data_8GPK
# 
_entry.id   8GPK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.373 
_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   8GPK         pdb_00008gpk 10.2210/pdb8gpk/pdb 
WWPDB D_1300031831 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB . EMD-34190 'other EM volume' 
EMDB . EMD-34192 'other EM volume' 
EMDB . EMD-34193 'other EM volume' 
EMDB . EMD-34194 'other EM volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8GPK 
_pdbx_database_status.recvd_initial_deposition_date   2022-08-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Niu, J.'  1 ? 
'Yang, B.' 2 ? 
# 
_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                     
'Structure and immune recognition of Env timers from two Asia prevalent HIV-1 circulating recombinant forms' 
_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 'Niu, J.'  1 ? 
primary 'Yang, B.' 2 ? 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   105.18 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8GPK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     91.245 
_cell.length_a_esd                 ? 
_cell.length_b                     62.271 
_cell.length_b_esd                 ? 
_cell.length_c                     97.843 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8GPK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'F6 Fab heavy Chain' 25333.791 2 ? ? ? ? 
2 polymer man 'F6 Fab light chain' 24109.902 2 ? ? ? ? 
# 
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 
;QVQLQQWGTGLLKPSETLSLTCAVYGVSLRGYYWTWIRQSPKKGLEWIGEIDEIGRTKYSQSLRSRATLSIDTSKKQFSL
RLTSVTAADMATYYCARWRLMMVDEVTRHGMDVWSQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEP
VTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
;
;QVQLQQWGTGLLKPSETLSLTCAVYGVSLRGYYWTWIRQSPKKGLEWIGEIDEIGRTKYSQSLRSRATLSIDTSKKQFSL
RLTSVTAADMATYYCARWRLMMVDEVTRHGMDVWSQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEP
VTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
;
A,C ? 
2 'polypeptide(L)' no no 
;DIVMTQSPLSLSVAPGEAASISCRSTQSLLNRNGDNYLEWYLRRPGRSPQLLIYLGSERALGVPDRFSGSGSGRDFTLKI
SRVEAQDVGTYYCLQTRQGAFTFGQGTKLEIKRTVAAPSVFIFPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ
SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECG
;
;DIVMTQSPLSLSVAPGEAASISCRSTQSLLNRNGDNYLEWYLRRPGRSPQLLIYLGSERALGVPDRFSGSGSGRDFTLKI
SRVEAQDVGTYYCLQTRQGAFTFGQGTKLEIKRTVAAPSVFIFPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ
SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECG
;
B,D ? 
# 
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   GLN n 
1 6   GLN n 
1 7   TRP n 
1 8   GLY n 
1 9   THR n 
1 10  GLY n 
1 11  LEU n 
1 12  LEU n 
1 13  LYS n 
1 14  PRO n 
1 15  SER n 
1 16  GLU n 
1 17  THR n 
1 18  LEU n 
1 19  SER n 
1 20  LEU n 
1 21  THR n 
1 22  CYS n 
1 23  ALA n 
1 24  VAL n 
1 25  TYR n 
1 26  GLY n 
1 27  VAL n 
1 28  SER n 
1 29  LEU n 
1 30  ARG n 
1 31  GLY n 
1 32  TYR n 
1 33  TYR n 
1 34  TRP n 
1 35  THR n 
1 36  TRP n 
1 37  ILE n 
1 38  ARG n 
1 39  GLN n 
1 40  SER n 
1 41  PRO n 
1 42  LYS n 
1 43  LYS n 
1 44  GLY n 
1 45  LEU n 
1 46  GLU n 
1 47  TRP n 
1 48  ILE n 
1 49  GLY n 
1 50  GLU n 
1 51  ILE n 
1 52  ASP n 
1 53  GLU n 
1 54  ILE n 
1 55  GLY n 
1 56  ARG n 
1 57  THR n 
1 58  LYS n 
1 59  TYR n 
1 60  SER n 
1 61  GLN n 
1 62  SER n 
1 63  LEU n 
1 64  ARG n 
1 65  SER n 
1 66  ARG n 
1 67  ALA n 
1 68  THR n 
1 69  LEU n 
1 70  SER n 
1 71  ILE n 
1 72  ASP n 
1 73  THR n 
1 74  SER n 
1 75  LYS n 
1 76  LYS n 
1 77  GLN n 
1 78  PHE n 
1 79  SER n 
1 80  LEU n 
1 81  ARG n 
1 82  LEU n 
1 83  THR n 
1 84  SER n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  ALA n 
1 89  ASP n 
1 90  MET n 
1 91  ALA n 
1 92  THR n 
1 93  TYR n 
1 94  TYR n 
1 95  CYS n 
1 96  ALA n 
1 97  ARG n 
1 98  TRP n 
1 99  ARG n 
1 100 LEU n 
1 101 MET n 
1 102 MET n 
1 103 VAL n 
1 104 ASP n 
1 105 GLU n 
1 106 VAL n 
1 107 THR n 
1 108 ARG n 
1 109 HIS n 
1 110 GLY n 
1 111 MET n 
1 112 ASP n 
1 113 VAL n 
1 114 TRP n 
1 115 SER n 
1 116 GLN n 
1 117 GLY n 
1 118 THR n 
1 119 MET n 
1 120 VAL n 
1 121 THR n 
1 122 VAL n 
1 123 SER n 
1 124 SER n 
1 125 ALA n 
1 126 SER n 
1 127 THR n 
1 128 LYS n 
1 129 GLY n 
1 130 PRO n 
1 131 SER n 
1 132 VAL n 
1 133 PHE n 
1 134 PRO n 
1 135 LEU n 
1 136 ALA n 
1 137 PRO n 
1 138 SER n 
1 139 SER n 
1 140 LYS n 
1 141 SER n 
1 142 THR n 
1 143 SER n 
1 144 GLY n 
1 145 GLY n 
1 146 THR n 
1 147 ALA n 
1 148 ALA n 
1 149 LEU n 
1 150 GLY n 
1 151 CYS n 
1 152 LEU n 
1 153 VAL n 
1 154 LYS n 
1 155 ASP n 
1 156 TYR n 
1 157 PHE n 
1 158 PRO n 
1 159 GLU n 
1 160 PRO n 
1 161 VAL n 
1 162 THR n 
1 163 VAL n 
1 164 SER n 
1 165 TRP n 
1 166 ASN n 
1 167 SER n 
1 168 GLY n 
1 169 ALA n 
1 170 LEU n 
1 171 THR n 
1 172 SER n 
1 173 GLY n 
1 174 VAL n 
1 175 HIS n 
1 176 THR n 
1 177 PHE n 
1 178 PRO n 
1 179 ALA n 
1 180 VAL n 
1 181 LEU n 
1 182 GLN n 
1 183 SER n 
1 184 SER n 
1 185 GLY n 
1 186 LEU n 
1 187 TYR n 
1 188 SER n 
1 189 LEU n 
1 190 SER n 
1 191 SER n 
1 192 VAL n 
1 193 VAL n 
1 194 THR n 
1 195 VAL n 
1 196 PRO n 
1 197 SER n 
1 198 SER n 
1 199 SER n 
1 200 LEU n 
1 201 GLY n 
1 202 THR n 
1 203 GLN n 
1 204 THR n 
1 205 TYR n 
1 206 ILE n 
1 207 CYS n 
1 208 ASN n 
1 209 VAL n 
1 210 ASN n 
1 211 HIS n 
1 212 LYS n 
1 213 PRO n 
1 214 SER n 
1 215 ASN n 
1 216 THR n 
1 217 LYS n 
1 218 VAL n 
1 219 ASP n 
1 220 LYS n 
1 221 LYS n 
1 222 VAL n 
1 223 GLU n 
1 224 PRO n 
1 225 LYS n 
1 226 SER n 
1 227 CYS n 
1 228 ASP n 
1 229 LYS n 
1 230 THR n 
1 231 HIS n 
1 232 THR n 
2 1   ASP n 
2 2   ILE n 
2 3   VAL n 
2 4   MET n 
2 5   THR n 
2 6   GLN n 
2 7   SER n 
2 8   PRO n 
2 9   LEU n 
2 10  SER n 
2 11  LEU n 
2 12  SER n 
2 13  VAL n 
2 14  ALA n 
2 15  PRO n 
2 16  GLY n 
2 17  GLU n 
2 18  ALA n 
2 19  ALA n 
2 20  SER n 
2 21  ILE n 
2 22  SER n 
2 23  CYS n 
2 24  ARG n 
2 25  SER n 
2 26  THR n 
2 27  GLN n 
2 28  SER n 
2 29  LEU n 
2 30  LEU n 
2 31  ASN n 
2 32  ARG n 
2 33  ASN n 
2 34  GLY n 
2 35  ASP n 
2 36  ASN n 
2 37  TYR n 
2 38  LEU n 
2 39  GLU n 
2 40  TRP n 
2 41  TYR n 
2 42  LEU n 
2 43  ARG n 
2 44  ARG n 
2 45  PRO n 
2 46  GLY n 
2 47  ARG n 
2 48  SER n 
2 49  PRO n 
2 50  GLN n 
2 51  LEU n 
2 52  LEU n 
2 53  ILE n 
2 54  TYR n 
2 55  LEU n 
2 56  GLY n 
2 57  SER n 
2 58  GLU n 
2 59  ARG n 
2 60  ALA n 
2 61  LEU n 
2 62  GLY n 
2 63  VAL n 
2 64  PRO n 
2 65  ASP n 
2 66  ARG n 
2 67  PHE n 
2 68  SER n 
2 69  GLY n 
2 70  SER n 
2 71  GLY n 
2 72  SER n 
2 73  GLY n 
2 74  ARG n 
2 75  ASP n 
2 76  PHE n 
2 77  THR n 
2 78  LEU n 
2 79  LYS n 
2 80  ILE n 
2 81  SER n 
2 82  ARG n 
2 83  VAL n 
2 84  GLU n 
2 85  ALA n 
2 86  GLN n 
2 87  ASP n 
2 88  VAL n 
2 89  GLY n 
2 90  THR n 
2 91  TYR n 
2 92  TYR n 
2 93  CYS n 
2 94  LEU n 
2 95  GLN n 
2 96  THR n 
2 97  ARG n 
2 98  GLN n 
2 99  GLY n 
2 100 ALA n 
2 101 PHE n 
2 102 THR n 
2 103 PHE n 
2 104 GLY n 
2 105 GLN n 
2 106 GLY n 
2 107 THR n 
2 108 LYS n 
2 109 LEU n 
2 110 GLU n 
2 111 ILE n 
2 112 LYS n 
2 113 ARG n 
2 114 THR n 
2 115 VAL n 
2 116 ALA n 
2 117 ALA n 
2 118 PRO n 
2 119 SER n 
2 120 VAL n 
2 121 PHE n 
2 122 ILE n 
2 123 PHE n 
2 124 PRO n 
2 125 PRO n 
2 126 SER n 
2 127 ASP n 
2 128 SER n 
2 129 GLN n 
2 130 LEU n 
2 131 LYS n 
2 132 SER n 
2 133 GLY n 
2 134 THR n 
2 135 ALA n 
2 136 SER n 
2 137 VAL n 
2 138 VAL n 
2 139 CYS n 
2 140 LEU n 
2 141 LEU n 
2 142 ASN n 
2 143 ASN n 
2 144 PHE n 
2 145 TYR n 
2 146 PRO n 
2 147 ARG n 
2 148 GLU n 
2 149 ALA n 
2 150 LYS n 
2 151 VAL n 
2 152 GLN n 
2 153 TRP n 
2 154 LYS n 
2 155 VAL n 
2 156 ASP n 
2 157 ASN n 
2 158 ALA n 
2 159 LEU n 
2 160 GLN n 
2 161 SER n 
2 162 GLY n 
2 163 ASN n 
2 164 SER n 
2 165 GLN n 
2 166 GLU n 
2 167 SER n 
2 168 VAL n 
2 169 THR n 
2 170 GLU n 
2 171 GLN n 
2 172 ASP n 
2 173 SER n 
2 174 LYS n 
2 175 ASP n 
2 176 SER n 
2 177 THR n 
2 178 TYR n 
2 179 SER n 
2 180 LEU n 
2 181 SER n 
2 182 SER n 
2 183 THR n 
2 184 LEU n 
2 185 THR n 
2 186 LEU n 
2 187 SER n 
2 188 LYS n 
2 189 ALA n 
2 190 ASP n 
2 191 TYR n 
2 192 GLU n 
2 193 LYS n 
2 194 HIS n 
2 195 LYS n 
2 196 VAL n 
2 197 TYR n 
2 198 ALA n 
2 199 CYS n 
2 200 GLU n 
2 201 VAL n 
2 202 THR n 
2 203 HIS n 
2 204 GLN n 
2 205 GLY n 
2 206 LEU n 
2 207 SER n 
2 208 SER n 
2 209 PRO n 
2 210 VAL n 
2 211 THR n 
2 212 LYS n 
2 213 SER n 
2 214 PHE n 
2 215 ASN n 
2 216 ARG n 
2 217 GLY n 
2 218 GLU n 
2 219 CYS n 
2 220 GLY 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' 1 232 ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Cricetulus griseus' 10029 ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 220 ? ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Cricetulus griseus' 10029 ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 8GPK 8GPK ? 1 ? 1 
2 PDB 8GPK 8GPK ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8GPK A 1 ? 232 ? 8GPK 1 ? 232 ? 1 232 
2 2 8GPK B 1 ? 220 ? 8GPK 1 ? 220 ? 1 220 
3 1 8GPK C 1 ? 232 ? 8GPK 1 ? 232 ? 1 232 
4 2 8GPK D 1 ? 220 ? 8GPK 1 ? 220 ? 1 220 
# 
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 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8GPK 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.66 
_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, HANGING 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    '0.2 M sodium citrate, 20% PEG 3,350.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-11-13 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          63.58 
_reflns.entry_id                                       8GPK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.3 
_reflns.d_resolution_low                               19.71 
_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                                     29265 
_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                           97.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.11 
_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                                0.24 
_reflns.pdbx_Rpim_I_all                                0.13 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.97 
_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                                    3.3 
_reflns_shell.d_res_low                                     3.5 
_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                             1352 
_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                                  0.87 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8GPK 
_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                            3.34 
_refine.ls_d_res_low                             19.71 
_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                     29265 
_refine.ls_number_reflns_R_free                  2955 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.34 
_refine.ls_percent_reflns_R_free                 10.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2455 
_refine.ls_R_factor_R_free                       0.2806 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2417 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.35 
_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                      5BMF 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 30.28 
_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                             ? 
_refine.overall_SU_ML                            0.42 
_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.details                          ? 
_refine_hist.d_res_high                       3.34 
_refine_hist.d_res_low                        19.71 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               5758 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5758 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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 ? 5875 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.741 ? 7964 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.360 ? 810  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046 ? 900  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1007 ? f_plane_restr      ? ? 
# 
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' 3.34 3.39  . . 91  817  63.00  . . . . 0.3573 . . . . . . . . . . . 0.3527 
'X-RAY DIFFRACTION' 3.39 3.45  . . 156 1243 97.00  . . . . 0.2985 . . . . . . . . . . . 0.3186 
'X-RAY DIFFRACTION' 3.45 3.51  . . 130 1284 100.00 . . . . 0.3033 . . . . . . . . . . . 0.2961 
'X-RAY DIFFRACTION' 3.51 3.58  . . 126 1254 98.00  . . . . 0.2911 . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 3.58 3.65  . . 169 1288 100.00 . . . . 0.2659 . . . . . . . . . . . 0.3645 
'X-RAY DIFFRACTION' 3.65 3.73  . . 126 1276 100.00 . . . . 0.2747 . . . . . . . . . . . 0.2791 
'X-RAY DIFFRACTION' 3.73 3.82  . . 162 1272 100.00 . . . . 0.2571 . . . . . . . . . . . 0.2711 
'X-RAY DIFFRACTION' 3.82 3.91  . . 115 1304 100.00 . . . . 0.2517 . . . . . . . . . . . 0.3176 
'X-RAY DIFFRACTION' 3.91 4.02  . . 150 1263 100.00 . . . . 0.2603 . . . . . . . . . . . 0.2887 
'X-RAY DIFFRACTION' 4.02 4.14  . . 148 1319 100.00 . . . . 0.2271 . . . . . . . . . . . 0.2991 
'X-RAY DIFFRACTION' 4.14 4.27  . . 156 1249 99.00  . . . . 0.2289 . . . . . . . . . . . 0.2804 
'X-RAY DIFFRACTION' 4.27 4.42  . . 135 1299 98.00  . . . . 0.2247 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 4.42 4.59  . . 139 1255 100.00 . . . . 0.2057 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 4.59 4.80  . . 162 1285 100.00 . . . . 0.2039 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 4.80 5.05  . . 151 1254 100.00 . . . . 0.2131 . . . . . . . . . . . 0.2322 
'X-RAY DIFFRACTION' 5.05 5.36  . . 130 1296 100.00 . . . . 0.2139 . . . . . . . . . . . 0.2626 
'X-RAY DIFFRACTION' 5.36 5.76  . . 149 1261 98.00  . . . . 0.2393 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 5.76 6.32  . . 141 1257 99.00  . . . . 0.2556 . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 6.33 7.20  . . 140 1301 100.00 . . . . 0.2544 . . . . . . . . . . . 0.2715 
'X-RAY DIFFRACTION' 7.20 8.93  . . 138 1269 98.00  . . . . 0.2282 . . . . . . . . . . . 0.2472 
'X-RAY DIFFRACTION' 8.93 19.71 . . 141 1264 98.00  . . . . 0.2302 . . . . . . . . . . . 0.2669 
# 
_struct.entry_id                     8GPK 
_struct.title                        'Crystal structure of human anti-HIV-1 broadly neutralizing antibody F6 Fab' 
_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        8GPK 
_struct_keywords.text            'Antibody, Fab, HIV-1, Env binding, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
# 
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 SER A 60  ? SER A 65  ? SER A 60  SER A 65  1 ? 6 
HELX_P HELX_P2 AA2 SER A 198 ? LEU A 200 ? SER A 198 LEU A 200 5 ? 3 
HELX_P HELX_P3 AA3 LYS A 212 ? ASN A 215 ? LYS A 212 ASN A 215 5 ? 4 
HELX_P HELX_P4 AA4 GLU B 84  ? VAL B 88  ? GLU B 84  VAL B 88  5 ? 5 
HELX_P HELX_P5 AA5 SER B 126 ? GLY B 133 ? SER B 126 GLY B 133 1 ? 8 
HELX_P HELX_P6 AA6 LYS B 188 ? HIS B 194 ? LYS B 188 HIS B 194 1 ? 7 
HELX_P HELX_P7 AA7 THR C 86  ? MET C 90  ? THR C 86  MET C 90  5 ? 5 
HELX_P HELX_P8 AA8 GLU D 84  ? VAL D 88  ? GLU D 84  VAL D 88  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 95  SG ? ? A CYS 22  A CYS 95  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf2 disulf ? ? A CYS 151 SG ? ? ? 1_555 A CYS 207 SG ? ? A CYS 151 A CYS 207 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf3 disulf ? ? B CYS 23  SG ? ? ? 1_555 B CYS 93  SG ? ? B CYS 23  B CYS 93  1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf4 disulf ? ? B CYS 139 SG ? ? ? 1_555 B CYS 199 SG ? ? B CYS 139 B CYS 199 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf5 disulf ? ? C CYS 22  SG ? ? ? 1_555 C CYS 95  SG ? ? C CYS 22  C CYS 95  1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf6 disulf ? ? C CYS 151 SG ? ? ? 1_555 C CYS 207 SG ? ? C CYS 151 C CYS 207 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf7 disulf ? ? D CYS 23  SG ? ? ? 1_555 D CYS 93  SG ? ? D CYS 23  D CYS 93  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 157 A . ? PHE 157 A PRO 158 A ? PRO 158 A 1 -9.29  
2 TYR 145 B . ? TYR 145 B PRO 146 B ? PRO 146 B 1 -2.18  
3 SER 7   D . ? SER 7   D PRO 8   D ? PRO 8   D 1 -10.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 5 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 7 ? 
AB2 ? 6 ? 
AB3 ? 4 ? 
AB4 ? 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 7 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 2 5 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 5 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 5 ? anti-parallel 
AA3 3 5 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 7 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 2 5 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 5 7 ? anti-parallel 
AB2 1 5 ? anti-parallel 
AB2 2 6 ? anti-parallel 
AB2 3 5 ? anti-parallel 
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
# 
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   ? GLY A 8   ? GLN A 3   GLY A 8   
AA1 2 LEU A 18  ? TYR A 25  ? LEU A 18  TYR A 25  
AA1 3 GLN A 77  ? LEU A 82  ? GLN A 77  LEU A 82  
AA1 4 ALA A 67  ? ASP A 72  ? ALA A 67  ASP A 72  
AA2 1 LEU A 11  ? LEU A 12  ? LEU A 11  LEU A 12  
AA2 2 TRP A 34  ? SER A 40  ? TRP A 34  SER A 40  
AA2 3 GLY A 44  ? ILE A 51  ? GLY A 44  ILE A 51  
AA2 4 THR A 57  ? TYR A 59  ? THR A 57  TYR A 59  
AA2 5 ALA A 91  ? MET A 102 ? ALA A 91  MET A 102 
AA2 6 VAL A 106 ? TRP A 114 ? VAL A 106 TRP A 114 
AA2 7 THR A 118 ? VAL A 122 ? THR A 118 VAL A 122 
AA3 1 VAL A 132 ? LEU A 135 ? VAL A 132 LEU A 135 
AA3 2 THR A 146 ? TYR A 156 ? THR A 146 TYR A 156 
AA3 3 VAL A 174 ? THR A 176 ? VAL A 174 THR A 176 
AA3 4 VAL A 180 ? LEU A 181 ? VAL A 180 LEU A 181 
AA3 5 TYR A 187 ? PRO A 196 ? TYR A 187 PRO A 196 
AA4 1 THR A 162 ? TRP A 165 ? THR A 162 TRP A 165 
AA4 2 ILE A 206 ? HIS A 211 ? ILE A 206 HIS A 211 
AA4 3 THR A 216 ? LYS A 221 ? THR A 216 LYS A 221 
AA5 1 MET B 4   ? GLN B 6   ? MET B 4   GLN B 6   
AA5 2 ALA B 19  ? SER B 25  ? ALA B 19  SER B 25  
AA5 3 ASP B 75  ? ILE B 80  ? ASP B 75  ILE B 80  
AA5 4 PHE B 67  ? SER B 72  ? PHE B 67  SER B 72  
AA6 1 SER B 10  ? VAL B 13  ? SER B 10  VAL B 13  
AA6 2 THR B 107 ? ILE B 111 ? THR B 107 ILE B 111 
AA6 3 GLY B 89  ? GLN B 95  ? GLY B 89  GLN B 95  
AA6 4 LEU B 38  ? ARG B 43  ? LEU B 38  ARG B 43  
AA6 5 PRO B 49  ? TYR B 54  ? PRO B 49  TYR B 54  
AA6 6 GLU B 58  ? ARG B 59  ? GLU B 58  ARG B 59  
AA7 1 SER B 119 ? PHE B 123 ? SER B 119 PHE B 123 
AA7 2 THR B 134 ? PHE B 144 ? THR B 134 PHE B 144 
AA7 3 TYR B 178 ? SER B 187 ? TYR B 178 SER B 187 
AA7 4 SER B 164 ? VAL B 168 ? SER B 164 VAL B 168 
AA8 1 ALA B 158 ? GLN B 160 ? ALA B 158 GLN B 160 
AA8 2 LYS B 150 ? VAL B 155 ? LYS B 150 VAL B 155 
AA8 3 TYR B 197 ? THR B 202 ? TYR B 197 THR B 202 
AA8 4 VAL B 210 ? PHE B 214 ? VAL B 210 PHE B 214 
AA9 1 GLN C 3   ? GLY C 8   ? GLN C 3   GLY C 8   
AA9 2 LEU C 18  ? TYR C 25  ? LEU C 18  TYR C 25  
AA9 3 GLN C 77  ? LEU C 82  ? GLN C 77  LEU C 82  
AA9 4 ALA C 67  ? ASP C 72  ? ALA C 67  ASP C 72  
AB1 1 LEU C 11  ? LEU C 12  ? LEU C 11  LEU C 12  
AB1 2 TYR C 32  ? SER C 40  ? TYR C 32  SER C 40  
AB1 3 GLY C 44  ? ILE C 51  ? GLY C 44  ILE C 51  
AB1 4 THR C 57  ? TYR C 59  ? THR C 57  TYR C 59  
AB1 5 ALA C 91  ? MET C 102 ? ALA C 91  MET C 102 
AB1 6 VAL C 106 ? TRP C 114 ? VAL C 106 TRP C 114 
AB1 7 THR C 118 ? VAL C 122 ? THR C 118 VAL C 122 
AB2 1 LEU C 152 ? TYR C 156 ? LEU C 152 TYR C 156 
AB2 2 THR C 162 ? TRP C 165 ? THR C 162 TRP C 165 
AB2 3 GLY C 173 ? THR C 176 ? GLY C 173 THR C 176 
AB2 4 VAL C 180 ? LEU C 181 ? VAL C 180 LEU C 181 
AB2 5 TYR C 187 ? VAL C 192 ? TYR C 187 VAL C 192 
AB2 6 ASN C 208 ? ASN C 210 ? ASN C 208 ASN C 210 
AB3 1 MET D 4   ? SER D 7   ? MET D 4   SER D 7   
AB3 2 ALA D 19  ? SER D 25  ? ALA D 19  SER D 25  
AB3 3 ASP D 75  ? ILE D 80  ? ASP D 75  ILE D 80  
AB3 4 PHE D 67  ? SER D 72  ? PHE D 67  SER D 72  
AB4 1 SER D 10  ? VAL D 13  ? SER D 10  VAL D 13  
AB4 2 THR D 107 ? ILE D 111 ? THR D 107 ILE D 111 
AB4 3 GLY D 89  ? GLN D 95  ? GLY D 89  GLN D 95  
AB4 4 LEU D 38  ? ARG D 43  ? LEU D 38  ARG D 43  
AB4 5 PRO D 49  ? TYR D 54  ? PRO D 49  TYR D 54  
AB4 6 GLU D 58  ? ARG D 59  ? GLU D 58  ARG D 59  
# 
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 GLN A 3   ? N GLN A 3   O TYR A 25  ? O TYR A 25  
AA1 2 3 N LEU A 18  ? N LEU A 18  O LEU A 82  ? O LEU A 82  
AA1 3 4 O SER A 79  ? O SER A 79  N SER A 70  ? N SER A 70  
AA2 1 7 N LEU A 12  ? N LEU A 12  O THR A 121 ? O THR A 121 
AA2 2 3 N ARG A 38  ? N ARG A 38  O GLU A 46  ? O GLU A 46  
AA2 2 5 N GLN A 39  ? N GLN A 39  O THR A 92  ? O THR A 92  
AA2 3 4 N GLU A 50  ? N GLU A 50  O LYS A 58  ? O LYS A 58  
AA2 5 6 N ARG A 99  ? N ARG A 99  O HIS A 109 ? O HIS A 109 
AA2 5 7 N ALA A 91  ? N ALA A 91  O VAL A 120 ? O VAL A 120 
AA3 1 2 N LEU A 135 ? N LEU A 135 O GLY A 150 ? O GLY A 150 
AA3 2 5 N VAL A 153 ? N VAL A 153 O LEU A 189 ? O LEU A 189 
AA3 3 5 N HIS A 175 ? N HIS A 175 O VAL A 192 ? O VAL A 192 
AA3 4 5 N VAL A 180 ? N VAL A 180 O SER A 188 ? O SER A 188 
AA4 1 2 N SER A 164 ? N SER A 164 O ASN A 208 ? O ASN A 208 
AA4 2 3 N HIS A 211 ? N HIS A 211 O THR A 216 ? O THR A 216 
AA5 1 2 N THR B 5   ? N THR B 5   O ARG B 24  ? O ARG B 24  
AA5 2 3 N CYS B 23  ? N CYS B 23  O PHE B 76  ? O PHE B 76  
AA5 3 4 O LYS B 79  ? O LYS B 79  N SER B 68  ? N SER B 68  
AA6 1 2 N LEU B 11  ? N LEU B 11  O GLU B 110 ? O GLU B 110 
AA6 2 3 O LEU B 109 ? O LEU B 109 N GLY B 89  ? N GLY B 89  
AA6 3 4 O THR B 90  ? O THR B 90  N ARG B 43  ? N ARG B 43  
AA6 4 5 N TRP B 40  ? N TRP B 40  O LEU B 52  ? O LEU B 52  
AA6 5 6 N TYR B 54  ? N TYR B 54  O GLU B 58  ? O GLU B 58  
AA7 1 2 N PHE B 121 ? N PHE B 121 O LEU B 140 ? O LEU B 140 
AA7 2 3 N LEU B 141 ? N LEU B 141 O LEU B 180 ? O LEU B 180 
AA7 3 4 O SER B 181 ? O SER B 181 N SER B 167 ? N SER B 167 
AA8 1 2 O GLN B 160 ? O GLN B 160 N TRP B 153 ? N TRP B 153 
AA8 2 3 N GLN B 152 ? N GLN B 152 O GLU B 200 ? O GLU B 200 
AA8 3 4 N VAL B 201 ? N VAL B 201 O VAL B 210 ? O VAL B 210 
AA9 1 2 N GLN C 3   ? N GLN C 3   O TYR C 25  ? O TYR C 25  
AA9 2 3 N LEU C 18  ? N LEU C 18  O LEU C 82  ? O LEU C 82  
AA9 3 4 O GLN C 77  ? O GLN C 77  N ASP C 72  ? N ASP C 72  
AB1 1 7 N LEU C 12  ? N LEU C 12  O THR C 121 ? O THR C 121 
AB1 2 3 N TRP C 36  ? N TRP C 36  O ILE C 48  ? O ILE C 48  
AB1 2 5 N TYR C 33  ? N TYR C 33  O TRP C 98  ? O TRP C 98  
AB1 3 4 N GLU C 50  ? N GLU C 50  O LYS C 58  ? O LYS C 58  
AB1 5 6 N ARG C 99  ? N ARG C 99  O HIS C 109 ? O HIS C 109 
AB1 5 7 N ALA C 91  ? N ALA C 91  O VAL C 120 ? O VAL C 120 
AB2 1 5 N VAL C 153 ? N VAL C 153 O LEU C 189 ? O LEU C 189 
AB2 2 6 N THR C 162 ? N THR C 162 O ASN C 210 ? O ASN C 210 
AB2 3 5 N HIS C 175 ? N HIS C 175 O VAL C 192 ? O VAL C 192 
AB2 4 5 N VAL C 180 ? N VAL C 180 O SER C 188 ? O SER C 188 
AB3 1 2 N SER D 7   ? N SER D 7   O SER D 22  ? O SER D 22  
AB3 2 3 N ILE D 21  ? N ILE D 21  O LEU D 78  ? O LEU D 78  
AB3 3 4 O LYS D 79  ? O LYS D 79  N SER D 68  ? N SER D 68  
AB4 1 2 N LEU D 11  ? N LEU D 11  O GLU D 110 ? O GLU D 110 
AB4 2 3 O THR D 107 ? O THR D 107 N TYR D 91  ? N TYR D 91  
AB4 3 4 O TYR D 92  ? O TYR D 92  N TYR D 41  ? N TYR D 41  
AB4 4 5 N LEU D 42  ? N LEU D 42  O GLN D 50  ? O GLN D 50  
AB4 5 6 N TYR D 54  ? N TYR D 54  O GLU D 58  ? O GLU D 58  
# 
_atom_sites.entry_id                    8GPK 
_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]   0.010960 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002973 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016059 
_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]   0.010590 
_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 
C 
N 
O 
S 
# 
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 1    N N   . GLN A 1 1   ? 4.756   37.533  -31.872 1.00 74.47  ? 1   GLN A N   1 
ATOM 2    C CA  . GLN A 1 1   ? 3.406   37.611  -31.330 1.00 70.98  ? 1   GLN A CA  1 
ATOM 3    C C   . GLN A 1 1   ? 2.376   37.288  -32.414 1.00 68.44  ? 1   GLN A C   1 
ATOM 4    O O   . GLN A 1 1   ? 1.168   37.406  -32.202 1.00 65.71  ? 1   GLN A O   1 
ATOM 5    C CB  . GLN A 1 1   ? 3.151   38.998  -30.732 1.00 69.05  ? 1   GLN A CB  1 
ATOM 6    C CG  . GLN A 1 1   ? 2.052   39.037  -29.679 1.00 68.22  ? 1   GLN A CG  1 
ATOM 7    C CD  . GLN A 1 1   ? 1.744   40.446  -29.213 1.00 72.39  ? 1   GLN A CD  1 
ATOM 8    O OE1 . GLN A 1 1   ? 2.366   41.409  -29.658 1.00 74.42  ? 1   GLN A OE1 1 
ATOM 9    N NE2 . GLN A 1 1   ? 0.777   40.573  -28.312 1.00 71.68  ? 1   GLN A NE2 1 
ATOM 10   N N   . VAL A 1 2   ? 2.869   36.882  -33.580 1.00 64.63  ? 2   VAL A N   1 
ATOM 11   C CA  . VAL A 1 2   ? 2.008   36.378  -34.643 1.00 62.97  ? 2   VAL A CA  1 
ATOM 12   C C   . VAL A 1 2   ? 1.605   34.949  -34.308 1.00 66.85  ? 2   VAL A C   1 
ATOM 13   O O   . VAL A 1 2   ? 2.457   34.107  -34.003 1.00 72.54  ? 2   VAL A O   1 
ATOM 14   C CB  . VAL A 1 2   ? 2.722   36.448  -36.002 1.00 63.97  ? 2   VAL A CB  1 
ATOM 15   C CG1 . VAL A 1 2   ? 1.739   36.190  -37.129 1.00 61.82  ? 2   VAL A CG1 1 
ATOM 16   C CG2 . VAL A 1 2   ? 3.391   37.801  -36.177 1.00 64.80  ? 2   VAL A CG2 1 
ATOM 17   N N   . GLN A 1 3   ? 0.306   34.669  -34.361 1.00 64.64  ? 3   GLN A N   1 
ATOM 18   C CA  . GLN A 1 3   ? -0.218  33.354  -34.022 1.00 62.44  ? 3   GLN A CA  1 
ATOM 19   C C   . GLN A 1 3   ? -0.972  32.780  -35.212 1.00 60.98  ? 3   GLN A C   1 
ATOM 20   O O   . GLN A 1 3   ? -1.869  33.429  -35.759 1.00 60.89  ? 3   GLN A O   1 
ATOM 21   C CB  . GLN A 1 3   ? -1.131  33.424  -32.796 1.00 64.85  ? 3   GLN A CB  1 
ATOM 22   C CG  . GLN A 1 3   ? -1.613  32.064  -32.315 1.00 74.06  ? 3   GLN A CG  1 
ATOM 23   C CD  . GLN A 1 3   ? -2.709  32.169  -31.274 1.00 77.53  ? 3   GLN A CD  1 
ATOM 24   O OE1 . GLN A 1 3   ? -3.163  33.264  -30.943 1.00 81.39  ? 3   GLN A OE1 1 
ATOM 25   N NE2 . GLN A 1 3   ? -3.137  31.028  -30.749 1.00 73.35  ? 3   GLN A NE2 1 
ATOM 26   N N   . LEU A 1 4   ? -0.602  31.566  -35.607 1.00 64.14  ? 4   LEU A N   1 
ATOM 27   C CA  . LEU A 1 4   ? -1.296  30.812  -36.643 1.00 60.84  ? 4   LEU A CA  1 
ATOM 28   C C   . LEU A 1 4   ? -1.985  29.626  -35.983 1.00 61.06  ? 4   LEU A C   1 
ATOM 29   O O   . LEU A 1 4   ? -1.319  28.771  -35.389 1.00 69.32  ? 4   LEU A O   1 
ATOM 30   C CB  . LEU A 1 4   ? -0.322  30.343  -37.725 1.00 56.21  ? 4   LEU A CB  1 
ATOM 31   C CG  . LEU A 1 4   ? -0.152  31.217  -38.969 1.00 57.87  ? 4   LEU A CG  1 
ATOM 32   C CD1 . LEU A 1 4   ? 0.357   32.607  -38.612 1.00 58.25  ? 4   LEU A CD1 1 
ATOM 33   C CD2 . LEU A 1 4   ? 0.791   30.541  -39.952 1.00 56.15  ? 4   LEU A CD2 1 
ATOM 34   N N   . GLN A 1 5   ? -3.311  29.579  -36.076 1.00 55.30  ? 5   GLN A N   1 
ATOM 35   C CA  . GLN A 1 5   ? -4.104  28.531  -35.446 1.00 62.49  ? 5   GLN A CA  1 
ATOM 36   C C   . GLN A 1 5   ? -4.755  27.661  -36.510 1.00 65.00  ? 5   GLN A C   1 
ATOM 37   O O   . GLN A 1 5   ? -5.375  28.177  -37.445 1.00 62.39  ? 5   GLN A O   1 
ATOM 38   C CB  . GLN A 1 5   ? -5.169  29.124  -34.524 1.00 64.65  ? 5   GLN A CB  1 
ATOM 39   C CG  . GLN A 1 5   ? -4.771  29.088  -33.063 1.00 77.23  ? 5   GLN A CG  1 
ATOM 40   C CD  . GLN A 1 5   ? -5.952  29.249  -32.133 1.00 83.99  ? 5   GLN A CD  1 
ATOM 41   O OE1 . GLN A 1 5   ? -7.044  29.628  -32.555 1.00 81.83  ? 5   GLN A OE1 1 
ATOM 42   N NE2 . GLN A 1 5   ? -5.744  28.942  -30.860 1.00 79.72  ? 5   GLN A NE2 1 
ATOM 43   N N   . GLN A 1 6   ? -4.632  26.345  -36.349 1.00 68.98  ? 6   GLN A N   1 
ATOM 44   C CA  . GLN A 1 6   ? -5.100  25.368  -37.322 1.00 62.05  ? 6   GLN A CA  1 
ATOM 45   C C   . GLN A 1 6   ? -6.221  24.527  -36.724 1.00 61.58  ? 6   GLN A C   1 
ATOM 46   O O   . GLN A 1 6   ? -6.149  24.113  -35.563 1.00 66.34  ? 6   GLN A O   1 
ATOM 47   C CB  . GLN A 1 6   ? -3.948  24.457  -37.772 1.00 59.40  ? 6   GLN A CB  1 
ATOM 48   C CG  . GLN A 1 6   ? -4.260  23.534  -38.944 1.00 59.13  ? 6   GLN A CG  1 
ATOM 49   C CD  . GLN A 1 6   ? -3.037  22.753  -39.394 1.00 58.69  ? 6   GLN A CD  1 
ATOM 50   O OE1 . GLN A 1 6   ? -1.905  23.166  -39.145 1.00 62.19  ? 6   GLN A OE1 1 
ATOM 51   N NE2 . GLN A 1 6   ? -3.258  21.627  -40.067 1.00 60.43  ? 6   GLN A NE2 1 
ATOM 52   N N   . TRP A 1 7   ? -7.257  24.279  -37.522 1.00 60.70  ? 7   TRP A N   1 
ATOM 53   C CA  . TRP A 1 7   ? -8.327  23.374  -37.129 1.00 57.22  ? 7   TRP A CA  1 
ATOM 54   C C   . TRP A 1 7   ? -8.846  22.663  -38.368 1.00 58.86  ? 7   TRP A C   1 
ATOM 55   O O   . TRP A 1 7   ? -8.458  22.971  -39.497 1.00 63.77  ? 7   TRP A O   1 
ATOM 56   C CB  . TRP A 1 7   ? -9.465  24.106  -36.407 1.00 60.18  ? 7   TRP A CB  1 
ATOM 57   C CG  . TRP A 1 7   ? -10.268 25.026  -37.278 1.00 64.27  ? 7   TRP A CG  1 
ATOM 58   C CD1 . TRP A 1 7   ? -11.395 24.714  -37.985 1.00 64.63  ? 7   TRP A CD1 1 
ATOM 59   C CD2 . TRP A 1 7   ? -10.024 26.416  -37.507 1.00 64.11  ? 7   TRP A CD2 1 
ATOM 60   N NE1 . TRP A 1 7   ? -11.856 25.823  -38.654 1.00 64.47  ? 7   TRP A NE1 1 
ATOM 61   C CE2 . TRP A 1 7   ? -11.032 26.882  -38.375 1.00 63.98  ? 7   TRP A CE2 1 
ATOM 62   C CE3 . TRP A 1 7   ? -9.046  27.312  -37.069 1.00 66.02  ? 7   TRP A CE3 1 
ATOM 63   C CZ2 . TRP A 1 7   ? -11.090 28.203  -38.811 1.00 65.51  ? 7   TRP A CZ2 1 
ATOM 64   C CZ3 . TRP A 1 7   ? -9.105  28.617  -37.501 1.00 65.86  ? 7   TRP A CZ3 1 
ATOM 65   C CH2 . TRP A 1 7   ? -10.118 29.054  -38.364 1.00 63.54  ? 7   TRP A CH2 1 
ATOM 66   N N   . GLY A 1 8   ? -9.733  21.700  -38.144 1.00 59.08  ? 8   GLY A N   1 
ATOM 67   C CA  . GLY A 1 8   ? -10.298 20.957  -39.249 1.00 58.04  ? 8   GLY A CA  1 
ATOM 68   C C   . GLY A 1 8   ? -10.508 19.490  -38.948 1.00 55.30  ? 8   GLY A C   1 
ATOM 69   O O   . GLY A 1 8   ? -10.763 19.108  -37.802 1.00 55.55  ? 8   GLY A O   1 
ATOM 70   N N   . THR A 1 9   ? -10.396 18.657  -39.976 1.00 54.62  ? 9   THR A N   1 
ATOM 71   C CA  . THR A 1 9   ? -10.695 17.238  -39.848 1.00 53.73  ? 9   THR A CA  1 
ATOM 72   C C   . THR A 1 9   ? -9.497  16.502  -39.265 1.00 55.82  ? 9   THR A C   1 
ATOM 73   O O   . THR A 1 9   ? -8.412  16.509  -39.855 1.00 56.10  ? 9   THR A O   1 
ATOM 74   C CB  . THR A 1 9   ? -11.070 16.657  -41.207 1.00 55.59  ? 9   THR A CB  1 
ATOM 75   O OG1 . THR A 1 9   ? -10.134 17.111  -42.194 1.00 54.64  ? 9   THR A OG1 1 
ATOM 76   C CG2 . THR A 1 9   ? -12.469 17.092  -41.602 1.00 59.42  ? 9   THR A CG2 1 
ATOM 77   N N   . GLY A 1 10  ? -9.694  15.865  -38.114 1.00 59.54  ? 10  GLY A N   1 
ATOM 78   C CA  . GLY A 1 10  ? -8.633  15.106  -37.483 1.00 58.26  ? 10  GLY A CA  1 
ATOM 79   C C   . GLY A 1 10  ? -8.686  13.628  -37.812 1.00 59.51  ? 10  GLY A C   1 
ATOM 80   O O   . GLY A 1 10  ? -7.676  12.926  -37.709 1.00 59.34  ? 10  GLY A O   1 
ATOM 81   N N   . LEU A 1 11  ? -9.861  13.145  -38.211 1.00 62.81  ? 11  LEU A N   1 
ATOM 82   C CA  . LEU A 1 11  ? -10.055 11.739  -38.553 1.00 59.63  ? 11  LEU A CA  1 
ATOM 83   C C   . LEU A 1 11  ? -10.878 11.654  -39.828 1.00 59.52  ? 11  LEU A C   1 
ATOM 84   O O   . LEU A 1 11  ? -11.974 12.218  -39.899 1.00 58.91  ? 11  LEU A O   1 
ATOM 85   C CB  . LEU A 1 11  ? -10.748 10.981  -37.415 1.00 61.19  ? 11  LEU A CB  1 
ATOM 86   C CG  . LEU A 1 11  ? -10.863 9.460   -37.561 1.00 60.39  ? 11  LEU A CG  1 
ATOM 87   C CD1 . LEU A 1 11  ? -9.491  8.803   -37.636 1.00 62.47  ? 11  LEU A CD1 1 
ATOM 88   C CD2 . LEU A 1 11  ? -11.684 8.865   -36.426 1.00 61.49  ? 11  LEU A CD2 1 
ATOM 89   N N   . LEU A 1 12  ? -10.352 10.954  -40.831 1.00 64.50  ? 12  LEU A N   1 
ATOM 90   C CA  . LEU A 1 12  ? -11.052 10.766  -42.091 1.00 63.33  ? 12  LEU A CA  1 
ATOM 91   C C   . LEU A 1 12  ? -11.152 9.283   -42.410 1.00 62.15  ? 12  LEU A C   1 
ATOM 92   O O   . LEU A 1 12  ? -10.268 8.491   -42.070 1.00 62.41  ? 12  LEU A O   1 
ATOM 93   C CB  . LEU A 1 12  ? -10.357 11.474  -43.269 1.00 59.64  ? 12  LEU A CB  1 
ATOM 94   C CG  . LEU A 1 12  ? -10.419 12.999  -43.400 1.00 54.20  ? 12  LEU A CG  1 
ATOM 95   C CD1 . LEU A 1 12  ? -11.864 13.493  -43.450 1.00 58.27  ? 12  LEU A CD1 1 
ATOM 96   C CD2 . LEU A 1 12  ? -9.610  13.703  -42.322 1.00 61.44  ? 12  LEU A CD2 1 
ATOM 97   N N   . LYS A 1 13  ? -12.218 8.925   -43.048 1.00 63.91  ? 13  LYS A N   1 
ATOM 98   C CA  . LYS A 1 13  ? -12.313 7.607   -43.648 1.00 62.04  ? 13  LYS A CA  1 
ATOM 99   C C   . LYS A 1 13  ? -11.811 7.666   -45.088 1.00 60.07  ? 13  LYS A C   1 
ATOM 100  O O   . LYS A 1 13  ? -11.915 8.708   -45.742 1.00 65.96  ? 13  LYS A O   1 
ATOM 101  C CB  . LYS A 1 13  ? -13.755 7.108   -43.610 1.00 59.02  ? 13  LYS A CB  1 
ATOM 102  C CG  . LYS A 1 13  ? -14.254 6.805   -42.201 1.00 62.55  ? 13  LYS A CG  1 
ATOM 103  C CD  . LYS A 1 13  ? -15.571 6.039   -42.204 1.00 63.27  ? 13  LYS A CD  1 
ATOM 104  C CE  . LYS A 1 13  ? -16.750 6.960   -42.479 1.00 66.10  ? 13  LYS A CE  1 
ATOM 105  N NZ  . LYS A 1 13  ? -18.058 6.262   -42.324 1.00 71.74  ? 13  LYS A NZ  1 
ATOM 106  N N   . PRO A 1 14  ? -11.237 6.573   -45.593 1.00 57.47  ? 14  PRO A N   1 
ATOM 107  C CA  . PRO A 1 14  ? -10.642 6.606   -46.936 1.00 58.32  ? 14  PRO A CA  1 
ATOM 108  C C   . PRO A 1 14  ? -11.635 7.071   -47.992 1.00 62.54  ? 14  PRO A C   1 
ATOM 109  O O   . PRO A 1 14  ? -12.818 6.726   -47.954 1.00 60.50  ? 14  PRO A O   1 
ATOM 110  C CB  . PRO A 1 14  ? -10.218 5.152   -47.166 1.00 57.27  ? 14  PRO A CB  1 
ATOM 111  C CG  . PRO A 1 14  ? -9.975  4.629   -45.790 1.00 57.99  ? 14  PRO A CG  1 
ATOM 112  C CD  . PRO A 1 14  ? -11.029 5.272   -44.934 1.00 59.24  ? 14  PRO A CD  1 
ATOM 113  N N   . SER A 1 15  ? -11.133 7.875   -48.930 1.00 64.31  ? 15  SER A N   1 
ATOM 114  C CA  . SER A 1 15  ? -11.832 8.496   -50.058 1.00 64.85  ? 15  SER A CA  1 
ATOM 115  C C   . SER A 1 15  ? -12.667 9.702   -49.636 1.00 67.83  ? 15  SER A C   1 
ATOM 116  O O   . SER A 1 15  ? -13.277 10.338  -50.504 1.00 66.41  ? 15  SER A O   1 
ATOM 117  C CB  . SER A 1 15  ? -12.732 7.517   -50.831 1.00 68.10  ? 15  SER A CB  1 
ATOM 118  O OG  . SER A 1 15  ? -12.022 6.343   -51.182 1.00 75.22  ? 15  SER A OG  1 
ATOM 119  N N   . GLU A 1 16  ? -12.719 10.044  -48.351 1.00 72.47  ? 16  GLU A N   1 
ATOM 120  C CA  . GLU A 1 16  ? -13.379 11.271  -47.932 1.00 73.41  ? 16  GLU A CA  1 
ATOM 121  C C   . GLU A 1 16  ? -12.434 12.454  -48.151 1.00 71.72  ? 16  GLU A C   1 
ATOM 122  O O   . GLU A 1 16  ? -11.325 12.305  -48.672 1.00 71.52  ? 16  GLU A O   1 
ATOM 123  C CB  . GLU A 1 16  ? -13.850 11.145  -46.485 1.00 70.28  ? 16  GLU A CB  1 
ATOM 124  C CG  . GLU A 1 16  ? -14.949 10.095  -46.315 1.00 75.96  ? 16  GLU A CG  1 
ATOM 125  C CD  . GLU A 1 16  ? -15.487 10.006  -44.902 1.00 82.19  ? 16  GLU A CD  1 
ATOM 126  O OE1 . GLU A 1 16  ? -14.852 10.565  -43.984 1.00 76.30  ? 16  GLU A OE1 1 
ATOM 127  O OE2 . GLU A 1 16  ? -16.549 9.377   -44.713 1.00 82.92  ? 16  GLU A OE2 1 
ATOM 128  N N   . THR A 1 17  ? -12.869 13.653  -47.769 1.00 65.36  ? 17  THR A N   1 
ATOM 129  C CA  . THR A 1 17  ? -12.134 14.870  -48.091 1.00 63.52  ? 17  THR A CA  1 
ATOM 130  C C   . THR A 1 17  ? -11.620 15.557  -46.830 1.00 59.93  ? 17  THR A C   1 
ATOM 131  O O   . THR A 1 17  ? -12.315 15.619  -45.810 1.00 58.96  ? 17  THR A O   1 
ATOM 132  C CB  . THR A 1 17  ? -13.001 15.841  -48.907 1.00 62.06  ? 17  THR A CB  1 
ATOM 133  O OG1 . THR A 1 17  ? -12.306 17.084  -49.069 1.00 67.24  ? 17  THR A OG1 1 
ATOM 134  C CG2 . THR A 1 17  ? -14.338 16.088  -48.224 1.00 62.92  ? 17  THR A CG2 1 
ATOM 135  N N   . LEU A 1 18  ? -10.395 16.078  -46.918 1.00 57.49  ? 18  LEU A N   1 
ATOM 136  C CA  . LEU A 1 18  ? -9.716  16.720  -45.799 1.00 56.91  ? 18  LEU A CA  1 
ATOM 137  C C   . LEU A 1 18  ? -9.981  18.220  -45.815 1.00 61.80  ? 18  LEU A C   1 
ATOM 138  O O   . LEU A 1 18  ? -9.911  18.860  -46.868 1.00 59.41  ? 18  LEU A O   1 
ATOM 139  C CB  . LEU A 1 18  ? -8.211  16.443  -45.869 1.00 54.30  ? 18  LEU A CB  1 
ATOM 140  C CG  . LEU A 1 18  ? -7.193  17.181  -44.992 1.00 53.92  ? 18  LEU A CG  1 
ATOM 141  C CD1 . LEU A 1 18  ? -6.022  16.265  -44.697 1.00 53.61  ? 18  LEU A CD1 1 
ATOM 142  C CD2 . LEU A 1 18  ? -6.682  18.444  -45.675 1.00 57.61  ? 18  LEU A CD2 1 
ATOM 143  N N   . SER A 1 19  ? -10.274 18.779  -44.646 1.00 58.81  ? 19  SER A N   1 
ATOM 144  C CA  . SER A 1 19  ? -10.459 20.216  -44.488 1.00 56.85  ? 19  SER A CA  1 
ATOM 145  C C   . SER A 1 19  ? -9.556  20.696  -43.364 1.00 57.92  ? 19  SER A C   1 
ATOM 146  O O   . SER A 1 19  ? -9.615  20.170  -42.249 1.00 58.29  ? 19  SER A O   1 
ATOM 147  C CB  . SER A 1 19  ? -11.919 20.559  -44.189 1.00 59.83  ? 19  SER A CB  1 
ATOM 148  O OG  . SER A 1 19  ? -12.037 21.893  -43.724 1.00 72.50  ? 19  SER A OG  1 
ATOM 149  N N   . LEU A 1 20  ? -8.715  21.680  -43.660 1.00 59.85  ? 20  LEU A N   1 
ATOM 150  C CA  . LEU A 1 20  ? -7.815  22.261  -42.674 1.00 60.66  ? 20  LEU A CA  1 
ATOM 151  C C   . LEU A 1 20  ? -7.729  23.757  -42.931 1.00 64.07  ? 20  LEU A C   1 
ATOM 152  O O   . LEU A 1 20  ? -7.552  24.180  -44.075 1.00 66.04  ? 20  LEU A O   1 
ATOM 153  C CB  . LEU A 1 20  ? -6.430  21.607  -42.742 1.00 53.82  ? 20  LEU A CB  1 
ATOM 154  C CG  . LEU A 1 20  ? -6.343  20.187  -42.182 1.00 53.40  ? 20  LEU A CG  1 
ATOM 155  C CD1 . LEU A 1 20  ? -4.976  19.593  -42.432 1.00 53.15  ? 20  LEU A CD1 1 
ATOM 156  C CD2 . LEU A 1 20  ? -6.657  20.189  -40.700 1.00 53.47  ? 20  LEU A CD2 1 
ATOM 157  N N   . THR A 1 21  ? -7.859  24.554  -41.872 1.00 62.69  ? 21  THR A N   1 
ATOM 158  C CA  . THR A 1 21  ? -7.961  26.001  -42.003 1.00 65.33  ? 21  THR A CA  1 
ATOM 159  C C   . THR A 1 21  ? -7.075  26.673  -40.965 1.00 63.24  ? 21  THR A C   1 
ATOM 160  O O   . THR A 1 21  ? -7.006  26.229  -39.816 1.00 61.76  ? 21  THR A O   1 
ATOM 161  C CB  . THR A 1 21  ? -9.414  26.465  -41.838 1.00 66.49  ? 21  THR A CB  1 
ATOM 162  O OG1 . THR A 1 21  ? -10.234 25.825  -42.824 1.00 66.32  ? 21  THR A OG1 1 
ATOM 163  C CG2 . THR A 1 21  ? -9.525  27.973  -41.996 1.00 63.06  ? 21  THR A CG2 1 
ATOM 164  N N   . CYS A 1 22  ? -6.404  27.747  -41.370 1.00 65.54  ? 22  CYS A N   1 
ATOM 165  C CA  . CYS A 1 22  ? -5.437  28.426  -40.518 1.00 64.44  ? 22  CYS A CA  1 
ATOM 166  C C   . CYS A 1 22  ? -5.867  29.872  -40.322 1.00 59.91  ? 22  CYS A C   1 
ATOM 167  O O   . CYS A 1 22  ? -5.963  30.630  -41.293 1.00 60.11  ? 22  CYS A O   1 
ATOM 168  C CB  . CYS A 1 22  ? -4.038  28.361  -41.129 1.00 61.69  ? 22  CYS A CB  1 
ATOM 169  S SG  . CYS A 1 22  ? -2.712  28.249  -39.919 1.00 73.62  ? 22  CYS A SG  1 
ATOM 170  N N   . ALA A 1 23  ? -6.129  30.250  -39.074 1.00 56.73  ? 23  ALA A N   1 
ATOM 171  C CA  . ALA A 1 23  ? -6.517  31.614  -38.736 1.00 56.62  ? 23  ALA A CA  1 
ATOM 172  C C   . ALA A 1 23  ? -5.297  32.365  -38.222 1.00 60.19  ? 23  ALA A C   1 
ATOM 173  O O   . ALA A 1 23  ? -4.651  31.927  -37.264 1.00 71.18  ? 23  ALA A O   1 
ATOM 174  C CB  . ALA A 1 23  ? -7.631  31.634  -37.692 1.00 54.98  ? 23  ALA A CB  1 
ATOM 175  N N   . VAL A 1 24  ? -4.991  33.494  -38.852 1.00 56.21  ? 24  VAL A N   1 
ATOM 176  C CA  . VAL A 1 24  ? -3.818  34.290  -38.518 1.00 55.28  ? 24  VAL A CA  1 
ATOM 177  C C   . VAL A 1 24  ? -4.241  35.424  -37.596 1.00 62.71  ? 24  VAL A C   1 
ATOM 178  O O   . VAL A 1 24  ? -5.102  36.239  -37.949 1.00 65.28  ? 24  VAL A O   1 
ATOM 179  C CB  . VAL A 1 24  ? -3.134  34.830  -39.781 1.00 55.49  ? 24  VAL A CB  1 
ATOM 180  C CG1 . VAL A 1 24  ? -1.885  35.603  -39.407 1.00 59.41  ? 24  VAL A CG1 1 
ATOM 181  C CG2 . VAL A 1 24  ? -2.790  33.681  -40.701 1.00 57.17  ? 24  VAL A CG2 1 
ATOM 182  N N   . TYR A 1 25  ? -3.630  35.474  -36.417 1.00 66.17  ? 25  TYR A N   1 
ATOM 183  C CA  . TYR A 1 25  ? -3.842  36.538  -35.448 1.00 62.37  ? 25  TYR A CA  1 
ATOM 184  C C   . TYR A 1 25  ? -2.565  37.359  -35.343 1.00 58.18  ? 25  TYR A C   1 
ATOM 185  O O   . TYR A 1 25  ? -1.488  36.807  -35.094 1.00 60.76  ? 25  TYR A O   1 
ATOM 186  C CB  . TYR A 1 25  ? -4.212  35.968  -34.075 1.00 64.14  ? 25  TYR A CB  1 
ATOM 187  C CG  . TYR A 1 25  ? -5.478  35.140  -34.050 1.00 63.07  ? 25  TYR A CG  1 
ATOM 188  C CD1 . TYR A 1 25  ? -5.458  33.799  -34.411 1.00 61.03  ? 25  TYR A CD1 1 
ATOM 189  C CD2 . TYR A 1 25  ? -6.689  35.693  -33.654 1.00 63.40  ? 25  TYR A CD2 1 
ATOM 190  C CE1 . TYR A 1 25  ? -6.605  33.034  -34.385 1.00 60.96  ? 25  TYR A CE1 1 
ATOM 191  C CE2 . TYR A 1 25  ? -7.844  34.934  -33.626 1.00 59.02  ? 25  TYR A CE2 1 
ATOM 192  C CZ  . TYR A 1 25  ? -7.795  33.606  -33.992 1.00 61.40  ? 25  TYR A CZ  1 
ATOM 193  O OH  . TYR A 1 25  ? -8.939  32.844  -33.967 1.00 65.50  ? 25  TYR A OH  1 
ATOM 194  N N   . GLY A 1 26  ? -2.682  38.670  -35.542 1.00 57.66  ? 26  GLY A N   1 
ATOM 195  C CA  . GLY A 1 26  ? -1.540  39.549  -35.379 1.00 62.27  ? 26  GLY A CA  1 
ATOM 196  C C   . GLY A 1 26  ? -1.175  40.361  -36.605 1.00 57.43  ? 26  GLY A C   1 
ATOM 197  O O   . GLY A 1 26  ? -0.872  41.552  -36.496 1.00 65.32  ? 26  GLY A O   1 
ATOM 198  N N   . VAL A 1 27  ? -1.186  39.733  -37.779 1.00 56.75  ? 27  VAL A N   1 
ATOM 199  C CA  . VAL A 1 27  ? -0.840  40.404  -39.024 1.00 57.09  ? 27  VAL A CA  1 
ATOM 200  C C   . VAL A 1 27  ? -1.910  40.113  -40.063 1.00 61.10  ? 27  VAL A C   1 
ATOM 201  O O   . VAL A 1 27  ? -2.544  39.053  -40.054 1.00 62.46  ? 27  VAL A O   1 
ATOM 202  C CB  . VAL A 1 27  ? 0.543   39.972  -39.563 1.00 57.11  ? 27  VAL A CB  1 
ATOM 203  C CG1 . VAL A 1 27  ? 1.662   40.537  -38.702 1.00 59.59  ? 27  VAL A CG1 1 
ATOM 204  C CG2 . VAL A 1 27  ? 0.626   38.458  -39.669 1.00 60.92  ? 27  VAL A CG2 1 
ATOM 205  N N   . SER A 1 28  ? -2.102  41.065  -40.970 1.00 60.02  ? 28  SER A N   1 
ATOM 206  C CA  . SER A 1 28  ? -2.934  40.825  -42.137 1.00 58.25  ? 28  SER A CA  1 
ATOM 207  C C   . SER A 1 28  ? -2.256  39.829  -43.070 1.00 58.59  ? 28  SER A C   1 
ATOM 208  O O   . SER A 1 28  ? -1.027  39.722  -43.115 1.00 59.60  ? 28  SER A O   1 
ATOM 209  C CB  . SER A 1 28  ? -3.205  42.134  -42.877 1.00 58.81  ? 28  SER A CB  1 
ATOM 210  O OG  . SER A 1 28  ? -4.152  41.948  -43.913 1.00 62.43  ? 28  SER A OG  1 
ATOM 211  N N   . LEU A 1 29  ? -3.072  39.088  -43.820 1.00 59.13  ? 29  LEU A N   1 
ATOM 212  C CA  . LEU A 1 29  ? -2.520  38.146  -44.786 1.00 59.75  ? 29  LEU A CA  1 
ATOM 213  C C   . LEU A 1 29  ? -1.814  38.855  -45.931 1.00 60.37  ? 29  LEU A C   1 
ATOM 214  O O   . LEU A 1 29  ? -0.990  38.238  -46.614 1.00 59.09  ? 29  LEU A O   1 
ATOM 215  C CB  . LEU A 1 29  ? -3.620  37.244  -45.341 1.00 62.70  ? 29  LEU A CB  1 
ATOM 216  C CG  . LEU A 1 29  ? -4.566  36.624  -44.315 1.00 63.60  ? 29  LEU A CG  1 
ATOM 217  C CD1 . LEU A 1 29  ? -5.626  35.791  -45.009 1.00 66.58  ? 29  LEU A CD1 1 
ATOM 218  C CD2 . LEU A 1 29  ? -3.781  35.787  -43.336 1.00 56.47  ? 29  LEU A CD2 1 
ATOM 219  N N   . ARG A 1 30  ? -2.118  40.131  -46.146 1.00 60.73  ? 30  ARG A N   1 
ATOM 220  C CA  . ARG A 1 30  ? -1.516  40.880  -47.237 1.00 60.59  ? 30  ARG A CA  1 
ATOM 221  C C   . ARG A 1 30  ? -0.026  41.080  -46.998 1.00 58.46  ? 30  ARG A C   1 
ATOM 222  O O   . ARG A 1 30  ? 0.404   41.437  -45.897 1.00 58.30  ? 30  ARG A O   1 
ATOM 223  C CB  . ARG A 1 30  ? -2.212  42.230  -47.389 1.00 65.14  ? 30  ARG A CB  1 
ATOM 224  C CG  . ARG A 1 30  ? -3.711  42.129  -47.621 1.00 67.90  ? 30  ARG A CG  1 
ATOM 225  C CD  . ARG A 1 30  ? -4.465  43.220  -46.875 1.00 75.23  ? 30  ARG A CD  1 
ATOM 226  N NE  . ARG A 1 30  ? -5.909  43.025  -46.935 1.00 78.44  ? 30  ARG A NE  1 
ATOM 227  C CZ  . ARG A 1 30  ? -6.766  43.479  -46.030 1.00 75.99  ? 30  ARG A CZ  1 
ATOM 228  N NH1 . ARG A 1 30  ? -6.355  44.158  -44.971 1.00 72.00  ? 30  ARG A NH1 1 
ATOM 229  N NH2 . ARG A 1 30  ? -8.066  43.248  -46.193 1.00 68.82  ? 30  ARG A NH2 1 
ATOM 230  N N   . GLY A 1 31  ? 0.764   40.848  -48.044 1.00 58.79  ? 31  GLY A N   1 
ATOM 231  C CA  . GLY A 1 31  ? 2.200   40.999  -47.979 1.00 58.11  ? 31  GLY A CA  1 
ATOM 232  C C   . GLY A 1 31  ? 2.981   39.711  -47.848 1.00 59.12  ? 31  GLY A C   1 
ATOM 233  O O   . GLY A 1 31  ? 4.217   39.760  -47.851 1.00 59.31  ? 31  GLY A O   1 
ATOM 234  N N   . TYR A 1 32  ? 2.311   38.565  -47.741 1.00 59.05  ? 32  TYR A N   1 
ATOM 235  C CA  . TYR A 1 32  ? 2.974   37.290  -47.508 1.00 56.34  ? 32  TYR A CA  1 
ATOM 236  C C   . TYR A 1 32  ? 2.429   36.231  -48.454 1.00 58.41  ? 32  TYR A C   1 
ATOM 237  O O   . TYR A 1 32  ? 1.392   36.409  -49.099 1.00 59.29  ? 32  TYR A O   1 
ATOM 238  C CB  . TYR A 1 32  ? 2.791   36.819  -46.059 1.00 58.77  ? 32  TYR A CB  1 
ATOM 239  C CG  . TYR A 1 32  ? 3.156   37.846  -45.015 1.00 57.96  ? 32  TYR A CG  1 
ATOM 240  C CD1 . TYR A 1 32  ? 4.484   38.123  -44.723 1.00 56.48  ? 32  TYR A CD1 1 
ATOM 241  C CD2 . TYR A 1 32  ? 2.173   38.529  -44.314 1.00 57.79  ? 32  TYR A CD2 1 
ATOM 242  C CE1 . TYR A 1 32  ? 4.823   39.057  -43.765 1.00 57.43  ? 32  TYR A CE1 1 
ATOM 243  C CE2 . TYR A 1 32  ? 2.501   39.467  -43.354 1.00 58.68  ? 32  TYR A CE2 1 
ATOM 244  C CZ  . TYR A 1 32  ? 3.828   39.727  -43.082 1.00 60.78  ? 32  TYR A CZ  1 
ATOM 245  O OH  . TYR A 1 32  ? 4.160   40.660  -42.125 1.00 69.17  ? 32  TYR A OH  1 
ATOM 246  N N   . TYR A 1 33  ? 3.151   35.117  -48.530 1.00 55.72  ? 33  TYR A N   1 
ATOM 247  C CA  . TYR A 1 33  ? 2.672   33.902  -49.169 1.00 55.57  ? 33  TYR A CA  1 
ATOM 248  C C   . TYR A 1 33  ? 2.330   32.931  -48.045 1.00 55.17  ? 33  TYR A C   1 
ATOM 249  O O   . TYR A 1 33  ? 2.944   32.972  -46.974 1.00 59.49  ? 33  TYR A O   1 
ATOM 250  C CB  . TYR A 1 33  ? 3.740   33.285  -50.080 1.00 55.31  ? 33  TYR A CB  1 
ATOM 251  C CG  . TYR A 1 33  ? 3.918   33.950  -51.433 1.00 55.77  ? 33  TYR A CG  1 
ATOM 252  C CD1 . TYR A 1 33  ? 3.231   35.113  -51.764 1.00 56.41  ? 33  TYR A CD1 1 
ATOM 253  C CD2 . TYR A 1 33  ? 4.775   33.406  -52.384 1.00 55.59  ? 33  TYR A CD2 1 
ATOM 254  C CE1 . TYR A 1 33  ? 3.411   35.722  -52.999 1.00 56.88  ? 33  TYR A CE1 1 
ATOM 255  C CE2 . TYR A 1 33  ? 4.957   34.006  -53.620 1.00 56.04  ? 33  TYR A CE2 1 
ATOM 256  C CZ  . TYR A 1 33  ? 4.273   35.162  -53.922 1.00 56.69  ? 33  TYR A CZ  1 
ATOM 257  O OH  . TYR A 1 33  ? 4.456   35.750  -55.155 1.00 61.44  ? 33  TYR A OH  1 
ATOM 258  N N   . TRP A 1 34  ? 1.352   32.055  -48.269 1.00 55.14  ? 34  TRP A N   1 
ATOM 259  C CA  . TRP A 1 34  ? 0.873   31.176  -47.206 1.00 54.80  ? 34  TRP A CA  1 
ATOM 260  C C   . TRP A 1 34  ? 0.880   29.731  -47.682 1.00 55.72  ? 34  TRP A C   1 
ATOM 261  O O   . TRP A 1 34  ? 0.214   29.397  -48.666 1.00 56.37  ? 34  TRP A O   1 
ATOM 262  C CB  . TRP A 1 34  ? -0.519  31.597  -46.738 1.00 55.26  ? 34  TRP A CB  1 
ATOM 263  C CG  . TRP A 1 34  ? -0.532  32.999  -46.209 1.00 56.90  ? 34  TRP A CG  1 
ATOM 264  C CD1 . TRP A 1 34  ? -0.701  34.145  -46.928 1.00 57.10  ? 34  TRP A CD1 1 
ATOM 265  C CD2 . TRP A 1 34  ? -0.293  33.407  -44.857 1.00 58.28  ? 34  TRP A CD2 1 
ATOM 266  N NE1 . TRP A 1 34  ? -0.621  35.240  -46.103 1.00 56.50  ? 34  TRP A NE1 1 
ATOM 267  C CE2 . TRP A 1 34  ? -0.367  34.814  -44.826 1.00 56.20  ? 34  TRP A CE2 1 
ATOM 268  C CE3 . TRP A 1 34  ? -0.039  32.719  -43.668 1.00 58.48  ? 34  TRP A CE3 1 
ATOM 269  C CZ2 . TRP A 1 34  ? -0.196  35.543  -43.653 1.00 59.21  ? 34  TRP A CZ2 1 
ATOM 270  C CZ3 . TRP A 1 34  ? 0.126   33.444  -42.505 1.00 58.04  ? 34  TRP A CZ3 1 
ATOM 271  C CH2 . TRP A 1 34  ? 0.050   34.841  -42.505 1.00 56.98  ? 34  TRP A CH2 1 
ATOM 272  N N   . THR A 1 35  ? 1.608   28.878  -46.963 1.00 54.66  ? 35  THR A N   1 
ATOM 273  C CA  . THR A 1 35  ? 1.914   27.520  -47.388 1.00 53.72  ? 35  THR A CA  1 
ATOM 274  C C   . THR A 1 35  ? 1.426   26.489  -46.379 1.00 53.44  ? 35  THR A C   1 
ATOM 275  O O   . THR A 1 35  ? 1.426   26.726  -45.167 1.00 53.28  ? 35  THR A O   1 
ATOM 276  C CB  . THR A 1 35  ? 3.425   27.358  -47.609 1.00 53.38  ? 35  THR A CB  1 
ATOM 277  O OG1 . THR A 1 35  ? 3.854   28.264  -48.628 1.00 62.32  ? 35  THR A OG1 1 
ATOM 278  C CG2 . THR A 1 35  ? 3.789   25.943  -47.996 1.00 53.09  ? 35  THR A CG2 1 
ATOM 279  N N   . TRP A 1 36  ? 1.006   25.340  -46.901 1.00 53.42  ? 36  TRP A N   1 
ATOM 280  C CA  . TRP A 1 36  ? 0.657   24.174  -46.103 1.00 53.16  ? 36  TRP A CA  1 
ATOM 281  C C   . TRP A 1 36  ? 1.747   23.130  -46.302 1.00 52.81  ? 36  TRP A C   1 
ATOM 282  O O   . TRP A 1 36  ? 2.007   22.708  -47.435 1.00 52.89  ? 36  TRP A O   1 
ATOM 283  C CB  . TRP A 1 36  ? -0.700  23.619  -46.526 1.00 53.46  ? 36  TRP A CB  1 
ATOM 284  C CG  . TRP A 1 36  ? -1.847  24.440  -46.048 1.00 53.74  ? 36  TRP A CG  1 
ATOM 285  C CD1 . TRP A 1 36  ? -2.402  25.499  -46.691 1.00 54.16  ? 36  TRP A CD1 1 
ATOM 286  C CD2 . TRP A 1 36  ? -2.599  24.262  -44.842 1.00 53.64  ? 36  TRP A CD2 1 
ATOM 287  N NE1 . TRP A 1 36  ? -3.449  26.003  -45.964 1.00 54.33  ? 36  TRP A NE1 1 
ATOM 288  C CE2 . TRP A 1 36  ? -3.591  25.261  -44.822 1.00 54.00  ? 36  TRP A CE2 1 
ATOM 289  C CE3 . TRP A 1 36  ? -2.528  23.361  -43.776 1.00 53.80  ? 36  TRP A CE3 1 
ATOM 290  C CZ2 . TRP A 1 36  ? -4.506  25.386  -43.780 1.00 57.92  ? 36  TRP A CZ2 1 
ATOM 291  C CZ3 . TRP A 1 36  ? -3.439  23.486  -42.739 1.00 56.17  ? 36  TRP A CZ3 1 
ATOM 292  C CH2 . TRP A 1 36  ? -4.413  24.492  -42.749 1.00 59.88  ? 36  TRP A CH2 1 
ATOM 293  N N   . ILE A 1 37  ? 2.392   22.729  -45.212 1.00 52.44  ? 37  ILE A N   1 
ATOM 294  C CA  . ILE A 1 37  ? 3.446   21.724  -45.243 1.00 53.60  ? 37  ILE A CA  1 
ATOM 295  C C   . ILE A 1 37  ? 3.022   20.578  -44.338 1.00 53.45  ? 37  ILE A C   1 
ATOM 296  O O   . ILE A 1 37  ? 2.598   20.808  -43.200 1.00 57.48  ? 37  ILE A O   1 
ATOM 297  C CB  . ILE A 1 37  ? 4.799   22.300  -44.790 1.00 51.82  ? 37  ILE A CB  1 
ATOM 298  C CG1 . ILE A 1 37  ? 5.173   23.510  -45.639 1.00 52.01  ? 37  ILE A CG1 1 
ATOM 299  C CG2 . ILE A 1 37  ? 5.889   21.243  -44.898 1.00 51.49  ? 37  ILE A CG2 1 
ATOM 300  C CD1 . ILE A 1 37  ? 5.033   24.810  -44.892 1.00 52.14  ? 37  ILE A CD1 1 
ATOM 301  N N   . ARG A 1 38  ? 3.131   19.351  -44.841 1.00 51.90  ? 38  ARG A N   1 
ATOM 302  C CA  . ARG A 1 38  ? 2.758   18.170  -44.081 1.00 51.94  ? 38  ARG A CA  1 
ATOM 303  C C   . ARG A 1 38  ? 3.985   17.317  -43.789 1.00 53.69  ? 38  ARG A C   1 
ATOM 304  O O   . ARG A 1 38  ? 4.967   17.329  -44.539 1.00 54.30  ? 38  ARG A O   1 
ATOM 305  C CB  . ARG A 1 38  ? 1.700   17.337  -44.816 1.00 53.36  ? 38  ARG A CB  1 
ATOM 306  C CG  . ARG A 1 38  ? 2.175   16.608  -46.064 1.00 52.40  ? 38  ARG A CG  1 
ATOM 307  C CD  . ARG A 1 38  ? 1.022   15.795  -46.635 1.00 52.49  ? 38  ARG A CD  1 
ATOM 308  N NE  . ARG A 1 38  ? 1.399   14.927  -47.743 1.00 52.60  ? 38  ARG A NE  1 
ATOM 309  C CZ  . ARG A 1 38  ? 0.544   14.146  -48.389 1.00 52.92  ? 38  ARG A CZ  1 
ATOM 310  N NH1 . ARG A 1 38  ? -0.735  14.101  -48.056 1.00 53.15  ? 38  ARG A NH1 1 
ATOM 311  N NH2 . ARG A 1 38  ? 0.981   13.392  -49.394 1.00 57.66  ? 38  ARG A NH2 1 
ATOM 312  N N   . GLN A 1 39  ? 3.920   16.585  -42.678 1.00 51.36  ? 39  GLN A N   1 
ATOM 313  C CA  . GLN A 1 39  ? 4.998   15.705  -42.246 1.00 51.10  ? 39  GLN A CA  1 
ATOM 314  C C   . GLN A 1 39  ? 4.439   14.332  -41.918 1.00 55.27  ? 39  GLN A C   1 
ATOM 315  O O   . GLN A 1 39  ? 3.495   14.213  -41.133 1.00 57.03  ? 39  GLN A O   1 
ATOM 316  C CB  . GLN A 1 39  ? 5.732   16.260  -41.021 1.00 52.30  ? 39  GLN A CB  1 
ATOM 317  C CG  . GLN A 1 39  ? 7.049   15.554  -40.730 1.00 53.39  ? 39  GLN A CG  1 
ATOM 318  C CD  . GLN A 1 39  ? 7.751   16.097  -39.501 1.00 56.32  ? 39  GLN A CD  1 
ATOM 319  O OE1 . GLN A 1 39  ? 8.979   16.099  -39.424 1.00 57.06  ? 39  GLN A OE1 1 
ATOM 320  N NE2 . GLN A 1 39  ? 6.972   16.565  -38.533 1.00 55.42  ? 39  GLN A NE2 1 
ATOM 321  N N   . SER A 1 40  ? 5.029   13.303  -42.511 1.00 53.87  ? 40  SER A N   1 
ATOM 322  C CA  . SER A 1 40  ? 4.724   11.920  -42.181 1.00 51.25  ? 40  SER A CA  1 
ATOM 323  C C   . SER A 1 40  ? 5.981   11.104  -42.409 1.00 53.09  ? 40  SER A C   1 
ATOM 324  O O   . SER A 1 40  ? 6.865   11.522  -43.163 1.00 51.46  ? 40  SER A O   1 
ATOM 325  C CB  . SER A 1 40  ? 3.582   11.369  -43.039 1.00 56.97  ? 40  SER A CB  1 
ATOM 326  O OG  . SER A 1 40  ? 4.055   10.995  -44.323 1.00 60.94  ? 40  SER A OG  1 
ATOM 327  N N   . PRO A 1 41  ? 6.107   9.948   -41.760 1.00 58.24  ? 41  PRO A N   1 
ATOM 328  C CA  . PRO A 1 41  ? 7.259   9.086   -42.071 1.00 57.16  ? 41  PRO A CA  1 
ATOM 329  C C   . PRO A 1 41  ? 7.256   8.556   -43.498 1.00 55.84  ? 41  PRO A C   1 
ATOM 330  O O   . PRO A 1 41  ? 8.334   8.367   -44.073 1.00 52.17  ? 41  PRO A O   1 
ATOM 331  C CB  . PRO A 1 41  ? 7.150   7.966   -41.024 1.00 61.16  ? 41  PRO A CB  1 
ATOM 332  C CG  . PRO A 1 41  ? 5.771   8.095   -40.443 1.00 65.34  ? 41  PRO A CG  1 
ATOM 333  C CD  . PRO A 1 41  ? 5.431   9.535   -40.520 1.00 60.68  ? 41  PRO A CD  1 
ATOM 334  N N   . LYS A 1 42  ? 6.087   8.324   -44.102 1.00 55.57  ? 42  LYS A N   1 
ATOM 335  C CA  . LYS A 1 42  ? 6.068   7.863   -45.488 1.00 54.17  ? 42  LYS A CA  1 
ATOM 336  C C   . LYS A 1 42  ? 6.522   8.956   -46.445 1.00 51.55  ? 42  LYS A C   1 
ATOM 337  O O   . LYS A 1 42  ? 7.358   8.716   -47.323 1.00 51.50  ? 42  LYS A O   1 
ATOM 338  C CB  . LYS A 1 42  ? 4.677   7.370   -45.881 1.00 60.32  ? 42  LYS A CB  1 
ATOM 339  C CG  . LYS A 1 42  ? 4.024   6.424   -44.904 1.00 66.76  ? 42  LYS A CG  1 
ATOM 340  C CD  . LYS A 1 42  ? 2.739   5.896   -45.509 1.00 63.65  ? 42  LYS A CD  1 
ATOM 341  C CE  . LYS A 1 42  ? 1.930   5.104   -44.508 1.00 68.11  ? 42  LYS A CE  1 
ATOM 342  N NZ  . LYS A 1 42  ? 1.455   5.963   -43.387 1.00 76.80  ? 42  LYS A NZ  1 
ATOM 343  N N   . LYS A 1 43  ? 5.984   10.166  -46.290 1.00 53.94  ? 43  LYS A N   1 
ATOM 344  C CA  . LYS A 1 43  ? 6.269   11.269  -47.196 1.00 53.84  ? 43  LYS A CA  1 
ATOM 345  C C   . LYS A 1 43  ? 7.389   12.176  -46.705 1.00 51.14  ? 43  LYS A C   1 
ATOM 346  O O   . LYS A 1 43  ? 7.866   13.015  -47.476 1.00 51.10  ? 43  LYS A O   1 
ATOM 347  C CB  . LYS A 1 43  ? 5.006   12.113  -47.412 1.00 54.77  ? 43  LYS A CB  1 
ATOM 348  C CG  . LYS A 1 43  ? 3.770   11.311  -47.789 1.00 57.75  ? 43  LYS A CG  1 
ATOM 349  C CD  . LYS A 1 43  ? 3.993   10.411  -48.996 1.00 58.85  ? 43  LYS A CD  1 
ATOM 350  C CE  . LYS A 1 43  ? 4.339   11.216  -50.239 1.00 56.59  ? 43  LYS A CE  1 
ATOM 351  N NZ  . LYS A 1 43  ? 4.912   10.367  -51.319 1.00 62.32  ? 43  LYS A NZ  1 
ATOM 352  N N   . GLY A 1 44  ? 7.812   12.037  -45.451 1.00 50.91  ? 44  GLY A N   1 
ATOM 353  C CA  . GLY A 1 44  ? 8.824   12.936  -44.920 1.00 50.60  ? 44  GLY A CA  1 
ATOM 354  C C   . GLY A 1 44  ? 8.242   14.310  -44.663 1.00 52.31  ? 44  GLY A C   1 
ATOM 355  O O   . GLY A 1 44  ? 7.123   14.456  -44.162 1.00 53.23  ? 44  GLY A O   1 
ATOM 356  N N   . LEU A 1 45  ? 9.011   15.336  -45.009 1.00 50.98  ? 45  LEU A N   1 
ATOM 357  C CA  . LEU A 1 45  ? 8.537   16.711  -44.984 1.00 50.64  ? 45  LEU A CA  1 
ATOM 358  C C   . LEU A 1 45  ? 8.172   17.099  -46.410 1.00 51.95  ? 45  LEU A C   1 
ATOM 359  O O   . LEU A 1 45  ? 9.032   17.090  -47.296 1.00 53.02  ? 45  LEU A O   1 
ATOM 360  C CB  . LEU A 1 45  ? 9.600   17.647  -44.414 1.00 50.39  ? 45  LEU A CB  1 
ATOM 361  C CG  . LEU A 1 45  ? 9.284   18.208  -43.027 1.00 50.38  ? 45  LEU A CG  1 
ATOM 362  C CD1 . LEU A 1 45  ? 10.311  19.252  -42.625 1.00 50.21  ? 45  LEU A CD1 1 
ATOM 363  C CD2 . LEU A 1 45  ? 7.877   18.776  -42.984 1.00 51.44  ? 45  LEU A CD2 1 
ATOM 364  N N   . GLU A 1 46  ? 6.901   17.427  -46.636 1.00 55.81  ? 46  GLU A N   1 
ATOM 365  C CA  . GLU A 1 46  ? 6.389   17.590  -47.991 1.00 56.13  ? 46  GLU A CA  1 
ATOM 366  C C   . GLU A 1 46  ? 5.654   18.915  -48.140 1.00 60.48  ? 46  GLU A C   1 
ATOM 367  O O   . GLU A 1 46  ? 4.752   19.228  -47.356 1.00 60.92  ? 46  GLU A O   1 
ATOM 368  C CB  . GLU A 1 46  ? 5.464   16.426  -48.371 1.00 56.37  ? 46  GLU A CB  1 
ATOM 369  C CG  . GLU A 1 46  ? 5.224   16.290  -49.866 1.00 62.01  ? 46  GLU A CG  1 
ATOM 370  C CD  . GLU A 1 46  ? 4.193   15.230  -50.197 1.00 70.94  ? 46  GLU A CD  1 
ATOM 371  O OE1 . GLU A 1 46  ? 3.604   14.662  -49.256 1.00 62.92  ? 46  GLU A OE1 1 
ATOM 372  O OE2 . GLU A 1 46  ? 3.981   14.957  -51.397 1.00 81.25  ? 46  GLU A OE2 1 
ATOM 373  N N   . TRP A 1 47  ? 6.043   19.678  -49.158 1.00 57.63  ? 47  TRP A N   1 
ATOM 374  C CA  . TRP A 1 47  ? 5.377   20.921  -49.518 1.00 52.27  ? 47  TRP A CA  1 
ATOM 375  C C   . TRP A 1 47  ? 4.100   20.594  -50.283 1.00 52.71  ? 47  TRP A C   1 
ATOM 376  O O   . TRP A 1 47  ? 4.144   19.889  -51.296 1.00 55.65  ? 47  TRP A O   1 
ATOM 377  C CB  . TRP A 1 47  ? 6.316   21.764  -50.382 1.00 54.00  ? 47  TRP A CB  1 
ATOM 378  C CG  . TRP A 1 47  ? 5.846   23.133  -50.756 1.00 61.32  ? 47  TRP A CG  1 
ATOM 379  C CD1 . TRP A 1 47  ? 5.839   24.241  -49.965 1.00 60.32  ? 47  TRP A CD1 1 
ATOM 380  C CD2 . TRP A 1 47  ? 5.329   23.543  -52.026 1.00 63.93  ? 47  TRP A CD2 1 
ATOM 381  N NE1 . TRP A 1 47  ? 5.353   25.322  -50.666 1.00 56.48  ? 47  TRP A NE1 1 
ATOM 382  C CE2 . TRP A 1 47  ? 5.028   24.916  -51.933 1.00 61.82  ? 47  TRP A CE2 1 
ATOM 383  C CE3 . TRP A 1 47  ? 5.090   22.880  -53.232 1.00 61.06  ? 47  TRP A CE3 1 
ATOM 384  C CZ2 . TRP A 1 47  ? 4.500   25.637  -53.000 1.00 61.23  ? 47  TRP A CZ2 1 
ATOM 385  C CZ3 . TRP A 1 47  ? 4.566   23.598  -54.290 1.00 62.12  ? 47  TRP A CZ3 1 
ATOM 386  C CH2 . TRP A 1 47  ? 4.277   24.960  -54.167 1.00 63.98  ? 47  TRP A CH2 1 
ATOM 387  N N   . ILE A 1 48  ? 2.963   21.092  -49.800 1.00 52.94  ? 48  ILE A N   1 
ATOM 388  C CA  . ILE A 1 48  ? 1.700   20.846  -50.488 1.00 53.75  ? 48  ILE A CA  1 
ATOM 389  C C   . ILE A 1 48  ? 1.423   21.974  -51.471 1.00 56.53  ? 48  ILE A C   1 
ATOM 390  O O   . ILE A 1 48  ? 1.247   21.736  -52.671 1.00 56.88  ? 48  ILE A O   1 
ATOM 391  C CB  . ILE A 1 48  ? 0.531   20.683  -49.501 1.00 53.43  ? 48  ILE A CB  1 
ATOM 392  C CG1 . ILE A 1 48  ? 0.918   19.745  -48.360 1.00 53.50  ? 48  ILE A CG1 1 
ATOM 393  C CG2 . ILE A 1 48  ? -0.696  20.156  -50.224 1.00 53.85  ? 48  ILE A CG2 1 
ATOM 394  C CD1 . ILE A 1 48  ? 0.048   19.889  -47.133 1.00 53.20  ? 48  ILE A CD1 1 
ATOM 395  N N   . GLY A 1 49  ? 1.377   23.204  -50.976 1.00 60.94  ? 49  GLY A N   1 
ATOM 396  C CA  . GLY A 1 49  ? 1.129   24.335  -51.849 1.00 62.35  ? 49  GLY A CA  1 
ATOM 397  C C   . GLY A 1 49  ? 1.176   25.634  -51.076 1.00 63.53  ? 49  GLY A C   1 
ATOM 398  O O   . GLY A 1 49  ? 1.117   25.660  -49.843 1.00 63.38  ? 49  GLY A O   1 
ATOM 399  N N   . GLU A 1 50  ? 1.279   26.724  -51.833 1.00 60.93  ? 50  GLU A N   1 
ATOM 400  C CA  . GLU A 1 50  ? 1.262   28.070  -51.284 1.00 55.20  ? 50  GLU A CA  1 
ATOM 401  C C   . GLU A 1 50  ? 0.130   28.860  -51.925 1.00 55.47  ? 50  GLU A C   1 
ATOM 402  O O   . GLU A 1 50  ? -0.401  28.482  -52.972 1.00 55.81  ? 50  GLU A O   1 
ATOM 403  C CB  . GLU A 1 50  ? 2.597   28.787  -51.506 1.00 54.71  ? 50  GLU A CB  1 
ATOM 404  C CG  . GLU A 1 50  ? 2.813   29.266  -52.928 1.00 57.49  ? 50  GLU A CG  1 
ATOM 405  C CD  . GLU A 1 50  ? 4.233   29.727  -53.166 1.00 58.26  ? 50  GLU A CD  1 
ATOM 406  O OE1 . GLU A 1 50  ? 5.086   29.494  -52.285 1.00 56.86  ? 50  GLU A OE1 1 
ATOM 407  O OE2 . GLU A 1 50  ? 4.497   30.322  -54.231 1.00 56.57  ? 50  GLU A OE2 1 
ATOM 408  N N   . ILE A 1 51  ? -0.242  29.971  -51.283 1.00 55.67  ? 51  ILE A N   1 
ATOM 409  C CA  . ILE A 1 51  ? -1.325  30.815  -51.771 1.00 56.78  ? 51  ILE A CA  1 
ATOM 410  C C   . ILE A 1 51  ? -0.967  32.284  -51.572 1.00 59.62  ? 51  ILE A C   1 
ATOM 411  O O   . ILE A 1 51  ? -0.163  32.645  -50.710 1.00 61.84  ? 51  ILE A O   1 
ATOM 412  C CB  . ILE A 1 51  ? -2.675  30.491  -51.086 1.00 56.37  ? 51  ILE A CB  1 
ATOM 413  C CG1 . ILE A 1 51  ? -3.834  30.994  -51.948 1.00 57.05  ? 51  ILE A CG1 1 
ATOM 414  C CG2 . ILE A 1 51  ? -2.741  31.105  -49.695 1.00 57.07  ? 51  ILE A CG2 1 
ATOM 415  C CD1 . ILE A 1 51  ? -5.191  30.616  -51.438 1.00 57.14  ? 51  ILE A CD1 1 
ATOM 416  N N   . ASP A 1 52  ? -1.574  33.129  -52.398 1.00 62.23  ? 52  ASP A N   1 
ATOM 417  C CA  . ASP A 1 52  ? -1.405  34.573  -52.351 1.00 63.28  ? 52  ASP A CA  1 
ATOM 418  C C   . ASP A 1 52  ? -2.597  35.215  -51.644 1.00 63.77  ? 52  ASP A C   1 
ATOM 419  O O   . ASP A 1 52  ? -3.583  34.556  -51.308 1.00 63.68  ? 52  ASP A O   1 
ATOM 420  C CB  . ASP A 1 52  ? -1.263  35.133  -53.770 1.00 64.21  ? 52  ASP A CB  1 
ATOM 421  C CG  . ASP A 1 52  ? -0.254  36.262  -53.862 1.00 72.31  ? 52  ASP A CG  1 
ATOM 422  O OD1 . ASP A 1 52  ? 0.099   36.842  -52.816 1.00 82.45  ? 52  ASP A OD1 1 
ATOM 423  O OD2 . ASP A 1 52  ? 0.183   36.572  -54.990 1.00 76.66  ? 52  ASP A OD2 1 
ATOM 424  N N   . GLU A 1 53  ? -2.498  36.526  -51.414 1.00 66.81  ? 53  GLU A N   1 
ATOM 425  C CA  . GLU A 1 53  ? -3.669  37.259  -50.943 1.00 66.53  ? 53  GLU A CA  1 
ATOM 426  C C   . GLU A 1 53  ? -4.634  37.545  -52.085 1.00 69.98  ? 53  GLU A C   1 
ATOM 427  O O   . GLU A 1 53  ? -5.842  37.671  -51.856 1.00 72.48  ? 53  GLU A O   1 
ATOM 428  C CB  . GLU A 1 53  ? -3.261  38.571  -50.272 1.00 61.57  ? 53  GLU A CB  1 
ATOM 429  C CG  . GLU A 1 53  ? -2.562  39.546  -51.198 1.00 63.03  ? 53  GLU A CG  1 
ATOM 430  C CD  . GLU A 1 53  ? -1.082  39.645  -50.922 1.00 61.60  ? 53  GLU A CD  1 
ATOM 431  O OE1 . GLU A 1 53  ? -0.433  38.589  -50.788 1.00 64.36  ? 53  GLU A OE1 1 
ATOM 432  O OE2 . GLU A 1 53  ? -0.565  40.776  -50.849 1.00 61.99  ? 53  GLU A OE2 1 
ATOM 433  N N   . ILE A 1 54  ? -4.117  37.651  -53.312 1.00 70.95  ? 54  ILE A N   1 
ATOM 434  C CA  . ILE A 1 54  ? -4.974  37.841  -54.475 1.00 67.35  ? 54  ILE A CA  1 
ATOM 435  C C   . ILE A 1 54  ? -5.784  36.583  -54.752 1.00 70.60  ? 54  ILE A C   1 
ATOM 436  O O   . ILE A 1 54  ? -6.900  36.656  -55.281 1.00 71.13  ? 54  ILE A O   1 
ATOM 437  C CB  . ILE A 1 54  ? -4.122  38.239  -55.695 1.00 70.99  ? 54  ILE A CB  1 
ATOM 438  C CG1 . ILE A 1 54  ? -2.966  39.148  -55.269 1.00 75.49  ? 54  ILE A CG1 1 
ATOM 439  C CG2 . ILE A 1 54  ? -4.977  38.918  -56.753 1.00 72.93  ? 54  ILE A CG2 1 
ATOM 440  C CD1 . ILE A 1 54  ? -1.841  39.224  -56.282 1.00 72.97  ? 54  ILE A CD1 1 
ATOM 441  N N   . GLY A 1 55  ? -5.248  35.421  -54.395 1.00 64.89  ? 55  GLY A N   1 
ATOM 442  C CA  . GLY A 1 55  ? -5.857  34.141  -54.704 1.00 63.29  ? 55  GLY A CA  1 
ATOM 443  C C   . GLY A 1 55  ? -5.003  33.239  -55.568 1.00 62.24  ? 55  GLY A C   1 
ATOM 444  O O   . GLY A 1 55  ? -5.362  32.067  -55.754 1.00 61.33  ? 55  GLY A O   1 
ATOM 445  N N   . ARG A 1 56  ? -3.890  33.733  -56.105 1.00 59.33  ? 56  ARG A N   1 
ATOM 446  C CA  . ARG A 1 56  ? -3.018  32.904  -56.924 1.00 58.99  ? 56  ARG A CA  1 
ATOM 447  C C   . ARG A 1 56  ? -2.410  31.785  -56.089 1.00 59.03  ? 56  ARG A C   1 
ATOM 448  O O   . ARG A 1 56  ? -2.062  31.975  -54.921 1.00 58.73  ? 56  ARG A O   1 
ATOM 449  C CB  . ARG A 1 56  ? -1.916  33.753  -57.552 1.00 60.84  ? 56  ARG A CB  1 
ATOM 450  C CG  . ARG A 1 56  ? -2.416  35.083  -58.084 1.00 72.13  ? 56  ARG A CG  1 
ATOM 451  C CD  . ARG A 1 56  ? -1.320  35.862  -58.785 1.00 77.36  ? 56  ARG A CD  1 
ATOM 452  N NE  . ARG A 1 56  ? -0.126  36.011  -57.960 1.00 87.59  ? 56  ARG A NE  1 
ATOM 453  C CZ  . ARG A 1 56  ? 0.984   36.615  -58.361 1.00 85.72  ? 56  ARG A CZ  1 
ATOM 454  N NH1 . ARG A 1 56  ? 1.082   37.151  -59.567 1.00 82.48  ? 56  ARG A NH1 1 
ATOM 455  N NH2 . ARG A 1 56  ? 2.022   36.686  -57.530 1.00 80.60  ? 56  ARG A NH2 1 
ATOM 456  N N   . THR A 1 57  ? -2.283  30.609  -56.699 1.00 59.95  ? 57  THR A N   1 
ATOM 457  C CA  . THR A 1 57  ? -1.870  29.400  -56.004 1.00 57.36  ? 57  THR A CA  1 
ATOM 458  C C   . THR A 1 57  ? -0.755  28.701  -56.767 1.00 57.12  ? 57  THR A C   1 
ATOM 459  O O   . THR A 1 57  ? -0.689  28.760  -57.997 1.00 57.54  ? 57  THR A O   1 
ATOM 460  C CB  . THR A 1 57  ? -3.046  28.428  -55.833 1.00 57.41  ? 57  THR A CB  1 
ATOM 461  O OG1 . THR A 1 57  ? -3.639  28.172  -57.112 1.00 59.19  ? 57  THR A OG1 1 
ATOM 462  C CG2 . THR A 1 57  ? -4.099  29.004  -54.901 1.00 57.53  ? 57  THR A CG2 1 
ATOM 463  N N   . LYS A 1 58  ? 0.119   28.030  -56.020 1.00 56.47  ? 58  LYS A N   1 
ATOM 464  C CA  . LYS A 1 58  ? 1.112   27.128  -56.586 1.00 56.16  ? 58  LYS A CA  1 
ATOM 465  C C   . LYS A 1 58  ? 1.005   25.793  -55.868 1.00 57.81  ? 58  LYS A C   1 
ATOM 466  O O   . LYS A 1 58  ? 1.006   25.750  -54.634 1.00 60.33  ? 58  LYS A O   1 
ATOM 467  C CB  . LYS A 1 58  ? 2.533   27.693  -56.463 1.00 55.82  ? 58  LYS A CB  1 
ATOM 468  C CG  . LYS A 1 58  ? 3.580   26.862  -57.195 1.00 55.55  ? 58  LYS A CG  1 
ATOM 469  C CD  . LYS A 1 58  ? 4.919   27.579  -57.284 1.00 57.18  ? 58  LYS A CD  1 
ATOM 470  C CE  . LYS A 1 58  ? 5.892   26.821  -58.176 1.00 64.38  ? 58  LYS A CE  1 
ATOM 471  N NZ  . LYS A 1 58  ? 7.123   27.611  -58.457 1.00 65.19  ? 58  LYS A NZ  1 
ATOM 472  N N   . TYR A 1 59  ? 0.903   24.711  -56.633 1.00 60.36  ? 59  TYR A N   1 
ATOM 473  C CA  . TYR A 1 59  ? 0.688   23.381  -56.082 1.00 58.27  ? 59  TYR A CA  1 
ATOM 474  C C   . TYR A 1 59  ? 1.823   22.441  -56.462 1.00 62.42  ? 59  TYR A C   1 
ATOM 475  O O   . TYR A 1 59  ? 2.520   22.650  -57.460 1.00 63.09  ? 59  TYR A O   1 
ATOM 476  C CB  . TYR A 1 59  ? -0.631  22.775  -56.576 1.00 57.60  ? 59  TYR A CB  1 
ATOM 477  C CG  . TYR A 1 59  ? -1.882  23.486  -56.126 1.00 56.23  ? 59  TYR A CG  1 
ATOM 478  C CD1 . TYR A 1 59  ? -2.341  23.358  -54.823 1.00 55.92  ? 59  TYR A CD1 1 
ATOM 479  C CD2 . TYR A 1 59  ? -2.622  24.258  -57.010 1.00 59.70  ? 59  TYR A CD2 1 
ATOM 480  C CE1 . TYR A 1 59  ? -3.493  23.991  -54.407 1.00 56.21  ? 59  TYR A CE1 1 
ATOM 481  C CE2 . TYR A 1 59  ? -3.776  24.897  -56.604 1.00 61.51  ? 59  TYR A CE2 1 
ATOM 482  C CZ  . TYR A 1 59  ? -4.207  24.759  -55.301 1.00 58.06  ? 59  TYR A CZ  1 
ATOM 483  O OH  . TYR A 1 59  ? -5.355  25.392  -54.890 1.00 65.28  ? 59  TYR A OH  1 
ATOM 484  N N   . SER A 1 60  ? 2.000   21.399  -55.654 1.00 61.87  ? 60  SER A N   1 
ATOM 485  C CA  . SER A 1 60  ? 2.819   20.272  -56.075 1.00 60.77  ? 60  SER A CA  1 
ATOM 486  C C   . SER A 1 60  ? 2.065   19.486  -57.141 1.00 70.93  ? 60  SER A C   1 
ATOM 487  O O   . SER A 1 60  ? 0.837   19.371  -57.091 1.00 74.68  ? 60  SER A O   1 
ATOM 488  C CB  . SER A 1 60  ? 3.159   19.373  -54.885 1.00 57.86  ? 60  SER A CB  1 
ATOM 489  O OG  . SER A 1 60  ? 3.529   20.132  -53.746 1.00 68.00  ? 60  SER A OG  1 
ATOM 490  N N   . GLN A 1 61  ? 2.802   18.959  -58.124 1.00 71.57  ? 61  GLN A N   1 
ATOM 491  C CA  . GLN A 1 61  ? 2.159   18.247  -59.227 1.00 74.58  ? 61  GLN A CA  1 
ATOM 492  C C   . GLN A 1 61  ? 1.383   17.032  -58.736 1.00 75.63  ? 61  GLN A C   1 
ATOM 493  O O   . GLN A 1 61  ? 0.267   16.771  -59.201 1.00 79.07  ? 61  GLN A O   1 
ATOM 494  C CB  . GLN A 1 61  ? 3.195   17.823  -60.267 1.00 77.77  ? 61  GLN A CB  1 
ATOM 495  C CG  . GLN A 1 61  ? 3.886   18.964  -60.991 1.00 86.63  ? 61  GLN A CG  1 
ATOM 496  C CD  . GLN A 1 61  ? 4.570   18.506  -62.269 1.00 90.47  ? 61  GLN A CD  1 
ATOM 497  O OE1 . GLN A 1 61  ? 4.416   17.361  -62.698 1.00 87.00  ? 61  GLN A OE1 1 
ATOM 498  N NE2 . GLN A 1 61  ? 5.326   19.405  -62.887 1.00 94.60  ? 61  GLN A NE2 1 
ATOM 499  N N   . SER A 1 62  ? 1.962   16.272  -57.804 1.00 80.74  ? 62  SER A N   1 
ATOM 500  C CA  . SER A 1 62  ? 1.305   15.060  -57.323 1.00 79.18  ? 62  SER A CA  1 
ATOM 501  C C   . SER A 1 62  ? -0.018  15.378  -56.640 1.00 82.82  ? 62  SER A C   1 
ATOM 502  O O   . SER A 1 62  ? -1.014  14.672  -56.839 1.00 84.40  ? 62  SER A O   1 
ATOM 503  C CB  . SER A 1 62  ? 2.225   14.306  -56.363 1.00 77.43  ? 62  SER A CB  1 
ATOM 504  O OG  . SER A 1 62  ? 3.512   14.119  -56.923 1.00 85.33  ? 62  SER A OG  1 
ATOM 505  N N   . LEU A 1 63  ? -0.050  16.434  -55.833 1.00 74.74  ? 63  LEU A N   1 
ATOM 506  C CA  . LEU A 1 63  ? -1.245  16.779  -55.079 1.00 72.39  ? 63  LEU A CA  1 
ATOM 507  C C   . LEU A 1 63  ? -2.145  17.773  -55.802 1.00 72.03  ? 63  LEU A C   1 
ATOM 508  O O   . LEU A 1 63  ? -3.236  18.067  -55.304 1.00 68.24  ? 63  LEU A O   1 
ATOM 509  C CB  . LEU A 1 63  ? -0.855  17.336  -53.706 1.00 62.24  ? 63  LEU A CB  1 
ATOM 510  C CG  . LEU A 1 63  ? -0.020  16.396  -52.837 1.00 63.45  ? 63  LEU A CG  1 
ATOM 511  C CD1 . LEU A 1 63  ? 0.956   17.178  -51.972 1.00 56.85  ? 63  LEU A CD1 1 
ATOM 512  C CD2 . LEU A 1 63  ? -0.925  15.530  -51.979 1.00 66.68  ? 63  LEU A CD2 1 
ATOM 513  N N   . ARG A 1 64  ? -1.723  18.276  -56.966 1.00 70.30  ? 64  ARG A N   1 
ATOM 514  C CA  . ARG A 1 64  ? -2.523  19.253  -57.702 1.00 69.08  ? 64  ARG A CA  1 
ATOM 515  C C   . ARG A 1 64  ? -3.918  18.720  -58.006 1.00 70.38  ? 64  ARG A C   1 
ATOM 516  O O   . ARG A 1 64  ? -4.892  19.482  -58.022 1.00 71.22  ? 64  ARG A O   1 
ATOM 517  C CB  . ARG A 1 64  ? -1.817  19.629  -59.004 1.00 70.02  ? 64  ARG A CB  1 
ATOM 518  C CG  . ARG A 1 64  ? -2.580  20.618  -59.867 1.00 75.08  ? 64  ARG A CG  1 
ATOM 519  C CD  . ARG A 1 64  ? -1.819  21.921  -59.995 1.00 79.96  ? 64  ARG A CD  1 
ATOM 520  N NE  . ARG A 1 64  ? -0.419  21.679  -60.321 1.00 85.28  ? 64  ARG A NE  1 
ATOM 521  C CZ  . ARG A 1 64  ? 0.065   21.636  -61.555 1.00 93.43  ? 64  ARG A CZ  1 
ATOM 522  N NH1 . ARG A 1 64  ? -0.713  21.826  -62.609 1.00 87.43  ? 64  ARG A NH1 1 
ATOM 523  N NH2 . ARG A 1 64  ? 1.361   21.389  -61.736 1.00 84.48  ? 64  ARG A NH2 1 
ATOM 524  N N   . SER A 1 65  ? -4.032  17.412  -58.248 1.00 69.44  ? 65  SER A N   1 
ATOM 525  C CA  . SER A 1 65  ? -5.297  16.851  -58.714 1.00 63.68  ? 65  SER A CA  1 
ATOM 526  C C   . SER A 1 65  ? -6.387  16.956  -57.655 1.00 66.72  ? 65  SER A C   1 
ATOM 527  O O   . SER A 1 65  ? -7.560  17.162  -57.985 1.00 66.86  ? 65  SER A O   1 
ATOM 528  C CB  . SER A 1 65  ? -5.103  15.394  -59.131 1.00 60.48  ? 65  SER A CB  1 
ATOM 529  O OG  . SER A 1 65  ? -3.860  15.200  -59.783 1.00 58.12  ? 65  SER A OG  1 
ATOM 530  N N   . ARG A 1 66  ? -6.028  16.813  -56.378 1.00 67.35  ? 66  ARG A N   1 
ATOM 531  C CA  . ARG A 1 66  ? -7.022  16.728  -55.314 1.00 64.05  ? 66  ARG A CA  1 
ATOM 532  C C   . ARG A 1 66  ? -6.880  17.820  -54.260 1.00 65.94  ? 66  ARG A C   1 
ATOM 533  O O   . ARG A 1 66  ? -7.487  17.705  -53.189 1.00 68.24  ? 66  ARG A O   1 
ATOM 534  C CB  . ARG A 1 66  ? -6.958  15.359  -54.627 1.00 65.87  ? 66  ARG A CB  1 
ATOM 535  C CG  . ARG A 1 66  ? -6.826  14.167  -55.559 1.00 64.07  ? 66  ARG A CG  1 
ATOM 536  C CD  . ARG A 1 66  ? -5.503  13.453  -55.319 1.00 57.94  ? 66  ARG A CD  1 
ATOM 537  N NE  . ARG A 1 66  ? -5.305  13.162  -53.904 1.00 55.82  ? 66  ARG A NE  1 
ATOM 538  C CZ  . ARG A 1 66  ? -4.214  12.605  -53.395 1.00 58.78  ? 66  ARG A CZ  1 
ATOM 539  N NH1 . ARG A 1 66  ? -3.196  12.251  -54.162 1.00 65.58  ? 66  ARG A NH1 1 
ATOM 540  N NH2 . ARG A 1 66  ? -4.143  12.399  -52.082 1.00 56.40  ? 66  ARG A NH2 1 
ATOM 541  N N   . ALA A 1 67  ? -6.104  18.869  -54.519 1.00 69.11  ? 67  ALA A N   1 
ATOM 542  C CA  . ALA A 1 67  ? -5.862  19.913  -53.531 1.00 66.55  ? 67  ALA A CA  1 
ATOM 543  C C   . ALA A 1 67  ? -6.428  21.244  -54.007 1.00 64.68  ? 67  ALA A C   1 
ATOM 544  O O   . ALA A 1 67  ? -6.250  21.629  -55.167 1.00 67.83  ? 67  ALA A O   1 
ATOM 545  C CB  . ALA A 1 67  ? -4.369  20.063  -53.230 1.00 61.83  ? 67  ALA A CB  1 
ATOM 546  N N   . THR A 1 68  ? -7.104  21.946  -53.099 1.00 67.29  ? 68  THR A N   1 
ATOM 547  C CA  . THR A 1 68  ? -7.686  23.255  -53.379 1.00 68.80  ? 68  THR A CA  1 
ATOM 548  C C   . THR A 1 68  ? -7.327  24.199  -52.241 1.00 65.71  ? 68  THR A C   1 
ATOM 549  O O   . THR A 1 68  ? -7.807  24.032  -51.115 1.00 63.00  ? 68  THR A O   1 
ATOM 550  C CB  . THR A 1 68  ? -9.203  23.168  -53.549 1.00 74.09  ? 68  THR A CB  1 
ATOM 551  O OG1 . THR A 1 68  ? -9.524  22.133  -54.488 1.00 88.58  ? 68  THR A OG1 1 
ATOM 552  C CG2 . THR A 1 68  ? -9.762  24.495  -54.040 1.00 66.25  ? 68  THR A CG2 1 
ATOM 553  N N   . LEU A 1 69  ? -6.486  25.186  -52.534 1.00 62.50  ? 69  LEU A N   1 
ATOM 554  C CA  . LEU A 1 69  ? -6.108  26.199  -51.558 1.00 56.39  ? 69  LEU A CA  1 
ATOM 555  C C   . LEU A 1 69  ? -7.025  27.407  -51.694 1.00 56.91  ? 69  LEU A C   1 
ATOM 556  O O   . LEU A 1 69  ? -7.239  27.910  -52.802 1.00 63.99  ? 69  LEU A O   1 
ATOM 557  C CB  . LEU A 1 69  ? -4.648  26.613  -51.749 1.00 56.16  ? 69  LEU A CB  1 
ATOM 558  C CG  . LEU A 1 69  ? -3.624  25.777  -50.983 1.00 55.53  ? 69  LEU A CG  1 
ATOM 559  C CD1 . LEU A 1 69  ? -2.211  26.286  -51.213 1.00 55.33  ? 69  LEU A CD1 1 
ATOM 560  C CD2 . LEU A 1 69  ? -3.968  25.806  -49.516 1.00 56.69  ? 69  LEU A CD2 1 
ATOM 561  N N   . SER A 1 70  ? -7.570  27.864  -50.569 1.00 56.80  ? 70  SER A N   1 
ATOM 562  C CA  . SER A 1 70  ? -8.451  29.021  -50.539 1.00 58.05  ? 70  SER A CA  1 
ATOM 563  C C   . SER A 1 70  ? -7.925  30.029  -49.529 1.00 63.09  ? 70  SER A C   1 
ATOM 564  O O   . SER A 1 70  ? -7.100  29.706  -48.671 1.00 67.21  ? 70  SER A O   1 
ATOM 565  C CB  . SER A 1 70  ? -9.888  28.631  -50.180 1.00 57.55  ? 70  SER A CB  1 
ATOM 566  O OG  . SER A 1 70  ? -9.936  27.990  -48.917 1.00 62.66  ? 70  SER A OG  1 
ATOM 567  N N   . ILE A 1 71  ? -8.415  31.263  -49.639 1.00 59.11  ? 71  ILE A N   1 
ATOM 568  C CA  . ILE A 1 71  ? -8.020  32.335  -48.733 1.00 61.95  ? 71  ILE A CA  1 
ATOM 569  C C   . ILE A 1 71  ? -9.149  33.353  -48.653 1.00 65.04  ? 71  ILE A C   1 
ATOM 570  O O   . ILE A 1 71  ? -9.893  33.566  -49.615 1.00 68.20  ? 71  ILE A O   1 
ATOM 571  C CB  . ILE A 1 71  ? -6.694  33.006  -49.169 1.00 61.33  ? 71  ILE A CB  1 
ATOM 572  C CG1 . ILE A 1 71  ? -6.091  33.795  -48.007 1.00 62.79  ? 71  ILE A CG1 1 
ATOM 573  C CG2 . ILE A 1 71  ? -6.908  33.906  -50.377 1.00 61.79  ? 71  ILE A CG2 1 
ATOM 574  C CD1 . ILE A 1 71  ? -4.713  34.349  -48.281 1.00 58.52  ? 71  ILE A CD1 1 
ATOM 575  N N   . ASP A 1 72  ? -9.275  33.975  -47.482 1.00 67.63  ? 72  ASP A N   1 
ATOM 576  C CA  . ASP A 1 72  ? -10.243 35.045  -47.240 1.00 74.59  ? 72  ASP A CA  1 
ATOM 577  C C   . ASP A 1 72  ? -9.515  36.110  -46.426 1.00 79.20  ? 72  ASP A C   1 
ATOM 578  O O   . ASP A 1 72  ? -9.360  35.968  -45.210 1.00 81.00  ? 72  ASP A O   1 
ATOM 579  C CB  . ASP A 1 72  ? -11.479 34.526  -46.512 1.00 72.52  ? 72  ASP A CB  1 
ATOM 580  C CG  . ASP A 1 72  ? -12.590 35.559  -46.424 1.00 79.54  ? 72  ASP A CG  1 
ATOM 581  O OD1 . ASP A 1 72  ? -12.425 36.674  -46.965 1.00 81.84  ? 72  ASP A OD1 1 
ATOM 582  O OD2 . ASP A 1 72  ? -13.632 35.253  -45.808 1.00 83.08  ? 72  ASP A OD2 1 
ATOM 583  N N   . THR A 1 73  ? -9.064  37.169  -47.104 1.00 72.75  ? 73  THR A N   1 
ATOM 584  C CA  . THR A 1 73  ? -8.299  38.216  -46.434 1.00 68.20  ? 73  THR A CA  1 
ATOM 585  C C   . THR A 1 73  ? -9.121  38.924  -45.365 1.00 73.00  ? 73  THR A C   1 
ATOM 586  O O   . THR A 1 73  ? -8.573  39.346  -44.340 1.00 77.97  ? 73  THR A O   1 
ATOM 587  C CB  . THR A 1 73  ? -7.790  39.226  -47.459 1.00 74.43  ? 73  THR A CB  1 
ATOM 588  O OG1 . THR A 1 73  ? -8.906  39.798  -48.156 1.00 84.51  ? 73  THR A OG1 1 
ATOM 589  C CG2 . THR A 1 73  ? -6.862  38.552  -48.457 1.00 71.48  ? 73  THR A CG2 1 
ATOM 590  N N   . SER A 1 74  ? -10.429 39.072  -45.587 1.00 73.83  ? 74  SER A N   1 
ATOM 591  C CA  . SER A 1 74  ? -11.270 39.748  -44.605 1.00 79.23  ? 74  SER A CA  1 
ATOM 592  C C   . SER A 1 74  ? -11.345 38.959  -43.304 1.00 79.69  ? 74  SER A C   1 
ATOM 593  O O   . SER A 1 74  ? -11.227 39.534  -42.214 1.00 76.62  ? 74  SER A O   1 
ATOM 594  C CB  . SER A 1 74  ? -12.669 39.973  -45.175 1.00 82.76  ? 74  SER A CB  1 
ATOM 595  O OG  . SER A 1 74  ? -13.315 38.741  -45.447 1.00 90.06  ? 74  SER A OG  1 
ATOM 596  N N   . LYS A 1 75  ? -11.540 37.647  -43.394 1.00 84.97  ? 75  LYS A N   1 
ATOM 597  C CA  . LYS A 1 75  ? -11.600 36.801  -42.211 1.00 84.93  ? 75  LYS A CA  1 
ATOM 598  C C   . LYS A 1 75  ? -10.223 36.353  -41.748 1.00 84.46  ? 75  LYS A C   1 
ATOM 599  O O   . LYS A 1 75  ? -10.117 35.709  -40.699 1.00 84.33  ? 75  LYS A O   1 
ATOM 600  C CB  . LYS A 1 75  ? -12.491 35.584  -42.481 1.00 84.55  ? 75  LYS A CB  1 
ATOM 601  C CG  . LYS A 1 75  ? -13.957 35.945  -42.628 1.00 86.07  ? 75  LYS A CG  1 
ATOM 602  C CD  . LYS A 1 75  ? -14.511 36.572  -41.360 1.00 98.05  ? 75  LYS A CD  1 
ATOM 603  C CE  . LYS A 1 75  ? -15.845 37.244  -41.633 1.00 93.86  ? 75  LYS A CE  1 
ATOM 604  N NZ  . LYS A 1 75  ? -15.686 38.405  -42.557 1.00 89.19  ? 75  LYS A NZ  1 
ATOM 605  N N   . LYS A 1 76  ? -9.178  36.686  -42.504 1.00 76.51  ? 76  LYS A N   1 
ATOM 606  C CA  . LYS A 1 76  ? -7.792  36.373  -42.158 1.00 68.35  ? 76  LYS A CA  1 
ATOM 607  C C   . LYS A 1 76  ? -7.605  34.883  -41.882 1.00 68.66  ? 76  LYS A C   1 
ATOM 608  O O   . LYS A 1 76  ? -6.998  34.478  -40.888 1.00 69.30  ? 76  LYS A O   1 
ATOM 609  C CB  . LYS A 1 76  ? -7.319  37.220  -40.974 1.00 69.25  ? 76  LYS A CB  1 
ATOM 610  C CG  . LYS A 1 76  ? -7.264  38.707  -41.277 1.00 65.08  ? 76  LYS A CG  1 
ATOM 611  C CD  . LYS A 1 76  ? -7.123  39.538  -40.014 1.00 63.82  ? 76  LYS A CD  1 
ATOM 612  C CE  . LYS A 1 76  ? -5.779  39.301  -39.351 1.00 65.43  ? 76  LYS A CE  1 
ATOM 613  N NZ  . LYS A 1 76  ? -5.576  40.199  -38.184 1.00 61.37  ? 76  LYS A NZ  1 
ATOM 614  N N   . GLN A 1 77  ? -8.125  34.056  -42.786 1.00 68.33  ? 77  GLN A N   1 
ATOM 615  C CA  . GLN A 1 77  ? -7.938  32.615  -42.673 1.00 63.34  ? 77  GLN A CA  1 
ATOM 616  C C   . GLN A 1 77  ? -7.895  31.987  -44.059 1.00 64.43  ? 77  GLN A C   1 
ATOM 617  O O   . GLN A 1 77  ? -8.720  32.310  -44.919 1.00 69.95  ? 77  GLN A O   1 
ATOM 618  C CB  . GLN A 1 77  ? -9.042  31.977  -41.820 1.00 62.57  ? 77  GLN A CB  1 
ATOM 619  C CG  . GLN A 1 77  ? -10.451 32.192  -42.334 1.00 66.44  ? 77  GLN A CG  1 
ATOM 620  C CD  . GLN A 1 77  ? -11.504 31.836  -41.307 1.00 65.70  ? 77  GLN A CD  1 
ATOM 621  O OE1 . GLN A 1 77  ? -11.249 31.863  -40.103 1.00 62.34  ? 77  GLN A OE1 1 
ATOM 622  N NE2 . GLN A 1 77  ? -12.697 31.499  -41.778 1.00 63.13  ? 77  GLN A NE2 1 
ATOM 623  N N   . PHE A 1 78  ? -6.921  31.106  -44.267 1.00 62.53  ? 78  PHE A N   1 
ATOM 624  C CA  . PHE A 1 78  ? -6.780  30.322  -45.484 1.00 59.59  ? 78  PHE A CA  1 
ATOM 625  C C   . PHE A 1 78  ? -6.968  28.843  -45.165 1.00 65.90  ? 78  PHE A C   1 
ATOM 626  O O   . PHE A 1 78  ? -6.853  28.415  -44.014 1.00 63.81  ? 78  PHE A O   1 
ATOM 627  C CB  . PHE A 1 78  ? -5.416  30.558  -46.154 1.00 55.80  ? 78  PHE A CB  1 
ATOM 628  C CG  . PHE A 1 78  ? -4.228  30.283  -45.265 1.00 55.28  ? 78  PHE A CG  1 
ATOM 629  C CD1 . PHE A 1 78  ? -3.924  31.116  -44.197 1.00 60.83  ? 78  PHE A CD1 1 
ATOM 630  C CD2 . PHE A 1 78  ? -3.407  29.193  -45.508 1.00 56.01  ? 78  PHE A CD2 1 
ATOM 631  C CE1 . PHE A 1 78  ? -2.834  30.861  -43.386 1.00 64.15  ? 78  PHE A CE1 1 
ATOM 632  C CE2 . PHE A 1 78  ? -2.313  28.935  -44.701 1.00 61.71  ? 78  PHE A CE2 1 
ATOM 633  C CZ  . PHE A 1 78  ? -2.026  29.772  -43.641 1.00 67.19  ? 78  PHE A CZ  1 
ATOM 634  N N   . SER A 1 79  ? -7.268  28.059  -46.199 1.00 68.03  ? 79  SER A N   1 
ATOM 635  C CA  . SER A 1 79  ? -7.629  26.663  -46.001 1.00 65.94  ? 79  SER A CA  1 
ATOM 636  C C   . SER A 1 79  ? -7.053  25.798  -47.112 1.00 65.13  ? 79  SER A C   1 
ATOM 637  O O   . SER A 1 79  ? -6.803  26.261  -48.226 1.00 65.49  ? 79  SER A O   1 
ATOM 638  C CB  . SER A 1 79  ? -9.152  26.483  -45.944 1.00 66.66  ? 79  SER A CB  1 
ATOM 639  O OG  . SER A 1 79  ? -9.757  27.504  -45.172 1.00 72.57  ? 79  SER A OG  1 
ATOM 640  N N   . LEU A 1 80  ? -6.853  24.520  -46.789 1.00 64.87  ? 80  LEU A N   1 
ATOM 641  C CA  . LEU A 1 80  ? -6.442  23.505  -47.751 1.00 59.71  ? 80  LEU A CA  1 
ATOM 642  C C   . LEU A 1 80  ? -7.451  22.369  -47.738 1.00 59.43  ? 80  LEU A C   1 
ATOM 643  O O   . LEU A 1 80  ? -7.837  21.890  -46.666 1.00 55.66  ? 80  LEU A O   1 
ATOM 644  C CB  . LEU A 1 80  ? -5.046  22.960  -47.435 1.00 55.64  ? 80  LEU A CB  1 
ATOM 645  C CG  . LEU A 1 80  ? -4.626  21.743  -48.266 1.00 54.46  ? 80  LEU A CG  1 
ATOM 646  C CD1 . LEU A 1 80  ? -4.017  22.155  -49.600 1.00 59.24  ? 80  LEU A CD1 1 
ATOM 647  C CD2 . LEU A 1 80  ? -3.677  20.856  -47.479 1.00 53.97  ? 80  LEU A CD2 1 
ATOM 648  N N   . ARG A 1 81  ? -7.868  21.933  -48.925 1.00 62.53  ? 81  ARG A N   1 
ATOM 649  C CA  . ARG A 1 81  ? -8.779  20.803  -49.077 1.00 63.12  ? 81  ARG A CA  1 
ATOM 650  C C   . ARG A 1 81  ? -8.080  19.700  -49.858 1.00 63.31  ? 81  ARG A C   1 
ATOM 651  O O   . ARG A 1 81  ? -7.660  19.919  -50.998 1.00 65.20  ? 81  ARG A O   1 
ATOM 652  C CB  . ARG A 1 81  ? -10.064 21.214  -49.800 1.00 64.57  ? 81  ARG A CB  1 
ATOM 653  C CG  . ARG A 1 81  ? -11.137 20.139  -49.795 1.00 67.78  ? 81  ARG A CG  1 
ATOM 654  C CD  . ARG A 1 81  ? -12.043 20.270  -51.004 1.00 70.93  ? 81  ARG A CD  1 
ATOM 655  N NE  . ARG A 1 81  ? -11.302 20.012  -52.234 1.00 74.57  ? 81  ARG A NE  1 
ATOM 656  C CZ  . ARG A 1 81  ? -11.834 20.007  -53.448 1.00 79.75  ? 81  ARG A CZ  1 
ATOM 657  N NH1 . ARG A 1 81  ? -13.119 20.253  -53.640 1.00 88.29  ? 81  ARG A NH1 1 
ATOM 658  N NH2 . ARG A 1 81  ? -11.058 19.747  -54.497 1.00 78.66  ? 81  ARG A NH2 1 
ATOM 659  N N   . LEU A 1 82  ? -7.969  18.518  -49.256 1.00 62.18  ? 82  LEU A N   1 
ATOM 660  C CA  . LEU A 1 82  ? -7.387  17.353  -49.914 1.00 62.35  ? 82  LEU A CA  1 
ATOM 661  C C   . LEU A 1 82  ? -8.473  16.296  -50.075 1.00 62.51  ? 82  LEU A C   1 
ATOM 662  O O   . LEU A 1 82  ? -9.044  15.830  -49.083 1.00 63.82  ? 82  LEU A O   1 
ATOM 663  C CB  . LEU A 1 82  ? -6.205  16.801  -49.119 1.00 57.23  ? 82  LEU A CB  1 
ATOM 664  C CG  . LEU A 1 82  ? -5.195  15.950  -49.896 1.00 54.62  ? 82  LEU A CG  1 
ATOM 665  C CD1 . LEU A 1 82  ? -4.673  16.709  -51.110 1.00 59.67  ? 82  LEU A CD1 1 
ATOM 666  C CD2 . LEU A 1 82  ? -4.048  15.511  -49.002 1.00 54.12  ? 82  LEU A CD2 1 
ATOM 667  N N   . THR A 1 83  ? -8.749  15.921  -51.318 1.00 62.10  ? 83  THR A N   1 
ATOM 668  C CA  . THR A 1 83  ? -9.838  15.020  -51.659 1.00 64.99  ? 83  THR A CA  1 
ATOM 669  C C   . THR A 1 83  ? -9.306  13.601  -51.853 1.00 68.10  ? 83  THR A C   1 
ATOM 670  O O   . THR A 1 83  ? -8.126  13.390  -52.145 1.00 64.64  ? 83  THR A O   1 
ATOM 671  C CB  . THR A 1 83  ? -10.552 15.522  -52.921 1.00 66.66  ? 83  THR A CB  1 
ATOM 672  O OG1 . THR A 1 83  ? -10.837 16.919  -52.772 1.00 68.08  ? 83  THR A OG1 1 
ATOM 673  C CG2 . THR A 1 83  ? -11.861 14.780  -53.159 1.00 72.22  ? 83  THR A CG2 1 
ATOM 674  N N   . SER A 1 84  ? -10.193 12.624  -51.654 1.00 68.86  ? 84  SER A N   1 
ATOM 675  C CA  . SER A 1 84  ? -9.867  11.207  -51.834 1.00 68.14  ? 84  SER A CA  1 
ATOM 676  C C   . SER A 1 84  ? -8.684  10.804  -50.958 1.00 70.63  ? 84  SER A C   1 
ATOM 677  O O   . SER A 1 84  ? -7.690  10.250  -51.433 1.00 73.53  ? 84  SER A O   1 
ATOM 678  C CB  . SER A 1 84  ? -9.594  10.888  -53.306 1.00 69.71  ? 84  SER A CB  1 
ATOM 679  O OG  . SER A 1 84  ? -10.712 11.215  -54.108 1.00 77.95  ? 84  SER A OG  1 
ATOM 680  N N   . VAL A 1 85  ? -8.804  11.093  -49.659 1.00 67.87  ? 85  VAL A N   1 
ATOM 681  C CA  . VAL A 1 85  ? -7.712  10.834  -48.731 1.00 61.66  ? 85  VAL A CA  1 
ATOM 682  C C   . VAL A 1 85  ? -7.370  9.353   -48.755 1.00 64.68  ? 85  VAL A C   1 
ATOM 683  O O   . VAL A 1 85  ? -8.249  8.484   -48.682 1.00 60.73  ? 85  VAL A O   1 
ATOM 684  C CB  . VAL A 1 85  ? -8.078  11.309  -47.316 1.00 57.24  ? 85  VAL A CB  1 
ATOM 685  C CG1 . VAL A 1 85  ? -8.168  12.829  -47.273 1.00 62.99  ? 85  VAL A CG1 1 
ATOM 686  C CG2 . VAL A 1 85  ? -9.375  10.667  -46.844 1.00 64.06  ? 85  VAL A CG2 1 
ATOM 687  N N   . THR A 1 86  ? -6.083  9.060   -48.888 1.00 64.49  ? 86  THR A N   1 
ATOM 688  C CA  . THR A 1 86  ? -5.560  7.706   -48.872 1.00 61.72  ? 86  THR A CA  1 
ATOM 689  C C   . THR A 1 86  ? -4.668  7.536   -47.649 1.00 62.72  ? 86  THR A C   1 
ATOM 690  O O   . THR A 1 86  ? -4.419  8.483   -46.898 1.00 59.66  ? 86  THR A O   1 
ATOM 691  C CB  . THR A 1 86  ? -4.786  7.403   -50.162 1.00 55.86  ? 86  THR A CB  1 
ATOM 692  O OG1 . THR A 1 86  ? -4.003  6.215   -49.992 1.00 61.17  ? 86  THR A OG1 1 
ATOM 693  C CG2 . THR A 1 86  ? -3.871  8.566   -50.513 1.00 56.27  ? 86  THR A CG2 1 
ATOM 694  N N   . ALA A 1 87  ? -4.183  6.308   -47.449 1.00 62.56  ? 87  ALA A N   1 
ATOM 695  C CA  . ALA A 1 87  ? -3.332  6.028   -46.300 1.00 58.95  ? 87  ALA A CA  1 
ATOM 696  C C   . ALA A 1 87  ? -2.039  6.826   -46.339 1.00 59.15  ? 87  ALA A C   1 
ATOM 697  O O   . ALA A 1 87  ? -1.387  6.982   -45.301 1.00 64.41  ? 87  ALA A O   1 
ATOM 698  C CB  . ALA A 1 87  ? -3.020  4.533   -46.228 1.00 60.16  ? 87  ALA A CB  1 
ATOM 699  N N   . ALA A 1 88  ? -1.651  7.322   -47.513 1.00 53.73  ? 88  ALA A N   1 
ATOM 700  C CA  . ALA A 1 88  ? -0.484  8.180   -47.640 1.00 55.56  ? 88  ALA A CA  1 
ATOM 701  C C   . ALA A 1 88  ? -0.781  9.627   -47.272 1.00 60.16  ? 88  ALA A C   1 
ATOM 702  O O   . ALA A 1 88  ? 0.158   10.416  -47.127 1.00 60.01  ? 88  ALA A O   1 
ATOM 703  C CB  . ALA A 1 88  ? 0.062   8.104   -49.067 1.00 57.63  ? 88  ALA A CB  1 
ATOM 704  N N   . ASP A 1 89  ? -2.053  9.991   -47.115 1.00 59.78  ? 89  ASP A N   1 
ATOM 705  C CA  . ASP A 1 89  ? -2.426  11.340  -46.715 1.00 56.08  ? 89  ASP A CA  1 
ATOM 706  C C   . ASP A 1 89  ? -2.481  11.515  -45.203 1.00 56.10  ? 89  ASP A C   1 
ATOM 707  O O   . ASP A 1 89  ? -2.526  12.656  -44.730 1.00 56.59  ? 89  ASP A O   1 
ATOM 708  C CB  . ASP A 1 89  ? -3.781  11.719  -47.326 1.00 55.58  ? 89  ASP A CB  1 
ATOM 709  C CG  . ASP A 1 89  ? -3.708  11.906  -48.830 1.00 57.75  ? 89  ASP A CG  1 
ATOM 710  O OD1 . ASP A 1 89  ? -2.585  12.033  -49.360 1.00 58.26  ? 89  ASP A OD1 1 
ATOM 711  O OD2 . ASP A 1 89  ? -4.773  11.930  -49.482 1.00 56.69  ? 89  ASP A OD2 1 
ATOM 712  N N   . MET A 1 90  ? -2.483  10.422  -44.440 1.00 57.35  ? 90  MET A N   1 
ATOM 713  C CA  . MET A 1 90  ? -2.376  10.511  -42.989 1.00 58.35  ? 90  MET A CA  1 
ATOM 714  C C   . MET A 1 90  ? -1.029  11.105  -42.604 1.00 54.98  ? 90  MET A C   1 
ATOM 715  O O   . MET A 1 90  ? 0.019   10.503  -42.862 1.00 58.09  ? 90  MET A O   1 
ATOM 716  C CB  . MET A 1 90  ? -2.539  9.129   -42.359 1.00 58.22  ? 90  MET A CB  1 
ATOM 717  C CG  . MET A 1 90  ? -2.351  9.122   -40.848 1.00 57.96  ? 90  MET A CG  1 
ATOM 718  S SD  . MET A 1 90  ? -2.672  7.524   -40.089 1.00 52.78  ? 90  MET A SD  1 
ATOM 719  C CE  . MET A 1 90  ? -1.437  6.520   -40.913 1.00 66.44  ? 90  MET A CE  1 
ATOM 720  N N   . ALA A 1 91  ? -1.056  12.281  -41.982 1.00 52.28  ? 91  ALA A N   1 
ATOM 721  C CA  . ALA A 1 91  ? 0.167   12.999  -41.645 1.00 51.99  ? 91  ALA A CA  1 
ATOM 722  C C   . ALA A 1 91  ? -0.170  14.118  -40.669 1.00 55.67  ? 91  ALA A C   1 
ATOM 723  O O   . ALA A 1 91  ? -1.339  14.405  -40.397 1.00 61.26  ? 91  ALA A O   1 
ATOM 724  C CB  . ALA A 1 91  ? 0.845   13.569  -42.894 1.00 51.99  ? 91  ALA A CB  1 
ATOM 725  N N   . THR A 1 92  ? 0.880   14.738  -40.136 1.00 51.68  ? 92  THR A N   1 
ATOM 726  C CA  . THR A 1 92  ? 0.759   15.999  -39.421 1.00 52.37  ? 92  THR A CA  1 
ATOM 727  C C   . THR A 1 92  ? 0.820   17.132  -40.435 1.00 54.48  ? 92  THR A C   1 
ATOM 728  O O   . THR A 1 92  ? 1.639   17.108  -41.357 1.00 52.75  ? 92  THR A O   1 
ATOM 729  C CB  . THR A 1 92  ? 1.875   16.161  -38.387 1.00 55.58  ? 92  THR A CB  1 
ATOM 730  O OG1 . THR A 1 92  ? 2.018   14.947  -37.639 1.00 51.33  ? 92  THR A OG1 1 
ATOM 731  C CG2 . THR A 1 92  ? 1.557   17.305  -37.429 1.00 59.43  ? 92  THR A CG2 1 
ATOM 732  N N   . TYR A 1 93  ? -0.057  18.114  -40.273 1.00 53.79  ? 93  TYR A N   1 
ATOM 733  C CA  . TYR A 1 93  ? -0.176  19.208  -41.225 1.00 52.23  ? 93  TYR A CA  1 
ATOM 734  C C   . TYR A 1 93  ? 0.097   20.533  -40.531 1.00 55.12  ? 93  TYR A C   1 
ATOM 735  O O   . TYR A 1 93  ? -0.390  20.778  -39.422 1.00 53.82  ? 93  TYR A O   1 
ATOM 736  C CB  . TYR A 1 93  ? -1.563  19.223  -41.867 1.00 52.42  ? 93  TYR A CB  1 
ATOM 737  C CG  . TYR A 1 93  ? -1.780  18.141  -42.902 1.00 52.54  ? 93  TYR A CG  1 
ATOM 738  C CD1 . TYR A 1 93  ? -2.117  16.848  -42.523 1.00 52.50  ? 93  TYR A CD1 1 
ATOM 739  C CD2 . TYR A 1 93  ? -1.657  18.416  -44.258 1.00 52.74  ? 93  TYR A CD2 1 
ATOM 740  C CE1 . TYR A 1 93  ? -2.320  15.855  -43.468 1.00 52.66  ? 93  TYR A CE1 1 
ATOM 741  C CE2 . TYR A 1 93  ? -1.859  17.433  -45.208 1.00 52.90  ? 93  TYR A CE2 1 
ATOM 742  C CZ  . TYR A 1 93  ? -2.190  16.155  -44.808 1.00 52.86  ? 93  TYR A CZ  1 
ATOM 743  O OH  . TYR A 1 93  ? -2.390  15.178  -45.757 1.00 53.06  ? 93  TYR A OH  1 
ATOM 744  N N   . TYR A 1 94  ? 0.880   21.383  -41.189 1.00 53.81  ? 94  TYR A N   1 
ATOM 745  C CA  . TYR A 1 94  ? 1.239   22.689  -40.664 1.00 55.41  ? 94  TYR A CA  1 
ATOM 746  C C   . TYR A 1 94  ? 0.838   23.752  -41.675 1.00 56.60  ? 94  TYR A C   1 
ATOM 747  O O   . TYR A 1 94  ? 0.807   23.498  -42.882 1.00 52.54  ? 94  TYR A O   1 
ATOM 748  C CB  . TYR A 1 94  ? 2.748   22.805  -40.404 1.00 54.43  ? 94  TYR A CB  1 
ATOM 749  C CG  . TYR A 1 94  ? 3.344   21.710  -39.551 1.00 51.87  ? 94  TYR A CG  1 
ATOM 750  C CD1 . TYR A 1 94  ? 3.075   21.628  -38.191 1.00 58.28  ? 94  TYR A CD1 1 
ATOM 751  C CD2 . TYR A 1 94  ? 4.202   20.770  -40.107 1.00 51.33  ? 94  TYR A CD2 1 
ATOM 752  C CE1 . TYR A 1 94  ? 3.633   20.630  -37.412 1.00 59.65  ? 94  TYR A CE1 1 
ATOM 753  C CE2 . TYR A 1 94  ? 4.765   19.769  -39.336 1.00 57.20  ? 94  TYR A CE2 1 
ATOM 754  C CZ  . TYR A 1 94  ? 4.476   19.705  -37.990 1.00 56.40  ? 94  TYR A CZ  1 
ATOM 755  O OH  . TYR A 1 94  ? 5.034   18.711  -37.218 1.00 57.00  ? 94  TYR A OH  1 
ATOM 756  N N   . CYS A 1 95  ? 0.534   24.946  -41.179 1.00 60.27  ? 95  CYS A N   1 
ATOM 757  C CA  . CYS A 1 95  ? 0.440   26.126  -42.026 1.00 56.01  ? 95  CYS A CA  1 
ATOM 758  C C   . CYS A 1 95  ? 1.598   27.051  -41.691 1.00 56.90  ? 95  CYS A C   1 
ATOM 759  O O   . CYS A 1 95  ? 1.957   27.210  -40.521 1.00 60.15  ? 95  CYS A O   1 
ATOM 760  C CB  . CYS A 1 95  ? -0.889  26.865  -41.854 1.00 57.56  ? 95  CYS A CB  1 
ATOM 761  S SG  . CYS A 1 95  ? -1.835  26.475  -40.376 1.00 73.70  ? 95  CYS A SG  1 
ATOM 762  N N   . ALA A 1 96  ? 2.189   27.647  -42.720 1.00 52.97  ? 96  ALA A N   1 
ATOM 763  C CA  . ALA A 1 96  ? 3.336   28.520  -42.543 1.00 52.91  ? 96  ALA A CA  1 
ATOM 764  C C   . ALA A 1 96  ? 3.105   29.833  -43.273 1.00 53.35  ? 96  ALA A C   1 
ATOM 765  O O   . ALA A 1 96  ? 2.313   29.919  -44.214 1.00 54.55  ? 96  ALA A O   1 
ATOM 766  C CB  . ALA A 1 96  ? 4.630   27.862  -43.040 1.00 52.57  ? 96  ALA A CB  1 
ATOM 767  N N   . ARG A 1 97  ? 3.809   30.860  -42.812 1.00 53.41  ? 97  ARG A N   1 
ATOM 768  C CA  . ARG A 1 97  ? 3.797   32.183  -43.417 1.00 53.85  ? 97  ARG A CA  1 
ATOM 769  C C   . ARG A 1 97  ? 5.159   32.426  -44.046 1.00 53.71  ? 97  ARG A C   1 
ATOM 770  O O   . ARG A 1 97  ? 6.171   32.468  -43.337 1.00 53.43  ? 97  ARG A O   1 
ATOM 771  C CB  . ARG A 1 97  ? 3.489   33.254  -42.370 1.00 55.92  ? 97  ARG A CB  1 
ATOM 772  C CG  . ARG A 1 97  ? 3.934   34.668  -42.726 1.00 59.01  ? 97  ARG A CG  1 
ATOM 773  C CD  . ARG A 1 97  ? 3.713   35.605  -41.545 1.00 61.12  ? 97  ARG A CD  1 
ATOM 774  N NE  . ARG A 1 97  ? 4.861   36.467  -41.288 1.00 62.39  ? 97  ARG A NE  1 
ATOM 775  C CZ  . ARG A 1 97  ? 4.906   37.382  -40.328 1.00 67.64  ? 97  ARG A CZ  1 
ATOM 776  N NH1 . ARG A 1 97  ? 3.884   37.577  -39.513 1.00 68.13  ? 97  ARG A NH1 1 
ATOM 777  N NH2 . ARG A 1 97  ? 6.005   38.117  -40.182 1.00 73.69  ? 97  ARG A NH2 1 
ATOM 778  N N   . TRP A 1 98  ? 5.190   32.569  -45.366 1.00 53.92  ? 98  TRP A N   1 
ATOM 779  C CA  . TRP A 1 98  ? 6.428   32.926  -46.037 1.00 53.84  ? 98  TRP A CA  1 
ATOM 780  C C   . TRP A 1 98  ? 6.760   34.392  -45.793 1.00 54.19  ? 98  TRP A C   1 
ATOM 781  O O   . TRP A 1 98  ? 5.877   35.225  -45.572 1.00 54.63  ? 98  TRP A O   1 
ATOM 782  C CB  . TRP A 1 98  ? 6.335   32.678  -47.540 1.00 54.01  ? 98  TRP A CB  1 
ATOM 783  C CG  . TRP A 1 98  ? 6.634   31.278  -47.957 1.00 53.61  ? 98  TRP A CG  1 
ATOM 784  C CD1 . TRP A 1 98  ? 5.735   30.292  -48.204 1.00 53.61  ? 98  TRP A CD1 1 
ATOM 785  C CD2 . TRP A 1 98  ? 7.929   30.705  -48.170 1.00 53.37  ? 98  TRP A CD2 1 
ATOM 786  N NE1 . TRP A 1 98  ? 6.383   29.136  -48.570 1.00 53.23  ? 98  TRP A NE1 1 
ATOM 787  C CE2 . TRP A 1 98  ? 7.734   29.364  -48.554 1.00 52.95  ? 98  TRP A CE2 1 
ATOM 788  C CE3 . TRP A 1 98  ? 9.233   31.196  -48.076 1.00 52.98  ? 98  TRP A CE3 1 
ATOM 789  C CZ2 . TRP A 1 98  ? 8.793   28.510  -48.845 1.00 53.27  ? 98  TRP A CZ2 1 
ATOM 790  C CZ3 . TRP A 1 98  ? 10.283  30.347  -48.362 1.00 52.54  ? 98  TRP A CZ3 1 
ATOM 791  C CH2 . TRP A 1 98  ? 10.057  29.018  -48.742 1.00 53.38  ? 98  TRP A CH2 1 
ATOM 792  N N   . ARG A 1 99  ? 8.052   34.699  -45.831 1.00 54.00  ? 99  ARG A N   1 
ATOM 793  C CA  . ARG A 1 99  ? 8.536   36.071  -45.801 1.00 54.35  ? 99  ARG A CA  1 
ATOM 794  C C   . ARG A 1 99  ? 9.284   36.311  -47.099 1.00 54.43  ? 99  ARG A C   1 
ATOM 795  O O   . ARG A 1 99  ? 10.208  35.564  -47.431 1.00 53.99  ? 99  ARG A O   1 
ATOM 796  C CB  . ARG A 1 99  ? 9.446   36.318  -44.597 1.00 54.10  ? 99  ARG A CB  1 
ATOM 797  C CG  . ARG A 1 99  ? 8.735   36.974  -43.431 1.00 59.92  ? 99  ARG A CG  1 
ATOM 798  C CD  . ARG A 1 99  ? 9.609   37.984  -42.716 1.00 66.39  ? 99  ARG A CD  1 
ATOM 799  N NE  . ARG A 1 99  ? 8.832   38.761  -41.758 1.00 67.68  ? 99  ARG A NE  1 
ATOM 800  C CZ  . ARG A 1 99  ? 9.322   39.725  -40.991 1.00 68.35  ? 99  ARG A CZ  1 
ATOM 801  N NH1 . ARG A 1 99  ? 10.597  40.075  -41.050 1.00 66.89  ? 99  ARG A NH1 1 
ATOM 802  N NH2 . ARG A 1 99  ? 8.513   40.350  -40.140 1.00 67.23  ? 99  ARG A NH2 1 
ATOM 803  N N   . LEU A 1 100 ? 8.873   37.327  -47.846 1.00 55.00  ? 100 LEU A N   1 
ATOM 804  C CA  . LEU A 1 100 ? 9.403   37.533  -49.183 1.00 55.16  ? 100 LEU A CA  1 
ATOM 805  C C   . LEU A 1 100 ? 9.877   38.970  -49.334 1.00 55.62  ? 100 LEU A C   1 
ATOM 806  O O   . LEU A 1 100 ? 9.331   39.887  -48.719 1.00 56.03  ? 100 LEU A O   1 
ATOM 807  C CB  . LEU A 1 100 ? 8.356   37.205  -50.254 1.00 55.49  ? 100 LEU A CB  1 
ATOM 808  C CG  . LEU A 1 100 ? 7.621   35.870  -50.084 1.00 55.17  ? 100 LEU A CG  1 
ATOM 809  C CD1 . LEU A 1 100 ? 6.305   36.061  -49.314 1.00 55.42  ? 100 LEU A CD1 1 
ATOM 810  C CD2 . LEU A 1 100 ? 7.404   35.177  -51.404 1.00 57.81  ? 100 LEU A CD2 1 
ATOM 811  N N   . MET A 1 101 ? 10.902  39.156  -50.158 1.00 55.56  ? 101 MET A N   1 
ATOM 812  C CA  . MET A 1 101 ? 11.459  40.473  -50.428 1.00 56.01  ? 101 MET A CA  1 
ATOM 813  C C   . MET A 1 101 ? 11.746  40.583  -51.916 1.00 56.24  ? 101 MET A C   1 
ATOM 814  O O   . MET A 1 101 ? 12.304  39.657  -52.515 1.00 56.03  ? 101 MET A O   1 
ATOM 815  C CB  . MET A 1 101 ? 12.722  40.712  -49.600 1.00 55.65  ? 101 MET A CB  1 
ATOM 816  C CG  . MET A 1 101 ? 13.316  42.097  -49.736 1.00 57.24  ? 101 MET A CG  1 
ATOM 817  S SD  . MET A 1 101 ? 14.145  42.533  -48.202 1.00 62.80  ? 101 MET A SD  1 
ATOM 818  C CE  . MET A 1 101 ? 12.758  42.477  -47.073 1.00 57.44  ? 101 MET A CE  1 
ATOM 819  N N   . MET A 1 102 ? 11.363  41.710  -52.508 1.00 60.79  ? 102 MET A N   1 
ATOM 820  C CA  . MET A 1 102 ? 11.406  41.883  -53.954 1.00 61.07  ? 102 MET A CA  1 
ATOM 821  C C   . MET A 1 102 ? 12.603  42.737  -54.348 1.00 61.13  ? 102 MET A C   1 
ATOM 822  O O   . MET A 1 102 ? 12.651  43.933  -54.047 1.00 61.36  ? 102 MET A O   1 
ATOM 823  C CB  . MET A 1 102 ? 10.116  42.506  -54.473 1.00 61.28  ? 102 MET A CB  1 
ATOM 824  C CG  . MET A 1 102 ? 10.160  42.684  -55.966 1.00 67.36  ? 102 MET A CG  1 
ATOM 825  S SD  . MET A 1 102 ? 9.165   41.472  -56.834 1.00 75.74  ? 102 MET A SD  1 
ATOM 826  C CE  . MET A 1 102 ? 9.829   41.679  -58.478 1.00 77.05  ? 102 MET A CE  1 
ATOM 827  N N   . VAL A 1 103 ? 13.566  42.117  -55.023 1.00 65.99  ? 103 VAL A N   1 
ATOM 828  C CA  . VAL A 1 103 ? 14.673  42.828  -55.648 1.00 71.12  ? 103 VAL A CA  1 
ATOM 829  C C   . VAL A 1 103 ? 14.796  42.326  -57.081 1.00 87.24  ? 103 VAL A C   1 
ATOM 830  O O   . VAL A 1 103 ? 15.668  41.506  -57.390 1.00 89.31  ? 103 VAL A O   1 
ATOM 831  C CB  . VAL A 1 103 ? 15.986  42.642  -54.861 1.00 63.57  ? 103 VAL A CB  1 
ATOM 832  C CG1 . VAL A 1 103 ? 17.030  43.639  -55.326 1.00 59.79  ? 103 VAL A CG1 1 
ATOM 833  C CG2 . VAL A 1 103 ? 15.743  42.814  -53.363 1.00 63.41  ? 103 VAL A CG2 1 
ATOM 834  N N   . ASP A 1 104 ? 13.894  42.797  -57.950 1.00 105.55 ? 104 ASP A N   1 
ATOM 835  C CA  . ASP A 1 104 ? 13.802  42.406  -59.357 1.00 105.51 ? 104 ASP A CA  1 
ATOM 836  C C   . ASP A 1 104 ? 13.308  40.974  -59.529 1.00 107.70 ? 104 ASP A C   1 
ATOM 837  O O   . ASP A 1 104 ? 13.040  40.531  -60.649 1.00 115.65 ? 104 ASP A O   1 
ATOM 838  C CB  . ASP A 1 104 ? 15.145  42.585  -60.064 1.00 106.84 ? 104 ASP A CB  1 
ATOM 839  C CG  . ASP A 1 104 ? 15.018  43.360  -61.351 1.00 121.22 ? 104 ASP A CG  1 
ATOM 840  O OD1 . ASP A 1 104 ? 13.939  43.951  -61.576 1.00 121.09 ? 104 ASP A OD1 1 
ATOM 841  O OD2 . ASP A 1 104 ? 15.995  43.387  -62.124 1.00 127.23 ? 104 ASP A OD2 1 
ATOM 842  N N   . GLU A 1 105 ? 13.199  40.243  -58.426 1.00 90.80  ? 105 GLU A N   1 
ATOM 843  C CA  . GLU A 1 105 ? 12.617  38.912  -58.414 1.00 75.06  ? 105 GLU A CA  1 
ATOM 844  C C   . GLU A 1 105 ? 12.145  38.653  -56.996 1.00 70.98  ? 105 GLU A C   1 
ATOM 845  O O   . GLU A 1 105 ? 12.790  39.089  -56.038 1.00 76.48  ? 105 GLU A O   1 
ATOM 846  C CB  . GLU A 1 105 ? 13.631  37.849  -58.855 1.00 75.07  ? 105 GLU A CB  1 
ATOM 847  C CG  . GLU A 1 105 ? 13.080  36.420  -58.823 1.00 83.71  ? 105 GLU A CG  1 
ATOM 848  C CD  . GLU A 1 105 ? 14.109  35.409  -58.364 1.00 87.73  ? 105 GLU A CD  1 
ATOM 849  O OE1 . GLU A 1 105 ? 15.317  35.703  -58.454 1.00 91.71  ? 105 GLU A OE1 1 
ATOM 850  O OE2 . GLU A 1 105 ? 13.709  34.312  -57.923 1.00 84.25  ? 105 GLU A OE2 1 
ATOM 851  N N   . VAL A 1 106 ? 11.013  37.970  -56.862 1.00 57.68  ? 106 VAL A N   1 
ATOM 852  C CA  . VAL A 1 106 ? 10.523  37.663  -55.524 1.00 56.18  ? 106 VAL A CA  1 
ATOM 853  C C   . VAL A 1 106 ? 11.470  36.652  -54.888 1.00 58.28  ? 106 VAL A C   1 
ATOM 854  O O   . VAL A 1 106 ? 11.421  35.458  -55.197 1.00 65.78  ? 106 VAL A O   1 
ATOM 855  C CB  . VAL A 1 106 ? 9.088   37.139  -55.546 1.00 56.41  ? 106 VAL A CB  1 
ATOM 856  C CG1 . VAL A 1 106 ? 8.595   36.993  -54.129 1.00 56.16  ? 106 VAL A CG1 1 
ATOM 857  C CG2 . VAL A 1 106 ? 8.188   38.078  -56.321 1.00 57.25  ? 106 VAL A CG2 1 
ATOM 858  N N   . THR A 1 107 ? 12.354  37.138  -54.025 1.00 55.10  ? 107 THR A N   1 
ATOM 859  C CA  . THR A 1 107 ? 13.194  36.279  -53.210 1.00 54.38  ? 107 THR A CA  1 
ATOM 860  C C   . THR A 1 107 ? 12.465  35.917  -51.926 1.00 54.22  ? 107 THR A C   1 
ATOM 861  O O   . THR A 1 107 ? 11.649  36.688  -51.415 1.00 54.63  ? 107 THR A O   1 
ATOM 862  C CB  . THR A 1 107 ? 14.522  36.957  -52.879 1.00 54.18  ? 107 THR A CB  1 
ATOM 863  O OG1 . THR A 1 107 ? 14.273  38.139  -52.108 1.00 61.93  ? 107 THR A OG1 1 
ATOM 864  C CG2 . THR A 1 107 ? 15.264  37.323  -54.151 1.00 54.33  ? 107 THR A CG2 1 
ATOM 865  N N   . ARG A 1 108 ? 12.770  34.734  -51.405 1.00 53.64  ? 108 ARG A N   1 
ATOM 866  C CA  . ARG A 1 108 ? 12.076  34.182  -50.251 1.00 53.47  ? 108 ARG A CA  1 
ATOM 867  C C   . ARG A 1 108 ? 13.010  34.178  -49.048 1.00 53.05  ? 108 ARG A C   1 
ATOM 868  O O   . ARG A 1 108 ? 14.120  33.638  -49.118 1.00 52.60  ? 108 ARG A O   1 
ATOM 869  C CB  . ARG A 1 108 ? 11.570  32.768  -50.550 1.00 53.21  ? 108 ARG A CB  1 
ATOM 870  C CG  . ARG A 1 108 ? 11.272  32.528  -52.024 1.00 53.47  ? 108 ARG A CG  1 
ATOM 871  C CD  . ARG A 1 108 ? 10.726  31.132  -52.278 1.00 59.40  ? 108 ARG A CD  1 
ATOM 872  N NE  . ARG A 1 108 ? 9.353   30.988  -51.808 1.00 59.19  ? 108 ARG A NE  1 
ATOM 873  C CZ  . ARG A 1 108 ? 8.287   31.049  -52.594 1.00 57.39  ? 108 ARG A CZ  1 
ATOM 874  N NH1 . ARG A 1 108 ? 8.402   31.246  -53.898 1.00 54.97  ? 108 ARG A NH1 1 
ATOM 875  N NH2 . ARG A 1 108 ? 7.077   30.911  -52.060 1.00 55.32  ? 108 ARG A NH2 1 
ATOM 876  N N   . HIS A 1 109 ? 12.556  34.782  -47.949 1.00 53.22  ? 109 HIS A N   1 
ATOM 877  C CA  . HIS A 1 109 ? 13.347  34.912  -46.733 1.00 52.94  ? 109 HIS A CA  1 
ATOM 878  C C   . HIS A 1 109 ? 12.923  33.931  -45.647 1.00 52.62  ? 109 HIS A C   1 
ATOM 879  O O   . HIS A 1 109 ? 13.142  34.197  -44.461 1.00 52.56  ? 109 HIS A O   1 
ATOM 880  C CB  . HIS A 1 109 ? 13.270  36.344  -46.203 1.00 53.39  ? 109 HIS A CB  1 
ATOM 881  C CG  . HIS A 1 109 ? 14.206  37.291  -46.886 1.00 53.58  ? 109 HIS A CG  1 
ATOM 882  N ND1 . HIS A 1 109 ? 14.944  36.939  -47.997 1.00 53.38  ? 109 HIS A ND1 1 
ATOM 883  C CD2 . HIS A 1 109 ? 14.519  38.581  -46.620 1.00 53.97  ? 109 HIS A CD2 1 
ATOM 884  C CE1 . HIS A 1 109 ? 15.673  37.970  -48.383 1.00 53.62  ? 109 HIS A CE1 1 
ATOM 885  N NE2 . HIS A 1 109 ? 15.433  38.979  -47.565 1.00 53.99  ? 109 HIS A NE2 1 
ATOM 886  N N   . GLY A 1 110 ? 12.315  32.814  -46.022 1.00 52.46  ? 110 GLY A N   1 
ATOM 887  C CA  . GLY A 1 110 ? 12.019  31.763  -45.074 1.00 52.14  ? 110 GLY A CA  1 
ATOM 888  C C   . GLY A 1 110 ? 10.622  31.859  -44.486 1.00 52.43  ? 110 GLY A C   1 
ATOM 889  O O   . GLY A 1 110 ? 9.955   32.892  -44.536 1.00 52.87  ? 110 GLY A O   1 
ATOM 890  N N   . MET A 1 111 ? 10.183  30.739  -43.918 1.00 52.17  ? 111 MET A N   1 
ATOM 891  C CA  . MET A 1 111 ? 8.876   30.635  -43.274 1.00 53.81  ? 111 MET A CA  1 
ATOM 892  C C   . MET A 1 111 ? 9.073   30.959  -41.800 1.00 57.28  ? 111 MET A C   1 
ATOM 893  O O   . MET A 1 111 ? 9.429   30.100  -40.994 1.00 56.10  ? 111 MET A O   1 
ATOM 894  C CB  . MET A 1 111 ? 8.292   29.245  -43.478 1.00 52.24  ? 111 MET A CB  1 
ATOM 895  C CG  . MET A 1 111 ? 8.446   28.719  -44.894 1.00 52.58  ? 111 MET A CG  1 
ATOM 896  S SD  . MET A 1 111 ? 7.467   27.235  -45.156 1.00 52.08  ? 111 MET A SD  1 
ATOM 897  C CE  . MET A 1 111 ? 8.557   26.258  -46.189 1.00 51.77  ? 111 MET A CE  1 
ATOM 898  N N   . ASP A 1 112 ? 8.843   32.223  -41.444 1.00 67.79  ? 112 ASP A N   1 
ATOM 899  C CA  . ASP A 1 112 ? 9.181   32.678  -40.100 1.00 67.67  ? 112 ASP A CA  1 
ATOM 900  C C   . ASP A 1 112 ? 8.232   32.103  -39.054 1.00 67.83  ? 112 ASP A C   1 
ATOM 901  O O   . ASP A 1 112 ? 8.663   31.751  -37.950 1.00 73.74  ? 112 ASP A O   1 
ATOM 902  C CB  . ASP A 1 112 ? 9.180   34.204  -40.046 1.00 68.29  ? 112 ASP A CB  1 
ATOM 903  C CG  . ASP A 1 112 ? 7.878   34.805  -40.535 1.00 69.32  ? 112 ASP A CG  1 
ATOM 904  O OD1 . ASP A 1 112 ? 6.999   34.041  -40.986 1.00 69.60  ? 112 ASP A OD1 1 
ATOM 905  O OD2 . ASP A 1 112 ? 7.729   36.041  -40.456 1.00 69.85  ? 112 ASP A OD2 1 
ATOM 906  N N   . VAL A 1 113 ? 6.943   32.001  -39.371 1.00 58.74  ? 113 VAL A N   1 
ATOM 907  C CA  . VAL A 1 113 ? 5.939   31.527  -38.425 1.00 56.87  ? 113 VAL A CA  1 
ATOM 908  C C   . VAL A 1 113 ? 5.351   30.221  -38.944 1.00 53.85  ? 113 VAL A C   1 
ATOM 909  O O   . VAL A 1 113 ? 4.996   30.119  -40.125 1.00 57.52  ? 113 VAL A O   1 
ATOM 910  C CB  . VAL A 1 113 ? 4.832   32.573  -38.195 1.00 56.63  ? 113 VAL A CB  1 
ATOM 911  C CG1 . VAL A 1 113 ? 3.702   31.978  -37.367 1.00 61.06  ? 113 VAL A CG1 1 
ATOM 912  C CG2 . VAL A 1 113 ? 5.398   33.806  -37.513 1.00 59.48  ? 113 VAL A CG2 1 
ATOM 913  N N   . TRP A 1 114 ? 5.256   29.229  -38.062 1.00 52.40  ? 114 TRP A N   1 
ATOM 914  C CA  . TRP A 1 114 ? 4.621   27.948  -38.332 1.00 52.23  ? 114 TRP A CA  1 
ATOM 915  C C   . TRP A 1 114 ? 3.436   27.777  -37.387 1.00 55.14  ? 114 TRP A C   1 
ATOM 916  O O   . TRP A 1 114 ? 3.204   28.591  -36.490 1.00 59.12  ? 114 TRP A O   1 
ATOM 917  C CB  . TRP A 1 114 ? 5.623   26.793  -38.174 1.00 51.83  ? 114 TRP A CB  1 
ATOM 918  C CG  . TRP A 1 114 ? 6.645   26.730  -39.282 1.00 51.69  ? 114 TRP A CG  1 
ATOM 919  C CD1 . TRP A 1 114 ? 7.651   27.626  -39.514 1.00 51.69  ? 114 TRP A CD1 1 
ATOM 920  C CD2 . TRP A 1 114 ? 6.772   25.718  -40.294 1.00 51.53  ? 114 TRP A CD2 1 
ATOM 921  N NE1 . TRP A 1 114 ? 8.385   27.243  -40.610 1.00 51.53  ? 114 TRP A NE1 1 
ATOM 922  C CE2 . TRP A 1 114 ? 7.869   26.075  -41.106 1.00 51.43  ? 114 TRP A CE2 1 
ATOM 923  C CE3 . TRP A 1 114 ? 6.064   24.549  -40.593 1.00 51.49  ? 114 TRP A CE3 1 
ATOM 924  C CZ2 . TRP A 1 114 ? 8.273   25.307  -42.196 1.00 51.29  ? 114 TRP A CZ2 1 
ATOM 925  C CZ3 . TRP A 1 114 ? 6.469   23.788  -41.677 1.00 51.37  ? 114 TRP A CZ3 1 
ATOM 926  C CH2 . TRP A 1 114 ? 7.563   24.170  -42.464 1.00 51.27  ? 114 TRP A CH2 1 
ATOM 927  N N   . SER A 1 115 ? 2.676   26.708  -37.592 1.00 59.95  ? 115 SER A N   1 
ATOM 928  C CA  . SER A 1 115 ? 1.480   26.457  -36.802 1.00 64.17  ? 115 SER A CA  1 
ATOM 929  C C   . SER A 1 115 ? 1.726   25.370  -35.761 1.00 67.95  ? 115 SER A C   1 
ATOM 930  O O   . SER A 1 115 ? 2.772   24.718  -35.729 1.00 65.78  ? 115 SER A O   1 
ATOM 931  C CB  . SER A 1 115 ? 0.308   26.065  -37.705 1.00 65.98  ? 115 SER A CB  1 
ATOM 932  O OG  . SER A 1 115 ? -0.908  26.039  -36.977 1.00 70.46  ? 115 SER A OG  1 
ATOM 933  N N   . GLN A 1 116 ? 0.725   25.185  -34.898 1.00 84.68  ? 116 GLN A N   1 
ATOM 934  C CA  . GLN A 1 116 ? 0.804   24.167  -33.857 1.00 83.45  ? 116 GLN A CA  1 
ATOM 935  C C   . GLN A 1 116 ? 0.958   22.775  -34.452 1.00 85.96  ? 116 GLN A C   1 
ATOM 936  O O   . GLN A 1 116 ? 1.770   21.971  -33.979 1.00 89.63  ? 116 GLN A O   1 
ATOM 937  C CB  . GLN A 1 116 ? -0.447  24.233  -32.983 1.00 85.02  ? 116 GLN A CB  1 
ATOM 938  C CG  . GLN A 1 116 ? -1.730  24.409  -33.794 1.00 91.49  ? 116 GLN A CG  1 
ATOM 939  C CD  . GLN A 1 116 ? -2.985  24.326  -32.951 1.00 102.23 ? 116 GLN A CD  1 
ATOM 940  O OE1 . GLN A 1 116 ? -3.164  23.391  -32.173 1.00 108.27 ? 116 GLN A OE1 1 
ATOM 941  N NE2 . GLN A 1 116 ? -3.864  25.311  -33.103 1.00 91.47  ? 116 GLN A NE2 1 
ATOM 942  N N   . GLY A 1 117 ? 0.195   22.478  -35.486 1.00 75.87  ? 117 GLY A N   1 
ATOM 943  C CA  . GLY A 1 117 ? 0.173   21.167  -36.101 1.00 67.82  ? 117 GLY A CA  1 
ATOM 944  C C   . GLY A 1 117 ? -1.171  20.516  -35.830 1.00 67.98  ? 117 GLY A C   1 
ATOM 945  O O   . GLY A 1 117 ? -1.759  20.671  -34.751 1.00 67.96  ? 117 GLY A O   1 
ATOM 946  N N   . THR A 1 118 ? -1.675  19.790  -36.826 1.00 59.95  ? 118 THR A N   1 
ATOM 947  C CA  . THR A 1 118 ? -2.943  19.076  -36.704 1.00 55.87  ? 118 THR A CA  1 
ATOM 948  C C   . THR A 1 118 ? -2.755  17.688  -37.292 1.00 65.54  ? 118 THR A C   1 
ATOM 949  O O   . THR A 1 118 ? -2.620  17.541  -38.511 1.00 65.20  ? 118 THR A O   1 
ATOM 950  C CB  . THR A 1 118 ? -4.078  19.823  -37.406 1.00 54.15  ? 118 THR A CB  1 
ATOM 951  O OG1 . THR A 1 118 ? -4.326  21.067  -36.735 1.00 61.53  ? 118 THR A OG1 1 
ATOM 952  C CG2 . THR A 1 118 ? -5.341  18.983  -37.421 1.00 56.98  ? 118 THR A CG2 1 
ATOM 953  N N   . MET A 1 119 ? -2.753  16.675  -36.431 1.00 69.34  ? 119 MET A N   1 
ATOM 954  C CA  . MET A 1 119 ? -2.644  15.303  -36.900 1.00 61.81  ? 119 MET A CA  1 
ATOM 955  C C   . MET A 1 119 ? -3.924  14.893  -37.616 1.00 60.21  ? 119 MET A C   1 
ATOM 956  O O   . MET A 1 119 ? -5.026  15.070  -37.089 1.00 61.40  ? 119 MET A O   1 
ATOM 957  C CB  . MET A 1 119 ? -2.362  14.361  -35.732 1.00 63.62  ? 119 MET A CB  1 
ATOM 958  C CG  . MET A 1 119 ? -0.939  14.428  -35.208 1.00 64.70  ? 119 MET A CG  1 
ATOM 959  S SD  . MET A 1 119 ? -0.771  13.628  -33.601 1.00 80.37  ? 119 MET A SD  1 
ATOM 960  C CE  . MET A 1 119 ? 1.010   13.500  -33.470 1.00 62.45  ? 119 MET A CE  1 
ATOM 961  N N   . VAL A 1 120 ? -3.778  14.350  -38.822 1.00 59.29  ? 120 VAL A N   1 
ATOM 962  C CA  . VAL A 1 120 ? -4.905  13.908  -39.635 1.00 58.52  ? 120 VAL A CA  1 
ATOM 963  C C   . VAL A 1 120 ? -4.754  12.412  -39.862 1.00 58.35  ? 120 VAL A C   1 
ATOM 964  O O   . VAL A 1 120 ? -3.797  11.972  -40.513 1.00 52.63  ? 120 VAL A O   1 
ATOM 965  C CB  . VAL A 1 120 ? -4.976  14.652  -40.977 1.00 54.52  ? 120 VAL A CB  1 
ATOM 966  C CG1 . VAL A 1 120 ? -5.933  13.938  -41.925 1.00 60.19  ? 120 VAL A CG1 1 
ATOM 967  C CG2 . VAL A 1 120 ? -5.381  16.100  -40.769 1.00 52.96  ? 120 VAL A CG2 1 
ATOM 968  N N   . THR A 1 121 ? -5.699  11.635  -39.342 1.00 65.81  ? 121 THR A N   1 
ATOM 969  C CA  . THR A 1 121 ? -5.651  10.180  -39.408 1.00 70.66  ? 121 THR A CA  1 
ATOM 970  C C   . THR A 1 121 ? -6.652  9.670   -40.435 1.00 68.82  ? 121 THR A C   1 
ATOM 971  O O   . THR A 1 121 ? -7.823  10.064  -40.419 1.00 68.60  ? 121 THR A O   1 
ATOM 972  C CB  . THR A 1 121 ? -5.939  9.563   -38.036 1.00 66.27  ? 121 THR A CB  1 
ATOM 973  O OG1 . THR A 1 121 ? -5.211  10.274  -37.027 1.00 67.31  ? 121 THR A OG1 1 
ATOM 974  C CG2 . THR A 1 121 ? -5.540  8.097   -38.011 1.00 65.83  ? 121 THR A CG2 1 
ATOM 975  N N   . VAL A 1 122 ? -6.188  8.798   -41.324 1.00 65.74  ? 122 VAL A N   1 
ATOM 976  C CA  . VAL A 1 122 ? -7.036  8.162   -42.324 1.00 65.73  ? 122 VAL A CA  1 
ATOM 977  C C   . VAL A 1 122 ? -7.308  6.741   -41.852 1.00 63.22  ? 122 VAL A C   1 
ATOM 978  O O   . VAL A 1 122 ? -6.413  5.889   -41.869 1.00 58.58  ? 122 VAL A O   1 
ATOM 979  C CB  . VAL A 1 122 ? -6.387  8.176   -43.714 1.00 60.40  ? 122 VAL A CB  1 
ATOM 980  C CG1 . VAL A 1 122 ? -7.367  7.655   -44.752 1.00 57.87  ? 122 VAL A CG1 1 
ATOM 981  C CG2 . VAL A 1 122 ? -5.924  9.579   -44.064 1.00 60.74  ? 122 VAL A CG2 1 
ATOM 982  N N   . SER A 1 123 ? -8.542  6.484   -41.428 1.00 61.90  ? 123 SER A N   1 
ATOM 983  C CA  . SER A 1 123 ? -8.908  5.178   -40.898 1.00 59.23  ? 123 SER A CA  1 
ATOM 984  C C   . SER A 1 123 ? -10.423 5.055   -40.873 1.00 58.85  ? 123 SER A C   1 
ATOM 985  O O   . SER A 1 123 ? -11.147 6.053   -40.851 1.00 58.09  ? 123 SER A O   1 
ATOM 986  C CB  . SER A 1 123 ? -8.334  4.962   -39.494 1.00 63.10  ? 123 SER A CB  1 
ATOM 987  O OG  . SER A 1 123 ? -8.851  3.776   -38.918 1.00 61.40  ? 123 SER A OG  1 
ATOM 988  N N   . SER A 1 124 ? -10.890 3.809   -40.868 1.00 61.22  ? 124 SER A N   1 
ATOM 989  C CA  . SER A 1 124 ? -12.313 3.511   -40.776 1.00 61.58  ? 124 SER A CA  1 
ATOM 990  C C   . SER A 1 124 ? -12.771 3.284   -39.343 1.00 61.60  ? 124 SER A C   1 
ATOM 991  O O   . SER A 1 124 ? -13.960 3.031   -39.120 1.00 60.43  ? 124 SER A O   1 
ATOM 992  C CB  . SER A 1 124 ? -12.657 2.280   -41.623 1.00 56.43  ? 124 SER A CB  1 
ATOM 993  O OG  . SER A 1 124 ? -11.950 1.132   -41.183 1.00 61.10  ? 124 SER A OG  1 
ATOM 994  N N   . ALA A 1 125 ? -11.864 3.368   -38.375 1.00 60.11  ? 125 ALA A N   1 
ATOM 995  C CA  . ALA A 1 125 ? -12.216 3.113   -36.989 1.00 60.03  ? 125 ALA A CA  1 
ATOM 996  C C   . ALA A 1 125 ? -13.060 4.250   -36.426 1.00 62.35  ? 125 ALA A C   1 
ATOM 997  O O   . ALA A 1 125 ? -12.900 5.418   -36.791 1.00 70.87  ? 125 ALA A O   1 
ATOM 998  C CB  . ALA A 1 125 ? -10.955 2.928   -36.145 1.00 63.39  ? 125 ALA A CB  1 
ATOM 999  N N   . SER A 1 126 ? -13.972 3.892   -35.528 1.00 62.85  ? 126 SER A N   1 
ATOM 1000 C CA  . SER A 1 126 ? -14.819 4.873   -34.871 1.00 67.04  ? 126 SER A CA  1 
ATOM 1001 C C   . SER A 1 126 ? -14.072 5.536   -33.721 1.00 70.58  ? 126 SER A C   1 
ATOM 1002 O O   . SER A 1 126 ? -13.140 4.968   -33.144 1.00 71.06  ? 126 SER A O   1 
ATOM 1003 C CB  . SER A 1 126 ? -16.099 4.218   -34.353 1.00 71.04  ? 126 SER A CB  1 
ATOM 1004 O OG  . SER A 1 126 ? -16.989 5.186   -33.825 1.00 75.33  ? 126 SER A OG  1 
ATOM 1005 N N   . THR A 1 127 ? -14.494 6.754   -33.391 1.00 79.83  ? 127 THR A N   1 
ATOM 1006 C CA  . THR A 1 127 ? -13.863 7.498   -32.311 1.00 75.94  ? 127 THR A CA  1 
ATOM 1007 C C   . THR A 1 127 ? -14.193 6.856   -30.970 1.00 72.23  ? 127 THR A C   1 
ATOM 1008 O O   . THR A 1 127 ? -15.361 6.602   -30.661 1.00 73.64  ? 127 THR A O   1 
ATOM 1009 C CB  . THR A 1 127 ? -14.327 8.953   -32.332 1.00 73.55  ? 127 THR A CB  1 
ATOM 1010 O OG1 . THR A 1 127 ? -13.790 9.610   -33.487 1.00 76.89  ? 127 THR A OG1 1 
ATOM 1011 C CG2 . THR A 1 127 ? -13.857 9.679   -31.083 1.00 70.68  ? 127 THR A CG2 1 
ATOM 1012 N N   . LYS A 1 128 ? -13.160 6.588   -30.175 1.00 68.79  ? 128 LYS A N   1 
ATOM 1013 C CA  . LYS A 1 128 ? -13.310 5.952   -28.874 1.00 69.51  ? 128 LYS A CA  1 
ATOM 1014 C C   . LYS A 1 128 ? -12.691 6.836   -27.802 1.00 68.57  ? 128 LYS A C   1 
ATOM 1015 O O   . LYS A 1 128 ? -11.566 7.321   -27.965 1.00 65.35  ? 128 LYS A O   1 
ATOM 1016 C CB  . LYS A 1 128 ? -12.661 4.567   -28.864 1.00 69.53  ? 128 LYS A CB  1 
ATOM 1017 C CG  . LYS A 1 128 ? -13.282 3.592   -29.849 1.00 78.18  ? 128 LYS A CG  1 
ATOM 1018 C CD  . LYS A 1 128 ? -14.663 3.161   -29.385 1.00 84.03  ? 128 LYS A CD  1 
ATOM 1019 C CE  . LYS A 1 128 ? -15.261 2.123   -30.318 1.00 78.86  ? 128 LYS A CE  1 
ATOM 1020 N NZ  . LYS A 1 128 ? -16.610 1.687   -29.867 1.00 76.83  ? 128 LYS A NZ  1 
ATOM 1021 N N   . GLY A 1 129 ? -13.425 7.041   -26.712 1.00 66.99  ? 129 GLY A N   1 
ATOM 1022 C CA  . GLY A 1 129 ? -12.958 7.864   -25.624 1.00 71.09  ? 129 GLY A CA  1 
ATOM 1023 C C   . GLY A 1 129 ? -11.942 7.152   -24.754 1.00 76.58  ? 129 GLY A C   1 
ATOM 1024 O O   . GLY A 1 129 ? -12.005 5.933   -24.555 1.00 78.91  ? 129 GLY A O   1 
ATOM 1025 N N   . PRO A 1 130 ? -10.992 7.905   -24.209 1.00 76.53  ? 130 PRO A N   1 
ATOM 1026 C CA  . PRO A 1 130 ? -9.937  7.298   -23.394 1.00 76.10  ? 130 PRO A CA  1 
ATOM 1027 C C   . PRO A 1 130 ? -10.408 6.942   -21.991 1.00 89.01  ? 130 PRO A C   1 
ATOM 1028 O O   . PRO A 1 130 ? -11.361 7.507   -21.454 1.00 87.94  ? 130 PRO A O   1 
ATOM 1029 C CB  . PRO A 1 130 ? -8.866  8.390   -23.349 1.00 73.26  ? 130 PRO A CB  1 
ATOM 1030 C CG  . PRO A 1 130 ? -9.648  9.652   -23.439 1.00 80.97  ? 130 PRO A CG  1 
ATOM 1031 C CD  . PRO A 1 130 ? -10.796 9.357   -24.371 1.00 80.61  ? 130 PRO A CD  1 
ATOM 1032 N N   . SER A 1 131 ? -9.707  5.975   -21.403 1.00 105.47 ? 131 SER A N   1 
ATOM 1033 C CA  . SER A 1 131 ? -9.881  5.599   -20.008 1.00 104.53 ? 131 SER A CA  1 
ATOM 1034 C C   . SER A 1 131 ? -8.663  6.068   -19.226 1.00 104.42 ? 131 SER A C   1 
ATOM 1035 O O   . SER A 1 131 ? -7.526  5.747   -19.588 1.00 104.03 ? 131 SER A O   1 
ATOM 1036 C CB  . SER A 1 131 ? -10.071 4.089   -19.861 1.00 104.28 ? 131 SER A CB  1 
ATOM 1037 O OG  . SER A 1 131 ? -11.334 3.690   -20.363 1.00 107.66 ? 131 SER A OG  1 
ATOM 1038 N N   . VAL A 1 132 ? -8.902  6.838   -18.170 1.00 94.16  ? 132 VAL A N   1 
ATOM 1039 C CA  . VAL A 1 132 ? -7.843  7.469   -17.391 1.00 87.57  ? 132 VAL A CA  1 
ATOM 1040 C C   . VAL A 1 132 ? -7.710  6.724   -16.069 1.00 84.03  ? 132 VAL A C   1 
ATOM 1041 O O   . VAL A 1 132 ? -8.684  6.594   -15.316 1.00 83.44  ? 132 VAL A O   1 
ATOM 1042 C CB  . VAL A 1 132 ? -8.118  8.966   -17.180 1.00 86.92  ? 132 VAL A CB  1 
ATOM 1043 C CG1 . VAL A 1 132 ? -9.557  9.191   -16.748 1.00 91.06  ? 132 VAL A CG1 1 
ATOM 1044 C CG2 . VAL A 1 132 ? -7.166  9.537   -16.154 1.00 87.58  ? 132 VAL A CG2 1 
ATOM 1045 N N   . PHE A 1 133 ? -6.505  6.225   -15.795 1.00 79.96  ? 133 PHE A N   1 
ATOM 1046 C CA  . PHE A 1 133 ? -6.219  5.448   -14.602 1.00 78.55  ? 133 PHE A CA  1 
ATOM 1047 C C   . PHE A 1 133 ? -5.033  6.052   -13.863 1.00 79.59  ? 133 PHE A C   1 
ATOM 1048 O O   . PHE A 1 133 ? -4.042  6.443   -14.492 1.00 80.85  ? 133 PHE A O   1 
ATOM 1049 C CB  . PHE A 1 133 ? -5.918  3.988   -14.961 1.00 75.18  ? 133 PHE A CB  1 
ATOM 1050 C CG  . PHE A 1 133 ? -7.074  3.272   -15.597 1.00 77.40  ? 133 PHE A CG  1 
ATOM 1051 C CD1 . PHE A 1 133 ? -8.272  3.117   -14.916 1.00 79.12  ? 133 PHE A CD1 1 
ATOM 1052 C CD2 . PHE A 1 133 ? -6.970  2.767   -16.882 1.00 79.04  ? 133 PHE A CD2 1 
ATOM 1053 C CE1 . PHE A 1 133 ? -9.339  2.461   -15.503 1.00 81.42  ? 133 PHE A CE1 1 
ATOM 1054 C CE2 . PHE A 1 133 ? -8.033  2.112   -17.474 1.00 81.10  ? 133 PHE A CE2 1 
ATOM 1055 C CZ  . PHE A 1 133 ? -9.219  1.959   -16.784 1.00 82.00  ? 133 PHE A CZ  1 
ATOM 1056 N N   . PRO A 1 134 ? -5.100  6.141   -12.533 1.00 80.17  ? 134 PRO A N   1 
ATOM 1057 C CA  . PRO A 1 134 ? -4.016  6.790   -11.785 1.00 78.59  ? 134 PRO A CA  1 
ATOM 1058 C C   . PRO A 1 134 ? -2.865  5.854   -11.450 1.00 76.23  ? 134 PRO A C   1 
ATOM 1059 O O   . PRO A 1 134 ? -3.066  4.791   -10.854 1.00 78.59  ? 134 PRO A O   1 
ATOM 1060 C CB  . PRO A 1 134 ? -4.722  7.278   -10.515 1.00 78.81  ? 134 PRO A CB  1 
ATOM 1061 C CG  . PRO A 1 134 ? -5.818  6.280   -10.301 1.00 78.65  ? 134 PRO A CG  1 
ATOM 1062 C CD  . PRO A 1 134 ? -6.215  5.739   -11.659 1.00 79.37  ? 134 PRO A CD  1 
ATOM 1063 N N   . LEU A 1 135 ? -1.652  6.245   -11.832 1.00 76.18  ? 135 LEU A N   1 
ATOM 1064 C CA  . LEU A 1 135 ? -0.437  5.567   -11.392 1.00 79.44  ? 135 LEU A CA  1 
ATOM 1065 C C   . LEU A 1 135 ? 0.016   6.241   -10.101 1.00 82.22  ? 135 LEU A C   1 
ATOM 1066 O O   . LEU A 1 135 ? 0.420   7.408   -10.110 1.00 82.55  ? 135 LEU A O   1 
ATOM 1067 C CB  . LEU A 1 135 ? 0.641   5.628   -12.472 1.00 78.20  ? 135 LEU A CB  1 
ATOM 1068 C CG  . LEU A 1 135 ? 0.184   5.284   -13.893 1.00 77.16  ? 135 LEU A CG  1 
ATOM 1069 C CD1 . LEU A 1 135 ? 1.332   5.404   -14.890 1.00 74.91  ? 135 LEU A CD1 1 
ATOM 1070 C CD2 . LEU A 1 135 ? -0.434  3.893   -13.942 1.00 78.61  ? 135 LEU A CD2 1 
ATOM 1071 N N   . ALA A 1 136 ? -0.058  5.504   -8.986  1.00 82.78  ? 136 ALA A N   1 
ATOM 1072 C CA  . ALA A 1 136 ? 0.035   6.138   -7.682  1.00 84.93  ? 136 ALA A CA  1 
ATOM 1073 C C   . ALA A 1 136 ? 1.426   5.981   -7.079  1.00 91.55  ? 136 ALA A C   1 
ATOM 1074 O O   . ALA A 1 136 ? 2.136   5.014   -7.371  1.00 95.78  ? 136 ALA A O   1 
ATOM 1075 C CB  . ALA A 1 136 ? -1.000  5.541   -6.725  1.00 84.17  ? 136 ALA A CB  1 
ATOM 1076 N N   . PRO A 1 137 ? 1.835   6.926   -6.233  1.00 93.34  ? 137 PRO A N   1 
ATOM 1077 C CA  . PRO A 1 137 ? 3.108   6.778   -5.524  1.00 96.68  ? 137 PRO A CA  1 
ATOM 1078 C C   . PRO A 1 137 ? 3.034   5.690   -4.465  1.00 106.50 ? 137 PRO A C   1 
ATOM 1079 O O   . PRO A 1 137 ? 1.990   5.443   -3.857  1.00 104.23 ? 137 PRO A O   1 
ATOM 1080 C CB  . PRO A 1 137 ? 3.324   8.158   -4.886  1.00 94.70  ? 137 PRO A CB  1 
ATOM 1081 C CG  . PRO A 1 137 ? 2.375   9.075   -5.614  1.00 91.94  ? 137 PRO A CG  1 
ATOM 1082 C CD  . PRO A 1 137 ? 1.199   8.216   -5.927  1.00 91.00  ? 137 PRO A CD  1 
ATOM 1083 N N   . SER A 1 138 ? 4.172   5.037   -4.250  1.00 119.09 ? 138 SER A N   1 
ATOM 1084 C CA  . SER A 1 138 ? 4.288   3.969   -3.269  1.00 120.76 ? 138 SER A CA  1 
ATOM 1085 C C   . SER A 1 138 ? 5.747   3.871   -2.852  1.00 124.92 ? 138 SER A C   1 
ATOM 1086 O O   . SER A 1 138 ? 6.600   4.617   -3.340  1.00 126.10 ? 138 SER A O   1 
ATOM 1087 C CB  . SER A 1 138 ? 3.779   2.640   -3.833  1.00 123.09 ? 138 SER A CB  1 
ATOM 1088 O OG  . SER A 1 138 ? 3.760   1.638   -2.833  1.00 127.89 ? 138 SER A OG  1 
ATOM 1089 N N   . SER A 1 139 ? 6.033   2.943   -1.935  1.00 119.38 ? 139 SER A N   1 
ATOM 1090 C CA  . SER A 1 139 ? 7.424   2.645   -1.617  1.00 113.75 ? 139 SER A CA  1 
ATOM 1091 C C   . SER A 1 139 ? 8.182   2.250   -2.874  1.00 111.17 ? 139 SER A C   1 
ATOM 1092 O O   . SER A 1 139 ? 9.358   2.595   -3.039  1.00 108.92 ? 139 SER A O   1 
ATOM 1093 C CB  . SER A 1 139 ? 7.502   1.531   -0.572  1.00 109.90 ? 139 SER A CB  1 
ATOM 1094 O OG  . SER A 1 139 ? 6.498   1.687   0.414   1.00 115.41 ? 139 SER A OG  1 
ATOM 1095 N N   . LYS A 1 140 ? 7.509   1.548   -3.785  1.00 118.68 ? 140 LYS A N   1 
ATOM 1096 C CA  . LYS A 1 140 ? 8.138   1.165   -5.041  1.00 111.24 ? 140 LYS A CA  1 
ATOM 1097 C C   . LYS A 1 140 ? 8.302   2.369   -5.958  1.00 112.99 ? 140 LYS A C   1 
ATOM 1098 O O   . LYS A 1 140 ? 9.291   2.467   -6.693  1.00 104.63 ? 140 LYS A O   1 
ATOM 1099 C CB  . LYS A 1 140 ? 7.309   0.078   -5.721  1.00 100.26 ? 140 LYS A CB  1 
ATOM 1100 C CG  . LYS A 1 140 ? 7.177   -1.184  -4.890  1.00 91.79  ? 140 LYS A CG  1 
ATOM 1101 C CD  . LYS A 1 140 ? 8.536   -1.755  -4.532  1.00 87.49  ? 140 LYS A CD  1 
ATOM 1102 C CE  . LYS A 1 140 ? 8.475   -2.527  -3.219  1.00 84.82  ? 140 LYS A CE  1 
ATOM 1103 N NZ  . LYS A 1 140 ? 7.404   -3.563  -3.221  1.00 85.56  ? 140 LYS A NZ  1 
ATOM 1104 N N   . SER A 1 141 ? 7.343   3.298   -5.928  1.00 129.30 ? 141 SER A N   1 
ATOM 1105 C CA  . SER A 1 141 ? 7.434   4.472   -6.790  1.00 128.53 ? 141 SER A CA  1 
ATOM 1106 C C   . SER A 1 141 ? 8.435   5.484   -6.246  1.00 128.67 ? 141 SER A C   1 
ATOM 1107 O O   . SER A 1 141 ? 9.119   6.166   -7.018  1.00 128.14 ? 141 SER A O   1 
ATOM 1108 C CB  . SER A 1 141 ? 6.058   5.113   -6.951  1.00 128.20 ? 141 SER A CB  1 
ATOM 1109 O OG  . SER A 1 141 ? 5.067   4.131   -7.191  1.00 129.09 ? 141 SER A OG  1 
ATOM 1110 N N   . THR A 1 142 ? 8.535   5.600   -4.927  1.00 119.60 ? 142 THR A N   1 
ATOM 1111 C CA  . THR A 1 142 ? 9.448   6.560   -4.327  1.00 108.33 ? 142 THR A CA  1 
ATOM 1112 C C   . THR A 1 142 ? 10.889  6.069   -4.408  1.00 101.01 ? 142 THR A C   1 
ATOM 1113 O O   . THR A 1 142 ? 11.168  4.868   -4.354  1.00 101.31 ? 142 THR A O   1 
ATOM 1114 C CB  . THR A 1 142 ? 9.070   6.830   -2.870  1.00 105.56 ? 142 THR A CB  1 
ATOM 1115 O OG1 . THR A 1 142 ? 9.036   5.594   -2.143  1.00 115.96 ? 142 THR A OG1 1 
ATOM 1116 C CG2 . THR A 1 142 ? 7.712   7.514   -2.786  1.00 100.85 ? 142 THR A CG2 1 
ATOM 1117 N N   . SER A 1 143 ? 11.810  7.023   -4.547  1.00 96.48  ? 143 SER A N   1 
ATOM 1118 C CA  . SER A 1 143 ? 13.242  6.723   -4.594  1.00 97.29  ? 143 SER A CA  1 
ATOM 1119 C C   . SER A 1 143 ? 13.969  7.877   -3.900  1.00 97.52  ? 143 SER A C   1 
ATOM 1120 O O   . SER A 1 143 ? 14.378  8.846   -4.544  1.00 99.75  ? 143 SER A O   1 
ATOM 1121 C CB  . SER A 1 143 ? 13.729  6.528   -6.022  1.00 95.26  ? 143 SER A CB  1 
ATOM 1122 O OG  . SER A 1 143 ? 15.127  6.303   -6.050  1.00 95.46  ? 143 SER A OG  1 
ATOM 1123 N N   . GLY A 1 144 ? 14.125  7.753   -2.587  1.00 93.21  ? 144 GLY A N   1 
ATOM 1124 C CA  . GLY A 1 144 ? 14.764  8.817   -1.829  1.00 90.27  ? 144 GLY A CA  1 
ATOM 1125 C C   . GLY A 1 144 ? 13.869  10.039  -1.779  1.00 92.56  ? 144 GLY A C   1 
ATOM 1126 O O   . GLY A 1 144 ? 12.685  9.956   -1.432  1.00 93.28  ? 144 GLY A O   1 
ATOM 1127 N N   . GLY A 1 145 ? 14.436  11.193  -2.131  1.00 93.06  ? 145 GLY A N   1 
ATOM 1128 C CA  . GLY A 1 145 ? 13.642  12.409  -2.164  1.00 91.82  ? 145 GLY A CA  1 
ATOM 1129 C C   . GLY A 1 145 ? 12.663  12.434  -3.322  1.00 99.84  ? 145 GLY A C   1 
ATOM 1130 O O   . GLY A 1 145 ? 11.556  12.963  -3.199  1.00 102.32 ? 145 GLY A O   1 
ATOM 1131 N N   . THR A 1 146 ? 13.051  11.856  -4.456  1.00 102.72 ? 146 THR A N   1 
ATOM 1132 C CA  . THR A 1 146 ? 12.197  11.851  -5.635  1.00 103.98 ? 146 THR A CA  1 
ATOM 1133 C C   . THR A 1 146 ? 11.105  10.798  -5.499  1.00 102.91 ? 146 THR A C   1 
ATOM 1134 O O   . THR A 1 146 ? 11.378  9.644   -5.151  1.00 105.35 ? 146 THR A O   1 
ATOM 1135 C CB  . THR A 1 146 ? 13.022  11.587  -6.894  1.00 109.80 ? 146 THR A CB  1 
ATOM 1136 O OG1 . THR A 1 146 ? 13.603  10.279  -6.821  1.00 110.65 ? 146 THR A OG1 1 
ATOM 1137 C CG2 . THR A 1 146 ? 14.129  12.619  -7.028  1.00 104.05 ? 146 THR A CG2 1 
ATOM 1138 N N   . ALA A 1 147 ? 9.868   11.202  -5.775  1.00 95.73  ? 147 ALA A N   1 
ATOM 1139 C CA  . ALA A 1 147 ? 8.723   10.307  -5.811  1.00 95.18  ? 147 ALA A CA  1 
ATOM 1140 C C   . ALA A 1 147 ? 8.046   10.421  -7.168  1.00 96.33  ? 147 ALA A C   1 
ATOM 1141 O O   . ALA A 1 147 ? 7.945   11.516  -7.731  1.00 95.84  ? 147 ALA A O   1 
ATOM 1142 C CB  . ALA A 1 147 ? 7.724   10.630  -4.698  1.00 90.66  ? 147 ALA A CB  1 
ATOM 1143 N N   . ALA A 1 148 ? 7.585   9.286   -7.687  1.00 99.29  ? 148 ALA A N   1 
ATOM 1144 C CA  . ALA A 1 148 ? 6.984   9.215   -9.008  1.00 87.55  ? 148 ALA A CA  1 
ATOM 1145 C C   . ALA A 1 148 ? 5.520   8.811   -8.905  1.00 86.50  ? 148 ALA A C   1 
ATOM 1146 O O   . ALA A 1 148 ? 5.163   7.885   -8.169  1.00 94.40  ? 148 ALA A O   1 
ATOM 1147 C CB  . ALA A 1 148 ? 7.742   8.234   -9.911  1.00 88.76  ? 148 ALA A CB  1 
ATOM 1148 N N   . LEU A 1 149 ? 4.688   9.548   -9.633  1.00 79.42  ? 149 LEU A N   1 
ATOM 1149 C CA  . LEU A 1 149 ? 3.279   9.266   -9.866  1.00 79.24  ? 149 LEU A CA  1 
ATOM 1150 C C   . LEU A 1 149 ? 2.959   9.439   -11.345 1.00 77.29  ? 149 LEU A C   1 
ATOM 1151 O O   . LEU A 1 149 ? 3.800   9.867   -12.139 1.00 78.24  ? 149 LEU A O   1 
ATOM 1152 C CB  . LEU A 1 149 ? 2.361   10.134  -8.984  1.00 82.37  ? 149 LEU A CB  1 
ATOM 1153 C CG  . LEU A 1 149 ? 2.269   11.638  -9.262  1.00 84.04  ? 149 LEU A CG  1 
ATOM 1154 C CD1 . LEU A 1 149 ? 1.191   12.296  -8.474  1.00 82.98  ? 149 LEU A CD1 1 
ATOM 1155 C CD2 . LEU A 1 149 ? 3.559   12.246  -8.654  1.00 83.75  ? 149 LEU A CD2 1 
ATOM 1156 N N   . GLY A 1 150 ? 1.736   9.082   -11.725 1.00 76.91  ? 150 GLY A N   1 
ATOM 1157 C CA  . GLY A 1 150 ? 1.430   9.077   -13.144 1.00 77.71  ? 150 GLY A CA  1 
ATOM 1158 C C   . GLY A 1 150 ? -0.053  9.025   -13.430 1.00 80.14  ? 150 GLY A C   1 
ATOM 1159 O O   . GLY A 1 150 ? -0.884  8.810   -12.543 1.00 80.67  ? 150 GLY A O   1 
ATOM 1160 N N   . CYS A 1 151 ? -0.361  9.229   -14.708 1.00 79.18  ? 151 CYS A N   1 
ATOM 1161 C CA  . CYS A 1 151 ? -1.709  9.175   -15.253 1.00 75.70  ? 151 CYS A CA  1 
ATOM 1162 C C   . CYS A 1 151 ? -1.655  8.347   -16.526 1.00 75.18  ? 151 CYS A C   1 
ATOM 1163 O O   . CYS A 1 151 ? -0.841  8.628   -17.411 1.00 73.94  ? 151 CYS A O   1 
ATOM 1164 C CB  . CYS A 1 151 ? -2.238  10.585  -15.547 1.00 85.09  ? 151 CYS A CB  1 
ATOM 1165 S SG  . CYS A 1 151 ? -4.024  10.802  -15.377 1.00 102.01 ? 151 CYS A SG  1 
ATOM 1166 N N   . LEU A 1 152 ? -2.509  7.330   -16.619 1.00 78.21  ? 152 LEU A N   1 
ATOM 1167 C CA  . LEU A 1 152 ? -2.490  6.392   -17.736 1.00 75.63  ? 152 LEU A CA  1 
ATOM 1168 C C   . LEU A 1 152 ? -3.710  6.625   -18.619 1.00 76.31  ? 152 LEU A C   1 
ATOM 1169 O O   . LEU A 1 152 ? -4.850  6.472   -18.167 1.00 79.72  ? 152 LEU A O   1 
ATOM 1170 C CB  . LEU A 1 152 ? -2.452  4.948   -17.237 1.00 71.58  ? 152 LEU A CB  1 
ATOM 1171 C CG  . LEU A 1 152 ? -2.234  3.864   -18.295 1.00 70.20  ? 152 LEU A CG  1 
ATOM 1172 C CD1 . LEU A 1 152 ? -0.756  3.757   -18.659 1.00 70.52  ? 152 LEU A CD1 1 
ATOM 1173 C CD2 . LEU A 1 152 ? -2.772  2.530   -17.812 1.00 69.12  ? 152 LEU A CD2 1 
ATOM 1174 N N   . VAL A 1 153 ? -3.463  6.987   -19.874 1.00 74.84  ? 153 VAL A N   1 
ATOM 1175 C CA  . VAL A 1 153 ? -4.516  7.214   -20.862 1.00 75.58  ? 153 VAL A CA  1 
ATOM 1176 C C   . VAL A 1 153 ? -4.588  5.927   -21.679 1.00 79.61  ? 153 VAL A C   1 
ATOM 1177 O O   . VAL A 1 153 ? -3.862  5.743   -22.658 1.00 76.92  ? 153 VAL A O   1 
ATOM 1178 C CB  . VAL A 1 153 ? -4.228  8.444   -21.721 1.00 72.15  ? 153 VAL A CB  1 
ATOM 1179 C CG1 . VAL A 1 153 ? -5.478  8.905   -22.451 1.00 78.41  ? 153 VAL A CG1 1 
ATOM 1180 C CG2 . VAL A 1 153 ? -3.641  9.563   -20.861 1.00 70.62  ? 153 VAL A CG2 1 
ATOM 1181 N N   . LYS A 1 154 ? -5.487  5.024   -21.271 1.00 76.30  ? 154 LYS A N   1 
ATOM 1182 C CA  . LYS A 1 154 ? -5.401  3.624   -21.685 1.00 77.15  ? 154 LYS A CA  1 
ATOM 1183 C C   . LYS A 1 154 ? -5.810  3.387   -23.134 1.00 80.01  ? 154 LYS A C   1 
ATOM 1184 O O   . LYS A 1 154 ? -5.028  2.840   -23.914 1.00 83.02  ? 154 LYS A O   1 
ATOM 1185 C CB  . LYS A 1 154 ? -6.215  2.739   -20.745 1.00 82.54  ? 154 LYS A CB  1 
ATOM 1186 C CG  . LYS A 1 154 ? -5.859  1.274   -20.942 1.00 86.28  ? 154 LYS A CG  1 
ATOM 1187 C CD  . LYS A 1 154 ? -4.376  1.026   -20.792 1.00 85.45  ? 154 LYS A CD  1 
ATOM 1188 C CE  . LYS A 1 154 ? -4.003  -0.306  -21.419 1.00 81.52  ? 154 LYS A CE  1 
ATOM 1189 N NZ  . LYS A 1 154 ? -2.559  -0.353  -21.777 1.00 82.57  ? 154 LYS A NZ  1 
ATOM 1190 N N   . ASP A 1 155 ? -7.048  3.706   -23.498 1.00 74.71  ? 155 ASP A N   1 
ATOM 1191 C CA  . ASP A 1 155 ? -7.622  3.219   -24.749 1.00 71.05  ? 155 ASP A CA  1 
ATOM 1192 C C   . ASP A 1 155 ? -8.316  4.362   -25.476 1.00 71.92  ? 155 ASP A C   1 
ATOM 1193 O O   . ASP A 1 155 ? -9.419  4.760   -25.089 1.00 77.67  ? 155 ASP A O   1 
ATOM 1194 C CB  . ASP A 1 155 ? -8.606  2.078   -24.476 1.00 71.98  ? 155 ASP A CB  1 
ATOM 1195 C CG  . ASP A 1 155 ? -7.923  0.726   -24.384 1.00 76.39  ? 155 ASP A CG  1 
ATOM 1196 O OD1 . ASP A 1 155 ? -6.873  0.546   -25.038 1.00 76.02  ? 155 ASP A OD1 1 
ATOM 1197 O OD2 . ASP A 1 155 ? -8.420  -0.144  -23.638 1.00 72.42  ? 155 ASP A OD2 1 
ATOM 1198 N N   . TYR A 1 156 ? -7.702  4.867   -26.548 1.00 67.36  ? 156 TYR A N   1 
ATOM 1199 C CA  . TYR A 1 156 ? -8.287  5.993   -27.267 1.00 65.33  ? 156 TYR A CA  1 
ATOM 1200 C C   . TYR A 1 156 ? -7.946  5.951   -28.751 1.00 61.15  ? 156 TYR A C   1 
ATOM 1201 O O   . TYR A 1 156 ? -6.883  5.472   -29.155 1.00 59.81  ? 156 TYR A O   1 
ATOM 1202 C CB  . TYR A 1 156 ? -7.844  7.333   -26.663 1.00 63.86  ? 156 TYR A CB  1 
ATOM 1203 C CG  . TYR A 1 156 ? -6.385  7.685   -26.865 1.00 58.73  ? 156 TYR A CG  1 
ATOM 1204 C CD1 . TYR A 1 156 ? -5.953  8.330   -28.017 1.00 61.92  ? 156 TYR A CD1 1 
ATOM 1205 C CD2 . TYR A 1 156 ? -5.450  7.422   -25.874 1.00 61.94  ? 156 TYR A CD2 1 
ATOM 1206 C CE1 . TYR A 1 156 ? -4.626  8.658   -28.197 1.00 62.48  ? 156 TYR A CE1 1 
ATOM 1207 C CE2 . TYR A 1 156 ? -4.120  7.758   -26.039 1.00 64.42  ? 156 TYR A CE2 1 
ATOM 1208 C CZ  . TYR A 1 156 ? -3.716  8.379   -27.201 1.00 61.83  ? 156 TYR A CZ  1 
ATOM 1209 O OH  . TYR A 1 156 ? -2.397  8.718   -27.371 1.00 65.83  ? 156 TYR A OH  1 
ATOM 1210 N N   . PHE A 1 157 ? -8.876  6.478   -29.552 1.00 62.24  ? 157 PHE A N   1 
ATOM 1211 C CA  . PHE A 1 157 ? -8.763  6.720   -30.988 1.00 64.03  ? 157 PHE A CA  1 
ATOM 1212 C C   . PHE A 1 157 ? -9.554  7.983   -31.306 1.00 65.62  ? 157 PHE A C   1 
ATOM 1213 O O   . PHE A 1 157 ? -10.645 8.179   -30.749 1.00 71.45  ? 157 PHE A O   1 
ATOM 1214 C CB  . PHE A 1 157 ? -9.313  5.553   -31.823 1.00 59.84  ? 157 PHE A CB  1 
ATOM 1215 C CG  . PHE A 1 157 ? -8.725  5.457   -33.207 1.00 57.59  ? 157 PHE A CG  1 
ATOM 1216 C CD1 . PHE A 1 157 ? -7.440  4.981   -33.413 1.00 58.22  ? 157 PHE A CD1 1 
ATOM 1217 C CD2 . PHE A 1 157 ? -9.461  5.877   -34.304 1.00 58.98  ? 157 PHE A CD2 1 
ATOM 1218 C CE1 . PHE A 1 157 ? -6.911  4.902   -34.695 1.00 58.70  ? 157 PHE A CE1 1 
ATOM 1219 C CE2 . PHE A 1 157 ? -8.938  5.808   -35.582 1.00 58.71  ? 157 PHE A CE2 1 
ATOM 1220 C CZ  . PHE A 1 157 ? -7.663  5.320   -35.779 1.00 58.23  ? 157 PHE A CZ  1 
ATOM 1221 N N   . PRO A 1 158 ? -9.041  8.865   -32.183 1.00 62.23  ? 158 PRO A N   1 
ATOM 1222 C CA  . PRO A 1 158 ? -7.692  8.872   -32.766 1.00 60.89  ? 158 PRO A CA  1 
ATOM 1223 C C   . PRO A 1 158 ? -6.639  9.486   -31.832 1.00 61.18  ? 158 PRO A C   1 
ATOM 1224 O O   . PRO A 1 158 ? -6.890  9.597   -30.637 1.00 60.72  ? 158 PRO A O   1 
ATOM 1225 C CB  . PRO A 1 158 ? -7.861  9.722   -34.033 1.00 64.00  ? 158 PRO A CB  1 
ATOM 1226 C CG  . PRO A 1 158 ? -9.028  10.603  -33.730 1.00 72.77  ? 158 PRO A CG  1 
ATOM 1227 C CD  . PRO A 1 158 ? -9.959  9.733   -32.943 1.00 65.51  ? 158 PRO A CD  1 
ATOM 1228 N N   . GLU A 1 159 ? -5.495  9.904   -32.380 1.00 70.15  ? 159 GLU A N   1 
ATOM 1229 C CA  . GLU A 1 159 ? -4.274  10.179  -31.619 1.00 74.35  ? 159 GLU A CA  1 
ATOM 1230 C C   . GLU A 1 159 ? -4.294  11.358  -30.638 1.00 78.76  ? 159 GLU A C   1 
ATOM 1231 O O   . GLU A 1 159 ? -3.760  11.218  -29.531 1.00 81.33  ? 159 GLU A O   1 
ATOM 1232 C CB  . GLU A 1 159 ? -3.100  10.373  -32.582 1.00 75.86  ? 159 GLU A CB  1 
ATOM 1233 C CG  . GLU A 1 159 ? -1.792  10.719  -31.886 1.00 72.85  ? 159 GLU A CG  1 
ATOM 1234 C CD  . GLU A 1 159 ? -1.160  9.514   -31.223 1.00 71.97  ? 159 GLU A CD  1 
ATOM 1235 O OE1 . GLU A 1 159 ? -1.689  9.057   -30.186 1.00 70.55  ? 159 GLU A OE1 1 
ATOM 1236 O OE2 . GLU A 1 159 ? -0.144  9.018   -31.747 1.00 75.87  ? 159 GLU A OE2 1 
ATOM 1237 N N   . PRO A 1 160 ? -4.835  12.530  -30.985 1.00 72.26  ? 160 PRO A N   1 
ATOM 1238 C CA  . PRO A 1 160 ? -4.665  13.706  -30.108 1.00 65.46  ? 160 PRO A CA  1 
ATOM 1239 C C   . PRO A 1 160 ? -5.157  13.483  -28.683 1.00 65.58  ? 160 PRO A C   1 
ATOM 1240 O O   . PRO A 1 160 ? -6.356  13.317  -28.435 1.00 71.19  ? 160 PRO A O   1 
ATOM 1241 C CB  . PRO A 1 160 ? -5.489  14.790  -30.813 1.00 68.97  ? 160 PRO A CB  1 
ATOM 1242 C CG  . PRO A 1 160 ? -5.463  14.405  -32.226 1.00 73.99  ? 160 PRO A CG  1 
ATOM 1243 C CD  . PRO A 1 160 ? -5.510  12.905  -32.240 1.00 67.32  ? 160 PRO A CD  1 
ATOM 1244 N N   . VAL A 1 161 ? -4.212  13.497  -27.738 1.00 60.78  ? 161 VAL A N   1 
ATOM 1245 C CA  . VAL A 1 161 ? -4.494  13.547  -26.303 1.00 65.59  ? 161 VAL A CA  1 
ATOM 1246 C C   . VAL A 1 161 ? -3.536  14.533  -25.654 1.00 68.50  ? 161 VAL A C   1 
ATOM 1247 O O   . VAL A 1 161 ? -2.321  14.455  -25.861 1.00 69.95  ? 161 VAL A O   1 
ATOM 1248 C CB  . VAL A 1 161 ? -4.376  12.172  -25.619 1.00 62.92  ? 161 VAL A CB  1 
ATOM 1249 C CG1 . VAL A 1 161 ? -4.685  12.302  -24.142 1.00 61.51  ? 161 VAL A CG1 1 
ATOM 1250 C CG2 . VAL A 1 161 ? -5.360  11.219  -26.219 1.00 67.15  ? 161 VAL A CG2 1 
ATOM 1251 N N   . THR A 1 162 ? -4.084  15.443  -24.853 1.00 68.88  ? 162 THR A N   1 
ATOM 1252 C CA  . THR A 1 162 ? -3.323  16.472  -24.161 1.00 67.10  ? 162 THR A CA  1 
ATOM 1253 C C   . THR A 1 162 ? -3.458  16.270  -22.659 1.00 74.69  ? 162 THR A C   1 
ATOM 1254 O O   . THR A 1 162 ? -4.577  16.180  -22.143 1.00 77.50  ? 162 THR A O   1 
ATOM 1255 C CB  . THR A 1 162 ? -3.820  17.864  -24.553 1.00 70.92  ? 162 THR A CB  1 
ATOM 1256 O OG1 . THR A 1 162 ? -5.248  17.834  -24.678 1.00 73.27  ? 162 THR A OG1 1 
ATOM 1257 C CG2 . THR A 1 162 ? -3.215  18.289  -25.879 1.00 66.58  ? 162 THR A CG2 1 
ATOM 1258 N N   . VAL A 1 163 ? -2.325  16.202  -21.960 1.00 78.40  ? 163 VAL A N   1 
ATOM 1259 C CA  . VAL A 1 163 ? -2.297  15.954  -20.522 1.00 82.75  ? 163 VAL A CA  1 
ATOM 1260 C C   . VAL A 1 163 ? -1.559  17.093  -19.834 1.00 87.59  ? 163 VAL A C   1 
ATOM 1261 O O   . VAL A 1 163 ? -0.415  17.403  -20.188 1.00 84.29  ? 163 VAL A O   1 
ATOM 1262 C CB  . VAL A 1 163 ? -1.640  14.602  -20.187 1.00 77.24  ? 163 VAL A CB  1 
ATOM 1263 C CG1 . VAL A 1 163 ? -1.869  14.254  -18.725 1.00 86.00  ? 163 VAL A CG1 1 
ATOM 1264 C CG2 . VAL A 1 163 ? -2.186  13.505  -21.085 1.00 75.64  ? 163 VAL A CG2 1 
ATOM 1265 N N   . SER A 1 164 ? -2.211  17.707  -18.850 1.00 98.88  ? 164 SER A N   1 
ATOM 1266 C CA  . SER A 1 164 ? -1.605  18.722  -18.003 1.00 101.30 ? 164 SER A CA  1 
ATOM 1267 C C   . SER A 1 164 ? -1.782  18.327  -16.543 1.00 103.72 ? 164 SER A C   1 
ATOM 1268 O O   . SER A 1 164 ? -2.720  17.606  -16.190 1.00 102.10 ? 164 SER A O   1 
ATOM 1269 C CB  . SER A 1 164 ? -2.221  20.107  -18.252 1.00 103.02 ? 164 SER A CB  1 
ATOM 1270 O OG  . SER A 1 164 ? -3.603  20.123  -17.938 1.00 104.07 ? 164 SER A OG  1 
ATOM 1271 N N   . TRP A 1 165 ? -0.873  18.799  -15.696 1.00 96.85  ? 165 TRP A N   1 
ATOM 1272 C CA  . TRP A 1 165 ? -0.879  18.464  -14.278 1.00 91.62  ? 165 TRP A CA  1 
ATOM 1273 C C   . TRP A 1 165 ? -1.197  19.696  -13.446 1.00 92.43  ? 165 TRP A C   1 
ATOM 1274 O O   . TRP A 1 165 ? -0.628  20.770  -13.675 1.00 93.79  ? 165 TRP A O   1 
ATOM 1275 C CB  . TRP A 1 165 ? 0.459   17.864  -13.852 1.00 86.09  ? 165 TRP A CB  1 
ATOM 1276 C CG  . TRP A 1 165 ? 0.673   16.489  -14.385 1.00 88.78  ? 165 TRP A CG  1 
ATOM 1277 C CD1 . TRP A 1 165 ? 1.137   16.149  -15.620 1.00 88.21  ? 165 TRP A CD1 1 
ATOM 1278 C CD2 . TRP A 1 165 ? 0.402   15.259  -13.705 1.00 92.59  ? 165 TRP A CD2 1 
ATOM 1279 N NE1 . TRP A 1 165 ? 1.187   14.781  -15.747 1.00 90.49  ? 165 TRP A NE1 1 
ATOM 1280 C CE2 . TRP A 1 165 ? 0.739   14.212  -14.584 1.00 88.53  ? 165 TRP A CE2 1 
ATOM 1281 C CE3 . TRP A 1 165 ? -0.088  14.942  -12.435 1.00 93.86  ? 165 TRP A CE3 1 
ATOM 1282 C CZ2 . TRP A 1 165 ? 0.603   12.873  -14.236 1.00 85.97  ? 165 TRP A CZ2 1 
ATOM 1283 C CZ3 . TRP A 1 165 ? -0.222  13.613  -12.090 1.00 94.86  ? 165 TRP A CZ3 1 
ATOM 1284 C CH2 . TRP A 1 165 ? 0.122   12.594  -12.987 1.00 90.46  ? 165 TRP A CH2 1 
ATOM 1285 N N   . ASN A 1 166 ? -2.105  19.529  -12.484 1.00 84.57  ? 166 ASN A N   1 
ATOM 1286 C CA  . ASN A 1 166 ? -2.536  20.610  -11.598 1.00 82.96  ? 166 ASN A CA  1 
ATOM 1287 C C   . ASN A 1 166 ? -3.050  21.805  -12.398 1.00 82.60  ? 166 ASN A C   1 
ATOM 1288 O O   . ASN A 1 166 ? -2.808  22.962  -12.048 1.00 78.41  ? 166 ASN A O   1 
ATOM 1289 C CB  . ASN A 1 166 ? -1.411  21.022  -10.647 1.00 84.03  ? 166 ASN A CB  1 
ATOM 1290 C CG  . ASN A 1 166 ? -1.167  19.993  -9.558  1.00 89.00  ? 166 ASN A CG  1 
ATOM 1291 O OD1 . ASN A 1 166 ? -1.820  18.950  -9.517  1.00 91.08  ? 166 ASN A OD1 1 
ATOM 1292 N ND2 . ASN A 1 166 ? -0.223  20.282  -8.671  1.00 90.74  ? 166 ASN A ND2 1 
ATOM 1293 N N   . SER A 1 167 ? -3.769  21.513  -13.485 1.00 83.96  ? 167 SER A N   1 
ATOM 1294 C CA  . SER A 1 167 ? -4.334  22.532  -14.372 1.00 78.09  ? 167 SER A CA  1 
ATOM 1295 C C   . SER A 1 167 ? -3.247  23.450  -14.928 1.00 78.21  ? 167 SER A C   1 
ATOM 1296 O O   . SER A 1 167 ? -3.406  24.670  -14.988 1.00 79.67  ? 167 SER A O   1 
ATOM 1297 C CB  . SER A 1 167 ? -5.427  23.338  -13.665 1.00 73.52  ? 167 SER A CB  1 
ATOM 1298 O OG  . SER A 1 167 ? -6.470  22.490  -13.217 1.00 73.16  ? 167 SER A OG  1 
ATOM 1299 N N   . GLY A 1 168 ? -2.128  22.853  -15.339 1.00 82.55  ? 168 GLY A N   1 
ATOM 1300 C CA  . GLY A 1 168 ? -1.025  23.588  -15.918 1.00 78.88  ? 168 GLY A CA  1 
ATOM 1301 C C   . GLY A 1 168 ? -0.045  24.174  -14.925 1.00 75.19  ? 168 GLY A C   1 
ATOM 1302 O O   . GLY A 1 168 ? 1.006   24.676  -15.343 1.00 70.84  ? 168 GLY A O   1 
ATOM 1303 N N   . ALA A 1 169 ? -0.350  24.128  -13.627 1.00 77.76  ? 169 ALA A N   1 
ATOM 1304 C CA  . ALA A 1 169 ? 0.557   24.706  -12.641 1.00 72.96  ? 169 ALA A CA  1 
ATOM 1305 C C   . ALA A 1 169 ? 1.838   23.891  -12.523 1.00 77.70  ? 169 ALA A C   1 
ATOM 1306 O O   . ALA A 1 169 ? 2.926   24.456  -12.358 1.00 75.80  ? 169 ALA A O   1 
ATOM 1307 C CB  . ALA A 1 169 ? -0.137  24.813  -11.283 1.00 68.64  ? 169 ALA A CB  1 
ATOM 1308 N N   . LEU A 1 170 ? 1.734   22.568  -12.613 1.00 82.23  ? 170 LEU A N   1 
ATOM 1309 C CA  . LEU A 1 170 ? 2.884   21.679  -12.460 1.00 80.40  ? 170 LEU A CA  1 
ATOM 1310 C C   . LEU A 1 170 ? 3.409   21.304  -13.841 1.00 80.93  ? 170 LEU A C   1 
ATOM 1311 O O   . LEU A 1 170 ? 2.805   20.498  -14.552 1.00 80.37  ? 170 LEU A O   1 
ATOM 1312 C CB  . LEU A 1 170 ? 2.515   20.438  -11.655 1.00 77.79  ? 170 LEU A CB  1 
ATOM 1313 C CG  . LEU A 1 170 ? 3.701   19.547  -11.271 1.00 78.00  ? 170 LEU A CG  1 
ATOM 1314 C CD1 . LEU A 1 170 ? 4.883   20.377  -10.776 1.00 81.18  ? 170 LEU A CD1 1 
ATOM 1315 C CD2 . LEU A 1 170 ? 3.294   18.514  -10.236 1.00 79.68  ? 170 LEU A CD2 1 
ATOM 1316 N N   . THR A 1 171 ? 4.538   21.902  -14.217 1.00 83.06  ? 171 THR A N   1 
ATOM 1317 C CA  . THR A 1 171 ? 5.298   21.479  -15.382 1.00 82.91  ? 171 THR A CA  1 
ATOM 1318 C C   . THR A 1 171 ? 6.680   20.966  -15.007 1.00 88.90  ? 171 THR A C   1 
ATOM 1319 O O   . THR A 1 171 ? 7.429   20.537  -15.893 1.00 87.25  ? 171 THR A O   1 
ATOM 1320 C CB  . THR A 1 171 ? 5.437   22.628  -16.390 1.00 78.30  ? 171 THR A CB  1 
ATOM 1321 O OG1 . THR A 1 171 ? 6.344   23.610  -15.874 1.00 79.79  ? 171 THR A OG1 1 
ATOM 1322 C CG2 . THR A 1 171 ? 4.085   23.279  -16.651 1.00 73.53  ? 171 THR A CG2 1 
ATOM 1323 N N   . SER A 1 172 ? 7.036   20.998  -13.725 1.00 97.35  ? 172 SER A N   1 
ATOM 1324 C CA  . SER A 1 172 ? 8.361   20.594  -13.270 1.00 98.32  ? 172 SER A CA  1 
ATOM 1325 C C   . SER A 1 172 ? 8.407   19.075  -13.149 1.00 100.77 ? 172 SER A C   1 
ATOM 1326 O O   . SER A 1 172 ? 7.730   18.490  -12.297 1.00 99.75  ? 172 SER A O   1 
ATOM 1327 C CB  . SER A 1 172 ? 8.690   21.261  -11.937 1.00 97.41  ? 172 SER A CB  1 
ATOM 1328 O OG  . SER A 1 172 ? 8.313   22.626  -11.944 1.00 96.06  ? 172 SER A OG  1 
ATOM 1329 N N   . GLY A 1 173 ? 9.209   18.437  -13.997 1.00 93.79  ? 173 GLY A N   1 
ATOM 1330 C CA  . GLY A 1 173 ? 9.328   16.995  -13.984 1.00 86.89  ? 173 GLY A CA  1 
ATOM 1331 C C   . GLY A 1 173 ? 8.206   16.251  -14.670 1.00 81.11  ? 173 GLY A C   1 
ATOM 1332 O O   . GLY A 1 173 ? 8.109   15.030  -14.509 1.00 75.58  ? 173 GLY A O   1 
ATOM 1333 N N   . VAL A 1 174 ? 7.361   16.940  -15.432 1.00 81.20  ? 174 VAL A N   1 
ATOM 1334 C CA  . VAL A 1 174 ? 6.239   16.315  -16.123 1.00 77.21  ? 174 VAL A CA  1 
ATOM 1335 C C   . VAL A 1 174 ? 6.746   15.716  -17.430 1.00 75.26  ? 174 VAL A C   1 
ATOM 1336 O O   . VAL A 1 174 ? 7.147   16.440  -18.345 1.00 74.26  ? 174 VAL A O   1 
ATOM 1337 C CB  . VAL A 1 174 ? 5.105   17.315  -16.373 1.00 77.09  ? 174 VAL A CB  1 
ATOM 1338 C CG1 . VAL A 1 174 ? 4.045   16.694  -17.261 1.00 71.58  ? 174 VAL A CG1 1 
ATOM 1339 C CG2 . VAL A 1 174 ? 4.494   17.751  -15.051 1.00 81.50  ? 174 VAL A CG2 1 
ATOM 1340 N N   . HIS A 1 175 ? 6.719   14.390  -17.518 1.00 74.84  ? 175 HIS A N   1 
ATOM 1341 C CA  . HIS A 1 175 ? 7.092   13.655  -18.719 1.00 68.83  ? 175 HIS A CA  1 
ATOM 1342 C C   . HIS A 1 175 ? 5.833   13.013  -19.286 1.00 67.24  ? 175 HIS A C   1 
ATOM 1343 O O   . HIS A 1 175 ? 5.226   12.158  -18.632 1.00 69.03  ? 175 HIS A O   1 
ATOM 1344 C CB  . HIS A 1 175 ? 8.128   12.574  -18.407 1.00 66.51  ? 175 HIS A CB  1 
ATOM 1345 C CG  . HIS A 1 175 ? 9.542   13.064  -18.370 1.00 63.52  ? 175 HIS A CG  1 
ATOM 1346 N ND1 . HIS A 1 175 ? 10.306  13.030  -17.223 1.00 62.63  ? 175 HIS A ND1 1 
ATOM 1347 C CD2 . HIS A 1 175 ? 10.339  13.581  -19.336 1.00 61.73  ? 175 HIS A CD2 1 
ATOM 1348 C CE1 . HIS A 1 175 ? 11.509  13.509  -17.481 1.00 66.52  ? 175 HIS A CE1 1 
ATOM 1349 N NE2 . HIS A 1 175 ? 11.555  13.853  -18.756 1.00 65.41  ? 175 HIS A NE2 1 
ATOM 1350 N N   . THR A 1 176 ? 5.440   13.423  -20.488 1.00 63.79  ? 176 THR A N   1 
ATOM 1351 C CA  . THR A 1 176 ? 4.340   12.791  -21.212 1.00 61.42  ? 176 THR A CA  1 
ATOM 1352 C C   . THR A 1 176 ? 4.944   11.985  -22.353 1.00 60.98  ? 176 THR A C   1 
ATOM 1353 O O   . THR A 1 176 ? 5.439   12.556  -23.331 1.00 60.76  ? 176 THR A O   1 
ATOM 1354 C CB  . THR A 1 176 ? 3.339   13.822  -21.730 1.00 63.49  ? 176 THR A CB  1 
ATOM 1355 O OG1 . THR A 1 176 ? 2.761   14.526  -20.625 1.00 71.26  ? 176 THR A OG1 1 
ATOM 1356 C CG2 . THR A 1 176 ? 2.231   13.136  -22.516 1.00 61.74  ? 176 THR A CG2 1 
ATOM 1357 N N   . PHE A 1 177 ? 4.906   10.670  -22.222 1.00 60.63  ? 177 PHE A N   1 
ATOM 1358 C CA  . PHE A 1 177 ? 5.556   9.778   -23.164 1.00 52.89  ? 177 PHE A CA  1 
ATOM 1359 C C   . PHE A 1 177 ? 4.773   9.694   -24.470 1.00 52.29  ? 177 PHE A C   1 
ATOM 1360 O O   . PHE A 1 177 ? 3.553   9.879   -24.485 1.00 53.69  ? 177 PHE A O   1 
ATOM 1361 C CB  . PHE A 1 177 ? 5.690   8.385   -22.565 1.00 55.53  ? 177 PHE A CB  1 
ATOM 1362 C CG  . PHE A 1 177 ? 6.625   8.319   -21.398 1.00 56.46  ? 177 PHE A CG  1 
ATOM 1363 C CD1 . PHE A 1 177 ? 6.197   8.655   -20.126 1.00 60.19  ? 177 PHE A CD1 1 
ATOM 1364 C CD2 . PHE A 1 177 ? 7.932   7.907   -21.574 1.00 55.02  ? 177 PHE A CD2 1 
ATOM 1365 C CE1 . PHE A 1 177 ? 7.063   8.591   -19.053 1.00 62.59  ? 177 PHE A CE1 1 
ATOM 1366 C CE2 . PHE A 1 177 ? 8.802   7.842   -20.506 1.00 56.87  ? 177 PHE A CE2 1 
ATOM 1367 C CZ  . PHE A 1 177 ? 8.367   8.183   -19.242 1.00 60.13  ? 177 PHE A CZ  1 
ATOM 1368 N N   . PRO A 1 178 ? 5.460   9.432   -25.580 1.00 51.93  ? 178 PRO A N   1 
ATOM 1369 C CA  . PRO A 1 178 ? 4.753   9.128   -26.826 1.00 51.84  ? 178 PRO A CA  1 
ATOM 1370 C C   . PRO A 1 178 ? 3.800   7.960   -26.627 1.00 52.08  ? 178 PRO A C   1 
ATOM 1371 O O   . PRO A 1 178 ? 4.094   7.010   -25.898 1.00 59.17  ? 178 PRO A O   1 
ATOM 1372 C CB  . PRO A 1 178 ? 5.888   8.768   -27.785 1.00 51.67  ? 178 PRO A CB  1 
ATOM 1373 C CG  . PRO A 1 178 ? 7.027   9.603   -27.311 1.00 51.54  ? 178 PRO A CG  1 
ATOM 1374 C CD  . PRO A 1 178 ? 6.907   9.612   -25.802 1.00 51.77  ? 178 PRO A CD  1 
ATOM 1375 N N   . ALA A 1 179 ? 2.639   8.044   -27.267 1.00 53.36  ? 179 ALA A N   1 
ATOM 1376 C CA  . ALA A 1 179 ? 1.665   6.972   -27.165 1.00 57.24  ? 179 ALA A CA  1 
ATOM 1377 C C   . ALA A 1 179 ? 2.146   5.736   -27.918 1.00 56.92  ? 179 ALA A C   1 
ATOM 1378 O O   . ALA A 1 179 ? 3.000   5.804   -28.804 1.00 61.06  ? 179 ALA A O   1 
ATOM 1379 C CB  . ALA A 1 179 ? 0.318   7.416   -27.723 1.00 57.10  ? 179 ALA A CB  1 
ATOM 1380 N N   . VAL A 1 180 ? 1.578   4.591   -27.554 1.00 57.81  ? 180 VAL A N   1 
ATOM 1381 C CA  . VAL A 1 180 ? 1.825   3.334   -28.244 1.00 58.26  ? 180 VAL A CA  1 
ATOM 1382 C C   . VAL A 1 180 ? 0.514   2.863   -28.853 1.00 58.99  ? 180 VAL A C   1 
ATOM 1383 O O   . VAL A 1 180 ? -0.555  3.027   -28.254 1.00 61.65  ? 180 VAL A O   1 
ATOM 1384 C CB  . VAL A 1 180 ? 2.410   2.264   -27.298 1.00 61.50  ? 180 VAL A CB  1 
ATOM 1385 C CG1 . VAL A 1 180 ? 3.822   2.642   -26.883 1.00 63.14  ? 180 VAL A CG1 1 
ATOM 1386 C CG2 . VAL A 1 180 ? 1.523   2.089   -26.075 1.00 60.60  ? 180 VAL A CG2 1 
ATOM 1387 N N   . LEU A 1 181 ? 0.593   2.293   -30.050 1.00 58.38  ? 181 LEU A N   1 
ATOM 1388 C CA  . LEU A 1 181 ? -0.586  1.774   -30.727 1.00 59.51  ? 181 LEU A CA  1 
ATOM 1389 C C   . LEU A 1 181 ? -0.700  0.281   -30.443 1.00 64.36  ? 181 LEU A C   1 
ATOM 1390 O O   . LEU A 1 181 ? 0.175   -0.502  -30.828 1.00 57.81  ? 181 LEU A O   1 
ATOM 1391 C CB  . LEU A 1 181 ? -0.522  2.052   -32.228 1.00 61.07  ? 181 LEU A CB  1 
ATOM 1392 C CG  . LEU A 1 181 ? -1.761  1.652   -33.030 1.00 56.05  ? 181 LEU A CG  1 
ATOM 1393 C CD1 . LEU A 1 181 ? -2.983  2.368   -32.494 1.00 57.74  ? 181 LEU A CD1 1 
ATOM 1394 C CD2 . LEU A 1 181 ? -1.566  1.998   -34.492 1.00 58.18  ? 181 LEU A CD2 1 
ATOM 1395 N N   . GLN A 1 182 ? -1.772  -0.102  -29.755 1.00 68.22  ? 182 GLN A N   1 
ATOM 1396 C CA  . GLN A 1 182 ? -1.988  -1.473  -29.330 1.00 70.32  ? 182 GLN A CA  1 
ATOM 1397 C C   . GLN A 1 182 ? -2.418  -2.339  -30.513 1.00 70.59  ? 182 GLN A C   1 
ATOM 1398 O O   . GLN A 1 182 ? -2.762  -1.847  -31.591 1.00 72.17  ? 182 GLN A O   1 
ATOM 1399 C CB  . GLN A 1 182 ? -3.042  -1.523  -28.223 1.00 71.06  ? 182 GLN A CB  1 
ATOM 1400 C CG  . GLN A 1 182 ? -2.667  -0.754  -26.963 1.00 70.31  ? 182 GLN A CG  1 
ATOM 1401 C CD  . GLN A 1 182 ? -3.796  -0.704  -25.946 1.00 77.35  ? 182 GLN A CD  1 
ATOM 1402 O OE1 . GLN A 1 182 ? -3.564  -0.485  -24.756 1.00 86.18  ? 182 GLN A OE1 1 
ATOM 1403 N NE2 . GLN A 1 182 ? -5.024  -0.901  -26.412 1.00 76.97  ? 182 GLN A NE2 1 
ATOM 1404 N N   . SER A 1 183 ? -2.391  -3.657  -30.297 1.00 69.47  ? 183 SER A N   1 
ATOM 1405 C CA  . SER A 1 183 ? -2.890  -4.578  -31.312 1.00 64.54  ? 183 SER A CA  1 
ATOM 1406 C C   . SER A 1 183 ? -4.367  -4.343  -31.594 1.00 60.57  ? 183 SER A C   1 
ATOM 1407 O O   . SER A 1 183 ? -4.825  -4.555  -32.723 1.00 60.18  ? 183 SER A O   1 
ATOM 1408 C CB  . SER A 1 183 ? -2.659  -6.023  -30.869 1.00 63.50  ? 183 SER A CB  1 
ATOM 1409 O OG  . SER A 1 183 ? -3.207  -6.250  -29.581 1.00 64.10  ? 183 SER A OG  1 
ATOM 1410 N N   . SER A 1 184 ? -5.120  -3.893  -30.589 1.00 59.13  ? 184 SER A N   1 
ATOM 1411 C CA  . SER A 1 184 ? -6.545  -3.631  -30.746 1.00 60.14  ? 184 SER A CA  1 
ATOM 1412 C C   . SER A 1 184 ? -6.838  -2.438  -31.646 1.00 60.92  ? 184 SER A C   1 
ATOM 1413 O O   . SER A 1 184 ? -8.012  -2.171  -31.924 1.00 60.88  ? 184 SER A O   1 
ATOM 1414 C CB  . SER A 1 184 ? -7.185  -3.407  -29.374 1.00 58.58  ? 184 SER A CB  1 
ATOM 1415 O OG  . SER A 1 184 ? -6.500  -2.400  -28.650 1.00 61.48  ? 184 SER A OG  1 
ATOM 1416 N N   . GLY A 1 185 ? -5.814  -1.719  -32.107 1.00 59.93  ? 185 GLY A N   1 
ATOM 1417 C CA  . GLY A 1 185 ? -6.006  -0.554  -32.939 1.00 59.87  ? 185 GLY A CA  1 
ATOM 1418 C C   . GLY A 1 185 ? -6.195  0.745   -32.187 1.00 60.80  ? 185 GLY A C   1 
ATOM 1419 O O   . GLY A 1 185 ? -6.215  1.811   -32.817 1.00 60.20  ? 185 GLY A O   1 
ATOM 1420 N N   . LEU A 1 186 ? -6.337  0.693   -30.869 1.00 58.59  ? 186 LEU A N   1 
ATOM 1421 C CA  . LEU A 1 186 ? -6.463  1.878   -30.036 1.00 57.54  ? 186 LEU A CA  1 
ATOM 1422 C C   . LEU A 1 186 ? -5.103  2.231   -29.442 1.00 61.35  ? 186 LEU A C   1 
ATOM 1423 O O   . LEU A 1 186 ? -4.187  1.408   -29.400 1.00 63.79  ? 186 LEU A O   1 
ATOM 1424 C CB  . LEU A 1 186 ? -7.489  1.646   -28.924 1.00 61.04  ? 186 LEU A CB  1 
ATOM 1425 C CG  . LEU A 1 186 ? -8.861  1.155   -29.399 1.00 58.85  ? 186 LEU A CG  1 
ATOM 1426 C CD1 . LEU A 1 186 ? -9.841  1.003   -28.237 1.00 62.95  ? 186 LEU A CD1 1 
ATOM 1427 C CD2 . LEU A 1 186 ? -9.427  2.073   -30.471 1.00 58.90  ? 186 LEU A CD2 1 
ATOM 1428 N N   . TYR A 1 187 ? -4.976  3.471   -28.983 1.00 63.29  ? 187 TYR A N   1 
ATOM 1429 C CA  . TYR A 1 187 ? -3.717  3.968   -28.448 1.00 63.20  ? 187 TYR A CA  1 
ATOM 1430 C C   . TYR A 1 187 ? -3.663  3.837   -26.934 1.00 63.62  ? 187 TYR A C   1 
ATOM 1431 O O   . TYR A 1 187 ? -4.680  3.669   -26.264 1.00 67.10  ? 187 TYR A O   1 
ATOM 1432 C CB  . TYR A 1 187 ? -3.498  5.429   -28.835 1.00 61.77  ? 187 TYR A CB  1 
ATOM 1433 C CG  . TYR A 1 187 ? -3.281  5.662   -30.303 1.00 58.26  ? 187 TYR A CG  1 
ATOM 1434 C CD1 . TYR A 1 187 ? -4.350  5.824   -31.171 1.00 55.56  ? 187 TYR A CD1 1 
ATOM 1435 C CD2 . TYR A 1 187 ? -1.996  5.725   -30.820 1.00 56.23  ? 187 TYR A CD2 1 
ATOM 1436 C CE1 . TYR A 1 187 ? -4.143  6.044   -32.518 1.00 56.61  ? 187 TYR A CE1 1 
ATOM 1437 C CE2 . TYR A 1 187 ? -1.779  5.941   -32.158 1.00 57.21  ? 187 TYR A CE2 1 
ATOM 1438 C CZ  . TYR A 1 187 ? -2.853  6.100   -33.004 1.00 58.09  ? 187 TYR A CZ  1 
ATOM 1439 O OH  . TYR A 1 187 ? -2.627  6.316   -34.342 1.00 57.66  ? 187 TYR A OH  1 
ATOM 1440 N N   . SER A 1 188 ? -2.445  3.943   -26.401 1.00 60.79  ? 188 SER A N   1 
ATOM 1441 C CA  . SER A 1 188 ? -2.201  3.950   -24.964 1.00 64.69  ? 188 SER A CA  1 
ATOM 1442 C C   . SER A 1 188 ? -1.065  4.919   -24.666 1.00 67.60  ? 188 SER A C   1 
ATOM 1443 O O   . SER A 1 188 ? -0.062  4.942   -25.384 1.00 62.77  ? 188 SER A O   1 
ATOM 1444 C CB  . SER A 1 188 ? -1.850  2.550   -24.447 1.00 71.65  ? 188 SER A CB  1 
ATOM 1445 O OG  . SER A 1 188 ? -2.005  2.473   -23.041 1.00 70.67  ? 188 SER A OG  1 
ATOM 1446 N N   . LEU A 1 189 ? -1.217  5.708   -23.602 1.00 66.71  ? 189 LEU A N   1 
ATOM 1447 C CA  . LEU A 1 189 ? -0.252  6.755   -23.295 1.00 68.85  ? 189 LEU A CA  1 
ATOM 1448 C C   . LEU A 1 189 ? -0.121  6.914   -21.787 1.00 71.65  ? 189 LEU A C   1 
ATOM 1449 O O   . LEU A 1 189 ? -1.090  6.745   -21.043 1.00 73.37  ? 189 LEU A O   1 
ATOM 1450 C CB  . LEU A 1 189 ? -0.663  8.089   -23.936 1.00 67.93  ? 189 LEU A CB  1 
ATOM 1451 C CG  . LEU A 1 189 ? 0.164   9.358   -23.706 1.00 67.94  ? 189 LEU A CG  1 
ATOM 1452 C CD1 . LEU A 1 189 ? 0.261   10.162  -24.996 1.00 64.28  ? 189 LEU A CD1 1 
ATOM 1453 C CD2 . LEU A 1 189 ? -0.434  10.208  -22.597 1.00 69.80  ? 189 LEU A CD2 1 
ATOM 1454 N N   . SER A 1 190 ? 1.087   7.258   -21.345 1.00 66.84  ? 190 SER A N   1 
ATOM 1455 C CA  . SER A 1 190 ? 1.347   7.523   -19.938 1.00 65.92  ? 190 SER A CA  1 
ATOM 1456 C C   . SER A 1 190 ? 2.050   8.862   -19.783 1.00 68.44  ? 190 SER A C   1 
ATOM 1457 O O   . SER A 1 190 ? 2.978   9.177   -20.533 1.00 69.59  ? 190 SER A O   1 
ATOM 1458 C CB  . SER A 1 190 ? 2.196   6.416   -19.307 1.00 63.26  ? 190 SER A CB  1 
ATOM 1459 O OG  . SER A 1 190 ? 3.443   6.302   -19.966 1.00 63.55  ? 190 SER A OG  1 
ATOM 1460 N N   . SER A 1 191 ? 1.595   9.649   -18.811 1.00 69.28  ? 191 SER A N   1 
ATOM 1461 C CA  . SER A 1 191 ? 2.247   10.888  -18.415 1.00 69.53  ? 191 SER A CA  1 
ATOM 1462 C C   . SER A 1 191 ? 2.589   10.795  -16.938 1.00 74.40  ? 191 SER A C   1 
ATOM 1463 O O   . SER A 1 191 ? 1.741   10.413  -16.126 1.00 80.34  ? 191 SER A O   1 
ATOM 1464 C CB  . SER A 1 191 ? 1.355   12.102  -18.676 1.00 68.73  ? 191 SER A CB  1 
ATOM 1465 O OG  . SER A 1 191 ? 1.981   13.291  -18.228 1.00 67.53  ? 191 SER A OG  1 
ATOM 1466 N N   . VAL A 1 192 ? 3.826   11.141  -16.593 1.00 73.00  ? 192 VAL A N   1 
ATOM 1467 C CA  . VAL A 1 192 ? 4.313   10.990  -15.234 1.00 72.70  ? 192 VAL A CA  1 
ATOM 1468 C C   . VAL A 1 192 ? 4.987   12.285  -14.816 1.00 75.49  ? 192 VAL A C   1 
ATOM 1469 O O   . VAL A 1 192 ? 5.333   13.137  -15.640 1.00 77.12  ? 192 VAL A O   1 
ATOM 1470 C CB  . VAL A 1 192 ? 5.295   9.813   -15.096 1.00 72.55  ? 192 VAL A CB  1 
ATOM 1471 C CG1 . VAL A 1 192 ? 4.603   8.497   -15.445 1.00 72.55  ? 192 VAL A CG1 1 
ATOM 1472 C CG2 . VAL A 1 192 ? 6.507   10.045  -15.971 1.00 70.68  ? 192 VAL A CG2 1 
ATOM 1473 N N   . VAL A 1 193 ? 5.186   12.410  -13.513 1.00 78.59  ? 193 VAL A N   1 
ATOM 1474 C CA  . VAL A 1 193 ? 5.851   13.572  -12.942 1.00 78.68  ? 193 VAL A CA  1 
ATOM 1475 C C   . VAL A 1 193 ? 6.566   13.145  -11.660 1.00 77.09  ? 193 VAL A C   1 
ATOM 1476 O O   . VAL A 1 193 ? 6.041   12.354  -10.867 1.00 77.65  ? 193 VAL A O   1 
ATOM 1477 C CB  . VAL A 1 193 ? 4.871   14.746  -12.722 1.00 81.12  ? 193 VAL A CB  1 
ATOM 1478 C CG1 . VAL A 1 193 ? 3.667   14.294  -11.927 1.00 80.44  ? 193 VAL A CG1 1 
ATOM 1479 C CG2 . VAL A 1 193 ? 5.590   15.847  -11.972 1.00 81.89  ? 193 VAL A CG2 1 
ATOM 1480 N N   . THR A 1 194 ? 7.803   13.633  -11.501 1.00 77.76  ? 194 THR A N   1 
ATOM 1481 C CA  . THR A 1 194 ? 8.667   13.339  -10.357 1.00 78.79  ? 194 THR A CA  1 
ATOM 1482 C C   . THR A 1 194 ? 8.638   14.543  -9.420  1.00 82.71  ? 194 THR A C   1 
ATOM 1483 O O   . THR A 1 194 ? 9.101   15.632  -9.777  1.00 82.49  ? 194 THR A O   1 
ATOM 1484 C CB  . THR A 1 194 ? 10.100  13.033  -10.801 1.00 73.31  ? 194 THR A CB  1 
ATOM 1485 O OG1 . THR A 1 194 ? 10.542  14.030  -11.731 1.00 72.26  ? 194 THR A OG1 1 
ATOM 1486 C CG2 . THR A 1 194 ? 10.183  11.659  -11.454 1.00 78.59  ? 194 THR A CG2 1 
ATOM 1487 N N   . VAL A 1 195 ? 8.079   14.348  -8.231  1.00 86.62  ? 195 VAL A N   1 
ATOM 1488 C CA  . VAL A 1 195 ? 7.928   15.415  -7.246  1.00 89.34  ? 195 VAL A CA  1 
ATOM 1489 C C   . VAL A 1 195 ? 8.750   15.039  -6.020  1.00 96.74  ? 195 VAL A C   1 
ATOM 1490 O O   . VAL A 1 195 ? 9.179   13.882  -5.898  1.00 96.89  ? 195 VAL A O   1 
ATOM 1491 C CB  . VAL A 1 195 ? 6.449   15.633  -6.887  1.00 89.82  ? 195 VAL A CB  1 
ATOM 1492 C CG1 . VAL A 1 195 ? 5.627   15.864  -8.146  1.00 86.79  ? 195 VAL A CG1 1 
ATOM 1493 C CG2 . VAL A 1 195 ? 5.917   14.441  -6.106  1.00 95.32  ? 195 VAL A CG2 1 
ATOM 1494 N N   . PRO A 1 196 ? 9.017   15.970  -5.106  1.00 94.48  ? 196 PRO A N   1 
ATOM 1495 C CA  . PRO A 1 196 ? 9.627   15.582  -3.831  1.00 92.11  ? 196 PRO A CA  1 
ATOM 1496 C C   . PRO A 1 196 ? 8.684   14.697  -3.031  1.00 94.87  ? 196 PRO A C   1 
ATOM 1497 O O   . PRO A 1 196 ? 7.476   14.939  -2.972  1.00 94.54  ? 196 PRO A O   1 
ATOM 1498 C CB  . PRO A 1 196 ? 9.878   16.922  -3.126  1.00 92.22  ? 196 PRO A CB  1 
ATOM 1499 C CG  . PRO A 1 196 ? 9.026   17.918  -3.848  1.00 89.15  ? 196 PRO A CG  1 
ATOM 1500 C CD  . PRO A 1 196 ? 8.923   17.432  -5.254  1.00 93.14  ? 196 PRO A CD  1 
ATOM 1501 N N   . SER A 1 197 ? 9.252   13.654  -2.418  1.00 97.81  ? 197 SER A N   1 
ATOM 1502 C CA  . SER A 1 197 ? 8.441   12.709  -1.656  1.00 95.05  ? 197 SER A CA  1 
ATOM 1503 C C   . SER A 1 197 ? 7.745   13.381  -0.481  1.00 96.54  ? 197 SER A C   1 
ATOM 1504 O O   . SER A 1 197 ? 6.677   12.929  -0.052  1.00 98.63  ? 197 SER A O   1 
ATOM 1505 C CB  . SER A 1 197 ? 9.309   11.549  -1.165  1.00 89.45  ? 197 SER A CB  1 
ATOM 1506 O OG  . SER A 1 197 ? 10.506  12.023  -0.576  1.00 82.58  ? 197 SER A OG  1 
ATOM 1507 N N   . SER A 1 198 ? 8.329   14.458  0.050   1.00 93.95  ? 198 SER A N   1 
ATOM 1508 C CA  . SER A 1 198 ? 7.691   15.185  1.143   1.00 95.99  ? 198 SER A CA  1 
ATOM 1509 C C   . SER A 1 198 ? 6.375   15.814  0.707   1.00 94.74  ? 198 SER A C   1 
ATOM 1510 O O   . SER A 1 198 ? 5.475   16.007  1.533   1.00 95.96  ? 198 SER A O   1 
ATOM 1511 C CB  . SER A 1 198 ? 8.636   16.259  1.680   1.00 97.38  ? 198 SER A CB  1 
ATOM 1512 O OG  . SER A 1 198 ? 7.908   17.329  2.259   1.00 95.07  ? 198 SER A OG  1 
ATOM 1513 N N   . SER A 1 199 ? 6.243   16.139  -0.581  1.00 92.56  ? 199 SER A N   1 
ATOM 1514 C CA  . SER A 1 199 ? 5.023   16.760  -1.081  1.00 96.67  ? 199 SER A CA  1 
ATOM 1515 C C   . SER A 1 199 ? 3.836   15.806  -1.075  1.00 98.19  ? 199 SER A C   1 
ATOM 1516 O O   . SER A 1 199 ? 2.691   16.265  -1.137  1.00 100.50 ? 199 SER A O   1 
ATOM 1517 C CB  . SER A 1 199 ? 5.248   17.292  -2.497  1.00 94.61  ? 199 SER A CB  1 
ATOM 1518 O OG  . SER A 1 199 ? 6.079   18.438  -2.493  1.00 95.69  ? 199 SER A OG  1 
ATOM 1519 N N   . LEU A 1 200 ? 4.080   14.500  -1.007  1.00 96.01  ? 200 LEU A N   1 
ATOM 1520 C CA  . LEU A 1 200 ? 2.994   13.532  -1.027  1.00 96.60  ? 200 LEU A CA  1 
ATOM 1521 C C   . LEU A 1 200 ? 2.125   13.668  0.219   1.00 97.24  ? 200 LEU A C   1 
ATOM 1522 O O   . LEU A 1 200 ? 2.608   13.967  1.314   1.00 98.90  ? 200 LEU A O   1 
ATOM 1523 C CB  . LEU A 1 200 ? 3.545   12.110  -1.127  1.00 95.08  ? 200 LEU A CB  1 
ATOM 1524 C CG  . LEU A 1 200 ? 4.394   11.829  -2.368  1.00 90.52  ? 200 LEU A CG  1 
ATOM 1525 C CD1 . LEU A 1 200 ? 4.921   10.400  -2.356  1.00 93.62  ? 200 LEU A CD1 1 
ATOM 1526 C CD2 . LEU A 1 200 ? 3.604   12.113  -3.637  1.00 92.31  ? 200 LEU A CD2 1 
ATOM 1527 N N   . GLY A 1 201 ? 0.832   13.442  0.038   1.00 94.36  ? 201 GLY A N   1 
ATOM 1528 C CA  . GLY A 1 201 ? -0.128  13.610  1.127   1.00 96.51  ? 201 GLY A CA  1 
ATOM 1529 C C   . GLY A 1 201 ? -0.580  15.034  1.345   1.00 105.59 ? 201 GLY A C   1 
ATOM 1530 O O   . GLY A 1 201 ? -1.783  15.309  1.344   1.00 106.57 ? 201 GLY A O   1 
ATOM 1531 N N   . THR A 1 202 ? 0.364   15.959  1.524   1.00 107.18 ? 202 THR A N   1 
ATOM 1532 C CA  . THR A 1 202 ? 0.007   17.354  1.759   1.00 100.93 ? 202 THR A CA  1 
ATOM 1533 C C   . THR A 1 202 ? -0.435  18.039  0.472   1.00 101.88 ? 202 THR A C   1 
ATOM 1534 O O   . THR A 1 202 ? -1.477  18.702  0.441   1.00 103.14 ? 202 THR A O   1 
ATOM 1535 C CB  . THR A 1 202 ? 1.186   18.097  2.387   1.00 98.27  ? 202 THR A CB  1 
ATOM 1536 O OG1 . THR A 1 202 ? 2.112   18.481  1.363   1.00 99.05  ? 202 THR A OG1 1 
ATOM 1537 C CG2 . THR A 1 202 ? 1.893   17.207  3.400   1.00 100.37 ? 202 THR A CG2 1 
ATOM 1538 N N   . GLN A 1 203 ? 0.345   17.895  -0.595  1.00 100.63 ? 203 GLN A N   1 
ATOM 1539 C CA  . GLN A 1 203 ? -0.024  18.475  -1.875  1.00 106.42 ? 203 GLN A CA  1 
ATOM 1540 C C   . GLN A 1 203 ? -1.108  17.640  -2.550  1.00 105.30 ? 203 GLN A C   1 
ATOM 1541 O O   . GLN A 1 203 ? -1.294  16.455  -2.257  1.00 105.27 ? 203 GLN A O   1 
ATOM 1542 C CB  . GLN A 1 203 ? 1.196   18.593  -2.788  1.00 102.30 ? 203 GLN A CB  1 
ATOM 1543 C CG  . GLN A 1 203 ? 2.303   19.478  -2.236  1.00 105.44 ? 203 GLN A CG  1 
ATOM 1544 C CD  . GLN A 1 203 ? 2.096   20.942  -2.570  1.00 106.18 ? 203 GLN A CD  1 
ATOM 1545 O OE1 . GLN A 1 203 ? 1.519   21.277  -3.604  1.00 101.80 ? 203 GLN A OE1 1 
ATOM 1546 N NE2 . GLN A 1 203 ? 2.574   21.824  -1.699  1.00 103.31 ? 203 GLN A NE2 1 
ATOM 1547 N N   . THR A 1 204 ? -1.829  18.279  -3.467  1.00 101.92 ? 204 THR A N   1 
ATOM 1548 C CA  . THR A 1 204 ? -2.925  17.651  -4.199  1.00 103.03 ? 204 THR A CA  1 
ATOM 1549 C C   . THR A 1 204 ? -2.551  17.608  -5.674  1.00 102.88 ? 204 THR A C   1 
ATOM 1550 O O   . THR A 1 204 ? -2.526  18.646  -6.344  1.00 102.69 ? 204 THR A O   1 
ATOM 1551 C CB  . THR A 1 204 ? -4.235  18.410  -3.991  1.00 104.99 ? 204 THR A CB  1 
ATOM 1552 O OG1 . THR A 1 204 ? -4.335  18.828  -2.623  1.00 104.43 ? 204 THR A OG1 1 
ATOM 1553 C CG2 . THR A 1 204 ? -5.422  17.524  -4.334  1.00 101.53 ? 204 THR A CG2 1 
ATOM 1554 N N   . TYR A 1 205 ? -2.264  16.412  -6.176  1.00 101.03 ? 205 TYR A N   1 
ATOM 1555 C CA  . TYR A 1 205 ? -1.864  16.222  -7.562  1.00 94.72  ? 205 TYR A CA  1 
ATOM 1556 C C   . TYR A 1 205 ? -3.034  15.698  -8.382  1.00 91.68  ? 205 TYR A C   1 
ATOM 1557 O O   . TYR A 1 205 ? -3.702  14.738  -7.983  1.00 91.95  ? 205 TYR A O   1 
ATOM 1558 C CB  . TYR A 1 205 ? -0.673  15.270  -7.661  1.00 91.37  ? 205 TYR A CB  1 
ATOM 1559 C CG  . TYR A 1 205 ? 0.590   15.830  -7.051  1.00 93.35  ? 205 TYR A CG  1 
ATOM 1560 C CD1 . TYR A 1 205 ? 1.190   16.962  -7.583  1.00 89.25  ? 205 TYR A CD1 1 
ATOM 1561 C CD2 . TYR A 1 205 ? 1.182   15.231  -5.947  1.00 94.48  ? 205 TYR A CD2 1 
ATOM 1562 C CE1 . TYR A 1 205 ? 2.342   17.483  -7.037  1.00 87.94  ? 205 TYR A CE1 1 
ATOM 1563 C CE2 . TYR A 1 205 ? 2.339   15.747  -5.392  1.00 92.21  ? 205 TYR A CE2 1 
ATOM 1564 C CZ  . TYR A 1 205 ? 2.914   16.874  -5.944  1.00 90.05  ? 205 TYR A CZ  1 
ATOM 1565 O OH  . TYR A 1 205 ? 4.064   17.401  -5.406  1.00 94.31  ? 205 TYR A OH  1 
ATOM 1566 N N   . ILE A 1 206 ? -3.271  16.334  -9.525  1.00 91.14  ? 206 ILE A N   1 
ATOM 1567 C CA  . ILE A 1 206 ? -4.348  15.971  -10.433 1.00 89.07  ? 206 ILE A CA  1 
ATOM 1568 C C   . ILE A 1 206 ? -3.789  15.969  -11.850 1.00 89.56  ? 206 ILE A C   1 
ATOM 1569 O O   . ILE A 1 206 ? -2.883  16.741  -12.181 1.00 91.59  ? 206 ILE A O   1 
ATOM 1570 C CB  . ILE A 1 206 ? -5.551  16.937  -10.296 1.00 88.02  ? 206 ILE A CB  1 
ATOM 1571 C CG1 . ILE A 1 206 ? -6.830  16.307  -10.844 1.00 90.66  ? 206 ILE A CG1 1 
ATOM 1572 C CG2 . ILE A 1 206 ? -5.270  18.268  -10.978 1.00 88.74  ? 206 ILE A CG2 1 
ATOM 1573 C CD1 . ILE A 1 206 ? -8.089  16.984  -10.348 1.00 90.06  ? 206 ILE A CD1 1 
ATOM 1574 N N   . CYS A 1 207 ? -4.310  15.069  -12.681 1.00 89.50  ? 207 CYS A N   1 
ATOM 1575 C CA  . CYS A 1 207 ? -3.915  14.974  -14.081 1.00 91.39  ? 207 CYS A CA  1 
ATOM 1576 C C   . CYS A 1 207 ? -5.134  15.246  -14.948 1.00 87.85  ? 207 CYS A C   1 
ATOM 1577 O O   . CYS A 1 207 ? -6.154  14.558  -14.826 1.00 86.41  ? 207 CYS A O   1 
ATOM 1578 C CB  . CYS A 1 207 ? -3.306  13.605  -14.405 1.00 89.08  ? 207 CYS A CB  1 
ATOM 1579 S SG  . CYS A 1 207 ? -4.264  12.159  -13.880 1.00 100.93 ? 207 CYS A SG  1 
ATOM 1580 N N   . ASN A 1 208 ? -5.030  16.252  -15.813 1.00 87.78  ? 208 ASN A N   1 
ATOM 1581 C CA  . ASN A 1 208 ? -6.109  16.640  -16.713 1.00 86.95  ? 208 ASN A CA  1 
ATOM 1582 C C   . ASN A 1 208 ? -5.840  16.025  -18.081 1.00 82.84  ? 208 ASN A C   1 
ATOM 1583 O O   . ASN A 1 208 ? -4.878  16.401  -18.757 1.00 83.01  ? 208 ASN A O   1 
ATOM 1584 C CB  . ASN A 1 208 ? -6.214  18.160  -16.818 1.00 88.68  ? 208 ASN A CB  1 
ATOM 1585 C CG  . ASN A 1 208 ? -6.315  18.836  -15.467 1.00 86.28  ? 208 ASN A CG  1 
ATOM 1586 O OD1 . ASN A 1 208 ? -6.182  18.194  -14.425 1.00 90.24  ? 208 ASN A OD1 1 
ATOM 1587 N ND2 . ASN A 1 208 ? -6.545  20.144  -15.478 1.00 83.67  ? 208 ASN A ND2 1 
ATOM 1588 N N   . VAL A 1 209 ? -6.683  15.082  -18.486 1.00 81.56  ? 209 VAL A N   1 
ATOM 1589 C CA  . VAL A 1 209 ? -6.623  14.502  -19.823 1.00 81.97  ? 209 VAL A CA  1 
ATOM 1590 C C   . VAL A 1 209 ? -7.704  15.146  -20.676 1.00 84.04  ? 209 VAL A C   1 
ATOM 1591 O O   . VAL A 1 209 ? -8.824  15.386  -20.206 1.00 86.02  ? 209 VAL A O   1 
ATOM 1592 C CB  . VAL A 1 209 ? -6.777  12.968  -19.785 1.00 77.44  ? 209 VAL A CB  1 
ATOM 1593 C CG1 . VAL A 1 209 ? -5.574  12.333  -19.108 1.00 74.70  ? 209 VAL A CG1 1 
ATOM 1594 C CG2 . VAL A 1 209 ? -8.061  12.568  -19.074 1.00 83.84  ? 209 VAL A CG2 1 
ATOM 1595 N N   . ASN A 1 210 ? -7.367  15.445  -21.928 1.00 80.85  ? 210 ASN A N   1 
ATOM 1596 C CA  . ASN A 1 210 ? -8.302  16.077  -22.854 1.00 80.78  ? 210 ASN A CA  1 
ATOM 1597 C C   . ASN A 1 210 ? -8.176  15.390  -24.206 1.00 80.71  ? 210 ASN A C   1 
ATOM 1598 O O   . ASN A 1 210 ? -7.164  15.550  -24.896 1.00 79.57  ? 210 ASN A O   1 
ATOM 1599 C CB  . ASN A 1 210 ? -8.038  17.578  -22.978 1.00 82.95  ? 210 ASN A CB  1 
ATOM 1600 C CG  . ASN A 1 210 ? -9.175  18.313  -23.661 1.00 89.41  ? 210 ASN A CG  1 
ATOM 1601 O OD1 . ASN A 1 210 ? -10.267 17.770  -23.831 1.00 88.42  ? 210 ASN A OD1 1 
ATOM 1602 N ND2 . ASN A 1 210 ? -8.923  19.555  -24.060 1.00 91.52  ? 210 ASN A ND2 1 
ATOM 1603 N N   . HIS A 1 211 ? -9.198  14.627  -24.577 1.00 80.01  ? 211 HIS A N   1 
ATOM 1604 C CA  . HIS A 1 211 ? -9.277  13.962  -25.875 1.00 76.25  ? 211 HIS A CA  1 
ATOM 1605 C C   . HIS A 1 211 ? -10.428 14.617  -26.634 1.00 79.85  ? 211 HIS A C   1 
ATOM 1606 O O   . HIS A 1 211 ? -11.587 14.225  -26.494 1.00 84.81  ? 211 HIS A O   1 
ATOM 1607 C CB  . HIS A 1 211 ? -9.486  12.460  -25.712 1.00 76.84  ? 211 HIS A CB  1 
ATOM 1608 C CG  . HIS A 1 211 ? -9.444  11.699  -27.001 1.00 71.46  ? 211 HIS A CG  1 
ATOM 1609 N ND1 . HIS A 1 211 ? -10.580 11.265  -27.647 1.00 72.75  ? 211 HIS A ND1 1 
ATOM 1610 C CD2 . HIS A 1 211 ? -8.401  11.282  -27.757 1.00 67.07  ? 211 HIS A CD2 1 
ATOM 1611 C CE1 . HIS A 1 211 ? -10.241 10.622  -28.750 1.00 68.47  ? 211 HIS A CE1 1 
ATOM 1612 N NE2 . HIS A 1 211 ? -8.923  10.618  -28.840 1.00 63.88  ? 211 HIS A NE2 1 
ATOM 1613 N N   . LYS A 1 212 ? -10.097 15.628  -27.434 1.00 78.34  ? 212 LYS A N   1 
ATOM 1614 C CA  . LYS A 1 212 ? -11.088 16.428  -28.147 1.00 78.85  ? 212 LYS A CA  1 
ATOM 1615 C C   . LYS A 1 212 ? -11.869 15.640  -29.200 1.00 78.06  ? 212 LYS A C   1 
ATOM 1616 O O   . LYS A 1 212 ? -13.075 15.876  -29.349 1.00 80.69  ? 212 LYS A O   1 
ATOM 1617 C CB  . LYS A 1 212 ? -10.419 17.647  -28.789 1.00 76.13  ? 212 LYS A CB  1 
ATOM 1618 C CG  . LYS A 1 212 ? -10.114 18.767  -27.804 1.00 76.40  ? 212 LYS A CG  1 
ATOM 1619 C CD  . LYS A 1 212 ? -8.894  19.577  -28.214 1.00 79.87  ? 212 LYS A CD  1 
ATOM 1620 C CE  . LYS A 1 212 ? -7.611  18.777  -28.072 1.00 83.78  ? 212 LYS A CE  1 
ATOM 1621 N NZ  . LYS A 1 212 ? -6.418  19.592  -28.430 1.00 80.59  ? 212 LYS A NZ  1 
ATOM 1622 N N   . PRO A 1 213 ? -11.246 14.728  -29.963 1.00 74.29  ? 213 PRO A N   1 
ATOM 1623 C CA  . PRO A 1 213 ? -12.037 13.929  -30.916 1.00 73.99  ? 213 PRO A CA  1 
ATOM 1624 C C   . PRO A 1 213 ? -13.216 13.201  -30.291 1.00 77.82  ? 213 PRO A C   1 
ATOM 1625 O O   . PRO A 1 213 ? -14.241 13.015  -30.959 1.00 75.04  ? 213 PRO A O   1 
ATOM 1626 C CB  . PRO A 1 213 ? -10.999 12.951  -31.475 1.00 69.78  ? 213 PRO A CB  1 
ATOM 1627 C CG  . PRO A 1 213 ? -9.761  13.757  -31.497 1.00 68.66  ? 213 PRO A CG  1 
ATOM 1628 C CD  . PRO A 1 213 ? -9.801  14.557  -30.215 1.00 74.76  ? 213 PRO A CD  1 
ATOM 1629 N N   . SER A 1 214 ? -13.109 12.785  -29.032 1.00 83.22  ? 214 SER A N   1 
ATOM 1630 C CA  . SER A 1 214 ? -14.226 12.177  -28.324 1.00 86.27  ? 214 SER A CA  1 
ATOM 1631 C C   . SER A 1 214 ? -14.932 13.150  -27.391 1.00 92.61  ? 214 SER A C   1 
ATOM 1632 O O   . SER A 1 214 ? -15.921 12.769  -26.758 1.00 92.44  ? 214 SER A O   1 
ATOM 1633 C CB  . SER A 1 214 ? -13.750 10.957  -27.530 1.00 85.01  ? 214 SER A CB  1 
ATOM 1634 O OG  . SER A 1 214 ? -12.793 11.336  -26.555 1.00 81.01  ? 214 SER A OG  1 
ATOM 1635 N N   . ASN A 1 215 ? -14.449 14.392  -27.298 1.00 107.95 ? 215 ASN A N   1 
ATOM 1636 C CA  . ASN A 1 215 ? -15.010 15.402  -26.399 1.00 108.30 ? 215 ASN A CA  1 
ATOM 1637 C C   . ASN A 1 215 ? -15.017 14.897  -24.956 1.00 111.09 ? 215 ASN A C   1 
ATOM 1638 O O   . ASN A 1 215 ? -16.016 14.991  -24.240 1.00 119.30 ? 215 ASN A O   1 
ATOM 1639 C CB  . ASN A 1 215 ? -16.412 15.822  -26.846 1.00 108.56 ? 215 ASN A CB  1 
ATOM 1640 C CG  . ASN A 1 215 ? -16.396 17.047  -27.740 1.00 109.25 ? 215 ASN A CG  1 
ATOM 1641 O OD1 . ASN A 1 215 ? -16.196 18.169  -27.273 1.00 120.50 ? 215 ASN A OD1 1 
ATOM 1642 N ND2 . ASN A 1 215 ? -16.606 16.838  -29.035 1.00 109.07 ? 215 ASN A ND2 1 
ATOM 1643 N N   . THR A 1 216 ? -13.877 14.354  -24.532 1.00 97.48  ? 216 THR A N   1 
ATOM 1644 C CA  . THR A 1 216 ? -13.728 13.731  -23.220 1.00 91.10  ? 216 THR A CA  1 
ATOM 1645 C C   . THR A 1 216 ? -12.585 14.412  -22.480 1.00 87.28  ? 216 THR A C   1 
ATOM 1646 O O   . THR A 1 216 ? -11.413 14.212  -22.818 1.00 87.72  ? 216 THR A O   1 
ATOM 1647 C CB  . THR A 1 216 ? -13.474 12.230  -23.353 1.00 89.22  ? 216 THR A CB  1 
ATOM 1648 O OG1 . THR A 1 216 ? -14.488 11.640  -24.177 1.00 89.38  ? 216 THR A OG1 1 
ATOM 1649 C CG2 . THR A 1 216 ? -13.481 11.565  -21.987 1.00 85.32  ? 216 THR A CG2 1 
ATOM 1650 N N   . LYS A 1 217 ? -12.925 15.214  -21.474 1.00 89.21  ? 217 LYS A N   1 
ATOM 1651 C CA  . LYS A 1 217 ? -11.949 15.826  -20.582 1.00 89.23  ? 217 LYS A CA  1 
ATOM 1652 C C   . LYS A 1 217 ? -12.212 15.328  -19.170 1.00 91.43  ? 217 LYS A C   1 
ATOM 1653 O O   . LYS A 1 217 ? -13.290 15.568  -18.616 1.00 93.53  ? 217 LYS A O   1 
ATOM 1654 C CB  . LYS A 1 217 ? -12.018 17.354  -20.635 1.00 90.14  ? 217 LYS A CB  1 
ATOM 1655 C CG  . LYS A 1 217 ? -11.091 18.034  -19.637 1.00 88.51  ? 217 LYS A CG  1 
ATOM 1656 C CD  . LYS A 1 217 ? -10.732 19.448  -20.065 1.00 90.47  ? 217 LYS A CD  1 
ATOM 1657 C CE  . LYS A 1 217 ? -11.965 20.241  -20.462 1.00 92.78  ? 217 LYS A CE  1 
ATOM 1658 N NZ  . LYS A 1 217 ? -11.604 21.573  -21.022 1.00 94.31  ? 217 LYS A NZ  1 
ATOM 1659 N N   . VAL A 1 218 ? -11.233 14.634  -18.593 1.00 93.31  ? 218 VAL A N   1 
ATOM 1660 C CA  . VAL A 1 218 ? -11.359 14.049  -17.264 1.00 94.54  ? 218 VAL A CA  1 
ATOM 1661 C C   . VAL A 1 218 ? -10.210 14.540  -16.395 1.00 91.95  ? 218 VAL A C   1 
ATOM 1662 O O   . VAL A 1 218 ? -9.072  14.664  -16.862 1.00 87.23  ? 218 VAL A O   1 
ATOM 1663 C CB  . VAL A 1 218 ? -11.373 12.506  -17.313 1.00 89.14  ? 218 VAL A CB  1 
ATOM 1664 C CG1 . VAL A 1 218 ? -11.770 11.936  -15.959 1.00 92.26  ? 218 VAL A CG1 1 
ATOM 1665 C CG2 . VAL A 1 218 ? -12.304 12.008  -18.406 1.00 85.14  ? 218 VAL A CG2 1 
ATOM 1666 N N   . ASP A 1 219 ? -10.511 14.817  -15.130 1.00 88.87  ? 219 ASP A N   1 
ATOM 1667 C CA  . ASP A 1 219 ? -9.517  15.186  -14.131 1.00 85.72  ? 219 ASP A CA  1 
ATOM 1668 C C   . ASP A 1 219 ? -9.460  14.081  -13.085 1.00 88.94  ? 219 ASP A C   1 
ATOM 1669 O O   . ASP A 1 219 ? -10.446 13.839  -12.381 1.00 91.43  ? 219 ASP A O   1 
ATOM 1670 C CB  . ASP A 1 219 ? -9.867  16.526  -13.485 1.00 89.44  ? 219 ASP A CB  1 
ATOM 1671 C CG  . ASP A 1 219 ? -10.105 17.617  -14.506 1.00 90.37  ? 219 ASP A CG  1 
ATOM 1672 O OD1 . ASP A 1 219 ? -11.186 17.621  -15.132 1.00 92.49  ? 219 ASP A OD1 1 
ATOM 1673 O OD2 . ASP A 1 219 ? -9.215  18.475  -14.679 1.00 87.31  ? 219 ASP A OD2 1 
ATOM 1674 N N   . LYS A 1 220 ? -8.314  13.413  -12.988 1.00 91.77  ? 220 LYS A N   1 
ATOM 1675 C CA  . LYS A 1 220 ? -8.147  12.266  -12.107 1.00 88.74  ? 220 LYS A CA  1 
ATOM 1676 C C   . LYS A 1 220 ? -7.162  12.592  -10.993 1.00 86.54  ? 220 LYS A C   1 
ATOM 1677 O O   . LYS A 1 220 ? -6.119  13.209  -11.233 1.00 87.97  ? 220 LYS A O   1 
ATOM 1678 C CB  . LYS A 1 220 ? -7.664  11.040  -12.886 1.00 87.57  ? 220 LYS A CB  1 
ATOM 1679 C CG  . LYS A 1 220 ? -7.902  9.719   -12.176 1.00 86.61  ? 220 LYS A CG  1 
ATOM 1680 C CD  . LYS A 1 220 ? -9.302  9.194   -12.450 1.00 83.71  ? 220 LYS A CD  1 
ATOM 1681 C CE  . LYS A 1 220 ? -9.538  7.857   -11.764 1.00 76.19  ? 220 LYS A CE  1 
ATOM 1682 N NZ  . LYS A 1 220 ? -9.589  7.983   -10.282 1.00 70.58  ? 220 LYS A NZ  1 
ATOM 1683 N N   . LYS A 1 221 ? -7.497  12.165  -9.778  1.00 85.35  ? 221 LYS A N   1 
ATOM 1684 C CA  . LYS A 1 221 ? -6.660  12.401  -8.610  1.00 86.62  ? 221 LYS A CA  1 
ATOM 1685 C C   . LYS A 1 221 ? -5.723  11.222  -8.388  1.00 84.33  ? 221 LYS A C   1 
ATOM 1686 O O   . LYS A 1 221 ? -6.132  10.062  -8.484  1.00 83.03  ? 221 LYS A O   1 
ATOM 1687 C CB  . LYS A 1 221 ? -7.514  12.621  -7.358  1.00 88.43  ? 221 LYS A CB  1 
ATOM 1688 C CG  . LYS A 1 221 ? -8.989  12.911  -7.612  1.00 97.17  ? 221 LYS A CG  1 
ATOM 1689 C CD  . LYS A 1 221 ? -9.216  14.284  -8.224  1.00 94.72  ? 221 LYS A CD  1 
ATOM 1690 C CE  . LYS A 1 221 ? -10.698 14.542  -8.438  1.00 89.32  ? 221 LYS A CE  1 
ATOM 1691 N NZ  . LYS A 1 221 ? -10.952 15.857  -9.084  1.00 85.04  ? 221 LYS A NZ  1 
ATOM 1692 N N   . VAL A 1 222 ? -4.465  11.525  -8.085  1.00 83.38  ? 222 VAL A N   1 
ATOM 1693 C CA  . VAL A 1 222 ? -3.461  10.509  -7.794  1.00 84.33  ? 222 VAL A CA  1 
ATOM 1694 C C   . VAL A 1 222 ? -3.225  10.517  -6.290  1.00 85.68  ? 222 VAL A C   1 
ATOM 1695 O O   . VAL A 1 222 ? -2.676  11.478  -5.741  1.00 91.38  ? 222 VAL A O   1 
ATOM 1696 C CB  . VAL A 1 222 ? -2.158  10.753  -8.564  1.00 83.39  ? 222 VAL A CB  1 
ATOM 1697 C CG1 . VAL A 1 222 ? -1.149  9.667   -8.231  1.00 85.00  ? 222 VAL A CG1 1 
ATOM 1698 C CG2 . VAL A 1 222 ? -2.420  10.811  -10.060 1.00 82.53  ? 222 VAL A CG2 1 
ATOM 1699 N N   . GLU A 1 223 ? -3.639  9.443   -5.620  1.00 82.50  ? 223 GLU A N   1 
ATOM 1700 C CA  . GLU A 1 223 ? -3.525  9.328   -4.177  1.00 84.47  ? 223 GLU A CA  1 
ATOM 1701 C C   . GLU A 1 223 ? -2.518  8.247   -3.823  1.00 86.81  ? 223 GLU A C   1 
ATOM 1702 O O   . GLU A 1 223 ? -2.654  7.109   -4.292  1.00 87.18  ? 223 GLU A O   1 
ATOM 1703 C CB  . GLU A 1 223 ? -4.887  8.995   -3.557  1.00 84.23  ? 223 GLU A CB  1 
ATOM 1704 C CG  . GLU A 1 223 ? -5.978  10.011  -3.865  1.00 83.14  ? 223 GLU A CG  1 
ATOM 1705 C CD  . GLU A 1 223 ? -6.018  11.155  -2.871  1.00 85.14  ? 223 GLU A CD  1 
ATOM 1706 O OE1 . GLU A 1 223 ? -5.251  11.120  -1.887  1.00 83.59  ? 223 GLU A OE1 1 
ATOM 1707 O OE2 . GLU A 1 223 ? -6.821  12.089  -3.076  1.00 87.67  ? 223 GLU A OE2 1 
ATOM 1708 N N   . PRO A 1 224 ? -1.496  8.557   -3.009  1.00 87.42  ? 224 PRO A N   1 
ATOM 1709 C CA  . PRO A 1 224 ? -0.435  7.619   -2.622  1.00 87.72  ? 224 PRO A CA  1 
ATOM 1710 C C   . PRO A 1 224 ? -0.964  6.341   -1.974  1.00 81.67  ? 224 PRO A C   1 
ATOM 1711 O O   . PRO A 1 224 ? -2.094  6.338   -1.487  1.00 82.38  ? 224 PRO A O   1 
ATOM 1712 C CB  . PRO A 1 224 ? 0.395   8.427   -1.621  1.00 88.30  ? 224 PRO A CB  1 
ATOM 1713 C CG  . PRO A 1 224 ? 0.165   9.847   -2.009  1.00 88.49  ? 224 PRO A CG  1 
ATOM 1714 C CD  . PRO A 1 224 ? -1.263  9.906   -2.463  1.00 85.57  ? 224 PRO A CD  1 
ATOM 1715 N N   . ASP B 2 1   ? 11.053  17.574  -58.747 1.00 69.35  ? 1   ASP B N   1 
ATOM 1716 C CA  . ASP B 2 1   ? 12.007  16.580  -59.226 1.00 72.41  ? 1   ASP B CA  1 
ATOM 1717 C C   . ASP B 2 1   ? 13.440  16.920  -58.823 1.00 75.79  ? 1   ASP B C   1 
ATOM 1718 O O   . ASP B 2 1   ? 14.395  16.338  -59.337 1.00 79.60  ? 1   ASP B O   1 
ATOM 1719 C CB  . ASP B 2 1   ? 11.901  16.433  -60.745 1.00 79.93  ? 1   ASP B CB  1 
ATOM 1720 C CG  . ASP B 2 1   ? 11.989  17.762  -61.463 1.00 96.06  ? 1   ASP B CG  1 
ATOM 1721 O OD1 . ASP B 2 1   ? 10.954  18.457  -61.538 1.00 103.51 ? 1   ASP B OD1 1 
ATOM 1722 O OD2 . ASP B 2 1   ? 13.084  18.116  -61.945 1.00 96.86  ? 1   ASP B OD2 1 
ATOM 1723 N N   . ILE B 2 2   ? 13.583  17.871  -57.904 1.00 70.26  ? 2   ILE B N   1 
ATOM 1724 C CA  . ILE B 2 2   ? 14.866  18.187  -57.288 1.00 65.21  ? 2   ILE B CA  1 
ATOM 1725 C C   . ILE B 2 2   ? 14.932  17.454  -55.956 1.00 62.60  ? 2   ILE B C   1 
ATOM 1726 O O   . ILE B 2 2   ? 14.103  17.687  -55.070 1.00 62.58  ? 2   ILE B O   1 
ATOM 1727 C CB  . ILE B 2 2   ? 15.045  19.701  -57.097 1.00 62.96  ? 2   ILE B CB  1 
ATOM 1728 C CG1 . ILE B 2 2   ? 15.151  20.402  -58.454 1.00 68.76  ? 2   ILE B CG1 1 
ATOM 1729 C CG2 . ILE B 2 2   ? 16.263  19.985  -56.226 1.00 63.38  ? 2   ILE B CG2 1 
ATOM 1730 C CD1 . ILE B 2 2   ? 15.929  21.706  -58.421 1.00 68.50  ? 2   ILE B CD1 1 
ATOM 1731 N N   . VAL B 2 3   ? 15.913  16.567  -55.812 1.00 62.23  ? 3   VAL B N   1 
ATOM 1732 C CA  . VAL B 2 3   ? 16.043  15.721  -54.631 1.00 60.68  ? 3   VAL B CA  1 
ATOM 1733 C C   . VAL B 2 3   ? 17.143  16.280  -53.742 1.00 56.35  ? 3   VAL B C   1 
ATOM 1734 O O   . VAL B 2 3   ? 18.232  16.617  -54.223 1.00 61.31  ? 3   VAL B O   1 
ATOM 1735 C CB  . VAL B 2 3   ? 16.339  14.263  -55.018 1.00 52.74  ? 3   VAL B CB  1 
ATOM 1736 C CG1 . VAL B 2 3   ? 16.330  13.378  -53.783 1.00 51.16  ? 3   VAL B CG1 1 
ATOM 1737 C CG2 . VAL B 2 3   ? 15.330  13.771  -56.041 1.00 57.83  ? 3   VAL B CG2 1 
ATOM 1738 N N   . MET B 2 4   ? 16.865  16.369  -52.444 1.00 51.29  ? 4   MET B N   1 
ATOM 1739 C CA  . MET B 2 4   ? 17.814  16.872  -51.459 1.00 56.37  ? 4   MET B CA  1 
ATOM 1740 C C   . MET B 2 4   ? 18.244  15.725  -50.553 1.00 60.23  ? 4   MET B C   1 
ATOM 1741 O O   . MET B 2 4   ? 17.409  15.124  -49.868 1.00 63.30  ? 4   MET B O   1 
ATOM 1742 C CB  . MET B 2 4   ? 17.202  18.005  -50.636 1.00 52.46  ? 4   MET B CB  1 
ATOM 1743 C CG  . MET B 2 4   ? 16.468  19.054  -51.456 1.00 51.18  ? 4   MET B CG  1 
ATOM 1744 S SD  . MET B 2 4   ? 17.594  20.098  -52.401 1.00 53.48  ? 4   MET B SD  1 
ATOM 1745 C CE  . MET B 2 4   ? 18.216  21.175  -51.114 1.00 55.61  ? 4   MET B CE  1 
ATOM 1746 N N   . THR B 2 5   ? 19.541  15.431  -50.544 1.00 58.39  ? 5   THR B N   1 
ATOM 1747 C CA  . THR B 2 5   ? 20.105  14.358  -49.735 1.00 59.28  ? 5   THR B CA  1 
ATOM 1748 C C   . THR B 2 5   ? 21.074  14.955  -48.727 1.00 61.05  ? 5   THR B C   1 
ATOM 1749 O O   . THR B 2 5   ? 22.036  15.631  -49.108 1.00 61.24  ? 5   THR B O   1 
ATOM 1750 C CB  . THR B 2 5   ? 20.810  13.319  -50.610 1.00 64.40  ? 5   THR B CB  1 
ATOM 1751 O OG1 . THR B 2 5   ? 21.617  13.984  -51.589 1.00 70.68  ? 5   THR B OG1 1 
ATOM 1752 C CG2 . THR B 2 5   ? 19.791  12.434  -51.309 1.00 60.01  ? 5   THR B CG2 1 
ATOM 1753 N N   . GLN B 2 6   ? 20.820  14.707  -47.446 1.00 63.30  ? 6   GLN B N   1 
ATOM 1754 C CA  . GLN B 2 6   ? 21.658  15.208  -46.367 1.00 65.59  ? 6   GLN B CA  1 
ATOM 1755 C C   . GLN B 2 6   ? 22.663  14.138  -45.959 1.00 68.19  ? 6   GLN B C   1 
ATOM 1756 O O   . GLN B 2 6   ? 22.331  12.950  -45.911 1.00 67.77  ? 6   GLN B O   1 
ATOM 1757 C CB  . GLN B 2 6   ? 20.802  15.630  -45.171 1.00 61.13  ? 6   GLN B CB  1 
ATOM 1758 C CG  . GLN B 2 6   ? 19.635  16.533  -45.559 1.00 55.47  ? 6   GLN B CG  1 
ATOM 1759 C CD  . GLN B 2 6   ? 18.849  17.032  -44.364 1.00 50.24  ? 6   GLN B CD  1 
ATOM 1760 O OE1 . GLN B 2 6   ? 17.661  17.338  -44.472 1.00 48.62  ? 6   GLN B OE1 1 
ATOM 1761 N NE2 . GLN B 2 6   ? 19.509  17.118  -43.216 1.00 48.80  ? 6   GLN B NE2 1 
ATOM 1762 N N   . SER B 2 7   ? 23.898  14.562  -45.672 1.00 76.63  ? 7   SER B N   1 
ATOM 1763 C CA  . SER B 2 7   ? 24.988  13.612  -45.476 1.00 76.59  ? 7   SER B CA  1 
ATOM 1764 C C   . SER B 2 7   ? 24.859  12.874  -44.141 1.00 76.34  ? 7   SER B C   1 
ATOM 1765 O O   . SER B 2 7   ? 24.555  11.676  -44.157 1.00 82.80  ? 7   SER B O   1 
ATOM 1766 C CB  . SER B 2 7   ? 26.345  14.312  -45.622 1.00 77.36  ? 7   SER B CB  1 
ATOM 1767 O OG  . SER B 2 7   ? 27.397  13.502  -45.133 1.00 79.41  ? 7   SER B OG  1 
ATOM 1768 N N   . PRO B 2 8   ? 25.048  13.513  -42.957 1.00 68.16  ? 8   PRO B N   1 
ATOM 1769 C CA  . PRO B 2 8   ? 24.947  12.746  -41.705 1.00 55.57  ? 8   PRO B CA  1 
ATOM 1770 C C   . PRO B 2 8   ? 23.495  12.562  -41.309 1.00 54.82  ? 8   PRO B C   1 
ATOM 1771 O O   . PRO B 2 8   ? 22.794  13.528  -40.984 1.00 62.12  ? 8   PRO B O   1 
ATOM 1772 C CB  . PRO B 2 8   ? 25.710  13.624  -40.697 1.00 57.07  ? 8   PRO B CB  1 
ATOM 1773 C CG  . PRO B 2 8   ? 26.149  14.866  -41.459 1.00 67.59  ? 8   PRO B CG  1 
ATOM 1774 C CD  . PRO B 2 8   ? 25.269  14.936  -42.658 1.00 65.94  ? 8   PRO B CD  1 
ATOM 1775 N N   . LEU B 2 9   ? 23.026  11.313  -41.336 1.00 49.18  ? 9   LEU B N   1 
ATOM 1776 C CA  . LEU B 2 9   ? 21.632  11.049  -40.997 1.00 49.14  ? 9   LEU B CA  1 
ATOM 1777 C C   . LEU B 2 9   ? 21.373  11.251  -39.508 1.00 49.76  ? 9   LEU B C   1 
ATOM 1778 O O   . LEU B 2 9   ? 20.348  11.823  -39.122 1.00 52.79  ? 9   LEU B O   1 
ATOM 1779 C CB  . LEU B 2 9   ? 21.245  9.636   -41.426 1.00 54.16  ? 9   LEU B CB  1 
ATOM 1780 C CG  . LEU B 2 9   ? 19.742  9.348   -41.441 1.00 53.53  ? 9   LEU B CG  1 
ATOM 1781 C CD1 . LEU B 2 9   ? 18.999  10.402  -42.243 1.00 50.88  ? 9   LEU B CD1 1 
ATOM 1782 C CD2 . LEU B 2 9   ? 19.469  7.960   -41.991 1.00 57.41  ? 9   LEU B CD2 1 
ATOM 1783 N N   . SER B 2 10  ? 22.281  10.780  -38.660 1.00 55.61  ? 10  SER B N   1 
ATOM 1784 C CA  . SER B 2 10  ? 22.217  11.014  -37.227 1.00 48.20  ? 10  SER B CA  1 
ATOM 1785 C C   . SER B 2 10  ? 23.593  11.436  -36.735 1.00 47.99  ? 10  SER B C   1 
ATOM 1786 O O   . SER B 2 10  ? 24.618  10.968  -37.237 1.00 47.78  ? 10  SER B O   1 
ATOM 1787 C CB  . SER B 2 10  ? 21.741  9.767   -36.472 1.00 55.33  ? 10  SER B CB  1 
ATOM 1788 O OG  . SER B 2 10  ? 22.467  8.620   -36.881 1.00 71.28  ? 10  SER B OG  1 
ATOM 1789 N N   . LEU B 2 11  ? 23.609  12.333  -35.753 1.00 48.90  ? 11  LEU B N   1 
ATOM 1790 C CA  . LEU B 2 11  ? 24.857  12.890  -35.243 1.00 48.46  ? 11  LEU B CA  1 
ATOM 1791 C C   . LEU B 2 11  ? 24.757  13.075  -33.739 1.00 48.16  ? 11  LEU B C   1 
ATOM 1792 O O   . LEU B 2 11  ? 23.846  13.753  -33.253 1.00 57.50  ? 11  LEU B O   1 
ATOM 1793 C CB  . LEU B 2 11  ? 25.178  14.227  -35.917 1.00 50.60  ? 11  LEU B CB  1 
ATOM 1794 C CG  . LEU B 2 11  ? 26.587  14.788  -35.722 1.00 53.06  ? 11  LEU B CG  1 
ATOM 1795 C CD1 . LEU B 2 11  ? 27.631  13.707  -35.943 1.00 62.70  ? 11  LEU B CD1 1 
ATOM 1796 C CD2 . LEU B 2 11  ? 26.815  15.958  -36.665 1.00 47.27  ? 11  LEU B CD2 1 
ATOM 1797 N N   . SER B 2 12  ? 25.695  12.484  -33.008 1.00 48.19  ? 12  SER B N   1 
ATOM 1798 C CA  . SER B 2 12  ? 25.864  12.732  -31.582 1.00 55.83  ? 12  SER B CA  1 
ATOM 1799 C C   . SER B 2 12  ? 27.159  13.506  -31.386 1.00 58.48  ? 12  SER B C   1 
ATOM 1800 O O   . SER B 2 12  ? 28.238  13.010  -31.725 1.00 63.83  ? 12  SER B O   1 
ATOM 1801 C CB  . SER B 2 12  ? 25.887  11.430  -30.782 1.00 57.38  ? 12  SER B CB  1 
ATOM 1802 O OG  . SER B 2 12  ? 26.881  10.551  -31.277 1.00 68.42  ? 12  SER B OG  1 
ATOM 1803 N N   . VAL B 2 13  ? 27.049  14.716  -30.846 1.00 53.93  ? 13  VAL B N   1 
ATOM 1804 C CA  . VAL B 2 13  ? 28.189  15.595  -30.626 1.00 54.58  ? 13  VAL B CA  1 
ATOM 1805 C C   . VAL B 2 13  ? 28.252  15.964  -29.152 1.00 59.41  ? 13  VAL B C   1 
ATOM 1806 O O   . VAL B 2 13  ? 27.217  16.149  -28.503 1.00 61.11  ? 13  VAL B O   1 
ATOM 1807 C CB  . VAL B 2 13  ? 28.109  16.859  -31.504 1.00 53.14  ? 13  VAL B CB  1 
ATOM 1808 C CG1 . VAL B 2 13  ? 28.463  16.528  -32.940 1.00 56.10  ? 13  VAL B CG1 1 
ATOM 1809 C CG2 . VAL B 2 13  ? 26.709  17.438  -31.441 1.00 55.48  ? 13  VAL B CG2 1 
ATOM 1810 N N   . ALA B 2 14  ? 29.467  16.072  -28.629 1.00 57.26  ? 14  ALA B N   1 
ATOM 1811 C CA  . ALA B 2 14  ? 29.637  16.437  -27.235 1.00 54.64  ? 14  ALA B CA  1 
ATOM 1812 C C   . ALA B 2 14  ? 29.365  17.928  -27.047 1.00 59.10  ? 14  ALA B C   1 
ATOM 1813 O O   . ALA B 2 14  ? 29.652  18.728  -27.945 1.00 60.57  ? 14  ALA B O   1 
ATOM 1814 C CB  . ALA B 2 14  ? 31.048  16.092  -26.764 1.00 59.12  ? 14  ALA B CB  1 
ATOM 1815 N N   . PRO B 2 15  ? 28.800  18.331  -25.907 1.00 59.83  ? 15  PRO B N   1 
ATOM 1816 C CA  . PRO B 2 15  ? 28.558  19.764  -25.672 1.00 57.78  ? 15  PRO B CA  1 
ATOM 1817 C C   . PRO B 2 15  ? 29.860  20.549  -25.718 1.00 57.29  ? 15  PRO B C   1 
ATOM 1818 O O   . PRO B 2 15  ? 30.819  20.244  -25.006 1.00 58.88  ? 15  PRO B O   1 
ATOM 1819 C CB  . PRO B 2 15  ? 27.917  19.794  -24.277 1.00 56.00  ? 15  PRO B CB  1 
ATOM 1820 C CG  . PRO B 2 15  ? 28.176  18.440  -23.685 1.00 62.63  ? 15  PRO B CG  1 
ATOM 1821 C CD  . PRO B 2 15  ? 28.238  17.494  -24.835 1.00 58.09  ? 15  PRO B CD  1 
ATOM 1822 N N   . GLY B 2 16  ? 29.895  21.554  -26.587 1.00 58.21  ? 16  GLY B N   1 
ATOM 1823 C CA  . GLY B 2 16  ? 31.080  22.349  -26.812 1.00 62.51  ? 16  GLY B CA  1 
ATOM 1824 C C   . GLY B 2 16  ? 31.814  22.036  -28.099 1.00 66.07  ? 16  GLY B C   1 
ATOM 1825 O O   . GLY B 2 16  ? 32.693  22.810  -28.495 1.00 75.74  ? 16  GLY B O   1 
ATOM 1826 N N   . GLU B 2 17  ? 31.484  20.930  -28.762 1.00 60.47  ? 17  GLU B N   1 
ATOM 1827 C CA  . GLU B 2 17  ? 32.141  20.555  -30.002 1.00 61.66  ? 17  GLU B CA  1 
ATOM 1828 C C   . GLU B 2 17  ? 31.327  21.037  -31.200 1.00 59.97  ? 17  GLU B C   1 
ATOM 1829 O O   . GLU B 2 17  ? 30.234  21.591  -31.062 1.00 57.41  ? 17  GLU B O   1 
ATOM 1830 C CB  . GLU B 2 17  ? 32.359  19.044  -30.060 1.00 66.03  ? 17  GLU B CB  1 
ATOM 1831 C CG  . GLU B 2 17  ? 33.704  18.607  -29.523 1.00 66.26  ? 17  GLU B CG  1 
ATOM 1832 C CD  . GLU B 2 17  ? 34.837  18.954  -30.470 1.00 69.39  ? 17  GLU B CD  1 
ATOM 1833 O OE1 . GLU B 2 17  ? 34.581  19.090  -31.686 1.00 74.29  ? 17  GLU B OE1 1 
ATOM 1834 O OE2 . GLU B 2 17  ? 35.985  19.091  -30.000 1.00 60.19  ? 17  GLU B OE2 1 
ATOM 1835 N N   . ALA B 2 18  ? 31.861  20.819  -32.395 1.00 60.60  ? 18  ALA B N   1 
ATOM 1836 C CA  . ALA B 2 18  ? 31.267  21.351  -33.611 1.00 60.56  ? 18  ALA B CA  1 
ATOM 1837 C C   . ALA B 2 18  ? 30.532  20.261  -34.379 1.00 59.04  ? 18  ALA B C   1 
ATOM 1838 O O   . ALA B 2 18  ? 30.960  19.103  -34.403 1.00 66.62  ? 18  ALA B O   1 
ATOM 1839 C CB  . ALA B 2 18  ? 32.335  21.989  -34.501 1.00 64.95  ? 18  ALA B CB  1 
ATOM 1840 N N   . ALA B 2 19  ? 29.417  20.639  -34.996 1.00 53.95  ? 19  ALA B N   1 
ATOM 1841 C CA  . ALA B 2 19  ? 28.650  19.757  -35.860 1.00 54.31  ? 19  ALA B CA  1 
ATOM 1842 C C   . ALA B 2 19  ? 28.568  20.368  -37.251 1.00 56.98  ? 19  ALA B C   1 
ATOM 1843 O O   . ALA B 2 19  ? 28.572  21.593  -37.409 1.00 58.02  ? 19  ALA B O   1 
ATOM 1844 C CB  . ALA B 2 19  ? 27.239  19.515  -35.310 1.00 52.97  ? 19  ALA B CB  1 
ATOM 1845 N N   . SER B 2 20  ? 28.490  19.501  -38.264 1.00 58.59  ? 20  SER B N   1 
ATOM 1846 C CA  . SER B 2 20  ? 28.489  19.934  -39.664 1.00 57.89  ? 20  SER B CA  1 
ATOM 1847 C C   . SER B 2 20  ? 27.525  19.048  -40.452 1.00 53.38  ? 20  SER B C   1 
ATOM 1848 O O   . SER B 2 20  ? 27.924  18.026  -41.018 1.00 57.57  ? 20  SER B O   1 
ATOM 1849 C CB  . SER B 2 20  ? 29.896  19.893  -40.246 1.00 60.20  ? 20  SER B CB  1 
ATOM 1850 O OG  . SER B 2 20  ? 30.773  20.737  -39.516 1.00 71.81  ? 20  SER B OG  1 
ATOM 1851 N N   . ILE B 2 21  ? 26.258  19.448  -40.485 1.00 48.92  ? 21  ILE B N   1 
ATOM 1852 C CA  . ILE B 2 21  ? 25.269  18.784  -41.325 1.00 49.89  ? 21  ILE B CA  1 
ATOM 1853 C C   . ILE B 2 21  ? 25.456  19.258  -42.760 1.00 50.61  ? 21  ILE B C   1 
ATOM 1854 O O   . ILE B 2 21  ? 25.557  20.462  -43.020 1.00 52.13  ? 21  ILE B O   1 
ATOM 1855 C CB  . ILE B 2 21  ? 23.844  19.070  -40.826 1.00 47.46  ? 21  ILE B CB  1 
ATOM 1856 C CG1 . ILE B 2 21  ? 23.711  18.702  -39.348 1.00 47.59  ? 21  ILE B CG1 1 
ATOM 1857 C CG2 . ILE B 2 21  ? 22.824  18.305  -41.658 1.00 47.95  ? 21  ILE B CG2 1 
ATOM 1858 C CD1 . ILE B 2 21  ? 22.408  19.143  -38.718 1.00 47.92  ? 21  ILE B CD1 1 
ATOM 1859 N N   . SER B 2 22  ? 25.511  18.314  -43.693 1.00 50.47  ? 22  SER B N   1 
ATOM 1860 C CA  . SER B 2 22  ? 25.729  18.612  -45.099 1.00 50.00  ? 22  SER B CA  1 
ATOM 1861 C C   . SER B 2 22  ? 24.478  18.287  -45.904 1.00 55.57  ? 22  SER B C   1 
ATOM 1862 O O   . SER B 2 22  ? 23.723  17.373  -45.568 1.00 61.21  ? 22  SER B O   1 
ATOM 1863 C CB  . SER B 2 22  ? 26.923  17.825  -45.646 1.00 53.76  ? 22  SER B CB  1 
ATOM 1864 O OG  . SER B 2 22  ? 27.321  18.316  -46.913 1.00 52.80  ? 22  SER B OG  1 
ATOM 1865 N N   . CYS B 2 23  ? 24.264  19.049  -46.973 1.00 57.70  ? 23  CYS B N   1 
ATOM 1866 C CA  . CYS B 2 23  ? 23.108  18.885  -47.841 1.00 55.34  ? 23  CYS B CA  1 
ATOM 1867 C C   . CYS B 2 23  ? 23.573  18.926  -49.289 1.00 54.03  ? 23  CYS B C   1 
ATOM 1868 O O   . CYS B 2 23  ? 24.574  19.570  -49.616 1.00 53.47  ? 23  CYS B O   1 
ATOM 1869 C CB  . CYS B 2 23  ? 22.057  19.980  -47.575 1.00 52.16  ? 23  CYS B CB  1 
ATOM 1870 S SG  . CYS B 2 23  ? 20.577  19.947  -48.619 1.00 60.30  ? 23  CYS B SG  1 
ATOM 1871 N N   . ARG B 2 24  ? 22.851  18.220  -50.157 1.00 54.78  ? 24  ARG B N   1 
ATOM 1872 C CA  . ARG B 2 24  ? 23.202  18.192  -51.569 1.00 60.16  ? 24  ARG B CA  1 
ATOM 1873 C C   . ARG B 2 24  ? 21.938  18.142  -52.412 1.00 64.48  ? 24  ARG B C   1 
ATOM 1874 O O   . ARG B 2 24  ? 20.973  17.457  -52.062 1.00 66.26  ? 24  ARG B O   1 
ATOM 1875 C CB  . ARG B 2 24  ? 24.104  17.000  -51.911 1.00 60.81  ? 24  ARG B CB  1 
ATOM 1876 C CG  . ARG B 2 24  ? 24.970  17.256  -53.134 1.00 63.53  ? 24  ARG B CG  1 
ATOM 1877 C CD  . ARG B 2 24  ? 25.569  15.987  -53.716 1.00 60.60  ? 24  ARG B CD  1 
ATOM 1878 N NE  . ARG B 2 24  ? 26.727  16.283  -54.552 1.00 70.75  ? 24  ARG B NE  1 
ATOM 1879 C CZ  . ARG B 2 24  ? 26.659  16.769  -55.785 1.00 77.90  ? 24  ARG B CZ  1 
ATOM 1880 N NH1 . ARG B 2 24  ? 25.497  17.023  -56.365 1.00 71.61  ? 24  ARG B NH1 1 
ATOM 1881 N NH2 . ARG B 2 24  ? 27.785  17.009  -56.452 1.00 81.80  ? 24  ARG B NH2 1 
ATOM 1882 N N   . SER B 2 25  ? 21.959  18.868  -53.527 1.00 61.12  ? 25  SER B N   1 
ATOM 1883 C CA  . SER B 2 25  ? 20.845  18.933  -54.458 1.00 56.79  ? 25  SER B CA  1 
ATOM 1884 C C   . SER B 2 25  ? 21.272  18.385  -55.813 1.00 58.19  ? 25  SER B C   1 
ATOM 1885 O O   . SER B 2 25  ? 22.445  18.463  -56.190 1.00 58.97  ? 25  SER B O   1 
ATOM 1886 C CB  . SER B 2 25  ? 20.328  20.372  -54.612 1.00 59.83  ? 25  SER B CB  1 
ATOM 1887 O OG  . SER B 2 25  ? 21.328  21.228  -55.136 1.00 66.79  ? 25  SER B OG  1 
ATOM 1888 N N   . THR B 2 26  ? 20.305  17.821  -56.540 1.00 59.95  ? 26  THR B N   1 
ATOM 1889 C CA  . THR B 2 26  ? 20.593  17.285  -57.866 1.00 59.32  ? 26  THR B CA  1 
ATOM 1890 C C   . THR B 2 26  ? 20.981  18.392  -58.837 1.00 63.03  ? 26  THR B C   1 
ATOM 1891 O O   . THR B 2 26  ? 21.805  18.180  -59.734 1.00 63.65  ? 26  THR B O   1 
ATOM 1892 C CB  . THR B 2 26  ? 19.382  16.521  -58.400 1.00 58.77  ? 26  THR B CB  1 
ATOM 1893 O OG1 . THR B 2 26  ? 18.224  17.364  -58.353 1.00 63.20  ? 26  THR B OG1 1 
ATOM 1894 C CG2 . THR B 2 26  ? 19.127  15.272  -57.571 1.00 54.54  ? 26  THR B CG2 1 
ATOM 1895 N N   . GLN B 2 27  ? 20.394  19.575  -58.676 1.00 64.99  ? 27  GLN B N   1 
ATOM 1896 C CA  . GLN B 2 27  ? 20.601  20.687  -59.587 1.00 61.48  ? 27  GLN B CA  1 
ATOM 1897 C C   . GLN B 2 27  ? 21.007  21.920  -58.792 1.00 60.83  ? 27  GLN B C   1 
ATOM 1898 O O   . GLN B 2 27  ? 20.640  22.072  -57.624 1.00 62.67  ? 27  GLN B O   1 
ATOM 1899 C CB  . GLN B 2 27  ? 19.332  20.965  -60.406 1.00 59.50  ? 27  GLN B CB  1 
ATOM 1900 C CG  . GLN B 2 27  ? 18.835  19.752  -61.186 1.00 70.30  ? 27  GLN B CG  1 
ATOM 1901 C CD  . GLN B 2 27  ? 17.557  20.026  -61.954 1.00 83.89  ? 27  GLN B CD  1 
ATOM 1902 O OE1 . GLN B 2 27  ? 17.265  21.167  -62.309 1.00 95.04  ? 27  GLN B OE1 1 
ATOM 1903 N NE2 . GLN B 2 27  ? 16.790  18.974  -62.219 1.00 79.01  ? 27  GLN B NE2 1 
ATOM 1904 N N   . SER B 2 28  ? 21.773  22.797  -59.438 1.00 62.54  ? 28  SER B N   1 
ATOM 1905 C CA  . SER B 2 28  ? 22.282  23.984  -58.765 1.00 59.70  ? 28  SER B CA  1 
ATOM 1906 C C   . SER B 2 28  ? 21.143  24.908  -58.351 1.00 60.55  ? 28  SER B C   1 
ATOM 1907 O O   . SER B 2 28  ? 20.203  25.144  -59.114 1.00 65.81  ? 28  SER B O   1 
ATOM 1908 C CB  . SER B 2 28  ? 23.263  24.724  -59.676 1.00 53.61  ? 28  SER B CB  1 
ATOM 1909 O OG  . SER B 2 28  ? 22.612  25.247  -60.821 1.00 70.54  ? 28  SER B OG  1 
ATOM 1910 N N   . LEU B 2 29  ? 21.231  25.424  -57.126 1.00 56.54  ? 29  LEU B N   1 
ATOM 1911 C CA  . LEU B 2 29  ? 20.243  26.340  -56.574 1.00 60.86  ? 29  LEU B CA  1 
ATOM 1912 C C   . LEU B 2 29  ? 20.662  27.796  -56.724 1.00 65.98  ? 29  LEU B C   1 
ATOM 1913 O O   . LEU B 2 29  ? 20.044  28.680  -56.123 1.00 66.98  ? 29  LEU B O   1 
ATOM 1914 C CB  . LEU B 2 29  ? 19.999  26.015  -55.100 1.00 58.59  ? 29  LEU B CB  1 
ATOM 1915 C CG  . LEU B 2 29  ? 19.656  24.551  -54.828 1.00 58.48  ? 29  LEU B CG  1 
ATOM 1916 C CD1 . LEU B 2 29  ? 19.594  24.265  -53.331 1.00 51.93  ? 29  LEU B CD1 1 
ATOM 1917 C CD2 . LEU B 2 29  ? 18.354  24.171  -55.517 1.00 62.52  ? 29  LEU B CD2 1 
ATOM 1918 N N   . LEU B 2 30  ? 21.695  28.055  -57.517 1.00 65.27  ? 30  LEU B N   1 
ATOM 1919 C CA  . LEU B 2 30  ? 22.258  29.387  -57.667 1.00 63.63  ? 30  LEU B CA  1 
ATOM 1920 C C   . LEU B 2 30  ? 21.349  30.274  -58.513 1.00 73.22  ? 30  LEU B C   1 
ATOM 1921 O O   . LEU B 2 30  ? 20.629  29.804  -59.398 1.00 74.18  ? 30  LEU B O   1 
ATOM 1922 C CB  . LEU B 2 30  ? 23.639  29.274  -58.312 1.00 62.20  ? 30  LEU B CB  1 
ATOM 1923 C CG  . LEU B 2 30  ? 24.733  30.332  -58.202 1.00 66.30  ? 30  LEU B CG  1 
ATOM 1924 C CD1 . LEU B 2 30  ? 25.421  30.287  -56.853 1.00 73.43  ? 30  LEU B CD1 1 
ATOM 1925 C CD2 . LEU B 2 30  ? 25.737  30.067  -59.304 1.00 60.78  ? 30  LEU B CD2 1 
ATOM 1926 N N   . ASN B 2 31  ? 21.380  31.571  -58.229 1.00 80.08  ? 31  ASN B N   1 
ATOM 1927 C CA  . ASN B 2 31  ? 20.706  32.565  -59.052 1.00 75.96  ? 31  ASN B CA  1 
ATOM 1928 C C   . ASN B 2 31  ? 21.736  33.547  -59.605 1.00 81.63  ? 31  ASN B C   1 
ATOM 1929 O O   . ASN B 2 31  ? 22.930  33.460  -59.305 1.00 79.43  ? 31  ASN B O   1 
ATOM 1930 C CB  . ASN B 2 31  ? 19.583  33.266  -58.273 1.00 75.61  ? 31  ASN B CB  1 
ATOM 1931 C CG  . ASN B 2 31  ? 20.085  34.274  -57.246 1.00 86.57  ? 31  ASN B CG  1 
ATOM 1932 O OD1 . ASN B 2 31  ? 21.284  34.398  -56.997 1.00 92.49  ? 31  ASN B OD1 1 
ATOM 1933 N ND2 . ASN B 2 31  ? 19.154  35.016  -56.658 1.00 85.51  ? 31  ASN B ND2 1 
ATOM 1934 N N   . ARG B 2 32  ? 21.255  34.482  -60.431 1.00 85.01  ? 32  ARG B N   1 
ATOM 1935 C CA  . ARG B 2 32  ? 22.147  35.404  -61.130 1.00 85.49  ? 32  ARG B CA  1 
ATOM 1936 C C   . ARG B 2 32  ? 23.072  36.127  -60.162 1.00 82.31  ? 32  ARG B C   1 
ATOM 1937 O O   . ARG B 2 32  ? 24.277  36.249  -60.407 1.00 79.93  ? 32  ARG B O   1 
ATOM 1938 C CB  . ARG B 2 32  ? 21.340  36.426  -61.932 1.00 89.92  ? 32  ARG B CB  1 
ATOM 1939 C CG  . ARG B 2 32  ? 20.806  35.943  -63.272 1.00 92.86  ? 32  ARG B CG  1 
ATOM 1940 C CD  . ARG B 2 32  ? 19.678  34.942  -63.123 1.00 99.65  ? 32  ARG B CD  1 
ATOM 1941 N NE  . ARG B 2 32  ? 18.609  35.460  -62.279 1.00 104.78 ? 32  ARG B NE  1 
ATOM 1942 C CZ  . ARG B 2 32  ? 17.560  34.755  -61.879 1.00 101.74 ? 32  ARG B CZ  1 
ATOM 1943 N NH1 . ARG B 2 32  ? 17.395  33.493  -62.243 1.00 98.47  ? 32  ARG B NH1 1 
ATOM 1944 N NH2 . ARG B 2 32  ? 16.651  35.331  -61.097 1.00 99.91  ? 32  ARG B NH2 1 
ATOM 1945 N N   . ASN B 2 33  ? 22.516  36.612  -59.050 1.00 81.98  ? 33  ASN B N   1 
ATOM 1946 C CA  . ASN B 2 33  ? 23.304  37.385  -58.097 1.00 84.85  ? 33  ASN B CA  1 
ATOM 1947 C C   . ASN B 2 33  ? 24.429  36.551  -57.503 1.00 86.12  ? 33  ASN B C   1 
ATOM 1948 O O   . ASN B 2 33  ? 25.530  37.060  -57.260 1.00 80.56  ? 33  ASN B O   1 
ATOM 1949 C CB  . ASN B 2 33  ? 22.400  37.909  -56.985 1.00 85.58  ? 33  ASN B CB  1 
ATOM 1950 C CG  . ASN B 2 33  ? 21.089  38.447  -57.509 1.00 93.15  ? 33  ASN B CG  1 
ATOM 1951 O OD1 . ASN B 2 33  ? 20.050  37.796  -57.393 1.00 92.44  ? 33  ASN B OD1 1 
ATOM 1952 N ND2 . ASN B 2 33  ? 21.128  39.636  -58.094 1.00 90.91  ? 33  ASN B ND2 1 
ATOM 1953 N N   . GLY B 2 34  ? 24.173  35.270  -57.268 1.00 86.89  ? 34  GLY B N   1 
ATOM 1954 C CA  . GLY B 2 34  ? 25.114  34.431  -56.560 1.00 81.16  ? 34  GLY B CA  1 
ATOM 1955 C C   . GLY B 2 34  ? 24.461  33.786  -55.361 1.00 80.13  ? 34  GLY B C   1 
ATOM 1956 O O   . GLY B 2 34  ? 25.027  32.874  -54.751 1.00 79.30  ? 34  GLY B O   1 
ATOM 1957 N N   . ASP B 2 35  ? 23.261  34.249  -55.015 1.00 90.28  ? 35  ASP B N   1 
ATOM 1958 C CA  . ASP B 2 35  ? 22.543  33.653  -53.897 1.00 90.28  ? 35  ASP B CA  1 
ATOM 1959 C C   . ASP B 2 35  ? 21.995  32.287  -54.282 1.00 90.12  ? 35  ASP B C   1 
ATOM 1960 O O   . ASP B 2 35  ? 21.643  32.027  -55.437 1.00 90.22  ? 35  ASP B O   1 
ATOM 1961 C CB  . ASP B 2 35  ? 21.393  34.542  -53.424 1.00 91.10  ? 35  ASP B CB  1 
ATOM 1962 C CG  . ASP B 2 35  ? 21.845  35.933  -53.054 1.00 91.64  ? 35  ASP B CG  1 
ATOM 1963 O OD1 . ASP B 2 35  ? 23.058  36.139  -52.870 1.00 93.23  ? 35  ASP B OD1 1 
ATOM 1964 O OD2 . ASP B 2 35  ? 20.974  36.798  -52.862 1.00 92.35  ? 35  ASP B OD2 1 
ATOM 1965 N N   . ASN B 2 36  ? 21.922  31.411  -53.293 1.00 75.41  ? 36  ASN B N   1 
ATOM 1966 C CA  . ASN B 2 36  ? 21.394  30.071  -53.469 1.00 62.35  ? 36  ASN B CA  1 
ATOM 1967 C C   . ASN B 2 36  ? 20.040  29.984  -52.781 1.00 59.93  ? 36  ASN B C   1 
ATOM 1968 O O   . ASN B 2 36  ? 19.801  30.641  -51.765 1.00 62.44  ? 36  ASN B O   1 
ATOM 1969 C CB  . ASN B 2 36  ? 22.364  29.036  -52.900 1.00 61.46  ? 36  ASN B CB  1 
ATOM 1970 C CG  . ASN B 2 36  ? 23.684  29.014  -53.647 1.00 65.14  ? 36  ASN B CG  1 
ATOM 1971 O OD1 . ASN B 2 36  ? 23.904  28.180  -54.527 1.00 67.03  ? 36  ASN B OD1 1 
ATOM 1972 N ND2 . ASN B 2 36  ? 24.563  29.955  -53.317 1.00 69.41  ? 36  ASN B ND2 1 
ATOM 1973 N N   . TYR B 2 37  ? 19.149  29.181  -53.348 1.00 56.37  ? 37  TYR B N   1 
ATOM 1974 C CA  . TYR B 2 37  ? 17.785  29.059  -52.834 1.00 57.17  ? 37  TYR B CA  1 
ATOM 1975 C C   . TYR B 2 37  ? 17.677  27.889  -51.860 1.00 52.41  ? 37  TYR B C   1 
ATOM 1976 O O   . TYR B 2 37  ? 16.960  26.917  -52.090 1.00 53.53  ? 37  TYR B O   1 
ATOM 1977 C CB  . TYR B 2 37  ? 16.799  28.906  -53.986 1.00 62.49  ? 37  TYR B CB  1 
ATOM 1978 C CG  . TYR B 2 37  ? 16.678  30.128  -54.859 1.00 64.24  ? 37  TYR B CG  1 
ATOM 1979 C CD1 . TYR B 2 37  ? 16.078  31.284  -54.382 1.00 67.73  ? 37  TYR B CD1 1 
ATOM 1980 C CD2 . TYR B 2 37  ? 17.151  30.124  -56.164 1.00 62.52  ? 37  TYR B CD2 1 
ATOM 1981 C CE1 . TYR B 2 37  ? 15.961  32.406  -55.176 1.00 74.81  ? 37  TYR B CE1 1 
ATOM 1982 C CE2 . TYR B 2 37  ? 17.037  31.237  -56.965 1.00 68.59  ? 37  TYR B CE2 1 
ATOM 1983 C CZ  . TYR B 2 37  ? 16.443  32.374  -56.468 1.00 77.29  ? 37  TYR B CZ  1 
ATOM 1984 O OH  . TYR B 2 37  ? 16.331  33.483  -57.271 1.00 78.60  ? 37  TYR B OH  1 
ATOM 1985 N N   . LEU B 2 38  ? 18.401  27.997  -50.746 1.00 51.82  ? 38  LEU B N   1 
ATOM 1986 C CA  . LEU B 2 38  ? 18.390  26.956  -49.727 1.00 49.85  ? 38  LEU B CA  1 
ATOM 1987 C C   . LEU B 2 38  ? 18.063  27.563  -48.373 1.00 49.94  ? 38  LEU B C   1 
ATOM 1988 O O   . LEU B 2 38  ? 18.560  28.635  -48.019 1.00 50.37  ? 38  LEU B O   1 
ATOM 1989 C CB  . LEU B 2 38  ? 19.732  26.195  -49.680 1.00 49.35  ? 38  LEU B CB  1 
ATOM 1990 C CG  . LEU B 2 38  ? 19.868  24.909  -48.840 1.00 49.02  ? 38  LEU B CG  1 
ATOM 1991 C CD1 . LEU B 2 38  ? 21.232  24.372  -49.027 1.00 48.59  ? 38  LEU B CD1 1 
ATOM 1992 C CD2 . LEU B 2 38  ? 19.671  25.074  -47.337 1.00 49.01  ? 38  LEU B CD2 1 
ATOM 1993 N N   . GLU B 2 39  ? 17.228  26.853  -47.622 1.00 49.95  ? 39  GLU B N   1 
ATOM 1994 C CA  . GLU B 2 39  ? 16.816  27.249  -46.291 1.00 50.04  ? 39  GLU B CA  1 
ATOM 1995 C C   . GLU B 2 39  ? 16.973  26.055  -45.357 1.00 49.73  ? 39  GLU B C   1 
ATOM 1996 O O   . GLU B 2 39  ? 16.762  24.906  -45.754 1.00 50.35  ? 39  GLU B O   1 
ATOM 1997 C CB  . GLU B 2 39  ? 15.369  27.753  -46.314 1.00 50.49  ? 39  GLU B CB  1 
ATOM 1998 C CG  . GLU B 2 39  ? 15.196  29.016  -47.163 1.00 50.92  ? 39  GLU B CG  1 
ATOM 1999 C CD  . GLU B 2 39  ? 13.773  29.537  -47.187 1.00 53.37  ? 39  GLU B CD  1 
ATOM 2000 O OE1 . GLU B 2 39  ? 12.853  28.770  -46.843 1.00 54.81  ? 39  GLU B OE1 1 
ATOM 2001 O OE2 . GLU B 2 39  ? 13.572  30.707  -47.581 1.00 51.73  ? 39  GLU B OE2 1 
ATOM 2002 N N   . TRP B 2 40  ? 17.362  26.333  -44.115 1.00 49.64  ? 40  TRP B N   1 
ATOM 2003 C CA  . TRP B 2 40  ? 17.558  25.306  -43.100 1.00 49.40  ? 40  TRP B CA  1 
ATOM 2004 C C   . TRP B 2 40  ? 16.498  25.439  -42.017 1.00 49.64  ? 40  TRP B C   1 
ATOM 2005 O O   . TRP B 2 40  ? 16.273  26.535  -41.492 1.00 49.88  ? 40  TRP B O   1 
ATOM 2006 C CB  . TRP B 2 40  ? 18.954  25.390  -42.477 1.00 49.12  ? 40  TRP B CB  1 
ATOM 2007 C CG  . TRP B 2 40  ? 20.078  24.994  -43.394 1.00 48.80  ? 40  TRP B CG  1 
ATOM 2008 C CD1 . TRP B 2 40  ? 20.843  25.821  -44.163 1.00 48.77  ? 40  TRP B CD1 1 
ATOM 2009 C CD2 . TRP B 2 40  ? 20.571  23.667  -43.620 1.00 48.50  ? 40  TRP B CD2 1 
ATOM 2010 N NE1 . TRP B 2 40  ? 21.778  25.091  -44.857 1.00 48.43  ? 40  TRP B NE1 1 
ATOM 2011 C CE2 . TRP B 2 40  ? 21.630  23.767  -44.543 1.00 48.27  ? 40  TRP B CE2 1 
ATOM 2012 C CE3 . TRP B 2 40  ? 20.217  22.405  -43.133 1.00 48.42  ? 40  TRP B CE3 1 
ATOM 2013 C CZ2 . TRP B 2 40  ? 22.337  22.654  -44.989 1.00 47.96  ? 40  TRP B CZ2 1 
ATOM 2014 C CZ3 . TRP B 2 40  ? 20.920  21.304  -43.576 1.00 48.14  ? 40  TRP B CZ3 1 
ATOM 2015 C CH2 . TRP B 2 40  ? 21.969  21.435  -44.492 1.00 47.91  ? 40  TRP B CH2 1 
ATOM 2016 N N   . TYR B 2 41  ? 15.862  24.323  -41.677 1.00 49.60  ? 41  TYR B N   1 
ATOM 2017 C CA  . TYR B 2 41  ? 14.842  24.293  -40.644 1.00 49.79  ? 41  TYR B CA  1 
ATOM 2018 C C   . TYR B 2 41  ? 15.215  23.285  -39.567 1.00 49.60  ? 41  TYR B C   1 
ATOM 2019 O O   . TYR B 2 41  ? 15.848  22.261  -39.838 1.00 49.95  ? 41  TYR B O   1 
ATOM 2020 C CB  . TYR B 2 41  ? 13.465  23.959  -41.226 1.00 50.02  ? 41  TYR B CB  1 
ATOM 2021 C CG  . TYR B 2 41  ? 12.966  24.988  -42.214 1.00 50.30  ? 41  TYR B CG  1 
ATOM 2022 C CD1 . TYR B 2 41  ? 13.302  24.908  -43.558 1.00 52.25  ? 41  TYR B CD1 1 
ATOM 2023 C CD2 . TYR B 2 41  ? 12.174  26.050  -41.799 1.00 50.62  ? 41  TYR B CD2 1 
ATOM 2024 C CE1 . TYR B 2 41  ? 12.851  25.850  -44.465 1.00 52.04  ? 41  TYR B CE1 1 
ATOM 2025 C CE2 . TYR B 2 41  ? 11.719  26.995  -42.694 1.00 50.93  ? 41  TYR B CE2 1 
ATOM 2026 C CZ  . TYR B 2 41  ? 12.060  26.892  -44.025 1.00 50.91  ? 41  TYR B CZ  1 
ATOM 2027 O OH  . TYR B 2 41  ? 11.607  27.837  -44.915 1.00 53.85  ? 41  TYR B OH  1 
ATOM 2028 N N   . LEU B 2 42  ? 14.815  23.593  -38.337 1.00 49.74  ? 42  LEU B N   1 
ATOM 2029 C CA  . LEU B 2 42  ? 15.099  22.766  -37.174 1.00 50.95  ? 42  LEU B CA  1 
ATOM 2030 C C   . LEU B 2 42  ? 13.776  22.455  -36.495 1.00 52.12  ? 42  LEU B C   1 
ATOM 2031 O O   . LEU B 2 42  ? 13.075  23.372  -36.054 1.00 50.48  ? 42  LEU B O   1 
ATOM 2032 C CB  . LEU B 2 42  ? 16.050  23.489  -36.213 1.00 51.32  ? 42  LEU B CB  1 
ATOM 2033 C CG  . LEU B 2 42  ? 16.759  22.796  -35.042 1.00 55.16  ? 42  LEU B CG  1 
ATOM 2034 C CD1 . LEU B 2 42  ? 17.607  23.827  -34.314 1.00 55.39  ? 42  LEU B CD1 1 
ATOM 2035 C CD2 . LEU B 2 42  ? 15.826  22.094  -34.062 1.00 55.67  ? 42  LEU B CD2 1 
ATOM 2036 N N   . ARG B 2 43  ? 13.439  21.172  -36.402 1.00 53.91  ? 43  ARG B N   1 
ATOM 2037 C CA  . ARG B 2 43  ? 12.242  20.726  -35.692 1.00 59.05  ? 43  ARG B CA  1 
ATOM 2038 C C   . ARG B 2 43  ? 12.683  20.151  -34.350 1.00 71.42  ? 43  ARG B C   1 
ATOM 2039 O O   . ARG B 2 43  ? 13.159  19.015  -34.273 1.00 63.31  ? 43  ARG B O   1 
ATOM 2040 C CB  . ARG B 2 43  ? 11.462  19.698  -36.504 1.00 54.68  ? 43  ARG B CB  1 
ATOM 2041 C CG  . ARG B 2 43  ? 10.180  19.242  -35.823 1.00 57.87  ? 43  ARG B CG  1 
ATOM 2042 C CD  . ARG B 2 43  ? 9.244   18.552  -36.797 1.00 55.14  ? 43  ARG B CD  1 
ATOM 2043 N NE  . ARG B 2 43  ? 9.530   17.127  -36.901 1.00 57.53  ? 43  ARG B NE  1 
ATOM 2044 C CZ  . ARG B 2 43  ? 9.048   16.209  -36.075 1.00 62.32  ? 43  ARG B CZ  1 
ATOM 2045 N NH1 . ARG B 2 43  ? 8.244   16.533  -35.076 1.00 59.14  ? 43  ARG B NH1 1 
ATOM 2046 N NH2 . ARG B 2 43  ? 9.380   14.933  -36.258 1.00 76.92  ? 43  ARG B NH2 1 
ATOM 2047 N N   . ARG B 2 44  ? 12.522  20.943  -33.294 1.00 83.77  ? 44  ARG B N   1 
ATOM 2048 C CA  . ARG B 2 44  ? 12.859  20.505  -31.952 1.00 81.19  ? 44  ARG B CA  1 
ATOM 2049 C C   . ARG B 2 44  ? 11.914  19.386  -31.512 1.00 81.26  ? 44  ARG B C   1 
ATOM 2050 O O   . ARG B 2 44  ? 10.852  19.191  -32.108 1.00 81.68  ? 44  ARG B O   1 
ATOM 2051 C CB  . ARG B 2 44  ? 12.788  21.691  -30.991 1.00 81.85  ? 44  ARG B CB  1 
ATOM 2052 C CG  . ARG B 2 44  ? 14.101  22.448  -30.863 1.00 81.94  ? 44  ARG B CG  1 
ATOM 2053 C CD  . ARG B 2 44  ? 14.196  23.207  -29.549 1.00 91.40  ? 44  ARG B CD  1 
ATOM 2054 N NE  . ARG B 2 44  ? 14.073  24.646  -29.747 1.00 92.43  ? 44  ARG B NE  1 
ATOM 2055 C CZ  . ARG B 2 44  ? 13.072  25.384  -29.287 1.00 92.44  ? 44  ARG B CZ  1 
ATOM 2056 N NH1 . ARG B 2 44  ? 12.089  24.852  -28.579 1.00 91.51  ? 44  ARG B NH1 1 
ATOM 2057 N NH2 . ARG B 2 44  ? 13.056  26.689  -29.544 1.00 97.13  ? 44  ARG B NH2 1 
ATOM 2058 N N   . PRO B 2 45  ? 12.288  18.616  -30.473 1.00 79.07  ? 45  PRO B N   1 
ATOM 2059 C CA  . PRO B 2 45  ? 11.401  17.537  -30.014 1.00 73.97  ? 45  PRO B CA  1 
ATOM 2060 C C   . PRO B 2 45  ? 10.063  18.043  -29.497 1.00 73.56  ? 45  PRO B C   1 
ATOM 2061 O O   . PRO B 2 45  ? 9.996   18.721  -28.466 1.00 71.17  ? 45  PRO B O   1 
ATOM 2062 C CB  . PRO B 2 45  ? 12.217  16.863  -28.904 1.00 71.03  ? 45  PRO B CB  1 
ATOM 2063 C CG  . PRO B 2 45  ? 13.144  17.925  -28.422 1.00 70.54  ? 45  PRO B CG  1 
ATOM 2064 C CD  . PRO B 2 45  ? 13.513  18.694  -29.656 1.00 76.53  ? 45  PRO B CD  1 
ATOM 2065 N N   . GLY B 2 46  ? 8.989   17.722  -30.221 1.00 73.27  ? 46  GLY B N   1 
ATOM 2066 C CA  . GLY B 2 46  ? 7.644   18.071  -29.830 1.00 74.61  ? 46  GLY B CA  1 
ATOM 2067 C C   . GLY B 2 46  ? 7.101   19.335  -30.466 1.00 71.59  ? 46  GLY B C   1 
ATOM 2068 O O   . GLY B 2 46  ? 5.882   19.541  -30.452 1.00 71.01  ? 46  GLY B O   1 
ATOM 2069 N N   . ARG B 2 47  ? 7.963   20.179  -31.026 1.00 71.98  ? 47  ARG B N   1 
ATOM 2070 C CA  . ARG B 2 47  ? 7.543   21.459  -31.568 1.00 73.67  ? 47  ARG B CA  1 
ATOM 2071 C C   . ARG B 2 47  ? 7.445   21.403  -33.091 1.00 70.68  ? 47  ARG B C   1 
ATOM 2072 O O   . ARG B 2 47  ? 7.770   20.401  -33.733 1.00 70.99  ? 47  ARG B O   1 
ATOM 2073 C CB  . ARG B 2 47  ? 8.502   22.568  -31.131 1.00 76.59  ? 47  ARG B CB  1 
ATOM 2074 C CG  . ARG B 2 47  ? 8.740   22.638  -29.634 1.00 81.63  ? 47  ARG B CG  1 
ATOM 2075 C CD  . ARG B 2 47  ? 8.980   24.072  -29.191 1.00 84.72  ? 47  ARG B CD  1 
ATOM 2076 N NE  . ARG B 2 47  ? 8.957   24.209  -27.740 1.00 93.67  ? 47  ARG B NE  1 
ATOM 2077 C CZ  . ARG B 2 47  ? 9.093   25.358  -27.092 1.00 100.13 ? 47  ARG B CZ  1 
ATOM 2078 N NH1 . ARG B 2 47  ? 9.264   26.500  -27.738 1.00 101.24 ? 47  ARG B NH1 1 
ATOM 2079 N NH2 . ARG B 2 47  ? 9.060   25.361  -25.761 1.00 98.89  ? 47  ARG B NH2 1 
ATOM 2080 N N   . SER B 2 48  ? 6.987   22.506  -33.666 1.00 61.33  ? 48  SER B N   1 
ATOM 2081 C CA  . SER B 2 48  ? 6.898   22.681  -35.108 1.00 54.43  ? 48  SER B CA  1 
ATOM 2082 C C   . SER B 2 48  ? 8.228   23.180  -35.652 1.00 54.08  ? 48  SER B C   1 
ATOM 2083 O O   . SER B 2 48  ? 9.115   23.581  -34.895 1.00 62.43  ? 48  SER B O   1 
ATOM 2084 C CB  . SER B 2 48  ? 5.761   23.648  -35.434 1.00 53.38  ? 48  SER B CB  1 
ATOM 2085 O OG  . SER B 2 48  ? 5.819   24.807  -34.622 1.00 62.65  ? 48  SER B OG  1 
ATOM 2086 N N   . PRO B 2 49  ? 8.417   23.147  -36.974 1.00 50.79  ? 49  PRO B N   1 
ATOM 2087 C CA  . PRO B 2 49  ? 9.677   23.634  -37.546 1.00 50.64  ? 49  PRO B CA  1 
ATOM 2088 C C   . PRO B 2 49  ? 9.936   25.101  -37.235 1.00 51.02  ? 49  PRO B C   1 
ATOM 2089 O O   . PRO B 2 49  ? 9.014   25.911  -37.107 1.00 51.10  ? 49  PRO B O   1 
ATOM 2090 C CB  . PRO B 2 49  ? 9.486   23.411  -39.050 1.00 50.65  ? 49  PRO B CB  1 
ATOM 2091 C CG  . PRO B 2 49  ? 8.575   22.245  -39.117 1.00 50.67  ? 49  PRO B CG  1 
ATOM 2092 C CD  . PRO B 2 49  ? 7.602   22.458  -37.991 1.00 54.77  ? 49  PRO B CD  1 
ATOM 2093 N N   . GLN B 2 50  ? 11.218  25.429  -37.102 1.00 50.67  ? 50  GLN B N   1 
ATOM 2094 C CA  . GLN B 2 50  ? 11.694  26.798  -36.989 1.00 50.83  ? 50  GLN B CA  1 
ATOM 2095 C C   . GLN B 2 50  ? 12.680  27.071  -38.116 1.00 50.69  ? 50  GLN B C   1 
ATOM 2096 O O   . GLN B 2 50  ? 13.309  26.156  -38.650 1.00 50.73  ? 50  GLN B O   1 
ATOM 2097 C CB  . GLN B 2 50  ? 12.369  27.054  -35.637 1.00 54.63  ? 50  GLN B CB  1 
ATOM 2098 C CG  . GLN B 2 50  ? 11.597  26.537  -34.439 1.00 62.10  ? 50  GLN B CG  1 
ATOM 2099 C CD  . GLN B 2 50  ? 12.447  26.500  -33.186 1.00 65.41  ? 50  GLN B CD  1 
ATOM 2100 O OE1 . GLN B 2 50  ? 12.111  25.829  -32.212 1.00 72.13  ? 50  GLN B OE1 1 
ATOM 2101 N NE2 . GLN B 2 50  ? 13.556  27.229  -33.205 1.00 56.92  ? 50  GLN B NE2 1 
ATOM 2102 N N   . LEU B 2 51  ? 12.816  28.344  -38.474 1.00 50.92  ? 51  LEU B N   1 
ATOM 2103 C CA  . LEU B 2 51  ? 13.742  28.752  -39.522 1.00 50.83  ? 51  LEU B CA  1 
ATOM 2104 C C   . LEU B 2 51  ? 15.096  29.091  -38.912 1.00 50.66  ? 51  LEU B C   1 
ATOM 2105 O O   . LEU B 2 51  ? 15.175  29.857  -37.946 1.00 50.86  ? 51  LEU B O   1 
ATOM 2106 C CB  . LEU B 2 51  ? 13.192  29.951  -40.300 1.00 51.21  ? 51  LEU B CB  1 
ATOM 2107 C CG  . LEU B 2 51  ? 14.184  30.686  -41.209 1.00 51.21  ? 51  LEU B CG  1 
ATOM 2108 C CD1 . LEU B 2 51  ? 14.493  29.852  -42.439 1.00 50.96  ? 51  LEU B CD1 1 
ATOM 2109 C CD2 . LEU B 2 51  ? 13.662  32.058  -41.614 1.00 51.68  ? 51  LEU B CD2 1 
ATOM 2110 N N   . LEU B 2 52  ? 16.155  28.508  -39.472 1.00 50.32  ? 52  LEU B N   1 
ATOM 2111 C CA  . LEU B 2 52  ? 17.525  28.803  -39.062 1.00 50.15  ? 52  LEU B CA  1 
ATOM 2112 C C   . LEU B 2 52  ? 18.219  29.661  -40.113 1.00 50.17  ? 52  LEU B C   1 
ATOM 2113 O O   . LEU B 2 52  ? 18.539  30.823  -39.851 1.00 50.40  ? 52  LEU B O   1 
ATOM 2114 C CB  . LEU B 2 52  ? 18.308  27.510  -38.810 1.00 49.74  ? 52  LEU B CB  1 
ATOM 2115 C CG  . LEU B 2 52  ? 17.916  26.610  -37.634 1.00 49.71  ? 52  LEU B CG  1 
ATOM 2116 C CD1 . LEU B 2 52  ? 19.034  25.629  -37.297 1.00 49.37  ? 52  LEU B CD1 1 
ATOM 2117 C CD2 . LEU B 2 52  ? 17.568  27.451  -36.422 1.00 50.01  ? 52  LEU B CD2 1 
ATOM 2118 N N   . ILE B 2 53  ? 18.454  29.121  -41.304 1.00 49.97  ? 53  ILE B N   1 
ATOM 2119 C CA  . ILE B 2 53  ? 19.194  29.802  -42.357 1.00 49.96  ? 53  ILE B CA  1 
ATOM 2120 C C   . ILE B 2 53  ? 18.273  29.977  -43.555 1.00 50.21  ? 53  ILE B C   1 
ATOM 2121 O O   . ILE B 2 53  ? 17.456  29.099  -43.851 1.00 50.19  ? 53  ILE B O   1 
ATOM 2122 C CB  . ILE B 2 53  ? 20.461  29.010  -42.749 1.00 49.50  ? 53  ILE B CB  1 
ATOM 2123 C CG1 . ILE B 2 53  ? 21.406  28.866  -41.554 1.00 49.30  ? 53  ILE B CG1 1 
ATOM 2124 C CG2 . ILE B 2 53  ? 21.188  29.686  -43.897 1.00 49.49  ? 53  ILE B CG2 1 
ATOM 2125 C CD1 . ILE B 2 53  ? 21.618  30.141  -40.773 1.00 49.58  ? 53  ILE B CD1 1 
ATOM 2126 N N   . TYR B 2 54  ? 18.393  31.118  -44.234 1.00 50.48  ? 54  TYR B N   1 
ATOM 2127 C CA  . TYR B 2 54  ? 17.723  31.336  -45.507 1.00 50.74  ? 54  TYR B CA  1 
ATOM 2128 C C   . TYR B 2 54  ? 18.706  31.965  -46.484 1.00 50.73  ? 54  TYR B C   1 
ATOM 2129 O O   . TYR B 2 54  ? 19.645  32.658  -46.083 1.00 50.68  ? 54  TYR B O   1 
ATOM 2130 C CB  . TYR B 2 54  ? 16.450  32.204  -45.346 1.00 51.27  ? 54  TYR B CB  1 
ATOM 2131 C CG  . TYR B 2 54  ? 16.647  33.639  -44.883 1.00 51.62  ? 54  TYR B CG  1 
ATOM 2132 C CD1 . TYR B 2 54  ? 17.196  34.604  -45.722 1.00 51.84  ? 54  TYR B CD1 1 
ATOM 2133 C CD2 . TYR B 2 54  ? 16.280  34.026  -43.601 1.00 51.77  ? 54  TYR B CD2 1 
ATOM 2134 C CE1 . TYR B 2 54  ? 17.362  35.912  -45.300 1.00 52.22  ? 54  TYR B CE1 1 
ATOM 2135 C CE2 . TYR B 2 54  ? 16.450  35.329  -43.168 1.00 52.14  ? 54  TYR B CE2 1 
ATOM 2136 C CZ  . TYR B 2 54  ? 16.992  36.267  -44.020 1.00 52.37  ? 54  TYR B CZ  1 
ATOM 2137 O OH  . TYR B 2 54  ? 17.161  37.564  -43.591 1.00 52.78  ? 54  TYR B OH  1 
ATOM 2138 N N   . LEU B 2 55  ? 18.482  31.701  -47.772 1.00 50.79  ? 55  LEU B N   1 
ATOM 2139 C CA  . LEU B 2 55  ? 19.363  32.163  -48.847 1.00 50.77  ? 55  LEU B CA  1 
ATOM 2140 C C   . LEU B 2 55  ? 20.797  31.677  -48.642 1.00 50.25  ? 55  LEU B C   1 
ATOM 2141 O O   . LEU B 2 55  ? 21.762  32.359  -48.987 1.00 50.21  ? 55  LEU B O   1 
ATOM 2142 C CB  . LEU B 2 55  ? 19.316  33.686  -48.996 1.00 53.97  ? 55  LEU B CB  1 
ATOM 2143 C CG  . LEU B 2 55  ? 18.121  34.225  -49.785 1.00 51.81  ? 55  LEU B CG  1 
ATOM 2144 C CD1 . LEU B 2 55  ? 18.149  35.741  -49.835 1.00 52.31  ? 55  LEU B CD1 1 
ATOM 2145 C CD2 . LEU B 2 55  ? 18.099  33.647  -51.195 1.00 60.12  ? 55  LEU B CD2 1 
ATOM 2146 N N   . GLY B 2 56  ? 20.940  30.486  -48.076 1.00 49.86  ? 56  GLY B N   1 
ATOM 2147 C CA  . GLY B 2 56  ? 22.235  29.842  -48.002 1.00 49.78  ? 56  GLY B CA  1 
ATOM 2148 C C   . GLY B 2 56  ? 23.050  30.192  -46.776 1.00 51.56  ? 56  GLY B C   1 
ATOM 2149 O O   . GLY B 2 56  ? 23.648  29.308  -46.157 1.00 48.83  ? 56  GLY B O   1 
ATOM 2150 N N   . SER B 2 57  ? 23.084  31.474  -46.409 1.00 51.91  ? 57  SER B N   1 
ATOM 2151 C CA  . SER B 2 57  ? 23.957  31.939  -45.338 1.00 52.91  ? 57  SER B CA  1 
ATOM 2152 C C   . SER B 2 57  ? 23.296  32.871  -44.335 1.00 53.30  ? 57  SER B C   1 
ATOM 2153 O O   . SER B 2 57  ? 23.818  33.005  -43.221 1.00 53.90  ? 57  SER B O   1 
ATOM 2154 C CB  . SER B 2 57  ? 25.184  32.656  -45.923 1.00 54.39  ? 57  SER B CB  1 
ATOM 2155 O OG  . SER B 2 57  ? 24.791  33.713  -46.782 1.00 52.86  ? 57  SER B OG  1 
ATOM 2156 N N   . GLU B 2 58  ? 22.188  33.519  -44.677 1.00 55.57  ? 58  GLU B N   1 
ATOM 2157 C CA  . GLU B 2 58  ? 21.608  34.534  -43.810 1.00 55.85  ? 58  GLU B CA  1 
ATOM 2158 C C   . GLU B 2 58  ? 20.902  33.895  -42.620 1.00 55.52  ? 58  GLU B C   1 
ATOM 2159 O O   . GLU B 2 58  ? 20.042  33.024  -42.785 1.00 54.96  ? 58  GLU B O   1 
ATOM 2160 C CB  . GLU B 2 58  ? 20.640  35.410  -44.598 1.00 56.91  ? 58  GLU B CB  1 
ATOM 2161 C CG  . GLU B 2 58  ? 21.296  36.197  -45.718 1.00 62.03  ? 58  GLU B CG  1 
ATOM 2162 C CD  . GLU B 2 58  ? 22.495  36.991  -45.241 1.00 68.19  ? 58  GLU B CD  1 
ATOM 2163 O OE1 . GLU B 2 58  ? 22.289  38.070  -44.646 1.00 71.48  ? 58  GLU B OE1 1 
ATOM 2164 O OE2 . GLU B 2 58  ? 23.640  36.549  -45.473 1.00 67.02  ? 58  GLU B OE2 1 
ATOM 2165 N N   . ARG B 2 59  ? 21.272  34.333  -41.419 1.00 53.31  ? 59  ARG B N   1 
ATOM 2166 C CA  . ARG B 2 59  ? 20.646  33.829  -40.207 1.00 50.81  ? 59  ARG B CA  1 
ATOM 2167 C C   . ARG B 2 59  ? 19.258  34.431  -40.029 1.00 51.28  ? 59  ARG B C   1 
ATOM 2168 O O   . ARG B 2 59  ? 19.002  35.583  -40.389 1.00 53.34  ? 59  ARG B O   1 
ATOM 2169 C CB  . ARG B 2 59  ? 21.507  34.150  -38.984 1.00 50.81  ? 59  ARG B CB  1 
ATOM 2170 C CG  . ARG B 2 59  ? 22.263  32.963  -38.408 1.00 51.65  ? 59  ARG B CG  1 
ATOM 2171 C CD  . ARG B 2 59  ? 23.251  33.410  -37.342 1.00 59.28  ? 59  ARG B CD  1 
ATOM 2172 N NE  . ARG B 2 59  ? 24.610  33.486  -37.864 1.00 62.31  ? 59  ARG B NE  1 
ATOM 2173 C CZ  . ARG B 2 59  ? 25.417  34.526  -37.701 1.00 69.32  ? 59  ARG B CZ  1 
ATOM 2174 N NH1 . ARG B 2 59  ? 25.031  35.602  -37.033 1.00 69.73  ? 59  ARG B NH1 1 
ATOM 2175 N NH2 . ARG B 2 59  ? 26.638  34.487  -38.226 1.00 68.35  ? 59  ARG B NH2 1 
ATOM 2176 N N   . ALA B 2 60  ? 18.357  33.635  -39.465 1.00 51.23  ? 60  ALA B N   1 
ATOM 2177 C CA  . ALA B 2 60  ? 17.036  34.130  -39.123 1.00 51.65  ? 60  ALA B CA  1 
ATOM 2178 C C   . ALA B 2 60  ? 17.103  34.962  -37.844 1.00 54.65  ? 60  ALA B C   1 
ATOM 2179 O O   . ALA B 2 60  ? 18.137  35.046  -37.176 1.00 59.44  ? 60  ALA B O   1 
ATOM 2180 C CB  . ALA B 2 60  ? 16.054  32.971  -38.964 1.00 51.49  ? 60  ALA B CB  1 
ATOM 2181 N N   . LEU B 2 61  ? 15.980  35.589  -37.505 1.00 58.61  ? 61  LEU B N   1 
ATOM 2182 C CA  . LEU B 2 61  ? 15.911  36.408  -36.303 1.00 57.90  ? 61  LEU B CA  1 
ATOM 2183 C C   . LEU B 2 61  ? 15.791  35.515  -35.074 1.00 60.24  ? 61  LEU B C   1 
ATOM 2184 O O   . LEU B 2 61  ? 14.968  34.594  -35.040 1.00 58.24  ? 61  LEU B O   1 
ATOM 2185 C CB  . LEU B 2 61  ? 14.734  37.378  -36.378 1.00 56.89  ? 61  LEU B CB  1 
ATOM 2186 C CG  . LEU B 2 61  ? 15.037  38.796  -35.887 1.00 53.76  ? 61  LEU B CG  1 
ATOM 2187 C CD1 . LEU B 2 61  ? 16.195  39.395  -36.671 1.00 53.76  ? 61  LEU B CD1 1 
ATOM 2188 C CD2 . LEU B 2 61  ? 13.803  39.677  -35.989 1.00 55.75  ? 61  LEU B CD2 1 
ATOM 2189 N N   . GLY B 2 62  ? 16.616  35.788  -34.067 1.00 69.58  ? 62  GLY B N   1 
ATOM 2190 C CA  . GLY B 2 62  ? 16.668  34.953  -32.888 1.00 69.00  ? 62  GLY B CA  1 
ATOM 2191 C C   . GLY B 2 62  ? 17.509  33.705  -33.025 1.00 68.09  ? 62  GLY B C   1 
ATOM 2192 O O   . GLY B 2 62  ? 17.468  32.851  -32.132 1.00 73.35  ? 62  GLY B O   1 
ATOM 2193 N N   . VAL B 2 63  ? 18.265  33.566  -34.106 1.00 63.29  ? 63  VAL B N   1 
ATOM 2194 C CA  . VAL B 2 63  ? 19.120  32.404  -34.334 1.00 62.18  ? 63  VAL B CA  1 
ATOM 2195 C C   . VAL B 2 63  ? 20.528  32.762  -33.866 1.00 61.61  ? 63  VAL B C   1 
ATOM 2196 O O   . VAL B 2 63  ? 21.103  33.738  -34.373 1.00 65.09  ? 63  VAL B O   1 
ATOM 2197 C CB  . VAL B 2 63  ? 19.123  31.985  -35.811 1.00 54.56  ? 63  VAL B CB  1 
ATOM 2198 C CG1 . VAL B 2 63  ? 20.292  31.059  -36.096 1.00 55.42  ? 63  VAL B CG1 1 
ATOM 2199 C CG2 . VAL B 2 63  ? 17.807  31.317  -36.177 1.00 54.59  ? 63  VAL B CG2 1 
ATOM 2200 N N   . PRO B 2 64  ? 21.106  32.025  -32.919 1.00 54.24  ? 64  PRO B N   1 
ATOM 2201 C CA  . PRO B 2 64  ? 22.406  32.416  -32.361 1.00 57.04  ? 64  PRO B CA  1 
ATOM 2202 C C   . PRO B 2 64  ? 23.513  32.411  -33.404 1.00 59.56  ? 64  PRO B C   1 
ATOM 2203 O O   . PRO B 2 64  ? 23.381  31.880  -34.509 1.00 60.28  ? 64  PRO B O   1 
ATOM 2204 C CB  . PRO B 2 64  ? 22.642  31.348  -31.292 1.00 62.73  ? 64  PRO B CB  1 
ATOM 2205 C CG  . PRO B 2 64  ? 21.256  31.042  -30.825 1.00 65.05  ? 64  PRO B CG  1 
ATOM 2206 C CD  . PRO B 2 64  ? 20.503  30.936  -32.132 1.00 55.33  ? 64  PRO B CD  1 
ATOM 2207 N N   . ASP B 2 65  ? 24.642  33.013  -33.019 1.00 63.19  ? 65  ASP B N   1 
ATOM 2208 C CA  . ASP B 2 65  ? 25.785  33.127  -33.917 1.00 63.56  ? 65  ASP B CA  1 
ATOM 2209 C C   . ASP B 2 65  ? 26.392  31.773  -34.254 1.00 64.34  ? 65  ASP B C   1 
ATOM 2210 O O   . ASP B 2 65  ? 27.088  31.652  -35.268 1.00 64.68  ? 65  ASP B O   1 
ATOM 2211 C CB  . ASP B 2 65  ? 26.854  34.023  -33.290 1.00 65.36  ? 65  ASP B CB  1 
ATOM 2212 C CG  . ASP B 2 65  ? 26.397  35.460  -33.133 1.00 81.17  ? 65  ASP B CG  1 
ATOM 2213 O OD1 . ASP B 2 65  ? 25.175  35.712  -33.191 1.00 83.21  ? 65  ASP B OD1 1 
ATOM 2214 O OD2 . ASP B 2 65  ? 27.264  36.340  -32.945 1.00 85.50  ? 65  ASP B OD2 1 
ATOM 2215 N N   . ARG B 2 66  ? 26.150  30.757  -33.422 1.00 58.73  ? 66  ARG B N   1 
ATOM 2216 C CA  . ARG B 2 66  ? 26.733  29.440  -33.658 1.00 58.78  ? 66  ARG B CA  1 
ATOM 2217 C C   . ARG B 2 66  ? 26.243  28.855  -34.976 1.00 57.61  ? 66  ARG B C   1 
ATOM 2218 O O   . ARG B 2 66  ? 27.035  28.352  -35.782 1.00 55.56  ? 66  ARG B O   1 
ATOM 2219 C CB  . ARG B 2 66  ? 26.388  28.512  -32.495 1.00 56.43  ? 66  ARG B CB  1 
ATOM 2220 C CG  . ARG B 2 66  ? 26.372  29.216  -31.152 1.00 56.78  ? 66  ARG B CG  1 
ATOM 2221 C CD  . ARG B 2 66  ? 26.097  28.241  -30.026 1.00 62.90  ? 66  ARG B CD  1 
ATOM 2222 N NE  . ARG B 2 66  ? 24.843  27.521  -30.221 1.00 60.47  ? 66  ARG B NE  1 
ATOM 2223 C CZ  . ARG B 2 66  ? 23.702  27.817  -29.616 1.00 61.28  ? 66  ARG B CZ  1 
ATOM 2224 N NH1 . ARG B 2 66  ? 23.612  28.829  -28.766 1.00 60.93  ? 66  ARG B NH1 1 
ATOM 2225 N NH2 . ARG B 2 66  ? 22.623  27.080  -29.870 1.00 53.37  ? 66  ARG B NH2 1 
ATOM 2226 N N   . PHE B 2 67  ? 24.934  28.914  -35.209 1.00 58.96  ? 67  PHE B N   1 
ATOM 2227 C CA  . PHE B 2 67  ? 24.367  28.417  -36.454 1.00 49.61  ? 67  PHE B CA  1 
ATOM 2228 C C   . PHE B 2 67  ? 24.878  29.253  -37.620 1.00 48.99  ? 67  PHE B C   1 
ATOM 2229 O O   . PHE B 2 67  ? 24.819  30.485  -37.586 1.00 56.20  ? 67  PHE B O   1 
ATOM 2230 C CB  . PHE B 2 67  ? 22.841  28.473  -36.382 1.00 49.60  ? 67  PHE B CB  1 
ATOM 2231 C CG  . PHE B 2 67  ? 22.252  27.588  -35.319 1.00 50.78  ? 67  PHE B CG  1 
ATOM 2232 C CD1 . PHE B 2 67  ? 22.177  26.217  -35.496 1.00 49.12  ? 67  PHE B CD1 1 
ATOM 2233 C CD2 . PHE B 2 67  ? 21.778  28.134  -34.137 1.00 51.85  ? 67  PHE B CD2 1 
ATOM 2234 C CE1 . PHE B 2 67  ? 21.634  25.408  -34.514 1.00 49.37  ? 67  PHE B CE1 1 
ATOM 2235 C CE2 . PHE B 2 67  ? 21.235  27.330  -33.151 1.00 53.45  ? 67  PHE B CE2 1 
ATOM 2236 C CZ  . PHE B 2 67  ? 21.164  25.964  -33.341 1.00 53.21  ? 67  PHE B CZ  1 
ATOM 2237 N N   . SER B 2 68  ? 25.392  28.584  -38.651 1.00 48.64  ? 68  SER B N   1 
ATOM 2238 C CA  . SER B 2 68  ? 26.004  29.300  -39.768 1.00 48.56  ? 68  SER B CA  1 
ATOM 2239 C C   . SER B 2 68  ? 25.946  28.428  -41.014 1.00 51.42  ? 68  SER B C   1 
ATOM 2240 O O   . SER B 2 68  ? 26.636  27.407  -41.087 1.00 56.59  ? 68  SER B O   1 
ATOM 2241 C CB  . SER B 2 68  ? 27.440  29.684  -39.433 1.00 49.75  ? 68  SER B CB  1 
ATOM 2242 O OG  . SER B 2 68  ? 28.174  28.553  -38.993 1.00 55.25  ? 68  SER B OG  1 
ATOM 2243 N N   . GLY B 2 69  ? 25.139  28.839  -41.987 1.00 49.22  ? 69  GLY B N   1 
ATOM 2244 C CA  . GLY B 2 69  ? 25.101  28.147  -43.255 1.00 48.27  ? 69  GLY B CA  1 
ATOM 2245 C C   . GLY B 2 69  ? 26.163  28.640  -44.221 1.00 50.65  ? 69  GLY B C   1 
ATOM 2246 O O   . GLY B 2 69  ? 26.663  29.760  -44.126 1.00 55.55  ? 69  GLY B O   1 
ATOM 2247 N N   . SER B 2 70  ? 26.509  27.773  -45.170 1.00 50.15  ? 70  SER B N   1 
ATOM 2248 C CA  . SER B 2 70  ? 27.528  28.085  -46.162 1.00 47.59  ? 70  SER B CA  1 
ATOM 2249 C C   . SER B 2 70  ? 27.375  27.128  -47.336 1.00 50.65  ? 70  SER B C   1 
ATOM 2250 O O   . SER B 2 70  ? 26.571  26.194  -47.300 1.00 54.54  ? 70  SER B O   1 
ATOM 2251 C CB  . SER B 2 70  ? 28.934  28.001  -45.560 1.00 47.63  ? 70  SER B CB  1 
ATOM 2252 O OG  . SER B 2 70  ? 29.052  26.902  -44.672 1.00 51.81  ? 70  SER B OG  1 
ATOM 2253 N N   . GLY B 2 71  ? 28.154  27.377  -48.378 1.00 52.06  ? 71  GLY B N   1 
ATOM 2254 C CA  . GLY B 2 71  ? 28.167  26.541  -49.559 1.00 57.95  ? 71  GLY B CA  1 
ATOM 2255 C C   . GLY B 2 71  ? 27.500  27.220  -50.748 1.00 56.46  ? 71  GLY B C   1 
ATOM 2256 O O   . GLY B 2 71  ? 26.691  28.140  -50.609 1.00 56.92  ? 71  GLY B O   1 
ATOM 2257 N N   . SER B 2 72  ? 27.857  26.745  -51.941 1.00 59.85  ? 72  SER B N   1 
ATOM 2258 C CA  . SER B 2 72  ? 27.321  27.308  -53.169 1.00 65.59  ? 72  SER B CA  1 
ATOM 2259 C C   . SER B 2 72  ? 27.148  26.204  -54.196 1.00 67.97  ? 72  SER B C   1 
ATOM 2260 O O   . SER B 2 72  ? 27.865  25.201  -54.180 1.00 69.86  ? 72  SER B O   1 
ATOM 2261 C CB  . SER B 2 72  ? 28.239  28.407  -53.727 1.00 72.81  ? 72  SER B CB  1 
ATOM 2262 O OG  . SER B 2 72  ? 27.834  28.799  -55.026 1.00 69.50  ? 72  SER B OG  1 
ATOM 2263 N N   . GLY B 2 73  ? 26.181  26.397  -55.092 1.00 69.95  ? 73  GLY B N   1 
ATOM 2264 C CA  . GLY B 2 73  ? 25.943  25.445  -56.165 1.00 64.54  ? 73  GLY B CA  1 
ATOM 2265 C C   . GLY B 2 73  ? 25.038  24.300  -55.765 1.00 56.75  ? 73  GLY B C   1 
ATOM 2266 O O   . GLY B 2 73  ? 23.820  24.470  -55.628 1.00 54.77  ? 73  GLY B O   1 
ATOM 2267 N N   . ARG B 2 74  ? 25.624  23.118  -55.578 1.00 52.79  ? 74  ARG B N   1 
ATOM 2268 C CA  . ARG B 2 74  ? 24.878  21.916  -55.233 1.00 57.62  ? 74  ARG B CA  1 
ATOM 2269 C C   . ARG B 2 74  ? 25.181  21.400  -53.837 1.00 56.92  ? 74  ARG B C   1 
ATOM 2270 O O   . ARG B 2 74  ? 24.300  20.812  -53.205 1.00 58.94  ? 74  ARG B O   1 
ATOM 2271 C CB  . ARG B 2 74  ? 25.171  20.804  -56.247 1.00 62.01  ? 74  ARG B CB  1 
ATOM 2272 C CG  . ARG B 2 74  ? 24.624  21.088  -57.634 1.00 60.43  ? 74  ARG B CG  1 
ATOM 2273 C CD  . ARG B 2 74  ? 25.614  20.683  -58.711 1.00 61.74  ? 74  ARG B CD  1 
ATOM 2274 N NE  . ARG B 2 74  ? 25.344  19.347  -59.225 1.00 68.34  ? 74  ARG B NE  1 
ATOM 2275 C CZ  . ARG B 2 74  ? 24.689  19.100  -60.352 1.00 73.20  ? 74  ARG B CZ  1 
ATOM 2276 N NH1 . ARG B 2 74  ? 24.230  20.079  -61.110 1.00 74.97  ? 74  ARG B NH1 1 
ATOM 2277 N NH2 . ARG B 2 74  ? 24.489  17.837  -60.726 1.00 75.01  ? 74  ARG B NH2 1 
ATOM 2278 N N   . ASP B 2 75  ? 26.397  21.609  -53.341 1.00 57.35  ? 75  ASP B N   1 
ATOM 2279 C CA  . ASP B 2 75  ? 26.801  21.163  -52.016 1.00 58.37  ? 75  ASP B CA  1 
ATOM 2280 C C   . ASP B 2 75  ? 26.685  22.311  -51.023 1.00 55.21  ? 75  ASP B C   1 
ATOM 2281 O O   . ASP B 2 75  ? 27.034  23.454  -51.333 1.00 56.10  ? 75  ASP B O   1 
ATOM 2282 C CB  . ASP B 2 75  ? 28.233  20.627  -52.033 1.00 60.05  ? 75  ASP B CB  1 
ATOM 2283 C CG  . ASP B 2 75  ? 28.520  19.775  -53.251 1.00 60.70  ? 75  ASP B CG  1 
ATOM 2284 O OD1 . ASP B 2 75  ? 27.609  19.046  -53.696 1.00 60.79  ? 75  ASP B OD1 1 
ATOM 2285 O OD2 . ASP B 2 75  ? 29.659  19.829  -53.762 1.00 66.13  ? 75  ASP B OD2 1 
ATOM 2286 N N   . PHE B 2 76  ? 26.197  21.996  -49.827 1.00 54.34  ? 76  PHE B N   1 
ATOM 2287 C CA  . PHE B 2 76  ? 25.933  23.007  -48.817 1.00 51.22  ? 76  PHE B CA  1 
ATOM 2288 C C   . PHE B 2 76  ? 26.140  22.387  -47.444 1.00 52.30  ? 76  PHE B C   1 
ATOM 2289 O O   . PHE B 2 76  ? 25.842  21.208  -47.239 1.00 55.49  ? 76  PHE B O   1 
ATOM 2290 C CB  . PHE B 2 76  ? 24.506  23.543  -48.933 1.00 49.67  ? 76  PHE B CB  1 
ATOM 2291 C CG  . PHE B 2 76  ? 24.223  24.273  -50.221 1.00 50.12  ? 76  PHE B CG  1 
ATOM 2292 C CD1 . PHE B 2 76  ? 24.438  25.637  -50.329 1.00 55.91  ? 76  PHE B CD1 1 
ATOM 2293 C CD2 . PHE B 2 76  ? 23.698  23.596  -51.313 1.00 54.96  ? 76  PHE B CD2 1 
ATOM 2294 C CE1 . PHE B 2 76  ? 24.161  26.308  -51.509 1.00 57.64  ? 76  PHE B CE1 1 
ATOM 2295 C CE2 . PHE B 2 76  ? 23.419  24.261  -52.493 1.00 61.12  ? 76  PHE B CE2 1 
ATOM 2296 C CZ  . PHE B 2 76  ? 23.651  25.619  -52.591 1.00 60.09  ? 76  PHE B CZ  1 
ATOM 2297 N N   . THR B 2 77  ? 26.630  23.188  -46.501 1.00 49.88  ? 77  THR B N   1 
ATOM 2298 C CA  . THR B 2 77  ? 26.967  22.698  -45.170 1.00 47.63  ? 77  THR B CA  1 
ATOM 2299 C C   . THR B 2 77  ? 26.427  23.655  -44.120 1.00 47.15  ? 77  THR B C   1 
ATOM 2300 O O   . THR B 2 77  ? 26.761  24.845  -44.132 1.00 51.66  ? 77  THR B O   1 
ATOM 2301 C CB  . THR B 2 77  ? 28.481  22.533  -45.014 1.00 51.41  ? 77  THR B CB  1 
ATOM 2302 O OG1 . THR B 2 77  ? 29.026  21.970  -46.213 1.00 54.66  ? 77  THR B OG1 1 
ATOM 2303 C CG2 . THR B 2 77  ? 28.797  21.614  -43.844 1.00 55.83  ? 77  THR B CG2 1 
ATOM 2304 N N   . LEU B 2 78  ? 25.591  23.137  -43.223 1.00 48.03  ? 78  LEU B N   1 
ATOM 2305 C CA  . LEU B 2 78  ? 25.169  23.862  -42.032 1.00 47.57  ? 78  LEU B CA  1 
ATOM 2306 C C   . LEU B 2 78  ? 26.107  23.500  -40.889 1.00 49.48  ? 78  LEU B C   1 
ATOM 2307 O O   . LEU B 2 78  ? 26.259  22.320  -40.556 1.00 52.84  ? 78  LEU B O   1 
ATOM 2308 C CB  . LEU B 2 78  ? 23.722  23.526  -41.669 1.00 47.85  ? 78  LEU B CB  1 
ATOM 2309 C CG  . LEU B 2 78  ? 23.228  24.099  -40.337 1.00 48.12  ? 78  LEU B CG  1 
ATOM 2310 C CD1 . LEU B 2 78  ? 23.056  25.610  -40.418 1.00 48.38  ? 78  LEU B CD1 1 
ATOM 2311 C CD2 . LEU B 2 78  ? 21.935  23.427  -39.899 1.00 48.31  ? 78  LEU B CD2 1 
ATOM 2312 N N   . LYS B 2 79  ? 26.739  24.510  -40.299 1.00 47.47  ? 79  LYS B N   1 
ATOM 2313 C CA  . LYS B 2 79  ? 27.730  24.310  -39.253 1.00 48.99  ? 79  LYS B CA  1 
ATOM 2314 C C   . LYS B 2 79  ? 27.245  24.945  -37.960 1.00 50.85  ? 79  LYS B C   1 
ATOM 2315 O O   . LYS B 2 79  ? 26.795  26.095  -37.958 1.00 55.69  ? 79  LYS B O   1 
ATOM 2316 C CB  . LYS B 2 79  ? 29.083  24.908  -39.652 1.00 51.88  ? 79  LYS B CB  1 
ATOM 2317 C CG  . LYS B 2 79  ? 29.608  24.442  -41.001 1.00 56.13  ? 79  LYS B CG  1 
ATOM 2318 C CD  . LYS B 2 79  ? 30.935  25.113  -41.322 1.00 64.21  ? 79  LYS B CD  1 
ATOM 2319 C CE  . LYS B 2 79  ? 31.512  24.611  -42.635 1.00 72.77  ? 79  LYS B CE  1 
ATOM 2320 N NZ  . LYS B 2 79  ? 32.835  25.225  -42.936 1.00 82.41  ? 79  LYS B NZ  1 
ATOM 2321 N N   . ILE B 2 80  ? 27.334  24.192  -36.869 1.00 47.72  ? 80  ILE B N   1 
ATOM 2322 C CA  . ILE B 2 80  ? 27.109  24.700  -35.522 1.00 48.04  ? 80  ILE B CA  1 
ATOM 2323 C C   . ILE B 2 80  ? 28.446  24.646  -34.798 1.00 58.57  ? 80  ILE B C   1 
ATOM 2324 O O   . ILE B 2 80  ? 29.004  23.561  -34.596 1.00 57.67  ? 80  ILE B O   1 
ATOM 2325 C CB  . ILE B 2 80  ? 26.039  23.887  -34.779 1.00 48.37  ? 80  ILE B CB  1 
ATOM 2326 C CG1 . ILE B 2 80  ? 24.818  23.674  -35.678 1.00 53.54  ? 80  ILE B CG1 1 
ATOM 2327 C CG2 . ILE B 2 80  ? 25.646  24.582  -33.481 1.00 54.60  ? 80  ILE B CG2 1 
ATOM 2328 C CD1 . ILE B 2 80  ? 23.833  22.640  -35.160 1.00 56.81  ? 80  ILE B CD1 1 
ATOM 2329 N N   . SER B 2 81  ? 28.963  25.816  -34.415 1.00 59.25  ? 81  SER B N   1 
ATOM 2330 C CA  . SER B 2 81  ? 30.306  25.905  -33.848 1.00 57.93  ? 81  SER B CA  1 
ATOM 2331 C C   . SER B 2 81  ? 30.382  25.299  -32.452 1.00 59.78  ? 81  SER B C   1 
ATOM 2332 O O   . SER B 2 81  ? 31.337  24.580  -32.136 1.00 66.20  ? 81  SER B O   1 
ATOM 2333 C CB  . SER B 2 81  ? 30.765  27.363  -33.828 1.00 61.48  ? 81  SER B CB  1 
ATOM 2334 O OG  . SER B 2 81  ? 29.918  28.166  -33.021 1.00 64.59  ? 81  SER B OG  1 
ATOM 2335 N N   . ARG B 2 82  ? 29.398  25.582  -31.603 1.00 53.70  ? 82  ARG B N   1 
ATOM 2336 C CA  . ARG B 2 82  ? 29.362  25.072  -30.234 1.00 56.56  ? 82  ARG B CA  1 
ATOM 2337 C C   . ARG B 2 82  ? 27.959  24.536  -29.974 1.00 57.86  ? 82  ARG B C   1 
ATOM 2338 O O   . ARG B 2 82  ? 27.029  25.304  -29.719 1.00 60.53  ? 82  ARG B O   1 
ATOM 2339 C CB  . ARG B 2 82  ? 29.739  26.154  -29.230 1.00 60.21  ? 82  ARG B CB  1 
ATOM 2340 C CG  . ARG B 2 82  ? 29.520  25.763  -27.779 1.00 61.85  ? 82  ARG B CG  1 
ATOM 2341 C CD  . ARG B 2 82  ? 29.901  26.900  -26.851 1.00 62.87  ? 82  ARG B CD  1 
ATOM 2342 N NE  . ARG B 2 82  ? 31.123  26.595  -26.118 1.00 68.32  ? 82  ARG B NE  1 
ATOM 2343 C CZ  . ARG B 2 82  ? 32.345  26.807  -26.588 1.00 70.40  ? 82  ARG B CZ  1 
ATOM 2344 N NH1 . ARG B 2 82  ? 32.542  27.335  -27.785 1.00 73.05  ? 82  ARG B NH1 1 
ATOM 2345 N NH2 . ARG B 2 82  ? 33.395  26.475  -25.842 1.00 67.20  ? 82  ARG B NH2 1 
ATOM 2346 N N   . VAL B 2 83  ? 27.811  23.215  -30.045 1.00 52.27  ? 83  VAL B N   1 
ATOM 2347 C CA  . VAL B 2 83  ? 26.517  22.595  -29.807 1.00 52.91  ? 83  VAL B CA  1 
ATOM 2348 C C   . VAL B 2 83  ? 26.162  22.707  -28.332 1.00 51.01  ? 83  VAL B C   1 
ATOM 2349 O O   . VAL B 2 83  ? 27.028  22.598  -27.452 1.00 57.51  ? 83  VAL B O   1 
ATOM 2350 C CB  . VAL B 2 83  ? 26.535  21.130  -30.271 1.00 58.45  ? 83  VAL B CB  1 
ATOM 2351 C CG1 . VAL B 2 83  ? 25.142  20.537  -30.211 1.00 55.33  ? 83  VAL B CG1 1 
ATOM 2352 C CG2 . VAL B 2 83  ? 27.099  21.035  -31.678 1.00 60.17  ? 83  VAL B CG2 1 
ATOM 2353 N N   . GLU B 2 84  ? 24.882  22.931  -28.055 1.00 49.67  ? 84  GLU B N   1 
ATOM 2354 C CA  . GLU B 2 84  ? 24.369  23.031  -26.700 1.00 55.48  ? 84  GLU B CA  1 
ATOM 2355 C C   . GLU B 2 84  ? 23.142  22.137  -26.573 1.00 57.10  ? 84  GLU B C   1 
ATOM 2356 O O   . GLU B 2 84  ? 22.649  21.578  -27.556 1.00 62.59  ? 84  GLU B O   1 
ATOM 2357 C CB  . GLU B 2 84  ? 24.043  24.489  -26.344 1.00 64.40  ? 84  GLU B CB  1 
ATOM 2358 C CG  . GLU B 2 84  ? 25.255  25.422  -26.402 1.00 65.18  ? 84  GLU B CG  1 
ATOM 2359 C CD  . GLU B 2 84  ? 24.927  26.857  -26.021 1.00 66.46  ? 84  GLU B CD  1 
ATOM 2360 O OE1 . GLU B 2 84  ? 23.841  27.095  -25.454 1.00 70.99  ? 84  GLU B OE1 1 
ATOM 2361 O OE2 . GLU B 2 84  ? 25.762  27.748  -26.287 1.00 63.02  ? 84  GLU B OE2 1 
ATOM 2362 N N   . ALA B 2 85  ? 22.652  22.003  -25.339 1.00 59.04  ? 85  ALA B N   1 
ATOM 2363 C CA  . ALA B 2 85  ? 21.550  21.083  -25.074 1.00 65.19  ? 85  ALA B CA  1 
ATOM 2364 C C   . ALA B 2 85  ? 20.294  21.478  -25.839 1.00 66.55  ? 85  ALA B C   1 
ATOM 2365 O O   . ALA B 2 85  ? 19.523  20.613  -26.270 1.00 65.52  ? 85  ALA B O   1 
ATOM 2366 C CB  . ALA B 2 85  ? 21.267  21.028  -23.574 1.00 68.80  ? 85  ALA B CB  1 
ATOM 2367 N N   . GLN B 2 86  ? 20.075  22.781  -26.025 1.00 70.75  ? 86  GLN B N   1 
ATOM 2368 C CA  . GLN B 2 86  ? 18.869  23.258  -26.692 1.00 72.18  ? 86  GLN B CA  1 
ATOM 2369 C C   . GLN B 2 86  ? 18.828  22.880  -28.167 1.00 69.35  ? 86  GLN B C   1 
ATOM 2370 O O   . GLN B 2 86  ? 17.742  22.843  -28.754 1.00 68.90  ? 86  GLN B O   1 
ATOM 2371 C CB  . GLN B 2 86  ? 18.770  24.775  -26.543 1.00 72.06  ? 86  GLN B CB  1 
ATOM 2372 C CG  . GLN B 2 86  ? 19.021  25.257  -25.128 1.00 80.65  ? 86  GLN B CG  1 
ATOM 2373 C CD  . GLN B 2 86  ? 20.290  26.078  -25.024 1.00 88.78  ? 86  GLN B CD  1 
ATOM 2374 O OE1 . GLN B 2 86  ? 21.241  25.865  -25.774 1.00 84.68  ? 86  GLN B OE1 1 
ATOM 2375 N NE2 . GLN B 2 86  ? 20.315  27.015  -24.086 1.00 88.38  ? 86  GLN B NE2 1 
ATOM 2376 N N   . ASP B 2 87  ? 19.980  22.588  -28.772 1.00 61.25  ? 87  ASP B N   1 
ATOM 2377 C CA  . ASP B 2 87  ? 20.072  22.343  -30.207 1.00 53.30  ? 87  ASP B CA  1 
ATOM 2378 C C   . ASP B 2 87  ? 19.523  20.986  -30.629 1.00 61.88  ? 87  ASP B C   1 
ATOM 2379 O O   . ASP B 2 87  ? 19.630  20.647  -31.813 1.00 62.53  ? 87  ASP B O   1 
ATOM 2380 C CB  . ASP B 2 87  ? 21.529  22.464  -30.654 1.00 53.52  ? 87  ASP B CB  1 
ATOM 2381 C CG  . ASP B 2 87  ? 22.121  23.823  -30.339 1.00 58.84  ? 87  ASP B CG  1 
ATOM 2382 O OD1 . ASP B 2 87  ? 21.425  24.641  -29.703 1.00 60.76  ? 87  ASP B OD1 1 
ATOM 2383 O OD2 . ASP B 2 87  ? 23.285  24.072  -30.718 1.00 58.98  ? 87  ASP B OD2 1 
ATOM 2384 N N   . VAL B 2 88  ? 18.952  20.205  -29.709 1.00 65.07  ? 88  VAL B N   1 
ATOM 2385 C CA  . VAL B 2 88  ? 18.443  18.882  -30.053 1.00 57.87  ? 88  VAL B CA  1 
ATOM 2386 C C   . VAL B 2 88  ? 17.276  19.000  -31.021 1.00 56.86  ? 88  VAL B C   1 
ATOM 2387 O O   . VAL B 2 88  ? 16.518  19.977  -31.009 1.00 66.26  ? 88  VAL B O   1 
ATOM 2388 C CB  . VAL B 2 88  ? 18.024  18.101  -28.795 1.00 56.03  ? 88  VAL B CB  1 
ATOM 2389 C CG1 . VAL B 2 88  ? 19.239  17.661  -28.018 1.00 52.42  ? 88  VAL B CG1 1 
ATOM 2390 C CG2 . VAL B 2 88  ? 17.120  18.949  -27.917 1.00 64.34  ? 88  VAL B CG2 1 
ATOM 2391 N N   . GLY B 2 89  ? 17.131  17.985  -31.866 1.00 53.01  ? 89  GLY B N   1 
ATOM 2392 C CA  . GLY B 2 89  ? 16.069  17.958  -32.850 1.00 61.48  ? 89  GLY B CA  1 
ATOM 2393 C C   . GLY B 2 89  ? 16.560  17.465  -34.193 1.00 50.90  ? 89  GLY B C   1 
ATOM 2394 O O   . GLY B 2 89  ? 17.741  17.145  -34.349 1.00 49.71  ? 89  GLY B O   1 
ATOM 2395 N N   . THR B 2 90  ? 15.664  17.406  -35.170 1.00 53.15  ? 90  THR B N   1 
ATOM 2396 C CA  . THR B 2 90  ? 16.003  16.997  -36.525 1.00 60.86  ? 90  THR B CA  1 
ATOM 2397 C C   . THR B 2 90  ? 16.070  18.207  -37.451 1.00 57.94  ? 90  THR B C   1 
ATOM 2398 O O   . THR B 2 90  ? 15.230  19.110  -37.385 1.00 52.96  ? 90  THR B O   1 
ATOM 2399 C CB  . THR B 2 90  ? 14.997  15.968  -37.056 1.00 60.20  ? 90  THR B CB  1 
ATOM 2400 O OG1 . THR B 2 90  ? 15.444  15.468  -38.322 1.00 60.23  ? 90  THR B OG1 1 
ATOM 2401 C CG2 . THR B 2 90  ? 13.601  16.568  -37.186 1.00 62.79  ? 90  THR B CG2 1 
ATOM 2402 N N   . TYR B 2 91  ? 17.080  18.220  -38.314 1.00 59.84  ? 91  TYR B N   1 
ATOM 2403 C CA  . TYR B 2 91  ? 17.371  19.355  -39.177 1.00 48.84  ? 91  TYR B CA  1 
ATOM 2404 C C   . TYR B 2 91  ? 17.050  19.010  -40.626 1.00 48.82  ? 91  TYR B C   1 
ATOM 2405 O O   . TYR B 2 91  ? 17.240  17.870  -41.060 1.00 52.09  ? 91  TYR B O   1 
ATOM 2406 C CB  . TYR B 2 91  ? 18.840  19.766  -39.057 1.00 48.60  ? 91  TYR B CB  1 
ATOM 2407 C CG  . TYR B 2 91  ? 19.240  20.391  -37.734 1.00 51.60  ? 91  TYR B CG  1 
ATOM 2408 C CD1 . TYR B 2 91  ? 19.232  19.653  -36.555 1.00 51.72  ? 91  TYR B CD1 1 
ATOM 2409 C CD2 . TYR B 2 91  ? 19.664  21.712  -37.673 1.00 48.71  ? 91  TYR B CD2 1 
ATOM 2410 C CE1 . TYR B 2 91  ? 19.613  20.223  -35.349 1.00 54.02  ? 91  TYR B CE1 1 
ATOM 2411 C CE2 . TYR B 2 91  ? 20.048  22.287  -36.478 1.00 48.81  ? 91  TYR B CE2 1 
ATOM 2412 C CZ  . TYR B 2 91  ? 20.022  21.539  -35.319 1.00 48.86  ? 91  TYR B CZ  1 
ATOM 2413 O OH  . TYR B 2 91  ? 20.404  22.115  -34.128 1.00 49.01  ? 91  TYR B OH  1 
ATOM 2414 N N   . TYR B 2 92  ? 16.581  20.006  -41.375 1.00 48.97  ? 92  TYR B N   1 
ATOM 2415 C CA  . TYR B 2 92  ? 16.185  19.820  -42.763 1.00 49.04  ? 92  TYR B CA  1 
ATOM 2416 C C   . TYR B 2 92  ? 16.793  20.916  -43.626 1.00 49.01  ? 92  TYR B C   1 
ATOM 2417 O O   . TYR B 2 92  ? 17.032  22.034  -43.158 1.00 50.61  ? 92  TYR B O   1 
ATOM 2418 C CB  . TYR B 2 92  ? 14.660  19.847  -42.911 1.00 49.36  ? 92  TYR B CB  1 
ATOM 2419 C CG  . TYR B 2 92  ? 13.945  18.781  -42.117 1.00 49.42  ? 92  TYR B CG  1 
ATOM 2420 C CD1 . TYR B 2 92  ? 13.822  17.484  -42.600 1.00 49.40  ? 92  TYR B CD1 1 
ATOM 2421 C CD2 . TYR B 2 92  ? 13.391  19.076  -40.881 1.00 49.54  ? 92  TYR B CD2 1 
ATOM 2422 C CE1 . TYR B 2 92  ? 13.164  16.513  -41.871 1.00 49.49  ? 92  TYR B CE1 1 
ATOM 2423 C CE2 . TYR B 2 92  ? 12.729  18.114  -40.148 1.00 49.61  ? 92  TYR B CE2 1 
ATOM 2424 C CZ  . TYR B 2 92  ? 12.621  16.834  -40.646 1.00 49.59  ? 92  TYR B CZ  1 
ATOM 2425 O OH  . TYR B 2 92  ? 11.964  15.872  -39.915 1.00 54.68  ? 92  TYR B OH  1 
ATOM 2426 N N   . CYS B 2 93  ? 17.048  20.585  -44.891 1.00 48.96  ? 93  CYS B N   1 
ATOM 2427 C CA  . CYS B 2 93  ? 17.393  21.569  -45.910 1.00 49.02  ? 93  CYS B CA  1 
ATOM 2428 C C   . CYS B 2 93  ? 16.311  21.556  -46.980 1.00 49.34  ? 93  CYS B C   1 
ATOM 2429 O O   . CYS B 2 93  ? 15.776  20.498  -47.320 1.00 50.66  ? 93  CYS B O   1 
ATOM 2430 C CB  . CYS B 2 93  ? 18.777  21.304  -46.542 1.00 48.69  ? 93  CYS B CB  1 
ATOM 2431 S SG  . CYS B 2 93  ? 19.023  19.682  -47.323 1.00 53.04  ? 93  CYS B SG  1 
ATOM 2432 N N   . LEU B 2 94  ? 15.986  22.736  -47.499 1.00 49.59  ? 94  LEU B N   1 
ATOM 2433 C CA  . LEU B 2 94  ? 14.886  22.914  -48.436 1.00 49.97  ? 94  LEU B CA  1 
ATOM 2434 C C   . LEU B 2 94  ? 15.357  23.731  -49.628 1.00 50.09  ? 94  LEU B C   1 
ATOM 2435 O O   . LEU B 2 94  ? 16.077  24.719  -49.464 1.00 52.47  ? 94  LEU B O   1 
ATOM 2436 C CB  . LEU B 2 94  ? 13.701  23.618  -47.758 1.00 50.29  ? 94  LEU B CB  1 
ATOM 2437 C CG  . LEU B 2 94  ? 12.541  24.110  -48.628 1.00 50.75  ? 94  LEU B CG  1 
ATOM 2438 C CD1 . LEU B 2 94  ? 11.711  22.953  -49.169 1.00 50.86  ? 94  LEU B CD1 1 
ATOM 2439 C CD2 . LEU B 2 94  ? 11.672  25.101  -47.870 1.00 51.13  ? 94  LEU B CD2 1 
ATOM 2440 N N   . GLN B 2 95  ? 14.946  23.326  -50.828 1.00 50.29  ? 95  GLN B N   1 
ATOM 2441 C CA  . GLN B 2 95  ? 15.212  24.101  -52.030 1.00 52.69  ? 95  GLN B CA  1 
ATOM 2442 C C   . GLN B 2 95  ? 13.951  24.875  -52.391 1.00 53.74  ? 95  GLN B C   1 
ATOM 2443 O O   . GLN B 2 95  ? 12.841  24.338  -52.313 1.00 52.09  ? 95  GLN B O   1 
ATOM 2444 C CB  . GLN B 2 95  ? 15.636  23.212  -53.202 1.00 53.55  ? 95  GLN B CB  1 
ATOM 2445 C CG  . GLN B 2 95  ? 14.600  22.188  -53.635 1.00 54.04  ? 95  GLN B CG  1 
ATOM 2446 C CD  . GLN B 2 95  ? 13.892  22.604  -54.915 1.00 58.18  ? 95  GLN B CD  1 
ATOM 2447 O OE1 . GLN B 2 95  ? 14.291  23.565  -55.571 1.00 65.09  ? 95  GLN B OE1 1 
ATOM 2448 N NE2 . GLN B 2 95  ? 12.824  21.894  -55.263 1.00 67.45  ? 95  GLN B NE2 1 
ATOM 2449 N N   . THR B 2 96  ? 14.123  26.141  -52.760 1.00 57.65  ? 96  THR B N   1 
ATOM 2450 C CA  . THR B 2 96  ? 13.022  26.978  -53.214 1.00 59.82  ? 96  THR B CA  1 
ATOM 2451 C C   . THR B 2 96  ? 13.173  27.370  -54.675 1.00 58.53  ? 96  THR B C   1 
ATOM 2452 O O   . THR B 2 96  ? 12.425  28.225  -55.156 1.00 61.98  ? 96  THR B O   1 
ATOM 2453 C CB  . THR B 2 96  ? 12.914  28.230  -52.341 1.00 57.25  ? 96  THR B CB  1 
ATOM 2454 O OG1 . THR B 2 96  ? 14.174  28.911  -52.319 1.00 61.59  ? 96  THR B OG1 1 
ATOM 2455 C CG2 . THR B 2 96  ? 12.531  27.855  -50.918 1.00 53.81  ? 96  THR B CG2 1 
ATOM 2456 N N   . ARG B 2 97  ? 14.111  26.753  -55.394 1.00 58.90  ? 97  ARG B N   1 
ATOM 2457 C CA  . ARG B 2 97  ? 14.456  27.227  -56.729 1.00 62.82  ? 97  ARG B CA  1 
ATOM 2458 C C   . ARG B 2 97  ? 13.412  26.827  -57.770 1.00 64.71  ? 97  ARG B C   1 
ATOM 2459 O O   . ARG B 2 97  ? 12.880  27.685  -58.486 1.00 69.70  ? 97  ARG B O   1 
ATOM 2460 C CB  . ARG B 2 97  ? 15.834  26.703  -57.126 1.00 64.05  ? 97  ARG B CB  1 
ATOM 2461 C CG  . ARG B 2 97  ? 16.398  27.390  -58.355 1.00 69.54  ? 97  ARG B CG  1 
ATOM 2462 C CD  . ARG B 2 97  ? 17.089  26.379  -59.245 1.00 74.70  ? 97  ARG B CD  1 
ATOM 2463 N NE  . ARG B 2 97  ? 17.533  26.976  -60.497 1.00 77.38  ? 97  ARG B NE  1 
ATOM 2464 C CZ  . ARG B 2 97  ? 18.093  26.297  -61.487 1.00 77.34  ? 97  ARG B CZ  1 
ATOM 2465 N NH1 . ARG B 2 97  ? 18.321  24.999  -61.389 1.00 77.72  ? 97  ARG B NH1 1 
ATOM 2466 N NH2 . ARG B 2 97  ? 18.424  26.934  -62.606 1.00 78.44  ? 97  ARG B NH2 1 
ATOM 2467 N N   . GLN B 2 98  ? 13.112  25.529  -57.884 1.00 70.60  ? 98  GLN B N   1 
ATOM 2468 C CA  . GLN B 2 98  ? 12.432  25.003  -59.066 1.00 80.71  ? 98  GLN B CA  1 
ATOM 2469 C C   . GLN B 2 98  ? 11.061  24.395  -58.772 1.00 82.15  ? 98  GLN B C   1 
ATOM 2470 O O   . GLN B 2 98  ? 10.674  23.402  -59.393 1.00 84.51  ? 98  GLN B O   1 
ATOM 2471 C CB  . GLN B 2 98  ? 13.317  23.981  -59.773 1.00 79.18  ? 98  GLN B CB  1 
ATOM 2472 C CG  . GLN B 2 98  ? 14.237  24.595  -60.809 1.00 82.80  ? 98  GLN B CG  1 
ATOM 2473 C CD  . GLN B 2 98  ? 14.859  23.551  -61.706 1.00 90.51  ? 98  GLN B CD  1 
ATOM 2474 O OE1 . GLN B 2 98  ? 14.503  22.374  -61.647 1.00 98.63  ? 98  GLN B OE1 1 
ATOM 2475 N NE2 . GLN B 2 98  ? 15.780  23.977  -62.559 1.00 90.01  ? 98  GLN B NE2 1 
ATOM 2476 N N   . GLY B 2 99  ? 10.308  24.982  -57.841 1.00 109.28 ? 99  GLY B N   1 
ATOM 2477 C CA  . GLY B 2 99  ? 8.885   24.717  -57.715 1.00 109.66 ? 99  GLY B CA  1 
ATOM 2478 C C   . GLY B 2 99  ? 8.473   23.321  -57.293 1.00 108.97 ? 99  GLY B C   1 
ATOM 2479 O O   . GLY B 2 99  ? 7.268   23.064  -57.176 1.00 109.33 ? 99  GLY B O   1 
ATOM 2480 N N   . ALA B 2 100 ? 9.408   22.395  -57.093 1.00 81.99  ? 100 ALA B N   1 
ATOM 2481 C CA  . ALA B 2 100 ? 9.047   21.168  -56.397 1.00 75.02  ? 100 ALA B CA  1 
ATOM 2482 C C   . ALA B 2 100 ? 9.005   21.407  -54.899 1.00 71.68  ? 100 ALA B C   1 
ATOM 2483 O O   . ALA B 2 100 ? 8.201   20.787  -54.192 1.00 70.99  ? 100 ALA B O   1 
ATOM 2484 C CB  . ALA B 2 100 ? 10.037  20.051  -56.732 1.00 77.16  ? 100 ALA B CB  1 
ATOM 2485 N N   . PHE B 2 101 ? 9.842   22.329  -54.427 1.00 67.58  ? 101 PHE B N   1 
ATOM 2486 C CA  . PHE B 2 101 ? 9.948   22.711  -53.023 1.00 59.19  ? 101 PHE B CA  1 
ATOM 2487 C C   . PHE B 2 101 ? 10.136  21.476  -52.147 1.00 57.92  ? 101 PHE B C   1 
ATOM 2488 O O   . PHE B 2 101 ? 9.317   21.146  -51.292 1.00 58.54  ? 101 PHE B O   1 
ATOM 2489 C CB  . PHE B 2 101 ? 8.734   23.533  -52.588 1.00 63.97  ? 101 PHE B CB  1 
ATOM 2490 C CG  . PHE B 2 101 ? 8.816   24.990  -52.965 1.00 65.67  ? 101 PHE B CG  1 
ATOM 2491 C CD1 . PHE B 2 101 ? 9.092   25.378  -54.267 1.00 66.42  ? 101 PHE B CD1 1 
ATOM 2492 C CD2 . PHE B 2 101 ? 8.614   25.970  -52.012 1.00 64.49  ? 101 PHE B CD2 1 
ATOM 2493 C CE1 . PHE B 2 101 ? 9.162   26.716  -54.607 1.00 59.75  ? 101 PHE B CE1 1 
ATOM 2494 C CE2 . PHE B 2 101 ? 8.682   27.308  -52.344 1.00 63.24  ? 101 PHE B CE2 1 
ATOM 2495 C CZ  . PHE B 2 101 ? 8.957   27.683  -53.643 1.00 59.10  ? 101 PHE B CZ  1 
ATOM 2496 N N   . THR B 2 102 ? 11.243  20.787  -52.393 1.00 55.85  ? 102 THR B N   1 
ATOM 2497 C CA  . THR B 2 102 ? 11.528  19.511  -51.755 1.00 53.76  ? 102 THR B CA  1 
ATOM 2498 C C   . THR B 2 102 ? 12.459  19.714  -50.569 1.00 52.37  ? 102 THR B C   1 
ATOM 2499 O O   . THR B 2 102 ? 13.453  20.443  -50.667 1.00 50.34  ? 102 THR B O   1 
ATOM 2500 C CB  . THR B 2 102 ? 12.161  18.535  -52.745 1.00 55.60  ? 102 THR B CB  1 
ATOM 2501 O OG1 . THR B 2 102 ? 13.276  19.164  -53.391 1.00 59.28  ? 102 THR B OG1 1 
ATOM 2502 C CG2 . THR B 2 102 ? 11.150  18.107  -53.793 1.00 58.59  ? 102 THR B CG2 1 
ATOM 2503 N N   . PHE B 2 103 ? 12.138  19.059  -49.460 1.00 53.33  ? 103 PHE B N   1 
ATOM 2504 C CA  . PHE B 2 103 ? 12.983  19.103  -48.282 1.00 50.06  ? 103 PHE B CA  1 
ATOM 2505 C C   . PHE B 2 103 ? 14.080  18.047  -48.378 1.00 49.73  ? 103 PHE B C   1 
ATOM 2506 O O   . PHE B 2 103 ? 14.219  17.334  -49.379 1.00 49.78  ? 103 PHE B O   1 
ATOM 2507 C CB  . PHE B 2 103 ? 12.151  18.901  -47.019 1.00 50.11  ? 103 PHE B CB  1 
ATOM 2508 C CG  . PHE B 2 103 ? 11.297  20.081  -46.655 1.00 50.36  ? 103 PHE B CG  1 
ATOM 2509 C CD1 . PHE B 2 103 ? 10.021  20.217  -47.171 1.00 50.73  ? 103 PHE B CD1 1 
ATOM 2510 C CD2 . PHE B 2 103 ? 11.760  21.036  -45.766 1.00 50.26  ? 103 PHE B CD2 1 
ATOM 2511 C CE1 . PHE B 2 103 ? 9.231   21.295  -46.826 1.00 50.97  ? 103 PHE B CE1 1 
ATOM 2512 C CE2 . PHE B 2 103 ? 10.973  22.114  -45.416 1.00 50.52  ? 103 PHE B CE2 1 
ATOM 2513 C CZ  . PHE B 2 103 ? 9.709   22.244  -45.946 1.00 50.87  ? 103 PHE B CZ  1 
ATOM 2514 N N   . GLY B 2 104 ? 14.873  17.947  -47.311 1.00 49.44  ? 104 GLY B N   1 
ATOM 2515 C CA  . GLY B 2 104 ? 15.891  16.928  -47.200 1.00 49.14  ? 104 GLY B CA  1 
ATOM 2516 C C   . GLY B 2 104 ? 15.429  15.761  -46.338 1.00 49.18  ? 104 GLY B C   1 
ATOM 2517 O O   . GLY B 2 104 ? 14.340  15.756  -45.770 1.00 49.39  ? 104 GLY B O   1 
ATOM 2518 N N   . GLN B 2 105 ? 16.306  14.755  -46.250 1.00 50.23  ? 105 GLN B N   1 
ATOM 2519 C CA  . GLN B 2 105 ? 15.987  13.547  -45.494 1.00 54.07  ? 105 GLN B CA  1 
ATOM 2520 C C   . GLN B 2 105 ? 15.667  13.868  -44.040 1.00 56.91  ? 105 GLN B C   1 
ATOM 2521 O O   . GLN B 2 105 ? 14.735  13.299  -43.458 1.00 59.26  ? 105 GLN B O   1 
ATOM 2522 C CB  . GLN B 2 105 ? 17.152  12.556  -45.548 1.00 49.57  ? 105 GLN B CB  1 
ATOM 2523 C CG  . GLN B 2 105 ? 17.931  12.523  -46.850 1.00 59.65  ? 105 GLN B CG  1 
ATOM 2524 C CD  . GLN B 2 105 ? 19.287  11.856  -46.687 1.00 64.51  ? 105 GLN B CD  1 
ATOM 2525 O OE1 . GLN B 2 105 ? 19.649  11.420  -45.595 1.00 61.74  ? 105 GLN B OE1 1 
ATOM 2526 N NE2 . GLN B 2 105 ? 20.043  11.775  -47.774 1.00 71.10  ? 105 GLN B NE2 1 
ATOM 2527 N N   . GLY B 2 106 ? 16.428  14.776  -43.439 1.00 59.64  ? 106 GLY B N   1 
ATOM 2528 C CA  . GLY B 2 106 ? 16.386  14.972  -42.006 1.00 59.79  ? 106 GLY B CA  1 
ATOM 2529 C C   . GLY B 2 106 ? 17.686  14.551  -41.353 1.00 60.27  ? 106 GLY B C   1 
ATOM 2530 O O   . GLY B 2 106 ? 18.423  13.728  -41.904 1.00 61.91  ? 106 GLY B O   1 
ATOM 2531 N N   . THR B 2 107 ? 17.983  15.109  -40.182 1.00 58.26  ? 107 THR B N   1 
ATOM 2532 C CA  . THR B 2 107 ? 19.223  14.784  -39.480 1.00 48.36  ? 107 THR B CA  1 
ATOM 2533 C C   . THR B 2 107 ? 19.022  15.032  -37.996 1.00 48.50  ? 107 THR B C   1 
ATOM 2534 O O   . THR B 2 107 ? 18.829  16.181  -37.585 1.00 57.32  ? 107 THR B O   1 
ATOM 2535 C CB  . THR B 2 107 ? 20.386  15.623  -40.010 1.00 48.51  ? 107 THR B CB  1 
ATOM 2536 O OG1 . THR B 2 107 ? 20.823  15.096  -41.268 1.00 52.46  ? 107 THR B OG1 1 
ATOM 2537 C CG2 . THR B 2 107 ? 21.545  15.603  -39.026 1.00 48.53  ? 107 THR B CG2 1 
ATOM 2538 N N   . LYS B 2 108 ? 19.076  13.972  -37.192 1.00 49.67  ? 108 LYS B N   1 
ATOM 2539 C CA  . LYS B 2 108 ? 18.927  14.120  -35.750 1.00 54.85  ? 108 LYS B CA  1 
ATOM 2540 C C   . LYS B 2 108 ? 20.236  14.555  -35.110 1.00 52.31  ? 108 LYS B C   1 
ATOM 2541 O O   . LYS B 2 108 ? 21.277  13.917  -35.299 1.00 54.60  ? 108 LYS B O   1 
ATOM 2542 C CB  . LYS B 2 108 ? 18.449  12.819  -35.106 1.00 54.18  ? 108 LYS B CB  1 
ATOM 2543 C CG  . LYS B 2 108 ? 17.718  13.051  -33.790 1.00 60.22  ? 108 LYS B CG  1 
ATOM 2544 C CD  . LYS B 2 108 ? 17.288  11.751  -33.130 1.00 71.00  ? 108 LYS B CD  1 
ATOM 2545 C CE  . LYS B 2 108 ? 18.476  10.895  -32.728 1.00 77.88  ? 108 LYS B CE  1 
ATOM 2546 N NZ  . LYS B 2 108 ? 18.045  9.712   -31.932 1.00 71.71  ? 108 LYS B NZ  1 
ATOM 2547 N N   . LEU B 2 109 ? 20.178  15.642  -34.348 1.00 50.85  ? 109 LEU B N   1 
ATOM 2548 C CA  . LEU B 2 109 ? 21.287  16.044  -33.499 1.00 52.32  ? 109 LEU B CA  1 
ATOM 2549 C C   . LEU B 2 109 ? 21.045  15.527  -32.089 1.00 60.06  ? 109 LEU B C   1 
ATOM 2550 O O   . LEU B 2 109 ? 19.972  15.735  -31.514 1.00 59.56  ? 109 LEU B O   1 
ATOM 2551 C CB  . LEU B 2 109 ? 21.467  17.562  -33.488 1.00 51.16  ? 109 LEU B CB  1 
ATOM 2552 C CG  . LEU B 2 109 ? 22.901  18.008  -33.177 1.00 51.16  ? 109 LEU B CG  1 
ATOM 2553 C CD1 . LEU B 2 109 ? 23.885  17.512  -34.234 1.00 53.08  ? 109 LEU B CD1 1 
ATOM 2554 C CD2 . LEU B 2 109 ? 22.988  19.520  -33.018 1.00 56.13  ? 109 LEU B CD2 1 
ATOM 2555 N N   . GLU B 2 110 ? 22.042  14.842  -31.551 1.00 60.53  ? 110 GLU B N   1 
ATOM 2556 C CA  . GLU B 2 110 ? 21.991  14.261  -30.223 1.00 61.44  ? 110 GLU B CA  1 
ATOM 2557 C C   . GLU B 2 110 ? 23.220  14.732  -29.461 1.00 63.67  ? 110 GLU B C   1 
ATOM 2558 O O   . GLU B 2 110 ? 24.300  14.882  -30.036 1.00 63.31  ? 110 GLU B O   1 
ATOM 2559 C CB  . GLU B 2 110 ? 21.925  12.723  -30.314 1.00 66.13  ? 110 GLU B CB  1 
ATOM 2560 C CG  . GLU B 2 110 ? 22.004  11.961  -29.002 1.00 70.04  ? 110 GLU B CG  1 
ATOM 2561 C CD  . GLU B 2 110 ? 21.868  10.460  -29.211 1.00 89.41  ? 110 GLU B CD  1 
ATOM 2562 O OE1 . GLU B 2 110 ? 21.479  10.046  -30.326 1.00 88.16  ? 110 GLU B OE1 1 
ATOM 2563 O OE2 . GLU B 2 110 ? 22.142  9.693   -28.266 1.00 85.64  ? 110 GLU B OE2 1 
ATOM 2564 N N   . ILE B 2 111 ? 23.044  15.003  -28.173 1.00 59.72  ? 111 ILE B N   1 
ATOM 2565 C CA  . ILE B 2 111 ? 24.109  15.554  -27.344 1.00 54.71  ? 111 ILE B CA  1 
ATOM 2566 C C   . ILE B 2 111 ? 24.781  14.416  -26.593 1.00 57.18  ? 111 ILE B C   1 
ATOM 2567 O O   . ILE B 2 111 ? 24.159  13.769  -25.742 1.00 53.60  ? 111 ILE B O   1 
ATOM 2568 C CB  . ILE B 2 111 ? 23.579  16.619  -26.372 1.00 57.20  ? 111 ILE B CB  1 
ATOM 2569 C CG1 . ILE B 2 111 ? 22.540  17.495  -27.063 1.00 64.11  ? 111 ILE B CG1 1 
ATOM 2570 C CG2 . ILE B 2 111 ? 24.716  17.480  -25.862 1.00 59.12  ? 111 ILE B CG2 1 
ATOM 2571 C CD1 . ILE B 2 111 ? 23.108  18.354  -28.170 1.00 62.50  ? 111 ILE B CD1 1 
ATOM 2572 N N   . LYS B 2 112 ? 26.053  14.181  -26.902 1.00 56.50  ? 112 LYS B N   1 
ATOM 2573 C CA  . LYS B 2 112 ? 26.855  13.162  -26.230 1.00 53.03  ? 112 LYS B CA  1 
ATOM 2574 C C   . LYS B 2 112 ? 27.188  13.643  -24.826 1.00 54.99  ? 112 LYS B C   1 
ATOM 2575 O O   . LYS B 2 112 ? 28.163  14.369  -24.623 1.00 58.23  ? 112 LYS B O   1 
ATOM 2576 C CB  . LYS B 2 112 ? 28.126  12.889  -27.026 1.00 52.50  ? 112 LYS B CB  1 
ATOM 2577 C CG  . LYS B 2 112 ? 28.383  11.427  -27.320 1.00 59.96  ? 112 LYS B CG  1 
ATOM 2578 C CD  . LYS B 2 112 ? 29.568  11.279  -28.257 1.00 66.81  ? 112 LYS B CD  1 
ATOM 2579 C CE  . LYS B 2 112 ? 29.693  9.858   -28.772 1.00 76.11  ? 112 LYS B CE  1 
ATOM 2580 N NZ  . LYS B 2 112 ? 30.766  9.725   -29.796 1.00 75.31  ? 112 LYS B NZ  1 
ATOM 2581 N N   . ARG B 2 113 ? 26.393  13.236  -23.844 1.00 51.83  ? 113 ARG B N   1 
ATOM 2582 C CA  . ARG B 2 113 ? 26.568  13.710  -22.483 1.00 50.88  ? 113 ARG B CA  1 
ATOM 2583 C C   . ARG B 2 113 ? 27.146  12.607  -21.596 1.00 54.54  ? 113 ARG B C   1 
ATOM 2584 O O   . ARG B 2 113 ? 27.551  11.536  -22.067 1.00 53.77  ? 113 ARG B O   1 
ATOM 2585 C CB  . ARG B 2 113 ? 25.243  14.219  -21.915 1.00 51.14  ? 113 ARG B CB  1 
ATOM 2586 C CG  . ARG B 2 113 ? 24.149  13.172  -21.864 1.00 52.11  ? 113 ARG B CG  1 
ATOM 2587 C CD  . ARG B 2 113 ? 23.298  13.375  -20.624 1.00 53.19  ? 113 ARG B CD  1 
ATOM 2588 N NE  . ARG B 2 113 ? 24.044  13.007  -19.425 1.00 52.91  ? 113 ARG B NE  1 
ATOM 2589 C CZ  . ARG B 2 113 ? 23.638  13.230  -18.182 1.00 56.80  ? 113 ARG B CZ  1 
ATOM 2590 N NH1 . ARG B 2 113 ? 22.484  13.821  -17.928 1.00 58.78  ? 113 ARG B NH1 1 
ATOM 2591 N NH2 . ARG B 2 113 ? 24.413  12.853  -17.168 1.00 59.55  ? 113 ARG B NH2 1 
ATOM 2592 N N   . THR B 2 114 ? 27.168  12.879  -20.294 1.00 58.21  ? 114 THR B N   1 
ATOM 2593 C CA  . THR B 2 114 ? 27.698  11.944  -19.313 1.00 53.31  ? 114 THR B CA  1 
ATOM 2594 C C   . THR B 2 114 ? 26.799  10.718  -19.187 1.00 53.11  ? 114 THR B C   1 
ATOM 2595 O O   . THR B 2 114 ? 25.570  10.831  -19.157 1.00 52.44  ? 114 THR B O   1 
ATOM 2596 C CB  . THR B 2 114 ? 27.828  12.645  -17.960 1.00 52.60  ? 114 THR B CB  1 
ATOM 2597 O OG1 . THR B 2 114 ? 28.997  13.473  -17.956 1.00 54.26  ? 114 THR B OG1 1 
ATOM 2598 C CG2 . THR B 2 114 ? 27.919  11.645  -16.828 1.00 53.15  ? 114 THR B CG2 1 
ATOM 2599 N N   . VAL B 2 115 ? 27.421  9.538   -19.115 1.00 52.44  ? 115 VAL B N   1 
ATOM 2600 C CA  . VAL B 2 115 ? 26.671  8.311   -18.869 1.00 52.73  ? 115 VAL B CA  1 
ATOM 2601 C C   . VAL B 2 115 ? 25.904  8.441   -17.561 1.00 53.27  ? 115 VAL B C   1 
ATOM 2602 O O   . VAL B 2 115 ? 26.471  8.808   -16.527 1.00 53.64  ? 115 VAL B O   1 
ATOM 2603 C CB  . VAL B 2 115 ? 27.622  7.104   -18.847 1.00 52.88  ? 115 VAL B CB  1 
ATOM 2604 C CG1 . VAL B 2 115 ? 26.835  5.805   -18.836 1.00 53.15  ? 115 VAL B CG1 1 
ATOM 2605 C CG2 . VAL B 2 115 ? 28.563  7.150   -20.042 1.00 63.31  ? 115 VAL B CG2 1 
ATOM 2606 N N   . ALA B 2 116 ? 24.603  8.162   -17.603 1.00 53.34  ? 116 ALA B N   1 
ATOM 2607 C CA  . ALA B 2 116 ? 23.751  8.251   -16.425 1.00 53.82  ? 116 ALA B CA  1 
ATOM 2608 C C   . ALA B 2 116 ? 23.014  6.930   -16.243 1.00 54.12  ? 116 ALA B C   1 
ATOM 2609 O O   . ALA B 2 116 ? 23.125  6.015   -17.063 1.00 56.67  ? 116 ALA B O   1 
ATOM 2610 C CB  . ALA B 2 116 ? 22.765  9.421   -16.531 1.00 53.65  ? 116 ALA B CB  1 
ATOM 2611 N N   . ALA B 2 117 ? 22.248  6.830   -15.157 1.00 54.60  ? 117 ALA B N   1 
ATOM 2612 C CA  . ALA B 2 117 ? 21.584  5.589   -14.794 1.00 54.97  ? 117 ALA B CA  1 
ATOM 2613 C C   . ALA B 2 117 ? 20.093  5.820   -14.583 1.00 55.03  ? 117 ALA B C   1 
ATOM 2614 O O   . ALA B 2 117 ? 19.690  6.880   -14.090 1.00 57.68  ? 117 ALA B O   1 
ATOM 2615 C CB  . ALA B 2 117 ? 22.204  4.993   -13.521 1.00 55.64  ? 117 ALA B CB  1 
ATOM 2616 N N   . PRO B 2 118 ? 19.251  4.853   -14.947 1.00 55.07  ? 118 PRO B N   1 
ATOM 2617 C CA  . PRO B 2 118 ? 17.799  5.060   -14.833 1.00 55.71  ? 118 PRO B CA  1 
ATOM 2618 C C   . PRO B 2 118 ? 17.329  4.987   -13.386 1.00 60.48  ? 118 PRO B C   1 
ATOM 2619 O O   . PRO B 2 118 ? 17.718  4.092   -12.633 1.00 67.27  ? 118 PRO B O   1 
ATOM 2620 C CB  . PRO B 2 118 ? 17.210  3.914   -15.666 1.00 57.62  ? 118 PRO B CB  1 
ATOM 2621 C CG  . PRO B 2 118 ? 18.278  2.870   -15.678 1.00 59.88  ? 118 PRO B CG  1 
ATOM 2622 C CD  . PRO B 2 118 ? 19.575  3.617   -15.682 1.00 56.46  ? 118 PRO B CD  1 
ATOM 2623 N N   . SER B 2 119 ? 16.480  5.939   -13.004 1.00 65.21  ? 119 SER B N   1 
ATOM 2624 C CA  . SER B 2 119 ? 15.766  5.872   -11.732 1.00 66.86  ? 119 SER B CA  1 
ATOM 2625 C C   . SER B 2 119 ? 14.508  5.048   -11.960 1.00 68.40  ? 119 SER B C   1 
ATOM 2626 O O   . SER B 2 119 ? 13.508  5.547   -12.480 1.00 71.02  ? 119 SER B O   1 
ATOM 2627 C CB  . SER B 2 119 ? 15.440  7.270   -11.218 1.00 72.08  ? 119 SER B CB  1 
ATOM 2628 O OG  . SER B 2 119 ? 16.590  8.096   -11.214 1.00 80.61  ? 119 SER B OG  1 
ATOM 2629 N N   . VAL B 2 120 ? 14.556  3.777   -11.580 1.00 67.09  ? 120 VAL B N   1 
ATOM 2630 C CA  . VAL B 2 120 ? 13.499  2.829   -11.907 1.00 60.65  ? 120 VAL B CA  1 
ATOM 2631 C C   . VAL B 2 120 ? 12.396  2.904   -10.862 1.00 63.94  ? 120 VAL B C   1 
ATOM 2632 O O   . VAL B 2 120 ? 12.653  2.796   -9.658  1.00 76.29  ? 120 VAL B O   1 
ATOM 2633 C CB  . VAL B 2 120 ? 14.055  1.401   -12.015 1.00 64.27  ? 120 VAL B CB  1 
ATOM 2634 C CG1 . VAL B 2 120 ? 12.997  0.480   -12.591 1.00 68.86  ? 120 VAL B CG1 1 
ATOM 2635 C CG2 . VAL B 2 120 ? 15.305  1.392   -12.879 1.00 66.67  ? 120 VAL B CG2 1 
ATOM 2636 N N   . PHE B 2 121 ? 11.164  3.082   -11.329 1.00 64.05  ? 121 PHE B N   1 
ATOM 2637 C CA  . PHE B 2 121 ? 9.980   3.048   -10.488 1.00 72.02  ? 121 PHE B CA  1 
ATOM 2638 C C   . PHE B 2 121 ? 8.997   2.072   -11.116 1.00 74.45  ? 121 PHE B C   1 
ATOM 2639 O O   . PHE B 2 121 ? 8.974   1.904   -12.338 1.00 76.12  ? 121 PHE B O   1 
ATOM 2640 C CB  . PHE B 2 121 ? 9.331   4.430   -10.367 1.00 78.35  ? 121 PHE B CB  1 
ATOM 2641 C CG  . PHE B 2 121 ? 10.314  5.565   -10.319 1.00 77.85  ? 121 PHE B CG  1 
ATOM 2642 C CD1 . PHE B 2 121 ? 11.107  5.777   -9.207  1.00 79.62  ? 121 PHE B CD1 1 
ATOM 2643 C CD2 . PHE B 2 121 ? 10.423  6.438   -11.389 1.00 79.45  ? 121 PHE B CD2 1 
ATOM 2644 C CE1 . PHE B 2 121 ? 12.002  6.826   -9.169  1.00 79.30  ? 121 PHE B CE1 1 
ATOM 2645 C CE2 . PHE B 2 121 ? 11.315  7.493   -11.356 1.00 77.66  ? 121 PHE B CE2 1 
ATOM 2646 C CZ  . PHE B 2 121 ? 12.106  7.685   -10.240 1.00 77.26  ? 121 PHE B CZ  1 
ATOM 2647 N N   . ILE B 2 122 ? 8.186   1.425   -10.283 1.00 79.02  ? 122 ILE B N   1 
ATOM 2648 C CA  . ILE B 2 122 ? 7.195   0.469   -10.765 1.00 73.82  ? 122 ILE B CA  1 
ATOM 2649 C C   . ILE B 2 122 ? 5.846   0.793   -10.137 1.00 74.59  ? 122 ILE B C   1 
ATOM 2650 O O   . ILE B 2 122 ? 5.754   1.021   -8.925  1.00 83.94  ? 122 ILE B O   1 
ATOM 2651 C CB  . ILE B 2 122 ? 7.610   -0.990  -10.479 1.00 77.04  ? 122 ILE B CB  1 
ATOM 2652 C CG1 . ILE B 2 122 ? 6.543   -1.960  -10.990 1.00 78.69  ? 122 ILE B CG1 1 
ATOM 2653 C CG2 . ILE B 2 122 ? 7.895   -1.211  -9.001  1.00 81.86  ? 122 ILE B CG2 1 
ATOM 2654 C CD1 . ILE B 2 122 ? 7.019   -3.389  -11.081 1.00 74.88  ? 122 ILE B CD1 1 
ATOM 2655 N N   . PHE B 2 123 ? 4.803   0.825   -10.967 1.00 72.95  ? 123 PHE B N   1 
ATOM 2656 C CA  . PHE B 2 123 ? 3.460   1.181   -10.529 1.00 73.41  ? 123 PHE B CA  1 
ATOM 2657 C C   . PHE B 2 123 ? 2.540   -0.023  -10.656 1.00 78.38  ? 123 PHE B C   1 
ATOM 2658 O O   . PHE B 2 123 ? 2.413   -0.585  -11.755 1.00 80.88  ? 123 PHE B O   1 
ATOM 2659 C CB  . PHE B 2 123 ? 2.919   2.351   -11.352 1.00 74.24  ? 123 PHE B CB  1 
ATOM 2660 C CG  . PHE B 2 123 ? 3.800   3.571   -11.334 1.00 77.18  ? 123 PHE B CG  1 
ATOM 2661 C CD1 . PHE B 2 123 ? 3.737   4.476   -10.287 1.00 83.48  ? 123 PHE B CD1 1 
ATOM 2662 C CD2 . PHE B 2 123 ? 4.693   3.812   -12.367 1.00 76.13  ? 123 PHE B CD2 1 
ATOM 2663 C CE1 . PHE B 2 123 ? 4.547   5.599   -10.271 1.00 87.36  ? 123 PHE B CE1 1 
ATOM 2664 C CE2 . PHE B 2 123 ? 5.506   4.933   -12.355 1.00 78.72  ? 123 PHE B CE2 1 
ATOM 2665 C CZ  . PHE B 2 123 ? 5.431   5.827   -11.305 1.00 84.44  ? 123 PHE B CZ  1 
ATOM 2666 N N   . PRO B 2 124 ? 1.888   -0.455  -9.580  1.00 87.81  ? 124 PRO B N   1 
ATOM 2667 C CA  . PRO B 2 124 ? 0.904   -1.534  -9.684  1.00 85.44  ? 124 PRO B CA  1 
ATOM 2668 C C   . PRO B 2 124 ? -0.367  -1.040  -10.350 1.00 82.66  ? 124 PRO B C   1 
ATOM 2669 O O   . PRO B 2 124 ? -0.569  0.175   -10.494 1.00 79.44  ? 124 PRO B O   1 
ATOM 2670 C CB  . PRO B 2 124 ? 0.663   -1.921  -8.218  1.00 81.75  ? 124 PRO B CB  1 
ATOM 2671 C CG  . PRO B 2 124 ? 0.892   -0.656  -7.473  1.00 89.16  ? 124 PRO B CG  1 
ATOM 2672 C CD  . PRO B 2 124 ? 2.019   0.041   -8.198  1.00 91.09  ? 124 PRO B CD  1 
ATOM 2673 N N   . PRO B 2 125 ? -1.247  -1.945  -10.777 1.00 80.87  ? 125 PRO B N   1 
ATOM 2674 C CA  . PRO B 2 125 ? -2.446  -1.518  -11.504 1.00 79.36  ? 125 PRO B CA  1 
ATOM 2675 C C   . PRO B 2 125 ? -3.428  -0.781  -10.608 1.00 77.50  ? 125 PRO B C   1 
ATOM 2676 O O   . PRO B 2 125 ? -3.446  -0.934  -9.384  1.00 81.67  ? 125 PRO B O   1 
ATOM 2677 C CB  . PRO B 2 125 ? -3.038  -2.840  -12.001 1.00 78.24  ? 125 PRO B CB  1 
ATOM 2678 C CG  . PRO B 2 125 ? -2.593  -3.828  -10.976 1.00 81.53  ? 125 PRO B CG  1 
ATOM 2679 C CD  . PRO B 2 125 ? -1.179  -3.414  -10.681 1.00 82.97  ? 125 PRO B CD  1 
ATOM 2680 N N   . SER B 2 126 ? -4.256  0.036   -11.250 1.00 80.23  ? 126 SER B N   1 
ATOM 2681 C CA  . SER B 2 126 ? -5.272  0.794   -10.538 1.00 77.98  ? 126 SER B CA  1 
ATOM 2682 C C   . SER B 2 126 ? -6.407  -0.116  -10.086 1.00 79.22  ? 126 SER B C   1 
ATOM 2683 O O   . SER B 2 126 ? -6.702  -1.139  -10.709 1.00 82.63  ? 126 SER B O   1 
ATOM 2684 C CB  . SER B 2 126 ? -5.828  1.902   -11.430 1.00 79.32  ? 126 SER B CB  1 
ATOM 2685 O OG  . SER B 2 126 ? -7.068  1.516   -12.000 1.00 79.50  ? 126 SER B OG  1 
ATOM 2686 N N   . ASP B 2 127 ? -7.049  0.270   -8.981  1.00 81.09  ? 127 ASP B N   1 
ATOM 2687 C CA  . ASP B 2 127 ? -8.243  -0.445  -8.545  1.00 85.95  ? 127 ASP B CA  1 
ATOM 2688 C C   . ASP B 2 127 ? -9.350  -0.334  -9.584  1.00 87.98  ? 127 ASP B C   1 
ATOM 2689 O O   . ASP B 2 127 ? -10.091 -1.295  -9.821  1.00 94.70  ? 127 ASP B O   1 
ATOM 2690 C CB  . ASP B 2 127 ? -8.723  0.096   -7.199  1.00 96.23  ? 127 ASP B CB  1 
ATOM 2691 C CG  . ASP B 2 127 ? -7.675  -0.026  -6.115  1.00 103.76 ? 127 ASP B CG  1 
ATOM 2692 O OD1 . ASP B 2 127 ? -6.748  -0.846  -6.274  1.00 92.96  ? 127 ASP B OD1 1 
ATOM 2693 O OD2 . ASP B 2 127 ? -7.784  0.693   -5.099  1.00 108.47 ? 127 ASP B OD2 1 
ATOM 2694 N N   . SER B 2 128 ? -9.469  0.834   -10.220 1.00 85.02  ? 128 SER B N   1 
ATOM 2695 C CA  . SER B 2 128 ? -10.502 1.034   -11.230 1.00 86.42  ? 128 SER B CA  1 
ATOM 2696 C C   . SER B 2 128 ? -10.287 0.126   -12.434 1.00 86.99  ? 128 SER B C   1 
ATOM 2697 O O   . SER B 2 128 ? -11.250 -0.410  -12.995 1.00 89.09  ? 128 SER B O   1 
ATOM 2698 C CB  . SER B 2 128 ? -10.528 2.497   -11.668 1.00 82.67  ? 128 SER B CB  1 
ATOM 2699 O OG  . SER B 2 128 ? -11.599 2.736   -12.563 1.00 89.67  ? 128 SER B OG  1 
ATOM 2700 N N   . GLN B 2 129 ? -9.030  -0.051  -12.852 1.00 86.89  ? 129 GLN B N   1 
ATOM 2701 C CA  . GLN B 2 129 ? -8.748  -0.893  -14.011 1.00 84.11  ? 129 GLN B CA  1 
ATOM 2702 C C   . GLN B 2 129 ? -9.127  -2.342  -13.748 1.00 91.78  ? 129 GLN B C   1 
ATOM 2703 O O   . GLN B 2 129 ? -9.698  -3.008  -14.620 1.00 95.93  ? 129 GLN B O   1 
ATOM 2704 C CB  . GLN B 2 129 ? -7.273  -0.803  -14.395 1.00 78.61  ? 129 GLN B CB  1 
ATOM 2705 C CG  . GLN B 2 129 ? -7.022  -1.137  -15.856 1.00 77.43  ? 129 GLN B CG  1 
ATOM 2706 C CD  . GLN B 2 129 ? -5.560  -1.075  -16.242 1.00 73.89  ? 129 GLN B CD  1 
ATOM 2707 O OE1 . GLN B 2 129 ? -5.199  -1.378  -17.380 1.00 68.83  ? 129 GLN B OE1 1 
ATOM 2708 N NE2 . GLN B 2 129 ? -4.709  -0.692  -15.297 1.00 73.95  ? 129 GLN B NE2 1 
ATOM 2709 N N   . LEU B 2 130 ? -8.797  -2.856  -12.561 1.00 90.39  ? 130 LEU B N   1 
ATOM 2710 C CA  . LEU B 2 130 ? -9.190  -4.219  -12.219 1.00 87.87  ? 130 LEU B CA  1 
ATOM 2711 C C   . LEU B 2 130 ? -10.699 -4.388  -12.333 1.00 89.57  ? 130 LEU B C   1 
ATOM 2712 O O   . LEU B 2 130 ? -11.180 -5.391  -12.872 1.00 89.91  ? 130 LEU B O   1 
ATOM 2713 C CB  . LEU B 2 130 ? -8.703  -4.571  -10.812 1.00 84.09  ? 130 LEU B CB  1 
ATOM 2714 C CG  . LEU B 2 130 ? -7.302  -5.178  -10.651 1.00 83.97  ? 130 LEU B CG  1 
ATOM 2715 C CD1 . LEU B 2 130 ? -7.253  -6.565  -11.275 1.00 85.86  ? 130 LEU B CD1 1 
ATOM 2716 C CD2 . LEU B 2 130 ? -6.209  -4.293  -11.233 1.00 82.66  ? 130 LEU B CD2 1 
ATOM 2717 N N   . LYS B 2 131 ? -11.461 -3.400  -11.859 1.00 90.61  ? 131 LYS B N   1 
ATOM 2718 C CA  . LYS B 2 131 ? -12.907 -3.428  -12.041 1.00 91.12  ? 131 LYS B CA  1 
ATOM 2719 C C   . LYS B 2 131 ? -13.274 -3.437  -13.521 1.00 97.06  ? 131 LYS B C   1 
ATOM 2720 O O   . LYS B 2 131 ? -14.271 -4.051  -13.920 1.00 104.85 ? 131 LYS B O   1 
ATOM 2721 C CB  . LYS B 2 131 ? -13.540 -2.231  -11.335 1.00 85.73  ? 131 LYS B CB  1 
ATOM 2722 C CG  . LYS B 2 131 ? -14.876 -2.521  -10.677 1.00 86.25  ? 131 LYS B CG  1 
ATOM 2723 C CD  . LYS B 2 131 ? -15.237 -1.411  -9.704  1.00 88.57  ? 131 LYS B CD  1 
ATOM 2724 C CE  . LYS B 2 131 ? -16.509 -1.727  -8.937  1.00 92.88  ? 131 LYS B CE  1 
ATOM 2725 N NZ  . LYS B 2 131 ? -16.837 -0.653  -7.958  1.00 84.83  ? 131 LYS B NZ  1 
ATOM 2726 N N   . SER B 2 132 ? -12.472 -2.769  -14.353 1.00 100.30 ? 132 SER B N   1 
ATOM 2727 C CA  . SER B 2 132 ? -12.721 -2.738  -15.790 1.00 100.32 ? 132 SER B CA  1 
ATOM 2728 C C   . SER B 2 132 ? -12.428 -4.068  -16.473 1.00 101.20 ? 132 SER B C   1 
ATOM 2729 O O   . SER B 2 132 ? -12.813 -4.246  -17.633 1.00 101.36 ? 132 SER B O   1 
ATOM 2730 C CB  . SER B 2 132 ? -11.890 -1.630  -16.445 1.00 99.60  ? 132 SER B CB  1 
ATOM 2731 O OG  . SER B 2 132 ? -12.082 -0.386  -15.793 1.00 110.32 ? 132 SER B OG  1 
ATOM 2732 N N   . GLY B 2 133 ? -11.760 -5.000  -15.795 1.00 91.04  ? 133 GLY B N   1 
ATOM 2733 C CA  . GLY B 2 133 ? -11.477 -6.302  -16.361 1.00 90.62  ? 133 GLY B CA  1 
ATOM 2734 C C   . GLY B 2 133 ? -10.087 -6.474  -16.931 1.00 88.77  ? 133 GLY B C   1 
ATOM 2735 O O   . GLY B 2 133 ? -9.770  -7.563  -17.423 1.00 90.24  ? 133 GLY B O   1 
ATOM 2736 N N   . THR B 2 134 ? -9.252  -5.439  -16.889 1.00 85.84  ? 134 THR B N   1 
ATOM 2737 C CA  . THR B 2 134 ? -7.875  -5.526  -17.347 1.00 81.27  ? 134 THR B CA  1 
ATOM 2738 C C   . THR B 2 134 ? -6.948  -5.027  -16.250 1.00 80.23  ? 134 THR B C   1 
ATOM 2739 O O   . THR B 2 134 ? -7.355  -4.293  -15.348 1.00 82.31  ? 134 THR B O   1 
ATOM 2740 C CB  . THR B 2 134 ? -7.641  -4.712  -18.625 1.00 79.65  ? 134 THR B CB  1 
ATOM 2741 O OG1 . THR B 2 134 ? -8.131  -3.379  -18.438 1.00 85.60  ? 134 THR B OG1 1 
ATOM 2742 C CG2 . THR B 2 134 ? -8.342  -5.353  -19.810 1.00 75.37  ? 134 THR B CG2 1 
ATOM 2743 N N   . ALA B 2 135 ? -5.686  -5.434  -16.338 1.00 76.96  ? 135 ALA B N   1 
ATOM 2744 C CA  . ALA B 2 135 ? -4.670  -5.024  -15.379 1.00 73.84  ? 135 ALA B CA  1 
ATOM 2745 C C   . ALA B 2 135 ? -3.424  -4.584  -16.130 1.00 72.35  ? 135 ALA B C   1 
ATOM 2746 O O   . ALA B 2 135 ? -2.928  -5.313  -16.995 1.00 71.42  ? 135 ALA B O   1 
ATOM 2747 C CB  . ALA B 2 135 ? -4.339  -6.159  -14.408 1.00 79.48  ? 135 ALA B CB  1 
ATOM 2748 N N   . SER B 2 136 ? -2.919  -3.396  -15.801 1.00 72.67  ? 136 SER B N   1 
ATOM 2749 C CA  . SER B 2 136 ? -1.735  -2.843  -16.450 1.00 71.21  ? 136 SER B CA  1 
ATOM 2750 C C   . SER B 2 136 ? -0.720  -2.439  -15.393 1.00 68.63  ? 136 SER B C   1 
ATOM 2751 O O   . SER B 2 136 ? -1.006  -1.582  -14.550 1.00 71.23  ? 136 SER B O   1 
ATOM 2752 C CB  . SER B 2 136 ? -2.092  -1.639  -17.325 1.00 71.46  ? 136 SER B CB  1 
ATOM 2753 O OG  . SER B 2 136 ? -2.426  -0.519  -16.526 1.00 77.64  ? 136 SER B OG  1 
ATOM 2754 N N   . VAL B 2 137 ? 0.466   -3.039  -15.453 1.00 69.61  ? 137 VAL B N   1 
ATOM 2755 C CA  . VAL B 2 137 ? 1.580   -2.683  -14.583 1.00 72.05  ? 137 VAL B CA  1 
ATOM 2756 C C   . VAL B 2 137 ? 2.572   -1.852  -15.383 1.00 72.84  ? 137 VAL B C   1 
ATOM 2757 O O   . VAL B 2 137 ? 2.984   -2.251  -16.479 1.00 74.27  ? 137 VAL B O   1 
ATOM 2758 C CB  . VAL B 2 137 ? 2.257   -3.934  -14.000 1.00 66.94  ? 137 VAL B CB  1 
ATOM 2759 C CG1 . VAL B 2 137 ? 3.371   -3.526  -13.055 1.00 72.32  ? 137 VAL B CG1 1 
ATOM 2760 C CG2 . VAL B 2 137 ? 1.235   -4.809  -13.290 1.00 65.78  ? 137 VAL B CG2 1 
ATOM 2761 N N   . VAL B 2 138 ? 2.967   -0.707  -14.833 1.00 68.62  ? 138 VAL B N   1 
ATOM 2762 C CA  . VAL B 2 138 ? 3.852   0.233   -15.509 1.00 68.65  ? 138 VAL B CA  1 
ATOM 2763 C C   . VAL B 2 138 ? 5.225   0.188   -14.853 1.00 68.19  ? 138 VAL B C   1 
ATOM 2764 O O   . VAL B 2 138 ? 5.337   0.088   -13.626 1.00 73.32  ? 138 VAL B O   1 
ATOM 2765 C CB  . VAL B 2 138 ? 3.281   1.665   -15.478 1.00 72.58  ? 138 VAL B CB  1 
ATOM 2766 C CG1 . VAL B 2 138 ? 4.008   2.554   -16.479 1.00 69.04  ? 138 VAL B CG1 1 
ATOM 2767 C CG2 . VAL B 2 138 ? 1.786   1.646   -15.756 1.00 76.49  ? 138 VAL B CG2 1 
ATOM 2768 N N   . CYS B 2 139 ? 6.268   0.252   -15.678 1.00 68.96  ? 139 CYS B N   1 
ATOM 2769 C CA  . CYS B 2 139 ? 7.635   0.453   -15.222 1.00 67.51  ? 139 CYS B CA  1 
ATOM 2770 C C   . CYS B 2 139 ? 8.163   1.749   -15.817 1.00 64.57  ? 139 CYS B C   1 
ATOM 2771 O O   . CYS B 2 139 ? 7.940   2.035   -16.998 1.00 63.34  ? 139 CYS B O   1 
ATOM 2772 C CB  . CYS B 2 139 ? 8.547   -0.713  -15.619 1.00 68.40  ? 139 CYS B CB  1 
ATOM 2773 S SG  . CYS B 2 139 ? 10.142  -0.710  -14.767 1.00 82.03  ? 139 CYS B SG  1 
ATOM 2774 N N   . LEU B 2 140 ? 8.864   2.530   -15.001 1.00 65.09  ? 140 LEU B N   1 
ATOM 2775 C CA  . LEU B 2 140 ? 9.343   3.846   -15.399 1.00 60.82  ? 140 LEU B CA  1 
ATOM 2776 C C   . LEU B 2 140 ? 10.858  3.894   -15.278 1.00 61.60  ? 140 LEU B C   1 
ATOM 2777 O O   . LEU B 2 140 ? 11.417  3.532   -14.237 1.00 68.11  ? 140 LEU B O   1 
ATOM 2778 C CB  . LEU B 2 140 ? 8.706   4.945   -14.541 1.00 61.87  ? 140 LEU B CB  1 
ATOM 2779 C CG  . LEU B 2 140 ? 8.481   6.341   -15.136 1.00 63.65  ? 140 LEU B CG  1 
ATOM 2780 C CD1 . LEU B 2 140 ? 7.727   7.192   -14.132 1.00 71.27  ? 140 LEU B CD1 1 
ATOM 2781 C CD2 . LEU B 2 140 ? 9.774   7.033   -15.549 1.00 62.95  ? 140 LEU B CD2 1 
ATOM 2782 N N   . LEU B 2 141 ? 11.513  4.340   -16.343 1.00 58.12  ? 141 LEU B N   1 
ATOM 2783 C CA  . LEU B 2 141 ? 12.946  4.595   -16.360 1.00 58.49  ? 141 LEU B CA  1 
ATOM 2784 C C   . LEU B 2 141 ? 13.127  6.081   -16.623 1.00 60.43  ? 141 LEU B C   1 
ATOM 2785 O O   . LEU B 2 141 ? 12.725  6.571   -17.682 1.00 63.00  ? 141 LEU B O   1 
ATOM 2786 C CB  . LEU B 2 141 ? 13.637  3.770   -17.445 1.00 56.70  ? 141 LEU B CB  1 
ATOM 2787 C CG  . LEU B 2 141 ? 13.987  2.303   -17.205 1.00 56.85  ? 141 LEU B CG  1 
ATOM 2788 C CD1 . LEU B 2 141 ? 12.739  1.439   -17.073 1.00 57.92  ? 141 LEU B CD1 1 
ATOM 2789 C CD2 . LEU B 2 141 ? 14.851  1.825   -18.356 1.00 54.58  ? 141 LEU B CD2 1 
ATOM 2790 N N   . ASN B 2 142 ? 13.716  6.798   -15.671 1.00 63.55  ? 142 ASN B N   1 
ATOM 2791 C CA  . ASN B 2 142 ? 13.731  8.255   -15.709 1.00 59.13  ? 142 ASN B CA  1 
ATOM 2792 C C   . ASN B 2 142 ? 15.153  8.788   -15.803 1.00 59.66  ? 142 ASN B C   1 
ATOM 2793 O O   . ASN B 2 142 ? 16.028  8.383   -15.032 1.00 63.94  ? 142 ASN B O   1 
ATOM 2794 C CB  . ASN B 2 142 ? 13.041  8.845   -14.479 1.00 62.78  ? 142 ASN B CB  1 
ATOM 2795 C CG  . ASN B 2 142 ? 12.980  10.357  -14.522 1.00 71.46  ? 142 ASN B CG  1 
ATOM 2796 O OD1 . ASN B 2 142 ? 12.659  10.946  -15.552 1.00 75.84  ? 142 ASN B OD1 1 
ATOM 2797 N ND2 . ASN B 2 142 ? 13.297  10.996  -13.402 1.00 65.71  ? 142 ASN B ND2 1 
ATOM 2798 N N   . ASN B 2 143 ? 15.367  9.703   -16.746 1.00 57.81  ? 143 ASN B N   1 
ATOM 2799 C CA  . ASN B 2 143 ? 16.588  10.502  -16.855 1.00 57.06  ? 143 ASN B CA  1 
ATOM 2800 C C   . ASN B 2 143 ? 17.841  9.622   -16.901 1.00 55.03  ? 143 ASN B C   1 
ATOM 2801 O O   . ASN B 2 143 ? 18.632  9.550   -15.959 1.00 58.25  ? 143 ASN B O   1 
ATOM 2802 C CB  . ASN B 2 143 ? 16.663  11.526  -15.718 1.00 58.99  ? 143 ASN B CB  1 
ATOM 2803 C CG  . ASN B 2 143 ? 15.542  12.555  -15.783 1.00 61.65  ? 143 ASN B CG  1 
ATOM 2804 O OD1 . ASN B 2 143 ? 14.972  12.803  -16.847 1.00 64.87  ? 143 ASN B OD1 1 
ATOM 2805 N ND2 . ASN B 2 143 ? 15.241  13.176  -14.648 1.00 67.15  ? 143 ASN B ND2 1 
ATOM 2806 N N   . PHE B 2 144 ? 18.007  8.956   -18.044 1.00 53.26  ? 144 PHE B N   1 
ATOM 2807 C CA  . PHE B 2 144 ? 19.174  8.122   -18.285 1.00 53.25  ? 144 PHE B CA  1 
ATOM 2808 C C   . PHE B 2 144 ? 19.788  8.484   -19.631 1.00 52.72  ? 144 PHE B C   1 
ATOM 2809 O O   . PHE B 2 144 ? 19.185  9.179   -20.454 1.00 52.38  ? 144 PHE B O   1 
ATOM 2810 C CB  . PHE B 2 144 ? 18.827  6.625   -18.248 1.00 53.51  ? 144 PHE B CB  1 
ATOM 2811 C CG  . PHE B 2 144 ? 17.723  6.225   -19.187 1.00 53.29  ? 144 PHE B CG  1 
ATOM 2812 C CD1 . PHE B 2 144 ? 16.402  6.211   -18.771 1.00 53.47  ? 144 PHE B CD1 1 
ATOM 2813 C CD2 . PHE B 2 144 ? 18.015  5.836   -20.483 1.00 52.93  ? 144 PHE B CD2 1 
ATOM 2814 C CE1 . PHE B 2 144 ? 15.396  5.836   -19.641 1.00 53.30  ? 144 PHE B CE1 1 
ATOM 2815 C CE2 . PHE B 2 144 ? 17.015  5.458   -21.357 1.00 52.78  ? 144 PHE B CE2 1 
ATOM 2816 C CZ  . PHE B 2 144 ? 15.701  5.456   -20.933 1.00 52.97  ? 144 PHE B CZ  1 
ATOM 2817 N N   . TYR B 2 145 ? 21.011  7.998   -19.842 1.00 52.66  ? 145 TYR B N   1 
ATOM 2818 C CA  . TYR B 2 145 ? 21.763  8.170   -21.069 1.00 52.18  ? 145 TYR B CA  1 
ATOM 2819 C C   . TYR B 2 145 ? 22.774  7.034   -21.061 1.00 52.30  ? 145 TYR B C   1 
ATOM 2820 O O   . TYR B 2 145 ? 23.335  6.732   -19.996 1.00 52.70  ? 145 TYR B O   1 
ATOM 2821 C CB  . TYR B 2 145 ? 22.481  9.525   -21.152 1.00 51.94  ? 145 TYR B CB  1 
ATOM 2822 C CG  . TYR B 2 145 ? 23.167  9.780   -22.477 1.00 51.43  ? 145 TYR B CG  1 
ATOM 2823 C CD1 . TYR B 2 145 ? 22.455  10.270  -23.562 1.00 51.09  ? 145 TYR B CD1 1 
ATOM 2824 C CD2 . TYR B 2 145 ? 24.522  9.516   -22.648 1.00 51.32  ? 145 TYR B CD2 1 
ATOM 2825 C CE1 . TYR B 2 145 ? 23.075  10.502  -24.780 1.00 51.04  ? 145 TYR B CE1 1 
ATOM 2826 C CE2 . TYR B 2 145 ? 25.149  9.742   -23.859 1.00 50.85  ? 145 TYR B CE2 1 
ATOM 2827 C CZ  . TYR B 2 145 ? 24.421  10.234  -24.921 1.00 50.53  ? 145 TYR B CZ  1 
ATOM 2828 O OH  . TYR B 2 145 ? 25.037  10.462  -26.130 1.00 56.22  ? 145 TYR B OH  1 
ATOM 2829 N N   . PRO B 2 146 ? 23.027  6.378   -22.204 1.00 52.01  ? 146 PRO B N   1 
ATOM 2830 C CA  . PRO B 2 146 ? 22.405  6.584   -23.518 1.00 51.60  ? 146 PRO B CA  1 
ATOM 2831 C C   . PRO B 2 146 ? 20.951  6.118   -23.614 1.00 52.98  ? 146 PRO B C   1 
ATOM 2832 O O   . PRO B 2 146 ? 20.372  5.652   -22.634 1.00 52.17  ? 146 PRO B O   1 
ATOM 2833 C CB  . PRO B 2 146 ? 23.285  5.742   -24.444 1.00 51.40  ? 146 PRO B CB  1 
ATOM 2834 C CG  . PRO B 2 146 ? 24.610  5.727   -23.774 1.00 51.51  ? 146 PRO B CG  1 
ATOM 2835 C CD  . PRO B 2 146 ? 24.273  5.600   -22.317 1.00 52.03  ? 146 PRO B CD  1 
ATOM 2836 N N   . ARG B 2 147 ? 20.379  6.252   -24.813 1.00 65.11  ? 147 ARG B N   1 
ATOM 2837 C CA  . ARG B 2 147 ? 18.999  5.831   -25.041 1.00 66.06  ? 147 ARG B CA  1 
ATOM 2838 C C   . ARG B 2 147 ? 18.843  4.325   -24.880 1.00 67.25  ? 147 ARG B C   1 
ATOM 2839 O O   . ARG B 2 147 ? 17.825  3.848   -24.365 1.00 68.42  ? 147 ARG B O   1 
ATOM 2840 C CB  . ARG B 2 147 ? 18.559  6.258   -26.440 1.00 66.60  ? 147 ARG B CB  1 
ATOM 2841 C CG  . ARG B 2 147 ? 17.098  6.013   -26.767 1.00 67.92  ? 147 ARG B CG  1 
ATOM 2842 C CD  . ARG B 2 147 ? 16.936  5.842   -28.271 1.00 73.96  ? 147 ARG B CD  1 
ATOM 2843 N NE  . ARG B 2 147 ? 15.546  5.908   -28.701 1.00 84.45  ? 147 ARG B NE  1 
ATOM 2844 C CZ  . ARG B 2 147 ? 14.997  6.967   -29.280 1.00 95.79  ? 147 ARG B CZ  1 
ATOM 2845 N NH1 . ARG B 2 147 ? 15.696  8.066   -29.517 1.00 90.44  ? 147 ARG B NH1 1 
ATOM 2846 N NH2 . ARG B 2 147 ? 13.716  6.922   -29.635 1.00 94.73  ? 147 ARG B NH2 1 
ATOM 2847 N N   . GLU B 2 148 ? 19.841  3.564   -25.316 1.00 55.48  ? 148 GLU B N   1 
ATOM 2848 C CA  . GLU B 2 148 ? 19.738  2.111   -25.370 1.00 54.45  ? 148 GLU B CA  1 
ATOM 2849 C C   . GLU B 2 148 ? 19.523  1.520   -23.982 1.00 58.93  ? 148 GLU B C   1 
ATOM 2850 O O   . GLU B 2 148 ? 20.339  1.719   -23.077 1.00 64.38  ? 148 GLU B O   1 
ATOM 2851 C CB  . GLU B 2 148 ? 20.999  1.543   -26.010 1.00 60.24  ? 148 GLU B CB  1 
ATOM 2852 C CG  . GLU B 2 148 ? 21.249  2.091   -27.405 1.00 68.83  ? 148 GLU B CG  1 
ATOM 2853 C CD  . GLU B 2 148 ? 22.533  2.888   -27.498 1.00 67.05  ? 148 GLU B CD  1 
ATOM 2854 O OE1 . GLU B 2 148 ? 23.425  2.678   -26.650 1.00 69.03  ? 148 GLU B OE1 1 
ATOM 2855 O OE2 . GLU B 2 148 ? 22.648  3.729   -28.414 1.00 65.88  ? 148 GLU B OE2 1 
ATOM 2856 N N   . ALA B 2 149 ? 18.423  0.786   -23.824 1.00 58.46  ? 149 ALA B N   1 
ATOM 2857 C CA  . ALA B 2 149 ? 18.086  0.153   -22.558 1.00 59.55  ? 149 ALA B CA  1 
ATOM 2858 C C   . ALA B 2 149 ? 17.275  -1.104  -22.832 1.00 64.90  ? 149 ALA B C   1 
ATOM 2859 O O   . ALA B 2 149 ? 16.703  -1.274  -23.912 1.00 73.96  ? 149 ALA B O   1 
ATOM 2860 C CB  . ALA B 2 149 ? 17.302  1.099   -21.641 1.00 53.65  ? 149 ALA B CB  1 
ATOM 2861 N N   . LYS B 2 150 ? 17.227  -1.982  -21.832 1.00 61.08  ? 150 LYS B N   1 
ATOM 2862 C CA  . LYS B 2 150 ? 16.456  -3.217  -21.895 1.00 61.74  ? 150 LYS B CA  1 
ATOM 2863 C C   . LYS B 2 150 ? 15.555  -3.291  -20.674 1.00 61.22  ? 150 LYS B C   1 
ATOM 2864 O O   . LYS B 2 150 ? 16.026  -3.140  -19.542 1.00 65.04  ? 150 LYS B O   1 
ATOM 2865 C CB  . LYS B 2 150 ? 17.368  -4.450  -21.958 1.00 68.22  ? 150 LYS B CB  1 
ATOM 2866 C CG  . LYS B 2 150 ? 18.298  -4.487  -23.165 1.00 71.99  ? 150 LYS B CG  1 
ATOM 2867 C CD  . LYS B 2 150 ? 19.649  -3.862  -22.849 1.00 76.53  ? 150 LYS B CD  1 
ATOM 2868 C CE  . LYS B 2 150 ? 20.544  -3.839  -24.076 1.00 77.09  ? 150 LYS B CE  1 
ATOM 2869 N NZ  . LYS B 2 150 ? 21.852  -3.193  -23.784 1.00 74.28  ? 150 LYS B NZ  1 
ATOM 2870 N N   . VAL B 2 151 ? 14.264  -3.516  -20.904 1.00 58.25  ? 151 VAL B N   1 
ATOM 2871 C CA  . VAL B 2 151 ? 13.262  -3.590  -19.844 1.00 62.57  ? 151 VAL B CA  1 
ATOM 2872 C C   . VAL B 2 151 ? 12.495  -4.889  -20.051 1.00 68.28  ? 151 VAL B C   1 
ATOM 2873 O O   . VAL B 2 151 ? 11.590  -4.956  -20.891 1.00 74.13  ? 151 VAL B O   1 
ATOM 2874 C CB  . VAL B 2 151 ? 12.318  -2.383  -19.845 1.00 67.38  ? 151 VAL B CB  1 
ATOM 2875 C CG1 . VAL B 2 151 ? 11.295  -2.503  -18.726 1.00 72.20  ? 151 VAL B CG1 1 
ATOM 2876 C CG2 . VAL B 2 151 ? 13.112  -1.098  -19.705 1.00 64.61  ? 151 VAL B CG2 1 
ATOM 2877 N N   . GLN B 2 152 ? 12.852  -5.922  -19.296 1.00 70.83  ? 152 GLN B N   1 
ATOM 2878 C CA  . GLN B 2 152 ? 12.187  -7.213  -19.375 1.00 71.97  ? 152 GLN B CA  1 
ATOM 2879 C C   . GLN B 2 152 ? 11.229  -7.382  -18.204 1.00 69.85  ? 152 GLN B C   1 
ATOM 2880 O O   . GLN B 2 152 ? 11.532  -6.982  -17.076 1.00 72.21  ? 152 GLN B O   1 
ATOM 2881 C CB  . GLN B 2 152 ? 13.205  -8.355  -19.386 1.00 72.93  ? 152 GLN B CB  1 
ATOM 2882 C CG  . GLN B 2 152 ? 13.796  -8.646  -20.756 1.00 73.67  ? 152 GLN B CG  1 
ATOM 2883 C CD  . GLN B 2 152 ? 14.782  -9.795  -20.726 1.00 75.59  ? 152 GLN B CD  1 
ATOM 2884 O OE1 . GLN B 2 152 ? 15.186  -10.251 -19.657 1.00 69.37  ? 152 GLN B OE1 1 
ATOM 2885 N NE2 . GLN B 2 152 ? 15.174  -10.271 -21.901 1.00 80.75  ? 152 GLN B NE2 1 
ATOM 2886 N N   . TRP B 2 153 ? 10.071  -7.971  -18.482 1.00 68.65  ? 153 TRP B N   1 
ATOM 2887 C CA  . TRP B 2 153 ? 9.051   -8.215  -17.473 1.00 68.99  ? 153 TRP B CA  1 
ATOM 2888 C C   . TRP B 2 153 ? 9.116   -9.670  -17.030 1.00 72.80  ? 153 TRP B C   1 
ATOM 2889 O O   . TRP B 2 153 ? 9.191   -10.576 -17.866 1.00 74.95  ? 153 TRP B O   1 
ATOM 2890 C CB  . TRP B 2 153 ? 7.659   -7.891  -18.014 1.00 70.76  ? 153 TRP B CB  1 
ATOM 2891 C CG  . TRP B 2 153 ? 7.388   -6.426  -18.151 1.00 72.91  ? 153 TRP B CG  1 
ATOM 2892 C CD1 . TRP B 2 153 ? 7.552   -5.666  -19.271 1.00 70.71  ? 153 TRP B CD1 1 
ATOM 2893 C CD2 . TRP B 2 153 ? 6.901   -5.542  -17.133 1.00 71.62  ? 153 TRP B CD2 1 
ATOM 2894 N NE1 . TRP B 2 153 ? 7.199   -4.363  -19.015 1.00 70.06  ? 153 TRP B NE1 1 
ATOM 2895 C CE2 . TRP B 2 153 ? 6.796   -4.261  -17.710 1.00 71.16  ? 153 TRP B CE2 1 
ATOM 2896 C CE3 . TRP B 2 153 ? 6.546   -5.709  -15.790 1.00 68.05  ? 153 TRP B CE3 1 
ATOM 2897 C CZ2 . TRP B 2 153 ? 6.350   -3.153  -16.992 1.00 71.02  ? 153 TRP B CZ2 1 
ATOM 2898 C CZ3 . TRP B 2 153 ? 6.103   -4.608  -15.081 1.00 67.43  ? 153 TRP B CZ3 1 
ATOM 2899 C CH2 . TRP B 2 153 ? 6.010   -3.347  -15.682 1.00 71.72  ? 153 TRP B CH2 1 
ATOM 2900 N N   . LYS B 2 154 ? 9.087   -9.887  -15.718 1.00 73.14  ? 154 LYS B N   1 
ATOM 2901 C CA  . LYS B 2 154 ? 9.123   -11.226 -15.145 1.00 68.36  ? 154 LYS B CA  1 
ATOM 2902 C C   . LYS B 2 154 ? 8.003   -11.357 -14.128 1.00 70.63  ? 154 LYS B C   1 
ATOM 2903 O O   . LYS B 2 154 ? 7.999   -10.653 -13.113 1.00 76.80  ? 154 LYS B O   1 
ATOM 2904 C CB  . LYS B 2 154 ? 10.477  -11.517 -14.490 1.00 64.52  ? 154 LYS B CB  1 
ATOM 2905 C CG  . LYS B 2 154 ? 11.612  -11.740 -15.474 1.00 64.75  ? 154 LYS B CG  1 
ATOM 2906 C CD  . LYS B 2 154 ? 12.907  -12.058 -14.747 1.00 64.92  ? 154 LYS B CD  1 
ATOM 2907 C CE  . LYS B 2 154 ? 14.016  -12.414 -15.723 1.00 60.74  ? 154 LYS B CE  1 
ATOM 2908 N NZ  . LYS B 2 154 ? 15.326  -12.601 -15.037 1.00 63.77  ? 154 LYS B NZ  1 
ATOM 2909 N N   . VAL B 2 155 ? 7.056   -12.250 -14.400 1.00 72.71  ? 155 VAL B N   1 
ATOM 2910 C CA  . VAL B 2 155 ? 5.989   -12.569 -13.463 1.00 74.72  ? 155 VAL B CA  1 
ATOM 2911 C C   . VAL B 2 155 ? 6.320   -13.924 -12.841 1.00 79.42  ? 155 VAL B C   1 
ATOM 2912 O O   . VAL B 2 155 ? 6.590   -14.900 -13.554 1.00 79.57  ? 155 VAL B O   1 
ATOM 2913 C CB  . VAL B 2 155 ? 4.608   -12.545 -14.148 1.00 70.57  ? 155 VAL B CB  1 
ATOM 2914 C CG1 . VAL B 2 155 ? 4.497   -11.324 -15.052 1.00 71.51  ? 155 VAL B CG1 1 
ATOM 2915 C CG2 . VAL B 2 155 ? 4.315   -13.812 -14.945 1.00 73.37  ? 155 VAL B CG2 1 
ATOM 2916 N N   . ASP B 2 156 ? 6.368   -13.964 -11.510 1.00 78.69  ? 156 ASP B N   1 
ATOM 2917 C CA  . ASP B 2 156 ? 6.765   -15.157 -10.760 1.00 77.17  ? 156 ASP B CA  1 
ATOM 2918 C C   . ASP B 2 156 ? 8.054   -15.762 -11.319 1.00 75.71  ? 156 ASP B C   1 
ATOM 2919 O O   . ASP B 2 156 ? 8.161   -16.970 -11.541 1.00 77.05  ? 156 ASP B O   1 
ATOM 2920 C CB  . ASP B 2 156 ? 5.633   -16.184 -10.741 1.00 81.82  ? 156 ASP B CB  1 
ATOM 2921 C CG  . ASP B 2 156 ? 4.390   -15.661 -10.051 1.00 83.40  ? 156 ASP B CG  1 
ATOM 2922 O OD1 . ASP B 2 156 ? 4.352   -14.453 -9.737  1.00 82.02  ? 156 ASP B OD1 1 
ATOM 2923 O OD2 . ASP B 2 156 ? 3.453   -16.454 -9.820  1.00 90.15  ? 156 ASP B OD2 1 
ATOM 2924 N N   . ASN B 2 157 ? 9.038   -14.892 -11.557 1.00 80.35  ? 157 ASN B N   1 
ATOM 2925 C CA  . ASN B 2 157 ? 10.342  -15.259 -12.112 1.00 79.13  ? 157 ASN B CA  1 
ATOM 2926 C C   . ASN B 2 157 ? 10.233  -15.931 -13.477 1.00 73.71  ? 157 ASN B C   1 
ATOM 2927 O O   . ASN B 2 157 ? 11.150  -16.647 -13.893 1.00 76.60  ? 157 ASN B O   1 
ATOM 2928 C CB  . ASN B 2 157 ? 11.132  -16.154 -11.151 1.00 78.06  ? 157 ASN B CB  1 
ATOM 2929 C CG  . ASN B 2 157 ? 12.172  -15.385 -10.362 1.00 88.51  ? 157 ASN B CG  1 
ATOM 2930 O OD1 . ASN B 2 157 ? 12.526  -14.259 -10.710 1.00 92.31  ? 157 ASN B OD1 1 
ATOM 2931 N ND2 . ASN B 2 157 ? 12.673  -15.994 -9.295  1.00 86.78  ? 157 ASN B ND2 1 
ATOM 2932 N N   . ALA B 2 158 ? 9.131   -15.716 -14.189 1.00 69.34  ? 158 ALA B N   1 
ATOM 2933 C CA  . ALA B 2 158 ? 8.946   -16.241 -15.536 1.00 70.07  ? 158 ALA B CA  1 
ATOM 2934 C C   . ALA B 2 158 ? 8.910   -15.063 -16.502 1.00 73.03  ? 158 ALA B C   1 
ATOM 2935 O O   . ALA B 2 158 ? 7.974   -14.255 -16.467 1.00 72.26  ? 158 ALA B O   1 
ATOM 2936 C CB  . ALA B 2 158 ? 7.673   -17.079 -15.634 1.00 72.61  ? 158 ALA B CB  1 
ATOM 2937 N N   . LEU B 2 159 ? 9.936   -14.962 -17.348 1.00 71.35  ? 159 LEU B N   1 
ATOM 2938 C CA  . LEU B 2 159 ? 9.985   -13.917 -18.361 1.00 69.08  ? 159 LEU B CA  1 
ATOM 2939 C C   . LEU B 2 159 ? 8.737   -13.964 -19.232 1.00 67.25  ? 159 LEU B C   1 
ATOM 2940 O O   . LEU B 2 159 ? 8.285   -15.036 -19.640 1.00 71.69  ? 159 LEU B O   1 
ATOM 2941 C CB  . LEU B 2 159 ? 11.240  -14.072 -19.226 1.00 66.56  ? 159 LEU B CB  1 
ATOM 2942 C CG  . LEU B 2 159 ? 11.401  -13.089 -20.391 1.00 69.06  ? 159 LEU B CG  1 
ATOM 2943 C CD1 . LEU B 2 159 ? 11.512  -11.662 -19.879 1.00 69.04  ? 159 LEU B CD1 1 
ATOM 2944 C CD2 . LEU B 2 159 ? 12.601  -13.446 -21.264 1.00 66.54  ? 159 LEU B CD2 1 
ATOM 2945 N N   . GLN B 2 160 ? 8.176   -12.789 -19.504 1.00 65.57  ? 160 GLN B N   1 
ATOM 2946 C CA  . GLN B 2 160 ? 6.935   -12.663 -20.254 1.00 70.46  ? 160 GLN B CA  1 
ATOM 2947 C C   . GLN B 2 160 ? 7.178   -11.824 -21.498 1.00 71.54  ? 160 GLN B C   1 
ATOM 2948 O O   . GLN B 2 160 ? 7.741   -10.727 -21.415 1.00 75.57  ? 160 GLN B O   1 
ATOM 2949 C CB  . GLN B 2 160 ? 5.836   -12.039 -19.390 1.00 69.28  ? 160 GLN B CB  1 
ATOM 2950 C CG  . GLN B 2 160 ? 5.191   -13.029 -18.433 1.00 71.95  ? 160 GLN B CG  1 
ATOM 2951 C CD  . GLN B 2 160 ? 3.702   -12.804 -18.253 1.00 75.13  ? 160 GLN B CD  1 
ATOM 2952 O OE1 . GLN B 2 160 ? 3.219   -11.674 -18.311 1.00 72.55  ? 160 GLN B OE1 1 
ATOM 2953 N NE2 . GLN B 2 160 ? 2.965   -13.887 -18.033 1.00 76.33  ? 160 GLN B NE2 1 
ATOM 2954 N N   . SER B 2 161 ? 6.747   -12.342 -22.644 1.00 71.25  ? 161 SER B N   1 
ATOM 2955 C CA  . SER B 2 161 ? 6.956   -11.708 -23.936 1.00 74.37  ? 161 SER B CA  1 
ATOM 2956 C C   . SER B 2 161 ? 5.625   -11.541 -24.652 1.00 75.59  ? 161 SER B C   1 
ATOM 2957 O O   . SER B 2 161 ? 4.780   -12.442 -24.629 1.00 79.08  ? 161 SER B O   1 
ATOM 2958 C CB  . SER B 2 161 ? 7.912   -12.532 -24.804 1.00 69.11  ? 161 SER B CB  1 
ATOM 2959 O OG  . SER B 2 161 ? 7.822   -12.149 -26.164 1.00 66.99  ? 161 SER B OG  1 
ATOM 2960 N N   . GLY B 2 162 ? 5.445   -10.386 -25.289 1.00 78.23  ? 162 GLY B N   1 
ATOM 2961 C CA  . GLY B 2 162 ? 4.263   -10.121 -26.080 1.00 80.15  ? 162 GLY B CA  1 
ATOM 2962 C C   . GLY B 2 162 ? 3.135   -9.419  -25.357 1.00 78.96  ? 162 GLY B C   1 
ATOM 2963 O O   . GLY B 2 162 ? 2.104   -9.139  -25.982 1.00 84.38  ? 162 GLY B O   1 
ATOM 2964 N N   . ASN B 2 163 ? 3.291   -9.121  -24.068 1.00 78.20  ? 163 ASN B N   1 
ATOM 2965 C CA  . ASN B 2 163 ? 2.243   -8.481  -23.286 1.00 78.00  ? 163 ASN B CA  1 
ATOM 2966 C C   . ASN B 2 163 ? 2.606   -7.061  -22.874 1.00 81.50  ? 163 ASN B C   1 
ATOM 2967 O O   . ASN B 2 163 ? 1.905   -6.468  -22.048 1.00 81.15  ? 163 ASN B O   1 
ATOM 2968 C CB  . ASN B 2 163 ? 1.923   -9.316  -22.044 1.00 73.29  ? 163 ASN B CB  1 
ATOM 2969 C CG  . ASN B 2 163 ? 3.170   -9.822  -21.341 1.00 79.05  ? 163 ASN B CG  1 
ATOM 2970 O OD1 . ASN B 2 163 ? 4.248   -9.236  -21.456 1.00 78.50  ? 163 ASN B OD1 1 
ATOM 2971 N ND2 . ASN B 2 163 ? 3.026   -10.913 -20.600 1.00 76.23  ? 163 ASN B ND2 1 
ATOM 2972 N N   . SER B 2 164 ? 3.681   -6.502  -23.426 1.00 78.19  ? 164 SER B N   1 
ATOM 2973 C CA  . SER B 2 164 ? 4.173   -5.194  -23.024 1.00 72.38  ? 164 SER B CA  1 
ATOM 2974 C C   . SER B 2 164 ? 4.462   -4.338  -24.248 1.00 75.70  ? 164 SER B C   1 
ATOM 2975 O O   . SER B 2 164 ? 4.832   -4.845  -25.311 1.00 76.21  ? 164 SER B O   1 
ATOM 2976 C CB  . SER B 2 164 ? 5.439   -5.315  -22.164 1.00 73.16  ? 164 SER B CB  1 
ATOM 2977 O OG  . SER B 2 164 ? 6.523   -5.812  -22.929 1.00 73.46  ? 164 SER B OG  1 
ATOM 2978 N N   . GLN B 2 165 ? 4.284   -3.030  -24.078 1.00 75.81  ? 165 GLN B N   1 
ATOM 2979 C CA  . GLN B 2 165 ? 4.615   -2.029  -25.082 1.00 73.53  ? 165 GLN B CA  1 
ATOM 2980 C C   . GLN B 2 165 ? 5.357   -0.895  -24.391 1.00 70.00  ? 165 GLN B C   1 
ATOM 2981 O O   . GLN B 2 165 ? 4.951   -0.449  -23.315 1.00 70.43  ? 165 GLN B O   1 
ATOM 2982 C CB  . GLN B 2 165 ? 3.357   -1.495  -25.781 1.00 70.20  ? 165 GLN B CB  1 
ATOM 2983 C CG  . GLN B 2 165 ? 3.302   -1.774  -27.277 1.00 71.36  ? 165 GLN B CG  1 
ATOM 2984 C CD  . GLN B 2 165 ? 1.896   -1.678  -27.840 1.00 83.87  ? 165 GLN B CD  1 
ATOM 2985 O OE1 . GLN B 2 165 ? 0.962   -1.277  -27.147 1.00 78.30  ? 165 GLN B OE1 1 
ATOM 2986 N NE2 . GLN B 2 165 ? 1.740   -2.050  -29.105 1.00 89.60  ? 165 GLN B NE2 1 
ATOM 2987 N N   . GLU B 2 166 ? 6.444   -0.435  -25.001 1.00 62.61  ? 166 GLU B N   1 
ATOM 2988 C CA  . GLU B 2 166 ? 7.290   0.574   -24.384 1.00 60.58  ? 166 GLU B CA  1 
ATOM 2989 C C   . GLU B 2 166 ? 7.355   1.826   -25.252 1.00 58.38  ? 166 GLU B C   1 
ATOM 2990 O O   . GLU B 2 166 ? 7.122   1.787   -26.463 1.00 57.56  ? 166 GLU B O   1 
ATOM 2991 C CB  . GLU B 2 166 ? 8.697   0.023   -24.123 1.00 60.93  ? 166 GLU B CB  1 
ATOM 2992 C CG  . GLU B 2 166 ? 9.653   0.141   -25.289 1.00 62.24  ? 166 GLU B CG  1 
ATOM 2993 C CD  . GLU B 2 166 ? 11.057  -0.278  -24.914 1.00 63.41  ? 166 GLU B CD  1 
ATOM 2994 O OE1 . GLU B 2 166 ? 11.222  -0.911  -23.851 1.00 59.04  ? 166 GLU B OE1 1 
ATOM 2995 O OE2 . GLU B 2 166 ? 11.996  0.032   -25.675 1.00 66.25  ? 166 GLU B OE2 1 
ATOM 2996 N N   . SER B 2 167 ? 7.672   2.946   -24.602 1.00 56.93  ? 167 SER B N   1 
ATOM 2997 C CA  . SER B 2 167 ? 7.739   4.251   -25.243 1.00 53.27  ? 167 SER B CA  1 
ATOM 2998 C C   . SER B 2 167 ? 8.871   5.052   -24.618 1.00 53.30  ? 167 SER B C   1 
ATOM 2999 O O   . SER B 2 167 ? 9.046   5.040   -23.397 1.00 56.93  ? 167 SER B O   1 
ATOM 3000 C CB  . SER B 2 167 ? 6.412   5.006   -25.104 1.00 52.60  ? 167 SER B CB  1 
ATOM 3001 O OG  . SER B 2 167 ? 6.421   6.206   -25.856 1.00 56.37  ? 167 SER B OG  1 
ATOM 3002 N N   . VAL B 2 168 ? 9.636   5.744   -25.458 1.00 52.19  ? 168 VAL B N   1 
ATOM 3003 C CA  . VAL B 2 168 ? 10.820  6.482   -25.029 1.00 52.06  ? 168 VAL B CA  1 
ATOM 3004 C C   . VAL B 2 168 ? 10.659  7.937   -25.443 1.00 51.77  ? 168 VAL B C   1 
ATOM 3005 O O   . VAL B 2 168 ? 10.435  8.231   -26.624 1.00 51.53  ? 168 VAL B O   1 
ATOM 3006 C CB  . VAL B 2 168 ? 12.109  5.892   -25.621 1.00 53.27  ? 168 VAL B CB  1 
ATOM 3007 C CG1 . VAL B 2 168 ? 13.325  6.429   -24.884 1.00 61.26  ? 168 VAL B CG1 1 
ATOM 3008 C CG2 . VAL B 2 168 ? 12.074  4.373   -25.566 1.00 53.77  ? 168 VAL B CG2 1 
ATOM 3009 N N   . THR B 2 169 ? 10.773  8.842   -24.474 1.00 57.42  ? 169 THR B N   1 
ATOM 3010 C CA  . THR B 2 169 ? 10.806  10.262  -24.781 1.00 53.86  ? 169 THR B CA  1 
ATOM 3011 C C   . THR B 2 169 ? 12.062  10.602  -25.575 1.00 56.83  ? 169 THR B C   1 
ATOM 3012 O O   . THR B 2 169 ? 13.027  9.834   -25.629 1.00 59.37  ? 169 THR B O   1 
ATOM 3013 C CB  . THR B 2 169 ? 10.767  11.098  -23.501 1.00 51.80  ? 169 THR B CB  1 
ATOM 3014 O OG1 . THR B 2 169 ? 11.963  10.873  -22.742 1.00 51.93  ? 169 THR B OG1 1 
ATOM 3015 C CG2 . THR B 2 169 ? 9.559   10.738  -22.659 1.00 52.09  ? 169 THR B CG2 1 
ATOM 3016 N N   . GLU B 2 170 ? 12.042  11.775  -26.201 1.00 54.91  ? 170 GLU B N   1 
ATOM 3017 C CA  . GLU B 2 170 ? 13.230  12.258  -26.881 1.00 58.00  ? 170 GLU B CA  1 
ATOM 3018 C C   . GLU B 2 170 ? 14.171  12.907  -25.870 1.00 57.76  ? 170 GLU B C   1 
ATOM 3019 O O   . GLU B 2 170 ? 13.869  13.018  -24.678 1.00 54.62  ? 170 GLU B O   1 
ATOM 3020 C CB  . GLU B 2 170 ? 12.854  13.228  -27.997 1.00 57.08  ? 170 GLU B CB  1 
ATOM 3021 C CG  . GLU B 2 170 ? 12.903  12.601  -29.377 1.00 72.67  ? 170 GLU B CG  1 
ATOM 3022 C CD  . GLU B 2 170 ? 14.319  12.310  -29.828 1.00 78.91  ? 170 GLU B CD  1 
ATOM 3023 O OE1 . GLU B 2 170 ? 15.214  13.134  -29.549 1.00 72.46  ? 170 GLU B OE1 1 
ATOM 3024 O OE2 . GLU B 2 170 ? 14.537  11.257  -30.463 1.00 83.51  ? 170 GLU B OE2 1 
ATOM 3025 N N   . GLN B 2 171 ? 15.331  13.345  -26.354 1.00 53.20  ? 171 GLN B N   1 
ATOM 3026 C CA  . GLN B 2 171 ? 16.337  13.929  -25.477 1.00 54.05  ? 171 GLN B CA  1 
ATOM 3027 C C   . GLN B 2 171 ? 15.836  15.239  -24.883 1.00 59.39  ? 171 GLN B C   1 
ATOM 3028 O O   . GLN B 2 171 ? 15.361  16.119  -25.607 1.00 62.94  ? 171 GLN B O   1 
ATOM 3029 C CB  . GLN B 2 171 ? 17.637  14.163  -26.245 1.00 52.52  ? 171 GLN B CB  1 
ATOM 3030 C CG  . GLN B 2 171 ? 18.878  13.689  -25.512 1.00 54.26  ? 171 GLN B CG  1 
ATOM 3031 C CD  . GLN B 2 171 ? 20.157  13.932  -26.291 1.00 54.21  ? 171 GLN B CD  1 
ATOM 3032 O OE1 . GLN B 2 171 ? 20.128  14.408  -27.425 1.00 53.26  ? 171 GLN B OE1 1 
ATOM 3033 N NE2 . GLN B 2 171 ? 21.289  13.588  -25.687 1.00 54.32  ? 171 GLN B NE2 1 
ATOM 3034 N N   . ASP B 2 172 ? 15.945  15.363  -23.561 1.00 61.40  ? 172 ASP B N   1 
ATOM 3035 C CA  . ASP B 2 172 ? 15.558  16.594  -22.885 1.00 60.18  ? 172 ASP B CA  1 
ATOM 3036 C C   . ASP B 2 172 ? 16.435  17.748  -23.354 1.00 64.98  ? 172 ASP B C   1 
ATOM 3037 O O   . ASP B 2 172 ? 17.665  17.668  -23.309 1.00 64.09  ? 172 ASP B O   1 
ATOM 3038 C CB  . ASP B 2 172 ? 15.677  16.418  -21.370 1.00 61.86  ? 172 ASP B CB  1 
ATOM 3039 C CG  . ASP B 2 172 ? 14.761  17.346  -20.595 1.00 66.61  ? 172 ASP B CG  1 
ATOM 3040 O OD1 . ASP B 2 172 ? 13.550  17.383  -20.900 1.00 69.98  ? 172 ASP B OD1 1 
ATOM 3041 O OD2 . ASP B 2 172 ? 15.252  18.031  -19.674 1.00 70.84  ? 172 ASP B OD2 1 
ATOM 3042 N N   . SER B 2 173 ? 15.796  18.828  -23.804 1.00 69.91  ? 173 SER B N   1 
ATOM 3043 C CA  . SER B 2 173 ? 16.525  19.993  -24.296 1.00 65.06  ? 173 SER B CA  1 
ATOM 3044 C C   . SER B 2 173 ? 17.311  20.709  -23.206 1.00 63.66  ? 173 SER B C   1 
ATOM 3045 O O   . SER B 2 173 ? 17.951  21.725  -23.500 1.00 66.70  ? 173 SER B O   1 
ATOM 3046 C CB  . SER B 2 173 ? 15.554  20.967  -24.967 1.00 64.74  ? 173 SER B CB  1 
ATOM 3047 O OG  . SER B 2 173 ? 14.762  21.645  -24.010 1.00 66.93  ? 173 SER B OG  1 
ATOM 3048 N N   . LYS B 2 174 ? 17.290  20.211  -21.971 1.00 68.97  ? 174 LYS B N   1 
ATOM 3049 C CA  . LYS B 2 174 ? 18.005  20.820  -20.859 1.00 71.84  ? 174 LYS B CA  1 
ATOM 3050 C C   . LYS B 2 174 ? 19.148  19.941  -20.367 1.00 69.57  ? 174 LYS B C   1 
ATOM 3051 O O   . LYS B 2 174 ? 20.305  20.369  -20.360 1.00 69.00  ? 174 LYS B O   1 
ATOM 3052 C CB  . LYS B 2 174 ? 17.022  21.113  -19.717 1.00 76.88  ? 174 LYS B CB  1 
ATOM 3053 C CG  . LYS B 2 174 ? 16.535  22.548  -19.675 1.00 78.06  ? 174 LYS B CG  1 
ATOM 3054 C CD  . LYS B 2 174 ? 15.274  22.667  -18.836 1.00 87.40  ? 174 LYS B CD  1 
ATOM 3055 C CE  . LYS B 2 174 ? 14.051  22.180  -19.601 1.00 86.14  ? 174 LYS B CE  1 
ATOM 3056 N NZ  . LYS B 2 174 ? 12.802  22.347  -18.807 1.00 85.42  ? 174 LYS B NZ  1 
ATOM 3057 N N   . ASP B 2 175 ? 18.849  18.711  -19.958 1.00 70.97  ? 175 ASP B N   1 
ATOM 3058 C CA  . ASP B 2 175 ? 19.842  17.795  -19.416 1.00 67.04  ? 175 ASP B CA  1 
ATOM 3059 C C   . ASP B 2 175 ? 20.196  16.655  -20.360 1.00 61.85  ? 175 ASP B C   1 
ATOM 3060 O O   . ASP B 2 175 ? 21.039  15.825  -20.009 1.00 60.84  ? 175 ASP B O   1 
ATOM 3061 C CB  . ASP B 2 175 ? 19.349  17.235  -18.077 1.00 62.24  ? 175 ASP B CB  1 
ATOM 3062 C CG  . ASP B 2 175 ? 17.925  16.723  -18.149 1.00 64.72  ? 175 ASP B CG  1 
ATOM 3063 O OD1 . ASP B 2 175 ? 17.693  15.697  -18.813 1.00 63.73  ? 175 ASP B OD1 1 
ATOM 3064 O OD2 . ASP B 2 175 ? 17.035  17.348  -17.534 1.00 70.20  ? 175 ASP B OD2 1 
ATOM 3065 N N   . SER B 2 176 ? 19.583  16.598  -21.544 1.00 61.17  ? 176 SER B N   1 
ATOM 3066 C CA  . SER B 2 176 ? 19.896  15.596  -22.568 1.00 63.07  ? 176 SER B CA  1 
ATOM 3067 C C   . SER B 2 176 ? 19.696  14.169  -22.067 1.00 63.58  ? 176 SER B C   1 
ATOM 3068 O O   . SER B 2 176 ? 20.406  13.250  -22.484 1.00 56.46  ? 176 SER B O   1 
ATOM 3069 C CB  . SER B 2 176 ? 21.317  15.770  -23.112 1.00 62.59  ? 176 SER B CB  1 
ATOM 3070 O OG  . SER B 2 176 ? 21.514  17.074  -23.628 1.00 58.13  ? 176 SER B OG  1 
ATOM 3071 N N   . THR B 2 177 ? 18.729  13.960  -21.183 1.00 67.42  ? 177 THR B N   1 
ATOM 3072 C CA  . THR B 2 177 ? 18.404  12.626  -20.702 1.00 66.32  ? 177 THR B CA  1 
ATOM 3073 C C   . THR B 2 177 ? 17.162  12.093  -21.402 1.00 64.98  ? 177 THR B C   1 
ATOM 3074 O O   . THR B 2 177 ? 16.406  12.834  -22.036 1.00 65.78  ? 177 THR B O   1 
ATOM 3075 C CB  . THR B 2 177 ? 18.178  12.622  -19.191 1.00 66.71  ? 177 THR B CB  1 
ATOM 3076 O OG1 . THR B 2 177 ? 17.056  13.457  -18.876 1.00 67.99  ? 177 THR B OG1 1 
ATOM 3077 C CG2 . THR B 2 177 ? 19.412  13.113  -18.458 1.00 66.48  ? 177 THR B CG2 1 
ATOM 3078 N N   . TYR B 2 178 ? 16.958  10.788  -21.274 1.00 62.93  ? 178 TYR B N   1 
ATOM 3079 C CA  . TYR B 2 178 ? 15.814  10.098  -21.849 1.00 53.07  ? 178 TYR B CA  1 
ATOM 3080 C C   . TYR B 2 178 ? 14.941  9.577   -20.716 1.00 52.44  ? 178 TYR B C   1 
ATOM 3081 O O   . TYR B 2 178 ? 15.348  9.545   -19.553 1.00 54.92  ? 178 TYR B O   1 
ATOM 3082 C CB  . TYR B 2 178 ? 16.261  8.935   -22.743 1.00 51.89  ? 178 TYR B CB  1 
ATOM 3083 C CG  . TYR B 2 178 ? 17.032  9.351   -23.977 1.00 51.46  ? 178 TYR B CG  1 
ATOM 3084 C CD1 . TYR B 2 178 ? 16.391  9.572   -25.189 1.00 55.65  ? 178 TYR B CD1 1 
ATOM 3085 C CD2 . TYR B 2 178 ? 18.410  9.507   -23.928 1.00 51.36  ? 178 TYR B CD2 1 
ATOM 3086 C CE1 . TYR B 2 178 ? 17.100  9.949   -26.314 1.00 59.37  ? 178 TYR B CE1 1 
ATOM 3087 C CE2 . TYR B 2 178 ? 19.129  9.883   -25.045 1.00 53.58  ? 178 TYR B CE2 1 
ATOM 3088 C CZ  . TYR B 2 178 ? 18.471  10.103  -26.236 1.00 57.02  ? 178 TYR B CZ  1 
ATOM 3089 O OH  . TYR B 2 178 ? 19.192  10.476  -27.349 1.00 62.79  ? 178 TYR B OH  1 
ATOM 3090 N N   . SER B 2 179 ? 13.730  9.154   -21.063 1.00 52.45  ? 179 SER B N   1 
ATOM 3091 C CA  . SER B 2 179 ? 12.867  8.454   -20.123 1.00 52.83  ? 179 SER B CA  1 
ATOM 3092 C C   . SER B 2 179 ? 12.072  7.392   -20.864 1.00 52.92  ? 179 SER B C   1 
ATOM 3093 O O   . SER B 2 179 ? 11.710  7.567   -22.030 1.00 58.71  ? 179 SER B O   1 
ATOM 3094 C CB  . SER B 2 179 ? 11.923  9.407   -19.378 1.00 55.09  ? 179 SER B CB  1 
ATOM 3095 O OG  . SER B 2 179 ? 12.652  10.426  -18.715 1.00 55.10  ? 179 SER B OG  1 
ATOM 3096 N N   . LEU B 2 180 ? 11.805  6.285   -20.177 1.00 54.76  ? 180 LEU B N   1 
ATOM 3097 C CA  . LEU B 2 180 ? 11.158  5.133   -20.783 1.00 55.96  ? 180 LEU B CA  1 
ATOM 3098 C C   . LEU B 2 180 ? 9.976   4.700   -19.928 1.00 57.01  ? 180 LEU B C   1 
ATOM 3099 O O   . LEU B 2 180 ? 10.034  4.757   -18.695 1.00 58.24  ? 180 LEU B O   1 
ATOM 3100 C CB  . LEU B 2 180 ? 12.154  3.974   -20.958 1.00 56.53  ? 180 LEU B CB  1 
ATOM 3101 C CG  . LEU B 2 180 ? 11.700  2.739   -21.739 1.00 57.49  ? 180 LEU B CG  1 
ATOM 3102 C CD1 . LEU B 2 180 ? 12.883  2.157   -22.494 1.00 56.37  ? 180 LEU B CD1 1 
ATOM 3103 C CD2 . LEU B 2 180 ? 11.087  1.685   -20.828 1.00 60.76  ? 180 LEU B CD2 1 
ATOM 3104 N N   . SER B 2 181 ? 8.905   4.272   -20.592 1.00 55.95  ? 181 SER B N   1 
ATOM 3105 C CA  . SER B 2 181 ? 7.695   3.797   -19.931 1.00 58.90  ? 181 SER B CA  1 
ATOM 3106 C C   . SER B 2 181 ? 7.248   2.505   -20.594 1.00 62.63  ? 181 SER B C   1 
ATOM 3107 O O   . SER B 2 181 ? 6.906   2.500   -21.781 1.00 63.61  ? 181 SER B O   1 
ATOM 3108 C CB  . SER B 2 181 ? 6.579   4.844   -19.995 1.00 57.93  ? 181 SER B CB  1 
ATOM 3109 O OG  . SER B 2 181 ? 5.322   4.260   -19.700 1.00 62.14  ? 181 SER B OG  1 
ATOM 3110 N N   . SER B 2 182 ? 7.249   1.417   -19.831 1.00 65.54  ? 182 SER B N   1 
ATOM 3111 C CA  . SER B 2 182 ? 6.814   0.113   -20.308 1.00 63.98  ? 182 SER B CA  1 
ATOM 3112 C C   . SER B 2 182 ? 5.572   -0.312  -19.538 1.00 64.04  ? 182 SER B C   1 
ATOM 3113 O O   . SER B 2 182 ? 5.507   -0.154  -18.315 1.00 66.98  ? 182 SER B O   1 
ATOM 3114 C CB  . SER B 2 182 ? 7.924   -0.931  -20.148 1.00 66.36  ? 182 SER B CB  1 
ATOM 3115 O OG  . SER B 2 182 ? 7.517   -2.190  -20.650 1.00 70.50  ? 182 SER B OG  1 
ATOM 3116 N N   . THR B 2 183 ? 4.589   -0.853  -20.255 1.00 64.18  ? 183 THR B N   1 
ATOM 3117 C CA  . THR B 2 183 ? 3.292   -1.194  -19.678 1.00 66.21  ? 183 THR B CA  1 
ATOM 3118 C C   . THR B 2 183 ? 2.978   -2.655  -19.972 1.00 75.45  ? 183 THR B C   1 
ATOM 3119 O O   . THR B 2 183 ? 2.666   -3.008  -21.114 1.00 78.19  ? 183 THR B O   1 
ATOM 3120 C CB  . THR B 2 183 ? 2.191   -0.287  -20.227 1.00 69.06  ? 183 THR B CB  1 
ATOM 3121 O OG1 . THR B 2 183 ? 2.671   1.062   -20.300 1.00 72.39  ? 183 THR B OG1 1 
ATOM 3122 C CG2 . THR B 2 183 ? 0.963   -0.334  -19.328 1.00 71.00  ? 183 THR B CG2 1 
ATOM 3123 N N   . LEU B 2 184 ? 3.059   -3.499  -18.945 1.00 72.37  ? 184 LEU B N   1 
ATOM 3124 C CA  . LEU B 2 184 ? 2.608   -4.882  -19.047 1.00 73.10  ? 184 LEU B CA  1 
ATOM 3125 C C   . LEU B 2 184 ? 1.102   -4.923  -18.817 1.00 70.92  ? 184 LEU B C   1 
ATOM 3126 O O   . LEU B 2 184 ? 0.622   -4.517  -17.754 1.00 67.38  ? 184 LEU B O   1 
ATOM 3127 C CB  . LEU B 2 184 ? 3.328   -5.762  -18.025 1.00 74.86  ? 184 LEU B CB  1 
ATOM 3128 C CG  . LEU B 2 184 ? 3.505   -7.262  -18.309 1.00 71.61  ? 184 LEU B CG  1 
ATOM 3129 C CD1 . LEU B 2 184 ? 4.218   -7.933  -17.146 1.00 68.49  ? 184 LEU B CD1 1 
ATOM 3130 C CD2 . LEU B 2 184 ? 2.194   -7.972  -18.604 1.00 75.70  ? 184 LEU B CD2 1 
ATOM 3131 N N   . THR B 2 185 ? 0.361   -5.421  -19.802 1.00 71.04  ? 185 THR B N   1 
ATOM 3132 C CA  . THR B 2 185 ? -1.090  -5.510  -19.727 1.00 71.89  ? 185 THR B CA  1 
ATOM 3133 C C   . THR B 2 185 ? -1.531  -6.959  -19.864 1.00 73.97  ? 185 THR B C   1 
ATOM 3134 O O   . THR B 2 185 ? -0.983  -7.713  -20.676 1.00 72.08  ? 185 THR B O   1 
ATOM 3135 C CB  . THR B 2 185 ? -1.758  -4.672  -20.817 1.00 74.67  ? 185 THR B CB  1 
ATOM 3136 O OG1 . THR B 2 185 ? -1.294  -5.106  -22.101 1.00 85.69  ? 185 THR B OG1 1 
ATOM 3137 C CG2 . THR B 2 185 ? -1.423  -3.206  -20.637 1.00 73.17  ? 185 THR B CG2 1 
ATOM 3138 N N   . LEU B 2 186 ? -2.533  -7.336  -19.075 1.00 74.80  ? 186 LEU B N   1 
ATOM 3139 C CA  . LEU B 2 186 ? -3.085  -8.684  -19.102 1.00 76.82  ? 186 LEU B CA  1 
ATOM 3140 C C   . LEU B 2 186 ? -4.434  -8.663  -18.391 1.00 77.45  ? 186 LEU B C   1 
ATOM 3141 O O   . LEU B 2 186 ? -4.844  -7.649  -17.819 1.00 79.82  ? 186 LEU B O   1 
ATOM 3142 C CB  . LEU B 2 186 ? -2.104  -9.693  -18.489 1.00 80.23  ? 186 LEU B CB  1 
ATOM 3143 C CG  . LEU B 2 186 ? -1.524  -9.455  -17.092 1.00 79.01  ? 186 LEU B CG  1 
ATOM 3144 C CD1 . LEU B 2 186 ? -2.439  -9.995  -16.031 1.00 85.34  ? 186 LEU B CD1 1 
ATOM 3145 C CD2 . LEU B 2 186 ? -0.154  -10.100 -16.967 1.00 72.33  ? 186 LEU B CD2 1 
ATOM 3146 N N   . SER B 2 187 ? -5.123  -9.801  -18.433 1.00 82.25  ? 187 SER B N   1 
ATOM 3147 C CA  . SER B 2 187 ? -6.489  -9.894  -17.939 1.00 85.69  ? 187 SER B CA  1 
ATOM 3148 C C   . SER B 2 187 ? -6.547  -9.709  -16.425 1.00 86.59  ? 187 SER B C   1 
ATOM 3149 O O   . SER B 2 187 ? -5.543  -9.818  -15.716 1.00 88.55  ? 187 SER B O   1 
ATOM 3150 C CB  . SER B 2 187 ? -7.096  -11.245 -18.313 1.00 88.97  ? 187 SER B CB  1 
ATOM 3151 O OG  . SER B 2 187 ? -6.834  -11.568 -19.667 1.00 89.76  ? 187 SER B OG  1 
ATOM 3152 N N   . LYS B 2 188 ? -7.755  -9.425  -15.931 1.00 84.75  ? 188 LYS B N   1 
ATOM 3153 C CA  . LYS B 2 188 ? -7.966  -9.367  -14.489 1.00 87.81  ? 188 LYS B CA  1 
ATOM 3154 C C   . LYS B 2 188 ? -7.736  -10.731 -13.855 1.00 92.60  ? 188 LYS B C   1 
ATOM 3155 O O   . LYS B 2 188 ? -7.055  -10.848 -12.830 1.00 90.70  ? 188 LYS B O   1 
ATOM 3156 C CB  . LYS B 2 188 ? -9.377  -8.873  -14.174 1.00 87.80  ? 188 LYS B CB  1 
ATOM 3157 C CG  . LYS B 2 188 ? -9.695  -8.885  -12.683 1.00 89.21  ? 188 LYS B CG  1 
ATOM 3158 C CD  . LYS B 2 188 ? -11.100 -8.389  -12.393 1.00 86.12  ? 188 LYS B CD  1 
ATOM 3159 C CE  . LYS B 2 188 ? -11.465 -8.586  -10.930 1.00 84.98  ? 188 LYS B CE  1 
ATOM 3160 N NZ  . LYS B 2 188 ? -10.508 -7.880  -10.030 1.00 85.93  ? 188 LYS B NZ  1 
ATOM 3161 N N   . ALA B 2 189 ? -8.308  -11.778 -14.455 1.00 89.55  ? 189 ALA B N   1 
ATOM 3162 C CA  . ALA B 2 189 ? -8.112  -13.127 -13.939 1.00 88.60  ? 189 ALA B CA  1 
ATOM 3163 C C   . ALA B 2 189 ? -6.648  -13.536 -14.017 1.00 91.77  ? 189 ALA B C   1 
ATOM 3164 O O   . ALA B 2 189 ? -6.105  -14.108 -13.065 1.00 95.93  ? 189 ALA B O   1 
ATOM 3165 C CB  . ALA B 2 189 ? -8.989  -14.116 -14.707 1.00 90.07  ? 189 ALA B CB  1 
ATOM 3166 N N   . ASP B 2 190 ? -5.990  -13.243 -15.143 1.00 88.92  ? 190 ASP B N   1 
ATOM 3167 C CA  . ASP B 2 190 ? -4.574  -13.566 -15.278 1.00 93.39  ? 190 ASP B CA  1 
ATOM 3168 C C   . ASP B 2 190 ? -3.727  -12.814 -14.259 1.00 98.16  ? 190 ASP B C   1 
ATOM 3169 O O   . ASP B 2 190 ? -2.643  -13.279 -13.889 1.00 95.52  ? 190 ASP B O   1 
ATOM 3170 C CB  . ASP B 2 190 ? -4.095  -13.255 -16.697 1.00 93.24  ? 190 ASP B CB  1 
ATOM 3171 C CG  . ASP B 2 190 ? -4.575  -14.274 -17.713 1.00 102.16 ? 190 ASP B CG  1 
ATOM 3172 O OD1 . ASP B 2 190 ? -5.391  -15.145 -17.344 1.00 102.67 ? 190 ASP B OD1 1 
ATOM 3173 O OD2 . ASP B 2 190 ? -4.132  -14.207 -18.879 1.00 101.93 ? 190 ASP B OD2 1 
ATOM 3174 N N   . TYR B 2 191 ? -4.200  -11.654 -13.797 1.00 94.70  ? 191 TYR B N   1 
ATOM 3175 C CA  . TYR B 2 191 ? -3.483  -10.916 -12.765 1.00 91.56  ? 191 TYR B CA  1 
ATOM 3176 C C   . TYR B 2 191 ? -3.700  -11.522 -11.386 1.00 93.03  ? 191 TYR B C   1 
ATOM 3177 O O   . TYR B 2 191 ? -2.813  -11.439 -10.529 1.00 93.51  ? 191 TYR B O   1 
ATOM 3178 C CB  . TYR B 2 191 ? -3.913  -9.448  -12.777 1.00 87.05  ? 191 TYR B CB  1 
ATOM 3179 C CG  . TYR B 2 191 ? -3.307  -8.611  -11.675 1.00 85.31  ? 191 TYR B CG  1 
ATOM 3180 C CD1 . TYR B 2 191 ? -1.999  -8.152  -11.764 1.00 81.71  ? 191 TYR B CD1 1 
ATOM 3181 C CD2 . TYR B 2 191 ? -4.045  -8.270  -10.550 1.00 88.55  ? 191 TYR B CD2 1 
ATOM 3182 C CE1 . TYR B 2 191 ? -1.442  -7.382  -10.760 1.00 85.30  ? 191 TYR B CE1 1 
ATOM 3183 C CE2 . TYR B 2 191 ? -3.497  -7.501  -9.541  1.00 92.95  ? 191 TYR B CE2 1 
ATOM 3184 C CZ  . TYR B 2 191 ? -2.196  -7.061  -9.651  1.00 90.21  ? 191 TYR B CZ  1 
ATOM 3185 O OH  . TYR B 2 191 ? -1.652  -6.295  -8.647  1.00 82.10  ? 191 TYR B OH  1 
ATOM 3186 N N   . GLU B 2 192 ? -4.866  -12.129 -11.155 1.00 95.25  ? 192 GLU B N   1 
ATOM 3187 C CA  . GLU B 2 192 ? -5.095  -12.860 -9.916  1.00 92.61  ? 192 GLU B CA  1 
ATOM 3188 C C   . GLU B 2 192 ? -4.299  -14.157 -9.864  1.00 92.30  ? 192 GLU B C   1 
ATOM 3189 O O   . GLU B 2 192 ? -4.026  -14.659 -8.769  1.00 94.21  ? 192 GLU B O   1 
ATOM 3190 C CB  . GLU B 2 192 ? -6.586  -13.175 -9.750  1.00 91.30  ? 192 GLU B CB  1 
ATOM 3191 C CG  . GLU B 2 192 ? -7.523  -11.979 -9.870  1.00 94.26  ? 192 GLU B CG  1 
ATOM 3192 C CD  . GLU B 2 192 ? -7.275  -10.911 -8.822  1.00 98.18  ? 192 GLU B CD  1 
ATOM 3193 O OE1 . GLU B 2 192 ? -6.798  -11.250 -7.719  1.00 101.98 ? 192 GLU B OE1 1 
ATOM 3194 O OE2 . GLU B 2 192 ? -7.561  -9.729  -9.104  1.00 93.08  ? 192 GLU B OE2 1 
ATOM 3195 N N   . LYS B 2 193 ? -3.915  -14.702 -11.022 1.00 92.04  ? 193 LYS B N   1 
ATOM 3196 C CA  . LYS B 2 193 ? -3.302  -16.026 -11.058 1.00 90.92  ? 193 LYS B CA  1 
ATOM 3197 C C   . LYS B 2 193 ? -1.871  -16.005 -10.533 1.00 86.48  ? 193 LYS B C   1 
ATOM 3198 O O   . LYS B 2 193 ? -1.440  -16.950 -9.864  1.00 86.62  ? 193 LYS B O   1 
ATOM 3199 C CB  . LYS B 2 193 ? -3.346  -16.584 -12.481 1.00 93.65  ? 193 LYS B CB  1 
ATOM 3200 C CG  . LYS B 2 193 ? -4.749  -16.917 -12.967 1.00 94.52  ? 193 LYS B CG  1 
ATOM 3201 C CD  . LYS B 2 193 ? -4.731  -17.785 -14.215 1.00 97.73  ? 193 LYS B CD  1 
ATOM 3202 C CE  . LYS B 2 193 ? -3.857  -17.180 -15.300 1.00 96.86  ? 193 LYS B CE  1 
ATOM 3203 N NZ  . LYS B 2 193 ? -3.893  -17.982 -16.554 1.00 98.76  ? 193 LYS B NZ  1 
ATOM 3204 N N   . HIS B 2 194 ? -1.120  -14.947 -10.824 1.00 86.90  ? 194 HIS B N   1 
ATOM 3205 C CA  . HIS B 2 194 ? 0.276   -14.851 -10.426 1.00 87.00  ? 194 HIS B CA  1 
ATOM 3206 C C   . HIS B 2 194 ? 0.443   -13.883 -9.261  1.00 87.10  ? 194 HIS B C   1 
ATOM 3207 O O   . HIS B 2 194 ? -0.443  -13.081 -8.954  1.00 88.07  ? 194 HIS B O   1 
ATOM 3208 C CB  . HIS B 2 194 ? 1.154   -14.421 -11.606 1.00 85.93  ? 194 HIS B CB  1 
ATOM 3209 C CG  . HIS B 2 194 ? 0.888   -15.192 -12.863 1.00 88.81  ? 194 HIS B CG  1 
ATOM 3210 N ND1 . HIS B 2 194 ? 1.084   -16.553 -12.954 1.00 86.07  ? 194 HIS B ND1 1 
ATOM 3211 C CD2 . HIS B 2 194 ? 0.439   -14.795 -14.076 1.00 90.49  ? 194 HIS B CD2 1 
ATOM 3212 C CE1 . HIS B 2 194 ? 0.768   -16.961 -14.170 1.00 81.78  ? 194 HIS B CE1 1 
ATOM 3213 N NE2 . HIS B 2 194 ? 0.374   -15.914 -14.871 1.00 84.71  ? 194 HIS B NE2 1 
ATOM 3214 N N   . LYS B 2 195 ? 1.606   -13.970 -8.614  1.00 84.62  ? 195 LYS B N   1 
ATOM 3215 C CA  . LYS B 2 195 ? 1.841   -13.262 -7.362  1.00 87.78  ? 195 LYS B CA  1 
ATOM 3216 C C   . LYS B 2 195 ? 2.711   -12.024 -7.545  1.00 88.49  ? 195 LYS B C   1 
ATOM 3217 O O   . LYS B 2 195 ? 2.240   -10.896 -7.363  1.00 87.37  ? 195 LYS B O   1 
ATOM 3218 C CB  . LYS B 2 195 ? 2.481   -14.206 -6.340  1.00 90.17  ? 195 LYS B CB  1 
ATOM 3219 C CG  . LYS B 2 195 ? 2.795   -13.564 -4.999  1.00 95.71  ? 195 LYS B CG  1 
ATOM 3220 C CD  . LYS B 2 195 ? 3.132   -14.615 -3.950  1.00 98.55  ? 195 LYS B CD  1 
ATOM 3221 C CE  . LYS B 2 195 ? 4.340   -15.449 -4.344  1.00 92.25  ? 195 LYS B CE  1 
ATOM 3222 N NZ  . LYS B 2 195 ? 5.609   -14.679 -4.229  1.00 87.13  ? 195 LYS B NZ  1 
ATOM 3223 N N   . VAL B 2 196 ? 3.979   -12.219 -7.896  1.00 89.83  ? 196 VAL B N   1 
ATOM 3224 C CA  . VAL B 2 196 ? 4.952   -11.135 -7.964  1.00 85.43  ? 196 VAL B CA  1 
ATOM 3225 C C   . VAL B 2 196 ? 5.149   -10.719 -9.416  1.00 81.97  ? 196 VAL B C   1 
ATOM 3226 O O   . VAL B 2 196 ? 5.240   -11.565 -10.314 1.00 82.33  ? 196 VAL B O   1 
ATOM 3227 C CB  . VAL B 2 196 ? 6.284   -11.553 -7.306  1.00 82.01  ? 196 VAL B CB  1 
ATOM 3228 C CG1 . VAL B 2 196 ? 6.785   -12.869 -7.883  1.00 85.21  ? 196 VAL B CG1 1 
ATOM 3229 C CG2 . VAL B 2 196 ? 7.330   -10.460 -7.454  1.00 81.60  ? 196 VAL B CG2 1 
ATOM 3230 N N   . TYR B 2 197 ? 5.195   -9.407  -9.647  1.00 81.45  ? 197 TYR B N   1 
ATOM 3231 C CA  . TYR B 2 197 ? 5.421   -8.832  -10.969 1.00 78.77  ? 197 TYR B CA  1 
ATOM 3232 C C   . TYR B 2 197 ? 6.610   -7.889  -10.882 1.00 74.64  ? 197 TYR B C   1 
ATOM 3233 O O   . TYR B 2 197 ? 6.559   -6.892  -10.154 1.00 78.58  ? 197 TYR B O   1 
ATOM 3234 C CB  . TYR B 2 197 ? 4.174   -8.094  -11.466 1.00 77.17  ? 197 TYR B CB  1 
ATOM 3235 C CG  . TYR B 2 197 ? 2.940   -8.965  -11.524 1.00 79.19  ? 197 TYR B CG  1 
ATOM 3236 C CD1 . TYR B 2 197 ? 2.685   -9.768  -12.626 1.00 77.47  ? 197 TYR B CD1 1 
ATOM 3237 C CD2 . TYR B 2 197 ? 2.042   -9.003  -10.466 1.00 81.15  ? 197 TYR B CD2 1 
ATOM 3238 C CE1 . TYR B 2 197 ? 1.564   -10.572 -12.683 1.00 81.37  ? 197 TYR B CE1 1 
ATOM 3239 C CE2 . TYR B 2 197 ? 0.919   -9.806  -10.512 1.00 84.44  ? 197 TYR B CE2 1 
ATOM 3240 C CZ  . TYR B 2 197 ? 0.684   -10.588 -11.623 1.00 88.07  ? 197 TYR B CZ  1 
ATOM 3241 O OH  . TYR B 2 197 ? -0.434  -11.387 -11.670 1.00 93.09  ? 197 TYR B OH  1 
ATOM 3242 N N   . ALA B 2 198 ? 7.675   -8.200  -11.619 1.00 72.70  ? 198 ALA B N   1 
ATOM 3243 C CA  . ALA B 2 198 ? 8.930   -7.470  -11.525 1.00 74.74  ? 198 ALA B CA  1 
ATOM 3244 C C   . ALA B 2 198 ? 9.329   -6.900  -12.880 1.00 83.71  ? 198 ALA B C   1 
ATOM 3245 O O   . ALA B 2 198 ? 9.024   -7.474  -13.929 1.00 86.75  ? 198 ALA B O   1 
ATOM 3246 C CB  . ALA B 2 198 ? 10.054  -8.368  -10.992 1.00 76.60  ? 198 ALA B CB  1 
ATOM 3247 N N   . CYS B 2 199 ? 10.023  -5.761  -12.841 1.00 89.13  ? 199 CYS B N   1 
ATOM 3248 C CA  . CYS B 2 199 ? 10.540  -5.087  -14.029 1.00 88.31  ? 199 CYS B CA  1 
ATOM 3249 C C   . CYS B 2 199 ? 12.060  -5.044  -13.931 1.00 88.03  ? 199 CYS B C   1 
ATOM 3250 O O   . CYS B 2 199 ? 12.613  -4.312  -13.103 1.00 87.87  ? 199 CYS B O   1 
ATOM 3251 C CB  . CYS B 2 199 ? 9.958   -3.679  -14.161 1.00 87.70  ? 199 CYS B CB  1 
ATOM 3252 S SG  . CYS B 2 199 ? 10.936  -2.538  -15.171 1.00 106.94 ? 199 CYS B SG  1 
ATOM 3253 N N   . GLU B 2 200 ? 12.730  -5.824  -14.774 1.00 75.52  ? 200 GLU B N   1 
ATOM 3254 C CA  . GLU B 2 200 ? 14.182  -5.940  -14.758 1.00 75.21  ? 200 GLU B CA  1 
ATOM 3255 C C   . GLU B 2 200 ? 14.768  -4.983  -15.790 1.00 72.77  ? 200 GLU B C   1 
ATOM 3256 O O   . GLU B 2 200 ? 14.465  -5.088  -16.984 1.00 73.61  ? 200 GLU B O   1 
ATOM 3257 C CB  . GLU B 2 200 ? 14.608  -7.381  -15.038 1.00 73.46  ? 200 GLU B CB  1 
ATOM 3258 C CG  . GLU B 2 200 ? 16.050  -7.683  -14.679 1.00 71.91  ? 200 GLU B CG  1 
ATOM 3259 C CD  . GLU B 2 200 ? 16.362  -9.166  -14.716 1.00 80.26  ? 200 GLU B CD  1 
ATOM 3260 O OE1 . GLU B 2 200 ? 15.976  -9.835  -15.697 1.00 82.36  ? 200 GLU B OE1 1 
ATOM 3261 O OE2 . GLU B 2 200 ? 16.989  -9.663  -13.758 1.00 82.75  ? 200 GLU B OE2 1 
ATOM 3262 N N   . VAL B 2 201 ? 15.609  -4.060  -15.330 1.00 72.36  ? 201 VAL B N   1 
ATOM 3263 C CA  . VAL B 2 201 ? 16.140  -2.976  -16.149 1.00 66.54  ? 201 VAL B CA  1 
ATOM 3264 C C   . VAL B 2 201 ? 17.628  -3.206  -16.375 1.00 64.31  ? 201 VAL B C   1 
ATOM 3265 O O   . VAL B 2 201 ? 18.376  -3.462  -15.424 1.00 69.54  ? 201 VAL B O   1 
ATOM 3266 C CB  . VAL B 2 201 ? 15.885  -1.610  -15.487 1.00 66.12  ? 201 VAL B CB  1 
ATOM 3267 C CG1 . VAL B 2 201 ? 16.566  -0.504  -16.267 1.00 67.13  ? 201 VAL B CG1 1 
ATOM 3268 C CG2 . VAL B 2 201 ? 14.391  -1.349  -15.396 1.00 66.93  ? 201 VAL B CG2 1 
ATOM 3269 N N   . THR B 2 202 ? 18.055  -3.115  -17.633 1.00 62.54  ? 202 THR B N   1 
ATOM 3270 C CA  . THR B 2 202 ? 19.456  -3.239  -18.012 1.00 60.76  ? 202 THR B CA  1 
ATOM 3271 C C   . THR B 2 202 ? 19.900  -1.952  -18.692 1.00 61.67  ? 202 THR B C   1 
ATOM 3272 O O   . THR B 2 202 ? 19.245  -1.484  -19.628 1.00 63.65  ? 202 THR B O   1 
ATOM 3273 C CB  . THR B 2 202 ? 19.675  -4.437  -18.943 1.00 57.72  ? 202 THR B CB  1 
ATOM 3274 O OG1 . THR B 2 202 ? 19.152  -5.623  -18.329 1.00 63.42  ? 202 THR B OG1 1 
ATOM 3275 C CG2 . THR B 2 202 ? 21.160  -4.632  -19.232 1.00 58.70  ? 202 THR B CG2 1 
ATOM 3276 N N   . HIS B 2 203 ? 21.006  -1.382  -18.218 1.00 61.95  ? 203 HIS B N   1 
ATOM 3277 C CA  . HIS B 2 203 ? 21.523  -0.139  -18.770 1.00 59.21  ? 203 HIS B CA  1 
ATOM 3278 C C   . HIS B 2 203 ? 23.038  -0.118  -18.622 1.00 58.05  ? 203 HIS B C   1 
ATOM 3279 O O   . HIS B 2 203 ? 23.608  -0.809  -17.773 1.00 62.82  ? 203 HIS B O   1 
ATOM 3280 C CB  . HIS B 2 203 ? 20.895  1.084   -18.088 1.00 58.38  ? 203 HIS B CB  1 
ATOM 3281 C CG  . HIS B 2 203 ? 21.200  2.381   -18.771 1.00 57.04  ? 203 HIS B CG  1 
ATOM 3282 N ND1 . HIS B 2 203 ? 20.953  2.595   -20.110 1.00 57.60  ? 203 HIS B ND1 1 
ATOM 3283 C CD2 . HIS B 2 203 ? 21.742  3.529   -18.300 1.00 54.00  ? 203 HIS B CD2 1 
ATOM 3284 C CE1 . HIS B 2 203 ? 21.325  3.820   -20.433 1.00 54.54  ? 203 HIS B CE1 1 
ATOM 3285 N NE2 . HIS B 2 203 ? 21.806  4.409   -19.353 1.00 54.12  ? 203 HIS B NE2 1 
ATOM 3286 N N   . GLN B 2 204 ? 23.686  0.688   -19.471 1.00 58.03  ? 204 GLN B N   1 
ATOM 3287 C CA  . GLN B 2 204 ? 25.141  0.805   -19.426 1.00 57.97  ? 204 GLN B CA  1 
ATOM 3288 C C   . GLN B 2 204 ? 25.611  1.400   -18.105 1.00 62.75  ? 204 GLN B C   1 
ATOM 3289 O O   . GLN B 2 204 ? 26.570  0.907   -17.497 1.00 66.78  ? 204 GLN B O   1 
ATOM 3290 C CB  . GLN B 2 204 ? 25.640  1.659   -20.592 1.00 57.09  ? 204 GLN B CB  1 
ATOM 3291 C CG  . GLN B 2 204 ? 24.911  1.451   -21.907 1.00 56.50  ? 204 GLN B CG  1 
ATOM 3292 C CD  . GLN B 2 204 ? 25.618  2.135   -23.064 1.00 52.43  ? 204 GLN B CD  1 
ATOM 3293 O OE1 . GLN B 2 204 ? 26.682  2.730   -22.890 1.00 52.27  ? 204 GLN B OE1 1 
ATOM 3294 N NE2 . GLN B 2 204 ? 25.029  2.052   -24.251 1.00 53.31  ? 204 GLN B NE2 1 
ATOM 3295 N N   . GLY B 2 205 ? 24.957  2.471   -17.653 1.00 63.34  ? 205 GLY B N   1 
ATOM 3296 C CA  . GLY B 2 205 ? 25.363  3.133   -16.423 1.00 62.24  ? 205 GLY B CA  1 
ATOM 3297 C C   . GLY B 2 205 ? 25.233  2.276   -15.181 1.00 58.12  ? 205 GLY B C   1 
ATOM 3298 O O   . GLY B 2 205 ? 25.897  2.555   -14.177 1.00 55.87  ? 205 GLY B O   1 
ATOM 3299 N N   . LEU B 2 206 ? 24.395  1.245   -15.223 1.00 61.89  ? 206 LEU B N   1 
ATOM 3300 C CA  . LEU B 2 206 ? 24.246  0.350   -14.086 1.00 62.55  ? 206 LEU B CA  1 
ATOM 3301 C C   . LEU B 2 206 ? 25.356  -0.694  -14.068 1.00 65.78  ? 206 LEU B C   1 
ATOM 3302 O O   . LEU B 2 206 ? 25.853  -1.124  -15.113 1.00 61.85  ? 206 LEU B O   1 
ATOM 3303 C CB  . LEU B 2 206 ? 22.884  -0.345  -14.116 1.00 58.93  ? 206 LEU B CB  1 
ATOM 3304 C CG  . LEU B 2 206 ? 21.653  0.544   -13.941 1.00 58.95  ? 206 LEU B CG  1 
ATOM 3305 C CD1 . LEU B 2 206 ? 20.391  -0.251  -14.224 1.00 64.94  ? 206 LEU B CD1 1 
ATOM 3306 C CD2 . LEU B 2 206 ? 21.618  1.132   -12.541 1.00 56.97  ? 206 LEU B CD2 1 
ATOM 3307 N N   . SER B 2 207 ? 25.750  -1.095  -12.857 1.00 68.08  ? 207 SER B N   1 
ATOM 3308 C CA  . SER B 2 207 ? 26.722  -2.173  -12.716 1.00 73.91  ? 207 SER B CA  1 
ATOM 3309 C C   . SER B 2 207 ? 26.105  -3.509  -13.107 1.00 71.19  ? 207 SER B C   1 
ATOM 3310 O O   . SER B 2 207 ? 26.684  -4.270  -13.890 1.00 72.26  ? 207 SER B O   1 
ATOM 3311 C CB  . SER B 2 207 ? 27.253  -2.225  -11.282 1.00 91.97  ? 207 SER B CB  1 
ATOM 3312 O OG  . SER B 2 207 ? 26.205  -2.404  -10.344 1.00 83.96  ? 207 SER B OG  1 
ATOM 3313 N N   . SER B 2 208 ? 24.926  -3.803  -12.577 1.00 68.54  ? 208 SER B N   1 
ATOM 3314 C CA  . SER B 2 208 ? 24.170  -5.010  -12.860 1.00 66.94  ? 208 SER B CA  1 
ATOM 3315 C C   . SER B 2 208 ? 22.710  -4.643  -13.093 1.00 64.43  ? 208 SER B C   1 
ATOM 3316 O O   . SER B 2 208 ? 22.267  -3.559  -12.704 1.00 69.91  ? 208 SER B O   1 
ATOM 3317 C CB  . SER B 2 208 ? 24.272  -6.019  -11.706 1.00 68.34  ? 208 SER B CB  1 
ATOM 3318 O OG  . SER B 2 208 ? 23.851  -5.439  -10.484 1.00 68.73  ? 208 SER B OG  1 
ATOM 3319 N N   . PRO B 2 209 ? 21.958  -5.514  -13.764 1.00 63.96  ? 209 PRO B N   1 
ATOM 3320 C CA  . PRO B 2 209 ? 20.515  -5.299  -13.900 1.00 66.15  ? 209 PRO B CA  1 
ATOM 3321 C C   . PRO B 2 209 ? 19.861  -4.948  -12.570 1.00 65.19  ? 209 PRO B C   1 
ATOM 3322 O O   . PRO B 2 209 ? 20.157  -5.544  -11.532 1.00 67.47  ? 209 PRO B O   1 
ATOM 3323 C CB  . PRO B 2 209 ? 20.021  -6.653  -14.420 1.00 67.61  ? 209 PRO B CB  1 
ATOM 3324 C CG  . PRO B 2 209 ? 21.264  -7.308  -15.065 1.00 68.42  ? 209 PRO B CG  1 
ATOM 3325 C CD  . PRO B 2 209 ? 22.437  -6.383  -14.845 1.00 66.49  ? 209 PRO B CD  1 
ATOM 3326 N N   . VAL B 2 210 ? 18.967  -3.962  -12.607 1.00 66.98  ? 210 VAL B N   1 
ATOM 3327 C CA  . VAL B 2 210 ? 18.214  -3.524  -11.438 1.00 75.01  ? 210 VAL B CA  1 
ATOM 3328 C C   . VAL B 2 210 ? 16.777  -3.996  -11.599 1.00 77.51  ? 210 VAL B C   1 
ATOM 3329 O O   . VAL B 2 210 ? 16.159  -3.774  -12.648 1.00 82.53  ? 210 VAL B O   1 
ATOM 3330 C CB  . VAL B 2 210 ? 18.281  -1.996  -11.265 1.00 75.54  ? 210 VAL B CB  1 
ATOM 3331 C CG1 . VAL B 2 210 ? 17.167  -1.508  -10.346 1.00 71.86  ? 210 VAL B CG1 1 
ATOM 3332 C CG2 . VAL B 2 210 ? 19.643  -1.583  -10.728 1.00 82.12  ? 210 VAL B CG2 1 
ATOM 3333 N N   . THR B 2 211 ? 16.248  -4.651  -10.570 1.00 76.45  ? 211 THR B N   1 
ATOM 3334 C CA  . THR B 2 211 ? 14.893  -5.181  -10.599 1.00 78.76  ? 211 THR B CA  1 
ATOM 3335 C C   . THR B 2 211 ? 14.056  -4.542  -9.500  1.00 80.89  ? 211 THR B C   1 
ATOM 3336 O O   . THR B 2 211 ? 14.520  -4.372  -8.368  1.00 84.66  ? 211 THR B O   1 
ATOM 3337 C CB  . THR B 2 211 ? 14.882  -6.704  -10.432 1.00 80.90  ? 211 THR B CB  1 
ATOM 3338 O OG1 . THR B 2 211 ? 15.996  -7.271  -11.132 1.00 79.97  ? 211 THR B OG1 1 
ATOM 3339 C CG2 . THR B 2 211 ? 13.591  -7.287  -10.992 1.00 78.88  ? 211 THR B CG2 1 
ATOM 3340 N N   . LYS B 2 212 ? 12.819  -4.192  -9.847  1.00 82.06  ? 212 LYS B N   1 
ATOM 3341 C CA  . LYS B 2 212 ? 11.843  -3.651  -8.913  1.00 86.24  ? 212 LYS B CA  1 
ATOM 3342 C C   . LYS B 2 212 ? 10.596  -4.517  -8.990  1.00 83.52  ? 212 LYS B C   1 
ATOM 3343 O O   . LYS B 2 212 ? 10.224  -4.972  -10.075 1.00 88.53  ? 212 LYS B O   1 
ATOM 3344 C CB  . LYS B 2 212 ? 11.497  -2.197  -9.251  1.00 83.92  ? 212 LYS B CB  1 
ATOM 3345 C CG  . LYS B 2 212 ? 12.617  -1.202  -8.988  1.00 80.70  ? 212 LYS B CG  1 
ATOM 3346 C CD  . LYS B 2 212 ? 12.680  -0.761  -7.538  1.00 83.00  ? 212 LYS B CD  1 
ATOM 3347 C CE  . LYS B 2 212 ? 13.823  0.221   -7.332  1.00 77.52  ? 212 LYS B CE  1 
ATOM 3348 N NZ  . LYS B 2 212 ? 13.847  0.784   -5.957  1.00 77.02  ? 212 LYS B NZ  1 
ATOM 3349 N N   . SER B 2 213 ? 9.945   -4.748  -7.850  1.00 80.00  ? 213 SER B N   1 
ATOM 3350 C CA  . SER B 2 213 ? 8.833   -5.690  -7.822  1.00 78.68  ? 213 SER B CA  1 
ATOM 3351 C C   . SER B 2 213 ? 7.782   -5.276  -6.801  1.00 81.73  ? 213 SER B C   1 
ATOM 3352 O O   . SER B 2 213 ? 8.109   -4.728  -5.745  1.00 91.46  ? 213 SER B O   1 
ATOM 3353 C CB  . SER B 2 213 ? 9.327   -7.104  -7.499  1.00 81.15  ? 213 SER B CB  1 
ATOM 3354 O OG  . SER B 2 213 ? 9.912   -7.152  -6.208  1.00 85.70  ? 213 SER B OG  1 
ATOM 3355 N N   . PHE B 2 214 ? 6.520   -5.548  -7.131  1.00 78.37  ? 214 PHE B N   1 
ATOM 3356 C CA  . PHE B 2 214 ? 5.424   -5.556  -6.174  1.00 80.67  ? 214 PHE B CA  1 
ATOM 3357 C C   . PHE B 2 214 ? 4.839   -6.962  -6.147  1.00 85.95  ? 214 PHE B C   1 
ATOM 3358 O O   . PHE B 2 214 ? 4.870   -7.677  -7.152  1.00 87.66  ? 214 PHE B O   1 
ATOM 3359 C CB  . PHE B 2 214 ? 4.337   -4.523  -6.529  1.00 78.14  ? 214 PHE B CB  1 
ATOM 3360 C CG  . PHE B 2 214 ? 3.466   -4.920  -7.686  1.00 84.02  ? 214 PHE B CG  1 
ATOM 3361 C CD1 . PHE B 2 214 ? 3.881   -4.718  -8.988  1.00 80.85  ? 214 PHE B CD1 1 
ATOM 3362 C CD2 . PHE B 2 214 ? 2.210   -5.468  -7.465  1.00 87.72  ? 214 PHE B CD2 1 
ATOM 3363 C CE1 . PHE B 2 214 ? 3.075   -5.079  -10.047 1.00 79.01  ? 214 PHE B CE1 1 
ATOM 3364 C CE2 . PHE B 2 214 ? 1.400   -5.827  -8.525  1.00 83.58  ? 214 PHE B CE2 1 
ATOM 3365 C CZ  . PHE B 2 214 ? 1.833   -5.630  -9.817  1.00 81.28  ? 214 PHE B CZ  1 
ATOM 3366 N N   . ASN B 2 215 ? 4.312   -7.367  -4.991  1.00 91.38  ? 215 ASN B N   1 
ATOM 3367 C CA  . ASN B 2 215 ? 4.011   -8.772  -4.748  1.00 92.15  ? 215 ASN B CA  1 
ATOM 3368 C C   . ASN B 2 215 ? 2.531   -9.095  -4.591  1.00 94.02  ? 215 ASN B C   1 
ATOM 3369 O O   . ASN B 2 215 ? 2.189   -10.276 -4.457  1.00 103.45 ? 215 ASN B O   1 
ATOM 3370 C CB  . ASN B 2 215 ? 4.767   -9.260  -3.505  1.00 91.43  ? 215 ASN B CB  1 
ATOM 3371 C CG  . ASN B 2 215 ? 6.246   -9.457  -3.770  1.00 95.76  ? 215 ASN B CG  1 
ATOM 3372 O OD1 . ASN B 2 215 ? 6.911   -8.578  -4.319  1.00 92.74  ? 215 ASN B OD1 1 
ATOM 3373 N ND2 . ASN B 2 215 ? 6.768   -10.614 -3.382  1.00 95.96  ? 215 ASN B ND2 1 
ATOM 3374 N N   . ARG B 2 216 ? 1.645   -8.104  -4.596  1.00 81.77  ? 216 ARG B N   1 
ATOM 3375 C CA  . ARG B 2 216 ? 0.222   -8.409  -4.574  1.00 84.11  ? 216 ARG B CA  1 
ATOM 3376 C C   . ARG B 2 216 ? -0.241  -8.891  -5.945  1.00 90.65  ? 216 ARG B C   1 
ATOM 3377 O O   . ARG B 2 216 ? 0.246   -8.441  -6.986  1.00 96.29  ? 216 ARG B O   1 
ATOM 3378 C CB  . ARG B 2 216 ? -0.594  -7.190  -4.142  1.00 82.74  ? 216 ARG B CB  1 
ATOM 3379 C CG  . ARG B 2 216 ? -0.407  -6.802  -2.682  1.00 82.67  ? 216 ARG B CG  1 
ATOM 3380 C CD  . ARG B 2 216 ? -0.878  -5.382  -2.412  1.00 88.50  ? 216 ARG B CD  1 
ATOM 3381 N NE  . ARG B 2 216 ? -0.492  -4.932  -1.081  1.00 82.33  ? 216 ARG B NE  1 
ATOM 3382 C CZ  . ARG B 2 216 ? 0.663   -4.343  -0.801  1.00 80.83  ? 216 ARG B CZ  1 
ATOM 3383 N NH1 . ARG B 2 216 ? 1.566   -4.115  -1.739  1.00 75.66  ? 216 ARG B NH1 1 
ATOM 3384 N NH2 . ARG B 2 216 ? 0.917   -3.977  0.452   1.00 87.51  ? 216 ARG B NH2 1 
ATOM 3385 N N   . GLY B 2 217 ? -1.188  -9.823  -5.936  1.00 93.59  ? 217 GLY B N   1 
ATOM 3386 C CA  . GLY B 2 217 ? -1.704  -10.396 -7.165  1.00 91.29  ? 217 GLY B CA  1 
ATOM 3387 C C   . GLY B 2 217 ? -2.780  -11.437 -6.932  1.00 90.69  ? 217 GLY B C   1 
ATOM 3388 O O   . GLY B 2 217 ? -3.940  -11.100 -6.705  1.00 91.75  ? 217 GLY B O   1 
ATOM 3389 N N   . GLN C 1 1   ? -40.116 -0.450  -16.525 1.00 84.28  ? 1   GLN C N   1 
ATOM 3390 C CA  . GLN C 1 1   ? -40.728 -0.372  -17.845 1.00 81.68  ? 1   GLN C CA  1 
ATOM 3391 C C   . GLN C 1 1   ? -42.176 0.095   -17.760 1.00 84.30  ? 1   GLN C C   1 
ATOM 3392 O O   . GLN C 1 1   ? -42.794 0.405   -18.777 1.00 92.48  ? 1   GLN C O   1 
ATOM 3393 C CB  . GLN C 1 1   ? -40.645 -1.725  -18.551 1.00 88.28  ? 1   GLN C CB  1 
ATOM 3394 C CG  . GLN C 1 1   ? -39.232 -2.131  -18.941 1.00 95.10  ? 1   GLN C CG  1 
ATOM 3395 C CD  . GLN C 1 1   ? -39.207 -3.385  -19.787 1.00 103.65 ? 1   GLN C CD  1 
ATOM 3396 O OE1 . GLN C 1 1   ? -40.230 -4.045  -19.964 1.00 103.32 ? 1   GLN C OE1 1 
ATOM 3397 N NE2 . GLN C 1 1   ? -38.039 -3.716  -20.327 1.00 107.16 ? 1   GLN C NE2 1 
ATOM 3398 N N   . VAL C 1 2   ? -42.717 0.138   -16.540 1.00 77.60  ? 2   VAL C N   1 
ATOM 3399 C CA  . VAL C 1 2   ? -44.043 0.710   -16.343 1.00 76.78  ? 2   VAL C CA  1 
ATOM 3400 C C   . VAL C 1 2   ? -43.993 2.193   -16.674 1.00 82.26  ? 2   VAL C C   1 
ATOM 3401 O O   . VAL C 1 2   ? -43.165 2.939   -16.136 1.00 84.97  ? 2   VAL C O   1 
ATOM 3402 C CB  . VAL C 1 2   ? -44.524 0.468   -14.905 1.00 70.52  ? 2   VAL C CB  1 
ATOM 3403 C CG1 . VAL C 1 2   ? -45.904 1.068   -14.701 1.00 69.29  ? 2   VAL C CG1 1 
ATOM 3404 C CG2 . VAL C 1 2   ? -44.536 -1.020  -14.596 1.00 76.82  ? 2   VAL C CG2 1 
ATOM 3405 N N   . GLN C 1 3   ? -44.872 2.628   -17.574 1.00 77.77  ? 3   GLN C N   1 
ATOM 3406 C CA  . GLN C 1 3   ? -44.860 3.999   -18.062 1.00 78.45  ? 3   GLN C CA  1 
ATOM 3407 C C   . GLN C 1 3   ? -46.250 4.605   -17.952 1.00 77.00  ? 3   GLN C C   1 
ATOM 3408 O O   . GLN C 1 3   ? -47.253 3.938   -18.222 1.00 74.64  ? 3   GLN C O   1 
ATOM 3409 C CB  . GLN C 1 3   ? -44.364 4.066   -19.512 1.00 77.12  ? 3   GLN C CB  1 
ATOM 3410 C CG  . GLN C 1 3   ? -42.891 3.728   -19.666 1.00 76.99  ? 3   GLN C CG  1 
ATOM 3411 C CD  . GLN C 1 3   ? -42.426 3.762   -21.107 1.00 90.07  ? 3   GLN C CD  1 
ATOM 3412 O OE1 . GLN C 1 3   ? -43.099 4.316   -21.976 1.00 100.59 ? 3   GLN C OE1 1 
ATOM 3413 N NE2 . GLN C 1 3   ? -41.263 3.176   -21.366 1.00 90.52  ? 3   GLN C NE2 1 
ATOM 3414 N N   . LEU C 1 4   ? -46.300 5.874   -17.552 1.00 79.70  ? 4   LEU C N   1 
ATOM 3415 C CA  . LEU C 1 4   ? -47.549 6.609   -17.380 1.00 75.70  ? 4   LEU C CA  1 
ATOM 3416 C C   . LEU C 1 4   ? -47.509 7.823   -18.299 1.00 74.39  ? 4   LEU C C   1 
ATOM 3417 O O   . LEU C 1 4   ? -46.710 8.742   -18.087 1.00 77.27  ? 4   LEU C O   1 
ATOM 3418 C CB  . LEU C 1 4   ? -47.747 7.022   -15.921 1.00 67.31  ? 4   LEU C CB  1 
ATOM 3419 C CG  . LEU C 1 4   ? -48.620 6.135   -15.027 1.00 70.23  ? 4   LEU C CG  1 
ATOM 3420 C CD1 . LEU C 1 4   ? -48.178 4.682   -15.084 1.00 71.73  ? 4   LEU C CD1 1 
ATOM 3421 C CD2 . LEU C 1 4   ? -48.591 6.637   -13.591 1.00 64.29  ? 4   LEU C CD2 1 
ATOM 3422 N N   . GLN C 1 5   ? -48.361 7.821   -19.321 1.00 76.53  ? 5   GLN C N   1 
ATOM 3423 C CA  . GLN C 1 5   ? -48.428 8.897   -20.298 1.00 81.57  ? 5   GLN C CA  1 
ATOM 3424 C C   . GLN C 1 5   ? -49.658 9.755   -20.039 1.00 80.11  ? 5   GLN C C   1 
ATOM 3425 O O   . GLN C 1 5   ? -50.717 9.241   -19.666 1.00 76.01  ? 5   GLN C O   1 
ATOM 3426 C CB  . GLN C 1 5   ? -48.464 8.341   -21.723 1.00 74.98  ? 5   GLN C CB  1 
ATOM 3427 C CG  . GLN C 1 5   ? -47.355 7.345   -22.019 1.00 83.15  ? 5   GLN C CG  1 
ATOM 3428 C CD  . GLN C 1 5   ? -46.459 7.800   -23.151 1.00 85.82  ? 5   GLN C CD  1 
ATOM 3429 O OE1 . GLN C 1 5   ? -46.594 8.916   -23.651 1.00 85.52  ? 5   GLN C OE1 1 
ATOM 3430 N NE2 . GLN C 1 5   ? -45.540 6.937   -23.566 1.00 81.04  ? 5   GLN C NE2 1 
ATOM 3431 N N   . GLN C 1 6   ? -49.515 11.063  -20.244 1.00 73.95  ? 6   GLN C N   1 
ATOM 3432 C CA  . GLN C 1 6   ? -50.559 12.026  -19.932 1.00 66.24  ? 6   GLN C CA  1 
ATOM 3433 C C   . GLN C 1 6   ? -50.960 12.822  -21.167 1.00 63.27  ? 6   GLN C C   1 
ATOM 3434 O O   . GLN C 1 6   ? -50.136 13.110  -22.041 1.00 62.07  ? 6   GLN C O   1 
ATOM 3435 C CB  . GLN C 1 6   ? -50.107 12.998  -18.834 1.00 64.75  ? 6   GLN C CB  1 
ATOM 3436 C CG  . GLN C 1 6   ? -51.244 13.619  -18.033 1.00 64.06  ? 6   GLN C CG  1 
ATOM 3437 C CD  . GLN C 1 6   ? -50.775 14.783  -17.179 1.00 59.63  ? 6   GLN C CD  1 
ATOM 3438 O OE1 . GLN C 1 6   ? -49.577 15.047  -17.078 1.00 58.21  ? 6   GLN C OE1 1 
ATOM 3439 N NE2 . GLN C 1 6   ? -51.719 15.504  -16.586 1.00 56.75  ? 6   GLN C NE2 1 
ATOM 3440 N N   . TRP C 1 7   ? -52.241 13.179  -21.219 1.00 58.90  ? 7   TRP C N   1 
ATOM 3441 C CA  . TRP C 1 7   ? -52.760 14.111  -22.207 1.00 57.09  ? 7   TRP C CA  1 
ATOM 3442 C C   . TRP C 1 7   ? -54.006 14.768  -21.632 1.00 55.82  ? 7   TRP C C   1 
ATOM 3443 O O   . TRP C 1 7   ? -54.593 14.285  -20.660 1.00 54.95  ? 7   TRP C O   1 
ATOM 3444 C CB  . TRP C 1 7   ? -53.071 13.424  -23.544 1.00 59.65  ? 7   TRP C CB  1 
ATOM 3445 C CG  . TRP C 1 7   ? -54.172 12.399  -23.484 1.00 60.71  ? 7   TRP C CG  1 
ATOM 3446 C CD1 . TRP C 1 7   ? -55.517 12.636  -23.503 1.00 59.62  ? 7   TRP C CD1 1 
ATOM 3447 C CD2 . TRP C 1 7   ? -54.019 10.976  -23.420 1.00 59.14  ? 7   TRP C CD2 1 
ATOM 3448 N NE1 . TRP C 1 7   ? -56.208 11.451  -23.442 1.00 54.38  ? 7   TRP C NE1 1 
ATOM 3449 C CE2 . TRP C 1 7   ? -55.312 10.417  -23.392 1.00 55.67  ? 7   TRP C CE2 1 
ATOM 3450 C CE3 . TRP C 1 7   ? -52.914 10.122  -23.378 1.00 62.13  ? 7   TRP C CE3 1 
ATOM 3451 C CZ2 . TRP C 1 7   ? -55.529 9.044   -23.325 1.00 60.16  ? 7   TRP C CZ2 1 
ATOM 3452 C CZ3 . TRP C 1 7   ? -53.132 8.760   -23.311 1.00 61.64  ? 7   TRP C CZ3 1 
ATOM 3453 C CH2 . TRP C 1 7   ? -54.429 8.234   -23.284 1.00 61.66  ? 7   TRP C CH2 1 
ATOM 3454 N N   . GLY C 1 8   ? -54.402 15.880  -22.239 1.00 55.42  ? 8   GLY C N   1 
ATOM 3455 C CA  . GLY C 1 8   ? -55.598 16.571  -21.796 1.00 54.68  ? 8   GLY C CA  1 
ATOM 3456 C C   . GLY C 1 8   ? -55.583 18.024  -22.240 1.00 52.70  ? 8   GLY C C   1 
ATOM 3457 O O   . GLY C 1 8   ? -54.892 18.391  -23.189 1.00 52.98  ? 8   GLY C O   1 
ATOM 3458 N N   . THR C 1 9   ? -56.363 18.831  -21.524 1.00 52.53  ? 9   THR C N   1 
ATOM 3459 C CA  . THR C 1 9   ? -56.528 20.233  -21.881 1.00 52.71  ? 9   THR C CA  1 
ATOM 3460 C C   . THR C 1 9   ? -55.293 21.032  -21.487 1.00 52.71  ? 9   THR C C   1 
ATOM 3461 O O   . THR C 1 9   ? -54.852 20.990  -20.335 1.00 52.44  ? 9   THR C O   1 
ATOM 3462 C CB  . THR C 1 9   ? -57.770 20.810  -21.202 1.00 52.54  ? 9   THR C CB  1 
ATOM 3463 O OG1 . THR C 1 9   ? -57.879 20.289  -19.871 1.00 52.14  ? 9   THR C OG1 1 
ATOM 3464 C CG2 . THR C 1 9   ? -59.020 20.441  -21.986 1.00 54.79  ? 9   THR C CG2 1 
ATOM 3465 N N   . GLY C 1 10  ? -54.737 21.764  -22.449 1.00 53.05  ? 10  GLY C N   1 
ATOM 3466 C CA  . GLY C 1 10  ? -53.540 22.546  -22.213 1.00 55.11  ? 10  GLY C CA  1 
ATOM 3467 C C   . GLY C 1 10  ? -53.830 24.006  -21.930 1.00 53.51  ? 10  GLY C C   1 
ATOM 3468 O O   . GLY C 1 10  ? -53.075 24.668  -21.212 1.00 53.16  ? 10  GLY C O   1 
ATOM 3469 N N   . LEU C 1 11  ? -54.923 24.519  -22.491 1.00 55.73  ? 11  LEU C N   1 
ATOM 3470 C CA  . LEU C 1 11  ? -55.344 25.898  -22.288 1.00 53.57  ? 11  LEU C CA  1 
ATOM 3471 C C   . LEU C 1 11  ? -56.833 25.902  -21.978 1.00 54.31  ? 11  LEU C C   1 
ATOM 3472 O O   . LEU C 1 11  ? -57.612 25.210  -22.643 1.00 61.00  ? 11  LEU C O   1 
ATOM 3473 C CB  . LEU C 1 11  ? -55.040 26.757  -23.525 1.00 54.31  ? 11  LEU C CB  1 
ATOM 3474 C CG  . LEU C 1 11  ? -54.924 28.288  -23.450 1.00 58.87  ? 11  LEU C CG  1 
ATOM 3475 C CD1 . LEU C 1 11  ? -54.575 28.837  -24.826 1.00 67.94  ? 11  LEU C CD1 1 
ATOM 3476 C CD2 . LEU C 1 11  ? -56.175 28.987  -22.923 1.00 60.88  ? 11  LEU C CD2 1 
ATOM 3477 N N   . LEU C 1 12  ? -57.222 26.675  -20.970 1.00 54.66  ? 12  LEU C N   1 
ATOM 3478 C CA  . LEU C 1 12  ? -58.613 26.789  -20.565 1.00 56.66  ? 12  LEU C CA  1 
ATOM 3479 C C   . LEU C 1 12  ? -58.975 28.245  -20.318 1.00 60.49  ? 12  LEU C C   1 
ATOM 3480 O O   . LEU C 1 12  ? -58.164 29.031  -19.823 1.00 60.99  ? 12  LEU C O   1 
ATOM 3481 C CB  . LEU C 1 12  ? -58.905 25.977  -19.296 1.00 56.01  ? 12  LEU C CB  1 
ATOM 3482 C CG  . LEU C 1 12  ? -58.875 24.454  -19.408 1.00 55.25  ? 12  LEU C CG  1 
ATOM 3483 C CD1 . LEU C 1 12  ? -57.482 23.910  -19.129 1.00 57.09  ? 12  LEU C CD1 1 
ATOM 3484 C CD2 . LEU C 1 12  ? -59.889 23.844  -18.458 1.00 54.23  ? 12  LEU C CD2 1 
ATOM 3485 N N   . LYS C 1 13  ? -60.199 28.590  -20.675 1.00 64.10  ? 13  LYS C N   1 
ATOM 3486 C CA  . LYS C 1 13  ? -60.750 29.861  -20.248 1.00 64.60  ? 13  LYS C CA  1 
ATOM 3487 C C   . LYS C 1 13  ? -61.308 29.715  -18.835 1.00 61.14  ? 13  LYS C C   1 
ATOM 3488 O O   . LYS C 1 13  ? -61.702 28.617  -18.432 1.00 60.74  ? 13  LYS C O   1 
ATOM 3489 C CB  . LYS C 1 13  ? -61.853 30.313  -21.200 1.00 68.45  ? 13  LYS C CB  1 
ATOM 3490 C CG  . LYS C 1 13  ? -61.452 30.324  -22.666 1.00 68.48  ? 13  LYS C CG  1 
ATOM 3491 C CD  . LYS C 1 13  ? -60.709 31.591  -23.040 1.00 72.02  ? 13  LYS C CD  1 
ATOM 3492 C CE  . LYS C 1 13  ? -60.082 31.470  -24.420 1.00 75.14  ? 13  LYS C CE  1 
ATOM 3493 N NZ  . LYS C 1 13  ? -58.925 30.528  -24.433 1.00 67.62  ? 13  LYS C NZ  1 
ATOM 3494 N N   . PRO C 1 14  ? -61.323 30.793  -18.055 1.00 57.67  ? 14  PRO C N   1 
ATOM 3495 C CA  . PRO C 1 14  ? -61.916 30.722  -16.717 1.00 55.47  ? 14  PRO C CA  1 
ATOM 3496 C C   . PRO C 1 14  ? -63.344 30.194  -16.768 1.00 59.09  ? 14  PRO C C   1 
ATOM 3497 O O   . PRO C 1 14  ? -64.104 30.499  -17.688 1.00 58.98  ? 14  PRO C O   1 
ATOM 3498 C CB  . PRO C 1 14  ? -61.863 32.174  -16.239 1.00 56.69  ? 14  PRO C CB  1 
ATOM 3499 C CG  . PRO C 1 14  ? -60.630 32.703  -16.896 1.00 60.73  ? 14  PRO C CG  1 
ATOM 3500 C CD  . PRO C 1 14  ? -60.594 32.056  -18.263 1.00 58.96  ? 14  PRO C CD  1 
ATOM 3501 N N   . SER C 1 15  ? -63.689 29.375  -15.773 1.00 65.96  ? 15  SER C N   1 
ATOM 3502 C CA  . SER C 1 15  ? -64.973 28.695  -15.615 1.00 65.41  ? 15  SER C CA  1 
ATOM 3503 C C   . SER C 1 15  ? -65.155 27.522  -16.571 1.00 65.35  ? 15  SER C C   1 
ATOM 3504 O O   . SER C 1 15  ? -66.265 26.985  -16.675 1.00 65.47  ? 15  SER C O   1 
ATOM 3505 C CB  . SER C 1 15  ? -66.162 29.654  -15.761 1.00 66.11  ? 15  SER C CB  1 
ATOM 3506 O OG  . SER C 1 15  ? -67.359 29.062  -15.290 1.00 79.53  ? 15  SER C OG  1 
ATOM 3507 N N   . GLU C 1 16  ? -64.102 27.095  -17.264 1.00 59.25  ? 16  GLU C N   1 
ATOM 3508 C CA  . GLU C 1 16  ? -64.181 25.912  -18.107 1.00 59.81  ? 16  GLU C CA  1 
ATOM 3509 C C   . GLU C 1 16  ? -63.854 24.677  -17.267 1.00 62.13  ? 16  GLU C C   1 
ATOM 3510 O O   . GLU C 1 16  ? -63.726 24.751  -16.042 1.00 60.51  ? 16  GLU C O   1 
ATOM 3511 C CB  . GLU C 1 16  ? -63.265 26.058  -19.321 1.00 59.24  ? 16  GLU C CB  1 
ATOM 3512 C CG  . GLU C 1 16  ? -63.826 26.979  -20.398 1.00 59.24  ? 16  GLU C CG  1 
ATOM 3513 C CD  . GLU C 1 16  ? -62.978 27.012  -21.655 1.00 63.82  ? 16  GLU C CD  1 
ATOM 3514 O OE1 . GLU C 1 16  ? -61.819 26.553  -21.607 1.00 64.08  ? 16  GLU C OE1 1 
ATOM 3515 O OE2 . GLU C 1 16  ? -63.471 27.506  -22.692 1.00 65.14  ? 16  GLU C OE2 1 
ATOM 3516 N N   . THR C 1 17  ? -63.711 23.524  -17.917 1.00 61.01  ? 17  THR C N   1 
ATOM 3517 C CA  . THR C 1 17  ? -63.563 22.251  -17.224 1.00 60.26  ? 17  THR C CA  1 
ATOM 3518 C C   . THR C 1 17  ? -62.250 21.587  -17.616 1.00 59.10  ? 17  THR C C   1 
ATOM 3519 O O   . THR C 1 17  ? -61.987 21.376  -18.805 1.00 59.52  ? 17  THR C O   1 
ATOM 3520 C CB  . THR C 1 17  ? -64.733 21.318  -17.537 1.00 59.31  ? 17  THR C CB  1 
ATOM 3521 O OG1 . THR C 1 17  ? -65.965 21.973  -17.211 1.00 64.82  ? 17  THR C OG1 1 
ATOM 3522 C CG2 . THR C 1 17  ? -64.621 20.039  -16.721 1.00 54.66  ? 17  THR C CG2 1 
ATOM 3523 N N   . LEU C 1 18  ? -61.438 21.255  -16.613 1.00 58.12  ? 18  LEU C N   1 
ATOM 3524 C CA  . LEU C 1 18  ? -60.153 20.600  -16.829 1.00 56.33  ? 18  LEU C CA  1 
ATOM 3525 C C   . LEU C 1 18  ? -60.353 19.103  -17.025 1.00 58.10  ? 18  LEU C C   1 
ATOM 3526 O O   . LEU C 1 18  ? -60.914 18.431  -16.157 1.00 56.15  ? 18  LEU C O   1 
ATOM 3527 C CB  . LEU C 1 18  ? -59.224 20.858  -15.645 1.00 52.50  ? 18  LEU C CB  1 
ATOM 3528 C CG  . LEU C 1 18  ? -57.852 20.185  -15.687 1.00 51.57  ? 18  LEU C CG  1 
ATOM 3529 C CD1 . LEU C 1 18  ? -56.924 20.946  -16.601 1.00 52.39  ? 18  LEU C CD1 1 
ATOM 3530 C CD2 . LEU C 1 18  ? -57.259 20.083  -14.289 1.00 51.67  ? 18  LEU C CD2 1 
ATOM 3531 N N   . SER C 1 19  ? -59.883 18.579  -18.153 1.00 59.29  ? 19  SER C N   1 
ATOM 3532 C CA  . SER C 1 19  ? -59.920 17.147  -18.426 1.00 55.77  ? 19  SER C CA  1 
ATOM 3533 C C   . SER C 1 19  ? -58.504 16.666  -18.707 1.00 54.84  ? 19  SER C C   1 
ATOM 3534 O O   . SER C 1 19  ? -57.868 17.122  -19.663 1.00 52.26  ? 19  SER C O   1 
ATOM 3535 C CB  . SER C 1 19  ? -60.845 16.832  -19.604 1.00 57.57  ? 19  SER C CB  1 
ATOM 3536 O OG  . SER C 1 19  ? -62.188 17.156  -19.290 1.00 56.26  ? 19  SER C OG  1 
ATOM 3537 N N   . LEU C 1 20  ? -58.011 15.755  -17.872 1.00 60.25  ? 20  LEU C N   1 
ATOM 3538 C CA  . LEU C 1 20  ? -56.705 15.140  -18.058 1.00 59.38  ? 20  LEU C CA  1 
ATOM 3539 C C   . LEU C 1 20  ? -56.852 13.631  -17.947 1.00 57.59  ? 20  LEU C C   1 
ATOM 3540 O O   . LEU C 1 20  ? -57.587 13.138  -17.090 1.00 57.28  ? 20  LEU C O   1 
ATOM 3541 C CB  . LEU C 1 20  ? -55.695 15.644  -17.023 1.00 63.46  ? 20  LEU C CB  1 
ATOM 3542 C CG  . LEU C 1 20  ? -55.335 17.129  -17.071 1.00 65.14  ? 20  LEU C CG  1 
ATOM 3543 C CD1 . LEU C 1 20  ? -54.793 17.584  -15.723 1.00 58.63  ? 20  LEU C CD1 1 
ATOM 3544 C CD2 . LEU C 1 20  ? -54.330 17.396  -18.179 1.00 63.41  ? 20  LEU C CD2 1 
ATOM 3545 N N   . THR C 1 21  ? -56.151 12.900  -18.813 1.00 58.46  ? 21  THR C N   1 
ATOM 3546 C CA  . THR C 1 21  ? -56.225 11.444  -18.850 1.00 57.31  ? 21  THR C CA  1 
ATOM 3547 C C   . THR C 1 21  ? -54.820 10.860  -18.826 1.00 61.64  ? 21  THR C C   1 
ATOM 3548 O O   . THR C 1 21  ? -53.898 11.412  -19.433 1.00 60.15  ? 21  THR C O   1 
ATOM 3549 C CB  . THR C 1 21  ? -56.985 10.955  -20.096 1.00 56.66  ? 21  THR C CB  1 
ATOM 3550 O OG1 . THR C 1 21  ? -58.315 11.489  -20.087 1.00 61.32  ? 21  THR C OG1 1 
ATOM 3551 C CG2 . THR C 1 21  ? -57.063 9.437   -20.131 1.00 63.09  ? 21  THR C CG2 1 
ATOM 3552 N N   . CYS C 1 22  ? -54.662 9.738   -18.126 1.00 67.72  ? 22  CYS C N   1 
ATOM 3553 C CA  . CYS C 1 22  ? -53.357 9.127   -17.924 1.00 68.41  ? 22  CYS C CA  1 
ATOM 3554 C C   . CYS C 1 22  ? -53.422 7.673   -18.368 1.00 68.94  ? 22  CYS C C   1 
ATOM 3555 O O   . CYS C 1 22  ? -54.332 6.941   -17.967 1.00 69.00  ? 22  CYS C O   1 
ATOM 3556 C CB  . CYS C 1 22  ? -52.949 9.230   -16.455 1.00 68.75  ? 22  CYS C CB  1 
ATOM 3557 S SG  . CYS C 1 22  ? -51.286 8.688   -16.070 1.00 75.03  ? 22  CYS C SG  1 
ATOM 3558 N N   . ALA C 1 23  ? -52.467 7.257   -19.194 1.00 70.73  ? 23  ALA C N   1 
ATOM 3559 C CA  . ALA C 1 23  ? -52.460 5.916   -19.770 1.00 69.01  ? 23  ALA C CA  1 
ATOM 3560 C C   . ALA C 1 23  ? -51.331 5.102   -19.156 1.00 71.74  ? 23  ALA C C   1 
ATOM 3561 O O   . ALA C 1 23  ? -50.159 5.479   -19.269 1.00 74.93  ? 23  ALA C O   1 
ATOM 3562 C CB  . ALA C 1 23  ? -52.311 5.969   -21.289 1.00 69.47  ? 23  ALA C CB  1 
ATOM 3563 N N   . VAL C 1 24  ? -51.681 3.986   -18.528 1.00 72.02  ? 24  VAL C N   1 
ATOM 3564 C CA  . VAL C 1 24  ? -50.700 3.110   -17.900 1.00 69.41  ? 24  VAL C CA  1 
ATOM 3565 C C   . VAL C 1 24  ? -50.253 2.064   -18.910 1.00 71.93  ? 24  VAL C C   1 
ATOM 3566 O O   . VAL C 1 24  ? -51.070 1.293   -19.427 1.00 76.10  ? 24  VAL C O   1 
ATOM 3567 C CB  . VAL C 1 24  ? -51.268 2.447   -16.639 1.00 65.93  ? 24  VAL C CB  1 
ATOM 3568 C CG1 . VAL C 1 24  ? -50.179 1.651   -15.940 1.00 65.51  ? 24  VAL C CG1 1 
ATOM 3569 C CG2 . VAL C 1 24  ? -51.832 3.503   -15.719 1.00 70.31  ? 24  VAL C CG2 1 
ATOM 3570 N N   . TYR C 1 25  ? -48.955 2.038   -19.185 1.00 70.97  ? 25  TYR C N   1 
ATOM 3571 C CA  . TYR C 1 25  ? -48.345 1.041   -20.048 1.00 73.65  ? 25  TYR C CA  1 
ATOM 3572 C C   . TYR C 1 25  ? -47.417 0.177   -19.207 1.00 78.11  ? 25  TYR C C   1 
ATOM 3573 O O   . TYR C 1 25  ? -46.604 0.697   -18.434 1.00 80.01  ? 25  TYR C O   1 
ATOM 3574 C CB  . TYR C 1 25  ? -47.555 1.703   -21.182 1.00 69.02  ? 25  TYR C CB  1 
ATOM 3575 C CG  . TYR C 1 25  ? -48.411 2.430   -22.191 1.00 71.53  ? 25  TYR C CG  1 
ATOM 3576 C CD1 . TYR C 1 25  ? -49.617 1.894   -22.628 1.00 75.63  ? 25  TYR C CD1 1 
ATOM 3577 C CD2 . TYR C 1 25  ? -48.017 3.658   -22.702 1.00 76.51  ? 25  TYR C CD2 1 
ATOM 3578 C CE1 . TYR C 1 25  ? -50.402 2.561   -23.549 1.00 78.22  ? 25  TYR C CE1 1 
ATOM 3579 C CE2 . TYR C 1 25  ? -48.796 4.334   -23.625 1.00 77.02  ? 25  TYR C CE2 1 
ATOM 3580 C CZ  . TYR C 1 25  ? -49.988 3.780   -24.044 1.00 75.27  ? 25  TYR C CZ  1 
ATOM 3581 O OH  . TYR C 1 25  ? -50.767 4.448   -24.962 1.00 67.98  ? 25  TYR C OH  1 
ATOM 3582 N N   . GLY C 1 26  ? -47.551 -1.140  -19.341 1.00 72.41  ? 26  GLY C N   1 
ATOM 3583 C CA  . GLY C 1 26  ? -46.658 -2.067  -18.680 1.00 63.77  ? 26  GLY C CA  1 
ATOM 3584 C C   . GLY C 1 26  ? -47.192 -2.709  -17.412 1.00 63.06  ? 26  GLY C C   1 
ATOM 3585 O O   . GLY C 1 26  ? -46.464 -3.515  -16.814 1.00 68.84  ? 26  GLY C O   1 
ATOM 3586 N N   . VAL C 1 27  ? -48.400 -2.387  -16.987 1.00 59.82  ? 27  VAL C N   1 
ATOM 3587 C CA  . VAL C 1 27  ? -49.012 -3.026  -15.820 1.00 61.14  ? 27  VAL C CA  1 
ATOM 3588 C C   . VAL C 1 27  ? -50.492 -2.688  -15.800 1.00 59.68  ? 27  VAL C C   1 
ATOM 3589 O O   . VAL C 1 27  ? -50.920 -1.689  -16.388 1.00 69.73  ? 27  VAL C O   1 
ATOM 3590 C CB  . VAL C 1 27  ? -48.301 -2.579  -14.514 1.00 66.48  ? 27  VAL C CB  1 
ATOM 3591 C CG1 . VAL C 1 27  ? -48.853 -1.247  -14.029 1.00 67.73  ? 27  VAL C CG1 1 
ATOM 3592 C CG2 . VAL C 1 27  ? -48.455 -3.650  -13.440 1.00 67.35  ? 27  VAL C CG2 1 
ATOM 3593 N N   . SER C 1 28  ? -51.277 -3.523  -15.124 1.00 59.00  ? 28  SER C N   1 
ATOM 3594 C CA  . SER C 1 28  ? -52.687 -3.246  -14.920 1.00 60.38  ? 28  SER C CA  1 
ATOM 3595 C C   . SER C 1 28  ? -52.865 -2.175  -13.843 1.00 70.14  ? 28  SER C C   1 
ATOM 3596 O O   . SER C 1 28  ? -51.914 -1.747  -13.183 1.00 70.74  ? 28  SER C O   1 
ATOM 3597 C CB  . SER C 1 28  ? -53.428 -4.525  -14.532 1.00 69.14  ? 28  SER C CB  1 
ATOM 3598 O OG  . SER C 1 28  ? -54.726 -4.242  -14.038 1.00 71.68  ? 28  SER C OG  1 
ATOM 3599 N N   . LEU C 1 29  ? -54.112 -1.740  -13.666 1.00 75.74  ? 29  LEU C N   1 
ATOM 3600 C CA  . LEU C 1 29  ? -54.425 -0.701  -12.693 1.00 74.79  ? 29  LEU C CA  1 
ATOM 3601 C C   . LEU C 1 29  ? -54.714 -1.236  -11.297 1.00 75.71  ? 29  LEU C C   1 
ATOM 3602 O O   . LEU C 1 29  ? -54.695 -0.452  -10.342 1.00 77.38  ? 29  LEU C O   1 
ATOM 3603 C CB  . LEU C 1 29  ? -55.617 0.142   -13.167 1.00 70.16  ? 29  LEU C CB  1 
ATOM 3604 C CG  . LEU C 1 29  ? -55.557 0.683   -14.594 1.00 64.54  ? 29  LEU C CG  1 
ATOM 3605 C CD1 . LEU C 1 29  ? -56.946 0.829   -15.179 1.00 76.84  ? 29  LEU C CD1 1 
ATOM 3606 C CD2 . LEU C 1 29  ? -54.844 2.014   -14.592 1.00 62.03  ? 29  LEU C CD2 1 
ATOM 3607 N N   . ARG C 1 30  ? -54.974 -2.530  -11.140 1.00 77.99  ? 30  ARG C N   1 
ATOM 3608 C CA  . ARG C 1 30  ? -55.238 -3.066  -9.814  1.00 81.53  ? 30  ARG C CA  1 
ATOM 3609 C C   . ARG C 1 30  ? -53.944 -3.517  -9.153  1.00 72.80  ? 30  ARG C C   1 
ATOM 3610 O O   . ARG C 1 30  ? -52.973 -3.887  -9.819  1.00 68.60  ? 30  ARG C O   1 
ATOM 3611 C CB  . ARG C 1 30  ? -56.238 -4.222  -9.857  1.00 91.38  ? 30  ARG C CB  1 
ATOM 3612 C CG  . ARG C 1 30  ? -56.965 -4.400  -8.526  1.00 91.75  ? 30  ARG C CG  1 
ATOM 3613 C CD  . ARG C 1 30  ? -57.273 -3.036  -7.938  1.00 100.17 ? 30  ARG C CD  1 
ATOM 3614 N NE  . ARG C 1 30  ? -57.977 -3.059  -6.663  1.00 95.02  ? 30  ARG C NE  1 
ATOM 3615 C CZ  . ARG C 1 30  ? -57.723 -2.218  -5.669  1.00 87.77  ? 30  ARG C CZ  1 
ATOM 3616 N NH1 . ARG C 1 30  ? -56.763 -1.310  -5.761  1.00 85.37  ? 30  ARG C NH1 1 
ATOM 3617 N NH2 . ARG C 1 30  ? -58.452 -2.282  -4.558  1.00 72.91  ? 30  ARG C NH2 1 
ATOM 3618 N N   . GLY C 1 31  ? -53.947 -3.487  -7.825  1.00 74.44  ? 31  GLY C N   1 
ATOM 3619 C CA  . GLY C 1 31  ? -52.737 -3.624  -7.051  1.00 78.56  ? 31  GLY C CA  1 
ATOM 3620 C C   . GLY C 1 31  ? -52.077 -2.312  -6.694  1.00 73.73  ? 31  GLY C C   1 
ATOM 3621 O O   . GLY C 1 31  ? -51.085 -2.317  -5.953  1.00 72.35  ? 31  GLY C O   1 
ATOM 3622 N N   . TYR C 1 32  ? -52.601 -1.190  -7.188  1.00 65.89  ? 32  TYR C N   1 
ATOM 3623 C CA  . TYR C 1 32  ? -51.999 0.117   -6.982  1.00 62.97  ? 32  TYR C CA  1 
ATOM 3624 C C   . TYR C 1 32  ? -53.089 1.134   -6.674  1.00 64.47  ? 32  TYR C C   1 
ATOM 3625 O O   . TYR C 1 32  ? -54.285 0.836   -6.725  1.00 70.45  ? 32  TYR C O   1 
ATOM 3626 C CB  . TYR C 1 32  ? -51.206 0.572   -8.213  1.00 61.48  ? 32  TYR C CB  1 
ATOM 3627 C CG  . TYR C 1 32  ? -50.162 -0.411  -8.683  1.00 62.61  ? 32  TYR C CG  1 
ATOM 3628 C CD1 . TYR C 1 32  ? -48.872 -0.385  -8.173  1.00 66.59  ? 32  TYR C CD1 1 
ATOM 3629 C CD2 . TYR C 1 32  ? -50.465 -1.360  -9.650  1.00 66.04  ? 32  TYR C CD2 1 
ATOM 3630 C CE1 . TYR C 1 32  ? -47.913 -1.284  -8.607  1.00 68.53  ? 32  TYR C CE1 1 
ATOM 3631 C CE2 . TYR C 1 32  ? -49.516 -2.262  -10.090 1.00 70.30  ? 32  TYR C CE2 1 
ATOM 3632 C CZ  . TYR C 1 32  ? -48.242 -2.220  -9.566  1.00 69.60  ? 32  TYR C CZ  1 
ATOM 3633 O OH  . TYR C 1 32  ? -47.297 -3.118  -10.006 1.00 70.17  ? 32  TYR C OH  1 
ATOM 3634 N N   . TYR C 1 33  ? -52.654 2.347   -6.345  1.00 64.63  ? 33  TYR C N   1 
ATOM 3635 C CA  . TYR C 1 33  ? -53.512 3.519   -6.262  1.00 64.26  ? 33  TYR C CA  1 
ATOM 3636 C C   . TYR C 1 33  ? -53.015 4.533   -7.283  1.00 63.56  ? 33  TYR C C   1 
ATOM 3637 O O   . TYR C 1 33  ? -51.836 4.529   -7.652  1.00 64.14  ? 33  TYR C O   1 
ATOM 3638 C CB  . TYR C 1 33  ? -53.492 4.127   -4.853  1.00 65.85  ? 33  TYR C CB  1 
ATOM 3639 C CG  . TYR C 1 33  ? -54.493 3.546   -3.879  1.00 65.24  ? 33  TYR C CG  1 
ATOM 3640 C CD1 . TYR C 1 33  ? -54.827 2.199   -3.911  1.00 66.43  ? 33  TYR C CD1 1 
ATOM 3641 C CD2 . TYR C 1 33  ? -55.052 4.335   -2.882  1.00 65.11  ? 33  TYR C CD2 1 
ATOM 3642 C CE1 . TYR C 1 33  ? -55.729 1.665   -3.006  1.00 70.89  ? 33  TYR C CE1 1 
ATOM 3643 C CE2 . TYR C 1 33  ? -55.947 3.810   -1.971  1.00 66.66  ? 33  TYR C CE2 1 
ATOM 3644 C CZ  . TYR C 1 33  ? -56.281 2.475   -2.036  1.00 68.36  ? 33  TYR C CZ  1 
ATOM 3645 O OH  . TYR C 1 33  ? -57.174 1.953   -1.128  1.00 69.06  ? 33  TYR C OH  1 
ATOM 3646 N N   . TRP C 1 34  ? -53.910 5.399   -7.750  1.00 57.22  ? 34  TRP C N   1 
ATOM 3647 C CA  . TRP C 1 34  ? -53.579 6.317   -8.834  1.00 56.39  ? 34  TRP C CA  1 
ATOM 3648 C C   . TRP C 1 34  ? -53.958 7.735   -8.434  1.00 57.22  ? 34  TRP C C   1 
ATOM 3649 O O   . TRP C 1 34  ? -55.120 8.001   -8.110  1.00 58.03  ? 34  TRP C O   1 
ATOM 3650 C CB  . TRP C 1 34  ? -54.279 5.900   -10.129 1.00 60.00  ? 34  TRP C CB  1 
ATOM 3651 C CG  . TRP C 1 34  ? -54.008 4.467   -10.493 1.00 61.16  ? 34  TRP C CG  1 
ATOM 3652 C CD1 . TRP C 1 34  ? -54.767 3.379   -10.169 1.00 60.20  ? 34  TRP C CD1 1 
ATOM 3653 C CD2 . TRP C 1 34  ? -52.865 3.962   -11.193 1.00 58.14  ? 34  TRP C CD2 1 
ATOM 3654 N NE1 . TRP C 1 34  ? -54.186 2.234   -10.654 1.00 56.24  ? 34  TRP C NE1 1 
ATOM 3655 C CE2 . TRP C 1 34  ? -53.014 2.565   -11.284 1.00 57.66  ? 34  TRP C CE2 1 
ATOM 3656 C CE3 . TRP C 1 34  ? -51.736 4.559   -11.761 1.00 62.39  ? 34  TRP C CE3 1 
ATOM 3657 C CZ2 . TRP C 1 34  ? -52.077 1.755   -11.922 1.00 60.63  ? 34  TRP C CZ2 1 
ATOM 3658 C CZ3 . TRP C 1 34  ? -50.809 3.755   -12.395 1.00 64.00  ? 34  TRP C CZ3 1 
ATOM 3659 C CH2 . TRP C 1 34  ? -50.985 2.367   -12.471 1.00 62.48  ? 34  TRP C CH2 1 
ATOM 3660 N N   . THR C 1 35  ? -52.979 8.640   -8.464  1.00 54.87  ? 35  THR C N   1 
ATOM 3661 C CA  . THR C 1 35  ? -53.141 10.006  -7.989  1.00 53.04  ? 35  THR C CA  1 
ATOM 3662 C C   . THR C 1 35  ? -52.954 11.028  -9.101  1.00 59.50  ? 35  THR C C   1 
ATOM 3663 O O   . THR C 1 35  ? -52.443 10.730  -10.185 1.00 63.98  ? 35  THR C O   1 
ATOM 3664 C CB  . THR C 1 35  ? -52.152 10.333  -6.859  1.00 52.86  ? 35  THR C CB  1 
ATOM 3665 O OG1 . THR C 1 35  ? -50.842 9.850   -7.194  1.00 56.16  ? 35  THR C OG1 1 
ATOM 3666 C CG2 . THR C 1 35  ? -52.612 9.759   -5.556  1.00 55.48  ? 35  THR C CG2 1 
ATOM 3667 N N   . TRP C 1 36  ? -53.391 12.249  -8.797  1.00 54.09  ? 36  TRP C N   1 
ATOM 3668 C CA  . TRP C 1 36  ? -53.119 13.439  -9.591  1.00 55.33  ? 36  TRP C CA  1 
ATOM 3669 C C   . TRP C 1 36  ? -52.478 14.466  -8.671  1.00 58.86  ? 36  TRP C C   1 
ATOM 3670 O O   . TRP C 1 36  ? -53.059 14.828  -7.643  1.00 55.21  ? 36  TRP C O   1 
ATOM 3671 C CB  . TRP C 1 36  ? -54.397 14.002  -10.217 1.00 57.35  ? 36  TRP C CB  1 
ATOM 3672 C CG  . TRP C 1 36  ? -54.905 13.178  -11.344 1.00 55.36  ? 36  TRP C CG  1 
ATOM 3673 C CD1 . TRP C 1 36  ? -55.948 12.310  -11.308 1.00 55.85  ? 36  TRP C CD1 1 
ATOM 3674 C CD2 . TRP C 1 36  ? -54.391 13.136  -12.679 1.00 55.82  ? 36  TRP C CD2 1 
ATOM 3675 N NE1 . TRP C 1 36  ? -56.122 11.723  -12.539 1.00 53.26  ? 36  TRP C NE1 1 
ATOM 3676 C CE2 . TRP C 1 36  ? -55.177 12.215  -13.399 1.00 53.97  ? 36  TRP C CE2 1 
ATOM 3677 C CE3 . TRP C 1 36  ? -53.342 13.786  -13.335 1.00 57.17  ? 36  TRP C CE3 1 
ATOM 3678 C CZ2 . TRP C 1 36  ? -54.949 11.929  -14.741 1.00 56.58  ? 36  TRP C CZ2 1 
ATOM 3679 C CZ3 . TRP C 1 36  ? -53.118 13.499  -14.668 1.00 58.52  ? 36  TRP C CZ3 1 
ATOM 3680 C CH2 . TRP C 1 36  ? -53.918 12.579  -15.357 1.00 59.71  ? 36  TRP C CH2 1 
ATOM 3681 N N   . ILE C 1 37  ? -51.277 14.916  -9.029  1.00 57.18  ? 37  ILE C N   1 
ATOM 3682 C CA  . ILE C 1 37  ? -50.529 15.893  -8.246  1.00 61.49  ? 37  ILE C CA  1 
ATOM 3683 C C   . ILE C 1 37  ? -50.184 17.065  -9.153  1.00 59.63  ? 37  ILE C C   1 
ATOM 3684 O O   . ILE C 1 37  ? -49.693 16.864  -10.270 1.00 58.52  ? 37  ILE C O   1 
ATOM 3685 C CB  . ILE C 1 37  ? -49.247 15.288  -7.639  1.00 61.09  ? 37  ILE C CB  1 
ATOM 3686 C CG1 . ILE C 1 37  ? -49.526 13.897  -7.067  1.00 59.35  ? 37  ILE C CG1 1 
ATOM 3687 C CG2 . ILE C 1 37  ? -48.684 16.205  -6.562  1.00 56.51  ? 37  ILE C CG2 1 
ATOM 3688 C CD1 . ILE C 1 37  ? -50.158 13.915  -5.697  1.00 61.04  ? 37  ILE C CD1 1 
ATOM 3689 N N   . ARG C 1 38  ? -50.430 18.282  -8.675  1.00 57.91  ? 38  ARG C N   1 
ATOM 3690 C CA  . ARG C 1 38  ? -50.167 19.487  -9.446  1.00 51.14  ? 38  ARG C CA  1 
ATOM 3691 C C   . ARG C 1 38  ? -49.139 20.354  -8.735  1.00 51.28  ? 38  ARG C C   1 
ATOM 3692 O O   . ARG C 1 38  ? -49.009 20.317  -7.507  1.00 51.27  ? 38  ARG C O   1 
ATOM 3693 C CB  . ARG C 1 38  ? -51.454 20.287  -9.695  1.00 51.06  ? 38  ARG C CB  1 
ATOM 3694 C CG  . ARG C 1 38  ? -52.160 20.782  -8.441  1.00 50.94  ? 38  ARG C CG  1 
ATOM 3695 C CD  . ARG C 1 38  ? -53.418 21.562  -8.809  1.00 50.87  ? 38  ARG C CD  1 
ATOM 3696 N NE  . ARG C 1 38  ? -54.020 22.240  -7.667  1.00 52.25  ? 38  ARG C NE  1 
ATOM 3697 C CZ  . ARG C 1 38  ? -55.142 22.946  -7.721  1.00 54.90  ? 38  ARG C CZ  1 
ATOM 3698 N NH1 . ARG C 1 38  ? -55.809 23.097  -8.854  1.00 51.68  ? 38  ARG C NH1 1 
ATOM 3699 N NH2 . ARG C 1 38  ? -55.606 23.514  -6.611  1.00 57.84  ? 38  ARG C NH2 1 
ATOM 3700 N N   . GLN C 1 39  ? -48.405 21.136  -9.522  1.00 51.46  ? 39  GLN C N   1 
ATOM 3701 C CA  . GLN C 1 39  ? -47.318 21.960  -9.007  1.00 54.12  ? 39  GLN C CA  1 
ATOM 3702 C C   . GLN C 1 39  ? -47.440 23.369  -9.556  1.00 59.26  ? 39  GLN C C   1 
ATOM 3703 O O   . GLN C 1 39  ? -47.448 23.564  -10.774 1.00 65.87  ? 39  GLN C O   1 
ATOM 3704 C CB  . GLN C 1 39  ? -45.956 21.369  -9.372  1.00 59.80  ? 39  GLN C CB  1 
ATOM 3705 C CG  . GLN C 1 39  ? -44.789 22.170  -8.833  1.00 62.70  ? 39  GLN C CG  1 
ATOM 3706 C CD  . GLN C 1 39  ? -43.463 21.494  -9.084  1.00 72.39  ? 39  GLN C CD  1 
ATOM 3707 O OE1 . GLN C 1 39  ? -43.303 20.770  -10.064 1.00 75.02  ? 39  GLN C OE1 1 
ATOM 3708 N NE2 . GLN C 1 39  ? -42.495 21.738  -8.207  1.00 72.34  ? 39  GLN C NE2 1 
ATOM 3709 N N   . SER C 1 40  ? -47.509 24.346  -8.661  1.00 61.32  ? 40  SER C N   1 
ATOM 3710 C CA  . SER C 1 40  ? -47.594 25.740  -9.056  1.00 59.36  ? 40  SER C CA  1 
ATOM 3711 C C   . SER C 1 40  ? -46.830 26.554  -8.030  1.00 64.63  ? 40  SER C C   1 
ATOM 3712 O O   . SER C 1 40  ? -46.802 26.177  -6.852  1.00 58.25  ? 40  SER C O   1 
ATOM 3713 C CB  . SER C 1 40  ? -49.053 26.209  -9.138  1.00 59.75  ? 40  SER C CB  1 
ATOM 3714 O OG  . SER C 1 40  ? -49.779 25.827  -7.977  1.00 58.76  ? 40  SER C OG  1 
ATOM 3715 N N   . PRO C 1 41  ? -46.225 27.686  -8.428  1.00 68.63  ? 41  PRO C N   1 
ATOM 3716 C CA  . PRO C 1 41  ? -45.595 28.574  -7.435  1.00 65.77  ? 41  PRO C CA  1 
ATOM 3717 C C   . PRO C 1 41  ? -46.525 28.885  -6.302  1.00 61.63  ? 41  PRO C C   1 
ATOM 3718 O O   . PRO C 1 41  ? -46.106 29.357  -5.237  1.00 60.26  ? 41  PRO C O   1 
ATOM 3719 C CB  . PRO C 1 41  ? -45.332 29.845  -8.243  1.00 62.47  ? 41  PRO C CB  1 
ATOM 3720 C CG  . PRO C 1 41  ? -45.086 29.354  -9.599  1.00 72.19  ? 41  PRO C CG  1 
ATOM 3721 C CD  . PRO C 1 41  ? -46.049 28.203  -9.799  1.00 73.87  ? 41  PRO C CD  1 
ATOM 3722 N N   . LYS C 1 42  ? -47.802 28.612  -6.522  1.00 61.86  ? 42  LYS C N   1 
ATOM 3723 C CA  . LYS C 1 42  ? -48.884 29.258  -5.828  1.00 55.95  ? 42  LYS C CA  1 
ATOM 3724 C C   . LYS C 1 42  ? -49.576 28.319  -4.856  1.00 59.49  ? 42  LYS C C   1 
ATOM 3725 O O   . LYS C 1 42  ? -49.902 28.726  -3.738  1.00 52.70  ? 42  LYS C O   1 
ATOM 3726 C CB  . LYS C 1 42  ? -49.857 29.831  -6.856  1.00 59.32  ? 42  LYS C CB  1 
ATOM 3727 C CG  . LYS C 1 42  ? -50.789 30.705  -6.170  1.00 60.19  ? 42  LYS C CG  1 
ATOM 3728 C CD  . LYS C 1 42  ? -51.642 31.583  -7.021  1.00 57.64  ? 42  LYS C CD  1 
ATOM 3729 C CE  . LYS C 1 42  ? -52.785 31.783  -6.154  1.00 61.14  ? 42  LYS C CE  1 
ATOM 3730 N NZ  . LYS C 1 42  ? -52.297 32.713  -5.084  1.00 66.05  ? 42  LYS C NZ  1 
ATOM 3731 N N   . LYS C 1 43  ? -49.841 27.088  -5.280  1.00 64.29  ? 43  LYS C N   1 
ATOM 3732 C CA  . LYS C 1 43  ? -50.336 26.037  -4.400  1.00 62.14  ? 43  LYS C CA  1 
ATOM 3733 C C   . LYS C 1 43  ? -49.220 25.101  -3.950  1.00 52.37  ? 43  LYS C C   1 
ATOM 3734 O O   . LYS C 1 43  ? -49.454 24.222  -3.114  1.00 52.24  ? 43  LYS C O   1 
ATOM 3735 C CB  . LYS C 1 43  ? -51.426 25.238  -5.115  1.00 61.16  ? 43  LYS C CB  1 
ATOM 3736 C CG  . LYS C 1 43  ? -52.295 26.104  -6.027  1.00 64.06  ? 43  LYS C CG  1 
ATOM 3737 C CD  . LYS C 1 43  ? -53.259 26.971  -5.261  1.00 71.42  ? 43  LYS C CD  1 
ATOM 3738 C CE  . LYS C 1 43  ? -54.457 26.133  -4.859  1.00 63.48  ? 43  LYS C CE  1 
ATOM 3739 N NZ  . LYS C 1 43  ? -55.590 26.948  -4.364  1.00 69.13  ? 43  LYS C NZ  1 
ATOM 3740 N N   . GLY C 1 44  ? -48.019 25.274  -4.496  1.00 51.95  ? 44  GLY C N   1 
ATOM 3741 C CA  . GLY C 1 44  ? -46.919 24.383  -4.175  1.00 52.00  ? 44  GLY C CA  1 
ATOM 3742 C C   . GLY C 1 44  ? -47.125 23.025  -4.815  1.00 55.33  ? 44  GLY C C   1 
ATOM 3743 O O   . GLY C 1 44  ? -47.507 22.908  -5.982  1.00 63.58  ? 44  GLY C O   1 
ATOM 3744 N N   . LEU C 1 45  ? -46.872 21.978  -4.034  1.00 55.78  ? 45  LEU C N   1 
ATOM 3745 C CA  . LEU C 1 45  ? -47.133 20.605  -4.447  1.00 54.14  ? 45  LEU C CA  1 
ATOM 3746 C C   . LEU C 1 45  ? -48.452 20.191  -3.808  1.00 54.34  ? 45  LEU C C   1 
ATOM 3747 O O   . LEU C 1 45  ? -48.509 19.898  -2.612  1.00 51.66  ? 45  LEU C O   1 
ATOM 3748 C CB  . LEU C 1 45  ? -45.996 19.682  -4.035  1.00 56.78  ? 45  LEU C CB  1 
ATOM 3749 C CG  . LEU C 1 45  ? -45.043 19.218  -5.138  1.00 58.28  ? 45  LEU C CG  1 
ATOM 3750 C CD1 . LEU C 1 45  ? -45.782 18.371  -6.158  1.00 56.21  ? 45  LEU C CD1 1 
ATOM 3751 C CD2 . LEU C 1 45  ? -44.372 20.411  -5.798  1.00 62.81  ? 45  LEU C CD2 1 
ATOM 3752 N N   . GLU C 1 46  ? -49.515 20.169  -4.606  1.00 54.32  ? 46  GLU C N   1 
ATOM 3753 C CA  . GLU C 1 46  ? -50.856 19.882  -4.117  1.00 58.96  ? 46  GLU C CA  1 
ATOM 3754 C C   . GLU C 1 46  ? -51.304 18.508  -4.592  1.00 55.76  ? 46  GLU C C   1 
ATOM 3755 O O   . GLU C 1 46  ? -51.210 18.197  -5.784  1.00 52.99  ? 46  GLU C O   1 
ATOM 3756 C CB  . GLU C 1 46  ? -51.851 20.946  -4.585  1.00 54.47  ? 46  GLU C CB  1 
ATOM 3757 C CG  . GLU C 1 46  ? -53.101 21.014  -3.734  1.00 56.39  ? 46  GLU C CG  1 
ATOM 3758 C CD  . GLU C 1 46  ? -53.996 22.165  -4.119  1.00 59.51  ? 46  GLU C CD  1 
ATOM 3759 O OE1 . GLU C 1 46  ? -53.643 22.895  -5.067  1.00 60.90  ? 46  GLU C OE1 1 
ATOM 3760 O OE2 . GLU C 1 46  ? -55.050 22.341  -3.474  1.00 60.46  ? 46  GLU C OE2 1 
ATOM 3761 N N   . TRP C 1 47  ? -51.791 17.696  -3.658  1.00 53.90  ? 47  TRP C N   1 
ATOM 3762 C CA  . TRP C 1 47  ? -52.365 16.392  -3.959  1.00 57.36  ? 47  TRP C CA  1 
ATOM 3763 C C   . TRP C 1 47  ? -53.859 16.561  -4.206  1.00 59.53  ? 47  TRP C C   1 
ATOM 3764 O O   . TRP C 1 47  ? -54.600 16.961  -3.301  1.00 59.70  ? 47  TRP C O   1 
ATOM 3765 C CB  . TRP C 1 47  ? -52.100 15.422  -2.806  1.00 58.21  ? 47  TRP C CB  1 
ATOM 3766 C CG  . TRP C 1 47  ? -52.948 14.182  -2.813  1.00 52.03  ? 47  TRP C CG  1 
ATOM 3767 C CD1 . TRP C 1 47  ? -52.721 13.036  -3.517  1.00 54.82  ? 47  TRP C CD1 1 
ATOM 3768 C CD2 . TRP C 1 47  ? -54.146 13.956  -2.055  1.00 51.98  ? 47  TRP C CD2 1 
ATOM 3769 N NE1 . TRP C 1 47  ? -53.706 12.114  -3.254  1.00 61.89  ? 47  TRP C NE1 1 
ATOM 3770 C CE2 . TRP C 1 47  ? -54.593 12.654  -2.360  1.00 61.08  ? 47  TRP C CE2 1 
ATOM 3771 C CE3 . TRP C 1 47  ? -54.885 14.729  -1.154  1.00 57.90  ? 47  TRP C CE3 1 
ATOM 3772 C CZ2 . TRP C 1 47  ? -55.746 12.109  -1.797  1.00 63.82  ? 47  TRP C CZ2 1 
ATOM 3773 C CZ3 . TRP C 1 47  ? -56.030 14.187  -0.596  1.00 58.55  ? 47  TRP C CZ3 1 
ATOM 3774 C CH2 . TRP C 1 47  ? -56.449 12.889  -0.920  1.00 62.60  ? 47  TRP C CH2 1 
ATOM 3775 N N   . ILE C 1 48  ? -54.299 16.260  -5.426  1.00 58.32  ? 48  ILE C N   1 
ATOM 3776 C CA  . ILE C 1 48  ? -55.697 16.475  -5.791  1.00 53.15  ? 48  ILE C CA  1 
ATOM 3777 C C   . ILE C 1 48  ? -56.577 15.352  -5.252  1.00 55.04  ? 48  ILE C C   1 
ATOM 3778 O O   . ILE C 1 48  ? -57.536 15.595  -4.510  1.00 55.41  ? 48  ILE C O   1 
ATOM 3779 C CB  . ILE C 1 48  ? -55.838 16.625  -7.317  1.00 50.36  ? 48  ILE C CB  1 
ATOM 3780 C CG1 . ILE C 1 48  ? -54.783 17.592  -7.859  1.00 51.36  ? 48  ILE C CG1 1 
ATOM 3781 C CG2 . ILE C 1 48  ? -57.234 17.100  -7.679  1.00 50.62  ? 48  ILE C CG2 1 
ATOM 3782 C CD1 . ILE C 1 48  ? -54.641 17.564  -9.364  1.00 50.53  ? 48  ILE C CD1 1 
ATOM 3783 N N   . GLY C 1 49  ? -56.266 14.114  -5.616  1.00 53.09  ? 49  GLY C N   1 
ATOM 3784 C CA  . GLY C 1 49  ? -57.041 12.979  -5.149  1.00 53.63  ? 49  GLY C CA  1 
ATOM 3785 C C   . GLY C 1 49  ? -56.446 11.688  -5.665  1.00 58.70  ? 49  GLY C C   1 
ATOM 3786 O O   . GLY C 1 49  ? -55.474 11.684  -6.427  1.00 57.38  ? 49  GLY C O   1 
ATOM 3787 N N   . GLU C 1 50  ? -57.051 10.579  -5.239  1.00 60.89  ? 50  GLU C N   1 
ATOM 3788 C CA  . GLU C 1 50  ? -56.605 9.257   -5.659  1.00 58.75  ? 50  GLU C CA  1 
ATOM 3789 C C   . GLU C 1 50  ? -57.805 8.351   -5.888  1.00 59.69  ? 50  GLU C C   1 
ATOM 3790 O O   . GLU C 1 50  ? -58.918 8.626   -5.432  1.00 54.17  ? 50  GLU C O   1 
ATOM 3791 C CB  . GLU C 1 50  ? -55.653 8.622   -4.637  1.00 63.72  ? 50  GLU C CB  1 
ATOM 3792 C CG  . GLU C 1 50  ? -56.290 8.141   -3.357  1.00 64.85  ? 50  GLU C CG  1 
ATOM 3793 C CD  . GLU C 1 50  ? -55.257 7.639   -2.369  1.00 67.67  ? 50  GLU C CD  1 
ATOM 3794 O OE1 . GLU C 1 50  ? -54.049 7.802   -2.647  1.00 68.72  ? 50  GLU C OE1 1 
ATOM 3795 O OE2 . GLU C 1 50  ? -55.645 7.092   -1.316  1.00 69.91  ? 50  GLU C OE2 1 
ATOM 3796 N N   . ILE C 1 51  ? -57.557 7.255   -6.608  1.00 67.04  ? 51  ILE C N   1 
ATOM 3797 C CA  . ILE C 1 51  ? -58.594 6.288   -6.944  1.00 70.20  ? 51  ILE C CA  1 
ATOM 3798 C C   . ILE C 1 51  ? -57.971 4.901   -6.983  1.00 73.77  ? 51  ILE C C   1 
ATOM 3799 O O   . ILE C 1 51  ? -56.776 4.742   -7.247  1.00 68.72  ? 51  ILE C O   1 
ATOM 3800 C CB  . ILE C 1 51  ? -59.282 6.626   -8.290  1.00 63.95  ? 51  ILE C CB  1 
ATOM 3801 C CG1 . ILE C 1 51  ? -60.611 5.873   -8.429  1.00 68.28  ? 51  ILE C CG1 1 
ATOM 3802 C CG2 . ILE C 1 51  ? -58.357 6.337   -9.461  1.00 61.16  ? 51  ILE C CG2 1 
ATOM 3803 C CD1 . ILE C 1 51  ? -61.449 6.297   -9.625  1.00 69.36  ? 51  ILE C CD1 1 
ATOM 3804 N N   . ASP C 1 52  ? -58.788 3.897   -6.696  1.00 86.68  ? 52  ASP C N   1 
ATOM 3805 C CA  . ASP C 1 52  ? -58.433 2.508   -6.921  1.00 89.43  ? 52  ASP C CA  1 
ATOM 3806 C C   . ASP C 1 52  ? -59.256 1.968   -8.084  1.00 105.16 ? 52  ASP C C   1 
ATOM 3807 O O   . ASP C 1 52  ? -60.189 2.613   -8.568  1.00 106.63 ? 52  ASP C O   1 
ATOM 3808 C CB  . ASP C 1 52  ? -58.647 1.674   -5.652  1.00 84.51  ? 52  ASP C CB  1 
ATOM 3809 C CG  . ASP C 1 52  ? -60.001 1.913   -5.018  1.00 84.10  ? 52  ASP C CG  1 
ATOM 3810 O OD1 . ASP C 1 52  ? -60.999 1.377   -5.542  1.00 83.69  ? 52  ASP C OD1 1 
ATOM 3811 O OD2 . ASP C 1 52  ? -60.070 2.632   -3.998  1.00 90.50  ? 52  ASP C OD2 1 
ATOM 3812 N N   . GLU C 1 53  ? -58.888 0.770   -8.539  1.00 168.85 ? 53  GLU C N   1 
ATOM 3813 C CA  . GLU C 1 53  ? -59.528 0.197   -9.720  1.00 168.93 ? 53  GLU C CA  1 
ATOM 3814 C C   . GLU C 1 53  ? -61.002 -0.112  -9.484  1.00 168.55 ? 53  GLU C C   1 
ATOM 3815 O O   . GLU C 1 53  ? -61.808 -0.001  -10.415 1.00 167.85 ? 53  GLU C O   1 
ATOM 3816 C CB  . GLU C 1 53  ? -58.776 -1.058  -10.156 1.00 170.08 ? 53  GLU C CB  1 
ATOM 3817 C CG  . GLU C 1 53  ? -59.431 -1.853  -11.269 1.00 170.43 ? 53  GLU C CG  1 
ATOM 3818 C CD  . GLU C 1 53  ? -60.114 -3.116  -10.768 1.00 171.25 ? 53  GLU C CD  1 
ATOM 3819 O OE1 . GLU C 1 53  ? -60.444 -3.181  -9.565  1.00 171.47 ? 53  GLU C OE1 1 
ATOM 3820 O OE2 . GLU C 1 53  ? -60.329 -4.040  -11.581 1.00 171.56 ? 53  GLU C OE2 1 
ATOM 3821 N N   . ILE C 1 54  ? -61.375 -0.497  -8.261  1.00 124.24 ? 54  ILE C N   1 
ATOM 3822 C CA  . ILE C 1 54  ? -62.782 -0.768  -7.974  1.00 108.64 ? 54  ILE C CA  1 
ATOM 3823 C C   . ILE C 1 54  ? -63.622 0.489   -8.160  1.00 103.93 ? 54  ILE C C   1 
ATOM 3824 O O   . ILE C 1 54  ? -64.815 0.408   -8.476  1.00 98.85  ? 54  ILE C O   1 
ATOM 3825 C CB  . ILE C 1 54  ? -62.941 -1.353  -6.556  1.00 99.97  ? 54  ILE C CB  1 
ATOM 3826 C CG1 . ILE C 1 54  ? -61.930 -2.478  -6.326  1.00 109.06 ? 54  ILE C CG1 1 
ATOM 3827 C CG2 . ILE C 1 54  ? -64.358 -1.865  -6.337  1.00 85.38  ? 54  ILE C CG2 1 
ATOM 3828 C CD1 . ILE C 1 54  ? -62.115 -3.207  -5.009  1.00 98.23  ? 54  ILE C CD1 1 
ATOM 3829 N N   . GLY C 1 55  ? -63.022 1.662   -7.981  1.00 99.69  ? 55  GLY C N   1 
ATOM 3830 C CA  . GLY C 1 55  ? -63.683 2.924   -8.256  1.00 82.87  ? 55  GLY C CA  1 
ATOM 3831 C C   . GLY C 1 55  ? -63.783 3.867   -7.078  1.00 80.79  ? 55  GLY C C   1 
ATOM 3832 O O   . GLY C 1 55  ? -64.205 5.018   -7.266  1.00 82.20  ? 55  GLY C O   1 
ATOM 3833 N N   . ARG C 1 56  ? -63.418 3.444   -5.871  1.00 81.22  ? 56  ARG C N   1 
ATOM 3834 C CA  . ARG C 1 56  ? -63.528 4.323   -4.717  1.00 77.99  ? 56  ARG C CA  1 
ATOM 3835 C C   . ARG C 1 56  ? -62.486 5.432   -4.792  1.00 74.47  ? 56  ARG C C   1 
ATOM 3836 O O   . ARG C 1 56  ? -61.344 5.211   -5.207  1.00 71.34  ? 56  ARG C O   1 
ATOM 3837 C CB  . ARG C 1 56  ? -63.367 3.530   -3.422  1.00 82.29  ? 56  ARG C CB  1 
ATOM 3838 C CG  . ARG C 1 56  ? -63.676 4.340   -2.176  1.00 85.04  ? 56  ARG C CG  1 
ATOM 3839 C CD  . ARG C 1 56  ? -65.131 4.787   -2.169  1.00 81.30  ? 56  ARG C CD  1 
ATOM 3840 N NE  . ARG C 1 56  ? -65.308 6.067   -1.492  1.00 79.49  ? 56  ARG C NE  1 
ATOM 3841 C CZ  . ARG C 1 56  ? -65.589 7.210   -2.103  1.00 82.89  ? 56  ARG C CZ  1 
ATOM 3842 N NH1 . ARG C 1 56  ? -65.737 7.274   -3.417  1.00 84.95  ? 56  ARG C NH1 1 
ATOM 3843 N NH2 . ARG C 1 56  ? -65.726 8.317   -1.377  1.00 77.48  ? 56  ARG C NH2 1 
ATOM 3844 N N   . THR C 1 57  ? -62.887 6.633   -4.384  1.00 80.35  ? 57  THR C N   1 
ATOM 3845 C CA  . THR C 1 57  ? -62.061 7.822   -4.511  1.00 77.46  ? 57  THR C CA  1 
ATOM 3846 C C   . THR C 1 57  ? -61.897 8.496   -3.156  1.00 71.93  ? 57  THR C C   1 
ATOM 3847 O O   . THR C 1 57  ? -62.719 8.333   -2.251  1.00 77.11  ? 57  THR C O   1 
ATOM 3848 C CB  . THR C 1 57  ? -62.676 8.828   -5.494  1.00 78.98  ? 57  THR C CB  1 
ATOM 3849 O OG1 . THR C 1 57  ? -64.000 9.165   -5.064  1.00 79.67  ? 57  THR C OG1 1 
ATOM 3850 C CG2 . THR C 1 57  ? -62.762 8.232   -6.885  1.00 78.32  ? 57  THR C CG2 1 
ATOM 3851 N N   . LYS C 1 58  ? -60.811 9.257   -3.032  1.00 60.61  ? 58  LYS C N   1 
ATOM 3852 C CA  . LYS C 1 58  ? -60.644 10.217  -1.949  1.00 64.09  ? 58  LYS C CA  1 
ATOM 3853 C C   . LYS C 1 58  ? -60.025 11.476  -2.538  1.00 66.95  ? 58  LYS C C   1 
ATOM 3854 O O   . LYS C 1 58  ? -59.034 11.401  -3.270  1.00 66.06  ? 58  LYS C O   1 
ATOM 3855 C CB  . LYS C 1 58  ? -59.797 9.645   -0.795  1.00 64.85  ? 58  LYS C CB  1 
ATOM 3856 C CG  . LYS C 1 58  ? -58.284 9.700   -0.964  1.00 63.64  ? 58  LYS C CG  1 
ATOM 3857 C CD  . LYS C 1 58  ? -57.563 9.385   0.338   1.00 66.64  ? 58  LYS C CD  1 
ATOM 3858 C CE  . LYS C 1 58  ? -57.978 10.336  1.445   1.00 65.59  ? 58  LYS C CE  1 
ATOM 3859 N NZ  . LYS C 1 58  ? -57.199 10.089  2.688   1.00 68.03  ? 58  LYS C NZ  1 
ATOM 3860 N N   . TYR C 1 59  ? -60.640 12.622  -2.265  1.00 63.30  ? 59  TYR C N   1 
ATOM 3861 C CA  . TYR C 1 59  ? -60.207 13.898  -2.816  1.00 63.84  ? 59  TYR C CA  1 
ATOM 3862 C C   . TYR C 1 59  ? -59.701 14.812  -1.709  1.00 70.95  ? 59  TYR C C   1 
ATOM 3863 O O   . TYR C 1 59  ? -59.763 14.491  -0.519  1.00 69.51  ? 59  TYR C O   1 
ATOM 3864 C CB  . TYR C 1 59  ? -61.348 14.594  -3.572  1.00 67.84  ? 59  TYR C CB  1 
ATOM 3865 C CG  . TYR C 1 59  ? -62.021 13.759  -4.641  1.00 60.08  ? 59  TYR C CG  1 
ATOM 3866 C CD1 . TYR C 1 59  ? -61.422 13.562  -5.879  1.00 55.54  ? 59  TYR C CD1 1 
ATOM 3867 C CD2 . TYR C 1 59  ? -63.265 13.184  -4.417  1.00 54.97  ? 59  TYR C CD2 1 
ATOM 3868 C CE1 . TYR C 1 59  ? -62.041 12.807  -6.858  1.00 54.67  ? 59  TYR C CE1 1 
ATOM 3869 C CE2 . TYR C 1 59  ? -63.888 12.426  -5.389  1.00 58.92  ? 59  TYR C CE2 1 
ATOM 3870 C CZ  . TYR C 1 59  ? -63.272 12.241  -6.608  1.00 60.28  ? 59  TYR C CZ  1 
ATOM 3871 O OH  . TYR C 1 59  ? -63.893 11.487  -7.578  1.00 65.31  ? 59  TYR C OH  1 
ATOM 3872 N N   . SER C 1 60  ? -59.186 15.965  -2.126  1.00 76.00  ? 60  SER C N   1 
ATOM 3873 C CA  . SER C 1 60  ? -58.889 17.040  -1.193  1.00 76.79  ? 60  SER C CA  1 
ATOM 3874 C C   . SER C 1 60  ? -60.155 17.841  -0.930  1.00 77.98  ? 60  SER C C   1 
ATOM 3875 O O   . SER C 1 60  ? -60.958 18.071  -1.839  1.00 79.72  ? 60  SER C O   1 
ATOM 3876 C CB  . SER C 1 60  ? -57.791 17.948  -1.747  1.00 76.91  ? 60  SER C CB  1 
ATOM 3877 O OG  . SER C 1 60  ? -57.641 19.112  -0.954  1.00 77.48  ? 60  SER C OG  1 
ATOM 3878 N N   . GLN C 1 61  ? -60.340 18.252  0.326   1.00 71.75  ? 61  GLN C N   1 
ATOM 3879 C CA  . GLN C 1 61  ? -61.544 18.995  0.685   1.00 72.73  ? 61  GLN C CA  1 
ATOM 3880 C C   . GLN C 1 61  ? -61.625 20.323  -0.053  1.00 76.79  ? 61  GLN C C   1 
ATOM 3881 O O   . GLN C 1 61  ? -62.725 20.796  -0.362  1.00 83.62  ? 61  GLN C O   1 
ATOM 3882 C CB  . GLN C 1 61  ? -61.589 19.222  2.196   1.00 75.20  ? 61  GLN C CB  1 
ATOM 3883 C CG  . GLN C 1 61  ? -61.616 17.939  3.010   1.00 85.58  ? 61  GLN C CG  1 
ATOM 3884 C CD  . GLN C 1 61  ? -62.925 17.187  2.868   1.00 95.93  ? 61  GLN C CD  1 
ATOM 3885 O OE1 . GLN C 1 61  ? -63.954 17.766  2.522   1.00 95.71  ? 61  GLN C OE1 1 
ATOM 3886 N NE2 . GLN C 1 61  ? -62.890 15.886  3.129   1.00 92.62  ? 61  GLN C NE2 1 
ATOM 3887 N N   . SER C 1 62  ? -60.477 20.935  -0.351  1.00 70.92  ? 62  SER C N   1 
ATOM 3888 C CA  . SER C 1 62  ? -60.486 22.206  -1.066  1.00 70.29  ? 62  SER C CA  1 
ATOM 3889 C C   . SER C 1 62  ? -60.899 22.034  -2.522  1.00 76.11  ? 62  SER C C   1 
ATOM 3890 O O   . SER C 1 62  ? -61.432 22.971  -3.127  1.00 75.12  ? 62  SER C O   1 
ATOM 3891 C CB  . SER C 1 62  ? -59.108 22.863  -0.986  1.00 67.18  ? 62  SER C CB  1 
ATOM 3892 O OG  . SER C 1 62  ? -58.091 21.970  -1.406  1.00 66.66  ? 62  SER C OG  1 
ATOM 3893 N N   . LEU C 1 63  ? -60.667 20.854  -3.098  1.00 75.59  ? 63  LEU C N   1 
ATOM 3894 C CA  . LEU C 1 63  ? -60.915 20.616  -4.513  1.00 59.93  ? 63  LEU C CA  1 
ATOM 3895 C C   . LEU C 1 63  ? -62.042 19.626  -4.774  1.00 68.84  ? 63  LEU C C   1 
ATOM 3896 O O   . LEU C 1 63  ? -62.367 19.382  -5.939  1.00 69.00  ? 63  LEU C O   1 
ATOM 3897 C CB  . LEU C 1 63  ? -59.634 20.114  -5.194  1.00 54.88  ? 63  LEU C CB  1 
ATOM 3898 C CG  . LEU C 1 63  ? -58.424 21.050  -5.223  1.00 59.37  ? 63  LEU C CG  1 
ATOM 3899 C CD1 . LEU C 1 63  ? -57.206 20.328  -5.782  1.00 54.84  ? 63  LEU C CD1 1 
ATOM 3900 C CD2 . LEU C 1 63  ? -58.733 22.293  -6.042  1.00 62.83  ? 63  LEU C CD2 1 
ATOM 3901 N N   . ARG C 1 64  ? -62.663 19.072  -3.729  1.00 66.93  ? 64  ARG C N   1 
ATOM 3902 C CA  . ARG C 1 64  ? -63.572 17.940  -3.910  1.00 68.33  ? 64  ARG C CA  1 
ATOM 3903 C C   . ARG C 1 64  ? -64.787 18.307  -4.756  1.00 67.61  ? 64  ARG C C   1 
ATOM 3904 O O   . ARG C 1 64  ? -65.141 17.583  -5.692  1.00 73.93  ? 64  ARG C O   1 
ATOM 3905 C CB  . ARG C 1 64  ? -64.017 17.403  -2.551  1.00 73.77  ? 64  ARG C CB  1 
ATOM 3906 C CG  . ARG C 1 64  ? -64.751 16.074  -2.634  1.00 81.63  ? 64  ARG C CG  1 
ATOM 3907 C CD  . ARG C 1 64  ? -64.653 15.298  -1.333  1.00 84.88  ? 64  ARG C CD  1 
ATOM 3908 N NE  . ARG C 1 64  ? -65.629 15.766  -0.356  1.00 90.50  ? 64  ARG C NE  1 
ATOM 3909 C CZ  . ARG C 1 64  ? -66.790 15.174  -0.112  1.00 90.36  ? 64  ARG C CZ  1 
ATOM 3910 N NH1 . ARG C 1 64  ? -67.168 14.091  -0.772  1.00 81.39  ? 64  ARG C NH1 1 
ATOM 3911 N NH2 . ARG C 1 64  ? -67.594 15.683  0.817   1.00 88.84  ? 64  ARG C NH2 1 
ATOM 3912 N N   . SER C 1 65  ? -65.452 19.420  -4.427  1.00 62.42  ? 65  SER C N   1 
ATOM 3913 C CA  . SER C 1 65  ? -66.703 19.771  -5.095  1.00 61.85  ? 65  SER C CA  1 
ATOM 3914 C C   . SER C 1 65  ? -66.529 19.927  -6.600  1.00 62.88  ? 65  SER C C   1 
ATOM 3915 O O   . SER C 1 65  ? -67.445 19.610  -7.368  1.00 61.69  ? 65  SER C O   1 
ATOM 3916 C CB  . SER C 1 65  ? -67.272 21.058  -4.499  1.00 58.12  ? 65  SER C CB  1 
ATOM 3917 O OG  . SER C 1 65  ? -68.561 21.330  -5.017  1.00 69.93  ? 65  SER C OG  1 
ATOM 3918 N N   . ARG C 1 66  ? -65.374 20.414  -7.038  1.00 56.46  ? 66  ARG C N   1 
ATOM 3919 C CA  . ARG C 1 66  ? -65.113 20.622  -8.453  1.00 55.76  ? 66  ARG C CA  1 
ATOM 3920 C C   . ARG C 1 66  ? -64.386 19.456  -9.104  1.00 62.41  ? 66  ARG C C   1 
ATOM 3921 O O   . ARG C 1 66  ? -64.200 19.471  -10.325 1.00 62.25  ? 66  ARG C O   1 
ATOM 3922 C CB  . ARG C 1 66  ? -64.285 21.890  -8.652  1.00 57.81  ? 66  ARG C CB  1 
ATOM 3923 C CG  . ARG C 1 66  ? -64.804 23.112  -7.919  1.00 55.16  ? 66  ARG C CG  1 
ATOM 3924 C CD  . ARG C 1 66  ? -63.633 24.002  -7.564  1.00 49.66  ? 66  ARG C CD  1 
ATOM 3925 N NE  . ARG C 1 66  ? -62.709 24.126  -8.682  1.00 49.95  ? 66  ARG C NE  1 
ATOM 3926 C CZ  . ARG C 1 66  ? -61.435 24.469  -8.563  1.00 50.15  ? 66  ARG C CZ  1 
ATOM 3927 N NH1 . ARG C 1 66  ? -60.891 24.710  -7.381  1.00 50.12  ? 66  ARG C NH1 1 
ATOM 3928 N NH2 . ARG C 1 66  ? -60.684 24.558  -9.657  1.00 50.40  ? 66  ARG C NH2 1 
ATOM 3929 N N   . ALA C 1 67  ? -63.963 18.460  -8.333  1.00 63.96  ? 67  ALA C N   1 
ATOM 3930 C CA  . ALA C 1 67  ? -63.156 17.368  -8.853  1.00 63.44  ? 67  ALA C CA  1 
ATOM 3931 C C   . ALA C 1 67  ? -63.987 16.101  -8.985  1.00 56.07  ? 67  ALA C C   1 
ATOM 3932 O O   . ALA C 1 67  ? -64.870 15.832  -8.163  1.00 54.61  ? 67  ALA C O   1 
ATOM 3933 C CB  . ALA C 1 67  ? -61.944 17.096  -7.961  1.00 59.11  ? 67  ALA C CB  1 
ATOM 3934 N N   . THR C 1 68  ? -63.698 15.330  -10.029 1.00 58.24  ? 68  THR C N   1 
ATOM 3935 C CA  . THR C 1 68  ? -64.294 14.015  -10.226 1.00 58.79  ? 68  THR C CA  1 
ATOM 3936 C C   . THR C 1 68  ? -63.228 13.097  -10.795 1.00 59.04  ? 68  THR C C   1 
ATOM 3937 O O   . THR C 1 68  ? -62.712 13.345  -11.889 1.00 52.94  ? 68  THR C O   1 
ATOM 3938 C CB  . THR C 1 68  ? -65.504 14.071  -11.164 1.00 59.59  ? 68  THR C CB  1 
ATOM 3939 O OG1 . THR C 1 68  ? -66.551 14.840  -10.557 1.00 63.37  ? 68  THR C OG1 1 
ATOM 3940 C CG2 . THR C 1 68  ? -66.010 12.669  -11.446 1.00 58.06  ? 68  THR C CG2 1 
ATOM 3941 N N   . LEU C 1 69  ? -62.893 12.050  -10.054 1.00 63.45  ? 69  LEU C N   1 
ATOM 3942 C CA  . LEU C 1 69  ? -61.904 11.079  -10.488 1.00 64.29  ? 69  LEU C CA  1 
ATOM 3943 C C   . LEU C 1 69  ? -62.590 9.851   -11.069 1.00 60.78  ? 69  LEU C C   1 
ATOM 3944 O O   . LEU C 1 69  ? -63.687 9.472   -10.651 1.00 58.21  ? 69  LEU C O   1 
ATOM 3945 C CB  . LEU C 1 69  ? -60.991 10.670  -9.333  1.00 62.53  ? 69  LEU C CB  1 
ATOM 3946 C CG  . LEU C 1 69  ? -59.654 11.406  -9.314  1.00 60.00  ? 69  LEU C CG  1 
ATOM 3947 C CD1 . LEU C 1 69  ? -58.880 11.083  -8.051  1.00 61.63  ? 69  LEU C CD1 1 
ATOM 3948 C CD2 . LEU C 1 69  ? -58.867 11.016  -10.539 1.00 64.47  ? 69  LEU C CD2 1 
ATOM 3949 N N   . SER C 1 70  ? -61.929 9.230   -12.040 1.00 56.15  ? 70  SER C N   1 
ATOM 3950 C CA  . SER C 1 70  ? -62.519 8.104   -12.743 1.00 58.20  ? 70  SER C CA  1 
ATOM 3951 C C   . SER C 1 70  ? -61.417 7.221   -13.305 1.00 57.71  ? 70  SER C C   1 
ATOM 3952 O O   . SER C 1 70  ? -60.268 7.645   -13.457 1.00 56.55  ? 70  SER C O   1 
ATOM 3953 C CB  . SER C 1 70  ? -63.448 8.578   -13.859 1.00 60.98  ? 70  SER C CB  1 
ATOM 3954 O OG  . SER C 1 70  ? -62.749 9.401   -14.778 1.00 60.71  ? 70  SER C OG  1 
ATOM 3955 N N   . ILE C 1 71  ? -61.787 5.983   -13.622 1.00 57.00  ? 71  ILE C N   1 
ATOM 3956 C CA  . ILE C 1 71  ? -60.845 4.982   -14.102 1.00 66.00  ? 71  ILE C CA  1 
ATOM 3957 C C   . ILE C 1 71  ? -61.543 4.100   -15.131 1.00 71.81  ? 71  ILE C C   1 
ATOM 3958 O O   . ILE C 1 71  ? -62.654 3.613   -14.894 1.00 66.56  ? 71  ILE C O   1 
ATOM 3959 C CB  . ILE C 1 71  ? -60.268 4.143   -12.940 1.00 61.56  ? 71  ILE C CB  1 
ATOM 3960 C CG1 . ILE C 1 71  ? -59.166 3.203   -13.434 1.00 63.46  ? 71  ILE C CG1 1 
ATOM 3961 C CG2 . ILE C 1 71  ? -61.362 3.395   -12.185 1.00 65.60  ? 71  ILE C CG2 1 
ATOM 3962 C CD1 . ILE C 1 71  ? -58.440 2.497   -12.309 1.00 83.77  ? 71  ILE C CD1 1 
ATOM 3963 N N   . ASP C 1 72  ? -60.907 3.924   -16.285 1.00 66.95  ? 72  ASP C N   1 
ATOM 3964 C CA  . ASP C 1 72  ? -61.362 2.989   -17.307 1.00 65.37  ? 72  ASP C CA  1 
ATOM 3965 C C   . ASP C 1 72  ? -60.385 1.823   -17.317 1.00 70.32  ? 72  ASP C C   1 
ATOM 3966 O O   . ASP C 1 72  ? -59.233 1.974   -17.740 1.00 68.72  ? 72  ASP C O   1 
ATOM 3967 C CB  . ASP C 1 72  ? -61.446 3.654   -18.678 1.00 74.00  ? 72  ASP C CB  1 
ATOM 3968 C CG  . ASP C 1 72  ? -61.980 2.717   -19.747 1.00 79.97  ? 72  ASP C CG  1 
ATOM 3969 O OD1 . ASP C 1 72  ? -62.506 1.638   -19.395 1.00 76.45  ? 72  ASP C OD1 1 
ATOM 3970 O OD2 . ASP C 1 72  ? -61.872 3.056   -20.944 1.00 77.13  ? 72  ASP C OD2 1 
ATOM 3971 N N   . THR C 1 73  ? -60.848 0.661   -16.856 1.00 76.62  ? 73  THR C N   1 
ATOM 3972 C CA  . THR C 1 73  ? -59.966 -0.490  -16.709 1.00 75.28  ? 73  THR C CA  1 
ATOM 3973 C C   . THR C 1 73  ? -59.676 -1.169  -18.040 1.00 79.02  ? 73  THR C C   1 
ATOM 3974 O O   . THR C 1 73  ? -58.616 -1.786  -18.197 1.00 83.33  ? 73  THR C O   1 
ATOM 3975 C CB  . THR C 1 73  ? -60.584 -1.499  -15.744 1.00 78.34  ? 73  THR C CB  1 
ATOM 3976 O OG1 . THR C 1 73  ? -61.908 -1.823  -16.181 1.00 79.69  ? 73  THR C OG1 1 
ATOM 3977 C CG2 . THR C 1 73  ? -60.678 -0.894  -14.363 1.00 84.17  ? 73  THR C CG2 1 
ATOM 3978 N N   . SER C 1 74  ? -60.600 -1.073  -19.000 1.00 75.91  ? 74  SER C N   1 
ATOM 3979 C CA  . SER C 1 74  ? -60.414 -1.749  -20.280 1.00 73.85  ? 74  SER C CA  1 
ATOM 3980 C C   . SER C 1 74  ? -59.247 -1.153  -21.057 1.00 73.72  ? 74  SER C C   1 
ATOM 3981 O O   . SER C 1 74  ? -58.420 -1.889  -21.609 1.00 70.80  ? 74  SER C O   1 
ATOM 3982 C CB  . SER C 1 74  ? -61.701 -1.680  -21.103 1.00 75.25  ? 74  SER C CB  1 
ATOM 3983 O OG  . SER C 1 74  ? -62.835 -1.969  -20.304 1.00 78.78  ? 74  SER C OG  1 
ATOM 3984 N N   . LYS C 1 75  ? -59.161 0.173   -21.112 1.00 74.68  ? 75  LYS C N   1 
ATOM 3985 C CA  . LYS C 1 75  ? -58.069 0.848   -21.801 1.00 74.28  ? 75  LYS C CA  1 
ATOM 3986 C C   . LYS C 1 75  ? -56.893 1.159   -20.885 1.00 76.43  ? 75  LYS C C   1 
ATOM 3987 O O   . LYS C 1 75  ? -55.927 1.783   -21.335 1.00 75.74  ? 75  LYS C O   1 
ATOM 3988 C CB  . LYS C 1 75  ? -58.576 2.140   -22.450 1.00 70.79  ? 75  LYS C CB  1 
ATOM 3989 C CG  . LYS C 1 75  ? -59.687 1.923   -23.465 1.00 68.92  ? 75  LYS C CG  1 
ATOM 3990 C CD  . LYS C 1 75  ? -60.114 3.231   -24.108 1.00 63.44  ? 75  LYS C CD  1 
ATOM 3991 C CE  . LYS C 1 75  ? -61.377 3.048   -24.933 1.00 63.89  ? 75  LYS C CE  1 
ATOM 3992 N NZ  . LYS C 1 75  ? -62.550 2.712   -24.082 1.00 58.76  ? 75  LYS C NZ  1 
ATOM 3993 N N   . LYS C 1 76  ? -56.951 0.731   -19.624 1.00 78.38  ? 76  LYS C N   1 
ATOM 3994 C CA  . LYS C 1 76  ? -55.898 0.970   -18.638 1.00 78.68  ? 76  LYS C CA  1 
ATOM 3995 C C   . LYS C 1 76  ? -55.587 2.464   -18.527 1.00 80.32  ? 76  LYS C C   1 
ATOM 3996 O O   . LYS C 1 76  ? -54.469 2.922   -18.771 1.00 81.81  ? 76  LYS C O   1 
ATOM 3997 C CB  . LYS C 1 76  ? -54.644 0.157   -18.971 1.00 81.35  ? 76  LYS C CB  1 
ATOM 3998 C CG  . LYS C 1 76  ? -54.781 -1.320  -18.639 1.00 84.68  ? 76  LYS C CG  1 
ATOM 3999 C CD  . LYS C 1 76  ? -53.949 -2.194  -19.563 1.00 82.27  ? 76  LYS C CD  1 
ATOM 4000 C CE  . LYS C 1 76  ? -52.483 -1.802  -19.541 1.00 80.49  ? 76  LYS C CE  1 
ATOM 4001 N NZ  . LYS C 1 76  ? -51.688 -2.641  -20.481 1.00 81.69  ? 76  LYS C NZ  1 
ATOM 4002 N N   . GLN C 1 77  ? -56.615 3.222   -18.147 1.00 73.75  ? 77  GLN C N   1 
ATOM 4003 C CA  . GLN C 1 77  ? -56.524 4.671   -18.066 1.00 68.90  ? 77  GLN C CA  1 
ATOM 4004 C C   . GLN C 1 77  ? -57.282 5.168   -16.843 1.00 64.95  ? 77  GLN C C   1 
ATOM 4005 O O   . GLN C 1 77  ? -58.158 4.485   -16.308 1.00 66.30  ? 77  GLN C O   1 
ATOM 4006 C CB  . GLN C 1 77  ? -57.088 5.351   -19.324 1.00 65.52  ? 77  GLN C CB  1 
ATOM 4007 C CG  . GLN C 1 77  ? -56.243 5.197   -20.581 1.00 67.72  ? 77  GLN C CG  1 
ATOM 4008 C CD  . GLN C 1 77  ? -56.946 5.730   -21.818 1.00 60.91  ? 77  GLN C CD  1 
ATOM 4009 O OE1 . GLN C 1 77  ? -58.045 6.278   -21.732 1.00 55.52  ? 77  GLN C OE1 1 
ATOM 4010 N NE2 . GLN C 1 77  ? -56.316 5.569   -22.977 1.00 59.07  ? 77  GLN C NE2 1 
ATOM 4011 N N   . PHE C 1 78  ? -56.929 6.376   -16.408 1.00 60.70  ? 78  PHE C N   1 
ATOM 4012 C CA  . PHE C 1 78  ? -57.681 7.093   -15.389 1.00 56.93  ? 78  PHE C CA  1 
ATOM 4013 C C   . PHE C 1 78  ? -57.652 8.574   -15.730 1.00 62.22  ? 78  PHE C C   1 
ATOM 4014 O O   . PHE C 1 78  ? -56.699 9.066   -16.341 1.00 62.38  ? 78  PHE C O   1 
ATOM 4015 C CB  . PHE C 1 78  ? -57.136 6.859   -13.968 1.00 58.97  ? 78  PHE C CB  1 
ATOM 4016 C CG  . PHE C 1 78  ? -55.645 7.036   -13.832 1.00 56.83  ? 78  PHE C CG  1 
ATOM 4017 C CD1 . PHE C 1 78  ? -54.766 6.051   -14.250 1.00 62.39  ? 78  PHE C CD1 1 
ATOM 4018 C CD2 . PHE C 1 78  ? -55.129 8.175   -13.239 1.00 57.60  ? 78  PHE C CD2 1 
ATOM 4019 C CE1 . PHE C 1 78  ? -53.402 6.217   -14.111 1.00 61.54  ? 78  PHE C CE1 1 
ATOM 4020 C CE2 . PHE C 1 78  ? -53.768 8.341   -13.091 1.00 61.54  ? 78  PHE C CE2 1 
ATOM 4021 C CZ  . PHE C 1 78  ? -52.903 7.358   -13.522 1.00 65.47  ? 78  PHE C CZ  1 
ATOM 4022 N N   . SER C 1 79  ? -58.708 9.283   -15.335 1.00 61.39  ? 79  SER C N   1 
ATOM 4023 C CA  . SER C 1 79  ? -58.902 10.658  -15.769 1.00 59.00  ? 79  SER C CA  1 
ATOM 4024 C C   . SER C 1 79  ? -59.380 11.515  -14.605 1.00 61.31  ? 79  SER C C   1 
ATOM 4025 O O   . SER C 1 79  ? -59.818 11.014  -13.565 1.00 59.50  ? 79  SER C O   1 
ATOM 4026 C CB  . SER C 1 79  ? -59.896 10.738  -16.935 1.00 52.58  ? 79  SER C CB  1 
ATOM 4027 O OG  . SER C 1 79  ? -59.490 9.908   -18.009 1.00 53.82  ? 79  SER C OG  1 
ATOM 4028 N N   . LEU C 1 80  ? -59.301 12.831  -14.807 1.00 63.22  ? 80  LEU C N   1 
ATOM 4029 C CA  . LEU C 1 80  ? -59.655 13.829  -13.808 1.00 56.59  ? 80  LEU C CA  1 
ATOM 4030 C C   . LEU C 1 80  ? -60.463 14.932  -14.474 1.00 53.85  ? 80  LEU C C   1 
ATOM 4031 O O   . LEU C 1 80  ? -60.152 15.341  -15.596 1.00 50.85  ? 80  LEU C O   1 
ATOM 4032 C CB  . LEU C 1 80  ? -58.397 14.419  -13.152 1.00 61.22  ? 80  LEU C CB  1 
ATOM 4033 C CG  . LEU C 1 80  ? -58.545 15.640  -12.242 1.00 57.40  ? 80  LEU C CG  1 
ATOM 4034 C CD1 . LEU C 1 80  ? -59.085 15.249  -10.876 1.00 60.26  ? 80  LEU C CD1 1 
ATOM 4035 C CD2 . LEU C 1 80  ? -57.214 16.364  -12.107 1.00 51.34  ? 80  LEU C CD2 1 
ATOM 4036 N N   . ARG C 1 81  ? -61.501 15.410  -13.787 1.00 57.30  ? 81  ARG C N   1 
ATOM 4037 C CA  . ARG C 1 81  ? -62.304 16.523  -14.282 1.00 58.61  ? 81  ARG C CA  1 
ATOM 4038 C C   . ARG C 1 81  ? -62.393 17.593  -13.205 1.00 61.07  ? 81  ARG C C   1 
ATOM 4039 O O   . ARG C 1 81  ? -62.801 17.305  -12.075 1.00 63.17  ? 81  ARG C O   1 
ATOM 4040 C CB  . ARG C 1 81  ? -63.704 16.070  -14.703 1.00 56.66  ? 81  ARG C CB  1 
ATOM 4041 C CG  . ARG C 1 81  ? -63.940 16.137  -16.206 1.00 69.06  ? 81  ARG C CG  1 
ATOM 4042 C CD  . ARG C 1 81  ? -65.413 16.013  -16.534 1.00 69.60  ? 81  ARG C CD  1 
ATOM 4043 N NE  . ARG C 1 81  ? -66.180 17.074  -15.891 1.00 68.79  ? 81  ARG C NE  1 
ATOM 4044 C CZ  . ARG C 1 81  ? -67.487 17.247  -16.027 1.00 68.45  ? 81  ARG C CZ  1 
ATOM 4045 N NH1 . ARG C 1 81  ? -68.216 16.437  -16.778 1.00 68.89  ? 81  ARG C NH1 1 
ATOM 4046 N NH2 . ARG C 1 81  ? -68.077 18.256  -15.392 1.00 58.31  ? 81  ARG C NH2 1 
ATOM 4047 N N   . LEU C 1 82  ? -62.016 18.824  -13.554 1.00 58.27  ? 82  LEU C N   1 
ATOM 4048 C CA  . LEU C 1 82  ? -62.052 19.959  -12.636 1.00 56.86  ? 82  LEU C CA  1 
ATOM 4049 C C   . LEU C 1 82  ? -62.964 21.032  -13.215 1.00 54.82  ? 82  LEU C C   1 
ATOM 4050 O O   . LEU C 1 82  ? -62.633 21.653  -14.230 1.00 58.44  ? 82  LEU C O   1 
ATOM 4051 C CB  . LEU C 1 82  ? -60.652 20.517  -12.387 1.00 53.69  ? 82  LEU C CB  1 
ATOM 4052 C CG  . LEU C 1 82  ? -60.429 21.215  -11.043 1.00 50.25  ? 82  LEU C CG  1 
ATOM 4053 C CD1 . LEU C 1 82  ? -60.820 20.305  -9.888  1.00 49.96  ? 82  LEU C CD1 1 
ATOM 4054 C CD2 . LEU C 1 82  ? -58.987 21.681  -10.903 1.00 50.44  ? 82  LEU C CD2 1 
ATOM 4055 N N   . THR C 1 83  ? -64.099 21.259  -12.562 1.00 52.94  ? 83  THR C N   1 
ATOM 4056 C CA  . THR C 1 83  ? -65.029 22.284  -13.002 1.00 55.40  ? 83  THR C CA  1 
ATOM 4057 C C   . THR C 1 83  ? -64.611 23.657  -12.483 1.00 60.82  ? 83  THR C C   1 
ATOM 4058 O O   . THR C 1 83  ? -63.916 23.787  -11.471 1.00 58.31  ? 83  THR C O   1 
ATOM 4059 C CB  . THR C 1 83  ? -66.445 21.971  -12.527 1.00 50.73  ? 83  THR C CB  1 
ATOM 4060 O OG1 . THR C 1 83  ? -66.594 22.391  -11.164 1.00 60.20  ? 83  THR C OG1 1 
ATOM 4061 C CG2 . THR C 1 83  ? -66.729 20.484  -12.631 1.00 54.14  ? 83  THR C CG2 1 
ATOM 4062 N N   . SER C 1 84  ? -65.054 24.690  -13.202 1.00 57.93  ? 84  SER C N   1 
ATOM 4063 C CA  . SER C 1 84  ? -64.912 26.080  -12.770 1.00 56.65  ? 84  SER C CA  1 
ATOM 4064 C C   . SER C 1 84  ? -63.449 26.435  -12.509 1.00 54.52  ? 84  SER C C   1 
ATOM 4065 O O   . SER C 1 84  ? -63.099 27.000  -11.471 1.00 57.45  ? 84  SER C O   1 
ATOM 4066 C CB  . SER C 1 84  ? -65.774 26.349  -11.536 1.00 58.63  ? 84  SER C CB  1 
ATOM 4067 O OG  . SER C 1 84  ? -67.142 26.096  -11.808 1.00 63.76  ? 84  SER C OG  1 
ATOM 4068 N N   . VAL C 1 85  ? -62.587 26.094  -13.470 1.00 51.70  ? 85  VAL C N   1 
ATOM 4069 C CA  . VAL C 1 85  ? -61.168 26.383  -13.319 1.00 51.24  ? 85  VAL C CA  1 
ATOM 4070 C C   . VAL C 1 85  ? -60.947 27.888  -13.265 1.00 54.98  ? 85  VAL C C   1 
ATOM 4071 O O   . VAL C 1 85  ? -61.569 28.662  -14.005 1.00 56.75  ? 85  VAL C O   1 
ATOM 4072 C CB  . VAL C 1 85  ? -60.352 25.736  -14.452 1.00 51.42  ? 85  VAL C CB  1 
ATOM 4073 C CG1 . VAL C 1 85  ? -60.519 24.226  -14.430 1.00 56.30  ? 85  VAL C CG1 1 
ATOM 4074 C CG2 . VAL C 1 85  ? -60.760 26.290  -15.809 1.00 57.59  ? 85  VAL C CG2 1 
ATOM 4075 N N   . THR C 1 86  ? -60.080 28.309  -12.354 1.00 55.58  ? 86  THR C N   1 
ATOM 4076 C CA  . THR C 1 86  ? -59.650 29.693  -12.228 1.00 53.77  ? 86  THR C CA  1 
ATOM 4077 C C   . THR C 1 86  ? -58.155 29.774  -12.519 1.00 53.23  ? 86  THR C C   1 
ATOM 4078 O O   . THR C 1 86  ? -57.505 28.771  -12.826 1.00 57.08  ? 86  THR C O   1 
ATOM 4079 C CB  . THR C 1 86  ? -59.969 30.247  -10.835 1.00 54.22  ? 86  THR C CB  1 
ATOM 4080 O OG1 . THR C 1 86  ? -59.021 29.742  -9.887  1.00 58.54  ? 86  THR C OG1 1 
ATOM 4081 C CG2 . THR C 1 86  ? -61.373 29.844  -10.408 1.00 58.13  ? 86  THR C CG2 1 
ATOM 4082 N N   . ALA C 1 87  ? -57.608 30.989  -12.424 1.00 52.42  ? 87  ALA C N   1 
ATOM 4083 C CA  . ALA C 1 87  ? -56.178 31.176  -12.635 1.00 52.64  ? 87  ALA C CA  1 
ATOM 4084 C C   . ALA C 1 87  ? -55.346 30.435  -11.603 1.00 52.39  ? 87  ALA C C   1 
ATOM 4085 O O   . ALA C 1 87  ? -54.155 30.200  -11.834 1.00 52.68  ? 87  ALA C O   1 
ATOM 4086 C CB  . ALA C 1 87  ? -55.829 32.664  -12.605 1.00 53.06  ? 87  ALA C CB  1 
ATOM 4087 N N   . ALA C 1 88  ? -55.943 30.072  -10.466 1.00 55.49  ? 88  ALA C N   1 
ATOM 4088 C CA  . ALA C 1 88  ? -55.202 29.340  -9.447  1.00 55.75  ? 88  ALA C CA  1 
ATOM 4089 C C   . ALA C 1 88  ? -54.812 27.954  -9.943  1.00 54.96  ? 88  ALA C C   1 
ATOM 4090 O O   . ALA C 1 88  ? -53.708 27.474  -9.662  1.00 54.20  ? 88  ALA C O   1 
ATOM 4091 C CB  . ALA C 1 88  ? -56.033 29.246  -8.167  1.00 55.44  ? 88  ALA C CB  1 
ATOM 4092 N N   . ASP C 1 89  ? -55.693 27.307  -10.710 1.00 57.11  ? 89  ASP C N   1 
ATOM 4093 C CA  . ASP C 1 89  ? -55.440 25.948  -11.172 1.00 51.42  ? 89  ASP C CA  1 
ATOM 4094 C C   . ASP C 1 89  ? -54.384 25.874  -12.268 1.00 51.65  ? 89  ASP C C   1 
ATOM 4095 O O   . ASP C 1 89  ? -53.976 24.766  -12.631 1.00 51.56  ? 89  ASP C O   1 
ATOM 4096 C CB  . ASP C 1 89  ? -56.740 25.316  -11.665 1.00 51.24  ? 89  ASP C CB  1 
ATOM 4097 C CG  . ASP C 1 89  ? -57.870 25.469  -10.673 1.00 51.01  ? 89  ASP C CG  1 
ATOM 4098 O OD1 . ASP C 1 89  ? -57.713 25.025  -9.516  1.00 51.02  ? 89  ASP C OD1 1 
ATOM 4099 O OD2 . ASP C 1 89  ? -58.916 26.037  -11.047 1.00 51.04  ? 89  ASP C OD2 1 
ATOM 4100 N N   . MET C 1 90  ? -53.937 27.009  -12.804 1.00 51.96  ? 90  MET C N   1 
ATOM 4101 C CA  . MET C 1 90  ? -52.853 27.009  -13.777 1.00 52.18  ? 90  MET C CA  1 
ATOM 4102 C C   . MET C 1 90  ? -51.588 26.446  -13.142 1.00 53.83  ? 90  MET C C   1 
ATOM 4103 O O   . MET C 1 90  ? -51.000 27.077  -12.258 1.00 56.59  ? 90  MET C O   1 
ATOM 4104 C CB  . MET C 1 90  ? -52.600 28.419  -14.315 1.00 55.29  ? 90  MET C CB  1 
ATOM 4105 C CG  . MET C 1 90  ? -51.383 28.521  -15.222 1.00 59.56  ? 90  MET C CG  1 
ATOM 4106 S SD  . MET C 1 90  ? -51.234 30.128  -16.024 1.00 71.01  ? 90  MET C SD  1 
ATOM 4107 C CE  . MET C 1 90  ? -49.660 29.939  -16.856 1.00 67.81  ? 90  MET C CE  1 
ATOM 4108 N N   . ALA C 1 91  ? -51.165 25.266  -13.586 1.00 52.00  ? 91  ALA C N   1 
ATOM 4109 C CA  . ALA C 1 91  ? -50.061 24.555  -12.955 1.00 51.92  ? 91  ALA C CA  1 
ATOM 4110 C C   . ALA C 1 91  ? -49.641 23.409  -13.865 1.00 52.22  ? 91  ALA C C   1 
ATOM 4111 O O   . ALA C 1 91  ? -50.267 23.143  -14.894 1.00 51.94  ? 91  ALA C O   1 
ATOM 4112 C CB  . ALA C 1 91  ? -50.457 24.033  -11.573 1.00 52.31  ? 91  ALA C CB  1 
ATOM 4113 N N   . THR C 1 92  ? -48.564 22.734  -13.469 1.00 51.87  ? 92  THR C N   1 
ATOM 4114 C CA  . THR C 1 92  ? -48.139 21.499  -14.112 1.00 51.84  ? 92  THR C CA  1 
ATOM 4115 C C   . THR C 1 92  ? -48.744 20.317  -13.365 1.00 54.19  ? 92  THR C C   1 
ATOM 4116 O O   . THR C 1 92  ? -48.587 20.201  -12.147 1.00 57.63  ? 92  THR C O   1 
ATOM 4117 C CB  . THR C 1 92  ? -46.613 21.385  -14.137 1.00 51.95  ? 92  THR C CB  1 
ATOM 4118 O OG1 . THR C 1 92  ? -46.054 22.545  -14.766 1.00 52.16  ? 92  THR C OG1 1 
ATOM 4119 C CG2 . THR C 1 92  ? -46.178 20.139  -14.896 1.00 51.95  ? 92  THR C CG2 1 
ATOM 4120 N N   . TYR C 1 93  ? -49.438 19.450  -14.095 1.00 51.58  ? 93  TYR C N   1 
ATOM 4121 C CA  . TYR C 1 93  ? -50.161 18.331  -13.508 1.00 51.41  ? 93  TYR C CA  1 
ATOM 4122 C C   . TYR C 1 93  ? -49.431 17.025  -13.783 1.00 54.40  ? 93  TYR C C   1 
ATOM 4123 O O   . TYR C 1 93  ? -48.842 16.846  -14.852 1.00 56.61  ? 93  TYR C O   1 
ATOM 4124 C CB  . TYR C 1 93  ? -51.587 18.255  -14.059 1.00 51.35  ? 93  TYR C CB  1 
ATOM 4125 C CG  . TYR C 1 93  ? -52.525 19.302  -13.501 1.00 51.25  ? 93  TYR C CG  1 
ATOM 4126 C CD1 . TYR C 1 93  ? -52.442 20.629  -13.905 1.00 51.39  ? 93  TYR C CD1 1 
ATOM 4127 C CD2 . TYR C 1 93  ? -53.501 18.961  -12.573 1.00 51.03  ? 93  TYR C CD2 1 
ATOM 4128 C CE1 . TYR C 1 93  ? -53.302 21.586  -13.397 1.00 51.34  ? 93  TYR C CE1 1 
ATOM 4129 C CE2 . TYR C 1 93  ? -54.364 19.910  -12.061 1.00 50.94  ? 93  TYR C CE2 1 
ATOM 4130 C CZ  . TYR C 1 93  ? -54.261 21.220  -12.476 1.00 51.10  ? 93  TYR C CZ  1 
ATOM 4131 O OH  . TYR C 1 93  ? -55.122 22.162  -11.965 1.00 51.04  ? 93  TYR C OH  1 
ATOM 4132 N N   . TYR C 1 94  ? -49.481 16.112  -12.815 1.00 58.93  ? 94  TYR C N   1 
ATOM 4133 C CA  . TYR C 1 94  ? -48.835 14.812  -12.919 1.00 57.83  ? 94  TYR C CA  1 
ATOM 4134 C C   . TYR C 1 94  ? -49.822 13.733  -12.494 1.00 57.85  ? 94  TYR C C   1 
ATOM 4135 O O   . TYR C 1 94  ? -50.616 13.941  -11.570 1.00 56.43  ? 94  TYR C O   1 
ATOM 4136 C CB  . TYR C 1 94  ? -47.594 14.723  -12.018 1.00 56.68  ? 94  TYR C CB  1 
ATOM 4137 C CG  . TYR C 1 94  ? -46.527 15.774  -12.248 1.00 56.64  ? 94  TYR C CG  1 
ATOM 4138 C CD1 . TYR C 1 94  ? -45.538 15.602  -13.211 1.00 61.39  ? 94  TYR C CD1 1 
ATOM 4139 C CD2 . TYR C 1 94  ? -46.489 16.926  -11.472 1.00 54.82  ? 94  TYR C CD2 1 
ATOM 4140 C CE1 . TYR C 1 94  ? -44.554 16.561  -13.404 1.00 63.77  ? 94  TYR C CE1 1 
ATOM 4141 C CE2 . TYR C 1 94  ? -45.512 17.887  -11.657 1.00 54.61  ? 94  TYR C CE2 1 
ATOM 4142 C CZ  . TYR C 1 94  ? -44.547 17.700  -12.624 1.00 58.60  ? 94  TYR C CZ  1 
ATOM 4143 O OH  . TYR C 1 94  ? -43.573 18.656  -12.809 1.00 55.32  ? 94  TYR C OH  1 
ATOM 4144 N N   . CYS C 1 95  ? -49.771 12.582  -13.161 1.00 58.86  ? 95  CYS C N   1 
ATOM 4145 C CA  . CYS C 1 95  ? -50.391 11.368  -12.646 1.00 55.21  ? 95  CYS C CA  1 
ATOM 4146 C C   . CYS C 1 95  ? -49.298 10.450  -12.118 1.00 55.57  ? 95  CYS C C   1 
ATOM 4147 O O   . CYS C 1 95  ? -48.192 10.406  -12.661 1.00 57.98  ? 95  CYS C O   1 
ATOM 4148 C CB  . CYS C 1 95  ? -51.237 10.637  -13.704 1.00 56.78  ? 95  CYS C CB  1 
ATOM 4149 S SG  . CYS C 1 95  ? -50.451 10.372  -15.304 1.00 77.63  ? 95  CYS C SG  1 
ATOM 4150 N N   . ALA C 1 96  ? -49.608 9.730   -11.039 1.00 56.74  ? 96  ALA C N   1 
ATOM 4151 C CA  . ALA C 1 96  ? -48.605 8.932   -10.349 1.00 60.28  ? 96  ALA C CA  1 
ATOM 4152 C C   . ALA C 1 96  ? -49.194 7.603   -9.902  1.00 59.61  ? 96  ALA C C   1 
ATOM 4153 O O   . ALA C 1 96  ? -50.406 7.464   -9.707  1.00 56.45  ? 96  ALA C O   1 
ATOM 4154 C CB  . ALA C 1 96  ? -48.026 9.679   -9.141  1.00 60.27  ? 96  ALA C CB  1 
ATOM 4155 N N   . ARG C 1 97  ? -48.305 6.622   -9.735  1.00 58.45  ? 97  ARG C N   1 
ATOM 4156 C CA  . ARG C 1 97  ? -48.664 5.284   -9.280  1.00 66.76  ? 97  ARG C CA  1 
ATOM 4157 C C   . ARG C 1 97  ? -48.276 5.140   -7.815  1.00 64.90  ? 97  ARG C C   1 
ATOM 4158 O O   . ARG C 1 97  ? -47.088 5.151   -7.482  1.00 61.35  ? 97  ARG C O   1 
ATOM 4159 C CB  . ARG C 1 97  ? -47.956 4.219   -10.110 1.00 69.55  ? 97  ARG C CB  1 
ATOM 4160 C CG  . ARG C 1 97  ? -48.402 2.798   -9.795  1.00 65.58  ? 97  ARG C CG  1 
ATOM 4161 C CD  . ARG C 1 97  ? -47.743 1.784   -10.713 1.00 65.44  ? 97  ARG C CD  1 
ATOM 4162 N NE  . ARG C 1 97  ? -46.329 1.637   -10.381 1.00 61.17  ? 97  ARG C NE  1 
ATOM 4163 C CZ  . ARG C 1 97  ? -45.562 0.629   -10.773 1.00 65.68  ? 97  ARG C CZ  1 
ATOM 4164 N NH1 . ARG C 1 97  ? -46.048 -0.374  -11.483 1.00 70.22  ? 97  ARG C NH1 1 
ATOM 4165 N NH2 . ARG C 1 97  ? -44.276 0.623   -10.436 1.00 67.45  ? 97  ARG C NH2 1 
ATOM 4166 N N   . TRP C 1 98  ? -49.264 4.992   -6.942  1.00 70.55  ? 98  TRP C N   1 
ATOM 4167 C CA  . TRP C 1 98  ? -48.979 4.676   -5.552  1.00 71.47  ? 98  TRP C CA  1 
ATOM 4168 C C   . TRP C 1 98  ? -48.618 3.201   -5.437  1.00 72.61  ? 98  TRP C C   1 
ATOM 4169 O O   . TRP C 1 98  ? -49.193 2.353   -6.125  1.00 74.39  ? 98  TRP C O   1 
ATOM 4170 C CB  . TRP C 1 98  ? -50.190 4.966   -4.671  1.00 71.70  ? 98  TRP C CB  1 
ATOM 4171 C CG  . TRP C 1 98  ? -50.202 6.285   -3.978  1.00 74.84  ? 98  TRP C CG  1 
ATOM 4172 C CD1 . TRP C 1 98  ? -51.113 7.271   -4.153  1.00 76.13  ? 98  TRP C CD1 1 
ATOM 4173 C CD2 . TRP C 1 98  ? -49.282 6.759   -2.986  1.00 73.92  ? 98  TRP C CD2 1 
ATOM 4174 N NE1 . TRP C 1 98  ? -50.823 8.341   -3.344  1.00 77.75  ? 98  TRP C NE1 1 
ATOM 4175 C CE2 . TRP C 1 98  ? -49.701 8.052   -2.616  1.00 73.86  ? 98  TRP C CE2 1 
ATOM 4176 C CE3 . TRP C 1 98  ? -48.144 6.220   -2.380  1.00 70.27  ? 98  TRP C CE3 1 
ATOM 4177 C CZ2 . TRP C 1 98  ? -49.026 8.813   -1.671  1.00 72.74  ? 98  TRP C CZ2 1 
ATOM 4178 C CZ3 . TRP C 1 98  ? -47.477 6.981   -1.439  1.00 72.97  ? 98  TRP C CZ3 1 
ATOM 4179 C CH2 . TRP C 1 98  ? -47.917 8.262   -1.097  1.00 77.80  ? 98  TRP C CH2 1 
ATOM 4180 N N   . ARG C 1 99  ? -47.664 2.892   -4.565  1.00 67.76  ? 99  ARG C N   1 
ATOM 4181 C CA  . ARG C 1 99  ? -47.322 1.512   -4.246  1.00 56.80  ? 99  ARG C CA  1 
ATOM 4182 C C   . ARG C 1 99  ? -47.783 1.211   -2.829  1.00 56.21  ? 99  ARG C C   1 
ATOM 4183 O O   . ARG C 1 99  ? -47.521 1.991   -1.907  1.00 65.14  ? 99  ARG C O   1 
ATOM 4184 C CB  . ARG C 1 99  ? -45.825 1.254   -4.397  1.00 56.52  ? 99  ARG C CB  1 
ATOM 4185 C CG  . ARG C 1 99  ? -45.451 0.726   -5.771  1.00 58.52  ? 99  ARG C CG  1 
ATOM 4186 C CD  . ARG C 1 99  ? -45.627 -0.783  -5.874  1.00 62.30  ? 99  ARG C CD  1 
ATOM 4187 N NE  . ARG C 1 99  ? -44.403 -1.507  -5.558  1.00 63.81  ? 99  ARG C NE  1 
ATOM 4188 C CZ  . ARG C 1 99  ? -43.500 -1.875  -6.456  1.00 63.00  ? 99  ARG C CZ  1 
ATOM 4189 N NH1 . ARG C 1 99  ? -43.645 -1.587  -7.739  1.00 65.09  ? 99  ARG C NH1 1 
ATOM 4190 N NH2 . ARG C 1 99  ? -42.423 -2.546  -6.057  1.00 63.62  ? 99  ARG C NH2 1 
ATOM 4191 N N   . LEU C 1 100 ? -48.463 0.082   -2.657  1.00 58.74  ? 100 LEU C N   1 
ATOM 4192 C CA  . LEU C 1 100 ? -49.241 -0.168  -1.456  1.00 57.87  ? 100 LEU C CA  1 
ATOM 4193 C C   . LEU C 1 100 ? -48.893 -1.520  -0.853  1.00 61.40  ? 100 LEU C C   1 
ATOM 4194 O O   . LEU C 1 100 ? -48.493 -2.453  -1.553  1.00 61.04  ? 100 LEU C O   1 
ATOM 4195 C CB  . LEU C 1 100 ? -50.740 -0.105  -1.767  1.00 57.48  ? 100 LEU C CB  1 
ATOM 4196 C CG  . LEU C 1 100 ? -51.328 1.302   -1.704  1.00 62.64  ? 100 LEU C CG  1 
ATOM 4197 C CD1 . LEU C 1 100 ? -51.166 1.992   -3.041  1.00 63.97  ? 100 LEU C CD1 1 
ATOM 4198 C CD2 . LEU C 1 100 ? -52.781 1.255   -1.322  1.00 65.73  ? 100 LEU C CD2 1 
ATOM 4199 N N   . MET C 1 101 ? -49.059 -1.611  0.464   1.00 60.15  ? 101 MET C N   1 
ATOM 4200 C CA  . MET C 1 101 ? -48.804 -2.828  1.216   1.00 56.39  ? 101 MET C CA  1 
ATOM 4201 C C   . MET C 1 101 ? -49.821 -2.925  2.339   1.00 57.25  ? 101 MET C C   1 
ATOM 4202 O O   . MET C 1 101 ? -50.107 -1.931  3.013   1.00 62.07  ? 101 MET C O   1 
ATOM 4203 C CB  . MET C 1 101 ? -47.383 -2.850  1.791   1.00 55.39  ? 101 MET C CB  1 
ATOM 4204 C CG  . MET C 1 101 ? -47.022 -4.136  2.510   1.00 57.17  ? 101 MET C CG  1 
ATOM 4205 S SD  . MET C 1 101 ? -46.344 -5.378  1.397   1.00 62.16  ? 101 MET C SD  1 
ATOM 4206 C CE  . MET C 1 101 ? -44.922 -4.506  0.745   1.00 56.04  ? 101 MET C CE  1 
ATOM 4207 N N   . MET C 1 102 ? -50.367 -4.118  2.540   1.00 59.41  ? 102 MET C N   1 
ATOM 4208 C CA  . MET C 1 102 ? -51.320 -4.355  3.613   1.00 66.93  ? 102 MET C CA  1 
ATOM 4209 C C   . MET C 1 102 ? -50.691 -5.273  4.651   1.00 70.52  ? 102 MET C C   1 
ATOM 4210 O O   . MET C 1 102 ? -50.338 -6.415  4.339   1.00 71.18  ? 102 MET C O   1 
ATOM 4211 C CB  . MET C 1 102 ? -52.611 -4.981  3.097   1.00 61.95  ? 102 MET C CB  1 
ATOM 4212 C CG  . MET C 1 102 ? -53.751 -4.010  2.980   1.00 67.58  ? 102 MET C CG  1 
ATOM 4213 S SD  . MET C 1 102 ? -54.500 -3.866  4.607   1.00 94.22  ? 102 MET C SD  1 
ATOM 4214 C CE  . MET C 1 102 ? -55.021 -5.547  4.879   1.00 72.67  ? 102 MET C CE  1 
ATOM 4215 N N   . VAL C 1 103 ? -50.565 -4.777  5.879   1.00 80.21  ? 103 VAL C N   1 
ATOM 4216 C CA  . VAL C 1 103 ? -50.097 -5.581  7.003   1.00 81.65  ? 103 VAL C CA  1 
ATOM 4217 C C   . VAL C 1 103 ? -51.208 -5.685  8.049   1.00 87.06  ? 103 VAL C C   1 
ATOM 4218 O O   . VAL C 1 103 ? -51.771 -6.765  8.260   1.00 100.98 ? 103 VAL C O   1 
ATOM 4219 C CB  . VAL C 1 103 ? -48.782 -5.009  7.573   1.00 80.07  ? 103 VAL C CB  1 
ATOM 4220 C CG1 . VAL C 1 103 ? -48.906 -3.524  7.895   1.00 82.83  ? 103 VAL C CG1 1 
ATOM 4221 C CG2 . VAL C 1 103 ? -48.360 -5.782  8.810   1.00 82.99  ? 103 VAL C CG2 1 
ATOM 4222 N N   . ASP C 1 104 ? -51.534 -4.575  8.702   1.00 78.60  ? 104 ASP C N   1 
ATOM 4223 C CA  . ASP C 1 104 ? -52.714 -4.421  9.542   1.00 84.90  ? 104 ASP C CA  1 
ATOM 4224 C C   . ASP C 1 104 ? -53.642 -3.344  9.011   1.00 88.79  ? 104 ASP C C   1 
ATOM 4225 O O   . ASP C 1 104 ? -54.866 -3.503  9.054   1.00 88.72  ? 104 ASP C O   1 
ATOM 4226 C CB  . ASP C 1 104 ? -52.303 -4.082  10.985  1.00 90.66  ? 104 ASP C CB  1 
ATOM 4227 C CG  . ASP C 1 104 ? -53.483 -4.054  11.940  1.00 98.29  ? 104 ASP C CG  1 
ATOM 4228 O OD1 . ASP C 1 104 ? -54.523 -4.670  11.626  1.00 97.29  ? 104 ASP C OD1 1 
ATOM 4229 O OD2 . ASP C 1 104 ? -53.372 -3.411  13.006  1.00 96.31  ? 104 ASP C OD2 1 
ATOM 4230 N N   . GLU C 1 105 ? -53.076 -2.253  8.507   1.00 85.49  ? 105 GLU C N   1 
ATOM 4231 C CA  . GLU C 1 105 ? -53.781 -1.232  7.754   1.00 72.07  ? 105 GLU C CA  1 
ATOM 4232 C C   . GLU C 1 105 ? -53.004 -0.968  6.471   1.00 66.42  ? 105 GLU C C   1 
ATOM 4233 O O   . GLU C 1 105 ? -51.872 -1.429  6.301   1.00 66.05  ? 105 GLU C O   1 
ATOM 4234 C CB  . GLU C 1 105 ? -53.935 0.057   8.569   1.00 75.81  ? 105 GLU C CB  1 
ATOM 4235 C CG  . GLU C 1 105 ? -52.616 0.600   9.085   1.00 80.06  ? 105 GLU C CG  1 
ATOM 4236 C CD  . GLU C 1 105 ? -52.767 1.942   9.765   1.00 87.02  ? 105 GLU C CD  1 
ATOM 4237 O OE1 . GLU C 1 105 ? -53.914 2.332   10.062  1.00 93.47  ? 105 GLU C OE1 1 
ATOM 4238 O OE2 . GLU C 1 105 ? -51.737 2.604   10.007  1.00 89.96  ? 105 GLU C OE2 1 
ATOM 4239 N N   . VAL C 1 106 ? -53.621 -0.215  5.560   1.00 66.54  ? 106 VAL C N   1 
ATOM 4240 C CA  . VAL C 1 106 ? -52.963 0.103   4.299   1.00 63.34  ? 106 VAL C CA  1 
ATOM 4241 C C   . VAL C 1 106 ? -51.719 0.939   4.561   1.00 62.02  ? 106 VAL C C   1 
ATOM 4242 O O   . VAL C 1 106 ? -51.769 1.961   5.256   1.00 70.88  ? 106 VAL C O   1 
ATOM 4243 C CB  . VAL C 1 106 ? -53.940 0.818   3.357   1.00 58.73  ? 106 VAL C CB  1 
ATOM 4244 C CG1 . VAL C 1 106 ? -53.293 1.022   2.020   1.00 57.46  ? 106 VAL C CG1 1 
ATOM 4245 C CG2 . VAL C 1 106 ? -55.213 -0.001  3.195   1.00 57.90  ? 106 VAL C CG2 1 
ATOM 4246 N N   . THR C 1 107 ? -50.590 0.502   4.004   1.00 55.12  ? 107 THR C N   1 
ATOM 4247 C CA  . THR C 1 107 ? -49.308 1.177   4.163   1.00 57.50  ? 107 THR C CA  1 
ATOM 4248 C C   . THR C 1 107 ? -48.756 1.519   2.786   1.00 58.19  ? 107 THR C C   1 
ATOM 4249 O O   . THR C 1 107 ? -48.683 0.651   1.910   1.00 63.88  ? 107 THR C O   1 
ATOM 4250 C CB  . THR C 1 107 ? -48.311 0.306   4.934   1.00 62.51  ? 107 THR C CB  1 
ATOM 4251 O OG1 . THR C 1 107 ? -48.897 -0.113  6.173   1.00 64.71  ? 107 THR C OG1 1 
ATOM 4252 C CG2 . THR C 1 107 ? -47.041 1.088   5.233   1.00 65.04  ? 107 THR C CG2 1 
ATOM 4253 N N   . ARG C 1 108 ? -48.364 2.776   2.603   1.00 54.10  ? 108 ARG C N   1 
ATOM 4254 C CA  . ARG C 1 108 ? -47.941 3.291   1.309   1.00 55.37  ? 108 ARG C CA  1 
ATOM 4255 C C   . ARG C 1 108 ? -46.422 3.266   1.187   1.00 53.55  ? 108 ARG C C   1 
ATOM 4256 O O   . ARG C 1 108 ? -45.707 3.599   2.136   1.00 56.34  ? 108 ARG C O   1 
ATOM 4257 C CB  . ARG C 1 108 ? -48.461 4.717   1.107   1.00 65.57  ? 108 ARG C CB  1 
ATOM 4258 C CG  . ARG C 1 108 ? -49.973 4.805   0.963   1.00 66.94  ? 108 ARG C CG  1 
ATOM 4259 C CD  . ARG C 1 108 ? -50.450 6.251   0.979   1.00 63.87  ? 108 ARG C CD  1 
ATOM 4260 N NE  . ARG C 1 108 ? -51.871 6.366   0.673   1.00 66.71  ? 108 ARG C NE  1 
ATOM 4261 C CZ  . ARG C 1 108 ? -52.842 6.312   1.576   1.00 65.99  ? 108 ARG C CZ  1 
ATOM 4262 N NH1 . ARG C 1 108 ? -52.581 6.146   2.864   1.00 59.13  ? 108 ARG C NH1 1 
ATOM 4263 N NH2 . ARG C 1 108 ? -54.106 6.426   1.178   1.00 62.87  ? 108 ARG C NH2 1 
ATOM 4264 N N   . HIS C 1 109 ? -45.937 2.869   0.008   1.00 53.58  ? 109 HIS C N   1 
ATOM 4265 C CA  . HIS C 1 109 ? -44.512 2.780   -0.290  1.00 53.82  ? 109 HIS C CA  1 
ATOM 4266 C C   . HIS C 1 109 ? -44.040 3.837   -1.282  1.00 53.54  ? 109 HIS C C   1 
ATOM 4267 O O   . HIS C 1 109 ? -42.945 3.710   -1.838  1.00 53.69  ? 109 HIS C O   1 
ATOM 4268 C CB  . HIS C 1 109 ? -44.159 1.383   -0.807  1.00 61.68  ? 109 HIS C CB  1 
ATOM 4269 C CG  . HIS C 1 109 ? -44.098 0.335   0.264   1.00 60.74  ? 109 HIS C CG  1 
ATOM 4270 N ND1 . HIS C 1 109 ? -44.796 0.436   1.448   1.00 59.49  ? 109 HIS C ND1 1 
ATOM 4271 C CD2 . HIS C 1 109 ? -43.390 -0.817  0.342   1.00 55.20  ? 109 HIS C CD2 1 
ATOM 4272 C CE1 . HIS C 1 109 ? -44.535 -0.617  2.202   1.00 58.78  ? 109 HIS C CE1 1 
ATOM 4273 N NE2 . HIS C 1 109 ? -43.684 -1.392  1.554   1.00 59.08  ? 109 HIS C NE2 1 
ATOM 4274 N N   . GLY C 1 110 ? -44.834 4.875   -1.513  1.00 54.61  ? 110 GLY C N   1 
ATOM 4275 C CA  . GLY C 1 110 ? -44.425 5.973   -2.362  1.00 58.84  ? 110 GLY C CA  1 
ATOM 4276 C C   . GLY C 1 110 ? -44.930 5.834   -3.789  1.00 58.81  ? 110 GLY C C   1 
ATOM 4277 O O   . GLY C 1 110 ? -45.409 4.785   -4.226  1.00 65.26  ? 110 GLY C O   1 
ATOM 4278 N N   . MET C 1 111 ? -44.807 6.940   -4.524  1.00 58.34  ? 111 MET C N   1 
ATOM 4279 C CA  . MET C 1 111 ? -45.216 7.030   -5.926  1.00 63.07  ? 111 MET C CA  1 
ATOM 4280 C C   . MET C 1 111 ? -43.980 6.823   -6.797  1.00 61.88  ? 111 MET C C   1 
ATOM 4281 O O   . MET C 1 111 ? -43.213 7.758   -7.038  1.00 59.70  ? 111 MET C O   1 
ATOM 4282 C CB  . MET C 1 111 ? -45.883 8.373   -6.206  1.00 60.16  ? 111 MET C CB  1 
ATOM 4283 C CG  . MET C 1 111 ? -47.178 8.596   -5.435  1.00 62.43  ? 111 MET C CG  1 
ATOM 4284 S SD  . MET C 1 111 ? -47.837 10.268  -5.586  1.00 70.70  ? 111 MET C SD  1 
ATOM 4285 C CE  . MET C 1 111 ? -47.076 11.057  -4.169  1.00 62.36  ? 111 MET C CE  1 
ATOM 4286 N N   . ASP C 1 112 ? -43.795 5.592   -7.280  1.00 63.99  ? 112 ASP C N   1 
ATOM 4287 C CA  . ASP C 1 112 ? -42.581 5.260   -8.016  1.00 65.87  ? 112 ASP C CA  1 
ATOM 4288 C C   . ASP C 1 112 ? -42.624 5.731   -9.464  1.00 64.62  ? 112 ASP C C   1 
ATOM 4289 O O   . ASP C 1 112 ? -41.580 6.081   -10.025 1.00 65.24  ? 112 ASP C O   1 
ATOM 4290 C CB  . ASP C 1 112 ? -42.330 3.751   -7.974  1.00 69.97  ? 112 ASP C CB  1 
ATOM 4291 C CG  . ASP C 1 112 ? -43.596 2.936   -8.171  1.00 69.97  ? 112 ASP C CG  1 
ATOM 4292 O OD1 . ASP C 1 112 ? -44.650 3.520   -8.502  1.00 74.61  ? 112 ASP C OD1 1 
ATOM 4293 O OD2 . ASP C 1 112 ? -43.526 1.700   -8.013  1.00 62.86  ? 112 ASP C OD2 1 
ATOM 4294 N N   . VAL C 1 113 ? -43.800 5.743   -10.084 1.00 62.60  ? 113 VAL C N   1 
ATOM 4295 C CA  . VAL C 1 113 ? -43.949 6.110   -11.487 1.00 62.60  ? 113 VAL C CA  1 
ATOM 4296 C C   . VAL C 1 113 ? -44.763 7.393   -11.568 1.00 60.17  ? 113 VAL C C   1 
ATOM 4297 O O   . VAL C 1 113 ? -45.870 7.468   -11.024 1.00 60.18  ? 113 VAL C O   1 
ATOM 4298 C CB  . VAL C 1 113 ? -44.613 4.985   -12.300 1.00 65.56  ? 113 VAL C CB  1 
ATOM 4299 C CG1 . VAL C 1 113 ? -44.566 5.311   -13.784 1.00 66.24  ? 113 VAL C CG1 1 
ATOM 4300 C CG2 . VAL C 1 113 ? -43.926 3.657   -12.022 1.00 67.00  ? 113 VAL C CG2 1 
ATOM 4301 N N   . TRP C 1 114 ? -44.212 8.397   -12.245 1.00 53.74  ? 114 TRP C N   1 
ATOM 4302 C CA  . TRP C 1 114 ? -44.845 9.697   -12.411 1.00 58.85  ? 114 TRP C CA  1 
ATOM 4303 C C   . TRP C 1 114 ? -45.012 9.997   -13.892 1.00 63.83  ? 114 TRP C C   1 
ATOM 4304 O O   . TRP C 1 114 ? -44.162 9.625   -14.707 1.00 63.58  ? 114 TRP C O   1 
ATOM 4305 C CB  . TRP C 1 114 ? -44.010 10.810  -11.765 1.00 64.14  ? 114 TRP C CB  1 
ATOM 4306 C CG  . TRP C 1 114 ? -43.976 10.782  -10.269 1.00 58.35  ? 114 TRP C CG  1 
ATOM 4307 C CD1 . TRP C 1 114 ? -43.253 9.935   -9.482  1.00 59.83  ? 114 TRP C CD1 1 
ATOM 4308 C CD2 . TRP C 1 114 ? -44.667 11.666  -9.377  1.00 60.57  ? 114 TRP C CD2 1 
ATOM 4309 N NE1 . TRP C 1 114 ? -43.465 10.223  -8.156  1.00 62.20  ? 114 TRP C NE1 1 
ATOM 4310 C CE2 . TRP C 1 114 ? -44.328 11.283  -8.065  1.00 63.30  ? 114 TRP C CE2 1 
ATOM 4311 C CE3 . TRP C 1 114 ? -45.546 12.738  -9.562  1.00 62.72  ? 114 TRP C CE3 1 
ATOM 4312 C CZ2 . TRP C 1 114 ? -44.838 11.934  -6.942  1.00 63.77  ? 114 TRP C CZ2 1 
ATOM 4313 C CZ3 . TRP C 1 114 ? -46.051 13.384  -8.446  1.00 62.40  ? 114 TRP C CZ3 1 
ATOM 4314 C CH2 . TRP C 1 114 ? -45.695 12.979  -7.154  1.00 64.24  ? 114 TRP C CH2 1 
ATOM 4315 N N   . SER C 1 115 ? -46.103 10.675  -14.239 1.00 67.00  ? 115 SER C N   1 
ATOM 4316 C CA  . SER C 1 115 ? -46.242 11.185  -15.595 1.00 67.27  ? 115 SER C CA  1 
ATOM 4317 C C   . SER C 1 115 ? -45.199 12.259  -15.863 1.00 74.56  ? 115 SER C C   1 
ATOM 4318 O O   . SER C 1 115 ? -44.688 12.905  -14.945 1.00 81.61  ? 115 SER C O   1 
ATOM 4319 C CB  . SER C 1 115 ? -47.630 11.767  -15.821 1.00 63.44  ? 115 SER C CB  1 
ATOM 4320 O OG  . SER C 1 115 ? -47.669 13.154  -15.547 1.00 64.37  ? 115 SER C OG  1 
ATOM 4321 N N   . GLN C 1 116 ? -44.891 12.451  -17.148 1.00 87.81  ? 116 GLN C N   1 
ATOM 4322 C CA  . GLN C 1 116 ? -43.964 13.510  -17.530 1.00 89.13  ? 116 GLN C CA  1 
ATOM 4323 C C   . GLN C 1 116 ? -44.495 14.884  -17.144 1.00 88.19  ? 116 GLN C C   1 
ATOM 4324 O O   . GLN C 1 116 ? -43.710 15.802  -16.878 1.00 88.46  ? 116 GLN C O   1 
ATOM 4325 C CB  . GLN C 1 116 ? -43.679 13.446  -19.032 1.00 93.12  ? 116 GLN C CB  1 
ATOM 4326 C CG  . GLN C 1 116 ? -44.892 13.675  -19.926 1.00 95.54  ? 116 GLN C CG  1 
ATOM 4327 C CD  . GLN C 1 116 ? -45.672 12.400  -20.199 1.00 100.02 ? 116 GLN C CD  1 
ATOM 4328 O OE1 . GLN C 1 116 ? -46.322 11.851  -19.308 1.00 98.14  ? 116 GLN C OE1 1 
ATOM 4329 N NE2 . GLN C 1 116 ? -45.608 11.921  -21.436 1.00 102.51 ? 116 GLN C NE2 1 
ATOM 4330 N N   . GLY C 1 117 ? -45.814 15.045  -17.096 1.00 73.05  ? 117 GLY C N   1 
ATOM 4331 C CA  . GLY C 1 117 ? -46.399 16.288  -16.643 1.00 66.84  ? 117 GLY C CA  1 
ATOM 4332 C C   . GLY C 1 117 ? -46.785 17.230  -17.762 1.00 69.49  ? 117 GLY C C   1 
ATOM 4333 O O   . GLY C 1 117 ? -45.943 17.617  -18.579 1.00 70.31  ? 117 GLY C O   1 
ATOM 4334 N N   . THR C 1 118 ? -48.057 17.611  -17.809 1.00 66.69  ? 118 THR C N   1 
ATOM 4335 C CA  . THR C 1 118 ? -48.564 18.550  -18.798 1.00 59.26  ? 118 THR C CA  1 
ATOM 4336 C C   . THR C 1 118 ? -48.908 19.863  -18.112 1.00 55.70  ? 118 THR C C   1 
ATOM 4337 O O   . THR C 1 118 ? -49.582 19.870  -17.077 1.00 55.11  ? 118 THR C O   1 
ATOM 4338 C CB  . THR C 1 118 ? -49.799 17.995  -19.511 1.00 55.98  ? 118 THR C CB  1 
ATOM 4339 O OG1 . THR C 1 118 ? -50.764 17.576  -18.540 1.00 54.39  ? 118 THR C OG1 1 
ATOM 4340 C CG2 . THR C 1 118 ? -49.419 16.813  -20.385 1.00 53.82  ? 118 THR C CG2 1 
ATOM 4341 N N   . MET C 1 119 ? -48.443 20.967  -18.689 1.00 55.32  ? 119 MET C N   1 
ATOM 4342 C CA  . MET C 1 119 ? -48.797 22.285  -18.187 1.00 55.03  ? 119 MET C CA  1 
ATOM 4343 C C   . MET C 1 119 ? -50.225 22.634  -18.578 1.00 52.45  ? 119 MET C C   1 
ATOM 4344 O O   . MET C 1 119 ? -50.669 22.347  -19.694 1.00 52.61  ? 119 MET C O   1 
ATOM 4345 C CB  . MET C 1 119 ? -47.836 23.344  -18.727 1.00 61.80  ? 119 MET C CB  1 
ATOM 4346 C CG  . MET C 1 119 ? -46.392 22.893  -18.803 1.00 66.18  ? 119 MET C CG  1 
ATOM 4347 S SD  . MET C 1 119 ? -45.275 24.273  -19.109 1.00 80.94  ? 119 MET C SD  1 
ATOM 4348 C CE  . MET C 1 119 ? -43.721 23.406  -19.298 1.00 73.60  ? 119 MET C CE  1 
ATOM 4349 N N   . VAL C 1 120 ? -50.944 23.256  -17.650 1.00 52.33  ? 120 VAL C N   1 
ATOM 4350 C CA  . VAL C 1 120 ? -52.311 23.707  -17.868 1.00 52.35  ? 120 VAL C CA  1 
ATOM 4351 C C   . VAL C 1 120 ? -52.346 25.205  -17.608 1.00 57.23  ? 120 VAL C C   1 
ATOM 4352 O O   . VAL C 1 120 ? -52.066 25.651  -16.489 1.00 60.65  ? 120 VAL C O   1 
ATOM 4353 C CB  . VAL C 1 120 ? -53.307 22.967  -16.963 1.00 52.03  ? 120 VAL C CB  1 
ATOM 4354 C CG1 . VAL C 1 120 ? -54.624 23.724  -16.887 1.00 52.03  ? 120 VAL C CG1 1 
ATOM 4355 C CG2 . VAL C 1 120 ? -53.514 21.550  -17.459 1.00 51.96  ? 120 VAL C CG2 1 
ATOM 4356 N N   . THR C 1 121 ? -52.678 25.977  -18.637 1.00 54.22  ? 121 THR C N   1 
ATOM 4357 C CA  . THR C 1 121 ? -52.716 27.431  -18.560 1.00 55.22  ? 121 THR C CA  1 
ATOM 4358 C C   . THR C 1 121 ? -54.167 27.891  -18.568 1.00 57.10  ? 121 THR C C   1 
ATOM 4359 O O   . THR C 1 121 ? -54.912 27.588  -19.507 1.00 61.20  ? 121 THR C O   1 
ATOM 4360 C CB  . THR C 1 121 ? -51.948 28.060  -19.723 1.00 56.80  ? 121 THR C CB  1 
ATOM 4361 O OG1 . THR C 1 121 ? -50.577 27.646  -19.675 1.00 61.18  ? 121 THR C OG1 1 
ATOM 4362 C CG2 . THR C 1 121 ? -52.019 29.579  -19.658 1.00 60.68  ? 121 THR C CG2 1 
ATOM 4363 N N   . VAL C 1 122 ? -54.564 28.611  -17.524 1.00 54.88  ? 122 VAL C N   1 
ATOM 4364 C CA  . VAL C 1 122 ? -55.887 29.217  -17.437 1.00 54.94  ? 122 VAL C CA  1 
ATOM 4365 C C   . VAL C 1 122 ? -55.738 30.690  -17.791 1.00 59.25  ? 122 VAL C C   1 
ATOM 4366 O O   . VAL C 1 122 ? -55.117 31.459  -17.048 1.00 59.26  ? 122 VAL C O   1 
ATOM 4367 C CB  . VAL C 1 122 ? -56.510 29.038  -16.047 1.00 53.74  ? 122 VAL C CB  1 
ATOM 4368 C CG1 . VAL C 1 122 ? -57.755 29.901  -15.915 1.00 55.66  ? 122 VAL C CG1 1 
ATOM 4369 C CG2 . VAL C 1 122 ? -56.842 27.575  -15.798 1.00 54.83  ? 122 VAL C CG2 1 
ATOM 4370 N N   . SER C 1 123 ? -56.306 31.081  -18.928 1.00 61.83  ? 123 SER C N   1 
ATOM 4371 C CA  . SER C 1 123 ? -56.243 32.455  -19.401 1.00 57.75  ? 123 SER C CA  1 
ATOM 4372 C C   . SER C 1 123 ? -57.317 32.649  -20.459 1.00 66.23  ? 123 SER C C   1 
ATOM 4373 O O   . SER C 1 123 ? -57.875 31.685  -20.988 1.00 65.83  ? 123 SER C O   1 
ATOM 4374 C CB  . SER C 1 123 ? -54.861 32.797  -19.965 1.00 56.32  ? 123 SER C CB  1 
ATOM 4375 O OG  . SER C 1 123 ? -54.957 33.794  -20.967 1.00 63.85  ? 123 SER C OG  1 
ATOM 4376 N N   . SER C 1 124 ? -57.599 33.914  -20.759 1.00 65.88  ? 124 SER C N   1 
ATOM 4377 C CA  . SER C 1 124 ? -58.557 34.276  -21.794 1.00 63.82  ? 124 SER C CA  1 
ATOM 4378 C C   . SER C 1 124 ? -57.893 34.618  -23.120 1.00 65.65  ? 124 SER C C   1 
ATOM 4379 O O   . SER C 1 124 ? -58.596 34.889  -24.098 1.00 68.86  ? 124 SER C O   1 
ATOM 4380 C CB  . SER C 1 124 ? -59.414 35.458  -21.329 1.00 60.96  ? 124 SER C CB  1 
ATOM 4381 O OG  . SER C 1 124 ? -58.611 36.604  -21.105 1.00 62.00  ? 124 SER C OG  1 
ATOM 4382 N N   . ALA C 1 125 ? -56.564 34.608  -23.178 1.00 65.37  ? 125 ALA C N   1 
ATOM 4383 C CA  . ALA C 1 125 ? -55.862 35.011  -24.387 1.00 73.08  ? 125 ALA C CA  1 
ATOM 4384 C C   . ALA C 1 125 ? -56.028 33.972  -25.491 1.00 77.27  ? 125 ALA C C   1 
ATOM 4385 O O   . ALA C 1 125 ? -56.144 32.770  -25.236 1.00 77.23  ? 125 ALA C O   1 
ATOM 4386 C CB  . ALA C 1 125 ? -54.377 35.227  -24.096 1.00 75.64  ? 125 ALA C CB  1 
ATOM 4387 N N   . SER C 1 126 ? -56.039 34.452  -26.731 1.00 82.79  ? 126 SER C N   1 
ATOM 4388 C CA  . SER C 1 126 ? -56.159 33.576  -27.886 1.00 82.30  ? 126 SER C CA  1 
ATOM 4389 C C   . SER C 1 126 ? -54.828 32.890  -28.175 1.00 80.93  ? 126 SER C C   1 
ATOM 4390 O O   . SER C 1 126 ? -53.754 33.409  -27.858 1.00 76.33  ? 126 SER C O   1 
ATOM 4391 C CB  . SER C 1 126 ? -56.619 34.366  -29.111 1.00 84.73  ? 126 SER C CB  1 
ATOM 4392 O OG  . SER C 1 126 ? -57.769 35.141  -28.818 1.00 88.64  ? 126 SER C OG  1 
ATOM 4393 N N   . THR C 1 127 ? -54.910 31.707  -28.780 1.00 82.35  ? 127 THR C N   1 
ATOM 4394 C CA  . THR C 1 127 ? -53.711 30.960  -29.143 1.00 83.94  ? 127 THR C CA  1 
ATOM 4395 C C   . THR C 1 127 ? -52.994 31.665  -30.288 1.00 87.49  ? 127 THR C C   1 
ATOM 4396 O O   . THR C 1 127 ? -53.586 31.908  -31.345 1.00 89.86  ? 127 THR C O   1 
ATOM 4397 C CB  . THR C 1 127 ? -54.075 29.529  -29.539 1.00 79.75  ? 127 THR C CB  1 
ATOM 4398 O OG1 . THR C 1 127 ? -54.478 28.796  -28.376 1.00 79.45  ? 127 THR C OG1 1 
ATOM 4399 C CG2 . THR C 1 127 ? -52.885 28.829  -30.187 1.00 85.98  ? 127 THR C CG2 1 
ATOM 4400 N N   . LYS C 1 128 ? -51.726 32.005  -30.077 1.00 91.80  ? 128 LYS C N   1 
ATOM 4401 C CA  . LYS C 1 128 ? -50.900 32.629  -31.100 1.00 97.87  ? 128 LYS C CA  1 
ATOM 4402 C C   . LYS C 1 128 ? -49.780 31.681  -31.506 1.00 107.67 ? 128 LYS C C   1 
ATOM 4403 O O   . LYS C 1 128 ? -49.183 31.010  -30.658 1.00 111.27 ? 128 LYS C O   1 
ATOM 4404 C CB  . LYS C 1 128 ? -50.308 33.954  -30.612 1.00 102.88 ? 128 LYS C CB  1 
ATOM 4405 C CG  . LYS C 1 128 ? -49.727 34.802  -31.732 1.00 109.63 ? 128 LYS C CG  1 
ATOM 4406 C CD  . LYS C 1 128 ? -49.248 36.150  -31.229 1.00 113.60 ? 128 LYS C CD  1 
ATOM 4407 C CE  . LYS C 1 128 ? -48.501 36.898  -32.320 1.00 122.84 ? 128 LYS C CE  1 
ATOM 4408 N NZ  . LYS C 1 128 ? -47.439 36.057  -32.942 1.00 130.00 ? 128 LYS C NZ  1 
ATOM 4409 N N   . GLY C 1 129 ? -49.500 31.629  -32.805 1.00 112.45 ? 129 GLY C N   1 
ATOM 4410 C CA  . GLY C 1 129 ? -48.478 30.758  -33.331 1.00 124.08 ? 129 GLY C CA  1 
ATOM 4411 C C   . GLY C 1 129 ? -47.083 31.329  -33.180 1.00 133.06 ? 129 GLY C C   1 
ATOM 4412 O O   . GLY C 1 129 ? -46.895 32.538  -33.010 1.00 131.61 ? 129 GLY C O   1 
ATOM 4413 N N   . PRO C 1 130 ? -46.064 30.457  -33.239 1.00 143.08 ? 130 PRO C N   1 
ATOM 4414 C CA  . PRO C 1 130 ? -44.659 30.858  -33.145 1.00 147.59 ? 130 PRO C CA  1 
ATOM 4415 C C   . PRO C 1 130 ? -44.040 31.193  -34.499 1.00 146.26 ? 130 PRO C C   1 
ATOM 4416 O O   . PRO C 1 130 ? -44.559 30.751  -35.524 1.00 139.14 ? 130 PRO C O   1 
ATOM 4417 C CB  . PRO C 1 130 ? -43.995 29.626  -32.535 1.00 147.43 ? 130 PRO C CB  1 
ATOM 4418 C CG  . PRO C 1 130 ? -44.811 28.477  -33.047 1.00 137.85 ? 130 PRO C CG  1 
ATOM 4419 C CD  . PRO C 1 130 ? -46.204 28.995  -33.359 1.00 137.55 ? 130 PRO C CD  1 
ATOM 4420 N N   . CYS C 1 151 ? -31.663 28.590  -33.226 1.00 109.90 ? 151 CYS C N   1 
ATOM 4421 C CA  . CYS C 1 151 ? -33.050 28.855  -33.587 1.00 110.12 ? 151 CYS C CA  1 
ATOM 4422 C C   . CYS C 1 151 ? -33.712 29.771  -32.558 1.00 120.52 ? 151 CYS C C   1 
ATOM 4423 O O   . CYS C 1 151 ? -33.296 29.822  -31.401 1.00 126.90 ? 151 CYS C O   1 
ATOM 4424 C CB  . CYS C 1 151 ? -33.833 27.542  -33.718 1.00 110.20 ? 151 CYS C CB  1 
ATOM 4425 S SG  . CYS C 1 151 ? -33.202 26.412  -34.992 1.00 113.27 ? 151 CYS C SG  1 
ATOM 4426 N N   . LEU C 1 152 ? -34.739 30.499  -32.992 1.00 130.92 ? 152 LEU C N   1 
ATOM 4427 C CA  . LEU C 1 152 ? -35.453 31.426  -32.124 1.00 143.72 ? 152 LEU C CA  1 
ATOM 4428 C C   . LEU C 1 152 ? -36.949 31.264  -32.343 1.00 159.12 ? 152 LEU C C   1 
ATOM 4429 O O   . LEU C 1 152 ? -37.411 31.204  -33.487 1.00 147.06 ? 152 LEU C O   1 
ATOM 4430 C CB  . LEU C 1 152 ? -35.030 32.875  -32.392 1.00 127.33 ? 152 LEU C CB  1 
ATOM 4431 C CG  . LEU C 1 152 ? -35.543 33.925  -31.404 1.00 125.85 ? 152 LEU C CG  1 
ATOM 4432 C CD1 . LEU C 1 152 ? -34.569 34.102  -30.247 1.00 119.79 ? 152 LEU C CD1 1 
ATOM 4433 C CD2 . LEU C 1 152 ? -35.785 35.248  -32.112 1.00 114.99 ? 152 LEU C CD2 1 
ATOM 4434 N N   . VAL C 1 153 ? -37.698 31.191  -31.245 1.00 191.92 ? 153 VAL C N   1 
ATOM 4435 C CA  . VAL C 1 153 ? -39.148 31.044  -31.271 1.00 190.98 ? 153 VAL C CA  1 
ATOM 4436 C C   . VAL C 1 153 ? -39.764 32.384  -30.890 1.00 191.45 ? 153 VAL C C   1 
ATOM 4437 O O   . VAL C 1 153 ? -39.276 33.061  -29.977 1.00 191.78 ? 153 VAL C O   1 
ATOM 4438 C CB  . VAL C 1 153 ? -39.607 29.921  -30.319 1.00 189.71 ? 153 VAL C CB  1 
ATOM 4439 C CG1 . VAL C 1 153 ? -41.117 29.778  -30.339 1.00 189.08 ? 153 VAL C CG1 1 
ATOM 4440 C CG2 . VAL C 1 153 ? -38.926 28.606  -30.683 1.00 188.73 ? 153 VAL C CG2 1 
ATOM 4441 N N   . LYS C 1 154 ? -40.832 32.770  -31.589 1.00 172.67 ? 154 LYS C N   1 
ATOM 4442 C CA  . LYS C 1 154 ? -41.356 34.130  -31.513 1.00 161.92 ? 154 LYS C CA  1 
ATOM 4443 C C   . LYS C 1 154 ? -42.837 34.137  -31.164 1.00 161.88 ? 154 LYS C C   1 
ATOM 4444 O O   . LYS C 1 154 ? -43.654 33.582  -31.906 1.00 153.90 ? 154 LYS C O   1 
ATOM 4445 C CB  . LYS C 1 154 ? -41.129 34.874  -32.831 1.00 151.52 ? 154 LYS C CB  1 
ATOM 4446 C CG  . LYS C 1 154 ? -40.827 36.342  -32.632 1.00 152.62 ? 154 LYS C CG  1 
ATOM 4447 C CD  . LYS C 1 154 ? -39.638 36.519  -31.709 1.00 140.43 ? 154 LYS C CD  1 
ATOM 4448 C CE  . LYS C 1 154 ? -39.565 37.938  -31.182 1.00 124.42 ? 154 LYS C CE  1 
ATOM 4449 N NZ  . LYS C 1 154 ? -40.673 38.215  -30.226 1.00 127.64 ? 154 LYS C NZ  1 
ATOM 4450 N N   . ASP C 1 155 ? -43.171 34.781  -30.045 1.00 169.52 ? 155 ASP C N   1 
ATOM 4451 C CA  . ASP C 1 155 ? -44.527 35.229  -29.720 1.00 169.36 ? 155 ASP C CA  1 
ATOM 4452 C C   . ASP C 1 155 ? -45.543 34.085  -29.806 1.00 168.61 ? 155 ASP C C   1 
ATOM 4453 O O   . ASP C 1 155 ? -46.428 34.056  -30.661 1.00 168.37 ? 155 ASP C O   1 
ATOM 4454 C CB  . ASP C 1 155 ? -44.934 36.392  -30.631 1.00 169.52 ? 155 ASP C CB  1 
ATOM 4455 C CG  . ASP C 1 155 ? -44.180 37.670  -30.318 1.00 170.11 ? 155 ASP C CG  1 
ATOM 4456 O OD1 . ASP C 1 155 ? -43.556 37.746  -29.238 1.00 170.34 ? 155 ASP C OD1 1 
ATOM 4457 O OD2 . ASP C 1 155 ? -44.209 38.600  -31.152 1.00 170.31 ? 155 ASP C OD2 1 
ATOM 4458 N N   . TYR C 1 156 ? -45.401 33.148  -28.874 1.00 133.35 ? 156 TYR C N   1 
ATOM 4459 C CA  . TYR C 1 156 ? -46.320 32.025  -28.749 1.00 124.84 ? 156 TYR C CA  1 
ATOM 4460 C C   . TYR C 1 156 ? -46.934 32.046  -27.357 1.00 119.83 ? 156 TYR C C   1 
ATOM 4461 O O   . TYR C 1 156 ? -46.213 32.128  -26.357 1.00 124.23 ? 156 TYR C O   1 
ATOM 4462 C CB  . TYR C 1 156 ? -45.607 30.695  -29.032 1.00 128.75 ? 156 TYR C CB  1 
ATOM 4463 C CG  . TYR C 1 156 ? -44.725 30.165  -27.918 1.00 124.12 ? 156 TYR C CG  1 
ATOM 4464 C CD1 . TYR C 1 156 ? -43.408 30.585  -27.785 1.00 125.76 ? 156 TYR C CD1 1 
ATOM 4465 C CD2 . TYR C 1 156 ? -45.201 29.216  -27.023 1.00 120.28 ? 156 TYR C CD2 1 
ATOM 4466 C CE1 . TYR C 1 156 ? -42.599 30.092  -26.776 1.00 127.33 ? 156 TYR C CE1 1 
ATOM 4467 C CE2 . TYR C 1 156 ? -44.400 28.717  -26.013 1.00 123.14 ? 156 TYR C CE2 1 
ATOM 4468 C CZ  . TYR C 1 156 ? -43.101 29.157  -25.894 1.00 122.22 ? 156 TYR C CZ  1 
ATOM 4469 O OH  . TYR C 1 156 ? -42.305 28.659  -24.888 1.00 111.17 ? 156 TYR C OH  1 
ATOM 4470 N N   . PHE C 1 157 ? -48.266 31.997  -27.294 1.00 105.57 ? 157 PHE C N   1 
ATOM 4471 C CA  . PHE C 1 157 ? -48.936 32.125  -26.006 1.00 100.94 ? 157 PHE C CA  1 
ATOM 4472 C C   . PHE C 1 157 ? -48.966 30.821  -25.209 1.00 105.73 ? 157 PHE C C   1 
ATOM 4473 O O   . PHE C 1 157 ? -48.537 30.821  -24.050 1.00 109.84 ? 157 PHE C O   1 
ATOM 4474 C CB  . PHE C 1 157 ? -50.359 32.661  -26.162 1.00 95.12  ? 157 PHE C CB  1 
ATOM 4475 C CG  . PHE C 1 157 ? -51.098 32.736  -24.864 1.00 92.54  ? 157 PHE C CG  1 
ATOM 4476 C CD1 . PHE C 1 157 ? -50.711 33.630  -23.881 1.00 97.90  ? 157 PHE C CD1 1 
ATOM 4477 C CD2 . PHE C 1 157 ? -52.147 31.871  -24.603 1.00 91.59  ? 157 PHE C CD2 1 
ATOM 4478 C CE1 . PHE C 1 157 ? -51.375 33.684  -22.676 1.00 94.30  ? 157 PHE C CE1 1 
ATOM 4479 C CE2 . PHE C 1 157 ? -52.815 31.921  -23.399 1.00 88.78  ? 157 PHE C CE2 1 
ATOM 4480 C CZ  . PHE C 1 157 ? -52.427 32.827  -22.434 1.00 87.15  ? 157 PHE C CZ  1 
ATOM 4481 N N   . PRO C 1 158 ? -49.469 29.706  -25.746 1.00 106.03 ? 158 PRO C N   1 
ATOM 4482 C CA  . PRO C 1 158 ? -49.512 28.479  -24.934 1.00 97.94  ? 158 PRO C CA  1 
ATOM 4483 C C   . PRO C 1 158 ? -48.103 27.993  -24.626 1.00 101.78 ? 158 PRO C C   1 
ATOM 4484 O O   . PRO C 1 158 ? -47.359 27.600  -25.526 1.00 106.93 ? 158 PRO C O   1 
ATOM 4485 C CB  . PRO C 1 158 ? -50.274 27.491  -25.824 1.00 101.41 ? 158 PRO C CB  1 
ATOM 4486 C CG  . PRO C 1 158 ? -51.052 28.358  -26.758 1.00 102.21 ? 158 PRO C CG  1 
ATOM 4487 C CD  . PRO C 1 158 ? -50.110 29.480  -27.054 1.00 101.59 ? 158 PRO C CD  1 
ATOM 4488 N N   . GLU C 1 159 ? -47.747 28.018  -23.341 1.00 93.26  ? 159 GLU C N   1 
ATOM 4489 C CA  . GLU C 1 159 ? -46.363 27.771  -22.943 1.00 96.85  ? 159 GLU C CA  1 
ATOM 4490 C C   . GLU C 1 159 ? -45.794 26.433  -23.412 1.00 102.53 ? 159 GLU C C   1 
ATOM 4491 O O   . GLU C 1 159 ? -44.620 26.415  -23.821 1.00 106.31 ? 159 GLU C O   1 
ATOM 4492 C CB  . GLU C 1 159 ? -46.234 27.907  -21.419 1.00 87.83  ? 159 GLU C CB  1 
ATOM 4493 C CG  . GLU C 1 159 ? -44.889 27.461  -20.849 1.00 87.20  ? 159 GLU C CG  1 
ATOM 4494 C CD  . GLU C 1 159 ? -43.754 28.435  -21.130 1.00 92.57  ? 159 GLU C CD  1 
ATOM 4495 O OE1 . GLU C 1 159 ? -43.618 28.906  -22.280 1.00 93.72  ? 159 GLU C OE1 1 
ATOM 4496 O OE2 . GLU C 1 159 ? -42.985 28.727  -20.191 1.00 90.78  ? 159 GLU C OE2 1 
ATOM 4497 N N   . PRO C 1 160 ? -46.527 25.292  -23.371 1.00 96.54  ? 160 PRO C N   1 
ATOM 4498 C CA  . PRO C 1 160 ? -45.935 24.032  -23.850 1.00 99.49  ? 160 PRO C CA  1 
ATOM 4499 C C   . PRO C 1 160 ? -45.371 24.109  -25.259 1.00 107.20 ? 160 PRO C C   1 
ATOM 4500 O O   . PRO C 1 160 ? -46.110 24.266  -26.237 1.00 111.45 ? 160 PRO C O   1 
ATOM 4501 C CB  . PRO C 1 160 ? -47.107 23.047  -23.782 1.00 103.10 ? 160 PRO C CB  1 
ATOM 4502 C CG  . PRO C 1 160 ? -47.936 23.552  -22.680 1.00 92.37  ? 160 PRO C CG  1 
ATOM 4503 C CD  . PRO C 1 160 ? -47.832 25.055  -22.725 1.00 89.12  ? 160 PRO C CD  1 
ATOM 4504 N N   . VAL C 1 161 ? -44.049 23.997  -25.363 1.00 110.67 ? 161 VAL C N   1 
ATOM 4505 C CA  . VAL C 1 161 ? -43.353 23.977  -26.642 1.00 115.67 ? 161 VAL C CA  1 
ATOM 4506 C C   . VAL C 1 161 ? -42.193 22.998  -26.532 1.00 122.62 ? 161 VAL C C   1 
ATOM 4507 O O   . VAL C 1 161 ? -41.604 22.816  -25.461 1.00 122.64 ? 161 VAL C O   1 
ATOM 4508 C CB  . VAL C 1 161 ? -42.866 25.386  -27.058 1.00 113.65 ? 161 VAL C CB  1 
ATOM 4509 C CG1 . VAL C 1 161 ? -41.534 25.709  -26.414 1.00 117.80 ? 161 VAL C CG1 1 
ATOM 4510 C CG2 . VAL C 1 161 ? -42.772 25.490  -28.572 1.00 118.16 ? 161 VAL C CG2 1 
ATOM 4511 N N   . THR C 1 162 ? -41.879 22.348  -27.649 1.00 127.83 ? 162 THR C N   1 
ATOM 4512 C CA  . THR C 1 162 ? -40.859 21.306  -27.686 1.00 130.74 ? 162 THR C CA  1 
ATOM 4513 C C   . THR C 1 162 ? -39.915 21.578  -28.846 1.00 131.51 ? 162 THR C C   1 
ATOM 4514 O O   . THR C 1 162 ? -40.357 21.714  -29.991 1.00 135.84 ? 162 THR C O   1 
ATOM 4515 C CB  . THR C 1 162 ? -41.495 19.920  -27.821 1.00 131.18 ? 162 THR C CB  1 
ATOM 4516 O OG1 . THR C 1 162 ? -42.501 19.952  -28.839 1.00 127.14 ? 162 THR C OG1 1 
ATOM 4517 C CG2 . THR C 1 162 ? -42.124 19.492  -26.504 1.00 125.19 ? 162 THR C CG2 1 
ATOM 4518 N N   . VAL C 1 163 ? -38.622 21.655  -28.547 1.00 127.63 ? 163 VAL C N   1 
ATOM 4519 C CA  . VAL C 1 163 ? -37.588 21.938  -29.534 1.00 128.74 ? 163 VAL C CA  1 
ATOM 4520 C C   . VAL C 1 163 ? -36.613 20.771  -29.556 1.00 130.14 ? 163 VAL C C   1 
ATOM 4521 O O   . VAL C 1 163 ? -36.182 20.295  -28.499 1.00 130.95 ? 163 VAL C O   1 
ATOM 4522 C CB  . VAL C 1 163 ? -36.852 23.254  -29.225 1.00 127.77 ? 163 VAL C CB  1 
ATOM 4523 C CG1 . VAL C 1 163 ? -35.925 23.623  -30.372 1.00 125.40 ? 163 VAL C CG1 1 
ATOM 4524 C CG2 . VAL C 1 163 ? -37.848 24.370  -28.954 1.00 129.92 ? 163 VAL C CG2 1 
ATOM 4525 N N   . SER C 1 164 ? -36.265 20.316  -30.756 1.00 128.21 ? 164 SER C N   1 
ATOM 4526 C CA  . SER C 1 164 ? -35.313 19.233  -30.943 1.00 127.53 ? 164 SER C CA  1 
ATOM 4527 C C   . SER C 1 164 ? -34.295 19.632  -32.002 1.00 131.62 ? 164 SER C C   1 
ATOM 4528 O O   . SER C 1 164 ? -34.448 20.640  -32.698 1.00 129.43 ? 164 SER C O   1 
ATOM 4529 C CB  . SER C 1 164 ? -36.020 17.931  -31.344 1.00 129.18 ? 164 SER C CB  1 
ATOM 4530 O OG  . SER C 1 164 ? -36.598 18.044  -32.633 1.00 127.17 ? 164 SER C OG  1 
ATOM 4531 N N   . TRP C 1 165 ? -33.244 18.827  -32.118 1.00 135.44 ? 165 TRP C N   1 
ATOM 4532 C CA  . TRP C 1 165 ? -32.205 19.068  -33.112 1.00 131.58 ? 165 TRP C CA  1 
ATOM 4533 C C   . TRP C 1 165 ? -31.844 17.778  -33.843 1.00 130.33 ? 165 TRP C C   1 
ATOM 4534 O O   . TRP C 1 165 ? -31.484 16.779  -33.218 1.00 128.42 ? 165 TRP C O   1 
ATOM 4535 C CB  . TRP C 1 165 ? -30.958 19.668  -32.458 1.00 132.05 ? 165 TRP C CB  1 
ATOM 4536 C CG  . TRP C 1 165 ? -30.986 21.165  -32.364 1.00 126.68 ? 165 TRP C CG  1 
ATOM 4537 C CD1 . TRP C 1 165 ? -31.534 21.912  -31.363 1.00 126.09 ? 165 TRP C CD1 1 
ATOM 4538 C CD2 . TRP C 1 165 ? -30.450 22.097  -33.313 1.00 129.20 ? 165 TRP C CD2 1 
ATOM 4539 N NE1 . TRP C 1 165 ? -31.369 23.251  -31.625 1.00 128.19 ? 165 TRP C NE1 1 
ATOM 4540 C CE2 . TRP C 1 165 ? -30.705 23.391  -32.816 1.00 127.29 ? 165 TRP C CE2 1 
ATOM 4541 C CE3 . TRP C 1 165 ? -29.777 21.962  -34.531 1.00 127.25 ? 165 TRP C CE3 1 
ATOM 4542 C CZ2 . TRP C 1 165 ? -30.314 24.542  -33.496 1.00 121.48 ? 165 TRP C CZ2 1 
ATOM 4543 C CZ3 . TRP C 1 165 ? -29.388 23.108  -35.204 1.00 122.30 ? 165 TRP C CZ3 1 
ATOM 4544 C CH2 . TRP C 1 165 ? -29.658 24.380  -34.686 1.00 119.30 ? 165 TRP C CH2 1 
ATOM 4545 N N   . SER C 1 172 ? -25.644 16.716  -28.437 1.00 132.65 ? 172 SER C N   1 
ATOM 4546 C CA  . SER C 1 172 ? -24.360 17.087  -27.856 1.00 132.29 ? 172 SER C CA  1 
ATOM 4547 C C   . SER C 1 172 ? -24.268 18.596  -27.649 1.00 135.33 ? 172 SER C C   1 
ATOM 4548 O O   . SER C 1 172 ? -24.175 19.359  -28.610 1.00 134.17 ? 172 SER C O   1 
ATOM 4549 C CB  . SER C 1 172 ? -23.210 16.606  -28.744 1.00 130.49 ? 172 SER C CB  1 
ATOM 4550 O OG  . SER C 1 172 ? -23.417 16.981  -30.096 1.00 127.51 ? 172 SER C OG  1 
ATOM 4551 N N   . GLY C 1 173 ? -24.295 19.020  -26.388 1.00 145.51 ? 173 GLY C N   1 
ATOM 4552 C CA  . GLY C 1 173 ? -24.214 20.433  -26.074 1.00 148.45 ? 173 GLY C CA  1 
ATOM 4553 C C   . GLY C 1 173 ? -25.439 21.233  -26.457 1.00 154.24 ? 173 GLY C C   1 
ATOM 4554 O O   . GLY C 1 173 ? -25.329 22.434  -26.721 1.00 157.62 ? 173 GLY C O   1 
ATOM 4555 N N   . VAL C 1 174 ? -26.607 20.599  -26.494 1.00 146.94 ? 174 VAL C N   1 
ATOM 4556 C CA  . VAL C 1 174 ? -27.849 21.270  -26.862 1.00 141.86 ? 174 VAL C CA  1 
ATOM 4557 C C   . VAL C 1 174 ? -28.448 21.882  -25.600 1.00 148.88 ? 174 VAL C C   1 
ATOM 4558 O O   . VAL C 1 174 ? -28.908 21.166  -24.708 1.00 144.70 ? 174 VAL C O   1 
ATOM 4559 C CB  . VAL C 1 174 ? -28.833 20.305  -27.533 1.00 133.64 ? 174 VAL C CB  1 
ATOM 4560 C CG1 . VAL C 1 174 ? -30.122 21.028  -27.893 1.00 129.23 ? 174 VAL C CG1 1 
ATOM 4561 C CG2 . VAL C 1 174 ? -28.202 19.687  -28.771 1.00 132.13 ? 174 VAL C CG2 1 
ATOM 4562 N N   . HIS C 1 175 ? -28.441 23.211  -25.526 1.00 149.95 ? 175 HIS C N   1 
ATOM 4563 C CA  . HIS C 1 175 ? -29.013 23.950  -24.408 1.00 150.63 ? 175 HIS C CA  1 
ATOM 4564 C C   . HIS C 1 175 ? -30.286 24.638  -24.878 1.00 153.96 ? 175 HIS C C   1 
ATOM 4565 O O   . HIS C 1 175 ? -30.239 25.498  -25.765 1.00 148.66 ? 175 HIS C O   1 
ATOM 4566 C CB  . HIS C 1 175 ? -28.026 24.982  -23.861 1.00 145.39 ? 175 HIS C CB  1 
ATOM 4567 C CG  . HIS C 1 175 ? -26.737 24.395  -23.375 1.00 148.89 ? 175 HIS C CG  1 
ATOM 4568 N ND1 . HIS C 1 175 ? -26.529 24.039  -22.060 1.00 152.33 ? 175 HIS C ND1 1 
ATOM 4569 C CD2 . HIS C 1 175 ? -25.584 24.115  -24.028 1.00 148.87 ? 175 HIS C CD2 1 
ATOM 4570 C CE1 . HIS C 1 175 ? -25.306 23.556  -21.925 1.00 148.94 ? 175 HIS C CE1 1 
ATOM 4571 N NE2 . HIS C 1 175 ? -24.712 23.592  -23.104 1.00 150.75 ? 175 HIS C NE2 1 
ATOM 4572 N N   . THR C 1 176 ? -31.417 24.262  -24.289 1.00 161.27 ? 176 THR C N   1 
ATOM 4573 C CA  . THR C 1 176 ? -32.700 24.901  -24.571 1.00 157.09 ? 176 THR C CA  1 
ATOM 4574 C C   . THR C 1 176 ? -32.999 25.856  -23.420 1.00 151.79 ? 176 THR C C   1 
ATOM 4575 O O   . THR C 1 176 ? -33.399 25.431  -22.335 1.00 150.73 ? 176 THR C O   1 
ATOM 4576 C CB  . THR C 1 176 ? -33.805 23.863  -24.746 1.00 156.11 ? 176 THR C CB  1 
ATOM 4577 O OG1 . THR C 1 176 ? -33.398 22.887  -25.714 1.00 146.98 ? 176 THR C OG1 1 
ATOM 4578 C CG2 . THR C 1 176 ? -35.087 24.532  -25.216 1.00 153.33 ? 176 THR C CG2 1 
ATOM 4579 N N   . PHE C 1 177 ? -32.803 27.149  -23.660 1.00 138.51 ? 177 PHE C N   1 
ATOM 4580 C CA  . PHE C 1 177 ? -32.909 28.129  -22.592 1.00 123.98 ? 177 PHE C CA  1 
ATOM 4581 C C   . PHE C 1 177 ? -34.363 28.308  -22.153 1.00 115.08 ? 177 PHE C C   1 
ATOM 4582 O O   . PHE C 1 177 ? -35.289 28.148  -22.953 1.00 117.70 ? 177 PHE C O   1 
ATOM 4583 C CB  . PHE C 1 177 ? -32.324 29.466  -23.036 1.00 123.49 ? 177 PHE C CB  1 
ATOM 4584 C CG  . PHE C 1 177 ? -30.846 29.420  -23.297 1.00 125.61 ? 177 PHE C CG  1 
ATOM 4585 C CD1 . PHE C 1 177 ? -30.351 29.068  -24.541 1.00 129.22 ? 177 PHE C CD1 1 
ATOM 4586 C CD2 . PHE C 1 177 ? -29.949 29.729  -22.287 1.00 123.78 ? 177 PHE C CD2 1 
ATOM 4587 C CE1 . PHE C 1 177 ? -28.992 29.028  -24.772 1.00 122.81 ? 177 PHE C CE1 1 
ATOM 4588 C CE2 . PHE C 1 177 ? -28.589 29.691  -22.512 1.00 124.49 ? 177 PHE C CE2 1 
ATOM 4589 C CZ  . PHE C 1 177 ? -28.109 29.340  -23.757 1.00 124.27 ? 177 PHE C CZ  1 
ATOM 4590 N N   . PRO C 1 178 ? -34.587 28.634  -20.879 1.00 111.78 ? 178 PRO C N   1 
ATOM 4591 C CA  . PRO C 1 178 ? -35.957 28.794  -20.372 1.00 109.18 ? 178 PRO C CA  1 
ATOM 4592 C C   . PRO C 1 178 ? -36.735 29.862  -21.132 1.00 113.89 ? 178 PRO C C   1 
ATOM 4593 O O   . PRO C 1 178 ? -36.168 30.783  -21.720 1.00 116.99 ? 178 PRO C O   1 
ATOM 4594 C CB  . PRO C 1 178 ? -35.739 29.209  -18.911 1.00 100.59 ? 178 PRO C CB  1 
ATOM 4595 C CG  . PRO C 1 178 ? -34.433 28.580  -18.547 1.00 109.36 ? 178 PRO C CG  1 
ATOM 4596 C CD  . PRO C 1 178 ? -33.590 28.669  -19.792 1.00 115.82 ? 178 PRO C CD  1 
ATOM 4597 N N   . ALA C 1 179 ? -38.063 29.735  -21.094 1.00 118.86 ? 179 ALA C N   1 
ATOM 4598 C CA  . ALA C 1 179 ? -38.958 30.617  -21.838 1.00 120.23 ? 179 ALA C CA  1 
ATOM 4599 C C   . ALA C 1 179 ? -39.077 31.994  -21.182 1.00 121.03 ? 179 ALA C C   1 
ATOM 4600 O O   . ALA C 1 179 ? -38.889 32.144  -19.972 1.00 107.13 ? 179 ALA C O   1 
ATOM 4601 C CB  . ALA C 1 179 ? -40.343 29.976  -21.966 1.00 117.24 ? 179 ALA C CB  1 
ATOM 4602 N N   . VAL C 1 180 ? -39.364 33.008  -22.004 1.00 130.77 ? 180 VAL C N   1 
ATOM 4603 C CA  . VAL C 1 180 ? -39.570 34.376  -21.532 1.00 130.03 ? 180 VAL C CA  1 
ATOM 4604 C C   . VAL C 1 180 ? -40.848 34.948  -22.141 1.00 129.07 ? 180 VAL C C   1 
ATOM 4605 O O   . VAL C 1 180 ? -40.904 35.288  -23.327 1.00 129.32 ? 180 VAL C O   1 
ATOM 4606 C CB  . VAL C 1 180 ? -38.372 35.310  -21.773 1.00 130.33 ? 180 VAL C CB  1 
ATOM 4607 C CG1 . VAL C 1 180 ? -37.266 34.992  -20.752 1.00 129.93 ? 180 VAL C CG1 1 
ATOM 4608 C CG2 . VAL C 1 180 ? -37.881 35.271  -23.244 1.00 132.10 ? 180 VAL C CG2 1 
ATOM 4609 N N   . LEU C 1 181 ? -41.871 35.052  -21.313 1.00 110.17 ? 181 LEU C N   1 
ATOM 4610 C CA  . LEU C 1 181 ? -43.086 35.812  -21.550 1.00 109.69 ? 181 LEU C CA  1 
ATOM 4611 C C   . LEU C 1 181 ? -42.756 37.284  -21.741 1.00 111.97 ? 181 LEU C C   1 
ATOM 4612 O O   . LEU C 1 181 ? -42.264 37.953  -20.827 1.00 114.67 ? 181 LEU C O   1 
ATOM 4613 C CB  . LEU C 1 181 ? -44.073 35.608  -20.387 1.00 100.26 ? 181 LEU C CB  1 
ATOM 4614 C CG  . LEU C 1 181 ? -45.426 36.266  -20.479 1.00 100.93 ? 181 LEU C CG  1 
ATOM 4615 C CD1 . LEU C 1 181 ? -46.510 35.283  -20.100 1.00 98.33  ? 181 LEU C CD1 1 
ATOM 4616 C CD2 . LEU C 1 181 ? -45.401 37.454  -19.518 1.00 111.59 ? 181 LEU C CD2 1 
ATOM 4617 N N   . GLN C 1 182 ? -42.996 37.787  -22.944 1.00 111.93 ? 182 GLN C N   1 
ATOM 4618 C CA  . GLN C 1 182 ? -42.702 39.176  -23.237 1.00 106.25 ? 182 GLN C CA  1 
ATOM 4619 C C   . GLN C 1 182 ? -43.780 40.058  -22.613 1.00 100.05 ? 182 GLN C C   1 
ATOM 4620 O O   . GLN C 1 182 ? -44.724 39.583  -21.974 1.00 97.85  ? 182 GLN C O   1 
ATOM 4621 C CB  . GLN C 1 182 ? -42.556 39.380  -24.750 1.00 107.48 ? 182 GLN C CB  1 
ATOM 4622 C CG  . GLN C 1 182 ? -41.341 38.650  -25.358 1.00 109.79 ? 182 GLN C CG  1 
ATOM 4623 C CD  . GLN C 1 182 ? -41.043 39.026  -26.813 1.00 110.28 ? 182 GLN C CD  1 
ATOM 4624 O OE1 . GLN C 1 182 ? -39.984 38.682  -27.348 1.00 104.27 ? 182 GLN C OE1 1 
ATOM 4625 N NE2 . GLN C 1 182 ? -41.976 39.723  -27.454 1.00 114.12 ? 182 GLN C NE2 1 
ATOM 4626 N N   . SER C 1 183 ? -43.608 41.371  -22.760 1.00 96.48  ? 183 SER C N   1 
ATOM 4627 C CA  . SER C 1 183 ? -44.511 42.289  -22.078 1.00 92.56  ? 183 SER C CA  1 
ATOM 4628 C C   . SER C 1 183 ? -45.937 42.095  -22.563 1.00 91.91  ? 183 SER C C   1 
ATOM 4629 O O   . SER C 1 183 ? -46.892 42.283  -21.800 1.00 87.35  ? 183 SER C O   1 
ATOM 4630 C CB  . SER C 1 183 ? -44.065 43.734  -22.294 1.00 86.88  ? 183 SER C CB  1 
ATOM 4631 O OG  . SER C 1 183 ? -43.833 43.994  -23.665 1.00 84.30  ? 183 SER C OG  1 
ATOM 4632 N N   . SER C 1 184 ? -46.098 41.693  -23.824 1.00 92.14  ? 184 SER C N   1 
ATOM 4633 C CA  . SER C 1 184 ? -47.431 41.526  -24.389 1.00 88.58  ? 184 SER C CA  1 
ATOM 4634 C C   . SER C 1 184 ? -48.197 40.428  -23.668 1.00 93.73  ? 184 SER C C   1 
ATOM 4635 O O   . SER C 1 184 ? -49.401 40.560  -23.418 1.00 90.20  ? 184 SER C O   1 
ATOM 4636 C CB  . SER C 1 184 ? -47.326 41.208  -25.879 1.00 90.71  ? 184 SER C CB  1 
ATOM 4637 O OG  . SER C 1 184 ? -46.244 40.326  -26.123 1.00 90.45  ? 184 SER C OG  1 
ATOM 4638 N N   . GLY C 1 185 ? -47.513 39.346  -23.315 1.00 98.35  ? 185 GLY C N   1 
ATOM 4639 C CA  . GLY C 1 185 ? -48.159 38.201  -22.709 1.00 92.00  ? 185 GLY C CA  1 
ATOM 4640 C C   . GLY C 1 185 ? -47.834 36.938  -23.474 1.00 92.39  ? 185 GLY C C   1 
ATOM 4641 O O   . GLY C 1 185 ? -48.433 35.884  -23.245 1.00 89.31  ? 185 GLY C O   1 
ATOM 4642 N N   . LEU C 1 186 ? -46.871 37.042  -24.385 1.00 100.86 ? 186 LEU C N   1 
ATOM 4643 C CA  . LEU C 1 186 ? -46.487 35.956  -25.275 1.00 107.29 ? 186 LEU C CA  1 
ATOM 4644 C C   . LEU C 1 186 ? -45.039 35.575  -25.008 1.00 111.06 ? 186 LEU C C   1 
ATOM 4645 O O   . LEU C 1 186 ? -44.164 36.446  -24.936 1.00 112.33 ? 186 LEU C O   1 
ATOM 4646 C CB  . LEU C 1 186 ? -46.676 36.365  -26.738 1.00 114.52 ? 186 LEU C CB  1 
ATOM 4647 C CG  . LEU C 1 186 ? -47.912 37.224  -27.024 1.00 102.78 ? 186 LEU C CG  1 
ATOM 4648 C CD1 . LEU C 1 186 ? -47.728 38.040  -28.296 1.00 114.12 ? 186 LEU C CD1 1 
ATOM 4649 C CD2 . LEU C 1 186 ? -49.157 36.360  -27.115 1.00 98.64  ? 186 LEU C CD2 1 
ATOM 4650 N N   . TYR C 1 187 ? -44.792 34.276  -24.864 1.00 117.12 ? 187 TYR C N   1 
ATOM 4651 C CA  . TYR C 1 187 ? -43.458 33.772  -24.577 1.00 121.80 ? 187 TYR C CA  1 
ATOM 4652 C C   . TYR C 1 187 ? -42.587 33.778  -25.832 1.00 128.95 ? 187 TYR C C   1 
ATOM 4653 O O   . TYR C 1 187 ? -43.075 33.835  -26.963 1.00 137.16 ? 187 TYR C O   1 
ATOM 4654 C CB  . TYR C 1 187 ? -43.521 32.352  -24.003 1.00 119.36 ? 187 TYR C CB  1 
ATOM 4655 C CG  . TYR C 1 187 ? -44.454 32.174  -22.820 1.00 106.18 ? 187 TYR C CG  1 
ATOM 4656 C CD1 . TYR C 1 187 ? -45.816 31.973  -23.004 1.00 101.29 ? 187 TYR C CD1 1 
ATOM 4657 C CD2 . TYR C 1 187 ? -43.966 32.188  -21.518 1.00 102.06 ? 187 TYR C CD2 1 
ATOM 4658 C CE1 . TYR C 1 187 ? -46.668 31.805  -21.925 1.00 94.33  ? 187 TYR C CE1 1 
ATOM 4659 C CE2 . TYR C 1 187 ? -44.813 32.019  -20.435 1.00 95.23  ? 187 TYR C CE2 1 
ATOM 4660 C CZ  . TYR C 1 187 ? -46.161 31.827  -20.645 1.00 88.04  ? 187 TYR C CZ  1 
ATOM 4661 O OH  . TYR C 1 187 ? -47.004 31.660  -19.571 1.00 78.17  ? 187 TYR C OH  1 
ATOM 4662 N N   . SER C 1 188 ? -41.276 33.718  -25.610 1.00 124.29 ? 188 SER C N   1 
ATOM 4663 C CA  . SER C 1 188 ? -40.295 33.581  -26.675 1.00 130.70 ? 188 SER C CA  1 
ATOM 4664 C C   . SER C 1 188 ? -39.113 32.827  -26.084 1.00 132.60 ? 188 SER C C   1 
ATOM 4665 O O   . SER C 1 188 ? -38.985 32.729  -24.861 1.00 125.43 ? 188 SER C O   1 
ATOM 4666 C CB  . SER C 1 188 ? -39.883 34.951  -27.235 1.00 130.17 ? 188 SER C CB  1 
ATOM 4667 O OG  . SER C 1 188 ? -38.786 34.860  -28.126 1.00 134.22 ? 188 SER C OG  1 
ATOM 4668 N N   . LEU C 1 189 ? -38.260 32.276  -26.945 1.00 134.44 ? 189 LEU C N   1 
ATOM 4669 C CA  . LEU C 1 189 ? -37.133 31.496  -26.446 1.00 133.51 ? 189 LEU C CA  1 
ATOM 4670 C C   . LEU C 1 189 ? -36.106 31.279  -27.548 1.00 143.65 ? 189 LEU C C   1 
ATOM 4671 O O   . LEU C 1 189 ? -36.363 31.505  -28.732 1.00 146.09 ? 189 LEU C O   1 
ATOM 4672 C CB  . LEU C 1 189 ? -37.601 30.152  -25.869 1.00 127.65 ? 189 LEU C CB  1 
ATOM 4673 C CG  . LEU C 1 189 ? -38.117 28.998  -26.741 1.00 134.23 ? 189 LEU C CG  1 
ATOM 4674 C CD1 . LEU C 1 189 ? -37.022 28.090  -27.354 1.00 140.32 ? 189 LEU C CD1 1 
ATOM 4675 C CD2 . LEU C 1 189 ? -39.132 28.208  -25.931 1.00 124.21 ? 189 LEU C CD2 1 
ATOM 4676 N N   . SER C 1 190 ? -34.935 30.808  -27.131 1.00 152.86 ? 190 SER C N   1 
ATOM 4677 C CA  . SER C 1 190 ? -33.849 30.493  -28.040 1.00 150.77 ? 190 SER C CA  1 
ATOM 4678 C C   . SER C 1 190 ? -33.270 29.136  -27.678 1.00 150.07 ? 190 SER C C   1 
ATOM 4679 O O   . SER C 1 190 ? -33.167 28.787  -26.497 1.00 151.84 ? 190 SER C O   1 
ATOM 4680 C CB  . SER C 1 190 ? -32.757 31.562  -27.991 1.00 148.41 ? 190 SER C CB  1 
ATOM 4681 O OG  . SER C 1 190 ? -32.522 31.992  -26.661 1.00 143.70 ? 190 SER C OG  1 
ATOM 4682 N N   . SER C 1 191 ? -32.894 28.376  -28.702 1.00 142.44 ? 191 SER C N   1 
ATOM 4683 C CA  . SER C 1 191 ? -32.295 27.061  -28.530 1.00 135.96 ? 191 SER C CA  1 
ATOM 4684 C C   . SER C 1 191 ? -30.994 27.002  -29.315 1.00 130.94 ? 191 SER C C   1 
ATOM 4685 O O   . SER C 1 191 ? -30.971 27.312  -30.511 1.00 128.80 ? 191 SER C O   1 
ATOM 4686 C CB  . SER C 1 191 ? -33.248 25.954  -28.991 1.00 130.69 ? 191 SER C CB  1 
ATOM 4687 O OG  . SER C 1 191 ? -32.593 24.699  -29.010 1.00 129.25 ? 191 SER C OG  1 
ATOM 4688 N N   . VAL C 1 192 ? -29.919 26.598  -28.647 1.00 126.88 ? 192 VAL C N   1 
ATOM 4689 C CA  . VAL C 1 192 ? -28.606 26.551  -29.280 1.00 123.22 ? 192 VAL C CA  1 
ATOM 4690 C C   . VAL C 1 192 ? -27.984 25.163  -29.156 1.00 123.41 ? 192 VAL C C   1 
ATOM 4691 O O   . VAL C 1 192 ? -28.352 24.379  -28.281 1.00 131.04 ? 192 VAL C O   1 
ATOM 4692 C CB  . VAL C 1 192 ? -27.670 27.617  -28.684 1.00 124.55 ? 192 VAL C CB  1 
ATOM 4693 C CG1 . VAL C 1 192 ? -27.298 27.258  -27.254 1.00 126.79 ? 192 VAL C CG1 1 
ATOM 4694 C CG2 . VAL C 1 192 ? -26.427 27.774  -29.547 1.00 120.94 ? 192 VAL C CG2 1 
ATOM 4695 N N   . CYS C 1 207 ? -33.011 22.328  -37.095 1.00 123.21 ? 207 CYS C N   1 
ATOM 4696 C CA  . CYS C 1 207 ? -33.713 22.210  -35.822 1.00 129.26 ? 207 CYS C CA  1 
ATOM 4697 C C   . CYS C 1 207 ? -35.224 22.124  -36.024 1.00 130.30 ? 207 CYS C C   1 
ATOM 4698 O O   . CYS C 1 207 ? -35.786 22.787  -36.897 1.00 129.56 ? 207 CYS C O   1 
ATOM 4699 C CB  . CYS C 1 207 ? -33.351 23.385  -34.905 1.00 125.65 ? 207 CYS C CB  1 
ATOM 4700 S SG  . CYS C 1 207 ? -34.462 24.817  -34.949 1.00 111.12 ? 207 CYS C SG  1 
ATOM 4701 N N   . ASN C 1 208 ? -35.875 21.290  -35.217 1.00 128.27 ? 208 ASN C N   1 
ATOM 4702 C CA  . ASN C 1 208 ? -37.311 21.059  -35.305 1.00 128.58 ? 208 ASN C CA  1 
ATOM 4703 C C   . ASN C 1 208 ? -37.986 21.619  -34.061 1.00 129.83 ? 208 ASN C C   1 
ATOM 4704 O O   . ASN C 1 208 ? -37.749 21.134  -32.949 1.00 128.60 ? 208 ASN C O   1 
ATOM 4705 C CB  . ASN C 1 208 ? -37.622 19.569  -35.455 1.00 128.60 ? 208 ASN C CB  1 
ATOM 4706 C CG  . ASN C 1 208 ? -36.551 18.823  -36.223 1.00 128.81 ? 208 ASN C CG  1 
ATOM 4707 O OD1 . ASN C 1 208 ? -35.734 18.112  -35.638 1.00 131.85 ? 208 ASN C OD1 1 
ATOM 4708 N ND2 . ASN C 1 208 ? -36.551 18.979  -37.542 1.00 122.51 ? 208 ASN C ND2 1 
ATOM 4709 N N   . VAL C 1 209 ? -38.821 22.634  -34.252 1.00 129.93 ? 209 VAL C N   1 
ATOM 4710 C CA  . VAL C 1 209 ? -39.636 23.204  -33.186 1.00 127.22 ? 209 VAL C CA  1 
ATOM 4711 C C   . VAL C 1 209 ? -41.063 22.709  -33.360 1.00 127.74 ? 209 VAL C C   1 
ATOM 4712 O O   . VAL C 1 209 ? -41.600 22.705  -34.475 1.00 128.95 ? 209 VAL C O   1 
ATOM 4713 C CB  . VAL C 1 209 ? -39.577 24.743  -33.196 1.00 121.50 ? 209 VAL C CB  1 
ATOM 4714 C CG1 . VAL C 1 209 ? -40.378 25.313  -32.036 1.00 125.01 ? 209 VAL C CG1 1 
ATOM 4715 C CG2 . VAL C 1 209 ? -38.133 25.217  -33.140 1.00 118.10 ? 209 VAL C CG2 1 
ATOM 4716 N N   . ASN C 1 210 ? -41.681 22.283  -32.259 1.00 123.00 ? 210 ASN C N   1 
ATOM 4717 C CA  . ASN C 1 210 ? -43.034 21.738  -32.280 1.00 120.20 ? 210 ASN C CA  1 
ATOM 4718 C C   . ASN C 1 210 ? -43.894 22.494  -31.276 1.00 119.18 ? 210 ASN C C   1 
ATOM 4719 O O   . ASN C 1 210 ? -43.731 22.327  -30.063 1.00 119.57 ? 210 ASN C O   1 
ATOM 4720 C CB  . ASN C 1 210 ? -43.029 20.240  -31.972 1.00 123.82 ? 210 ASN C CB  1 
ATOM 4721 C CG  . ASN C 1 210 ? -44.173 19.506  -32.640 1.00 123.00 ? 210 ASN C CG  1 
ATOM 4722 O OD1 . ASN C 1 210 ? -45.021 20.117  -33.290 1.00 121.81 ? 210 ASN C OD1 1 
ATOM 4723 N ND2 . ASN C 1 210 ? -44.205 18.188  -32.483 1.00 118.01 ? 210 ASN C ND2 1 
ATOM 4724 N N   . HIS C 1 211 ? -44.805 23.322  -31.782 1.00 121.68 ? 211 HIS C N   1 
ATOM 4725 C CA  . HIS C 1 211 ? -45.800 24.012  -30.963 1.00 116.00 ? 211 HIS C CA  1 
ATOM 4726 C C   . HIS C 1 211 ? -47.109 23.242  -31.094 1.00 116.81 ? 211 HIS C C   1 
ATOM 4727 O O   . HIS C 1 211 ? -47.803 23.344  -32.109 1.00 116.82 ? 211 HIS C O   1 
ATOM 4728 C CB  . HIS C 1 211 ? -45.958 25.464  -31.398 1.00 113.91 ? 211 HIS C CB  1 
ATOM 4729 C CG  . HIS C 1 211 ? -46.644 26.328  -30.386 1.00 112.71 ? 211 HIS C CG  1 
ATOM 4730 N ND1 . HIS C 1 211 ? -47.902 26.049  -29.897 1.00 108.54 ? 211 HIS C ND1 1 
ATOM 4731 C CD2 . HIS C 1 211 ? -46.249 27.470  -29.776 1.00 116.09 ? 211 HIS C CD2 1 
ATOM 4732 C CE1 . HIS C 1 211 ? -48.251 26.980  -29.027 1.00 108.52 ? 211 HIS C CE1 1 
ATOM 4733 N NE2 . HIS C 1 211 ? -47.266 27.855  -28.936 1.00 111.05 ? 211 HIS C NE2 1 
ATOM 4734 N N   . LYS C 1 212 ? -47.448 22.467  -30.058 1.00 117.47 ? 212 LYS C N   1 
ATOM 4735 C CA  . LYS C 1 212 ? -48.625 21.605  -30.152 1.00 115.01 ? 212 LYS C CA  1 
ATOM 4736 C C   . LYS C 1 212 ? -49.931 22.393  -30.119 1.00 113.90 ? 212 LYS C C   1 
ATOM 4737 O O   . LYS C 1 212 ? -50.798 22.137  -30.973 1.00 111.83 ? 212 LYS C O   1 
ATOM 4738 C CB  . LYS C 1 212 ? -48.574 20.530  -29.062 1.00 114.86 ? 212 LYS C CB  1 
ATOM 4739 C CG  . LYS C 1 212 ? -47.319 19.672  -29.093 1.00 121.39 ? 212 LYS C CG  1 
ATOM 4740 C CD  . LYS C 1 212 ? -46.814 19.362  -27.691 1.00 125.00 ? 212 LYS C CD  1 
ATOM 4741 C CE  . LYS C 1 212 ? -46.402 20.624  -26.950 1.00 117.90 ? 212 LYS C CE  1 
ATOM 4742 N NZ  . LYS C 1 212 ? -45.918 20.321  -25.574 1.00 109.01 ? 212 LYS C NZ  1 
ATOM 4743 N N   . PRO C 1 213 ? -50.153 23.336  -29.194 1.00 114.47 ? 213 PRO C N   1 
ATOM 4744 C CA  . PRO C 1 213 ? -51.433 24.065  -29.207 1.00 111.53 ? 213 PRO C CA  1 
ATOM 4745 C C   . PRO C 1 213 ? -51.645 24.910  -30.450 1.00 111.41 ? 213 PRO C C   1 
ATOM 4746 O O   . PRO C 1 213 ? -52.793 25.252  -30.757 1.00 103.77 ? 213 PRO C O   1 
ATOM 4747 C CB  . PRO C 1 213 ? -51.346 24.940  -27.953 1.00 99.83  ? 213 PRO C CB  1 
ATOM 4748 C CG  . PRO C 1 213 ? -50.460 24.184  -27.044 1.00 101.09 ? 213 PRO C CG  1 
ATOM 4749 C CD  . PRO C 1 213 ? -49.410 23.599  -27.947 1.00 109.36 ? 213 PRO C CD  1 
ATOM 4750 N N   . SER C 1 214 ? -50.583 25.269  -31.169 1.00 110.16 ? 214 SER C N   1 
ATOM 4751 C CA  . SER C 1 214 ? -50.708 26.046  -32.395 1.00 108.28 ? 214 SER C CA  1 
ATOM 4752 C C   . SER C 1 214 ? -50.743 25.186  -33.649 1.00 118.17 ? 214 SER C C   1 
ATOM 4753 O O   . SER C 1 214 ? -50.937 25.729  -34.743 1.00 120.10 ? 214 SER C O   1 
ATOM 4754 C CB  . SER C 1 214 ? -49.558 27.051  -32.512 1.00 110.61 ? 214 SER C CB  1 
ATOM 4755 O OG  . SER C 1 214 ? -49.688 27.821  -33.694 1.00 114.34 ? 214 SER C OG  1 
ATOM 4756 N N   . ASN C 1 215 ? -50.568 23.870  -33.517 1.00 133.99 ? 215 ASN C N   1 
ATOM 4757 C CA  . ASN C 1 215 ? -50.488 22.958  -34.659 1.00 132.79 ? 215 ASN C CA  1 
ATOM 4758 C C   . ASN C 1 215 ? -49.401 23.404  -35.635 1.00 135.59 ? 215 ASN C C   1 
ATOM 4759 O O   . ASN C 1 215 ? -49.588 23.408  -36.854 1.00 132.52 ? 215 ASN C O   1 
ATOM 4760 C CB  . ASN C 1 215 ? -51.842 22.830  -35.362 1.00 129.90 ? 215 ASN C CB  1 
ATOM 4761 C CG  . ASN C 1 215 ? -51.998 21.507  -36.087 1.00 136.46 ? 215 ASN C CG  1 
ATOM 4762 O OD1 . ASN C 1 215 ? -51.047 20.735  -36.205 1.00 140.16 ? 215 ASN C OD1 1 
ATOM 4763 N ND2 . ASN C 1 215 ? -53.205 21.238  -36.574 1.00 138.59 ? 215 ASN C ND2 1 
ATOM 4764 N N   . THR C 1 216 ? -48.252 23.787  -35.087 1.00 127.57 ? 216 THR C N   1 
ATOM 4765 C CA  . THR C 1 216 ? -47.134 24.265  -35.890 1.00 119.29 ? 216 THR C CA  1 
ATOM 4766 C C   . THR C 1 216 ? -45.895 23.402  -35.672 1.00 114.28 ? 216 THR C C   1 
ATOM 4767 O O   . THR C 1 216 ? -45.227 23.505  -34.644 1.00 119.13 ? 216 THR C O   1 
ATOM 4768 C CB  . THR C 1 216 ? -46.798 25.733  -35.565 1.00 117.10 ? 216 THR C CB  1 
ATOM 4769 O OG1 . THR C 1 216 ? -48.011 26.480  -35.406 1.00 120.39 ? 216 THR C OG1 1 
ATOM 4770 C CG2 . THR C 1 216 ? -45.970 26.353  -36.677 1.00 113.51 ? 216 THR C CG2 1 
ATOM 4771 N N   . ASP D 2 1   ? -55.303 18.799  7.418   1.00 86.61  ? 1   ASP D N   1 
ATOM 4772 C CA  . ASP D 2 1   ? -54.883 20.152  7.765   1.00 83.36  ? 1   ASP D CA  1 
ATOM 4773 C C   . ASP D 2 1   ? -53.459 20.171  8.316   1.00 79.79  ? 1   ASP D C   1 
ATOM 4774 O O   . ASP D 2 1   ? -53.022 21.166  8.893   1.00 81.70  ? 1   ASP D O   1 
ATOM 4775 C CB  . ASP D 2 1   ? -55.851 20.770  8.778   1.00 83.21  ? 1   ASP D CB  1 
ATOM 4776 C CG  . ASP D 2 1   ? -56.392 19.753  9.763   1.00 98.32  ? 1   ASP D CG  1 
ATOM 4777 O OD1 . ASP D 2 1   ? -55.645 18.821  10.131  1.00 92.92  ? 1   ASP D OD1 1 
ATOM 4778 O OD2 . ASP D 2 1   ? -57.562 19.892  10.177  1.00 104.94 ? 1   ASP D OD2 1 
ATOM 4779 N N   . ILE D 2 2   ? -52.739 19.063  8.135   1.00 76.00  ? 2   ILE D N   1 
ATOM 4780 C CA  . ILE D 2 2   ? -51.346 19.001  8.557   1.00 74.86  ? 2   ILE D CA  1 
ATOM 4781 C C   . ILE D 2 2   ? -50.515 19.949  7.704   1.00 71.31  ? 2   ILE D C   1 
ATOM 4782 O O   . ILE D 2 2   ? -50.657 19.997  6.476   1.00 73.19  ? 2   ILE D O   1 
ATOM 4783 C CB  . ILE D 2 2   ? -50.818 17.558  8.468   1.00 77.83  ? 2   ILE D CB  1 
ATOM 4784 C CG1 . ILE D 2 2   ? -51.478 16.685  9.536   1.00 79.09  ? 2   ILE D CG1 1 
ATOM 4785 C CG2 . ILE D 2 2   ? -49.301 17.525  8.608   1.00 70.66  ? 2   ILE D CG2 1 
ATOM 4786 C CD1 . ILE D 2 2   ? -50.853 15.316  9.681   1.00 69.89  ? 2   ILE D CD1 1 
ATOM 4787 N N   . VAL D 2 3   ? -49.652 20.723  8.357   1.00 71.65  ? 3   VAL D N   1 
ATOM 4788 C CA  . VAL D 2 3   ? -48.740 21.641  7.686   1.00 67.88  ? 3   VAL D CA  1 
ATOM 4789 C C   . VAL D 2 3   ? -47.322 21.140  7.917   1.00 67.98  ? 3   VAL D C   1 
ATOM 4790 O O   . VAL D 2 3   ? -46.951 20.810  9.049   1.00 71.77  ? 3   VAL D O   1 
ATOM 4791 C CB  . VAL D 2 3   ? -48.916 23.082  8.195   1.00 63.99  ? 3   VAL D CB  1 
ATOM 4792 C CG1 . VAL D 2 3   ? -48.041 24.038  7.402   1.00 63.19  ? 3   VAL D CG1 1 
ATOM 4793 C CG2 . VAL D 2 3   ? -50.381 23.497  8.119   1.00 64.98  ? 3   VAL D CG2 1 
ATOM 4794 N N   . MET D 2 4   ? -46.534 21.071  6.847   1.00 67.81  ? 4   MET D N   1 
ATOM 4795 C CA  . MET D 2 4   ? -45.180 20.530  6.914   1.00 70.30  ? 4   MET D CA  1 
ATOM 4796 C C   . MET D 2 4   ? -44.207 21.535  6.313   1.00 70.77  ? 4   MET D C   1 
ATOM 4797 O O   . MET D 2 4   ? -44.210 21.763  5.099   1.00 81.20  ? 4   MET D O   1 
ATOM 4798 C CB  . MET D 2 4   ? -45.091 19.180  6.204   1.00 68.88  ? 4   MET D CB  1 
ATOM 4799 C CG  . MET D 2 4   ? -45.797 18.053  6.953   1.00 66.19  ? 4   MET D CG  1 
ATOM 4800 S SD  . MET D 2 4   ? -44.920 16.486  6.856   1.00 76.12  ? 4   MET D SD  1 
ATOM 4801 C CE  . MET D 2 4   ? -44.603 16.416  5.098   1.00 65.64  ? 4   MET D CE  1 
ATOM 4802 N N   . THR D 2 5   ? -43.381 22.130  7.166   1.00 66.37  ? 5   THR D N   1 
ATOM 4803 C CA  . THR D 2 5   ? -42.359 23.078  6.756   1.00 71.05  ? 5   THR D CA  1 
ATOM 4804 C C   . THR D 2 5   ? -41.000 22.395  6.706   1.00 67.07  ? 5   THR D C   1 
ATOM 4805 O O   . THR D 2 5   ? -40.725 21.466  7.468   1.00 71.74  ? 5   THR D O   1 
ATOM 4806 C CB  . THR D 2 5   ? -42.314 24.273  7.711   1.00 70.92  ? 5   THR D CB  1 
ATOM 4807 O OG1 . THR D 2 5   ? -42.245 23.804  9.064   1.00 76.34  ? 5   THR D OG1 1 
ATOM 4808 C CG2 . THR D 2 5   ? -43.554 25.132  7.541   1.00 71.02  ? 5   THR D CG2 1 
ATOM 4809 N N   . GLN D 2 6   ? -40.148 22.864  5.799   1.00 67.12  ? 6   GLN D N   1 
ATOM 4810 C CA  . GLN D 2 6   ? -38.827 22.279  5.630   1.00 65.54  ? 6   GLN D CA  1 
ATOM 4811 C C   . GLN D 2 6   ? -37.731 23.260  6.026   1.00 67.00  ? 6   GLN D C   1 
ATOM 4812 O O   . GLN D 2 6   ? -37.952 24.465  6.170   1.00 68.81  ? 6   GLN D O   1 
ATOM 4813 C CB  . GLN D 2 6   ? -38.604 21.796  4.192   1.00 61.17  ? 6   GLN D CB  1 
ATOM 4814 C CG  . GLN D 2 6   ? -39.699 20.896  3.662   1.00 58.01  ? 6   GLN D CG  1 
ATOM 4815 C CD  . GLN D 2 6   ? -39.330 20.262  2.338   1.00 59.57  ? 6   GLN D CD  1 
ATOM 4816 O OE1 . GLN D 2 6   ? -40.199 19.883  1.553   1.00 56.45  ? 6   GLN D OE1 1 
ATOM 4817 N NE2 . GLN D 2 6   ? -38.033 20.143  2.082   1.00 59.00  ? 6   GLN D NE2 1 
ATOM 4818 N N   . SER D 2 7   ? -36.531 22.707  6.191   1.00 65.17  ? 7   SER D N   1 
ATOM 4819 C CA  . SER D 2 7   ? -35.321 23.403  6.610   1.00 64.43  ? 7   SER D CA  1 
ATOM 4820 C C   . SER D 2 7   ? -34.108 22.873  5.853   1.00 66.25  ? 7   SER D C   1 
ATOM 4821 O O   . SER D 2 7   ? -33.850 21.662  5.869   1.00 73.08  ? 7   SER D O   1 
ATOM 4822 C CB  . SER D 2 7   ? -35.110 23.231  8.116   1.00 67.26  ? 7   SER D CB  1 
ATOM 4823 O OG  . SER D 2 7   ? -33.841 23.720  8.515   1.00 75.35  ? 7   SER D OG  1 
ATOM 4824 N N   . PRO D 2 8   ? -33.342 23.737  5.162   1.00 62.88  ? 8   PRO D N   1 
ATOM 4825 C CA  . PRO D 2 8   ? -33.629 25.145  4.863   1.00 69.90  ? 8   PRO D CA  1 
ATOM 4826 C C   . PRO D 2 8   ? -34.500 25.322  3.618   1.00 66.70  ? 8   PRO D C   1 
ATOM 4827 O O   . PRO D 2 8   ? -35.081 24.353  3.135   1.00 67.67  ? 8   PRO D O   1 
ATOM 4828 C CB  . PRO D 2 8   ? -32.233 25.740  4.620   1.00 76.93  ? 8   PRO D CB  1 
ATOM 4829 C CG  . PRO D 2 8   ? -31.282 24.768  5.233   1.00 72.98  ? 8   PRO D CG  1 
ATOM 4830 C CD  . PRO D 2 8   ? -31.913 23.439  4.981   1.00 67.96  ? 8   PRO D CD  1 
ATOM 4831 N N   . LEU D 2 9   ? -34.601 26.553  3.109   1.00 67.62  ? 9   LEU D N   1 
ATOM 4832 C CA  . LEU D 2 9   ? -35.247 26.756  1.816   1.00 63.06  ? 9   LEU D CA  1 
ATOM 4833 C C   . LEU D 2 9   ? -34.278 26.531  0.664   1.00 63.05  ? 9   LEU D C   1 
ATOM 4834 O O   . LEU D 2 9   ? -34.700 26.130  -0.426  1.00 65.91  ? 9   LEU D O   1 
ATOM 4835 C CB  . LEU D 2 9   ? -35.853 28.158  1.730   1.00 69.06  ? 9   LEU D CB  1 
ATOM 4836 C CG  . LEU D 2 9   ? -37.309 28.311  2.180   1.00 76.74  ? 9   LEU D CG  1 
ATOM 4837 C CD1 . LEU D 2 9   ? -38.204 27.326  1.440   1.00 63.98  ? 9   LEU D CD1 1 
ATOM 4838 C CD2 . LEU D 2 9   ? -37.436 28.123  3.681   1.00 68.68  ? 9   LEU D CD2 1 
ATOM 4839 N N   . SER D 2 10  ? -32.991 26.779  0.886   1.00 63.53  ? 10  SER D N   1 
ATOM 4840 C CA  . SER D 2 10  ? -31.962 26.541  -0.113  1.00 66.45  ? 10  SER D CA  1 
ATOM 4841 C C   . SER D 2 10  ? -30.639 26.325  0.602   1.00 73.27  ? 10  SER D C   1 
ATOM 4842 O O   . SER D 2 10  ? -30.386 26.908  1.660   1.00 77.65  ? 10  SER D O   1 
ATOM 4843 C CB  . SER D 2 10  ? -31.850 27.706  -1.105  1.00 65.95  ? 10  SER D CB  1 
ATOM 4844 O OG  . SER D 2 10  ? -30.840 27.461  -2.068  1.00 68.59  ? 10  SER D OG  1 
ATOM 4845 N N   . LEU D 2 11  ? -29.798 25.477  0.017   1.00 75.05  ? 11  LEU D N   1 
ATOM 4846 C CA  . LEU D 2 11  ? -28.494 25.177  0.588   1.00 75.92  ? 11  LEU D CA  1 
ATOM 4847 C C   . LEU D 2 11  ? -27.548 24.777  -0.532  1.00 78.62  ? 11  LEU D C   1 
ATOM 4848 O O   . LEU D 2 11  ? -27.958 24.133  -1.501  1.00 82.18  ? 11  LEU D O   1 
ATOM 4849 C CB  . LEU D 2 11  ? -28.586 24.070  1.649   1.00 76.50  ? 11  LEU D CB  1 
ATOM 4850 C CG  . LEU D 2 11  ? -29.151 22.708  1.234   1.00 77.27  ? 11  LEU D CG  1 
ATOM 4851 C CD1 . LEU D 2 11  ? -28.051 21.751  0.810   1.00 80.11  ? 11  LEU D CD1 1 
ATOM 4852 C CD2 . LEU D 2 11  ? -29.964 22.100  2.362   1.00 70.98  ? 11  LEU D CD2 1 
ATOM 4853 N N   . SER D 2 12  ? -26.285 25.168  -0.396  1.00 78.94  ? 12  SER D N   1 
ATOM 4854 C CA  . SER D 2 12  ? -25.251 24.864  -1.376  1.00 86.11  ? 12  SER D CA  1 
ATOM 4855 C C   . SER D 2 12  ? -24.147 24.084  -0.682  1.00 90.16  ? 12  SER D C   1 
ATOM 4856 O O   . SER D 2 12  ? -23.495 24.603  0.230   1.00 95.41  ? 12  SER D O   1 
ATOM 4857 C CB  . SER D 2 12  ? -24.697 26.143  -2.007  1.00 90.36  ? 12  SER D CB  1 
ATOM 4858 O OG  . SER D 2 12  ? -23.997 25.859  -3.206  1.00 96.15  ? 12  SER D OG  1 
ATOM 4859 N N   . VAL D 2 13  ? -23.944 22.841  -1.108  1.00 92.33  ? 13  VAL D N   1 
ATOM 4860 C CA  . VAL D 2 13  ? -22.905 21.983  -0.555  1.00 99.16  ? 13  VAL D CA  1 
ATOM 4861 C C   . VAL D 2 13  ? -21.800 21.812  -1.587  1.00 105.67 ? 13  VAL D C   1 
ATOM 4862 O O   . VAL D 2 13  ? -22.038 21.836  -2.801  1.00 103.87 ? 13  VAL D O   1 
ATOM 4863 C CB  . VAL D 2 13  ? -23.462 20.611  -0.113  1.00 92.13  ? 13  VAL D CB  1 
ATOM 4864 C CG1 . VAL D 2 13  ? -24.605 20.796  0.868   1.00 86.61  ? 13  VAL D CG1 1 
ATOM 4865 C CG2 . VAL D 2 13  ? -23.924 19.804  -1.316  1.00 94.22  ? 13  VAL D CG2 1 
ATOM 4866 N N   . ALA D 2 14  ? -20.576 21.661  -1.091  1.00 119.62 ? 14  ALA D N   1 
ATOM 4867 C CA  . ALA D 2 14  ? -19.452 21.370  -1.962  1.00 120.13 ? 14  ALA D CA  1 
ATOM 4868 C C   . ALA D 2 14  ? -19.548 19.932  -2.469  1.00 119.02 ? 14  ALA D C   1 
ATOM 4869 O O   . ALA D 2 14  ? -20.126 19.069  -1.802  1.00 117.45 ? 14  ALA D O   1 
ATOM 4870 C CB  . ALA D 2 14  ? -18.134 21.578  -1.220  1.00 120.60 ? 14  ALA D CB  1 
ATOM 4871 N N   . PRO D 2 15  ? -18.999 19.649  -3.657  1.00 105.42 ? 15  PRO D N   1 
ATOM 4872 C CA  . PRO D 2 15  ? -19.037 18.274  -4.175  1.00 101.89 ? 15  PRO D CA  1 
ATOM 4873 C C   . PRO D 2 15  ? -18.316 17.291  -3.266  1.00 97.61  ? 15  PRO D C   1 
ATOM 4874 O O   . PRO D 2 15  ? -17.087 17.327  -3.145  1.00 96.64  ? 15  PRO D O   1 
ATOM 4875 C CB  . PRO D 2 15  ? -18.346 18.400  -5.540  1.00 98.18  ? 15  PRO D CB  1 
ATOM 4876 C CG  . PRO D 2 15  ? -17.482 19.621  -5.401  1.00 97.99  ? 15  PRO D CG  1 
ATOM 4877 C CD  . PRO D 2 15  ? -18.336 20.560  -4.604  1.00 102.97 ? 15  PRO D CD  1 
ATOM 4878 N N   . GLY D 2 16  ? -19.077 16.415  -2.612  1.00 95.67  ? 16  GLY D N   1 
ATOM 4879 C CA  . GLY D 2 16  ? -18.544 15.435  -1.692  1.00 91.53  ? 16  GLY D CA  1 
ATOM 4880 C C   . GLY D 2 16  ? -18.971 15.630  -0.253  1.00 88.42  ? 16  GLY D C   1 
ATOM 4881 O O   . GLY D 2 16  ? -18.879 14.682  0.539   1.00 92.47  ? 16  GLY D O   1 
ATOM 4882 N N   . GLU D 2 17  ? -19.435 16.824  0.109   1.00 87.86  ? 17  GLU D N   1 
ATOM 4883 C CA  . GLU D 2 17  ? -19.843 17.102  1.477   1.00 89.16  ? 17  GLU D CA  1 
ATOM 4884 C C   . GLU D 2 17  ? -21.260 16.585  1.723   1.00 82.64  ? 17  GLU D C   1 
ATOM 4885 O O   . GLU D 2 17  ? -21.883 15.959  0.862   1.00 85.59  ? 17  GLU D O   1 
ATOM 4886 C CB  . GLU D 2 17  ? -19.745 18.598  1.770   1.00 92.26  ? 17  GLU D CB  1 
ATOM 4887 C CG  . GLU D 2 17  ? -18.495 18.996  2.539   1.00 86.34  ? 17  GLU D CG  1 
ATOM 4888 C CD  . GLU D 2 17  ? -18.476 18.431  3.946   1.00 84.37  ? 17  GLU D CD  1 
ATOM 4889 O OE1 . GLU D 2 17  ? -19.422 18.704  4.713   1.00 81.40  ? 17  GLU D OE1 1 
ATOM 4890 O OE2 . GLU D 2 17  ? -17.511 17.715  4.285   1.00 79.85  ? 17  GLU D OE2 1 
ATOM 4891 N N   . ALA D 2 18  ? -21.782 16.858  2.915   1.00 80.94  ? 18  ALA D N   1 
ATOM 4892 C CA  . ALA D 2 18  ? -23.065 16.326  3.349   1.00 79.26  ? 18  ALA D CA  1 
ATOM 4893 C C   . ALA D 2 18  ? -24.134 17.412  3.353   1.00 78.32  ? 18  ALA D C   1 
ATOM 4894 O O   . ALA D 2 18  ? -23.894 18.534  3.809   1.00 79.09  ? 18  ALA D O   1 
ATOM 4895 C CB  . ALA D 2 18  ? -22.957 15.705  4.745   1.00 83.18  ? 18  ALA D CB  1 
ATOM 4896 N N   . ALA D 2 19  ? -25.314 17.068  2.844   1.00 77.53  ? 19  ALA D N   1 
ATOM 4897 C CA  . ALA D 2 19  ? -26.493 17.916  2.924   1.00 71.61  ? 19  ALA D CA  1 
ATOM 4898 C C   . ALA D 2 19  ? -27.480 17.321  3.920   1.00 69.24  ? 19  ALA D C   1 
ATOM 4899 O O   . ALA D 2 19  ? -27.468 16.119  4.194   1.00 79.32  ? 19  ALA D O   1 
ATOM 4900 C CB  . ALA D 2 19  ? -27.157 18.076  1.553   1.00 75.48  ? 19  ALA D CB  1 
ATOM 4901 N N   . SER D 2 20  ? -28.350 18.180  4.465   1.00 66.55  ? 20  SER D N   1 
ATOM 4902 C CA  . SER D 2 20  ? -29.245 17.730  5.533   1.00 68.23  ? 20  SER D CA  1 
ATOM 4903 C C   . SER D 2 20  ? -30.542 18.543  5.467   1.00 66.78  ? 20  SER D C   1 
ATOM 4904 O O   . SER D 2 20  ? -30.755 19.507  6.207   1.00 69.62  ? 20  SER D O   1 
ATOM 4905 C CB  . SER D 2 20  ? -28.581 17.848  6.902   1.00 70.93  ? 20  SER D CB  1 
ATOM 4906 O OG  . SER D 2 20  ? -27.484 16.957  7.008   1.00 74.70  ? 20  SER D OG  1 
ATOM 4907 N N   . ILE D 2 21  ? -31.434 18.130  4.563   1.00 63.08  ? 21  ILE D N   1 
ATOM 4908 C CA  . ILE D 2 21  ? -32.765 18.720  4.512   1.00 63.08  ? 21  ILE D CA  1 
ATOM 4909 C C   . ILE D 2 21  ? -33.579 18.190  5.683   1.00 66.75  ? 21  ILE D C   1 
ATOM 4910 O O   . ILE D 2 21  ? -33.445 17.024  6.078   1.00 74.16  ? 21  ILE D O   1 
ATOM 4911 C CB  . ILE D 2 21  ? -33.448 18.409  3.169   1.00 59.77  ? 21  ILE D CB  1 
ATOM 4912 C CG1 . ILE D 2 21  ? -32.614 18.933  1.999   1.00 59.82  ? 21  ILE D CG1 1 
ATOM 4913 C CG2 . ILE D 2 21  ? -34.832 19.043  3.106   1.00 60.89  ? 21  ILE D CG2 1 
ATOM 4914 C CD1 . ILE D 2 21  ? -31.826 17.857  1.284   1.00 61.24  ? 21  ILE D CD1 1 
ATOM 4915 N N   . SER D 2 22  ? -34.418 19.046  6.257   1.00 65.04  ? 22  SER D N   1 
ATOM 4916 C CA  . SER D 2 22  ? -35.226 18.690  7.413   1.00 65.93  ? 22  SER D CA  1 
ATOM 4917 C C   . SER D 2 22  ? -36.695 18.949  7.117   1.00 62.43  ? 22  SER D C   1 
ATOM 4918 O O   . SER D 2 22  ? -37.041 19.857  6.360   1.00 69.31  ? 22  SER D O   1 
ATOM 4919 C CB  . SER D 2 22  ? -34.799 19.480  8.659   1.00 66.87  ? 22  SER D CB  1 
ATOM 4920 O OG  . SER D 2 22  ? -35.741 19.337  9.709   1.00 67.18  ? 22  SER D OG  1 
ATOM 4921 N N   . CYS D 2 23  ? -37.554 18.138  7.724   1.00 59.48  ? 23  CYS D N   1 
ATOM 4922 C CA  . CYS D 2 23  ? -38.995 18.277  7.593   1.00 60.97  ? 23  CYS D CA  1 
ATOM 4923 C C   . CYS D 2 23  ? -39.621 18.257  8.980   1.00 65.01  ? 23  CYS D C   1 
ATOM 4924 O O   . CYS D 2 23  ? -39.152 17.553  9.879   1.00 71.16  ? 23  CYS D O   1 
ATOM 4925 C CB  . CYS D 2 23  ? -39.586 17.158  6.722   1.00 65.45  ? 23  CYS D CB  1 
ATOM 4926 S SG  . CYS D 2 23  ? -41.330 17.349  6.298   1.00 68.66  ? 23  CYS D SG  1 
ATOM 4927 N N   . ARG D 2 24  ? -40.684 19.043  9.149   1.00 67.33  ? 24  ARG D N   1 
ATOM 4928 C CA  . ARG D 2 24  ? -41.337 19.206  10.442  1.00 67.53  ? 24  ARG D CA  1 
ATOM 4929 C C   . ARG D 2 24  ? -42.838 19.333  10.234  1.00 68.94  ? 24  ARG D C   1 
ATOM 4930 O O   . ARG D 2 24  ? -43.285 20.128  9.403   1.00 74.21  ? 24  ARG D O   1 
ATOM 4931 C CB  . ARG D 2 24  ? -40.797 20.437  11.179  1.00 67.73  ? 24  ARG D CB  1 
ATOM 4932 C CG  . ARG D 2 24  ? -39.414 20.238  11.779  1.00 75.41  ? 24  ARG D CG  1 
ATOM 4933 C CD  . ARG D 2 24  ? -38.598 21.521  11.757  1.00 76.24  ? 24  ARG D CD  1 
ATOM 4934 N NE  . ARG D 2 24  ? -38.410 22.074  13.093  1.00 80.35  ? 24  ARG D NE  1 
ATOM 4935 C CZ  . ARG D 2 24  ? -37.327 21.883  13.834  1.00 81.67  ? 24  ARG D CZ  1 
ATOM 4936 N NH1 . ARG D 2 24  ? -36.311 21.154  13.400  1.00 78.42  ? 24  ARG D NH1 1 
ATOM 4937 N NH2 . ARG D 2 24  ? -37.263 22.434  15.043  1.00 81.06  ? 24  ARG D NH2 1 
ATOM 4938 N N   . SER D 2 25  ? -43.609 18.562  10.999  1.00 64.53  ? 25  SER D N   1 
ATOM 4939 C CA  . SER D 2 25  ? -45.057 18.492  10.860  1.00 64.87  ? 25  SER D CA  1 
ATOM 4940 C C   . SER D 2 25  ? -45.741 18.959  12.139  1.00 63.33  ? 25  SER D C   1 
ATOM 4941 O O   . SER D 2 25  ? -45.205 18.807  13.240  1.00 66.57  ? 25  SER D O   1 
ATOM 4942 C CB  . SER D 2 25  ? -45.509 17.063  10.517  1.00 71.25  ? 25  SER D CB  1 
ATOM 4943 O OG  . SER D 2 25  ? -45.683 16.280  11.685  1.00 73.83  ? 25  SER D OG  1 
ATOM 4944 N N   . THR D 2 26  ? -46.938 19.532  11.979  1.00 65.82  ? 26  THR D N   1 
ATOM 4945 C CA  . THR D 2 26  ? -47.716 19.988  13.126  1.00 72.19  ? 26  THR D CA  1 
ATOM 4946 C C   . THR D 2 26  ? -48.313 18.838  13.927  1.00 73.13  ? 26  THR D C   1 
ATOM 4947 O O   . THR D 2 26  ? -48.604 19.015  15.114  1.00 70.63  ? 26  THR D O   1 
ATOM 4948 C CB  . THR D 2 26  ? -48.839 20.927  12.674  1.00 71.31  ? 26  THR D CB  1 
ATOM 4949 O OG1 . THR D 2 26  ? -49.923 20.158  12.133  1.00 76.16  ? 26  THR D OG1 1 
ATOM 4950 C CG2 . THR D 2 26  ? -48.338 21.915  11.636  1.00 63.74  ? 26  THR D CG2 1 
ATOM 4951 N N   . GLN D 2 27  ? -48.507 17.674  13.313  1.00 74.98  ? 27  GLN D N   1 
ATOM 4952 C CA  . GLN D 2 27  ? -49.060 16.518  14.000  1.00 82.15  ? 27  GLN D CA  1 
ATOM 4953 C C   . GLN D 2 27  ? -48.118 15.333  13.841  1.00 85.09  ? 27  GLN D C   1 
ATOM 4954 O O   . GLN D 2 27  ? -47.327 15.261  12.898  1.00 83.53  ? 27  GLN D O   1 
ATOM 4955 C CB  . GLN D 2 27  ? -50.462 16.169  13.477  1.00 81.67  ? 27  GLN D CB  1 
ATOM 4956 C CG  . GLN D 2 27  ? -51.483 17.281  13.675  1.00 84.82  ? 27  GLN D CG  1 
ATOM 4957 C CD  . GLN D 2 27  ? -52.882 16.879  13.253  1.00 94.91  ? 27  GLN D CD  1 
ATOM 4958 O OE1 . GLN D 2 27  ? -53.210 15.694  13.198  1.00 92.78  ? 27  GLN D OE1 1 
ATOM 4959 N NE2 . GLN D 2 27  ? -53.717 17.868  12.953  1.00 96.58  ? 27  GLN D NE2 1 
ATOM 4960 N N   . SER D 2 28  ? -48.215 14.397  14.783  1.00 91.01  ? 28  SER D N   1 
ATOM 4961 C CA  . SER D 2 28  ? -47.283 13.277  14.839  1.00 97.19  ? 28  SER D CA  1 
ATOM 4962 C C   . SER D 2 28  ? -47.578 12.284  13.721  1.00 98.18  ? 28  SER D C   1 
ATOM 4963 O O   . SER D 2 28  ? -48.701 11.781  13.604  1.00 96.05  ? 28  SER D O   1 
ATOM 4964 C CB  . SER D 2 28  ? -47.364 12.593  16.200  1.00 96.52  ? 28  SER D CB  1 
ATOM 4965 O OG  . SER D 2 28  ? -48.707 12.303  16.547  1.00 103.53 ? 28  SER D OG  1 
ATOM 4966 N N   . LEU D 2 29  ? -46.562 11.993  12.907  1.00 97.53  ? 29  LEU D N   1 
ATOM 4967 C CA  . LEU D 2 29  ? -46.687 11.076  11.774  1.00 95.27  ? 29  LEU D CA  1 
ATOM 4968 C C   . LEU D 2 29  ? -46.083 9.732   12.174  1.00 96.94  ? 29  LEU D C   1 
ATOM 4969 O O   . LEU D 2 29  ? -44.963 9.390   11.801  1.00 90.96  ? 29  LEU D O   1 
ATOM 4970 C CB  . LEU D 2 29  ? -45.992 11.653  10.540  1.00 84.53  ? 29  LEU D CB  1 
ATOM 4971 C CG  . LEU D 2 29  ? -46.276 13.087  10.082  1.00 75.94  ? 29  LEU D CG  1 
ATOM 4972 C CD1 . LEU D 2 29  ? -45.335 13.468  8.946   1.00 61.31  ? 29  LEU D CD1 1 
ATOM 4973 C CD2 . LEU D 2 29  ? -47.723 13.252  9.649   1.00 77.87  ? 29  LEU D CD2 1 
ATOM 4974 N N   . LEU D 2 30  ? -46.842 8.953   12.947  1.00 107.00 ? 30  LEU D N   1 
ATOM 4975 C CA  . LEU D 2 30  ? -46.356 7.675   13.449  1.00 107.82 ? 30  LEU D CA  1 
ATOM 4976 C C   . LEU D 2 30  ? -47.500 6.679   13.571  1.00 108.64 ? 30  LEU D C   1 
ATOM 4977 O O   . LEU D 2 30  ? -48.657 7.053   13.774  1.00 108.89 ? 30  LEU D O   1 
ATOM 4978 C CB  . LEU D 2 30  ? -45.630 7.846   14.800  1.00 107.96 ? 30  LEU D CB  1 
ATOM 4979 C CG  . LEU D 2 30  ? -46.160 8.842   15.843  1.00 110.37 ? 30  LEU D CG  1 
ATOM 4980 C CD1 . LEU D 2 30  ? -47.499 8.420   16.432  1.00 111.65 ? 30  LEU D CD1 1 
ATOM 4981 C CD2 . LEU D 2 30  ? -45.139 9.068   16.957  1.00 110.46 ? 30  LEU D CD2 1 
ATOM 4982 N N   . ASN D 2 31  ? -47.158 5.403   13.427  1.00 92.82  ? 31  ASN D N   1 
ATOM 4983 C CA  . ASN D 2 31  ? -48.086 4.284   13.534  1.00 87.93  ? 31  ASN D CA  1 
ATOM 4984 C C   . ASN D 2 31  ? -47.766 3.509   14.802  1.00 96.46  ? 31  ASN D C   1 
ATOM 4985 O O   . ASN D 2 31  ? -46.951 3.942   15.629  1.00 99.09  ? 31  ASN D O   1 
ATOM 4986 C CB  . ASN D 2 31  ? -48.014 3.381   12.304  1.00 84.38  ? 31  ASN D CB  1 
ATOM 4987 C CG  . ASN D 2 31  ? -49.255 2.511   12.129  1.00 89.52  ? 31  ASN D CG  1 
ATOM 4988 O OD1 . ASN D 2 31  ? -50.314 2.770   12.699  1.00 90.99  ? 31  ASN D OD1 1 
ATOM 4989 N ND2 . ASN D 2 31  ? -49.118 1.467   11.318  1.00 86.64  ? 31  ASN D ND2 1 
ATOM 4990 N N   . ARG D 2 32  ? -48.383 2.335   14.951  1.00 94.22  ? 32  ARG D N   1 
ATOM 4991 C CA  . ARG D 2 32  ? -48.243 1.683   16.241  1.00 87.73  ? 32  ARG D CA  1 
ATOM 4992 C C   . ARG D 2 32  ? -46.886 1.013   16.309  1.00 81.44  ? 32  ARG D C   1 
ATOM 4993 O O   . ARG D 2 32  ? -46.104 1.257   17.233  1.00 90.42  ? 32  ARG D O   1 
ATOM 4994 C CB  . ARG D 2 32  ? -49.393 0.710   16.510  1.00 84.84  ? 32  ARG D CB  1 
ATOM 4995 C CG  . ARG D 2 32  ? -50.606 1.481   17.015  1.00 91.75  ? 32  ARG D CG  1 
ATOM 4996 C CD  . ARG D 2 32  ? -50.035 2.778   17.570  1.00 105.09 ? 32  ARG D CD  1 
ATOM 4997 N NE  . ARG D 2 32  ? -50.845 3.654   18.361  1.00 113.38 ? 32  ARG D NE  1 
ATOM 4998 C CZ  . ARG D 2 32  ? -50.391 4.818   18.797  1.00 111.93 ? 32  ARG D CZ  1 
ATOM 4999 N NH1 . ARG D 2 32  ? -49.236 5.317   18.364  1.00 110.97 ? 32  ARG D NH1 1 
ATOM 5000 N NH2 . ARG D 2 32  ? -51.119 5.510   19.673  1.00 116.48 ? 32  ARG D NH2 1 
ATOM 5001 N N   . ASN D 2 33  ? -46.586 0.179   15.322  1.00 79.46  ? 33  ASN D N   1 
ATOM 5002 C CA  . ASN D 2 33  ? -45.198 -0.117  14.988  1.00 80.26  ? 33  ASN D CA  1 
ATOM 5003 C C   . ASN D 2 33  ? -44.465 1.187   14.666  1.00 79.48  ? 33  ASN D C   1 
ATOM 5004 O O   . ASN D 2 33  ? -45.040 2.137   14.122  1.00 83.09  ? 33  ASN D O   1 
ATOM 5005 C CB  . ASN D 2 33  ? -45.146 -1.087  13.801  1.00 81.59  ? 33  ASN D CB  1 
ATOM 5006 C CG  . ASN D 2 33  ? -43.737 -1.470  13.409  1.00 78.29  ? 33  ASN D CG  1 
ATOM 5007 O OD1 . ASN D 2 33  ? -42.961 -0.640  12.952  1.00 77.82  ? 33  ASN D OD1 1 
ATOM 5008 N ND2 . ASN D 2 33  ? -43.403 -2.755  13.569  1.00 70.70  ? 33  ASN D ND2 1 
ATOM 5009 N N   . GLY D 2 34  ? -43.181 1.233   15.000  1.00 77.47  ? 34  GLY D N   1 
ATOM 5010 C CA  . GLY D 2 34  ? -42.400 2.451   14.827  1.00 80.30  ? 34  GLY D CA  1 
ATOM 5011 C C   . GLY D 2 34  ? -42.170 2.917   13.402  1.00 81.92  ? 34  GLY D C   1 
ATOM 5012 O O   . GLY D 2 34  ? -41.051 3.307   13.055  1.00 81.98  ? 34  GLY D O   1 
ATOM 5013 N N   . ASP D 2 35  ? -43.210 2.909   12.575  1.00 84.12  ? 35  ASP D N   1 
ATOM 5014 C CA  . ASP D 2 35  ? -43.111 3.354   11.192  1.00 75.42  ? 35  ASP D CA  1 
ATOM 5015 C C   . ASP D 2 35  ? -43.747 4.730   11.068  1.00 76.61  ? 35  ASP D C   1 
ATOM 5016 O O   . ASP D 2 35  ? -44.898 4.930   11.473  1.00 77.10  ? 35  ASP D O   1 
ATOM 5017 C CB  . ASP D 2 35  ? -43.776 2.362   10.232  1.00 75.10  ? 35  ASP D CB  1 
ATOM 5018 C CG  . ASP D 2 35  ? -45.224 2.088   10.583  1.00 78.30  ? 35  ASP D CG  1 
ATOM 5019 O OD1 . ASP D 2 35  ? -45.477 1.307   11.523  1.00 74.53  ? 35  ASP D OD1 1 
ATOM 5020 O OD2 . ASP D 2 35  ? -46.111 2.654   9.909   1.00 85.60  ? 35  ASP D OD2 1 
ATOM 5021 N N   . ASN D 2 36  ? -42.987 5.673   10.524  1.00 77.42  ? 36  ASN D N   1 
ATOM 5022 C CA  . ASN D 2 36  ? -43.418 7.054   10.383  1.00 74.19  ? 36  ASN D CA  1 
ATOM 5023 C C   . ASN D 2 36  ? -43.845 7.318   8.946   1.00 69.10  ? 36  ASN D C   1 
ATOM 5024 O O   . ASN D 2 36  ? -43.089 7.045   8.008   1.00 65.16  ? 36  ASN D O   1 
ATOM 5025 C CB  . ASN D 2 36  ? -42.299 8.009   10.796  1.00 72.08  ? 36  ASN D CB  1 
ATOM 5026 C CG  . ASN D 2 36  ? -41.916 7.856   12.256  1.00 79.40  ? 36  ASN D CG  1 
ATOM 5027 O OD1 . ASN D 2 36  ? -42.754 8.008   13.144  1.00 81.68  ? 36  ASN D OD1 1 
ATOM 5028 N ND2 . ASN D 2 36  ? -40.650 7.550   12.511  1.00 82.14  ? 36  ASN D ND2 1 
ATOM 5029 N N   . TYR D 2 37  ? -45.051 7.852   8.779   1.00 70.65  ? 37  TYR D N   1 
ATOM 5030 C CA  . TYR D 2 37  ? -45.619 8.075   7.452   1.00 65.95  ? 37  TYR D CA  1 
ATOM 5031 C C   . TYR D 2 37  ? -45.053 9.368   6.881   1.00 60.53  ? 37  TYR D C   1 
ATOM 5032 O O   . TYR D 2 37  ? -45.558 10.460  7.155   1.00 62.19  ? 37  TYR D O   1 
ATOM 5033 C CB  . TYR D 2 37  ? -47.139 8.107   7.523   1.00 67.53  ? 37  TYR D CB  1 
ATOM 5034 C CG  . TYR D 2 37  ? -47.728 6.756   7.837   1.00 69.87  ? 37  TYR D CG  1 
ATOM 5035 C CD1 . TYR D 2 37  ? -47.420 5.645   7.060   1.00 71.43  ? 37  TYR D CD1 1 
ATOM 5036 C CD2 . TYR D 2 37  ? -48.574 6.584   8.921   1.00 72.56  ? 37  TYR D CD2 1 
ATOM 5037 C CE1 . TYR D 2 37  ? -47.952 4.404   7.349   1.00 73.39  ? 37  TYR D CE1 1 
ATOM 5038 C CE2 . TYR D 2 37  ? -49.109 5.350   9.218   1.00 76.78  ? 37  TYR D CE2 1 
ATOM 5039 C CZ  . TYR D 2 37  ? -48.797 4.264   8.432   1.00 77.21  ? 37  TYR D CZ  1 
ATOM 5040 O OH  . TYR D 2 37  ? -49.338 3.039   8.740   1.00 74.21  ? 37  TYR D OH  1 
ATOM 5041 N N   . LEU D 2 38  ? -44.004 9.239   6.065   1.00 53.83  ? 38  LEU D N   1 
ATOM 5042 C CA  . LEU D 2 38  ? -43.333 10.381  5.457   1.00 53.71  ? 38  LEU D CA  1 
ATOM 5043 C C   . LEU D 2 38  ? -42.436 9.930   4.311   1.00 53.72  ? 38  LEU D C   1 
ATOM 5044 O O   . LEU D 2 38  ? -41.554 9.090   4.507   1.00 56.79  ? 38  LEU D O   1 
ATOM 5045 C CB  . LEU D 2 38  ? -42.518 11.140  6.506   1.00 54.04  ? 38  LEU D CB  1 
ATOM 5046 C CG  . LEU D 2 38  ? -41.826 12.425  6.058   1.00 55.50  ? 38  LEU D CG  1 
ATOM 5047 C CD1 . LEU D 2 38  ? -42.182 13.581  6.980   1.00 60.31  ? 38  LEU D CD1 1 
ATOM 5048 C CD2 . LEU D 2 38  ? -40.324 12.210  6.011   1.00 56.08  ? 38  LEU D CD2 1 
ATOM 5049 N N   . GLU D 2 39  ? -42.645 10.479  3.117   1.00 53.58  ? 39  GLU D N   1 
ATOM 5050 C CA  . GLU D 2 39  ? -41.856 10.124  1.947   1.00 60.30  ? 39  GLU D CA  1 
ATOM 5051 C C   . GLU D 2 39  ? -41.088 11.333  1.432   1.00 59.96  ? 39  GLU D C   1 
ATOM 5052 O O   . GLU D 2 39  ? -41.604 12.454  1.428   1.00 56.23  ? 39  GLU D O   1 
ATOM 5053 C CB  . GLU D 2 39  ? -42.737 9.553   0.832   1.00 59.45  ? 39  GLU D CB  1 
ATOM 5054 C CG  . GLU D 2 39  ? -43.265 8.162   1.124   1.00 58.48  ? 39  GLU D CG  1 
ATOM 5055 C CD  . GLU D 2 39  ? -44.754 8.140   1.378   1.00 60.25  ? 39  GLU D CD  1 
ATOM 5056 O OE1 . GLU D 2 39  ? -45.430 9.132   1.036   1.00 58.64  ? 39  GLU D OE1 1 
ATOM 5057 O OE2 . GLU D 2 39  ? -45.249 7.129   1.918   1.00 60.69  ? 39  GLU D OE2 1 
ATOM 5058 N N   . TRP D 2 40  ? -39.854 11.097  0.997   1.00 67.17  ? 40  TRP D N   1 
ATOM 5059 C CA  . TRP D 2 40  ? -38.993 12.151  0.481   1.00 66.62  ? 40  TRP D CA  1 
ATOM 5060 C C   . TRP D 2 40  ? -38.905 12.045  -1.033  1.00 68.64  ? 40  TRP D C   1 
ATOM 5061 O O   . TRP D 2 40  ? -38.586 10.978  -1.571  1.00 67.53  ? 40  TRP D O   1 
ATOM 5062 C CB  . TRP D 2 40  ? -37.598 12.075  1.098   1.00 68.07  ? 40  TRP D CB  1 
ATOM 5063 C CG  . TRP D 2 40  ? -37.513 12.692  2.457   1.00 68.91  ? 40  TRP D CG  1 
ATOM 5064 C CD1 . TRP D 2 40  ? -37.585 12.051  3.659   1.00 71.14  ? 40  TRP D CD1 1 
ATOM 5065 C CD2 . TRP D 2 40  ? -37.377 14.085  2.751   1.00 69.51  ? 40  TRP D CD2 1 
ATOM 5066 N NE1 . TRP D 2 40  ? -37.474 12.958  4.685   1.00 68.59  ? 40  TRP D NE1 1 
ATOM 5067 C CE2 . TRP D 2 40  ? -37.353 14.215  4.153   1.00 70.21  ? 40  TRP D CE2 1 
ATOM 5068 C CE3 . TRP D 2 40  ? -37.263 15.234  1.963   1.00 68.97  ? 40  TRP D CE3 1 
ATOM 5069 C CZ2 . TRP D 2 40  ? -37.215 15.449  4.783   1.00 73.53  ? 40  TRP D CZ2 1 
ATOM 5070 C CZ3 . TRP D 2 40  ? -37.131 16.456  2.590   1.00 74.38  ? 40  TRP D CZ3 1 
ATOM 5071 C CH2 . TRP D 2 40  ? -37.109 16.555  3.986   1.00 74.63  ? 40  TRP D CH2 1 
ATOM 5072 N N   . TYR D 2 41  ? -39.181 13.150  -1.712  1.00 68.36  ? 41  TYR D N   1 
ATOM 5073 C CA  . TYR D 2 41  ? -39.187 13.185  -3.163  1.00 55.52  ? 41  TYR D CA  1 
ATOM 5074 C C   . TYR D 2 41  ? -38.165 14.198  -3.658  1.00 52.86  ? 41  TYR D C   1 
ATOM 5075 O O   . TYR D 2 41  ? -37.856 15.178  -2.975  1.00 61.94  ? 41  TYR D O   1 
ATOM 5076 C CB  . TYR D 2 41  ? -40.575 13.533  -3.697  1.00 52.54  ? 41  TYR D CB  1 
ATOM 5077 C CG  . TYR D 2 41  ? -41.621 12.489  -3.384  1.00 55.85  ? 41  TYR D CG  1 
ATOM 5078 C CD1 . TYR D 2 41  ? -41.786 11.372  -4.195  1.00 54.79  ? 41  TYR D CD1 1 
ATOM 5079 C CD2 . TYR D 2 41  ? -42.440 12.617  -2.273  1.00 55.59  ? 41  TYR D CD2 1 
ATOM 5080 C CE1 . TYR D 2 41  ? -42.742 10.418  -3.910  1.00 52.44  ? 41  TYR D CE1 1 
ATOM 5081 C CE2 . TYR D 2 41  ? -43.398 11.668  -1.979  1.00 57.49  ? 41  TYR D CE2 1 
ATOM 5082 C CZ  . TYR D 2 41  ? -43.546 10.570  -2.799  1.00 53.13  ? 41  TYR D CZ  1 
ATOM 5083 O OH  . TYR D 2 41  ? -44.501 9.622   -2.509  1.00 52.69  ? 41  TYR D OH  1 
ATOM 5084 N N   . LEU D 2 42  ? -37.640 13.948  -4.854  1.00 52.81  ? 42  LEU D N   1 
ATOM 5085 C CA  . LEU D 2 42  ? -36.669 14.833  -5.489  1.00 58.69  ? 42  LEU D CA  1 
ATOM 5086 C C   . LEU D 2 42  ? -37.163 15.156  -6.891  1.00 71.25  ? 42  LEU D C   1 
ATOM 5087 O O   . LEU D 2 42  ? -37.189 14.280  -7.761  1.00 69.76  ? 42  LEU D O   1 
ATOM 5088 C CB  . LEU D 2 42  ? -35.281 14.194  -5.539  1.00 57.94  ? 42  LEU D CB  1 
ATOM 5089 C CG  . LEU D 2 42  ? -34.283 14.776  -6.546  1.00 64.07  ? 42  LEU D CG  1 
ATOM 5090 C CD1 . LEU D 2 42  ? -33.986 16.238  -6.238  1.00 73.08  ? 42  LEU D CD1 1 
ATOM 5091 C CD2 . LEU D 2 42  ? -33.001 13.957  -6.588  1.00 69.52  ? 42  LEU D CD2 1 
ATOM 5092 N N   . ARG D 2 43  ? -37.554 16.405  -7.113  1.00 74.15  ? 43  ARG D N   1 
ATOM 5093 C CA  . ARG D 2 43  ? -37.887 16.876  -8.450  1.00 75.77  ? 43  ARG D CA  1 
ATOM 5094 C C   . ARG D 2 43  ? -36.637 17.502  -9.053  1.00 77.75  ? 43  ARG D C   1 
ATOM 5095 O O   . ARG D 2 43  ? -36.215 18.587  -8.637  1.00 80.93  ? 43  ARG D O   1 
ATOM 5096 C CB  . ARG D 2 43  ? -39.035 17.881  -8.421  1.00 77.63  ? 43  ARG D CB  1 
ATOM 5097 C CG  . ARG D 2 43  ? -39.151 18.670  -9.717  1.00 81.55  ? 43  ARG D CG  1 
ATOM 5098 C CD  . ARG D 2 43  ? -40.405 19.515  -9.782  1.00 84.44  ? 43  ARG D CD  1 
ATOM 5099 N NE  . ARG D 2 43  ? -40.371 20.420  -10.926 1.00 90.65  ? 43  ARG D NE  1 
ATOM 5100 C CZ  . ARG D 2 43  ? -39.683 21.554  -10.966 1.00 96.76  ? 43  ARG D CZ  1 
ATOM 5101 N NH1 . ARG D 2 43  ? -38.961 21.961  -9.934  1.00 85.86  ? 43  ARG D NH1 1 
ATOM 5102 N NH2 . ARG D 2 43  ? -39.718 22.295  -12.070 1.00 101.12 ? 43  ARG D NH2 1 
ATOM 5103 N N   . ARG D 2 44  ? -36.031 16.812  -10.015 1.00 71.71  ? 44  ARG D N   1 
ATOM 5104 C CA  . ARG D 2 44  ? -34.931 17.390  -10.762 1.00 77.11  ? 44  ARG D CA  1 
ATOM 5105 C C   . ARG D 2 44  ? -35.443 18.545  -11.619 1.00 83.59  ? 44  ARG D C   1 
ATOM 5106 O O   . ARG D 2 44  ? -36.634 18.620  -11.929 1.00 86.21  ? 44  ARG D O   1 
ATOM 5107 C CB  . ARG D 2 44  ? -34.270 16.331  -11.641 1.00 79.95  ? 44  ARG D CB  1 
ATOM 5108 C CG  . ARG D 2 44  ? -33.351 15.379  -10.896 1.00 79.32  ? 44  ARG D CG  1 
ATOM 5109 C CD  . ARG D 2 44  ? -32.300 14.796  -11.830 1.00 83.44  ? 44  ARG D CD  1 
ATOM 5110 N NE  . ARG D 2 44  ? -32.755 13.566  -12.467 1.00 89.27  ? 44  ARG D NE  1 
ATOM 5111 C CZ  . ARG D 2 44  ? -32.305 12.355  -12.168 1.00 96.72  ? 44  ARG D CZ  1 
ATOM 5112 N NH1 . ARG D 2 44  ? -31.383 12.171  -11.236 1.00 94.66  ? 44  ARG D NH1 1 
ATOM 5113 N NH2 . ARG D 2 44  ? -32.791 11.303  -12.819 1.00 103.84 ? 44  ARG D NH2 1 
ATOM 5114 N N   . PRO D 2 45  ? -34.564 19.470  -12.008 1.00 84.53  ? 45  PRO D N   1 
ATOM 5115 C CA  . PRO D 2 45  ? -34.988 20.552  -12.909 1.00 85.24  ? 45  PRO D CA  1 
ATOM 5116 C C   . PRO D 2 45  ? -35.331 20.005  -14.288 1.00 84.90  ? 45  PRO D C   1 
ATOM 5117 O O   . PRO D 2 45  ? -34.487 19.414  -14.966 1.00 83.87  ? 45  PRO D O   1 
ATOM 5118 C CB  . PRO D 2 45  ? -33.767 21.478  -12.945 1.00 88.83  ? 45  PRO D CB  1 
ATOM 5119 C CG  . PRO D 2 45  ? -32.616 20.566  -12.681 1.00 85.45  ? 45  PRO D CG  1 
ATOM 5120 C CD  . PRO D 2 45  ? -33.138 19.591  -11.654 1.00 83.16  ? 45  PRO D CD  1 
ATOM 5121 N N   . GLY D 2 46  ? -36.583 20.193  -14.695 1.00 85.40  ? 46  GLY D N   1 
ATOM 5122 C CA  . GLY D 2 46  ? -37.031 19.733  -15.994 1.00 85.31  ? 46  GLY D CA  1 
ATOM 5123 C C   . GLY D 2 46  ? -37.806 18.434  -15.941 1.00 80.61  ? 46  GLY D C   1 
ATOM 5124 O O   . GLY D 2 46  ? -38.810 18.275  -16.642 1.00 76.92  ? 46  GLY D O   1 
ATOM 5125 N N   . ARG D 2 47  ? -37.354 17.497  -15.113 1.00 79.70  ? 47  ARG D N   1 
ATOM 5126 C CA  . ARG D 2 47  ? -38.000 16.200  -14.994 1.00 78.08  ? 47  ARG D CA  1 
ATOM 5127 C C   . ARG D 2 47  ? -39.099 16.237  -13.931 1.00 78.19  ? 47  ARG D C   1 
ATOM 5128 O O   . ARG D 2 47  ? -39.266 17.216  -13.199 1.00 80.91  ? 47  ARG D O   1 
ATOM 5129 C CB  . ARG D 2 47  ? -36.968 15.120  -14.666 1.00 76.72  ? 47  ARG D CB  1 
ATOM 5130 C CG  . ARG D 2 47  ? -37.280 13.754  -15.266 1.00 89.11  ? 47  ARG D CG  1 
ATOM 5131 C CD  . ARG D 2 47  ? -36.020 12.917  -15.442 1.00 102.45 ? 47  ARG D CD  1 
ATOM 5132 N NE  . ARG D 2 47  ? -35.461 13.030  -16.785 1.00 105.66 ? 47  ARG D NE  1 
ATOM 5133 C CZ  . ARG D 2 47  ? -34.249 13.493  -17.056 1.00 105.72 ? 47  ARG D CZ  1 
ATOM 5134 N NH1 . ARG D 2 47  ? -33.433 13.898  -16.096 1.00 102.77 ? 47  ARG D NH1 1 
ATOM 5135 N NH2 . ARG D 2 47  ? -33.846 13.555  -18.322 1.00 106.95 ? 47  ARG D NH2 1 
ATOM 5136 N N   . SER D 2 48  ? -39.857 15.146  -13.858 1.00 71.55  ? 48  SER D N   1 
ATOM 5137 C CA  . SER D 2 48  ? -40.958 15.008  -12.914 1.00 68.87  ? 48  SER D CA  1 
ATOM 5138 C C   . SER D 2 48  ? -40.421 14.637  -11.536 1.00 70.44  ? 48  SER D C   1 
ATOM 5139 O O   . SER D 2 48  ? -39.234 14.347  -11.377 1.00 72.25  ? 48  SER D O   1 
ATOM 5140 C CB  . SER D 2 48  ? -41.942 13.958  -13.429 1.00 70.51  ? 48  SER D CB  1 
ATOM 5141 O OG  . SER D 2 48  ? -41.270 12.856  -14.011 1.00 80.22  ? 48  SER D OG  1 
ATOM 5142 N N   . PRO D 2 49  ? -41.268 14.657  -10.501 1.00 66.69  ? 49  PRO D N   1 
ATOM 5143 C CA  . PRO D 2 49  ? -40.805 14.224  -9.177  1.00 63.08  ? 49  PRO D CA  1 
ATOM 5144 C C   . PRO D 2 49  ? -40.313 12.782  -9.185  1.00 67.42  ? 49  PRO D C   1 
ATOM 5145 O O   . PRO D 2 49  ? -40.702 11.965  -10.024 1.00 68.04  ? 49  PRO D O   1 
ATOM 5146 C CB  . PRO D 2 49  ? -42.048 14.394  -8.296  1.00 58.89  ? 49  PRO D CB  1 
ATOM 5147 C CG  . PRO D 2 49  ? -42.792 15.506  -8.954  1.00 61.45  ? 49  PRO D CG  1 
ATOM 5148 C CD  . PRO D 2 49  ? -42.607 15.272  -10.427 1.00 66.47  ? 49  PRO D CD  1 
ATOM 5149 N N   . GLN D 2 50  ? -39.434 12.486  -8.230  1.00 66.64  ? 50  GLN D N   1 
ATOM 5150 C CA  . GLN D 2 50  ? -38.762 11.201  -8.103  1.00 61.30  ? 50  GLN D CA  1 
ATOM 5151 C C   . GLN D 2 50  ? -38.824 10.758  -6.651  1.00 57.57  ? 50  GLN D C   1 
ATOM 5152 O O   . GLN D 2 50  ? -38.626 11.569  -5.744  1.00 64.18  ? 50  GLN D O   1 
ATOM 5153 C CB  . GLN D 2 50  ? -37.302 11.304  -8.561  1.00 59.94  ? 50  GLN D CB  1 
ATOM 5154 C CG  . GLN D 2 50  ? -36.409 10.135  -8.186  1.00 62.49  ? 50  GLN D CG  1 
ATOM 5155 C CD  . GLN D 2 50  ? -35.040 10.241  -8.827  1.00 68.34  ? 50  GLN D CD  1 
ATOM 5156 O OE1 . GLN D 2 50  ? -34.799 11.120  -9.653  1.00 64.74  ? 50  GLN D OE1 1 
ATOM 5157 N NE2 . GLN D 2 50  ? -34.129 9.357   -8.437  1.00 79.79  ? 50  GLN D NE2 1 
ATOM 5158 N N   . LEU D 2 51  ? -39.098 9.476   -6.429  1.00 58.40  ? 51  LEU D N   1 
ATOM 5159 C CA  . LEU D 2 51  ? -39.207 8.946   -5.076  1.00 61.93  ? 51  LEU D CA  1 
ATOM 5160 C C   . LEU D 2 51  ? -37.831 8.530   -4.572  1.00 64.72  ? 51  LEU D C   1 
ATOM 5161 O O   . LEU D 2 51  ? -37.120 7.769   -5.236  1.00 60.56  ? 51  LEU D O   1 
ATOM 5162 C CB  . LEU D 2 51  ? -40.171 7.760   -5.029  1.00 61.79  ? 51  LEU D CB  1 
ATOM 5163 C CG  . LEU D 2 51  ? -40.166 6.954   -3.725  1.00 54.44  ? 51  LEU D CG  1 
ATOM 5164 C CD1 . LEU D 2 51  ? -40.665 7.799   -2.564  1.00 60.12  ? 51  LEU D CD1 1 
ATOM 5165 C CD2 . LEU D 2 51  ? -40.995 5.687   -3.857  1.00 58.85  ? 51  LEU D CD2 1 
ATOM 5166 N N   . LEU D 2 52  ? -37.460 9.037   -3.397  1.00 67.28  ? 52  LEU D N   1 
ATOM 5167 C CA  . LEU D 2 52  ? -36.175 8.742   -2.779  1.00 65.66  ? 52  LEU D CA  1 
ATOM 5168 C C   . LEU D 2 52  ? -36.300 7.845   -1.559  1.00 60.75  ? 52  LEU D C   1 
ATOM 5169 O O   . LEU D 2 52  ? -35.565 6.862   -1.437  1.00 64.50  ? 52  LEU D O   1 
ATOM 5170 C CB  . LEU D 2 52  ? -35.463 10.045  -2.384  1.00 59.17  ? 52  LEU D CB  1 
ATOM 5171 C CG  . LEU D 2 52  ? -34.975 10.980  -3.488  1.00 56.51  ? 52  LEU D CG  1 
ATOM 5172 C CD1 . LEU D 2 52  ? -34.237 12.152  -2.865  1.00 62.50  ? 52  LEU D CD1 1 
ATOM 5173 C CD2 . LEU D 2 52  ? -34.079 10.237  -4.459  1.00 64.29  ? 52  LEU D CD2 1 
ATOM 5174 N N   . ILE D 2 53  ? -37.220 8.157   -0.649  1.00 57.17  ? 53  ILE D N   1 
ATOM 5175 C CA  . ILE D 2 53  ? -37.363 7.418   0.599   1.00 54.82  ? 53  ILE D CA  1 
ATOM 5176 C C   . ILE D 2 53  ? -38.840 7.313   0.954   1.00 54.94  ? 53  ILE D C   1 
ATOM 5177 O O   . ILE D 2 53  ? -39.600 8.272   0.783   1.00 69.50  ? 53  ILE D O   1 
ATOM 5178 C CB  . ILE D 2 53  ? -36.553 8.078   1.737   1.00 59.53  ? 53  ILE D CB  1 
ATOM 5179 C CG1 . ILE D 2 53  ? -35.102 7.597   1.697   1.00 67.20  ? 53  ILE D CG1 1 
ATOM 5180 C CG2 . ILE D 2 53  ? -37.174 7.808   3.101   1.00 57.28  ? 53  ILE D CG2 1 
ATOM 5181 C CD1 . ILE D 2 53  ? -34.162 8.431   2.518   1.00 73.56  ? 53  ILE D CD1 1 
ATOM 5182 N N   . TYR D 2 54  ? -39.249 6.138   1.436   1.00 57.49  ? 54  TYR D N   1 
ATOM 5183 C CA  . TYR D 2 54  ? -40.616 5.902   1.873   1.00 58.16  ? 54  TYR D CA  1 
ATOM 5184 C C   . TYR D 2 54  ? -40.620 5.338   3.287   1.00 59.66  ? 54  TYR D C   1 
ATOM 5185 O O   . TYR D 2 54  ? -39.667 4.680   3.716   1.00 60.18  ? 54  TYR D O   1 
ATOM 5186 C CB  . TYR D 2 54  ? -41.363 4.946   0.925   1.00 61.14  ? 54  TYR D CB  1 
ATOM 5187 C CG  . TYR D 2 54  ? -40.770 3.555   0.836   1.00 62.71  ? 54  TYR D CG  1 
ATOM 5188 C CD1 . TYR D 2 54  ? -39.688 3.290   0.006   1.00 59.89  ? 54  TYR D CD1 1 
ATOM 5189 C CD2 . TYR D 2 54  ? -41.306 2.504   1.570   1.00 57.01  ? 54  TYR D CD2 1 
ATOM 5190 C CE1 . TYR D 2 54  ? -39.149 2.020   -0.080  1.00 63.75  ? 54  TYR D CE1 1 
ATOM 5191 C CE2 . TYR D 2 54  ? -40.774 1.232   1.489   1.00 57.37  ? 54  TYR D CE2 1 
ATOM 5192 C CZ  . TYR D 2 54  ? -39.697 0.996   0.663   1.00 64.39  ? 54  TYR D CZ  1 
ATOM 5193 O OH  . TYR D 2 54  ? -39.166 -0.270  0.581   1.00 63.73  ? 54  TYR D OH  1 
ATOM 5194 N N   . LEU D 2 55  ? -41.710 5.613   4.006   1.00 57.94  ? 55  LEU D N   1 
ATOM 5195 C CA  . LEU D 2 55  ? -41.895 5.157   5.387   1.00 60.61  ? 55  LEU D CA  1 
ATOM 5196 C C   . LEU D 2 55  ? -40.766 5.639   6.298   1.00 58.41  ? 55  LEU D C   1 
ATOM 5197 O O   . LEU D 2 55  ? -40.344 4.940   7.223   1.00 59.36  ? 55  LEU D O   1 
ATOM 5198 C CB  . LEU D 2 55  ? -42.038 3.635   5.450   1.00 55.13  ? 55  LEU D CB  1 
ATOM 5199 C CG  . LEU D 2 55  ? -43.433 3.119   5.109   1.00 54.87  ? 55  LEU D CG  1 
ATOM 5200 C CD1 . LEU D 2 55  ? -43.421 1.608   4.933   1.00 56.23  ? 55  LEU D CD1 1 
ATOM 5201 C CD2 . LEU D 2 55  ? -44.423 3.540   6.183   1.00 54.78  ? 55  LEU D CD2 1 
ATOM 5202 N N   . GLY D 2 56  ? -40.266 6.843   6.028   1.00 60.42  ? 56  GLY D N   1 
ATOM 5203 C CA  . GLY D 2 56  ? -39.352 7.533   6.912   1.00 60.13  ? 56  GLY D CA  1 
ATOM 5204 C C   . GLY D 2 56  ? -37.879 7.207   6.727   1.00 62.66  ? 56  GLY D C   1 
ATOM 5205 O O   . GLY D 2 56  ? -37.031 8.071   6.987   1.00 62.94  ? 56  GLY D O   1 
ATOM 5206 N N   . SER D 2 57  ? -37.542 5.992   6.281   1.00 62.20  ? 57  SER D N   1 
ATOM 5207 C CA  . SER D 2 57  ? -36.144 5.565   6.382   1.00 63.00  ? 57  SER D CA  1 
ATOM 5208 C C   . SER D 2 57  ? -35.576 4.745   5.219   1.00 66.32  ? 57  SER D C   1 
ATOM 5209 O O   . SER D 2 57  ? -34.351 4.752   5.070   1.00 67.08  ? 57  SER D O   1 
ATOM 5210 C CB  . SER D 2 57  ? -35.917 4.777   7.681   1.00 64.07  ? 57  SER D CB  1 
ATOM 5211 O OG  . SER D 2 57  ? -36.891 3.766   7.854   1.00 56.88  ? 57  SER D OG  1 
ATOM 5212 N N   . GLU D 2 58  ? -36.348 4.046   4.382   1.00 66.87  ? 58  GLU D N   1 
ATOM 5213 C CA  . GLU D 2 58  ? -35.714 3.275   3.313   1.00 66.32  ? 58  GLU D CA  1 
ATOM 5214 C C   . GLU D 2 58  ? -35.575 4.091   2.039   1.00 68.20  ? 58  GLU D C   1 
ATOM 5215 O O   . GLU D 2 58  ? -36.521 4.752   1.601   1.00 69.44  ? 58  GLU D O   1 
ATOM 5216 C CB  . GLU D 2 58  ? -36.435 1.974   2.948   1.00 67.09  ? 58  GLU D CB  1 
ATOM 5217 C CG  . GLU D 2 58  ? -36.309 0.852   3.907   1.00 73.00  ? 58  GLU D CG  1 
ATOM 5218 C CD  . GLU D 2 58  ? -34.902 0.519   4.328   1.00 75.90  ? 58  GLU D CD  1 
ATOM 5219 O OE1 . GLU D 2 58  ? -34.251 -0.298  3.647   1.00 80.61  ? 58  GLU D OE1 1 
ATOM 5220 O OE2 . GLU D 2 58  ? -34.477 1.041   5.388   1.00 70.32  ? 58  GLU D OE2 1 
ATOM 5221 N N   . ARG D 2 59  ? -34.414 3.958   1.406   1.00 77.72  ? 59  ARG D N   1 
ATOM 5222 C CA  . ARG D 2 59  ? -34.250 4.336   0.011   1.00 77.94  ? 59  ARG D CA  1 
ATOM 5223 C C   . ARG D 2 59  ? -35.162 3.491   -0.869  1.00 78.37  ? 59  ARG D C   1 
ATOM 5224 O O   . ARG D 2 59  ? -35.354 2.295   -0.627  1.00 80.13  ? 59  ARG D O   1 
ATOM 5225 C CB  . ARG D 2 59  ? -32.782 4.167   -0.394  1.00 84.80  ? 59  ARG D CB  1 
ATOM 5226 C CG  . ARG D 2 59  ? -32.240 2.726   -0.346  1.00 96.07  ? 59  ARG D CG  1 
ATOM 5227 C CD  . ARG D 2 59  ? -32.351 2.007   -1.695  1.00 100.98 ? 59  ARG D CD  1 
ATOM 5228 N NE  . ARG D 2 59  ? -32.147 0.563   -1.607  1.00 103.49 ? 59  ARG D NE  1 
ATOM 5229 C CZ  . ARG D 2 59  ? -31.522 -0.167  -2.523  1.00 99.80  ? 59  ARG D CZ  1 
ATOM 5230 N NH1 . ARG D 2 59  ? -30.986 0.382   -3.602  1.00 90.09  ? 59  ARG D NH1 1 
ATOM 5231 N NH2 . ARG D 2 59  ? -31.427 -1.483  -2.351  1.00 103.02 ? 59  ARG D NH2 1 
ATOM 5232 N N   . ALA D 2 60  ? -35.731 4.122   -1.890  1.00 86.66  ? 60  ALA D N   1 
ATOM 5233 C CA  . ALA D 2 60  ? -36.608 3.440   -2.825  1.00 87.46  ? 60  ALA D CA  1 
ATOM 5234 C C   . ALA D 2 60  ? -35.787 2.619   -3.818  1.00 91.65  ? 60  ALA D C   1 
ATOM 5235 O O   . ALA D 2 60  ? -34.556 2.571   -3.760  1.00 93.72  ? 60  ALA D O   1 
ATOM 5236 C CB  . ALA D 2 60  ? -37.499 4.447   -3.546  1.00 87.59  ? 60  ALA D CB  1 
ATOM 5237 N N   . LEU D 2 61  ? -36.479 1.960   -4.745  1.00 83.64  ? 61  LEU D N   1 
ATOM 5238 C CA  . LEU D 2 61  ? -35.801 1.142   -5.743  1.00 80.35  ? 61  LEU D CA  1 
ATOM 5239 C C   . LEU D 2 61  ? -34.988 2.023   -6.683  1.00 76.68  ? 61  LEU D C   1 
ATOM 5240 O O   . LEU D 2 61  ? -35.519 2.951   -7.299  1.00 76.41  ? 61  LEU D O   1 
ATOM 5241 C CB  . LEU D 2 61  ? -36.805 0.304   -6.538  1.00 78.37  ? 61  LEU D CB  1 
ATOM 5242 C CG  . LEU D 2 61  ? -37.940 -0.402  -5.784  1.00 77.14  ? 61  LEU D CG  1 
ATOM 5243 C CD1 . LEU D 2 61  ? -39.146 0.517   -5.588  1.00 73.19  ? 61  LEU D CD1 1 
ATOM 5244 C CD2 . LEU D 2 61  ? -38.352 -1.694  -6.488  1.00 71.19  ? 61  LEU D CD2 1 
ATOM 5245 N N   . GLY D 2 62  ? -33.692 1.730   -6.783  1.00 76.43  ? 62  GLY D N   1 
ATOM 5246 C CA  . GLY D 2 62  ? -32.799 2.457   -7.656  1.00 76.37  ? 62  GLY D CA  1 
ATOM 5247 C C   . GLY D 2 62  ? -32.139 3.672   -7.045  1.00 77.75  ? 62  GLY D C   1 
ATOM 5248 O O   . GLY D 2 62  ? -31.342 4.330   -7.726  1.00 76.11  ? 62  GLY D O   1 
ATOM 5249 N N   . VAL D 2 63  ? -32.438 3.993   -5.794  1.00 80.22  ? 63  VAL D N   1 
ATOM 5250 C CA  . VAL D 2 63  ? -31.853 5.173   -5.156  1.00 79.28  ? 63  VAL D CA  1 
ATOM 5251 C C   . VAL D 2 63  ? -30.466 4.809   -4.632  1.00 79.48  ? 63  VAL D C   1 
ATOM 5252 O O   . VAL D 2 63  ? -30.332 3.812   -3.905  1.00 85.01  ? 63  VAL D O   1 
ATOM 5253 C CB  . VAL D 2 63  ? -32.753 5.677   -4.030  1.00 78.56  ? 63  VAL D CB  1 
ATOM 5254 C CG1 . VAL D 2 63  ? -32.137 6.894   -3.347  1.00 80.58  ? 63  VAL D CG1 1 
ATOM 5255 C CG2 . VAL D 2 63  ? -34.136 6.005   -4.567  1.00 79.64  ? 63  VAL D CG2 1 
ATOM 5256 N N   . PRO D 2 64  ? -29.426 5.568   -4.976  1.00 79.96  ? 64  PRO D N   1 
ATOM 5257 C CA  . PRO D 2 64  ? -28.103 5.293   -4.403  1.00 80.76  ? 64  PRO D CA  1 
ATOM 5258 C C   . PRO D 2 64  ? -28.113 5.545   -2.904  1.00 86.90  ? 64  PRO D C   1 
ATOM 5259 O O   . PRO D 2 64  ? -28.694 6.520   -2.422  1.00 90.72  ? 64  PRO D O   1 
ATOM 5260 C CB  . PRO D 2 64  ? -27.172 6.264   -5.144  1.00 84.38  ? 64  PRO D CB  1 
ATOM 5261 C CG  . PRO D 2 64  ? -28.027 7.041   -6.105  1.00 82.14  ? 64  PRO D CG  1 
ATOM 5262 C CD  . PRO D 2 64  ? -29.458 6.808   -5.768  1.00 81.72  ? 64  PRO D CD  1 
ATOM 5263 N N   . ASP D 2 65  ? -27.466 4.646   -2.163  1.00 88.54  ? 65  ASP D N   1 
ATOM 5264 C CA  . ASP D 2 65  ? -27.595 4.648   -0.707  1.00 91.50  ? 65  ASP D CA  1 
ATOM 5265 C C   . ASP D 2 65  ? -26.858 5.805   -0.034  1.00 93.40  ? 65  ASP D C   1 
ATOM 5266 O O   . ASP D 2 65  ? -26.779 5.824   1.206   1.00 91.19  ? 65  ASP D O   1 
ATOM 5267 C CB  . ASP D 2 65  ? -27.114 3.312   -0.141  1.00 92.62  ? 65  ASP D CB  1 
ATOM 5268 C CG  . ASP D 2 65  ? -28.125 2.683   0.800   1.00 96.58  ? 65  ASP D CG  1 
ATOM 5269 O OD1 . ASP D 2 65  ? -28.855 3.437   1.478   1.00 93.89  ? 65  ASP D OD1 1 
ATOM 5270 O OD2 . ASP D 2 65  ? -28.196 1.437   0.857   1.00 103.28 ? 65  ASP D OD2 1 
ATOM 5271 N N   . ARG D 2 66  ? -26.320 6.766   -0.788  1.00 102.05 ? 66  ARG D N   1 
ATOM 5272 C CA  . ARG D 2 66  ? -25.838 7.997   -0.172  1.00 102.82 ? 66  ARG D CA  1 
ATOM 5273 C C   . ARG D 2 66  ? -26.976 8.753   0.497   1.00 100.09 ? 66  ARG D C   1 
ATOM 5274 O O   . ARG D 2 66  ? -26.746 9.531   1.429   1.00 97.63  ? 66  ARG D O   1 
ATOM 5275 C CB  . ARG D 2 66  ? -25.162 8.877   -1.223  1.00 100.17 ? 66  ARG D CB  1 
ATOM 5276 C CG  . ARG D 2 66  ? -24.496 8.090   -2.338  1.00 102.01 ? 66  ARG D CG  1 
ATOM 5277 C CD  . ARG D 2 66  ? -23.785 8.999   -3.321  1.00 104.52 ? 66  ARG D CD  1 
ATOM 5278 N NE  . ARG D 2 66  ? -24.669 10.044  -3.823  1.00 108.62 ? 66  ARG D NE  1 
ATOM 5279 C CZ  . ARG D 2 66  ? -25.231 10.042  -5.023  1.00 109.09 ? 66  ARG D CZ  1 
ATOM 5280 N NH1 . ARG D 2 66  ? -25.023 9.058   -5.883  1.00 112.20 ? 66  ARG D NH1 1 
ATOM 5281 N NH2 . ARG D 2 66  ? -26.026 11.052  -5.369  1.00 101.67 ? 66  ARG D NH2 1 
ATOM 5282 N N   . PHE D 2 67  ? -28.205 8.528   0.040   1.00 89.63  ? 67  PHE D N   1 
ATOM 5283 C CA  . PHE D 2 67  ? -29.382 9.166   0.605   1.00 82.80  ? 67  PHE D CA  1 
ATOM 5284 C C   . PHE D 2 67  ? -29.870 8.343   1.790   1.00 79.72  ? 67  PHE D C   1 
ATOM 5285 O O   . PHE D 2 67  ? -30.033 7.123   1.680   1.00 81.99  ? 67  PHE D O   1 
ATOM 5286 C CB  . PHE D 2 67  ? -30.482 9.287   -0.451  1.00 82.59  ? 67  PHE D CB  1 
ATOM 5287 C CG  . PHE D 2 67  ? -30.110 10.158  -1.621  1.00 82.58  ? 67  PHE D CG  1 
ATOM 5288 C CD1 . PHE D 2 67  ? -29.359 9.646   -2.671  1.00 83.84  ? 67  PHE D CD1 1 
ATOM 5289 C CD2 . PHE D 2 67  ? -30.507 11.482  -1.673  1.00 78.20  ? 67  PHE D CD2 1 
ATOM 5290 C CE1 . PHE D 2 67  ? -29.015 10.441  -3.751  1.00 86.27  ? 67  PHE D CE1 1 
ATOM 5291 C CE2 . PHE D 2 67  ? -30.166 12.282  -2.750  1.00 81.44  ? 67  PHE D CE2 1 
ATOM 5292 C CZ  . PHE D 2 67  ? -29.419 11.761  -3.789  1.00 86.76  ? 67  PHE D CZ  1 
ATOM 5293 N N   . SER D 2 68  ? -30.096 9.009   2.919   1.00 75.37  ? 68  SER D N   1 
ATOM 5294 C CA  . SER D 2 68  ? -30.490 8.331   4.146   1.00 75.37  ? 68  SER D CA  1 
ATOM 5295 C C   . SER D 2 68  ? -31.549 9.145   4.872   1.00 70.15  ? 68  SER D C   1 
ATOM 5296 O O   . SER D 2 68  ? -31.438 10.369  4.984   1.00 68.87  ? 68  SER D O   1 
ATOM 5297 C CB  . SER D 2 68  ? -29.286 8.102   5.068   1.00 80.50  ? 68  SER D CB  1 
ATOM 5298 O OG  . SER D 2 68  ? -28.740 9.334   5.509   1.00 82.61  ? 68  SER D OG  1 
ATOM 5299 N N   . GLY D 2 69  ? -32.570 8.451   5.371   1.00 66.17  ? 69  GLY D N   1 
ATOM 5300 C CA  . GLY D 2 69  ? -33.623 9.074   6.136   1.00 64.97  ? 69  GLY D CA  1 
ATOM 5301 C C   . GLY D 2 69  ? -33.492 8.794   7.620   1.00 64.54  ? 69  GLY D C   1 
ATOM 5302 O O   . GLY D 2 69  ? -32.831 7.848   8.039   1.00 72.08  ? 69  GLY D O   1 
ATOM 5303 N N   . SER D 2 70  ? -34.138 9.640   8.414   1.00 59.38  ? 70  SER D N   1 
ATOM 5304 C CA  . SER D 2 70  ? -34.111 9.522   9.867   1.00 57.14  ? 70  SER D CA  1 
ATOM 5305 C C   . SER D 2 70  ? -35.194 10.424  10.435  1.00 56.96  ? 70  SER D C   1 
ATOM 5306 O O   . SER D 2 70  ? -35.736 11.286  9.739   1.00 64.91  ? 70  SER D O   1 
ATOM 5307 C CB  . SER D 2 70  ? -32.737 9.889   10.439  1.00 57.63  ? 70  SER D CB  1 
ATOM 5308 O OG  . SER D 2 70  ? -32.225 11.057  9.827   1.00 57.40  ? 70  SER D OG  1 
ATOM 5309 N N   . GLY D 2 71  ? -35.499 10.214  11.703  1.00 57.34  ? 71  GLY D N   1 
ATOM 5310 C CA  . GLY D 2 71  ? -36.456 11.067  12.372  1.00 57.23  ? 71  GLY D CA  1 
ATOM 5311 C C   . GLY D 2 71  ? -37.708 10.297  12.772  1.00 61.78  ? 71  GLY D C   1 
ATOM 5312 O O   . GLY D 2 71  ? -38.080 9.282   12.160  1.00 65.21  ? 71  GLY D O   1 
ATOM 5313 N N   . SER D 2 72  ? -38.372 10.791  13.814  1.00 65.56  ? 72  SER D N   1 
ATOM 5314 C CA  . SER D 2 72  ? -39.594 10.177  14.307  1.00 73.01  ? 72  SER D CA  1 
ATOM 5315 C C   . SER D 2 72  ? -40.475 11.256  14.912  1.00 81.48  ? 72  SER D C   1 
ATOM 5316 O O   . SER D 2 72  ? -40.013 12.351  15.247  1.00 81.71  ? 72  SER D O   1 
ATOM 5317 C CB  . SER D 2 72  ? -39.301 9.081   15.340  1.00 83.04  ? 72  SER D CB  1 
ATOM 5318 O OG  . SER D 2 72  ? -40.502 8.548   15.866  1.00 92.01  ? 72  SER D OG  1 
ATOM 5319 N N   . GLY D 2 73  ? -41.757 10.933  15.048  1.00 107.39 ? 73  GLY D N   1 
ATOM 5320 C CA  . GLY D 2 73  ? -42.706 11.853  15.644  1.00 107.31 ? 73  GLY D CA  1 
ATOM 5321 C C   . GLY D 2 73  ? -43.095 12.999  14.733  1.00 106.78 ? 73  GLY D C   1 
ATOM 5322 O O   . GLY D 2 73  ? -43.924 12.833  13.833  1.00 106.10 ? 73  GLY D O   1 
ATOM 5323 N N   . ARG D 2 74  ? -42.495 14.166  14.954  1.00 86.07  ? 74  ARG D N   1 
ATOM 5324 C CA  . ARG D 2 74  ? -42.842 15.369  14.211  1.00 76.27  ? 74  ARG D CA  1 
ATOM 5325 C C   . ARG D 2 74  ? -41.685 15.962  13.422  1.00 70.24  ? 74  ARG D C   1 
ATOM 5326 O O   . ARG D 2 74  ? -41.927 16.608  12.401  1.00 74.06  ? 74  ARG D O   1 
ATOM 5327 C CB  . ARG D 2 74  ? -43.394 16.441  15.163  1.00 72.84  ? 74  ARG D CB  1 
ATOM 5328 C CG  . ARG D 2 74  ? -44.682 16.032  15.855  1.00 74.35  ? 74  ARG D CG  1 
ATOM 5329 C CD  . ARG D 2 74  ? -44.876 16.776  17.164  1.00 73.39  ? 74  ARG D CD  1 
ATOM 5330 N NE  . ARG D 2 74  ? -45.641 18.003  16.982  1.00 73.38  ? 74  ARG D NE  1 
ATOM 5331 C CZ  . ARG D 2 74  ? -46.817 18.240  17.548  1.00 73.04  ? 74  ARG D CZ  1 
ATOM 5332 N NH1 . ARG D 2 74  ? -47.393 17.350  18.340  1.00 69.12  ? 74  ARG D NH1 1 
ATOM 5333 N NH2 . ARG D 2 74  ? -47.430 19.396  17.312  1.00 70.64  ? 74  ARG D NH2 1 
ATOM 5334 N N   . ASP D 2 75  ? -40.446 15.767  13.861  1.00 67.18  ? 75  ASP D N   1 
ATOM 5335 C CA  . ASP D 2 75  ? -39.275 16.260  13.152  1.00 66.33  ? 75  ASP D CA  1 
ATOM 5336 C C   . ASP D 2 75  ? -38.614 15.125  12.384  1.00 64.81  ? 75  ASP D C   1 
ATOM 5337 O O   . ASP D 2 75  ? -38.536 13.993  12.871  1.00 68.77  ? 75  ASP D O   1 
ATOM 5338 C CB  . ASP D 2 75  ? -38.273 16.893  14.119  1.00 70.60  ? 75  ASP D CB  1 
ATOM 5339 C CG  . ASP D 2 75  ? -38.938 17.799  15.132  1.00 71.52  ? 75  ASP D CG  1 
ATOM 5340 O OD1 . ASP D 2 75  ? -39.380 18.899  14.739  1.00 70.45  ? 75  ASP D OD1 1 
ATOM 5341 O OD2 . ASP D 2 75  ? -39.021 17.418  16.319  1.00 73.40  ? 75  ASP D OD2 1 
ATOM 5342 N N   . PHE D 2 76  ? -38.136 15.435  11.180  1.00 62.94  ? 76  PHE D N   1 
ATOM 5343 C CA  . PHE D 2 76  ? -37.574 14.435  10.286  1.00 61.73  ? 76  PHE D CA  1 
ATOM 5344 C C   . PHE D 2 76  ? -36.362 15.023  9.577   1.00 60.35  ? 76  PHE D C   1 
ATOM 5345 O O   . PHE D 2 76  ? -36.165 16.239  9.547   1.00 66.33  ? 76  PHE D O   1 
ATOM 5346 C CB  . PHE D 2 76  ? -38.614 13.955  9.264   1.00 63.30  ? 76  PHE D CB  1 
ATOM 5347 C CG  . PHE D 2 76  ? -39.717 13.129  9.864   1.00 63.65  ? 76  PHE D CG  1 
ATOM 5348 C CD1 . PHE D 2 76  ? -40.833 13.735  10.422  1.00 67.52  ? 76  PHE D CD1 1 
ATOM 5349 C CD2 . PHE D 2 76  ? -39.633 11.748  9.882   1.00 61.62  ? 76  PHE D CD2 1 
ATOM 5350 C CE1 . PHE D 2 76  ? -41.847 12.977  10.980  1.00 70.04  ? 76  PHE D CE1 1 
ATOM 5351 C CE2 . PHE D 2 76  ? -40.642 10.988  10.437  1.00 69.61  ? 76  PHE D CE2 1 
ATOM 5352 C CZ  . PHE D 2 76  ? -41.751 11.603  10.986  1.00 70.83  ? 76  PHE D CZ  1 
ATOM 5353 N N   . THR D 2 77  ? -35.547 14.142  8.999   1.00 58.77  ? 77  THR D N   1 
ATOM 5354 C CA  . THR D 2 77  ? -34.320 14.555  8.333   1.00 60.15  ? 77  THR D CA  1 
ATOM 5355 C C   . THR D 2 77  ? -34.053 13.676  7.120   1.00 63.21  ? 77  THR D C   1 
ATOM 5356 O O   . THR D 2 77  ? -34.197 12.452  7.181   1.00 66.55  ? 77  THR D O   1 
ATOM 5357 C CB  . THR D 2 77  ? -33.115 14.495  9.283   1.00 60.71  ? 77  THR D CB  1 
ATOM 5358 O OG1 . THR D 2 77  ? -33.477 15.046  10.555  1.00 63.38  ? 77  THR D OG1 1 
ATOM 5359 C CG2 . THR D 2 77  ? -31.947 15.286  8.711   1.00 65.49  ? 77  THR D CG2 1 
ATOM 5360 N N   . LEU D 2 78  ? -33.664 14.315  6.019   1.00 64.28  ? 78  LEU D N   1 
ATOM 5361 C CA  . LEU D 2 78  ? -33.205 13.644  4.807   1.00 65.98  ? 78  LEU D CA  1 
ATOM 5362 C C   . LEU D 2 78  ? -31.754 14.052  4.605   1.00 65.53  ? 78  LEU D C   1 
ATOM 5363 O O   . LEU D 2 78  ? -31.473 15.195  4.229   1.00 69.59  ? 78  LEU D O   1 
ATOM 5364 C CB  . LEU D 2 78  ? -34.070 14.025  3.602   1.00 67.48  ? 78  LEU D CB  1 
ATOM 5365 C CG  . LEU D 2 78  ? -33.818 13.428  2.209   1.00 68.89  ? 78  LEU D CG  1 
ATOM 5366 C CD1 . LEU D 2 78  ? -32.729 14.173  1.437   1.00 69.21  ? 78  LEU D CD1 1 
ATOM 5367 C CD2 . LEU D 2 78  ? -33.493 11.948  2.305   1.00 71.47  ? 78  LEU D CD2 1 
ATOM 5368 N N   . LYS D 2 79  ? -30.835 13.126  4.859   1.00 64.56  ? 79  LYS D N   1 
ATOM 5369 C CA  . LYS D 2 79  ? -29.409 13.404  4.799   1.00 69.78  ? 79  LYS D CA  1 
ATOM 5370 C C   . LYS D 2 79  ? -28.783 12.743  3.580   1.00 72.43  ? 79  LYS D C   1 
ATOM 5371 O O   . LYS D 2 79  ? -29.126 11.611  3.225   1.00 79.14  ? 79  LYS D O   1 
ATOM 5372 C CB  . LYS D 2 79  ? -28.701 12.926  6.070   1.00 73.72  ? 79  LYS D CB  1 
ATOM 5373 C CG  . LYS D 2 79  ? -28.833 13.889  7.238   1.00 75.89  ? 79  LYS D CG  1 
ATOM 5374 C CD  . LYS D 2 79  ? -27.562 13.949  8.070   1.00 77.84  ? 79  LYS D CD  1 
ATOM 5375 C CE  . LYS D 2 79  ? -27.807 14.686  9.379   1.00 76.54  ? 79  LYS D CE  1 
ATOM 5376 N NZ  . LYS D 2 79  ? -26.550 15.244  9.949   1.00 70.56  ? 79  LYS D NZ  1 
ATOM 5377 N N   . ILE D 2 80  ? -27.868 13.467  2.943   1.00 73.10  ? 80  ILE D N   1 
ATOM 5378 C CA  . ILE D 2 80  ? -27.044 12.960  1.854   1.00 82.97  ? 80  ILE D CA  1 
ATOM 5379 C C   . ILE D 2 80  ? -25.603 12.970  2.339   1.00 88.36  ? 80  ILE D C   1 
ATOM 5380 O O   . ILE D 2 80  ? -25.109 14.008  2.794   1.00 89.59  ? 80  ILE D O   1 
ATOM 5381 C CB  . ILE D 2 80  ? -27.196 13.814  0.582   1.00 86.39  ? 80  ILE D CB  1 
ATOM 5382 C CG1 . ILE D 2 80  ? -28.674 14.097  0.304   1.00 80.55  ? 80  ILE D CG1 1 
ATOM 5383 C CG2 . ILE D 2 80  ? -26.549 13.116  -0.609  1.00 92.71  ? 80  ILE D CG2 1 
ATOM 5384 C CD1 . ILE D 2 80  ? -28.905 15.037  -0.859  1.00 72.44  ? 80  ILE D CD1 1 
ATOM 5385 N N   . SER D 2 81  ? -24.934 11.821  2.250   1.00 102.99 ? 81  SER D N   1 
ATOM 5386 C CA  . SER D 2 81  ? -23.573 11.694  2.758   1.00 105.99 ? 81  SER D CA  1 
ATOM 5387 C C   . SER D 2 81  ? -22.524 12.131  1.741   1.00 103.37 ? 81  SER D C   1 
ATOM 5388 O O   . SER D 2 81  ? -21.551 12.801  2.104   1.00 103.31 ? 81  SER D O   1 
ATOM 5389 C CB  . SER D 2 81  ? -23.311 10.250  3.192   1.00 106.52 ? 81  SER D CB  1 
ATOM 5390 O OG  . SER D 2 81  ? -24.475 9.671   3.759   1.00 104.36 ? 81  SER D OG  1 
ATOM 5391 N N   . ARG D 2 82  ? -22.698 11.761  0.474   1.00 97.31  ? 82  ARG D N   1 
ATOM 5392 C CA  . ARG D 2 82  ? -21.778 12.139  -0.596  1.00 101.28 ? 82  ARG D CA  1 
ATOM 5393 C C   . ARG D 2 82  ? -22.596 12.726  -1.737  1.00 103.33 ? 82  ARG D C   1 
ATOM 5394 O O   . ARG D 2 82  ? -23.364 12.010  -2.387  1.00 107.17 ? 82  ARG D O   1 
ATOM 5395 C CB  . ARG D 2 82  ? -20.955 10.941  -1.073  1.00 111.67 ? 82  ARG D CB  1 
ATOM 5396 C CG  . ARG D 2 82  ? -19.541 10.897  -0.510  1.00 113.79 ? 82  ARG D CG  1 
ATOM 5397 C CD  . ARG D 2 82  ? -18.564 10.248  -1.482  1.00 121.22 ? 82  ARG D CD  1 
ATOM 5398 N NE  . ARG D 2 82  ? -17.215 10.168  -0.930  1.00 128.70 ? 82  ARG D NE  1 
ATOM 5399 C CZ  . ARG D 2 82  ? -16.192 10.908  -1.336  1.00 131.91 ? 82  ARG D CZ  1 
ATOM 5400 N NH1 . ARG D 2 82  ? -16.326 11.806  -2.299  1.00 129.74 ? 82  ARG D NH1 1 
ATOM 5401 N NH2 . ARG D 2 82  ? -15.004 10.745  -0.759  1.00 134.52 ? 82  ARG D NH2 1 
ATOM 5402 N N   . VAL D 2 83  ? -22.431 14.021  -1.985  1.00 103.76 ? 83  VAL D N   1 
ATOM 5403 C CA  . VAL D 2 83  ? -23.209 14.722  -2.999  1.00 99.13  ? 83  VAL D CA  1 
ATOM 5404 C C   . VAL D 2 83  ? -22.458 14.681  -4.322  1.00 99.03  ? 83  VAL D C   1 
ATOM 5405 O O   . VAL D 2 83  ? -21.294 15.094  -4.403  1.00 97.54  ? 83  VAL D O   1 
ATOM 5406 C CB  . VAL D 2 83  ? -23.493 16.171  -2.570  1.00 93.13  ? 83  VAL D CB  1 
ATOM 5407 C CG1 . VAL D 2 83  ? -23.895 17.019  -3.771  1.00 93.29  ? 83  VAL D CG1 1 
ATOM 5408 C CG2 . VAL D 2 83  ? -24.574 16.202  -1.501  1.00 88.81  ? 83  VAL D CG2 1 
ATOM 5409 N N   . GLU D 2 84  ? -23.121 14.178  -5.359  1.00 98.43  ? 84  GLU D N   1 
ATOM 5410 C CA  . GLU D 2 84  ? -22.583 14.179  -6.708  1.00 96.91  ? 84  GLU D CA  1 
ATOM 5411 C C   . GLU D 2 84  ? -23.261 15.275  -7.527  1.00 98.45  ? 84  GLU D C   1 
ATOM 5412 O O   . GLU D 2 84  ? -24.096 16.034  -7.031  1.00 96.16  ? 84  GLU D O   1 
ATOM 5413 C CB  . GLU D 2 84  ? -22.754 12.802  -7.353  1.00 101.04 ? 84  GLU D CB  1 
ATOM 5414 C CG  . GLU D 2 84  ? -21.960 11.707  -6.659  1.00 105.05 ? 84  GLU D CG  1 
ATOM 5415 C CD  . GLU D 2 84  ? -22.171 10.346  -7.284  1.00 107.89 ? 84  GLU D CD  1 
ATOM 5416 O OE1 . GLU D 2 84  ? -22.986 10.242  -8.224  1.00 110.03 ? 84  GLU D OE1 1 
ATOM 5417 O OE2 . GLU D 2 84  ? -21.519 9.379   -6.838  1.00 102.54 ? 84  GLU D OE2 1 
ATOM 5418 N N   . ALA D 2 85  ? -22.893 15.353  -8.807  1.00 104.06 ? 85  ALA D N   1 
ATOM 5419 C CA  . ALA D 2 85  ? -23.383 16.442  -9.646  1.00 110.64 ? 85  ALA D CA  1 
ATOM 5420 C C   . ALA D 2 85  ? -24.876 16.325  -9.926  1.00 107.44 ? 85  ALA D C   1 
ATOM 5421 O O   . ALA D 2 85  ? -25.539 17.339  -10.171 1.00 101.91 ? 85  ALA D O   1 
ATOM 5422 C CB  . ALA D 2 85  ? -22.600 16.488  -10.957 1.00 119.30 ? 85  ALA D CB  1 
ATOM 5423 N N   . GLN D 2 86  ? -25.422 15.110  -9.890  1.00 112.77 ? 86  GLN D N   1 
ATOM 5424 C CA  . GLN D 2 86  ? -26.822 14.893  -10.229 1.00 107.45 ? 86  GLN D CA  1 
ATOM 5425 C C   . GLN D 2 86  ? -27.780 15.267  -9.106  1.00 107.71 ? 86  GLN D C   1 
ATOM 5426 O O   . GLN D 2 86  ? -28.990 15.336  -9.347  1.00 109.49 ? 86  GLN D O   1 
ATOM 5427 C CB  . GLN D 2 86  ? -27.045 13.429  -10.614 1.00 102.12 ? 86  GLN D CB  1 
ATOM 5428 C CG  . GLN D 2 86  ? -26.769 12.456  -9.482  1.00 104.52 ? 86  GLN D CG  1 
ATOM 5429 C CD  . GLN D 2 86  ? -26.897 11.009  -9.910  1.00 115.81 ? 86  GLN D CD  1 
ATOM 5430 O OE1 . GLN D 2 86  ? -26.603 10.659  -11.053 1.00 122.02 ? 86  GLN D OE1 1 
ATOM 5431 N NE2 . GLN D 2 86  ? -27.335 10.158  -8.991  1.00 116.22 ? 86  GLN D NE2 1 
ATOM 5432 N N   . ASP D 2 87  ? -27.278 15.515  -7.897  1.00 97.93  ? 87  ASP D N   1 
ATOM 5433 C CA  . ASP D 2 87  ? -28.150 15.771  -6.757  1.00 90.90  ? 87  ASP D CA  1 
ATOM 5434 C C   . ASP D 2 87  ? -28.829 17.134  -6.805  1.00 89.52  ? 87  ASP D C   1 
ATOM 5435 O O   . ASP D 2 87  ? -29.587 17.451  -5.882  1.00 85.70  ? 87  ASP D O   1 
ATOM 5436 C CB  . ASP D 2 87  ? -27.358 15.631  -5.458  1.00 90.72  ? 87  ASP D CB  1 
ATOM 5437 C CG  . ASP D 2 87  ? -26.729 14.261  -5.308  1.00 94.56  ? 87  ASP D CG  1 
ATOM 5438 O OD1 . ASP D 2 87  ? -26.133 13.768  -6.288  1.00 99.97  ? 87  ASP D OD1 1 
ATOM 5439 O OD2 . ASP D 2 87  ? -26.834 13.677  -4.209  1.00 90.12  ? 87  ASP D OD2 1 
ATOM 5440 N N   . VAL D 2 88  ? -28.591 17.941  -7.839  1.00 95.63  ? 88  VAL D N   1 
ATOM 5441 C CA  . VAL D 2 88  ? -29.245 19.240  -7.931  1.00 89.33  ? 88  VAL D CA  1 
ATOM 5442 C C   . VAL D 2 88  ? -30.732 19.049  -8.200  1.00 82.66  ? 88  VAL D C   1 
ATOM 5443 O O   . VAL D 2 88  ? -31.143 18.124  -8.914  1.00 84.70  ? 88  VAL D O   1 
ATOM 5444 C CB  . VAL D 2 88  ? -28.584 20.103  -9.019  1.00 90.48  ? 88  VAL D CB  1 
ATOM 5445 C CG1 . VAL D 2 88  ? -27.288 20.702  -8.500  1.00 95.03  ? 88  VAL D CG1 1 
ATOM 5446 C CG2 . VAL D 2 88  ? -28.327 19.278  -10.271 1.00 94.30  ? 88  VAL D CG2 1 
ATOM 5447 N N   . GLY D 2 89  ? -31.542 19.917  -7.618  1.00 76.38  ? 89  GLY D N   1 
ATOM 5448 C CA  . GLY D 2 89  ? -32.980 19.845  -7.766  1.00 74.41  ? 89  GLY D CA  1 
ATOM 5449 C C   . GLY D 2 89  ? -33.655 20.363  -6.512  1.00 72.10  ? 89  GLY D C   1 
ATOM 5450 O O   . GLY D 2 89  ? -33.038 21.020  -5.679  1.00 75.19  ? 89  GLY D O   1 
ATOM 5451 N N   . THR D 2 90  ? -34.942 20.049  -6.391  1.00 69.00  ? 90  THR D N   1 
ATOM 5452 C CA  . THR D 2 90  ? -35.738 20.457  -5.242  1.00 70.72  ? 90  THR D CA  1 
ATOM 5453 C C   . THR D 2 90  ? -36.216 19.221  -4.497  1.00 72.19  ? 90  THR D C   1 
ATOM 5454 O O   . THR D 2 90  ? -36.756 18.292  -5.105  1.00 69.59  ? 90  THR D O   1 
ATOM 5455 C CB  . THR D 2 90  ? -36.931 21.318  -5.664  1.00 71.99  ? 90  THR D CB  1 
ATOM 5456 O OG1 . THR D 2 90  ? -36.530 22.215  -6.706  1.00 75.82  ? 90  THR D OG1 1 
ATOM 5457 C CG2 . THR D 2 90  ? -37.436 22.129  -4.482  1.00 69.69  ? 90  THR D CG2 1 
ATOM 5458 N N   . TYR D 2 91  ? -36.021 19.215  -3.183  1.00 69.68  ? 91  TYR D N   1 
ATOM 5459 C CA  . TYR D 2 91  ? -36.306 18.056  -2.347  1.00 61.02  ? 91  TYR D CA  1 
ATOM 5460 C C   . TYR D 2 91  ? -37.549 18.342  -1.515  1.00 60.18  ? 91  TYR D C   1 
ATOM 5461 O O   . TYR D 2 91  ? -37.609 19.355  -0.810  1.00 63.08  ? 91  TYR D O   1 
ATOM 5462 C CB  . TYR D 2 91  ? -35.113 17.736  -1.449  1.00 59.57  ? 91  TYR D CB  1 
ATOM 5463 C CG  . TYR D 2 91  ? -33.918 17.171  -2.191  1.00 61.14  ? 91  TYR D CG  1 
ATOM 5464 C CD1 . TYR D 2 91  ? -33.033 18.009  -2.858  1.00 64.70  ? 91  TYR D CD1 1 
ATOM 5465 C CD2 . TYR D 2 91  ? -33.668 15.804  -2.214  1.00 60.61  ? 91  TYR D CD2 1 
ATOM 5466 C CE1 . TYR D 2 91  ? -31.938 17.502  -3.535  1.00 68.81  ? 91  TYR D CE1 1 
ATOM 5467 C CE2 . TYR D 2 91  ? -32.574 15.290  -2.886  1.00 63.88  ? 91  TYR D CE2 1 
ATOM 5468 C CZ  . TYR D 2 91  ? -31.712 16.142  -3.544  1.00 68.32  ? 91  TYR D CZ  1 
ATOM 5469 O OH  . TYR D 2 91  ? -30.624 15.629  -4.213  1.00 73.24  ? 91  TYR D OH  1 
ATOM 5470 N N   . TYR D 2 92  ? -38.534 17.452  -1.600  1.00 55.29  ? 92  TYR D N   1 
ATOM 5471 C CA  . TYR D 2 92  ? -39.820 17.638  -0.945  1.00 56.91  ? 92  TYR D CA  1 
ATOM 5472 C C   . TYR D 2 92  ? -40.087 16.487  0.014   1.00 59.95  ? 92  TYR D C   1 
ATOM 5473 O O   . TYR D 2 92  ? -39.811 15.326  -0.306  1.00 65.86  ? 92  TYR D O   1 
ATOM 5474 C CB  . TYR D 2 92  ? -40.957 17.711  -1.972  1.00 59.74  ? 92  TYR D CB  1 
ATOM 5475 C CG  . TYR D 2 92  ? -40.926 18.930  -2.865  1.00 61.35  ? 92  TYR D CG  1 
ATOM 5476 C CD1 . TYR D 2 92  ? -40.210 18.921  -4.054  1.00 64.18  ? 92  TYR D CD1 1 
ATOM 5477 C CD2 . TYR D 2 92  ? -41.606 20.091  -2.518  1.00 58.79  ? 92  TYR D CD2 1 
ATOM 5478 C CE1 . TYR D 2 92  ? -40.178 20.027  -4.879  1.00 68.07  ? 92  TYR D CE1 1 
ATOM 5479 C CE2 . TYR D 2 92  ? -41.576 21.205  -3.335  1.00 59.44  ? 92  TYR D CE2 1 
ATOM 5480 C CZ  . TYR D 2 92  ? -40.860 21.168  -4.513  1.00 63.00  ? 92  TYR D CZ  1 
ATOM 5481 O OH  . TYR D 2 92  ? -40.827 22.276  -5.329  1.00 65.30  ? 92  TYR D OH  1 
ATOM 5482 N N   . CYS D 2 93  ? -40.622 16.809  1.189   1.00 57.64  ? 93  CYS D N   1 
ATOM 5483 C CA  . CYS D 2 93  ? -41.183 15.813  2.090   1.00 58.50  ? 93  CYS D CA  1 
ATOM 5484 C C   . CYS D 2 93  ? -42.700 15.808  1.946   1.00 55.25  ? 93  CYS D C   1 
ATOM 5485 O O   . CYS D 2 93  ? -43.306 16.811  1.563   1.00 61.44  ? 93  CYS D O   1 
ATOM 5486 C CB  . CYS D 2 93  ? -40.780 16.075  3.550   1.00 62.03  ? 93  CYS D CB  1 
ATOM 5487 S SG  . CYS D 2 93  ? -41.348 17.644  4.280   1.00 53.53  ? 93  CYS D SG  1 
ATOM 5488 N N   . LEU D 2 94  ? -43.309 14.659  2.233   1.00 52.80  ? 94  LEU D N   1 
ATOM 5489 C CA  . LEU D 2 94  ? -44.749 14.504  2.072   1.00 54.12  ? 94  LEU D CA  1 
ATOM 5490 C C   . LEU D 2 94  ? -45.269 13.558  3.141   1.00 52.61  ? 94  LEU D C   1 
ATOM 5491 O O   . LEU D 2 94  ? -44.734 12.457  3.308   1.00 58.35  ? 94  LEU D O   1 
ATOM 5492 C CB  . LEU D 2 94  ? -45.102 13.970  0.677   1.00 58.75  ? 94  LEU D CB  1 
ATOM 5493 C CG  . LEU D 2 94  ? -46.436 13.227  0.575   1.00 56.71  ? 94  LEU D CG  1 
ATOM 5494 C CD1 . LEU D 2 94  ? -47.594 14.212  0.606   1.00 59.27  ? 94  LEU D CD1 1 
ATOM 5495 C CD2 . LEU D 2 94  ? -46.499 12.361  -0.671  1.00 53.21  ? 94  LEU D CD2 1 
ATOM 5496 N N   . GLN D 2 95  ? -46.304 13.985  3.856   1.00 52.49  ? 95  GLN D N   1 
ATOM 5497 C CA  . GLN D 2 95  ? -46.934 13.148  4.863   1.00 54.51  ? 95  GLN D CA  1 
ATOM 5498 C C   . GLN D 2 95  ? -48.055 12.337  4.229   1.00 63.09  ? 95  GLN D C   1 
ATOM 5499 O O   . GLN D 2 95  ? -48.717 12.782  3.289   1.00 67.57  ? 95  GLN D O   1 
ATOM 5500 C CB  . GLN D 2 95  ? -47.494 13.984  6.013   1.00 58.88  ? 95  GLN D CB  1 
ATOM 5501 C CG  . GLN D 2 95  ? -48.553 14.984  5.584   1.00 66.70  ? 95  GLN D CG  1 
ATOM 5502 C CD  . GLN D 2 95  ? -49.950 14.547  5.984   1.00 72.56  ? 95  GLN D CD  1 
ATOM 5503 O OE1 . GLN D 2 95  ? -50.142 13.454  6.516   1.00 71.00  ? 95  GLN D OE1 1 
ATOM 5504 N NE2 . GLN D 2 95  ? -50.935 15.397  5.724   1.00 76.41  ? 95  GLN D NE2 1 
ATOM 5505 N N   . THR D 2 96  ? -48.258 11.132  4.753   1.00 63.71  ? 96  THR D N   1 
ATOM 5506 C CA  . THR D 2 96  ? -49.338 10.268  4.304   1.00 62.58  ? 96  THR D CA  1 
ATOM 5507 C C   . THR D 2 96  ? -50.251 9.826   5.435   1.00 64.55  ? 96  THR D C   1 
ATOM 5508 O O   . THR D 2 96  ? -51.137 8.995   5.202   1.00 68.89  ? 96  THR D O   1 
ATOM 5509 C CB  . THR D 2 96  ? -48.774 9.030   3.593   1.00 58.88  ? 96  THR D CB  1 
ATOM 5510 O OG1 . THR D 2 96  ? -47.615 8.562   4.294   1.00 62.09  ? 96  THR D OG1 1 
ATOM 5511 C CG2 . THR D 2 96  ? -48.411 9.358   2.161   1.00 59.93  ? 96  THR D CG2 1 
ATOM 5512 N N   . ARG D 2 97  ? -50.075 10.362  6.644   1.00 64.14  ? 97  ARG D N   1 
ATOM 5513 C CA  . ARG D 2 97  ? -50.807 9.842   7.792   1.00 69.09  ? 97  ARG D CA  1 
ATOM 5514 C C   . ARG D 2 97  ? -52.294 10.160  7.711   1.00 69.28  ? 97  ARG D C   1 
ATOM 5515 O O   . ARG D 2 97  ? -53.135 9.267   7.868   1.00 77.23  ? 97  ARG D O   1 
ATOM 5516 C CB  . ARG D 2 97  ? -50.214 10.380  9.093   1.00 75.55  ? 97  ARG D CB  1 
ATOM 5517 C CG  . ARG D 2 97  ? -50.364 9.391   10.238  1.00 80.38  ? 97  ARG D CG  1 
ATOM 5518 C CD  . ARG D 2 97  ? -50.549 10.097  11.568  1.00 88.84  ? 97  ARG D CD  1 
ATOM 5519 N NE  . ARG D 2 97  ? -50.452 9.174   12.691  1.00 95.28  ? 97  ARG D NE  1 
ATOM 5520 C CZ  . ARG D 2 97  ? -51.482 8.495   13.177  1.00 96.72  ? 97  ARG D CZ  1 
ATOM 5521 N NH1 . ARG D 2 97  ? -52.692 8.613   12.655  1.00 90.87  ? 97  ARG D NH1 1 
ATOM 5522 N NH2 . ARG D 2 97  ? -51.296 7.680   14.211  1.00 99.85  ? 97  ARG D NH2 1 
ATOM 5523 N N   . GLN D 2 98  ? -52.643 11.423  7.490   1.00 69.93  ? 98  GLN D N   1 
ATOM 5524 C CA  . GLN D 2 98  ? -54.041 11.815  7.584   1.00 78.25  ? 98  GLN D CA  1 
ATOM 5525 C C   . GLN D 2 98  ? -54.279 13.074  6.764   1.00 84.41  ? 98  GLN D C   1 
ATOM 5526 O O   . GLN D 2 98  ? -53.343 13.740  6.313   1.00 83.55  ? 98  GLN D O   1 
ATOM 5527 C CB  . GLN D 2 98  ? -54.453 12.033  9.043   1.00 82.08  ? 98  GLN D CB  1 
ATOM 5528 C CG  . GLN D 2 98  ? -53.891 13.302  9.658   1.00 87.54  ? 98  GLN D CG  1 
ATOM 5529 C CD  . GLN D 2 98  ? -54.939 14.389  9.760   1.00 86.21  ? 98  GLN D CD  1 
ATOM 5530 O OE1 . GLN D 2 98  ? -56.135 14.110  9.720   1.00 90.07  ? 98  GLN D OE1 1 
ATOM 5531 N NE2 . GLN D 2 98  ? -54.498 15.633  9.891   1.00 84.18  ? 98  GLN D NE2 1 
ATOM 5532 N N   . GLY D 2 99  ? -55.564 13.389  6.587   1.00 99.36  ? 99  GLY D N   1 
ATOM 5533 C CA  . GLY D 2 99  ? -56.104 14.508  5.848   1.00 101.37 ? 99  GLY D CA  1 
ATOM 5534 C C   . GLY D 2 99  ? -55.579 14.545  4.423   1.00 101.56 ? 99  GLY D C   1 
ATOM 5535 O O   . GLY D 2 99  ? -55.102 13.551  3.868   1.00 100.92 ? 99  GLY D O   1 
ATOM 5536 N N   . ALA D 2 100 ? -55.690 15.729  3.825   1.00 87.99  ? 100 ALA D N   1 
ATOM 5537 C CA  . ALA D 2 100 ? -55.036 15.969  2.549   1.00 78.37  ? 100 ALA D CA  1 
ATOM 5538 C C   . ALA D 2 100 ? -53.537 15.760  2.702   1.00 74.68  ? 100 ALA D C   1 
ATOM 5539 O O   . ALA D 2 100 ? -52.908 16.334  3.595   1.00 77.50  ? 100 ALA D O   1 
ATOM 5540 C CB  . ALA D 2 100 ? -55.331 17.385  2.055   1.00 75.99  ? 100 ALA D CB  1 
ATOM 5541 N N   . PHE D 2 101 ? -52.972 14.910  1.852   1.00 70.82  ? 101 PHE D N   1 
ATOM 5542 C CA  . PHE D 2 101 ? -51.543 14.630  1.911   1.00 68.59  ? 101 PHE D CA  1 
ATOM 5543 C C   . PHE D 2 101 ? -50.765 15.905  1.617   1.00 69.08  ? 101 PHE D C   1 
ATOM 5544 O O   . PHE D 2 101 ? -50.816 16.430  0.500   1.00 72.60  ? 101 PHE D O   1 
ATOM 5545 C CB  . PHE D 2 101 ? -51.176 13.528  0.923   1.00 67.19  ? 101 PHE D CB  1 
ATOM 5546 C CG  . PHE D 2 101 ? -51.854 12.214  1.195   1.00 67.81  ? 101 PHE D CG  1 
ATOM 5547 C CD1 . PHE D 2 101 ? -52.423 11.945  2.432   1.00 69.69  ? 101 PHE D CD1 1 
ATOM 5548 C CD2 . PHE D 2 101 ? -51.920 11.245  0.210   1.00 69.46  ? 101 PHE D CD2 1 
ATOM 5549 C CE1 . PHE D 2 101 ? -53.041 10.737  2.677   1.00 67.17  ? 101 PHE D CE1 1 
ATOM 5550 C CE2 . PHE D 2 101 ? -52.537 10.035  0.449   1.00 73.65  ? 101 PHE D CE2 1 
ATOM 5551 C CZ  . PHE D 2 101 ? -53.099 9.781   1.684   1.00 73.14  ? 101 PHE D CZ  1 
ATOM 5552 N N   . THR D 2 102 ? -50.050 16.405  2.619   1.00 71.23  ? 102 THR D N   1 
ATOM 5553 C CA  . THR D 2 102 ? -49.398 17.704  2.543   1.00 60.50  ? 102 THR D CA  1 
ATOM 5554 C C   . THR D 2 102 ? -47.923 17.529  2.208   1.00 55.92  ? 102 THR D C   1 
ATOM 5555 O O   . THR D 2 102 ? -47.185 16.876  2.953   1.00 67.56  ? 102 THR D O   1 
ATOM 5556 C CB  . THR D 2 102 ? -49.550 18.470  3.855   1.00 59.91  ? 102 THR D CB  1 
ATOM 5557 O OG1 . THR D 2 102 ? -50.852 18.234  4.405   1.00 61.55  ? 102 THR D OG1 1 
ATOM 5558 C CG2 . THR D 2 102 ? -49.368 19.963  3.613   1.00 68.45  ? 102 THR D CG2 1 
ATOM 5559 N N   . PHE D 2 103 ? -47.500 18.121  1.097   1.00 53.12  ? 103 PHE D N   1 
ATOM 5560 C CA  . PHE D 2 103 ? -46.089 18.188  0.767   1.00 52.89  ? 103 PHE D CA  1 
ATOM 5561 C C   . PHE D 2 103 ? -45.413 19.286  1.584   1.00 57.14  ? 103 PHE D C   1 
ATOM 5562 O O   . PHE D 2 103 ? -46.059 20.070  2.284   1.00 55.59  ? 103 PHE D O   1 
ATOM 5563 C CB  . PHE D 2 103 ? -45.893 18.446  -0.726  1.00 56.93  ? 103 PHE D CB  1 
ATOM 5564 C CG  . PHE D 2 103 ? -46.210 17.262  -1.599  1.00 56.45  ? 103 PHE D CG  1 
ATOM 5565 C CD1 . PHE D 2 103 ? -47.522 16.894  -1.845  1.00 59.67  ? 103 PHE D CD1 1 
ATOM 5566 C CD2 . PHE D 2 103 ? -45.192 16.519  -2.175  1.00 57.16  ? 103 PHE D CD2 1 
ATOM 5567 C CE1 . PHE D 2 103 ? -47.813 15.808  -2.647  1.00 58.76  ? 103 PHE D CE1 1 
ATOM 5568 C CE2 . PHE D 2 103 ? -45.478 15.432  -2.978  1.00 56.45  ? 103 PHE D CE2 1 
ATOM 5569 C CZ  . PHE D 2 103 ? -46.791 15.077  -3.213  1.00 58.95  ? 103 PHE D CZ  1 
ATOM 5570 N N   . GLY D 2 104 ? -44.089 19.334  1.492   1.00 56.98  ? 104 GLY D N   1 
ATOM 5571 C CA  . GLY D 2 104 ? -43.341 20.412  2.100   1.00 54.19  ? 104 GLY D CA  1 
ATOM 5572 C C   . GLY D 2 104 ? -43.270 21.630  1.199   1.00 59.88  ? 104 GLY D C   1 
ATOM 5573 O O   . GLY D 2 104 ? -43.631 21.587  0.024   1.00 65.55  ? 104 GLY D O   1 
ATOM 5574 N N   . GLN D 2 105 ? -42.795 22.734  1.777   1.00 64.01  ? 105 GLN D N   1 
ATOM 5575 C CA  . GLN D 2 105 ? -42.622 23.954  0.999   1.00 60.83  ? 105 GLN D CA  1 
ATOM 5576 C C   . GLN D 2 105 ? -41.552 23.787  -0.071  1.00 57.10  ? 105 GLN D C   1 
ATOM 5577 O O   . GLN D 2 105 ? -41.648 24.395  -1.142  1.00 59.43  ? 105 GLN D O   1 
ATOM 5578 C CB  . GLN D 2 105 ? -42.273 25.119  1.924   1.00 62.65  ? 105 GLN D CB  1 
ATOM 5579 C CG  . GLN D 2 105 ? -41.103 24.837  2.850   1.00 59.28  ? 105 GLN D CG  1 
ATOM 5580 C CD  . GLN D 2 105 ? -41.110 25.709  4.089   1.00 71.27  ? 105 GLN D CD  1 
ATOM 5581 O OE1 . GLN D 2 105 ? -42.154 26.208  4.510   1.00 85.23  ? 105 GLN D OE1 1 
ATOM 5582 N NE2 . GLN D 2 105 ? -39.939 25.896  4.682   1.00 71.82  ? 105 GLN D NE2 1 
ATOM 5583 N N   . GLY D 2 106 ? -40.531 22.975  0.192   1.00 53.27  ? 106 GLY D N   1 
ATOM 5584 C CA  . GLY D 2 106 ? -39.479 22.752  -0.780  1.00 54.19  ? 106 GLY D CA  1 
ATOM 5585 C C   . GLY D 2 106 ? -38.096 23.111  -0.274  1.00 58.90  ? 106 GLY D C   1 
ATOM 5586 O O   . GLY D 2 106 ? -37.947 23.940  0.630   1.00 64.73  ? 106 GLY D O   1 
ATOM 5587 N N   . THR D 2 107 ? -37.073 22.488  -0.852  1.00 59.45  ? 107 THR D N   1 
ATOM 5588 C CA  . THR D 2 107 ? -35.687 22.767  -0.501  1.00 60.94  ? 107 THR D CA  1 
ATOM 5589 C C   . THR D 2 107 ? -34.825 22.496  -1.724  1.00 66.80  ? 107 THR D C   1 
ATOM 5590 O O   . THR D 2 107 ? -34.947 21.436  -2.343  1.00 69.97  ? 107 THR D O   1 
ATOM 5591 C CB  . THR D 2 107 ? -35.220 21.904  0.675   1.00 63.03  ? 107 THR D CB  1 
ATOM 5592 O OG1 . THR D 2 107 ? -36.037 22.167  1.823   1.00 61.36  ? 107 THR D OG1 1 
ATOM 5593 C CG2 . THR D 2 107 ? -33.768 22.212  1.014   1.00 64.24  ? 107 THR D CG2 1 
ATOM 5594 N N   . LYS D 2 108 ? -33.962 23.445  -2.069  1.00 67.85  ? 108 LYS D N   1 
ATOM 5595 C CA  . LYS D 2 108 ? -33.104 23.326  -3.236  1.00 72.70  ? 108 LYS D CA  1 
ATOM 5596 C C   . LYS D 2 108 ? -31.672 23.018  -2.820  1.00 75.73  ? 108 LYS D C   1 
ATOM 5597 O O   . LYS D 2 108 ? -31.215 23.415  -1.745  1.00 80.86  ? 108 LYS D O   1 
ATOM 5598 C CB  . LYS D 2 108 ? -33.128 24.605  -4.076  1.00 78.45  ? 108 LYS D CB  1 
ATOM 5599 C CG  . LYS D 2 108 ? -32.572 24.441  -5.484  1.00 83.18  ? 108 LYS D CG  1 
ATOM 5600 C CD  . LYS D 2 108 ? -32.736 25.719  -6.292  1.00 78.02  ? 108 LYS D CD  1 
ATOM 5601 C CE  . LYS D 2 108 ? -31.955 26.869  -5.686  1.00 87.06  ? 108 LYS D CE  1 
ATOM 5602 N NZ  . LYS D 2 108 ? -32.112 28.125  -6.471  1.00 97.22  ? 108 LYS D NZ  1 
ATOM 5603 N N   . LEU D 2 109 ? -30.970 22.306  -3.695  1.00 77.75  ? 109 LEU D N   1 
ATOM 5604 C CA  . LEU D 2 109 ? -29.568 21.971  -3.504  1.00 84.96  ? 109 LEU D CA  1 
ATOM 5605 C C   . LEU D 2 109 ? -28.772 22.526  -4.675  1.00 88.52  ? 109 LEU D C   1 
ATOM 5606 O O   . LEU D 2 109 ? -29.141 22.320  -5.836  1.00 88.96  ? 109 LEU D O   1 
ATOM 5607 C CB  . LEU D 2 109 ? -29.378 20.454  -3.385  1.00 78.23  ? 109 LEU D CB  1 
ATOM 5608 C CG  . LEU D 2 109 ? -28.016 19.942  -2.907  1.00 81.89  ? 109 LEU D CG  1 
ATOM 5609 C CD1 . LEU D 2 109 ? -28.185 18.716  -2.018  1.00 89.78  ? 109 LEU D CD1 1 
ATOM 5610 C CD2 . LEU D 2 109 ? -27.110 19.624  -4.088  1.00 85.61  ? 109 LEU D CD2 1 
ATOM 5611 N N   . GLU D 2 110 ? -27.693 23.240  -4.367  1.00 94.40  ? 110 GLU D N   1 
ATOM 5612 C CA  . GLU D 2 110 ? -26.800 23.789  -5.373  1.00 96.50  ? 110 GLU D CA  1 
ATOM 5613 C C   . GLU D 2 110 ? -25.389 23.281  -5.113  1.00 101.39 ? 110 GLU D C   1 
ATOM 5614 O O   . GLU D 2 110 ? -25.072 22.796  -4.024  1.00 101.29 ? 110 GLU D O   1 
ATOM 5615 C CB  . GLU D 2 110 ? -26.826 25.324  -5.369  1.00 105.19 ? 110 GLU D CB  1 
ATOM 5616 C CG  . GLU D 2 110 ? -28.035 25.919  -6.072  1.00 113.22 ? 110 GLU D CG  1 
ATOM 5617 C CD  . GLU D 2 110 ? -27.910 27.414  -6.283  1.00 114.84 ? 110 GLU D CD  1 
ATOM 5618 O OE1 . GLU D 2 110 ? -26.879 27.989  -5.875  1.00 109.37 ? 110 GLU D OE1 1 
ATOM 5619 O OE2 . GLU D 2 110 ? -28.843 28.017  -6.852  1.00 102.25 ? 110 GLU D OE2 1 
ATOM 5620 N N   . ILE D 2 111 ? -24.540 23.397  -6.131  1.00 102.39 ? 111 ILE D N   1 
ATOM 5621 C CA  . ILE D 2 111 ? -23.166 22.913  -6.076  1.00 105.85 ? 111 ILE D CA  1 
ATOM 5622 C C   . ILE D 2 111 ? -22.224 24.102  -6.198  1.00 110.27 ? 111 ILE D C   1 
ATOM 5623 O O   . ILE D 2 111 ? -22.492 25.044  -6.951  1.00 111.41 ? 111 ILE D O   1 
ATOM 5624 C CB  . ILE D 2 111 ? -22.888 21.876  -7.184  1.00 101.11 ? 111 ILE D CB  1 
ATOM 5625 C CG1 . ILE D 2 111 ? -23.941 20.770  -7.150  1.00 97.55  ? 111 ILE D CG1 1 
ATOM 5626 C CG2 . ILE D 2 111 ? -21.497 21.278  -7.027  1.00 103.00 ? 111 ILE D CG2 1 
ATOM 5627 C CD1 . ILE D 2 111 ? -23.741 19.711  -8.203  1.00 99.63  ? 111 ILE D CD1 1 
ATOM 5628 N N   . LYS D 2 112 ? -21.125 24.057  -5.450  1.00 111.45 ? 112 LYS D N   1 
ATOM 5629 C CA  . LYS D 2 112 ? -20.103 25.095  -5.484  1.00 110.68 ? 112 LYS D CA  1 
ATOM 5630 C C   . LYS D 2 112 ? -18.937 24.617  -6.342  1.00 113.98 ? 112 LYS D C   1 
ATOM 5631 O O   . LYS D 2 112 ? -18.330 23.581  -6.050  1.00 110.00 ? 112 LYS D O   1 
ATOM 5632 C CB  . LYS D 2 112 ? -19.626 25.438  -4.073  1.00 105.80 ? 112 LYS D CB  1 
ATOM 5633 C CG  . LYS D 2 112 ? -20.722 25.945  -3.152  1.00 99.92  ? 112 LYS D CG  1 
ATOM 5634 C CD  . LYS D 2 112 ? -20.214 26.111  -1.730  1.00 95.76  ? 112 LYS D CD  1 
ATOM 5635 C CE  . LYS D 2 112 ? -21.255 26.777  -0.846  1.00 87.61  ? 112 LYS D CE  1 
ATOM 5636 N NZ  . LYS D 2 112 ? -20.831 26.815  0.581   1.00 79.97  ? 112 LYS D NZ  1 
ATOM 5637 N N   . ARG D 2 113 ? -18.632 25.368  -7.395  1.00 118.03 ? 113 ARG D N   1 
ATOM 5638 C CA  . ARG D 2 113 ? -17.508 25.045  -8.266  1.00 117.03 ? 113 ARG D CA  1 
ATOM 5639 C C   . ARG D 2 113 ? -16.415 26.104  -8.156  1.00 119.67 ? 113 ARG D C   1 
ATOM 5640 O O   . ARG D 2 113 ? -15.415 26.054  -8.873  1.00 120.46 ? 113 ARG D O   1 
ATOM 5641 C CB  . ARG D 2 113 ? -17.968 24.913  -9.719  1.00 114.07 ? 113 ARG D CB  1 
ATOM 5642 C CG  . ARG D 2 113 ? -17.348 23.737  -10.458 1.00 115.07 ? 113 ARG D CG  1 
ATOM 5643 C CD  . ARG D 2 113 ? -17.483 23.896  -11.965 1.00 118.94 ? 113 ARG D CD  1 
ATOM 5644 N NE  . ARG D 2 113 ? -17.125 22.677  -12.680 1.00 125.59 ? 113 ARG D NE  1 
ATOM 5645 C CZ  . ARG D 2 113 ? -16.957 22.601  -13.993 1.00 122.84 ? 113 ARG D CZ  1 
ATOM 5646 N NH1 . ARG D 2 113 ? -17.117 23.658  -14.773 1.00 117.44 ? 113 ARG D NH1 1 
ATOM 5647 N NH2 . ARG D 2 113 ? -16.619 21.436  -14.539 1.00 125.91 ? 113 ARG D NH2 1 
ATOM 5648 N N   . GLY D 2 162 ? -34.853 47.832  -20.651 1.00 111.27 ? 162 GLY D N   1 
ATOM 5649 C CA  . GLY D 2 162 ? -36.258 47.516  -20.822 1.00 114.02 ? 162 GLY D CA  1 
ATOM 5650 C C   . GLY D 2 162 ? -36.577 46.956  -22.193 1.00 113.82 ? 162 GLY D C   1 
ATOM 5651 O O   . GLY D 2 162 ? -37.744 46.796  -22.552 1.00 115.09 ? 162 GLY D O   1 
ATOM 5652 N N   . ASN D 2 163 ? -35.530 46.662  -22.967 1.00 111.22 ? 163 ASN D N   1 
ATOM 5653 C CA  . ASN D 2 163 ? -35.683 46.091  -24.297 1.00 108.64 ? 163 ASN D CA  1 
ATOM 5654 C C   . ASN D 2 163 ? -35.151 44.671  -24.406 1.00 111.83 ? 163 ASN D C   1 
ATOM 5655 O O   . ASN D 2 163 ? -35.322 44.044  -25.458 1.00 109.72 ? 163 ASN D O   1 
ATOM 5656 C CB  . ASN D 2 163 ? -34.979 46.970  -25.341 1.00 103.57 ? 163 ASN D CB  1 
ATOM 5657 C CG  . ASN D 2 163 ? -33.467 46.848  -25.282 1.00 101.33 ? 163 ASN D CG  1 
ATOM 5658 O OD1 . ASN D 2 163 ? -32.856 46.169  -26.107 1.00 96.03  ? 163 ASN D OD1 1 
ATOM 5659 N ND2 . ASN D 2 163 ? -32.856 47.502  -24.301 1.00 101.74 ? 163 ASN D ND2 1 
ATOM 5660 N N   . SER D 2 164 ? -34.516 44.147  -23.361 1.00 111.21 ? 164 SER D N   1 
ATOM 5661 C CA  . SER D 2 164 ? -33.951 42.807  -23.397 1.00 112.42 ? 164 SER D CA  1 
ATOM 5662 C C   . SER D 2 164 ? -34.191 42.113  -22.064 1.00 119.62 ? 164 SER D C   1 
ATOM 5663 O O   . SER D 2 164 ? -34.427 42.752  -21.036 1.00 119.90 ? 164 SER D O   1 
ATOM 5664 C CB  . SER D 2 164 ? -32.450 42.833  -23.718 1.00 108.63 ? 164 SER D CB  1 
ATOM 5665 O OG  . SER D 2 164 ? -31.735 43.591  -22.757 1.00 110.32 ? 164 SER D OG  1 
ATOM 5666 N N   . GLN D 2 165 ? -34.126 40.785  -22.104 1.00 125.68 ? 165 GLN D N   1 
ATOM 5667 C CA  . GLN D 2 165 ? -34.293 39.948  -20.927 1.00 134.83 ? 165 GLN D CA  1 
ATOM 5668 C C   . GLN D 2 165 ? -33.464 38.689  -21.131 1.00 139.74 ? 165 GLN D C   1 
ATOM 5669 O O   . GLN D 2 165 ? -32.968 38.423  -22.228 1.00 142.08 ? 165 GLN D O   1 
ATOM 5670 C CB  . GLN D 2 165 ? -35.769 39.617  -20.685 1.00 135.79 ? 165 GLN D CB  1 
ATOM 5671 C CG  . GLN D 2 165 ? -36.506 39.178  -21.939 1.00 136.32 ? 165 GLN D CG  1 
ATOM 5672 C CD  . GLN D 2 165 ? -38.006 39.357  -21.825 1.00 130.90 ? 165 GLN D CD  1 
ATOM 5673 O OE1 . GLN D 2 165 ? -38.497 39.989  -20.890 1.00 131.33 ? 165 GLN D OE1 1 
ATOM 5674 N NE2 . GLN D 2 165 ? -38.743 38.804  -22.782 1.00 125.98 ? 165 GLN D NE2 1 
ATOM 5675 N N   . GLU D 2 166 ? -33.306 37.911  -20.063 1.00 131.31 ? 166 GLU D N   1 
ATOM 5676 C CA  . GLU D 2 166 ? -32.473 36.720  -20.132 1.00 122.38 ? 166 GLU D CA  1 
ATOM 5677 C C   . GLU D 2 166 ? -33.065 35.607  -19.282 1.00 121.58 ? 166 GLU D C   1 
ATOM 5678 O O   . GLU D 2 166 ? -33.765 35.854  -18.297 1.00 121.74 ? 166 GLU D O   1 
ATOM 5679 C CB  . GLU D 2 166 ? -31.033 37.008  -19.681 1.00 120.33 ? 166 GLU D CB  1 
ATOM 5680 C CG  . GLU D 2 166 ? -30.904 37.521  -18.257 1.00 120.45 ? 166 GLU D CG  1 
ATOM 5681 C CD  . GLU D 2 166 ? -29.582 37.131  -17.623 1.00 116.22 ? 166 GLU D CD  1 
ATOM 5682 O OE1 . GLU D 2 166 ? -28.806 36.399  -18.273 1.00 111.83 ? 166 GLU D OE1 1 
ATOM 5683 O OE2 . GLU D 2 166 ? -29.314 37.561  -16.482 1.00 111.34 ? 166 GLU D OE2 1 
ATOM 5684 N N   . SER D 2 167 ? -32.770 34.374  -19.683 1.00 118.82 ? 167 SER D N   1 
ATOM 5685 C CA  . SER D 2 167 ? -33.184 33.179  -18.963 1.00 115.58 ? 167 SER D CA  1 
ATOM 5686 C C   . SER D 2 167 ? -31.948 32.341  -18.679 1.00 111.69 ? 167 SER D C   1 
ATOM 5687 O O   . SER D 2 167 ? -31.182 32.031  -19.596 1.00 107.79 ? 167 SER D O   1 
ATOM 5688 C CB  . SER D 2 167 ? -34.212 32.377  -19.766 1.00 112.29 ? 167 SER D CB  1 
ATOM 5689 O OG  . SER D 2 167 ? -33.688 31.989  -21.024 1.00 111.73 ? 167 SER D OG  1 
ATOM 5690 N N   . VAL D 2 168 ? -31.751 31.986  -17.414 1.00 115.20 ? 168 VAL D N   1 
ATOM 5691 C CA  . VAL D 2 168 ? -30.547 31.294  -16.969 1.00 115.80 ? 168 VAL D CA  1 
ATOM 5692 C C   . VAL D 2 168 ? -30.846 29.806  -16.870 1.00 115.05 ? 168 VAL D C   1 
ATOM 5693 O O   . VAL D 2 168 ? -31.790 29.397  -16.183 1.00 112.89 ? 168 VAL D O   1 
ATOM 5694 C CB  . VAL D 2 168 ? -30.045 31.847  -15.627 1.00 113.84 ? 168 VAL D CB  1 
ATOM 5695 C CG1 . VAL D 2 168 ? -28.594 31.451  -15.404 1.00 108.88 ? 168 VAL D CG1 1 
ATOM 5696 C CG2 . VAL D 2 168 ? -30.203 33.360  -15.588 1.00 111.77 ? 168 VAL D CG2 1 
ATOM 5697 N N   . THR D 2 169 ? -30.042 28.998  -17.556 1.00 117.31 ? 169 THR D N   1 
ATOM 5698 C CA  . THR D 2 169 ? -30.175 27.552  -17.455 1.00 124.77 ? 169 THR D CA  1 
ATOM 5699 C C   . THR D 2 169 ? -29.811 27.089  -16.051 1.00 118.45 ? 169 THR D C   1 
ATOM 5700 O O   . THR D 2 169 ? -28.848 27.573  -15.450 1.00 119.91 ? 169 THR D O   1 
ATOM 5701 C CB  . THR D 2 169 ? -29.273 26.860  -18.476 1.00 125.23 ? 169 THR D CB  1 
ATOM 5702 O OG1 . THR D 2 169 ? -28.006 27.529  -18.526 1.00 128.87 ? 169 THR D OG1 1 
ATOM 5703 C CG2 . THR D 2 169 ? -29.907 26.888  -19.858 1.00 123.02 ? 169 THR D CG2 1 
ATOM 5704 N N   . GLU D 2 170 ? -30.591 26.149  -15.527 1.00 114.32 ? 170 GLU D N   1 
ATOM 5705 C CA  . GLU D 2 170 ? -30.267 25.555  -14.242 1.00 114.61 ? 170 GLU D CA  1 
ATOM 5706 C C   . GLU D 2 170 ? -28.979 24.744  -14.355 1.00 121.33 ? 170 GLU D C   1 
ATOM 5707 O O   . GLU D 2 170 ? -28.535 24.385  -15.450 1.00 125.77 ? 170 GLU D O   1 
ATOM 5708 C CB  . GLU D 2 170 ? -31.414 24.670  -13.755 1.00 110.66 ? 170 GLU D CB  1 
ATOM 5709 C CG  . GLU D 2 170 ? -31.872 24.959  -12.333 1.00 107.30 ? 170 GLU D CG  1 
ATOM 5710 C CD  . GLU D 2 170 ? -31.011 24.284  -11.282 1.00 108.20 ? 170 GLU D CD  1 
ATOM 5711 O OE1 . GLU D 2 170 ? -30.294 23.319  -11.623 1.00 109.57 ? 170 GLU D OE1 1 
ATOM 5712 O OE2 . GLU D 2 170 ? -31.054 24.716  -10.111 1.00 98.88  ? 170 GLU D OE2 1 
ATOM 5713 N N   . GLN D 2 171 ? -28.371 24.463  -13.204 1.00 115.91 ? 171 GLN D N   1 
ATOM 5714 C CA  . GLN D 2 171 ? -27.121 23.712  -13.185 1.00 118.80 ? 171 GLN D CA  1 
ATOM 5715 C C   . GLN D 2 171 ? -27.317 22.347  -13.831 1.00 128.75 ? 171 GLN D C   1 
ATOM 5716 O O   . GLN D 2 171 ? -28.143 21.547  -13.382 1.00 127.73 ? 171 GLN D O   1 
ATOM 5717 C CB  . GLN D 2 171 ? -26.612 23.561  -11.752 1.00 112.64 ? 171 GLN D CB  1 
ATOM 5718 C CG  . GLN D 2 171 ? -26.408 24.875  -11.014 1.00 109.11 ? 171 GLN D CG  1 
ATOM 5719 C CD  . GLN D 2 171 ? -25.807 24.676  -9.636  1.00 108.41 ? 171 GLN D CD  1 
ATOM 5720 O OE1 . GLN D 2 171 ? -25.465 23.558  -9.252  1.00 109.46 ? 171 GLN D OE1 1 
ATOM 5721 N NE2 . GLN D 2 171 ? -25.674 25.764  -8.886  1.00 113.08 ? 171 GLN D NE2 1 
ATOM 5722 N N   . ASP D 2 172 ? -26.561 22.091  -14.895 1.00 142.57 ? 172 ASP D N   1 
ATOM 5723 C CA  . ASP D 2 172 ? -26.712 20.860  -15.651 1.00 149.99 ? 172 ASP D CA  1 
ATOM 5724 C C   . ASP D 2 172 ? -26.185 19.669  -14.855 1.00 153.28 ? 172 ASP D C   1 
ATOM 5725 O O   . ASP D 2 172 ? -25.450 19.817  -13.874 1.00 149.71 ? 172 ASP D O   1 
ATOM 5726 C CB  . ASP D 2 172 ? -25.970 20.957  -16.983 1.00 150.81 ? 172 ASP D CB  1 
ATOM 5727 C CG  . ASP D 2 172 ? -26.803 21.604  -18.067 1.00 156.60 ? 172 ASP D CG  1 
ATOM 5728 O OD1 . ASP D 2 172 ? -27.922 22.064  -17.760 1.00 151.37 ? 172 ASP D OD1 1 
ATOM 5729 O OD2 . ASP D 2 172 ? -26.337 21.654  -19.225 1.00 157.06 ? 172 ASP D OD2 1 
ATOM 5730 N N   . SER D 2 173 ? -26.585 18.471  -15.291 1.00 148.63 ? 173 SER D N   1 
ATOM 5731 C CA  . SER D 2 173 ? -25.995 17.255  -14.741 1.00 144.28 ? 173 SER D CA  1 
ATOM 5732 C C   . SER D 2 173 ? -24.481 17.276  -14.897 1.00 145.14 ? 173 SER D C   1 
ATOM 5733 O O   . SER D 2 173 ? -23.745 16.919  -13.970 1.00 141.13 ? 173 SER D O   1 
ATOM 5734 C CB  . SER D 2 173 ? -26.595 16.024  -15.420 1.00 139.94 ? 173 SER D CB  1 
ATOM 5735 O OG  . SER D 2 173 ? -25.883 14.853  -15.066 1.00 134.31 ? 173 SER D OG  1 
ATOM 5736 N N   . LYS D 2 174 ? -24.000 17.686  -16.067 1.00 148.82 ? 174 LYS D N   1 
ATOM 5737 C CA  . LYS D 2 174 ? -22.616 18.117  -16.202 1.00 145.15 ? 174 LYS D CA  1 
ATOM 5738 C C   . LYS D 2 174 ? -22.431 19.386  -15.382 1.00 138.50 ? 174 LYS D C   1 
ATOM 5739 O O   . LYS D 2 174 ? -23.093 20.396  -15.644 1.00 136.64 ? 174 LYS D O   1 
ATOM 5740 C CB  . LYS D 2 174 ? -22.286 18.373  -17.669 1.00 145.77 ? 174 LYS D CB  1 
ATOM 5741 C CG  . LYS D 2 174 ? -22.715 17.258  -18.608 1.00 141.15 ? 174 LYS D CG  1 
ATOM 5742 C CD  . LYS D 2 174 ? -22.616 17.694  -20.060 1.00 131.30 ? 174 LYS D CD  1 
ATOM 5743 C CE  . LYS D 2 174 ? -23.578 18.839  -20.349 1.00 134.68 ? 174 LYS D CE  1 
ATOM 5744 N NZ  . LYS D 2 174 ? -23.519 19.285  -21.768 1.00 130.31 ? 174 LYS D NZ  1 
ATOM 5745 N N   . ASP D 2 175 ? -21.554 19.336  -14.381 1.00 139.27 ? 175 ASP D N   1 
ATOM 5746 C CA  . ASP D 2 175 ? -21.429 20.451  -13.448 1.00 135.79 ? 175 ASP D CA  1 
ATOM 5747 C C   . ASP D 2 175 ? -21.069 21.744  -14.172 1.00 132.47 ? 175 ASP D C   1 
ATOM 5748 O O   . ASP D 2 175 ? -20.144 21.782  -14.988 1.00 134.86 ? 175 ASP D O   1 
ATOM 5749 C CB  . ASP D 2 175 ? -20.389 20.131  -12.374 1.00 133.05 ? 175 ASP D CB  1 
ATOM 5750 C CG  . ASP D 2 175 ? -19.130 19.507  -12.943 1.00 138.29 ? 175 ASP D CG  1 
ATOM 5751 O OD1 . ASP D 2 175 ? -18.980 19.471  -14.181 1.00 144.93 ? 175 ASP D OD1 1 
ATOM 5752 O OD2 . ASP D 2 175 ? -18.282 19.058  -12.144 1.00 129.56 ? 175 ASP D OD2 1 
ATOM 5753 N N   . SER D 2 176 ? -21.818 22.802  -13.875 1.00 132.80 ? 176 SER D N   1 
ATOM 5754 C CA  . SER D 2 176 ? -21.614 24.098  -14.509 1.00 122.69 ? 176 SER D CA  1 
ATOM 5755 C C   . SER D 2 176 ? -21.875 25.235  -13.526 1.00 112.60 ? 176 SER D C   1 
ATOM 5756 O O   . SER D 2 176 ? -22.130 25.001  -12.344 1.00 110.55 ? 176 SER D O   1 
ATOM 5757 C CB  . SER D 2 176 ? -22.520 24.243  -15.735 1.00 113.98 ? 176 SER D CB  1 
ATOM 5758 O OG  . SER D 2 176 ? -23.876 24.006  -15.399 1.00 122.02 ? 176 SER D OG  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   ? 1.0538 0.7457 1.0299 0.0208  -0.1668 -0.0509 1   GLN A N   
2    C CA  . GLN A 1   ? 1.0061 0.7022 0.9887 0.0185  -0.1663 -0.0482 1   GLN A CA  
3    C C   . GLN A 1   ? 0.9764 0.6695 0.9547 0.0184  -0.1708 -0.0335 1   GLN A C   
4    O O   . GLN A 1   ? 0.9388 0.6347 0.9231 0.0167  -0.1705 -0.0289 1   GLN A O   
5    C CB  . GLN A 1   ? 0.9702 0.6724 0.9809 0.0181  -0.1560 -0.0537 1   GLN A CB  
6    C CG  . GLN A 1   ? 0.9558 0.6641 0.9722 0.0152  -0.1550 -0.0567 1   GLN A CG  
7    C CD  . GLN A 1   ? 0.9967 0.7110 1.0429 0.0147  -0.1443 -0.0614 1   GLN A CD  
8    O OE1 . GLN A 1   ? 1.0167 0.7305 1.0802 0.0166  -0.1371 -0.0626 1   GLN A OE1 
9    N NE2 . GLN A 1   ? 0.9835 0.7033 1.0366 0.0119  -0.1428 -0.0642 1   GLN A NE2 
10   N N   . VAL A 2   ? 0.9332 0.6213 0.9011 0.0200  -0.1749 -0.0265 2   VAL A N   
11   C CA  . VAL A 2   ? 0.9151 0.6019 0.8754 0.0197  -0.1802 -0.0135 2   VAL A CA  
12   C C   . VAL A 2   ? 0.9728 0.6575 0.9096 0.0173  -0.1886 -0.0138 2   VAL A C   
13   O O   . VAL A 2   ? 1.0516 0.7329 0.9719 0.0172  -0.1926 -0.0199 2   VAL A O   
14   C CB  . VAL A 2   ? 0.9296 0.6135 0.8876 0.0222  -0.1814 -0.0066 2   VAL A CB  
15   C CG1 . VAL A 2   ? 0.9026 0.5885 0.8579 0.0219  -0.1851 0.0071  2   VAL A CG1 
16   C CG2 . VAL A 2   ? 0.9321 0.6172 0.9127 0.0249  -0.1725 -0.0086 2   VAL A CG2 
17   N N   . GLN A 3   ? 0.9445 0.6314 0.8801 0.0155  -0.1910 -0.0070 3   GLN A N   
18   C CA  . GLN A 3   ? 0.9240 0.6090 0.8395 0.0131  -0.1981 -0.0069 3   GLN A CA  
19   C C   . GLN A 3   ? 0.9083 0.5931 0.8154 0.0123  -0.2031 0.0046  3   GLN A C   
20   O O   . GLN A 3   ? 0.9017 0.5906 0.8212 0.0124  -0.2008 0.0128  3   GLN A O   
21   C CB  . GLN A 3   ? 0.9516 0.6403 0.8720 0.0111  -0.1966 -0.0111 3   GLN A CB  
22   C CG  . GLN A 3   ? 1.0756 0.7624 0.9761 0.0089  -0.2033 -0.0117 3   GLN A CG  
23   C CD  . GLN A 3   ? 1.1162 0.8071 1.0223 0.0069  -0.2021 -0.0137 3   GLN A CD  
24   O OE1 . GLN A 3   ? 1.1574 0.8526 1.0826 0.0069  -0.1962 -0.0144 3   GLN A OE1 
25   N NE2 . GLN A 3   ? 1.0690 0.7586 0.9592 0.0052  -0.2073 -0.0146 3   GLN A NE2 
26   N N   . LEU A 4   ? 0.9564 0.6372 0.8433 0.0114  -0.2097 0.0049  4   LEU A N   
27   C CA  . LEU A 4   ? 0.9178 0.5993 0.7945 0.0099  -0.2149 0.0139  4   LEU A CA  
28   C C   . LEU A 4   ? 0.9261 0.6059 0.7879 0.0072  -0.2197 0.0118  4   LEU A C   
29   O O   . LEU A 4   ? 1.0367 0.7120 0.8853 0.0068  -0.2222 0.0051  4   LEU A O   
30   C CB  . LEU A 4   ? 0.8634 0.5423 0.7299 0.0108  -0.2182 0.0158  4   LEU A CB  
31   C CG  . LEU A 4   ? 0.8792 0.5622 0.7574 0.0129  -0.2158 0.0238  4   LEU A CG  
32   C CD1 . LEU A 4   ? 0.8770 0.5608 0.7753 0.0158  -0.2082 0.0211  4   LEU A CD1 
33   C CD2 . LEU A 4   ? 0.8626 0.5430 0.7277 0.0132  -0.2201 0.0246  4   LEU A CD2 
34   N N   . GLN A 5   ? 0.8511 0.5347 0.7155 0.0054  -0.2205 0.0177  5   GLN A N   
35   C CA  . GLN A 5   ? 0.9466 0.6288 0.7989 0.0028  -0.2243 0.0163  5   GLN A CA  
36   C C   . GLN A 5   ? 0.9816 0.6651 0.8231 0.0007  -0.2291 0.0234  5   GLN A C   
37   O O   . GLN A 5   ? 0.9440 0.6332 0.7932 0.0008  -0.2284 0.0315  5   GLN A O   
38   C CB  . GLN A 5   ? 0.9690 0.6546 0.8326 0.0020  -0.2212 0.0158  5   GLN A CB  
39   C CG  . GLN A 5   ? 1.1289 0.8130 0.9923 0.0022  -0.2195 0.0060  5   GLN A CG  
40   C CD  . GLN A 5   ? 1.2115 0.8988 1.0808 0.0005  -0.2184 0.0054  5   GLN A CD  
41   O OE1 . GLN A 5   ? 1.1808 0.8711 1.0574 -0.0005 -0.2178 0.0123  5   GLN A OE1 
42   N NE2 . GLN A 5   ? 1.1585 0.8459 1.0244 0.0002  -0.2181 -0.0026 5   GLN A NE2 
43   N N   . GLN A 6   ? 1.0390 0.7182 0.8636 -0.0011 -0.2336 0.0204  6   GLN A N   
44   C CA  . GLN A 6   ? 0.9545 0.6350 0.7679 -0.0035 -0.2380 0.0251  6   GLN A CA  
45   C C   . GLN A 6   ? 0.9511 0.6312 0.7575 -0.0062 -0.2401 0.0248  6   GLN A C   
46   O O   . GLN A 6   ? 1.0141 0.6900 0.8164 -0.0061 -0.2400 0.0191  6   GLN A O   
47   C CB  . GLN A 6   ? 0.9271 0.6025 0.7271 -0.0036 -0.2410 0.0217  6   GLN A CB  
48   C CG  . GLN A 6   ? 0.9262 0.6041 0.7165 -0.0063 -0.2449 0.0258  6   GLN A CG  
49   C CD  . GLN A 6   ? 0.9260 0.5989 0.7051 -0.0064 -0.2472 0.0221  6   GLN A CD  
50   O OE1 . GLN A 6   ? 0.9712 0.6401 0.7518 -0.0039 -0.2457 0.0184  6   GLN A OE1 
51   N NE2 . GLN A 6   ? 0.9514 0.6247 0.7198 -0.0095 -0.2505 0.0228  6   GLN A NE2 
52   N N   . TRP A 7   ? 0.9385 0.6239 0.7440 -0.0083 -0.2419 0.0311  7   TRP A N   
53   C CA  . TRP A 7   ? 0.8970 0.5820 0.6950 -0.0112 -0.2441 0.0310  7   TRP A CA  
54   C C   . TRP A 7   ? 0.9184 0.6084 0.7095 -0.0139 -0.2470 0.0357  7   TRP A C   
55   O O   . TRP A 7   ? 0.9783 0.6733 0.7715 -0.0135 -0.2474 0.0396  7   TRP A O   
56   C CB  . TRP A 7   ? 0.9299 0.6181 0.7384 -0.0112 -0.2417 0.0330  7   TRP A CB  
57   C CG  . TRP A 7   ? 0.9751 0.6719 0.7951 -0.0111 -0.2402 0.0413  7   TRP A CG  
58   C CD1 . TRP A 7   ? 0.9781 0.6814 0.7962 -0.0134 -0.2420 0.0472  7   TRP A CD1 
59   C CD2 . TRP A 7   ? 0.9664 0.6670 0.8025 -0.0084 -0.2360 0.0449  7   TRP A CD2 
60   N NE1 . TRP A 7   ? 0.9688 0.6804 0.8004 -0.0121 -0.2394 0.0549  7   TRP A NE1 
61   C CE2 . TRP A 7   ? 0.9592 0.6690 0.8026 -0.0089 -0.2355 0.0539  7   TRP A CE2 
62   C CE3 . TRP A 7   ? 0.9882 0.6861 0.8340 -0.0055 -0.2323 0.0414  7   TRP A CE3 
63   C CZ2 . TRP A 7   ? 0.9710 0.6867 0.8315 -0.0064 -0.2312 0.0601  7   TRP A CZ2 
64   C CZ3 . TRP A 7   ? 0.9787 0.6819 0.8416 -0.0033 -0.2278 0.0467  7   TRP A CZ3 
65   C CH2 . TRP A 7   ? 0.9439 0.6558 0.8144 -0.0036 -0.2272 0.0564  7   TRP A CH2 
66   N N   . GLY A 8   ? 0.9239 0.6135 0.7072 -0.0168 -0.2490 0.0349  8   GLY A N   
67   C CA  . GLY A 8   ? 0.9109 0.6064 0.6879 -0.0199 -0.2515 0.0381  8   GLY A CA  
68   C C   . GLY A 8   ? 0.8822 0.5726 0.6466 -0.0228 -0.2535 0.0334  8   GLY A C   
69   O O   . GLY A 8   ? 0.8882 0.5723 0.6501 -0.0227 -0.2530 0.0299  8   GLY A O   
70   N N   . THR A 9   ? 0.8748 0.5685 0.6320 -0.0256 -0.2554 0.0333  9   THR A N   
71   C CA  . THR A 9   ? 0.8682 0.5582 0.6152 -0.0288 -0.2566 0.0292  9   THR A CA  
72   C C   . THR A 9   ? 0.9005 0.5799 0.6403 -0.0277 -0.2565 0.0233  9   THR A C   
73   O O   . THR A 9   ? 0.9051 0.5835 0.6429 -0.0270 -0.2570 0.0222  9   THR A O   
74   C CB  . THR A 9   ? 0.8897 0.5890 0.6334 -0.0326 -0.2581 0.0307  9   THR A CB  
75   O OG1 . THR A 9   ? 0.8756 0.5794 0.6210 -0.0317 -0.2587 0.0324  9   THR A OG1 
76   C CG2 . THR A 9   ? 0.9328 0.6431 0.6819 -0.0342 -0.2581 0.0360  9   THR A CG2 
77   N N   . GLY A 10  ? 0.9514 0.6235 0.6875 -0.0274 -0.2557 0.0199  10  GLY A N   
78   C CA  . GLY A 10  ? 0.9404 0.6034 0.6698 -0.0261 -0.2552 0.0151  10  GLY A CA  
79   C C   . GLY A 10  ? 0.9600 0.6201 0.6812 -0.0294 -0.2555 0.0122  10  GLY A C   
80   O O   . GLY A 10  ? 0.9616 0.6155 0.6774 -0.0288 -0.2551 0.0089  10  GLY A O   
81   N N   . LEU A 11  ? 1.0003 0.6651 0.7212 -0.0329 -0.2557 0.0133  11  LEU A N   
82   C CA  . LEU A 11  ? 0.9627 0.6255 0.6775 -0.0365 -0.2551 0.0101  11  LEU A CA  
83   C C   . LEU A 11  ? 0.9573 0.6309 0.6734 -0.0408 -0.2561 0.0115  11  LEU A C   
84   O O   . LEU A 11  ? 0.9459 0.6263 0.6661 -0.0415 -0.2565 0.0149  11  LEU A O   
85   C CB  . LEU A 11  ? 0.9849 0.6419 0.6980 -0.0365 -0.2534 0.0086  11  LEU A CB  
86   C CG  . LEU A 11  ? 0.9777 0.6308 0.6859 -0.0398 -0.2516 0.0049  11  LEU A CG  
87   C CD1 . LEU A 11  ? 1.0077 0.6541 0.7118 -0.0388 -0.2507 0.0019  11  LEU A CD1 
88   C CD2 . LEU A 11  ? 0.9934 0.6418 0.7013 -0.0393 -0.2497 0.0046  11  LEU A CD2 
89   N N   . LEU A 12  ? 1.0207 0.6967 0.7334 -0.0438 -0.2563 0.0088  12  LEU A N   
90   C CA  . LEU A 12  ? 1.0015 0.6898 0.7151 -0.0482 -0.2570 0.0092  12  LEU A CA  
91   C C   . LEU A 12  ? 0.9884 0.6752 0.6977 -0.0528 -0.2553 0.0034  12  LEU A C   
92   O O   . LEU A 12  ? 0.9961 0.6733 0.7019 -0.0524 -0.2539 -0.0004 12  LEU A O   
93   C CB  . LEU A 12  ? 0.9511 0.6482 0.6666 -0.0481 -0.2589 0.0116  12  LEU A CB  
94   C CG  . LEU A 12  ? 0.8780 0.5812 0.6001 -0.0445 -0.2601 0.0181  12  LEU A CG  
95   C CD1 . LEU A 12  ? 0.9248 0.6374 0.6517 -0.0455 -0.2601 0.0226  12  LEU A CD1 
96   C CD2 . LEU A 12  ? 0.9728 0.6650 0.6966 -0.0394 -0.2596 0.0187  12  LEU A CD2 
97   N N   . LYS A 13  ? 1.0070 0.7037 0.7174 -0.0570 -0.2549 0.0027  13  LYS A N   
98   C CA  . LYS A 13  ? 0.9834 0.6821 0.6916 -0.0622 -0.2529 -0.0034 13  LYS A CA  
99   C C   . LYS A 13  ? 0.9544 0.6652 0.6629 -0.0653 -0.2543 -0.0046 13  LYS A C   
100  O O   . LYS A 13  ? 1.0244 0.7461 0.7356 -0.0642 -0.2568 0.0003  13  LYS A O   
101  C CB  . LYS A 13  ? 0.9429 0.6473 0.6524 -0.0658 -0.2514 -0.0048 13  LYS A CB  
102  C CG  . LYS A 13  ? 0.9917 0.6841 0.7007 -0.0634 -0.2496 -0.0045 13  LYS A CG  
103  C CD  . LYS A 13  ? 0.9992 0.6957 0.7091 -0.0675 -0.2474 -0.0073 13  LYS A CD  
104  C CE  . LYS A 13  ? 1.0303 0.7386 0.7428 -0.0679 -0.2495 -0.0028 13  LYS A CE  
105  N NZ  . LYS A 13  ? 1.1005 0.8117 0.8135 -0.0714 -0.2474 -0.0055 13  LYS A NZ  
106  N N   . PRO A 14  ? 0.9226 0.6320 0.6291 -0.0690 -0.2525 -0.0109 14  PRO A N   
107  C CA  . PRO A 14  ? 0.9294 0.6503 0.6361 -0.0719 -0.2540 -0.0125 14  PRO A CA  
108  C C   . PRO A 14  ? 0.9750 0.7163 0.6848 -0.0751 -0.2554 -0.0103 14  PRO A C   
109  O O   . PRO A 14  ? 0.9466 0.6942 0.6578 -0.0779 -0.2540 -0.0116 14  PRO A O   
110  C CB  . PRO A 14  ? 0.9182 0.6345 0.6235 -0.0765 -0.2507 -0.0208 14  PRO A CB  
111  C CG  . PRO A 14  ? 0.9339 0.6317 0.6375 -0.0732 -0.2482 -0.0214 14  PRO A CG  
112  C CD  . PRO A 14  ? 0.9497 0.6467 0.6545 -0.0704 -0.2488 -0.0165 14  PRO A CD  
113  N N   . SER A 15  ? 0.9933 0.7457 0.7044 -0.0743 -0.2581 -0.0067 15  SER A N   
114  C CA  . SER A 15  ? 0.9917 0.7661 0.7063 -0.0763 -0.2598 -0.0030 15  SER A CA  
115  C C   . SER A 15  ? 1.0270 0.8050 0.7452 -0.0722 -0.2610 0.0057  15  SER A C   
116  O O   . SER A 15  ? 1.0017 0.7982 0.7235 -0.0729 -0.2622 0.0105  15  SER A O   
117  C CB  . SER A 15  ? 1.0278 0.8168 0.7430 -0.0833 -0.2579 -0.0092 15  SER A CB  
118  O OG  . SER A 15  ? 1.1198 0.9053 0.8331 -0.0876 -0.2560 -0.0180 15  SER A OG  
119  N N   . GLU A 16  ? 1.0911 0.8532 0.8091 -0.0679 -0.2605 0.0080  16  GLU A N   
120  C CA  . GLU A 16  ? 1.1007 0.8654 0.8233 -0.0638 -0.2614 0.0161  16  GLU A CA  
121  C C   . GLU A 16  ? 1.0782 0.8428 0.8041 -0.0590 -0.2630 0.0220  16  GLU A C   
122  O O   . GLU A 16  ? 1.0767 0.8401 0.8007 -0.0590 -0.2638 0.0199  16  GLU A O   
123  C CB  . GLU A 16  ? 1.0665 0.8158 0.7881 -0.0616 -0.2601 0.0154  16  GLU A CB  
124  C CG  . GLU A 16  ? 1.1386 0.8895 0.8582 -0.0661 -0.2582 0.0106  16  GLU A CG  
125  C CD  . GLU A 16  ? 1.2222 0.9594 0.9412 -0.0638 -0.2570 0.0107  16  GLU A CD  
126  O OE1 . GLU A 16  ? 1.1514 0.8766 0.8709 -0.0591 -0.2573 0.0129  16  GLU A OE1 
127  O OE2 . GLU A 16  ? 1.2310 0.9702 0.9494 -0.0668 -0.2556 0.0083  16  GLU A OE2 
128  N N   . THR A 17  ? 0.9951 0.7612 0.7270 -0.0549 -0.2632 0.0294  17  THR A N   
129  C CA  . THR A 17  ? 0.9691 0.7379 0.7065 -0.0505 -0.2640 0.0357  17  THR A CA  
130  C C   . THR A 17  ? 0.9283 0.6806 0.6680 -0.0454 -0.2631 0.0367  17  THR A C   
131  O O   . THR A 17  ? 0.9181 0.6633 0.6586 -0.0445 -0.2620 0.0367  17  THR A O   
132  C CB  . THR A 17  ? 0.9418 0.7295 0.6868 -0.0498 -0.2642 0.0444  17  THR A CB  
133  O OG1 . THR A 17  ? 1.0047 0.7932 0.7568 -0.0449 -0.2641 0.0511  17  THR A OG1 
134  C CG2 . THR A 17  ? 0.9514 0.7398 0.6994 -0.0497 -0.2631 0.0473  17  THR A CG2 
135  N N   . LEU A 18  ? 0.8988 0.6459 0.6396 -0.0422 -0.2634 0.0373  18  LEU A N   
136  C CA  . LEU A 18  ? 0.8955 0.6284 0.6386 -0.0375 -0.2623 0.0371  18  LEU A CA  
137  C C   . LEU A 18  ? 0.9517 0.6905 0.7060 -0.0335 -0.2611 0.0450  18  LEU A C   
138  O O   . LEU A 18  ? 0.9155 0.6667 0.6751 -0.0329 -0.2614 0.0507  18  LEU A O   
139  C CB  . LEU A 18  ? 0.8669 0.5909 0.6054 -0.0364 -0.2629 0.0328  18  LEU A CB  
140  C CG  . LEU A 18  ? 0.8652 0.5774 0.6063 -0.0315 -0.2618 0.0321  18  LEU A CG  
141  C CD1 . LEU A 18  ? 0.8679 0.5686 0.6003 -0.0319 -0.2623 0.0252  18  LEU A CD1 
142  C CD2 . LEU A 18  ? 0.9068 0.6258 0.6563 -0.0282 -0.2615 0.0379  18  LEU A CD2 
143  N N   . SER A 19  ? 0.9151 0.6456 0.6738 -0.0309 -0.2594 0.0454  19  SER A N   
144  C CA  . SER A 19  ? 0.8851 0.6190 0.6559 -0.0270 -0.2574 0.0520  19  SER A CA  
145  C C   . SER A 19  ? 0.9023 0.6227 0.6755 -0.0233 -0.2557 0.0483  19  SER A C   
146  O O   . SER A 19  ? 0.9119 0.6223 0.6805 -0.0236 -0.2555 0.0430  19  SER A O   
147  C CB  . SER A 19  ? 0.9189 0.6589 0.6953 -0.0277 -0.2564 0.0564  19  SER A CB  
148  O OG  . SER A 19  ? 1.0754 0.8152 0.8642 -0.0238 -0.2536 0.0613  19  SER A OG  
149  N N   . LEU A 20  ? 0.9241 0.6452 0.7049 -0.0199 -0.2542 0.0510  20  LEU A N   
150  C CA  . LEU A 20  ? 0.9366 0.6470 0.7211 -0.0165 -0.2521 0.0472  20  LEU A CA  
151  C C   . LEU A 20  ? 0.9729 0.6888 0.7726 -0.0128 -0.2489 0.0534  20  LEU A C   
152  O O   . LEU A 20  ? 0.9934 0.7184 0.7974 -0.0122 -0.2489 0.0592  20  LEU A O   
153  C CB  . LEU A 20  ? 0.8557 0.5581 0.6310 -0.0163 -0.2536 0.0411  20  LEU A CB  
154  C CG  . LEU A 20  ? 0.8575 0.5519 0.6197 -0.0190 -0.2555 0.0343  20  LEU A CG  
155  C CD1 . LEU A 20  ? 0.8592 0.5470 0.6133 -0.0188 -0.2568 0.0294  20  LEU A CD1 
156  C CD2 . LEU A 20  ? 0.8607 0.5472 0.6235 -0.0178 -0.2540 0.0307  20  LEU A CD2 
157  N N   . THR A 21  ? 0.9540 0.6651 0.7627 -0.0106 -0.2457 0.0522  21  THR A N   
158  C CA  . THR A 21  ? 0.9802 0.6963 0.8059 -0.0073 -0.2415 0.0581  21  THR A CA  
159  C C   . THR A 21  ? 0.9545 0.6618 0.7867 -0.0045 -0.2381 0.0522  21  THR A C   
160  O O   . THR A 21  ? 0.9400 0.6396 0.7669 -0.0051 -0.2384 0.0451  21  THR A O   
161  C CB  . THR A 21  ? 0.9897 0.7128 0.8239 -0.0081 -0.2399 0.0640  21  THR A CB  
162  O OG1 . THR A 21  ? 0.9863 0.7192 0.8142 -0.0108 -0.2429 0.0690  21  THR A OG1 
163  C CG2 . THR A 21  ? 0.9380 0.6664 0.7915 -0.0046 -0.2347 0.0707  21  THR A CG2 
164  N N   . CYS A 22  ? 0.9788 0.6882 0.8231 -0.0013 -0.2346 0.0551  22  CYS A N   
165  C CA  . CYS A 22  ? 0.9650 0.6673 0.8163 0.0014  -0.2310 0.0488  22  CYS A CA  
166  C C   . CYS A 22  ? 0.8991 0.6058 0.7714 0.0038  -0.2249 0.0533  22  CYS A C   
167  O O   . CYS A 22  ? 0.8957 0.6097 0.7787 0.0056  -0.2226 0.0616  22  CYS A O   
168  C CB  . CYS A 22  ? 0.9326 0.6318 0.7796 0.0030  -0.2317 0.0466  22  CYS A CB  
169  S SG  . CYS A 22  ? 1.0889 0.7770 0.9315 0.0044  -0.2305 0.0346  22  CYS A SG  
170  N N   . ALA A 23  ? 0.8579 0.5608 0.7367 0.0038  -0.2219 0.0479  23  ALA A N   
171  C CA  . ALA A 23  ? 0.8483 0.5546 0.7483 0.0058  -0.2153 0.0506  23  ALA A CA  
172  C C   . ALA A 23  ? 0.8920 0.5939 0.8012 0.0083  -0.2107 0.0435  23  ALA A C   
173  O O   . ALA A 23  ? 1.0358 0.7316 0.9373 0.0078  -0.2115 0.0337  23  ALA A O   
174  C CB  . ALA A 23  ? 0.8264 0.5328 0.7297 0.0039  -0.2144 0.0487  23  ALA A CB  
175  N N   . VAL A 24  ? 0.8347 0.5403 0.7607 0.0112  -0.2054 0.0487  24  VAL A N   
176  C CA  . VAL A 24  ? 0.8205 0.5226 0.7571 0.0137  -0.2003 0.0425  24  VAL A CA  
177  C C   . VAL A 24  ? 0.9072 0.6109 0.8648 0.0143  -0.1928 0.0397  24  VAL A C   
178  O O   . VAL A 24  ? 0.9324 0.6418 0.9061 0.0151  -0.1886 0.0480  24  VAL A O   
179  C CB  . VAL A 24  ? 0.8201 0.5251 0.7632 0.0167  -0.1986 0.0495  24  VAL A CB  
180  C CG1 . VAL A 24  ? 0.8677 0.5685 0.8212 0.0192  -0.1932 0.0421  24  VAL A CG1 
181  C CG2 . VAL A 24  ? 0.8482 0.5529 0.7710 0.0156  -0.2061 0.0519  24  VAL A CG2 
182  N N   . TYR A 25  ? 0.9523 0.6518 0.9102 0.0138  -0.1908 0.0279  25  TYR A N   
183  C CA  . TYR A 25  ? 0.8967 0.5982 0.8748 0.0140  -0.1832 0.0226  25  TYR A CA  
184  C C   . TYR A 25  ? 0.8402 0.5401 0.8303 0.0164  -0.1772 0.0160  25  TYR A C   
185  O O   . TYR A 25  ? 0.8785 0.5743 0.8558 0.0166  -0.1799 0.0081  25  TYR A O   
186  C CB  . TYR A 25  ? 0.9220 0.6225 0.8923 0.0112  -0.1852 0.0134  25  TYR A CB  
187  C CG  . TYR A 25  ? 0.9121 0.6135 0.8709 0.0086  -0.1908 0.0188  25  TYR A CG  
188  C CD1 . TYR A 25  ? 0.8950 0.5932 0.8307 0.0074  -0.1988 0.0203  25  TYR A CD1 
189  C CD2 . TYR A 25  ? 0.9107 0.6161 0.8823 0.0073  -0.1877 0.0220  25  TYR A CD2 
190  C CE1 . TYR A 25  ? 0.8971 0.5963 0.8229 0.0050  -0.2034 0.0246  25  TYR A CE1 
191  C CE2 . TYR A 25  ? 0.8584 0.5646 0.8193 0.0050  -0.1928 0.0266  25  TYR A CE2 
192  C CZ  . TYR A 25  ? 0.8973 0.6004 0.8353 0.0039  -0.2005 0.0277  25  TYR A CZ  
193  O OH  . TYR A 25  ? 0.9522 0.6562 0.8802 0.0014  -0.2051 0.0317  25  TYR A OH  
194  N N   . GLY A 26  ? 0.8242 0.5276 0.8391 0.0183  -0.1688 0.0192  26  GLY A N   
195  C CA  . GLY A 26  ? 0.8782 0.5805 0.9074 0.0205  -0.1618 0.0122  26  GLY A CA  
196  C C   . GLY A 26  ? 0.8118 0.5153 0.8548 0.0241  -0.1574 0.0217  26  GLY A C   
197  O O   . GLY A 26  ? 0.9034 0.6085 0.9701 0.0259  -0.1481 0.0199  26  GLY A O   
198  N N   . VAL A 27  ? 0.8077 0.5114 0.8372 0.0250  -0.1635 0.0315  27  VAL A N   
199  C CA  . VAL A 27  ? 0.8074 0.5137 0.8482 0.0286  -0.1602 0.0415  27  VAL A CA  
200  C C   . VAL A 27  ? 0.8572 0.5699 0.8943 0.0287  -0.1641 0.0564  27  VAL A C   
201  O O   . VAL A 27  ? 0.8807 0.5937 0.8987 0.0259  -0.1719 0.0576  27  VAL A O   
202  C CB  . VAL A 27  ? 0.8135 0.5151 0.8414 0.0302  -0.1636 0.0379  27  VAL A CB  
203  C CG1 . VAL A 27  ? 0.8434 0.5406 0.8800 0.0309  -0.1577 0.0245  27  VAL A CG1 
204  C CG2 . VAL A 27  ? 0.8726 0.5710 0.8709 0.0276  -0.1744 0.0360  27  VAL A CG2 
205  N N   . SER A 28  ? 0.8351 0.5539 0.8913 0.0320  -0.1584 0.0677  28  SER A N   
206  C CA  . SER A 28  ? 0.8111 0.5383 0.8639 0.0327  -0.1619 0.0826  28  SER A CA  
207  C C   . SER A 28  ? 0.8229 0.5499 0.8536 0.0327  -0.1703 0.0842  28  SER A C   
208  O O   . SER A 28  ? 0.8394 0.5606 0.8647 0.0337  -0.1708 0.0775  28  SER A O   
209  C CB  . SER A 28  ? 0.8065 0.5414 0.8865 0.0369  -0.1530 0.0949  28  SER A CB  
210  O OG  . SER A 28  ? 0.8495 0.5950 0.9276 0.0376  -0.1560 0.1096  28  SER A OG  
211  N N   . LEU A 29  ? 0.8315 0.5655 0.8497 0.0312  -0.1766 0.0929  29  LEU A N   
212  C CA  . LEU A 29  ? 0.8454 0.5809 0.8440 0.0307  -0.1842 0.0949  29  LEU A CA  
213  C C   . LEU A 29  ? 0.8475 0.5887 0.8574 0.0349  -0.1808 0.1034  29  LEU A C   
214  O O   . LEU A 29  ? 0.8363 0.5767 0.8321 0.0349  -0.1859 0.1023  29  LEU A O   
215  C CB  . LEU A 29  ? 0.8847 0.6283 0.8693 0.0279  -0.1909 0.1019  29  LEU A CB  
216  C CG  . LEU A 29  ? 0.9001 0.6400 0.8762 0.0240  -0.1937 0.0962  29  LEU A CG  
217  C CD1 . LEU A 29  ? 0.9389 0.6880 0.9027 0.0215  -0.1997 0.1037  29  LEU A CD1 
218  C CD2 . LEU A 29  ? 0.8195 0.5471 0.7792 0.0216  -0.1975 0.0818  29  LEU A CD2 
219  N N   . ARG A 30  ? 0.8417 0.5887 0.8770 0.0385  -0.1721 0.1118  30  ARG A N   
220  C CA  . ARG A 30  ? 0.8335 0.5868 0.8819 0.0431  -0.1680 0.1212  30  ARG A CA  
221  C C   . ARG A 30  ? 0.8099 0.5530 0.8582 0.0446  -0.1661 0.1112  30  ARG A C   
222  O O   . ARG A 30  ? 0.8090 0.5426 0.8636 0.0441  -0.1618 0.0998  30  ARG A O   
223  C CB  . ARG A 30  ? 0.8787 0.6399 0.9565 0.0468  -0.1580 0.1324  30  ARG A CB  
224  C CG  . ARG A 30  ? 0.9094 0.6815 0.9890 0.0456  -0.1592 0.1430  30  ARG A CG  
225  C CD  . ARG A 30  ? 0.9939 0.7659 1.0986 0.0467  -0.1497 0.1451  30  ARG A CD  
226  N NE  . ARG A 30  ? 1.0319 0.8127 1.1359 0.0450  -0.1515 0.1534  30  ARG A NE  
227  C CZ  . ARG A 30  ? 0.9976 0.7763 1.1136 0.0437  -0.1469 0.1516  30  ARG A CZ  
228  N NH1 . ARG A 30  ? 0.9456 0.7144 1.0758 0.0436  -0.1400 0.1414  30  ARG A NH1 
229  N NH2 . ARG A 30  ? 0.9046 0.6919 1.0184 0.0422  -0.1491 0.1599  30  ARG A NH2 
230  N N   . GLY A 31  ? 0.8154 0.5616 0.8567 0.0464  -0.1693 0.1153  31  GLY A N   
231  C CA  . GLY A 31  ? 0.8102 0.5474 0.8503 0.0480  -0.1680 0.1069  31  GLY A CA  
232  C C   . GLY A 31  ? 0.8348 0.5641 0.8472 0.0447  -0.1773 0.0963  31  GLY A C   
233  O O   . GLY A 31  ? 0.8407 0.5628 0.8501 0.0460  -0.1769 0.0894  31  GLY A O   
234  N N   . TYR A 32  ? 0.8403 0.5706 0.8328 0.0405  -0.1852 0.0949  32  TYR A N   
235  C CA  . TYR A 32  ? 0.8171 0.5394 0.7841 0.0371  -0.1933 0.0847  32  TYR A CA  
236  C C   . TYR A 32  ? 0.8462 0.5769 0.7962 0.0344  -0.2015 0.0911  32  TYR A C   
237  O O   . TYR A 32  ? 0.8512 0.5940 0.8074 0.0346  -0.2013 0.1023  32  TYR A O   
238  C CB  . TYR A 32  ? 0.8536 0.5664 0.8129 0.0340  -0.1942 0.0726  32  TYR A CB  
239  C CG  . TYR A 32  ? 0.8395 0.5463 0.8164 0.0359  -0.1859 0.0653  32  TYR A CG  
240  C CD1 . TYR A 32  ? 0.8230 0.5221 0.8010 0.0376  -0.1834 0.0563  32  TYR A CD1 
241  C CD2 . TYR A 32  ? 0.8312 0.5406 0.8240 0.0357  -0.1803 0.0667  32  TYR A CD2 
242  C CE1 . TYR A 32  ? 0.8307 0.5259 0.8255 0.0389  -0.1753 0.0485  32  TYR A CE1 
243  C CE2 . TYR A 32  ? 0.8382 0.5433 0.8482 0.0370  -0.1722 0.0591  32  TYR A CE2 
244  C CZ  . TYR A 32  ? 0.8665 0.5650 0.8777 0.0385  -0.1697 0.0497  32  TYR A CZ  
245  O OH  . TYR A 32  ? 0.9678 0.6633 0.9969 0.0394  -0.1612 0.0411  32  TYR A OH  
246  N N   . TYR A 33  ? 0.8213 0.5459 0.7500 0.0318  -0.2084 0.0836  33  TYR A N   
247  C CA  . TYR A 33  ? 0.8236 0.5539 0.7339 0.0280  -0.2163 0.0858  33  TYR A CA  
248  C C   . TYR A 33  ? 0.8264 0.5477 0.7221 0.0240  -0.2198 0.0759  33  TYR A C   
249  O O   . TYR A 33  ? 0.8853 0.5952 0.7797 0.0242  -0.2181 0.0659  33  TYR A O   
250  C CB  . TYR A 33  ? 0.8246 0.5547 0.7221 0.0277  -0.2212 0.0843  33  TYR A CB  
251  C CG  . TYR A 33  ? 0.8227 0.5655 0.7308 0.0308  -0.2197 0.0958  33  TYR A CG  
252  C CD1 . TYR A 33  ? 0.8203 0.5734 0.7497 0.0345  -0.2134 0.1071  33  TYR A CD1 
253  C CD2 . TYR A 33  ? 0.8233 0.5684 0.7206 0.0303  -0.2243 0.0957  33  TYR A CD2 
254  C CE1 . TYR A 33  ? 0.8186 0.5844 0.7583 0.0378  -0.2116 0.1185  33  TYR A CE1 
255  C CE2 . TYR A 33  ? 0.8215 0.5793 0.7283 0.0334  -0.2230 0.1063  33  TYR A CE2 
256  C CZ  . TYR A 33  ? 0.8191 0.5876 0.7472 0.0373  -0.2167 0.1180  33  TYR A CZ  
257  O OH  . TYR A 33  ? 0.8713 0.6536 0.8094 0.0407  -0.2151 0.1295  33  TYR A OH  
258  N N   . TRP A 34  ? 0.8276 0.5548 0.7128 0.0204  -0.2246 0.0785  34  TRP A N   
259  C CA  . TRP A 34  ? 0.8297 0.5494 0.7030 0.0169  -0.2273 0.0705  34  TRP A CA  
260  C C   . TRP A 34  ? 0.8480 0.5682 0.7008 0.0128  -0.2346 0.0677  34  TRP A C   
261  O O   . TRP A 34  ? 0.8532 0.5852 0.7036 0.0111  -0.2373 0.0748  34  TRP A O   
262  C CB  . TRP A 34  ? 0.8305 0.5555 0.7137 0.0164  -0.2245 0.0753  34  TRP A CB  
263  C CG  . TRP A 34  ? 0.8444 0.5685 0.7491 0.0202  -0.2167 0.0772  34  TRP A CG  
264  C CD1 . TRP A 34  ? 0.8376 0.5706 0.7612 0.0237  -0.2115 0.0873  34  TRP A CD1 
265  C CD2 . TRP A 34  ? 0.8632 0.5776 0.7738 0.0207  -0.2127 0.0682  34  TRP A CD2 
266  N NE1 . TRP A 34  ? 0.8255 0.5541 0.7671 0.0262  -0.2041 0.0851  34  TRP A NE1 
267  C CE2 . TRP A 34  ? 0.8279 0.5456 0.7617 0.0242  -0.2048 0.0729  34  TRP A CE2 
268  C CE3 . TRP A 34  ? 0.8728 0.5773 0.7719 0.0185  -0.2147 0.0569  34  TRP A CE3 
269  C CZ2 . TRP A 34  ? 0.8642 0.5756 0.8102 0.0252  -0.1989 0.0656  34  TRP A CZ2 
270  C CZ3 . TRP A 34  ? 0.8651 0.5646 0.7756 0.0197  -0.2092 0.0501  34  TRP A CZ3 
271  C CH2 . TRP A 34  ? 0.8427 0.5457 0.7764 0.0227  -0.2014 0.0540  34  TRP A CH2 
272  N N   . THR A 35  ? 0.8431 0.5516 0.6821 0.0111  -0.2372 0.0574  35  THR A N   
273  C CA  . THR A 35  ? 0.8379 0.5447 0.6585 0.0074  -0.2432 0.0535  35  THR A CA  
274  C C   . THR A 35  ? 0.8406 0.5403 0.6496 0.0042  -0.2455 0.0467  35  THR A C   
275  O O   . THR A 35  ? 0.8403 0.5323 0.6519 0.0052  -0.2429 0.0416  35  THR A O   
276  C CB  . THR A 35  ? 0.8382 0.5374 0.6524 0.0087  -0.2444 0.0480  35  THR A CB  
277  O OG1 . THR A 35  ? 0.9455 0.6521 0.7703 0.0116  -0.2425 0.0549  35  THR A OG1 
278  C CG2 . THR A 35  ? 0.8414 0.5381 0.6375 0.0048  -0.2501 0.0434  35  THR A CG2 
279  N N   . TRP A 36  ? 0.8432 0.5464 0.6401 0.0002  -0.2499 0.0466  36  TRP A N   
280  C CA  . TRP A 36  ? 0.8463 0.5426 0.6310 -0.0030 -0.2522 0.0402  36  TRP A CA  
281  C C   . TRP A 36  ? 0.8489 0.5380 0.6197 -0.0047 -0.2555 0.0337  36  TRP A C   
282  O O   . TRP A 36  ? 0.8495 0.5445 0.6158 -0.0065 -0.2581 0.0356  36  TRP A O   
283  C CB  . TRP A 36  ? 0.8476 0.5533 0.6302 -0.0066 -0.2541 0.0445  36  TRP A CB  
284  C CG  . TRP A 36  ? 0.8457 0.5562 0.6398 -0.0054 -0.2511 0.0496  36  TRP A CG  
285  C CD1 . TRP A 36  ? 0.8429 0.5644 0.6505 -0.0033 -0.2486 0.0585  36  TRP A CD1 
286  C CD2 . TRP A 36  ? 0.8464 0.5514 0.6402 -0.0061 -0.2500 0.0464  36  TRP A CD2 
287  N NE1 . TRP A 36  ? 0.8419 0.5645 0.6578 -0.0029 -0.2460 0.0609  36  TRP A NE1 
288  C CE2 . TRP A 36  ? 0.8439 0.5565 0.6513 -0.0046 -0.2469 0.0533  36  TRP A CE2 
289  C CE3 . TRP A 36  ? 0.8551 0.5500 0.6390 -0.0076 -0.2510 0.0388  36  TRP A CE3 
290  C CZ2 . TRP A 36  ? 0.8932 0.6033 0.7041 -0.0050 -0.2453 0.0523  36  TRP A CZ2 
291  C CZ3 . TRP A 36  ? 0.8846 0.5776 0.6719 -0.0078 -0.2494 0.0381  36  TRP A CZ3 
292  C CH2 . TRP A 36  ? 0.9248 0.6251 0.7252 -0.0067 -0.2467 0.0445  36  TRP A CH2 
293  N N   . ILE A 37  ? 0.8502 0.5276 0.6148 -0.0040 -0.2550 0.0262  37  ILE A N   
294  C CA  . ILE A 37  ? 0.8718 0.5412 0.6236 -0.0053 -0.2575 0.0200  37  ILE A CA  
295  C C   . ILE A 37  ? 0.8750 0.5384 0.6174 -0.0077 -0.2584 0.0153  37  ILE A C   
296  O O   . ILE A 37  ? 0.9262 0.5863 0.6716 -0.0064 -0.2563 0.0136  37  ILE A O   
297  C CB  . ILE A 37  ? 0.8515 0.5130 0.6046 -0.0016 -0.2557 0.0155  37  ILE A CB  
298  C CG1 . ILE A 37  ? 0.8481 0.5155 0.6125 0.0012  -0.2540 0.0206  37  ILE A CG1 
299  C CG2 . ILE A 37  ? 0.8542 0.5081 0.5940 -0.0029 -0.2583 0.0097  37  ILE A CG2 
300  C CD1 . ILE A 37  ? 0.8450 0.5123 0.6236 0.0049  -0.2491 0.0214  37  ILE A CD1 
301  N N   . ARG A 38  ? 0.8593 0.5216 0.5912 -0.0113 -0.2612 0.0131  38  ARG A N   
302  C CA  . ARG A 38  ? 0.8644 0.5211 0.5879 -0.0137 -0.2616 0.0091  38  ARG A CA  
303  C C   . ARG A 38  ? 0.8931 0.5400 0.6068 -0.0135 -0.2622 0.0031  38  ARG A C   
304  O O   . ARG A 38  ? 0.9020 0.5479 0.6131 -0.0134 -0.2635 0.0021  38  ARG A O   
305  C CB  . ARG A 38  ? 0.8809 0.5448 0.6016 -0.0184 -0.2633 0.0111  38  ARG A CB  
306  C CG  . ARG A 38  ? 0.8694 0.5371 0.5845 -0.0217 -0.2657 0.0102  38  ARG A CG  
307  C CD  . ARG A 38  ? 0.8682 0.5443 0.5817 -0.0266 -0.2666 0.0111  38  ARG A CD  
308  N NE  . ARG A 38  ? 0.8699 0.5504 0.5781 -0.0308 -0.2685 0.0087  38  ARG A NE  
309  C CZ  . ARG A 38  ? 0.8716 0.5608 0.5784 -0.0357 -0.2691 0.0082  38  ARG A CZ  
310  N NH1 . ARG A 38  ? 0.8720 0.5658 0.5817 -0.0369 -0.2682 0.0102  38  ARG A NH1 
311  N NH2 . ARG A 38  ? 0.9314 0.6252 0.6342 -0.0396 -0.2706 0.0051  38  ARG A NH2 
312  N N   . GLN A 39  ? 0.8676 0.5076 0.5763 -0.0134 -0.2612 -0.0005 39  GLN A N   
313  C CA  . GLN A 39  ? 0.8703 0.5013 0.5701 -0.0130 -0.2612 -0.0055 39  GLN A CA  
314  C C   . GLN A 39  ? 0.9261 0.5542 0.6196 -0.0160 -0.2611 -0.0070 39  GLN A C   
315  O O   . GLN A 39  ? 0.9475 0.5764 0.6429 -0.0161 -0.2598 -0.0061 39  GLN A O   
316  C CB  . GLN A 39  ? 0.8868 0.5126 0.5876 -0.0085 -0.2591 -0.0085 39  GLN A CB  
317  C CG  . GLN A 39  ? 0.9061 0.5241 0.5983 -0.0073 -0.2591 -0.0130 39  GLN A CG  
318  C CD  . GLN A 39  ? 0.9438 0.5591 0.6371 -0.0030 -0.2568 -0.0163 39  GLN A CD  
319  O OE1 . GLN A 39  ? 0.9560 0.5670 0.6451 -0.0010 -0.2567 -0.0196 39  GLN A OE1 
320  N NE2 . GLN A 39  ? 0.9294 0.5479 0.6283 -0.0016 -0.2549 -0.0159 39  GLN A NE2 
321  N N   . SER A 40  ? 0.9118 0.5366 0.5985 -0.0186 -0.2620 -0.0095 40  SER A N   
322  C CA  . SER A 40  ? 0.8817 0.5023 0.5632 -0.0213 -0.2609 -0.0115 40  SER A CA  
323  C C   . SER A 40  ? 0.9096 0.5231 0.5843 -0.0217 -0.2610 -0.0151 40  SER A C   
324  O O   . SER A 40  ? 0.8893 0.5031 0.5630 -0.0213 -0.2626 -0.0158 40  SER A O   
325  C CB  . SER A 40  ? 0.9513 0.5789 0.6343 -0.0264 -0.2616 -0.0102 40  SER A CB  
326  O OG  . SER A 40  ? 1.0012 0.6319 0.6821 -0.0298 -0.2633 -0.0116 40  SER A OG  
327  N N   . PRO A 41  ? 0.9785 0.5856 0.6488 -0.0222 -0.2589 -0.0171 41  PRO A N   
328  C CA  . PRO A 41  ? 0.9689 0.5695 0.6335 -0.0230 -0.2586 -0.0202 41  PRO A CA  
329  C C   . PRO A 41  ? 0.9511 0.5552 0.6153 -0.0283 -0.2601 -0.0217 41  PRO A C   
330  O O   . PRO A 41  ? 0.9069 0.5078 0.5676 -0.0287 -0.2610 -0.0239 41  PRO A O   
331  C CB  . PRO A 41  ? 1.0224 0.6169 0.6846 -0.0223 -0.2552 -0.0207 41  PRO A CB  
332  C CG  . PRO A 41  ? 1.0725 0.6712 0.7389 -0.0226 -0.2543 -0.0183 41  PRO A CG  
333  C CD  . PRO A 41  ? 1.0100 0.6149 0.6808 -0.0207 -0.2564 -0.0163 41  PRO A CD  
334  N N   . LYS A 42  ? 0.9441 0.5556 0.6118 -0.0325 -0.2603 -0.0208 42  LYS A N   
335  C CA  . LYS A 42  ? 0.9242 0.5417 0.5921 -0.0378 -0.2617 -0.0228 42  LYS A CA  
336  C C   . LYS A 42  ? 0.8884 0.5127 0.5576 -0.0371 -0.2650 -0.0211 42  LYS A C   
337  O O   . LYS A 42  ? 0.8884 0.5131 0.5553 -0.0390 -0.2664 -0.0235 42  LYS A O   
338  C CB  . LYS A 42  ? 0.9982 0.6238 0.6697 -0.0425 -0.2608 -0.0227 42  LYS A CB  
339  C CG  . LYS A 42  ? 1.0817 0.7016 0.7533 -0.0429 -0.2573 -0.0235 42  LYS A CG  
340  C CD  . LYS A 42  ? 1.0380 0.6668 0.7134 -0.0483 -0.2565 -0.0245 42  LYS A CD  
341  C CE  . LYS A 42  ? 1.0959 0.7196 0.7724 -0.0483 -0.2529 -0.0246 42  LYS A CE  
342  N NZ  . LYS A 42  ? 1.2062 0.8283 0.8836 -0.0433 -0.2533 -0.0203 42  LYS A NZ  
343  N N   . LYS A 43  ? 0.9152 0.5451 0.5890 -0.0342 -0.2660 -0.0169 43  LYS A N   
344  C CA  . LYS A 43  ? 0.9103 0.5479 0.5875 -0.0331 -0.2685 -0.0141 43  LYS A CA  
345  C C   . LYS A 43  ? 0.8786 0.5094 0.5552 -0.0277 -0.2687 -0.0139 43  LYS A C   
346  O O   . LYS A 43  ? 0.8756 0.5111 0.5547 -0.0266 -0.2705 -0.0120 43  LYS A O   
347  C CB  . LYS A 43  ? 0.9161 0.5648 0.6003 -0.0331 -0.2689 -0.0090 43  LYS A CB  
348  C CG  . LYS A 43  ? 0.9509 0.6073 0.6361 -0.0382 -0.2685 -0.0093 43  LYS A CG  
349  C CD  . LYS A 43  ? 0.9635 0.6260 0.6463 -0.0437 -0.2695 -0.0129 43  LYS A CD  
350  C CE  . LYS A 43  ? 0.9302 0.6041 0.6158 -0.0439 -0.2722 -0.0101 43  LYS A CE  
351  N NZ  . LYS A 43  ? 1.0024 0.6805 0.6848 -0.0488 -0.2734 -0.0146 43  LYS A NZ  
352  N N   . GLY A 44  ? 0.8798 0.5010 0.5537 -0.0244 -0.2668 -0.0157 44  GLY A N   
353  C CA  . GLY A 44  ? 0.8774 0.4937 0.5515 -0.0193 -0.2666 -0.0161 44  GLY A CA  
354  C C   . GLY A 44  ? 0.8944 0.5163 0.5768 -0.0163 -0.2660 -0.0124 44  GLY A C   
355  O O   . GLY A 44  ? 0.9035 0.5290 0.5901 -0.0165 -0.2649 -0.0101 44  GLY A O   
356  N N   . LEU A 45  ? 0.8762 0.4989 0.5619 -0.0134 -0.2665 -0.0117 45  LEU A N   
357  C CA  . LEU A 45  ? 0.8665 0.4953 0.5623 -0.0107 -0.2655 -0.0078 45  LEU A CA  
358  C C   . LEU A 45  ? 0.8782 0.5171 0.5784 -0.0127 -0.2674 -0.0032 45  LEU A C   
359  O O   . LEU A 45  ? 0.8925 0.5318 0.5903 -0.0132 -0.2691 -0.0038 45  LEU A O   
360  C CB  . LEU A 45  ? 0.8641 0.4881 0.5624 -0.0059 -0.2638 -0.0101 45  LEU A CB  
361  C CG  . LEU A 45  ? 0.8629 0.4853 0.5660 -0.0028 -0.2607 -0.0114 45  LEU A CG  
362  C CD1 . LEU A 45  ? 0.8601 0.4799 0.5676 0.0015  -0.2586 -0.0142 45  LEU A CD1 
363  C CD2 . LEU A 45  ? 0.8709 0.5008 0.5830 -0.0035 -0.2597 -0.0067 45  LEU A CD2 
364  N N   . GLU A 46  ? 0.9220 0.5699 0.6287 -0.0140 -0.2671 0.0016  46  GLU A N   
365  C CA  . GLU A 46  ? 0.9207 0.5809 0.6310 -0.0165 -0.2690 0.0063  46  GLU A CA  
366  C C   . GLU A 46  ? 0.9688 0.6380 0.6912 -0.0139 -0.2674 0.0131  46  GLU A C   
367  O O   . GLU A 46  ? 0.9726 0.6422 0.6998 -0.0130 -0.2654 0.0147  46  GLU A O   
368  C CB  . GLU A 46  ? 0.9236 0.5890 0.6293 -0.0219 -0.2702 0.0056  46  GLU A CB  
369  C CG  . GLU A 46  ? 0.9902 0.6690 0.6970 -0.0254 -0.2725 0.0083  46  GLU A CG  
370  C CD  . GLU A 46  ? 1.1020 0.7875 0.8058 -0.0309 -0.2731 0.0070  46  GLU A CD  
371  O OE1 . GLU A 46  ? 1.0032 0.6825 0.7049 -0.0316 -0.2716 0.0048  46  GLU A OE1 
372  O OE2 . GLU A 46  ? 1.2283 0.9263 0.9325 -0.0345 -0.2748 0.0080  46  GLU A OE2 
373  N N   . TRP A 47  ? 0.9284 0.6050 0.6563 -0.0125 -0.2679 0.0173  47  TRP A N   
374  C CA  . TRP A 47  ? 0.8528 0.5397 0.5935 -0.0100 -0.2661 0.0251  47  TRP A CA  
375  C C   . TRP A 47  ? 0.8531 0.5541 0.5954 -0.0136 -0.2674 0.0301  47  TRP A C   
376  O O   . TRP A 47  ? 0.8896 0.5982 0.6267 -0.0172 -0.2701 0.0299  47  TRP A O   
377  C CB  . TRP A 47  ? 0.8719 0.5621 0.6179 -0.0071 -0.2660 0.0282  47  TRP A CB  
378  C CG  . TRP A 47  ? 0.9563 0.6563 0.7172 -0.0036 -0.2632 0.0367  47  TRP A CG  
379  C CD1 . TRP A 47  ? 0.9415 0.6372 0.7133 0.0007  -0.2589 0.0380  47  TRP A CD1 
380  C CD2 . TRP A 47  ? 0.9817 0.6982 0.7493 -0.0039 -0.2639 0.0452  47  TRP A CD2 
381  N NE1 . TRP A 47  ? 0.8843 0.5918 0.6699 0.0032  -0.2566 0.0472  47  TRP A NE1 
382  C CE2 . TRP A 47  ? 0.9484 0.6692 0.7314 0.0006  -0.2597 0.0522  47  TRP A CE2 
383  C CE3 . TRP A 47  ? 0.9427 0.6720 0.7055 -0.0077 -0.2674 0.0475  47  TRP A CE3 
384  C CZ2 . TRP A 47  ? 0.9319 0.6692 0.7254 0.0019  -0.2589 0.0624  47  TRP A CZ2 
385  C CZ3 . TRP A 47  ? 0.9470 0.6938 0.7195 -0.0066 -0.2669 0.0571  47  TRP A CZ3 
386  C CH2 . TRP A 47  ? 0.9643 0.7149 0.7519 -0.0016 -0.2627 0.0649  47  TRP A CH2 
387  N N   . ILE A 48  ? 0.8522 0.5574 0.6019 -0.0128 -0.2653 0.0343  48  ILE A N   
388  C CA  . ILE A 48  ? 0.8571 0.5766 0.6087 -0.0160 -0.2663 0.0393  48  ILE A CA  
389  C C   . ILE A 48  ? 0.8833 0.6177 0.6467 -0.0135 -0.2653 0.0488  48  ILE A C   
390  O O   . ILE A 48  ? 0.8834 0.6319 0.6461 -0.0159 -0.2674 0.0523  48  ILE A O   
391  C CB  . ILE A 48  ? 0.8534 0.5705 0.6061 -0.0168 -0.2648 0.0390  48  ILE A CB  
392  C CG1 . ILE A 48  ? 0.8627 0.5643 0.6057 -0.0178 -0.2650 0.0304  48  ILE A CG1 
393  C CG2 . ILE A 48  ? 0.8542 0.5854 0.6062 -0.0210 -0.2663 0.0423  48  ILE A CG2 
394  C CD1 . ILE A 48  ? 0.8597 0.5564 0.6055 -0.0170 -0.2629 0.0300  48  ILE A CD1 
395  N N   . GLY A 49  ? 0.9359 0.6683 0.7110 -0.0088 -0.2617 0.0532  49  GLY A N   
396  C CA  . GLY A 49  ? 0.9450 0.6911 0.7331 -0.0059 -0.2598 0.0632  49  GLY A CA  
397  C C   . GLY A 49  ? 0.9572 0.6977 0.7590 -0.0008 -0.2549 0.0661  49  GLY A C   
398  O O   . GLY A 49  ? 0.9593 0.6879 0.7609 -0.0001 -0.2530 0.0608  49  GLY A O   
399  N N   . GLU A 50  ? 0.9166 0.6669 0.7314 0.0028  -0.2523 0.0748  50  GLU A N   
400  C CA  . GLU A 50  ? 0.8396 0.5871 0.6707 0.0077  -0.2466 0.0788  50  GLU A CA  
401  C C   . GLU A 50  ? 0.8328 0.5970 0.6778 0.0092  -0.2439 0.0909  50  GLU A C   
402  O O   . GLU A 50  ? 0.8329 0.6124 0.6751 0.0072  -0.2467 0.0968  50  GLU A O   
403  C CB  . GLU A 50  ? 0.8333 0.5753 0.6700 0.0116  -0.2444 0.0780  50  GLU A CB  
404  C CG  . GLU A 50  ? 0.8614 0.6181 0.7048 0.0135  -0.2446 0.0874  50  GLU A CG  
405  C CD  . GLU A 50  ? 0.8728 0.6227 0.7183 0.0166  -0.2434 0.0850  50  GLU A CD  
406  O OE1 . GLU A 50  ? 0.8625 0.5965 0.7016 0.0167  -0.2434 0.0750  50  GLU A OE1 
407  O OE2 . GLU A 50  ? 0.8450 0.6059 0.6986 0.0192  -0.2425 0.0932  50  GLU A OE2 
408  N N   . ILE A 51  ? 0.8309 0.5930 0.6915 0.0127  -0.2383 0.0946  51  ILE A N   
409  C CA  . ILE A 51  ? 0.8349 0.6119 0.7106 0.0147  -0.2348 0.1067  51  ILE A CA  
410  C C   . ILE A 51  ? 0.8646 0.6398 0.7608 0.0202  -0.2276 0.1118  51  ILE A C   
411  O O   . ILE A 51  ? 0.8965 0.6575 0.7957 0.0219  -0.2247 0.1042  51  ILE A O   
412  C CB  . ILE A 51  ? 0.8299 0.6080 0.7040 0.0120  -0.2351 0.1066  51  ILE A CB  
413  C CG1 . ILE A 51  ? 0.8284 0.6261 0.7130 0.0128  -0.2335 0.1197  51  ILE A CG1 
414  C CG2 . ILE A 51  ? 0.8403 0.6050 0.7229 0.0136  -0.2305 0.1016  51  ILE A CG2 
415  C CD1 . ILE A 51  ? 0.8294 0.6300 0.7116 0.0099  -0.2343 0.1201  51  ILE A CD1 
416  N N   . ASP A 52  ? 0.8875 0.6783 0.7988 0.0231  -0.2242 0.1248  52  ASP A N   
417  C CA  . ASP A 52  ? 0.8929 0.6846 0.8268 0.0286  -0.2163 0.1318  52  ASP A CA  
418  C C   . ASP A 52  ? 0.8941 0.6875 0.8414 0.0292  -0.2114 0.1360  52  ASP A C   
419  O O   . ASP A 52  ? 0.8952 0.6905 0.8339 0.0256  -0.2145 0.1347  52  ASP A O   
420  C CB  . ASP A 52  ? 0.8957 0.7048 0.8393 0.0320  -0.2150 0.1448  52  ASP A CB  
421  C CG  . ASP A 52  ? 0.9944 0.7988 0.9544 0.0373  -0.2086 0.1471  52  ASP A CG  
422  O OD1 . ASP A 52  ? 1.1247 0.9149 1.0933 0.0388  -0.2036 0.1404  52  ASP A OD1 
423  O OD2 . ASP A 52  ? 1.0440 0.8598 1.0088 0.0401  -0.2084 0.1555  52  ASP A OD2 
424  N N   . GLU A 53  ? 0.9255 0.7180 0.8950 0.0338  -0.2032 0.1411  53  GLU A N   
425  C CA  . GLU A 53  ? 0.9153 0.7121 0.9006 0.0348  -0.1978 0.1474  53  GLU A CA  
426  C C   . GLU A 53  ? 0.9493 0.7672 0.9426 0.0363  -0.1972 0.1633  53  GLU A C   
427  O O   . GLU A 53  ? 0.9772 0.8014 0.9755 0.0354  -0.1959 0.1685  53  GLU A O   
428  C CB  . GLU A 53  ? 0.8474 0.6363 0.8556 0.0388  -0.1884 0.1468  53  GLU A CB  
429  C CG  . GLU A 53  ? 0.8579 0.6538 0.8830 0.0442  -0.1829 0.1562  53  GLU A CG  
430  C CD  . GLU A 53  ? 0.8450 0.6277 0.8680 0.0454  -0.1820 0.1460  53  GLU A CD  
431  O OE1 . GLU A 53  ? 0.8897 0.6647 0.8909 0.0421  -0.1893 0.1359  53  GLU A OE1 
432  O OE2 . GLU A 53  ? 0.8437 0.6241 0.8875 0.0496  -0.1737 0.1482  53  GLU A OE2 
433  N N   . ILE A 54  ? 0.9572 0.7870 0.9517 0.0387  -0.1981 0.1713  54  ILE A N   
434  C CA  . ILE A 54  ? 0.9019 0.7546 0.9025 0.0402  -0.1981 0.1866  54  ILE A CA  
435  C C   . ILE A 54  ? 0.9471 0.8082 0.9273 0.0347  -0.2061 0.1844  54  ILE A C   
436  O O   . ILE A 54  ? 0.9466 0.8250 0.9309 0.0346  -0.2059 0.1947  54  ILE A O   
437  C CB  . ILE A 54  ? 0.9423 0.8062 0.9488 0.0441  -0.1972 0.1950  54  ILE A CB  
438  C CG1 . ILE A 54  ? 0.9995 0.8491 1.0197 0.0483  -0.1909 0.1913  54  ILE A CG1 
439  C CG2 . ILE A 54  ? 0.9536 0.8419 0.9755 0.0478  -0.1936 0.2134  54  ILE A CG2 
440  C CD1 . ILE A 54  ? 0.9661 0.8209 0.9856 0.0509  -0.1920 0.1944  54  ILE A CD1 
441  N N   . GLY A 55  ? 0.8858 0.7353 0.8446 0.0301  -0.2129 0.1709  55  GLY A N   
442  C CA  . GLY A 55  ? 0.8696 0.7262 0.8089 0.0246  -0.2202 0.1673  55  GLY A CA  
443  C C   . GLY A 55  ? 0.8601 0.7208 0.7838 0.0222  -0.2264 0.1631  55  GLY A C   
444  O O   . GLY A 55  ? 0.8530 0.7173 0.7597 0.0170  -0.2324 0.1576  55  GLY A O   
445  N N   . ARG A 56  ? 0.8216 0.6818 0.7508 0.0256  -0.2249 0.1651  56  ARG A N   
446  C CA  . ARG A 56  ? 0.8210 0.6846 0.7358 0.0234  -0.2306 0.1608  56  ARG A CA  
447  C C   . ARG A 56  ? 0.8344 0.6782 0.7301 0.0187  -0.2354 0.1446  56  ARG A C   
448  O O   . ARG A 56  ? 0.8367 0.6614 0.7333 0.0194  -0.2331 0.1368  56  ARG A O   
449  C CB  . ARG A 56  ? 0.8403 0.7055 0.7661 0.0284  -0.2274 0.1661  56  ARG A CB  
450  C CG  . ARG A 56  ? 0.9705 0.8508 0.9195 0.0343  -0.2205 0.1821  56  ARG A CG  
451  C CD  . ARG A 56  ? 1.0322 0.9151 0.9921 0.0394  -0.2173 0.1878  56  ARG A CD  
452  N NE  . ARG A 56  ? 1.1701 1.0295 1.1284 0.0403  -0.2159 0.1764  56  ARG A NE  
453  C CZ  . ARG A 56  ? 1.1448 1.0014 1.1108 0.0443  -0.2132 0.1780  56  ARG A CZ  
454  N NH1 . ARG A 56  ? 1.0941 0.9694 1.0703 0.0480  -0.2116 0.1910  56  ARG A NH1 
455  N NH2 . ARG A 56  ? 1.0879 0.9233 1.0514 0.0446  -0.2120 0.1665  56  ARG A NH2 
456  N N   . THR A 57  ? 0.8497 0.6993 0.7287 0.0140  -0.2418 0.1396  57  THR A N   
457  C CA  . THR A 57  ? 0.8285 0.6619 0.6892 0.0092  -0.2463 0.1254  57  THR A CA  
458  C C   . THR A 57  ? 0.8291 0.6629 0.6784 0.0073  -0.2508 0.1203  57  THR A C   
459  O O   . THR A 57  ? 0.8277 0.6796 0.6789 0.0075  -0.2522 0.1272  57  THR A O   
460  C CB  . THR A 57  ? 0.8306 0.6695 0.6813 0.0039  -0.2495 0.1226  57  THR A CB  
461  O OG1 . THR A 57  ? 0.8453 0.7083 0.6955 0.0021  -0.2517 0.1300  57  THR A OG1 
462  C CG2 . THR A 57  ? 0.8303 0.6654 0.6902 0.0053  -0.2456 0.1256  57  THR A CG2 
463  N N   . LYS A 58  ? 0.8312 0.6455 0.6688 0.0055  -0.2528 0.1082  58  LYS A N   
464  C CA  . LYS A 58  ? 0.8325 0.6445 0.6568 0.0025  -0.2575 0.1013  58  LYS A CA  
465  C C   . LYS A 58  ? 0.8627 0.6628 0.6709 -0.0028 -0.2610 0.0897  58  LYS A C   
466  O O   . LYS A 58  ? 0.9007 0.6843 0.7072 -0.0024 -0.2594 0.0837  58  LYS A O   
467  C CB  . LYS A 58  ? 0.8315 0.6310 0.6585 0.0064  -0.2560 0.0986  58  LYS A CB  
468  C CG  . LYS A 58  ? 0.8324 0.6314 0.6470 0.0037  -0.2607 0.0929  58  LYS A CG  
469  C CD  . LYS A 58  ? 0.8544 0.6447 0.6737 0.0081  -0.2589 0.0924  58  LYS A CD  
470  C CE  . LYS A 58  ? 0.9484 0.7411 0.7565 0.0054  -0.2637 0.0881  58  LYS A CE  
471  N NZ  . LYS A 58  ? 0.9585 0.7459 0.7724 0.0100  -0.2620 0.0895  58  LYS A NZ  
472  N N   . TYR A 59  ? 0.8956 0.7050 0.6930 -0.0079 -0.2653 0.0864  59  TYR A N   
473  C CA  . TYR A 59  ? 0.8767 0.6771 0.6602 -0.0133 -0.2680 0.0763  59  TYR A CA  
474  C C   . TYR A 59  ? 0.9353 0.7295 0.7069 -0.0164 -0.2715 0.0678  59  TYR A C   
475  O O   . TYR A 59  ? 0.9405 0.7435 0.7134 -0.0157 -0.2728 0.0705  59  TYR A O   
476  C CB  . TYR A 59  ? 0.8632 0.6805 0.6448 -0.0178 -0.2694 0.0785  59  TYR A CB  
477  C CG  . TYR A 59  ? 0.8408 0.6637 0.6321 -0.0158 -0.2663 0.0858  59  TYR A CG  
478  C CD1 . TYR A 59  ? 0.8425 0.6501 0.6323 -0.0158 -0.2648 0.0813  59  TYR A CD1 
479  C CD2 . TYR A 59  ? 0.8740 0.7183 0.6762 -0.0139 -0.2650 0.0973  59  TYR A CD2 
480  C CE1 . TYR A 59  ? 0.8415 0.6539 0.6402 -0.0142 -0.2621 0.0876  59  TYR A CE1 
481  C CE2 . TYR A 59  ? 0.8921 0.7415 0.7034 -0.0121 -0.2620 0.1041  59  TYR A CE2 
482  C CZ  . TYR A 59  ? 0.8545 0.6874 0.6640 -0.0124 -0.2606 0.0990  59  TYR A CZ  
483  O OH  . TYR A 59  ? 0.9413 0.7790 0.7599 -0.0108 -0.2577 0.1055  59  TYR A OH  
484  N N   . SER A 60  ? 0.9369 0.7162 0.6975 -0.0196 -0.2727 0.0579  60  SER A N   
485  C CA  . SER A 60  ? 0.9281 0.7037 0.6772 -0.0238 -0.2758 0.0498  60  SER A CA  
486  C C   . SER A 60  ? 1.0512 0.8463 0.7976 -0.0295 -0.2781 0.0500  60  SER A C   
487  O O   . SER A 60  ? 1.0946 0.8993 0.8434 -0.0313 -0.2774 0.0527  60  SER A O   
488  C CB  . SER A 60  ? 0.9013 0.6565 0.6408 -0.0254 -0.2757 0.0401  60  SER A CB  
489  O OG  . SER A 60  ? 1.0334 0.7737 0.7767 -0.0204 -0.2731 0.0400  60  SER A OG  
490  N N   . GLN A 61  ? 1.0586 0.8606 0.8002 -0.0324 -0.2808 0.0470  61  GLN A N   
491  C CA  . GLN A 61  ? 1.0902 0.9134 0.8302 -0.0380 -0.2827 0.0466  61  GLN A CA  
492  C C   . GLN A 61  ? 1.1069 0.9265 0.8401 -0.0436 -0.2825 0.0388  61  GLN A C   
493  O O   . GLN A 61  ? 1.1441 0.9808 0.8794 -0.0470 -0.2825 0.0406  61  GLN A O   
494  C CB  . GLN A 61  ? 1.1299 0.9593 0.8657 -0.0406 -0.2855 0.0430  61  GLN A CB  
495  C CG  . GLN A 61  ? 1.2371 1.0745 0.9801 -0.0356 -0.2858 0.0513  61  GLN A CG  
496  C CD  . GLN A 61  ? 1.2820 1.1334 1.0219 -0.0391 -0.2889 0.0490  61  GLN A CD  
497  O OE1 . GLN A 61  ? 1.2380 1.0959 0.9715 -0.0457 -0.2906 0.0415  61  GLN A OE1 
498  N NE2 . GLN A 61  ? 1.3309 1.1874 1.0762 -0.0348 -0.2893 0.0554  61  GLN A NE2 
499  N N   . SER A 62  ? 1.1814 0.9796 0.9069 -0.0446 -0.2822 0.0303  62  SER A N   
500  C CA  . SER A 62  ? 1.1650 0.9587 0.8848 -0.0498 -0.2815 0.0229  62  SER A CA  
501  C C   . SER A 62  ? 1.2090 1.0047 0.9330 -0.0487 -0.2795 0.0270  62  SER A C   
502  O O   . SER A 62  ? 1.2261 1.0315 0.9492 -0.0534 -0.2792 0.0247  62  SER A O   
503  C CB  . SER A 62  ? 1.1534 0.9234 0.8654 -0.0498 -0.2809 0.0147  62  SER A CB  
504  O OG  . SER A 62  ? 1.2558 1.0224 0.9640 -0.0502 -0.2827 0.0114  62  SER A OG  
505  N N   . LEU A 63  ? 1.1080 0.8948 0.8371 -0.0427 -0.2780 0.0327  63  LEU A N   
506  C CA  . LEU A 63  ? 1.0768 0.8636 0.8102 -0.0415 -0.2760 0.0364  63  LEU A CA  
507  C C   . LEU A 63  ? 1.0622 0.8692 0.8053 -0.0397 -0.2756 0.0467  63  LEU A C   
508  O O   . LEU A 63  ? 1.0121 0.8215 0.7592 -0.0390 -0.2740 0.0503  63  LEU A O   
509  C CB  . LEU A 63  ? 0.9548 0.7211 0.6891 -0.0364 -0.2741 0.0361  63  LEU A CB  
510  C CG  . LEU A 63  ? 0.9797 0.7263 0.7048 -0.0374 -0.2741 0.0270  63  LEU A CG  
511  C CD1 . LEU A 63  ? 0.9007 0.6319 0.6273 -0.0318 -0.2729 0.0271  63  LEU A CD1 
512  C CD2 . LEU A 63  ? 1.0238 0.7644 0.7452 -0.0402 -0.2729 0.0228  63  LEU A CD2 
513  N N   . ARG A 64  ? 1.0339 0.8562 0.7810 -0.0389 -0.2768 0.0518  64  ARG A N   
514  C CA  . ARG A 64  ? 1.0080 0.8513 0.7654 -0.0366 -0.2760 0.0628  64  ARG A CA  
515  C C   . ARG A 64  ? 1.0191 0.8787 0.7762 -0.0411 -0.2760 0.0633  64  ARG A C   
516  O O   . ARG A 64  ? 1.0235 0.8940 0.7887 -0.0388 -0.2744 0.0718  64  ARG A O   
517  C CB  . ARG A 64  ? 1.0135 0.8728 0.7740 -0.0359 -0.2776 0.0673  64  ARG A CB  
518  C CG  . ARG A 64  ? 1.0659 0.9494 0.8375 -0.0332 -0.2765 0.0798  64  ARG A CG  
519  C CD  . ARG A 64  ? 1.1251 1.0065 0.9065 -0.0263 -0.2748 0.0883  64  ARG A CD  
520  N NE  . ARG A 64  ? 1.1970 1.0702 0.9731 -0.0264 -0.2768 0.0831  64  ARG A NE  
521  C CZ  . ARG A 64  ? 1.2944 1.1846 1.0708 -0.0274 -0.2789 0.0854  64  ARG A CZ  
522  N NH1 . ARG A 64  ? 1.2074 1.1252 0.9893 -0.0285 -0.2793 0.0931  64  ARG A NH1 
523  N NH2 . ARG A 64  ? 1.1862 1.0663 0.9572 -0.0275 -0.2807 0.0800  64  ARG A NH2 
524  N N   . SER A 65  ? 1.0094 0.8711 0.7580 -0.0475 -0.2775 0.0541  65  SER A N   
525  C CA  . SER A 65  ? 0.9303 0.8104 0.6788 -0.0524 -0.2774 0.0535  65  SER A CA  
526  C C   . SER A 65  ? 0.9712 0.8429 0.7210 -0.0514 -0.2754 0.0548  65  SER A C   
527  O O   . SER A 65  ? 0.9658 0.8546 0.7199 -0.0524 -0.2747 0.0598  65  SER A O   
528  C CB  . SER A 65  ? 0.8918 0.7741 0.6319 -0.0597 -0.2786 0.0420  65  SER A CB  
529  O OG  . SER A 65  ? 0.8631 0.7449 0.6005 -0.0604 -0.2804 0.0388  65  SER A OG  
530  N N   . ARG A 66  ? 0.9886 0.8353 0.7349 -0.0495 -0.2744 0.0503  66  ARG A N   
531  C CA  . ARG A 66  ? 0.9497 0.7876 0.6962 -0.0493 -0.2727 0.0498  66  ARG A CA  
532  C C   . ARG A 66  ? 0.9767 0.7998 0.7290 -0.0429 -0.2709 0.0551  66  ARG A C   
533  O O   . ARG A 66  ? 1.0098 0.8215 0.7613 -0.0425 -0.2696 0.0533  66  ARG A O   
534  C CB  . ARG A 66  ? 0.9808 0.8039 0.7181 -0.0537 -0.2725 0.0387  66  ARG A CB  
535  C CG  . ARG A 66  ? 0.9563 0.7899 0.6882 -0.0603 -0.2735 0.0310  66  ARG A CG  
536  C CD  . ARG A 66  ? 0.8864 0.7033 0.6119 -0.0611 -0.2740 0.0232  66  ARG A CD  
537  N NE  . ARG A 66  ? 0.8686 0.6618 0.5905 -0.0589 -0.2725 0.0196  66  ARG A NE  
538  C CZ  . ARG A 66  ? 0.9137 0.6895 0.6302 -0.0585 -0.2724 0.0137  66  ARG A CZ  
539  N NH1 . ARG A 66  ? 1.0001 0.7778 0.7139 -0.0603 -0.2737 0.0101  66  ARG A NH1 
540  N NH2 . ARG A 66  ? 0.8906 0.6476 0.6045 -0.0562 -0.2708 0.0114  66  ARG A NH2 
541  N N   . ALA A 67  ? 1.0147 0.8379 0.7732 -0.0381 -0.2706 0.0611  67  ALA A N   
542  C CA  . ALA A 67  ? 0.9846 0.7940 0.7498 -0.0323 -0.2683 0.0649  67  ALA A CA  
543  C C   . ALA A 67  ? 0.9518 0.7757 0.7301 -0.0282 -0.2663 0.0769  67  ALA A C   
544  O O   . ALA A 67  ? 0.9846 0.8255 0.7673 -0.0276 -0.2669 0.0829  67  ALA A O   
545  C CB  . ALA A 67  ? 0.9309 0.7248 0.6937 -0.0295 -0.2685 0.0609  67  ALA A CB  
546  N N   . THR A 68  ? 0.9845 0.8023 0.7698 -0.0254 -0.2636 0.0805  68  THR A N   
547  C CA  . THR A 68  ? 0.9951 0.8245 0.7945 -0.0212 -0.2608 0.0921  68  THR A CA  
548  C C   . THR A 68  ? 0.9588 0.7715 0.7663 -0.0163 -0.2574 0.0926  68  THR A C   
549  O O   . THR A 68  ? 0.9289 0.7298 0.7348 -0.0169 -0.2565 0.0884  68  THR A O   
550  C CB  . THR A 68  ? 1.0565 0.9003 0.8582 -0.0234 -0.2604 0.0968  68  THR A CB  
551  O OG1 . THR A 68  ? 1.2380 1.0966 1.0312 -0.0287 -0.2634 0.0938  68  THR A OG1 
552  C CG2 . THR A 68  ? 0.9471 0.8060 0.7642 -0.0189 -0.2573 0.1101  68  THR A CG2 
553  N N   . LEU A 69  ? 0.9151 0.7277 0.7319 -0.0118 -0.2553 0.0974  69  LEU A N   
554  C CA  . LEU A 69  ? 0.8389 0.6381 0.6657 -0.0072 -0.2512 0.0979  69  LEU A CA  
555  C C   . LEU A 69  ? 0.8361 0.6465 0.6797 -0.0038 -0.2469 0.1093  69  LEU A C   
556  O O   . LEU A 69  ? 0.9174 0.7455 0.7685 -0.0023 -0.2462 0.1191  69  LEU A O   
557  C CB  . LEU A 69  ? 0.8378 0.6297 0.6664 -0.0041 -0.2505 0.0960  69  LEU A CB  
558  C CG  . LEU A 69  ? 0.8402 0.6136 0.6561 -0.0057 -0.2527 0.0839  69  LEU A CG  
559  C CD1 . LEU A 69  ? 0.8389 0.6061 0.6574 -0.0024 -0.2518 0.0826  69  LEU A CD1 
560  C CD2 . LEU A 69  ? 0.8595 0.6187 0.6756 -0.0054 -0.2508 0.0785  69  LEU A CD2 
561  N N   . SER A 70  ? 0.8358 0.6367 0.6856 -0.0026 -0.2439 0.1083  70  SER A N   
562  C CA  . SER A 70  ? 0.8432 0.6526 0.7099 0.0005  -0.2392 0.1185  70  SER A CA  
563  C C   . SER A 70  ? 0.9076 0.7031 0.7866 0.0044  -0.2341 0.1165  70  SER A C   
564  O O   . SER A 70  ? 0.9673 0.7468 0.8397 0.0040  -0.2347 0.1064  70  SER A O   
565  C CB  . SER A 70  ? 0.8361 0.6502 0.7002 -0.0025 -0.2400 0.1196  70  SER A CB  
566  O OG  . SER A 70  ? 0.9094 0.7067 0.7647 -0.0048 -0.2413 0.1091  70  SER A OG  
567  N N   . ILE A 71  ? 0.8484 0.6512 0.7462 0.0081  -0.2286 0.1263  71  ILE A N   
568  C CA  . ILE A 71  ? 0.8831 0.6750 0.7958 0.0117  -0.2226 0.1248  71  ILE A CA  
569  C C   . ILE A 71  ? 0.9132 0.7138 0.8441 0.0138  -0.2172 0.1349  71  ILE A C   
570  O O   . ILE A 71  ? 0.9459 0.7634 0.8819 0.0145  -0.2170 0.1462  71  ILE A O   
571  C CB  . ILE A 71  ? 0.8735 0.6629 0.7939 0.0156  -0.2199 0.1255  71  ILE A CB  
572  C CG1 . ILE A 71  ? 0.8932 0.6679 0.8245 0.0179  -0.2145 0.1189  71  ILE A CG1 
573  C CG2 . ILE A 71  ? 0.8685 0.6751 0.8040 0.0193  -0.2164 0.1400  71  ILE A CG2 
574  C CD1 . ILE A 71  ? 0.8388 0.6087 0.7761 0.0213  -0.2119 0.1171  71  ILE A CD1 
575  N N   . ASP A 72  ? 0.9463 0.7360 0.8873 0.0148  -0.2127 0.1307  72  ASP A N   
576  C CA  . ASP A 72  ? 1.0260 0.8214 0.9866 0.0169  -0.2065 0.1390  72  ASP A CA  
577  C C   . ASP A 72  ? 1.0824 0.8670 1.0599 0.0200  -0.1995 0.1349  72  ASP A C   
578  O O   . ASP A 72  ? 1.1102 0.8821 1.0851 0.0183  -0.1992 0.1241  72  ASP A O   
579  C CB  . ASP A 72  ? 1.0023 0.7965 0.9566 0.0133  -0.2088 0.1366  72  ASP A CB  
580  C CG  . ASP A 72  ? 1.0820 0.8842 1.0557 0.0152  -0.2028 0.1466  72  ASP A CG  
581  O OD1 . ASP A 72  ? 1.1024 0.9117 1.0953 0.0195  -0.1967 0.1562  72  ASP A OD1 
582  O OD2 . ASP A 72  ? 1.1284 0.9296 1.0986 0.0125  -0.2041 0.1451  72  ASP A OD2 
583  N N   . THR A 73  ? 0.9926 0.7834 0.9880 0.0245  -0.1937 0.1434  73  THR A N   
584  C CA  . THR A 73  ? 0.9322 0.7138 0.9454 0.0275  -0.1862 0.1393  73  THR A CA  
585  C C   . THR A 73  ? 0.9891 0.7670 1.0175 0.0272  -0.1804 0.1378  73  THR A C   
586  O O   . THR A 73  ? 1.0533 0.8202 1.0890 0.0273  -0.1764 0.1279  73  THR A O   
587  C CB  . THR A 73  ? 1.0021 0.7926 1.0332 0.0326  -0.1805 0.1503  73  THR A CB  
588  O OG1 . THR A 73  ? 1.1202 0.9261 1.1647 0.0346  -0.1773 0.1654  73  THR A OG1 
589  C CG2 . THR A 73  ? 0.9686 0.7623 0.9849 0.0329  -0.1862 0.1505  73  THR A CG2 
590  N N   . SER A 74  ? 0.9945 0.7823 1.0284 0.0267  -0.1798 0.1473  74  SER A N   
591  C CA  . SER A 74  ? 1.0589 0.8436 1.1077 0.0262  -0.1743 0.1463  74  SER A CA  
592  C C   . SER A 74  ? 1.0739 0.8461 1.1080 0.0218  -0.1785 0.1318  74  SER A C   
593  O O   . SER A 74  ? 1.0338 0.7981 1.0794 0.0215  -0.1735 0.1241  74  SER A O   
594  C CB  . SER A 74  ? 1.0968 0.8952 1.1524 0.0265  -0.1734 0.1599  74  SER A CB  
595  O OG  . SER A 74  ? 1.1955 0.9981 1.2283 0.0227  -0.1822 0.1592  74  SER A OG  
596  N N   . LYS A 75  ? 1.1491 0.9204 1.1588 0.0183  -0.1873 0.1279  75  LYS A N   
597  C CA  . LYS A 75  ? 1.1573 0.9176 1.1521 0.0145  -0.1916 0.1150  75  LYS A CA  
598  C C   . LYS A 75  ? 1.1585 0.9079 1.1429 0.0143  -0.1936 0.1030  75  LYS A C   
599  O O   . LYS A 75  ? 1.1634 0.9040 1.1368 0.0116  -0.1964 0.0921  75  LYS A O   
600  C CB  . LYS A 75  ? 1.1578 0.9221 1.1326 0.0108  -0.1993 0.1163  75  LYS A CB  
601  C CG  . LYS A 75  ? 1.1710 0.9447 1.1545 0.0103  -0.1975 0.1258  75  LYS A CG  
602  C CD  . LYS A 75  ? 1.3207 1.0881 1.3168 0.0096  -0.1929 0.1212  75  LYS A CD  
603  C CE  . LYS A 75  ? 1.2595 1.0370 1.2696 0.0102  -0.1893 0.1327  75  LYS A CE  
604  N NZ  . LYS A 75  ? 1.1901 0.9773 1.2213 0.0147  -0.1825 0.1449  75  LYS A NZ  
605  N N   . LYS A 76  ? 1.0562 0.8067 1.0442 0.0171  -0.1920 0.1051  76  LYS A N   
606  C CA  . LYS A 76  ? 0.9588 0.6995 0.9385 0.0174  -0.1933 0.0944  76  LYS A CA  
607  C C   . LYS A 76  ? 0.9735 0.7083 0.9270 0.0138  -0.2018 0.0863  76  LYS A C   
608  O O   . LYS A 76  ? 0.9873 0.7126 0.9331 0.0126  -0.2029 0.0749  76  LYS A O   
609  C CB  . LYS A 76  ? 0.9678 0.7010 0.9623 0.0184  -0.1866 0.0855  76  LYS A CB  
610  C CG  . LYS A 76  ? 0.9044 0.6422 0.9263 0.0222  -0.1772 0.0923  76  LYS A CG  
611  C CD  . LYS A 76  ? 0.8847 0.6169 0.9232 0.0221  -0.1700 0.0831  76  LYS A CD  
612  C CE  . LYS A 76  ? 0.9105 0.6340 0.9418 0.0219  -0.1704 0.0695  76  LYS A CE  
613  N NZ  . LYS A 76  ? 0.8539 0.5744 0.9034 0.0218  -0.1626 0.0601  76  LYS A NZ  
614  N N   . GLN A 77  ? 0.9715 0.7130 0.9119 0.0121  -0.2075 0.0924  77  GLN A N   
615  C CA  . GLN A 77  ? 0.9177 0.6543 0.8346 0.0087  -0.2149 0.0854  77  GLN A CA  
616  C C   . GLN A 77  ? 0.9319 0.6773 0.8387 0.0080  -0.2194 0.0920  77  GLN A C   
617  O O   . GLN A 77  ? 0.9955 0.7534 0.9089 0.0085  -0.2188 0.1025  77  GLN A O   
618  C CB  . GLN A 77  ? 0.9111 0.6456 0.8206 0.0054  -0.2173 0.0822  77  GLN A CB  
619  C CG  . GLN A 77  ? 0.9545 0.7000 0.8699 0.0046  -0.2170 0.0924  77  GLN A CG  
620  C CD  . GLN A 77  ? 0.9473 0.6894 0.8595 0.0018  -0.2179 0.0887  77  GLN A CD  
621  O OE1 . GLN A 77  ? 0.9077 0.6407 0.8203 0.0014  -0.2167 0.0800  77  GLN A OE1 
622  N NE2 . GLN A 77  ? 0.9131 0.6636 0.8221 -0.0001 -0.2201 0.0953  77  GLN A NE2 
623  N N   . PHE A 78  ? 0.9148 0.6547 0.8063 0.0069  -0.2238 0.0856  78  PHE A N   
624  C CA  . PHE A 78  ? 0.8789 0.6264 0.7587 0.0054  -0.2287 0.0892  78  PHE A CA  
625  C C   . PHE A 78  ? 0.9673 0.7096 0.8270 0.0010  -0.2345 0.0817  78  PHE A C   
626  O O   . PHE A 78  ? 0.9465 0.6778 0.8002 -0.0002 -0.2350 0.0732  78  PHE A O   
627  C CB  . PHE A 78  ? 0.8312 0.5773 0.7114 0.0078  -0.2284 0.0886  78  PHE A CB  
628  C CG  . PHE A 78  ? 0.8319 0.5633 0.7053 0.0081  -0.2286 0.0772  78  PHE A CG  
629  C CD1 . PHE A 78  ? 0.9010 0.6247 0.7858 0.0103  -0.2236 0.0725  78  PHE A CD1 
630  C CD2 . PHE A 78  ? 0.8485 0.5748 0.7048 0.0061  -0.2336 0.0710  78  PHE A CD2 
631  C CE1 . PHE A 78  ? 0.9488 0.6611 0.8273 0.0106  -0.2237 0.0619  78  PHE A CE1 
632  C CE2 . PHE A 78  ? 0.9270 0.6408 0.7770 0.0066  -0.2337 0.0611  78  PHE A CE2 
633  C CZ  . PHE A 78  ? 0.9949 0.7023 0.8557 0.0090  -0.2288 0.0566  78  PHE A CZ  
634  N N   . SER A 79  ? 0.9944 0.7459 0.8444 -0.0016 -0.2387 0.0850  79  SER A N   
635  C CA  . SER A 79  ? 0.9746 0.7231 0.8078 -0.0060 -0.2434 0.0789  79  SER A CA  
636  C C   . SER A 79  ? 0.9663 0.7201 0.7882 -0.0082 -0.2475 0.0781  79  SER A C   
637  O O   . SER A 79  ? 0.9654 0.7303 0.7927 -0.0068 -0.2472 0.0848  79  SER A O   
638  C CB  . SER A 79  ? 0.9808 0.7372 0.8148 -0.0084 -0.2438 0.0831  79  SER A CB  
639  O OG  . SER A 79  ? 1.0515 0.8064 0.8993 -0.0061 -0.2395 0.0862  79  SER A OG  
640  N N   . LEU A 80  ? 0.9705 0.7168 0.7774 -0.0117 -0.2509 0.0699  80  LEU A N   
641  C CA  . LEU A 80  ? 0.9073 0.6583 0.7029 -0.0149 -0.2547 0.0676  80  LEU A CA  
642  C C   . LEU A 80  ? 0.9058 0.6602 0.6920 -0.0197 -0.2571 0.0649  80  LEU A C   
643  O O   . LEU A 80  ? 0.8629 0.6073 0.6448 -0.0208 -0.2569 0.0598  80  LEU A O   
644  C CB  . LEU A 80  ? 0.8631 0.6009 0.6499 -0.0146 -0.2560 0.0593  80  LEU A CB  
645  C CG  . LEU A 80  ? 0.8515 0.5920 0.6259 -0.0186 -0.2597 0.0552  80  LEU A CG  
646  C CD1 . LEU A 80  ? 0.9072 0.6589 0.6848 -0.0177 -0.2606 0.0601  80  LEU A CD1 
647  C CD2 . LEU A 80  ? 0.8542 0.5787 0.6178 -0.0193 -0.2607 0.0457  80  LEU A CD2 
648  N N   . ARG A 81  ? 0.9410 0.7103 0.7245 -0.0226 -0.2591 0.0680  81  ARG A N   
649  C CA  . ARG A 81  ? 0.9497 0.7240 0.7247 -0.0277 -0.2611 0.0647  81  ARG A CA  
650  C C   . ARG A 81  ? 0.9549 0.7311 0.7196 -0.0314 -0.2638 0.0589  81  ARG A C   
651  O O   . ARG A 81  ? 0.9741 0.7624 0.7407 -0.0315 -0.2648 0.0624  81  ARG A O   
652  C CB  . ARG A 81  ? 0.9596 0.7527 0.7412 -0.0286 -0.2606 0.0730  81  ARG A CB  
653  C CG  . ARG A 81  ? 1.0012 0.7990 0.7752 -0.0337 -0.2620 0.0692  81  ARG A CG  
654  C CD  . ARG A 81  ? 1.0320 0.8534 0.8096 -0.0357 -0.2624 0.0760  81  ARG A CD  
655  N NE  . ARG A 81  ? 1.0751 0.9081 0.8503 -0.0371 -0.2642 0.0760  81  ARG A NE  
656  C CZ  . ARG A 81  ? 1.1323 0.9883 0.9096 -0.0391 -0.2649 0.0809  81  ARG A CZ  
657  N NH1 . ARG A 81  ? 1.2343 1.1044 1.0160 -0.0398 -0.2641 0.0865  81  ARG A NH1 
658  N NH2 . ARG A 81  ? 1.1160 0.9818 0.8910 -0.0404 -0.2666 0.0800  81  ARG A NH2 
659  N N   . LEU A 82  ? 0.9475 0.7126 0.7023 -0.0346 -0.2647 0.0502  82  LEU A N   
660  C CA  . LEU A 82  ? 0.9525 0.7185 0.6982 -0.0387 -0.2666 0.0438  82  LEU A CA  
661  C C   . LEU A 82  ? 0.9537 0.7266 0.6947 -0.0441 -0.2669 0.0403  82  LEU A C   
662  O O   . LEU A 82  ? 0.9744 0.7375 0.7128 -0.0448 -0.2659 0.0370  82  LEU A O   
663  C CB  . LEU A 82  ? 0.8961 0.6433 0.6350 -0.0378 -0.2666 0.0364  82  LEU A CB  
664  C CG  . LEU A 82  ? 0.8654 0.6125 0.5974 -0.0406 -0.2683 0.0310  82  LEU A CG  
665  C CD1 . LEU A 82  ? 0.9234 0.6835 0.6601 -0.0393 -0.2695 0.0363  82  LEU A CD1 
666  C CD2 . LEU A 82  ? 0.8674 0.5956 0.5934 -0.0389 -0.2679 0.0249  82  LEU A CD2 
667  N N   . THR A 83  ? 0.9429 0.7332 0.6833 -0.0479 -0.2681 0.0407  83  THR A N   
668  C CA  . THR A 83  ? 0.9770 0.7778 0.7145 -0.0533 -0.2680 0.0375  83  THR A CA  
669  C C   . THR A 83  ? 1.0208 0.8165 0.7502 -0.0583 -0.2683 0.0275  83  THR A C   
670  O O   . THR A 83  ? 0.9797 0.7701 0.7062 -0.0581 -0.2691 0.0244  83  THR A O   
671  C CB  . THR A 83  ? 0.9879 0.8141 0.7308 -0.0546 -0.2687 0.0442  83  THR A CB  
672  O OG1 . THR A 83  ? 1.0017 0.8315 0.7536 -0.0492 -0.2679 0.0545  83  THR A OG1 
673  C CG2 . THR A 83  ? 1.0548 0.8931 0.7960 -0.0597 -0.2682 0.0417  83  THR A CG2 
674  N N   . SER A 84  ? 1.0311 0.8279 0.7575 -0.0628 -0.2671 0.0222  84  SER A N   
675  C CA  . SER A 84  ? 1.0251 0.8181 0.7457 -0.0680 -0.2663 0.0124  84  SER A CA  
676  C C   . SER A 84  ? 1.0655 0.8364 0.7817 -0.0657 -0.2657 0.0080  84  SER A C   
677  O O   . SER A 84  ? 1.1041 0.8726 0.8172 -0.0675 -0.2661 0.0033  84  SER A O   
678  C CB  . SER A 84  ? 1.0386 0.8507 0.7595 -0.0724 -0.2674 0.0102  84  SER A CB  
679  O OG  . SER A 84  ? 1.1341 0.9688 0.8590 -0.0746 -0.2677 0.0143  84  SER A OG  
680  N N   . VAL A 85  ? 1.0357 0.7911 0.7517 -0.0618 -0.2648 0.0097  85  VAL A N   
681  C CA  . VAL A 85  ? 0.9650 0.7009 0.6771 -0.0588 -0.2641 0.0065  85  VAL A CA  
682  C C   . VAL A 85  ? 1.0069 0.7364 0.7141 -0.0632 -0.2624 -0.0019 85  VAL A C   
683  O O   . VAL A 85  ? 0.9563 0.6882 0.6632 -0.0672 -0.2605 -0.0057 85  VAL A O   
684  C CB  . VAL A 85  ? 0.9126 0.6362 0.6259 -0.0544 -0.2631 0.0091  85  VAL A CB  
685  C CG1 . VAL A 85  ? 0.9819 0.7100 0.7014 -0.0498 -0.2642 0.0170  85  VAL A CG1 
686  C CG2 . VAL A 85  ? 0.9988 0.7233 0.7119 -0.0572 -0.2615 0.0075  85  VAL A CG2 
687  N N   . THR A 86  ? 1.0081 0.7299 0.7122 -0.0626 -0.2627 -0.0050 86  THR A N   
688  C CA  . THR A 86  ? 0.9769 0.6910 0.6773 -0.0663 -0.2606 -0.0126 86  THR A CA  
689  C C   . THR A 86  ? 0.9971 0.6917 0.6942 -0.0619 -0.2594 -0.0134 86  THR A C   
690  O O   . THR A 86  ? 0.9602 0.6488 0.6578 -0.0565 -0.2604 -0.0088 86  THR A O   
691  C CB  . THR A 86  ? 0.8999 0.6230 0.5997 -0.0699 -0.2618 -0.0160 86  THR A CB  
692  O OG1 . THR A 86  ? 0.9718 0.6839 0.6685 -0.0722 -0.2594 -0.0229 86  THR A OG1 
693  C CG2 . THR A 86  ? 0.9045 0.6289 0.6045 -0.0655 -0.2648 -0.0109 86  THR A CG2 
694  N N   . ALA A 87  ? 0.9988 0.6847 0.6934 -0.0643 -0.2568 -0.0193 87  ALA A N   
695  C CA  . ALA A 87  ? 0.9598 0.6287 0.6512 -0.0601 -0.2552 -0.0197 87  ALA A CA  
696  C C   . ALA A 87  ? 0.9646 0.6290 0.6537 -0.0559 -0.2576 -0.0177 87  ALA A C   
697  O O   . ALA A 87  ? 1.0359 0.6886 0.7228 -0.0513 -0.2570 -0.0167 87  ALA A O   
698  C CB  . ALA A 87  ? 0.9780 0.6397 0.6683 -0.0637 -0.2514 -0.0259 87  ALA A CB  
699  N N   . ALA A 88  ? 0.8925 0.5668 0.5823 -0.0574 -0.2602 -0.0172 88  ALA A N   
700  C CA  . ALA A 88  ? 0.9172 0.5883 0.6056 -0.0535 -0.2625 -0.0150 88  ALA A CA  
701  C C   . ALA A 88  ? 0.9733 0.6473 0.6653 -0.0486 -0.2641 -0.0086 88  ALA A C   
702  O O   . ALA A 88  ? 0.9730 0.6425 0.6647 -0.0444 -0.2653 -0.0068 88  ALA A O   
703  C CB  . ALA A 88  ? 0.9402 0.6212 0.6284 -0.0570 -0.2644 -0.0169 88  ALA A CB  
704  N N   . ASP A 89  ? 0.9648 0.6459 0.6607 -0.0490 -0.2639 -0.0053 89  ASP A N   
705  C CA  . ASP A 89  ? 0.9154 0.5992 0.6163 -0.0446 -0.2646 0.0007  89  ASP A CA  
706  C C   . ASP A 89  ? 0.9197 0.5915 0.6203 -0.0405 -0.2630 0.0010  89  ASP A C   
707  O O   . ASP A 89  ? 0.9244 0.5962 0.6294 -0.0365 -0.2631 0.0049  89  ASP A O   
708  C CB  . ASP A 89  ? 0.9024 0.6010 0.6083 -0.0469 -0.2652 0.0047  89  ASP A CB  
709  C CG  . ASP A 89  ? 0.9242 0.6382 0.6318 -0.0498 -0.2670 0.0062  89  ASP A CG  
710  O OD1 . ASP A 89  ? 0.9317 0.6444 0.6377 -0.0490 -0.2683 0.0052  89  ASP A OD1 
711  O OD2 . ASP A 89  ? 0.9050 0.6333 0.6157 -0.0527 -0.2673 0.0083  89  ASP A OD2 
712  N N   . MET A 90  ? 0.9400 0.6027 0.6364 -0.0415 -0.2610 -0.0030 90  MET A N   
713  C CA  . MET A 90  ? 0.9563 0.6087 0.6519 -0.0375 -0.2594 -0.0030 90  MET A CA  
714  C C   . MET A 90  ? 0.9165 0.5620 0.6107 -0.0330 -0.2598 -0.0034 90  MET A C   
715  O O   . MET A 90  ? 0.9590 0.5994 0.6487 -0.0335 -0.2598 -0.0065 90  MET A O   
716  C CB  . MET A 90  ? 0.9585 0.6034 0.6503 -0.0393 -0.2569 -0.0066 90  MET A CB  
717  C CG  . MET A 90  ? 0.9586 0.5943 0.6494 -0.0350 -0.2551 -0.0064 90  MET A CG  
718  S SD  . MET A 90  ? 0.8965 0.5246 0.5844 -0.0366 -0.2515 -0.0091 90  MET A SD  
719  C CE  . MET A 90  ? 1.0723 0.6959 0.7562 -0.0391 -0.2507 -0.0133 90  MET A CE  
720  N N   . ALA A 91  ? 0.8807 0.5266 0.5793 -0.0290 -0.2599 -0.0005 91  ALA A N   
721  C CA  . ALA A 91  ? 0.8786 0.5197 0.5772 -0.0248 -0.2600 -0.0013 91  ALA A CA  
722  C C   . ALA A 91  ? 0.9230 0.5646 0.6279 -0.0209 -0.2589 0.0008  91  ALA A C   
723  O O   . ALA A 91  ? 0.9907 0.6368 0.7001 -0.0216 -0.2584 0.0034  91  ALA A O   
724  C CB  . ALA A 91  ? 0.8765 0.5225 0.5764 -0.0252 -0.2619 -0.0001 91  ALA A CB  
725  N N   . THR A 92  ? 0.8735 0.5109 0.5790 -0.0170 -0.2582 -0.0009 92  THR A N   
726  C CA  . THR A 92  ? 0.8790 0.5184 0.5924 -0.0135 -0.2568 0.0003  92  THR A CA  
727  C C   . THR A 92  ? 0.9011 0.5469 0.6219 -0.0130 -0.2574 0.0038  92  THR A C   
728  O O   . THR A 92  ? 0.8799 0.5258 0.5984 -0.0133 -0.2587 0.0036  92  THR A O   
729  C CB  . THR A 92  ? 0.9222 0.5558 0.6337 -0.0097 -0.2552 -0.0039 92  THR A CB  
730  O OG1 . THR A 92  ? 0.8728 0.5009 0.5765 -0.0101 -0.2547 -0.0064 92  THR A OG1 
731  C CG2 . THR A 92  ? 0.9671 0.6035 0.6874 -0.0068 -0.2531 -0.0040 92  THR A CG2 
732  N N   . TYR A 93  ? 0.8873 0.5388 0.6176 -0.0121 -0.2562 0.0074  93  TYR A N   
733  C CA  . TYR A 93  ? 0.8621 0.5211 0.6013 -0.0114 -0.2561 0.0123  93  TYR A CA  
734  C C   . TYR A 93  ? 0.8952 0.5540 0.6450 -0.0074 -0.2530 0.0122  93  TYR A C   
735  O O   . TYR A 93  ? 0.8780 0.5355 0.6313 -0.0064 -0.2511 0.0106  93  TYR A O   
736  C CB  . TYR A 93  ? 0.8603 0.5282 0.6032 -0.0141 -0.2568 0.0178  93  TYR A CB  
737  C CG  . TYR A 93  ? 0.8632 0.5348 0.5983 -0.0183 -0.2594 0.0180  93  TYR A CG  
738  C CD1 . TYR A 93  ? 0.8669 0.5342 0.5936 -0.0212 -0.2601 0.0144  93  TYR A CD1 
739  C CD2 . TYR A 93  ? 0.8620 0.5425 0.5993 -0.0194 -0.2608 0.0218  93  TYR A CD2 
740  C CE1 . TYR A 93  ? 0.8695 0.5408 0.5905 -0.0255 -0.2618 0.0136  93  TYR A CE1 
741  C CE2 . TYR A 93  ? 0.8644 0.5500 0.5953 -0.0237 -0.2630 0.0211  93  TYR A CE2 
742  C CZ  . TYR A 93  ? 0.8682 0.5490 0.5912 -0.0269 -0.2633 0.0166  93  TYR A CZ  
743  O OH  . TYR A 93  ? 0.8705 0.5570 0.5885 -0.0315 -0.2647 0.0150  93  TYR A OH  
744  N N   . TYR A 94  ? 0.8762 0.5367 0.6316 -0.0053 -0.2523 0.0136  94  TYR A N   
745  C CA  . TYR A 94  ? 0.8925 0.5532 0.6597 -0.0017 -0.2486 0.0131  94  TYR A CA  
746  C C   . TYR A 94  ? 0.9007 0.5697 0.6799 -0.0008 -0.2473 0.0204  94  TYR A C   
747  O O   . TYR A 94  ? 0.8486 0.5226 0.6252 -0.0023 -0.2497 0.0247  94  TYR A O   
748  C CB  . TYR A 94  ? 0.8833 0.5375 0.6473 0.0008  -0.2479 0.0074  94  TYR A CB  
749  C CG  . TYR A 94  ? 0.8575 0.5044 0.6091 0.0004  -0.2491 0.0010  94  TYR A CG  
750  C CD1 . TYR A 94  ? 0.9390 0.5843 0.6910 0.0012  -0.2473 -0.0029 94  TYR A CD1 
751  C CD2 . TYR A 94  ? 0.8559 0.4983 0.5962 -0.0007 -0.2518 -0.0010 94  TYR A CD2 
752  C CE1 . TYR A 94  ? 0.9616 0.6017 0.7029 0.0013  -0.2481 -0.0077 94  TYR A CE1 
753  C CE2 . TYR A 94  ? 0.9358 0.5718 0.6657 -0.0008 -0.2524 -0.0060 94  TYR A CE2 
754  C CZ  . TYR A 94  ? 0.9257 0.5609 0.6562 0.0004  -0.2505 -0.0090 94  TYR A CZ  
755  O OH  . TYR A 94  ? 0.9382 0.5684 0.6591 0.0008  -0.2507 -0.0129 94  TYR A OH  
756  N N   . CYS A 95  ? 0.9418 0.6132 0.7350 0.0016  -0.2432 0.0218  95  CYS A N   
757  C CA  . CYS A 95  ? 0.8809 0.5593 0.6880 0.0036  -0.2406 0.0286  95  CYS A CA  
758  C C   . CYS A 95  ? 0.8908 0.5651 0.7060 0.0072  -0.2368 0.0245  95  CYS A C   
759  O O   . CYS A 95  ? 0.9332 0.6025 0.7497 0.0082  -0.2345 0.0176  95  CYS A O   
760  C CB  . CYS A 95  ? 0.8940 0.5793 0.7137 0.0036  -0.2379 0.0345  95  CYS A CB  
761  S SG  . CYS A 95  ? 1.1003 0.7821 0.9179 0.0019  -0.2375 0.0299  95  CYS A SG  
762  N N   . ALA A 96  ? 0.8381 0.5155 0.6590 0.0090  -0.2361 0.0287  96  ALA A N   
763  C CA  . ALA A 96  ? 0.8359 0.5097 0.6649 0.0124  -0.2323 0.0250  96  ALA A CA  
764  C C   . ALA A 96  ? 0.8328 0.5139 0.6803 0.0151  -0.2278 0.0329  96  ALA A C   
765  O O   . ALA A 96  ? 0.8441 0.5337 0.6950 0.0145  -0.2288 0.0420  96  ALA A O   
766  C CB  . ALA A 96  ? 0.8376 0.5059 0.6539 0.0124  -0.2356 0.0210  96  ALA A CB  
767  N N   . ARG A 97  ? 0.8304 0.5087 0.6905 0.0182  -0.2223 0.0293  97  ARG A N   
768  C CA  . ARG A 97  ? 0.8274 0.5113 0.7072 0.0214  -0.2167 0.0360  97  ARG A CA  
769  C C   . ARG A 97  ? 0.8270 0.5077 0.7061 0.0238  -0.2164 0.0342  97  ARG A C   
770  O O   . ARG A 97  ? 0.8268 0.5001 0.7034 0.0247  -0.2149 0.0248  97  ARG A O   
771  C CB  . ARG A 97  ? 0.8478 0.5313 0.7455 0.0229  -0.2095 0.0327  97  ARG A CB  
772  C CG  . ARG A 97  ? 0.8789 0.5650 0.7982 0.0268  -0.2021 0.0358  97  ARG A CG  
773  C CD  . ARG A 97  ? 0.9003 0.5854 0.8366 0.0275  -0.1947 0.0300  97  ARG A CD  
774  N NE  . ARG A 97  ? 0.9136 0.5952 0.8616 0.0303  -0.1887 0.0233  97  ARG A NE  
775  C CZ  . ARG A 97  ? 0.9745 0.6560 0.9394 0.0311  -0.1812 0.0167  97  ARG A CZ  
776  N NH1 . ARG A 97  ? 0.9774 0.6618 0.9496 0.0293  -0.1790 0.0158  97  ARG A NH1 
777  N NH2 . ARG A 97  ? 1.0487 0.7275 1.0236 0.0334  -0.1757 0.0102  97  ARG A NH2 
778  N N   . TRP A 98  ? 0.8268 0.5139 0.7079 0.0248  -0.2177 0.0432  98  TRP A N   
779  C CA  . TRP A 98  ? 0.8260 0.5110 0.7087 0.0274  -0.2169 0.0426  98  TRP A CA  
780  C C   . TRP A 98  ? 0.8229 0.5080 0.7279 0.0314  -0.2084 0.0430  98  TRP A C   
781  O O   . TRP A 98  ? 0.8211 0.5115 0.7430 0.0325  -0.2031 0.0481  98  TRP A O   
782  C CB  . TRP A 98  ? 0.8264 0.5202 0.7057 0.0273  -0.2207 0.0524  98  TRP A CB  
783  C CG  . TRP A 98  ? 0.8293 0.5211 0.6866 0.0237  -0.2285 0.0493  98  TRP A CG  
784  C CD1 . TRP A 98  ? 0.8314 0.5280 0.6776 0.0198  -0.2335 0.0516  98  TRP A CD1 
785  C CD2 . TRP A 98  ? 0.8329 0.5173 0.6777 0.0234  -0.2318 0.0428  98  TRP A CD2 
786  N NE1 . TRP A 98  ? 0.8339 0.5266 0.6621 0.0171  -0.2393 0.0469  98  TRP A NE1 
787  C CE2 . TRP A 98  ? 0.8334 0.5184 0.6602 0.0193  -0.2385 0.0417  98  TRP A CE2 
788  C CE3 . TRP A 98  ? 0.8295 0.5068 0.6768 0.0263  -0.2294 0.0376  98  TRP A CE3 
789  C CZ2 . TRP A 98  ? 0.8444 0.5232 0.6564 0.0179  -0.2428 0.0359  98  TRP A CZ2 
790  C CZ3 . TRP A 98  ? 0.8313 0.5023 0.6627 0.0250  -0.2341 0.0320  98  TRP A CZ3 
791  C CH2 . TRP A 98  ? 0.8474 0.5191 0.6616 0.0208  -0.2407 0.0314  98  TRP A CH2 
792  N N   . ARG A 99  ? 0.8222 0.5015 0.7280 0.0336  -0.2066 0.0374  99  ARG A N   
793  C CA  . ARG A 99  ? 0.8194 0.4989 0.7468 0.0376  -0.1982 0.0378  99  ARG A CA  
794  C C   . ARG A 99  ? 0.8190 0.5012 0.7478 0.0402  -0.1989 0.0444  99  ARG A C   
795  O O   . ARG A 99  ? 0.8205 0.4978 0.7331 0.0393  -0.2042 0.0400  99  ARG A O   
796  C CB  . ARG A 99  ? 0.8187 0.4894 0.7474 0.0381  -0.1944 0.0242  99  ARG A CB  
797  C CG  . ARG A 99  ? 0.8873 0.5591 0.8304 0.0377  -0.1882 0.0200  99  ARG A CG  
798  C CD  . ARG A 99  ? 0.9651 0.6335 0.9238 0.0400  -0.1801 0.0107  99  ARG A CD  
799  N NE  . ARG A 99  ? 0.9745 0.6460 0.9510 0.0396  -0.1731 0.0081  99  ARG A NE  
800  C CZ  . ARG A 99  ? 0.9775 0.6482 0.9713 0.0410  -0.1647 -0.0005 99  ARG A CZ  
801  N NH1 . ARG A 99  ? 0.9596 0.6263 0.9555 0.0430  -0.1618 -0.0074 99  ARG A NH1 
802  N NH2 . ARG A 99  ? 0.9569 0.6313 0.9664 0.0400  -0.1588 -0.0029 99  ARG A NH2 
803  N N   . LEU A 100 ? 0.8170 0.5075 0.7653 0.0433  -0.1937 0.0553  100 LEU A N   
804  C CA  . LEU A 100 ? 0.8165 0.5124 0.7667 0.0458  -0.1947 0.0637  100 LEU A CA  
805  C C   . LEU A 100 ? 0.8138 0.5105 0.7889 0.0508  -0.1851 0.0668  100 LEU A C   
806  O O   . LEU A 100 ? 0.8122 0.5100 0.8068 0.0523  -0.1774 0.0675  100 LEU A O   
807  C CB  . LEU A 100 ? 0.8169 0.5262 0.7652 0.0449  -0.1987 0.0770  100 LEU A CB  
808  C CG  . LEU A 100 ? 0.8195 0.5297 0.7469 0.0398  -0.2068 0.0748  100 LEU A CG  
809  C CD1 . LEU A 100 ? 0.8193 0.5323 0.7542 0.0385  -0.2042 0.0767  100 LEU A CD1 
810  C CD2 . LEU A 100 ? 0.8529 0.5740 0.7698 0.0384  -0.2132 0.0832  100 LEU A CD2 
811  N N   . MET A 101 ? 0.8134 0.5094 0.7883 0.0533  -0.1854 0.0684  101 MET A N   
812  C CA  . MET A 101 ? 0.8110 0.5077 0.8093 0.0583  -0.1763 0.0717  101 MET A CA  
813  C C   . MET A 101 ? 0.8105 0.5161 0.8102 0.0610  -0.1783 0.0837  101 MET A C   
814  O O   . MET A 101 ? 0.8147 0.5195 0.7945 0.0592  -0.1864 0.0821  101 MET A O   
815  C CB  . MET A 101 ? 0.8107 0.4948 0.8088 0.0590  -0.1729 0.0572  101 MET A CB  
816  C CG  . MET A 101 ? 0.8225 0.5062 0.8462 0.0639  -0.1624 0.0586  101 MET A CG  
817  S SD  . MET A 101 ? 0.8949 0.5669 0.9244 0.0633  -0.1558 0.0398  101 MET A SD  
818  C CE  . MET A 101 ? 0.8246 0.4994 0.8586 0.0600  -0.1541 0.0378  101 MET A CE  
819  N N   . MET A 102 ? 0.8570 0.5717 0.8809 0.0655  -0.1707 0.0957  102 MET A N   
820  C CA  . MET A 102 ? 0.8553 0.5822 0.8829 0.0684  -0.1720 0.1097  102 MET A CA  
821  C C   . MET A 102 ? 0.8529 0.5760 0.8937 0.0731  -0.1662 0.1094  102 MET A C   
822  O O   . MET A 102 ? 0.8479 0.5697 0.9137 0.0770  -0.1556 0.1112  102 MET A O   
823  C CB  . MET A 102 ? 0.8468 0.5892 0.8922 0.0706  -0.1678 0.1256  102 MET A CB  
824  C CG  . MET A 102 ? 0.9174 0.6750 0.9671 0.0738  -0.1691 0.1405  102 MET A CG  
825  S SD  . MET A 102 ? 1.0251 0.7986 1.0542 0.0696  -0.1800 0.1486  102 MET A SD  
826  C CE  . MET A 102 ? 1.0358 0.8239 1.0679 0.0735  -0.1816 0.1609  102 MET A CE  
827  N N   . VAL A 103 ? 0.9206 0.6416 0.9451 0.0726  -0.1727 0.1070  103 VAL A N   
828  C CA  . VAL A 103 ? 0.9826 0.7020 1.0176 0.0772  -0.1685 0.1089  103 VAL A CA  
829  C C   . VAL A 103 ? 1.1860 0.9176 1.2110 0.0776  -0.1755 0.1195  103 VAL A C   
830  O O   . VAL A 103 ? 1.2206 0.9471 1.2257 0.0754  -0.1830 0.1129  103 VAL A O   
831  C CB  . VAL A 103 ? 0.8959 0.5982 0.9213 0.0762  -0.1687 0.0919  103 VAL A CB  
832  C CG1 . VAL A 103 ? 0.8433 0.5432 0.8854 0.0815  -0.1616 0.0934  103 VAL A CG1 
833  C CG2 . VAL A 103 ? 0.8958 0.5884 0.9252 0.0742  -0.1641 0.0797  103 VAL A CG2 
834  N N   . ASP A 104 ? 1.4076 1.1564 1.4465 0.0803  -0.1731 0.1361  104 ASP A N   
835  C CA  . ASP A 104 ? 1.4037 1.1690 1.4360 0.0809  -0.1791 0.1480  104 ASP A CA  
836  C C   . ASP A 104 ? 1.4389 1.2086 1.4446 0.0745  -0.1905 0.1447  104 ASP A C   
837  O O   . ASP A 104 ? 1.5364 1.3222 1.5356 0.0738  -0.1959 0.1539  104 ASP A O   
838  C CB  . ASP A 104 ? 1.4221 1.1843 1.4532 0.0837  -0.1796 0.1470  104 ASP A CB  
839  C CG  . ASP A 104 ? 1.5921 1.3727 1.6410 0.0892  -0.1758 0.1649  104 ASP A CG  
840  O OD1 . ASP A 104 ? 1.5802 1.3746 1.6462 0.0917  -0.1708 0.1779  104 ASP A OD1 
841  O OD2 . ASP A 104 ? 1.6688 1.4504 1.7150 0.0913  -0.1777 0.1661  104 ASP A OD2 
842  N N   . GLU A 105 ? 1.2342 0.9906 1.2252 0.0698  -0.1938 0.1314  105 GLU A N   
843  C CA  . GLU A 105 ? 1.0416 0.8008 1.0097 0.0636  -0.2032 0.1276  105 GLU A CA  
844  C C   . GLU A 105 ? 0.9955 0.7421 0.9595 0.0606  -0.2021 0.1170  105 GLU A C   
845  O O   . GLU A 105 ? 1.0683 0.8003 1.0372 0.0618  -0.1974 0.1072  105 GLU A O   
846  C CB  . GLU A 105 ? 1.0510 0.8051 0.9962 0.0603  -0.2119 0.1195  105 GLU A CB  
847  C CG  . GLU A 105 ? 1.1674 0.9236 1.0897 0.0537  -0.2210 0.1145  105 GLU A CG  
848  C CD  . GLU A 105 ? 1.2307 0.9711 1.1315 0.0499  -0.2269 0.0998  105 GLU A CD  
849  O OE1 . GLU A 105 ? 1.2840 1.0156 1.1849 0.0522  -0.2258 0.0953  105 GLU A OE1 
850  O OE2 . GLU A 105 ? 1.1935 0.9303 1.0776 0.0447  -0.2324 0.0931  105 GLU A OE2 
851  N N   . VAL A 106 ? 0.8276 0.5808 0.7833 0.0568  -0.2061 0.1190  106 VAL A N   
852  C CA  . VAL A 106 ? 0.8138 0.5559 0.7648 0.0538  -0.2056 0.1093  106 VAL A CA  
853  C C   . VAL A 106 ? 0.8528 0.5794 0.7820 0.0501  -0.2113 0.0941  106 VAL A C   
854  O O   . VAL A 106 ? 0.9540 0.6820 0.8633 0.0458  -0.2194 0.0912  106 VAL A O   
855  C CB  . VAL A 106 ? 0.8146 0.5673 0.7615 0.0505  -0.2086 0.1149  106 VAL A CB  
856  C CG1 . VAL A 106 ? 0.8158 0.5571 0.7610 0.0482  -0.2069 0.1057  106 VAL A CG1 
857  C CG2 . VAL A 106 ? 0.8125 0.5827 0.7800 0.0543  -0.2034 0.1313  106 VAL A CG2 
858  N N   . THR A 107 ? 0.8156 0.5284 0.7495 0.0519  -0.2068 0.0844  107 THR A N   
859  C CA  . THR A 107 ? 0.8175 0.5158 0.7328 0.0489  -0.2110 0.0699  107 THR A CA  
860  C C   . THR A 107 ? 0.8188 0.5113 0.7301 0.0460  -0.2107 0.0627  107 THR A C   
861  O O   . THR A 107 ? 0.8175 0.5131 0.7450 0.0474  -0.2046 0.0660  107 THR A O   
862  C CB  . THR A 107 ? 0.8165 0.5041 0.7381 0.0522  -0.2063 0.0623  107 THR A CB  
863  O OG1 . THR A 107 ? 0.9079 0.5937 0.8515 0.0553  -0.1967 0.0616  107 THR A OG1 
864  C CG2 . THR A 107 ? 0.8152 0.5083 0.7410 0.0553  -0.2066 0.0695  107 THR A CG2 
865  N N   . ARG A 108 ? 0.8212 0.5057 0.7113 0.0420  -0.2169 0.0531  108 ARG A N   
866  C CA  . ARG A 108 ? 0.8227 0.5027 0.7061 0.0389  -0.2178 0.0467  108 ARG A CA  
867  C C   . ARG A 108 ? 0.8230 0.4901 0.7025 0.0392  -0.2157 0.0333  108 ARG A C   
868  O O   . ARG A 108 ? 0.8241 0.4840 0.6906 0.0388  -0.2191 0.0266  108 ARG A O   
869  C CB  . ARG A 108 ? 0.8254 0.5078 0.6885 0.0341  -0.2262 0.0469  108 ARG A CB  
870  C CG  . ARG A 108 ? 0.8252 0.5201 0.6865 0.0335  -0.2301 0.0573  108 ARG A CG  
871  C CD  . ARG A 108 ? 0.9054 0.6033 0.7482 0.0282  -0.2375 0.0562  108 ARG A CD  
872  N NE  . ARG A 108 ? 0.9001 0.6031 0.7455 0.0263  -0.2370 0.0593  108 ARG A NE  
873  C CZ  . ARG A 108 ? 0.8709 0.5884 0.7213 0.0255  -0.2378 0.0694  108 ARG A CZ  
874  N NH1 . ARG A 108 ? 0.8350 0.5648 0.6887 0.0265  -0.2391 0.0778  108 ARG A NH1 
875  N NH2 . ARG A 108 ? 0.8430 0.5638 0.6952 0.0237  -0.2372 0.0712  108 ARG A NH2 
876  N N   . HIS A 109 ? 0.8220 0.4872 0.7129 0.0399  -0.2100 0.0293  109 HIS A N   
877  C CA  . HIS A 109 ? 0.8218 0.4778 0.7117 0.0402  -0.2069 0.0165  109 HIS A CA  
878  C C   . HIS A 109 ? 0.8239 0.4762 0.6993 0.0367  -0.2106 0.0093  109 HIS A C   
879  O O   . HIS A 109 ? 0.8232 0.4718 0.7022 0.0369  -0.2067 0.0002  109 HIS A O   
880  C CB  . HIS A 109 ? 0.8189 0.4763 0.7335 0.0435  -0.1970 0.0156  109 HIS A CB  
881  C CG  . HIS A 109 ? 0.8170 0.4739 0.7447 0.0474  -0.1921 0.0173  109 HIS A CG  
882  N ND1 . HIS A 109 ? 0.8177 0.4742 0.7362 0.0483  -0.1967 0.0213  109 HIS A ND1 
883  C CD2 . HIS A 109 ? 0.8145 0.4713 0.7646 0.0508  -0.1827 0.0156  109 HIS A CD2 
884  C CE1 . HIS A 109 ? 0.8157 0.4717 0.7498 0.0522  -0.1905 0.0223  109 HIS A CE1 
885  N NE2 . HIS A 109 ? 0.8138 0.4699 0.7676 0.0538  -0.1817 0.0188  109 HIS A NE2 
886  N N   . GLY A 110 ? 0.8263 0.4805 0.6864 0.0334  -0.2175 0.0131  110 GLY A N   
887  C CA  . GLY A 110 ? 0.8286 0.4787 0.6738 0.0302  -0.2213 0.0066  110 GLY A CA  
888  C C   . GLY A 110 ? 0.8283 0.4835 0.6802 0.0287  -0.2197 0.0098  110 GLY A C   
889  O O   . GLY A 110 ? 0.8260 0.4868 0.6961 0.0304  -0.2144 0.0151  110 GLY A O   
890  N N   . MET A 111 ? 0.8308 0.4838 0.6678 0.0255  -0.2243 0.0066  111 MET A N   
891  C CA  . MET A 111 ? 0.8492 0.5060 0.6894 0.0237  -0.2237 0.0086  111 MET A CA  
892  C C   . MET A 111 ? 0.8928 0.5462 0.7373 0.0244  -0.2196 -0.0008 111 MET A C   
893  O O   . MET A 111 ? 0.8839 0.5327 0.7150 0.0230  -0.2222 -0.0081 111 MET A O   
894  C CB  . MET A 111 ? 0.8352 0.4919 0.6579 0.0199  -0.2304 0.0103  111 MET A CB  
895  C CG  . MET A 111 ? 0.8410 0.5009 0.6561 0.0187  -0.2351 0.0165  111 MET A CG  
896  S SD  . MET A 111 ? 0.8390 0.5014 0.6384 0.0138  -0.2414 0.0189  111 MET A SD  
897  C CE  . MET A 111 ? 0.8412 0.5006 0.6252 0.0122  -0.2468 0.0172  111 MET A CE  
898  N N   . ASP A 112 ? 1.0183 0.6749 0.8827 0.0265  -0.2126 -0.0008 112 ASP A N   
899  C CA  . ASP A 112 ? 1.0151 0.6702 0.8859 0.0272  -0.2078 -0.0109 112 ASP A CA  
900  C C   . ASP A 112 ? 1.0182 0.6749 0.8840 0.0246  -0.2093 -0.0134 112 ASP A C   
901  O O   . ASP A 112 ? 1.0958 0.7507 0.9553 0.0242  -0.2090 -0.0226 112 ASP A O   
902  C CB  . ASP A 112 ? 1.0136 0.6723 0.9090 0.0298  -0.1992 -0.0106 112 ASP A CB  
903  C CG  . ASP A 112 ? 1.0197 0.6847 0.9293 0.0298  -0.1969 0.0000  112 ASP A CG  
904  O OD1 . ASP A 112 ? 1.0259 0.6931 0.9256 0.0276  -0.2023 0.0070  112 ASP A OD1 
905  O OD2 . ASP A 112 ? 1.0181 0.6864 0.9495 0.0318  -0.1893 0.0012  112 ASP A OD2 
906  N N   . VAL A 113 ? 0.9009 0.5617 0.7693 0.0230  -0.2107 -0.0053 113 VAL A N   
907  C CA  . VAL A 113 ? 0.8778 0.5403 0.7427 0.0207  -0.2118 -0.0069 113 VAL A CA  
908  C C   . VAL A 113 ? 0.8457 0.5072 0.6931 0.0180  -0.2190 -0.0017 113 VAL A C   
909  O O   . VAL A 113 ? 0.8917 0.5557 0.7382 0.0176  -0.2214 0.0067  113 VAL A O   
910  C CB  . VAL A 113 ? 0.8662 0.5347 0.7509 0.0209  -0.2064 -0.0027 113 VAL A CB  
911  C CG1 . VAL A 113 ? 0.9234 0.5936 0.8029 0.0182  -0.2085 -0.0031 113 VAL A CG1 
912  C CG2 . VAL A 113 ? 0.8958 0.5654 0.7989 0.0230  -0.1984 -0.0096 113 VAL A CG2 
913  N N   . TRP A 114 ? 0.8326 0.4914 0.6668 0.0162  -0.2221 -0.0070 114 TRP A N   
914  C CA  . TRP A 114 ? 0.8360 0.4937 0.6548 0.0133  -0.2280 -0.0035 114 TRP A CA  
915  C C   . TRP A 114 ? 0.8714 0.5317 0.6921 0.0116  -0.2275 -0.0037 114 TRP A C   
916  O O   . TRP A 114 ? 0.9169 0.5799 0.7496 0.0126  -0.2230 -0.0073 114 TRP A O   
917  C CB  . TRP A 114 ? 0.8390 0.4904 0.6400 0.0129  -0.2319 -0.0089 114 TRP A CB  
918  C CG  . TRP A 114 ? 0.8396 0.4882 0.6361 0.0137  -0.2337 -0.0076 114 TRP A CG  
919  C CD1 . TRP A 114 ? 0.8374 0.4850 0.6417 0.0165  -0.2305 -0.0100 114 TRP A CD1 
920  C CD2 . TRP A 114 ? 0.8425 0.4892 0.6261 0.0117  -0.2388 -0.0041 114 TRP A CD2 
921  N NE1 . TRP A 114 ? 0.8387 0.4838 0.6354 0.0164  -0.2337 -0.0077 114 TRP A NE1 
922  C CE2 . TRP A 114 ? 0.8418 0.4866 0.6258 0.0134  -0.2388 -0.0042 114 TRP A CE2 
923  C CE3 . TRP A 114 ? 0.8457 0.4924 0.6181 0.0084  -0.2431 -0.0012 114 TRP A CE3 
924  C CZ2 . TRP A 114 ? 0.8439 0.4874 0.6174 0.0118  -0.2432 -0.0017 114 TRP A CZ2 
925  C CZ3 . TRP A 114 ? 0.8478 0.4935 0.6106 0.0067  -0.2470 0.0009  114 TRP A CZ3 
926  C CH2 . TRP A 114 ? 0.8468 0.4911 0.6101 0.0083  -0.2472 0.0006  114 TRP A CH2 
927  N N   . SER A 115 ? 0.9362 0.5961 0.7454 0.0090  -0.2320 -0.0003 115 SER A N   
928  C CA  . SER A 115 ? 0.9886 0.6508 0.7986 0.0072  -0.2320 0.0003  115 SER A CA  
929  C C   . SER A 115 ? 1.0423 0.7006 0.8391 0.0065  -0.2341 -0.0059 115 SER A C   
930  O O   . SER A 115 ? 1.0197 0.6736 0.8060 0.0071  -0.2358 -0.0099 115 SER A O   
931  C CB  . SER A 115 ? 1.0111 0.6768 0.8191 0.0048  -0.2349 0.0086  115 SER A CB  
932  O OG  . SER A 115 ? 1.0659 0.7342 0.8772 0.0034  -0.2344 0.0096  115 SER A OG  
933  N N   . GLN A 116 ? 1.2530 0.9136 1.0510 0.0052  -0.2338 -0.0062 116 GLN A N   
934  C CA  . GLN A 116 ? 1.2418 0.9002 1.0287 0.0047  -0.2354 -0.0109 116 GLN A CA  
935  C C   . GLN A 116 ? 1.2805 0.9339 1.0516 0.0030  -0.2399 -0.0089 116 GLN A C   
936  O O   . GLN A 116 ? 1.3315 0.9813 1.0926 0.0037  -0.2408 -0.0131 116 GLN A O   
937  C CB  . GLN A 116 ? 1.2589 0.9210 1.0506 0.0034  -0.2345 -0.0103 116 GLN A CB  
938  C CG  . GLN A 116 ? 1.3384 1.0029 1.1348 0.0014  -0.2356 -0.0026 116 GLN A CG  
939  C CD  . GLN A 116 ? 1.4726 1.1399 1.2718 -0.0001 -0.2352 -0.0020 116 GLN A CD  
940  O OE1 . GLN A 116 ? 1.5527 1.2183 1.3427 -0.0008 -0.2369 -0.0045 116 GLN A OE1 
941  N NE2 . GLN A 116 ? 1.3303 1.0021 1.1429 -0.0005 -0.2329 0.0018  116 GLN A NE2 
942  N N   . GLY A 117 ? 1.1530 0.8071 0.9226 0.0008  -0.2422 -0.0027 117 GLY A N   
943  C CA  . GLY A 117 ? 1.0565 0.7072 0.8130 -0.0016 -0.2459 -0.0012 117 GLY A CA  
944  C C   . GLY A 117 ? 1.0589 0.7110 0.8130 -0.0041 -0.2471 0.0015  117 GLY A C   
945  O O   . GLY A 117 ? 1.0570 0.7105 0.8146 -0.0037 -0.2456 0.0000  117 GLY A O   
946  N N   . THR A 118 ? 0.9589 0.6116 0.7075 -0.0070 -0.2497 0.0052  118 THR A N   
947  C CA  . THR A 118 ? 0.9076 0.5619 0.6534 -0.0098 -0.2508 0.0075  118 THR A CA  
948  C C   . THR A 118 ? 1.0350 0.6858 0.7693 -0.0125 -0.2530 0.0067  118 THR A C   
949  O O   . THR A 118 ? 1.0305 0.6838 0.7631 -0.0143 -0.2546 0.0088  118 THR A O   
950  C CB  . THR A 118 ? 0.8805 0.5422 0.6350 -0.0112 -0.2507 0.0134  118 THR A CB  
951  O OG1 . THR A 118 ? 0.9690 0.6334 0.7355 -0.0089 -0.2478 0.0139  118 THR A OG1 
952  C CG2 . THR A 118 ? 0.9171 0.5805 0.6673 -0.0144 -0.2521 0.0154  118 THR A CG2 
953  N N   . MET A 119 ? 1.0871 0.7330 0.8143 -0.0127 -0.2528 0.0037  119 MET A N   
954  C CA  . MET A 119 ? 0.9962 0.6384 0.7141 -0.0154 -0.2541 0.0027  119 MET A CA  
955  C C   . MET A 119 ? 0.9741 0.6210 0.6925 -0.0194 -0.2551 0.0058  119 MET A C   
956  O O   . MET A 119 ? 0.9872 0.6367 0.7091 -0.0198 -0.2546 0.0075  119 MET A O   
957  C CB  . MET A 119 ? 1.0229 0.6593 0.7349 -0.0142 -0.2528 -0.0003 119 MET A CB  
958  C CG  . MET A 119 ? 1.0390 0.6713 0.7480 -0.0108 -0.2519 -0.0038 119 MET A CG  
959  S SD  . MET A 119 ? 1.2398 0.8692 0.9447 -0.0083 -0.2498 -0.0060 119 MET A SD  
960  C CE  . MET A 119 ? 1.0160 0.6415 0.7155 -0.0052 -0.2493 -0.0095 119 MET A CE  
961  N N   . VAL A 120 ? 0.9630 0.6119 0.6778 -0.0223 -0.2565 0.0061  120 VAL A N   
962  C CA  . VAL A 120 ? 0.9510 0.6063 0.6660 -0.0265 -0.2574 0.0082  120 VAL A CA  
963  C C   . VAL A 120 ? 0.9528 0.6039 0.6603 -0.0297 -0.2571 0.0047  120 VAL A C   
964  O O   . VAL A 120 ? 0.8824 0.5315 0.5859 -0.0305 -0.2576 0.0024  120 VAL A O   
965  C CB  . VAL A 120 ? 0.8957 0.5605 0.6151 -0.0277 -0.2589 0.0119  120 VAL A CB  
966  C CG1 . VAL A 120 ? 0.9655 0.6382 0.6833 -0.0325 -0.2597 0.0127  120 VAL A CG1 
967  C CG2 . VAL A 120 ? 0.8712 0.5409 0.6002 -0.0248 -0.2582 0.0163  120 VAL A CG2 
968  N N   . THR A 121 ? 1.0482 0.6980 0.7543 -0.0316 -0.2559 0.0040  121 THR A N   
969  C CA  . THR A 121 ? 1.1129 0.7582 0.8137 -0.0345 -0.2545 0.0005  121 THR A CA  
970  C C   . THR A 121 ? 1.0866 0.7399 0.7882 -0.0397 -0.2548 0.0003  121 THR A C   
971  O O   . THR A 121 ? 1.0807 0.7401 0.7857 -0.0407 -0.2552 0.0029  121 THR A O   
972  C CB  . THR A 121 ? 1.0601 0.6983 0.7594 -0.0326 -0.2523 -0.0003 121 THR A CB  
973  O OG1 . THR A 121 ? 1.0743 0.7088 0.7743 -0.0277 -0.2522 0.0002  121 THR A OG1 
974  C CG2 . THR A 121 ? 1.0582 0.6900 0.7531 -0.0345 -0.2500 -0.0036 121 THR A CG2 
975  N N   . VAL A 122 ? 1.0484 0.7023 0.7470 -0.0431 -0.2545 -0.0030 122 VAL A N   
976  C CA  . VAL A 122 ? 1.0452 0.7078 0.7446 -0.0487 -0.2542 -0.0047 122 VAL A CA  
977  C C   . VAL A 122 ? 1.0163 0.6721 0.7136 -0.0511 -0.2509 -0.0089 122 VAL A C   
978  O O   . VAL A 122 ? 0.9607 0.6097 0.6555 -0.0517 -0.2491 -0.0123 122 VAL A O   
979  C CB  . VAL A 122 ? 0.9754 0.6455 0.6742 -0.0515 -0.2558 -0.0061 122 VAL A CB  
980  C CG1 . VAL A 122 ? 0.9386 0.6212 0.6391 -0.0573 -0.2556 -0.0080 122 VAL A CG1 
981  C CG2 . VAL A 122 ? 0.9772 0.6522 0.6785 -0.0481 -0.2586 -0.0015 122 VAL A CG2 
982  N N   . SER A 123 ? 0.9983 0.6560 0.6975 -0.0525 -0.2496 -0.0084 123 SER A N   
983  C CA  . SER A 123 ? 0.9669 0.6181 0.6656 -0.0544 -0.2458 -0.0118 123 SER A CA  
984  C C   . SER A 123 ? 0.9592 0.6164 0.6604 -0.0572 -0.2451 -0.0115 123 SER A C   
985  O O   . SER A 123 ? 0.9469 0.6106 0.6499 -0.0561 -0.2475 -0.0077 123 SER A O   
986  C CB  . SER A 123 ? 1.0205 0.6594 0.7175 -0.0495 -0.2441 -0.0106 123 SER A CB  
987  O OG  . SER A 123 ? 1.0005 0.6340 0.6983 -0.0508 -0.2400 -0.0126 123 SER A OG  
988  N N   . SER A 124 ? 0.9897 0.6448 0.6917 -0.0608 -0.2414 -0.0158 124 SER A N   
989  C CA  . SER A 124 ? 0.9919 0.6517 0.6962 -0.0636 -0.2400 -0.0164 124 SER A CA  
990  C C   . SER A 124 ? 0.9953 0.6455 0.6998 -0.0601 -0.2381 -0.0143 124 SER A C   
991  O O   . SER A 124 ? 0.9790 0.6317 0.6853 -0.0620 -0.2369 -0.0146 124 SER A O   
992  C CB  . SER A 124 ? 0.9245 0.5887 0.6309 -0.0699 -0.2364 -0.0230 124 SER A CB  
993  O OG  . SER A 124 ? 0.9872 0.6403 0.6940 -0.0698 -0.2320 -0.0263 124 SER A OG  
994  N N   . ALA A 125 ? 0.9802 0.6207 0.6829 -0.0551 -0.2378 -0.0121 125 ALA A N   
995  C CA  . ALA A 125 ? 0.9816 0.6145 0.6847 -0.0516 -0.2359 -0.0099 125 ALA A CA  
996  C C   . ALA A 125 ? 1.0093 0.6463 0.7133 -0.0493 -0.2390 -0.0058 125 ALA A C   
997  O O   . ALA A 125 ? 1.1154 0.7578 0.8195 -0.0482 -0.2426 -0.0035 125 ALA A O   
998  C CB  . ALA A 125 ? 1.0278 0.6519 0.7290 -0.0468 -0.2348 -0.0086 125 ALA A CB  
999  N N   . SER A 126 ? 1.0163 0.6504 0.7214 -0.0487 -0.2373 -0.0049 126 SER A N   
1000 C CA  . SER A 126 ? 1.0678 0.7050 0.7743 -0.0466 -0.2397 -0.0014 126 SER A CA  
1001 C C   . SER A 126 ? 1.1143 0.7471 0.8203 -0.0409 -0.2407 0.0015  126 SER A C   
1002 O O   . SER A 126 ? 1.1230 0.7496 0.8274 -0.0382 -0.2387 0.0011  126 SER A O   
1003 C CB  . SER A 126 ? 1.1184 0.7546 0.8263 -0.0483 -0.2375 -0.0018 126 SER A CB  
1004 O OG  . SER A 126 ? 1.1710 0.8108 0.8803 -0.0469 -0.2401 0.0014  126 SER A OG  
1005 N N   . THR A 127 ? 1.2294 0.8665 0.9374 -0.0392 -0.2435 0.0043  127 THR A N   
1006 C CA  . THR A 127 ? 1.1804 0.8156 0.8892 -0.0342 -0.2443 0.0061  127 THR A CA  
1007 C C   . THR A 127 ? 1.1350 0.7658 0.8436 -0.0318 -0.2421 0.0067  127 THR A C   
1008 O O   . THR A 127 ? 1.1522 0.7837 0.8621 -0.0333 -0.2416 0.0073  127 THR A O   
1009 C CB  . THR A 127 ? 1.1468 0.7882 0.8597 -0.0335 -0.2471 0.0085  127 THR A CB  
1010 O OG1 . THR A 127 ? 1.1873 0.8330 0.9010 -0.0346 -0.2489 0.0088  127 THR A OG1 
1011 C CG2 . THR A 127 ? 1.1100 0.7504 0.8250 -0.0289 -0.2473 0.0093  127 THR A CG2 
1012 N N   . LYS A 128 ? 1.0932 0.7203 0.8003 -0.0280 -0.2407 0.0068  128 LYS A N   
1013 C CA  . LYS A 128 ? 1.1032 0.7275 0.8103 -0.0250 -0.2383 0.0080  128 LYS A CA  
1014 C C   . LYS A 128 ? 1.0899 0.7174 0.7982 -0.0204 -0.2394 0.0090  128 LYS A C   
1015 O O   . LYS A 128 ? 1.0492 0.6774 0.7565 -0.0185 -0.2401 0.0081  128 LYS A O   
1016 C CB  . LYS A 128 ? 1.1061 0.7245 0.8112 -0.0246 -0.2344 0.0075  128 LYS A CB  
1017 C CG  . LYS A 128 ? 1.2164 0.8323 0.9218 -0.0295 -0.2324 0.0054  128 LYS A CG  
1018 C CD  . LYS A 128 ? 1.2898 0.9057 0.9973 -0.0310 -0.2310 0.0061  128 LYS A CD  
1019 C CE  . LYS A 128 ? 1.2246 0.8386 0.9332 -0.0360 -0.2281 0.0031  128 LYS A CE  
1020 N NZ  . LYS A 128 ? 1.1982 0.8120 0.9090 -0.0374 -0.2265 0.0035  128 LYS A NZ  
1021 N N   . GLY A 129 ? 1.0682 0.6984 0.7787 -0.0187 -0.2393 0.0104  129 GLY A N   
1022 C CA  . GLY A 129 ? 1.1178 0.7529 0.8303 -0.0148 -0.2400 0.0106  129 GLY A CA  
1023 C C   . GLY A 129 ? 1.1882 0.8229 0.8985 -0.0106 -0.2374 0.0113  129 GLY A C   
1024 O O   . GLY A 129 ? 1.2197 0.8504 0.9282 -0.0102 -0.2345 0.0130  129 GLY A O   
1025 N N   . PRO A 130 ? 1.1857 0.8253 0.8966 -0.0074 -0.2380 0.0101  130 PRO A N   
1026 C CA  . PRO A 130 ? 1.1806 0.8217 0.8893 -0.0032 -0.2356 0.0110  130 PRO A CA  
1027 C C   . PRO A 130 ? 1.3416 0.9883 1.0519 -0.0002 -0.2339 0.0133  130 PRO A C   
1028 O O   . PRO A 130 ? 1.3256 0.9766 1.0393 -0.0009 -0.2352 0.0131  130 PRO A O   
1029 C CB  . PRO A 130 ? 1.1426 0.7887 0.8521 -0.0013 -0.2370 0.0082  130 PRO A CB  
1030 C CG  . PRO A 130 ? 1.2373 0.8873 0.9519 -0.0033 -0.2394 0.0064  130 PRO A CG  
1031 C CD  . PRO A 130 ? 1.2346 0.8791 0.9492 -0.0076 -0.2405 0.0078  130 PRO A CD  
1032 N N   . SER A 131 ? 1.5507 1.1976 1.2589 0.0033  -0.2309 0.0158  131 SER A N   
1033 C CA  . SER A 131 ? 1.5358 1.1902 1.2455 0.0072  -0.2289 0.0187  131 SER A CA  
1034 C C   . SER A 131 ? 1.5315 1.1954 1.2407 0.0115  -0.2285 0.0178  131 SER A C   
1035 O O   . SER A 131 ? 1.5283 1.1899 1.2345 0.0130  -0.2273 0.0178  131 SER A O   
1036 C CB  . SER A 131 ? 1.5347 1.1837 1.2436 0.0083  -0.2248 0.0233  131 SER A CB  
1037 O OG  . SER A 131 ? 1.5793 1.2217 1.2896 0.0044  -0.2248 0.0237  131 SER A OG  
1038 N N   . VAL A 132 ? 1.3966 1.0718 1.1092 0.0133  -0.2294 0.0165  132 VAL A N   
1039 C CA  . VAL A 132 ? 1.3090 0.9960 1.0222 0.0168  -0.2291 0.0141  132 VAL A CA  
1040 C C   . VAL A 132 ? 1.2606 0.9579 0.9741 0.0215  -0.2263 0.0184  132 VAL A C   
1041 O O   . VAL A 132 ? 1.2506 0.9527 0.9669 0.0218  -0.2261 0.0203  132 VAL A O   
1042 C CB  . VAL A 132 ? 1.2967 0.9911 1.0150 0.0151  -0.2317 0.0086  132 VAL A CB  
1043 C CG1 . VAL A 132 ? 1.3471 1.0432 1.0695 0.0130  -0.2328 0.0092  132 VAL A CG1 
1044 C CG2 . VAL A 132 ? 1.2994 1.0086 1.0195 0.0188  -0.2307 0.0056  132 VAL A CG2 
1045 N N   . PHE A 133 ? 1.2087 0.9101 0.9194 0.0254  -0.2239 0.0202  133 PHE A N   
1046 C CA  . PHE A 133 ? 1.1870 0.8995 0.8980 0.0306  -0.2207 0.0253  133 PHE A CA  
1047 C C   . PHE A 133 ? 1.1952 0.9229 0.9060 0.0342  -0.2203 0.0225  133 PHE A C   
1048 O O   . PHE A 133 ? 1.2131 0.9378 0.9212 0.0339  -0.2209 0.0190  133 PHE A O   
1049 C CB  . PHE A 133 ? 1.1483 0.8514 0.8568 0.0323  -0.2169 0.0318  133 PHE A CB  
1050 C CG  . PHE A 133 ? 1.1806 0.8702 0.8901 0.0289  -0.2164 0.0342  133 PHE A CG  
1051 C CD1 . PHE A 133 ? 1.2001 0.8930 0.9129 0.0288  -0.2162 0.0365  133 PHE A CD1 
1052 C CD2 . PHE A 133 ? 1.2071 0.8817 0.9145 0.0256  -0.2159 0.0336  133 PHE A CD2 
1053 C CE1 . PHE A 133 ? 1.2329 0.9139 0.9468 0.0255  -0.2155 0.0381  133 PHE A CE1 
1054 C CE2 . PHE A 133 ? 1.2363 0.9000 0.9450 0.0221  -0.2151 0.0349  133 PHE A CE2 
1055 C CZ  . PHE A 133 ? 1.2456 0.9124 0.9576 0.0221  -0.2148 0.0371  133 PHE A CZ  
1056 N N   . PRO A 134 ? 1.1957 0.9409 0.9093 0.0377  -0.2191 0.0237  134 PRO A N   
1057 C CA  . PRO A 134 ? 1.1699 0.9323 0.8839 0.0409  -0.2186 0.0200  134 PRO A CA  
1058 C C   . PRO A 134 ? 1.1394 0.9073 0.8497 0.0461  -0.2151 0.0254  134 PRO A C   
1059 O O   . PRO A 134 ? 1.1680 0.9394 0.8785 0.0497  -0.2120 0.0333  134 PRO A O   
1060 C CB  . PRO A 134 ? 1.1651 0.9452 0.8843 0.0418  -0.2189 0.0187  134 PRO A CB  
1061 C CG  . PRO A 134 ? 1.1648 0.9391 0.8846 0.0422  -0.2178 0.0260  134 PRO A CG  
1062 C CD  . PRO A 134 ? 1.1826 0.9336 0.8995 0.0386  -0.2184 0.0278  134 PRO A CD  
1063 N N   . LEU A 135 ? 1.1395 0.9083 0.8468 0.0468  -0.2151 0.0216  135 LEU A N   
1064 C CA  . LEU A 135 ? 1.1788 0.9564 0.8830 0.0521  -0.2119 0.0258  135 LEU A CA  
1065 C C   . LEU A 135 ? 1.2047 1.0079 0.9115 0.0554  -0.2113 0.0225  135 LEU A C   
1066 O O   . LEU A 135 ? 1.2062 1.0160 0.9145 0.0535  -0.2131 0.0137  135 LEU A O   
1067 C CB  . LEU A 135 ? 1.1687 0.9344 0.8680 0.0510  -0.2123 0.0232  135 LEU A CB  
1068 C CG  . LEU A 135 ? 1.1642 0.9061 0.8616 0.0464  -0.2138 0.0236  135 LEU A CG  
1069 C CD1 . LEU A 135 ? 1.1403 0.8729 0.8332 0.0456  -0.2143 0.0206  135 LEU A CD1 
1070 C CD2 . LEU A 135 ? 1.1852 0.9184 0.8830 0.0474  -0.2108 0.0322  135 LEU A CD2 
1071 N N   . ALA A 136 ? 1.2062 1.0247 0.9144 0.0602  -0.2083 0.0295  136 ALA A N   
1072 C CA  . ALA A 136 ? 1.2234 1.0682 0.9354 0.0626  -0.2080 0.0263  136 ALA A CA  
1073 C C   . ALA A 136 ? 1.3020 1.1649 1.0116 0.0678  -0.2052 0.0273  136 ALA A C   
1074 O O   . ALA A 136 ? 1.3589 1.2158 1.0644 0.0711  -0.2025 0.0344  136 ALA A O   
1075 C CB  . ALA A 136 ? 1.2093 1.0635 0.9251 0.0647  -0.2067 0.0330  136 ALA A CB  
1076 N N   . PRO A 137 ? 1.3161 1.2017 1.0286 0.0685  -0.2055 0.0199  137 PRO A N   
1077 C CA  . PRO A 137 ? 1.3520 1.2587 1.0625 0.0737  -0.2026 0.0208  137 PRO A CA  
1078 C C   . PRO A 137 ? 1.4706 1.3941 1.1818 0.0799  -0.1990 0.0321  137 PRO A C   
1079 O O   . PRO A 137 ? 1.4388 1.3675 1.1540 0.0801  -0.1990 0.0361  137 PRO A O   
1080 C CB  . PRO A 137 ? 1.3185 1.2459 1.0337 0.0717  -0.2038 0.0086  137 PRO A CB  
1081 C CG  . PRO A 137 ? 1.2880 1.1985 1.0069 0.0650  -0.2073 0.0010  137 PRO A CG  
1082 C CD  . PRO A 137 ? 1.2818 1.1755 1.0003 0.0642  -0.2080 0.0097  137 PRO A CD  
1083 N N   . SER A 138 ? 1.6284 1.5607 1.3359 0.0852  -0.1957 0.0378  138 SER A N   
1084 C CA  . SER A 138 ? 1.6432 1.5931 1.3519 0.0920  -0.1915 0.0498  138 SER A CA  
1085 C C   . SER A 138 ? 1.6907 1.6594 1.3962 0.0970  -0.1887 0.0507  138 SER A C   
1086 O O   . SER A 138 ? 1.7074 1.6741 1.4097 0.0949  -0.1902 0.0417  138 SER A O   
1087 C CB  . SER A 138 ? 1.6802 1.6081 1.3884 0.0933  -0.1892 0.0617  138 SER A CB  
1088 O OG  . SER A 138 ? 1.7343 1.6795 1.4454 0.1001  -0.1846 0.0740  138 SER A OG  
1089 N N   . SER A 139 ? 1.6139 1.6016 1.3205 0.1039  -0.1843 0.0621  139 SER A N   
1090 C CA  . SER A 139 ? 1.5382 1.5423 1.2415 0.1094  -0.1811 0.0653  139 SER A CA  
1091 C C   . SER A 139 ? 1.5163 1.4937 1.2138 0.1082  -0.1809 0.0662  139 SER A C   
1092 O O   . SER A 139 ? 1.4874 1.4706 1.1806 0.1091  -0.1806 0.0616  139 SER A O   
1093 C CB  . SER A 139 ? 1.4814 1.5065 1.1876 0.1173  -0.1759 0.0801  139 SER A CB  
1094 O OG  . SER A 139 ? 1.5434 1.5863 1.2554 0.1178  -0.1763 0.0813  139 SER A OG  
1095 N N   . LYS A 140 ? 1.6211 1.5695 1.3187 0.1057  -0.1809 0.0714  140 LYS A N   
1096 C CA  . LYS A 140 ? 1.5372 1.4596 1.2300 0.1039  -0.1808 0.0716  140 LYS A CA  
1097 C C   . LYS A 140 ? 1.5649 1.4739 1.2543 0.0972  -0.1860 0.0574  140 LYS A C   
1098 O O   . LYS A 140 ? 1.4638 1.3633 1.1482 0.0966  -0.1863 0.0543  140 LYS A O   
1099 C CB  . LYS A 140 ? 1.4057 1.3031 1.1008 0.1028  -0.1790 0.0803  140 LYS A CB  
1100 C CG  . LYS A 140 ? 1.2930 1.2017 0.9928 0.1096  -0.1730 0.0952  140 LYS A CG  
1101 C CD  . LYS A 140 ? 1.2346 1.1572 0.9324 0.1161  -0.1685 0.1023  140 LYS A CD  
1102 C CE  . LYS A 140 ? 1.1903 1.1389 0.8936 0.1240  -0.1632 0.1151  140 LYS A CE  
1103 N NZ  . LYS A 140 ? 1.2016 1.1378 0.9115 0.1249  -0.1597 0.1255  140 LYS A NZ  
1104 N N   . SER A 141 ? 1.7707 1.6788 1.4632 0.0924  -0.1898 0.0492  141 SER A N   
1105 C CA  . SER A 141 ? 1.7657 1.6614 1.4565 0.0863  -0.1941 0.0364  141 SER A CA  
1106 C C   . SER A 141 ? 1.7604 1.6780 1.4505 0.0872  -0.1944 0.0270  141 SER A C   
1107 O O   . SER A 141 ? 1.7577 1.6659 1.4449 0.0844  -0.1963 0.0188  141 SER A O   
1108 C CB  . SER A 141 ? 1.7628 1.6501 1.4582 0.0808  -0.1975 0.0314  141 SER A CB  
1109 O OG  . SER A 141 ? 1.7785 1.6510 1.4753 0.0806  -0.1967 0.0404  141 SER A OG  
1110 N N   . THR A 142 ? 1.6343 1.5821 1.3277 0.0911  -0.1924 0.0277  142 THR A N   
1111 C CA  . THR A 142 ? 1.4836 1.4552 1.1772 0.0919  -0.1921 0.0179  142 THR A CA  
1112 C C   . THR A 142 ? 1.3911 1.3681 1.0787 0.0965  -0.1894 0.0213  142 THR A C   
1113 O O   . THR A 142 ? 1.3966 1.3713 1.0815 0.1012  -0.1864 0.0337  142 THR A O   
1114 C CB  . THR A 142 ? 1.4356 1.4402 1.1350 0.0943  -0.1907 0.0171  142 THR A CB  
1115 O OG1 . THR A 142 ? 1.5634 1.5799 1.2626 0.1008  -0.1872 0.0313  142 THR A OG1 
1116 C CG2 . THR A 142 ? 1.3753 1.3756 1.0811 0.0892  -0.1936 0.0115  142 THR A CG2 
1117 N N   . SER A 143 ? 1.3319 1.3159 1.0179 0.0950  -0.1902 0.0101  143 SER A N   
1118 C CA  . SER A 143 ? 1.3419 1.3329 1.0220 0.0990  -0.1879 0.0115  143 SER A CA  
1119 C C   . SER A 143 ? 1.3350 1.3530 1.0172 0.0987  -0.1875 -0.0013 143 SER A C   
1120 O O   . SER A 143 ? 1.3664 1.3755 1.0482 0.0946  -0.1893 -0.0130 143 SER A O   
1121 C CB  . SER A 143 ? 1.3285 1.2881 1.0027 0.0964  -0.1895 0.0113  143 SER A CB  
1122 O OG  . SER A 143 ? 1.3306 1.2974 0.9991 0.1001  -0.1875 0.0119  143 SER A OG  
1123 N N   . GLY A 144 ? 1.2683 1.3200 0.9532 0.1032  -0.1846 0.0009  144 GLY A N   
1124 C CA  . GLY A 144 ? 1.2204 1.3012 0.9083 0.1028  -0.1837 -0.0119 144 GLY A CA  
1125 C C   . GLY A 144 ? 1.2466 1.3275 0.9427 0.0964  -0.1860 -0.0247 144 GLY A C   
1126 O O   . GLY A 144 ? 1.2541 1.3348 0.9552 0.0950  -0.1871 -0.0217 144 GLY A O   
1127 N N   . GLY A 145 ? 1.2523 1.3332 0.9503 0.0925  -0.1866 -0.0391 145 GLY A N   
1128 C CA  . GLY A 145 ? 1.2341 1.3135 0.9411 0.0863  -0.1882 -0.0516 145 GLY A CA  
1129 C C   . GLY A 145 ? 1.3477 1.3908 1.0551 0.0816  -0.1918 -0.0492 145 GLY A C   
1130 O O   . GLY A 145 ? 1.3774 1.4181 1.0921 0.0776  -0.1932 -0.0528 145 GLY A O   
1131 N N   . THR A 146 ? 1.3959 1.4114 1.0957 0.0819  -0.1931 -0.0431 146 THR A N   
1132 C CA  . THR A 146 ? 1.4231 1.4051 1.1227 0.0775  -0.1965 -0.0410 146 THR A CA  
1133 C C   . THR A 146 ? 1.4125 1.3862 1.1113 0.0788  -0.1972 -0.0283 146 THR A C   
1134 O O   . THR A 146 ? 1.4434 1.4219 1.1374 0.0839  -0.1953 -0.0169 146 THR A O   
1135 C CB  . THR A 146 ? 1.5076 1.4647 1.1995 0.0771  -0.1976 -0.0394 146 THR A CB  
1136 O OG1 . THR A 146 ? 1.5211 1.4778 1.2052 0.0825  -0.1959 -0.0274 146 THR A OG1 
1137 C CG2 . THR A 146 ? 1.4319 1.3969 1.1247 0.0761  -0.1966 -0.0519 146 THR A CG2 
1138 N N   . ALA A 147 ? 1.3239 1.2854 1.0281 0.0742  -0.1995 -0.0301 147 ALA A N   
1139 C CA  . ALA A 147 ? 1.3209 1.2708 1.0248 0.0745  -0.2005 -0.0194 147 ALA A CA  
1140 C C   . ALA A 147 ? 1.3465 1.2637 1.0497 0.0694  -0.2037 -0.0195 147 ALA A C   
1141 O O   . ALA A 147 ? 1.3416 1.2512 1.0486 0.0648  -0.2054 -0.0292 147 ALA A O   
1142 C CB  . ALA A 147 ? 1.2545 1.2243 0.9661 0.0740  -0.2003 -0.0210 147 ALA A CB  
1143 N N   . ALA A 148 ? 1.3916 1.2906 1.0905 0.0704  -0.2040 -0.0085 148 ALA A N   
1144 C CA  . ALA A 148 ? 1.2533 1.1225 0.9507 0.0659  -0.2067 -0.0075 148 ALA A CA  
1145 C C   . ALA A 148 ? 1.2413 1.1033 0.9421 0.0641  -0.2078 -0.0021 148 ALA A C   
1146 O O   . ALA A 148 ? 1.3385 1.2089 1.0393 0.0677  -0.2058 0.0066  148 ALA A O   
1147 C CB  . ALA A 148 ? 1.2770 1.1287 0.9669 0.0676  -0.2060 -0.0007 148 ALA A CB  
1148 N N   . LEU A 149 ? 1.1553 1.0028 0.8595 0.0587  -0.2107 -0.0073 149 LEU A N   
1149 C CA  . LEU A 149 ? 1.1563 0.9916 0.8630 0.0558  -0.2123 -0.0032 149 LEU A CA  
1150 C C   . LEU A 149 ? 1.1409 0.9500 0.8458 0.0511  -0.2150 -0.0046 149 LEU A C   
1151 O O   . LEU A 149 ? 1.1563 0.9577 0.8587 0.0500  -0.2157 -0.0090 149 LEU A O   
1152 C CB  . LEU A 149 ? 1.1884 1.0385 0.9029 0.0539  -0.2131 -0.0086 149 LEU A CB  
1153 C CG  . LEU A 149 ? 1.2071 1.0581 0.9280 0.0494  -0.2148 -0.0202 149 LEU A CG  
1154 C CD1 . LEU A 149 ? 1.1871 1.0496 0.9162 0.0472  -0.2153 -0.0239 149 LEU A CD1 
1155 C CD2 . LEU A 149 ? 1.1965 1.0676 0.9183 0.0518  -0.2126 -0.0274 149 LEU A CD2 
1156 N N   . GLY A 150 ? 1.1399 0.9361 0.8462 0.0484  -0.2164 -0.0006 150 GLY A N   
1157 C CA  . GLY A 150 ? 1.1585 0.9315 0.8627 0.0442  -0.2186 -0.0007 150 GLY A CA  
1158 C C   . GLY A 150 ? 1.1916 0.9547 0.8989 0.0405  -0.2204 0.0013  150 GLY A C   
1159 O O   . GLY A 150 ? 1.1941 0.9662 0.9046 0.0415  -0.2198 0.0039  150 GLY A O   
1160 N N   . CYS A 151 ? 1.1856 0.9308 0.8919 0.0364  -0.2225 -0.0001 151 CYS A N   
1161 C CA  . CYS A 151 ? 1.1447 0.8783 0.8532 0.0324  -0.2244 0.0016  151 CYS A CA  
1162 C C   . CYS A 151 ? 1.1460 0.8609 0.8496 0.0304  -0.2247 0.0053  151 CYS A C   
1163 O O   . CYS A 151 ? 1.1336 0.8415 0.8345 0.0294  -0.2255 0.0026  151 CYS A O   
1164 C CB  . CYS A 151 ? 1.2615 0.9955 0.9760 0.0285  -0.2268 -0.0053 151 CYS A CB  
1165 S SG  . CYS A 151 ? 1.4748 1.2064 1.1947 0.0250  -0.2285 -0.0040 151 CYS A SG  
1166 N N   . LEU A 152 ? 1.1871 0.8946 0.8900 0.0298  -0.2238 0.0111  152 LEU A N   
1167 C CA  . LEU A 152 ? 1.1611 0.8524 0.8602 0.0279  -0.2232 0.0144  152 LEU A CA  
1168 C C   . LEU A 152 ? 1.1725 0.8532 0.8736 0.0227  -0.2256 0.0133  152 LEU A C   
1169 O O   . LEU A 152 ? 1.2143 0.8964 0.9183 0.0218  -0.2256 0.0153  152 LEU A O   
1170 C CB  . LEU A 152 ? 1.1103 0.8012 0.8082 0.0312  -0.2192 0.0218  152 LEU A CB  
1171 C CG  . LEU A 152 ? 1.0988 0.7745 0.7940 0.0296  -0.2173 0.0248  152 LEU A CG  
1172 C CD1 . LEU A 152 ? 1.1045 0.7793 0.7957 0.0315  -0.2165 0.0239  152 LEU A CD1 
1173 C CD2 . LEU A 152 ? 1.0850 0.7590 0.7823 0.0315  -0.2131 0.0319  152 LEU A CD2 
1174 N N   . VAL A 153 ? 1.1577 0.8286 0.8572 0.0193  -0.2275 0.0104  153 VAL A N   
1175 C CA  . VAL A 153 ? 1.1697 0.8315 0.8706 0.0143  -0.2298 0.0095  153 VAL A CA  
1176 C C   . VAL A 153 ? 1.2255 0.8759 0.9233 0.0126  -0.2280 0.0128  153 VAL A C   
1177 O O   . VAL A 153 ? 1.1947 0.8381 0.8896 0.0112  -0.2282 0.0116  153 VAL A O   
1178 C CB  . VAL A 153 ? 1.1262 0.7865 0.8284 0.0118  -0.2327 0.0046  153 VAL A CB  
1179 C CG1 . VAL A 153 ? 1.2060 0.8617 0.9113 0.0073  -0.2350 0.0042  153 VAL A CG1 
1180 C CG2 . VAL A 153 ? 1.1019 0.7741 0.8074 0.0143  -0.2330 0.0006  153 VAL A CG2 
1181 N N   . LYS A 154 ? 1.1837 0.8324 0.8829 0.0126  -0.2259 0.0166  154 LYS A N   
1182 C CA  . LYS A 154 ? 1.1977 0.8379 0.8956 0.0123  -0.2224 0.0201  154 LYS A CA  
1183 C C   . LYS A 154 ? 1.2377 0.8672 0.9350 0.0068  -0.2233 0.0179  154 LYS A C   
1184 O O   . LYS A 154 ? 1.2787 0.9020 0.9738 0.0059  -0.2221 0.0174  154 LYS A O   
1185 C CB  . LYS A 154 ? 1.2643 0.9068 0.9651 0.0143  -0.2191 0.0250  154 LYS A CB  
1186 C CG  . LYS A 154 ? 1.3140 0.9494 1.0150 0.0153  -0.2141 0.0291  154 LYS A CG  
1187 C CD  . LYS A 154 ? 1.3036 0.9411 1.0020 0.0191  -0.2122 0.0304  154 LYS A CD  
1188 C CE  . LYS A 154 ? 1.2569 0.8845 0.9562 0.0184  -0.2075 0.0330  154 LYS A CE  
1189 N NZ  . LYS A 154 ? 1.2716 0.8981 0.9675 0.0201  -0.2070 0.0323  154 LYS A NZ  
1190 N N   . ASP A 155 ? 1.1705 0.7985 0.8698 0.0030  -0.2253 0.0168  155 ASP A N   
1191 C CA  . ASP A 155 ? 1.1268 0.7466 0.8262 -0.0021 -0.2252 0.0153  155 ASP A CA  
1192 C C   . ASP A 155 ? 1.1370 0.7583 0.8371 -0.0058 -0.2296 0.0123  155 ASP A C   
1193 O O   . ASP A 155 ? 1.2080 0.8323 0.9106 -0.0068 -0.2308 0.0127  155 ASP A O   
1194 C CB  . ASP A 155 ? 1.1389 0.7551 0.8409 -0.0030 -0.2216 0.0180  155 ASP A CB  
1195 C CG  . ASP A 155 ? 1.1961 0.8075 0.8987 -0.0012 -0.2163 0.0206  155 ASP A CG  
1196 O OD1 . ASP A 155 ? 1.1933 0.8013 0.8937 -0.0014 -0.2158 0.0193  155 ASP A OD1 
1197 O OD2 . ASP A 155 ? 1.1451 0.7561 0.8507 0.0007  -0.2124 0.0244  155 ASP A OD2 
1198 N N   . TYR A 156 ? 1.0804 0.7000 0.7789 -0.0079 -0.2317 0.0096  156 TYR A N   
1199 C CA  . TYR A 156 ? 1.0534 0.6755 0.7535 -0.0109 -0.2354 0.0077  156 TYR A CA  
1200 C C   . TYR A 156 ? 1.0021 0.6207 0.7005 -0.0147 -0.2366 0.0056  156 TYR A C   
1201 O O   . TYR A 156 ? 0.9873 0.6024 0.6829 -0.0141 -0.2355 0.0047  156 TYR A O   
1202 C CB  . TYR A 156 ? 1.0320 0.6606 0.7339 -0.0081 -0.2376 0.0067  156 TYR A CB  
1203 C CG  . TYR A 156 ? 0.9677 0.5964 0.6673 -0.0058 -0.2379 0.0049  156 TYR A CG  
1204 C CD1 . TYR A 156 ? 1.0087 0.6359 0.7080 -0.0079 -0.2401 0.0030  156 TYR A CD1 
1205 C CD2 . TYR A 156 ? 1.0081 0.6394 0.7061 -0.0014 -0.2360 0.0053  156 TYR A CD2 
1206 C CE1 . TYR A 156 ? 1.0165 0.6436 0.7138 -0.0059 -0.2403 0.0012  156 TYR A CE1 
1207 C CE2 . TYR A 156 ? 1.0401 0.6718 0.7358 0.0006  -0.2362 0.0034  156 TYR A CE2 
1208 C CZ  . TYR A 156 ? 1.0083 0.6373 0.7036 -0.0017 -0.2384 0.0012  156 TYR A CZ  
1209 O OH  . TYR A 156 ? 1.0597 0.6888 0.7527 0.0004  -0.2386 -0.0009 156 TYR A OH  
1210 N N   . PHE A 157 ? 1.0147 0.6353 0.7150 -0.0184 -0.2388 0.0050  157 PHE A N   
1211 C CA  . PHE A 157 ? 1.0374 0.6583 0.7372 -0.0222 -0.2406 0.0034  157 PHE A CA  
1212 C C   . PHE A 157 ? 1.0543 0.6811 0.7577 -0.0234 -0.2437 0.0042  157 PHE A C   
1213 O O   . PHE A 157 ? 1.1266 0.7557 0.8326 -0.0237 -0.2438 0.0056  157 PHE A O   
1214 C CB  . PHE A 157 ? 0.9856 0.6036 0.6846 -0.0266 -0.2387 0.0022  157 PHE A CB  
1215 C CG  . PHE A 157 ? 0.9574 0.5756 0.6550 -0.0299 -0.2396 -0.0001 157 PHE A CG  
1216 C CD1 . PHE A 157 ? 0.9678 0.5817 0.6627 -0.0287 -0.2385 -0.0014 157 PHE A CD1 
1217 C CD2 . PHE A 157 ? 0.9727 0.5966 0.6718 -0.0340 -0.2417 -0.0007 157 PHE A CD2 
1218 C CE1 . PHE A 157 ? 0.9739 0.5886 0.6676 -0.0319 -0.2395 -0.0038 157 PHE A CE1 
1219 C CE2 . PHE A 157 ? 0.9689 0.5949 0.6668 -0.0370 -0.2427 -0.0028 157 PHE A CE2 
1220 C CZ  . PHE A 157 ? 0.9654 0.5865 0.6607 -0.0360 -0.2416 -0.0045 157 PHE A CZ  
1221 N N   . PRO A 158 ? 1.0101 0.6398 0.7145 -0.0239 -0.2458 0.0038  158 PRO A N   
1222 C CA  . PRO A 158 ? 0.9948 0.6224 0.6965 -0.0231 -0.2462 0.0023  158 PRO A CA  
1223 C C   . PRO A 158 ? 0.9985 0.6257 0.7003 -0.0183 -0.2459 0.0017  158 PRO A C   
1224 O O   . PRO A 158 ? 0.9919 0.6202 0.6951 -0.0156 -0.2450 0.0023  158 PRO A O   
1225 C CB  . PRO A 158 ? 1.0317 0.6643 0.7358 -0.0256 -0.2486 0.0028  158 PRO A CB  
1226 C CG  . PRO A 158 ? 1.1392 0.7771 0.8485 -0.0258 -0.2496 0.0052  158 PRO A CG  
1227 C CD  . PRO A 158 ? 1.0484 0.6841 0.7567 -0.0265 -0.2480 0.0053  158 PRO A CD  
1228 N N   . GLU A 159 ? 1.1129 0.7394 0.8133 -0.0172 -0.2468 0.0004  159 GLU A N   
1229 C CA  . GLU A 159 ? 1.1667 0.7923 0.8658 -0.0130 -0.2460 -0.0010 159 GLU A CA  
1230 C C   . GLU A 159 ? 1.2192 0.8500 0.9232 -0.0099 -0.2461 -0.0015 159 GLU A C   
1231 O O   . GLU A 159 ? 1.2518 0.8836 0.9548 -0.0065 -0.2446 -0.0025 159 GLU A O   
1232 C CB  . GLU A 159 ? 1.1874 0.8109 0.8840 -0.0132 -0.2471 -0.0026 159 GLU A CB  
1233 C CG  . GLU A 159 ? 1.1499 0.7730 0.8450 -0.0089 -0.2463 -0.0046 159 GLU A CG  
1234 C CD  . GLU A 159 ? 1.1420 0.7610 0.8318 -0.0071 -0.2440 -0.0047 159 GLU A CD  
1235 O OE1 . GLU A 159 ? 1.1233 0.7437 0.8137 -0.0056 -0.2423 -0.0033 159 GLU A OE1 
1236 O OE2 . GLU A 159 ? 1.1941 0.8089 0.8797 -0.0070 -0.2438 -0.0058 159 GLU A OE2 
1237 N N   . PRO A 160 ? 1.1334 0.7685 0.8436 -0.0107 -0.2474 -0.0009 160 PRO A N   
1238 C CA  . PRO A 160 ? 1.0435 0.6838 0.7600 -0.0079 -0.2468 -0.0025 160 PRO A CA  
1239 C C   . PRO A 160 ? 1.0438 0.6869 0.7612 -0.0061 -0.2454 -0.0029 160 PRO A C   
1240 O O   . PRO A 160 ? 1.1138 0.7580 0.8331 -0.0077 -0.2456 -0.0009 160 PRO A O   
1241 C CB  . PRO A 160 ? 1.0842 0.7281 0.8082 -0.0098 -0.2479 -0.0005 160 PRO A CB  
1242 C CG  . PRO A 160 ? 1.1496 0.7912 0.8704 -0.0126 -0.2494 0.0013  160 PRO A CG  
1243 C CD  . PRO A 160 ? 1.0695 0.7062 0.7823 -0.0141 -0.2492 0.0011  160 PRO A CD  
1244 N N   . VAL A 161 ? 0.9826 0.6281 0.6988 -0.0026 -0.2439 -0.0054 161 VAL A N   
1245 C CA  . VAL A 161 ? 1.0407 0.6922 0.7592 -0.0003 -0.2425 -0.0064 161 VAL A CA  
1246 C C   . VAL A 161 ? 1.0739 0.7320 0.7967 0.0026  -0.2413 -0.0107 161 VAL A C   
1247 O O   . VAL A 161 ? 1.0940 0.7507 0.8131 0.0043  -0.2409 -0.0126 161 VAL A O   
1248 C CB  . VAL A 161 ? 1.0096 0.6594 0.7215 0.0012  -0.2412 -0.0046 161 VAL A CB  
1249 C CG1 . VAL A 161 ? 0.9880 0.6462 0.7029 0.0037  -0.2398 -0.0053 161 VAL A CG1 
1250 C CG2 . VAL A 161 ? 1.0662 0.7099 0.7754 -0.0019 -0.2416 -0.0012 161 VAL A CG2 
1251 N N   . THR A 162 ? 1.0737 0.7392 0.8043 0.0029  -0.2405 -0.0127 162 THR A N   
1252 C CA  . THR A 162 ? 1.0464 0.7200 0.7833 0.0051  -0.2387 -0.0179 162 THR A CA  
1253 C C   . THR A 162 ? 1.1391 0.8221 0.8768 0.0072  -0.2371 -0.0198 162 THR A C   
1254 O O   . THR A 162 ? 1.1730 0.8583 0.9134 0.0061  -0.2374 -0.0181 162 THR A O   
1255 C CB  . THR A 162 ? 1.0903 0.7660 0.8383 0.0034  -0.2383 -0.0194 162 THR A CB  
1256 O OG1 . THR A 162 ? 1.1196 0.7939 0.8704 0.0009  -0.2394 -0.0157 162 THR A OG1 
1257 C CG2 . THR A 162 ? 1.0372 0.7070 0.7856 0.0027  -0.2390 -0.0186 162 THR A CG2 
1258 N N   . VAL A 163 ? 1.1846 0.8739 0.9202 0.0103  -0.2355 -0.0232 163 VAL A N   
1259 C CA  . VAL A 163 ? 1.2358 0.9367 0.9718 0.0128  -0.2339 -0.0249 163 VAL A CA  
1260 C C   . VAL A 163 ? 1.2907 1.0033 1.0343 0.0142  -0.2316 -0.0323 163 VAL A C   
1261 O O   . VAL A 163 ? 1.2493 0.9615 0.9917 0.0155  -0.2309 -0.0355 163 VAL A O   
1262 C CB  . VAL A 163 ? 1.1695 0.8696 0.8955 0.0156  -0.2335 -0.0215 163 VAL A CB  
1263 C CG1 . VAL A 163 ? 1.2760 0.9889 1.0028 0.0181  -0.2319 -0.0215 163 VAL A CG1 
1264 C CG2 . VAL A 163 ? 1.1558 0.8428 0.8752 0.0138  -0.2350 -0.0154 163 VAL A CG2 
1265 N N   . SER A 164 ? 1.4272 1.1507 1.1789 0.0138  -0.2304 -0.0354 164 SER A N   
1266 C CA  . SER A 164 ? 1.4504 1.1879 1.2106 0.0148  -0.2276 -0.0434 164 SER A CA  
1267 C C   . SER A 164 ? 1.4761 1.2286 1.2362 0.0167  -0.2264 -0.0446 164 SER A C   
1268 O O   . SER A 164 ? 1.4569 1.2084 1.2140 0.0164  -0.2278 -0.0396 164 SER A O   
1269 C CB  . SER A 164 ? 1.4675 1.2058 1.2412 0.0119  -0.2263 -0.0474 164 SER A CB  
1270 O OG  . SER A 164 ? 1.4792 1.2179 1.2570 0.0098  -0.2273 -0.0447 164 SER A OG  
1271 N N   . TRP A 165 ? 1.3829 1.1503 1.1465 0.0187  -0.2238 -0.0514 165 TRP A N   
1272 C CA  . TRP A 165 ? 1.3108 1.0958 1.0745 0.0209  -0.2225 -0.0531 165 TRP A CA  
1273 C C   . TRP A 165 ? 1.3114 1.1116 1.0888 0.0190  -0.2199 -0.0617 165 TRP A C   
1274 O O   . TRP A 165 ? 1.3251 1.1279 1.1107 0.0179  -0.2176 -0.0691 165 TRP A O   
1275 C CB  . TRP A 165 ? 1.2405 1.0340 0.9966 0.0249  -0.2212 -0.0538 165 TRP A CB  
1276 C CG  . TRP A 165 ? 1.2828 1.0642 1.0264 0.0269  -0.2230 -0.0448 165 TRP A CG  
1277 C CD1 . TRP A 165 ? 1.2833 1.0479 1.0206 0.0265  -0.2244 -0.0417 165 TRP A CD1 
1278 C CD2 . TRP A 165 ? 1.3318 1.1173 1.0688 0.0296  -0.2231 -0.0379 165 TRP A CD2 
1279 N NE1 . TRP A 165 ? 1.3176 1.0755 1.0452 0.0285  -0.2252 -0.0338 165 TRP A NE1 
1280 C CE2 . TRP A 165 ? 1.2887 1.0588 1.0162 0.0306  -0.2242 -0.0310 165 TRP A CE2 
1281 C CE3 . TRP A 165 ? 1.3420 1.1433 1.0809 0.0314  -0.2221 -0.0367 165 TRP A CE3 
1282 C CZ2 . TRP A 165 ? 1.2587 1.0281 0.9796 0.0332  -0.2238 -0.0231 165 TRP A CZ2 
1283 C CZ3 . TRP A 165 ? 1.3573 1.1581 1.0890 0.0344  -0.2220 -0.0282 165 TRP A CZ3 
1284 C CH2 . TRP A 165 ? 1.3098 1.0944 1.0330 0.0353  -0.2226 -0.0214 165 TRP A CH2 
1285 N N   . ASN A 166 ? 1.2076 1.0178 0.9879 0.0186  -0.2201 -0.0610 166 ASN A N   
1286 C CA  . ASN A 166 ? 1.1774 1.0032 0.9713 0.0165  -0.2176 -0.0693 166 ASN A CA  
1287 C C   . ASN A 166 ? 1.1722 0.9884 0.9776 0.0126  -0.2168 -0.0727 166 ASN A C   
1288 O O   . ASN A 166 ? 1.1115 0.9380 0.9296 0.0110  -0.2133 -0.0818 166 ASN A O   
1289 C CB  . ASN A 166 ? 1.1827 1.0297 0.9802 0.0185  -0.2142 -0.0781 166 ASN A CB  
1290 C CG  . ASN A 166 ? 1.2432 1.1055 1.0328 0.0222  -0.2144 -0.0748 166 ASN A CG  
1291 O OD1 . ASN A 166 ? 1.2743 1.1303 1.0560 0.0234  -0.2169 -0.0658 166 ASN A OD1 
1292 N ND2 . ASN A 166 ? 1.2573 1.1408 1.0496 0.0241  -0.2115 -0.0821 166 ASN A ND2 
1293 N N   . SER A 167 ? 1.1972 0.9943 0.9985 0.0111  -0.2195 -0.0652 167 SER A N   
1294 C CA  . SER A 167 ? 1.1228 0.9099 0.9342 0.0078  -0.2189 -0.0660 167 SER A CA  
1295 C C   . SER A 167 ? 1.1224 0.9090 0.9402 0.0080  -0.2160 -0.0721 167 SER A C   
1296 O O   . SER A 167 ? 1.1351 0.9247 0.9674 0.0059  -0.2128 -0.0778 167 SER A O   
1297 C CB  . SER A 167 ? 1.0578 0.8534 0.8823 0.0049  -0.2174 -0.0698 167 SER A CB  
1298 O OG  . SER A 167 ? 1.0554 0.8503 0.8738 0.0047  -0.2203 -0.0638 167 SER A OG  
1299 N N   . GLY A 168 ? 1.1821 0.9648 0.9896 0.0107  -0.2168 -0.0708 168 GLY A N   
1300 C CA  . GLY A 168 ? 1.1348 0.9158 0.9464 0.0112  -0.2144 -0.0759 168 GLY A CA  
1301 C C   . GLY A 168 ? 1.0799 0.8791 0.8979 0.0124  -0.2103 -0.0864 168 GLY A C   
1302 O O   . GLY A 168 ? 1.0243 0.8229 0.8445 0.0133  -0.2082 -0.0910 168 GLY A O   
1303 N N   . ALA A 169 ? 1.1056 0.9221 0.9269 0.0125  -0.2091 -0.0905 169 ALA A N   
1304 C CA  . ALA A 169 ? 1.0358 0.8725 0.8640 0.0134  -0.2049 -0.1013 169 ALA A CA  
1305 C C   . ALA A 169 ? 1.0988 0.9395 0.9141 0.0173  -0.2056 -0.1007 169 ALA A C   
1306 O O   . ALA A 169 ? 1.0703 0.9201 0.8896 0.0181  -0.2023 -0.1089 169 ALA A O   
1307 C CB  . ALA A 169 ? 0.9724 0.8283 0.8072 0.0123  -0.2036 -0.1055 169 ALA A CB  
1308 N N   . LEU A 170 ? 1.1632 0.9974 0.9636 0.0196  -0.2094 -0.0911 170 LEU A N   
1309 C CA  . LEU A 170 ? 1.1429 0.9809 0.9310 0.0236  -0.2099 -0.0892 170 LEU A CA  
1310 C C   . LEU A 170 ? 1.1596 0.9764 0.9390 0.0241  -0.2121 -0.0837 170 LEU A C   
1311 O O   . LEU A 170 ? 1.1603 0.9614 0.9319 0.0238  -0.2155 -0.0745 170 LEU A O   
1312 C CB  . LEU A 170 ? 1.1106 0.9557 0.8892 0.0261  -0.2118 -0.0820 170 LEU A CB  
1313 C CG  . LEU A 170 ? 1.1142 0.9676 0.8818 0.0307  -0.2114 -0.0800 170 LEU A CG  
1314 C CD1 . LEU A 170 ? 1.1469 1.0174 0.9201 0.0315  -0.2076 -0.0910 170 LEU A CD1 
1315 C CD2 . LEU A 170 ? 1.1332 0.9990 0.8954 0.0334  -0.2120 -0.0738 170 LEU A CD2 
1316 N N   . THR A 171 ? 1.1857 1.0030 0.9671 0.0248  -0.2100 -0.0898 171 THR A N   
1317 C CA  . THR A 171 ? 1.1925 0.9931 0.9645 0.0259  -0.2119 -0.0855 171 THR A CA  
1318 C C   . THR A 171 ? 1.2684 1.0775 1.0317 0.0296  -0.2110 -0.0876 171 THR A C   
1319 O O   . THR A 171 ? 1.2545 1.0511 1.0093 0.0307  -0.2125 -0.0843 171 THR A O   
1320 C CB  . THR A 171 ? 1.1344 0.9248 0.9158 0.0235  -0.2106 -0.0896 171 THR A CB  
1321 O OG1 . THR A 171 ? 1.1456 0.9498 0.9362 0.0239  -0.2061 -0.1007 171 THR A OG1 
1322 C CG2 . THR A 171 ? 1.0723 0.8572 0.8644 0.0201  -0.2107 -0.0880 171 THR A CG2 
1323 N N   . SER A 172 ? 1.3675 1.1986 1.1329 0.0314  -0.2084 -0.0930 172 SER A N   
1324 C CA  . SER A 172 ? 1.3784 1.2209 1.1365 0.0350  -0.2070 -0.0955 172 SER A CA  
1325 C C   . SER A 172 ? 1.4152 1.2544 1.1593 0.0383  -0.2095 -0.0847 172 SER A C   
1326 O O   . SER A 172 ? 1.3993 1.2483 1.1426 0.0393  -0.2098 -0.0805 172 SER A O   
1327 C CB  . SER A 172 ? 1.3548 1.2246 1.1216 0.0355  -0.2029 -0.1058 172 SER A CB  
1328 O OG  . SER A 172 ? 1.3315 1.2045 1.1139 0.0318  -0.2001 -0.1153 172 SER A OG  
1329 N N   . GLY A 173 ? 1.3347 1.1603 1.0687 0.0399  -0.2110 -0.0801 173 GLY A N   
1330 C CA  . GLY A 173 ? 1.2530 1.0737 0.9749 0.0429  -0.2127 -0.0699 173 GLY A CA  
1331 C C   . GLY A 173 ? 1.1868 0.9894 0.9056 0.0411  -0.2157 -0.0605 173 GLY A C   
1332 O O   . GLY A 173 ? 1.1202 0.9204 0.8312 0.0434  -0.2163 -0.0520 173 GLY A O   
1333 N N   . VAL A 174 ? 1.1899 0.9802 0.9150 0.0371  -0.2172 -0.0617 174 VAL A N   
1334 C CA  . VAL A 174 ? 1.1457 0.9196 0.8682 0.0350  -0.2200 -0.0536 174 VAL A CA  
1335 C C   . VAL A 174 ? 1.1301 0.8849 0.8444 0.0346  -0.2220 -0.0489 174 VAL A C   
1336 O O   . VAL A 174 ? 1.1197 0.8659 0.8362 0.0329  -0.2226 -0.0526 174 VAL A O   
1337 C CB  . VAL A 174 ? 1.1417 0.9124 0.8749 0.0310  -0.2205 -0.0565 174 VAL A CB  
1338 C CG1 . VAL A 174 ? 1.0789 0.8322 0.8088 0.0286  -0.2235 -0.0485 174 VAL A CG1 
1339 C CG2 . VAL A 174 ? 1.1887 0.9780 0.9298 0.0310  -0.2187 -0.0604 174 VAL A CG2 
1340 N N   . HIS A 175 ? 1.1298 0.8784 0.8354 0.0362  -0.2227 -0.0409 175 HIS A N   
1341 C CA  . HIS A 175 ? 1.0621 0.7930 0.7601 0.0355  -0.2244 -0.0361 175 HIS A CA  
1342 C C   . HIS A 175 ? 1.0463 0.7648 0.7438 0.0328  -0.2263 -0.0296 175 HIS A C   
1343 O O   . HIS A 175 ? 1.0682 0.7901 0.7643 0.0340  -0.2256 -0.0244 175 HIS A O   
1344 C CB  . HIS A 175 ? 1.0348 0.7682 0.7242 0.0395  -0.2230 -0.0323 175 HIS A CB  
1345 C CG  . HIS A 175 ? 0.9956 0.7350 0.6829 0.0416  -0.2218 -0.0381 175 HIS A CG  
1346 N ND1 . HIS A 175 ? 0.9785 0.7363 0.6649 0.0456  -0.2192 -0.0403 175 HIS A ND1 
1347 C CD2 . HIS A 175 ? 0.9765 0.7067 0.6623 0.0404  -0.2228 -0.0420 175 HIS A CD2 
1348 C CE1 . HIS A 175 ? 1.0279 0.7873 0.7123 0.0466  -0.2186 -0.0458 175 HIS A CE1 
1349 N NE2 . HIS A 175 ? 1.0197 0.7619 0.7037 0.0436  -0.2208 -0.0469 175 HIS A NE2 
1350 N N   . THR A 176 ? 1.0065 0.7117 0.7056 0.0291  -0.2285 -0.0299 176 THR A N   
1351 C CA  . THR A 176 ? 0.9808 0.6739 0.6788 0.0261  -0.2303 -0.0243 176 THR A CA  
1352 C C   . THR A 176 ? 0.9823 0.6618 0.6729 0.0254  -0.2313 -0.0212 176 THR A C   
1353 O O   . THR A 176 ? 0.9817 0.6546 0.6723 0.0238  -0.2327 -0.0239 176 THR A O   
1354 C CB  . THR A 176 ? 1.0056 0.6957 0.7113 0.0225  -0.2319 -0.0264 176 THR A CB  
1355 O OG1 . THR A 176 ? 1.0972 0.8001 0.8103 0.0230  -0.2307 -0.0295 176 THR A OG1 
1356 C CG2 . THR A 176 ? 0.9876 0.6664 0.6916 0.0193  -0.2337 -0.0208 176 THR A CG2 
1357 N N   . PHE A 177 ? 0.9808 0.6566 0.6661 0.0265  -0.2303 -0.0156 177 PHE A N   
1358 C CA  . PHE A 177 ? 0.8888 0.5531 0.5678 0.0259  -0.2305 -0.0129 177 PHE A CA  
1359 C C   . PHE A 177 ? 0.8851 0.5369 0.5647 0.0211  -0.2328 -0.0117 177 PHE A C   
1360 O O   . PHE A 177 ? 0.9016 0.5531 0.5853 0.0187  -0.2336 -0.0106 177 PHE A O   
1361 C CB  . PHE A 177 ? 0.9233 0.5882 0.5984 0.0286  -0.2277 -0.0071 177 PHE A CB  
1362 C CG  . PHE A 177 ? 0.9313 0.6092 0.6047 0.0336  -0.2252 -0.0073 177 PHE A CG  
1363 C CD1 . PHE A 177 ? 0.9723 0.6649 0.6497 0.0360  -0.2240 -0.0076 177 PHE A CD1 
1364 C CD2 . PHE A 177 ? 0.9153 0.5918 0.5833 0.0360  -0.2241 -0.0071 177 PHE A CD2 
1365 C CE1 . PHE A 177 ? 0.9983 0.7054 0.6744 0.0407  -0.2217 -0.0079 177 PHE A CE1 
1366 C CE2 . PHE A 177 ? 0.9347 0.6249 0.6012 0.0408  -0.2217 -0.0071 177 PHE A CE2 
1367 C CZ  . PHE A 177 ? 0.9693 0.6755 0.6398 0.0432  -0.2204 -0.0075 177 PHE A CZ  
1368 N N   . PRO A 178 ? 0.8850 0.5274 0.5605 0.0195  -0.2338 -0.0121 178 PRO A N   
1369 C CA  . PRO A 178 ? 0.8873 0.5196 0.5629 0.0150  -0.2356 -0.0105 178 PRO A CA  
1370 C C   . PRO A 178 ? 0.8914 0.5206 0.5669 0.0138  -0.2340 -0.0059 178 PRO A C   
1371 O O   . PRO A 178 ? 0.9814 0.6120 0.6548 0.0165  -0.2311 -0.0028 178 PRO A O   
1372 C CB  . PRO A 178 ? 0.8893 0.5141 0.5598 0.0144  -0.2361 -0.0115 178 PRO A CB  
1373 C CG  . PRO A 178 ? 0.8859 0.5167 0.5556 0.0178  -0.2359 -0.0154 178 PRO A CG  
1374 C CD  . PRO A 178 ? 0.8846 0.5265 0.5560 0.0216  -0.2336 -0.0149 178 PRO A CD  
1375 N N   . ALA A 179 ? 0.9077 0.5334 0.5862 0.0098  -0.2355 -0.0052 179 ALA A N   
1376 C CA  . ALA A 179 ? 0.9577 0.5802 0.6368 0.0082  -0.2338 -0.0015 179 ALA A CA  
1377 C C   . ALA A 179 ? 0.9577 0.5715 0.6333 0.0067  -0.2320 -0.0001 179 ALA A C   
1378 O O   . ALA A 179 ? 1.0127 0.6221 0.6854 0.0055  -0.2331 -0.0022 179 ALA A O   
1379 C CB  . ALA A 179 ? 0.9550 0.5767 0.6380 0.0042  -0.2359 -0.0016 179 ALA A CB  
1380 N N   . VAL A 180 ? 0.9695 0.5810 0.6460 0.0066  -0.2289 0.0034  180 VAL A N   
1381 C CA  . VAL A 180 ? 0.9783 0.5815 0.6537 0.0045  -0.2262 0.0046  180 VAL A CA  
1382 C C   . VAL A 180 ? 0.9876 0.5872 0.6664 -0.0003 -0.2259 0.0048  180 VAL A C   
1383 O O   . VAL A 180 ? 1.0192 0.6224 0.7009 -0.0002 -0.2260 0.0062  180 VAL A O   
1384 C CB  . VAL A 180 ? 1.0193 0.6229 0.6944 0.0088  -0.2215 0.0089  180 VAL A CB  
1385 C CG1 . VAL A 180 ? 1.0401 0.6475 0.7113 0.0131  -0.2217 0.0083  180 VAL A CG1 
1386 C CG2 . VAL A 180 ? 1.0048 0.6146 0.6832 0.0115  -0.2196 0.0126  180 VAL A CG2 
1387 N N   . LEU A 181 ? 0.9821 0.5754 0.6606 -0.0046 -0.2256 0.0028  181 LEU A N   
1388 C CA  . LEU A 181 ? 0.9961 0.5869 0.6779 -0.0096 -0.2249 0.0020  181 LEU A CA  
1389 C C   . LEU A 181 ? 1.0582 0.6441 0.7430 -0.0097 -0.2191 0.0043  181 LEU A C   
1390 O O   . LEU A 181 ? 0.9771 0.5580 0.6615 -0.0100 -0.2164 0.0039  181 LEU A O   
1391 C CB  . LEU A 181 ? 1.0167 0.6060 0.6977 -0.0148 -0.2277 -0.0020 181 LEU A CB  
1392 C CG  . LEU A 181 ? 0.9520 0.5414 0.6364 -0.0204 -0.2274 -0.0036 181 LEU A CG  
1393 C CD1 . LEU A 181 ? 0.9710 0.5656 0.6574 -0.0201 -0.2293 -0.0021 181 LEU A CD1 
1394 C CD2 . LEU A 181 ? 0.9788 0.5694 0.6622 -0.0251 -0.2303 -0.0073 181 LEU A CD2 
1395 N N   . GLN A 182 ? 1.1055 0.6927 0.7939 -0.0093 -0.2169 0.0067  182 GLN A N   
1396 C CA  . GLN A 182 ? 1.1320 0.7151 0.8247 -0.0087 -0.2107 0.0096  182 GLN A CA  
1397 C C   . GLN A 182 ? 1.1361 0.7136 0.8323 -0.0150 -0.2082 0.0060  182 GLN A C   
1398 O O   . GLN A 182 ? 1.1561 0.7347 0.8512 -0.0198 -0.2117 0.0016  182 GLN A O   
1399 C CB  . GLN A 182 ? 1.1391 0.7260 0.8347 -0.0063 -0.2095 0.0133  182 GLN A CB  
1400 C CG  . GLN A 182 ? 1.1280 0.7224 0.8212 -0.0003 -0.2113 0.0165  182 GLN A CG  
1401 C CD  . GLN A 182 ? 1.2146 0.8137 0.9108 0.0014  -0.2107 0.0195  182 GLN A CD  
1402 O OE1 . GLN A 182 ? 1.3242 0.9300 1.0201 0.0065  -0.2102 0.0229  182 GLN A OE1 
1403 N NE2 . GLN A 182 ? 1.2097 0.8062 0.9087 -0.0030 -0.2107 0.0179  182 GLN A NE2 
1404 N N   . SER A 183 ? 1.1219 0.6944 0.8232 -0.0148 -0.2016 0.0079  183 SER A N   
1405 C CA  . SER A 183 ? 1.0592 0.6273 0.7657 -0.0209 -0.1981 0.0038  183 SER A CA  
1406 C C   . SER A 183 ? 1.0072 0.5784 0.7158 -0.0250 -0.1996 0.0013  183 SER A C   
1407 O O   . SER A 183 ? 1.0015 0.5728 0.7121 -0.0312 -0.1997 -0.0040 183 SER A O   
1408 C CB  . SER A 183 ? 1.0455 0.6079 0.7592 -0.0195 -0.1896 0.0068  183 SER A CB  
1409 O OG  . SER A 183 ? 1.0517 0.6159 0.7680 -0.0146 -0.1870 0.0128  183 SER A OG  
1410 N N   . SER A 184 ? 0.9879 0.5626 0.6960 -0.0217 -0.2010 0.0050  184 SER A N   
1411 C CA  . SER A 184 ? 0.9991 0.5769 0.7089 -0.0251 -0.2025 0.0032  184 SER A CA  
1412 C C   . SER A 184 ? 1.0087 0.5917 0.7143 -0.0286 -0.2093 -0.0005 184 SER A C   
1413 O O   . SER A 184 ? 1.0067 0.5930 0.7134 -0.0318 -0.2108 -0.0021 184 SER A O   
1414 C CB  . SER A 184 ? 0.9783 0.5588 0.6886 -0.0204 -0.2024 0.0083  184 SER A CB  
1415 O OG  . SER A 184 ? 1.0151 0.6001 0.7206 -0.0154 -0.2065 0.0110  184 SER A OG  
1416 N N   . GLY A 185 ? 0.9972 0.5814 0.6983 -0.0278 -0.2130 -0.0015 185 GLY A N   
1417 C CA  . GLY A 185 ? 0.9958 0.5854 0.6938 -0.0304 -0.2189 -0.0040 185 GLY A CA  
1418 C C   . GLY A 185 ? 1.0068 0.6012 0.7023 -0.0266 -0.2234 -0.0013 185 GLY A C   
1419 O O   . GLY A 185 ? 0.9982 0.5971 0.6920 -0.0279 -0.2280 -0.0026 185 GLY A O   
1420 N N   . LEU A 186 ? 0.9785 0.5730 0.6747 -0.0220 -0.2219 0.0025  186 LEU A N   
1421 C CA  . LEU A 186 ? 0.9639 0.5637 0.6588 -0.0183 -0.2255 0.0044  186 LEU A CA  
1422 C C   . LEU A 186 ? 1.0129 0.6133 0.7049 -0.0134 -0.2258 0.0056  186 LEU A C   
1423 O O   . LEU A 186 ? 1.0455 0.6418 0.7365 -0.0119 -0.2227 0.0062  186 LEU A O   
1424 C CB  . LEU A 186 ? 1.0067 0.6082 0.7043 -0.0165 -0.2238 0.0074  186 LEU A CB  
1425 C CG  . LEU A 186 ? 0.9783 0.5788 0.6788 -0.0211 -0.2227 0.0062  186 LEU A CG  
1426 C CD1 . LEU A 186 ? 1.0289 0.6311 0.7319 -0.0189 -0.2213 0.0092  186 LEU A CD1 
1427 C CD2 . LEU A 186 ? 0.9777 0.5823 0.6777 -0.0254 -0.2271 0.0034  186 LEU A CD2 
1428 N N   . TYR A 187 ? 1.0359 0.6419 0.7271 -0.0110 -0.2293 0.0056  187 TYR A N   
1429 C CA  . TYR A 187 ? 1.0348 0.6430 0.7235 -0.0066 -0.2299 0.0057  187 TYR A CA  
1430 C C   . TYR A 187 ? 1.0383 0.6512 0.7279 -0.0015 -0.2278 0.0088  187 TYR A C   
1431 O O   . TYR A 187 ? 1.0807 0.6959 0.7729 -0.0013 -0.2269 0.0107  187 TYR A O   
1432 C CB  . TYR A 187 ? 1.0152 0.6277 0.7039 -0.0069 -0.2342 0.0033  187 TYR A CB  
1433 C CG  . TYR A 187 ? 0.9720 0.5817 0.6597 -0.0109 -0.2363 0.0009  187 TYR A CG  
1434 C CD1 . TYR A 187 ? 0.9369 0.5475 0.6267 -0.0154 -0.2379 0.0003  187 TYR A CD1 
1435 C CD2 . TYR A 187 ? 0.9482 0.5555 0.6327 -0.0100 -0.2368 -0.0008 187 TYR A CD2 
1436 C CE1 . TYR A 187 ? 0.9505 0.5608 0.6397 -0.0189 -0.2398 -0.0016 187 TYR A CE1 
1437 C CE2 . TYR A 187 ? 0.9613 0.5672 0.6451 -0.0136 -0.2388 -0.0029 187 TYR A CE2 
1438 C CZ  . TYR A 187 ? 0.9710 0.5789 0.6571 -0.0180 -0.2403 -0.0032 187 TYR A CZ  
1439 O OH  . TYR A 187 ? 0.9655 0.5741 0.6512 -0.0214 -0.2423 -0.0049 187 TYR A OH  
1440 N N   . SER A 188 ? 1.0024 0.6177 0.6896 0.0026  -0.2271 0.0091  188 SER A N   
1441 C CA  . SER A 188 ? 1.0491 0.6720 0.7368 0.0078  -0.2253 0.0117  188 SER A CA  
1442 C C   . SER A 188 ? 1.0847 0.7136 0.7704 0.0108  -0.2271 0.0091  188 SER A C   
1443 O O   . SER A 188 ? 1.0259 0.6507 0.7084 0.0105  -0.2276 0.0073  188 SER A O   
1444 C CB  . SER A 188 ? 1.1381 0.7586 0.8258 0.0105  -0.2203 0.0162  188 SER A CB  
1445 O OG  . SER A 188 ? 1.1222 0.7515 0.8115 0.0151  -0.2185 0.0198  188 SER A OG  
1446 N N   . LEU A 189 ? 1.0693 0.7082 0.7571 0.0136  -0.2278 0.0086  189 LEU A N   
1447 C CA  . LEU A 189 ? 1.0943 0.7403 0.7815 0.0159  -0.2292 0.0049  189 LEU A CA  
1448 C C   . LEU A 189 ? 1.1249 0.7837 0.8138 0.0205  -0.2275 0.0059  189 LEU A C   
1449 O O   . LEU A 189 ? 1.1442 0.8075 0.8361 0.0208  -0.2269 0.0081  189 LEU A O   
1450 C CB  . LEU A 189 ? 1.0816 0.7277 0.7719 0.0128  -0.2327 0.0007  189 LEU A CB  
1451 C CG  . LEU A 189 ? 1.0787 0.7319 0.7708 0.0146  -0.2338 -0.0041 189 LEU A CG  
1452 C CD1 . LEU A 189 ? 1.0340 0.6811 0.7271 0.0113  -0.2364 -0.0068 189 LEU A CD1 
1453 C CD2 . LEU A 189 ? 1.0967 0.7610 0.7945 0.0158  -0.2337 -0.0059 189 LEU A CD2 
1454 N N   . SER A 190 ? 1.0623 0.7281 0.7493 0.0239  -0.2269 0.0038  190 SER A N   
1455 C CA  . SER A 190 ? 1.0451 0.7260 0.7338 0.0281  -0.2253 0.0037  190 SER A CA  
1456 C C   . SER A 190 ? 1.0736 0.7627 0.7641 0.0287  -0.2267 -0.0031 190 SER A C   
1457 O O   . SER A 190 ? 1.0907 0.7749 0.7786 0.0282  -0.2276 -0.0060 190 SER A O   
1458 C CB  . SER A 190 ? 1.0113 0.6961 0.6964 0.0327  -0.2218 0.0086  190 SER A CB  
1459 O OG  . SER A 190 ? 1.0181 0.6978 0.6987 0.0333  -0.2216 0.0072  190 SER A OG  
1460 N N   . SER A 191 ? 1.0783 0.7801 0.7740 0.0294  -0.2268 -0.0059 191 SER A N   
1461 C CA  . SER A 191 ? 1.0766 0.7892 0.7759 0.0303  -0.2269 -0.0129 191 SER A CA  
1462 C C   . SER A 191 ? 1.1318 0.8629 0.8322 0.0345  -0.2245 -0.0131 191 SER A C   
1463 O O   . SER A 191 ? 1.2041 0.9418 0.9067 0.0353  -0.2238 -0.0098 191 SER A O   
1464 C CB  . SER A 191 ? 1.0642 0.7764 0.7710 0.0266  -0.2288 -0.0173 191 SER A CB  
1465 O OG  . SER A 191 ? 1.0435 0.7669 0.7555 0.0274  -0.2280 -0.0246 191 SER A OG  
1466 N N   . VAL A 192 ? 1.1114 0.8519 0.8104 0.0372  -0.2232 -0.0171 192 VAL A N   
1467 C CA  . VAL A 192 ? 1.1009 0.8611 0.8002 0.0415  -0.2207 -0.0172 192 VAL A CA  
1468 C C   . VAL A 192 ? 1.1301 0.9038 0.8343 0.0416  -0.2201 -0.0268 192 VAL A C   
1469 O O   . VAL A 192 ? 1.1527 0.9187 0.8588 0.0392  -0.2212 -0.0323 192 VAL A O   
1470 C CB  . VAL A 192 ? 1.1012 0.8620 0.7932 0.0458  -0.2185 -0.0112 192 VAL A CB  
1471 C CG1 . VAL A 192 ? 1.1064 0.8545 0.7955 0.0457  -0.2181 -0.0021 192 VAL A CG1 
1472 C CG2 . VAL A 192 ? 1.0817 0.8346 0.7693 0.0456  -0.2190 -0.0147 192 VAL A CG2 
1473 N N   . VAL A 193 ? 1.1614 0.9564 0.8683 0.0446  -0.2180 -0.0287 193 VAL A N   
1474 C CA  . VAL A 193 ? 1.1552 0.9666 0.8676 0.0448  -0.2166 -0.0386 193 VAL A CA  
1475 C C   . VAL A 193 ? 1.1280 0.9624 0.8385 0.0496  -0.2138 -0.0380 193 VAL A C   
1476 O O   . VAL A 193 ? 1.1325 0.9755 0.8422 0.0520  -0.2130 -0.0314 193 VAL A O   
1477 C CB  . VAL A 193 ? 1.1812 0.9968 0.9043 0.0409  -0.2171 -0.0452 193 VAL A CB  
1478 C CG1 . VAL A 193 ? 1.1696 0.9917 0.8952 0.0409  -0.2174 -0.0405 193 VAL A CG1 
1479 C CG2 . VAL A 193 ? 1.1820 1.0175 0.9121 0.0413  -0.2146 -0.0559 193 VAL A CG2 
1480 N N   . THR A 194 ? 1.1334 0.9781 0.8431 0.0513  -0.2121 -0.0444 194 THR A N   
1481 C CA  . THR A 194 ? 1.1391 1.0078 0.8469 0.0560  -0.2093 -0.0448 194 THR A CA  
1482 C C   . THR A 194 ? 1.1778 1.0694 0.8954 0.0548  -0.2075 -0.0559 194 THR A C   
1483 O O   . THR A 194 ? 1.1735 1.0647 0.8959 0.0523  -0.2070 -0.0659 194 THR A O   
1484 C CB  . THR A 194 ? 1.0731 0.9390 0.7733 0.0587  -0.2084 -0.0448 194 THR A CB  
1485 O OG1 . THR A 194 ? 1.0629 0.9173 0.7653 0.0554  -0.2094 -0.0532 194 THR A OG1 
1486 C CG2 . THR A 194 ? 1.1487 0.9972 0.8402 0.0607  -0.2091 -0.0332 194 THR A CG2 
1487 N N   . VAL A 195 ? 1.2194 1.1311 0.9405 0.0563  -0.2063 -0.0544 195 VAL A N   
1488 C CA  . VAL A 195 ? 1.2426 1.1780 0.9739 0.0548  -0.2044 -0.0650 195 VAL A CA  
1489 C C   . VAL A 195 ? 1.3270 1.2922 1.0564 0.0597  -0.2015 -0.0651 195 VAL A C   
1490 O O   . VAL A 195 ? 1.3316 1.2974 1.0524 0.0643  -0.2011 -0.0550 195 VAL A O   
1491 C CB  . VAL A 195 ? 1.2462 1.1817 0.9848 0.0518  -0.2057 -0.0642 195 VAL A CB  
1492 C CG1 . VAL A 195 ? 1.2174 1.1236 0.9568 0.0475  -0.2086 -0.0623 195 VAL A CG1 
1493 C CG2 . VAL A 195 ? 1.3145 1.2584 1.0488 0.0555  -0.2058 -0.0532 195 VAL A CG2 
1494 N N   . PRO A 196 ? 1.2870 1.2781 1.0246 0.0589  -0.1990 -0.0762 196 PRO A N   
1495 C CA  . PRO A 196 ? 1.2467 1.2699 0.9832 0.0635  -0.1962 -0.0758 196 PRO A CA  
1496 C C   . PRO A 196 ? 1.2789 1.3111 1.0147 0.0659  -0.1968 -0.0655 196 PRO A C   
1497 O O   . PRO A 196 ? 1.2747 1.3011 1.0164 0.0626  -0.1984 -0.0654 196 PRO A O   
1498 C CB  . PRO A 196 ? 1.2362 1.2836 0.9841 0.0605  -0.1934 -0.0917 196 PRO A CB  
1499 C CG  . PRO A 196 ? 1.2007 1.2290 0.9575 0.0544  -0.1948 -0.0985 196 PRO A CG  
1500 C CD  . PRO A 196 ? 1.2656 1.2587 1.0145 0.0539  -0.1979 -0.0902 196 PRO A CD  
1501 N N   . SER A 197 ? 1.3135 1.3603 1.0426 0.0719  -0.1952 -0.0562 197 SER A N   
1502 C CA  . SER A 197 ? 1.2757 1.3314 1.0042 0.0750  -0.1952 -0.0450 197 SER A CA  
1503 C C   . SER A 197 ? 1.2823 1.3653 1.0206 0.0733  -0.1944 -0.0520 197 SER A C   
1504 O O   . SER A 197 ? 1.3078 1.3916 1.0482 0.0736  -0.1954 -0.0452 197 SER A O   
1505 C CB  . SER A 197 ? 1.2028 1.2722 0.9238 0.0822  -0.1927 -0.0340 197 SER A CB  
1506 O OG  . SER A 197 ? 1.1069 1.2026 0.8280 0.0843  -0.1900 -0.0418 197 SER A OG  
1507 N N   . SER A 198 ? 1.2396 1.3455 0.9847 0.0715  -0.1923 -0.0659 198 SER A N   
1508 C CA  . SER A 198 ? 1.2529 1.3856 1.0087 0.0691  -0.1913 -0.0743 198 SER A CA  
1509 C C   . SER A 198 ? 1.2410 1.3545 1.0041 0.0631  -0.1937 -0.0779 198 SER A C   
1510 O O   . SER A 198 ? 1.2490 1.3778 1.0192 0.0616  -0.1938 -0.0794 198 SER A O   
1511 C CB  . SER A 198 ? 1.2593 1.4188 1.0218 0.0676  -0.1880 -0.0900 198 SER A CB  
1512 O OG  . SER A 198 ? 1.2210 1.3949 0.9965 0.0624  -0.1872 -0.1021 198 SER A OG  
1513 N N   . SER A 199 ? 1.2247 1.3056 0.9864 0.0596  -0.1957 -0.0791 199 SER A N   
1514 C CA  . SER A 199 ? 1.2807 1.3428 1.0494 0.0540  -0.1979 -0.0820 199 SER A CA  
1515 C C   . SER A 199 ? 1.3054 1.3550 1.0703 0.0550  -0.2006 -0.0693 199 SER A C   
1516 O O   . SER A 199 ? 1.3351 1.3770 1.1067 0.0508  -0.2022 -0.0714 199 SER A O   
1517 C CB  . SER A 199 ? 1.2649 1.2969 1.0328 0.0506  -0.1992 -0.0853 199 SER A CB  
1518 O OG  . SER A 199 ? 1.2727 1.3152 1.0478 0.0484  -0.1964 -0.0992 199 SER A OG  
1519 N N   . LEU A 200 ? 1.2817 1.3293 1.0369 0.0604  -0.2008 -0.0562 200 LEU A N   
1520 C CA  . LEU A 200 ? 1.2945 1.3295 1.0465 0.0615  -0.2027 -0.0440 200 LEU A CA  
1521 C C   . LEU A 200 ? 1.2921 1.3513 1.0514 0.0614  -0.2023 -0.0450 200 LEU A C   
1522 O O   . LEU A 200 ? 1.3009 1.3924 1.0644 0.0632  -0.2000 -0.0503 200 LEU A O   
1523 C CB  . LEU A 200 ? 1.2801 1.3106 1.0220 0.0677  -0.2017 -0.0302 200 LEU A CB  
1524 C CG  . LEU A 200 ? 1.2330 1.2392 0.9673 0.0679  -0.2021 -0.0281 200 LEU A CG  
1525 C CD1 . LEU A 200 ? 1.2758 1.2796 1.0017 0.0741  -0.2005 -0.0144 200 LEU A CD1 
1526 C CD2 . LEU A 200 ? 1.2666 1.2398 1.0009 0.0627  -0.2053 -0.0290 200 LEU A CD2 
1527 N N   . GLY A 201 ? 1.2601 1.3042 1.0209 0.0591  -0.2046 -0.0402 201 GLY A N   
1528 C CA  . GLY A 201 ? 1.2784 1.3423 1.0463 0.0583  -0.2048 -0.0413 201 GLY A CA  
1529 C C   . GLY A 201 ? 1.3869 1.4588 1.1663 0.0522  -0.2050 -0.0557 201 GLY A C   
1530 O O   . GLY A 201 ? 1.4003 1.4640 1.1847 0.0485  -0.2069 -0.0562 201 GLY A O   
1531 N N   . THR A 202 ? 1.4000 1.4877 1.1844 0.0509  -0.2026 -0.0677 202 THR A N   
1532 C CA  . THR A 202 ? 1.3136 1.4103 1.1110 0.0449  -0.2017 -0.0823 202 THR A CA  
1533 C C   . THR A 202 ? 1.3355 1.4001 1.1355 0.0398  -0.2034 -0.0857 202 THR A C   
1534 O O   . THR A 202 ? 1.3505 1.4093 1.1590 0.0352  -0.2043 -0.0899 202 THR A O   
1535 C CB  . THR A 202 ? 1.2686 1.3938 1.0715 0.0452  -0.1979 -0.0946 202 THR A CB  
1536 O OG1 . THR A 202 ? 1.2851 1.3932 1.0852 0.0444  -0.1972 -0.0987 202 THR A OG1 
1537 C CG2 . THR A 202 ? 1.2876 1.4414 1.0845 0.0516  -0.1963 -0.0884 202 THR A CG2 
1538 N N   . GLN A 203 ? 1.3287 1.3731 1.1218 0.0408  -0.2036 -0.0836 203 GLN A N   
1539 C CA  . GLN A 203 ? 1.4113 1.4261 1.2063 0.0365  -0.2052 -0.0855 203 GLN A CA  
1540 C C   . GLN A 203 ? 1.4078 1.3969 1.1962 0.0364  -0.2088 -0.0734 203 GLN A C   
1541 O O   . GLN A 203 ? 1.4101 1.3995 1.1902 0.0403  -0.2098 -0.0625 203 GLN A O   
1542 C CB  . GLN A 203 ? 1.3646 1.3677 1.1545 0.0376  -0.2043 -0.0874 203 GLN A CB  
1543 C CG  . GLN A 203 ? 1.3942 1.4209 1.1909 0.0374  -0.2004 -0.1003 203 GLN A CG  
1544 C CD  . GLN A 203 ? 1.4001 1.4236 1.2108 0.0317  -0.1984 -0.1131 203 GLN A CD  
1545 O OE1 . GLN A 203 ? 1.3524 1.3504 1.1650 0.0287  -0.2001 -0.1113 203 GLN A OE1 
1546 N NE2 . GLN A 203 ? 1.3511 1.4015 1.1726 0.0303  -0.1944 -0.1261 203 GLN A NE2 
1547 N N   . THR A 204 ? 1.3707 1.3382 1.1636 0.0318  -0.2103 -0.0754 204 THR A N   
1548 C CA  . THR A 204 ? 1.3945 1.3377 1.1825 0.0307  -0.2136 -0.0657 204 THR A CA  
1549 C C   . THR A 204 ? 1.4035 1.3196 1.1858 0.0298  -0.2149 -0.0630 204 THR A C   
1550 O O   . THR A 204 ? 1.4016 1.3093 1.1910 0.0262  -0.2144 -0.0698 204 THR A O   
1551 C CB  . THR A 204 ? 1.4163 1.3586 1.2145 0.0260  -0.2144 -0.0697 204 THR A CB  
1552 O OG1 . THR A 204 ? 1.3967 1.3679 1.2032 0.0258  -0.2125 -0.0764 204 THR A OG1 
1553 C CG2 . THR A 204 ? 1.3802 1.3050 1.1724 0.0259  -0.2176 -0.0588 204 THR A CG2 
1554 N N   . TYR A 205 ? 1.3882 1.2916 1.1588 0.0331  -0.2162 -0.0529 205 TYR A N   
1555 C CA  . TYR A 205 ? 1.3185 1.1977 1.0829 0.0325  -0.2174 -0.0498 205 TYR A CA  
1556 C C   . TYR A 205 ? 1.2885 1.1452 1.0497 0.0303  -0.2203 -0.0421 205 TYR A C   
1557 O O   . TYR A 205 ? 1.2933 1.1498 1.0505 0.0320  -0.2210 -0.0344 205 TYR A O   
1558 C CB  . TYR A 205 ? 1.2792 1.1591 1.0335 0.0372  -0.2165 -0.0447 205 TYR A CB  
1559 C CG  . TYR A 205 ? 1.2967 1.1970 1.0533 0.0392  -0.2137 -0.0527 205 TYR A CG  
1560 C CD1 . TYR A 205 ? 1.2437 1.1416 1.0059 0.0366  -0.2128 -0.0623 205 TYR A CD1 
1561 C CD2 . TYR A 205 ? 1.3045 1.2272 1.0582 0.0438  -0.2118 -0.0506 205 TYR A CD2 
1562 C CE1 . TYR A 205 ? 1.2199 1.1366 0.9846 0.0382  -0.2099 -0.0705 205 TYR A CE1 
1563 C CE2 . TYR A 205 ? 1.2683 1.2112 1.0241 0.0455  -0.2091 -0.0584 205 TYR A CE2 
1564 C CZ  . TYR A 205 ? 1.2403 1.1797 1.0014 0.0425  -0.2082 -0.0688 205 TYR A CZ  
1565 O OH  . TYR A 205 ? 1.2868 1.2464 1.0503 0.0440  -0.2052 -0.0774 205 TYR A OH  
1566 N N   . ILE A 206 ? 1.2868 1.1258 1.0504 0.0267  -0.2215 -0.0441 206 ILE A N   
1567 C CA  . ILE A 206 ? 1.2683 1.0867 1.0294 0.0241  -0.2241 -0.0379 206 ILE A CA  
1568 C C   . ILE A 206 ? 1.2823 1.0818 1.0388 0.0231  -0.2251 -0.0366 206 ILE A C   
1569 O O   . ILE A 206 ? 1.3065 1.1076 1.0659 0.0229  -0.2239 -0.0427 206 ILE A O   
1570 C CB  . ILE A 206 ? 1.2513 1.0704 1.0227 0.0198  -0.2248 -0.0419 206 ILE A CB  
1571 C CG1 . ILE A 206 ? 1.2912 1.0944 1.0592 0.0180  -0.2274 -0.0343 206 ILE A CG1 
1572 C CG2 . ILE A 206 ? 1.2588 1.0739 1.0389 0.0168  -0.2239 -0.0494 206 ILE A CG2 
1573 C CD1 . ILE A 206 ? 1.2791 1.0868 1.0560 0.0148  -0.2279 -0.0368 206 ILE A CD1 
1574 N N   . CYS A 207 ? 1.2897 1.0719 1.0392 0.0225  -0.2270 -0.0289 207 CYS A N   
1575 C CA  . CYS A 207 ? 1.3211 1.0855 1.0660 0.0212  -0.2282 -0.0271 207 CYS A CA  
1576 C C   . CYS A 207 ? 1.2798 1.0305 1.0275 0.0171  -0.2304 -0.0250 207 CYS A C   
1577 O O   . CYS A 207 ? 1.2637 1.0103 1.0093 0.0164  -0.2314 -0.0199 207 CYS A O   
1578 C CB  . CYS A 207 ? 1.2978 1.0548 1.0321 0.0241  -0.2281 -0.0204 207 CYS A CB  
1579 S SG  . CYS A 207 ? 1.4501 1.2050 1.1797 0.0256  -0.2280 -0.0114 207 CYS A SG  
1580 N N   . ASN A 208 ? 1.2792 1.0238 1.0320 0.0145  -0.2307 -0.0287 208 ASN A N   
1581 C CA  . ASN A 208 ? 1.2714 1.0046 1.0276 0.0107  -0.2325 -0.0266 208 ASN A CA  
1582 C C   . ASN A 208 ? 1.2271 0.9447 0.9758 0.0100  -0.2341 -0.0221 208 ASN A C   
1583 O O   . ASN A 208 ? 1.2304 0.9449 0.9785 0.0104  -0.2337 -0.0243 208 ASN A O   
1584 C CB  . ASN A 208 ? 1.2879 1.0253 1.0562 0.0086  -0.2313 -0.0327 208 ASN A CB  
1585 C CG  . ASN A 208 ? 1.2489 1.0034 1.0260 0.0090  -0.2292 -0.0389 208 ASN A CG  
1586 O OD1 . ASN A 208 ? 1.2968 1.0617 1.0703 0.0113  -0.2287 -0.0386 208 ASN A OD1 
1587 N ND2 . ASN A 208 ? 1.2104 0.9689 0.9999 0.0067  -0.2275 -0.0444 208 ASN A ND2 
1588 N N   . VAL A 209 ? 1.2157 0.9243 0.9590 0.0088  -0.2356 -0.0162 209 VAL A N   
1589 C CA  . VAL A 209 ? 1.2274 0.9223 0.9646 0.0072  -0.2370 -0.0124 209 VAL A CA  
1590 C C   . VAL A 209 ? 1.2540 0.9429 0.9961 0.0034  -0.2386 -0.0113 209 VAL A C   
1591 O O   . VAL A 209 ? 1.2767 0.9685 1.0233 0.0019  -0.2390 -0.0107 209 VAL A O   
1592 C CB  . VAL A 209 ? 1.1749 0.8641 0.9035 0.0082  -0.2369 -0.0070 209 VAL A CB  
1593 C CG1 . VAL A 209 ? 1.1399 0.8346 0.8638 0.0123  -0.2350 -0.0071 209 VAL A CG1 
1594 C CG2 . VAL A 209 ? 1.2546 0.9461 0.9848 0.0075  -0.2370 -0.0043 209 VAL A CG2 
1595 N N   . ASN A 210 ? 1.2162 0.8977 0.9578 0.0018  -0.2395 -0.0109 210 ASN A N   
1596 C CA  . ASN A 210 ? 1.2152 0.8924 0.9616 -0.0015 -0.2409 -0.0091 210 ASN A CA  
1597 C C   . ASN A 210 ? 1.2198 0.8874 0.9595 -0.0032 -0.2423 -0.0057 210 ASN A C   
1598 O O   . ASN A 210 ? 1.2068 0.8718 0.9447 -0.0025 -0.2423 -0.0068 210 ASN A O   
1599 C CB  . ASN A 210 ? 1.2376 0.9195 0.9945 -0.0017 -0.2397 -0.0127 210 ASN A CB  
1600 C CG  . ASN A 210 ? 1.3177 0.9977 1.0817 -0.0047 -0.2405 -0.0101 210 ASN A CG  
1601 O OD1 . ASN A 210 ? 1.3071 0.9841 1.0685 -0.0066 -0.2419 -0.0064 210 ASN A OD1 
1602 N ND2 . ASN A 210 ? 1.3404 1.0228 1.1141 -0.0049 -0.2391 -0.0119 210 ASN A ND2 
1603 N N   . HIS A 211 ? 1.2135 0.8765 0.9499 -0.0055 -0.2434 -0.0020 211 HIS A N   
1604 C CA  . HIS A 211 ? 1.1702 0.8258 0.9012 -0.0079 -0.2446 0.0006  211 HIS A CA  
1605 C C   . HIS A 211 ? 1.2139 0.8699 0.9500 -0.0111 -0.2460 0.0028  211 HIS A C   
1606 O O   . HIS A 211 ? 1.2769 0.9325 1.0128 -0.0130 -0.2464 0.0048  211 HIS A O   
1607 C CB  . HIS A 211 ? 1.1817 0.8325 0.9052 -0.0081 -0.2441 0.0025  211 HIS A CB  
1608 C CG  . HIS A 211 ? 1.1174 0.7617 0.8360 -0.0108 -0.2447 0.0040  211 HIS A CG  
1609 N ND1 . HIS A 211 ? 1.1346 0.7767 0.8528 -0.0143 -0.2454 0.0059  211 HIS A ND1 
1610 C CD2 . HIS A 211 ? 1.0647 0.7050 0.7789 -0.0107 -0.2446 0.0032  211 HIS A CD2 
1611 C CE1 . HIS A 211 ? 1.0832 0.7211 0.7974 -0.0165 -0.2455 0.0060  211 HIS A CE1 
1612 N NE2 . HIS A 211 ? 1.0263 0.6627 0.7381 -0.0143 -0.2451 0.0045  211 HIS A NE2 
1613 N N   . LYS A 212 ? 1.1927 0.8500 0.9338 -0.0115 -0.2463 0.0027  212 LYS A N   
1614 C CA  . LYS A 212 ? 1.1963 0.8558 0.9440 -0.0139 -0.2471 0.0055  212 LYS A CA  
1615 C C   . LYS A 212 ? 1.1888 0.8456 0.9315 -0.0172 -0.2487 0.0088  212 LYS A C   
1616 O O   . LYS A 212 ? 1.2202 0.8793 0.9662 -0.0193 -0.2492 0.0113  212 LYS A O   
1617 C CB  . LYS A 212 ? 1.1585 0.8205 0.9134 -0.0131 -0.2465 0.0052  212 LYS A CB  
1618 C CG  . LYS A 212 ? 1.1571 0.8242 0.9216 -0.0109 -0.2443 0.0018  212 LYS A CG  
1619 C CD  . LYS A 212 ? 1.1994 0.8672 0.9682 -0.0090 -0.2430 -0.0004 212 LYS A CD  
1620 C CE  . LYS A 212 ? 1.2531 0.9176 1.0126 -0.0071 -0.2433 -0.0033 212 LYS A CE  
1621 N NZ  . LYS A 212 ? 1.2111 0.8763 0.9747 -0.0052 -0.2419 -0.0059 212 LYS A NZ  
1622 N N   . PRO A 213 ? 1.1450 0.7976 0.8802 -0.0180 -0.2492 0.0086  213 PRO A N   
1623 C CA  . PRO A 213 ? 1.1429 0.7944 0.8741 -0.0216 -0.2502 0.0107  213 PRO A CA  
1624 C C   . PRO A 213 ? 1.1922 0.8428 0.9217 -0.0231 -0.2498 0.0113  213 PRO A C   
1625 O O   . PRO A 213 ? 1.1564 0.8088 0.8859 -0.0262 -0.2506 0.0132  213 PRO A O   
1626 C CB  . PRO A 213 ? 1.0936 0.7404 0.8175 -0.0218 -0.2499 0.0089  213 PRO A CB  
1627 C CG  . PRO A 213 ? 1.0785 0.7258 0.8045 -0.0190 -0.2499 0.0076  213 PRO A CG  
1628 C CD  . PRO A 213 ? 1.1531 0.8030 0.8846 -0.0161 -0.2488 0.0064  213 PRO A CD  
1629 N N   . SER A 214 ? 1.2617 0.9104 0.9898 -0.0208 -0.2486 0.0099  214 SER A N   
1630 C CA  . SER A 214 ? 1.3009 0.9489 1.0282 -0.0217 -0.2482 0.0107  214 SER A CA  
1631 C C   . SER A 214 ? 1.3774 1.0300 1.1114 -0.0207 -0.2484 0.0110  214 SER A C   
1632 O O   . SER A 214 ? 1.3752 1.0278 1.1091 -0.0215 -0.2483 0.0118  214 SER A O   
1633 C CB  . SER A 214 ? 1.2881 0.9318 1.0100 -0.0199 -0.2463 0.0096  214 SER A CB  
1634 O OG  . SER A 214 ? 1.2364 0.8822 0.9594 -0.0159 -0.2456 0.0082  214 SER A OG  
1635 N N   . ASN A 215 ? 1.5682 1.2248 1.3086 -0.0192 -0.2485 0.0103  215 ASN A N   
1636 C CA  . ASN A 215 ? 1.5683 1.2299 1.3168 -0.0184 -0.2481 0.0098  215 ASN A CA  
1637 C C   . ASN A 215 ? 1.6038 1.2666 1.3507 -0.0163 -0.2472 0.0078  215 ASN A C   
1638 O O   . ASN A 215 ? 1.7061 1.3711 1.4557 -0.0170 -0.2473 0.0083  215 ASN A O   
1639 C CB  . ASN A 215 ? 1.5695 1.2330 1.3222 -0.0213 -0.2491 0.0128  215 ASN A CB  
1640 C CG  . ASN A 215 ? 1.5745 1.2416 1.3350 -0.0219 -0.2491 0.0148  215 ASN A CG  
1641 O OD1 . ASN A 215 ? 1.7127 1.3836 1.4822 -0.0205 -0.2478 0.0137  215 ASN A OD1 
1642 N ND2 . ASN A 215 ? 1.5731 1.2401 1.3310 -0.0240 -0.2501 0.0177  215 ASN A ND2 
1643 N N   . THR A 216 ? 1.4332 1.0951 1.1756 -0.0137 -0.2462 0.0059  216 THR A N   
1644 C CA  . THR A 216 ? 1.3523 1.0166 1.0924 -0.0111 -0.2451 0.0048  216 THR A CA  
1645 C C   . THR A 216 ? 1.3007 0.9713 1.0442 -0.0080 -0.2438 0.0012  216 THR A C   
1646 O O   . THR A 216 ? 1.3080 0.9769 1.0479 -0.0064 -0.2433 0.0001  216 THR A O   
1647 C CB  . THR A 216 ? 1.3334 0.9918 1.0650 -0.0107 -0.2443 0.0066  216 THR A CB  
1648 O OG1 . THR A 216 ? 1.3378 0.9910 1.0671 -0.0141 -0.2450 0.0090  216 THR A OG1 
1649 C CG2 . THR A 216 ? 1.2833 0.9452 1.0135 -0.0078 -0.2428 0.0069  216 THR A CG2 
1650 N N   . LYS A 217 ? 1.3202 0.9985 1.0707 -0.0073 -0.2433 -0.0011 217 LYS A N   
1651 C CA  . LYS A 217 ? 1.3164 1.0032 1.0709 -0.0046 -0.2416 -0.0056 217 LYS A CA  
1652 C C   . LYS A 217 ? 1.3419 1.0361 1.0957 -0.0027 -0.2409 -0.0061 217 LYS A C   
1653 O O   . LYS A 217 ? 1.3661 1.0635 1.1242 -0.0040 -0.2413 -0.0058 217 LYS A O   
1654 C CB  . LYS A 217 ? 1.3224 1.0143 1.0883 -0.0057 -0.2409 -0.0090 217 LYS A CB  
1655 C CG  . LYS A 217 ? 1.2964 0.9986 1.0678 -0.0033 -0.2386 -0.0149 217 LYS A CG  
1656 C CD  . LYS A 217 ? 1.3168 1.0214 1.0991 -0.0041 -0.2370 -0.0185 217 LYS A CD  
1657 C CE  . LYS A 217 ? 1.3437 1.0468 1.1347 -0.0071 -0.2372 -0.0164 217 LYS A CE  
1658 N NZ  . LYS A 217 ? 1.3588 1.0632 1.1613 -0.0076 -0.2350 -0.0187 217 LYS A NZ  
1659 N N   . VAL A 218 ? 1.3663 1.0639 1.1150 0.0006  -0.2397 -0.0066 218 VAL A N   
1660 C CA  . VAL A 218 ? 1.3795 1.0857 1.1270 0.0031  -0.2387 -0.0061 218 VAL A CA  
1661 C C   . VAL A 218 ? 1.3416 1.0602 1.0918 0.0061  -0.2369 -0.0108 218 VAL A C   
1662 O O   . VAL A 218 ? 1.2830 1.0003 1.0311 0.0074  -0.2362 -0.0126 218 VAL A O   
1663 C CB  . VAL A 218 ? 1.3161 1.0159 1.0548 0.0046  -0.2382 -0.0007 218 VAL A CB  
1664 C CG1 . VAL A 218 ? 1.3526 1.0615 1.0915 0.0071  -0.2371 0.0010  218 VAL A CG1 
1665 C CG2 . VAL A 218 ? 1.2706 0.9579 1.0064 0.0012  -0.2395 0.0027  218 VAL A CG2 
1666 N N   . ASP A 219 ? 1.2967 1.0283 1.0517 0.0072  -0.2360 -0.0131 219 ASP A N   
1667 C CA  . ASP A 219 ? 1.2508 0.9976 1.0086 0.0101  -0.2341 -0.0179 219 ASP A CA  
1668 C C   . ASP A 219 ? 1.2906 1.0456 1.0433 0.0136  -0.2332 -0.0141 219 ASP A C   
1669 O O   . ASP A 219 ? 1.3201 1.0793 1.0746 0.0133  -0.2336 -0.0121 219 ASP A O   
1670 C CB  . ASP A 219 ? 1.2903 1.0485 1.0596 0.0082  -0.2333 -0.0247 219 ASP A CB  
1671 C CG  . ASP A 219 ? 1.3024 1.0524 1.0786 0.0048  -0.2336 -0.0272 219 ASP A CG  
1672 O OD1 . ASP A 219 ? 1.3323 1.0726 1.1091 0.0021  -0.2353 -0.0236 219 ASP A OD1 
1673 O OD2 . ASP A 219 ? 1.2607 1.0145 1.0421 0.0050  -0.2319 -0.0325 219 ASP A OD2 
1674 N N   . LYS A 220 ? 1.3275 1.0850 1.0742 0.0172  -0.2317 -0.0126 220 LYS A N   
1675 C CA  . LYS A 220 ? 1.2884 1.0531 1.0303 0.0212  -0.2303 -0.0074 220 LYS A CA  
1676 C C   . LYS A 220 ? 1.2530 1.0380 0.9972 0.0246  -0.2283 -0.0114 220 LYS A C   
1677 O O   . LYS A 220 ? 1.2698 1.0580 1.0148 0.0250  -0.2275 -0.0165 220 LYS A O   
1678 C CB  . LYS A 220 ? 1.2808 1.0323 1.0141 0.0228  -0.2296 -0.0011 220 LYS A CB  
1679 C CG  . LYS A 220 ? 1.2689 1.0233 0.9987 0.0262  -0.2278 0.0062  220 LYS A CG  
1680 C CD  . LYS A 220 ? 1.2356 0.9794 0.9656 0.0237  -0.2288 0.0103  220 LYS A CD  
1681 C CE  . LYS A 220 ? 1.1404 0.8864 0.8680 0.0273  -0.2263 0.0179  220 LYS A CE  
1682 N NZ  . LYS A 220 ? 1.0615 0.8274 0.7926 0.0306  -0.2252 0.0182  220 LYS A NZ  
1683 N N   . LYS A 221 ? 1.2327 1.0322 0.9782 0.0272  -0.2272 -0.0091 221 LYS A N   
1684 C CA  . LYS A 221 ? 1.2405 1.0626 0.9883 0.0306  -0.2252 -0.0125 221 LYS A CA  
1685 C C   . LYS A 221 ? 1.2128 1.0381 0.9533 0.0358  -0.2231 -0.0059 221 LYS A C   
1686 O O   . LYS A 221 ? 1.2007 1.0176 0.9366 0.0375  -0.2226 0.0026  221 LYS A O   
1687 C CB  . LYS A 221 ? 1.2557 1.0948 1.0096 0.0306  -0.2251 -0.0137 221 LYS A CB  
1688 C CG  . LYS A 221 ? 1.3686 1.1974 1.1262 0.0264  -0.2274 -0.0134 221 LYS A CG  
1689 C CD  . LYS A 221 ? 1.3368 1.1606 1.1017 0.0216  -0.2284 -0.0214 221 LYS A CD  
1690 C CE  . LYS A 221 ? 1.2702 1.0848 1.0389 0.0176  -0.2305 -0.0204 221 LYS A CE  
1691 N NZ  . LYS A 221 ? 1.2151 1.0243 0.9918 0.0132  -0.2311 -0.0270 221 LYS A NZ  
1692 N N   . VAL A 222 ? 1.1967 1.0345 0.9367 0.0382  -0.2214 -0.0098 222 VAL A N   
1693 C CA  . VAL A 222 ? 1.2090 1.0525 0.9427 0.0435  -0.2190 -0.0038 222 VAL A CA  
1694 C C   . VAL A 222 ? 1.2156 1.0872 0.9527 0.0473  -0.2170 -0.0042 222 VAL A C   
1695 O O   . VAL A 222 ? 1.2804 1.1694 1.0221 0.0469  -0.2164 -0.0128 222 VAL A O   
1696 C CB  . VAL A 222 ? 1.2002 1.0380 0.9301 0.0439  -0.2185 -0.0072 222 VAL A CB  
1697 C CG1 . VAL A 222 ? 1.2206 1.0647 0.9444 0.0495  -0.2158 -0.0003 222 VAL A CG1 
1698 C CG2 . VAL A 222 ? 1.1988 1.0108 0.9260 0.0400  -0.2207 -0.0070 222 VAL A CG2 
1699 N N   . GLU A 223 ? 1.1741 1.0512 0.9094 0.0509  -0.2156 0.0049  223 GLU A N   
1700 C CA  . GLU A 223 ? 1.1887 1.0936 0.9272 0.0549  -0.2137 0.0061  223 GLU A CA  
1701 C C   . GLU A 223 ? 1.2172 1.1306 0.9505 0.0613  -0.2104 0.0145  223 GLU A C   
1702 O O   . GLU A 223 ? 1.2283 1.1265 0.9575 0.0633  -0.2091 0.0241  223 GLU A O   
1703 C CB  . GLU A 223 ? 1.1836 1.0909 0.9256 0.0544  -0.2144 0.0105  223 GLU A CB  
1704 C CG  . GLU A 223 ? 1.1709 1.0699 0.9183 0.0482  -0.2175 0.0031  223 GLU A CG  
1705 C CD  . GLU A 223 ? 1.1854 1.1086 0.9409 0.0466  -0.2176 -0.0065 223 GLU A CD  
1706 O OE1 . GLU A 223 ? 1.1571 1.1052 0.9137 0.0504  -0.2155 -0.0075 223 GLU A OE1 
1707 O OE2 . GLU A 223 ? 1.2173 1.1353 0.9786 0.0415  -0.2196 -0.0133 223 GLU A OE2 
1708 N N   . PRO A 224 ? 1.2164 1.1545 0.9506 0.0646  -0.2084 0.0112  224 PRO A N   
1709 C CA  . PRO A 224 ? 1.2180 1.1671 0.9478 0.0710  -0.2050 0.0191  224 PRO A CA  
1710 C C   . PRO A 224 ? 1.1399 1.0937 0.8696 0.0759  -0.2025 0.0322  224 PRO A C   
1711 O O   . PRO A 224 ? 1.1465 1.1032 0.8803 0.0747  -0.2036 0.0336  224 PRO A O   
1712 C CB  . PRO A 224 ? 1.2139 1.1944 0.9469 0.0727  -0.2038 0.0112  224 PRO A CB  
1713 C CG  . PRO A 224 ? 1.2159 1.1924 0.9537 0.0663  -0.2064 -0.0024 224 PRO A CG  
1714 C CD  . PRO A 224 ? 1.1847 1.1418 0.9249 0.0620  -0.2091 -0.0013 224 PRO A CD  
1715 N N   . ASP B 1   ? 1.0645 0.7998 0.7708 -0.0298 -0.2896 0.0160  1   ASP B N   
1716 C CA  . ASP B 1   ? 1.1077 0.8386 0.8051 -0.0340 -0.2921 0.0085  1   ASP B CA  
1717 C C   . ASP B 1   ? 1.1574 0.8714 0.8509 -0.0300 -0.2922 0.0056  1   ASP B C   
1718 O O   . ASP B 1   ? 1.2087 0.9196 0.8960 -0.0324 -0.2944 0.0006  1   ASP B O   
1719 C CB  . ASP B 1   ? 1.1951 0.9475 0.8946 -0.0379 -0.2949 0.0106  1   ASP B CB  
1720 C CG  . ASP B 1   ? 1.3920 1.1571 1.1007 -0.0330 -0.2950 0.0202  1   ASP B CG  
1721 O OD1 . ASP B 1   ? 1.4793 1.2568 1.1966 -0.0310 -0.2934 0.0281  1   ASP B OD1 
1722 O OD2 . ASP B 1   ? 1.4032 1.1658 1.1111 -0.0310 -0.2965 0.0203  1   ASP B OD2 
1723 N N   . ILE B 2   ? 1.0893 0.7932 0.7871 -0.0240 -0.2896 0.0083  2   ILE B N   
1724 C CA  . ILE B 2   ? 1.0322 0.7192 0.7264 -0.0201 -0.2890 0.0046  2   ILE B CA  
1725 C C   . ILE B 2   ? 1.0069 0.6775 0.6941 -0.0204 -0.2873 -0.0019 2   ILE B C   
1726 O O   . ILE B 2   ? 1.0061 0.6748 0.6968 -0.0189 -0.2848 -0.0003 2   ILE B O   
1727 C CB  . ILE B 2   ? 1.0003 0.6873 0.7047 -0.0134 -0.2864 0.0108  2   ILE B CB  
1728 C CG1 . ILE B 2   ? 1.0661 0.7691 0.7775 -0.0125 -0.2879 0.0177  2   ILE B CG1 
1729 C CG2 . ILE B 2   ? 1.0128 0.6819 0.7135 -0.0095 -0.2850 0.0055  2   ILE B CG2 
1730 C CD1 . ILE B 2   ? 1.0614 0.7604 0.7808 -0.0061 -0.2856 0.0215  2   ILE B CD1 
1731 N N   . VAL B 3   ? 1.0092 0.6687 0.6867 -0.0224 -0.2885 -0.0089 3   VAL B N   
1732 C CA  . VAL B 3   ? 0.9966 0.6418 0.6671 -0.0229 -0.2869 -0.0147 3   VAL B CA  
1733 C C   . VAL B 3   ? 0.9472 0.5784 0.6155 -0.0176 -0.2854 -0.0172 3   VAL B C   
1734 O O   . VAL B 3   ? 1.0117 0.6399 0.6781 -0.0160 -0.2867 -0.0184 3   VAL B O   
1735 C CB  . VAL B 3   ? 0.8996 0.5424 0.5618 -0.0288 -0.2885 -0.0207 3   VAL B CB  
1736 C CG1 . VAL B 3   ? 0.8858 0.5155 0.5425 -0.0290 -0.2861 -0.0252 3   VAL B CG1 
1737 C CG2 . VAL B 3   ? 0.9576 0.6168 0.6230 -0.0344 -0.2899 -0.0191 3   VAL B CG2 
1738 N N   . MET B 4   ? 0.8856 0.5090 0.5541 -0.0149 -0.2826 -0.0183 4   MET B N   
1739 C CA  . MET B 4   ? 0.9544 0.5662 0.6212 -0.0100 -0.2806 -0.0215 4   MET B CA  
1740 C C   . MET B 4   ? 1.0101 0.6109 0.6673 -0.0112 -0.2799 -0.0271 4   MET B C   
1741 O O   . MET B 4   ? 1.0494 0.6498 0.7060 -0.0126 -0.2784 -0.0272 4   MET B O   
1742 C CB  . MET B 4   ? 0.9012 0.5148 0.5773 -0.0057 -0.2773 -0.0184 4   MET B CB  
1743 C CG  . MET B 4   ? 0.8770 0.5030 0.5645 -0.0048 -0.2771 -0.0112 4   MET B CG  
1744 S SD  . MET B 4   ? 0.9041 0.5318 0.5961 -0.0015 -0.2778 -0.0094 4   MET B SD  
1745 C CE  . MET B 4   ? 0.9325 0.5506 0.6299 0.0047  -0.2732 -0.0125 4   MET B CE  
1746 N N   . THR B 5   ? 0.9922 0.5842 0.6423 -0.0103 -0.2806 -0.0315 5   THR B N   
1747 C CA  . THR B 5   ? 1.0098 0.5916 0.6511 -0.0108 -0.2797 -0.0362 5   THR B CA  
1748 C C   . THR B 5   ? 1.0355 0.6093 0.6748 -0.0055 -0.2777 -0.0392 5   THR B C   
1749 O O   . THR B 5   ? 1.0386 0.6104 0.6778 -0.0031 -0.2785 -0.0405 5   THR B O   
1750 C CB  . THR B 5   ? 1.0779 0.6568 0.7121 -0.0151 -0.2821 -0.0392 5   THR B CB  
1751 O OG1 . THR B 5   ? 1.1566 0.7375 0.7914 -0.0144 -0.2845 -0.0391 5   THR B OG1 
1752 C CG2 . THR B 5   ? 1.0193 0.6058 0.6549 -0.0210 -0.2830 -0.0381 5   THR B CG2 
1753 N N   . GLN B 6   ? 1.0655 0.6360 0.7037 -0.0035 -0.2749 -0.0404 6   GLN B N   
1754 C CA  . GLN B 6   ? 1.0967 0.6620 0.7333 0.0014  -0.2725 -0.0437 6   GLN B CA  
1755 C C   . GLN B 6   ? 1.1360 0.6928 0.7622 0.0012  -0.2724 -0.0475 6   GLN B C   
1756 O O   . GLN B 6   ? 1.1327 0.6876 0.7549 -0.0019 -0.2724 -0.0471 6   GLN B O   
1757 C CB  . GLN B 6   ? 1.0374 0.6060 0.6794 0.0038  -0.2694 -0.0427 6   GLN B CB  
1758 C CG  . GLN B 6   ? 0.9592 0.5363 0.6120 0.0034  -0.2692 -0.0382 6   GLN B CG  
1759 C CD  . GLN B 6   ? 0.8900 0.4702 0.5488 0.0058  -0.2660 -0.0378 6   GLN B CD  
1760 O OE1 . GLN B 6   ? 0.8650 0.4514 0.5308 0.0046  -0.2657 -0.0339 6   GLN B OE1 
1761 N NE2 . GLN B 6   ? 0.8737 0.4506 0.5299 0.0091  -0.2636 -0.0420 6   GLN B NE2 
1762 N N   . SER B 7   ? 1.2456 0.7978 0.8682 0.0047  -0.2720 -0.0512 7   SER B N   
1763 C CA  . SER B 7   ? 1.2510 0.7954 0.8638 0.0046  -0.2721 -0.0544 7   SER B CA  
1764 C C   . SER B 7   ? 1.2494 0.7923 0.8587 0.0063  -0.2691 -0.0548 7   SER B C   
1765 O O   . SER B 7   ? 1.3331 0.8737 0.9392 0.0033  -0.2688 -0.0534 7   SER B O   
1766 C CB  . SER B 7   ? 1.2631 0.8035 0.8728 0.0077  -0.2726 -0.0582 7   SER B CB  
1767 O OG  . SER B 7   ? 1.2943 0.8280 0.8948 0.0088  -0.2720 -0.0613 7   SER B OG  
1768 N N   . PRO B 8   ? 1.1446 0.6898 0.7554 0.0108  -0.2663 -0.0567 8   PRO B N   
1769 C CA  . PRO B 8   ? 0.9862 0.5318 0.5936 0.0125  -0.2634 -0.0565 8   PRO B CA  
1770 C C   . PRO B 8   ? 0.9730 0.5238 0.5863 0.0110  -0.2623 -0.0528 8   PRO B C   
1771 O O   . PRO B 8   ? 1.0610 0.6177 0.6817 0.0124  -0.2614 -0.0523 8   PRO B O   
1772 C CB  . PRO B 8   ? 1.0041 0.5526 0.6117 0.0177  -0.2610 -0.0605 8   PRO B CB  
1773 C CG  . PRO B 8   ? 1.1357 0.6844 0.7478 0.0185  -0.2623 -0.0629 8   PRO B CG  
1774 C CD  . PRO B 8   ? 1.1131 0.6622 0.7300 0.0145  -0.2650 -0.0589 8   PRO B CD  
1775 N N   . LEU B 9   ? 0.9032 0.4516 0.5138 0.0082  -0.2619 -0.0502 9   LEU B N   
1776 C CA  . LEU B 9   ? 0.8995 0.4522 0.5152 0.0065  -0.2609 -0.0468 9   LEU B CA  
1777 C C   . LEU B 9   ? 0.9053 0.4627 0.5225 0.0105  -0.2577 -0.0467 9   LEU B C   
1778 O O   . LEU B 9   ? 0.9396 0.5028 0.5634 0.0107  -0.2570 -0.0453 9   LEU B O   
1779 C CB  . LEU B 9   ? 0.9652 0.5141 0.5785 0.0023  -0.2607 -0.0447 9   LEU B CB  
1780 C CG  . LEU B 9   ? 0.9539 0.5070 0.5728 -0.0007 -0.2602 -0.0415 9   LEU B CG  
1781 C CD1 . LEU B 9   ? 0.9164 0.4752 0.5417 -0.0023 -0.2627 -0.0407 9   LEU B CD1 
1782 C CD2 . LEU B 9   ? 1.0048 0.5542 0.6223 -0.0053 -0.2595 -0.0407 9   LEU B CD2 
1783 N N   . SER B 10  ? 0.9818 0.5379 0.5933 0.0137  -0.2556 -0.0481 10  SER B N   
1784 C CA  . SER B 10  ? 0.8853 0.4480 0.4979 0.0179  -0.2526 -0.0485 10  SER B CA  
1785 C C   . SER B 10  ? 0.8839 0.4475 0.4919 0.0219  -0.2516 -0.0527 10  SER B C   
1786 O O   . SER B 10  ? 0.8855 0.4428 0.4871 0.0217  -0.2525 -0.0539 10  SER B O   
1787 C CB  . SER B 10  ? 0.9762 0.5392 0.5870 0.0179  -0.2501 -0.0446 10  SER B CB  
1788 O OG  . SER B 10  ? 1.1826 0.7384 0.7873 0.0167  -0.2497 -0.0435 10  SER B OG  
1789 N N   . LEU B 11  ? 0.8915 0.4634 0.5031 0.0254  -0.2496 -0.0556 11  LEU B N   
1790 C CA  . LEU B 11  ? 0.8860 0.4608 0.4944 0.0292  -0.2483 -0.0607 11  LEU B CA  
1791 C C   . LEU B 11  ? 0.8778 0.4641 0.4881 0.0329  -0.2448 -0.0621 11  LEU B C   
1792 O O   . LEU B 11  ? 0.9912 0.5844 0.6093 0.0330  -0.2438 -0.0625 11  LEU B O   
1793 C CB  . LEU B 11  ? 0.9116 0.4858 0.5250 0.0292  -0.2496 -0.0651 11  LEU B CB  
1794 C CG  . LEU B 11  ? 0.9437 0.5187 0.5535 0.0323  -0.2486 -0.0711 11  LEU B CG  
1795 C CD1 . LEU B 11  ? 1.0717 0.6400 0.6706 0.0326  -0.2495 -0.0703 11  LEU B CD1 
1796 C CD2 . LEU B 11  ? 0.8695 0.4416 0.4849 0.0316  -0.2500 -0.0741 11  LEU B CD2 
1797 N N   . SER B 12  ? 0.8795 0.4687 0.4830 0.0361  -0.2429 -0.0627 12  SER B N   
1798 C CA  . SER B 12  ? 0.9714 0.5740 0.5760 0.0401  -0.2395 -0.0650 12  SER B CA  
1799 C C   . SER B 12  ? 1.0044 0.6109 0.6065 0.0429  -0.2386 -0.0721 12  SER B C   
1800 O O   . SER B 12  ? 1.0767 0.6777 0.6709 0.0438  -0.2392 -0.0724 12  SER B O   
1801 C CB  . SER B 12  ? 0.9917 0.5975 0.5910 0.0420  -0.2374 -0.0595 12  SER B CB  
1802 O OG  . SER B 12  ? 1.1370 0.7346 0.7282 0.0422  -0.2379 -0.0577 12  SER B OG  
1803 N N   . VAL B 13  ? 0.9411 0.5572 0.5507 0.0442  -0.2368 -0.0780 13  VAL B N   
1804 C CA  . VAL B 13  ? 0.9478 0.5688 0.5571 0.0467  -0.2352 -0.0860 13  VAL B CA  
1805 C C   . VAL B 13  ? 1.0019 0.6408 0.6144 0.0499  -0.2311 -0.0904 13  VAL B C   
1806 O O   . VAL B 13  ? 1.0185 0.6654 0.6379 0.0495  -0.2298 -0.0892 13  VAL B O   
1807 C CB  . VAL B 13  ? 0.9286 0.5446 0.5460 0.0448  -0.2360 -0.0905 13  VAL B CB  
1808 C CG1 . VAL B 13  ? 0.9728 0.5735 0.5853 0.0424  -0.2399 -0.0876 13  VAL B CG1 
1809 C CG2 . VAL B 13  ? 0.9535 0.5726 0.5819 0.0428  -0.2356 -0.0888 13  VAL B CG2 
1810 N N   . ALA B 14  ? 0.9740 0.6201 0.5816 0.0530  -0.2292 -0.0956 14  ALA B N   
1811 C CA  . ALA B 14  ? 0.9333 0.5989 0.5439 0.0560  -0.2251 -0.1006 14  ALA B CA  
1812 C C   . ALA B 14  ? 0.9833 0.6562 0.6062 0.0553  -0.2228 -0.1094 14  ALA B C   
1813 O O   . ALA B 14  ? 1.0037 0.6675 0.6304 0.0538  -0.2236 -0.1133 14  ALA B O   
1814 C CB  . ALA B 14  ? 0.9909 0.6632 0.5924 0.0596  -0.2236 -0.1037 14  ALA B CB  
1815 N N   . PRO B 15  ? 0.9845 0.6740 0.6147 0.0562  -0.2196 -0.1126 15  PRO B N   
1816 C CA  . PRO B 15  ? 0.9514 0.6488 0.5950 0.0552  -0.2165 -0.1217 15  PRO B CA  
1817 C C   . PRO B 15  ? 0.9440 0.6450 0.5879 0.0568  -0.2140 -0.1316 15  PRO B C   
1818 O O   . PRO B 15  ? 0.9626 0.6747 0.5997 0.0596  -0.2122 -0.1351 15  PRO B O   
1819 C CB  . PRO B 15  ? 0.9206 0.6377 0.5695 0.0563  -0.2133 -0.1233 15  PRO B CB  
1820 C CG  . PRO B 15  ? 1.0069 0.7290 0.6439 0.0589  -0.2142 -0.1163 15  PRO B CG  
1821 C CD  . PRO B 15  ? 0.9593 0.6608 0.5872 0.0577  -0.2185 -0.1074 15  PRO B CD  
1822 N N   . GLY B 16  ? 0.9561 0.6477 0.6081 0.0550  -0.2138 -0.1357 16  GLY B N   
1823 C CA  . GLY B 16  ? 1.0098 0.7020 0.6632 0.0562  -0.2114 -0.1448 16  GLY B CA  
1824 C C   . GLY B 16  ? 1.0639 0.7377 0.7088 0.0559  -0.2153 -0.1414 16  GLY B C   
1825 O O   . GLY B 16  ? 1.1863 0.8576 0.8338 0.0565  -0.2136 -0.1485 16  GLY B O   
1826 N N   . GLU B 17  ? 1.0004 0.6616 0.6357 0.0548  -0.2201 -0.1312 17  GLU B N   
1827 C CA  . GLU B 17  ? 1.0237 0.6681 0.6509 0.0540  -0.2239 -0.1278 17  GLU B CA  
1828 C C   . GLU B 17  ? 1.0041 0.6356 0.6389 0.0510  -0.2263 -0.1237 17  GLU B C   
1829 O O   . GLU B 17  ? 0.9668 0.6018 0.6126 0.0496  -0.2250 -0.1227 17  GLU B O   
1830 C CB  . GLU B 17  ? 1.0857 0.7246 0.6987 0.0544  -0.2272 -0.1197 17  GLU B CB  
1831 C CG  . GLU B 17  ? 1.0900 0.7348 0.6928 0.0576  -0.2260 -0.1233 17  GLU B CG  
1832 C CD  . GLU B 17  ? 1.1347 0.7686 0.7332 0.0577  -0.2274 -0.1273 17  GLU B CD  
1833 O OE1 . GLU B 17  ? 1.2011 0.8205 0.8012 0.0551  -0.2306 -0.1242 17  GLU B OE1 
1834 O OE2 . GLU B 17  ? 1.0174 0.6584 0.6111 0.0603  -0.2253 -0.1336 17  GLU B OE2 
1835 N N   . ALA B 18  ? 1.0186 0.6361 0.6477 0.0500  -0.2298 -0.1210 18  ALA B N   
1836 C CA  . ALA B 18  ? 1.0193 0.6263 0.6555 0.0475  -0.2319 -0.1175 18  ALA B CA  
1837 C C   . ALA B 18  ? 1.0054 0.6026 0.6351 0.0447  -0.2367 -0.1076 18  ALA B C   
1838 O O   . ALA B 18  ? 1.1068 0.6998 0.7246 0.0447  -0.2390 -0.1042 18  ALA B O   
1839 C CB  . ALA B 18  ? 1.0775 0.6768 0.7135 0.0481  -0.2322 -0.1218 18  ALA B CB  
1840 N N   . ALA B 19  ? 0.9390 0.5333 0.5775 0.0423  -0.2378 -0.1031 19  ALA B N   
1841 C CA  . ALA B 19  ? 0.9478 0.5337 0.5821 0.0392  -0.2420 -0.0945 19  ALA B CA  
1842 C C   . ALA B 19  ? 0.9824 0.5606 0.6218 0.0374  -0.2443 -0.0923 19  ALA B C   
1843 O O   . ALA B 19  ? 0.9911 0.5718 0.6415 0.0384  -0.2418 -0.0956 19  ALA B O   
1844 C CB  . ALA B 19  ? 0.9271 0.5187 0.5668 0.0378  -0.2415 -0.0900 19  ALA B CB  
1845 N N   . SER B 20  ? 1.0081 0.5777 0.6404 0.0347  -0.2486 -0.0867 20  SER B N   
1846 C CA  . SER B 20  ? 1.0002 0.5636 0.6358 0.0329  -0.2513 -0.0840 20  SER B CA  
1847 C C   . SER B 20  ? 0.9449 0.5050 0.5781 0.0290  -0.2550 -0.0766 20  SER B C   
1848 O O   . SER B 20  ? 1.0034 0.5572 0.6269 0.0270  -0.2581 -0.0747 20  SER B O   
1849 C CB  . SER B 20  ? 1.0342 0.5909 0.6623 0.0339  -0.2528 -0.0876 20  SER B CB  
1850 O OG  . SER B 20  ? 1.1790 0.7396 0.8098 0.0374  -0.2490 -0.0952 20  SER B OG  
1851 N N   . ILE B 21  ? 0.8837 0.4486 0.5263 0.0277  -0.2543 -0.0727 21  ILE B N   
1852 C CA  . ILE B 21  ? 0.8967 0.4601 0.5388 0.0238  -0.2575 -0.0661 21  ILE B CA  
1853 C C   . ILE B 21  ? 0.9058 0.4665 0.5508 0.0224  -0.2601 -0.0637 21  ILE B C   
1854 O O   . ILE B 21  ? 0.9211 0.4842 0.5756 0.0243  -0.2583 -0.0645 21  ILE B O   
1855 C CB  . ILE B 21  ? 0.8607 0.4308 0.5117 0.0231  -0.2558 -0.0628 21  ILE B CB  
1856 C CG1 . ILE B 21  ? 0.8617 0.4358 0.5105 0.0249  -0.2530 -0.0654 21  ILE B CG1 
1857 C CG2 . ILE B 21  ? 0.8676 0.4369 0.5174 0.0189  -0.2589 -0.0565 21  ILE B CG2 
1858 C CD1 . ILE B 21  ? 0.8604 0.4416 0.5186 0.0247  -0.2509 -0.0633 21  ILE B CD1 
1859 N N   . SER B 22  ? 0.9079 0.4643 0.5456 0.0190  -0.2639 -0.0608 22  SER B N   
1860 C CA  . SER B 22  ? 0.9017 0.4570 0.5411 0.0173  -0.2668 -0.0585 22  SER B CA  
1861 C C   . SER B 22  ? 0.9694 0.5295 0.6127 0.0134  -0.2690 -0.0523 22  SER B C   
1862 O O   . SER B 22  ? 1.0416 0.6023 0.6818 0.0110  -0.2693 -0.0506 22  SER B O   
1863 C CB  . SER B 22  ? 0.9555 0.5033 0.5837 0.0162  -0.2696 -0.0610 22  SER B CB  
1864 O OG  . SER B 22  ? 0.9427 0.4902 0.5731 0.0154  -0.2721 -0.0597 22  SER B OG  
1865 N N   . CYS B 23  ? 0.9926 0.5568 0.6431 0.0130  -0.2702 -0.0488 23  CYS B N   
1866 C CA  . CYS B 23  ? 0.9588 0.5299 0.6138 0.0095  -0.2721 -0.0428 23  CYS B CA  
1867 C C   . CYS B 23  ? 0.9421 0.5147 0.5962 0.0077  -0.2755 -0.0408 23  CYS B C   
1868 O O   . CYS B 23  ? 0.9357 0.5055 0.5904 0.0102  -0.2755 -0.0427 23  CYS B O   
1869 C CB  . CYS B 23  ? 0.9117 0.4904 0.5799 0.0114  -0.2693 -0.0389 23  CYS B CB  
1870 S SG  . CYS B 23  ? 1.0088 0.5984 0.6840 0.0077  -0.2712 -0.0308 23  CYS B SG  
1871 N N   . ARG B 24  ? 0.9502 0.5282 0.6032 0.0031  -0.2784 -0.0372 24  ARG B N   
1872 C CA  . ARG B 24  ? 1.0172 0.5992 0.6696 0.0008  -0.2818 -0.0353 24  ARG B CA  
1873 C C   . ARG B 24  ? 1.0657 0.6600 0.7242 -0.0025 -0.2831 -0.0293 24  ARG B C   
1874 O O   . ARG B 24  ? 1.0877 0.6844 0.7454 -0.0053 -0.2828 -0.0285 24  ARG B O   
1875 C CB  . ARG B 24  ? 1.0316 0.6066 0.6722 -0.0024 -0.2845 -0.0398 24  ARG B CB  
1876 C CG  . ARG B 24  ? 1.0661 0.6424 0.7055 -0.0030 -0.2875 -0.0397 24  ARG B CG  
1877 C CD  . ARG B 24  ? 1.0336 0.6059 0.6631 -0.0077 -0.2905 -0.0434 24  ARG B CD  
1878 N NE  . ARG B 24  ? 1.1638 0.7338 0.7905 -0.0071 -0.2930 -0.0450 24  ARG B NE  
1879 C CZ  . ARG B 24  ? 1.2496 0.8292 0.8811 -0.0082 -0.2954 -0.0414 24  ARG B CZ  
1880 N NH1 . ARG B 24  ? 1.1629 0.7557 0.8023 -0.0100 -0.2957 -0.0358 24  ARG B NH1 
1881 N NH2 . ARG B 24  ? 1.3011 0.8775 0.9294 -0.0074 -0.2975 -0.0433 24  ARG B NH2 
1882 N N   . SER B 25  ? 1.0183 0.6210 0.6831 -0.0021 -0.2845 -0.0249 25  SER B N   
1883 C CA  . SER B 25  ? 0.9565 0.5737 0.6278 -0.0050 -0.2859 -0.0186 25  SER B CA  
1884 C C   . SER B 25  ? 0.9736 0.5969 0.6406 -0.0089 -0.2899 -0.0186 25  SER B C   
1885 O O   . SER B 25  ? 0.9866 0.6044 0.6495 -0.0079 -0.2914 -0.0214 25  SER B O   
1886 C CB  . SER B 25  ? 0.9877 0.6131 0.6726 -0.0007 -0.2833 -0.0118 25  SER B CB  
1887 O OG  . SER B 25  ? 1.0751 0.6993 0.7634 0.0028  -0.2832 -0.0111 25  SER B OG  
1888 N N   . THR B 26  ? 0.9912 0.6268 0.6596 -0.0136 -0.2917 -0.0159 26  THR B N   
1889 C CA  . THR B 26  ? 0.9813 0.6258 0.6468 -0.0180 -0.2954 -0.0162 26  THR B CA  
1890 C C   . THR B 26  ? 1.0228 0.6766 0.6954 -0.0150 -0.2964 -0.0106 26  THR B C   
1891 O O   . THR B 26  ? 1.0312 0.6871 0.7002 -0.0166 -0.2993 -0.0122 26  THR B O   
1892 C CB  . THR B 26  ? 0.9694 0.6274 0.6362 -0.0237 -0.2964 -0.0148 26  THR B CB  
1893 O OG1 . THR B 26  ? 1.0184 0.6876 0.6952 -0.0215 -0.2945 -0.0074 26  THR B OG1 
1894 C CG2 . THR B 26  ? 0.9214 0.5699 0.5810 -0.0273 -0.2953 -0.0209 26  THR B CG2 
1895 N N   . GLN B 27  ? 1.0420 0.7017 0.7256 -0.0104 -0.2937 -0.0037 27  GLN B N   
1896 C CA  . GLN B 27  ? 0.9909 0.6611 0.6838 -0.0070 -0.2937 0.0032  27  GLN B CA  
1897 C C   . GLN B 27  ? 0.9832 0.6443 0.6837 -0.0002 -0.2895 0.0048  27  GLN B C   
1898 O O   . GLN B 27  ? 1.0089 0.6617 0.7108 0.0017  -0.2863 0.0029  27  GLN B O   
1899 C CB  . GLN B 27  ? 0.9559 0.6470 0.6578 -0.0084 -0.2939 0.0117  27  GLN B CB  
1900 C CG  . GLN B 27  ? 1.0910 0.7935 0.7866 -0.0157 -0.2975 0.0094  27  GLN B CG  
1901 C CD  . GLN B 27  ? 1.2528 0.9776 0.9571 -0.0171 -0.2975 0.0175  27  GLN B CD  
1902 O OE1 . GLN B 27  ? 1.3869 1.1217 1.1023 -0.0126 -0.2957 0.0263  27  GLN B OE1 
1903 N NE2 . GLN B 27  ? 1.1896 0.9229 0.8896 -0.0233 -0.2991 0.0145  27  GLN B NE2 
1904 N N   . SER B 28  ? 1.0023 0.6655 0.7083 0.0035  -0.2892 0.0080  28  SER B N   
1905 C CA  . SER B 28  ? 0.9664 0.6211 0.6808 0.0098  -0.2847 0.0085  28  SER B CA  
1906 C C   . SER B 28  ? 0.9700 0.6319 0.6986 0.0128  -0.2801 0.0155  28  SER B C   
1907 O O   . SER B 28  ? 1.0288 0.7068 0.7650 0.0121  -0.2804 0.0238  28  SER B O   
1908 C CB  . SER B 28  ? 0.8871 0.5441 0.6058 0.0129  -0.2851 0.0112  28  SER B CB  
1909 O OG  . SER B 28  ? 1.0918 0.7676 0.8207 0.0133  -0.2855 0.0214  28  SER B OG  
1910 N N   . LEU B 29  ? 0.9217 0.5725 0.6539 0.0161  -0.2757 0.0119  29  LEU B N   
1911 C CA  . LEU B 29  ? 0.9702 0.6257 0.7165 0.0191  -0.2706 0.0172  29  LEU B CA  
1912 C C   . LEU B 29  ? 1.0294 0.6860 0.7913 0.0251  -0.2656 0.0217  29  LEU B C   
1913 O O   . LEU B 29  ? 1.0373 0.6953 0.8124 0.0281  -0.2602 0.0248  29  LEU B O   
1914 C CB  . LEU B 29  ? 0.9466 0.5910 0.6886 0.0188  -0.2685 0.0103  29  LEU B CB  
1915 C CG  . LEU B 29  ? 0.9510 0.5926 0.6783 0.0133  -0.2726 0.0055  29  LEU B CG  
1916 C CD1 . LEU B 29  ? 0.8733 0.5036 0.5964 0.0137  -0.2703 -0.0013 29  LEU B CD1 
1917 C CD2 . LEU B 29  ? 0.9966 0.6526 0.7262 0.0098  -0.2746 0.0123  29  LEU B CD2 
1918 N N   . LEU B 30  ? 1.0208 0.6769 0.7821 0.0267  -0.2668 0.0220  30  LEU B N   
1919 C CA  . LEU B 30  ? 0.9954 0.6509 0.7713 0.0325  -0.2617 0.0253  30  LEU B CA  
1920 C C   . LEU B 30  ? 1.1056 0.7780 0.8984 0.0349  -0.2590 0.0383  30  LEU B C   
1921 O O   . LEU B 30  ? 1.1138 0.8002 0.9045 0.0321  -0.2627 0.0449  30  LEU B O   
1922 C CB  . LEU B 30  ? 0.9815 0.6315 0.7503 0.0331  -0.2645 0.0216  30  LEU B CB  
1923 C CG  . LEU B 30  ? 1.0332 0.6754 0.8107 0.0384  -0.2598 0.0195  30  LEU B CG  
1924 C CD1 . LEU B 30  ? 1.1307 0.7567 0.9028 0.0393  -0.2572 0.0079  30  LEU B CD1 
1925 C CD2 . LEU B 30  ? 0.9652 0.6084 0.7356 0.0380  -0.2644 0.0198  30  LEU B CD2 
1926 N N   . ASN B 31  ? 1.1868 0.8586 0.9973 0.0403  -0.2519 0.0419  31  ASN B N   
1927 C CA  . ASN B 31  ? 1.1234 0.8106 0.9523 0.0438  -0.2481 0.0550  31  ASN B CA  
1928 C C   . ASN B 31  ? 1.1919 0.8778 1.0317 0.0490  -0.2445 0.0576  31  ASN B C   
1929 O O   . ASN B 31  ? 1.1709 0.8435 1.0035 0.0496  -0.2450 0.0486  31  ASN B O   
1930 C CB  . ASN B 31  ? 1.1130 0.8030 0.9568 0.0456  -0.2419 0.0590  31  ASN B CB  
1931 C CG  . ASN B 31  ? 1.2517 0.9296 1.1079 0.0499  -0.2341 0.0534  31  ASN B CG  
1932 O OD1 . ASN B 31  ? 1.3317 0.9982 1.1843 0.0513  -0.2334 0.0455  31  ASN B OD1 
1933 N ND2 . ASN B 31  ? 1.2319 0.9132 1.1037 0.0517  -0.2280 0.0574  31  ASN B ND2 
1934 N N   . ARG B 32  ? 1.2240 0.9243 1.0815 0.0528  -0.2406 0.0705  32  ARG B N   
1935 C CA  . ARG B 32  ? 1.2258 0.9274 1.0950 0.0579  -0.2372 0.0750  32  ARG B CA  
1936 C C   . ARG B 32  ? 1.1891 0.8735 1.0649 0.0613  -0.2308 0.0658  32  ARG B C   
1937 O O   . ARG B 32  ? 1.1626 0.8392 1.0350 0.0630  -0.2313 0.0610  32  ARG B O   
1938 C CB  . ARG B 32  ? 1.2687 0.9884 1.1596 0.0623  -0.2320 0.0910  32  ARG B CB  
1939 C CG  . ARG B 32  ? 1.3002 1.0408 1.1872 0.0604  -0.2378 0.1017  32  ARG B CG  
1940 C CD  . ARG B 32  ? 1.3877 1.1356 1.2631 0.0547  -0.2429 0.1012  32  ARG B CD  
1941 N NE  . ARG B 32  ? 1.4487 1.1965 1.3361 0.0559  -0.2372 0.1041  32  ARG B NE  
1942 C CZ  . ARG B 32  ? 1.4114 1.1629 1.2914 0.0516  -0.2399 0.1029  32  ARG B CZ  
1943 N NH1 . ARG B 32  ? 1.3748 1.1305 1.2361 0.0457  -0.2479 0.0990  32  ARG B NH1 
1944 N NH2 . ARG B 32  ? 1.3844 1.1351 1.2765 0.0532  -0.2343 0.1056  32  ARG B NH2 
1945 N N   . ASN B 33  ? 1.1835 0.8625 1.0690 0.0623  -0.2248 0.0626  33  ASN B N   
1946 C CA  . ASN B 33  ? 1.2216 0.8866 1.1159 0.0654  -0.2177 0.0535  33  ASN B CA  
1947 C C   . ASN B 33  ? 1.2495 0.8994 1.1235 0.0627  -0.2224 0.0390  33  ASN B C   
1948 O O   . ASN B 33  ? 1.1812 0.8215 1.0584 0.0654  -0.2189 0.0322  33  ASN B O   
1949 C CB  . ASN B 33  ? 1.2270 0.8908 1.1340 0.0659  -0.2112 0.0521  33  ASN B CB  
1950 C CG  . ASN B 33  ? 1.3123 0.9917 1.2355 0.0674  -0.2081 0.0665  33  ASN B CG  
1951 O OD1 . ASN B 33  ? 1.3035 0.9891 1.2195 0.0639  -0.2119 0.0692  33  ASN B OD1 
1952 N ND2 . ASN B 33  ? 1.2742 0.9603 1.2197 0.0728  -0.2008 0.0761  33  ASN B ND2 
1953 N N   . GLY B 34  ? 1.2667 0.9145 1.1202 0.0573  -0.2300 0.0342  34  GLY B N   
1954 C CA  . GLY B 34  ? 1.2051 0.8389 1.0398 0.0547  -0.2338 0.0209  34  GLY B CA  
1955 C C   . GLY B 34  ? 1.1961 0.8254 1.0229 0.0514  -0.2345 0.0142  34  GLY B C   
1956 O O   . GLY B 34  ? 1.1946 0.8143 1.0041 0.0485  -0.2384 0.0044  34  GLY B O   
1957 N N   . ASP B 35  ? 1.3181 0.9546 1.1576 0.0518  -0.2305 0.0199  35  ASP B N   
1958 C CA  . ASP B 35  ? 1.3214 0.9547 1.1541 0.0488  -0.2311 0.0144  35  ASP B CA  
1959 C C   . ASP B 35  ? 1.3242 0.9611 1.1389 0.0436  -0.2394 0.0161  35  ASP B C   
1960 O O   . ASP B 35  ? 1.3226 0.9696 1.1359 0.0423  -0.2433 0.0245  35  ASP B O   
1961 C CB  . ASP B 35  ? 1.3233 0.9632 1.1751 0.0506  -0.2244 0.0199  35  ASP B CB  
1962 C CG  . ASP B 35  ? 1.3240 0.9613 1.1966 0.0555  -0.2151 0.0183  35  ASP B CG  
1963 O OD1 . ASP B 35  ? 1.3477 0.9764 1.2181 0.0571  -0.2136 0.0103  35  ASP B OD1 
1964 O OD2 . ASP B 35  ? 1.3246 0.9682 1.2160 0.0574  -0.2088 0.0242  35  ASP B OD2 
1965 N N   . ASN B 36  ? 1.1447 0.7743 0.9462 0.0405  -0.2417 0.0077  36  ASN B N   
1966 C CA  . ASN B 36  ? 0.9841 0.6156 0.7693 0.0354  -0.2486 0.0079  36  ASN B CA  
1967 C C   . ASN B 36  ? 0.9505 0.5866 0.7400 0.0338  -0.2470 0.0103  36  ASN B C   
1968 O O   . ASN B 36  ? 0.9800 0.6132 0.7791 0.0359  -0.2415 0.0072  36  ASN B O   
1969 C CB  . ASN B 36  ? 0.9830 0.6025 0.7496 0.0331  -0.2524 -0.0028 36  ASN B CB  
1970 C CG  . ASN B 36  ? 1.0331 0.6480 0.7938 0.0341  -0.2547 -0.0052 36  ASN B CG  
1971 O OD1 . ASN B 36  ? 1.0601 0.6770 0.8098 0.0310  -0.2605 -0.0037 36  ASN B OD1 
1972 N ND2 . ASN B 36  ? 1.0865 0.6955 0.8552 0.0382  -0.2499 -0.0092 36  ASN B ND2 
1973 N N   . TYR B 37  ? 0.9048 0.5490 0.6879 0.0301  -0.2516 0.0155  37  TYR B N   
1974 C CA  . TYR B 37  ? 0.9119 0.5616 0.6988 0.0284  -0.2505 0.0188  37  TYR B CA  
1975 C C   . TYR B 37  ? 0.8594 0.5009 0.6311 0.0247  -0.2534 0.0106  37  TYR B C   
1976 O O   . TYR B 37  ? 0.8751 0.5207 0.6380 0.0207  -0.2575 0.0121  37  TYR B O   
1977 C CB  . TYR B 37  ? 0.9733 0.6380 0.7631 0.0265  -0.2532 0.0292  37  TYR B CB  
1978 C CG  . TYR B 37  ? 0.9861 0.6613 0.7935 0.0306  -0.2495 0.0393  37  TYR B CG  
1979 C CD1 . TYR B 37  ? 1.0233 0.7012 0.8490 0.0342  -0.2426 0.0437  37  TYR B CD1 
1980 C CD2 . TYR B 37  ? 0.9619 0.6452 0.7684 0.0308  -0.2524 0.0446  37  TYR B CD2 
1981 C CE1 . TYR B 37  ? 1.1038 0.7916 0.9470 0.0383  -0.2384 0.0538  37  TYR B CE1 
1982 C CE2 . TYR B 37  ? 1.0296 0.7236 0.8530 0.0350  -0.2486 0.0547  37  TYR B CE2 
1983 C CZ  . TYR B 37  ? 1.1329 0.8289 0.9748 0.0389  -0.2415 0.0596  37  TYR B CZ  
1984 O OH  . TYR B 37  ? 1.1399 0.8467 0.9998 0.0434  -0.2370 0.0705  37  TYR B OH  
1985 N N   . LEU B 38  ? 0.8563 0.4871 0.6256 0.0264  -0.2508 0.0018  38  LEU B N   
1986 C CA  . LEU B 38  ? 0.8383 0.4617 0.5943 0.0238  -0.2528 -0.0056 38  LEU B CA  
1987 C C   . LEU B 38  ? 0.8375 0.4584 0.6017 0.0258  -0.2475 -0.0097 38  LEU B C   
1988 O O   . LEU B 38  ? 0.8396 0.4591 0.6153 0.0294  -0.2424 -0.0121 38  LEU B O   
1989 C CB  . LEU B 38  ? 0.8400 0.4537 0.5812 0.0231  -0.2559 -0.0132 38  LEU B CB  
1990 C CG  . LEU B 38  ? 0.8435 0.4500 0.5692 0.0203  -0.2586 -0.0198 38  LEU B CG  
1991 C CD1 . LEU B 38  ? 0.8447 0.4430 0.5587 0.0202  -0.2611 -0.0255 38  LEU B CD1 
1992 C CD2 . LEU B 38  ? 0.8437 0.4469 0.5714 0.0218  -0.2547 -0.0252 38  LEU B CD2 
1993 N N   . GLU B 39  ? 0.8394 0.4605 0.5981 0.0233  -0.2486 -0.0110 39  GLU B N   
1994 C CA  . GLU B 39  ? 0.8388 0.4588 0.6037 0.0246  -0.2442 -0.0152 39  GLU B CA  
1995 C C   . GLU B 39  ? 0.8419 0.4559 0.5916 0.0224  -0.2468 -0.0216 39  GLU B C   
1996 O O   . GLU B 39  ? 0.8541 0.4672 0.5917 0.0191  -0.2515 -0.0202 39  GLU B O   
1997 C CB  . GLU B 39  ? 0.8376 0.4661 0.6147 0.0241  -0.2421 -0.0080 39  GLU B CB  
1998 C CG  . GLU B 39  ? 0.8351 0.4702 0.6294 0.0269  -0.2385 -0.0006 39  GLU B CG  
1999 C CD  . GLU B 39  ? 0.8589 0.5029 0.6659 0.0267  -0.2361 0.0070  39  GLU B CD  
2000 O OE1 . GLU B 39  ? 0.8790 0.5246 0.6791 0.0236  -0.2387 0.0078  39  GLU B OE1 
2001 O OE2 . GLU B 39  ? 0.8307 0.4800 0.6548 0.0296  -0.2314 0.0127  39  GLU B OE2 
2002 N N   . TRP B 40  ? 0.8413 0.4523 0.5926 0.0243  -0.2433 -0.0289 40  TRP B N   
2003 C CA  . TRP B 40  ? 0.8439 0.4508 0.5824 0.0231  -0.2448 -0.0347 40  TRP B CA  
2004 C C   . TRP B 40  ? 0.8435 0.4547 0.5880 0.0227  -0.2421 -0.0351 40  TRP B C   
2005 O O   . TRP B 40  ? 0.8407 0.4555 0.5990 0.0248  -0.2372 -0.0366 40  TRP B O   
2006 C CB  . TRP B 40  ? 0.8437 0.4453 0.5773 0.0255  -0.2432 -0.0433 40  TRP B CB  
2007 C CG  . TRP B 40  ? 0.8447 0.4407 0.5690 0.0254  -0.2465 -0.0439 40  TRP B CG  
2008 C CD1 . TRP B 40  ? 0.8426 0.4375 0.5729 0.0275  -0.2453 -0.0438 40  TRP B CD1 
2009 C CD2 . TRP B 40  ? 0.8481 0.4386 0.5559 0.0231  -0.2512 -0.0449 40  TRP B CD2 
2010 N NE1 . TRP B 40  ? 0.8443 0.4336 0.5623 0.0265  -0.2495 -0.0448 40  TRP B NE1 
2011 C CE2 . TRP B 40  ? 0.8477 0.4342 0.5520 0.0238  -0.2530 -0.0456 40  TRP B CE2 
2012 C CE3 . TRP B 40  ? 0.8515 0.4402 0.5481 0.0207  -0.2536 -0.0452 40  TRP B CE3 
2013 C CZ2 . TRP B 40  ? 0.8505 0.4312 0.5405 0.0218  -0.2573 -0.0468 40  TRP B CZ2 
2014 C CZ3 . TRP B 40  ? 0.8543 0.4372 0.5376 0.0189  -0.2574 -0.0462 40  TRP B CZ3 
2015 C CH2 . TRP B 40  ? 0.8538 0.4328 0.5338 0.0193  -0.2592 -0.0471 40  TRP B CH2 
2016 N N   . TYR B 41  ? 0.8464 0.4570 0.5810 0.0201  -0.2451 -0.0340 41  TYR B N   
2017 C CA  . TYR B 41  ? 0.8464 0.4608 0.5848 0.0196  -0.2432 -0.0343 41  TYR B CA  
2018 C C   . TYR B 41  ? 0.8489 0.4603 0.5753 0.0194  -0.2440 -0.0397 41  TYR B C   
2019 O O   . TYR B 41  ? 0.8593 0.4656 0.5729 0.0183  -0.2472 -0.0405 41  TYR B O   
2020 C CB  . TYR B 41  ? 0.8473 0.4657 0.5874 0.0166  -0.2454 -0.0266 41  TYR B CB  
2021 C CG  . TYR B 41  ? 0.8447 0.4684 0.5978 0.0172  -0.2441 -0.0202 41  TYR B CG  
2022 C CD1 . TYR B 41  ? 0.8700 0.4942 0.6210 0.0165  -0.2469 -0.0158 41  TYR B CD1 
2023 C CD2 . TYR B 41  ? 0.8420 0.4711 0.6103 0.0185  -0.2398 -0.0182 41  TYR B CD2 
2024 C CE1 . TYR B 41  ? 0.8611 0.4917 0.6246 0.0174  -0.2455 -0.0089 41  TYR B CE1 
2025 C CE2 . TYR B 41  ? 0.8397 0.4742 0.6211 0.0194  -0.2380 -0.0114 41  TYR B CE2 
2026 C CZ  . TYR B 41  ? 0.8400 0.4756 0.6188 0.0190  -0.2409 -0.0064 41  TYR B CZ  
2027 O OH  . TYR B 41  ? 0.8703 0.5129 0.6627 0.0203  -0.2389 0.0014  41  TYR B OH  
2028 N N   . LEU B 42  ? 0.8477 0.4632 0.5793 0.0204  -0.2408 -0.0431 42  LEU B N   
2029 C CA  . LEU B 42  ? 0.8661 0.4814 0.5885 0.0208  -0.2407 -0.0477 42  LEU B CA  
2030 C C   . LEU B 42  ? 0.8787 0.4982 0.6034 0.0193  -0.2405 -0.0450 42  LEU B C   
2031 O O   . LEU B 42  ? 0.8521 0.4771 0.5890 0.0197  -0.2374 -0.0452 42  LEU B O   
2032 C CB  . LEU B 42  ? 0.8684 0.4867 0.5949 0.0239  -0.2366 -0.0559 42  LEU B CB  
2033 C CG  . LEU B 42  ? 0.9197 0.5396 0.6367 0.0254  -0.2360 -0.0617 42  LEU B CG  
2034 C CD1 . LEU B 42  ? 0.9181 0.5434 0.6430 0.0282  -0.2313 -0.0700 42  LEU B CD1 
2035 C CD2 . LEU B 42  ? 0.9255 0.5498 0.6399 0.0245  -0.2361 -0.0602 42  LEU B CD2 
2036 N N   . ARG B 43  ? 0.9060 0.5228 0.6196 0.0174  -0.2435 -0.0425 43  ARG B N   
2037 C CA  . ARG B 43  ? 0.9697 0.5900 0.6840 0.0160  -0.2434 -0.0402 43  ARG B CA  
2038 C C   . ARG B 43  ? 1.1276 0.7500 0.8358 0.0178  -0.2419 -0.0447 43  ARG B C   
2039 O O   . ARG B 43  ? 1.0300 0.6485 0.7269 0.0177  -0.2436 -0.0444 43  ARG B O   
2040 C CB  . ARG B 43  ? 0.9176 0.5346 0.6254 0.0126  -0.2470 -0.0342 43  ARG B CB  
2041 C CG  . ARG B 43  ? 0.9566 0.5767 0.6654 0.0112  -0.2468 -0.0317 43  ARG B CG  
2042 C CD  . ARG B 43  ? 0.9235 0.5420 0.6296 0.0075  -0.2497 -0.0259 43  ARG B CD  
2043 N NE  . ARG B 43  ? 0.9593 0.5727 0.6539 0.0059  -0.2515 -0.0258 43  ARG B NE  
2044 C CZ  . ARG B 43  ? 1.0215 0.6345 0.7117 0.0055  -0.2509 -0.0255 43  ARG B CZ  
2045 N NH1 . ARG B 43  ? 0.9780 0.5958 0.6734 0.0064  -0.2492 -0.0254 43  ARG B NH1 
2046 N NH2 . ARG B 43  ? 1.2112 0.8191 0.8923 0.0041  -0.2519 -0.0251 43  ARG B NH2 
2047 N N   . ARG B 44  ? 1.2788 0.9085 0.9955 0.0196  -0.2384 -0.0489 44  ARG B N   
2048 C CA  . ARG B 44  ? 1.2459 0.8808 0.9582 0.0214  -0.2367 -0.0531 44  ARG B CA  
2049 C C   . ARG B 44  ? 1.2487 0.8836 0.9550 0.0200  -0.2383 -0.0486 44  ARG B C   
2050 O O   . ARG B 44  ? 1.2544 0.8867 0.9625 0.0174  -0.2401 -0.0433 44  ARG B O   
2051 C CB  . ARG B 44  ? 1.2470 0.8915 0.9716 0.0230  -0.2324 -0.0590 44  ARG B CB  
2052 C CG  . ARG B 44  ? 1.2465 0.8931 0.9738 0.0254  -0.2297 -0.0662 44  ARG B CG  
2053 C CD  . ARG B 44  ? 1.3595 1.0180 1.0955 0.0270  -0.2250 -0.0738 44  ARG B CD  
2054 N NE  . ARG B 44  ? 1.3662 1.0275 1.1183 0.0269  -0.2212 -0.0773 44  ARG B NE  
2055 C CZ  . ARG B 44  ? 1.3599 1.0273 1.1250 0.0259  -0.2184 -0.0778 44  ARG B CZ  
2056 N NH1 . ARG B 44  ? 1.3474 1.0190 1.1107 0.0248  -0.2194 -0.0753 44  ARG B NH1 
2057 N NH2 . ARG B 44  ? 1.4134 1.0827 1.1942 0.0260  -0.2142 -0.0808 44  ARG B NH2 
2058 N N   . PRO B 45  ? 1.2220 0.8606 0.9216 0.0218  -0.2375 -0.0503 45  PRO B N   
2059 C CA  . PRO B 45  ? 1.1590 0.7977 0.8538 0.0207  -0.2385 -0.0457 45  PRO B CA  
2060 C C   . PRO B 45  ? 1.1489 0.7933 0.8527 0.0195  -0.2375 -0.0445 45  PRO B C   
2061 O O   . PRO B 45  ? 1.1133 0.7670 0.8237 0.0210  -0.2348 -0.0488 45  PRO B O   
2062 C CB  . PRO B 45  ? 1.1224 0.7663 0.8103 0.0238  -0.2368 -0.0481 45  PRO B CB  
2063 C CG  . PRO B 45  ? 1.1122 0.7632 0.8050 0.0262  -0.2343 -0.0554 45  PRO B CG  
2064 C CD  . PRO B 45  ? 1.1892 0.8330 0.8855 0.0250  -0.2353 -0.0562 45  PRO B CD  
2065 N N   . GLY B 46  ? 1.1467 0.7863 0.8511 0.0165  -0.2396 -0.0391 46  GLY B N   
2066 C CA  . GLY B 46  ? 1.1597 0.8036 0.8716 0.0151  -0.2391 -0.0371 46  GLY B CA  
2067 C C   . GLY B 46  ? 1.1172 0.7622 0.8406 0.0138  -0.2386 -0.0368 46  GLY B C   
2068 O O   . GLY B 46  ? 1.1074 0.7542 0.8364 0.0120  -0.2388 -0.0337 46  GLY B O   
2069 N N   . ARG B 47  ? 1.1211 0.7651 0.8485 0.0149  -0.2377 -0.0396 47  ARG B N   
2070 C CA  . ARG B 47  ? 1.1377 0.7835 0.8779 0.0143  -0.2362 -0.0391 47  ARG B CA  
2071 C C   . ARG B 47  ? 1.1023 0.7420 0.8411 0.0125  -0.2388 -0.0337 47  ARG B C   
2072 O O   . ARG B 47  ? 1.1117 0.7457 0.8397 0.0114  -0.2418 -0.0314 47  ARG B O   
2073 C CB  . ARG B 47  ? 1.1705 0.8207 0.9189 0.0168  -0.2324 -0.0460 47  ARG B CB  
2074 C CG  . ARG B 47  ? 1.2310 0.8897 0.9808 0.0185  -0.2296 -0.0524 47  ARG B CG  
2075 C CD  . ARG B 47  ? 1.2628 0.9286 1.0277 0.0196  -0.2247 -0.0587 47  ARG B CD  
2076 N NE  . ARG B 47  ? 1.3714 1.0480 1.1396 0.0205  -0.2218 -0.0650 47  ARG B NE  
2077 C CZ  . ARG B 47  ? 1.4458 1.1310 1.2277 0.0210  -0.2170 -0.0721 47  ARG B CZ  
2078 N NH1 . ARG B 47  ? 1.4563 1.1397 1.2507 0.0210  -0.2140 -0.0735 47  ARG B NH1 
2079 N NH2 . ARG B 47  ? 1.4257 1.1222 1.2096 0.0216  -0.2147 -0.0779 47  ARG B NH2 
2080 N N   . SER B 48  ? 0.9792 0.6211 0.7299 0.0122  -0.2374 -0.0315 48  SER B N   
2081 C CA  . SER B 48  ? 0.8923 0.5314 0.6443 0.0110  -0.2393 -0.0262 48  SER B CA  
2082 C C   . SER B 48  ? 0.8886 0.5251 0.6410 0.0130  -0.2385 -0.0291 48  SER B C   
2083 O O   . SER B 48  ? 0.9935 0.6310 0.7476 0.0153  -0.2359 -0.0355 48  SER B O   
2084 C CB  . SER B 48  ? 0.8729 0.5168 0.6384 0.0102  -0.2376 -0.0215 48  SER B CB  
2085 O OG  . SER B 48  ? 0.9845 0.6329 0.7632 0.0121  -0.2329 -0.0257 48  SER B OG  
2086 N N   . PRO B 49  ? 0.8484 0.4822 0.5991 0.0121  -0.2408 -0.0247 49  PRO B N   
2087 C CA  . PRO B 49  ? 0.8473 0.4784 0.5986 0.0140  -0.2402 -0.0272 49  PRO B CA  
2088 C C   . PRO B 49  ? 0.8456 0.4805 0.6124 0.0166  -0.2351 -0.0300 49  PRO B C   
2089 O O   . PRO B 49  ? 0.8408 0.4805 0.6204 0.0165  -0.2324 -0.0274 49  PRO B O   
2090 C CB  . PRO B 49  ? 0.8484 0.4786 0.5975 0.0122  -0.2434 -0.0206 49  PRO B CB  
2091 C CG  . PRO B 49  ? 0.8516 0.4816 0.5920 0.0090  -0.2467 -0.0174 49  PRO B CG  
2092 C CD  . PRO B 49  ? 0.9005 0.5341 0.6466 0.0091  -0.2444 -0.0180 49  PRO B CD  
2093 N N   . GLN B 50  ? 0.8421 0.4747 0.6082 0.0189  -0.2335 -0.0358 50  GLN B N   
2094 C CA  . GLN B 50  ? 0.8384 0.4737 0.6192 0.0213  -0.2283 -0.0393 50  GLN B CA  
2095 C C   . GLN B 50  ? 0.8382 0.4695 0.6183 0.0226  -0.2291 -0.0380 50  GLN B C   
2096 O O   . GLN B 50  ? 0.8451 0.4713 0.6113 0.0218  -0.2334 -0.0376 50  GLN B O   
2097 C CB  . GLN B 50  ? 0.8851 0.5232 0.6675 0.0230  -0.2246 -0.0490 50  GLN B CB  
2098 C CG  . GLN B 50  ? 0.9791 0.6216 0.7588 0.0219  -0.2246 -0.0509 50  GLN B CG  
2099 C CD  . GLN B 50  ? 1.0206 0.6671 0.7976 0.0236  -0.2221 -0.0603 50  GLN B CD  
2100 O OE1 . GLN B 50  ? 1.1064 0.7566 0.8774 0.0231  -0.2228 -0.0620 50  GLN B OE1 
2101 N NE2 . GLN B 50  ? 0.9113 0.5581 0.6933 0.0257  -0.2189 -0.0664 50  GLN B NE2 
2102 N N   . LEU B 51  ? 0.8351 0.4687 0.6308 0.0245  -0.2246 -0.0375 51  LEU B N   
2103 C CA  . LEU B 51  ? 0.8345 0.4650 0.6317 0.0261  -0.2247 -0.0361 51  LEU B CA  
2104 C C   . LEU B 51  ? 0.8334 0.4615 0.6301 0.0284  -0.2217 -0.0458 51  LEU B C   
2105 O O   . LEU B 51  ? 0.8310 0.4629 0.6385 0.0296  -0.2163 -0.0523 51  LEU B O   
2106 C CB  . LEU B 51  ? 0.8318 0.4665 0.6473 0.0273  -0.2209 -0.0294 51  LEU B CB  
2107 C CG  . LEU B 51  ? 0.8304 0.4631 0.6522 0.0298  -0.2190 -0.0287 51  LEU B CG  
2108 C CD1 . LEU B 51  ? 0.8327 0.4626 0.6411 0.0286  -0.2254 -0.0231 51  LEU B CD1 
2109 C CD2 . LEU B 51  ? 0.8273 0.4652 0.6713 0.0318  -0.2130 -0.0233 51  LEU B CD2 
2110 N N   . LEU B 52  ? 0.8351 0.4575 0.6195 0.0287  -0.2252 -0.0471 52  LEU B N   
2111 C CA  . LEU B 52  ? 0.8342 0.4541 0.6170 0.0310  -0.2228 -0.0559 52  LEU B CA  
2112 C C   . LEU B 52  ? 0.8325 0.4501 0.6237 0.0330  -0.2210 -0.0540 52  LEU B C   
2113 O O   . LEU B 52  ? 0.8295 0.4496 0.6359 0.0352  -0.2148 -0.0581 52  LEU B O   
2114 C CB  . LEU B 52  ? 0.8374 0.4524 0.6001 0.0303  -0.2275 -0.0593 52  LEU B CB  
2115 C CG  . LEU B 52  ? 0.8392 0.4566 0.5929 0.0291  -0.2287 -0.0622 52  LEU B CG  
2116 C CD1 . LEU B 52  ? 0.8417 0.4550 0.5791 0.0296  -0.2313 -0.0669 52  LEU B CD1 
2117 C CD2 . LEU B 52  ? 0.8363 0.4614 0.6026 0.0302  -0.2229 -0.0680 52  LEU B CD2 
2118 N N   . ILE B 53  ? 0.8342 0.4479 0.6166 0.0322  -0.2259 -0.0481 53  ILE B N   
2119 C CA  . ILE B 53  ? 0.8328 0.4444 0.6211 0.0342  -0.2250 -0.0459 53  ILE B CA  
2120 C C   . ILE B 53  ? 0.8325 0.4480 0.6271 0.0333  -0.2268 -0.0346 53  ILE B C   
2121 O O   . ILE B 53  ? 0.8346 0.4517 0.6205 0.0304  -0.2315 -0.0293 53  ILE B O   
2122 C CB  . ILE B 53  ? 0.8347 0.4394 0.6066 0.0341  -0.2294 -0.0495 53  ILE B CB  
2123 C CG1 . ILE B 53  ? 0.8349 0.4373 0.6008 0.0353  -0.2272 -0.0605 53  ILE B CG1 
2124 C CG2 . ILE B 53  ? 0.8333 0.4361 0.6110 0.0360  -0.2288 -0.0467 53  ILE B CG2 
2125 C CD1 . ILE B 53  ? 0.8315 0.4380 0.6143 0.0379  -0.2195 -0.0671 53  ILE B CD1 
2126 N N   . TYR B 54  ? 0.8300 0.4480 0.6402 0.0358  -0.2227 -0.0307 54  TYR B N   
2127 C CA  . TYR B 54  ? 0.8295 0.4527 0.6457 0.0356  -0.2243 -0.0194 54  TYR B CA  
2128 C C   . TYR B 54  ? 0.8281 0.4499 0.6494 0.0383  -0.2231 -0.0176 54  TYR B C   
2129 O O   . TYR B 54  ? 0.8266 0.4446 0.6543 0.0410  -0.2186 -0.0244 54  TYR B O   
2130 C CB  . TYR B 54  ? 0.8276 0.4584 0.6620 0.0362  -0.2194 -0.0132 54  TYR B CB  
2131 C CG  . TYR B 54  ? 0.8244 0.4566 0.6804 0.0396  -0.2106 -0.0159 54  TYR B CG  
2132 C CD1 . TYR B 54  ? 0.8224 0.4556 0.6917 0.0429  -0.2067 -0.0120 54  TYR B CD1 
2133 C CD2 . TYR B 54  ? 0.8234 0.4564 0.6873 0.0395  -0.2057 -0.0226 54  TYR B CD2 
2134 C CE1 . TYR B 54  ? 0.8197 0.4540 0.7103 0.0459  -0.1977 -0.0148 54  TYR B CE1 
2135 C CE2 . TYR B 54  ? 0.8204 0.4553 0.7054 0.0421  -0.1970 -0.0261 54  TYR B CE2 
2136 C CZ  . TYR B 54  ? 0.8187 0.4538 0.7173 0.0453  -0.1928 -0.0222 54  TYR B CZ  
2137 O OH  . TYR B 54  ? 0.8159 0.4527 0.7370 0.0479  -0.1832 -0.0259 54  TYR B OH  
2138 N N   . LEU B 55  ? 0.8285 0.4543 0.6470 0.0376  -0.2273 -0.0086 55  LEU B N   
2139 C CA  . LEU B 55  ? 0.8272 0.4528 0.6491 0.0399  -0.2273 -0.0055 55  LEU B CA  
2140 C C   . LEU B 55  ? 0.8283 0.4443 0.6366 0.0401  -0.2296 -0.0150 55  LEU B C   
2141 O O   . LEU B 55  ? 0.8268 0.4399 0.6410 0.0430  -0.2269 -0.0169 55  LEU B O   
2142 C CB  . LEU B 55  ? 0.8585 0.4881 0.7041 0.0442  -0.2192 -0.0017 55  LEU B CB  
2143 C CG  . LEU B 55  ? 0.8228 0.4635 0.6824 0.0448  -0.2176 0.0113  55  LEU B CG  
2144 C CD1 . LEU B 55  ? 0.8198 0.4636 0.7044 0.0494  -0.2085 0.0147  55  LEU B CD1 
2145 C CD2 . LEU B 55  ? 0.9288 0.5757 0.7798 0.0436  -0.2239 0.0199  55  LEU B CD2 
2146 N N   . GLY B 56  ? 0.8310 0.4420 0.6214 0.0370  -0.2343 -0.0207 56  GLY B N   
2147 C CA  . GLY B 56  ? 0.8378 0.4403 0.6133 0.0368  -0.2374 -0.0283 56  GLY B CA  
2148 C C   . GLY B 56  ? 0.8618 0.4589 0.6382 0.0388  -0.2330 -0.0392 56  GLY B C   
2149 O O   . GLY B 56  ? 0.8340 0.4257 0.5954 0.0375  -0.2358 -0.0460 56  GLY B O   
2150 N N   . SER B 57  ? 0.8596 0.4589 0.6540 0.0419  -0.2257 -0.0410 57  SER B N   
2151 C CA  . SER B 57  ? 0.8725 0.4684 0.6696 0.0439  -0.2208 -0.0522 57  SER B CA  
2152 C C   . SER B 57  ? 0.8698 0.4710 0.6843 0.0450  -0.2133 -0.0553 57  SER B C   
2153 O O   . SER B 57  ? 0.8777 0.4783 0.6921 0.0456  -0.2099 -0.0656 57  SER B O   
2154 C CB  . SER B 57  ? 0.8908 0.4828 0.6929 0.0469  -0.2183 -0.0550 57  SER B CB  
2155 O OG  . SER B 57  ? 0.8639 0.4602 0.6845 0.0492  -0.2143 -0.0469 57  SER B OG  
2156 N N   . GLU B 58  ? 0.8915 0.4987 0.7213 0.0453  -0.2105 -0.0471 58  GLU B N   
2157 C CA  . GLU B 58  ? 0.8869 0.4990 0.7359 0.0464  -0.2026 -0.0500 58  GLU B CA  
2158 C C   . GLU B 58  ? 0.8843 0.4987 0.7264 0.0439  -0.2038 -0.0544 58  GLU B C   
2159 O O   . GLU B 58  ? 0.8801 0.4957 0.7122 0.0413  -0.2093 -0.0483 58  GLU B O   
2160 C CB  . GLU B 58  ? 0.8922 0.5101 0.7600 0.0477  -0.1991 -0.0388 58  GLU B CB  
2161 C CG  . GLU B 58  ? 0.9538 0.5710 0.8321 0.0509  -0.1965 -0.0339 58  GLU B CG  
2162 C CD  . GLU B 58  ? 1.0304 0.6435 0.9171 0.0535  -0.1901 -0.0444 58  GLU B CD  
2163 O OE1 . GLU B 58  ? 1.0641 0.6803 0.9714 0.0552  -0.1813 -0.0478 58  GLU B OE1 
2164 O OE2 . GLU B 58  ? 1.0220 0.6291 0.8954 0.0539  -0.1935 -0.0494 58  GLU B OE2 
2165 N N   . ARG B 59  ? 0.8538 0.4698 0.7018 0.0445  -0.1984 -0.0651 59  ARG B N   
2166 C CA  . ARG B 59  ? 0.8226 0.4423 0.6658 0.0424  -0.1988 -0.0697 59  ARG B CA  
2167 C C   . ARG B 59  ? 0.8211 0.4470 0.6804 0.0417  -0.1952 -0.0640 59  ARG B C   
2168 O O   . ARG B 59  ? 0.8395 0.4680 0.7191 0.0435  -0.1890 -0.0610 59  ARG B O   
2169 C CB  . ARG B 59  ? 0.8212 0.4431 0.6663 0.0434  -0.1939 -0.0833 59  ARG B CB  
2170 C CG  . ARG B 59  ? 0.8400 0.4595 0.6630 0.0425  -0.1992 -0.0893 59  ARG B CG  
2171 C CD  . ARG B 59  ? 0.9343 0.5577 0.7605 0.0438  -0.1939 -0.1028 59  ARG B CD  
2172 N NE  . ARG B 59  ? 0.9764 0.5941 0.7970 0.0457  -0.1942 -0.1068 59  ARG B NE  
2173 C CZ  . ARG B 59  ? 1.0603 0.6796 0.8941 0.0478  -0.1873 -0.1150 59  ARG B CZ  
2174 N NH1 . ARG B 59  ? 1.0562 0.6828 0.9106 0.0481  -0.1790 -0.1204 59  ARG B NH1 
2175 N NH2 . ARG B 59  ? 1.0522 0.6656 0.8790 0.0494  -0.1884 -0.1180 59  ARG B NH2 
2176 N N   . ALA B 60  ? 0.8226 0.4508 0.6731 0.0392  -0.1989 -0.0623 60  ALA B N   
2177 C CA  . ALA B 60  ? 0.8213 0.4554 0.6856 0.0382  -0.1957 -0.0581 60  ALA B CA  
2178 C C   . ALA B 60  ? 0.8527 0.4923 0.7315 0.0387  -0.1880 -0.0686 60  ALA B C   
2179 O O   . ALA B 60  ? 0.9142 0.5539 0.7905 0.0395  -0.1856 -0.0793 60  ALA B O   
2180 C CB  . ALA B 60  ? 0.8239 0.4586 0.6737 0.0353  -0.2022 -0.0531 60  ALA B CB  
2181 N N   . LEU B 61  ? 0.8959 0.5409 0.7903 0.0379  -0.1838 -0.0657 61  LEU B N   
2182 C CA  . LEU B 61  ? 0.8794 0.5309 0.7895 0.0378  -0.1761 -0.0757 61  LEU B CA  
2183 C C   . LEU B 61  ? 0.9126 0.5678 0.8087 0.0357  -0.1794 -0.0828 61  LEU B C   
2184 O O   . LEU B 61  ? 0.8915 0.5461 0.7752 0.0338  -0.1853 -0.0768 61  LEU B O   
2185 C CB  . LEU B 61  ? 0.8577 0.5138 0.7900 0.0376  -0.1704 -0.0699 61  LEU B CB  
2186 C CG  . LEU B 61  ? 0.8080 0.4686 0.7661 0.0389  -0.1593 -0.0778 61  LEU B CG  
2187 C CD1 . LEU B 61  ? 0.8075 0.4636 0.7716 0.0418  -0.1560 -0.0790 61  LEU B CD1 
2188 C CD2 . LEU B 61  ? 0.8244 0.4892 0.8045 0.0386  -0.1538 -0.0709 61  LEU B CD2 
2189 N N   . GLY B 62  ? 1.0286 0.6884 0.9270 0.0361  -0.1751 -0.0954 62  GLY B N   
2190 C CA  . GLY B 62  ? 1.0239 0.6889 0.9090 0.0347  -0.1779 -0.1023 62  GLY B CA  
2191 C C   . GLY B 62  ? 1.0222 0.6821 0.8827 0.0351  -0.1851 -0.1024 62  GLY B C   
2192 O O   . GLY B 62  ? 1.0917 0.7557 0.9396 0.0342  -0.1881 -0.1058 62  GLY B O   
2193 N N   . VAL B 63  ? 0.9664 0.6180 0.8203 0.0365  -0.1878 -0.0986 63  VAL B N   
2194 C CA  . VAL B 63  ? 0.9617 0.6077 0.7932 0.0368  -0.1944 -0.0985 63  VAL B CA  
2195 C C   . VAL B 63  ? 0.9538 0.6018 0.7852 0.0387  -0.1907 -0.1099 63  VAL B C   
2196 O O   . VAL B 63  ? 0.9943 0.6405 0.8383 0.0403  -0.1860 -0.1124 63  VAL B O   
2197 C CB  . VAL B 63  ? 0.8709 0.5074 0.6947 0.0368  -0.1999 -0.0879 63  VAL B CB  
2198 C CG1 . VAL B 63  ? 0.8903 0.5207 0.6948 0.0375  -0.2049 -0.0900 63  VAL B CG1 
2199 C CG2 . VAL B 63  ? 0.8731 0.5088 0.6921 0.0346  -0.2047 -0.0777 63  VAL B CG2 
2200 N N   . PRO B 64  ? 0.8634 0.5157 0.6816 0.0387  -0.1924 -0.1167 64  PRO B N   
2201 C CA  . PRO B 64  ? 0.8972 0.5539 0.7162 0.0405  -0.1883 -0.1284 64  PRO B CA  
2202 C C   . PRO B 64  ? 0.9345 0.5814 0.7471 0.0422  -0.1901 -0.1274 64  PRO B C   
2203 O O   . PRO B 64  ? 0.9497 0.5870 0.7537 0.0419  -0.1957 -0.1179 64  PRO B O   
2204 C CB  . PRO B 64  ? 0.9725 0.6358 0.7753 0.0402  -0.1914 -0.1323 64  PRO B CB  
2205 C CG  . PRO B 64  ? 0.9997 0.6671 0.8048 0.0382  -0.1927 -0.1269 64  PRO B CG  
2206 C CD  . PRO B 64  ? 0.8802 0.5365 0.6856 0.0373  -0.1966 -0.1148 64  PRO B CD  
2207 N N   . ASP B 65  ? 0.9778 0.6284 0.7949 0.0438  -0.1852 -0.1382 65  ASP B N   
2208 C CA  . ASP B 65  ? 0.9868 0.6289 0.7993 0.0456  -0.1862 -0.1388 65  ASP B CA  
2209 C C   . ASP B 65  ? 1.0072 0.6423 0.7953 0.0456  -0.1942 -0.1349 65  ASP B C   
2210 O O   . ASP B 65  ? 1.0166 0.6423 0.7985 0.0465  -0.1971 -0.1318 65  ASP B O   
2211 C CB  . ASP B 65  ? 1.0041 0.6528 0.8264 0.0472  -0.1788 -0.1525 65  ASP B CB  
2212 C CG  . ASP B 65  ? 1.1936 0.8477 1.0426 0.0472  -0.1697 -0.1568 65  ASP B CG  
2213 O OD1 . ASP B 65  ? 1.2157 0.8710 1.0750 0.0458  -0.1689 -0.1503 65  ASP B OD1 
2214 O OD2 . ASP B 65  ? 1.2436 0.9009 1.1039 0.0485  -0.1630 -0.1669 65  ASP B OD2 
2215 N N   . ARG B 66  ? 0.9389 0.5787 0.7138 0.0447  -0.1976 -0.1349 66  ARG B N   
2216 C CA  . ARG B 66  ? 0.9488 0.5825 0.7020 0.0448  -0.2044 -0.1313 66  ARG B CA  
2217 C C   . ARG B 66  ? 0.9402 0.5621 0.6866 0.0435  -0.2106 -0.1195 66  ARG B C   
2218 O O   . ARG B 66  ? 0.9208 0.5341 0.6560 0.0438  -0.2145 -0.1173 66  ARG B O   
2219 C CB  . ARG B 66  ? 0.9197 0.5616 0.6629 0.0443  -0.2060 -0.1322 66  ARG B CB  
2220 C CG  . ARG B 66  ? 0.9152 0.5724 0.6696 0.0448  -0.1995 -0.1425 66  ARG B CG  
2221 C CD  . ARG B 66  ? 0.9933 0.6598 0.7370 0.0447  -0.2013 -0.1426 66  ARG B CD  
2222 N NE  . ARG B 66  ? 0.9650 0.6275 0.7051 0.0428  -0.2056 -0.1323 66  ARG B NE  
2223 C CZ  . ARG B 66  ? 0.9695 0.6392 0.7196 0.0414  -0.2036 -0.1315 66  ARG B CZ  
2224 N NH1 . ARG B 66  ? 0.9560 0.6379 0.7212 0.0415  -0.1972 -0.1405 66  ARG B NH1 
2225 N NH2 . ARG B 66  ? 0.8725 0.5376 0.6177 0.0397  -0.2078 -0.1220 66  ARG B NH2 
2226 N N   . PHE B 67  ? 0.9548 0.5771 0.7082 0.0417  -0.2114 -0.1121 67  PHE B N   
2227 C CA  . PHE B 67  ? 0.8410 0.4546 0.5895 0.0401  -0.2168 -0.1012 67  PHE B CA  
2228 C C   . PHE B 67  ? 0.8323 0.4403 0.5890 0.0413  -0.2156 -0.0995 67  PHE B C   
2229 O O   . PHE B 67  ? 0.9166 0.5280 0.6908 0.0426  -0.2096 -0.1024 67  PHE B O   
2230 C CB  . PHE B 67  ? 0.8369 0.4541 0.5934 0.0382  -0.2169 -0.0945 67  PHE B CB  
2231 C CG  . PHE B 67  ? 0.8530 0.4752 0.6013 0.0370  -0.2184 -0.0949 67  PHE B CG  
2232 C CD1 . PHE B 67  ? 0.8390 0.4566 0.5706 0.0357  -0.2242 -0.0900 67  PHE B CD1 
2233 C CD2 . PHE B 67  ? 0.8597 0.4920 0.6182 0.0372  -0.2136 -0.1004 67  PHE B CD2 
2234 C CE1 . PHE B 67  ? 0.8428 0.4652 0.5679 0.0349  -0.2251 -0.0898 67  PHE B CE1 
2235 C CE2 . PHE B 67  ? 0.8805 0.5183 0.6319 0.0364  -0.2150 -0.1004 67  PHE B CE2 
2236 C CZ  . PHE B 67  ? 0.8848 0.5175 0.6194 0.0354  -0.2207 -0.0948 67  PHE B CZ  
2237 N N   . SER B 68  ? 0.8346 0.4343 0.5792 0.0408  -0.2210 -0.0948 68  SER B N   
2238 C CA  . SER B 68  ? 0.8332 0.4279 0.5840 0.0422  -0.2203 -0.0932 68  SER B CA  
2239 C C   . SER B 68  ? 0.8756 0.4634 0.6146 0.0404  -0.2274 -0.0846 68  SER B C   
2240 O O   . SER B 68  ? 0.9482 0.5311 0.6708 0.0396  -0.2318 -0.0858 68  SER B O   
2241 C CB  . SER B 68  ? 0.8492 0.4426 0.5983 0.0446  -0.2174 -0.1031 68  SER B CB  
2242 O OG  . SER B 68  ? 0.9260 0.5170 0.6563 0.0442  -0.2214 -0.1064 68  SER B OG  
2243 N N   . GLY B 69  ? 0.8444 0.4330 0.5926 0.0397  -0.2280 -0.0760 69  GLY B N   
2244 C CA  . GLY B 69  ? 0.8369 0.4212 0.5760 0.0379  -0.2341 -0.0684 69  GLY B CA  
2245 C C   . GLY B 69  ? 0.8681 0.4480 0.6084 0.0397  -0.2342 -0.0688 69  GLY B C   
2246 O O   . GLY B 69  ? 0.9257 0.5064 0.6786 0.0426  -0.2288 -0.0726 69  GLY B O   
2247 N N   . SER B 70  ? 0.8676 0.4429 0.5951 0.0378  -0.2403 -0.0650 70  SER B N   
2248 C CA  . SER B 70  ? 0.8369 0.4079 0.5634 0.0392  -0.2415 -0.0649 70  SER B CA  
2249 C C   . SER B 70  ? 0.8798 0.4493 0.5954 0.0361  -0.2484 -0.0582 70  SER B C   
2250 O O   . SER B 70  ? 0.9308 0.5020 0.6393 0.0329  -0.2519 -0.0547 70  SER B O   
2251 C CB  . SER B 70  ? 0.8421 0.4072 0.5603 0.0410  -0.2405 -0.0748 70  SER B CB  
2252 O OG  . SER B 70  ? 0.9004 0.4637 0.6043 0.0394  -0.2428 -0.0789 70  SER B OG  
2253 N N   . GLY B 71  ? 0.8986 0.4656 0.6137 0.0369  -0.2502 -0.0567 71  GLY B N   
2254 C CA  . GLY B 71  ? 0.9766 0.5432 0.6821 0.0339  -0.2565 -0.0514 71  GLY B CA  
2255 C C   . GLY B 71  ? 0.9510 0.5256 0.6686 0.0341  -0.2566 -0.0419 71  GLY B C   
2256 O O   . GLY B 71  ? 0.9496 0.5306 0.6826 0.0360  -0.2522 -0.0377 71  GLY B O   
2257 N N   . SER B 72  ? 0.9960 0.5712 0.7069 0.0322  -0.2616 -0.0384 72  SER B N   
2258 C CA  . SER B 72  ? 1.0621 0.6468 0.7833 0.0325  -0.2622 -0.0290 72  SER B CA  
2259 C C   . SER B 72  ? 1.0947 0.6831 0.8047 0.0279  -0.2690 -0.0254 72  SER B C   
2260 O O   . SER B 72  ? 1.1259 0.7072 0.8212 0.0253  -0.2729 -0.0309 72  SER B O   
2261 C CB  . SER B 72  ? 1.1507 0.7342 0.8814 0.0367  -0.2594 -0.0285 72  SER B CB  
2262 O OG  . SER B 72  ? 1.1028 0.6964 0.8416 0.0370  -0.2607 -0.0187 72  SER B OG  
2263 N N   . GLY B 73  ? 1.1131 0.7137 0.8309 0.0268  -0.2701 -0.0163 73  GLY B N   
2264 C CA  . GLY B 73  ? 1.0452 0.6525 0.7546 0.0221  -0.2760 -0.0130 73  GLY B CA  
2265 C C   . GLY B 73  ? 0.9487 0.5575 0.6499 0.0173  -0.2784 -0.0141 73  GLY B C   
2266 O O   . GLY B 73  ? 0.9185 0.5355 0.6270 0.0168  -0.2769 -0.0089 73  GLY B O   
2267 N N   . ARG B 74  ? 0.9063 0.5069 0.5926 0.0139  -0.2818 -0.0207 74  ARG B N   
2268 C CA  . ARG B 74  ? 0.9701 0.5710 0.6484 0.0092  -0.2838 -0.0223 74  ARG B CA  
2269 C C   . ARG B 74  ? 0.9677 0.5566 0.6384 0.0098  -0.2819 -0.0293 74  ARG B C   
2270 O O   . ARG B 74  ? 0.9935 0.5834 0.6627 0.0078  -0.2813 -0.0293 74  ARG B O   
2271 C CB  . ARG B 74  ? 1.0281 0.6314 0.6965 0.0039  -0.2890 -0.0234 74  ARG B CB  
2272 C CG  . ARG B 74  ? 1.0006 0.6198 0.6758 0.0022  -0.2913 -0.0161 74  ARG B CG  
2273 C CD  . ARG B 74  ? 1.0192 0.6389 0.6878 0.0000  -0.2954 -0.0181 74  ARG B CD  
2274 N NE  . ARG B 74  ? 1.1042 0.7278 0.7644 -0.0067 -0.2991 -0.0208 74  ARG B NE  
2275 C CZ  . ARG B 74  ? 1.1594 0.7992 0.8227 -0.0106 -0.3016 -0.0166 74  ARG B CZ  
2276 N NH1 . ARG B 74  ? 1.1735 0.8274 0.8475 -0.0082 -0.3012 -0.0085 74  ARG B NH1 
2277 N NH2 . ARG B 74  ? 1.1838 0.8264 0.8399 -0.0170 -0.3042 -0.0206 74  ARG B NH2 
2278 N N   . ASP B 75  ? 0.9780 0.5567 0.6442 0.0127  -0.2808 -0.0352 75  ASP B N   
2279 C CA  . ASP B 75  ? 0.9965 0.5656 0.6557 0.0137  -0.2788 -0.0418 75  ASP B CA  
2280 C C   . ASP B 75  ? 0.9532 0.5221 0.6225 0.0185  -0.2735 -0.0430 75  ASP B C   
2281 O O   . ASP B 75  ? 0.9608 0.5313 0.6396 0.0219  -0.2712 -0.0418 75  ASP B O   
2282 C CB  . ASP B 75  ? 1.0251 0.5841 0.6726 0.0138  -0.2807 -0.0481 75  ASP B CB  
2283 C CG  . ASP B 75  ? 1.0353 0.5953 0.6756 0.0094  -0.2857 -0.0471 75  ASP B CG  
2284 O OD1 . ASP B 75  ? 1.0346 0.6009 0.6744 0.0051  -0.2877 -0.0439 75  ASP B OD1 
2285 O OD2 . ASP B 75  ? 1.1074 0.6623 0.7429 0.0100  -0.2875 -0.0499 75  ASP B OD2 
2286 N N   . PHE B 76  ? 0.9432 0.5105 0.6110 0.0187  -0.2712 -0.0455 76  PHE B N   
2287 C CA  . PHE B 76  ? 0.8997 0.4686 0.5779 0.0224  -0.2660 -0.0471 76  PHE B CA  
2288 C C   . PHE B 76  ? 0.9176 0.4817 0.5880 0.0229  -0.2644 -0.0532 76  PHE B C   
2289 O O   . PHE B 76  ? 0.9617 0.5241 0.6227 0.0199  -0.2668 -0.0531 76  PHE B O   
2290 C CB  . PHE B 76  ? 0.8729 0.4510 0.5632 0.0220  -0.2643 -0.0404 76  PHE B CB  
2291 C CG  . PHE B 76  ? 0.8730 0.4582 0.5729 0.0223  -0.2650 -0.0332 76  PHE B CG  
2292 C CD1 . PHE B 76  ? 0.9410 0.5285 0.6548 0.0264  -0.2607 -0.0318 76  PHE B CD1 
2293 C CD2 . PHE B 76  ? 0.9336 0.5246 0.6298 0.0185  -0.2694 -0.0278 76  PHE B CD2 
2294 C CE1 . PHE B 76  ? 0.9571 0.5524 0.6807 0.0271  -0.2610 -0.0241 76  PHE B CE1 
2295 C CE2 . PHE B 76  ? 1.0058 0.6057 0.7110 0.0189  -0.2700 -0.0206 76  PHE B CE2 
2296 C CZ  . PHE B 76  ? 0.9875 0.5895 0.7064 0.0235  -0.2658 -0.0183 76  PHE B CZ  
2297 N N   . THR B 77  ? 0.8855 0.4487 0.5609 0.0266  -0.2600 -0.0585 77  THR B N   
2298 C CA  . THR B 77  ? 0.8601 0.4209 0.5287 0.0276  -0.2582 -0.0646 77  THR B CA  
2299 C C   . THR B 77  ? 0.8481 0.4147 0.5287 0.0301  -0.2527 -0.0669 77  THR B C   
2300 O O   . THR B 77  ? 0.9009 0.4692 0.5926 0.0329  -0.2489 -0.0692 77  THR B O   
2301 C CB  . THR B 77  ? 0.9133 0.4675 0.5727 0.0294  -0.2584 -0.0713 77  THR B CB  
2302 O OG1 . THR B 77  ? 0.9586 0.5079 0.6103 0.0273  -0.2631 -0.0690 77  THR B OG1 
2303 C CG2 . THR B 77  ? 0.9733 0.5258 0.6223 0.0296  -0.2579 -0.0756 77  THR B CG2 
2304 N N   . LEU B 78  ? 0.8586 0.4285 0.5379 0.0291  -0.2521 -0.0665 78  LEU B N   
2305 C CA  . LEU B 78  ? 0.8476 0.4234 0.5364 0.0311  -0.2470 -0.0700 78  LEU B CA  
2306 C C   . LEU B 78  ? 0.8748 0.4499 0.5554 0.0330  -0.2453 -0.0779 78  LEU B C   
2307 O O   . LEU B 78  ? 0.9224 0.4950 0.5904 0.0319  -0.2479 -0.0777 78  LEU B O   
2308 C CB  . LEU B 78  ? 0.8485 0.4291 0.5406 0.0291  -0.2472 -0.0651 78  LEU B CB  
2309 C CG  . LEU B 78  ? 0.8468 0.4341 0.5474 0.0307  -0.2424 -0.0690 78  LEU B CG  
2310 C CD1 . LEU B 78  ? 0.8428 0.4344 0.5610 0.0327  -0.2375 -0.0701 78  LEU B CD1 
2311 C CD2 . LEU B 78  ? 0.8485 0.4392 0.5480 0.0284  -0.2436 -0.0646 78  LEU B CD2 
2312 N N   . LYS B 79  ? 0.8457 0.4238 0.5340 0.0360  -0.2407 -0.0847 79  LYS B N   
2313 C CA  . LYS B 79  ? 0.8668 0.4464 0.5483 0.0381  -0.2386 -0.0928 79  LYS B CA  
2314 C C   . LYS B 79  ? 0.8837 0.4732 0.5751 0.0394  -0.2333 -0.0977 79  LYS B C   
2315 O O   . LYS B 79  ? 0.9385 0.5320 0.6453 0.0401  -0.2293 -0.0987 79  LYS B O   
2316 C CB  . LYS B 79  ? 0.9048 0.4805 0.5859 0.0403  -0.2374 -0.0985 79  LYS B CB  
2317 C CG  . LYS B 79  ? 0.9644 0.5309 0.6374 0.0390  -0.2424 -0.0941 79  LYS B CG  
2318 C CD  . LYS B 79  ? 1.0678 0.6306 0.7412 0.0414  -0.2408 -0.1001 79  LYS B CD  
2319 C CE  . LYS B 79  ? 1.1820 0.7363 0.8468 0.0401  -0.2460 -0.0961 79  LYS B CE  
2320 N NZ  . LYS B 79  ? 1.3056 0.8557 0.9700 0.0425  -0.2447 -0.1020 79  LYS B NZ  
2321 N N   . ILE B 80  ? 0.8454 0.4394 0.5285 0.0398  -0.2331 -0.1004 80  ILE B N   
2322 C CA  . ILE B 80  ? 0.8433 0.4484 0.5338 0.0412  -0.2282 -0.1066 80  ILE B CA  
2323 C C   . ILE B 80  ? 0.9777 0.5865 0.6613 0.0437  -0.2261 -0.1152 80  ILE B C   
2324 O O   . ILE B 80  ? 0.9718 0.5785 0.6410 0.0441  -0.2290 -0.1142 80  ILE B O   
2325 C CB  . ILE B 80  ? 0.8469 0.4569 0.5342 0.0398  -0.2293 -0.1023 80  ILE B CB  
2326 C CG1 . ILE B 80  ? 0.9130 0.5178 0.6033 0.0370  -0.2325 -0.0930 80  ILE B CG1 
2327 C CG2 . ILE B 80  ? 0.9180 0.5408 0.6157 0.0409  -0.2241 -0.1084 80  ILE B CG2 
2328 C CD1 . ILE B 80  ? 0.9556 0.5625 0.6402 0.0354  -0.2346 -0.0879 80  ILE B CD1 
2329 N N   . SER B 81  ? 0.9806 0.5953 0.6754 0.0455  -0.2208 -0.1238 81  SER B N   
2330 C CA  . SER B 81  ? 0.9644 0.5831 0.6537 0.0479  -0.2185 -0.1328 81  SER B CA  
2331 C C   . SER B 81  ? 0.9859 0.6167 0.6688 0.0489  -0.2170 -0.1366 81  SER B C   
2332 O O   . SER B 81  ? 1.0712 0.7029 0.7412 0.0504  -0.2183 -0.1386 81  SER B O   
2333 C CB  . SER B 81  ? 1.0029 0.6254 0.7077 0.0492  -0.2124 -0.1414 81  SER B CB  
2334 O OG  . SER B 81  ? 1.0335 0.6669 0.7538 0.0488  -0.2072 -0.1450 81  SER B OG  
2335 N N   . ARG B 82  ? 0.9024 0.5436 0.5946 0.0482  -0.2143 -0.1372 82  ARG B N   
2336 C CA  . ARG B 82  ? 0.9354 0.5904 0.6232 0.0493  -0.2126 -0.1405 82  ARG B CA  
2337 C C   . ARG B 82  ? 0.9510 0.6073 0.6400 0.0474  -0.2146 -0.1326 82  ARG B C   
2338 O O   . ARG B 82  ? 0.9786 0.6400 0.6814 0.0462  -0.2117 -0.1336 82  ARG B O   
2339 C CB  . ARG B 82  ? 0.9725 0.6429 0.6723 0.0505  -0.2058 -0.1525 82  ARG B CB  
2340 C CG  . ARG B 82  ? 0.9880 0.6759 0.6860 0.0513  -0.2037 -0.1559 82  ARG B CG  
2341 C CD  . ARG B 82  ? 0.9910 0.6954 0.7022 0.0520  -0.1965 -0.1690 82  ARG B CD  
2342 N NE  . ARG B 82  ? 1.0594 0.7750 0.7614 0.0545  -0.1950 -0.1762 82  ARG B NE  
2343 C CZ  . ARG B 82  ? 1.0890 0.7996 0.7864 0.0559  -0.1945 -0.1812 82  ARG B CZ  
2344 N NH1 . ARG B 82  ? 1.1264 0.8213 0.8279 0.0552  -0.1954 -0.1798 82  ARG B NH1 
2345 N NH2 . ARG B 82  ? 1.0473 0.7698 0.7360 0.0581  -0.1931 -0.1873 82  ARG B NH2 
2346 N N   . VAL B 83  ? 0.8864 0.5379 0.5617 0.0472  -0.2190 -0.1249 83  VAL B N   
2347 C CA  . VAL B 83  ? 0.8941 0.5464 0.5697 0.0455  -0.2209 -0.1174 83  VAL B CA  
2348 C C   . VAL B 83  ? 0.8628 0.5324 0.5429 0.0466  -0.2172 -0.1218 83  VAL B C   
2349 O O   . VAL B 83  ? 0.9429 0.6235 0.6187 0.0490  -0.2149 -0.1278 83  VAL B O   
2350 C CB  . VAL B 83  ? 0.9724 0.6151 0.6332 0.0449  -0.2259 -0.1086 83  VAL B CB  
2351 C CG1 . VAL B 83  ? 0.9328 0.5745 0.5949 0.0428  -0.2278 -0.1008 83  VAL B CG1 
2352 C CG2 . VAL B 83  ? 1.0008 0.6286 0.6567 0.0438  -0.2293 -0.1060 83  VAL B CG2 
2353 N N   . GLU B 84  ? 0.8418 0.5148 0.5307 0.0449  -0.2166 -0.1190 84  GLU B N   
2354 C CA  . GLU B 84  ? 0.9081 0.5976 0.6021 0.0455  -0.2135 -0.1225 84  GLU B CA  
2355 C C   . GLU B 84  ? 0.9306 0.6178 0.6212 0.0440  -0.2165 -0.1132 84  GLU B C   
2356 O O   . GLU B 84  ? 1.0061 0.6796 0.6923 0.0423  -0.2204 -0.1050 84  GLU B O   
2357 C CB  . GLU B 84  ? 1.0122 0.7105 0.7242 0.0446  -0.2083 -0.1308 84  GLU B CB  
2358 C CG  . GLU B 84  ? 1.0193 0.7209 0.7363 0.0460  -0.2043 -0.1411 84  GLU B CG  
2359 C CD  . GLU B 84  ? 1.0259 0.7365 0.7626 0.0450  -0.1982 -0.1499 84  GLU B CD  
2360 O OE1 . GLU B 84  ? 1.0780 0.7957 0.8237 0.0435  -0.1967 -0.1492 84  GLU B OE1 
2361 O OE2 . GLU B 84  ? 0.9801 0.6906 0.7238 0.0457  -0.1945 -0.1577 84  GLU B OE2 
2362 N N   . ALA B 85  ? 0.9494 0.6514 0.6426 0.0447  -0.2143 -0.1148 85  ALA B N   
2363 C CA  . ALA B 85  ? 1.0287 0.7298 0.7183 0.0438  -0.2167 -0.1063 85  ALA B CA  
2364 C C   . ALA B 85  ? 1.0464 0.7380 0.7442 0.0406  -0.2183 -0.1015 85  ALA B C   
2365 O O   . ALA B 85  ? 1.0380 0.7210 0.7304 0.0392  -0.2217 -0.0929 85  ALA B O   
2366 C CB  . ALA B 85  ? 1.0671 0.7876 0.7595 0.0452  -0.2137 -0.1096 85  ALA B CB  
2367 N N   . GLN B 86  ? 1.0944 0.7877 0.8061 0.0395  -0.2155 -0.1070 86  GLN B N   
2368 C CA  . GLN B 86  ? 1.1117 0.7980 0.8327 0.0368  -0.2163 -0.1023 86  GLN B CA  
2369 C C   . GLN B 86  ? 1.0834 0.7529 0.7988 0.0354  -0.2206 -0.0949 86  GLN B C   
2370 O O   . GLN B 86  ? 1.0785 0.7421 0.7974 0.0331  -0.2225 -0.0885 86  GLN B O   
2371 C CB  . GLN B 86  ? 1.1023 0.7948 0.8408 0.0362  -0.2114 -0.1100 86  GLN B CB  
2372 C CG  . GLN B 86  ? 1.2029 0.9137 0.9480 0.0374  -0.2065 -0.1196 86  GLN B CG  
2373 C CD  . GLN B 86  ? 1.3024 1.0185 1.0521 0.0389  -0.2024 -0.1298 86  GLN B CD  
2374 O OE1 . GLN B 86  ? 1.2562 0.9632 0.9980 0.0401  -0.2041 -0.1293 86  GLN B OE1 
2375 N NE2 . GLN B 86  ? 1.2880 1.0192 1.0508 0.0388  -0.1967 -0.1398 86  GLN B NE2 
2376 N N   . ASP B 87  ? 0.9860 0.6487 0.6927 0.0366  -0.2220 -0.0957 87  ASP B N   
2377 C CA  . ASP B 87  ? 0.8914 0.5398 0.5938 0.0352  -0.2257 -0.0900 87  ASP B CA  
2378 C C   . ASP B 87  ? 1.0064 0.6471 0.6976 0.0336  -0.2302 -0.0813 87  ASP B C   
2379 O O   . ASP B 87  ? 1.0197 0.6497 0.7064 0.0321  -0.2335 -0.0768 87  ASP B O   
2380 C CB  . ASP B 87  ? 0.8975 0.5417 0.5942 0.0369  -0.2257 -0.0944 87  ASP B CB  
2381 C CG  . ASP B 87  ? 0.9586 0.6096 0.6673 0.0384  -0.2208 -0.1035 87  ASP B CG  
2382 O OD1 . ASP B 87  ? 0.9758 0.6356 0.6973 0.0379  -0.2171 -0.1068 87  ASP B OD1 
2383 O OD2 . ASP B 87  ? 0.9625 0.6103 0.6682 0.0398  -0.2203 -0.1078 87  ASP B OD2 
2384 N N   . VAL B 88  ? 1.0461 0.6926 0.7335 0.0338  -0.2302 -0.0790 88  VAL B N   
2385 C CA  . VAL B 88  ? 0.9605 0.6000 0.6384 0.0323  -0.2336 -0.0712 88  VAL B CA  
2386 C C   . VAL B 88  ? 0.9483 0.5809 0.6312 0.0290  -0.2359 -0.0655 88  VAL B C   
2387 O O   . VAL B 88  ? 1.0624 0.6986 0.7566 0.0281  -0.2344 -0.0663 88  VAL B O   
2388 C CB  . VAL B 88  ? 0.9354 0.5836 0.6100 0.0335  -0.2324 -0.0698 88  VAL B CB  
2389 C CG1 . VAL B 88  ? 0.8901 0.5446 0.5571 0.0369  -0.2308 -0.0733 88  VAL B CG1 
2390 C CG2 . VAL B 88  ? 1.0332 0.6923 0.7192 0.0334  -0.2298 -0.0726 88  VAL B CG2 
2391 N N   . GLY B 89  ? 0.9053 0.5287 0.5801 0.0270  -0.2392 -0.0598 89  GLY B N   
2392 C CA  . GLY B 89  ? 1.0132 0.6313 0.6914 0.0237  -0.2416 -0.0543 89  GLY B CA  
2393 C C   . GLY B 89  ? 0.8845 0.4930 0.5564 0.0218  -0.2448 -0.0517 89  GLY B C   
2394 O O   . GLY B 89  ? 0.8730 0.4779 0.5378 0.0231  -0.2452 -0.0541 89  GLY B O   
2395 N N   . THR B 90  ? 0.9132 0.5184 0.5877 0.0186  -0.2470 -0.0469 90  THR B N   
2396 C CA  . THR B 90  ? 1.0148 0.6130 0.6846 0.0163  -0.2500 -0.0445 90  THR B CA  
2397 C C   . THR B 90  ? 0.9748 0.5736 0.6529 0.0162  -0.2504 -0.0444 90  THR B C   
2398 O O   . THR B 90  ? 0.9067 0.5105 0.5952 0.0162  -0.2490 -0.0431 90  THR B O   
2399 C CB  . THR B 90  ? 1.0082 0.6040 0.6751 0.0125  -0.2521 -0.0393 90  THR B CB  
2400 O OG1 . THR B 90  ? 1.0121 0.6023 0.6740 0.0100  -0.2549 -0.0380 90  THR B OG1 
2401 C CG2 . THR B 90  ? 1.0363 0.6370 0.7123 0.0109  -0.2520 -0.0359 90  THR B CG2 
2402 N N   . TYR B 91  ? 1.0019 0.5958 0.6759 0.0163  -0.2520 -0.0456 91  TYR B N   
2403 C CA  . TYR B 91  ? 0.8598 0.4543 0.5414 0.0169  -0.2519 -0.0456 91  TYR B CA  
2404 C C   . TYR B 91  ? 0.8609 0.4533 0.5409 0.0136  -0.2555 -0.0406 91  TYR B C   
2405 O O   . TYR B 91  ? 0.9068 0.4949 0.5774 0.0112  -0.2580 -0.0397 91  TYR B O   
2406 C CB  . TYR B 91  ? 0.8586 0.4503 0.5375 0.0198  -0.2508 -0.0513 91  TYR B CB  
2407 C CG  . TYR B 91  ? 0.8938 0.4903 0.5766 0.0232  -0.2468 -0.0573 91  TYR B CG  
2408 C CD1 . TYR B 91  ? 0.8964 0.4954 0.5733 0.0240  -0.2457 -0.0592 91  TYR B CD1 
2409 C CD2 . TYR B 91  ? 0.8527 0.4522 0.5458 0.0255  -0.2436 -0.0612 91  TYR B CD2 
2410 C CE1 . TYR B 91  ? 0.9220 0.5278 0.6027 0.0269  -0.2420 -0.0651 91  TYR B CE1 
2411 C CE2 . TYR B 91  ? 0.8506 0.4559 0.5480 0.0281  -0.2395 -0.0678 91  TYR B CE2 
2412 C CZ  . TYR B 91  ? 0.8522 0.4613 0.5431 0.0287  -0.2389 -0.0699 91  TYR B CZ  
2413 O OH  . TYR B 91  ? 0.8498 0.4670 0.5453 0.0312  -0.2347 -0.0768 91  TYR B OH  
2414 N N   . TYR B 92  ? 0.8581 0.4544 0.5481 0.0136  -0.2553 -0.0374 92  TYR B N   
2415 C CA  . TYR B 92  ? 0.8585 0.4561 0.5487 0.0106  -0.2584 -0.0322 92  TYR B CA  
2416 C C   . TYR B 92  ? 0.8554 0.4543 0.5527 0.0125  -0.2580 -0.0313 92  TYR B C   
2417 O O   . TYR B 92  ? 0.8720 0.4724 0.5785 0.0157  -0.2545 -0.0333 92  TYR B O   
2418 C CB  . TYR B 92  ? 0.8584 0.4624 0.5548 0.0083  -0.2585 -0.0267 92  TYR B CB  
2419 C CG  . TYR B 92  ? 0.8615 0.4645 0.5520 0.0064  -0.2587 -0.0271 92  TYR B CG  
2420 C CD1 . TYR B 92  ? 0.8651 0.4655 0.5465 0.0029  -0.2613 -0.0262 92  TYR B CD1 
2421 C CD2 . TYR B 92  ? 0.8607 0.4659 0.5555 0.0081  -0.2559 -0.0284 92  TYR B CD2 
2422 C CE1 . TYR B 92  ? 0.8680 0.4673 0.5452 0.0013  -0.2608 -0.0263 92  TYR B CE1 
2423 C CE2 . TYR B 92  ? 0.8635 0.4681 0.5534 0.0067  -0.2559 -0.0282 92  TYR B CE2 
2424 C CZ  . TYR B 92  ? 0.8672 0.4685 0.5484 0.0034  -0.2583 -0.0269 92  TYR B CZ  
2425 O OH  . TYR B 92  ? 0.9333 0.5338 0.6106 0.0022  -0.2577 -0.0265 92  TYR B OH  
2426 N N   . CYS B 93  ? 0.8559 0.4548 0.5496 0.0103  -0.2613 -0.0286 93  CYS B N   
2427 C CA  . CYS B 93  ? 0.8530 0.4551 0.5544 0.0117  -0.2613 -0.0257 93  CYS B CA  
2428 C C   . CYS B 93  ? 0.8526 0.4633 0.5587 0.0089  -0.2632 -0.0183 93  CYS B C   
2429 O O   . CYS B 93  ? 0.8713 0.4833 0.5703 0.0050  -0.2661 -0.0170 93  CYS B O   
2430 C CB  . CYS B 93  ? 0.8535 0.4496 0.5469 0.0120  -0.2635 -0.0289 93  CYS B CB  
2431 S SG  . CYS B 93  ? 0.9145 0.5074 0.5934 0.0071  -0.2685 -0.0293 93  CYS B SG  
2432 N N   . LEU B 94  ? 0.8494 0.4667 0.5682 0.0110  -0.2613 -0.0133 94  LEU B N   
2433 C CA  . LEU B 94  ? 0.8485 0.4764 0.5738 0.0091  -0.2624 -0.0054 94  LEU B CA  
2434 C C   . LEU B 94  ? 0.8459 0.4792 0.5782 0.0108  -0.2626 -0.0008 94  LEU B C   
2435 O O   . LEU B 94  ? 0.8744 0.5050 0.6143 0.0147  -0.2595 -0.0019 94  LEU B O   
2436 C CB  . LEU B 94  ? 0.8471 0.4800 0.5838 0.0102  -0.2589 -0.0020 94  LEU B CB  
2437 C CG  . LEU B 94  ? 0.8455 0.4907 0.5921 0.0094  -0.2588 0.0070  94  LEU B CG  
2438 C CD1 . LEU B 94  ? 0.8480 0.4985 0.5861 0.0045  -0.2628 0.0091  94  LEU B CD1 
2439 C CD2 . LEU B 94  ? 0.8447 0.4930 0.6049 0.0118  -0.2542 0.0097  94  LEU B CD2 
2440 N N   . GLN B 95  ? 0.8460 0.4881 0.5767 0.0078  -0.2660 0.0044  95  GLN B N   
2441 C CA  . GLN B 95  ? 0.8711 0.5215 0.6095 0.0094  -0.2663 0.0104  95  GLN B CA  
2442 C C   . GLN B 95  ? 0.8756 0.5389 0.6274 0.0103  -0.2641 0.0195  95  GLN B C   
2443 O O   . GLN B 95  ? 0.8533 0.5223 0.6036 0.0072  -0.2652 0.0217  95  GLN B O   
2444 C CB  . GLN B 95  ? 0.8839 0.5382 0.6126 0.0057  -0.2713 0.0104  95  GLN B CB  
2445 C CG  . GLN B 95  ? 0.8891 0.5518 0.6124 0.0004  -0.2743 0.0121  95  GLN B CG  
2446 C CD  . GLN B 95  ? 0.9330 0.6134 0.6643 -0.0004 -0.2754 0.0209  95  GLN B CD  
2447 O OE1 . GLN B 95  ? 1.0158 0.7018 0.7557 0.0030  -0.2743 0.0261  95  GLN B OE1 
2448 N NE2 . GLN B 95  ? 1.0477 0.7381 0.7769 -0.0047 -0.2772 0.0229  95  GLN B NE2 
2449 N N   . THR B 96  ? 0.9190 0.5869 0.6847 0.0145  -0.2606 0.0250  96  THR B N   
2450 C CA  . THR B 96  ? 0.9372 0.6183 0.7173 0.0160  -0.2580 0.0349  96  THR B CA  
2451 C C   . THR B 96  ? 0.9148 0.6087 0.7002 0.0168  -0.2594 0.0431  96  THR B C   
2452 O O   . THR B 96  ? 0.9499 0.6559 0.7492 0.0191  -0.2565 0.0527  96  THR B O   
2453 C CB  . THR B 96  ? 0.9009 0.5782 0.6962 0.0206  -0.2514 0.0356  96  THR B CB  
2454 O OG1 . THR B 96  ? 0.9569 0.6270 0.7562 0.0242  -0.2489 0.0322  96  THR B OG1 
2455 C CG2 . THR B 96  ? 0.8617 0.5301 0.6528 0.0194  -0.2501 0.0285  96  THR B CG2 
2456 N N   . ARG B 97  ? 0.9234 0.6159 0.6985 0.0151  -0.2635 0.0400  97  ARG B N   
2457 C CA  . ARG B 97  ? 0.9672 0.6715 0.7480 0.0165  -0.2645 0.0472  97  ARG B CA  
2458 C C   . ARG B 97  ? 0.9846 0.7080 0.7659 0.0133  -0.2674 0.0549  97  ARG B C   
2459 O O   . ARG B 97  ? 1.0385 0.7766 0.8330 0.0160  -0.2652 0.0653  97  ARG B O   
2460 C CB  . ARG B 97  ? 0.9892 0.6856 0.7588 0.0156  -0.2680 0.0407  97  ARG B CB  
2461 C CG  . ARG B 97  ? 1.0530 0.7593 0.8299 0.0183  -0.2682 0.0476  97  ARG B CG  
2462 C CD  . ARG B 97  ? 1.1222 0.8307 0.8855 0.0141  -0.2743 0.0438  97  ARG B CD  
2463 N NE  . ARG B 97  ? 1.1498 0.8704 0.9199 0.0163  -0.2750 0.0510  97  ARG B NE  
2464 C CZ  . ARG B 97  ? 1.1503 0.8768 0.9116 0.0131  -0.2800 0.0496  97  ARG B CZ  
2465 N NH1 . ARG B 97  ? 1.1622 0.8828 0.9082 0.0074  -0.2844 0.0409  97  ARG B NH1 
2466 N NH2 . ARG B 97  ? 1.1574 0.8967 0.9264 0.0155  -0.2802 0.0571  97  ARG B NH2 
2467 N N   . GLN B 98  ? 1.0633 0.7879 0.8311 0.0075  -0.2720 0.0499  98  GLN B N   
2468 C CA  . GLN B 98  ? 1.1856 0.9294 0.9517 0.0036  -0.2755 0.0550  98  GLN B CA  
2469 C C   . GLN B 98  ? 1.2021 0.9528 0.9664 -0.0002 -0.2759 0.0556  98  GLN B C   
2470 O O   . GLN B 98  ? 1.2314 0.9916 0.9879 -0.0056 -0.2796 0.0537  98  GLN B O   
2471 C CB  . GLN B 98  ? 1.1708 0.9138 0.9239 -0.0007 -0.2805 0.0486  98  GLN B CB  
2472 C CG  . GLN B 98  ? 1.2131 0.9627 0.9705 0.0020  -0.2814 0.0528  98  GLN B CG  
2473 C CD  . GLN B 98  ? 1.3130 1.0671 1.0588 -0.0031 -0.2867 0.0477  98  GLN B CD  
2474 O OE1 . GLN B 98  ? 1.4192 1.1733 1.1551 -0.0089 -0.2893 0.0416  98  GLN B OE1 
2475 N NE2 . GLN B 98  ? 1.3047 1.0629 1.0525 -0.0011 -0.2879 0.0501  98  GLN B NE2 
2476 N N   . GLY B 99  ? 1.5446 1.2911 1.3166 0.0023  -0.2720 0.0580  99  GLY B N   
2477 C CA  . GLY B 99  ? 1.5454 1.3018 1.3194 -0.0002 -0.2717 0.0614  99  GLY B CA  
2478 C C   . GLY B 99  ? 1.5428 1.2943 1.3034 -0.0062 -0.2747 0.0532  99  GLY B C   
2479 O O   . GLY B 99  ? 1.5442 1.3038 1.3062 -0.0085 -0.2744 0.0556  99  GLY B O   
2480 N N   . ALA B 100 ? 1.2093 0.9485 0.9575 -0.0088 -0.2772 0.0439  100 ALA B N   
2481 C CA  . ALA B 100 ? 1.1273 0.8582 0.8648 -0.0134 -0.2785 0.0361  100 ALA B CA  
2482 C C   . ALA B 100 ? 1.0903 0.8049 0.8283 -0.0106 -0.2755 0.0326  100 ALA B C   
2483 O O   . ALA B 100 ? 1.0838 0.7954 0.8183 -0.0129 -0.2751 0.0300  100 ALA B O   
2484 C CB  . ALA B 100 ? 1.1608 0.8851 0.8860 -0.0172 -0.2819 0.0279  100 ALA B CB  
2485 N N   . PHE B 101 ? 1.0398 0.7451 0.7828 -0.0055 -0.2730 0.0326  101 PHE B N   
2486 C CA  . PHE B 101 ? 0.9375 0.6291 0.6825 -0.0025 -0.2697 0.0288  101 PHE B CA  
2487 C C   . PHE B 101 ? 0.9297 0.6091 0.6617 -0.0055 -0.2711 0.0201  101 PHE B C   
2488 O O   . PHE B 101 ? 0.9388 0.6155 0.6699 -0.0066 -0.2700 0.0188  101 PHE B O   
2489 C CB  . PHE B 101 ? 0.9919 0.6899 0.7487 -0.0005 -0.2663 0.0351  101 PHE B CB  
2490 C CG  . PHE B 101 ? 1.0062 0.7105 0.7784 0.0044  -0.2627 0.0426  101 PHE B CG  
2491 C CD1 . PHE B 101 ? 1.0102 0.7264 0.7869 0.0052  -0.2638 0.0491  101 PHE B CD1 
2492 C CD2 . PHE B 101 ? 0.9894 0.6884 0.7725 0.0083  -0.2578 0.0433  101 PHE B CD2 
2493 C CE1 . PHE B 101 ? 0.9187 0.6408 0.7109 0.0101  -0.2598 0.0568  101 PHE B CE1 
2494 C CE2 . PHE B 101 ? 0.9663 0.6709 0.7654 0.0128  -0.2536 0.0502  101 PHE B CE2 
2495 C CZ  . PHE B 101 ? 0.9087 0.6245 0.7125 0.0139  -0.2545 0.0573  101 PHE B CZ  
2496 N N   . THR B 102 ? 0.9091 0.5814 0.6314 -0.0069 -0.2735 0.0144  102 THR B N   
2497 C CA  . THR B 102 ? 0.8903 0.5521 0.6004 -0.0099 -0.2748 0.0069  102 THR B CA  
2498 C C   . THR B 102 ? 0.8785 0.5256 0.5858 -0.0063 -0.2727 0.0014  102 THR B C   
2499 O O   . THR B 102 ? 0.8532 0.4966 0.5629 -0.0029 -0.2719 0.0006  102 THR B O   
2500 C CB  . THR B 102 ? 0.9160 0.5794 0.6173 -0.0141 -0.2783 0.0038  102 THR B CB  
2501 O OG1 . THR B 102 ? 0.9623 0.6251 0.6649 -0.0116 -0.2792 0.0044  102 THR B OG1 
2502 C CG2 . THR B 102 ? 0.9479 0.6271 0.6509 -0.0187 -0.2802 0.0075  102 THR B CG2 
2503 N N   . PHE B 103 ? 0.8946 0.5346 0.5971 -0.0070 -0.2716 -0.0025 103 PHE B N   
2504 C CA  . PHE B 103 ? 0.8583 0.4864 0.5572 -0.0039 -0.2696 -0.0081 103 PHE B CA  
2505 C C   . PHE B 103 ? 0.8610 0.4807 0.5480 -0.0056 -0.2716 -0.0137 103 PHE B C   
2506 O O   . PHE B 103 ? 0.8622 0.4847 0.5444 -0.0093 -0.2744 -0.0137 103 PHE B O   
2507 C CB  . PHE B 103 ? 0.8596 0.4853 0.5592 -0.0036 -0.2673 -0.0092 103 PHE B CB  
2508 C CG  . PHE B 103 ? 0.8566 0.4883 0.5687 -0.0010 -0.2645 -0.0049 103 PHE B CG  
2509 C CD1 . PHE B 103 ? 0.8560 0.4975 0.5740 -0.0030 -0.2649 0.0010  103 PHE B CD1 
2510 C CD2 . PHE B 103 ? 0.8545 0.4824 0.5728 0.0032  -0.2612 -0.0072 103 PHE B CD2 
2511 C CE1 . PHE B 103 ? 0.8534 0.5001 0.5833 -0.0007 -0.2620 0.0052  103 PHE B CE1 
2512 C CE2 . PHE B 103 ? 0.8518 0.4850 0.5827 0.0053  -0.2580 -0.0037 103 PHE B CE2 
2513 C CZ  . PHE B 103 ? 0.8513 0.4935 0.5881 0.0034  -0.2584 0.0028  103 PHE B CZ  
2514 N N   . GLY B 104 ? 0.8619 0.4719 0.5445 -0.0030 -0.2700 -0.0187 104 GLY B N   
2515 C CA  . GLY B 104 ? 0.8648 0.4662 0.5363 -0.0041 -0.2712 -0.0237 104 GLY B CA  
2516 C C   . GLY B 104 ? 0.8685 0.4658 0.5341 -0.0060 -0.2703 -0.0257 104 GLY B C   
2517 O O   . GLY B 104 ? 0.8688 0.4696 0.5383 -0.0064 -0.2689 -0.0237 104 GLY B O   
2518 N N   . GLN B 105 ? 0.8874 0.4772 0.5438 -0.0071 -0.2709 -0.0296 105 GLN B N   
2519 C CA  . GLN B 105 ? 0.9393 0.5249 0.5904 -0.0087 -0.2696 -0.0311 105 GLN B CA  
2520 C C   . GLN B 105 ? 0.9749 0.5594 0.6281 -0.0050 -0.2667 -0.0314 105 GLN B C   
2521 O O   . GLN B 105 ? 1.0040 0.5897 0.6578 -0.0063 -0.2654 -0.0301 105 GLN B O   
2522 C CB  . GLN B 105 ? 0.8880 0.4653 0.5302 -0.0095 -0.2700 -0.0349 105 GLN B CB  
2523 C CG  . GLN B 105 ? 1.0166 0.5937 0.6563 -0.0118 -0.2729 -0.0360 105 GLN B CG  
2524 C CD  . GLN B 105 ? 1.0840 0.6519 0.7154 -0.0110 -0.2728 -0.0400 105 GLN B CD  
2525 O OE1 . GLN B 105 ? 1.0519 0.6142 0.6795 -0.0086 -0.2705 -0.0416 105 GLN B OE1 
2526 N NE2 . GLN B 105 ? 1.1685 0.7356 0.7973 -0.0131 -0.2754 -0.0415 105 GLN B NE2 
2527 N N   . GLY B 106 ? 1.0095 0.5924 0.6642 -0.0006 -0.2654 -0.0335 106 GLY B N   
2528 C CA  . GLY B 106 ? 1.0113 0.5938 0.6668 0.0029  -0.2625 -0.0351 106 GLY B CA  
2529 C C   . GLY B 106 ? 1.0218 0.5984 0.6697 0.0055  -0.2615 -0.0393 106 GLY B C   
2530 O O   . GLY B 106 ? 1.0468 0.6180 0.6875 0.0038  -0.2629 -0.0404 106 GLY B O   
2531 N N   . THR B 107 ? 0.9953 0.5736 0.6448 0.0094  -0.2588 -0.0419 107 THR B N   
2532 C CA  . THR B 107 ? 0.8734 0.4482 0.5160 0.0124  -0.2576 -0.0458 107 THR B CA  
2533 C C   . THR B 107 ? 0.8726 0.4527 0.5175 0.0157  -0.2543 -0.0475 107 THR B C   
2534 O O   . THR B 107 ? 0.9800 0.5654 0.6326 0.0176  -0.2527 -0.0494 107 THR B O   
2535 C CB  . THR B 107 ? 0.8760 0.4487 0.5185 0.0142  -0.2582 -0.0493 107 THR B CB  
2536 O OG1 . THR B 107 ? 0.9294 0.4968 0.5670 0.0113  -0.2613 -0.0482 107 THR B OG1 
2537 C CG2 . THR B 107 ? 0.8782 0.4502 0.5155 0.0181  -0.2561 -0.0540 107 THR B CG2 
2538 N N   . LYS B 108 ? 0.8897 0.4691 0.5286 0.0162  -0.2531 -0.0469 108 LYS B N   
2539 C CA  . LYS B 108 ? 0.9524 0.5386 0.5930 0.0195  -0.2500 -0.0483 108 LYS B CA  
2540 C C   . LYS B 108 ? 0.9205 0.5089 0.5581 0.0234  -0.2483 -0.0534 108 LYS B C   
2541 O O   . LYS B 108 ? 0.9537 0.5373 0.5834 0.0241  -0.2488 -0.0543 108 LYS B O   
2542 C CB  . LYS B 108 ? 0.9454 0.5313 0.5817 0.0190  -0.2489 -0.0447 108 LYS B CB  
2543 C CG  . LYS B 108 ? 1.0175 0.6123 0.6583 0.0212  -0.2463 -0.0445 108 LYS B CG  
2544 C CD  . LYS B 108 ? 1.1553 0.7501 0.7924 0.0212  -0.2448 -0.0404 108 LYS B CD  
2545 C CE  . LYS B 108 ? 1.2457 0.8386 0.8748 0.0238  -0.2433 -0.0405 108 LYS B CE  
2546 N NZ  . LYS B 108 ? 1.1675 0.7621 0.7949 0.0247  -0.2409 -0.0359 108 LYS B NZ  
2547 N N   . LEU B 109 ? 0.8971 0.4934 0.5416 0.0258  -0.2460 -0.0572 109 LEU B N   
2548 C CA  . LEU B 109 ? 0.9146 0.5162 0.5572 0.0296  -0.2436 -0.0629 109 LEU B CA  
2549 C C   . LEU B 109 ? 1.0101 0.6207 0.6514 0.0318  -0.2410 -0.0626 109 LEU B C   
2550 O O   . LEU B 109 ? 0.9997 0.6162 0.6472 0.0313  -0.2400 -0.0612 109 LEU B O   
2551 C CB  . LEU B 109 ? 0.8951 0.5014 0.5474 0.0308  -0.2419 -0.0683 109 LEU B CB  
2552 C CG  . LEU B 109 ? 0.8954 0.5038 0.5447 0.0338  -0.2401 -0.0751 109 LEU B CG  
2553 C CD1 . LEU B 109 ? 0.9261 0.5239 0.5667 0.0332  -0.2430 -0.0743 109 LEU B CD1 
2554 C CD2 . LEU B 109 ? 0.9525 0.5667 0.6136 0.0350  -0.2372 -0.0811 109 LEU B CD2 
2555 N N   . GLU B 110 ? 1.0183 0.6302 0.6514 0.0344  -0.2400 -0.0636 110 GLU B N   
2556 C CA  . GLU B 110 ? 1.0273 0.6491 0.6582 0.0371  -0.2373 -0.0626 110 GLU B CA  
2557 C C   . GLU B 110 ? 1.0533 0.6839 0.6819 0.0409  -0.2349 -0.0690 110 GLU B C   
2558 O O   . GLU B 110 ? 1.0521 0.6773 0.6762 0.0414  -0.2357 -0.0720 110 GLU B O   
2559 C CB  . GLU B 110 ? 1.0912 0.7069 0.7145 0.0366  -0.2378 -0.0559 110 GLU B CB  
2560 C CG  . GLU B 110 ? 1.1383 0.7640 0.7588 0.0400  -0.2348 -0.0533 110 GLU B CG  
2561 C CD  . GLU B 110 ? 1.3880 1.0063 1.0031 0.0392  -0.2347 -0.0461 110 GLU B CD  
2562 O OE1 . GLU B 110 ? 1.3761 0.9826 0.9909 0.0354  -0.2369 -0.0436 110 GLU B OE1 
2563 O OE2 . GLU B 110 ? 1.3388 0.9641 0.9510 0.0425  -0.2319 -0.0429 110 GLU B OE2 
2564 N N   . ILE B 111 ? 0.9972 0.6423 0.6294 0.0434  -0.2319 -0.0714 111 ILE B N   
2565 C CA  . ILE B 111 ? 0.9301 0.5871 0.5616 0.0468  -0.2291 -0.0785 111 ILE B CA  
2566 C C   . ILE B 111 ? 0.9625 0.6253 0.5848 0.0500  -0.2278 -0.0750 111 ILE B C   
2567 O O   . ILE B 111 ? 0.9144 0.5851 0.5369 0.0512  -0.2264 -0.0704 111 ILE B O   
2568 C CB  . ILE B 111 ? 0.9531 0.6251 0.5951 0.0474  -0.2261 -0.0844 111 ILE B CB  
2569 C CG1 . ILE B 111 ? 1.0393 0.7051 0.6915 0.0441  -0.2272 -0.0846 111 ILE B CG1 
2570 C CG2 . ILE B 111 ? 0.9734 0.6559 0.6169 0.0499  -0.2232 -0.0939 111 ILE B CG2 
2571 C CD1 . ILE B 111 ? 1.0211 0.6774 0.6762 0.0429  -0.2281 -0.0885 111 ILE B CD1 
2572 N N   . LYS B 112 ? 0.9576 0.6167 0.5722 0.0516  -0.2280 -0.0768 112 LYS B N   
2573 C CA  . LYS B 112 ? 0.9146 0.5797 0.5207 0.0551  -0.2263 -0.0735 112 LYS B CA  
2574 C C   . LYS B 112 ? 0.9314 0.6180 0.5399 0.0588  -0.2226 -0.0786 112 LYS B C   
2575 O O   . LYS B 112 ? 0.9703 0.6640 0.5783 0.0604  -0.2212 -0.0863 112 LYS B O   
2576 C CB  . LYS B 112 ? 0.9141 0.5689 0.5119 0.0555  -0.2276 -0.0746 112 LYS B CB  
2577 C CG  . LYS B 112 ? 1.0141 0.6602 0.6039 0.0558  -0.2281 -0.0663 112 LYS B CG  
2578 C CD  . LYS B 112 ? 1.1072 0.7416 0.6897 0.0554  -0.2299 -0.0681 112 LYS B CD  
2579 C CE  . LYS B 112 ? 1.2308 0.8538 0.8074 0.0545  -0.2305 -0.0601 112 LYS B CE  
2580 N NZ  . LYS B 112 ? 1.2269 0.8374 0.7970 0.0534  -0.2326 -0.0621 112 LYS B NZ  
2581 N N   . ARG B 113 ? 0.8865 0.5848 0.4979 0.0600  -0.2208 -0.0745 113 ARG B N   
2582 C CA  . ARG B 113 ? 0.8658 0.5869 0.4806 0.0631  -0.2173 -0.0794 113 ARG B CA  
2583 C C   . ARG B 113 ? 0.9106 0.6434 0.5182 0.0676  -0.2150 -0.0734 113 ARG B C   
2584 O O   . ARG B 113 ? 0.9070 0.6290 0.5071 0.0684  -0.2157 -0.0662 113 ARG B O   
2585 C CB  . ARG B 113 ? 0.8631 0.5923 0.4879 0.0615  -0.2166 -0.0801 113 ARG B CB  
2586 C CG  . ARG B 113 ? 0.8774 0.6011 0.5016 0.0608  -0.2176 -0.0697 113 ARG B CG  
2587 C CD  . ARG B 113 ? 0.8826 0.6247 0.5135 0.0619  -0.2154 -0.0700 113 ARG B CD  
2588 N NE  . ARG B 113 ? 0.8735 0.6361 0.5009 0.0666  -0.2121 -0.0700 113 ARG B NE  
2589 C CZ  . ARG B 113 ? 0.9138 0.6979 0.5463 0.0684  -0.2096 -0.0717 113 ARG B CZ  
2590 N NH1 . ARG B 113 ? 0.9349 0.7220 0.5763 0.0659  -0.2098 -0.0737 113 ARG B NH1 
2591 N NH2 . ARG B 113 ? 0.9434 0.7472 0.5721 0.0729  -0.2066 -0.0712 113 ARG B NH2 
2592 N N   . THR B 114 ? 0.9483 0.7043 0.5590 0.0705  -0.2118 -0.0764 114 THR B N   
2593 C CA  . THR B 114 ? 0.8830 0.6544 0.4881 0.0753  -0.2090 -0.0706 114 THR B CA  
2594 C C   . THR B 114 ? 0.8823 0.6486 0.4869 0.0758  -0.2090 -0.0583 114 THR B C   
2595 O O   . THR B 114 ? 0.8727 0.6362 0.4835 0.0734  -0.2100 -0.0565 114 THR B O   
2596 C CB  . THR B 114 ? 0.8628 0.6627 0.4729 0.0778  -0.2056 -0.0776 114 THR B CB  
2597 O OG1 . THR B 114 ? 0.8820 0.6891 0.4906 0.0786  -0.2044 -0.0880 114 THR B OG1 
2598 C CG2 . THR B 114 ? 0.8647 0.6833 0.4716 0.0827  -0.2027 -0.0693 114 THR B CG2 
2599 N N   . VAL B 115 ? 0.8766 0.6416 0.4742 0.0790  -0.2076 -0.0499 115 VAL B N   
2600 C CA  . VAL B 115 ? 0.8811 0.6434 0.4791 0.0802  -0.2064 -0.0380 115 VAL B CA  
2601 C C   . VAL B 115 ? 0.8786 0.6630 0.4825 0.0824  -0.2041 -0.0367 115 VAL B C   
2602 O O   . VAL B 115 ? 0.8754 0.6833 0.4794 0.0860  -0.2015 -0.0404 115 VAL B O   
2603 C CB  . VAL B 115 ? 0.8858 0.6468 0.4767 0.0840  -0.2041 -0.0296 115 VAL B CB  
2604 C CG1 . VAL B 115 ? 0.8910 0.6445 0.4838 0.0846  -0.2025 -0.0174 115 VAL B CG1 
2605 C CG2 . VAL B 115 ? 1.0262 0.7685 0.6108 0.0819  -0.2064 -0.0330 115 VAL B CG2 
2606 N N   . ALA B 116 ? 0.8797 0.6578 0.4890 0.0802  -0.2049 -0.0319 116 ALA B N   
2607 C CA  . ALA B 116 ? 0.8774 0.6749 0.4928 0.0819  -0.2030 -0.0303 116 ALA B CA  
2608 C C   . ALA B 116 ? 0.8825 0.6753 0.4985 0.0834  -0.2014 -0.0175 116 ALA B C   
2609 O O   . ALA B 116 ? 0.9221 0.6963 0.5348 0.0827  -0.2015 -0.0109 116 ALA B O   
2610 C CB  . ALA B 116 ? 0.8730 0.6694 0.4959 0.0775  -0.2053 -0.0385 116 ALA B CB  
2611 N N   . ALA B 117 ? 0.8811 0.6912 0.5021 0.0855  -0.1995 -0.0141 117 ALA B N   
2612 C CA  . ALA B 117 ? 0.8856 0.6949 0.5083 0.0878  -0.1970 -0.0017 117 ALA B CA  
2613 C C   . ALA B 117 ? 0.8842 0.6925 0.5140 0.0850  -0.1983 -0.0014 117 ALA B C   
2614 O O   . ALA B 117 ? 0.9124 0.7329 0.5464 0.0835  -0.1995 -0.0095 117 ALA B O   
2615 C CB  . ALA B 117 ? 0.8858 0.7207 0.5075 0.0947  -0.1925 0.0049  117 ALA B CB  
2616 N N   . PRO B 118 ? 0.8889 0.6829 0.5205 0.0839  -0.1978 0.0074  118 PRO B N   
2617 C CA  . PRO B 118 ? 0.8958 0.6871 0.5337 0.0808  -0.1993 0.0075  118 PRO B CA  
2618 C C   . PRO B 118 ? 0.9465 0.7627 0.5888 0.0849  -0.1966 0.0111  118 PRO B C   
2619 O O   . PRO B 118 ? 1.0286 0.8573 0.6701 0.0902  -0.1927 0.0199  118 PRO B O   
2620 C CB  . PRO B 118 ? 0.9273 0.6966 0.5655 0.0789  -0.1987 0.0160  118 PRO B CB  
2621 C CG  . PRO B 118 ? 0.9576 0.7262 0.5915 0.0831  -0.1951 0.0233  118 PRO B CG  
2622 C CD  . PRO B 118 ? 0.9133 0.6899 0.5419 0.0844  -0.1961 0.0159  118 PRO B CD  
2623 N N   . SER B 119 ? 1.0022 0.8260 0.6496 0.0822  -0.1987 0.0045  119 SER B N   
2624 C CA  . SER B 119 ? 1.0143 0.8594 0.6669 0.0849  -0.1968 0.0077  119 SER B CA  
2625 C C   . SER B 119 ? 1.0372 0.8684 0.6931 0.0834  -0.1967 0.0160  119 SER B C   
2626 O O   . SER B 119 ? 1.0734 0.8924 0.7326 0.0785  -0.1997 0.0121  119 SER B O   
2627 C CB  . SER B 119 ? 1.0739 0.9336 0.7314 0.0825  -0.1986 -0.0038 119 SER B CB  
2628 O OG  . SER B 119 ? 1.1796 1.0485 0.8347 0.0829  -0.1986 -0.0130 119 SER B OG  
2629 N N   . VAL B 120 ? 1.0200 0.8534 0.6757 0.0878  -0.1929 0.0278  120 VAL B N   
2630 C CA  . VAL B 120 ? 0.9426 0.7606 0.6014 0.0865  -0.1919 0.0362  120 VAL B CA  
2631 C C   . VAL B 120 ? 0.9772 0.8104 0.6420 0.0877  -0.1914 0.0387  120 VAL B C   
2632 O O   . VAL B 120 ? 1.1249 0.9828 0.7912 0.0928  -0.1886 0.0422  120 VAL B O   
2633 C CB  . VAL B 120 ? 0.9907 0.8029 0.6483 0.0906  -0.1873 0.0478  120 VAL B CB  
2634 C CG1 . VAL B 120 ? 1.0541 0.8468 0.7156 0.0881  -0.1861 0.0544  120 VAL B CG1 
2635 C CG2 . VAL B 120 ? 1.0268 0.8282 0.6782 0.0901  -0.1877 0.0448  120 VAL B CG2 
2636 N N   . PHE B 121 ? 0.9820 0.8013 0.6502 0.0829  -0.1939 0.0370  121 PHE B N   
2637 C CA  . PHE B 121 ? 1.0778 0.9071 0.7517 0.0833  -0.1935 0.0399  121 PHE B CA  
2638 C C   . PHE B 121 ? 1.1146 0.9233 0.7908 0.0812  -0.1926 0.0471  121 PHE B C   
2639 O O   . PHE B 121 ? 1.1440 0.9301 0.8181 0.0771  -0.1941 0.0453  121 PHE B O   
2640 C CB  . PHE B 121 ? 1.1552 0.9897 0.8319 0.0789  -0.1977 0.0289  121 PHE B CB  
2641 C CG  . PHE B 121 ? 1.1460 0.9912 0.8208 0.0785  -0.1992 0.0185  121 PHE B CG  
2642 C CD1 . PHE B 121 ? 1.1594 1.0315 0.8342 0.0831  -0.1969 0.0174  121 PHE B CD1 
2643 C CD2 . PHE B 121 ? 1.1721 1.0012 0.8456 0.0733  -0.2026 0.0095  121 PHE B CD2 
2644 C CE1 . PHE B 121 ? 1.1524 1.0345 0.8260 0.0824  -0.1978 0.0069  121 PHE B CE1 
2645 C CE2 . PHE B 121 ? 1.1466 0.9849 0.8194 0.0729  -0.2035 -0.0003 121 PHE B CE2 
2646 C CZ  . PHE B 121 ? 1.1327 0.9973 0.8056 0.0773  -0.2010 -0.0020 121 PHE B CZ  
2647 N N   . ILE B 122 ? 1.1681 0.9854 0.8490 0.0840  -0.1900 0.0549  122 ILE B N   
2648 C CA  . ILE B 122 ? 1.1071 0.9065 0.7912 0.0822  -0.1884 0.0616  122 ILE B CA  
2649 C C   . ILE B 122 ? 1.1131 0.9189 0.8021 0.0808  -0.1899 0.0611  122 ILE B C   
2650 O O   . ILE B 122 ? 1.2231 1.0518 0.9146 0.0845  -0.1890 0.0627  122 ILE B O   
2651 C CB  . ILE B 122 ? 1.1470 0.9470 0.8332 0.0877  -0.1820 0.0742  122 ILE B CB  
2652 C CG1 . ILE B 122 ? 1.1725 0.9540 0.8634 0.0855  -0.1797 0.0801  122 ILE B CG1 
2653 C CG2 . ILE B 122 ? 1.1978 1.0259 0.8865 0.0949  -0.1785 0.0812  122 ILE B CG2 
2654 C CD1 . ILE B 122 ? 1.1253 0.9007 0.8192 0.0894  -0.1730 0.0911  122 ILE B CD1 
2655 N N   . PHE B 123 ? 1.0982 0.8848 0.7887 0.0753  -0.1923 0.0586  123 PHE B N   
2656 C CA  . PHE B 123 ? 1.1017 0.8912 0.7964 0.0731  -0.1942 0.0574  123 PHE B CA  
2657 C C   . PHE B 123 ? 1.1672 0.9450 0.8658 0.0733  -0.1908 0.0661  123 PHE B C   
2658 O O   . PHE B 123 ? 1.2061 0.9630 0.9041 0.0700  -0.1902 0.0666  123 PHE B O   
2659 C CB  . PHE B 123 ? 1.1161 0.8947 0.8099 0.0663  -0.1997 0.0467  123 PHE B CB  
2660 C CG  . PHE B 123 ? 1.1510 0.9391 0.8423 0.0657  -0.2025 0.0375  123 PHE B CG  
2661 C CD1 . PHE B 123 ? 1.2228 1.0323 0.9168 0.0669  -0.2035 0.0327  123 PHE B CD1 
2662 C CD2 . PHE B 123 ? 1.1433 0.9192 0.8301 0.0637  -0.2038 0.0332  123 PHE B CD2 
2663 C CE1 . PHE B 123 ? 1.2692 1.0877 0.9622 0.0661  -0.2053 0.0235  123 PHE B CE1 
2664 C CE2 . PHE B 123 ? 1.1738 0.9580 0.8590 0.0632  -0.2058 0.0245  123 PHE B CE2 
2665 C CZ  . PHE B 123 ? 1.2380 1.0435 0.9267 0.0643  -0.2064 0.0195  123 PHE B CZ  
2666 N N   . PRO B 124 ? 1.2807 1.0718 0.9839 0.0769  -0.1884 0.0727  124 PRO B N   
2667 C CA  . PRO B 124 ? 1.2528 1.0325 0.9608 0.0768  -0.1850 0.0802  124 PRO B CA  
2668 C C   . PRO B 124 ? 1.2223 0.9874 0.9310 0.0701  -0.1892 0.0740  124 PRO B C   
2669 O O   . PRO B 124 ? 1.1815 0.9489 0.8880 0.0664  -0.1944 0.0649  124 PRO B O   
2670 C CB  . PRO B 124 ? 1.1972 0.9992 0.9097 0.0831  -0.1817 0.0884  124 PRO B CB  
2671 C CG  . PRO B 124 ? 1.2849 1.1074 0.9954 0.0832  -0.1859 0.0810  124 PRO B CG  
2672 C CD  . PRO B 124 ? 1.3125 1.1310 1.0174 0.0812  -0.1883 0.0732  124 PRO B CD  
2673 N N   . PRO B 125 ? 1.2033 0.9537 0.9156 0.0684  -0.1866 0.0784  125 PRO B N   
2674 C CA  . PRO B 125 ? 1.1888 0.9251 0.9014 0.0619  -0.1904 0.0725  125 PRO B CA  
2675 C C   . PRO B 125 ? 1.1603 0.9092 0.8751 0.0616  -0.1934 0.0704  125 PRO B C   
2676 O O   . PRO B 125 ? 1.2062 0.9732 0.9237 0.0666  -0.1915 0.0756  125 PRO B O   
2677 C CB  . PRO B 125 ? 1.1783 0.8991 0.8952 0.0612  -0.1855 0.0787  125 PRO B CB  
2678 C CG  . PRO B 125 ? 1.2146 0.9475 0.9358 0.0685  -0.1792 0.0895  125 PRO B CG  
2679 C CD  . PRO B 125 ? 1.2301 0.9755 0.9470 0.0722  -0.1796 0.0889  125 PRO B CD  
2680 N N   . SER B 126 ? 1.1983 0.9380 0.9121 0.0556  -0.1982 0.0629  126 SER B N   
2681 C CA  . SER B 126 ? 1.1659 0.9150 0.8821 0.0543  -0.2013 0.0601  126 SER B CA  
2682 C C   . SER B 126 ? 1.1808 0.9276 0.9015 0.0554  -0.1985 0.0669  126 SER B C   
2683 O O   . SER B 126 ? 1.2286 0.9605 0.9506 0.0545  -0.1951 0.0711  126 SER B O   
2684 C CB  . SER B 126 ? 1.1866 0.9257 0.9013 0.0477  -0.2067 0.0508  126 SER B CB  
2685 O OG  . SER B 126 ? 1.1931 0.9180 0.9094 0.0438  -0.2071 0.0516  126 SER B OG  
2686 N N   . ASP B 127 ? 1.1985 0.9606 0.9221 0.0571  -0.1996 0.0676  127 ASP B N   
2687 C CA  . ASP B 127 ? 1.2594 1.0192 0.9872 0.0576  -0.1975 0.0732  127 ASP B CA  
2688 C C   . ASP B 127 ? 1.2917 1.0319 1.0191 0.0510  -0.2000 0.0687  127 ASP B C   
2689 O O   . ASP B 127 ? 1.3795 1.1088 1.1096 0.0505  -0.1969 0.0732  127 ASP B O   
2690 C CB  . ASP B 127 ? 1.3816 1.1624 1.1122 0.0600  -0.1990 0.0735  127 ASP B CB  
2691 C CG  . ASP B 127 ? 1.4692 1.2727 1.2006 0.0667  -0.1964 0.0781  127 ASP B CG  
2692 O OD1 . ASP B 127 ? 1.3332 1.1351 1.0639 0.0705  -0.1922 0.0840  127 ASP B OD1 
2693 O OD2 . ASP B 127 ? 1.5216 1.3453 1.2546 0.0680  -0.1984 0.0757  127 ASP B OD2 
2694 N N   . SER B 128 ? 1.2565 0.9927 0.9812 0.0459  -0.2053 0.0598  128 SER B N   
2695 C CA  . SER B 128 ? 1.2799 0.9995 1.0041 0.0397  -0.2079 0.0556  128 SER B CA  
2696 C C   . SER B 128 ? 1.2936 0.9951 1.0164 0.0376  -0.2051 0.0570  128 SER B C   
2697 O O   . SER B 128 ? 1.3238 1.0132 1.0481 0.0344  -0.2042 0.0574  128 SER B O   
2698 C CB  . SER B 128 ? 1.2327 0.9532 0.9553 0.0354  -0.2134 0.0467  128 SER B CB  
2699 O OG  . SER B 128 ? 1.3258 1.0328 1.0483 0.0298  -0.2159 0.0434  128 SER B OG  
2700 N N   . GLN B 129 ? 1.2936 0.9939 1.0139 0.0392  -0.2037 0.0571  129 GLN B N   
2701 C CA  . GLN B 129 ? 1.2641 0.9481 0.9836 0.0369  -0.2010 0.0577  129 GLN B CA  
2702 C C   . GLN B 129 ? 1.3612 1.0404 1.0855 0.0394  -0.1946 0.0653  129 GLN B C   
2703 O O   . GLN B 129 ? 1.4179 1.0829 1.1440 0.0356  -0.1926 0.0646  129 GLN B O   
2704 C CB  . GLN B 129 ? 1.1954 0.8800 0.9114 0.0386  -0.2005 0.0566  129 GLN B CB  
2705 C CG  . GLN B 129 ? 1.1866 0.8546 0.9007 0.0341  -0.2003 0.0534  129 GLN B CG  
2706 C CD  . GLN B 129 ? 1.1430 0.8111 0.8535 0.0357  -0.1999 0.0524  129 GLN B CD  
2707 O OE1 . GLN B 129 ? 1.0834 0.7394 0.7924 0.0324  -0.1995 0.0500  129 GLN B OE1 
2708 N NE2 . GLN B 129 ? 1.1393 0.8218 0.8486 0.0407  -0.1999 0.0541  129 GLN B NE2 
2709 N N   . LEU B 130 ? 1.3384 1.0303 1.0657 0.0458  -0.1908 0.0727  130 LEU B N   
2710 C CA  . LEU B 130 ? 1.3057 0.9940 1.0391 0.0487  -0.1841 0.0809  130 LEU B CA  
2711 C C   . LEU B 130 ? 1.3287 1.0095 1.0651 0.0451  -0.1845 0.0798  130 LEU B C   
2712 O O   . LEU B 130 ? 1.3357 1.0040 1.0763 0.0433  -0.1799 0.0817  130 LEU B O   
2713 C CB  . LEU B 130 ? 1.2507 0.9572 0.9872 0.0565  -0.1806 0.0895  130 LEU B CB  
2714 C CG  . LEU B 130 ? 1.2474 0.9589 0.9843 0.0617  -0.1760 0.0952  130 LEU B CG  
2715 C CD1 . LEU B 130 ? 1.2744 0.9711 1.0169 0.0619  -0.1687 0.1005  130 LEU B CD1 
2716 C CD2 . LEU B 130 ? 1.2329 0.9450 0.9629 0.0600  -0.1803 0.0884  130 LEU B CD2 
2717 N N   . LYS B 131 ? 1.3400 1.0283 1.0746 0.0435  -0.1899 0.0760  131 LYS B N   
2718 C CA  . LYS B 131 ? 1.3483 1.0291 1.0848 0.0395  -0.1911 0.0740  131 LYS B CA  
2719 C C   . LYS B 131 ? 1.4299 1.0936 1.1645 0.0326  -0.1923 0.0677  131 LYS B C   
2720 O O   . LYS B 131 ? 1.5307 1.1846 1.2683 0.0297  -0.1902 0.0676  131 LYS B O   
2721 C CB  . LYS B 131 ? 1.2768 0.9689 1.0116 0.0386  -0.1970 0.0704  131 LYS B CB  
2722 C CG  . LYS B 131 ? 1.2818 0.9752 1.0203 0.0387  -0.1964 0.0731  131 LYS B CG  
2723 C CD  . LYS B 131 ? 1.3062 1.0150 1.0441 0.0393  -0.2013 0.0707  131 LYS B CD  
2724 C CE  . LYS B 131 ? 1.3587 1.0702 1.1003 0.0399  -0.2007 0.0740  131 LYS B CE  
2725 N NZ  . LYS B 131 ? 1.2514 0.9788 0.9931 0.0404  -0.2052 0.0713  131 LYS B NZ  
2726 N N   . SER B 132 ? 1.4734 1.1342 1.2034 0.0301  -0.1956 0.0623  132 SER B N   
2727 C CA  . SER B 132 ? 1.4789 1.1257 1.2070 0.0238  -0.1969 0.0564  132 SER B CA  
2728 C C   . SER B 132 ? 1.4926 1.1283 1.2242 0.0232  -0.1905 0.0588  132 SER B C   
2729 O O   . SER B 132 ? 1.4983 1.1232 1.2297 0.0177  -0.1906 0.0540  132 SER B O   
2730 C CB  . SER B 132 ? 1.4712 1.1192 1.1939 0.0217  -0.2020 0.0506  132 SER B CB  
2731 O OG  . SER B 132 ? 1.6039 1.2627 1.3250 0.0222  -0.2071 0.0481  132 SER B OG  
2732 N N   . GLY B 133 ? 1.3615 1.0005 1.0970 0.0287  -0.1846 0.0659  133 GLY B N   
2733 C CA  . GLY B 133 ? 1.3579 0.9866 1.0986 0.0285  -0.1775 0.0685  133 GLY B CA  
2734 C C   . GLY B 133 ? 1.3360 0.9622 1.0748 0.0293  -0.1761 0.0681  133 GLY B C   
2735 O O   . GLY B 133 ? 1.3556 0.9734 1.0996 0.0289  -0.1697 0.0701  133 GLY B O   
2736 N N   . THR B 134 ? 1.2987 0.9319 1.0309 0.0302  -0.1814 0.0654  134 THR B N   
2737 C CA  . THR B 134 ? 1.2422 0.8740 0.9719 0.0314  -0.1805 0.0652  134 THR B CA  
2738 C C   . THR B 134 ? 1.2249 0.8717 0.9519 0.0377  -0.1817 0.0691  134 THR B C   
2739 O O   . THR B 134 ? 1.2478 0.9061 0.9736 0.0397  -0.1850 0.0695  134 THR B O   
2740 C CB  . THR B 134 ? 1.2258 0.8507 0.9499 0.0254  -0.1860 0.0565  134 THR B CB  
2741 O OG1 . THR B 134 ? 1.3005 0.9319 1.0201 0.0239  -0.1930 0.0521  134 THR B OG1 
2742 C CG2 . THR B 134 ? 1.1750 0.7867 0.9020 0.0192  -0.1839 0.0525  134 THR B CG2 
2743 N N   . ALA B 135 ? 1.1835 0.8308 0.9099 0.0407  -0.1788 0.0718  135 ALA B N   
2744 C CA  . ALA B 135 ? 1.1399 0.8022 0.8636 0.0468  -0.1794 0.0753  135 ALA B CA  
2745 C C   . ALA B 135 ? 1.1238 0.7832 0.8419 0.0456  -0.1816 0.0709  135 ALA B C   
2746 O O   . ALA B 135 ? 1.1154 0.7634 0.8347 0.0439  -0.1784 0.0709  135 ALA B O   
2747 C CB  . ALA B 135 ? 1.2069 0.8763 0.9368 0.0536  -0.1719 0.0861  135 ALA B CB  
2748 N N   . SER B 136 ? 1.1262 0.7961 0.8388 0.0465  -0.1869 0.0667  136 SER B N   
2749 C CA  . SER B 136 ? 1.1102 0.7784 0.8173 0.0457  -0.1895 0.0620  136 SER B CA  
2750 C C   . SER B 136 ? 1.0723 0.7579 0.7772 0.0518  -0.1895 0.0645  136 SER B C   
2751 O O   . SER B 136 ? 1.1010 0.8002 0.8053 0.0532  -0.1925 0.0626  136 SER B O   
2752 C CB  . SER B 136 ? 1.1165 0.7794 0.8195 0.0398  -0.1963 0.0527  136 SER B CB  
2753 O OG  . SER B 136 ? 1.1907 0.8665 0.8929 0.0407  -0.2003 0.0499  136 SER B OG  
2754 N N   . VAL B 137 ? 1.0851 0.7709 0.7889 0.0551  -0.1859 0.0681  137 VAL B N   
2755 C CA  . VAL B 137 ? 1.1114 0.8139 0.8125 0.0607  -0.1856 0.0700  137 VAL B CA  
2756 C C   . VAL B 137 ? 1.1247 0.8233 0.8195 0.0582  -0.1897 0.0623  137 VAL B C   
2757 O O   . VAL B 137 ? 1.1483 0.8320 0.8416 0.0552  -0.1891 0.0607  137 VAL B O   
2758 C CB  . VAL B 137 ? 1.0437 0.7510 0.7485 0.0669  -0.1784 0.0805  137 VAL B CB  
2759 C CG1 . VAL B 137 ? 1.1064 0.8335 0.8080 0.0728  -0.1782 0.0824  137 VAL B CG1 
2760 C CG2 . VAL B 137 ? 1.0258 0.7355 0.7380 0.0693  -0.1738 0.0885  137 VAL B CG2 
2761 N N   . VAL B 138 ? 1.0677 0.7802 0.7593 0.0594  -0.1934 0.0573  138 VAL B N   
2762 C CA  . VAL B 138 ? 1.0707 0.7809 0.7570 0.0572  -0.1974 0.0494  138 VAL B CA  
2763 C C   . VAL B 138 ? 1.0613 0.7851 0.7447 0.0628  -0.1952 0.0516  138 VAL B C   
2764 O O   . VAL B 138 ? 1.1195 0.8617 0.8047 0.0679  -0.1929 0.0560  138 VAL B O   
2765 C CB  . VAL B 138 ? 1.1190 0.8339 0.8050 0.0538  -0.2029 0.0409  138 VAL B CB  
2766 C CG1 . VAL B 138 ? 1.0780 0.7855 0.7598 0.0504  -0.2066 0.0329  138 VAL B CG1 
2767 C CG2 . VAL B 138 ? 1.1700 0.8765 0.8597 0.0496  -0.2043 0.0406  138 VAL B CG2 
2768 N N   . CYS B 139 ? 1.0752 0.7909 0.7542 0.0618  -0.1959 0.0485  139 CYS B N   
2769 C CA  . CYS B 139 ? 1.0541 0.7819 0.7293 0.0662  -0.1949 0.0483  139 CYS B CA  
2770 C C   . CYS B 139 ? 1.0187 0.7450 0.6896 0.0629  -0.1999 0.0378  139 CYS B C   
2771 O O   . CYS B 139 ? 1.0091 0.7189 0.6787 0.0577  -0.2028 0.0330  139 CYS B O   
2772 C CB  . CYS B 139 ? 1.0684 0.7882 0.7423 0.0686  -0.1904 0.0548  139 CYS B CB  
2773 S SG  . CYS B 139 ? 1.2360 0.9746 0.9060 0.0755  -0.1878 0.0574  139 CYS B SG  
2774 N N   . LEU B 140 ? 1.0198 0.7642 0.6892 0.0660  -0.2005 0.0342  140 LEU B N   
2775 C CA  . LEU B 140 ? 0.9661 0.7116 0.6332 0.0634  -0.2045 0.0239  140 LEU B CA  
2776 C C   . LEU B 140 ? 0.9751 0.7280 0.6373 0.0669  -0.2031 0.0226  140 LEU B C   
2777 O O   . LEU B 140 ? 1.0518 0.8223 0.7138 0.0723  -0.1999 0.0269  140 LEU B O   
2778 C CB  . LEU B 140 ? 0.9728 0.7341 0.6440 0.0629  -0.2063 0.0182  140 LEU B CB  
2779 C CG  . LEU B 140 ? 0.9962 0.7532 0.6690 0.0581  -0.2105 0.0078  140 LEU B CG  
2780 C CD1 . LEU B 140 ? 1.0853 0.8589 0.7639 0.0580  -0.2112 0.0039  140 LEU B CD1 
2781 C CD2 . LEU B 140 ? 0.9883 0.7462 0.6573 0.0583  -0.2114 0.0011  140 LEU B CD2 
2782 N N   . LEU B 141 ? 0.9365 0.6767 0.5949 0.0639  -0.2056 0.0169  141 LEU B N   
2783 C CA  . LEU B 141 ? 0.9411 0.6868 0.5945 0.0664  -0.2051 0.0137  141 LEU B CA  
2784 C C   . LEU B 141 ? 0.9646 0.7129 0.6186 0.0635  -0.2087 0.0025  141 LEU B C   
2785 O O   . LEU B 141 ? 1.0021 0.7349 0.6566 0.0586  -0.2118 -0.0017 141 LEU B O   
2786 C CB  . LEU B 141 ? 0.9259 0.6535 0.5749 0.0654  -0.2045 0.0168  141 LEU B CB  
2787 C CG  . LEU B 141 ? 0.9285 0.6547 0.5770 0.0693  -0.1997 0.0273  141 LEU B CG  
2788 C CD1 . LEU B 141 ? 0.9420 0.6627 0.5960 0.0685  -0.1976 0.0344  141 LEU B CD1 
2789 C CD2 . LEU B 141 ? 0.9068 0.6160 0.5509 0.0675  -0.1997 0.0271  141 LEU B CD2 
2790 N N   . ASN B 142 ? 0.9971 0.7658 0.6517 0.0665  -0.2078 -0.0023 142 ASN B N   
2791 C CA  . ASN B 142 ? 0.9383 0.7123 0.5960 0.0638  -0.2101 -0.0132 142 ASN B CA  
2792 C C   . ASN B 142 ? 0.9445 0.7241 0.5982 0.0655  -0.2097 -0.0195 142 ASN B C   
2793 O O   . ASN B 142 ? 0.9948 0.7894 0.6454 0.0702  -0.2070 -0.0173 142 ASN B O   
2794 C CB  . ASN B 142 ? 0.9755 0.7702 0.6397 0.0648  -0.2092 -0.0159 142 ASN B CB  
2795 C CG  . ASN B 142 ? 1.0819 0.8818 0.7515 0.0616  -0.2108 -0.0274 142 ASN B CG  
2796 O OD1 . ASN B 142 ? 1.1423 0.9259 0.8135 0.0573  -0.2134 -0.0312 142 ASN B OD1 
2797 N ND2 . ASN B 142 ? 1.0000 0.8235 0.6733 0.0638  -0.2089 -0.0331 142 ASN B ND2 
2798 N N   . ASN B 143 ? 0.9247 0.6929 0.5789 0.0617  -0.2123 -0.0270 143 ASN B N   
2799 C CA  . ASN B 143 ? 0.9140 0.6876 0.5662 0.0625  -0.2121 -0.0353 143 ASN B CA  
2800 C C   . ASN B 143 ? 0.8912 0.6647 0.5351 0.0663  -0.2104 -0.0309 143 ASN B C   
2801 O O   . ASN B 143 ? 0.9263 0.7187 0.5684 0.0706  -0.2078 -0.0315 143 ASN B O   
2802 C CB  . ASN B 143 ? 0.9286 0.7259 0.5868 0.0638  -0.2103 -0.0434 143 ASN B CB  
2803 C CG  . ASN B 143 ? 0.9596 0.7558 0.6270 0.0596  -0.2118 -0.0490 143 ASN B CG  
2804 O OD1 . ASN B 143 ? 1.0062 0.7835 0.6751 0.0557  -0.2144 -0.0490 143 ASN B OD1 
2805 N ND2 . ASN B 143 ? 1.0200 0.8374 0.6940 0.0604  -0.2099 -0.0540 143 ASN B ND2 
2806 N N   . PHE B 144 ? 0.8773 0.6297 0.5166 0.0646  -0.2119 -0.0267 144 PHE B N   
2807 C CA  . PHE B 144 ? 0.8810 0.6296 0.5128 0.0674  -0.2105 -0.0226 144 PHE B CA  
2808 C C   . PHE B 144 ? 0.8815 0.6117 0.5097 0.0641  -0.2133 -0.0272 144 PHE B C   
2809 O O   . PHE B 144 ? 0.8800 0.5988 0.5115 0.0597  -0.2163 -0.0314 144 PHE B O   
2810 C CB  . PHE B 144 ? 0.8869 0.6291 0.5171 0.0691  -0.2084 -0.0109 144 PHE B CB  
2811 C CG  . PHE B 144 ? 0.8898 0.6125 0.5226 0.0644  -0.2104 -0.0077 144 PHE B CG  
2812 C CD1 . PHE B 144 ? 0.8893 0.6146 0.5278 0.0631  -0.2105 -0.0053 144 PHE B CD1 
2813 C CD2 . PHE B 144 ? 0.8931 0.5956 0.5225 0.0613  -0.2121 -0.0072 144 PHE B CD2 
2814 C CE1 . PHE B 144 ? 0.8920 0.6003 0.5327 0.0588  -0.2121 -0.0027 144 PHE B CE1 
2815 C CE2 . PHE B 144 ? 0.8957 0.5822 0.5276 0.0568  -0.2137 -0.0048 144 PHE B CE2 
2816 C CZ  . PHE B 144 ? 0.8952 0.5847 0.5327 0.0556  -0.2136 -0.0025 144 PHE B CZ  
2817 N N   . TYR B 145 ? 0.8837 0.6119 0.5052 0.0665  -0.2123 -0.0260 145 TYR B N   
2818 C CA  . TYR B 145 ? 0.8847 0.5964 0.5017 0.0641  -0.2147 -0.0295 145 TYR B CA  
2819 C C   . TYR B 145 ? 0.8891 0.5988 0.4993 0.0674  -0.2124 -0.0232 145 TYR B C   
2820 O O   . TYR B 145 ? 0.8889 0.6158 0.4975 0.0723  -0.2092 -0.0207 145 TYR B O   
2821 C CB  . TYR B 145 ? 0.8796 0.5969 0.4971 0.0636  -0.2159 -0.0404 145 TYR B CB  
2822 C CG  . TYR B 145 ? 0.8803 0.5801 0.4939 0.0609  -0.2186 -0.0439 145 TYR B CG  
2823 C CD1 . TYR B 145 ? 0.8798 0.5646 0.4969 0.0561  -0.2218 -0.0458 145 TYR B CD1 
2824 C CD2 . TYR B 145 ? 0.8815 0.5804 0.4879 0.0632  -0.2179 -0.0449 145 TYR B CD2 
2825 C CE1 . TYR B 145 ? 0.8851 0.5552 0.4989 0.0537  -0.2243 -0.0487 145 TYR B CE1 
2826 C CE2 . TYR B 145 ? 0.8821 0.5652 0.4848 0.0607  -0.2206 -0.0481 145 TYR B CE2 
2827 C CZ  . TYR B 145 ? 0.8814 0.5505 0.4880 0.0559  -0.2238 -0.0499 145 TYR B CZ  
2828 O OH  . TYR B 145 ? 0.9593 0.6141 0.5626 0.0535  -0.2264 -0.0528 145 TYR B OH  
2829 N N   . PRO B 146 ? 0.8931 0.5835 0.4998 0.0649  -0.2137 -0.0204 146 PRO B N   
2830 C CA  . PRO B 146 ? 0.8937 0.5651 0.5020 0.0592  -0.2173 -0.0224 146 PRO B CA  
2831 C C   . PRO B 146 ? 0.9111 0.5770 0.5250 0.0564  -0.2174 -0.0174 146 PRO B C   
2832 O O   . PRO B 146 ? 0.8964 0.5727 0.5133 0.0589  -0.2148 -0.0123 146 PRO B O   
2833 C CB  . PRO B 146 ? 0.8979 0.5548 0.5003 0.0584  -0.2174 -0.0197 146 PRO B CB  
2834 C CG  . PRO B 146 ? 0.8973 0.5654 0.4944 0.0633  -0.2152 -0.0206 146 PRO B CG  
2835 C CD  . PRO B 146 ? 0.8962 0.5845 0.4963 0.0678  -0.2118 -0.0171 146 PRO B CD  
2836 N N   . ARG B 147 ? 1.0693 0.7197 0.6847 0.0512  -0.2205 -0.0189 147 ARG B N   
2837 C CA  . ARG B 147 ? 1.0817 0.7261 0.7021 0.0480  -0.2208 -0.0150 147 ARG B CA  
2838 C C   . ARG B 147 ? 1.0983 0.7385 0.7186 0.0491  -0.2172 -0.0064 147 ARG B C   
2839 O O   . ARG B 147 ? 1.1105 0.7538 0.7354 0.0493  -0.2155 -0.0017 147 ARG B O   
2840 C CB  . ARG B 147 ? 1.0929 0.7230 0.7144 0.0424  -0.2247 -0.0185 147 ARG B CB  
2841 C CG  . ARG B 147 ? 1.1097 0.7345 0.7365 0.0386  -0.2254 -0.0157 147 ARG B CG  
2842 C CD  . ARG B 147 ? 1.1914 0.8013 0.8176 0.0333  -0.2281 -0.0168 147 ARG B CD  
2843 N NE  . ARG B 147 ? 1.3236 0.9300 0.9550 0.0293  -0.2295 -0.0159 147 ARG B NE  
2844 C CZ  . ARG B 147 ? 1.4664 1.0722 1.1009 0.0265  -0.2328 -0.0198 147 ARG B CZ  
2845 N NH1 . ARG B 147 ? 1.3982 1.0060 1.0320 0.0272  -0.2348 -0.0250 147 ARG B NH1 
2846 N NH2 . ARG B 147 ? 1.4523 1.0557 1.0913 0.0230  -0.2337 -0.0182 147 ARG B NH2 
2847 N N   . GLU B 148 ? 0.9530 0.5862 0.5688 0.0499  -0.2158 -0.0042 148 GLU B N   
2848 C CA  . GLU B 148 ? 0.9416 0.5684 0.5589 0.0503  -0.2119 0.0036  148 GLU B CA  
2849 C C   . GLU B 148 ? 0.9927 0.6335 0.6127 0.0557  -0.2072 0.0108  148 GLU B C   
2850 O O   . GLU B 148 ? 1.0581 0.7126 0.6753 0.0607  -0.2056 0.0114  148 GLU B O   
2851 C CB  . GLU B 148 ? 1.0194 0.6378 0.6317 0.0505  -0.2110 0.0040  148 GLU B CB  
2852 C CG  . GLU B 148 ? 1.1334 0.7388 0.7430 0.0453  -0.2156 -0.0028 148 GLU B CG  
2853 C CD  . GLU B 148 ? 1.1121 0.7202 0.7153 0.0472  -0.2177 -0.0083 148 GLU B CD  
2854 O OE1 . GLU B 148 ? 1.1351 0.7527 0.7351 0.0523  -0.2150 -0.0062 148 GLU B OE1 
2855 O OE2 . GLU B 148 ? 1.0999 0.7016 0.7016 0.0438  -0.2219 -0.0147 148 GLU B OE2 
2856 N N   . ALA B 149 ? 0.9857 0.6240 0.6115 0.0546  -0.2050 0.0162  149 ALA B N   
2857 C CA  . ALA B 149 ? 0.9941 0.6451 0.6236 0.0596  -0.2004 0.0239  149 ALA B CA  
2858 C C   . ALA B 149 ? 1.0632 0.7041 0.6987 0.0578  -0.1965 0.0308  149 ALA B C   
2859 O O   . ALA B 149 ? 1.1821 0.8085 0.8195 0.0521  -0.1982 0.0281  149 ALA B O   
2860 C CB  . ALA B 149 ? 0.9137 0.5792 0.5455 0.0607  -0.2022 0.0214  149 ALA B CB  
2861 N N   . LYS B 150 ? 1.0105 0.6604 0.6497 0.0628  -0.1910 0.0397  150 LYS B N   
2862 C CA  . LYS B 150 ? 1.0190 0.6613 0.6656 0.0621  -0.1861 0.0470  150 LYS B CA  
2863 C C   . LYS B 150 ? 1.0061 0.6623 0.6575 0.0658  -0.1838 0.0525  150 LYS B C   
2864 O O   . LYS B 150 ? 1.0490 0.7227 0.6993 0.0717  -0.1822 0.0562  150 LYS B O   
2865 C CB  . LYS B 150 ? 1.1019 0.7398 0.7502 0.0649  -0.1800 0.0542  150 LYS B CB  
2866 C CG  . LYS B 150 ? 1.1558 0.7798 0.7997 0.0612  -0.1818 0.0491  150 LYS B CG  
2867 C CD  . LYS B 150 ? 1.2130 0.8460 0.8489 0.0651  -0.1837 0.0468  150 LYS B CD  
2868 C CE  . LYS B 150 ? 1.2263 0.8452 0.8575 0.0612  -0.1860 0.0414  150 LYS B CE  
2869 N NZ  . LYS B 150 ? 1.1907 0.8180 0.8138 0.0648  -0.1879 0.0385  150 LYS B NZ  
2870 N N   . VAL B 151 ? 0.9689 0.6184 0.6258 0.0622  -0.1839 0.0528  151 VAL B N   
2871 C CA  . VAL B 151 ? 1.0182 0.6790 0.6801 0.0649  -0.1821 0.0575  151 VAL B CA  
2872 C C   . VAL B 151 ? 1.0912 0.7419 0.7614 0.0637  -0.1765 0.0643  151 VAL B C   
2873 O O   . VAL B 151 ? 1.1687 0.8066 0.8414 0.0578  -0.1780 0.0605  151 VAL B O   
2874 C CB  . VAL B 151 ? 1.0786 0.7425 0.7393 0.0614  -0.1881 0.0501  151 VAL B CB  
2875 C CG1 . VAL B 151 ? 1.1338 0.8096 0.7997 0.0642  -0.1862 0.0551  151 VAL B CG1 
2876 C CG2 . VAL B 151 ? 1.0426 0.7157 0.6968 0.0622  -0.1928 0.0427  151 VAL B CG2 
2877 N N   . GLN B 152 ? 1.1198 0.7767 0.7947 0.0694  -0.1696 0.0744  152 GLN B N   
2878 C CA  . GLN B 152 ? 1.1339 0.7822 0.8183 0.0691  -0.1629 0.0816  152 GLN B CA  
2879 C C   . GLN B 152 ? 1.1010 0.7620 0.7909 0.0730  -0.1604 0.0881  152 GLN B C   
2880 O O   . GLN B 152 ? 1.1254 0.8051 0.8131 0.0788  -0.1606 0.0917  152 GLN B O   
2881 C CB  . GLN B 152 ? 1.1457 0.7912 0.8339 0.0727  -0.1557 0.0894  152 GLN B CB  
2882 C CG  . GLN B 152 ? 1.1615 0.7892 0.8485 0.0672  -0.1561 0.0838  152 GLN B CG  
2883 C CD  . GLN B 152 ? 1.1851 0.8100 0.8769 0.0708  -0.1485 0.0918  152 GLN B CD  
2884 O OE1 . GLN B 152 ? 1.1010 0.7391 0.7957 0.0782  -0.1434 0.1017  152 GLN B OE1 
2885 N NE2 . GLN B 152 ? 1.2554 0.8641 0.9486 0.0658  -0.1474 0.0878  152 GLN B NE2 
2886 N N   . TRP B 153 ? 1.0866 0.7380 0.7837 0.0697  -0.1580 0.0893  153 TRP B N   
2887 C CA  . TRP B 153 ? 1.0857 0.7467 0.7888 0.0729  -0.1555 0.0955  153 TRP B CA  
2888 C C   . TRP B 153 ? 1.1306 0.7912 0.8441 0.0774  -0.1456 0.1074  153 TRP B C   
2889 O O   . TRP B 153 ? 1.1612 0.8063 0.8804 0.0744  -0.1409 0.1080  153 TRP B O   
2890 C CB  . TRP B 153 ? 1.1107 0.7623 0.8155 0.0665  -0.1590 0.0892  153 TRP B CB  
2891 C CG  . TRP B 153 ? 1.1392 0.7951 0.8359 0.0633  -0.1678 0.0797  153 TRP B CG  
2892 C CD1 . TRP B 153 ? 1.1167 0.7625 0.8076 0.0573  -0.1736 0.0700  153 TRP B CD1 
2893 C CD2 . TRP B 153 ? 1.1183 0.7900 0.8129 0.0658  -0.1714 0.0791  153 TRP B CD2 
2894 N NE1 . TRP B 153 ? 1.1074 0.7612 0.7935 0.0562  -0.1802 0.0638  153 TRP B NE1 
2895 C CE2 . TRP B 153 ? 1.1152 0.7849 0.8035 0.0611  -0.1789 0.0687  153 TRP B CE2 
2896 C CE3 . TRP B 153 ? 1.0663 0.7547 0.7646 0.0716  -0.1687 0.0863  153 TRP B CE3 
2897 C CZ2 . TRP B 153 ? 1.1098 0.7926 0.7959 0.0618  -0.1835 0.0650  153 TRP B CZ2 
2898 C CZ3 . TRP B 153 ? 1.0549 0.7570 0.7502 0.0720  -0.1737 0.0822  153 TRP B CZ3 
2899 C CH2 . TRP B 153 ? 1.1122 0.8110 0.8017 0.0670  -0.1809 0.0714  153 TRP B CH2 
2900 N N   . LYS B 154 ? 1.1281 0.8063 0.8447 0.0847  -0.1421 0.1167  154 LYS B N   
2901 C CA  . LYS B 154 ? 1.0630 0.7436 0.7907 0.0902  -0.1322 0.1296  154 LYS B CA  
2902 C C   . LYS B 154 ? 1.0863 0.7777 0.8197 0.0933  -0.1304 0.1355  154 LYS B C   
2903 O O   . LYS B 154 ? 1.1593 0.8702 0.8885 0.0975  -0.1337 0.1369  154 LYS B O   
2904 C CB  . LYS B 154 ? 1.0102 0.7045 0.7367 0.0976  -0.1283 0.1378  154 LYS B CB  
2905 C CG  . LYS B 154 ? 1.0183 0.7001 0.7418 0.0952  -0.1277 0.1345  154 LYS B CG  
2906 C CD  . LYS B 154 ? 1.0159 0.7124 0.7385 0.1031  -0.1235 0.1435  154 LYS B CD  
2907 C CE  . LYS B 154 ? 0.9680 0.6510 0.6887 0.1008  -0.1221 0.1411  154 LYS B CE  
2908 N NZ  . LYS B 154 ? 1.0021 0.7003 0.7205 0.1083  -0.1187 0.1491  154 LYS B NZ  
2909 N N   . VAL B 155 ? 1.1133 0.7927 0.8568 0.0911  -0.1251 0.1385  155 VAL B N   
2910 C CA  . VAL B 155 ? 1.1334 0.8215 0.8840 0.0944  -0.1221 0.1454  155 VAL B CA  
2911 C C   . VAL B 155 ? 1.1874 0.8798 0.9503 0.1015  -0.1108 0.1601  155 VAL B C   
2912 O O   . VAL B 155 ? 1.1917 0.8692 0.9625 0.0999  -0.1041 0.1623  155 VAL B O   
2913 C CB  . VAL B 155 ? 1.0851 0.7579 0.8385 0.0871  -0.1241 0.1382  155 VAL B CB  
2914 C CG1 . VAL B 155 ? 1.1031 0.7687 0.8454 0.0797  -0.1342 0.1241  155 VAL B CG1 
2915 C CG2 . VAL B 155 ? 1.1228 0.7772 0.8878 0.0841  -0.1159 0.1403  155 VAL B CG2 
2916 N N   . ASP B 156 ? 1.1702 0.8843 0.9352 0.1094  -0.1086 0.1702  156 ASP B N   
2917 C CA  . ASP B 156 ? 1.1443 0.8669 0.9209 0.1176  -0.0978 0.1859  156 ASP B CA  
2918 C C   . ASP B 156 ? 1.1275 0.8433 0.9058 0.1189  -0.0928 0.1890  156 ASP B C   
2919 O O   . ASP B 156 ? 1.1435 0.8497 0.9343 0.1205  -0.0830 0.1970  156 ASP B O   
2920 C CB  . ASP B 156 ? 1.2019 0.9144 0.9926 0.1172  -0.0902 0.1917  156 ASP B CB  
2921 C CG  . ASP B 156 ? 1.2194 0.9405 1.0090 0.1169  -0.0945 0.1903  156 ASP B CG  
2922 O OD1 . ASP B 156 ? 1.2020 0.9345 0.9800 0.1158  -0.1037 0.1831  156 ASP B OD1 
2923 O OD2 . ASP B 156 ? 1.3026 1.0191 1.1034 0.1178  -0.0882 0.1962  156 ASP B OD2 
2924 N N   . ASN B 157 ? 1.1888 0.9094 0.9548 0.1180  -0.0995 0.1822  157 ASN B N   
2925 C CA  . ASN B 157 ? 1.1757 0.8905 0.9405 0.1187  -0.0966 0.1834  157 ASN B CA  
2926 C C   . ASN B 157 ? 1.1141 0.8020 0.8847 0.1115  -0.0934 0.1778  157 ASN B C   
2927 O O   . ASN B 157 ? 1.1515 0.8326 0.9265 0.1126  -0.0876 0.1818  157 ASN B O   
2928 C CB  . ASN B 157 ? 1.1540 0.8850 0.9270 0.1287  -0.0873 0.1998  157 ASN B CB  
2929 C CG  . ASN B 157 ? 1.2819 1.0366 1.0445 0.1343  -0.0915 0.2014  157 ASN B CG  
2930 O OD1 . ASN B 157 ? 1.3341 1.0896 1.0836 0.1304  -0.1006 0.1895  157 ASN B OD1 
2931 N ND2 . ASN B 157 ? 1.2511 1.0261 1.0200 0.1437  -0.0844 0.2162  157 ASN B ND2 
2932 N N   . ALA B 158 ? 1.0634 0.7367 0.8344 0.1039  -0.0969 0.1684  158 ALA B N   
2933 C CA  . ALA B 158 ? 1.0790 0.7286 0.8548 0.0961  -0.0948 0.1610  158 ALA B CA  
2934 C C   . ALA B 158 ? 1.1237 0.7651 0.8861 0.0881  -0.1059 0.1455  158 ALA B C   
2935 O O   . ALA B 158 ? 1.1152 0.7581 0.8723 0.0848  -0.1127 0.1388  158 ALA B O   
2936 C CB  . ALA B 158 ? 1.1101 0.7498 0.8990 0.0937  -0.0885 0.1631  158 ALA B CB  
2937 N N   . LEU B 159 ? 1.1068 0.7401 0.8641 0.0854  -0.1076 0.1404  159 LEU B N   
2938 C CA  . LEU B 159 ? 1.0847 0.7095 0.8305 0.0780  -0.1173 0.1264  159 LEU B CA  
2939 C C   . LEU B 159 ? 1.0650 0.6756 0.8145 0.0699  -0.1188 0.1181  159 LEU B C   
2940 O O   . LEU B 159 ? 1.1210 0.7205 0.8824 0.0675  -0.1112 0.1203  159 LEU B O   
2941 C CB  . LEU B 159 ? 1.0568 0.6728 0.7993 0.0760  -0.1170 0.1231  159 LEU B CB  
2942 C CG  . LEU B 159 ? 1.0953 0.7018 0.8269 0.0684  -0.1263 0.1092  159 LEU B CG  
2943 C CD1 . LEU B 159 ? 1.0948 0.7147 0.8137 0.0700  -0.1357 0.1046  159 LEU B CD1 
2944 C CD2 . LEU B 159 ? 1.0670 0.6639 0.7975 0.0664  -0.1247 0.1069  159 LEU B CD2 
2945 N N   . GLN B 160 ? 1.0467 0.6583 0.7865 0.0656  -0.1283 0.1086  160 GLN B N   
2946 C CA  . GLN B 160 ? 1.1115 0.7125 0.8533 0.0582  -0.1308 0.1008  160 GLN B CA  
2947 C C   . GLN B 160 ? 1.1311 0.7233 0.8640 0.0510  -0.1387 0.0885  160 GLN B C   
2948 O O   . GLN B 160 ? 1.1834 0.7824 0.9054 0.0518  -0.1460 0.0846  160 GLN B O   
2949 C CB  . GLN B 160 ? 1.0936 0.7048 0.8337 0.0599  -0.1345 0.1017  160 GLN B CB  
2950 C CG  . GLN B 160 ? 1.1220 0.7381 0.8737 0.0649  -0.1262 0.1124  160 GLN B CG  
2951 C CD  . GLN B 160 ? 1.1617 0.7774 0.9156 0.0621  -0.1283 0.1099  160 GLN B CD  
2952 O OE1 . GLN B 160 ? 1.1308 0.7500 0.8759 0.0593  -0.1368 0.1027  160 GLN B OE1 
2953 N NE2 . GLN B 160 ? 1.1743 0.7855 0.9404 0.0629  -0.1201 0.1158  160 GLN B NE2 
2954 N N   . SER B 161 ? 1.1304 0.7083 0.8684 0.0439  -0.1368 0.0826  161 SER B N   
2955 C CA  . SER B 161 ? 1.1750 0.7445 0.9061 0.0367  -0.1432 0.0715  161 SER B CA  
2956 C C   . SER B 161 ? 1.1918 0.7552 0.9251 0.0296  -0.1457 0.0642  161 SER B C   
2957 O O   . SER B 161 ? 1.2340 0.7929 0.9777 0.0281  -0.1393 0.0662  161 SER B O   
2958 C CB  . SER B 161 ? 1.1104 0.6698 0.8457 0.0343  -0.1383 0.0704  161 SER B CB  
2959 O OG  . SER B 161 ? 1.0876 0.6382 0.8193 0.0262  -0.1432 0.0596  161 SER B OG  
2960 N N   . GLY B 162 ? 1.2281 0.7919 0.9521 0.0253  -0.1546 0.0558  162 GLY B N   
2961 C CA  . GLY B 162 ? 1.2537 0.8129 0.9786 0.0184  -0.1577 0.0485  162 GLY B CA  
2962 C C   . GLY B 162 ? 1.2369 0.8035 0.9598 0.0196  -0.1616 0.0492  162 GLY B C   
2963 O O   . GLY B 162 ? 1.3064 0.8700 1.0297 0.0140  -0.1644 0.0434  162 GLY B O   
2964 N N   . ASN B 163 ? 1.2244 0.8014 0.9453 0.0266  -0.1617 0.0560  163 ASN B N   
2965 C CA  . ASN B 163 ? 1.2197 0.8046 0.9393 0.0280  -0.1651 0.0570  163 ASN B CA  
2966 C C   . ASN B 163 ? 1.2640 0.8588 0.9738 0.0302  -0.1730 0.0544  163 ASN B C   
2967 O O   . ASN B 163 ? 1.2571 0.8606 0.9658 0.0323  -0.1756 0.0557  163 ASN B O   
2968 C CB  . ASN B 163 ? 1.1555 0.7464 0.8826 0.0342  -0.1582 0.0669  163 ASN B CB  
2969 C CG  . ASN B 163 ? 1.2263 0.8229 0.9544 0.0410  -0.1536 0.0748  163 ASN B CG  
2970 O OD1 . ASN B 163 ? 1.2207 0.8205 0.9414 0.0424  -0.1571 0.0729  163 ASN B OD1 
2971 N ND2 . ASN B 163 ? 1.1869 0.7852 0.9244 0.0455  -0.1452 0.0839  163 ASN B ND2 
2972 N N   . SER B 164 ? 1.2245 0.8184 0.9278 0.0296  -0.1766 0.0505  164 SER B N   
2973 C CA  . SER B 164 ? 1.1504 0.7539 0.8456 0.0319  -0.1831 0.0478  164 SER B CA  
2974 C C   . SER B 164 ? 1.1964 0.7938 0.8859 0.0264  -0.1892 0.0392  164 SER B C   
2975 O O   . SER B 164 ? 1.2061 0.7935 0.8962 0.0225  -0.1879 0.0364  164 SER B O   
2976 C CB  . SER B 164 ? 1.1582 0.7704 0.8510 0.0387  -0.1808 0.0531  164 SER B CB  
2977 O OG  . SER B 164 ? 1.1651 0.7694 0.8567 0.0378  -0.1788 0.0523  164 SER B OG  
2978 N N   . GLN B 165 ? 1.1973 0.8014 0.8819 0.0263  -0.1954 0.0351  165 GLN B N   
2979 C CA  . GLN B 165 ? 1.1712 0.7720 0.8506 0.0224  -0.2012 0.0278  165 GLN B CA  
2980 C C   . GLN B 165 ? 1.1247 0.7360 0.7991 0.0264  -0.2048 0.0264  165 GLN B C   
2981 O O   . GLN B 165 ? 1.1263 0.7482 0.8016 0.0297  -0.2052 0.0282  165 GLN B O   
2982 C CB  . GLN B 165 ? 1.1296 0.7272 0.8104 0.0167  -0.2049 0.0234  165 GLN B CB  
2983 C CG  . GLN B 165 ? 1.1477 0.7351 0.8287 0.0104  -0.2058 0.0188  165 GLN B CG  
2984 C CD  . GLN B 165 ? 1.3058 0.8911 0.9900 0.0052  -0.2073 0.0162  165 GLN B CD  
2985 O OE1 . GLN B 165 ? 1.2329 0.8234 0.9187 0.0062  -0.2083 0.0176  165 GLN B OE1 
2986 N NE2 . GLN B 165 ? 1.3802 0.9587 1.0656 -0.0005 -0.2073 0.0123  165 GLN B NE2 
2987 N N   . GLU B 166 ? 1.0334 0.6425 0.7030 0.0260  -0.2072 0.0226  166 GLU B N   
2988 C CA  . GLU B 166 ? 1.0059 0.6248 0.6712 0.0298  -0.2097 0.0205  166 GLU B CA  
2989 C C   . GLU B 166 ? 0.9797 0.5964 0.6422 0.0262  -0.2154 0.0133  166 GLU B C   
2990 O O   . GLU B 166 ? 0.9724 0.5796 0.6349 0.0212  -0.2172 0.0105  166 GLU B O   
2991 C CB  . GLU B 166 ? 1.0109 0.6312 0.6731 0.0340  -0.2067 0.0233  166 GLU B CB  
2992 C CG  . GLU B 166 ? 1.0319 0.6430 0.6898 0.0312  -0.2087 0.0189  166 GLU B CG  
2993 C CD  . GLU B 166 ? 1.0470 0.6609 0.7015 0.0357  -0.2060 0.0215  166 GLU B CD  
2994 O OE1 . GLU B 166 ? 0.9884 0.6102 0.6447 0.0408  -0.2017 0.0278  166 GLU B OE1 
2995 O OE2 . GLU B 166 ? 1.0861 0.6949 0.7361 0.0344  -0.2082 0.0174  166 GLU B OE2 
2996 N N   . SER B 167 ? 0.9584 0.5853 0.6196 0.0288  -0.2178 0.0105  167 SER B N   
2997 C CA  . SER B 167 ? 0.9123 0.5390 0.5726 0.0262  -0.2224 0.0041  167 SER B CA  
2998 C C   . SER B 167 ? 0.9105 0.5466 0.5680 0.0302  -0.2229 0.0010  167 SER B C   
2999 O O   . SER B 167 ? 0.9524 0.6002 0.6104 0.0346  -0.2208 0.0029  167 SER B O   
3000 C CB  . SER B 167 ? 0.9013 0.5312 0.5661 0.0239  -0.2246 0.0026  167 SER B CB  
3001 O OG  . SER B 167 ? 0.9493 0.5779 0.6146 0.0212  -0.2285 -0.0026 167 SER B OG  
3002 N N   . VAL B 168 ? 0.8988 0.5305 0.5536 0.0287  -0.2255 -0.0038 168 VAL B N   
3003 C CA  . VAL B 168 ? 0.8956 0.5349 0.5476 0.0321  -0.2258 -0.0076 168 VAL B CA  
3004 C C   . VAL B 168 ? 0.8904 0.5313 0.5454 0.0300  -0.2291 -0.0139 168 VAL B C   
3005 O O   . VAL B 168 ? 0.8904 0.5219 0.5457 0.0261  -0.2316 -0.0156 168 VAL B O   
3006 C CB  . VAL B 168 ? 0.9151 0.5476 0.5614 0.0329  -0.2250 -0.0074 168 VAL B CB  
3007 C CG1 . VAL B 168 ? 1.0139 0.6566 0.6572 0.0374  -0.2243 -0.0103 168 VAL B CG1 
3008 C CG2 . VAL B 168 ? 0.9235 0.5505 0.5690 0.0335  -0.2215 -0.0008 168 VAL B CG2 
3009 N N   . THR B 169 ? 0.9569 0.6104 0.6146 0.0326  -0.2286 -0.0173 169 THR B N   
3010 C CA  . THR B 169 ? 0.9095 0.5654 0.5713 0.0312  -0.2306 -0.0236 169 THR B CA  
3011 C C   . THR B 169 ? 0.9504 0.6008 0.6082 0.0313  -0.2317 -0.0273 169 THR B C   
3012 O O   . THR B 169 ? 0.9855 0.6333 0.6371 0.0332  -0.2306 -0.0257 169 THR B O   
3013 C CB  . THR B 169 ? 0.8766 0.5485 0.5432 0.0340  -0.2291 -0.0274 169 THR B CB  
3014 O OG1 . THR B 169 ? 0.8765 0.5576 0.5389 0.0382  -0.2268 -0.0286 169 THR B OG1 
3015 C CG2 . THR B 169 ? 0.8769 0.5549 0.5472 0.0341  -0.2281 -0.0236 169 THR B CG2 
3016 N N   . GLU B 170 ? 0.9251 0.5740 0.5871 0.0294  -0.2335 -0.0321 170 GLU B N   
3017 C CA  . GLU B 170 ? 0.9666 0.6115 0.6257 0.0298  -0.2343 -0.0361 170 GLU B CA  
3018 C C   . GLU B 170 ? 0.9593 0.6165 0.6190 0.0336  -0.2321 -0.0416 170 GLU B C   
3019 O O   . GLU B 170 ? 0.9142 0.5840 0.5769 0.0358  -0.2300 -0.0423 170 GLU B O   
3020 C CB  . GLU B 170 ? 0.9554 0.5940 0.6196 0.0264  -0.2367 -0.0383 170 GLU B CB  
3021 C CG  . GLU B 170 ? 1.1585 0.7843 0.8183 0.0233  -0.2391 -0.0353 170 GLU B CG  
3022 C CD  . GLU B 170 ? 1.2414 0.8624 0.8943 0.0246  -0.2394 -0.0371 170 GLU B CD  
3023 O OE1 . GLU B 170 ? 1.1581 0.7836 0.8116 0.0270  -0.2386 -0.0421 170 GLU B OE1 
3024 O OE2 . GLU B 170 ? 1.3044 0.9171 0.9516 0.0232  -0.2401 -0.0339 170 GLU B OE2 
3025 N N   . GLN B 171 ? 0.9032 0.5579 0.5602 0.0344  -0.2324 -0.0458 171 GLN B N   
3026 C CA  . GLN B 171 ? 0.9099 0.5766 0.5671 0.0379  -0.2301 -0.0517 171 GLN B CA  
3027 C C   . GLN B 171 ? 0.9705 0.6479 0.6381 0.0377  -0.2286 -0.0576 171 GLN B C   
3028 O O   . GLN B 171 ? 1.0150 0.6871 0.6893 0.0351  -0.2297 -0.0596 171 GLN B O   
3029 C CB  . GLN B 171 ? 0.8943 0.5545 0.5467 0.0385  -0.2308 -0.0552 171 GLN B CB  
3030 C CG  . GLN B 171 ? 0.9161 0.5839 0.5616 0.0425  -0.2288 -0.0567 171 GLN B CG  
3031 C CD  . GLN B 171 ? 0.9195 0.5803 0.5600 0.0428  -0.2297 -0.0604 171 GLN B CD  
3032 O OE1 . GLN B 171 ? 0.9104 0.5604 0.5527 0.0401  -0.2320 -0.0615 171 GLN B OE1 
3033 N NE2 . GLN B 171 ? 0.9206 0.5884 0.5551 0.0464  -0.2279 -0.0620 171 GLN B NE2 
3034 N N   . ASP B 172 ? 0.9901 0.6834 0.6596 0.0404  -0.2259 -0.0604 172 ASP B N   
3035 C CA  . ASP B 172 ? 0.9670 0.6724 0.6473 0.0401  -0.2238 -0.0673 172 ASP B CA  
3036 C C   . ASP B 172 ? 1.0264 0.7313 0.7111 0.0399  -0.2228 -0.0752 172 ASP B C   
3037 O O   . ASP B 172 ? 1.0163 0.7234 0.6956 0.0422  -0.2219 -0.0785 172 ASP B O   
3038 C CB  . ASP B 172 ? 0.9815 0.7064 0.6624 0.0431  -0.2209 -0.0693 172 ASP B CB  
3039 C CG  . ASP B 172 ? 1.0339 0.7707 0.7263 0.0418  -0.2191 -0.0738 172 ASP B CG  
3040 O OD1 . ASP B 172 ? 1.0773 0.8076 0.7742 0.0392  -0.2206 -0.0700 172 ASP B OD1 
3041 O OD2 . ASP B 172 ? 1.0802 0.8338 0.7776 0.0434  -0.2160 -0.0815 172 ASP B OD2 
3042 N N   . SER B 173 ? 1.0862 0.7884 0.7816 0.0374  -0.2225 -0.0781 173 SER B N   
3043 C CA  . SER B 173 ? 1.0230 0.7242 0.7249 0.0372  -0.2209 -0.0853 173 SER B CA  
3044 C C   . SER B 173 ? 0.9980 0.7161 0.7048 0.0394  -0.2166 -0.0951 173 SER B C   
3045 O O   . SER B 173 ? 1.0340 0.7527 0.7475 0.0393  -0.2144 -0.1022 173 SER B O   
3046 C CB  . SER B 173 ? 1.0169 0.7124 0.7306 0.0342  -0.2209 -0.0851 173 SER B CB  
3047 O OG  . SER B 173 ? 1.0367 0.7446 0.7616 0.0336  -0.2180 -0.0889 173 SER B OG  
3048 N N   . LYS B 174 ? 1.0612 0.7941 0.7654 0.0413  -0.2152 -0.0957 174 LYS B N   
3049 C CA  . LYS B 174 ? 1.0895 0.8418 0.7982 0.0433  -0.2110 -0.1053 174 LYS B CA  
3050 C C   . LYS B 174 ? 1.0624 0.8218 0.7591 0.0469  -0.2108 -0.1047 174 LYS B C   
3051 O O   . LYS B 174 ? 1.0541 0.8179 0.7497 0.0483  -0.2089 -0.1116 174 LYS B O   
3052 C CB  . LYS B 174 ? 1.1451 0.9132 0.8627 0.0426  -0.2089 -0.1074 174 LYS B CB  
3053 C CG  . LYS B 174 ? 1.1531 0.9255 0.8873 0.0400  -0.2056 -0.1154 174 LYS B CG  
3054 C CD  . LYS B 174 ? 1.2655 1.0478 1.0076 0.0384  -0.2048 -0.1147 174 LYS B CD  
3055 C CE  . LYS B 174 ? 1.2555 1.0216 0.9958 0.0363  -0.2088 -0.1044 174 LYS B CE  
3056 N NZ  . LYS B 174 ? 1.2407 1.0158 0.9890 0.0347  -0.2080 -0.1039 174 LYS B NZ  
3057 N N   . ASP B 175 ? 1.0827 0.8433 0.7706 0.0484  -0.2125 -0.0964 175 ASP B N   
3058 C CA  . ASP B 175 ? 1.0339 0.8025 0.7111 0.0522  -0.2119 -0.0942 175 ASP B CA  
3059 C C   . ASP B 175 ? 0.9780 0.7285 0.6436 0.0527  -0.2150 -0.0853 175 ASP B C   
3060 O O   . ASP B 175 ? 0.9666 0.7217 0.6233 0.0559  -0.2144 -0.0825 175 ASP B O   
3061 C CB  . ASP B 175 ? 0.9667 0.7539 0.6441 0.0544  -0.2102 -0.0914 175 ASP B CB  
3062 C CG  . ASP B 175 ? 0.9999 0.7798 0.6793 0.0525  -0.2123 -0.0833 175 ASP B CG  
3063 O OD1 . ASP B 175 ? 0.9949 0.7597 0.6669 0.0523  -0.2148 -0.0742 175 ASP B OD1 
3064 O OD2 . ASP B 175 ? 1.0630 0.8526 0.7518 0.0509  -0.2111 -0.0866 175 ASP B OD2 
3065 N N   . SER B 176 ? 0.9758 0.7068 0.6417 0.0495  -0.2181 -0.0811 176 SER B N   
3066 C CA  . SER B 176 ? 1.0089 0.7225 0.6652 0.0491  -0.2210 -0.0738 176 SER B CA  
3067 C C   . SER B 176 ? 1.0172 0.7323 0.6662 0.0512  -0.2209 -0.0649 176 SER B C   
3068 O O   . SER B 176 ? 0.9325 0.6397 0.5729 0.0524  -0.2215 -0.0605 176 SER B O   
3069 C CB  . SER B 176 ? 1.0062 0.7153 0.6567 0.0504  -0.2210 -0.0781 176 SER B CB  
3070 O OG  . SER B 176 ? 0.9480 0.6548 0.6060 0.0487  -0.2207 -0.0859 176 SER B OG  
3071 N N   . THR B 177 ? 1.0612 0.7862 0.7143 0.0515  -0.2198 -0.0621 177 THR B N   
3072 C CA  . THR B 177 ? 1.0485 0.7748 0.6966 0.0535  -0.2192 -0.0529 177 THR B CA  
3073 C C   . THR B 177 ? 1.0359 0.7476 0.6855 0.0501  -0.2214 -0.0464 177 THR B C   
3074 O O   . THR B 177 ? 1.0466 0.7509 0.7019 0.0465  -0.2233 -0.0488 177 THR B O   
3075 C CB  . THR B 177 ? 1.0449 0.7936 0.6963 0.0567  -0.2163 -0.0533 177 THR B CB  
3076 O OG1 . THR B 177 ? 1.0563 0.8100 0.7171 0.0541  -0.2165 -0.0568 177 THR B OG1 
3077 C CG2 . THR B 177 ? 1.0367 0.8026 0.6866 0.0600  -0.2137 -0.0602 177 THR B CG2 
3078 N N   . TYR B 178 ? 1.0127 0.7208 0.6577 0.0514  -0.2208 -0.0378 178 TYR B N   
3079 C CA  . TYR B 178 ? 0.8915 0.5870 0.5378 0.0484  -0.2222 -0.0315 178 TYR B CA  
3080 C C   . TYR B 178 ? 0.8788 0.5857 0.5281 0.0503  -0.2201 -0.0265 178 TYR B C   
3081 O O   . TYR B 178 ? 0.9044 0.6285 0.5537 0.0543  -0.2176 -0.0267 178 TYR B O   
3082 C CB  . TYR B 178 ? 0.8838 0.5642 0.5235 0.0478  -0.2225 -0.0258 178 TYR B CB  
3083 C CG  . TYR B 178 ? 0.8837 0.5516 0.5201 0.0455  -0.2249 -0.0300 178 TYR B CG  
3084 C CD1 . TYR B 178 ? 0.9406 0.5948 0.5790 0.0407  -0.2279 -0.0304 178 TYR B CD1 
3085 C CD2 . TYR B 178 ? 0.8830 0.5541 0.5145 0.0481  -0.2242 -0.0334 178 TYR B CD2 
3086 C CE1 . TYR B 178 ? 0.9920 0.6361 0.6277 0.0388  -0.2301 -0.0338 178 TYR B CE1 
3087 C CE2 . TYR B 178 ? 0.9158 0.5756 0.5443 0.0460  -0.2265 -0.0371 178 TYR B CE2 
3088 C CZ  . TYR B 178 ? 0.9631 0.6095 0.5938 0.0414  -0.2295 -0.0372 178 TYR B CZ  
3089 O OH  . TYR B 178 ? 1.0404 0.6769 0.6685 0.0396  -0.2317 -0.0405 178 TYR B OH  
3090 N N   . SER B 179 ? 0.8809 0.5790 0.5330 0.0475  -0.2211 -0.0221 179 SER B N   
3091 C CA  . SER B 179 ? 0.8823 0.5883 0.5368 0.0492  -0.2191 -0.0161 179 SER B CA  
3092 C C   . SER B 179 ? 0.8888 0.5793 0.5427 0.0466  -0.2194 -0.0093 179 SER B C   
3093 O O   . SER B 179 ? 0.9668 0.6431 0.6209 0.0423  -0.2220 -0.0108 179 SER B O   
3094 C CB  . SER B 179 ? 0.9046 0.6222 0.5664 0.0483  -0.2196 -0.0200 179 SER B CB  
3095 O OG  . SER B 179 ? 0.8991 0.6317 0.5628 0.0502  -0.2188 -0.0275 179 SER B OG  
3096 N N   . LEU B 180 ? 0.9108 0.6052 0.5646 0.0494  -0.2164 -0.0018 180 LEU B N   
3097 C CA  . LEU B 180 ? 0.9305 0.6113 0.5845 0.0473  -0.2154 0.0046  180 LEU B CA  
3098 C C   . LEU B 180 ? 0.9401 0.6273 0.5988 0.0482  -0.2137 0.0096  180 LEU B C   
3099 O O   . LEU B 180 ? 0.9497 0.6533 0.6099 0.0524  -0.2117 0.0113  180 LEU B O   
3100 C CB  . LEU B 180 ? 0.9407 0.6166 0.5904 0.0499  -0.2123 0.0099  180 LEU B CB  
3101 C CG  . LEU B 180 ? 0.9578 0.6183 0.6084 0.0474  -0.2105 0.0153  180 LEU B CG  
3102 C CD1 . LEU B 180 ? 0.9481 0.5994 0.5943 0.0475  -0.2094 0.0158  180 LEU B CD1 
3103 C CD2 . LEU B 180 ? 0.9959 0.6620 0.6506 0.0505  -0.2060 0.0237  180 LEU B CD2 
3104 N N   . SER B 181 ? 0.9298 0.6049 0.5911 0.0443  -0.2144 0.0117  181 SER B N   
3105 C CA  . SER B 181 ? 0.9645 0.6432 0.6304 0.0446  -0.2128 0.0164  181 SER B CA  
3106 C C   . SER B 181 ? 1.0160 0.6807 0.6828 0.0426  -0.2104 0.0219  181 SER B C   
3107 O O   . SER B 181 ? 1.0330 0.6842 0.6995 0.0376  -0.2124 0.0193  181 SER B O   
3108 C CB  . SER B 181 ? 0.9506 0.6304 0.6203 0.0410  -0.2163 0.0116  181 SER B CB  
3109 O OG  . SER B 181 ? 1.0030 0.6813 0.6765 0.0400  -0.2152 0.0161  181 SER B OG  
3110 N N   . SER B 182 ? 1.0509 0.7199 0.7195 0.0465  -0.2057 0.0295  182 SER B N   
3111 C CA  . SER B 182 ? 1.0341 0.6912 0.7056 0.0451  -0.2020 0.0350  182 SER B CA  
3112 C C   . SER B 182 ? 1.0316 0.6931 0.7086 0.0459  -0.1999 0.0398  182 SER B C   
3113 O O   . SER B 182 ? 1.0633 0.7399 0.7416 0.0504  -0.1988 0.0428  182 SER B O   
3114 C CB  . SER B 182 ? 1.0647 0.7214 0.7353 0.0491  -0.1971 0.0409  182 SER B CB  
3115 O OG  . SER B 182 ? 1.1196 0.7645 0.7946 0.0474  -0.1927 0.0456  182 SER B OG  
3116 N N   . THR B 183 ? 1.0362 0.6856 0.7165 0.0415  -0.1994 0.0401  183 THR B N   
3117 C CA  . THR B 183 ? 1.0596 0.7111 0.7450 0.0414  -0.1979 0.0436  183 THR B CA  
3118 C C   . THR B 183 ? 1.1782 0.8198 0.8686 0.0410  -0.1920 0.0494  183 THR B C   
3119 O O   . THR B 183 ? 1.2171 0.8453 0.9085 0.0357  -0.1921 0.0463  183 THR B O   
3120 C CB  . THR B 183 ? 1.0969 0.7445 0.7825 0.0360  -0.2029 0.0375  183 THR B CB  
3121 O OG1 . THR B 183 ? 1.1385 0.7919 0.8203 0.0355  -0.2078 0.0312  183 THR B OG1 
3122 C CG2 . THR B 183 ? 1.1178 0.7720 0.8078 0.0370  -0.2022 0.0405  183 THR B CG2 
3123 N N   . LEU B 184 ? 1.1354 0.7844 0.8298 0.0464  -0.1866 0.0576  184 LEU B N   
3124 C CA  . LEU B 184 ? 1.1451 0.7859 0.8465 0.0465  -0.1800 0.0637  184 LEU B CA  
3125 C C   . LEU B 184 ? 1.1163 0.7562 0.8221 0.0442  -0.1803 0.0639  184 LEU B C   
3126 O O   . LEU B 184 ? 1.0672 0.7194 0.7736 0.0475  -0.1814 0.0664  184 LEU B O   
3127 C CB  . LEU B 184 ? 1.1630 0.8131 0.8680 0.0538  -0.1735 0.0735  184 LEU B CB  
3128 C CG  . LEU B 184 ? 1.1226 0.7630 0.8352 0.0547  -0.1653 0.0801  184 LEU B CG  
3129 C CD1 . LEU B 184 ? 1.0777 0.7308 0.7937 0.0629  -0.1593 0.0908  184 LEU B CD1 
3130 C CD2 . LEU B 184 ? 1.1752 0.8060 0.8953 0.0511  -0.1621 0.0808  184 LEU B CD2 
3131 N N   . THR B 185 ? 1.1213 0.7475 0.8304 0.0386  -0.1793 0.0610  185 THR B N   
3132 C CA  . THR B 185 ? 1.1316 0.7554 0.8447 0.0358  -0.1794 0.0605  185 THR B CA  
3133 C C   . THR B 185 ? 1.1578 0.7731 0.8796 0.0354  -0.1716 0.0654  185 THR B C   
3134 O O   . THR B 185 ? 1.1363 0.7419 0.8607 0.0334  -0.1677 0.0647  185 THR B O   
3135 C CB  . THR B 185 ? 1.1702 0.7870 0.8798 0.0287  -0.1855 0.0517  185 THR B CB  
3136 O OG1 . THR B 185 ? 1.3137 0.9189 1.0231 0.0242  -0.1845 0.0477  185 THR B OG1 
3137 C CG2 . THR B 185 ? 1.1506 0.7758 0.8535 0.0291  -0.1925 0.0471  185 THR B CG2 
3138 N N   . LEU B 186 ? 1.1654 0.7844 0.8925 0.0373  -0.1689 0.0699  186 LEU B N   
3139 C CA  . LEU B 186 ? 1.1901 0.8016 0.9270 0.0372  -0.1609 0.0746  186 LEU B CA  
3140 C C   . LEU B 186 ? 1.1958 0.8112 0.9360 0.0377  -0.1609 0.0767  186 LEU B C   
3141 O O   . LEU B 186 ? 1.2244 0.8489 0.9595 0.0384  -0.1669 0.0750  186 LEU B O   
3142 C CB  . LEU B 186 ? 1.2304 0.8450 0.9728 0.0436  -0.1531 0.0839  186 LEU B CB  
3143 C CG  . LEU B 186 ? 1.2100 0.8414 0.9507 0.0519  -0.1528 0.0919  186 LEU B CG  
3144 C CD1 . LEU B 186 ? 1.2855 0.9237 1.0334 0.0559  -0.1486 0.0996  186 LEU B CD1 
3145 C CD2 . LEU B 186 ? 1.1242 0.7575 0.8666 0.0566  -0.1477 0.0979  186 LEU B CD2 
3146 N N   . SER B 187 ? 1.2558 0.8641 1.0054 0.0370  -0.1538 0.0800  187 SER B N   
3147 C CA  . SER B 187 ? 1.2977 0.9071 1.0510 0.0365  -0.1534 0.0811  187 SER B CA  
3148 C C   . SER B 187 ? 1.3039 0.9283 1.0577 0.0438  -0.1532 0.0893  187 SER B C   
3149 O O   . SER B 187 ? 1.3257 0.9596 1.0791 0.0499  -0.1513 0.0957  187 SER B O   
3150 C CB  . SER B 187 ? 1.3390 0.9377 1.1036 0.0345  -0.1446 0.0828  187 SER B CB  
3151 O OG  . SER B 187 ? 1.3527 0.9395 1.1182 0.0282  -0.1434 0.0757  187 SER B OG  
3152 N N   . LYS B 188 ? 1.2794 0.9069 1.0339 0.0431  -0.1554 0.0890  188 LYS B N   
3153 C CA  . LYS B 188 ? 1.3127 0.9548 1.0689 0.0497  -0.1546 0.0968  188 LYS B CA  
3154 C C   . LYS B 188 ? 1.3695 1.0128 1.1361 0.0556  -0.1446 0.1077  188 LYS B C   
3155 O O   . LYS B 188 ? 1.3404 0.9975 1.1081 0.0628  -0.1424 0.1160  188 LYS B O   
3156 C CB  . LYS B 188 ? 1.3123 0.9559 1.0679 0.0472  -0.1586 0.0940  188 LYS B CB  
3157 C CG  . LYS B 188 ? 1.3240 0.9831 1.0823 0.0537  -0.1575 0.1020  188 LYS B CG  
3158 C CD  . LYS B 188 ? 1.2849 0.9448 1.0426 0.0509  -0.1615 0.0989  188 LYS B CD  
3159 C CE  . LYS B 188 ? 1.2641 0.9390 1.0259 0.0574  -0.1595 0.1075  188 LYS B CE  
3160 N NZ  . LYS B 188 ? 1.2713 0.9650 1.0288 0.0625  -0.1625 0.1100  188 LYS B NZ  
3161 N N   . ALA B 189 ? 1.3324 0.9623 1.1076 0.0527  -0.1380 0.1078  189 ALA B N   
3162 C CA  . ALA B 189 ? 1.3166 0.9461 1.1038 0.0581  -0.1273 0.1182  189 ALA B CA  
3163 C C   . ALA B 189 ? 1.3557 0.9870 1.1440 0.0619  -0.1233 0.1229  189 ALA B C   
3164 O O   . ALA B 189 ? 1.4032 1.0447 1.1971 0.0696  -0.1176 0.1340  189 ALA B O   
3165 C CB  . ALA B 189 ? 1.3371 0.9509 1.1341 0.0532  -0.1207 0.1154  189 ALA B CB  
3166 N N   . ASP B 190 ? 1.3244 0.9466 1.1074 0.0568  -0.1263 0.1150  190 ASP B N   
3167 C CA  . ASP B 190 ? 1.3807 1.0040 1.1639 0.0600  -0.1231 0.1186  190 ASP B CA  
3168 C C   . ASP B 190 ? 1.4374 1.0789 1.2132 0.0666  -0.1273 0.1236  190 ASP B C   
3169 O O   . ASP B 190 ? 1.4013 1.0486 1.1794 0.0721  -0.1228 0.1309  190 ASP B O   
3170 C CB  . ASP B 190 ? 1.3846 0.9956 1.1624 0.0527  -0.1267 0.1081  190 ASP B CB  
3171 C CG  . ASP B 190 ? 1.4998 1.0947 1.2873 0.0470  -0.1200 0.1043  190 ASP B CG  
3172 O OD1 . ASP B 190 ? 1.5035 1.0958 1.3018 0.0482  -0.1129 0.1089  190 ASP B OD1 
3173 O OD2 . ASP B 190 ? 1.5008 1.0863 1.2859 0.0413  -0.1215 0.0964  190 ASP B OD2 
3174 N N   . TYR B 191 ? 1.3932 1.0443 1.1605 0.0660  -0.1357 0.1194  191 TYR B N   
3175 C CA  . TYR B 191 ? 1.3490 1.0195 1.1104 0.0719  -0.1394 0.1232  191 TYR B CA  
3176 C C   . TYR B 191 ? 1.3602 1.0457 1.1288 0.0799  -0.1338 0.1354  191 TYR B C   
3177 O O   . TYR B 191 ? 1.3612 1.0632 1.1285 0.0865  -0.1328 0.1420  191 TYR B O   
3178 C CB  . TYR B 191 ? 1.2934 0.9693 1.0448 0.0681  -0.1497 0.1138  191 TYR B CB  
3179 C CG  . TYR B 191 ? 1.2660 0.9632 1.0121 0.0735  -0.1535 0.1160  191 TYR B CG  
3180 C CD1 . TYR B 191 ? 1.2203 0.9237 0.9605 0.0753  -0.1554 0.1143  191 TYR B CD1 
3181 C CD2 . TYR B 191 ? 1.3018 1.0137 1.0491 0.0765  -0.1550 0.1191  191 TYR B CD2 
3182 C CE1 . TYR B 191 ? 1.2603 0.9845 0.9962 0.0798  -0.1585 0.1154  191 TYR B CE1 
3183 C CE2 . TYR B 191 ? 1.3517 1.0850 1.0950 0.0810  -0.1582 0.1201  191 TYR B CE2 
3184 C CZ  . TYR B 191 ? 1.3167 1.0564 1.0544 0.0826  -0.1598 0.1181  191 TYR B CZ  
3185 O OH  . TYR B 191 ? 1.2076 0.9699 0.9418 0.0867  -0.1626 0.1183  191 TYR B OH  
3186 N N   . GLU B 192 ? 1.3873 1.0682 1.1636 0.0795  -0.1301 0.1385  192 GLU B N   
3187 C CA  . GLU B 192 ? 1.3466 1.0406 1.1316 0.0872  -0.1236 0.1511  192 GLU B CA  
3188 C C   . GLU B 192 ? 1.3399 1.0316 1.1353 0.0924  -0.1129 0.1617  192 GLU B C   
3189 O O   . GLU B 192 ? 1.3571 1.0642 1.1584 0.1005  -0.1076 0.1738  192 GLU B O   
3190 C CB  . GLU B 192 ? 1.3300 1.0182 1.1208 0.0850  -0.1222 0.1511  192 GLU B CB  
3191 C CG  . GLU B 192 ? 1.3703 1.0587 1.1524 0.0794  -0.1320 0.1408  192 GLU B CG  
3192 C CD  . GLU B 192 ? 1.4152 1.1251 1.1900 0.0831  -0.1386 0.1413  192 GLU B CD  
3193 O OE1 . GLU B 192 ? 1.4563 1.1837 1.2349 0.0908  -0.1348 0.1515  192 GLU B OE1 
3194 O OE2 . GLU B 192 ? 1.3534 1.0638 1.1196 0.0782  -0.1472 0.1313  192 GLU B OE2 
3195 N N   . LYS B 193 ? 1.3418 1.0156 1.1399 0.0879  -0.1094 0.1576  193 LYS B N   
3196 C CA  . LYS B 193 ? 1.3250 0.9941 1.1354 0.0920  -0.0981 0.1672  193 LYS B CA  
3197 C C   . LYS B 193 ? 1.2650 0.9480 1.0728 0.0988  -0.0967 0.1747  193 LYS B C   
3198 O O   . LYS B 193 ? 1.2609 0.9513 1.0791 0.1060  -0.0876 0.1877  193 LYS B O   
3199 C CB  . LYS B 193 ? 1.3657 1.0121 1.1803 0.0844  -0.0949 0.1593  193 LYS B CB  
3200 C CG  . LYS B 193 ? 1.3792 1.0126 1.1998 0.0785  -0.0933 0.1537  193 LYS B CG  
3201 C CD  . LYS B 193 ? 1.4234 1.0373 1.2524 0.0724  -0.0869 0.1482  193 LYS B CD  
3202 C CE  . LYS B 193 ? 1.4179 1.0252 1.2371 0.0670  -0.0929 0.1384  193 LYS B CE  
3203 N NZ  . LYS B 193 ? 1.4451 1.0348 1.2725 0.0602  -0.0870 0.1318  193 LYS B NZ  
3204 N N   . HIS B 194 ? 1.2732 0.9605 1.0681 0.0967  -0.1052 0.1670  194 HIS B N   
3205 C CA  . HIS B 194 ? 1.2714 0.9715 1.0626 0.1023  -0.1045 0.1724  194 HIS B CA  
3206 C C   . HIS B 194 ? 1.2672 0.9919 1.0505 0.1072  -0.1106 0.1743  194 HIS B C   
3207 O O   . HIS B 194 ? 1.2795 1.0090 1.0580 0.1048  -0.1171 0.1687  194 HIS B O   
3208 C CB  . HIS B 194 ? 1.2647 0.9525 1.0479 0.0967  -0.1088 0.1625  194 HIS B CB  
3209 C CG  . HIS B 194 ? 1.3067 0.9711 1.0966 0.0902  -0.1043 0.1576  194 HIS B CG  
3210 N ND1 . HIS B 194 ? 1.2699 0.9268 1.0737 0.0928  -0.0930 0.1662  194 HIS B ND1 
3211 C CD2 . HIS B 194 ? 1.3349 0.9829 1.1204 0.0812  -0.1092 0.1450  194 HIS B CD2 
3212 C CE1 . HIS B 194 ? 1.2208 0.8579 1.0285 0.0852  -0.0911 0.1581  194 HIS B CE1 
3213 N NE2 . HIS B 194 ? 1.2634 0.8953 1.0598 0.0782  -0.1011 0.1454  194 HIS B NE2 
3214 N N   . LYS B 195 ? 1.2307 0.9716 1.0129 0.1141  -0.1082 0.1820  195 LYS B N   
3215 C CA  . LYS B 195 ? 1.2632 1.0314 1.0405 0.1200  -0.1119 0.1858  195 LYS B CA  
3216 C C   . LYS B 195 ? 1.2742 1.0500 1.0382 0.1178  -0.1205 0.1758  195 LYS B C   
3217 O O   . LYS B 195 ? 1.2603 1.0426 1.0168 0.1146  -0.1286 0.1668  195 LYS B O   
3218 C CB  . LYS B 195 ? 1.2846 1.0705 1.0708 0.1301  -0.1028 0.2024  195 LYS B CB  
3219 C CG  . LYS B 195 ? 1.3457 1.1632 1.1277 0.1366  -0.1057 0.2070  195 LYS B CG  
3220 C CD  . LYS B 195 ? 1.3719 1.2076 1.1650 0.1468  -0.0958 0.2252  195 LYS B CD  
3221 C CE  . LYS B 195 ? 1.2923 1.1231 1.0896 0.1504  -0.0885 0.2327  195 LYS B CE  
3222 N NZ  . LYS B 195 ? 1.2263 1.0717 1.0126 0.1519  -0.0932 0.2288  195 LYS B NZ  
3223 N N   . VAL B 196 ? 1.2921 1.0672 1.0538 0.1196  -0.1184 0.1773  196 VAL B N   
3224 C CA  . VAL B 196 ? 1.2372 1.0217 0.9872 0.1188  -0.1253 0.1692  196 VAL B CA  
3225 C C   . VAL B 196 ? 1.2033 0.9642 0.9470 0.1105  -0.1300 0.1568  196 VAL B C   
3226 O O   . VAL B 196 ? 1.2128 0.9541 0.9615 0.1079  -0.1253 0.1579  196 VAL B O   
3227 C CB  . VAL B 196 ? 1.1877 0.9900 0.9384 0.1269  -0.1202 0.1792  196 VAL B CB  
3228 C CG1 . VAL B 196 ? 1.2304 1.0176 0.9898 0.1286  -0.1112 0.1878  196 VAL B CG1 
3229 C CG2 . VAL B 196 ? 1.1836 0.9944 0.9224 0.1257  -0.1270 0.1699  196 VAL B CG2 
3230 N N   . TYR B 197 ? 1.1992 0.9626 0.9328 0.1061  -0.1390 0.1448  197 TYR B N   
3231 C CA  . TYR B 197 ? 1.1738 0.9182 0.9007 0.0986  -0.1443 0.1328  197 TYR B CA  
3232 C C   . TYR B 197 ? 1.1209 0.8767 0.8384 0.0997  -0.1490 0.1273  197 TYR B C   
3233 O O   . TYR B 197 ? 1.1664 0.9397 0.8795 0.1008  -0.1538 0.1231  197 TYR B O   
3234 C CB  . TYR B 197 ? 1.1578 0.8918 0.8826 0.0914  -0.1506 0.1230  197 TYR B CB  
3235 C CG  . TYR B 197 ? 1.1838 0.9074 0.9175 0.0900  -0.1462 0.1276  197 TYR B CG  
3236 C CD1 . TYR B 197 ? 1.1679 0.8695 0.9062 0.0854  -0.1427 0.1264  197 TYR B CD1 
3237 C CD2 . TYR B 197 ? 1.2030 0.9395 0.9410 0.0933  -0.1453 0.1328  197 TYR B CD2 
3238 C CE1 . TYR B 197 ? 1.2173 0.9098 0.9645 0.0840  -0.1381 0.1298  197 TYR B CE1 
3239 C CE2 . TYR B 197 ? 1.2450 0.9718 0.9914 0.0921  -0.1411 0.1369  197 TYR B CE2 
3240 C CZ  . TYR B 197 ? 1.2969 1.0015 1.0479 0.0875  -0.1374 0.1352  197 TYR B CZ  
3241 O OH  . TYR B 197 ? 1.3606 1.0560 1.1204 0.0861  -0.1327 0.1384  197 TYR B OH  
3242 N N   . ALA B 198 ? 1.1003 0.8467 0.8154 0.0993  -0.1474 0.1267  198 ALA B N   
3243 C CA  . ALA B 198 ? 1.1252 0.8823 0.8320 0.1011  -0.1506 0.1226  198 ALA B CA  
3244 C C   . ALA B 198 ? 1.2474 0.9855 0.9475 0.0942  -0.1557 0.1113  198 ALA B C   
3245 O O   . ALA B 198 ? 1.2920 1.0090 0.9950 0.0894  -0.1543 0.1099  198 ALA B O   
3246 C CB  . ALA B 198 ? 1.1444 0.9120 0.8541 0.1086  -0.1434 0.1340  198 ALA B CB  
3247 N N   . CYS B 199 ? 1.3159 1.0630 1.0078 0.0936  -0.1613 0.1032  199 CYS B N   
3248 C CA  . CYS B 199 ? 1.3127 1.0450 0.9977 0.0879  -0.1664 0.0927  199 CYS B CA  
3249 C C   . CYS B 199 ? 1.3082 1.0484 0.9881 0.0918  -0.1654 0.0935  199 CYS B C   
3250 O O   . CYS B 199 ? 1.3008 1.0609 0.9768 0.0954  -0.1672 0.0917  199 CYS B O   
3251 C CB  . CYS B 199 ? 1.3058 1.0401 0.9865 0.0832  -0.1741 0.0814  199 CYS B CB  
3252 S SG  . CYS B 199 ? 1.5548 1.2817 1.2266 0.0789  -0.1802 0.0692  199 CYS B SG  
3253 N N   . GLU B 200 ? 1.1547 0.8797 0.8349 0.0908  -0.1623 0.0958  200 GLU B N   
3254 C CA  . GLU B 200 ? 1.1506 0.8807 0.8262 0.0944  -0.1606 0.0975  200 GLU B CA  
3255 C C   . GLU B 200 ? 1.1260 0.8455 0.7934 0.0891  -0.1671 0.0854  200 GLU B C   
3256 O O   . GLU B 200 ? 1.1436 0.8424 0.8110 0.0829  -0.1689 0.0805  200 GLU B O   
3257 C CB  . GLU B 200 ? 1.1297 0.8500 0.8115 0.0968  -0.1529 0.1075  200 GLU B CB  
3258 C CG  . GLU B 200 ? 1.1075 0.8382 0.7864 0.1025  -0.1495 0.1128  200 GLU B CG  
3259 C CD  . GLU B 200 ? 1.2126 0.9368 0.9001 0.1060  -0.1405 0.1248  200 GLU B CD  
3260 O OE1 . GLU B 200 ? 1.2446 0.9474 0.9372 0.1010  -0.1384 0.1239  200 GLU B OE1 
3261 O OE2 . GLU B 200 ? 1.2375 0.9791 0.9275 0.1136  -0.1352 0.1352  200 GLU B OE2 
3262 N N   . VAL B 201 ? 1.1181 0.8525 0.7789 0.0915  -0.1702 0.0806  201 VAL B N   
3263 C CA  . VAL B 201 ? 1.0491 0.7765 0.7025 0.0870  -0.1764 0.0688  201 VAL B CA  
3264 C C   . VAL B 201 ? 1.0225 0.7502 0.6706 0.0897  -0.1748 0.0696  201 VAL B C   
3265 O O   . VAL B 201 ? 1.0830 0.8288 0.7305 0.0962  -0.1712 0.0756  201 VAL B O   
3266 C CB  . VAL B 201 ? 1.0393 0.7830 0.6901 0.0869  -0.1812 0.0608  201 VAL B CB  
3267 C CG1 . VAL B 201 ? 1.0562 0.7939 0.7004 0.0831  -0.1865 0.0493  201 VAL B CG1 
3268 C CG2 . VAL B 201 ? 1.0488 0.7897 0.7046 0.0835  -0.1831 0.0594  201 VAL B CG2 
3269 N N   . THR B 202 ? 1.0077 0.7164 0.6522 0.0848  -0.1774 0.0638  202 THR B N   
3270 C CA  . THR B 202 ? 0.9878 0.6941 0.6267 0.0864  -0.1768 0.0630  202 THR B CA  
3271 C C   . THR B 202 ? 1.0031 0.7054 0.6348 0.0823  -0.1834 0.0506  202 THR B C   
3272 O O   . THR B 202 ? 1.0328 0.7207 0.6647 0.0762  -0.1876 0.0440  202 THR B O   
3273 C CB  . THR B 202 ? 0.9547 0.6415 0.5967 0.0843  -0.1729 0.0679  202 THR B CB  
3274 O OG1 . THR B 202 ? 1.0231 0.7128 0.6737 0.0878  -0.1660 0.0795  202 THR B OG1 
3275 C CG2 . THR B 202 ? 0.9695 0.6551 0.6059 0.0865  -0.1718 0.0682  202 THR B CG2 
3276 N N   . HIS B 203 ? 1.0040 0.7199 0.6300 0.0860  -0.1841 0.0477  203 HIS B N   
3277 C CA  . HIS B 203 ? 0.9720 0.6857 0.5920 0.0828  -0.1896 0.0360  203 HIS B CA  
3278 C C   . HIS B 203 ? 0.9571 0.6779 0.5706 0.0867  -0.1885 0.0354  203 HIS B C   
3279 O O   . HIS B 203 ? 1.0129 0.7473 0.6266 0.0926  -0.1837 0.0435  203 HIS B O   
3280 C CB  . HIS B 203 ? 0.9562 0.6845 0.5775 0.0824  -0.1928 0.0291  203 HIS B CB  
3281 C CG  . HIS B 203 ? 0.9421 0.6655 0.5598 0.0784  -0.1980 0.0171  203 HIS B CG  
3282 N ND1 . HIS B 203 ? 0.9565 0.6586 0.5734 0.0725  -0.2017 0.0125  203 HIS B ND1 
3283 C CD2 . HIS B 203 ? 0.8996 0.6372 0.5151 0.0796  -0.1998 0.0088  203 HIS B CD2 
3284 C CE1 . HIS B 203 ? 0.9182 0.6213 0.5327 0.0705  -0.2054 0.0027  203 HIS B CE1 
3285 N NE2 . HIS B 203 ? 0.9062 0.6301 0.5201 0.0746  -0.2042 -0.0001 203 HIS B NE2 
3286 N N   . GLN B 204 ? 0.9617 0.6735 0.5697 0.0833  -0.1927 0.0261  204 GLN B N   
3287 C CA  . GLN B 204 ? 0.9614 0.6786 0.5627 0.0864  -0.1921 0.0241  204 GLN B CA  
3288 C C   . GLN B 204 ? 1.0132 0.7577 0.6132 0.0918  -0.1907 0.0226  204 GLN B C   
3289 O O   . GLN B 204 ? 1.0611 0.8180 0.6581 0.0972  -0.1871 0.0277  204 GLN B O   
3290 C CB  . GLN B 204 ? 0.9567 0.6593 0.5531 0.0815  -0.1972 0.0137  204 GLN B CB  
3291 C CG  . GLN B 204 ? 0.9563 0.6354 0.5549 0.0750  -0.2000 0.0124  204 GLN B CG  
3292 C CD  . GLN B 204 ? 0.9109 0.5768 0.5043 0.0711  -0.2044 0.0038  204 GLN B CD  
3293 O OE1 . GLN B 204 ? 0.9083 0.5813 0.4963 0.0734  -0.2051 -0.0012 204 GLN B OE1 
3294 N NE2 . GLN B 204 ? 0.9275 0.5751 0.5227 0.0653  -0.2071 0.0019  204 GLN B NE2 
3295 N N   . GLY B 205 ? 1.0163 0.7714 0.6189 0.0905  -0.1933 0.0154  205 GLY B N   
3296 C CA  . GLY B 205 ? 0.9935 0.7759 0.5956 0.0948  -0.1919 0.0122  205 GLY B CA  
3297 C C   . GLY B 205 ? 0.9335 0.7362 0.5386 0.1009  -0.1868 0.0230  205 GLY B C   
3298 O O   . GLY B 205 ? 0.8974 0.7246 0.5009 0.1056  -0.1848 0.0222  205 GLY B O   
3299 N N   . LEU B 206 ? 0.9825 0.7765 0.5924 0.1011  -0.1845 0.0331  206 LEU B N   
3300 C CA  . LEU B 206 ? 0.9836 0.7959 0.5974 0.1073  -0.1791 0.0449  206 LEU B CA  
3301 C C   . LEU B 206 ? 1.0252 0.8381 0.6361 0.1121  -0.1745 0.0541  206 LEU B C   
3302 O O   . LEU B 206 ? 0.9834 0.7752 0.5915 0.1096  -0.1749 0.0543  206 LEU B O   
3303 C CB  . LEU B 206 ? 0.9384 0.7411 0.5595 0.1056  -0.1779 0.0521  206 LEU B CB  
3304 C CG  . LEU B 206 ? 0.9367 0.7415 0.5618 0.1017  -0.1816 0.0453  206 LEU B CG  
3305 C CD1 . LEU B 206 ? 1.0151 0.8055 0.6466 0.0995  -0.1804 0.0523  206 LEU B CD1 
3306 C CD2 . LEU B 206 ? 0.9007 0.7364 0.5275 0.1059  -0.1806 0.0440  206 LEU B CD2 
3307 N N   . SER B 207 ? 1.0453 0.8840 0.6574 0.1191  -0.1699 0.0620  207 SER B N   
3308 C CA  . SER B 207 ? 1.1186 0.9602 0.7295 0.1245  -0.1645 0.0729  207 SER B CA  
3309 C C   . SER B 207 ? 1.0877 0.9117 0.7056 0.1245  -0.1602 0.0850  207 SER B C   
3310 O O   . SER B 207 ? 1.1073 0.9138 0.7244 0.1239  -0.1581 0.0890  207 SER B O   
3311 C CB  . SER B 207 ? 1.3356 1.2120 0.9467 0.1323  -0.1605 0.0788  207 SER B CB  
3312 O OG  . SER B 207 ? 1.2267 1.1185 0.8450 0.1346  -0.1585 0.0848  207 SER B OG  
3313 N N   . SER B 208 ? 1.0502 0.8786 0.6755 0.1250  -0.1586 0.0904  208 SER B N   
3314 C CA  . SER B 208 ? 1.0322 0.8454 0.6658 0.1248  -0.1542 0.1011  208 SER B CA  
3315 C C   . SER B 208 ? 1.0024 0.8056 0.6403 0.1194  -0.1576 0.0964  208 SER B C   
3316 O O   . SER B 208 ? 1.0687 0.8829 0.7046 0.1177  -0.1622 0.0878  208 SER B O   
3317 C CB  . SER B 208 ? 1.0409 0.8747 0.6809 0.1332  -0.1464 0.1167  208 SER B CB  
3318 O OG  . SER B 208 ? 1.0364 0.8979 0.6773 0.1367  -0.1470 0.1167  208 SER B OG  
3319 N N   . PRO B 209 ? 1.0013 0.7836 0.6455 0.1164  -0.1553 0.1013  209 PRO B N   
3320 C CA  . PRO B 209 ? 1.0300 0.8043 0.6790 0.1119  -0.1578 0.0984  209 PRO B CA  
3321 C C   . PRO B 209 ? 1.0085 0.8078 0.6606 0.1160  -0.1573 0.1014  209 PRO B C   
3322 O O   . PRO B 209 ? 1.0297 0.8489 0.6851 0.1232  -0.1519 0.1120  209 PRO B O   
3323 C CB  . PRO B 209 ? 1.0517 0.8078 0.7092 0.1111  -0.1521 0.1076  209 PRO B CB  
3324 C CG  . PRO B 209 ? 1.0661 0.8120 0.7214 0.1120  -0.1490 0.1105  209 PRO B CG  
3325 C CD  . PRO B 209 ? 1.0407 0.7998 0.6860 0.1140  -0.1528 0.1039  209 PRO B CD  
3326 N N   . VAL B 210 ? 1.0315 0.8305 0.6829 0.1115  -0.1628 0.0920  210 VAL B N   
3327 C CA  . VAL B 210 ? 1.1248 0.9458 0.7794 0.1141  -0.1632 0.0930  210 VAL B CA  
3328 C C   . VAL B 210 ? 1.1582 0.9668 0.8200 0.1112  -0.1625 0.0965  210 VAL B C   
3329 O O   . VAL B 210 ? 1.2293 1.0156 0.8908 0.1044  -0.1661 0.0899  210 VAL B O   
3330 C CB  . VAL B 210 ? 1.1296 0.9615 0.7791 0.1113  -0.1694 0.0793  210 VAL B CB  
3331 C CG1 . VAL B 210 ? 1.0762 0.9238 0.7304 0.1114  -0.1706 0.0783  210 VAL B CG1 
3332 C CG2 . VAL B 210 ? 1.2082 1.0601 0.8520 0.1156  -0.1688 0.0770  210 VAL B CG2 
3333 N N   . THR B 211 ? 1.1375 0.9612 0.8059 0.1163  -0.1578 0.1070  211 THR B N   
3334 C CA  . THR B 211 ? 1.1676 0.9815 0.8435 0.1143  -0.1564 0.1114  211 THR B CA  
3335 C C   . THR B 211 ? 1.1869 1.0217 0.8649 0.1158  -0.1584 0.1102  211 THR B C   
3336 O O   . THR B 211 ? 1.2256 1.0876 0.9034 0.1217  -0.1567 0.1138  211 THR B O   
3337 C CB  . THR B 211 ? 1.1933 1.0032 0.8773 0.1189  -0.1481 0.1261  211 THR B CB  
3338 O OG1 . THR B 211 ? 1.1860 0.9847 0.8679 0.1195  -0.1453 0.1283  211 THR B OG1 
3339 C CG2 . THR B 211 ? 1.1722 0.9619 0.8632 0.1145  -0.1469 0.1276  211 THR B CG2 
3340 N N   . LYS B 212 ? 1.2048 1.0278 0.8851 0.1104  -0.1619 0.1051  212 LYS B N   
3341 C CA  . LYS B 212 ? 1.2514 1.0907 0.9348 0.1109  -0.1638 0.1039  212 LYS B CA  
3342 C C   . LYS B 212 ? 1.2184 1.0454 0.9093 0.1099  -0.1609 0.1110  212 LYS B C   
3343 O O   . LYS B 212 ? 1.2899 1.0917 0.9820 0.1052  -0.1607 0.1099  212 LYS B O   
3344 C CB  . LYS B 212 ? 1.2240 1.0614 0.9030 0.1048  -0.1712 0.0892  212 LYS B CB  
3345 C CG  . LYS B 212 ? 1.1800 1.0334 0.8530 0.1058  -0.1738 0.0810  212 LYS B CG  
3346 C CD  . LYS B 212 ? 1.1974 1.0838 0.8722 0.1106  -0.1729 0.0817  212 LYS B CD  
3347 C CE  . LYS B 212 ? 1.1247 1.0267 0.7940 0.1112  -0.1749 0.0725  212 LYS B CE  
3348 N NZ  . LYS B 212 ? 1.1064 1.0423 0.7780 0.1149  -0.1744 0.0708  212 LYS B NZ  
3349 N N   . SER B 213 ? 1.1660 1.0114 0.8622 0.1142  -0.1585 0.1180  213 SER B N   
3350 C CA  . SER B 213 ? 1.1501 0.9853 0.8542 0.1142  -0.1547 0.1262  213 SER B CA  
3351 C C   . SER B 213 ? 1.1819 1.0340 0.8895 0.1153  -0.1563 0.1266  213 SER B C   
3352 O O   . SER B 213 ? 1.2966 1.1755 1.0030 0.1192  -0.1572 0.1264  213 SER B O   
3353 C CB  . SER B 213 ? 1.1783 1.0160 0.8889 0.1209  -0.1459 0.1412  213 SER B CB  
3354 O OG  . SER B 213 ? 1.2255 1.0937 0.9371 0.1288  -0.1430 0.1489  213 SER B OG  
3355 N N   . PHE B 214 ? 1.1429 0.9798 0.8549 0.1115  -0.1567 0.1266  214 PHE B N   
3356 C CA  . PHE B 214 ? 1.1659 1.0158 0.8832 0.1132  -0.1564 0.1305  214 PHE B CA  
3357 C C   . PHE B 214 ? 1.2332 1.0733 0.9593 0.1161  -0.1492 0.1429  214 PHE B C   
3358 O O   . PHE B 214 ? 1.2620 1.0788 0.9900 0.1133  -0.1464 0.1440  214 PHE B O   
3359 C CB  . PHE B 214 ? 1.1375 0.9789 0.8525 0.1060  -0.1634 0.1188  214 PHE B CB  
3360 C CG  . PHE B 214 ? 1.2212 1.0335 0.9379 0.0999  -0.1639 0.1165  214 PHE B CG  
3361 C CD1 . PHE B 214 ? 1.1894 0.9809 0.9016 0.0945  -0.1663 0.1092  214 PHE B CD1 
3362 C CD2 . PHE B 214 ? 1.2676 1.0746 0.9906 0.0993  -0.1619 0.1211  214 PHE B CD2 
3363 C CE1 . PHE B 214 ? 1.1736 0.9408 0.8876 0.0887  -0.1666 0.1066  214 PHE B CE1 
3364 C CE2 . PHE B 214 ? 1.2230 1.0049 0.9478 0.0935  -0.1622 0.1182  214 PHE B CE2 
3365 C CZ  . PHE B 214 ? 1.2018 0.9644 0.9221 0.0881  -0.1645 0.1109  214 PHE B CZ  
3366 N N   . ASN B 215 ? 1.2937 1.1523 1.0259 0.1215  -0.1458 0.1522  215 ASN B N   
3367 C CA  . ASN B 215 ? 1.3014 1.1562 1.0435 0.1263  -0.1373 0.1663  215 ASN B CA  
3368 C C   . ASN B 215 ? 1.3256 1.1727 1.0740 0.1244  -0.1366 0.1683  215 ASN B C   
3369 O O   . ASN B 215 ? 1.4437 1.2855 1.2015 0.1279  -0.1291 0.1795  215 ASN B O   
3370 C CB  . ASN B 215 ? 1.2814 1.1652 1.0273 0.1360  -0.1317 0.1792  215 ASN B CB  
3371 C CG  . ASN B 215 ? 1.3364 1.2231 1.0788 0.1391  -0.1291 0.1815  215 ASN B CG  
3372 O OD1 . ASN B 215 ? 1.3023 1.1856 1.0358 0.1351  -0.1347 0.1703  215 ASN B OD1 
3373 N ND2 . ASN B 215 ? 1.3345 1.2273 1.0844 0.1463  -0.1204 0.1962  215 ASN B ND2 
3374 N N   . ARG B 216 ? 1.1720 1.0186 0.9165 0.1190  -0.1437 0.1581  216 ARG B N   
3375 C CA  . ARG B 216 ? 1.2031 1.0398 0.9531 0.1165  -0.1434 0.1592  216 ARG B CA  
3376 C C   . ARG B 216 ? 1.2960 1.1010 1.0473 0.1100  -0.1425 0.1550  216 ARG B C   
3377 O O   . ARG B 216 ? 1.3742 1.1649 1.1194 0.1048  -0.1461 0.1460  216 ARG B O   
3378 C CB  . ARG B 216 ? 1.1839 1.0303 0.9297 0.1128  -0.1511 0.1497  216 ARG B CB  
3379 C CG  . ARG B 216 ? 1.1716 1.0512 0.9182 0.1188  -0.1514 0.1539  216 ARG B CG  
3380 C CD  . ARG B 216 ? 1.2440 1.1332 0.9855 0.1141  -0.1595 0.1415  216 ARG B CD  
3381 N NE  . ARG B 216 ? 1.1544 1.0774 0.8964 0.1194  -0.1598 0.1437  216 ARG B NE  
3382 C CZ  . ARG B 216 ? 1.1310 1.0715 0.8686 0.1214  -0.1610 0.1400  216 ARG B CZ  
3383 N NH1 . ARG B 216 ? 1.0720 0.9988 0.8040 0.1188  -0.1622 0.1343  216 ARG B NH1 
3384 N NH2 . ARG B 216 ? 1.2042 1.1775 0.9431 0.1260  -0.1609 0.1418  216 ARG B NH2 
3385 N N   . GLY B 217 ? 1.3337 1.1288 1.0935 0.1104  -0.1374 0.1614  217 GLY B N   
3386 C CA  . GLY B 217 ? 1.3129 1.0801 1.0756 0.1043  -0.1354 0.1577  217 GLY B CA  
3387 C C   . GLY B 217 ? 1.3040 1.0642 1.0775 0.1056  -0.1290 0.1654  217 GLY B C   
3388 O O   . GLY B 217 ? 1.3176 1.0773 1.0913 0.1030  -0.1322 0.1622  217 GLY B O   
3389 N N   . GLN C 1   ? 1.2902 0.8928 1.0190 -0.0414 -0.2271 0.0193  1   GLN C N   
3390 C CA  . GLN C 1   ? 1.2583 0.8604 0.9846 -0.0470 -0.2273 0.0145  1   GLN C CA  
3391 C C   . GLN C 1   ? 1.2919 0.8948 1.0162 -0.0501 -0.2304 0.0132  1   GLN C C   
3392 O O   . GLN C 1   ? 1.3956 1.0006 1.1175 -0.0547 -0.2317 0.0098  1   GLN C O   
3393 C CB  . GLN C 1   ? 1.3431 0.9399 1.0715 -0.0487 -0.2204 0.0110  1   GLN C CB  
3394 C CG  . GLN C 1   ? 1.4289 1.0251 1.1592 -0.0469 -0.2174 0.0115  1   GLN C CG  
3395 C CD  . GLN C 1   ? 1.5378 1.1295 1.2710 -0.0496 -0.2104 0.0070  1   GLN C CD  
3396 O OE1 . GLN C 1   ? 1.5340 1.1228 1.2687 -0.0524 -0.2072 0.0035  1   GLN C OE1 
3397 N NE2 . GLN C 1   ? 1.5818 1.1731 1.3166 -0.0490 -0.2078 0.0065  1   GLN C NE2 
3398 N N   . VAL C 2   ? 1.2070 0.8091 0.9323 -0.0474 -0.2316 0.0160  2   VAL C N   
3399 C CA  . VAL C 2   ? 1.1969 0.8000 0.9203 -0.0500 -0.2352 0.0152  2   VAL C CA  
3400 C C   . VAL C 2   ? 1.2646 0.8742 0.9866 -0.0517 -0.2412 0.0158  2   VAL C C   
3401 O O   . VAL C 2   ? 1.2971 0.9107 1.0208 -0.0488 -0.2437 0.0184  2   VAL C O   
3402 C CB  . VAL C 2   ? 1.1175 0.7191 0.8428 -0.0465 -0.2354 0.0183  2   VAL C CB  
3403 C CG1 . VAL C 2   ? 1.1025 0.7047 0.8257 -0.0494 -0.2392 0.0172  2   VAL C CG1 
3404 C CG2 . VAL C 2   ? 1.1986 0.7938 0.9266 -0.0444 -0.2287 0.0185  2   VAL C CG2 
3405 N N   . GLN C 3   ? 1.2080 0.8194 0.9276 -0.0562 -0.2430 0.0133  3   GLN C N   
3406 C CA  . GLN C 3   ? 1.2145 0.8323 0.9338 -0.0579 -0.2477 0.0143  3   GLN C CA  
3407 C C   . GLN C 3   ? 1.1960 0.8153 0.9143 -0.0607 -0.2508 0.0142  3   GLN C C   
3408 O O   . GLN C 3   ? 1.1678 0.7844 0.8838 -0.0633 -0.2490 0.0117  3   GLN C O   
3409 C CB  . GLN C 3   ? 1.1969 0.8181 0.9150 -0.0607 -0.2467 0.0124  3   GLN C CB  
3410 C CG  . GLN C 3   ? 1.1952 0.8157 0.9145 -0.0580 -0.2445 0.0128  3   GLN C CG  
3411 C CD  . GLN C 3   ? 1.3600 0.9843 1.0780 -0.0609 -0.2436 0.0107  3   GLN C CD  
3412 O OE1 . GLN C 3   ? 1.4919 1.1215 1.2086 -0.0644 -0.2454 0.0099  3   GLN C OE1 
3413 N NE2 . GLN C 3   ? 1.3660 0.9885 1.0847 -0.0593 -0.2407 0.0101  3   GLN C NE2 
3414 N N   . LEU C 4   ? 1.2279 0.8517 0.9486 -0.0603 -0.2551 0.0168  4   LEU C N   
3415 C CA  . LEU C 4   ? 1.1767 0.8023 0.8974 -0.0627 -0.2583 0.0173  4   LEU C CA  
3416 C C   . LEU C 4   ? 1.1572 0.7896 0.8796 -0.0649 -0.2607 0.0188  4   LEU C C   
3417 O O   . LEU C 4   ? 1.1911 0.8270 0.9178 -0.0631 -0.2624 0.0209  4   LEU C O   
3418 C CB  . LEU C 4   ? 1.0696 0.6948 0.7933 -0.0602 -0.2606 0.0190  4   LEU C CB  
3419 C CG  . LEU C 4   ? 1.1089 0.7288 0.8308 -0.0596 -0.2595 0.0182  4   LEU C CG  
3420 C CD1 . LEU C 4   ? 1.1302 0.7447 0.8504 -0.0578 -0.2546 0.0169  4   LEU C CD1 
3421 C CD2 . LEU C 4   ? 1.0317 0.6537 0.7574 -0.0568 -0.2620 0.0201  4   LEU C CD2 
3422 N N   . GLN C 5   ? 1.1844 0.8194 0.9041 -0.0686 -0.2606 0.0179  5   GLN C N   
3423 C CA  . GLN C 5   ? 1.2450 0.8878 0.9666 -0.0706 -0.2624 0.0202  5   GLN C CA  
3424 C C   . GLN C 5   ? 1.2251 0.8704 0.9484 -0.0724 -0.2652 0.0222  5   GLN C C   
3425 O O   . GLN C 5   ? 1.1754 0.8172 0.8955 -0.0739 -0.2653 0.0205  5   GLN C O   
3426 C CB  . GLN C 5   ? 1.1614 0.8083 0.8792 -0.0734 -0.2602 0.0181  5   GLN C CB  
3427 C CG  . GLN C 5   ? 1.2664 0.9103 0.9827 -0.0722 -0.2568 0.0154  5   GLN C CG  
3428 C CD  . GLN C 5   ? 1.2975 0.9483 1.0149 -0.0726 -0.2567 0.0165  5   GLN C CD  
3429 O OE1 . GLN C 5   ? 1.2904 0.9484 1.0104 -0.0733 -0.2590 0.0200  5   GLN C OE1 
3430 N NE2 . GLN C 5   ? 1.2381 0.8870 0.9541 -0.0721 -0.2537 0.0138  5   GLN C NE2 
3431 N N   . GLN C 6   ? 1.1433 0.7944 0.8721 -0.0724 -0.2673 0.0259  6   GLN C N   
3432 C CA  . GLN C 6   ? 1.0437 0.6973 0.7760 -0.0738 -0.2697 0.0284  6   GLN C CA  
3433 C C   . GLN C 6   ? 1.0025 0.6649 0.7367 -0.0761 -0.2699 0.0320  6   GLN C C   
3434 O O   . GLN C 6   ? 0.9850 0.6526 0.7209 -0.0755 -0.2689 0.0336  6   GLN C O   
3435 C CB  . GLN C 6   ? 1.0223 0.6754 0.7624 -0.0716 -0.2713 0.0300  6   GLN C CB  
3436 C CG  . GLN C 6   ? 1.0126 0.6652 0.7559 -0.0729 -0.2735 0.0309  6   GLN C CG  
3437 C CD  . GLN C 6   ? 0.9526 0.6075 0.7057 -0.0714 -0.2746 0.0322  6   GLN C CD  
3438 O OE1 . GLN C 6   ? 0.9327 0.5892 0.6897 -0.0692 -0.2737 0.0320  6   GLN C OE1 
3439 N NE2 . GLN C 6   ? 0.9142 0.5699 0.6720 -0.0729 -0.2762 0.0331  6   GLN C NE2 
3440 N N   . TRP C 7   ? 0.9464 0.6111 0.6803 -0.0784 -0.2711 0.0334  7   TRP C N   
3441 C CA  . TRP C 7   ? 0.9191 0.5934 0.6564 -0.0801 -0.2715 0.0382  7   TRP C CA  
3442 C C   . TRP C 7   ? 0.9023 0.5763 0.6424 -0.0815 -0.2733 0.0403  7   TRP C C   
3443 O O   . TRP C 7   ? 0.8945 0.5614 0.6318 -0.0818 -0.2744 0.0372  7   TRP C O   
3444 C CB  . TRP C 7   ? 0.9514 0.6327 0.6822 -0.0825 -0.2699 0.0371  7   TRP C CB  
3445 C CG  . TRP C 7   ? 0.9684 0.6469 0.6914 -0.0851 -0.2695 0.0327  7   TRP C CG  
3446 C CD1 . TRP C 7   ? 0.9541 0.6353 0.6757 -0.0874 -0.2706 0.0338  7   TRP C CD1 
3447 C CD2 . TRP C 7   ? 0.9527 0.6253 0.6691 -0.0856 -0.2673 0.0264  7   TRP C CD2 
3448 N NE1 . TRP C 7   ? 0.8915 0.5688 0.6057 -0.0894 -0.2694 0.0282  7   TRP C NE1 
3449 C CE2 . TRP C 7   ? 0.9106 0.5825 0.6220 -0.0883 -0.2672 0.0236  7   TRP C CE2 
3450 C CE3 . TRP C 7   ? 0.9927 0.6604 0.7075 -0.0840 -0.2652 0.0230  7   TRP C CE3 
3451 C CZ2 . TRP C 7   ? 0.9712 0.6377 0.6770 -0.0895 -0.2645 0.0172  7   TRP C CZ2 
3452 C CZ3 . TRP C 7   ? 0.9900 0.6524 0.6995 -0.0851 -0.2626 0.0172  7   TRP C CZ3 
3453 C CH2 . TRP C 7   ? 0.9919 0.6536 0.6973 -0.0878 -0.2621 0.0142  7   TRP C CH2 
3454 N N   . GLY C 8   ? 0.8924 0.5747 0.6387 -0.0823 -0.2735 0.0459  8   GLY C N   
3455 C CA  . GLY C 8   ? 0.8816 0.5645 0.6314 -0.0838 -0.2750 0.0484  8   GLY C CA  
3456 C C   . GLY C 8   ? 0.8501 0.5411 0.6111 -0.0834 -0.2744 0.0555  8   GLY C C   
3457 O O   . GLY C 8   ? 0.8503 0.5486 0.6143 -0.0824 -0.2728 0.0590  8   GLY C O   
3458 N N   . THR C 9   ? 0.8462 0.5358 0.6138 -0.0841 -0.2754 0.0577  9   THR C N   
3459 C CA  . THR C 9   ? 0.8420 0.5389 0.6218 -0.0838 -0.2741 0.0648  9   THR C CA  
3460 C C   . THR C 9   ? 0.8387 0.5346 0.6296 -0.0814 -0.2727 0.0654  9   THR C C   
3461 O O   . THR C 9   ? 0.8368 0.5257 0.6301 -0.0806 -0.2735 0.0608  9   THR C O   
3462 C CB  . THR C 9   ? 0.8389 0.5342 0.6230 -0.0856 -0.2753 0.0663  9   THR C CB  
3463 O OG1 . THR C 9   ? 0.8384 0.5235 0.6193 -0.0859 -0.2774 0.0599  9   THR C OG1 
3464 C CG2 . THR C 9   ? 0.8682 0.5690 0.6445 -0.0880 -0.2758 0.0686  9   THR C CG2 
3465 N N   . GLY C 10  ? 0.8378 0.5420 0.6358 -0.0801 -0.2704 0.0711  10  GLY C N   
3466 C CA  . GLY C 10  ? 0.8602 0.5644 0.6693 -0.0778 -0.2685 0.0717  10  GLY C CA  
3467 C C   . GLY C 10  ? 0.8333 0.5407 0.6590 -0.0777 -0.2664 0.0768  10  GLY C C   
3468 O O   . GLY C 10  ? 0.8262 0.5311 0.6625 -0.0765 -0.2649 0.0748  10  GLY C O   
3469 N N   . LEU C 11  ? 0.8582 0.5719 0.6872 -0.0790 -0.2657 0.0832  11  LEU C N   
3470 C CA  . LEU C 11  ? 0.8241 0.5413 0.6699 -0.0791 -0.2631 0.0888  11  LEU C CA  
3471 C C   . LEU C 11  ? 0.8346 0.5510 0.6780 -0.0817 -0.2647 0.0900  11  LEU C C   
3472 O O   . LEU C 11  ? 0.9219 0.6419 0.7538 -0.0828 -0.2663 0.0915  11  LEU C O   
3473 C CB  . LEU C 11  ? 0.8266 0.5548 0.6822 -0.0773 -0.2594 0.0982  11  LEU C CB  
3474 C CG  . LEU C 11  ? 0.8758 0.6080 0.7528 -0.0762 -0.2548 0.1045  11  LEU C CG  
3475 C CD1 . LEU C 11  ? 0.9847 0.7287 0.8680 -0.0739 -0.2515 0.1141  11  LEU C CD1 
3476 C CD2 . LEU C 11  ? 0.8985 0.6306 0.7842 -0.0782 -0.2541 0.1075  11  LEU C CD2 
3477 N N   . LEU C 12  ? 0.8365 0.5490 0.6912 -0.0827 -0.2640 0.0890  12  LEU C N   
3478 C CA  . LEU C 12  ? 0.8625 0.5738 0.7166 -0.0852 -0.2655 0.0900  12  LEU C CA  
3479 C C   . LEU C 12  ? 0.9032 0.6177 0.7773 -0.0856 -0.2618 0.0955  12  LEU C C   
3480 O O   . LEU C 12  ? 0.9052 0.6188 0.7935 -0.0847 -0.2590 0.0941  12  LEU C O   
3481 C CB  . LEU C 12  ? 0.8606 0.5617 0.7057 -0.0868 -0.2693 0.0809  12  LEU C CB  
3482 C CG  . LEU C 12  ? 0.8590 0.5557 0.6847 -0.0870 -0.2726 0.0755  12  LEU C CG  
3483 C CD1 . LEU C 12  ? 0.8845 0.5776 0.7072 -0.0848 -0.2726 0.0701  12  LEU C CD1 
3484 C CD2 . LEU C 12  ? 0.8510 0.5405 0.6689 -0.0892 -0.2759 0.0705  12  LEU C CD2 
3485 N N   . LYS C 13  ? 0.9471 0.6658 0.8227 -0.0870 -0.2616 0.1015  13  LYS C N   
3486 C CA  . LYS C 13  ? 0.9467 0.6668 0.8408 -0.0879 -0.2583 0.1058  13  LYS C CA  
3487 C C   . LYS C 13  ? 0.9062 0.6172 0.7998 -0.0907 -0.2611 0.0978  13  LYS C C   
3488 O O   . LYS C 13  ? 0.9086 0.6138 0.7857 -0.0919 -0.2657 0.0919  13  LYS C O   
3489 C CB  . LYS C 13  ? 0.9917 0.7209 0.8883 -0.0882 -0.2567 0.1162  13  LYS C CB  
3490 C CG  . LYS C 13  ? 0.9888 0.7295 0.8837 -0.0856 -0.2545 0.1245  13  LYS C CG  
3491 C CD  . LYS C 13  ? 1.0246 0.7712 0.9405 -0.0831 -0.2485 0.1317  13  LYS C CD  
3492 C CE  . LYS C 13  ? 1.0615 0.8190 0.9744 -0.0802 -0.2468 0.1386  13  LYS C CE  
3493 N NZ  . LYS C 13  ? 0.9719 0.7249 0.8725 -0.0793 -0.2495 0.1307  13  LYS C NZ  
3494 N N   . PRO C 14  ? 0.8565 0.5664 0.7684 -0.0917 -0.2581 0.0973  14  PRO C N   
3495 C CA  . PRO C 14  ? 0.8307 0.5336 0.7432 -0.0946 -0.2606 0.0899  14  PRO C CA  
3496 C C   . PRO C 14  ? 0.8811 0.5822 0.7817 -0.0967 -0.2642 0.0915  14  PRO C C   
3497 O O   . PRO C 14  ? 0.8776 0.5846 0.7789 -0.0966 -0.2628 0.1001  14  PRO C O   
3498 C CB  . PRO C 14  ? 0.8371 0.5425 0.7745 -0.0955 -0.2553 0.0916  14  PRO C CB  
3499 C CG  . PRO C 14  ? 0.8832 0.5935 0.8308 -0.0926 -0.2508 0.0947  14  PRO C CG  
3500 C CD  . PRO C 14  ? 0.8639 0.5788 0.7976 -0.0902 -0.2519 0.1016  14  PRO C CD  
3501 N N   . SER C 15  ? 0.9744 0.6679 0.8639 -0.0984 -0.2687 0.0833  15  SER C N   
3502 C CA  . SER C 15  ? 0.9731 0.6630 0.8493 -0.1005 -0.2727 0.0825  15  SER C CA  
3503 C C   . SER C 15  ? 0.9785 0.6694 0.8351 -0.0995 -0.2752 0.0838  15  SER C C   
3504 O O   . SER C 15  ? 0.9841 0.6736 0.8299 -0.1012 -0.2778 0.0841  15  SER C O   
3505 C CB  . SER C 15  ? 0.9771 0.6703 0.8643 -0.1025 -0.2708 0.0893  15  SER C CB  
3506 O OG  . SER C 15  ? 1.1525 0.8407 1.0284 -0.1049 -0.2748 0.0866  15  SER C OG  
3507 N N   . GLU C 16  ? 0.9019 0.5955 0.7538 -0.0970 -0.2743 0.0840  16  GLU C N   
3508 C CA  . GLU C 16  ? 0.9145 0.6094 0.7485 -0.0964 -0.2763 0.0836  16  GLU C CA  
3509 C C   . GLU C 16  ? 0.9514 0.6370 0.7721 -0.0965 -0.2798 0.0741  16  GLU C C   
3510 O O   . GLU C 16  ? 0.9316 0.6111 0.7563 -0.0971 -0.2811 0.0686  16  GLU C O   
3511 C CB  . GLU C 16  ? 0.9040 0.6071 0.7398 -0.0939 -0.2734 0.0888  16  GLU C CB  
3512 C CG  . GLU C 16  ? 0.8973 0.6116 0.7419 -0.0936 -0.2702 0.0995  16  GLU C CG  
3513 C CD  . GLU C 16  ? 0.9520 0.6758 0.7969 -0.0910 -0.2677 0.1047  16  GLU C CD  
3514 O OE1 . GLU C 16  ? 0.9575 0.6783 0.7991 -0.0895 -0.2679 0.1001  16  GLU C OE1 
3515 O OE2 . GLU C 16  ? 0.9638 0.6989 0.8123 -0.0905 -0.2654 0.1138  16  GLU C OE2 
3516 N N   . THR C 17  ? 0.9422 0.6278 0.7480 -0.0959 -0.2810 0.0721  17  THR C N   
3517 C CA  . THR C 17  ? 0.9399 0.6170 0.7329 -0.0959 -0.2837 0.0641  17  THR C CA  
3518 C C   . THR C 17  ? 0.9267 0.6039 0.7150 -0.0935 -0.2827 0.0616  17  THR C C   
3519 O O   . THR C 17  ? 0.9312 0.6148 0.7156 -0.0928 -0.2812 0.0648  17  THR C O   
3520 C CB  . THR C 17  ? 0.9329 0.6086 0.7120 -0.0978 -0.2856 0.0627  17  THR C CB  
3521 O OG1 . THR C 17  ? 1.0011 0.6771 0.7846 -0.1000 -0.2866 0.0654  17  THR C OG1 
3522 C CG2 . THR C 17  ? 0.8809 0.5472 0.6488 -0.0976 -0.2878 0.0547  17  THR C CG2 
3523 N N   . LEU C 18  ? 0.9161 0.5872 0.7050 -0.0922 -0.2835 0.0560  18  LEU C N   
3524 C CA  . LEU C 18  ? 0.8952 0.5654 0.6799 -0.0898 -0.2827 0.0533  18  LEU C CA  
3525 C C   . LEU C 18  ? 0.9242 0.5900 0.6935 -0.0899 -0.2838 0.0491  18  LEU C C   
3526 O O   . LEU C 18  ? 0.9036 0.5627 0.6671 -0.0906 -0.2857 0.0449  18  LEU C O   
3527 C CB  . LEU C 18  ? 0.8452 0.5122 0.6372 -0.0882 -0.2828 0.0492  18  LEU C CB  
3528 C CG  . LEU C 18  ? 0.8352 0.5009 0.6233 -0.0855 -0.2819 0.0462  18  LEU C CG  
3529 C CD1 . LEU C 18  ? 0.8409 0.5129 0.6367 -0.0842 -0.2792 0.0503  18  LEU C CD1 
3530 C CD2 . LEU C 18  ? 0.8365 0.4989 0.6279 -0.0843 -0.2829 0.0409  18  LEU C CD2 
3531 N N   . SER C 19  ? 0.9399 0.6096 0.7033 -0.0893 -0.2822 0.0501  19  SER C N   
3532 C CA  . SER C 19  ? 0.9009 0.5669 0.6514 -0.0895 -0.2822 0.0455  19  SER C CA  
3533 C C   . SER C 19  ? 0.8895 0.5552 0.6389 -0.0871 -0.2806 0.0437  19  SER C C   
3534 O O   . SER C 19  ? 0.8534 0.5261 0.6062 -0.0864 -0.2790 0.0472  19  SER C O   
3535 C CB  . SER C 19  ? 0.9238 0.5962 0.6674 -0.0918 -0.2816 0.0473  19  SER C CB  
3536 O OG  . SER C 19  ? 0.9074 0.5794 0.6509 -0.0940 -0.2832 0.0486  19  SER C OG  
3537 N N   . LEU C 20  ? 0.9620 0.6202 0.7070 -0.0856 -0.2809 0.0387  20  LEU C N   
3538 C CA  . LEU C 20  ? 0.9521 0.6090 0.6951 -0.0833 -0.2793 0.0367  20  LEU C CA  
3539 C C   . LEU C 20  ? 0.9349 0.5856 0.6678 -0.0833 -0.2784 0.0318  20  LEU C C   
3540 O O   . LEU C 20  ? 0.9339 0.5788 0.6637 -0.0838 -0.2795 0.0293  20  LEU C O   
3541 C CB  . LEU C 20  ? 1.0018 0.6568 0.7524 -0.0807 -0.2796 0.0360  20  LEU C CB  
3542 C CG  . LEU C 20  ? 1.0171 0.6779 0.7799 -0.0804 -0.2795 0.0399  20  LEU C CG  
3543 C CD1 . LEU C 20  ? 0.9328 0.5917 0.7031 -0.0789 -0.2802 0.0375  20  LEU C CD1 
3544 C CD2 . LEU C 20  ? 0.9928 0.6589 0.7576 -0.0792 -0.2774 0.0425  20  LEU C CD2 
3545 N N   . THR C 21  ? 0.9468 0.5990 0.6753 -0.0829 -0.2761 0.0303  21  THR C N   
3546 C CA  . THR C 21  ? 0.9367 0.5836 0.6572 -0.0831 -0.2742 0.0255  21  THR C CA  
3547 C C   . THR C 21  ? 0.9923 0.6367 0.7129 -0.0804 -0.2722 0.0240  21  THR C C   
3548 O O   . THR C 21  ? 0.9707 0.6201 0.6948 -0.0795 -0.2718 0.0262  21  THR C O   
3549 C CB  . THR C 21  ? 0.9287 0.5809 0.6434 -0.0864 -0.2727 0.0242  21  THR C CB  
3550 O OG1 . THR C 21  ? 0.9870 0.6417 0.7013 -0.0888 -0.2745 0.0259  21  THR C OG1 
3551 C CG2 . THR C 21  ? 1.0141 0.6607 0.7221 -0.0869 -0.2698 0.0184  21  THR C CG2 
3552 N N   . CYS C 22  ? 1.0730 0.7100 0.7902 -0.0790 -0.2707 0.0205  22  CYS C N   
3553 C CA  . CYS C 22  ? 1.0824 0.7166 0.8001 -0.0760 -0.2686 0.0194  22  CYS C CA  
3554 C C   . CYS C 22  ? 1.0924 0.7225 0.8045 -0.0767 -0.2648 0.0152  22  CYS C C   
3555 O O   . CYS C 22  ? 1.0958 0.7212 0.8048 -0.0777 -0.2639 0.0128  22  CYS C O   
3556 C CB  . CYS C 22  ? 1.0870 0.7172 0.8082 -0.0727 -0.2698 0.0200  22  CYS C CB  
3557 S SG  . CYS C 22  ? 1.1664 0.7950 0.8893 -0.0685 -0.2676 0.0197  22  CYS C SG  
3558 N N   . ALA C 23  ? 1.1146 0.7467 0.8262 -0.0764 -0.2622 0.0141  23  ALA C N   
3559 C CA  . ALA C 23  ? 1.0950 0.7243 0.8028 -0.0777 -0.2579 0.0096  23  ALA C CA  
3560 C C   . ALA C 23  ? 1.1310 0.7543 0.8405 -0.0740 -0.2551 0.0090  23  ALA C C   
3561 O O   . ALA C 23  ? 1.1699 0.7953 0.8817 -0.0719 -0.2554 0.0109  23  ALA C O   
3562 C CB  . ALA C 23  ? 1.0986 0.7362 0.8049 -0.0807 -0.2565 0.0083  23  ALA C CB  
3563 N N   . VAL C 24  ? 1.1373 0.7535 0.8458 -0.0732 -0.2521 0.0066  24  VAL C N   
3564 C CA  . VAL C 24  ? 1.1053 0.7160 0.8160 -0.0694 -0.2487 0.0068  24  VAL C CA  
3565 C C   . VAL C 24  ? 1.1377 0.7476 0.8477 -0.0710 -0.2434 0.0027  24  VAL C C   
3566 O O   . VAL C 24  ? 1.1915 0.8002 0.8999 -0.0742 -0.2402 -0.0017 24  VAL C O   
3567 C CB  . VAL C 24  ? 1.0631 0.6672 0.7745 -0.0671 -0.2476 0.0073  24  VAL C CB  
3568 C CG1 . VAL C 24  ? 1.0582 0.6583 0.7727 -0.0625 -0.2441 0.0089  24  VAL C CG1 
3569 C CG2 . VAL C 24  ? 1.1178 0.7238 0.8299 -0.0664 -0.2529 0.0103  24  VAL C CG2 
3570 N N   . TYR C 25  ? 1.1245 0.7355 0.8363 -0.0691 -0.2422 0.0038  25  TYR C N   
3571 C CA  . TYR C 25  ? 1.1586 0.7687 0.8710 -0.0703 -0.2370 0.0000  25  TYR C CA  
3572 C C   . TYR C 25  ? 1.2161 0.8196 0.9319 -0.0658 -0.2332 0.0016  25  TYR C C   
3573 O O   . TYR C 25  ? 1.2396 0.8434 0.9569 -0.0618 -0.2356 0.0060  25  TYR C O   
3574 C CB  . TYR C 25  ? 1.0978 0.7153 0.8095 -0.0718 -0.2385 0.0001  25  TYR C CB  
3575 C CG  . TYR C 25  ? 1.1276 0.7536 0.8367 -0.0762 -0.2412 -0.0011 25  TYR C CG  
3576 C CD1 . TYR C 25  ? 1.1798 0.8070 0.8868 -0.0801 -0.2393 -0.0054 25  TYR C CD1 
3577 C CD2 . TYR C 25  ? 1.1881 0.8216 0.8974 -0.0764 -0.2453 0.0023  25  TYR C CD2 
3578 C CE1 . TYR C 25  ? 1.2102 0.8469 0.9148 -0.0839 -0.2416 -0.0060 25  TYR C CE1 
3579 C CE2 . TYR C 25  ? 1.1921 0.8346 0.8997 -0.0799 -0.2474 0.0024  25  TYR C CE2 
3580 C CZ  . TYR C 25  ? 1.1702 0.8147 0.8751 -0.0837 -0.2456 -0.0017 25  TYR C CZ  
3581 O OH  . TYR C 25  ? 1.0749 0.7300 0.7781 -0.0870 -0.2476 -0.0012 25  TYR C OH  
3582 N N   . GLY C 26  ? 1.1450 0.7433 0.8629 -0.0664 -0.2269 -0.0019 26  GLY C N   
3583 C CA  . GLY C 26  ? 1.0361 0.6286 0.7582 -0.0621 -0.2222 -0.0001 26  GLY C CA  
3584 C C   . GLY C 26  ? 1.0283 0.6148 0.7530 -0.0588 -0.2200 0.0023  26  GLY C C   
3585 O O   . GLY C 26  ? 1.1014 0.6838 0.8305 -0.0547 -0.2155 0.0049  26  GLY C O   
3586 N N   . VAL C 27  ? 0.9881 0.5743 0.7106 -0.0601 -0.2228 0.0021  27  VAL C N   
3587 C CA  . VAL C 27  ? 1.0058 0.5865 0.7308 -0.0571 -0.2207 0.0042  27  VAL C CA  
3588 C C   . VAL C 27  ? 0.9884 0.5691 0.7100 -0.0606 -0.2236 0.0018  27  VAL C C   
3589 O O   . VAL C 27  ? 1.1154 0.7012 0.8327 -0.0639 -0.2287 0.0006  27  VAL C O   
3590 C CB  . VAL C 27  ? 1.0722 0.6547 0.7990 -0.0514 -0.2237 0.0110  27  VAL C CB  
3591 C CG1 . VAL C 27  ? 1.0875 0.6751 0.8109 -0.0520 -0.2314 0.0129  27  VAL C CG1 
3592 C CG2 . VAL C 27  ? 1.0834 0.6608 0.8149 -0.0471 -0.2187 0.0140  27  VAL C CG2 
3593 N N   . SER C 28  ? 0.9810 0.5559 0.7047 -0.0595 -0.2201 0.0014  28  SER C N   
3594 C CA  . SER C 28  ? 0.9999 0.5740 0.7204 -0.0622 -0.2229 -0.0004 28  SER C CA  
3595 C C   . SER C 28  ? 1.1230 0.7001 0.8417 -0.0597 -0.2299 0.0048  28  SER C C   
3596 O O   . SER C 28  ? 1.1290 0.7090 0.8496 -0.0557 -0.2320 0.0095  28  SER C O   
3597 C CB  . SER C 28  ? 1.1121 0.6787 0.8362 -0.0617 -0.2164 -0.0026 28  SER C CB  
3598 O OG  . SER C 28  ? 1.1457 0.7110 0.8668 -0.0631 -0.2196 -0.0032 28  SER C OG  
3599 N N   . LEU C 29  ? 1.1951 0.7720 0.9105 -0.0622 -0.2334 0.0035  29  LEU C N   
3600 C CA  . LEU C 29  ? 1.1825 0.7625 0.8969 -0.0608 -0.2399 0.0075  29  LEU C CA  
3601 C C   . LEU C 29  ? 1.1942 0.7709 0.9114 -0.0566 -0.2389 0.0107  29  LEU C C   
3602 O O   . LEU C 29  ? 1.2139 0.7946 0.9316 -0.0546 -0.2438 0.0143  29  LEU C O   
3603 C CB  . LEU C 29  ? 1.1245 0.7068 0.8343 -0.0655 -0.2445 0.0050  29  LEU C CB  
3604 C CG  . LEU C 29  ? 1.0526 0.6400 0.7597 -0.0698 -0.2454 0.0022  29  LEU C CG  
3605 C CD1 . LEU C 29  ? 1.2095 0.7977 0.9124 -0.0746 -0.2465 -0.0014 29  LEU C CD1 
3606 C CD2 . LEU C 29  ? 1.0183 0.6124 0.7261 -0.0691 -0.2506 0.0059  29  LEU C CD2 
3607 N N   . ARG C 30  ? 1.2244 0.7946 0.9443 -0.0553 -0.2325 0.0096  30  ARG C N   
3608 C CA  . ARG C 30  ? 1.2689 0.8367 0.9922 -0.0509 -0.2312 0.0136  30  ARG C CA  
3609 C C   . ARG C 30  ? 1.1558 0.7258 0.8844 -0.0451 -0.2281 0.0189  30  ARG C C   
3610 O O   . ARG C 30  ? 1.1021 0.6719 0.8326 -0.0446 -0.2244 0.0185  30  ARG C O   
3611 C CB  . ARG C 30  ? 1.3959 0.9557 1.1206 -0.0520 -0.2255 0.0104  30  ARG C CB  
3612 C CG  . ARG C 30  ? 1.4005 0.9588 1.1267 -0.0488 -0.2266 0.0141  30  ARG C CG  
3613 C CD  . ARG C 30  ? 1.5064 1.0710 1.2287 -0.0496 -0.2355 0.0160  30  ARG C CD  
3614 N NE  . ARG C 30  ? 1.4407 1.0055 1.1641 -0.0470 -0.2376 0.0192  30  ARG C NE  
3615 C CZ  . ARG C 30  ? 1.3461 0.9184 1.0702 -0.0447 -0.2431 0.0232  30  ARG C CZ  
3616 N NH1 . ARG C 30  ? 1.3132 0.8930 1.0374 -0.0443 -0.2466 0.0245  30  ARG C NH1 
3617 N NH2 . ARG C 30  ? 1.1574 0.7304 0.8824 -0.0428 -0.2449 0.0255  30  ARG C NH2 
3618 N N   . GLY C 31  ? 1.1747 0.7477 0.9058 -0.0406 -0.2297 0.0241  31  GLY C N   
3619 C CA  . GLY C 31  ? 1.2236 0.8022 0.9592 -0.0349 -0.2284 0.0300  31  GLY C CA  
3620 C C   . GLY C 31  ? 1.1597 0.7481 0.8936 -0.0344 -0.2353 0.0317  31  GLY C C   
3621 O O   . GLY C 31  ? 1.1387 0.7340 0.8761 -0.0296 -0.2348 0.0364  31  GLY C O   
3622 N N   . TYR C 32  ? 1.0614 0.6515 0.7909 -0.0391 -0.2411 0.0281  32  TYR C N   
3623 C CA  . TYR C 32  ? 1.0215 0.6205 0.7507 -0.0394 -0.2469 0.0289  32  TYR C CA  
3624 C C   . TYR C 32  ? 1.0404 0.6415 0.7675 -0.0428 -0.2530 0.0271  32  TYR C C   
3625 O O   . TYR C 32  ? 1.1189 0.7142 0.8437 -0.0451 -0.2530 0.0252  32  TYR C O   
3626 C CB  . TYR C 32  ? 1.0030 0.6023 0.7306 -0.0418 -0.2470 0.0265  32  TYR C CB  
3627 C CG  . TYR C 32  ? 1.0177 0.6142 0.7472 -0.0393 -0.2410 0.0274  32  TYR C CG  
3628 C CD1 . TYR C 32  ? 1.0650 0.6675 0.7976 -0.0348 -0.2402 0.0311  32  TYR C CD1 
3629 C CD2 . TYR C 32  ? 1.0640 0.6526 0.7927 -0.0416 -0.2359 0.0242  32  TYR C CD2 
3630 C CE1 . TYR C 32  ? 1.0898 0.6895 0.8245 -0.0325 -0.2345 0.0322  32  TYR C CE1 
3631 C CE2 . TYR C 32  ? 1.1179 0.7039 0.8494 -0.0396 -0.2299 0.0247  32  TYR C CE2 
3632 C CZ  . TYR C 32  ? 1.1063 0.6974 0.8407 -0.0350 -0.2294 0.0290  32  TYR C CZ  
3633 O OH  . TYR C 32  ? 1.1135 0.7017 0.8509 -0.0330 -0.2233 0.0298  32  TYR C OH  
3634 N N   . TYR C 33  ? 1.0392 0.6487 0.7678 -0.0430 -0.2579 0.0275  33  TYR C N   
3635 C CA  . TYR C 33  ? 1.0339 0.6460 0.7617 -0.0469 -0.2635 0.0255  33  TYR C CA  
3636 C C   . TYR C 33  ? 1.0244 0.6388 0.7519 -0.0499 -0.2655 0.0237  33  TYR C C   
3637 O O   . TYR C 33  ? 1.0304 0.6474 0.7592 -0.0481 -0.2638 0.0244  33  TYR C O   
3638 C CB  . TYR C 33  ? 1.0496 0.6709 0.7816 -0.0447 -0.2670 0.0273  33  TYR C CB  
3639 C CG  . TYR C 33  ? 1.0425 0.6620 0.7743 -0.0435 -0.2672 0.0285  33  TYR C CG  
3640 C CD1 . TYR C 33  ? 1.0607 0.6724 0.7909 -0.0415 -0.2624 0.0298  33  TYR C CD1 
3641 C CD2 . TYR C 33  ? 1.0378 0.6641 0.7720 -0.0442 -0.2717 0.0283  33  TYR C CD2 
3642 C CE1 . TYR C 33  ? 1.1176 0.7278 0.8482 -0.0402 -0.2622 0.0312  33  TYR C CE1 
3643 C CE2 . TYR C 33  ? 1.0578 0.6832 0.7920 -0.0430 -0.2721 0.0295  33  TYR C CE2 
3644 C CZ  . TYR C 33  ? 1.0827 0.6998 0.8148 -0.0408 -0.2674 0.0312  33  TYR C CZ  
3645 O OH  . TYR C 33  ? 1.0919 0.7080 0.8243 -0.0394 -0.2675 0.0327  33  TYR C OH  
3646 N N   . TRP C 34  ? 0.9447 0.5585 0.6708 -0.0543 -0.2690 0.0217  34  TRP C N   
3647 C CA  . TRP C 34  ? 0.9335 0.5495 0.6597 -0.0573 -0.2703 0.0206  34  TRP C CA  
3648 C C   . TRP C 34  ? 0.9406 0.5626 0.6710 -0.0594 -0.2750 0.0205  34  TRP C C   
3649 O O   . TRP C 34  ? 0.9515 0.5720 0.6812 -0.0617 -0.2773 0.0199  34  TRP C O   
3650 C CB  . TRP C 34  ? 0.9828 0.5928 0.7039 -0.0609 -0.2686 0.0185  34  TRP C CB  
3651 C CG  . TRP C 34  ? 1.0004 0.6045 0.7188 -0.0593 -0.2633 0.0177  34  TRP C CG  
3652 C CD1 . TRP C 34  ? 0.9910 0.5888 0.7075 -0.0589 -0.2605 0.0167  34  TRP C CD1 
3653 C CD2 . TRP C 34  ? 0.9622 0.5661 0.6809 -0.0579 -0.2597 0.0176  34  TRP C CD2 
3654 N NE1 . TRP C 34  ? 0.9423 0.5360 0.6586 -0.0575 -0.2549 0.0159  34  TRP C NE1 
3655 C CE2 . TRP C 34  ? 0.9587 0.5560 0.6761 -0.0569 -0.2545 0.0164  34  TRP C CE2 
3656 C CE3 . TRP C 34  ? 1.0140 0.6224 0.7342 -0.0574 -0.2601 0.0183  34  TRP C CE3 
3657 C CZ2 . TRP C 34  ? 0.9968 0.5922 0.7148 -0.0557 -0.2497 0.0158  34  TRP C CZ2 
3658 C CZ3 . TRP C 34  ? 1.0352 0.6416 0.7550 -0.0561 -0.2559 0.0178  34  TRP C CZ3 
3659 C CH2 . TRP C 34  ? 1.0184 0.6184 0.7372 -0.0554 -0.2507 0.0165  34  TRP C CH2 
3660 N N   . THR C 35  ? 0.9069 0.5356 0.6422 -0.0587 -0.2760 0.0210  35  THR C N   
3661 C CA  . THR C 35  ? 0.8794 0.5148 0.6210 -0.0604 -0.2794 0.0205  35  THR C CA  
3662 C C   . THR C 35  ? 0.9598 0.5970 0.7040 -0.0631 -0.2799 0.0207  35  THR C C   
3663 O O   . THR C 35  ? 1.0184 0.6532 0.7595 -0.0632 -0.2778 0.0212  35  THR C O   
3664 C CB  . THR C 35  ? 0.8721 0.5163 0.6199 -0.0571 -0.2798 0.0204  35  THR C CB  
3665 O OG1 . THR C 35  ? 0.9139 0.5591 0.6609 -0.0540 -0.2770 0.0213  35  THR C OG1 
3666 C CG2 . THR C 35  ? 0.9048 0.5509 0.6525 -0.0551 -0.2805 0.0207  35  THR C CG2 
3667 N N   . TRP C 36  ? 0.8876 0.5293 0.6383 -0.0653 -0.2824 0.0204  36  TRP C N   
3668 C CA  . TRP C 36  ? 0.9002 0.5455 0.6565 -0.0673 -0.2826 0.0211  36  TRP C CA  
3669 C C   . TRP C 36  ? 0.9387 0.5924 0.7053 -0.0666 -0.2834 0.0197  36  TRP C C   
3670 O O   . TRP C 36  ? 0.8901 0.5469 0.6609 -0.0674 -0.2853 0.0182  36  TRP C O   
3671 C CB  . TRP C 36  ? 0.9265 0.5698 0.6827 -0.0712 -0.2840 0.0223  36  TRP C CB  
3672 C CG  . TRP C 36  ? 0.9062 0.5439 0.6534 -0.0724 -0.2828 0.0231  36  TRP C CG  
3673 C CD1 . TRP C 36  ? 0.9167 0.5488 0.6568 -0.0736 -0.2830 0.0222  36  TRP C CD1 
3674 C CD2 . TRP C 36  ? 0.9125 0.5510 0.6576 -0.0728 -0.2809 0.0245  36  TRP C CD2 
3675 N NE1 . TRP C 36  ? 0.8867 0.5164 0.6205 -0.0749 -0.2811 0.0224  36  TRP C NE1 
3676 C CE2 . TRP C 36  ? 0.8933 0.5273 0.6299 -0.0744 -0.2799 0.0239  36  TRP C CE2 
3677 C CE3 . TRP C 36  ? 0.9265 0.5695 0.6762 -0.0720 -0.2798 0.0259  36  TRP C CE3 
3678 C CZ2 . TRP C 36  ? 0.9273 0.5625 0.6602 -0.0754 -0.2780 0.0244  36  TRP C CZ2 
3679 C CZ3 . TRP C 36  ? 0.9449 0.5883 0.6905 -0.0727 -0.2781 0.0271  36  TRP C CZ3 
3680 C CH2 . TRP C 36  ? 0.9638 0.6038 0.7010 -0.0745 -0.2772 0.0262  36  TRP C CH2 
3681 N N   . ILE C 37  ? 0.9146 0.5725 0.6855 -0.0652 -0.2819 0.0197  37  ILE C N   
3682 C CA  . ILE C 37  ? 0.9627 0.6296 0.7442 -0.0645 -0.2818 0.0176  37  ILE C CA  
3683 C C   . ILE C 37  ? 0.9359 0.6051 0.7249 -0.0662 -0.2807 0.0186  37  ILE C C   
3684 O O   . ILE C 37  ? 0.9240 0.5903 0.7093 -0.0656 -0.2792 0.0207  37  ILE C O   
3685 C CB  . ILE C 37  ? 0.9566 0.6278 0.7370 -0.0605 -0.2805 0.0163  37  ILE C CB  
3686 C CG1 . ILE C 37  ? 0.9387 0.6060 0.7104 -0.0582 -0.2806 0.0171  37  ILE C CG1 
3687 C CG2 . ILE C 37  ? 0.8912 0.5736 0.6823 -0.0602 -0.2807 0.0129  37  ILE C CG2 
3688 C CD1 . ILE C 37  ? 0.9574 0.6297 0.7320 -0.0581 -0.2825 0.0155  37  ILE C CD1 
3689 N N   . ARG C 38  ? 0.9083 0.5832 0.7088 -0.0683 -0.2810 0.0171  38  ARG C N   
3690 C CA  . ARG C 38  ? 0.8185 0.4961 0.6286 -0.0698 -0.2792 0.0184  38  ARG C CA  
3691 C C   . ARG C 38  ? 0.8133 0.4998 0.6355 -0.0690 -0.2775 0.0146  38  ARG C C   
3692 O O   . ARG C 38  ? 0.8100 0.5024 0.6354 -0.0685 -0.2783 0.0105  38  ARG C O   
3693 C CB  . ARG C 38  ? 0.8161 0.4924 0.6315 -0.0734 -0.2799 0.0204  38  ARG C CB  
3694 C CG  . ARG C 38  ? 0.8109 0.4909 0.6336 -0.0753 -0.2814 0.0171  38  ARG C CG  
3695 C CD  . ARG C 38  ? 0.8089 0.4870 0.6368 -0.0788 -0.2818 0.0197  38  ARG C CD  
3696 N NE  . ARG C 38  ? 0.8217 0.5042 0.6592 -0.0812 -0.2826 0.0161  38  ARG C NE  
3697 C CZ  . ARG C 38  ? 0.8538 0.5352 0.6971 -0.0844 -0.2830 0.0177  38  ARG C CZ  
3698 N NH1 . ARG C 38  ? 0.8153 0.4922 0.6559 -0.0854 -0.2826 0.0232  38  ARG C NH1 
3699 N NH2 . ARG C 38  ? 0.8864 0.5722 0.7389 -0.0866 -0.2837 0.0137  38  ARG C NH2 
3700 N N   . GLN C 39  ? 0.8124 0.5010 0.6417 -0.0688 -0.2750 0.0158  39  GLN C N   
3701 C CA  . GLN C 39  ? 0.8395 0.5365 0.6805 -0.0680 -0.2727 0.0118  39  GLN C CA  
3702 C C   . GLN C 39  ? 0.8989 0.5984 0.7544 -0.0703 -0.2700 0.0130  39  GLN C C   
3703 O O   . GLN C 39  ? 0.9841 0.6798 0.8387 -0.0702 -0.2689 0.0180  39  GLN C O   
3704 C CB  . GLN C 39  ? 0.9132 0.6105 0.7485 -0.0646 -0.2715 0.0116  39  GLN C CB  
3705 C CG  . GLN C 39  ? 0.9430 0.6495 0.7897 -0.0637 -0.2690 0.0070  39  GLN C CG  
3706 C CD  . GLN C 39  ? 1.0679 0.7748 0.9079 -0.0601 -0.2681 0.0067  39  GLN C CD  
3707 O OE1 . GLN C 39  ? 1.1070 0.8066 0.9369 -0.0588 -0.2685 0.0107  39  GLN C OE1 
3708 N NE2 . GLN C 39  ? 1.0621 0.7784 0.9080 -0.0587 -0.2668 0.0016  39  GLN C NE2 
3709 N N   . SER C 40  ? 0.9178 0.6246 0.7875 -0.0722 -0.2686 0.0085  40  SER C N   
3710 C CA  . SER C 40  ? 0.8864 0.5961 0.7728 -0.0743 -0.2651 0.0093  40  SER C CA  
3711 C C   . SER C 40  ? 0.9448 0.6650 0.8460 -0.0749 -0.2623 0.0018  40  SER C C   
3712 O O   . SER C 40  ? 0.8626 0.5883 0.7622 -0.0750 -0.2641 -0.0036 40  SER C O   
3713 C CB  . SER C 40  ? 0.8911 0.5978 0.7815 -0.0775 -0.2658 0.0123  40  SER C CB  
3714 O OG  . SER C 40  ? 0.8789 0.5870 0.7666 -0.0790 -0.2687 0.0084  40  SER C OG  
3715 N N   . PRO C 41  ? 0.9890 0.7131 0.9056 -0.0754 -0.2578 0.0011  41  PRO C N   
3716 C CA  . PRO C 41  ? 0.9435 0.6786 0.8767 -0.0767 -0.2544 -0.0071 41  PRO C CA  
3717 C C   . PRO C 41  ? 0.8871 0.6272 0.8274 -0.0801 -0.2554 -0.0117 41  PRO C C   
3718 O O   . PRO C 41  ? 0.8624 0.6134 0.8137 -0.0815 -0.2536 -0.0199 41  PRO C O   
3719 C CB  . PRO C 41  ? 0.8959 0.6315 0.8461 -0.0776 -0.2489 -0.0049 41  PRO C CB  
3720 C CG  . PRO C 41  ? 1.0255 0.7530 0.9645 -0.0749 -0.2497 0.0031  41  PRO C CG  
3721 C CD  . PRO C 41  ? 1.0556 0.7753 0.9758 -0.0746 -0.2550 0.0077  41  PRO C CD  
3722 N N   . LYS C 42  ? 0.8945 0.6274 0.8285 -0.0816 -0.2582 -0.0069 42  LYS C N   
3723 C CA  . LYS C 42  ? 0.8153 0.5507 0.7599 -0.0855 -0.2581 -0.0093 42  LYS C CA  
3724 C C   . LYS C 42  ? 0.8640 0.5997 0.7967 -0.0859 -0.2631 -0.0116 42  LYS C C   
3725 O O   . LYS C 42  ? 0.7722 0.5161 0.7142 -0.0886 -0.2631 -0.0179 42  LYS C O   
3726 C CB  . LYS C 42  ? 0.8591 0.5868 0.8079 -0.0871 -0.2568 -0.0015 42  LYS C CB  
3727 C CG  . LYS C 42  ? 0.8642 0.5953 0.8276 -0.0912 -0.2554 -0.0044 42  LYS C CG  
3728 C CD  . LYS C 42  ? 0.8299 0.5565 0.8036 -0.0930 -0.2525 0.0025  42  LYS C CD  
3729 C CE  . LYS C 42  ? 0.8725 0.6001 0.8505 -0.0967 -0.2542 -0.0003 42  LYS C CE  
3730 N NZ  . LYS C 42  ? 0.9242 0.6629 0.9224 -0.0993 -0.2501 -0.0100 42  LYS C NZ  
3731 N N   . LYS C 43  ? 0.9341 0.6615 0.8472 -0.0835 -0.2672 -0.0066 43  LYS C N   
3732 C CA  . LYS C 43  ? 0.9110 0.6383 0.8118 -0.0829 -0.2716 -0.0082 43  LYS C CA  
3733 C C   . LYS C 43  ? 0.7889 0.5208 0.6803 -0.0791 -0.2726 -0.0107 43  LYS C C   
3734 O O   . LYS C 43  ? 0.7895 0.5234 0.6721 -0.0780 -0.2756 -0.0120 43  LYS C O   
3735 C CB  . LYS C 43  ? 0.9075 0.6227 0.7937 -0.0828 -0.2749 -0.0014 43  LYS C CB  
3736 C CG  . LYS C 43  ? 0.9436 0.6535 0.8370 -0.0855 -0.2733 0.0035  43  LYS C CG  
3737 C CD  . LYS C 43  ? 1.0313 0.7448 0.9374 -0.0895 -0.2730 0.0006  43  LYS C CD  
3738 C CE  . LYS C 43  ? 0.9367 0.6447 0.8305 -0.0904 -0.2776 0.0018  43  LYS C CE  
3739 N NZ  . LYS C 43  ? 1.0043 0.7134 0.9088 -0.0946 -0.2777 0.0005  43  LYS C NZ  
3740 N N   . GLY C 44  ? 0.7822 0.5159 0.6757 -0.0769 -0.2698 -0.0108 44  GLY C N   
3741 C CA  . GLY C 44  ? 0.7845 0.5221 0.6690 -0.0731 -0.2704 -0.0123 44  GLY C CA  
3742 C C   . GLY C 44  ? 0.8367 0.5634 0.7024 -0.0703 -0.2732 -0.0062 44  GLY C C   
3743 O O   . GLY C 44  ? 0.9463 0.6628 0.8065 -0.0705 -0.2733 -0.0007 44  GLY C O   
3744 N N   . LEU C 45  ? 0.8445 0.5742 0.7008 -0.0677 -0.2751 -0.0072 45  LEU C N   
3745 C CA  . LEU C 45  ? 0.8325 0.5525 0.6723 -0.0652 -0.2772 -0.0022 45  LEU C CA  
3746 C C   . LEU C 45  ? 0.8371 0.5545 0.6729 -0.0668 -0.2802 -0.0016 45  LEU C C   
3747 O O   . LEU C 45  ? 0.8002 0.5258 0.6367 -0.0661 -0.2814 -0.0046 45  LEU C O   
3748 C CB  . LEU C 45  ? 0.8665 0.5911 0.6996 -0.0608 -0.2768 -0.0027 45  LEU C CB  
3749 C CG  . LEU C 45  ? 0.8899 0.6081 0.7162 -0.0582 -0.2751 0.0005  45  LEU C CG  
3750 C CD1 . LEU C 45  ? 0.8722 0.5767 0.6868 -0.0583 -0.2763 0.0059  45  LEU C CD1 
3751 C CD2 . LEU C 45  ? 0.9430 0.6637 0.7800 -0.0595 -0.2725 -0.0011 45  LEU C CD2 
3752 N N   . GLU C 46  ? 0.8418 0.5487 0.6734 -0.0689 -0.2813 0.0022  46  GLU C N   
3753 C CA  . GLU C 46  ? 0.9028 0.6062 0.7310 -0.0709 -0.2840 0.0027  46  GLU C CA  
3754 C C   . GLU C 46  ? 0.8710 0.5640 0.6837 -0.0690 -0.2853 0.0069  46  GLU C C   
3755 O O   . GLU C 46  ? 0.8406 0.5258 0.6471 -0.0686 -0.2844 0.0104  46  GLU C O   
3756 C CB  . GLU C 46  ? 0.8443 0.5447 0.6805 -0.0751 -0.2839 0.0035  46  GLU C CB  
3757 C CG  . GLU C 46  ? 0.8682 0.5689 0.7056 -0.0777 -0.2865 0.0020  46  GLU C CG  
3758 C CD  . GLU C 46  ? 0.9050 0.6040 0.7523 -0.0819 -0.2860 0.0028  46  GLU C CD  
3759 O OE1 . GLU C 46  ? 0.9209 0.6187 0.7743 -0.0824 -0.2833 0.0050  46  GLU C OE1 
3760 O OE2 . GLU C 46  ? 0.9162 0.6153 0.7656 -0.0845 -0.2880 0.0015  46  GLU C OE2 
3761 N N   . TRP C 47  ? 0.8490 0.5427 0.6563 -0.0679 -0.2872 0.0063  47  TRP C N   
3762 C CA  . TRP C 47  ? 0.9004 0.5843 0.6947 -0.0664 -0.2880 0.0096  47  TRP C CA  
3763 C C   . TRP C 47  ? 0.9310 0.6078 0.7232 -0.0699 -0.2900 0.0107  47  TRP C C   
3764 O O   . TRP C 47  ? 0.9302 0.6109 0.7271 -0.0718 -0.2920 0.0086  47  TRP C O   
3765 C CB  . TRP C 47  ? 0.9108 0.5996 0.7014 -0.0629 -0.2884 0.0091  47  TRP C CB  
3766 C CG  . TRP C 47  ? 0.8390 0.5187 0.6190 -0.0618 -0.2891 0.0119  47  TRP C CG  
3767 C CD1 . TRP C 47  ? 0.8804 0.5516 0.6511 -0.0595 -0.2872 0.0148  47  TRP C CD1 
3768 C CD2 . TRP C 47  ? 0.8394 0.5178 0.6179 -0.0632 -0.2915 0.0115  47  TRP C CD2 
3769 N NE1 . TRP C 47  ? 0.9743 0.6388 0.7384 -0.0592 -0.2879 0.0162  47  TRP C NE1 
3770 C CE2 . TRP C 47  ? 0.9614 0.6300 0.7296 -0.0614 -0.2907 0.0144  47  TRP C CE2 
3771 C CE3 . TRP C 47  ? 0.9100 0.5946 0.6954 -0.0659 -0.2940 0.0088  47  TRP C CE3 
3772 C CZ2 . TRP C 47  ? 0.9986 0.6632 0.7629 -0.0620 -0.2923 0.0148  47  TRP C CZ2 
3773 C CZ3 . TRP C 47  ? 0.9210 0.6017 0.7019 -0.0665 -0.2960 0.0093  47  TRP C CZ3 
3774 C CH2 . TRP C 47  ? 0.9792 0.6498 0.7495 -0.0645 -0.2952 0.0124  47  TRP C CH2 
3775 N N   . ILE C 48  ? 0.9210 0.5884 0.7064 -0.0709 -0.2895 0.0138  48  ILE C N   
3776 C CA  . ILE C 48  ? 0.8582 0.5196 0.6416 -0.0743 -0.2911 0.0150  48  ILE C CA  
3777 C C   . ILE C 48  ? 0.8871 0.5429 0.6613 -0.0737 -0.2927 0.0150  48  ILE C C   
3778 O O   . ILE C 48  ? 0.8909 0.5473 0.6671 -0.0757 -0.2949 0.0138  48  ILE C O   
3779 C CB  . ILE C 48  ? 0.8257 0.4818 0.6058 -0.0757 -0.2898 0.0182  48  ILE C CB  
3780 C CG1 . ILE C 48  ? 0.8336 0.4952 0.6226 -0.0754 -0.2877 0.0186  48  ILE C CG1 
3781 C CG2 . ILE C 48  ? 0.8301 0.4827 0.6103 -0.0794 -0.2913 0.0197  48  ILE C CG2 
3782 C CD1 . ILE C 48  ? 0.8256 0.4837 0.6107 -0.0757 -0.2861 0.0222  48  ILE C CD1 
3783 N N   . GLY C 49  ? 0.8673 0.5177 0.6322 -0.0711 -0.2911 0.0164  49  GLY C N   
3784 C CA  . GLY C 49  ? 0.8786 0.5233 0.6358 -0.0701 -0.2917 0.0165  49  GLY C CA  
3785 C C   . GLY C 49  ? 0.9471 0.5865 0.6966 -0.0670 -0.2887 0.0179  49  GLY C C   
3786 O O   . GLY C 49  ? 0.9302 0.5703 0.6796 -0.0659 -0.2866 0.0186  49  GLY C O   
3787 N N   . GLU C 50  ? 0.9786 0.6128 0.7222 -0.0657 -0.2882 0.0181  50  GLU C N   
3788 C CA  . GLU C 50  ? 0.9554 0.5839 0.6928 -0.0629 -0.2846 0.0192  50  GLU C CA  
3789 C C   . GLU C 50  ? 0.9726 0.5921 0.7033 -0.0643 -0.2839 0.0188  50  GLU C C   
3790 O O   . GLU C 50  ? 0.9033 0.5215 0.6336 -0.0664 -0.2865 0.0180  50  GLU C O   
3791 C CB  . GLU C 50  ? 1.0160 0.6497 0.7556 -0.0580 -0.2830 0.0205  50  GLU C CB  
3792 C CG  . GLU C 50  ? 1.0295 0.6649 0.7695 -0.0563 -0.2841 0.0210  50  GLU C CG  
3793 C CD  . GLU C 50  ? 1.0615 0.7050 0.8046 -0.0512 -0.2825 0.0231  50  GLU C CD  
3794 O OE1 . GLU C 50  ? 1.0726 0.7206 0.8179 -0.0494 -0.2809 0.0235  50  GLU C OE1 
3795 O OE2 . GLU C 50  ? 1.0888 0.7349 0.8324 -0.0489 -0.2827 0.0245  50  GLU C OE2 
3796 N N   . ILE C 51  ? 1.0694 0.6828 0.7951 -0.0631 -0.2800 0.0189  51  ILE C N   
3797 C CA  . ILE C 51  ? 1.1141 0.7191 0.8340 -0.0644 -0.2781 0.0176  51  ILE C CA  
3798 C C   . ILE C 51  ? 1.1613 0.7620 0.8796 -0.0609 -0.2729 0.0182  51  ILE C C   
3799 O O   . ILE C 51  ? 1.0959 0.6991 0.8161 -0.0585 -0.2707 0.0193  51  ILE C O   
3800 C CB  . ILE C 51  ? 1.0372 0.6393 0.7532 -0.0690 -0.2783 0.0158  51  ILE C CB  
3801 C CG1 . ILE C 51  ? 1.0963 0.6913 0.8068 -0.0711 -0.2774 0.0136  51  ILE C CG1 
3802 C CG2 . ILE C 51  ? 1.0023 0.6046 0.7171 -0.0689 -0.2750 0.0155  51  ILE C CG2 
3803 C CD1 . ILE C 51  ? 1.1113 0.7060 0.8181 -0.0758 -0.2781 0.0119  51  ILE C CD1 
3804 N N   . ASP C 52  ? 1.3278 0.9221 1.0436 -0.0604 -0.2707 0.0175  52  ASP C N   
3805 C CA  . ASP C 52  ? 1.3647 0.9533 1.0797 -0.0579 -0.2646 0.0175  52  ASP C CA  
3806 C C   . ASP C 52  ? 1.5679 1.1497 1.2782 -0.0619 -0.2619 0.0135  52  ASP C C   
3807 O O   . ASP C 52  ? 1.5875 1.1692 1.2946 -0.0661 -0.2650 0.0113  52  ASP C O   
3808 C CB  . ASP C 52  ? 1.3021 0.8895 1.0195 -0.0538 -0.2629 0.0201  52  ASP C CB  
3809 C CG  . ASP C 52  ? 1.2981 0.8835 1.0137 -0.0557 -0.2663 0.0192  52  ASP C CG  
3810 O OD1 . ASP C 52  ? 1.2967 0.8746 1.0086 -0.0584 -0.2646 0.0162  52  ASP C OD1 
3811 O OD2 . ASP C 52  ? 1.3762 0.9681 1.0944 -0.0548 -0.2707 0.0209  52  ASP C OD2 
3812 N N   . GLU C 53  ? 2.3760 1.9529 2.0867 -0.0606 -0.2557 0.0123  53  GLU C N   
3813 C CA  . GLU C 53  ? 2.3798 1.9520 2.0870 -0.0645 -0.2523 0.0075  53  GLU C CA  
3814 C C   . GLU C 53  ? 2.3775 1.9447 2.0818 -0.0668 -0.2526 0.0049  53  GLU C C   
3815 O O   . GLU C 53  ? 2.3703 1.9370 2.0705 -0.0714 -0.2527 0.0008  53  GLU C O   
3816 C CB  . GLU C 53  ? 2.3947 1.9630 2.1046 -0.0626 -0.2449 0.0063  53  GLU C CB  
3817 C CG  . GLU C 53  ? 2.4012 1.9654 2.1090 -0.0666 -0.2400 0.0003  53  GLU C CG  
3818 C CD  . GLU C 53  ? 2.4133 1.9697 2.1235 -0.0653 -0.2343 -0.0014 53  GLU C CD  
3819 O OE1 . GLU C 53  ? 2.4162 1.9707 2.1281 -0.0621 -0.2358 0.0023  53  GLU C OE1 
3820 O OE2 . GLU C 53  ? 2.4182 1.9710 2.1294 -0.0677 -0.2281 -0.0066 53  GLU C OE2 
3821 N N   . ILE C 54  ? 1.8166 1.3811 1.5229 -0.0637 -0.2527 0.0073  54  ILE C N   
3822 C CA  . ILE C 54  ? 1.6217 1.1811 1.3252 -0.0658 -0.2532 0.0049  54  ILE C CA  
3823 C C   . ILE C 54  ? 1.5622 1.1251 1.2615 -0.0700 -0.2600 0.0040  54  ILE C C   
3824 O O   . ILE C 54  ? 1.5003 1.0599 1.1957 -0.0734 -0.2604 0.0006  54  ILE C O   
3825 C CB  . ILE C 54  ? 1.5115 1.0685 1.2185 -0.0612 -0.2523 0.0086  54  ILE C CB  
3826 C CG1 . ILE C 54  ? 1.6253 1.1805 1.3380 -0.0563 -0.2455 0.0111  54  ILE C CG1 
3827 C CG2 . ILE C 54  ? 1.3298 0.8801 1.0343 -0.0631 -0.2515 0.0056  54  ILE C CG2 
3828 C CD1 . ILE C 54  ? 1.4873 1.0408 1.2043 -0.0513 -0.2434 0.0154  54  ILE C CD1 
3829 N N   . GLY C 55  ? 1.5057 1.0756 1.2066 -0.0697 -0.2649 0.0069  55  GLY C N   
3830 C CA  . GLY C 55  ? 1.2920 0.8658 0.9907 -0.0736 -0.2705 0.0065  55  GLY C CA  
3831 C C   . GLY C 55  ? 1.2632 0.8412 0.9651 -0.0724 -0.2759 0.0095  55  GLY C C   
3832 O O   . GLY C 55  ? 1.2799 0.8616 0.9818 -0.0755 -0.2803 0.0097  55  GLY C O   
3833 N N   . ARG C 56  ? 1.2674 0.8459 0.9728 -0.0683 -0.2756 0.0119  56  ARG C N   
3834 C CA  . ARG C 56  ? 1.2233 0.8076 0.9323 -0.0675 -0.2806 0.0139  56  ARG C CA  
3835 C C   . ARG C 56  ? 1.1744 0.7673 0.8879 -0.0674 -0.2830 0.0153  56  ARG C C   
3836 O O   . ARG C 56  ? 1.1336 0.7285 0.8486 -0.0652 -0.2802 0.0163  56  ARG C O   
3837 C CB  . ARG C 56  ? 1.2768 0.8616 0.9885 -0.0628 -0.2792 0.0163  56  ARG C CB  
3838 C CG  . ARG C 56  ? 1.3081 0.8998 1.0234 -0.0626 -0.2844 0.0175  56  ARG C CG  
3839 C CD  . ARG C 56  ? 1.2632 0.8507 0.9752 -0.0669 -0.2879 0.0151  56  ARG C CD  
3840 N NE  . ARG C 56  ? 1.2363 0.8315 0.9525 -0.0688 -0.2934 0.0151  56  ARG C NE  
3841 C CZ  . ARG C 56  ? 1.2786 0.8754 0.9955 -0.0730 -0.2963 0.0137  56  ARG C CZ  
3842 N NH1 . ARG C 56  ? 1.3074 0.8998 1.0204 -0.0756 -0.2948 0.0126  56  ARG C NH1 
3843 N NH2 . ARG C 56  ? 1.2058 0.8098 0.9283 -0.0746 -0.3005 0.0134  56  ARG C NH2 
3844 N N   . THR C 57  ? 1.2462 0.8441 0.9627 -0.0697 -0.2878 0.0152  57  THR C N   
3845 C CA  . THR C 57  ? 1.2051 0.8110 0.9271 -0.0704 -0.2898 0.0159  57  THR C CA  
3846 C C   . THR C 57  ? 1.1301 0.7442 0.8587 -0.0692 -0.2930 0.0163  57  THR C C   
3847 O O   . THR C 57  ? 1.1959 0.8096 0.9243 -0.0692 -0.2950 0.0160  57  THR C O   
3848 C CB  . THR C 57  ? 1.2246 0.8302 0.9461 -0.0751 -0.2918 0.0150  57  THR C CB  
3849 O OG1 . THR C 57  ? 1.2345 0.8378 0.9549 -0.0779 -0.2949 0.0141  57  THR C OG1 
3850 C CG2 . THR C 57  ? 1.2200 0.8204 0.9355 -0.0764 -0.2886 0.0143  57  THR C CG2 
3851 N N   . LYS C 58  ? 0.9818 0.6044 0.7166 -0.0682 -0.2934 0.0167  58  LYS C N   
3852 C CA  . LYS C 58  ? 1.0199 0.6526 0.7626 -0.0684 -0.2964 0.0158  58  LYS C CA  
3853 C C   . LYS C 58  ? 1.0523 0.6902 0.8013 -0.0706 -0.2970 0.0150  58  LYS C C   
3854 O O   . LYS C 58  ? 1.0410 0.6793 0.7898 -0.0692 -0.2945 0.0159  58  LYS C O   
3855 C CB  . LYS C 58  ? 1.0260 0.6667 0.7715 -0.0636 -0.2955 0.0169  58  LYS C CB  
3856 C CG  . LYS C 58  ? 1.0073 0.6546 0.7561 -0.0606 -0.2931 0.0178  58  LYS C CG  
3857 C CD  . LYS C 58  ? 1.0401 0.6988 0.7931 -0.0564 -0.2928 0.0188  58  LYS C CD  
3858 C CE  . LYS C 58  ? 1.0209 0.6903 0.7810 -0.0584 -0.2966 0.0163  58  LYS C CE  
3859 N NZ  . LYS C 58  ? 1.0455 0.7292 0.8102 -0.0542 -0.2962 0.0171  58  LYS C NZ  
3860 N N   . TYR C 59  ? 1.0028 0.6444 0.7578 -0.0742 -0.2998 0.0134  59  TYR C N   
3861 C CA  . TYR C 59  ? 1.0055 0.6517 0.7682 -0.0765 -0.2998 0.0129  59  TYR C CA  
3862 C C   . TYR C 59  ? 1.0880 0.7461 0.8618 -0.0767 -0.3010 0.0103  59  TYR C C   
3863 O O   . TYR C 59  ? 1.0674 0.7312 0.8425 -0.0752 -0.3023 0.0089  59  TYR C O   
3864 C CB  . TYR C 59  ? 1.0580 0.6990 0.8206 -0.0810 -0.3011 0.0135  59  TYR C CB  
3865 C CG  . TYR C 59  ? 0.9666 0.5977 0.7185 -0.0815 -0.3000 0.0152  59  TYR C CG  
3866 C CD1 . TYR C 59  ? 0.9108 0.5399 0.6595 -0.0810 -0.2975 0.0168  59  TYR C CD1 
3867 C CD2 . TYR C 59  ? 0.9061 0.5308 0.6516 -0.0829 -0.3015 0.0147  59  TYR C CD2 
3868 C CE1 . TYR C 59  ? 0.9051 0.5272 0.6448 -0.0819 -0.2962 0.0175  59  TYR C CE1 
3869 C CE2 . TYR C 59  ? 0.9617 0.5787 0.6982 -0.0837 -0.3001 0.0154  59  TYR C CE2 
3870 C CZ  . TYR C 59  ? 0.9802 0.5964 0.7139 -0.0834 -0.2974 0.0166  59  TYR C CZ  
3871 O OH  . TYR C 59  ? 1.0486 0.6590 0.7740 -0.0846 -0.2958 0.0164  59  TYR C OH  
3872 N N   . SER C 60  ? 1.1473 0.8103 0.9299 -0.0785 -0.3002 0.0094  60  SER C N   
3873 C CA  . SER C 60  ? 1.1493 0.8237 0.9445 -0.0800 -0.3009 0.0059  60  SER C CA  
3874 C C   . SER C 60  ? 1.1632 0.8365 0.9634 -0.0845 -0.3031 0.0046  60  SER C C   
3875 O O   . SER C 60  ? 1.1888 0.8540 0.9863 -0.0869 -0.3033 0.0070  60  SER C O   
3876 C CB  . SER C 60  ? 1.1462 0.8260 0.9501 -0.0801 -0.2983 0.0052  60  SER C CB  
3877 O OG  . SER C 60  ? 1.1451 0.8358 0.9630 -0.0824 -0.2984 0.0010  60  SER C OG  
3878 N N   . GLN C 61  ? 1.0786 0.7611 0.8865 -0.0856 -0.3048 0.0008  61  GLN C N   
3879 C CA  . GLN C 61  ? 1.0894 0.7712 0.9027 -0.0900 -0.3069 -0.0008 61  GLN C CA  
3880 C C   . GLN C 61  ? 1.1373 0.8191 0.9614 -0.0936 -0.3052 -0.0007 61  GLN C C   
3881 O O   . GLN C 61  ? 1.2252 0.9015 1.0505 -0.0969 -0.3062 0.0005  61  GLN C O   
3882 C CB  . GLN C 61  ? 1.1143 0.8081 0.9350 -0.0907 -0.3088 -0.0056 61  GLN C CB  
3883 C CG  . GLN C 61  ? 1.2485 0.9434 1.0597 -0.0870 -0.3104 -0.0048 61  GLN C CG  
3884 C CD  . GLN C 61  ? 1.3872 1.0701 1.1877 -0.0876 -0.3127 -0.0022 61  GLN C CD  
3885 O OE1 . GLN C 61  ? 1.3860 1.0627 1.1877 -0.0915 -0.3140 -0.0023 61  GLN C OE1 
3886 N NE2 . GLN C 61  ? 1.3497 1.0293 1.1401 -0.0837 -0.3128 0.0002  61  GLN C NE2 
3887 N N   . SER C 62  ? 1.0581 0.7462 0.8905 -0.0927 -0.3022 -0.0017 62  SER C N   
3888 C CA  . SER C 62  ? 1.0461 0.7346 0.8902 -0.0956 -0.2997 -0.0010 62  SER C CA  
3889 C C   . SER C 62  ? 1.1259 0.8037 0.9623 -0.0955 -0.2989 0.0052  62  SER C C   
3890 O O   . SER C 62  ? 1.1113 0.7875 0.9553 -0.0983 -0.2976 0.0074  62  SER C O   
3891 C CB  . SER C 62  ? 0.9996 0.6979 0.8549 -0.0945 -0.2964 -0.0039 62  SER C CB  
3892 O OG  . SER C 62  ? 0.9967 0.6936 0.8425 -0.0902 -0.2956 -0.0020 62  SER C OG  
3893 N N   . LEU C 63  ? 1.1262 0.7975 0.9482 -0.0924 -0.2993 0.0080  63  LEU C N   
3894 C CA  . LEU C 63  ? 0.9330 0.5965 0.7474 -0.0922 -0.2983 0.0131  63  LEU C CA  
3895 C C   . LEU C 63  ? 1.0535 0.7079 0.8541 -0.0925 -0.3005 0.0150  63  LEU C C   
3896 O O   . LEU C 63  ? 1.0594 0.7087 0.8534 -0.0927 -0.2997 0.0187  63  LEU C O   
3897 C CB  . LEU C 63  ? 0.8704 0.5342 0.6805 -0.0887 -0.2960 0.0143  63  LEU C CB  
3898 C CG  . LEU C 63  ? 0.9204 0.5923 0.7431 -0.0880 -0.2932 0.0130  63  LEU C CG  
3899 C CD1 . LEU C 63  ? 0.8655 0.5368 0.6815 -0.0843 -0.2916 0.0139  63  LEU C CD1 
3900 C CD2 . LEU C 63  ? 0.9605 0.6330 0.7938 -0.0906 -0.2911 0.0159  63  LEU C CD2 
3901 N N   . ARG C 64  ? 1.0309 0.6843 0.8277 -0.0927 -0.3031 0.0124  64  ARG C N   
3902 C CA  . ARG C 64  ? 1.0561 0.7008 0.8393 -0.0923 -0.3047 0.0136  64  ARG C CA  
3903 C C   . ARG C 64  ? 1.0497 0.6889 0.8304 -0.0956 -0.3053 0.0163  64  ARG C C   
3904 O O   . ARG C 64  ? 1.1351 0.7684 0.9055 -0.0952 -0.3047 0.0185  64  ARG C O   
3905 C CB  . ARG C 64  ? 1.1253 0.7709 0.9066 -0.0918 -0.3073 0.0106  64  ARG C CB  
3906 C CG  . ARG C 64  ? 1.2323 0.8691 1.0001 -0.0906 -0.3082 0.0114  64  ARG C CG  
3907 C CD  . ARG C 64  ? 1.2733 0.9126 1.0392 -0.0880 -0.3095 0.0094  64  ARG C CD  
3908 N NE  . ARG C 64  ? 1.3424 0.9839 1.1125 -0.0907 -0.3127 0.0072  64  ARG C NE  
3909 C CZ  . ARG C 64  ? 1.3453 0.9799 1.1082 -0.0916 -0.3146 0.0073  64  ARG C CZ  
3910 N NH1 . ARG C 64  ? 1.2385 0.8637 0.9901 -0.0903 -0.3134 0.0090  64  ARG C NH1 
3911 N NH2 . ARG C 64  ? 1.3235 0.9610 1.0910 -0.0942 -0.3176 0.0051  64  ARG C NH2 
3912 N N   . SER C 65  ? 0.9796 0.6217 0.7702 -0.0989 -0.3063 0.0161  65  SER C N   
3913 C CA  . SER C 65  ? 0.9746 0.6123 0.7631 -0.1019 -0.3070 0.0190  65  SER C CA  
3914 C C   . SER C 65  ? 0.9885 0.6257 0.7748 -0.1017 -0.3044 0.0238  65  SER C C   
3915 O O   . SER C 65  ? 0.9775 0.6106 0.7557 -0.1029 -0.3048 0.0263  65  SER C O   
3916 C CB  . SER C 65  ? 0.9214 0.5632 0.7236 -0.1054 -0.3076 0.0183  65  SER C CB  
3917 O OG  . SER C 65  ? 1.0732 0.7108 0.8729 -0.1082 -0.3085 0.0213  65  SER C OG  
3918 N N   . ARG C 66  ? 0.9033 0.5455 0.6966 -0.1001 -0.3018 0.0249  66  ARG C N   
3919 C CA  . ARG C 66  ? 0.8944 0.5377 0.6866 -0.0997 -0.2992 0.0297  66  ARG C CA  
3920 C C   . ARG C 66  ? 0.9832 0.6241 0.7638 -0.0968 -0.2983 0.0295  66  ARG C C   
3921 O O   . ARG C 66  ? 0.9816 0.6241 0.7597 -0.0965 -0.2964 0.0331  66  ARG C O   
3922 C CB  . ARG C 66  ? 0.9129 0.5632 0.7206 -0.0997 -0.2964 0.0315  66  ARG C CB  
3923 C CG  . ARG C 66  ? 0.8733 0.5268 0.6957 -0.1025 -0.2963 0.0308  66  ARG C CG  
3924 C CD  . ARG C 66  ? 0.7963 0.4566 0.6337 -0.1018 -0.2935 0.0289  66  ARG C CD  
3925 N NE  . ARG C 66  ? 0.7991 0.4616 0.6372 -0.0996 -0.2905 0.0327  66  ARG C NE  
3926 C CZ  . ARG C 66  ? 0.7975 0.4646 0.6434 -0.0978 -0.2882 0.0308  66  ARG C CZ  
3927 N NH1 . ARG C 66  ? 0.7932 0.4644 0.6469 -0.0979 -0.2883 0.0249  66  ARG C NH1 
3928 N NH2 . ARG C 66  ? 0.8002 0.4689 0.6460 -0.0958 -0.2856 0.0347  66  ARG C NH2 
3929 N N   . ALA C 67  ? 1.0059 0.6440 0.7803 -0.0947 -0.2992 0.0256  67  ALA C N   
3930 C CA  . ALA C 67  ? 1.0031 0.6389 0.7684 -0.0918 -0.2977 0.0252  67  ALA C CA  
3931 C C   . ALA C 67  ? 0.9164 0.5452 0.6687 -0.0920 -0.2984 0.0240  67  ALA C C   
3932 O O   . ALA C 67  ? 0.8999 0.5252 0.6497 -0.0930 -0.3006 0.0221  67  ALA C O   
3933 C CB  . ALA C 67  ? 0.9464 0.5847 0.7148 -0.0888 -0.2973 0.0224  67  ALA C CB  
3934 N N   . THR C 68  ? 0.9470 0.5742 0.6915 -0.0911 -0.2963 0.0246  68  THR C N   
3935 C CA  . THR C 68  ? 0.9600 0.5809 0.6930 -0.0910 -0.2958 0.0226  68  THR C CA  
3936 C C   . THR C 68  ? 0.9648 0.5850 0.6934 -0.0884 -0.2929 0.0217  68  THR C C   
3937 O O   . THR C 68  ? 0.8861 0.5102 0.6152 -0.0887 -0.2911 0.0235  68  THR C O   
3938 C CB  . THR C 68  ? 0.9719 0.5925 0.6998 -0.0942 -0.2960 0.0238  68  THR C CB  
3939 O OG1 . THR C 68  ? 1.0186 0.6390 0.7502 -0.0965 -0.2987 0.0245  68  THR C OG1 
3940 C CG2 . THR C 68  ? 0.9581 0.5730 0.6750 -0.0943 -0.2946 0.0206  68  THR C CG2 
3941 N N   . LEU C 69  ? 1.0233 0.6391 0.7484 -0.0859 -0.2921 0.0193  69  LEU C N   
3942 C CA  . LEU C 69  ? 1.0357 0.6500 0.7572 -0.0834 -0.2889 0.0184  69  LEU C CA  
3943 C C   . LEU C 69  ? 0.9961 0.6047 0.7087 -0.0844 -0.2865 0.0160  69  LEU C C   
3944 O O   . LEU C 69  ? 0.9662 0.5705 0.6752 -0.0857 -0.2875 0.0145  69  LEU C O   
3945 C CB  . LEU C 69  ? 1.0124 0.6266 0.7368 -0.0796 -0.2885 0.0177  69  LEU C CB  
3946 C CG  . LEU C 69  ? 0.9759 0.5964 0.7074 -0.0777 -0.2882 0.0191  69  LEU C CG  
3947 C CD1 . LEU C 69  ? 0.9948 0.6173 0.7295 -0.0741 -0.2883 0.0185  69  LEU C CD1 
3948 C CD2 . LEU C 69  ? 1.0335 0.6541 0.7620 -0.0772 -0.2852 0.0196  69  LEU C CD2 
3949 N N   . SER C 70  ? 0.9382 0.5473 0.6479 -0.0839 -0.2832 0.0152  70  SER C N   
3950 C CA  . SER C 70  ? 0.9678 0.5731 0.6705 -0.0853 -0.2802 0.0121  70  SER C CA  
3951 C C   . SER C 70  ? 0.9622 0.5668 0.6638 -0.0834 -0.2760 0.0107  70  SER C C   
3952 O O   . SER C 70  ? 0.9450 0.5533 0.6505 -0.0816 -0.2759 0.0126  70  SER C O   
3953 C CB  . SER C 70  ? 1.0026 0.6123 0.7022 -0.0894 -0.2808 0.0121  70  SER C CB  
3954 O OG  . SER C 70  ? 0.9955 0.6129 0.6983 -0.0898 -0.2808 0.0150  70  SER C OG  
3955 N N   . ILE C 71  ? 0.9562 0.5562 0.6533 -0.0840 -0.2723 0.0069  71  ILE C N   
3956 C CA  . ILE C 71  ? 1.0708 0.6692 0.7676 -0.0824 -0.2675 0.0050  71  ILE C CA  
3957 C C   . ILE C 71  ? 1.1462 0.7441 0.8383 -0.0858 -0.2637 0.0001  71  ILE C C   
3958 O O   . ILE C 71  ? 1.0819 0.6759 0.7711 -0.0874 -0.2631 -0.0026 71  ILE C O   
3959 C CB  . ILE C 71  ? 1.0159 0.6082 0.7151 -0.0781 -0.2655 0.0055  71  ILE C CB  
3960 C CG1 . ILE C 71  ? 1.0400 0.6310 0.7403 -0.0762 -0.2604 0.0042  71  ILE C CG1 
3961 C CG2 . ILE C 71  ? 1.0699 0.6555 0.7671 -0.0782 -0.2647 0.0036  71  ILE C CG2 
3962 C CD1 . ILE C 71  ? 1.2974 0.8842 1.0012 -0.0713 -0.2583 0.0062  71  ILE C CD1 
3963 N N   . ASP C 72  ? 1.0831 0.6860 0.7748 -0.0870 -0.2610 -0.0015 72  ASP C N   
3964 C CA  . ASP C 72  ? 1.0637 0.6679 0.7522 -0.0902 -0.2565 -0.0071 72  ASP C CA  
3965 C C   . ASP C 72  ? 1.1271 0.7267 0.8181 -0.0881 -0.2509 -0.0097 72  ASP C C   
3966 O O   . ASP C 72  ? 1.1050 0.7078 0.7982 -0.0867 -0.2502 -0.0082 72  ASP C O   
3967 C CB  . ASP C 72  ? 1.1699 0.7854 0.8565 -0.0937 -0.2573 -0.0073 72  ASP C CB  
3968 C CG  . ASP C 72  ? 1.2452 0.8647 0.9288 -0.0975 -0.2526 -0.0140 72  ASP C CG  
3969 O OD1 . ASP C 72  ? 1.2031 0.8156 0.8859 -0.0980 -0.2488 -0.0189 72  ASP C OD1 
3970 O OD2 . ASP C 72  ? 1.2060 0.8363 0.8884 -0.1002 -0.2523 -0.0147 72  ASP C OD2 
3971 N N   . THR C 73  ? 1.2093 0.8013 0.9005 -0.0876 -0.2466 -0.0133 73  THR C N   
3972 C CA  . THR C 73  ? 1.1929 0.7795 0.8880 -0.0851 -0.2407 -0.0150 73  THR C CA  
3973 C C   . THR C 73  ? 1.2386 0.8296 0.9340 -0.0884 -0.2354 -0.0208 73  THR C C   
3974 O O   . THR C 73  ? 1.2926 0.8819 0.9918 -0.0866 -0.2313 -0.0213 73  THR C O   
3975 C CB  . THR C 73  ? 1.2342 0.8114 0.9310 -0.0833 -0.2372 -0.0164 73  THR C CB  
3976 O OG1 . THR C 73  ? 1.2524 0.8296 0.9459 -0.0875 -0.2358 -0.0218 73  THR C OG1 
3977 C CG2 . THR C 73  ? 1.3087 0.8829 1.0063 -0.0796 -0.2421 -0.0105 73  THR C CG2 
3978 N N   . SER C 74  ? 1.1983 0.7959 0.8900 -0.0933 -0.2352 -0.0255 74  SER C N   
3979 C CA  . SER C 74  ? 1.1700 0.7739 0.8623 -0.0970 -0.2299 -0.0320 74  SER C CA  
3980 C C   . SER C 74  ? 1.1655 0.7771 0.8585 -0.0967 -0.2315 -0.0295 74  SER C C   
3981 O O   . SER C 74  ? 1.1272 0.7393 0.8234 -0.0970 -0.2265 -0.0328 74  SER C O   
3982 C CB  . SER C 74  ? 1.1865 0.7982 0.8743 -0.1023 -0.2299 -0.0373 74  SER C CB  
3983 O OG  . SER C 74  ? 1.2342 0.8388 0.9205 -0.1024 -0.2300 -0.0385 74  SER C OG  
3984 N N   . LYS C 75  ? 1.1764 0.7939 0.8672 -0.0962 -0.2379 -0.0236 75  LYS C N   
3985 C CA  . LYS C 75  ? 1.1686 0.7934 0.8605 -0.0956 -0.2397 -0.0205 75  LYS C CA  
3986 C C   . LYS C 75  ? 1.1969 0.8152 0.8921 -0.0905 -0.2415 -0.0149 75  LYS C C   
3987 O O   . LYS C 75  ? 1.1861 0.8094 0.8825 -0.0895 -0.2433 -0.0119 75  LYS C O   
3988 C CB  . LYS C 75  ? 1.1215 0.7575 0.8107 -0.0978 -0.2449 -0.0170 75  LYS C CB  
3989 C CG  . LYS C 75  ? 1.0958 0.7414 0.7813 -0.1028 -0.2433 -0.0221 75  LYS C CG  
3990 C CD  . LYS C 75  ? 1.0229 0.6807 0.7067 -0.1043 -0.2480 -0.0171 75  LYS C CD  
3991 C CE  . LYS C 75  ? 1.0265 0.6945 0.7063 -0.1091 -0.2468 -0.0216 75  LYS C CE  
3992 N NZ  . LYS C 75  ? 0.9652 0.6249 0.6427 -0.1096 -0.2471 -0.0237 75  LYS C NZ  
3993 N N   . LYS C 76  ? 1.2242 0.8325 0.9212 -0.0871 -0.2411 -0.0134 76  LYS C N   
3994 C CA  . LYS C 76  ? 1.2286 0.8322 0.9289 -0.0821 -0.2426 -0.0082 76  LYS C CA  
3995 C C   . LYS C 76  ? 1.2474 0.8568 0.9478 -0.0812 -0.2489 -0.0027 76  LYS C C   
3996 O O   . LYS C 76  ? 1.2645 0.8770 0.9668 -0.0795 -0.2497 -0.0002 76  LYS C O   
3997 C CB  . LYS C 76  ? 1.2618 0.8637 0.9652 -0.0804 -0.2377 -0.0095 76  LYS C CB  
3998 C CG  . LYS C 76  ? 1.3058 0.8996 1.0120 -0.0797 -0.2309 -0.0134 76  LYS C CG  
3999 C CD  . LYS C 76  ? 1.2741 0.8688 0.9830 -0.0809 -0.2249 -0.0176 76  LYS C CD  
4000 C CE  . LYS C 76  ? 1.2504 0.8465 0.9612 -0.0776 -0.2262 -0.0134 76  LYS C CE  
4001 N NZ  . LYS C 76  ? 1.2643 0.8615 0.9779 -0.0791 -0.2204 -0.0177 76  LYS C NZ  
4002 N N   . GLN C 77  ? 1.1643 0.7748 0.8630 -0.0824 -0.2530 -0.0010 77  GLN C N   
4003 C CA  . GLN C 77  ? 1.1005 0.7166 0.8007 -0.0821 -0.2583 0.0038  77  GLN C CA  
4004 C C   . GLN C 77  ? 1.0515 0.6639 0.7525 -0.0810 -0.2619 0.0061  77  GLN C C   
4005 O O   . GLN C 77  ? 1.0711 0.6780 0.7701 -0.0815 -0.2609 0.0039  77  GLN C O   
4006 C CB  . GLN C 77  ? 1.0552 0.6808 0.7534 -0.0861 -0.2596 0.0038  77  GLN C CB  
4007 C CG  . GLN C 77  ? 1.0808 0.7132 0.7789 -0.0872 -0.2572 0.0025  77  GLN C CG  
4008 C CD  . GLN C 77  ? 0.9916 0.6352 0.6875 -0.0911 -0.2580 0.0024  77  GLN C CD  
4009 O OE1 . GLN C 77  ? 0.9229 0.5690 0.6175 -0.0929 -0.2604 0.0038  77  GLN C OE1 
4010 N NE2 . GLN C 77  ? 0.9657 0.6170 0.6615 -0.0925 -0.2559 0.0010  77  GLN C NE2 
4011 N N   . PHE C 78  ? 0.9952 0.6110 0.7000 -0.0797 -0.2659 0.0103  78  PHE C N   
4012 C CA  . PHE C 78  ? 0.9473 0.5619 0.6538 -0.0795 -0.2698 0.0124  78  PHE C CA  
4013 C C   . PHE C 78  ? 1.0106 0.6324 0.7211 -0.0807 -0.2732 0.0160  78  PHE C C   
4014 O O   . PHE C 78  ? 1.0101 0.6367 0.7234 -0.0800 -0.2728 0.0177  78  PHE C O   
4015 C CB  . PHE C 78  ? 0.9735 0.5839 0.6832 -0.0755 -0.2702 0.0134  78  PHE C CB  
4016 C CG  . PHE C 78  ? 0.9443 0.5572 0.6579 -0.0723 -0.2695 0.0151  78  PHE C CG  
4017 C CD1 . PHE C 78  ? 1.0159 0.6266 0.7282 -0.0706 -0.2654 0.0138  78  PHE C CD1 
4018 C CD2 . PHE C 78  ? 0.9506 0.5682 0.6698 -0.0710 -0.2725 0.0177  78  PHE C CD2 
4019 C CE1 . PHE C 78  ? 1.0032 0.6162 0.7189 -0.0676 -0.2648 0.0155  78  PHE C CE1 
4020 C CE2 . PHE C 78  ? 0.9984 0.6188 0.7212 -0.0680 -0.2718 0.0188  78  PHE C CE2 
4021 C CZ  . PHE C 78  ? 1.0498 0.6677 0.7703 -0.0662 -0.2681 0.0179  78  PHE C CZ  
4022 N N   . SER C 79  ? 0.9996 0.6221 0.7110 -0.0824 -0.2762 0.0172  79  SER C N   
4023 C CA  . SER C 79  ? 0.9655 0.5948 0.6815 -0.0840 -0.2786 0.0209  79  SER C CA  
4024 C C   . SER C 79  ? 0.9933 0.6217 0.7146 -0.0838 -0.2818 0.0225  79  SER C C   
4025 O O   . SER C 79  ? 0.9726 0.5956 0.6924 -0.0830 -0.2827 0.0206  79  SER C O   
4026 C CB  . SER C 79  ? 0.8840 0.5181 0.5959 -0.0876 -0.2782 0.0212  79  SER C CB  
4027 O OG  . SER C 79  ? 0.9003 0.5368 0.6079 -0.0883 -0.2750 0.0188  79  SER C OG  
4028 N N   . LEU C 80  ? 1.0131 0.6473 0.7415 -0.0845 -0.2833 0.0260  80  LEU C N   
4029 C CA  . LEU C 80  ? 0.9265 0.5614 0.6622 -0.0848 -0.2859 0.0272  80  LEU C CA  
4030 C C   . LEU C 80  ? 0.8887 0.5288 0.6285 -0.0875 -0.2868 0.0310  80  LEU C C   
4031 O O   . LEU C 80  ? 0.8483 0.4941 0.5896 -0.0879 -0.2854 0.0339  80  LEU C O   
4032 C CB  . LEU C 80  ? 0.9815 0.6190 0.7255 -0.0821 -0.2858 0.0275  80  LEU C CB  
4033 C CG  . LEU C 80  ? 0.9286 0.5693 0.6830 -0.0827 -0.2877 0.0282  80  LEU C CG  
4034 C CD1 . LEU C 80  ? 0.9664 0.6035 0.7197 -0.0825 -0.2897 0.0253  80  LEU C CD1 
4035 C CD2 . LEU C 80  ? 0.8473 0.4930 0.6104 -0.0807 -0.2865 0.0286  80  LEU C CD2 
4036 N N   . ARG C 81  ? 0.9321 0.5708 0.6743 -0.0893 -0.2890 0.0312  81  ARG C N   
4037 C CA  . ARG C 81  ? 0.9452 0.5889 0.6929 -0.0917 -0.2896 0.0353  81  ARG C CA  
4038 C C   . ARG C 81  ? 0.9726 0.6167 0.7312 -0.0920 -0.2911 0.0358  81  ARG C C   
4039 O O   . ARG C 81  ? 1.0009 0.6406 0.7586 -0.0922 -0.2931 0.0325  81  ARG C O   
4040 C CB  . ARG C 81  ? 0.9236 0.5659 0.6632 -0.0943 -0.2904 0.0352  81  ARG C CB  
4041 C CG  . ARG C 81  ? 1.0794 0.7289 0.8158 -0.0956 -0.2886 0.0385  81  ARG C CG  
4042 C CD  . ARG C 81  ? 1.0878 0.7382 0.8186 -0.0985 -0.2896 0.0389  81  ARG C CD  
4043 N NE  . ARG C 81  ? 1.0750 0.7253 0.8133 -0.0998 -0.2915 0.0418  81  ARG C NE  
4044 C CZ  . ARG C 81  ? 1.0713 0.7226 0.8069 -0.1023 -0.2926 0.0431  81  ARG C CZ  
4045 N NH1 . ARG C 81  ? 1.0797 0.7328 0.8050 -0.1039 -0.2920 0.0415  81  ARG C NH1 
4046 N NH2 . ARG C 81  ? 0.9402 0.5912 0.6841 -0.1034 -0.2941 0.0458  81  ARG C NH2 
4047 N N   . LEU C 82  ? 0.9313 0.5816 0.7012 -0.0922 -0.2899 0.0396  82  LEU C N   
4048 C CA  . LEU C 82  ? 0.9085 0.5606 0.6914 -0.0929 -0.2904 0.0396  82  LEU C CA  
4049 C C   . LEU C 82  ? 0.8788 0.5350 0.6690 -0.0953 -0.2897 0.0449  82  LEU C C   
4050 O O   . LEU C 82  ? 0.9211 0.5831 0.7164 -0.0949 -0.2873 0.0499  82  LEU C O   
4051 C CB  . LEU C 82  ? 0.8639 0.5197 0.6564 -0.0908 -0.2886 0.0388  82  LEU C CB  
4052 C CG  . LEU C 82  ? 0.8161 0.4733 0.6198 -0.0911 -0.2891 0.0353  82  LEU C CG  
4053 C CD1 . LEU C 82  ? 0.8165 0.4692 0.6127 -0.0910 -0.2920 0.0305  82  LEU C CD1 
4054 C CD2 . LEU C 82  ? 0.8140 0.4759 0.6264 -0.0890 -0.2869 0.0340  82  LEU C CD2 
4055 N N   . THR C 83  ? 0.8555 0.5092 0.6466 -0.0976 -0.2917 0.0443  83  THR C N   
4056 C CA  . THR C 83  ? 0.8828 0.5403 0.6817 -0.0999 -0.2910 0.0495  83  THR C CA  
4057 C C   . THR C 83  ? 0.9441 0.6054 0.7613 -0.1003 -0.2890 0.0507  83  THR C C   
4058 O O   . THR C 83  ? 0.9105 0.5712 0.7338 -0.0997 -0.2892 0.0458  83  THR C O   
4059 C CB  . THR C 83  ? 0.8273 0.4802 0.6198 -0.1024 -0.2937 0.0482  83  THR C CB  
4060 O OG1 . THR C 83  ? 0.9456 0.5959 0.7458 -0.1035 -0.2953 0.0443  83  THR C OG1 
4061 C CG2 . THR C 83  ? 0.8780 0.5255 0.6535 -0.1019 -0.2955 0.0445  83  THR C CG2 
4062 N N   . SER C 84  ? 0.9025 0.5691 0.7296 -0.1013 -0.2866 0.0573  84  SER C N   
4063 C CA  . SER C 84  ? 0.8786 0.5488 0.7252 -0.1023 -0.2838 0.0589  84  SER C CA  
4064 C C   . SER C 84  ? 0.8476 0.5204 0.7035 -0.1002 -0.2814 0.0561  84  SER C C   
4065 O O   . SER C 84  ? 0.8807 0.5541 0.7480 -0.1011 -0.2808 0.0515  84  SER C O   
4066 C CB  . SER C 84  ? 0.9033 0.5700 0.7544 -0.1051 -0.2860 0.0547  84  SER C CB  
4067 O OG  . SER C 84  ? 0.9717 0.6360 0.8148 -0.1070 -0.2880 0.0575  84  SER C OG  
4068 N N   . VAL C 85  ? 0.8127 0.4879 0.6638 -0.0977 -0.2800 0.0587  85  VAL C N   
4069 C CA  . VAL C 85  ? 0.8035 0.4811 0.6623 -0.0956 -0.2776 0.0563  85  VAL C CA  
4070 C C   . VAL C 85  ? 0.8419 0.5248 0.7223 -0.0962 -0.2732 0.0591  85  VAL C C   
4071 O O   . VAL C 85  ? 0.8605 0.5470 0.7489 -0.0969 -0.2707 0.0664  85  VAL C O   
4072 C CB  . VAL C 85  ? 0.8084 0.4877 0.6578 -0.0928 -0.2769 0.0589  85  VAL C CB  
4073 C CG1 . VAL C 85  ? 0.8785 0.5523 0.7083 -0.0924 -0.2805 0.0551  85  VAL C CG1 
4074 C CG2 . VAL C 85  ? 0.8835 0.5687 0.7360 -0.0927 -0.2744 0.0679  85  VAL C CG2 
4075 N N   . THR C 86  ? 0.8456 0.5297 0.7365 -0.0961 -0.2718 0.0532  86  THR C N   
4076 C CA  . THR C 86  ? 0.8136 0.5029 0.7266 -0.0967 -0.2667 0.0542  86  THR C CA  
4077 C C   . THR C 86  ? 0.8044 0.4968 0.7212 -0.0939 -0.2641 0.0527  86  THR C C   
4078 O O   . THR C 86  ? 0.8588 0.5491 0.7609 -0.0916 -0.2664 0.0514  86  THR C O   
4079 C CB  . THR C 86  ? 0.8151 0.5050 0.7400 -0.0996 -0.2667 0.0473  86  THR C CB  
4080 O OG1 . THR C 86  ? 0.8706 0.5613 0.7924 -0.0988 -0.2683 0.0387  86  THR C OG1 
4081 C CG2 . THR C 86  ? 0.8689 0.5544 0.7853 -0.1022 -0.2707 0.0472  86  THR C CG2 
4082 N N   . ALA C 87  ? 0.7857 0.4829 0.7230 -0.0941 -0.2589 0.0528  87  ALA C N   
4083 C CA  . ALA C 87  ? 0.7857 0.4860 0.7283 -0.0916 -0.2560 0.0509  87  ALA C CA  
4084 C C   . ALA C 87  ? 0.7853 0.4850 0.7204 -0.0911 -0.2587 0.0413  87  ALA C C   
4085 O O   . ALA C 87  ? 0.7892 0.4904 0.7222 -0.0885 -0.2578 0.0396  87  ALA C O   
4086 C CB  . ALA C 87  ? 0.7808 0.4865 0.7488 -0.0924 -0.2492 0.0519  87  ALA C CB  
4087 N N   . ALA C 88  ? 0.8261 0.5245 0.7576 -0.0932 -0.2620 0.0354  88  ALA C N   
4088 C CA  . ALA C 88  ? 0.8313 0.5308 0.7559 -0.0923 -0.2646 0.0271  88  ALA C CA  
4089 C C   . ALA C 88  ? 0.8300 0.5247 0.7333 -0.0893 -0.2682 0.0285  88  ALA C C   
4090 O O   . ALA C 88  ? 0.8212 0.5177 0.7204 -0.0871 -0.2684 0.0245  88  ALA C O   
4091 C CB  . ALA C 88  ? 0.8271 0.5271 0.7524 -0.0952 -0.2674 0.0214  88  ALA C CB  
4092 N N   . ASP C 89  ? 0.8635 0.5527 0.7538 -0.0893 -0.2707 0.0340  89  ASP C N   
4093 C CA  . ASP C 89  ? 0.7994 0.4840 0.6702 -0.0870 -0.2737 0.0347  89  ASP C CA  
4094 C C   . ASP C 89  ? 0.8025 0.4883 0.6715 -0.0843 -0.2714 0.0380  89  ASP C C   
4095 O O   . ASP C 89  ? 0.8073 0.4899 0.6618 -0.0823 -0.2733 0.0378  89  ASP C O   
4096 C CB  . ASP C 89  ? 0.8029 0.4824 0.6616 -0.0883 -0.2764 0.0387  89  ASP C CB  
4097 C CG  . ASP C 89  ? 0.7998 0.4777 0.6607 -0.0911 -0.2786 0.0361  89  ASP C CG  
4098 O OD1 . ASP C 89  ? 0.8007 0.4784 0.6594 -0.0911 -0.2807 0.0300  89  ASP C OD1 
4099 O OD2 . ASP C 89  ? 0.7988 0.4764 0.6640 -0.0933 -0.2782 0.0404  89  ASP C OD2 
4100 N N   . MET C 90  ? 0.8000 0.4903 0.6837 -0.0841 -0.2673 0.0412  90  MET C N   
4101 C CA  . MET C 90  ? 0.8025 0.4946 0.6856 -0.0815 -0.2651 0.0440  90  MET C CA  
4102 C C   . MET C 90  ? 0.8246 0.5169 0.7037 -0.0793 -0.2656 0.0375  90  MET C C   
4103 O O   . MET C 90  ? 0.8542 0.5507 0.7452 -0.0796 -0.2637 0.0323  90  MET C O   
4104 C CB  . MET C 90  ? 0.8337 0.5310 0.7359 -0.0815 -0.2599 0.0484  90  MET C CB  
4105 C CG  . MET C 90  ? 0.8866 0.5863 0.7900 -0.0787 -0.2574 0.0508  90  MET C CG  
4106 S SD  . MET C 90  ? 1.0221 0.7279 0.9480 -0.0784 -0.2508 0.0579  90  MET C SD  
4107 C CE  . MET C 90  ? 0.9818 0.6894 0.9051 -0.0748 -0.2491 0.0586  90  MET C CE  
4108 N N   . ALA C 91  ? 0.8080 0.4968 0.6711 -0.0773 -0.2678 0.0377  91  ALA C N   
4109 C CA  . ALA C 91  ? 0.8089 0.4976 0.6663 -0.0751 -0.2686 0.0322  91  ALA C CA  
4110 C C   . ALA C 91  ? 0.8191 0.5038 0.6611 -0.0731 -0.2698 0.0344  91  ALA C C   
4111 O O   . ALA C 91  ? 0.8184 0.5011 0.6540 -0.0737 -0.2703 0.0393  91  ALA C O   
4112 C CB  . ALA C 91  ? 0.8151 0.5032 0.6690 -0.0759 -0.2713 0.0265  91  ALA C CB  
4113 N N   . THR C 92  ? 0.8166 0.5010 0.6532 -0.0707 -0.2701 0.0305  92  THR C N   
4114 C CA  . THR C 92  ? 0.8225 0.5026 0.6446 -0.0688 -0.2711 0.0314  92  THR C CA  
4115 C C   . THR C 92  ? 0.8576 0.5331 0.6684 -0.0689 -0.2738 0.0289  92  THR C C   
4116 O O   . THR C 92  ? 0.8999 0.5771 0.7126 -0.0682 -0.2746 0.0248  92  THR C O   
4117 C CB  . THR C 92  ? 0.8229 0.5051 0.6457 -0.0660 -0.2695 0.0292  92  THR C CB  
4118 O OG1 . THR C 92  ? 0.8202 0.5068 0.6549 -0.0659 -0.2667 0.0314  92  THR C OG1 
4119 C CG2 . THR C 92  ? 0.8291 0.5067 0.6380 -0.0644 -0.2701 0.0303  92  THR C CG2 
4120 N N   . TYR C 93  ? 0.8299 0.5005 0.6295 -0.0696 -0.2749 0.0313  93  TYR C N   
4121 C CA  . TYR C 93  ? 0.8327 0.4983 0.6222 -0.0698 -0.2769 0.0294  93  TYR C CA  
4122 C C   . TYR C 93  ? 0.8755 0.5373 0.6543 -0.0675 -0.2763 0.0283  93  TYR C C   
4123 O O   . TYR C 93  ? 0.9044 0.5662 0.6804 -0.0669 -0.2749 0.0300  93  TYR C O   
4124 C CB  . TYR C 93  ? 0.8342 0.4972 0.6195 -0.0726 -0.2781 0.0320  93  TYR C CB  
4125 C CG  . TYR C 93  ? 0.8291 0.4944 0.6237 -0.0750 -0.2789 0.0326  93  TYR C CG  
4126 C CD1 . TYR C 93  ? 0.8251 0.4955 0.6321 -0.0759 -0.2773 0.0355  93  TYR C CD1 
4127 C CD2 . TYR C 93  ? 0.8282 0.4906 0.6200 -0.0762 -0.2811 0.0305  93  TYR C CD2 
4128 C CE1 . TYR C 93  ? 0.8205 0.4929 0.6372 -0.0782 -0.2775 0.0360  93  TYR C CE1 
4129 C CE2 . TYR C 93  ? 0.8234 0.4879 0.6240 -0.0786 -0.2819 0.0308  93  TYR C CE2 
4130 C CZ  . TYR C 93  ? 0.8196 0.4890 0.6328 -0.0797 -0.2800 0.0335  93  TYR C CZ  
4131 O OH  . TYR C 93  ? 0.8149 0.4862 0.6380 -0.0822 -0.2802 0.0338  93  TYR C OH  
4132 N N   . TYR C 94  ? 0.9355 0.5945 0.7092 -0.0661 -0.2771 0.0256  94  TYR C N   
4133 C CA  . TYR C 94  ? 0.9258 0.5809 0.6907 -0.0637 -0.2759 0.0248  94  TYR C CA  
4134 C C   . TYR C 94  ? 0.9305 0.5799 0.6876 -0.0642 -0.2766 0.0240  94  TYR C C   
4135 O O   . TYR C 94  ? 0.9116 0.5615 0.6709 -0.0650 -0.2784 0.0231  94  TYR C O   
4136 C CB  . TYR C 94  ? 0.9089 0.5677 0.6769 -0.0603 -0.2751 0.0228  94  TYR C CB  
4137 C CG  . TYR C 94  ? 0.9037 0.5683 0.6801 -0.0596 -0.2741 0.0225  94  TYR C CG  
4138 C CD1 . TYR C 94  ? 0.9647 0.6288 0.7390 -0.0584 -0.2724 0.0236  94  TYR C CD1 
4139 C CD2 . TYR C 94  ? 0.8748 0.5460 0.6622 -0.0603 -0.2745 0.0208  94  TYR C CD2 
4140 C CE1 . TYR C 94  ? 0.9905 0.6597 0.7727 -0.0576 -0.2713 0.0233  94  TYR C CE1 
4141 C CE2 . TYR C 94  ? 0.8674 0.5441 0.6636 -0.0597 -0.2730 0.0201  94  TYR C CE2 
4142 C CZ  . TYR C 94  ? 0.9193 0.5946 0.7126 -0.0582 -0.2714 0.0215  94  TYR C CZ  
4143 O OH  . TYR C 94  ? 0.8730 0.5536 0.6754 -0.0575 -0.2696 0.0207  94  TYR C OH  
4144 N N   . CYS C 95  ? 0.9478 0.5922 0.6966 -0.0637 -0.2750 0.0240  95  CYS C N   
4145 C CA  . CYS C 95  ? 0.9056 0.5443 0.6479 -0.0632 -0.2745 0.0228  95  CYS C CA  
4146 C C   . CYS C 95  ? 0.9110 0.5488 0.6517 -0.0593 -0.2723 0.0223  95  CYS C C   
4147 O O   . CYS C 95  ? 0.9409 0.5801 0.6820 -0.0578 -0.2707 0.0225  95  CYS C O   
4148 C CB  . CYS C 95  ? 0.9293 0.5634 0.6646 -0.0658 -0.2733 0.0225  95  CYS C CB  
4149 S SG  . CYS C 95  ? 1.1941 0.8291 0.9264 -0.0664 -0.2708 0.0227  95  CYS C SG  
4150 N N   . ALA C 96  ? 0.9267 0.5628 0.6662 -0.0574 -0.2722 0.0219  96  ALA C N   
4151 C CA  . ALA C 96  ? 0.9714 0.6083 0.7107 -0.0531 -0.2700 0.0224  96  ALA C CA  
4152 C C   . ALA C 96  ? 0.9663 0.5973 0.7012 -0.0518 -0.2680 0.0227  96  ALA C C   
4153 O O   . ALA C 96  ? 0.9281 0.5558 0.6611 -0.0538 -0.2691 0.0221  96  ALA C O   
4154 C CB  . ALA C 96  ? 0.9661 0.6118 0.7120 -0.0509 -0.2717 0.0223  96  ALA C CB  
4155 N N   . ARG C 97  ? 0.9523 0.5822 0.6863 -0.0482 -0.2645 0.0238  97  ARG C N   
4156 C CA  . ARG C 97  ? 1.0601 0.6846 0.7917 -0.0460 -0.2613 0.0248  97  ARG C CA  
4157 C C   . ARG C 97  ? 1.0332 0.6641 0.7684 -0.0417 -0.2616 0.0272  97  ARG C C   
4158 O O   . ARG C 97  ? 0.9856 0.6221 0.7233 -0.0383 -0.2605 0.0286  97  ARG C O   
4159 C CB  . ARG C 97  ? 1.0980 0.7173 0.8274 -0.0449 -0.2565 0.0248  97  ARG C CB  
4160 C CG  . ARG C 97  ? 1.0503 0.6630 0.7786 -0.0431 -0.2520 0.0255  97  ARG C CG  
4161 C CD  . ARG C 97  ? 1.0505 0.6579 0.7779 -0.0428 -0.2467 0.0247  97  ARG C CD  
4162 N NE  . ARG C 97  ? 0.9943 0.6057 0.7244 -0.0385 -0.2449 0.0275  97  ARG C NE  
4163 C CZ  . ARG C 97  ? 1.0522 0.6600 0.7833 -0.0366 -0.2396 0.0281  97  ARG C CZ  
4164 N NH1 . ARG C 97  ? 1.1126 0.7126 0.8428 -0.0386 -0.2351 0.0258  97  ARG C NH1 
4165 N NH2 . ARG C 97  ? 1.0724 0.6847 0.8056 -0.0327 -0.2386 0.0308  97  ARG C NH2 
4166 N N   . TRP C 98  ? 1.1047 0.7356 0.8402 -0.0416 -0.2629 0.0276  98  TRP C N   
4167 C CA  . TRP C 98  ? 1.1130 0.7509 0.8518 -0.0372 -0.2626 0.0304  98  TRP C CA  
4168 C C   . TRP C 98  ? 1.1291 0.7625 0.8671 -0.0332 -0.2571 0.0335  98  TRP C C   
4169 O O   . TRP C 98  ? 1.1560 0.7794 0.8911 -0.0346 -0.2540 0.0327  98  TRP C O   
4170 C CB  . TRP C 98  ? 1.1151 0.7546 0.8546 -0.0385 -0.2658 0.0299  98  TRP C CB  
4171 C CG  . TRP C 98  ? 1.1498 0.7996 0.8940 -0.0399 -0.2704 0.0283  98  TRP C CG  
4172 C CD1 . TRP C 98  ? 1.1663 0.8154 0.9111 -0.0444 -0.2741 0.0256  98  TRP C CD1 
4173 C CD2 . TRP C 98  ? 1.1320 0.7951 0.8815 -0.0369 -0.2713 0.0289  98  TRP C CD2 
4174 N NE1 . TRP C 98  ? 1.1808 0.8413 0.9320 -0.0446 -0.2770 0.0242  98  TRP C NE1 
4175 C CE2 . TRP C 98  ? 1.1276 0.7973 0.8815 -0.0402 -0.2754 0.0257  98  TRP C CE2 
4176 C CE3 . TRP C 98  ? 1.0825 0.7534 0.8340 -0.0318 -0.2686 0.0317  98  TRP C CE3 
4177 C CZ2 . TRP C 98  ? 1.1063 0.7904 0.8669 -0.0389 -0.2768 0.0244  98  TRP C CZ2 
4178 C CZ3 . TRP C 98  ? 1.1098 0.7957 0.8670 -0.0303 -0.2704 0.0308  98  TRP C CZ3 
4179 C CH2 . TRP C 98  ? 1.1673 0.8598 0.9291 -0.0340 -0.2744 0.0267  98  TRP C CH2 
4180 N N   . ARG C 99  ? 1.0639 0.7054 0.8054 -0.0281 -0.2555 0.0369  99  ARG C N   
4181 C CA  . ARG C 99  ? 0.9257 0.5644 0.6681 -0.0235 -0.2498 0.0412  99  ARG C CA  
4182 C C   . ARG C 99  ? 0.9148 0.5606 0.6603 -0.0200 -0.2502 0.0448  99  ARG C C   
4183 O O   . ARG C 99  ? 1.0227 0.6812 0.7710 -0.0187 -0.2537 0.0452  99  ARG C O   
4184 C CB  . ARG C 99  ? 0.9200 0.5631 0.6643 -0.0199 -0.2468 0.0435  99  ARG C CB  
4185 C CG  . ARG C 99  ? 0.9497 0.5823 0.6914 -0.0218 -0.2432 0.0416  99  ARG C CG  
4186 C CD  . ARG C 99  ? 1.0000 0.6242 0.7430 -0.0195 -0.2364 0.0442  99  ARG C CD  
4187 N NE  . ARG C 99  ? 1.0167 0.6446 0.7633 -0.0141 -0.2317 0.0488  99  ARG C NE  
4188 C CZ  . ARG C 99  ? 1.0079 0.6316 0.7543 -0.0142 -0.2283 0.0481  99  ARG C CZ  
4189 N NH1 . ARG C 99  ? 1.0379 0.6546 0.7807 -0.0193 -0.2292 0.0429  99  ARG C NH1 
4190 N NH2 . ARG C 99  ? 1.0132 0.6408 0.7632 -0.0090 -0.2239 0.0530  99  ARG C NH2 
4191 N N   . LEU C 100 ? 0.9493 0.5878 0.6949 -0.0184 -0.2462 0.0472  100 LEU C N   
4192 C CA  . LEU C 100 ? 0.9359 0.5792 0.6837 -0.0161 -0.2470 0.0500  100 LEU C CA  
4193 C C   . LEU C 100 ? 0.9790 0.6228 0.7310 -0.0099 -0.2405 0.0566  100 LEU C C   
4194 O O   . LEU C 100 ? 0.9772 0.6123 0.7298 -0.0087 -0.2347 0.0577  100 LEU C O   
4195 C CB  . LEU C 100 ? 0.9353 0.5688 0.6797 -0.0208 -0.2491 0.0464  100 LEU C CB  
4196 C CG  . LEU C 100 ? 0.9999 0.6377 0.7426 -0.0255 -0.2562 0.0420  100 LEU C CG  
4197 C CD1 . LEU C 100 ? 1.0196 0.6517 0.7590 -0.0303 -0.2576 0.0375  100 LEU C CD1 
4198 C CD2 . LEU C 100 ? 1.0411 0.6743 0.7822 -0.0278 -0.2583 0.0408  100 LEU C CD2 
4199 N N   . MET C 101 ? 0.9585 0.6131 0.7139 -0.0059 -0.2414 0.0610  101 MET C N   
4200 C CA  . MET C 101 ? 0.9082 0.5657 0.6687 0.0006  -0.2353 0.0685  101 MET C CA  
4201 C C   . MET C 101 ? 0.9168 0.5795 0.6791 0.0021  -0.2371 0.0709  101 MET C C   
4202 O O   . MET C 101 ? 0.9745 0.6478 0.7362 0.0004  -0.2434 0.0688  101 MET C O   
4203 C CB  . MET C 101 ? 0.8893 0.5613 0.6538 0.0062  -0.2336 0.0736  101 MET C CB  
4204 C CG  . MET C 101 ? 0.9085 0.5844 0.6792 0.0135  -0.2265 0.0827  101 MET C CG  
4205 S SD  . MET C 101 ? 0.9759 0.6371 0.7488 0.0151  -0.2175 0.0847  101 MET C SD  
4206 C CE  . MET C 101 ? 0.8974 0.5644 0.6673 0.0137  -0.2202 0.0814  101 MET C CE  
4207 N N   . MET C 102 ? 0.9455 0.6009 0.7108 0.0051  -0.2315 0.0752  102 MET C N   
4208 C CA  . MET C 102 ? 1.0385 0.6984 0.8060 0.0071  -0.2324 0.0784  102 MET C CA  
4209 C C   . MET C 102 ? 1.0777 0.7490 0.8526 0.0154  -0.2270 0.0883  102 MET C C   
4210 O O   . MET C 102 ? 1.0870 0.7510 0.8663 0.0190  -0.2191 0.0928  102 MET C O   
4211 C CB  . MET C 102 ? 0.9818 0.6247 0.7475 0.0040  -0.2301 0.0755  102 MET C CB  
4212 C CG  . MET C 102 ? 1.0561 0.6956 0.8160 -0.0024 -0.2374 0.0686  102 MET C CG  
4213 S SD  . MET C 102 ? 1.3882 1.0407 1.1510 0.0007  -0.2410 0.0729  102 MET C SD  
4214 C CE  . MET C 102 ? 1.1165 0.7599 0.8847 0.0059  -0.2321 0.0793  102 MET C CE  
4215 N N   . VAL C 103 ? 1.1934 0.8834 0.9706 0.0183  -0.2308 0.0917  103 VAL C N   
4216 C CA  . VAL C 103 ? 1.2046 0.9088 0.9891 0.0265  -0.2262 0.1019  103 VAL C CA  
4217 C C   . VAL C 103 ? 1.2706 0.9803 1.0569 0.0277  -0.2283 0.1044  103 VAL C C   
4218 O O   . VAL C 103 ? 1.4479 1.1505 1.2383 0.0312  -0.2226 0.1097  103 VAL C O   
4219 C CB  . VAL C 103 ? 1.1770 0.9021 0.9634 0.0299  -0.2280 0.1045  103 VAL C CB  
4220 C CG1 . VAL C 103 ? 1.2093 0.9460 0.9920 0.0249  -0.2370 0.0972  103 VAL C CG1 
4221 C CG2 . VAL C 103 ? 1.2054 0.9483 0.9994 0.0385  -0.2236 0.1156  103 VAL C CG2 
4222 N N   . ASP C 104 ? 1.1601 0.8825 0.9440 0.0248  -0.2361 0.1003  104 ASP C N   
4223 C CA  . ASP C 104 ? 1.2385 0.9646 1.0226 0.0240  -0.2399 0.1001  104 ASP C CA  
4224 C C   . ASP C 104 ? 1.2931 1.0098 1.0706 0.0155  -0.2471 0.0898  104 ASP C C   
4225 O O   . ASP C 104 ? 1.2962 1.0031 1.0717 0.0130  -0.2483 0.0880  104 ASP C O   
4226 C CB  . ASP C 104 ? 1.3008 1.0542 1.0898 0.0285  -0.2425 0.1051  104 ASP C CB  
4227 C CG  . ASP C 104 ? 1.3953 1.1540 1.1853 0.0284  -0.2457 0.1060  104 ASP C CG  
4228 O OD1 . ASP C 104 ? 1.3888 1.1302 1.1774 0.0272  -0.2437 0.1059  104 ASP C OD1 
4229 O OD2 . ASP C 104 ? 1.3619 1.1428 1.1545 0.0293  -0.2502 0.1064  104 ASP C OD2 
4230 N N   . GLU C 105 ? 1.2513 0.9710 1.0258 0.0111  -0.2515 0.0834  105 GLU C N   
4231 C CA  . GLU C 105 ? 1.0867 0.7960 0.8555 0.0031  -0.2572 0.0742  105 GLU C CA  
4232 C C   . GLU C 105 ? 1.0193 0.7190 0.7851 0.0003  -0.2559 0.0703  105 GLU C C   
4233 O O   . GLU C 105 ? 1.0128 0.7161 0.7807 0.0044  -0.2516 0.0742  105 GLU C O   
4234 C CB  . GLU C 105 ? 1.1281 0.8540 0.8983 0.0001  -0.2644 0.0698  105 GLU C CB  
4235 C CG  . GLU C 105 ? 1.1737 0.9201 0.9480 0.0027  -0.2650 0.0707  105 GLU C CG  
4236 C CD  . GLU C 105 ? 1.2559 1.0180 1.0325 -0.0013 -0.2716 0.0646  105 GLU C CD  
4237 O OE1 . GLU C 105 ? 1.3388 1.0980 1.1146 -0.0051 -0.2756 0.0612  105 GLU C OE1 
4238 O OE2 . GLU C 105 ? 1.2868 1.0644 1.0667 -0.0008 -0.2726 0.0628  105 GLU C OE2 
4239 N N   . VAL C 106 ? 1.0264 0.7144 0.7872 -0.0065 -0.2596 0.0630  106 VAL C N   
4240 C CA  . VAL C 106 ? 0.9899 0.6692 0.7476 -0.0095 -0.2588 0.0592  106 VAL C CA  
4241 C C   . VAL C 106 ? 0.9670 0.6618 0.7276 -0.0084 -0.2608 0.0586  106 VAL C C   
4242 O O   . VAL C 106 ? 1.0741 0.7820 0.8369 -0.0102 -0.2658 0.0557  106 VAL C O   
4243 C CB  . VAL C 106 ? 0.9375 0.6039 0.6900 -0.0168 -0.2626 0.0522  106 VAL C CB  
4244 C CG1 . VAL C 106 ? 0.9252 0.5831 0.6749 -0.0194 -0.2612 0.0491  106 VAL C CG1 
4245 C CG2 . VAL C 106 ? 0.9324 0.5852 0.6823 -0.0178 -0.2607 0.0523  106 VAL C CG2 
4246 N N   . THR C 107 ? 0.8799 0.5735 0.6408 -0.0057 -0.2566 0.0608  107 THR C N   
4247 C CA  . THR C 107 ? 0.9047 0.6120 0.6680 -0.0044 -0.2576 0.0603  107 THR C CA  
4248 C C   . THR C 107 ? 0.9183 0.6146 0.6782 -0.0078 -0.2571 0.0562  107 THR C C   
4249 O O   . THR C 107 ? 0.9956 0.6783 0.7532 -0.0074 -0.2526 0.0576  107 THR C O   
4250 C CB  . THR C 107 ? 0.9626 0.6821 0.7303 0.0032  -0.2529 0.0680  107 THR C CB  
4251 O OG1 . THR C 107 ? 0.9860 0.7158 0.7571 0.0068  -0.2529 0.0727  107 THR C OG1 
4252 C CG2 . THR C 107 ? 0.9882 0.7245 0.7584 0.0045  -0.2544 0.0669  107 THR C CG2 
4253 N N   . ARG C 108 ? 0.8642 0.5669 0.6246 -0.0113 -0.2613 0.0511  108 ARG C N   
4254 C CA  . ARG C 108 ? 0.8843 0.5777 0.6418 -0.0151 -0.2616 0.0470  108 ARG C CA  
4255 C C   . ARG C 108 ? 0.8581 0.5591 0.6174 -0.0117 -0.2592 0.0486  108 ARG C C   
4256 O O   . ARG C 108 ? 0.8865 0.6044 0.6499 -0.0087 -0.2599 0.0497  108 ARG C O   
4257 C CB  . ARG C 108 ? 1.0127 0.7077 0.7708 -0.0210 -0.2672 0.0406  108 ARG C CB  
4258 C CG  . ARG C 108 ? 1.0343 0.7194 0.7897 -0.0251 -0.2696 0.0386  108 ARG C CG  
4259 C CD  . ARG C 108 ? 0.9933 0.6825 0.7511 -0.0304 -0.2747 0.0332  108 ARG C CD  
4260 N NE  . ARG C 108 ? 1.0337 0.7125 0.7885 -0.0346 -0.2770 0.0313  108 ARG C NE  
4261 C CZ  . ARG C 108 ? 1.0233 0.7049 0.7790 -0.0349 -0.2791 0.0315  108 ARG C CZ  
4262 N NH1 . ARG C 108 ? 0.9306 0.6259 0.6903 -0.0313 -0.2794 0.0336  108 ARG C NH1 
4263 N NH2 . ARG C 108 ? 0.9884 0.6595 0.7407 -0.0389 -0.2811 0.0296  108 ARG C NH2 
4264 N N   . HIS C 109 ? 0.8634 0.5527 0.6196 -0.0124 -0.2562 0.0484  109 HIS C N   
4265 C CA  . HIS C 109 ? 0.8647 0.5585 0.6217 -0.0095 -0.2536 0.0497  109 HIS C CA  
4266 C C   . HIS C 109 ? 0.8626 0.5536 0.6182 -0.0138 -0.2562 0.0443  109 HIS C C   
4267 O O   . HIS C 109 ? 0.8647 0.5554 0.6199 -0.0123 -0.2539 0.0449  109 HIS C O   
4268 C CB  . HIS C 109 ? 0.9681 0.6518 0.7238 -0.0062 -0.2474 0.0543  109 HIS C CB  
4269 C CG  . HIS C 109 ? 0.9527 0.6431 0.7120 0.0000  -0.2434 0.0613  109 HIS C CG  
4270 N ND1 . HIS C 109 ? 0.9329 0.6330 0.6946 0.0015  -0.2456 0.0632  109 HIS C ND1 
4271 C CD2 . HIS C 109 ? 0.8820 0.5718 0.6436 0.0053  -0.2372 0.0675  109 HIS C CD2 
4272 C CE1 . HIS C 109 ? 0.9208 0.6264 0.6861 0.0076  -0.2409 0.0705  109 HIS C CE1 
4273 N NE2 . HIS C 109 ? 0.9267 0.6259 0.6923 0.0101  -0.2356 0.0734  109 HIS C NE2 
4274 N N   . GLY C 110 ? 0.8767 0.5660 0.6322 -0.0189 -0.2606 0.0396  110 GLY C N   
4275 C CA  . GLY C 110 ? 0.9304 0.6188 0.6863 -0.0227 -0.2628 0.0351  110 GLY C CA  
4276 C C   . GLY C 110 ? 0.9368 0.6097 0.6879 -0.0266 -0.2622 0.0336  110 GLY C C   
4277 O O   . GLY C 110 ? 1.0233 0.6858 0.7707 -0.0263 -0.2594 0.0354  110 GLY C O   
4278 N N   . MET C 111 ? 0.9307 0.6032 0.6828 -0.0304 -0.2646 0.0300  111 MET C N   
4279 C CA  . MET C 111 ? 0.9957 0.6567 0.7439 -0.0343 -0.2646 0.0284  111 MET C CA  
4280 C C   . MET C 111 ? 0.9817 0.6409 0.7286 -0.0330 -0.2620 0.0287  111 MET C C   
4281 O O   . MET C 111 ? 0.9513 0.6160 0.7012 -0.0336 -0.2632 0.0270  111 MET C O   
4282 C CB  . MET C 111 ? 0.9575 0.6200 0.7084 -0.0390 -0.2684 0.0252  111 MET C CB  
4283 C CG  . MET C 111 ? 0.9857 0.6489 0.7377 -0.0409 -0.2711 0.0246  111 MET C CG  
4284 S SD  . MET C 111 ? 1.0872 0.7540 0.8449 -0.0459 -0.2751 0.0212  111 MET C SD  
4285 C CE  . MET C 111 ? 0.9733 0.6565 0.7397 -0.0439 -0.2762 0.0193  111 MET C CE  
4286 N N   . ASP C 112 ? 1.0122 0.6637 0.7554 -0.0314 -0.2581 0.0307  112 ASP C N   
4287 C CA  . ASP C 112 ? 1.0369 0.6868 0.7790 -0.0298 -0.2553 0.0312  112 ASP C CA  
4288 C C   . ASP C 112 ? 1.0239 0.6678 0.7635 -0.0340 -0.2560 0.0286  112 ASP C C   
4289 O O   . ASP C 112 ? 1.0310 0.6768 0.7711 -0.0336 -0.2556 0.0281  112 ASP C O   
4290 C CB  . ASP C 112 ? 1.0912 0.7356 0.8317 -0.0265 -0.2501 0.0343  112 ASP C CB  
4291 C CG  . ASP C 112 ? 1.0950 0.7302 0.8332 -0.0284 -0.2485 0.0341  112 ASP C CG  
4292 O OD1 . ASP C 112 ? 1.1552 0.7878 0.8918 -0.0326 -0.2516 0.0315  112 ASP C OD1 
4293 O OD2 . ASP C 112 ? 1.0063 0.6371 0.7448 -0.0256 -0.2437 0.0366  112 ASP C OD2 
4294 N N   . VAL C 113 ? 1.0013 0.6389 0.7384 -0.0380 -0.2569 0.0271  113 VAL C N   
4295 C CA  . VAL C 113 ? 1.0034 0.6370 0.7382 -0.0419 -0.2574 0.0251  113 VAL C CA  
4296 C C   . VAL C 113 ? 0.9708 0.6076 0.7076 -0.0454 -0.2616 0.0239  113 VAL C C   
4297 O O   . VAL C 113 ? 0.9713 0.6072 0.7081 -0.0467 -0.2632 0.0238  113 VAL C O   
4298 C CB  . VAL C 113 ? 1.0452 0.6701 0.7756 -0.0439 -0.2542 0.0241  113 VAL C CB  
4299 C CG1 . VAL C 113 ? 1.0551 0.6785 0.7832 -0.0476 -0.2543 0.0221  113 VAL C CG1 
4300 C CG2 . VAL C 113 ? 1.0646 0.6861 0.7949 -0.0402 -0.2493 0.0256  113 VAL C CG2 
4301 N N   . TRP C 114 ? 0.8875 0.5278 0.6266 -0.0468 -0.2630 0.0234  114 TRP C N   
4302 C CA  . TRP C 114 ? 0.9497 0.5936 0.6927 -0.0498 -0.2661 0.0229  114 TRP C CA  
4303 C C   . TRP C 114 ? 1.0141 0.6559 0.7551 -0.0530 -0.2660 0.0229  114 TRP C C   
4304 O O   . TRP C 114 ? 1.0120 0.6527 0.7509 -0.0524 -0.2640 0.0229  114 TRP C O   
4305 C CB  . TRP C 114 ? 1.0116 0.6637 0.7617 -0.0484 -0.2675 0.0224  114 TRP C CB  
4306 C CG  . TRP C 114 ? 0.9353 0.5929 0.6887 -0.0459 -0.2682 0.0219  114 TRP C CG  
4307 C CD1 . TRP C 114 ? 0.9538 0.6136 0.7059 -0.0419 -0.2664 0.0227  114 TRP C CD1 
4308 C CD2 . TRP C 114 ? 0.9598 0.6229 0.7188 -0.0473 -0.2707 0.0207  114 TRP C CD2 
4309 N NE1 . TRP C 114 ? 0.9798 0.6472 0.7361 -0.0406 -0.2679 0.0222  114 TRP C NE1 
4310 C CE2 . TRP C 114 ? 0.9917 0.6611 0.7524 -0.0441 -0.2706 0.0205  114 TRP C CE2 
4311 C CE3 . TRP C 114 ? 0.9852 0.6492 0.7488 -0.0510 -0.2729 0.0199  114 TRP C CE3 
4312 C CZ2 . TRP C 114 ? 0.9932 0.6701 0.7596 -0.0448 -0.2727 0.0188  114 TRP C CZ2 
4313 C CZ3 . TRP C 114 ? 0.9770 0.6472 0.7466 -0.0517 -0.2748 0.0182  114 TRP C CZ3 
4314 C CH2 . TRP C 114 ? 0.9977 0.6745 0.7685 -0.0487 -0.2748 0.0173  114 TRP C CH2 
4315 N N   . SER C 115 ? 1.0538 0.6961 0.7958 -0.0563 -0.2680 0.0232  115 SER C N   
4316 C CA  . SER C 115 ? 1.0570 0.7005 0.7986 -0.0591 -0.2680 0.0241  115 SER C CA  
4317 C C   . SER C 115 ? 1.1453 0.7943 0.8932 -0.0581 -0.2683 0.0251  115 SER C C   
4318 O O   . SER C 115 ? 1.2315 0.8841 0.9854 -0.0563 -0.2690 0.0246  115 SER C O   
4319 C CB  . SER C 115 ? 1.0080 0.6522 0.7503 -0.0625 -0.2699 0.0249  115 SER C CB  
4320 O OG  . SER C 115 ? 1.0153 0.6648 0.7658 -0.0630 -0.2717 0.0263  115 SER C OG  
4321 N N   . GLN C 116 ? 1.3130 0.9634 1.0600 -0.0593 -0.2675 0.0262  116 GLN C N   
4322 C CA  . GLN C 116 ? 1.3258 0.9813 1.0793 -0.0585 -0.2674 0.0275  116 GLN C CA  
4323 C C   . GLN C 116 ? 1.3095 0.9695 1.0719 -0.0596 -0.2689 0.0289  116 GLN C C   
4324 O O   . GLN C 116 ? 1.3089 0.9730 1.0792 -0.0583 -0.2685 0.0289  116 GLN C O   
4325 C CB  . GLN C 116 ? 1.3767 1.0339 1.1276 -0.0598 -0.2663 0.0290  116 GLN C CB  
4326 C CG  . GLN C 116 ? 1.4070 1.0666 1.1564 -0.0632 -0.2670 0.0310  116 GLN C CG  
4327 C CD  . GLN C 116 ? 1.4679 1.1235 1.2088 -0.0650 -0.2662 0.0288  116 GLN C CD  
4328 O OE1 . GLN C 116 ? 1.4464 1.0974 1.1849 -0.0649 -0.2666 0.0271  116 GLN C OE1 
4329 N NE2 . GLN C 116 ? 1.5001 1.1581 1.2367 -0.0667 -0.2649 0.0286  116 GLN C NE2 
4330 N N   . GLY C 117 ? 1.1179 0.7774 0.8800 -0.0621 -0.2702 0.0299  117 GLY C N   
4331 C CA  . GLY C 117 ? 1.0351 0.6983 0.8064 -0.0634 -0.2713 0.0311  117 GLY C CA  
4332 C C   . GLY C 117 ? 1.0656 0.7332 0.8417 -0.0653 -0.2708 0.0352  117 GLY C C   
4333 O O   . GLY C 117 ? 1.0739 0.7446 0.8528 -0.0644 -0.2695 0.0370  117 GLY C O   
4334 N N   . THR C 118 ? 1.0294 0.6977 0.8069 -0.0677 -0.2719 0.0371  118 THR C N   
4335 C CA  . THR C 118 ? 0.9317 0.6053 0.7148 -0.0694 -0.2713 0.0420  118 THR C CA  
4336 C C   . THR C 118 ? 0.8812 0.5577 0.6773 -0.0699 -0.2711 0.0433  118 THR C C   
4337 O O   . THR C 118 ? 0.8742 0.5483 0.6714 -0.0709 -0.2725 0.0409  118 THR C O   
4338 C CB  . THR C 118 ? 0.8926 0.5664 0.6679 -0.0719 -0.2721 0.0437  118 THR C CB  
4339 O OG1 . THR C 118 ? 0.8752 0.5441 0.6471 -0.0730 -0.2738 0.0411  118 THR C OG1 
4340 C CG2 . THR C 118 ? 0.8692 0.5420 0.6339 -0.0718 -0.2714 0.0422  118 THR C CG2 
4341 N N   . MET C 119 ? 0.8712 0.5531 0.6778 -0.0694 -0.2690 0.0469  119 MET C N   
4342 C CA  . MET C 119 ? 0.8616 0.5468 0.6826 -0.0703 -0.2678 0.0484  119 MET C CA  
4343 C C   . MET C 119 ? 0.8280 0.5148 0.6500 -0.0727 -0.2684 0.0529  119 MET C C   
4344 O O   . MET C 119 ? 0.8311 0.5206 0.6472 -0.0733 -0.2684 0.0572  119 MET C O   
4345 C CB  . MET C 119 ? 0.9415 0.6318 0.7747 -0.0688 -0.2646 0.0512  119 MET C CB  
4346 C CG  . MET C 119 ? 0.9984 0.6878 0.8281 -0.0662 -0.2640 0.0481  119 MET C CG  
4347 S SD  . MET C 119 ? 1.1780 0.8729 1.0244 -0.0645 -0.2600 0.0500  119 MET C SD  
4348 C CE  . MET C 119 ? 1.0887 0.7815 0.9261 -0.0618 -0.2602 0.0463  119 MET C CE  
4349 N N   . VAL C 120 ? 0.8240 0.5103 0.6539 -0.0743 -0.2687 0.0518  120 VAL C N   
4350 C CA  . VAL C 120 ? 0.8229 0.5107 0.6554 -0.0766 -0.2690 0.0560  120 VAL C CA  
4351 C C   . VAL C 120 ? 0.8771 0.5691 0.7284 -0.0771 -0.2660 0.0586  120 VAL C C   
4352 O O   . VAL C 120 ? 0.9178 0.6090 0.7777 -0.0774 -0.2656 0.0537  120 VAL C O   
4353 C CB  . VAL C 120 ? 0.8236 0.5058 0.6476 -0.0784 -0.2722 0.0521  120 VAL C CB  
4354 C CG1 . VAL C 120 ? 0.8208 0.5047 0.6515 -0.0809 -0.2723 0.0556  120 VAL C CG1 
4355 C CG2 . VAL C 120 ? 0.8295 0.5081 0.6365 -0.0783 -0.2742 0.0508  120 VAL C CG2 
4356 N N   . THR C 121 ? 0.8346 0.5323 0.6931 -0.0771 -0.2636 0.0661  121 THR C N   
4357 C CA  . THR C 121 ? 0.8392 0.5414 0.7175 -0.0774 -0.2596 0.0698  121 THR C CA  
4358 C C   . THR C 121 ? 0.8614 0.5648 0.7435 -0.0797 -0.2598 0.0743  121 THR C C   
4359 O O   . THR C 121 ? 0.9148 0.6213 0.7894 -0.0801 -0.2606 0.0800  121 THR C O   
4360 C CB  . THR C 121 ? 0.8546 0.5631 0.7406 -0.0751 -0.2560 0.0762  121 THR C CB  
4361 O OG1 . THR C 121 ? 0.9118 0.6186 0.7942 -0.0730 -0.2559 0.0717  121 THR C OG1 
4362 C CG2 . THR C 121 ? 0.8948 0.6078 0.8030 -0.0752 -0.2509 0.0805  121 THR C CG2 
4363 N N   . VAL C 122 ? 0.8297 0.5317 0.7237 -0.0815 -0.2588 0.0714  122 VAL C N   
4364 C CA  . VAL C 122 ? 0.8278 0.5310 0.7285 -0.0838 -0.2583 0.0756  122 VAL C CA  
4365 C C   . VAL C 122 ? 0.8731 0.5822 0.7959 -0.0834 -0.2524 0.0816  122 VAL C C   
4366 O O   . VAL C 122 ? 0.8681 0.5774 0.8061 -0.0836 -0.2493 0.0774  122 VAL C O   
4367 C CB  . VAL C 122 ? 0.8146 0.5126 0.7147 -0.0864 -0.2610 0.0684  122 VAL C CB  
4368 C CG1 . VAL C 122 ? 0.8348 0.5343 0.7457 -0.0889 -0.2596 0.0727  122 VAL C CG1 
4369 C CG2 . VAL C 122 ? 0.8374 0.5297 0.7162 -0.0866 -0.2663 0.0640  122 VAL C CG2 
4370 N N   . SER C 123 ? 0.9030 0.6179 0.8284 -0.0827 -0.2504 0.0916  123 SER C N   
4371 C CA  . SER C 123 ? 0.8420 0.5633 0.7890 -0.0818 -0.2442 0.0993  123 SER C CA  
4372 C C   . SER C 123 ? 0.9476 0.6755 0.8934 -0.0816 -0.2435 0.1102  123 SER C C   
4373 O O   . SER C 123 ? 0.9484 0.6769 0.8760 -0.0819 -0.2476 0.1113  123 SER C O   
4374 C CB  . SER C 123 ? 0.8205 0.5451 0.7745 -0.0788 -0.2407 0.1005  123 SER C CB  
4375 O OG  . SER C 123 ? 0.9081 0.6409 0.8769 -0.0770 -0.2353 0.1115  123 SER C OG  
4376 N N   . SER C 124 ? 0.9345 0.6680 0.9007 -0.0812 -0.2377 0.1182  124 SER C N   
4377 C CA  . SER C 124 ? 0.9047 0.6468 0.8732 -0.0805 -0.2359 0.1302  124 SER C CA  
4378 C C   . SER C 124 ? 0.9230 0.6751 0.8963 -0.0768 -0.2322 0.1397  124 SER C C   
4379 O O   . SER C 124 ? 0.9599 0.7217 0.9346 -0.0757 -0.2305 0.1506  124 SER C O   
4380 C CB  . SER C 124 ? 0.8615 0.6045 0.8504 -0.0821 -0.2314 0.1346  124 SER C CB  
4381 O OG  . SER C 124 ? 0.8665 0.6105 0.8789 -0.0810 -0.2247 0.1354  124 SER C OG  
4382 N N   . ALA C 125 ? 0.9191 0.6699 0.8947 -0.0749 -0.2309 0.1361  125 ALA C N   
4383 C CA  . ALA C 125 ? 1.0115 0.7717 0.9934 -0.0713 -0.2270 0.1449  125 ALA C CA  
4384 C C   . ALA C 125 ? 1.0693 0.8362 1.0305 -0.0704 -0.2313 0.1484  125 ALA C C   
4385 O O   . ALA C 125 ? 1.0772 0.8388 1.0182 -0.0721 -0.2371 0.1406  125 ALA C O   
4386 C CB  . ALA C 125 ? 1.0429 0.7992 1.0319 -0.0697 -0.2248 0.1390  125 ALA C CB  
4387 N N   . SER C 126 ? 1.1328 0.9125 1.1003 -0.0677 -0.2278 0.1602  126 SER C N   
4388 C CA  . SER C 126 ? 1.1291 0.9185 1.0794 -0.0669 -0.2309 0.1639  126 SER C CA  
4389 C C   . SER C 126 ? 1.1158 0.9028 1.0565 -0.0655 -0.2328 0.1579  126 SER C C   
4390 O O   . SER C 126 ? 1.0553 0.8378 1.0071 -0.0639 -0.2299 0.1555  126 SER C O   
4391 C CB  . SER C 126 ? 1.1507 0.9569 1.1119 -0.0643 -0.2264 0.1791  126 SER C CB  
4392 O OG  . SER C 126 ? 1.1955 1.0037 1.1686 -0.0652 -0.2237 0.1855  126 SER C OG  
4393 N N   . THR C 127 ? 1.1393 0.9298 1.0598 -0.0664 -0.2374 0.1552  127 THR C N   
4394 C CA  . THR C 127 ? 1.1634 0.9523 1.0737 -0.0653 -0.2393 0.1498  127 THR C CA  
4395 C C   . THR C 127 ? 1.2006 1.0020 1.1217 -0.0617 -0.2350 0.1596  127 THR C C   
4396 O O   . THR C 127 ? 1.2250 1.0414 1.1477 -0.0607 -0.2334 0.1698  127 THR C O   
4397 C CB  . THR C 127 ? 1.1174 0.9078 1.0049 -0.0674 -0.2445 0.1444  127 THR C CB  
4398 O OG1 . THR C 127 ? 1.1215 0.8983 0.9991 -0.0702 -0.2483 0.1341  127 THR C OG1 
4399 C CG2 . THR C 127 ? 1.1988 0.9908 1.0773 -0.0661 -0.2456 0.1409  127 THR C CG2 
4400 N N   . LYS C 128 ? 1.2544 1.0504 1.1832 -0.0598 -0.2329 0.1567  128 LYS C N   
4401 C CA  . LYS C 128 ? 1.3245 1.1308 1.2634 -0.0563 -0.2289 0.1651  128 LYS C CA  
4402 C C   . LYS C 128 ? 1.4538 1.2585 1.3786 -0.0558 -0.2321 0.1586  128 LYS C C   
4403 O O   . LYS C 128 ? 1.5067 1.2984 1.4228 -0.0571 -0.2350 0.1473  128 LYS C O   
4404 C CB  . LYS C 128 ? 1.3812 1.1838 1.3439 -0.0541 -0.2228 0.1679  128 LYS C CB  
4405 C CG  . LYS C 128 ? 1.4579 1.2731 1.4346 -0.0501 -0.2174 0.1795  128 LYS C CG  
4406 C CD  . LYS C 128 ? 1.5009 1.3123 1.5031 -0.0482 -0.2104 0.1822  128 LYS C CD  
4407 C CE  . LYS C 128 ? 1.6097 1.4324 1.6253 -0.0438 -0.2050 0.1929  128 LYS C CE  
4408 N NZ  . LYS C 128 ? 1.7049 1.5288 1.7055 -0.0429 -0.2087 0.1888  128 LYS C NZ  
4409 N N   . GLY C 129 ? 1.5103 1.3290 1.4333 -0.0539 -0.2312 0.1660  129 GLY C N   
4410 C CA  . GLY C 129 ? 1.6618 1.4807 1.5720 -0.0535 -0.2339 0.1608  129 GLY C CA  
4411 C C   . GLY C 129 ? 1.7738 1.5872 1.6947 -0.0508 -0.2310 0.1595  129 GLY C C   
4412 O O   . GLY C 129 ? 1.7487 1.5626 1.6893 -0.0485 -0.2258 0.1654  129 GLY C O   
4413 N N   . PRO C 130 ? 1.9066 1.7146 1.8152 -0.0510 -0.2339 0.1514  130 PRO C N   
4414 C CA  . PRO C 130 ? 1.9629 1.7657 1.8792 -0.0485 -0.2317 0.1492  130 PRO C CA  
4415 C C   . PRO C 130 ? 1.9399 1.7566 1.8607 -0.0456 -0.2294 0.1581  130 PRO C C   
4416 O O   . PRO C 130 ? 1.8479 1.6781 1.7606 -0.0461 -0.2309 0.1633  130 PRO C O   
4417 C CB  . PRO C 130 ? 1.9706 1.7613 1.8697 -0.0504 -0.2364 0.1364  130 PRO C CB  
4418 C CG  . PRO C 130 ? 1.8534 1.6493 1.7348 -0.0531 -0.2406 0.1348  130 PRO C CG  
4419 C CD  . PRO C 130 ? 1.8445 1.6504 1.7314 -0.0538 -0.2393 0.1434  130 PRO C CD  
4420 N N   . CYS C 151 ? 1.5112 1.2647 1.4000 -0.0349 -0.2341 0.0994  151 CYS C N   
4421 C CA  . CYS C 151 ? 1.5101 1.2716 1.4024 -0.0361 -0.2338 0.1068  151 CYS C CA  
4422 C C   . CYS C 151 ? 1.6383 1.3964 1.5447 -0.0363 -0.2307 0.1068  151 CYS C C   
4423 O O   . CYS C 151 ? 1.7215 1.4704 1.6299 -0.0365 -0.2303 0.0988  151 CYS C O   
4424 C CB  . CYS C 151 ? 1.5171 1.2787 1.3913 -0.0393 -0.2386 0.1038  151 CYS C CB  
4425 S SG  . CYS C 151 ? 1.5592 1.3267 1.4178 -0.0400 -0.2419 0.1032  151 CYS C SG  
4426 N N   . LEU C 152 ? 1.7638 1.5304 1.6804 -0.0362 -0.2283 0.1159  152 LEU C N   
4427 C CA  . LEU C 152 ? 1.9216 1.6861 1.8532 -0.0365 -0.2248 0.1169  152 LEU C CA  
4428 C C   . LEU C 152 ? 2.1158 1.8861 2.0442 -0.0385 -0.2263 0.1224  152 LEU C C   
4429 O O   . LEU C 152 ? 1.9599 1.7415 1.8860 -0.0380 -0.2266 0.1310  152 LEU C O   
4430 C CB  . LEU C 152 ? 1.7048 1.4738 1.6592 -0.0335 -0.2180 0.1236  152 LEU C CB  
4431 C CG  . LEU C 152 ? 1.6810 1.4469 1.6540 -0.0339 -0.2132 0.1229  152 LEU C CG  
4432 C CD1 . LEU C 152 ? 1.6058 1.3621 1.5835 -0.0340 -0.2118 0.1117  152 LEU C CD1 
4433 C CD2 . LEU C 152 ? 1.5330 1.3082 1.5280 -0.0312 -0.2064 0.1348  152 LEU C CD2 
4434 N N   . VAL C 153 ? 2.5335 2.2971 2.4617 -0.0407 -0.2272 0.1175  153 VAL C N   
4435 C CA  . VAL C 153 ? 2.5212 2.2888 2.4465 -0.0429 -0.2287 0.1216  153 VAL C CA  
4436 C C   . VAL C 153 ? 2.5193 2.2891 2.4659 -0.0422 -0.2233 0.1273  153 VAL C C   
4437 O O   . VAL C 153 ? 2.5215 2.2848 2.4805 -0.0419 -0.2201 0.1224  153 VAL C O   
4438 C CB  . VAL C 153 ? 2.5136 2.2718 2.4228 -0.0460 -0.2337 0.1120  153 VAL C CB  
4439 C CG1 . VAL C 153 ? 2.5053 2.2673 2.4114 -0.0482 -0.2352 0.1159  153 VAL C CG1 
4440 C CG2 . VAL C 153 ? 2.5084 2.2640 2.3986 -0.0465 -0.2380 0.1063  153 VAL C CG2 
4441 N N   . LYS C 154 ? 2.2765 2.0563 2.2278 -0.0422 -0.2220 0.1374  154 LYS C N   
4442 C CA  . LYS C 154 ? 2.1314 1.9156 2.1052 -0.0409 -0.2157 0.1455  154 LYS C CA  
4443 C C   . LYS C 154 ? 2.1306 1.9162 2.1039 -0.0433 -0.2168 0.1481  154 LYS C C   
4444 O O   . LYS C 154 ? 2.0305 1.8241 1.9928 -0.0441 -0.2197 0.1533  154 LYS C O   
4445 C CB  . LYS C 154 ? 1.9915 1.7890 1.9768 -0.0374 -0.2114 0.1583  154 LYS C CB  
4446 C CG  . LYS C 154 ? 1.9961 1.7944 2.0082 -0.0349 -0.2033 0.1634  154 LYS C CG  
4447 C CD  . LYS C 154 ? 1.8439 1.6306 1.8611 -0.0348 -0.2018 0.1524  154 LYS C CD  
4448 C CE  . LYS C 154 ? 1.6323 1.4180 1.6769 -0.0336 -0.1935 0.1545  154 LYS C CE  
4449 N NZ  . LYS C 154 ? 1.6723 1.4542 1.7231 -0.0365 -0.1929 0.1522  154 LYS C NZ  
4450 N N   . ASP C 155 ? 2.2256 2.0042 2.2113 -0.0446 -0.2142 0.1442  155 ASP C N   
4451 C CA  . ASP C 155 ? 2.2205 2.0011 2.2134 -0.0463 -0.2129 0.1487  155 ASP C CA  
4452 C C   . ASP C 155 ? 2.2179 1.9990 2.1897 -0.0490 -0.2194 0.1471  155 ASP C C   
4453 O O   . ASP C 155 ? 2.2122 2.0037 2.1814 -0.0489 -0.2197 0.1562  155 ASP C O   
4454 C CB  . ASP C 155 ? 2.2120 2.0047 2.2244 -0.0436 -0.2065 0.1632  155 ASP C CB  
4455 C CG  . ASP C 155 ? 2.2117 2.0026 2.2492 -0.0414 -0.1987 0.1644  155 ASP C CG  
4456 O OD1 . ASP C 155 ? 2.2169 1.9974 2.2580 -0.0428 -0.1982 0.1533  155 ASP C OD1 
4457 O OD2 . ASP C 155 ? 2.2053 2.0060 2.2597 -0.0383 -0.1927 0.1764  155 ASP C OD2 
4458 N N   . TYR C 156 ? 1.7796 1.5500 1.7370 -0.0515 -0.2243 0.1354  156 TYR C N   
4459 C CA  . TYR C 156 ? 1.6789 1.4474 1.6171 -0.0542 -0.2301 0.1319  156 TYR C CA  
4460 C C   . TYR C 156 ? 1.6181 1.3770 1.5579 -0.0569 -0.2312 0.1246  156 TYR C C   
4461 O O   . TYR C 156 ? 1.6754 1.4258 1.6188 -0.0572 -0.2309 0.1161  156 TYR C O   
4462 C CB  . TYR C 156 ? 1.7362 1.5017 1.6539 -0.0546 -0.2350 0.1252  156 TYR C CB  
4463 C CG  . TYR C 156 ? 1.6836 1.4367 1.5956 -0.0551 -0.2370 0.1133  156 TYR C CG  
4464 C CD1 . TYR C 156 ? 1.7027 1.4533 1.6225 -0.0530 -0.2345 0.1105  156 TYR C CD1 
4465 C CD2 . TYR C 156 ? 1.6421 1.3870 1.5409 -0.0577 -0.2414 0.1052  156 TYR C CD2 
4466 C CE1 . TYR C 156 ? 1.7275 1.4685 1.6419 -0.0534 -0.2363 0.1000  156 TYR C CE1 
4467 C CE2 . TYR C 156 ? 1.6832 1.4186 1.5770 -0.0578 -0.2430 0.0952  156 TYR C CE2 
4468 C CZ  . TYR C 156 ? 1.6695 1.4035 1.5710 -0.0557 -0.2405 0.0927  156 TYR C CZ  
4469 O OH  . TYR C 156 ? 1.5337 1.2599 1.4303 -0.0557 -0.2421 0.0831  156 TYR C OH  
4470 N N   . PHE C 157 ? 1.4375 1.1985 1.3750 -0.0589 -0.2325 0.1279  157 PHE C N   
4471 C CA  . PHE C 157 ? 1.3805 1.1334 1.3212 -0.0615 -0.2333 0.1219  157 PHE C CA  
4472 C C   . PHE C 157 ? 1.4507 1.1944 1.3720 -0.0636 -0.2393 0.1111  157 PHE C C   
4473 O O   . PHE C 157 ? 1.5046 1.2404 1.4284 -0.0644 -0.2397 0.1026  157 PHE C O   
4474 C CB  . PHE C 157 ? 1.3029 1.0610 1.2502 -0.0627 -0.2320 0.1296  157 PHE C CB  
4475 C CG  . PHE C 157 ? 1.2721 1.0221 1.2218 -0.0657 -0.2332 0.1232  157 PHE C CG  
4476 C CD1 . PHE C 157 ? 1.3357 1.0812 1.3028 -0.0660 -0.2295 0.1189  157 PHE C CD1 
4477 C CD2 . PHE C 157 ? 1.2661 1.0134 1.2004 -0.0682 -0.2381 0.1206  157 PHE C CD2 
4478 C CE1 . PHE C 157 ? 1.2915 1.0306 1.2608 -0.0690 -0.2307 0.1125  157 PHE C CE1 
4479 C CE2 . PHE C 157 ? 1.2323 0.9723 1.1685 -0.0708 -0.2395 0.1147  157 PHE C CE2 
4480 C CZ  . PHE C 157 ? 1.2072 0.9434 1.1608 -0.0713 -0.2359 0.1107  157 PHE C CZ  
4481 N N   . PRO C 158 ? 1.4603 1.2053 1.3630 -0.0647 -0.2436 0.1110  158 PRO C N   
4482 C CA  . PRO C 158 ? 1.3665 1.1022 1.2525 -0.0665 -0.2485 0.1011  158 PRO C CA  
4483 C C   . PRO C 158 ? 1.4184 1.1486 1.3000 -0.0650 -0.2491 0.0940  158 PRO C C   
4484 O O   . PRO C 158 ? 1.4845 1.2182 1.3602 -0.0635 -0.2492 0.0955  158 PRO C O   
4485 C CB  . PRO C 158 ? 1.4143 1.1548 1.2842 -0.0677 -0.2516 0.1034  158 PRO C CB  
4486 C CG  . PRO C 158 ? 1.4173 1.1694 1.2967 -0.0673 -0.2487 0.1144  158 PRO C CG  
4487 C CD  . PRO C 158 ? 1.4025 1.1583 1.2990 -0.0644 -0.2440 0.1194  158 PRO C CD  
4488 N N   . GLU C 159 ? 1.3122 1.0347 1.1967 -0.0655 -0.2496 0.0862  159 GLU C N   
4489 C CA  . GLU C 159 ? 1.3593 1.0779 1.2427 -0.0638 -0.2494 0.0798  159 GLU C CA  
4490 C C   . GLU C 159 ? 1.4381 1.1543 1.3033 -0.0632 -0.2526 0.0767  159 GLU C C   
4491 O O   . GLU C 159 ? 1.4856 1.2025 1.3511 -0.0612 -0.2515 0.0760  159 GLU C O   
4492 C CB  . GLU C 159 ? 1.2454 0.9582 1.1337 -0.0647 -0.2497 0.0717  159 GLU C CB  
4493 C CG  . GLU C 159 ? 1.2398 0.9491 1.1244 -0.0631 -0.2502 0.0642  159 GLU C CG  
4494 C CD  . GLU C 159 ? 1.3019 1.0147 1.2007 -0.0611 -0.2457 0.0652  159 GLU C CD  
4495 O OE1 . GLU C 159 ? 1.3132 1.0308 1.2168 -0.0598 -0.2435 0.0725  159 GLU C OE1 
4496 O OE2 . GLU C 159 ? 1.2773 0.9890 1.1829 -0.0606 -0.2444 0.0585  159 GLU C OE2 
4497 N N   . PRO C 160 ? 1.3684 1.0815 1.2183 -0.0649 -0.2563 0.0743  160 PRO C N   
4498 C CA  . PRO C 160 ? 1.4116 1.1225 1.2461 -0.0644 -0.2584 0.0711  160 PRO C CA  
4499 C C   . PRO C 160 ? 1.5070 1.2253 1.3409 -0.0632 -0.2571 0.0763  160 PRO C C   
4500 O O   . PRO C 160 ? 1.5583 1.2846 1.3918 -0.0640 -0.2567 0.0826  160 PRO C O   
4501 C CB  . PRO C 160 ? 1.4622 1.1709 1.2841 -0.0669 -0.2613 0.0695  160 PRO C CB  
4502 C CG  . PRO C 160 ? 1.3254 1.0307 1.1537 -0.0681 -0.2617 0.0682  160 PRO C CG  
4503 C CD  . PRO C 160 ? 1.2765 0.9868 1.1229 -0.0673 -0.2583 0.0732  160 PRO C CD  
4504 N N   . VAL C 161 ? 1.5515 1.2682 1.3853 -0.0612 -0.2563 0.0738  161 VAL C N   
4505 C CA  . VAL C 161 ? 1.6131 1.3364 1.4456 -0.0599 -0.2553 0.0778  161 VAL C CA  
4506 C C   . VAL C 161 ? 1.7063 1.4239 1.5289 -0.0589 -0.2565 0.0714  161 VAL C C   
4507 O O   . VAL C 161 ? 1.7090 1.4192 1.5315 -0.0581 -0.2569 0.0655  161 VAL C O   
4508 C CB  . VAL C 161 ? 1.5798 1.3093 1.4292 -0.0578 -0.2514 0.0841  161 VAL C CB  
4509 C CG1 . VAL C 161 ? 1.6321 1.3563 1.4874 -0.0557 -0.2500 0.0793  161 VAL C CG1 
4510 C CG2 . VAL C 161 ? 1.6336 1.3737 1.4823 -0.0570 -0.2505 0.0914  161 VAL C CG2 
4511 N N   . THR C 162 ? 1.7735 1.4955 1.5878 -0.0591 -0.2570 0.0727  162 THR C N   
4512 C CA  . THR C 162 ? 1.8154 1.5324 1.6197 -0.0585 -0.2580 0.0670  162 THR C CA  
4513 C C   . THR C 162 ? 1.8222 1.5459 1.6286 -0.0570 -0.2567 0.0705  162 THR C C   
4514 O O   . THR C 162 ? 1.8737 1.6074 1.6801 -0.0579 -0.2563 0.0759  162 THR C O   
4515 C CB  . THR C 162 ? 1.8264 1.5411 1.6166 -0.0609 -0.2600 0.0631  162 THR C CB  
4516 O OG1 . THR C 162 ? 1.7726 1.4970 1.5612 -0.0630 -0.2601 0.0678  162 THR C OG1 
4517 C CG2 . THR C 162 ? 1.7545 1.4605 1.5418 -0.0617 -0.2614 0.0585  162 THR C CG2 
4518 N N   . VAL C 163 ? 1.7740 1.4931 1.5823 -0.0549 -0.2560 0.0674  163 VAL C N   
4519 C CA  . VAL C 163 ? 1.7856 1.5098 1.5963 -0.0532 -0.2547 0.0701  163 VAL C CA  
4520 C C   . VAL C 163 ? 1.8089 1.5274 1.6083 -0.0530 -0.2560 0.0639  163 VAL C C   
4521 O O   . VAL C 163 ? 1.8232 1.5328 1.6194 -0.0524 -0.2566 0.0581  163 VAL C O   
4522 C CB  . VAL C 163 ? 1.7682 1.4928 1.5937 -0.0505 -0.2520 0.0725  163 VAL C CB  
4523 C CG1 . VAL C 163 ? 1.7349 1.4660 1.5636 -0.0487 -0.2505 0.0766  163 VAL C CG1 
4524 C CG2 . VAL C 163 ? 1.7900 1.5184 1.6280 -0.0508 -0.2502 0.0777  163 VAL C CG2 
4525 N N   . SER C 164 ? 1.7842 1.5087 1.5783 -0.0536 -0.2562 0.0654  164 SER C N   
4526 C CA  . SER C 164 ? 1.7803 1.5003 1.5648 -0.0537 -0.2569 0.0600  164 SER C CA  
4527 C C   . SER C 164 ? 1.8291 1.5553 1.6165 -0.0522 -0.2560 0.0630  164 SER C C   
4528 O O   . SER C 164 ? 1.7955 1.5307 1.5916 -0.0513 -0.2548 0.0697  164 SER C O   
4529 C CB  . SER C 164 ? 1.8048 1.5256 1.5778 -0.0569 -0.2580 0.0567  164 SER C CB  
4530 O OG  . SER C 164 ? 1.7752 1.5086 1.5480 -0.0587 -0.2579 0.0612  164 SER C OG  
4531 N N   . TRP C 165 ? 1.8814 1.6029 1.6619 -0.0518 -0.2563 0.0583  165 TRP C N   
4532 C CA  . TRP C 165 ? 1.8303 1.5570 1.6122 -0.0506 -0.2557 0.0603  165 TRP C CA  
4533 C C   . TRP C 165 ? 1.8179 1.5453 1.5889 -0.0528 -0.2566 0.0560  165 TRP C C   
4534 O O   . TRP C 165 ? 1.7992 1.5173 1.5629 -0.0532 -0.2569 0.0499  165 TRP C O   
4535 C CB  . TRP C 165 ? 1.8366 1.5566 1.6242 -0.0473 -0.2547 0.0587  165 TRP C CB  
4536 C CG  . TRP C 165 ? 1.7625 1.4865 1.5642 -0.0451 -0.2528 0.0642  165 TRP C CG  
4537 C CD1 . TRP C 165 ? 1.7532 1.4744 1.5632 -0.0445 -0.2517 0.0646  165 TRP C CD1 
4538 C CD2 . TRP C 165 ? 1.7889 1.5208 1.5991 -0.0433 -0.2511 0.0700  165 TRP C CD2 
4539 N NE1 . TRP C 165 ? 1.7735 1.4998 1.5974 -0.0426 -0.2491 0.0701  165 TRP C NE1 
4540 C CE2 . TRP C 165 ? 1.7597 1.4927 1.5841 -0.0416 -0.2486 0.0738  165 TRP C CE2 
4541 C CE3 . TRP C 165 ? 1.7628 1.5014 1.5708 -0.0430 -0.2512 0.0724  165 TRP C CE3 
4542 C CZ2 . TRP C 165 ? 1.6796 1.4196 1.5164 -0.0393 -0.2458 0.0803  165 TRP C CZ2 
4543 C CZ3 . TRP C 165 ? 1.6938 1.4399 1.5133 -0.0407 -0.2490 0.0791  165 TRP C CZ3 
4544 C CH2 . TRP C 165 ? 1.6508 1.3972 1.4847 -0.0387 -0.2461 0.0832  165 TRP C CH2 
4545 N N   . SER C 172 ? 1.8652 1.5441 1.6306 -0.0384 -0.2541 0.0315  172 SER C N   
4546 C CA  . SER C 172 ? 1.8606 1.5374 1.6286 -0.0353 -0.2532 0.0289  172 SER C CA  
4547 C C   . SER C 172 ? 1.8934 1.5747 1.6737 -0.0339 -0.2520 0.0305  172 SER C C   
4548 O O   . SER C 172 ? 1.8755 1.5611 1.6613 -0.0341 -0.2515 0.0341  172 SER C O   
4549 C CB  . SER C 172 ? 1.8398 1.5153 1.6027 -0.0348 -0.2531 0.0281  172 SER C CB  
4550 O OG  . SER C 172 ? 1.7998 1.4808 1.5644 -0.0364 -0.2535 0.0319  172 SER C OG  
4551 N N   . GLY C 173 ? 2.0208 1.7017 1.8061 -0.0326 -0.2512 0.0278  173 GLY C N   
4552 C CA  . GLY C 173 ? 2.0523 1.7374 1.8508 -0.0316 -0.2493 0.0282  173 GLY C CA  
4553 C C   . GLY C 173 ? 2.1216 1.8109 1.9281 -0.0335 -0.2489 0.0329  173 GLY C C   
4554 O O   . GLY C 173 ? 2.1590 1.8524 1.9775 -0.0328 -0.2468 0.0352  173 GLY C O   
4555 N N   . VAL C 174 ? 2.0312 1.7197 1.8321 -0.0357 -0.2507 0.0346  174 VAL C N   
4556 C CA  . VAL C 174 ? 1.9632 1.6560 1.7707 -0.0375 -0.2505 0.0395  174 VAL C CA  
4557 C C   . VAL C 174 ? 2.0494 1.7424 1.8650 -0.0376 -0.2496 0.0373  174 VAL C C   
4558 O O   . VAL C 174 ? 1.9994 1.6893 1.8090 -0.0383 -0.2510 0.0342  174 VAL C O   
4559 C CB  . VAL C 174 ? 1.8625 1.5552 1.6601 -0.0401 -0.2526 0.0418  174 VAL C CB  
4560 C CG1 . VAL C 174 ? 1.8025 1.5007 1.6069 -0.0418 -0.2523 0.0471  174 VAL C CG1 
4561 C CG2 . VAL C 174 ? 1.8454 1.5393 1.6358 -0.0404 -0.2532 0.0429  174 VAL C CG2 
4562 N N   . HIS C 175 ? 2.0568 1.7539 1.8867 -0.0370 -0.2470 0.0389  175 HIS C N   
4563 C CA  . HIS C 175 ? 2.0615 1.7601 1.9015 -0.0375 -0.2455 0.0367  175 HIS C CA  
4564 C C   . HIS C 175 ? 2.0999 1.8021 1.9476 -0.0393 -0.2449 0.0427  175 HIS C C   
4565 O O   . HIS C 175 ? 2.0284 1.7347 1.8852 -0.0388 -0.2426 0.0480  175 HIS C O   
4566 C CB  . HIS C 175 ? 1.9901 1.6912 1.8429 -0.0357 -0.2421 0.0329  175 HIS C CB  
4567 C CG  . HIS C 175 ? 2.0374 1.7364 1.8834 -0.0338 -0.2425 0.0270  175 HIS C CG  
4568 N ND1 . HIS C 175 ? 2.0816 1.7808 1.9255 -0.0334 -0.2429 0.0207  175 HIS C ND1 
4569 C CD2 . HIS C 175 ? 2.0393 1.7368 1.8804 -0.0320 -0.2424 0.0267  175 HIS C CD2 
4570 C CE1 . HIS C 175 ? 2.0410 1.7392 1.8790 -0.0313 -0.2430 0.0171  175 HIS C CE1 
4571 N NE2 . HIS C 175 ? 2.0651 1.7616 1.9012 -0.0306 -0.2427 0.0205  175 HIS C NE2 
4572 N N   . THR C 176 ? 2.1941 1.8950 2.0383 -0.0412 -0.2466 0.0423  176 THR C N   
4573 C CA  . THR C 176 ? 2.1377 1.8419 1.9892 -0.0430 -0.2460 0.0477  176 THR C CA  
4574 C C   . THR C 176 ? 2.0655 1.7712 1.9307 -0.0434 -0.2437 0.0446  176 THR C C   
4575 O O   . THR C 176 ? 2.0540 1.7574 1.9156 -0.0444 -0.2452 0.0400  176 THR C O   
4576 C CB  . THR C 176 ? 2.1301 1.8323 1.9689 -0.0452 -0.2493 0.0492  176 THR C CB  
4577 O OG1 . THR C 176 ? 2.0188 1.7202 1.8454 -0.0451 -0.2511 0.0502  176 THR C OG1 
4578 C CG2 . THR C 176 ? 2.0910 1.7979 1.9368 -0.0468 -0.2487 0.0555  176 THR C CG2 
4579 N N   . PHE C 177 ? 1.8904 1.6002 1.7720 -0.0427 -0.2396 0.0472  177 PHE C N   
4580 C CA  . PHE C 177 ? 1.7006 1.4125 1.5975 -0.0433 -0.2364 0.0431  177 PHE C CA  
4581 C C   . PHE C 177 ? 1.5867 1.2991 1.4868 -0.0458 -0.2371 0.0451  177 PHE C C   
4582 O O   . PHE C 177 ? 1.6209 1.3340 1.5172 -0.0467 -0.2384 0.0519  177 PHE C O   
4583 C CB  . PHE C 177 ? 1.6869 1.4030 1.6022 -0.0419 -0.2310 0.0455  177 PHE C CB  
4584 C CG  . PHE C 177 ? 1.7143 1.4299 1.6283 -0.0395 -0.2298 0.0423  177 PHE C CG  
4585 C CD1 . PHE C 177 ? 1.7626 1.4779 1.6693 -0.0380 -0.2309 0.0475  177 PHE C CD1 
4586 C CD2 . PHE C 177 ? 1.6888 1.4053 1.6090 -0.0389 -0.2277 0.0338  177 PHE C CD2 
4587 C CE1 . PHE C 177 ? 1.6822 1.3967 1.5875 -0.0358 -0.2299 0.0446  177 PHE C CE1 
4588 C CE2 . PHE C 177 ? 1.6983 1.4145 1.6172 -0.0367 -0.2266 0.0308  177 PHE C CE2 
4589 C CZ  . PHE C 177 ? 1.6986 1.4131 1.6098 -0.0351 -0.2278 0.0363  177 PHE C CZ  
4590 N N   . PRO C 178 ? 1.5423 1.2555 1.4494 -0.0470 -0.2362 0.0390  178 PRO C N   
4591 C CA  . PRO C 178 ? 1.5083 1.2217 1.4184 -0.0496 -0.2371 0.0402  178 PRO C CA  
4592 C C   . PRO C 178 ? 1.5622 1.2789 1.4863 -0.0502 -0.2337 0.0481  178 PRO C C   
4593 O O   . PRO C 178 ? 1.5960 1.3158 1.5332 -0.0488 -0.2293 0.0512  178 PRO C O   
4594 C CB  . PRO C 178 ? 1.3957 1.1114 1.3149 -0.0505 -0.2355 0.0315  178 PRO C CB  
4595 C CG  . PRO C 178 ? 1.5095 1.2249 1.4206 -0.0485 -0.2365 0.0254  178 PRO C CG  
4596 C CD  . PRO C 178 ? 1.5922 1.3065 1.5020 -0.0463 -0.2352 0.0300  178 PRO C CD  
4597 N N   . ALA C 179 ? 1.6260 1.3422 1.5478 -0.0523 -0.2355 0.0516  179 ALA C N   
4598 C CA  . ALA C 179 ? 1.6384 1.3583 1.5717 -0.0528 -0.2327 0.0603  179 ALA C CA  
4599 C C   . ALA C 179 ? 1.6397 1.3628 1.5961 -0.0537 -0.2271 0.0588  179 ALA C C   
4600 O O   . ALA C 179 ? 1.4621 1.1847 1.4235 -0.0550 -0.2265 0.0503  179 ALA C O   
4601 C CB  . ALA C 179 ? 1.6045 1.3231 1.5270 -0.0549 -0.2365 0.0640  179 ALA C CB  
4602 N N   . VAL C 180 ? 1.7567 1.4840 1.7280 -0.0529 -0.2224 0.0671  180 VAL C N   
4603 C CA  . VAL C 180 ? 1.7381 1.4687 1.7338 -0.0538 -0.2160 0.0669  180 VAL C CA  
4604 C C   . VAL C 180 ? 1.7222 1.4559 1.7260 -0.0545 -0.2142 0.0772  180 VAL C C   
4605 O O   . VAL C 180 ? 1.7228 1.4606 1.7303 -0.0525 -0.2120 0.0871  180 VAL C O   
4606 C CB  . VAL C 180 ? 1.7354 1.4687 1.7478 -0.0516 -0.2098 0.0660  180 VAL C CB  
4607 C CG1 . VAL C 180 ? 1.7320 1.4636 1.7412 -0.0517 -0.2105 0.0537  180 VAL C CG1 
4608 C CG2 . VAL C 180 ? 1.7582 1.4938 1.7671 -0.0484 -0.2092 0.0753  180 VAL C CG2 
4609 N N   . LEU C 181 ? 1.4822 1.2147 1.4890 -0.0574 -0.2149 0.0748  181 LEU C N   
4610 C CA  . LEU C 181 ? 1.4710 1.2065 1.4901 -0.0586 -0.2120 0.0826  181 LEU C CA  
4611 C C   . LEU C 181 ? 1.4893 1.2292 1.5360 -0.0575 -0.2032 0.0863  181 LEU C C   
4612 O O   . LEU C 181 ? 1.5184 1.2582 1.5804 -0.0587 -0.1990 0.0782  181 LEU C O   
4613 C CB  . LEU C 181 ? 1.3533 1.0858 1.3704 -0.0621 -0.2147 0.0767  181 LEU C CB  
4614 C CG  . LEU C 181 ? 1.3574 1.0921 1.3852 -0.0639 -0.2125 0.0838  181 LEU C CG  
4615 C CD1 . LEU C 181 ? 1.3320 1.0629 1.3413 -0.0661 -0.2193 0.0824  181 LEU C CD1 
4616 C CD2 . LEU C 181 ? 1.4837 1.2197 1.5363 -0.0658 -0.2061 0.0784  181 LEU C CD2 
4617 N N   . GLN C 182 ? 1.4848 1.2297 1.5385 -0.0552 -0.2000 0.0985  182 GLN C N   
4618 C CA  . GLN C 182 ? 1.4023 1.1516 1.4831 -0.0536 -0.1909 0.1036  182 GLN C CA  
4619 C C   . GLN C 182 ? 1.3172 1.0676 1.4166 -0.0562 -0.1865 0.1049  182 GLN C C   
4620 O O   . GLN C 182 ? 1.2933 1.0409 1.3835 -0.0591 -0.1910 0.1018  182 GLN C O   
4621 C CB  . GLN C 182 ? 1.4153 1.1710 1.4974 -0.0498 -0.1889 0.1170  182 GLN C CB  
4622 C CG  . GLN C 182 ? 1.4498 1.2047 1.5169 -0.0474 -0.1922 0.1149  182 GLN C CG  
4623 C CD  . GLN C 182 ? 1.4518 1.2144 1.5239 -0.0435 -0.1891 0.1276  182 GLN C CD  
4624 O OE1 . GLN C 182 ? 1.3781 1.1408 1.4430 -0.0413 -0.1902 0.1266  182 GLN C OE1 
4625 N NE2 . GLN C 182 ? 1.4940 1.2636 1.5784 -0.0425 -0.1852 0.1398  182 GLN C NE2 
4626 N N   . SER C 183 ? 1.2615 1.0156 1.3885 -0.0552 -0.1773 0.1091  183 SER C N   
4627 C CA  . SER C 183 ? 1.2048 0.9596 1.3525 -0.0579 -0.1720 0.1090  183 SER C CA  
4628 C C   . SER C 183 ? 1.1981 0.9549 1.3391 -0.0585 -0.1748 0.1196  183 SER C C   
4629 O O   . SER C 183 ? 1.1393 0.8945 1.2852 -0.0617 -0.1749 0.1170  183 SER C O   
4630 C CB  . SER C 183 ? 1.1208 0.8796 1.3007 -0.0564 -0.1605 0.1129  183 SER C CB  
4631 O OG  . SER C 183 ? 1.0854 0.8494 1.2684 -0.0519 -0.1577 0.1266  183 SER C OG  
4632 N N   . SER C 184 ? 1.2034 0.9647 1.3328 -0.0554 -0.1772 0.1312  184 SER C N   
4633 C CA  . SER C 184 ? 1.1590 0.9243 1.2822 -0.0556 -0.1794 0.1418  184 SER C CA  
4634 C C   . SER C 184 ? 1.2337 0.9933 1.3342 -0.0591 -0.1882 0.1342  184 SER C C   
4635 O O   . SER C 184 ? 1.1883 0.9482 1.2906 -0.0612 -0.1887 0.1373  184 SER C O   
4636 C CB  . SER C 184 ? 1.1867 0.9598 1.3002 -0.0517 -0.1807 0.1542  184 SER C CB  
4637 O OG  . SER C 184 ? 1.1901 0.9608 1.2857 -0.0505 -0.1856 0.1482  184 SER C OG  
4638 N N   . GLY C 185 ? 1.3010 1.0552 1.3806 -0.0597 -0.1948 0.1244  185 GLY C N   
4639 C CA  . GLY C 185 ? 1.2298 0.9788 1.2870 -0.0625 -0.2030 0.1178  185 GLY C CA  
4640 C C   . GLY C 185 ? 1.2433 0.9923 1.2748 -0.0609 -0.2096 0.1186  185 GLY C C   
4641 O O   . GLY C 185 ? 1.2121 0.9576 1.2236 -0.0628 -0.2162 0.1152  185 GLY C O   
4642 N N   . LEU C 186 ? 1.3488 1.1017 1.3816 -0.0577 -0.2076 0.1229  186 LEU C N   
4643 C CA  . LEU C 186 ? 1.4369 1.1915 1.4482 -0.0562 -0.2128 0.1245  186 LEU C CA  
4644 C C   . LEU C 186 ? 1.4878 1.2378 1.4941 -0.0550 -0.2137 0.1158  186 LEU C C   
4645 O O   . LEU C 186 ? 1.4980 1.2488 1.5213 -0.0534 -0.2081 0.1151  186 LEU C O   
4646 C CB  . LEU C 186 ? 1.5233 1.2887 1.5393 -0.0533 -0.2099 0.1384  186 LEU C CB  
4647 C CG  . LEU C 186 ? 1.3675 1.1397 1.3979 -0.0535 -0.2059 0.1491  186 LEU C CG  
4648 C CD1 . LEU C 186 ? 1.5027 1.2866 1.5469 -0.0496 -0.2002 0.1630  186 LEU C CD1 
4649 C CD2 . LEU C 186 ? 1.3207 1.0939 1.3331 -0.0558 -0.2118 0.1503  186 LEU C CD2 
4650 N N   . TYR C 187 ? 1.5737 1.3190 1.5573 -0.0558 -0.2203 0.1093  187 TYR C N   
4651 C CA  . TYR C 187 ? 1.6368 1.3777 1.6135 -0.0547 -0.2218 0.1010  187 TYR C CA  
4652 C C   . TYR C 187 ? 1.7261 1.4721 1.7014 -0.0515 -0.2205 0.1071  187 TYR C C   
4653 O O   . TYR C 187 ? 1.8280 1.5815 1.8020 -0.0504 -0.2201 0.1171  187 TYR C O   
4654 C CB  . TYR C 187 ? 1.6157 1.3500 1.5695 -0.0564 -0.2287 0.0927  187 TYR C CB  
4655 C CG  . TYR C 187 ? 1.4509 1.1806 1.4031 -0.0594 -0.2309 0.0871  187 TYR C CG  
4656 C CD1 . TYR C 187 ? 1.3901 1.1211 1.3374 -0.0612 -0.2330 0.0919  187 TYR C CD1 
4657 C CD2 . TYR C 187 ? 1.3990 1.1243 1.3544 -0.0604 -0.2310 0.0769  187 TYR C CD2 
4658 C CE1 . TYR C 187 ? 1.3040 1.0306 1.2496 -0.0640 -0.2351 0.0868  187 TYR C CE1 
4659 C CE2 . TYR C 187 ? 1.3141 1.0362 1.2681 -0.0632 -0.2331 0.0718  187 TYR C CE2 
4660 C CZ  . TYR C 187 ? 1.2246 0.9469 1.1737 -0.0649 -0.2353 0.0769  187 TYR C CZ  
4661 O OH  . TYR C 187 ? 1.1011 0.8201 1.0488 -0.0676 -0.2375 0.0719  187 TYR C OH  
4662 N N   . SER C 188 ? 1.6680 1.4109 1.6436 -0.0501 -0.2197 0.1008  188 SER C N   
4663 C CA  . SER C 188 ? 1.7492 1.4955 1.7213 -0.0473 -0.2192 0.1046  188 SER C CA  
4664 C C   . SER C 188 ? 1.7792 1.5187 1.7402 -0.0471 -0.2220 0.0940  188 SER C C   
4665 O O   . SER C 188 ? 1.6900 1.4241 1.6516 -0.0486 -0.2227 0.0849  188 SER C O   
4666 C CB  . SER C 188 ? 1.7328 1.4851 1.7280 -0.0447 -0.2118 0.1120  188 SER C CB  
4667 O OG  . SER C 188 ? 1.7840 1.5390 1.7767 -0.0419 -0.2112 0.1144  188 SER C OG  
4668 N N   . LEU C 189 ? 1.8054 1.5461 1.7564 -0.0452 -0.2237 0.0953  189 LEU C N   
4669 C CA  . LEU C 189 ? 1.7995 1.5341 1.7393 -0.0448 -0.2264 0.0859  189 LEU C CA  
4670 C C   . LEU C 189 ? 1.9286 1.6659 1.8636 -0.0423 -0.2264 0.0890  189 LEU C C   
4671 O O   . LEU C 189 ? 1.9566 1.7010 1.8933 -0.0412 -0.2254 0.0982  189 LEU C O   
4672 C CB  . LEU C 189 ? 1.7337 1.4627 1.6535 -0.0470 -0.2325 0.0799  189 LEU C CB  
4673 C CG  . LEU C 189 ? 1.8229 1.5531 1.7241 -0.0478 -0.2371 0.0831  189 LEU C CG  
4674 C CD1 . LEU C 189 ? 1.9049 1.6337 1.7928 -0.0465 -0.2394 0.0806  189 LEU C CD1 
4675 C CD2 . LEU C 189 ? 1.7011 1.4267 1.5918 -0.0505 -0.2408 0.0790  189 LEU C CD2 
4676 N N   . SER C 190 ? 2.0490 1.7812 1.9776 -0.0415 -0.2276 0.0812  190 SER C N   
4677 C CA  . SER C 190 ? 2.0242 1.7576 1.9467 -0.0394 -0.2280 0.0825  190 SER C CA  
4678 C C   . SER C 190 ? 2.0240 1.7510 1.9270 -0.0400 -0.2330 0.0747  190 SER C C   
4679 O O   . SER C 190 ? 2.0493 1.7708 1.9491 -0.0409 -0.2342 0.0667  190 SER C O   
4680 C CB  . SER C 190 ? 1.9885 1.7228 1.9277 -0.0370 -0.2227 0.0816  190 SER C CB  
4681 O OG  . SER C 190 ? 1.9272 1.6575 1.8752 -0.0378 -0.2205 0.0732  190 SER C OG  
4682 N N   . SER C 191 ? 1.9308 1.6594 1.8217 -0.0395 -0.2355 0.0771  191 SER C N   
4683 C CA  . SER C 191 ? 1.8566 1.5795 1.7299 -0.0400 -0.2395 0.0707  191 SER C CA  
4684 C C   . SER C 191 ? 1.7933 1.5171 1.6648 -0.0378 -0.2389 0.0709  191 SER C C   
4685 O O   . SER C 191 ? 1.7630 1.4936 1.6371 -0.0370 -0.2380 0.0779  191 SER C O   
4686 C CB  . SER C 191 ? 1.7945 1.5182 1.6530 -0.0423 -0.2434 0.0722  191 SER C CB  
4687 O OG  . SER C 191 ? 1.7830 1.5017 1.6261 -0.0426 -0.2464 0.0668  191 SER C OG  
4688 N N   . VAL C 192 ? 1.7454 1.4631 1.6122 -0.0369 -0.2395 0.0634  192 VAL C N   
4689 C CA  . VAL C 192 ? 1.6997 1.4173 1.5648 -0.0348 -0.2389 0.0628  192 VAL C CA  
4690 C C   . VAL C 192 ? 1.7098 1.4217 1.5576 -0.0352 -0.2425 0.0570  192 VAL C C   
4691 O O   . VAL C 192 ? 1.8108 1.5179 1.6503 -0.0365 -0.2446 0.0522  192 VAL C O   
4692 C CB  . VAL C 192 ? 1.7119 1.4288 1.5915 -0.0327 -0.2348 0.0595  192 VAL C CB  
4693 C CG1 . VAL C 192 ? 1.7432 1.4546 1.6196 -0.0329 -0.2354 0.0502  192 VAL C CG1 
4694 C CG2 . VAL C 192 ? 1.6657 1.3837 1.5457 -0.0304 -0.2337 0.0607  192 VAL C CG2 
4695 N N   . CYS C 207 ? 1.6983 1.4743 1.5089 -0.0479 -0.2514 0.0905  207 CYS C N   
4696 C CA  . CYS C 207 ? 1.7787 1.5442 1.5886 -0.0488 -0.2519 0.0867  207 CYS C CA  
4697 C C   . CYS C 207 ? 1.7896 1.5630 1.5982 -0.0512 -0.2524 0.0900  207 CYS C C   
4698 O O   . CYS C 207 ? 1.7735 1.5607 1.5885 -0.0508 -0.2512 0.0983  207 CYS C O   
4699 C CB  . CYS C 207 ? 1.7308 1.4895 1.5537 -0.0458 -0.2496 0.0883  207 CYS C CB  
4700 S SG  . CYS C 207 ? 1.5386 1.3059 1.3775 -0.0447 -0.2466 0.0982  207 CYS C SG  
4701 N N   . ASN C 208 ? 1.7693 1.5345 1.5698 -0.0535 -0.2540 0.0839  208 ASN C N   
4702 C CA  . ASN C 208 ? 1.7722 1.5433 1.5698 -0.0561 -0.2547 0.0856  208 ASN C CA  
4703 C C   . ASN C 208 ? 1.7890 1.5514 1.5925 -0.0556 -0.2543 0.0856  208 ASN C C   
4704 O O   . ASN C 208 ? 1.7790 1.5285 1.5786 -0.0557 -0.2552 0.0788  208 ASN C O   
4705 C CB  . ASN C 208 ? 1.7777 1.5471 1.5613 -0.0596 -0.2564 0.0782  208 ASN C CB  
4706 C CG  . ASN C 208 ? 1.7819 1.5532 1.5592 -0.0601 -0.2567 0.0744  208 ASN C CG  
4707 O OD1 . ASN C 208 ? 1.8261 1.5856 1.5981 -0.0598 -0.2571 0.0677  208 ASN C OD1 
4708 N ND2 . ASN C 208 ? 1.6965 1.4836 1.4748 -0.0607 -0.2563 0.0789  208 ASN C ND2 
4709 N N   . VAL C 209 ? 1.7843 1.5547 1.5978 -0.0550 -0.2529 0.0934  209 VAL C N   
4710 C CA  . VAL C 209 ? 1.7500 1.5142 1.5698 -0.0550 -0.2524 0.0939  209 VAL C CA  
4711 C C   . VAL C 209 ? 1.7569 1.5265 1.5703 -0.0580 -0.2538 0.0947  209 VAL C C   
4712 O O   . VAL C 209 ? 1.7679 1.5514 1.5801 -0.0589 -0.2535 0.1000  209 VAL C O   
4713 C CB  . VAL C 209 ? 1.6702 1.4388 1.5076 -0.0523 -0.2490 0.1019  209 VAL C CB  
4714 C CG1 . VAL C 209 ? 1.7143 1.4762 1.5591 -0.0527 -0.2483 0.1014  209 VAL C CG1 
4715 C CG2 . VAL C 209 ? 1.6263 1.3908 1.4702 -0.0494 -0.2473 0.1008  209 VAL C CG2 
4716 N N   . ASN C 210 ? 1.7017 1.4610 1.5109 -0.0595 -0.2552 0.0894  210 ASN C N   
4717 C CA  . ASN C 210 ? 1.6674 1.4297 1.4698 -0.0624 -0.2566 0.0889  210 ASN C CA  
4718 C C   . ASN C 210 ? 1.6536 1.4109 1.4639 -0.0624 -0.2562 0.0908  210 ASN C C   
4719 O O   . ASN C 210 ? 1.6627 1.4078 1.4726 -0.0622 -0.2570 0.0850  210 ASN C O   
4720 C CB  . ASN C 210 ? 1.7206 1.4752 1.5086 -0.0648 -0.2586 0.0797  210 ASN C CB  
4721 C CG  . ASN C 210 ? 1.7102 1.4734 1.4899 -0.0681 -0.2594 0.0793  210 ASN C CG  
4722 O OD1 . ASN C 210 ? 1.6896 1.4649 1.4736 -0.0686 -0.2588 0.0860  210 ASN C OD1 
4723 N ND2 . ASN C 210 ? 1.6527 1.4101 1.4212 -0.0703 -0.2604 0.0713  210 ASN C ND2 
4724 N N   . HIS C 211 ? 1.6792 1.4469 1.4972 -0.0624 -0.2549 0.0989  211 HIS C N   
4725 C CA  . HIS C 211 ? 1.6058 1.3704 1.4313 -0.0629 -0.2544 0.1012  211 HIS C CA  
4726 C C   . HIS C 211 ? 1.6185 1.3862 1.4335 -0.0660 -0.2564 0.0999  211 HIS C C   
4727 O O   . HIS C 211 ? 1.6143 1.3956 1.4287 -0.0668 -0.2559 0.1059  211 HIS C O   
4728 C CB  . HIS C 211 ? 1.5707 1.3445 1.4129 -0.0608 -0.2509 0.1116  211 HIS C CB  
4729 C CG  . HIS C 211 ? 1.5537 1.3219 1.4070 -0.0609 -0.2495 0.1129  211 HIS C CG  
4730 N ND1 . HIS C 211 ? 1.5030 1.2693 1.3518 -0.0633 -0.2513 0.1118  211 HIS C ND1 
4731 C CD2 . HIS C 211 ? 1.5922 1.3568 1.4617 -0.0590 -0.2464 0.1150  211 HIS C CD2 
4732 C CE1 . HIS C 211 ? 1.5001 1.2617 1.3615 -0.0631 -0.2495 0.1131  211 HIS C CE1 
4733 N NE2 . HIS C 211 ? 1.5280 1.2888 1.4025 -0.0606 -0.2463 0.1149  211 HIS C NE2 
4734 N N   . LYS C 212 ? 1.6334 1.3892 1.4406 -0.0677 -0.2586 0.0921  212 LYS C N   
4735 C CA  . LYS C 212 ? 1.6053 1.3628 1.4018 -0.0708 -0.2604 0.0895  212 LYS C CA  
4736 C C   . LYS C 212 ? 1.5871 1.3506 1.3900 -0.0716 -0.2599 0.0959  212 LYS C C   
4737 O O   . LYS C 212 ? 1.5588 1.3336 1.3568 -0.0734 -0.2601 0.0990  212 LYS C O   
4738 C CB  . LYS C 212 ? 1.6114 1.3546 1.3983 -0.0720 -0.2625 0.0798  212 LYS C CB  
4739 C CG  . LYS C 212 ? 1.6981 1.4356 1.4787 -0.0711 -0.2627 0.0738  212 LYS C CG  
4740 C CD  . LYS C 212 ? 1.7489 1.4719 1.5287 -0.0701 -0.2635 0.0675  212 LYS C CD  
4741 C CE  . LYS C 212 ? 1.6554 1.3758 1.4484 -0.0678 -0.2625 0.0704  212 LYS C CE  
4742 N NZ  . LYS C 212 ? 1.5469 1.2559 1.3393 -0.0669 -0.2634 0.0640  212 LYS C NZ  
4743 N N   . PRO C 213 ? 1.5927 1.3502 1.4066 -0.0707 -0.2591 0.0980  213 PRO C N   
4744 C CA  . PRO C 213 ? 1.5514 1.3147 1.3716 -0.0716 -0.2584 0.1044  213 PRO C CA  
4745 C C   . PRO C 213 ? 1.5415 1.3214 1.3701 -0.0703 -0.2557 0.1153  213 PRO C C   
4746 O O   . PRO C 213 ? 1.4414 1.2295 1.2719 -0.0713 -0.2552 0.1211  213 PRO C O   
4747 C CB  . PRO C 213 ? 1.4025 1.1557 1.2348 -0.0708 -0.2574 0.1035  213 PRO C CB  
4748 C CG  . PRO C 213 ? 1.4248 1.1655 1.2505 -0.0706 -0.2592 0.0939  213 PRO C CG  
4749 C CD  . PRO C 213 ? 1.5304 1.2749 1.3498 -0.0694 -0.2591 0.0929  213 PRO C CD  
4750 N N   . SER C 214 ? 1.5220 1.3077 1.3559 -0.0679 -0.2538 0.1188  214 SER C N   
4751 C CA  . SER C 214 ? 1.4896 1.2926 1.3319 -0.0661 -0.2510 0.1299  214 SER C CA  
4752 C C   . SER C 214 ? 1.6143 1.4309 1.4447 -0.0673 -0.2521 0.1302  214 SER C C   
4753 O O   . SER C 214 ? 1.6312 1.4649 1.4672 -0.0660 -0.2501 0.1396  214 SER C O   
4754 C CB  . SER C 214 ? 1.5143 1.3173 1.3711 -0.0626 -0.2476 0.1346  214 SER C CB  
4755 O OG  . SER C 214 ? 1.5527 1.3730 1.4186 -0.0605 -0.2445 0.1463  214 SER C OG  
4756 N N   . ASN C 215 ? 1.8218 1.6321 1.6371 -0.0697 -0.2550 0.1201  215 ASN C N   
4757 C CA  . ASN C 215 ? 1.8060 1.6288 1.6105 -0.0713 -0.2558 0.1182  215 ASN C CA  
4758 C C   . ASN C 215 ? 1.8361 1.6691 1.6465 -0.0687 -0.2540 0.1236  215 ASN C C   
4759 O O   . ASN C 215 ? 1.7913 1.6430 1.6008 -0.0688 -0.2531 0.1289  215 ASN C O   
4760 C CB  . ASN C 215 ? 1.7656 1.6040 1.5661 -0.0735 -0.2559 0.1223  215 ASN C CB  
4761 C CG  . ASN C 215 ? 1.8508 1.6970 1.6369 -0.0768 -0.2572 0.1149  215 ASN C CG  
4762 O OD1 . ASN C 215 ? 1.9014 1.7427 1.6815 -0.0773 -0.2578 0.1080  215 ASN C OD1 
4763 N ND2 . ASN C 215 ? 1.8753 1.7342 1.6565 -0.0793 -0.2574 0.1162  215 ASN C ND2 
4764 N N   . THR C 216 ? 1.7364 1.5578 1.5530 -0.0663 -0.2533 0.1220  216 THR C N   
4765 C CA  . THR C 216 ? 1.6269 1.4557 1.4499 -0.0635 -0.2514 0.1267  216 THR C CA  
4766 C C   . THR C 216 ? 1.5698 1.3877 1.3847 -0.0637 -0.2530 0.1174  216 THR C C   
4767 O O   . THR C 216 ? 1.6356 1.4378 1.4530 -0.0626 -0.2531 0.1126  216 THR C O   
4768 C CB  . THR C 216 ? 1.5937 1.4207 1.4349 -0.0599 -0.2481 0.1349  216 THR C CB  
4769 O OG1 . THR C 216 ? 1.6309 1.4632 1.4801 -0.0600 -0.2466 0.1421  216 THR C OG1 
4770 C CG2 . THR C 216 ? 1.5411 1.3812 1.3903 -0.0569 -0.2456 0.1429  216 THR C CG2 
4771 N N   . ASP D 1   ? 1.2174 1.0059 1.0676 -0.0757 -0.3029 -0.0233 1   ASP D N   
4772 C CA  . ASP D 1   ? 1.1662 0.9685 1.0325 -0.0798 -0.3013 -0.0311 1   ASP D CA  
4773 C C   . ASP D 1   ? 1.1131 0.9340 0.9845 -0.0768 -0.2989 -0.0343 1   ASP D C   
4774 O O   . ASP D 1   ? 1.1272 0.9643 1.0127 -0.0798 -0.2973 -0.0420 1   ASP D O   
4775 C CB  . ASP D 1   ? 1.1582 0.9699 1.0335 -0.0844 -0.3036 -0.0365 1   ASP D CB  
4776 C CG  . ASP D 1   ? 1.3504 1.1676 1.2178 -0.0817 -0.3068 -0.0340 1   ASP D CG  
4777 O OD1 . ASP D 1   ? 1.2817 1.1062 1.1426 -0.0763 -0.3063 -0.0307 1   ASP D OD1 
4778 O OD2 . ASP D 1   ? 1.4349 1.2493 1.3031 -0.0848 -0.3096 -0.0350 1   ASP D OD2 
4779 N N   . ILE D 2   ? 1.0694 0.8884 0.9299 -0.0710 -0.2982 -0.0287 2   ILE D N   
4780 C CA  . ILE D 2   ? 1.0482 0.8840 0.9121 -0.0677 -0.2958 -0.0308 2   ILE D CA  
4781 C C   . ILE D 2   ? 1.0014 0.8350 0.8729 -0.0696 -0.2926 -0.0343 2   ILE D C   
4782 O O   . ILE D 2   ? 1.0330 0.8479 0.8998 -0.0701 -0.2918 -0.0306 2   ILE D O   
4783 C CB  . ILE D 2   ? 1.0914 0.9236 0.9420 -0.0608 -0.2955 -0.0229 2   ILE D CB  
4784 C CG1 . ILE D 2   ? 1.1065 0.9461 0.9526 -0.0584 -0.2979 -0.0199 2   ILE D CG1 
4785 C CG2 . ILE D 2   ? 0.9951 0.8414 0.8483 -0.0573 -0.2925 -0.0242 2   ILE D CG2 
4786 C CD1 . ILE D 2   ? 0.9928 0.8336 0.8290 -0.0513 -0.2966 -0.0124 2   ILE D CD1 
4787 N N   . VAL D 3   ? 0.9950 0.8485 0.8788 -0.0707 -0.2904 -0.0417 3   VAL D N   
4788 C CA  . VAL D 3   ? 0.9441 0.7982 0.8367 -0.0723 -0.2867 -0.0457 3   VAL D CA  
4789 C C   . VAL D 3   ? 0.9422 0.8088 0.8319 -0.0673 -0.2847 -0.0455 3   VAL D C   
4790 O O   . VAL D 3   ? 0.9830 0.8697 0.8743 -0.0653 -0.2851 -0.0478 3   VAL D O   
4791 C CB  . VAL D 3   ? 0.8844 0.7512 0.7959 -0.0784 -0.2849 -0.0557 3   VAL D CB  
4792 C CG1 . VAL D 3   ? 0.8715 0.7367 0.7928 -0.0799 -0.2806 -0.0593 3   VAL D CG1 
4793 C CG2 . VAL D 3   ? 0.8996 0.7556 0.8138 -0.0830 -0.2871 -0.0554 3   VAL D CG2 
4794 N N   . MET D 4   ? 0.9451 0.8006 0.8307 -0.0653 -0.2826 -0.0425 4   MET D N   
4795 C CA  . MET D 4   ? 0.9750 0.8396 0.8566 -0.0603 -0.2806 -0.0414 4   MET D CA  
4796 C C   . MET D 4   ? 0.9770 0.8437 0.8683 -0.0621 -0.2769 -0.0466 4   MET D C   
4797 O O   . MET D 4   ? 1.1157 0.9647 1.0047 -0.0628 -0.2759 -0.0436 4   MET D O   
4798 C CB  . MET D 4   ? 0.9680 0.8164 0.8329 -0.0552 -0.2815 -0.0315 4   MET D CB  
4799 C CG  . MET D 4   ? 0.9363 0.7861 0.7924 -0.0522 -0.2842 -0.0262 4   MET D CG  
4800 S SD  . MET D 4   ? 1.0671 0.9152 0.9099 -0.0444 -0.2830 -0.0175 4   MET D SD  
4801 C CE  . MET D 4   ? 0.9449 0.7683 0.7807 -0.0445 -0.2814 -0.0138 4   MET D CE  
4802 N N   . THR D 5   ? 0.9101 0.7994 0.8124 -0.0627 -0.2747 -0.0546 5   THR D N   
4803 C CA  . THR D 5   ? 0.9641 0.8585 0.8770 -0.0641 -0.2706 -0.0607 5   THR D CA  
4804 C C   . THR D 5   ? 0.9139 0.8150 0.8194 -0.0586 -0.2691 -0.0585 5   THR D C   
4805 O O   . THR D 5   ? 0.9716 0.8842 0.8698 -0.0545 -0.2705 -0.0556 5   THR D O   
4806 C CB  . THR D 5   ? 0.9490 0.8649 0.8808 -0.0691 -0.2683 -0.0724 5   THR D CB  
4807 O OG1 . THR D 5   ? 1.0101 0.9487 0.9417 -0.0676 -0.2698 -0.0752 5   THR D OG1 
4808 C CG2 . THR D 5   ? 0.9502 0.8569 0.8914 -0.0749 -0.2686 -0.0748 5   THR D CG2 
4809 N N   . GLN D 6   ? 0.9160 0.8103 0.8240 -0.0585 -0.2662 -0.0595 6   GLN D N   
4810 C CA  . GLN D 6   ? 0.8966 0.7956 0.7979 -0.0535 -0.2647 -0.0575 6   GLN D CA  
4811 C C   . GLN D 6   ? 0.9041 0.8223 0.8192 -0.0550 -0.2606 -0.0675 6   GLN D C   
4812 O O   . GLN D 6   ? 0.9200 0.8440 0.8507 -0.0601 -0.2583 -0.0757 6   GLN D O   
4813 C CB  . GLN D 6   ? 0.8529 0.7280 0.7432 -0.0512 -0.2647 -0.0496 6   GLN D CB  
4814 C CG  . GLN D 6   ? 0.8236 0.6791 0.7013 -0.0503 -0.2681 -0.0407 6   GLN D CG  
4815 C CD  . GLN D 6   ? 0.8537 0.6894 0.7200 -0.0476 -0.2678 -0.0334 6   GLN D CD  
4816 O OE1 . GLN D 6   ? 0.8228 0.6404 0.6818 -0.0483 -0.2696 -0.0278 6   GLN D OE1 
4817 N NE2 . GLN D 6   ? 0.8456 0.6856 0.7105 -0.0446 -0.2656 -0.0339 6   GLN D NE2 
4818 N N   . SER D 7   ? 0.8795 0.8076 0.7891 -0.0504 -0.2594 -0.0666 7   SER D N   
4819 C CA  . SER D 7   ? 0.8600 0.8080 0.7801 -0.0507 -0.2555 -0.0756 7   SER D CA  
4820 C C   . SER D 7   ? 0.8883 0.8297 0.7992 -0.0460 -0.2541 -0.0712 7   SER D C   
4821 O O   . SER D 7   ? 0.9804 0.9190 0.8773 -0.0407 -0.2560 -0.0630 7   SER D O   
4822 C CB  . SER D 7   ? 0.8845 0.8623 0.8088 -0.0499 -0.2557 -0.0808 7   SER D CB  
4823 O OG  . SER D 7   ? 0.9775 0.9759 0.9097 -0.0494 -0.2519 -0.0889 7   SER D OG  
4824 N N   . PRO D 8   ? 0.8440 0.7823 0.7628 -0.0476 -0.2507 -0.0761 8   PRO D N   
4825 C CA  . PRO D 8   ? 0.9280 0.8644 0.8636 -0.0534 -0.2476 -0.0841 8   PRO D CA  
4826 C C   . PRO D 8   ? 0.8974 0.8067 0.8303 -0.0552 -0.2487 -0.0775 8   PRO D C   
4827 O O   . PRO D 8   ? 0.9199 0.8132 0.8382 -0.0528 -0.2524 -0.0679 8   PRO D O   
4828 C CB  . PRO D 8   ? 1.0119 0.9567 0.9544 -0.0527 -0.2431 -0.0904 8   PRO D CB  
4829 C CG  . PRO D 8   ? 0.9604 0.9199 0.8926 -0.0473 -0.2439 -0.0885 8   PRO D CG  
4830 C CD  . PRO D 8   ? 0.9078 0.8523 0.8222 -0.0435 -0.2485 -0.0763 8   PRO D CD  
4831 N N   . LEU D 9   ? 0.9056 0.8105 0.8531 -0.0595 -0.2453 -0.0826 9   LEU D N   
4832 C CA  . LEU D 9   ? 0.8566 0.7374 0.8019 -0.0606 -0.2457 -0.0757 9   LEU D CA  
4833 C C   . LEU D 9   ? 0.8629 0.7316 0.8010 -0.0573 -0.2445 -0.0711 9   LEU D C   
4834 O O   . LEU D 9   ? 0.9090 0.7578 0.8376 -0.0562 -0.2464 -0.0625 9   LEU D O   
4835 C CB  . LEU D 9   ? 0.9261 0.8070 0.8911 -0.0663 -0.2422 -0.0818 9   LEU D CB  
4836 C CG  . LEU D 9   ? 1.0228 0.9015 0.9913 -0.0700 -0.2445 -0.0812 9   LEU D CG  
4837 C CD1 . LEU D 9   ? 0.8739 0.7322 0.8248 -0.0679 -0.2494 -0.0696 9   LEU D CD1 
4838 C CD2 . LEU D 9   ? 0.9124 0.8130 0.8840 -0.0709 -0.2457 -0.0880 9   LEU D CD2 
4839 N N   . SER D 10  ? 0.8635 0.7446 0.8059 -0.0557 -0.2414 -0.0769 10  SER D N   
4840 C CA  . SER D 10  ? 0.9060 0.7775 0.8415 -0.0524 -0.2402 -0.0732 10  SER D CA  
4841 C C   . SER D 10  ? 0.9862 0.8763 0.9213 -0.0496 -0.2385 -0.0789 10  SER D C   
4842 O O   . SER D 10  ? 1.0307 0.9418 0.9777 -0.0516 -0.2361 -0.0885 10  SER D O   
4843 C CB  . SER D 10  ? 0.8984 0.7605 0.8468 -0.0551 -0.2362 -0.0749 10  SER D CB  
4844 O OG  . SER D 10  ? 0.9371 0.7904 0.8785 -0.0518 -0.2353 -0.0713 10  SER D OG  
4845 N N   . LEU D 11  ? 1.0158 0.8987 0.9371 -0.0450 -0.2396 -0.0731 11  LEU D N   
4846 C CA  . LEU D 11  ? 1.0221 0.9213 0.9413 -0.0417 -0.2380 -0.0772 11  LEU D CA  
4847 C C   . LEU D 11  ? 1.0640 0.9496 0.9737 -0.0383 -0.2376 -0.0720 11  LEU D C   
4848 O O   . LEU D 11  ? 1.1195 0.9851 1.0179 -0.0369 -0.2402 -0.0629 11  LEU D O   
4849 C CB  . LEU D 11  ? 1.0285 0.9405 0.9375 -0.0385 -0.2409 -0.0744 11  LEU D CB  
4850 C CG  . LEU D 11  ? 1.0496 0.9454 0.9408 -0.0350 -0.2452 -0.0625 11  LEU D CG  
4851 C CD1 . LEU D 11  ? 1.0911 0.9832 0.9696 -0.0297 -0.2452 -0.0570 11  LEU D CD1 
4852 C CD2 . LEU D 11  ? 0.9673 0.8741 0.8558 -0.0345 -0.2478 -0.0610 11  LEU D CD2 
4853 N N   . SER D 12  ? 1.0625 0.9597 0.9771 -0.0371 -0.2343 -0.0782 12  SER D N   
4854 C CA  . SER D 12  ? 1.1595 1.0460 1.0662 -0.0339 -0.2336 -0.0746 12  SER D CA  
4855 C C   . SER D 12  ? 1.2084 1.1101 1.1070 -0.0295 -0.2335 -0.0754 12  SER D C   
4856 O O   . SER D 12  ? 1.2645 1.1881 1.1724 -0.0300 -0.2307 -0.0845 12  SER D O   
4857 C CB  . SER D 12  ? 1.2092 1.0939 1.1301 -0.0365 -0.2290 -0.0811 12  SER D CB  
4858 O OG  . SER D 12  ? 1.2904 1.1596 1.2030 -0.0340 -0.2291 -0.0755 12  SER D OG  
4859 N N   . VAL D 13  ? 1.2450 1.1360 1.1271 -0.0252 -0.2363 -0.0660 13  VAL D N   
4860 C CA  . VAL D 13  ? 1.3303 1.2337 1.2038 -0.0204 -0.2361 -0.0647 13  VAL D CA  
4861 C C   . VAL D 13  ? 1.4185 1.3107 1.2858 -0.0179 -0.2350 -0.0623 13  VAL D C   
4862 O O   . VAL D 13  ? 1.4039 1.2751 1.2676 -0.0188 -0.2359 -0.0577 13  VAL D O   
4863 C CB  . VAL D 13  ? 1.2460 1.1479 1.1066 -0.0169 -0.2394 -0.0556 13  VAL D CB  
4864 C CG1 . VAL D 13  ? 1.1706 1.0827 1.0373 -0.0195 -0.2408 -0.0577 13  VAL D CG1 
4865 C CG2 . VAL D 13  ? 1.2852 1.1608 1.1339 -0.0159 -0.2418 -0.0456 13  VAL D CG2 
4866 N N   . ALA D 14  ? 1.5904 1.4981 1.4565 -0.0149 -0.2330 -0.0658 14  ALA D N   
4867 C CA  . ALA D 14  ? 1.6023 1.5008 1.4612 -0.0120 -0.2322 -0.0633 14  ALA D CA  
4868 C C   . ALA D 14  ? 1.5987 1.4823 1.4412 -0.0081 -0.2350 -0.0517 14  ALA D C   
4869 O O   . ALA D 14  ? 1.5792 1.4671 1.4161 -0.0062 -0.2368 -0.0466 14  ALA D O   
4870 C CB  . ALA D 14  ? 1.5998 1.5204 1.4620 -0.0098 -0.2292 -0.0703 14  ALA D CB  
4871 N N   . PRO D 15  ? 1.4346 1.3009 1.2701 -0.0069 -0.2352 -0.0475 15  PRO D N   
4872 C CA  . PRO D 15  ? 1.3993 1.2517 1.2204 -0.0035 -0.2371 -0.0373 15  PRO D CA  
4873 C C   . PRO D 15  ? 1.3424 1.2094 1.1570 0.0015  -0.2364 -0.0343 15  PRO D C   
4874 O O   . PRO D 15  ? 1.3272 1.2035 1.1410 0.0040  -0.2344 -0.0370 15  PRO D O   
4875 C CB  . PRO D 15  ? 1.3591 1.1949 1.1766 -0.0037 -0.2367 -0.0360 15  PRO D CB  
4876 C CG  . PRO D 15  ? 1.3492 1.1964 1.1774 -0.0050 -0.2339 -0.0455 15  PRO D CG  
4877 C CD  . PRO D 15  ? 1.4043 1.2629 1.2451 -0.0087 -0.2333 -0.0519 15  PRO D CD  
4878 N N   . GLY D 16  ? 1.3183 1.1881 1.1286 0.0032  -0.2378 -0.0285 16  GLY D N   
4879 C CA  . GLY D 16  ? 1.2627 1.1472 1.0677 0.0084  -0.2368 -0.0242 16  GLY D CA  
4880 C C   . GLY D 16  ? 1.2132 1.1214 1.0248 0.0086  -0.2367 -0.0273 16  GLY D C   
4881 O O   . GLY D 16  ? 1.2623 1.1816 1.0694 0.0129  -0.2363 -0.0214 16  GLY D O   
4882 N N   . GLU D 17  ? 1.1996 1.1163 1.0223 0.0040  -0.2367 -0.0362 17  GLU D N   
4883 C CA  . GLU D 17  ? 1.2056 1.1464 1.0357 0.0035  -0.2366 -0.0405 17  GLU D CA  
4884 C C   . GLU D 17  ? 1.1263 1.0596 0.9542 0.0026  -0.2392 -0.0347 17  GLU D C   
4885 O O   . GLU D 17  ? 1.1738 1.0841 0.9942 0.0025  -0.2409 -0.0275 17  GLU D O   
4886 C CB  . GLU D 17  ? 1.2360 1.1894 1.0802 -0.0013 -0.2349 -0.0532 17  GLU D CB  
4887 C CG  . GLU D 17  ? 1.1506 1.1301 1.0000 0.0004  -0.2318 -0.0608 17  GLU D CG  
4888 C CD  . GLU D 17  ? 1.1166 1.1232 0.9658 0.0036  -0.2317 -0.0596 17  GLU D CD  
4889 O OE1 . GLU D 17  ? 1.0735 1.0902 0.9291 0.0010  -0.2327 -0.0622 17  GLU D OE1 
4890 O OE2 . GLU D 17  ? 1.0576 1.0760 0.9005 0.0087  -0.2304 -0.0558 17  GLU D OE2 
4891 N N   . ALA D 18  ? 1.0957 1.0493 0.9304 0.0016  -0.2395 -0.0385 18  ALA D N   
4892 C CA  . ALA D 18  ? 1.0761 1.0263 0.9089 0.0012  -0.2419 -0.0332 18  ALA D CA  
4893 C C   . ALA D 18  ? 1.0620 1.0091 0.9047 -0.0051 -0.2432 -0.0402 18  ALA D C   
4894 O O   . ALA D 18  ? 1.0627 1.0252 0.9171 -0.0085 -0.2416 -0.0505 18  ALA D O   
4895 C CB  . ALA D 18  ? 1.1171 1.0934 0.9500 0.0053  -0.2414 -0.0307 18  ALA D CB  
4896 N N   . ALA D 19  ? 1.0599 0.9872 0.8985 -0.0068 -0.2457 -0.0347 19  ALA D N   
4897 C CA  . ALA D 19  ? 0.9833 0.9072 0.8302 -0.0123 -0.2472 -0.0394 19  ALA D CA  
4898 C C   . ALA D 19  ? 0.9509 0.8834 0.7965 -0.0115 -0.2492 -0.0358 19  ALA D C   
4899 O O   . ALA D 19  ? 1.0816 1.0141 0.9181 -0.0067 -0.2497 -0.0273 19  ALA D O   
4900 C CB  . ALA D 19  ? 1.0429 0.9384 0.8866 -0.0152 -0.2485 -0.0362 19  ALA D CB  
4901 N N   . SER D 20  ? 0.9110 0.8509 0.7666 -0.0162 -0.2501 -0.0423 20  SER D N   
4902 C CA  . SER D 20  ? 0.9284 0.8799 0.7841 -0.0157 -0.2520 -0.0401 20  SER D CA  
4903 C C   . SER D 20  ? 0.9102 0.8538 0.7734 -0.0217 -0.2538 -0.0443 20  SER D C   
4904 O O   . SER D 20  ? 0.9365 0.8967 0.8120 -0.0256 -0.2531 -0.0533 20  SER D O   
4905 C CB  . SER D 20  ? 0.9495 0.9340 0.8114 -0.0138 -0.2505 -0.0452 20  SER D CB  
4906 O OG  . SER D 20  ? 0.9974 0.9893 0.8516 -0.0076 -0.2489 -0.0395 20  SER D OG  
4907 N N   . ILE D 21  ? 0.8741 0.7924 0.7301 -0.0226 -0.2559 -0.0376 21  ILE D N   
4908 C CA  . ILE D 21  ? 0.8751 0.7851 0.7364 -0.0276 -0.2578 -0.0398 21  ILE D CA  
4909 C C   . ILE D 21  ? 0.9177 0.8402 0.7783 -0.0268 -0.2599 -0.0379 21  ILE D C   
4910 O O   . ILE D 21  ? 1.0134 0.9392 0.8651 -0.0217 -0.2604 -0.0305 21  ILE D O   
4911 C CB  . ILE D 21  ? 0.8457 0.7264 0.6989 -0.0287 -0.2593 -0.0332 21  ILE D CB  
4912 C CG1 . ILE D 21  ? 0.8497 0.7193 0.7038 -0.0293 -0.2572 -0.0347 21  ILE D CG1 
4913 C CG2 . ILE D 21  ? 0.8607 0.7335 0.7195 -0.0338 -0.2612 -0.0351 21  ILE D CG2 
4914 C CD1 . ILE D 21  ? 0.8754 0.7344 0.7170 -0.0245 -0.2568 -0.0273 21  ILE D CD1 
4915 N N   . SER D 22  ? 0.8900 0.8203 0.7609 -0.0317 -0.2608 -0.0444 22  SER D N   
4916 C CA  . SER D 22  ? 0.8965 0.8403 0.7683 -0.0315 -0.2629 -0.0438 22  SER D CA  
4917 C C   . SER D 22  ? 0.8573 0.7849 0.7299 -0.0359 -0.2655 -0.0429 22  SER D C   
4918 O O   . SER D 22  ? 0.9466 0.8617 0.8252 -0.0404 -0.2651 -0.0466 22  SER D O   
4919 C CB  . SER D 22  ? 0.8936 0.8687 0.7784 -0.0334 -0.2614 -0.0539 22  SER D CB  
4920 O OG  . SER D 22  ? 0.8925 0.8800 0.7799 -0.0345 -0.2637 -0.0544 22  SER D OG  
4921 N N   . CYS D 23  ? 0.8217 0.7499 0.6885 -0.0342 -0.2681 -0.0375 23  CYS D N   
4922 C CA  . CYS D 23  ? 0.8450 0.7598 0.7119 -0.0380 -0.2708 -0.0365 23  CYS D CA  
4923 C C   . CYS D 23  ? 0.8878 0.8228 0.7596 -0.0387 -0.2725 -0.0391 23  CYS D C   
4924 O O   . CYS D 23  ? 0.9604 0.9136 0.8298 -0.0342 -0.2723 -0.0365 23  CYS D O   
4925 C CB  . CYS D 23  ? 0.9147 0.8046 0.7675 -0.0353 -0.2724 -0.0261 23  CYS D CB  
4926 S SG  . CYS D 23  ? 0.9624 0.8325 0.8139 -0.0401 -0.2755 -0.0247 23  CYS D SG  
4927 N N   . ARG D 24  ? 0.9154 0.8481 0.7948 -0.0443 -0.2741 -0.0440 24  ARG D N   
4928 C CA  . ARG D 24  ? 0.9091 0.8615 0.7951 -0.0461 -0.2758 -0.0480 24  ARG D CA  
4929 C C   . ARG D 24  ? 0.9328 0.8687 0.8179 -0.0500 -0.2788 -0.0466 24  ARG D C   
4930 O O   . ARG D 24  ? 1.0033 0.9236 0.8928 -0.0545 -0.2785 -0.0492 24  ARG D O   
4931 C CB  . ARG D 24  ? 0.8980 0.8751 0.8005 -0.0502 -0.2735 -0.0604 24  ARG D CB  
4932 C CG  . ARG D 24  ? 0.9868 0.9878 0.8907 -0.0462 -0.2710 -0.0627 24  ARG D CG  
4933 C CD  . ARG D 24  ? 0.9882 1.0020 0.9067 -0.0503 -0.2672 -0.0744 24  ARG D CD  
4934 N NE  . ARG D 24  ? 1.0251 1.0718 0.9560 -0.0527 -0.2662 -0.0843 24  ARG D NE  
4935 C CZ  . ARG D 24  ? 1.0325 1.1055 0.9651 -0.0494 -0.2642 -0.0871 24  ARG D CZ  
4936 N NH1 . ARG D 24  ? 0.9956 1.0655 0.9183 -0.0436 -0.2631 -0.0807 24  ARG D NH1 
4937 N NH2 . ARG D 24  ? 1.0102 1.1145 0.9551 -0.0522 -0.2633 -0.0968 24  ARG D NH2 
4938 N N   . SER D 25  ? 0.8772 0.8174 0.7572 -0.0482 -0.2815 -0.0422 25  SER D N   
4939 C CA  . SER D 25  ? 0.8877 0.8123 0.7649 -0.0511 -0.2846 -0.0398 25  SER D CA  
4940 C C   . SER D 25  ? 0.8583 0.8030 0.7449 -0.0545 -0.2864 -0.0459 25  SER D C   
4941 O O   . SER D 25  ? 0.8894 0.8600 0.7800 -0.0523 -0.2860 -0.0484 25  SER D O   
4942 C CB  . SER D 25  ? 0.9791 0.8870 0.8410 -0.0461 -0.2861 -0.0285 25  SER D CB  
4943 O OG  . SER D 25  ? 1.0070 0.9314 0.8668 -0.0424 -0.2873 -0.0252 25  SER D OG  
4944 N N   . THR D 26  ? 0.8924 0.8258 0.7826 -0.0597 -0.2884 -0.0484 26  THR D N   
4945 C CA  . THR D 26  ? 0.9646 0.9148 0.8637 -0.0635 -0.2904 -0.0543 26  THR D CA  
4946 C C   . THR D 26  ? 0.9778 0.9329 0.8678 -0.0594 -0.2934 -0.0474 26  THR D C   
4947 O O   . THR D 26  ? 0.9366 0.9136 0.8335 -0.0608 -0.2948 -0.0518 26  THR D O   
4948 C CB  . THR D 26  ? 0.9561 0.8916 0.8619 -0.0703 -0.2915 -0.0584 26  THR D CB  
4949 O OG1 . THR D 26  ? 1.0293 0.9417 0.9227 -0.0692 -0.2945 -0.0500 26  THR D OG1 
4950 C CG2 . THR D 26  ? 0.8612 0.7863 0.7743 -0.0734 -0.2882 -0.0623 26  THR D CG2 
4951 N N   . GLN D 27  ? 1.0124 0.9485 0.8882 -0.0545 -0.2941 -0.0369 27  GLN D N   
4952 C CA  . GLN D 27  ? 1.1050 1.0438 0.9726 -0.0501 -0.2962 -0.0295 27  GLN D CA  
4953 C C   . GLN D 27  ? 1.1453 1.0843 1.0034 -0.0424 -0.2940 -0.0207 27  GLN D C   
4954 O O   . GLN D 27  ? 1.1304 1.0582 0.9850 -0.0408 -0.2916 -0.0190 27  GLN D O   
4955 C CB  . GLN D 27  ? 1.1096 1.0237 0.9697 -0.0520 -0.2989 -0.0251 27  GLN D CB  
4956 C CG  . GLN D 27  ? 1.1467 1.0601 1.0158 -0.0594 -0.3012 -0.0329 27  GLN D CG  
4957 C CD  . GLN D 27  ? 1.2847 1.1757 1.1459 -0.0609 -0.3041 -0.0283 27  GLN D CD  
4958 O OE1 . GLN D 27  ? 1.2645 1.1460 1.1146 -0.0563 -0.3047 -0.0201 27  GLN D OE1 
4959 N NE2 . GLN D 27  ? 1.3064 1.1891 1.1739 -0.0674 -0.3053 -0.0337 27  GLN D NE2 
4960 N N   . SER D 28  ? 1.2169 1.1694 1.0718 -0.0375 -0.2945 -0.0150 28  SER D N   
4961 C CA  . SER D 28  ? 1.2957 1.2530 1.1440 -0.0297 -0.2918 -0.0064 28  SER D CA  
4962 C C   . SER D 28  ? 1.3223 1.2496 1.1587 -0.0268 -0.2908 0.0025  28  SER D C   
4963 O O   . SER D 28  ? 1.3021 1.2142 1.1332 -0.0273 -0.2926 0.0063  28  SER D O   
4964 C CB  . SER D 28  ? 1.2787 1.2603 1.1283 -0.0252 -0.2923 -0.0021 28  SER D CB  
4965 O OG  . SER D 28  ? 1.3707 1.3447 1.2182 -0.0266 -0.2953 0.0001  28  SER D OG  
4966 N N   . LEU D 29  ? 1.3179 1.2375 1.1503 -0.0239 -0.2878 0.0052  29  LEU D N   
4967 C CA  . LEU D 29  ? 1.3017 1.1944 1.1238 -0.0214 -0.2862 0.0126  29  LEU D CA  
4968 C C   . LEU D 29  ? 1.3223 1.2214 1.1397 -0.0134 -0.2831 0.0224  29  LEU D C   
4969 O O   . LEU D 29  ? 1.2466 1.1471 1.0623 -0.0097 -0.2800 0.0252  29  LEU D O   
4970 C CB  . LEU D 29  ? 1.1705 1.0496 0.9918 -0.0239 -0.2847 0.0092  29  LEU D CB  
4971 C CG  . LEU D 29  ? 1.0606 0.9360 0.8887 -0.0312 -0.2864 -0.0002 29  LEU D CG  
4972 C CD1 . LEU D 29  ? 0.8789 0.7443 0.7062 -0.0317 -0.2842 -0.0017 29  LEU D CD1 
4973 C CD2 . LEU D 29  ? 1.0921 0.9487 0.9177 -0.0357 -0.2892 -0.0005 29  LEU D CD2 
4974 N N   . LEU D 30  ? 1.4487 1.3518 1.2648 -0.0105 -0.2837 0.0280  30  LEU D N   
4975 C CA  . LEU D 30  ? 1.4573 1.3684 1.2708 -0.0025 -0.2803 0.0382  30  LEU D CA  
4976 C C   . LEU D 30  ? 1.4738 1.3714 1.2828 -0.0004 -0.2803 0.0451  30  LEU D C   
4977 O O   . LEU D 30  ? 1.4785 1.3710 1.2879 -0.0047 -0.2838 0.0416  30  LEU D O   
4978 C CB  . LEU D 30  ? 1.4450 1.3911 1.2658 0.0009  -0.2800 0.0380  30  LEU D CB  
4979 C CG  . LEU D 30  ? 1.4657 1.4334 1.2945 -0.0037 -0.2839 0.0298  30  LEU D CG  
4980 C CD1 . LEU D 30  ? 1.4833 1.4478 1.3111 -0.0040 -0.2864 0.0330  30  LEU D CD1 
4981 C CD2 . LEU D 30  ? 1.4525 1.4561 1.2885 -0.0006 -0.2828 0.0285  30  LEU D CD2 
4982 N N   . ASN D 31  ? 1.2766 1.1683 1.0818 0.0061  -0.2759 0.0550  31  ASN D N   
4983 C CA  . ASN D 31  ? 1.2199 1.0992 1.0217 0.0092  -0.2744 0.0626  31  ASN D CA  
4984 C C   . ASN D 31  ? 1.3186 1.2217 1.1248 0.0166  -0.2720 0.0712  31  ASN D C   
4985 O O   . ASN D 31  ? 1.3410 1.2714 1.1526 0.0185  -0.2724 0.0701  31  ASN D O   
4986 C CB  . ASN D 31  ? 1.1860 1.0385 0.9816 0.0108  -0.2702 0.0672  31  ASN D CB  
4987 C CG  . ASN D 31  ? 1.2585 1.0923 1.0506 0.0111  -0.2693 0.0713  31  ASN D CG  
4988 O OD1 . ASN D 31  ? 1.2762 1.1119 1.0690 0.0086  -0.2728 0.0693  31  ASN D OD1 
4989 N ND2 . ASN D 31  ? 1.2292 1.0447 1.0178 0.0140  -0.2642 0.0768  31  ASN D ND2 
4990 N N   . ARG D 32  ? 1.2937 1.1878 1.0983 0.0211  -0.2691 0.0799  32  ARG D N   
4991 C CA  . ARG D 32  ? 1.2018 1.1200 1.0115 0.0280  -0.2672 0.0884  32  ARG D CA  
4992 C C   . ARG D 32  ? 1.1175 1.0474 0.9293 0.0351  -0.2616 0.0962  32  ARG D C   
4993 O O   . ARG D 32  ? 1.2198 1.1790 1.0366 0.0384  -0.2616 0.0976  32  ARG D O   
4994 C CB  . ARG D 32  ? 1.1693 1.0762 0.9781 0.0305  -0.2658 0.0953  32  ARG D CB  
4995 C CG  . ARG D 32  ? 1.2560 1.1651 1.0651 0.0247  -0.2720 0.0883  32  ARG D CG  
4996 C CD  . ARG D 32  ? 1.4154 1.3488 1.2288 0.0208  -0.2763 0.0796  32  ARG D CD  
4997 N NE  . ARG D 32  ? 1.5148 1.4613 1.3317 0.0159  -0.2819 0.0726  32  ARG D NE  
4998 C CZ  . ARG D 32  ? 1.4879 1.4549 1.3098 0.0118  -0.2852 0.0638  32  ARG D CZ  
4999 N NH1 . ARG D 32  ? 1.4737 1.4461 1.2967 0.0113  -0.2838 0.0600  32  ARG D NH1 
5000 N NH2 . ARG D 32  ? 1.5390 1.5212 1.3655 0.0079  -0.2897 0.0580  32  ARG D NH2 
5001 N N   . ASN D 33  ? 1.1010 1.0088 0.9092 0.0374  -0.2567 0.1010  33  ASN D N   
5002 C CA  . ASN D 33  ? 1.1092 1.0223 0.9180 0.0416  -0.2524 0.1047  33  ASN D CA  
5003 C C   . ASN D 33  ? 1.0970 1.0176 0.9052 0.0363  -0.2563 0.0941  33  ASN D C   
5004 O O   . ASN D 33  ? 1.1475 1.0563 0.9532 0.0287  -0.2609 0.0842  33  ASN D O   
5005 C CB  . ASN D 33  ? 1.1368 1.0212 0.9418 0.0430  -0.2470 0.1091  33  ASN D CB  
5006 C CG  . ASN D 33  ? 1.0937 0.9816 0.8993 0.0474  -0.2422 0.1134  33  ASN D CG  
5007 O OD1 . ASN D 33  ? 1.0875 0.9781 0.8913 0.0441  -0.2444 0.1065  33  ASN D OD1 
5008 N ND2 . ASN D 33  ? 0.9966 0.8841 0.8055 0.0549  -0.2352 0.1250  33  ASN D ND2 
5009 N N   . GLY D 34  ? 1.0640 1.0046 0.8750 0.0403  -0.2541 0.0963  34  GLY D N   
5010 C CA  . GLY D 34  ? 1.0960 1.0471 0.9078 0.0358  -0.2571 0.0864  34  GLY D CA  
5011 C C   . GLY D 34  ? 1.1267 1.0525 0.9334 0.0306  -0.2576 0.0797  34  GLY D C   
5012 O O   . GLY D 34  ? 1.1256 1.0568 0.9324 0.0307  -0.2566 0.0769  34  GLY D O   
5013 N N   . ASP D 35  ? 1.1650 1.0641 0.9672 0.0259  -0.2593 0.0769  35  ASP D N   
5014 C CA  . ASP D 35  ? 1.0641 0.9398 0.8617 0.0207  -0.2599 0.0708  35  ASP D CA  
5015 C C   . ASP D 35  ? 1.0792 0.9538 0.8778 0.0127  -0.2656 0.0598  35  ASP D C   
5016 O O   . ASP D 35  ? 1.0857 0.9587 0.8849 0.0098  -0.2687 0.0579  35  ASP D O   
5017 C CB  . ASP D 35  ? 1.0713 0.9185 0.8636 0.0210  -0.2570 0.0754  35  ASP D CB  
5018 C CG  . ASP D 35  ? 1.1146 0.9542 0.9062 0.0194  -0.2589 0.0763  35  ASP D CG  
5019 O OD1 . ASP D 35  ? 1.0623 0.9126 0.8569 0.0246  -0.2568 0.0837  35  ASP D OD1 
5020 O OD2 . ASP D 35  ? 1.2137 1.0368 1.0021 0.0130  -0.2622 0.0698  35  ASP D OD2 
5021 N N   . ASN D 36  ? 1.0887 0.9647 0.8882 0.0093  -0.2667 0.0527  36  ASN D N   
5022 C CA  . ASN D 36  ? 1.0466 0.9230 0.8491 0.0019  -0.2711 0.0423  36  ASN D CA  
5023 C C   . ASN D 36  ? 0.9932 0.8417 0.7906 -0.0030 -0.2718 0.0391  36  ASN D C   
5024 O O   . ASN D 36  ? 0.9482 0.7856 0.7420 -0.0018 -0.2692 0.0406  36  ASN D O   
5025 C CB  . ASN D 36  ? 1.0106 0.9091 0.8192 0.0013  -0.2713 0.0360  36  ASN D CB  
5026 C CG  . ASN D 36  ? 1.0909 1.0206 0.9052 0.0055  -0.2709 0.0382  36  ASN D CG  
5027 O OD1 . ASN D 36  ? 1.1151 1.0557 0.9328 0.0043  -0.2734 0.0371  36  ASN D OD1 
5028 N ND2 . ASN D 36  ? 1.1202 1.0654 0.9355 0.0105  -0.2678 0.0413  36  ASN D ND2 
5029 N N   . TYR D 37  ? 1.0163 0.8547 0.8136 -0.0084 -0.2752 0.0349  37  TYR D N   
5030 C CA  . TYR D 37  ? 0.9666 0.7800 0.7591 -0.0130 -0.2759 0.0325  37  TYR D CA  
5031 C C   . TYR D 37  ? 0.8961 0.7111 0.6926 -0.0176 -0.2772 0.0248  37  TYR D C   
5032 O O   . TYR D 37  ? 0.9135 0.7340 0.7156 -0.0225 -0.2801 0.0182  37  TYR D O   
5033 C CB  . TYR D 37  ? 0.9907 0.7936 0.7816 -0.0166 -0.2788 0.0316  37  TYR D CB  
5034 C CG  . TYR D 37  ? 1.0239 0.8205 0.8104 -0.0122 -0.2768 0.0394  37  TYR D CG  
5035 C CD1 . TYR D 37  ? 1.0503 0.8322 0.8314 -0.0087 -0.2727 0.0452  37  TYR D CD1 
5036 C CD2 . TYR D 37  ? 1.0540 0.8601 0.8428 -0.0115 -0.2788 0.0408  37  TYR D CD2 
5037 C CE1 . TYR D 37  ? 1.0779 0.8540 0.8567 -0.0047 -0.2699 0.0521  37  TYR D CE1 
5038 C CE2 . TYR D 37  ? 1.1104 0.9108 0.8962 -0.0072 -0.2765 0.0481  37  TYR D CE2 
5039 C CZ  . TYR D 37  ? 1.1224 0.9077 0.9036 -0.0038 -0.2718 0.0538  37  TYR D CZ  
5040 O OH  . TYR D 37  ? 1.0868 0.8664 0.8665 0.0004  -0.2687 0.0609  37  TYR D OH  
5041 N N   . LEU D 38  ? 0.8138 0.6235 0.6080 -0.0159 -0.2746 0.0257  38  LEU D N   
5042 C CA  . LEU D 38  ? 0.8107 0.6214 0.6088 -0.0195 -0.2750 0.0192  38  LEU D CA  
5043 C C   . LEU D 38  ? 0.8168 0.6149 0.6096 -0.0176 -0.2721 0.0220  38  LEU D C   
5044 O O   . LEU D 38  ? 0.8546 0.6579 0.6451 -0.0123 -0.2692 0.0269  38  LEU D O   
5045 C CB  . LEU D 38  ? 0.8034 0.6400 0.6101 -0.0190 -0.2751 0.0144  38  LEU D CB  
5046 C CG  . LEU D 38  ? 0.8184 0.6589 0.6315 -0.0228 -0.2751 0.0066  38  LEU D CG  
5047 C CD1 . LEU D 38  ? 0.8699 0.7280 0.6937 -0.0270 -0.2771 -0.0014 38  LEU D CD1 
5048 C CD2 . LEU D 38  ? 0.8226 0.6727 0.6354 -0.0186 -0.2721 0.0076  38  LEU D CD2 
5049 N N   . GLU D 39  ? 0.8207 0.6030 0.6119 -0.0218 -0.2728 0.0192  39  GLU D N   
5050 C CA  . GLU D 39  ? 0.9116 0.6817 0.6978 -0.0207 -0.2704 0.0212  39  GLU D CA  
5051 C C   . GLU D 39  ? 0.9044 0.6780 0.6957 -0.0235 -0.2706 0.0154  39  GLU D C   
5052 O O   . GLU D 39  ? 0.8546 0.6300 0.6519 -0.0282 -0.2727 0.0101  39  GLU D O   
5053 C CB  . GLU D 39  ? 0.9106 0.6586 0.6898 -0.0227 -0.2703 0.0239  39  GLU D CB  
5054 C CG  . GLU D 39  ? 0.9020 0.6441 0.6760 -0.0192 -0.2685 0.0300  39  GLU D CG  
5055 C CD  . GLU D 39  ? 0.9267 0.6627 0.6998 -0.0221 -0.2709 0.0297  39  GLU D CD  
5056 O OE1 . GLU D 39  ? 0.9068 0.6393 0.6819 -0.0272 -0.2739 0.0251  39  GLU D OE1 
5057 O OE2 . GLU D 39  ? 0.9335 0.6683 0.7043 -0.0191 -0.2696 0.0342  39  GLU D OE2 
5058 N N   . TRP D 40  ? 0.9959 0.7705 0.7856 -0.0207 -0.2681 0.0165  40  TRP D N   
5059 C CA  . TRP D 40  ? 0.9863 0.7641 0.7807 -0.0227 -0.2678 0.0114  40  TRP D CA  
5060 C C   . TRP D 40  ? 1.0199 0.7789 0.8090 -0.0243 -0.2670 0.0130  40  TRP D C   
5061 O O   . TRP D 40  ? 1.0114 0.7612 0.7933 -0.0214 -0.2651 0.0178  40  TRP D O   
5062 C CB  . TRP D 40  ? 0.9983 0.7927 0.7952 -0.0186 -0.2656 0.0109  40  TRP D CB  
5063 C CG  . TRP D 40  ? 0.9987 0.8157 0.8038 -0.0186 -0.2664 0.0064  40  TRP D CG  
5064 C CD1 . TRP D 40  ? 1.0219 0.8538 0.8272 -0.0150 -0.2663 0.0093  40  TRP D CD1 
5065 C CD2 . TRP D 40  ? 0.9991 0.8276 0.8144 -0.0226 -0.2671 -0.0019 40  TRP D CD2 
5066 N NE1 . TRP D 40  ? 0.9795 0.8325 0.7941 -0.0166 -0.2671 0.0028  40  TRP D NE1 
5067 C CE2 . TRP D 40  ? 0.9986 0.8495 0.8197 -0.0215 -0.2675 -0.0045 40  TRP D CE2 
5068 C CE3 . TRP D 40  ? 0.9923 0.8148 0.8133 -0.0270 -0.2670 -0.0074 40  TRP D CE3 
5069 C CZ2 . TRP D 40  ? 1.0312 0.8988 0.8639 -0.0250 -0.2677 -0.0134 40  TRP D CZ2 
5070 C CZ3 . TRP D 40  ? 1.0518 0.8897 0.8846 -0.0302 -0.2669 -0.0156 40  TRP D CZ3 
5071 C CH2 . TRP D 40  ? 1.0456 0.9058 0.8843 -0.0294 -0.2671 -0.0190 40  TRP D CH2 
5072 N N   . TYR D 41  ? 1.0165 0.7708 0.8100 -0.0288 -0.2682 0.0089  41  TYR D N   
5073 C CA  . TYR D 41  ? 0.8605 0.5990 0.6498 -0.0307 -0.2678 0.0102  41  TYR D CA  
5074 C C   . TYR D 41  ? 0.8236 0.5662 0.6187 -0.0317 -0.2667 0.0064  41  TYR D C   
5075 O O   . TYR D 41  ? 0.9312 0.6868 0.7355 -0.0328 -0.2667 0.0013  41  TYR D O   
5076 C CB  . TYR D 41  ? 0.8265 0.5542 0.6154 -0.0351 -0.2698 0.0102  41  TYR D CB  
5077 C CG  . TYR D 41  ? 0.8727 0.5940 0.6553 -0.0345 -0.2706 0.0139  41  TYR D CG  
5078 C CD1 . TYR D 41  ? 0.8665 0.5748 0.6404 -0.0333 -0.2693 0.0181  41  TYR D CD1 
5079 C CD2 . TYR D 41  ? 0.8659 0.5947 0.6518 -0.0351 -0.2725 0.0128  41  TYR D CD2 
5080 C CE1 . TYR D 41  ? 0.8404 0.5426 0.6094 -0.0327 -0.2694 0.0210  41  TYR D CE1 
5081 C CE2 . TYR D 41  ? 0.8938 0.6164 0.6741 -0.0343 -0.2730 0.0162  41  TYR D CE2 
5082 C CZ  . TYR D 41  ? 0.8458 0.5550 0.6179 -0.0331 -0.2713 0.0202  41  TYR D CZ  
5083 O OH  . TYR D 41  ? 0.8438 0.5468 0.6113 -0.0323 -0.2713 0.0232  41  TYR D OH  
5084 N N   . LEU D 42  ? 0.8280 0.5601 0.6183 -0.0313 -0.2655 0.0084  42  LEU D N   
5085 C CA  . LEU D 42  ? 0.9003 0.6343 0.6954 -0.0320 -0.2643 0.0055  42  LEU D CA  
5086 C C   . LEU D 42  ? 1.0645 0.7850 0.8578 -0.0352 -0.2647 0.0071  42  LEU D C   
5087 O O   . LEU D 42  ? 1.0521 0.7617 0.8369 -0.0345 -0.2643 0.0108  42  LEU D O   
5088 C CB  . LEU D 42  ? 0.8911 0.6281 0.6821 -0.0278 -0.2622 0.0067  42  LEU D CB  
5089 C CG  . LEU D 42  ? 0.9693 0.7033 0.7619 -0.0282 -0.2608 0.0053  42  LEU D CG  
5090 C CD1 . LEU D 42  ? 1.0760 0.8202 0.8804 -0.0304 -0.2605 -0.0007 42  LEU D CD1 
5091 C CD2 . LEU D 42  ? 1.0395 0.7752 0.8267 -0.0238 -0.2588 0.0071  42  LEU D CD2 
5092 N N   . ARG D 43  ? 1.0978 0.8198 0.8998 -0.0387 -0.2652 0.0043  43  ARG D N   
5093 C CA  . ARG D 43  ? 1.1216 0.8337 0.9237 -0.0413 -0.2652 0.0061  43  ARG D CA  
5094 C C   . ARG D 43  ? 1.1444 0.8590 0.9507 -0.0404 -0.2631 0.0046  43  ARG D C   
5095 O O   . ARG D 43  ? 1.1781 0.9016 0.9952 -0.0412 -0.2620 0.0003  43  ARG D O   
5096 C CB  . ARG D 43  ? 1.1425 0.8547 0.9525 -0.0453 -0.2662 0.0051  43  ARG D CB  
5097 C CG  . ARG D 43  ? 1.1929 0.8992 1.0065 -0.0476 -0.2655 0.0069  43  ARG D CG  
5098 C CD  . ARG D 43  ? 1.2276 0.9328 1.0481 -0.0514 -0.2663 0.0074  43  ARG D CD  
5099 N NE  . ARG D 43  ? 1.3050 1.0075 1.1316 -0.0530 -0.2648 0.0095  43  ARG D NE  
5100 C CZ  . ARG D 43  ? 1.3765 1.0849 1.2152 -0.0533 -0.2623 0.0070  43  ARG D CZ  
5101 N NH1 . ARG D 43  ? 1.2327 0.9506 1.0789 -0.0525 -0.2610 0.0015  43  ARG D NH1 
5102 N NH2 . ARG D 43  ? 1.4309 1.1365 1.2749 -0.0544 -0.2608 0.0102  43  ARG D NH2 
5103 N N   . ARG D 44  ? 1.0731 0.7802 0.8714 -0.0388 -0.2625 0.0075  44  ARG D N   
5104 C CA  . ARG D 44  ? 1.1401 0.8480 0.9418 -0.0382 -0.2608 0.0066  44  ARG D CA  
5105 C C   . ARG D 44  ? 1.2205 0.9258 1.0299 -0.0415 -0.2605 0.0071  44  ARG D C   
5106 O O   . ARG D 44  ? 1.2553 0.9560 1.0642 -0.0440 -0.2618 0.0095  44  ARG D O   
5107 C CB  . ARG D 44  ? 1.1821 0.8822 0.9733 -0.0361 -0.2602 0.0098  44  ARG D CB  
5108 C CG  . ARG D 44  ? 1.1747 0.8786 0.9607 -0.0322 -0.2593 0.0094  44  ARG D CG  
5109 C CD  . ARG D 44  ? 1.2307 0.9292 1.0106 -0.0303 -0.2579 0.0111  44  ARG D CD  
5110 N NE  . ARG D 44  ? 1.3110 0.9994 1.0814 -0.0303 -0.2579 0.0148  44  ARG D NE  
5111 C CZ  . ARG D 44  ? 1.4080 1.0947 1.1721 -0.0274 -0.2566 0.0166  44  ARG D CZ  
5112 N NH1 . ARG D 44  ? 1.3789 1.0737 1.1441 -0.0238 -0.2554 0.0157  44  ARG D NH1 
5113 N NH2 . ARG D 44  ? 1.5036 1.1809 1.2608 -0.0280 -0.2559 0.0192  44  ARG D NH2 
5114 N N   . PRO D 45  ? 1.2285 0.9375 1.0458 -0.0413 -0.2585 0.0053  45  PRO D N   
5115 C CA  . PRO D 45  ? 1.2355 0.9423 1.0611 -0.0438 -0.2576 0.0070  45  PRO D CA  
5116 C C   . PRO D 45  ? 1.2371 0.9347 1.0541 -0.0444 -0.2585 0.0125  45  PRO D C   
5117 O O   . PRO D 45  ? 1.2274 0.9217 1.0375 -0.0426 -0.2582 0.0137  45  PRO D O   
5118 C CB  . PRO D 45  ? 1.2756 0.9886 1.1109 -0.0428 -0.2548 0.0035  45  PRO D CB  
5119 C CG  . PRO D 45  ? 1.2353 0.9494 1.0619 -0.0394 -0.2548 0.0021  45  PRO D CG  
5120 C CD  . PRO D 45  ? 1.2082 0.9237 1.0277 -0.0386 -0.2567 0.0017  45  PRO D CD  
5121 N N   . GLY D 46  ? 1.2444 0.9386 1.0619 -0.0470 -0.2596 0.0156  46  GLY D N   
5122 C CA  . GLY D 46  ? 1.2478 0.9357 1.0579 -0.0480 -0.2604 0.0205  46  GLY D CA  
5123 C C   . GLY D 46  ? 1.1943 0.8764 0.9922 -0.0484 -0.2623 0.0217  46  GLY D C   
5124 O O   . GLY D 46  ? 1.1497 0.8286 0.9443 -0.0505 -0.2633 0.0248  46  GLY D O   
5125 N N   . ARG D 47  ? 1.1849 0.8665 0.9767 -0.0462 -0.2626 0.0194  47  ARG D N   
5126 C CA  . ARG D 47  ? 1.1698 0.8458 0.9512 -0.0462 -0.2637 0.0204  47  ARG D CA  
5127 C C   . ARG D 47  ? 1.1701 0.8474 0.9534 -0.0474 -0.2651 0.0194  47  ARG D C   
5128 O O   . ARG D 47  ? 1.1995 0.8827 0.9920 -0.0481 -0.2653 0.0174  47  ARG D O   
5129 C CB  . ARG D 47  ? 1.1552 0.8300 0.9300 -0.0430 -0.2626 0.0194  47  ARG D CB  
5130 C CG  . ARG D 47  ? 1.3181 0.9852 1.0824 -0.0431 -0.2623 0.0211  47  ARG D CG  
5131 C CD  . ARG D 47  ? 1.4892 1.1547 1.2488 -0.0402 -0.2604 0.0209  47  ARG D CD  
5132 N NE  . ARG D 47  ? 1.5312 1.1945 1.2891 -0.0411 -0.2597 0.0218  47  ARG D NE  
5133 C CZ  . ARG D 47  ? 1.5301 1.1961 1.2906 -0.0394 -0.2589 0.0211  47  ARG D CZ  
5134 N NH1 . ARG D 47  ? 1.4895 1.1610 1.2545 -0.0369 -0.2585 0.0191  47  ARG D NH1 
5135 N NH2 . ARG D 47  ? 1.5469 1.2110 1.3057 -0.0405 -0.2585 0.0221  47  ARG D NH2 
5136 N N   . SER D 48  ? 1.0906 0.7625 0.8655 -0.0476 -0.2659 0.0205  48  SER D N   
5137 C CA  . SER D 48  ? 1.0565 0.7286 0.8316 -0.0486 -0.2674 0.0199  48  SER D CA  
5138 C C   . SER D 48  ? 1.0744 0.7517 0.8505 -0.0457 -0.2672 0.0178  48  SER D C   
5139 O O   . SER D 48  ? 1.0966 0.7766 0.8719 -0.0428 -0.2658 0.0171  48  SER D O   
5140 C CB  . SER D 48  ? 1.0829 0.7472 0.8490 -0.0500 -0.2678 0.0218  48  SER D CB  
5141 O OG  . SER D 48  ? 1.2098 0.8697 0.9687 -0.0483 -0.2660 0.0224  48  SER D OG  
5142 N N   . PRO D 49  ? 1.0253 0.7052 0.8032 -0.0463 -0.2686 0.0168  49  PRO D N   
5143 C CA  . PRO D 49  ? 0.9771 0.6639 0.7557 -0.0433 -0.2684 0.0153  49  PRO D CA  
5144 C C   . PRO D 49  ? 1.0364 0.7189 0.8063 -0.0399 -0.2668 0.0176  49  PRO D C   
5145 O O   . PRO D 49  ? 1.0496 0.7228 0.8126 -0.0406 -0.2661 0.0198  49  PRO D O   
5146 C CB  . PRO D 49  ? 0.9226 0.6113 0.7036 -0.0451 -0.2704 0.0146  49  PRO D CB  
5147 C CG  . PRO D 49  ? 0.9538 0.6405 0.7403 -0.0491 -0.2714 0.0143  49  PRO D CG  
5148 C CD  . PRO D 49  ? 1.0218 0.7007 0.8031 -0.0497 -0.2704 0.0169  49  PRO D CD  
5149 N N   . GLN D 50  ? 1.0234 0.7139 0.7946 -0.0363 -0.2658 0.0170  50  GLN D N   
5150 C CA  . GLN D 50  ? 0.9585 0.6470 0.7236 -0.0324 -0.2636 0.0196  50  GLN D CA  
5151 C C   . GLN D 50  ? 0.9078 0.6053 0.6743 -0.0294 -0.2635 0.0203  50  GLN D C   
5152 O O   . GLN D 50  ? 0.9853 0.6947 0.7584 -0.0293 -0.2646 0.0175  50  GLN D O   
5153 C CB  . GLN D 50  ? 0.9404 0.6313 0.7057 -0.0303 -0.2618 0.0192  50  GLN D CB  
5154 C CG  . GLN D 50  ? 0.9737 0.6658 0.7349 -0.0257 -0.2591 0.0218  50  GLN D CG  
5155 C CD  . GLN D 50  ? 1.0478 0.7404 0.8084 -0.0241 -0.2575 0.0213  50  GLN D CD  
5156 O OE1 . GLN D 50  ? 1.0020 0.6929 0.7649 -0.0266 -0.2583 0.0192  50  GLN D OE1 
5157 N NE2 . GLN D 50  ? 1.1928 0.8881 0.9509 -0.0199 -0.2550 0.0236  50  GLN D NE2 
5158 N N   . LEU D 51  ? 0.9217 0.6144 0.6829 -0.0270 -0.2619 0.0238  51  LEU D N   
5159 C CA  . LEU D 51  ? 0.9629 0.6645 0.7254 -0.0236 -0.2615 0.0257  51  LEU D CA  
5160 C C   . LEU D 51  ? 0.9950 0.7058 0.7582 -0.0187 -0.2590 0.0273  51  LEU D C   
5161 O O   . LEU D 51  ? 0.9458 0.6501 0.7050 -0.0167 -0.2563 0.0298  51  LEU D O   
5162 C CB  . LEU D 51  ? 0.9658 0.6583 0.7236 -0.0230 -0.2603 0.0292  51  LEU D CB  
5163 C CG  . LEU D 51  ? 0.8696 0.5705 0.6284 -0.0185 -0.2589 0.0328  51  LEU D CG  
5164 C CD1 . LEU D 51  ? 0.9355 0.6492 0.6996 -0.0193 -0.2621 0.0304  51  LEU D CD1 
5165 C CD2 . LEU D 51  ? 0.9305 0.6205 0.6851 -0.0176 -0.2565 0.0365  51  LEU D CD2 
5166 N N   . LEU D 52  ? 1.0204 0.7472 0.7889 -0.0169 -0.2598 0.0258  52  LEU D N   
5167 C CA  . LEU D 52  ? 0.9953 0.7343 0.7651 -0.0122 -0.2576 0.0272  52  LEU D CA  
5168 C C   . LEU D 52  ? 0.9298 0.6784 0.6999 -0.0077 -0.2562 0.0318  52  LEU D C   
5169 O O   . LEU D 52  ? 0.9777 0.7276 0.7455 -0.0030 -0.2529 0.0367  52  LEU D O   
5170 C CB  . LEU D 52  ? 0.9062 0.6592 0.6828 -0.0134 -0.2589 0.0215  52  LEU D CB  
5171 C CG  . LEU D 52  ? 0.8741 0.6209 0.6521 -0.0166 -0.2594 0.0175  52  LEU D CG  
5172 C CD1 . LEU D 52  ? 0.9419 0.7048 0.7282 -0.0171 -0.2597 0.0117  52  LEU D CD1 
5173 C CD2 . LEU D 52  ? 0.9778 0.7151 0.7499 -0.0144 -0.2569 0.0206  52  LEU D CD2 
5174 N N   . ILE D 53  ? 0.8810 0.6371 0.6543 -0.0088 -0.2585 0.0307  53  ILE D N   
5175 C CA  . ILE D 53  ? 0.8468 0.6148 0.6213 -0.0044 -0.2574 0.0351  53  ILE D CA  
5176 C C   . ILE D 53  ? 0.8499 0.6131 0.6244 -0.0068 -0.2596 0.0354  53  ILE D C   
5177 O O   . ILE D 53  ? 1.0345 0.7952 0.8111 -0.0118 -0.2628 0.0304  53  ILE D O   
5178 C CB  . ILE D 53  ? 0.8963 0.6883 0.6771 -0.0024 -0.2579 0.0324  53  ILE D CB  
5179 C CG1 . ILE D 53  ? 0.9916 0.7903 0.7713 0.0024  -0.2545 0.0354  53  ILE D CG1 
5180 C CG2 . ILE D 53  ? 0.8619 0.6686 0.6458 -0.0002 -0.2587 0.0346  53  ILE D CG2 
5181 C CD1 . ILE D 53  ? 1.0627 0.8839 0.8482 0.0035  -0.2549 0.0309  53  ILE D CD1 
5182 N N   . TYR D 54  ? 0.8835 0.6451 0.6559 -0.0030 -0.2574 0.0417  54  TYR D N   
5183 C CA  . TYR D 54  ? 0.8933 0.6509 0.6654 -0.0045 -0.2591 0.0426  54  TYR D CA  
5184 C C   . TYR D 54  ? 0.9057 0.6801 0.6810 0.0005  -0.2581 0.0474  54  TYR D C   
5185 O O   . TYR D 54  ? 0.9087 0.6927 0.6850 0.0060  -0.2547 0.0523  54  TYR D O   
5186 C CB  . TYR D 54  ? 0.9400 0.6764 0.7065 -0.0054 -0.2570 0.0456  54  TYR D CB  
5187 C CG  . TYR D 54  ? 0.9618 0.6942 0.7266 0.0000  -0.2515 0.0524  54  TYR D CG  
5188 C CD1 . TYR D 54  ? 0.9284 0.6557 0.6914 0.0012  -0.2487 0.0531  54  TYR D CD1 
5189 C CD2 . TYR D 54  ? 0.8891 0.6223 0.6548 0.0039  -0.2489 0.0584  54  TYR D CD2 
5190 C CE1 . TYR D 54  ? 0.9788 0.7022 0.7414 0.0060  -0.2432 0.0594  54  TYR D CE1 
5191 C CE2 . TYR D 54  ? 0.8949 0.6242 0.6607 0.0089  -0.2431 0.0651  54  TYR D CE2 
5192 C CZ  . TYR D 54  ? 0.9859 0.7103 0.7503 0.0099  -0.2402 0.0655  54  TYR D CZ  
5193 O OH  . TYR D 54  ? 0.9784 0.6989 0.7440 0.0147  -0.2339 0.0721  54  TYR D OH  
5194 N N   . LEU D 55  ? 0.8818 0.6603 0.6591 -0.0015 -0.2610 0.0460  55  LEU D N   
5195 C CA  . LEU D 55  ? 0.9089 0.7044 0.6897 0.0028  -0.2606 0.0503  55  LEU D CA  
5196 C C   . LEU D 55  ? 0.8710 0.6915 0.6570 0.0057  -0.2605 0.0493  55  LEU D C   
5197 O O   . LEU D 55  ? 0.8771 0.7129 0.6652 0.0116  -0.2581 0.0554  55  LEU D O   
5198 C CB  . LEU D 55  ? 0.8428 0.6308 0.6211 0.0082  -0.2560 0.0593  55  LEU D CB  
5199 C CG  . LEU D 55  ? 0.8464 0.6167 0.6216 0.0058  -0.2563 0.0602  55  LEU D CG  
5200 C CD1 . LEU D 55  ? 0.8674 0.6278 0.6413 0.0108  -0.2505 0.0683  55  LEU D CD1 
5201 C CD2 . LEU D 55  ? 0.8407 0.6218 0.6189 0.0045  -0.2601 0.0588  55  LEU D CD2 
5202 N N   . GLY D 56  ? 0.8937 0.7195 0.6824 0.0018  -0.2627 0.0416  56  GLY D N   
5203 C CA  . GLY D 56  ? 0.8797 0.7305 0.6745 0.0031  -0.2630 0.0382  56  GLY D CA  
5204 C C   . GLY D 56  ? 0.9098 0.7674 0.7038 0.0075  -0.2596 0.0408  56  GLY D C   
5205 O O   . GLY D 56  ? 0.9066 0.7797 0.7051 0.0066  -0.2600 0.0351  56  GLY D O   
5206 N N   . SER D 57  ? 0.9092 0.7559 0.6983 0.0121  -0.2558 0.0488  57  SER D N   
5207 C CA  . SER D 57  ? 0.9157 0.7730 0.7049 0.0174  -0.2522 0.0526  57  SER D CA  
5208 C C   . SER D 57  ? 0.9662 0.8038 0.7500 0.0192  -0.2486 0.0570  57  SER D C   
5209 O O   . SER D 57  ? 0.9735 0.8179 0.7573 0.0217  -0.2465 0.0574  57  SER D O   
5210 C CB  . SER D 57  ? 0.9211 0.7998 0.7134 0.0241  -0.2498 0.0603  57  SER D CB  
5211 O OG  . SER D 57  ? 0.8338 0.7027 0.6246 0.0263  -0.2484 0.0673  57  SER D OG  
5212 N N   . GLU D 58  ? 0.9822 0.7970 0.7618 0.0178  -0.2475 0.0597  58  GLU D N   
5213 C CA  . GLU D 58  ? 0.9819 0.7805 0.7574 0.0194  -0.2436 0.0631  58  GLU D CA  
5214 C C   . GLU D 58  ? 1.0115 0.7957 0.7840 0.0136  -0.2458 0.0559  58  GLU D C   
5215 O O   . GLU D 58  ? 1.0307 0.8055 0.8024 0.0082  -0.2493 0.0508  58  GLU D O   
5216 C CB  . GLU D 58  ? 0.9980 0.7798 0.7714 0.0211  -0.2400 0.0695  58  GLU D CB  
5217 C CG  . GLU D 58  ? 1.0684 0.8603 0.8449 0.0281  -0.2356 0.0789  58  GLU D CG  
5218 C CD  . GLU D 58  ? 1.0994 0.9065 0.8781 0.0340  -0.2321 0.0839  58  GLU D CD  
5219 O OE1 . GLU D 58  ? 1.1629 0.9596 0.9404 0.0365  -0.2274 0.0881  58  GLU D OE1 
5220 O OE2 . GLU D 58  ? 1.0197 0.8504 0.8018 0.0363  -0.2337 0.0837  58  GLU D OE2 
5221 N N   . ARG D 59  ? 1.1334 0.9153 0.9043 0.0152  -0.2435 0.0564  59  ARG D N   
5222 C CA  . ARG D 59  ? 1.1431 0.9080 0.9104 0.0109  -0.2442 0.0520  59  ARG D CA  
5223 C C   . ARG D 59  ? 1.1568 0.9006 0.9203 0.0090  -0.2426 0.0542  59  ARG D C   
5224 O O   . ARG D 59  ? 1.1803 0.9205 0.9436 0.0127  -0.2387 0.0606  59  ARG D O   
5225 C CB  . ARG D 59  ? 1.2295 0.9969 0.9957 0.0138  -0.2415 0.0531  59  ARG D CB  
5226 C CG  . ARG D 59  ? 1.3735 1.1381 1.1387 0.0195  -0.2359 0.0615  59  ARG D CG  
5227 C CD  . ARG D 59  ? 1.4444 1.1867 1.2057 0.0176  -0.2333 0.0623  59  ARG D CD  
5228 N NE  . ARG D 59  ? 1.4774 1.2151 1.2395 0.0224  -0.2273 0.0702  59  ARG D NE  
5229 C CZ  . ARG D 59  ? 1.4351 1.1611 1.1957 0.0231  -0.2233 0.0719  59  ARG D CZ  
5230 N NH1 . ARG D 59  ? 1.3158 1.0340 1.0731 0.0194  -0.2249 0.0667  59  ARG D NH1 
5231 N NH2 . ARG D 59  ? 1.4762 1.1986 1.2394 0.0275  -0.2172 0.0793  59  ARG D NH2 
5232 N N   . ALA D 60  ? 1.2670 0.9978 1.0280 0.0032  -0.2453 0.0489  60  ALA D N   
5233 C CA  . ALA D 60  ? 1.2845 0.9966 1.0418 0.0006  -0.2440 0.0496  60  ALA D CA  
5234 C C   . ALA D 60  ? 1.3420 1.0437 1.0966 0.0019  -0.2398 0.0517  60  ALA D C   
5235 O O   . ALA D 60  ? 1.3658 1.0740 1.1211 0.0050  -0.2380 0.0530  60  ALA D O   
5236 C CB  . ALA D 60  ? 1.2892 0.9937 1.0452 -0.0059 -0.2483 0.0436  60  ALA D CB  
5237 N N   . LEU D 61  ? 1.2467 0.9326 0.9986 -0.0007 -0.2379 0.0515  61  LEU D N   
5238 C CA  . LEU D 61  ? 1.2091 0.8847 0.9592 -0.0002 -0.2336 0.0526  61  LEU D CA  
5239 C C   . LEU D 61  ? 1.1636 0.8382 0.9116 -0.0030 -0.2359 0.0481  61  LEU D C   
5240 O O   . LEU D 61  ? 1.1618 0.8332 0.9083 -0.0079 -0.2398 0.0434  61  LEU D O   
5241 C CB  . LEU D 61  ? 1.1897 0.8501 0.9381 -0.0032 -0.2310 0.0520  61  LEU D CB  
5242 C CG  . LEU D 61  ? 1.1740 0.8327 0.9243 -0.0020 -0.2294 0.0550  61  LEU D CG  
5243 C CD1 . LEU D 61  ? 1.1242 0.7837 0.8730 -0.0062 -0.2350 0.0512  61  LEU D CD1 
5244 C CD2 . LEU D 61  ? 1.1031 0.7482 0.8538 -0.0025 -0.2235 0.0560  61  LEU D CD2 
5245 N N   . GLY D 62  ? 1.1592 0.8371 0.9075 0.0002  -0.2333 0.0501  62  GLY D N   
5246 C CA  . GLY D 62  ? 1.1595 0.8364 0.9059 -0.0018 -0.2349 0.0463  62  GLY D CA  
5247 C C   . GLY D 62  ? 1.1716 0.8623 0.9201 -0.0011 -0.2385 0.0439  62  GLY D C   
5248 O O   . GLY D 62  ? 1.1513 0.8418 0.8989 -0.0025 -0.2396 0.0408  62  GLY D O   
5249 N N   . VAL D 63  ? 1.1977 0.9009 0.9494 0.0009  -0.2400 0.0447  63  VAL D N   
5250 C CA  . VAL D 63  ? 1.1798 0.8978 0.9348 0.0011  -0.2429 0.0412  63  VAL D CA  
5251 C C   . VAL D 63  ? 1.1783 0.9073 0.9341 0.0065  -0.2401 0.0441  63  VAL D C   
5252 O O   . VAL D 63  ? 1.2466 0.9803 1.0030 0.0112  -0.2368 0.0501  63  VAL D O   
5253 C CB  . VAL D 63  ? 1.1659 0.8944 0.9246 0.0006  -0.2456 0.0402  63  VAL D CB  
5254 C CG1 . VAL D 63  ? 1.1844 0.9296 0.9478 0.0005  -0.2479 0.0356  63  VAL D CG1 
5255 C CG2 . VAL D 63  ? 1.1838 0.9010 0.9413 -0.0046 -0.2482 0.0377  63  VAL D CG2 
5256 N N   . PRO D 64  ? 1.1828 0.9163 0.9389 0.0061  -0.2409 0.0405  64  PRO D N   
5257 C CA  . PRO D 64  ? 1.1885 0.9343 0.9455 0.0112  -0.2384 0.0430  64  PRO D CA  
5258 C C   . PRO D 64  ? 1.2580 1.0244 1.0194 0.0142  -0.2390 0.0437  64  PRO D C   
5259 O O   . PRO D 64  ? 1.3027 1.0768 1.0677 0.0113  -0.2422 0.0389  64  PRO D O   
5260 C CB  . PRO D 64  ? 1.2345 0.9801 0.9913 0.0090  -0.2399 0.0374  64  PRO D CB  
5261 C CG  . PRO D 64  ? 1.2103 0.9439 0.9667 0.0030  -0.2429 0.0328  64  PRO D CG  
5262 C CD  . PRO D 64  ? 1.2061 0.9358 0.9630 0.0011  -0.2442 0.0341  64  PRO D CD  
5263 N N   . ASP D 65  ? 1.2754 1.0516 1.0372 0.0201  -0.2355 0.0499  65  ASP D N   
5264 C CA  . ASP D 65  ? 1.3046 1.1014 1.0706 0.0236  -0.2355 0.0522  65  ASP D CA  
5265 C C   . ASP D 65  ? 1.3206 1.1377 1.0904 0.0234  -0.2375 0.0461  65  ASP D C   
5266 O O   . ASP D 65  ? 1.2845 1.1224 1.0581 0.0265  -0.2373 0.0475  65  ASP D O   
5267 C CB  . ASP D 65  ? 1.3170 1.1192 1.0830 0.0304  -0.2306 0.0617  65  ASP D CB  
5268 C CG  . ASP D 65  ? 1.3645 1.1720 1.1330 0.0327  -0.2298 0.0671  65  ASP D CG  
5269 O OD1 . ASP D 65  ? 1.3264 1.1436 1.0976 0.0303  -0.2334 0.0632  65  ASP D OD1 
5270 O OD2 . ASP D 65  ? 1.4511 1.2531 1.2198 0.0368  -0.2253 0.0753  65  ASP D OD2 
5271 N N   . ARG D 66  ? 1.4316 1.2447 1.2013 0.0198  -0.2392 0.0392  66  ARG D N   
5272 C CA  . ARG D 66  ? 1.4334 1.2649 1.2085 0.0184  -0.2410 0.0317  66  ARG D CA  
5273 C C   . ARG D 66  ? 1.3948 1.2332 1.1751 0.0148  -0.2441 0.0273  66  ARG D C   
5274 O O   . ARG D 66  ? 1.3548 1.2137 1.1410 0.0145  -0.2448 0.0222  66  ARG D O   
5275 C CB  . ARG D 66  ? 1.4027 1.2257 1.1775 0.0150  -0.2419 0.0254  66  ARG D CB  
5276 C CG  . ARG D 66  ? 1.4337 1.2401 1.2021 0.0165  -0.2397 0.0296  66  ARG D CG  
5277 C CD  . ARG D 66  ? 1.4677 1.2676 1.2361 0.0134  -0.2406 0.0235  66  ARG D CD  
5278 N NE  . ARG D 66  ? 1.5209 1.3134 1.2927 0.0076  -0.2436 0.0178  66  ARG D NE  
5279 C CZ  . ARG D 66  ? 1.5342 1.3076 1.3030 0.0041  -0.2447 0.0182  66  ARG D CZ  
5280 N NH1 . ARG D 66  ? 1.5804 1.3396 1.3429 0.0052  -0.2431 0.0229  66  ARG D NH1 
5281 N NH2 . ARG D 66  ? 1.4403 1.2096 1.2132 -0.0008 -0.2471 0.0136  66  ARG D NH2 
5282 N N   . PHE D 67  ? 1.2683 1.0905 1.0466 0.0118  -0.2456 0.0288  67  PHE D N   
5283 C CA  . PHE D 67  ? 1.1790 1.0054 0.9617 0.0082  -0.2485 0.0253  67  PHE D CA  
5284 C C   . PHE D 67  ? 1.1358 0.9741 0.9191 0.0122  -0.2478 0.0310  67  PHE D C   
5285 O O   . PHE D 67  ? 1.1689 0.9987 0.9478 0.0157  -0.2455 0.0389  67  PHE D O   
5286 C CB  . PHE D 67  ? 1.1847 0.9887 0.9647 0.0034  -0.2505 0.0246  67  PHE D CB  
5287 C CG  . PHE D 67  ? 1.1880 0.9814 0.9683 -0.0006 -0.2513 0.0195  67  PHE D CG  
5288 C CD1 . PHE D 67  ? 1.2099 0.9909 0.9848 0.0006  -0.2495 0.0220  67  PHE D CD1 
5289 C CD2 . PHE D 67  ? 1.1296 0.9257 0.9162 -0.0054 -0.2535 0.0124  67  PHE D CD2 
5290 C CE1 . PHE D 67  ? 1.2435 1.0156 1.0187 -0.0028 -0.2502 0.0178  67  PHE D CE1 
5291 C CE2 . PHE D 67  ? 1.1732 0.9601 0.9610 -0.0085 -0.2538 0.0086  67  PHE D CE2 
5292 C CZ  . PHE D 67  ? 1.2465 1.0217 1.0283 -0.0071 -0.2523 0.0115  67  PHE D CZ  
5293 N N   . SER D 68  ? 1.0718 0.9305 0.8614 0.0116  -0.2493 0.0270  68  SER D N   
5294 C CA  . SER D 68  ? 1.0662 0.9402 0.8573 0.0155  -0.2487 0.0323  68  SER D CA  
5295 C C   . SER D 68  ? 0.9953 0.8781 0.7921 0.0114  -0.2520 0.0268  68  SER D C   
5296 O O   . SER D 68  ? 0.9742 0.8656 0.7770 0.0072  -0.2537 0.0179  68  SER D O   
5297 C CB  . SER D 68  ? 1.1222 1.0210 0.9155 0.0210  -0.2462 0.0344  68  SER D CB  
5298 O OG  . SER D 68  ? 1.1406 1.0578 0.9403 0.0184  -0.2474 0.0249  68  SER D OG  
5299 N N   . GLY D 69  ? 0.9460 0.8267 0.7416 0.0126  -0.2526 0.0320  69  GLY D N   
5300 C CA  . GLY D 69  ? 0.9262 0.8156 0.7269 0.0091  -0.2557 0.0278  69  GLY D CA  
5301 C C   . GLY D 69  ? 0.9102 0.8271 0.7151 0.0133  -0.2551 0.0303  69  GLY D C   
5302 O O   . GLY D 69  ? 1.0032 0.9293 0.8062 0.0196  -0.2521 0.0380  69  GLY D O   
5303 N N   . SER D 70  ? 0.8380 0.7689 0.6494 0.0096  -0.2579 0.0239  70  SER D N   
5304 C CA  . SER D 70  ? 0.7983 0.7582 0.6147 0.0127  -0.2578 0.0249  70  SER D CA  
5305 C C   . SER D 70  ? 0.7917 0.7580 0.6145 0.0070  -0.2614 0.0175  70  SER D C   
5306 O O   . SER D 70  ? 0.8969 0.8482 0.7213 0.0009  -0.2635 0.0107  70  SER D O   
5307 C CB  . SER D 70  ? 0.7942 0.7803 0.6150 0.0153  -0.2557 0.0216  70  SER D CB  
5308 O OG  . SER D 70  ? 0.7911 0.7743 0.6155 0.0103  -0.2562 0.0115  70  SER D OG  
5309 N N   . GLY D 71  ? 0.7876 0.7769 0.6143 0.0093  -0.2620 0.0192  71  GLY D N   
5310 C CA  . GLY D 71  ? 0.7807 0.7796 0.6143 0.0039  -0.2652 0.0117  71  GLY D CA  
5311 C C   . GLY D 71  ? 0.8416 0.8336 0.6721 0.0052  -0.2669 0.0185  71  GLY D C   
5312 O O   . GLY D 71  ? 0.8948 0.8652 0.7176 0.0081  -0.2659 0.0273  71  GLY D O   
5313 N N   . SER D 72  ? 0.8810 0.8918 0.7182 0.0027  -0.2693 0.0140  72  SER D N   
5314 C CA  . SER D 72  ? 0.9774 0.9840 0.8126 0.0035  -0.2712 0.0195  72  SER D CA  
5315 C C   . SER D 72  ? 1.0787 1.0953 0.9217 -0.0032 -0.2748 0.0097  72  SER D C   
5316 O O   . SER D 72  ? 1.0730 1.1071 0.9245 -0.0072 -0.2751 -0.0005 72  SER D O   
5317 C CB  . SER D 72  ? 1.0977 1.1251 0.9322 0.0114  -0.2691 0.0295  72  SER D CB  
5318 O OG  . SER D 72  ? 1.2127 1.2372 1.0463 0.0120  -0.2710 0.0343  72  SER D OG  
5319 N N   . GLY D 73  ? 1.4115 1.4166 1.2522 -0.0045 -0.2773 0.0126  73  GLY D N   
5320 C CA  . GLY D 73  ? 1.4055 1.4187 1.2533 -0.0107 -0.2808 0.0042  73  GLY D CA  
5321 C C   . GLY D 73  ? 1.4037 1.3987 1.2545 -0.0184 -0.2823 -0.0050 73  GLY D C   
5322 O O   . GLY D 73  ? 1.4065 1.3735 1.2514 -0.0206 -0.2835 -0.0025 73  GLY D O   
5323 N N   . ARG D 74  ? 1.1328 1.1440 0.9934 -0.0226 -0.2817 -0.0155 74  ARG D N   
5324 C CA  . ARG D 74  ? 1.0114 1.0089 0.8777 -0.0299 -0.2825 -0.0245 74  ARG D CA  
5325 C C   . ARG D 74  ? 0.9351 0.9298 0.8038 -0.0307 -0.2796 -0.0289 74  ARG D C   
5326 O O   . ARG D 74  ? 0.9900 0.9642 0.8596 -0.0349 -0.2795 -0.0320 74  ARG D O   
5327 C CB  . ARG D 74  ? 0.9570 0.9747 0.8361 -0.0359 -0.2841 -0.0351 74  ARG D CB  
5328 C CG  . ARG D 74  ? 0.9766 0.9945 0.8539 -0.0365 -0.2875 -0.0320 74  ARG D CG  
5329 C CD  . ARG D 74  ? 0.9500 0.9988 0.8398 -0.0401 -0.2885 -0.0410 74  ARG D CD  
5330 N NE  . ARG D 74  ? 0.9488 0.9912 0.8483 -0.0484 -0.2897 -0.0510 74  ARG D NE  
5331 C CZ  . ARG D 74  ? 0.9428 0.9866 0.8458 -0.0522 -0.2927 -0.0535 74  ARG D CZ  
5332 N NH1 . ARG D 74  ? 0.8923 0.9439 0.7899 -0.0486 -0.2951 -0.0469 74  ARG D NH1 
5333 N NH2 . ARG D 74  ? 0.9112 0.9487 0.8240 -0.0598 -0.2931 -0.0624 74  ARG D NH2 
5334 N N   . ASP D 75  ? 0.8891 0.9043 0.7591 -0.0265 -0.2770 -0.0290 75  ASP D N   
5335 C CA  . ASP D 75  ? 0.8783 0.8917 0.7501 -0.0267 -0.2741 -0.0329 75  ASP D CA  
5336 C C   . ASP D 75  ? 0.8682 0.8662 0.7279 -0.0203 -0.2725 -0.0223 75  ASP D C   
5337 O O   . ASP D 75  ? 0.9186 0.9225 0.7719 -0.0143 -0.2722 -0.0134 75  ASP D O   
5338 C CB  . ASP D 75  ? 0.9176 0.9651 0.7998 -0.0268 -0.2720 -0.0413 75  ASP D CB  
5339 C CG  . ASP D 75  ? 0.9182 0.9864 0.8130 -0.0324 -0.2733 -0.0513 75  ASP D CG  
5340 O OD1 . ASP D 75  ? 0.9045 0.9643 0.8079 -0.0391 -0.2733 -0.0598 75  ASP D OD1 
5341 O OD2 . ASP D 75  ? 0.9328 1.0263 0.8295 -0.0301 -0.2741 -0.0503 75  ASP D OD2 
5342 N N   . PHE D 76  ? 0.8518 0.8305 0.7091 -0.0216 -0.2711 -0.0233 76  PHE D N   
5343 C CA  . PHE D 76  ? 0.8461 0.8070 0.6923 -0.0167 -0.2696 -0.0142 76  PHE D CA  
5344 C C   . PHE D 76  ? 0.8283 0.7883 0.6765 -0.0171 -0.2671 -0.0188 76  PHE D C   
5345 O O   . PHE D 76  ? 0.8986 0.8652 0.7566 -0.0220 -0.2666 -0.0286 76  PHE D O   
5346 C CB  . PHE D 76  ? 0.8792 0.8088 0.7172 -0.0180 -0.2712 -0.0085 76  PHE D CB  
5347 C CG  . PHE D 76  ? 0.8855 0.8132 0.7195 -0.0163 -0.2731 -0.0024 76  PHE D CG  
5348 C CD1 . PHE D 76  ? 0.9314 0.8630 0.7710 -0.0210 -0.2760 -0.0071 76  PHE D CD1 
5349 C CD2 . PHE D 76  ? 0.8644 0.7868 0.6899 -0.0101 -0.2717 0.0081  76  PHE D CD2 
5350 C CE1 . PHE D 76  ? 0.9652 0.8951 0.8010 -0.0194 -0.2778 -0.0015 76  PHE D CE1 
5351 C CE2 . PHE D 76  ? 0.9673 0.8879 0.7899 -0.0085 -0.2731 0.0137  76  PHE D CE2 
5352 C CZ  . PHE D 76  ? 0.9799 0.9042 0.8072 -0.0131 -0.2763 0.0089  76  PHE D CZ  
5353 N N   . THR D 77  ? 0.8139 0.7654 0.6536 -0.0120 -0.2651 -0.0116 77  THR D N   
5354 C CA  . THR D 77  ? 0.8315 0.7821 0.6719 -0.0117 -0.2627 -0.0149 77  THR D CA  
5355 C C   . THR D 77  ? 0.8822 0.8076 0.7118 -0.0087 -0.2617 -0.0067 77  THR D C   
5356 O O   . THR D 77  ? 0.9290 0.8488 0.7508 -0.0040 -0.2612 0.0025  77  THR D O   
5357 C CB  . THR D 77  ? 0.8275 0.8075 0.6716 -0.0077 -0.2604 -0.0167 77  THR D CB  
5358 O OG1 . THR D 77  ? 0.8496 0.8557 0.7030 -0.0097 -0.2613 -0.0229 77  THR D OG1 
5359 C CG2 . THR D 77  ? 0.8862 0.8680 0.7340 -0.0090 -0.2581 -0.0235 77  THR D CG2 
5360 N N   . LEU D 78  ? 0.9004 0.8114 0.7304 -0.0116 -0.2611 -0.0104 78  LEU D N   
5361 C CA  . LEU D 78  ? 0.9321 0.8218 0.7530 -0.0094 -0.2599 -0.0045 78  LEU D CA  
5362 C C   . LEU D 78  ? 0.9226 0.8214 0.7458 -0.0080 -0.2574 -0.0082 78  LEU D C   
5363 O O   . LEU D 78  ? 0.9716 0.8709 0.8017 -0.0120 -0.2571 -0.0161 78  LEU D O   
5364 C CB  . LEU D 78  ? 0.9601 0.8247 0.7792 -0.0142 -0.2615 -0.0050 78  LEU D CB  
5365 C CG  . LEU D 78  ? 0.9887 0.8299 0.7990 -0.0132 -0.2606 0.0002  78  LEU D CG  
5366 C CD1 . LEU D 78  ? 0.9924 0.8321 0.8053 -0.0142 -0.2590 -0.0042 78  LEU D CD1 
5367 C CD2 . LEU D 78  ? 1.0252 0.8636 0.8268 -0.0073 -0.2589 0.0091  78  LEU D CD2 
5368 N N   . LYS D 79  ? 0.9096 0.8158 0.7275 -0.0021 -0.2553 -0.0025 79  LYS D N   
5369 C CA  . LYS D 79  ? 0.9716 0.8888 0.7910 0.0000  -0.2529 -0.0056 79  LYS D CA  
5370 C C   . LYS D 79  ? 1.0149 0.9115 0.8256 0.0022  -0.2515 -0.0001 79  LYS D C   
5371 O O   . LYS D 79  ? 1.1071 0.9898 0.9101 0.0050  -0.2512 0.0085  79  LYS D O   
5372 C CB  . LYS D 79  ? 1.0118 0.9567 0.8326 0.0051  -0.2512 -0.0037 79  LYS D CB  
5373 C CG  . LYS D 79  ? 1.0267 0.9984 0.8583 0.0024  -0.2518 -0.0127 79  LYS D CG  
5374 C CD  . LYS D 79  ? 1.0408 1.0410 0.8757 0.0060  -0.2493 -0.0153 79  LYS D CD  
5375 C CE  . LYS D 79  ? 1.0110 1.0409 0.8564 0.0037  -0.2497 -0.0234 79  LYS D CE  
5376 N NZ  . LYS D 79  ? 0.9242 0.9810 0.7758 0.0047  -0.2470 -0.0307 79  LYS D NZ  
5377 N N   . ILE D 80  ? 1.0232 0.9182 0.8361 0.0007  -0.2504 -0.0054 80  ILE D N   
5378 C CA  . ILE D 80  ? 1.1557 1.0352 0.9614 0.0029  -0.2489 -0.0015 80  ILE D CA  
5379 C C   . ILE D 80  ? 1.2175 1.1157 1.0243 0.0067  -0.2464 -0.0032 80  ILE D C   
5380 O O   . ILE D 80  ? 1.2249 1.1395 1.0398 0.0047  -0.2459 -0.0119 80  ILE D O   
5381 C CB  . ILE D 80  ? 1.2049 1.0656 1.0119 -0.0021 -0.2498 -0.0058 80  ILE D CB  
5382 C CG1 . ILE D 80  ? 1.1347 0.9826 0.9431 -0.0065 -0.2523 -0.0059 80  ILE D CG1 
5383 C CG2 . ILE D 80  ? 1.2938 1.1365 1.0922 -0.0001 -0.2486 -0.0007 80  ILE D CG2 
5384 C CD1 . ILE D 80  ? 1.0362 0.8688 0.8475 -0.0113 -0.2530 -0.0098 80  ILE D CD1 
5385 N N   . SER D 81  ? 1.4059 1.3020 1.2053 0.0121  -0.2445 0.0048  81  SER D N   
5386 C CA  . SER D 81  ? 1.4376 1.3524 1.2373 0.0164  -0.2419 0.0044  81  SER D CA  
5387 C C   . SER D 81  ? 1.4081 1.3133 1.2061 0.0156  -0.2409 0.0008  81  SER D C   
5388 O O   . SER D 81  ? 1.4003 1.3222 1.2027 0.0159  -0.2395 -0.0055 81  SER D O   
5389 C CB  . SER D 81  ? 1.4451 1.3636 1.2387 0.0231  -0.2398 0.0154  81  SER D CB  
5390 O OG  . SER D 81  ? 1.4179 1.3359 1.2115 0.0236  -0.2408 0.0206  81  SER D OG  
5391 N N   . ARG D 82  ? 1.3420 1.2216 1.1339 0.0144  -0.2413 0.0044  82  ARG D N   
5392 C CA  . ARG D 82  ? 1.3965 1.2653 1.1865 0.0134  -0.2405 0.0016  82  ARG D CA  
5393 C C   . ARG D 82  ? 1.4294 1.2767 1.2199 0.0080  -0.2426 -0.0008 82  ARG D C   
5394 O O   . ARG D 82  ? 1.4858 1.3153 1.2708 0.0074  -0.2435 0.0049  82  ARG D O   
5395 C CB  . ARG D 82  ? 1.5336 1.3943 1.3151 0.0182  -0.2384 0.0095  82  ARG D CB  
5396 C CG  . ARG D 82  ? 1.5541 1.4334 1.3359 0.0225  -0.2359 0.0086  82  ARG D CG  
5397 C CD  . ARG D 82  ? 1.6551 1.5207 1.4299 0.0249  -0.2341 0.0127  82  ARG D CD  
5398 N NE  . ARG D 82  ? 1.7439 1.6276 1.5185 0.0292  -0.2317 0.0123  82  ARG D NE  
5399 C CZ  . ARG D 82  ? 1.7834 1.6696 1.5591 0.0283  -0.2312 0.0059  82  ARG D CZ  
5400 N NH1 . ARG D 82  ? 1.7600 1.6322 1.5375 0.0234  -0.2328 -0.0002 82  ARG D NH1 
5401 N NH2 . ARG D 82  ? 1.8107 1.7146 1.5858 0.0325  -0.2289 0.0060  82  ARG D NH2 
5402 N N   . VAL D 83  ? 1.4316 1.2815 1.2293 0.0041  -0.2430 -0.0091 83  VAL D N   
5403 C CA  . VAL D 83  ? 1.3780 1.2105 1.1779 -0.0009 -0.2446 -0.0113 83  VAL D CA  
5404 C C   . VAL D 83  ? 1.3835 1.2004 1.1787 -0.0009 -0.2440 -0.0101 83  VAL D C   
5405 O O   . VAL D 83  ? 1.3618 1.1855 1.1588 0.0003  -0.2423 -0.0139 83  VAL D O   
5406 C CB  . VAL D 83  ? 1.2943 1.1378 1.1065 -0.0052 -0.2447 -0.0204 83  VAL D CB  
5407 C CG1 . VAL D 83  ? 1.3007 1.1275 1.1164 -0.0096 -0.2453 -0.0225 83  VAL D CG1 
5408 C CG2 . VAL D 83  ? 1.2347 1.0886 1.0512 -0.0064 -0.2460 -0.0211 83  VAL D CG2 
5409 N N   . GLU D 84  ? 1.3846 1.1815 1.1739 -0.0024 -0.2452 -0.0051 84  GLU D N   
5410 C CA  . GLU D 84  ? 1.3716 1.1535 1.1569 -0.0031 -0.2450 -0.0041 84  GLU D CA  
5411 C C   . GLU D 84  ? 1.3921 1.1652 1.1833 -0.0081 -0.2462 -0.0074 84  GLU D C   
5412 O O   . GLU D 84  ? 1.3589 1.1373 1.1575 -0.0109 -0.2470 -0.0107 84  GLU D O   
5413 C CB  . GLU D 84  ? 1.4321 1.1995 1.2073 -0.0013 -0.2448 0.0035  84  GLU D CB  
5414 C CG  . GLU D 84  ? 1.4820 1.2572 1.2524 0.0040  -0.2428 0.0078  84  GLU D CG  
5415 C CD  . GLU D 84  ? 1.5255 1.2861 1.2879 0.0055  -0.2418 0.0150  84  GLU D CD  
5416 O OE1 . GLU D 84  ? 1.5584 1.3037 1.3186 0.0022  -0.2430 0.0161  84  GLU D OE1 
5417 O OE2 . GLU D 84  ? 1.4573 1.2224 1.2164 0.0100  -0.2394 0.0195  84  GLU D OE2 
5418 N N   . ALA D 85  ? 1.4685 1.2286 1.2567 -0.0091 -0.2462 -0.0062 85  ALA D N   
5419 C CA  . ALA D 85  ? 1.5520 1.3053 1.3465 -0.0131 -0.2468 -0.0086 85  ALA D CA  
5420 C C   . ALA D 85  ? 1.5146 1.2590 1.3084 -0.0161 -0.2488 -0.0055 85  ALA D C   
5421 O O   . ALA D 85  ? 1.4423 1.1858 1.2440 -0.0195 -0.2492 -0.0077 85  ALA D O   
5422 C CB  . ALA D 85  ? 1.6663 1.4091 1.4573 -0.0131 -0.2463 -0.0075 85  ALA D CB  
5423 N N   . GLN D 86  ? 1.5872 1.3251 1.3724 -0.0150 -0.2497 -0.0003 86  GLN D N   
5424 C CA  . GLN D 86  ? 1.5234 1.2523 1.3069 -0.0178 -0.2514 0.0026  86  GLN D CA  
5425 C C   . GLN D 86  ? 1.5219 1.2593 1.3111 -0.0190 -0.2524 0.0007  86  GLN D C   
5426 O O   . GLN D 86  ? 1.5466 1.2775 1.3360 -0.0218 -0.2540 0.0023  86  GLN D O   
5427 C CB  . GLN D 86  ? 1.4627 1.1815 1.2358 -0.0162 -0.2513 0.0082  86  GLN D CB  
5428 C CG  . GLN D 86  ? 1.4916 1.2179 1.2617 -0.0122 -0.2502 0.0103  86  GLN D CG  
5429 C CD  . GLN D 86  ? 1.6410 1.3568 1.4026 -0.0105 -0.2490 0.0157  86  GLN D CD  
5430 O OE1 . GLN D 86  ? 1.7245 1.4297 1.4818 -0.0114 -0.2484 0.0170  86  GLN D OE1 
5431 N NE2 . GLN D 86  ? 1.6455 1.3649 1.4056 -0.0082 -0.2482 0.0188  86  GLN D NE2 
5432 N N   . ASP D 87  ? 1.3914 1.1441 1.1854 -0.0171 -0.2516 -0.0028 87  ASP D N   
5433 C CA  . ASP D 87  ? 1.2974 1.0598 1.0965 -0.0181 -0.2525 -0.0047 87  ASP D CA  
5434 C C   . ASP D 87  ? 1.2757 1.0401 1.0857 -0.0225 -0.2530 -0.0094 87  ASP D C   
5435 O O   . ASP D 87  ? 1.2228 0.9954 1.0381 -0.0240 -0.2538 -0.0117 87  ASP D O   
5436 C CB  . ASP D 87  ? 1.2882 1.0690 1.0897 -0.0148 -0.2512 -0.0073 87  ASP D CB  
5437 C CG  . ASP D 87  ? 1.3402 1.1203 1.1322 -0.0100 -0.2503 -0.0017 87  ASP D CG  
5438 O OD1 . ASP D 87  ? 1.4146 1.1834 1.2004 -0.0089 -0.2495 0.0013  87  ASP D OD1 
5439 O OD2 . ASP D 87  ? 1.2805 1.0718 1.0718 -0.0073 -0.2500 0.0001  87  ASP D OD2 
5440 N N   . VAL D 88  ? 1.3540 1.1115 1.1680 -0.0246 -0.2523 -0.0107 88  VAL D N   
5441 C CA  . VAL D 88  ? 1.2698 1.0288 1.0955 -0.0286 -0.2520 -0.0143 88  VAL D CA  
5442 C C   . VAL D 88  ? 1.1893 0.9389 1.0126 -0.0313 -0.2542 -0.0104 88  VAL D C   
5443 O O   . VAL D 88  ? 1.2224 0.9602 1.0355 -0.0308 -0.2556 -0.0049 88  VAL D O   
5444 C CB  . VAL D 88  ? 1.2843 1.0384 1.1152 -0.0296 -0.2502 -0.0154 88  VAL D CB  
5445 C CG1 . VAL D 88  ? 1.3355 1.1020 1.1733 -0.0281 -0.2475 -0.0217 88  VAL D CG1 
5446 C CG2 . VAL D 88  ? 1.3410 1.0812 1.1606 -0.0283 -0.2510 -0.0095 88  VAL D CG2 
5447 N N   . GLY D 89  ? 1.1044 0.8598 0.9377 -0.0343 -0.2543 -0.0138 89  GLY D N   
5448 C CA  . GLY D 89  ? 1.0824 0.8303 0.9145 -0.0369 -0.2564 -0.0107 89  GLY D CA  
5449 C C   . GLY D 89  ? 1.0465 0.8057 0.8873 -0.0388 -0.2568 -0.0151 89  GLY D C   
5450 O O   . GLY D 89  ? 1.0779 0.8509 0.9279 -0.0389 -0.2550 -0.0213 89  GLY D O   
5451 N N   . THR D 90  ? 1.0101 0.7638 0.8478 -0.0406 -0.2590 -0.0123 90  THR D N   
5452 C CA  . THR D 90  ? 1.0263 0.7894 0.8712 -0.0427 -0.2598 -0.0160 90  THR D CA  
5453 C C   . THR D 90  ? 1.0481 0.8119 0.8828 -0.0405 -0.2622 -0.0129 90  THR D C   
5454 O O   . THR D 90  ? 1.0229 0.7742 0.8470 -0.0397 -0.2637 -0.0071 90  THR D O   
5455 C CB  . THR D 90  ? 1.0420 0.7990 0.8943 -0.0470 -0.2603 -0.0156 90  THR D CB  
5456 O OG1 . THR D 90  ? 1.0897 0.8420 0.9489 -0.0483 -0.2580 -0.0154 90  THR D OG1 
5457 C CG2 . THR D 90  ? 1.0046 0.7742 0.8692 -0.0498 -0.2599 -0.0217 90  THR D CG2 
5458 N N   . TYR D 91  ? 1.0098 0.7890 0.8486 -0.0395 -0.2621 -0.0169 91  TYR D N   
5459 C CA  . TYR D 91  ? 0.9017 0.6846 0.7322 -0.0366 -0.2637 -0.0137 91  TYR D CA  
5460 C C   . TYR D 91  ? 0.8880 0.6754 0.7233 -0.0395 -0.2657 -0.0154 91  TYR D C   
5461 O O   . TYR D 91  ? 0.9165 0.7164 0.7637 -0.0421 -0.2650 -0.0219 91  TYR D O   
5462 C CB  . TYR D 91  ? 0.8777 0.6771 0.7087 -0.0327 -0.2621 -0.0159 91  TYR D CB  
5463 C CG  . TYR D 91  ? 0.9016 0.6958 0.7256 -0.0292 -0.2605 -0.0129 91  TYR D CG  
5464 C CD1 . TYR D 91  ? 0.9450 0.7390 0.7744 -0.0301 -0.2585 -0.0165 91  TYR D CD1 
5465 C CD2 . TYR D 91  ? 0.9002 0.6898 0.7131 -0.0250 -0.2605 -0.0066 91  TYR D CD2 
5466 C CE1 . TYR D 91  ? 1.0007 0.7900 0.8236 -0.0270 -0.2571 -0.0141 91  TYR D CE1 
5467 C CE2 . TYR D 91  ? 0.9450 0.7299 0.7521 -0.0219 -0.2588 -0.0041 91  TYR D CE2 
5468 C CZ  . TYR D 91  ? 0.9999 0.7846 0.8115 -0.0231 -0.2574 -0.0079 91  TYR D CZ  
5469 O OH  . TYR D 91  ? 1.0657 0.8457 0.8714 -0.0202 -0.2558 -0.0056 91  TYR D OH  
5470 N N   . TYR D 92  ? 0.8323 0.6096 0.6589 -0.0391 -0.2678 -0.0102 92  TYR D N   
5471 C CA  . TYR D 92  ? 0.8514 0.6301 0.6809 -0.0419 -0.2700 -0.0110 92  TYR D CA  
5472 C C   . TYR D 92  ? 0.8904 0.6744 0.7130 -0.0385 -0.2712 -0.0077 92  TYR D C   
5473 O O   . TYR D 92  ? 0.9710 0.7478 0.7836 -0.0348 -0.2706 -0.0021 92  TYR D O   
5474 C CB  . TYR D 92  ? 0.8943 0.6553 0.7203 -0.0450 -0.2714 -0.0077 92  TYR D CB  
5475 C CG  . TYR D 92  ? 0.9134 0.6700 0.7477 -0.0485 -0.2701 -0.0100 92  TYR D CG  
5476 C CD1 . TYR D 92  ? 0.9531 0.7013 0.7842 -0.0475 -0.2686 -0.0076 92  TYR D CD1 
5477 C CD2 . TYR D 92  ? 0.8753 0.6367 0.7216 -0.0527 -0.2702 -0.0143 92  TYR D CD2 
5478 C CE1 . TYR D 92  ? 1.0006 0.7455 0.8401 -0.0503 -0.2672 -0.0088 92  TYR D CE1 
5479 C CE2 . TYR D 92  ? 0.8818 0.6395 0.7372 -0.0556 -0.2683 -0.0156 92  TYR D CE2 
5480 C CZ  . TYR D 92  ? 0.9307 0.6803 0.7826 -0.0542 -0.2668 -0.0125 92  TYR D CZ  
5481 O OH  . TYR D 92  ? 0.9575 0.7042 0.8192 -0.0566 -0.2646 -0.0130 92  TYR D OH  
5482 N N   . CYS D 93  ? 0.8546 0.6518 0.6835 -0.0398 -0.2724 -0.0112 93  CYS D N   
5483 C CA  . CYS D 93  ? 0.8659 0.6674 0.6893 -0.0372 -0.2739 -0.0075 93  CYS D CA  
5484 C C   . CYS D 93  ? 0.8293 0.6191 0.6507 -0.0405 -0.2764 -0.0061 93  CYS D C   
5485 O O   . CYS D 93  ? 0.9071 0.6925 0.7349 -0.0452 -0.2772 -0.0095 93  CYS D O   
5486 C CB  . CYS D 93  ? 0.9000 0.7259 0.7309 -0.0361 -0.2737 -0.0119 93  CYS D CB  
5487 S SG  . CYS D 93  ? 0.7826 0.6221 0.6291 -0.0423 -0.2746 -0.0217 93  CYS D SG  
5488 N N   . LEU D 94  ? 0.8028 0.5876 0.6159 -0.0380 -0.2774 -0.0006 94  LEU D N   
5489 C CA  . LEU D 94  ? 0.8245 0.5974 0.6344 -0.0408 -0.2797 0.0011  94  LEU D CA  
5490 C C   . LEU D 94  ? 0.8045 0.5836 0.6109 -0.0378 -0.2807 0.0043  94  LEU D C   
5491 O O   . LEU D 94  ? 0.8789 0.6588 0.6794 -0.0328 -0.2789 0.0094  94  LEU D O   
5492 C CB  . LEU D 94  ? 0.8932 0.6449 0.6942 -0.0412 -0.2792 0.0054  94  LEU D CB  
5493 C CG  . LEU D 94  ? 0.8736 0.6132 0.6678 -0.0421 -0.2808 0.0090  94  LEU D CG  
5494 C CD1 . LEU D 94  ? 0.9051 0.6426 0.7045 -0.0474 -0.2834 0.0056  94  LEU D CD1 
5495 C CD2 . LEU D 94  ? 0.8382 0.5606 0.6229 -0.0412 -0.2793 0.0133  94  LEU D CD2 
5496 N N   . GLN D 95  ? 0.8001 0.5836 0.6107 -0.0408 -0.2832 0.0018  95  GLN D N   
5497 C CA  . GLN D 95  ? 0.8248 0.6138 0.6325 -0.0383 -0.2844 0.0049  95  GLN D CA  
5498 C C   . GLN D 95  ? 0.9431 0.7123 0.7418 -0.0388 -0.2852 0.0097  95  GLN D C   
5499 O O   . GLN D 95  ? 1.0050 0.7601 0.8024 -0.0428 -0.2861 0.0085  95  GLN D O   
5500 C CB  . GLN D 95  ? 0.8718 0.6768 0.6887 -0.0415 -0.2868 -0.0006 95  GLN D CB  
5501 C CG  . GLN D 95  ? 0.9725 0.7683 0.7937 -0.0478 -0.2889 -0.0048 95  GLN D CG  
5502 C CD  . GLN D 95  ? 1.0500 0.8394 0.8673 -0.0490 -0.2917 -0.0027 95  GLN D CD  
5503 O OE1 . GLN D 95  ? 1.0320 0.8224 0.8432 -0.0450 -0.2917 0.0022  95  GLN D OE1 
5504 N NE2 . GLN D 95  ? 1.0998 0.8824 0.9210 -0.0544 -0.2936 -0.0060 95  GLN D NE2 
5505 N N   . THR D 96  ? 0.9527 0.7219 0.7461 -0.0345 -0.2844 0.0151  96  THR D N   
5506 C CA  . THR D 96  ? 0.9467 0.6988 0.7324 -0.0346 -0.2847 0.0191  96  THR D CA  
5507 C C   . THR D 96  ? 0.9694 0.7277 0.7555 -0.0336 -0.2864 0.0208  96  THR D C   
5508 O O   . THR D 96  ? 1.0307 0.7761 0.8108 -0.0331 -0.2861 0.0243  96  THR D O   
5509 C CB  . THR D 96  ? 0.9058 0.6472 0.6843 -0.0303 -0.2809 0.0249  96  THR D CB  
5510 O OG1 . THR D 96  ? 0.9410 0.6967 0.7215 -0.0249 -0.2784 0.0277  96  THR D OG1 
5511 C CG2 . THR D 96  ? 0.9244 0.6527 0.7000 -0.0328 -0.2798 0.0234  96  THR D CG2 
5512 N N   . ARG D 97  ? 0.9550 0.7335 0.7484 -0.0334 -0.2880 0.0180  97  ARG D N   
5513 C CA  . ARG D 97  ? 1.0147 0.8017 0.8086 -0.0315 -0.2893 0.0204  97  ARG D CA  
5514 C C   . ARG D 97  ? 1.0213 0.7972 0.8138 -0.0364 -0.2926 0.0181  97  ARG D C   
5515 O O   . ARG D 97  ? 1.1265 0.8941 0.9139 -0.0347 -0.2927 0.0223  97  ARG D O   
5516 C CB  . ARG D 97  ? 1.0847 0.8985 0.8872 -0.0304 -0.2902 0.0173  97  ARG D CB  
5517 C CG  . ARG D 97  ? 1.1421 0.9682 0.9439 -0.0251 -0.2897 0.0231  97  ARG D CG  
5518 C CD  . ARG D 97  ? 1.2382 1.0885 1.0486 -0.0267 -0.2924 0.0185  97  ARG D CD  
5519 N NE  . ARG D 97  ? 1.3144 1.1808 1.1250 -0.0207 -0.2914 0.0248  97  ARG D NE  
5520 C CZ  . ARG D 97  ? 1.3349 1.1973 1.1428 -0.0194 -0.2926 0.0290  97  ARG D CZ  
5521 N NH1 . ARG D 97  ? 1.2685 1.1114 1.0726 -0.0238 -0.2949 0.0273  97  ARG D NH1 
5522 N NH2 . ARG D 97  ? 1.3685 1.2476 1.1778 -0.0135 -0.2912 0.0354  97  ARG D NH2 
5523 N N   . GLN D 98  ? 1.0277 0.8038 0.8256 -0.0422 -0.2951 0.0116  98  GLN D N   
5524 C CA  . GLN D 98  ? 1.1354 0.9042 0.9334 -0.0468 -0.2983 0.0094  98  GLN D CA  
5525 C C   . GLN D 98  ? 1.2143 0.9762 1.0166 -0.0528 -0.2994 0.0041  98  GLN D C   
5526 O O   . GLN D 98  ? 1.2006 0.9664 1.0076 -0.0535 -0.2978 0.0015  98  GLN D O   
5527 C CB  . GLN D 98  ? 1.1758 0.9629 0.9799 -0.0470 -0.3008 0.0072  98  GLN D CB  
5528 C CG  . GLN D 98  ? 1.2345 1.0411 1.0504 -0.0502 -0.3016 -0.0002 98  GLN D CG  
5529 C CD  . GLN D 98  ? 1.2163 1.0210 1.0384 -0.0569 -0.3046 -0.0062 98  GLN D CD  
5530 O OE1 . GLN D 98  ? 1.2706 1.0638 1.0880 -0.0585 -0.3068 -0.0046 98  GLN D OE1 
5531 N NE2 . GLN D 98  ? 1.1831 0.9990 1.0163 -0.0608 -0.3044 -0.0133 98  GLN D NE2 
5532 N N   . GLY D 99  ? 1.4073 1.1593 1.2086 -0.0570 -0.3019 0.0028  99  GLY D N   
5533 C CA  . GLY D 99  ? 1.4341 1.1782 1.2395 -0.0628 -0.3030 -0.0009 99  GLY D CA  
5534 C C   . GLY D 99  ? 1.4420 1.1735 1.2435 -0.0627 -0.3006 0.0010  99  GLY D C   
5535 O O   . GLY D 99  ? 1.4390 1.1631 1.2324 -0.0589 -0.2985 0.0053  99  GLY D O   
5536 N N   . ALA D 100 ? 1.2686 0.9980 1.0768 -0.0672 -0.3007 -0.0023 100 ALA D N   
5537 C CA  . ALA D 100 ? 1.1498 0.8712 0.9568 -0.0672 -0.2983 -0.0009 100 ALA D CA  
5538 C C   . ALA D 100 ? 1.0992 0.8303 0.9079 -0.0632 -0.2958 -0.0011 100 ALA D C   
5539 O O   . ALA D 100 ? 1.1266 0.8739 0.9443 -0.0632 -0.2955 -0.0052 100 ALA D O   
5540 C CB  . ALA D 100 ? 1.1166 0.8375 0.9334 -0.0723 -0.2983 -0.0042 100 ALA D CB  
5541 N N   . PHE D 101 ? 1.0562 0.7784 0.8564 -0.0600 -0.2938 0.0031  101 PHE D N   
5542 C CA  . PHE D 101 ? 1.0251 0.7551 0.8259 -0.0561 -0.2913 0.0035  101 PHE D CA  
5543 C C   . PHE D 101 ? 1.0256 0.7627 0.8365 -0.0584 -0.2901 -0.0008 101 PHE D C   
5544 O O   . PHE D 101 ? 1.0731 0.8008 0.8844 -0.0607 -0.2893 -0.0004 101 PHE D O   
5545 C CB  . PHE D 101 ? 1.0151 0.7324 0.8054 -0.0529 -0.2891 0.0085  101 PHE D CB  
5546 C CG  . PHE D 101 ? 1.0281 0.7385 0.8099 -0.0504 -0.2891 0.0126  101 PHE D CG  
5547 C CD1 . PHE D 101 ? 1.0488 0.7671 0.8321 -0.0494 -0.2908 0.0126  101 PHE D CD1 
5548 C CD2 . PHE D 101 ? 1.0567 0.7530 0.8296 -0.0490 -0.2871 0.0163  101 PHE D CD2 
5549 C CE1 . PHE D 101 ? 1.0214 0.7331 0.7977 -0.0468 -0.2904 0.0166  101 PHE D CE1 
5550 C CE2 . PHE D 101 ? 1.1140 0.8038 0.8805 -0.0467 -0.2863 0.0196  101 PHE D CE2 
5551 C CZ  . PHE D 101 ? 1.1046 0.8016 0.8728 -0.0454 -0.2879 0.0201  101 PHE D CZ  
5552 N N   . THR D 102 ? 1.0441 0.7986 0.8636 -0.0578 -0.2896 -0.0051 102 THR D N   
5553 C CA  . THR D 102 ? 0.9012 0.6645 0.7328 -0.0605 -0.2882 -0.0105 102 THR D CA  
5554 C C   . THR D 102 ? 0.8420 0.6097 0.6729 -0.0569 -0.2854 -0.0102 102 THR D C   
5555 O O   . THR D 102 ? 0.9865 0.7652 0.8153 -0.0529 -0.2848 -0.0097 102 THR D O   
5556 C CB  . THR D 102 ? 0.8839 0.6652 0.7271 -0.0628 -0.2890 -0.0169 102 THR D CB  
5557 O OG1 . THR D 102 ? 0.9064 0.6849 0.7474 -0.0646 -0.2920 -0.0162 102 THR D OG1 
5558 C CG2 . THR D 102 ? 0.9858 0.7717 0.8433 -0.0674 -0.2872 -0.0230 102 THR D CG2 
5559 N N   . PHE D 103 ? 0.8084 0.5684 0.6414 -0.0583 -0.2836 -0.0102 103 PHE D N   
5560 C CA  . PHE D 103 ? 0.8034 0.5683 0.6377 -0.0556 -0.2809 -0.0110 103 PHE D CA  
5561 C C   . PHE D 103 ? 0.8466 0.6297 0.6949 -0.0573 -0.2794 -0.0185 103 PHE D C   
5562 O O   . PHE D 103 ? 0.8211 0.6121 0.6792 -0.0609 -0.2802 -0.0232 103 PHE D O   
5563 C CB  . PHE D 103 ? 0.8601 0.6109 0.6919 -0.0565 -0.2796 -0.0083 103 PHE D CB  
5564 C CG  . PHE D 103 ? 0.8638 0.5993 0.6817 -0.0544 -0.2801 -0.0019 103 PHE D CG  
5565 C CD1 . PHE D 103 ? 0.9100 0.6349 0.7223 -0.0564 -0.2822 0.0009  103 PHE D CD1 
5566 C CD2 . PHE D 103 ? 0.8762 0.6083 0.6872 -0.0508 -0.2783 0.0009  103 PHE D CD2 
5567 C CE1 . PHE D 103 ? 0.9067 0.6186 0.7073 -0.0548 -0.2821 0.0058  103 PHE D CE1 
5568 C CE2 . PHE D 103 ? 0.8754 0.5942 0.6751 -0.0493 -0.2783 0.0060  103 PHE D CE2 
5569 C CZ  . PHE D 103 ? 0.9120 0.6211 0.7067 -0.0514 -0.2800 0.0081  103 PHE D CZ  
5570 N N   . GLY D 104 ? 0.8415 0.6318 0.6915 -0.0547 -0.2770 -0.0200 104 GLY D N   
5571 C CA  . GLY D 104 ? 0.7959 0.6031 0.6598 -0.0564 -0.2748 -0.0277 104 GLY D CA  
5572 C C   . GLY D 104 ? 0.8667 0.6678 0.7406 -0.0601 -0.2725 -0.0304 104 GLY D C   
5573 O O   . GLY D 104 ? 0.9457 0.7302 0.8146 -0.0606 -0.2726 -0.0255 104 GLY D O   
5574 N N   . GLN D 105 ? 0.9091 0.7249 0.7982 -0.0626 -0.2700 -0.0384 105 GLN D N   
5575 C CA  . GLN D 105 ? 0.8661 0.6779 0.7673 -0.0658 -0.2667 -0.0412 105 GLN D CA  
5576 C C   . GLN D 105 ? 0.8231 0.6273 0.7193 -0.0628 -0.2648 -0.0380 105 GLN D C   
5577 O O   . GLN D 105 ? 0.8550 0.6482 0.7549 -0.0643 -0.2631 -0.0358 105 GLN D O   
5578 C CB  . GLN D 105 ? 0.8767 0.7073 0.7966 -0.0691 -0.2637 -0.0515 105 GLN D CB  
5579 C CG  . GLN D 105 ? 0.8272 0.6772 0.7478 -0.0663 -0.2625 -0.0567 105 GLN D CG  
5580 C CD  . GLN D 105 ? 0.9664 0.8382 0.9033 -0.0700 -0.2607 -0.0672 105 GLN D CD  
5581 O OE1 . GLN D 105 ? 1.1403 1.0131 1.0849 -0.0741 -0.2615 -0.0697 105 GLN D OE1 
5582 N NE2 . GLN D 105 ? 0.9654 0.8555 0.9080 -0.0687 -0.2580 -0.0737 105 GLN D NE2 
5583 N N   . GLY D 106 ? 0.7753 0.5855 0.6634 -0.0585 -0.2648 -0.0374 106 GLY D N   
5584 C CA  . GLY D 106 ? 0.7910 0.5943 0.6738 -0.0556 -0.2631 -0.0345 106 GLY D CA  
5585 C C   . GLY D 106 ? 0.8430 0.6621 0.7326 -0.0540 -0.2601 -0.0407 106 GLY D C   
5586 O O   . GLY D 106 ? 0.9071 0.7425 0.8100 -0.0564 -0.2582 -0.0488 106 GLY D O   
5587 N N   . THR D 107 ? 0.8543 0.6694 0.7350 -0.0501 -0.2595 -0.0374 107 THR D N   
5588 C CA  . THR D 107 ? 0.8670 0.6959 0.7526 -0.0482 -0.2566 -0.0428 107 THR D CA  
5589 C C   . THR D 107 ? 0.9477 0.7642 0.8262 -0.0456 -0.2555 -0.0385 107 THR D C   
5590 O O   . THR D 107 ? 0.9968 0.8006 0.8614 -0.0430 -0.2575 -0.0310 107 THR D O   
5591 C CB  . THR D 107 ? 0.8900 0.7348 0.7699 -0.0446 -0.2576 -0.0435 107 THR D CB  
5592 O OG1 . THR D 107 ? 0.8623 0.7198 0.7491 -0.0471 -0.2587 -0.0477 107 THR D OG1 
5593 C CG2 . THR D 107 ? 0.8986 0.7588 0.7835 -0.0427 -0.2545 -0.0492 107 THR D CG2 
5594 N N   . LYS D 108 ? 0.9563 0.7769 0.8450 -0.0465 -0.2520 -0.0434 108 LYS D N   
5595 C CA  . LYS D 108 ? 1.0229 0.8328 0.9064 -0.0444 -0.2508 -0.0399 108 LYS D CA  
5596 C C   . LYS D 108 ? 1.0582 0.8798 0.9394 -0.0409 -0.2491 -0.0432 108 LYS D C   
5597 O O   . LYS D 108 ? 1.1142 0.9545 1.0037 -0.0412 -0.2475 -0.0505 108 LYS D O   
5598 C CB  . LYS D 108 ? 1.0932 0.8977 0.9897 -0.0476 -0.2478 -0.0421 108 LYS D CB  
5599 C CG  . LYS D 108 ? 1.1601 0.9504 1.0500 -0.0458 -0.2473 -0.0365 108 LYS D CG  
5600 C CD  . LYS D 108 ? 1.0917 0.8773 0.9955 -0.0487 -0.2440 -0.0374 108 LYS D CD  
5601 C CE  . LYS D 108 ? 1.1956 0.9955 1.1168 -0.0502 -0.2393 -0.0468 108 LYS D CE  
5602 N NZ  . LYS D 108 ? 1.3208 1.1159 1.2573 -0.0528 -0.2353 -0.0471 108 LYS D NZ  
5603 N N   . LEU D 109 ? 1.0909 0.9022 0.9611 -0.0376 -0.2495 -0.0378 109 LEU D N   
5604 C CA  . LEU D 109 ? 1.1804 1.0002 1.0473 -0.0340 -0.2479 -0.0398 109 LEU D CA  
5605 C C   . LEU D 109 ? 1.2277 1.0386 1.0969 -0.0341 -0.2457 -0.0398 109 LEU D C   
5606 O O   . LEU D 109 ? 1.2409 1.0351 1.1043 -0.0344 -0.2468 -0.0338 109 LEU D O   
5607 C CB  . LEU D 109 ? 1.1016 0.9181 0.9526 -0.0296 -0.2501 -0.0329 109 LEU D CB  
5608 C CG  . LEU D 109 ? 1.1454 0.9737 0.9923 -0.0253 -0.2486 -0.0341 109 LEU D CG  
5609 C CD1 . LEU D 109 ? 1.2460 1.0811 1.0840 -0.0217 -0.2502 -0.0296 109 LEU D CD1 
5610 C CD2 . LEU D 109 ? 1.1991 1.0148 1.0389 -0.0232 -0.2478 -0.0306 109 LEU D CD2 
5611 N N   . GLU D 110 ? 1.2952 1.1183 1.1733 -0.0338 -0.2424 -0.0469 110 GLU D N   
5612 C CA  . GLU D 110 ? 1.3230 1.1396 1.2041 -0.0334 -0.2399 -0.0476 110 GLU D CA  
5613 C C   . GLU D 110 ? 1.3840 1.2090 1.2591 -0.0295 -0.2389 -0.0495 110 GLU D C   
5614 O O   . GLU D 110 ? 1.3787 1.2185 1.2514 -0.0276 -0.2392 -0.0519 110 GLU D O   
5615 C CB  . GLU D 110 ? 1.4248 1.2470 1.3250 -0.0372 -0.2359 -0.0550 110 GLU D CB  
5616 C CG  . GLU D 110 ? 1.5285 1.3384 1.4348 -0.0406 -0.2362 -0.0513 110 GLU D CG  
5617 C CD  . GLU D 110 ? 1.5413 1.3548 1.4673 -0.0438 -0.2312 -0.0572 110 GLU D CD  
5618 O OE1 . GLU D 110 ? 1.4650 1.2903 1.4001 -0.0435 -0.2275 -0.0650 110 GLU D OE1 
5619 O OE2 . GLU D 110 ? 1.3824 1.1872 1.3155 -0.0464 -0.2307 -0.0541 110 GLU D OE2 
5620 N N   . ILE D 111 ? 1.4004 1.2166 1.2733 -0.0282 -0.2376 -0.0480 111 ILE D N   
5621 C CA  . ILE D 111 ? 1.4446 1.2663 1.3110 -0.0245 -0.2367 -0.0491 111 ILE D CA  
5622 C C   . ILE D 111 ? 1.4938 1.3229 1.3732 -0.0256 -0.2324 -0.0571 111 ILE D C   
5623 O O   . ILE D 111 ? 1.5075 1.3289 1.3965 -0.0282 -0.2306 -0.0579 111 ILE D O   
5624 C CB  . ILE D 111 ? 1.3951 1.1999 1.2465 -0.0218 -0.2389 -0.0405 111 ILE D CB  
5625 C CG1 . ILE D 111 ? 1.3566 1.1528 1.1971 -0.0213 -0.2423 -0.0330 111 ILE D CG1 
5626 C CG2 . ILE D 111 ? 1.4194 1.2303 1.2637 -0.0177 -0.2379 -0.0411 111 ILE D CG2 
5627 C CD1 . ILE D 111 ? 1.3926 1.1731 1.2196 -0.0192 -0.2440 -0.0254 111 ILE D CD1 
5628 N N   . LYS D 112 ? 1.5032 1.3479 1.3833 -0.0234 -0.2305 -0.0629 112 LYS D N   
5629 C CA  . LYS D 112 ? 1.4866 1.3400 1.3786 -0.0242 -0.2261 -0.0714 112 LYS D CA  
5630 C C   . LYS D 112 ? 1.5346 1.3795 1.4167 -0.0207 -0.2261 -0.0681 112 LYS D C   
5631 O O   . LYS D 112 ? 1.4871 1.3355 1.3569 -0.0170 -0.2278 -0.0650 112 LYS D O   
5632 C CB  . LYS D 112 ? 1.4136 1.2922 1.3140 -0.0244 -0.2236 -0.0812 112 LYS D CB  
5633 C CG  . LYS D 112 ? 1.3322 1.2211 1.2433 -0.0281 -0.2234 -0.0855 112 LYS D CG  
5634 C CD  . LYS D 112 ? 1.2682 1.1844 1.1859 -0.0280 -0.2213 -0.0949 112 LYS D CD  
5635 C CE  . LYS D 112 ? 1.1567 1.0843 1.0876 -0.0324 -0.2205 -0.1008 112 LYS D CE  
5636 N NZ  . LYS D 112 ? 1.0487 1.0049 0.9848 -0.0323 -0.2189 -0.1095 112 LYS D NZ  
5637 N N   . ARG D 113 ? 1.5874 1.4218 1.4754 -0.0219 -0.2241 -0.0684 113 ARG D N   
5638 C CA  . ARG D 113 ? 1.5800 1.4065 1.4601 -0.0190 -0.2239 -0.0659 113 ARG D CA  
5639 C C   . ARG D 113 ? 1.6059 1.4425 1.4985 -0.0194 -0.2190 -0.0754 113 ARG D C   
5640 O O   . ARG D 113 ? 1.6192 1.4502 1.5077 -0.0174 -0.2182 -0.0747 113 ARG D O   
5641 C CB  . ARG D 113 ? 1.5513 1.3566 1.4262 -0.0195 -0.2258 -0.0575 113 ARG D CB  
5642 C CG  . ARG D 113 ? 1.5732 1.3677 1.4311 -0.0161 -0.2286 -0.0505 113 ARG D CG  
5643 C CD  . ARG D 113 ? 1.6286 1.4059 1.4845 -0.0169 -0.2293 -0.0447 113 ARG D CD  
5644 N NE  . ARG D 113 ? 1.7218 1.4884 1.5616 -0.0144 -0.2323 -0.0378 113 ARG D NE  
5645 C CZ  . ARG D 113 ? 1.6928 1.4464 1.5284 -0.0144 -0.2331 -0.0330 113 ARG D CZ  
5646 N NH1 . ARG D 113 ? 1.6222 1.3718 1.4682 -0.0164 -0.2312 -0.0333 113 ARG D NH1 
5647 N NH2 . ARG D 113 ? 1.7391 1.4843 1.5605 -0.0125 -0.2354 -0.0277 113 ARG D NH2 
5648 N N   . GLY D 162 ? 1.3921 1.1578 1.6780 -0.0502 -0.1154 0.0550  162 GLY D N   
5649 C CA  . GLY D 162 ? 1.4300 1.1946 1.7075 -0.0512 -0.1201 0.0644  162 GLY D CA  
5650 C C   . GLY D 162 ? 1.4337 1.1972 1.6939 -0.0470 -0.1253 0.0807  162 GLY D C   
5651 O O   . GLY D 162 ? 1.4513 1.2152 1.7065 -0.0472 -0.1280 0.0907  162 GLY D O   
5652 N N   . ASN D 163 ? 1.4037 1.1669 1.6551 -0.0433 -0.1265 0.0831  163 ASN D N   
5653 C CA  . ASN D 163 ? 1.3765 1.1403 1.6110 -0.0394 -0.1316 0.0974  163 ASN D CA  
5654 C C   . ASN D 163 ? 1.4293 1.1896 1.6301 -0.0390 -0.1428 0.0929  163 ASN D C   
5655 O O   . ASN D 163 ? 1.4078 1.1692 1.5920 -0.0364 -0.1479 0.1032  163 ASN D O   
5656 C CB  . ASN D 163 ? 1.3047 1.0721 1.5582 -0.0348 -0.1232 0.1070  163 ASN D CB  
5657 C CG  . ASN D 163 ? 1.2780 1.0435 1.5286 -0.0333 -0.1226 0.0977  163 ASN D CG  
5658 O OD1 . ASN D 163 ? 1.2171 0.9822 1.4495 -0.0304 -0.1279 0.1020  163 ASN D OD1 
5659 N ND2 . ASN D 163 ? 1.2773 1.0423 1.5461 -0.0356 -0.1161 0.0846  163 ASN D ND2 
5660 N N   . SER D 164 ? 1.4258 1.1829 1.6168 -0.0414 -0.1463 0.0779  164 SER D N   
5661 C CA  . SER D 164 ? 1.4523 1.2059 1.6130 -0.0410 -0.1561 0.0733  164 SER D CA  
5662 C C   . SER D 164 ? 1.5485 1.2997 1.6968 -0.0449 -0.1616 0.0605  164 SER D C   
5663 O O   . SER D 164 ? 1.5459 1.2989 1.7107 -0.0479 -0.1571 0.0523  164 SER D O   
5664 C CB  . SER D 164 ? 1.4046 1.1578 1.5651 -0.0382 -0.1543 0.0691  164 SER D CB  
5665 O OG  . SER D 164 ? 1.4192 1.1737 1.5987 -0.0398 -0.1475 0.0568  164 SER D OG  
5666 N N   . GLN D 165 ? 1.6359 1.3837 1.7557 -0.0448 -0.1711 0.0590  165 GLN D N   
5667 C CA  . GLN D 165 ? 1.7574 1.5032 1.8624 -0.0477 -0.1771 0.0482  165 GLN D CA  
5668 C C   . GLN D 165 ? 1.8293 1.5718 1.9083 -0.0460 -0.1845 0.0452  165 GLN D C   
5669 O O   . GLN D 165 ? 1.8619 1.6033 1.9331 -0.0431 -0.1856 0.0523  165 GLN D O   
5670 C CB  . GLN D 165 ? 1.7721 1.5168 1.8706 -0.0502 -0.1810 0.0522  165 GLN D CB  
5671 C CG  . GLN D 165 ? 1.7830 1.5269 1.8697 -0.0484 -0.1846 0.0660  165 GLN D CG  
5672 C CD  . GLN D 165 ? 1.7130 1.4574 1.8031 -0.0506 -0.1851 0.0717  165 GLN D CD  
5673 O OE1 . GLN D 165 ? 1.7132 1.4585 1.8182 -0.0534 -0.1816 0.0665  165 GLN D OE1 
5674 N NE2 . GLN D 165 ? 1.6551 1.3998 1.7318 -0.0496 -0.1893 0.0822  165 GLN D NE2 
5675 N N   . GLU D 166 ? 1.7273 1.4687 1.7933 -0.0479 -0.1892 0.0350  166 GLU D N   
5676 C CA  . GLU D 166 ? 1.6228 1.3612 1.6658 -0.0463 -0.1955 0.0316  166 GLU D CA  
5677 C C   . GLU D 166 ? 1.6197 1.3560 1.6439 -0.0483 -0.2026 0.0270  166 GLU D C   
5678 O O   . GLU D 166 ? 1.6186 1.3572 1.6497 -0.0511 -0.2020 0.0221  166 GLU D O   
5679 C CB  . GLU D 166 ? 1.5940 1.3349 1.6432 -0.0452 -0.1921 0.0221  166 GLU D CB  
5680 C CG  . GLU D 166 ? 1.5892 1.3357 1.6517 -0.0479 -0.1887 0.0098  166 GLU D CG  
5681 C CD  . GLU D 166 ? 1.5368 1.2860 1.5929 -0.0470 -0.1893 -0.0008 166 GLU D CD  
5682 O OE1 . GLU D 166 ? 1.4878 1.2333 1.5281 -0.0443 -0.1929 0.0017  166 GLU D OE1 
5683 O OE2 . GLU D 166 ? 1.4691 1.2251 1.5363 -0.0491 -0.1862 -0.0117 166 GLU D OE2 
5684 N N   . SER D 167 ? 1.5938 1.3260 1.5950 -0.0468 -0.2089 0.0285  167 SER D N   
5685 C CA  . SER D 167 ? 1.5598 1.2896 1.5421 -0.0480 -0.2155 0.0247  167 SER D CA  
5686 C C   . SER D 167 ? 1.5152 1.2442 1.4841 -0.0462 -0.2181 0.0184  167 SER D C   
5687 O O   . SER D 167 ? 1.4691 1.1957 1.4308 -0.0438 -0.2188 0.0219  167 SER D O   
5688 C CB  . SER D 167 ? 1.5246 1.2501 1.4917 -0.0483 -0.2204 0.0335  167 SER D CB  
5689 O OG  . SER D 167 ? 1.5212 1.2447 1.4793 -0.0459 -0.2216 0.0399  167 SER D OG  
5690 N N   . VAL D 168 ? 1.5598 1.2917 1.5257 -0.0472 -0.2195 0.0094  168 VAL D N   
5691 C CA  . VAL D 168 ? 1.5704 1.3034 1.5260 -0.0454 -0.2212 0.0029  168 VAL D CA  
5692 C C   . VAL D 168 ? 1.5701 1.2984 1.5029 -0.0448 -0.2278 0.0045  168 VAL D C   
5693 O O   . VAL D 168 ? 1.5442 1.2726 1.4727 -0.0466 -0.2305 0.0038  168 VAL D O   
5694 C CB  . VAL D 168 ? 1.5386 1.2804 1.5063 -0.0465 -0.2179 -0.0081 168 VAL D CB  
5695 C CG1 . VAL D 168 ? 1.4771 1.2216 1.4385 -0.0441 -0.2179 -0.0140 168 VAL D CG1 
5696 C CG2 . VAL D 168 ? 1.5024 1.2488 1.4955 -0.0482 -0.2108 -0.0098 168 VAL D CG2 
5697 N N   . THR D 169 ? 1.6046 1.3289 1.5238 -0.0424 -0.2301 0.0066  169 THR D N   
5698 C CA  . THR D 169 ? 1.7074 1.4271 1.6062 -0.0417 -0.2354 0.0076  169 THR D CA  
5699 C C   . THR D 169 ? 1.6267 1.3515 1.5223 -0.0415 -0.2364 -0.0003 169 THR D C   
5700 O O   . THR D 169 ? 1.6405 1.3717 1.5439 -0.0406 -0.2336 -0.0069 169 THR D O   
5701 C CB  . THR D 169 ? 1.7187 1.4338 1.6057 -0.0394 -0.2369 0.0107  169 THR D CB  
5702 O OG1 . THR D 169 ? 1.7608 1.4793 1.6564 -0.0377 -0.2333 0.0069  169 THR D OG1 
5703 C CG2 . THR D 169 ? 1.6929 1.4038 1.5777 -0.0398 -0.2376 0.0195  169 THR D CG2 
5704 N N   . GLU D 170 ? 1.5788 1.3015 1.4632 -0.0421 -0.2402 0.0004  170 GLU D N   
5705 C CA  . GLU D 170 ? 1.5822 1.3104 1.4620 -0.0414 -0.2414 -0.0057 170 GLU D CA  
5706 C C   . GLU D 170 ? 1.6711 1.3988 1.5401 -0.0382 -0.2421 -0.0070 170 GLU D C   
5707 O O   . GLU D 170 ? 1.7319 1.4529 1.5938 -0.0370 -0.2427 -0.0027 170 GLU D O   
5708 C CB  . GLU D 170 ? 1.5364 1.2617 1.4063 -0.0425 -0.2452 -0.0036 170 GLU D CB  
5709 C CG  . GLU D 170 ? 1.4886 1.2227 1.3657 -0.0439 -0.2450 -0.0094 170 GLU D CG  
5710 C CD  . GLU D 170 ? 1.4994 1.2410 1.3708 -0.0416 -0.2455 -0.0145 170 GLU D CD  
5711 O OE1 . GLU D 170 ? 1.5221 1.2599 1.3811 -0.0389 -0.2469 -0.0124 170 GLU D OE1 
5712 O OE2 . GLU D 170 ? 1.3749 1.1272 1.2547 -0.0426 -0.2444 -0.0207 170 GLU D OE2 
5713 N N   . GLN D 171 ? 1.6001 1.3358 1.4683 -0.0370 -0.2420 -0.0130 171 GLN D N   
5714 C CA  . GLN D 171 ? 1.6396 1.3761 1.4983 -0.0338 -0.2423 -0.0144 171 GLN D CA  
5715 C C   . GLN D 171 ? 1.7745 1.5011 1.6163 -0.0325 -0.2456 -0.0082 171 GLN D C   
5716 O O   . GLN D 171 ? 1.7646 1.4893 1.5991 -0.0328 -0.2480 -0.0062 171 GLN D O   
5717 C CB  . GLN D 171 ? 1.5569 1.3056 1.4172 -0.0326 -0.2417 -0.0210 171 GLN D CB  
5718 C CG  . GLN D 171 ? 1.5023 1.2629 1.3804 -0.0344 -0.2379 -0.0287 171 GLN D CG  
5719 C CD  . GLN D 171 ? 1.4883 1.2635 1.3673 -0.0332 -0.2373 -0.0357 171 GLN D CD  
5720 O OE1 . GLN D 171 ? 1.5055 1.2819 1.3718 -0.0304 -0.2395 -0.0339 171 GLN D OE1 
5721 N NE2 . GLN D 171 ? 1.5381 1.3255 1.4329 -0.0351 -0.2338 -0.0436 171 GLN D NE2 
5722 N N   . ASP D 172 ? 1.9535 1.6739 1.7897 -0.0311 -0.2455 -0.0054 172 ASP D N   
5723 C CA  . ASP D 172 ? 2.0553 1.7666 1.8771 -0.0303 -0.2480 -0.0001 172 ASP D CA  
5724 C C   . ASP D 172 ? 2.0998 1.8126 1.9114 -0.0277 -0.2489 -0.0013 172 ASP D C   
5725 O O   . ASP D 172 ? 2.0505 1.7723 1.8653 -0.0259 -0.2477 -0.0059 172 ASP D O   
5726 C CB  . ASP D 172 ? 2.0682 1.7740 1.8879 -0.0297 -0.2474 0.0026  172 ASP D CB  
5727 C CG  . ASP D 172 ? 2.1413 1.8432 1.9658 -0.0321 -0.2473 0.0072  172 ASP D CG  
5728 O OD1 . ASP D 172 ? 2.0726 1.7758 1.9030 -0.0342 -0.2476 0.0080  172 ASP D OD1 
5729 O OD2 . ASP D 172 ? 2.1489 1.8472 1.9715 -0.0318 -0.2471 0.0102  172 ASP D OD2 
5730 N N   . SER D 173 ? 2.0475 1.7524 1.8475 -0.0275 -0.2507 0.0030  173 SER D N   
5731 C CA  . SER D 173 ? 1.9954 1.7006 1.7861 -0.0246 -0.2509 0.0032  173 SER D CA  
5732 C C   . SER D 173 ? 2.0057 1.7133 1.7954 -0.0219 -0.2493 0.0012  173 SER D C   
5733 O O   . SER D 173 ? 1.9530 1.6677 1.7414 -0.0192 -0.2484 -0.0011 173 SER D O   
5734 C CB  . SER D 173 ? 1.9474 1.6425 1.7274 -0.0251 -0.2521 0.0079  173 SER D CB  
5735 O OG  . SER D 173 ? 1.8789 1.5731 1.6510 -0.0220 -0.2514 0.0087  173 SER D OG  
5736 N N   . LYS D 174 ? 2.0538 1.7564 1.8441 -0.0226 -0.2489 0.0021  174 LYS D N   
5737 C CA  . LYS D 174 ? 2.0053 1.7115 1.7981 -0.0206 -0.2472 -0.0009 174 LYS D CA  
5738 C C   . LYS D 174 ? 1.9134 1.6301 1.7190 -0.0209 -0.2454 -0.0063 174 LYS D C   
5739 O O   . LYS D 174 ? 1.8865 1.6035 1.7015 -0.0234 -0.2448 -0.0066 174 LYS D O   
5740 C CB  . LYS D 174 ? 2.0159 1.7149 1.8077 -0.0216 -0.2472 0.0016  174 LYS D CB  
5741 C CG  . LYS D 174 ? 1.9641 1.6536 1.7453 -0.0224 -0.2488 0.0064  174 LYS D CG  
5742 C CD  . LYS D 174 ? 1.8406 1.5256 1.6227 -0.0240 -0.2490 0.0089  174 LYS D CD  
5743 C CE  . LYS D 174 ? 1.8794 1.5666 1.6714 -0.0264 -0.2489 0.0103  174 LYS D CE  
5744 N NZ  . LYS D 174 ? 1.8243 1.5091 1.6179 -0.0276 -0.2489 0.0138  174 LYS D NZ  
5745 N N   . ASP D 175 ? 1.9197 1.6458 1.7263 -0.0186 -0.2441 -0.0107 175 ASP D N   
5746 C CA  . ASP D 175 ? 1.8674 1.6056 1.6865 -0.0192 -0.2420 -0.0171 175 ASP D CA  
5747 C C   . ASP D 175 ? 1.8218 1.5595 1.6522 -0.0207 -0.2397 -0.0195 175 ASP D C   
5748 O O   . ASP D 175 ? 1.8542 1.5877 1.6823 -0.0194 -0.2389 -0.0189 175 ASP D O   
5749 C CB  . ASP D 175 ? 1.8292 1.5792 1.6468 -0.0162 -0.2408 -0.0215 175 ASP D CB  
5750 C CG  . ASP D 175 ? 1.8997 1.6459 1.7088 -0.0133 -0.2404 -0.0201 175 ASP D CG  
5751 O OD1 . ASP D 175 ? 1.9886 1.7236 1.7943 -0.0139 -0.2410 -0.0168 175 ASP D OD1 
5752 O OD2 . ASP D 175 ? 1.7872 1.5424 1.5931 -0.0104 -0.2396 -0.0223 175 ASP D OD2 
5753 N N   . SER D 176 ? 1.8201 1.5621 1.6634 -0.0233 -0.2382 -0.0220 176 SER D N   
5754 C CA  . SER D 176 ? 1.6877 1.4296 1.5443 -0.0247 -0.2352 -0.0237 176 SER D CA  
5755 C C   . SER D 176 ? 1.5506 1.3039 1.4236 -0.0267 -0.2320 -0.0307 176 SER D C   
5756 O O   . SER D 176 ? 1.5216 1.2840 1.3948 -0.0269 -0.2325 -0.0346 176 SER D O   
5757 C CB  . SER D 176 ? 1.5812 1.3123 1.4374 -0.0265 -0.2364 -0.0165 176 SER D CB  
5758 O OG  . SER D 176 ? 1.6837 1.4134 1.5389 -0.0286 -0.2384 -0.0139 176 SER D OG  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   1   1   GLN GLN A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  TRP 34  34  34  TRP TRP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  TRP 36  36  36  TRP TRP A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  TRP 47  47  47  TRP TRP A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  MET 90  90  90  MET MET A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 MET 101 101 101 MET MET A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 TRP 114 114 114 TRP TRP A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 THR 127 127 127 THR THR A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 CYS 151 151 151 CYS CYS A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 TRP 165 165 165 TRP TRP A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 HIS 175 175 175 HIS HIS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 GLN 203 203 203 GLN GLN A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 TYR 205 205 205 TYR TYR A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 CYS 207 207 207 CYS CYS A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 HIS 211 211 211 HIS HIS A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 SER 214 214 214 SER SER A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 VAL 218 218 218 VAL VAL A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 LYS 221 221 221 LYS LYS A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 PRO 224 224 224 PRO PRO A . n 
A 1 225 LYS 225 225 ?   ?   ?   A . n 
A 1 226 SER 226 226 ?   ?   ?   A . n 
A 1 227 CYS 227 227 ?   ?   ?   A . n 
A 1 228 ASP 228 228 ?   ?   ?   A . n 
A 1 229 LYS 229 229 ?   ?   ?   A . n 
A 1 230 THR 230 230 ?   ?   ?   A . n 
A 1 231 HIS 231 231 ?   ?   ?   A . n 
A 1 232 THR 232 232 ?   ?   ?   A . n 
B 2 1   ASP 1   1   1   ASP ASP B . n 
B 2 2   ILE 2   2   2   ILE ILE B . n 
B 2 3   VAL 3   3   3   VAL VAL B . n 
B 2 4   MET 4   4   4   MET MET B . n 
B 2 5   THR 5   5   5   THR THR B . n 
B 2 6   GLN 6   6   6   GLN GLN B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   PRO 8   8   8   PRO PRO B . n 
B 2 9   LEU 9   9   9   LEU LEU B . n 
B 2 10  SER 10  10  10  SER SER B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  SER 12  12  12  SER SER B . n 
B 2 13  VAL 13  13  13  VAL VAL B . n 
B 2 14  ALA 14  14  14  ALA ALA B . n 
B 2 15  PRO 15  15  15  PRO PRO B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  GLU 17  17  17  GLU GLU B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  ALA 19  19  19  ALA ALA B . n 
B 2 20  SER 20  20  20  SER SER B . n 
B 2 21  ILE 21  21  21  ILE ILE B . n 
B 2 22  SER 22  22  22  SER SER B . n 
B 2 23  CYS 23  23  23  CYS CYS B . n 
B 2 24  ARG 24  24  24  ARG ARG B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  THR 26  26  26  THR THR B . n 
B 2 27  GLN 27  27  27  GLN GLN B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  LEU 29  29  29  LEU LEU B . n 
B 2 30  LEU 30  30  30  LEU LEU B . n 
B 2 31  ASN 31  31  31  ASN ASN B . n 
B 2 32  ARG 32  32  32  ARG ARG B . n 
B 2 33  ASN 33  33  33  ASN ASN B . n 
B 2 34  GLY 34  34  34  GLY GLY B . n 
B 2 35  ASP 35  35  35  ASP ASP B . n 
B 2 36  ASN 36  36  36  ASN ASN B . n 
B 2 37  TYR 37  37  37  TYR TYR B . n 
B 2 38  LEU 38  38  38  LEU LEU B . n 
B 2 39  GLU 39  39  39  GLU GLU B . n 
B 2 40  TRP 40  40  40  TRP TRP B . n 
B 2 41  TYR 41  41  41  TYR TYR B . n 
B 2 42  LEU 42  42  42  LEU LEU B . n 
B 2 43  ARG 43  43  43  ARG ARG B . n 
B 2 44  ARG 44  44  44  ARG ARG B . n 
B 2 45  PRO 45  45  45  PRO PRO B . n 
B 2 46  GLY 46  46  46  GLY GLY B . n 
B 2 47  ARG 47  47  47  ARG ARG B . n 
B 2 48  SER 48  48  48  SER SER B . n 
B 2 49  PRO 49  49  49  PRO PRO B . n 
B 2 50  GLN 50  50  50  GLN GLN B . n 
B 2 51  LEU 51  51  51  LEU LEU B . n 
B 2 52  LEU 52  52  52  LEU LEU B . n 
B 2 53  ILE 53  53  53  ILE ILE B . n 
B 2 54  TYR 54  54  54  TYR TYR B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  SER 57  57  57  SER SER B . n 
B 2 58  GLU 58  58  58  GLU GLU B . n 
B 2 59  ARG 59  59  59  ARG ARG B . n 
B 2 60  ALA 60  60  60  ALA ALA B . n 
B 2 61  LEU 61  61  61  LEU LEU B . n 
B 2 62  GLY 62  62  62  GLY GLY B . n 
B 2 63  VAL 63  63  63  VAL VAL B . n 
B 2 64  PRO 64  64  64  PRO PRO B . n 
B 2 65  ASP 65  65  65  ASP ASP B . n 
B 2 66  ARG 66  66  66  ARG ARG B . n 
B 2 67  PHE 67  67  67  PHE PHE B . n 
B 2 68  SER 68  68  68  SER SER B . n 
B 2 69  GLY 69  69  69  GLY GLY B . n 
B 2 70  SER 70  70  70  SER SER B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  SER 72  72  72  SER SER B . n 
B 2 73  GLY 73  73  73  GLY GLY B . n 
B 2 74  ARG 74  74  74  ARG ARG B . n 
B 2 75  ASP 75  75  75  ASP ASP B . n 
B 2 76  PHE 76  76  76  PHE PHE B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  LYS 79  79  79  LYS LYS B . n 
B 2 80  ILE 80  80  80  ILE ILE B . n 
B 2 81  SER 81  81  81  SER SER B . n 
B 2 82  ARG 82  82  82  ARG ARG B . n 
B 2 83  VAL 83  83  83  VAL VAL B . n 
B 2 84  GLU 84  84  84  GLU GLU B . n 
B 2 85  ALA 85  85  85  ALA ALA B . n 
B 2 86  GLN 86  86  86  GLN GLN B . n 
B 2 87  ASP 87  87  87  ASP ASP B . n 
B 2 88  VAL 88  88  88  VAL VAL B . n 
B 2 89  GLY 89  89  89  GLY GLY B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  TYR 91  91  91  TYR TYR B . n 
B 2 92  TYR 92  92  92  TYR TYR B . n 
B 2 93  CYS 93  93  93  CYS CYS B . n 
B 2 94  LEU 94  94  94  LEU LEU B . n 
B 2 95  GLN 95  95  95  GLN GLN B . n 
B 2 96  THR 96  96  96  THR THR B . n 
B 2 97  ARG 97  97  97  ARG ARG B . n 
B 2 98  GLN 98  98  98  GLN GLN B . n 
B 2 99  GLY 99  99  99  GLY GLY B . n 
B 2 100 ALA 100 100 100 ALA ALA B . n 
B 2 101 PHE 101 101 101 PHE PHE B . n 
B 2 102 THR 102 102 102 THR THR B . n 
B 2 103 PHE 103 103 103 PHE PHE B . n 
B 2 104 GLY 104 104 104 GLY GLY B . n 
B 2 105 GLN 105 105 105 GLN GLN B . n 
B 2 106 GLY 106 106 106 GLY GLY B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 LYS 108 108 108 LYS LYS B . n 
B 2 109 LEU 109 109 109 LEU LEU B . n 
B 2 110 GLU 110 110 110 GLU GLU B . n 
B 2 111 ILE 111 111 111 ILE ILE B . n 
B 2 112 LYS 112 112 112 LYS LYS B . n 
B 2 113 ARG 113 113 113 ARG ARG B . n 
B 2 114 THR 114 114 114 THR THR B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 ALA 116 116 116 ALA ALA B . n 
B 2 117 ALA 117 117 117 ALA ALA B . n 
B 2 118 PRO 118 118 118 PRO PRO B . n 
B 2 119 SER 119 119 119 SER SER B . n 
B 2 120 VAL 120 120 120 VAL VAL B . n 
B 2 121 PHE 121 121 121 PHE PHE B . n 
B 2 122 ILE 122 122 122 ILE ILE B . n 
B 2 123 PHE 123 123 123 PHE PHE B . n 
B 2 124 PRO 124 124 124 PRO PRO B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 ASP 127 127 127 ASP ASP B . n 
B 2 128 SER 128 128 128 SER SER B . n 
B 2 129 GLN 129 129 129 GLN GLN B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 SER 132 132 132 SER SER B . n 
B 2 133 GLY 133 133 133 GLY GLY B . n 
B 2 134 THR 134 134 134 THR THR B . n 
B 2 135 ALA 135 135 135 ALA ALA B . n 
B 2 136 SER 136 136 136 SER SER B . n 
B 2 137 VAL 137 137 137 VAL VAL B . n 
B 2 138 VAL 138 138 138 VAL VAL B . n 
B 2 139 CYS 139 139 139 CYS CYS B . n 
B 2 140 LEU 140 140 140 LEU LEU B . n 
B 2 141 LEU 141 141 141 LEU LEU B . n 
B 2 142 ASN 142 142 142 ASN ASN B . n 
B 2 143 ASN 143 143 143 ASN ASN B . n 
B 2 144 PHE 144 144 144 PHE PHE B . n 
B 2 145 TYR 145 145 145 TYR TYR B . n 
B 2 146 PRO 146 146 146 PRO PRO B . n 
B 2 147 ARG 147 147 147 ARG ARG B . n 
B 2 148 GLU 148 148 148 GLU GLU B . n 
B 2 149 ALA 149 149 149 ALA ALA B . n 
B 2 150 LYS 150 150 150 LYS LYS B . n 
B 2 151 VAL 151 151 151 VAL VAL B . n 
B 2 152 GLN 152 152 152 GLN GLN B . n 
B 2 153 TRP 153 153 153 TRP TRP B . n 
B 2 154 LYS 154 154 154 LYS LYS B . n 
B 2 155 VAL 155 155 155 VAL VAL B . n 
B 2 156 ASP 156 156 156 ASP ASP B . n 
B 2 157 ASN 157 157 157 ASN ASN B . n 
B 2 158 ALA 158 158 158 ALA ALA B . n 
B 2 159 LEU 159 159 159 LEU LEU B . n 
B 2 160 GLN 160 160 160 GLN GLN B . n 
B 2 161 SER 161 161 161 SER SER B . n 
B 2 162 GLY 162 162 162 GLY GLY B . n 
B 2 163 ASN 163 163 163 ASN ASN B . n 
B 2 164 SER 164 164 164 SER SER B . n 
B 2 165 GLN 165 165 165 GLN GLN B . n 
B 2 166 GLU 166 166 166 GLU GLU B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 VAL 168 168 168 VAL VAL B . n 
B 2 169 THR 169 169 169 THR THR B . n 
B 2 170 GLU 170 170 170 GLU GLU B . n 
B 2 171 GLN 171 171 171 GLN GLN B . n 
B 2 172 ASP 172 172 172 ASP ASP B . n 
B 2 173 SER 173 173 173 SER SER B . n 
B 2 174 LYS 174 174 174 LYS LYS B . n 
B 2 175 ASP 175 175 175 ASP ASP B . n 
B 2 176 SER 176 176 176 SER SER B . n 
B 2 177 THR 177 177 177 THR THR B . n 
B 2 178 TYR 178 178 178 TYR TYR B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 SER 181 181 181 SER SER B . n 
B 2 182 SER 182 182 182 SER SER B . n 
B 2 183 THR 183 183 183 THR THR B . n 
B 2 184 LEU 184 184 184 LEU LEU B . n 
B 2 185 THR 185 185 185 THR THR B . n 
B 2 186 LEU 186 186 186 LEU LEU B . n 
B 2 187 SER 187 187 187 SER SER B . n 
B 2 188 LYS 188 188 188 LYS LYS B . n 
B 2 189 ALA 189 189 189 ALA ALA B . n 
B 2 190 ASP 190 190 190 ASP ASP B . n 
B 2 191 TYR 191 191 191 TYR TYR B . n 
B 2 192 GLU 192 192 192 GLU GLU B . n 
B 2 193 LYS 193 193 193 LYS LYS B . n 
B 2 194 HIS 194 194 194 HIS HIS B . n 
B 2 195 LYS 195 195 195 LYS LYS B . n 
B 2 196 VAL 196 196 196 VAL VAL B . n 
B 2 197 TYR 197 197 197 TYR TYR B . n 
B 2 198 ALA 198 198 198 ALA ALA B . n 
B 2 199 CYS 199 199 199 CYS CYS B . n 
B 2 200 GLU 200 200 200 GLU GLU B . n 
B 2 201 VAL 201 201 201 VAL VAL B . n 
B 2 202 THR 202 202 202 THR THR B . n 
B 2 203 HIS 203 203 203 HIS HIS B . n 
B 2 204 GLN 204 204 204 GLN GLN B . n 
B 2 205 GLY 205 205 205 GLY GLY B . n 
B 2 206 LEU 206 206 206 LEU LEU B . n 
B 2 207 SER 207 207 207 SER SER B . n 
B 2 208 SER 208 208 208 SER SER B . n 
B 2 209 PRO 209 209 209 PRO PRO B . n 
B 2 210 VAL 210 210 210 VAL VAL B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 LYS 212 212 212 LYS LYS B . n 
B 2 213 SER 213 213 213 SER SER B . n 
B 2 214 PHE 214 214 214 PHE PHE B . n 
B 2 215 ASN 215 215 215 ASN ASN B . n 
B 2 216 ARG 216 216 216 ARG ARG B . n 
B 2 217 GLY 217 217 217 GLY GLY B . n 
B 2 218 GLU 218 218 ?   ?   ?   B . n 
B 2 219 CYS 219 219 ?   ?   ?   B . n 
B 2 220 GLY 220 220 ?   ?   ?   B . n 
C 1 1   GLN 1   1   1   GLN GLN C . n 
C 1 2   VAL 2   2   2   VAL VAL C . n 
C 1 3   GLN 3   3   3   GLN GLN C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   GLN 5   5   5   GLN GLN C . n 
C 1 6   GLN 6   6   6   GLN GLN C . n 
C 1 7   TRP 7   7   7   TRP TRP C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   THR 9   9   9   THR THR C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  LEU 12  12  12  LEU LEU C . n 
C 1 13  LYS 13  13  13  LYS LYS C . n 
C 1 14  PRO 14  14  14  PRO PRO C . n 
C 1 15  SER 15  15  15  SER SER C . n 
C 1 16  GLU 16  16  16  GLU GLU C . n 
C 1 17  THR 17  17  17  THR THR C . n 
C 1 18  LEU 18  18  18  LEU LEU C . n 
C 1 19  SER 19  19  19  SER SER C . n 
C 1 20  LEU 20  20  20  LEU LEU C . n 
C 1 21  THR 21  21  21  THR THR C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  VAL 24  24  24  VAL VAL C . n 
C 1 25  TYR 25  25  25  TYR TYR C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  VAL 27  27  27  VAL VAL C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  LEU 29  29  29  LEU LEU C . n 
C 1 30  ARG 30  30  30  ARG ARG C . n 
C 1 31  GLY 31  31  31  GLY GLY C . n 
C 1 32  TYR 32  32  32  TYR TYR C . n 
C 1 33  TYR 33  33  33  TYR TYR C . n 
C 1 34  TRP 34  34  34  TRP TRP C . n 
C 1 35  THR 35  35  35  THR THR C . n 
C 1 36  TRP 36  36  36  TRP TRP C . n 
C 1 37  ILE 37  37  37  ILE ILE C . n 
C 1 38  ARG 38  38  38  ARG ARG C . n 
C 1 39  GLN 39  39  39  GLN GLN C . n 
C 1 40  SER 40  40  40  SER SER C . n 
C 1 41  PRO 41  41  41  PRO PRO C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  LYS 43  43  43  LYS LYS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  LEU 45  45  45  LEU LEU C . n 
C 1 46  GLU 46  46  46  GLU GLU C . n 
C 1 47  TRP 47  47  47  TRP TRP C . n 
C 1 48  ILE 48  48  48  ILE ILE C . n 
C 1 49  GLY 49  49  49  GLY GLY C . n 
C 1 50  GLU 50  50  50  GLU GLU C . n 
C 1 51  ILE 51  51  51  ILE ILE C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  GLU 53  53  53  GLU GLU C . n 
C 1 54  ILE 54  54  54  ILE ILE C . n 
C 1 55  GLY 55  55  55  GLY GLY C . n 
C 1 56  ARG 56  56  56  ARG ARG C . n 
C 1 57  THR 57  57  57  THR THR C . n 
C 1 58  LYS 58  58  58  LYS LYS C . n 
C 1 59  TYR 59  59  59  TYR TYR C . n 
C 1 60  SER 60  60  60  SER SER C . n 
C 1 61  GLN 61  61  61  GLN GLN C . n 
C 1 62  SER 62  62  62  SER SER C . n 
C 1 63  LEU 63  63  63  LEU LEU C . n 
C 1 64  ARG 64  64  64  ARG ARG C . n 
C 1 65  SER 65  65  65  SER SER C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  ALA 67  67  67  ALA ALA C . n 
C 1 68  THR 68  68  68  THR THR C . n 
C 1 69  LEU 69  69  69  LEU LEU C . n 
C 1 70  SER 70  70  70  SER SER C . n 
C 1 71  ILE 71  71  71  ILE ILE C . n 
C 1 72  ASP 72  72  72  ASP ASP C . n 
C 1 73  THR 73  73  73  THR THR C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  GLN 77  77  77  GLN GLN C . n 
C 1 78  PHE 78  78  78  PHE PHE C . n 
C 1 79  SER 79  79  79  SER SER C . n 
C 1 80  LEU 80  80  80  LEU LEU C . n 
C 1 81  ARG 81  81  81  ARG ARG C . n 
C 1 82  LEU 82  82  82  LEU LEU C . n 
C 1 83  THR 83  83  83  THR THR C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  VAL 85  85  85  VAL VAL C . n 
C 1 86  THR 86  86  86  THR THR C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  ALA 88  88  88  ALA ALA C . n 
C 1 89  ASP 89  89  89  ASP ASP C . n 
C 1 90  MET 90  90  90  MET MET C . n 
C 1 91  ALA 91  91  91  ALA ALA C . n 
C 1 92  THR 92  92  92  THR THR C . n 
C 1 93  TYR 93  93  93  TYR TYR C . n 
C 1 94  TYR 94  94  94  TYR TYR C . n 
C 1 95  CYS 95  95  95  CYS CYS C . n 
C 1 96  ALA 96  96  96  ALA ALA C . n 
C 1 97  ARG 97  97  97  ARG ARG C . n 
C 1 98  TRP 98  98  98  TRP TRP C . n 
C 1 99  ARG 99  99  99  ARG ARG C . n 
C 1 100 LEU 100 100 100 LEU LEU C . n 
C 1 101 MET 101 101 101 MET MET C . n 
C 1 102 MET 102 102 102 MET MET C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ASP 104 104 104 ASP ASP C . n 
C 1 105 GLU 105 105 105 GLU GLU C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 THR 107 107 107 THR THR C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 HIS 109 109 109 HIS HIS C . n 
C 1 110 GLY 110 110 110 GLY GLY C . n 
C 1 111 MET 111 111 111 MET MET C . n 
C 1 112 ASP 112 112 112 ASP ASP C . n 
C 1 113 VAL 113 113 113 VAL VAL C . n 
C 1 114 TRP 114 114 114 TRP TRP C . n 
C 1 115 SER 115 115 115 SER SER C . n 
C 1 116 GLN 116 116 116 GLN GLN C . n 
C 1 117 GLY 117 117 117 GLY GLY C . n 
C 1 118 THR 118 118 118 THR THR C . n 
C 1 119 MET 119 119 119 MET MET C . n 
C 1 120 VAL 120 120 120 VAL VAL C . n 
C 1 121 THR 121 121 121 THR THR C . n 
C 1 122 VAL 122 122 122 VAL VAL C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 SER 124 124 124 SER SER C . n 
C 1 125 ALA 125 125 125 ALA ALA C . n 
C 1 126 SER 126 126 126 SER SER C . n 
C 1 127 THR 127 127 127 THR THR C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 PRO 130 130 130 PRO PRO C . n 
C 1 131 SER 131 131 ?   ?   ?   C . n 
C 1 132 VAL 132 132 ?   ?   ?   C . n 
C 1 133 PHE 133 133 ?   ?   ?   C . n 
C 1 134 PRO 134 134 ?   ?   ?   C . n 
C 1 135 LEU 135 135 ?   ?   ?   C . n 
C 1 136 ALA 136 136 ?   ?   ?   C . n 
C 1 137 PRO 137 137 ?   ?   ?   C . n 
C 1 138 SER 138 138 ?   ?   ?   C . n 
C 1 139 SER 139 139 ?   ?   ?   C . n 
C 1 140 LYS 140 140 ?   ?   ?   C . n 
C 1 141 SER 141 141 ?   ?   ?   C . n 
C 1 142 THR 142 142 ?   ?   ?   C . n 
C 1 143 SER 143 143 ?   ?   ?   C . n 
C 1 144 GLY 144 144 ?   ?   ?   C . n 
C 1 145 GLY 145 145 ?   ?   ?   C . n 
C 1 146 THR 146 146 ?   ?   ?   C . n 
C 1 147 ALA 147 147 ?   ?   ?   C . n 
C 1 148 ALA 148 148 ?   ?   ?   C . n 
C 1 149 LEU 149 149 ?   ?   ?   C . n 
C 1 150 GLY 150 150 ?   ?   ?   C . n 
C 1 151 CYS 151 151 151 CYS CYS C . n 
C 1 152 LEU 152 152 152 LEU LEU C . n 
C 1 153 VAL 153 153 153 VAL VAL C . n 
C 1 154 LYS 154 154 154 LYS LYS C . n 
C 1 155 ASP 155 155 155 ASP ASP C . n 
C 1 156 TYR 156 156 156 TYR TYR C . n 
C 1 157 PHE 157 157 157 PHE PHE C . n 
C 1 158 PRO 158 158 158 PRO PRO C . n 
C 1 159 GLU 159 159 159 GLU GLU C . n 
C 1 160 PRO 160 160 160 PRO PRO C . n 
C 1 161 VAL 161 161 161 VAL VAL C . n 
C 1 162 THR 162 162 162 THR THR C . n 
C 1 163 VAL 163 163 163 VAL VAL C . n 
C 1 164 SER 164 164 164 SER SER C . n 
C 1 165 TRP 165 165 165 TRP TRP C . n 
C 1 166 ASN 166 166 ?   ?   ?   C . n 
C 1 167 SER 167 167 ?   ?   ?   C . n 
C 1 168 GLY 168 168 ?   ?   ?   C . n 
C 1 169 ALA 169 169 ?   ?   ?   C . n 
C 1 170 LEU 170 170 ?   ?   ?   C . n 
C 1 171 THR 171 171 ?   ?   ?   C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 GLY 173 173 173 GLY GLY C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 HIS 175 175 175 HIS HIS C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 PRO 178 178 178 PRO PRO C . n 
C 1 179 ALA 179 179 179 ALA ALA C . n 
C 1 180 VAL 180 180 180 VAL VAL C . n 
C 1 181 LEU 181 181 181 LEU LEU C . n 
C 1 182 GLN 182 182 182 GLN GLN C . n 
C 1 183 SER 183 183 183 SER SER C . n 
C 1 184 SER 184 184 184 SER SER C . n 
C 1 185 GLY 185 185 185 GLY GLY C . n 
C 1 186 LEU 186 186 186 LEU LEU C . n 
C 1 187 TYR 187 187 187 TYR TYR C . n 
C 1 188 SER 188 188 188 SER SER C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 SER 190 190 190 SER SER C . n 
C 1 191 SER 191 191 191 SER SER C . n 
C 1 192 VAL 192 192 192 VAL VAL C . n 
C 1 193 VAL 193 193 ?   ?   ?   C . n 
C 1 194 THR 194 194 ?   ?   ?   C . n 
C 1 195 VAL 195 195 ?   ?   ?   C . n 
C 1 196 PRO 196 196 ?   ?   ?   C . n 
C 1 197 SER 197 197 ?   ?   ?   C . n 
C 1 198 SER 198 198 ?   ?   ?   C . n 
C 1 199 SER 199 199 ?   ?   ?   C . n 
C 1 200 LEU 200 200 ?   ?   ?   C . n 
C 1 201 GLY 201 201 ?   ?   ?   C . n 
C 1 202 THR 202 202 ?   ?   ?   C . n 
C 1 203 GLN 203 203 ?   ?   ?   C . n 
C 1 204 THR 204 204 ?   ?   ?   C . n 
C 1 205 TYR 205 205 ?   ?   ?   C . n 
C 1 206 ILE 206 206 ?   ?   ?   C . n 
C 1 207 CYS 207 207 207 CYS CYS C . n 
C 1 208 ASN 208 208 208 ASN ASN C . n 
C 1 209 VAL 209 209 209 VAL VAL C . n 
C 1 210 ASN 210 210 210 ASN ASN C . n 
C 1 211 HIS 211 211 211 HIS HIS C . n 
C 1 212 LYS 212 212 212 LYS LYS C . n 
C 1 213 PRO 213 213 213 PRO PRO C . n 
C 1 214 SER 214 214 214 SER SER C . n 
C 1 215 ASN 215 215 215 ASN ASN C . n 
C 1 216 THR 216 216 216 THR THR C . n 
C 1 217 LYS 217 217 ?   ?   ?   C . n 
C 1 218 VAL 218 218 ?   ?   ?   C . n 
C 1 219 ASP 219 219 ?   ?   ?   C . n 
C 1 220 LYS 220 220 ?   ?   ?   C . n 
C 1 221 LYS 221 221 ?   ?   ?   C . n 
C 1 222 VAL 222 222 ?   ?   ?   C . n 
C 1 223 GLU 223 223 ?   ?   ?   C . n 
C 1 224 PRO 224 224 ?   ?   ?   C . n 
C 1 225 LYS 225 225 ?   ?   ?   C . n 
C 1 226 SER 226 226 ?   ?   ?   C . n 
C 1 227 CYS 227 227 ?   ?   ?   C . n 
C 1 228 ASP 228 228 ?   ?   ?   C . n 
C 1 229 LYS 229 229 ?   ?   ?   C . n 
C 1 230 THR 230 230 ?   ?   ?   C . n 
C 1 231 HIS 231 231 ?   ?   ?   C . n 
C 1 232 THR 232 232 ?   ?   ?   C . n 
D 2 1   ASP 1   1   1   ASP ASP D . n 
D 2 2   ILE 2   2   2   ILE ILE D . n 
D 2 3   VAL 3   3   3   VAL VAL D . n 
D 2 4   MET 4   4   4   MET MET D . n 
D 2 5   THR 5   5   5   THR THR D . n 
D 2 6   GLN 6   6   6   GLN GLN D . n 
D 2 7   SER 7   7   7   SER SER D . n 
D 2 8   PRO 8   8   8   PRO PRO D . n 
D 2 9   LEU 9   9   9   LEU LEU D . n 
D 2 10  SER 10  10  10  SER SER D . n 
D 2 11  LEU 11  11  11  LEU LEU D . n 
D 2 12  SER 12  12  12  SER SER D . n 
D 2 13  VAL 13  13  13  VAL VAL D . n 
D 2 14  ALA 14  14  14  ALA ALA D . n 
D 2 15  PRO 15  15  15  PRO PRO D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  GLU 17  17  17  GLU GLU D . n 
D 2 18  ALA 18  18  18  ALA ALA D . n 
D 2 19  ALA 19  19  19  ALA ALA D . n 
D 2 20  SER 20  20  20  SER SER D . n 
D 2 21  ILE 21  21  21  ILE ILE D . n 
D 2 22  SER 22  22  22  SER SER D . n 
D 2 23  CYS 23  23  23  CYS CYS D . n 
D 2 24  ARG 24  24  24  ARG ARG D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  THR 26  26  26  THR THR D . n 
D 2 27  GLN 27  27  27  GLN GLN D . n 
D 2 28  SER 28  28  28  SER SER D . n 
D 2 29  LEU 29  29  29  LEU LEU D . n 
D 2 30  LEU 30  30  30  LEU LEU D . n 
D 2 31  ASN 31  31  31  ASN ASN D . n 
D 2 32  ARG 32  32  32  ARG ARG D . n 
D 2 33  ASN 33  33  33  ASN ASN D . n 
D 2 34  GLY 34  34  34  GLY GLY D . n 
D 2 35  ASP 35  35  35  ASP ASP D . n 
D 2 36  ASN 36  36  36  ASN ASN D . n 
D 2 37  TYR 37  37  37  TYR TYR D . n 
D 2 38  LEU 38  38  38  LEU LEU D . n 
D 2 39  GLU 39  39  39  GLU GLU D . n 
D 2 40  TRP 40  40  40  TRP TRP D . n 
D 2 41  TYR 41  41  41  TYR TYR D . n 
D 2 42  LEU 42  42  42  LEU LEU D . n 
D 2 43  ARG 43  43  43  ARG ARG D . n 
D 2 44  ARG 44  44  44  ARG ARG D . n 
D 2 45  PRO 45  45  45  PRO PRO D . n 
D 2 46  GLY 46  46  46  GLY GLY D . n 
D 2 47  ARG 47  47  47  ARG ARG D . n 
D 2 48  SER 48  48  48  SER SER D . n 
D 2 49  PRO 49  49  49  PRO PRO D . n 
D 2 50  GLN 50  50  50  GLN GLN D . n 
D 2 51  LEU 51  51  51  LEU LEU D . n 
D 2 52  LEU 52  52  52  LEU LEU D . n 
D 2 53  ILE 53  53  53  ILE ILE D . n 
D 2 54  TYR 54  54  54  TYR TYR D . n 
D 2 55  LEU 55  55  55  LEU LEU D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  SER 57  57  57  SER SER D . n 
D 2 58  GLU 58  58  58  GLU GLU D . n 
D 2 59  ARG 59  59  59  ARG ARG D . n 
D 2 60  ALA 60  60  60  ALA ALA D . n 
D 2 61  LEU 61  61  61  LEU LEU D . n 
D 2 62  GLY 62  62  62  GLY GLY D . n 
D 2 63  VAL 63  63  63  VAL VAL D . n 
D 2 64  PRO 64  64  64  PRO PRO D . n 
D 2 65  ASP 65  65  65  ASP ASP D . n 
D 2 66  ARG 66  66  66  ARG ARG D . n 
D 2 67  PHE 67  67  67  PHE PHE D . n 
D 2 68  SER 68  68  68  SER SER D . n 
D 2 69  GLY 69  69  69  GLY GLY D . n 
D 2 70  SER 70  70  70  SER SER D . n 
D 2 71  GLY 71  71  71  GLY GLY D . n 
D 2 72  SER 72  72  72  SER SER D . n 
D 2 73  GLY 73  73  73  GLY GLY D . n 
D 2 74  ARG 74  74  74  ARG ARG D . n 
D 2 75  ASP 75  75  75  ASP ASP D . n 
D 2 76  PHE 76  76  76  PHE PHE D . n 
D 2 77  THR 77  77  77  THR THR D . n 
D 2 78  LEU 78  78  78  LEU LEU D . n 
D 2 79  LYS 79  79  79  LYS LYS D . n 
D 2 80  ILE 80  80  80  ILE ILE D . n 
D 2 81  SER 81  81  81  SER SER D . n 
D 2 82  ARG 82  82  82  ARG ARG D . n 
D 2 83  VAL 83  83  83  VAL VAL D . n 
D 2 84  GLU 84  84  84  GLU GLU D . n 
D 2 85  ALA 85  85  85  ALA ALA D . n 
D 2 86  GLN 86  86  86  GLN GLN D . n 
D 2 87  ASP 87  87  87  ASP ASP D . n 
D 2 88  VAL 88  88  88  VAL VAL D . n 
D 2 89  GLY 89  89  89  GLY GLY D . n 
D 2 90  THR 90  90  90  THR THR D . n 
D 2 91  TYR 91  91  91  TYR TYR D . n 
D 2 92  TYR 92  92  92  TYR TYR D . n 
D 2 93  CYS 93  93  93  CYS CYS D . n 
D 2 94  LEU 94  94  94  LEU LEU D . n 
D 2 95  GLN 95  95  95  GLN GLN D . n 
D 2 96  THR 96  96  96  THR THR D . n 
D 2 97  ARG 97  97  97  ARG ARG D . n 
D 2 98  GLN 98  98  98  GLN GLN D . n 
D 2 99  GLY 99  99  99  GLY GLY D . n 
D 2 100 ALA 100 100 100 ALA ALA D . n 
D 2 101 PHE 101 101 101 PHE PHE D . n 
D 2 102 THR 102 102 102 THR THR D . n 
D 2 103 PHE 103 103 103 PHE PHE D . n 
D 2 104 GLY 104 104 104 GLY GLY D . n 
D 2 105 GLN 105 105 105 GLN GLN D . n 
D 2 106 GLY 106 106 106 GLY GLY D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 LYS 108 108 108 LYS LYS D . n 
D 2 109 LEU 109 109 109 LEU LEU D . n 
D 2 110 GLU 110 110 110 GLU GLU D . n 
D 2 111 ILE 111 111 111 ILE ILE D . n 
D 2 112 LYS 112 112 112 LYS LYS D . n 
D 2 113 ARG 113 113 113 ARG ARG D . n 
D 2 114 THR 114 114 ?   ?   ?   D . n 
D 2 115 VAL 115 115 ?   ?   ?   D . n 
D 2 116 ALA 116 116 ?   ?   ?   D . n 
D 2 117 ALA 117 117 ?   ?   ?   D . n 
D 2 118 PRO 118 118 ?   ?   ?   D . n 
D 2 119 SER 119 119 ?   ?   ?   D . n 
D 2 120 VAL 120 120 ?   ?   ?   D . n 
D 2 121 PHE 121 121 ?   ?   ?   D . n 
D 2 122 ILE 122 122 ?   ?   ?   D . n 
D 2 123 PHE 123 123 ?   ?   ?   D . n 
D 2 124 PRO 124 124 ?   ?   ?   D . n 
D 2 125 PRO 125 125 ?   ?   ?   D . n 
D 2 126 SER 126 126 ?   ?   ?   D . n 
D 2 127 ASP 127 127 ?   ?   ?   D . n 
D 2 128 SER 128 128 ?   ?   ?   D . n 
D 2 129 GLN 129 129 ?   ?   ?   D . n 
D 2 130 LEU 130 130 ?   ?   ?   D . n 
D 2 131 LYS 131 131 ?   ?   ?   D . n 
D 2 132 SER 132 132 ?   ?   ?   D . n 
D 2 133 GLY 133 133 ?   ?   ?   D . n 
D 2 134 THR 134 134 ?   ?   ?   D . n 
D 2 135 ALA 135 135 ?   ?   ?   D . n 
D 2 136 SER 136 136 ?   ?   ?   D . n 
D 2 137 VAL 137 137 ?   ?   ?   D . n 
D 2 138 VAL 138 138 ?   ?   ?   D . n 
D 2 139 CYS 139 139 ?   ?   ?   D . n 
D 2 140 LEU 140 140 ?   ?   ?   D . n 
D 2 141 LEU 141 141 ?   ?   ?   D . n 
D 2 142 ASN 142 142 ?   ?   ?   D . n 
D 2 143 ASN 143 143 ?   ?   ?   D . n 
D 2 144 PHE 144 144 ?   ?   ?   D . n 
D 2 145 TYR 145 145 ?   ?   ?   D . n 
D 2 146 PRO 146 146 ?   ?   ?   D . n 
D 2 147 ARG 147 147 ?   ?   ?   D . n 
D 2 148 GLU 148 148 ?   ?   ?   D . n 
D 2 149 ALA 149 149 ?   ?   ?   D . n 
D 2 150 LYS 150 150 ?   ?   ?   D . n 
D 2 151 VAL 151 151 ?   ?   ?   D . n 
D 2 152 GLN 152 152 ?   ?   ?   D . n 
D 2 153 TRP 153 153 ?   ?   ?   D . n 
D 2 154 LYS 154 154 ?   ?   ?   D . n 
D 2 155 VAL 155 155 ?   ?   ?   D . n 
D 2 156 ASP 156 156 ?   ?   ?   D . n 
D 2 157 ASN 157 157 ?   ?   ?   D . n 
D 2 158 ALA 158 158 ?   ?   ?   D . n 
D 2 159 LEU 159 159 ?   ?   ?   D . n 
D 2 160 GLN 160 160 ?   ?   ?   D . n 
D 2 161 SER 161 161 ?   ?   ?   D . n 
D 2 162 GLY 162 162 162 GLY GLY D . n 
D 2 163 ASN 163 163 163 ASN ASN D . n 
D 2 164 SER 164 164 164 SER SER D . n 
D 2 165 GLN 165 165 165 GLN GLN D . n 
D 2 166 GLU 166 166 166 GLU GLU D . n 
D 2 167 SER 167 167 167 SER SER D . n 
D 2 168 VAL 168 168 168 VAL VAL D . n 
D 2 169 THR 169 169 169 THR THR D . n 
D 2 170 GLU 170 170 170 GLU GLU D . n 
D 2 171 GLN 171 171 171 GLN GLN D . n 
D 2 172 ASP 172 172 172 ASP ASP D . n 
D 2 173 SER 173 173 173 SER SER D . n 
D 2 174 LYS 174 174 174 LYS LYS D . n 
D 2 175 ASP 175 175 175 ASP ASP D . n 
D 2 176 SER 176 176 176 SER SER D . n 
D 2 177 THR 177 177 ?   ?   ?   D . n 
D 2 178 TYR 178 178 ?   ?   ?   D . n 
D 2 179 SER 179 179 ?   ?   ?   D . n 
D 2 180 LEU 180 180 ?   ?   ?   D . n 
D 2 181 SER 181 181 ?   ?   ?   D . n 
D 2 182 SER 182 182 ?   ?   ?   D . n 
D 2 183 THR 183 183 ?   ?   ?   D . n 
D 2 184 LEU 184 184 ?   ?   ?   D . n 
D 2 185 THR 185 185 ?   ?   ?   D . n 
D 2 186 LEU 186 186 ?   ?   ?   D . n 
D 2 187 SER 187 187 ?   ?   ?   D . n 
D 2 188 LYS 188 188 ?   ?   ?   D . n 
D 2 189 ALA 189 189 ?   ?   ?   D . n 
D 2 190 ASP 190 190 ?   ?   ?   D . n 
D 2 191 TYR 191 191 ?   ?   ?   D . n 
D 2 192 GLU 192 192 ?   ?   ?   D . n 
D 2 193 LYS 193 193 ?   ?   ?   D . n 
D 2 194 HIS 194 194 ?   ?   ?   D . n 
D 2 195 LYS 195 195 ?   ?   ?   D . n 
D 2 196 VAL 196 196 ?   ?   ?   D . n 
D 2 197 TYR 197 197 ?   ?   ?   D . n 
D 2 198 ALA 198 198 ?   ?   ?   D . n 
D 2 199 CYS 199 199 ?   ?   ?   D . n 
D 2 200 GLU 200 200 ?   ?   ?   D . n 
D 2 201 VAL 201 201 ?   ?   ?   D . n 
D 2 202 THR 202 202 ?   ?   ?   D . n 
D 2 203 HIS 203 203 ?   ?   ?   D . n 
D 2 204 GLN 204 204 ?   ?   ?   D . n 
D 2 205 GLY 205 205 ?   ?   ?   D . n 
D 2 206 LEU 206 206 ?   ?   ?   D . n 
D 2 207 SER 207 207 ?   ?   ?   D . n 
D 2 208 SER 208 208 ?   ?   ?   D . n 
D 2 209 PRO 209 209 ?   ?   ?   D . n 
D 2 210 VAL 210 210 ?   ?   ?   D . n 
D 2 211 THR 211 211 ?   ?   ?   D . n 
D 2 212 LYS 212 212 ?   ?   ?   D . n 
D 2 213 SER 213 213 ?   ?   ?   D . n 
D 2 214 PHE 214 214 ?   ?   ?   D . n 
D 2 215 ASN 215 215 ?   ?   ?   D . n 
D 2 216 ARG 216 216 ?   ?   ?   D . n 
D 2 217 GLY 217 217 ?   ?   ?   D . n 
D 2 218 GLU 218 218 ?   ?   ?   D . n 
D 2 219 CYS 219 219 ?   ?   ?   D . n 
D 2 220 GLY 220 220 ?   ?   ?   D . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yangbei@shanghaitech.edu.cn 
_pdbx_contact_author.name_first         Bei 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5389-3859 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B 
2 1 C,D 
# 
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)' 3500  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  20100 ? 
2 'ABSA (A^2)' 2170  ? 
2 MORE         -12   ? 
2 'SSA (A^2)'  15400 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2023-08-09 
# 
_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_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -14.4640 
_pdbx_refine_tls.origin_y         15.8549 
_pdbx_refine_tls.origin_z         -22.6410 
_pdbx_refine_tls.T[1][1]          0.8583 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0120 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.2451 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.5322 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0023 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6138 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.9815 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0137 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.4615 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          -0.1365 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0509 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.0630 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0207 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0809 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0980 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0402 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0598 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0405 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1013 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0140 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0501 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.19.2_4158 1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.19.2_4158 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27        3 
# 
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 SER A 15  ? ? 77.23   -1.87   
2  1 ASP A 104 ? ? 70.23   -8.27   
3  1 LEU B 52  ? ? -106.04 -66.42  
4  1 ASN B 143 ? ? 54.06   72.16   
5  1 SER B 173 ? ? -66.57  1.63    
6  1 LYS B 195 ? ? -103.61 -67.12  
7  1 SER D 20  ? ? -150.20 81.28   
8  1 LEU D 29  ? ? -101.74 78.29   
9  1 ASN D 31  ? ? -110.45 -169.98 
10 1 SER D 57  ? ? -141.80 -22.75  
# 
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 A LYS 225 ? A LYS 225 
2   1 Y 1 A SER 226 ? A SER 226 
3   1 Y 1 A CYS 227 ? A CYS 227 
4   1 Y 1 A ASP 228 ? A ASP 228 
5   1 Y 1 A LYS 229 ? A LYS 229 
6   1 Y 1 A THR 230 ? A THR 230 
7   1 Y 1 A HIS 231 ? A HIS 231 
8   1 Y 1 A THR 232 ? A THR 232 
9   1 Y 1 B GLU 218 ? B GLU 218 
10  1 Y 1 B CYS 219 ? B CYS 219 
11  1 Y 1 B GLY 220 ? B GLY 220 
12  1 Y 1 C SER 131 ? C SER 131 
13  1 Y 1 C VAL 132 ? C VAL 132 
14  1 Y 1 C PHE 133 ? C PHE 133 
15  1 Y 1 C PRO 134 ? C PRO 134 
16  1 Y 1 C LEU 135 ? C LEU 135 
17  1 Y 1 C ALA 136 ? C ALA 136 
18  1 Y 1 C PRO 137 ? C PRO 137 
19  1 Y 1 C SER 138 ? C SER 138 
20  1 Y 1 C SER 139 ? C SER 139 
21  1 Y 1 C LYS 140 ? C LYS 140 
22  1 Y 1 C SER 141 ? C SER 141 
23  1 Y 1 C THR 142 ? C THR 142 
24  1 Y 1 C SER 143 ? C SER 143 
25  1 Y 1 C GLY 144 ? C GLY 144 
26  1 Y 1 C GLY 145 ? C GLY 145 
27  1 Y 1 C THR 146 ? C THR 146 
28  1 Y 1 C ALA 147 ? C ALA 147 
29  1 Y 1 C ALA 148 ? C ALA 148 
30  1 Y 1 C LEU 149 ? C LEU 149 
31  1 Y 1 C GLY 150 ? C GLY 150 
32  1 Y 1 C ASN 166 ? C ASN 166 
33  1 Y 1 C SER 167 ? C SER 167 
34  1 Y 1 C GLY 168 ? C GLY 168 
35  1 Y 1 C ALA 169 ? C ALA 169 
36  1 Y 1 C LEU 170 ? C LEU 170 
37  1 Y 1 C THR 171 ? C THR 171 
38  1 Y 1 C VAL 193 ? C VAL 193 
39  1 Y 1 C THR 194 ? C THR 194 
40  1 Y 1 C VAL 195 ? C VAL 195 
41  1 Y 1 C PRO 196 ? C PRO 196 
42  1 Y 1 C SER 197 ? C SER 197 
43  1 Y 1 C SER 198 ? C SER 198 
44  1 Y 1 C SER 199 ? C SER 199 
45  1 Y 1 C LEU 200 ? C LEU 200 
46  1 Y 1 C GLY 201 ? C GLY 201 
47  1 Y 1 C THR 202 ? C THR 202 
48  1 Y 1 C GLN 203 ? C GLN 203 
49  1 Y 1 C THR 204 ? C THR 204 
50  1 Y 1 C TYR 205 ? C TYR 205 
51  1 Y 1 C ILE 206 ? C ILE 206 
52  1 Y 1 C LYS 217 ? C LYS 217 
53  1 Y 1 C VAL 218 ? C VAL 218 
54  1 Y 1 C ASP 219 ? C ASP 219 
55  1 Y 1 C LYS 220 ? C LYS 220 
56  1 Y 1 C LYS 221 ? C LYS 221 
57  1 Y 1 C VAL 222 ? C VAL 222 
58  1 Y 1 C GLU 223 ? C GLU 223 
59  1 Y 1 C PRO 224 ? C PRO 224 
60  1 Y 1 C LYS 225 ? C LYS 225 
61  1 Y 1 C SER 226 ? C SER 226 
62  1 Y 1 C CYS 227 ? C CYS 227 
63  1 Y 1 C ASP 228 ? C ASP 228 
64  1 Y 1 C LYS 229 ? C LYS 229 
65  1 Y 1 C THR 230 ? C THR 230 
66  1 Y 1 C HIS 231 ? C HIS 231 
67  1 Y 1 C THR 232 ? C THR 232 
68  1 Y 1 D THR 114 ? D THR 114 
69  1 Y 1 D VAL 115 ? D VAL 115 
70  1 Y 1 D ALA 116 ? D ALA 116 
71  1 Y 1 D ALA 117 ? D ALA 117 
72  1 Y 1 D PRO 118 ? D PRO 118 
73  1 Y 1 D SER 119 ? D SER 119 
74  1 Y 1 D VAL 120 ? D VAL 120 
75  1 Y 1 D PHE 121 ? D PHE 121 
76  1 Y 1 D ILE 122 ? D ILE 122 
77  1 Y 1 D PHE 123 ? D PHE 123 
78  1 Y 1 D PRO 124 ? D PRO 124 
79  1 Y 1 D PRO 125 ? D PRO 125 
80  1 Y 1 D SER 126 ? D SER 126 
81  1 Y 1 D ASP 127 ? D ASP 127 
82  1 Y 1 D SER 128 ? D SER 128 
83  1 Y 1 D GLN 129 ? D GLN 129 
84  1 Y 1 D LEU 130 ? D LEU 130 
85  1 Y 1 D LYS 131 ? D LYS 131 
86  1 Y 1 D SER 132 ? D SER 132 
87  1 Y 1 D GLY 133 ? D GLY 133 
88  1 Y 1 D THR 134 ? D THR 134 
89  1 Y 1 D ALA 135 ? D ALA 135 
90  1 Y 1 D SER 136 ? D SER 136 
91  1 Y 1 D VAL 137 ? D VAL 137 
92  1 Y 1 D VAL 138 ? D VAL 138 
93  1 Y 1 D CYS 139 ? D CYS 139 
94  1 Y 1 D LEU 140 ? D LEU 140 
95  1 Y 1 D LEU 141 ? D LEU 141 
96  1 Y 1 D ASN 142 ? D ASN 142 
97  1 Y 1 D ASN 143 ? D ASN 143 
98  1 Y 1 D PHE 144 ? D PHE 144 
99  1 Y 1 D TYR 145 ? D TYR 145 
100 1 Y 1 D PRO 146 ? D PRO 146 
101 1 Y 1 D ARG 147 ? D ARG 147 
102 1 Y 1 D GLU 148 ? D GLU 148 
103 1 Y 1 D ALA 149 ? D ALA 149 
104 1 Y 1 D LYS 150 ? D LYS 150 
105 1 Y 1 D VAL 151 ? D VAL 151 
106 1 Y 1 D GLN 152 ? D GLN 152 
107 1 Y 1 D TRP 153 ? D TRP 153 
108 1 Y 1 D LYS 154 ? D LYS 154 
109 1 Y 1 D VAL 155 ? D VAL 155 
110 1 Y 1 D ASP 156 ? D ASP 156 
111 1 Y 1 D ASN 157 ? D ASN 157 
112 1 Y 1 D ALA 158 ? D ALA 158 
113 1 Y 1 D LEU 159 ? D LEU 159 
114 1 Y 1 D GLN 160 ? D GLN 160 
115 1 Y 1 D SER 161 ? D SER 161 
116 1 Y 1 D THR 177 ? D THR 177 
117 1 Y 1 D TYR 178 ? D TYR 178 
118 1 Y 1 D SER 179 ? D SER 179 
119 1 Y 1 D LEU 180 ? D LEU 180 
120 1 Y 1 D SER 181 ? D SER 181 
121 1 Y 1 D SER 182 ? D SER 182 
122 1 Y 1 D THR 183 ? D THR 183 
123 1 Y 1 D LEU 184 ? D LEU 184 
124 1 Y 1 D THR 185 ? D THR 185 
125 1 Y 1 D LEU 186 ? D LEU 186 
126 1 Y 1 D SER 187 ? D SER 187 
127 1 Y 1 D LYS 188 ? D LYS 188 
128 1 Y 1 D ALA 189 ? D ALA 189 
129 1 Y 1 D ASP 190 ? D ASP 190 
130 1 Y 1 D TYR 191 ? D TYR 191 
131 1 Y 1 D GLU 192 ? D GLU 192 
132 1 Y 1 D LYS 193 ? D LYS 193 
133 1 Y 1 D HIS 194 ? D HIS 194 
134 1 Y 1 D LYS 195 ? D LYS 195 
135 1 Y 1 D VAL 196 ? D VAL 196 
136 1 Y 1 D TYR 197 ? D TYR 197 
137 1 Y 1 D ALA 198 ? D ALA 198 
138 1 Y 1 D CYS 199 ? D CYS 199 
139 1 Y 1 D GLU 200 ? D GLU 200 
140 1 Y 1 D VAL 201 ? D VAL 201 
141 1 Y 1 D THR 202 ? D THR 202 
142 1 Y 1 D HIS 203 ? D HIS 203 
143 1 Y 1 D GLN 204 ? D GLN 204 
144 1 Y 1 D GLY 205 ? D GLY 205 
145 1 Y 1 D LEU 206 ? D LEU 206 
146 1 Y 1 D SER 207 ? D SER 207 
147 1 Y 1 D SER 208 ? D SER 208 
148 1 Y 1 D PRO 209 ? D PRO 209 
149 1 Y 1 D VAL 210 ? D VAL 210 
150 1 Y 1 D THR 211 ? D THR 211 
151 1 Y 1 D LYS 212 ? D LYS 212 
152 1 Y 1 D SER 213 ? D SER 213 
153 1 Y 1 D PHE 214 ? D PHE 214 
154 1 Y 1 D ASN 215 ? D ASN 215 
155 1 Y 1 D ARG 216 ? D ARG 216 
156 1 Y 1 D GLY 217 ? D GLY 217 
157 1 Y 1 D GLU 218 ? D GLU 218 
158 1 Y 1 D CYS 219 ? D CYS 219 
159 1 Y 1 D GLY 220 ? D GLY 220 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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                ? 
# 
