . GLY F 17  ? 0.585 1.410 0.996 -0.266 0.026  0.025  17  GLY FFF N   
6100 C CA  . GLY F 17  ? 0.600 1.356 0.987 -0.286 0.010  0.016  17  GLY FFF CA  
6101 C C   . GLY F 17  ? 0.582 1.307 0.939 -0.267 -0.011 -0.008 17  GLY FFF C   
6102 O O   . GLY F 17  ? 0.597 1.261 0.930 -0.277 -0.022 -0.021 17  GLY FFF O   
6103 N N   . GLY F 18  ? 0.550 1.316 0.908 -0.241 -0.016 -0.013 18  GLY FFF N   
6104 C CA  . GLY F 18  ? 0.554 1.304 0.884 -0.225 -0.036 -0.032 18  GLY FFF CA  
6105 C C   . GLY F 18  ? 0.547 1.243 0.828 -0.197 -0.027 -0.034 18  GLY FFF C   
6106 O O   . GLY F 18  ? 0.548 1.219 0.819 -0.192 -0.007 -0.021 18  GLY FFF O   
6107 N N   . SER F 19  ? 0.547 1.232 0.800 -0.182 -0.040 -0.048 19  SER FFF N   
6108 C CA  . SER F 19  ? 0.533 1.168 0.741 -0.159 -0.035 -0.053 19  SER FFF CA  
6109 C C   . SER F 19  ? 0.506 1.168 0.702 -0.132 -0.040 -0.050 19  SER FFF C   
6110 O O   . SER F 19  ? 0.510 1.216 0.721 -0.135 -0.056 -0.052 19  SER FFF O   
6111 C CB  . SER F 19  ? 0.564 1.152 0.747 -0.170 -0.045 -0.074 19  SER FFF CB  
6112 O OG  . SER F 19  ? 0.585 1.127 0.772 -0.185 -0.036 -0.072 19  SER FFF OG  
6113 N N   . LEU F 20  ? 0.492 1.125 0.661 -0.109 -0.028 -0.043 20  LEU FFF N   
6114 C CA  . LEU F 20  ? 0.479 1.123 0.631 -0.084 -0.032 -0.038 20  LEU FFF CA  
6115 C C   . LEU F 20  ? 0.466 1.062 0.579 -0.072 -0.025 -0.042 20  LEU FFF C   
6116 O O   . LEU F 20  ? 0.449 1.008 0.554 -0.078 -0.015 -0.044 20  LEU FFF O   
6117 C CB  . LEU F 20  ? 0.466 1.140 0.644 -0.067 -0.022 -0.022 20  LEU FFF CB  
6118 C CG  . LEU F 20  ? 0.492 1.226 0.714 -0.071 -0.031 -0.017 20  LEU FFF CG  
6119 C CD1 . LEU F 20  ? 0.491 1.249 0.741 -0.051 -0.016 -0.005 20  LEU FFF CD1 
6120 C CD2 . LEU F 20  ? 0.505 1.265 0.723 -0.068 -0.055 -0.017 20  LEU FFF CD2 
6121 N N   . ARG F 21  ? 0.475 1.074 0.567 -0.056 -0.031 -0.039 21  ARG FFF N   
6122 C CA  . ARG F 21  ? 0.483 1.047 0.541 -0.044 -0.026 -0.041 21  ARG FFF CA  
6123 C C   . ARG F 21  ? 0.484 1.058 0.537 -0.024 -0.026 -0.026 21  ARG FFF C   
6124 O O   . ARG F 21  ? 0.548 1.148 0.597 -0.021 -0.039 -0.021 21  ARG FFF O   
6125 C CB  . ARG F 21  ? 0.511 1.071 0.545 -0.052 -0.036 -0.060 21  ARG FFF CB  
6126 C CG  . ARG F 21  ? 0.520 1.054 0.524 -0.040 -0.030 -0.063 21  ARG FFF CG  
6127 C CD  . ARG F 21  ? 0.575 1.111 0.556 -0.049 -0.037 -0.086 21  ARG FFF CD  
6128 N NE  . ARG F 21  ? 0.609 1.158 0.561 -0.039 -0.038 -0.085 21  ARG FFF NE  
6129 C CZ  . ARG F 21  ? 0.613 1.194 0.558 -0.034 -0.047 -0.067 21  ARG FFF CZ  
6130 N NH1 . ARG F 21  ? 0.646 1.248 0.615 -0.033 -0.055 -0.049 21  ARG FFF NH1 
6131 N NH2 . ARG F 21  ? 0.610 1.203 0.527 -0.030 -0.047 -0.064 21  ARG FFF NH2 
6132 N N   . LEU F 22  ? 0.475 1.029 0.529 -0.013 -0.012 -0.017 22  LEU FFF N   
6133 C CA  . LEU F 22  ? 0.460 1.010 0.507 0.005  -0.011 -0.004 22  LEU FFF CA  
6134 C C   . LEU F 22  ? 0.464 0.992 0.479 0.006  -0.013 -0.006 22  LEU FFF C   
6135 O O   . LEU F 22  ? 0.452 0.962 0.454 -0.001 -0.009 -0.017 22  LEU FFF O   
6136 C CB  . LEU F 22  ? 0.459 0.994 0.514 0.012  0.004  -0.000 22  LEU FFF CB  
6137 C CG  . LEU F 22  ? 0.466 1.030 0.555 0.019  0.008  0.003  22  LEU FFF CG  
6138 C CD1 . LEU F 22  ? 0.475 1.073 0.588 0.005  0.001  -0.001 22  LEU FFF CD1 
6139 C CD2 . LEU F 22  ? 0.469 1.020 0.558 0.021  0.026  0.001  22  LEU FFF CD2 
6140 N N   . SER F 23  ? 0.455 0.987 0.462 0.016  -0.019 0.007  23  SER FFF N   
6141 C CA  . SER F 23  ? 0.447 0.965 0.426 0.018  -0.019 0.010  23  SER FFF CA  
6142 C C   . SER F 23  ? 0.433 0.932 0.412 0.029  -0.015 0.024  23  SER FFF C   
6143 O O   . SER F 23  ? 0.402 0.906 0.400 0.037  -0.019 0.033  23  SER FFF O   
6144 C CB  . SER F 23  ? 0.470 1.016 0.436 0.014  -0.031 0.013  23  SER FFF CB  
6145 O OG  . SER F 23  ? 0.526 1.079 0.479 0.003  -0.032 -0.007 23  SER FFF OG  
6146 N N   . CYS F 24  ? 0.448 0.927 0.410 0.028  -0.009 0.023  24  CYS FFF N   
6147 C CA  . CYS F 24  ? 0.445 0.903 0.403 0.034  -0.007 0.035  24  CYS FFF CA  
6148 C C   . CYS F 24  ? 0.420 0.882 0.359 0.029  -0.008 0.041  24  CYS FFF C   
6149 O O   . CYS F 24  ? 0.391 0.852 0.322 0.026  -0.001 0.030  24  CYS FFF O   
6150 C CB  . CYS F 24  ? 0.437 0.871 0.397 0.035  0.003  0.029  24  CYS FFF CB  
6151 S SG  . CYS F 24  ? 0.502 0.910 0.460 0.040  0.002  0.038  24  CYS FFF SG  
6152 N N   . ALA F 25  ? 0.419 0.885 0.355 0.030  -0.015 0.058  25  ALA FFF N   
6153 C CA  . ALA F 25  ? 0.434 0.913 0.354 0.023  -0.015 0.068  25  ALA FFF CA  
6154 C C   . ALA F 25  ? 0.435 0.891 0.358 0.022  -0.016 0.083  25  ALA FFF C   
6155 O O   . ALA F 25  ? 0.433 0.869 0.369 0.028  -0.022 0.091  25  ALA FFF O   
6156 C CB  . ALA F 25  ? 0.446 0.955 0.356 0.019  -0.024 0.079  25  ALA FFF CB  
6157 N N   . ALA F 26  ? 0.433 0.894 0.347 0.016  -0.011 0.086  26  ALA FFF N   
6158 C CA  . ALA F 26  ? 0.458 0.903 0.376 0.010  -0.013 0.100  26  ALA FFF CA  
6159 C C   . ALA F 26  ? 0.458 0.932 0.367 0.001  -0.008 0.108  26  ALA FFF C   
6160 O O   . ALA F 26  ? 0.451 0.946 0.355 0.004  0.001  0.092  26  ALA FFF O   
6161 C CB  . ALA F 26  ? 0.453 0.870 0.376 0.012  -0.009 0.087  26  ALA FFF CB  
6162 N N   . SER F 27  ? 0.466 0.942 0.375 -0.009 -0.013 0.132  27  SER FFF N   
6163 C CA  . SER F 27  ? 0.494 1.009 0.394 -0.020 -0.007 0.144  27  SER FFF CA  
6164 C C   . SER F 27  ? 0.465 0.992 0.373 -0.021 0.003  0.132  27  SER FFF C   
6165 O O   . SER F 27  ? 0.429 0.928 0.348 -0.020 0.000  0.128  27  SER FFF O   
6166 C CB  . SER F 27  ? 0.531 1.044 0.433 -0.034 -0.017 0.177  27  SER FFF CB  
6167 O OG  . SER F 27  ? 0.554 1.035 0.471 -0.040 -0.021 0.182  27  SER FFF OG  
6168 N N   . GLY F 28  ? 0.460 1.029 0.361 -0.021 0.015  0.125  28  GLY FFF N   
6169 C CA  . GLY F 28  ? 0.461 1.054 0.375 -0.021 0.026  0.119  28  GLY FFF CA  
6170 C C   . GLY F 28  ? 0.444 1.011 0.373 -0.010 0.026  0.101  28  GLY FFF C   
6171 O O   . GLY F 28  ? 0.391 0.942 0.316 0.002  0.027  0.081  28  GLY FFF O   
6172 N N   . ARG F 29  ? 0.452 1.018 0.399 -0.016 0.023  0.109  29  ARG FFF N   
6173 C CA  . ARG F 29  ? 0.463 1.019 0.426 -0.007 0.023  0.097  29  ARG FFF CA  
6174 C C   . ARG F 29  ? 0.434 0.944 0.391 -0.007 0.012  0.094  29  ARG FFF C   
6175 O O   . ARG F 29  ? 0.435 0.936 0.401 -0.003 0.009  0.089  29  ARG FFF O   
6176 C CB  . ARG F 29  ? 0.501 1.088 0.486 -0.016 0.024  0.110  29  ARG FFF CB  
6177 C CG  . ARG F 29  ? 0.565 1.207 0.558 -0.016 0.039  0.112  29  ARG FFF CG  
6178 C CD  . ARG F 29  ? 0.621 1.300 0.638 -0.029 0.040  0.129  29  ARG FFF CD  
6179 N NE  . ARG F 29  ? 0.712 1.449 0.733 -0.031 0.057  0.132  29  ARG FFF NE  
6180 C CZ  . ARG F 29  ? 0.759 1.518 0.764 -0.046 0.061  0.149  29  ARG FFF CZ  
6181 N NH1 . ARG F 29  ? 0.781 1.501 0.766 -0.060 0.047  0.167  29  ARG FFF NH1 
6182 N NH2 . ARG F 29  ? 0.791 1.609 0.798 -0.048 0.079  0.150  29  ARG FFF NH2 
6183 N N   . THR F 30  ? 0.419 0.902 0.362 -0.010 0.006  0.097  30  THR FFF N   
6184 C CA  . THR F 30  ? 0.408 0.851 0.346 -0.009 -0.002 0.092  30  THR FFF CA  
6185 C C   . THR F 30  ? 0.394 0.828 0.332 0.002  0.002  0.076  30  THR FFF C   
6186 O O   . THR F 30  ? 0.373 0.794 0.311 -0.001 -0.003 0.075  30  THR FFF O   
6187 C CB  . THR F 30  ? 0.413 0.837 0.343 -0.008 -0.005 0.095  30  THR FFF CB  
6188 O OG1 . THR F 30  ? 0.430 0.856 0.362 -0.019 -0.011 0.115  30  THR FFF OG1 
6189 C CG2 . THR F 30  ? 0.406 0.794 0.333 -0.004 -0.009 0.085  30  THR FFF CG2 
6190 N N   . PHE F 31  ? 0.379 0.820 0.314 0.011  0.008  0.065  31  PHE FFF N   
6191 C CA  . PHE F 31  ? 0.379 0.808 0.315 0.019  0.011  0.052  31  PHE FFF CA  
6192 C C   . PHE F 31  ? 0.378 0.817 0.327 0.023  0.013  0.052  31  PHE FFF C   
6193 O O   . PHE F 31  ? 0.375 0.798 0.327 0.027  0.011  0.048  31  PHE FFF O   
6194 C CB  . PHE F 31  ? 0.369 0.801 0.301 0.024  0.016  0.041  31  PHE FFF CB  
6195 C CG  . PHE F 31  ? 0.388 0.810 0.314 0.023  0.013  0.041  31  PHE FFF CG  
6196 C CD1 . PHE F 31  ? 0.391 0.790 0.315 0.022  0.010  0.043  31  PHE FFF CD1 
6197 C CD2 . PHE F 31  ? 0.389 0.828 0.311 0.023  0.012  0.039  31  PHE FFF CD2 
6198 C CE1 . PHE F 31  ? 0.384 0.778 0.309 0.024  0.008  0.042  31  PHE FFF CE1 
6199 C CE2 . PHE F 31  ? 0.388 0.821 0.310 0.024  0.007  0.042  31  PHE FFF CE2 
6200 C CZ  . PHE F 31  ? 0.389 0.799 0.316 0.026  0.006  0.043  31  PHE FFF CZ  
6201 N N   . SER F 32  ? 0.383 0.850 0.343 0.023  0.016  0.057  32  SER FFF N   
6202 C CA  . SER F 32  ? 0.391 0.877 0.374 0.029  0.017  0.058  32  SER FFF CA  
6203 C C   . SER F 32  ? 0.373 0.855 0.361 0.021  0.006  0.072  32  SER FFF C   
6204 O O   . SER F 32  ? 0.361 0.857 0.369 0.026  0.003  0.076  32  SER FFF O   
6205 C CB  . SER F 32  ? 0.398 0.924 0.393 0.033  0.027  0.056  32  SER FFF CB  
6206 O OG  . SER F 32  ? 0.434 0.965 0.426 0.043  0.037  0.037  32  SER FFF OG  
6207 N N   . THR F 33  ? 0.373 0.838 0.345 0.008  -0.001 0.078  33  THR FFF N   
6208 C CA  . THR F 33  ? 0.383 0.843 0.354 -0.005 -0.013 0.088  33  THR FFF CA  
6209 C C   . THR F 33  ? 0.407 0.833 0.357 -0.008 -0.020 0.082  33  THR FFF C   
6210 O O   . THR F 33  ? 0.415 0.840 0.363 -0.014 -0.030 0.087  33  THR FFF O   
6211 C CB  . THR F 33  ? 0.394 0.857 0.364 -0.020 -0.017 0.097  33  THR FFF CB  
6212 O OG1 . THR F 33  ? 0.382 0.883 0.369 -0.018 -0.008 0.103  33  THR FFF OG1 
6213 C CG2 . THR F 33  ? 0.406 0.867 0.379 -0.036 -0.031 0.105  33  THR FFF CG2 
6214 N N   . TYR F 34  ? 0.395 0.799 0.330 -0.004 -0.014 0.073  34  TYR FFF N   
6215 C CA  . TYR F 34  ? 0.416 0.793 0.330 -0.007 -0.016 0.066  34  TYR FFF CA  
6216 C C   . TYR F 34  ? 0.425 0.795 0.336 0.003  -0.007 0.058  34  TYR FFF C   
6217 O O   . TYR F 34  ? 0.409 0.783 0.326 0.009  -0.001 0.054  34  TYR FFF O   
6218 C CB  . TYR F 34  ? 0.433 0.791 0.339 -0.013 -0.017 0.062  34  TYR FFF CB  
6219 C CG  . TYR F 34  ? 0.452 0.811 0.363 -0.026 -0.027 0.070  34  TYR FFF CG  
6220 C CD1 . TYR F 34  ? 0.468 0.827 0.374 -0.038 -0.037 0.071  34  TYR FFF CD1 
6221 C CD2 . TYR F 34  ? 0.450 0.814 0.372 -0.029 -0.026 0.079  34  TYR FFF CD2 
6222 C CE1 . TYR F 34  ? 0.491 0.853 0.405 -0.053 -0.047 0.079  34  TYR FFF CE1 
6223 C CE2 . TYR F 34  ? 0.471 0.836 0.400 -0.044 -0.035 0.089  34  TYR FFF CE2 
6224 C CZ  . TYR F 34  ? 0.505 0.868 0.432 -0.057 -0.046 0.088  34  TYR FFF CZ  
6225 O OH  . TYR F 34  ? 0.547 0.912 0.484 -0.075 -0.056 0.098  34  TYR FFF OH  
6226 N N   . SER F 35  ? 0.426 0.789 0.329 0.002  -0.008 0.059  35  SER FFF N   
6227 C CA  . SER F 35  ? 0.442 0.797 0.341 0.006  -0.001 0.054  35  SER FFF CA  
6228 C C   . SER F 35  ? 0.437 0.784 0.329 0.007  0.006  0.043  35  SER FFF C   
6229 O O   . SER F 35  ? 0.446 0.785 0.329 0.003  0.004  0.039  35  SER FFF O   
6230 C CB  . SER F 35  ? 0.453 0.802 0.339 0.000  -0.004 0.061  35  SER FFF CB  
6231 O OG  . SER F 35  ? 0.472 0.829 0.372 0.003  -0.012 0.073  35  SER FFF OG  
6232 N N   . MET F 36  ? 0.406 0.756 0.307 0.012  0.013  0.038  36  MET FFF N   
6233 C CA  . MET F 36  ? 0.418 0.768 0.321 0.015  0.018  0.030  36  MET FFF CA  
6234 C C   . MET F 36  ? 0.406 0.756 0.305 0.012  0.026  0.026  36  MET FFF C   
6235 O O   . MET F 36  ? 0.388 0.736 0.286 0.008  0.026  0.032  36  MET FFF O   
6236 C CB  . MET F 36  ? 0.397 0.759 0.313 0.020  0.018  0.029  36  MET FFF CB  
6237 C CG  . MET F 36  ? 0.408 0.776 0.333 0.020  0.021  0.025  36  MET FFF CG  
6238 S SD  . MET F 36  ? 0.472 0.843 0.404 0.018  0.027  0.019  36  MET FFF SD  
6239 C CE  . MET F 36  ? 0.485 0.867 0.422 0.024  0.026  0.016  36  MET FFF CE  
6240 N N   . GLY F 37  ? 0.406 0.757 0.305 0.015  0.032  0.019  37  GLY FFF N   
6241 C CA  . GLY F 37  ? 0.431 0.790 0.330 0.012  0.043  0.014  37  GLY FFF CA  
6242 C C   . GLY F 37  ? 0.413 0.787 0.333 0.019  0.048  0.008  37  GLY FFF C   
6243 O O   . GLY F 37  ? 0.407 0.779 0.335 0.027  0.044  0.004  37  GLY FFF O   
6244 N N   . TRP F 38  ? 0.408 0.797 0.340 0.014  0.054  0.008  38  TRP FFF N   
6245 C CA  . TRP F 38  ? 0.417 0.828 0.372 0.018  0.060  0.002  38  TRP FFF CA  
6246 C C   . TRP F 38  ? 0.424 0.847 0.375 0.017  0.075  -0.004 38  TRP FFF C   
6247 O O   . TRP F 38  ? 0.441 0.864 0.376 0.005  0.081  0.001  38  TRP FFF O   
6248 C CB  . TRP F 38  ? 0.429 0.854 0.402 0.011  0.056  0.005  38  TRP FFF CB  
6249 C CG  . TRP F 38  ? 0.419 0.840 0.395 0.013  0.044  0.006  38  TRP FFF CG  
6250 C CD1 . TRP F 38  ? 0.436 0.842 0.403 0.008  0.038  0.007  38  TRP FFF CD1 
6251 C CD2 . TRP F 38  ? 0.422 0.857 0.410 0.021  0.036  0.004  38  TRP FFF CD2 
6252 N NE1 . TRP F 38  ? 0.443 0.855 0.413 0.012  0.030  0.004  38  TRP FFF NE1 
6253 C CE2 . TRP F 38  ? 0.446 0.876 0.426 0.019  0.027  0.004  38  TRP FFF CE2 
6254 C CE3 . TRP F 38  ? 0.428 0.881 0.435 0.031  0.035  0.004  38  TRP FFF CE3 
6255 C CZ2 . TRP F 38  ? 0.445 0.891 0.429 0.023  0.017  0.006  38  TRP FFF CZ2 
6256 C CZ3 . TRP F 38  ? 0.437 0.902 0.452 0.036  0.023  0.009  38  TRP FFF CZ3 
6257 C CH2 . TRP F 38  ? 0.435 0.897 0.435 0.030  0.014  0.010  38  TRP FFF CH2 
6258 N N   . PHE F 39  ? 0.428 0.861 0.394 0.030  0.081  -0.014 39  PHE FFF N   
6259 C CA  . PHE F 39  ? 0.447 0.899 0.416 0.033  0.099  -0.026 39  PHE FFF CA  
6260 C C   . PHE F 39  ? 0.447 0.932 0.457 0.043  0.103  -0.029 39  PHE FFF C   
6261 O O   . PHE F 39  ? 0.432 0.920 0.463 0.048  0.090  -0.023 39  PHE FFF O   
6262 C CB  . PHE F 39  ? 0.472 0.902 0.424 0.044  0.102  -0.040 39  PHE FFF CB  
6263 C CG  . PHE F 39  ? 0.501 0.907 0.414 0.032  0.097  -0.038 39  PHE FFF CG  
6264 C CD1 . PHE F 39  ? 0.487 0.869 0.392 0.029  0.079  -0.027 39  PHE FFF CD1 
6265 C CD2 . PHE F 39  ? 0.535 0.946 0.418 0.024  0.109  -0.046 39  PHE FFF CD2 
6266 C CE1 . PHE F 39  ? 0.515 0.880 0.389 0.019  0.073  -0.024 39  PHE FFF CE1 
6267 C CE2 . PHE F 39  ? 0.561 0.953 0.409 0.012  0.101  -0.042 39  PHE FFF CE2 
6268 C CZ  . PHE F 39  ? 0.541 0.910 0.386 0.010  0.082  -0.030 39  PHE FFF CZ  
6269 N N   . ARG F 40  ? 0.468 0.983 0.488 0.043  0.122  -0.038 40  ARG FFF N   
6270 C CA  . ARG F 40  ? 0.471 1.027 0.538 0.053  0.129  -0.042 40  ARG FFF CA  
6271 C C   . ARG F 40  ? 0.493 1.066 0.565 0.067  0.152  -0.061 40  ARG FFF C   
6272 O O   . ARG F 40  ? 0.507 1.074 0.544 0.058  0.165  -0.068 40  ARG FFF O   
6273 C CB  . ARG F 40  ? 0.468 1.055 0.551 0.034  0.131  -0.029 40  ARG FFF CB  
6274 C CG  . ARG F 40  ? 0.493 1.098 0.559 0.016  0.150  -0.027 40  ARG FFF CG  
6275 C CD  . ARG F 40  ? 0.496 1.120 0.579 -0.006 0.145  -0.011 40  ARG FFF CD  
6276 N NE  . ARG F 40  ? 0.516 1.154 0.583 -0.028 0.161  -0.002 40  ARG FFF NE  
6277 C CZ  . ARG F 40  ? 0.530 1.178 0.610 -0.052 0.158  0.014  40  ARG FFF CZ  
6278 N NH1 . ARG F 40  ? 0.513 1.160 0.620 -0.057 0.141  0.017  40  ARG FFF NH1 
6279 N NH2 . ARG F 40  ? 0.561 1.222 0.625 -0.073 0.173  0.027  40  ARG FFF NH2 
6280 N N   . GLN F 41  ? 0.516 1.113 0.633 0.088  0.155  -0.069 41  GLN FFF N   
6281 C CA  . GLN F 41  ? 0.556 1.174 0.691 0.107  0.177  -0.092 41  GLN FFF CA  
6282 C C   . GLN F 41  ? 0.565 1.242 0.761 0.117  0.185  -0.090 41  GLN FFF C   
6283 O O   . GLN F 41  ? 0.563 1.244 0.797 0.131  0.167  -0.081 41  GLN FFF O   
6284 C CB  . GLN F 41  ? 0.578 1.153 0.713 0.131  0.170  -0.107 41  GLN FFF CB  
6285 C CG  . GLN F 41  ? 0.617 1.201 0.762 0.151  0.195  -0.137 41  GLN FFF CG  
6286 C CD  . GLN F 41  ? 0.643 1.170 0.770 0.165  0.188  -0.155 41  GLN FFF CD  
6287 O OE1 . GLN F 41  ? 0.637 1.119 0.739 0.156  0.166  -0.142 41  GLN FFF OE1 
6288 N NE2 . GLN F 41  ? 0.702 1.231 0.844 0.186  0.207  -0.186 41  GLN FFF NE2 
6289 N N   . ALA F 42  ? 0.595 1.320 0.798 0.107  0.210  -0.096 42  ALA FFF N   
6290 C CA  . ALA F 42  ? 0.606 1.398 0.870 0.116  0.223  -0.097 42  ALA FFF CA  
6291 C C   . ALA F 42  ? 0.646 1.451 0.939 0.150  0.242  -0.125 42  ALA FFF C   
6292 O O   . ALA F 42  ? 0.654 1.424 0.909 0.157  0.253  -0.146 42  ALA FFF O   
6293 C CB  . ALA F 42  ? 0.619 1.457 0.878 0.088  0.241  -0.088 42  ALA FFF CB  
6294 N N   . PRO F 43  ? 0.646 1.502 1.009 0.171  0.247  -0.127 43  PRO FFF N   
6295 C CA  . PRO F 43  ? 0.683 1.550 1.083 0.208  0.265  -0.155 43  PRO FFF CA  
6296 C C   . PRO F 43  ? 0.726 1.602 1.089 0.207  0.301  -0.185 43  PRO FFF C   
6297 O O   . PRO F 43  ? 0.692 1.620 1.048 0.186  0.323  -0.182 43  PRO FFF O   
6298 C CB  . PRO F 43  ? 0.676 1.619 1.157 0.222  0.269  -0.147 43  PRO FFF CB  
6299 C CG  . PRO F 43  ? 0.635 1.614 1.113 0.184  0.260  -0.120 43  PRO FFF CG  
6300 C CD  . PRO F 43  ? 0.613 1.521 1.025 0.161  0.235  -0.105 43  PRO FFF CD  
6301 N N   . GLY F 44  ? 0.781 1.603 1.116 0.225  0.305  -0.211 44  GLY FFF N   
6302 C CA  . GLY F 44  ? 0.856 1.680 1.151 0.227  0.337  -0.247 44  GLY FFF CA  
6303 C C   . GLY F 44  ? 0.875 1.694 1.095 0.188  0.343  -0.238 44  GLY FFF C   
6304 O O   . GLY F 44  ? 0.913 1.785 1.118 0.176  0.374  -0.248 44  GLY FFF O   
6305 N N   . LYS F 45  ? 0.866 1.627 1.040 0.168  0.314  -0.217 45  LYS FFF N   
6306 C CA  . LYS F 45  ? 0.879 1.624 0.982 0.133  0.313  -0.204 45  LYS FFF CA  
6307 C C   . LYS F 45  ? 0.902 1.571 0.961 0.129  0.285  -0.202 45  LYS FFF C   
6308 O O   . LYS F 45  ? 0.893 1.524 0.980 0.151  0.267  -0.205 45  LYS FFF O   
6309 C CB  . LYS F 45  ? 0.842 1.618 0.953 0.105  0.304  -0.167 45  LYS FFF CB  
6310 C CG  . LYS F 45  ? 0.872 1.725 1.006 0.093  0.333  -0.164 45  LYS FFF CG  
6311 C CD  . LYS F 45  ? 0.853 1.725 0.990 0.060  0.322  -0.127 45  LYS FFF CD  
6312 C CE  . LYS F 45  ? 0.875 1.711 0.944 0.030  0.313  -0.108 45  LYS FFF CE  
6313 N NZ  . LYS F 45  ? 0.847 1.678 0.924 0.004  0.293  -0.074 45  LYS FFF NZ  
6314 N N   . GLU F 46  ? 0.952 1.603 0.948 0.102  0.282  -0.193 46  GLU FFF N   
6315 C CA  . GLU F 46  ? 0.997 1.585 0.951 0.094  0.257  -0.188 46  GLU FFF CA  
6316 C C   . GLU F 46  ? 0.892 1.461 0.860 0.083  0.228  -0.152 46  GLU FFF C   
6317 O O   . GLU F 46  ? 0.847 1.452 0.837 0.072  0.230  -0.131 46  GLU FFF O   
6318 C CB  . GLU F 46  ? 1.129 1.714 1.014 0.070  0.264  -0.193 46  GLU FFF CB  
6319 C CG  . GLU F 46  ? 1.229 1.755 1.073 0.063  0.241  -0.194 46  GLU FFF CG  
6320 C CD  . GLU F 46  ? 1.307 1.793 1.160 0.086  0.238  -0.227 46  GLU FFF CD  
6321 O OE1 . GLU F 46  ? 1.372 1.865 1.208 0.094  0.260  -0.263 46  GLU FFF OE1 
6322 O OE2 . GLU F 46  ? 1.281 1.725 1.155 0.094  0.214  -0.217 46  GLU FFF OE2 
6323 N N   . ARG F 47  ? 0.735 1.212 0.846 0.151  0.160  -0.082 47  ARG FFF N   
6324 C CA  . ARG F 47  ? 0.703 1.175 0.816 0.133  0.143  -0.065 47  ARG FFF CA  
6325 C C   . ARG F 47  ? 0.659 1.127 0.740 0.111  0.143  -0.063 47  ARG FFF C   
6326 O O   . ARG F 47  ? 0.663 1.097 0.714 0.106  0.139  -0.070 47  ARG FFF O   
6327 C CB  . ARG F 47  ? 0.736 1.166 0.845 0.136  0.127  -0.063 47  ARG FFF CB  
6328 C CG  . ARG F 47  ? 0.732 1.173 0.872 0.142  0.115  -0.046 47  ARG FFF CG  
6329 C CD  . ARG F 47  ? 0.763 1.163 0.901 0.146  0.102  -0.043 47  ARG FFF CD  
6330 N NE  . ARG F 47  ? 0.820 1.221 0.987 0.168  0.101  -0.037 47  ARG FFF NE  
6331 C CZ  . ARG F 47  ? 0.883 1.253 1.057 0.173  0.090  -0.028 47  ARG FFF CZ  
6332 N NH1 . ARG F 47  ? 0.912 1.249 1.065 0.157  0.080  -0.025 47  ARG FFF NH1 
6333 N NH2 . ARG F 47  ? 0.942 1.314 1.143 0.195  0.089  -0.020 47  ARG FFF NH2 
6334 N N   . GLU F 48  ? 0.600 1.101 0.690 0.097  0.148  -0.053 48  GLU FFF N   
6335 C CA  . GLU F 48  ? 0.574 1.069 0.636 0.076  0.148  -0.047 48  GLU FFF CA  
6336 C C   . GLU F 48  ? 0.537 1.016 0.599 0.063  0.131  -0.035 48  GLU FFF C   
6337 O O   . GLU F 48  ? 0.490 0.984 0.578 0.065  0.123  -0.029 48  GLU FFF O   
6338 C CB  . GLU F 48  ? 0.580 1.113 0.650 0.067  0.164  -0.042 48  GLU FFF CB  
6339 C CG  . GLU F 48  ? 0.564 1.133 0.670 0.060  0.161  -0.032 48  GLU FFF CG  
6340 C CD  . GLU F 48  ? 0.570 1.177 0.685 0.046  0.176  -0.026 48  GLU FFF CD  
6341 O OE1 . GLU F 48  ? 0.665 1.285 0.768 0.050  0.194  -0.032 48  GLU FFF OE1 
6342 O OE2 . GLU F 48  ? 0.555 1.180 0.688 0.029  0.171  -0.017 48  GLU FFF OE2 
6343 N N   . PHE F 49  ? 0.498 0.951 0.531 0.053  0.125  -0.034 49  PHE FFF N   
6344 C CA  . PHE F 49  ? 0.465 0.903 0.494 0.042  0.111  -0.024 49  PHE FFF CA  
6345 C C   . PHE F 49  ? 0.451 0.910 0.494 0.028  0.113  -0.016 49  PHE FFF C   
6346 O O   . PHE F 49  ? 0.430 0.905 0.471 0.021  0.126  -0.014 49  PHE FFF O   
6347 C CB  . PHE F 49  ? 0.449 0.860 0.446 0.036  0.107  -0.024 49  PHE FFF CB  
6348 C CG  . PHE F 49  ? 0.428 0.826 0.421 0.027  0.095  -0.015 49  PHE FFF CG  
6349 C CD1 . PHE F 49  ? 0.412 0.802 0.415 0.031  0.083  -0.014 49  PHE FFF CD1 
6350 C CD2 . PHE F 49  ? 0.426 0.822 0.409 0.016  0.097  -0.007 49  PHE FFF CD2 
6351 C CE1 . PHE F 49  ? 0.409 0.792 0.410 0.026  0.074  -0.007 49  PHE FFF CE1 
6352 C CE2 . PHE F 49  ? 0.442 0.823 0.423 0.011  0.087  -0.001 49  PHE FFF CE2 
6353 C CZ  . PHE F 49  ? 0.423 0.800 0.413 0.017  0.076  -0.002 49  PHE FFF CZ  
6354 N N   . VAL F 50  ? 0.445 0.904 0.500 0.024  0.102  -0.011 50  VAL FFF N   
6355 C CA  . VAL F 50  ? 0.446 0.922 0.514 0.010  0.101  -0.006 50  VAL FFF CA  
6356 C C   . VAL F 50  ? 0.442 0.889 0.491 0.001  0.092  -0.002 50  VAL FFF C   
6357 O O   . VAL F 50  ? 0.475 0.912 0.512 -0.012 0.097  0.001  50  VAL FFF O   
6358 C CB  . VAL F 50  ? 0.432 0.935 0.528 0.014  0.094  -0.005 50  VAL FFF CB  
6359 C CG1 . VAL F 50  ? 0.423 0.941 0.530 -0.003 0.090  -0.003 50  VAL FFF CG1 
6360 C CG2 . VAL F 50  ? 0.437 0.970 0.556 0.026  0.103  -0.008 50  VAL FFF CG2 
6361 N N   . ALA F 51  ? 0.428 0.863 0.474 0.007  0.081  -0.003 51  ALA FFF N   
6362 C CA  . ALA F 51  ? 0.420 0.834 0.454 0.002  0.073  -0.001 51  ALA FFF CA  
6363 C C   . ALA F 51  ? 0.422 0.827 0.452 0.013  0.064  -0.001 51  ALA FFF C   
6364 O O   . ALA F 51  ? 0.461 0.878 0.504 0.021  0.062  -0.001 51  ALA FFF O   
6365 C CB  . ALA F 51  ? 0.407 0.833 0.452 -0.008 0.069  -0.003 51  ALA FFF CB  
6366 N N   . GLY F 52  ? 0.403 0.790 0.419 0.013  0.059  0.000  52  GLY FFF N   
6367 C CA  . GLY F 52  ? 0.379 0.762 0.393 0.021  0.051  0.002  52  GLY FFF CA  
6368 C C   . GLY F 52  ? 0.366 0.740 0.372 0.021  0.046  0.003  52  GLY FFF C   
6369 O O   . GLY F 52  ? 0.369 0.732 0.368 0.016  0.048  0.002  52  GLY FFF O   
6370 N N   . MET F 53  ? 0.362 0.740 0.369 0.027  0.040  0.005  53  MET FFF N   
6371 C CA  . MET F 53  ? 0.384 0.758 0.386 0.030  0.036  0.006  53  MET FFF CA  
6372 C C   . MET F 53  ? 0.376 0.753 0.377 0.035  0.031  0.011  53  MET FFF C   
6373 O O   . MET F 53  ? 0.339 0.723 0.348 0.034  0.029  0.013  53  MET FFF O   
6374 C CB  . MET F 53  ? 0.374 0.766 0.384 0.031  0.034  0.003  53  MET FFF CB  
6375 C CG  . MET F 53  ? 0.396 0.786 0.399 0.037  0.032  0.001  53  MET FFF CG  
6376 S SD  . MET F 53  ? 0.394 0.808 0.401 0.038  0.031  -0.004 53  MET FFF SD  
6377 C CE  . MET F 53  ? 0.404 0.802 0.403 0.031  0.033  -0.018 53  MET FFF CE  
6378 N N   . ARG F 54  ? 0.385 0.753 0.377 0.039  0.029  0.012  54  ARG FFF N   
6379 C CA  . ARG F 54  ? 0.385 0.762 0.379 0.043  0.023  0.017  54  ARG FFF CA  
6380 C C   . ARG F 54  ? 0.359 0.758 0.366 0.045  0.021  0.019  54  ARG FFF C   
6381 O O   . ARG F 54  ? 0.341 0.744 0.349 0.048  0.025  0.015  54  ARG FFF O   
6382 C CB  . ARG F 54  ? 0.409 0.777 0.394 0.050  0.021  0.020  54  ARG FFF CB  
6383 C CG  . ARG F 54  ? 0.418 0.766 0.386 0.047  0.022  0.021  54  ARG FFF CG  
6384 C CD  . ARG F 54  ? 0.415 0.766 0.378 0.042  0.019  0.021  54  ARG FFF CD  
6385 N NE  . ARG F 54  ? 0.427 0.763 0.370 0.040  0.023  0.023  54  ARG FFF NE  
6386 C CZ  . ARG F 54  ? 0.454 0.790 0.385 0.036  0.020  0.021  54  ARG FFF CZ  
6387 N NH1 . ARG F 54  ? 0.441 0.787 0.378 0.033  0.014  0.016  54  ARG FFF NH1 
6388 N NH2 . ARG F 54  ? 0.484 0.810 0.395 0.035  0.025  0.024  54  ARG FFF NH2 
6389 N N   . TRP F 55  ? 0.349 0.761 0.364 0.043  0.017  0.025  55  TRP FFF N   
6390 C CA  . TRP F 55  ? 0.353 0.790 0.381 0.044  0.016  0.030  55  TRP FFF CA  
6391 C C   . TRP F 55  ? 0.346 0.795 0.373 0.054  0.019  0.028  55  TRP FFF C   
6392 O O   . TRP F 55  ? 0.357 0.829 0.390 0.056  0.022  0.030  55  TRP FFF O   
6393 C CB  . TRP F 55  ? 0.360 0.808 0.398 0.037  0.010  0.037  55  TRP FFF CB  
6394 C CG  . TRP F 55  ? 0.357 0.815 0.396 0.042  0.005  0.039  55  TRP FFF CG  
6395 C CD1 . TRP F 55  ? 0.355 0.838 0.402 0.051  0.006  0.042  55  TRP FFF CD1 
6396 C CD2 . TRP F 55  ? 0.356 0.804 0.388 0.040  -0.001 0.037  55  TRP FFF CD2 
6397 N NE1 . TRP F 55  ? 0.368 0.857 0.415 0.055  0.000  0.044  55  TRP FFF NE1 
6398 C CE2 . TRP F 55  ? 0.356 0.824 0.393 0.047  -0.005 0.041  55  TRP FFF CE2 
6399 C CE3 . TRP F 55  ? 0.357 0.783 0.376 0.033  -0.004 0.032  55  TRP FFF CE3 
6400 C CZ2 . TRP F 55  ? 0.367 0.835 0.398 0.047  -0.014 0.042  55  TRP FFF CZ2 
6401 C CZ3 . TRP F 55  ? 0.368 0.793 0.378 0.032  -0.011 0.031  55  TRP FFF CZ3 
6402 C CH2 . TRP F 55  ? 0.376 0.823 0.392 0.039  -0.017 0.037  55  TRP FFF CH2 
6403 N N   . THR F 56  ? 0.361 0.797 0.380 0.062  0.019  0.024  56  THR FFF N   
6404 C CA  . THR F 56  ? 0.370 0.810 0.387 0.075  0.022  0.020  56  THR FFF CA  
6405 C C   . THR F 56  ? 0.380 0.814 0.390 0.077  0.028  0.010  56  THR FFF C   
6406 O O   . THR F 56  ? 0.366 0.811 0.376 0.087  0.032  0.005  56  THR FFF O   
6407 C CB  . THR F 56  ? 0.383 0.801 0.392 0.083  0.020  0.021  56  THR FFF CB  
6408 O OG1 . THR F 56  ? 0.384 0.771 0.379 0.076  0.022  0.017  56  THR FFF OG1 
6409 C CG2 . THR F 56  ? 0.377 0.806 0.390 0.082  0.012  0.030  56  THR FFF CG2 
6410 N N   . GLY F 57  ? 0.416 0.834 0.421 0.067  0.029  0.006  57  GLY FFF N   
6411 C CA  . GLY F 57  ? 0.423 0.833 0.420 0.065  0.032  -0.005 57  GLY FFF CA  
6412 C C   . GLY F 57  ? 0.459 0.837 0.446 0.069  0.034  -0.013 57  GLY FFF C   
6413 O O   . GLY F 57  ? 0.495 0.861 0.476 0.064  0.036  -0.023 57  GLY FFF O   
6414 N N   . SER F 58  ? 0.453 0.815 0.437 0.077  0.033  -0.007 58  SER FFF N   
6415 C CA  . SER F 58  ? 0.481 0.809 0.456 0.084  0.035  -0.011 58  SER FFF CA  
6416 C C   . SER F 58  ? 0.484 0.786 0.451 0.074  0.034  -0.003 58  SER FFF C   
6417 O O   . SER F 58  ? 0.499 0.769 0.458 0.079  0.035  -0.000 58  SER FFF O   
6418 C CB  . SER F 58  ? 0.493 0.825 0.471 0.103  0.034  -0.007 58  SER FFF CB  
6419 O OG  . SER F 58  ? 0.528 0.875 0.511 0.104  0.028  0.006  58  SER FFF OG  
6420 N N   . SER F 59  ? 0.452 0.767 0.422 0.063  0.033  0.002  59  SER FFF N   
6421 C CA  . SER F 59  ? 0.468 0.767 0.431 0.054  0.035  0.009  59  SER FFF CA  
6422 C C   . SER F 59  ? 0.455 0.767 0.423 0.041  0.038  0.006  59  SER FFF C   
6423 O O   . SER F 59  ? 0.436 0.772 0.414 0.041  0.035  0.006  59  SER FFF O   
6424 C CB  . SER F 59  ? 0.468 0.772 0.426 0.059  0.030  0.019  59  SER FFF CB  
6425 O OG  . SER F 59  ? 0.498 0.789 0.444 0.051  0.033  0.025  59  SER FFF OG  
6426 N N   . THR F 60  ? 0.465 0.763 0.430 0.030  0.042  0.004  60  THR FFF N   
6427 C CA  . THR F 60  ? 0.467 0.779 0.439 0.019  0.046  0.003  60  THR FFF CA  
6428 C C   . THR F 60  ? 0.505 0.804 0.468 0.012  0.052  0.010  60  THR FFF C   
6429 O O   . THR F 60  ? 0.532 0.806 0.482 0.014  0.053  0.017  60  THR FFF O   
6430 C CB  . THR F 60  ? 0.452 0.770 0.434 0.010  0.047  -0.006 60  THR FFF CB  
6431 O OG1 . THR F 60  ? 0.470 0.761 0.445 0.004  0.049  -0.009 60  THR FFF OG1 
6432 C CG2 . THR F 60  ? 0.440 0.776 0.428 0.017  0.042  -0.013 60  THR FFF CG2 
6433 N N   . PHE F 61  ? 0.484 0.800 0.452 0.007  0.057  0.010  61  PHE FFF N   
6434 C CA  . PHE F 61  ? 0.481 0.792 0.438 0.001  0.064  0.016  61  PHE FFF CA  
6435 C C   . PHE F 61  ? 0.476 0.811 0.449 -0.006 0.071  0.012  61  PHE FFF C   
6436 O O   . PHE F 61  ? 0.465 0.818 0.453 -0.002 0.068  0.006  61  PHE FFF O   
6437 C CB  . PHE F 61  ? 0.475 0.785 0.418 0.010  0.061  0.020  61  PHE FFF CB  
6438 C CG  . PHE F 61  ? 0.458 0.783 0.410 0.017  0.055  0.014  61  PHE FFF CG  
6439 C CD1 . PHE F 61  ? 0.467 0.792 0.423 0.024  0.046  0.015  61  PHE FFF CD1 
6440 C CD2 . PHE F 61  ? 0.450 0.788 0.408 0.018  0.058  0.009  61  PHE FFF CD2 
6441 C CE1 . PHE F 61  ? 0.441 0.779 0.406 0.028  0.041  0.012  61  PHE FFF CE1 
6442 C CE2 . PHE F 61  ? 0.439 0.784 0.405 0.023  0.052  0.005  61  PHE FFF CE2 
6443 C CZ  . PHE F 61  ? 0.429 0.774 0.399 0.027  0.043  0.007  61  PHE FFF CZ  
6444 N N   . TYR F 62  ? 0.504 0.839 0.473 -0.016 0.081  0.017  62  TYR FFF N   
6445 C CA  . TYR F 62  ? 0.492 0.852 0.479 -0.026 0.090  0.015  62  TYR FFF CA  
6446 C C   . TYR F 62  ? 0.509 0.877 0.485 -0.029 0.102  0.020  62  TYR FFF C   
6447 O O   . TYR F 62  ? 0.534 0.882 0.488 -0.031 0.104  0.029  62  TYR FFF O   
6448 C CB  . TYR F 62  ? 0.505 0.859 0.502 -0.041 0.089  0.015  62  TYR FFF CB  
6449 C CG  . TYR F 62  ? 0.496 0.840 0.496 -0.038 0.078  0.007  62  TYR FFF CG  
6450 C CD1 . TYR F 62  ? 0.483 0.853 0.502 -0.036 0.072  -0.001 62  TYR FFF CD1 
6451 C CD2 . TYR F 62  ? 0.513 0.823 0.497 -0.034 0.073  0.009  62  TYR FFF CD2 
6452 C CE1 . TYR F 62  ? 0.482 0.846 0.500 -0.033 0.063  -0.008 62  TYR FFF CE1 
6453 C CE2 . TYR F 62  ? 0.521 0.826 0.507 -0.028 0.065  0.000  62  TYR FFF CE2 
6454 C CZ  . TYR F 62  ? 0.493 0.825 0.495 -0.029 0.060  -0.009 62  TYR FFF CZ  
6455 O OH  . TYR F 62  ? 0.468 0.798 0.469 -0.023 0.053  -0.017 62  TYR FFF OH  
6456 N N   . SER F 63  ? 0.513 0.911 0.504 -0.026 0.109  0.015  63  SER FFF N   
6457 C CA  . SER F 63  ? 0.546 0.961 0.531 -0.029 0.124  0.018  63  SER FFF CA  
6458 C C   . SER F 63  ? 0.555 0.970 0.541 -0.048 0.133  0.029  63  SER FFF C   
6459 O O   . SER F 63  ? 0.572 0.983 0.573 -0.060 0.127  0.029  63  SER FFF O   
6460 C CB  . SER F 63  ? 0.540 0.989 0.547 -0.020 0.131  0.009  63  SER FFF CB  
6461 O OG  . SER F 63  ? 0.569 1.045 0.606 -0.029 0.132  0.009  63  SER FFF OG  
6462 N N   . ASP F 64  ? 0.563 0.983 0.531 -0.053 0.146  0.037  64  ASP FFF N   
6463 C CA  . ASP F 64  ? 0.585 1.003 0.551 -0.075 0.156  0.051  64  ASP FFF CA  
6464 C C   . ASP F 64  ? 0.559 1.008 0.562 -0.089 0.160  0.048  64  ASP FFF C   
6465 O O   . ASP F 64  ? 0.589 1.026 0.597 -0.110 0.161  0.057  64  ASP FFF O   
6466 C CB  . ASP F 64  ? 0.609 1.041 0.552 -0.076 0.172  0.060  64  ASP FFF CB  
6467 C CG  . ASP F 64  ? 0.633 1.035 0.535 -0.067 0.168  0.067  64  ASP FFF CG  
6468 O OD1 . ASP F 64  ? 0.621 0.993 0.516 -0.058 0.152  0.066  64  ASP FFF OD1 
6469 O OD2 . ASP F 64  ? 0.699 1.113 0.577 -0.067 0.180  0.074  64  ASP FFF OD2 
6470 N N   . SER F 65  ? 0.520 1.006 0.548 -0.078 0.161  0.037  65  SER FFF N   
6471 C CA  . SER F 65  ? 0.517 1.047 0.583 -0.090 0.166  0.034  65  SER FFF CA  
6472 C C   . SER F 65  ? 0.483 1.009 0.569 -0.095 0.149  0.028  65  SER FFF C   
6473 O O   . SER F 65  ? 0.462 1.024 0.579 -0.108 0.150  0.026  65  SER FFF O   
6474 C CB  . SER F 65  ? 0.518 1.092 0.601 -0.073 0.175  0.026  65  SER FFF CB  
6475 O OG  . SER F 65  ? 0.545 1.111 0.631 -0.051 0.163  0.015  65  SER FFF OG  
6476 N N   . VAL F 66  ? 0.474 0.963 0.544 -0.087 0.135  0.023  66  VAL FFF N   
6477 C CA  . VAL F 66  ? 0.471 0.957 0.555 -0.091 0.120  0.015  66  VAL FFF CA  
6478 C C   . VAL F 66  ? 0.503 0.939 0.565 -0.098 0.111  0.016  66  VAL FFF C   
6479 O O   . VAL F 66  ? 0.556 0.988 0.627 -0.107 0.101  0.008  66  VAL FFF O   
6480 C CB  . VAL F 66  ? 0.434 0.934 0.526 -0.069 0.110  0.007  66  VAL FFF CB  
6481 C CG1 . VAL F 66  ? 0.414 0.960 0.531 -0.059 0.117  0.006  66  VAL FFF CG1 
6482 C CG2 . VAL F 66  ? 0.437 0.904 0.504 -0.052 0.105  0.006  66  VAL FFF CG2 
6483 N N   . LYS F 67  ? 0.520 0.921 0.555 -0.093 0.114  0.024  67  LYS FFF N   
6484 C CA  . LYS F 67  ? 0.553 0.905 0.569 -0.096 0.107  0.027  67  LYS FFF CA  
6485 C C   . LYS F 67  ? 0.571 0.912 0.598 -0.121 0.107  0.026  67  LYS FFF C   
6486 O O   . LYS F 67  ? 0.602 0.955 0.636 -0.139 0.118  0.036  67  LYS FFF O   
6487 C CB  . LYS F 67  ? 0.588 0.911 0.574 -0.089 0.112  0.040  67  LYS FFF CB  
6488 C CG  . LYS F 67  ? 0.615 0.891 0.584 -0.084 0.103  0.042  67  LYS FFF CG  
6489 C CD  . LYS F 67  ? 0.648 0.900 0.588 -0.073 0.105  0.057  67  LYS FFF CD  
6490 C CE  . LYS F 67  ? 0.652 0.869 0.581 -0.059 0.093  0.057  67  LYS FFF CE  
6491 N NZ  . LYS F 67  ? 0.693 0.880 0.596 -0.055 0.095  0.076  67  LYS FFF NZ  
6492 N N   . GLY F 68  ? 0.582 0.901 0.609 -0.123 0.096  0.015  68  GLY FFF N   
6493 C CA  . GLY F 68  ? 0.612 0.914 0.648 -0.148 0.094  0.010  68  GLY FFF CA  
6494 C C   . GLY F 68  ? 0.606 0.950 0.669 -0.160 0.087  -0.004 68  GLY FFF C   
6495 O O   . GLY F 68  ? 0.659 0.989 0.728 -0.179 0.081  -0.013 68  GLY FFF O   
6496 N N   . ARG F 69  ? 0.565 0.960 0.644 -0.148 0.088  -0.004 69  ARG FFF N   
6497 C CA  . ARG F 69  ? 0.548 0.994 0.656 -0.155 0.082  -0.014 69  ARG FFF CA  
6498 C C   . ARG F 69  ? 0.534 0.992 0.638 -0.133 0.070  -0.023 69  ARG FFF C   
6499 O O   . ARG F 69  ? 0.512 0.987 0.625 -0.139 0.059  -0.035 69  ARG FFF O   
6500 C CB  . ARG F 69  ? 0.524 1.022 0.656 -0.159 0.093  -0.005 69  ARG FFF CB  
6501 C CG  . ARG F 69  ? 0.547 1.044 0.687 -0.185 0.105  0.005  69  ARG FFF CG  
6502 C CD  . ARG F 69  ? 0.528 1.087 0.698 -0.191 0.116  0.012  69  ARG FFF CD  
6503 N NE  . ARG F 69  ? 0.490 1.069 0.656 -0.163 0.125  0.016  69  ARG FFF NE  
6504 C CZ  . ARG F 69  ? 0.452 1.075 0.639 -0.144 0.122  0.011  69  ARG FFF CZ  
6505 N NH1 . ARG F 69  ? 0.428 1.086 0.641 -0.149 0.110  0.003  69  ARG FFF NH1 
6506 N NH2 . ARG F 69  ? 0.439 1.069 0.619 -0.120 0.131  0.013  69  ARG FFF NH2 
6507 N N   . PHE F 70  ? 0.519 0.970 0.611 -0.109 0.073  -0.017 70  PHE FFF N   
6508 C CA  . PHE F 70  ? 0.497 0.957 0.585 -0.087 0.064  -0.022 70  PHE FFF CA  
6509 C C   . PHE F 70  ? 0.503 0.919 0.565 -0.078 0.060  -0.024 70  PHE FFF C   
6510 O O   . PHE F 70  ? 0.501 0.882 0.547 -0.078 0.066  -0.018 70  PHE FFF O   
6511 C CB  . PHE F 70  ? 0.477 0.959 0.571 -0.069 0.070  -0.014 70  PHE FFF CB  
6512 C CG  . PHE F 70  ? 0.470 1.001 0.593 -0.071 0.074  -0.012 70  PHE FFF CG  
6513 C CD1 . PHE F 70  ? 0.469 1.029 0.614 -0.091 0.073  -0.014 70  PHE FFF CD1 
6514 C CD2 . PHE F 70  ? 0.456 1.004 0.586 -0.051 0.078  -0.007 70  PHE FFF CD2 
6515 C CE1 . PHE F 70  ? 0.459 1.071 0.634 -0.090 0.077  -0.011 70  PHE FFF CE1 
6516 C CE2 . PHE F 70  ? 0.440 1.035 0.599 -0.049 0.083  -0.005 70  PHE FFF CE2 
6517 C CZ  . PHE F 70  ? 0.444 1.073 0.627 -0.067 0.082  -0.006 70  PHE FFF CZ  
6518 N N   . THR F 71  ? 0.478 0.900 0.537 -0.069 0.050  -0.032 71  THR FFF N   
6519 C CA  . THR F 71  ? 0.472 0.863 0.509 -0.055 0.046  -0.035 71  THR FFF CA  
6520 C C   . THR F 71  ? 0.440 0.857 0.480 -0.038 0.041  -0.033 71  THR FFF C   
6521 O O   . THR F 71  ? 0.431 0.882 0.485 -0.040 0.036  -0.034 71  THR FFF O   
6522 C CB  . THR F 71  ? 0.491 0.859 0.519 -0.064 0.041  -0.049 71  THR FFF CB  
6523 O OG1 . THR F 71  ? 0.479 0.878 0.515 -0.070 0.033  -0.061 71  THR FFF OG1 
6524 C CG2 . THR F 71  ? 0.528 0.864 0.553 -0.082 0.046  -0.050 71  THR FFF CG2 
6525 N N   . VAL F 72  ? 0.424 0.824 0.452 -0.024 0.042  -0.028 72  VAL FFF N   
6526 C CA  . VAL F 72  ? 0.403 0.820 0.432 -0.010 0.037  -0.025 72  VAL FFF CA  
6527 C C   . VAL F 72  ? 0.412 0.818 0.427 -0.004 0.033  -0.032 72  VAL FFF C   
6528 O O   . VAL F 72  ? 0.438 0.814 0.442 -0.003 0.036  -0.035 72  VAL FFF O   
6529 C CB  . VAL F 72  ? 0.398 0.809 0.425 0.001  0.040  -0.014 72  VAL FFF CB  
6530 C CG1 . VAL F 72  ? 0.392 0.818 0.423 0.011  0.035  -0.009 72  VAL FFF CG1 
6531 C CG2 . VAL F 72  ? 0.391 0.809 0.428 -0.002 0.046  -0.010 72  VAL FFF CG2 
6532 N N   . SER F 73  ? 0.408 0.840 0.424 -0.000 0.028  -0.034 73  SER FFF N   
6533 C CA  . SER F 73  ? 0.420 0.852 0.423 0.007  0.026  -0.042 73  SER FFF CA  
6534 C C   . SER F 73  ? 0.407 0.867 0.414 0.017  0.023  -0.030 73  SER FFF C   
6535 O O   . SER F 73  ? 0.417 0.892 0.437 0.017  0.022  -0.019 73  SER FFF O   
6536 C CB  . SER F 73  ? 0.440 0.878 0.436 -0.002 0.022  -0.058 73  SER FFF CB  
6537 O OG  . SER F 73  ? 0.428 0.904 0.432 -0.006 0.015  -0.056 73  SER FFF OG  
6538 N N   . ARG F 74  ? 0.407 0.871 0.403 0.025  0.024  -0.033 74  ARG FFF N   
6539 C CA  . ARG F 74  ? 0.416 0.907 0.415 0.032  0.023  -0.021 74  ARG FFF CA  
6540 C C   . ARG F 74  ? 0.408 0.920 0.393 0.035  0.022  -0.030 74  ARG FFF C   
6541 O O   . ARG F 74  ? 0.418 0.913 0.390 0.037  0.024  -0.047 74  ARG FFF O   
6542 C CB  . ARG F 74  ? 0.445 0.923 0.447 0.040  0.026  -0.011 74  ARG FFF CB  
6543 C CG  . ARG F 74  ? 0.447 0.947 0.457 0.042  0.025  0.005  74  ARG FFF CG  
6544 C CD  . ARG F 74  ? 0.440 0.926 0.456 0.045  0.026  0.013  74  ARG FFF CD  
6545 N NE  . ARG F 74  ? 0.433 0.919 0.444 0.052  0.030  0.008  74  ARG FFF NE  
6546 C CZ  . ARG F 74  ? 0.437 0.919 0.453 0.056  0.030  0.014  74  ARG FFF CZ  
6547 N NH1 . ARG F 74  ? 0.427 0.900 0.451 0.050  0.026  0.023  74  ARG FFF NH1 
6548 N NH2 . ARG F 74  ? 0.456 0.944 0.471 0.065  0.032  0.010  74  ARG FFF NH2 
6549 N N   . ASN F 75  ? 0.395 0.940 0.380 0.037  0.019  -0.019 75  ASN FFF N   
6550 C CA  . ASN F 75  ? 0.397 0.970 0.365 0.040  0.020  -0.027 75  ASN FFF CA  
6551 C C   . ASN F 75  ? 0.396 0.971 0.359 0.051  0.028  -0.026 75  ASN FFF C   
6552 O O   . ASN F 75  ? 0.364 0.924 0.339 0.054  0.030  -0.016 75  ASN FFF O   
6553 C CB  . ASN F 75  ? 0.397 1.007 0.365 0.038  0.014  -0.011 75  ASN FFF CB  
6554 C CG  . ASN F 75  ? 0.384 1.004 0.364 0.042  0.015  0.015  75  ASN FFF CG  
6555 O OD1 . ASN F 75  ? 0.375 0.972 0.366 0.044  0.019  0.020  75  ASN FFF OD1 
6556 N ND2 . ASN F 75  ? 0.368 1.018 0.345 0.041  0.011  0.031  75  ASN FFF ND2 
6557 N N   . ASN F 76  ? 0.437 1.032 0.382 0.057  0.031  -0.038 76  ASN FFF N   
6558 C CA  . ASN F 76  ? 0.456 1.061 0.397 0.069  0.040  -0.040 76  ASN FFF CA  
6559 C C   . ASN F 76  ? 0.424 1.054 0.379 0.069  0.043  -0.013 76  ASN FFF C   
6560 O O   . ASN F 76  ? 0.426 1.056 0.391 0.076  0.048  -0.009 76  ASN FFF O   
6561 C CB  . ASN F 76  ? 0.525 1.154 0.443 0.076  0.045  -0.059 76  ASN FFF CB  
6562 C CG  . ASN F 76  ? 0.583 1.179 0.487 0.075  0.043  -0.089 76  ASN FFF CG  
6563 O OD1 . ASN F 76  ? 0.568 1.124 0.481 0.072  0.041  -0.094 76  ASN FFF OD1 
6564 N ND2 . ASN F 76  ? 0.634 1.248 0.514 0.076  0.044  -0.109 76  ASN FFF ND2 
6565 N N   . ALA F 77  ? 0.406 1.057 0.364 0.061  0.037  0.005  77  ALA FFF N   
6566 C CA  . ALA F 77  ? 0.399 1.067 0.371 0.058  0.038  0.033  77  ALA FFF CA  
6567 C C   . ALA F 77  ? 0.381 1.018 0.374 0.055  0.036  0.041  77  ALA FFF C   
6568 O O   . ALA F 77  ? 0.360 1.006 0.366 0.053  0.038  0.057  77  ALA FFF O   
6569 C CB  . ALA F 77  ? 0.396 1.085 0.366 0.052  0.032  0.050  77  ALA FFF CB  
6570 N N   . LYS F 78  ? 0.423 1.027 0.419 0.053  0.032  0.029  78  LYS FFF N   
6571 C CA  . LYS F 78  ? 0.432 1.005 0.442 0.051  0.030  0.033  78  LYS FFF CA  
6572 C C   . LYS F 78  ? 0.384 0.954 0.407 0.044  0.025  0.052  78  LYS FFF C   
6573 O O   . LYS F 78  ? 0.371 0.923 0.406 0.041  0.024  0.057  78  LYS FFF O   
6574 C CB  . LYS F 78  ? 0.464 1.036 0.481 0.055  0.034  0.034  78  LYS FFF CB  
6575 C CG  . LYS F 78  ? 0.527 1.107 0.534 0.066  0.040  0.020  78  LYS FFF CG  
6576 C CD  . LYS F 78  ? 0.546 1.126 0.564 0.073  0.043  0.022  78  LYS FFF CD  
6577 C CE  . LYS F 78  ? 0.588 1.181 0.599 0.088  0.050  0.008  78  LYS FFF CE  
6578 N NZ  . LYS F 78  ? 0.623 1.227 0.649 0.096  0.052  0.014  78  LYS FFF NZ  
6579 N N   . ASP F 79  ? 0.357 0.946 0.378 0.042  0.022  0.061  79  ASP FFF N   
6580 C CA  . ASP F 79  ? 0.353 0.937 0.386 0.039  0.017  0.081  79  ASP FFF CA  
6581 C C   . ASP F 79  ? 0.340 0.916 0.378 0.040  0.012  0.076  79  ASP FFF C   
6582 O O   . ASP F 79  ? 0.319 0.885 0.369 0.040  0.009  0.089  79  ASP FFF O   
6583 C CB  . ASP F 79  ? 0.360 0.974 0.391 0.037  0.017  0.102  79  ASP FFF CB  
6584 C CG  . ASP F 79  ? 0.371 1.019 0.385 0.040  0.016  0.098  79  ASP FFF CG  
6585 O OD1 . ASP F 79  ? 0.359 1.005 0.365 0.042  0.013  0.080  79  ASP FFF OD1 
6586 O OD2 . ASP F 79  ? 0.406 1.083 0.412 0.039  0.018  0.114  79  ASP FFF OD2 
6587 N N   . THR F 80  ? 0.337 0.916 0.365 0.040  0.012  0.057  80  THR FFF N   
6588 C CA  . THR F 80  ? 0.364 0.942 0.397 0.038  0.007  0.051  80  THR FFF CA  
6589 C C   . THR F 80  ? 0.380 0.934 0.412 0.035  0.011  0.031  80  THR FFF C   
6590 O O   . THR F 80  ? 0.429 0.980 0.448 0.034  0.013  0.017  80  THR FFF O   
6591 C CB  . THR F 80  ? 0.364 0.976 0.389 0.038  0.001  0.050  80  THR FFF CB  
6592 O OG1 . THR F 80  ? 0.363 0.998 0.384 0.040  -0.000 0.070  80  THR FFF OG1 
6593 C CG2 . THR F 80  ? 0.373 0.995 0.412 0.037  -0.005 0.051  80  THR FFF CG2 
6594 N N   . VAL F 81  ? 0.381 0.919 0.426 0.034  0.011  0.031  81  VAL FFF N   
6595 C CA  . VAL F 81  ? 0.400 0.916 0.443 0.030  0.015  0.017  81  VAL FFF CA  
6596 C C   . VAL F 81  ? 0.394 0.927 0.447 0.025  0.012  0.013  81  VAL FFF C   
6597 O O   . VAL F 81  ? 0.372 0.922 0.439 0.029  0.009  0.024  81  VAL FFF O   
6598 C CB  . VAL F 81  ? 0.429 0.919 0.477 0.032  0.020  0.020  81  VAL FFF CB  
6599 C CG1 . VAL F 81  ? 0.461 0.933 0.507 0.027  0.025  0.010  81  VAL FFF CG1 
6600 C CG2 . VAL F 81  ? 0.449 0.928 0.489 0.035  0.021  0.023  81  VAL FFF CG2 
6601 N N   . TYR F 82  ? 0.400 0.927 0.448 0.016  0.013  -0.002 82  TYR FFF N   
6602 C CA  . TYR F 82  ? 0.418 0.964 0.477 0.007  0.010  -0.008 82  TYR FFF CA  
6603 C C   . TYR F 82  ? 0.426 0.950 0.491 0.000  0.018  -0.013 82  TYR FFF C   
6604 O O   . TYR F 82  ? 0.485 0.978 0.537 -0.002 0.023  -0.018 82  TYR FFF O   
6605 C CB  . TYR F 82  ? 0.436 0.996 0.484 -0.002 0.004  -0.021 82  TYR FFF CB  
6606 C CG  . TYR F 82  ? 0.439 1.020 0.474 0.005  -0.001 -0.017 82  TYR FFF CG  
6607 C CD1 . TYR F 82  ? 0.424 1.044 0.468 0.008  -0.010 -0.006 82  TYR FFF CD1 
6608 C CD2 . TYR F 82  ? 0.436 1.004 0.453 0.010  0.002  -0.022 82  TYR FFF CD2 
6609 C CE1 . TYR F 82  ? 0.442 1.084 0.472 0.013  -0.014 0.001  82  TYR FFF CE1 
6610 C CE2 . TYR F 82  ? 0.452 1.046 0.457 0.015  -0.001 -0.017 82  TYR FFF CE2 
6611 C CZ  . TYR F 82  ? 0.457 1.087 0.467 0.016  -0.009 -0.005 82  TYR FFF CZ  
6612 O OH  . TYR F 82  ? 0.454 1.111 0.451 0.021  -0.012 0.003  82  TYR FFF OH  
6613 N N   . LEU F 83  ? 0.418 0.961 0.503 -0.001 0.019  -0.009 83  LEU FFF N   
6614 C CA  . LEU F 83  ? 0.389 0.924 0.481 -0.011 0.027  -0.013 83  LEU FFF CA  
6615 C C   . LEU F 83  ? 0.408 0.968 0.510 -0.027 0.022  -0.021 83  LEU FFF C   
6616 O O   . LEU F 83  ? 0.400 1.000 0.522 -0.026 0.017  -0.017 83  LEU FFF O   
6617 C CB  . LEU F 83  ? 0.361 0.905 0.469 -0.002 0.033  -0.004 83  LEU FFF CB  
6618 C CG  . LEU F 83  ? 0.372 0.912 0.486 -0.010 0.044  -0.007 83  LEU FFF CG  
6619 C CD1 . LEU F 83  ? 0.373 0.872 0.464 -0.014 0.050  -0.009 83  LEU FFF CD1 
6620 C CD2 . LEU F 83  ? 0.356 0.913 0.488 0.002  0.051  -0.001 83  LEU FFF CD2 
6621 N N   . HIS F 84  ? 0.435 0.972 0.524 -0.041 0.022  -0.033 84  HIS FFF N   
6622 C CA  . HIS F 84  ? 0.464 1.016 0.561 -0.062 0.018  -0.044 84  HIS FFF CA  
6623 C C   . HIS F 84  ? 0.470 1.026 0.584 -0.074 0.027  -0.040 84  HIS FFF C   
6624 O O   . HIS F 84  ? 0.476 0.995 0.579 -0.078 0.036  -0.038 84  HIS FFF O   
6625 C CB  . HIS F 84  ? 0.496 1.014 0.571 -0.072 0.015  -0.059 84  HIS FFF CB  
6626 C CG  . HIS F 84  ? 0.497 1.012 0.553 -0.058 0.010  -0.063 84  HIS FFF CG  
6627 N ND1 . HIS F 84  ? 0.506 1.051 0.558 -0.061 -0.001 -0.072 84  HIS FFF ND1 
6628 C CD2 . HIS F 84  ? 0.492 0.982 0.532 -0.043 0.014  -0.060 84  HIS FFF CD2 
6629 C CE1 . HIS F 84  ? 0.516 1.054 0.549 -0.047 -0.002 -0.073 84  HIS FFF CE1 
6630 N NE2 . HIS F 84  ? 0.500 1.006 0.528 -0.036 0.007  -0.065 84  HIS FFF NE2 
6631 N N   . MET F 85  ? 0.454 1.057 0.595 -0.077 0.025  -0.036 85  MET FFF N   
6632 C CA  . MET F 85  ? 0.454 1.075 0.617 -0.087 0.036  -0.030 85  MET FFF CA  
6633 C C   . MET F 85  ? 0.473 1.112 0.650 -0.115 0.031  -0.039 85  MET FFF C   
6634 O O   . MET F 85  ? 0.494 1.180 0.690 -0.120 0.020  -0.042 85  MET FFF O   
6635 C CB  . MET F 85  ? 0.436 1.100 0.624 -0.070 0.038  -0.020 85  MET FFF CB  
6636 C CG  . MET F 85  ? 0.429 1.075 0.606 -0.044 0.039  -0.013 85  MET FFF CG  
6637 S SD  . MET F 85  ? 0.409 1.089 0.614 -0.023 0.046  -0.003 85  MET FFF SD  
6638 C CE  . MET F 85  ? 0.429 1.169 0.661 -0.022 0.030  0.000  85  MET FFF CE  
6639 N N   . ASN F 86  ? 0.500 1.103 0.667 -0.134 0.038  -0.043 86  ASN FFF N   
6640 C CA  . ASN F 86  ? 0.529 1.139 0.708 -0.166 0.035  -0.051 86  ASN FFF CA  
6641 C C   . ASN F 86  ? 0.544 1.168 0.743 -0.181 0.049  -0.040 86  ASN FFF C   
6642 O O   . ASN F 86  ? 0.530 1.140 0.721 -0.166 0.063  -0.029 86  ASN FFF O   
6643 C CB  . ASN F 86  ? 0.561 1.112 0.712 -0.178 0.031  -0.064 86  ASN FFF CB  
6644 C CG  . ASN F 86  ? 0.562 1.101 0.691 -0.162 0.020  -0.075 86  ASN FFF CG  
6645 O OD1 . ASN F 86  ? 0.580 1.075 0.685 -0.147 0.023  -0.075 86  ASN FFF OD1 
6646 N ND2 . ASN F 86  ? 0.557 1.139 0.695 -0.164 0.006  -0.083 86  ASN FFF ND2 
6647 N N   . SER F 87  ? 0.594 1.245 0.816 -0.210 0.047  -0.044 87  SER FFF N   
6648 C CA  . SER F 87  ? 0.603 1.274 0.848 -0.230 0.062  -0.033 87  SER FFF CA  
6649 C C   . SER F 87  ? 0.582 1.298 0.845 -0.207 0.074  -0.020 87  SER FFF C   
6650 O O   . SER F 87  ? 0.619 1.319 0.874 -0.204 0.091  -0.009 87  SER FFF O   
6651 C CB  . SER F 87  ? 0.631 1.238 0.851 -0.242 0.073  -0.027 87  SER FFF CB  
6652 O OG  . SER F 87  ? 0.672 1.230 0.873 -0.258 0.061  -0.041 87  SER FFF OG  
6653 N N   . LEU F 88  ? 0.556 1.323 0.839 -0.190 0.065  -0.021 88  LEU FFF N   
6654 C CA  . LEU F 88  ? 0.519 1.322 0.818 -0.161 0.074  -0.012 88  LEU FFF CA  
6655 C C   . LEU F 88  ? 0.521 1.378 0.855 -0.172 0.089  -0.004 88  LEU FFF C   
6656 O O   . LEU F 88  ? 0.498 1.397 0.861 -0.198 0.083  -0.006 88  LEU FFF O   
6657 C CB  . LEU F 88  ? 0.496 1.333 0.807 -0.139 0.058  -0.014 88  LEU FFF CB  
6658 C CG  . LEU F 88  ? 0.485 1.276 0.763 -0.117 0.051  -0.017 88  LEU FFF CG  
6659 C CD1 . LEU F 88  ? 0.474 1.297 0.760 -0.107 0.032  -0.019 88  LEU FFF CD1 
6660 C CD2 . LEU F 88  ? 0.468 1.239 0.736 -0.089 0.064  -0.009 88  LEU FFF CD2 
6661 N N   . LYS F 89  ? 0.609 1.197 1.015 -0.136 -0.000 0.000  89  LYS FFF N   
6662 C CA  . LYS F 89  ? 0.599 1.225 1.038 -0.146 0.018  0.020  89  LYS FFF CA  
6663 C C   . LYS F 89  ? 0.572 1.233 1.007 -0.127 0.027  0.017  89  LYS FFF C   
6664 O O   . LYS F 89  ? 0.571 1.220 0.972 -0.108 0.024  0.006  89  LYS FFF O   
6665 C CB  . LYS F 89  ? 0.616 1.230 1.041 -0.151 0.039  0.041  89  LYS FFF CB  
6666 C CG  . LYS F 89  ? 0.652 1.228 1.081 -0.170 0.029  0.048  89  LYS FFF CG  
6667 C CD  . LYS F 89  ? 0.668 1.223 1.066 -0.169 0.047  0.066  89  LYS FFF CD  
6668 C CE  . LYS F 89  ? 0.701 1.247 1.126 -0.194 0.048  0.090  89  LYS FFF CE  
6669 N NZ  . LYS F 89  ? 0.718 1.224 1.160 -0.207 0.020  0.080  89  LYS FFF NZ  
6670 N N   . PRO F 90  ? 0.558 1.265 1.029 -0.131 0.039  0.028  90  PRO FFF N   
6671 C CA  . PRO F 90  ? 0.533 1.272 1.000 -0.110 0.050  0.026  90  PRO FFF CA  
6672 C C   . PRO F 90  ? 0.514 1.236 0.938 -0.093 0.069  0.029  90  PRO FFF C   
6673 O O   . PRO F 90  ? 0.470 1.195 0.876 -0.072 0.070  0.021  90  PRO FFF O   
6674 C CB  . PRO F 90  ? 0.531 1.324 1.048 -0.120 0.061  0.038  90  PRO FFF CB  
6675 C CG  . PRO F 90  ? 0.544 1.334 1.098 -0.148 0.046  0.043  90  PRO FFF CG  
6676 C CD  . PRO F 90  ? 0.562 1.295 1.083 -0.155 0.040  0.043  90  PRO FFF CD  
6677 N N   . GLU F 91  ? 0.556 1.260 0.965 -0.102 0.081  0.042  91  GLU FFF N   
6678 C CA  . GLU F 91  ? 0.604 1.289 0.971 -0.089 0.097  0.045  91  GLU FFF CA  
6679 C C   . GLU F 91  ? 0.564 1.207 0.889 -0.074 0.086  0.030  91  GLU FFF C   
6680 O O   . GLU F 91  ? 0.574 1.206 0.867 -0.059 0.095  0.029  91  GLU FFF O   
6681 C CB  . GLU F 91  ? 0.679 1.350 1.041 -0.107 0.107  0.063  91  GLU FFF CB  
6682 C CG  . GLU F 91  ? 0.734 1.387 1.053 -0.095 0.123  0.068  91  GLU FFF CG  
6683 C CD  . GLU F 91  ? 0.798 1.424 1.106 -0.111 0.126  0.084  91  GLU FFF CD  
6684 O OE1 . GLU F 91  ? 0.838 1.483 1.179 -0.132 0.129  0.102  91  GLU FFF OE1 
6685 O OE2 . GLU F 91  ? 0.762 1.349 1.031 -0.104 0.124  0.079  91  GLU FFF OE2 
6686 N N   . ASP F 92  ? 0.514 1.139 0.840 -0.079 0.065  0.020  92  ASP FFF N   
6687 C CA  . ASP F 92  ? 0.483 1.077 0.773 -0.067 0.053  0.008  92  ASP FFF CA  
6688 C C   . ASP F 92  ? 0.447 1.057 0.735 -0.049 0.048  0.001  92  ASP FFF C   
6689 O O   . ASP F 92  ? 0.446 1.036 0.704 -0.038 0.041  -0.005 92  ASP FFF O   
6690 C CB  . ASP F 92  ? 0.480 1.054 0.772 -0.077 0.033  -0.002 92  ASP FFF CB  
6691 C CG  . ASP F 92  ? 0.498 1.044 0.787 -0.092 0.034  0.003  92  ASP FFF CG  
6692 O OD1 . ASP F 92  ? 0.494 1.022 0.758 -0.089 0.047  0.011  92  ASP FFF OD1 
6693 O OD2 . ASP F 92  ? 0.506 1.049 0.821 -0.106 0.019  -0.001 92  ASP FFF OD2 
6694 N N   . THR F 93  ? 0.418 1.066 0.738 -0.046 0.050  0.002  93  THR FFF N   
6695 C CA  . THR F 93  ? 0.396 1.061 0.720 -0.029 0.043  -0.003 93  THR FFF CA  
6696 C C   . THR F 93  ? 0.382 1.030 0.677 -0.011 0.052  -0.002 93  THR FFF C   
6697 O O   . THR F 93  ? 0.391 1.046 0.686 -0.007 0.069  0.001  93  THR FFF O   
6698 C CB  . THR F 93  ? 0.393 1.104 0.762 -0.029 0.045  -0.002 93  THR FFF CB  
6699 O OG1 . THR F 93  ? 0.401 1.124 0.797 -0.046 0.032  -0.004 93  THR FFF OG1 
6700 C CG2 . THR F 93  ? 0.387 1.115 0.763 -0.009 0.038  -0.006 93  THR FFF CG2 
6701 N N   . ALA F 94  ? 0.377 1.004 0.648 -0.001 0.040  -0.005 94  ALA FFF N   
6702 C CA  . ALA F 94  ? 0.376 0.981 0.621 0.015  0.043  -0.005 94  ALA FFF CA  
6703 C C   . ALA F 94  ? 0.378 0.968 0.607 0.021  0.026  -0.003 94  ALA FFF C   
6704 O O   . ALA F 94  ? 0.368 0.967 0.600 0.013  0.013  -0.005 94  ALA FFF O   
6705 C CB  . ALA F 94  ? 0.381 0.959 0.599 0.010  0.055  -0.003 94  ALA FFF CB  
6706 N N   . VAL F 95  ? 0.387 0.959 0.601 0.034  0.024  -0.001 95  VAL FFF N   
6707 C CA  . VAL F 95  ? 0.394 0.947 0.586 0.036  0.010  0.005  95  VAL FFF CA  
6708 C C   . VAL F 95  ? 0.387 0.914 0.548 0.028  0.015  0.006  95  VAL FFF C   
6709 O O   . VAL F 95  ? 0.378 0.887 0.528 0.031  0.026  0.004  95  VAL FFF O   
6710 C CB  . VAL F 95  ? 0.406 0.948 0.601 0.052  0.003  0.010  95  VAL FFF CB  
6711 C CG1 . VAL F 95  ? 0.417 0.941 0.593 0.051  -0.012 0.021  95  VAL FFF CG1 
6712 C CG2 . VAL F 95  ? 0.413 0.982 0.641 0.063  -0.004 0.008  95  VAL FFF CG2 
6713 N N   . TYR F 96  ? 0.379 0.907 0.527 0.019  0.007  0.007  96  TYR FFF N   
6714 C CA  . TYR F 96  ? 0.381 0.888 0.501 0.012  0.010  0.006  96  TYR FFF CA  
6715 C C   . TYR F 96  ? 0.383 0.879 0.483 0.016  0.002  0.015  96  TYR FFF C   
6716 O O   . TYR F 96  ? 0.372 0.883 0.477 0.019  -0.010 0.023  96  TYR FFF O   
6717 C CB  . TYR F 96  ? 0.378 0.897 0.499 0.002  0.005  -0.002 96  TYR FFF CB  
6718 C CG  . TYR F 96  ? 0.384 0.904 0.522 -0.006 0.014  -0.009 96  TYR FFF CG  
6719 C CD1 . TYR F 96  ? 0.396 0.938 0.565 -0.007 0.015  -0.009 96  TYR FFF CD1 
6720 C CD2 . TYR F 96  ? 0.391 0.891 0.517 -0.014 0.021  -0.012 96  TYR FFF CD2 
6721 C CE1 . TYR F 96  ? 0.395 0.942 0.584 -0.017 0.023  -0.011 96  TYR FFF CE1 
6722 C CE2 . TYR F 96  ? 0.394 0.895 0.539 -0.023 0.028  -0.013 96  TYR FFF CE2 
6723 C CZ  . TYR F 96  ? 0.399 0.925 0.575 -0.026 0.029  -0.012 96  TYR FFF CZ  
6724 O OH  . TYR F 96  ? 0.394 0.924 0.592 -0.038 0.036  -0.009 96  TYR FFF OH  
6725 N N   . TYR F 97  ? 0.386 0.858 0.467 0.016  0.008  0.016  97  TYR FFF N   
6726 C CA  . TYR F 97  ? 0.420 0.879 0.484 0.017  0.002  0.027  97  TYR FFF CA  
6727 C C   . TYR F 97  ? 0.418 0.871 0.459 0.010  0.006  0.024  97  TYR FFF C   
6728 O O   . TYR F 97  ? 0.414 0.855 0.450 0.007  0.015  0.014  97  TYR FFF O   
6729 C CB  . TYR F 97  ? 0.441 0.876 0.505 0.024  0.004  0.029  97  TYR FFF CB  
6730 C CG  . TYR F 97  ? 0.458 0.896 0.545 0.035  -0.000 0.029  97  TYR FFF CG  
6731 C CD1 . TYR F 97  ? 0.475 0.920 0.576 0.040  0.010  0.018  97  TYR FFF CD1 
6732 C CD2 . TYR F 97  ? 0.475 0.911 0.572 0.040  -0.015 0.041  97  TYR FFF CD2 
6733 C CE1 . TYR F 97  ? 0.488 0.941 0.612 0.052  0.007  0.015  97  TYR FFF CE1 
6734 C CE2 . TYR F 97  ? 0.501 0.939 0.621 0.052  -0.021 0.040  97  TYR FFF CE2 
6735 C CZ  . TYR F 97  ? 0.504 0.951 0.638 0.059  -0.010 0.025  97  TYR FFF CZ  
6736 O OH  . TYR F 97  ? 0.569 1.022 0.727 0.074  -0.015 0.021  97  TYR FFF OH  
6737 N N   . CYS F 98  ? 0.415 0.875 0.443 0.008  -0.002 0.033  98  CYS FFF N   
6738 C CA  . CYS F 98  ? 0.428 0.882 0.435 0.004  0.001  0.031  98  CYS FFF CA  
6739 C C   . CYS F 98  ? 0.406 0.844 0.407 0.004  -0.001 0.044  98  CYS FFF C   
6740 O O   . CYS F 98  ? 0.402 0.836 0.414 0.006  -0.009 0.056  98  CYS FFF O   
6741 C CB  . CYS F 98  ? 0.443 0.927 0.440 0.002  -0.005 0.030  98  CYS FFF CB  
6742 S SG  . CYS F 98  ? 0.494 1.007 0.493 0.002  -0.018 0.051  98  CYS FFF SG  
6743 N N   . ALA F 99  ? 0.401 0.827 0.387 0.001  0.003  0.041  99  ALA FFF N   
6744 C CA  . ALA F 99  ? 0.416 0.824 0.397 -0.000 0.000  0.051  99  ALA FFF CA  
6745 C C   . ALA F 99  ? 0.417 0.826 0.381 -0.004 0.004  0.047  99  ALA FFF C   
6746 O O   . ALA F 99  ? 0.403 0.820 0.360 -0.003 0.010  0.035  99  ALA FFF O   
6747 C CB  . ALA F 99  ? 0.413 0.792 0.401 0.005  0.003  0.045  99  ALA FFF CB  
6748 N N   . ILE F 100 ? 0.426 0.828 0.387 -0.007 0.000  0.057  100 ILE FFF N   
6749 C CA  . ILE F 100 ? 0.438 0.841 0.385 -0.010 0.003  0.055  100 ILE FFF CA  
6750 C C   . ILE F 100 ? 0.470 0.841 0.415 -0.009 0.002  0.052  100 ILE FFF C   
6751 O O   . ILE F 100 ? 0.524 0.877 0.480 -0.008 -0.003 0.056  100 ILE FFF O   
6752 C CB  . ILE F 100 ? 0.434 0.871 0.381 -0.016 -0.003 0.071  100 ILE FFF CB  
6753 C CG1 . ILE F 100 ? 0.439 0.875 0.401 -0.022 -0.014 0.093  100 ILE FFF CG1 
6754 C CG2 . ILE F 100 ? 0.414 0.887 0.356 -0.013 -0.001 0.066  100 ILE FFF CG2 
6755 C CD1 . ILE F 100 ? 0.436 0.903 0.399 -0.031 -0.019 0.114  100 ILE FFF CD1 
6756 N N   . THR F 101 ? 0.454 0.820 0.387 -0.009 0.006  0.045  101 THR FFF N   
6757 C CA  . THR F 101 ? 0.459 0.798 0.387 -0.008 0.005  0.041  101 THR FFF CA  
6758 C C   . THR F 101 ? 0.469 0.819 0.392 -0.013 0.001  0.046  101 THR FFF C   
6759 O O   . THR F 101 ? 0.448 0.822 0.365 -0.012 0.005  0.044  101 THR FFF O   
6760 C CB  . THR F 101 ? 0.456 0.775 0.372 -0.001 0.014  0.026  101 THR FFF CB  
6761 O OG1 . THR F 101 ? 0.454 0.751 0.363 0.002  0.012  0.022  101 THR FFF OG1 
6762 C CG2 . THR F 101 ? 0.443 0.772 0.350 0.000  0.021  0.019  101 THR FFF CG2 
6763 N N   . THR F 102 ? 0.493 0.827 0.421 -0.016 -0.007 0.052  102 THR FFF N   
6764 C CA  . THR F 102 ? 0.500 0.841 0.425 -0.021 -0.011 0.055  102 THR FFF CA  
6765 C C   . THR F 102 ? 0.495 0.815 0.403 -0.013 -0.006 0.038  102 THR FFF C   
6766 O O   . THR F 102 ? 0.499 0.829 0.402 -0.014 -0.008 0.038  102 THR FFF O   
6767 C CB  . THR F 102 ? 0.520 0.853 0.462 -0.030 -0.025 0.068  102 THR FFF CB  
6768 O OG1 . THR F 102 ? 0.557 0.852 0.499 -0.025 -0.031 0.058  102 THR FFF OG1 
6769 C CG2 . THR F 102 ? 0.534 0.888 0.494 -0.040 -0.032 0.090  102 THR FFF CG2 
6770 N N   . ILE F 103 ? 0.493 0.792 0.393 -0.006 -0.001 0.027  103 ILE FFF N   
6771 C CA  . ILE F 103 ? 0.516 0.796 0.398 0.002  0.004  0.014  103 ILE FFF CA  
6772 C C   . ILE F 103 ? 0.506 0.796 0.378 0.005  0.014  0.010  103 ILE FFF C   
6773 O O   . ILE F 103 ? 0.497 0.791 0.372 0.006  0.020  0.009  103 ILE FFF O   
6774 C CB  . ILE F 103 ? 0.538 0.797 0.416 0.009  0.007  0.006  103 ILE FFF CB  
6775 C CG1 . ILE F 103 ? 0.562 0.808 0.452 0.008  -0.005 0.007  103 ILE FFF CG1 
6776 C CG2 . ILE F 103 ? 0.543 0.790 0.400 0.016  0.013  -0.004 103 ILE FFF CG2 
6777 C CD1 . ILE F 103 ? 0.571 0.800 0.458 0.019  -0.003 -0.006 103 ILE FFF CD1 
6778 N N   . VAL F 104 ? 0.514 0.807 0.377 0.006  0.012  0.008  104 VAL FFF N   
6779 C CA  . VAL F 104 ? 0.500 0.797 0.356 0.010  0.017  0.003  104 VAL FFF CA  
6780 C C   . VAL F 104 ? 0.505 0.778 0.345 0.016  0.021  -0.002 104 VAL FFF C   
6781 O O   . VAL F 104 ? 0.487 0.752 0.317 0.018  0.017  -0.003 104 VAL FFF O   
6782 C CB  . VAL F 104 ? 0.493 0.811 0.351 0.011  0.012  0.003  104 VAL FFF CB  
6783 C CG1 . VAL F 104 ? 0.499 0.819 0.353 0.018  0.014  -0.006 104 VAL FFF CG1 
6784 C CG2 . VAL F 104 ? 0.483 0.831 0.355 0.005  0.009  0.011  104 VAL FFF CG2 
6785 N N   . ARG F 105 ? 0.494 0.760 0.334 0.016  0.029  -0.003 105 ARG FFF N   
6786 C CA  . ARG F 105 ? 0.486 0.735 0.312 0.020  0.035  -0.003 105 ARG FFF CA  
6787 C C   . ARG F 105 ? 0.487 0.733 0.314 0.020  0.035  -0.002 105 ARG FFF C   
6788 O O   . ARG F 105 ? 0.518 0.770 0.359 0.017  0.037  -0.004 105 ARG FFF O   
6789 C CB  . ARG F 105 ? 0.485 0.733 0.314 0.019  0.043  -0.001 105 ARG FFF CB  
6790 C CG  . ARG F 105 ? 0.491 0.739 0.322 0.021  0.041  -0.005 105 ARG FFF CG  
6791 C CD  . ARG F 105 ? 0.522 0.770 0.353 0.025  0.050  -0.006 105 ARG FFF CD  
6792 N NE  . ARG F 105 ? 0.539 0.785 0.375 0.030  0.046  -0.012 105 ARG FFF NE  
6793 C CZ  . ARG F 105 ? 0.566 0.802 0.389 0.036  0.040  -0.020 105 ARG FFF CZ  
6794 N NH1 . ARG F 105 ? 0.581 0.811 0.385 0.038  0.039  -0.021 105 ARG FFF NH1 
6795 N NH2 . ARG F 105 ? 0.585 0.817 0.417 0.041  0.033  -0.027 105 ARG FFF NH2 
6796 N N   . ALA F 106 ? 0.486 0.722 0.301 0.024  0.031  -0.002 106 ALA FFF N   
6797 C CA  . ALA F 106 ? 0.501 0.728 0.319 0.026  0.028  -0.002 106 ALA FFF CA  
6798 C C   . ALA F 106 ? 0.509 0.726 0.333 0.021  0.035  0.005  106 ALA FFF C   
6799 O O   . ALA F 106 ? 0.517 0.730 0.354 0.019  0.030  0.002  106 ALA FFF O   
6800 C CB  . ALA F 106 ? 0.534 0.749 0.336 0.032  0.022  0.001  106 ALA FFF CB  
6801 N N   . TYR F 107 ? 0.523 0.739 0.339 0.018  0.044  0.012  107 TYR FFF N   
6802 C CA  . TYR F 107 ? 0.528 0.742 0.351 0.012  0.053  0.021  107 TYR FFF CA  
6803 C C   . TYR F 107 ? 0.510 0.741 0.348 0.009  0.058  0.016  107 TYR FFF C   
6804 O O   . TYR F 107 ? 0.508 0.747 0.339 0.012  0.062  0.014  107 TYR FFF O   
6805 C CB  . TYR F 107 ? 0.555 0.767 0.359 0.013  0.061  0.032  107 TYR FFF CB  
6806 C CG  . TYR F 107 ? 0.579 0.776 0.368 0.016  0.055  0.040  107 TYR FFF CG  
6807 C CD1 . TYR F 107 ? 0.599 0.783 0.395 0.010  0.054  0.054  107 TYR FFF CD1 
6808 C CD2 . TYR F 107 ? 0.575 0.770 0.344 0.024  0.050  0.036  107 TYR FFF CD2 
6809 C CE1 . TYR F 107 ? 0.619 0.787 0.401 0.013  0.048  0.064  107 TYR FFF CE1 
6810 C CE2 . TYR F 107 ? 0.586 0.768 0.340 0.028  0.044  0.044  107 TYR FFF CE2 
6811 C CZ  . TYR F 107 ? 0.609 0.778 0.369 0.022  0.043  0.059  107 TYR FFF CZ  
6812 O OH  . TYR F 107 ? 0.631 0.786 0.377 0.026  0.036  0.070  107 TYR FFF OH  
6813 N N   . TYR F 108 ? 0.489 0.725 0.347 0.004  0.055  0.012  108 TYR FFF N   
6814 C CA  . TYR F 108 ? 0.464 0.717 0.338 0.001  0.058  0.008  108 TYR FFF CA  
6815 C C   . TYR F 108 ? 0.468 0.728 0.344 -0.001 0.070  0.016  108 TYR FFF C   
6816 O O   . TYR F 108 ? 0.462 0.736 0.347 0.001  0.073  0.012  108 TYR FFF O   
6817 C CB  . TYR F 108 ? 0.452 0.710 0.346 -0.003 0.051  0.003  108 TYR FFF CB  
6818 C CG  . TYR F 108 ? 0.453 0.706 0.363 -0.011 0.054  0.009  108 TYR FFF CG  
6819 C CD1 . TYR F 108 ? 0.439 0.706 0.363 -0.017 0.061  0.013  108 TYR FFF CD1 
6820 C CD2 . TYR F 108 ? 0.474 0.707 0.386 -0.014 0.048  0.013  108 TYR FFF CD2 
6821 C CE1 . TYR F 108 ? 0.449 0.715 0.392 -0.027 0.064  0.022  108 TYR FFF CE1 
6822 C CE2 . TYR F 108 ? 0.486 0.713 0.416 -0.025 0.049  0.023  108 TYR FFF CE2 
6823 C CZ  . TYR F 108 ? 0.472 0.718 0.419 -0.032 0.057  0.028  108 TYR FFF CZ  
6824 O OH  . TYR F 108 ? 0.498 0.741 0.466 -0.044 0.058  0.039  108 TYR FFF OH  
6825 N N   . THR F 109 ? 0.486 0.739 0.357 -0.004 0.076  0.026  109 THR FFF N   
6826 C CA  . THR F 109 ? 0.492 0.759 0.365 -0.007 0.089  0.036  109 THR FFF CA  
6827 C C   . THR F 109 ? 0.498 0.776 0.355 0.004  0.095  0.030  109 THR FFF C   
6828 O O   . THR F 109 ? 0.509 0.805 0.368 0.006  0.106  0.033  109 THR FFF O   
6829 C CB  . THR F 109 ? 0.524 0.783 0.389 -0.013 0.093  0.053  109 THR FFF CB  
6830 O OG1 . THR F 109 ? 0.518 0.763 0.357 -0.005 0.089  0.052  109 THR FFF OG1 
6831 C CG2 . THR F 109 ? 0.529 0.774 0.415 -0.023 0.084  0.059  109 THR FFF CG2 
6832 N N   . GLU F 110 ? 0.491 0.758 0.333 0.011  0.087  0.021  110 GLU FFF N   
6833 C CA  . GLU F 110 ? 0.522 0.793 0.351 0.022  0.087  0.012  110 GLU FFF CA  
6834 C C   . GLU F 110 ? 0.502 0.775 0.345 0.024  0.081  0.002  110 GLU FFF C   
6835 O O   . GLU F 110 ? 0.538 0.810 0.376 0.033  0.078  -0.006 110 GLU FFF O   
6836 C CB  . GLU F 110 ? 0.537 0.793 0.342 0.027  0.080  0.010  110 GLU FFF CB  
6837 C CG  . GLU F 110 ? 0.576 0.830 0.362 0.026  0.086  0.021  110 GLU FFF CG  
6838 C CD  . GLU F 110 ? 0.616 0.861 0.376 0.034  0.080  0.017  110 GLU FFF CD  
6839 O OE1 . GLU F 110 ? 0.624 0.858 0.384 0.035  0.068  0.010  110 GLU FFF OE1 
6840 O OE2 . GLU F 110 ? 0.652 0.905 0.392 0.039  0.087  0.022  110 GLU FFF OE2 
6841 N N   . TYR F 111 ? 0.501 0.779 0.364 0.017  0.077  0.004  111 TYR FFF N   
6842 C CA  . TYR F 111 ? 0.491 0.774 0.370 0.019  0.070  -0.001 111 TYR FFF CA  
6843 C C   . TYR F 111 ? 0.495 0.791 0.385 0.024  0.077  -0.003 111 TYR FFF C   
6844 O O   . TYR F 111 ? 0.513 0.822 0.411 0.020  0.087  0.001  111 TYR FFF O   
6845 C CB  . TYR F 111 ? 0.477 0.766 0.369 0.011  0.064  0.001  111 TYR FFF CB  
6846 C CG  . TYR F 111 ? 0.453 0.736 0.337 0.010  0.054  0.000  111 TYR FFF CG  
6847 C CD1 . TYR F 111 ? 0.455 0.735 0.335 0.013  0.047  -0.000 111 TYR FFF CD1 
6848 C CD2 . TYR F 111 ? 0.446 0.730 0.330 0.007  0.051  -0.000 111 TYR FFF CD2 
6849 C CE1 . TYR F 111 ? 0.451 0.732 0.326 0.011  0.039  0.001  111 TYR FFF CE1 
6850 C CE2 . TYR F 111 ? 0.445 0.731 0.323 0.008  0.044  -0.002 111 TYR FFF CE2 
6851 C CZ  . TYR F 111 ? 0.443 0.730 0.317 0.009  0.039  0.000  111 TYR FFF CZ  
6852 O OH  . TYR F 111 ? 0.441 0.736 0.312 0.009  0.032  0.000  111 TYR FFF OH  
6853 N N   . THR F 112 ? 0.505 0.800 0.400 0.031  0.071  -0.010 112 THR FFF N   
6854 C CA  . THR F 112 ? 0.522 0.829 0.433 0.039  0.073  -0.015 112 THR FFF CA  
6855 C C   . THR F 112 ? 0.535 0.838 0.462 0.038  0.060  -0.014 112 THR FFF C   
6856 O O   . THR F 112 ? 0.522 0.813 0.444 0.033  0.050  -0.010 112 THR FFF O   
6857 C CB  . THR F 112 ? 0.537 0.844 0.437 0.053  0.077  -0.026 112 THR FFF CB  
6858 O OG1 . THR F 112 ? 0.535 0.823 0.433 0.059  0.063  -0.034 112 THR FFF OG1 
6859 C CG2 . THR F 112 ? 0.558 0.867 0.434 0.053  0.088  -0.024 112 THR FFF CG2 
6860 N N   . GLU F 113 ? 0.570 0.884 0.517 0.044  0.059  -0.016 113 GLU FFF N   
6861 C CA  . GLU F 113 ? 0.603 0.916 0.568 0.044  0.046  -0.012 113 GLU FFF CA  
6862 C C   . GLU F 113 ? 0.578 0.867 0.537 0.048  0.032  -0.014 113 GLU FFF C   
6863 O O   . GLU F 113 ? 0.569 0.853 0.537 0.041  0.019  -0.004 113 GLU FFF O   
6864 C CB  . GLU F 113 ? 0.654 0.984 0.641 0.052  0.048  -0.015 113 GLU FFF CB  
6865 C CG  . GLU F 113 ? 0.717 1.035 0.717 0.063  0.034  -0.019 113 GLU FFF CG  
6866 C CD  . GLU F 113 ? 0.773 1.085 0.769 0.079  0.036  -0.036 113 GLU FFF CD  
6867 O OE1 . GLU F 113 ? 0.820 1.154 0.821 0.088  0.049  -0.043 113 GLU FFF OE1 
6868 O OE2 . GLU F 113 ? 0.769 1.056 0.758 0.084  0.025  -0.042 113 GLU FFF OE2 
6869 N N   . ALA F 114 ? 0.533 0.810 0.480 0.057  0.033  -0.026 114 ALA FFF N   
6870 C CA  . ALA F 114 ? 0.523 0.775 0.467 0.061  0.018  -0.031 114 ALA FFF CA  
6871 C C   . ALA F 114 ? 0.503 0.747 0.440 0.047  0.011  -0.019 114 ALA FFF C   
6872 O O   . ALA F 114 ? 0.502 0.729 0.446 0.045  -0.005 -0.017 114 ALA FFF O   
6873 C CB  . ALA F 114 ? 0.538 0.784 0.465 0.074  0.022  -0.049 114 ALA FFF CB  
6874 N N   . ASP F 115 ? 0.483 0.739 0.407 0.038  0.021  -0.013 115 ASP FFF N   
6875 C CA  . ASP F 115 ? 0.476 0.731 0.393 0.028  0.016  -0.004 115 ASP FFF CA  
6876 C C   . ASP F 115 ? 0.475 0.743 0.408 0.018  0.008  0.011  115 ASP FFF C   
6877 O O   . ASP F 115 ? 0.465 0.736 0.397 0.010  0.002  0.019  115 ASP FFF O   
6878 C CB  . ASP F 115 ? 0.475 0.738 0.375 0.024  0.028  -0.004 115 ASP FFF CB  
6879 C CG  . ASP F 115 ? 0.496 0.752 0.378 0.032  0.036  -0.014 115 ASP FFF CG  
6880 O OD1 . ASP F 115 ? 0.516 0.758 0.391 0.039  0.029  -0.022 115 ASP FFF OD1 
6881 O OD2 . ASP F 115 ? 0.524 0.788 0.399 0.031  0.048  -0.013 115 ASP FFF OD2 
6882 N N   . PHE F 116 ? 0.458 0.737 0.406 0.020  0.009  0.014  116 PHE FFF N   
6883 C CA  . PHE F 116 ? 0.442 0.741 0.401 0.012  0.004  0.028  116 PHE FFF CA  
6884 C C   . PHE F 116 ? 0.459 0.751 0.437 0.012  -0.010 0.038  116 PHE FFF C   
6885 O O   . PHE F 116 ? 0.491 0.765 0.478 0.022  -0.015 0.030  116 PHE FFF O   
6886 C CB  . PHE F 116 ? 0.414 0.732 0.375 0.013  0.014  0.024  116 PHE FFF CB  
6887 C CG  . PHE F 116 ? 0.400 0.723 0.347 0.010  0.024  0.018  116 PHE FFF CG  
6888 C CD1 . PHE F 116 ? 0.410 0.720 0.346 0.014  0.034  0.009  116 PHE FFF CD1 
6889 C CD2 . PHE F 116 ? 0.383 0.724 0.326 0.004  0.023  0.021  116 PHE FFF CD2 
6890 C CE1 . PHE F 116 ? 0.408 0.720 0.334 0.011  0.040  0.006  116 PHE FFF CE1 
6891 C CE2 . PHE F 116 ? 0.378 0.719 0.311 0.003  0.030  0.014  116 PHE FFF CE2 
6892 C CZ  . PHE F 116 ? 0.391 0.715 0.316 0.006  0.038  0.008  116 PHE FFF CZ  
6893 N N   . GLY F 117 ? 0.467 0.775 0.452 0.003  -0.018 0.056  117 GLY FFF N   
6894 C CA  . GLY F 117 ? 0.478 0.784 0.482 -0.000 -0.033 0.073  117 GLY FFF CA  
6895 C C   . GLY F 117 ? 0.473 0.813 0.480 -0.007 -0.034 0.090  117 GLY FFF C   
6896 O O   . GLY F 117 ? 0.466 0.828 0.461 -0.006 -0.023 0.082  117 GLY FFF O   
6897 N N   . SER F 118 ? 0.480 0.824 0.503 -0.012 -0.048 0.112  118 SER FFF N   
6898 C CA  . SER F 118 ? 0.483 0.863 0.508 -0.018 -0.051 0.130  118 SER FFF CA  
6899 C C   . SER F 118 ? 0.463 0.857 0.486 -0.009 -0.043 0.116  118 SER FFF C   
6900 O O   . SER F 118 ? 0.460 0.886 0.472 -0.011 -0.037 0.115  118 SER FFF O   
6901 C CB  . SER F 118 ? 0.489 0.902 0.500 -0.027 -0.046 0.140  118 SER FFF CB  
6902 O OG  . SER F 118 ? 0.509 0.915 0.527 -0.038 -0.055 0.157  118 SER FFF OG  
6903 N N   . TRP F 119 ? 0.444 0.816 0.479 0.002  -0.043 0.103  119 TRP FFF N   
6904 C CA  . TRP F 119 ? 0.434 0.819 0.472 0.010  -0.036 0.090  119 TRP FFF CA  
6905 C C   . TRP F 119 ? 0.432 0.848 0.478 0.007  -0.044 0.105  119 TRP FFF C   
6906 O O   . TRP F 119 ? 0.420 0.832 0.478 0.006  -0.059 0.125  119 TRP FFF O   
6907 C CB  . TRP F 119 ? 0.439 0.801 0.493 0.022  -0.037 0.077  119 TRP FFF CB  
6908 C CG  . TRP F 119 ? 0.442 0.782 0.485 0.026  -0.027 0.058  119 TRP FFF CG  
6909 C CD1 . TRP F 119 ? 0.463 0.774 0.505 0.028  -0.033 0.056  119 TRP FFF CD1 
6910 C CD2 . TRP F 119 ? 0.424 0.771 0.456 0.028  -0.010 0.042  119 TRP FFF CD2 
6911 N NE1 . TRP F 119 ? 0.463 0.766 0.491 0.033  -0.020 0.038  119 TRP FFF NE1 
6912 C CE2 . TRP F 119 ? 0.441 0.765 0.463 0.032  -0.005 0.031  119 TRP FFF CE2 
6913 C CE3 . TRP F 119 ? 0.410 0.780 0.441 0.026  0.000  0.036  119 TRP FFF CE3 
6914 C CZ2 . TRP F 119 ? 0.431 0.756 0.440 0.034  0.010  0.017  119 TRP FFF CZ2 
6915 C CZ3 . TRP F 119 ? 0.420 0.788 0.443 0.026  0.014  0.023  119 TRP FFF CZ3 
6916 C CH2 . TRP F 119 ? 0.423 0.770 0.434 0.030  0.020  0.015  119 TRP FFF CH2 
6917 N N   . GLY F 120 ? 0.428 0.872 0.466 0.007  -0.037 0.096  120 GLY FFF N   
6918 C CA  . GLY F 120 ? 0.467 0.942 0.511 0.008  -0.044 0.104  120 GLY FFF CA  
6919 C C   . GLY F 120 ? 0.489 0.955 0.555 0.017  -0.050 0.101  120 GLY FFF C   
6920 O O   . GLY F 120 ? 0.500 0.943 0.575 0.024  -0.043 0.087  120 GLY FFF O   
6921 N N   . GLN F 121 ? 0.527 1.015 0.604 0.019  -0.062 0.115  121 GLN FFF N   
6922 C CA  . GLN F 121 ? 0.548 1.037 0.649 0.030  -0.068 0.111  121 GLN FFF CA  
6923 C C   . GLN F 121 ? 0.546 1.051 0.649 0.031  -0.056 0.087  121 GLN FFF C   
6924 O O   . GLN F 121 ? 0.606 1.132 0.695 0.025  -0.051 0.081  121 GLN FFF O   
6925 C CB  . GLN F 121 ? 0.585 1.094 0.695 0.030  -0.085 0.134  121 GLN FFF CB  
6926 C CG  . GLN F 121 ? 0.607 1.160 0.708 0.028  -0.087 0.134  121 GLN FFF CG  
6927 C CD  . GLN F 121 ? 0.624 1.200 0.698 0.019  -0.082 0.136  121 GLN FFF CD  
6928 O OE1 . GLN F 121 ? 0.619 1.181 0.680 0.012  -0.077 0.143  121 GLN FFF OE1 
6929 N NE2 . GLN F 121 ? 0.616 1.229 0.681 0.019  -0.083 0.128  121 GLN FFF NE2 
6930 N N   . GLY F 122 ? 0.523 1.017 0.644 0.040  -0.050 0.073  122 GLY FFF N   
6931 C CA  . GLY F 122 ? 0.520 1.028 0.648 0.039  -0.038 0.054  122 GLY FFF CA  
6932 C C   . GLY F 122 ? 0.512 1.055 0.649 0.037  -0.046 0.054  122 GLY FFF C   
6933 O O   . GLY F 122 ? 0.557 1.113 0.702 0.041  -0.060 0.067  122 GLY FFF O   
6934 N N   . THR F 123 ? 0.474 1.031 0.609 0.030  -0.038 0.039  123 THR FFF N   
6935 C CA  . THR F 123 ? 0.466 1.055 0.613 0.028  -0.046 0.033  123 THR FFF CA  
6936 C C   . THR F 123 ? 0.459 1.053 0.631 0.026  -0.037 0.019  123 THR FFF C   
6937 O O   . THR F 123 ? 0.459 1.036 0.625 0.020  -0.023 0.011  123 THR FFF O   
6938 C CB  . THR F 123 ? 0.470 1.072 0.594 0.021  -0.051 0.028  123 THR FFF CB  
6939 O OG1 . THR F 123 ? 0.484 1.118 0.619 0.021  -0.062 0.021  123 THR FFF OG1 
6940 C CG2 . THR F 123 ? 0.473 1.059 0.586 0.013  -0.039 0.014  123 THR FFF CG2 
6941 N N   . GLN F 124 ? 0.447 1.066 0.647 0.030  -0.044 0.017  124 GLN FFF N   
6942 C CA  . GLN F 124 ? 0.429 1.060 0.659 0.028  -0.036 0.007  124 GLN FFF CA  
6943 C C   . GLN F 124 ? 0.418 1.061 0.652 0.015  -0.037 -0.005 124 GLN FFF C   
6944 O O   . GLN F 124 ? 0.413 1.071 0.641 0.013  -0.051 -0.008 124 GLN FFF O   
6945 C CB  . GLN F 124 ? 0.432 1.089 0.692 0.039  -0.045 0.010  124 GLN FFF CB  
6946 C CG  . GLN F 124 ? 0.425 1.105 0.721 0.037  -0.036 0.002  124 GLN FFF CG  
6947 C CD  . GLN F 124 ? 0.426 1.092 0.724 0.041  -0.017 -0.000 124 GLN FFF CD  
6948 O OE1 . GLN F 124 ? 0.425 1.092 0.727 0.031  -0.003 -0.005 124 GLN FFF OE1 
6949 N NE2 . GLN F 124 ? 0.433 1.086 0.728 0.057  -0.017 0.003  124 GLN FFF NE2 
6950 N N   . VAL F 125 ? 0.423 1.058 0.667 0.006  -0.023 -0.010 125 VAL FFF N   
6951 C CA  . VAL F 125 ? 0.419 1.062 0.677 -0.008 -0.024 -0.021 125 VAL FFF CA  
6952 C C   . VAL F 125 ? 0.422 1.087 0.720 -0.013 -0.016 -0.020 125 VAL FFF C   
6953 O O   . VAL F 125 ? 0.410 1.069 0.709 -0.009 0.001  -0.014 125 VAL FFF O   
6954 C CB  . VAL F 125 ? 0.427 1.040 0.662 -0.017 -0.016 -0.024 125 VAL FFF CB  
6955 C CG1 . VAL F 125 ? 0.430 1.044 0.684 -0.032 -0.021 -0.033 125 VAL FFF CG1 
6956 C CG2 . VAL F 125 ? 0.435 1.032 0.633 -0.011 -0.022 -0.024 125 VAL FFF CG2 
6957 N N   . THR F 126 ? 0.432 1.125 0.761 -0.019 -0.028 -0.026 126 THR FFF N   
6958 C CA  . THR F 126 ? 0.427 1.151 0.800 -0.025 -0.022 -0.024 126 THR FFF CA  
6959 C C   . THR F 126 ? 0.434 1.163 0.830 -0.045 -0.029 -0.031 126 THR FFF C   
6960 O O   . THR F 126 ? 0.414 1.146 0.808 -0.048 -0.049 -0.042 126 THR FFF O   
6961 C CB  . THR F 126 ? 0.436 1.192 0.831 -0.012 -0.032 -0.024 126 THR FFF CB  
6962 O OG1 . THR F 126 ? 0.443 1.186 0.815 0.006  -0.029 -0.017 126 THR FFF OG1 
6963 C CG2 . THR F 126 ? 0.429 1.223 0.871 -0.015 -0.025 -0.022 126 THR FFF CG2 
6964 N N   . VAL F 127 ? 0.451 1.183 0.869 -0.058 -0.015 -0.024 127 VAL FFF N   
6965 C CA  . VAL F 127 ? 0.476 1.210 0.925 -0.081 -0.022 -0.027 127 VAL FFF CA  
6966 C C   . VAL F 127 ? 0.498 1.275 0.996 -0.089 -0.014 -0.017 127 VAL FFF C   
6967 O O   . VAL F 127 ? 0.489 1.278 0.989 -0.085 0.009  -0.005 127 VAL FFF O   
6968 C CB  . VAL F 127 ? 0.471 1.167 0.899 -0.092 -0.013 -0.022 127 VAL FFF CB  
6969 C CG1 . VAL F 127 ? 0.488 1.177 0.947 -0.114 -0.025 -0.025 127 VAL FFF CG1 
6970 C CG2 . VAL F 127 ? 0.468 1.127 0.846 -0.080 -0.016 -0.029 127 VAL FFF CG2 
6971 N N   . SER F 128 ? 0.527 1.329 1.065 -0.101 -0.031 -0.024 128 SER FFF N   
6972 C CA  . SER F 128 ? 0.545 1.398 1.137 -0.108 -0.028 -0.017 128 SER FFF CA  
6973 C C   . SER F 128 ? 0.573 1.432 1.209 -0.136 -0.039 -0.015 128 SER FFF C   
6974 O O   . SER F 128 ? 0.597 1.416 1.219 -0.147 -0.051 -0.022 128 SER FFF O   
6975 C CB  . SER F 128 ? 0.542 1.427 1.146 -0.092 -0.041 -0.025 128 SER FFF CB  
6976 O OG  . SER F 128 ? 0.553 1.427 1.119 -0.067 -0.034 -0.025 128 SER FFF OG  
6977 N N   . SER F 129 ? 0.598 1.506 1.288 -0.147 -0.037 -0.007 129 SER FFF N   
6978 C CA  . SER F 129 ? 0.603 1.525 1.347 -0.176 -0.051 -0.004 129 SER FFF CA  
6979 C C   . SER F 129 ? 0.599 1.578 1.393 -0.176 -0.061 -0.007 129 SER FFF C   
6980 O O   . SER F 129 ? 0.604 1.589 1.394 -0.164 -0.083 -0.025 129 SER FFF O   
6981 C CB  . SER F 129 ? 0.609 1.533 1.373 -0.198 -0.030 0.020  129 SER FFF CB  
6982 O OG  . SER F 129 ? 0.620 1.490 1.338 -0.197 -0.024 0.023  129 SER FFF OG  
# 
