data_9DXV
# 
_entry.id   9DXV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9DXV         pdb_00009dxv 10.2210/pdb9dxv/pdb 
WWPDB D_1000289034 ?            ?                   
# 
_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       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DXV 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mark.white@sydney.edu.au 
_pdbx_contact_author.name_first         Mark 
_pdbx_contact_author.name_last          White 
_pdbx_contact_author.name_mi            D 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1431-0339 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jiramongkol, Y.' 1 ? 
'Patel, K.'       2 ? 
'White, M.D.'     3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                4761 
_citation.page_last                 4761 
_citation.title                     
'An mRNA-display derived cyclic peptide scaffold reveals the substrate binding interactions of an N-terminal cysteine oxidase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59960-3 
_citation.pdbx_database_id_PubMed   40404614 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jiramongkol, Y.'    1  0000-0003-1824-4313 
primary 'Patel, K.'          2  0000-0003-3034-3840 
primary 'Johansen-Leete, J.' 3  ?                   
primary 'Maxwell, J.W.C.'    4  ?                   
primary 'Chang, Y.'          5  ?                   
primary 'Du, J.J.'           6  0000-0002-7750-4413 
primary 'Passioura, T.'      7  ?                   
primary 'Cook, K.M.'         8  0000-0002-0503-7166 
primary 'Payne, R.J.'        9  0000-0002-3618-9226 
primary 'White, M.D.'        10 0000-0002-1431-0339 
# 
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 '2-aminoethanethiol dioxygenase' 29841.811 1   1.13.11.19 ? ? ? 
2 polymer     syn CP6-L8K-Ser                      1867.182  1   ?          ? ? ? 
3 non-polymer syn 'COBALT (II) ION'                58.933    1   ?          ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                   35.453    1   ?          ? ? ? 
5 non-polymer syn GLYCEROL                         92.094    8   ?          ? ? ? 
6 non-polymer syn 'THIOCYANATE ION'                58.082    4   ?          ? ? ? 
7 water       nat water                            18.015    221 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cysteamine dioxygenase' 
# 
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  
;SMPRDNMASLIQRIARQASLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLP
PNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQP
REREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSAS
DLPREVWLLETPQADDFWCEGEPYPGPKVFP
;
;SMPRDNMASLIQRIARQASLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLP
PNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQP
REREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSAS
DLPREVWLLETPQADDFWCEGEPYPGPKVFP
;
A ? 
2 'polypeptide(L)' no yes '(ACE)YIVKTFW(A1BDE)GSHRQC(NH2)' XYIVKTFWKGSHRQCX B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'COBALT (II) ION' CO  
4 'CHLORIDE ION'    CL  
5 GLYCEROL          GOL 
6 'THIOCYANATE ION' SCN 
7 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER   n 
1 2   MET   n 
1 3   PRO   n 
1 4   ARG   n 
1 5   ASP   n 
1 6   ASN   n 
1 7   MET   n 
1 8   ALA   n 
1 9   SER   n 
1 10  LEU   n 
1 11  ILE   n 
1 12  GLN   n 
1 13  ARG   n 
1 14  ILE   n 
1 15  ALA   n 
1 16  ARG   n 
1 17  GLN   n 
1 18  ALA   n 
1 19  SER   n 
1 20  LEU   n 
1 21  THR   n 
1 22  PHE   n 
1 23  ARG   n 
1 24  GLY   n 
1 25  SER   n 
1 26  GLY   n 
1 27  GLY   n 
1 28  GLY   n 
1 29  ARG   n 
1 30  GLY   n 
1 31  ALA   n 
1 32  SER   n 
1 33  ASP   n 
1 34  ARG   n 
1 35  ASP   n 
1 36  ALA   n 
1 37  ALA   n 
1 38  SER   n 
1 39  GLY   n 
1 40  PRO   n 
1 41  GLU   n 
1 42  ALA   n 
1 43  PRO   n 
1 44  MET   n 
1 45  GLN   n 
1 46  PRO   n 
1 47  GLY   n 
1 48  PHE   n 
1 49  PRO   n 
1 50  GLU   n 
1 51  ASN   n 
1 52  LEU   n 
1 53  SER   n 
1 54  LYS   n 
1 55  LEU   n 
1 56  LYS   n 
1 57  SER   n 
1 58  LEU   n 
1 59  LEU   n 
1 60  THR   n 
1 61  GLN   n 
1 62  LEU   n 
1 63  ARG   n 
1 64  ALA   n 
1 65  GLU   n 
1 66  ASP   n 
1 67  LEU   n 
1 68  ASN   n 
1 69  ILE   n 
1 70  ALA   n 
1 71  PRO   n 
1 72  ARG   n 
1 73  LYS   n 
1 74  ALA   n 
1 75  THR   n 
1 76  LEU   n 
1 77  GLN   n 
1 78  PRO   n 
1 79  LEU   n 
1 80  PRO   n 
1 81  PRO   n 
1 82  ASN   n 
1 83  LEU   n 
1 84  PRO   n 
1 85  PRO   n 
1 86  VAL   n 
1 87  THR   n 
1 88  TYR   n 
1 89  MET   n 
1 90  HIS   n 
1 91  ILE   n 
1 92  TYR   n 
1 93  GLU   n 
1 94  THR   n 
1 95  ASP   n 
1 96  GLY   n 
1 97  PHE   n 
1 98  SER   n 
1 99  LEU   n 
1 100 GLY   n 
1 101 VAL   n 
1 102 PHE   n 
1 103 LEU   n 
1 104 LEU   n 
1 105 LYS   n 
1 106 SER   n 
1 107 GLY   n 
1 108 THR   n 
1 109 SER   n 
1 110 ILE   n 
1 111 PRO   n 
1 112 LEU   n 
1 113 HIS   n 
1 114 ASP   n 
1 115 HIS   n 
1 116 PRO   n 
1 117 GLY   n 
1 118 MET   n 
1 119 HIS   n 
1 120 GLY   n 
1 121 MET   n 
1 122 LEU   n 
1 123 LYS   n 
1 124 VAL   n 
1 125 LEU   n 
1 126 TYR   n 
1 127 GLY   n 
1 128 THR   n 
1 129 VAL   n 
1 130 ARG   n 
1 131 ILE   n 
1 132 SER   n 
1 133 CYS   n 
1 134 MET   n 
1 135 ASP   n 
1 136 LYS   n 
1 137 LEU   n 
1 138 ASP   n 
1 139 ALA   n 
1 140 GLY   n 
1 141 GLY   n 
1 142 GLY   n 
1 143 GLN   n 
1 144 ARG   n 
1 145 PRO   n 
1 146 ARG   n 
1 147 ALA   n 
1 148 LEU   n 
1 149 PRO   n 
1 150 PRO   n 
1 151 GLU   n 
1 152 GLN   n 
1 153 GLN   n 
1 154 PHE   n 
1 155 GLU   n 
1 156 PRO   n 
1 157 PRO   n 
1 158 LEU   n 
1 159 GLN   n 
1 160 PRO   n 
1 161 ARG   n 
1 162 GLU   n 
1 163 ARG   n 
1 164 GLU   n 
1 165 ALA   n 
1 166 VAL   n 
1 167 ARG   n 
1 168 PRO   n 
1 169 GLY   n 
1 170 VAL   n 
1 171 LEU   n 
1 172 ARG   n 
1 173 SER   n 
1 174 ARG   n 
1 175 ALA   n 
1 176 GLU   n 
1 177 TYR   n 
1 178 THR   n 
1 179 GLU   n 
1 180 ALA   n 
1 181 SER   n 
1 182 GLY   n 
1 183 PRO   n 
1 184 CYS   n 
1 185 ILE   n 
1 186 LEU   n 
1 187 THR   n 
1 188 PRO   n 
1 189 HIS   n 
1 190 ARG   n 
1 191 ASP   n 
1 192 ASN   n 
1 193 LEU   n 
1 194 HIS   n 
1 195 GLN   n 
1 196 ILE   n 
1 197 ASP   n 
1 198 ALA   n 
1 199 VAL   n 
1 200 GLU   n 
1 201 GLY   n 
1 202 PRO   n 
1 203 ALA   n 
1 204 ALA   n 
1 205 PHE   n 
1 206 LEU   n 
1 207 ASP   n 
1 208 ILE   n 
1 209 LEU   n 
1 210 ALA   n 
1 211 PRO   n 
1 212 PRO   n 
1 213 TYR   n 
1 214 ASP   n 
1 215 PRO   n 
1 216 ASP   n 
1 217 ASP   n 
1 218 GLY   n 
1 219 ARG   n 
1 220 ASP   n 
1 221 CYS   n 
1 222 HIS   n 
1 223 TYR   n 
1 224 TYR   n 
1 225 ARG   n 
1 226 VAL   n 
1 227 LEU   n 
1 228 GLU   n 
1 229 PRO   n 
1 230 VAL   n 
1 231 ARG   n 
1 232 PRO   n 
1 233 LYS   n 
1 234 GLU   n 
1 235 ALA   n 
1 236 SER   n 
1 237 SER   n 
1 238 SER   n 
1 239 ALA   n 
1 240 SER   n 
1 241 ASP   n 
1 242 LEU   n 
1 243 PRO   n 
1 244 ARG   n 
1 245 GLU   n 
1 246 VAL   n 
1 247 TRP   n 
1 248 LEU   n 
1 249 LEU   n 
1 250 GLU   n 
1 251 THR   n 
1 252 PRO   n 
1 253 GLN   n 
1 254 ALA   n 
1 255 ASP   n 
1 256 ASP   n 
1 257 PHE   n 
1 258 TRP   n 
1 259 CYS   n 
1 260 GLU   n 
1 261 GLY   n 
1 262 GLU   n 
1 263 PRO   n 
1 264 TYR   n 
1 265 PRO   n 
1 266 GLY   n 
1 267 PRO   n 
1 268 LYS   n 
1 269 VAL   n 
1 270 PHE   n 
1 271 PRO   n 
2 1   ACE   n 
2 2   TYR   n 
2 3   ILE   n 
2 4   VAL   n 
2 5   LYS   n 
2 6   THR   n 
2 7   PHE   n 
2 8   TRP   n 
2 9   A1BDE n 
2 10  GLY   n 
2 11  SER   n 
2 12  HIS   n 
2 13  ARG   n 
2 14  GLN   n 
2 15  CYS   n 
2 16  NH2   n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   271 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ADO, C10orf22' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       16 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
A1BDE 'L-peptide linking' n N~6~-L-seryl-L-lysine ?                               'C9 H19 N3 O4'   233.265 
ACE   non-polymer         . 'ACETYL GROUP'        ?                               'C2 H4 O'        44.053  
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 
CL    non-polymer         . 'CHLORIDE ION'        ?                               'Cl -1'          35.453  
CO    non-polymer         . 'COBALT (II) ION'     ?                               'Co 2'           58.933  
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  
GOL   non-polymer         . GLYCEROL              'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS   'L-peptide linking' y HISTIDINE             ?                               'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                 ?                               'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE            ?                               'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE               ?                               'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                ?                               'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE            ?                               'C5 H11 N O2 S'  149.211 
NH2   non-polymer         . 'AMINO GROUP'         ?                               'H2 N'           16.023  
PHE   'L-peptide linking' y PHENYLALANINE         ?                               'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE               ?                               'C5 H9 N O2'     115.130 
SCN   non-polymer         . 'THIOCYANATE ION'     ?                               'C N S -1'       58.082  
SER   'L-peptide linking' y SERINE                ?                               'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE             ?                               'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN            ?                               'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE              ?                               'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_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   SER   1   0   ?   ?     ?   A . n 
A 1 2   MET   2   1   ?   ?     ?   A . n 
A 1 3   PRO   3   2   ?   ?     ?   A . n 
A 1 4   ARG   4   3   ?   ?     ?   A . n 
A 1 5   ASP   5   4   ?   ?     ?   A . n 
A 1 6   ASN   6   5   5   ASN   ASN A . n 
A 1 7   MET   7   6   6   MET   MET A . n 
A 1 8   ALA   8   7   7   ALA   ALA A . n 
A 1 9   SER   9   8   8   SER   SER A . n 
A 1 10  LEU   10  9   9   LEU   LEU A . n 
A 1 11  ILE   11  10  10  ILE   ILE A . n 
A 1 12  GLN   12  11  11  GLN   GLN A . n 
A 1 13  ARG   13  12  12  ARG   ARG A . n 
A 1 14  ILE   14  13  13  ILE   ILE A . n 
A 1 15  ALA   15  14  14  ALA   ALA A . n 
A 1 16  ARG   16  15  15  ARG   ARG A . n 
A 1 17  GLN   17  16  16  GLN   GLN A . n 
A 1 18  ALA   18  17  17  ALA   ALA A . n 
A 1 19  SER   19  18  18  SER   SER A . n 
A 1 20  LEU   20  19  19  LEU   LEU A . n 
A 1 21  THR   21  20  20  THR   THR A . n 
A 1 22  PHE   22  21  21  PHE   PHE A . n 
A 1 23  ARG   23  22  22  ARG   ARG A . n 
A 1 24  GLY   24  23  ?   ?     ?   A . n 
A 1 25  SER   25  24  ?   ?     ?   A . n 
A 1 26  GLY   26  25  ?   ?     ?   A . n 
A 1 27  GLY   27  26  ?   ?     ?   A . n 
A 1 28  GLY   28  27  ?   ?     ?   A . n 
A 1 29  ARG   29  28  ?   ?     ?   A . n 
A 1 30  GLY   30  29  ?   ?     ?   A . n 
A 1 31  ALA   31  30  ?   ?     ?   A . n 
A 1 32  SER   32  31  ?   ?     ?   A . n 
A 1 33  ASP   33  32  ?   ?     ?   A . n 
A 1 34  ARG   34  33  ?   ?     ?   A . n 
A 1 35  ASP   35  34  ?   ?     ?   A . n 
A 1 36  ALA   36  35  ?   ?     ?   A . n 
A 1 37  ALA   37  36  ?   ?     ?   A . n 
A 1 38  SER   38  37  ?   ?     ?   A . n 
A 1 39  GLY   39  38  ?   ?     ?   A . n 
A 1 40  PRO   40  39  ?   ?     ?   A . n 
A 1 41  GLU   41  40  ?   ?     ?   A . n 
A 1 42  ALA   42  41  ?   ?     ?   A . n 
A 1 43  PRO   43  42  ?   ?     ?   A . n 
A 1 44  MET   44  43  ?   ?     ?   A . n 
A 1 45  GLN   45  44  44  GLN   GLN A . n 
A 1 46  PRO   46  45  45  PRO   PRO A . n 
A 1 47  GLY   47  46  46  GLY   GLY A . n 
A 1 48  PHE   48  47  47  PHE   PHE A . n 
A 1 49  PRO   49  48  48  PRO   PRO A . n 
A 1 50  GLU   50  49  49  GLU   GLU A . n 
A 1 51  ASN   51  50  50  ASN   ASN A . n 
A 1 52  LEU   52  51  51  LEU   LEU A . n 
A 1 53  SER   53  52  52  SER   SER A . n 
A 1 54  LYS   54  53  53  LYS   LYS A . n 
A 1 55  LEU   55  54  54  LEU   LEU A . n 
A 1 56  LYS   56  55  55  LYS   LYS A . n 
A 1 57  SER   57  56  56  SER   SER A . n 
A 1 58  LEU   58  57  57  LEU   LEU A . n 
A 1 59  LEU   59  58  58  LEU   LEU A . n 
A 1 60  THR   60  59  59  THR   THR A . n 
A 1 61  GLN   61  60  60  GLN   GLN A . n 
A 1 62  LEU   62  61  61  LEU   LEU A . n 
A 1 63  ARG   63  62  62  ARG   ARG A . n 
A 1 64  ALA   64  63  63  ALA   ALA A . n 
A 1 65  GLU   65  64  64  GLU   GLU A . n 
A 1 66  ASP   66  65  65  ASP   ASP A . n 
A 1 67  LEU   67  66  66  LEU   LEU A . n 
A 1 68  ASN   68  67  67  ASN   ASN A . n 
A 1 69  ILE   69  68  68  ILE   ILE A . n 
A 1 70  ALA   70  69  69  ALA   ALA A . n 
A 1 71  PRO   71  70  70  PRO   PRO A . n 
A 1 72  ARG   72  71  71  ARG   ARG A . n 
A 1 73  LYS   73  72  72  LYS   LYS A . n 
A 1 74  ALA   74  73  73  ALA   ALA A . n 
A 1 75  THR   75  74  74  THR   THR A . n 
A 1 76  LEU   76  75  75  LEU   LEU A . n 
A 1 77  GLN   77  76  76  GLN   GLN A . n 
A 1 78  PRO   78  77  77  PRO   PRO A . n 
A 1 79  LEU   79  78  78  LEU   LEU A . n 
A 1 80  PRO   80  79  79  PRO   PRO A . n 
A 1 81  PRO   81  80  80  PRO   PRO A . n 
A 1 82  ASN   82  81  81  ASN   ASN A . n 
A 1 83  LEU   83  82  82  LEU   LEU A . n 
A 1 84  PRO   84  83  83  PRO   PRO A . n 
A 1 85  PRO   85  84  84  PRO   PRO A . n 
A 1 86  VAL   86  85  85  VAL   VAL A . n 
A 1 87  THR   87  86  86  THR   THR A . n 
A 1 88  TYR   88  87  87  TYR   TYR A . n 
A 1 89  MET   89  88  88  MET   MET A . n 
A 1 90  HIS   90  89  89  HIS   HIS A . n 
A 1 91  ILE   91  90  90  ILE   ILE A . n 
A 1 92  TYR   92  91  91  TYR   TYR A . n 
A 1 93  GLU   93  92  92  GLU   GLU A . n 
A 1 94  THR   94  93  93  THR   THR A . n 
A 1 95  ASP   95  94  94  ASP   ASP A . n 
A 1 96  GLY   96  95  95  GLY   GLY A . n 
A 1 97  PHE   97  96  96  PHE   PHE A . n 
A 1 98  SER   98  97  97  SER   SER A . n 
A 1 99  LEU   99  98  98  LEU   LEU A . n 
A 1 100 GLY   100 99  99  GLY   GLY A . n 
A 1 101 VAL   101 100 100 VAL   VAL A . n 
A 1 102 PHE   102 101 101 PHE   PHE A . n 
A 1 103 LEU   103 102 102 LEU   LEU A . n 
A 1 104 LEU   104 103 103 LEU   LEU A . n 
A 1 105 LYS   105 104 104 LYS   LYS A . n 
A 1 106 SER   106 105 105 SER   SER A . n 
A 1 107 GLY   107 106 106 GLY   GLY A . n 
A 1 108 THR   108 107 107 THR   THR A . n 
A 1 109 SER   109 108 108 SER   SER A . n 
A 1 110 ILE   110 109 109 ILE   ILE A . n 
A 1 111 PRO   111 110 110 PRO   PRO A . n 
A 1 112 LEU   112 111 111 LEU   LEU A . n 
A 1 113 HIS   113 112 112 HIS   HIS A . n 
A 1 114 ASP   114 113 113 ASP   ASP A . n 
A 1 115 HIS   115 114 114 HIS   HIS A . n 
A 1 116 PRO   116 115 115 PRO   PRO A . n 
A 1 117 GLY   117 116 116 GLY   GLY A . n 
A 1 118 MET   118 117 117 MET   MET A . n 
A 1 119 HIS   119 118 118 HIS   HIS A . n 
A 1 120 GLY   120 119 119 GLY   GLY A . n 
A 1 121 MET   121 120 120 MET   MET A . n 
A 1 122 LEU   122 121 121 LEU   LEU A . n 
A 1 123 LYS   123 122 122 LYS   LYS A . n 
A 1 124 VAL   124 123 123 VAL   VAL A . n 
A 1 125 LEU   125 124 124 LEU   LEU A . n 
A 1 126 TYR   126 125 125 TYR   TYR A . n 
A 1 127 GLY   127 126 126 GLY   GLY A . n 
A 1 128 THR   128 127 127 THR   THR A . n 
A 1 129 VAL   129 128 128 VAL   VAL A . n 
A 1 130 ARG   130 129 129 ARG   ARG A . n 
A 1 131 ILE   131 130 130 ILE   ILE A . n 
A 1 132 SER   132 131 131 SER   SER A . n 
A 1 133 CYS   133 132 132 CYS   CYS A . n 
A 1 134 MET   134 133 133 MET   MET A . n 
A 1 135 ASP   135 134 134 ASP   ASP A . n 
A 1 136 LYS   136 135 135 LYS   LYS A . n 
A 1 137 LEU   137 136 136 LEU   LEU A . n 
A 1 138 ASP   138 137 137 ASP   ASP A . n 
A 1 139 ALA   139 138 ?   ?     ?   A . n 
A 1 140 GLY   140 139 ?   ?     ?   A . n 
A 1 141 GLY   141 140 ?   ?     ?   A . n 
A 1 142 GLY   142 141 ?   ?     ?   A . n 
A 1 143 GLN   143 142 ?   ?     ?   A . n 
A 1 144 ARG   144 143 ?   ?     ?   A . n 
A 1 145 PRO   145 144 144 PRO   PRO A . n 
A 1 146 ARG   146 145 145 ARG   ARG A . n 
A 1 147 ALA   147 146 146 ALA   ALA A . n 
A 1 148 LEU   148 147 147 LEU   LEU A . n 
A 1 149 PRO   149 148 148 PRO   PRO A . n 
A 1 150 PRO   150 149 149 PRO   PRO A . n 
A 1 151 GLU   151 150 150 GLU   GLU A . n 
A 1 152 GLN   152 151 151 GLN   GLN A . n 
A 1 153 GLN   153 152 152 GLN   GLN A . n 
A 1 154 PHE   154 153 153 PHE   PHE A . n 
A 1 155 GLU   155 154 154 GLU   GLU A . n 
A 1 156 PRO   156 155 155 PRO   PRO A . n 
A 1 157 PRO   157 156 156 PRO   PRO A . n 
A 1 158 LEU   158 157 157 LEU   LEU A . n 
A 1 159 GLN   159 158 158 GLN   GLN A . n 
A 1 160 PRO   160 159 159 PRO   PRO A . n 
A 1 161 ARG   161 160 160 ARG   ARG A . n 
A 1 162 GLU   162 161 161 GLU   GLU A . n 
A 1 163 ARG   163 162 162 ARG   ARG A . n 
A 1 164 GLU   164 163 163 GLU   GLU A . n 
A 1 165 ALA   165 164 164 ALA   ALA A . n 
A 1 166 VAL   166 165 165 VAL   VAL A . n 
A 1 167 ARG   167 166 166 ARG   ARG A . n 
A 1 168 PRO   168 167 167 PRO   PRO A . n 
A 1 169 GLY   169 168 168 GLY   GLY A . n 
A 1 170 VAL   170 169 169 VAL   VAL A . n 
A 1 171 LEU   171 170 170 LEU   LEU A . n 
A 1 172 ARG   172 171 171 ARG   ARG A . n 
A 1 173 SER   173 172 172 SER   SER A . n 
A 1 174 ARG   174 173 173 ARG   ARG A . n 
A 1 175 ALA   175 174 174 ALA   ALA A . n 
A 1 176 GLU   176 175 175 GLU   GLU A . n 
A 1 177 TYR   177 176 176 TYR   TYR A . n 
A 1 178 THR   178 177 177 THR   THR A . n 
A 1 179 GLU   179 178 178 GLU   GLU A . n 
A 1 180 ALA   180 179 179 ALA   ALA A . n 
A 1 181 SER   181 180 180 SER   SER A . n 
A 1 182 GLY   182 181 181 GLY   GLY A . n 
A 1 183 PRO   183 182 182 PRO   PRO A . n 
A 1 184 CYS   184 183 183 CYS   CYS A . n 
A 1 185 ILE   185 184 184 ILE   ILE A . n 
A 1 186 LEU   186 185 185 LEU   LEU A . n 
A 1 187 THR   187 186 186 THR   THR A . n 
A 1 188 PRO   188 187 187 PRO   PRO A . n 
A 1 189 HIS   189 188 188 HIS   HIS A . n 
A 1 190 ARG   190 189 189 ARG   ARG A . n 
A 1 191 ASP   191 190 190 ASP   ASP A . n 
A 1 192 ASN   192 191 191 ASN   ASN A . n 
A 1 193 LEU   193 192 192 LEU   LEU A . n 
A 1 194 HIS   194 193 193 HIS   HIS A . n 
A 1 195 GLN   195 194 194 GLN   GLN A . n 
A 1 196 ILE   196 195 195 ILE   ILE A . n 
A 1 197 ASP   197 196 196 ASP   ASP A . n 
A 1 198 ALA   198 197 197 ALA   ALA A . n 
A 1 199 VAL   199 198 198 VAL   VAL A . n 
A 1 200 GLU   200 199 199 GLU   GLU A . n 
A 1 201 GLY   201 200 200 GLY   GLY A . n 
A 1 202 PRO   202 201 201 PRO   PRO A . n 
A 1 203 ALA   203 202 202 ALA   ALA A . n 
A 1 204 ALA   204 203 203 ALA   ALA A . n 
A 1 205 PHE   205 204 204 PHE   PHE A . n 
A 1 206 LEU   206 205 205 LEU   LEU A . n 
A 1 207 ASP   207 206 206 ASP   ASP A . n 
A 1 208 ILE   208 207 207 ILE   ILE A . n 
A 1 209 LEU   209 208 208 LEU   LEU A . n 
A 1 210 ALA   210 209 209 ALA   ALA A . n 
A 1 211 PRO   211 210 210 PRO   PRO A . n 
A 1 212 PRO   212 211 211 PRO   PRO A . n 
A 1 213 TYR   213 212 212 TYR   TYR A . n 
A 1 214 ASP   214 213 213 ASP   ASP A . n 
A 1 215 PRO   215 214 214 PRO   PRO A . n 
A 1 216 ASP   216 215 215 ASP   ASP A . n 
A 1 217 ASP   217 216 216 ASP   ASP A . n 
A 1 218 GLY   218 217 217 GLY   GLY A . n 
A 1 219 ARG   219 218 218 ARG   ARG A . n 
A 1 220 ASP   220 219 219 ASP   ASP A . n 
A 1 221 CYS   221 220 220 CYS   CYS A . n 
A 1 222 HIS   222 221 221 HIS   HIS A . n 
A 1 223 TYR   223 222 222 TYR   TYR A . n 
A 1 224 TYR   224 223 223 TYR   TYR A . n 
A 1 225 ARG   225 224 224 ARG   ARG A . n 
A 1 226 VAL   226 225 225 VAL   VAL A . n 
A 1 227 LEU   227 226 226 LEU   LEU A . n 
A 1 228 GLU   228 227 227 GLU   GLU A . n 
A 1 229 PRO   229 228 228 PRO   PRO A . n 
A 1 230 VAL   230 229 229 VAL   VAL A . n 
A 1 231 ARG   231 230 ?   ?     ?   A . n 
A 1 232 PRO   232 231 ?   ?     ?   A . n 
A 1 233 LYS   233 232 ?   ?     ?   A . n 
A 1 234 GLU   234 233 ?   ?     ?   A . n 
A 1 235 ALA   235 234 ?   ?     ?   A . n 
A 1 236 SER   236 235 ?   ?     ?   A . n 
A 1 237 SER   237 236 ?   ?     ?   A . n 
A 1 238 SER   238 237 ?   ?     ?   A . n 
A 1 239 ALA   239 238 ?   ?     ?   A . n 
A 1 240 SER   240 239 ?   ?     ?   A . n 
A 1 241 ASP   241 240 240 ASP   ASP A . n 
A 1 242 LEU   242 241 241 LEU   LEU A . n 
A 1 243 PRO   243 242 242 PRO   PRO A . n 
A 1 244 ARG   244 243 243 ARG   ARG A . n 
A 1 245 GLU   245 244 244 GLU   GLU A . n 
A 1 246 VAL   246 245 245 VAL   VAL A . n 
A 1 247 TRP   247 246 246 TRP   TRP A . n 
A 1 248 LEU   248 247 247 LEU   LEU A . n 
A 1 249 LEU   249 248 248 LEU   LEU A . n 
A 1 250 GLU   250 249 249 GLU   GLU A . n 
A 1 251 THR   251 250 250 THR   THR A . n 
A 1 252 PRO   252 251 251 PRO   PRO A . n 
A 1 253 GLN   253 252 252 GLN   GLN A . n 
A 1 254 ALA   254 253 253 ALA   ALA A . n 
A 1 255 ASP   255 254 254 ASP   ASP A . n 
A 1 256 ASP   256 255 255 ASP   ASP A . n 
A 1 257 PHE   257 256 256 PHE   PHE A . n 
A 1 258 TRP   258 257 257 TRP   TRP A . n 
A 1 259 CYS   259 258 258 CYS   CYS A . n 
A 1 260 GLU   260 259 259 GLU   GLU A . n 
A 1 261 GLY   261 260 260 GLY   GLY A . n 
A 1 262 GLU   262 261 261 GLU   GLU A . n 
A 1 263 PRO   263 262 262 PRO   PRO A . n 
A 1 264 TYR   264 263 263 TYR   TYR A . n 
A 1 265 PRO   265 264 264 PRO   PRO A . n 
A 1 266 GLY   266 265 265 GLY   GLY A . n 
A 1 267 PRO   267 266 266 PRO   PRO A . n 
A 1 268 LYS   268 267 267 LYS   LYS A . n 
A 1 269 VAL   269 268 268 VAL   VAL A . n 
A 1 270 PHE   270 269 269 PHE   PHE A . n 
A 1 271 PRO   271 270 270 PRO   PRO A . n 
B 2 1   ACE   1   0   0   ACE   ACE B . n 
B 2 2   TYR   2   1   1   TYR   TYR B . n 
B 2 3   ILE   3   2   2   ILE   ILE B . n 
B 2 4   VAL   4   3   3   VAL   VAL B . n 
B 2 5   LYS   5   4   4   LYS   LYS B . n 
B 2 6   THR   6   5   5   THR   THR B . n 
B 2 7   PHE   7   6   6   PHE   PHE B . n 
B 2 8   TRP   8   7   7   TRP   TRP B . n 
B 2 9   A1BDE 9   8   8   A1BDE LIG B . n 
B 2 10  GLY   10  9   9   GLY   GLY B . n 
B 2 11  SER   11  10  10  SER   SER B . n 
B 2 12  HIS   12  11  11  HIS   HIS B . n 
B 2 13  ARG   13  12  12  ARG   ARG B . n 
B 2 14  GLN   14  13  13  GLN   GLN B . n 
B 2 15  CYS   15  14  14  CYS   CYS B . n 
B 2 16  NH2   16  15  15  NH2   NH2 B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CO  1   301 1   CO  CO  A . 
D 4 CL  1   302 1   CL  CL  A . 
E 5 GOL 1   303 2   GOL GOL A . 
F 5 GOL 1   304 3   GOL GOL A . 
G 5 GOL 1   305 4   GOL GOL A . 
H 5 GOL 1   306 5   GOL GOL A . 
I 5 GOL 1   307 7   GOL GOL A . 
J 5 GOL 1   308 8   GOL GOL A . 
K 6 SCN 1   309 10  SCN SCN A . 
L 6 SCN 1   310 11  SCN SCN A . 
M 6 SCN 1   311 12  SCN SCN A . 
N 6 SCN 1   312 13  SCN SCN A . 
O 5 GOL 1   101 6   GOL GOL B . 
P 5 GOL 1   102 9   GOL GOL B . 
Q 7 HOH 1   401 207 HOH HOH A . 
Q 7 HOH 2   402 92  HOH HOH A . 
Q 7 HOH 3   403 117 HOH HOH A . 
Q 7 HOH 4   404 69  HOH HOH A . 
Q 7 HOH 5   405 210 HOH HOH A . 
Q 7 HOH 6   406 88  HOH HOH A . 
Q 7 HOH 7   407 186 HOH HOH A . 
Q 7 HOH 8   408 143 HOH HOH A . 
Q 7 HOH 9   409 138 HOH HOH A . 
Q 7 HOH 10  410 86  HOH HOH A . 
Q 7 HOH 11  411 68  HOH HOH A . 
Q 7 HOH 12  412 159 HOH HOH A . 
Q 7 HOH 13  413 95  HOH HOH A . 
Q 7 HOH 14  414 153 HOH HOH A . 
Q 7 HOH 15  415 125 HOH HOH A . 
Q 7 HOH 16  416 84  HOH HOH A . 
Q 7 HOH 17  417 109 HOH HOH A . 
Q 7 HOH 18  418 104 HOH HOH A . 
Q 7 HOH 19  419 9   HOH HOH A . 
Q 7 HOH 20  420 220 HOH HOH A . 
Q 7 HOH 21  421 146 HOH HOH A . 
Q 7 HOH 22  422 120 HOH HOH A . 
Q 7 HOH 23  423 28  HOH HOH A . 
Q 7 HOH 24  424 161 HOH HOH A . 
Q 7 HOH 25  425 160 HOH HOH A . 
Q 7 HOH 26  426 112 HOH HOH A . 
Q 7 HOH 27  427 199 HOH HOH A . 
Q 7 HOH 28  428 53  HOH HOH A . 
Q 7 HOH 29  429 6   HOH HOH A . 
Q 7 HOH 30  430 37  HOH HOH A . 
Q 7 HOH 31  431 27  HOH HOH A . 
Q 7 HOH 32  432 115 HOH HOH A . 
Q 7 HOH 33  433 58  HOH HOH A . 
Q 7 HOH 34  434 113 HOH HOH A . 
Q 7 HOH 35  435 20  HOH HOH A . 
Q 7 HOH 36  436 17  HOH HOH A . 
Q 7 HOH 37  437 108 HOH HOH A . 
Q 7 HOH 38  438 147 HOH HOH A . 
Q 7 HOH 39  439 215 HOH HOH A . 
Q 7 HOH 40  440 1   HOH HOH A . 
Q 7 HOH 41  441 43  HOH HOH A . 
Q 7 HOH 42  442 122 HOH HOH A . 
Q 7 HOH 43  443 18  HOH HOH A . 
Q 7 HOH 44  444 85  HOH HOH A . 
Q 7 HOH 45  445 194 HOH HOH A . 
Q 7 HOH 46  446 29  HOH HOH A . 
Q 7 HOH 47  447 52  HOH HOH A . 
Q 7 HOH 48  448 173 HOH HOH A . 
Q 7 HOH 49  449 55  HOH HOH A . 
Q 7 HOH 50  450 145 HOH HOH A . 
Q 7 HOH 51  451 35  HOH HOH A . 
Q 7 HOH 52  452 42  HOH HOH A . 
Q 7 HOH 53  453 19  HOH HOH A . 
Q 7 HOH 54  454 39  HOH HOH A . 
Q 7 HOH 55  455 124 HOH HOH A . 
Q 7 HOH 56  456 16  HOH HOH A . 
Q 7 HOH 57  457 22  HOH HOH A . 
Q 7 HOH 58  458 114 HOH HOH A . 
Q 7 HOH 59  459 110 HOH HOH A . 
Q 7 HOH 60  460 12  HOH HOH A . 
Q 7 HOH 61  461 106 HOH HOH A . 
Q 7 HOH 62  462 36  HOH HOH A . 
Q 7 HOH 63  463 116 HOH HOH A . 
Q 7 HOH 64  464 91  HOH HOH A . 
Q 7 HOH 65  465 189 HOH HOH A . 
Q 7 HOH 66  466 119 HOH HOH A . 
Q 7 HOH 67  467 44  HOH HOH A . 
Q 7 HOH 68  468 107 HOH HOH A . 
Q 7 HOH 69  469 25  HOH HOH A . 
Q 7 HOH 70  470 61  HOH HOH A . 
Q 7 HOH 71  471 49  HOH HOH A . 
Q 7 HOH 72  472 213 HOH HOH A . 
Q 7 HOH 73  473 62  HOH HOH A . 
Q 7 HOH 74  474 2   HOH HOH A . 
Q 7 HOH 75  475 196 HOH HOH A . 
Q 7 HOH 76  476 206 HOH HOH A . 
Q 7 HOH 77  477 94  HOH HOH A . 
Q 7 HOH 78  478 48  HOH HOH A . 
Q 7 HOH 79  479 74  HOH HOH A . 
Q 7 HOH 80  480 78  HOH HOH A . 
Q 7 HOH 81  481 201 HOH HOH A . 
Q 7 HOH 82  482 34  HOH HOH A . 
Q 7 HOH 83  483 26  HOH HOH A . 
Q 7 HOH 84  484 150 HOH HOH A . 
Q 7 HOH 85  485 75  HOH HOH A . 
Q 7 HOH 86  486 136 HOH HOH A . 
Q 7 HOH 87  487 80  HOH HOH A . 
Q 7 HOH 88  488 191 HOH HOH A . 
Q 7 HOH 89  489 127 HOH HOH A . 
Q 7 HOH 90  490 172 HOH HOH A . 
Q 7 HOH 91  491 5   HOH HOH A . 
Q 7 HOH 92  492 32  HOH HOH A . 
Q 7 HOH 93  493 77  HOH HOH A . 
Q 7 HOH 94  494 123 HOH HOH A . 
Q 7 HOH 95  495 214 HOH HOH A . 
Q 7 HOH 96  496 126 HOH HOH A . 
Q 7 HOH 97  497 64  HOH HOH A . 
Q 7 HOH 98  498 97  HOH HOH A . 
Q 7 HOH 99  499 162 HOH HOH A . 
Q 7 HOH 100 500 31  HOH HOH A . 
Q 7 HOH 101 501 81  HOH HOH A . 
Q 7 HOH 102 502 219 HOH HOH A . 
Q 7 HOH 103 503 111 HOH HOH A . 
Q 7 HOH 104 504 65  HOH HOH A . 
Q 7 HOH 105 505 3   HOH HOH A . 
Q 7 HOH 106 506 212 HOH HOH A . 
Q 7 HOH 107 507 128 HOH HOH A . 
Q 7 HOH 108 508 197 HOH HOH A . 
Q 7 HOH 109 509 79  HOH HOH A . 
Q 7 HOH 110 510 72  HOH HOH A . 
Q 7 HOH 111 511 134 HOH HOH A . 
Q 7 HOH 112 512 132 HOH HOH A . 
Q 7 HOH 113 513 56  HOH HOH A . 
Q 7 HOH 114 514 63  HOH HOH A . 
Q 7 HOH 115 515 15  HOH HOH A . 
Q 7 HOH 116 516 24  HOH HOH A . 
Q 7 HOH 117 517 165 HOH HOH A . 
Q 7 HOH 118 518 190 HOH HOH A . 
Q 7 HOH 119 519 59  HOH HOH A . 
Q 7 HOH 120 520 218 HOH HOH A . 
Q 7 HOH 121 521 57  HOH HOH A . 
Q 7 HOH 122 522 14  HOH HOH A . 
Q 7 HOH 123 523 51  HOH HOH A . 
Q 7 HOH 124 524 8   HOH HOH A . 
Q 7 HOH 125 525 183 HOH HOH A . 
Q 7 HOH 126 526 38  HOH HOH A . 
Q 7 HOH 127 527 182 HOH HOH A . 
Q 7 HOH 128 528 83  HOH HOH A . 
Q 7 HOH 129 529 40  HOH HOH A . 
Q 7 HOH 130 530 141 HOH HOH A . 
Q 7 HOH 131 531 137 HOH HOH A . 
Q 7 HOH 132 532 168 HOH HOH A . 
Q 7 HOH 133 533 13  HOH HOH A . 
Q 7 HOH 134 534 87  HOH HOH A . 
Q 7 HOH 135 535 45  HOH HOH A . 
Q 7 HOH 136 536 154 HOH HOH A . 
Q 7 HOH 137 537 4   HOH HOH A . 
Q 7 HOH 138 538 50  HOH HOH A . 
Q 7 HOH 139 539 11  HOH HOH A . 
Q 7 HOH 140 540 195 HOH HOH A . 
Q 7 HOH 141 541 21  HOH HOH A . 
Q 7 HOH 142 542 202 HOH HOH A . 
Q 7 HOH 143 543 73  HOH HOH A . 
Q 7 HOH 144 544 151 HOH HOH A . 
Q 7 HOH 145 545 54  HOH HOH A . 
Q 7 HOH 146 546 204 HOH HOH A . 
Q 7 HOH 147 547 96  HOH HOH A . 
Q 7 HOH 148 548 208 HOH HOH A . 
Q 7 HOH 149 549 169 HOH HOH A . 
Q 7 HOH 150 550 142 HOH HOH A . 
Q 7 HOH 151 551 131 HOH HOH A . 
Q 7 HOH 152 552 209 HOH HOH A . 
Q 7 HOH 153 553 135 HOH HOH A . 
Q 7 HOH 154 554 102 HOH HOH A . 
Q 7 HOH 155 555 103 HOH HOH A . 
Q 7 HOH 156 556 192 HOH HOH A . 
Q 7 HOH 157 557 157 HOH HOH A . 
Q 7 HOH 158 558 41  HOH HOH A . 
Q 7 HOH 159 559 171 HOH HOH A . 
Q 7 HOH 160 560 221 HOH HOH A . 
Q 7 HOH 161 561 178 HOH HOH A . 
Q 7 HOH 162 562 67  HOH HOH A . 
Q 7 HOH 163 563 71  HOH HOH A . 
Q 7 HOH 164 564 133 HOH HOH A . 
Q 7 HOH 165 565 174 HOH HOH A . 
Q 7 HOH 166 566 177 HOH HOH A . 
Q 7 HOH 167 567 140 HOH HOH A . 
Q 7 HOH 168 568 193 HOH HOH A . 
Q 7 HOH 169 569 23  HOH HOH A . 
Q 7 HOH 170 570 216 HOH HOH A . 
Q 7 HOH 171 571 93  HOH HOH A . 
Q 7 HOH 172 572 33  HOH HOH A . 
Q 7 HOH 173 573 217 HOH HOH A . 
Q 7 HOH 174 574 200 HOH HOH A . 
Q 7 HOH 175 575 152 HOH HOH A . 
Q 7 HOH 176 576 211 HOH HOH A . 
Q 7 HOH 177 577 129 HOH HOH A . 
Q 7 HOH 178 578 205 HOH HOH A . 
Q 7 HOH 179 579 180 HOH HOH A . 
Q 7 HOH 180 580 185 HOH HOH A . 
Q 7 HOH 181 581 30  HOH HOH A . 
Q 7 HOH 182 582 98  HOH HOH A . 
Q 7 HOH 183 583 188 HOH HOH A . 
Q 7 HOH 184 584 121 HOH HOH A . 
Q 7 HOH 185 585 203 HOH HOH A . 
Q 7 HOH 186 586 82  HOH HOH A . 
Q 7 HOH 187 587 139 HOH HOH A . 
Q 7 HOH 188 588 179 HOH HOH A . 
Q 7 HOH 189 589 105 HOH HOH A . 
Q 7 HOH 190 590 163 HOH HOH A . 
Q 7 HOH 191 591 46  HOH HOH A . 
Q 7 HOH 192 592 184 HOH HOH A . 
Q 7 HOH 193 593 187 HOH HOH A . 
Q 7 HOH 194 594 76  HOH HOH A . 
Q 7 HOH 195 595 149 HOH HOH A . 
Q 7 HOH 196 596 181 HOH HOH A . 
Q 7 HOH 197 597 198 HOH HOH A . 
Q 7 HOH 198 598 70  HOH HOH A . 
Q 7 HOH 199 599 7   HOH HOH A . 
Q 7 HOH 200 600 60  HOH HOH A . 
Q 7 HOH 201 601 90  HOH HOH A . 
Q 7 HOH 202 602 144 HOH HOH A . 
Q 7 HOH 203 603 118 HOH HOH A . 
Q 7 HOH 204 604 166 HOH HOH A . 
Q 7 HOH 205 605 148 HOH HOH A . 
Q 7 HOH 206 606 130 HOH HOH A . 
Q 7 HOH 207 607 164 HOH HOH A . 
Q 7 HOH 208 608 66  HOH HOH A . 
R 7 HOH 1   201 167 HOH HOH B . 
R 7 HOH 2   202 101 HOH HOH B . 
R 7 HOH 3   203 155 HOH HOH B . 
R 7 HOH 4   204 175 HOH HOH B . 
R 7 HOH 5   205 156 HOH HOH B . 
R 7 HOH 6   206 89  HOH HOH B . 
R 7 HOH 7   207 10  HOH HOH B . 
R 7 HOH 8   208 100 HOH HOH B . 
R 7 HOH 9   209 99  HOH HOH B . 
R 7 HOH 10  210 170 HOH HOH B . 
R 7 HOH 11  211 158 HOH HOH B . 
R 7 HOH 12  212 176 HOH HOH B . 
R 7 HOH 13  213 47  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASN 5   ? CG  ? A ASN 6   CG  
2  1 Y 1 A ASN 5   ? OD1 ? A ASN 6   OD1 
3  1 Y 1 A ASN 5   ? ND2 ? A ASN 6   ND2 
4  1 Y 0 A ASN 5   ? C   ? A ASN 6   C   
5  1 Y 0 A ASN 5   ? O   ? A ASN 6   O   
6  1 Y 0 A ASN 5   ? CB  ? A ASN 6   CB  
7  1 Y 0 A ARG 22  ? CD  ? A ARG 23  CD  
8  1 Y 0 A ARG 22  ? NE  ? A ARG 23  NE  
9  1 Y 0 A ARG 22  ? CZ  ? A ARG 23  CZ  
10 1 Y 0 A ARG 22  ? NH1 ? A ARG 23  NH1 
11 1 Y 0 A ARG 22  ? NH2 ? A ARG 23  NH2 
12 1 Y 0 A ARG 62  ? CZ  ? A ARG 63  CZ  
13 1 Y 1 A ASP 137 ? CG  ? A ASP 138 CG  
14 1 Y 1 A ASP 137 ? OD1 ? A ASP 138 OD1 
15 1 Y 1 A ASP 137 ? OD2 ? A ASP 138 OD2 
16 1 Y 1 A GLU 150 ? CG  ? A GLU 151 CG  
17 1 Y 1 A GLU 150 ? CD  ? A GLU 151 CD  
18 1 Y 1 A GLU 150 ? OE1 ? A GLU 151 OE1 
19 1 Y 1 A GLU 150 ? OE2 ? A GLU 151 OE2 
20 1 Y 0 A ARG 160 ? CD  ? A ARG 161 CD  
21 1 Y 0 A ARG 160 ? NE  ? A ARG 161 NE  
22 1 Y 0 A ARG 160 ? CZ  ? A ARG 161 CZ  
23 1 Y 0 A ARG 160 ? NH1 ? A ARG 161 NH1 
24 1 Y 0 A ARG 160 ? NH2 ? A ARG 161 NH2 
25 1 Y 0 A GLU 178 ? CD  ? A GLU 179 CD  
26 1 Y 0 A GLU 227 ? CD  ? A GLU 228 CD  
27 1 Y 0 A GLU 227 ? OE1 ? A GLU 228 OE1 
28 1 Y 0 A GLU 227 ? OE2 ? A GLU 228 OE2 
29 1 Y 1 A ASP 240 ? CG  ? A ASP 241 CG  
30 1 Y 1 A ASP 240 ? OD1 ? A ASP 241 OD1 
31 1 Y 1 A ASP 240 ? OD2 ? A ASP 241 OD2 
32 1 Y 0 A GLU 244 ? CD  ? A GLU 245 CD  
33 1 Y 0 A PRO 270 ? C   ? A PRO 271 C   
34 1 Y 0 A PRO 270 ? O   ? A PRO 271 O   
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 ? 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           ? 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           ? 4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           ? 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DXV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     35.939 
_cell.length_a_esd                 ? 
_cell.length_b                     71.588 
_cell.length_b_esd                 ? 
_cell.length_c                     108.526 
_cell.length_c_esd                 ? 
_cell.volume                       279215.816 
_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                         9DXV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DXV 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M sodium nitrate, 20% w/v PEG3350, 0.1 M Bis-Tris propane, pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-08-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          25.64 
_reflns.entry_id                                       9DXV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               43.24 
_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                                     37903 
_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                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_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                                    1.60 
_reflns_shell.d_res_low                                     1.62 
_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                             1616 
_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                                  0.666 
_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                               33.79 
_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                                 9DXV 
_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                            1.60 
_refine.ls_d_res_low                             43.24 
_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                     37801 
_refine.ls_number_reflns_R_free                  1896 
_refine.ls_number_reflns_R_work                  35905 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.19 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1716 
_refine.ls_R_factor_R_free                       0.1916 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1706 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 18.7148 
_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                            0.1537 
_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                       1.60 
_refine_hist.d_res_low                        43.24 
_refine_hist.number_atoms_solvent             221 
_refine_hist.number_atoms_total               2222 
_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        1939 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         62 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0075  ? 2144 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.0402  ? 2918 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0638  ? 312  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0117  ? 378  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 11.0612 ? 316  ? f_dihedral_angle_d ? ? ? 
# 
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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.60 1.64  . . 127 2287 89.11  . . . . 0.2491 . . . . . . . . . . . . . . . 0.2837 
'X-RAY DIFFRACTION' 1.64 1.68  . . 132 2510 99.89  . . . . 0.2049 . . . . . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 1.68 1.73  . . 138 2557 99.96  . . . . 0.1953 . . . . . . . . . . . . . . . 0.2042 
'X-RAY DIFFRACTION' 1.73 1.79  . . 147 2536 100.00 . . . . 0.2065 . . . . . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 1.79 1.85  . . 126 2532 100.00 . . . . 0.2013 . . . . . . . . . . . . . . . 0.2420 
'X-RAY DIFFRACTION' 1.85 1.92  . . 123 2560 100.00 . . . . 0.1749 . . . . . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 1.92 2.01  . . 136 2591 100.00 . . . . 0.1618 . . . . . . . . . . . . . . . 0.1741 
'X-RAY DIFFRACTION' 2.01 2.12  . . 149 2556 99.96  . . . . 0.1628 . . . . . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 2.12 2.25  . . 125 2584 100.00 . . . . 0.1797 . . . . . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.25 2.42  . . 123 2567 99.96  . . . . 0.1780 . . . . . . . . . . . . . . . 0.2249 
'X-RAY DIFFRACTION' 2.42 2.67  . . 153 2577 100.00 . . . . 0.1874 . . . . . . . . . . . . . . . 0.2344 
'X-RAY DIFFRACTION' 2.67 3.05  . . 135 2610 100.00 . . . . 0.1803 . . . . . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 3.05 3.85  . . 127 2656 99.93  . . . . 0.1579 . . . . . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 3.85 43.24 . . 155 2782 99.80  . . . . 0.1567 . . . . . . . . . . . . . . . 0.1667 
# 
_struct.entry_id                     9DXV 
_struct.title                        
;Crystal structure of cobalt-incorporated human 2-aminoethanethiol (aka cysteamine) dioxygenase (ADO) variant C18S/C239S in complex with CP6-L8K-Ser
;
_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        9DXV 
_struct_keywords.text            'oxygen-sensor, thiol dioxygenase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N N N 6 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 7 ? 
R N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP AEDO_HUMAN Q96SZ5 ? 1 
;MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQLRAEDLNIAPRKATLQPLPP
NLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGMLKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPR
EREAVRPGVLRSRAEYTEASGPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
;
1 
2 PDB 9DXV       9DXV   ? 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 9DXV A 2 ? 271 ? Q96SZ5 1 ? 270 ? 1 270 
2 2 9DXV B 1 ? 16  ? 9DXV   0 ? 15  ? 0 15  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DXV SER A 1   ? UNP Q96SZ5 ?   ?   'expression tag' 0   1 
1 9DXV SER A 19  ? UNP Q96SZ5 CYS 18  conflict         18  2 
1 9DXV SER A 240 ? UNP Q96SZ5 CYS 239 conflict         239 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 4540  ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  12870 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 9   ? PHE A 22  ? SER A 8   PHE A 21  1 ? 14 
HELX_P HELX_P2 AA2 GLY A 47  ? LEU A 62  ? GLY A 46  LEU A 61  1 ? 16 
HELX_P HELX_P3 AA3 ARG A 63  ? ASN A 68  ? ARG A 62  ASN A 67  5 ? 6  
HELX_P HELX_P4 AA4 GLN A 159 ? VAL A 166 ? GLN A 158 VAL A 165 1 ? 8  
HELX_P HELX_P5 AA5 ASP A 214 ? GLY A 218 ? ASP A 213 GLY A 217 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 
covale1 covale both ? B ACE   1   C   ? ? ? 1_555 B TYR   2  N   ? ? B ACE   0   B TYR   1   1_555 ? ? ? ? ? ? ? 1.323 ? ? 
covale2 covale none ? B ACE   1   CH3 ? ? ? 1_555 B CYS   15 SG  ? ? B ACE   0   B CYS   14  1_555 ? ? ? ? ? ? ? 1.768 ? ? 
covale3 covale one  ? B TRP   8   C   ? ? ? 1_555 B A1BDE 9  N   ? ? B TRP   7   B A1BDE 8   1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale4 covale both ? B A1BDE 9   C   ? ? ? 1_555 B GLY   10 N   ? ? B A1BDE 8   B GLY   9   1_555 ? ? ? ? ? ? ? 1.427 ? ? 
covale5 covale both ? B CYS   15  C   ? ? ? 1_555 B NH2   16 N   ? ? B CYS   14  B NH2   15  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
metalc1 metalc ?    ? A HIS   113 NE2 ? ? ? 1_555 C CO    .  CO  ? ? A HIS   112 A CO    301 1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc2 metalc ?    ? A HIS   115 NE2 ? ? ? 1_555 C CO    .  CO  ? ? A HIS   114 A CO    301 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc3 metalc ?    ? A HIS   194 NE2 ? ? ? 1_555 C CO    .  CO  ? ? A HIS   193 A CO    301 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc4 metalc ?    ? C CO    .   CO  ? ? ? 1_555 Q HOH   .  O   ? ? A CO    301 A HOH   440 1_555 ? ? ? ? ? ? ? 2.215 ? ? 
metalc5 metalc ?    ? C CO    .   CO  ? ? ? 1_555 B A1BDE 9  N14 ? ? A CO    301 B A1BDE 8   1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc6 metalc ?    ? C CO    .   CO  ? ? ? 1_555 B A1BDE 9  O15 ? ? A CO    301 B A1BDE 8   1_555 ? ? ? ? ? ? ? 2.095 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 NE2 ? A HIS   115 ? A HIS   114 ? 1_555 93.2  ? 
2  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 NE2 ? A HIS   194 ? A HIS   193 ? 1_555 92.7  ? 
3  NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 NE2 ? A HIS   194 ? A HIS   193 ? 1_555 92.7  ? 
4  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O   ? Q HOH   .   ? A HOH   440 ? 1_555 176.6 ? 
5  NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O   ? Q HOH   .   ? A HOH   440 ? 1_555 88.2  ? 
6  NE2 ? A HIS   194 ? A HIS   193 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O   ? Q HOH   .   ? A HOH   440 ? 1_555 90.3  ? 
7  NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N14 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 100.9 ? 
8  NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N14 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 159.1 ? 
9  NE2 ? A HIS   194 ? A HIS   193 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N14 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 101.8 ? 
10 O   ? Q HOH   .   ? A HOH   440 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 N14 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 77.0  ? 
11 NE2 ? A HIS   113 ? A HIS   112 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O15 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 89.8  ? 
12 NE2 ? A HIS   115 ? A HIS   114 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O15 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 85.8  ? 
13 NE2 ? A HIS   194 ? A HIS   193 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O15 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 177.2 ? 
14 O   ? Q HOH   .   ? A HOH   440 ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O15 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 87.2  ? 
15 N14 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 CO ? C CO . ? A CO 301 ? 1_555 O15 ? B A1BDE 9   ? B A1BDE 8   ? 1_555 79.0  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1BDE B 9  ? .   . .  . A1BDE B 8  ? 1_555 .   . .  . .     .   .  LYS 1  A1BDE None 'Non-standard residue' 
2 ACE   B 1  ? TYR B 2  ? ACE   B 0  ? 1_555 TYR B 1  ? 1_555 .   .  TYR 5  ACE   None 'Terminal acetylation' 
3 NH2   B 16 ? CYS B 15 ? NH2   B 15 ? 1_555 CYS B 14 ? 1_555 .   .  CYS 11 NH2   None 'Terminal amidation'   
4 ACE   B 1  ? CYS B 15 ? ACE   B 0  ? 1_555 CYS B 14 ? 1_555 CH3 SG .   .  .     None 'Non-standard linkage' 
# 
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 GLU 155 A . ? GLU 154 A PRO 156 A ? PRO 155 A 1 -3.49 
2 ALA 210 A . ? ALA 209 A PRO 211 A ? PRO 210 A 1 -6.68 
3 LEU 242 A . ? LEU 241 A PRO 243 A ? PRO 242 A 1 -1.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 6  ? 
AA3 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? anti-parallel 
AA2 5 6  ? parallel      
AA3 1 2  ? 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  CYS A 184 ? LEU A 186 ? CYS A 183 LEU A 185 
AA1 2  HIS A 119 ? LYS A 136 ? HIS A 118 LYS A 135 
AA1 3  ARG A 167 ? TYR A 177 ? ARG A 166 TYR A 176 
AA1 4  ARG A 244 ? THR A 251 ? ARG A 243 THR A 250 
AA1 5  TYR A 223 ? LEU A 227 ? TYR A 222 LEU A 226 
AA1 6  SER A 109 ? HIS A 113 ? SER A 108 HIS A 112 
AA1 7  LEU A 193 ? ALA A 210 ? LEU A 192 ALA A 209 
AA1 8  SER A 98  ? LEU A 104 ? SER A 97  LEU A 103 
AA1 9  VAL A 86  ? GLU A 93  ? VAL A 85  GLU A 92  
AA1 10 CYS A 259 ? GLY A 261 ? CYS A 258 GLY A 260 
AA2 1  CYS A 184 ? LEU A 186 ? CYS A 183 LEU A 185 
AA2 2  HIS A 119 ? LYS A 136 ? HIS A 118 LYS A 135 
AA2 3  LEU A 193 ? ALA A 210 ? LEU A 192 ALA A 209 
AA2 4  SER A 98  ? LEU A 104 ? SER A 97  LEU A 103 
AA2 5  VAL A 86  ? GLU A 93  ? VAL A 85  GLU A 92  
AA2 6  CYS A 259 ? GLY A 261 ? CYS A 258 GLY A 260 
AA3 1  ILE B 3   ? THR B 6   ? ILE B 2   THR B 5   
AA3 2  GLY B 10  ? ARG B 13  ? GLY B 9   ARG B 12  
# 
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  O CYS A 184 ? O CYS A 183 N LEU A 122 ? N LEU A 121 
AA1 2 3  N VAL A 129 ? N VAL A 128 O TYR A 177 ? O TYR A 176 
AA1 3 4  N ARG A 167 ? N ARG A 166 O LEU A 248 ? O LEU A 247 
AA1 4 5  O LEU A 249 ? O LEU A 248 N ARG A 225 ? N ARG A 224 
AA1 5 6  O TYR A 224 ? O TYR A 223 N LEU A 112 ? N LEU A 111 
AA1 6 7  N ILE A 110 ? N ILE A 109 O ILE A 196 ? O ILE A 195 
AA1 7 8  O ALA A 203 ? O ALA A 202 N LEU A 104 ? N LEU A 103 
AA1 8 9  O LEU A 103 ? O LEU A 102 N THR A 87  ? N THR A 86  
AA1 9 10 N TYR A 88  ? N TYR A 87  O GLU A 260 ? O GLU A 259 
AA2 1 2  O CYS A 184 ? O CYS A 183 N LEU A 122 ? N LEU A 121 
AA2 2 3  N HIS A 119 ? N HIS A 118 O ALA A 210 ? O ALA A 209 
AA2 3 4  O ALA A 203 ? O ALA A 202 N LEU A 104 ? N LEU A 103 
AA2 4 5  O LEU A 103 ? O LEU A 102 N THR A 87  ? N THR A 86  
AA2 5 6  N TYR A 88  ? N TYR A 87  O GLU A 260 ? O GLU A 259 
AA3 1 2  N VAL B 4   ? N VAL B 3   O HIS B 12  ? O HIS B 11  
# 
_pdbx_entry_details.entry_id                   9DXV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 488 ? ? O A HOH 590 ? ? 2.00 
2 1 O A HOH 420 ? ? O A HOH 517 ? ? 2.04 
3 1 O A LEU 226 ? ? O A HOH 401 ? ? 2.12 
4 1 O A HOH 407 ? ? O A HOH 593 ? ? 2.13 
5 1 O A HOH 585 ? ? O A HOH 603 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     536 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     560 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              2.09 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A PRO 156 ? ? N  A PRO 156 ? ? CD A PRO 156 ? ? 101.04 111.70 -10.66 1.40 N 
2 1 N  A PRO 156 ? ? CD A PRO 156 ? ? CG A PRO 156 ? ? 92.86  103.20 -10.34 1.50 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    A1BDE 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     8 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -146.65 
_pdbx_validate_torsion.psi             25.81 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -1.97919254634 -9.83199112383 29.5543383533  0.260661998813 ? -0.0625740643764  ? -0.0123706233741 
? 0.330867333416 ? -0.049506595672   ? 0.32428349521  ? 0.386175986136  ? 0.0774301404593  ? 0.182077947006   ? 0.280566033377  ? 
0.0432659375091   ? 0.211462052048 ? 0.0784494274401 ? -0.497506398356 ? 0.234806554476   ? 0.129396568199   ? -0.0184184602206  ? 
-0.261533971818   ? -0.257400660231  ? 0.501348362293   ? 0.00202303049023   ? 
2 'X-RAY DIFFRACTION' ? refined -16.2723034852 -19.8686681504 20.7869530456  0.182441185384 ? -0.00686996150225 ? 0.00615571641796 
? 0.160543762698 ? -0.00251787449751 ? 0.199745913388 ? 1.45784244591   ? -0.238346688218  ? -0.046586495342  ? 0.858835435108  ? 
0.0446837091267   ? 1.35151054599  ? 0.0214097124196 ? 0.0222880589175 ? -0.0906397035696 ? 0.0162555710841  ? -0.00024642968793 ? 
0.00710596827315  ? -0.0834424035693 ? -0.0333885541044 ? -3.69391522152e-05 ? 
3 'X-RAY DIFFRACTION' ? refined -14.1840365762 -19.2716721579 -10.7940413598 0.360319792454 ? -0.0192812004766  ? -0.0186557715743 
? 0.401874859467 ? 0.00595615326644  ? 0.215873558489 ? 0.184470074291  ? -0.217226412632  ? 0.0569381097332  ? 0.221242799682  ? 
-0.00514546564326 ? 0.318752516472 ? 0.100298409679  ? -0.192682586982 ? -0.0426037989914 ? -0.171177803518  ? 0.0201921583881   ? 
0.025669029334    ? 0.092019053694   ? 0.325408301542   ? 1.21233315913e-05  ? 
4 'X-RAY DIFFRACTION' ? refined -12.8913121306 -17.6647317206 12.5499309473  0.198098987857 ? 0.00811336125243  ? 0.0130571305399 
? 0.193490235914 ? -0.00983958046735 ? 0.208774534259 ? 1.21180247599   ? 0.091390819172   ? -0.0913966201398 ? 0.565388323917  ? 
0.0416488913837   ? 2.21961404643  ? 0.0146534408274 ? 0.217963293432  ? -0.0387033497893 ? -0.0684654115149 ? 0.00267157407386  ? 
-0.00692399751086 ? -0.118094126624  ? -0.0229040950348 ? 1.46962178283e-05  ? 
5 'X-RAY DIFFRACTION' ? refined -23.7863394269 -10.2020810107 14.8494247999  0.361341739515 ? 0.0421198914673   ? 
-0.00349627816751 ? 0.348968573998 ? -0.00777693311432 ? 0.382031645835 ? 0.0958587486615 ? -0.0111238981738 ? -0.0588163262946 ? 
0.0534583533236 ? 0.00904343458618  ? 0.026425003018 ? -0.071305195    ? 0.0581372476092 ? 0.0928946331163  ? -0.100227373997  ? 
0.0549864748296   ? 0.313224915034    ? -0.200802858919  ? -0.21462445912   ? -0.00021084222781  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 5   ? A 35  A 60  ? ? 
;chain 'A' and (resid 5 through 60 )
;
2 'X-RAY DIFFRACTION' 2 A 36  A 61  ? A 110 A 135 ? ? 
;chain 'A' and (resid 61 through 135 )
;
3 'X-RAY DIFFRACTION' 3 A 111 A 136 ? A 134 A 165 ? ? 
;chain 'A' and (resid 136 through 165 )
;
4 'X-RAY DIFFRACTION' 4 A 135 A 166 ? A 229 A 270 ? ? 
;chain 'A' and (resid 166 through 270 )
;
5 'X-RAY DIFFRACTION' 5 C 3   B 2   ? F ?   B 15  ? ? 
;chain 'B' and (resid 2 through 15 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 608 ? 5.87 .    
2 1 O ? B HOH 213 ? .    7.49 
# 
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 SER 0   ? A SER 1   
2  1 Y 1 A MET 1   ? A MET 2   
3  1 Y 1 A PRO 2   ? A PRO 3   
4  1 Y 1 A ARG 3   ? A ARG 4   
5  1 Y 1 A ASP 4   ? A ASP 5   
6  1 Y 1 A GLY 23  ? A GLY 24  
7  1 Y 1 A SER 24  ? A SER 25  
8  1 Y 1 A GLY 25  ? A GLY 26  
9  1 Y 1 A GLY 26  ? A GLY 27  
10 1 Y 1 A GLY 27  ? A GLY 28  
11 1 Y 1 A ARG 28  ? A ARG 29  
12 1 Y 1 A GLY 29  ? A GLY 30  
13 1 Y 1 A ALA 30  ? A ALA 31  
14 1 Y 1 A SER 31  ? A SER 32  
15 1 Y 1 A ASP 32  ? A ASP 33  
16 1 Y 1 A ARG 33  ? A ARG 34  
17 1 Y 1 A ASP 34  ? A ASP 35  
18 1 Y 1 A ALA 35  ? A ALA 36  
19 1 Y 1 A ALA 36  ? A ALA 37  
20 1 Y 1 A SER 37  ? A SER 38  
21 1 Y 1 A GLY 38  ? A GLY 39  
22 1 Y 1 A PRO 39  ? A PRO 40  
23 1 Y 1 A GLU 40  ? A GLU 41  
24 1 Y 1 A ALA 41  ? A ALA 42  
25 1 Y 1 A PRO 42  ? A PRO 43  
26 1 Y 1 A MET 43  ? A MET 44  
27 1 Y 1 A ALA 138 ? A ALA 139 
28 1 Y 1 A GLY 139 ? A GLY 140 
29 1 Y 1 A GLY 140 ? A GLY 141 
30 1 Y 1 A GLY 141 ? A GLY 142 
31 1 Y 1 A GLN 142 ? A GLN 143 
32 1 Y 1 A ARG 143 ? A ARG 144 
33 1 Y 1 A ARG 230 ? A ARG 231 
34 1 Y 1 A PRO 231 ? A PRO 232 
35 1 Y 1 A LYS 232 ? A LYS 233 
36 1 Y 1 A GLU 233 ? A GLU 234 
37 1 Y 1 A ALA 234 ? A ALA 235 
38 1 Y 1 A SER 235 ? A SER 236 
39 1 Y 1 A SER 236 ? A SER 237 
40 1 Y 1 A SER 237 ? A SER 238 
41 1 Y 1 A ALA 238 ? A ALA 239 
42 1 Y 1 A SER 239 ? A SER 240 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BDE C10  C  N N 1   
A1BDE C13  C  N N 2   
A1BDE CG   C  N N 3   
A1BDE CE   C  N N 4   
A1BDE CD   C  N N 5   
A1BDE CB   C  N N 6   
A1BDE CA   C  N S 7   
A1BDE C    C  N N 8   
A1BDE C12  C  N S 9   
A1BDE N    N  N N 10  
A1BDE NZ   N  N N 11  
A1BDE N14  N  N N 12  
A1BDE O    O  N N 13  
A1BDE O11  O  N N 14  
A1BDE O15  O  N N 15  
A1BDE H1   H  N N 16  
A1BDE H3   H  N N 17  
A1BDE HG2  H  N N 18  
A1BDE HG3  H  N N 19  
A1BDE HE2  H  N N 20  
A1BDE HE3  H  N N 21  
A1BDE HD2  H  N N 22  
A1BDE HD3  H  N N 23  
A1BDE HB2  H  N N 24  
A1BDE HB3  H  N N 25  
A1BDE HA   H  N N 26  
A1BDE H13  H  N N 27  
A1BDE H    H  N N 28  
A1BDE H2   H  N N 29  
A1BDE HZ1  H  N N 30  
A1BDE H18  H  N N 31  
A1BDE H19  H  N N 32  
A1BDE H21  H  N N 33  
A1BDE OXT  O  N N 34  
A1BDE H4   H  N N 35  
ACE   C    C  N N 36  
ACE   O    O  N N 37  
ACE   CH3  C  N N 38  
ACE   H    H  N N 39  
ACE   H1   H  N N 40  
ACE   H2   H  N N 41  
ACE   H3   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CL    CL   CL N N 116 
CO    CO   CO N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
GOL   C1   C  N N 181 
GOL   O1   O  N N 182 
GOL   C2   C  N N 183 
GOL   O2   O  N N 184 
GOL   C3   C  N N 185 
GOL   O3   O  N N 186 
GOL   H11  H  N N 187 
GOL   H12  H  N N 188 
GOL   HO1  H  N N 189 
GOL   H2   H  N N 190 
GOL   HO2  H  N N 191 
GOL   H31  H  N N 192 
GOL   H32  H  N N 193 
GOL   HO3  H  N N 194 
HIS   N    N  N N 195 
HIS   CA   C  N S 196 
HIS   C    C  N N 197 
HIS   O    O  N N 198 
HIS   CB   C  N N 199 
HIS   CG   C  Y N 200 
HIS   ND1  N  Y N 201 
HIS   CD2  C  Y N 202 
HIS   CE1  C  Y N 203 
HIS   NE2  N  Y N 204 
HIS   OXT  O  N N 205 
HIS   H    H  N N 206 
HIS   H2   H  N N 207 
HIS   HA   H  N N 208 
HIS   HB2  H  N N 209 
HIS   HB3  H  N N 210 
HIS   HD1  H  N N 211 
HIS   HD2  H  N N 212 
HIS   HE1  H  N N 213 
HIS   HE2  H  N N 214 
HIS   HXT  H  N N 215 
HOH   O    O  N N 216 
HOH   H1   H  N N 217 
HOH   H2   H  N N 218 
ILE   N    N  N N 219 
ILE   CA   C  N S 220 
ILE   C    C  N N 221 
ILE   O    O  N N 222 
ILE   CB   C  N S 223 
ILE   CG1  C  N N 224 
ILE   CG2  C  N N 225 
ILE   CD1  C  N N 226 
ILE   OXT  O  N N 227 
ILE   H    H  N N 228 
ILE   H2   H  N N 229 
ILE   HA   H  N N 230 
ILE   HB   H  N N 231 
ILE   HG12 H  N N 232 
ILE   HG13 H  N N 233 
ILE   HG21 H  N N 234 
ILE   HG22 H  N N 235 
ILE   HG23 H  N N 236 
ILE   HD11 H  N N 237 
ILE   HD12 H  N N 238 
ILE   HD13 H  N N 239 
ILE   HXT  H  N N 240 
LEU   N    N  N N 241 
LEU   CA   C  N S 242 
LEU   C    C  N N 243 
LEU   O    O  N N 244 
LEU   CB   C  N N 245 
LEU   CG   C  N N 246 
LEU   CD1  C  N N 247 
LEU   CD2  C  N N 248 
LEU   OXT  O  N N 249 
LEU   H    H  N N 250 
LEU   H2   H  N N 251 
LEU   HA   H  N N 252 
LEU   HB2  H  N N 253 
LEU   HB3  H  N N 254 
LEU   HG   H  N N 255 
LEU   HD11 H  N N 256 
LEU   HD12 H  N N 257 
LEU   HD13 H  N N 258 
LEU   HD21 H  N N 259 
LEU   HD22 H  N N 260 
LEU   HD23 H  N N 261 
LEU   HXT  H  N N 262 
LYS   N    N  N N 263 
LYS   CA   C  N S 264 
LYS   C    C  N N 265 
LYS   O    O  N N 266 
LYS   CB   C  N N 267 
LYS   CG   C  N N 268 
LYS   CD   C  N N 269 
LYS   CE   C  N N 270 
LYS   NZ   N  N N 271 
LYS   OXT  O  N N 272 
LYS   H    H  N N 273 
LYS   H2   H  N N 274 
LYS   HA   H  N N 275 
LYS   HB2  H  N N 276 
LYS   HB3  H  N N 277 
LYS   HG2  H  N N 278 
LYS   HG3  H  N N 279 
LYS   HD2  H  N N 280 
LYS   HD3  H  N N 281 
LYS   HE2  H  N N 282 
LYS   HE3  H  N N 283 
LYS   HZ1  H  N N 284 
LYS   HZ2  H  N N 285 
LYS   HZ3  H  N N 286 
LYS   HXT  H  N N 287 
MET   N    N  N N 288 
MET   CA   C  N S 289 
MET   C    C  N N 290 
MET   O    O  N N 291 
MET   CB   C  N N 292 
MET   CG   C  N N 293 
MET   SD   S  N N 294 
MET   CE   C  N N 295 
MET   OXT  O  N N 296 
MET   H    H  N N 297 
MET   H2   H  N N 298 
MET   HA   H  N N 299 
MET   HB2  H  N N 300 
MET   HB3  H  N N 301 
MET   HG2  H  N N 302 
MET   HG3  H  N N 303 
MET   HE1  H  N N 304 
MET   HE2  H  N N 305 
MET   HE3  H  N N 306 
MET   HXT  H  N N 307 
NH2   N    N  N N 308 
NH2   HN1  H  N N 309 
NH2   HN2  H  N N 310 
PHE   N    N  N N 311 
PHE   CA   C  N S 312 
PHE   C    C  N N 313 
PHE   O    O  N N 314 
PHE   CB   C  N N 315 
PHE   CG   C  Y N 316 
PHE   CD1  C  Y N 317 
PHE   CD2  C  Y N 318 
PHE   CE1  C  Y N 319 
PHE   CE2  C  Y N 320 
PHE   CZ   C  Y N 321 
PHE   OXT  O  N N 322 
PHE   H    H  N N 323 
PHE   H2   H  N N 324 
PHE   HA   H  N N 325 
PHE   HB2  H  N N 326 
PHE   HB3  H  N N 327 
PHE   HD1  H  N N 328 
PHE   HD2  H  N N 329 
PHE   HE1  H  N N 330 
PHE   HE2  H  N N 331 
PHE   HZ   H  N N 332 
PHE   HXT  H  N N 333 
PRO   N    N  N N 334 
PRO   CA   C  N S 335 
PRO   C    C  N N 336 
PRO   O    O  N N 337 
PRO   CB   C  N N 338 
PRO   CG   C  N N 339 
PRO   CD   C  N N 340 
PRO   OXT  O  N N 341 
PRO   H    H  N N 342 
PRO   HA   H  N N 343 
PRO   HB2  H  N N 344 
PRO   HB3  H  N N 345 
PRO   HG2  H  N N 346 
PRO   HG3  H  N N 347 
PRO   HD2  H  N N 348 
PRO   HD3  H  N N 349 
PRO   HXT  H  N N 350 
SCN   S    S  N N 351 
SCN   C    C  N N 352 
SCN   N    N  N N 353 
SER   N    N  N N 354 
SER   CA   C  N S 355 
SER   C    C  N N 356 
SER   O    O  N N 357 
SER   CB   C  N N 358 
SER   OG   O  N N 359 
SER   OXT  O  N N 360 
SER   H    H  N N 361 
SER   H2   H  N N 362 
SER   HA   H  N N 363 
SER   HB2  H  N N 364 
SER   HB3  H  N N 365 
SER   HG   H  N N 366 
SER   HXT  H  N N 367 
THR   N    N  N N 368 
THR   CA   C  N S 369 
THR   C    C  N N 370 
THR   O    O  N N 371 
THR   CB   C  N R 372 
THR   OG1  O  N N 373 
THR   CG2  C  N N 374 
THR   OXT  O  N N 375 
THR   H    H  N N 376 
THR   H2   H  N N 377 
THR   HA   H  N N 378 
THR   HB   H  N N 379 
THR   HG1  H  N N 380 
THR   HG21 H  N N 381 
THR   HG22 H  N N 382 
THR   HG23 H  N N 383 
THR   HXT  H  N N 384 
TRP   N    N  N N 385 
TRP   CA   C  N S 386 
TRP   C    C  N N 387 
TRP   O    O  N N 388 
TRP   CB   C  N N 389 
TRP   CG   C  Y N 390 
TRP   CD1  C  Y N 391 
TRP   CD2  C  Y N 392 
TRP   NE1  N  Y N 393 
TRP   CE2  C  Y N 394 
TRP   CE3  C  Y N 395 
TRP   CZ2  C  Y N 396 
TRP   CZ3  C  Y N 397 
TRP   CH2  C  Y N 398 
TRP   OXT  O  N N 399 
TRP   H    H  N N 400 
TRP   H2   H  N N 401 
TRP   HA   H  N N 402 
TRP   HB2  H  N N 403 
TRP   HB3  H  N N 404 
TRP   HD1  H  N N 405 
TRP   HE1  H  N N 406 
TRP   HE3  H  N N 407 
TRP   HZ2  H  N N 408 
TRP   HZ3  H  N N 409 
TRP   HH2  H  N N 410 
TRP   HXT  H  N N 411 
TYR   N    N  N N 412 
TYR   CA   C  N S 413 
TYR   C    C  N N 414 
TYR   O    O  N N 415 
TYR   CB   C  N N 416 
TYR   CG   C  Y N 417 
TYR   CD1  C  Y N 418 
TYR   CD2  C  Y N 419 
TYR   CE1  C  Y N 420 
TYR   CE2  C  Y N 421 
TYR   CZ   C  Y N 422 
TYR   OH   O  N N 423 
TYR   OXT  O  N N 424 
TYR   H    H  N N 425 
TYR   H2   H  N N 426 
TYR   HA   H  N N 427 
TYR   HB2  H  N N 428 
TYR   HB3  H  N N 429 
TYR   HD1  H  N N 430 
TYR   HD2  H  N N 431 
TYR   HE1  H  N N 432 
TYR   HE2  H  N N 433 
TYR   HH   H  N N 434 
TYR   HXT  H  N N 435 
VAL   N    N  N N 436 
VAL   CA   C  N S 437 
VAL   C    C  N N 438 
VAL   O    O  N N 439 
VAL   CB   C  N N 440 
VAL   CG1  C  N N 441 
VAL   CG2  C  N N 442 
VAL   OXT  O  N N 443 
VAL   H    H  N N 444 
VAL   H2   H  N N 445 
VAL   HA   H  N N 446 
VAL   HB   H  N N 447 
VAL   HG11 H  N N 448 
VAL   HG12 H  N N 449 
VAL   HG13 H  N N 450 
VAL   HG21 H  N N 451 
VAL   HG22 H  N N 452 
VAL   HG23 H  N N 453 
VAL   HXT  H  N N 454 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BDE O   C    doub N N 1   
A1BDE C   CA   sing N N 2   
A1BDE CD  CE   sing N N 3   
A1BDE CD  CG   sing N N 4   
A1BDE CE  NZ   sing N N 5   
A1BDE O15 C13  sing N N 6   
A1BDE CA  CB   sing N N 7   
A1BDE CA  N    sing N N 8   
A1BDE CB  CG   sing N N 9   
A1BDE O11 C10  doub N N 10  
A1BDE NZ  C10  sing N N 11  
A1BDE C10 C12  sing N N 12  
A1BDE N14 C12  sing N N 13  
A1BDE C13 C12  sing N N 14  
A1BDE C13 H1   sing N N 15  
A1BDE C13 H3   sing N N 16  
A1BDE CG  HG2  sing N N 17  
A1BDE CG  HG3  sing N N 18  
A1BDE CE  HE2  sing N N 19  
A1BDE CE  HE3  sing N N 20  
A1BDE CD  HD2  sing N N 21  
A1BDE CD  HD3  sing N N 22  
A1BDE CB  HB2  sing N N 23  
A1BDE CB  HB3  sing N N 24  
A1BDE CA  HA   sing N N 25  
A1BDE C12 H13  sing N N 26  
A1BDE N   H    sing N N 27  
A1BDE N   H2   sing N N 28  
A1BDE NZ  HZ1  sing N N 29  
A1BDE N14 H18  sing N N 30  
A1BDE N14 H19  sing N N 31  
A1BDE O15 H21  sing N N 32  
A1BDE C   OXT  sing N N 33  
A1BDE OXT H4   sing N N 34  
ACE   C   O    doub N N 35  
ACE   C   CH3  sing N N 36  
ACE   C   H    sing N N 37  
ACE   CH3 H1   sing N N 38  
ACE   CH3 H2   sing N N 39  
ACE   CH3 H3   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
GOL   C1  O1   sing N N 169 
GOL   C1  C2   sing N N 170 
GOL   C1  H11  sing N N 171 
GOL   C1  H12  sing N N 172 
GOL   O1  HO1  sing N N 173 
GOL   C2  O2   sing N N 174 
GOL   C2  C3   sing N N 175 
GOL   C2  H2   sing N N 176 
GOL   O2  HO2  sing N N 177 
GOL   C3  O3   sing N N 178 
GOL   C3  H31  sing N N 179 
GOL   C3  H32  sing N N 180 
GOL   O3  HO3  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
NH2   N   HN1  sing N N 290 
NH2   N   HN2  sing N N 291 
PHE   N   CA   sing N N 292 
PHE   N   H    sing N N 293 
PHE   N   H2   sing N N 294 
PHE   CA  C    sing N N 295 
PHE   CA  CB   sing N N 296 
PHE   CA  HA   sing N N 297 
PHE   C   O    doub N N 298 
PHE   C   OXT  sing N N 299 
PHE   CB  CG   sing N N 300 
PHE   CB  HB2  sing N N 301 
PHE   CB  HB3  sing N N 302 
PHE   CG  CD1  doub Y N 303 
PHE   CG  CD2  sing Y N 304 
PHE   CD1 CE1  sing Y N 305 
PHE   CD1 HD1  sing N N 306 
PHE   CD2 CE2  doub Y N 307 
PHE   CD2 HD2  sing N N 308 
PHE   CE1 CZ   doub Y N 309 
PHE   CE1 HE1  sing N N 310 
PHE   CE2 CZ   sing Y N 311 
PHE   CE2 HE2  sing N N 312 
PHE   CZ  HZ   sing N N 313 
PHE   OXT HXT  sing N N 314 
PRO   N   CA   sing N N 315 
PRO   N   CD   sing N N 316 
PRO   N   H    sing N N 317 
PRO   CA  C    sing N N 318 
PRO   CA  CB   sing N N 319 
PRO   CA  HA   sing N N 320 
PRO   C   O    doub N N 321 
PRO   C   OXT  sing N N 322 
PRO   CB  CG   sing N N 323 
PRO   CB  HB2  sing N N 324 
PRO   CB  HB3  sing N N 325 
PRO   CG  CD   sing N N 326 
PRO   CG  HG2  sing N N 327 
PRO   CG  HG3  sing N N 328 
PRO   CD  HD2  sing N N 329 
PRO   CD  HD3  sing N N 330 
PRO   OXT HXT  sing N N 331 
SCN   S   C    sing N N 332 
SCN   C   N    trip N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_pdbx_audit_support.funding_organization   'National Health and Medical Research Council (NHMRC, Australia)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           2008546 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7REI 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DXV 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.027825 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013969 
_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]   0.009214 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CO ? ? 21.85313 5.04979 ? ? 2.45200  36.11361 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? 0.51345  0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ASN   A 1 6   ? -7.32585  -8.95395  47.27020  1.000 94.02658 ? 5   ASN   A N   1 
ATOM   2    C  CA  . ASN   A 1 6   ? -6.06387  -9.64875  47.04844  1.000 82.26770 ? 5   ASN   A CA  1 
ATOM   3    C  C   . ASN   A 1 6   ? -5.89069  -10.03794 45.58267  0.000 75.59318 ? 5   ASN   A C   1 
ATOM   4    O  O   . ASN   A 1 6   ? -6.14589  -9.24105  44.67950  0.000 73.45020 ? 5   ASN   A O   1 
ATOM   5    C  CB  . ASN   A 1 6   ? -5.97700  -10.89360 47.93417  0.000 81.32519 ? 5   ASN   A CB  1 
ATOM   6    N  N   . MET   A 1 7   ? -5.46091  -11.27649 45.36100  1.000 73.22792 ? 6   MET   A N   1 
ATOM   7    C  CA  . MET   A 1 7   ? -5.16773  -11.75637 44.01631  1.000 73.87313 ? 6   MET   A CA  1 
ATOM   8    C  C   . MET   A 1 7   ? -6.41968  -11.72737 43.13857  1.000 67.24028 ? 6   MET   A C   1 
ATOM   9    O  O   . MET   A 1 7   ? -7.40881  -12.41184 43.42064  1.000 54.52994 ? 6   MET   A O   1 
ATOM   10   C  CB  . MET   A 1 7   ? -4.59418  -13.17166 44.09305  1.000 71.63070 ? 6   MET   A CB  1 
ATOM   11   C  CG  . MET   A 1 7   ? -4.79225  -13.99715 42.83260  1.000 74.23696 ? 6   MET   A CG  1 
ATOM   12   S  SD  . MET   A 1 7   ? -3.36432  -13.97778 41.72783  1.000 88.99383 ? 6   MET   A SD  1 
ATOM   13   C  CE  . MET   A 1 7   ? -2.68726  -15.60912 42.03736  1.000 82.75267 ? 6   MET   A CE  1 
ATOM   14   N  N   . ALA   A 1 8   ? -6.37156  -10.93255 42.07179  1.000 43.82892 ? 7   ALA   A N   1 
ATOM   15   C  CA  . ALA   A 1 8   ? -7.48513  -10.84300 41.13835  1.000 40.65098 ? 7   ALA   A CA  1 
ATOM   16   C  C   . ALA   A 1 8   ? -7.71971  -12.18654 40.45183  1.000 41.24338 ? 7   ALA   A C   1 
ATOM   17   O  O   . ALA   A 1 8   ? -6.81697  -13.02032 40.33400  1.000 38.53082 ? 7   ALA   A O   1 
ATOM   18   C  CB  . ALA   A 1 8   ? -7.21598  -9.75887  40.09266  1.000 42.46681 ? 7   ALA   A CB  1 
ATOM   19   N  N   . SER   A 1 9   ? -8.95446  -12.39223 39.98773  1.000 33.55560 ? 8   SER   A N   1 
ATOM   20   C  CA  . SER   A 1 9   ? -9.27167  -13.61379 39.26064  1.000 30.24235 ? 8   SER   A CA  1 
ATOM   21   C  C   . SER   A 1 9   ? -8.42778  -13.69814 37.99004  1.000 27.14230 ? 8   SER   A C   1 
ATOM   22   O  O   . SER   A 1 9   ? -7.97139  -12.69113 37.44110  1.000 28.66829 ? 8   SER   A O   1 
ATOM   23   C  CB  . SER   A 1 9   ? -10.75593 -13.66688 38.88939  1.000 29.67145 ? 8   SER   A CB  1 
ATOM   24   O  OG  . SER   A 1 9   ? -11.08303 -12.63272 37.96325  1.000 30.80689 ? 8   SER   A OG  1 
ATOM   25   N  N   . LEU   A 1 10  ? -8.22108  -14.91934 37.51117  1.000 27.77138 ? 9   LEU   A N   1 
ATOM   26   C  CA  . LEU   A 1 10  ? -7.44115  -15.06745 36.28565  1.000 26.99954 ? 9   LEU   A CA  1 
ATOM   27   C  C   . LEU   A 1 10  ? -8.11295  -14.35694 35.11352  1.000 23.90299 ? 9   LEU   A C   1 
ATOM   28   O  O   . LEU   A 1 10  ? -7.43437  -13.72839 34.29715  1.000 23.18357 ? 9   LEU   A O   1 
ATOM   29   C  CB  . LEU   A 1 10  ? -7.21625  -16.54462 35.98649  1.000 24.33591 ? 9   LEU   A CB  1 
ATOM   30   C  CG  . LEU   A 1 10  ? -6.47150  -16.88038 34.69496  1.000 27.91893 ? 9   LEU   A CG  1 
ATOM   31   C  CD1 . LEU   A 1 10  ? -5.12477  -16.15311 34.64466  1.000 27.74598 ? 9   LEU   A CD1 1 
ATOM   32   C  CD2 . LEU   A 1 10  ? -6.28651  -18.38486 34.55414  1.000 32.29507 ? 9   LEU   A CD2 1 
ATOM   33   N  N   . ILE   A 1 11  ? -9.44754  -14.41543 35.01581  1.000 24.65991 ? 10  ILE   A N   1 
ATOM   34   C  CA  . ILE   A 1 11  ? -10.08315 -13.73389 33.88904  1.000 25.00571 ? 10  ILE   A CA  1 
ATOM   35   C  C   . ILE   A 1 11  ? -9.93996  -12.21566 34.01222  1.000 24.28136 ? 10  ILE   A C   1 
ATOM   36   O  O   . ILE   A 1 11  ? -9.76457  -11.53082 32.99345  1.000 24.38298 ? 10  ILE   A O   1 
ATOM   37   C  CB  . ILE   A 1 11  ? -11.55514 -14.17760 33.70676  1.000 23.54924 ? 10  ILE   A CB  1 
ATOM   38   C  CG1 . ILE   A 1 11  ? -12.12966 -13.64312 32.39222  1.000 23.57198 ? 10  ILE   A CG1 1 
ATOM   39   C  CG2 . ILE   A 1 11  ? -12.42746 -13.74344 34.90668  1.000 26.62416 ? 10  ILE   A CG2 1 
ATOM   40   C  CD1 . ILE   A 1 11  ? -11.42377 -14.14930 31.11468  1.000 21.38982 ? 10  ILE   A CD1 1 
ATOM   41   N  N   . GLN   A 1 12  ? -9.97296  -11.65694 35.23329  1.000 22.64516 ? 11  GLN   A N   1 
ATOM   42   C  CA  . GLN   A 1 12  ? -9.68615  -10.22996 35.37050  1.000 22.80692 ? 11  GLN   A CA  1 
ATOM   43   C  C   . GLN   A 1 12  ? -8.25426  -9.92374  34.94562  1.000 26.47596 ? 11  GLN   A C   1 
ATOM   44   O  O   . GLN   A 1 12  ? -7.99853  -8.91763  34.26767  1.000 26.56968 ? 11  GLN   A O   1 
ATOM   45   C  CB  . GLN   A 1 12  ? -9.92905  -9.76472  36.80772  1.000 28.72432 ? 11  GLN   A CB  1 
ATOM   46   C  CG  . GLN   A 1 12  ? -9.52774  -8.31322  37.03892  1.000 30.33286 ? 11  GLN   A CG  1 
ATOM   47   C  CD  . GLN   A 1 12  ? -10.60315 -7.32601  36.60012  1.000 34.21213 ? 11  GLN   A CD  1 
ATOM   48   O  OE1 . GLN   A 1 12  ? -11.79291 -7.60163  36.71608  1.000 35.31117 ? 11  GLN   A OE1 1 
ATOM   49   N  NE2 . GLN   A 1 12  ? -10.17707 -6.15416  36.10361  1.000 35.45621 ? 11  GLN   A NE2 1 
ATOM   50   N  N   . ARG   A 1 13  ? -7.30403  -10.79098 35.31422  1.000 23.97753 ? 12  ARG   A N   1 
ATOM   51   C  CA  A ARG   A 1 13  ? -5.92154  -10.55697 34.90675  0.433 24.86563 ? 12  ARG   A CA  1 
ATOM   52   C  CA  B ARG   A 1 13  ? -5.91924  -10.56286 34.90942  0.567 24.82278 ? 12  ARG   A CA  1 
ATOM   53   C  C   . ARG   A 1 13  ? -5.76420  -10.66395 33.39489  1.000 26.06619 ? 12  ARG   A C   1 
ATOM   54   O  O   . ARG   A 1 13  ? -4.97497  -9.92057  32.78900  1.000 26.09233 ? 12  ARG   A O   1 
ATOM   55   C  CB  A ARG   A 1 13  ? -4.98893  -11.52892 35.61858  0.433 26.52942 ? 12  ARG   A CB  1 
ATOM   56   C  CB  B ARG   A 1 13  ? -5.00158  -11.54781 35.63149  0.567 26.47092 ? 12  ARG   A CB  1 
ATOM   57   C  CG  A ARG   A 1 13  ? -4.93171  -11.30939 37.11660  0.433 31.42384 ? 12  ARG   A CG  1 
ATOM   58   C  CG  B ARG   A 1 13  ? -4.86026  -11.23269 37.11801  0.567 31.42985 ? 12  ARG   A CG  1 
ATOM   59   C  CD  A ARG   A 1 13  ? -4.46854  -12.55832 37.82663  0.433 37.63089 ? 12  ARG   A CD  1 
ATOM   60   C  CD  B ARG   A 1 13  ? -3.87295  -12.16320 37.80063  0.567 37.57259 ? 12  ARG   A CD  1 
ATOM   61   N  NE  A ARG   A 1 13  ? -3.02354  -12.68778 37.68338  0.433 37.90419 ? 12  ARG   A NE  1 
ATOM   62   N  NE  B ARG   A 1 13  ? -4.50377  -13.41622 38.19586  0.567 37.39327 ? 12  ARG   A NE  1 
ATOM   63   C  CZ  A ARG   A 1 13  ? -2.41795  -13.71520 37.10787  0.433 34.97922 ? 12  ARG   A CZ  1 
ATOM   64   C  CZ  B ARG   A 1 13  ? -3.95370  -14.61348 38.04657  0.567 37.85047 ? 12  ARG   A CZ  1 
ATOM   65   N  NH1 A ARG   A 1 13  ? -3.09501  -14.77452 36.70340  0.433 44.59059 ? 12  ARG   A NH1 1 
ATOM   66   N  NH1 B ARG   A 1 13  ? -2.74739  -14.76019 37.52123  0.567 33.76380 ? 12  ARG   A NH1 1 
ATOM   67   N  NH2 A ARG   A 1 13  ? -1.09739  -13.68293 36.94392  0.433 37.43452 ? 12  ARG   A NH2 1 
ATOM   68   N  NH2 B ARG   A 1 13  ? -4.62540  -15.68916 38.44841  0.567 37.07514 ? 12  ARG   A NH2 1 
ATOM   69   N  N   . ILE   A 1 14  ? -6.50618  -11.57310 32.76380  1.000 23.58163 ? 13  ILE   A N   1 
ATOM   70   C  CA  . ILE   A 1 14  ? -6.46670  -11.66720 31.30793  1.000 24.64403 ? 13  ILE   A CA  1 
ATOM   71   C  C   . ILE   A 1 14  ? -6.98642  -10.37927 30.68223  1.000 26.17638 ? 13  ILE   A C   1 
ATOM   72   O  O   . ILE   A 1 14  ? -6.38568  -9.84376  29.74485  1.000 24.73096 ? 13  ILE   A O   1 
ATOM   73   C  CB  . ILE   A 1 14  ? -7.26260  -12.89665 30.83636  1.000 20.63254 ? 13  ILE   A CB  1 
ATOM   74   C  CG1 . ILE   A 1 14  ? -6.44477  -14.16662 31.09959  1.000 21.68483 ? 13  ILE   A CG1 1 
ATOM   75   C  CG2 . ILE   A 1 14  ? -7.63756  -12.76570 29.35167  1.000 22.35340 ? 13  ILE   A CG2 1 
ATOM   76   C  CD1 . ILE   A 1 14  ? -7.29977  -15.46373 31.02894  1.000 25.41441 ? 13  ILE   A CD1 1 
ATOM   77   N  N   . ALA   A 1 15  ? -8.09832  -9.84854  31.20132  1.000 21.08196 ? 14  ALA   A N   1 
ATOM   78   C  CA  . ALA   A 1 15  ? -8.64900  -8.61431  30.64720  1.000 24.09187 ? 14  ALA   A CA  1 
ATOM   79   C  C   . ALA   A 1 15  ? -7.67525  -7.45297  30.82875  1.000 25.97275 ? 14  ALA   A C   1 
ATOM   80   O  O   . ALA   A 1 15  ? -7.43790  -6.67157  29.89816  1.000 27.69772 ? 14  ALA   A O   1 
ATOM   81   C  CB  . ALA   A 1 15  ? -10.00015 -8.30123  31.30696  1.000 25.46307 ? 14  ALA   A CB  1 
ATOM   82   N  N   . ARG   A 1 16  ? -7.12144  -7.31850  32.03861  1.000 25.74067 ? 15  ARG   A N   1 
ATOM   83   C  CA  A ARG   A 1 16  ? -6.12086  -6.28995  32.31312  0.522 27.43265 ? 15  ARG   A CA  1 
ATOM   84   C  CA  B ARG   A 1 16  ? -6.13886  -6.26998  32.28634  0.478 27.44421 ? 15  ARG   A CA  1 
ATOM   85   C  C   . ARG   A 1 16  ? -4.94762  -6.38732  31.34494  1.000 32.81335 ? 15  ARG   A C   1 
ATOM   86   O  O   . ARG   A 1 16  ? -4.45337  -5.37319  30.83496  1.000 30.50976 ? 15  ARG   A O   1 
ATOM   87   C  CB  A ARG   A 1 16  ? -5.65838  -6.43235  33.76815  0.522 30.25489 ? 15  ARG   A CB  1 
ATOM   88   C  CB  B ARG   A 1 16  ? -5.66948  -6.31050  33.74076  0.478 30.25529 ? 15  ARG   A CB  1 
ATOM   89   C  CG  A ARG   A 1 16  ? -4.69044  -5.38947  34.30889  0.522 38.92287 ? 15  ARG   A CG  1 
ATOM   90   C  CG  B ARG   A 1 16  ? -4.88914  -5.07473  34.14006  0.478 38.81582 ? 15  ARG   A CG  1 
ATOM   91   C  CD  A ARG   A 1 16  ? -4.75578  -5.35853  35.84228  0.522 37.75951 ? 15  ARG   A CD  1 
ATOM   92   C  CD  B ARG   A 1 16  ? -3.96190  -5.36486  35.30080  0.478 38.57084 ? 15  ARG   A CD  1 
ATOM   93   N  NE  A ARG   A 1 16  ? -5.96643  -6.00212  36.34291  0.522 40.29513 ? 15  ARG   A NE  1 
ATOM   94   N  NE  B ARG   A 1 16  ? -4.36565  -4.65059  36.50400  0.478 47.27255 ? 15  ARG   A NE  1 
ATOM   95   C  CZ  A ARG   A 1 16  ? -6.31897  -6.06721  37.61895  0.522 43.66465 ? 15  ARG   A CZ  1 
ATOM   96   C  CZ  B ARG   A 1 16  ? -3.59971  -3.78088  37.14818  0.478 41.21374 ? 15  ARG   A CZ  1 
ATOM   97   N  NH1 A ARG   A 1 16  ? -5.46654  -5.78416  38.58862  0.522 50.64956 ? 15  ARG   A NH1 1 
ATOM   98   N  NH1 B ARG   A 1 16  ? -2.37856  -3.49523  36.73061  0.478 45.77699 ? 15  ARG   A NH1 1 
ATOM   99   N  NH2 A ARG   A 1 16  ? -7.56112  -6.41500  37.92923  0.522 52.95023 ? 15  ARG   A NH2 1 
ATOM   100  N  NH2 B ARG   A 1 16  ? -4.07483  -3.17729  38.23395  0.478 47.22983 ? 15  ARG   A NH2 1 
ATOM   101  N  N   . GLN   A 1 17  ? -4.46279  -7.60261  31.10523  1.000 27.92733 ? 16  GLN   A N   1 
ATOM   102  C  CA  . GLN   A 1 17  ? -3.30617  -7.73711  30.22896  1.000 28.87061 ? 16  GLN   A CA  1 
ATOM   103  C  C   . GLN   A 1 17  ? -3.68129  -7.51122  28.76965  1.000 29.30546 ? 16  GLN   A C   1 
ATOM   104  O  O   . GLN   A 1 17  ? -2.87317  -6.97259  28.00170  1.000 28.15179 ? 16  GLN   A O   1 
ATOM   105  C  CB  . GLN   A 1 17  ? -2.66532  -9.11091  30.42137  1.000 27.14085 ? 16  GLN   A CB  1 
ATOM   106  C  CG  . GLN   A 1 17  ? -1.40681  -9.35976  29.58422  1.000 25.79456 ? 16  GLN   A CG  1 
ATOM   107  C  CD  . GLN   A 1 17  ? -0.24487  -8.45396  29.95960  1.000 30.31377 ? 16  GLN   A CD  1 
ATOM   108  O  OE1 . GLN   A 1 17  ? -0.14379  -7.97085  31.09755  1.000 31.96423 ? 16  GLN   A OE1 1 
ATOM   109  N  NE2 . GLN   A 1 17  ? 0.64622   -8.21460  28.99855  1.000 30.77154 ? 16  GLN   A NE2 1 
ATOM   110  N  N   . ALA   A 1 18  ? -4.89159  -7.91150  28.36749  1.000 24.66683 ? 17  ALA   A N   1 
ATOM   111  C  CA  . ALA   A 1 18  ? -5.35262  -7.60526  27.01943  1.000 27.50259 ? 17  ALA   A CA  1 
ATOM   112  C  C   . ALA   A 1 18  ? -5.42477  -6.09770  26.79919  1.000 29.18381 ? 17  ALA   A C   1 
ATOM   113  O  O   . ALA   A 1 18  ? -5.03761  -5.60057  25.73563  1.000 29.46612 ? 17  ALA   A O   1 
ATOM   114  C  CB  . ALA   A 1 18  ? -6.71233  -8.25576  26.76876  1.000 22.32817 ? 17  ALA   A CB  1 
ATOM   115  N  N   . SER   A 1 19  ? -5.90624  -5.35102  27.80238  1.000 29.72215 ? 18  SER   A N   1 
ATOM   116  C  CA  . SER   A 1 19  ? -5.94515  -3.89332  27.67788  1.000 30.20247 ? 18  SER   A CA  1 
ATOM   117  C  C   . SER   A 1 19  ? -4.55112  -3.30686  27.50058  1.000 37.23618 ? 18  SER   A C   1 
ATOM   118  O  O   . SER   A 1 19  ? -4.34545  -2.41832  26.66527  1.000 39.97779 ? 18  SER   A O   1 
ATOM   119  C  CB  . SER   A 1 19  ? -6.62225  -3.26677  28.89199  1.000 34.80581 ? 18  SER   A CB  1 
ATOM   120  O  OG  . SER   A 1 19  ? -7.00842  -1.93204  28.59494  0.464 31.95382 ? 18  SER   A OG  1 
ATOM   121  N  N   . LEU   A 1 20  ? -3.57984  -3.79427  28.27074  1.000 28.67390 ? 19  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 20  ? -2.21123  -3.30036  28.14554  1.000 32.85811 ? 19  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 20  ? -1.60700  -3.64110  26.78247  1.000 34.97548 ? 19  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 20  ? -0.86663  -2.83648  26.20227  1.000 37.42719 ? 19  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 20  ? -1.36750  -3.88884  29.26998  1.000 33.10281 ? 19  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 20  ? -0.07451  -3.19617  29.63540  1.000 48.41469 ? 19  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 20  ? -0.37247  -1.97616  30.48590  1.000 45.88702 ? 19  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 20  ? 0.78166   -4.18918  30.39116  1.000 54.72641 ? 19  LEU   A CD2 1 
ATOM   129  N  N   . THR   A 1 21  ? -1.90416  -4.83421  26.26255  1.000 30.59851 ? 20  THR   A N   1 
ATOM   130  C  CA  . THR   A 1 21  ? -1.33374  -5.28623  24.99926  1.000 31.52677 ? 20  THR   A CA  1 
ATOM   131  C  C   . THR   A 1 21  ? -1.93812  -4.54130  23.81968  1.000 35.05832 ? 20  THR   A C   1 
ATOM   132  O  O   . THR   A 1 21  ? -1.22218  -4.15193  22.88834  1.000 37.88065 ? 20  THR   A O   1 
ATOM   133  C  CB  . THR   A 1 21  ? -1.58305  -6.78305  24.84038  1.000 30.21236 ? 20  THR   A CB  1 
ATOM   134  O  OG1 . THR   A 1 21  ? -1.01867  -7.47194  25.96127  1.000 27.89023 ? 20  THR   A OG1 1 
ATOM   135  C  CG2 . THR   A 1 21  ? -0.97250  -7.31091  23.53628  1.000 32.79090 ? 20  THR   A CG2 1 
ATOM   136  N  N   . PHE   A 1 22  ? -3.25312  -4.33720  23.85253  1.000 34.69386 ? 21  PHE   A N   1 
ATOM   137  C  CA  . PHE   A 1 22  ? -4.03411  -3.73457  22.77591  1.000 40.79203 ? 21  PHE   A CA  1 
ATOM   138  C  C   . PHE   A 1 22  ? -4.65180  -2.44419  23.31618  1.000 52.79744 ? 21  PHE   A C   1 
ATOM   139  O  O   . PHE   A 1 22  ? -5.75451  -2.45708  23.87684  1.000 49.49639 ? 21  PHE   A O   1 
ATOM   140  C  CB  . PHE   A 1 22  ? -5.12911  -4.68505  22.27502  1.000 33.26677 ? 21  PHE   A CB  1 
ATOM   141  C  CG  . PHE   A 1 22  ? -4.64145  -6.05614  21.87541  1.000 30.24072 ? 21  PHE   A CG  1 
ATOM   142  C  CD1 . PHE   A 1 22  ? -3.90169  -6.24055  20.71083  1.000 30.81609 ? 21  PHE   A CD1 1 
ATOM   143  C  CD2 . PHE   A 1 22  ? -4.96899  -7.16944  22.63308  1.000 31.65568 ? 21  PHE   A CD2 1 
ATOM   144  C  CE1 . PHE   A 1 22  ? -3.48065  -7.50850  20.33079  1.000 28.62868 ? 21  PHE   A CE1 1 
ATOM   145  C  CE2 . PHE   A 1 22  ? -4.54861  -8.44210  22.25804  1.000 34.28041 ? 21  PHE   A CE2 1 
ATOM   146  C  CZ  . PHE   A 1 22  ? -3.80084  -8.61238  21.10439  1.000 31.64728 ? 21  PHE   A CZ  1 
ATOM   147  N  N   . ARG   A 1 23  ? -3.94222  -1.33381  23.15293  1.000 56.73534 ? 22  ARG   A N   1 
ATOM   148  C  CA  . ARG   A 1 23  ? -4.46196  -0.02613  23.54746  1.000 57.11313 ? 22  ARG   A CA  1 
ATOM   149  C  C   . ARG   A 1 23  ? -4.95474  0.75506   22.33110  1.000 61.02781 ? 22  ARG   A C   1 
ATOM   150  O  O   . ARG   A 1 23  ? -5.94277  0.37910   21.69515  1.000 63.04379 ? 22  ARG   A O   1 
ATOM   151  C  CB  . ARG   A 1 23  ? -3.39507  0.78521   24.28338  1.000 58.64500 ? 22  ARG   A CB  1 
ATOM   152  C  CG  . ARG   A 1 23  ? -2.72208  0.06038   25.43059  1.000 52.95534 ? 22  ARG   A CG  1 
ATOM   153  C  CD  . ARG   A 1 23  ? -2.06374  1.04644   26.38781  0.000 52.25605 ? 22  ARG   A CD  1 
ATOM   154  N  NE  . ARG   A 1 23  ? -0.86726  1.66018   25.82234  0.000 53.12923 ? 22  ARG   A NE  1 
ATOM   155  C  CZ  . ARG   A 1 23  ? 0.22772   0.99573   25.47816  0.000 52.70060 ? 22  ARG   A CZ  1 
ATOM   156  N  NH1 . ARG   A 1 23  ? 0.31693   -0.31570  25.62852  0.000 50.12643 ? 22  ARG   A NH1 1 
ATOM   157  N  NH2 . ARG   A 1 23  ? 1.26104   1.66452   24.97384  0.000 53.70887 ? 22  ARG   A NH2 1 
ATOM   158  N  N   . GLN   A 1 45  ? 4.59479   -1.51132  17.54060  1.000 62.02124 ? 44  GLN   A N   1 
ATOM   159  C  CA  . GLN   A 1 45  ? 5.02867   -0.67581  18.65211  1.000 60.31031 ? 44  GLN   A CA  1 
ATOM   160  C  C   . GLN   A 1 45  ? 5.93086   -1.45237  19.60239  1.000 62.89438 ? 44  GLN   A C   1 
ATOM   161  O  O   . GLN   A 1 45  ? 5.69149   -2.63147  19.86039  1.000 52.54655 ? 44  GLN   A O   1 
ATOM   162  C  CB  . GLN   A 1 45  ? 3.82095   -0.13405  19.41359  1.000 62.04122 ? 44  GLN   A CB  1 
ATOM   163  C  CG  . GLN   A 1 45  ? 2.98637   0.84707   18.62546  1.000 68.66392 ? 44  GLN   A CG  1 
ATOM   164  C  CD  . GLN   A 1 45  ? 1.56900   0.93033   19.14256  0.380 74.24569 ? 44  GLN   A CD  1 
ATOM   165  O  OE1 . GLN   A 1 45  ? 1.15378   0.11826   19.97016  1.000 72.59992 ? 44  GLN   A OE1 1 
ATOM   166  N  NE2 . GLN   A 1 45  ? 0.81572   1.91225   18.65869  1.000 90.40740 ? 44  GLN   A NE2 1 
ATOM   167  N  N   . PRO   A 1 46  ? 6.98125   -0.80306  20.10447  1.000 69.49720 ? 45  PRO   A N   1 
ATOM   168  C  CA  . PRO   A 1 46  ? 7.79005   -1.42721  21.15572  1.000 60.78400 ? 45  PRO   A CA  1 
ATOM   169  C  C   . PRO   A 1 46  ? 6.90906   -1.84229  22.32451  1.000 58.94885 ? 45  PRO   A C   1 
ATOM   170  O  O   . PRO   A 1 46  ? 5.89986   -1.20130  22.62700  1.000 59.26971 ? 45  PRO   A O   1 
ATOM   171  C  CB  . PRO   A 1 46  ? 8.77441   -0.32162  21.55565  1.000 64.18078 ? 45  PRO   A CB  1 
ATOM   172  C  CG  . PRO   A 1 46  ? 8.90211   0.52965   20.34126  1.000 67.01027 ? 45  PRO   A CG  1 
ATOM   173  C  CD  . PRO   A 1 46  ? 7.59769   0.42883   19.57908  1.000 68.56553 ? 45  PRO   A CD  1 
ATOM   174  N  N   . GLY   A 1 47  ? 7.29693   -2.93429  22.97860  1.000 50.42958 ? 46  GLY   A N   1 
ATOM   175  C  CA  . GLY   A 1 47  ? 6.55088   -3.46770  24.09305  1.000 40.57237 ? 46  GLY   A CA  1 
ATOM   176  C  C   . GLY   A 1 47  ? 5.44673   -4.43113  23.71451  1.000 36.33610 ? 46  GLY   A C   1 
ATOM   177  O  O   . GLY   A 1 47  ? 5.07337   -5.27396  24.53840  1.000 35.22999 ? 46  GLY   A O   1 
ATOM   178  N  N   . PHE   A 1 48  ? 4.93283   -4.35147  22.48268  1.000 36.65277 ? 47  PHE   A N   1 
ATOM   179  C  CA  . PHE   A 1 48  ? 3.85375   -5.24621  22.05923  1.000 32.80712 ? 47  PHE   A CA  1 
ATOM   180  C  C   . PHE   A 1 48  ? 4.21040   -6.72195  22.16037  1.000 32.87711 ? 47  PHE   A C   1 
ATOM   181  O  O   . PHE   A 1 48  ? 3.42227   -7.48864  22.74221  1.000 30.94782 ? 47  PHE   A O   1 
ATOM   182  C  CB  . PHE   A 1 48  ? 3.43017   -4.90917  20.62682  1.000 38.88797 ? 47  PHE   A CB  1 
ATOM   183  C  CG  . PHE   A 1 48  ? 2.37802   -5.82658  20.08541  1.000 31.22305 ? 47  PHE   A CG  1 
ATOM   184  C  CD1 . PHE   A 1 48  ? 1.06075   -5.69990  20.47732  1.000 33.10461 ? 47  PHE   A CD1 1 
ATOM   185  C  CD2 . PHE   A 1 48  ? 2.71909   -6.83615  19.19851  1.000 34.94151 ? 47  PHE   A CD2 1 
ATOM   186  C  CE1 . PHE   A 1 48  ? 0.09134   -6.56186  19.98306  1.000 36.20103 ? 47  PHE   A CE1 1 
ATOM   187  C  CE2 . PHE   A 1 48  ? 1.76301   -7.69339  18.69550  1.000 33.16014 ? 47  PHE   A CE2 1 
ATOM   188  C  CZ  . PHE   A 1 48  ? 0.44263   -7.56127  19.09312  1.000 33.76840 ? 47  PHE   A CZ  1 
ATOM   189  N  N   . PRO   A 1 49  ? 5.32651   -7.19495  21.60465  1.000 31.99065 ? 48  PRO   A N   1 
ATOM   190  C  CA  . PRO   A 1 49  ? 5.59800   -8.64264  21.64765  1.000 31.56552 ? 48  PRO   A CA  1 
ATOM   191  C  C   . PRO   A 1 49  ? 5.67054   -9.18425  23.06311  1.000 31.79097 ? 48  PRO   A C   1 
ATOM   192  O  O   . PRO   A 1 49  ? 5.16164   -10.27645 23.35469  1.000 30.61658 ? 48  PRO   A O   1 
ATOM   193  C  CB  . PRO   A 1 49  ? 6.95399   -8.75953  20.93140  1.000 36.65725 ? 48  PRO   A CB  1 
ATOM   194  C  CG  . PRO   A 1 49  ? 7.11197   -7.47189  20.17266  1.000 40.43648 ? 48  PRO   A CG  1 
ATOM   195  C  CD  . PRO   A 1 49  ? 6.42696   -6.43742  20.98458  1.000 36.94992 ? 48  PRO   A CD  1 
ATOM   196  N  N   . GLU   A 1 50  ? 6.30593   -8.43207  23.95389  1.000 33.27483 ? 49  GLU   A N   1 
ATOM   197  C  CA  . GLU   A 1 50  ? 6.43190   -8.85904  25.33987  1.000 31.42117 ? 49  GLU   A CA  1 
ATOM   198  C  C   . GLU   A 1 50  ? 5.06627   -8.92693  26.01174  1.000 33.08429 ? 49  GLU   A C   1 
ATOM   199  O  O   . GLU   A 1 50  ? 4.77433   -9.86907  26.76355  1.000 31.10464 ? 49  GLU   A O   1 
ATOM   200  C  CB  . GLU   A 1 50  ? 7.34862   -7.88289  26.06988  1.000 35.00699 ? 49  GLU   A CB  1 
ATOM   201  C  CG  . GLU   A 1 50  ? 8.80413   -7.97644  25.61963  1.000 39.91189 ? 49  GLU   A CG  1 
ATOM   202  C  CD  . GLU   A 1 50  ? 9.08377   -7.20043  24.32292  1.000 53.08441 ? 49  GLU   A CD  1 
ATOM   203  O  OE1 . GLU   A 1 50  ? 8.23144   -6.39818  23.89116  0.601 36.35091 ? 49  GLU   A OE1 1 
ATOM   204  O  OE2 . GLU   A 1 50  ? 10.17176  -7.38916  23.73300  1.000 64.97241 ? 49  GLU   A OE2 1 
ATOM   205  N  N   . ASN   A 1 51  ? 4.21311   -7.93718  25.74225  1.000 30.79658 ? 50  ASN   A N   1 
ATOM   206  C  CA  . ASN   A 1 51  ? 2.86598   -7.95591  26.30082  1.000 29.51550 ? 50  ASN   A CA  1 
ATOM   207  C  C   . ASN   A 1 51  ? 2.03990   -9.09006  25.71180  1.000 28.22563 ? 50  ASN   A C   1 
ATOM   208  O  O   . ASN   A 1 51  ? 1.27919   -9.75151  26.43267  1.000 28.21837 ? 50  ASN   A O   1 
ATOM   209  C  CB  . ASN   A 1 51  ? 2.18631   -6.61198  26.05638  1.000 28.31162 ? 50  ASN   A CB  1 
ATOM   210  C  CG  . ASN   A 1 51  ? 2.60558   -5.57044  27.06384  1.000 36.90781 ? 50  ASN   A CG  1 
ATOM   211  O  OD1 . ASN   A 1 51  ? 2.94555   -5.90116  28.20650  1.000 39.97280 ? 50  ASN   A OD1 1 
ATOM   212  N  ND2 . ASN   A 1 51  ? 2.62601   -4.31370  26.64131  1.000 34.69410 ? 50  ASN   A ND2 1 
ATOM   213  N  N   . LEU   A 1 52  ? 2.15396   -9.31804  24.39885  1.000 26.33422 ? 51  LEU   A N   1 
ATOM   214  C  CA  . LEU   A 1 52  ? 1.41546   -10.41550 23.78500  1.000 25.01585 ? 51  LEU   A CA  1 
ATOM   215  C  C   . LEU   A 1 52  ? 1.87206   -11.75385 24.33993  1.000 25.98391 ? 51  LEU   A C   1 
ATOM   216  O  O   . LEU   A 1 52  ? 1.05515   -12.66050 24.54329  1.000 25.79608 ? 51  LEU   A O   1 
ATOM   217  C  CB  . LEU   A 1 52  ? 1.57867   -10.37178 22.26497  1.000 26.53236 ? 51  LEU   A CB  1 
ATOM   218  C  CG  . LEU   A 1 52  ? 0.66455   -11.28562 21.44178  1.000 27.70384 ? 51  LEU   A CG  1 
ATOM   219  C  CD1 . LEU   A 1 52  ? -0.77038  -10.80711 21.45888  1.000 30.36706 ? 51  LEU   A CD1 1 
ATOM   220  C  CD2 . LEU   A 1 52  ? 1.20117   -11.35789 20.00791  1.000 30.66382 ? 51  LEU   A CD2 1 
ATOM   221  N  N   . SER   A 1 53  ? 3.17430   -11.90710 24.58613  1.000 29.58663 ? 52  SER   A N   1 
ATOM   222  C  CA  A SER   A 1 53  ? 3.66134   -13.16274 25.14467  0.641 28.91505 ? 52  SER   A CA  1 
ATOM   223  C  CA  B SER   A 1 53  ? 3.65514   -13.16635 25.14200  0.359 28.99685 ? 52  SER   A CA  1 
ATOM   224  C  C   . SER   A 1 53  ? 3.08006   -13.40121 26.53049  1.000 27.59307 ? 52  SER   A C   1 
ATOM   225  O  O   . SER   A 1 53  ? 2.66868   -14.52264 26.86107  1.000 29.12250 ? 52  SER   A O   1 
ATOM   226  C  CB  A SER   A 1 53  ? 5.18834   -13.15590 25.19384  0.641 32.77177 ? 52  SER   A CB  1 
ATOM   227  C  CB  B SER   A 1 53  ? 5.18165   -13.17635 25.17338  0.359 32.82139 ? 52  SER   A CB  1 
ATOM   228  O  OG  A SER   A 1 53  ? 5.66336   -14.26883 25.92407  0.641 37.13677 ? 52  SER   A OG  1 
ATOM   229  O  OG  B SER   A 1 53  ? 5.69733   -13.32264 23.86261  0.359 34.60850 ? 52  SER   A OG  1 
ATOM   230  N  N   . LYS   A 1 54  ? 3.03882   -12.35275 27.35599  1.000 27.84997 ? 53  LYS   A N   1 
ATOM   231  C  CA  A LYS   A 1 54  ? 2.45650   -12.49210 28.68343  0.491 28.89433 ? 53  LYS   A CA  1 
ATOM   232  C  CA  B LYS   A 1 54  ? 2.45154   -12.47656 28.68463  0.509 28.90034 ? 53  LYS   A CA  1 
ATOM   233  C  C   . LYS   A 1 54  ? 0.97125   -12.82900 28.59771  1.000 29.00617 ? 53  LYS   A C   1 
ATOM   234  O  O   . LYS   A 1 54  ? 0.47515   -13.66001 29.36673  1.000 26.13468 ? 53  LYS   A O   1 
ATOM   235  C  CB  A LYS   A 1 54  ? 2.68780   -11.21565 29.49227  0.491 30.22208 ? 53  LYS   A CB  1 
ATOM   236  C  CB  B LYS   A 1 54  ? 2.65467   -11.17602 29.46038  0.509 30.21638 ? 53  LYS   A CB  1 
ATOM   237  C  CG  A LYS   A 1 54  ? 1.88014   -11.15318 30.77588  0.491 30.98129 ? 53  LYS   A CG  1 
ATOM   238  C  CG  B LYS   A 1 54  ? 4.10187   -10.87156 29.77717  0.509 35.99964 ? 53  LYS   A CG  1 
ATOM   239  C  CD  A LYS   A 1 54  ? 2.75220   -10.89339 31.97856  0.491 41.99694 ? 53  LYS   A CD  1 
ATOM   240  C  CD  B LYS   A 1 54  ? 4.23579   -9.54099  30.51368  0.509 43.24372 ? 53  LYS   A CD  1 
ATOM   241  C  CE  A LYS   A 1 54  ? 1.90877   -10.85119 33.23685  0.491 39.45147 ? 53  LYS   A CE  1 
ATOM   242  C  CE  B LYS   A 1 54  ? 5.68119   -9.24780  30.86914  0.509 40.08102 ? 53  LYS   A CE  1 
ATOM   243  N  NZ  A LYS   A 1 54  ? 1.54413   -9.45503  33.60809  0.491 49.31446 ? 53  LYS   A NZ  1 
ATOM   244  N  NZ  B LYS   A 1 54  ? 5.82160   -7.95585  31.59095  0.509 53.81536 ? 53  LYS   A NZ  1 
ATOM   245  N  N   . LEU   A 1 55  ? 0.24586   -12.20479 27.65839  1.000 25.08047 ? 54  LEU   A N   1 
ATOM   246  C  CA  . LEU   A 1 55  ? -1.16592  -12.53786 27.47465  1.000 22.46816 ? 54  LEU   A CA  1 
ATOM   247  C  C   . LEU   A 1 55  ? -1.33321  -13.99938 27.07970  1.000 24.68242 ? 54  LEU   A C   1 
ATOM   248  O  O   . LEU   A 1 55  ? -2.21150  -14.69307 27.59671  1.000 24.06334 ? 54  LEU   A O   1 
ATOM   249  C  CB  . LEU   A 1 55  ? -1.78705  -11.63270 26.40921  1.000 24.98171 ? 54  LEU   A CB  1 
ATOM   250  C  CG  . LEU   A 1 55  ? -3.28293  -11.79137 26.11017  1.000 21.38430 ? 54  LEU   A CG  1 
ATOM   251  C  CD1 . LEU   A 1 55  ? -4.15445  -11.62362 27.35820  1.000 23.67091 ? 54  LEU   A CD1 1 
ATOM   252  C  CD2 . LEU   A 1 55  ? -3.68736  -10.81151 25.00518  1.000 25.49100 ? 54  LEU   A CD2 1 
ATOM   253  N  N   . LYS   A 1 56  ? -0.50159  -14.48104 26.14798  1.000 24.27932 ? 55  LYS   A N   1 
ATOM   254  C  CA  . LYS   A 1 56  ? -0.56547  -15.88570 25.75514  1.000 24.51542 ? 55  LYS   A CA  1 
ATOM   255  C  C   . LYS   A 1 56  ? -0.32331  -16.79710 26.94648  1.000 26.30667 ? 55  LYS   A C   1 
ATOM   256  O  O   . LYS   A 1 56  ? -0.97353  -17.83810 27.08349  1.000 25.82365 ? 55  LYS   A O   1 
ATOM   257  C  CB  . LYS   A 1 56  ? 0.47152   -16.18289 24.66587  1.000 26.44975 ? 55  LYS   A CB  1 
ATOM   258  C  CG  . LYS   A 1 56  ? 0.24002   -15.46364 23.36067  1.000 37.42148 ? 55  LYS   A CG  1 
ATOM   259  C  CD  . LYS   A 1 56  ? 1.27960   -15.85307 22.30455  1.000 38.17828 ? 55  LYS   A CD  1 
ATOM   260  C  CE  . LYS   A 1 56  ? 1.17590   -17.32287 21.93089  1.000 47.02461 ? 55  LYS   A CE  1 
ATOM   261  N  NZ  . LYS   A 1 56  ? 2.15658   -18.16436 22.67406  1.000 58.87508 ? 55  LYS   A NZ  1 
ATOM   262  N  N   . SER   A 1 57  ? 0.63703   -16.44079 27.80078  1.000 27.30114 ? 56  SER   A N   1 
ATOM   263  C  CA  . SER   A 1 57  ? 0.94648   -17.28447 28.94906  1.000 27.17661 ? 56  SER   A CA  1 
ATOM   264  C  C   . SER   A 1 57  ? -0.23035  -17.33869 29.92032  1.000 29.71246 ? 56  SER   A C   1 
ATOM   265  O  O   . SER   A 1 57  ? -0.51605  -18.39508 30.50054  1.000 30.00368 ? 56  SER   A O   1 
ATOM   266  C  CB  . SER   A 1 57  ? 2.20951   -16.77692 29.65225  1.000 34.56527 ? 56  SER   A CB  1 
ATOM   267  O  OG  . SER   A 1 57  ? 2.25757   -17.21660 31.00136  1.000 44.29380 ? 56  SER   A OG  1 
ATOM   268  N  N   . LEU   A 1 58  ? -0.93936  -16.21712 30.09416  1.000 26.88164 ? 57  LEU   A N   1 
ATOM   269  C  CA  . LEU   A 1 58  ? -2.13883  -16.23846 30.92899  1.000 23.46568 ? 57  LEU   A CA  1 
ATOM   270  C  C   . LEU   A 1 58  ? -3.21860  -17.11755 30.31200  1.000 26.36019 ? 57  LEU   A C   1 
ATOM   271  O  O   . LEU   A 1 58  ? -3.88022  -17.88522 31.02421  1.000 26.97825 ? 57  LEU   A O   1 
ATOM   272  C  CB  . LEU   A 1 58  ? -2.67877  -14.82138 31.13588  1.000 28.29928 ? 57  LEU   A CB  1 
ATOM   273  C  CG  . LEU   A 1 58  ? -1.85484  -13.85989 31.98891  1.000 29.26781 ? 57  LEU   A CG  1 
ATOM   274  C  CD1 . LEU   A 1 58  ? -2.43858  -12.45936 31.85437  1.000 28.39048 ? 57  LEU   A CD1 1 
ATOM   275  C  CD2 . LEU   A 1 58  ? -1.79722  -14.30239 33.46148  1.000 32.30155 ? 57  LEU   A CD2 1 
ATOM   276  N  N   . LEU   A 1 59  ? -3.43569  -16.99675 28.99926  1.000 24.42449 ? 58  LEU   A N   1 
ATOM   277  C  CA  . LEU   A 1 59  ? -4.43964  -17.83648 28.34521  1.000 23.81747 ? 58  LEU   A CA  1 
ATOM   278  C  C   . LEU   A 1 59  ? -4.06045  -19.30525 28.41967  1.000 26.39396 ? 58  LEU   A C   1 
ATOM   279  O  O   . LEU   A 1 59  ? -4.93916  -20.17287 28.51723  1.000 27.71617 ? 58  LEU   A O   1 
ATOM   280  C  CB  . LEU   A 1 59  ? -4.61814  -17.41820 26.88587  1.000 25.68616 ? 58  LEU   A CB  1 
ATOM   281  C  CG  . LEU   A 1 59  ? -5.91510  -16.70168 26.54894  1.000 34.85226 ? 58  LEU   A CG  1 
ATOM   282  C  CD1 . LEU   A 1 59  ? -5.88711  -15.34873 27.22085  1.000 35.77315 ? 58  LEU   A CD1 1 
ATOM   283  C  CD2 . LEU   A 1 59  ? -6.07074  -16.56510 25.02830  1.000 28.55779 ? 58  LEU   A CD2 1 
ATOM   284  N  N   . THR   A 1 60  ? -2.76074  -19.60989 28.40698  1.000 24.40383 ? 59  THR   A N   1 
ATOM   285  C  CA  . THR   A 1 60  ? -2.34442  -21.00372 28.51737  1.000 30.12447 ? 59  THR   A CA  1 
ATOM   286  C  C   . THR   A 1 60  ? -2.81919  -21.61945 29.82417  1.000 31.91564 ? 59  THR   A C   1 
ATOM   287  O  O   . THR   A 1 60  ? -3.22391  -22.78483 29.84644  1.000 32.45969 ? 59  THR   A O   1 
ATOM   288  C  CB  . THR   A 1 60  ? -0.82378  -21.11426 28.37613  1.000 32.69821 ? 59  THR   A CB  1 
ATOM   289  O  OG1 . THR   A 1 60  ? -0.44880  -20.65626 27.07933  1.000 32.48639 ? 59  THR   A OG1 1 
ATOM   290  C  CG2 . THR   A 1 60  ? -0.36191  -22.54827 28.54274  1.000 36.46865 ? 59  THR   A CG2 1 
ATOM   291  N  N   . GLN   A 1 61  ? -2.80806  -20.83987 30.91717  1.000 30.34182 ? 60  GLN   A N   1 
ATOM   292  C  CA  . GLN   A 1 61  ? -3.23145  -21.29999 32.23601  1.000 35.15129 ? 60  GLN   A CA  1 
ATOM   293  C  C   . GLN   A 1 61  ? -4.74036  -21.40932 32.39925  1.000 37.48549 ? 60  GLN   A C   1 
ATOM   294  O  O   . GLN   A 1 61  ? -5.19944  -22.11873 33.30073  1.000 37.08474 ? 60  GLN   A O   1 
ATOM   295  C  CB  . GLN   A 1 61  ? -2.71071  -20.35305 33.31178  1.000 36.51849 ? 60  GLN   A CB  1 
ATOM   296  C  CG  . GLN   A 1 61  ? -1.27150  -19.95746 33.13733  1.000 39.53300 ? 60  GLN   A CG  1 
ATOM   297  C  CD  . GLN   A 1 61  ? -0.81755  -19.01742 34.23000  1.000 48.63234 ? 60  GLN   A CD  1 
ATOM   298  O  OE1 . GLN   A 1 61  ? 0.14571   -18.26695 34.05903  1.000 52.69635 ? 60  GLN   A OE1 1 
ATOM   299  N  NE2 . GLN   A 1 61  ? -1.52138  -19.04489 35.36565  1.000 49.56662 ? 60  GLN   A NE2 1 
ATOM   300  N  N   . LEU   A 1 62  ? -5.51172  -20.70129 31.58100  1.000 28.29419 ? 61  LEU   A N   1 
ATOM   301  C  CA  . LEU   A 1 62  ? -6.95985  -20.64734 31.74229  1.000 27.46200 ? 61  LEU   A CA  1 
ATOM   302  C  C   . LEU   A 1 62  ? -7.59486  -22.01447 31.52587  1.000 28.63334 ? 61  LEU   A C   1 
ATOM   303  O  O   . LEU   A 1 62  ? -7.24929  -22.73254 30.58390  1.000 32.81013 ? 61  LEU   A O   1 
ATOM   304  C  CB  . LEU   A 1 62  ? -7.54549  -19.63841 30.75162  1.000 26.73304 ? 61  LEU   A CB  1 
ATOM   305  C  CG  . LEU   A 1 62  ? -9.04916  -19.37592 30.81895  1.000 27.42350 ? 61  LEU   A CG  1 
ATOM   306  C  CD1 . LEU   A 1 62  ? -9.41094  -18.67536 32.13061  1.000 25.55519 ? 61  LEU   A CD1 1 
ATOM   307  C  CD2 . LEU   A 1 62  ? -9.49934  -18.54373 29.58635  1.000 28.97816 ? 61  LEU   A CD2 1 
ATOM   308  N  N   . ARG   A 1 63  ? -8.52486  -22.37689 32.41276  1.000 27.69257 ? 62  ARG   A N   1 
ATOM   309  C  CA  . ARG   A 1 63  ? -9.32634  -23.58916 32.30958  1.000 27.49911 ? 62  ARG   A CA  1 
ATOM   310  C  C   . ARG   A 1 63  ? -10.80525 -23.22062 32.35063  1.000 25.50829 ? 62  ARG   A C   1 
ATOM   311  O  O   . ARG   A 1 63  ? -11.18007 -22.15370 32.84071  1.000 25.81192 ? 62  ARG   A O   1 
ATOM   312  C  CB  . ARG   A 1 63  ? -8.97941  -24.58488 33.44619  1.000 31.28966 ? 62  ARG   A CB  1 
ATOM   313  C  CG  . ARG   A 1 63  ? -7.52435  -25.05830 33.39715  1.000 39.82554 ? 62  ARG   A CG  1 
ATOM   314  C  CD  . ARG   A 1 63  ? -6.90138  -25.49080 34.74130  1.000 52.16611 ? 62  ARG   A CD  1 
ATOM   315  N  NE  . ARG   A 1 63  ? -7.52338  -24.95638 35.94850  1.000 53.79179 ? 62  ARG   A NE  1 
ATOM   316  C  CZ  . ARG   A 1 63  ? -7.23656  -23.77993 36.49314  0.000 46.75708 ? 62  ARG   A CZ  1 
ATOM   317  N  NH1 . ARG   A 1 63  ? -6.41402  -22.92277 35.90376  1.000 51.19159 ? 62  ARG   A NH1 1 
ATOM   318  N  NH2 . ARG   A 1 63  ? -7.78561  -23.45627 37.66247  1.000 52.99167 ? 62  ARG   A NH2 1 
ATOM   319  N  N   . ALA   A 1 64  ? -11.65199 -24.12320 31.85032  1.000 24.18737 ? 63  ALA   A N   1 
ATOM   320  C  CA  . ALA   A 1 64  ? -13.08891 -23.85654 31.84362  1.000 23.47306 ? 63  ALA   A CA  1 
ATOM   321  C  C   . ALA   A 1 64  ? -13.60690 -23.56336 33.24780  1.000 24.49326 ? 63  ALA   A C   1 
ATOM   322  O  O   . ALA   A 1 64  ? -14.47923 -22.70451 33.42047  1.000 23.29642 ? 63  ALA   A O   1 
ATOM   323  C  CB  . ALA   A 1 64  ? -13.85300 -25.03192 31.23531  1.000 27.86978 ? 63  ALA   A CB  1 
ATOM   324  N  N   . GLU   A 1 65  ? -13.07207 -24.25456 34.26821  1.000 26.16046 ? 64  GLU   A N   1 
ATOM   325  C  CA  . GLU   A 1 65  ? -13.55918 -24.02975 35.63067  1.000 26.36554 ? 64  GLU   A CA  1 
ATOM   326  C  C   . GLU   A 1 65  ? -13.26050 -22.62226 36.12464  1.000 26.74955 ? 64  GLU   A C   1 
ATOM   327  O  O   . GLU   A 1 65  ? -13.98265 -22.12580 36.99453  1.000 26.64948 ? 64  GLU   A O   1 
ATOM   328  C  CB  . GLU   A 1 65  ? -12.95582 -25.04655 36.60660  1.000 31.05248 ? 64  GLU   A CB  1 
ATOM   329  C  CG  . GLU   A 1 65  ? -11.42395 -24.99875 36.66272  1.000 33.70954 ? 64  GLU   A CG  1 
ATOM   330  C  CD  . GLU   A 1 65  ? -10.80894 -26.13807 37.46031  1.000 56.15063 ? 64  GLU   A CD  1 
ATOM   331  O  OE1 . GLU   A 1 65  ? -11.12533 -26.26790 38.66211  1.000 51.75972 ? 64  GLU   A OE1 1 
ATOM   332  O  OE2 . GLU   A 1 65  ? -10.00952 -26.90634 36.88236  1.000 59.59109 ? 64  GLU   A OE2 1 
ATOM   333  N  N   . ASP   A 1 66  ? -12.22606 -21.96055 35.58674  1.000 24.81148 ? 65  ASP   A N   1 
ATOM   334  C  CA  . ASP   A 1 66  ? -11.94042 -20.58505 35.98152  1.000 24.06962 ? 65  ASP   A CA  1 
ATOM   335  C  C   . ASP   A 1 66  ? -13.00059 -19.61258 35.49686  1.000 21.05621 ? 65  ASP   A C   1 
ATOM   336  O  O   . ASP   A 1 66  ? -13.01819 -18.46218 35.95859  1.000 24.12584 ? 65  ASP   A O   1 
ATOM   337  C  CB  . ASP   A 1 66  ? -10.57507 -20.13894 35.46188  1.000 23.04424 ? 65  ASP   A CB  1 
ATOM   338  C  CG  . ASP   A 1 66  ? -9.43587  -21.01416 35.95862  1.000 34.03828 ? 65  ASP   A CG  1 
ATOM   339  O  OD1 . ASP   A 1 66  ? -9.39009  -21.31257 37.17264  1.000 38.60668 ? 65  ASP   A OD1 1 
ATOM   340  O  OD2 . ASP   A 1 66  ? -8.57702  -21.38562 35.13590  1.000 33.18359 ? 65  ASP   A OD2 1 
ATOM   341  N  N   . LEU   A 1 67  ? -13.87968 -20.05093 34.58776  1.000 22.30329 ? 66  LEU   A N   1 
ATOM   342  C  CA  . LEU   A 1 67  ? -14.99034 -19.24853 34.09367  1.000 21.78259 ? 66  LEU   A CA  1 
ATOM   343  C  C   . LEU   A 1 67  ? -16.33529 -19.77525 34.57526  1.000 20.80421 ? 66  LEU   A C   1 
ATOM   344  O  O   . LEU   A 1 67  ? -17.38575 -19.29290 34.12167  1.000 21.22162 ? 66  LEU   A O   1 
ATOM   345  C  CB  . LEU   A 1 67  ? -14.96968 -19.19165 32.56009  1.000 19.51547 ? 66  LEU   A CB  1 
ATOM   346  C  CG  . LEU   A 1 67  ? -13.64524 -18.70790 31.95385  1.000 21.09554 ? 66  LEU   A CG  1 
ATOM   347  C  CD1 . LEU   A 1 67  ? -13.71273 -18.75657 30.42721  1.000 21.10198 ? 66  LEU   A CD1 1 
ATOM   348  C  CD2 . LEU   A 1 67  ? -13.28857 -17.30409 32.45005  1.000 22.87111 ? 66  LEU   A CD2 1 
ATOM   349  N  N   . ASN   A 1 68  ? -16.32172 -20.76999 35.45296  1.000 22.03448 ? 67  ASN   A N   1 
ATOM   350  C  CA  . ASN   A 1 68  ? -17.53549 -21.41433 35.93299  1.000 23.20769 ? 67  ASN   A CA  1 
ATOM   351  C  C   . ASN   A 1 68  ? -18.35591 -22.00145 34.79692  1.000 24.57881 ? 67  ASN   A C   1 
ATOM   352  O  O   . ASN   A 1 68  ? -19.58509 -22.03800 34.87898  1.000 24.67770 ? 67  ASN   A O   1 
ATOM   353  C  CB  . ASN   A 1 68  ? -18.38264 -20.44320 36.75249  1.000 19.99062 ? 67  ASN   A CB  1 
ATOM   354  C  CG  . ASN   A 1 68  ? -17.70607 -20.05520 38.05471  1.000 24.26471 ? 67  ASN   A CG  1 
ATOM   355  O  OD1 . ASN   A 1 68  ? -17.27552 -18.91042 38.23318  1.000 25.39948 ? 67  ASN   A OD1 1 
ATOM   356  N  ND2 . ASN   A 1 68  ? -17.61114 -21.00554 38.96891  1.000 25.70429 ? 67  ASN   A ND2 1 
ATOM   357  N  N   . ILE   A 1 69  ? -17.68631 -22.47930 33.75068  1.000 23.00344 ? 68  ILE   A N   1 
ATOM   358  C  CA  . ILE   A 1 69  ? -18.35082 -23.12513 32.62180  1.000 20.73116 ? 68  ILE   A CA  1 
ATOM   359  C  C   . ILE   A 1 69  ? -18.09656 -24.62337 32.72503  1.000 21.84448 ? 68  ILE   A C   1 
ATOM   360  O  O   . ILE   A 1 69  ? -16.95946 -25.08405 32.59350  1.000 26.91995 ? 68  ILE   A O   1 
ATOM   361  C  CB  . ILE   A 1 69  ? -17.85386 -22.56012 31.28726  1.000 21.01977 ? 68  ILE   A CB  1 
ATOM   362  C  CG1 . ILE   A 1 69  ? -18.19961 -21.07301 31.17192  1.000 21.54511 ? 68  ILE   A CG1 1 
ATOM   363  C  CG2 . ILE   A 1 69  ? -18.43627 -23.37450 30.13233  1.000 26.83325 ? 68  ILE   A CG2 1 
ATOM   364  C  CD1 . ILE   A 1 69  ? -17.57141 -20.40490 29.95264  1.000 21.64324 ? 68  ILE   A CD1 1 
ATOM   365  N  N   . ALA   A 1 70  ? -19.14457 -25.38159 32.95462  1.000 24.91126 ? 69  ALA   A N   1 
ATOM   366  C  CA  . ALA   A 1 70  ? -18.98267 -26.82903 32.96929  1.000 29.12138 ? 69  ALA   A CA  1 
ATOM   367  C  C   . ALA   A 1 70  ? -18.86353 -27.35198 31.53846  1.000 24.44939 ? 69  ALA   A C   1 
ATOM   368  O  O   . ALA   A 1 70  ? -19.59995 -26.90215 30.65469  1.000 25.46496 ? 69  ALA   A O   1 
ATOM   369  C  CB  . ALA   A 1 70  ? -20.17610 -27.48769 33.65481  1.000 28.62253 ? 69  ALA   A CB  1 
ATOM   370  N  N   . PRO   A 1 71  ? -17.96245 -28.29454 31.27516  1.000 26.53596 ? 70  PRO   A N   1 
ATOM   371  C  CA  . PRO   A 1 71  ? -17.89708 -28.86465 29.92558  1.000 27.24262 ? 70  PRO   A CA  1 
ATOM   372  C  C   . PRO   A 1 71  ? -19.24690 -29.43341 29.53067  1.000 27.52939 ? 70  PRO   A C   1 
ATOM   373  O  O   . PRO   A 1 71  ? -19.93432 -30.06543 30.33605  1.000 27.44803 ? 70  PRO   A O   1 
ATOM   374  C  CB  . PRO   A 1 71  ? -16.82526 -29.94956 30.04499  1.000 27.15223 ? 70  PRO   A CB  1 
ATOM   375  C  CG  . PRO   A 1 71  ? -15.95077 -29.44947 31.17765  1.000 34.96978 ? 70  PRO   A CG  1 
ATOM   376  C  CD  . PRO   A 1 71  ? -16.91328 -28.83740 32.15696  1.000 30.66977 ? 70  PRO   A CD  1 
ATOM   377  N  N   . ARG   A 1 72  ? -19.64646 -29.15898 28.29159  1.000 24.51339 ? 71  ARG   A N   1 
ATOM   378  C  CA  . ARG   A 1 72  ? -20.91888 -29.62990 27.77131  1.000 25.46715 ? 71  ARG   A CA  1 
ATOM   379  C  C   . ARG   A 1 72  ? -20.69283 -30.86301 26.91299  1.000 23.19852 ? 71  ARG   A C   1 
ATOM   380  O  O   . ARG   A 1 72  ? -19.71943 -30.94077 26.16344  1.000 26.98208 ? 71  ARG   A O   1 
ATOM   381  C  CB  . ARG   A 1 72  ? -21.60472 -28.52994 26.96990  1.000 25.04863 ? 71  ARG   A CB  1 
ATOM   382  C  CG  . ARG   A 1 72  ? -21.91200 -27.32941 27.85871  1.000 23.06762 ? 71  ARG   A CG  1 
ATOM   383  C  CD  . ARG   A 1 72  ? -22.65647 -26.24008 27.12395  1.000 24.41366 ? 71  ARG   A CD  1 
ATOM   384  N  NE  . ARG   A 1 72  ? -22.88025 -25.12689 28.04341  1.000 23.47355 ? 71  ARG   A NE  1 
ATOM   385  C  CZ  . ARG   A 1 72  ? -23.49153 -23.99640 27.72319  1.000 22.80201 ? 71  ARG   A CZ  1 
ATOM   386  N  NH1 . ARG   A 1 72  ? -23.96990 -23.79015 26.50640  1.000 23.20880 ? 71  ARG   A NH1 1 
ATOM   387  N  NH2 . ARG   A 1 72  ? -23.62460 -23.04658 28.64810  1.000 27.01476 ? 71  ARG   A NH2 1 
ATOM   388  N  N   . LYS   A 1 73  ? -21.57675 -31.83977 27.05155  1.000 24.90944 ? 72  LYS   A N   1 
ATOM   389  C  CA  . LYS   A 1 73  ? -21.45362 -33.07905 26.30094  1.000 25.48423 ? 72  LYS   A CA  1 
ATOM   390  C  C   . LYS   A 1 73  ? -22.65133 -33.25131 25.38040  1.000 25.18185 ? 72  LYS   A C   1 
ATOM   391  O  O   . LYS   A 1 73  ? -23.66744 -32.56441 25.49391  1.000 26.92544 ? 72  LYS   A O   1 
ATOM   392  C  CB  . LYS   A 1 73  ? -21.30204 -34.28512 27.24919  1.000 24.68399 ? 72  LYS   A CB  1 
ATOM   393  C  CG  . LYS   A 1 73  ? -20.08798 -34.13137 28.15816  1.000 29.80123 ? 72  LYS   A CG  1 
ATOM   394  C  CD  . LYS   A 1 73  ? -19.84596 -35.35343 29.04389  1.000 32.78143 ? 72  LYS   A CD  1 
ATOM   395  C  CE  . LYS   A 1 73  ? -18.56203 -35.16280 29.84160  1.000 38.23247 ? 72  LYS   A CE  1 
ATOM   396  N  NZ  . LYS   A 1 73  ? -18.32959 -36.23158 30.85943  1.000 36.40282 ? 72  LYS   A NZ  1 
ATOM   397  N  N   . ALA   A 1 74  ? -22.51551 -34.17709 24.43816  1.000 25.28882 ? 73  ALA   A N   1 
ATOM   398  C  CA  . ALA   A 1 74  ? -23.51501 -34.29216 23.39033  1.000 24.93766 ? 73  ALA   A CA  1 
ATOM   399  C  C   . ALA   A 1 74  ? -24.87368 -34.68808 23.96148  1.000 29.49723 ? 73  ALA   A C   1 
ATOM   400  O  O   . ALA   A 1 74  ? -24.97290 -35.38743 24.97522  1.000 33.08076 ? 73  ALA   A O   1 
ATOM   401  C  CB  . ALA   A 1 74  ? -23.07354 -35.31696 22.34559  1.000 32.31207 ? 73  ALA   A CB  1 
ATOM   402  N  N   . THR   A 1 75  ? -25.92754 -34.21741 23.29913  1.000 29.76039 ? 74  THR   A N   1 
ATOM   403  C  CA  . THR   A 1 75  ? -27.28362 -34.64291 23.60651  1.000 32.81521 ? 74  THR   A CA  1 
ATOM   404  C  C   . THR   A 1 75  ? -27.67924 -35.92461 22.88939  1.000 30.91545 ? 74  THR   A C   1 
ATOM   405  O  O   . THR   A 1 75  ? -28.57602 -36.63541 23.36418  1.000 33.06698 ? 74  THR   A O   1 
ATOM   406  C  CB  . THR   A 1 75  ? -28.28778 -33.54498 23.23424  1.000 39.44205 ? 74  THR   A CB  1 
ATOM   407  O  OG1 . THR   A 1 75  ? -28.43822 -33.49030 21.80434  1.000 34.94108 ? 74  THR   A OG1 1 
ATOM   408  C  CG2 . THR   A 1 75  ? -27.85026 -32.18686 23.77856  1.000 37.19689 ? 74  THR   A CG2 1 
ATOM   409  N  N   . LEU   A 1 76  ? -27.03896 -36.22762 21.76694  1.000 28.70796 ? 75  LEU   A N   1 
ATOM   410  C  CA  . LEU   A 1 76  ? -27.40830 -37.32644 20.87719  1.000 27.82708 ? 75  LEU   A CA  1 
ATOM   411  C  C   . LEU   A 1 76  ? -28.78349 -37.13747 20.25601  1.000 31.38917 ? 75  LEU   A C   1 
ATOM   412  O  O   . LEU   A 1 76  ? -29.32098 -38.07761 19.66842  1.000 33.20788 ? 75  LEU   A O   1 
ATOM   413  C  CB  . LEU   A 1 76  ? -27.33913 -38.69105 21.58771  1.000 30.82034 ? 75  LEU   A CB  1 
ATOM   414  C  CG  . LEU   A 1 76  ? -25.98608 -38.95424 22.26278  1.000 33.13802 ? 75  LEU   A CG  1 
ATOM   415  C  CD1 . LEU   A 1 76  ? -25.93699 -40.35629 22.87702  1.000 32.75454 ? 75  LEU   A CD1 1 
ATOM   416  C  CD2 . LEU   A 1 76  ? -24.82649 -38.75085 21.29917  1.000 34.49070 ? 75  LEU   A CD2 1 
ATOM   417  N  N   . GLN   A 1 77  ? -29.37317 -35.94685 20.37650  1.000 32.23029 ? 76  GLN   A N   1 
ATOM   418  C  CA  . GLN   A 1 77  ? -30.62991 -35.63419 19.71723  1.000 35.74119 ? 76  GLN   A CA  1 
ATOM   419  C  C   . GLN   A 1 77  ? -30.40069 -34.64070 18.58223  1.000 32.73916 ? 76  GLN   A C   1 
ATOM   420  O  O   . GLN   A 1 77  ? -29.46701 -33.83320 18.63296  1.000 30.90722 ? 76  GLN   A O   1 
ATOM   421  C  CB  . GLN   A 1 77  ? -31.64663 -35.03713 20.69693  1.000 37.20996 ? 76  GLN   A CB  1 
ATOM   422  C  CG  . GLN   A 1 77  ? -31.80256 -35.80586 22.00435  1.000 38.62639 ? 76  GLN   A CG  1 
ATOM   423  C  CD  . GLN   A 1 77  ? -32.02377 -37.28688 21.78598  1.000 48.30524 ? 76  GLN   A CD  1 
ATOM   424  O  OE1 . GLN   A 1 77  ? -32.74508 -37.69153 20.86941  1.000 51.67580 ? 76  GLN   A OE1 1 
ATOM   425  N  NE2 . GLN   A 1 77  ? -31.36859 -38.11022 22.60363  1.000 37.84674 ? 76  GLN   A NE2 1 
ATOM   426  N  N   . PRO   A 1 78  ? -31.24809 -34.65071 17.55598  1.000 34.97484 ? 77  PRO   A N   1 
ATOM   427  C  CA  . PRO   A 1 78  ? -31.11664 -33.63830 16.50068  1.000 32.36120 ? 77  PRO   A CA  1 
ATOM   428  C  C   . PRO   A 1 78  ? -31.33873 -32.23831 17.06242  1.000 32.22057 ? 77  PRO   A C   1 
ATOM   429  O  O   . PRO   A 1 78  ? -32.04343 -32.04795 18.05526  1.000 35.73539 ? 77  PRO   A O   1 
ATOM   430  C  CB  . PRO   A 1 78  ? -32.20093 -34.01666 15.48225  1.000 36.50161 ? 77  PRO   A CB  1 
ATOM   431  C  CG  . PRO   A 1 78  ? -32.95119 -35.18378 16.04224  1.000 42.59078 ? 77  PRO   A CG  1 
ATOM   432  C  CD  . PRO   A 1 78  ? -32.41671 -35.53542 17.39188  1.000 39.52341 ? 77  PRO   A CD  1 
ATOM   433  N  N   . LEU   A 1 79  ? -30.71759 -31.25711 16.41854  1.000 30.58041 ? 78  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 79  ? -30.88330 -29.86597 16.83075  1.000 29.62011 ? 78  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 79  ? -32.18123 -29.30363 16.24861  1.000 26.87597 ? 78  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 79  ? -32.35716 -29.31087 15.02299  1.000 30.28729 ? 78  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 79  ? -29.69458 -29.03637 16.38514  1.000 30.27439 ? 78  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 79  ? -29.71631 -27.56476 16.78503  1.000 31.44043 ? 78  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 79  ? -29.56685 -27.41648 18.29202  1.000 34.28460 ? 78  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 79  ? -28.63466 -26.80848 16.02999  1.000 33.27356 ? 78  LEU   A CD2 1 
ATOM   441  N  N   . PRO   A 1 80  ? -33.10084 -28.82555 17.07220  1.000 27.21297 ? 79  PRO   A N   1 
ATOM   442  C  CA  . PRO   A 1 80  ? -34.37149 -28.29205 16.54757  1.000 30.72138 ? 79  PRO   A CA  1 
ATOM   443  C  C   . PRO   A 1 80  ? -34.13592 -26.98921 15.80933  1.000 28.65457 ? 79  PRO   A C   1 
ATOM   444  O  O   . PRO   A 1 80  ? -33.17252 -26.26323 16.11686  1.000 26.80617 ? 79  PRO   A O   1 
ATOM   445  C  CB  . PRO   A 1 80  ? -35.21274 -28.06482 17.81132  1.000 32.78777 ? 79  PRO   A CB  1 
ATOM   446  C  CG  . PRO   A 1 80  ? -34.48556 -28.79209 18.91691  1.000 35.04034 ? 79  PRO   A CG  1 
ATOM   447  C  CD  . PRO   A 1 80  ? -33.05335 -28.78924 18.54166  1.000 32.74353 ? 79  PRO   A CD  1 
ATOM   448  N  N   . PRO   A 1 81  ? -35.01838 -26.64574 14.86274  1.000 26.98136 ? 80  PRO   A N   1 
ATOM   449  C  CA  . PRO   A 1 81  ? -34.76862 -25.48293 13.99323  1.000 28.64507 ? 80  PRO   A CA  1 
ATOM   450  C  C   . PRO   A 1 81  ? -34.71150 -24.16218 14.73301  1.000 28.12963 ? 80  PRO   A C   1 
ATOM   451  O  O   . PRO   A 1 81  ? -34.14052 -23.19645 14.19941  1.000 29.79061 ? 80  PRO   A O   1 
ATOM   452  C  CB  . PRO   A 1 81  ? -35.96298 -25.50052 13.02291  1.000 35.76457 ? 80  PRO   A CB  1 
ATOM   453  C  CG  . PRO   A 1 81  ? -36.50987 -26.88283 13.08684  1.000 38.33726 ? 80  PRO   A CG  1 
ATOM   454  C  CD  . PRO   A 1 81  ? -36.23132 -27.38958 14.47667  1.000 30.61151 ? 80  PRO   A CD  1 
ATOM   455  N  N   . ASN   A 1 82  ? -35.30804 -24.07182 15.91474  1.000 27.59541 ? 81  ASN   A N   1 
ATOM   456  C  CA  . ASN   A 1 82  ? -35.37610 -22.80588 16.63774  1.000 25.45954 ? 81  ASN   A CA  1 
ATOM   457  C  C   . ASN   A 1 82  ? -34.17868 -22.58294 17.55254  1.000 29.73227 ? 81  ASN   A C   1 
ATOM   458  O  O   . ASN   A 1 82  ? -34.09514 -21.52644 18.19222  1.000 35.37498 ? 81  ASN   A O   1 
ATOM   459  C  CB  . ASN   A 1 82  ? -36.68328 -22.72912 17.44644  1.000 27.31379 ? 81  ASN   A CB  1 
ATOM   460  C  CG  . ASN   A 1 82  ? -36.76291 -23.78494 18.53172  1.000 31.03605 ? 81  ASN   A CG  1 
ATOM   461  O  OD1 . ASN   A 1 82  ? -36.33523 -24.92272 18.33835  1.000 30.36923 ? 81  ASN   A OD1 1 
ATOM   462  N  ND2 . ASN   A 1 82  ? -37.28801 -23.40482 19.69517  1.000 33.33698 ? 81  ASN   A ND2 1 
ATOM   463  N  N   . LEU   A 1 83  ? -33.24881 -23.53729 17.62550  1.000 25.87713 ? 82  LEU   A N   1 
ATOM   464  C  CA  . LEU   A 1 83  ? -32.08110 -23.36683 18.48614  1.000 23.68612 ? 82  LEU   A CA  1 
ATOM   465  C  C   . LEU   A 1 83  ? -30.83948 -23.04889 17.65864  1.000 21.85640 ? 82  LEU   A C   1 
ATOM   466  O  O   . LEU   A 1 83  ? -30.59553 -23.68765 16.63578  1.000 24.83875 ? 82  LEU   A O   1 
ATOM   467  C  CB  . LEU   A 1 83  ? -31.81987 -24.63849 19.28441  1.000 32.11875 ? 82  LEU   A CB  1 
ATOM   468  C  CG  . LEU   A 1 83  ? -32.91757 -25.08518 20.25753  1.000 41.03531 ? 82  LEU   A CG  1 
ATOM   469  C  CD1 . LEU   A 1 83  ? -32.38116 -26.16113 21.17672  1.000 37.65946 ? 82  LEU   A CD1 1 
ATOM   470  C  CD2 . LEU   A 1 83  ? -33.49405 -23.90788 21.03468  1.000 34.58689 ? 82  LEU   A CD2 1 
ATOM   471  N  N   . PRO   A 1 84  ? -30.01110 -22.10549 18.10830  1.000 23.91610 ? 83  PRO   A N   1 
ATOM   472  C  CA  . PRO   A 1 84  ? -28.81642 -21.76031 17.34379  1.000 24.48527 ? 83  PRO   A CA  1 
ATOM   473  C  C   . PRO   A 1 84  ? -27.77434 -22.85151 17.45332  1.000 22.20262 ? 83  PRO   A C   1 
ATOM   474  O  O   . PRO   A 1 84  ? -27.69902 -23.56082 18.47012  1.000 23.30257 ? 83  PRO   A O   1 
ATOM   475  C  CB  . PRO   A 1 84  ? -28.33362 -20.46033 18.01540  1.000 24.67977 ? 83  PRO   A CB  1 
ATOM   476  C  CG  . PRO   A 1 84  ? -28.80576 -20.60071 19.45159  1.000 24.74501 ? 83  PRO   A CG  1 
ATOM   477  C  CD  . PRO   A 1 84  ? -30.13954 -21.33730 19.36373  1.000 27.11427 ? 83  PRO   A CD  1 
ATOM   478  N  N   . PRO   A 1 85  ? -26.92029 -23.01349 16.44059  1.000 20.47352 ? 84  PRO   A N   1 
ATOM   479  C  CA  . PRO   A 1 85  ? -25.83800 -24.00214 16.54361  1.000 20.08711 ? 84  PRO   A CA  1 
ATOM   480  C  C   . PRO   A 1 85  ? -24.73017 -23.56811 17.49019  1.000 18.76424 ? 84  PRO   A C   1 
ATOM   481  O  O   . PRO   A 1 85  ? -23.99299 -24.42126 17.99234  1.000 20.85161 ? 84  PRO   A O   1 
ATOM   482  C  CB  . PRO   A 1 85  ? -25.32630 -24.10492 15.10070  1.000 25.32179 ? 84  PRO   A CB  1 
ATOM   483  C  CG  . PRO   A 1 85  ? -25.68918 -22.75087 14.47187  1.000 23.73485 ? 84  PRO   A CG  1 
ATOM   484  C  CD  . PRO   A 1 85  ? -27.01186 -22.39287 15.10526  1.000 20.12579 ? 84  PRO   A CD  1 
ATOM   485  N  N   . VAL   A 1 86  ? -24.60229 -22.27171 17.71996  1.000 20.06727 ? 85  VAL   A N   1 
ATOM   486  C  CA  . VAL   A 1 86  ? -23.51271 -21.67405 18.48091  1.000 18.64724 ? 85  VAL   A CA  1 
ATOM   487  C  C   . VAL   A 1 86  ? -24.08136 -20.58725 19.37882  1.000 18.26493 ? 85  VAL   A C   1 
ATOM   488  O  O   . VAL   A 1 86  ? -25.02704 -19.89156 19.00864  1.000 19.58457 ? 85  VAL   A O   1 
ATOM   489  C  CB  . VAL   A 1 86  ? -22.44228 -21.09180 17.53681  1.000 19.77689 ? 85  VAL   A CB  1 
ATOM   490  C  CG1 . VAL   A 1 86  ? -21.27125 -20.53200 18.32589  1.000 20.67154 ? 85  VAL   A CG1 1 
ATOM   491  C  CG2 . VAL   A 1 86  ? -21.93257 -22.16878 16.59130  1.000 21.28229 ? 85  VAL   A CG2 1 
ATOM   492  N  N   . THR   A 1 87  ? -23.51325 -20.43461 20.57468  1.000 18.55647 ? 86  THR   A N   1 
ATOM   493  C  CA  . THR   A 1 87  ? -23.89561 -19.33872 21.45805  1.000 18.24228 ? 86  THR   A CA  1 
ATOM   494  C  C   . THR   A 1 87  ? -22.62239 -18.64231 21.91079  1.000 16.12479 ? 86  THR   A C   1 
ATOM   495  O  O   . THR   A 1 87  ? -21.51563 -19.15914 21.72467  1.000 19.13261 ? 86  THR   A O   1 
ATOM   496  C  CB  . THR   A 1 87  ? -24.70509 -19.80989 22.68560  1.000 19.10610 ? 86  THR   A CB  1 
ATOM   497  O  OG1 . THR   A 1 87  ? -24.00406 -20.87635 23.35217  1.000 21.78009 ? 86  THR   A OG1 1 
ATOM   498  C  CG2 . THR   A 1 87  ? -26.09813 -20.29797 22.26435  1.000 22.72660 ? 86  THR   A CG2 1 
ATOM   499  N  N   . TYR   A 1 88  ? -22.80002 -17.44452 22.45088  1.000 17.79641 ? 87  TYR   A N   1 
ATOM   500  C  CA  . TYR   A 1 88  ? -21.69123 -16.57479 22.82660  1.000 18.89910 ? 87  TYR   A CA  1 
ATOM   501  C  C   . TYR   A 1 88  ? -21.93922 -16.00595 24.21555  1.000 20.18249 ? 87  TYR   A C   1 
ATOM   502  O  O   . TYR   A 1 88  ? -23.03434 -15.49223 24.48529  1.000 20.67969 ? 87  TYR   A O   1 
ATOM   503  C  CB  . TYR   A 1 88  ? -21.52487 -15.44530 21.80708  1.000 20.34427 ? 87  TYR   A CB  1 
ATOM   504  C  CG  . TYR   A 1 88  ? -20.46834 -14.44298 22.18654  1.000 20.36899 ? 87  TYR   A CG  1 
ATOM   505  C  CD1 . TYR   A 1 88  ? -19.11951 -14.72725 22.00357  1.000 19.43431 ? 87  TYR   A CD1 1 
ATOM   506  C  CD2 . TYR   A 1 88  ? -20.81938 -13.20114 22.71532  1.000 20.53010 ? 87  TYR   A CD2 1 
ATOM   507  C  CE1 . TYR   A 1 88  ? -18.13416 -13.80803 22.34666  1.000 18.98782 ? 87  TYR   A CE1 1 
ATOM   508  C  CE2 . TYR   A 1 88  ? -19.84935 -12.27637 23.07771  1.000 17.95998 ? 87  TYR   A CE2 1 
ATOM   509  C  CZ  . TYR   A 1 88  ? -18.50953 -12.58322 22.87349  1.000 19.27380 ? 87  TYR   A CZ  1 
ATOM   510  O  OH  . TYR   A 1 88  ? -17.51095 -11.66753 23.19185  1.000 20.63813 ? 87  TYR   A OH  1 
ATOM   511  N  N   . MET   A 1 89  ? -20.93463 -16.08189 25.09745  1.000 16.95721 ? 88  MET   A N   1 
ATOM   512  C  CA  . MET   A 1 89  ? -20.99268 -15.34199 26.35349  1.000 17.71158 ? 88  MET   A CA  1 
ATOM   513  C  C   . MET   A 1 89  ? -20.03449 -14.16129 26.30624  1.000 19.56871 ? 88  MET   A C   1 
ATOM   514  O  O   . MET   A 1 89  ? -18.84303 -14.32909 26.06246  1.000 20.13630 ? 88  MET   A O   1 
ATOM   515  C  CB  . MET   A 1 89  ? -20.72703 -16.13822 27.62882  1.000 22.81499 ? 88  MET   A CB  1 
ATOM   516  C  CG  . MET   A 1 89  ? -21.44980 -17.46667 27.89058  1.000 21.42353 ? 88  MET   A CG  1 
ATOM   517  S  SD  . MET   A 1 89  ? -20.44559 -18.66590 28.77179  1.000 20.19417 ? 88  MET   A SD  1 
ATOM   518  C  CE  . MET   A 1 89  ? -21.69963 -19.89533 29.10467  1.000 22.09058 ? 88  MET   A CE  1 
ATOM   519  N  N   . HIS   A 1 90  ? -20.55616 -12.96220 26.53711  1.000 17.99685 ? 89  HIS   A N   1 
ATOM   520  C  CA  A HIS   A 1 90  ? -19.74372 -11.75327 26.56026  0.316 18.30565 ? 89  HIS   A CA  1 
ATOM   521  C  CA  B HIS   A 1 90  ? -19.69569 -11.78650 26.54145  0.684 18.12886 ? 89  HIS   A CA  1 
ATOM   522  C  C   . HIS   A 1 90  ? -19.12480 -11.58479 27.93855  1.000 18.73798 ? 89  HIS   A C   1 
ATOM   523  O  O   . HIS   A 1 90  ? -19.84029 -11.65040 28.95073  1.000 22.05261 ? 89  HIS   A O   1 
ATOM   524  C  CB  A HIS   A 1 90  ? -20.62238 -10.54955 26.22889  0.316 23.17047 ? 89  HIS   A CB  1 
ATOM   525  C  CB  B HIS   A 1 90  ? -20.43598 -10.52797 26.07574  0.684 23.22207 ? 89  HIS   A CB  1 
ATOM   526  C  CG  A HIS   A 1 90  ? -20.02487 -9.23336  26.61151  0.316 21.98970 ? 89  HIS   A CG  1 
ATOM   527  C  CG  B HIS   A 1 90  ? -19.52631 -9.40392  25.66753  0.684 19.48601 ? 89  HIS   A CG  1 
ATOM   528  N  ND1 A HIS   A 1 90  ? -18.82855 -8.78088  26.10100  0.316 23.48861 ? 89  HIS   A ND1 1 
ATOM   529  N  ND1 B HIS   A 1 90  ? -18.47290 -9.56256  24.78983  0.684 19.90724 ? 89  HIS   A ND1 1 
ATOM   530  C  CD2 A HIS   A 1 90  ? -20.45876 -8.27224  27.46014  0.316 25.57761 ? 89  HIS   A CD2 1 
ATOM   531  C  CD2 B HIS   A 1 90  ? -19.49617 -8.10553  26.05682  0.684 20.67591 ? 89  HIS   A CD2 1 
ATOM   532  C  CE1 A HIS   A 1 90  ? -18.55805 -7.59022  26.60716  0.316 21.15148 ? 89  HIS   A CE1 1 
ATOM   533  C  CE1 B HIS   A 1 90  ? -17.85335 -8.40239  24.63293  0.684 20.97546 ? 89  HIS   A CE1 1 
ATOM   534  N  NE2 A HIS   A 1 90  ? -19.52918 -7.26143  27.43911  0.316 25.60379 ? 89  HIS   A NE2 1 
ATOM   535  N  NE2 B HIS   A 1 90  ? -18.45694 -7.50095  25.38846  0.684 22.54684 ? 89  HIS   A NE2 1 
ATOM   536  N  N   . ILE   A 1 91  ? -17.81975 -11.36323 27.99399  1.000 18.93805 ? 90  ILE   A N   1 
ATOM   537  C  CA  . ILE   A 1 91  ? -17.13979 -11.10930 29.25757  1.000 19.13185 ? 90  ILE   A CA  1 
ATOM   538  C  C   . ILE   A 1 91  ? -16.78181 -9.63369  29.40561  1.000 20.07907 ? 90  ILE   A C   1 
ATOM   539  O  O   . ILE   A 1 91  ? -17.06192 -9.02677  30.44285  1.000 21.41201 ? 90  ILE   A O   1 
ATOM   540  C  CB  . ILE   A 1 91  ? -15.89660 -12.01400 29.41832  1.000 18.72631 ? 90  ILE   A CB  1 
ATOM   541  C  CG1 . ILE   A 1 91  ? -16.35295 -13.47807 29.50460  1.000 19.14183 ? 90  ILE   A CG1 1 
ATOM   542  C  CG2 . ILE   A 1 91  ? -15.10136 -11.63235 30.67104  1.000 22.25183 ? 90  ILE   A CG2 1 
ATOM   543  C  CD1 . ILE   A 1 91  ? -15.19317 -14.47205 29.57221  1.000 22.09695 ? 90  ILE   A CD1 1 
ATOM   544  N  N   . TYR   A 1 92  ? -16.15080 -9.03890  28.38905  1.000 20.52980 ? 91  TYR   A N   1 
ATOM   545  C  CA  . TYR   A 1 92  ? -15.81825 -7.61314  28.48311  1.000 20.22478 ? 91  TYR   A CA  1 
ATOM   546  C  C   . TYR   A 1 92  ? -15.44693 -7.08842  27.10377  1.000 19.98227 ? 91  TYR   A C   1 
ATOM   547  O  O   . TYR   A 1 92  ? -15.01749 -7.84569  26.23463  1.000 21.92193 ? 91  TYR   A O   1 
ATOM   548  C  CB  . TYR   A 1 92  ? -14.64682 -7.36277  29.44073  1.000 20.63637 ? 91  TYR   A CB  1 
ATOM   549  C  CG  . TYR   A 1 92  ? -14.73336 -6.01317  30.11345  1.000 22.88221 ? 91  TYR   A CG  1 
ATOM   550  C  CD1 . TYR   A 1 92  ? -15.66342 -5.79725  31.11596  1.000 26.31298 ? 91  TYR   A CD1 1 
ATOM   551  C  CD2 . TYR   A 1 92  ? -13.94160 -4.95620  29.70592  1.000 26.32846 ? 91  TYR   A CD2 1 
ATOM   552  C  CE1 . TYR   A 1 92  ? -15.78080 -4.57617  31.73173  1.000 30.26312 ? 91  TYR   A CE1 1 
ATOM   553  C  CE2 . TYR   A 1 92  ? -14.04848 -3.71161  30.32817  1.000 26.57660 ? 91  TYR   A CE2 1 
ATOM   554  C  CZ  . TYR   A 1 92  ? -14.97825 -3.53307  31.32923  1.000 29.66643 ? 91  TYR   A CZ  1 
ATOM   555  O  OH  . TYR   A 1 92  ? -15.10710 -2.30679  31.94913  1.000 32.64458 ? 91  TYR   A OH  1 
ATOM   556  N  N   . GLU   A 1 93  ? -15.57619 -5.77487  26.92313  1.000 22.60601 ? 92  GLU   A N   1 
ATOM   557  C  CA  . GLU   A 1 93  ? -14.96550 -5.15217  25.75663  1.000 23.11242 ? 92  GLU   A CA  1 
ATOM   558  C  C   . GLU   A 1 93  ? -14.57258 -3.72255  26.08820  1.000 26.76811 ? 92  GLU   A C   1 
ATOM   559  O  O   . GLU   A 1 93  ? -15.20878 -3.05010  26.91077  1.000 28.39689 ? 92  GLU   A O   1 
ATOM   560  C  CB  . GLU   A 1 93  ? -15.88216 -5.18600  24.52364  1.000 27.19639 ? 92  GLU   A CB  1 
ATOM   561  C  CG  . GLU   A 1 93  ? -16.56975 -3.86074  24.22554  1.000 33.01352 ? 92  GLU   A CG  1 
ATOM   562  C  CD  . GLU   A 1 93  ? -17.75650 -3.65944  25.14278  0.438 24.50389 ? 92  GLU   A CD  1 
ATOM   563  O  OE1 . GLU   A 1 93  ? -18.20394 -4.66555  25.72808  0.600 25.24403 ? 92  GLU   A OE1 1 
ATOM   564  O  OE2 . GLU   A 1 93  ? -18.23312 -2.51662  25.29176  0.790 29.59474 ? 92  GLU   A OE2 1 
ATOM   565  N  N   . THR   A 1 94  ? -13.49371 -3.28082  25.45360  1.000 24.46879 ? 93  THR   A N   1 
ATOM   566  C  CA  . THR   A 1 94  ? -13.03965 -1.89594  25.47356  1.000 24.41278 ? 93  THR   A CA  1 
ATOM   567  C  C   . THR   A 1 94  ? -12.93041 -1.42820  24.02629  1.000 26.59725 ? 93  THR   A C   1 
ATOM   568  O  O   . THR   A 1 94  ? -13.31423 -2.13368  23.09155  1.000 29.15503 ? 93  THR   A O   1 
ATOM   569  C  CB  . THR   A 1 94  ? -11.69659 -1.74603  26.19629  1.000 30.40777 ? 93  THR   A CB  1 
ATOM   570  O  OG1 . THR   A 1 94  ? -10.66237 -2.32870  25.38868  1.000 30.27372 ? 93  THR   A OG1 1 
ATOM   571  C  CG2 . THR   A 1 94  ? -11.69963 -2.37822  27.57392  1.000 30.65382 ? 93  THR   A CG2 1 
ATOM   572  N  N   . ASP   A 1 95  ? -12.39770 -0.21558  23.82526  1.000 30.27391 ? 94  ASP   A N   1 
ATOM   573  C  CA  . ASP   A 1 95  ? -12.11711 0.20496   22.46147  1.000 31.71822 ? 94  ASP   A CA  1 
ATOM   574  C  C   . ASP   A 1 95  ? -10.99979 -0.63023  21.84381  1.000 33.36802 ? 94  ASP   A C   1 
ATOM   575  O  O   . ASP   A 1 95  ? -10.89065 -0.70107  20.61733  1.000 36.33163 ? 94  ASP   A O   1 
ATOM   576  C  CB  . ASP   A 1 95  ? -11.72337 1.68350   22.44959  1.000 38.18813 ? 94  ASP   A CB  1 
ATOM   577  C  CG  . ASP   A 1 95  ? -12.90150 2.59454   22.18938  0.390 39.64591 ? 94  ASP   A CG  1 
ATOM   578  O  OD1 . ASP   A 1 95  ? -14.00086 2.09538   21.86790  0.590 38.24061 ? 94  ASP   A OD1 1 
ATOM   579  O  OD2 . ASP   A 1 95  ? -12.71810 3.82090   22.31161  0.578 40.17299 ? 94  ASP   A OD2 1 
ATOM   580  N  N   . GLY   A 1 96  ? -10.17010 -1.25239  22.67422  1.000 28.37530 ? 95  GLY   A N   1 
ATOM   581  C  CA  . GLY   A 1 96  ? -9.01177  -1.97065  22.20388  1.000 27.05802 ? 95  GLY   A CA  1 
ATOM   582  C  C   . GLY   A 1 96  ? -9.22754  -3.45144  21.95518  1.000 28.14146 ? 95  GLY   A C   1 
ATOM   583  O  O   . GLY   A 1 96  ? -8.50724  -4.03081  21.14439  1.000 24.98967 ? 95  GLY   A O   1 
ATOM   584  N  N   . PHE   A 1 97  ? -10.17736 -4.08624  22.64041  1.000 24.23805 ? 96  PHE   A N   1 
ATOM   585  C  CA  . PHE   A 1 97  ? -10.34655 -5.52913  22.48940  1.000 22.23744 ? 96  PHE   A CA  1 
ATOM   586  C  C   . PHE   A 1 97  ? -11.72395 -5.95523  22.96525  1.000 23.35823 ? 96  PHE   A C   1 
ATOM   587  O  O   . PHE   A 1 97  ? -12.37300 -5.26807  23.76389  1.000 23.38496 ? 96  PHE   A O   1 
ATOM   588  C  CB  . PHE   A 1 97  ? -9.27490  -6.29918  23.27484  1.000 23.60262 ? 96  PHE   A CB  1 
ATOM   589  C  CG  . PHE   A 1 97  ? -9.50102  -6.27293  24.76373  1.000 22.16100 ? 96  PHE   A CG  1 
ATOM   590  C  CD1 . PHE   A 1 97  ? -9.02876  -5.21067  25.50341  1.000 26.15382 ? 96  PHE   A CD1 1 
ATOM   591  C  CD2 . PHE   A 1 97  ? -10.20570 -7.27924  25.40623  1.000 24.27014 ? 96  PHE   A CD2 1 
ATOM   592  C  CE1 . PHE   A 1 97  ? -9.23748  -5.14835  26.87501  1.000 28.80135 ? 96  PHE   A CE1 1 
ATOM   593  C  CE2 . PHE   A 1 97  ? -10.42280 -7.22669  26.78250  1.000 26.11414 ? 96  PHE   A CE2 1 
ATOM   594  C  CZ  . PHE   A 1 97  ? -9.93454  -6.14341  27.51104  1.000 26.63642 ? 96  PHE   A CZ  1 
ATOM   595  N  N   . SER   A 1 98  ? -12.13921 -7.12329  22.48387  1.000 21.92786 ? 97  SER   A N   1 
ATOM   596  C  CA  A SER   A 1 98  ? -13.33549 -7.80057  22.96121  0.328 20.65506 ? 97  SER   A CA  1 
ATOM   597  C  CA  B SER   A 1 98  ? -13.33901 -7.80629  22.94290  0.672 20.61413 ? 97  SER   A CA  1 
ATOM   598  C  C   . SER   A 1 98  ? -12.94532 -9.16832  23.50243  1.000 21.88258 ? 97  SER   A C   1 
ATOM   599  O  O   . SER   A 1 98  ? -12.03167 -9.80808  22.98364  1.000 22.16989 ? 97  SER   A O   1 
ATOM   600  C  CB  A SER   A 1 98  ? -14.36816 -7.96057  21.84316  0.328 24.42006 ? 97  SER   A CB  1 
ATOM   601  C  CB  B SER   A 1 98  ? -14.33417 -7.95745  21.78773  0.672 24.45003 ? 97  SER   A CB  1 
ATOM   602  O  OG  A SER   A 1 98  ? -14.01290 -9.03471  20.99284  0.328 23.04174 ? 97  SER   A OG  1 
ATOM   603  O  OG  B SER   A 1 98  ? -15.52962 -8.55850  22.23449  0.672 23.79789 ? 97  SER   A OG  1 
ATOM   604  N  N   . LEU   A 1 99  ? -13.65321 -9.61679  24.54776  1.000 19.83830 ? 98  LEU   A N   1 
ATOM   605  C  CA  . LEU   A 1 99  ? -13.32216 -10.83866 25.28062  1.000 19.91046 ? 98  LEU   A CA  1 
ATOM   606  C  C   . LEU   A 1 99  ? -14.59415 -11.63911 25.54965  1.000 18.41589 ? 98  LEU   A C   1 
ATOM   607  O  O   . LEU   A 1 99  ? -15.50988 -11.13776 26.20942  1.000 19.23982 ? 98  LEU   A O   1 
ATOM   608  C  CB  . LEU   A 1 99  ? -12.62354 -10.45384 26.59990  1.000 21.21201 ? 98  LEU   A CB  1 
ATOM   609  C  CG  . LEU   A 1 99  ? -12.30474 -11.51309 27.64574  1.000 20.69672 ? 98  LEU   A CG  1 
ATOM   610  C  CD1 . LEU   A 1 99  ? -11.22151 -12.46817 27.12247  1.000 22.46178 ? 98  LEU   A CD1 1 
ATOM   611  C  CD2 . LEU   A 1 99  ? -11.83047 -10.84571 28.95788  1.000 20.98424 ? 98  LEU   A CD2 1 
ATOM   612  N  N   . GLY   A 1 100 ? -14.64623 -12.88927 25.09787  1.000 17.00991 ? 99  GLY   A N   1 
ATOM   613  C  CA  . GLY   A 1 100 ? -15.83846 -13.69390 25.35124  1.000 17.68928 ? 99  GLY   A CA  1 
ATOM   614  C  C   . GLY   A 1 100 ? -15.59490 -15.15677 25.02680  1.000 18.71262 ? 99  GLY   A C   1 
ATOM   615  O  O   . GLY   A 1 100 ? -14.47170 -15.56306 24.73860  1.000 19.92710 ? 99  GLY   A O   1 
ATOM   616  N  N   . VAL   A 1 101 ? -16.66898 -15.95050 25.07593  1.000 16.72477 ? 100 VAL   A N   1 
ATOM   617  C  CA  . VAL   A 1 101 ? -16.58443 -17.39936 24.89106  1.000 15.75523 ? 100 VAL   A CA  1 
ATOM   618  C  C   . VAL   A 1 101 ? -17.59239 -17.79664 23.82748  1.000 17.98810 ? 100 VAL   A C   1 
ATOM   619  O  O   . VAL   A 1 101 ? -18.75573 -17.39234 23.89827  1.000 18.80461 ? 100 VAL   A O   1 
ATOM   620  C  CB  . VAL   A 1 101 ? -16.88298 -18.17817 26.18517  1.000 16.74702 ? 100 VAL   A CB  1 
ATOM   621  C  CG1 . VAL   A 1 101 ? -16.87723 -19.69036 25.89369  1.000 20.59620 ? 100 VAL   A CG1 1 
ATOM   622  C  CG2 . VAL   A 1 101 ? -15.86992 -17.83143 27.25733  1.000 19.55450 ? 100 VAL   A CG2 1 
ATOM   623  N  N   . PHE   A 1 102 ? -17.15616 -18.60263 22.86243  1.000 16.53751 ? 101 PHE   A N   1 
ATOM   624  C  CA  . PHE   A 1 102 ? -18.07570 -19.23064 21.91449  1.000 18.03010 ? 101 PHE   A CA  1 
ATOM   625  C  C   . PHE   A 1 102 ? -18.28571 -20.68122 22.29059  1.000 19.34047 ? 101 PHE   A C   1 
ATOM   626  O  O   . PHE   A 1 102 ? -17.32389 -21.40014 22.57762  1.000 17.36342 ? 101 PHE   A O   1 
ATOM   627  C  CB  . PHE   A 1 102 ? -17.55421 -19.16178 20.47354  1.000 15.82895 ? 101 PHE   A CB  1 
ATOM   628  C  CG  . PHE   A 1 102 ? -17.57213 -17.77756 19.90237  1.000 17.48845 ? 101 PHE   A CG  1 
ATOM   629  C  CD1 . PHE   A 1 102 ? -16.52020 -16.91084 20.13346  1.000 17.38196 ? 101 PHE   A CD1 1 
ATOM   630  C  CD2 . PHE   A 1 102 ? -18.65636 -17.34587 19.13750  1.000 20.34442 ? 101 PHE   A CD2 1 
ATOM   631  C  CE1 . PHE   A 1 102 ? -16.52951 -15.61988 19.62715  1.000 20.45505 ? 101 PHE   A CE1 1 
ATOM   632  C  CE2 . PHE   A 1 102 ? -18.67512 -16.04794 18.61411  1.000 20.51422 ? 101 PHE   A CE2 1 
ATOM   633  C  CZ  . PHE   A 1 102 ? -17.61590 -15.18243 18.87280  1.000 21.11152 ? 101 PHE   A CZ  1 
ATOM   634  N  N   . LEU   A 1 103 ? -19.54012 -21.12465 22.24183  1.000 16.93446 ? 102 LEU   A N   1 
ATOM   635  C  CA  . LEU   A 1 103 ? -19.91043 -22.47489 22.64611  1.000 17.34172 ? 102 LEU   A CA  1 
ATOM   636  C  C   . LEU   A 1 103 ? -20.59618 -23.16275 21.46556  1.000 18.48604 ? 102 LEU   A C   1 
ATOM   637  O  O   . LEU   A 1 103 ? -21.69370 -22.76804 21.05870  1.000 19.03109 ? 102 LEU   A O   1 
ATOM   638  C  CB  . LEU   A 1 103 ? -20.78680 -22.44703 23.90795  1.000 18.04218 ? 102 LEU   A CB  1 
ATOM   639  C  CG  . LEU   A 1 103 ? -20.14343 -21.70909 25.10018  1.000 18.89707 ? 102 LEU   A CG  1 
ATOM   640  C  CD1 . LEU   A 1 103 ? -20.62365 -20.23860 25.19301  1.000 18.14942 ? 102 LEU   A CD1 1 
ATOM   641  C  CD2 . LEU   A 1 103 ? -20.40785 -22.44734 26.42066  1.000 20.56262 ? 102 LEU   A CD2 1 
ATOM   642  N  N   . LEU   A 1 104 ? -19.94764 -24.19503 20.93192  1.000 17.32139 ? 103 LEU   A N   1 
ATOM   643  C  CA  . LEU   A 1 104 ? -20.40615 -24.89306 19.72824  1.000 18.50341 ? 103 LEU   A CA  1 
ATOM   644  C  C   . LEU   A 1 104 ? -21.12397 -26.17906 20.12317  1.000 19.69561 ? 103 LEU   A C   1 
ATOM   645  O  O   . LEU   A 1 104 ? -20.58204 -26.98589 20.88934  1.000 19.44909 ? 103 LEU   A O   1 
ATOM   646  C  CB  . LEU   A 1 104 ? -19.22778 -25.25416 18.81409  1.000 18.98540 ? 103 LEU   A CB  1 
ATOM   647  C  CG  . LEU   A 1 104 ? -18.61196 -24.14308 17.96224  1.000 17.93994 ? 103 LEU   A CG  1 
ATOM   648  C  CD1 . LEU   A 1 104 ? -17.90197 -23.14727 18.86165  1.000 23.89234 ? 103 LEU   A CD1 1 
ATOM   649  C  CD2 . LEU   A 1 104 ? -17.63162 -24.73517 16.92818  1.000 20.79689 ? 103 LEU   A CD2 1 
ATOM   650  N  N   . LYS   A 1 105 ? -22.31236 -26.39459 19.56685  1.000 18.51394 ? 104 LYS   A N   1 
ATOM   651  C  CA  . LYS   A 1 105 ? -22.98523 -27.66043 19.82134  1.000 19.64583 ? 104 LYS   A CA  1 
ATOM   652  C  C   . LYS   A 1 105 ? -22.38873 -28.76854 18.94163  1.000 23.55759 ? 104 LYS   A C   1 
ATOM   653  O  O   . LYS   A 1 105 ? -21.58578 -28.51625 18.03632  1.000 20.94236 ? 104 LYS   A O   1 
ATOM   654  C  CB  . LYS   A 1 105 ? -24.49050 -27.48964 19.60986  1.000 20.79893 ? 104 LYS   A CB  1 
ATOM   655  C  CG  . LYS   A 1 105 ? -25.11297 -26.45529 20.54912  1.000 22.02711 ? 104 LYS   A CG  1 
ATOM   656  C  CD  . LYS   A 1 105 ? -26.60103 -26.27613 20.26463  1.000 25.05521 ? 104 LYS   A CD  1 
ATOM   657  C  CE  . LYS   A 1 105 ? -27.23973 -25.39501 21.31201  1.000 25.31617 ? 104 LYS   A CE  1 
ATOM   658  N  NZ  . LYS   A 1 105 ? -26.86373 -23.96209 21.19881  1.000 25.77415 ? 104 LYS   A NZ  1 
ATOM   659  N  N   . SER   A 1 106 ? -22.73591 -30.03191 19.24943  1.000 24.65885 ? 105 SER   A N   1 
ATOM   660  C  CA  . SER   A 1 106 ? -22.18241 -31.15258 18.48406  1.000 24.41738 ? 105 SER   A CA  1 
ATOM   661  C  C   . SER   A 1 106 ? -22.44470 -30.98162 16.99830  1.000 21.46364 ? 105 SER   A C   1 
ATOM   662  O  O   . SER   A 1 106 ? -23.54552 -30.60131 16.58385  1.000 25.93602 ? 105 SER   A O   1 
ATOM   663  C  CB  . SER   A 1 106 ? -22.77322 -32.51180 18.91474  1.000 25.59895 ? 105 SER   A CB  1 
ATOM   664  O  OG  . SER   A 1 106 ? -22.78623 -32.67477 20.30480  1.000 36.20354 ? 105 SER   A OG  1 
ATOM   665  N  N   . GLY   A 1 107 ? -21.43652 -31.31837 16.19553  1.000 25.68875 ? 106 GLY   A N   1 
ATOM   666  C  CA  . GLY   A 1 107 ? -21.59822 -31.33345 14.75785  1.000 27.41651 ? 106 GLY   A CA  1 
ATOM   667  C  C   . GLY   A 1 107 ? -21.71887 -29.98091 14.10646  1.000 29.26994 ? 106 GLY   A C   1 
ATOM   668  O  O   . GLY   A 1 107 ? -22.03989 -29.91235 12.91436  1.000 30.02618 ? 106 GLY   A O   1 
ATOM   669  N  N   . THR   A 1 108 ? -21.46120 -28.90190 14.83578  1.000 23.12998 ? 107 THR   A N   1 
ATOM   670  C  CA  . THR   A 1 108 ? -21.59077 -27.56770 14.27842  1.000 20.75977 ? 107 THR   A CA  1 
ATOM   671  C  C   . THR   A 1 108 ? -20.22383 -27.01561 13.91761  1.000 22.54638 ? 107 THR   A C   1 
ATOM   672  O  O   . THR   A 1 108 ? -19.18018 -27.50197 14.36405  1.000 23.07578 ? 107 THR   A O   1 
ATOM   673  C  CB  . THR   A 1 108 ? -22.29122 -26.59903 15.24625  1.000 20.81818 ? 107 THR   A CB  1 
ATOM   674  O  OG1 . THR   A 1 108 ? -21.47470 -26.36151 16.40669  1.000 22.15606 ? 107 THR   A OG1 1 
ATOM   675  C  CG2 . THR   A 1 108 ? -23.64396 -27.13789 15.67848  1.000 25.84246 ? 107 THR   A CG2 1 
ATOM   676  N  N   . SER   A 1 109 ? -20.26327 -25.97686 13.09562  1.000 23.81965 ? 108 SER   A N   1 
ATOM   677  C  CA  A SER   A 1 109 ? -19.07335 -25.25181 12.69766  0.469 22.49141 ? 108 SER   A CA  1 
ATOM   678  C  CA  B SER   A 1 109 ? -19.07820 -25.24744 12.67820  0.531 22.48430 ? 108 SER   A CA  1 
ATOM   679  C  C   . SER   A 1 109 ? -19.38422 -23.76523 12.73202  1.000 25.38066 ? 108 SER   A C   1 
ATOM   680  O  O   . SER   A 1 109 ? -20.52219 -23.34507 12.50668  1.000 24.08504 ? 108 SER   A O   1 
ATOM   681  C  CB  A SER   A 1 109 ? -18.61818 -25.70476 11.29951  0.469 27.21393 ? 108 SER   A CB  1 
ATOM   682  C  CB  B SER   A 1 109 ? -18.65644 -25.61719 11.25185  0.531 27.19349 ? 108 SER   A CB  1 
ATOM   683  O  OG  A SER   A 1 109 ? -17.97957 -24.67053 10.58415  0.469 33.19936 ? 108 SER   A OG  1 
ATOM   684  O  OG  B SER   A 1 109 ? -18.24459 -26.96441 11.18430  0.531 26.37335 ? 108 SER   A OG  1 
ATOM   685  N  N   . ILE   A 1 110 ? -18.36893 -22.97080 13.05101  1.000 19.41590 ? 109 ILE   A N   1 
ATOM   686  C  CA  . ILE   A 1 110 ? -18.36799 -21.55053 12.72805  1.000 19.57439 ? 109 ILE   A CA  1 
ATOM   687  C  C   . ILE   A 1 110 ? -17.74521 -21.42515 11.33924  1.000 19.88500 ? 109 ILE   A C   1 
ATOM   688  O  O   . ILE   A 1 110 ? -16.56612 -21.76719 11.17643  1.000 20.32098 ? 109 ILE   A O   1 
ATOM   689  C  CB  . ILE   A 1 110 ? -17.58408 -20.72685 13.74821  1.000 17.99687 ? 109 ILE   A CB  1 
ATOM   690  C  CG1 . ILE   A 1 110 ? -18.24679 -20.81972 15.12615  1.000 21.52109 ? 109 ILE   A CG1 1 
ATOM   691  C  CG2 . ILE   A 1 110 ? -17.59529 -19.24666 13.31444  1.000 20.82887 ? 109 ILE   A CG2 1 
ATOM   692  C  CD1 . ILE   A 1 110 ? -17.40439 -20.13425 16.18263  1.000 20.30555 ? 109 ILE   A CD1 1 
ATOM   693  N  N   . PRO   A 1 111 ? -18.48646 -20.99965 10.33413  1.000 21.83085 ? 110 PRO   A N   1 
ATOM   694  C  CA  . PRO   A 1 111 ? -17.95604 -20.99197 8.97054   1.000 22.43108 ? 110 PRO   A CA  1 
ATOM   695  C  C   . PRO   A 1 111 ? -16.77911 -20.04486 8.78755   1.000 21.55285 ? 110 PRO   A C   1 
ATOM   696  O  O   . PRO   A 1 111 ? -16.61109 -19.05071 9.49314   1.000 20.47406 ? 110 PRO   A O   1 
ATOM   697  C  CB  . PRO   A 1 111 ? -19.16078 -20.53855 8.13664   1.000 23.40013 ? 110 PRO   A CB  1 
ATOM   698  C  CG  . PRO   A 1 111 ? -20.34481 -20.92814 8.98061   1.000 27.47324 ? 110 PRO   A CG  1 
ATOM   699  C  CD  . PRO   A 1 111 ? -19.89800 -20.59484 10.37640  1.000 23.16815 ? 110 PRO   A CD  1 
ATOM   700  N  N   . LEU   A 1 112 ? -15.98506 -20.36028 7.76903   1.000 22.36568 ? 111 LEU   A N   1 
ATOM   701  C  CA  . LEU   A 1 112 ? -14.82828 -19.57668 7.35157   1.000 22.77860 ? 111 LEU   A CA  1 
ATOM   702  C  C   . LEU   A 1 112 ? -15.12735 -18.08062 7.31979   1.000 21.35541 ? 111 LEU   A C   1 
ATOM   703  O  O   . LEU   A 1 112 ? -16.05512 -17.63273 6.63254   1.000 21.65036 ? 111 LEU   A O   1 
ATOM   704  C  CB  . LEU   A 1 112 ? -14.39810 -20.06807 5.96652   1.000 21.80320 ? 111 LEU   A CB  1 
ATOM   705  C  CG  . LEU   A 1 112 ? -13.09974 -19.48468 5.43592   1.000 22.88892 ? 111 LEU   A CG  1 
ATOM   706  C  CD1 . LEU   A 1 112 ? -11.95130 -19.79567 6.36668   1.000 23.74320 ? 111 LEU   A CD1 1 
ATOM   707  C  CD2 . LEU   A 1 112 ? -12.82682 -20.09274 4.06174   1.000 24.74720 ? 111 LEU   A CD2 1 
ATOM   708  N  N   . HIS   A 1 113 ? -14.33831 -17.29576 8.06111   1.000 20.41982 ? 112 HIS   A N   1 
ATOM   709  C  CA  . HIS   A 1 113 ? -14.57627 -15.85266 8.15506   1.000 23.58266 ? 112 HIS   A CA  1 
ATOM   710  C  C   . HIS   A 1 113 ? -13.27013 -15.11123 8.41299   1.000 22.34749 ? 112 HIS   A C   1 
ATOM   711  O  O   . HIS   A 1 113 ? -12.27582 -15.70050 8.84571   1.000 20.83806 ? 112 HIS   A O   1 
ATOM   712  C  CB  . HIS   A 1 113 ? -15.58234 -15.50478 9.27085   1.000 19.94823 ? 112 HIS   A CB  1 
ATOM   713  C  CG  . HIS   A 1 113 ? -15.11957 -15.89367 10.64216  1.000 19.73796 ? 112 HIS   A CG  1 
ATOM   714  N  ND1 . HIS   A 1 113 ? -15.33868 -17.14493 11.17369  1.000 20.69638 ? 112 HIS   A ND1 1 
ATOM   715  C  CD2 . HIS   A 1 113 ? -14.42410 -15.20152 11.57235  1.000 18.08489 ? 112 HIS   A CD2 1 
ATOM   716  C  CE1 . HIS   A 1 113 ? -14.80208 -17.20513 12.38176  1.000 17.84220 ? 112 HIS   A CE1 1 
ATOM   717  N  NE2 . HIS   A 1 113 ? -14.25119 -16.03579 12.65443  1.000 19.02490 ? 112 HIS   A NE2 1 
ATOM   718  N  N   . ASP   A 1 114 ? -13.27721 -13.79729 8.13524   1.000 21.98839 ? 113 ASP   A N   1 
ATOM   719  C  CA  . ASP   A 1 114 ? -12.09000 -12.96628 8.28901   1.000 22.20864 ? 113 ASP   A CA  1 
ATOM   720  C  C   . ASP   A 1 114 ? -12.19847 -12.04472 9.50575   1.000 23.25802 ? 113 ASP   A C   1 
ATOM   721  O  O   . ASP   A 1 114 ? -13.18950 -12.04063 10.24088  1.000 23.16014 ? 113 ASP   A O   1 
ATOM   722  C  CB  . ASP   A 1 114 ? -11.78973 -12.16740 7.01040   1.000 22.78260 ? 113 ASP   A CB  1 
ATOM   723  C  CG  . ASP   A 1 114 ? -12.86124 -11.13222 6.65392   1.000 27.58126 ? 113 ASP   A CG  1 
ATOM   724  O  OD1 . ASP   A 1 114 ? -13.80587 -10.89674 7.43471   1.000 26.42001 ? 113 ASP   A OD1 1 
ATOM   725  O  OD2 . ASP   A 1 114 ? -12.73004 -10.54742 5.55290   1.000 32.27870 ? 113 ASP   A OD2 1 
ATOM   726  N  N   . HIS   A 1 115 ? -11.12181 -11.29201 9.73234   1.000 21.89734 ? 114 HIS   A N   1 
ATOM   727  C  CA  . HIS   A 1 115 ? -10.99225 -10.38998 10.87444  1.000 21.24563 ? 114 HIS   A CA  1 
ATOM   728  C  C   . HIS   A 1 115 ? -10.24772 -9.15362  10.38785  1.000 22.21554 ? 114 HIS   A C   1 
ATOM   729  O  O   . HIS   A 1 115 ? -9.07911  -8.94290  10.70862  1.000 24.52851 ? 114 HIS   A O   1 
ATOM   730  C  CB  . HIS   A 1 115 ? -10.26429 -11.08489 12.03408  1.000 21.28579 ? 114 HIS   A CB  1 
ATOM   731  C  CG  . HIS   A 1 115 ? -10.78556 -12.46513 12.34732  1.000 21.81018 ? 114 HIS   A CG  1 
ATOM   732  N  ND1 . HIS   A 1 115 ? -10.47012 -13.57660 11.58663  1.000 21.73435 ? 114 HIS   A ND1 1 
ATOM   733  C  CD2 . HIS   A 1 115 ? -11.61198 -12.90871 13.32857  1.000 23.38677 ? 114 HIS   A CD2 1 
ATOM   734  C  CE1 . HIS   A 1 115 ? -11.06930 -14.64126 12.09358  1.000 20.14754 ? 114 HIS   A CE1 1 
ATOM   735  N  NE2 . HIS   A 1 115 ? -11.77197 -14.26113 13.14923  1.000 19.94990 ? 114 HIS   A NE2 1 
ATOM   736  N  N   . PRO   A 1 116 ? -10.90465 -8.31274  9.59202   1.000 23.03826 ? 115 PRO   A N   1 
ATOM   737  C  CA  . PRO   A 1 116 ? -10.17705 -7.26637  8.85293   1.000 26.34455 ? 115 PRO   A CA  1 
ATOM   738  C  C   . PRO   A 1 116 ? -9.46509  -6.30824  9.79265   1.000 25.84299 ? 115 PRO   A C   1 
ATOM   739  O  O   . PRO   A 1 116 ? -10.08317 -5.66967  10.64831  1.000 28.39119 ? 115 PRO   A O   1 
ATOM   740  C  CB  . PRO   A 1 116 ? -11.28500 -6.55949  8.05655   1.000 27.84733 ? 115 PRO   A CB  1 
ATOM   741  C  CG  . PRO   A 1 116 ? -12.38099 -7.55536  7.96384   1.000 27.82507 ? 115 PRO   A CG  1 
ATOM   742  C  CD  . PRO   A 1 116 ? -12.33768 -8.32697  9.26966   1.000 24.96144 ? 115 PRO   A CD  1 
ATOM   743  N  N   . GLY   A 1 117 ? -8.15584  -6.19338  9.60846   1.000 27.33054 ? 116 GLY   A N   1 
ATOM   744  C  CA  . GLY   A 1 117 ? -7.39000  -5.26462  10.40810  1.000 31.17176 ? 116 GLY   A CA  1 
ATOM   745  C  C   . GLY   A 1 117 ? -7.28274  -5.63794  11.86432  1.000 29.69604 ? 116 GLY   A C   1 
ATOM   746  O  O   . GLY   A 1 117 ? -6.94007  -4.79050  12.68418  1.000 30.43739 ? 116 GLY   A O   1 
ATOM   747  N  N   . MET   A 1 118 ? -7.54435  -6.89014  12.21314  1.000 24.08905 ? 117 MET   A N   1 
ATOM   748  C  CA  . MET   A 1 118 ? -7.56922  -7.27467  13.61293  1.000 25.03421 ? 117 MET   A CA  1 
ATOM   749  C  C   . MET   A 1 118 ? -6.60676  -8.39883  13.94400  1.000 22.78775 ? 117 MET   A C   1 
ATOM   750  O  O   . MET   A 1 118 ? -6.25793  -9.22334  13.09153  1.000 24.46448 ? 117 MET   A O   1 
ATOM   751  C  CB  . MET   A 1 118 ? -8.95228  -7.69359  14.13221  1.000 26.32529 ? 117 MET   A CB  1 
ATOM   752  C  CG  . MET   A 1 118 ? -10.14770 -6.75913  13.91626  1.000 27.09283 ? 117 MET   A CG  1 
ATOM   753  S  SD  . MET   A 1 118 ? -11.66478 -7.50983  13.29597  1.000 25.89081 ? 117 MET   A SD  1 
ATOM   754  C  CE  . MET   A 1 118 ? -12.16242 -8.32059  14.80532  1.000 26.14556 ? 117 MET   A CE  1 
ATOM   755  N  N   . HIS   A 1 119 ? -6.17633  -8.39325  15.20719  1.000 23.00017 ? 118 HIS   A N   1 
ATOM   756  C  CA  . HIS   A 1 119 ? -5.52942  -9.52521  15.85880  1.000 22.55724 ? 118 HIS   A CA  1 
ATOM   757  C  C   . HIS   A 1 119 ? -6.57634  -10.35746 16.59600  1.000 22.98097 ? 118 HIS   A C   1 
ATOM   758  O  O   . HIS   A 1 119 ? -7.61838  -9.84663  17.01347  1.000 23.82657 ? 118 HIS   A O   1 
ATOM   759  C  CB  . HIS   A 1 119 ? -4.48130  -9.05191  16.86841  1.000 25.70041 ? 118 HIS   A CB  1 
ATOM   760  C  CG  . HIS   A 1 119 ? -3.33508  -8.32858  16.24762  1.000 30.96517 ? 118 HIS   A CG  1 
ATOM   761  N  ND1 . HIS   A 1 119 ? -2.08448  -8.88947  16.11332  1.000 33.63202 ? 118 HIS   A ND1 1 
ATOM   762  C  CD2 . HIS   A 1 119 ? -3.25259  -7.08780  15.71277  1.000 30.42137 ? 118 HIS   A CD2 1 
ATOM   763  C  CE1 . HIS   A 1 119 ? -1.27730  -8.02330  15.52585  1.000 31.19050 ? 118 HIS   A CE1 1 
ATOM   764  N  NE2 . HIS   A 1 119 ? -1.96238  -6.92263  15.27375  1.000 38.74934 ? 118 HIS   A NE2 1 
ATOM   765  N  N   . GLY   A 1 120 ? -6.28498  -11.63446 16.78720  1.000 21.98821 ? 119 GLY   A N   1 
ATOM   766  C  CA  . GLY   A 1 120 ? -7.17652  -12.49609 17.55055  1.000 22.49746 ? 119 GLY   A CA  1 
ATOM   767  C  C   . GLY   A 1 120 ? -6.38440  -13.53612 18.30971  1.000 25.83211 ? 119 GLY   A C   1 
ATOM   768  O  O   . GLY   A 1 120 ? -5.31154  -13.96240 17.87796  1.000 25.34697 ? 119 GLY   A O   1 
ATOM   769  N  N   . MET   A 1 121 ? -6.90138  -13.92804 19.47164  1.000 21.72776 ? 120 MET   A N   1 
ATOM   770  C  CA  A MET   A 1 121 ? -6.28226  -14.98338 20.25716  0.643 19.43791 ? 120 MET   A CA  1 
ATOM   771  C  CA  B MET   A 1 121 ? -6.28723  -14.99104 20.25244  0.357 19.50289 ? 120 MET   A CA  1 
ATOM   772  C  C   . MET   A 1 121 ? -7.39163  -15.87115 20.79639  1.000 24.69055 ? 120 MET   A C   1 
ATOM   773  O  O   . MET   A 1 121 ? -8.33291  -15.37219 21.41661  1.000 28.05741 ? 120 MET   A O   1 
ATOM   774  C  CB  A MET   A 1 121 ? -5.44123  -14.39544 21.40550  0.643 22.09151 ? 120 MET   A CB  1 
ATOM   775  C  CB  B MET   A 1 121 ? -5.46726  -14.42453 21.40385  0.357 22.15726 ? 120 MET   A CB  1 
ATOM   776  C  CG  A MET   A 1 121 ? -4.58562  -15.42926 22.13478  0.643 21.90597 ? 120 MET   A CG  1 
ATOM   777  C  CG  B MET   A 1 121 ? -4.54220  -13.33928 20.98368  0.357 21.61106 ? 120 MET   A CG  1 
ATOM   778  S  SD  A MET   A 1 121 ? -3.47459  -14.78138 23.41701  0.643 25.84129 ? 120 MET   A SD  1 
ATOM   779  S  SD  B MET   A 1 121 ? -3.78028  -12.64419 22.44401  0.357 34.73806 ? 120 MET   A SD  1 
ATOM   780  C  CE  A MET   A 1 121 ? -2.35668  -13.76842 22.43488  0.643 27.61833 ? 120 MET   A CE  1 
ATOM   781  C  CE  B MET   A 1 121 ? -2.55298  -13.88812 22.81484  0.357 27.63357 ? 120 MET   A CE  1 
ATOM   782  N  N   . LEU   A 1 122 ? -7.28631  -17.17477 20.57069  1.000 18.66212 ? 121 LEU   A N   1 
ATOM   783  C  CA  A LEU   A 1 122 ? -8.30139  -18.04644 21.11131  0.592 20.77473 ? 121 LEU   A CA  1 
ATOM   784  C  CA  B LEU   A 1 122 ? -8.29816  -18.15965 20.94178  0.408 20.82532 ? 121 LEU   A CA  1 
ATOM   785  C  C   . LEU   A 1 122 ? -7.67951  -19.19777 21.87813  1.000 21.90186 ? 121 LEU   A C   1 
ATOM   786  O  O   . LEU   A 1 122 ? -6.52194  -19.58043 21.68114  1.000 23.18310 ? 121 LEU   A O   1 
ATOM   787  C  CB  A LEU   A 1 122 ? -9.25283  -18.51408 20.02892  0.592 24.35373 ? 121 LEU   A CB  1 
ATOM   788  C  CB  B LEU   A 1 122 ? -8.83441  -18.83062 19.66317  0.408 21.33266 ? 121 LEU   A CB  1 
ATOM   789  C  CG  A LEU   A 1 122 ? -8.73576  -19.53047 19.03544  0.592 20.61185 ? 121 LEU   A CG  1 
ATOM   790  C  CG  B LEU   A 1 122 ? -9.89061  -19.93535 19.64559  0.408 21.31409 ? 121 LEU   A CG  1 
ATOM   791  C  CD1 A LEU   A 1 122 ? -8.83471  -20.93758 19.55934  0.592 20.34498 ? 121 LEU   A CD1 1 
ATOM   792  C  CD1 B LEU   A 1 122 ? -10.60918 -19.88399 18.29672  0.408 23.06080 ? 121 LEU   A CD1 1 
ATOM   793  C  CD2 A LEU   A 1 122 ? -9.60983  -19.41222 17.78744  0.592 25.45845 ? 121 LEU   A CD2 1 
ATOM   794  C  CD2 B LEU   A 1 122 ? -9.27772  -21.29744 19.87269  0.408 25.05486 ? 121 LEU   A CD2 1 
ATOM   795  N  N   . LYS   A 1 123 ? -8.45514  -19.68570 22.84303  1.000 18.61994 ? 122 LYS   A N   1 
ATOM   796  C  CA  A LYS   A 1 123 ? -8.02147  -20.76990 23.72028  0.389 17.94727 ? 122 LYS   A CA  1 
ATOM   797  C  CA  B LYS   A 1 123 ? -8.02014  -20.76761 23.72521  0.611 17.86184 ? 122 LYS   A CA  1 
ATOM   798  C  C   . LYS   A 1 123 ? -9.18134  -21.73424 23.90358  1.000 19.65991 ? 122 LYS   A C   1 
ATOM   799  O  O   . LYS   A 1 123 ? -10.25611 -21.32778 24.35128  1.000 19.53297 ? 122 LYS   A O   1 
ATOM   800  C  CB  A LYS   A 1 123 ? -7.55491  -20.22449 25.07603  0.389 21.86443 ? 122 LYS   A CB  1 
ATOM   801  C  CB  B LYS   A 1 123 ? -7.55372  -20.21406 25.08069  0.611 21.84108 ? 122 LYS   A CB  1 
ATOM   802  C  CG  A LYS   A 1 123 ? -7.27973  -21.30461 26.11709  0.389 23.89376 ? 122 LYS   A CG  1 
ATOM   803  C  CG  B LYS   A 1 123 ? -7.32593  -21.28198 26.15477  0.611 23.85791 ? 122 LYS   A CG  1 
ATOM   804  C  CD  A LYS   A 1 123 ? -5.91619  -21.93023 25.88710  0.389 27.26836 ? 122 LYS   A CD  1 
ATOM   805  C  CD  B LYS   A 1 123 ? -5.97542  -21.94370 25.96008  0.611 27.35009 ? 122 LYS   A CD  1 
ATOM   806  C  CE  A LYS   A 1 123 ? -5.59738  -22.97785 26.94750  0.389 27.74428 ? 122 LYS   A CE  1 
ATOM   807  C  CE  B LYS   A 1 123 ? -5.85252  -23.23109 26.76993  0.611 28.60239 ? 122 LYS   A CE  1 
ATOM   808  N  NZ  A LYS   A 1 123 ? -6.57362  -24.10686 26.91320  0.389 28.27293 ? 122 LYS   A NZ  1 
ATOM   809  N  NZ  B LYS   A 1 123 ? -5.85501  -22.99454 28.24346  0.611 27.41738 ? 122 LYS   A NZ  1 
ATOM   810  N  N   . VAL   A 1 124 ? -8.96328  -23.01640 23.57632  1.000 18.99784 ? 123 VAL   A N   1 
ATOM   811  C  CA  . VAL   A 1 124 ? -10.01979 -24.01683 23.74780  1.000 18.29039 ? 123 VAL   A CA  1 
ATOM   812  C  C   . VAL   A 1 124 ? -10.22275 -24.28379 25.22723  1.000 21.17811 ? 123 VAL   A C   1 
ATOM   813  O  O   . VAL   A 1 124 ? -9.25151  -24.45657 25.98366  1.000 22.97689 ? 123 VAL   A O   1 
ATOM   814  C  CB  . VAL   A 1 124 ? -9.68190  -25.31979 23.00412  1.000 21.35885 ? 123 VAL   A CB  1 
ATOM   815  C  CG1 . VAL   A 1 124 ? -10.79553 -26.34184 23.22896  1.000 20.91326 ? 123 VAL   A CG1 1 
ATOM   816  C  CG2 . VAL   A 1 124 ? -9.47557  -25.03039 21.50255  1.000 22.21227 ? 123 VAL   A CG2 1 
ATOM   817  N  N   . LEU   A 1 125 ? -11.48967 -24.31109 25.65426  1.000 19.14498 ? 124 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 125 ? -11.86219 -24.54356 27.04402  1.000 19.26525 ? 124 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 125 ? -12.30416 -25.97392 27.31566  1.000 23.11688 ? 124 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 125 ? -11.98731 -26.52012 28.37627  1.000 25.39646 ? 124 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 125 ? -12.98780 -23.59241 27.45540  1.000 21.95331 ? 124 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 125 ? -12.66253 -22.11453 27.33544  1.000 23.26763 ? 124 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 125 ? -13.94660 -21.32889 27.59905  1.000 24.89181 ? 124 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 125 ? -11.59328 -21.75773 28.34717  1.000 25.71967 ? 124 LEU   A CD2 1 
ATOM   825  N  N   . TYR   A 1 126 ? -13.05976 -26.57637 26.40304  1.000 21.13118 ? 125 TYR   A N   1 
ATOM   826  C  CA  . TYR   A 1 126 ? -13.39038 -27.99051 26.49305  1.000 21.68308 ? 125 TYR   A CA  1 
ATOM   827  C  C   . TYR   A 1 126 ? -13.67908 -28.48965 25.09215  1.000 21.77381 ? 125 TYR   A C   1 
ATOM   828  O  O   . TYR   A 1 126 ? -13.93983 -27.71157 24.17547  1.000 19.85537 ? 125 TYR   A O   1 
ATOM   829  C  CB  . TYR   A 1 126 ? -14.58051 -28.27275 27.43011  1.000 21.78177 ? 125 TYR   A CB  1 
ATOM   830  C  CG  . TYR   A 1 126 ? -15.88882 -27.62882 27.04158  1.000 19.66532 ? 125 TYR   A CG  1 
ATOM   831  C  CD1 . TYR   A 1 126 ? -16.71156 -28.20421 26.08072  1.000 20.07323 ? 125 TYR   A CD1 1 
ATOM   832  C  CD2 . TYR   A 1 126 ? -16.31574 -26.46085 27.67770  1.000 19.86743 ? 125 TYR   A CD2 1 
ATOM   833  C  CE1 . TYR   A 1 126 ? -17.90523 -27.61400 25.73028  1.000 20.46362 ? 125 TYR   A CE1 1 
ATOM   834  C  CE2 . TYR   A 1 126 ? -17.49533 -25.86851 27.35047  1.000 20.36381 ? 125 TYR   A CE2 1 
ATOM   835  C  CZ  . TYR   A 1 126 ? -18.29854 -26.44452 26.37629  1.000 21.21939 ? 125 TYR   A CZ  1 
ATOM   836  O  OH  . TYR   A 1 126 ? -19.45859 -25.81596 26.05726  1.000 23.07803 ? 125 TYR   A OH  1 
ATOM   837  N  N   . GLY   A 1 127 ? -13.61677 -29.80200 24.93275  1.000 22.64000 ? 126 GLY   A N   1 
ATOM   838  C  CA  . GLY   A 1 127 ? -13.88379 -30.35409 23.63410  1.000 21.70964 ? 126 GLY   A CA  1 
ATOM   839  C  C   . GLY   A 1 127 ? -12.67676 -30.24788 22.72506  1.000 21.58009 ? 126 GLY   A C   1 
ATOM   840  O  O   . GLY   A 1 127 ? -11.55653 -29.89212 23.12977  1.000 24.43692 ? 126 GLY   A O   1 
ATOM   841  N  N   . THR   A 1 128 ? -12.92060 -30.60121 21.46750  1.000 22.26684 ? 127 THR   A N   1 
ATOM   842  C  CA  . THR   A 1 128 ? -11.92522 -30.55689 20.40280  1.000 22.12373 ? 127 THR   A CA  1 
ATOM   843  C  C   . THR   A 1 128 ? -12.48469 -29.72512 19.26220  1.000 22.36280 ? 127 THR   A C   1 
ATOM   844  O  O   . THR   A 1 128 ? -13.64074 -29.92044 18.87190  1.000 21.89206 ? 127 THR   A O   1 
ATOM   845  C  CB  . THR   A 1 128 ? -11.60060 -31.97492 19.88846  1.000 27.35050 ? 127 THR   A CB  1 
ATOM   846  O  OG1 . THR   A 1 128 ? -11.11919 -32.77934 20.96835  1.000 29.77567 ? 127 THR   A OG1 1 
ATOM   847  C  CG2 . THR   A 1 128 ? -10.53363 -31.92834 18.80268  1.000 28.33799 ? 127 THR   A CG2 1 
ATOM   848  N  N   . VAL   A 1 129 ? -11.67434 -28.81526 18.71623  1.000 21.91991 ? 128 VAL   A N   1 
ATOM   849  C  CA  . VAL   A 1 129 ? -12.05562 -28.12049 17.48729  1.000 21.48684 ? 128 VAL   A CA  1 
ATOM   850  C  C   . VAL   A 1 129 ? -10.99477 -28.33853 16.42046  1.000 24.68794 ? 128 VAL   A C   1 
ATOM   851  O  O   . VAL   A 1 129 ? -9.79595  -28.43345 16.70915  1.000 25.00374 ? 128 VAL   A O   1 
ATOM   852  C  CB  . VAL   A 1 129 ? -12.28611 -26.60417 17.67426  1.000 20.16399 ? 128 VAL   A CB  1 
ATOM   853  C  CG1 . VAL   A 1 129 ? -13.53168 -26.34455 18.56227  1.000 23.85333 ? 128 VAL   A CG1 1 
ATOM   854  C  CG2 . VAL   A 1 129 ? -11.04734 -25.92503 18.23650  1.000 21.64396 ? 128 VAL   A CG2 1 
ATOM   855  N  N   . ARG   A 1 130 ? -11.45750 -28.40899 15.17388  1.000 22.47006 ? 129 ARG   A N   1 
ATOM   856  C  CA  . ARG   A 1 130 ? -10.57804 -28.32259 14.00878  1.000 21.06717 ? 129 ARG   A CA  1 
ATOM   857  C  C   . ARG   A 1 130 ? -10.57700 -26.87501 13.53437  1.000 21.19768 ? 129 ARG   A C   1 
ATOM   858  O  O   . ARG   A 1 130 ? -11.63495 -26.32268 13.22568  1.000 21.63871 ? 129 ARG   A O   1 
ATOM   859  C  CB  . ARG   A 1 130 ? -11.05395 -29.24431 12.89222  1.000 22.66336 ? 129 ARG   A CB  1 
ATOM   860  C  CG  . ARG   A 1 130 ? -10.14506 -29.23441 11.67141  1.000 25.58745 ? 129 ARG   A CG  1 
ATOM   861  C  CD  . ARG   A 1 130 ? -10.76053 -30.06006 10.55859  1.000 32.24286 ? 129 ARG   A CD  1 
ATOM   862  N  NE  . ARG   A 1 130 ? -11.06916 -31.40808 11.01922  1.000 35.51527 ? 129 ARG   A NE  1 
ATOM   863  C  CZ  . ARG   A 1 130 ? -12.29463 -31.87996 11.21172  1.000 34.82535 ? 129 ARG   A CZ  1 
ATOM   864  N  NH1 . ARG   A 1 130 ? -13.36924 -31.13103 11.00278  1.000 32.21950 ? 129 ARG   A NH1 1 
ATOM   865  N  NH2 . ARG   A 1 130 ? -12.44685 -33.13958 11.61745  1.000 36.33125 ? 129 ARG   A NH2 1 
ATOM   866  N  N   . ILE   A 1 131 ? -9.40939  -26.24130 13.52079  1.000 20.56103 ? 130 ILE   A N   1 
ATOM   867  C  CA  . ILE   A 1 131 ? -9.29517  -24.86748 13.04725  1.000 21.28774 ? 130 ILE   A CA  1 
ATOM   868  C  C   . ILE   A 1 131 ? -8.52528  -24.88944 11.73627  1.000 20.71303 ? 130 ILE   A C   1 
ATOM   869  O  O   . ILE   A 1 131 ? -7.36803  -25.32177 11.69607  1.000 23.62559 ? 130 ILE   A O   1 
ATOM   870  C  CB  . ILE   A 1 131 ? -8.61295  -23.95896 14.07475  1.000 21.39247 ? 130 ILE   A CB  1 
ATOM   871  C  CG1 . ILE   A 1 131 ? -9.38963  -23.98398 15.39816  1.000 22.20014 ? 130 ILE   A CG1 1 
ATOM   872  C  CG2 . ILE   A 1 131 ? -8.56552  -22.53632 13.53900  1.000 23.12351 ? 130 ILE   A CG2 1 
ATOM   873  C  CD1 . ILE   A 1 131 ? -8.66871  -23.26130 16.53908  1.000 22.69437 ? 130 ILE   A CD1 1 
ATOM   874  N  N   . SER   A 1 132 ? -9.18730  -24.46382 10.67022  1.000 20.46283 ? 131 SER   A N   1 
ATOM   875  C  CA  . SER   A 1 132 ? -8.56166  -24.28477 9.36359   1.000 21.57738 ? 131 SER   A CA  1 
ATOM   876  C  C   . SER   A 1 132 ? -8.19048  -22.82011 9.18274   1.000 25.33082 ? 131 SER   A C   1 
ATOM   877  O  O   . SER   A 1 132 ? -9.04130  -21.93996 9.33845   1.000 23.17362 ? 131 SER   A O   1 
ATOM   878  C  CB  . SER   A 1 132 ? -9.51165  -24.73812 8.25914   1.000 23.29805 ? 131 SER   A CB  1 
ATOM   879  O  OG  . SER   A 1 132 ? -9.89085  -26.09494 8.45594   1.000 28.32897 ? 131 SER   A OG  1 
ATOM   880  N  N   . CYS   A 1 133 ? -6.93252  -22.55880 8.82445   1.000 23.98737 ? 132 CYS   A N   1 
ATOM   881  C  CA  . CYS   A 1 133 ? -6.37469  -21.21172 8.81751   1.000 22.84934 ? 132 CYS   A CA  1 
ATOM   882  C  C   . CYS   A 1 133 ? -5.93296  -20.85021 7.41108   1.000 25.53460 ? 132 CYS   A C   1 
ATOM   883  O  O   . CYS   A 1 133 ? -5.19485  -21.61713 6.77442   1.000 25.64512 ? 132 CYS   A O   1 
ATOM   884  C  CB  . CYS   A 1 133 ? -5.19459  -21.11748 9.76833   1.000 24.68272 ? 132 CYS   A CB  1 
ATOM   885  S  SG  . CYS   A 1 133 ? -5.61222  -21.50208 11.47593  1.000 27.70095 ? 132 CYS   A SG  1 
ATOM   886  N  N   . MET   A 1 134 ? -6.33800  -19.66642 6.95112   1.000 23.26344 ? 133 MET   A N   1 
ATOM   887  C  CA  . MET   A 1 134 ? -6.19837  -19.28893 5.54474   1.000 24.06725 ? 133 MET   A CA  1 
ATOM   888  C  C   . MET   A 1 134 ? -5.92202  -17.79713 5.44876   1.000 24.24305 ? 133 MET   A C   1 
ATOM   889  O  O   . MET   A 1 134 ? -6.14608  -17.04350 6.40142   1.000 22.84269 ? 133 MET   A O   1 
ATOM   890  C  CB  . MET   A 1 134 ? -7.50452  -19.60228 4.80463   1.000 26.14903 ? 133 MET   A CB  1 
ATOM   891  C  CG  . MET   A 1 134 ? -7.86089  -21.04038 4.90688   1.000 31.19655 ? 133 MET   A CG  1 
ATOM   892  S  SD  . MET   A 1 134 ? -9.18343  -21.46295 3.78716   1.000 29.87774 ? 133 MET   A SD  1 
ATOM   893  C  CE  . MET   A 1 134 ? -10.02416 -22.66970 4.80736   1.000 35.62849 ? 133 MET   A CE  1 
ATOM   894  N  N   . ASP   A 1 135 ? -5.47533  -17.36242 4.26571   1.000 24.31748 ? 134 ASP   A N   1 
ATOM   895  C  CA  . ASP   A 1 135 ? -5.33308  -15.94199 3.97711   1.000 26.29505 ? 134 ASP   A CA  1 
ATOM   896  C  C   . ASP   A 1 135 ? -5.70675  -15.67037 2.53226   1.000 27.11392 ? 134 ASP   A C   1 
ATOM   897  O  O   . ASP   A 1 135 ? -5.56904  -16.54196 1.67217   1.000 29.97600 ? 134 ASP   A O   1 
ATOM   898  C  CB  . ASP   A 1 135 ? -3.89833  -15.45148 4.19682   1.000 26.93854 ? 134 ASP   A CB  1 
ATOM   899  C  CG  . ASP   A 1 135 ? -3.58553  -15.26471 5.65995   1.000 29.10326 ? 134 ASP   A CG  1 
ATOM   900  O  OD1 . ASP   A 1 135 ? -4.15884  -14.33327 6.27680   1.000 27.09664 ? 134 ASP   A OD1 1 
ATOM   901  O  OD2 . ASP   A 1 135 ? -2.79084  -16.07136 6.18062   1.000 29.15701 ? 134 ASP   A OD2 1 
ATOM   902  N  N   . LYS   A 1 136 ? -6.18491  -14.46021 2.27055   1.000 27.18661 ? 135 LYS   A N   1 
ATOM   903  C  CA  . LYS   A 1 136 ? -6.29195  -14.03688 0.88183   1.000 28.37697 ? 135 LYS   A CA  1 
ATOM   904  C  C   . LYS   A 1 136 ? -4.92156  -13.67424 0.34396   1.000 34.11710 ? 135 LYS   A C   1 
ATOM   905  O  O   . LYS   A 1 136 ? -4.03875  -13.22936 1.07939   1.000 36.25129 ? 135 LYS   A O   1 
ATOM   906  C  CB  . LYS   A 1 136 ? -7.22417  -12.84094 0.71315   1.000 38.65977 ? 135 LYS   A CB  1 
ATOM   907  C  CG  . LYS   A 1 136 ? -8.56808  -12.97780 1.34068   1.000 36.98458 ? 135 LYS   A CG  1 
ATOM   908  C  CD  . LYS   A 1 136 ? -9.45471  -11.84312 0.86357   1.000 45.76130 ? 135 LYS   A CD  1 
ATOM   909  C  CE  . LYS   A 1 136 ? -10.51352 -11.48066 1.86020   1.000 43.60381 ? 135 LYS   A CE  1 
ATOM   910  N  NZ  . LYS   A 1 136 ? -10.89457 -10.05550 1.68946   1.000 41.77838 ? 135 LYS   A NZ  1 
ATOM   911  N  N   . LEU   A 1 137 ? -4.73896  -13.87569 -0.95566  1.000 32.46979 ? 136 LEU   A N   1 
ATOM   912  C  CA  . LEU   A 1 137 ? -3.45921  -13.60370 -1.58779  1.000 37.23384 ? 136 LEU   A CA  1 
ATOM   913  C  C   . LEU   A 1 137 ? -3.54255  -12.30773 -2.38143  1.000 55.06089 ? 136 LEU   A C   1 
ATOM   914  O  O   . LEU   A 1 137 ? -4.47592  -12.11858 -3.16673  1.000 56.92712 ? 136 LEU   A O   1 
ATOM   915  C  CB  . LEU   A 1 137 ? -3.04083  -14.76127 -2.49423  1.000 39.75851 ? 136 LEU   A CB  1 
ATOM   916  C  CG  . LEU   A 1 137 ? -2.64273  -16.02010 -1.71484  1.000 40.38206 ? 136 LEU   A CG  1 
ATOM   917  C  CD1 . LEU   A 1 137 ? -2.28220  -17.14945 -2.67449  1.000 46.44457 ? 136 LEU   A CD1 1 
ATOM   918  C  CD2 . LEU   A 1 137 ? -1.51810  -15.74812 -0.72803  1.000 49.72733 ? 136 LEU   A CD2 1 
ATOM   919  N  N   . ASP   A 1 138 ? -2.56440  -11.42572 -2.16567  1.000 68.74232 ? 137 ASP   A N   1 
ATOM   920  C  CA  . ASP   A 1 138 ? -2.41460  -10.15883 -2.89502  1.000 71.75704 ? 137 ASP   A CA  1 
ATOM   921  C  C   . ASP   A 1 138 ? -3.73767  -9.55624  -3.36406  1.000 72.57919 ? 137 ASP   A C   1 
ATOM   922  O  O   . ASP   A 1 138 ? -4.26256  -8.62936  -2.74577  1.000 77.23272 ? 137 ASP   A O   1 
ATOM   923  C  CB  . ASP   A 1 138 ? -1.48396  -10.35018 -4.09836  1.000 65.40990 ? 137 ASP   A CB  1 
ATOM   924  N  N   . PRO   A 1 145 ? -5.08930  -8.17679  -7.95341  1.000 89.99270 ? 144 PRO   A N   1 
ATOM   925  C  CA  . PRO   A 1 145 ? -5.49411  -9.53984  -7.58728  1.000 90.25317 ? 144 PRO   A CA  1 
ATOM   926  C  C   . PRO   A 1 145 ? -5.65501  -10.44781 -8.80838  1.000 83.22915 ? 144 PRO   A C   1 
ATOM   927  O  O   . PRO   A 1 145 ? -6.26443  -10.04881 -9.79970  1.000 80.31529 ? 144 PRO   A O   1 
ATOM   928  C  CB  . PRO   A 1 145 ? -6.84051  -9.33334  -6.87011  1.000 77.99885 ? 144 PRO   A CB  1 
ATOM   929  C  CG  . PRO   A 1 145 ? -7.25533  -7.92116  -7.18743  1.000 84.96776 ? 144 PRO   A CG  1 
ATOM   930  C  CD  . PRO   A 1 145 ? -5.98234  -7.16353  -7.36961  1.000 91.31044 ? 144 PRO   A CD  1 
ATOM   931  N  N   . ARG   A 1 146 ? -5.10904  -11.65827 -8.72095  1.000 76.78665 ? 145 ARG   A N   1 
ATOM   932  C  CA  . ARG   A 1 146 ? -5.12646  -12.58845 -9.84143  1.000 74.50682 ? 145 ARG   A CA  1 
ATOM   933  C  C   . ARG   A 1 146 ? -6.54043  -13.08703 -10.13228 1.000 69.81739 ? 145 ARG   A C   1 
ATOM   934  O  O   . ARG   A 1 146 ? -7.36119  -13.27671 -9.22908  1.000 58.39040 ? 145 ARG   A O   1 
ATOM   935  C  CB  . ARG   A 1 146 ? -4.20141  -13.77142 -9.55586  1.000 67.64715 ? 145 ARG   A CB  1 
ATOM   936  C  CG  . ARG   A 1 146 ? -4.21463  -14.84536 -10.61989 1.000 68.13599 ? 145 ARG   A CG  1 
ATOM   937  C  CD  . ARG   A 1 146 ? -3.07964  -15.81840 -10.40316 1.000 68.07518 ? 145 ARG   A CD  1 
ATOM   938  N  NE  . ARG   A 1 146 ? -3.30053  -16.65694 -9.22956  1.000 70.59560 ? 145 ARG   A NE  1 
ATOM   939  C  CZ  . ARG   A 1 146 ? -3.41184  -17.97846 -9.26438  1.000 73.02597 ? 145 ARG   A CZ  1 
ATOM   940  N  NH1 . ARG   A 1 146 ? -3.36932  -18.64575 -10.40742 1.000 67.91937 ? 145 ARG   A NH1 1 
ATOM   941  N  NH2 . ARG   A 1 146 ? -3.57672  -18.64640 -8.12528  1.000 64.49670 ? 145 ARG   A NH2 1 
ATOM   942  N  N   . ALA   A 1 147 ? -6.81429  -13.30611 -11.41597 1.000 62.68501 ? 146 ALA   A N   1 
ATOM   943  C  CA  . ALA   A 1 147 ? -8.12392  -13.73381 -11.88211 1.000 54.43911 ? 146 ALA   A CA  1 
ATOM   944  C  C   . ALA   A 1 147 ? -8.16323  -15.24537 -12.08733 1.000 45.95714 ? 146 ALA   A C   1 
ATOM   945  O  O   . ALA   A 1 147 ? -7.13997  -15.89272 -12.33276 1.000 44.75617 ? 146 ALA   A O   1 
ATOM   946  C  CB  . ALA   A 1 147 ? -8.49299  -13.02246 -13.18784 1.000 58.61766 ? 146 ALA   A CB  1 
ATOM   947  N  N   . LEU   A 1 148 ? -9.35844  -15.80156 -11.97896 1.000 40.42262 ? 147 LEU   A N   1 
ATOM   948  C  CA  . LEU   A 1 148 ? -9.53457  -17.23178 -12.21347 1.000 35.68461 ? 147 LEU   A CA  1 
ATOM   949  C  C   . LEU   A 1 148 ? -9.23134  -17.56390 -13.67636 1.000 34.31233 ? 147 LEU   A C   1 
ATOM   950  O  O   . LEU   A 1 148 ? -9.75862  -16.90251 -14.57592 1.000 41.21400 ? 147 LEU   A O   1 
ATOM   951  C  CB  . LEU   A 1 148 ? -10.96140 -17.63294 -11.86162 1.000 36.65755 ? 147 LEU   A CB  1 
ATOM   952  C  CG  . LEU   A 1 148 ? -11.41133 -19.05559 -12.14871 1.000 32.64433 ? 147 LEU   A CG  1 
ATOM   953  C  CD1 . LEU   A 1 148 ? -10.88250 -19.95226 -11.02466 1.000 30.77881 ? 147 LEU   A CD1 1 
ATOM   954  C  CD2 . LEU   A 1 148 ? -12.93233 -19.09289 -12.22402 1.000 35.59329 ? 147 LEU   A CD2 1 
ATOM   955  N  N   . PRO   A 1 149 ? -8.38982  -18.55715 -13.95333 1.000 33.99701 ? 148 PRO   A N   1 
ATOM   956  C  CA  . PRO   A 1 149 ? -8.16086  -18.97979 -15.34538 1.000 34.37833 ? 148 PRO   A CA  1 
ATOM   957  C  C   . PRO   A 1 149 ? -9.46451  -19.39224 -16.00129 1.000 31.25670 ? 148 PRO   A C   1 
ATOM   958  O  O   . PRO   A 1 149 ? -10.30285 -20.05104 -15.36288 1.000 29.75322 ? 148 PRO   A O   1 
ATOM   959  C  CB  . PRO   A 1 149 ? -7.21347  -20.18314 -15.21337 1.000 39.43904 ? 148 PRO   A CB  1 
ATOM   960  C  CG  . PRO   A 1 149 ? -6.79444  -20.24564 -13.78025 1.000 40.74059 ? 148 PRO   A CG  1 
ATOM   961  C  CD  . PRO   A 1 149 ? -7.36830  -19.08121 -13.03707 1.000 40.34646 ? 148 PRO   A CD  1 
ATOM   962  N  N   . PRO   A 1 150 ? -9.64785  -19.06865 -17.28862 1.000 29.26159 ? 149 PRO   A N   1 
ATOM   963  C  CA  . PRO   A 1 150 ? -10.96270 -19.30445 -17.91652 1.000 27.23281 ? 149 PRO   A CA  1 
ATOM   964  C  C   . PRO   A 1 150 ? -11.41698 -20.75118 -17.88131 1.000 31.21910 ? 149 PRO   A C   1 
ATOM   965  O  O   . PRO   A 1 150 ? -12.61856 -21.00606 -17.72685 1.000 29.06371 ? 149 PRO   A O   1 
ATOM   966  C  CB  . PRO   A 1 150 ? -10.75623 -18.82407 -19.36108 1.000 31.28977 ? 149 PRO   A CB  1 
ATOM   967  C  CG  . PRO   A 1 150 ? -9.56936  -17.91026 -19.30451 1.000 45.61907 ? 149 PRO   A CG  1 
ATOM   968  C  CD  . PRO   A 1 150 ? -8.69166  -18.42725 -18.20358 1.000 35.68864 ? 149 PRO   A CD  1 
ATOM   969  N  N   . GLU   A 1 151 ? -10.50706 -21.71227 -18.05237 1.000 31.02025 ? 150 GLU   A N   1 
ATOM   970  C  CA  . GLU   A 1 151 ? -10.92817 -23.10466 -18.15795 1.000 32.45567 ? 150 GLU   A CA  1 
ATOM   971  C  C   . GLU   A 1 151 ? -11.16477 -23.76846 -16.80768 1.000 34.54909 ? 150 GLU   A C   1 
ATOM   972  O  O   . GLU   A 1 151 ? -11.67973 -24.89355 -16.78015 1.000 37.16904 ? 150 GLU   A O   1 
ATOM   973  C  CB  . GLU   A 1 151 ? -9.89224  -23.92395 -18.93190 1.000 35.85305 ? 150 GLU   A CB  1 
ATOM   974  N  N   . GLN   A 1 152 ? -10.81888 -23.11393 -15.70000 1.000 35.24099 ? 151 GLN   A N   1 
ATOM   975  C  CA  . GLN   A 1 152 ? -10.97688 -23.75067 -14.39727 1.000 36.47735 ? 151 GLN   A CA  1 
ATOM   976  C  C   . GLN   A 1 152 ? -12.42950 -24.10667 -14.11998 1.000 36.56614 ? 151 GLN   A C   1 
ATOM   977  O  O   . GLN   A 1 152 ? -13.33674 -23.29298 -14.31949 1.000 32.15939 ? 151 GLN   A O   1 
ATOM   978  C  CB  . GLN   A 1 152 ? -10.42956 -22.86536 -13.28463 1.000 34.28159 ? 151 GLN   A CB  1 
ATOM   979  C  CG  . GLN   A 1 152 ? -10.11959 -23.68671 -12.02241 1.000 45.02911 ? 151 GLN   A CG  1 
ATOM   980  C  CD  . GLN   A 1 152 ? -8.73158  -24.29753 -12.02577 1.000 51.61226 ? 151 GLN   A CD  1 
ATOM   981  O  OE1 . GLN   A 1 152 ? -8.58839  -25.51948 -12.01397 1.000 59.73011 ? 151 GLN   A OE1 1 
ATOM   982  N  NE2 . GLN   A 1 152 ? -7.70341  -23.45259 -12.01616 1.000 59.86486 ? 151 GLN   A NE2 1 
ATOM   983  N  N   . GLN   A 1 153 ? -12.62942 -25.33191 -13.64327 1.000 35.36264 ? 152 GLN   A N   1 
ATOM   984  C  CA  A GLN   A 1 153 ? -13.93470 -25.89906 -13.34853 0.492 37.41631 ? 152 GLN   A CA  1 
ATOM   985  C  CA  B GLN   A 1 153 ? -13.94737 -25.85832 -13.33278 0.508 37.40033 ? 152 GLN   A CA  1 
ATOM   986  C  C   . GLN   A 1 153 ? -13.99603 -26.25797 -11.86543 1.000 39.80990 ? 152 GLN   A C   1 
ATOM   987  O  O   . GLN   A 1 153 ? -12.98422 -26.63978 -11.27150 1.000 41.96622 ? 152 GLN   A O   1 
ATOM   988  C  CB  A GLN   A 1 153 ? -14.15264 -27.13303 -14.23370 0.492 40.37330 ? 152 GLN   A CB  1 
ATOM   989  C  CB  B GLN   A 1 153 ? -14.30823 -27.06738 -14.21053 0.508 40.24361 ? 152 GLN   A CB  1 
ATOM   990  C  CG  A GLN   A 1 153 ? -15.57737 -27.50787 -14.56212 0.492 43.46007 ? 152 GLN   A CG  1 
ATOM   991  C  CG  B GLN   A 1 153 ? -13.12515 -27.91642 -14.65733 0.508 50.28698 ? 152 GLN   A CG  1 
ATOM   992  C  CD  A GLN   A 1 153 ? -15.62139 -28.69309 -15.51231 0.492 47.76641 ? 152 GLN   A CD  1 
ATOM   993  C  CD  B GLN   A 1 153 ? -13.49241 -28.87340 -15.78140 0.508 51.48795 ? 152 GLN   A CD  1 
ATOM   994  O  OE1 A GLN   A 1 153 ? -14.60518 -29.06479 -16.10105 0.492 52.57231 ? 152 GLN   A OE1 1 
ATOM   995  O  OE1 B GLN   A 1 153 ? -14.67091 -29.10789 -16.05339 0.508 52.60728 ? 152 GLN   A OE1 1 
ATOM   996  N  NE2 A GLN   A 1 153 ? -16.79673 -29.26333 -15.69773 0.492 48.39894 ? 152 GLN   A NE2 1 
ATOM   997  N  NE2 B GLN   A 1 153 ? -12.48145 -29.43004 -16.44077 0.508 54.46502 ? 152 GLN   A NE2 1 
ATOM   998  N  N   . PHE   A 1 154 ? -15.18357 -26.13693 -11.27321 1.000 37.28690 ? 153 PHE   A N   1 
ATOM   999  C  CA  . PHE   A 1 154 ? -15.39023 -26.44094 -9.86074  1.000 34.62994 ? 153 PHE   A CA  1 
ATOM   1000 C  C   . PHE   A 1 154 ? -16.55034 -27.41508 -9.69692  1.000 40.31101 ? 153 PHE   A C   1 
ATOM   1001 O  O   . PHE   A 1 154 ? -17.40941 -27.54857 -10.57281 1.000 41.77078 ? 153 PHE   A O   1 
ATOM   1002 C  CB  . PHE   A 1 154 ? -15.67057 -25.16698 -9.04702  1.000 40.60668 ? 153 PHE   A CB  1 
ATOM   1003 C  CG  . PHE   A 1 154 ? -14.50118 -24.21731 -8.96671  1.000 33.56835 ? 153 PHE   A CG  1 
ATOM   1004 C  CD1 . PHE   A 1 154 ? -13.46249 -24.43029 -8.07354  1.000 30.30310 ? 153 PHE   A CD1 1 
ATOM   1005 C  CD2 . PHE   A 1 154 ? -14.43382 -23.11804 -9.81602  1.000 40.04565 ? 153 PHE   A CD2 1 
ATOM   1006 C  CE1 . PHE   A 1 154 ? -12.39453 -23.55441 -8.00125  1.000 37.54973 ? 153 PHE   A CE1 1 
ATOM   1007 C  CE2 . PHE   A 1 154 ? -13.36059 -22.23740 -9.75302  1.000 34.37796 ? 153 PHE   A CE2 1 
ATOM   1008 C  CZ  . PHE   A 1 154 ? -12.34160 -22.45948 -8.85232  1.000 35.93899 ? 153 PHE   A CZ  1 
ATOM   1009 N  N   . GLU   A 1 155 ? -16.56721 -28.10028 -8.55271  1.000 45.82390 ? 154 GLU   A N   1 
ATOM   1010 C  CA  . GLU   A 1 155 ? -17.67409 -28.98431 -8.19648  1.000 48.73320 ? 154 GLU   A CA  1 
ATOM   1011 C  C   . GLU   A 1 155 ? -18.18537 -28.61426 -6.81290  1.000 47.73641 ? 154 GLU   A C   1 
ATOM   1012 O  O   . GLU   A 1 155 ? -17.42980 -28.71961 -5.82642  1.000 44.64884 ? 154 GLU   A O   1 
ATOM   1013 C  CB  . GLU   A 1 155 ? -17.27181 -30.46027 -8.24725  1.000 58.75530 ? 154 GLU   A CB  1 
ATOM   1014 C  CG  . GLU   A 1 155 ? -18.44798 -31.38683 -7.97707  1.000 62.75932 ? 154 GLU   A CG  1 
ATOM   1015 C  CD  . GLU   A 1 155 ? -19.25428 -31.68605 -9.22574  1.000 79.55830 ? 154 GLU   A CD  1 
ATOM   1016 O  OE1 . GLU   A 1 155 ? -20.48012 -31.44123 -9.21543  1.000 83.69755 ? 154 GLU   A OE1 1 
ATOM   1017 O  OE2 . GLU   A 1 155 ? -18.66247 -32.16167 -10.21936 1.000 82.98153 ? 154 GLU   A OE2 1 
ATOM   1018 N  N   . PRO   A 1 156 ? -19.43058 -28.16225 -6.69110  1.000 43.61156 ? 155 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 156 ? -20.39166 -27.90026 -7.77703  1.000 52.20668 ? 155 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 156 ? -19.95284 -26.74321 -8.67461  1.000 49.10403 ? 155 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 156 ? -19.16612 -25.88946 -8.26803  1.000 44.13921 ? 155 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 156 ? -21.67863 -27.58083 -7.00402  1.000 45.39144 ? 155 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 156 ? -21.17436 -26.98038 -5.72692  1.000 47.46519 ? 155 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 156 ? -20.02725 -27.87645 -5.37439  1.000 48.38256 ? 155 PRO   A CD  1 
ATOM   1025 N  N   . PRO   A 1 157 ? -20.43434 -26.72214 -9.91995  1.000 47.51891 ? 156 PRO   A N   1 
ATOM   1026 C  CA  . PRO   A 1 157 ? -20.10897 -25.61762 -10.82650 1.000 41.38239 ? 156 PRO   A CA  1 
ATOM   1027 C  C   . PRO   A 1 157 ? -20.49051 -24.27095 -10.22976 1.000 38.59721 ? 156 PRO   A C   1 
ATOM   1028 O  O   . PRO   A 1 157 ? -21.43195 -24.15587 -9.44430  1.000 41.63831 ? 156 PRO   A O   1 
ATOM   1029 C  CB  . PRO   A 1 157 ? -20.97042 -25.95501 -12.06343 1.000 42.59584 ? 156 PRO   A CB  1 
ATOM   1030 C  CG  . PRO   A 1 157 ? -21.70935 -27.22204 -11.48376 1.000 51.50445 ? 156 PRO   A CG  1 
ATOM   1031 C  CD  . PRO   A 1 157 ? -20.59687 -27.82333 -10.86729 1.000 56.50731 ? 156 PRO   A CD  1 
ATOM   1032 N  N   . LEU   A 1 158 ? -19.75021 -23.24318 -10.62349 1.000 36.45532 ? 157 LEU   A N   1 
ATOM   1033 C  CA  . LEU   A 1 158 ? -19.98130 -21.87996 -10.18749 1.000 32.62031 ? 157 LEU   A CA  1 
ATOM   1034 C  C   . LEU   A 1 158 ? -20.93898 -21.16969 -11.13252 1.000 32.55845 ? 157 LEU   A C   1 
ATOM   1035 O  O   . LEU   A 1 158 ? -20.91836 -21.38930 -12.35009 1.000 35.57030 ? 157 LEU   A O   1 
ATOM   1036 C  CB  . LEU   A 1 158 ? -18.66110 -21.11485 -10.15275 1.000 32.75699 ? 157 LEU   A CB  1 
ATOM   1037 C  CG  . LEU   A 1 158 ? -17.66466 -21.44984 -9.04679  1.000 36.01490 ? 157 LEU   A CG  1 
ATOM   1038 C  CD1 . LEU   A 1 158 ? -16.62598 -20.34489 -8.98482  1.000 35.81432 ? 157 LEU   A CD1 1 
ATOM   1039 C  CD2 . LEU   A 1 158 ? -18.36991 -21.59980 -7.70250  1.000 38.39531 ? 157 LEU   A CD2 1 
ATOM   1040 N  N   . GLN   A 1 159 ? -21.74986 -20.27952 -10.56980 1.000 34.62340 ? 158 GLN   A N   1 
ATOM   1041 C  CA  . GLN   A 1 159 ? -22.56127 -19.39762 -11.39236 1.000 32.08230 ? 158 GLN   A CA  1 
ATOM   1042 C  C   . GLN   A 1 159 ? -21.70732 -18.26398 -11.96043 1.000 29.35770 ? 158 GLN   A C   1 
ATOM   1043 O  O   . GLN   A 1 159 ? -20.63939 -17.95341 -11.42914 1.000 28.09366 ? 158 GLN   A O   1 
ATOM   1044 C  CB  . GLN   A 1 159 ? -23.71503 -18.82756 -10.57438 1.000 36.97692 ? 158 GLN   A CB  1 
ATOM   1045 C  CG  . GLN   A 1 159 ? -24.73789 -19.87252 -10.18809 1.000 44.69904 ? 158 GLN   A CG  1 
ATOM   1046 C  CD  . GLN   A 1 159 ? -25.35806 -20.55507 -11.39564 1.000 51.06951 ? 158 GLN   A CD  1 
ATOM   1047 O  OE1 . GLN   A 1 159 ? -25.78978 -19.90382 -12.35324 1.000 48.93160 ? 158 GLN   A OE1 1 
ATOM   1048 N  NE2 . GLN   A 1 159 ? -25.39897 -21.88469 -11.35686 1.000 58.25603 ? 158 GLN   A NE2 1 
ATOM   1049 N  N   . PRO   A 1 160 ? -22.15902 -17.61088 -13.03592 1.000 30.32790 ? 159 PRO   A N   1 
ATOM   1050 C  CA  . PRO   A 1 160 ? -21.29795 -16.58289 -13.65529 1.000 32.44036 ? 159 PRO   A CA  1 
ATOM   1051 C  C   . PRO   A 1 160 ? -20.84361 -15.50312 -12.69167 1.000 29.34688 ? 159 PRO   A C   1 
ATOM   1052 O  O   . PRO   A 1 160 ? -19.67594 -15.09398 -12.73290 1.000 26.67535 ? 159 PRO   A O   1 
ATOM   1053 C  CB  . PRO   A 1 160 ? -22.17228 -16.00270 -14.78219 1.000 30.17069 ? 159 PRO   A CB  1 
ATOM   1054 C  CG  . PRO   A 1 160 ? -23.17922 -17.05591 -15.06173 1.000 30.60975 ? 159 PRO   A CG  1 
ATOM   1055 C  CD  . PRO   A 1 160 ? -23.43312 -17.77803 -13.76191 1.000 31.07271 ? 159 PRO   A CD  1 
ATOM   1056 N  N   . ARG   A 1 161 ? -21.72765 -15.01802 -11.81660 1.000 28.14512 ? 160 ARG   A N   1 
ATOM   1057 C  CA  . ARG   A 1 161 ? -21.31952 -13.96705 -10.89459 1.000 28.47774 ? 160 ARG   A CA  1 
ATOM   1058 C  C   . ARG   A 1 161 ? -20.27869 -14.47458 -9.89899  1.000 27.50118 ? 160 ARG   A C   1 
ATOM   1059 O  O   . ARG   A 1 161 ? -19.40192 -13.71307 -9.47527  1.000 30.88858 ? 160 ARG   A O   1 
ATOM   1060 C  CB  . ARG   A 1 161 ? -22.55070 -13.42683 -10.16380 1.000 36.59684 ? 160 ARG   A CB  1 
ATOM   1061 C  CG  . ARG   A 1 161 ? -23.36027 -12.36332 -10.92628 1.000 44.54958 ? 160 ARG   A CG  1 
ATOM   1062 C  CD  . ARG   A 1 161 ? -22.52536 -11.48743 -11.85101 0.000 33.73833 ? 160 ARG   A CD  1 
ATOM   1063 N  NE  . ARG   A 1 161 ? -22.09592 -12.17639 -13.06170 0.000 32.79770 ? 160 ARG   A NE  1 
ATOM   1064 C  CZ  . ARG   A 1 161 ? -21.35390 -11.62201 -14.01028 0.000 32.75816 ? 160 ARG   A CZ  1 
ATOM   1065 N  NH1 . ARG   A 1 161 ? -20.94496 -10.36677 -13.92248 0.000 33.90934 ? 160 ARG   A NH1 1 
ATOM   1066 N  NH2 . ARG   A 1 161 ? -21.01447 -12.34426 -15.07385 0.000 31.56428 ? 160 ARG   A NH2 1 
ATOM   1067 N  N   . GLU   A 1 162 ? -20.35077 -15.75817 -9.53612  1.000 28.02476 ? 161 GLU   A N   1 
ATOM   1068 C  CA  . GLU   A 1 162 ? -19.34698 -16.33077 -8.64329  1.000 25.78137 ? 161 GLU   A CA  1 
ATOM   1069 C  C   . GLU   A 1 162 ? -17.99802 -16.48334 -9.33858  1.000 24.44503 ? 161 GLU   A C   1 
ATOM   1070 O  O   . GLU   A 1 162 ? -16.94606 -16.22303 -8.73749  1.000 27.85259 ? 161 GLU   A O   1 
ATOM   1071 C  CB  . GLU   A 1 162 ? -19.84405 -17.66639 -8.09802  1.000 30.09459 ? 161 GLU   A CB  1 
ATOM   1072 C  CG  . GLU   A 1 162 ? -21.16073 -17.53509 -7.32715  1.000 35.28114 ? 161 GLU   A CG  1 
ATOM   1073 C  CD  . GLU   A 1 162 ? -21.76026 -18.86358 -6.92456  1.000 35.43898 ? 161 GLU   A CD  1 
ATOM   1074 O  OE1 . GLU   A 1 162 ? -21.67911 -19.83963 -7.69410  1.000 34.48039 ? 161 GLU   A OE1 1 
ATOM   1075 O  OE2 . GLU   A 1 162 ? -22.35867 -18.93040 -5.83410  1.000 42.51010 ? 161 GLU   A OE2 1 
ATOM   1076 N  N   . ARG   A 1 163 ? -18.00138 -16.88397 -10.61361 1.000 25.60199 ? 162 ARG   A N   1 
ATOM   1077 C  CA  . ARG   A 1 163 ? -16.73757 -16.99079 -11.32312 1.000 25.37514 ? 162 ARG   A CA  1 
ATOM   1078 C  C   . ARG   A 1 163 ? -16.01824 -15.64822 -11.35987 1.000 29.10769 ? 162 ARG   A C   1 
ATOM   1079 O  O   . ARG   A 1 163 ? -14.78992 -15.59548 -11.26869 1.000 29.46504 ? 162 ARG   A O   1 
ATOM   1080 C  CB  . ARG   A 1 163 ? -16.98593 -17.51547 -12.73827 1.000 24.75096 ? 162 ARG   A CB  1 
ATOM   1081 C  CG  . ARG   A 1 163 ? -17.42056 -18.98049 -12.75510 1.000 25.04304 ? 162 ARG   A CG  1 
ATOM   1082 C  CD  . ARG   A 1 163 ? -17.58050 -19.51311 -14.18979 1.000 25.30743 ? 162 ARG   A CD  1 
ATOM   1083 N  NE  . ARG   A 1 163 ? -16.30173 -19.62420 -14.88118 1.000 27.37922 ? 162 ARG   A NE  1 
ATOM   1084 C  CZ  . ARG   A 1 163 ? -15.44693 -20.62751 -14.72704 1.000 30.98014 ? 162 ARG   A CZ  1 
ATOM   1085 N  NH1 . ARG   A 1 163 ? -15.68957 -21.62171 -13.89246 1.000 29.30062 ? 162 ARG   A NH1 1 
ATOM   1086 N  NH2 . ARG   A 1 163 ? -14.30320 -20.61641 -15.40745 1.000 29.45593 ? 162 ARG   A NH2 1 
ATOM   1087 N  N   . GLU   A 1 164 ? -16.77014 -14.54935 -11.50508 1.000 27.42009 ? 163 GLU   A N   1 
ATOM   1088 C  CA  . GLU   A 1 164 ? -16.16050 -13.22149 -11.49624 1.000 32.42956 ? 163 GLU   A CA  1 
ATOM   1089 C  C   . GLU   A 1 164 ? -15.58940 -12.86461 -10.12780 1.000 32.22683 ? 163 GLU   A C   1 
ATOM   1090 O  O   . GLU   A 1 164 ? -14.59530 -12.13144 -10.04872 1.000 30.66892 ? 163 GLU   A O   1 
ATOM   1091 C  CB  . GLU   A 1 164 ? -17.19242 -12.16673 -11.92156 1.000 35.20123 ? 163 GLU   A CB  1 
ATOM   1092 C  CG  . GLU   A 1 164 ? -17.69728 -12.26300 -13.36758 1.000 45.10042 ? 163 GLU   A CG  1 
ATOM   1093 C  CD  . GLU   A 1 164 ? -16.62024 -11.99591 -14.40979 0.242 38.13736 ? 163 GLU   A CD  1 
ATOM   1094 O  OE1 . GLU   A 1 164 ? -15.56172 -11.44911 -14.03793 0.862 47.25528 ? 163 GLU   A OE1 1 
ATOM   1095 O  OE2 . GLU   A 1 164 ? -16.83749 -12.31507 -15.60500 1.000 43.36533 ? 163 GLU   A OE2 1 
ATOM   1096 N  N   . ALA   A 1 165 ? -16.18298 -13.37829 -9.04408  1.000 29.62302 ? 164 ALA   A N   1 
ATOM   1097 C  CA  . ALA   A 1 165 ? -15.86570 -12.91374 -7.69814  1.000 32.74188 ? 164 ALA   A CA  1 
ATOM   1098 C  C   . ALA   A 1 165 ? -14.81603 -13.75506 -6.97692  1.000 27.42806 ? 164 ALA   A C   1 
ATOM   1099 O  O   . ALA   A 1 165 ? -14.28991 -13.31650 -5.94558  1.000 31.72293 ? 164 ALA   A O   1 
ATOM   1100 C  CB  . ALA   A 1 165 ? -17.14145 -12.87864 -6.84890  1.000 29.51963 ? 164 ALA   A CB  1 
ATOM   1101 N  N   . VAL   A 1 166 ? -14.49114 -14.94745 -7.46995  1.000 29.10024 ? 165 VAL   A N   1 
ATOM   1102 C  CA  A VAL   A 1 166 ? -13.56600 -15.78161 -6.72419  0.582 28.56254 ? 165 VAL   A CA  1 
ATOM   1103 C  CA  B VAL   A 1 166 ? -13.54483 -15.82068 -6.78190  0.418 28.62142 ? 165 VAL   A CA  1 
ATOM   1104 C  C   . VAL   A 1 166 ? -12.15924 -15.19036 -6.79337  1.000 29.33272 ? 165 VAL   A C   1 
ATOM   1105 O  O   . VAL   A 1 166 ? -11.74797 -14.58535 -7.79926  1.000 35.02277 ? 165 VAL   A O   1 
ATOM   1106 C  CB  A VAL   A 1 166 ? -13.62472 -17.23229 -7.23114  0.582 34.61190 ? 165 VAL   A CB  1 
ATOM   1107 C  CB  B VAL   A 1 166 ? -13.52489 -17.20753 -7.44771  0.418 33.85922 ? 165 VAL   A CB  1 
ATOM   1108 C  CG1 A VAL   A 1 166 ? -12.97625 -17.36304 -8.59379  0.582 32.16730 ? 165 VAL   A CG1 1 
ATOM   1109 C  CG1 B VAL   A 1 166 ? -14.87591 -17.87315 -7.32213  0.418 35.57903 ? 165 VAL   A CG1 1 
ATOM   1110 C  CG2 A VAL   A 1 166 ? -13.04488 -18.18982 -6.18402  0.582 30.23549 ? 165 VAL   A CG2 1 
ATOM   1111 C  CG2 B VAL   A 1 166 ? -13.14885 -17.08595 -8.90528  0.418 31.88391 ? 165 VAL   A CG2 1 
ATOM   1112 N  N   . ARG   A 1 167 ? -11.42580 -15.33408 -5.69184  1.000 28.18242 ? 166 ARG   A N   1 
ATOM   1113 C  CA  . ARG   A 1 167 ? -10.10166 -14.75522 -5.52620  1.000 30.92666 ? 166 ARG   A CA  1 
ATOM   1114 C  C   . ARG   A 1 167 ? -9.14312  -15.78886 -4.96016  1.000 28.96755 ? 166 ARG   A C   1 
ATOM   1115 O  O   . ARG   A 1 167 ? -9.56068  -16.74414 -4.30039  1.000 28.76460 ? 166 ARG   A O   1 
ATOM   1116 C  CB  . ARG   A 1 167 ? -10.14239 -13.52602 -4.60444  1.000 37.86828 ? 166 ARG   A CB  1 
ATOM   1117 C  CG  . ARG   A 1 167 ? -11.07251 -12.40556 -5.08429  1.000 43.05553 ? 166 ARG   A CG  1 
ATOM   1118 C  CD  . ARG   A 1 167 ? -10.39942 -11.52838 -6.14356  1.000 54.42521 ? 166 ARG   A CD  1 
ATOM   1119 N  NE  . ARG   A 1 167 ? -11.25241 -10.43700 -6.60731  1.000 58.48835 ? 166 ARG   A NE  1 
ATOM   1120 C  CZ  . ARG   A 1 167 ? -12.09541 -10.51155 -7.63231  1.000 62.58659 ? 166 ARG   A CZ  1 
ATOM   1121 N  NH1 . ARG   A 1 167 ? -12.26275 -11.63455 -8.31598  1.000 47.64231 ? 166 ARG   A NH1 1 
ATOM   1122 N  NH2 . ARG   A 1 167 ? -12.78729 -9.43037  -7.98382  1.000 54.18553 ? 166 ARG   A NH2 1 
ATOM   1123 N  N   . PRO   A 1 168 ? -7.84996  -15.63783 -5.21914  1.000 31.49023 ? 167 PRO   A N   1 
ATOM   1124 C  CA  . PRO   A 1 168 ? -6.88074  -16.61367 -4.71846  1.000 30.23022 ? 167 PRO   A CA  1 
ATOM   1125 C  C   . PRO   A 1 168 ? -6.61571  -16.45919 -3.22982  1.000 27.82203 ? 167 PRO   A C   1 
ATOM   1126 O  O   . PRO   A 1 168 ? -6.61784  -15.35559 -2.67710  1.000 29.53433 ? 167 PRO   A O   1 
ATOM   1127 C  CB  . PRO   A 1 168 ? -5.62162  -16.30413 -5.53579  1.000 36.63237 ? 167 PRO   A CB  1 
ATOM   1128 C  CG  . PRO   A 1 168 ? -5.74361  -14.85197 -5.85539  1.000 44.69899 ? 167 PRO   A CG  1 
ATOM   1129 C  CD  . PRO   A 1 168 ? -7.21614  -14.57643 -6.02030  1.000 35.93484 ? 167 PRO   A CD  1 
ATOM   1130 N  N   . GLY   A 1 169 ? -6.37126  -17.60448 -2.59095  1.000 26.43005 ? 168 GLY   A N   1 
ATOM   1131 C  CA  . GLY   A 1 169 ? -6.01096  -17.65337 -1.18529  1.000 27.61488 ? 168 GLY   A CA  1 
ATOM   1132 C  C   . GLY   A 1 169 ? -4.97770  -18.73787 -0.93834  1.000 29.74386 ? 168 GLY   A C   1 
ATOM   1133 O  O   . GLY   A 1 169 ? -4.55232  -19.43206 -1.86014  1.000 30.16973 ? 168 GLY   A O   1 
ATOM   1134 N  N   . VAL   A 1 170 ? -4.56662  -18.86179 0.32210   1.000 28.56977 ? 169 VAL   A N   1 
ATOM   1135 C  CA  . VAL   A 1 170 ? -3.64496  -19.91339 0.73695   1.000 28.18075 ? 169 VAL   A CA  1 
ATOM   1136 C  C   . VAL   A 1 170 ? -4.20109  -20.58188 1.98541   1.000 31.22591 ? 169 VAL   A C   1 
ATOM   1137 O  O   . VAL   A 1 170 ? -4.62034  -19.90077 2.93434   1.000 27.52270 ? 169 VAL   A O   1 
ATOM   1138 C  CB  . VAL   A 1 170 ? -2.22467  -19.37553 0.99451   1.000 33.71121 ? 169 VAL   A CB  1 
ATOM   1139 C  CG1 . VAL   A 1 170 ? -2.24364  -18.17785 1.94650   1.000 33.24909 ? 169 VAL   A CG1 1 
ATOM   1140 C  CG2 . VAL   A 1 170 ? -1.32507  -20.49749 1.52562   1.000 30.04479 ? 169 VAL   A CG2 1 
ATOM   1141 N  N   . LEU   A 1 171 ? -4.22859  -21.91231 1.97008   1.000 24.92921 ? 170 LEU   A N   1 
ATOM   1142 C  CA  . LEU   A 1 171 ? -4.57841  -22.70498 3.14047   1.000 28.23311 ? 170 LEU   A CA  1 
ATOM   1143 C  C   . LEU   A 1 171 ? -3.28712  -22.99872 3.88774   1.000 30.78038 ? 170 LEU   A C   1 
ATOM   1144 O  O   . LEU   A 1 171 ? -2.41422  -23.71051 3.37712   1.000 32.74347 ? 170 LEU   A O   1 
ATOM   1145 C  CB  . LEU   A 1 171 ? -5.29884  -23.98377 2.72311   1.000 29.50371 ? 170 LEU   A CB  1 
ATOM   1146 C  CG  . LEU   A 1 171 ? -5.47272  -25.03908 3.81221   1.000 32.06773 ? 170 LEU   A CG  1 
ATOM   1147 C  CD1 . LEU   A 1 171 ? -6.21908  -24.43590 4.98644   1.000 34.05623 ? 170 LEU   A CD1 1 
ATOM   1148 C  CD2 . LEU   A 1 171 ? -6.23313  -26.22784 3.25714   1.000 40.32104 ? 170 LEU   A CD2 1 
ATOM   1149 N  N   . ARG   A 1 172 ? -3.15591  -22.44202 5.08960   1.000 27.75181 ? 171 ARG   A N   1 
ATOM   1150 C  CA  . ARG   A 1 172 ? -1.89131  -22.54221 5.80238   1.000 27.24275 ? 171 ARG   A CA  1 
ATOM   1151 C  C   . ARG   A 1 172 ? -1.83958  -23.74508 6.72975   1.000 28.92428 ? 171 ARG   A C   1 
ATOM   1152 O  O   . ARG   A 1 172 ? -0.80122  -24.40692 6.82806   1.000 33.34058 ? 171 ARG   A O   1 
ATOM   1153 C  CB  . ARG   A 1 172 ? -1.63199  -21.25632 6.58137   1.000 27.06866 ? 171 ARG   A CB  1 
ATOM   1154 C  CG  . ARG   A 1 172 ? -1.48164  -20.03758 5.66966   1.000 29.55133 ? 171 ARG   A CG  1 
ATOM   1155 C  CD  . ARG   A 1 172 ? -0.82338  -18.90463 6.41061   1.000 33.66562 ? 171 ARG   A CD  1 
ATOM   1156 N  NE  . ARG   A 1 172 ? -0.66139  -17.69354 5.61194   1.000 29.37412 ? 171 ARG   A NE  1 
ATOM   1157 C  CZ  . ARG   A 1 172 ? 0.37011   -17.43761 4.82002   1.000 36.21429 ? 171 ARG   A CZ  1 
ATOM   1158 N  NH1 . ARG   A 1 172 ? 1.34068   -18.32053 4.63919   1.000 39.47123 ? 171 ARG   A NH1 1 
ATOM   1159 N  NH2 . ARG   A 1 172 ? 0.42903   -16.26539 4.19132   1.000 35.58808 ? 171 ARG   A NH2 1 
ATOM   1160 N  N   . SER   A 1 173 ? -2.94117  -24.07003 7.39489   1.000 28.24848 ? 172 SER   A N   1 
ATOM   1161 C  CA  . SER   A 1 173 ? -2.90788  -25.17628 8.33713   1.000 28.40603 ? 172 SER   A CA  1 
ATOM   1162 C  C   . SER   A 1 173 ? -4.32011  -25.63677 8.62641   1.000 29.53679 ? 172 SER   A C   1 
ATOM   1163 O  O   . SER   A 1 173 ? -5.30084  -24.91873 8.40139   1.000 26.94156 ? 172 SER   A O   1 
ATOM   1164 C  CB  . SER   A 1 173 ? -2.19599  -24.79780 9.64549   1.000 27.56787 ? 172 SER   A CB  1 
ATOM   1165 O  OG  . SER   A 1 173 ? -2.95969  -23.87515 10.40318  1.000 30.11972 ? 172 SER   A OG  1 
ATOM   1166 N  N   . ARG   A 1 174 ? -4.39658  -26.86952 9.11171   1.000 27.79941 ? 173 ARG   A N   1 
ATOM   1167 C  CA  . ARG   A 1 174 ? -5.66331  -27.47511 9.47597   1.000 26.52212 ? 173 ARG   A CA  1 
ATOM   1168 C  C   . ARG   A 1 174 ? -5.28905  -28.53079 10.51632  1.000 37.71102 ? 173 ARG   A C   1 
ATOM   1169 O  O   . ARG   A 1 174 ? -4.66228  -29.54112 10.18014  1.000 38.65231 ? 173 ARG   A O   1 
ATOM   1170 C  CB  . ARG   A 1 174 ? -6.35854  -28.06112 8.26054   1.000 31.25866 ? 173 ARG   A CB  1 
ATOM   1171 C  CG  . ARG   A 1 174 ? -7.58340  -28.86845 8.57157   1.000 32.02357 ? 173 ARG   A CG  1 
ATOM   1172 C  CD  . ARG   A 1 174 ? -8.23155  -29.34044 7.27231   1.000 43.60483 ? 173 ARG   A CD  1 
ATOM   1173 N  NE  . ARG   A 1 174 ? -8.43485  -30.78170 7.31896   0.323 47.93511 ? 173 ARG   A NE  1 
ATOM   1174 C  CZ  . ARG   A 1 174 ? -9.62011  -31.36719 7.40041   1.000 52.00094 ? 173 ARG   A CZ  1 
ATOM   1175 N  NH1 . ARG   A 1 174 ? -10.74362 -30.66716 7.34566   1.000 58.75817 ? 173 ARG   A NH1 1 
ATOM   1176 N  NH2 . ARG   A 1 174 ? -9.68073  -32.68490 7.55364   1.000 55.24902 ? 173 ARG   A NH2 1 
ATOM   1177 N  N   . ALA   A 1 175 ? -5.57786  -28.23738 11.77628  1.000 27.61072 ? 174 ALA   A N   1 
ATOM   1178 C  CA  . ALA   A 1 175 ? -5.21511  -29.12364 12.86847  1.000 23.56327 ? 174 ALA   A CA  1 
ATOM   1179 C  C   . ALA   A 1 175 ? -6.31562  -29.10800 13.91663  1.000 26.95246 ? 174 ALA   A C   1 
ATOM   1180 O  O   . ALA   A 1 175 ? -7.18999  -28.23389 13.92068  1.000 26.24225 ? 174 ALA   A O   1 
ATOM   1181 C  CB  . ALA   A 1 175 ? -3.87624  -28.72546 13.51239  1.000 27.72612 ? 174 ALA   A CB  1 
ATOM   1182 N  N   . GLU   A 1 176 ? -6.26523  -30.09552 14.80496  1.000 25.56639 ? 175 GLU   A N   1 
ATOM   1183 C  CA  . GLU   A 1 176 ? -7.19706  -30.18412 15.92198  1.000 24.81942 ? 175 GLU   A CA  1 
ATOM   1184 C  C   . GLU   A 1 176 ? -6.55803  -29.62242 17.18348  1.000 28.08629 ? 175 GLU   A C   1 
ATOM   1185 O  O   . GLU   A 1 176 ? -5.37393  -29.85085 17.44607  1.000 26.54869 ? 175 GLU   A O   1 
ATOM   1186 C  CB  . GLU   A 1 176 ? -7.61628  -31.63183 16.16732  1.000 26.68596 ? 175 GLU   A CB  1 
ATOM   1187 C  CG  . GLU   A 1 176 ? -8.38614  -32.21771 15.01712  1.000 28.38259 ? 175 GLU   A CG  1 
ATOM   1188 C  CD  . GLU   A 1 176 ? -8.91034  -33.61813 15.31022  1.000 37.49490 ? 175 GLU   A CD  1 
ATOM   1189 O  OE1 . GLU   A 1 176 ? -8.59844  -34.17150 16.38809  1.000 37.66165 ? 175 GLU   A OE1 1 
ATOM   1190 O  OE2 . GLU   A 1 176 ? -9.60696  -34.17527 14.44031  1.000 47.09010 ? 175 GLU   A OE2 1 
ATOM   1191 N  N   . TYR   A 1 177 ? -7.36066  -28.93399 17.98407  1.000 22.03222 ? 176 TYR   A N   1 
ATOM   1192 C  CA  . TYR   A 1 177 ? -6.90201  -28.28970 19.20883  1.000 22.85700 ? 176 TYR   A CA  1 
ATOM   1193 C  C   . TYR   A 1 177 ? -7.82741  -28.63684 20.36187  1.000 27.48706 ? 176 TYR   A C   1 
ATOM   1194 O  O   . TYR   A 1 177 ? -9.03691  -28.75147 20.17655  1.000 23.54517 ? 176 TYR   A O   1 
ATOM   1195 C  CB  . TYR   A 1 177 ? -6.83395  -26.76179 19.03884  1.000 25.28266 ? 176 TYR   A CB  1 
ATOM   1196 C  CG  . TYR   A 1 177 ? -5.96310  -26.31733 17.87721  1.000 24.49561 ? 176 TYR   A CG  1 
ATOM   1197 C  CD1 . TYR   A 1 177 ? -6.46926  -26.21687 16.58359  1.000 24.18006 ? 176 TYR   A CD1 1 
ATOM   1198 C  CD2 . TYR   A 1 177 ? -4.62409  -26.00988 18.08514  1.000 29.31019 ? 176 TYR   A CD2 1 
ATOM   1199 C  CE1 . TYR   A 1 177 ? -5.66327  -25.80299 15.51975  1.000 28.10497 ? 176 TYR   A CE1 1 
ATOM   1200 C  CE2 . TYR   A 1 177 ? -3.81496  -25.59751 17.03824  1.000 27.12989 ? 176 TYR   A CE2 1 
ATOM   1201 C  CZ  . TYR   A 1 177 ? -4.33264  -25.49517 15.76393  1.000 30.78173 ? 176 TYR   A CZ  1 
ATOM   1202 O  OH  . TYR   A 1 177 ? -3.51876  -25.08870 14.72646  1.000 29.12911 ? 176 TYR   A OH  1 
ATOM   1203 N  N   . THR   A 1 178 ? -7.24755  -28.82309 21.54572  1.000 23.98627 ? 177 THR   A N   1 
ATOM   1204 C  CA  . THR   A 1 178 ? -7.97782  -29.06311 22.79190  1.000 23.46978 ? 177 THR   A CA  1 
ATOM   1205 C  C   . THR   A 1 178 ? -7.51738  -28.06307 23.85190  1.000 22.28136 ? 177 THR   A C   1 
ATOM   1206 O  O   . THR   A 1 178 ? -6.67464  -27.20297 23.59893  1.000 27.07940 ? 177 THR   A O   1 
ATOM   1207 C  CB  . THR   A 1 178 ? -7.76511  -30.49499 23.30102  1.000 27.38416 ? 177 THR   A CB  1 
ATOM   1208 O  OG1 . THR   A 1 178 ? -6.41188  -30.64571 23.76026  1.000 30.78482 ? 177 THR   A OG1 1 
ATOM   1209 C  CG2 . THR   A 1 178 ? -8.06199  -31.52150 22.21291  1.000 29.10624 ? 177 THR   A CG2 1 
ATOM   1210 N  N   . GLU   A 1 179 ? -8.07618  -28.19433 25.05873  1.000 26.60569 ? 178 GLU   A N   1 
ATOM   1211 C  CA  . GLU   A 1 179 ? -7.65468  -27.32467 26.15436  1.000 29.36683 ? 178 GLU   A CA  1 
ATOM   1212 C  C   . GLU   A 1 179 ? -6.17574  -27.48086 26.47176  1.000 36.84052 ? 178 GLU   A C   1 
ATOM   1213 O  O   . GLU   A 1 179 ? -5.57780  -26.56685 27.05490  1.000 35.07271 ? 178 GLU   A O   1 
ATOM   1214 C  CB  . GLU   A 1 179 ? -8.49755  -27.59270 27.40846  1.000 32.44223 ? 178 GLU   A CB  1 
ATOM   1215 C  CG  . GLU   A 1 179 ? -8.38807  -29.00845 27.94667  1.000 37.37596 ? 178 GLU   A CG  1 
ATOM   1216 C  CD  . GLU   A 1 179 ? -7.16815  -29.20531 28.83210  0.000 42.06125 ? 178 GLU   A CD  1 
ATOM   1217 O  OE1 . GLU   A 1 179 ? -6.64512  -28.20977 29.37693  1.000 56.40651 ? 178 GLU   A OE1 1 
ATOM   1218 O  OE2 . GLU   A 1 179 ? -6.71713  -30.35867 28.96782  1.000 52.54690 ? 178 GLU   A OE2 1 
ATOM   1219 N  N   . ALA   A 1 180 ? -5.56317  -28.60677 26.09274  1.000 29.29688 ? 179 ALA   A N   1 
ATOM   1220 C  CA  . ALA   A 1 180 ? -4.13655  -28.78807 26.32897  1.000 30.54975 ? 179 ALA   A CA  1 
ATOM   1221 C  C   . ALA   A 1 180 ? -3.26492  -28.11031 25.28507  1.000 32.15858 ? 179 ALA   A C   1 
ATOM   1222 O  O   . ALA   A 1 180 ? -2.04423  -28.04934 25.46572  1.000 36.78341 ? 179 ALA   A O   1 
ATOM   1223 C  CB  . ALA   A 1 180 ? -3.79347  -30.28048 26.37268  1.000 36.59345 ? 179 ALA   A CB  1 
ATOM   1224 N  N   . SER   A 1 181 ? -3.84562  -27.62492 24.19381  1.000 32.83059 ? 180 SER   A N   1 
ATOM   1225 C  CA  . SER   A 1 181 ? -3.08875  -26.91226 23.18224  1.000 26.66084 ? 180 SER   A CA  1 
ATOM   1226 C  C   . SER   A 1 181 ? -2.83514  -25.47673 23.64657  1.000 27.00170 ? 180 SER   A C   1 
ATOM   1227 O  O   . SER   A 1 181 ? -3.54719  -24.93516 24.49588  1.000 37.07682 ? 180 SER   A O   1 
ATOM   1228 C  CB  . SER   A 1 181 ? -3.84625  -26.90324 21.84709  1.000 30.34613 ? 180 SER   A CB  1 
ATOM   1229 O  OG  . SER   A 1 181 ? -4.31978  -28.19525 21.48485  1.000 29.94393 ? 180 SER   A OG  1 
ATOM   1230 N  N   . GLY   A 1 182 ? -1.82296  -24.85483 23.07523  1.000 32.70527 ? 181 GLY   A N   1 
ATOM   1231 C  CA  . GLY   A 1 182 ? -1.60365  -23.45845 23.37822  1.000 36.52397 ? 181 GLY   A CA  1 
ATOM   1232 C  C   . GLY   A 1 182 ? -2.71167  -22.62819 22.76228  1.000 37.08522 ? 181 GLY   A C   1 
ATOM   1233 O  O   . GLY   A 1 182 ? -3.53424  -23.13538 21.99295  1.000 32.33354 ? 181 GLY   A O   1 
ATOM   1234 N  N   . PRO   A 1 183 ? -2.76607  -21.34162 23.09272  1.000 24.44180 ? 182 PRO   A N   1 
ATOM   1235 C  CA  . PRO   A 1 183 ? -3.62157  -20.42877 22.32620  1.000 25.90704 ? 182 PRO   A CA  1 
ATOM   1236 C  C   . PRO   A 1 183 ? -3.21332  -20.36031 20.85975  1.000 27.32301 ? 182 PRO   A C   1 
ATOM   1237 O  O   . PRO   A 1 183 ? -2.04798  -20.56532 20.49689  1.000 27.49602 ? 182 PRO   A O   1 
ATOM   1238 C  CB  . PRO   A 1 183 ? -3.42037  -19.07604 23.02032  1.000 26.11716 ? 182 PRO   A CB  1 
ATOM   1239 C  CG  . PRO   A 1 183 ? -2.25196  -19.24377 23.89434  1.000 36.26492 ? 182 PRO   A CG  1 
ATOM   1240 C  CD  . PRO   A 1 183 ? -2.15376  -20.67813 24.25305  1.000 25.93200 ? 182 PRO   A CD  1 
ATOM   1241 N  N   . CYS   A 1 184 ? -4.20425  -20.06590 20.01955  1.000 22.24786 ? 183 CYS   A N   1 
ATOM   1242 C  CA  . CYS   A 1 184 ? -4.01190  -19.79951 18.59778  1.000 23.19671 ? 183 CYS   A CA  1 
ATOM   1243 C  C   . CYS   A 1 184 ? -4.13967  -18.30886 18.35107  1.000 25.90390 ? 183 CYS   A C   1 
ATOM   1244 O  O   . CYS   A 1 184 ? -5.04903  -17.66800 18.88600  1.000 27.90386 ? 183 CYS   A O   1 
ATOM   1245 C  CB  . CYS   A 1 184 ? -5.04944  -20.51187 17.74873  1.000 24.50877 ? 183 CYS   A CB  1 
ATOM   1246 S  SG  . CYS   A 1 184 ? -4.86091  -22.28030 17.85100  1.000 33.79359 ? 183 CYS   A SG  1 
ATOM   1247 N  N   . ILE   A 1 185 ? -3.23711  -17.76921 17.53787  1.000 22.94124 ? 184 ILE   A N   1 
ATOM   1248 C  CA  . ILE   A 1 185 ? -3.14869  -16.33943 17.27217  1.000 23.56815 ? 184 ILE   A CA  1 
ATOM   1249 C  C   . ILE   A 1 185 ? -3.44264  -16.11566 15.79738  1.000 26.47678 ? 184 ILE   A C   1 
ATOM   1250 O  O   . ILE   A 1 185 ? -3.02021  -16.90033 14.94149  1.000 28.87298 ? 184 ILE   A O   1 
ATOM   1251 C  CB  . ILE   A 1 185 ? -1.74755  -15.78496 17.60351  1.000 26.46207 ? 184 ILE   A CB  1 
ATOM   1252 C  CG1 . ILE   A 1 185 ? -1.39853  -15.97666 19.07586  1.000 39.01411 ? 184 ILE   A CG1 1 
ATOM   1253 C  CG2 . ILE   A 1 185 ? -1.66418  -14.29158 17.27552  1.000 34.59987 ? 184 ILE   A CG2 1 
ATOM   1254 C  CD1 . ILE   A 1 185 ? -2.55144  -15.92396 19.98704  1.000 39.33672 ? 184 ILE   A CD1 1 
ATOM   1255 N  N   . LEU   A 1 186 ? -4.12609  -15.02871 15.49268  1.000 24.17508 ? 185 LEU   A N   1 
ATOM   1256 C  CA  . LEU   A 1 186 ? -4.18223  -14.54691 14.12692  1.000 23.05649 ? 185 LEU   A CA  1 
ATOM   1257 C  C   . LEU   A 1 186 ? -3.87679  -13.05420 14.13147  1.000 25.84556 ? 185 LEU   A C   1 
ATOM   1258 O  O   . LEU   A 1 186 ? -3.96220  -12.38473 15.16704  1.000 23.64469 ? 185 LEU   A O   1 
ATOM   1259 C  CB  . LEU   A 1 186 ? -5.55716  -14.84311 13.47117  1.000 23.90022 ? 185 LEU   A CB  1 
ATOM   1260 C  CG  . LEU   A 1 186 ? -6.78281  -14.18982 14.09374  1.000 22.98390 ? 185 LEU   A CG  1 
ATOM   1261 C  CD1 . LEU   A 1 186 ? -7.00749  -12.75386 13.57359  1.000 23.95088 ? 185 LEU   A CD1 1 
ATOM   1262 C  CD2 . LEU   A 1 186 ? -8.00700  -15.08416 13.83314  1.000 26.31569 ? 185 LEU   A CD2 1 
ATOM   1263 N  N   . THR   A 1 187 ? -3.47442  -12.54267 12.97664  1.000 24.34040 ? 186 THR   A N   1 
ATOM   1264 C  CA  . THR   A 1 187 ? -3.11726  -11.14252 12.80753  1.000 22.52206 ? 186 THR   A CA  1 
ATOM   1265 C  C   . THR   A 1 187 ? -3.80014  -10.59826 11.57135  1.000 24.05844 ? 186 THR   A C   1 
ATOM   1266 O  O   . THR   A 1 187 ? -4.41839  -11.34436 10.80749  1.000 25.50496 ? 186 THR   A O   1 
ATOM   1267 C  CB  . THR   A 1 187 ? -1.59704  -10.95777 12.68088  1.000 28.97191 ? 186 THR   A CB  1 
ATOM   1268 O  OG1 . THR   A 1 187 ? -1.19986  -11.34221 11.36454  1.000 29.21490 ? 186 THR   A OG1 1 
ATOM   1269 C  CG2 . THR   A 1 187 ? -0.84602  -11.79808 13.72543  1.000 29.22628 ? 186 THR   A CG2 1 
ATOM   1270 N  N   . PRO   A 1 188 ? -3.69214  -9.28997  11.32700  1.000 26.31820 ? 187 PRO   A N   1 
ATOM   1271 C  CA  . PRO   A 1 188 ? -4.34262  -8.73367  10.13740  1.000 26.72360 ? 187 PRO   A CA  1 
ATOM   1272 C  C   . PRO   A 1 188 ? -3.83513  -9.34318  8.86040   1.000 28.47970 ? 187 PRO   A C   1 
ATOM   1273 O  O   . PRO   A 1 188 ? -4.58752  -9.39778  7.88047   1.000 31.14486 ? 187 PRO   A O   1 
ATOM   1274 C  CB  . PRO   A 1 188 ? -4.01177  -7.23742  10.22034  1.000 30.15922 ? 187 PRO   A CB  1 
ATOM   1275 C  CG  . PRO   A 1 188 ? -3.86849  -6.98664  11.67572  1.000 30.04316 ? 187 PRO   A CG  1 
ATOM   1276 C  CD  . PRO   A 1 188 ? -3.19766  -8.22964  12.22771  1.000 28.92267 ? 187 PRO   A CD  1 
ATOM   1277 N  N   . HIS   A 1 189 ? -2.60206  -9.85335  8.85060   1.000 28.81458 ? 188 HIS   A N   1 
ATOM   1278 C  CA  . HIS   A 1 189 ? -1.96578  -10.28850 7.61906   1.000 32.07212 ? 188 HIS   A CA  1 
ATOM   1279 C  C   . HIS   A 1 189 ? -1.61399  -11.76750 7.59412   1.000 28.62825 ? 188 HIS   A C   1 
ATOM   1280 O  O   . HIS   A 1 189 ? -1.02562  -12.22180 6.60857   1.000 32.44035 ? 188 HIS   A O   1 
ATOM   1281 C  CB  . HIS   A 1 189 ? -0.70559  -9.45553  7.36205   1.000 36.50130 ? 188 HIS   A CB  1 
ATOM   1282 C  CG  . HIS   A 1 189 ? -0.96847  -7.98377  7.34800   1.000 39.11154 ? 188 HIS   A CG  1 
ATOM   1283 N  ND1 . HIS   A 1 189 ? -1.51822  -7.34238  6.25875   1.000 52.65946 ? 188 HIS   A ND1 1 
ATOM   1284 C  CD2 . HIS   A 1 189 ? -0.74287  -7.02553  8.27776   1.000 45.95747 ? 188 HIS   A CD2 1 
ATOM   1285 C  CE1 . HIS   A 1 189 ? -1.64189  -6.05529  6.52757   1.000 56.31918 ? 188 HIS   A CE1 1 
ATOM   1286 N  NE2 . HIS   A 1 189 ? -1.17232  -5.83508  7.74320   1.000 58.56799 ? 188 HIS   A NE2 1 
ATOM   1287 N  N   . ARG   A 1 190 ? -1.95211  -12.53484 8.62866   1.000 27.28803 ? 189 ARG   A N   1 
ATOM   1288 C  CA  . ARG   A 1 190 ? -1.61627  -13.95220 8.61130   1.000 29.07032 ? 189 ARG   A CA  1 
ATOM   1289 C  C   . ARG   A 1 190 ? -2.63311  -14.75400 9.40770   1.000 26.89295 ? 189 ARG   A C   1 
ATOM   1290 O  O   . ARG   A 1 190 ? -2.99825  -14.37522 10.52715  1.000 25.51386 ? 189 ARG   A O   1 
ATOM   1291 C  CB  . ARG   A 1 190 ? -0.22407  -14.19978 9.17666   1.000 30.90003 ? 189 ARG   A CB  1 
ATOM   1292 C  CG  . ARG   A 1 190 ? 0.32794   -15.53534 8.75009   1.000 34.07004 ? 189 ARG   A CG  1 
ATOM   1293 C  CD  . ARG   A 1 190 ? 1.67762   -15.75901 9.37477   1.000 39.75005 ? 189 ARG   A CD  1 
ATOM   1294 N  NE  . ARG   A 1 190 ? 2.23839   -17.04109 8.97458   1.000 35.39809 ? 189 ARG   A NE  1 
ATOM   1295 C  CZ  . ARG   A 1 190 ? 3.00285   -17.22000 7.90639   1.000 41.36487 ? 189 ARG   A CZ  1 
ATOM   1296 N  NH1 . ARG   A 1 190 ? 3.30699   -16.21614 7.09537   1.000 38.99442 ? 189 ARG   A NH1 1 
ATOM   1297 N  NH2 . ARG   A 1 190 ? 3.48065   -18.43352 7.64991   1.000 44.46174 ? 189 ARG   A NH2 1 
ATOM   1298 N  N   . ASP   A 1 191 ? -3.05838  -15.87961 8.82727   1.000 25.71400 ? 190 ASP   A N   1 
ATOM   1299 C  CA  . ASP   A 1 191 ? -4.12239  -16.71561 9.38006   1.000 21.98300 ? 190 ASP   A CA  1 
ATOM   1300 C  C   . ASP   A 1 191 ? -5.37859  -15.90283 9.65679   1.000 21.57681 ? 190 ASP   A C   1 
ATOM   1301 O  O   . ASP   A 1 191 ? -6.14524  -16.20436 10.58593  1.000 23.30787 ? 190 ASP   A O   1 
ATOM   1302 C  CB  . ASP   A 1 191 ? -3.65694  -17.42991 10.65112  1.000 23.81913 ? 190 ASP   A CB  1 
ATOM   1303 C  CG  . ASP   A 1 191 ? -2.46956  -18.32686 10.41149  1.000 30.27168 ? 190 ASP   A CG  1 
ATOM   1304 O  OD1 . ASP   A 1 191 ? -2.51506  -19.14015 9.46759   1.000 27.22974 ? 190 ASP   A OD1 1 
ATOM   1305 O  OD2 . ASP   A 1 191 ? -1.48329  -18.21836 11.16883  1.000 30.81189 ? 190 ASP   A OD2 1 
ATOM   1306 N  N   . ASN   A 1 192 ? -5.61486  -14.87787 8.84425   1.000 21.14302 ? 191 ASN   A N   1 
ATOM   1307 C  CA  . ASN   A 1 192 ? -6.72073  -13.96468 9.11237   1.000 19.29784 ? 191 ASN   A CA  1 
ATOM   1308 C  C   . ASN   A 1 192 ? -8.08067  -14.57092 8.83020   1.000 21.52824 ? 191 ASN   A C   1 
ATOM   1309 O  O   . ASN   A 1 192 ? -9.08468  -14.03367 9.30253   1.000 22.71874 ? 191 ASN   A O   1 
ATOM   1310 C  CB  . ASN   A 1 192 ? -6.56453  -12.66892 8.31268   1.000 21.98624 ? 191 ASN   A CB  1 
ATOM   1311 C  CG  . ASN   A 1 192 ? -7.49726  -11.57983 8.79276   1.000 21.94608 ? 191 ASN   A CG  1 
ATOM   1312 O  OD1 . ASN   A 1 192 ? -8.51337  -11.28907 8.16435   1.000 24.58316 ? 191 ASN   A OD1 1 
ATOM   1313 N  ND2 . ASN   A 1 192 ? -7.15395  -10.97327 9.92341   1.000 21.97824 ? 191 ASN   A ND2 1 
ATOM   1314 N  N   . LEU   A 1 193 ? -8.15868  -15.62173 8.02271   1.000 21.33622 ? 192 LEU   A N   1 
ATOM   1315 C  CA  . LEU   A 1 193 ? -9.40132  -16.33910 7.79755   1.000 20.06376 ? 192 LEU   A CA  1 
ATOM   1316 C  C   . LEU   A 1 193 ? -9.33981  -17.64279 8.57761   1.000 20.11024 ? 192 LEU   A C   1 
ATOM   1317 O  O   . LEU   A 1 193 ? -8.34405  -18.35580 8.51033   1.000 23.94430 ? 192 LEU   A O   1 
ATOM   1318 C  CB  . LEU   A 1 193 ? -9.59594  -16.62611 6.30071   1.000 22.34504 ? 192 LEU   A CB  1 
ATOM   1319 C  CG  . LEU   A 1 193 ? -10.21119 -15.49528 5.48048   1.000 24.78515 ? 192 LEU   A CG  1 
ATOM   1320 C  CD1 . LEU   A 1 193 ? -9.27918  -14.29844 5.48228   1.000 28.46625 ? 192 LEU   A CD1 1 
ATOM   1321 C  CD2 . LEU   A 1 193 ? -10.48424 -15.96092 4.03509   1.000 25.75358 ? 192 LEU   A CD2 1 
ATOM   1322 N  N   . HIS   A 1 194 ? -10.38572 -17.95767 9.33591   1.000 20.18311 ? 193 HIS   A N   1 
ATOM   1323 C  CA  . HIS   A 1 194 ? -10.40452 -19.28986 9.93607   1.000 20.27948 ? 193 HIS   A CA  1 
ATOM   1324 C  C   . HIS   A 1 194 ? -11.81820 -19.84468 9.98446   1.000 20.52124 ? 193 HIS   A C   1 
ATOM   1325 O  O   . HIS   A 1 194 ? -12.80887 -19.10482 9.93985   1.000 20.70096 ? 193 HIS   A O   1 
ATOM   1326 C  CB  . HIS   A 1 194 ? -9.72523  -19.36011 11.33828  1.000 22.38187 ? 193 HIS   A CB  1 
ATOM   1327 C  CG  . HIS   A 1 194 ? -10.36528 -18.53952 12.42586  1.000 20.31130 ? 193 HIS   A CG  1 
ATOM   1328 N  ND1 . HIS   A 1 194 ? -9.74208  -18.34175 13.64150  1.000 21.73278 ? 193 HIS   A ND1 1 
ATOM   1329 C  CD2 . HIS   A 1 194 ? -11.54052 -17.86568 12.49540  1.000 21.04836 ? 193 HIS   A CD2 1 
ATOM   1330 C  CE1 . HIS   A 1 194 ? -10.50008 -17.57737 14.40829  1.000 22.41198 ? 193 HIS   A CE1 1 
ATOM   1331 N  NE2 . HIS   A 1 194 ? -11.59839 -17.27506 13.73809  1.000 20.40610 ? 193 HIS   A NE2 1 
ATOM   1332 N  N   . GLN   A 1 195 ? -11.88057 -21.17841 9.98160   1.000 22.28352 ? 194 GLN   A N   1 
ATOM   1333 C  CA  . GLN   A 1 195 ? -13.10173 -21.95237 10.16976  1.000 21.21021 ? 194 GLN   A CA  1 
ATOM   1334 C  C   . GLN   A 1 195 ? -12.89379 -22.82559 11.39527  1.000 20.50886 ? 194 GLN   A C   1 
ATOM   1335 O  O   . GLN   A 1 195 ? -11.80750 -23.37342 11.57416  1.000 22.77976 ? 194 GLN   A O   1 
ATOM   1336 C  CB  . GLN   A 1 195 ? -13.37605 -22.83739 8.96017   1.000 22.52291 ? 194 GLN   A CB  1 
ATOM   1337 C  CG  . GLN   A 1 195 ? -14.52722 -23.78898 9.14093   1.000 23.27401 ? 194 GLN   A CG  1 
ATOM   1338 C  CD  . GLN   A 1 195 ? -14.86212 -24.52826 7.85823   1.000 34.40497 ? 194 GLN   A CD  1 
ATOM   1339 O  OE1 . GLN   A 1 195 ? -14.69883 -23.99851 6.76360   1.000 36.90462 ? 194 GLN   A OE1 1 
ATOM   1340 N  NE2 . GLN   A 1 195 ? -15.33583 -25.75880 7.99190   1.000 33.29486 ? 194 GLN   A NE2 1 
ATOM   1341 N  N   . ILE   A 1 196 ? -13.92562 -22.97835 12.22932  1.000 18.48937 ? 195 ILE   A N   1 
ATOM   1342 C  CA  . ILE   A 1 196 ? -13.79887 -23.70851 13.48754  1.000 19.17718 ? 195 ILE   A CA  1 
ATOM   1343 C  C   . ILE   A 1 196 ? -14.89385 -24.77249 13.54607  1.000 20.97349 ? 195 ILE   A C   1 
ATOM   1344 O  O   . ILE   A 1 196 ? -16.08575 -24.43506 13.54456  1.000 21.23926 ? 195 ILE   A O   1 
ATOM   1345 C  CB  . ILE   A 1 196 ? -13.87910 -22.76634 14.69523  1.000 20.54643 ? 195 ILE   A CB  1 
ATOM   1346 C  CG1 . ILE   A 1 196 ? -12.80009 -21.69438 14.57300  1.000 23.51635 ? 195 ILE   A CG1 1 
ATOM   1347 C  CG2 . ILE   A 1 196 ? -13.69831 -23.54482 15.99862  1.000 20.00548 ? 195 ILE   A CG2 1 
ATOM   1348 C  CD1 . ILE   A 1 196 ? -13.15232 -20.41796 15.25580  1.000 24.57481 ? 195 ILE   A CD1 1 
ATOM   1349 N  N   . ASP   A 1 197 ? -14.49253 -26.04493 13.57635  1.000 19.24902 ? 196 ASP   A N   1 
ATOM   1350 C  CA  . ASP   A 1 197 ? -15.43226 -27.17358 13.56936  1.000 21.09539 ? 196 ASP   A CA  1 
ATOM   1351 C  C   . ASP   A 1 197 ? -15.39173 -27.87657 14.91797  1.000 24.50951 ? 196 ASP   A C   1 
ATOM   1352 O  O   . ASP   A 1 197 ? -14.30697 -28.21475 15.40310  1.000 22.63120 ? 196 ASP   A O   1 
ATOM   1353 C  CB  . ASP   A 1 197 ? -15.09738 -28.21858 12.49947  1.000 23.25276 ? 196 ASP   A CB  1 
ATOM   1354 C  CG  . ASP   A 1 197 ? -14.88253 -27.63887 11.12200  1.000 26.32795 ? 196 ASP   A CG  1 
ATOM   1355 O  OD1 . ASP   A 1 197 ? -15.67704 -26.78207 10.70424  1.000 27.43282 ? 196 ASP   A OD1 1 
ATOM   1356 O  OD2 . ASP   A 1 197 ? -13.92753 -28.09162 10.44500  1.000 31.00328 ? 196 ASP   A OD2 1 
ATOM   1357 N  N   . ALA   A 1 198 ? -16.56461 -28.14147 15.50255  1.000 19.89632 ? 197 ALA   A N   1 
ATOM   1358 C  CA  . ALA   A 1 198 ? -16.60677 -28.97311 16.70223  1.000 20.84385 ? 197 ALA   A CA  1 
ATOM   1359 C  C   . ALA   A 1 198 ? -16.41041 -30.43403 16.31021  1.000 26.52481 ? 197 ALA   A C   1 
ATOM   1360 O  O   . ALA   A 1 198 ? -17.14683 -30.96112 15.47856  1.000 25.55659 ? 197 ALA   A O   1 
ATOM   1361 C  CB  . ALA   A 1 198 ? -17.93501 -28.79125 17.43065  1.000 22.46303 ? 197 ALA   A CB  1 
ATOM   1362 N  N   . VAL   A 1 199 ? -15.41109 -31.07847 16.91029  1.000 25.35572 ? 198 VAL   A N   1 
ATOM   1363 C  CA  . VAL   A 1 199 ? -14.99780 -32.43635 16.56890  1.000 24.81674 ? 198 VAL   A CA  1 
ATOM   1364 C  C   . VAL   A 1 199 ? -15.47550 -33.38406 17.66349  1.000 23.95891 ? 198 VAL   A C   1 
ATOM   1365 O  O   . VAL   A 1 199 ? -15.12267 -33.22146 18.83688  1.000 28.57474 ? 198 VAL   A O   1 
ATOM   1366 C  CB  . VAL   A 1 199 ? -13.47316 -32.52582 16.40395  1.000 27.31737 ? 198 VAL   A CB  1 
ATOM   1367 C  CG1 . VAL   A 1 199 ? -13.04805 -33.97618 16.17894  1.000 30.26455 ? 198 VAL   A CG1 1 
ATOM   1368 C  CG2 . VAL   A 1 199 ? -12.99599 -31.63869 15.25487  1.000 29.02962 ? 198 VAL   A CG2 1 
ATOM   1369 N  N   . GLU   A 1 200 ? -16.24823 -34.39570 17.27346  1.000 28.05336 ? 199 GLU   A N   1 
ATOM   1370 C  CA  . GLU   A 1 200 ? -16.65964 -35.46853 18.18776  1.000 33.74920 ? 199 GLU   A CA  1 
ATOM   1371 C  C   . GLU   A 1 200 ? -17.35911 -34.92701 19.43597  1.000 33.22226 ? 199 GLU   A C   1 
ATOM   1372 O  O   . GLU   A 1 200 ? -17.15084 -35.41713 20.54825  1.000 34.04320 ? 199 GLU   A O   1 
ATOM   1373 C  CB  . GLU   A 1 200 ? -15.46609 -36.34154 18.58305  1.000 46.30563 ? 199 GLU   A CB  1 
ATOM   1374 C  CG  . GLU   A 1 200 ? -14.63486 -36.82164 17.40817  0.736 43.22473 ? 199 GLU   A CG  1 
ATOM   1375 C  CD  . GLU   A 1 200 ? -14.02028 -38.18233 17.65492  1.000 58.91627 ? 199 GLU   A CD  1 
ATOM   1376 O  OE1 . GLU   A 1 200 ? -13.50117 -38.40764 18.76913  0.790 63.40381 ? 199 GLU   A OE1 1 
ATOM   1377 O  OE2 . GLU   A 1 200 ? -14.05147 -39.02432 16.73124  0.602 60.71754 ? 199 GLU   A OE2 1 
ATOM   1378 N  N   . GLY   A 1 201 ? -18.19786 -33.91323 19.26009  1.000 26.14991 ? 200 GLY   A N   1 
ATOM   1379 C  CA  . GLY   A 1 201 ? -19.02184 -33.43446 20.35000  1.000 23.25611 ? 200 GLY   A CA  1 
ATOM   1380 C  C   . GLY   A 1 201 ? -18.91529 -31.92895 20.52539  1.000 23.03700 ? 200 GLY   A C   1 
ATOM   1381 O  O   . GLY   A 1 201 ? -18.20779 -31.25652 19.77253  1.000 22.91302 ? 200 GLY   A O   1 
ATOM   1382 N  N   . PRO   A 1 202 ? -19.59588 -31.38188 21.53384  1.000 21.19908 ? 201 PRO   A N   1 
ATOM   1383 C  CA  . PRO   A 1 202 ? -19.55074 -29.93132 21.76929  1.000 19.32369 ? 201 PRO   A CA  1 
ATOM   1384 C  C   . PRO   A 1 202 ? -18.15295 -29.45369 22.13461  1.000 18.69911 ? 201 PRO   A C   1 
ATOM   1385 O  O   . PRO   A 1 202 ? -17.30890 -30.19864 22.65014  1.000 22.36292 ? 201 PRO   A O   1 
ATOM   1386 C  CB  . PRO   A 1 202 ? -20.51751 -29.71697 22.94529  1.000 22.61253 ? 201 PRO   A CB  1 
ATOM   1387 C  CG  . PRO   A 1 202 ? -21.35109 -30.97767 23.03124  1.000 23.58756 ? 201 PRO   A CG  1 
ATOM   1388 C  CD  . PRO   A 1 202 ? -20.44026 -32.08096 22.51772  1.000 23.49499 ? 201 PRO   A CD  1 
ATOM   1389 N  N   . ALA   A 1 203 ? -17.92309 -28.16579 21.89645  1.000 19.00767 ? 202 ALA   A N   1 
ATOM   1390 C  CA  . ALA   A 1 203 ? -16.63974 -27.57194 22.23792  1.000 17.56950 ? 202 ALA   A CA  1 
ATOM   1391 C  C   . ALA   A 1 203 ? -16.87249 -26.10978 22.55161  1.000 20.28778 ? 202 ALA   A C   1 
ATOM   1392 O  O   . ALA   A 1 203 ? -17.90301 -25.54245 22.18570  1.000 19.89007 ? 202 ALA   A O   1 
ATOM   1393 C  CB  . ALA   A 1 203 ? -15.63934 -27.70819 21.08051  1.000 17.71753 ? 202 ALA   A CB  1 
ATOM   1394 N  N   . ALA   A 1 204 ? -15.90280 -25.48959 23.22424  1.000 18.29514 ? 203 ALA   A N   1 
ATOM   1395 C  CA  . ALA   A 1 204 ? -16.02126 -24.05977 23.49718  1.000 18.19275 ? 203 ALA   A CA  1 
ATOM   1396 C  C   . ALA   A 1 204 ? -14.63298 -23.45374 23.51916  1.000 19.71915 ? 203 ALA   A C   1 
ATOM   1397 O  O   . ALA   A 1 204 ? -13.65299 -24.13296 23.86072  1.000 20.75289 ? 203 ALA   A O   1 
ATOM   1398 C  CB  . ALA   A 1 204 ? -16.73689 -23.78320 24.83269  1.000 18.28084 ? 203 ALA   A CB  1 
ATOM   1399 N  N   . PHE   A 1 205 ? -14.55150 -22.16699 23.17224  1.000 17.65488 ? 204 PHE   A N   1 
ATOM   1400 C  CA  . PHE   A 1 205 ? -13.27381 -21.47979 23.24931  1.000 15.81162 ? 204 PHE   A CA  1 
ATOM   1401 C  C   . PHE   A 1 205 ? -13.45632 -20.04403 23.70947  1.000 18.42116 ? 204 PHE   A C   1 
ATOM   1402 O  O   . PHE   A 1 205 ? -14.46372 -19.38834 23.42271  1.000 17.82819 ? 204 PHE   A O   1 
ATOM   1403 C  CB  . PHE   A 1 205 ? -12.50484 -21.48637 21.90581  1.000 17.25701 ? 204 PHE   A CB  1 
ATOM   1404 C  CG  . PHE   A 1 205 ? -13.23442 -20.85698 20.74640  1.000 19.59811 ? 204 PHE   A CG  1 
ATOM   1405 C  CD1 . PHE   A 1 205 ? -14.06911 -21.62247 19.92629  1.000 19.92465 ? 204 PHE   A CD1 1 
ATOM   1406 C  CD2 . PHE   A 1 205 ? -13.03145 -19.51361 20.42172  1.000 18.13997 ? 204 PHE   A CD2 1 
ATOM   1407 C  CE1 . PHE   A 1 205 ? -14.72566 -21.02644 18.80234  1.000 18.14905 ? 204 PHE   A CE1 1 
ATOM   1408 C  CE2 . PHE   A 1 205 ? -13.67229 -18.93234 19.31534  1.000 20.05489 ? 204 PHE   A CE2 1 
ATOM   1409 C  CZ  . PHE   A 1 205 ? -14.52860 -19.69926 18.53185  1.000 18.11860 ? 204 PHE   A CZ  1 
ATOM   1410 N  N   . LEU   A 1 206 ? -12.44124 -19.56739 24.43207  1.000 16.78700 ? 205 LEU   A N   1 
ATOM   1411 C  CA  A LEU   A 1 206 ? -12.28494 -18.15243 24.74639  0.442 17.96572 ? 205 LEU   A CA  1 
ATOM   1412 C  CA  B LEU   A 1 206 ? -12.33661 -18.14454 24.72286  0.558 17.90755 ? 205 LEU   A CA  1 
ATOM   1413 C  C   . LEU   A 1 206 ? -11.71157 -17.43846 23.52756  1.000 16.49075 ? 205 LEU   A C   1 
ATOM   1414 O  O   . LEU   A 1 206 ? -10.76081 -17.93654 22.91608  1.000 20.36670 ? 205 LEU   A O   1 
ATOM   1415 C  CB  A LEU   A 1 206 ? -11.33677 -18.02185 25.93941  0.442 19.35035 ? 205 LEU   A CB  1 
ATOM   1416 C  CB  B LEU   A 1 206 ? -11.48598 -17.90420 25.96865  0.558 19.12913 ? 205 LEU   A CB  1 
ATOM   1417 C  CG  A LEU   A 1 206 ? -10.99635 -16.74461 26.70588  0.442 22.85044 ? 205 LEU   A CG  1 
ATOM   1418 C  CG  B LEU   A 1 206 ? -11.30975 -16.43700 26.34825  0.558 16.01201 ? 205 LEU   A CG  1 
ATOM   1419 C  CD1 A LEU   A 1 206 ? -10.38966 -15.68694 25.78702  0.442 21.05277 ? 205 LEU   A CD1 1 
ATOM   1420 C  CD1 B LEU   A 1 206 ? -12.45138 -15.96820 27.21743  0.558 25.17189 ? 205 LEU   A CD1 1 
ATOM   1421 C  CD2 A LEU   A 1 206 ? -12.15466 -16.22630 27.53366  0.442 21.30486 ? 205 LEU   A CD2 1 
ATOM   1422 C  CD2 B LEU   A 1 206 ? -9.94619  -16.20528 27.00840  0.558 25.99484 ? 205 LEU   A CD2 1 
ATOM   1423 N  N   . ASP   A 1 207 ? -12.28005 -16.28058 23.16251  1.000 16.58141 ? 206 ASP   A N   1 
ATOM   1424 C  CA  . ASP   A 1 207 ? -11.77374 -15.51923 22.02027  1.000 17.75873 ? 206 ASP   A CA  1 
ATOM   1425 C  C   . ASP   A 1 207 ? -11.51049 -14.07963 22.42755  1.000 20.37154 ? 206 ASP   A C   1 
ATOM   1426 O  O   . ASP   A 1 207 ? -12.34278 -13.45785 23.09126  1.000 20.05840 ? 206 ASP   A O   1 
ATOM   1427 C  CB  . ASP   A 1 207 ? -12.74376 -15.53579 20.82952  1.000 20.77084 ? 206 ASP   A CB  1 
ATOM   1428 C  CG  . ASP   A 1 207 ? -12.01270 -15.42730 19.46381  1.000 28.54908 ? 206 ASP   A CG  1 
ATOM   1429 O  OD1 . ASP   A 1 207 ? -10.74756 -15.32052 19.40820  0.559 22.46907 ? 206 ASP   A OD1 1 
ATOM   1430 O  OD2 . ASP   A 1 207 ? -12.70748 -15.44397 18.42630  0.577 26.16746 ? 206 ASP   A OD2 1 
ATOM   1431 N  N   . ILE   A 1 208 ? -10.34233 -13.57044 22.04299  1.000 18.50577 ? 207 ILE   A N   1 
ATOM   1432 C  CA  . ILE   A 1 208 ? -9.98218  -12.16299 22.19156  1.000 19.08227 ? 207 ILE   A CA  1 
ATOM   1433 C  C   . ILE   A 1 208 ? -9.82238  -11.58097 20.79701  1.000 18.44267 ? 207 ILE   A C   1 
ATOM   1434 O  O   . ILE   A 1 208 ? -9.08228  -12.13899 19.98018  1.000 22.64942 ? 207 ILE   A O   1 
ATOM   1435 C  CB  . ILE   A 1 208 ? -8.67263  -11.99736 22.97963  1.000 21.35491 ? 207 ILE   A CB  1 
ATOM   1436 C  CG1 . ILE   A 1 208 ? -8.84757  -12.62566 24.36234  1.000 24.07204 ? 207 ILE   A CG1 1 
ATOM   1437 C  CG2 . ILE   A 1 208 ? -8.27466  -10.52527 23.08135  1.000 23.23264 ? 207 ILE   A CG2 1 
ATOM   1438 C  CD1 . ILE   A 1 208 ? -7.59822  -12.61450 25.20604  1.000 28.76729 ? 207 ILE   A CD1 1 
ATOM   1439 N  N   . LEU   A 1 209 ? -10.51978 -10.47039 20.51721  1.000 19.00813 ? 208 LEU   A N   1 
ATOM   1440 C  CA  . LEU   A 1 209 ? -10.40721 -9.78790  19.23295  1.000 19.05290 ? 208 LEU   A CA  1 
ATOM   1441 C  C   . LEU   A 1 209 ? -9.92063  -8.36870  19.47405  1.000 23.87609 ? 208 LEU   A C   1 
ATOM   1442 O  O   . LEU   A 1 209 ? -10.43050 -7.68695  20.37103  1.000 24.70217 ? 208 LEU   A O   1 
ATOM   1443 C  CB  . LEU   A 1 209 ? -11.74452 -9.74243  18.50229  1.000 21.88568 ? 208 LEU   A CB  1 
ATOM   1444 C  CG  . LEU   A 1 209 ? -12.40030 -11.07852 18.24113  1.000 23.95039 ? 208 LEU   A CG  1 
ATOM   1445 C  CD1 . LEU   A 1 209 ? -13.85514 -10.84670 17.86310  1.000 32.21701 ? 208 LEU   A CD1 1 
ATOM   1446 C  CD2 . LEU   A 1 209 ? -11.64435 -11.73820 17.11258  1.000 28.84274 ? 208 LEU   A CD2 1 
ATOM   1447 N  N   . ALA   A 1 210 ? -8.92634  -7.93506  18.69695  1.000 22.26106 ? 209 ALA   A N   1 
ATOM   1448 C  CA  . ALA   A 1 210 ? -8.37234  -6.60147  18.93888  1.000 21.89051 ? 209 ALA   A CA  1 
ATOM   1449 C  C   . ALA   A 1 210 ? -7.97696  -5.89473  17.64792  1.000 23.65440 ? 209 ALA   A C   1 
ATOM   1450 O  O   . ALA   A 1 210 ? -7.08899  -6.36009  16.91458  1.000 25.58181 ? 209 ALA   A O   1 
ATOM   1451 C  CB  . ALA   A 1 210 ? -7.16677  -6.70504  19.88186  1.000 25.97968 ? 209 ALA   A CB  1 
ATOM   1452 N  N   . PRO   A 1 211 ? -8.62406  -4.77180  17.32526  1.000 24.28238 ? 210 PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 211 ? -9.78345  -4.19850  18.01212  1.000 28.00192 ? 210 PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 211 ? -11.00727 -5.07474  17.77186  1.000 28.15435 ? 210 PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 211 ? -10.93506 -6.00995  16.98415  1.000 27.92728 ? 210 PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 211 ? -9.91444  -2.81088  17.36133  1.000 27.77739 ? 210 PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 211 ? -9.37072  -3.00532  15.97962  1.000 31.90603 ? 210 PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 211 ? -8.23116  -3.97492  16.14684  1.000 27.35678 ? 210 PRO   A CD  1 
ATOM   1459 N  N   . PRO   A 1 212 ? -12.13484 -4.79987  18.41790  1.000 28.74645 ? 211 PRO   A N   1 
ATOM   1460 C  CA  . PRO   A 1 212 ? -13.36406 -5.53156  18.09979  1.000 27.22610 ? 211 PRO   A CA  1 
ATOM   1461 C  C   . PRO   A 1 212 ? -13.79241 -5.24033  16.67334  1.000 31.80469 ? 211 PRO   A C   1 
ATOM   1462 O  O   . PRO   A 1 212 ? -13.30351 -4.31637  16.02268  1.000 30.39433 ? 211 PRO   A O   1 
ATOM   1463 C  CB  . PRO   A 1 212 ? -14.38854 -4.98574  19.10150  1.000 31.18069 ? 211 PRO   A CB  1 
ATOM   1464 C  CG  . PRO   A 1 212 ? -13.57296 -4.31502  20.18809  1.000 30.85999 ? 211 PRO   A CG  1 
ATOM   1465 C  CD  . PRO   A 1 212 ? -12.34043 -3.80530  19.48464  1.000 27.75073 ? 211 PRO   A CD  1 
ATOM   1466 N  N   . TYR   A 1 213 ? -14.71656 -6.05459  16.17486  1.000 26.76535 ? 212 TYR   A N   1 
ATOM   1467 C  CA  . TYR   A 1 213 ? -15.33637 -5.69930  14.91190  1.000 27.70774 ? 212 TYR   A CA  1 
ATOM   1468 C  C   . TYR   A 1 213 ? -16.02610 -4.35307  15.07607  1.000 30.38176 ? 212 TYR   A C   1 
ATOM   1469 O  O   . TYR   A 1 213 ? -16.48410 -3.99210  16.16642  1.000 30.20972 ? 212 TYR   A O   1 
ATOM   1470 C  CB  . TYR   A 1 213 ? -16.35790 -6.75690  14.48205  1.000 26.45748 ? 212 TYR   A CB  1 
ATOM   1471 C  CG  . TYR   A 1 213 ? -15.80349 -8.09667  14.00484  1.000 22.97520 ? 212 TYR   A CG  1 
ATOM   1472 C  CD1 . TYR   A 1 213 ? -15.25077 -8.24373  12.72949  1.000 25.85212 ? 212 TYR   A CD1 1 
ATOM   1473 C  CD2 . TYR   A 1 213 ? -15.88991 -9.22910  14.81924  1.000 22.71475 ? 212 TYR   A CD2 1 
ATOM   1474 C  CE1 . TYR   A 1 213 ? -14.76634 -9.47895  12.29609  1.000 23.38861 ? 212 TYR   A CE1 1 
ATOM   1475 C  CE2 . TYR   A 1 213 ? -15.40320 -10.46804 14.39587  1.000 23.45769 ? 212 TYR   A CE2 1 
ATOM   1476 C  CZ  . TYR   A 1 213 ? -14.85489 -10.57912 13.13231  1.000 22.86822 ? 212 TYR   A CZ  1 
ATOM   1477 O  OH  . TYR   A 1 213 ? -14.38867 -11.79925 12.71135  1.000 23.94961 ? 212 TYR   A OH  1 
ATOM   1478 N  N   . ASP   A 1 214 ? -16.08804 -3.60030  13.98031  1.000 29.92319 ? 213 ASP   A N   1 
ATOM   1479 C  CA  . ASP   A 1 214 ? -16.80210 -2.32432  13.95264  1.000 33.80588 ? 213 ASP   A CA  1 
ATOM   1480 C  C   . ASP   A 1 214 ? -17.28733 -2.11054  12.53341  1.000 38.01155 ? 213 ASP   A C   1 
ATOM   1481 O  O   . ASP   A 1 214 ? -16.56231 -1.57638  11.68365  1.000 42.17578 ? 213 ASP   A O   1 
ATOM   1482 C  CB  . ASP   A 1 214 ? -15.92549 -1.16342  14.42334  1.000 37.63825 ? 213 ASP   A CB  1 
ATOM   1483 C  CG  . ASP   A 1 214 ? -16.71152 0.12099   14.62379  1.000 50.85667 ? 213 ASP   A CG  1 
ATOM   1484 O  OD1 . ASP   A 1 214 ? -17.90885 0.15287   14.26734  1.000 49.42644 ? 213 ASP   A OD1 1 
ATOM   1485 O  OD2 . ASP   A 1 214 ? -16.13399 1.09499   15.15503  1.000 53.34961 ? 213 ASP   A OD2 1 
ATOM   1486 N  N   . PRO   A 1 215 ? -18.50844 -2.55663  12.22392  1.000 37.26385 ? 214 PRO   A N   1 
ATOM   1487 C  CA  . PRO   A 1 215 ? -19.00370 -2.41471  10.84235  1.000 41.00396 ? 214 PRO   A CA  1 
ATOM   1488 C  C   . PRO   A 1 215 ? -19.02148 -0.97557  10.36035  1.000 44.88065 ? 214 PRO   A C   1 
ATOM   1489 O  O   . PRO   A 1 215 ? -18.70677 -0.71047  9.19439   1.000 48.50378 ? 214 PRO   A O   1 
ATOM   1490 C  CB  . PRO   A 1 215 ? -20.41950 -3.00957  10.91664  1.000 41.53018 ? 214 PRO   A CB  1 
ATOM   1491 C  CG  . PRO   A 1 215 ? -20.38205 -3.93381  12.10537  1.000 38.27078 ? 214 PRO   A CG  1 
ATOM   1492 C  CD  . PRO   A 1 215 ? -19.44322 -3.30189  13.08557  1.000 37.03113 ? 214 PRO   A CD  1 
ATOM   1493 N  N   . ASP   A 1 216 ? -19.37724 -0.03495  11.22936  1.000 46.74711 ? 215 ASP   A N   1 
ATOM   1494 C  CA  . ASP   A 1 216 ? -19.42357 1.36485   10.82179  1.000 56.74715 ? 215 ASP   A CA  1 
ATOM   1495 C  C   . ASP   A 1 216 ? -18.04380 1.95386   10.57808  1.000 57.89351 ? 215 ASP   A C   1 
ATOM   1496 O  O   . ASP   A 1 216 ? -17.95061 3.11613   10.17100  1.000 68.52540 ? 215 ASP   A O   1 
ATOM   1497 C  CB  . ASP   A 1 216 ? -20.16575 2.18294   11.87753  1.000 57.77934 ? 215 ASP   A CB  1 
ATOM   1498 C  CG  . ASP   A 1 216 ? -21.58938 1.70932   12.07502  1.000 62.52533 ? 215 ASP   A CG  1 
ATOM   1499 O  OD1 . ASP   A 1 216 ? -22.19365 1.23300   11.08921  1.000 62.67351 ? 215 ASP   A OD1 1 
ATOM   1500 O  OD2 . ASP   A 1 216 ? -22.10199 1.80732   13.20874  1.000 68.14585 ? 215 ASP   A OD2 1 
ATOM   1501 N  N   . ASP   A 1 217 ? -16.97922 1.18528   10.80852  1.000 54.21274 ? 216 ASP   A N   1 
ATOM   1502 C  CA  . ASP   A 1 217 ? -15.60993 1.65462   10.63803  1.000 53.64473 ? 216 ASP   A CA  1 
ATOM   1503 C  C   . ASP   A 1 217 ? -14.81231 0.77173   9.68258   1.000 60.02872 ? 216 ASP   A C   1 
ATOM   1504 O  O   . ASP   A 1 217 ? -13.57835 0.74318   9.75306   1.000 62.68859 ? 216 ASP   A O   1 
ATOM   1505 C  CB  . ASP   A 1 217 ? -14.91330 1.73620   11.99765  1.000 56.58506 ? 216 ASP   A CB  1 
ATOM   1506 C  CG  . ASP   A 1 217 ? -13.59577 2.48040   11.93648  1.000 76.24392 ? 216 ASP   A CG  1 
ATOM   1507 O  OD1 . ASP   A 1 217 ? -12.58367 1.93333   12.43019  1.000 78.54702 ? 216 ASP   A OD1 1 
ATOM   1508 O  OD2 . ASP   A 1 217 ? -13.57278 3.60708   11.39293  1.000 75.34449 ? 216 ASP   A OD2 1 
ATOM   1509 N  N   . GLY   A 1 218 ? -15.48846 0.03476   8.80296   1.000 58.27798 ? 217 GLY   A N   1 
ATOM   1510 C  CA  . GLY   A 1 218 ? -14.79538 -0.79007  7.83265   1.000 55.00282 ? 217 GLY   A CA  1 
ATOM   1511 C  C   . GLY   A 1 218 ? -14.19741 -2.06977  8.36590   1.000 58.94318 ? 217 GLY   A C   1 
ATOM   1512 O  O   . GLY   A 1 218 ? -13.32646 -2.65072  7.70940   1.000 58.47274 ? 217 GLY   A O   1 
ATOM   1513 N  N   . ARG   A 1 219 ? -14.63102 -2.52903  9.53999   1.000 43.97838 ? 218 ARG   A N   1 
ATOM   1514 C  CA  . ARG   A 1 219 ? -14.17719 -3.78325  10.14435  1.000 42.96093 ? 218 ARG   A CA  1 
ATOM   1515 C  C   . ARG   A 1 219 ? -15.39750 -4.65933  10.38825  1.000 34.29151 ? 218 ARG   A C   1 
ATOM   1516 O  O   . ARG   A 1 219 ? -15.87507 -4.78707  11.51736  1.000 39.47101 ? 218 ARG   A O   1 
ATOM   1517 C  CB  . ARG   A 1 219 ? -13.40207 -3.53727  11.45362  1.000 44.66102 ? 218 ARG   A CB  1 
ATOM   1518 C  CG  . ARG   A 1 219 ? -11.97047 -3.09552  11.26743  1.000 54.97198 ? 218 ARG   A CG  1 
ATOM   1519 C  CD  . ARG   A 1 219 ? -11.17949 -3.32046  12.54339  1.000 36.73497 ? 218 ARG   A CD  1 
ATOM   1520 N  NE  . ARG   A 1 219 ? -11.96074 -3.04773  13.74434  1.000 39.84508 ? 218 ARG   A NE  1 
ATOM   1521 C  CZ  . ARG   A 1 219 ? -12.19907 -1.82915  14.21219  1.000 42.09348 ? 218 ARG   A CZ  1 
ATOM   1522 N  NH1 . ARG   A 1 219 ? -11.80086 -0.74585  13.55770  1.000 48.20254 ? 218 ARG   A NH1 1 
ATOM   1523 N  NH2 . ARG   A 1 219 ? -12.85243 -1.69075  15.36228  1.000 38.81980 ? 218 ARG   A NH2 1 
ATOM   1524 N  N   . ASP   A 1 220 ? -15.90117 -5.27123  9.32742   1.000 32.64856 ? 219 ASP   A N   1 
ATOM   1525 C  CA  . ASP   A 1 220 ? -16.99084 -6.22099  9.46705   1.000 26.67629 ? 219 ASP   A CA  1 
ATOM   1526 C  C   . ASP   A 1 220 ? -16.46379 -7.64414  9.37654   1.000 30.81832 ? 219 ASP   A C   1 
ATOM   1527 O  O   . ASP   A 1 220 ? -15.30153 -7.88780  9.04839   1.000 29.75689 ? 219 ASP   A O   1 
ATOM   1528 C  CB  . ASP   A 1 220 ? -18.06092 -5.98954  8.40056   1.000 29.42355 ? 219 ASP   A CB  1 
ATOM   1529 C  CG  . ASP   A 1 220 ? -19.46805 -6.18462  8.94262   1.000 41.97442 ? 219 ASP   A CG  1 
ATOM   1530 O  OD1 . ASP   A 1 220 ? -19.66782 -7.09915  9.77281   1.000 32.19827 ? 219 ASP   A OD1 1 
ATOM   1531 O  OD2 . ASP   A 1 220 ? -20.37056 -5.40775  8.56084   1.000 40.48853 ? 219 ASP   A OD2 1 
ATOM   1532 N  N   . CYS   A 1 221 ? -17.35586 -8.59024  9.65795   1.000 26.57574 ? 220 CYS   A N   1 
ATOM   1533 C  CA  . CYS   A 1 221 ? -17.06381 -10.01932 9.59133   1.000 23.71103 ? 220 CYS   A CA  1 
ATOM   1534 C  C   . CYS   A 1 221 ? -17.60587 -10.52967 8.26099   1.000 26.95922 ? 220 CYS   A C   1 
ATOM   1535 O  O   . CYS   A 1 221 ? -18.81798 -10.49251 8.03152   1.000 29.01177 ? 220 CYS   A O   1 
ATOM   1536 C  CB  . CYS   A 1 221 ? -17.70728 -10.74141 10.77606  1.000 24.93456 ? 220 CYS   A CB  1 
ATOM   1537 S  SG  . CYS   A 1 221 ? -17.40430 -12.49923 10.81489  1.000 26.08097 ? 220 CYS   A SG  1 
ATOM   1538 N  N   . HIS   A 1 222 ? -16.71450 -10.96026 7.37193   1.000 25.01690 ? 221 HIS   A N   1 
ATOM   1539 C  CA  . HIS   A 1 222 ? -17.10744 -11.51891 6.07721   1.000 25.14353 ? 221 HIS   A CA  1 
ATOM   1540 C  C   . HIS   A 1 222 ? -16.89201 -13.02212 6.06090   1.000 23.58660 ? 221 HIS   A C   1 
ATOM   1541 O  O   . HIS   A 1 222 ? -15.91215 -13.51645 6.61390   1.000 22.95281 ? 221 HIS   A O   1 
ATOM   1542 C  CB  . HIS   A 1 222 ? -16.31295 -10.89776 4.93283   1.000 28.73799 ? 221 HIS   A CB  1 
ATOM   1543 C  CG  . HIS   A 1 222 ? -16.19623 -9.41652  5.03535   1.000 30.99173 ? 221 HIS   A CG  1 
ATOM   1544 N  ND1 . HIS   A 1 222 ? -17.07788 -8.56030  4.41129   1.000 37.55920 ? 221 HIS   A ND1 1 
ATOM   1545 C  CD2 . HIS   A 1 222 ? -15.33413 -8.63771  5.72679   1.000 29.57884 ? 221 HIS   A CD2 1 
ATOM   1546 C  CE1 . HIS   A 1 222 ? -16.75071 -7.31252  4.70082   1.000 40.12152 ? 221 HIS   A CE1 1 
ATOM   1547 N  NE2 . HIS   A 1 222 ? -15.69513 -7.33173  5.49509   1.000 38.00588 ? 221 HIS   A NE2 1 
ATOM   1548 N  N   . TYR   A 1 223 ? -17.78889 -13.73498 5.38628   1.000 24.75950 ? 222 TYR   A N   1 
ATOM   1549 C  CA  . TYR   A 1 223 ? -17.73586 -15.18443 5.28721   1.000 23.73641 ? 222 TYR   A CA  1 
ATOM   1550 C  C   . TYR   A 1 223 ? -17.26791 -15.59202 3.89510   1.000 24.17244 ? 222 TYR   A C   1 
ATOM   1551 O  O   . TYR   A 1 223 ? -17.44257 -14.84515 2.92813   1.000 25.96401 ? 222 TYR   A O   1 
ATOM   1552 C  CB  . TYR   A 1 223 ? -19.10460 -15.81148 5.57806   1.000 23.09796 ? 222 TYR   A CB  1 
ATOM   1553 C  CG  . TYR   A 1 223 ? -19.52737 -15.56086 6.99475   1.000 23.64022 ? 222 TYR   A CG  1 
ATOM   1554 C  CD1 . TYR   A 1 223 ? -19.10892 -16.40388 8.01116   1.000 22.41728 ? 222 TYR   A CD1 1 
ATOM   1555 C  CD2 . TYR   A 1 223 ? -20.32321 -14.47322 7.31303   1.000 25.27484 ? 222 TYR   A CD2 1 
ATOM   1556 C  CE1 . TYR   A 1 223 ? -19.48579 -16.16558 9.32452   1.000 23.02423 ? 222 TYR   A CE1 1 
ATOM   1557 C  CE2 . TYR   A 1 223 ? -20.69625 -14.22462 8.64493   1.000 22.76238 ? 222 TYR   A CE2 1 
ATOM   1558 C  CZ  . TYR   A 1 223 ? -20.26950 -15.07979 9.61916   1.000 21.96733 ? 222 TYR   A CZ  1 
ATOM   1559 O  OH  . TYR   A 1 223 ? -20.63331 -14.84352 10.93750  1.000 23.35553 ? 222 TYR   A OH  1 
ATOM   1560 N  N   . TYR   A 1 224 ? -16.66515 -16.77908 3.80865   1.000 23.65607 ? 223 TYR   A N   1 
ATOM   1561 C  CA  . TYR   A 1 224 ? -16.07207 -17.27257 2.56805   1.000 25.28015 ? 223 TYR   A CA  1 
ATOM   1562 C  C   . TYR   A 1 224 ? -16.35334 -18.75641 2.39736   1.000 28.97135 ? 223 TYR   A C   1 
ATOM   1563 O  O   . TYR   A 1 224 ? -16.57047 -19.48205 3.36828   1.000 25.21540 ? 223 TYR   A O   1 
ATOM   1564 C  CB  . TYR   A 1 224 ? -14.54099 -17.04429 2.54852   1.000 23.87447 ? 223 TYR   A CB  1 
ATOM   1565 C  CG  . TYR   A 1 224 ? -14.15768 -15.59333 2.66161   1.000 25.51256 ? 223 TYR   A CG  1 
ATOM   1566 C  CD1 . TYR   A 1 224 ? -14.09166 -14.97920 3.90562   1.000 26.49580 ? 223 TYR   A CD1 1 
ATOM   1567 C  CD2 . TYR   A 1 224 ? -13.88673 -14.82538 1.53006   1.000 26.20810 ? 223 TYR   A CD2 1 
ATOM   1568 C  CE1 . TYR   A 1 224 ? -13.76429 -13.64872 4.03261   1.000 29.23370 ? 223 TYR   A CE1 1 
ATOM   1569 C  CE2 . TYR   A 1 224 ? -13.54850 -13.48815 1.64635   1.000 31.72331 ? 223 TYR   A CE2 1 
ATOM   1570 C  CZ  . TYR   A 1 224 ? -13.48559 -12.90760 2.90407   1.000 29.79453 ? 223 TYR   A CZ  1 
ATOM   1571 O  OH  . TYR   A 1 224 ? -13.15813 -11.58002 3.04528   1.000 31.88589 ? 223 TYR   A OH  1 
ATOM   1572 N  N   . ARG   A 1 225 ? -16.34174 -19.19983 1.13964   1.000 28.29525 ? 224 ARG   A N   1 
ATOM   1573 C  CA  . ARG   A 1 225 ? -16.29207 -20.60388 0.75884   1.000 26.55706 ? 224 ARG   A CA  1 
ATOM   1574 C  C   . ARG   A 1 225 ? -14.93726 -20.88677 0.11964   1.000 31.64204 ? 224 ARG   A C   1 
ATOM   1575 O  O   . ARG   A 1 225 ? -14.43843 -20.06820 -0.65675  1.000 31.64512 ? 224 ARG   A O   1 
ATOM   1576 C  CB  . ARG   A 1 225 ? -17.38328 -20.93949 -0.28812  1.000 33.37974 ? 224 ARG   A CB  1 
ATOM   1577 C  CG  . ARG   A 1 225 ? -18.81210 -21.00657 0.21353   1.000 46.85029 ? 224 ARG   A CG  1 
ATOM   1578 C  CD  . ARG   A 1 225 ? -19.81731 -21.02604 -0.94531  1.000 48.15673 ? 224 ARG   A CD  1 
ATOM   1579 N  NE  . ARG   A 1 225 ? -19.46508 -21.95661 -2.01362  1.000 52.72377 ? 224 ARG   A NE  1 
ATOM   1580 C  CZ  . ARG   A 1 225 ? -20.02719 -21.96083 -3.21562  1.000 56.99103 ? 224 ARG   A CZ  1 
ATOM   1581 N  NH1 . ARG   A 1 225 ? -20.94986 -21.07312 -3.55043  1.000 47.66932 ? 224 ARG   A NH1 1 
ATOM   1582 N  NH2 . ARG   A 1 225 ? -19.65552 -22.87849 -4.10498  1.000 54.93488 ? 224 ARG   A NH2 1 
ATOM   1583 N  N   . VAL   A 1 226 ? -14.32900 -22.03098 0.44068   1.000 28.87918 ? 225 VAL   A N   1 
ATOM   1584 C  CA  A VAL   A 1 226 ? -13.15406 -22.52502 -0.27342  0.517 30.03487 ? 225 VAL   A CA  1 
ATOM   1585 C  CA  B VAL   A 1 226 ? -13.15589 -22.51949 -0.28143  0.483 30.05003 ? 225 VAL   A CA  1 
ATOM   1586 C  C   . VAL   A 1 226 ? -13.62921 -23.52199 -1.32216  1.000 37.07934 ? 225 VAL   A C   1 
ATOM   1587 O  O   . VAL   A 1 226 ? -14.42320 -24.41798 -1.01953  1.000 35.55542 ? 225 VAL   A O   1 
ATOM   1588 C  CB  A VAL   A 1 226 ? -12.14021 -23.16989 0.68688   0.517 40.99639 ? 225 VAL   A CB  1 
ATOM   1589 C  CB  B VAL   A 1 226 ? -12.11815 -23.14682 0.66546   0.483 40.99063 ? 225 VAL   A CB  1 
ATOM   1590 C  CG1 A VAL   A 1 226 ? -12.86037 -23.91077 1.79749   0.517 38.55565 ? 225 VAL   A CG1 1 
ATOM   1591 C  CG1 B VAL   A 1 226 ? -10.75691 -22.48655 0.46360   0.483 34.55379 ? 225 VAL   A CG1 1 
ATOM   1592 C  CG2 A VAL   A 1 226 ? -11.21665 -24.11309 -0.08216  0.517 37.41766 ? 225 VAL   A CG2 1 
ATOM   1593 C  CG2 B VAL   A 1 226 ? -12.56135 -23.01091 2.10294   0.483 33.27891 ? 225 VAL   A CG2 1 
ATOM   1594 N  N   . LEU   A 1 227 ? -13.15979 -23.37228 -2.55995  1.000 40.75188 ? 226 LEU   A N   1 
ATOM   1595 C  CA  . LEU   A 1 227 ? -13.74187 -24.13055 -3.66378  1.000 40.88772 ? 226 LEU   A CA  1 
ATOM   1596 C  C   . LEU   A 1 227 ? -12.87421 -25.29440 -4.13668  1.000 53.15631 ? 226 LEU   A C   1 
ATOM   1597 O  O   . LEU   A 1 227 ? -11.64859 -25.18225 -4.23654  1.000 49.03988 ? 226 LEU   A O   1 
ATOM   1598 C  CB  . LEU   A 1 227 ? -14.05726 -23.21346 -4.84337  1.000 40.31592 ? 226 LEU   A CB  1 
ATOM   1599 C  CG  . LEU   A 1 227 ? -14.80309 -21.92722 -4.49919  1.000 39.34922 ? 226 LEU   A CG  1 
ATOM   1600 C  CD1 . LEU   A 1 227 ? -14.71963 -20.96789 -5.68273  1.000 43.49590 ? 226 LEU   A CD1 1 
ATOM   1601 C  CD2 . LEU   A 1 227 ? -16.24542 -22.24316 -4.16237  1.000 46.99024 ? 226 LEU   A CD2 1 
ATOM   1602 N  N   . GLU   A 1 228 ? -13.53764 -26.41254 -4.45903  1.000 42.69901 ? 227 GLU   A N   1 
ATOM   1603 C  CA  . GLU   A 1 228 ? -12.85062 -27.63465 -4.85410  1.000 58.38791 ? 227 GLU   A CA  1 
ATOM   1604 C  C   . GLU   A 1 228 ? -12.78966 -27.73022 -6.37336  1.000 48.44436 ? 227 GLU   A C   1 
ATOM   1605 O  O   . GLU   A 1 228 ? -13.82565 -27.99808 -7.00802  1.000 44.41427 ? 227 GLU   A O   1 
ATOM   1606 C  CB  . GLU   A 1 228 ? -13.55885 -28.85847 -4.26507  1.000 62.28164 ? 227 GLU   A CB  1 
ATOM   1607 C  CG  . GLU   A 1 228 ? -13.09311 -30.20785 -4.81413  1.000 61.25760 ? 227 GLU   A CG  1 
ATOM   1608 C  CD  . GLU   A 1 228 ? -14.17824 -30.93234 -5.58662  0.000 58.23431 ? 227 GLU   A CD  1 
ATOM   1609 O  OE1 . GLU   A 1 228 ? -15.27892 -31.12435 -5.02739  0.000 57.37925 ? 227 GLU   A OE1 1 
ATOM   1610 O  OE2 . GLU   A 1 228 ? -13.93054 -31.31372 -6.74969  0.000 59.17635 ? 227 GLU   A OE2 1 
ATOM   1611 N  N   . PRO   A 1 229 ? -11.62479 -27.52258 -6.99496  1.000 50.86381 ? 228 PRO   A N   1 
ATOM   1612 C  CA  . PRO   A 1 229 ? -11.51791 -27.64169 -8.45773  1.000 53.21388 ? 228 PRO   A CA  1 
ATOM   1613 C  C   . PRO   A 1 229 ? -11.70255 -29.07570 -8.93075  1.000 62.21836 ? 228 PRO   A C   1 
ATOM   1614 O  O   . PRO   A 1 229 ? -11.66544 -30.03536 -8.15861  1.000 71.67934 ? 228 PRO   A O   1 
ATOM   1615 C  CB  . PRO   A 1 229 ? -10.09125 -27.15290 -8.73735  1.000 51.15599 ? 228 PRO   A CB  1 
ATOM   1616 C  CG  . PRO   A 1 229 ? -9.80951  -26.24064 -7.57632  1.000 56.60834 ? 228 PRO   A CG  1 
ATOM   1617 C  CD  . PRO   A 1 229 ? -10.35234 -27.05031 -6.43005  1.000 57.16553 ? 228 PRO   A CD  1 
ATOM   1618 N  N   . VAL   A 1 230 ? -11.89774 -29.20820 -10.24034 1.000 56.16712 ? 229 VAL   A N   1 
ATOM   1619 C  CA  . VAL   A 1 230 ? -11.98862 -30.51867 -10.87779 1.000 62.84367 ? 229 VAL   A CA  1 
ATOM   1620 C  C   . VAL   A 1 230 ? -11.23899 -30.49071 -12.20332 1.000 61.28937 ? 229 VAL   A C   1 
ATOM   1621 O  O   . VAL   A 1 230 ? -10.39892 -29.61853 -12.43271 1.000 67.20813 ? 229 VAL   A O   1 
ATOM   1622 C  CB  . VAL   A 1 230 ? -13.45413 -30.95454 -11.08590 1.000 61.96797 ? 229 VAL   A CB  1 
ATOM   1623 C  CG1 . VAL   A 1 230 ? -14.08660 -31.34395 -9.76310  1.000 60.86154 ? 229 VAL   A CG1 1 
ATOM   1624 C  CG2 . VAL   A 1 230 ? -14.25981 -29.86047 -11.77155 1.000 56.75031 ? 229 VAL   A CG2 1 
ATOM   1625 N  N   . ASP   A 1 241 ? -1.16332  -31.41269 1.16188   1.000 64.01134 ? 240 ASP   A N   1 
ATOM   1626 C  CA  . ASP   A 1 241 ? 0.11245   -30.73124 1.34184   1.000 59.64164 ? 240 ASP   A CA  1 
ATOM   1627 C  C   . ASP   A 1 241 ? -0.11282  -29.26478 1.69412   1.000 57.92779 ? 240 ASP   A C   1 
ATOM   1628 O  O   . ASP   A 1 241 ? -0.69736  -28.51723 0.91212   1.000 64.10362 ? 240 ASP   A O   1 
ATOM   1629 C  CB  . ASP   A 1 241 ? 0.96858   -30.84574 0.08003   1.000 56.93868 ? 240 ASP   A CB  1 
ATOM   1630 N  N   . LEU   A 1 242 ? 0.34750   -28.85408 2.87512   1.000 60.14851 ? 241 LEU   A N   1 
ATOM   1631 C  CA  . LEU   A 1 242 ? 0.13788   -27.48846 3.31392   1.000 49.55696 ? 241 LEU   A CA  1 
ATOM   1632 C  C   . LEU   A 1 242 ? 1.47458   -26.79125 3.51990   1.000 49.17899 ? 241 LEU   A C   1 
ATOM   1633 O  O   . LEU   A 1 242 ? 2.44515   -27.43109 3.93655   1.000 60.23791 ? 241 LEU   A O   1 
ATOM   1634 C  CB  . LEU   A 1 242 ? -0.66080  -27.44599 4.62644   1.000 42.55046 ? 241 LEU   A CB  1 
ATOM   1635 C  CG  . LEU   A 1 242 ? -2.11274  -27.90508 4.53651   1.000 46.10864 ? 241 LEU   A CG  1 
ATOM   1636 C  CD1 . LEU   A 1 242 ? -2.83886  -27.60473 5.84006   1.000 46.79359 ? 241 LEU   A CD1 1 
ATOM   1637 C  CD2 . LEU   A 1 242 ? -2.82567  -27.26456 3.35349   1.000 46.29216 ? 241 LEU   A CD2 1 
ATOM   1638 N  N   . PRO   A 1 243 ? 1.56231   -25.48742 3.23359   1.000 53.67788 ? 242 PRO   A N   1 
ATOM   1639 C  CA  . PRO   A 1 243 ? 0.49325   -24.62970 2.70569   1.000 46.07396 ? 242 PRO   A CA  1 
ATOM   1640 C  C   . PRO   A 1 243 ? 0.16945   -24.97905 1.26585   1.000 51.88223 ? 242 PRO   A C   1 
ATOM   1641 O  O   . PRO   A 1 243 ? 0.95304   -25.61933 0.56091   1.000 48.24854 ? 242 PRO   A O   1 
ATOM   1642 C  CB  . PRO   A 1 243 ? 1.07799   -23.21578 2.82522   1.000 39.23332 ? 242 PRO   A CB  1 
ATOM   1643 C  CG  . PRO   A 1 243 ? 2.57064   -23.41999 2.81430   1.000 47.05296 ? 242 PRO   A CG  1 
ATOM   1644 C  CD  . PRO   A 1 243 ? 2.78348   -24.72090 3.53332   1.000 50.56363 ? 242 PRO   A CD  1 
ATOM   1645 N  N   . ARG   A 1 244 ? -0.99378  -24.55128 0.79294   1.000 34.94269 ? 243 ARG   A N   1 
ATOM   1646 C  CA  . ARG   A 1 244 ? -1.36240  -24.82338 -0.58620  1.000 37.72191 ? 243 ARG   A CA  1 
ATOM   1647 C  C   . ARG   A 1 244 ? -2.34459  -23.75859 -1.04715  1.000 41.49165 ? 243 ARG   A C   1 
ATOM   1648 O  O   . ARG   A 1 244 ? -3.15359  -23.26827 -0.25635  1.000 34.42078 ? 243 ARG   A O   1 
ATOM   1649 C  CB  . ARG   A 1 244 ? -1.94332  -26.23553 -0.71254  1.000 46.97426 ? 243 ARG   A CB  1 
ATOM   1650 C  CG  . ARG   A 1 244 ? -3.44124  -26.31798 -0.61478  1.000 47.29114 ? 243 ARG   A CG  1 
ATOM   1651 C  CD  . ARG   A 1 244 ? -3.94623  -27.62527 -1.19119  1.000 55.42478 ? 243 ARG   A CD  1 
ATOM   1652 N  NE  . ARG   A 1 244 ? -5.27847  -27.94872 -0.69635  1.000 50.94155 ? 243 ARG   A NE  1 
ATOM   1653 C  CZ  . ARG   A 1 244 ? -5.52326  -28.69789 0.36871   1.000 48.41964 ? 243 ARG   A CZ  1 
ATOM   1654 N  NH1 . ARG   A 1 244 ? -4.54236  -29.23866 1.07487   1.000 51.46765 ? 243 ARG   A NH1 1 
ATOM   1655 N  NH2 . ARG   A 1 244 ? -6.78358  -28.90533 0.73824   1.000 52.63423 ? 243 ARG   A NH2 1 
ATOM   1656 N  N   . GLU   A 1 245 ? -2.24625  -23.38984 -2.32615  1.000 36.14337 ? 244 GLU   A N   1 
ATOM   1657 C  CA  . GLU   A 1 245 ? -3.12581  -22.37156 -2.88927  1.000 38.30451 ? 244 GLU   A CA  1 
ATOM   1658 C  C   . GLU   A 1 245 ? -4.54847  -22.89448 -3.01928  1.000 38.71867 ? 244 GLU   A C   1 
ATOM   1659 O  O   . GLU   A 1 245 ? -4.76854  -24.04232 -3.41042  1.000 42.71016 ? 244 GLU   A O   1 
ATOM   1660 C  CB  . GLU   A 1 245 ? -2.61911  -21.92962 -4.26366  1.000 41.96299 ? 244 GLU   A CB  1 
ATOM   1661 C  CG  . GLU   A 1 245 ? -1.61256  -20.79588 -4.21356  1.000 55.43317 ? 244 GLU   A CG  1 
ATOM   1662 C  CD  . GLU   A 1 245 ? -1.11835  -20.39515 -5.58856  0.000 60.96449 ? 244 GLU   A CD  1 
ATOM   1663 O  OE1 . GLU   A 1 245 ? -0.72555  -21.29306 -6.36211  1.000 67.73887 ? 244 GLU   A OE1 1 
ATOM   1664 O  OE2 . GLU   A 1 245 ? -1.12244  -19.18520 -5.89632  1.000 69.24818 ? 244 GLU   A OE2 1 
ATOM   1665 N  N   . VAL   A 1 246 ? -5.52047  -22.03802 -2.69310  1.000 33.48743 ? 245 VAL   A N   1 
ATOM   1666 C  CA  . VAL   A 1 246 ? -6.93868  -22.34712 -2.82150  1.000 32.11160 ? 245 VAL   A CA  1 
ATOM   1667 C  C   . VAL   A 1 246 ? -7.62848  -21.17728 -3.51372  1.000 30.30727 ? 245 VAL   A C   1 
ATOM   1668 O  O   . VAL   A 1 246 ? -7.03202  -20.12714 -3.74881  1.000 32.33526 ? 245 VAL   A O   1 
ATOM   1669 C  CB  . VAL   A 1 246 ? -7.60294  -22.63328 -1.45827  1.000 36.03577 ? 245 VAL   A CB  1 
ATOM   1670 C  CG1 . VAL   A 1 246 ? -6.99590  -23.86933 -0.82708  1.000 42.81285 ? 245 VAL   A CG1 1 
ATOM   1671 C  CG2 . VAL   A 1 246 ? -7.45369  -21.42495 -0.54224  1.000 32.48719 ? 245 VAL   A CG2 1 
ATOM   1672 N  N   . TRP   A 1 247 ? -8.90795  -21.37327 -3.83813  1.000 32.42562 ? 246 TRP   A N   1 
ATOM   1673 C  CA  . TRP   A 1 247 ? -9.76638  -20.31757 -4.35930  1.000 28.93985 ? 246 TRP   A CA  1 
ATOM   1674 C  C   . TRP   A 1 247 ? -10.83374 -19.97974 -3.32372  1.000 29.76267 ? 246 TRP   A C   1 
ATOM   1675 O  O   . TRP   A 1 247 ? -11.46271 -20.87895 -2.75762  1.000 35.01302 ? 246 TRP   A O   1 
ATOM   1676 C  CB  . TRP   A 1 247 ? -10.40048 -20.73275 -5.69776  1.000 30.43098 ? 246 TRP   A CB  1 
ATOM   1677 C  CG  . TRP   A 1 247 ? -9.39802  -20.80226 -6.81383  1.000 32.44328 ? 246 TRP   A CG  1 
ATOM   1678 C  CD1 . TRP   A 1 247 ? -8.79595  -21.92028 -7.31468  1.000 38.20022 ? 246 TRP   A CD1 1 
ATOM   1679 C  CD2 . TRP   A 1 247 ? -8.83491  -19.69100 -7.52046  1.000 34.67314 ? 246 TRP   A CD2 1 
ATOM   1680 N  NE1 . TRP   A 1 247 ? -7.91915  -21.57360 -8.32628  1.000 41.51840 ? 246 TRP   A NE1 1 
ATOM   1681 C  CE2 . TRP   A 1 247 ? -7.92281  -20.21013 -8.46387  1.000 40.98246 ? 246 TRP   A CE2 1 
ATOM   1682 C  CE3 . TRP   A 1 247 ? -9.04034  -18.30855 -7.46945  1.000 34.72795 ? 246 TRP   A CE3 1 
ATOM   1683 C  CZ2 . TRP   A 1 247 ? -7.20049  -19.39066 -9.33556  1.000 37.49460 ? 246 TRP   A CZ2 1 
ATOM   1684 C  CZ3 . TRP   A 1 247 ? -8.32302  -17.49644 -8.33920  1.000 39.96319 ? 246 TRP   A CZ3 1 
ATOM   1685 C  CH2 . TRP   A 1 247 ? -7.41381  -18.04007 -9.25255  1.000 37.46682 ? 246 TRP   A CH2 1 
ATOM   1686 N  N   . LEU   A 1 248 ? -11.03247 -18.68764 -3.07485  1.000 28.12976 ? 247 LEU   A N   1 
ATOM   1687 C  CA  . LEU   A 1 248 ? -11.93595 -18.20732 -2.03422  1.000 26.98611 ? 247 LEU   A CA  1 
ATOM   1688 C  C   . LEU   A 1 248 ? -13.07131 -17.41189 -2.65494  1.000 33.30675 ? 247 LEU   A C   1 
ATOM   1689 O  O   . LEU   A 1 248 ? -12.83178 -16.54288 -3.49951  1.000 33.31590 ? 247 LEU   A O   1 
ATOM   1690 C  CB  . LEU   A 1 248 ? -11.19355 -17.31860 -1.03841  1.000 27.19865 ? 247 LEU   A CB  1 
ATOM   1691 C  CG  . LEU   A 1 248 ? -10.09495 -17.96925 -0.21384  1.000 29.51289 ? 247 LEU   A CG  1 
ATOM   1692 C  CD1 . LEU   A 1 248 ? -9.29832  -16.88633 0.48123   1.000 30.40166 ? 247 LEU   A CD1 1 
ATOM   1693 C  CD2 . LEU   A 1 248 ? -10.71608 -18.93692 0.80459   1.000 34.67238 ? 247 LEU   A CD2 1 
ATOM   1694 N  N   . LEU   A 1 249 ? -14.29706 -17.68957 -2.22509  1.000 25.54896 ? 248 LEU   A N   1 
ATOM   1695 C  CA  . LEU   A 1 249 ? -15.46945 -16.94448 -2.67183  1.000 25.51454 ? 248 LEU   A CA  1 
ATOM   1696 C  C   . LEU   A 1 249 ? -16.17397 -16.33067 -1.47071  1.000 30.93758 ? 248 LEU   A C   1 
ATOM   1697 O  O   . LEU   A 1 249 ? -16.64299 -17.06112 -0.58887  1.000 31.36832 ? 248 LEU   A O   1 
ATOM   1698 C  CB  . LEU   A 1 249 ? -16.42586 -17.85991 -3.43432  1.000 25.87630 ? 248 LEU   A CB  1 
ATOM   1699 C  CG  . LEU   A 1 249 ? -17.74387 -17.20917 -3.85407  1.000 28.55647 ? 248 LEU   A CG  1 
ATOM   1700 C  CD1 . LEU   A 1 249 ? -17.47671 -16.07552 -4.84543  1.000 33.01251 ? 248 LEU   A CD1 1 
ATOM   1701 C  CD2 . LEU   A 1 249 ? -18.63624 -18.27328 -4.44083  1.000 33.98691 ? 248 LEU   A CD2 1 
ATOM   1702 N  N   . GLU   A 1 250 ? -16.26123 -14.99971 -1.43984  1.000 25.23149 ? 249 GLU   A N   1 
ATOM   1703 C  CA  . GLU   A 1 250 ? -17.01286 -14.34569 -0.36956  1.000 29.37082 ? 249 GLU   A CA  1 
ATOM   1704 C  C   . GLU   A 1 250 ? -18.49428 -14.66717 -0.50785  1.000 32.20485 ? 249 GLU   A C   1 
ATOM   1705 O  O   . GLU   A 1 250 ? -19.04641 -14.68728 -1.61414  1.000 32.18313 ? 249 GLU   A O   1 
ATOM   1706 C  CB  . GLU   A 1 250 ? -16.79813 -12.83492 -0.39579  1.000 31.76938 ? 249 GLU   A CB  1 
ATOM   1707 C  CG  . GLU   A 1 250 ? -17.41639 -12.11486 0.79913   1.000 32.27307 ? 249 GLU   A CG  1 
ATOM   1708 C  CD  . GLU   A 1 250 ? -16.97495 -10.66615 0.89400   1.000 44.04963 ? 249 GLU   A CD  1 
ATOM   1709 O  OE1 . GLU   A 1 250 ? -15.90975 -10.32404 0.33579   1.000 57.79290 ? 249 GLU   A OE1 1 
ATOM   1710 O  OE2 . GLU   A 1 250 ? -17.69822 -9.86782  1.51867   1.000 48.35282 ? 249 GLU   A OE2 1 
ATOM   1711 N  N   . THR   A 1 251 ? -19.14399 -14.91211 0.62237   1.000 30.13216 ? 250 THR   A N   1 
ATOM   1712 C  CA  . THR   A 1 251 ? -20.49425 -15.44309 0.62739   1.000 30.66753 ? 250 THR   A CA  1 
ATOM   1713 C  C   . THR   A 1 251 ? -21.26029 -14.83654 1.79112   1.000 30.00116 ? 250 THR   A C   1 
ATOM   1714 O  O   . THR   A 1 251 ? -20.65962 -14.47632 2.80892   1.000 27.31426 ? 250 THR   A O   1 
ATOM   1715 C  CB  . THR   A 1 251 ? -20.47103 -16.97805 0.74179   1.000 31.90573 ? 250 THR   A CB  1 
ATOM   1716 O  OG1 . THR   A 1 251 ? -21.74196 -17.52005 0.37324   1.000 47.46219 ? 250 THR   A OG1 1 
ATOM   1717 C  CG2 . THR   A 1 251 ? -20.09283 -17.42767 2.15078   1.000 32.55051 ? 250 THR   A CG2 1 
ATOM   1718 N  N   . PRO   A 1 252 ? -22.57249 -14.68082 1.65972   1.000 31.99811 ? 251 PRO   A N   1 
ATOM   1719 C  CA  . PRO   A 1 252 ? -23.37308 -14.23095 2.80330   1.000 30.00589 ? 251 PRO   A CA  1 
ATOM   1720 C  C   . PRO   A 1 252 ? -23.31294 -15.22337 3.96198   1.000 30.98793 ? 251 PRO   A C   1 
ATOM   1721 O  O   . PRO   A 1 252 ? -22.98538 -16.40159 3.81078   1.000 29.50452 ? 251 PRO   A O   1 
ATOM   1722 C  CB  . PRO   A 1 252 ? -24.79494 -14.10440 2.23389   1.000 37.07020 ? 251 PRO   A CB  1 
ATOM   1723 C  CG  . PRO   A 1 252 ? -24.77615 -14.71789 0.88265   1.000 34.22080 ? 251 PRO   A CG  1 
ATOM   1724 C  CD  . PRO   A 1 252 ? -23.36631 -14.91489 0.43776   1.000 36.35189 ? 251 PRO   A CD  1 
ATOM   1725 N  N   . GLN   A 1 253 ? -23.61027 -14.72034 5.15759   1.000 29.01635 ? 252 GLN   A N   1 
ATOM   1726 C  CA  . GLN   A 1 253 ? -23.76001 -15.60822 6.30055   1.000 29.48271 ? 252 GLN   A CA  1 
ATOM   1727 C  C   . GLN   A 1 253 ? -24.71539 -16.74870 5.96230   1.000 27.51120 ? 252 GLN   A C   1 
ATOM   1728 O  O   . GLN   A 1 253 ? -25.85750 -16.51274 5.54160   1.000 30.94200 ? 252 GLN   A O   1 
ATOM   1729 C  CB  . GLN   A 1 253 ? -24.29909 -14.81377 7.49058   1.000 24.83004 ? 252 GLN   A CB  1 
ATOM   1730 C  CG  . GLN   A 1 253 ? -24.27862 -15.55628 8.79333   1.000 25.87862 ? 252 GLN   A CG  1 
ATOM   1731 C  CD  . GLN   A 1 253 ? -24.90678 -14.74057 9.89284   1.000 26.74402 ? 252 GLN   A CD  1 
ATOM   1732 O  OE1 . GLN   A 1 253 ? -24.71363 -13.52112 9.96521   1.000 26.93340 ? 252 GLN   A OE1 1 
ATOM   1733 N  NE2 . GLN   A 1 253 ? -25.68641 -15.40026 10.74409  1.000 23.14174 ? 252 GLN   A NE2 1 
ATOM   1734 N  N   . ALA   A 1 254 ? -24.26989 -17.98587 6.21357   1.000 27.87133 ? 253 ALA   A N   1 
ATOM   1735 C  CA  . ALA   A 1 254 ? -25.07794 -19.16826 5.91278   1.000 30.55414 ? 253 ALA   A CA  1 
ATOM   1736 C  C   . ALA   A 1 254 ? -26.42332 -19.15771 6.63797   1.000 30.79358 ? 253 ALA   A C   1 
ATOM   1737 O  O   . ALA   A 1 254 ? -26.55005 -18.67759 7.76712   1.000 28.20627 ? 253 ALA   A O   1 
ATOM   1738 C  CB  . ALA   A 1 254 ? -24.31541 -20.44219 6.28441   1.000 32.01637 ? 253 ALA   A CB  1 
ATOM   1739 N  N   . ASP   A 1 255 ? -27.43613 -19.73549 5.98030   1.000 30.04917 ? 254 ASP   A N   1 
ATOM   1740 C  CA  . ASP   A 1 255 ? -28.78567 -19.77294 6.53538   1.000 30.43884 ? 254 ASP   A CA  1 
ATOM   1741 C  C   . ASP   A 1 255 ? -28.84587 -20.57049 7.83140   1.000 31.11272 ? 254 ASP   A C   1 
ATOM   1742 O  O   . ASP   A 1 255 ? -29.64033 -20.24975 8.73216   1.000 35.79316 ? 254 ASP   A O   1 
ATOM   1743 C  CB  . ASP   A 1 255 ? -29.74695 -20.39351 5.50846   1.000 34.99126 ? 254 ASP   A CB  1 
ATOM   1744 C  CG  . ASP   A 1 255 ? -30.71882 -19.38809 4.91609   1.000 48.78217 ? 254 ASP   A CG  1 
ATOM   1745 O  OD1 . ASP   A 1 255 ? -30.65838 -18.19036 5.27259   1.000 44.94322 ? 254 ASP   A OD1 1 
ATOM   1746 O  OD2 . ASP   A 1 255 ? -31.53693 -19.80113 4.06607   0.469 49.46463 ? 254 ASP   A OD2 1 
ATOM   1747 N  N   . ASP   A 1 256 ? -28.04004 -21.62620 7.94328   1.000 27.80304 ? 255 ASP   A N   1 
ATOM   1748 C  CA  . ASP   A 1 256 ? -28.09531 -22.49120 9.10441   1.000 32.37736 ? 255 ASP   A CA  1 
ATOM   1749 C  C   . ASP   A 1 256 ? -27.05833 -22.12611 10.15520  1.000 26.58226 ? 255 ASP   A C   1 
ATOM   1750 O  O   . ASP   A 1 256 ? -26.93839 -22.84769 11.14788  1.000 26.71775 ? 255 ASP   A O   1 
ATOM   1751 C  CB  . ASP   A 1 256 ? -27.95198 -23.96520 8.69654   1.000 33.11290 ? 255 ASP   A CB  1 
ATOM   1752 C  CG  . ASP   A 1 256 ? -26.59811 -24.30383 8.10063   1.000 42.96427 ? 255 ASP   A CG  1 
ATOM   1753 O  OD1 . ASP   A 1 256 ? -25.81033 -23.39154 7.77274   1.000 39.56824 ? 255 ASP   A OD1 1 
ATOM   1754 O  OD2 . ASP   A 1 256 ? -26.32800 -25.51768 7.94538   1.000 45.63754 ? 255 ASP   A OD2 1 
ATOM   1755 N  N   . PHE   A 1 257 ? -26.34034 -21.01174 9.98842   1.000 23.71630 ? 256 PHE   A N   1 
ATOM   1756 C  CA  . PHE   A 1 257 ? -25.41466 -20.53914 11.01205  1.000 21.97666 ? 256 PHE   A CA  1 
ATOM   1757 C  C   . PHE   A 1 257 ? -25.91326 -19.23441 11.61787  1.000 22.73806 ? 256 PHE   A C   1 
ATOM   1758 O  O   . PHE   A 1 257 ? -26.15498 -18.25979 10.90543  1.000 23.42727 ? 256 PHE   A O   1 
ATOM   1759 C  CB  . PHE   A 1 257 ? -24.00772 -20.31862 10.45874  1.000 24.55367 ? 256 PHE   A CB  1 
ATOM   1760 C  CG  . PHE   A 1 257 ? -23.09808 -19.65010 11.44529  1.000 21.13094 ? 256 PHE   A CG  1 
ATOM   1761 C  CD1 . PHE   A 1 257 ? -22.72046 -20.32009 12.61201  1.000 22.86517 ? 256 PHE   A CD1 1 
ATOM   1762 C  CD2 . PHE   A 1 257 ? -22.65127 -18.36167 11.24662  1.000 23.02404 ? 256 PHE   A CD2 1 
ATOM   1763 C  CE1 . PHE   A 1 257 ? -21.90246 -19.71369 13.54465  1.000 21.91465 ? 256 PHE   A CE1 1 
ATOM   1764 C  CE2 . PHE   A 1 257 ? -21.81984 -17.75489 12.19251  1.000 22.38283 ? 256 PHE   A CE2 1 
ATOM   1765 C  CZ  . PHE   A 1 257 ? -21.45803 -18.42383 13.33560  1.000 23.08222 ? 256 PHE   A CZ  1 
ATOM   1766 N  N   . TRP   A 1 258 ? -26.06136 -19.21439 12.93596  1.000 20.88529 ? 257 TRP   A N   1 
ATOM   1767 C  CA  . TRP   A 1 258 ? -26.10622 -17.95248 13.65128  1.000 22.98942 ? 257 TRP   A CA  1 
ATOM   1768 C  C   . TRP   A 1 258 ? -25.72403 -18.23114 15.09282  1.000 23.22329 ? 257 TRP   A C   1 
ATOM   1769 O  O   . TRP   A 1 258 ? -25.62177 -19.38735 15.51614  1.000 21.63137 ? 257 TRP   A O   1 
ATOM   1770 C  CB  . TRP   A 1 258 ? -27.47572 -17.26900 13.52718  1.000 23.32330 ? 257 TRP   A CB  1 
ATOM   1771 C  CG  . TRP   A 1 258 ? -28.56385 -17.84547 14.36461  1.000 27.93323 ? 257 TRP   A CG  1 
ATOM   1772 C  CD1 . TRP   A 1 258 ? -29.06990 -17.32564 15.53644  1.000 30.83045 ? 257 TRP   A CD1 1 
ATOM   1773 C  CD2 . TRP   A 1 258 ? -29.32911 -19.02621 14.09107  1.000 27.59285 ? 257 TRP   A CD2 1 
ATOM   1774 N  NE1 . TRP   A 1 258 ? -30.09260 -18.10588 15.99040  1.000 28.01319 ? 257 TRP   A NE1 1 
ATOM   1775 C  CE2 . TRP   A 1 258 ? -30.27538 -19.15440 15.12495  1.000 24.91724 ? 257 TRP   A CE2 1 
ATOM   1776 C  CE3 . TRP   A 1 258 ? -29.31028 -19.97888 13.06614  1.000 31.63949 ? 257 TRP   A CE3 1 
ATOM   1777 C  CZ2 . TRP   A 1 258 ? -31.18370 -20.21865 15.18569  1.000 35.20337 ? 257 TRP   A CZ2 1 
ATOM   1778 C  CZ3 . TRP   A 1 258 ? -30.21985 -21.03117 13.12087  1.000 32.14686 ? 257 TRP   A CZ3 1 
ATOM   1779 C  CH2 . TRP   A 1 258 ? -31.14385 -21.13816 14.17423  1.000 30.87229 ? 257 TRP   A CH2 1 
ATOM   1780 N  N   . CYS   A 1 259 ? -25.47668 -17.14391 15.82731  1.000 20.62174 ? 258 CYS   A N   1 
ATOM   1781 C  CA  A CYS   A 1 259 ? -24.94776 -17.17095 17.19226  0.382 20.13784 ? 258 CYS   A CA  1 
ATOM   1782 C  CA  B CYS   A 1 259 ? -24.97378 -17.20376 17.18898  0.618 20.00966 ? 258 CYS   A CA  1 
ATOM   1783 C  C   . CYS   A 1 259 ? -25.85123 -16.34929 18.09094  1.000 22.31760 ? 258 CYS   A C   1 
ATOM   1784 O  O   . CYS   A 1 259 ? -26.05323 -15.16340 17.82194  1.000 29.36648 ? 258 CYS   A O   1 
ATOM   1785 C  CB  A CYS   A 1 259 ? -23.55313 -16.54926 17.26087  0.382 24.79800 ? 258 CYS   A CB  1 
ATOM   1786 C  CB  B CYS   A 1 259 ? -23.51912 -16.72408 17.20699  0.618 24.48025 ? 258 CYS   A CB  1 
ATOM   1787 S  SG  A CYS   A 1 259 ? -22.23301 -17.41977 16.52036  0.382 25.55028 ? 258 CYS   A SG  1 
ATOM   1788 S  SG  B CYS   A 1 259 ? -22.66998 -16.92416 18.77212  0.618 22.51203 ? 258 CYS   A SG  1 
ATOM   1789 N  N   . GLU   A 1 260 ? -26.36066 -16.94652 19.16807  1.000 21.67352 ? 259 GLU   A N   1 
ATOM   1790 C  CA  . GLU   A 1 260 ? -27.15443 -16.18968 20.12907  1.000 22.96672 ? 259 GLU   A CA  1 
ATOM   1791 C  C   . GLU   A 1 260 ? -26.34983 -15.99818 21.40720  1.000 21.56997 ? 259 GLU   A C   1 
ATOM   1792 O  O   . GLU   A 1 260 ? -25.53964 -16.84433 21.77907  1.000 20.28695 ? 259 GLU   A O   1 
ATOM   1793 C  CB  . GLU   A 1 260 ? -28.47752 -16.89779 20.46355  1.000 27.32647 ? 259 GLU   A CB  1 
ATOM   1794 C  CG  . GLU   A 1 260 ? -29.55435 -16.66771 19.42169  1.000 31.91672 ? 259 GLU   A CG  1 
ATOM   1795 C  CD  . GLU   A 1 260 ? -30.76798 -17.55506 19.62955  1.000 37.04745 ? 259 GLU   A CD  1 
ATOM   1796 O  OE1 . GLU   A 1 260 ? -31.06081 -17.89184 20.79603  1.000 37.27379 ? 259 GLU   A OE1 1 
ATOM   1797 O  OE2 . GLU   A 1 260 ? -31.42273 -17.91413 18.62521  1.000 37.54574 ? 259 GLU   A OE2 1 
ATOM   1798 N  N   . GLY   A 1 261 ? -26.59640 -14.89418 22.10189  1.000 22.36794 ? 260 GLY   A N   1 
ATOM   1799 C  CA  . GLY   A 1 261 ? -25.97249 -14.71270 23.41051  1.000 21.94359 ? 260 GLY   A CA  1 
ATOM   1800 C  C   . GLY   A 1 261 ? -26.58621 -15.59583 24.48328  1.000 23.93674 ? 260 GLY   A C   1 
ATOM   1801 O  O   . GLY   A 1 261 ? -27.75883 -15.97253 24.44023  1.000 24.10658 ? 260 GLY   A O   1 
ATOM   1802 N  N   . GLU   A 1 262 ? -25.77324 -15.93523 25.47154  1.000 19.86521 ? 261 GLU   A N   1 
ATOM   1803 C  CA  . GLU   A 1 262 ? -26.25964 -16.56218 26.69358  1.000 22.06653 ? 261 GLU   A CA  1 
ATOM   1804 C  C   . GLU   A 1 262 ? -25.46145 -16.00978 27.86199  1.000 21.23750 ? 261 GLU   A C   1 
ATOM   1805 O  O   . GLU   A 1 262 ? -24.37422 -15.46093 27.67124  1.000 21.32240 ? 261 GLU   A O   1 
ATOM   1806 C  CB  . GLU   A 1 262 ? -26.16790 -18.09357 26.62153  1.000 24.44419 ? 261 GLU   A CB  1 
ATOM   1807 C  CG  . GLU   A 1 262 ? -24.78875 -18.71697 26.66881  1.000 24.64806 ? 261 GLU   A CG  1 
ATOM   1808 C  CD  . GLU   A 1 262 ? -24.87470 -20.23266 26.85095  1.000 28.23023 ? 261 GLU   A CD  1 
ATOM   1809 O  OE1 . GLU   A 1 262 ? -25.17712 -20.68085 27.98360  1.000 26.09588 ? 261 GLU   A OE1 1 
ATOM   1810 O  OE2 . GLU   A 1 262 ? -24.64069 -20.98440 25.87781  1.000 26.69599 ? 261 GLU   A OE2 1 
ATOM   1811 N  N   . PRO   A 1 263 ? -26.00378 -16.07970 29.07492  1.000 22.41674 ? 262 PRO   A N   1 
ATOM   1812 C  CA  . PRO   A 1 263 ? -25.32568 -15.43661 30.20863  1.000 21.83217 ? 262 PRO   A CA  1 
ATOM   1813 C  C   . PRO   A 1 263 ? -23.95389 -16.03681 30.47959  1.000 21.38212 ? 262 PRO   A C   1 
ATOM   1814 O  O   . PRO   A 1 263 ? -23.74103 -17.23804 30.35343  1.000 23.01659 ? 262 PRO   A O   1 
ATOM   1815 C  CB  . PRO   A 1 263 ? -26.27750 -15.67998 31.39022  1.000 24.51005 ? 262 PRO   A CB  1 
ATOM   1816 C  CG  . PRO   A 1 263 ? -27.61148 -15.91412 30.76033  1.000 26.83694 ? 262 PRO   A CG  1 
ATOM   1817 C  CD  . PRO   A 1 263 ? -27.34669 -16.57414 29.42182  1.000 24.43313 ? 262 PRO   A CD  1 
ATOM   1818 N  N   . TYR   A 1 264 ? -23.02214 -15.16184 30.85286  1.000 20.76496 ? 263 TYR   A N   1 
ATOM   1819 C  CA  . TYR   A 1 264 ? -21.69254 -15.56521 31.30177  1.000 21.35728 ? 263 TYR   A CA  1 
ATOM   1820 C  C   . TYR   A 1 264 ? -21.72598 -15.85746 32.80717  1.000 21.30979 ? 263 TYR   A C   1 
ATOM   1821 O  O   . TYR   A 1 264 ? -22.07876 -14.96125 33.58421  1.000 21.38667 ? 263 TYR   A O   1 
ATOM   1822 C  CB  . TYR   A 1 264 ? -20.71894 -14.43276 30.98271  1.000 19.55696 ? 263 TYR   A CB  1 
ATOM   1823 C  CG  . TYR   A 1 264 ? -19.41377 -14.53410 31.69026  1.000 20.44624 ? 263 TYR   A CG  1 
ATOM   1824 C  CD1 . TYR   A 1 264 ? -18.63526 -15.66997 31.55346  1.000 18.32922 ? 263 TYR   A CD1 1 
ATOM   1825 C  CD2 . TYR   A 1 264 ? -18.97058 -13.50535 32.52288  1.000 21.29359 ? 263 TYR   A CD2 1 
ATOM   1826 C  CE1 . TYR   A 1 264 ? -17.43623 -15.78657 32.22171  1.000 20.34025 ? 263 TYR   A CE1 1 
ATOM   1827 C  CE2 . TYR   A 1 264 ? -17.76521 -13.61328 33.18658  1.000 22.29457 ? 263 TYR   A CE2 1 
ATOM   1828 C  CZ  . TYR   A 1 264 ? -17.01786 -14.76728 33.03712  1.000 20.08110 ? 263 TYR   A CZ  1 
ATOM   1829 O  OH  . TYR   A 1 264 ? -15.81212 -14.92143 33.70288  1.000 22.15687 ? 263 TYR   A OH  1 
ATOM   1830 N  N   . PRO   A 1 265 ? -21.38135 -17.06803 33.26058  1.000 19.89798 ? 264 PRO   A N   1 
ATOM   1831 C  CA  . PRO   A 1 265 ? -21.51860 -17.41661 34.68485  1.000 21.60874 ? 264 PRO   A CA  1 
ATOM   1832 C  C   . PRO   A 1 265 ? -20.28505 -17.17086 35.53698  1.000 24.15465 ? 264 PRO   A C   1 
ATOM   1833 O  O   . PRO   A 1 265 ? -20.35228 -17.39612 36.75555  1.000 23.82721 ? 264 PRO   A O   1 
ATOM   1834 C  CB  . PRO   A 1 265 ? -21.80890 -18.92347 34.62847  1.000 25.20226 ? 264 PRO   A CB  1 
ATOM   1835 C  CG  . PRO   A 1 265 ? -20.95708 -19.38098 33.46693  1.000 23.86439 ? 264 PRO   A CG  1 
ATOM   1836 C  CD  . PRO   A 1 265 ? -21.08754 -18.26096 32.43707  1.000 21.73750 ? 264 PRO   A CD  1 
ATOM   1837 N  N   . GLY   A 1 266 ? -19.17674 -16.72600 34.96032  1.000 20.51562 ? 265 GLY   A N   1 
ATOM   1838 C  CA  . GLY   A 1 266 ? -17.92792 -16.69566 35.68813  1.000 22.02332 ? 265 GLY   A CA  1 
ATOM   1839 C  C   . GLY   A 1 266 ? -17.65750 -15.38460 36.40240  1.000 20.54086 ? 265 GLY   A C   1 
ATOM   1840 O  O   . GLY   A 1 266 ? -18.47890 -14.45566 36.42743  1.000 22.12519 ? 265 GLY   A O   1 
ATOM   1841 N  N   . PRO   A 1 267 ? -16.47725 -15.29769 37.01039  1.000 23.09507 ? 266 PRO   A N   1 
ATOM   1842 C  CA  . PRO   A 1 267 ? -16.07258 -14.06330 37.68757  1.000 25.15717 ? 266 PRO   A CA  1 
ATOM   1843 C  C   . PRO   A 1 267 ? -16.15185 -12.87365 36.74210  1.000 23.31597 ? 266 PRO   A C   1 
ATOM   1844 O  O   . PRO   A 1 267 ? -15.75277 -12.94931 35.57580  1.000 24.00782 ? 266 PRO   A O   1 
ATOM   1845 C  CB  . PRO   A 1 267 ? -14.62212 -14.34323 38.09757  1.000 28.19716 ? 266 PRO   A CB  1 
ATOM   1846 C  CG  . PRO   A 1 267 ? -14.48064 -15.84490 38.06174  1.000 27.17078 ? 266 PRO   A CG  1 
ATOM   1847 C  CD  . PRO   A 1 267 ? -15.40930 -16.31036 36.98107  1.000 22.88537 ? 266 PRO   A CD  1 
ATOM   1848 N  N   . LYS   A 1 268 ? -16.63402 -11.75072 37.26258  1.000 26.44405 ? 267 LYS   A N   1 
ATOM   1849 C  CA  . LYS   A 1 268 ? -16.85998 -10.59929 36.40527  1.000 28.40629 ? 267 LYS   A CA  1 
ATOM   1850 C  C   . LYS   A 1 268 ? -15.59584 -9.75852  36.28440  1.000 31.86055 ? 267 LYS   A C   1 
ATOM   1851 O  O   . LYS   A 1 268 ? -14.74262 -9.73141  37.18101  1.000 32.66986 ? 267 LYS   A O   1 
ATOM   1852 C  CB  . LYS   A 1 268 ? -18.02618 -9.75812  36.93252  1.000 29.29088 ? 267 LYS   A CB  1 
ATOM   1853 C  CG  . LYS   A 1 268 ? -19.21333 -10.60501 37.35497  1.000 34.81637 ? 267 LYS   A CG  1 
ATOM   1854 C  CD  . LYS   A 1 268 ? -19.76510 -11.42132 36.17823  1.000 30.78870 ? 267 LYS   A CD  1 
ATOM   1855 C  CE  . LYS   A 1 268 ? -20.89402 -12.36836 36.64599  1.000 29.10854 ? 267 LYS   A CE  1 
ATOM   1856 N  NZ  . LYS   A 1 268 ? -21.08485 -13.48956 35.65052  1.000 24.74757 ? 267 LYS   A NZ  1 
ATOM   1857 N  N   . VAL   A 1 269 ? -15.46841 -9.10191  35.14477  1.000 25.71620 ? 268 VAL   A N   1 
ATOM   1858 C  CA  . VAL   A 1 269 ? -14.37919 -8.16857  34.90729  1.000 24.87300 ? 268 VAL   A CA  1 
ATOM   1859 C  C   . VAL   A 1 269 ? -14.87090 -6.77938  35.28438  1.000 31.54341 ? 268 VAL   A C   1 
ATOM   1860 O  O   . VAL   A 1 269 ? -15.93925 -6.34566  34.83562  1.000 35.97085 ? 268 VAL   A O   1 
ATOM   1861 C  CB  . VAL   A 1 269 ? -13.90682 -8.23828  33.44898  1.000 26.70303 ? 268 VAL   A CB  1 
ATOM   1862 C  CG1 . VAL   A 1 269 ? -12.91697 -7.11464  33.14405  1.000 31.67795 ? 268 VAL   A CG1 1 
ATOM   1863 C  CG2 . VAL   A 1 269 ? -13.26607 -9.59721  33.18348  1.000 29.18188 ? 268 VAL   A CG2 1 
ATOM   1864 N  N   . PHE   A 1 270 ? -14.11119 -6.10544  36.14129  1.000 29.76292 ? 269 PHE   A N   1 
ATOM   1865 C  CA  A PHE   A 1 270 ? -14.42915 -4.81738  36.76054  0.491 35.09184 ? 269 PHE   A CA  1 
ATOM   1866 C  CA  B PHE   A 1 270 ? -14.48377 -4.80854  36.67456  0.509 35.04392 ? 269 PHE   A CA  1 
ATOM   1867 C  C   . PHE   A 1 270 ? -13.49898 -3.74105  36.22570  1.000 42.16862 ? 269 PHE   A C   1 
ATOM   1868 O  O   . PHE   A 1 270 ? -12.29872 -3.99980  36.09417  1.000 39.58942 ? 269 PHE   A O   1 
ATOM   1869 C  CB  A PHE   A 1 270 ? -14.25127 -4.87523  38.28547  0.491 37.94887 ? 269 PHE   A CB  1 
ATOM   1870 C  CB  B PHE   A 1 270 ? -14.56104 -4.81113  38.21201  0.509 37.59657 ? 269 PHE   A CB  1 
ATOM   1871 C  CG  A PHE   A 1 270 ? -15.25528 -5.72598  39.00844  0.491 41.46188 ? 269 PHE   A CG  1 
ATOM   1872 C  CG  B PHE   A 1 270 ? -13.27744 -5.21205  38.90545  0.509 40.56624 ? 269 PHE   A CG  1 
ATOM   1873 C  CD1 A PHE   A 1 270 ? -15.18968 -7.10749  38.94166  0.491 35.00684 ? 269 PHE   A CD1 1 
ATOM   1874 C  CD1 B PHE   A 1 270 ? -12.25252 -4.29599  39.09100  0.509 43.96795 ? 269 PHE   A CD1 1 
ATOM   1875 C  CD2 A PHE   A 1 270 ? -16.19860 -5.14728  39.84112  0.491 49.13774 ? 269 PHE   A CD2 1 
ATOM   1876 C  CD2 B PHE   A 1 270 ? -13.11760 -6.49267  39.41491  0.509 42.50391 ? 269 PHE   A CD2 1 
ATOM   1877 C  CE1 A PHE   A 1 270 ? -16.09161 -7.89536  39.63566  0.491 42.94003 ? 269 PHE   A CE1 1 
ATOM   1878 C  CE1 B PHE   A 1 270 ? -11.08065 -4.65658  39.74252  0.509 41.36992 ? 269 PHE   A CE1 1 
ATOM   1879 C  CE2 A PHE   A 1 270 ? -17.09719 -5.92814  40.54718  0.491 49.37589 ? 269 PHE   A CE2 1 
ATOM   1880 C  CE2 B PHE   A 1 270 ? -11.94951 -6.85785  40.07208  0.509 44.91292 ? 269 PHE   A CE2 1 
ATOM   1881 C  CZ  A PHE   A 1 270 ? -17.04410 -7.30429  40.44286  0.491 48.35928 ? 269 PHE   A CZ  1 
ATOM   1882 C  CZ  B PHE   A 1 270 ? -10.93192 -5.93869  40.23555  0.509 41.43643 ? 269 PHE   A CZ  1 
ATOM   1883 N  N   . PRO   A 1 271 ? -13.99306 -2.52580  35.95493  1.000 39.66712 ? 270 PRO   A N   1 
ATOM   1884 C  CA  . PRO   A 1 271 ? -13.10882 -1.42242  35.56938  1.000 49.59917 ? 270 PRO   A CA  1 
ATOM   1885 C  C   . PRO   A 1 271 ? -12.08052 -1.11302  36.65482  0.000 46.60216 ? 270 PRO   A C   1 
ATOM   1886 O  O   . PRO   A 1 271 ? -12.43825 -0.78417  37.78618  0.000 45.98893 ? 270 PRO   A O   1 
ATOM   1887 C  CB  . PRO   A 1 271 ? -14.07259 -0.24921  35.37965  1.000 43.09873 ? 270 PRO   A CB  1 
ATOM   1888 C  CG  . PRO   A 1 271 ? -15.37947 -0.87390  35.06838  1.000 48.40106 ? 270 PRO   A CG  1 
ATOM   1889 C  CD  . PRO   A 1 271 ? -15.41777 -2.18522  35.80946  1.000 41.43284 ? 270 PRO   A CD  1 
ATOM   1890 O  OXT . PRO   A 1 271 ? -10.87139 -1.18466  36.43178  1.000 61.80733 ? 270 PRO   A OXT 1 
HETATM 1891 C  C   . ACE   B 2 1   ? -33.84673 -11.35969 11.60222  1.000 39.20776 ? 0   ACE   B C   1 
HETATM 1892 O  O   . ACE   B 2 1   ? -34.70484 -10.63520 11.08917  1.000 36.65783 ? 0   ACE   B O   1 
HETATM 1893 C  CH3 . ACE   B 2 1   ? -33.91726 -12.85510 11.57979  1.000 30.87466 ? 0   ACE   B CH3 1 
ATOM   1894 N  N   . TYR   B 2 2   ? -32.78737 -10.86522 12.22158  1.000 34.05440 ? 1   TYR   B N   1 
ATOM   1895 C  CA  . TYR   B 2 2   ? -32.55707 -9.43534  12.33687  1.000 36.13090 ? 1   TYR   B CA  1 
ATOM   1896 C  C   . TYR   B 2 2   ? -31.04530 -9.24173  12.35408  1.000 31.60443 ? 1   TYR   B C   1 
ATOM   1897 O  O   . TYR   B 2 2   ? -30.30740 -10.16667 12.67759  1.000 31.73801 ? 1   TYR   B O   1 
ATOM   1898 C  CB  . TYR   B 2 2   ? -33.23112 -8.86658  13.60355  1.000 31.84536 ? 1   TYR   B CB  1 
ATOM   1899 C  CG  . TYR   B 2 2   ? -32.74603 -9.48569  14.90364  1.000 34.47115 ? 1   TYR   B CG  1 
ATOM   1900 C  CD1 . TYR   B 2 2   ? -31.58525 -9.03201  15.51723  1.000 35.71814 ? 1   TYR   B CD1 1 
ATOM   1901 C  CD2 . TYR   B 2 2   ? -33.43335 -10.53433 15.50105  1.000 36.83373 ? 1   TYR   B CD2 1 
ATOM   1902 C  CE1 . TYR   B 2 2   ? -31.12725 -9.59485  16.69576  1.000 36.23634 ? 1   TYR   B CE1 1 
ATOM   1903 C  CE2 . TYR   B 2 2   ? -32.97758 -11.11033 16.68725  1.000 36.95828 ? 1   TYR   B CE2 1 
ATOM   1904 C  CZ  . TYR   B 2 2   ? -31.82281 -10.62795 17.27636  1.000 36.00285 ? 1   TYR   B CZ  1 
ATOM   1905 O  OH  . TYR   B 2 2   ? -31.34808 -11.18744 18.44923  1.000 39.05427 ? 1   TYR   B OH  1 
ATOM   1906 N  N   . ILE   B 2 3   ? -30.57413 -8.05948  11.99968  1.000 33.09663 ? 2   ILE   B N   1 
ATOM   1907 C  CA  . ILE   B 2 3   ? -29.14406 -7.79654  11.96239  1.000 32.46396 ? 2   ILE   B CA  1 
ATOM   1908 C  C   . ILE   B 2 3   ? -28.78585 -6.99455  13.19980  1.000 36.31599 ? 2   ILE   B C   1 
ATOM   1909 O  O   . ILE   B 2 3   ? -29.48725 -6.03749  13.55814  1.000 37.39768 ? 2   ILE   B O   1 
ATOM   1910 C  CB  . ILE   B 2 3   ? -28.74780 -7.05888  10.67545  1.000 38.95641 ? 2   ILE   B CB  1 
ATOM   1911 C  CG1 . ILE   B 2 3   ? -29.15543 -7.91607  9.47723   1.000 42.43080 ? 2   ILE   B CG1 1 
ATOM   1912 C  CG2 . ILE   B 2 3   ? -27.25202 -6.74120  10.66996  1.000 40.32929 ? 2   ILE   B CG2 1 
ATOM   1913 C  CD1 . ILE   B 2 3   ? -28.13290 -8.93076  9.08074   1.000 41.73404 ? 2   ILE   B CD1 1 
ATOM   1914 N  N   . VAL   B 2 4   ? -27.71836 -7.40040  13.87550  1.000 31.57457 ? 3   VAL   B N   1 
ATOM   1915 C  CA  . VAL   B 2 4   ? -27.20959 -6.67978  15.03013  1.000 32.60898 ? 3   VAL   B CA  1 
ATOM   1916 C  C   . VAL   B 2 4   ? -25.72318 -6.42808  14.82993  1.000 30.72487 ? 3   VAL   B C   1 
ATOM   1917 O  O   . VAL   B 2 4   ? -24.98437 -7.31225  14.38040  1.000 31.00057 ? 3   VAL   B O   1 
ATOM   1918 C  CB  . VAL   B 2 4   ? -27.48276 -7.44031  16.34787  1.000 35.47702 ? 3   VAL   B CB  1 
ATOM   1919 C  CG1 . VAL   B 2 4   ? -26.92965 -8.83090  16.28911  1.000 38.35244 ? 3   VAL   B CG1 1 
ATOM   1920 C  CG2 . VAL   B 2 4   ? -26.85981 -6.69851  17.51493  1.000 44.11450 ? 3   VAL   B CG2 1 
ATOM   1921 N  N   . LYS   B 2 5   ? -25.29447 -5.20238  15.11618  1.000 31.87575 ? 4   LYS   B N   1 
ATOM   1922 C  CA  . LYS   B 2 5   ? -23.87561 -4.88139  15.08333  1.000 34.52892 ? 4   LYS   B CA  1 
ATOM   1923 C  C   . LYS   B 2 5   ? -23.25495 -5.33992  16.39546  1.000 30.44212 ? 4   LYS   B C   1 
ATOM   1924 O  O   . LYS   B 2 5   ? -23.65223 -4.88071  17.47161  1.000 36.50405 ? 4   LYS   B O   1 
ATOM   1925 C  CB  . LYS   B 2 5   ? -23.65932 -3.38860  14.84347  1.000 39.76621 ? 4   LYS   B CB  1 
ATOM   1926 C  CG  . LYS   B 2 5   ? -24.17601 -2.91647  13.49085  1.000 45.72166 ? 4   LYS   B CG  1 
ATOM   1927 C  CD  . LYS   B 2 5   ? -23.70808 -1.49994  13.18644  1.000 58.60953 ? 4   LYS   B CD  1 
ATOM   1928 C  CE  . LYS   B 2 5   ? -24.32715 -0.98893  11.89635  1.000 70.30918 ? 4   LYS   B CE  1 
ATOM   1929 N  NZ  . LYS   B 2 5   ? -25.68082 -1.57035  11.67735  1.000 78.32128 ? 4   LYS   B NZ  1 
ATOM   1930 N  N   . THR   B 2 6   ? -22.31713 -6.27880  16.30528  1.000 28.90489 ? 5   THR   B N   1 
ATOM   1931 C  CA  . THR   B 2 6   ? -21.70159 -6.89927  17.46948  1.000 29.24999 ? 5   THR   B CA  1 
ATOM   1932 C  C   . THR   B 2 6   ? -20.19832 -6.67489  17.44602  1.000 28.19465 ? 5   THR   B C   1 
ATOM   1933 O  O   . THR   B 2 6   ? -19.58621 -6.53947  16.38336  1.000 29.81782 ? 5   THR   B O   1 
ATOM   1934 C  CB  . THR   B 2 6   ? -21.96806 -8.42082  17.52955  1.000 28.79299 ? 5   THR   B CB  1 
ATOM   1935 O  OG1 . THR   B 2 6   ? -21.25585 -9.06959  16.46842  1.000 27.60486 ? 5   THR   B OG1 1 
ATOM   1936 C  CG2 . THR   B 2 6   ? -23.45376 -8.72032  17.36849  1.000 30.35803 ? 5   THR   B CG2 1 
ATOM   1937 N  N   . PHE   B 2 7   ? -19.60971 -6.64919  18.63821  1.000 29.07878 ? 6   PHE   B N   1 
ATOM   1938 C  CA  . PHE   B 2 7   ? -18.16229 -6.58984  18.75081  1.000 28.97480 ? 6   PHE   B CA  1 
ATOM   1939 C  C   . PHE   B 2 7   ? -17.50935 -7.88049  18.29063  1.000 29.62082 ? 6   PHE   B C   1 
ATOM   1940 O  O   . PHE   B 2 7   ? -16.32485 -7.87643  17.93842  1.000 25.38527 ? 6   PHE   B O   1 
ATOM   1941 C  CB  . PHE   B 2 7   ? -17.75584 -6.36004  20.21008  1.000 28.08335 ? 6   PHE   B CB  1 
ATOM   1942 C  CG  . PHE   B 2 7   ? -18.35122 -5.13878  20.83507  1.000 29.34241 ? 6   PHE   B CG  1 
ATOM   1943 C  CD1 . PHE   B 2 7   ? -18.10361 -3.88129  20.30853  1.000 36.66806 ? 6   PHE   B CD1 1 
ATOM   1944 C  CD2 . PHE   B 2 7   ? -19.15270 -5.25449  21.95931  1.000 32.88566 ? 6   PHE   B CD2 1 
ATOM   1945 C  CE1 . PHE   B 2 7   ? -18.65422 -2.75134  20.89473  1.000 37.72639 ? 6   PHE   B CE1 1 
ATOM   1946 C  CE2 . PHE   B 2 7   ? -19.70555 -4.12864  22.55279  1.000 38.56244 ? 6   PHE   B CE2 1 
ATOM   1947 C  CZ  . PHE   B 2 7   ? -19.45413 -2.87866  22.01756  1.000 38.84905 ? 6   PHE   B CZ  1 
ATOM   1948 N  N   . TRP   B 2 8   ? -18.24986 -8.98378  18.31854  1.000 26.34749 ? 7   TRP   B N   1 
ATOM   1949 C  CA  . TRP   B 2 8   ? -17.65062 -10.30856 18.31077  1.000 25.30003 ? 7   TRP   B CA  1 
ATOM   1950 C  C   . TRP   B 2 8   ? -17.96740 -11.09880 17.05612  1.000 25.40431 ? 7   TRP   B C   1 
ATOM   1951 O  O   . TRP   B 2 8   ? -17.24231 -12.02498 16.73154  1.000 24.85514 ? 7   TRP   B O   1 
ATOM   1952 C  CB  . TRP   B 2 8   ? -18.11166 -11.07371 19.56895  1.000 25.14868 ? 7   TRP   B CB  1 
ATOM   1953 C  CG  . TRP   B 2 8   ? -19.59621 -10.92166 19.87703  1.000 25.85366 ? 7   TRP   B CG  1 
ATOM   1954 C  CD1 . TRP   B 2 8   ? -20.19490 -9.96441  20.66002  1.000 29.48202 ? 7   TRP   B CD1 1 
ATOM   1955 C  CD2 . TRP   B 2 8   ? -20.65620 -11.76744 19.40332  1.000 26.19364 ? 7   TRP   B CD2 1 
ATOM   1956 N  NE1 . TRP   B 2 8   ? -21.55790 -10.16069 20.68314  1.000 33.02251 ? 7   TRP   B NE1 1 
ATOM   1957 C  CE2 . TRP   B 2 8   ? -21.86382 -11.26121 19.92804  1.000 27.05273 ? 7   TRP   B CE2 1 
ATOM   1958 C  CE3 . TRP   B 2 8   ? -20.69885 -12.90125 18.58710  1.000 27.60553 ? 7   TRP   B CE3 1 
ATOM   1959 C  CZ2 . TRP   B 2 8   ? -23.10431 -11.86075 19.66993  1.000 33.51558 ? 7   TRP   B CZ2 1 
ATOM   1960 C  CZ3 . TRP   B 2 8   ? -21.93705 -13.48711 18.31813  1.000 29.45659 ? 7   TRP   B CZ3 1 
ATOM   1961 C  CH2 . TRP   B 2 8   ? -23.11813 -12.96806 18.86443  1.000 33.27460 ? 7   TRP   B CH2 1 
HETATM 1962 C  C10 . A1BDE B 2 9   ? -16.23508 -15.96335 15.56915  1.000 27.21218 ? 8   A1BDE B C10 1 
HETATM 1963 C  C13 . A1BDE B 2 9   ? -14.64761 -14.08502 16.11434  1.000 28.26508 ? 8   A1BDE B C13 1 
HETATM 1964 C  CG  . A1BDE B 2 9   ? -19.97707 -13.62182 15.39057  1.000 26.41421 ? 8   A1BDE B CG  1 
HETATM 1965 C  CE  . A1BDE B 2 9   ? -18.40131 -15.45829 14.43662  1.000 35.82708 ? 8   A1BDE B CE  1 
HETATM 1966 C  CD  . A1BDE B 2 9   ? -19.32994 -14.23756 14.11389  1.000 26.63298 ? 8   A1BDE B CD  1 
HETATM 1967 C  CB  . A1BDE B 2 9   ? -20.46080 -12.20791 15.08593  1.000 26.57178 ? 8   A1BDE B CB  1 
HETATM 1968 C  CA  . A1BDE B 2 9   ? -19.25446 -11.20617 14.94535  1.000 26.28057 ? 8   A1BDE B CA  1 
HETATM 1969 C  C   . A1BDE B 2 9   ? -19.67856 -10.14571 13.95495  1.000 26.91105 ? 8   A1BDE B C   1 
HETATM 1970 C  C12 . A1BDE B 2 9   ? -15.01296 -15.56807 16.38254  1.000 26.62650 ? 8   A1BDE B C12 1 
HETATM 1971 N  N   . A1BDE B 2 9   ? -18.99065 -10.58112 16.20319  1.000 26.14746 ? 8   A1BDE B N   1 
HETATM 1972 N  NZ  . A1BDE B 2 9   ? -17.25500 -14.97320 15.24206  1.000 30.22106 ? 8   A1BDE B NZ  1 
HETATM 1973 N  N14 . A1BDE B 2 9   ? -13.97261 -16.44565 15.93584  1.000 24.32565 ? 8   A1BDE B N14 1 
HETATM 1974 O  O   . A1BDE B 2 9   ? -20.15943 -10.46512 12.87209  1.000 27.21341 ? 8   A1BDE B O   1 
HETATM 1975 O  O11 . A1BDE B 2 9   ? -16.35245 -17.09904 15.20344  1.000 28.45592 ? 8   A1BDE B O11 1 
HETATM 1976 O  O15 . A1BDE B 2 9   ? -14.05167 -13.98176 14.83572  1.000 25.09197 ? 8   A1BDE B O15 1 
ATOM   1977 N  N   . GLY   B 2 10  ? -19.19734 -8.82981  14.22720  1.000 26.99913 ? 9   GLY   B N   1 
ATOM   1978 C  CA  . GLY   B 2 10  ? -19.61597 -7.87883  13.19539  1.000 27.60999 ? 9   GLY   B CA  1 
ATOM   1979 C  C   . GLY   B 2 10  ? -21.11996 -7.71405  12.99097  1.000 29.09024 ? 9   GLY   B C   1 
ATOM   1980 O  O   . GLY   B 2 10  ? -21.90572 -7.92430  13.91733  1.000 28.59540 ? 9   GLY   B O   1 
ATOM   1981 N  N   . SER   B 2 11  ? -21.52552 -7.31640  11.77847  1.000 28.89705 ? 10  SER   B N   1 
ATOM   1982 C  CA  . SER   B 2 11  ? -22.94837 -7.21622  11.43194  1.000 31.52887 ? 10  SER   B CA  1 
ATOM   1983 C  C   . SER   B 2 11  ? -23.50570 -8.62477  11.30606  1.000 29.87792 ? 10  SER   B C   1 
ATOM   1984 O  O   . SER   B 2 11  ? -23.32070 -9.29325  10.28625  1.000 32.11836 ? 10  SER   B O   1 
ATOM   1985 C  CB  . SER   B 2 11  ? -23.14773 -6.44110  10.13081  1.000 36.94055 ? 10  SER   B CB  1 
ATOM   1986 O  OG  . SER   B 2 11  ? -22.64791 -5.12052  10.22247  1.000 44.42871 ? 10  SER   B OG  1 
ATOM   1987 N  N   . HIS   B 2 12  ? -24.19366 -9.09348  12.33948  1.000 29.62133 ? 11  HIS   B N   1 
ATOM   1988 C  CA  . HIS   B 2 12  ? -24.53033 -10.50337 12.46492  1.000 29.38464 ? 11  HIS   B CA  1 
ATOM   1989 C  C   . HIS   B 2 12  ? -26.02872 -10.70081 12.32373  1.000 30.08614 ? 11  HIS   B C   1 
ATOM   1990 O  O   . HIS   B 2 12  ? -26.81293 -9.97005  12.93745  1.000 30.57355 ? 11  HIS   B O   1 
ATOM   1991 C  CB  . HIS   B 2 12  ? -24.05822 -11.05348 13.81148  1.000 28.80472 ? 11  HIS   B CB  1 
ATOM   1992 C  CG  . HIS   B 2 12  ? -24.18171 -12.54081 13.92104  1.000 28.45182 ? 11  HIS   B CG  1 
ATOM   1993 N  ND1 . HIS   B 2 12  ? -23.48475 -13.40194 13.10151  1.000 28.00631 ? 11  HIS   B ND1 1 
ATOM   1994 C  CD2 . HIS   B 2 12  ? -24.90977 -13.31969 14.75724  1.000 28.47740 ? 11  HIS   B CD2 1 
ATOM   1995 C  CE1 . HIS   B 2 12  ? -23.77527 -14.64895 13.42918  1.000 27.77163 ? 11  HIS   B CE1 1 
ATOM   1996 N  NE2 . HIS   B 2 12  ? -24.65277 -14.62737 14.41931  1.000 28.05873 ? 11  HIS   B NE2 1 
ATOM   1997 N  N   . ARG   B 2 13  ? -26.42196 -11.67872 11.50471  1.000 30.14394 ? 12  ARG   B N   1 
ATOM   1998 C  CA  . ARG   B 2 13  ? -27.83284 -12.03508 11.37237  1.000 30.76489 ? 12  ARG   B CA  1 
ATOM   1999 C  C   . ARG   B 2 13  ? -28.15384 -13.01942 12.48637  1.000 30.48860 ? 12  ARG   B C   1 
ATOM   2000 O  O   . ARG   B 2 13  ? -27.80981 -14.20061 12.41713  1.000 30.01930 ? 12  ARG   B O   1 
ATOM   2001 C  CB  . ARG   B 2 13  ? -28.13114 -12.61801 9.99803   1.000 30.97632 ? 12  ARG   B CB  1 
ATOM   2002 C  CG  . ARG   B 2 13  ? -29.61774 -12.70300 9.69739   1.000 31.74075 ? 12  ARG   B CG  1 
ATOM   2003 C  CD  . ARG   B 2 13  ? -29.91823 -13.84056 8.73234   1.000 31.74917 ? 12  ARG   B CD  1 
ATOM   2004 N  NE  . ARG   B 2 13  ? -29.62533 -15.14504 9.30249   1.000 31.16856 ? 12  ARG   B NE  1 
ATOM   2005 C  CZ  . ARG   B 2 13  ? -28.73265 -15.98927 8.80080   1.000 30.80273 ? 12  ARG   B CZ  1 
ATOM   2006 N  NH1 . ARG   B 2 13  ? -28.00636 -15.67435 7.73485   1.000 30.48253 ? 12  ARG   B NH1 1 
ATOM   2007 N  NH2 . ARG   B 2 13  ? -28.54621 -17.16515 9.39573   1.000 30.09482 ? 12  ARG   B NH2 1 
ATOM   2008 N  N   . GLN   B 2 14  ? -28.77459 -12.52038 13.55086  1.000 30.76272 ? 13  GLN   B N   1 
ATOM   2009 C  CA  . GLN   B 2 14  ? -28.93116 -13.31178 14.76636  1.000 30.44697 ? 13  GLN   B CA  1 
ATOM   2010 C  C   . GLN   B 2 14  ? -30.25601 -14.06630 14.75364  1.000 30.90449 ? 13  GLN   B C   1 
ATOM   2011 O  O   . GLN   B 2 14  ? -31.14110 -13.86689 15.58927  1.000 31.97043 ? 13  GLN   B O   1 
ATOM   2012 C  CB  . GLN   B 2 14  ? -28.80625 -12.42389 15.99878  1.000 31.22969 ? 13  GLN   B CB  1 
ATOM   2013 C  CG  . GLN   B 2 14  ? -28.43074 -13.21859 17.22701  1.000 29.94730 ? 13  GLN   B CG  1 
ATOM   2014 C  CD  . GLN   B 2 14  ? -28.01840 -12.33334 18.37953  1.000 29.78296 ? 13  GLN   B CD  1 
ATOM   2015 O  OE1 . GLN   B 2 14  ? -28.76783 -11.45507 18.79189  1.000 35.37399 ? 13  GLN   B OE1 1 
ATOM   2016 N  NE2 . GLN   B 2 14  ? -26.81847 -12.55473 18.89919  1.000 32.24600 ? 13  GLN   B NE2 1 
ATOM   2017 N  N   . CYS   B 2 15  ? -30.36777 -14.94876 13.77053  1.000 30.87991 ? 14  CYS   B N   1 
ATOM   2018 C  CA  . CYS   B 2 15  ? -31.56425 -15.73581 13.54382  1.000 31.30502 ? 14  CYS   B CA  1 
ATOM   2019 C  C   . CYS   B 2 15  ? -31.31383 -16.71752 12.40490  1.000 31.77325 ? 14  CYS   B C   1 
ATOM   2020 O  O   . CYS   B 2 15  ? -30.41091 -16.51793 11.57988  1.000 30.83831 ? 14  CYS   B O   1 
ATOM   2021 C  CB  . CYS   B 2 15  ? -32.74994 -14.83269 13.19277  1.000 32.18380 ? 14  CYS   B CB  1 
ATOM   2022 S  SG  . CYS   B 2 15  ? -32.42867 -13.79616 11.74014  1.000 32.52430 ? 14  CYS   B SG  1 
HETATM 2023 N  N   . NH2   B 2 16  ? -32.13162 -17.76342 12.34104  1.000 31.25748 ? 15  NH2   B N   1 
HETATM 2024 CO CO  . CO    C 3 .   ? -12.88467 -15.62909 14.27484  1.000 20.69312 ? 301 CO    A CO  1 
HETATM 2025 CL CL  . CL    D 4 .   ? -24.91989 -31.17159 21.37024  1.000 39.40342 ? 302 CL    A CL  1 
HETATM 2026 C  C1  . GOL   E 5 .   ? -23.63450 -23.95548 11.27464  1.000 33.19433 ? 303 GOL   A C1  1 
HETATM 2027 O  O1  . GOL   E 5 .   ? -22.61830 -23.41584 10.49741  1.000 39.19184 ? 303 GOL   A O1  1 
HETATM 2028 C  C2  . GOL   E 5 .   ? -23.70876 -25.44296 10.88893  1.000 40.72193 ? 303 GOL   A C2  1 
HETATM 2029 O  O2  . GOL   E 5 .   ? -22.65159 -26.17141 11.41935  1.000 35.52175 ? 303 GOL   A O2  1 
HETATM 2030 C  C3  . GOL   E 5 .   ? -25.06993 -25.92014 11.42290  1.000 45.40527 ? 303 GOL   A C3  1 
HETATM 2031 O  O3  . GOL   E 5 .   ? -24.84842 -27.16896 12.00535  1.000 54.15009 ? 303 GOL   A O3  1 
HETATM 2032 C  C1  . GOL   F 5 .   ? -2.10120  -21.92188 13.70474  1.000 37.47519 ? 304 GOL   A C1  1 
HETATM 2033 O  O1  . GOL   F 5 .   ? -1.04054  -22.03052 12.76476  1.000 44.20086 ? 304 GOL   A O1  1 
HETATM 2034 C  C2  . GOL   F 5 .   ? -2.70863  -20.52063 13.48255  1.000 36.15583 ? 304 GOL   A C2  1 
HETATM 2035 O  O2  . GOL   F 5 .   ? -1.76470  -19.51733 13.70927  1.000 37.78384 ? 304 GOL   A O2  1 
HETATM 2036 C  C3  . GOL   F 5 .   ? -3.92661  -20.41536 14.45073  1.000 45.40604 ? 304 GOL   A C3  1 
HETATM 2037 O  O3  . GOL   F 5 .   ? -4.46460  -19.12810 14.25700  1.000 38.56794 ? 304 GOL   A O3  1 
HETATM 2038 C  C1  . GOL   G 5 .   ? -14.31745 -16.45606 -15.47611 1.000 48.24115 ? 305 GOL   A C1  1 
HETATM 2039 O  O1  . GOL   G 5 .   ? -13.31167 -17.34585 -15.86549 1.000 47.31724 ? 305 GOL   A O1  1 
HETATM 2040 C  C2  . GOL   G 5 .   ? -13.67983 -15.04509 -15.39158 1.000 54.69572 ? 305 GOL   A C2  1 
HETATM 2041 O  O2  . GOL   G 5 .   ? -14.52442 -14.11981 -14.78243 1.000 52.91256 ? 305 GOL   A O2  1 
HETATM 2042 C  C3  . GOL   G 5 .   ? -12.36542 -15.23743 -14.60151 1.000 48.41091 ? 305 GOL   A C3  1 
HETATM 2043 O  O3  . GOL   G 5 .   ? -11.67371 -14.03760 -14.70129 1.000 58.83769 ? 305 GOL   A O3  1 
HETATM 2044 C  C1  . GOL   H 5 .   ? -23.67089 -21.28862 32.33367  1.000 40.63348 ? 306 GOL   A C1  1 
HETATM 2045 O  O1  . GOL   H 5 .   ? -25.03558 -21.40250 32.52404  1.000 52.58935 ? 306 GOL   A O1  1 
HETATM 2046 C  C2  . GOL   H 5 .   ? -23.06223 -22.72072 32.31519  1.000 48.44771 ? 306 GOL   A C2  1 
HETATM 2047 O  O2  . GOL   H 5 .   ? -21.99177 -22.76949 31.45156  1.000 35.48589 ? 306 GOL   A O2  1 
HETATM 2048 C  C3  . GOL   H 5 .   ? -22.63028 -23.00694 33.79734  1.000 48.23538 ? 306 GOL   A C3  1 
HETATM 2049 O  O3  . GOL   H 5 .   ? -21.81559 -24.16322 33.80861  1.000 39.24660 ? 306 GOL   A O3  1 
HETATM 2050 C  C1  . GOL   I 5 .   ? 3.47525   -5.80890  7.06141   1.000 70.92060 ? 307 GOL   A C1  1 
HETATM 2051 O  O1  . GOL   I 5 .   ? 4.70725   -5.18118  6.81710   1.000 73.86805 ? 307 GOL   A O1  1 
HETATM 2052 C  C2  . GOL   I 5 .   ? 2.91145   -6.12274  5.66827   1.000 73.72841 ? 307 GOL   A C2  1 
HETATM 2053 O  O2  . GOL   I 5 .   ? 2.79007   -7.48399  5.43149   1.000 71.68252 ? 307 GOL   A O2  1 
HETATM 2054 C  C3  . GOL   I 5 .   ? 1.54710   -5.40784  5.61199   1.000 66.38582 ? 307 GOL   A C3  1 
HETATM 2055 O  O3  . GOL   I 5 .   ? 1.77590   -4.06661  5.94025   1.000 69.85945 ? 307 GOL   A O3  1 
HETATM 2056 H  H11 . GOL   I 5 .   ? 2.85331   -5.24909  7.55204   1.000 85.10472 ? 307 GOL   A H11 1 
HETATM 2057 H  H12 . GOL   I 5 .   ? 3.55997   -6.62654  7.57637   1.000 85.10472 ? 307 GOL   A H12 1 
HETATM 2058 H  HO1 . GOL   I 5 .   ? 4.55397   -4.57230  6.22626   1.000 88.64166 ? 307 GOL   A HO1 1 
HETATM 2059 H  H2  . GOL   I 5 .   ? 3.51576   -5.78719  4.98774   1.000 88.47410 ? 307 GOL   A H2  1 
HETATM 2060 H  HO2 . GOL   I 5 .   ? 2.42044   -7.82931  6.10347   1.000 86.01903 ? 307 GOL   A HO2 1 
HETATM 2061 H  H31 . GOL   I 5 .   ? 1.16610   -5.52800  4.72807   1.000 79.66299 ? 307 GOL   A H31 1 
HETATM 2062 H  H32 . GOL   I 5 .   ? 0.93430   -5.85309  6.21790   1.000 79.66299 ? 307 GOL   A H32 1 
HETATM 2063 H  HO3 . GOL   I 5 .   ? 2.42463   -3.81825  5.44644   1.000 83.83134 ? 307 GOL   A HO3 1 
HETATM 2064 C  C1  . GOL   J 5 .   ? -26.70908 -11.86908 28.13129  1.000 54.08803 ? 308 GOL   A C1  1 
HETATM 2065 O  O1  . GOL   J 5 .   ? -27.11079 -12.58260 29.25148  1.000 56.40092 ? 308 GOL   A O1  1 
HETATM 2066 C  C2  . GOL   J 5 .   ? -27.52730 -12.40004 26.95977  1.000 44.70525 ? 308 GOL   A C2  1 
HETATM 2067 O  O2  . GOL   J 5 .   ? -27.85441 -13.73129 27.10389  1.000 45.89177 ? 308 GOL   A O2  1 
HETATM 2068 C  C3  . GOL   J 5 .   ? -26.62494 -12.19554 25.74245  1.000 47.20109 ? 308 GOL   A C3  1 
HETATM 2069 O  O3  . GOL   J 5 .   ? -27.42656 -11.70706 24.69149  1.000 49.41366 ? 308 GOL   A O3  1 
HETATM 2070 H  H11 . GOL   J 5 .   ? -25.76416 -11.97439 27.93908  1.000 64.90564 ? 308 GOL   A H11 1 
HETATM 2071 H  H12 . GOL   J 5 .   ? -26.85704 -10.91474 28.22212  1.000 64.90564 ? 308 GOL   A H12 1 
HETATM 2072 H  HO1 . GOL   J 5 .   ? -27.49535 -13.29112 28.96375  1.000 67.68110 ? 308 GOL   A HO1 1 
HETATM 2073 H  H2  . GOL   J 5 .   ? -28.36390 -11.91402 26.89059  1.000 53.64630 ? 308 GOL   A H2  1 
HETATM 2074 H  HO2 . GOL   J 5 .   ? -28.15138 -13.99636 26.34869  1.000 55.07012 ? 308 GOL   A HO2 1 
HETATM 2075 H  H31 . GOL   J 5 .   ? -26.19176 -13.03778 25.53296  1.000 56.64131 ? 308 GOL   A H31 1 
HETATM 2076 H  H32 . GOL   J 5 .   ? -25.90639 -11.59174 25.98741  1.000 56.64131 ? 308 GOL   A H32 1 
HETATM 2077 H  HO3 . GOL   J 5 .   ? -27.91503 -12.35628 24.44637  1.000 59.29639 ? 308 GOL   A HO3 1 
HETATM 2078 S  S   . SCN   K 6 .   ? -11.56010 -37.54288 15.30935  1.000 83.80143 ? 309 SCN   A S   1 
HETATM 2079 C  C   . SCN   K 6 .   ? -10.57151 -36.89592 16.66939  1.000 56.52866 ? 309 SCN   A C   1 
HETATM 2080 N  N   . SCN   K 6 .   ? -9.92458  -36.45015 17.55492  1.000 52.68430 ? 309 SCN   A N   1 
HETATM 2081 S  S   . SCN   L 6 .   ? -6.97551  -27.46327 -2.89269  1.000 92.19941 ? 310 SCN   A S   1 
HETATM 2082 C  C   . SCN   L 6 .   ? -8.64699  -27.37932 -2.22801  1.000 63.20906 ? 310 SCN   A C   1 
HETATM 2083 N  N   . SCN   L 6 .   ? -9.74111  -27.32188 -1.79003  1.000 62.48582 ? 310 SCN   A N   1 
HETATM 2084 S  S   . SCN   M 6 .   ? -3.73921  -3.38130  9.14575   1.000 88.26390 ? 311 SCN   A S   1 
HETATM 2085 C  C   . SCN   M 6 .   ? -4.77734  -4.19034  7.91561   1.000 59.66130 ? 311 SCN   A C   1 
HETATM 2086 N  N   . SCN   M 6 .   ? -5.46124  -4.73642  7.11984   1.000 62.13200 ? 311 SCN   A N   1 
HETATM 2087 S  S   . SCN   N 6 .   ? -10.10973 -27.27850 4.24909   1.000 92.84763 ? 312 SCN   A S   1 
HETATM 2088 C  C   . SCN   N 6 .   ? -10.10214 -27.44367 2.45264   1.000 71.22795 ? 312 SCN   A C   1 
HETATM 2089 N  N   . SCN   N 6 .   ? -10.09568 -27.55197 1.27408   1.000 65.55324 ? 312 SCN   A N   1 
HETATM 2090 C  C1  . GOL   O 5 .   ? -33.73763 -4.29810  14.85226  1.000 56.68573 ? 101 GOL   B C1  1 
HETATM 2091 O  O1  . GOL   O 5 .   ? -34.75836 -4.40753  15.79022  1.000 61.60112 ? 101 GOL   B O1  1 
HETATM 2092 C  C2  . GOL   O 5 .   ? -32.50852 -5.06398  15.41729  1.000 58.72119 ? 101 GOL   B C2  1 
HETATM 2093 O  O2  . GOL   O 5 .   ? -32.83018 -6.36263  15.77948  1.000 59.31338 ? 101 GOL   B O2  1 
HETATM 2094 C  C3  . GOL   O 5 .   ? -31.99837 -4.22409  16.61490  1.000 54.07299 ? 101 GOL   B C3  1 
HETATM 2095 O  O3  . GOL   O 5 .   ? -31.24008 -3.17766  16.07841  1.000 63.47497 ? 101 GOL   B O3  1 
HETATM 2096 C  C1  . GOL   P 5 .   ? -29.01878 -3.08414  12.64881  1.000 57.61252 ? 102 GOL   B C1  1 
HETATM 2097 O  O1  . GOL   P 5 .   ? -29.95093 -3.24615  13.68649  1.000 68.89879 ? 102 GOL   B O1  1 
HETATM 2098 C  C2  . GOL   P 5 .   ? -29.74048 -2.33633  11.48100  1.000 68.90345 ? 102 GOL   B C2  1 
HETATM 2099 O  O2  . GOL   P 5 .   ? -28.84963 -1.62365  10.68833  1.000 74.63524 ? 102 GOL   B O2  1 
HETATM 2100 C  C3  . GOL   P 5 .   ? -30.47740 -3.43792  10.67256  1.000 65.87120 ? 102 GOL   B C3  1 
HETATM 2101 O  O3  . GOL   P 5 .   ? -31.83144 -3.37106  11.01416  1.000 68.07272 ? 102 GOL   B O3  1 
HETATM 2102 O  O   . HOH   Q 7 .   ? -9.81608  -24.14572 -3.99636  1.000 49.97426 ? 401 HOH   A O   1 
HETATM 2103 O  O   . HOH   Q 7 .   ? -19.61404 -10.28183 2.52382   1.000 45.90652 ? 402 HOH   A O   1 
HETATM 2104 O  O   . HOH   Q 7 .   ? -0.67250  -15.86831 36.58507  1.000 56.67103 ? 403 HOH   A O   1 
HETATM 2105 O  O   . HOH   Q 7 .   ? -13.315   5.980     22.824    1.000 39.42829 ? 404 HOH   A O   1 
HETATM 2106 O  O   . HOH   Q 7 .   ? -20.22003 -0.31178  14.56781  1.000 54.97829 ? 405 HOH   A O   1 
HETATM 2107 O  O   . HOH   Q 7 .   ? -23.57742 -18.25188 2.33124   1.000 44.67215 ? 406 HOH   A O   1 
HETATM 2108 O  O   . HOH   Q 7 .   ? -34.05040 -32.97155 19.11783  1.000 51.78167 ? 407 HOH   A O   1 
HETATM 2109 O  O   . HOH   Q 7 .   ? -22.56807 -23.01740 -13.15350 1.000 50.79863 ? 408 HOH   A O   1 
HETATM 2110 O  O   . HOH   Q 7 .   ? 5.42163   -15.75284 23.41966  1.000 47.72791 ? 409 HOH   A O   1 
HETATM 2111 O  O   . HOH   Q 7 .   ? -23.16977 -23.34632 8.06227   1.000 41.94266 ? 410 HOH   A O   1 
HETATM 2112 O  O   . HOH   Q 7 .   ? -16.368   -10.754   -17.547   1.000 46.41338 ? 411 HOH   A O   1 
HETATM 2113 O  O   . HOH   Q 7 .   ? -20.71702 -4.59472  26.06468  1.000 49.34109 ? 412 HOH   A O   1 
HETATM 2114 O  O   . HOH   Q 7 .   ? -21.17599 -10.65218 9.03423   1.000 31.74473 ? 413 HOH   A O   1 
HETATM 2115 O  O   . HOH   Q 7 .   ? -27.83870 -16.74192 3.90856   1.000 46.28376 ? 414 HOH   A O   1 
HETATM 2116 O  O   . HOH   Q 7 .   ? -0.83909  -16.83465 13.25185  1.000 38.28553 ? 415 HOH   A O   1 
HETATM 2117 O  O   . HOH   Q 7 .   ? -19.60929 -29.18666 11.17777  1.000 46.86346 ? 416 HOH   A O   1 
HETATM 2118 O  O   . HOH   Q 7 .   ? -10.53500 -9.53732  4.56536   1.000 44.04737 ? 417 HOH   A O   1 
HETATM 2119 O  O   . HOH   Q 7 .   ? -33.60875 -30.97367 13.42976  1.000 48.55266 ? 418 HOH   A O   1 
HETATM 2120 O  O   . HOH   Q 7 .   ? -31.764   -19.916   10.233    1.000 39.58765 ? 419 HOH   A O   1 
HETATM 2121 O  O   . HOH   Q 7 .   ? -4.36761  -11.79990 5.54306   1.000 43.97093 ? 420 HOH   A O   1 
HETATM 2122 O  O   . HOH   Q 7 .   ? -16.95118 -22.71359 6.23193   1.000 30.61058 ? 421 HOH   A O   1 
HETATM 2123 O  O   . HOH   Q 7 .   ? -21.08305 -14.92302 -3.29172  1.000 44.23992 ? 422 HOH   A O   1 
HETATM 2124 O  O   . HOH   Q 7 .   ? -21.90919 -25.60695 30.79876  1.000 28.73905 ? 423 HOH   A O   1 
HETATM 2125 O  O   . HOH   Q 7 .   ? -26.28324 -11.85514 31.66382  1.000 40.22605 ? 424 HOH   A O   1 
HETATM 2126 O  O   . HOH   Q 7 .   ? -22.46275 -11.31221 29.20883  1.000 38.06743 ? 425 HOH   A O   1 
HETATM 2127 O  O   . HOH   Q 7 .   ? -7.46767  -2.18413  12.54166  1.000 46.93098 ? 426 HOH   A O   1 
HETATM 2128 O  O   . HOH   Q 7 .   ? -18.28540 -19.35445 5.40485   1.000 39.83387 ? 427 HOH   A O   1 
HETATM 2129 O  O   . HOH   Q 7 .   ? -8.15406  -1.72264  26.06135  1.000 33.58095 ? 428 HOH   A O   1 
HETATM 2130 O  O   . HOH   Q 7 .   ? -1.44675  -21.57391 10.16890  1.000 34.15522 ? 429 HOH   A O   1 
HETATM 2131 O  O   . HOH   Q 7 .   ? -20.72276 -26.27865 23.75444  1.000 21.99778 ? 430 HOH   A O   1 
HETATM 2132 O  O   . HOH   Q 7 .   ? -18.48030 -30.32115 13.25389  1.000 34.48068 ? 431 HOH   A O   1 
HETATM 2133 O  O   . HOH   Q 7 .   ? 2.03111   -20.72726 5.57124   1.000 43.84096 ? 432 HOH   A O   1 
HETATM 2134 O  O   . HOH   Q 7 .   ? -13.16589 -11.06527 38.88187  1.000 32.55194 ? 433 HOH   A O   1 
HETATM 2135 O  O   . HOH   Q 7 .   ? -9.17738  -15.31010 17.24040  1.000 32.32903 ? 434 HOH   A O   1 
HETATM 2136 O  O   . HOH   Q 7 .   ? -10.43829 -29.55098 25.54099  1.000 29.60925 ? 435 HOH   A O   1 
HETATM 2137 O  O   . HOH   Q 7 .   ? -4.46336  -31.51447 22.13648  1.000 35.20015 ? 436 HOH   A O   1 
HETATM 2138 O  O   . HOH   Q 7 .   ? -6.59543  -7.64396  7.56934   1.000 32.54027 ? 437 HOH   A O   1 
HETATM 2139 O  O   . HOH   Q 7 .   ? -17.91988 -21.72860 3.96148   1.000 46.73157 ? 438 HOH   A O   1 
HETATM 2140 O  O   . HOH   Q 7 .   ? 0.44569   -20.74524 -8.71767  1.000 61.43805 ? 439 HOH   A O   1 
HETATM 2141 O  O   . HOH   Q 7 .   ? -11.58205 -15.15804 16.00301  1.000 27.01665 ? 440 HOH   A O   1 
HETATM 2142 O  O   . HOH   Q 7 .   ? -19.51814 -32.03844 32.11668  1.000 37.42871 ? 441 HOH   A O   1 
HETATM 2143 O  O   . HOH   Q 7 .   ? -19.57374 -11.03242 -9.31108  1.000 37.34380 ? 442 HOH   A O   1 
HETATM 2144 O  O   . HOH   Q 7 .   ? -2.08626  -28.79450 20.10130  1.000 37.28577 ? 443 HOH   A O   1 
HETATM 2145 O  O   . HOH   Q 7 .   ? -21.87938 -28.55981 10.43494  1.000 46.48839 ? 444 HOH   A O   1 
HETATM 2146 O  O   . HOH   Q 7 .   ? -29.36957 -18.09771 24.85281  1.000 48.53157 ? 445 HOH   A O   1 
HETATM 2147 O  O   . HOH   Q 7 .   ? -25.38678 -19.38051 30.34795  1.000 26.71276 ? 446 HOH   A O   1 
HETATM 2148 O  O   . HOH   Q 7 .   ? -23.38619 -12.95906 27.41797  1.000 29.86088 ? 447 HOH   A O   1 
HETATM 2149 O  O   . HOH   Q 7 .   ? -26.12005 -29.97148 17.11289  1.000 39.52970 ? 448 HOH   A O   1 
HETATM 2150 O  O   . HOH   Q 7 .   ? -11.93122 -26.20664 10.23236  1.000 26.28497 ? 449 HOH   A O   1 
HETATM 2151 O  O   . HOH   Q 7 .   ? -13.51343 -24.88536 4.49514   1.000 48.75438 ? 450 HOH   A O   1 
HETATM 2152 O  O   . HOH   Q 7 .   ? -31.41828 -27.32868 13.42981  1.000 36.29690 ? 451 HOH   A O   1 
HETATM 2153 O  O   . HOH   Q 7 .   ? -15.71480 -26.41821 34.59887  1.000 39.00172 ? 452 HOH   A O   1 
HETATM 2154 O  O   . HOH   Q 7 .   ? -9.13171  -34.61688 20.80781  1.000 39.28474 ? 453 HOH   A O   1 
HETATM 2155 O  O   . HOH   Q 7 .   ? -10.09482 -25.97695 30.24451  1.000 32.96250 ? 454 HOH   A O   1 
HETATM 2156 O  O   . HOH   Q 7 .   ? -5.02878  -31.75134 19.35347  1.000 39.21516 ? 455 HOH   A O   1 
HETATM 2157 O  O   . HOH   Q 7 .   ? -7.24382  -33.98494 18.73364  1.000 42.64037 ? 456 HOH   A O   1 
HETATM 2158 O  O   . HOH   Q 7 .   ? -17.54594 -31.88794 24.76411  1.000 35.05687 ? 457 HOH   A O   1 
HETATM 2159 O  O   . HOH   Q 7 .   ? -4.68535  -24.95750 12.27584  1.000 27.01267 ? 458 HOH   A O   1 
HETATM 2160 O  O   . HOH   Q 7 .   ? -8.30698  -10.83179 5.48355   1.000 41.12970 ? 459 HOH   A O   1 
HETATM 2161 O  O   . HOH   Q 7 .   ? -0.96791  -13.83126 4.40734   1.000 39.38699 ? 460 HOH   A O   1 
HETATM 2162 O  O   . HOH   Q 7 .   ? -16.49627 -26.56163 -4.42551  1.000 44.74858 ? 461 HOH   A O   1 
HETATM 2163 O  O   . HOH   Q 7 .   ? -30.78530 -24.75404 14.12163  1.000 32.22992 ? 462 HOH   A O   1 
HETATM 2164 O  O   . HOH   Q 7 .   ? -12.27709 -14.53069 -10.49160 1.000 34.98539 ? 463 HOH   A O   1 
HETATM 2165 O  O   . HOH   Q 7 .   ? -24.50842 -11.21966 8.48254   1.000 35.61841 ? 464 HOH   A O   1 
HETATM 2166 O  O   . HOH   Q 7 .   ? -1.32633  -19.44985 16.42116  1.000 32.25944 ? 465 HOH   A O   1 
HETATM 2167 O  O   . HOH   Q 7 .   ? -15.12120 -13.07084 -3.33481  1.000 35.41357 ? 466 HOH   A O   1 
HETATM 2168 O  O   . HOH   Q 7 .   ? -14.93763 -11.48729 21.85224  1.000 26.77396 ? 467 HOH   A O   1 
HETATM 2169 O  O   . HOH   Q 7 .   ? -18.29883 -24.69893 -5.93408  1.000 44.57847 ? 468 HOH   A O   1 
HETATM 2170 O  O   . HOH   Q 7 .   ? -15.52554 -31.89323 21.22506  1.000 27.82265 ? 469 HOH   A O   1 
HETATM 2171 O  O   . HOH   Q 7 .   ? -1.60336  -6.75303  33.10978  1.000 37.60651 ? 470 HOH   A O   1 
HETATM 2172 O  O   . HOH   Q 7 .   ? -18.40899 -6.93732  33.73221  1.000 44.57438 ? 471 HOH   A O   1 
HETATM 2173 O  O   . HOH   Q 7 .   ? -11.93722 0.21236   18.21926  1.000 51.63815 ? 472 HOH   A O   1 
HETATM 2174 O  O   . HOH   Q 7 .   ? -6.72564  -2.71711  19.45913  1.000 32.12969 ? 473 HOH   A O   1 
HETATM 2175 O  O   . HOH   Q 7 .   ? -6.61224  -18.34609 12.30052  1.000 28.93822 ? 474 HOH   A O   1 
HETATM 2176 O  O   . HOH   Q 7 .   ? -18.09200 -2.14605  17.49311  1.000 50.08254 ? 475 HOH   A O   1 
HETATM 2177 O  O   . HOH   Q 7 .   ? -13.72436 -28.70970 7.73598   1.000 46.84303 ? 476 HOH   A O   1 
HETATM 2178 O  O   . HOH   Q 7 .   ? -20.03210 -12.16935 4.23974   1.000 31.91420 ? 477 HOH   A O   1 
HETATM 2179 O  O   . HOH   Q 7 .   ? -17.59840 -2.12727  33.18622  1.000 39.42875 ? 478 HOH   A O   1 
HETATM 2180 O  O   . HOH   Q 7 .   ? -17.023   -1.568    28.426    1.000 41.81263 ? 479 HOH   A O   1 
HETATM 2181 O  O   . HOH   Q 7 .   ? -36.57117 -26.53982 20.60008  1.000 38.00673 ? 480 HOH   A O   1 
HETATM 2182 O  O   . HOH   Q 7 .   ? -18.57440 -12.81576 -3.63266  1.000 45.33465 ? 481 HOH   A O   1 
HETATM 2183 O  O   . HOH   Q 7 .   ? -29.05278 -31.90759 14.26742  1.000 44.11980 ? 482 HOH   A O   1 
HETATM 2184 O  O   . HOH   Q 7 .   ? -18.99342 -32.64899 16.72954  1.000 28.43757 ? 483 HOH   A O   1 
HETATM 2185 O  O   . HOH   Q 7 .   ? -21.58105 -18.35448 6.90707   1.000 41.97704 ? 484 HOH   A O   1 
HETATM 2186 O  O   . HOH   Q 7 .   ? -25.48232 -34.74052 19.96991  1.000 38.04217 ? 485 HOH   A O   1 
HETATM 2187 O  O   . HOH   Q 7 .   ? -7.73148  -21.40605 -18.31969 1.000 42.19517 ? 486 HOH   A O   1 
HETATM 2188 O  O   . HOH   Q 7 .   ? -28.17356 -24.90095 12.61251  1.000 39.46370 ? 487 HOH   A O   1 
HETATM 2189 O  O   . HOH   Q 7 .   ? -20.98967 -9.99641  30.91124  1.000 51.70577 ? 488 HOH   A O   1 
HETATM 2190 O  O   . HOH   Q 7 .   ? 1.82887   -23.49580 6.43101   1.000 50.93324 ? 489 HOH   A O   1 
HETATM 2191 O  O   . HOH   Q 7 .   ? 9.32943   -4.55443  21.90469  1.000 54.64755 ? 490 HOH   A O   1 
HETATM 2192 O  O   . HOH   Q 7 .   ? 1.08145   -19.18565 10.53741  1.000 35.12827 ? 491 HOH   A O   1 
HETATM 2193 O  O   . HOH   Q 7 .   ? -24.19406 -23.43021 22.18851  1.000 22.45034 ? 492 HOH   A O   1 
HETATM 2194 O  O   . HOH   Q 7 .   ? -29.83071 -31.49797 20.38398  1.000 40.43441 ? 493 HOH   A O   1 
HETATM 2195 O  O   . HOH   Q 7 .   ? -24.50646 -15.45798 -11.62255 1.000 40.98629 ? 494 HOH   A O   1 
HETATM 2196 O  O   . HOH   Q 7 .   ? -20.618   -36.444   32.495    1.000 44.35407 ? 495 HOH   A O   1 
HETATM 2197 O  O   . HOH   Q 7 .   ? -34.579   -18.943   17.159    1.000 49.60149 ? 496 HOH   A O   1 
HETATM 2198 O  O   . HOH   Q 7 .   ? -28.299   -12.681   21.668    1.000 43.18972 ? 497 HOH   A O   1 
HETATM 2199 O  O   . HOH   Q 7 .   ? -24.35345 -11.99426 5.24272   1.000 41.69050 ? 498 HOH   A O   1 
HETATM 2200 O  O   . HOH   Q 7 .   ? -12.831   -26.290   -18.955   1.000 45.06260 ? 499 HOH   A O   1 
HETATM 2201 O  O   . HOH   Q 7 .   ? -24.14406 -25.38508 24.17319  1.000 31.69109 ? 500 HOH   A O   1 
HETATM 2202 O  O   . HOH   Q 7 .   ? -17.66742 -9.72636  33.12172  1.000 26.64317 ? 501 HOH   A O   1 
HETATM 2203 O  O   . HOH   Q 7 .   ? -1.38509  -13.19599 2.08220   1.000 53.41636 ? 502 HOH   A O   1 
HETATM 2204 O  O   . HOH   Q 7 .   ? -15.00814 -4.73775  6.68449   1.000 43.31543 ? 503 HOH   A O   1 
HETATM 2205 O  O   . HOH   Q 7 .   ? 1.50506   -20.27282 31.17926  1.000 48.53269 ? 504 HOH   A O   1 
HETATM 2206 O  O   . HOH   Q 7 .   ? -7.22733  -18.99773 14.91777  1.000 30.44252 ? 505 HOH   A O   1 
HETATM 2207 O  O   . HOH   Q 7 .   ? 1.84825   -2.13965  17.99564  1.000 55.71210 ? 506 HOH   A O   1 
HETATM 2208 O  O   . HOH   Q 7 .   ? -9.09612  -33.35120 11.71105  1.000 48.01501 ? 507 HOH   A O   1 
HETATM 2209 O  O   . HOH   Q 7 .   ? -27.38207 -22.91183 5.43109   1.000 44.29440 ? 508 HOH   A O   1 
HETATM 2210 O  O   . HOH   Q 7 .   ? -2.602    -29.122   17.472    1.000 41.35522 ? 509 HOH   A O   1 
HETATM 2211 O  O   . HOH   Q 7 .   ? -23.76840 -31.45659 28.86847  1.000 33.51119 ? 510 HOH   A O   1 
HETATM 2212 O  O   . HOH   Q 7 .   ? 0.43715   -21.08089 21.84246  1.000 44.96227 ? 511 HOH   A O   1 
HETATM 2213 O  O   . HOH   Q 7 .   ? -11.98215 -28.85064 30.05835  1.000 49.05997 ? 512 HOH   A O   1 
HETATM 2214 O  O   . HOH   Q 7 .   ? -9.50845  -17.08585 38.89370  1.000 31.64559 ? 513 HOH   A O   1 
HETATM 2215 O  O   . HOH   Q 7 .   ? 4.87118   -12.12370 21.16412  1.000 42.60049 ? 514 HOH   A O   1 
HETATM 2216 O  O   . HOH   Q 7 .   ? -2.84653  -8.78932  34.36734  1.000 33.89500 ? 515 HOH   A O   1 
HETATM 2217 O  O   . HOH   Q 7 .   ? -20.11609 -35.70720 23.98623  1.000 33.56975 ? 516 HOH   A O   1 
HETATM 2218 O  O   . HOH   Q 7 .   ? -5.90097  -12.69174 4.52838   1.000 40.39146 ? 517 HOH   A O   1 
HETATM 2219 O  O   . HOH   Q 7 .   ? -6.35348  -24.06077 22.92474  1.000 29.67785 ? 518 HOH   A O   1 
HETATM 2220 O  O   . HOH   Q 7 .   ? -11.07320 -10.46749 40.38075  1.000 44.98882 ? 519 HOH   A O   1 
HETATM 2221 O  O   . HOH   Q 7 .   ? -9.89296  -28.01388 -14.78166 1.000 63.17699 ? 520 HOH   A O   1 
HETATM 2222 O  O   . HOH   Q 7 .   ? -10.99973 -16.49227 36.59159  1.000 24.38727 ? 521 HOH   A O   1 
HETATM 2223 O  O   . HOH   Q 7 .   ? -4.15562  -32.05238 14.51162  1.000 35.81176 ? 522 HOH   A O   1 
HETATM 2224 O  O   . HOH   Q 7 .   ? -23.80060 -12.39927 31.21624  1.000 32.43512 ? 523 HOH   A O   1 
HETATM 2225 O  O   . HOH   Q 7 .   ? -33.310   -23.177   11.425    1.000 48.13206 ? 524 HOH   A O   1 
HETATM 2226 O  O   . HOH   Q 7 .   ? -27.14215 -22.37488 25.40297  1.000 46.19974 ? 525 HOH   A O   1 
HETATM 2227 O  O   . HOH   Q 7 .   ? -28.93470 -22.73996 22.82700  1.000 38.38101 ? 526 HOH   A O   1 
HETATM 2228 O  O   . HOH   Q 7 .   ? -22.00838 -22.26472 36.46672  1.000 49.99393 ? 527 HOH   A O   1 
HETATM 2229 O  O   . HOH   Q 7 .   ? -16.76144 -34.80007 14.44079  1.000 43.80604 ? 528 HOH   A O   1 
HETATM 2230 O  O   . HOH   Q 7 .   ? -11.72134 -26.80622 33.92398  1.000 36.57529 ? 529 HOH   A O   1 
HETATM 2231 O  O   . HOH   Q 7 .   ? -17.32871 -23.83185 -12.12244 1.000 31.63987 ? 530 HOH   A O   1 
HETATM 2232 O  O   . HOH   Q 7 .   ? 3.86822   -16.91323 25.70611  1.000 44.59079 ? 531 HOH   A O   1 
HETATM 2233 O  O   . HOH   Q 7 .   ? 0.605     -26.501   8.287     1.000 50.08783 ? 532 HOH   A O   1 
HETATM 2234 O  O   . HOH   Q 7 .   ? -1.78885  -28.16443 9.27590   1.000 44.08113 ? 533 HOH   A O   1 
HETATM 2235 O  O   . HOH   Q 7 .   ? -27.08344 -20.93541 3.33904   1.000 41.01910 ? 534 HOH   A O   1 
HETATM 2236 O  O   . HOH   Q 7 .   ? -18.13311 -4.87226  28.64467  1.000 34.84212 ? 535 HOH   A O   1 
HETATM 2237 O  O   . HOH   Q 7 .   ? -32.13496 -17.22378 2.81512   1.000 54.12781 ? 536 HOH   A O   1 
HETATM 2238 O  O   . HOH   Q 7 .   ? -6.96386  -16.94690 16.79221  1.000 26.69864 ? 537 HOH   A O   1 
HETATM 2239 O  O   . HOH   Q 7 .   ? -22.04122 -11.63678 33.58343  1.000 29.89227 ? 538 HOH   A O   1 
HETATM 2240 O  O   . HOH   Q 7 .   ? 1.35071   -20.37729 13.19605  1.000 40.15332 ? 539 HOH   A O   1 
HETATM 2241 O  O   . HOH   Q 7 .   ? -5.58375  -25.53819 30.06491  1.000 49.15565 ? 540 HOH   A O   1 
HETATM 2242 O  O   . HOH   Q 7 .   ? -12.95509 -31.62724 27.16903  1.000 37.92984 ? 541 HOH   A O   1 
HETATM 2243 O  O   . HOH   Q 7 .   ? -14.27005 -10.80531 -2.09275  1.000 55.35818 ? 542 HOH   A O   1 
HETATM 2244 O  O   . HOH   Q 7 .   ? -24.41869 -30.00091 24.17952  1.000 40.49767 ? 543 HOH   A O   1 
HETATM 2245 O  O   . HOH   Q 7 .   ? -25.85392 -24.01465 31.32102  1.000 51.98622 ? 544 HOH   A O   1 
HETATM 2246 O  O   . HOH   Q 7 .   ? 1.58613   -3.66592  23.81708  1.000 41.07367 ? 545 HOH   A O   1 
HETATM 2247 O  O   . HOH   Q 7 .   ? -4.10946  -21.45907 -7.20220  1.000 58.61977 ? 546 HOH   A O   1 
HETATM 2248 O  O   . HOH   Q 7 .   ? -1.08703  -10.99251 35.59458  1.000 50.44882 ? 547 HOH   A O   1 
HETATM 2249 O  O   . HOH   Q 7 .   ? -10.31167 -2.73900  7.92824   1.000 53.91674 ? 548 HOH   A O   1 
HETATM 2250 O  O   . HOH   Q 7 .   ? -9.89597  4.80614   21.81578  1.000 57.48666 ? 549 HOH   A O   1 
HETATM 2251 O  O   . HOH   Q 7 .   ? -17.474   -11.938   40.175    1.000 46.12759 ? 550 HOH   A O   1 
HETATM 2252 O  O   . HOH   Q 7 .   ? -17.46064 -24.66268 -1.20463  1.000 52.20220 ? 551 HOH   A O   1 
HETATM 2253 O  O   . HOH   Q 7 .   ? -1.63872  -3.12241  6.41273   1.000 60.21291 ? 552 HOH   A O   1 
HETATM 2254 O  O   . HOH   Q 7 .   ? 5.42791   -14.61553 28.96333  1.000 43.20790 ? 553 HOH   A O   1 
HETATM 2255 O  O   . HOH   Q 7 .   ? -18.94004 -24.32770 7.68743   1.000 41.18869 ? 554 HOH   A O   1 
HETATM 2256 O  O   . HOH   Q 7 .   ? -16.03172 -23.82521 2.28830   1.000 39.87768 ? 555 HOH   A O   1 
HETATM 2257 O  O   . HOH   Q 7 .   ? -19.53934 -7.06381  30.53526  1.000 51.94991 ? 556 HOH   A O   1 
HETATM 2258 O  O   . HOH   Q 7 .   ? 11.137    -7.301    20.782    1.000 49.89566 ? 557 HOH   A O   1 
HETATM 2259 O  O   . HOH   Q 7 .   ? -3.92550  -25.01113 33.21115  1.000 53.26959 ? 558 HOH   A O   1 
HETATM 2260 O  O   . HOH   Q 7 .   ? 2.35804   -13.21905 6.66535   1.000 49.11812 ? 559 HOH   A O   1 
HETATM 2261 O  O   . HOH   Q 7 .   ? 2.78764   -15.51009 2.16877   1.000 58.27035 ? 560 HOH   A O   1 
HETATM 2262 O  O   . HOH   Q 7 .   ? -11.124   1.688     26.059    1.000 41.44925 ? 561 HOH   A O   1 
HETATM 2263 O  O   . HOH   Q 7 .   ? -18.644   -10.637   -17.664   1.000 45.57209 ? 562 HOH   A O   1 
HETATM 2264 O  O   . HOH   Q 7 .   ? -13.351   5.426     19.578    1.000 51.15771 ? 563 HOH   A O   1 
HETATM 2265 O  O   . HOH   Q 7 .   ? 1.25428   -21.91915 24.63705  1.000 46.07120 ? 564 HOH   A O   1 
HETATM 2266 O  O   . HOH   Q 7 .   ? -30.00453 -20.09850 22.93683  1.000 54.55251 ? 565 HOH   A O   1 
HETATM 2267 O  O   . HOH   Q 7 .   ? 5.481     -14.818   5.087     1.000 59.33376 ? 566 HOH   A O   1 
HETATM 2268 O  O   . HOH   Q 7 .   ? -3.26795  -7.87182  37.21264  1.000 45.44205 ? 567 HOH   A O   1 
HETATM 2269 O  O   . HOH   Q 7 .   ? -23.74468 -12.28087 25.14202  1.000 46.73740 ? 568 HOH   A O   1 
HETATM 2270 O  O   . HOH   Q 7 .   ? -17.58551 -34.46667 23.78430  1.000 41.46905 ? 569 HOH   A O   1 
HETATM 2271 O  O   . HOH   Q 7 .   ? -27.72323 -19.43300 31.62988  1.000 43.72983 ? 570 HOH   A O   1 
HETATM 2272 O  O   . HOH   Q 7 .   ? -21.95915 -7.78287  6.44001   1.000 54.51205 ? 571 HOH   A O   1 
HETATM 2273 O  O   . HOH   Q 7 .   ? -26.29615 -29.52456 14.25341  1.000 46.70132 ? 572 HOH   A O   1 
HETATM 2274 O  O   . HOH   Q 7 .   ? -4.32529  -20.61791 37.64741  1.000 58.23595 ? 573 HOH   A O   1 
HETATM 2275 O  O   . HOH   Q 7 .   ? -7.34947  -25.61760 -5.36978  1.000 58.67903 ? 574 HOH   A O   1 
HETATM 2276 O  O   . HOH   Q 7 .   ? -12.84408 -5.00111  5.01105   1.000 53.73078 ? 575 HOH   A O   1 
HETATM 2277 O  O   . HOH   Q 7 .   ? -7.50572  -0.17096  18.47076  1.000 49.86303 ? 576 HOH   A O   1 
HETATM 2278 O  O   . HOH   Q 7 .   ? -7.15852  -31.91032 11.37339  1.000 43.05893 ? 577 HOH   A O   1 
HETATM 2279 O  O   . HOH   Q 7 .   ? 0.50751   -18.50824 -9.11785  1.000 65.27121 ? 578 HOH   A O   1 
HETATM 2280 O  O   . HOH   Q 7 .   ? -16.26594 -31.97136 26.97354  1.000 43.59722 ? 579 HOH   A O   1 
HETATM 2281 O  O   . HOH   Q 7 .   ? -26.72663 -25.62005 28.22659  1.000 53.20444 ? 580 HOH   A O   1 
HETATM 2282 O  O   . HOH   Q 7 .   ? -22.99671 -27.63026 23.67889  1.000 35.72565 ? 581 HOH   A O   1 
HETATM 2283 O  O   . HOH   Q 7 .   ? -21.98485 -11.47896 6.22663   1.000 39.67858 ? 582 HOH   A O   1 
HETATM 2284 O  O   . HOH   Q 7 .   ? 1.412     -24.641   25.084    1.000 56.37558 ? 583 HOH   A O   1 
HETATM 2285 O  O   . HOH   Q 7 .   ? -20.60620 -13.97288 -5.86311  1.000 43.35788 ? 584 HOH   A O   1 
HETATM 2286 O  O   . HOH   Q 7 .   ? -11.49484 -10.96917 -1.96845  1.000 57.24606 ? 585 HOH   A O   1 
HETATM 2287 O  O   . HOH   Q 7 .   ? -19.77711 -34.52951 14.93100  1.000 42.38652 ? 586 HOH   A O   1 
HETATM 2288 O  O   . HOH   Q 7 .   ? -20.61012 -0.16162  16.98807  1.000 62.15857 ? 587 HOH   A O   1 
HETATM 2289 O  O   . HOH   Q 7 .   ? -17.15621 -32.93248 32.47709  1.000 51.19584 ? 588 HOH   A O   1 
HETATM 2290 O  O   . HOH   Q 7 .   ? -4.83070  -31.48722 -2.21640  1.000 61.80402 ? 589 HOH   A O   1 
HETATM 2291 O  O   . HOH   Q 7 .   ? -20.22137 -9.45194  32.67649  1.000 48.14112 ? 590 HOH   A O   1 
HETATM 2292 O  O   . HOH   Q 7 .   ? -18.58473 -2.70431  30.18871  1.000 52.47919 ? 591 HOH   A O   1 
HETATM 2293 O  O   . HOH   Q 7 .   ? -27.13687 -25.72342 25.22822  1.000 44.23269 ? 592 HOH   A O   1 
HETATM 2294 O  O   . HOH   Q 7 .   ? -34.64111 -32.26658 21.04167  1.000 57.16482 ? 593 HOH   A O   1 
HETATM 2295 O  O   . HOH   Q 7 .   ? -27.04418 -30.40732 19.65721  1.000 40.02000 ? 594 HOH   A O   1 
HETATM 2296 O  O   . HOH   Q 7 .   ? -20.86635 -19.98769 5.28488   1.000 46.03667 ? 595 HOH   A O   1 
HETATM 2297 O  O   . HOH   Q 7 .   ? 0.40306   -22.94530 32.33023  1.000 53.98012 ? 596 HOH   A O   1 
HETATM 2298 O  O   . HOH   Q 7 .   ? -22.33334 -20.44826 3.19473   1.000 55.97737 ? 597 HOH   A O   1 
HETATM 2299 O  O   . HOH   Q 7 .   ? -23.69682 -27.42237 31.36218  1.000 41.40390 ? 598 HOH   A O   1 
HETATM 2300 O  O   . HOH   Q 7 .   ? 1.12845   -21.63855 9.25944   1.000 45.03206 ? 599 HOH   A O   1 
HETATM 2301 O  O   . HOH   Q 7 .   ? 5.82254   -18.15818 27.35210  1.000 54.07411 ? 600 HOH   A O   1 
HETATM 2302 O  O   . HOH   Q 7 .   ? -26.46657 -11.08991 6.85525   1.000 48.31832 ? 601 HOH   A O   1 
HETATM 2303 O  O   . HOH   Q 7 .   ? -25.88854 -17.72186 -8.04636  1.000 58.24265 ? 602 HOH   A O   1 
HETATM 2304 O  O   . HOH   Q 7 .   ? -9.35048  -11.01782 -2.26263  1.000 49.67447 ? 603 HOH   A O   1 
HETATM 2305 O  O   . HOH   Q 7 .   ? 1.29286   0.22814   6.46497   1.000 61.78529 ? 604 HOH   A O   1 
HETATM 2306 O  O   . HOH   Q 7 .   ? -21.41640 -22.76585 5.93961   1.000 40.42726 ? 605 HOH   A O   1 
HETATM 2307 O  O   . HOH   Q 7 .   ? -19.44792 -23.43239 2.69059   1.000 56.22606 ? 606 HOH   A O   1 
HETATM 2308 O  O   . HOH   Q 7 .   ? -24.36541 -8.29262  31.71372  1.000 60.47609 ? 607 HOH   A O   1 
HETATM 2309 O  O   . HOH   Q 7 .   ? 0.86238   -35.77501 4.52298   1.000 59.74401 ? 608 HOH   A O   1 
HETATM 2310 O  O   . HOH   R 7 .   ? -36.047   -8.785    10.556    1.000 43.62374 ? 201 HOH   B O   1 
HETATM 2311 O  O   . HOH   R 7 .   ? -21.48618 -12.20365 11.39588  1.000 25.01431 ? 202 HOH   B O   1 
HETATM 2312 O  O   . HOH   R 7 .   ? -24.47996 -3.35648  9.29942   1.000 53.36267 ? 203 HOH   B O   1 
HETATM 2313 O  O   . HOH   R 7 .   ? -33.06282 -14.88305 17.21021  1.000 49.64079 ? 204 HOH   B O   1 
HETATM 2314 O  O   . HOH   R 7 .   ? -32.35983 -6.07663  10.73187  1.000 45.75859 ? 205 HOH   B O   1 
HETATM 2315 O  O   . HOH   R 7 .   ? -27.88805 -13.35481 6.10334   1.000 43.67951 ? 206 HOH   B O   1 
HETATM 2316 O  O   . HOH   R 7 .   ? -34.246   -17.940   14.296    1.000 37.47131 ? 207 HOH   B O   1 
HETATM 2317 O  O   . HOH   R 7 .   ? -21.77815 -6.66352  20.75882  1.000 34.93610 ? 208 HOH   B O   1 
HETATM 2318 O  O   . HOH   R 7 .   ? -27.04339 -3.03324  16.38502  1.000 45.53318 ? 209 HOH   B O   1 
HETATM 2319 O  O   . HOH   R 7 .   ? -32.845   -11.661   8.483     1.000 44.90124 ? 210 HOH   B O   1 
HETATM 2320 O  O   . HOH   R 7 .   ? -26.03957 -10.74982 21.68985  1.000 50.67230 ? 211 HOH   B O   1 
HETATM 2321 O  O   . HOH   R 7 .   ? -20.51313 -2.66433  17.63083  1.000 56.47034 ? 212 HOH   B O   1 
HETATM 2322 O  O   . HOH   R 7 .   ? -26.49462 2.13849   4.66070   1.000 63.09509 ? 213 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASN   A 6   ? 1.14767 1.36686 1.05806 -0.08367 -0.07068 -0.13055 5   ASN   A N   
2    C CA  . ASN   A 6   ? 0.98748 1.22828 0.91004 -0.08334 -0.07639 -0.12215 5   ASN   A CA  
3    C C   . ASN   A 6   ? 0.90387 1.12955 0.83878 -0.07742 -0.07191 -0.11181 5   ASN   A C   
4    O O   . ASN   A 6   ? 0.88322 1.08523 0.82232 -0.08017 -0.06503 -0.11650 5   ASN   A O   
5    C CB  . ASN   A 6   ? 0.96926 1.23468 0.88605 -0.07669 -0.08399 -0.11212 5   ASN   A CB  
6    N N   . MET   A 7   ? 0.86742 1.10696 0.80795 -0.06923 -0.07603 -0.09771 6   MET   A N   
7    C CA  . MET   A 7   ? 0.87497 1.10402 0.82785 -0.06334 -0.07267 -0.08736 6   MET   A CA  
8    C C   . MET   A 7   ? 0.80317 1.00023 0.75142 -0.05612 -0.06447 -0.08368 6   MET   A C   
9    O O   . MET   A 7   ? 0.64733 0.83893 0.58562 -0.04746 -0.06423 -0.07717 6   MET   A O   
10   C CB  . MET   A 7   ? 0.83759 1.08832 0.79573 -0.05493 -0.07930 -0.07298 6   MET   A CB  
11   C CG  . MET   A 7   ? 0.87271 1.10948 0.83848 -0.04441 -0.07561 -0.05954 6   MET   A CG  
12   S SD  . MET   A 7   ? 1.05044 1.29440 1.03651 -0.04754 -0.07546 -0.05656 6   MET   A SD  
13   C CE  . MET   A 7   ? 0.96013 1.23223 0.95187 -0.03800 -0.08446 -0.04149 6   MET   A CE  
14   N N   . ALA   A 8   ? 0.51124 0.68725 0.46682 -0.05987 -0.05788 -0.08772 7   ALA   A N   
15   C CA  . ALA   A 8   ? 0.48245 0.62721 0.43489 -0.05359 -0.05006 -0.08442 7   ALA   A CA  
16   C C   . ALA   A 8   ? 0.48960 0.63237 0.44509 -0.04053 -0.05023 -0.06769 7   ALA   A C   
17   O O   . ALA   A 8   ? 0.44586 0.60803 0.41011 -0.03749 -0.05507 -0.05913 7   ALA   A O   
18   C CB  . ALA   A 8   ? 0.50923 0.63403 0.47028 -0.06078 -0.04374 -0.09130 7   ALA   A CB  
19   N N   . SER   A 9   ? 0.40256 0.52135 0.35105 -0.03263 -0.04497 -0.06319 8   SER   A N   
20   C CA  . SER   A 9   ? 0.36140 0.47510 0.31257 -0.02010 -0.04459 -0.04767 8   SER   A CA  
21   C C   . SER   A 9   ? 0.31856 0.42823 0.28449 -0.01985 -0.04228 -0.04244 8   SER   A C   
22   O O   . SER   A 9   ? 0.33871 0.43951 0.31104 -0.02841 -0.03847 -0.05063 8   SER   A O   
23   C CB  . SER   A 9   ? 0.36655 0.45253 0.30830 -0.01266 -0.03864 -0.04496 8   SER   A CB  
24   O OG  . SER   A 9   ? 0.38902 0.44810 0.33340 -0.01701 -0.03108 -0.05175 8   SER   A OG  
25   N N   . LEU   A 10  ? 0.32250 0.43874 0.29394 -0.00991 -0.04462 -0.02857 9   LEU   A N   
26   C CA  . LEU   A 10  ? 0.30920 0.42212 0.29454 -0.00896 -0.04225 -0.02319 9   LEU   A CA  
27   C C   . LEU   A 10  ? 0.28075 0.36092 0.26653 -0.00918 -0.03328 -0.02535 9   LEU   A C   
28   O O   . LEU   A 10  ? 0.27024 0.34498 0.26565 -0.01526 -0.02990 -0.02880 9   LEU   A O   
29   C CB  . LEU   A 10  ? 0.26996 0.39427 0.26042 0.00274  -0.04630 -0.00790 9   LEU   A CB  
30   C CG  . LEU   A 10  ? 0.31155 0.43308 0.31616 0.00561  -0.04394 -0.00090 9   LEU   A CG  
31   C CD1 . LEU   A 10  ? 0.30039 0.43757 0.31626 -0.00563 -0.04512 -0.00882 9   LEU   A CD1 
32   C CD2 . LEU   A 10  ? 0.36122 0.49569 0.37016 0.01754  -0.04888 0.01372  9   LEU   A CD2 
33   N N   . ILE   A 11  ? 0.30120 0.35912 0.27664 -0.00298 -0.02933 -0.02352 10  ILE   A N   
34   C CA  . ILE   A 11  ? 0.31588 0.34233 0.29190 -0.00323 -0.02111 -0.02546 10  ILE   A CA  
35   C C   . ILE   A 11  ? 0.30982 0.32742 0.28535 -0.01624 -0.01778 -0.04067 10  ILE   A C   
36   O O   . ILE   A 11  ? 0.31474 0.31507 0.29664 -0.02036 -0.01243 -0.04320 10  ILE   A O   
37   C CB  . ILE   A 11  ? 0.30825 0.31246 0.27405 0.00684  -0.01773 -0.01955 10  ILE   A CB  
38   C CG1 . ILE   A 11  ? 0.31852 0.29067 0.28644 0.00792  -0.00970 -0.01929 10  ILE   A CG1 
39   C CG2 . ILE   A 11  ? 0.35178 0.35568 0.30414 0.00434  -0.01868 -0.02792 10  ILE   A CG2 
40   C CD1 . ILE   A 11  ? 0.28760 0.25745 0.26767 0.01174  -0.00799 -0.01002 10  ILE   A CD1 
41   N N   . GLN   A 12  ? 0.28756 0.31694 0.25591 -0.02317 -0.02101 -0.05101 11  GLN   A N   
42   C CA  . GLN   A 12  ? 0.29127 0.31473 0.26056 -0.03602 -0.01867 -0.06569 11  GLN   A CA  
43   C C   . GLN   A 12  ? 0.32846 0.36616 0.31135 -0.04389 -0.02014 -0.06747 11  GLN   A C   
44   O O   . GLN   A 12  ? 0.33259 0.35606 0.32087 -0.05181 -0.01567 -0.07435 11  GLN   A O   
45   C CB  . GLN   A 12  ? 0.36546 0.40131 0.32463 -0.04165 -0.02243 -0.07632 11  GLN   A CB  
46   C CG  . GLN   A 12  ? 0.38641 0.41893 0.34716 -0.05530 -0.02100 -0.09194 11  GLN   A CG  
47   C CD  . GLN   A 12  ? 0.44813 0.44862 0.40315 -0.05727 -0.01402 -0.09957 11  GLN   A CD  
48   O OE1 . GLN   A 12  ? 0.46999 0.45619 0.41548 -0.04995 -0.01169 -0.09712 11  GLN   A OE1 
49   N NE2 . GLN   A 12  ? 0.46558 0.45486 0.42673 -0.06744 -0.01085 -0.10899 11  GLN   A NE2 
50   N N   . ARG   A 13  ? 0.28543 0.35117 0.27443 -0.04182 -0.02645 -0.06108 12  ARG   A N   
51   C CA  A ARG   A 13  ? 0.28715 0.36778 0.28985 -0.04892 -0.02793 -0.06237 12  ARG   A CA  
52   C CA  B ARG   A 13  ? 0.28656 0.36732 0.28927 -0.04889 -0.02796 -0.06233 12  ARG   A CA  
53   C C   . ARG   A 13  ? 0.30486 0.36853 0.31700 -0.04570 -0.02219 -0.05525 12  ARG   A C   
54   O O   . ARG   A 13  ? 0.30256 0.36468 0.32415 -0.05422 -0.01976 -0.06012 12  ARG   A O   
55   C CB  A ARG   A 13  ? 0.29553 0.40957 0.30290 -0.04646 -0.03613 -0.05649 12  ARG   A CB  
56   C CB  B ARG   A 13  ? 0.29480 0.40897 0.30200 -0.04628 -0.03620 -0.05636 12  ARG   A CB  
57   C CG  A ARG   A 13  ? 0.35380 0.48722 0.35295 -0.05171 -0.04221 -0.06461 12  ARG   A CG  
58   C CG  B ARG   A 13  ? 0.35351 0.48746 0.35323 -0.05265 -0.04222 -0.06540 12  ARG   A CG  
59   C CD  A ARG   A 13  ? 0.42291 0.58415 0.42275 -0.04509 -0.05019 -0.05546 12  ARG   A CD  
60   C CD  B ARG   A 13  ? 0.41844 0.58571 0.42344 -0.05077 -0.05073 -0.05959 12  ARG   A CD  
61   N NE  A ARG   A 13  ? 0.41413 0.59817 0.42788 -0.04979 -0.05426 -0.05458 12  ARG   A NE  
62   N NE  B ARG   A 13  ? 0.41665 0.58950 0.41462 -0.03883 -0.05424 -0.04842 12  ARG   A NE  
63   C CZ  A ARG   A 13  ? 0.37015 0.56510 0.39380 -0.04252 -0.05647 -0.04296 12  ARG   A CZ  
64   C CZ  B ARG   A 13  ? 0.41455 0.60417 0.41943 -0.03100 -0.05890 -0.03650 12  ARG   A CZ  
65   N NH1 A ARG   A 13  ? 0.49543 0.68249 0.51632 -0.03003 -0.05586 -0.03082 12  ARG   A NH1 
66   N NH1 B ARG   A 13  ? 0.35336 0.55693 0.37258 -0.03347 -0.06061 -0.03413 12  ARG   A NH1 
67   N NH2 A ARG   A 13  ? 0.39028 0.60485 0.42721 -0.04789 -0.05950 -0.04369 12  ARG   A NH2 
68   N NH2 B ARG   A 13  ? 0.40613 0.59896 0.40360 -0.02054 -0.06206 -0.02684 12  ARG   A NH2 
69   N N   . ILE   A 14  ? 0.27851 0.32929 0.28819 -0.03368 -0.01996 -0.04377 13  ILE   A N   
70   C CA  . ILE   A 14  ? 0.29545 0.32811 0.31280 -0.03021 -0.01416 -0.03711 13  ILE   A CA  
71   C C   . ILE   A 14  ? 0.32507 0.32930 0.34022 -0.03751 -0.00705 -0.04598 13  ILE   A C   
72   O O   . ILE   A 14  ? 0.30616 0.30315 0.33036 -0.04301 -0.00324 -0.04726 13  ILE   A O   
73   C CB  . ILE   A 14  ? 0.24880 0.27245 0.26269 -0.01558 -0.01352 -0.02348 13  ILE   A CB  
74   C CG1 . ILE   A 14  ? 0.25054 0.30214 0.27124 -0.00896 -0.02017 -0.01352 13  ILE   A CG1 
75   C CG2 . ILE   A 14  ? 0.27846 0.27479 0.29608 -0.01216 -0.00610 -0.01864 13  ILE   A CG2 
76   C CD1 . ILE   A 14  ? 0.30112 0.34827 0.31624 0.00557  -0.02159 -0.00070 13  ILE   A CD1 
77   N N   . ALA   A 15  ? 0.26989 0.25794 0.27319 -0.03793 -0.00525 -0.05239 14  ALA   A N   
78   C CA  . ALA   A 15  ? 0.31804 0.27827 0.31907 -0.04464 0.00111  -0.06108 14  ALA   A CA  
79   C C   . ALA   A 15  ? 0.33701 0.30519 0.34465 -0.05905 0.00063  -0.07296 14  ALA   A C   
80   O O   . ALA   A 15  ? 0.36217 0.31439 0.37583 -0.06514 0.00543  -0.07592 14  ALA   A O   
81   C CB  . ALA   A 15  ? 0.34529 0.28962 0.33257 -0.04222 0.00242  -0.06633 14  ALA   A CB  
82   N N   . ARG   A 16  ? 0.32636 0.31899 0.33268 -0.06480 -0.00530 -0.07988 15  ARG   A N   
83   C CA  A ARG   A 16  ? 0.34197 0.34539 0.35496 -0.07847 -0.00673 -0.09102 15  ARG   A CA  
84   C CA  B ARG   A 16  ? 0.34241 0.34497 0.35538 -0.07851 -0.00654 -0.09107 15  ARG   A CA  
85   C C   . ARG   A 16  ? 0.40277 0.41374 0.43024 -0.08155 -0.00571 -0.08613 15  ARG   A C   
86   O O   . ARG   A 16  ? 0.37414 0.37711 0.40798 -0.09169 -0.00269 -0.09311 15  ARG   A O   
87   C CB  A ARG   A 16  ? 0.36926 0.40148 0.37881 -0.08194 -0.01422 -0.09655 15  ARG   A CB  
88   C CB  B ARG   A 16  ? 0.36982 0.40034 0.37940 -0.08285 -0.01383 -0.09756 15  ARG   A CB  
89   C CG  A ARG   A 16  ? 0.47276 0.51861 0.48752 -0.09606 -0.01687 -0.10915 15  ARG   A CG  
90   C CG  B ARG   A 16  ? 0.47453 0.51181 0.48848 -0.09745 -0.01502 -0.11125 15  ARG   A CG  
91   C CD  A ARG   A 16  ? 0.45443 0.51981 0.46045 -0.09868 -0.02311 -0.11661 15  ARG   A CD  
92   C CD  B ARG   A 16  ? 0.45954 0.53072 0.47525 -0.10141 -0.02297 -0.11424 15  ARG   A CD  
93   N NE  A ARG   A 16  ? 0.49313 0.55163 0.48627 -0.08867 -0.02318 -0.11244 15  ARG   A NE  
94   N NE  B ARG   A 16  ? 0.57210 0.64627 0.57778 -0.10750 -0.02557 -0.12663 15  ARG   A NE  
95   C CZ  A ARG   A 16  ? 0.53498 0.60611 0.51796 -0.08891 -0.02758 -0.11765 15  ARG   A CZ  
96   C CZ  B ARG   A 16  ? 0.48999 0.57728 0.49866 -0.11942 -0.02877 -0.13827 15  ARG   A CZ  
97   N NH1 A ARG   A 16  ? 0.61480 0.71050 0.59915 -0.09700 -0.03349 -0.12513 15  ARG   A NH1 
98   N NH1 B ARG   A 16  ? 0.53953 0.63862 0.56116 -0.12693 -0.02985 -0.13921 15  ARG   A NH1 
99   N NH2 A ARG   A 16  ? 0.66063 0.71952 0.63172 -0.08101 -0.02596 -0.11538 15  ARG   A NH2 
100  N NH2 B ARG   A 16  ? 0.56912 0.65778 0.56763 -0.12398 -0.03090 -0.14939 15  ARG   A NH2 
101  N N   . GLN   A 17  ? 0.33356 0.36087 0.36668 -0.07311 -0.00839 -0.07430 16  GLN   A N   
102  C CA  . GLN   A 17  ? 0.33761 0.37442 0.38493 -0.07585 -0.00756 -0.06986 16  GLN   A CA  
103  C C   . GLN   A 17  ? 0.35130 0.36045 0.40172 -0.07375 0.00016  -0.06522 16  GLN   A C   
104  O O   . GLN   A 17  ? 0.33362 0.34187 0.39414 -0.08107 0.00294  -0.06692 16  GLN   A O   
105  C CB  . GLN   A 17  ? 0.30512 0.36808 0.35803 -0.06723 -0.01301 -0.05894 16  GLN   A CB  
106  C CG  . GLN   A 17  ? 0.27845 0.35482 0.34681 -0.06934 -0.01267 -0.05414 16  GLN   A CG  
107  C CD  . GLN   A 17  ? 0.32720 0.42060 0.40399 -0.08323 -0.01493 -0.06435 16  GLN   A CD  
108  O OE1 . GLN   A 17  ? 0.34570 0.45097 0.41783 -0.08979 -0.01938 -0.07345 16  GLN   A OE1 
109  N NE2 . GLN   A 17  ? 0.32833 0.42323 0.41763 -0.08793 -0.01184 -0.06296 16  GLN   A NE2 
110  N N   . ALA   A 18  ? 0.30290 0.28954 0.34478 -0.06404 0.00364  -0.05928 17  ALA   A N   
111  C CA  . ALA   A 18  ? 0.34782 0.30593 0.39123 -0.06249 0.01096  -0.05570 17  ALA   A CA  
112  C C   . ALA   A 18  ? 0.37533 0.31507 0.41844 -0.07491 0.01502  -0.06757 17  ALA   A C   
113  O O   . ALA   A 18  ? 0.38049 0.30829 0.43080 -0.07966 0.01965  -0.06704 17  ALA   A O   
114  C CB  . ALA   A 18  ? 0.29254 0.22991 0.32591 -0.05017 0.01338  -0.04822 17  ALA   A CB  
115  N N   . SER   A 19  ? 0.38562 0.32316 0.42052 -0.08046 0.01321  -0.07848 18  SER   A N   
116  C CA  . SER   A 19  ? 0.39718 0.31825 0.43213 -0.09263 0.01634  -0.09053 18  SER   A CA  
117  C C   . SER   A 19  ? 0.47686 0.41391 0.52404 -0.10434 0.01523  -0.09520 18  SER   A C   
118  O O   . SER   A 19  ? 0.51532 0.43615 0.56750 -0.11209 0.01971  -0.09869 18  SER   A O   
119  C CB  . SER   A 19  ? 0.45946 0.37908 0.48393 -0.09629 0.01385  -0.10182 18  SER   A CB  
120  O OG  . SER   A 19  ? 0.43181 0.32759 0.45470 -0.10530 0.01788  -0.11205 18  SER   A OG  
121  N N   . LEU   A 20  ? 0.35609 0.32498 0.40841 -0.10586 0.00919  -0.09512 19  LEU   A N   
122  C CA  . LEU   A 20  ? 0.39914 0.38553 0.46379 -0.11676 0.00774  -0.09927 19  LEU   A CA  
123  C C   . LEU   A 20  ? 0.42350 0.40642 0.49899 -0.11503 0.01199  -0.09005 19  LEU   A C   
124  O O   . LEU   A 20  ? 0.45235 0.43319 0.53652 -0.12523 0.01448  -0.09423 19  LEU   A O   
125  C CB  . LEU   A 20  ? 0.38956 0.41114 0.45705 -0.11718 -0.00003 -0.10000 19  LEU   A CB  
126  C CG  . LEU   A 20  ? 0.57324 0.61559 0.65072 -0.13011 -0.00328 -0.10825 19  LEU   A CG  
127  C CD1 . LEU   A 20  ? 0.54554 0.58150 0.61646 -0.14052 -0.00448 -0.12286 19  LEU   A CD1 
128  C CD2 . LEU   A 20  ? 0.64006 0.71696 0.72233 -0.12650 -0.01043 -0.10368 19  LEU   A CD2 
129  N N   . THR   A 21  ? 0.36826 0.35091 0.44344 -0.10227 0.01282  -0.07752 20  THR   A N   
130  C CA  . THR   A 21  ? 0.37714 0.35841 0.46232 -0.09941 0.01661  -0.06826 20  THR   A CA  
131  C C   . THR   A 21  ? 0.43343 0.38161 0.51702 -0.10183 0.02426  -0.06840 20  THR   A C   
132  O O   . THR   A 21  ? 0.46688 0.41260 0.55981 -0.10790 0.02788  -0.06749 20  THR   A O   
133  C CB  . THR   A 21  ? 0.35817 0.34730 0.44247 -0.08449 0.01494  -0.05524 20  THR   A CB  
134  O OG1 . THR   A 21  ? 0.31803 0.33794 0.40373 -0.08243 0.00738  -0.05494 20  THR   A OG1 
135  C CG2 . THR   A 21  ? 0.38738 0.37632 0.48220 -0.08092 0.01876  -0.04570 20  THR   A CG2 
136  N N   . PHE   A 22  ? 0.44116 0.36401 0.51304 -0.09725 0.02669  -0.06948 21  PHE   A N   
137  C CA  . PHE   A 22  ? 0.53075 0.41983 0.59933 -0.09762 0.03356  -0.06874 21  PHE   A CA  
138  C C   . PHE   A 22  ? 0.69054 0.56477 0.75076 -0.10466 0.03324  -0.07986 21  PHE   A C   
139  O O   . PHE   A 22  ? 0.65588 0.52036 0.70440 -0.09791 0.03185  -0.08058 21  PHE   A O   
140  C CB  . PHE   A 22  ? 0.44346 0.31587 0.50465 -0.08313 0.03588  -0.05816 21  PHE   A CB  
141  C CG  . PHE   A 22  ? 0.39751 0.28693 0.46457 -0.07275 0.03446  -0.04565 21  PHE   A CG  
142  C CD1 . PHE   A 22  ? 0.40134 0.29120 0.47833 -0.07335 0.03801  -0.03935 21  PHE   A CD1 
143  C CD2 . PHE   A 22  ? 0.41215 0.31605 0.47457 -0.06211 0.02971  -0.03999 21  PHE   A CD2 
144  C CE1 . PHE   A 22  ? 0.36675 0.27171 0.44930 -0.06335 0.03670  -0.02817 21  PHE   A CE1 
145  C CE2 . PHE   A 22  ? 0.43860 0.35726 0.50664 -0.05220 0.02810  -0.02846 21  PHE   A CE2 
146  C CZ  . PHE   A 22  ? 0.40165 0.32087 0.47994 -0.05269 0.03159  -0.02274 21  PHE   A CZ  
147  N N   . ARG   A 23  ? 0.73798 0.61595 0.80176 -0.11326 0.03224  -0.08436 22  ARG   A N   
148  C CA  . ARG   A 23  ? 0.74881 0.61769 0.80353 -0.11452 0.02953  -0.08963 22  ARG   A CA  
149  C C   . ARG   A 23  ? 0.80581 0.65782 0.85515 -0.10745 0.02984  -0.08076 22  ARG   A C   
150  O O   . ARG   A 23  ? 0.83760 0.67839 0.87938 -0.09556 0.02976  -0.07157 22  ARG   A O   
151  C CB  . ARG   A 23  ? 0.76045 0.64550 0.82230 -0.12857 0.02695  -0.10095 22  ARG   A CB  
152  C CG  . ARG   A 23  ? 0.67764 0.58813 0.74629 -0.13695 0.02411  -0.11005 22  ARG   A CG  
153  C CD  . ARG   A 23  ? 0.66355 0.58826 0.73368 -0.14789 0.01965  -0.12149 22  ARG   A CD  
154  N NE  . ARG   A 23  ? 0.66823 0.60130 0.74914 -0.15610 0.01992  -0.12142 22  ARG   A NE  
155  C CZ  . ARG   A 23  ? 0.65159 0.60469 0.74609 -0.16128 0.02017  -0.11935 22  ARG   A CZ  
156  N NH1 . ARG   A 23  ? 0.61279 0.58225 0.70954 -0.15348 0.01852  -0.11239 22  ARG   A NH1 
157  N NH2 . ARG   A 23  ? 0.65944 0.61865 0.76260 -0.16835 0.02049  -0.11925 22  ARG   A NH2 
158  N N   . GLN   A 45  ? 0.74502 0.71136 0.90014 -0.15250 0.04647  -0.06192 44  GLN   A N   
159  C CA  . GLN   A 45  ? 0.71882 0.69735 0.87535 -0.16321 0.04170  -0.07312 44  GLN   A CA  
160  C C   . GLN   A 45  ? 0.73518 0.74987 0.90465 -0.16688 0.03719  -0.07642 44  GLN   A C   
161  O O   . GLN   A 45  ? 0.60146 0.62653 0.76853 -0.15428 0.03452  -0.06913 44  GLN   A O   
162  C CB  . GLN   A 45  ? 0.75233 0.71178 0.89318 -0.16008 0.03924  -0.07836 44  GLN   A CB  
163  C CG  . GLN   A 45  ? 0.85107 0.78069 0.97715 -0.15422 0.04046  -0.07456 44  GLN   A CG  
164  C CD  . GLN   A 45  ? 0.93283 0.84413 1.04403 -0.14607 0.03894  -0.07559 44  GLN   A CD  
165  O OE1 . GLN   A 45  ? 0.90997 0.82751 1.02098 -0.14387 0.03806  -0.07809 44  GLN   A OE1 
166  N NE2 . GLN   A 45  ? 1.14837 1.03901 1.24770 -0.14144 0.03804  -0.07344 44  GLN   A NE2 
167  N N   . PRO   A 46  ? 0.80923 0.84363 0.98772 -0.17902 0.03412  -0.08422 45  PRO   A N   
168  C CA  . PRO   A 46  ? 0.68547 0.75431 0.86974 -0.17776 0.02673  -0.08550 45  PRO   A CA  
169  C C   . PRO   A 46  ? 0.66618 0.73551 0.83810 -0.17005 0.02139  -0.08753 45  PRO   A C   
170  O O   . PRO   A 46  ? 0.68160 0.72836 0.84202 -0.17133 0.02234  -0.09308 45  PRO   A O   
171  C CB  . PRO   A 46  ? 0.72146 0.80284 0.91428 -0.19403 0.02473  -0.09605 45  PRO   A CB  
172  C CG  . PRO   A 46  ? 0.76520 0.82430 0.95659 -0.19626 0.03028  -0.09238 45  PRO   A CG  
173  C CD  . PRO   A 46  ? 0.80016 0.82646 0.97857 -0.18644 0.03509  -0.08611 45  PRO   A CD  
174  N N   . GLY   A 47  ? 0.54868 0.64419 0.72322 -0.16195 0.01572  -0.08288 46  GLY   A N   
175  C CA  . GLY   A 47  ? 0.42622 0.52564 0.58971 -0.15409 0.01031  -0.08354 46  GLY   A CA  
176  C C   . GLY   A 47  ? 0.38103 0.46438 0.53519 -0.13903 0.01244  -0.07368 46  GLY   A C   
177  O O   . GLY   A 47  ? 0.36540 0.45962 0.51356 -0.13006 0.00737  -0.07067 46  GLY   A O   
178  N N   . PHE   A 48  ? 0.39383 0.45204 0.54677 -0.13604 0.01964  -0.06826 47  PHE   A N   
179  C CA  . PHE   A 48  ? 0.35366 0.39503 0.49783 -0.12176 0.02186  -0.05880 47  PHE   A CA  
180  C C   . PHE   A 48  ? 0.34562 0.40927 0.49429 -0.10950 0.01800  -0.04852 47  PHE   A C   
181  O O   . PHE   A 48  ? 0.32447 0.38729 0.46412 -0.09911 0.01482  -0.04453 47  PHE   A O   
182  C CB  . PHE   A 48  ? 0.44018 0.45319 0.58419 -0.12153 0.03016  -0.05447 47  PHE   A CB  
183  C CG  . PHE   A 48  ? 0.35163 0.34708 0.48763 -0.10707 0.03266  -0.04444 47  PHE   A CG  
184  C CD1 . PHE   A 48  ? 0.38726 0.36112 0.50945 -0.10224 0.03288  -0.04606 47  PHE   A CD1 
185  C CD2 . PHE   A 48  ? 0.39455 0.39587 0.53720 -0.09819 0.03464  -0.03350 47  PHE   A CD2 
186  C CE1 . PHE   A 48  ? 0.43412 0.39210 0.54926 -0.08890 0.03500  -0.03665 47  PHE   A CE1 
187  C CE2 . PHE   A 48  ? 0.37972 0.36497 0.51524 -0.08486 0.03669  -0.02426 47  PHE   A CE2 
188  C CZ  . PHE   A 48  ? 0.39927 0.36278 0.52100 -0.08022 0.03679  -0.02569 47  PHE   A CZ  
189  N N   . PRO   A 49  ? 0.32339 0.40651 0.48560 -0.10969 0.01813  -0.04367 48  PRO   A N   
190  C CA  . PRO   A 49  ? 0.31009 0.41263 0.47663 -0.09702 0.01442  -0.03350 48  PRO   A CA  
191  C C   . PRO   A 49  ? 0.30641 0.43175 0.46975 -0.09383 0.00574  -0.03526 48  PRO   A C   
192  O O   . PRO   A 49  ? 0.29194 0.42094 0.45041 -0.08142 0.00252  -0.02764 48  PRO   A O   
193  C CB  . PRO   A 49  ? 0.36261 0.48448 0.54572 -0.10141 0.01584  -0.03122 48  PRO   A CB  
194  C CG  . PRO   A 49  ? 0.41560 0.51983 0.60097 -0.11402 0.02237  -0.03746 48  PRO   A CG  
195  C CD  . PRO   A 49  ? 0.37973 0.46982 0.55438 -0.12169 0.02117  -0.04759 48  PRO   A CD  
196  N N   . GLU   A 50  ? 0.31913 0.46004 0.48512 -0.10511 0.00169  -0.04516 49  GLU   A N   
197  C CA  . GLU   A 50  ? 0.28923 0.45263 0.45200 -0.10339 -0.00679 -0.04762 49  GLU   A CA  
198  C C   . GLU   A 50  ? 0.32164 0.46772 0.46769 -0.09737 -0.00783 -0.04848 49  GLU   A C   
199  O O   . GLU   A 50  ? 0.29418 0.45233 0.43533 -0.08828 -0.01336 -0.04372 49  GLU   A O   
200  C CB  . GLU   A 50  ? 0.32708 0.50741 0.49562 -0.11791 -0.01017 -0.05903 49  GLU   A CB  
201  C CG  . GLU   A 50  ? 0.37549 0.57946 0.56152 -0.12322 -0.01075 -0.05789 49  GLU   A CG  
202  C CD  . GLU   A 50  ? 0.54557 0.73289 0.73850 -0.13050 -0.00249 -0.05870 49  GLU   A CD  
203  O OE1 . GLU   A 50  ? 0.34622 0.50439 0.53056 -0.13377 0.00301  -0.06204 49  GLU   A OE1 
204  O OE2 . GLU   A 50  ? 0.68589 0.88968 0.89308 -0.13313 -0.00157 -0.05598 49  GLU   A OE2 
205  N N   . ASN   A 51  ? 0.30502 0.42272 0.44238 -0.10234 -0.00257 -0.05440 50  ASN   A N   
206  C CA  . ASN   A 51  ? 0.30005 0.39959 0.42181 -0.09664 -0.00280 -0.05544 50  ASN   A CA  
207  C C   . ASN   A 51  ? 0.28927 0.37689 0.40629 -0.08153 -0.00085 -0.04320 50  ASN   A C   
208  O O   . ASN   A 51  ? 0.29207 0.38058 0.39953 -0.07303 -0.00442 -0.04011 50  ASN   A O   
209  C CB  . ASN   A 51  ? 0.29645 0.36784 0.41142 -0.10552 0.00255  -0.06466 50  ASN   A CB  
210  C CG  . ASN   A 51  ? 0.40214 0.48366 0.51653 -0.11839 -0.00108 -0.07785 50  ASN   A CG  
211  O OD1 . ASN   A 51  ? 0.43352 0.53849 0.54677 -0.11849 -0.00800 -0.08047 50  ASN   A OD1 
212  N ND2 . ASN   A 51  ? 0.37938 0.44391 0.49493 -0.12953 0.00328  -0.08612 50  ASN   A ND2 
213  N N   . LEU   A 52  ? 0.26714 0.34304 0.39040 -0.07811 0.00484  -0.03614 51  LEU   A N   
214  C CA  . LEU   A 52  ? 0.25541 0.32019 0.37489 -0.06369 0.00660  -0.02438 51  LEU   A CA  
215  C C   . LEU   A 52  ? 0.25724 0.34919 0.38084 -0.05412 -0.00026 -0.01651 51  LEU   A C   
216  O O   . LEU   A 52  ? 0.25894 0.34622 0.37497 -0.04244 -0.00211 -0.00924 51  LEU   A O   
217  C CB  . LEU   A 52  ? 0.27759 0.32673 0.40379 -0.06276 0.01383  -0.01888 51  LEU   A CB  
218  C CG  . LEU   A 52  ? 0.30036 0.33077 0.42148 -0.04895 0.01712  -0.00776 51  LEU   A CG  
219  C CD1 . LEU   A 52  ? 0.34915 0.34868 0.45598 -0.04695 0.02045  -0.00999 51  LEU   A CD1 
220  C CD2 . LEU   A 52  ? 0.33673 0.36083 0.46753 -0.04880 0.02308  -0.00228 51  LEU   A CD2 
221  N N   . SER   A 53  ? 0.28924 0.40977 0.42515 -0.05883 -0.00430 -0.01763 52  SER   A N   
222  C CA  A SER   A 53  ? 0.27026 0.41755 0.41084 -0.05008 -0.01142 -0.01039 52  SER   A CA  
223  C CA  B SER   A 53  ? 0.27135 0.41852 0.41188 -0.05001 -0.01141 -0.01034 52  SER   A CA  
224  C C   . SER   A 53  ? 0.25462 0.40968 0.38412 -0.04761 -0.01800 -0.01277 52  SER   A C   
225  O O   . SER   A 53  ? 0.27328 0.43429 0.39895 -0.03609 -0.02205 -0.00439 52  SER   A O   
226  C CB  A SER   A 53  ? 0.30414 0.48067 0.46037 -0.05684 -0.01460 -0.01242 52  SER   A CB  
227  C CB  B SER   A 53  ? 0.30481 0.48116 0.46109 -0.05658 -0.01454 -0.01218 52  SER   A CB  
228  O OG  A SER   A 53  ? 0.34907 0.55266 0.50930 -0.04955 -0.02257 -0.00685 52  SER   A OG  
229  O OG  B SER   A 53  ? 0.32530 0.49750 0.49217 -0.05541 -0.00899 -0.00708 52  SER   A OG  
230  N N   . LYS   A 54  ? 0.25961 0.41478 0.38378 -0.05848 -0.01921 -0.02420 53  LYS   A N   
231  C CA  A LYS   A 54  ? 0.27441 0.43628 0.38717 -0.05693 -0.02501 -0.02734 53  LYS   A CA  
232  C CA  B LYS   A 54  ? 0.27458 0.43624 0.38726 -0.05705 -0.02496 -0.02747 53  LYS   A CA  
233  C C   . LYS   A 54  ? 0.28878 0.42566 0.38766 -0.04732 -0.02222 -0.02271 53  LYS   A C   
234  O O   . LYS   A 54  ? 0.25223 0.39689 0.34388 -0.03915 -0.02719 -0.01798 53  LYS   A O   
235  C CB  A LYS   A 54  ? 0.29120 0.45603 0.40107 -0.07091 -0.02614 -0.04129 53  LYS   A CB  
236  C CB  B LYS   A 54  ? 0.29165 0.45514 0.40129 -0.07107 -0.02580 -0.04147 53  LYS   A CB  
237  C CG  A LYS   A 54  ? 0.30523 0.47087 0.40105 -0.07015 -0.03046 -0.04602 53  LYS   A CG  
238  C CG  B LYS   A 54  ? 0.35146 0.54245 0.47392 -0.08076 -0.02990 -0.04659 53  LYS   A CG  
239  C CD  A LYS   A 54  ? 0.43448 0.62839 0.53282 -0.07845 -0.03786 -0.05366 53  LYS   A CD  
240  C CD  B LYS   A 54  ? 0.44453 0.63507 0.56347 -0.09471 -0.03057 -0.06078 53  LYS   A CD  
241  C CE  A LYS   A 54  ? 0.40701 0.60139 0.49057 -0.07743 -0.04185 -0.05821 53  LYS   A CE  
242  C CE  B LYS   A 54  ? 0.39081 0.60943 0.52266 -0.10448 -0.03506 -0.06591 53  LYS   A CE  
243  N NZ  A LYS   A 54  ? 0.53885 0.71920 0.61568 -0.08875 -0.03910 -0.07188 53  LYS   A NZ  
244  N NZ  B LYS   A 54  ? 0.56598 0.78418 0.69458 -0.11810 -0.03602 -0.07987 53  LYS   A NZ  
245  N N   . LEU   A 55  ? 0.25034 0.35710 0.34550 -0.04815 -0.01439 -0.02374 54  LEU   A N   
246  C CA  . LEU   A 55  ? 0.22957 0.31164 0.31247 -0.03871 -0.01141 -0.01891 54  LEU   A CA  
247  C C   . LEU   A 55  ? 0.25543 0.34214 0.34025 -0.02425 -0.01322 -0.00505 54  LEU   A C   
248  O O   . LEU   A 55  ? 0.25184 0.33531 0.32715 -0.01531 -0.01577 -0.00015 54  LEU   A O   
249  C CB  . LEU   A 55  ? 0.27301 0.32267 0.35351 -0.04227 -0.00280 -0.02182 54  LEU   A CB  
250  C CG  . LEU   A 55  ? 0.24121 0.26187 0.30942 -0.03376 0.00116  -0.01800 54  LEU   A CG  
251  C CD1 . LEU   A 55  ? 0.27479 0.29463 0.32997 -0.03350 -0.00221 -0.02357 54  LEU   A CD1 
252  C CD2 . LEU   A 55  ? 0.30331 0.29401 0.37122 -0.03888 0.00929  -0.02140 54  LEU   A CD2 
253  N N   . LYS   A 56  ? 0.24370 0.33786 0.34095 -0.02179 -0.01188 0.00136  55  LYS   A N   
254  C CA  . LYS   A 56  ? 0.24372 0.34367 0.34408 -0.00812 -0.01400 0.01427  55  LYS   A CA  
255  C C   . LYS   A 56  ? 0.25793 0.38441 0.35720 -0.00313 -0.02309 0.01754  55  LYS   A C   
256  O O   . LYS   A 56  ? 0.25404 0.37896 0.34819 0.00858  -0.02570 0.02656  55  LYS   A O   
257  C CB  . LYS   A 56  ? 0.26056 0.36860 0.37581 -0.00774 -0.01163 0.01902  55  LYS   A CB  
258  C CG  . LYS   A 56  ? 0.40773 0.48974 0.52437 -0.01114 -0.00265 0.01798  55  LYS   A CG  
259  C CD  . LYS   A 56  ? 0.40911 0.50110 0.54040 -0.01014 -0.00041 0.02320  55  LYS   A CD  
260  C CE  . LYS   A 56  ? 0.51821 0.61605 0.65247 0.00469  -0.00282 0.03576  55  LYS   A CE  
261  N NZ  . LYS   A 56  ? 0.65395 0.78581 0.79722 0.00730  -0.01096 0.03849  55  LYS   A NZ  
262  N N   . SER   A 57  ? 0.26051 0.41189 0.36492 -0.01191 -0.02823 0.01064  56  SER   A N   
263  C CA  . SER   A 57  ? 0.25032 0.42821 0.35406 -0.00786 -0.03734 0.01367  56  SER   A CA  
264  C C   . SER   A 57  ? 0.29063 0.46002 0.37828 -0.00467 -0.03955 0.01247  56  SER   A C   
265  O O   . SER   A 57  ? 0.29206 0.47204 0.37590 0.00454  -0.04523 0.02017  56  SER   A O   
266  C CB  . SER   A 57  ? 0.33196 0.53709 0.44428 -0.01895 -0.04217 0.00560  56  SER   A CB  
267  O OG  . SER   A 57  ? 0.44996 0.67600 0.55700 -0.01798 -0.05061 0.00504  56  SER   A OG  
268  N N   . LEU   A 58  ? 0.26440 0.41441 0.34257 -0.01205 -0.03509 0.00301  57  LEU   A N   
269  C CA  . LEU   A 58  ? 0.22966 0.36951 0.29242 -0.00873 -0.03622 0.00169  57  LEU   A CA  
270  C C   . LEU   A 58  ? 0.27474 0.39511 0.33171 0.00455  -0.03351 0.01266  57  LEU   A C   
271  O O   . LEU   A 58  ? 0.28408 0.40838 0.33260 0.01222  -0.03769 0.01791  57  LEU   A O   
272  C CB  . LEU   A 58  ? 0.29963 0.42117 0.35444 -0.01918 -0.03150 -0.01107 57  LEU   A CB  
273  C CG  . LEU   A 58  ? 0.30542 0.44413 0.36248 -0.03265 -0.03466 -0.02347 57  LEU   A CG  
274  C CD1 . LEU   A 58  ? 0.30429 0.41931 0.35511 -0.04196 -0.02860 -0.03503 57  LEU   A CD1 
275  C CD2 . LEU   A 58  ? 0.33813 0.50056 0.38863 -0.03215 -0.04301 -0.02481 57  LEU   A CD2 
276  N N   . LEU   A 59  ? 0.25607 0.35489 0.31706 0.00715  -0.02655 0.01614  58  LEU   A N   
277  C CA  . LEU   A 59  ? 0.25638 0.33614 0.31244 0.01984  -0.02396 0.02668  58  LEU   A CA  
278  C C   . LEU   A 59  ? 0.28079 0.37967 0.34239 0.03091  -0.03005 0.03874  58  LEU   A C   
279  O O   . LEU   A 59  ? 0.30227 0.39392 0.35690 0.04160  -0.03148 0.04708  58  LEU   A O   
280  C CB  . LEU   A 59  ? 0.28704 0.34166 0.34725 0.01993  -0.01562 0.02802  58  LEU   A CB  
281  C CG  . LEU   A 59  ? 0.41777 0.43968 0.46678 0.01965  -0.00915 0.02446  58  LEU   A CG  
282  C CD1 . LEU   A 59  ? 0.43156 0.45148 0.47618 0.00652  -0.00811 0.01049  58  LEU   A CD1 
283  C CD2 . LEU   A 59  ? 0.34431 0.34282 0.39793 0.02205  -0.00176 0.02864  58  LEU   A CD2 
284  N N   . THR   A 60  ? 0.24304 0.36680 0.31739 0.02855  -0.03401 0.03978  59  THR   A N   
285  C CA  . THR   A 60  ? 0.30700 0.45013 0.38746 0.03893  -0.04044 0.05088  59  THR   A CA  
286  C C   . THR   A 60  ? 0.32860 0.48452 0.39953 0.04307  -0.04783 0.05326  59  THR   A C   
287  O O   . THR   A 60  ? 0.33539 0.49319 0.40474 0.05461  -0.05135 0.06398  59  THR   A O   
288  C CB  . THR   A 60  ? 0.32572 0.49481 0.42185 0.03448  -0.04367 0.05011  59  THR   A CB  
289  O OG1 . THR   A 60  ? 0.32442 0.48079 0.42913 0.03181  -0.03645 0.04932  59  THR   A OG1 
290  C CG2 . THR   A 60  ? 0.36418 0.55425 0.46721 0.04513  -0.05094 0.06115  59  THR   A CG2 
291  N N   . GLN   A 61  ? 0.30820 0.47235 0.37230 0.03369  -0.05018 0.04333  60  GLN   A N   
292  C CA  . GLN   A 61  ? 0.36808 0.54529 0.42223 0.03602  -0.05704 0.04431  60  GLN   A CA  
293  C C   . GLN   A 61  ? 0.41009 0.56468 0.44951 0.04214  -0.05422 0.04673  60  GLN   A C   
294  O O   . GLN   A 61  ? 0.40450 0.56841 0.43614 0.04748  -0.05980 0.05135  60  GLN   A O   
295  C CB  . GLN   A 61  ? 0.38103 0.57387 0.43263 0.02336  -0.06003 0.03199  60  GLN   A CB  
296  C CG  . GLN   A 61  ? 0.40807 0.62028 0.47373 0.01497  -0.06165 0.02714  60  GLN   A CG  
297  C CD  . GLN   A 61  ? 0.51953 0.74629 0.58199 0.00254  -0.06483 0.01482  60  GLN   A CD  
298  O OE1 . GLN   A 61  ? 0.56508 0.80044 0.63669 -0.00723 -0.06402 0.00737  60  GLN   A OE1 
299  N NE2 . GLN   A 61  ? 0.53482 0.76441 0.58407 0.00270  -0.06845 0.01247  60  GLN   A NE2 
300  N N   . LEU   A 62  ? 0.34601 0.37117 0.35787 -0.01325 -0.02602 0.00441  61  LEU   A N   
301  C CA  . LEU   A 62  ? 0.34170 0.35650 0.34523 -0.01182 -0.02187 0.00641  61  LEU   A CA  
302  C C   . LEU   A 62  ? 0.35585 0.36780 0.36429 -0.00718 -0.01946 0.01317  61  LEU   A C   
303  O O   . LEU   A 62  ? 0.40521 0.41736 0.42406 -0.00617 -0.01864 0.01387  61  LEU   A O   
304  C CB  . LEU   A 62  ? 0.33584 0.34167 0.33823 -0.01568 -0.01780 0.00175  61  LEU   A CB  
305  C CG  . LEU   A 62  ? 0.35016 0.34684 0.34496 -0.01414 -0.01355 0.00269  61  LEU   A CG  
306  C CD1 . LEU   A 62  ? 0.33086 0.32708 0.31303 -0.01362 -0.01471 0.00097  61  LEU   A CD1 
307  C CD2 . LEU   A 62  ? 0.37207 0.36089 0.36808 -0.01671 -0.00998 -0.00081 61  LEU   A CD2 
308  N N   . ARG   A 63  ? 0.34732 0.35660 0.34828 -0.00456 -0.01809 0.01794  62  ARG   A N   
309  C CA  . ARG   A 63  ? 0.34498 0.34982 0.35005 -0.00153 -0.01513 0.02466  62  ARG   A CA  
310  C C   . ARG   A 63  ? 0.32374 0.32249 0.32297 -0.00249 -0.01027 0.02495  62  ARG   A C   
311  O O   . ARG   A 63  ? 0.33084 0.32947 0.32043 -0.00361 -0.00963 0.02139  62  ARG   A O   
312  C CB  . ARG   A 63  ? 0.39217 0.40146 0.39523 0.00288  -0.01782 0.03259  62  ARG   A CB  
313  C CG  . ARG   A 63  ? 0.49531 0.51215 0.50574 0.00527  -0.02296 0.03287  62  ARG   A CG  
314  C CD  . ARG   A 63  ? 0.65085 0.67588 0.65534 0.00965  -0.02773 0.03885  62  ARG   A CD  
315  N NE  . ARG   A 63  ? 0.67581 0.70261 0.66542 0.00961  -0.02757 0.04051  62  ARG   A NE  
316  C CZ  . ARG   A 63  ? 0.58787 0.62038 0.56830 0.00702  -0.03030 0.03388  62  ARG   A CZ  
317  N NH1 . ARG   A 63  ? 0.64129 0.67730 0.62645 0.00295  -0.03295 0.02540  62  ARG   A NH1 
318  N NH2 . ARG   A 63  ? 0.67088 0.70557 0.63699 0.00832  -0.03013 0.03562  62  ARG   A NH2 
319  N N   . ALA   A 64  ? 0.30640 0.30046 0.31215 -0.00192 -0.00691 0.02882  63  ALA   A N   
320  C CA  . ALA   A 64  ? 0.29946 0.29033 0.30208 -0.00280 -0.00229 0.02933  63  ALA   A CA  
321  C C   . ALA   A 64  ? 0.31510 0.30942 0.30612 -0.00118 -0.00109 0.03286  63  ALA   A C   
322  O O   . ALA   A 64  ? 0.30217 0.29625 0.28673 -0.00141 0.00183  0.03000  63  ALA   A O   
323  C CB  . ALA   A 64  ? 0.35312 0.33999 0.36582 -0.00317 0.00044  0.03334  63  ALA   A CB  
324  N N   . GLU   A 65  ? 0.33609 0.33418 0.32371 0.00122  -0.00325 0.03912  64  GLU   A N   
325  C CA  . GLU   A 65  ? 0.34137 0.34402 0.31638 0.00321  -0.00182 0.04292  64  GLU   A CA  
326  C C   . GLU   A 65  ? 0.34913 0.35480 0.31243 0.00306  -0.00387 0.03497  64  GLU   A C   
327  O O   . GLU   A 65  ? 0.35066 0.35891 0.30298 0.00458  -0.00121 0.03496  64  GLU   A O   
328  C CB  . GLU   A 65  ? 0.40029 0.40674 0.37281 0.00642  -0.00430 0.05194  64  GLU   A CB  
329  C CG  . GLU   A 65  ? 0.43216 0.44299 0.40566 0.00782  -0.01125 0.04944  64  GLU   A CG  
330  C CD  . GLU   A 65  ? 0.71540 0.72954 0.68852 0.01223  -0.01414 0.05931  64  GLU   A CD  
331  O OE1 . GLU   A 65  ? 0.66218 0.68072 0.62372 0.01478  -0.01347 0.06562  64  GLU   A OE1 
332  O OE2 . GLU   A 65  ? 0.75592 0.76837 0.73991 0.01376  -0.01690 0.06100  64  GLU   A OE2 
333  N N   . ASP   A 66  ? 0.32391 0.32924 0.28957 0.00107  -0.00818 0.02790  65  ASP   A N   
334  C CA  . ASP   A 66  ? 0.31763 0.32354 0.27337 -0.00025 -0.01019 0.01950  65  ASP   A CA  
335  C C   . ASP   A 66  ? 0.28265 0.28173 0.23566 -0.00108 -0.00561 0.01433  65  ASP   A C   
336  O O   . ASP   A 66  ? 0.32538 0.32271 0.26858 -0.00133 -0.00622 0.00757  65  ASP   A O   
337  C CB  . ASP   A 66  ? 0.30238 0.30978 0.26341 -0.00341 -0.01545 0.01378  65  ASP   A CB  
338  C CG  . ASP   A 66  ? 0.43756 0.45379 0.40196 -0.00163 -0.02071 0.01820  65  ASP   A CG  
339  O OD1 . ASP   A 66  ? 0.49641 0.51884 0.45162 0.00153  -0.02273 0.02214  65  ASP   A OD1 
340  O OD2 . ASP   A 66  ? 0.42238 0.44017 0.39827 -0.00282 -0.02281 0.01779  65  ASP   A OD2 
341  N N   . LEU   A 67  ? 0.29688 0.29213 0.25841 -0.00118 -0.00141 0.01702  66  LEU   A N   
342  C CA  . LEU   A 67  ? 0.29236 0.28279 0.25249 -0.00076 0.00286  0.01337  66  LEU   A CA  
343  C C   . LEU   A 67  ? 0.27906 0.27311 0.23829 0.00184  0.00809  0.01885  66  LEU   A C   
344  O O   . LEU   A 67  ? 0.28450 0.27689 0.24494 0.00291  0.01188  0.01687  66  LEU   A O   
345  C CB  . LEU   A 67  ? 0.26185 0.24707 0.23258 -0.00303 0.00318  0.01121  66  LEU   A CB  
346  C CG  . LEU   A 67  ? 0.28180 0.26466 0.25508 -0.00623 -0.00090 0.00662  66  LEU   A CG  
347  C CD1 . LEU   A 67  ? 0.28005 0.25910 0.26264 -0.00783 0.00027  0.00555  66  LEU   A CD1 
348  C CD2 . LEU   A 67  ? 0.30890 0.28795 0.27215 -0.00735 -0.00242 -0.00020 66  LEU   A CD2 
349  N N   . ASN   A 68  ? 0.29325 0.29284 0.25112 0.00291  0.00848  0.02627  67  ASN   A N   
350  C CA  . ASN   A 68  ? 0.30640 0.31045 0.26494 0.00427  0.01401  0.03304  67  ASN   A CA  
351  C C   . ASN   A 68  ? 0.31977 0.32175 0.29237 0.00207  0.01683  0.03484  67  ASN   A C   
352  O O   . ASN   A 68  ? 0.31902 0.32500 0.29362 0.00262  0.02183  0.03685  67  ASN   A O   
353  C CB  . ASN   A 68  ? 0.26837 0.27613 0.21505 0.00751  0.01781  0.02973  67  ASN   A CB  
354  C CG  . ASN   A 68  ? 0.32631 0.33785 0.25779 0.00983  0.01528  0.02845  67  ASN   A CG  
355  O OD1 . ASN   A 68  ? 0.34457 0.35311 0.26738 0.01057  0.01268  0.01967  67  ASN   A OD1 
356  N ND2 . ASN   A 68  ? 0.34365 0.36143 0.27156 0.01088  0.01585  0.03719  67  ASN   A ND2 
357  N N   . ILE   A 69  ? 0.29811 0.29526 0.28066 -0.00032 0.01362  0.03377  68  ILE   A N   
358  C CA  . ILE   A 69  ? 0.26557 0.26088 0.26123 -0.00262 0.01527  0.03444  68  ILE   A CA  
359  C C   . ILE   A 69  ? 0.27739 0.27131 0.28130 -0.00421 0.01488  0.04180  68  ILE   A C   
360  O O   . ILE   A 69  ? 0.34208 0.33282 0.34793 -0.00396 0.01097  0.04226  68  ILE   A O   
361  C CB  . ILE   A 69  ? 0.26936 0.25994 0.26935 -0.00368 0.01246  0.02729  68  ILE   A CB  
362  C CG1 . ILE   A 69  ? 0.27901 0.26859 0.27102 -0.00191 0.01329  0.02107  68  ILE   A CG1 
363  C CG2 . ILE   A 69  ? 0.33904 0.32864 0.35186 -0.00589 0.01327  0.02754  68  ILE   A CG2 
364  C CD1 . ILE   A 69  ? 0.28131 0.26559 0.27544 -0.00303 0.01075  0.01526  68  ILE   A CD1 
365  N N   . ALA   A 70  ? 0.31360 0.30982 0.32310 -0.00579 0.01904  0.04762  69  ALA   A N   
366  C CA  . ALA   A 70  ? 0.36532 0.35738 0.38378 -0.00782 0.01900  0.05472  69  ALA   A CA  
367  C C   . ALA   A 70  ? 0.30381 0.29008 0.33508 -0.01035 0.01685  0.04991  69  ALA   A C   
368  O O   . ALA   A 70  ? 0.31447 0.30280 0.35028 -0.01188 0.01775  0.04429  69  ALA   A O   
369  C CB  . ALA   A 70  ? 0.35668 0.35270 0.37815 -0.01000 0.02469  0.06286  69  ALA   A CB  
370  N N   . PRO   A 71  ? 0.33058 0.31019 0.36748 -0.01015 0.01393  0.05170  70  PRO   A N   
371  C CA  . PRO   A 71  ? 0.33744 0.31169 0.38597 -0.01219 0.01227  0.04638  70  PRO   A CA  
372  C C   . PRO   A 71  ? 0.33769 0.31227 0.39603 -0.01675 0.01554  0.04718  70  PRO   A C   
373  O O   . PRO   A 71  ? 0.33581 0.31074 0.39635 -0.01893 0.01900  0.05503  70  PRO   A O   
374  C CB  . PRO   A 71  ? 0.33737 0.30426 0.39003 -0.01026 0.00960  0.05014  70  PRO   A CB  
375  C CG  . PRO   A 71  ? 0.43885 0.40984 0.48000 -0.00628 0.00785  0.05408  70  PRO   A CG  
376  C CD  . PRO   A 71  ? 0.38517 0.36251 0.41763 -0.00709 0.01161  0.05794  70  PRO   A CD  
377  N N   . ARG   A 72  ? 0.29718 0.27300 0.36122 -0.01838 0.01448  0.03917  71  ARG   A N   
378  C CA  . ARG   A 72  ? 0.30493 0.28327 0.37944 -0.02304 0.01650  0.03812  71  ARG   A CA  
379  C C   . ARG   A 72  ? 0.27524 0.24480 0.36140 -0.02585 0.01435  0.03543  71  ARG   A C   
380  O O   . ARG   A 72  ? 0.32489 0.28958 0.41072 -0.02336 0.01100  0.03002  71  ARG   A O   
381  C CB  . ARG   A 72  ? 0.29741 0.28404 0.37028 -0.02242 0.01621  0.03097  71  ARG   A CB  
382  C CG  . ARG   A 72  ? 0.27370 0.26733 0.33544 -0.01916 0.01872  0.03312  71  ARG   A CG  
383  C CD  . ARG   A 72  ? 0.28887 0.28959 0.34915 -0.01749 0.01866  0.02709  71  ARG   A CD  
384  N NE  . ARG   A 72  ? 0.27913 0.28429 0.32846 -0.01365 0.02120  0.02867  71  ARG   A NE  
385  C CZ  . ARG   A 72  ? 0.27025 0.28048 0.31564 -0.01043 0.02182  0.02470  71  ARG   A CZ  
386  N NH1 . ARG   A 72  ? 0.27261 0.28559 0.32363 -0.01044 0.01991  0.01974  71  ARG   A NH1 
387  N NH2 . ARG   A 72  ? 0.32635 0.33875 0.36134 -0.00655 0.02425  0.02559  71  ARG   A NH2 
388  N N   . LYS   A 73  ? 0.29408 0.26156 0.39080 -0.03117 0.01658  0.03910  72  LYS   A N   
389  C CA  . LYS   A 73  ? 0.30090 0.25806 0.40932 -0.03443 0.01466  0.03604  72  LYS   A CA  
390  C C   . LYS   A 73  ? 0.29161 0.25432 0.41087 -0.04025 0.01442  0.02953  72  LYS   A C   
391  O O   . LYS   A 73  ? 0.30958 0.28453 0.42893 -0.04195 0.01641  0.02968  72  LYS   A O   
392  C CB  . LYS   A 73  ? 0.29290 0.23917 0.40581 -0.03633 0.01688  0.04629  72  LYS   A CB  
393  C CG  . LYS   A 73  ? 0.36256 0.30523 0.46452 -0.02976 0.01617  0.05275  72  LYS   A CG  
394  C CD  . LYS   A 73  ? 0.40306 0.33399 0.50849 -0.03023 0.01785  0.06379  72  LYS   A CD  
395  C CE  . LYS   A 73  ? 0.47619 0.40579 0.57068 -0.02265 0.01584  0.06913  72  LYS   A CE  
396  N NZ  . LYS   A 73  ? 0.45614 0.37570 0.55131 -0.02165 0.01748  0.08196  72  LYS   A NZ  
397  N N   . ALA   A 74  ? 0.29266 0.24692 0.42128 -0.04287 0.01163  0.02303  73  ALA   A N   
398  C CA  . ALA   A 74  ? 0.28291 0.24359 0.42102 -0.04795 0.00985  0.01448  73  ALA   A CA  
399  C C   . ALA   A 74  ? 0.33505 0.30190 0.48380 -0.05563 0.01339  0.01994  73  ALA   A C   
400  O O   . ALA   A 74  ? 0.38148 0.34171 0.53373 -0.05871 0.01712  0.02981  73  ALA   A O   
401  C CB  . ALA   A 74  ? 0.37758 0.32678 0.52335 -0.04944 0.00614  0.00576  73  ALA   A CB  
402  N N   . THR   A 75  ? 0.33196 0.31283 0.48597 -0.05852 0.01232  0.01393  74  THR   A N   
403  C CA  . THR   A 75  ? 0.36325 0.35291 0.53066 -0.06674 0.01511  0.01701  74  THR   A CA  
404  C C   . THR   A 75  ? 0.33642 0.31840 0.51983 -0.07534 0.01260  0.01109  74  THR   A C   
405  O O   . THR   A 75  ? 0.35878 0.34231 0.55531 -0.08396 0.01574  0.01603  74  THR   A O   
406  C CB  . THR   A 75  ? 0.44033 0.45075 0.60754 -0.06541 0.01472  0.01312  74  THR   A CB  
407  O OG1 . THR   A 75  ? 0.38078 0.39537 0.55145 -0.06560 0.00875  0.00092  74  THR   A OG1 
408  C CG2 . THR   A 75  ? 0.41561 0.43142 0.56629 -0.05633 0.01649  0.01668  74  THR   A CG2 
409  N N   . LEU   A 76  ? 0.31136 0.28533 0.49407 -0.07345 0.00730  0.00041  75  LEU   A N   
410  C CA  . LEU   A 76  ? 0.29779 0.26511 0.49439 -0.08089 0.00370  -0.00878 75  LEU   A CA  
411  C C   . LEU   A 76  ? 0.33299 0.31885 0.54080 -0.08748 0.00158  -0.01526 75  LEU   A C   
412  O O   . LEU   A 76  ? 0.35242 0.33507 0.57426 -0.09587 -0.00117 -0.02240 75  LEU   A O   
413  C CB  . LEU   A 76  ? 0.33837 0.28714 0.54553 -0.08764 0.00668  -0.00182 75  LEU   A CB  
414  C CG  . LEU   A 76  ? 0.37701 0.30815 0.57393 -0.08037 0.00840  0.00557  75  LEU   A CG  
415  C CD1 . LEU   A 76  ? 0.37537 0.28630 0.58285 -0.08639 0.01098  0.01275  75  LEU   A CD1 
416  C CD2 . LEU   A 76  ? 0.39914 0.32452 0.58683 -0.07201 0.00372  -0.00460 75  LEU   A CD2 
417  N N   . GLN   A 77  ? 0.33892 0.34427 0.54141 -0.08373 0.00252  -0.01329 76  GLN   A N   
418  C CA  . GLN   A 77  ? 0.37329 0.39913 0.58558 -0.08788 -0.00025 -0.01972 76  GLN   A CA  
419  C C   . GLN   A 77  ? 0.33578 0.37134 0.53682 -0.07968 -0.00566 -0.02900 76  GLN   A C   
420  O O   . GLN   A 77  ? 0.31951 0.35043 0.50439 -0.07054 -0.00509 -0.02695 76  GLN   A O   
421  C CB  . GLN   A 77  ? 0.38476 0.42775 0.60129 -0.08929 0.00521  -0.01018 76  GLN   A CB  
422  C CG  . GLN   A 77  ? 0.40302 0.43793 0.62668 -0.09577 0.01220  0.00207  76  GLN   A CG  
423  C CD  . GLN   A 77  ? 0.52423 0.54658 0.76456 -0.10731 0.01123  -0.00036 76  GLN   A CD  
424  O OE1 . GLN   A 77  ? 0.55999 0.58995 0.81350 -0.11416 0.00656  -0.01042 76  GLN   A OE1 
425  N NE2 . GLN   A 77  ? 0.39879 0.40093 0.63828 -0.10924 0.01516  0.00847  76  GLN   A NE2 
426  N N   . PRO   A 78  ? 0.35661 0.40652 0.56575 -0.08285 -0.01099 -0.03883 77  PRO   A N   
427  C CA  . PRO   A 78  ? 0.32384 0.38454 0.52120 -0.07444 -0.01585 -0.04597 77  PRO   A CA  
428  C C   . PRO   A 78  ? 0.32145 0.39399 0.50880 -0.06634 -0.01254 -0.03799 77  PRO   A C   
429  O O   . PRO   A 78  ? 0.36128 0.44173 0.55477 -0.06839 -0.00773 -0.02983 77  PRO   A O   
430  C CB  . PRO   A 78  ? 0.36658 0.44322 0.57709 -0.08056 -0.02214 -0.05671 77  PRO   A CB  
431  C CG  . PRO   A 78  ? 0.43756 0.51239 0.66831 -0.09319 -0.02025 -0.05532 77  PRO   A CG  
432  C CD  . PRO   A 78  ? 0.40450 0.46298 0.63423 -0.09451 -0.01260 -0.04283 77  PRO   A CD  
433  N N   . LEU   A 79  ? 0.30573 0.37885 0.47734 -0.05701 -0.01479 -0.04043 78  LEU   A N   
434  C CA  . LEU   A 79  ? 0.29411 0.37600 0.45532 -0.04870 -0.01221 -0.03407 78  LEU   A CA  
435  C C   . LEU   A 79  ? 0.24953 0.35428 0.41736 -0.04741 -0.01560 -0.03739 78  LEU   A C   
436  O O   . LEU   A 79  ? 0.29044 0.40253 0.45780 -0.04639 -0.02189 -0.04601 78  LEU   A O   
437  C CB  . LEU   A 79  ? 0.31182 0.38407 0.45441 -0.04002 -0.01291 -0.03456 78  LEU   A CB  
438  C CG  . LEU   A 79  ? 0.32905 0.40594 0.45960 -0.03140 -0.01031 -0.02845 78  LEU   A CG  
439  C CD1 . LEU   A 79  ? 0.36747 0.43830 0.49689 -0.03164 -0.00386 -0.01915 78  LEU   A CD1 
440  C CD2 . LEU   A 79  ? 0.36037 0.42928 0.47459 -0.02446 -0.01201 -0.03046 78  LEU   A CD2 
441  N N   . PRO   A 80  ? 0.24751 0.36507 0.42139 -0.04685 -0.01177 -0.03104 79  PRO   A N   
442  C CA  . PRO   A 80  ? 0.28132 0.42284 0.46311 -0.04474 -0.01508 -0.03395 79  PRO   A CA  
443  C C   . PRO   A 80  ? 0.25932 0.40419 0.42523 -0.03298 -0.01807 -0.03499 79  PRO   A C   
444  O O   . PRO   A 80  ? 0.24606 0.37655 0.39591 -0.02648 -0.01515 -0.03064 79  PRO   A O   
445  C CB  . PRO   A 80  ? 0.30113 0.45310 0.49155 -0.04578 -0.00838 -0.02551 79  PRO   A CB  
446  C CG  . PRO   A 80  ? 0.33603 0.46971 0.52564 -0.05127 -0.00232 -0.01900 79  PRO   A CG  
447  C CD  . PRO   A 80  ? 0.31919 0.43156 0.49335 -0.04782 -0.00413 -0.02100 79  PRO   A CD  
448  N N   . PRO   A 81  ? 0.23027 0.39435 0.40055 -0.03009 -0.02388 -0.04016 80  PRO   A N   
449  C CA  . PRO   A 81  ? 0.25597 0.42202 0.41040 -0.01887 -0.02739 -0.04089 80  PRO   A CA  
450  C C   . PRO   A 81  ? 0.25401 0.41721 0.39758 -0.00901 -0.02231 -0.03243 80  PRO   A C   
451  O O   . PRO   A 81  ? 0.28274 0.43896 0.41020 -0.00034 -0.02348 -0.03118 80  PRO   A O   
452  C CB  . PRO   A 81  ? 0.33436 0.52536 0.49917 -0.01836 -0.03462 -0.04717 80  PRO   A CB  
453  C CG  . PRO   A 81  ? 0.35815 0.55570 0.54278 -0.03135 -0.03633 -0.05293 80  PRO   A CG  
454  C CD  . PRO   A 81  ? 0.26274 0.44735 0.45300 -0.03767 -0.02810 -0.04591 80  PRO   A CD  
455  N N   . ASN   A 82  ? 0.24277 0.41129 0.39444 -0.01000 -0.01658 -0.02681 81  ASN   A N   
456  C CA  . ASN   A 82  ? 0.21948 0.38641 0.36146 -0.00014 -0.01186 -0.02018 81  ASN   A CA  
457  C C   . ASN   A 82  ? 0.28565 0.42964 0.41440 0.00026  -0.00621 -0.01531 81  ASN   A C   
458  O O   . ASN   A 82  ? 0.36183 0.50132 0.48094 0.00799  -0.00231 -0.01077 81  ASN   A O   
459  C CB  . ASN   A 82  ? 0.23133 0.41842 0.38805 0.00002  -0.00821 -0.01716 81  ASN   A CB  
460  C CG  . ASN   A 82  ? 0.27514 0.46058 0.44351 -0.01062 -0.00264 -0.01426 81  ASN   A CG  
461  O OD1 . ASN   A 82  ? 0.26745 0.44498 0.44146 -0.02049 -0.00422 -0.01701 81  ASN   A OD1 
462  N ND2 . ASN   A 82  ? 0.30116 0.49318 0.47232 -0.00816 0.00426  -0.00840 81  ASN   A ND2 
463  N N   . LEU   A 83  ? 0.24181 0.37141 0.36999 -0.00744 -0.00599 -0.01660 82  LEU   A N   
464  C CA  . LEU   A 83  ? 0.22455 0.33443 0.34098 -0.00702 -0.00142 -0.01215 82  LEU   A CA  
465  C C   . LEU   A 83  ? 0.21101 0.30612 0.31331 -0.00421 -0.00433 -0.01466 82  LEU   A C   
466  O O   . LEU   A 83  ? 0.24803 0.34326 0.35246 -0.00735 -0.00889 -0.02027 82  LEU   A O   
467  C CB  . LEU   A 83  ? 0.33049 0.43405 0.45583 -0.01659 0.00154  -0.01030 82  LEU   A CB  
468  C CG  . LEU   A 83  ? 0.43437 0.55101 0.57377 -0.02111 0.00600  -0.00618 82  LEU   A CG  
469  C CD1 . LEU   A 83  ? 0.39426 0.49926 0.53736 -0.02899 0.00986  -0.00189 82  LEU   A CD1 
470  C CD2 . LEU   A 83  ? 0.35171 0.47657 0.48587 -0.01291 0.01044  -0.00168 82  LEU   A CD2 
471  N N   . PRO   A 84  ? 0.24606 0.32846 0.33418 0.00113  -0.00151 -0.01095 83  PRO   A N   
472  C CA  . PRO   A 84  ? 0.26164 0.33138 0.33731 0.00318  -0.00352 -0.01263 83  PRO   A CA  
473  C C   . PRO   A 84  ? 0.23577 0.29464 0.31319 -0.00353 -0.00337 -0.01424 83  PRO   A C   
474  O O   . PRO   A 84  ? 0.24885 0.30425 0.33229 -0.00824 -0.00041 -0.01154 83  PRO   A O   
475  C CB  . PRO   A 84  ? 0.27179 0.33154 0.33439 0.00945  0.00003  -0.00797 83  PRO   A CB  
476  C CG  . PRO   A 84  ? 0.27022 0.33214 0.33784 0.00803  0.00469  -0.00426 83  PRO   A CG  
477  C CD  . PRO   A 84  ? 0.28905 0.36878 0.37239 0.00501  0.00382  -0.00555 83  PRO   A CD  
478  N N   . PRO   A 85  ? 0.21762 0.27087 0.28941 -0.00353 -0.00620 -0.01818 84  PRO   A N   
479  C CA  . PRO   A 85  ? 0.21582 0.25837 0.28902 -0.00841 -0.00584 -0.01989 84  PRO   A CA  
480  C C   . PRO   A 85  ? 0.20597 0.23607 0.27092 -0.00735 -0.00216 -0.01494 84  PRO   A C   
481  O O   . PRO   A 85  ? 0.23387 0.25638 0.30201 -0.01101 -0.00118 -0.01442 84  PRO   A O   
482  C CB  . PRO   A 85  ? 0.28359 0.32661 0.35191 -0.00709 -0.00957 -0.02595 84  PRO   A CB  
483  C CG  . PRO   A 85  ? 0.26503 0.31355 0.32324 -0.00018 -0.01049 -0.02418 84  PRO   A CG  
484  C CD  . PRO   A 85  ? 0.21380 0.27229 0.27860 0.00126  -0.00992 -0.02132 84  PRO   A CD  
485  N N   . VAL   A 86  ? 0.22667 0.25443 0.28137 -0.00229 -0.00051 -0.01162 85  VAL   A N   
486  C CA  . VAL   A 86  ? 0.21533 0.23203 0.26115 -0.00133 0.00214  -0.00819 85  VAL   A CA  
487  C C   . VAL   A 86  ? 0.21217 0.22895 0.25287 0.00259  0.00480  -0.00433 85  VAL   A C   
488  O O   . VAL   A 86  ? 0.22697 0.25031 0.26685 0.00690  0.00433  -0.00434 85  VAL   A O   
489  C CB  . VAL   A 86  ? 0.23466 0.24555 0.27122 0.00051  0.00118  -0.00973 85  VAL   A CB  
490  C CG1 . VAL   A 86  ? 0.25173 0.25250 0.28119 0.00017  0.00349  -0.00685 85  VAL   A CG1 
491  C CG2 . VAL   A 86  ? 0.25175 0.26396 0.29292 -0.00228 -0.00113 -0.01461 85  VAL   A CG2 
492  N N   . THR   A 87  ? 0.21937 0.22935 0.25634 0.00176  0.00741  -0.00137 86  THR   A N   
493  C CA  . THR   A 87  ? 0.21824 0.22654 0.24835 0.00591  0.01006  0.00101  86  THR   A CA  
494  C C   . THR   A 87  ? 0.19875 0.19521 0.21871 0.00585  0.01069  0.00152  86  THR   A C   
495  O O   . THR   A 87  ? 0.23823 0.23027 0.25845 0.00234  0.00948  0.00090  86  THR   A O   
496  C CB  . THR   A 87  ? 0.22523 0.23992 0.26079 0.00497  0.01300  0.00374  86  THR   A CB  
497  O OG1 . THR   A 87  ? 0.25909 0.27045 0.29800 -0.00013 0.01342  0.00563  86  THR   A OG1 
498  C CG2 . THR   A 87  ? 0.26275 0.29121 0.30955 0.00486  0.01271  0.00320  86  THR   A CG2 
499  N N   . TYR   A 88  ? 0.22422 0.21606 0.23590 0.00993  0.01243  0.00208  87  TYR   A N   
500  C CA  . TYR   A 88  ? 0.24525 0.22558 0.24726 0.00958  0.01271  0.00164  87  TYR   A CA  
501  C C   . TYR   A 88  ? 0.26423 0.24210 0.26051 0.01175  0.01509  0.00188  87  TYR   A C   
502  O O   . TYR   A 88  ? 0.26962 0.25105 0.26506 0.01674  0.01702  0.00193  87  TYR   A O   
503  C CB  . TYR   A 88  ? 0.26803 0.24146 0.26350 0.01248  0.01209  0.00107  87  TYR   A CB  
504  C CG  . TYR   A 88  ? 0.27552 0.23636 0.26205 0.01120  0.01264  0.00048  87  TYR   A CG  
505  C CD1 . TYR   A 88  ? 0.26470 0.22230 0.25141 0.00581  0.01156  0.00002  87  TYR   A CD1 
506  C CD2 . TYR   A 88  ? 0.28301 0.23539 0.26166 0.01536  0.01422  -0.00014 87  TYR   A CD2 
507  C CE1 . TYR   A 88  ? 0.26462 0.21207 0.24476 0.00343  0.01182  -0.00089 87  TYR   A CE1 
508  C CE2 . TYR   A 88  ? 0.25715 0.19696 0.22828 0.01310  0.01443  -0.00155 87  TYR   A CE2 
509  C CZ  . TYR   A 88  ? 0.27400 0.21197 0.24634 0.00659  0.01311  -0.00181 87  TYR   A CZ  
510  O OH  . TYR   A 88  ? 0.29691 0.22379 0.26345 0.00309  0.01306  -0.00349 87  TYR   A OH  
511  N N   . MET   A 89  ? 0.22637 0.19939 0.21854 0.00861  0.01486  0.00164  88  MET   A N   
512  C CA  . MET   A 89  ? 0.23997 0.20923 0.22375 0.01087  0.01659  0.00049  88  MET   A CA  
513  C C   . MET   A 89  ? 0.27063 0.22731 0.24558 0.01017  0.01546  -0.00256 88  MET   A C   
514  O O   . MET   A 89  ? 0.27873 0.23217 0.25419 0.00539  0.01332  -0.00296 88  MET   A O   
515  C CB  . MET   A 89  ? 0.30310 0.27713 0.28663 0.00867  0.01713  0.00223  88  MET   A CB  
516  C CG  . MET   A 89  ? 0.27884 0.26371 0.27145 0.00743  0.01859  0.00645  88  MET   A CG  
517  S SD  . MET   A 89  ? 0.26236 0.24861 0.25632 0.00300  0.01720  0.01009  88  MET   A SD  
518  C CE  . MET   A 89  ? 0.27962 0.27639 0.28333 0.00223  0.02054  0.01558  88  MET   A CE  
519  N N   . HIS   A 90  ? 0.25554 0.20511 0.22315 0.01490  0.01705  -0.00485 89  HIS   A N   
520  C CA  A HIS   A 90  ? 0.26694 0.20232 0.22627 0.01381  0.01628  -0.00808 89  HIS   A CA  
521  C CA  B HIS   A 90  ? 0.26459 0.20008 0.22414 0.01352  0.01617  -0.00801 89  HIS   A CA  
522  C C   . HIS   A 90  ? 0.27535 0.20849 0.22812 0.01173  0.01570  -0.01154 89  HIS   A C   
523  O O   . HIS   A 90  ? 0.31690 0.25483 0.26617 0.01559  0.01760  -0.01254 89  HIS   A O   
524  C CB  A HIS   A 90  ? 0.33311 0.25997 0.28729 0.02064  0.01818  -0.00918 89  HIS   A CB  
525  C CB  B HIS   A 90  ? 0.33411 0.25979 0.28843 0.01968  0.01782  -0.00902 89  HIS   A CB  
526  C CG  A HIS   A 90  ? 0.32690 0.23705 0.27156 0.02031  0.01813  -0.01334 89  HIS   A CG  
527  C CG  B HIS   A 90  ? 0.29423 0.20364 0.24251 0.01693  0.01700  -0.01073 89  HIS   A CG  
528  N ND1 A HIS   A 90  ? 0.34968 0.24976 0.29302 0.01400  0.01641  -0.01373 89  HIS   A ND1 
529  N ND1 B HIS   A 90  ? 0.29925 0.20658 0.25055 0.01062  0.01544  -0.00880 89  HIS   A ND1 
530  C CD2 A HIS   A 90  ? 0.37796 0.27948 0.31440 0.02520  0.01973  -0.01781 89  HIS   A CD2 
531  C CD2 B HIS   A 90  ? 0.31725 0.21134 0.25700 0.01921  0.01786  -0.01433 89  HIS   A CD2 
532  C CE1 A HIS   A 90  ? 0.32781 0.21282 0.26303 0.01423  0.01670  -0.01814 89  HIS   A CE1 
533  C CE1 B HIS   A 90  ? 0.31984 0.21184 0.26529 0.00849  0.01561  -0.01032 89  HIS   A CE1 
534  N NE2 A HIS   A 90  ? 0.38584 0.27074 0.31624 0.02134  0.01855  -0.02113 89  HIS   A NE2 
535  N NE2 B HIS   A 90  ? 0.34525 0.22780 0.28362 0.01350  0.01684  -0.01385 89  HIS   A NE2 
536  N N   . ILE   A 91  ? 0.28035 0.20781 0.23140 0.00578  0.01312  -0.01350 90  ILE   A N   
537  C CA  . ILE   A 91  ? 0.28559 0.21142 0.22991 0.00348  0.01148  -0.01771 90  ILE   A CA  
538  C C   . ILE   A 91  ? 0.30560 0.21570 0.24162 0.00281  0.01113  -0.02350 90  ILE   A C   
539  O O   . ILE   A 91  ? 0.32676 0.23272 0.25408 0.00565  0.01158  -0.02856 90  ILE   A O   
540  C CB  . ILE   A 91  ? 0.27625 0.20961 0.22565 -0.00283 0.00810  -0.01633 90  ILE   A CB  
541  C CG1 . ILE   A 91  ? 0.27482 0.22123 0.23125 -0.00139 0.00872  -0.01089 90  ILE   A CG1 
542  C CG2 . ILE   A 91  ? 0.32368 0.25614 0.26565 -0.00539 0.00532  -0.02125 90  ILE   A CG2 
543  C CD1 . ILE   A 91  ? 0.30790 0.26134 0.27035 -0.00595 0.00552  -0.00876 90  ILE   A CD1 
544  N N   . TYR   A 92  ? 0.31368 0.21441 0.25195 -0.00111 0.01057  -0.02297 91  TYR   A N   
545  C CA  . TYR   A 92  ? 0.31802 0.20126 0.24917 -0.00258 0.01053  -0.02796 91  TYR   A CA  
546  C C   . TYR   A 92  ? 0.31685 0.19093 0.25146 -0.00553 0.01144  -0.02424 91  TYR   A C   
547  O O   . TYR   A 92  ? 0.33599 0.21881 0.27814 -0.00864 0.01112  -0.01950 91  TYR   A O   
548  C CB  . TYR   A 92  ? 0.32473 0.20658 0.25279 -0.00950 0.00702  -0.03396 91  TYR   A CB  
549  C CG  . TYR   A 92  ? 0.36205 0.22719 0.28018 -0.00866 0.00705  -0.04170 91  TYR   A CG  
550  C CD1 . TYR   A 92  ? 0.40848 0.27323 0.31807 -0.00122 0.00845  -0.04605 91  TYR   A CD1 
551  C CD2 . TYR   A 92  ? 0.41116 0.26052 0.32869 -0.01508 0.00622  -0.04460 91  TYR   A CD2 
552  C CE1 . TYR   A 92  ? 0.46707 0.31572 0.36707 0.00049  0.00860  -0.05426 91  TYR   A CE1 
553  C CE2 . TYR   A 92  ? 0.42323 0.25482 0.33174 -0.01438 0.00616  -0.05253 91  TYR   A CE2 
554  C CZ  . TYR   A 92  ? 0.46556 0.29657 0.36506 -0.00611 0.00724  -0.05775 91  TYR   A CZ  
555  O OH  . TYR   A 92  ? 0.51257 0.32517 0.40260 -0.00454 0.00728  -0.06676 91  TYR   A OH  
556  N N   . GLU   A 93  ? 0.35823 0.21398 0.28672 -0.00446 0.01275  -0.02644 92  GLU   A N   
557  C CA  . GLU   A 93  ? 0.36747 0.21272 0.29798 -0.00915 0.01366  -0.02265 92  GLU   A CA  
558  C C   . GLU   A 93  ? 0.42320 0.24674 0.34713 -0.01229 0.01383  -0.02757 92  GLU   A C   
559  O O   . GLU   A 93  ? 0.44969 0.26317 0.36610 -0.00695 0.01419  -0.03316 92  GLU   A O   
560  C CB  . GLU   A 93  ? 0.41884 0.26409 0.35041 -0.00240 0.01619  -0.01559 92  GLU   A CB  
561  C CG  . GLU   A 93  ? 0.50160 0.32697 0.42579 0.00362  0.01840  -0.01505 92  GLU   A CG  
562  C CD  . GLU   A 93  ? 0.39569 0.22039 0.31495 0.01328  0.01913  -0.01935 92  GLU   A CD  
563  O OE1 . GLU   A 93  ? 0.39822 0.24026 0.32068 0.01560  0.01854  -0.02038 92  GLU   A OE1 
564  O OE2 . GLU   A 93  ? 0.46835 0.27534 0.38078 0.01865  0.02061  -0.02157 92  GLU   A OE2 
565  N N   . THR   A 94  ? 0.39529 0.21191 0.32250 -0.02133 0.01379  -0.02577 93  THR   A N   
566  C CA  . THR   A 94  ? 0.40368 0.19741 0.32649 -0.02619 0.01447  -0.02877 93  THR   A CA  
567  C C   . THR   A 94  ? 0.43388 0.21847 0.35823 -0.02752 0.01781  -0.01978 93  THR   A C   
568  O O   . THR   A 94  ? 0.46139 0.25767 0.38870 -0.02341 0.01921  -0.01256 93  THR   A O   
569  C CB  . THR   A 94  ? 0.47813 0.27295 0.40428 -0.03809 0.01119  -0.03537 93  THR   A CB  
570  O OG1 . THR   A 94  ? 0.46901 0.27639 0.40487 -0.04632 0.01126  -0.03001 93  THR   A OG1 
571  C CG2 . THR   A 94  ? 0.47754 0.28542 0.40175 -0.03675 0.00739  -0.04304 93  THR   A CG2 
572  N N   . ASP   A 95  ? 0.48843 0.25150 0.41034 -0.03357 0.01914  -0.02014 94  ASP   A N   
573  C CA  . ASP   A 95  ? 0.50885 0.26423 0.43206 -0.03637 0.02269  -0.01043 94  ASP   A CA  
574  C C   . ASP   A 95  ? 0.52020 0.29469 0.45295 -0.04563 0.02278  -0.00654 94  ASP   A C   
575  O O   . ASP   A 95  ? 0.55657 0.33335 0.49052 -0.04591 0.02594  0.00236  94  ASP   A O   
576  C CB  . ASP   A 95  ? 0.60166 0.32843 0.52088 -0.04213 0.02443  -0.01130 94  ASP   A CB  
577  C CG  . ASP   A 95  ? 0.63046 0.33561 0.54029 -0.03063 0.02673  -0.00835 94  ASP   A CG  
578  O OD1 . ASP   A 95  ? 0.61043 0.32490 0.51765 -0.01855 0.02712  -0.00459 94  ASP   A OD1 
579  O OD2 . ASP   A 95  ? 0.64736 0.32599 0.55305 -0.03375 0.02801  -0.00999 94  ASP   A OD2 
580  N N   . GLY   A 96  ? 0.45008 0.23889 0.38916 -0.05247 0.01939  -0.01308 95  GLY   A N   
581  C CA  . GLY   A 96  ? 0.42406 0.23083 0.37320 -0.06112 0.01935  -0.01054 95  GLY   A CA  
582  C C   . GLY   A 96  ? 0.42815 0.25913 0.38196 -0.05568 0.01835  -0.00829 95  GLY   A C   
583  O O   . GLY   A 96  ? 0.38148 0.22573 0.34229 -0.05975 0.01986  -0.00391 95  GLY   A O   
584  N N   . PHE   A 97  ? 0.37781 0.21483 0.32830 -0.04686 0.01615  -0.01135 96  PHE   A N   
585  C CA  . PHE   A 97  ? 0.34356 0.20198 0.29938 -0.04277 0.01500  -0.00967 96  PHE   A CA  
586  C C   . PHE   A 97  ? 0.35884 0.21898 0.30969 -0.03221 0.01429  -0.01068 96  PHE   A C   
587  O O   . PHE   A 97  ? 0.36531 0.21396 0.30925 -0.02842 0.01387  -0.01471 96  PHE   A O   
588  C CB  . PHE   A 97  ? 0.35309 0.22706 0.31665 -0.04898 0.01146  -0.01413 96  PHE   A CB  
589  C CG  . PHE   A 97  ? 0.33647 0.20963 0.29591 -0.04746 0.00774  -0.02131 96  PHE   A CG  
590  C CD1 . PHE   A 97  ? 0.39237 0.25305 0.34830 -0.05327 0.00611  -0.02740 96  PHE   A CD1 
591  C CD2 . PHE   A 97  ? 0.35977 0.24409 0.31830 -0.04045 0.00610  -0.02197 96  PHE   A CD2 
592  C CE1 . PHE   A 97  ? 0.42783 0.28825 0.37823 -0.05147 0.00263  -0.03478 96  PHE   A CE1 
593  C CE2 . PHE   A 97  ? 0.38492 0.26922 0.33808 -0.03872 0.00323  -0.02797 96  PHE   A CE2 
594  C CZ  . PHE   A 97  ? 0.39699 0.26964 0.34543 -0.04390 0.00140  -0.03471 96  PHE   A CZ  
595  N N   . SER   A 98  ? 0.33424 0.20959 0.28933 -0.02779 0.01428  -0.00748 97  SER   A N   
596  C CA  A SER   A 98  ? 0.31641 0.19837 0.27002 -0.01947 0.01353  -0.00819 97  SER   A CA  
597  C CA  B SER   A 98  ? 0.31586 0.19788 0.26951 -0.01944 0.01356  -0.00811 97  SER   A CA  
598  C C   . SER   A 98  ? 0.32389 0.22311 0.28444 -0.02092 0.01114  -0.00949 97  SER   A C   
599  O O   . SER   A 98  ? 0.32219 0.23058 0.28958 -0.02541 0.01068  -0.00802 97  SER   A O   
600  C CB  A SER   A 98  ? 0.36387 0.24736 0.31662 -0.01251 0.01548  -0.00301 97  SER   A CB  
601  C CB  B SER   A 98  ? 0.36421 0.24771 0.31708 -0.01270 0.01554  -0.00282 97  SER   A CB  
602  O OG  A SER   A 98  ? 0.33948 0.23698 0.29902 -0.01402 0.01531  -0.00024 97  SER   A OG  
603  O OG  B SER   A 98  ? 0.35349 0.24426 0.30647 -0.00543 0.01499  -0.00357 97  SER   A OG  
604  N N   . LEU   A 99  ? 0.29717 0.20076 0.25584 -0.01657 0.00998  -0.01185 98  LEU   A N   
605  C CA  . LEU   A 99  ? 0.29175 0.20925 0.25551 -0.01750 0.00769  -0.01245 98  LEU   A CA  
606  C C   . LEU   A 99  ? 0.27033 0.19481 0.23458 -0.01080 0.00860  -0.01062 98  LEU   A C   
607  O O   . LEU   A 99  ? 0.28425 0.20436 0.24242 -0.00616 0.00975  -0.01225 98  LEU   A O   
608  C CB  . LEU   A 99  ? 0.31007 0.22593 0.26996 -0.02107 0.00504  -0.01750 98  LEU   A CB  
609  C CG  . LEU   A 99  ? 0.29857 0.22714 0.26067 -0.02105 0.00225  -0.01798 98  LEU   A CG  
610  C CD1 . LEU   A 99  ? 0.31390 0.25350 0.28604 -0.02501 0.00052  -0.01548 98  LEU   A CD1 
611  C CD2 . LEU   A 99  ? 0.30564 0.23112 0.26054 -0.02337 -0.00053 -0.02392 98  LEU   A CD2 
612  N N   . GLY   A 100 ? 0.24629 0.18181 0.21821 -0.01045 0.00824  -0.00764 99  GLY   A N   
613  C CA  . GLY   A 100 ? 0.25185 0.19433 0.22593 -0.00559 0.00920  -0.00575 99  GLY   A CA  
614  C C   . GLY   A 100 ? 0.25830 0.21114 0.24155 -0.00697 0.00815  -0.00336 99  GLY   A C   
615  O O   . GLY   A 100 ? 0.27146 0.22682 0.25886 -0.01068 0.00661  -0.00348 99  GLY   A O   
616  N N   . VAL   A 101 ? 0.22982 0.18871 0.21694 -0.00392 0.00913  -0.00138 100 VAL   A N   
617  C CA  . VAL   A 101 ? 0.21200 0.17860 0.20803 -0.00515 0.00826  0.00065  100 VAL   A CA  
618  C C   . VAL   A 101 ? 0.23733 0.20754 0.23860 -0.00324 0.00906  0.00109  100 VAL   A C   
619  O O   . VAL   A 101 ? 0.24781 0.21917 0.24751 0.00003  0.01055  0.00142  100 VAL   A O   
620  C CB  . VAL   A 101 ? 0.22282 0.19389 0.21960 -0.00467 0.00848  0.00310  100 VAL   A CB  
621  C CG1 . VAL   A 101 ? 0.26652 0.24277 0.27327 -0.00593 0.00783  0.00567  100 VAL   A CG1 
622  C CG2 . VAL   A 101 ? 0.26090 0.23032 0.25176 -0.00616 0.00679  0.00231  100 VAL   A CG2 
623  N N   . PHE   A 102 ? 0.21585 0.18897 0.22354 -0.00492 0.00790  0.00055  101 PHE   A N   
624  C CA  . PHE   A 102 ? 0.23108 0.20928 0.24470 -0.00377 0.00775  -0.00003 101 PHE   A CA  
625  C C   . PHE   A 102 ? 0.24326 0.22574 0.26584 -0.00551 0.00722  0.00096  101 PHE   A C   
626  O O   . PHE   A 102 ? 0.21762 0.19895 0.24316 -0.00732 0.00629  0.00142  101 PHE   A O   
627  C CB  . PHE   A 102 ? 0.20306 0.18152 0.21685 -0.00408 0.00691  -0.00221 101 PHE   A CB  
628  C CG  . PHE   A 102 ? 0.22846 0.20220 0.23382 -0.00221 0.00783  -0.00188 101 PHE   A CG  
629  C CD1 . PHE   A 102 ? 0.23118 0.19829 0.23097 -0.00418 0.00855  -0.00145 101 PHE   A CD1 
630  C CD2 . PHE   A 102 ? 0.26451 0.24048 0.26801 0.00148  0.00778  -0.00171 101 PHE   A CD2 
631  C CE1 . PHE   A 102 ? 0.27491 0.23521 0.26708 -0.00296 0.00976  -0.00042 101 PHE   A CE1 
632  C CE2 . PHE   A 102 ? 0.27150 0.24135 0.26660 0.00399  0.00873  -0.00023 101 PHE   A CE2 
633  C CZ  . PHE   A 102 ? 0.28401 0.24480 0.27333 0.00156  0.00999  0.00063  101 PHE   A CZ  
634  N N   . LEU   A 103 ? 0.20937 0.19693 0.23713 -0.00497 0.00778  0.00144  102 LEU   A N   
635  C CA  . LEU   A 103 ? 0.21050 0.20089 0.24751 -0.00747 0.00783  0.00307  102 LEU   A CA  
636  C C   . LEU   A 103 ? 0.22075 0.21574 0.26589 -0.00859 0.00630  -0.00040 102 LEU   A C   
637  O O   . LEU   A 103 ? 0.22523 0.22632 0.27155 -0.00724 0.00635  -0.00140 102 LEU   A O   
638  C CB  . LEU   A 103 ? 0.21841 0.21190 0.25521 -0.00714 0.01043  0.00722  102 LEU   A CB  
639  C CG  . LEU   A 103 ? 0.23379 0.22344 0.26077 -0.00563 0.01151  0.00944  102 LEU   A CG  
640  C CD1 . LEU   A 103 ? 0.22746 0.21648 0.24566 -0.00190 0.01282  0.00773  102 LEU   A CD1 
641  C CD2 . LEU   A 103 ? 0.25368 0.24558 0.28203 -0.00668 0.01350  0.01466  102 LEU   A CD2 
642  N N   . LEU   A 104 ? 0.20489 0.19751 0.25574 -0.01064 0.00467  -0.00272 103 LEU   A N   
643  C CA  . LEU   A 104 ? 0.21644 0.21254 0.27406 -0.01186 0.00257  -0.00785 103 LEU   A CA  
644  C C   . LEU   A 104 ? 0.22754 0.22415 0.29666 -0.01582 0.00260  -0.00710 103 LEU   A C   
645  O O   . LEU   A 104 ? 0.22533 0.21581 0.29783 -0.01740 0.00341  -0.00388 103 LEU   A O   
646  C CB  . LEU   A 104 ? 0.22399 0.21670 0.28068 -0.01130 0.00108  -0.01214 103 LEU   A CB  
647  C CG  . LEU   A 104 ? 0.21356 0.20734 0.26074 -0.00851 0.00108  -0.01385 103 LEU   A CG  
648  C CD1 . LEU   A 104 ? 0.29277 0.28252 0.33251 -0.00766 0.00289  -0.00939 103 LEU   A CD1 
649  C CD2 . LEU   A 104 ? 0.24951 0.24295 0.29774 -0.00811 0.00014  -0.01886 103 LEU   A CD2 
650  N N   . LYS   A 105 ? 0.20795 0.21192 0.28357 -0.01755 0.00150  -0.00991 104 LYS   A N   
651  C CA  . LYS   A 105 ? 0.21808 0.22212 0.30626 -0.02275 0.00148  -0.00979 104 LYS   A CA  
652  C C   . LYS   A 105 ? 0.26783 0.26565 0.36160 -0.02469 -0.00123 -0.01606 104 LYS   A C   
653  O O   . LYS   A 105 ? 0.23712 0.23359 0.32500 -0.02164 -0.00297 -0.02095 104 LYS   A O   
654  C CB  . LYS   A 105 ? 0.22643 0.24256 0.32128 -0.02458 0.00117  -0.01084 104 LYS   A CB  
655  C CG  . LYS   A 105 ? 0.24153 0.26387 0.33153 -0.02171 0.00448  -0.00497 104 LYS   A CG  
656  C CD  . LYS   A 105 ? 0.27240 0.30922 0.37037 -0.02256 0.00409  -0.00634 104 LYS   A CD  
657  C CE  . LYS   A 105 ? 0.27482 0.31785 0.36923 -0.01929 0.00820  -0.00062 104 LYS   A CE  
658  N NZ  . LYS   A 105 ? 0.28589 0.32685 0.36656 -0.01186 0.00826  -0.00067 104 LYS   A NZ  
659  N N   . SER   A 106 ? 0.27955 0.27267 0.38471 -0.02976 -0.00113 -0.01571 105 SER   A N   
660  C CA  . SER   A 106 ? 0.27729 0.26226 0.38820 -0.03122 -0.00357 -0.02234 105 SER   A CA  
661  C C   . SER   A 106 ? 0.23788 0.22992 0.34772 -0.03040 -0.00731 -0.03247 105 SER   A C   
662  O O   . SER   A 106 ? 0.29002 0.29319 0.40224 -0.03202 -0.00885 -0.03477 105 SER   A O   
663  C CB  . SER   A 106 ? 0.28990 0.26814 0.41460 -0.03782 -0.00314 -0.02116 105 SER   A CB  
664  O OG  . SER   A 106 ? 0.42534 0.39924 0.55099 -0.03903 0.00062  -0.01062 105 SER   A OG  
665  N N   . GLY   A 107 ? 0.29432 0.28093 0.40081 -0.02752 -0.00881 -0.03862 106 GLY   A N   
666  C CA  . GLY   A 107 ? 0.31476 0.30756 0.41939 -0.02656 -0.01232 -0.04885 106 GLY   A CA  
667  C C   . GLY   A 107 ? 0.33832 0.34235 0.43145 -0.02220 -0.01286 -0.04886 106 GLY   A C   
668  O O   . GLY   A 107 ? 0.34624 0.35783 0.43679 -0.02120 -0.01605 -0.05646 106 GLY   A O   
669  N N   . THR   A 108 ? 0.26284 0.26760 0.34839 -0.01940 -0.01001 -0.04070 107 THR   A N   
670  C CA  . THR   A 108 ? 0.23378 0.24658 0.30842 -0.01517 -0.01016 -0.03960 107 THR   A CA  
671  C C   . THR   A 108 ? 0.26111 0.26999 0.32555 -0.01121 -0.00844 -0.03911 107 THR   A C   
672  O O   . THR   A 108 ? 0.26987 0.27112 0.33579 -0.01124 -0.00680 -0.03815 107 THR   A O   
673  C CB  . THR   A 108 ? 0.23411 0.25012 0.30676 -0.01446 -0.00806 -0.03175 107 THR   A CB  
674  O OG1 . THR   A 108 ? 0.25484 0.26252 0.32448 -0.01403 -0.00470 -0.02521 107 THR   A OG1 
675  C CG2 . THR   A 108 ? 0.29187 0.31407 0.37596 -0.01862 -0.00886 -0.03146 107 THR   A CG2 
676  N N   . SER   A 109 ? 0.27850 0.29354 0.33300 -0.00770 -0.00878 -0.03926 108 SER   A N   
677  C CA  A SER   A 109 ? 0.26567 0.27867 0.31022 -0.00464 -0.00653 -0.03769 108 SER   A CA  
678  C CA  B SER   A 109 ? 0.26558 0.27869 0.31004 -0.00460 -0.00655 -0.03776 108 SER   A CA  
679  C C   . SER   A 109 ? 0.30477 0.31982 0.33976 -0.00195 -0.00531 -0.03170 108 SER   A C   
680  O O   . SER   A 109 ? 0.28659 0.30766 0.32088 -0.00061 -0.00717 -0.03121 108 SER   A O   
681  C CB  A SER   A 109 ? 0.32513 0.34253 0.36635 -0.00285 -0.00786 -0.04541 108 SER   A CB  
682  C CB  B SER   A 109 ? 0.32494 0.34286 0.36543 -0.00265 -0.00789 -0.04523 108 SER   A CB  
683  O OG  A SER   A 109 ? 0.40386 0.42420 0.43336 0.00040  -0.00587 -0.04308 108 SER   A OG  
684  O OG  B SER   A 109 ? 0.31307 0.32715 0.36184 -0.00428 -0.00875 -0.05163 108 SER   A OG  
685  N N   . ILE   A 110 ? 0.23313 0.24300 0.26159 -0.00115 -0.00227 -0.02718 109 ILE   A N   
686  C CA  . ILE   A 110 ? 0.23879 0.24842 0.25653 0.00155  -0.00081 -0.02251 109 ILE   A CA  
687  C C   . ILE   A 110 ? 0.24366 0.25770 0.25418 0.00346  -0.00040 -0.02513 109 ILE   A C   
688  O O   . ILE   A 110 ? 0.24943 0.26232 0.26035 0.00234  0.00163  -0.02667 109 ILE   A O   
689  C CB  . ILE   A 110 ? 0.22255 0.22402 0.23723 0.00037  0.00219  -0.01690 109 ILE   A CB  
690  C CG1 . ILE   A 110 ? 0.26650 0.26483 0.28637 -0.00078 0.00203  -0.01440 109 ILE   A CG1 
691  C CG2 . ILE   A 110 ? 0.26297 0.26176 0.26668 0.00284  0.00381  -0.01228 109 ILE   A CG2 
692  C CD1 . ILE   A 110 ? 0.25463 0.24557 0.27131 -0.00217 0.00426  -0.01043 109 ILE   A CD1 
693  N N   . PRO   A 111 ? 0.26831 0.28876 0.27240 0.00670  -0.00221 -0.02572 110 PRO   A N   
694  C CA  . PRO   A 111 ? 0.27662 0.30290 0.27276 0.00884  -0.00179 -0.02844 110 PRO   A CA  
695  C C   . PRO   A 111 ? 0.26973 0.29167 0.25751 0.00877  0.00294  -0.02277 110 PRO   A C   
696  O O   . PRO   A 111 ? 0.25950 0.27371 0.24471 0.00793  0.00513  -0.01612 110 PRO   A O   
697  C CB  . PRO   A 111 ? 0.28828 0.32243 0.27839 0.01293  -0.00523 -0.02829 110 PRO   A CB  
698  C CG  . PRO   A 111 ? 0.33607 0.37139 0.33640 0.01173  -0.00835 -0.02945 110 PRO   A CG  
699  C CD  . PRO   A 111 ? 0.28379 0.30849 0.28801 0.00911  -0.00503 -0.02426 110 PRO   A CD  
700  N N   . LEU   A 112 ? 0.27957 0.30721 0.26302 0.00957  0.00461  -0.02598 111 LEU   A N   
701  C CA  . LEU   A 112 ? 0.28755 0.31430 0.26363 0.00900  0.00966  -0.02107 111 LEU   A CA  
702  C C   . LEU   A 112 ? 0.27469 0.29559 0.24113 0.01005  0.01134  -0.01178 111 LEU   A C   
703  O O   . LEU   A 112 ? 0.28000 0.30395 0.23866 0.01422  0.00918  -0.00985 111 LEU   A O   
704  C CB  . LEU   A 112 ? 0.27375 0.31099 0.24369 0.01157  0.01069  -0.02606 111 LEU   A CB  
705  C CG  . LEU   A 112 ? 0.28877 0.32825 0.25266 0.01056  0.01682  -0.02181 111 LEU   A CG  
706  C CD1 . LEU   A 112 ? 0.29719 0.33328 0.27166 0.00646  0.01958  -0.02215 111 LEU   A CD1 
707  C CD2 . LEU   A 112 ? 0.31048 0.36210 0.26770 0.01409  0.01773  -0.02795 111 LEU   A CD2 
708  N N   . HIS   A 113 ? 0.26551 0.27776 0.23258 0.00646  0.01492  -0.00615 112 HIS   A N   
709  C CA  . HIS   A 113 ? 0.31138 0.31448 0.27017 0.00698  0.01670  0.00239  112 HIS   A CA  
710  C C   . HIS   A 113 ? 0.29795 0.29502 0.25613 0.00177  0.02181  0.00718  112 HIS   A C   
711  O O   . HIS   A 113 ? 0.27513 0.27523 0.24139 -0.00220 0.02321  0.00387  112 HIS   A O   
712  C CB  . HIS   A 113 ? 0.26688 0.26192 0.22914 0.00802  0.01381  0.00355  112 HIS   A CB  
713  C CG  . HIS   A 113 ? 0.26254 0.25276 0.23466 0.00360  0.01380  0.00123  112 HIS   A CG  
714  N ND1 . HIS   A 113 ? 0.26974 0.26496 0.25167 0.00290  0.01111  -0.00478 112 HIS   A ND1 
715  C CD2 . HIS   A 113 ? 0.24431 0.22534 0.21749 -0.00037 0.01596  0.00421  112 HIS   A CD2 
716  C CE1 . HIS   A 113 ? 0.23343 0.22327 0.22122 -0.00062 0.01169  -0.00456 112 HIS   A CE1 
717  N NE2 . HIS   A 113 ? 0.25277 0.23468 0.23541 -0.00267 0.01430  0.00024  112 HIS   A NE2 
718  N N   . ASP   A 114 ? 0.29930 0.28780 0.24836 0.00180  0.02451  0.01522  113 ASP   A N   
719  C CA  . ASP   A 114 ? 0.30437 0.28657 0.25289 -0.00425 0.02955  0.02033  113 ASP   A CA  
720  C C   . ASP   A 114 ? 0.32213 0.28902 0.27254 -0.00723 0.02915  0.02305  113 ASP   A C   
721  O O   . ASP   A 114 ? 0.32223 0.28394 0.27382 -0.00394 0.02549  0.02127  113 ASP   A O   
722  C CB  . ASP   A 114 ? 0.31532 0.29814 0.25218 -0.00347 0.03407  0.02788  113 ASP   A CB  
723  C CG  . ASP   A 114 ? 0.38319 0.35597 0.30880 0.00192  0.03299  0.03503  113 ASP   A CG  
724  O OD1 . ASP   A 114 ? 0.37061 0.33537 0.29787 0.00490  0.02922  0.03414  113 ASP   A OD1 
725  O OD2 . ASP   A 114 ? 0.44601 0.41968 0.36075 0.00370  0.03630  0.04205  113 ASP   A OD2 
726  N N   . HIS   A 115 ? 0.30663 0.26736 0.25800 -0.01394 0.03312  0.02670  114 HIS   A N   
727  C CA  . HIS   A 115 ? 0.30265 0.24870 0.25588 -0.01814 0.03294  0.02800  114 HIS   A CA  
728  C C   . HIS   A 115 ? 0.31992 0.25638 0.26779 -0.02347 0.03811  0.03562  114 HIS   A C   
729  O O   . HIS   A 115 ? 0.34693 0.28402 0.30102 -0.03157 0.04071  0.03551  114 HIS   A O   
730  C CB  . HIS   A 115 ? 0.29770 0.24848 0.26258 -0.02298 0.03105  0.02158  114 HIS   A CB  
731  C CG  . HIS   A 115 ? 0.29881 0.26011 0.26977 -0.01865 0.02704  0.01513  114 HIS   A CG  
732  N ND1 . HIS   A 115 ? 0.29199 0.26730 0.26651 -0.01697 0.02727  0.01186  114 HIS   A ND1 
733  C CD2 . HIS   A 115 ? 0.31844 0.27762 0.29252 -0.01583 0.02307  0.01151  114 HIS   A CD2 
734  C CE1 . HIS   A 115 ? 0.26858 0.24826 0.24867 -0.01380 0.02338  0.00657  114 HIS   A CE1 
735  N NE2 . HIS   A 115 ? 0.26910 0.23980 0.24910 -0.01328 0.02099  0.00682  114 HIS   A NE2 
736  N N   . PRO   A 116 ? 0.33697 0.26474 0.27364 -0.01914 0.03968  0.04285  115 PRO   A N   
737  C CA  . PRO   A 116 ? 0.38341 0.30350 0.31406 -0.02403 0.04556  0.05175  115 PRO   A CA  
738  C C   . PRO   A 116 ? 0.38065 0.28536 0.31591 -0.03286 0.04721  0.05258  115 PRO   A C   
739  O O   . PRO   A 116 ? 0.41867 0.30766 0.35241 -0.03130 0.04462  0.05142  115 PRO   A O   
740  C CB  . PRO   A 116 ? 0.40989 0.32101 0.32718 -0.01559 0.04538  0.05927  115 PRO   A CB  
741  C CG  . PRO   A 116 ? 0.40562 0.32868 0.32293 -0.00674 0.03993  0.05342  115 PRO   A CG  
742  C CD  . PRO   A 116 ? 0.36428 0.29050 0.29364 -0.00932 0.03620  0.04378  115 PRO   A CD  
743  N N   . GLY   A 117 ? 0.39577 0.30581 0.33686 -0.04218 0.05163  0.05416  116 GLY   A N   
744  C CA  . GLY   A 117 ? 0.44710 0.34386 0.39342 -0.05206 0.05311  0.05459  116 GLY   A CA  
745  C C   . GLY   A 117 ? 0.42526 0.32213 0.38092 -0.05447 0.04789  0.04492  116 GLY   A C   
746  O O   . GLY   A 117 ? 0.43849 0.32146 0.39653 -0.06107 0.04750  0.04369  116 GLY   A O   
747  N N   . MET   A 118 ? 0.34754 0.25948 0.30825 -0.04951 0.04385  0.03799  117 MET   A N   
748  C CA  . MET   A 118 ? 0.35719 0.26917 0.32483 -0.05045 0.03879  0.02992  117 MET   A CA  
749  C C   . MET   A 118 ? 0.31829 0.24975 0.29779 -0.05370 0.03747  0.02440  117 MET   A C   
750  O O   . MET   A 118 ? 0.33352 0.28032 0.31569 -0.05182 0.03944  0.02489  117 MET   A O   
751  C CB  . MET   A 118 ? 0.37613 0.28472 0.33939 -0.04091 0.03424  0.02654  117 MET   A CB  
752  C CG  . MET   A 118 ? 0.39515 0.28684 0.34741 -0.03448 0.03439  0.03088  117 MET   A CG  
753  S SD  . MET   A 118 ? 0.37915 0.27856 0.32603 -0.02207 0.03180  0.03128  117 MET   A SD  
754  C CE  . MET   A 118 ? 0.37860 0.28232 0.33249 -0.02016 0.02681  0.02257  117 MET   A CE  
755  N N   . HIS   A 119 ? 0.31910 0.24960 0.30520 -0.05807 0.03396  0.01893  118 HIS   A N   
756  C CA  . HIS   A 119 ? 0.30445 0.25154 0.30108 -0.05861 0.03076  0.01312  118 HIS   A CA  
757  C C   . HIS   A 119 ? 0.31043 0.25759 0.30515 -0.05054 0.02602  0.00908  118 HIS   A C   
758  O O   . HIS   A 119 ? 0.32806 0.26209 0.31515 -0.04679 0.02457  0.00917  118 HIS   A O   
759  C CB  . HIS   A 119 ? 0.34153 0.28906 0.34591 -0.06768 0.02892  0.00966  118 HIS   A CB  
760  C CG  . HIS   A 119 ? 0.40559 0.35585 0.41510 -0.07729 0.03359  0.01320  118 HIS   A CG  
761  N ND1 . HIS   A 119 ? 0.42875 0.39857 0.45054 -0.08209 0.03461  0.01183  118 HIS   A ND1 
762  C CD2 . HIS   A 119 ? 0.40505 0.34118 0.40964 -0.08308 0.03790  0.01860  118 HIS   A CD2 
763  C CE1 . HIS   A 119 ? 0.39705 0.36617 0.42187 -0.09112 0.03962  0.01611  118 HIS   A CE1 
764  N NE2 . HIS   A 119 ? 0.50342 0.45123 0.51765 -0.09221 0.04175  0.02058  118 HIS   A NE2 
765  N N   . GLY   A 120 ? 0.29045 0.25235 0.29266 -0.04788 0.02387  0.00571  119 GLY   A N   
766  C CA  . GLY   A 120 ? 0.29682 0.25932 0.29866 -0.04151 0.01977  0.00257  119 GLY   A CA  
767  C C   . GLY   A 120 ? 0.33153 0.30673 0.34324 -0.04209 0.01672  -0.00106 119 GLY   A C   
768  O O   . GLY   A 120 ? 0.31871 0.30602 0.33834 -0.04452 0.01804  -0.00143 119 GLY   A O   
769  N N   . MET   A 121 ? 0.28046 0.25348 0.29162 -0.03941 0.01280  -0.00333 120 MET   A N   
770  C CA  A MET   A 121 ? 0.24508 0.22912 0.26435 -0.03848 0.00946  -0.00562 120 MET   A CA  
771  C CA  B MET   A 121 ? 0.24590 0.22996 0.26517 -0.03843 0.00947  -0.00561 120 MET   A CA  
772  C C   . MET   A 121 ? 0.31301 0.29500 0.33012 -0.03209 0.00729  -0.00579 120 MET   A C   
773  O O   . MET   A 121 ? 0.36109 0.33391 0.37105 -0.03069 0.00658  -0.00566 120 MET   A O   
774  C CB  A MET   A 121 ? 0.27770 0.26272 0.29897 -0.04402 0.00646  -0.00779 120 MET   A CB  
775  C CB  B MET   A 121 ? 0.27854 0.26357 0.29977 -0.04381 0.00645  -0.00777 120 MET   A CB  
776  C CG  A MET   A 121 ? 0.26776 0.26655 0.29801 -0.04291 0.00274  -0.00932 120 MET   A CG  
777  C CG  B MET   A 121 ? 0.27121 0.25556 0.29434 -0.05174 0.00865  -0.00765 120 MET   A CG  
778  S SD  A MET   A 121 ? 0.31475 0.31893 0.34817 -0.04957 -0.00189 -0.01259 120 MET   A SD  
779  S SD  B MET   A 121 ? 0.43695 0.42139 0.46154 -0.05832 0.00387  -0.01187 120 MET   A SD  
780  C CE  A MET   A 121 ? 0.33402 0.34174 0.37362 -0.05879 0.00190  -0.01259 120 MET   A CE  
781  C CE  B MET   A 121 ? 0.33512 0.34172 0.37310 -0.05741 0.00042  -0.01312 120 MET   A CE  
782  N N   . LEU   A 122 ? 0.23171 0.22198 0.25539 -0.02829 0.00656  -0.00614 121 LEU   A N   
783  C CA  A LEU   A 122 ? 0.25949 0.24746 0.28239 -0.02348 0.00481  -0.00573 121 LEU   A CA  
784  C CA  B LEU   A 122 ? 0.25969 0.24833 0.28325 -0.02314 0.00507  -0.00579 121 LEU   A CA  
785  C C   . LEU   A 122 ? 0.26881 0.26419 0.29917 -0.02158 0.00193  -0.00576 121 LEU   A C   
786  O O   . LEU   A 122 ? 0.27965 0.28385 0.31736 -0.02222 0.00145  -0.00663 121 LEU   A O   
787  C CB  A LEU   A 122 ? 0.30565 0.29211 0.32757 -0.01995 0.00670  -0.00572 121 LEU   A CB  
788  C CB  B LEU   A 122 ? 0.26509 0.25531 0.29015 -0.01986 0.00707  -0.00634 121 LEU   A CB  
789  C CG  A LEU   A 122 ? 0.25339 0.24759 0.28218 -0.01798 0.00758  -0.00750 121 LEU   A CG  
790  C CG  B LEU   A 122 ? 0.26454 0.25373 0.29157 -0.01560 0.00605  -0.00673 121 LEU   A CG  
791  C CD1 A LEU   A 122 ? 0.24694 0.24349 0.28259 -0.01462 0.00530  -0.00815 121 LEU   A CD1 
792  C CD1 B LEU   A 122 ? 0.28774 0.27657 0.31190 -0.01389 0.00791  -0.00796 121 LEU   A CD1 
793  C CD2 A LEU   A 122 ? 0.31693 0.30920 0.34118 -0.01602 0.00960  -0.00811 121 LEU   A CD2 
794  C CD2 B LEU   A 122 ? 0.30711 0.30176 0.34311 -0.01347 0.00447  -0.00771 121 LEU   A CD2 
795  N N   . LYS   A 123 ? 0.22907 0.22114 0.25726 -0.01899 0.00012  -0.00423 122 LYS   A N   
796  C CA  A LYS   A 123 ? 0.21712 0.21416 0.25063 -0.01647 -0.00272 -0.00264 122 LYS   A CA  
797  C CA  B LYS   A 123 ? 0.21605 0.21309 0.24953 -0.01647 -0.00273 -0.00264 122 LYS   A CA  
798  C C   . LYS   A 123 ? 0.24021 0.23280 0.27397 -0.01293 -0.00235 -0.00042 122 LYS   A C   
799  O O   . LYS   A 123 ? 0.24245 0.22981 0.26991 -0.01293 -0.00151 0.00074  122 LYS   A O   
800  C CB  A LYS   A 123 ? 0.26749 0.26631 0.29694 -0.01825 -0.00576 -0.00208 122 LYS   A CB  
801  C CB  B LYS   A 123 ? 0.26722 0.26602 0.29662 -0.01828 -0.00577 -0.00209 122 LYS   A CB  
802  C CG  A LYS   A 123 ? 0.29065 0.29407 0.32314 -0.01468 -0.00893 0.00107  122 LYS   A CG  
803  C CG  B LYS   A 123 ? 0.29044 0.29356 0.32249 -0.01469 -0.00892 0.00113  122 LYS   A CG  
804  C CD  A LYS   A 123 ? 0.32672 0.34026 0.36909 -0.01353 -0.01097 0.00065  122 LYS   A CD  
805  C CD  B LYS   A 123 ? 0.32804 0.34120 0.36994 -0.01341 -0.01105 0.00086  122 LYS   A CD  
806  C CE  A LYS   A 123 ? 0.33054 0.34817 0.37545 -0.00897 -0.01455 0.00477  122 LYS   A CE  
807  C CE  B LYS   A 123 ? 0.34191 0.35741 0.38744 -0.00811 -0.01372 0.00526  122 LYS   A CE  
808  N NZ  A LYS   A 123 ? 0.33944 0.34950 0.38531 -0.00496 -0.01295 0.00850  122 LYS   A NZ  
809  N NZ  B LYS   A 123 ? 0.32868 0.34609 0.36697 -0.00785 -0.01713 0.00796  122 LYS   A NZ  
810  N N   . VAL   A 124 ? 0.22848 0.22315 0.27020 -0.00996 -0.00278 0.00002  123 VAL   A N   
811  C CA  . VAL   A 124 ? 0.22052 0.21024 0.26419 -0.00777 -0.00239 0.00222  123 VAL   A CA  
812  C C   . VAL   A 124 ? 0.25837 0.24718 0.29912 -0.00686 -0.00398 0.00722  123 VAL   A C   
813  O O   . VAL   A 124 ? 0.27937 0.27260 0.32105 -0.00568 -0.00655 0.00908  123 VAL   A O   
814  C CB  . VAL   A 124 ? 0.25619 0.24613 0.30922 -0.00497 -0.00250 0.00069  123 VAL   A CB  
815  C CG1 . VAL   A 124 ? 0.25174 0.23516 0.30770 -0.00411 -0.00214 0.00297  123 VAL   A CG1 
816  C CG2 . VAL   A 124 ? 0.26578 0.25821 0.31998 -0.00545 -0.00062 -0.00472 123 VAL   A CG2 
817  N N   . LEU   A 125 ? 0.23524 0.21984 0.27234 -0.00717 -0.00243 0.00961  124 LEU   A N   
818  C CA  . LEU   A 125 ? 0.23829 0.22259 0.27112 -0.00626 -0.00286 0.01497  124 LEU   A CA  
819  C C   . LEU   A 125 ? 0.28600 0.26704 0.32529 -0.00469 -0.00238 0.01994  124 LEU   A C   
820  O O   . LEU   A 125 ? 0.31509 0.29676 0.35310 -0.00278 -0.00366 0.02555  124 LEU   A O   
821  C CB  . LEU   A 125 ? 0.27555 0.25850 0.30007 -0.00743 -0.00061 0.01485  124 LEU   A CB  
822  C CG  . LEU   A 125 ? 0.29465 0.27766 0.31176 -0.00893 -0.00088 0.01040  124 LEU   A CG  
823  C CD1 . LEU   A 125 ? 0.31833 0.29880 0.32864 -0.00856 0.00182  0.01008  124 LEU   A CD1 
824  C CD2 . LEU   A 125 ? 0.32604 0.31261 0.33859 -0.00917 -0.00393 0.01060  124 LEU   A CD2 
825  N N   . TYR   A 126 ? 0.25992 0.23722 0.30575 -0.00564 -0.00068 0.01817  125 TYR   A N   
826  C CA  . TYR   A 126 ? 0.26596 0.23809 0.31980 -0.00507 -0.00031 0.02190  125 TYR   A CA  
827  C C   . TYR   A 126 ? 0.26546 0.23472 0.32713 -0.00607 0.00007  0.01589  125 TYR   A C   
828  O O   . TYR   A 126 ? 0.24091 0.21309 0.30041 -0.00727 0.00057  0.01035  125 TYR   A O   
829  C CB  . TYR   A 126 ? 0.26830 0.23892 0.32039 -0.00674 0.00218  0.02824  125 TYR   A CB  
830  C CG  . TYR   A 126 ? 0.24113 0.21412 0.29194 -0.00953 0.00477  0.02564  125 TYR   A CG  
831  C CD1 . TYR   A 126 ? 0.24408 0.21517 0.30344 -0.01197 0.00559  0.02248  125 TYR   A CD1 
832  C CD2 . TYR   A 126 ? 0.24534 0.22295 0.28659 -0.00928 0.00612  0.02602  125 TYR   A CD2 
833  C CE1 . TYR   A 126 ? 0.24767 0.22317 0.30668 -0.01387 0.00739  0.02026  125 TYR   A CE1 
834  C CE2 . TYR   A 126 ? 0.25086 0.23139 0.29148 -0.01051 0.00843  0.02392  125 TYR   A CE2 
835  C CZ  . TYR   A 126 ? 0.25868 0.23905 0.30851 -0.01271 0.00896  0.02141  125 TYR   A CZ  
836  O OH  . TYR   A 126 ? 0.28059 0.26600 0.33027 -0.01326 0.01072  0.01940  125 TYR   A OH  
837  N N   . GLY   A 127 ? 0.27567 0.23864 0.34591 -0.00525 -0.00031 0.01697  126 GLY   A N   
838  C CA  . GLY   A 127 ? 0.26253 0.22251 0.33983 -0.00612 -0.00035 0.01008  126 GLY   A CA  
839  C C   . GLY   A 127 ? 0.25960 0.22244 0.33790 -0.00287 -0.00168 0.00398  126 GLY   A C   
840  O O   . GLY   A 127 ? 0.29518 0.26229 0.37102 -0.00012 -0.00274 0.00556  126 GLY   A O   
841  N N   . THR   A 128 ? 0.26730 0.22900 0.34974 -0.00328 -0.00161 -0.00340 127 THR   A N   
842  C CA  . THR   A 128 ? 0.26390 0.22943 0.34727 -0.00023 -0.00194 -0.01017 127 THR   A CA  
843  C C   . THR   A 128 ? 0.26675 0.23778 0.34515 -0.00231 -0.00114 -0.01607 127 THR   A C   
844  O O   . THR   A 128 ? 0.26099 0.23019 0.34062 -0.00502 -0.00130 -0.01832 127 THR   A O   
845  C CB  . THR   A 128 ? 0.32951 0.28761 0.42206 0.00274  -0.00266 -0.01437 127 THR   A CB  
846  O OG1 . THR   A 128 ? 0.36087 0.31261 0.45786 0.00547  -0.00349 -0.00758 127 THR   A OG1 
847  C CG2 . THR   A 128 ? 0.33986 0.30380 0.43305 0.00678  -0.00232 -0.02171 127 THR   A CG2 
848  N N   . VAL   A 129 ? 0.26042 0.23878 0.33366 -0.00114 -0.00033 -0.01819 128 VAL   A N   
849  C CA  . VAL   A 129 ? 0.25505 0.23833 0.32302 -0.00203 0.00057  -0.02332 128 VAL   A CA  
850  C C   . VAL   A 129 ? 0.29356 0.28182 0.36264 0.00111  0.00158  -0.02914 128 VAL   A C   
851  O O   . VAL   A 129 ? 0.29560 0.28689 0.36755 0.00344  0.00211  -0.02804 128 VAL   A O   
852  C CB  . VAL   A 129 ? 0.24008 0.22720 0.29886 -0.00413 0.00164  -0.01976 128 VAL   A CB  
853  C CG1 . VAL   A 129 ? 0.28851 0.27222 0.34559 -0.00642 0.00119  -0.01536 128 VAL   A CG1 
854  C CG2 . VAL   A 129 ? 0.25840 0.24885 0.31511 -0.00395 0.00231  -0.01663 128 VAL   A CG2 
855  N N   . ARG   A 130 ? 0.26544 0.25616 0.33215 0.00143  0.00181  -0.03554 129 ARG   A N   
856  C CA  . ARG   A 130 ? 0.24601 0.24399 0.31046 0.00429  0.00371  -0.04101 129 ARG   A CA  
857  C C   . ARG   A 130 ? 0.24878 0.25337 0.30327 0.00246  0.00570  -0.03824 129 ARG   A C   
858  O O   . ARG   A 130 ? 0.25646 0.26060 0.30512 0.00078  0.00492  -0.03768 129 ARG   A O   
859  C CB  . ARG   A 130 ? 0.26596 0.26315 0.33200 0.00611  0.00271  -0.05011 129 ARG   A CB  
860  C CG  . ARG   A 130 ? 0.30122 0.30697 0.36401 0.00988  0.00520  -0.05637 129 ARG   A CG  
861  C CD  . ARG   A 130 ? 0.38586 0.39106 0.44816 0.01151  0.00364  -0.06649 129 ARG   A CD  
862  N NE  . ARG   A 130 ? 0.42760 0.42175 0.50006 0.01187  0.00108  -0.07024 129 ARG   A NE  
863  C CZ  . ARG   A 130 ? 0.42007 0.40730 0.49583 0.00813  -0.00207 -0.07164 129 ARG   A CZ  
864  N NH1 . ARG   A 130 ? 0.38750 0.37910 0.45759 0.00450  -0.00346 -0.06996 129 ARG   A NH1 
865  N NH2 . ARG   A 130 ? 0.43964 0.41546 0.52532 0.00809  -0.00378 -0.07455 129 ARG   A NH2 
866  N N   . ILE   A 131 ? 0.23915 0.24974 0.29233 0.00267  0.00824  -0.03596 130 ILE   A N   
867  C CA  . ILE   A 131 ? 0.24983 0.26498 0.29403 0.00041  0.01070  -0.03268 130 ILE   A CA  
868  C C   . ILE   A 131 ? 0.24030 0.26470 0.28200 0.00270  0.01398  -0.03697 130 ILE   A C   
869  O O   . ILE   A 131 ? 0.27317 0.30354 0.32095 0.00461  0.01579  -0.03880 130 ILE   A O   
870  C CB  . ILE   A 131 ? 0.25118 0.26608 0.29555 -0.00279 0.01138  -0.02634 130 ILE   A CB  
871  C CG1 . ILE   A 131 ? 0.26377 0.27047 0.30927 -0.00431 0.00842  -0.02255 130 ILE   A CG1 
872  C CG2 . ILE   A 131 ? 0.27554 0.29223 0.31082 -0.00567 0.01412  -0.02288 130 ILE   A CG2 
873  C CD1 . ILE   A 131 ? 0.26991 0.27658 0.31578 -0.00703 0.00817  -0.01781 130 ILE   A CD1 
874  N N   . SER   A 132 ? 0.23933 0.26605 0.27212 0.00316  0.01471  -0.03856 131 SER   A N   
875  C CA  . SER   A 132 ? 0.25206 0.28854 0.27924 0.00522  0.01846  -0.04146 131 SER   A CA  
876  C C   . SER   A 132 ? 0.30133 0.34037 0.32076 0.00186  0.02208  -0.03392 131 SER   A C   
877  O O   . SER   A 132 ? 0.27827 0.31135 0.29087 -0.00006 0.02094  -0.02909 131 SER   A O   
878  C CB  . SER   A 132 ? 0.27538 0.31359 0.29625 0.00811  0.01668  -0.04780 131 SER   A CB  
879  O OG  . SER   A 132 ? 0.33786 0.37165 0.36686 0.01011  0.01321  -0.05515 131 SER   A OG  
880  N N   . CYS   A 133 ? 0.28085 0.32875 0.30182 0.00124  0.02668  -0.03291 132 CYS   A N   
881  C CA  . CYS   A 133 ? 0.26742 0.31681 0.28394 -0.00351 0.03054  -0.02527 132 CYS   A CA  
882  C C   . CYS   A 133 ? 0.30074 0.36034 0.30911 -0.00234 0.03594  -0.02493 132 CYS   A C   
883  O O   . CYS   A 133 ? 0.29736 0.36785 0.30918 0.00104  0.03859  -0.03042 132 CYS   A O   
884  C CB  . CYS   A 133 ? 0.28603 0.33862 0.31318 -0.00691 0.03149  -0.02320 132 CYS   A CB  
885  S SG  . CYS   A 133 ? 0.32519 0.36725 0.36008 -0.00793 0.02543  -0.02262 132 CYS   A SG  
886  N N   . MET   A 134 ? 0.27679 0.33291 0.27421 -0.00475 0.03796  -0.01810 133 MET   A N   
887  C CA  . MET   A 134 ? 0.28784 0.35245 0.27416 -0.00294 0.04273  -0.01647 133 MET   A CA  
888  C C   . MET   A 134 ? 0.29362 0.35416 0.27334 -0.00840 0.04705  -0.00588 133 MET   A C   
889  O O   . MET   A 134 ? 0.27909 0.32796 0.26087 -0.01269 0.04516  -0.00105 133 MET   A O   
890  C CB  . MET   A 134 ? 0.31824 0.38098 0.29433 0.00229  0.03889  -0.01991 133 MET   A CB  
891  C CG  . MET   A 134 ? 0.37932 0.44369 0.36232 0.00648  0.03441  -0.03055 133 MET   A CG  
892  S SD  . MET   A 134 ? 0.36552 0.43257 0.33712 0.01191  0.03029  -0.03643 133 MET   A SD  
893  C CE  . MET   A 134 ? 0.43708 0.49538 0.42126 0.01219  0.02306  -0.04408 133 MET   A CE  
894  N N   . ASP   A 135 ? 0.29454 0.36401 0.26541 -0.00805 0.05304  -0.00225 134 ASP   A N   
895  C CA  . ASP   A 135 ? 0.32417 0.38816 0.28676 -0.01289 0.05759  0.00885  134 ASP   A CA  
896  C C   . ASP   A 135 ? 0.33789 0.40795 0.28437 -0.00852 0.06089  0.01227  134 ASP   A C   
897  O O   . ASP   A 135 ? 0.37070 0.45409 0.31416 -0.00331 0.06200  0.00566  134 ASP   A O   
898  C CB  . ASP   A 135 ? 0.32719 0.39773 0.29862 -0.02032 0.06392  0.01303  134 ASP   A CB  
899  C CG  . ASP   A 135 ? 0.35310 0.41531 0.33738 -0.02600 0.06046  0.01255  134 ASP   A CG  
900  O OD1 . ASP   A 135 ? 0.33413 0.38055 0.31487 -0.02937 0.05820  0.01774  134 ASP   A OD1 
901  O OD2 . ASP   A 135 ? 0.34628 0.41798 0.34358 -0.02625 0.05979  0.00666  134 ASP   A OD2 
902  N N   . LYS   A 136 ? 0.34586 0.40574 0.28137 -0.01010 0.06231  0.02249  135 LYS   A N   
903  C CA  . LYS   A 136 ? 0.36398 0.43075 0.28346 -0.00673 0.06686  0.02841  135 LYS   A CA  
904  C C   . LYS   A 136 ? 0.43255 0.51036 0.35338 -0.01203 0.07640  0.03374  135 LYS   A C   
905  O O   . LYS   A 136 ? 0.45671 0.53166 0.38902 -0.02003 0.07948  0.03684  135 LYS   A O   
906  C CB  . LYS   A 136 ? 0.50339 0.55539 0.41012 -0.00576 0.06565  0.03898  135 LYS   A CB  
907  C CG  . LYS   A 136 ? 0.48576 0.52697 0.39251 -0.00126 0.05700  0.03541  135 LYS   A CG  
908  C CD  . LYS   A 136 ? 0.60538 0.63581 0.49753 0.00212  0.05652  0.04606  135 LYS   A CD  
909  C CE  . LYS   A 136 ? 0.58204 0.59710 0.47761 0.00368  0.05010  0.04598  135 LYS   A CE  
910  N NZ  . LYS   A 136 ? 0.56755 0.56729 0.45255 0.00425  0.05211  0.05866  135 LYS   A NZ  
911  N N   . LEU   A 137 ? 0.34038 0.63288 0.26044 -0.04628 0.02440  -0.03617 136 LEU   A N   
912  C CA  . LEU   A 137 ? 0.39779 0.69981 0.31712 -0.04666 0.02859  -0.04082 136 LEU   A CA  
913  C C   . LEU   A 137 ? 0.62647 0.92032 0.54527 -0.05514 0.03287  -0.04509 136 LEU   A C   
914  O O   . LEU   A 137 ? 0.65879 0.93126 0.57292 -0.05704 0.03173  -0.04288 136 LEU   A O   
915  C CB  . LEU   A 137 ? 0.43475 0.72877 0.34712 -0.03842 0.02659  -0.03756 136 LEU   A CB  
916  C CG  . LEU   A 137 ? 0.43858 0.74425 0.35151 -0.02975 0.02317  -0.03430 136 LEU   A CG  
917  C CD1 . LEU   A 137 ? 0.52118 0.81704 0.42646 -0.02151 0.02095  -0.03107 136 LEU   A CD1 
918  C CD2 . LEU   A 137 ? 0.54547 0.87877 0.46517 -0.03024 0.02605  -0.03891 136 LEU   A CD2 
919  N N   . ASP   A 138 ? 0.79243 1.10338 0.71608 -0.06015 0.03771  -0.05119 137 ASP   A N   
920  C CA  . ASP   A 138 ? 0.83225 1.13832 0.75587 -0.06836 0.04252  -0.05583 137 ASP   A CA  
921  C C   . ASP   A 138 ? 0.85122 1.13491 0.77155 -0.07314 0.04152  -0.05410 137 ASP   A C   
922  O O   . ASP   A 138 ? 0.90819 1.19365 0.83265 -0.07965 0.04242  -0.05632 137 ASP   A O   
923  C CB  . ASP   A 138 ? 0.75417 1.05797 0.67314 -0.06605 0.04542  -0.05702 137 ASP   A CB  
924  N N   . PRO   A 145 ? 1.10366 1.31523 1.00042 -0.08042 0.04642  -0.05317 144 PRO   A N   
925  C CA  . PRO   A 145 ? 1.10822 1.31743 1.00355 -0.07211 0.04053  -0.04774 144 PRO   A CA  
926  C C   . PRO   A 145 ? 1.02839 1.21920 0.91474 -0.06524 0.03795  -0.04387 144 PRO   A C   
927  O O   . PRO   A 145 ? 0.99990 1.17119 0.88053 -0.06721 0.03826  -0.04344 144 PRO   A O   
928  C CB  . PRO   A 145 ? 0.95495 1.15604 0.85261 -0.07485 0.03699  -0.04533 144 PRO   A CB  
929  C CG  . PRO   A 145 ? 1.04567 1.23921 0.94351 -0.08377 0.04065  -0.04906 144 PRO   A CG  
930  C CD  . PRO   A 145 ? 1.12030 1.32847 1.02061 -0.08786 0.04671  -0.05472 144 PRO   A CD  
931  N N   . ARG   A 146 ? 0.94519 1.14223 0.83012 -0.05702 0.03530  -0.04119 145 ARG   A N   
932  C CA  . ARG   A 146 ? 0.92444 1.10575 0.80073 -0.04974 0.03271  -0.03780 145 ARG   A CA  
933  C C   . ARG   A 146 ? 0.87414 1.03255 0.74605 -0.04755 0.02696  -0.03277 145 ARG   A C   
934  O O   . ARG   A 146 ? 0.72792 0.88671 0.60394 -0.04822 0.02350  -0.03024 145 ARG   A O   
935  C CB  . ARG   A 146 ? 0.83319 1.02780 0.70930 -0.04135 0.03102  -0.03622 145 ARG   A CB  
936  C CG  . ARG   A 146 ? 0.84764 1.02655 0.71467 -0.03292 0.02769  -0.03252 145 ARG   A CG  
937  C CD  . ARG   A 146 ? 0.84179 1.03619 0.70857 -0.02530 0.02735  -0.03214 145 ARG   A CD  
938  N NE  . ARG   A 146 ? 0.86923 1.07289 0.74019 -0.02140 0.02306  -0.02907 145 ARG   A NE  
939  C CZ  . ARG   A 146 ? 0.90332 1.10132 0.77002 -0.01265 0.01790  -0.02448 145 ARG   A CZ  
940  N NH1 . ARG   A 146 ? 0.84671 1.02920 0.70472 -0.00666 0.01592  -0.02241 145 ARG   A NH1 
941  N NH2 . ARG   A 146 ? 0.79059 0.99836 0.66163 -0.00972 0.01460  -0.02188 145 ARG   A NH2 
942  N N   . ALA   A 147 ? 0.79323 0.93175 0.65677 -0.04476 0.02594  -0.03130 146 ALA   A N   
943  C CA  . ALA   A 147 ? 0.69816 0.81334 0.55694 -0.04275 0.02056  -0.02694 146 ALA   A CA  
944  C C   . ALA   A 147 ? 0.59441 0.70307 0.44868 -0.03299 0.01482  -0.02204 146 ALA   A C   
945  O O   . ALA   A 147 ? 0.57727 0.69423 0.42903 -0.02724 0.01556  -0.02235 146 ALA   A O   
946  C CB  . ALA   A 147 ? 0.75988 0.85556 0.61176 -0.04560 0.02253  -0.02840 146 ALA   A CB  
947  N N   . LEU   A 148 ? 0.52959 0.62334 0.38294 -0.03118 0.00902  -0.01751 147 LEU   A N   
948  C CA  . LEU   A 148 ? 0.47407 0.55887 0.32291 -0.02224 0.00301  -0.01258 147 LEU   A CA  
949  C C   . LEU   A 148 ? 0.46519 0.53439 0.30413 -0.01733 0.00265  -0.01268 147 LEU   A C   
950  O O   . LEU   A 148 ? 0.55937 0.61258 0.39399 -0.02054 0.00361  -0.01387 147 LEU   A O   
951  C CB  . LEU   A 148 ? 0.49059 0.56131 0.34092 -0.02238 -0.00290 -0.00783 147 LEU   A CB  
952  C CG  . LEU   A 148 ? 0.44571 0.50310 0.29153 -0.01410 -0.00988 -0.00230 147 LEU   A CG  
953  C CD1 . LEU   A 148 ? 0.41467 0.48965 0.26513 -0.00957 -0.01148 -0.00001 147 LEU   A CD1 
954  C CD2 . LEU   A 148 ? 0.48927 0.52765 0.33546 -0.01618 -0.01473 0.00136  147 LEU   A CD2 
955  N N   . PRO   A 149 ? 0.46120 0.53448 0.29604 -0.00937 0.00136  -0.01156 148 PRO   A N   
956  C CA  . PRO   A 149 ? 0.47471 0.53205 0.29946 -0.00368 0.00036  -0.01122 148 PRO   A CA  
957  C C   . PRO   A 149 ? 0.44556 0.47690 0.26515 -0.00184 -0.00574 -0.00748 148 PRO   A C   
958  O O   . PRO   A 149 ? 0.42700 0.45388 0.24960 -0.00047 -0.01116 -0.00341 148 PRO   A O   
959  C CB  . PRO   A 149 ? 0.53632 0.60347 0.35872 0.00530  -0.00152 -0.00960 148 PRO   A CB  
960  C CG  . PRO   A 149 ? 0.54206 0.63236 0.37354 0.00367  -0.00038 -0.00988 148 PRO   A CG  
961  C CD  . PRO   A 149 ? 0.53252 0.62860 0.37186 -0.00606 0.00249  -0.01196 148 PRO   A CD  
962  N N   . PRO   A 150 ? 0.42877 0.44256 0.24047 -0.00134 -0.00516 -0.00862 149 PRO   A N   
963  C CA  . PRO   A 150 ? 0.41286 0.40168 0.22018 -0.00056 -0.01082 -0.00562 149 PRO   A CA  
964  C C   . PRO   A 150 ? 0.46757 0.44640 0.27221 0.00741  -0.01867 -0.00048 149 PRO   A C   
965  O O   . PRO   A 150 ? 0.44423 0.40969 0.25037 0.00645  -0.02388 0.00279  149 PRO   A O   
966  C CB  . PRO   A 150 ? 0.47210 0.44655 0.27022 0.00035  -0.00830 -0.00813 149 PRO   A CB  
967  C CG  . PRO   A 150 ? 0.64678 0.63950 0.44704 -0.00366 -0.00006 -0.01289 149 PRO   A CG  
968  C CD  . PRO   A 150 ? 0.51101 0.52723 0.31776 -0.00176 0.00082  -0.01271 149 PRO   A CD  
969  N N   . GLU   A 151 ? 0.46459 0.44890 0.26514 0.01534  -0.01979 0.00037  150 GLU   A N   
970  C CA  . GLU   A 151 ? 0.48800 0.46043 0.28474 0.02334  -0.02749 0.00518  150 GLU   A CA  
971  C C   . GLU   A 151 ? 0.50800 0.49209 0.31262 0.02372  -0.03055 0.00865  150 GLU   A C   
972  O O   . GLU   A 151 ? 0.54540 0.51887 0.34799 0.02938  -0.03726 0.01313  150 GLU   A O   
973  C CB  . GLU   A 151 ? 0.53401 0.50605 0.32220 0.03244  -0.02790 0.00488  150 GLU   A CB  
974  N N   . GLN   A 152 ? 0.50687 0.51190 0.32023 0.01801  -0.02598 0.00679  151 GLN   A N   
975  C CA  . GLN   A 152 ? 0.51614 0.53323 0.33661 0.01890  -0.02856 0.01009  151 GLN   A CA  
976  C C   . GLN   A 152 ? 0.52149 0.52326 0.34459 0.01749  -0.03460 0.01478  151 GLN   A C   
977  O O   . GLN   A 152 ? 0.46839 0.46029 0.29323 0.01125  -0.03421 0.01412  151 GLN   A O   
978  C CB  . GLN   A 152 ? 0.47729 0.51866 0.30659 0.01253  -0.02257 0.00687  151 GLN   A CB  
979  C CG  . GLN   A 152 ? 0.60611 0.66390 0.44089 0.01598  -0.02441 0.00965  151 GLN   A CG  
980  C CD  . GLN   A 152 ? 0.68561 0.75794 0.51747 0.02262  -0.02264 0.00822  151 GLN   A CD  
981  O OE1 . GLN   A 152 ? 0.79075 0.85974 0.61898 0.03053  -0.02723 0.01179  151 GLN   A OE1 
982  N NE2 . GLN   A 152 ? 0.78404 0.87287 0.61768 0.01941  -0.01602 0.00303  151 GLN   A NE2 
983  N N   . GLN   A 153 ? 0.50663 0.50687 0.33012 0.02338  -0.04011 0.01956  152 GLN   A N   
984  C CA  A GLN   A 153 ? 0.53641 0.52270 0.36254 0.02322  -0.04643 0.02479  152 GLN   A CA  
985  C CA  B GLN   A 153 ? 0.53605 0.52259 0.36240 0.02293  -0.04628 0.02471  152 GLN   A CA  
986  C C   . GLN   A 153 ? 0.55835 0.56123 0.39302 0.02253  -0.04682 0.02776  152 GLN   A C   
987  O O   . GLN   A 153 ? 0.57953 0.59986 0.41513 0.02610  -0.04480 0.02712  152 GLN   A O   
988  C CB  A GLN   A 153 ? 0.58309 0.54985 0.40106 0.03150  -0.05325 0.02824  152 GLN   A CB  
989  C CB  B GLN   A 153 ? 0.58164 0.54722 0.40022 0.03071  -0.05344 0.02843  152 GLN   A CB  
990  C CG  A GLN   A 153 ? 0.62960 0.57418 0.44750 0.03088  -0.05985 0.03238  152 GLN   A CG  
991  C CG  B GLN   A 153 ? 0.70997 0.67944 0.52127 0.03938  -0.05375 0.02779  152 GLN   A CG  
992  C CD  A GLN   A 153 ? 0.69328 0.61928 0.50234 0.03943  -0.06633 0.03495  152 GLN   A CD  
993  C CD  B GLN   A 153 ? 0.73606 0.68207 0.53818 0.04646  -0.06035 0.03026  152 GLN   A CD  
994  O OE1 A GLN   A 153 ? 0.75585 0.68391 0.55775 0.04544  -0.06529 0.03298  152 GLN   A OE1 
995  O OE1 B GLN   A 153 ? 0.75629 0.68399 0.55856 0.04541  -0.06565 0.03333  152 GLN   A OE1 
996  N NE2 A GLN   A 153 ? 0.70731 0.61491 0.51672 0.04001  -0.07304 0.03919  152 GLN   A NE2 
997  N NE2 B GLN   A 153 ? 0.77623 0.72284 0.57035 0.05384  -0.06015 0.02886  152 GLN   A NE2 
998  N N   . PHE   A 154 ? 0.52614 0.52369 0.36690 0.01818  -0.04939 0.03105  153 PHE   A N   
999  C CA  . PHE   A 154 ? 0.48498 0.49686 0.33393 0.01730  -0.04985 0.03432  153 PHE   A CA  
1000 C C   . PHE   A 154 ? 0.56154 0.55821 0.41189 0.01969  -0.05703 0.04098  153 PHE   A C   
1001 O O   . PHE   A 154 ? 0.58822 0.56375 0.43514 0.01962  -0.06115 0.04250  153 PHE   A O   
1002 C CB  . PHE   A 154 ? 0.55372 0.57857 0.41059 0.00855  -0.04479 0.03164  153 PHE   A CB  
1003 C CG  . PHE   A 154 ? 0.45843 0.50135 0.31567 0.00566  -0.03763 0.02530  153 PHE   A CG  
1004 C CD1 . PHE   A 154 ? 0.40867 0.47377 0.26894 0.00798  -0.03482 0.02415  153 PHE   A CD1 
1005 C CD2 . PHE   A 154 ? 0.54324 0.58061 0.39770 0.00070  -0.03378 0.02048  153 PHE   A CD2 
1006 C CE1 . PHE   A 154 ? 0.49453 0.57644 0.35575 0.00506  -0.02841 0.01826  153 PHE   A CE1 
1007 C CE2 . PHE   A 154 ? 0.46573 0.51952 0.32095 -0.00232 -0.02716 0.01476  153 PHE   A CE2 
1008 C CZ  . PHE   A 154 ? 0.47687 0.55297 0.33568 -0.00023 -0.02456 0.01361  153 PHE   A CZ  
1009 N N   . GLU   A 155 ? 0.62593 0.63369 0.48148 0.02185  -0.05851 0.04500  154 GLU   A N   
1010 C CA  . GLU   A 155 ? 0.66569 0.66174 0.52421 0.02338  -0.06476 0.05174  154 GLU   A CA  
1011 C C   . GLU   A 155 ? 0.64507 0.65530 0.51339 0.01859  -0.06287 0.05398  154 GLU   A C   
1012 O O   . GLU   A 155 ? 0.59826 0.62848 0.46971 0.02009  -0.05994 0.05365  154 GLU   A O   
1013 C CB  . GLU   A 155 ? 0.79550 0.78745 0.64948 0.03234  -0.06966 0.05579  154 GLU   A CB  
1014 C CG  . GLU   A 155 ? 0.84990 0.82783 0.70684 0.03368  -0.07638 0.06290  154 GLU   A CG  
1015 C CD  . GLU   A 155 ? 1.07310 1.02495 0.92481 0.03462  -0.08189 0.06407  154 GLU   A CD  
1016 O OE1 . GLU   A 155 ? 1.12767 1.06851 0.98395 0.02992  -0.08440 0.06664  154 GLU   A OE1 
1017 O OE2 . GLU   A 155 ? 1.12248 1.06499 0.96545 0.04022  -0.08376 0.06235  154 GLU   A OE2 
1018 N N   . PRO   A 156 ? 0.59422 0.59540 0.46743 0.01304  -0.06433 0.05611  155 PRO   A N   
1019 C CA  . PRO   A 156 ? 0.71149 0.69028 0.58185 0.01052  -0.06749 0.05615  155 PRO   A CA  
1020 C C   . PRO   A 156 ? 0.67421 0.65139 0.54012 0.00678  -0.06290 0.04932  155 PRO   A C   
1021 O O   . PRO   A 156 ? 0.60505 0.59942 0.47262 0.00372  -0.05677 0.04471  155 PRO   A O   
1022 C CB  . PRO   A 156 ? 0.62274 0.60028 0.50165 0.00498  -0.06867 0.05994  155 PRO   A CB  
1023 C CG  . PRO   A 156 ? 0.63883 0.64062 0.52401 0.00203  -0.06312 0.05836  155 PRO   A CG  
1024 C CD  . PRO   A 156 ? 0.64749 0.66091 0.52991 0.00893  -0.06299 0.05891  155 PRO   A CD  
1025 N N   . PRO   A 157 ? 0.66305 0.61938 0.52307 0.00720  -0.06588 0.04860  156 PRO   A N   
1026 C CA  . PRO   A 157 ? 0.58799 0.54094 0.44341 0.00364  -0.06161 0.04250  156 PRO   A CA  
1027 C C   . PRO   A 157 ? 0.54738 0.50998 0.40916 -0.00489 -0.05657 0.03968  156 PRO   A C   
1028 O O   . PRO   A 157 ? 0.58314 0.54695 0.45198 -0.00848 -0.05790 0.04290  156 PRO   A O   
1029 C CB  . PRO   A 157 ? 0.61404 0.54071 0.46370 0.00539  -0.06724 0.04396  156 PRO   A CB  
1030 C CG  . PRO   A 157 ? 0.72748 0.64842 0.58104 0.00906  -0.07399 0.05113  156 PRO   A CG  
1031 C CD  . PRO   A 157 ? 0.78556 0.72275 0.63871 0.01378  -0.07223 0.05136  156 PRO   A CD  
1032 N N   . LEU   A 158 ? 0.51894 0.48819 0.37801 -0.00806 -0.05071 0.03364  157 LEU   A N   
1033 C CA  . LEU   A 158 ? 0.46594 0.44370 0.32978 -0.01609 -0.04556 0.03005  157 LEU   A CA  
1034 C C   . LEU   A 158 ? 0.47257 0.43100 0.33350 -0.02011 -0.04658 0.02878  157 LEU   A C   
1035 O O   . LEU   A 158 ? 0.51874 0.46080 0.37197 -0.01708 -0.04866 0.02790  157 LEU   A O   
1036 C CB  . LEU   A 158 ? 0.46249 0.45713 0.32499 -0.01769 -0.03865 0.02406  157 LEU   A CB  
1037 C CG  . LEU   A 158 ? 0.49450 0.51262 0.36129 -0.01553 -0.03610 0.02389  157 LEU   A CG  
1038 C CD1 . LEU   A 158 ? 0.48655 0.52049 0.35374 -0.01970 -0.02887 0.01736  157 LEU   A CD1 
1039 C CD2 . LEU   A 158 ? 0.51871 0.54604 0.39410 -0.01752 -0.03751 0.02782  157 LEU   A CD2 
1040 N N   . GLN   A 159 ? 0.49601 0.45675 0.36277 -0.02676 -0.04494 0.02844  158 GLN   A N   
1041 C CA  . GLN   A 159 ? 0.46995 0.41498 0.33406 -0.03127 -0.04478 0.02630  158 GLN   A CA  
1042 C C   . GLN   A 159 ? 0.43537 0.38497 0.29512 -0.03466 -0.03829 0.01962  158 GLN   A C   
1043 O O   . GLN   A 159 ? 0.41263 0.38076 0.27404 -0.03542 -0.03338 0.01659  158 GLN   A O   
1044 C CB  . GLN   A 159 ? 0.52895 0.47533 0.40067 -0.03700 -0.04518 0.02823  158 GLN   A CB  
1045 C CG  . GLN   A 159 ? 0.62801 0.56645 0.50391 -0.03425 -0.05179 0.03507  158 GLN   A CG  
1046 C CD  . GLN   A 159 ? 0.71861 0.63320 0.58859 -0.03046 -0.05781 0.03722  158 GLN   A CD  
1047 O OE1 . GLN   A 159 ? 0.69783 0.59811 0.56324 -0.03271 -0.05777 0.03450  158 GLN   A OE1 
1048 N NE2 . GLN   A 159 ? 0.81125 0.72119 0.68103 -0.02447 -0.06317 0.04207  158 GLN   A NE2 
1049 N N   . PRO   A 160 ? 0.45500 0.38807 0.30926 -0.03686 -0.03807 0.01718  159 PRO   A N   
1050 C CA  . PRO   A 160 ? 0.48219 0.41868 0.33172 -0.03974 -0.03179 0.01109  159 PRO   A CA  
1051 C C   . PRO   A 160 ? 0.43437 0.39076 0.28992 -0.04620 -0.02547 0.00742  159 PRO   A C   
1052 O O   . PRO   A 160 ? 0.39686 0.36567 0.25101 -0.04680 -0.02028 0.00335  159 PRO   A O   
1053 C CB  . PRO   A 160 ? 0.46262 0.37720 0.30652 -0.04179 -0.03314 0.00988  159 PRO   A CB  
1054 C CG  . PRO   A 160 ? 0.47384 0.37200 0.31719 -0.03743 -0.04092 0.01519  159 PRO   A CG  
1055 C CD  . PRO   A 160 ? 0.47267 0.38332 0.32462 -0.03666 -0.04344 0.01976  159 PRO   A CD  
1056 N N   . ARG   A 161 ? 0.41567 0.37572 0.27800 -0.05103 -0.02576 0.00868  160 ARG   A N   
1057 C CA  . ARG   A 161 ? 0.41193 0.39039 0.27970 -0.05706 -0.02002 0.00497  160 ARG   A CA  
1058 C C   . ARG   A 161 ? 0.39067 0.39131 0.26293 -0.05459 -0.01825 0.00512  160 ARG   A C   
1059 O O   . ARG   A 161 ? 0.42754 0.44427 0.30182 -0.05801 -0.01275 0.00064  160 ARG   A O   
1060 C CB  . ARG   A 161 ? 0.51329 0.49023 0.38700 -0.06195 -0.02125 0.00672  160 ARG   A CB  
1061 C CG  . ARG   A 161 ? 0.62037 0.58171 0.49061 -0.06693 -0.02026 0.00416  160 ARG   A CG  
1062 C CD  . ARG   A 161 ? 0.48641 0.44538 0.35012 -0.06919 -0.01505 -0.00166 160 ARG   A CD  
1063 N NE  . ARG   A 161 ? 0.48139 0.42762 0.33715 -0.06363 -0.01690 -0.00132 160 ARG   A NE  
1064 C CZ  . ARG   A 161 ? 0.48440 0.42671 0.33355 -0.06420 -0.01289 -0.00557 160 ARG   A CZ  
1065 N NH1 . ARG   A 161 ? 0.49640 0.44601 0.34598 -0.07036 -0.00680 -0.01052 160 ARG   A NH1 
1066 N NH2 . ARG   A 161 ? 0.47562 0.40623 0.31745 -0.05836 -0.01505 -0.00477 160 ARG   A NH2 
1067 N N   . GLU   A 162 ? 0.39653 0.39803 0.27025 -0.04860 -0.02293 0.01017  161 GLU   A N   
1068 C CA  . GLU   A 162 ? 0.36021 0.38195 0.23742 -0.04538 -0.02158 0.01050  161 GLU   A CA  
1069 C C   . GLU   A 162 ? 0.34358 0.37007 0.21516 -0.04203 -0.01867 0.00700  161 GLU   A C   
1070 O O   . GLU   A 162 ? 0.37931 0.42537 0.25360 -0.04269 -0.01442 0.00390  161 GLU   A O   
1071 C CB  . GLU   A 162 ? 0.41455 0.43451 0.29440 -0.03980 -0.02746 0.01712  161 GLU   A CB  
1072 C CG  . GLU   A 162 ? 0.47908 0.49612 0.36532 -0.04308 -0.03006 0.02095  161 GLU   A CG  
1073 C CD  . GLU   A 162 ? 0.48185 0.49421 0.37046 -0.03781 -0.03611 0.02795  161 GLU   A CD  
1074 O OE1 . GLU   A 162 ? 0.47550 0.47559 0.35901 -0.03220 -0.04018 0.03037  161 GLU   A OE1 
1075 O OE2 . GLU   A 162 ? 0.56641 0.58680 0.46198 -0.03929 -0.03692 0.03121  161 GLU   A OE2 
1076 N N   . ARG   A 163 ? 0.36667 0.37571 0.23038 -0.03833 -0.02085 0.00732  162 ARG   A N   
1077 C CA  . ARG   A 163 ? 0.36428 0.37752 0.22234 -0.03504 -0.01782 0.00405  162 ARG   A CA  
1078 C C   . ARG   A 163 ? 0.40764 0.43183 0.26650 -0.04139 -0.01058 -0.00221 162 ARG   A C   
1079 O O   . ARG   A 163 ? 0.40720 0.44637 0.26597 -0.04027 -0.00665 -0.00523 162 ARG   A O   
1080 C CB  . ARG   A 163 ? 0.36684 0.35776 0.21582 -0.03038 -0.02132 0.00524  162 ARG   A CB  
1081 C CG  . ARG   A 163 ? 0.37413 0.35570 0.22169 -0.02306 -0.02847 0.01108  162 ARG   A CG  
1082 C CD  . ARG   A 163 ? 0.38797 0.34763 0.22597 -0.01794 -0.03209 0.01181  162 ARG   A CD  
1083 N NE  . ARG   A 163 ? 0.41474 0.37912 0.24642 -0.01392 -0.02885 0.00867  162 ARG   A NE  
1084 C CZ  . ARG   A 163 ? 0.45818 0.43070 0.28823 -0.00717 -0.03014 0.01010  162 ARG   A CZ  
1085 N NH1 . ARG   A 163 ? 0.43410 0.41104 0.26816 -0.00361 -0.03450 0.01460  162 ARG   A NH1 
1086 N NH2 . ARG   A 163 ? 0.43936 0.41620 0.26363 -0.00389 -0.02674 0.00696  162 ARG   A NH2 
1087 N N   . GLU   A 164 ? 0.38848 0.40522 0.24814 -0.04810 -0.00877 -0.00424 163 GLU   A N   
1088 C CA  . GLU   A 164 ? 0.44835 0.47475 0.30908 -0.05472 -0.00199 -0.01011 163 GLU   A CA  
1089 C C   . GLU   A 164 ? 0.43485 0.48571 0.30392 -0.05788 0.00122  -0.01198 163 GLU   A C   
1090 O O   . GLU   A 164 ? 0.41026 0.47459 0.28043 -0.06112 0.00675  -0.01682 163 GLU   A O   
1091 C CB  . GLU   A 164 ? 0.48877 0.50052 0.34819 -0.06087 -0.00131 -0.01152 163 GLU   A CB  
1092 C CG  . GLU   A 164 ? 0.62515 0.61272 0.47574 -0.05863 -0.00353 -0.01089 163 GLU   A CG  
1093 C CD  . GLU   A 164 ? 0.53963 0.52602 0.38340 -0.05734 0.00074  -0.01462 163 GLU   A CD  
1094 O OE1 . GLU   A 164 ? 0.64838 0.65226 0.49485 -0.06009 0.00625  -0.01843 163 GLU   A OE1 
1095 O OE2 . GLU   A 164 ? 0.61462 0.58266 0.45040 -0.05360 -0.00139 -0.01377 163 GLU   A OE2 
1096 N N   . ALA   A 165 ? 0.39782 0.45489 0.27283 -0.05688 -0.00216 -0.00820 164 ALA   A N   
1097 C CA  . ALA   A 165 ? 0.42751 0.50607 0.31046 -0.06040 0.00057  -0.00994 164 ALA   A CA  
1098 C C   . ALA   A 165 ? 0.35297 0.45049 0.23869 -0.05529 0.00067  -0.00929 164 ALA   A C   
1099 O O   . ALA   A 165 ? 0.39879 0.51607 0.29047 -0.05793 0.00366  -0.01181 164 ALA   A O   
1100 C CB  . ALA   A 165 ? 0.38596 0.46160 0.27405 -0.06253 -0.00265 -0.00631 164 ALA   A CB  
1101 N N   . VAL   A 166 ? 0.37734 0.46957 0.25876 -0.04787 -0.00263 -0.00612 165 VAL   A N   
1102 C CA  A VAL   A 166 ? 0.36375 0.47376 0.24774 -0.04267 -0.00286 -0.00520 165 VAL   A CA  
1103 C CA  B VAL   A 166 ? 0.36481 0.47424 0.24843 -0.04238 -0.00295 -0.00514 165 VAL   A CA  
1104 C C   . VAL   A 166 ? 0.36784 0.49459 0.25208 -0.04428 0.00298  -0.01107 165 VAL   A C   
1105 O O   . VAL   A 166 ? 0.44354 0.56391 0.32326 -0.04645 0.00620  -0.01462 165 VAL   A O   
1106 C CB  A VAL   A 166 ? 0.44567 0.54477 0.32465 -0.03409 -0.00822 -0.00015 165 VAL   A CB  
1107 C CB  B VAL   A 166 ? 0.43705 0.53463 0.31482 -0.03390 -0.00791 -0.00063 165 VAL   A CB  
1108 C CG1 A VAL   A 166 ? 0.42080 0.50978 0.29163 -0.03109 -0.00723 -0.00216 165 VAL   A CG1 
1109 C CG1 B VAL   A 166 ? 0.46381 0.54589 0.34214 -0.03221 -0.01397 0.00540  165 VAL   A CG1 
1110 C CG2 A VAL   A 166 ? 0.38334 0.49944 0.26604 -0.02868 -0.00972 0.00234  165 VAL   A CG2 
1111 C CG2 B VAL   A 166 ? 0.41933 0.50317 0.28894 -0.03259 -0.00679 -0.00285 165 VAL   A CG2 
1112 N N   . ARG   A 167 ? 0.34515 0.48570 0.23995 -0.00089 0.02193  0.00102  166 ARG   A N   
1113 C CA  . ARG   A 167 ? 0.38231 0.51754 0.27522 -0.00645 0.02776  0.00573  166 ARG   A CA  
1114 C C   . ARG   A 167 ? 0.35161 0.49065 0.25838 -0.00841 0.03128  -0.00592 166 ARG   A C   
1115 O O   . ARG   A 167 ? 0.34613 0.48231 0.26448 -0.00512 0.02888  -0.01494 166 ARG   A O   
1116 C CB  . ARG   A 167 ? 0.47850 0.59120 0.36912 -0.00682 0.02749  0.01784  166 ARG   A CB  
1117 C CG  . ARG   A 167 ? 0.55173 0.65664 0.42755 -0.00279 0.02413  0.03065  166 ARG   A CG  
1118 C CD  . ARG   A 167 ? 0.70054 0.80824 0.55912 -0.00813 0.02779  0.04055  166 ARG   A CD  
1119 N NE  . ARG   A 167 ? 0.76059 0.85834 0.60336 -0.00314 0.02452  0.05402  166 ARG   A NE  
1120 C CZ  . ARG   A 167 ? 0.81073 0.92280 0.64448 0.00218  0.02068  0.05614  166 ARG   A CZ  
1121 N NH1 . ARG   A 167 ? 0.61177 0.74818 0.45024 0.00225  0.01951  0.04476  166 ARG   A NH1 
1122 N NH2 . ARG   A 167 ? 0.71291 0.81420 0.53170 0.00785  0.01782  0.06991  166 ARG   A NH2 
1123 N N   . PRO   A 168 ? 0.38150 0.52790 0.28708 -0.01358 0.03703  -0.00570 167 PRO   A N   
1124 C CA  . PRO   A 168 ? 0.35909 0.51161 0.27791 -0.01363 0.04039  -0.01643 167 PRO   A CA  
1125 C C   . PRO   A 168 ? 0.33008 0.46651 0.26051 -0.01381 0.03980  -0.01455 167 PRO   A C   
1126 O O   . PRO   A 168 ? 0.35758 0.48034 0.28425 -0.01719 0.03949  -0.00411 167 PRO   A O   
1127 C CB  . PRO   A 168 ? 0.43659 0.60589 0.34938 -0.01932 0.04683  -0.01494 167 PRO   A CB  
1128 C CG  . PRO   A 168 ? 0.54612 0.70751 0.44473 -0.02490 0.04708  0.00017  167 PRO   A CG  
1129 C CD  . PRO   A 168 ? 0.44095 0.59189 0.33251 -0.01966 0.04085  0.00472  167 PRO   A CD  
1130 N N   . GLY   A 169 ? 0.30780 0.44510 0.25133 -0.01001 0.03969  -0.02508 168 GLY   A N   
1131 C CA  . GLY   A 169 ? 0.32291 0.44832 0.27801 -0.00969 0.03922  -0.02465 168 GLY   A CA  
1132 C C   . GLY   A 169 ? 0.34276 0.47845 0.30892 -0.00689 0.04226  -0.03467 168 GLY   A C   
1133 O O   . GLY   A 169 ? 0.34357 0.49453 0.30822 -0.00482 0.04508  -0.04243 168 GLY   A O   
1134 N N   . VAL   A 170 ? 0.32711 0.45462 0.30379 -0.00609 0.04167  -0.03440 169 VAL   A N   
1135 C CA  . VAL   A 170 ? 0.31580 0.45118 0.30376 -0.00133 0.04371  -0.04295 169 VAL   A CA  
1136 C C   . VAL   A 170 ? 0.35701 0.47556 0.35387 0.00326  0.03968  -0.04529 169 VAL   A C   
1137 O O   . VAL   A 170 ? 0.31418 0.41955 0.31201 0.00051  0.03705  -0.03823 169 VAL   A O   
1138 C CB  . VAL   A 170 ? 0.37985 0.52895 0.37207 -0.00563 0.04787  -0.03954 169 VAL   A CB  
1139 C CG1 . VAL   A 170 ? 0.37843 0.51522 0.36967 -0.01284 0.04631  -0.02911 169 VAL   A CG1 
1140 C CG2 . VAL   A 170 ? 0.32622 0.48423 0.33111 0.00173  0.04927  -0.04796 169 VAL   A CG2 
1141 N N   . LEU   A 171 ? 0.27579 0.39359 0.27782 0.01012  0.03939  -0.05524 170 LEU   A N   
1142 C CA  . LEU   A 171 ? 0.32003 0.42249 0.33021 0.01448  0.03628  -0.05767 170 LEU   A CA  
1143 C C   . LEU   A 171 ? 0.34681 0.45616 0.36655 0.01820  0.03836  -0.05845 170 LEU   A C   
1144 O O   . LEU   A 171 ? 0.36656 0.48849 0.38906 0.02374  0.04162  -0.06547 170 LEU   A O   
1145 C CB  . LEU   A 171 ? 0.33902 0.43408 0.34791 0.01907  0.03487  -0.06756 170 LEU   A CB  
1146 C CG  . LEU   A 171 ? 0.37440 0.45336 0.39067 0.02395  0.03264  -0.07115 170 LEU   A CG  
1147 C CD1 . LEU   A 171 ? 0.40295 0.46925 0.42178 0.02012  0.02899  -0.06265 170 LEU   A CD1 
1148 C CD2 . LEU   A 171 ? 0.48326 0.55310 0.49565 0.02606  0.03155  -0.08109 170 LEU   A CD2 
1149 N N   . ARG   A 172 ? 0.30906 0.41176 0.33363 0.01568  0.03647  -0.05154 171 ARG   A N   
1150 C CA  . ARG   A 172 ? 0.29612 0.40943 0.32954 0.01805  0.03798  -0.05105 171 ARG   A CA  
1151 C C   . ARG   A 172 ? 0.31807 0.42164 0.35928 0.02681  0.03581  -0.05529 171 ARG   A C   
1152 O O   . ARG   A 172 ? 0.36794 0.48299 0.41586 0.03395  0.03765  -0.05932 171 ARG   A O   
1153 C CB  . ARG   A 172 ? 0.29400 0.40715 0.32733 0.00962  0.03725  -0.04173 171 ARG   A CB  
1154 C CG  . ARG   A 172 ? 0.32562 0.44715 0.35005 0.00062  0.03999  -0.03661 171 ARG   A CG  
1155 C CD  . ARG   A 172 ? 0.37683 0.50064 0.40168 -0.00806 0.04035  -0.02922 171 ARG   A CD  
1156 N NE  . ARG   A 172 ? 0.32452 0.45234 0.33922 -0.01784 0.04311  -0.02323 171 ARG   A NE  
1157 C CZ  . ARG   A 172 ? 0.40432 0.55340 0.41826 -0.02246 0.04761  -0.02335 171 ARG   A CZ  
1158 N NH1 . ARG   A 172 ? 0.43515 0.60600 0.45858 -0.01683 0.05008  -0.03000 171 ARG   A NH1 
1159 N NH2 . ARG   A 172 ? 0.40028 0.54878 0.40313 -0.03267 0.04991  -0.01636 171 ARG   A NH2 
1160 N N   . SER   A 173 ? 0.31669 0.39985 0.35677 0.02690  0.03208  -0.05426 172 SER   A N   
1161 C CA  . SER   A 173 ? 0.32062 0.39217 0.36651 0.03421  0.03005  -0.05677 172 SER   A CA  
1162 C C   . SER   A 173 ? 0.34321 0.39374 0.38531 0.03255  0.02689  -0.05732 172 SER   A C   
1163 O O   . SER   A 173 ? 0.31336 0.36001 0.35029 0.02595  0.02561  -0.05407 172 SER   A O   
1164 C CB  . SER   A 173 ? 0.30663 0.38143 0.35939 0.03420  0.02858  -0.05051 172 SER   A CB  
1165 O OG  . SER   A 173 ? 0.34314 0.40807 0.39320 0.02654  0.02605  -0.04343 172 SER   A OG  
1166 N N   . ARG   A 174 ? 0.32478 0.36227 0.36921 0.03893  0.02576  -0.06138 173 ARG   A N   
1167 C CA  . ARG   A 174 ? 0.31623 0.33396 0.35753 0.03650  0.02304  -0.06220 173 ARG   A CA  
1168 C C   . ARG   A 174 ? 0.46103 0.46551 0.50631 0.04345  0.02184  -0.06222 173 ARG   A C   
1169 O O   . ARG   A 174 ? 0.47392 0.47521 0.51948 0.05179  0.02338  -0.06856 173 ARG   A O   
1170 C CB  . ARG   A 174 ? 0.37950 0.39388 0.41431 0.03520  0.02379  -0.07046 173 ARG   A CB  
1171 C CG  . ARG   A 174 ? 0.39653 0.39188 0.42834 0.03179  0.02125  -0.07274 173 ARG   A CG  
1172 C CD  . ARG   A 174 ? 0.54549 0.54102 0.57027 0.02893  0.02180  -0.08164 173 ARG   A CD  
1173 N NE  . ARG   A 174 ? 0.60775 0.58388 0.62968 0.03133  0.02167  -0.08943 173 ARG   A NE  
1174 C CZ  . ARG   A 174 ? 0.66508 0.62757 0.68315 0.02436  0.01946  -0.09199 173 ARG   A CZ  
1175 N NH1 . ARG   A 174 ? 0.74848 0.71815 0.76591 0.01568  0.01716  -0.08814 173 ARG   A NH1 
1176 N NH2 . ARG   A 174 ? 0.71450 0.65568 0.72903 0.02615  0.01964  -0.09841 173 ARG   A NH2 
1177 N N   . ALA   A 175 ? 0.33452 0.33228 0.38228 0.04094  0.01932  -0.05484 174 ALA   A N   
1178 C CA  . ALA   A 175 ? 0.28624 0.27219 0.33687 0.04725  0.01781  -0.05278 174 ALA   A CA  
1179 C C   . ALA   A 175 ? 0.33462 0.30596 0.38350 0.04107  0.01507  -0.04717 174 ALA   A C   
1180 O O   . ALA   A 175 ? 0.32527 0.29940 0.37241 0.03304  0.01440  -0.04428 174 ALA   A O   
1181 C CB  . ALA   A 175 ? 0.33161 0.33299 0.38886 0.05271  0.01789  -0.04850 174 ALA   A CB  
1182 N N   . GLU   A 176 ? 0.32223 0.27813 0.37105 0.04554  0.01367  -0.04542 175 GLU   A N   
1183 C CA  . GLU   A 176 ? 0.31765 0.26069 0.36469 0.03997  0.01144  -0.03948 175 GLU   A CA  
1184 C C   . GLU   A 176 ? 0.35532 0.30566 0.40617 0.04183  0.00981  -0.03154 175 GLU   A C   
1185 O O   . GLU   A 176 ? 0.33237 0.28949 0.38686 0.05012  0.00962  -0.03063 175 GLU   A O   
1186 C CB  . GLU   A 176 ? 0.35076 0.26991 0.39327 0.04200  0.01093  -0.04149 175 GLU   A CB  
1187 C CG  . GLU   A 176 ? 0.37686 0.28720 0.41434 0.03780  0.01217  -0.04998 175 GLU   A CG  
1188 C CD  . GLU   A 176 ? 0.50340 0.38659 0.53465 0.03705  0.01174  -0.05193 175 GLU   A CD  
1189 O OE1 . GLU   A 176 ? 0.51000 0.38042 0.54056 0.04134  0.01060  -0.04596 175 GLU   A OE1 
1190 O OE2 . GLU   A 176 ? 0.62962 0.50382 0.65576 0.03186  0.01250  -0.05945 175 GLU   A OE2 
1191 N N   . TYR   A 177 ? 0.27917 0.22899 0.32896 0.03448  0.00858  -0.02618 176 TYR   A N   
1192 C CA  . TYR   A 177 ? 0.28663 0.24337 0.33846 0.03440  0.00698  -0.01931 176 TYR   A CA  
1193 C C   . TYR   A 177 ? 0.35070 0.29449 0.39919 0.03041  0.00549  -0.01411 176 TYR   A C   
1194 O O   . TYR   A 177 ? 0.30432 0.24041 0.34987 0.02414  0.00602  -0.01518 176 TYR   A O   
1195 C CB  . TYR   A 177 ? 0.31198 0.28400 0.36465 0.02886  0.00763  -0.01822 176 TYR   A CB  
1196 C CG  . TYR   A 177 ? 0.29656 0.28259 0.35157 0.03075  0.00955  -0.02247 176 TYR   A CG  
1197 C CD1 . TYR   A 177 ? 0.29312 0.27979 0.34583 0.02859  0.01139  -0.02743 176 TYR   A CD1 
1198 C CD2 . TYR   A 177 ? 0.35115 0.35198 0.41052 0.03424  0.00951  -0.02135 176 TYR   A CD2 
1199 C CE1 . TYR   A 177 ? 0.33782 0.33835 0.39169 0.02981  0.01352  -0.03082 176 TYR   A CE1 
1200 C CE2 . TYR   A 177 ? 0.31780 0.33370 0.37932 0.03493  0.01176  -0.02492 176 TYR   A CE2 
1201 C CZ  . TYR   A 177 ? 0.36537 0.38043 0.42376 0.03275  0.01394  -0.02945 176 TYR   A CZ  
1202 O OH  . TYR   A 177 ? 0.33874 0.36967 0.39837 0.03300  0.01654  -0.03253 176 TYR   A OH  
1203 N N   . THR   A 178 ? 0.30632 0.24982 0.35522 0.03390  0.00362  -0.00837 177 THR   A N   
1204 C CA  . THR   A 178 ? 0.30423 0.23820 0.34932 0.03012  0.00232  -0.00225 177 THR   A CA  
1205 C C   . THR   A 178 ? 0.28461 0.23156 0.33042 0.02879  0.00088  0.00262  177 THR   A C   
1206 O O   . THR   A 178 ? 0.33930 0.30118 0.38841 0.02968  0.00084  0.00114  177 THR   A O   
1207 C CB  . THR   A 178 ? 0.36051 0.27738 0.40258 0.03596  0.00114  0.00078  177 THR   A CB  
1208 O OG1 . THR   A 178 ? 0.39999 0.32477 0.44492 0.04557  -0.00074 0.00364  177 THR   A OG1 
1209 C CG2 . THR   A 178 ? 0.38802 0.28977 0.42811 0.03757  0.00266  -0.00542 177 THR   A CG2 
1210 N N   . GLU   A 179 ? 0.34261 0.28382 0.38447 0.02572  -0.00017 0.00829  178 GLU   A N   
1211 C CA  . GLU   A 179 ? 0.37408 0.32664 0.41509 0.02423  -0.00169 0.01233  178 GLU   A CA  
1212 C C   . GLU   A 179 ? 0.46413 0.42721 0.50843 0.03160  -0.00414 0.01419  178 GLU   A C   
1213 O O   . GLU   A 179 ? 0.43686 0.41405 0.48169 0.02955  -0.00541 0.01529  178 GLU   A O   
1214 C CB  . GLU   A 179 ? 0.41743 0.36247 0.45275 0.02026  -0.00219 0.01814  178 GLU   A CB  
1215 C CG  . GLU   A 179 ? 0.48563 0.41665 0.51785 0.02476  -0.00362 0.02340  178 GLU   A CG  
1216 C CD  . GLU   A 179 ? 0.54262 0.48076 0.57476 0.03199  -0.00692 0.02864  178 GLU   A CD  
1217 O OE1 . GLU   A 179 ? 0.71858 0.67293 0.75168 0.03043  -0.00818 0.02900  178 GLU   A OE1 
1218 O OE2 . GLU   A 179 ? 0.67952 0.60688 0.71015 0.03946  -0.00840 0.03226  178 GLU   A OE2 
1219 N N   . ALA   A 180 ? 0.36988 0.32708 0.41619 0.04030  -0.00483 0.01414  179 ALA   A N   
1220 C CA  . ALA   A 180 ? 0.37979 0.35051 0.43045 0.04910  -0.00719 0.01577  179 ALA   A CA  
1221 C C   . ALA   A 180 ? 0.39198 0.38055 0.44935 0.05016  -0.00586 0.00981  179 ALA   A C   
1222 O O   . ALA   A 180 ? 0.44310 0.44911 0.50540 0.05593  -0.00763 0.01065  179 ALA   A O   
1223 C CB  . ALA   A 180 ? 0.46148 0.41802 0.51089 0.06016  -0.00832 0.01835  179 ALA   A CB  
1224 N N   . SER   A 181 ? 0.40118 0.38750 0.45874 0.04476  -0.00285 0.00419  180 SER   A N   
1225 C CA  . SER   A 181 ? 0.31588 0.31879 0.37833 0.04419  -0.00113 -0.00076 180 SER   A CA  
1226 C C   . SER   A 181 ? 0.31563 0.33265 0.37766 0.03546  -0.00156 0.00044  180 SER   A C   
1227 O O   . SER   A 181 ? 0.44690 0.45786 0.50399 0.02924  -0.00231 0.00326  180 SER   A O   
1228 C CB  . SER   A 181 ? 0.36568 0.36054 0.42680 0.04138  0.00203  -0.00653 180 SER   A CB  
1229 O OG  . SER   A 181 ? 0.36696 0.34458 0.42620 0.04677  0.00248  -0.00841 180 SER   A OG  
1230 N N   . GLY   A 182 ? 0.38021 0.41572 0.44672 0.03453  -0.00074 -0.00211 181 GLY   A N   
1231 C CA  . GLY   A 182 ? 0.42592 0.47142 0.49041 0.02452  -0.00069 -0.00174 181 GLY   A CA  
1232 C C   . GLY   A 182 ? 0.43922 0.47208 0.49777 0.01700  0.00195  -0.00368 181 GLY   A C   
1233 O O   . GLY   A 182 ? 0.38323 0.40455 0.44075 0.01935  0.00357  -0.00569 181 GLY   A O   
1234 N N   . PRO   A 183 ? 0.28011 0.31457 0.33400 0.00808  0.00227  -0.00322 182 PRO   A N   
1235 C CA  . PRO   A 183 ? 0.30391 0.32838 0.35205 0.00242  0.00494  -0.00486 182 PRO   A CA  
1236 C C   . PRO   A 183 ? 0.31877 0.35009 0.36929 0.00271  0.00751  -0.00781 182 PRO   A C   
1237 O O   . PRO   A 183 ? 0.31365 0.36131 0.36977 0.00419  0.00779  -0.00900 182 PRO   A O   
1238 C CB  . PRO   A 183 ? 0.30842 0.33345 0.35046 -0.00651 0.00472  -0.00399 182 PRO   A CB  
1239 C CG  . PRO   A 183 ? 0.43040 0.47105 0.47645 -0.00701 0.00209  -0.00289 182 PRO   A CG  
1240 C CD  . PRO   A 183 ? 0.29671 0.33975 0.34883 0.00297  0.00001  -0.00119 182 PRO   A CD  
1241 N N   . CYS   A 184 ? 0.25953 0.28016 0.30562 0.00156  0.00942  -0.00891 183 CYS   A N   
1242 C CA  . CYS   A 184 ? 0.27006 0.29568 0.31563 0.00053  0.01202  -0.01119 183 CYS   A CA  
1243 C C   . CYS   A 184 ? 0.30831 0.32995 0.34597 -0.00777 0.01355  -0.00945 183 CYS   A C   
1244 O O   . CYS   A 184 ? 0.34016 0.34849 0.37157 -0.00985 0.01310  -0.00770 183 CYS   A O   
1245 C CB  . CYS   A 184 ? 0.28976 0.30680 0.33466 0.00500  0.01272  -0.01346 183 CYS   A CB  
1246 S SG  . CYS   A 184 ? 0.40516 0.42197 0.45687 0.01411  0.01155  -0.01619 183 CYS   A SG  
1247 N N   . ILE   A 185 ? 0.26723 0.29989 0.30454 -0.01226 0.01561  -0.00986 184 ILE   A N   
1248 C CA  . ILE   A 185 ? 0.27980 0.30740 0.30827 -0.02137 0.01733  -0.00760 184 ILE   A CA  
1249 C C   . ILE   A 185 ? 0.31815 0.34531 0.34253 -0.02136 0.01993  -0.00759 184 ILE   A C   
1250 O O   . ILE   A 185 ? 0.34245 0.38230 0.37229 -0.01744 0.02109  -0.01023 184 ILE   A O   
1251 C CB  . ILE   A 185 ? 0.31099 0.35333 0.34112 -0.02959 0.01774  -0.00726 184 ILE   A CB  
1252 C CG1 . ILE   A 185 ? 0.46780 0.51321 0.50135 -0.02992 0.01466  -0.00722 184 ILE   A CG1 
1253 C CG2 . ILE   A 185 ? 0.42087 0.45401 0.43976 -0.04067 0.01989  -0.00479 184 ILE   A CG2 
1254 C CD1 . ILE   A 185 ? 0.47968 0.50656 0.50838 -0.02715 0.01291  -0.00630 184 ILE   A CD1 
1255 N N   . LEU   A 186 ? 0.29729 0.31004 0.31121 -0.02527 0.02091  -0.00465 185 LEU   A N   
1256 C CA  . LEU   A 186 ? 0.28495 0.29839 0.29270 -0.02731 0.02340  -0.00310 185 LEU   A CA  
1257 C C   . LEU   A 186 ? 0.32758 0.33055 0.32389 -0.03715 0.02508  0.00114  185 LEU   A C   
1258 O O   . LEU   A 186 ? 0.30520 0.29609 0.29711 -0.04088 0.02409  0.00212  185 LEU   A O   
1259 C CB  . LEU   A 186 ? 0.29954 0.30422 0.30433 -0.02007 0.02268  -0.00307 185 LEU   A CB  
1260 C CG  . LEU   A 186 ? 0.29629 0.28261 0.29438 -0.01786 0.02124  -0.00049 185 LEU   A CG  
1261 C CD1 . LEU   A 186 ? 0.31753 0.29040 0.30209 -0.02189 0.02285  0.00455  185 LEU   A CD1 
1262 C CD2 . LEU   A 186 ? 0.33713 0.32366 0.33909 -0.00977 0.01954  -0.00256 185 LEU   A CD2 
1263 N N   . THR   A 187 ? 0.30909 0.31615 0.29959 -0.04197 0.02783  0.00348  186 THR   A N   
1264 C CA  . THR   A 187 ? 0.29418 0.28955 0.27201 -0.05260 0.02995  0.00820  186 THR   A CA  
1265 C C   . THR   A 187 ? 0.32051 0.30625 0.28735 -0.05098 0.03153  0.01268  186 THR   A C   
1266 O O   . THR   A 187 ? 0.33537 0.32805 0.30565 -0.04263 0.03095  0.01132  186 THR   A O   
1267 C CB  . THR   A 187 ? 0.36862 0.38259 0.34959 -0.06374 0.03226  0.00781  186 THR   A CB  
1268 O OG1 . THR   A 187 ? 0.36546 0.39633 0.34824 -0.06319 0.03493  0.00792  186 THR   A OG1 
1269 C CG2 . THR   A 187 ? 0.36142 0.39292 0.35613 -0.06244 0.03019  0.00311  186 THR   A CG2 
1270 N N   . PRO   A 188 ? 0.35950 0.32860 0.31187 -0.05923 0.03345  0.01823  187 PRO   A N   
1271 C CA  . PRO   A 188 ? 0.37191 0.33117 0.31230 -0.05688 0.03469  0.02385  187 PRO   A CA  
1272 C C   . PRO   A 188 ? 0.38543 0.36720 0.32947 -0.05736 0.03675  0.02343  187 PRO   A C   
1273 O O   . PRO   A 188 ? 0.42138 0.40199 0.35999 -0.05116 0.03654  0.02594  187 PRO   A O   
1274 C CB  . PRO   A 188 ? 0.42856 0.36512 0.35224 -0.06787 0.03686  0.02997  187 PRO   A CB  
1275 C CG  . PRO   A 188 ? 0.42992 0.35606 0.35552 -0.07104 0.03540  0.02655  187 PRO   A CG  
1276 C CD  . PRO   A 188 ? 0.40037 0.35391 0.34465 -0.06982 0.03404  0.01975  187 PRO   A CD  
1277 N N   . HIS   A 189 ? 0.37896 0.38340 0.33246 -0.06360 0.03863  0.01981  188 HIS   A N   
1278 C CA  . HIS   A 189 ? 0.41214 0.43890 0.36755 -0.06526 0.04163  0.01925  188 HIS   A CA  
1279 C C   . HIS   A 189 ? 0.35484 0.40623 0.32667 -0.05728 0.04105  0.01108  188 HIS   A C   
1280 O O   . HIS   A 189 ? 0.39551 0.46735 0.36972 -0.05757 0.04388  0.00910  188 HIS   A O   
1281 C CB  . HIS   A 189 ? 0.46753 0.50194 0.41742 -0.08064 0.04567  0.02292  188 HIS   A CB  
1282 C CG  . HIS   A 189 ? 0.51604 0.52249 0.44753 -0.08968 0.04669  0.03116  188 HIS   A CG  
1283 N ND1 . HIS   A 189 ? 0.69674 0.69089 0.61319 -0.08946 0.04814  0.03828  188 HIS   A ND1 
1284 C CD2 . HIS   A 189 ? 0.61164 0.59856 0.53598 -0.09907 0.04649  0.03337  188 HIS   A CD2 
1285 C CE1 . HIS   A 189 ? 0.75776 0.72376 0.65835 -0.09740 0.04884  0.04501  188 HIS   A CE1 
1286 N NE2 . HIS   A 189 ? 0.78665 0.74720 0.69147 -0.10382 0.04802  0.04165  188 HIS   A NE2 
1287 N N   . ARG   A 190 ? 0.33516 0.38437 0.31728 -0.04992 0.03774  0.00636  189 ARG   A N   
1288 C CA  . ARG   A 190 ? 0.34670 0.41518 0.34266 -0.04171 0.03723  -0.00093 189 ARG   A CA  
1289 C C   . ARG   A 190 ? 0.32108 0.37801 0.32272 -0.03183 0.03323  -0.00416 189 ARG   A C   
1290 O O   . ARG   A 190 ? 0.30849 0.35135 0.30957 -0.03273 0.03093  -0.00239 189 ARG   A O   
1291 C CB  . ARG   A 190 ? 0.35986 0.44838 0.36582 -0.04611 0.03846  -0.00349 189 ARG   A CB  
1292 C CG  . ARG   A 190 ? 0.38871 0.49951 0.40629 -0.03733 0.03941  -0.01033 189 ARG   A CG  
1293 C CD  . ARG   A 190 ? 0.44979 0.58256 0.47797 -0.03996 0.04017  -0.01234 189 ARG   A CD  
1294 N NE  . ARG   A 190 ? 0.38424 0.53758 0.42314 -0.02943 0.04130  -0.01901 189 ARG   A NE  
1295 C CZ  . ARG   A 190 ? 0.45185 0.62769 0.49213 -0.02976 0.04561  -0.02153 189 ARG   A CZ  
1296 N NH1 . ARG   A 190 ? 0.42280 0.60446 0.45434 -0.04115 0.04923  -0.01719 189 ARG   A NH1 
1297 N NH2 . ARG   A 190 ? 0.48245 0.67468 0.53222 -0.01819 0.04656  -0.02846 189 ARG   A NH2 
1298 N N   . ASP   A 191 ? 0.30238 0.36572 0.30891 -0.02319 0.03268  -0.00928 190 ASP   A N   
1299 C CA  . ASP   A 191 ? 0.25726 0.31001 0.26798 -0.01509 0.02928  -0.01230 190 ASP   A CA  
1300 C C   . ASP   A 191 ? 0.26128 0.29487 0.26367 -0.01538 0.02722  -0.00752 190 ASP   A C   
1301 O O   . ASP   A 191 ? 0.28552 0.30903 0.29104 -0.01165 0.02456  -0.00813 190 ASP   A O   
1302 C CB  . ASP   A 191 ? 0.27658 0.33087 0.29758 -0.01221 0.02749  -0.01492 190 ASP   A CB  
1303 C CG  . ASP   A 191 ? 0.34883 0.42261 0.37874 -0.00897 0.02920  -0.01977 190 ASP   A CG  
1304 O OD1 . ASP   A 191 ? 0.30757 0.38836 0.33867 -0.00366 0.03051  -0.02466 190 ASP   A OD1 
1305 O OD2 . ASP   A 191 ? 0.35071 0.43377 0.38623 -0.01134 0.02921  -0.01906 190 ASP   A OD2 
1306 N N   . ASN   A 192 ? 0.26104 0.28995 0.25234 -0.01914 0.02859  -0.00246 191 ASN   A N   
1307 C CA  . ASN   A 192 ? 0.24678 0.25724 0.22921 -0.01809 0.02688  0.00275  191 ASN   A CA  
1308 C C   . ASN   A 192 ? 0.27520 0.28402 0.25876 -0.01014 0.02420  0.00078  191 ASN   A C   
1309 O O   . ASN   A 192 ? 0.29580 0.29209 0.27532 -0.00707 0.02237  0.00389  191 ASN   A O   
1310 C CB  . ASN   A 192 ? 0.28775 0.29130 0.25633 -0.02367 0.02904  0.00977  191 ASN   A CB  
1311 C CG  . ASN   A 192 ? 0.29801 0.27932 0.25651 -0.02199 0.02765  0.01548  191 ASN   A CG  
1312 O OD1 . ASN   A 192 ? 0.33549 0.31147 0.28709 -0.01632 0.02639  0.01869  191 ASN   A OD1 
1313 N ND2 . ASN   A 192 ? 0.30293 0.27191 0.26024 -0.02634 0.02780  0.01642  191 ASN   A ND2 
1314 N N   . LEU   A 193 ? 0.26695 0.28869 0.25504 -0.00700 0.02407  -0.00451 192 LEU   A N   
1315 C CA  . LEU   A 193 ? 0.24994 0.27229 0.24010 -0.00135 0.02133  -0.00764 192 LEU   A CA  
1316 C C   . LEU   A 193 ? 0.24623 0.27027 0.24760 0.00096  0.02022  -0.01420 192 LEU   A C   
1317 O O   . LEU   A 193 ? 0.29047 0.32208 0.29723 0.00067  0.02181  -0.01850 192 LEU   A O   
1318 C CB  . LEU   A 193 ? 0.27654 0.31062 0.26185 -0.00044 0.02177  -0.00967 192 LEU   A CB  
1319 C CG  . LEU   A 193 ? 0.31248 0.34374 0.28550 -0.00020 0.02137  -0.00242 192 LEU   A CG  
1320 C CD1 . LEU   A 193 ? 0.36400 0.38848 0.32911 -0.00578 0.02431  0.00450  192 LEU   A CD1 
1321 C CD2 . LEU   A 193 ? 0.32144 0.36704 0.29004 0.00097  0.02117  -0.00535 192 LEU   A CD2 
1322 N N   . HIS   A 194 ? 0.24839 0.26555 0.25293 0.00358  0.01768  -0.01463 193 HIS   A N   
1323 C CA  . HIS   A 194 ? 0.24665 0.26388 0.25999 0.00523  0.01670  -0.02037 193 HIS   A CA  
1324 C C   . HIS   A 194 ? 0.24978 0.26554 0.26439 0.00677  0.01417  -0.02233 193 HIS   A C   
1325 O O   . HIS   A 194 ? 0.25367 0.26858 0.26430 0.00770  0.01287  -0.01850 193 HIS   A O   
1326 C CB  . HIS   A 194 ? 0.27350 0.28464 0.29227 0.00465  0.01677  -0.01906 193 HIS   A CB  
1327 C CG  . HIS   A 194 ? 0.25119 0.25260 0.26795 0.00407  0.01565  -0.01420 193 HIS   A CG  
1328 N ND1 . HIS   A 194 ? 0.26992 0.26669 0.28913 0.00260  0.01568  -0.01247 193 HIS   A ND1 
1329 C CD2 . HIS   A 194 ? 0.26361 0.26024 0.27590 0.00544  0.01458  -0.01113 193 HIS   A CD2 
1330 C CE1 . HIS   A 194 ? 0.28258 0.27079 0.29818 0.00265  0.01498  -0.00910 193 HIS   A CE1 
1331 N NE2 . HIS   A 194 ? 0.25857 0.24652 0.27025 0.00498  0.01443  -0.00817 193 HIS   A NE2 
1332 N N   . GLN   A 195 ? 0.27026 0.28646 0.28995 0.00710  0.01361  -0.02861 194 GLN   A N   
1333 C CA  . GLN   A 195 ? 0.25641 0.27107 0.27841 0.00629  0.01142  -0.03146 194 GLN   A CA  
1334 C C   . GLN   A 195 ? 0.24875 0.25384 0.27665 0.00609  0.01122  -0.03245 194 GLN   A C   
1335 O O   . GLN   A 195 ? 0.27766 0.27984 0.30803 0.00779  0.01245  -0.03452 194 GLN   A O   
1336 C CB  . GLN   A 195 ? 0.27151 0.29252 0.29174 0.00525  0.01102  -0.03865 194 GLN   A CB  
1337 C CG  . GLN   A 195 ? 0.28081 0.30012 0.30338 0.00214  0.00889  -0.04273 194 GLN   A CG  
1338 C CD  . GLN   A 195 ? 0.42067 0.44686 0.43970 -0.00012 0.00823  -0.05049 194 GLN   A CD  
1339 O OE1 . GLN   A 195 ? 0.45068 0.48701 0.46452 0.00096  0.00854  -0.05081 194 GLN   A OE1 
1340 N NE2 . GLN   A 195 ? 0.40817 0.42806 0.42883 -0.00397 0.00735  -0.05679 194 GLN   A NE2 
1341 N N   . ILE   A 196 ? 0.22367 0.22518 0.25365 0.00443  0.00974  -0.03070 195 ILE   A N   
1342 C CA  . ILE   A 196 ? 0.23419 0.22617 0.26829 0.00379  0.00956  -0.02998 195 ILE   A CA  
1343 C C   . ILE   A 196 ? 0.25728 0.24683 0.29279 -0.00029 0.00831  -0.03340 195 ILE   A C   
1344 O O   . ILE   A 196 ? 0.25837 0.25479 0.29384 -0.00272 0.00725  -0.03214 195 ILE   A O   
1345 C CB  . ILE   A 196 ? 0.25226 0.24185 0.28657 0.00440  0.00962  -0.02362 195 ILE   A CB  
1346 C CG1 . ILE   A 196 ? 0.29026 0.28127 0.32198 0.00626  0.01086  -0.02081 195 ILE   A CG1 
1347 C CG2 . ILE   A 196 ? 0.24718 0.22819 0.28475 0.00369  0.00933  -0.02233 195 ILE   A CG2 
1348 C CD1 . ILE   A 196 ? 0.30547 0.29444 0.33382 0.00649  0.01102  -0.01568 195 ILE   A CD1 
1349 N N   . ASP   A 197 ? 0.23834 0.21835 0.27468 -0.00103 0.00851  -0.03774 196 ASP   A N   
1350 C CA  . ASP   A 197 ? 0.26369 0.23803 0.29981 -0.00679 0.00759  -0.04169 196 ASP   A CA  
1351 C C   . ASP   A 197 ? 0.31085 0.27186 0.34854 -0.00813 0.00766  -0.03824 196 ASP   A C   
1352 O O   . ASP   A 197 ? 0.28999 0.24183 0.32806 -0.00332 0.00828  -0.03699 196 ASP   A O   
1353 C CB  . ASP   A 197 ? 0.29381 0.26273 0.32696 -0.00730 0.00793  -0.05016 196 ASP   A CB  
1354 C CG  . ASP   A 197 ? 0.32934 0.31123 0.35976 -0.00532 0.00821  -0.05383 196 ASP   A CG  
1355 O OD1 . ASP   A 197 ? 0.33911 0.33437 0.36884 -0.00707 0.00708  -0.05167 196 ASP   A OD1 
1356 O OD2 . ASP   A 197 ? 0.39019 0.36914 0.41865 -0.00149 0.00965  -0.05892 196 ASP   A OD2 
1357 N N   . ALA   A 198 ? 0.25208 0.21343 0.29046 -0.01466 0.00701  -0.03654 197 ALA   A N   
1358 C CA  . ALA   A 198 ? 0.26874 0.21627 0.30696 -0.01739 0.00725  -0.03320 197 ALA   A CA  
1359 C C   . ALA   A 198 ? 0.34767 0.27785 0.38230 -0.02013 0.00732  -0.03870 197 ALA   A C   
1360 O O   . ALA   A 198 ? 0.33578 0.26682 0.36843 -0.02661 0.00690  -0.04474 197 ALA   A O   
1361 C CB  . ALA   A 198 ? 0.28615 0.24141 0.32594 -0.02437 0.00712  -0.02963 197 ALA   A CB  
1362 N N   . VAL   A 199 ? 0.33868 0.25292 0.37180 -0.01486 0.00773  -0.03678 198 VAL   A N   
1363 C CA  . VAL   A 199 ? 0.34029 0.23396 0.36867 -0.01423 0.00808  -0.04183 198 VAL   A CA  
1364 C C   . VAL   A 199 ? 0.33671 0.21210 0.36151 -0.02004 0.00801  -0.03719 198 VAL   A C   
1365 O O   . VAL   A 199 ? 0.39577 0.26852 0.42142 -0.01685 0.00782  -0.02931 198 VAL   A O   
1366 C CB  . VAL   A 199 ? 0.37328 0.26253 0.40213 -0.00213 0.00865  -0.04273 198 VAL   A CB  
1367 C CG1 . VAL   A 199 ? 0.42064 0.28564 0.44364 0.00070  0.00922  -0.04762 198 VAL   A CG1 
1368 C CG2 . VAL   A 199 ? 0.38808 0.29549 0.41943 0.00203  0.00926  -0.04723 198 VAL   A CG2 
1369 N N   . GLU   A 200 ? 0.39463 0.25688 0.41439 -0.02924 0.00817  -0.04210 199 GLU   A N   
1370 C CA  . GLU   A 200 ? 0.47602 0.31621 0.49008 -0.03614 0.00848  -0.03803 199 GLU   A CA  
1371 C C   . GLU   A 200 ? 0.46482 0.31564 0.48184 -0.04157 0.00852  -0.02868 199 GLU   A C   
1372 O O   . GLU   A 200 ? 0.48117 0.31769 0.49463 -0.04126 0.00874  -0.02135 199 GLU   A O   
1373 C CB  . GLU   A 200 ? 0.64514 0.46017 0.65409 -0.02589 0.00869  -0.03618 199 GLU   A CB  
1374 C CG  . GLU   A 200 ? 0.60997 0.41611 0.61626 -0.01772 0.00920  -0.04567 199 GLU   A CG  
1375 C CD  . GLU   A 200 ? 0.82283 0.59544 0.82028 -0.01237 0.00973  -0.04621 199 GLU   A CD  
1376 O OE1 . GLU   A 200 ? 0.88347 0.64586 0.87972 -0.00631 0.00920  -0.03718 199 GLU   A OE1 
1377 O OE2 . GLU   A 200 ? 0.85343 0.60932 0.84424 -0.01373 0.01061  -0.05574 199 GLU   A OE2 
1378 N N   . GLY   A 201 ? 0.36483 0.24108 0.38767 -0.04582 0.00838  -0.02877 200 GLY   A N   
1379 C CA  . GLY   A 201 ? 0.32342 0.21148 0.34872 -0.05143 0.00895  -0.02152 200 GLY   A CA  
1380 C C   . GLY   A 201 ? 0.31082 0.22214 0.34234 -0.04415 0.00880  -0.01881 200 GLY   A C   
1381 O O   . GLY   A 201 ? 0.30635 0.22418 0.34005 -0.03594 0.00819  -0.02201 200 GLY   A O   
1382 N N   . PRO   A 202 ? 0.28301 0.20601 0.31644 -0.04719 0.00965  -0.01293 201 PRO   A N   
1383 C CA  . PRO   A 202 ? 0.25157 0.19344 0.28920 -0.04022 0.00979  -0.01075 201 PRO   A CA  
1384 C C   . PRO   A 202 ? 0.24612 0.18146 0.28291 -0.02975 0.00923  -0.00815 201 PRO   A C   
1385 O O   . PRO   A 202 ? 0.29894 0.21819 0.33256 -0.02722 0.00880  -0.00546 201 PRO   A O   
1386 C CB  . PRO   A 202 ? 0.28977 0.24148 0.32792 -0.04583 0.01134  -0.00526 201 PRO   A CB  
1387 C CG  . PRO   A 202 ? 0.30548 0.24953 0.34121 -0.05841 0.01200  -0.00546 201 PRO   A CG  
1388 C CD  . PRO   A 202 ? 0.31445 0.23303 0.34522 -0.05748 0.01091  -0.00812 201 PRO   A CD  
1389 N N   . ALA   A 203 ? 0.24477 0.19335 0.28408 -0.02369 0.00916  -0.00859 202 ALA   A N   
1390 C CA  . ALA   A 203 ? 0.22765 0.17349 0.26642 -0.01566 0.00866  -0.00647 202 ALA   A CA  
1391 C C   . ALA   A 203 ? 0.25746 0.21649 0.29689 -0.01282 0.00930  -0.00489 202 ALA   A C   
1392 O O   . ALA   A 203 ? 0.24823 0.21851 0.28900 -0.01450 0.00994  -0.00629 202 ALA   A O   
1393 C CB  . ALA   A 203 ? 0.23050 0.17273 0.26996 -0.01062 0.00795  -0.01122 202 ALA   A CB  
1394 N N   . ALA   A 204 ? 0.23317 0.19079 0.27117 -0.00823 0.00902  -0.00218 203 ALA   A N   
1395 C CA  . ALA   A 204 ? 0.22951 0.19553 0.26620 -0.00564 0.00977  -0.00147 203 ALA   A CA  
1396 C C   . ALA   A 204 ? 0.24998 0.21379 0.28547 -0.00155 0.00900  -0.00125 203 ALA   A C   
1397 O O   . ALA   A 204 ? 0.26463 0.22323 0.30065 -0.00023 0.00784  0.00008  203 ALA   A O   
1398 C CB  . ALA   A 204 ? 0.23023 0.19968 0.26468 -0.00759 0.01095  0.00211  203 ALA   A CB  
1399 N N   . PHE   A 205 ? 0.22310 0.19112 0.25659 0.00043  0.00964  -0.00229 204 PHE   A N   
1400 C CA  . PHE   A 205 ? 0.20063 0.16775 0.23239 0.00205  0.00917  -0.00208 204 PHE   A CA  
1401 C C   . PHE   A 205 ? 0.23542 0.20272 0.26177 0.00228  0.01023  -0.00157 204 PHE   A C   
1402 O O   . PHE   A 205 ? 0.22821 0.19673 0.25245 0.00357  0.01144  -0.00217 204 PHE   A O   
1403 C CB  . PHE   A 205 ? 0.21774 0.18651 0.25143 0.00344  0.00903  -0.00485 204 PHE   A CB  
1404 C CG  . PHE   A 205 ? 0.24691 0.21856 0.27916 0.00391  0.00993  -0.00678 204 PHE   A CG  
1405 C CD1 . PHE   A 205 ? 0.24944 0.22343 0.28418 0.00345  0.00973  -0.00911 204 PHE   A CD1 
1406 C CD2 . PHE   A 205 ? 0.23008 0.20160 0.25755 0.00451  0.01079  -0.00617 204 PHE   A CD2 
1407 C CE1 . PHE   A 205 ? 0.22575 0.20500 0.25883 0.00442  0.01002  -0.01054 204 PHE   A CE1 
1408 C CE2 . PHE   A 205 ? 0.25439 0.22816 0.27944 0.00603  0.01133  -0.00684 204 PHE   A CE2 
1409 C CZ  . PHE   A 205 ? 0.22703 0.20611 0.25528 0.00639  0.01075  -0.00887 204 PHE   A CZ  
1410 N N   . LEU   A 206 ? 0.21602 0.18211 0.23970 0.00129  0.00964  -0.00069 205 LEU   A N   
1411 C CA  A LEU   A 206 ? 0.23428 0.19719 0.25115 0.00044  0.01060  -0.00126 205 LEU   A CA  
1412 C CA  B LEU   A 206 ? 0.23356 0.19642 0.25042 0.00054  0.01066  -0.00129 205 LEU   A CA  
1413 C C   . LEU   A 206 ? 0.21648 0.17813 0.23196 0.00004  0.01111  -0.00256 205 LEU   A C   
1414 O O   . LEU   A 206 ? 0.26271 0.22876 0.28237 -0.00080 0.01031  -0.00300 205 LEU   A O   
1415 C CB  A LEU   A 206 ? 0.25239 0.21603 0.26681 -0.00225 0.00938  -0.00037 205 LEU   A CB  
1416 C CB  B LEU   A 206 ? 0.25008 0.21303 0.26372 -0.00214 0.00964  -0.00048 205 LEU   A CB  
1417 C CG  A LEU   A 206 ? 0.30095 0.26030 0.30696 -0.00516 0.00991  -0.00159 205 LEU   A CG  
1418 C CG  B LEU   A 206 ? 0.21557 0.17243 0.22038 -0.00435 0.01074  -0.00213 205 LEU   A CG  
1419 C CD1 A LEU   A 206 ? 0.28099 0.23575 0.28317 -0.00755 0.01075  -0.00321 205 LEU   A CD1 
1420 C CD1 B LEU   A 206 ? 0.33471 0.28775 0.33395 -0.00229 0.01243  -0.00266 205 LEU   A CD1 
1421 C CD2 A LEU   A 206 ? 0.28480 0.23982 0.28487 -0.00339 0.01170  -0.00219 205 LEU   A CD2 
1422 C CD2 B LEU   A 206 ? 0.34151 0.30158 0.34460 -0.00917 0.00901  -0.00238 205 LEU   A CD2 
1423 N N   . ASP   A 207 ? 0.22177 0.17746 0.23079 0.00115  0.01263  -0.00289 206 ASP   A N   
1424 C CA  . ASP   A 207 ? 0.23882 0.19155 0.24439 0.00014  0.01335  -0.00296 206 ASP   A CA  
1425 C C   . ASP   A 207 ? 0.27913 0.22056 0.27433 -0.00224 0.01457  -0.00287 206 ASP   A C   
1426 O O   . ASP   A 207 ? 0.27950 0.21367 0.26896 0.00065  0.01555  -0.00318 206 ASP   A O   
1427 C CB  . ASP   A 207 ? 0.27629 0.23054 0.28237 0.00433  0.01383  -0.00268 206 ASP   A CB  
1428 C CG  . ASP   A 207 ? 0.37409 0.33075 0.37990 0.00274  0.01407  -0.00257 206 ASP   A CG  
1429 O OD1 . ASP   A 207 ? 0.29658 0.25468 0.30246 -0.00177 0.01423  -0.00276 206 ASP   A OD1 
1430 O OD2 . ASP   A 207 ? 0.34316 0.30246 0.34862 0.00581  0.01413  -0.00229 206 ASP   A OD2 
1431 N N   . ILE   A 208 ? 0.25688 0.19695 0.24931 -0.00783 0.01475  -0.00279 207 ILE   A N   
1432 C CA  . ILE   A 208 ? 0.27253 0.19907 0.25345 -0.01223 0.01613  -0.00277 207 ILE   A CA  
1433 C C   . ILE   A 208 ? 0.26730 0.18954 0.24390 -0.01310 0.01743  -0.00065 207 ILE   A C   
1434 O O   . ILE   A 208 ? 0.31484 0.24829 0.29744 -0.01563 0.01718  -0.00027 207 ILE   A O   
1435 C CB  . ILE   A 208 ? 0.30041 0.23033 0.28065 -0.02078 0.01527  -0.00419 207 ILE   A CB  
1436 C CG1 . ILE   A 208 ? 0.33189 0.26717 0.31556 -0.01939 0.01367  -0.00552 207 ILE   A CG1 
1437 C CG2 . ILE   A 208 ? 0.33405 0.24776 0.30093 -0.02760 0.01684  -0.00477 207 ILE   A CG2 
1438 C CD1 . ILE   A 208 ? 0.38868 0.33157 0.37278 -0.02689 0.01196  -0.00675 207 ILE   A CD1 
1439 N N   . LEU   A 209 ? 0.28353 0.18960 0.24909 -0.01022 0.01894  0.00090  208 LEU   A N   
1440 C CA  . LEU   A 209 ? 0.28863 0.18796 0.24733 -0.01098 0.02020  0.00418  208 LEU   A CA  
1441 C C   . LEU   A 209 ? 0.36166 0.23998 0.30555 -0.01728 0.02196  0.00510  208 LEU   A C   
1442 O O   . LEU   A 209 ? 0.37977 0.24312 0.31568 -0.01484 0.02256  0.00351  208 LEU   A O   
1443 C CB  . LEU   A 209 ? 0.32548 0.22324 0.28284 -0.00068 0.02013  0.00643  208 LEU   A CB  
1444 C CG  . LEU   A 209 ? 0.34109 0.25756 0.31136 0.00445  0.01844  0.00504  208 LEU   A CG  
1445 C CD1 . LEU   A 209 ? 0.44675 0.36247 0.41488 0.01430  0.01817  0.00668  208 LEU   A CD1 
1446 C CD2 . LEU   A 209 ? 0.39724 0.32580 0.37286 0.00070  0.01815  0.00530  208 LEU   A CD2 
1447 N N   . ALA   A 210 ? 0.34309 0.22006 0.28267 -0.02595 0.02308  0.00727  209 ALA   A N   
1448 C CA  . ALA   A 210 ? 0.35067 0.20599 0.27508 -0.03466 0.02490  0.00805  209 ALA   A CA  
1449 C C   . ALA   A 210 ? 0.37888 0.22592 0.29396 -0.03956 0.02683  0.01330  209 ALA   A C   
1450 O O   . ALA   A 210 ? 0.39544 0.25959 0.31696 -0.04617 0.02717  0.01433  209 ALA   A O   
1451 C CB  . ALA   A 210 ? 0.39873 0.26200 0.32638 -0.04646 0.02428  0.00415  209 ALA   A CB  
1452 N N   . PRO   A 211 ? 0.40079 0.22181 0.30002 -0.03582 0.02831  0.01702  210 PRO   A N   
1453 C CA  . PRO   A 211 ? 0.45709 0.25859 0.34826 -0.02501 0.02833  0.01603  210 PRO   A CA  
1454 C C   . PRO   A 211 ? 0.44996 0.26751 0.35227 -0.01033 0.02655  0.01622  210 PRO   A C   
1455 O O   . PRO   A 211 ? 0.43616 0.27522 0.34973 -0.00948 0.02538  0.01729  210 PRO   A O   
1456 C CB  . PRO   A 211 ? 0.47134 0.24199 0.34209 -0.02544 0.03055  0.02155  210 PRO   A CB  
1457 C CG  . PRO   A 211 ? 0.51955 0.30115 0.39158 -0.03047 0.03099  0.02720  210 PRO   A CG  
1458 C CD  . PRO   A 211 ? 0.44771 0.25687 0.33485 -0.04142 0.03034  0.02328  210 PRO   A CD  
1459 N N   . PRO   A 212 ? 0.46149 0.27005 0.36069 0.00089  0.02650  0.01478  211 PRO   A N   
1460 C CA  . PRO   A 212 ? 0.43348 0.25852 0.34247 0.01389  0.02495  0.01546  211 PRO   A CA  
1461 C C   . PRO   A 212 ? 0.49346 0.31746 0.39752 0.01970  0.02464  0.02181  211 PRO   A C   
1462 O O   . PRO   A 212 ? 0.48620 0.29189 0.37675 0.01565  0.02602  0.02643  211 PRO   A O   
1463 C CB  . PRO   A 212 ? 0.48946 0.30243 0.39284 0.02410  0.02579  0.01291  211 PRO   A CB  
1464 C CG  . PRO   A 212 ? 0.49459 0.28924 0.38871 0.01488  0.02735  0.00881  211 PRO   A CG  
1465 C CD  . PRO   A 212 ? 0.46133 0.24541 0.34767 0.00194  0.02808  0.01179  211 PRO   A CD  
1466 N N   . TYR   A 213 ? 0.41932 0.26379 0.33385 0.02847  0.02271  0.02224  212 TYR   A N   
1467 C CA  . TYR   A 213 ? 0.43321 0.27764 0.34191 0.03621  0.02192  0.02827  212 TYR   A CA  
1468 C C   . TYR   A 213 ? 0.48119 0.29953 0.37365 0.04637  0.02314  0.03200  212 TYR   A C   
1469 O O   . TYR   A 213 ? 0.48306 0.29153 0.37325 0.05154  0.02415  0.02846  212 TYR   A O   
1470 C CB  . TYR   A 213 ? 0.40376 0.27545 0.32605 0.04401  0.01934  0.02710  212 TYR   A CB  
1471 C CG  . TYR   A 213 ? 0.34731 0.24236 0.28328 0.03598  0.01805  0.02397  212 TYR   A CG  
1472 C CD1 . TYR   A 213 ? 0.38234 0.28362 0.31630 0.03168  0.01778  0.02686  212 TYR   A CD1 
1473 C CD2 . TYR   A 213 ? 0.33429 0.24455 0.28421 0.03353  0.01727  0.01816  212 TYR   A CD2 
1474 C CE1 . TYR   A 213 ? 0.34050 0.26203 0.28614 0.02574  0.01695  0.02295  212 TYR   A CE1 
1475 C CE2 . TYR   A 213 ? 0.33405 0.26215 0.29509 0.02748  0.01623  0.01505  212 TYR   A CE2 
1476 C CZ  . TYR   A 213 ? 0.32551 0.25899 0.28439 0.02414  0.01613  0.01698  212 TYR   A CZ  
1477 O OH  . TYR   A 213 ? 0.33040 0.28024 0.29933 0.01942  0.01544  0.01297  212 TYR   A OH  
1478 N N   . ASP   A 214 ? 0.48353 0.28985 0.36356 0.04975  0.02320  0.03931  213 ASP   A N   
1479 C CA  . ASP   A 214 ? 0.54720 0.32702 0.41026 0.06185  0.02411  0.04421  213 ASP   A CA  
1480 C C   . ASP   A 214 ? 0.60087 0.38523 0.45817 0.06964  0.02234  0.05261  213 ASP   A C   
1481 O O   . ASP   A 214 ? 0.66219 0.43279 0.50751 0.06263  0.02328  0.05877  213 ASP   A O   
1482 C CB  . ASP   A 214 ? 0.61391 0.35720 0.45897 0.05339  0.02720  0.04497  213 ASP   A CB  
1483 C CG  . ASP   A 214 ? 0.79798 0.50962 0.62472 0.06736  0.02850  0.04842  213 ASP   A CG  
1484 O OD1 . ASP   A 214 ? 0.77652 0.49676 0.60469 0.08462  0.02684  0.05149  213 ASP   A OD1 
1485 O OD2 . ASP   A 214 ? 0.84602 0.52434 0.65669 0.06123  0.03118  0.04770  213 ASP   A OD2 
1486 N N   . PRO   A 215 ? 0.58125 0.38756 0.44704 0.08334  0.01964  0.05321  214 PRO   A N   
1487 C CA  . PRO   A 215 ? 0.62747 0.44231 0.48819 0.09097  0.01724  0.06118  214 PRO   A CA  
1488 C C   . PRO   A 215 ? 0.69565 0.47643 0.53318 0.09811  0.01844  0.07054  214 PRO   A C   
1489 O O   . PRO   A 215 ? 0.74558 0.52362 0.57372 0.09576  0.01778  0.07828  214 PRO   A O   
1490 C CB  . PRO   A 215 ? 0.62036 0.46359 0.49401 0.10517  0.01423  0.05897  214 PRO   A CB  
1491 C CG  . PRO   A 215 ? 0.56884 0.42647 0.45881 0.09888  0.01502  0.04921  214 PRO   A CG  
1492 C CD  . PRO   A 215 ? 0.56586 0.39409 0.44707 0.09061  0.01855  0.04659  214 PRO   A CD  
1493 N N   . ASP   A 216 ? 0.73203 0.48535 0.55879 0.10683  0.02039  0.07008  215 ASP   A N   
1494 C CA  . ASP   A 216 ? 0.87933 0.59491 0.68189 0.11457  0.02173  0.07904  215 ASP   A CA  
1495 C C   . ASP   A 216 ? 0.90832 0.59531 0.69605 0.09643  0.02469  0.08230  215 ASP   A C   
1496 O O   . ASP   A 216 ? 1.06204 0.71408 0.82753 0.09980  0.02614  0.09056  215 ASP   A O   
1497 C CB  . ASP   A 216 ? 0.90284 0.59519 0.69732 0.12922  0.02345  0.07616  215 ASP   A CB  
1498 C CG  . ASP   A 216 ? 0.94834 0.67070 0.75664 0.14813  0.02088  0.07382  215 ASP   A CG  
1499 O OD1 . ASP   A 216 ? 0.93858 0.68865 0.75407 0.15489  0.01727  0.07868  215 ASP   A OD1 
1500 O OD2 . ASP   A 216 ? 1.01907 0.73919 0.83097 0.15556  0.02252  0.06691  215 ASP   A OD2 
1501 N N   . ASP   A 217 ? 0.85317 0.55442 0.65225 0.07746  0.02568  0.07637  216 ASP   A N   
1502 C CA  . ASP   A 217 ? 0.85663 0.53724 0.64439 0.05834  0.02862  0.07846  216 ASP   A CA  
1503 C C   . ASP   A 217 ? 0.92457 0.63372 0.72252 0.04530  0.02799  0.07964  216 ASP   A C   
1504 O O   . ASP   A 217 ? 0.95950 0.66570 0.75668 0.02726  0.03036  0.07794  216 ASP   A O   
1505 C CB  . ASP   A 217 ? 0.89742 0.56545 0.68711 0.04698  0.03103  0.06932  216 ASP   A CB  
1506 C CG  . ASP   A 217 ? 1.16013 0.80197 0.93482 0.02768  0.03423  0.07159  216 ASP   A CG  
1507 O OD1 . ASP   A 217 ? 1.18141 0.83670 0.96631 0.01133  0.03509  0.06522  216 ASP   A OD1 
1508 O OD2 . ASP   A 217 ? 1.16732 0.77566 0.91976 0.02872  0.03585  0.08004  216 ASP   A OD2 
1509 N N   . GLY   A 218 ? 0.88940 0.62783 0.69707 0.05399  0.02490  0.08181  217 GLY   A N   
1510 C CA  . GLY   A 218 ? 0.83646 0.60121 0.65218 0.04321  0.02453  0.08232  217 GLY   A CA  
1511 C C   . GLY   A 218 ? 0.86989 0.66269 0.70699 0.03308  0.02446  0.07190  217 GLY   A C   
1512 O O   . GLY   A 218 ? 0.85662 0.66632 0.69876 0.02184  0.02531  0.07122  217 GLY   A O   
1513 N N   . ARG   A 219 ? 0.67455 0.47272 0.52371 0.03727  0.02366  0.06397  218 ARG   A N   
1514 C CA  . ARG   A 219 ? 0.64679 0.46983 0.51570 0.02969  0.02323  0.05468  218 ARG   A CA  
1515 C C   . ARG   A 219 ? 0.52476 0.37022 0.40794 0.04169  0.02016  0.05041  218 ARG   A C   
1516 O O   . ARG   A 219 ? 0.58882 0.43284 0.47806 0.04599  0.02003  0.04544  218 ARG   A O   
1517 C CB  . ARG   A 219 ? 0.67311 0.48150 0.54230 0.02033  0.02540  0.04927  218 ARG   A CB  
1518 C CG  . ARG   A 219 ? 0.80966 0.60779 0.67123 0.00370  0.02821  0.05088  218 ARG   A CG  
1519 C CD  . ARG   A 219 ? 0.57648 0.37427 0.44501 -0.00628 0.02915  0.04344  218 ARG   A CD  
1520 N NE  . ARG   A 219 ? 0.62037 0.40544 0.48812 0.00208  0.02860  0.03944  218 ARG   A NE  
1521 C CZ  . ARG   A 219 ? 0.66520 0.41814 0.51602 0.00446  0.03018  0.04129  218 ARG   A CZ  
1522 N NH1 . ARG   A 219 ? 0.75723 0.48471 0.58954 -0.00054 0.03217  0.04803  218 ARG   A NH1 
1523 N NH2 . ARG   A 219 ? 0.62619 0.37121 0.47758 0.01194  0.03002  0.03622  218 ARG   A NH2 
1524 N N   . ASP   A 220 ? 0.49501 0.36238 0.38311 0.04611  0.01779  0.05212  219 ASP   A N   
1525 C CA  . ASP   A 220 ? 0.40635 0.29843 0.30880 0.05438  0.01481  0.04751  219 ASP   A CA  
1526 C C   . ASP   A 220 ? 0.44557 0.36161 0.36377 0.04510  0.01427  0.04027  219 ASP   A C   
1527 O O   . ASP   A 220 ? 0.43194 0.34854 0.35014 0.03437  0.01601  0.03928  219 ASP   A O   
1528 C CB  . ASP   A 220 ? 0.43937 0.34168 0.33690 0.06625  0.01188  0.05340  219 ASP   A CB  
1529 C CG  . ASP   A 220 ? 0.59140 0.50651 0.49693 0.07915  0.00951  0.05119  219 ASP   A CG  
1530 O OD1 . ASP   A 220 ? 0.45804 0.38718 0.37817 0.07614  0.00933  0.04361  219 ASP   A OD1 
1531 O OD2 . ASP   A 220 ? 0.57668 0.48814 0.47356 0.09254  0.00796  0.05743  219 ASP   A OD2 
1532 N N   . CYS   A 221 ? 0.38076 0.31691 0.31208 0.04960  0.01196  0.03521  220 CYS   A N   
1533 C CA  . CYS   A 221 ? 0.33289 0.28963 0.27839 0.04250  0.01116  0.02806  220 CYS   A CA  
1534 C C   . CYS   A 221 ? 0.36709 0.34379 0.31345 0.04492  0.00858  0.02857  220 CYS   A C   
1535 O O   . CYS   A 221 ? 0.38901 0.37681 0.33649 0.05356  0.00590  0.02991  220 CYS   A O   
1536 C CB  . CYS   A 221 ? 0.34191 0.30592 0.29957 0.04408  0.01048  0.02239  220 CYS   A CB  
1537 S SG  . CYS   A 221 ? 0.34488 0.32817 0.31791 0.03587  0.00961  0.01413  220 CYS   A SG  
1538 N N   . HIS   A 222 ? 0.34079 0.32362 0.28612 0.03756  0.00941  0.02740  221 HIS   A N   
1539 C CA  . HIS   A 222 ? 0.33589 0.33833 0.28112 0.03842  0.00715  0.02658  221 HIS   A CA  
1540 C C   . HIS   A 222 ? 0.30657 0.32510 0.26451 0.03213  0.00671  0.01699  221 HIS   A C   
1541 O O   . HIS   A 222 ? 0.29841 0.31194 0.26176 0.02564  0.00903  0.01281  221 HIS   A O   
1542 C CB  . HIS   A 222 ? 0.38695 0.38546 0.31951 0.03527  0.00872  0.03220  221 HIS   A CB  
1543 C CG  . HIS   A 222 ? 0.42800 0.40356 0.34599 0.03869  0.01017  0.04181  221 HIS   A CG  
1544 N ND1 . HIS   A 222 ? 0.51592 0.48846 0.42270 0.04851  0.00801  0.04990  221 HIS   A ND1 
1545 C CD2 . HIS   A 222 ? 0.41954 0.37275 0.33157 0.03372  0.01340  0.04448  221 HIS   A CD2 
1546 C CE1 . HIS   A 222 ? 0.56159 0.50772 0.45513 0.04979  0.01017  0.05735  221 HIS   A CE1 
1547 N NE2 . HIS   A 222 ? 0.53789 0.47192 0.43424 0.03998  0.01350  0.05385  221 HIS   A NE2 
1548 N N   . TYR   A 223 ? 0.31379 0.35140 0.27556 0.03409  0.00362  0.01358  222 TYR   A N   
1549 C CA  . TYR   A 223 ? 0.29316 0.34370 0.26501 0.02821  0.00299  0.00405  222 TYR   A CA  
1550 C C   . TYR   A 223 ? 0.29659 0.35855 0.26331 0.02480  0.00301  0.00141  222 TYR   A C   
1551 O O   . TYR   A 223 ? 0.32131 0.38754 0.27767 0.02804  0.00212  0.00730  222 TYR   A O   
1552 C CB  . TYR   A 223 ? 0.27773 0.34226 0.25763 0.03046  -0.00036 0.00048  222 TYR   A CB  
1553 C CG  . TYR   A 223 ? 0.28564 0.34127 0.27131 0.03317  0.00024  0.00190  222 TYR   A CG  
1554 C CD1 . TYR   A 223 ? 0.26934 0.31874 0.26368 0.02763  0.00180  -0.00331 222 TYR   A CD1 
1555 C CD2 . TYR   A 223 ? 0.30859 0.36170 0.29004 0.04204  -0.00060 0.00857  222 TYR   A CD2 
1556 C CE1 . TYR   A 223 ? 0.27797 0.32028 0.27657 0.02978  0.00254  -0.00191 222 TYR   A CE1 
1557 C CE2 . TYR   A 223 ? 0.27783 0.32320 0.26384 0.04488  0.00049  0.00912  222 TYR   A CE2 
1558 C CZ  . TYR   A 223 ? 0.26643 0.30735 0.26088 0.03811  0.00205  0.00383  222 TYR   A CZ  
1559 O OH  . TYR   A 223 ? 0.28492 0.31952 0.28296 0.04052  0.00324  0.00438  222 TYR   A OH  
1560 N N   . TYR   A 224 ? 0.28653 0.35269 0.25960 0.01884  0.00418  -0.00737 223 TYR   A N   
1561 C CA  . TYR   A 224 ? 0.30523 0.38166 0.27364 0.01549  0.00509  -0.01175 223 TYR   A CA  
1562 C C   . TYR   A 224 ? 0.34658 0.43205 0.32215 0.01165  0.00387  -0.02301 223 TYR   A C   
1563 O O   . TYR   A 224 ? 0.29796 0.37752 0.28260 0.00999  0.00358  -0.02725 223 TYR   A O   
1564 C CB  . TYR   A 224 ? 0.29091 0.35929 0.25691 0.01214  0.00962  -0.01092 223 TYR   A CB  
1565 C CG  . TYR   A 224 ? 0.31838 0.37546 0.27552 0.01340  0.01125  -0.00023 223 TYR   A CG  
1566 C CD1 . TYR   A 224 ? 0.33525 0.37644 0.29503 0.01435  0.01189  0.00389  223 TYR   A CD1 
1567 C CD2 . TYR   A 224 ? 0.33005 0.39099 0.27475 0.01315  0.01221  0.00579  223 TYR   A CD2 
1568 C CE1 . TYR   A 224 ? 0.37773 0.40515 0.32787 0.01470  0.01346  0.01291  223 TYR   A CE1 
1569 C CE2 . TYR   A 224 ? 0.40792 0.45467 0.34276 0.01332  0.01387  0.01599  223 TYR   A CE2 
1570 C CZ  . TYR   A 224 ? 0.38851 0.41751 0.32603 0.01393  0.01450  0.01912  223 TYR   A CZ  
1571 O OH  . TYR   A 224 ? 0.42454 0.43614 0.35084 0.01331  0.01625  0.02844  223 TYR   A OH  
1572 N N   . ARG   A 225 ? 0.33544 0.43419 0.30546 0.00980  0.00330  -0.02785 224 ARG   A N   
1573 C CA  . ARG   A 225 ? 0.31045 0.41467 0.28393 0.00533  0.00320  -0.03990 224 ARG   A CA  
1574 C C   . ARG   A 225 ? 0.37624 0.48009 0.34592 0.00409  0.00742  -0.04409 224 ARG   A C   
1575 O O   . ARG   A 225 ? 0.37727 0.48673 0.33837 0.00511  0.00904  -0.03865 224 ARG   A O   
1576 C CB  . ARG   A 225 ? 0.39227 0.51487 0.36114 0.00377  -0.00086 -0.04398 224 ARG   A CB  
1577 C CG  . ARG   A 225 ? 0.55873 0.68824 0.53313 0.00372  -0.00526 -0.04300 224 ARG   A CG  
1578 C CD  . ARG   A 225 ? 0.56970 0.72192 0.53812 0.00298  -0.00969 -0.04472 224 ARG   A CD  
1579 N NE  . ARG   A 225 ? 0.62681 0.78659 0.58986 -0.00251 -0.00931 -0.05545 224 ARG   A NE  
1580 C CZ  . ARG   A 225 ? 0.67678 0.85674 0.63188 -0.00370 -0.01255 -0.05771 224 ARG   A CZ  
1581 N NH1 . ARG   A 225 ? 0.55462 0.75024 0.50636 0.00106  -0.01668 -0.04910 224 ARG   A NH1 
1582 N NH2 . ARG   A 225 ? 0.65088 0.83574 0.60066 -0.00910 -0.01170 -0.06904 224 ARG   A NH2 
1583 N N   . VAL   A 226 ? 0.34144 0.43887 0.31697 0.00229  0.00945  -0.05336 225 VAL   A N   
1584 C CA  A VAL   A 226 ? 0.35596 0.45674 0.32848 0.00226  0.01341  -0.05985 225 VAL   A CA  
1585 C CA  B VAL   A 226 ? 0.35615 0.45702 0.32859 0.00226  0.01340  -0.05982 225 VAL   A CA  
1586 C C   . VAL   A 226 ? 0.44366 0.55388 0.41131 -0.00022 0.01209  -0.07107 225 VAL   A C   
1587 O O   . VAL   A 226 ? 0.42464 0.53039 0.39591 -0.00300 0.00947  -0.07773 225 VAL   A O   
1588 C CB  A VAL   A 226 ? 0.49615 0.58430 0.47723 0.00379  0.01646  -0.06331 225 VAL   A CB  
1589 C CB  B VAL   A 226 ? 0.49604 0.58447 0.47695 0.00382  0.01654  -0.06319 225 VAL   A CB  
1590 C CG1 A VAL   A 226 ? 0.46688 0.54218 0.45588 0.00284  0.01392  -0.06567 225 VAL   A CG1 
1591 C CG1 B VAL   A 226 ? 0.41362 0.50642 0.39285 0.00526  0.02096  -0.05909 225 VAL   A CG1 
1592 C CG2 A VAL   A 226 ? 0.44999 0.54263 0.42908 0.00505  0.01992  -0.07388 225 VAL   A CG2 
1593 C CG2 B VAL   A 226 ? 0.40010 0.47524 0.38911 0.00404  0.01465  -0.05801 225 VAL   A CG2 
1594 N N   . LEU   A 227 ? 0.48883 0.61220 0.44736 -0.00020 0.01401  -0.07343 226 LEU   A N   
1595 C CA  . LEU   A 227 ? 0.48911 0.62386 0.44058 -0.00311 0.01217  -0.08357 226 LEU   A CA  
1596 C C   . LEU   A 227 ? 0.64571 0.77830 0.59568 -0.00269 0.01605  -0.09714 226 LEU   A C   
1597 O O   . LEU   A 227 ? 0.59328 0.72662 0.54339 0.00075  0.02094  -0.09713 226 LEU   A O   
1598 C CB  . LEU   A 227 ? 0.47955 0.63276 0.41951 -0.00329 0.01080  -0.07755 226 LEU   A CB  
1599 C CG  . LEU   A 227 ? 0.46712 0.62167 0.40630 -0.00130 0.00747  -0.06310 226 LEU   A CG  
1600 C CD1 . LEU   A 227 ? 0.51913 0.68848 0.44504 -0.00022 0.00755  -0.05560 226 LEU   A CD1 
1601 C CD2 . LEU   A 227 ? 0.56143 0.71908 0.50490 -0.00289 0.00177  -0.06463 226 LEU   A CD2 
1602 N N   . GLU   A 228 ? 0.51459 0.64522 0.46256 -0.00637 0.01391  -0.10916 227 GLU   A N   
1603 C CA  . GLU   A 228 ? 0.71633 0.84041 0.66173 -0.00531 0.01736  -0.12360 227 GLU   A CA  
1604 C C   . GLU   A 228 ? 0.58856 0.73086 0.52124 -0.00677 0.01829  -0.13128 227 GLU   A C   
1605 O O   . GLU   A 228 ? 0.53685 0.68750 0.46319 -0.01257 0.01411  -0.13641 227 GLU   A O   
1606 C CB  . GLU   A 228 ? 0.77036 0.87683 0.71923 -0.00949 0.01493  -0.13293 227 GLU   A CB  
1607 C CG  . GLU   A 228 ? 0.76265 0.85927 0.70559 -0.00898 0.01779  -0.14959 227 GLU   A CG  
1608 C CD  . GLU   A 228 ? 0.72607 0.82611 0.66046 -0.01785 0.01410  -0.16079 227 GLU   A CD  
1609 O OE1 . GLU   A 228 ? 0.71566 0.81071 0.65378 -0.02505 0.00963  -0.15921 227 GLU   A OE1 
1610 O OE2 . GLU   A 228 ? 0.73852 0.84764 0.66227 -0.01820 0.01578  -0.17153 227 GLU   A OE2 
1611 N N   . PRO   A 229 ? 0.61767 0.76879 0.54613 -0.00222 0.02360  -0.13247 228 PRO   A N   
1612 C CA  . PRO   A 229 ? 0.64567 0.81530 0.56092 -0.00354 0.02507  -0.14028 228 PRO   A CA  
1613 C C   . PRO   A 229 ? 0.76400 0.92615 0.67386 -0.00523 0.02538  -0.15901 228 PRO   A C   
1614 O O   . PRO   A 229 ? 0.88900 1.02954 0.80495 -0.00417 0.02569  -0.16618 228 PRO   A O   
1615 C CB  . PRO   A 229 ? 0.61673 0.79555 0.53141 0.00197  0.03174  -0.13687 228 PRO   A CB  
1616 C CG  . PRO   A 229 ? 0.68492 0.85561 0.61033 0.00354  0.03159  -0.12196 228 PRO   A CG  
1617 C CD  . PRO   A 229 ? 0.69606 0.84473 0.63123 0.00361  0.02856  -0.12577 228 PRO   A CD  
1618 N N   . VAL   A 230 ? 0.68599 0.86536 0.58274 -0.00810 0.02534  -0.16693 229 VAL   A N   
1619 C CA  . VAL   A 230 ? 0.77535 0.94864 0.66378 -0.01007 0.02627  -0.18632 229 VAL   A CA  
1620 C C   . VAL   A 230 ? 0.75325 0.94642 0.62905 -0.00733 0.03106  -0.19371 229 VAL   A C   
1621 O O   . VAL   A 230 ? 0.82334 1.03098 0.69928 -0.00291 0.03502  -0.18428 229 VAL   A O   
1622 C CB  . VAL   A 230 ? 0.76569 0.93917 0.64965 -0.02028 0.01929  -0.19196 229 VAL   A CB  
1623 C CG1 . VAL   A 230 ? 0.75525 0.90614 0.65107 -0.02330 0.01601  -0.18893 229 VAL   A CG1 
1624 C CG2 . VAL   A 230 ? 0.69255 0.89279 0.57090 -0.02444 0.01443  -0.18124 229 VAL   A CG2 
1625 N N   . ASP   A 241 ? 0.77498 0.86437 0.79279 0.08018  0.05135  -0.13269 240 ASP   A N   
1626 C CA  . ASP   A 241 ? 0.70758 0.82416 0.73438 0.08389  0.05443  -0.12719 240 ASP   A CA  
1627 C C   . ASP   A 241 ? 0.68132 0.80907 0.71060 0.07109  0.05243  -0.11405 240 ASP   A C   
1628 O O   . ASP   A 241 ? 0.75992 0.89390 0.78182 0.06146  0.05253  -0.11202 240 ASP   A O   
1629 C CB  . ASP   A 241 ? 0.66615 0.80744 0.68982 0.08931  0.06063  -0.13608 240 ASP   A CB  
1630 N N   . LEU   A 242 ? 0.70581 0.83513 0.74443 0.07129  0.05048  -0.10519 241 LEU   A N   
1631 C CA  . LEU   A 242 ? 0.56916 0.70475 0.60903 0.05938  0.04857  -0.09343 241 LEU   A CA  
1632 C C   . LEU   A 242 ? 0.55265 0.71544 0.60049 0.05918  0.05151  -0.08867 241 LEU   A C   
1633 O O   . LEU   A 242 ? 0.68678 0.85904 0.74295 0.06959  0.05282  -0.09171 241 LEU   A O   
1634 C CB  . LEU   A 242 ? 0.48721 0.59987 0.52964 0.05640  0.04316  -0.08654 241 LEU   A CB  
1635 C CG  . LEU   A 242 ? 0.54280 0.63117 0.57796 0.05294  0.03987  -0.08907 241 LEU   A CG  
1636 C CD1 . LEU   A 242 ? 0.55608 0.62774 0.59412 0.04842  0.03529  -0.08069 241 LEU   A CD1 
1637 C CD2 . LEU   A 242 ? 0.54606 0.64090 0.57194 0.04480  0.04058  -0.08985 241 LEU   A CD2 
1638 N N   . PRO   A 243 ? 0.60613 0.78215 0.65124 0.04744  0.05258  -0.08109 242 PRO   A N   
1639 C CA  . PRO   A 243 ? 0.51644 0.68302 0.55114 0.03655  0.05112  -0.07631 242 PRO   A CA  
1640 C C   . PRO   A 243 ? 0.59128 0.76339 0.61662 0.03751  0.05390  -0.08392 242 PRO   A C   
1641 O O   . PRO   A 243 ? 0.53966 0.72762 0.56594 0.04460  0.05822  -0.09222 242 PRO   A O   
1642 C CB  . PRO   A 243 ? 0.42485 0.60624 0.45959 0.02571  0.05260  -0.06643 242 PRO   A CB  
1643 C CG  . PRO   A 243 ? 0.51186 0.72037 0.55556 0.03004  0.05678  -0.06914 242 PRO   A CG  
1644 C CD  . PRO   A 243 ? 0.55588 0.75709 0.60822 0.04383  0.05503  -0.07570 242 PRO   A CD  
1645 N N   . ARG   A 244 ? 0.38371 0.54446 0.39949 0.03082  0.05148  -0.08143 243 ARG   A N   
1646 C CA  . ARG   A 244 ? 0.42007 0.58745 0.42574 0.03070  0.05351  -0.08829 243 ARG   A CA  
1647 C C   . ARG   A 244 ? 0.47239 0.63604 0.46806 0.02096  0.05113  -0.08009 243 ARG   A C   
1648 O O   . ARG   A 244 ? 0.38795 0.53554 0.38435 0.01723  0.04677  -0.07285 243 ARG   A O   
1649 C CB  . ARG   A 244 ? 0.54279 0.69478 0.54724 0.03844  0.05198  -0.10013 243 ARG   A CB  
1650 C CG  . ARG   A 244 ? 0.55532 0.68737 0.55416 0.03364  0.04676  -0.09932 243 ARG   A CG  
1651 C CD  . ARG   A 244 ? 0.66343 0.78527 0.65719 0.03818  0.04646  -0.11262 243 ARG   A CD  
1652 N NE  . ARG   A 244 ? 0.61413 0.71503 0.60639 0.03406  0.04113  -0.11221 243 ARG   A NE  
1653 C CZ  . ARG   A 244 ? 0.58702 0.66760 0.58511 0.03702  0.03873  -0.11315 243 ARG   A CZ  
1654 N NH1 . ARG   A 244 ? 0.62438 0.70121 0.62995 0.04543  0.04066  -0.11442 243 ARG   A NH1 
1655 N NH2 . ARG   A 244 ? 0.64617 0.71127 0.64242 0.03143  0.03428  -0.11229 243 ARG   A NH2 
1656 N N   . GLU   A 245 ? 0.40262 0.58211 0.38855 0.01766  0.05416  -0.08097 244 GLU   A N   
1657 C CA  . GLU   A 245 ? 0.43436 0.61180 0.40923 0.00984  0.05199  -0.07254 244 GLU   A CA  
1658 C C   . GLU   A 245 ? 0.44601 0.60867 0.41645 0.01092  0.04683  -0.07650 244 GLU   A C   
1659 O O   . GLU   A 245 ? 0.49727 0.65838 0.46714 0.01562  0.04677  -0.08830 244 GLU   A O   
1660 C CB  . GLU   A 245 ? 0.47684 0.67625 0.44131 0.00632  0.05668  -0.07240 244 GLU   A CB  
1661 C CG  . GLU   A 245 ? 0.64322 0.85550 0.60749 -0.00069 0.06066  -0.06228 244 GLU   A CG  
1662 C CD  . GLU   A 245 ? 0.70953 0.94424 0.66261 -0.00496 0.06575  -0.06168 244 GLU   A CD  
1663 O OE1 . GLU   A 245 ? 0.79053 1.04038 0.74286 0.00060  0.06920  -0.07305 244 GLU   A OE1 
1664 O OE2 . GLU   A 245 ? 0.81696 1.05318 0.76097 -0.01380 0.06651  -0.04985 244 GLU   A OE2 
1665 N N   . VAL   A 246 ? 0.38446 0.53652 0.35138 0.00641  0.04260  -0.06687 245 VAL   A N   
1666 C CA  . VAL   A 246 ? 0.37150 0.51404 0.33456 0.00629  0.03743  -0.06890 245 VAL   A CA  
1667 C C   . VAL   A 246 ? 0.35078 0.49819 0.30257 0.00189  0.03557  -0.05891 245 VAL   A C   
1668 O O   . VAL   A 246 ? 0.37627 0.52931 0.32301 -0.00151 0.03820  -0.04977 245 VAL   A O   
1669 C CB  . VAL   A 246 ? 0.42454 0.54778 0.39688 0.00758  0.03335  -0.06743 245 VAL   A CB  
1670 C CG1 . VAL   A 246 ? 0.50954 0.62603 0.49112 0.01272  0.03476  -0.07679 245 VAL   A CG1 
1671 C CG2 . VAL   A 246 ? 0.38104 0.49738 0.35594 0.00492  0.03280  -0.05485 245 VAL   A CG2 
1672 N N   . TRP   A 247 ? 0.37980 0.52503 0.32719 0.00184  0.03086  -0.06045 246 TRP   A N   
1673 C CA  . TRP   A 247 ? 0.33792 0.48633 0.27534 -0.00013 0.02779  -0.05037 246 TRP   A CA  
1674 C C   . TRP   A 247 ? 0.35132 0.48541 0.29411 0.00103  0.02288  -0.04448 246 TRP   A C   
1675 O O   . TRP   A 247 ? 0.41734 0.54529 0.36770 0.00202  0.02019  -0.05157 246 TRP   A O   
1676 C CB  . TRP   A 247 ? 0.35518 0.51874 0.28232 -0.00067 0.02608  -0.05650 246 TRP   A CB  
1677 C CG  . TRP   A 247 ? 0.37795 0.55773 0.29702 -0.00187 0.03130  -0.06023 246 TRP   A CG  
1678 C CD1 . TRP   A 247 ? 0.44791 0.63565 0.36788 -0.00046 0.03462  -0.07407 246 TRP   A CD1 
1679 C CD2 . TRP   A 247 ? 0.40652 0.59592 0.31498 -0.00468 0.03436  -0.04978 246 TRP   A CD2 
1680 N NE1 . TRP   A 247 ? 0.48717 0.69213 0.39821 -0.00191 0.03967  -0.07333 246 TRP   A NE1 
1681 C CE2 . TRP   A 247 ? 0.48230 0.68868 0.38616 -0.00531 0.03960  -0.05806 246 TRP   A CE2 
1682 C CE3 . TRP   A 247 ? 0.41141 0.59554 0.31256 -0.00671 0.03334  -0.03418 246 TRP   A CE3 
1683 C CZ2 . TRP   A 247 ? 0.43712 0.65751 0.32999 -0.00905 0.04400  -0.05072 246 TRP   A CZ2 
1684 C CZ3 . TRP   A 247 ? 0.47817 0.67284 0.36741 -0.01065 0.03748  -0.02655 246 TRP   A CZ3 
1685 C CH2 . TRP   A 247 ? 0.44145 0.65514 0.32698 -0.01235 0.04280  -0.03458 246 TRP   A CH2 
1686 N N   . LEU   A 248 ? 0.33418 0.46233 0.27230 0.00082  0.02205  -0.03163 247 LEU   A N   
1687 C CA  . LEU   A 248 ? 0.32266 0.43735 0.26534 0.00301  0.01828  -0.02539 247 LEU   A CA  
1688 C C   . LEU   A 248 ? 0.40438 0.52377 0.33736 0.00550  0.01424  -0.01759 247 LEU   A C   
1689 O O   . LEU   A 248 ? 0.40701 0.53085 0.32800 0.00507  0.01539  -0.00982 247 LEU   A O   
1690 C CB  . LEU   A 248 ? 0.32929 0.42963 0.27451 0.00189  0.02077  -0.01725 247 LEU   A CB  
1691 C CG  . LEU   A 248 ? 0.35633 0.45277 0.31225 0.00038  0.02402  -0.02310 247 LEU   A CG  
1692 C CD1 . LEU   A 248 ? 0.37116 0.45780 0.32616 -0.00269 0.02650  -0.01427 247 LEU   A CD1 
1693 C CD2 . LEU   A 248 ? 0.42060 0.50901 0.38778 0.00287  0.02119  -0.02958 247 LEU   A CD2 
1694 N N   . LEU   A 249 ? 0.30454 0.42375 0.24245 0.00824  0.00958  -0.01901 248 LEU   A N   
1695 C CA  . LEU   A 249 ? 0.30440 0.42999 0.23504 0.01251  0.00514  -0.01138 248 LEU   A CA  
1696 C C   . LEU   A 249 ? 0.37554 0.48810 0.31184 0.01694  0.00312  -0.00492 248 LEU   A C   
1697 O O   . LEU   A 249 ? 0.37800 0.48828 0.32557 0.01641  0.00177  -0.01093 248 LEU   A O   
1698 C CB  . LEU   A 249 ? 0.30264 0.44703 0.23351 0.01171  0.00102  -0.01990 248 LEU   A CB  
1699 C CG  . LEU   A 249 ? 0.33454 0.49055 0.25993 0.01695  -0.00444 -0.01276 248 LEU   A CG  
1700 C CD1 . LEU   A 249 ? 0.39516 0.55428 0.30489 0.02012  -0.00396 -0.00158 248 LEU   A CD1 
1701 C CD2 . LEU   A 249 ? 0.39588 0.57165 0.32381 0.01381  -0.00856 -0.02324 248 LEU   A CD2 
1702 N N   . GLU   A 250 ? 0.30934 0.41254 0.23680 0.02131  0.00313  0.00721  249 GLU   A N   
1703 C CA  . GLU   A 250 ? 0.36455 0.45575 0.29566 0.02711  0.00131  0.01297  249 GLU   A CA  
1704 C C   . GLU   A 250 ? 0.39375 0.50121 0.32868 0.03222  -0.00404 0.01125  249 GLU   A C   
1705 O O   . GLU   A 250 ? 0.38990 0.51477 0.31814 0.03404  -0.00710 0.01209  249 GLU   A O   
1706 C CB  . GLU   A 250 ? 0.40458 0.47952 0.32300 0.03128  0.00261  0.02597  249 GLU   A CB  
1707 C CG  . GLU   A 250 ? 0.41537 0.47434 0.33652 0.03774  0.00173  0.03091  249 GLU   A CG  
1708 C CD  . GLU   A 250 ? 0.57669 0.61282 0.48418 0.04018  0.00402  0.04236  249 GLU   A CD  
1709 O OE1 . GLU   A 250 ? 0.75561 0.78577 0.65448 0.03362  0.00740  0.04551  249 GLU   A OE1 
1710 O OE2 . GLU   A 250 ? 0.63618 0.66009 0.54092 0.04847  0.00269  0.04802  249 GLU   A OE2 
1711 N N   . THR   A 251 ? 0.36511 0.46904 0.31073 0.03413  -0.00520 0.00894  250 THR   A N   
1712 C CA  . THR   A 251 ? 0.36339 0.48603 0.31580 0.03652  -0.00977 0.00525  250 THR   A CA  
1713 C C   . THR   A 251 ? 0.35556 0.47111 0.31324 0.04351  -0.01050 0.01008  250 THR   A C   
1714 O O   . THR   A 251 ? 0.32763 0.42296 0.28722 0.04337  -0.00720 0.01192  250 THR   A O   
1715 C CB  . THR   A 251 ? 0.37286 0.50386 0.33555 0.02748  -0.00988 -0.00766 250 THR   A CB  
1716 O OG1 . THR   A 251 ? 0.56107 0.71459 0.52769 0.02711  -0.01459 -0.01173 250 THR   A OG1 
1717 C CG2 . THR   A 251 ? 0.38293 0.49780 0.35604 0.02439  -0.00715 -0.01106 250 THR   A CG2 
1718 N N   . PRO   A 252 ? 0.37421 0.50762 0.33395 0.05001  -0.01471 0.01208  251 PRO   A N   
1719 C CA  . PRO   A 252 ? 0.34787 0.47820 0.31402 0.05705  -0.01503 0.01510  251 PRO   A CA  
1720 C C   . PRO   A 252 ? 0.35707 0.48393 0.33640 0.04923  -0.01315 0.00685  251 PRO   A C   
1721 O O   . PRO   A 252 ? 0.33497 0.46632 0.31975 0.03917  -0.01286 -0.00182 251 PRO   A O   
1722 C CB  . PRO   A 252 ? 0.42769 0.58585 0.39496 0.06450  -0.02029 0.01725  251 PRO   A CB  
1723 C CG  . PRO   A 252 ? 0.38674 0.56366 0.34983 0.05883  -0.02313 0.01337  251 PRO   A CG  
1724 C CD  . PRO   A 252 ? 0.42172 0.58154 0.37794 0.05126  -0.01939 0.01133  251 PRO   A CD  
1725 N N   . GLN   A 253 ? 0.33414 0.45098 0.31736 0.05436  -0.01163 0.00977  252 GLN   A N   
1726 C CA  . GLN   A 253 ? 0.33625 0.45262 0.33134 0.04789  -0.01025 0.00331  252 GLN   A CA  
1727 C C   . GLN   A 253 ? 0.29977 0.44191 0.30363 0.04150  -0.01346 -0.00375 252 GLN   A C   
1728 O O   . GLN   A 253 ? 0.33519 0.50007 0.34039 0.04687  -0.01697 -0.00187 252 GLN   A O   
1729 C CB  . GLN   A 253 ? 0.27890 0.38845 0.27608 0.05624  -0.00890 0.00776  252 GLN   A CB  
1730 C CG  . GLN   A 253 ? 0.29038 0.39542 0.29746 0.04982  -0.00669 0.00276  252 GLN   A CG  
1731 C CD  . GLN   A 253 ? 0.30211 0.40373 0.31031 0.05878  -0.00527 0.00659  252 GLN   A CD  
1732 O OE1 . GLN   A 253 ? 0.31246 0.39935 0.31153 0.06830  -0.00415 0.01270  252 GLN   A OE1 
1733 N NE2 . GLN   A 253 ? 0.24869 0.36345 0.26714 0.05568  -0.00507 0.00290  252 GLN   A NE2 
1734 N N   . ALA   A 254 ? 0.30364 0.44196 0.31338 0.03003  -0.01226 -0.01186 253 ALA   A N   
1735 C CA  . ALA   A 254 ? 0.32867 0.48695 0.34530 0.02115  -0.01490 -0.01962 253 ALA   A CA  
1736 C C   . ALA   A 254 ? 0.32252 0.49960 0.34790 0.02278  -0.01645 -0.01871 253 ALA   A C   
1737 O O   . ALA   A 254 ? 0.29128 0.46044 0.32000 0.02756  -0.01416 -0.01488 253 ALA   A O   
1738 C CB  . ALA   A 254 ? 0.35082 0.49467 0.37098 0.00974  -0.01261 -0.02762 253 ALA   A CB  
1739 N N   . ASP   A 255 ? 0.30281 0.50696 0.33196 0.01791  -0.02026 -0.02296 254 ASP   A N   
1740 C CA  . ASP   A 255 ? 0.29647 0.52522 0.33484 0.01849  -0.02195 -0.02253 254 ASP   A CA  
1741 C C   . ASP   A 255 ? 0.30515 0.52522 0.35177 0.00943  -0.01882 -0.02600 254 ASP   A C   
1742 O O   . ASP   A 255 ? 0.35851 0.58971 0.41176 0.01326  -0.01794 -0.02303 254 ASP   A O   
1743 C CB  . ASP   A 255 ? 0.34266 0.60345 0.38340 0.01173  -0.02687 -0.02777 254 ASP   A CB  
1744 C CG  . ASP   A 255 ? 0.50823 0.79708 0.54819 0.02473  -0.03089 -0.02129 254 ASP   A CG  
1745 O OD1 . ASP   A 255 ? 0.46344 0.74415 0.50004 0.03979  -0.02962 -0.01263 254 ASP   A OD1 
1746 O OD2 . ASP   A 255 ? 0.50624 0.82504 0.54815 0.02003  -0.03550 -0.02500 254 ASP   A OD2 
1747 N N   . ASP   A 256 ? 0.26986 0.47081 0.31572 -0.00207 -0.01701 -0.03211 255 ASP   A N   
1748 C CA  . ASP   A 256 ? 0.32880 0.52045 0.38094 -0.01150 -0.01437 -0.03488 255 ASP   A CA  
1749 C C   . ASP   A 256 ? 0.26557 0.42871 0.31573 -0.00673 -0.01026 -0.03079 255 ASP   A C   
1750 O O   . ASP   A 256 ? 0.26970 0.42192 0.32353 -0.01395 -0.00797 -0.03227 255 ASP   A O   
1751 C CB  . ASP   A 256 ? 0.33979 0.52660 0.39175 -0.02707 -0.01500 -0.04402 255 ASP   A CB  
1752 C CG  . ASP   A 256 ? 0.47536 0.63756 0.51952 -0.02749 -0.01379 -0.04744 255 ASP   A CG  
1753 O OD1 . ASP   A 256 ? 0.43702 0.59057 0.47582 -0.01719 -0.01302 -0.04290 255 ASP   A OD1 
1754 O OD2 . ASP   A 256 ? 0.51320 0.66465 0.55616 -0.03852 -0.01342 -0.05499 255 ASP   A OD2 
1755 N N   . PHE   A 257 ? 0.23525 0.38670 0.27916 0.00461  -0.00938 -0.02536 256 PHE   A N   
1756 C CA  . PHE   A 257 ? 0.22192 0.34930 0.26380 0.00881  -0.00583 -0.02153 256 PHE   A CA  
1757 C C   . PHE   A 257 ? 0.23062 0.36162 0.27170 0.02079  -0.00499 -0.01482 256 PHE   A C   
1758 O O   . PHE   A 257 ? 0.23884 0.37635 0.27494 0.03040  -0.00655 -0.01079 256 PHE   A O   
1759 C CB  . PHE   A 257 ? 0.26378 0.37099 0.29816 0.01047  -0.00473 -0.02126 256 PHE   A CB  
1760 C CG  . PHE   A 257 ? 0.22827 0.31446 0.26015 0.01493  -0.00163 -0.01696 256 PHE   A CG  
1761 C CD1 . PHE   A 257 ? 0.25279 0.32718 0.28879 0.00965  0.00045  -0.01838 256 PHE   A CD1 
1762 C CD2 . PHE   A 257 ? 0.25739 0.33540 0.28202 0.02371  -0.00090 -0.01134 256 PHE   A CD2 
1763 C CE1 . PHE   A 257 ? 0.24719 0.30475 0.28072 0.01309  0.00286  -0.01486 256 PHE   A CE1 
1764 C CE2 . PHE   A 257 ? 0.25659 0.31545 0.27841 0.02605  0.00184  -0.00826 256 PHE   A CE2 
1765 C CZ  . PHE   A 257 ? 0.26672 0.31696 0.29334 0.02082  0.00354  -0.01029 256 PHE   A CZ  
1766 N N   . TRP   A 258 ? 0.20767 0.33335 0.25253 0.02071  -0.00241 -0.01357 257 TRP   A N   
1767 C CA  . TRP   A 258 ? 0.23778 0.35662 0.27909 0.03223  -0.00048 -0.00819 257 TRP   A CA  
1768 C C   . TRP   A 258 ? 0.24455 0.34982 0.28801 0.02834  0.00278  -0.00847 257 TRP   A C   
1769 O O   . TRP   A 258 ? 0.22313 0.32739 0.27138 0.01763  0.00325  -0.01178 257 TRP   A O   
1770 C CB  . TRP   A 258 ? 0.23289 0.37633 0.27696 0.04181  -0.00187 -0.00566 257 TRP   A CB  
1771 C CG  . TRP   A 258 ? 0.28108 0.44539 0.33486 0.03761  -0.00106 -0.00770 257 TRP   A CG  
1772 C CD1 . TRP   A 258 ? 0.31607 0.48340 0.37195 0.04379  0.00184  -0.00577 257 TRP   A CD1 
1773 C CD2 . TRP   A 258 ? 0.26659 0.45313 0.32868 0.02567  -0.00289 -0.01222 257 TRP   A CD2 
1774 N NE1 . TRP   A 258 ? 0.26896 0.46089 0.33452 0.03650  0.00209  -0.00824 257 TRP   A NE1 
1775 C CE2 . TRP   A 258 ? 0.22458 0.42812 0.29405 0.02466  -0.00087 -0.01209 257 TRP   A CE2 
1776 C CE3 . TRP   A 258 ? 0.31513 0.50870 0.37833 0.01515  -0.00586 -0.01684 257 TRP   A CE3 
1777 C CZ2 . TRP   A 258 ? 0.34408 0.57122 0.42227 0.01204  -0.00165 -0.01579 257 TRP   A CZ2 
1778 C CZ3 . TRP   A 258 ? 0.31177 0.52674 0.38293 0.00284  -0.00689 -0.02121 257 TRP   A CZ3 
1779 C CH2 . TRP   A 258 ? 0.28755 0.51920 0.36625 0.00085  -0.00480 -0.02032 257 TRP   A CH2 
1780 N N   . CYS   A 259 ? 0.21740 0.31037 0.25577 0.03714  0.00499  -0.00486 258 CYS   A N   
1781 C CA  A CYS   A 259 ? 0.21643 0.29450 0.25422 0.03484  0.00800  -0.00470 258 CYS   A CA  
1782 C CA  B CYS   A 259 ? 0.21452 0.29319 0.25257 0.03463  0.00796  -0.00478 258 CYS   A CA  
1783 C C   . CYS   A 259 ? 0.24137 0.32741 0.27919 0.04375  0.01004  -0.00292 258 CYS   A C   
1784 O O   . CYS   A 259 ? 0.33372 0.41665 0.36542 0.05538  0.01016  -0.00025 258 CYS   A O   
1785 C CB  A CYS   A 259 ? 0.28678 0.33923 0.31620 0.03619  0.00905  -0.00314 258 CYS   A CB  
1786 C CB  B CYS   A 259 ? 0.28228 0.33538 0.31248 0.03483  0.00886  -0.00356 258 CYS   A CB  
1787 S SG  A CYS   A 259 ? 0.30021 0.34137 0.32922 0.02725  0.00794  -0.00540 258 CYS   A SG  
1788 S SG  B CYS   A 259 ? 0.26325 0.29957 0.29253 0.03018  0.01156  -0.00381 258 CYS   A SG  
1789 N N   . GLU   A 260 ? 0.22841 0.32317 0.27192 0.03884  0.01194  -0.00420 259 GLU   A N   
1790 C CA  . GLU   A 260 ? 0.24220 0.34502 0.28540 0.04746  0.01464  -0.00326 259 GLU   A CA  
1791 C C   . GLU   A 260 ? 0.23293 0.31577 0.27086 0.04572  0.01757  -0.00326 259 GLU   A C   
1792 O O   . GLU   A 260 ? 0.22001 0.29215 0.25865 0.03553  0.01749  -0.00386 259 GLU   A O   
1793 C CB  . GLU   A 260 ? 0.28403 0.41690 0.33735 0.04350  0.01518  -0.00456 259 GLU   A CB  
1794 C CG  . GLU   A 260 ? 0.33190 0.49080 0.38999 0.04969  0.01260  -0.00437 259 GLU   A CG  
1795 C CD  . GLU   A 260 ? 0.38241 0.57361 0.45162 0.04183  0.01270  -0.00621 259 GLU   A CD  
1796 O OE1 . GLU   A 260 ? 0.38272 0.57871 0.45480 0.03722  0.01603  -0.00658 259 GLU   A OE1 
1797 O OE2 . GLU   A 260 ? 0.37979 0.59243 0.45434 0.03940  0.00945  -0.00728 259 GLU   A OE2 
1798 N N   . GLY   A 261 ? 0.24652 0.32475 0.27861 0.05621  0.02009  -0.00280 260 GLY   A N   
1799 C CA  . GLY   A 261 ? 0.24802 0.31096 0.27478 0.05412  0.02287  -0.00359 260 GLY   A CA  
1800 C C   . GLY   A 261 ? 0.26575 0.34477 0.29897 0.04710  0.02500  -0.00438 260 GLY   A C   
1801 O O   . GLY   A 261 ? 0.25689 0.36117 0.29788 0.04722  0.02557  -0.00463 260 GLY   A O   
1802 N N   . GLU   A 262 ? 0.21987 0.28535 0.24956 0.04034  0.02616  -0.00440 261 GLU   A N   
1803 C CA  . GLU   A 262 ? 0.24302 0.32001 0.27540 0.03471  0.02883  -0.00430 261 GLU   A CA  
1804 C C   . GLU   A 262 ? 0.24139 0.30118 0.26436 0.03587  0.03078  -0.00495 261 GLU   A C   
1805 O O   . GLU   A 262 ? 0.25181 0.29046 0.26788 0.03711  0.02939  -0.00534 261 GLU   A O   
1806 C CB  . GLU   A 262 ? 0.26925 0.35109 0.30843 0.02080  0.02734  -0.00270 261 GLU   A CB  
1807 C CG  . GLU   A 262 ? 0.28018 0.34022 0.31611 0.01353  0.02525  -0.00149 261 GLU   A CG  
1808 C CD  . GLU   A 262 ? 0.32280 0.38616 0.36365 0.00114  0.02464  0.00034  261 GLU   A CD  
1809 O OE1 . GLU   A 262 ? 0.29444 0.36261 0.33447 -0.00379 0.02691  0.00236  261 GLU   A OE1 
1810 O OE2 . GLU   A 262 ? 0.30334 0.36328 0.34770 -0.00386 0.02209  -0.00023 261 GLU   A OE2 
1811 N N   . PRO   A 263 ? 0.25325 0.32328 0.27521 0.03529  0.03413  -0.00537 262 PRO   A N   
1812 C CA  . PRO   A 263 ? 0.25418 0.30954 0.26580 0.03711  0.03601  -0.00692 262 PRO   A CA  
1813 C C   . PRO   A 263 ? 0.25531 0.29322 0.26389 0.02771  0.03340  -0.00502 262 PRO   A C   
1814 O O   . PRO   A 263 ? 0.27315 0.31387 0.28750 0.01857  0.03160  -0.00195 262 PRO   A O   
1815 C CB  . PRO   A 263 ? 0.28128 0.35616 0.29383 0.03640  0.04014  -0.00725 262 PRO   A CB  
1816 C CG  . PRO   A 263 ? 0.29886 0.39939 0.32143 0.03925  0.04106  -0.00700 262 PRO   A CG  
1817 C CD  . PRO   A 263 ? 0.26702 0.36484 0.29649 0.03394  0.03670  -0.00504 262 PRO   A CD  
1818 N N   . TYR   A 264 ? 0.25682 0.27644 0.25572 0.03036  0.03320  -0.00709 263 TYR   A N   
1819 C CA  . TYR   A 264 ? 0.26993 0.27629 0.26526 0.02269  0.03085  -0.00571 263 TYR   A CA  
1820 C C   . TYR   A 264 ? 0.26914 0.28076 0.25978 0.01889  0.03279  -0.00524 263 TYR   A C   
1821 O O   . TYR   A 264 ? 0.27266 0.28442 0.25551 0.02417  0.03580  -0.00889 263 TYR   A O   
1822 C CB  . TYR   A 264 ? 0.25643 0.24331 0.24333 0.02584  0.02976  -0.00844 263 TYR   A CB  
1823 C CG  . TYR   A 264 ? 0.27287 0.24953 0.25446 0.01916  0.02788  -0.00829 263 TYR   A CG  
1824 C CD1 . TYR   A 264 ? 0.24352 0.22173 0.23117 0.01203  0.02483  -0.00454 263 TYR   A CD1 
1825 C CD2 . TYR   A 264 ? 0.29098 0.25705 0.26102 0.02027  0.02909  -0.01221 263 TYR   A CD2 
1826 C CE1 . TYR   A 264 ? 0.27231 0.24467 0.25586 0.00695  0.02271  -0.00397 263 TYR   A CE1 
1827 C CE2 . TYR   A 264 ? 0.30710 0.26733 0.27266 0.01335  0.02686  -0.01220 263 TYR   A CE2 
1828 C CZ  . TYR   A 264 ? 0.27495 0.24007 0.24797 0.00717  0.02356  -0.00769 263 TYR   A CZ  
1829 O OH  . TYR   A 264 ? 0.30316 0.26601 0.27269 0.00137  0.02091  -0.00712 263 TYR   A OH  
1830 N N   . PRO   A 265 ? 0.24901 0.26413 0.24289 0.01043  0.03132  -0.00085 264 PRO   A N   
1831 C CA  . PRO   A 265 ? 0.27007 0.29209 0.25888 0.00660  0.03323  0.00084  264 PRO   A CA  
1832 C C   . PRO   A 265 ? 0.30895 0.31993 0.28889 0.00403  0.03127  0.00063  264 PRO   A C   
1833 O O   . PRO   A 265 ? 0.30471 0.32172 0.27890 0.00111  0.03263  0.00206  264 PRO   A O   
1834 C CB  . PRO   A 265 ? 0.31065 0.34016 0.30675 -0.00151 0.03235  0.00685  264 PRO   A CB  
1835 C CG  . PRO   A 265 ? 0.29592 0.31352 0.29729 -0.00300 0.02825  0.00792  264 PRO   A CG  
1836 C CD  . PRO   A 265 ? 0.26979 0.28409 0.27205 0.00456  0.02834  0.00304  264 PRO   A CD  
1837 N N   . GLY   A 266 ? 0.26791 0.26521 0.24638 0.00439  0.02816  -0.00096 265 GLY   A N   
1838 C CA  . GLY   A 266 ? 0.29131 0.28200 0.26348 0.00034  0.02544  -0.00047 265 GLY   A CA  
1839 C C   . GLY   A 266 ? 0.27861 0.26287 0.23898 0.00241  0.02685  -0.00662 265 GLY   A C   
1840 O O   . GLY   A 266 ? 0.30064 0.28359 0.25643 0.00835  0.03046  -0.01145 265 GLY   A O   
1841 N N   . PRO   A 267 ? 0.31422 0.29437 0.26892 -0.00231 0.02390  -0.00680 266 PRO   A N   
1842 C CA  . PRO   A 267 ? 0.34716 0.31941 0.28929 -0.00253 0.02474  -0.01350 266 PRO   A CA  
1843 C C   . PRO   A 267 ? 0.32972 0.28718 0.26900 0.00173  0.02616  -0.01881 266 PRO   A C   
1844 O O   . PRO   A 267 ? 0.33805 0.29011 0.28403 0.00159  0.02431  -0.01699 266 PRO   A O   
1845 C CB  . PRO   A 267 ? 0.38617 0.35871 0.32649 -0.00954 0.01997  -0.01178 266 PRO   A CB  
1846 C CG  . PRO   A 267 ? 0.36661 0.34918 0.31657 -0.01119 0.01742  -0.00335 266 PRO   A CG  
1847 C CD  . PRO   A 267 ? 0.30914 0.29146 0.26894 -0.00728 0.01938  -0.00122 266 PRO   A CD  
1848 N N   . LYS   A 268 ? 0.37573 0.32540 0.30362 0.00575  0.02959  -0.02543 267 LYS   A N   
1849 C CA  . LYS   A 268 ? 0.40771 0.34062 0.33098 0.01135  0.03141  -0.02973 267 LYS   A CA  
1850 C C   . LYS   A 268 ? 0.46006 0.37596 0.37454 0.00462  0.02912  -0.03334 267 LYS   A C   
1851 O O   . LYS   A 268 ? 0.47193 0.38921 0.38016 -0.00303 0.02716  -0.03541 267 LYS   A O   
1852 C CB  . LYS   A 268 ? 0.42272 0.35293 0.33727 0.02070  0.03654  -0.03535 267 LYS   A CB  
1853 C CG  . LYS   A 268 ? 0.48281 0.43491 0.40514 0.02496  0.03915  -0.03229 267 LYS   A CG  
1854 C CD  . LYS   A 268 ? 0.42343 0.38550 0.36089 0.02714  0.03809  -0.02611 267 LYS   A CD  
1855 C CE  . LYS   A 268 ? 0.39175 0.37713 0.33711 0.02818  0.04055  -0.02273 267 LYS   A CE  
1856 N NZ  . LYS   A 268 ? 0.32861 0.32338 0.28831 0.02503  0.03814  -0.01626 267 LYS   A NZ  
1857 N N   . VAL   A 269 ? 0.38724 0.28859 0.30127 0.00671  0.02920  -0.03361 268 VAL   A N   
1858 C CA  . VAL   A 269 ? 0.38575 0.26900 0.29031 -0.00039 0.02785  -0.03702 268 VAL   A CA  
1859 C C   . VAL   A 269 ? 0.48308 0.34463 0.37080 0.00451  0.03169  -0.04444 268 VAL   A C   
1860 O O   . VAL   A 269 ? 0.54183 0.39677 0.42813 0.01588  0.03489  -0.04483 268 VAL   A O   
1861 C CB  . VAL   A 269 ? 0.40796 0.28668 0.31995 -0.00184 0.02607  -0.03257 268 VAL   A CB  
1862 C CG1 . VAL   A 269 ? 0.48166 0.33985 0.38211 -0.00960 0.02566  -0.03599 268 VAL   A CG1 
1863 C CG2 . VAL   A 269 ? 0.42782 0.32629 0.35467 -0.00674 0.02236  -0.02666 268 VAL   A CG2 
1864 N N   . PHE   A 270 ? 0.46837 0.31954 0.34295 -0.00360 0.03129  -0.05059 269 PHE   A N   
1865 C CA  A PHE   A 270 ? 0.54972 0.37827 0.40534 -0.00074 0.03488  -0.05941 269 PHE   A CA  
1866 C CA  B PHE   A 270 ? 0.54913 0.37720 0.40518 0.00001  0.03501  -0.05910 269 PHE   A CA  
1867 C C   . PHE   A 270 ? 0.65214 0.45418 0.49589 -0.00926 0.03419  -0.06252 269 PHE   A C   
1868 O O   . PHE   A 270 ? 0.61638 0.42418 0.46365 -0.02226 0.03040  -0.06076 269 PHE   A O   
1869 C CB  A PHE   A 270 ? 0.58592 0.42285 0.43312 -0.00564 0.03498  -0.06534 269 PHE   A CB  
1870 C CB  B PHE   A 270 ? 0.58189 0.41755 0.42905 -0.00222 0.03602  -0.06542 269 PHE   A CB  
1871 C CG  A PHE   A 270 ? 0.62046 0.48024 0.47467 0.00223  0.03687  -0.06335 269 PHE   A CG  
1872 C CG  B PHE   A 270 ? 0.61597 0.46259 0.46277 -0.01698 0.03151  -0.06583 269 PHE   A CG  
1873 C CD1 A PHE   A 270 ? 0.52483 0.40987 0.39540 0.00004  0.03401  -0.05498 269 PHE   A CD1 
1874 C CD1 B PHE   A 270 ? 0.66924 0.49860 0.50274 -0.02846 0.03012  -0.07203 269 PHE   A CD1 
1875 C CD2 A PHE   A 270 ? 0.72272 0.57850 0.56579 0.01083  0.04169  -0.07023 269 PHE   A CD2 
1876 C CD2 B PHE   A 270 ? 0.62726 0.50162 0.48608 -0.01939 0.02862  -0.06000 269 PHE   A CD2 
1877 C CE1 A PHE   A 270 ? 0.61691 0.52198 0.49264 0.00520  0.03597  -0.05261 269 PHE   A CE1 
1878 C CE1 B PHE   A 270 ? 0.63150 0.47504 0.46533 -0.04184 0.02557  -0.07252 269 PHE   A CE1 
1879 C CE2 A PHE   A 270 ? 0.71589 0.59511 0.56506 0.01653  0.04384  -0.06824 269 PHE   A CE2 
1880 C CE2 B PHE   A 270 ? 0.65396 0.54021 0.51232 -0.03118 0.02408  -0.05983 269 PHE   A CE2 
1881 C CZ  A PHE   A 270 ? 0.68948 0.59309 0.55486 0.01290  0.04094  -0.05906 269 PHE   A CZ  
1882 C CZ  B PHE   A 270 ? 0.61835 0.49117 0.46488 -0.04225 0.02241  -0.06623 269 PHE   A CZ  
1883 N N   . PRO   A 271 ? 0.63508 0.40809 0.46399 -0.00262 0.03784  -0.06712 270 PRO   A N   
1884 C CA  . PRO   A 271 ? 0.77556 0.51925 0.58974 -0.01260 0.03765  -0.07048 270 PRO   A CA  
1885 C C   . PRO   A 271 ? 0.74197 0.48353 0.54517 -0.02809 0.03589  -0.07799 270 PRO   A C   
1886 O O   . PRO   A 271 ? 0.73911 0.47719 0.53107 -0.02597 0.03789  -0.08588 270 PRO   A O   
1887 C CB  . PRO   A 271 ? 0.70894 0.42144 0.50717 0.00072  0.04250  -0.07472 270 PRO   A CB  
1888 C CG  . PRO   A 271 ? 0.76580 0.49633 0.57689 0.01814  0.04423  -0.06993 270 PRO   A CG  
1889 C CD  . PRO   A 271 ? 0.66025 0.42716 0.48685 0.01526  0.04219  -0.06789 270 PRO   A CD  
1890 O OXT . PRO   A 271 ? 0.93260 0.67792 0.73787 -0.04319 0.03242  -0.07664 270 PRO   A OXT 
1906 N N   . ILE   B 3   ? 0.38657 0.40694 0.46401 0.06796  -0.03448 0.00384  2   ILE   B N   
1907 C CA  . ILE   B 3   ? 0.38853 0.39600 0.44896 0.06384  -0.03249 0.00326  2   ILE   B CA  
1908 C C   . ILE   B 3   ? 0.44043 0.44103 0.49838 0.06828  -0.02614 0.00187  2   ILE   B C   
1909 O O   . ILE   B 3   ? 0.45261 0.45223 0.51610 0.07517  -0.02675 0.00286  2   ILE   B O   
1910 C CB  . ILE   B 3   ? 0.47796 0.47561 0.52660 0.06256  -0.03996 0.00605  2   ILE   B CB  
1911 C CG1 . ILE   B 3   ? 0.51826 0.52372 0.57020 0.05815  -0.04612 0.00728  2   ILE   B CG1 
1912 C CG2 . ILE   B 3   ? 0.50585 0.48971 0.53678 0.05847  -0.03771 0.00541  2   ILE   B CG2 
1913 C CD1 . ILE   B 3   ? 0.51284 0.51707 0.55580 0.04976  -0.04495 0.00598  2   ILE   B CD1 
1914 N N   . VAL   B 4   ? 0.38448 0.38069 0.43451 0.06440  -0.01993 -0.00048 3   VAL   B N   
1915 C CA  . VAL   B 4   ? 0.40144 0.39026 0.44729 0.06779  -0.01369 -0.00202 3   VAL   B CA  
1916 C C   . VAL   B 4   ? 0.38798 0.36355 0.41587 0.06306  -0.01253 -0.00249 3   VAL   B C   
1917 O O   . VAL   B 4   ? 0.39361 0.36923 0.41504 0.05616  -0.01244 -0.00318 3   VAL   B O   
1918 C CB  . VAL   B 4   ? 0.43122 0.42928 0.48746 0.06872  -0.00581 -0.00487 3   VAL   B CB  
1919 C CG1 . VAL   B 4   ? 0.46617 0.46979 0.52125 0.06144  -0.00313 -0.00659 3   VAL   B CG1 
1920 C CG2 . VAL   B 4   ? 0.54520 0.53504 0.59590 0.07181  0.00063  -0.00655 3   VAL   B CG2 
1921 N N   . LYS   B 5   ? 0.40908 0.37317 0.42888 0.06676  -0.01189 -0.00203 4   LYS   B N   
1922 C CA  . LYS   B 5   ? 0.45259 0.40371 0.45564 0.06286  -0.01001 -0.00272 4   LYS   B CA  
1923 C C   . LYS   B 5   ? 0.40080 0.35255 0.40330 0.06173  -0.00116 -0.00598 4   LYS   B C   
1924 O O   . LYS   B 5   ? 0.47498 0.42811 0.48390 0.06713  0.00339  -0.00714 4   LYS   B O   
1925 C CB  . LYS   B 5   ? 0.52593 0.46447 0.52054 0.06718  -0.01289 -0.00095 4   LYS   B CB  
1926 C CG  . LYS   B 5   ? 0.60213 0.53918 0.59591 0.06799  -0.02178 0.00242  4   LYS   B CG  
1927 C CD  . LYS   B 5   ? 0.77374 0.69669 0.75646 0.07104  -0.02435 0.00411  4   LYS   B CD  
1928 C CE  . LYS   B 5   ? 0.92210 0.84420 0.90514 0.07258  -0.03310 0.00760  4   LYS   B CE  
1929 N NZ  . LYS   B 5   ? 1.01352 0.94980 1.01252 0.07477  -0.03607 0.00847  4   LYS   B NZ  
1930 N N   . THR   B 6   ? 0.38388 0.33516 0.37921 0.05474  0.00127  -0.00743 5   THR   B N   
1931 C CA  . THR   B 6   ? 0.38782 0.34081 0.38273 0.05279  0.00952  -0.01049 5   THR   B CA  
1932 C C   . THR   B 6   ? 0.38440 0.32471 0.36216 0.04826  0.01166  -0.01139 5   THR   B C   
1933 O O   . THR   B 6   ? 0.41096 0.34402 0.37796 0.04430  0.00679  -0.00989 5   THR   B O   
1934 C CB  . THR   B 6   ? 0.37491 0.34066 0.37844 0.04825  0.01158  -0.01177 5   THR   B CB  
1935 O OG1 . THR   B 6   ? 0.36366 0.32700 0.35820 0.04103  0.00801  -0.01110 5   THR   B OG1 
1936 C CG2 . THR   B 6   ? 0.38488 0.36345 0.40514 0.05201  0.00861  -0.01070 5   THR   B CG2 
1937 N N   . PHE   B 7   ? 0.39720 0.33507 0.37259 0.04887  0.01905  -0.01389 6   PHE   B N   
1938 C CA  . PHE   B 7   ? 0.40460 0.33171 0.36460 0.04424  0.02203  -0.01517 6   PHE   B CA  
1939 C C   . PHE   B 7   ? 0.41292 0.34355 0.36898 0.03624  0.02250  -0.01591 6   PHE   B C   
1940 O O   . PHE   B 7   ? 0.36700 0.28835 0.30917 0.03132  0.02263  -0.01621 6   PHE   B O   
1941 C CB  . PHE   B 7   ? 0.39403 0.31924 0.35377 0.04682  0.03021  -0.01787 6   PHE   B CB  
1942 C CG  . PHE   B 7   ? 0.40964 0.33168 0.37356 0.05468  0.03089  -0.01758 6   PHE   B CG  
1943 C CD1 . PHE   B 7   ? 0.50922 0.41961 0.46439 0.05719  0.02681  -0.01589 6   PHE   B CD1 
1944 C CD2 . PHE   B 7   ? 0.44739 0.37807 0.42405 0.05953  0.03576  -0.01902 6   PHE   B CD2 
1945 C CE1 . PHE   B 7   ? 0.52227 0.42971 0.48145 0.06446  0.02758  -0.01566 6   PHE   B CE1 
1946 C CE2 . PHE   B 7   ? 0.51892 0.44671 0.49957 0.06680  0.03653  -0.01882 6   PHE   B CE2 
1947 C CZ  . PHE   B 7   ? 0.52934 0.44549 0.50126 0.06923  0.03243  -0.01715 6   PHE   B CZ  
1948 N N   . TRP   B 8   ? 0.36306 0.30686 0.33116 0.03489  0.02301  -0.01630 7   TRP   B N   
1949 C CA  . TRP   B 8   ? 0.34868 0.29739 0.31521 0.02796  0.02598  -0.01779 7   TRP   B CA  
1950 C C   . TRP   B 8   ? 0.34743 0.30177 0.31604 0.02336  0.01992  -0.01618 7   TRP   B C   
1951 O O   . TRP   B 8   ? 0.34208 0.29701 0.30529 0.01671  0.02087  -0.01694 7   TRP   B O   
1952 C CB  . TRP   B 8   ? 0.33911 0.29875 0.31767 0.02963  0.03314  -0.02011 7   TRP   B CB  
1953 C CG  . TRP   B 8   ? 0.33915 0.30901 0.33417 0.03605  0.03209  -0.01945 7   TRP   B CG  
1954 C CD1 . TRP   B 8   ? 0.38359 0.35247 0.38412 0.04337  0.03385  -0.01954 7   TRP   B CD1 
1955 C CD2 . TRP   B 8   ? 0.33484 0.31747 0.34293 0.03560  0.02909  -0.01864 7   TRP   B CD2 
1956 N NE1 . TRP   B 8   ? 0.41948 0.39964 0.43559 0.04747  0.03202  -0.01876 7   TRP   B NE1 
1957 C CE2 . TRP   B 8   ? 0.33935 0.32813 0.36040 0.04284  0.02912  -0.01823 7   TRP   B CE2 
1958 C CE3 . TRP   B 8   ? 0.34976 0.33922 0.35990 0.02975  0.02642  -0.01828 7   TRP   B CE3 
1959 C CZ2 . TRP   B 8   ? 0.41196 0.41354 0.44794 0.04438  0.02661  -0.01749 7   TRP   B CZ2 
1960 C CZ3 . TRP   B 8   ? 0.36403 0.36619 0.38900 0.03129  0.02384  -0.01757 7   TRP   B CZ3 
1961 C CH2 . TRP   B 8   ? 0.40617 0.41426 0.44385 0.03854  0.02398  -0.01720 7   TRP   B CH2 
1962 C C10 . A1BDE B 9   ? 0.36581 0.33867 0.32946 -0.00390 0.02286  -0.01916 8   A1BDE B C10 
1963 C C13 . A1BDE B 9   ? 0.39451 0.34371 0.33572 -0.00125 0.02534  -0.01943 8   A1BDE B C13 
1964 C CG  . A1BDE B 9   ? 0.34183 0.32577 0.33602 0.01730  0.01150  -0.01445 8   A1BDE B CG  
1965 C CE  . A1BDE B 9   ? 0.46559 0.44905 0.44663 0.00283  0.01215  -0.01570 8   A1BDE B CE  
1966 C CD  . A1BDE B 9   ? 0.34847 0.32985 0.33361 0.00985  0.00674  -0.01349 8   A1BDE B CD  
1967 C CB  . A1BDE B 9   ? 0.34649 0.32369 0.33942 0.02354  0.00672  -0.01234 8   A1BDE B CB  
1968 C CA  . A1BDE B 9   ? 0.35398 0.31500 0.32956 0.02273  0.00649  -0.01198 8   A1BDE B CA  
1969 C C   . A1BDE B 9   ? 0.36488 0.32004 0.33758 0.02595  -0.00123 -0.00908 8   A1BDE B C   
1970 C C12 . A1BDE B 9   ? 0.36576 0.32837 0.31756 -0.00478 0.02863  -0.02080 8   A1BDE B C12 
1971 N N   . A1BDE B 9   ? 0.35398 0.31077 0.32874 0.02692  0.01277  -0.01363 8   A1BDE B N   
1972 N NZ  . A1BDE B 9   ? 0.40191 0.37487 0.37149 0.00252  0.01766  -0.01718 8   A1BDE B NZ  
1973 N N14 . A1BDE B 9   ? 0.34045 0.30073 0.28308 -0.01262 0.02954  -0.02150 8   A1BDE B N14 
1974 O O   . A1BDE B 9   ? 0.36648 0.32577 0.34173 0.02406  -0.00745 -0.00730 8   A1BDE B O   
1975 O O11 . A1BDE B 9   ? 0.37736 0.35830 0.34553 -0.00852 0.02267  -0.01954 8   A1BDE B O11 
1976 O O15 . A1BDE B 9   ? 0.36051 0.30232 0.29055 -0.00589 0.01939  -0.01776 8   A1BDE B O15 
1977 N N   . GLY   B 10  ? 0.37316 0.31593 0.33675 0.02976  -0.00087 -0.00861 9   GLY   B N   
1978 C CA  . GLY   B 10  ? 0.38352 0.32106 0.34448 0.03254  -0.00855 -0.00564 9   GLY   B CA  
1979 C C   . GLY   B 10  ? 0.39403 0.34136 0.36990 0.03803  -0.01257 -0.00403 9   GLY   B C   
1980 O O   . GLY   B 10  ? 0.38064 0.33676 0.36909 0.04201  -0.00865 -0.00524 9   GLY   B O   
1981 N N   . SER   B 11  ? 0.39258 0.33833 0.36704 0.03836  -0.02043 -0.00124 10  SER   B N   
1982 C CA  . SER   B 11  ? 0.41811 0.37344 0.40641 0.04303  -0.02503 0.00049  10  SER   B CA  
1983 C C   . SER   B 11  ? 0.38893 0.35827 0.38803 0.03937  -0.02471 -0.00046 10  SER   B C   
1984 O O   . SER   B 11  ? 0.41775 0.38898 0.41362 0.03397  -0.02895 0.00035  10  SER   B O   
1985 C CB  . SER   B 11  ? 0.49039 0.43991 0.47328 0.04394  -0.03356 0.00374  10  SER   B CB  
1986 O OG  . SER   B 11  ? 0.59287 0.52931 0.56591 0.04740  -0.03393 0.00471  10  SER   B OG  
1987 N N   . HIS   B 12  ? 0.37802 0.35734 0.39012 0.04225  -0.01961 -0.00222 11  HIS   B N   
1988 C CA  . HIS   B 12  ? 0.36766 0.35962 0.38920 0.03835  -0.01740 -0.00375 11  HIS   B CA  
1989 C C   . HIS   B 12  ? 0.36678 0.37132 0.40503 0.04255  -0.02055 -0.00276 11  HIS   B C   
1990 O O   . HIS   B 12  ? 0.36972 0.37591 0.41602 0.04942  -0.01969 -0.00242 11  HIS   B O   
1991 C CB  . HIS   B 12  ? 0.35902 0.35315 0.38227 0.03758  -0.00834 -0.00681 11  HIS   B CB  
1992 C CG  . HIS   B 12  ? 0.34824 0.35386 0.37894 0.03266  -0.00560 -0.00846 11  HIS   B CG  
1993 N ND1 . HIS   B 12  ? 0.34513 0.35033 0.36865 0.02514  -0.00746 -0.00854 11  HIS   B ND1 
1994 C CD2 . HIS   B 12  ? 0.33989 0.35759 0.38453 0.03414  -0.00102 -0.01011 11  HIS   B CD2 
1995 C CE1 . HIS   B 12  ? 0.33530 0.35183 0.36807 0.02219  -0.00411 -0.01018 11  HIS   B CE1 
1996 N NE2 . HIS   B 12  ? 0.33198 0.35636 0.37777 0.02757  -0.00025 -0.01111 11  HIS   B NE2 
1997 N N   . ARG   B 13  ? 0.36287 0.37620 0.40626 0.03840  -0.02424 -0.00234 12  ARG   B N   
1998 C CA  . ARG   B 13  ? 0.36085 0.38733 0.42075 0.04168  -0.02695 -0.00168 12  ARG   B CA  
1999 C C   . ARG   B 13  ? 0.34998 0.38717 0.42128 0.04149  -0.01976 -0.00436 12  ARG   B C   
2000 O O   . ARG   B 13  ? 0.34200 0.38470 0.41390 0.03562  -0.01758 -0.00583 12  ARG   B O   
2001 C CB  . ARG   B 13  ? 0.36175 0.39296 0.42225 0.03745  -0.03417 -0.00008 12  ARG   B CB  
2002 C CG  . ARG   B 13  ? 0.36225 0.40524 0.43852 0.04166  -0.03842 0.00114  12  ARG   B CG  
2003 C CD  . ARG   B 13  ? 0.35783 0.41006 0.43843 0.03615  -0.04249 0.00131  12  ARG   B CD  
2004 N NE  . ARG   B 13  ? 0.34665 0.40630 0.43131 0.03131  -0.03658 -0.00138 12  ARG   B NE  
2005 C CZ  . ARG   B 13  ? 0.34534 0.40337 0.42165 0.02379  -0.03629 -0.00221 12  ARG   B CZ  
2006 N NH1 . ARG   B 13  ? 0.34873 0.39772 0.41175 0.02010  -0.04142 -0.00065 12  ARG   B NH1 
2007 N NH2 . ARG   B 13  ? 0.33228 0.39768 0.41351 0.01992  -0.03058 -0.00464 12  ARG   B NH2 
2008 N N   . GLN   B 14  ? 0.34969 0.38946 0.42970 0.04793  -0.01576 -0.00504 13  GLN   B N   
2009 C CA  . GLN   B 14  ? 0.33991 0.38791 0.42902 0.04819  -0.00798 -0.00769 13  GLN   B CA  
2010 C C   . GLN   B 14  ? 0.33471 0.39799 0.44153 0.04990  -0.00910 -0.00775 13  GLN   B C   
2011 O O   . GLN   B 14  ? 0.34209 0.41172 0.46091 0.05562  -0.00630 -0.00827 13  GLN   B O   
2012 C CB  . GLN   B 14  ? 0.35187 0.39433 0.44039 0.05387  -0.00237 -0.00868 13  GLN   B CB  
2013 C CG  . GLN   B 14  ? 0.33314 0.37993 0.42479 0.05234  0.00640  -0.01162 13  GLN   B CG  
2014 C CD  . GLN   B 14  ? 0.33497 0.37412 0.42252 0.05681  0.01203  -0.01275 13  GLN   B CD  
2015 O OE1 . GLN   B 14  ? 0.40367 0.44285 0.49754 0.06361  0.01164  -0.01205 13  GLN   B OE1 
2016 N NE2 . GLN   B 14  ? 0.37193 0.40447 0.44880 0.05300  0.01729  -0.01452 13  GLN   B NE2 
2017 N N   . CYS   B 15  ? 0.33202 0.40110 0.44017 0.04471  -0.01329 -0.00726 14  CYS   B N   
2018 C CA  . CYS   B 15  ? 0.32736 0.41079 0.45130 0.04533  -0.01530 -0.00721 14  CYS   B CA  
2019 C C   . CYS   B 15  ? 0.33303 0.42006 0.45415 0.03810  -0.01952 -0.00691 14  CYS   B C   
2020 O O   . CYS   B 15  ? 0.32889 0.40668 0.43615 0.03386  -0.02289 -0.00596 14  CYS   B O   
2021 C CB  . CYS   B 15  ? 0.33486 0.42074 0.46724 0.05212  -0.02092 -0.00498 14  CYS   B CB  
2022 S SG  . CYS   B 15  ? 0.34723 0.42187 0.46667 0.05175  -0.03027 -0.00173 14  CYS   B SG  
2023 N N   . NH2   B 16  ? 0.31758 0.41808 0.45199 0.03675  -0.01945 -0.00770 15  NH2   B N   
# 
