data_9QYF
# 
_entry.id   9QYF 
# 
_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   9QYF         pdb_00009qyf 10.2210/pdb9qyf/pdb 
WWPDB D_1292147148 ?            ?                   
# 
_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       2025-05-28 
_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                        9QYF 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              G.A.Spyroulias@upatras.gr 
_pdbx_contact_author.name_first         Georgios 
_pdbx_contact_author.name_last          Spyroulias 
_pdbx_contact_author.name_mi            A. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1799-3312 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fourkiotis, K.N.' 1 0000-0002-5197-4142 
'Chikunova, A.'    2 0000-0002-2818-0539 
'Tsika, C.A.'      3 0000-0002-3723-0606 
'Kravvariti, P.K.' 4 0000-0001-7127-1666 
'Tsatsouli, A.S.'  5 ?                   
'Perrakis, A.'     6 0000-0002-1151-6227 
'Spyroulias, A.G.' 7 0000-0003-1799-3312 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Comparative analysis of hPARP9 macro domains' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fourkiotis, K.N.' 1 0000-0002-5197-4142 
primary 'Chikunova, A.'    2 0000-0002-2818-0539 
primary 'Tsika, C.A.'      3 0000-0002-3723-0606 
primary 'Kravvariti, P.K.' 4 0000-0001-7127-1666 
primary 'Tsatsouli, A.S.'  5 ?                   
primary 'Perrakis, A.'     6 0000-0002-1151-6227 
primary 'Spyroulias, A.G.' 7 0000-0003-1799-3312 
# 
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 'Protein mono-ADP-ribosyltransferase PARP9' 22232.867 1   2.4.2.- ? ? ? 
2 non-polymer syn ADENOSINE-5-DIPHOSPHORIBOSE 559.316   1   ?       ? ? ? 
3 non-polymer syn 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
559.316   1   ?       ? ? ? 
4 water       nat water 18.015    211 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'ADP-ribosyltransferase diphtheria toxin-like 9,ARTD9,B aggressive lymphoma protein,Poly [ADP-ribose] polymerase 9,PARP-9' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GAMATTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLV
TKGFNLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKH
QLTVKFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMATTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLV
TKGFNLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKH
QLTVKFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 ADENOSINE-5-DIPHOSPHORIBOSE APR 
3 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
AR6 
4 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   ALA n 
1 5   THR n 
1 6   THR n 
1 7   PRO n 
1 8   SER n 
1 9   PHE n 
1 10  ASN n 
1 11  ALA n 
1 12  MET n 
1 13  VAL n 
1 14  VAL n 
1 15  ASN n 
1 16  ASN n 
1 17  LEU n 
1 18  THR n 
1 19  LEU n 
1 20  GLN n 
1 21  ILE n 
1 22  VAL n 
1 23  GLN n 
1 24  GLY n 
1 25  HIS n 
1 26  ILE n 
1 27  GLU n 
1 28  TRP n 
1 29  GLN n 
1 30  THR n 
1 31  ALA n 
1 32  ASP n 
1 33  VAL n 
1 34  ILE n 
1 35  VAL n 
1 36  ASN n 
1 37  SER n 
1 38  VAL n 
1 39  ASN n 
1 40  PRO n 
1 41  HIS n 
1 42  ASP n 
1 43  ILE n 
1 44  THR n 
1 45  VAL n 
1 46  GLY n 
1 47  PRO n 
1 48  VAL n 
1 49  ALA n 
1 50  LYS n 
1 51  SER n 
1 52  ILE n 
1 53  LEU n 
1 54  GLN n 
1 55  GLN n 
1 56  ALA n 
1 57  GLY n 
1 58  VAL n 
1 59  GLU n 
1 60  MET n 
1 61  LYS n 
1 62  SER n 
1 63  GLU n 
1 64  PHE n 
1 65  LEU n 
1 66  ALA n 
1 67  THR n 
1 68  LYS n 
1 69  ALA n 
1 70  LYS n 
1 71  GLN n 
1 72  PHE n 
1 73  GLN n 
1 74  ARG n 
1 75  SER n 
1 76  GLN n 
1 77  LEU n 
1 78  VAL n 
1 79  LEU n 
1 80  VAL n 
1 81  THR n 
1 82  LYS n 
1 83  GLY n 
1 84  PHE n 
1 85  ASN n 
1 86  LEU n 
1 87  PHE n 
1 88  CYS n 
1 89  LYS n 
1 90  TYR n 
1 91  ILE n 
1 92  TYR n 
1 93  HIS n 
1 94  VAL n 
1 95  LEU n 
1 96  TRP n 
1 97  HIS n 
1 98  SER n 
1 99  GLU n 
1 100 PHE n 
1 101 PRO n 
1 102 LYS n 
1 103 PRO n 
1 104 GLN n 
1 105 ILE n 
1 106 LEU n 
1 107 LYS n 
1 108 HIS n 
1 109 ALA n 
1 110 MET n 
1 111 LYS n 
1 112 GLU n 
1 113 CYS n 
1 114 LEU n 
1 115 GLU n 
1 116 LYS n 
1 117 CYS n 
1 118 ILE n 
1 119 GLU n 
1 120 GLN n 
1 121 ASN n 
1 122 ILE n 
1 123 THR n 
1 124 SER n 
1 125 ILE n 
1 126 SER n 
1 127 PHE n 
1 128 PRO n 
1 129 ALA n 
1 130 LEU n 
1 131 GLY n 
1 132 THR n 
1 133 GLY n 
1 134 ASN n 
1 135 MET n 
1 136 GLU n 
1 137 ILE n 
1 138 LYS n 
1 139 LYS n 
1 140 GLU n 
1 141 THR n 
1 142 ALA n 
1 143 ALA n 
1 144 GLU n 
1 145 ILE n 
1 146 LEU n 
1 147 PHE n 
1 148 ASP n 
1 149 GLU n 
1 150 VAL n 
1 151 LEU n 
1 152 THR n 
1 153 PHE n 
1 154 ALA n 
1 155 LYS n 
1 156 ASP n 
1 157 HIS n 
1 158 VAL n 
1 159 LYS n 
1 160 HIS n 
1 161 GLN n 
1 162 LEU n 
1 163 THR n 
1 164 VAL n 
1 165 LYS n 
1 166 PHE n 
1 167 VAL n 
1 168 ILE n 
1 169 PHE n 
1 170 PRO n 
1 171 THR n 
1 172 ASP n 
1 173 LEU n 
1 174 GLU n 
1 175 ILE n 
1 176 TYR n 
1 177 LYS n 
1 178 ALA n 
1 179 PHE n 
1 180 SER n 
1 181 SER n 
1 182 GLU n 
1 183 MET n 
1 184 ALA n 
1 185 LYS n 
1 186 ARG n 
1 187 SER n 
1 188 LYS n 
1 189 MET n 
1 190 LEU n 
1 191 SER n 
1 192 LEU n 
1 193 ASN n 
1 194 ASN n 
1 195 TYR n 
1 196 SER n 
1 197 VAL 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                   197 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PARP9, BAL, BAL1' 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                           'C3 H7 N O2'        89.093  
APR non-polymer         . ADENOSINE-5-DIPHOSPHORIBOSE ?                           'C15 H23 N5 O14 P2' 559.316 
AR6 non-polymer         . 
;[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE
;
Adenosine-5-Diphosphoribose 'C15 H23 N5 O14 P2' 559.316 
ARG 'L-peptide linking' y ARGININE ?                           'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                           'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                           'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                           'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                           'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                           'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                           'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?                           'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?                           'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                           'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                           'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                           'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                           'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                           'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                           'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                           'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                           'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                           'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                           'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                           'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_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   GLY 1   301 ?   ?   ?   A . n 
A 1 2   ALA 2   302 ?   ?   ?   A . n 
A 1 3   MET 3   303 ?   ?   ?   A . n 
A 1 4   ALA 4   304 ?   ?   ?   A . n 
A 1 5   THR 5   305 ?   ?   ?   A . n 
A 1 6   THR 6   306 ?   ?   ?   A . n 
A 1 7   PRO 7   307 ?   ?   ?   A . n 
A 1 8   SER 8   308 308 SER SER A . n 
A 1 9   PHE 9   309 309 PHE PHE A . n 
A 1 10  ASN 10  310 310 ASN ASN A . n 
A 1 11  ALA 11  311 311 ALA ALA A . n 
A 1 12  MET 12  312 312 MET MET A . n 
A 1 13  VAL 13  313 313 VAL VAL A . n 
A 1 14  VAL 14  314 314 VAL VAL A . n 
A 1 15  ASN 15  315 315 ASN ASN A . n 
A 1 16  ASN 16  316 316 ASN ASN A . n 
A 1 17  LEU 17  317 317 LEU LEU A . n 
A 1 18  THR 18  318 318 THR THR A . n 
A 1 19  LEU 19  319 319 LEU LEU A . n 
A 1 20  GLN 20  320 320 GLN GLN A . n 
A 1 21  ILE 21  321 321 ILE ILE A . n 
A 1 22  VAL 22  322 322 VAL VAL A . n 
A 1 23  GLN 23  323 323 GLN GLN A . n 
A 1 24  GLY 24  324 324 GLY GLY A . n 
A 1 25  HIS 25  325 325 HIS HIS A . n 
A 1 26  ILE 26  326 326 ILE ILE A . n 
A 1 27  GLU 27  327 327 GLU GLU A . n 
A 1 28  TRP 28  328 328 TRP TRP A . n 
A 1 29  GLN 29  329 329 GLN GLN A . n 
A 1 30  THR 30  330 330 THR THR A . n 
A 1 31  ALA 31  331 331 ALA ALA A . n 
A 1 32  ASP 32  332 332 ASP ASP A . n 
A 1 33  VAL 33  333 333 VAL VAL A . n 
A 1 34  ILE 34  334 334 ILE ILE A . n 
A 1 35  VAL 35  335 335 VAL VAL A . n 
A 1 36  ASN 36  336 336 ASN ASN A . n 
A 1 37  SER 37  337 337 SER SER A . n 
A 1 38  VAL 38  338 338 VAL VAL A . n 
A 1 39  ASN 39  339 339 ASN ASN A . n 
A 1 40  PRO 40  340 340 PRO PRO A . n 
A 1 41  HIS 41  341 341 HIS HIS A . n 
A 1 42  ASP 42  342 342 ASP ASP A . n 
A 1 43  ILE 43  343 343 ILE ILE A . n 
A 1 44  THR 44  344 344 THR THR A . n 
A 1 45  VAL 45  345 345 VAL VAL A . n 
A 1 46  GLY 46  346 346 GLY GLY A . n 
A 1 47  PRO 47  347 347 PRO PRO A . n 
A 1 48  VAL 48  348 348 VAL VAL A . n 
A 1 49  ALA 49  349 349 ALA ALA A . n 
A 1 50  LYS 50  350 350 LYS LYS A . n 
A 1 51  SER 51  351 351 SER SER A . n 
A 1 52  ILE 52  352 352 ILE ILE A . n 
A 1 53  LEU 53  353 353 LEU LEU A . n 
A 1 54  GLN 54  354 354 GLN GLN A . n 
A 1 55  GLN 55  355 355 GLN GLN A . n 
A 1 56  ALA 56  356 356 ALA ALA A . n 
A 1 57  GLY 57  357 357 GLY GLY A . n 
A 1 58  VAL 58  358 358 VAL VAL A . n 
A 1 59  GLU 59  359 359 GLU GLU A . n 
A 1 60  MET 60  360 360 MET MET A . n 
A 1 61  LYS 61  361 361 LYS LYS A . n 
A 1 62  SER 62  362 362 SER SER A . n 
A 1 63  GLU 63  363 363 GLU GLU A . n 
A 1 64  PHE 64  364 364 PHE PHE A . n 
A 1 65  LEU 65  365 365 LEU LEU A . n 
A 1 66  ALA 66  366 366 ALA ALA A . n 
A 1 67  THR 67  367 367 THR THR A . n 
A 1 68  LYS 68  368 368 LYS LYS A . n 
A 1 69  ALA 69  369 369 ALA ALA A . n 
A 1 70  LYS 70  370 370 LYS LYS A . n 
A 1 71  GLN 71  371 371 GLN GLN A . n 
A 1 72  PHE 72  372 372 PHE PHE A . n 
A 1 73  GLN 73  373 373 GLN GLN A . n 
A 1 74  ARG 74  374 374 ARG ARG A . n 
A 1 75  SER 75  375 375 SER SER A . n 
A 1 76  GLN 76  376 376 GLN GLN A . n 
A 1 77  LEU 77  377 377 LEU LEU A . n 
A 1 78  VAL 78  378 378 VAL VAL A . n 
A 1 79  LEU 79  379 379 LEU LEU A . n 
A 1 80  VAL 80  380 380 VAL VAL A . n 
A 1 81  THR 81  381 381 THR THR A . n 
A 1 82  LYS 82  382 382 LYS LYS A . n 
A 1 83  GLY 83  383 383 GLY GLY A . n 
A 1 84  PHE 84  384 384 PHE PHE A . n 
A 1 85  ASN 85  385 385 ASN ASN A . n 
A 1 86  LEU 86  386 386 LEU LEU A . n 
A 1 87  PHE 87  387 387 PHE PHE A . n 
A 1 88  CYS 88  388 388 CYS CYS A . n 
A 1 89  LYS 89  389 389 LYS LYS A . n 
A 1 90  TYR 90  390 390 TYR TYR A . n 
A 1 91  ILE 91  391 391 ILE ILE A . n 
A 1 92  TYR 92  392 392 TYR TYR A . n 
A 1 93  HIS 93  393 393 HIS HIS A . n 
A 1 94  VAL 94  394 394 VAL VAL A . n 
A 1 95  LEU 95  395 395 LEU LEU A . n 
A 1 96  TRP 96  396 396 TRP TRP A . n 
A 1 97  HIS 97  397 397 HIS HIS A . n 
A 1 98  SER 98  398 398 SER SER A . n 
A 1 99  GLU 99  399 399 GLU GLU A . n 
A 1 100 PHE 100 400 400 PHE PHE A . n 
A 1 101 PRO 101 401 401 PRO PRO A . n 
A 1 102 LYS 102 402 402 LYS LYS A . n 
A 1 103 PRO 103 403 403 PRO PRO A . n 
A 1 104 GLN 104 404 404 GLN GLN A . n 
A 1 105 ILE 105 405 405 ILE ILE A . n 
A 1 106 LEU 106 406 406 LEU LEU A . n 
A 1 107 LYS 107 407 407 LYS LYS A . n 
A 1 108 HIS 108 408 408 HIS HIS A . n 
A 1 109 ALA 109 409 409 ALA ALA A . n 
A 1 110 MET 110 410 410 MET MET A . n 
A 1 111 LYS 111 411 411 LYS LYS A . n 
A 1 112 GLU 112 412 412 GLU GLU A . n 
A 1 113 CYS 113 413 413 CYS CYS A . n 
A 1 114 LEU 114 414 414 LEU LEU A . n 
A 1 115 GLU 115 415 415 GLU GLU A . n 
A 1 116 LYS 116 416 416 LYS LYS A . n 
A 1 117 CYS 117 417 417 CYS CYS A . n 
A 1 118 ILE 118 418 418 ILE ILE A . n 
A 1 119 GLU 119 419 419 GLU GLU A . n 
A 1 120 GLN 120 420 420 GLN GLN A . n 
A 1 121 ASN 121 421 421 ASN ASN A . n 
A 1 122 ILE 122 422 422 ILE ILE A . n 
A 1 123 THR 123 423 423 THR THR A . n 
A 1 124 SER 124 424 424 SER SER A . n 
A 1 125 ILE 125 425 425 ILE ILE A . n 
A 1 126 SER 126 426 426 SER SER A . n 
A 1 127 PHE 127 427 427 PHE PHE A . n 
A 1 128 PRO 128 428 428 PRO PRO A . n 
A 1 129 ALA 129 429 429 ALA ALA A . n 
A 1 130 LEU 130 430 430 LEU LEU A . n 
A 1 131 GLY 131 431 431 GLY GLY A . n 
A 1 132 THR 132 432 432 THR THR A . n 
A 1 133 GLY 133 433 433 GLY GLY A . n 
A 1 134 ASN 134 434 434 ASN ASN A . n 
A 1 135 MET 135 435 435 MET MET A . n 
A 1 136 GLU 136 436 436 GLU GLU A . n 
A 1 137 ILE 137 437 437 ILE ILE A . n 
A 1 138 LYS 138 438 438 LYS LYS A . n 
A 1 139 LYS 139 439 439 LYS LYS A . n 
A 1 140 GLU 140 440 440 GLU GLU A . n 
A 1 141 THR 141 441 441 THR THR A . n 
A 1 142 ALA 142 442 442 ALA ALA A . n 
A 1 143 ALA 143 443 443 ALA ALA A . n 
A 1 144 GLU 144 444 444 GLU GLU A . n 
A 1 145 ILE 145 445 445 ILE ILE A . n 
A 1 146 LEU 146 446 446 LEU LEU A . n 
A 1 147 PHE 147 447 447 PHE PHE A . n 
A 1 148 ASP 148 448 448 ASP ASP A . n 
A 1 149 GLU 149 449 449 GLU GLU A . n 
A 1 150 VAL 150 450 450 VAL VAL A . n 
A 1 151 LEU 151 451 451 LEU LEU A . n 
A 1 152 THR 152 452 452 THR THR A . n 
A 1 153 PHE 153 453 453 PHE PHE A . n 
A 1 154 ALA 154 454 454 ALA ALA A . n 
A 1 155 LYS 155 455 455 LYS LYS A . n 
A 1 156 ASP 156 456 456 ASP ASP A . n 
A 1 157 HIS 157 457 457 HIS HIS A . n 
A 1 158 VAL 158 458 458 VAL VAL A . n 
A 1 159 LYS 159 459 459 LYS LYS A . n 
A 1 160 HIS 160 460 460 HIS HIS A . n 
A 1 161 GLN 161 461 461 GLN GLN A . n 
A 1 162 LEU 162 462 462 LEU LEU A . n 
A 1 163 THR 163 463 463 THR THR A . n 
A 1 164 VAL 164 464 464 VAL VAL A . n 
A 1 165 LYS 165 465 465 LYS LYS A . n 
A 1 166 PHE 166 466 466 PHE PHE A . n 
A 1 167 VAL 167 467 467 VAL VAL A . n 
A 1 168 ILE 168 468 468 ILE ILE A . n 
A 1 169 PHE 169 469 469 PHE PHE A . n 
A 1 170 PRO 170 470 470 PRO PRO A . n 
A 1 171 THR 171 471 471 THR THR A . n 
A 1 172 ASP 172 472 472 ASP ASP A . n 
A 1 173 LEU 173 473 473 LEU LEU A . n 
A 1 174 GLU 174 474 474 GLU GLU A . n 
A 1 175 ILE 175 475 475 ILE ILE A . n 
A 1 176 TYR 176 476 476 TYR TYR A . n 
A 1 177 LYS 177 477 477 LYS LYS A . n 
A 1 178 ALA 178 478 478 ALA ALA A . n 
A 1 179 PHE 179 479 479 PHE PHE A . n 
A 1 180 SER 180 480 480 SER SER A . n 
A 1 181 SER 181 481 481 SER SER A . n 
A 1 182 GLU 182 482 482 GLU GLU A . n 
A 1 183 MET 183 483 483 MET MET A . n 
A 1 184 ALA 184 484 484 ALA ALA A . n 
A 1 185 LYS 185 485 485 LYS LYS A . n 
A 1 186 ARG 186 486 486 ARG ARG A . n 
A 1 187 SER 187 487 487 SER SER A . n 
A 1 188 LYS 188 488 488 LYS LYS A . n 
A 1 189 MET 189 489 489 MET MET A . n 
A 1 190 LEU 190 490 490 LEU LEU A . n 
A 1 191 SER 191 491 491 SER SER A . n 
A 1 192 LEU 192 492 492 LEU LEU A . n 
A 1 193 ASN 193 493 493 ASN ASN A . n 
A 1 194 ASN 194 494 494 ASN ASN A . n 
A 1 195 TYR 195 495 495 TYR TYR A . n 
A 1 196 SER 196 496 496 SER SER A . n 
A 1 197 VAL 197 497 497 VAL VAL A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 APR ? ? APR ? ? 'SUBJECT OF INVESTIGATION' ? 
2 AR6 ? ? AR6 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
B 2 APR 1   501 1   APR APR A . 
C 3 AR6 1   502 2   AR6 AR6 A . 
D 4 HOH 1   601 218 HOH HOH A . 
D 4 HOH 2   602 190 HOH HOH A . 
D 4 HOH 3   603 195 HOH HOH A . 
D 4 HOH 4   604 231 HOH HOH A . 
D 4 HOH 5   605 101 HOH HOH A . 
D 4 HOH 6   606 194 HOH HOH A . 
D 4 HOH 7   607 7   HOH HOH A . 
D 4 HOH 8   608 96  HOH HOH A . 
D 4 HOH 9   609 133 HOH HOH A . 
D 4 HOH 10  610 191 HOH HOH A . 
D 4 HOH 11  611 62  HOH HOH A . 
D 4 HOH 12  612 232 HOH HOH A . 
D 4 HOH 13  613 65  HOH HOH A . 
D 4 HOH 14  614 170 HOH HOH A . 
D 4 HOH 15  615 10  HOH HOH A . 
D 4 HOH 16  616 52  HOH HOH A . 
D 4 HOH 17  617 144 HOH HOH A . 
D 4 HOH 18  618 161 HOH HOH A . 
D 4 HOH 19  619 75  HOH HOH A . 
D 4 HOH 20  620 11  HOH HOH A . 
D 4 HOH 21  621 70  HOH HOH A . 
D 4 HOH 22  622 115 HOH HOH A . 
D 4 HOH 23  623 149 HOH HOH A . 
D 4 HOH 24  624 236 HOH HOH A . 
D 4 HOH 25  625 110 HOH HOH A . 
D 4 HOH 26  626 47  HOH HOH A . 
D 4 HOH 27  627 2   HOH HOH A . 
D 4 HOH 28  628 74  HOH HOH A . 
D 4 HOH 29  629 100 HOH HOH A . 
D 4 HOH 30  630 1   HOH HOH A . 
D 4 HOH 31  631 69  HOH HOH A . 
D 4 HOH 32  632 23  HOH HOH A . 
D 4 HOH 33  633 159 HOH HOH A . 
D 4 HOH 34  634 51  HOH HOH A . 
D 4 HOH 35  635 95  HOH HOH A . 
D 4 HOH 36  636 129 HOH HOH A . 
D 4 HOH 37  637 116 HOH HOH A . 
D 4 HOH 38  638 9   HOH HOH A . 
D 4 HOH 39  639 85  HOH HOH A . 
D 4 HOH 40  640 31  HOH HOH A . 
D 4 HOH 41  641 239 HOH HOH A . 
D 4 HOH 42  642 6   HOH HOH A . 
D 4 HOH 43  643 42  HOH HOH A . 
D 4 HOH 44  644 150 HOH HOH A . 
D 4 HOH 45  645 210 HOH HOH A . 
D 4 HOH 46  646 157 HOH HOH A . 
D 4 HOH 47  647 117 HOH HOH A . 
D 4 HOH 48  648 130 HOH HOH A . 
D 4 HOH 49  649 82  HOH HOH A . 
D 4 HOH 50  650 234 HOH HOH A . 
D 4 HOH 51  651 71  HOH HOH A . 
D 4 HOH 52  652 26  HOH HOH A . 
D 4 HOH 53  653 203 HOH HOH A . 
D 4 HOH 54  654 97  HOH HOH A . 
D 4 HOH 55  655 113 HOH HOH A . 
D 4 HOH 56  656 108 HOH HOH A . 
D 4 HOH 57  657 66  HOH HOH A . 
D 4 HOH 58  658 22  HOH HOH A . 
D 4 HOH 59  659 141 HOH HOH A . 
D 4 HOH 60  660 81  HOH HOH A . 
D 4 HOH 61  661 255 HOH HOH A . 
D 4 HOH 62  662 158 HOH HOH A . 
D 4 HOH 63  663 59  HOH HOH A . 
D 4 HOH 64  664 79  HOH HOH A . 
D 4 HOH 65  665 84  HOH HOH A . 
D 4 HOH 66  666 5   HOH HOH A . 
D 4 HOH 67  667 43  HOH HOH A . 
D 4 HOH 68  668 240 HOH HOH A . 
D 4 HOH 69  669 49  HOH HOH A . 
D 4 HOH 70  670 91  HOH HOH A . 
D 4 HOH 71  671 114 HOH HOH A . 
D 4 HOH 72  672 13  HOH HOH A . 
D 4 HOH 73  673 105 HOH HOH A . 
D 4 HOH 74  674 25  HOH HOH A . 
D 4 HOH 75  675 48  HOH HOH A . 
D 4 HOH 76  676 189 HOH HOH A . 
D 4 HOH 77  677 206 HOH HOH A . 
D 4 HOH 78  678 17  HOH HOH A . 
D 4 HOH 79  679 16  HOH HOH A . 
D 4 HOH 80  680 107 HOH HOH A . 
D 4 HOH 81  681 140 HOH HOH A . 
D 4 HOH 82  682 61  HOH HOH A . 
D 4 HOH 83  683 146 HOH HOH A . 
D 4 HOH 84  684 211 HOH HOH A . 
D 4 HOH 85  685 248 HOH HOH A . 
D 4 HOH 86  686 50  HOH HOH A . 
D 4 HOH 87  687 12  HOH HOH A . 
D 4 HOH 88  688 153 HOH HOH A . 
D 4 HOH 89  689 53  HOH HOH A . 
D 4 HOH 90  690 32  HOH HOH A . 
D 4 HOH 91  691 39  HOH HOH A . 
D 4 HOH 92  692 54  HOH HOH A . 
D 4 HOH 93  693 73  HOH HOH A . 
D 4 HOH 94  694 8   HOH HOH A . 
D 4 HOH 95  695 89  HOH HOH A . 
D 4 HOH 96  696 235 HOH HOH A . 
D 4 HOH 97  697 175 HOH HOH A . 
D 4 HOH 98  698 44  HOH HOH A . 
D 4 HOH 99  699 29  HOH HOH A . 
D 4 HOH 100 700 109 HOH HOH A . 
D 4 HOH 101 701 57  HOH HOH A . 
D 4 HOH 102 702 30  HOH HOH A . 
D 4 HOH 103 703 134 HOH HOH A . 
D 4 HOH 104 704 63  HOH HOH A . 
D 4 HOH 105 705 169 HOH HOH A . 
D 4 HOH 106 706 18  HOH HOH A . 
D 4 HOH 107 707 20  HOH HOH A . 
D 4 HOH 108 708 111 HOH HOH A . 
D 4 HOH 109 709 182 HOH HOH A . 
D 4 HOH 110 710 3   HOH HOH A . 
D 4 HOH 111 711 77  HOH HOH A . 
D 4 HOH 112 712 35  HOH HOH A . 
D 4 HOH 113 713 86  HOH HOH A . 
D 4 HOH 114 714 45  HOH HOH A . 
D 4 HOH 115 715 24  HOH HOH A . 
D 4 HOH 116 716 83  HOH HOH A . 
D 4 HOH 117 717 21  HOH HOH A . 
D 4 HOH 118 718 68  HOH HOH A . 
D 4 HOH 119 719 58  HOH HOH A . 
D 4 HOH 120 720 177 HOH HOH A . 
D 4 HOH 121 721 37  HOH HOH A . 
D 4 HOH 122 722 99  HOH HOH A . 
D 4 HOH 123 723 64  HOH HOH A . 
D 4 HOH 124 724 41  HOH HOH A . 
D 4 HOH 125 725 38  HOH HOH A . 
D 4 HOH 126 726 88  HOH HOH A . 
D 4 HOH 127 727 14  HOH HOH A . 
D 4 HOH 128 728 27  HOH HOH A . 
D 4 HOH 129 729 213 HOH HOH A . 
D 4 HOH 130 730 229 HOH HOH A . 
D 4 HOH 131 731 80  HOH HOH A . 
D 4 HOH 132 732 67  HOH HOH A . 
D 4 HOH 133 733 55  HOH HOH A . 
D 4 HOH 134 734 145 HOH HOH A . 
D 4 HOH 135 735 33  HOH HOH A . 
D 4 HOH 136 736 139 HOH HOH A . 
D 4 HOH 137 737 119 HOH HOH A . 
D 4 HOH 138 738 19  HOH HOH A . 
D 4 HOH 139 739 164 HOH HOH A . 
D 4 HOH 140 740 106 HOH HOH A . 
D 4 HOH 141 741 87  HOH HOH A . 
D 4 HOH 142 742 112 HOH HOH A . 
D 4 HOH 143 743 36  HOH HOH A . 
D 4 HOH 144 744 132 HOH HOH A . 
D 4 HOH 145 745 148 HOH HOH A . 
D 4 HOH 146 746 160 HOH HOH A . 
D 4 HOH 147 747 121 HOH HOH A . 
D 4 HOH 148 748 243 HOH HOH A . 
D 4 HOH 149 749 237 HOH HOH A . 
D 4 HOH 150 750 28  HOH HOH A . 
D 4 HOH 151 751 127 HOH HOH A . 
D 4 HOH 152 752 183 HOH HOH A . 
D 4 HOH 153 753 125 HOH HOH A . 
D 4 HOH 154 754 227 HOH HOH A . 
D 4 HOH 155 755 128 HOH HOH A . 
D 4 HOH 156 756 233 HOH HOH A . 
D 4 HOH 157 757 225 HOH HOH A . 
D 4 HOH 158 758 174 HOH HOH A . 
D 4 HOH 159 759 184 HOH HOH A . 
D 4 HOH 160 760 226 HOH HOH A . 
D 4 HOH 161 761 56  HOH HOH A . 
D 4 HOH 162 762 135 HOH HOH A . 
D 4 HOH 163 763 76  HOH HOH A . 
D 4 HOH 164 764 244 HOH HOH A . 
D 4 HOH 165 765 98  HOH HOH A . 
D 4 HOH 166 766 102 HOH HOH A . 
D 4 HOH 167 767 92  HOH HOH A . 
D 4 HOH 168 768 176 HOH HOH A . 
D 4 HOH 169 769 200 HOH HOH A . 
D 4 HOH 170 770 224 HOH HOH A . 
D 4 HOH 171 771 78  HOH HOH A . 
D 4 HOH 172 772 154 HOH HOH A . 
D 4 HOH 173 773 209 HOH HOH A . 
D 4 HOH 174 774 192 HOH HOH A . 
D 4 HOH 175 775 204 HOH HOH A . 
D 4 HOH 176 776 247 HOH HOH A . 
D 4 HOH 177 777 40  HOH HOH A . 
D 4 HOH 178 778 60  HOH HOH A . 
D 4 HOH 179 779 72  HOH HOH A . 
D 4 HOH 180 780 196 HOH HOH A . 
D 4 HOH 181 781 238 HOH HOH A . 
D 4 HOH 182 782 242 HOH HOH A . 
D 4 HOH 183 783 245 HOH HOH A . 
D 4 HOH 184 784 156 HOH HOH A . 
D 4 HOH 185 785 137 HOH HOH A . 
D 4 HOH 186 786 180 HOH HOH A . 
D 4 HOH 187 787 155 HOH HOH A . 
D 4 HOH 188 788 120 HOH HOH A . 
D 4 HOH 189 789 228 HOH HOH A . 
D 4 HOH 190 790 93  HOH HOH A . 
D 4 HOH 191 791 131 HOH HOH A . 
D 4 HOH 192 792 168 HOH HOH A . 
D 4 HOH 193 793 152 HOH HOH A . 
D 4 HOH 194 794 217 HOH HOH A . 
D 4 HOH 195 795 142 HOH HOH A . 
D 4 HOH 196 796 122 HOH HOH A . 
D 4 HOH 197 797 124 HOH HOH A . 
D 4 HOH 198 798 126 HOH HOH A . 
D 4 HOH 199 799 34  HOH HOH A . 
D 4 HOH 200 800 193 HOH HOH A . 
D 4 HOH 201 801 241 HOH HOH A . 
D 4 HOH 202 802 103 HOH HOH A . 
D 4 HOH 203 803 246 HOH HOH A . 
D 4 HOH 204 804 179 HOH HOH A . 
D 4 HOH 205 805 185 HOH HOH A . 
D 4 HOH 206 806 250 HOH HOH A . 
D 4 HOH 207 807 251 HOH HOH A . 
D 4 HOH 208 808 249 HOH HOH A . 
D 4 HOH 209 809 252 HOH HOH A . 
D 4 HOH 210 810 253 HOH HOH A . 
D 4 HOH 211 811 254 HOH HOH A . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9QYF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.143 
_cell.length_a_esd                 ? 
_cell.length_b                     52.143 
_cell.length_b_esd                 ? 
_cell.length_c                     132.158 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9QYF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   9QYF 
_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             2.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.12 
_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    '0.1M Succinic acid, 15% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-26 
_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   0.9655 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9655 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9QYF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.3 
_reflns.d_resolution_low                               40.93 
_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                                     45496 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17 
_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                                    1.3 
_reflns_shell.d_res_low                                     1.32 
_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                             2206 
_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                                  0.698 
_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]                            1.69 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.69 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -3.38 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.498 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.982 
_refine.correlation_coeff_Fo_to_Fc_free          0.973 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9QYF 
_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                            1.30 
_refine.ls_d_res_low                             40.97 
_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                     43241 
_refine.ls_number_reflns_R_free                  2255 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.26 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.13517 
_refine.ls_R_factor_R_free                       0.17313 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.13325 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.047 
_refine.pdbx_overall_ESU_R_Free                  0.048 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.304 
_refine.overall_SU_ML                            0.041 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.30 
_refine_hist.d_res_low                        40.97 
_refine_hist.number_atoms_solvent             211 
_refine_hist.number_atoms_total               1801 
_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        1518 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.010  0.012  1697 ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1615 ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.747  1.821  2316 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.605  1.759  3738 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 5.693  5.000  204  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 3.225  5.000  2    ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 12.007 10.000 308  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.098  0.200  271  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  1886 ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  364  ? r_gen_planes_other           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? ? 
'X-RAY DIFFRACTION' ? 4.746  1.649  798  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 4.703  1.648  798  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 6.370  2.971  1008 ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 6.383  2.973  1009 ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 6.969  1.966  899  ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 6.965  1.966  900  ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 9.547  3.474  1309 ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 13.871 24.10  1933 ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 12.500 19.26  1867 ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? 3.902  3.000  3312 ? r_rigid_bond_restr           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.300 
_refine_ls_shell.d_res_low                           1.334 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                175 
_refine_ls_shell.number_reflns_R_work                3122 
_refine_ls_shell.percent_reflns_obs                  99.13 
_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                     0.233 
_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      20 
_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                     0.251 
# 
_struct.entry_id                     9QYF 
_struct.title                        'PARP9 Macro Domain 2 in complex with ADPr' 
_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        9QYF 
_struct_keywords.text            'Complex, ADP-ribose, ADPribosylation, PARP9, Macro domain, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PARP9_HUMAN 
_struct_ref.pdbx_db_accession          Q8IXQ6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGF
NLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTV
KFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSV
;
_struct_ref.pdbx_align_begin           305 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9QYF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 197 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8IXQ6 
_struct_ref_seq.db_align_beg                  305 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  497 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       305 
_struct_ref_seq.pdbx_auth_seq_align_end       497 
# 
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 9QYF GLY A 1 ? UNP Q8IXQ6 ? ? 'expression tag' 301 1 
1 9QYF ALA A 2 ? UNP Q8IXQ6 ? ? 'expression tag' 302 2 
1 9QYF MET A 3 ? UNP Q8IXQ6 ? ? 'expression tag' 303 3 
1 9QYF ALA A 4 ? UNP Q8IXQ6 ? ? 'expression tag' 304 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 700  ? 
1 MORE         -7   ? 
1 'SSA (A^2)'  9290 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 25  ? GLN A 29  ? HIS A 325 GLN A 329 5 ? 5  
HELX_P HELX_P2 AA2 GLY A 46  ? GLY A 57  ? GLY A 346 GLY A 357 1 ? 12 
HELX_P HELX_P3 AA3 GLY A 57  ? PHE A 72  ? GLY A 357 PHE A 372 1 ? 16 
HELX_P HELX_P4 AA4 PRO A 101 ? GLN A 120 ? PRO A 401 GLN A 420 1 ? 20 
HELX_P HELX_P5 AA5 LYS A 138 ? HIS A 157 ? LYS A 438 HIS A 457 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 172 ? LEU A 190 ? ASP A 472 LEU A 490 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 VAL A 78  ? LYS A 82  ? VAL A 378 LYS A 382 
AA1 2 TYR A 90  ? LEU A 95  ? TYR A 390 LEU A 395 
AA1 3 VAL A 33  ? VAL A 38  ? VAL A 333 VAL A 338 
AA1 4 SER A 124 ? PRO A 128 ? SER A 424 PRO A 428 
AA1 5 LEU A 162 ? ILE A 168 ? LEU A 462 ILE A 468 
AA1 6 LEU A 17  ? GLN A 23  ? LEU A 317 GLN A 323 
AA1 7 ALA A 11  ? VAL A 14  ? ALA A 311 VAL A 314 
AA1 8 ASN A 193 ? TYR A 195 ? ASN A 493 TYR A 495 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 79  ? N LEU A 379 O HIS A 93  ? O HIS A 393 
AA1 2 3 O VAL A 94  ? O VAL A 394 N VAL A 38  ? N VAL A 338 
AA1 3 4 N VAL A 35  ? N VAL A 335 O SER A 126 ? O SER A 426 
AA1 4 5 N PHE A 127 ? N PHE A 427 O VAL A 167 ? O VAL A 467 
AA1 5 6 O ILE A 168 ? O ILE A 468 N VAL A 22  ? N VAL A 322 
AA1 6 7 O LEU A 17  ? O LEU A 317 N VAL A 14  ? N VAL A 314 
AA1 7 8 N ALA A 11  ? N ALA A 311 O TYR A 195 ? O TYR A 495 
# 
_pdbx_entry_details.entry_id                   9QYF 
_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   N 
# 
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 764 ? ? O A HOH 783 ? ? 1.81 
2 1 O A HOH 684 ? ? O A HOH 750 ? ? 2.00 
3 1 O A HOH 606 ? ? O A HOH 667 ? ? 2.04 
4 1 O A HOH 677 ? ? O A HOH 774 ? ? 2.13 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 772 ? ? 1_555 O A HOH 800 ? ? 6_455 1.60 
2 1 O A HOH 769 ? ? 1_555 O A HOH 786 ? ? 3_454 1.86 
3 1 O A HOH 610 ? ? 1_555 O A HOH 773 ? ? 7_455 2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 315 ? ? 52.84   -118.06 
2 1 ASP A 342 ? ? -164.95 94.17   
3 1 PHE A 384 ? ? 51.57   -123.98 
4 1 HIS A 397 ? ? -159.51 46.93   
# 
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 806 ? 5.87  . 
2 1 O ? A HOH 807 ? 6.62  . 
3 1 O ? A HOH 808 ? 6.75  . 
4 1 O ? A HOH 809 ? 9.73  . 
5 1 O ? A HOH 810 ? 10.20 . 
6 1 O ? A HOH 811 ? 10.82 . 
# 
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 GLY 301 ? A GLY 1 
2 1 Y 1 A ALA 302 ? A ALA 2 
3 1 Y 1 A MET 303 ? A MET 3 
4 1 Y 1 A ALA 304 ? A ALA 4 
5 1 Y 1 A THR 305 ? A THR 5 
6 1 Y 1 A THR 306 ? A THR 6 
7 1 Y 1 A PRO 307 ? A PRO 7 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
APR N1     N Y N 14  
APR C2     C Y N 15  
APR N3     N Y N 16  
APR C4     C Y N 17  
APR C5     C Y N 18  
APR C6     C Y N 19  
APR N6     N N N 20  
APR N7     N Y N 21  
APR C8     C Y N 22  
APR N9     N Y N 23  
APR "C1'"  C N R 24  
APR "C2'"  C N R 25  
APR "O2'"  O N N 26  
APR "C3'"  C N S 27  
APR "O3'"  O N N 28  
APR "O4'"  O N N 29  
APR "C4'"  C N R 30  
APR "C5'"  C N N 31  
APR "O5'"  O N N 32  
APR PA     P N S 33  
APR O1A    O N N 34  
APR O2A    O N N 35  
APR O3A    O N N 36  
APR PB     P N R 37  
APR O1B    O N N 38  
APR O2B    O N N 39  
APR O5D    O N N 40  
APR C5D    C N N 41  
APR O4D    O N N 42  
APR O1D    O N N 43  
APR C1D    C N R 44  
APR O2D    O N N 45  
APR C2D    C N R 46  
APR O3D    O N N 47  
APR C3D    C N S 48  
APR C4D    C N R 49  
APR H2     H N N 50  
APR H61    H N N 51  
APR H62    H N N 52  
APR H8     H N N 53  
APR "H'1"  H N N 54  
APR "H'2"  H N N 55  
APR "HO'2" H N N 56  
APR "H'3"  H N N 57  
APR "HO'3" H N N 58  
APR "H'4"  H N N 59  
APR "H5'1" H N N 60  
APR "H5'2" H N N 61  
APR HOA2   H N N 62  
APR HOB2   H N N 63  
APR H5R1   H N N 64  
APR H5R2   H N N 65  
APR HOR1   H N N 66  
APR "HR'1" H N N 67  
APR HOR2   H N N 68  
APR "HR'2" H N N 69  
APR HOR3   H N N 70  
APR "HR'3" H N N 71  
APR "HR'4" H N N 72  
AR6 N1     N Y N 73  
AR6 C2     C Y N 74  
AR6 N3     N Y N 75  
AR6 C4     C Y N 76  
AR6 C5     C Y N 77  
AR6 C6     C Y N 78  
AR6 N6     N N N 79  
AR6 N7     N Y N 80  
AR6 C8     C Y N 81  
AR6 N9     N Y N 82  
AR6 PA     P N N 83  
AR6 PB     P N N 84  
AR6 "C1'"  C N R 85  
AR6 O1A    O N N 86  
AR6 O1B    O N N 87  
AR6 C1D    C N S 88  
AR6 O1D    O N N 89  
AR6 "C2'"  C N R 90  
AR6 "O2'"  O N N 91  
AR6 O2A    O N N 92  
AR6 O2B    O N N 93  
AR6 C2D    C N R 94  
AR6 O2D    O N N 95  
AR6 "C3'"  C N S 96  
AR6 "O3'"  O N N 97  
AR6 O3A    O N N 98  
AR6 C3D    C N S 99  
AR6 O3D    O N N 100 
AR6 "C4'"  C N R 101 
AR6 "O4'"  O N N 102 
AR6 C4D    C N R 103 
AR6 O4D    O N N 104 
AR6 "C5'"  C N N 105 
AR6 "O5'"  O N N 106 
AR6 C5D    C N N 107 
AR6 O5D    O N N 108 
AR6 H2     H N N 109 
AR6 HN6    H N N 110 
AR6 HN6A   H N N 111 
AR6 H8     H N N 112 
AR6 "H1'"  H N N 113 
AR6 H1D    H N N 114 
AR6 "H2'"  H N N 115 
AR6 "HO2'" H N N 116 
AR6 H2D    H N N 117 
AR6 HO2D   H N N 118 
AR6 "H3'"  H N N 119 
AR6 "HO3'" H N N 120 
AR6 H3D    H N N 121 
AR6 HO3D   H N N 122 
AR6 "H4'"  H N N 123 
AR6 H4D    H N N 124 
AR6 "H5'"  H N N 125 
AR6 "H5'A" H N N 126 
AR6 H5D    H N N 127 
AR6 H5DA   H N N 128 
AR6 H1A    H N N 129 
AR6 H1B    H N N 130 
AR6 HD1    H N N 131 
ARG N      N N N 132 
ARG CA     C N S 133 
ARG C      C N N 134 
ARG O      O N N 135 
ARG CB     C N N 136 
ARG CG     C N N 137 
ARG CD     C N N 138 
ARG NE     N N N 139 
ARG CZ     C N N 140 
ARG NH1    N N N 141 
ARG NH2    N N N 142 
ARG OXT    O N N 143 
ARG H      H N N 144 
ARG H2     H N N 145 
ARG HA     H N N 146 
ARG HB2    H N N 147 
ARG HB3    H N N 148 
ARG HG2    H N N 149 
ARG HG3    H N N 150 
ARG HD2    H N N 151 
ARG HD3    H N N 152 
ARG HE     H N N 153 
ARG HH11   H N N 154 
ARG HH12   H N N 155 
ARG HH21   H N N 156 
ARG HH22   H N N 157 
ARG HXT    H N N 158 
ASN N      N N N 159 
ASN CA     C N S 160 
ASN C      C N N 161 
ASN O      O N N 162 
ASN CB     C N N 163 
ASN CG     C N N 164 
ASN OD1    O N N 165 
ASN ND2    N N N 166 
ASN OXT    O N N 167 
ASN H      H N N 168 
ASN H2     H N N 169 
ASN HA     H N N 170 
ASN HB2    H N N 171 
ASN HB3    H N N 172 
ASN HD21   H N N 173 
ASN HD22   H N N 174 
ASN HXT    H N N 175 
ASP N      N N N 176 
ASP CA     C N S 177 
ASP C      C N N 178 
ASP O      O N N 179 
ASP CB     C N N 180 
ASP CG     C N N 181 
ASP OD1    O N N 182 
ASP OD2    O N N 183 
ASP OXT    O N N 184 
ASP H      H N N 185 
ASP H2     H N N 186 
ASP HA     H N N 187 
ASP HB2    H N N 188 
ASP HB3    H N N 189 
ASP HD2    H N N 190 
ASP HXT    H N N 191 
CYS N      N N N 192 
CYS CA     C N R 193 
CYS C      C N N 194 
CYS O      O N N 195 
CYS CB     C N N 196 
CYS SG     S N N 197 
CYS OXT    O N N 198 
CYS H      H N N 199 
CYS H2     H N N 200 
CYS HA     H N N 201 
CYS HB2    H N N 202 
CYS HB3    H N N 203 
CYS HG     H N N 204 
CYS HXT    H N N 205 
GLN N      N N N 206 
GLN CA     C N S 207 
GLN C      C N N 208 
GLN O      O N N 209 
GLN CB     C N N 210 
GLN CG     C N N 211 
GLN CD     C N N 212 
GLN OE1    O N N 213 
GLN NE2    N N N 214 
GLN OXT    O N N 215 
GLN H      H N N 216 
GLN H2     H N N 217 
GLN HA     H N N 218 
GLN HB2    H N N 219 
GLN HB3    H N N 220 
GLN HG2    H N N 221 
GLN HG3    H N N 222 
GLN HE21   H N N 223 
GLN HE22   H N N 224 
GLN HXT    H N N 225 
GLU N      N N N 226 
GLU CA     C N S 227 
GLU C      C N N 228 
GLU O      O N N 229 
GLU CB     C N N 230 
GLU CG     C N N 231 
GLU CD     C N N 232 
GLU OE1    O N N 233 
GLU OE2    O N N 234 
GLU OXT    O N N 235 
GLU H      H N N 236 
GLU H2     H N N 237 
GLU HA     H N N 238 
GLU HB2    H N N 239 
GLU HB3    H N N 240 
GLU HG2    H N N 241 
GLU HG3    H N N 242 
GLU HE2    H N N 243 
GLU HXT    H N N 244 
GLY N      N N N 245 
GLY CA     C N N 246 
GLY C      C N N 247 
GLY O      O N N 248 
GLY OXT    O N N 249 
GLY H      H N N 250 
GLY H2     H N N 251 
GLY HA2    H N N 252 
GLY HA3    H N N 253 
GLY HXT    H N N 254 
HIS N      N N N 255 
HIS CA     C N S 256 
HIS C      C N N 257 
HIS O      O N N 258 
HIS CB     C N N 259 
HIS CG     C Y N 260 
HIS ND1    N Y N 261 
HIS CD2    C Y N 262 
HIS CE1    C Y N 263 
HIS NE2    N Y N 264 
HIS OXT    O N N 265 
HIS H      H N N 266 
HIS H2     H N N 267 
HIS HA     H N N 268 
HIS HB2    H N N 269 
HIS HB3    H N N 270 
HIS HD1    H N N 271 
HIS HD2    H N N 272 
HIS HE1    H N N 273 
HIS HE2    H N N 274 
HIS HXT    H N N 275 
HOH O      O N N 276 
HOH H1     H N N 277 
HOH H2     H N N 278 
ILE N      N N N 279 
ILE CA     C N S 280 
ILE C      C N N 281 
ILE O      O N N 282 
ILE CB     C N S 283 
ILE CG1    C N N 284 
ILE CG2    C N N 285 
ILE CD1    C N N 286 
ILE OXT    O N N 287 
ILE H      H N N 288 
ILE H2     H N N 289 
ILE HA     H N N 290 
ILE HB     H N N 291 
ILE HG12   H N N 292 
ILE HG13   H N N 293 
ILE HG21   H N N 294 
ILE HG22   H N N 295 
ILE HG23   H N N 296 
ILE HD11   H N N 297 
ILE HD12   H N N 298 
ILE HD13   H N N 299 
ILE HXT    H N N 300 
LEU N      N N N 301 
LEU CA     C N S 302 
LEU C      C N N 303 
LEU O      O N N 304 
LEU CB     C N N 305 
LEU CG     C N N 306 
LEU CD1    C N N 307 
LEU CD2    C N N 308 
LEU OXT    O N N 309 
LEU H      H N N 310 
LEU H2     H N N 311 
LEU HA     H N N 312 
LEU HB2    H N N 313 
LEU HB3    H N N 314 
LEU HG     H N N 315 
LEU HD11   H N N 316 
LEU HD12   H N N 317 
LEU HD13   H N N 318 
LEU HD21   H N N 319 
LEU HD22   H N N 320 
LEU HD23   H N N 321 
LEU HXT    H N N 322 
LYS N      N N N 323 
LYS CA     C N S 324 
LYS C      C N N 325 
LYS O      O N N 326 
LYS CB     C N N 327 
LYS CG     C N N 328 
LYS CD     C N N 329 
LYS CE     C N N 330 
LYS NZ     N N N 331 
LYS OXT    O N N 332 
LYS H      H N N 333 
LYS H2     H N N 334 
LYS HA     H N N 335 
LYS HB2    H N N 336 
LYS HB3    H N N 337 
LYS HG2    H N N 338 
LYS HG3    H N N 339 
LYS HD2    H N N 340 
LYS HD3    H N N 341 
LYS HE2    H N N 342 
LYS HE3    H N N 343 
LYS HZ1    H N N 344 
LYS HZ2    H N N 345 
LYS HZ3    H N N 346 
LYS HXT    H N N 347 
MET N      N N N 348 
MET CA     C N S 349 
MET C      C N N 350 
MET O      O N N 351 
MET CB     C N N 352 
MET CG     C N N 353 
MET SD     S N N 354 
MET CE     C N N 355 
MET OXT    O N N 356 
MET H      H N N 357 
MET H2     H N N 358 
MET HA     H N N 359 
MET HB2    H N N 360 
MET HB3    H N N 361 
MET HG2    H N N 362 
MET HG3    H N N 363 
MET HE1    H N N 364 
MET HE2    H N N 365 
MET HE3    H N N 366 
MET HXT    H N N 367 
PHE N      N N N 368 
PHE CA     C N S 369 
PHE C      C N N 370 
PHE O      O N N 371 
PHE CB     C N N 372 
PHE CG     C Y N 373 
PHE CD1    C Y N 374 
PHE CD2    C Y N 375 
PHE CE1    C Y N 376 
PHE CE2    C Y N 377 
PHE CZ     C Y N 378 
PHE OXT    O N N 379 
PHE H      H N N 380 
PHE H2     H N N 381 
PHE HA     H N N 382 
PHE HB2    H N N 383 
PHE HB3    H N N 384 
PHE HD1    H N N 385 
PHE HD2    H N N 386 
PHE HE1    H N N 387 
PHE HE2    H N N 388 
PHE HZ     H N N 389 
PHE HXT    H N N 390 
PRO N      N N N 391 
PRO CA     C N S 392 
PRO C      C N N 393 
PRO O      O N N 394 
PRO CB     C N N 395 
PRO CG     C N N 396 
PRO CD     C N N 397 
PRO OXT    O N N 398 
PRO H      H N N 399 
PRO HA     H N N 400 
PRO HB2    H N N 401 
PRO HB3    H N N 402 
PRO HG2    H N N 403 
PRO HG3    H N N 404 
PRO HD2    H N N 405 
PRO HD3    H N N 406 
PRO HXT    H N N 407 
SER N      N N N 408 
SER CA     C N S 409 
SER C      C N N 410 
SER O      O N N 411 
SER CB     C N N 412 
SER OG     O N N 413 
SER OXT    O N N 414 
SER H      H N N 415 
SER H2     H N N 416 
SER HA     H N N 417 
SER HB2    H N N 418 
SER HB3    H N N 419 
SER HG     H N N 420 
SER HXT    H N N 421 
THR N      N N N 422 
THR CA     C N S 423 
THR C      C N N 424 
THR O      O N N 425 
THR CB     C N R 426 
THR OG1    O N N 427 
THR CG2    C N N 428 
THR OXT    O N N 429 
THR H      H N N 430 
THR H2     H N N 431 
THR HA     H N N 432 
THR HB     H N N 433 
THR HG1    H N N 434 
THR HG21   H N N 435 
THR HG22   H N N 436 
THR HG23   H N N 437 
THR HXT    H N N 438 
TRP N      N N N 439 
TRP CA     C N S 440 
TRP C      C N N 441 
TRP O      O N N 442 
TRP CB     C N N 443 
TRP CG     C Y N 444 
TRP CD1    C Y N 445 
TRP CD2    C Y N 446 
TRP NE1    N Y N 447 
TRP CE2    C Y N 448 
TRP CE3    C Y N 449 
TRP CZ2    C Y N 450 
TRP CZ3    C Y N 451 
TRP CH2    C Y N 452 
TRP OXT    O N N 453 
TRP H      H N N 454 
TRP H2     H N N 455 
TRP HA     H N N 456 
TRP HB2    H N N 457 
TRP HB3    H N N 458 
TRP HD1    H N N 459 
TRP HE1    H N N 460 
TRP HE3    H N N 461 
TRP HZ2    H N N 462 
TRP HZ3    H N N 463 
TRP HH2    H N N 464 
TRP HXT    H N N 465 
TYR N      N N N 466 
TYR CA     C N S 467 
TYR C      C N N 468 
TYR O      O N N 469 
TYR CB     C N N 470 
TYR CG     C Y N 471 
TYR CD1    C Y N 472 
TYR CD2    C Y N 473 
TYR CE1    C Y N 474 
TYR CE2    C Y N 475 
TYR CZ     C Y N 476 
TYR OH     O N N 477 
TYR OXT    O N N 478 
TYR H      H N N 479 
TYR H2     H N N 480 
TYR HA     H N N 481 
TYR HB2    H N N 482 
TYR HB3    H N N 483 
TYR HD1    H N N 484 
TYR HD2    H N N 485 
TYR HE1    H N N 486 
TYR HE2    H N N 487 
TYR HH     H N N 488 
TYR HXT    H N N 489 
VAL N      N N N 490 
VAL CA     C N S 491 
VAL C      C N N 492 
VAL O      O N N 493 
VAL CB     C N N 494 
VAL CG1    C N N 495 
VAL CG2    C N N 496 
VAL OXT    O N N 497 
VAL H      H N N 498 
VAL H2     H N N 499 
VAL HA     H N N 500 
VAL HB     H N N 501 
VAL HG11   H N N 502 
VAL HG12   H N N 503 
VAL HG13   H N N 504 
VAL HG21   H N N 505 
VAL HG22   H N N 506 
VAL HG23   H N N 507 
VAL HXT    H N N 508 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
APR N1    C2     sing Y N 13  
APR N1    C6     doub Y N 14  
APR C2    N3     doub Y N 15  
APR C2    H2     sing N N 16  
APR N3    C4     sing Y N 17  
APR C4    C5     doub Y N 18  
APR C4    N9     sing Y N 19  
APR C5    C6     sing Y N 20  
APR C5    N7     sing Y N 21  
APR C6    N6     sing N N 22  
APR N6    H61    sing N N 23  
APR N6    H62    sing N N 24  
APR N7    C8     doub Y N 25  
APR C8    N9     sing Y N 26  
APR C8    H8     sing N N 27  
APR N9    "C1'"  sing N N 28  
APR "C1'" "C2'"  sing N N 29  
APR "C1'" "O4'"  sing N N 30  
APR "C1'" "H'1"  sing N N 31  
APR "C2'" "O2'"  sing N N 32  
APR "C2'" "C3'"  sing N N 33  
APR "C2'" "H'2"  sing N N 34  
APR "O2'" "HO'2" sing N N 35  
APR "C3'" "O3'"  sing N N 36  
APR "C3'" "C4'"  sing N N 37  
APR "C3'" "H'3"  sing N N 38  
APR "O3'" "HO'3" sing N N 39  
APR "O4'" "C4'"  sing N N 40  
APR "C4'" "C5'"  sing N N 41  
APR "C4'" "H'4"  sing N N 42  
APR "C5'" "O5'"  sing N N 43  
APR "C5'" "H5'1" sing N N 44  
APR "C5'" "H5'2" sing N N 45  
APR "O5'" PA     sing N N 46  
APR PA    O1A    doub N N 47  
APR PA    O2A    sing N N 48  
APR PA    O3A    sing N N 49  
APR O2A   HOA2   sing N N 50  
APR O3A   PB     sing N N 51  
APR PB    O1B    doub N N 52  
APR PB    O2B    sing N N 53  
APR PB    O5D    sing N N 54  
APR O2B   HOB2   sing N N 55  
APR O5D   C5D    sing N N 56  
APR C5D   C4D    sing N N 57  
APR C5D   H5R1   sing N N 58  
APR C5D   H5R2   sing N N 59  
APR O4D   C1D    sing N N 60  
APR O4D   C4D    sing N N 61  
APR O1D   C1D    sing N N 62  
APR O1D   HOR1   sing N N 63  
APR C1D   C2D    sing N N 64  
APR C1D   "HR'1" sing N N 65  
APR O2D   C2D    sing N N 66  
APR O2D   HOR2   sing N N 67  
APR C2D   C3D    sing N N 68  
APR C2D   "HR'2" sing N N 69  
APR O3D   C3D    sing N N 70  
APR O3D   HOR3   sing N N 71  
APR C3D   C4D    sing N N 72  
APR C3D   "HR'3" sing N N 73  
APR C4D   "HR'4" sing N N 74  
AR6 N1    C2     doub Y N 75  
AR6 N1    C6     sing Y N 76  
AR6 C2    N3     sing Y N 77  
AR6 N3    C4     doub Y N 78  
AR6 C4    C5     sing Y N 79  
AR6 C4    N9     sing Y N 80  
AR6 C5    C6     doub Y N 81  
AR6 C5    N7     sing Y N 82  
AR6 C6    N6     sing N N 83  
AR6 N7    C8     doub Y N 84  
AR6 C8    N9     sing Y N 85  
AR6 N9    "C1'"  sing N N 86  
AR6 PA    O1A    sing N N 87  
AR6 PA    O2A    doub N N 88  
AR6 PA    O3A    sing N N 89  
AR6 PA    "O5'"  sing N N 90  
AR6 PB    O1B    sing N N 91  
AR6 PB    O2B    doub N N 92  
AR6 PB    O3A    sing N N 93  
AR6 PB    O5D    sing N N 94  
AR6 "C1'" "C2'"  sing N N 95  
AR6 "C1'" "O4'"  sing N N 96  
AR6 C1D   O1D    sing N N 97  
AR6 C1D   C2D    sing N N 98  
AR6 C1D   O4D    sing N N 99  
AR6 "C2'" "O2'"  sing N N 100 
AR6 "C2'" "C3'"  sing N N 101 
AR6 C2D   O2D    sing N N 102 
AR6 C2D   C3D    sing N N 103 
AR6 "C3'" "O3'"  sing N N 104 
AR6 "C3'" "C4'"  sing N N 105 
AR6 C3D   O3D    sing N N 106 
AR6 C3D   C4D    sing N N 107 
AR6 "C4'" "O4'"  sing N N 108 
AR6 "C4'" "C5'"  sing N N 109 
AR6 C4D   O4D    sing N N 110 
AR6 C4D   C5D    sing N N 111 
AR6 "C5'" "O5'"  sing N N 112 
AR6 C5D   O5D    sing N N 113 
AR6 C2    H2     sing N N 114 
AR6 N6    HN6    sing N N 115 
AR6 N6    HN6A   sing N N 116 
AR6 C8    H8     sing N N 117 
AR6 "C1'" "H1'"  sing N N 118 
AR6 C1D   H1D    sing N N 119 
AR6 "C2'" "H2'"  sing N N 120 
AR6 "O2'" "HO2'" sing N N 121 
AR6 C2D   H2D    sing N N 122 
AR6 O2D   HO2D   sing N N 123 
AR6 "C3'" "H3'"  sing N N 124 
AR6 "O3'" "HO3'" sing N N 125 
AR6 C3D   H3D    sing N N 126 
AR6 O3D   HO3D   sing N N 127 
AR6 "C4'" "H4'"  sing N N 128 
AR6 C4D   H4D    sing N N 129 
AR6 "C5'" "H5'"  sing N N 130 
AR6 "C5'" "H5'A" sing N N 131 
AR6 C5D   H5D    sing N N 132 
AR6 C5D   H5DA   sing N N 133 
AR6 O1A   H1A    sing N N 134 
AR6 O1B   H1B    sing N N 135 
AR6 O1D   HD1    sing N N 136 
ARG N     CA     sing N N 137 
ARG N     H      sing N N 138 
ARG N     H2     sing N N 139 
ARG CA    C      sing N N 140 
ARG CA    CB     sing N N 141 
ARG CA    HA     sing N N 142 
ARG C     O      doub N N 143 
ARG C     OXT    sing N N 144 
ARG CB    CG     sing N N 145 
ARG CB    HB2    sing N N 146 
ARG CB    HB3    sing N N 147 
ARG CG    CD     sing N N 148 
ARG CG    HG2    sing N N 149 
ARG CG    HG3    sing N N 150 
ARG CD    NE     sing N N 151 
ARG CD    HD2    sing N N 152 
ARG CD    HD3    sing N N 153 
ARG NE    CZ     sing N N 154 
ARG NE    HE     sing N N 155 
ARG CZ    NH1    sing N N 156 
ARG CZ    NH2    doub N N 157 
ARG NH1   HH11   sing N N 158 
ARG NH1   HH12   sing N N 159 
ARG NH2   HH21   sing N N 160 
ARG NH2   HH22   sing N N 161 
ARG OXT   HXT    sing N N 162 
ASN N     CA     sing N N 163 
ASN N     H      sing N N 164 
ASN N     H2     sing N N 165 
ASN CA    C      sing N N 166 
ASN CA    CB     sing N N 167 
ASN CA    HA     sing N N 168 
ASN C     O      doub N N 169 
ASN C     OXT    sing N N 170 
ASN CB    CG     sing N N 171 
ASN CB    HB2    sing N N 172 
ASN CB    HB3    sing N N 173 
ASN CG    OD1    doub N N 174 
ASN CG    ND2    sing N N 175 
ASN ND2   HD21   sing N N 176 
ASN ND2   HD22   sing N N 177 
ASN OXT   HXT    sing N N 178 
ASP N     CA     sing N N 179 
ASP N     H      sing N N 180 
ASP N     H2     sing N N 181 
ASP CA    C      sing N N 182 
ASP CA    CB     sing N N 183 
ASP CA    HA     sing N N 184 
ASP C     O      doub N N 185 
ASP C     OXT    sing N N 186 
ASP CB    CG     sing N N 187 
ASP CB    HB2    sing N N 188 
ASP CB    HB3    sing N N 189 
ASP CG    OD1    doub N N 190 
ASP CG    OD2    sing N N 191 
ASP OD2   HD2    sing N N 192 
ASP OXT   HXT    sing N N 193 
CYS N     CA     sing N N 194 
CYS N     H      sing N N 195 
CYS N     H2     sing N N 196 
CYS CA    C      sing N N 197 
CYS CA    CB     sing N N 198 
CYS CA    HA     sing N N 199 
CYS C     O      doub N N 200 
CYS C     OXT    sing N N 201 
CYS CB    SG     sing N N 202 
CYS CB    HB2    sing N N 203 
CYS CB    HB3    sing N N 204 
CYS SG    HG     sing N N 205 
CYS OXT   HXT    sing N N 206 
GLN N     CA     sing N N 207 
GLN N     H      sing N N 208 
GLN N     H2     sing N N 209 
GLN CA    C      sing N N 210 
GLN CA    CB     sing N N 211 
GLN CA    HA     sing N N 212 
GLN C     O      doub N N 213 
GLN C     OXT    sing N N 214 
GLN CB    CG     sing N N 215 
GLN CB    HB2    sing N N 216 
GLN CB    HB3    sing N N 217 
GLN CG    CD     sing N N 218 
GLN CG    HG2    sing N N 219 
GLN CG    HG3    sing N N 220 
GLN CD    OE1    doub N N 221 
GLN CD    NE2    sing N N 222 
GLN NE2   HE21   sing N N 223 
GLN NE2   HE22   sing N N 224 
GLN OXT   HXT    sing N N 225 
GLU N     CA     sing N N 226 
GLU N     H      sing N N 227 
GLU N     H2     sing N N 228 
GLU CA    C      sing N N 229 
GLU CA    CB     sing N N 230 
GLU CA    HA     sing N N 231 
GLU C     O      doub N N 232 
GLU C     OXT    sing N N 233 
GLU CB    CG     sing N N 234 
GLU CB    HB2    sing N N 235 
GLU CB    HB3    sing N N 236 
GLU CG    CD     sing N N 237 
GLU CG    HG2    sing N N 238 
GLU CG    HG3    sing N N 239 
GLU CD    OE1    doub N N 240 
GLU CD    OE2    sing N N 241 
GLU OE2   HE2    sing N N 242 
GLU OXT   HXT    sing N N 243 
GLY N     CA     sing N N 244 
GLY N     H      sing N N 245 
GLY N     H2     sing N N 246 
GLY CA    C      sing N N 247 
GLY CA    HA2    sing N N 248 
GLY CA    HA3    sing N N 249 
GLY C     O      doub N N 250 
GLY C     OXT    sing N N 251 
GLY OXT   HXT    sing N N 252 
HIS N     CA     sing N N 253 
HIS N     H      sing N N 254 
HIS N     H2     sing N N 255 
HIS CA    C      sing N N 256 
HIS CA    CB     sing N N 257 
HIS CA    HA     sing N N 258 
HIS C     O      doub N N 259 
HIS C     OXT    sing N N 260 
HIS CB    CG     sing N N 261 
HIS CB    HB2    sing N N 262 
HIS CB    HB3    sing N N 263 
HIS CG    ND1    sing Y N 264 
HIS CG    CD2    doub Y N 265 
HIS ND1   CE1    doub Y N 266 
HIS ND1   HD1    sing N N 267 
HIS CD2   NE2    sing Y N 268 
HIS CD2   HD2    sing N N 269 
HIS CE1   NE2    sing Y N 270 
HIS CE1   HE1    sing N N 271 
HIS NE2   HE2    sing N N 272 
HIS OXT   HXT    sing N N 273 
HOH O     H1     sing N N 274 
HOH O     H2     sing N N 275 
ILE N     CA     sing N N 276 
ILE N     H      sing N N 277 
ILE N     H2     sing N N 278 
ILE CA    C      sing N N 279 
ILE CA    CB     sing N N 280 
ILE CA    HA     sing N N 281 
ILE C     O      doub N N 282 
ILE C     OXT    sing N N 283 
ILE CB    CG1    sing N N 284 
ILE CB    CG2    sing N N 285 
ILE CB    HB     sing N N 286 
ILE CG1   CD1    sing N N 287 
ILE CG1   HG12   sing N N 288 
ILE CG1   HG13   sing N N 289 
ILE CG2   HG21   sing N N 290 
ILE CG2   HG22   sing N N 291 
ILE CG2   HG23   sing N N 292 
ILE CD1   HD11   sing N N 293 
ILE CD1   HD12   sing N N 294 
ILE CD1   HD13   sing N N 295 
ILE OXT   HXT    sing N N 296 
LEU N     CA     sing N N 297 
LEU N     H      sing N N 298 
LEU N     H2     sing N N 299 
LEU CA    C      sing N N 300 
LEU CA    CB     sing N N 301 
LEU CA    HA     sing N N 302 
LEU C     O      doub N N 303 
LEU C     OXT    sing N N 304 
LEU CB    CG     sing N N 305 
LEU CB    HB2    sing N N 306 
LEU CB    HB3    sing N N 307 
LEU CG    CD1    sing N N 308 
LEU CG    CD2    sing N N 309 
LEU CG    HG     sing N N 310 
LEU CD1   HD11   sing N N 311 
LEU CD1   HD12   sing N N 312 
LEU CD1   HD13   sing N N 313 
LEU CD2   HD21   sing N N 314 
LEU CD2   HD22   sing N N 315 
LEU CD2   HD23   sing N N 316 
LEU OXT   HXT    sing N N 317 
LYS N     CA     sing N N 318 
LYS N     H      sing N N 319 
LYS N     H2     sing N N 320 
LYS CA    C      sing N N 321 
LYS CA    CB     sing N N 322 
LYS CA    HA     sing N N 323 
LYS C     O      doub N N 324 
LYS C     OXT    sing N N 325 
LYS CB    CG     sing N N 326 
LYS CB    HB2    sing N N 327 
LYS CB    HB3    sing N N 328 
LYS CG    CD     sing N N 329 
LYS CG    HG2    sing N N 330 
LYS CG    HG3    sing N N 331 
LYS CD    CE     sing N N 332 
LYS CD    HD2    sing N N 333 
LYS CD    HD3    sing N N 334 
LYS CE    NZ     sing N N 335 
LYS CE    HE2    sing N N 336 
LYS CE    HE3    sing N N 337 
LYS NZ    HZ1    sing N N 338 
LYS NZ    HZ2    sing N N 339 
LYS NZ    HZ3    sing N N 340 
LYS OXT   HXT    sing N N 341 
MET N     CA     sing N N 342 
MET N     H      sing N N 343 
MET N     H2     sing N N 344 
MET CA    C      sing N N 345 
MET CA    CB     sing N N 346 
MET CA    HA     sing N N 347 
MET C     O      doub N N 348 
MET C     OXT    sing N N 349 
MET CB    CG     sing N N 350 
MET CB    HB2    sing N N 351 
MET CB    HB3    sing N N 352 
MET CG    SD     sing N N 353 
MET CG    HG2    sing N N 354 
MET CG    HG3    sing N N 355 
MET SD    CE     sing N N 356 
MET CE    HE1    sing N N 357 
MET CE    HE2    sing N N 358 
MET CE    HE3    sing N N 359 
MET OXT   HXT    sing N N 360 
PHE N     CA     sing N N 361 
PHE N     H      sing N N 362 
PHE N     H2     sing N N 363 
PHE CA    C      sing N N 364 
PHE CA    CB     sing N N 365 
PHE CA    HA     sing N N 366 
PHE C     O      doub N N 367 
PHE C     OXT    sing N N 368 
PHE CB    CG     sing N N 369 
PHE CB    HB2    sing N N 370 
PHE CB    HB3    sing N N 371 
PHE CG    CD1    doub Y N 372 
PHE CG    CD2    sing Y N 373 
PHE CD1   CE1    sing Y N 374 
PHE CD1   HD1    sing N N 375 
PHE CD2   CE2    doub Y N 376 
PHE CD2   HD2    sing N N 377 
PHE CE1   CZ     doub Y N 378 
PHE CE1   HE1    sing N N 379 
PHE CE2   CZ     sing Y N 380 
PHE CE2   HE2    sing N N 381 
PHE CZ    HZ     sing N N 382 
PHE OXT   HXT    sing N N 383 
PRO N     CA     sing N N 384 
PRO N     CD     sing N N 385 
PRO N     H      sing N N 386 
PRO CA    C      sing N N 387 
PRO CA    CB     sing N N 388 
PRO CA    HA     sing N N 389 
PRO C     O      doub N N 390 
PRO C     OXT    sing N N 391 
PRO CB    CG     sing N N 392 
PRO CB    HB2    sing N N 393 
PRO CB    HB3    sing N N 394 
PRO CG    CD     sing N N 395 
PRO CG    HG2    sing N N 396 
PRO CG    HG3    sing N N 397 
PRO CD    HD2    sing N N 398 
PRO CD    HD3    sing N N 399 
PRO OXT   HXT    sing N N 400 
SER N     CA     sing N N 401 
SER N     H      sing N N 402 
SER N     H2     sing N N 403 
SER CA    C      sing N N 404 
SER CA    CB     sing N N 405 
SER CA    HA     sing N N 406 
SER C     O      doub N N 407 
SER C     OXT    sing N N 408 
SER CB    OG     sing N N 409 
SER CB    HB2    sing N N 410 
SER CB    HB3    sing N N 411 
SER OG    HG     sing N N 412 
SER OXT   HXT    sing N N 413 
THR N     CA     sing N N 414 
THR N     H      sing N N 415 
THR N     H2     sing N N 416 
THR CA    C      sing N N 417 
THR CA    CB     sing N N 418 
THR CA    HA     sing N N 419 
THR C     O      doub N N 420 
THR C     OXT    sing N N 421 
THR CB    OG1    sing N N 422 
THR CB    CG2    sing N N 423 
THR CB    HB     sing N N 424 
THR OG1   HG1    sing N N 425 
THR CG2   HG21   sing N N 426 
THR CG2   HG22   sing N N 427 
THR CG2   HG23   sing N N 428 
THR OXT   HXT    sing N N 429 
TRP N     CA     sing N N 430 
TRP N     H      sing N N 431 
TRP N     H2     sing N N 432 
TRP CA    C      sing N N 433 
TRP CA    CB     sing N N 434 
TRP CA    HA     sing N N 435 
TRP C     O      doub N N 436 
TRP C     OXT    sing N N 437 
TRP CB    CG     sing N N 438 
TRP CB    HB2    sing N N 439 
TRP CB    HB3    sing N N 440 
TRP CG    CD1    doub Y N 441 
TRP CG    CD2    sing Y N 442 
TRP CD1   NE1    sing Y N 443 
TRP CD1   HD1    sing N N 444 
TRP CD2   CE2    doub Y N 445 
TRP CD2   CE3    sing Y N 446 
TRP NE1   CE2    sing Y N 447 
TRP NE1   HE1    sing N N 448 
TRP CE2   CZ2    sing Y N 449 
TRP CE3   CZ3    doub Y N 450 
TRP CE3   HE3    sing N N 451 
TRP CZ2   CH2    doub Y N 452 
TRP CZ2   HZ2    sing N N 453 
TRP CZ3   CH2    sing Y N 454 
TRP CZ3   HZ3    sing N N 455 
TRP CH2   HH2    sing N N 456 
TRP OXT   HXT    sing N N 457 
TYR N     CA     sing N N 458 
TYR N     H      sing N N 459 
TYR N     H2     sing N N 460 
TYR CA    C      sing N N 461 
TYR CA    CB     sing N N 462 
TYR CA    HA     sing N N 463 
TYR C     O      doub N N 464 
TYR C     OXT    sing N N 465 
TYR CB    CG     sing N N 466 
TYR CB    HB2    sing N N 467 
TYR CB    HB3    sing N N 468 
TYR CG    CD1    doub Y N 469 
TYR CG    CD2    sing Y N 470 
TYR CD1   CE1    sing Y N 471 
TYR CD1   HD1    sing N N 472 
TYR CD2   CE2    doub Y N 473 
TYR CD2   HD2    sing N N 474 
TYR CE1   CZ     doub Y N 475 
TYR CE1   HE1    sing N N 476 
TYR CE2   CZ     sing Y N 477 
TYR CE2   HE2    sing N N 478 
TYR CZ    OH     sing N N 479 
TYR OH    HH     sing N N 480 
TYR OXT   HXT    sing N N 481 
VAL N     CA     sing N N 482 
VAL N     H      sing N N 483 
VAL N     H2     sing N N 484 
VAL CA    C      sing N N 485 
VAL CA    CB     sing N N 486 
VAL CA    HA     sing N N 487 
VAL C     O      doub N N 488 
VAL C     OXT    sing N N 489 
VAL CB    CG1    sing N N 490 
VAL CB    CG2    sing N N 491 
VAL CB    HB     sing N N 492 
VAL CG1   HG11   sing N N 493 
VAL CG1   HG12   sing N N 494 
VAL CG1   HG13   sing N N 495 
VAL CG2   HG21   sing N N 496 
VAL CG2   HG22   sing N N 497 
VAL CG2   HG23   sing N N 498 
VAL OXT   HXT    sing N N 499 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'European Union (EU)'                'European Union' 101087215-ESPERANCE    1 
'European Union (EU)'                'European Union' 871037-iNEXT-Discovery 2 
'European Regional Development Fund' 'European Union' 5002550-INSPIRED       3 
'European Union (EU)'                'European Union' 101159708-MILESTONE    4 
# 
_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   5AIL 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9QYF 
_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]   0.019178 
_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]   0.019178 
_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]   0.007567 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . SER A 1 8   ? -14.585 7.201  -21.875 1.00 48.42 ? 308 SER A N     1 
ATOM   2    C CA    . SER A 1 8   ? -14.286 7.402  -20.438 1.00 43.48 ? 308 SER A CA    1 
ATOM   3    C C     . SER A 1 8   ? -15.497 8.075  -19.808 1.00 39.27 ? 308 SER A C     1 
ATOM   4    O O     . SER A 1 8   ? -16.246 8.734  -20.522 1.00 48.82 ? 308 SER A O     1 
ATOM   5    C CB    . SER A 1 8   ? -13.040 8.234  -20.268 1.00 48.43 ? 308 SER A CB    1 
ATOM   6    O OG    . SER A 1 8   ? -12.510 8.060  -18.966 1.00 54.05 ? 308 SER A OG    1 
ATOM   7    N N     . PHE A 1 9   ? -15.716 7.861  -18.504 1.00 27.20 ? 309 PHE A N     1 
ATOM   8    C CA    . PHE A 1 9   ? -16.796 8.537  -17.799 1.00 21.58 ? 309 PHE A CA    1 
ATOM   9    C C     . PHE A 1 9   ? -16.402 8.744  -16.335 1.00 20.77 ? 309 PHE A C     1 
ATOM   10   O O     . PHE A 1 9   ? -15.541 8.031  -15.793 1.00 25.00 ? 309 PHE A O     1 
ATOM   11   C CB    . PHE A 1 9   ? -18.151 7.835  -17.925 1.00 26.55 ? 309 PHE A CB    1 
ATOM   12   C CG    . PHE A 1 9   ? -18.091 6.361  -17.591 1.00 28.83 ? 309 PHE A CG    1 
ATOM   13   C CD1   . PHE A 1 9   ? -18.102 5.932  -16.263 1.00 33.78 ? 309 PHE A CD1   1 
ATOM   14   C CD2   . PHE A 1 9   ? -18.124 5.399  -18.602 1.00 32.38 ? 309 PHE A CD2   1 
ATOM   15   C CE1   . PHE A 1 9   ? -18.056 4.567  -15.952 1.00 33.55 ? 309 PHE A CE1   1 
ATOM   16   C CE2   . PHE A 1 9   ? -18.094 4.040  -18.282 1.00 36.55 ? 309 PHE A CE2   1 
ATOM   17   C CZ    . PHE A 1 9   ? -18.060 3.632  -16.963 1.00 35.59 ? 309 PHE A CZ    1 
ATOM   18   N N     . ASN A 1 10  ? -17.018 9.772  -15.723 1.00 18.25 ? 310 ASN A N     1 
ATOM   19   C CA    . ASN A 1 10  ? -16.731 10.150 -14.351 1.00 17.46 ? 310 ASN A CA    1 
ATOM   20   C C     . ASN A 1 10  ? -17.985 10.357 -13.501 1.00 16.52 ? 310 ASN A C     1 
ATOM   21   O O     . ASN A 1 10  ? -17.874 10.737 -12.350 1.00 18.67 ? 310 ASN A O     1 
ATOM   22   C CB    . ASN A 1 10  ? -15.763 11.321 -14.291 1.00 19.13 ? 310 ASN A CB    1 
ATOM   23   C CG    . ASN A 1 10  ? -16.217 12.569 -15.011 1.00 22.25 ? 310 ASN A CG    1 
ATOM   24   O OD1   . ASN A 1 10  ? -17.262 12.625 -15.630 1.00 22.68 ? 310 ASN A OD1   1 
ATOM   25   N ND2   . ASN A 1 10  ? -15.395 13.607 -14.991 1.00 28.99 ? 310 ASN A ND2   1 
ATOM   26   N N     . ALA A 1 11  ? -19.168 10.076 -14.051 1.00 14.28 ? 311 ALA A N     1 
ATOM   27   C CA    . ALA A 1 11  ? -20.386 10.227 -13.276 1.00 14.30 ? 311 ALA A CA    1 
ATOM   28   C C     . ALA A 1 11  ? -21.325 9.047  -13.566 1.00 14.51 ? 311 ALA A C     1 
ATOM   29   O O     . ALA A 1 11  ? -21.317 8.514  -14.678 1.00 16.08 ? 311 ALA A O     1 
ATOM   30   C CB    . ALA A 1 11  ? -21.030 11.527 -13.598 1.00 15.92 ? 311 ALA A CB    1 
ATOM   31   N N     . MET A 1 12  ? -22.168 8.688  -12.577 1.00 15.50 ? 312 MET A N     1 
ATOM   32   C CA    . MET A 1 12  ? -23.211 7.676  -12.733 1.00 15.88 ? 312 MET A CA    1 
ATOM   33   C C     . MET A 1 12  ? -24.431 8.173  -11.976 1.00 15.29 ? 312 MET A C     1 
ATOM   34   O O     . MET A 1 12  ? -24.311 8.881  -11.000 1.00 15.83 ? 312 MET A O     1 
ATOM   35   C CB    . MET A 1 12  ? -22.761 6.314  -12.194 1.00 16.12 ? 312 MET A CB    1 
ATOM   36   C CG    . MET A 1 12  ? -22.704 6.175  -10.709 1.00 18.16 ? 312 MET A CG    1 
ATOM   37   S SD    . MET A 1 12  ? -21.874 4.662  -10.113 1.00 21.00 ? 312 MET A SD    1 
ATOM   38   C CE    . MET A 1 12  ? -22.750 4.559  -8.547  1.00 24.03 ? 312 MET A CE    1 
ATOM   39   N N     . VAL A 1 13  ? -25.604 7.738  -12.414 1.00 13.80 ? 313 VAL A N     1 
ATOM   40   C CA    . VAL A 1 13  ? -26.846 8.029  -11.724 1.00 14.86 ? 313 VAL A CA    1 
ATOM   41   C C     . VAL A 1 13  ? -27.514 6.704  -11.353 1.00 14.29 ? 313 VAL A C     1 
ATOM   42   O O     . VAL A 1 13  ? -27.593 5.810  -12.202 1.00 14.30 ? 313 VAL A O     1 
ATOM   43   C CB    . VAL A 1 13  ? -27.775 8.897  -12.595 1.00 15.48 ? 313 VAL A CB    1 
ATOM   44   C CG1   . VAL A 1 13  ? -29.026 9.267  -11.832 1.00 16.52 ? 313 VAL A CG1   1 
ATOM   45   C CG2   . VAL A 1 13  ? -27.051 10.154 -13.041 1.00 16.28 ? 313 VAL A CG2   1 
ATOM   46   N N     . VAL A 1 14  ? -27.923 6.589  -10.083 1.00 14.19 ? 314 VAL A N     1 
ATOM   47   C CA    . VAL A 1 14  ? -28.587 5.401  -9.598  1.00 14.66 ? 314 VAL A CA    1 
ATOM   48   C C     . VAL A 1 14  ? -29.761 5.840  -8.724  1.00 14.28 ? 314 VAL A C     1 
ATOM   49   O O     . VAL A 1 14  ? -29.588 6.534  -7.732  1.00 14.28 ? 314 VAL A O     1 
ATOM   50   C CB    . VAL A 1 14  ? -27.631 4.454  -8.856  1.00 15.82 ? 314 VAL A CB    1 
ATOM   51   C CG1   . VAL A 1 14  ? -26.850 5.123  -7.726  1.00 16.90 ? 314 VAL A CG1   1 
ATOM   52   C CG2   . VAL A 1 14  ? -28.327 3.194  -8.338  1.00 16.41 ? 314 VAL A CG2   1 
ATOM   53   N N     . ASN A 1 15  ? -30.977 5.434  -9.092  1.00 15.81 ? 315 ASN A N     1 
ATOM   54   C CA    . ASN A 1 15  ? -32.199 5.831  -8.393  1.00 15.30 ? 315 ASN A CA    1 
ATOM   55   C C     . ASN A 1 15  ? -32.226 7.366  -8.291  1.00 14.46 ? 315 ASN A C     1 
ATOM   56   O O     . ASN A 1 15  ? -32.273 8.023  -9.321  1.00 17.71 ? 315 ASN A O     1 
ATOM   57   C CB    . ASN A 1 15  ? -32.317 5.075  -7.067  1.00 15.53 ? 315 ASN A CB    1 
ATOM   58   C CG    . ASN A 1 15  ? -32.432 3.572  -7.211  1.00 18.71 ? 315 ASN A CG    1 
ATOM   59   O OD1   . ASN A 1 15  ? -32.777 3.076  -8.274  1.00 22.47 ? 315 ASN A OD1   1 
ATOM   60   N ND2   . ASN A 1 15  ? -32.281 2.854  -6.108  1.00 19.00 ? 315 ASN A ND2   1 
ATOM   61   N N     . ASN A 1 16  ? -32.219 7.913  -7.067  1.00 13.64 ? 316 ASN A N     1 
ATOM   62   C CA    . ASN A 1 16  ? -32.200 9.356  -6.830  1.00 14.06 ? 316 ASN A CA    1 
ATOM   63   C C     . ASN A 1 16  ? -30.843 9.915  -6.430  1.00 14.83 ? 316 ASN A C     1 
ATOM   64   O O     . ASN A 1 16  ? -30.766 11.055 -5.963  1.00 16.58 ? 316 ASN A O     1 
ATOM   65   C CB    . ASN A 1 16  ? -33.216 9.752  -5.763  1.00 15.57 ? 316 ASN A CB    1 
ATOM   66   C CG    . ASN A 1 16  ? -34.503 10.289 -6.316  1.00 16.17 ? 316 ASN A CG    1 
ATOM   67   O OD1   . ASN A 1 16  ? -34.531 10.922 -7.368  1.00 16.44 ? 316 ASN A OD1   1 
ATOM   68   N ND2   . ASN A 1 16  ? -35.582 9.990  -5.624  1.00 21.50 ? 316 ASN A ND2   1 
ATOM   69   N N     . LEU A 1 17  ? -29.785 9.188  -6.746  1.00 13.70 ? 317 LEU A N     1 
ATOM   70   C CA    . LEU A 1 17  ? -28.443 9.568  -6.371  1.00 13.80 ? 317 LEU A CA    1 
ATOM   71   C C     . LEU A 1 17  ? -27.564 9.735  -7.604  1.00 13.83 ? 317 LEU A C     1 
ATOM   72   O O     . LEU A 1 17  ? -27.563 8.909  -8.520  1.00 14.50 ? 317 LEU A O     1 
ATOM   73   C CB    . LEU A 1 17  ? -27.911 8.590  -5.358  1.00 13.98 ? 317 LEU A CB    1 
ATOM   74   C CG    . LEU A 1 17  ? -26.586 8.962  -4.739  1.00 14.91 ? 317 LEU A CG    1 
ATOM   75   C CD1   . LEU A 1 17  ? -26.505 8.440  -3.323  1.00 14.80 ? 317 LEU A CD1   1 
ATOM   76   C CD2   . LEU A 1 17  ? -25.450 8.432  -5.581  1.00 15.44 ? 317 LEU A CD2   1 
ATOM   77   N N     . THR A 1 18  ? -26.828 10.864 -7.598  1.00 12.90 ? 318 THR A N     1 
ATOM   78   C CA    . THR A 1 18  ? -25.812 11.142 -8.596  1.00 13.45 ? 318 THR A CA    1 
ATOM   79   C C     . THR A 1 18  ? -24.438 11.034 -7.931  1.00 14.27 ? 318 THR A C     1 
ATOM   80   O O     . THR A 1 18  ? -24.233 11.589 -6.866  1.00 16.07 ? 318 THR A O     1 
ATOM   81   C CB    . THR A 1 18  ? -26.011 12.517 -9.209  1.00 15.53 ? 318 THR A CB    1 
ATOM   82   O OG1   . THR A 1 18  ? -27.328 12.590 -9.772  1.00 17.33 ? 318 THR A OG1   1 
ATOM   83   C CG2   . THR A 1 18  ? -24.965 12.810 -10.255 1.00 17.06 ? 318 THR A CG2   1 
ATOM   84   N N     . LEU A 1 19  ? -23.565 10.228 -8.532  1.00 14.75 ? 319 LEU A N     1 
ATOM   85   C CA    . LEU A 1 19  ? -22.209 10.101 -8.022  1.00 15.82 ? 319 LEU A CA    1 
ATOM   86   C C     . LEU A 1 19  ? -21.219 10.563 -9.096  1.00 15.91 ? 319 LEU A C     1 
ATOM   87   O O     . LEU A 1 19  ? -21.265 10.081 -10.219 1.00 16.58 ? 319 LEU A O     1 
ATOM   88   C CB    . LEU A 1 19  ? -21.932 8.652  -7.639  1.00 16.44 ? 319 LEU A CB    1 
ATOM   89   C CG    . LEU A 1 19  ? -20.510 8.396  -7.090  1.00 17.56 ? 319 LEU A CG    1 
ATOM   90   C CD1   . LEU A 1 19  ? -20.196 9.124  -5.818  1.00 18.27 ? 319 LEU A CD1   1 
ATOM   91   C CD2   . LEU A 1 19  ? -20.287 6.925  -6.861  1.00 18.80 ? 319 LEU A CD2   1 
ATOM   92   N N     . GLN A 1 20  ? -20.293 11.469 -8.723  1.00 15.02 ? 320 GLN A N     1 
ATOM   93   C CA    . GLN A 1 20  ? -19.294 11.938 -9.654  1.00 15.41 ? 320 GLN A CA    1 
ATOM   94   C C     . GLN A 1 20  ? -17.914 11.839 -9.003  1.00 15.91 ? 320 GLN A C     1 
ATOM   95   O O     . GLN A 1 20  ? -17.782 12.101 -7.825  1.00 17.01 ? 320 GLN A O     1 
ATOM   96   C CB    . GLN A 1 20  ? -19.455 13.420 -9.952  1.00 18.98 ? 320 GLN A CB    1 
ATOM   97   C CG    . GLN A 1 20  ? -20.713 13.830 -10.662 1.00 24.86 ? 320 GLN A CG    1 
ATOM   98   C CD    . GLN A 1 20  ? -20.693 15.306 -10.985 1.00 29.54 ? 320 GLN A CD    1 
ATOM   99   O OE1   . GLN A 1 20  ? -19.691 15.846 -11.482 1.00 34.05 ? 320 GLN A OE1   1 
ATOM   100  N NE2   . GLN A 1 20  ? -21.790 15.969 -10.638 1.00 35.54 ? 320 GLN A NE2   1 
ATOM   101  N N     . ILE A 1 21  ? -16.922 11.405 -9.795  1.00 15.05 ? 321 ILE A N     1 
ATOM   102  C CA    . ILE A 1 21  ? -15.535 11.475 -9.403  1.00 15.65 ? 321 ILE A CA    1 
ATOM   103  C C     . ILE A 1 21  ? -14.913 12.717 -10.027 1.00 16.54 ? 321 ILE A C     1 
ATOM   104  O O     . ILE A 1 21  ? -15.029 12.940 -11.225 1.00 18.47 ? 321 ILE A O     1 
ATOM   105  C CB    . ILE A 1 21  ? -14.772 10.206 -9.800  1.00 17.47 ? 321 ILE A CB    1 
ATOM   106  C CG1   . ILE A 1 21  ? -15.411 8.945  -9.300  1.00 20.42 ? 321 ILE A CG1   1 
ATOM   107  C CG2   . ILE A 1 21  ? -13.316 10.322 -9.369  1.00 22.01 ? 321 ILE A CG2   1 
ATOM   108  C CD1   . ILE A 1 21  ? -15.008 7.759  -10.139 1.00 21.76 ? 321 ILE A CD1   1 
ATOM   109  N N     . VAL A 1 22  ? -14.306 13.508 -9.156  1.00 17.10 ? 322 VAL A N     1 
ATOM   110  C CA    . VAL A 1 22  ? -13.728 14.789 -9.510  1.00 18.28 ? 322 VAL A CA    1 
ATOM   111  C C     . VAL A 1 22  ? -12.234 14.760 -9.193  1.00 18.62 ? 322 VAL A C     1 
ATOM   112  O O     . VAL A 1 22  ? -11.843 14.217 -8.188  1.00 20.88 ? 322 VAL A O     1 
ATOM   113  C CB    . VAL A 1 22  ? -14.415 15.942 -8.739  1.00 22.65 ? 322 VAL A CB    1 
ATOM   114  C CG1   . VAL A 1 22  ? -13.693 17.253 -8.910  1.00 26.49 ? 322 VAL A CG1   1 
ATOM   115  C CG2   . VAL A 1 22  ? -15.878 16.033 -9.142  1.00 25.98 ? 322 VAL A CG2   1 
ATOM   116  N N     . GLN A 1 23  ? -11.427 15.339 -10.075 1.00 18.75 ? 323 GLN A N     1 
ATOM   117  C CA    . GLN A 1 23  ? -10.032 15.613 -9.783  1.00 20.05 ? 323 GLN A CA    1 
ATOM   118  C C     . GLN A 1 23  ? -9.931  17.068 -9.338  1.00 19.32 ? 323 GLN A C     1 
ATOM   119  O O     . GLN A 1 23  ? -10.167 17.972 -10.130 1.00 23.42 ? 323 GLN A O     1 
ATOM   120  C CB    . GLN A 1 23  ? -9.140  15.346 -10.993 1.00 21.82 ? 323 GLN A CB    1 
ATOM   121  C CG    . GLN A 1 23  ? -9.085  13.866 -11.333 1.00 23.54 ? 323 GLN A CG    1 
ATOM   122  C CD    . GLN A 1 23  ? -8.456  13.576 -12.677 1.00 27.44 ? 323 GLN A CD    1 
ATOM   123  O OE1   . GLN A 1 23  ? -8.834  14.118 -13.717 1.00 37.62 ? 323 GLN A OE1   1 
ATOM   124  N NE2   . GLN A 1 23  ? -7.445  12.736 -12.675 1.00 28.11 ? 323 GLN A NE2   1 
ATOM   125  N N     . GLY A 1 24  ? -9.592  17.257 -8.068  1.00 18.89 ? 324 GLY A N     1 
ATOM   126  C CA    . GLY A 1 24  ? -9.509  18.605 -7.528  1.00 17.37 ? 324 GLY A CA    1 
ATOM   127  C C     . GLY A 1 24  ? -9.199  18.642 -6.035  1.00 17.13 ? 324 GLY A C     1 
ATOM   128  O O     . GLY A 1 24  ? -8.798  17.651 -5.430  1.00 19.39 ? 324 GLY A O     1 
ATOM   129  N N     . HIS A 1 25  ? -9.463  19.813 -5.453  1.00 18.62 ? 325 HIS A N     1 
ATOM   130  C CA    . HIS A 1 25  ? -9.175  20.115 -4.069  1.00 17.74 ? 325 HIS A CA    1 
ATOM   131  C C     . HIS A 1 25  ? -10.466 20.066 -3.276  1.00 16.53 ? 325 HIS A C     1 
ATOM   132  O O     . HIS A 1 25  ? -11.415 20.780 -3.619  1.00 16.88 ? 325 HIS A O     1 
ATOM   133  C CB    . HIS A 1 25  ? -8.545  21.510 -3.957  1.00 19.70 ? 325 HIS A CB    1 
ATOM   134  C CG    . HIS A 1 25  ? -7.143  21.591 -4.454  1.00 20.90 ? 325 HIS A CG    1 
ATOM   135  N ND1   . HIS A 1 25  ? -6.129  22.003 -3.619  1.00 22.41 ? 325 HIS A ND1   1 
ATOM   136  C CD2   . HIS A 1 25  ? -6.597  21.321 -5.646  1.00 20.49 ? 325 HIS A CD2   1 
ATOM   137  C CE1   . HIS A 1 25  ? -4.991  21.989 -4.314  1.00 24.66 ? 325 HIS A CE1   1 
ATOM   138  N NE2   . HIS A 1 25  ? -5.254  21.601 -5.546  1.00 23.40 ? 325 HIS A NE2   1 
ATOM   139  N N     . ILE A 1 26  ? -10.490 19.273 -2.198  1.00 16.03 ? 326 ILE A N     1 
ATOM   140  C CA    . ILE A 1 26  ? -11.695 19.158 -1.382  1.00 17.02 ? 326 ILE A CA    1 
ATOM   141  C C     . ILE A 1 26  ? -12.115 20.518 -0.834  1.00 15.80 ? 326 ILE A C     1 
ATOM   142  O O     . ILE A 1 26  ? -13.333 20.807 -0.775  1.00 17.39 ? 326 ILE A O     1 
ATOM   143  C CB    . ILE A 1 26  ? -11.501 18.104 -0.279  1.00 15.59 ? 326 ILE A CB    1 
ATOM   144  C CG1   . ILE A 1 26  ? -12.805 17.761 0.449   1.00 15.79 ? 326 ILE A CG1   1 
ATOM   145  C CG2   . ILE A 1 26  ? -10.447 18.499 0.746   1.00 16.84 ? 326 ILE A CG2   1 
ATOM   146  C CD1   . ILE A 1 26  ? -13.912 17.135 -0.386  1.00 17.57 ? 326 ILE A CD1   1 
ATOM   147  N N     . GLU A 1 27  ? -11.119 21.364 -0.485  1.00 16.57 ? 327 GLU A N     1 
ATOM   148  C CA    . GLU A 1 27  ? -11.437 22.608 0.178   1.00 17.90 ? 327 GLU A CA    1 
ATOM   149  C C     . GLU A 1 27  ? -12.020 23.671 -0.756  1.00 17.38 ? 327 GLU A C     1 
ATOM   150  O O     . GLU A 1 27  ? -12.476 24.723 -0.289  1.00 19.33 ? 327 GLU A O     1 
ATOM   151  C CB    . GLU A 1 27  ? -10.250 23.170 0.934   1.00 17.69 ? 327 GLU A CB    1 
ATOM   152  C CG    . GLU A 1 27  ? -9.106  23.681 0.075   1.00 18.97 ? 327 GLU A CG    1 
ATOM   153  C CD    . GLU A 1 27  ? -8.156  22.689 -0.551  1.00 18.47 ? 327 GLU A CD    1 
ATOM   154  O OE1   . GLU A 1 27  ? -8.469  21.488 -0.625  1.00 16.58 ? 327 GLU A OE1   1 
ATOM   155  O OE2   . GLU A 1 27  ? -7.021  23.110 -0.864  1.00 21.39 ? 327 GLU A OE2   1 
ATOM   156  N N     . TRP A 1 28  ? -12.004 23.413 -2.068  1.00 17.96 ? 328 TRP A N     1 
ATOM   157  C CA    . TRP A 1 28  ? -12.530 24.345 -3.057  1.00 19.09 ? 328 TRP A CA    1 
ATOM   158  C C     . TRP A 1 28  ? -13.873 23.889 -3.631  1.00 18.52 ? 328 TRP A C     1 
ATOM   159  O O     . TRP A 1 28  ? -14.385 24.497 -4.566  1.00 20.61 ? 328 TRP A O     1 
ATOM   160  C CB    . TRP A 1 28  ? -11.512 24.554 -4.186  1.00 21.63 ? 328 TRP A CB    1 
ATOM   161  C CG    . TRP A 1 28  ? -10.237 25.218 -3.734  1.00 24.27 ? 328 TRP A CG    1 
ATOM   162  C CD1   . TRP A 1 28  ? -10.063 26.019 -2.639  1.00 26.57 ? 328 TRP A CD1   1 
ATOM   163  C CD2   . TRP A 1 28  ? -8.958  25.197 -4.398  1.00 25.20 ? 328 TRP A CD2   1 
ATOM   164  N NE1   . TRP A 1 28  ? -8.776  26.470 -2.558  1.00 27.19 ? 328 TRP A NE1   1 
ATOM   165  C CE2   . TRP A 1 28  ? -8.078  26.003 -3.637  1.00 26.55 ? 328 TRP A CE2   1 
ATOM   166  C CE3   . TRP A 1 28  ? -8.478  24.629 -5.579  1.00 26.86 ? 328 TRP A CE3   1 
ATOM   167  C CZ2   . TRP A 1 28  ? -6.743  26.216 -4.009  1.00 27.38 ? 328 TRP A CZ2   1 
ATOM   168  C CZ3   . TRP A 1 28  ? -7.161  24.836 -5.946  1.00 28.46 ? 328 TRP A CZ3   1 
ATOM   169  C CH2   . TRP A 1 28  ? -6.304  25.625 -5.175  1.00 29.21 ? 328 TRP A CH2   1 
ATOM   170  N N     A GLN A 1 29  ? -14.438 22.806 -3.082  0.50 16.38 ? 329 GLN A N     1 
ATOM   171  N N     B GLN A 1 29  ? -14.458 22.836 -3.058  0.50 17.69 ? 329 GLN A N     1 
ATOM   172  C CA    A GLN A 1 29  ? -15.758 22.340 -3.477  0.50 16.45 ? 329 GLN A CA    1 
ATOM   173  C CA    B GLN A 1 29  ? -15.749 22.355 -3.517  0.50 18.51 ? 329 GLN A CA    1 
ATOM   174  C C     A GLN A 1 29  ? -16.844 23.347 -3.109  0.50 16.35 ? 329 GLN A C     1 
ATOM   175  C C     B GLN A 1 29  ? -16.889 23.246 -3.038  0.50 17.33 ? 329 GLN A C     1 
ATOM   176  O O     A GLN A 1 29  ? -16.711 24.122 -2.167  0.50 18.33 ? 329 GLN A O     1 
ATOM   177  O O     B GLN A 1 29  ? -16.843 23.828 -1.956  0.50 17.23 ? 329 GLN A O     1 
ATOM   178  C CB    A GLN A 1 29  ? -16.112 21.028 -2.788  0.50 15.29 ? 329 GLN A CB    1 
ATOM   179  C CB    B GLN A 1 29  ? -15.947 20.934 -3.015  0.50 19.04 ? 329 GLN A CB    1 
ATOM   180  C CG    A GLN A 1 29  ? -15.426 19.815 -3.415  0.50 14.98 ? 329 GLN A CG    1 
ATOM   181  C CG    B GLN A 1 29  ? -14.857 19.998 -3.517  0.50 20.05 ? 329 GLN A CG    1 
ATOM   182  C CD    A GLN A 1 29  ? -16.030 19.391 -4.740  0.50 14.23 ? 329 GLN A CD    1 
ATOM   183  C CD    B GLN A 1 29  ? -14.744 20.009 -5.028  0.50 19.88 ? 329 GLN A CD    1 
ATOM   184  O OE1   A GLN A 1 29  ? -17.175 18.932 -4.799  0.50 16.25 ? 329 GLN A OE1   1 
ATOM   185  O OE1   B GLN A 1 29  ? -15.759 19.792 -5.720  0.50 17.50 ? 329 GLN A OE1   1 
ATOM   186  N NE2   A GLN A 1 29  ? -15.303 19.558 -5.831  0.50 15.95 ? 329 GLN A NE2   1 
ATOM   187  N NE2   B GLN A 1 29  ? -13.519 20.267 -5.519  0.50 21.29 ? 329 GLN A NE2   1 
ATOM   188  N N     . THR A 1 30  ? -17.949 23.238 -3.850  1.00 16.42 ? 330 THR A N     1 
ATOM   189  C CA    . THR A 1 30  ? -19.242 23.828 -3.511  1.00 17.53 ? 330 THR A CA    1 
ATOM   190  C C     . THR A 1 30  ? -20.211 22.665 -3.329  1.00 17.47 ? 330 THR A C     1 
ATOM   191  O O     . THR A 1 30  ? -20.439 21.891 -4.258  1.00 19.57 ? 330 THR A O     1 
ATOM   192  C CB    . THR A 1 30  ? -19.717 24.824 -4.584  1.00 19.21 ? 330 THR A CB    1 
ATOM   193  O OG1   . THR A 1 30  ? -18.740 25.855 -4.726  1.00 21.91 ? 330 THR A OG1   1 
ATOM   194  C CG2   . THR A 1 30  ? -21.067 25.424 -4.251  1.00 20.95 ? 330 THR A CG2   1 
ATOM   195  N N     . ALA A 1 31  ? -20.711 22.516 -2.104  1.00 16.53 ? 331 ALA A N     1 
ATOM   196  C CA    . ALA A 1 31  ? -21.667 21.459 -1.797  1.00 15.77 ? 331 ALA A CA    1 
ATOM   197  C C     . ALA A 1 31  ? -22.315 21.824 -0.476  1.00 15.59 ? 331 ALA A C     1 
ATOM   198  O O     . ALA A 1 31  ? -21.786 22.668 0.236   1.00 17.39 ? 331 ALA A O     1 
ATOM   199  C CB    . ALA A 1 31  ? -21.003 20.101 -1.672  1.00 16.14 ? 331 ALA A CB    1 
ATOM   200  N N     . ASP A 1 32  ? -23.455 21.199 -0.133  1.00 14.30 ? 332 ASP A N     1 
ATOM   201  C CA    . ASP A 1 32  ? -24.010 21.453 1.172   1.00 13.66 ? 332 ASP A CA    1 
ATOM   202  C C     . ASP A 1 32  ? -23.069 21.035 2.299   1.00 13.61 ? 332 ASP A C     1 
ATOM   203  O O     . ASP A 1 32  ? -22.971 21.703 3.329   1.00 14.33 ? 332 ASP A O     1 
ATOM   204  C CB    . ASP A 1 32  ? -25.371 20.779 1.316   1.00 14.39 ? 332 ASP A CB    1 
ATOM   205  C CG    . ASP A 1 32  ? -26.456 21.253 0.375   1.00 16.16 ? 332 ASP A CG    1 
ATOM   206  O OD1   . ASP A 1 32  ? -26.363 22.437 -0.105  1.00 19.13 ? 332 ASP A OD1   1 
ATOM   207  O OD2   . ASP A 1 32  ? -27.429 20.535 0.253   1.00 18.26 ? 332 ASP A OD2   1 
ATOM   208  N N     . VAL A 1 33  ? -22.450 19.857 2.123   1.00 13.58 ? 333 VAL A N     1 
ATOM   209  C CA    . VAL A 1 33  ? -21.511 19.305 3.098   1.00 12.98 ? 333 VAL A CA    1 
ATOM   210  C C     . VAL A 1 33  ? -20.178 18.958 2.419   1.00 12.21 ? 333 VAL A C     1 
ATOM   211  O O     . VAL A 1 33  ? -20.154 18.420 1.319   1.00 13.15 ? 333 VAL A O     1 
ATOM   212  C CB    . VAL A 1 33  ? -22.056 18.035 3.758   1.00 13.22 ? 333 VAL A CB    1 
ATOM   213  C CG1   . VAL A 1 33  ? -21.040 17.360 4.657   1.00 13.78 ? 333 VAL A CG1   1 
ATOM   214  C CG2   . VAL A 1 33  ? -23.325 18.324 4.553   1.00 15.14 ? 333 VAL A CG2   1 
ATOM   215  N N     . ILE A 1 34  ? -19.089 19.298 3.099   1.00 13.30 ? 334 ILE A N     1 
ATOM   216  C CA    . ILE A 1 34  ? -17.743 18.895 2.711   1.00 13.06 ? 334 ILE A CA    1 
ATOM   217  C C     . ILE A 1 34  ? -17.231 18.075 3.884   1.00 12.58 ? 334 ILE A C     1 
ATOM   218  O O     . ILE A 1 34  ? -17.411 18.405 5.055   1.00 13.54 ? 334 ILE A O     1 
ATOM   219  C CB    . ILE A 1 34  ? -16.859 20.112 2.388   1.00 14.04 ? 334 ILE A CB    1 
ATOM   220  C CG1   . ILE A 1 34  ? -17.354 20.839 1.132   1.00 15.20 ? 334 ILE A CG1   1 
ATOM   221  C CG2   . ILE A 1 34  ? -15.403 19.666 2.227   1.00 15.37 ? 334 ILE A CG2   1 
ATOM   222  C CD1   . ILE A 1 34  ? -16.610 22.157 0.859   1.00 16.25 ? 334 ILE A CD1   1 
ATOM   223  N N     . VAL A 1 35  ? -16.596 16.950 3.559   1.00 13.69 ? 335 VAL A N     1 
ATOM   224  C CA    . VAL A 1 35  ? -16.070 16.032 4.558   1.00 13.98 ? 335 VAL A CA    1 
ATOM   225  C C     . VAL A 1 35  ? -14.573 16.217 4.788   1.00 12.64 ? 335 VAL A C     1 
ATOM   226  O O     . VAL A 1 35  ? -13.794 16.224 3.845   1.00 14.05 ? 335 VAL A O     1 
ATOM   227  C CB    . VAL A 1 35  ? -16.455 14.573 4.154   1.00 12.89 ? 335 VAL A CB    1 
ATOM   228  C CG1   . VAL A 1 35  ? -16.008 13.592 5.217   1.00 14.07 ? 335 VAL A CG1   1 
ATOM   229  C CG2   . VAL A 1 35  ? -17.940 14.445 3.939   1.00 13.53 ? 335 VAL A CG2   1 
ATOM   230  N N     . ASN A 1 36  ? -14.227 16.291 6.078   1.00 12.11 ? 336 ASN A N     1 
ATOM   231  C CA    . ASN A 1 36  ? -12.839 16.409 6.525   1.00 12.38 ? 336 ASN A CA    1 
ATOM   232  C C     . ASN A 1 36  ? -12.371 15.075 7.115   1.00 13.72 ? 336 ASN A C     1 
ATOM   233  O O     . ASN A 1 36  ? -13.190 14.226 7.410   1.00 14.42 ? 336 ASN A O     1 
ATOM   234  C CB    . ASN A 1 36  ? -12.747 17.557 7.528   1.00 13.11 ? 336 ASN A CB    1 
ATOM   235  C CG    . ASN A 1 36  ? -11.367 18.050 7.872   1.00 14.46 ? 336 ASN A CG    1 
ATOM   236  O OD1   . ASN A 1 36  ? -10.386 17.764 7.173   1.00 14.27 ? 336 ASN A OD1   1 
ATOM   237  N ND2   . ASN A 1 36  ? -11.308 18.884 8.919   1.00 13.81 ? 336 ASN A ND2   1 
ATOM   238  N N     . SER A 1 37  ? -11.073 14.952 7.355   1.00 14.42 ? 337 SER A N     1 
ATOM   239  C CA    . SER A 1 37  ? -10.480 13.740 7.876   1.00 14.50 ? 337 SER A CA    1 
ATOM   240  C C     . SER A 1 37  ? -9.398  14.125 8.887   1.00 15.77 ? 337 SER A C     1 
ATOM   241  O O     . SER A 1 37  ? -8.355  14.646 8.482   1.00 16.08 ? 337 SER A O     1 
ATOM   242  C CB    . SER A 1 37  ? -9.900  12.921 6.746   1.00 15.70 ? 337 SER A CB    1 
ATOM   243  O OG    . SER A 1 37  ? -9.595  11.598 7.183   1.00 15.58 ? 337 SER A OG    1 
ATOM   244  N N     . VAL A 1 38  ? -9.660  13.888 10.179  1.00 14.03 ? 338 VAL A N     1 
ATOM   245  C CA    . VAL A 1 38  ? -8.827  14.436 11.233  1.00 13.85 ? 338 VAL A CA    1 
ATOM   246  C C     . VAL A 1 38  ? -8.543  13.449 12.353  1.00 14.94 ? 338 VAL A C     1 
ATOM   247  O O     . VAL A 1 38  ? -9.298  12.485 12.597  1.00 14.85 ? 338 VAL A O     1 
ATOM   248  C CB    . VAL A 1 38  ? -9.479  15.683 11.862  1.00 15.48 ? 338 VAL A CB    1 
ATOM   249  C CG1   . VAL A 1 38  ? -9.729  16.800 10.853  1.00 16.52 ? 338 VAL A CG1   1 
ATOM   250  C CG2   . VAL A 1 38  ? -10.752 15.390 12.613  1.00 14.85 ? 338 VAL A CG2   1 
ATOM   251  N N     . ASN A 1 39  ? -7.502  13.792 13.097  1.00 15.33 ? 339 ASN A N     1 
ATOM   252  C CA    . ASN A 1 39  ? -7.284  13.354 14.456  1.00 15.91 ? 339 ASN A CA    1 
ATOM   253  C C     . ASN A 1 39  ? -8.043  14.322 15.348  1.00 14.28 ? 339 ASN A C     1 
ATOM   254  O O     . ASN A 1 39  ? -7.740  15.521 15.305  1.00 15.01 ? 339 ASN A O     1 
ATOM   255  C CB    . ASN A 1 39  ? -5.808  13.348 14.787  1.00 17.17 ? 339 ASN A CB    1 
ATOM   256  C CG    . ASN A 1 39  ? -5.500  12.996 16.217  1.00 18.69 ? 339 ASN A CG    1 
ATOM   257  O OD1   . ASN A 1 39  ? -6.356  12.899 17.107  1.00 18.70 ? 339 ASN A OD1   1 
ATOM   258  N ND2   . ASN A 1 39  ? -4.211  12.793 16.453  1.00 21.98 ? 339 ASN A ND2   1 
ATOM   259  N N     . PRO A 1 40  ? -9.096  13.880 16.089  1.00 14.64 ? 340 PRO A N     1 
ATOM   260  C CA    . PRO A 1 40  ? -9.875  14.798 16.904  1.00 15.66 ? 340 PRO A CA    1 
ATOM   261  C C     . PRO A 1 40  ? -9.088  15.553 17.950  1.00 15.72 ? 340 PRO A C     1 
ATOM   262  O O     . PRO A 1 40  ? -9.556  16.597 18.401  1.00 18.55 ? 340 PRO A O     1 
ATOM   263  C CB    . PRO A 1 40  ? -10.955 13.918 17.525  1.00 16.11 ? 340 PRO A CB    1 
ATOM   264  C CG    . PRO A 1 40  ? -10.326 12.541 17.594  1.00 16.56 ? 340 PRO A CG    1 
ATOM   265  C CD    . PRO A 1 40  ? -9.478  12.478 16.318  1.00 15.60 ? 340 PRO A CD    1 
ATOM   266  N N     . HIS A 1 41  ? -7.905  15.037 18.311  1.00 16.27 ? 341 HIS A N     1 
ATOM   267  C CA    . HIS A 1 41  ? -7.047  15.683 19.298  1.00 18.37 ? 341 HIS A CA    1 
ATOM   268  C C     . HIS A 1 41  ? -6.137  16.754 18.682  1.00 19.43 ? 341 HIS A C     1 
ATOM   269  O O     . HIS A 1 41  ? -5.528  17.501 19.432  1.00 20.98 ? 341 HIS A O     1 
ATOM   270  C CB    . HIS A 1 41  ? -6.255  14.616 20.067  1.00 20.34 ? 341 HIS A CB    1 
ATOM   271  C CG    . HIS A 1 41  ? -7.132  13.728 20.873  1.00 22.55 ? 341 HIS A CG    1 
ATOM   272  N ND1   . HIS A 1 41  ? -7.801  14.141 22.018  1.00 26.26 ? 341 HIS A ND1   1 
ATOM   273  C CD2   . HIS A 1 41  ? -7.552  12.461 20.604  1.00 21.03 ? 341 HIS A CD2   1 
ATOM   274  C CE1   . HIS A 1 41  ? -8.532  13.121 22.455  1.00 28.04 ? 341 HIS A CE1   1 
ATOM   275  N NE2   . HIS A 1 41  ? -8.384  12.091 21.615  1.00 25.80 ? 341 HIS A NE2   1 
ATOM   276  N N     . ASP A 1 42  ? -6.071  16.829 17.344  1.00 17.17 ? 342 ASP A N     1 
ATOM   277  C CA    . ASP A 1 42  ? -5.301  17.866 16.674  1.00 17.85 ? 342 ASP A CA    1 
ATOM   278  C C     . ASP A 1 42  ? -5.704  17.932 15.206  1.00 16.76 ? 342 ASP A C     1 
ATOM   279  O O     . ASP A 1 42  ? -5.201  17.183 14.380  1.00 16.86 ? 342 ASP A O     1 
ATOM   280  C CB    . ASP A 1 42  ? -3.820  17.566 16.767  1.00 19.53 ? 342 ASP A CB    1 
ATOM   281  C CG    . ASP A 1 42  ? -2.928  18.678 16.250  1.00 21.13 ? 342 ASP A CG    1 
ATOM   282  O OD1   . ASP A 1 42  ? -3.489  19.678 15.700  1.00 19.98 ? 342 ASP A OD1   1 
ATOM   283  O OD2   . ASP A 1 42  ? -1.697  18.578 16.469  1.00 25.17 ? 342 ASP A OD2   1 
ATOM   284  N N     . ILE A 1 43  ? -6.651  18.825 14.890  1.00 15.59 ? 343 ILE A N     1 
ATOM   285  C CA    . ILE A 1 43  ? -7.196  18.936 13.550  1.00 15.40 ? 343 ILE A CA    1 
ATOM   286  C C     . ILE A 1 43  ? -6.282  19.724 12.606  1.00 15.65 ? 343 ILE A C     1 
ATOM   287  O O     . ILE A 1 43  ? -6.683  19.986 11.489  1.00 16.53 ? 343 ILE A O     1 
ATOM   288  C CB    . ILE A 1 43  ? -8.592  19.604 13.566  1.00 16.91 ? 343 ILE A CB    1 
ATOM   289  C CG1   . ILE A 1 43  ? -8.625  21.079 13.918  1.00 18.13 ? 343 ILE A CG1   1 
ATOM   290  C CG2   . ILE A 1 43  ? -9.518  18.778 14.455  1.00 17.89 ? 343 ILE A CG2   1 
ATOM   291  C CD1   . ILE A 1 43  ? -9.915  21.738 13.469  1.00 19.11 ? 343 ILE A CD1   1 
ATOM   292  N N     . THR A 1 44  ? -5.028  20.014 13.030  1.00 15.87 ? 344 THR A N     1 
ATOM   293  C CA    . THR A 1 44  ? -4.076  20.710 12.179  1.00 18.02 ? 344 THR A CA    1 
ATOM   294  C C     . THR A 1 44  ? -3.102  19.777 11.469  1.00 18.42 ? 344 THR A C     1 
ATOM   295  O O     . THR A 1 44  ? -2.297  20.238 10.687  1.00 19.87 ? 344 THR A O     1 
ATOM   296  C CB    . THR A 1 44  ? -3.281  21.731 13.010  1.00 17.91 ? 344 THR A CB    1 
ATOM   297  O OG1   . THR A 1 44  ? -2.283  21.078 13.808  1.00 19.10 ? 344 THR A OG1   1 
ATOM   298  C CG2   . THR A 1 44  ? -4.190  22.647 13.826  1.00 17.68 ? 344 THR A CG2   1 
ATOM   299  N N     . VAL A 1 45  ? -3.169  18.472 11.731  1.00 17.14 ? 345 VAL A N     1 
ATOM   300  C CA    . VAL A 1 45  ? -2.286  17.452 11.186  1.00 18.27 ? 345 VAL A CA    1 
ATOM   301  C C     . VAL A 1 45  ? -2.960  16.746 10.012  1.00 17.28 ? 345 VAL A C     1 
ATOM   302  O O     . VAL A 1 45  ? -4.098  16.319 10.119  1.00 17.88 ? 345 VAL A O     1 
ATOM   303  C CB    . VAL A 1 45  ? -1.956  16.407 12.276  1.00 22.72 ? 345 VAL A CB    1 
ATOM   304  C CG1   . VAL A 1 45  ? -1.117  15.264 11.721  1.00 23.34 ? 345 VAL A CG1   1 
ATOM   305  C CG2   . VAL A 1 45  ? -1.292  17.082 13.475  1.00 23.52 ? 345 VAL A CG2   1 
ATOM   306  N N     . GLY A 1 46  ? -2.245  16.613 8.901   1.00 16.81 ? 346 GLY A N     1 
ATOM   307  C CA    . GLY A 1 46  ? -2.701  15.906 7.720   1.00 16.57 ? 346 GLY A CA    1 
ATOM   308  C C     . GLY A 1 46  ? -3.026  16.860 6.584   1.00 16.14 ? 346 GLY A C     1 
ATOM   309  O O     . GLY A 1 46  ? -3.462  17.985 6.855   1.00 17.28 ? 346 GLY A O     1 
ATOM   310  N N     . PRO A 1 47  ? -2.865  16.462 5.311   1.00 15.78 ? 347 PRO A N     1 
ATOM   311  C CA    . PRO A 1 47  ? -3.064  17.409 4.207   1.00 17.23 ? 347 PRO A CA    1 
ATOM   312  C C     . PRO A 1 47  ? -4.527  17.771 3.992   1.00 15.57 ? 347 PRO A C     1 
ATOM   313  O O     . PRO A 1 47  ? -4.832  18.939 3.727   1.00 17.61 ? 347 PRO A O     1 
ATOM   314  C CB    . PRO A 1 47  ? -2.411  16.754 3.002   1.00 18.64 ? 347 PRO A CB    1 
ATOM   315  C CG    . PRO A 1 47  ? -2.487  15.271 3.352   1.00 17.83 ? 347 PRO A CG    1 
ATOM   316  C CD    . PRO A 1 47  ? -2.264  15.185 4.868   1.00 17.98 ? 347 PRO A CD    1 
ATOM   317  N N     . VAL A 1 48  ? -5.478  16.817 4.118   1.00 15.59 ? 348 VAL A N     1 
ATOM   318  C CA    . VAL A 1 48  ? -6.900  17.186 3.984   1.00 14.90 ? 348 VAL A CA    1 
ATOM   319  C C     . VAL A 1 48  ? -7.236  18.150 5.121   1.00 14.61 ? 348 VAL A C     1 
ATOM   320  O O     . VAL A 1 48  ? -7.843  19.216 4.914   1.00 15.65 ? 348 VAL A O     1 
ATOM   321  C CB    . VAL A 1 48  ? -7.841  15.963 3.985   1.00 15.35 ? 348 VAL A CB    1 
ATOM   322  C CG1   . VAL A 1 48  ? -9.285  16.355 4.193   1.00 14.77 ? 348 VAL A CG1   1 
ATOM   323  C CG2   . VAL A 1 48  ? -7.670  15.139 2.709   1.00 16.04 ? 348 VAL A CG2   1 
ATOM   324  N N     . ALA A 1 49  ? -6.836  17.811 6.349   1.00 15.07 ? 349 ALA A N     1 
ATOM   325  C CA    . ALA A 1 49  ? -7.124  18.625 7.518   1.00 15.63 ? 349 ALA A CA    1 
ATOM   326  C C     . ALA A 1 49  ? -6.576  20.039 7.360   1.00 14.58 ? 349 ALA A C     1 
ATOM   327  O O     . ALA A 1 49  ? -7.271  21.017 7.627   1.00 15.47 ? 349 ALA A O     1 
ATOM   328  C CB    . ALA A 1 49  ? -6.595  17.972 8.762   1.00 15.40 ? 349 ALA A CB    1 
ATOM   329  N N     . LYS A 1 50  ? -5.286  20.164 6.982   1.00 14.70 ? 350 LYS A N     1 
ATOM   330  C CA    . LYS A 1 50  ? -4.727  21.493 6.812   1.00 16.37 ? 350 LYS A CA    1 
ATOM   331  C C     . LYS A 1 50  ? -5.417  22.248 5.682   1.00 16.91 ? 350 LYS A C     1 
ATOM   332  O O     . LYS A 1 50  ? -5.621  23.447 5.784   1.00 19.31 ? 350 LYS A O     1 
ATOM   333  C CB    . LYS A 1 50  ? -3.244  21.430 6.504   1.00 17.45 ? 350 LYS A CB    1 
ATOM   334  C CG    . LYS A 1 50  ? -2.291  21.170 7.660   1.00 18.56 ? 350 LYS A CG    1 
ATOM   335  C CD    . LYS A 1 50  ? -0.833  21.273 7.208   1.00 18.89 ? 350 LYS A CD    1 
ATOM   336  C CE    . LYS A 1 50  ? 0.121   21.247 8.357   1.00 20.07 ? 350 LYS A CE    1 
ATOM   337  N NZ    . LYS A 1 50  ? 0.011   20.034 9.170   1.00 23.06 ? 350 LYS A NZ    1 
ATOM   338  N N     . SER A 1 51  ? -5.775  21.559 4.596   1.00 17.37 ? 351 SER A N     1 
ATOM   339  C CA    . SER A 1 51  ? -6.428  22.196 3.461   1.00 18.46 ? 351 SER A CA    1 
ATOM   340  C C     . SER A 1 51  ? -7.762  22.808 3.888   1.00 17.03 ? 351 SER A C     1 
ATOM   341  O O     . SER A 1 51  ? -8.076  23.972 3.596   1.00 16.18 ? 351 SER A O     1 
ATOM   342  C CB    . SER A 1 51  ? -6.591  21.211 2.329   1.00 18.64 ? 351 SER A CB    1 
ATOM   343  O OG    . SER A 1 51  ? -5.346  20.768 1.800   1.00 20.26 ? 351 SER A OG    1 
ATOM   344  N N     . ILE A 1 52  ? -8.582  21.997 4.555   1.00 16.00 ? 352 ILE A N     1 
ATOM   345  C CA    . ILE A 1 52  ? -9.912  22.434 4.962   1.00 15.32 ? 352 ILE A CA    1 
ATOM   346  C C     . ILE A 1 52  ? -9.807  23.546 6.017   1.00 15.37 ? 352 ILE A C     1 
ATOM   347  O O     . ILE A 1 52  ? -10.519 24.546 5.932   1.00 16.18 ? 352 ILE A O     1 
ATOM   348  C CB    . ILE A 1 52  ? -10.741 21.219 5.446   1.00 16.37 ? 352 ILE A CB    1 
ATOM   349  C CG1   . ILE A 1 52  ? -11.219 20.437 4.203   1.00 18.40 ? 352 ILE A CG1   1 
ATOM   350  C CG2   . ILE A 1 52  ? -11.895 21.663 6.330   1.00 16.21 ? 352 ILE A CG2   1 
ATOM   351  C CD1   . ILE A 1 52  ? -11.897 19.118 4.445   1.00 20.57 ? 352 ILE A CD1   1 
ATOM   352  N N     . LEU A 1 53  ? -8.900  23.412 6.986   1.00 15.88 ? 353 LEU A N     1 
ATOM   353  C CA    . LEU A 1 53  ? -8.784  24.401 8.050   1.00 15.14 ? 353 LEU A CA    1 
ATOM   354  C C     . LEU A 1 53  ? -8.364  25.762 7.495   1.00 16.13 ? 353 LEU A C     1 
ATOM   355  O O     . LEU A 1 53  ? -8.988  26.787 7.796   1.00 16.51 ? 353 LEU A O     1 
ATOM   356  C CB    . LEU A 1 53  ? -7.805  23.909 9.108   1.00 17.26 ? 353 LEU A CB    1 
ATOM   357  C CG    . LEU A 1 53  ? -7.431  24.909 10.196  1.00 18.39 ? 353 LEU A CG    1 
ATOM   358  C CD1   . LEU A 1 53  ? -8.675  25.505 10.859  1.00 19.65 ? 353 LEU A CD1   1 
ATOM   359  C CD2   . LEU A 1 53  ? -6.508  24.252 11.179  1.00 19.54 ? 353 LEU A CD2   1 
ATOM   360  N N     . GLN A 1 54  ? -7.327  25.797 6.643   1.00 15.78 ? 354 GLN A N     1 
ATOM   361  C CA    . GLN A 1 54  ? -6.878  27.056 6.099   1.00 17.07 ? 354 GLN A CA    1 
ATOM   362  C C     . GLN A 1 54  ? -7.960  27.745 5.280   1.00 19.17 ? 354 GLN A C     1 
ATOM   363  O O     . GLN A 1 54  ? -8.067  28.958 5.336   1.00 22.42 ? 354 GLN A O     1 
ATOM   364  C CB    . GLN A 1 54  ? -5.591  26.849 5.318   1.00 18.35 ? 354 GLN A CB    1 
ATOM   365  C CG    . GLN A 1 54  ? -4.434  26.396 6.196   1.00 22.04 ? 354 GLN A CG    1 
ATOM   366  C CD    . GLN A 1 54  ? -3.173  26.189 5.388   1.00 24.78 ? 354 GLN A CD    1 
ATOM   367  O OE1   . GLN A 1 54  ? -2.386  27.120 5.125   1.00 28.89 ? 354 GLN A OE1   1 
ATOM   368  N NE2   . GLN A 1 54  ? -3.006  24.976 4.902   1.00 24.23 ? 354 GLN A NE2   1 
ATOM   369  N N     . GLN A 1 55  ? -8.735  27.002 4.494   1.00 18.01 ? 355 GLN A N     1 
ATOM   370  C CA    . GLN A 1 55  ? -9.775  27.602 3.681   1.00 18.29 ? 355 GLN A CA    1 
ATOM   371  C C     . GLN A 1 55  ? -10.985 28.014 4.520   1.00 18.55 ? 355 GLN A C     1 
ATOM   372  O O     . GLN A 1 55  ? -11.585 29.045 4.219   1.00 20.37 ? 355 GLN A O     1 
ATOM   373  C CB    . GLN A 1 55  ? -10.132 26.646 2.547   1.00 18.97 ? 355 GLN A CB    1 
ATOM   374  C CG    . GLN A 1 55  ? -10.974 27.256 1.450   1.00 23.67 ? 355 GLN A CG    1 
ATOM   375  C CD    . GLN A 1 55  ? -10.173 28.231 0.616   1.00 28.66 ? 355 GLN A CD    1 
ATOM   376  O OE1   . GLN A 1 55  ? -8.952  28.096 0.406   1.00 33.38 ? 355 GLN A OE1   1 
ATOM   377  N NE2   . GLN A 1 55  ? -10.844 29.273 0.201   1.00 35.69 ? 355 GLN A NE2   1 
ATOM   378  N N     . ALA A 1 56  ? -11.368 27.214 5.541   1.00 16.08 ? 356 ALA A N     1 
ATOM   379  C CA    . ALA A 1 56  ? -12.546 27.518 6.350   1.00 16.41 ? 356 ALA A CA    1 
ATOM   380  C C     . ALA A 1 56  ? -12.233 28.708 7.244   1.00 16.22 ? 356 ALA A C     1 
ATOM   381  O O     . ALA A 1 56  ? -13.122 29.509 7.504   1.00 18.71 ? 356 ALA A O     1 
ATOM   382  C CB    . ALA A 1 56  ? -12.952 26.316 7.176   1.00 17.38 ? 356 ALA A CB    1 
ATOM   383  N N     . GLY A 1 57  ? -10.982 28.771 7.732   1.00 17.49 ? 357 GLY A N     1 
ATOM   384  C CA    . GLY A 1 57  ? -10.589 29.807 8.642   1.00 18.85 ? 357 GLY A CA    1 
ATOM   385  C C     . GLY A 1 57  ? -10.528 29.360 10.100  1.00 18.27 ? 357 GLY A C     1 
ATOM   386  O O     . GLY A 1 57  ? -11.123 28.361 10.517  1.00 19.46 ? 357 GLY A O     1 
ATOM   387  N N     . VAL A 1 58  ? -9.827  30.177 10.897  1.00 18.81 ? 358 VAL A N     1 
ATOM   388  C CA    . VAL A 1 58  ? -9.527  29.798 12.262  1.00 19.04 ? 358 VAL A CA    1 
ATOM   389  C C     . VAL A 1 58  ? -10.805 29.681 13.105  1.00 18.17 ? 358 VAL A C     1 
ATOM   390  O O     . VAL A 1 58  ? -10.836 28.953 14.103  1.00 20.78 ? 358 VAL A O     1 
ATOM   391  C CB    . VAL A 1 58  ? -8.531  30.781 12.883  1.00 20.09 ? 358 VAL A CB    1 
ATOM   392  C CG1   . VAL A 1 58  ? -9.114  32.195 13.060  1.00 20.15 ? 358 VAL A CG1   1 
ATOM   393  C CG2   . VAL A 1 58  ? -8.001  30.241 14.196  1.00 21.44 ? 358 VAL A CG2   1 
ATOM   394  N N     . GLU A 1 59  ? -11.869 30.386 12.710  1.00 18.23 ? 359 GLU A N     1 
ATOM   395  C CA    . GLU A 1 59  ? -13.130 30.306 13.452  1.00 18.16 ? 359 GLU A CA    1 
ATOM   396  C C     . GLU A 1 59  ? -13.727 28.892 13.443  1.00 18.42 ? 359 GLU A C     1 
ATOM   397  O O     . GLU A 1 59  ? -14.423 28.473 14.383  1.00 18.61 ? 359 GLU A O     1 
ATOM   398  C CB    . GLU A 1 59  ? -14.159 31.303 12.936  1.00 19.93 ? 359 GLU A CB    1 
ATOM   399  C CG    . GLU A 1 59  ? -13.743 32.759 13.167  1.00 23.81 ? 359 GLU A CG    1 
ATOM   400  C CD    . GLU A 1 59  ? -12.774 33.393 12.161  1.00 31.02 ? 359 GLU A CD    1 
ATOM   401  O OE1   . GLU A 1 59  ? -12.382 32.724 11.163  1.00 31.51 ? 359 GLU A OE1   1 
ATOM   402  O OE2   . GLU A 1 59  ? -12.401 34.593 12.373  1.00 38.27 ? 359 GLU A OE2   1 
ATOM   403  N N     . MET A 1 60  ? -13.481 28.150 12.359  1.00 17.20 ? 360 MET A N     1 
ATOM   404  C CA    . MET A 1 60  ? -13.917 26.776 12.285  1.00 17.50 ? 360 MET A CA    1 
ATOM   405  C C     . MET A 1 60  ? -13.198 25.954 13.347  1.00 17.01 ? 360 MET A C     1 
ATOM   406  O O     . MET A 1 60  ? -13.803 25.137 14.009  1.00 18.54 ? 360 MET A O     1 
ATOM   407  C CB    . MET A 1 60  ? -13.653 26.250 10.886  1.00 18.47 ? 360 MET A CB    1 
ATOM   408  C CG    . MET A 1 60  ? -14.201 24.866 10.694  1.00 17.56 ? 360 MET A CG    1 
ATOM   409  S SD    . MET A 1 60  ? -13.143 23.584 11.357  1.00 20.39 ? 360 MET A SD    1 
ATOM   410  C CE    . MET A 1 60  ? -12.168 23.504 9.850   1.00 19.47 ? 360 MET A CE    1 
ATOM   411  N N     . LYS A 1 61  ? -11.886 26.156 13.524  1.00 16.51 ? 361 LYS A N     1 
ATOM   412  C CA    . LYS A 1 61  ? -11.191 25.418 14.580  1.00 16.89 ? 361 LYS A CA    1 
ATOM   413  C C     . LYS A 1 61  ? -11.768 25.686 15.963  1.00 15.74 ? 361 LYS A C     1 
ATOM   414  O O     . LYS A 1 61  ? -11.878 24.778 16.778  1.00 15.51 ? 361 LYS A O     1 
ATOM   415  C CB    . LYS A 1 61  ? -9.723  25.817 14.527  1.00 18.94 ? 361 LYS A CB    1 
ATOM   416  C CG    . LYS A 1 61  ? -8.791  25.114 15.477  1.00 19.55 ? 361 LYS A CG    1 
ATOM   417  C CD    . LYS A 1 61  ? -7.399  25.717 15.316  1.00 22.71 ? 361 LYS A CD    1 
ATOM   418  C CE    . LYS A 1 61  ? -6.401  25.035 16.174  1.00 21.86 ? 361 LYS A CE    1 
ATOM   419  N NZ    . LYS A 1 61  ? -5.162  25.795 16.211  1.00 21.33 ? 361 LYS A NZ    1 
ATOM   420  N N     . SER A 1 62  ? -12.110 26.952 16.256  1.00 16.87 ? 362 SER A N     1 
ATOM   421  C CA    . SER A 1 62  ? -12.709 27.290 17.535  1.00 18.23 ? 362 SER A CA    1 
ATOM   422  C C     . SER A 1 62  ? -13.988 26.467 17.748  1.00 17.28 ? 362 SER A C     1 
ATOM   423  O O     . SER A 1 62  ? -14.253 25.978 18.838  1.00 16.84 ? 362 SER A O     1 
ATOM   424  C CB    . SER A 1 62  ? -12.967 28.814 17.659  1.00 20.78 ? 362 SER A CB    1 
ATOM   425  O OG    . SER A 1 62  ? -11.716 29.502 17.692  1.00 26.26 ? 362 SER A OG    1 
ATOM   426  N N     . GLU A 1 63  ? -14.826 26.442 16.717  1.00 15.37 ? 363 GLU A N     1 
ATOM   427  C CA    . GLU A 1 63  ? -16.087 25.733 16.803  1.00 15.72 ? 363 GLU A CA    1 
ATOM   428  C C     . GLU A 1 63  ? -15.872 24.226 16.941  1.00 16.00 ? 363 GLU A C     1 
ATOM   429  O O     . GLU A 1 63  ? -16.508 23.593 17.759  1.00 17.04 ? 363 GLU A O     1 
ATOM   430  C CB    . GLU A 1 63  ? -17.002 26.032 15.624  1.00 18.87 ? 363 GLU A CB    1 
ATOM   431  C CG    . GLU A 1 63  ? -18.333 25.292 15.736  1.00 21.57 ? 363 GLU A CG    1 
ATOM   432  C CD    . GLU A 1 63  ? -19.460 25.736 14.813  1.00 27.47 ? 363 GLU A CD    1 
ATOM   433  O OE1   . GLU A 1 63  ? -19.886 26.913 14.959  1.00 34.76 ? 363 GLU A OE1   1 
ATOM   434  O OE2   . GLU A 1 63  ? -19.938 24.956 14.009  1.00 30.29 ? 363 GLU A OE2   1 
ATOM   435  N N     . PHE A 1 64  ? -14.895 23.677 16.214  1.00 14.67 ? 364 PHE A N     1 
ATOM   436  C CA    . PHE A 1 64  ? -14.541 22.281 16.354  1.00 14.80 ? 364 PHE A CA    1 
ATOM   437  C C     . PHE A 1 64  ? -14.241 21.964 17.817  1.00 15.53 ? 364 PHE A C     1 
ATOM   438  O O     . PHE A 1 64  ? -14.715 20.976 18.385  1.00 16.19 ? 364 PHE A O     1 
ATOM   439  C CB    . PHE A 1 64  ? -13.360 21.902 15.450  1.00 14.87 ? 364 PHE A CB    1 
ATOM   440  C CG    . PHE A 1 64  ? -13.101 20.405 15.529  1.00 14.13 ? 364 PHE A CG    1 
ATOM   441  C CD1   . PHE A 1 64  ? -12.322 19.896 16.549  1.00 15.40 ? 364 PHE A CD1   1 
ATOM   442  C CD2   . PHE A 1 64  ? -13.596 19.511 14.599  1.00 14.81 ? 364 PHE A CD2   1 
ATOM   443  C CE1   . PHE A 1 64  ? -12.082 18.535 16.663  1.00 14.54 ? 364 PHE A CE1   1 
ATOM   444  C CE2   . PHE A 1 64  ? -13.327 18.153 14.705  1.00 14.84 ? 364 PHE A CE2   1 
ATOM   445  C CZ    . PHE A 1 64  ? -12.599 17.646 15.745  1.00 15.50 ? 364 PHE A CZ    1 
ATOM   446  N N     . LEU A 1 65  ? -13.306 22.716 18.374  1.00 14.77 ? 365 LEU A N     1 
ATOM   447  C CA    . LEU A 1 65  ? -12.876 22.478 19.740  1.00 16.28 ? 365 LEU A CA    1 
ATOM   448  C C     . LEU A 1 65  ? -14.017 22.555 20.747  1.00 18.18 ? 365 LEU A C     1 
ATOM   449  O O     . LEU A 1 65  ? -14.075 21.736 21.674  1.00 18.46 ? 365 LEU A O     1 
ATOM   450  C CB    . LEU A 1 65  ? -11.748 23.426 20.106  1.00 18.40 ? 365 LEU A CB    1 
ATOM   451  C CG    . LEU A 1 65  ? -10.419 23.149 19.385  1.00 20.40 ? 365 LEU A CG    1 
ATOM   452  C CD1   . LEU A 1 65  ? -9.454  24.310 19.598  1.00 22.58 ? 365 LEU A CD1   1 
ATOM   453  C CD2   . LEU A 1 65  ? -9.786  21.877 19.823  1.00 22.81 ? 365 LEU A CD2   1 
ATOM   454  N N     . ALA A 1 66  ? -14.858 23.589 20.606  1.00 17.49 ? 366 ALA A N     1 
ATOM   455  C CA    . ALA A 1 66  ? -15.980 23.743 21.516  1.00 19.11 ? 366 ALA A CA    1 
ATOM   456  C C     . ALA A 1 66  ? -17.011 22.615 21.365  1.00 17.51 ? 366 ALA A C     1 
ATOM   457  O O     . ALA A 1 66  ? -17.516 22.116 22.361  1.00 20.91 ? 366 ALA A O     1 
ATOM   458  C CB    . ALA A 1 66  ? -16.567 25.082 21.308  1.00 20.26 ? 366 ALA A CB    1 
ATOM   459  N N     . THR A 1 67  ? -17.253 22.185 20.135  1.00 16.24 ? 367 THR A N     1 
ATOM   460  C CA    . THR A 1 67  ? -18.200 21.101 19.910  1.00 18.41 ? 367 THR A CA    1 
ATOM   461  C C     . THR A 1 67  ? -17.596 19.796 20.429  1.00 17.77 ? 367 THR A C     1 
ATOM   462  O O     . THR A 1 67  ? -18.310 18.992 21.009  1.00 19.26 ? 367 THR A O     1 
ATOM   463  C CB    . THR A 1 67  ? -18.578 21.023 18.427  1.00 18.41 ? 367 THR A CB    1 
ATOM   464  O OG1   . THR A 1 67  ? -19.156 22.277 18.063  1.00 21.37 ? 367 THR A OG1   1 
ATOM   465  C CG2   . THR A 1 67  ? -19.441 19.807 18.097  1.00 18.75 ? 367 THR A CG2   1 
ATOM   466  N N     . LYS A 1 68  ? -16.272 19.622 20.257  1.00 15.52 ? 368 LYS A N     1 
ATOM   467  C CA    . LYS A 1 68  ? -15.614 18.418 20.749  1.00 16.64 ? 368 LYS A CA    1 
ATOM   468  C C     . LYS A 1 68  ? -15.774 18.354 22.270  1.00 18.85 ? 368 LYS A C     1 
ATOM   469  O O     . LYS A 1 68  ? -16.071 17.320 22.835  1.00 19.45 ? 368 LYS A O     1 
ATOM   470  C CB    . LYS A 1 68  ? -14.136 18.429 20.360  1.00 18.03 ? 368 LYS A CB    1 
ATOM   471  C CG    . LYS A 1 68  ? -13.304 17.266 20.935  1.00 20.14 ? 368 LYS A CG    1 
ATOM   472  C CD    . LYS A 1 68  ? -11.825 17.398 20.712  1.00 22.44 ? 368 LYS A CD    1 
ATOM   473  C CE    . LYS A 1 68  ? -10.997 16.321 21.315  1.00 24.21 ? 368 LYS A CE    1 
ATOM   474  N NZ    . LYS A 1 68  ? -10.851 16.518 22.743  1.00 29.88 ? 368 LYS A NZ    1 
ATOM   475  N N     . ALA A 1 69  ? -15.549 19.481 22.947  1.00 19.78 ? 369 ALA A N     1 
ATOM   476  C CA    . ALA A 1 69  ? -15.679 19.472 24.399  1.00 22.54 ? 369 ALA A CA    1 
ATOM   477  C C     . ALA A 1 69  ? -17.088 19.033 24.825  1.00 23.88 ? 369 ALA A C     1 
ATOM   478  O O     . ALA A 1 69  ? -17.243 18.351 25.835  1.00 28.92 ? 369 ALA A O     1 
ATOM   479  C CB    . ALA A 1 69  ? -15.327 20.831 24.951  1.00 24.07 ? 369 ALA A CB    1 
ATOM   480  N N     . LYS A 1 70  ? -18.123 19.384 24.058  1.00 22.84 ? 370 LYS A N     1 
ATOM   481  C CA    . LYS A 1 70  ? -19.490 19.011 24.423  1.00 24.74 ? 370 LYS A CA    1 
ATOM   482  C C     . LYS A 1 70  ? -19.835 17.560 24.073  1.00 23.24 ? 370 LYS A C     1 
ATOM   483  O O     . LYS A 1 70  ? -20.558 16.891 24.823  1.00 26.60 ? 370 LYS A O     1 
ATOM   484  C CB    . LYS A 1 70  ? -20.510 19.972 23.790  1.00 26.54 ? 370 LYS A CB    1 
ATOM   485  C CG    . LYS A 1 70  ? -20.494 21.372 24.303  1.00 33.07 ? 370 LYS A CG    1 
ATOM   486  C CD    . LYS A 1 70  ? -21.621 22.271 23.819  1.00 39.26 ? 370 LYS A CD    1 
ATOM   487  C CE    . LYS A 1 70  ? -22.538 22.686 24.931  1.00 44.62 ? 370 LYS A CE    1 
ATOM   488  N NZ    . LYS A 1 70  ? -21.901 23.530 25.951  1.00 45.51 ? 370 LYS A NZ    1 
ATOM   489  N N     . GLN A 1 71  ? -19.361 17.086 22.910  1.00 20.42 ? 371 GLN A N     1 
ATOM   490  C CA    . GLN A 1 71  ? -19.884 15.877 22.281  1.00 19.55 ? 371 GLN A CA    1 
ATOM   491  C C     . GLN A 1 71  ? -18.927 14.690 22.330  1.00 18.60 ? 371 GLN A C     1 
ATOM   492  O O     . GLN A 1 71  ? -19.370 13.548 22.233  1.00 20.24 ? 371 GLN A O     1 
ATOM   493  C CB    . GLN A 1 71  ? -20.164 16.090 20.790  1.00 20.48 ? 371 GLN A CB    1 
ATOM   494  C CG    . GLN A 1 71  ? -21.297 17.075 20.525  1.00 21.38 ? 371 GLN A CG    1 
ATOM   495  C CD    . GLN A 1 71  ? -21.502 17.303 19.051  1.00 22.65 ? 371 GLN A CD    1 
ATOM   496  O OE1   . GLN A 1 71  ? -20.792 16.735 18.202  1.00 19.23 ? 371 GLN A OE1   1 
ATOM   497  N NE2   . GLN A 1 71  ? -22.506 18.105 18.739  1.00 25.93 ? 371 GLN A NE2   1 
ATOM   498  N N     . PHE A 1 72  ? -17.618 14.942 22.360  1.00 17.04 ? 372 PHE A N     1 
ATOM   499  C CA    . PHE A 1 72  ? -16.642 13.919 22.003  1.00 16.95 ? 372 PHE A CA    1 
ATOM   500  C C     . PHE A 1 72  ? -16.598 12.790 23.023  1.00 16.21 ? 372 PHE A C     1 
ATOM   501  O O     . PHE A 1 72  ? -16.601 12.992 24.222  1.00 19.27 ? 372 PHE A O     1 
ATOM   502  C CB    . PHE A 1 72  ? -15.263 14.536 21.832  1.00 18.47 ? 372 PHE A CB    1 
ATOM   503  C CG    . PHE A 1 72  ? -14.199 13.557 21.398  1.00 18.60 ? 372 PHE A CG    1 
ATOM   504  C CD1   . PHE A 1 72  ? -14.251 13.011 20.123  1.00 19.78 ? 372 PHE A CD1   1 
ATOM   505  C CD2   . PHE A 1 72  ? -13.236 13.117 22.277  1.00 21.39 ? 372 PHE A CD2   1 
ATOM   506  C CE1   . PHE A 1 72  ? -13.245 12.180 19.694  1.00 21.27 ? 372 PHE A CE1   1 
ATOM   507  C CE2   . PHE A 1 72  ? -12.238 12.270 21.853  1.00 21.64 ? 372 PHE A CE2   1 
ATOM   508  C CZ    . PHE A 1 72  ? -12.251 11.783 20.568  1.00 22.04 ? 372 PHE A CZ    1 
ATOM   509  N N     . GLN A 1 73  ? -16.534 11.568 22.512  1.00 16.29 ? 373 GLN A N     1 
ATOM   510  C CA    . GLN A 1 73  ? -16.448 10.333 23.282  1.00 15.37 ? 373 GLN A CA    1 
ATOM   511  C C     . GLN A 1 73  ? -15.882 9.290  22.322  1.00 14.79 ? 373 GLN A C     1 
ATOM   512  O O     . GLN A 1 73  ? -15.863 9.502  21.127  1.00 15.38 ? 373 GLN A O     1 
ATOM   513  C CB    . GLN A 1 73  ? -17.766 9.929  23.949  1.00 17.51 ? 373 GLN A CB    1 
ATOM   514  C CG    . GLN A 1 73  ? -18.978 9.880  23.016  1.00 18.46 ? 373 GLN A CG    1 
ATOM   515  C CD    . GLN A 1 73  ? -20.289 9.606  23.745  1.00 20.90 ? 373 GLN A CD    1 
ATOM   516  O OE1   . GLN A 1 73  ? -20.363 9.501  24.964  1.00 21.45 ? 373 GLN A OE1   1 
ATOM   517  N NE2   . GLN A 1 73  ? -21.361 9.454  22.999  1.00 25.50 ? 373 GLN A NE2   1 
ATOM   518  N N     . ARG A 1 74  ? -15.515 8.115  22.857  1.00 14.82 ? 374 ARG A N     1 
ATOM   519  C CA    . ARG A 1 74  ? -14.911 7.096  22.012  1.00 16.19 ? 374 ARG A CA    1 
ATOM   520  C C     . ARG A 1 74  ? -15.767 6.689  20.823  1.00 15.56 ? 374 ARG A C     1 
ATOM   521  O O     . ARG A 1 74  ? -15.262 6.407  19.742  1.00 16.98 ? 374 ARG A O     1 
ATOM   522  C CB    . ARG A 1 74  ? -14.596 5.829  22.805  1.00 17.79 ? 374 ARG A CB    1 
ATOM   523  C CG    . ARG A 1 74  ? -13.486 5.975  23.806  1.00 19.55 ? 374 ARG A CG    1 
ATOM   524  C CD    . ARG A 1 74  ? -13.079 4.595  24.267  1.00 19.36 ? 374 ARG A CD    1 
ATOM   525  N NE    . ARG A 1 74  ? -11.880 4.698  25.105  1.00 22.01 ? 374 ARG A NE    1 
ATOM   526  C CZ    . ARG A 1 74  ? -11.247 3.663  25.634  1.00 21.81 ? 374 ARG A CZ    1 
ATOM   527  N NH1   . ARG A 1 74  ? -11.734 2.436  25.493  1.00 23.21 ? 374 ARG A NH1   1 
ATOM   528  N NH2   . ARG A 1 74  ? -10.149 3.860  26.330  1.00 22.88 ? 374 ARG A NH2   1 
ATOM   529  N N     . SER A 1 75  ? -17.090 6.666  21.025  1.00 15.25 ? 375 SER A N     1 
ATOM   530  C CA    . SER A 1 75  ? -17.984 6.212  19.963  1.00 16.60 ? 375 SER A CA    1 
ATOM   531  C C     . SER A 1 75  ? -18.156 7.220  18.823  1.00 15.40 ? 375 SER A C     1 
ATOM   532  O O     . SER A 1 75  ? -18.743 6.882  17.777  1.00 17.46 ? 375 SER A O     1 
ATOM   533  C CB    . SER A 1 75  ? -19.342 5.903  20.537  1.00 16.28 ? 375 SER A CB    1 
ATOM   534  O OG    . SER A 1 75  ? -19.940 7.058  21.066  1.00 16.61 ? 375 SER A OG    1 
ATOM   535  N N     . GLN A 1 76  ? -17.738 8.480  19.015  1.00 15.20 ? 376 GLN A N     1 
ATOM   536  C CA    . GLN A 1 76  ? -17.985 9.490  18.004  1.00 15.12 ? 376 GLN A CA    1 
ATOM   537  C C     . GLN A 1 76  ? -17.057 9.328  16.800  1.00 14.16 ? 376 GLN A C     1 
ATOM   538  O O     . GLN A 1 76  ? -15.827 9.423  16.934  1.00 16.43 ? 376 GLN A O     1 
ATOM   539  C CB    . GLN A 1 76  ? -17.884 10.902 18.591  1.00 14.83 ? 376 GLN A CB    1 
ATOM   540  C CG    . GLN A 1 76  ? -18.293 11.936 17.553  1.00 16.31 ? 376 GLN A CG    1 
ATOM   541  C CD    . GLN A 1 76  ? -18.373 13.352 18.104  1.00 17.10 ? 376 GLN A CD    1 
ATOM   542  O OE1   . GLN A 1 76  ? -17.719 13.717 19.074  1.00 20.83 ? 376 GLN A OE1   1 
ATOM   543  N NE2   . GLN A 1 76  ? -19.212 14.164 17.503  1.00 17.20 ? 376 GLN A NE2   1 
ATOM   544  N N     . LEU A 1 77  ? -17.621 9.143  15.615  1.00 14.12 ? 377 LEU A N     1 
ATOM   545  C CA    . LEU A 1 77  ? -16.852 9.018  14.383  1.00 13.82 ? 377 LEU A CA    1 
ATOM   546  C C     . LEU A 1 77  ? -16.987 10.235 13.481  1.00 13.80 ? 377 LEU A C     1 
ATOM   547  O O     . LEU A 1 77  ? -16.206 10.400 12.563  1.00 13.68 ? 377 LEU A O     1 
ATOM   548  C CB    . LEU A 1 77  ? -17.181 7.765  13.583  1.00 14.30 ? 377 LEU A CB    1 
ATOM   549  C CG    . LEU A 1 77  ? -16.958 6.429  14.285  1.00 16.06 ? 377 LEU A CG    1 
ATOM   550  C CD1   . LEU A 1 77  ? -17.337 5.315  13.340  1.00 16.95 ? 377 LEU A CD1   1 
ATOM   551  C CD2   . LEU A 1 77  ? -15.530 6.399  14.750  1.00 18.90 ? 377 LEU A CD2   1 
ATOM   552  N N     . VAL A 1 78  ? -18.075 11.001 13.642  1.00 13.90 ? 378 VAL A N     1 
ATOM   553  C CA    . VAL A 1 78  ? -18.291 12.177 12.818  1.00 13.94 ? 378 VAL A CA    1 
ATOM   554  C C     . VAL A 1 78  ? -18.716 13.312 13.750  1.00 14.32 ? 378 VAL A C     1 
ATOM   555  O O     . VAL A 1 78  ? -19.673 13.180 14.524  1.00 15.94 ? 378 VAL A O     1 
ATOM   556  C CB    . VAL A 1 78  ? -19.352 11.928 11.732  1.00 14.58 ? 378 VAL A CB    1 
ATOM   557  C CG1   . VAL A 1 78  ? -19.536 13.178 10.872  1.00 16.09 ? 378 VAL A CG1   1 
ATOM   558  C CG2   . VAL A 1 78  ? -19.074 10.730 10.851  1.00 15.61 ? 378 VAL A CG2   1 
ATOM   559  N N     . LEU A 1 79  ? -18.058 14.464 13.608  1.00 14.01 ? 379 LEU A N     1 
ATOM   560  C CA    . LEU A 1 79  ? -18.377 15.696 14.320  1.00 13.65 ? 379 LEU A CA    1 
ATOM   561  C C     . LEU A 1 79  ? -18.720 16.771 13.279  1.00 13.37 ? 379 LEU A C     1 
ATOM   562  O O     . LEU A 1 79  ? -18.013 16.920 12.296  1.00 14.27 ? 379 LEU A O     1 
ATOM   563  C CB    . LEU A 1 79  ? -17.196 16.066 15.219  1.00 14.25 ? 379 LEU A CB    1 
ATOM   564  C CG    . LEU A 1 79  ? -17.401 17.288 16.127  1.00 14.76 ? 379 LEU A CG    1 
ATOM   565  C CD1   . LEU A 1 79  ? -16.485 17.228 17.363  1.00 16.93 ? 379 LEU A CD1   1 
ATOM   566  C CD2   . LEU A 1 79  ? -17.204 18.616 15.416  1.00 14.25 ? 379 LEU A CD2   1 
ATOM   567  N N     . VAL A 1 80  ? -19.856 17.443 13.478  1.00 14.35 ? 380 VAL A N     1 
ATOM   568  C CA    . VAL A 1 80  ? -20.366 18.427 12.533  1.00 13.39 ? 380 VAL A CA    1 
ATOM   569  C C     . VAL A 1 80  ? -20.082 19.844 13.023  1.00 13.62 ? 380 VAL A C     1 
ATOM   570  O O     . VAL A 1 80  ? -20.379 20.178 14.171  1.00 15.22 ? 380 VAL A O     1 
ATOM   571  C CB    . VAL A 1 80  ? -21.883 18.222 12.309  1.00 14.75 ? 380 VAL A CB    1 
ATOM   572  C CG1   . VAL A 1 80  ? -22.444 19.215 11.298  1.00 16.31 ? 380 VAL A CG1   1 
ATOM   573  C CG2   . VAL A 1 80  ? -22.158 16.781 11.862  1.00 15.64 ? 380 VAL A CG2   1 
ATOM   574  N N     . THR A 1 81  ? -19.527 20.659 12.126  1.00 15.41 ? 381 THR A N     1 
ATOM   575  C CA    . THR A 1 81  ? -19.455 22.093 12.334  1.00 15.07 ? 381 THR A CA    1 
ATOM   576  C C     . THR A 1 81  ? -20.056 22.794 11.131  1.00 15.42 ? 381 THR A C     1 
ATOM   577  O O     . THR A 1 81  ? -20.328 22.191 10.100  1.00 14.62 ? 381 THR A O     1 
ATOM   578  C CB    . THR A 1 81  ? -18.009 22.555 12.518  1.00 15.29 ? 381 THR A CB    1 
ATOM   579  O OG1   . THR A 1 81  ? -17.268 22.482 11.301  1.00 15.49 ? 381 THR A OG1   1 
ATOM   580  C CG2   . THR A 1 81  ? -17.251 21.883 13.643  1.00 16.19 ? 381 THR A CG2   1 
ATOM   581  N N     . LYS A 1 82  ? -20.237 24.116 11.289  1.00 15.56 ? 382 LYS A N     1 
ATOM   582  C CA    . LYS A 1 82  ? -20.564 24.943 10.141  1.00 16.96 ? 382 LYS A CA    1 
ATOM   583  C C     . LYS A 1 82  ? -19.365 24.991 9.186   1.00 15.72 ? 382 LYS A C     1 
ATOM   584  O O     . LYS A 1 82  ? -18.267 24.577 9.554   1.00 17.08 ? 382 LYS A O     1 
ATOM   585  C CB    . LYS A 1 82  ? -20.916 26.347 10.617  1.00 19.85 ? 382 LYS A CB    1 
ATOM   586  C CG    . LYS A 1 82  ? -22.180 26.429 11.429  1.00 22.48 ? 382 LYS A CG    1 
ATOM   587  C CD    . LYS A 1 82  ? -22.599 27.868 11.623  1.00 26.99 ? 382 LYS A CD    1 
ATOM   588  C CE    . LYS A 1 82  ? -21.600 28.738 12.328  1.00 34.65 ? 382 LYS A CE    1 
ATOM   589  N NZ    . LYS A 1 82  ? -21.318 28.228 13.677  1.00 38.52 ? 382 LYS A NZ    1 
ATOM   590  N N     . GLY A 1 83  ? -19.570 25.496 7.982   1.00 16.69 ? 383 GLY A N     1 
ATOM   591  C CA    . GLY A 1 83  ? -18.581 25.578 6.936   1.00 16.83 ? 383 GLY A CA    1 
ATOM   592  C C     . GLY A 1 83  ? -17.690 26.820 6.979   1.00 17.31 ? 383 GLY A C     1 
ATOM   593  O O     . GLY A 1 83  ? -16.615 26.823 6.367   1.00 17.39 ? 383 GLY A O     1 
ATOM   594  N N     . PHE A 1 84  ? -18.121 27.881 7.662   1.00 17.00 ? 384 PHE A N     1 
ATOM   595  C CA    . PHE A 1 84  ? -17.375 29.127 7.706   1.00 17.81 ? 384 PHE A CA    1 
ATOM   596  C C     . PHE A 1 84  ? -17.025 29.588 6.297   1.00 17.47 ? 384 PHE A C     1 
ATOM   597  O O     . PHE A 1 84  ? -17.929 29.762 5.491   1.00 18.17 ? 384 PHE A O     1 
ATOM   598  C CB    . PHE A 1 84  ? -16.216 28.986 8.685   1.00 17.90 ? 384 PHE A CB    1 
ATOM   599  C CG    . PHE A 1 84  ? -16.702 28.761 10.094  1.00 18.59 ? 384 PHE A CG    1 
ATOM   600  C CD1   . PHE A 1 84  ? -17.046 29.821 10.919  1.00 19.78 ? 384 PHE A CD1   1 
ATOM   601  C CD2   . PHE A 1 84  ? -16.960 27.484 10.554  1.00 19.03 ? 384 PHE A CD2   1 
ATOM   602  C CE1   . PHE A 1 84  ? -17.513 29.587 12.196  1.00 22.48 ? 384 PHE A CE1   1 
ATOM   603  C CE2   . PHE A 1 84  ? -17.451 27.268 11.829  1.00 20.31 ? 384 PHE A CE2   1 
ATOM   604  C CZ    . PHE A 1 84  ? -17.724 28.323 12.640  1.00 20.59 ? 384 PHE A CZ    1 
ATOM   605  N N     . ASN A 1 85  ? -15.742 29.814 5.974   1.00 17.72 ? 385 ASN A N     1 
ATOM   606  C CA    . ASN A 1 85  ? -15.392 30.410 4.693   1.00 18.92 ? 385 ASN A CA    1 
ATOM   607  C C     . ASN A 1 85  ? -15.376 29.398 3.541   1.00 17.68 ? 385 ASN A C     1 
ATOM   608  O O     . ASN A 1 85  ? -15.213 29.739 2.382   1.00 21.62 ? 385 ASN A O     1 
ATOM   609  C CB    . ASN A 1 85  ? -14.026 31.091 4.735   1.00 20.25 ? 385 ASN A CB    1 
ATOM   610  C CG    . ASN A 1 85  ? -14.022 32.331 5.582   1.00 25.01 ? 385 ASN A CG    1 
ATOM   611  O OD1   . ASN A 1 85  ? -15.062 32.956 5.791   1.00 30.07 ? 385 ASN A OD1   1 
ATOM   612  N ND2   . ASN A 1 85  ? -12.840 32.694 6.040   1.00 29.30 ? 385 ASN A ND2   1 
ATOM   613  N N     . LEU A 1 86  ? -15.615 28.127 3.839   1.00 17.57 ? 386 LEU A N     1 
ATOM   614  C CA    . LEU A 1 86  ? -15.863 27.153 2.770   1.00 17.91 ? 386 LEU A CA    1 
ATOM   615  C C     . LEU A 1 86  ? -17.190 27.451 2.076   1.00 17.23 ? 386 LEU A C     1 
ATOM   616  O O     . LEU A 1 86  ? -18.118 27.996 2.690   1.00 19.49 ? 386 LEU A O     1 
ATOM   617  C CB    . LEU A 1 86  ? -15.941 25.711 3.265   1.00 18.55 ? 386 LEU A CB    1 
ATOM   618  C CG    . LEU A 1 86  ? -14.683 25.181 3.939   1.00 19.21 ? 386 LEU A CG    1 
ATOM   619  C CD1   . LEU A 1 86  ? -14.881 23.691 4.174   1.00 20.57 ? 386 LEU A CD1   1 
ATOM   620  C CD2   . LEU A 1 86  ? -13.437 25.403 3.102   1.00 21.16 ? 386 LEU A CD2   1 
ATOM   621  N N     . PHE A 1 87  ? -17.324 26.981 0.833   1.00 17.59 ? 387 PHE A N     1 
ATOM   622  C CA    . PHE A 1 87  ? -18.577 27.108 0.094   1.00 17.74 ? 387 PHE A CA    1 
ATOM   623  C C     . PHE A 1 87  ? -19.492 25.917 0.408   1.00 18.03 ? 387 PHE A C     1 
ATOM   624  O O     . PHE A 1 87  ? -19.938 25.235 -0.509  1.00 18.34 ? 387 PHE A O     1 
ATOM   625  C CB    . PHE A 1 87  ? -18.338 27.244 -1.411  1.00 19.23 ? 387 PHE A CB    1 
ATOM   626  C CG    . PHE A 1 87  ? -17.511 28.420 -1.885  1.00 26.33 ? 387 PHE A CG    1 
ATOM   627  C CD1   . PHE A 1 87  ? -17.669 29.670 -1.326  1.00 32.02 ? 387 PHE A CD1   1 
ATOM   628  C CD2   . PHE A 1 87  ? -16.569 28.228 -2.874  1.00 33.44 ? 387 PHE A CD2   1 
ATOM   629  C CE1   . PHE A 1 87  ? -16.908 30.738 -1.771  1.00 37.12 ? 387 PHE A CE1   1 
ATOM   630  C CE2   . PHE A 1 87  ? -15.814 29.293 -3.321  1.00 37.56 ? 387 PHE A CE2   1 
ATOM   631  C CZ    . PHE A 1 87  ? -15.974 30.542 -2.759  1.00 38.67 ? 387 PHE A CZ    1 
ATOM   632  N N     . CYS A 1 88  ? -19.797 25.760 1.699   1.00 17.39 ? 388 CYS A N     1 
ATOM   633  C CA    . CYS A 1 88  ? -20.685 24.713 2.170   1.00 17.49 ? 388 CYS A CA    1 
ATOM   634  C C     . CYS A 1 88  ? -21.413 25.182 3.425   1.00 17.31 ? 388 CYS A C     1 
ATOM   635  O O     . CYS A 1 88  ? -21.023 26.160 4.044   1.00 19.59 ? 388 CYS A O     1 
ATOM   636  C CB    . CYS A 1 88  ? -19.939 23.405 2.411   1.00 15.97 ? 388 CYS A CB    1 
ATOM   637  S SG    . CYS A 1 88  ? -18.747 23.492 3.775   1.00 17.12 ? 388 CYS A SG    1 
ATOM   638  N N     . LYS A 1 89  ? -22.470 24.450 3.783   1.00 17.19 ? 389 LYS A N     1 
ATOM   639  C CA    . LYS A 1 89  ? -23.236 24.682 4.997   1.00 17.39 ? 389 LYS A CA    1 
ATOM   640  C C     . LYS A 1 89  ? -22.530 24.083 6.208   1.00 16.54 ? 389 LYS A C     1 
ATOM   641  O O     . LYS A 1 89  ? -22.438 24.700 7.258   1.00 17.57 ? 389 LYS A O     1 
ATOM   642  C CB    . LYS A 1 89  ? -24.669 24.168 4.890   1.00 18.86 ? 389 LYS A CB    1 
ATOM   643  C CG    . LYS A 1 89  ? -25.512 24.730 3.759   1.00 21.39 ? 389 LYS A CG    1 
ATOM   644  C CD    . LYS A 1 89  ? -26.906 24.108 3.643   1.00 24.56 ? 389 LYS A CD    1 
ATOM   645  C CE    . LYS A 1 89  ? -27.597 24.643 2.419   1.00 29.23 ? 389 LYS A CE    1 
ATOM   646  N NZ    . LYS A 1 89  ? -28.969 24.169 2.276   1.00 29.67 ? 389 LYS A NZ    1 
ATOM   647  N N     . TYR A 1 90  ? -22.160 22.804 6.091   1.00 15.64 ? 390 TYR A N     1 
ATOM   648  C CA    . TYR A 1 90  ? -21.572 22.059 7.195   1.00 14.59 ? 390 TYR A CA    1 
ATOM   649  C C     . TYR A 1 90  ? -20.299 21.342 6.728   1.00 13.93 ? 390 TYR A C     1 
ATOM   650  O O     . TYR A 1 90  ? -20.177 21.023 5.562   1.00 15.03 ? 390 TYR A O     1 
ATOM   651  C CB    . TYR A 1 90  ? -22.538 20.993 7.728   1.00 15.03 ? 390 TYR A CB    1 
ATOM   652  C CG    . TYR A 1 90  ? -23.874 21.570 8.116   1.00 17.07 ? 390 TYR A CG    1 
ATOM   653  C CD1   . TYR A 1 90  ? -24.036 22.276 9.301   1.00 19.56 ? 390 TYR A CD1   1 
ATOM   654  C CD2   . TYR A 1 90  ? -24.970 21.371 7.310   1.00 19.17 ? 390 TYR A CD2   1 
ATOM   655  C CE1   . TYR A 1 90  ? -25.275 22.808 9.662   1.00 22.91 ? 390 TYR A CE1   1 
ATOM   656  C CE2   . TYR A 1 90  ? -26.197 21.861 7.668   1.00 23.06 ? 390 TYR A CE2   1 
ATOM   657  C CZ    . TYR A 1 90  ? -26.346 22.601 8.825   1.00 23.55 ? 390 TYR A CZ    1 
ATOM   658  O OH    . TYR A 1 90  ? -27.625 23.033 9.098   1.00 34.95 ? 390 TYR A OH    1 
ATOM   659  N N     . ILE A 1 91  ? -19.412 21.094 7.687   1.00 13.28 ? 391 ILE A N     1 
ATOM   660  C CA    . ILE A 1 91  ? -18.290 20.197 7.529   1.00 12.91 ? 391 ILE A CA    1 
ATOM   661  C C     . ILE A 1 91  ? -18.569 18.989 8.418   1.00 12.98 ? 391 ILE A C     1 
ATOM   662  O O     . ILE A 1 91  ? -18.878 19.123 9.591   1.00 13.69 ? 391 ILE A O     1 
ATOM   663  C CB    . ILE A 1 91  ? -16.939 20.810 7.924   1.00 13.34 ? 391 ILE A CB    1 
ATOM   664  C CG1   . ILE A 1 91  ? -16.650 22.083 7.112   1.00 15.25 ? 391 ILE A CG1   1 
ATOM   665  C CG2   . ILE A 1 91  ? -15.797 19.813 7.782   1.00 14.35 ? 391 ILE A CG2   1 
ATOM   666  C CD1   . ILE A 1 91  ? -15.547 22.954 7.681   1.00 16.93 ? 391 ILE A CD1   1 
ATOM   667  N N     . TYR A 1 92  ? -18.480 17.800 7.820   1.00 12.73 ? 392 TYR A N     1 
ATOM   668  C CA    . TYR A 1 92  ? -18.497 16.558 8.577   1.00 13.93 ? 392 TYR A CA    1 
ATOM   669  C C     . TYR A 1 92  ? -17.054 16.104 8.761   1.00 12.99 ? 392 TYR A C     1 
ATOM   670  O O     . TYR A 1 92  ? -16.406 15.745 7.787   1.00 13.94 ? 392 TYR A O     1 
ATOM   671  C CB    . TYR A 1 92  ? -19.262 15.494 7.815   1.00 12.81 ? 392 TYR A CB    1 
ATOM   672  C CG    . TYR A 1 92  ? -20.767 15.713 7.751   1.00 13.01 ? 392 TYR A CG    1 
ATOM   673  C CD1   . TYR A 1 92  ? -21.410 16.850 8.259   1.00 13.54 ? 392 TYR A CD1   1 
ATOM   674  C CD2   . TYR A 1 92  ? -21.601 14.773 7.124   1.00 14.76 ? 392 TYR A CD2   1 
ATOM   675  C CE1   . TYR A 1 92  ? -22.782 17.023 8.162   1.00 12.78 ? 392 TYR A CE1   1 
ATOM   676  C CE2   . TYR A 1 92  ? -22.968 14.946 6.983   1.00 13.69 ? 392 TYR A CE2   1 
ATOM   677  C CZ    . TYR A 1 92  ? -23.556 16.083 7.491   1.00 13.73 ? 392 TYR A CZ    1 
ATOM   678  O OH    . TYR A 1 92  ? -24.929 16.186 7.386   1.00 15.44 ? 392 TYR A OH    1 
ATOM   679  N N     . HIS A 1 93  ? -16.602 16.181 10.005  1.00 12.81 ? 393 HIS A N     1 
ATOM   680  C CA    . HIS A 1 93  ? -15.234 15.826 10.334  1.00 12.63 ? 393 HIS A CA    1 
ATOM   681  C C     . HIS A 1 93  ? -15.199 14.356 10.746  1.00 12.69 ? 393 HIS A C     1 
ATOM   682  O O     . HIS A 1 93  ? -15.767 13.988 11.773  1.00 13.97 ? 393 HIS A O     1 
ATOM   683  C CB    . HIS A 1 93  ? -14.708 16.686 11.490  1.00 12.81 ? 393 HIS A CB    1 
ATOM   684  C CG    . HIS A 1 93  ? -14.758 18.156 11.273  1.00 13.89 ? 393 HIS A CG    1 
ATOM   685  N ND1   . HIS A 1 93  ? -13.704 18.846 10.741  1.00 13.85 ? 393 HIS A ND1   1 
ATOM   686  C CD2   . HIS A 1 93  ? -15.766 19.013 11.455  1.00 13.29 ? 393 HIS A CD2   1 
ATOM   687  C CE1   . HIS A 1 93  ? -14.053 20.143 10.685  1.00 14.85 ? 393 HIS A CE1   1 
ATOM   688  N NE2   . HIS A 1 93  ? -15.316 20.270 11.127  1.00 14.17 ? 393 HIS A NE2   1 
ATOM   689  N N     . VAL A 1 94  ? -14.589 13.520 9.900   1.00 13.66 ? 394 VAL A N     1 
ATOM   690  C CA    . VAL A 1 94  ? -14.445 12.112 10.219  1.00 13.67 ? 394 VAL A CA    1 
ATOM   691  C C     . VAL A 1 94  ? -13.292 11.999 11.208  1.00 13.47 ? 394 VAL A C     1 
ATOM   692  O O     . VAL A 1 94  ? -12.176 12.513 10.943  1.00 14.48 ? 394 VAL A O     1 
ATOM   693  C CB    . VAL A 1 94  ? -14.204 11.269 8.959   1.00 13.24 ? 394 VAL A CB    1 
ATOM   694  C CG1   . VAL A 1 94  ? -13.737 9.853  9.301   1.00 13.92 ? 394 VAL A CG1   1 
ATOM   695  C CG2   . VAL A 1 94  ? -15.444 11.240 8.087   1.00 14.49 ? 394 VAL A CG2   1 
ATOM   696  N N     . LEU A 1 95  ? -13.509 11.326 12.352  1.00 12.75 ? 395 LEU A N     1 
ATOM   697  C CA    . LEU A 1 95  ? -12.550 11.334 13.450  1.00 13.24 ? 395 LEU A CA    1 
ATOM   698  C C     . LEU A 1 95  ? -11.865 9.972  13.548  1.00 13.25 ? 395 LEU A C     1 
ATOM   699  O O     . LEU A 1 95  ? -12.499 8.928  13.749  1.00 14.62 ? 395 LEU A O     1 
ATOM   700  C CB    . LEU A 1 95  ? -13.293 11.595 14.754  1.00 13.80 ? 395 LEU A CB    1 
ATOM   701  C CG    . LEU A 1 95  ? -14.246 12.795 14.785  1.00 14.51 ? 395 LEU A CG    1 
ATOM   702  C CD1   . LEU A 1 95  ? -14.843 12.951 16.194  1.00 15.25 ? 395 LEU A CD1   1 
ATOM   703  C CD2   . LEU A 1 95  ? -13.584 14.101 14.375  1.00 13.84 ? 395 LEU A CD2   1 
ATOM   704  N N     . TRP A 1 96  ? -10.528 9.962  13.421  1.00 14.00 ? 396 TRP A N     1 
ATOM   705  C CA    . TRP A 1 96  ? -9.712  8.754  13.556  1.00 14.82 ? 396 TRP A CA    1 
ATOM   706  C C     . TRP A 1 96  ? -9.066  8.755  14.941  1.00 16.09 ? 396 TRP A C     1 
ATOM   707  O O     . TRP A 1 96  ? -8.146  9.539  15.216  1.00 16.72 ? 396 TRP A O     1 
ATOM   708  C CB    . TRP A 1 96  ? -8.665  8.732  12.442  1.00 15.15 ? 396 TRP A CB    1 
ATOM   709  C CG    . TRP A 1 96  ? -9.213  8.797  11.048  1.00 15.04 ? 396 TRP A CG    1 
ATOM   710  C CD1   . TRP A 1 96  ? -9.452  9.921  10.302  1.00 15.82 ? 396 TRP A CD1   1 
ATOM   711  C CD2   . TRP A 1 96  ? -9.573  7.681  10.212  1.00 14.54 ? 396 TRP A CD2   1 
ATOM   712  N NE1   . TRP A 1 96  ? -9.922  9.588  9.066   1.00 15.81 ? 396 TRP A NE1   1 
ATOM   713  C CE2   . TRP A 1 96  ? -9.998  8.206  8.980   1.00 15.29 ? 396 TRP A CE2   1 
ATOM   714  C CE3   . TRP A 1 96  ? -9.536  6.291  10.372  1.00 16.46 ? 396 TRP A CE3   1 
ATOM   715  C CZ2   . TRP A 1 96  ? -10.379 7.389  7.926   1.00 17.12 ? 396 TRP A CZ2   1 
ATOM   716  C CZ3   . TRP A 1 96  ? -9.930  5.481  9.321   1.00 16.92 ? 396 TRP A CZ3   1 
ATOM   717  C CH2   . TRP A 1 96  ? -10.353 6.024  8.120   1.00 18.32 ? 396 TRP A CH2   1 
ATOM   718  N N     . HIS A 1 97  ? -9.505  7.855  15.812  1.00 17.75 ? 397 HIS A N     1 
ATOM   719  C CA    . HIS A 1 97  ? -9.036  7.826  17.184  1.00 19.47 ? 397 HIS A CA    1 
ATOM   720  C C     . HIS A 1 97  ? -9.272  6.461  17.830  1.00 23.33 ? 397 HIS A C     1 
ATOM   721  O O     . HIS A 1 97  ? -9.853  6.354  18.914  1.00 30.17 ? 397 HIS A O     1 
ATOM   722  C CB    . HIS A 1 97  ? -9.688  8.913  18.020  1.00 18.04 ? 397 HIS A CB    1 
ATOM   723  C CG    . HIS A 1 97  ? -11.174 8.868  18.098  1.00 17.43 ? 397 HIS A CG    1 
ATOM   724  N ND1   . HIS A 1 97  ? -11.805 8.789  19.315  1.00 22.53 ? 397 HIS A ND1   1 
ATOM   725  C CD2   . HIS A 1 97  ? -12.138 8.995  17.185  1.00 16.63 ? 397 HIS A CD2   1 
ATOM   726  C CE1   . HIS A 1 97  ? -13.135 8.845  19.110  1.00 22.09 ? 397 HIS A CE1   1 
ATOM   727  N NE2   . HIS A 1 97  ? -13.364 8.911  17.801  1.00 21.07 ? 397 HIS A NE2   1 
ATOM   728  N N     . SER A 1 98  ? -8.926  5.398  17.144  1.00 20.96 ? 398 SER A N     1 
ATOM   729  C CA    . SER A 1 98  ? -8.934  4.109  17.803  1.00 25.07 ? 398 SER A CA    1 
ATOM   730  C C     . SER A 1 98  ? -7.861  3.228  17.217  1.00 24.03 ? 398 SER A C     1 
ATOM   731  O O     . SER A 1 98  ? -7.250  3.565  16.219  1.00 24.69 ? 398 SER A O     1 
ATOM   732  C CB    . SER A 1 98  ? -10.270 3.470  17.731  1.00 24.79 ? 398 SER A CB    1 
ATOM   733  O OG    . SER A 1 98  ? -10.539 2.902  16.473  1.00 27.33 ? 398 SER A OG    1 
ATOM   734  N N     . GLU A 1 99  ? -7.710  2.058  17.820  1.00 26.38 ? 399 GLU A N     1 
ATOM   735  C CA    . GLU A 1 99  ? -6.765  1.075  17.312  1.00 27.52 ? 399 GLU A CA    1 
ATOM   736  C C     . GLU A 1 99  ? -7.447  0.005  16.450  1.00 22.90 ? 399 GLU A C     1 
ATOM   737  O O     . GLU A 1 99  ? -6.827  -0.977 16.060  1.00 24.33 ? 399 GLU A O     1 
ATOM   738  C CB    . GLU A 1 99  ? -5.943  0.395  18.413  1.00 35.41 ? 399 GLU A CB    1 
ATOM   739  C CG    . GLU A 1 99  ? -5.202  1.376  19.319  1.00 42.56 ? 399 GLU A CG    1 
ATOM   740  C CD    . GLU A 1 99  ? -3.867  1.850  18.792  1.00 50.12 ? 399 GLU A CD    1 
ATOM   741  O OE1   . GLU A 1 99  ? -3.870  2.449  17.696  1.00 53.96 ? 399 GLU A OE1   1 
ATOM   742  O OE2   . GLU A 1 99  ? -2.837  1.610  19.472  1.00 55.10 ? 399 GLU A OE2   1 
ATOM   743  N N     . PHE A 1 100 ? -8.735  0.138  16.151  1.00 20.01 ? 400 PHE A N     1 
ATOM   744  C CA    . PHE A 1 100 ? -9.448  -0.839 15.351  1.00 18.30 ? 400 PHE A CA    1 
ATOM   745  C C     . PHE A 1 100 ? -9.027  -0.752 13.884  1.00 18.46 ? 400 PHE A C     1 
ATOM   746  O O     . PHE A 1 100 ? -8.476  0.266  13.428  1.00 18.02 ? 400 PHE A O     1 
ATOM   747  C CB    . PHE A 1 100 ? -10.964 -0.683 15.522  1.00 20.42 ? 400 PHE A CB    1 
ATOM   748  C CG    . PHE A 1 100 ? -11.440 -1.135 16.887  1.00 22.51 ? 400 PHE A CG    1 
ATOM   749  C CD1   . PHE A 1 100 ? -11.163 -2.414 17.323  1.00 24.36 ? 400 PHE A CD1   1 
ATOM   750  C CD2   . PHE A 1 100 ? -12.115 -0.277 17.737  1.00 25.37 ? 400 PHE A CD2   1 
ATOM   751  C CE1   . PHE A 1 100 ? -11.567 -2.844 18.577  1.00 26.88 ? 400 PHE A CE1   1 
ATOM   752  C CE2   . PHE A 1 100 ? -12.529 -0.715 18.984  1.00 25.30 ? 400 PHE A CE2   1 
ATOM   753  C CZ    . PHE A 1 100 ? -12.203 -1.982 19.418  1.00 25.36 ? 400 PHE A CZ    1 
ATOM   754  N N     . PRO A 1 101 ? -9.258  -1.822 13.095  1.00 18.31 ? 401 PRO A N     1 
ATOM   755  C CA    . PRO A 1 101 ? -8.854  -1.852 11.690  1.00 17.46 ? 401 PRO A CA    1 
ATOM   756  C C     . PRO A 1 101 ? -9.435  -0.703 10.871  1.00 16.77 ? 401 PRO A C     1 
ATOM   757  O O     . PRO A 1 101 ? -10.626 -0.364 10.927  1.00 16.57 ? 401 PRO A O     1 
ATOM   758  C CB    . PRO A 1 101 ? -9.323  -3.213 11.205  1.00 20.15 ? 401 PRO A CB    1 
ATOM   759  C CG    . PRO A 1 101 ? -9.362  -4.057 12.456  1.00 21.07 ? 401 PRO A CG    1 
ATOM   760  C CD    . PRO A 1 101 ? -9.817  -3.118 13.548  1.00 19.67 ? 401 PRO A CD    1 
ATOM   761  N N     . LYS A 1 102 ? -8.571  -0.028 10.126  1.00 16.88 ? 402 LYS A N     1 
ATOM   762  C CA    . LYS A 1 102 ? -8.959  1.231  9.522   1.00 17.13 ? 402 LYS A CA    1 
ATOM   763  C C     . LYS A 1 102 ? -10.032 1.055  8.470   1.00 14.90 ? 402 LYS A C     1 
ATOM   764  O O     . LYS A 1 102 ? -10.934 1.896  8.420   1.00 15.70 ? 402 LYS A O     1 
ATOM   765  C CB    . LYS A 1 102 ? -7.781  1.967  8.908   1.00 17.72 ? 402 LYS A CB    1 
ATOM   766  C CG    . LYS A 1 102 ? -6.668  2.256  9.926   1.00 22.43 ? 402 LYS A CG    1 
ATOM   767  C CD    . LYS A 1 102 ? -7.175  2.765  11.271  1.00 22.69 ? 402 LYS A CD    1 
ATOM   768  C CE    . LYS A 1 102 ? -6.126  2.697  12.365  1.00 29.97 ? 402 LYS A CE    1 
ATOM   769  N NZ    . LYS A 1 102 ? -6.696  2.541  13.712  1.00 28.21 ? 402 LYS A NZ    1 
ATOM   770  N N     . PRO A 1 103 ? -10.060 -0.027 7.656   1.00 16.84 ? 403 PRO A N     1 
ATOM   771  C CA    . PRO A 1 103 ? -11.188 -0.195 6.739   1.00 15.50 ? 403 PRO A CA    1 
ATOM   772  C C     . PRO A 1 103 ? -12.536 -0.334 7.457   1.00 15.01 ? 403 PRO A C     1 
ATOM   773  O O     . PRO A 1 103 ? -13.597 0.019  6.912   1.00 16.00 ? 403 PRO A O     1 
ATOM   774  C CB    . PRO A 1 103 ? -10.838 -1.479 5.978   1.00 17.62 ? 403 PRO A CB    1 
ATOM   775  C CG    . PRO A 1 103 ? -9.340  -1.531 6.063   1.00 17.96 ? 403 PRO A CG    1 
ATOM   776  C CD    . PRO A 1 103 ? -9.031  -1.073 7.465   1.00 16.89 ? 403 PRO A CD    1 
ATOM   777  N N     . GLN A 1 104 ? -12.538 -0.900 8.672   1.00 15.12 ? 404 GLN A N     1 
ATOM   778  C CA    . GLN A 1 104 ? -13.766 -1.062 9.440   1.00 14.58 ? 404 GLN A CA    1 
ATOM   779  C C     . GLN A 1 104 ? -14.265 0.302  9.901   1.00 14.58 ? 404 GLN A C     1 
ATOM   780  O O     . GLN A 1 104 ? -15.470 0.616  9.858   1.00 14.68 ? 404 GLN A O     1 
ATOM   781  C CB    . GLN A 1 104 ? -13.616 -2.094 10.568  1.00 16.05 ? 404 GLN A CB    1 
ATOM   782  C CG    . GLN A 1 104 ? -13.282 -3.493 10.037  1.00 17.31 ? 404 GLN A CG    1 
ATOM   783  C CD    . GLN A 1 104 ? -12.945 -4.504 11.104  1.00 19.58 ? 404 GLN A CD    1 
ATOM   784  O OE1   . GLN A 1 104 ? -12.212 -5.498 10.920  1.00 22.59 ? 404 GLN A OE1   1 
ATOM   785  N NE2   . GLN A 1 104 ? -13.442 -4.254 12.275  1.00 18.74 ? 404 GLN A NE2   1 
ATOM   786  N N     . ILE A 1 105 ? -13.336 1.100  10.421  1.00 14.97 ? 405 ILE A N     1 
ATOM   787  C CA    . ILE A 1 105 ? -13.684 2.470  10.833  1.00 14.83 ? 405 ILE A CA    1 
ATOM   788  C C     . ILE A 1 105 ? -14.220 3.241  9.644   1.00 14.29 ? 405 ILE A C     1 
ATOM   789  O O     . ILE A 1 105 ? -15.243 3.895  9.744   1.00 15.25 ? 405 ILE A O     1 
ATOM   790  C CB    . ILE A 1 105 ? -12.455 3.188  11.423  1.00 14.87 ? 405 ILE A CB    1 
ATOM   791  C CG1   . ILE A 1 105 ? -11.933 2.482  12.673  1.00 16.25 ? 405 ILE A CG1   1 
ATOM   792  C CG2   . ILE A 1 105 ? -12.813 4.634  11.711  1.00 15.70 ? 405 ILE A CG2   1 
ATOM   793  C CD1   . ILE A 1 105 ? -10.597 3.056  13.139  1.00 17.70 ? 405 ILE A CD1   1 
ATOM   794  N N     . LEU A 1 106 ? -13.571 3.156  8.495   1.00 14.30 ? 406 LEU A N     1 
ATOM   795  C CA    . LEU A 1 106 ? -13.981 3.839  7.288   1.00 14.76 ? 406 LEU A CA    1 
ATOM   796  C C     . LEU A 1 106 ? -15.434 3.514  6.932   1.00 14.65 ? 406 LEU A C     1 
ATOM   797  O O     . LEU A 1 106 ? -16.209 4.405  6.590   1.00 16.13 ? 406 LEU A O     1 
ATOM   798  C CB    . LEU A 1 106 ? -13.026 3.567  6.142   1.00 14.70 ? 406 LEU A CB    1 
ATOM   799  C CG    . LEU A 1 106 ? -13.395 4.191  4.809   1.00 14.69 ? 406 LEU A CG    1 
ATOM   800  C CD1   . LEU A 1 106 ? -13.393 5.713  4.921   1.00 16.03 ? 406 LEU A CD1   1 
ATOM   801  C CD2   . LEU A 1 106 ? -12.484 3.727  3.690   1.00 18.24 ? 406 LEU A CD2   1 
ATOM   802  N N     . LYS A 1 107 ? -15.769 2.240  6.913   1.00 13.81 ? 407 LYS A N     1 
ATOM   803  C CA    . LYS A 1 107 ? -17.110 1.816  6.555   1.00 13.90 ? 407 LYS A CA    1 
ATOM   804  C C     . LYS A 1 107 ? -18.152 2.448  7.491   1.00 14.10 ? 407 LYS A C     1 
ATOM   805  O O     . LYS A 1 107 ? -19.165 2.977  7.035   1.00 14.55 ? 407 LYS A O     1 
ATOM   806  C CB    . LYS A 1 107 ? -17.188 0.294  6.486   1.00 15.13 ? 407 LYS A CB    1 
ATOM   807  C CG    . LYS A 1 107 ? -18.567 -0.215 6.041   1.00 16.94 ? 407 LYS A CG    1 
ATOM   808  C CD    . LYS A 1 107 ? -18.563 -1.726 5.835   1.00 21.24 ? 407 LYS A CD    1 
ATOM   809  C CE    . LYS A 1 107 ? -19.922 -2.251 5.427   1.00 24.15 ? 407 LYS A CE    1 
ATOM   810  N NZ    . LYS A 1 107 ? -20.191 -1.893 4.028   1.00 27.32 ? 407 LYS A NZ    1 
ATOM   811  N N     . HIS A 1 108 ? -17.912 2.418  8.799   1.00 13.76 ? 408 HIS A N     1 
ATOM   812  C CA    . HIS A 1 108 ? -18.822 3.010  9.754   1.00 13.62 ? 408 HIS A CA    1 
ATOM   813  C C     . HIS A 1 108 ? -18.933 4.532  9.540   1.00 13.66 ? 408 HIS A C     1 
ATOM   814  O O     . HIS A 1 108 ? -20.027 5.078  9.575   1.00 14.66 ? 408 HIS A O     1 
ATOM   815  C CB    . HIS A 1 108 ? -18.418 2.783  11.209  1.00 14.31 ? 408 HIS A CB    1 
ATOM   816  C CG    . HIS A 1 108 ? -18.485 1.339  11.648  1.00 15.86 ? 408 HIS A CG    1 
ATOM   817  N ND1   . HIS A 1 108 ? -19.585 0.537  11.430  1.00 18.16 ? 408 HIS A ND1   1 
ATOM   818  C CD2   . HIS A 1 108 ? -17.603 0.573  12.309  1.00 16.58 ? 408 HIS A CD2   1 
ATOM   819  C CE1   . HIS A 1 108 ? -19.353 -0.666 11.951  1.00 18.26 ? 408 HIS A CE1   1 
ATOM   820  N NE2   . HIS A 1 108 ? -18.150 -0.661 12.503  1.00 18.04 ? 408 HIS A NE2   1 
ATOM   821  N N     . ALA A 1 109 ? -17.803 5.192  9.330   1.00 13.21 ? 409 ALA A N     1 
ATOM   822  C CA    . ALA A 1 109 ? -17.802 6.647  9.180   1.00 13.18 ? 409 ALA A CA    1 
ATOM   823  C C     . ALA A 1 109 ? -18.520 7.059  7.904   1.00 13.89 ? 409 ALA A C     1 
ATOM   824  O O     . ALA A 1 109 ? -19.261 8.050  7.895   1.00 14.25 ? 409 ALA A O     1 
ATOM   825  C CB    . ALA A 1 109 ? -16.403 7.165  9.154   1.00 14.91 ? 409 ALA A CB    1 
ATOM   826  N N     . MET A 1 110 ? -18.336 6.289  6.822   1.00 14.84 ? 410 MET A N     1 
ATOM   827  C CA    . MET A 1 110 ? -19.027 6.602  5.572   1.00 15.35 ? 410 MET A CA    1 
ATOM   828  C C     . MET A 1 110 ? -20.534 6.498  5.741   1.00 13.97 ? 410 MET A C     1 
ATOM   829  O O     . MET A 1 110 ? -21.300 7.372  5.300   1.00 15.27 ? 410 MET A O     1 
ATOM   830  C CB    . MET A 1 110 ? -18.607 5.663  4.432   1.00 17.10 ? 410 MET A CB    1 
ATOM   831  C CG    . MET A 1 110 ? -17.366 6.065  3.735   1.00 19.11 ? 410 MET A CG    1 
ATOM   832  S SD    . MET A 1 110 ? -17.463 7.663  2.927   1.00 21.67 ? 410 MET A SD    1 
ATOM   833  C CE    . MET A 1 110 ? -18.848 7.675  1.813   1.00 20.74 ? 410 MET A CE    1 
ATOM   834  N N     . LYS A 1 111 ? -20.971 5.407  6.352   1.00 13.66 ? 411 LYS A N     1 
ATOM   835  C CA    . LYS A 1 111 ? -22.429 5.209  6.545   1.00 13.72 ? 411 LYS A CA    1 
ATOM   836  C C     . LYS A 1 111 ? -22.944 6.383  7.385   1.00 13.91 ? 411 LYS A C     1 
ATOM   837  O O     . LYS A 1 111 ? -24.036 6.884  7.091   1.00 16.00 ? 411 LYS A O     1 
ATOM   838  C CB    . LYS A 1 111 ? -22.664 3.860  7.227   1.00 15.58 ? 411 LYS A CB    1 
ATOM   839  C CG    . LYS A 1 111 ? -24.159 3.619  7.392   1.00 18.86 ? 411 LYS A CG    1 
ATOM   840  C CD    . LYS A 1 111 ? -24.567 2.301  8.031   1.00 21.79 ? 411 LYS A CD    1 
ATOM   841  C CE    . LYS A 1 111 ? -26.028 2.342  8.359   1.00 27.05 ? 411 LYS A CE    1 
ATOM   842  N NZ    . LYS A 1 111 ? -26.496 1.093  8.961   1.00 29.29 ? 411 LYS A NZ    1 
ATOM   843  N N     . GLU A 1 112 ? -22.226 6.743  8.424   1.00 13.35 ? 412 GLU A N     1 
ATOM   844  C CA    . GLU A 1 112 ? -22.719 7.799  9.336   1.00 14.55 ? 412 GLU A CA    1 
ATOM   845  C C     . GLU A 1 112 ? -22.828 9.143  8.600   1.00 13.30 ? 412 GLU A C     1 
ATOM   846  O O     . GLU A 1 112 ? -23.812 9.835  8.811   1.00 15.52 ? 412 GLU A O     1 
ATOM   847  C CB    . GLU A 1 112 ? -21.835 7.925  10.568  1.00 30.00 ? 412 GLU A CB    1 
ATOM   848  C CG    . GLU A 1 112 ? -22.374 8.967  11.538  1.00 30.00 ? 412 GLU A CG    1 
ATOM   849  C CD    . GLU A 1 112 ? -21.745 8.950  12.910  1.00 30.00 ? 412 GLU A CD    1 
ATOM   850  O OE1   . GLU A 1 112 ? -21.017 7.993  13.217  1.00 30.00 ? 412 GLU A OE1   1 
ATOM   851  O OE2   . GLU A 1 112 ? -21.997 9.910  13.660  1.00 30.00 ? 412 GLU A OE2   1 
ATOM   852  N N     . CYS A 1 113 ? -21.852 9.473  7.773   1.00 13.17 ? 413 CYS A N     1 
ATOM   853  C CA    . CYS A 1 113 ? -21.934 10.721 6.985   1.00 13.01 ? 413 CYS A CA    1 
ATOM   854  C C     . CYS A 1 113 ? -23.197 10.713 6.116   1.00 14.02 ? 413 CYS A C     1 
ATOM   855  O O     . CYS A 1 113 ? -23.839 11.751 6.035   1.00 15.57 ? 413 CYS A O     1 
ATOM   856  C CB    . CYS A 1 113 ? -20.723 10.854 6.078   1.00 12.03 ? 413 CYS A CB    1 
ATOM   857  S SG    . CYS A 1 113 ? -19.195 11.325 6.937   1.00 14.94 ? 413 CYS A SG    1 
ATOM   858  N N     . LEU A 1 114 ? -23.469 9.611  5.440   1.00 14.10 ? 414 LEU A N     1 
ATOM   859  C CA    . LEU A 1 114 ? -24.635 9.511  4.572   1.00 14.24 ? 414 LEU A CA    1 
ATOM   860  C C     . LEU A 1 114 ? -25.934 9.529  5.369   1.00 15.61 ? 414 LEU A C     1 
ATOM   861  O O     . LEU A 1 114 ? -26.846 10.243 4.976   1.00 16.13 ? 414 LEU A O     1 
ATOM   862  C CB    . LEU A 1 114 ? -24.507 8.264  3.691   1.00 14.66 ? 414 LEU A CB    1 
ATOM   863  C CG    . LEU A 1 114 ? -23.354 8.310  2.674   1.00 15.24 ? 414 LEU A CG    1 
ATOM   864  C CD1   . LEU A 1 114 ? -23.129 6.957  2.060   1.00 16.16 ? 414 LEU A CD1   1 
ATOM   865  C CD2   . LEU A 1 114 ? -23.580 9.427  1.636   1.00 17.51 ? 414 LEU A CD2   1 
ATOM   866  N N     . GLU A 1 115 ? -26.002 8.832  6.513   1.00 14.85 ? 415 GLU A N     1 
ATOM   867  C CA    . GLU A 1 115 ? -27.178 8.896  7.358   1.00 14.88 ? 415 GLU A CA    1 
ATOM   868  C C     . GLU A 1 115 ? -27.432 10.335 7.849   1.00 15.93 ? 415 GLU A C     1 
ATOM   869  O O     . GLU A 1 115 ? -28.587 10.760 7.963   1.00 16.70 ? 415 GLU A O     1 
ATOM   870  C CB    . GLU A 1 115 ? -27.080 7.922  8.527   1.00 16.93 ? 415 GLU A CB    1 
ATOM   871  C CG    . GLU A 1 115 ? -27.139 6.465  8.102   1.00 19.17 ? 415 GLU A CG    1 
ATOM   872  C CD    . GLU A 1 115 ? -28.471 5.993  7.562   1.00 21.18 ? 415 GLU A CD    1 
ATOM   873  O OE1   . GLU A 1 115 ? -29.506 6.122  8.250   1.00 28.64 ? 415 GLU A OE1   1 
ATOM   874  O OE2   . GLU A 1 115 ? -28.482 5.493  6.407   1.00 28.71 ? 415 GLU A OE2   1 
ATOM   875  N N     A LYS A 1 116 ? -26.367 11.074 8.145   0.50 14.22 ? 416 LYS A N     1 
ATOM   876  N N     B LYS A 1 116 ? -26.362 11.067 8.166   0.50 15.80 ? 416 LYS A N     1 
ATOM   877  C CA    A LYS A 1 116 ? -26.516 12.452 8.601   0.50 13.38 ? 416 LYS A CA    1 
ATOM   878  C CA    B LYS A 1 116 ? -26.490 12.458 8.589   0.50 16.80 ? 416 LYS A CA    1 
ATOM   879  C C     A LYS A 1 116 ? -27.127 13.352 7.521   0.50 13.64 ? 416 LYS A C     1 
ATOM   880  C C     B LYS A 1 116 ? -27.207 13.299 7.529   0.50 15.28 ? 416 LYS A C     1 
ATOM   881  O O     A LYS A 1 116 ? -27.678 14.412 7.834   0.50 14.27 ? 416 LYS A O     1 
ATOM   882  O O     B LYS A 1 116 ? -27.889 14.281 7.856   0.50 15.06 ? 416 LYS A O     1 
ATOM   883  C CB    A LYS A 1 116 ? -25.186 12.990 9.100   0.50 13.53 ? 416 LYS A CB    1 
ATOM   884  C CB    B LYS A 1 116 ? -25.143 13.126 8.832   0.50 20.35 ? 416 LYS A CB    1 
ATOM   885  C CG    A LYS A 1 116 ? -24.850 12.605 10.498  0.50 14.59 ? 416 LYS A CG    1 
ATOM   886  C CG    B LYS A 1 116 ? -24.231 12.480 9.835   0.50 25.34 ? 416 LYS A CG    1 
ATOM   887  C CD    A LYS A 1 116 ? -23.454 13.158 10.840  0.50 15.33 ? 416 LYS A CD    1 
ATOM   888  C CD    B LYS A 1 116 ? -24.570 12.806 11.279  0.50 29.15 ? 416 LYS A CD    1 
ATOM   889  C CE    A LYS A 1 116 ? -23.090 13.194 12.278  0.50 18.90 ? 416 LYS A CE    1 
ATOM   890  C CE    B LYS A 1 116 ? -23.337 12.628 12.066  0.50 28.84 ? 416 LYS A CE    1 
ATOM   891  N NZ    A LYS A 1 116 ? -24.236 13.486 13.137  0.50 20.50 ? 416 LYS A NZ    1 
ATOM   892  N NZ    B LYS A 1 116 ? -23.631 12.059 13.374  0.50 27.08 ? 416 LYS A NZ    1 
ATOM   893  N N     . CYS A 1 117 ? -26.999 12.934 6.254   1.00 15.20 ? 417 CYS A N     1 
ATOM   894  C CA    . CYS A 1 117 ? -27.611 13.639 5.158   1.00 15.50 ? 417 CYS A CA    1 
ATOM   895  C C     . CYS A 1 117 ? -29.127 13.624 5.262   1.00 16.86 ? 417 CYS A C     1 
ATOM   896  O O     . CYS A 1 117 ? -29.788 14.563 4.829   1.00 17.35 ? 417 CYS A O     1 
ATOM   897  C CB    . CYS A 1 117 ? -27.178 13.167 3.787   1.00 16.13 ? 417 CYS A CB    1 
ATOM   898  S SG    . CYS A 1 117 ? -25.451 13.518 3.411   1.00 16.30 ? 417 CYS A SG    1 
ATOM   899  N N     . ILE A 1 118 ? -29.697 12.554 5.837   1.00 15.44 ? 418 ILE A N     1 
ATOM   900  C CA    . ILE A 1 118 ? -31.122 12.512 6.111   1.00 15.76 ? 418 ILE A CA    1 
ATOM   901  C C     . ILE A 1 118 ? -31.455 13.466 7.267   1.00 16.95 ? 418 ILE A C     1 
ATOM   902  O O     . ILE A 1 118 ? -32.372 14.302 7.164   1.00 16.92 ? 418 ILE A O     1 
ATOM   903  C CB    . ILE A 1 118 ? -31.592 11.099 6.442   1.00 17.51 ? 418 ILE A CB    1 
ATOM   904  C CG1   . ILE A 1 118 ? -31.254 10.110 5.363   1.00 17.94 ? 418 ILE A CG1   1 
ATOM   905  C CG2   . ILE A 1 118 ? -33.084 11.089 6.728   1.00 18.36 ? 418 ILE A CG2   1 
ATOM   906  C CD1   . ILE A 1 118 ? -31.748 10.447 3.992   1.00 20.96 ? 418 ILE A CD1   1 
ATOM   907  N N     . GLU A 1 119 ? -30.734 13.328 8.387   1.00 17.47 ? 419 GLU A N     1 
ATOM   908  C CA    . GLU A 1 119 ? -31.013 14.113 9.576   1.00 17.31 ? 419 GLU A CA    1 
ATOM   909  C C     . GLU A 1 119 ? -30.981 15.617 9.267   1.00 17.15 ? 419 GLU A C     1 
ATOM   910  O O     . GLU A 1 119 ? -31.824 16.347 9.765   1.00 18.99 ? 419 GLU A O     1 
ATOM   911  C CB    . GLU A 1 119 ? -30.014 13.756 10.669  1.00 19.24 ? 419 GLU A CB    1 
ATOM   912  C CG    . GLU A 1 119 ? -30.076 14.620 11.913  1.00 20.66 ? 419 GLU A CG    1 
ATOM   913  C CD    . GLU A 1 119 ? -29.172 14.116 13.024  1.00 23.36 ? 419 GLU A CD    1 
ATOM   914  O OE1   . GLU A 1 119 ? -28.373 13.165 12.834  1.00 30.31 ? 419 GLU A OE1   1 
ATOM   915  O OE2   . GLU A 1 119 ? -29.257 14.721 14.107  1.00 28.92 ? 419 GLU A OE2   1 
ATOM   916  N N     . GLN A 1 120 ? -29.999 16.061 8.481   1.00 15.86 ? 420 GLN A N     1 
ATOM   917  C CA    . GLN A 1 120 ? -29.818 17.484 8.217   1.00 15.33 ? 420 GLN A CA    1 
ATOM   918  C C     . GLN A 1 120 ? -30.317 17.931 6.851   1.00 15.59 ? 420 GLN A C     1 
ATOM   919  O O     . GLN A 1 120 ? -30.118 19.092 6.477   1.00 16.72 ? 420 GLN A O     1 
ATOM   920  C CB    . GLN A 1 120 ? -28.341 17.845 8.305   1.00 16.08 ? 420 GLN A CB    1 
ATOM   921  C CG    . GLN A 1 120 ? -27.785 17.757 9.714   1.00 17.93 ? 420 GLN A CG    1 
ATOM   922  C CD    . GLN A 1 120 ? -26.437 18.420 9.809   1.00 19.08 ? 420 GLN A CD    1 
ATOM   923  O OE1   . GLN A 1 120 ? -25.510 18.006 9.150   1.00 23.30 ? 420 GLN A OE1   1 
ATOM   924  N NE2   . GLN A 1 120 ? -26.333 19.551 10.492  1.00 26.24 ? 420 GLN A NE2   1 
ATOM   925  N N     . ASN A 1 121 ? -31.050 17.045 6.167   1.00 15.69 ? 421 ASN A N     1 
ATOM   926  C CA    . ASN A 1 121 ? -31.701 17.350 4.911   1.00 16.26 ? 421 ASN A CA    1 
ATOM   927  C C     . ASN A 1 121 ? -30.765 17.930 3.875   1.00 15.88 ? 421 ASN A C     1 
ATOM   928  O O     . ASN A 1 121 ? -30.962 19.012 3.343   1.00 17.17 ? 421 ASN A O     1 
ATOM   929  C CB    . ASN A 1 121 ? -32.876 18.294 5.130   1.00 16.88 ? 421 ASN A CB    1 
ATOM   930  C CG    . ASN A 1 121 ? -33.758 18.329 3.911   1.00 18.04 ? 421 ASN A CG    1 
ATOM   931  O OD1   . ASN A 1 121 ? -33.912 17.306 3.235   1.00 23.44 ? 421 ASN A OD1   1 
ATOM   932  N ND2   . ASN A 1 121 ? -34.372 19.449 3.610   1.00 17.94 ? 421 ASN A ND2   1 
ATOM   933  N N     . ILE A 1 122 ? -29.714 17.178 3.612   1.00 14.76 ? 422 ILE A N     1 
ATOM   934  C CA    . ILE A 1 122 ? -28.606 17.575 2.766   1.00 14.23 ? 422 ILE A CA    1 
ATOM   935  C C     . ILE A 1 122 ? -28.855 17.126 1.325   1.00 13.64 ? 422 ILE A C     1 
ATOM   936  O O     . ILE A 1 122 ? -29.251 15.964 1.108   1.00 14.74 ? 422 ILE A O     1 
ATOM   937  C CB    . ILE A 1 122 ? -27.299 16.917 3.300   1.00 14.99 ? 422 ILE A CB    1 
ATOM   938  C CG1   . ILE A 1 122 ? -27.038 17.375 4.738   1.00 14.94 ? 422 ILE A CG1   1 
ATOM   939  C CG2   . ILE A 1 122 ? -26.116 17.152 2.369   1.00 15.05 ? 422 ILE A CG2   1 
ATOM   940  C CD1   . ILE A 1 122 ? -26.915 18.898 4.917   1.00 15.30 ? 422 ILE A CD1   1 
ATOM   941  N N     . THR A 1 123 ? -28.565 17.974 0.336   1.00 14.17 ? 423 THR A N     1 
ATOM   942  C CA    . THR A 1 123 ? -28.784 17.657 -1.060  1.00 14.19 ? 423 THR A CA    1 
ATOM   943  C C     . THR A 1 123 ? -27.486 17.337 -1.797  1.00 13.30 ? 423 THR A C     1 
ATOM   944  O O     . THR A 1 123 ? -27.538 16.722 -2.873  1.00 14.46 ? 423 THR A O     1 
ATOM   945  C CB    . THR A 1 123 ? -29.496 18.798 -1.790  1.00 15.83 ? 423 THR A CB    1 
ATOM   946  O OG1   . THR A 1 123 ? -28.638 19.908 -2.076  1.00 17.79 ? 423 THR A OG1   1 
ATOM   947  C CG2   . THR A 1 123 ? -30.704 19.295 -1.032  1.00 15.71 ? 423 THR A CG2   1 
ATOM   948  N N     . SER A 1 124 ? -26.321 17.724 -1.242  1.00 13.74 ? 424 SER A N     1 
ATOM   949  C CA    . SER A 1 124 ? -25.047 17.452 -1.883  1.00 13.65 ? 424 SER A CA    1 
ATOM   950  C C     . SER A 1 124 ? -23.967 17.295 -0.824  1.00 13.91 ? 424 SER A C     1 
ATOM   951  O O     . SER A 1 124 ? -23.927 18.038 0.161   1.00 14.88 ? 424 SER A O     1 
ATOM   952  C CB    . SER A 1 124 ? -24.664 18.490 -2.869  1.00 14.20 ? 424 SER A CB    1 
ATOM   953  O OG    . SER A 1 124 ? -24.638 19.797 -2.331  1.00 15.59 ? 424 SER A OG    1 
ATOM   954  N N     . ILE A 1 125 ? -23.055 16.340 -1.073  1.00 13.61 ? 425 ILE A N     1 
ATOM   955  C CA    . ILE A 1 125 ? -21.963 16.062 -0.146  1.00 13.71 ? 425 ILE A CA    1 
ATOM   956  C C     . ILE A 1 125 ? -20.737 15.659 -0.945  1.00 13.35 ? 425 ILE A C     1 
ATOM   957  O O     . ILE A 1 125 ? -20.864 14.890 -1.908  1.00 14.04 ? 425 ILE A O     1 
ATOM   958  C CB    . ILE A 1 125 ? -22.371 14.984 0.877   1.00 13.35 ? 425 ILE A CB    1 
ATOM   959  C CG1   . ILE A 1 125 ? -21.267 14.732 1.903   1.00 13.59 ? 425 ILE A CG1   1 
ATOM   960  C CG2   . ILE A 1 125 ? -22.818 13.674 0.218   1.00 13.80 ? 425 ILE A CG2   1 
ATOM   961  C CD1   . ILE A 1 125 ? -21.704 13.984 3.152   1.00 14.27 ? 425 ILE A CD1   1 
ATOM   962  N N     . SER A 1 126 ? -19.583 16.229 -0.547  1.00 13.43 ? 426 SER A N     1 
ATOM   963  C CA    . SER A 1 126 ? -18.333 15.967 -1.225  1.00 13.32 ? 426 SER A CA    1 
ATOM   964  C C     . SER A 1 126 ? -17.310 15.368 -0.250  1.00 13.49 ? 426 SER A C     1 
ATOM   965  O O     . SER A 1 126 ? -17.070 15.911 0.819   1.00 14.03 ? 426 SER A O     1 
ATOM   966  C CB    . SER A 1 126 ? -17.793 17.210 -1.843  1.00 15.33 ? 426 SER A CB    1 
ATOM   967  O OG    . SER A 1 126 ? -18.677 17.662 -2.868  1.00 16.54 ? 426 SER A OG    1 
ATOM   968  N N     . PHE A 1 127 ? -16.793 14.185 -0.609  1.00 13.49 ? 427 PHE A N     1 
ATOM   969  C CA    . PHE A 1 127 ? -15.811 13.450 0.179   1.00 12.55 ? 427 PHE A CA    1 
ATOM   970  C C     . PHE A 1 127 ? -14.446 13.517 -0.501  1.00 12.44 ? 427 PHE A C     1 
ATOM   971  O O     . PHE A 1 127 ? -14.387 13.347 -1.713  1.00 13.87 ? 427 PHE A O     1 
ATOM   972  C CB    . PHE A 1 127 ? -16.146 11.950 0.246   1.00 12.63 ? 427 PHE A CB    1 
ATOM   973  C CG    . PHE A 1 127 ? -17.464 11.653 0.941   1.00 12.92 ? 427 PHE A CG    1 
ATOM   974  C CD1   . PHE A 1 127 ? -18.697 11.699 0.284   1.00 13.47 ? 427 PHE A CD1   1 
ATOM   975  C CD2   . PHE A 1 127 ? -17.461 11.297 2.272   1.00 13.44 ? 427 PHE A CD2   1 
ATOM   976  C CE1   . PHE A 1 127 ? -19.849 11.334 0.952   1.00 14.13 ? 427 PHE A CE1   1 
ATOM   977  C CE2   . PHE A 1 127 ? -18.618 10.937 2.926   1.00 13.40 ? 427 PHE A CE2   1 
ATOM   978  C CZ    . PHE A 1 127 ? -19.825 11.003 2.286   1.00 13.51 ? 427 PHE A CZ    1 
ATOM   979  N N     . PRO A 1 128 ? -13.344 13.604 0.269   1.00 13.55 ? 428 PRO A N     1 
ATOM   980  C CA    . PRO A 1 128 ? -12.026 13.244 -0.226  1.00 13.94 ? 428 PRO A CA    1 
ATOM   981  C C     . PRO A 1 128 ? -11.926 11.707 -0.155  1.00 14.00 ? 428 PRO A C     1 
ATOM   982  O O     . PRO A 1 128 ? -12.836 11.062 0.337   1.00 15.16 ? 428 PRO A O     1 
ATOM   983  C CB    . PRO A 1 128 ? -11.107 13.908 0.759   1.00 15.67 ? 428 PRO A CB    1 
ATOM   984  C CG    . PRO A 1 128 ? -11.888 13.811 2.090   1.00 14.12 ? 428 PRO A CG    1 
ATOM   985  C CD    . PRO A 1 128 ? -13.329 13.856 1.733   1.00 14.08 ? 428 PRO A CD    1 
ATOM   986  N N     . ALA A 1 129 ? -10.782 11.162 -0.590  1.00 14.35 ? 429 ALA A N     1 
ATOM   987  C CA    . ALA A 1 129 ? -10.523 9.736  -0.561  1.00 14.93 ? 429 ALA A CA    1 
ATOM   988  C C     . ALA A 1 129 ? -10.093 9.371  0.848   1.00 15.17 ? 429 ALA A C     1 
ATOM   989  O O     . ALA A 1 129 ? -8.905  9.103  1.134   1.00 15.06 ? 429 ALA A O     1 
ATOM   990  C CB    . ALA A 1 129 ? -9.557  9.383  -1.620  1.00 15.66 ? 429 ALA A CB    1 
ATOM   991  N N     . LEU A 1 130 ? -11.076 9.353  1.739   1.00 15.47 ? 430 LEU A N     1 
ATOM   992  C CA    . LEU A 1 130 ? -10.846 9.144  3.159   1.00 15.36 ? 430 LEU A CA    1 
ATOM   993  C C     . LEU A 1 130 ? -10.005 7.903  3.368   1.00 15.70 ? 430 LEU A C     1 
ATOM   994  O O     . LEU A 1 130 ? -10.284 6.845  2.780   1.00 16.59 ? 430 LEU A O     1 
ATOM   995  C CB    . LEU A 1 130 ? -12.173 8.937  3.873   1.00 15.63 ? 430 LEU A CB    1 
ATOM   996  C CG    . LEU A 1 130 ? -13.131 10.115 3.969   1.00 16.59 ? 430 LEU A CG    1 
ATOM   997  C CD1   . LEU A 1 130 ? -14.494 9.632  4.419   1.00 16.89 ? 430 LEU A CD1   1 
ATOM   998  C CD2   . LEU A 1 130 ? -12.549 11.156 4.924   1.00 17.52 ? 430 LEU A CD2   1 
ATOM   999  N N     . GLY A 1 131 ? -8.970  8.021  4.227   1.00 15.50 ? 431 GLY A N     1 
ATOM   1000 C CA    . GLY A 1 131 ? -8.220  6.872  4.687   1.00 16.24 ? 431 GLY A CA    1 
ATOM   1001 C C     . GLY A 1 131 ? -7.026  6.489  3.807   1.00 16.27 ? 431 GLY A C     1 
ATOM   1002 O O     . GLY A 1 131 ? -6.258  5.589  4.198   1.00 17.91 ? 431 GLY A O     1 
ATOM   1003 N N     . THR A 1 132 ? -6.939  7.040  2.597   1.00 15.68 ? 432 THR A N     1 
ATOM   1004 C CA    . THR A 1 132 ? -5.957  6.613  1.606   1.00 15.68 ? 432 THR A CA    1 
ATOM   1005 C C     . THR A 1 132 ? -4.592  7.268  1.790   1.00 16.48 ? 432 THR A C     1 
ATOM   1006 O O     . THR A 1 132 ? -3.692  6.945  1.015   1.00 18.93 ? 432 THR A O     1 
ATOM   1007 C CB    . THR A 1 132 ? -6.479  6.808  0.178   1.00 15.95 ? 432 THR A CB    1 
ATOM   1008 O OG1   . THR A 1 132 ? -6.702  8.201  -0.086  1.00 16.00 ? 432 THR A OG1   1 
ATOM   1009 C CG2   . THR A 1 132 ? -7.726  5.989  -0.068  1.00 17.93 ? 432 THR A CG2   1 
ATOM   1010 N N     . GLY A 1 133 ? -4.481  8.279  2.671   1.00 15.98 ? 433 GLY A N     1 
ATOM   1011 C CA    . GLY A 1 133 ? -3.224  8.972  2.902   1.00 17.09 ? 433 GLY A CA    1 
ATOM   1012 C C     . GLY A 1 133 ? -2.536  8.416  4.139   1.00 18.05 ? 433 GLY A C     1 
ATOM   1013 O O     . GLY A 1 133 ? -2.053  7.280  4.149   1.00 18.39 ? 433 GLY A O     1 
ATOM   1014 N N     . ASN A 1 134 ? -2.558  9.193  5.214   1.00 17.48 ? 434 ASN A N     1 
ATOM   1015 C CA    . ASN A 1 134 ? -1.967  8.791  6.467   1.00 18.10 ? 434 ASN A CA    1 
ATOM   1016 C C     . ASN A 1 134 ? -2.500  7.472  7.029   1.00 17.08 ? 434 ASN A C     1 
ATOM   1017 O O     . ASN A 1 134 ? -1.752  6.796  7.718   1.00 20.64 ? 434 ASN A O     1 
ATOM   1018 C CB    . ASN A 1 134 ? -2.140  9.873  7.514   1.00 19.51 ? 434 ASN A CB    1 
ATOM   1019 C CG    . ASN A 1 134 ? -1.171  11.011 7.287   1.00 20.08 ? 434 ASN A CG    1 
ATOM   1020 O OD1   . ASN A 1 134 ? 0.021   10.844 7.035   1.00 26.09 ? 434 ASN A OD1   1 
ATOM   1021 N ND2   . ASN A 1 134 ? -1.608  12.240 7.370   1.00 23.06 ? 434 ASN A ND2   1 
ATOM   1022 N N     A MET A 1 135 ? -3.771  7.118  6.756   0.50 17.42 ? 435 MET A N     1 
ATOM   1023 N N     B MET A 1 135 ? -3.776  7.120  6.770   0.50 17.42 ? 435 MET A N     1 
ATOM   1024 C CA    A MET A 1 135 ? -4.321  5.885  7.316   0.50 18.54 ? 435 MET A CA    1 
ATOM   1025 C CA    B MET A 1 135 ? -4.322  5.883  7.330   0.50 18.27 ? 435 MET A CA    1 
ATOM   1026 C C     A MET A 1 135 ? -3.917  4.658  6.494   0.50 19.05 ? 435 MET A C     1 
ATOM   1027 C C     B MET A 1 135 ? -3.936  4.660  6.487   0.50 19.01 ? 435 MET A C     1 
ATOM   1028 O O     A MET A 1 135 ? -4.127  3.535  6.936   0.50 20.00 ? 435 MET A O     1 
ATOM   1029 O O     B MET A 1 135 ? -4.175  3.535  6.911   0.50 20.05 ? 435 MET A O     1 
ATOM   1030 C CB    A MET A 1 135 ? -5.847  5.970  7.474   0.50 19.21 ? 435 MET A CB    1 
ATOM   1031 C CB    B MET A 1 135 ? -5.846  5.970  7.534   0.50 18.96 ? 435 MET A CB    1 
ATOM   1032 C CG    A MET A 1 135 ? -6.316  7.151  8.292   0.50 20.22 ? 435 MET A CG    1 
ATOM   1033 C CG    B MET A 1 135 ? -6.291  6.836  8.708   0.50 19.83 ? 435 MET A CG    1 
ATOM   1034 S SD    A MET A 1 135 ? -5.533  7.293  9.913   0.50 27.32 ? 435 MET A SD    1 
ATOM   1035 S SD    B MET A 1 135 ? -5.882  6.200  10.350  0.50 21.94 ? 435 MET A SD    1 
ATOM   1036 C CE    A MET A 1 135 ? -5.340  5.558  10.321  0.50 27.20 ? 435 MET A CE    1 
ATOM   1037 C CE    B MET A 1 135 ? -4.303  7.026  10.549  0.50 22.31 ? 435 MET A CE    1 
ATOM   1038 N N     . GLU A 1 136 ? -3.334  4.874  5.312   1.00 20.13 ? 436 GLU A N     1 
ATOM   1039 C CA    . GLU A 1 136 ? -2.740  3.803  4.500   1.00 20.67 ? 436 GLU A CA    1 
ATOM   1040 C C     . GLU A 1 136 ? -3.721  2.715  4.059   1.00 19.38 ? 436 GLU A C     1 
ATOM   1041 O O     . GLU A 1 136 ? -3.303  1.582  3.804   1.00 21.86 ? 436 GLU A O     1 
ATOM   1042 C CB    . GLU A 1 136 ? -1.533  3.196  5.212   1.00 24.20 ? 436 GLU A CB    1 
ATOM   1043 C CG    . GLU A 1 136 ? -0.497  4.239  5.604   1.00 28.63 ? 436 GLU A CG    1 
ATOM   1044 C CD    . GLU A 1 136 ? 0.775   3.608  6.109   1.00 32.56 ? 436 GLU A CD    1 
ATOM   1045 O OE1   . GLU A 1 136 ? 0.859   2.404  6.377   1.00 40.14 ? 436 GLU A OE1   1 
ATOM   1046 O OE2   . GLU A 1 136 ? 1.718   4.378  6.171   1.00 42.27 ? 436 GLU A OE2   1 
ATOM   1047 N N     . ILE A 1 137 ? -5.026  3.053  3.891   1.00 17.22 ? 437 ILE A N     1 
ATOM   1048 C CA    . ILE A 1 137 ? -5.976  2.092  3.347   1.00 17.47 ? 437 ILE A CA    1 
ATOM   1049 C C     . ILE A 1 137 ? -5.693  1.929  1.851   1.00 18.09 ? 437 ILE A C     1 
ATOM   1050 O O     . ILE A 1 137 ? -5.589  2.918  1.114   1.00 18.90 ? 437 ILE A O     1 
ATOM   1051 C CB    . ILE A 1 137 ? -7.440  2.525  3.622   1.00 17.51 ? 437 ILE A CB    1 
ATOM   1052 C CG1   . ILE A 1 137 ? -7.703  2.606  5.108   1.00 18.03 ? 437 ILE A CG1   1 
ATOM   1053 C CG2   . ILE A 1 137 ? -8.399  1.568  2.910   1.00 20.06 ? 437 ILE A CG2   1 
ATOM   1054 C CD1   . ILE A 1 137 ? -9.093  3.063  5.530   1.00 17.46 ? 437 ILE A CD1   1 
ATOM   1055 N N     . LYS A 1 138 ? -5.595  0.678  1.383   1.00 18.68 ? 438 LYS A N     1 
ATOM   1056 C CA    . LYS A 1 138 ? -5.372  0.374  -0.009  1.00 20.44 ? 438 LYS A CA    1 
ATOM   1057 C C     . LYS A 1 138 ? -6.434  1.066  -0.863  1.00 19.01 ? 438 LYS A C     1 
ATOM   1058 O O     . LYS A 1 138 ? -7.604  1.040  -0.522  1.00 18.51 ? 438 LYS A O     1 
ATOM   1059 C CB    . LYS A 1 138 ? -5.423  -1.156 -0.147  1.00 23.62 ? 438 LYS A CB    1 
ATOM   1060 C CG    . LYS A 1 138 ? -5.255  -1.734 -1.553  1.00 29.71 ? 438 LYS A CG    1 
ATOM   1061 C CD    . LYS A 1 138 ? -4.903  -3.216 -1.685  1.00 35.26 ? 438 LYS A CD    1 
ATOM   1062 C CE    . LYS A 1 138 ? -6.054  -4.075 -1.270  1.00 39.43 ? 438 LYS A CE    1 
ATOM   1063 N NZ    . LYS A 1 138 ? -5.894  -5.482 -1.656  1.00 39.70 ? 438 LYS A NZ    1 
ATOM   1064 N N     . LYS A 1 139 ? -6.036  1.601  -2.008  1.00 18.53 ? 439 LYS A N     1 
ATOM   1065 C CA    . LYS A 1 139 ? -6.940  2.378  -2.859  1.00 18.07 ? 439 LYS A CA    1 
ATOM   1066 C C     . LYS A 1 139 ? -8.178  1.599  -3.299  1.00 17.78 ? 439 LYS A C     1 
ATOM   1067 O O     . LYS A 1 139 ? -9.310  2.111  -3.280  1.00 17.79 ? 439 LYS A O     1 
ATOM   1068 C CB    . LYS A 1 139 ? -6.129  3.008  -4.009  1.00 19.92 ? 439 LYS A CB    1 
ATOM   1069 C CG    . LYS A 1 139 ? -5.455  1.993  -4.917  1.00 21.95 ? 439 LYS A CG    1 
ATOM   1070 C CD    . LYS A 1 139 ? -4.397  2.606  -5.828  1.00 26.57 ? 439 LYS A CD    1 
ATOM   1071 C CE    . LYS A 1 139 ? -3.474  1.604  -6.460  1.00 29.91 ? 439 LYS A CE    1 
ATOM   1072 N NZ    . LYS A 1 139 ? -4.057  0.784  -7.521  1.00 32.55 ? 439 LYS A NZ    1 
ATOM   1073 N N     . GLU A 1 140 ? -7.989  0.318  -3.626  1.00 17.94 ? 440 GLU A N     1 
ATOM   1074 C CA    . GLU A 1 140 ? -9.110  -0.500 -4.057  1.00 19.52 ? 440 GLU A CA    1 
ATOM   1075 C C     . GLU A 1 140 ? -10.066 -0.803 -2.921  1.00 17.38 ? 440 GLU A C     1 
ATOM   1076 O O     . GLU A 1 140 ? -11.257 -0.853 -3.161  1.00 19.46 ? 440 GLU A O     1 
ATOM   1077 C CB    . GLU A 1 140 ? -8.689  -1.822 -4.667  1.00 21.71 ? 440 GLU A CB    1 
ATOM   1078 C CG    . GLU A 1 140 ? -7.940  -1.668 -5.983  1.00 26.82 ? 440 GLU A CG    1 
ATOM   1079 C CD    . GLU A 1 140 ? -6.474  -1.264 -5.830  1.00 28.35 ? 440 GLU A CD    1 
ATOM   1080 O OE1   . GLU A 1 140 ? -5.877  -1.348 -4.704  1.00 30.95 ? 440 GLU A OE1   1 
ATOM   1081 O OE2   . GLU A 1 140 ? -5.930  -0.810 -6.866  1.00 35.70 ? 440 GLU A OE2   1 
ATOM   1082 N N     . THR A 1 141 ? -9.554  -1.006 -1.713  1.00 16.83 ? 441 THR A N     1 
ATOM   1083 C CA    . THR A 1 141 ? -10.390 -1.211 -0.535  1.00 17.34 ? 441 THR A CA    1 
ATOM   1084 C C     . THR A 1 141 ? -11.204 0.049  -0.258  1.00 16.08 ? 441 THR A C     1 
ATOM   1085 O O     . THR A 1 141 ? -12.394 -0.028 0.010   1.00 16.59 ? 441 THR A O     1 
ATOM   1086 C CB    . THR A 1 141 ? -9.496  -1.582 0.649   1.00 18.42 ? 441 THR A CB    1 
ATOM   1087 O OG1   . THR A 1 141 ? -8.821  -2.781 0.257   1.00 21.77 ? 441 THR A OG1   1 
ATOM   1088 C CG2   . THR A 1 141 ? -10.332 -1.822 1.899   1.00 19.85 ? 441 THR A CG2   1 
ATOM   1089 N N     . ALA A 1 142 ? -10.571 1.215  -0.239  1.00 15.11 ? 442 ALA A N     1 
ATOM   1090 C CA    . ALA A 1 142 ? -11.282 2.461  -0.010  1.00 15.16 ? 442 ALA A CA    1 
ATOM   1091 C C     . ALA A 1 142 ? -12.392 2.662  -1.047  1.00 15.25 ? 442 ALA A C     1 
ATOM   1092 O O     . ALA A 1 142 ? -13.509 3.037  -0.720  1.00 15.01 ? 442 ALA A O     1 
ATOM   1093 C CB    . ALA A 1 142 ? -10.323 3.621  0.017   1.00 15.13 ? 442 ALA A CB    1 
ATOM   1094 N N     . ALA A 1 143 ? -12.070 2.470  -2.326  1.00 16.29 ? 443 ALA A N     1 
ATOM   1095 C CA    . ALA A 1 143 ? -13.042 2.579  -3.392  1.00 16.16 ? 443 ALA A CA    1 
ATOM   1096 C C     . ALA A 1 143 ? -14.206 1.622  -3.177  1.00 14.98 ? 443 ALA A C     1 
ATOM   1097 O O     . ALA A 1 143 ? -15.371 2.032  -3.271  1.00 15.66 ? 443 ALA A O     1 
ATOM   1098 C CB    . ALA A 1 143 ? -12.436 2.356  -4.738  1.00 15.39 ? 443 ALA A CB    1 
ATOM   1099 N N     A GLU A 1 144 ? -13.940 0.341  -2.848  0.50 14.33 ? 444 GLU A N     1 
ATOM   1100 N N     B GLU A 1 144 ? -13.908 0.348  -2.865  0.50 15.59 ? 444 GLU A N     1 
ATOM   1101 C CA    A GLU A 1 144 ? -15.050 -0.597 -2.680  0.50 14.96 ? 444 GLU A CA    1 
ATOM   1102 C CA    B GLU A 1 144 ? -14.969 -0.627 -2.642  0.50 16.89 ? 444 GLU A CA    1 
ATOM   1103 C C     A GLU A 1 144 ? -15.935 -0.191 -1.508  0.50 14.42 ? 444 GLU A C     1 
ATOM   1104 C C     B GLU A 1 144 ? -15.911 -0.134 -1.548  0.50 15.04 ? 444 GLU A C     1 
ATOM   1105 O O     A GLU A 1 144 ? -17.151 -0.347 -1.587  0.50 15.72 ? 444 GLU A O     1 
ATOM   1106 O O     B GLU A 1 144 ? -17.131 -0.139 -1.738  0.50 15.02 ? 444 GLU A O     1 
ATOM   1107 C CB    A GLU A 1 144 ? -14.541 -2.021 -2.442  0.50 16.48 ? 444 GLU A CB    1 
ATOM   1108 C CB    B GLU A 1 144 ? -14.294 -1.956 -2.293  0.50 19.71 ? 444 GLU A CB    1 
ATOM   1109 C CG    A GLU A 1 144 ? -13.899 -2.669 -3.663  0.50 16.08 ? 444 GLU A CG    1 
ATOM   1110 C CG    B GLU A 1 144 ? -15.261 -3.106 -2.021  0.50 21.82 ? 444 GLU A CG    1 
ATOM   1111 C CD    A GLU A 1 144 ? -12.924 -3.807 -3.317  0.50 19.20 ? 444 GLU A CD    1 
ATOM   1112 C CD    B GLU A 1 144 ? -14.510 -4.380 -1.671  0.50 23.93 ? 444 GLU A CD    1 
ATOM   1113 O OE1   A GLU A 1 144 ? -12.659 -4.075 -2.117  0.50 21.25 ? 444 GLU A OE1   1 
ATOM   1114 O OE1   B GLU A 1 144 ? -14.556 -4.785 -0.490  0.50 29.68 ? 444 GLU A OE1   1 
ATOM   1115 O OE2   A GLU A 1 144 ? -12.358 -4.427 -4.250  0.50 23.54 ? 444 GLU A OE2   1 
ATOM   1116 O OE2   B GLU A 1 144 ? -13.824 -4.927 -2.557  0.50 29.80 ? 444 GLU A OE2   1 
ATOM   1117 N N     . ILE A 1 145 ? -15.355 0.311  -0.415  1.00 14.31 ? 445 ILE A N     1 
ATOM   1118 C CA    . ILE A 1 145 ? -16.172 0.715  0.730   1.00 15.60 ? 445 ILE A CA    1 
ATOM   1119 C C     . ILE A 1 145 ? -17.007 1.953  0.416   1.00 14.81 ? 445 ILE A C     1 
ATOM   1120 O O     . ILE A 1 145 ? -18.188 1.996  0.742   1.00 15.16 ? 445 ILE A O     1 
ATOM   1121 C CB    . ILE A 1 145 ? -15.291 0.960  1.962   1.00 15.99 ? 445 ILE A CB    1 
ATOM   1122 C CG1   . ILE A 1 145 ? -14.695 -0.394 2.420   1.00 17.31 ? 445 ILE A CG1   1 
ATOM   1123 C CG2   . ILE A 1 145 ? -16.037 1.614  3.099   1.00 16.87 ? 445 ILE A CG2   1 
ATOM   1124 C CD1   . ILE A 1 145 ? -13.538 -0.275 3.382   1.00 18.44 ? 445 ILE A CD1   1 
ATOM   1125 N N     . LEU A 1 146 ? -16.406 2.952  -0.220  1.00 14.35 ? 446 LEU A N     1 
ATOM   1126 C CA    . LEU A 1 146 ? -17.123 4.185  -0.499  1.00 14.54 ? 446 LEU A CA    1 
ATOM   1127 C C     . LEU A 1 146 ? -18.280 3.914  -1.458  1.00 13.88 ? 446 LEU A C     1 
ATOM   1128 O O     . LEU A 1 146 ? -19.405 4.401  -1.274  1.00 14.40 ? 446 LEU A O     1 
ATOM   1129 C CB    . LEU A 1 146 ? -16.161 5.249  -1.036  1.00 14.61 ? 446 LEU A CB    1 
ATOM   1130 C CG    . LEU A 1 146 ? -15.673 6.259  0.007   1.00 15.41 ? 446 LEU A CG    1 
ATOM   1131 C CD1   . LEU A 1 146 ? -14.879 5.543  1.090   1.00 15.96 ? 446 LEU A CD1   1 
ATOM   1132 C CD2   . LEU A 1 146 ? -14.847 7.353  -0.611  1.00 16.51 ? 446 LEU A CD2   1 
ATOM   1133 N N     . PHE A 1 147 ? -18.016 3.119  -2.495  1.00 14.60 ? 447 PHE A N     1 
ATOM   1134 C CA    . PHE A 1 147 ? -19.070 2.768  -3.449  1.00 14.52 ? 447 PHE A CA    1 
ATOM   1135 C C     . PHE A 1 147 ? -20.155 1.932  -2.783  1.00 13.81 ? 447 PHE A C     1 
ATOM   1136 O O     . PHE A 1 147 ? -21.350 2.161  -2.995  1.00 14.43 ? 447 PHE A O     1 
ATOM   1137 C CB    . PHE A 1 147 ? -18.559 2.062  -4.719  1.00 13.82 ? 447 PHE A CB    1 
ATOM   1138 C CG    . PHE A 1 147 ? -18.028 3.083  -5.727  1.00 15.21 ? 447 PHE A CG    1 
ATOM   1139 C CD1   . PHE A 1 147 ? -16.736 3.609  -5.658  1.00 16.03 ? 447 PHE A CD1   1 
ATOM   1140 C CD2   . PHE A 1 147 ? -18.820 3.474  -6.783  1.00 15.95 ? 447 PHE A CD2   1 
ATOM   1141 C CE1   . PHE A 1 147 ? -16.307 4.541  -6.578  1.00 17.70 ? 447 PHE A CE1   1 
ATOM   1142 C CE2   . PHE A 1 147 ? -18.357 4.380  -7.720  1.00 17.12 ? 447 PHE A CE2   1 
ATOM   1143 C CZ    . PHE A 1 147 ? -17.103 4.890  -7.618  1.00 16.85 ? 447 PHE A CZ    1 
ATOM   1144 N N     . ASP A 1 148 ? -19.767 1.002  -1.915  1.00 15.10 ? 448 ASP A N     1 
ATOM   1145 C CA    . ASP A 1 148 ? -20.729 0.148  -1.246  1.00 15.87 ? 448 ASP A CA    1 
ATOM   1146 C C     . ASP A 1 148 ? -21.684 1.015  -0.430  1.00 14.29 ? 448 ASP A C     1 
ATOM   1147 O O     . ASP A 1 148 ? -22.907 0.817  -0.478  1.00 14.40 ? 448 ASP A O     1 
ATOM   1148 C CB    . ASP A 1 148 ? -20.074 -0.841 -0.287  1.00 15.61 ? 448 ASP A CB    1 
ATOM   1149 C CG    . ASP A 1 148 ? -19.484 -2.104 -0.896  1.00 17.06 ? 448 ASP A CG    1 
ATOM   1150 O OD1   . ASP A 1 148 ? -19.673 -2.311 -2.118  1.00 18.64 ? 448 ASP A OD1   1 
ATOM   1151 O OD2   . ASP A 1 148 ? -18.811 -2.875 -0.151  1.00 21.30 ? 448 ASP A OD2   1 
ATOM   1152 N N     . GLU A 1 149 ? -21.172 2.016  0.297   1.00 14.16 ? 449 GLU A N     1 
ATOM   1153 C CA    . GLU A 1 149 ? -22.029 2.742  1.206   1.00 14.54 ? 449 GLU A CA    1 
ATOM   1154 C C     . GLU A 1 149 ? -22.918 3.730  0.439   1.00 13.22 ? 449 GLU A C     1 
ATOM   1155 O O     . GLU A 1 149 ? -24.100 3.878  0.769   1.00 15.24 ? 449 GLU A O     1 
ATOM   1156 C CB    . GLU A 1 149 ? -21.233 3.461  2.300   1.00 16.17 ? 449 GLU A CB    1 
ATOM   1157 C CG    . GLU A 1 149 ? -20.627 2.478  3.306   1.00 16.29 ? 449 GLU A CG    1 
ATOM   1158 C CD    . GLU A 1 149 ? -21.652 1.564  3.938   1.00 18.55 ? 449 GLU A CD    1 
ATOM   1159 O OE1   . GLU A 1 149 ? -22.781 1.995  4.238   1.00 19.07 ? 449 GLU A OE1   1 
ATOM   1160 O OE2   . GLU A 1 149 ? -21.301 0.408  4.123   1.00 26.67 ? 449 GLU A OE2   1 
ATOM   1161 N N     . VAL A 1 150 ? -22.424 4.282  -0.651  1.00 14.51 ? 450 VAL A N     1 
ATOM   1162 C CA    . VAL A 1 150 ? -23.222 5.165  -1.477  1.00 14.98 ? 450 VAL A CA    1 
ATOM   1163 C C     . VAL A 1 150 ? -24.370 4.361  -2.110  1.00 14.68 ? 450 VAL A C     1 
ATOM   1164 O O     . VAL A 1 150 ? -25.512 4.820  -2.156  1.00 14.96 ? 450 VAL A O     1 
ATOM   1165 C CB    . VAL A 1 150 ? -22.348 5.935  -2.478  1.00 18.19 ? 450 VAL A CB    1 
ATOM   1166 C CG1   . VAL A 1 150 ? -23.181 6.517  -3.585  1.00 19.23 ? 450 VAL A CG1   1 
ATOM   1167 C CG2   . VAL A 1 150 ? -21.526 7.011  -1.751  1.00 17.93 ? 450 VAL A CG2   1 
ATOM   1168 N N     . LEU A 1 151 ? -24.091 3.159  -2.580  1.00 15.50 ? 451 LEU A N     1 
ATOM   1169 C CA    . LEU A 1 151 ? -25.122 2.364  -3.222  1.00 16.83 ? 451 LEU A CA    1 
ATOM   1170 C C     . LEU A 1 151 ? -26.159 1.871  -2.214  1.00 13.93 ? 451 LEU A C     1 
ATOM   1171 O O     . LEU A 1 151 ? -27.337 1.824  -2.530  1.00 16.47 ? 451 LEU A O     1 
ATOM   1172 C CB    . LEU A 1 151 ? -24.505 1.210  -4.001  1.00 16.60 ? 451 LEU A CB    1 
ATOM   1173 C CG    . LEU A 1 151 ? -23.879 1.659  -5.320  1.00 19.84 ? 451 LEU A CG    1 
ATOM   1174 C CD1   . LEU A 1 151 ? -22.960 0.570  -5.809  1.00 18.91 ? 451 LEU A CD1   1 
ATOM   1175 C CD2   . LEU A 1 151 ? -24.909 1.985  -6.357  1.00 21.79 ? 451 LEU A CD2   1 
ATOM   1176 N N     . THR A 1 152 ? -25.743 1.528  -0.989  1.00 15.78 ? 452 THR A N     1 
ATOM   1177 C CA    . THR A 1 152 ? -26.654 1.214  0.101   1.00 15.60 ? 452 THR A CA    1 
ATOM   1178 C C     . THR A 1 152 ? -27.609 2.374  0.364   1.00 14.71 ? 452 THR A C     1 
ATOM   1179 O O     . THR A 1 152 ? -28.820 2.161  0.493   1.00 16.46 ? 452 THR A O     1 
ATOM   1180 C CB    . THR A 1 152 ? -25.893 0.815  1.360   1.00 17.71 ? 452 THR A CB    1 
ATOM   1181 O OG1   . THR A 1 152 ? -25.285 -0.450 1.115   1.00 19.22 ? 452 THR A OG1   1 
ATOM   1182 C CG2   . THR A 1 152 ? -26.790 0.730  2.581   1.00 19.12 ? 452 THR A CG2   1 
ATOM   1183 N N     . PHE A 1 153 ? -27.074 3.590  0.430   1.00 14.79 ? 453 PHE A N     1 
ATOM   1184 C CA    . PHE A 1 153 ? -27.863 4.786  0.624   1.00 15.12 ? 453 PHE A CA    1 
ATOM   1185 C C     . PHE A 1 153 ? -28.884 4.928  -0.491  1.00 14.24 ? 453 PHE A C     1 
ATOM   1186 O O     . PHE A 1 153 ? -30.072 5.198  -0.232  1.00 15.35 ? 453 PHE A O     1 
ATOM   1187 C CB    . PHE A 1 153 ? -26.969 6.029  0.758   1.00 15.80 ? 453 PHE A CB    1 
ATOM   1188 C CG    . PHE A 1 153 ? -27.741 7.291  1.057   1.00 15.56 ? 453 PHE A CG    1 
ATOM   1189 C CD1   . PHE A 1 153 ? -28.350 8.012  0.033   1.00 15.41 ? 453 PHE A CD1   1 
ATOM   1190 C CD2   . PHE A 1 153 ? -27.889 7.722  2.360   1.00 16.01 ? 453 PHE A CD2   1 
ATOM   1191 C CE1   . PHE A 1 153 ? -29.053 9.179  0.313   1.00 15.29 ? 453 PHE A CE1   1 
ATOM   1192 C CE2   . PHE A 1 153 ? -28.589 8.880  2.646   1.00 16.81 ? 453 PHE A CE2   1 
ATOM   1193 C CZ    . PHE A 1 153 ? -29.154 9.620  1.622   1.00 16.32 ? 453 PHE A CZ    1 
ATOM   1194 N N     . ALA A 1 154 ? -28.463 4.770  -1.732  1.00 15.12 ? 454 ALA A N     1 
ATOM   1195 C CA    . ALA A 1 154 ? -29.324 4.965  -2.885  1.00 15.72 ? 454 ALA A CA    1 
ATOM   1196 C C     . ALA A 1 154 ? -30.501 4.000  -2.874  1.00 15.82 ? 454 ALA A C     1 
ATOM   1197 O O     . ALA A 1 154 ? -31.581 4.328  -3.380  1.00 16.82 ? 454 ALA A O     1 
ATOM   1198 C CB    . ALA A 1 154 ? -28.520 4.803  -4.152  1.00 15.63 ? 454 ALA A CB    1 
ATOM   1199 N N     . LYS A 1 155 ? -30.297 2.810  -2.279  1.00 16.63 ? 455 LYS A N     1 
ATOM   1200 C CA    . LYS A 1 155 ? -31.370 1.810  -2.213  1.00 18.79 ? 455 LYS A CA    1 
ATOM   1201 C C     . LYS A 1 155 ? -32.247 2.005  -0.977  1.00 17.96 ? 455 LYS A C     1 
ATOM   1202 O O     . LYS A 1 155 ? -33.483 1.966  -1.055  1.00 22.17 ? 455 LYS A O     1 
ATOM   1203 C CB    . LYS A 1 155 ? -30.711 0.413  -2.183  1.00 22.39 ? 455 LYS A CB    1 
ATOM   1204 C CG    . LYS A 1 155 ? -31.567 -0.748 -2.419  1.00 26.66 ? 455 LYS A CG    1 
ATOM   1205 C CD    . LYS A 1 155 ? -30.709 -2.010 -2.619  1.00 28.39 ? 455 LYS A CD    1 
ATOM   1206 C CE    . LYS A 1 155 ? -29.735 -2.246 -1.515  1.00 36.48 ? 455 LYS A CE    1 
ATOM   1207 N NZ    . LYS A 1 155 ? -30.413 -2.696 -0.291  1.00 37.94 ? 455 LYS A NZ    1 
ATOM   1208 N N     . ASP A 1 156 ? -31.634 2.276  0.170   1.00 18.72 ? 456 ASP A N     1 
ATOM   1209 C CA    . ASP A 1 156 ? -32.343 2.309  1.443   1.00 19.55 ? 456 ASP A CA    1 
ATOM   1210 C C     . ASP A 1 156 ? -33.023 3.656  1.698   1.00 18.01 ? 456 ASP A C     1 
ATOM   1211 O O     . ASP A 1 156 ? -33.910 3.739  2.551   1.00 22.35 ? 456 ASP A O     1 
ATOM   1212 C CB    . ASP A 1 156 ? -31.407 1.978  2.592   1.00 21.30 ? 456 ASP A CB    1 
ATOM   1213 C CG    . ASP A 1 156 ? -31.002 0.524  2.715   1.00 24.92 ? 456 ASP A CG    1 
ATOM   1214 O OD1   . ASP A 1 156 ? -31.477 -0.307 1.889   1.00 27.80 ? 456 ASP A OD1   1 
ATOM   1215 O OD2   . ASP A 1 156 ? -30.176 0.266  3.610   1.00 29.77 ? 456 ASP A OD2   1 
ATOM   1216 N N     . HIS A 1 157 ? -32.536 4.734  1.062   1.00 16.23 ? 457 HIS A N     1 
ATOM   1217 C CA    . HIS A 1 157 ? -33.072 6.070  1.151   1.00 16.19 ? 457 HIS A CA    1 
ATOM   1218 C C     . HIS A 1 157 ? -33.444 6.571  -0.230  1.00 17.64 ? 457 HIS A C     1 
ATOM   1219 O O     . HIS A 1 157 ? -33.043 7.654  -0.626  1.00 16.84 ? 457 HIS A O     1 
ATOM   1220 C CB    . HIS A 1 157 ? -32.114 6.987  1.890   1.00 17.78 ? 457 HIS A CB    1 
ATOM   1221 C CG    . HIS A 1 157 ? -31.802 6.551  3.261   1.00 20.14 ? 457 HIS A CG    1 
ATOM   1222 N ND1   . HIS A 1 157 ? -32.723 6.632  4.280   1.00 21.83 ? 457 HIS A ND1   1 
ATOM   1223 C CD2   . HIS A 1 157 ? -30.677 6.005  3.778   1.00 21.98 ? 457 HIS A CD2   1 
ATOM   1224 C CE1   . HIS A 1 157 ? -32.144 6.144  5.388   1.00 24.02 ? 457 HIS A CE1   1 
ATOM   1225 N NE2   . HIS A 1 157 ? -30.884 5.801  5.106   1.00 22.80 ? 457 HIS A NE2   1 
ATOM   1226 N N     . VAL A 1 158 ? -34.332 5.828  -0.897  1.00 17.01 ? 458 VAL A N     1 
ATOM   1227 C CA    . VAL A 1 158 ? -34.592 6.013  -2.307  1.00 16.89 ? 458 VAL A CA    1 
ATOM   1228 C C     . VAL A 1 158 ? -35.291 7.360  -2.601  1.00 18.59 ? 458 VAL A C     1 
ATOM   1229 O O     . VAL A 1 158 ? -35.182 7.820  -3.722  1.00 21.56 ? 458 VAL A O     1 
ATOM   1230 C CB    . VAL A 1 158 ? -35.335 4.782  -2.842  1.00 20.08 ? 458 VAL A CB    1 
ATOM   1231 C CG1   . VAL A 1 158 ? -36.812 4.848  -2.519  1.00 21.75 ? 458 VAL A CG1   1 
ATOM   1232 C CG2   . VAL A 1 158 ? -35.067 4.609  -4.318  1.00 23.02 ? 458 VAL A CG2   1 
ATOM   1233 N N     . LYS A 1 159 ? -36.032 7.972  -1.661  1.00 16.81 ? 459 LYS A N     1 
ATOM   1234 C CA    . LYS A 1 159 ? -36.695 9.232  -1.921  1.00 18.74 ? 459 LYS A CA    1 
ATOM   1235 C C     . LYS A 1 159 ? -35.811 10.436 -1.637  1.00 18.79 ? 459 LYS A C     1 
ATOM   1236 O O     . LYS A 1 159 ? -36.231 11.549 -1.902  1.00 21.01 ? 459 LYS A O     1 
ATOM   1237 C CB    . LYS A 1 159 ? -37.965 9.326  -1.079  1.00 21.56 ? 459 LYS A CB    1 
ATOM   1238 C CG    . LYS A 1 159 ? -39.014 8.243  -1.345  1.00 24.89 ? 459 LYS A CG    1 
ATOM   1239 C CD    . LYS A 1 159 ? -39.439 8.215  -2.803  1.00 30.06 ? 459 LYS A CD    1 
ATOM   1240 C CE    . LYS A 1 159 ? -40.736 8.811  -3.178  1.00 38.73 ? 459 LYS A CE    1 
ATOM   1241 N NZ    . LYS A 1 159 ? -41.082 8.371  -4.534  1.00 38.76 ? 459 LYS A NZ    1 
ATOM   1242 N N     . HIS A 1 160 ? -34.570 10.225 -1.146  1.00 16.99 ? 460 HIS A N     1 
ATOM   1243 C CA    . HIS A 1 160 ? -33.730 11.341 -0.757  1.00 16.37 ? 460 HIS A CA    1 
ATOM   1244 C C     . HIS A 1 160 ? -32.730 11.643 -1.864  1.00 14.52 ? 460 HIS A C     1 
ATOM   1245 O O     . HIS A 1 160 ? -31.710 10.975 -1.968  1.00 16.19 ? 460 HIS A O     1 
ATOM   1246 C CB    . HIS A 1 160 ? -32.985 11.112 0.563   1.00 15.21 ? 460 HIS A CB    1 
ATOM   1247 C CG    . HIS A 1 160 ? -32.380 12.361 1.051   1.00 17.08 ? 460 HIS A CG    1 
ATOM   1248 N ND1   . HIS A 1 160 ? -32.997 13.115 2.013   1.00 17.38 ? 460 HIS A ND1   1 
ATOM   1249 C CD2   . HIS A 1 160 ? -31.221 12.962 0.782   1.00 16.28 ? 460 HIS A CD2   1 
ATOM   1250 C CE1   . HIS A 1 160 ? -32.253 14.186 2.269   1.00 19.79 ? 460 HIS A CE1   1 
ATOM   1251 N NE2   . HIS A 1 160 ? -31.168 14.120 1.531   1.00 17.62 ? 460 HIS A NE2   1 
ATOM   1252 N N     . GLN A 1 161 ? -33.004 12.683 -2.649  1.00 14.17 ? 461 GLN A N     1 
ATOM   1253 C CA    . GLN A 1 161 ? -32.085 13.070 -3.706  1.00 14.37 ? 461 GLN A CA    1 
ATOM   1254 C C     . GLN A 1 161 ? -30.748 13.481 -3.116  1.00 13.68 ? 461 GLN A C     1 
ATOM   1255 O O     . GLN A 1 161 ? -30.711 14.160 -2.096  1.00 15.03 ? 461 GLN A O     1 
ATOM   1256 C CB    . GLN A 1 161 ? -32.578 14.249 -4.529  1.00 15.85 ? 461 GLN A CB    1 
ATOM   1257 C CG    . GLN A 1 161 ? -33.777 13.931 -5.391  1.00 17.78 ? 461 GLN A CG    1 
ATOM   1258 C CD    . GLN A 1 161 ? -34.128 15.117 -6.246  1.00 18.86 ? 461 GLN A CD    1 
ATOM   1259 O OE1   . GLN A 1 161 ? -35.208 15.703 -6.091  1.00 24.47 ? 461 GLN A OE1   1 
ATOM   1260 N NE2   . GLN A 1 161 ? -33.247 15.470 -7.148  1.00 19.16 ? 461 GLN A NE2   1 
ATOM   1261 N N     . LEU A 1 162 ? -29.649 13.028 -3.726  1.00 13.62 ? 462 LEU A N     1 
ATOM   1262 C CA    . LEU A 1 162 ? -28.327 13.397 -3.223  1.00 12.11 ? 462 LEU A CA    1 
ATOM   1263 C C     . LEU A 1 162 ? -27.332 13.364 -4.379  1.00 13.34 ? 462 LEU A C     1 
ATOM   1264 O O     . LEU A 1 162 ? -27.272 12.397 -5.137  1.00 14.70 ? 462 LEU A O     1 
ATOM   1265 C CB    . LEU A 1 162 ? -27.909 12.410 -2.134  1.00 14.17 ? 462 LEU A CB    1 
ATOM   1266 C CG    . LEU A 1 162 ? -26.658 12.738 -1.316  1.00 13.77 ? 462 LEU A CG    1 
ATOM   1267 C CD1   . LEU A 1 162 ? -26.933 13.993 -0.478  1.00 14.83 ? 462 LEU A CD1   1 
ATOM   1268 C CD2   . LEU A 1 162 ? -26.300 11.576 -0.440  1.00 14.88 ? 462 LEU A CD2   1 
ATOM   1269 N N     . THR A 1 163 ? -26.508 14.420 -4.428  1.00 13.12 ? 463 THR A N     1 
ATOM   1270 C CA    . THR A 1 163 ? -25.356 14.473 -5.301  1.00 13.69 ? 463 THR A CA    1 
ATOM   1271 C C     . THR A 1 163 ? -24.085 14.289 -4.467  1.00 14.62 ? 463 THR A C     1 
ATOM   1272 O O     . THR A 1 163 ? -23.787 15.101 -3.610  1.00 15.40 ? 463 THR A O     1 
ATOM   1273 C CB    . THR A 1 163 ? -25.278 15.806 -6.046  1.00 16.25 ? 463 THR A CB    1 
ATOM   1274 O OG1   . THR A 1 163 ? -26.374 15.916 -6.928  1.00 19.73 ? 463 THR A OG1   1 
ATOM   1275 C CG2   . THR A 1 163 ? -23.987 15.879 -6.853  1.00 18.06 ? 463 THR A CG2   1 
ATOM   1276 N N     . VAL A 1 164 ? -23.442 13.165 -4.717  1.00 14.04 ? 464 VAL A N     1 
ATOM   1277 C CA    . VAL A 1 164 ? -22.228 12.794 -4.006  1.00 13.43 ? 464 VAL A CA    1 
ATOM   1278 C C     . VAL A 1 164 ? -21.045 12.949 -4.949  1.00 13.51 ? 464 VAL A C     1 
ATOM   1279 O O     . VAL A 1 164 ? -21.076 12.530 -6.102  1.00 15.78 ? 464 VAL A O     1 
ATOM   1280 C CB    . VAL A 1 164 ? -22.279 11.336 -3.501  1.00 13.17 ? 464 VAL A CB    1 
ATOM   1281 C CG1   . VAL A 1 164 ? -21.003 10.924 -2.768  1.00 14.13 ? 464 VAL A CG1   1 
ATOM   1282 C CG2   . VAL A 1 164 ? -23.534 11.104 -2.681  1.00 13.59 ? 464 VAL A CG2   1 
ATOM   1283 N N     . LYS A 1 165 ? -19.999 13.629 -4.467  1.00 13.74 ? 465 LYS A N     1 
ATOM   1284 C CA    . LYS A 1 165 ? -18.753 13.719 -5.187  1.00 13.62 ? 465 LYS A CA    1 
ATOM   1285 C C     . LYS A 1 165 ? -17.626 13.073 -4.383  1.00 14.78 ? 465 LYS A C     1 
ATOM   1286 O O     . LYS A 1 165 ? -17.524 13.264 -3.174  1.00 14.95 ? 465 LYS A O     1 
ATOM   1287 C CB    . LYS A 1 165 ? -18.438 15.166 -5.535  1.00 14.79 ? 465 LYS A CB    1 
ATOM   1288 C CG    . LYS A 1 165 ? -19.381 15.740 -6.570  1.00 17.44 ? 465 LYS A CG    1 
ATOM   1289 C CD    . LYS A 1 165 ? -19.156 17.208 -6.840  1.00 19.43 ? 465 LYS A CD    1 
ATOM   1290 C CE    . LYS A 1 165 ? -20.031 17.758 -7.911  1.00 21.93 ? 465 LYS A CE    1 
ATOM   1291 N NZ    . LYS A 1 165 ? -20.005 19.219 -8.024  1.00 25.38 ? 465 LYS A NZ    1 
ATOM   1292 N N     . PHE A 1 166 ? -16.829 12.279 -5.101  1.00 13.85 ? 466 PHE A N     1 
ATOM   1293 C CA    . PHE A 1 166 ? -15.555 11.776 -4.607  1.00 14.30 ? 466 PHE A CA    1 
ATOM   1294 C C     . PHE A 1 166 ? -14.427 12.566 -5.241  1.00 14.05 ? 466 PHE A C     1 
ATOM   1295 O O     . PHE A 1 166 ? -14.265 12.504 -6.446  1.00 16.16 ? 466 PHE A O     1 
ATOM   1296 C CB    . PHE A 1 166 ? -15.397 10.281 -4.937  1.00 14.56 ? 466 PHE A CB    1 
ATOM   1297 C CG    . PHE A 1 166 ? -16.421 9.334  -4.319  1.00 14.68 ? 466 PHE A CG    1 
ATOM   1298 C CD1   . PHE A 1 166 ? -17.097 9.666  -3.154  1.00 14.32 ? 466 PHE A CD1   1 
ATOM   1299 C CD2   . PHE A 1 166 ? -16.622 8.064  -4.842  1.00 15.50 ? 466 PHE A CD2   1 
ATOM   1300 C CE1   . PHE A 1 166 ? -17.989 8.770  -2.571  1.00 15.33 ? 466 PHE A CE1   1 
ATOM   1301 C CE2   . PHE A 1 166 ? -17.486 7.178  -4.244  1.00 16.12 ? 466 PHE A CE2   1 
ATOM   1302 C CZ    . PHE A 1 166 ? -18.150 7.514  -3.104  1.00 16.36 ? 466 PHE A CZ    1 
ATOM   1303 N N     . VAL A 1 167 ? -13.792 13.387 -4.402  1.00 14.92 ? 467 VAL A N     1 
ATOM   1304 C CA    . VAL A 1 167 ? -12.822 14.358 -4.851  1.00 14.39 ? 467 VAL A CA    1 
ATOM   1305 C C     . VAL A 1 167 ? -11.417 13.793 -4.641  1.00 14.82 ? 467 VAL A C     1 
ATOM   1306 O O     . VAL A 1 167 ? -10.999 13.594 -3.505  1.00 15.96 ? 467 VAL A O     1 
ATOM   1307 C CB    . VAL A 1 167 ? -13.020 15.724 -4.151  1.00 15.19 ? 467 VAL A CB    1 
ATOM   1308 C CG1   . VAL A 1 167 ? -12.022 16.746 -4.656  1.00 17.76 ? 467 VAL A CG1   1 
ATOM   1309 C CG2   . VAL A 1 167 ? -14.452 16.186 -4.268  1.00 15.52 ? 467 VAL A CG2   1 
ATOM   1310 N N     . ILE A 1 168 ? -10.734 13.522 -5.755  1.00 16.36 ? 468 ILE A N     1 
ATOM   1311 C CA    . ILE A 1 168 ? -9.419  12.902 -5.786  1.00 15.95 ? 468 ILE A CA    1 
ATOM   1312 C C     . ILE A 1 168 ? -8.398  14.002 -6.069  1.00 16.32 ? 468 ILE A C     1 
ATOM   1313 O O     . ILE A 1 168 ? -8.566  14.730 -7.025  1.00 16.70 ? 468 ILE A O     1 
ATOM   1314 C CB    . ILE A 1 168 ? -9.392  11.796 -6.847  1.00 17.74 ? 468 ILE A CB    1 
ATOM   1315 C CG1   . ILE A 1 168 ? -10.573 10.821 -6.739  1.00 18.27 ? 468 ILE A CG1   1 
ATOM   1316 C CG2   . ILE A 1 168 ? -8.037  11.098 -6.808  1.00 18.73 ? 468 ILE A CG2   1 
ATOM   1317 C CD1   . ILE A 1 168 ? -10.758 10.208 -5.365  1.00 20.06 ? 468 ILE A CD1   1 
ATOM   1318 N N     . PHE A 1 169 ? -7.350  14.092 -5.251  1.00 16.83 ? 469 PHE A N     1 
ATOM   1319 C CA    . PHE A 1 169 ? -6.348  15.117 -5.414  1.00 17.58 ? 469 PHE A CA    1 
ATOM   1320 C C     . PHE A 1 169 ? -5.735  14.977 -6.804  1.00 17.87 ? 469 PHE A C     1 
ATOM   1321 O O     . PHE A 1 169 ? -5.524  13.847 -7.268  1.00 18.89 ? 469 PHE A O     1 
ATOM   1322 C CB    . PHE A 1 169 ? -5.285  15.014 -4.321  1.00 17.45 ? 469 PHE A CB    1 
ATOM   1323 C CG    . PHE A 1 169 ? -4.497  16.299 -4.191  1.00 17.93 ? 469 PHE A CG    1 
ATOM   1324 C CD1   . PHE A 1 169 ? -5.109  17.458 -3.698  1.00 18.79 ? 469 PHE A CD1   1 
ATOM   1325 C CD2   . PHE A 1 169 ? -3.195  16.387 -4.671  1.00 20.45 ? 469 PHE A CD2   1 
ATOM   1326 C CE1   . PHE A 1 169 ? -4.406  18.650 -3.593  1.00 20.62 ? 469 PHE A CE1   1 
ATOM   1327 C CE2   . PHE A 1 169 ? -2.492  17.586 -4.598  1.00 22.26 ? 469 PHE A CE2   1 
ATOM   1328 C CZ    . PHE A 1 169 ? -3.096  18.723 -4.060  1.00 22.68 ? 469 PHE A CZ    1 
ATOM   1329 N N     . PRO A 1 170 ? -5.477  16.096 -7.541  1.00 19.47 ? 470 PRO A N     1 
ATOM   1330 C CA    . PRO A 1 170 ? -5.087  15.985 -8.938  1.00 22.52 ? 470 PRO A CA    1 
ATOM   1331 C C     . PRO A 1 170 ? -3.911  15.058 -9.204  1.00 23.86 ? 470 PRO A C     1 
ATOM   1332 O O     . PRO A 1 170 ? -3.906  14.355 -10.219 1.00 27.82 ? 470 PRO A O     1 
ATOM   1333 C CB    . PRO A 1 170 ? -4.858  17.416 -9.382  1.00 23.17 ? 470 PRO A CB    1 
ATOM   1334 C CG    . PRO A 1 170 ? -5.782  18.200 -8.467  1.00 22.64 ? 470 PRO A CG    1 
ATOM   1335 C CD    . PRO A 1 170 ? -5.673  17.501 -7.138  1.00 21.52 ? 470 PRO A CD    1 
ATOM   1336 N N     . THR A 1 171 ? -2.939  15.038 -8.292  1.00 19.92 ? 471 THR A N     1 
ATOM   1337 C CA    . THR A 1 171 ? -1.756  14.219 -8.499  1.00 23.32 ? 471 THR A CA    1 
ATOM   1338 C C     . THR A 1 171 ? -1.893  12.787 -7.985  1.00 22.24 ? 471 THR A C     1 
ATOM   1339 O O     . THR A 1 171 ? -0.967  11.985 -8.201  1.00 23.24 ? 471 THR A O     1 
ATOM   1340 C CB    . THR A 1 171 ? -0.530  14.908 -7.902  1.00 26.56 ? 471 THR A CB    1 
ATOM   1341 O OG1   . THR A 1 171 ? -0.797  15.237 -6.541  1.00 28.54 ? 471 THR A OG1   1 
ATOM   1342 C CG2   . THR A 1 171 ? -0.206  16.171 -8.676  1.00 30.72 ? 471 THR A CG2   1 
ATOM   1343 N N     . ASP A 1 172 ? -3.029  12.450 -7.377  1.00 20.29 ? 472 ASP A N     1 
ATOM   1344 C CA    . ASP A 1 172 ? -3.284  11.091 -6.907  1.00 19.93 ? 472 ASP A CA    1 
ATOM   1345 C C     . ASP A 1 172 ? -3.912  10.258 -8.014  1.00 19.41 ? 472 ASP A C     1 
ATOM   1346 O O     . ASP A 1 172 ? -5.021  9.725  -7.876  1.00 18.95 ? 472 ASP A O     1 
ATOM   1347 C CB    . ASP A 1 172 ? -4.134  11.095 -5.650  1.00 21.39 ? 472 ASP A CB    1 
ATOM   1348 C CG    . ASP A 1 172 ? -3.411  11.577 -4.402  1.00 21.51 ? 472 ASP A CG    1 
ATOM   1349 O OD1   . ASP A 1 172 ? -2.156  11.664 -4.426  1.00 27.16 ? 472 ASP A OD1   1 
ATOM   1350 O OD2   . ASP A 1 172 ? -4.100  11.833 -3.417  1.00 20.06 ? 472 ASP A OD2   1 
ATOM   1351 N N     . LEU A 1 173 ? -3.196  10.101 -9.101  1.00 18.85 ? 473 LEU A N     1 
ATOM   1352 C CA    . LEU A 1 173 ? -3.741  9.475  -10.289 1.00 19.53 ? 473 LEU A CA    1 
ATOM   1353 C C     . LEU A 1 173 ? -4.056  7.995  -10.060 1.00 18.77 ? 473 LEU A C     1 
ATOM   1354 O O     . LEU A 1 173 ? -5.073  7.492  -10.549 1.00 18.42 ? 473 LEU A O     1 
ATOM   1355 C CB    . LEU A 1 173 ? -2.821  9.637  -11.478 1.00 22.05 ? 473 LEU A CB    1 
ATOM   1356 C CG    . LEU A 1 173 ? -3.360  9.058  -12.789 1.00 24.05 ? 473 LEU A CG    1 
ATOM   1357 C CD1   . LEU A 1 173 ? -4.633  9.744  -13.255 1.00 27.04 ? 473 LEU A CD1   1 
ATOM   1358 C CD2   . LEU A 1 173 ? -2.292  9.124  -13.846 1.00 24.30 ? 473 LEU A CD2   1 
ATOM   1359 N N     . GLU A 1 174 ? -3.225  7.265  -9.309  1.00 19.56 ? 474 GLU A N     1 
ATOM   1360 C CA    . GLU A 1 174 ? -3.535  5.858  -9.045  1.00 19.68 ? 474 GLU A CA    1 
ATOM   1361 C C     . GLU A 1 174 ? -4.852  5.709  -8.278  1.00 19.40 ? 474 GLU A C     1 
ATOM   1362 O O     . GLU A 1 174 ? -5.663  4.792  -8.536  1.00 18.95 ? 474 GLU A O     1 
ATOM   1363 C CB    . GLU A 1 174 ? -2.353  5.174  -8.346  1.00 24.67 ? 474 GLU A CB    1 
ATOM   1364 C CG    . GLU A 1 174 ? -1.101  5.092  -9.220  1.00 31.49 ? 474 GLU A CG    1 
ATOM   1365 C CD    . GLU A 1 174 ? -1.344  4.255  -10.480 1.00 40.35 ? 474 GLU A CD    1 
ATOM   1366 O OE1   . GLU A 1 174 ? -1.782  3.077  -10.342 1.00 48.20 ? 474 GLU A OE1   1 
ATOM   1367 O OE2   . GLU A 1 174 ? -1.132  4.774  -11.611 1.00 48.18 ? 474 GLU A OE2   1 
ATOM   1368 N N     . ILE A 1 175 ? -5.093  6.603  -7.302  1.00 18.12 ? 475 ILE A N     1 
ATOM   1369 C CA    . ILE A 1 175 ? -6.368  6.576  -6.597  1.00 17.41 ? 475 ILE A CA    1 
ATOM   1370 C C     . ILE A 1 175 ? -7.490  6.864  -7.585  1.00 17.26 ? 475 ILE A C     1 
ATOM   1371 O O     . ILE A 1 175 ? -8.526  6.179  -7.549  1.00 18.13 ? 475 ILE A O     1 
ATOM   1372 C CB    . ILE A 1 175 ? -6.362  7.508  -5.372  1.00 17.81 ? 475 ILE A CB    1 
ATOM   1373 C CG1   . ILE A 1 175 ? -5.276  7.058  -4.353  1.00 20.60 ? 475 ILE A CG1   1 
ATOM   1374 C CG2   . ILE A 1 175 ? -7.760  7.620  -4.760  1.00 18.62 ? 475 ILE A CG2   1 
ATOM   1375 C CD1   . ILE A 1 175 ? -5.176  7.979  -3.152  1.00 19.88 ? 475 ILE A CD1   1 
ATOM   1376 N N     . TYR A 1 176 ? -7.336  7.931  -8.405  1.00 16.45 ? 476 TYR A N     1 
ATOM   1377 C CA    . TYR A 1 176 ? -8.356  8.229  -9.406  1.00 16.93 ? 476 TYR A CA    1 
ATOM   1378 C C     . TYR A 1 176 ? -8.695  7.009  -10.259 1.00 15.71 ? 476 TYR A C     1 
ATOM   1379 O O     . TYR A 1 176 ? -9.886  6.730  -10.474 1.00 17.11 ? 476 TYR A O     1 
ATOM   1380 C CB    . TYR A 1 176 ? -7.861  9.351  -10.318 1.00 17.71 ? 476 TYR A CB    1 
ATOM   1381 C CG    . TYR A 1 176 ? -8.970  9.766  -11.283 1.00 19.28 ? 476 TYR A CG    1 
ATOM   1382 C CD1   . TYR A 1 176 ? -10.024 10.583 -10.868 1.00 21.41 ? 476 TYR A CD1   1 
ATOM   1383 C CD2   . TYR A 1 176 ? -9.014  9.301  -12.599 1.00 22.43 ? 476 TYR A CD2   1 
ATOM   1384 C CE1   . TYR A 1 176 ? -11.057 10.946 -11.713 1.00 24.67 ? 476 TYR A CE1   1 
ATOM   1385 C CE2   . TYR A 1 176 ? -10.084 9.634  -13.437 1.00 24.52 ? 476 TYR A CE2   1 
ATOM   1386 C CZ    . TYR A 1 176 ? -11.080 10.476 -13.004 1.00 25.63 ? 476 TYR A CZ    1 
ATOM   1387 O OH    . TYR A 1 176 ? -12.135 10.859 -13.781 1.00 31.17 ? 476 TYR A OH    1 
ATOM   1388 N N     . LYS A 1 177 ? -7.668  6.302  -10.722 1.00 17.88 ? 477 LYS A N     1 
ATOM   1389 C CA    . LYS A 1 177 ? -7.918  5.132  -11.553 1.00 18.01 ? 477 LYS A CA    1 
ATOM   1390 C C     . LYS A 1 177 ? -8.647  4.001  -10.826 1.00 18.06 ? 477 LYS A C     1 
ATOM   1391 O O     . LYS A 1 177 ? -9.561  3.368  -11.400 1.00 18.81 ? 477 LYS A O     1 
ATOM   1392 C CB    . LYS A 1 177 ? -6.617  4.613  -12.141 1.00 19.64 ? 477 LYS A CB    1 
ATOM   1393 C CG    . LYS A 1 177 ? -6.031  5.533  -13.170 1.00 23.09 ? 477 LYS A CG    1 
ATOM   1394 C CD    . LYS A 1 177 ? -4.649  5.042  -13.608 1.00 27.17 ? 477 LYS A CD    1 
ATOM   1395 C CE    . LYS A 1 177 ? -4.145  5.673  -14.863 1.00 33.46 ? 477 LYS A CE    1 
ATOM   1396 N NZ    . LYS A 1 177 ? -2.844  5.094  -15.209 1.00 41.67 ? 477 LYS A NZ    1 
ATOM   1397 N N     . ALA A 1 178 ? -8.310  3.794  -9.550  1.00 16.80 ? 478 ALA A N     1 
ATOM   1398 C CA    . ALA A 1 178 ? -9.016  2.810  -8.746  1.00 16.60 ? 478 ALA A CA    1 
ATOM   1399 C C     . ALA A 1 178 ? -10.496 3.190  -8.587  1.00 15.31 ? 478 ALA A C     1 
ATOM   1400 O O     . ALA A 1 178 ? -11.379 2.317  -8.657  1.00 16.24 ? 478 ALA A O     1 
ATOM   1401 C CB    . ALA A 1 178 ? -8.344  2.671  -7.390  1.00 18.24 ? 478 ALA A CB    1 
ATOM   1402 N N     . PHE A 1 179 ? -10.809 4.469  -8.297  1.00 15.77 ? 479 PHE A N     1 
ATOM   1403 C CA    . PHE A 1 179 ? -12.190 4.915  -8.153  1.00 14.27 ? 479 PHE A CA    1 
ATOM   1404 C C     . PHE A 1 179 ? -12.912 4.794  -9.495  1.00 14.90 ? 479 PHE A C     1 
ATOM   1405 O O     . PHE A 1 179 ? -14.076 4.415  -9.529  1.00 14.90 ? 479 PHE A O     1 
ATOM   1406 C CB    . PHE A 1 179 ? -12.221 6.367  -7.590  1.00 15.03 ? 479 PHE A CB    1 
ATOM   1407 C CG    . PHE A 1 179 ? -12.131 6.365  -6.063  1.00 14.48 ? 479 PHE A CG    1 
ATOM   1408 C CD1   . PHE A 1 179 ? -11.017 5.878  -5.385  1.00 17.12 ? 479 PHE A CD1   1 
ATOM   1409 C CD2   . PHE A 1 179 ? -13.202 6.804  -5.300  1.00 16.68 ? 479 PHE A CD2   1 
ATOM   1410 C CE1   . PHE A 1 179 ? -10.969 5.894  -3.995  1.00 17.26 ? 479 PHE A CE1   1 
ATOM   1411 C CE2   . PHE A 1 179 ? -13.174 6.767  -3.926  1.00 16.68 ? 479 PHE A CE2   1 
ATOM   1412 C CZ    . PHE A 1 179 ? -12.052 6.321  -3.273  1.00 17.10 ? 479 PHE A CZ    1 
ATOM   1413 N N     A SER A 1 180 ? -12.269 5.159  -10.610 0.50 16.35 ? 480 SER A N     1 
ATOM   1414 N N     B SER A 1 180 ? -12.246 5.167  -10.588 0.50 16.50 ? 480 SER A N     1 
ATOM   1415 C CA    A SER A 1 180 ? -12.912 5.116  -11.921 0.50 16.72 ? 480 SER A CA    1 
ATOM   1416 C CA    B SER A 1 180 ? -12.816 5.114  -11.926 0.50 17.07 ? 480 SER A CA    1 
ATOM   1417 C C     A SER A 1 180 ? -13.183 3.669  -12.337 0.50 15.71 ? 480 SER A C     1 
ATOM   1418 C C     B SER A 1 180 ? -13.172 3.681  -12.311 0.50 15.94 ? 480 SER A C     1 
ATOM   1419 O O     A SER A 1 180 ? -14.234 3.342  -12.903 0.50 15.25 ? 480 SER A O     1 
ATOM   1420 O O     B SER A 1 180 ? -14.252 3.387  -12.835 0.50 16.17 ? 480 SER A O     1 
ATOM   1421 C CB    A SER A 1 180 ? -12.075 5.835  -12.974 0.50 18.80 ? 480 SER A CB    1 
ATOM   1422 C CB    B SER A 1 180 ? -11.830 5.693  -12.908 0.50 18.48 ? 480 SER A CB    1 
ATOM   1423 O OG    A SER A 1 180 ? -11.869 7.215  -12.683 0.50 20.85 ? 480 SER A OG    1 
ATOM   1424 O OG    B SER A 1 180 ? -12.385 5.722  -14.212 0.50 20.89 ? 480 SER A OG    1 
ATOM   1425 N N     . SER A 1 181 ? -12.271 2.764  -11.988 1.00 15.97 ? 481 SER A N     1 
ATOM   1426 C CA    . SER A 1 181 ? -12.487 1.348  -12.245 1.00 16.66 ? 481 SER A CA    1 
ATOM   1427 C C     . SER A 1 181 ? -13.671 0.825  -11.446 1.00 16.41 ? 481 SER A C     1 
ATOM   1428 O O     . SER A 1 181 ? -14.481 0.070  -11.987 1.00 16.57 ? 481 SER A O     1 
ATOM   1429 C CB    . SER A 1 181 ? -11.194 0.554  -11.945 1.00 18.35 ? 481 SER A CB    1 
ATOM   1430 O OG    . SER A 1 181 ? -11.471 -0.844 -12.034 1.00 22.36 ? 481 SER A OG    1 
ATOM   1431 N N     . GLU A 1 182 ? -13.777 1.225  -10.179 1.00 15.15 ? 482 GLU A N     1 
ATOM   1432 C CA    . GLU A 1 182 ? -14.927 0.830  -9.376  1.00 15.58 ? 482 GLU A CA    1 
ATOM   1433 C C     . GLU A 1 182 ? -16.231 1.348  -9.973  1.00 15.84 ? 482 GLU A C     1 
ATOM   1434 O O     . GLU A 1 182 ? -17.202 0.617  -10.031 1.00 16.39 ? 482 GLU A O     1 
ATOM   1435 C CB    . GLU A 1 182 ? -14.713 1.278  -7.927  1.00 16.80 ? 482 GLU A CB    1 
ATOM   1436 C CG    . GLU A 1 182 ? -15.519 0.488  -6.904  1.00 17.14 ? 482 GLU A CG    1 
ATOM   1437 C CD    . GLU A 1 182 ? -15.165 -0.980 -6.791  1.00 19.81 ? 482 GLU A CD    1 
ATOM   1438 O OE1   . GLU A 1 182 ? -14.023 -1.361 -7.063  1.00 22.00 ? 482 GLU A OE1   1 
ATOM   1439 O OE2   . GLU A 1 182 ? -16.055 -1.719 -6.384  1.00 21.72 ? 482 GLU A OE2   1 
ATOM   1440 N N     . MET A 1 183 ? -16.260 2.614  -10.364 1.00 14.36 ? 483 MET A N     1 
ATOM   1441 C CA    . MET A 1 183 ? -17.455 3.164  -10.970 1.00 15.21 ? 483 MET A CA    1 
ATOM   1442 C C     . MET A 1 183 ? -17.867 2.356  -12.198 1.00 14.20 ? 483 MET A C     1 
ATOM   1443 O O     . MET A 1 183 ? -19.045 2.039  -12.382 1.00 15.28 ? 483 MET A O     1 
ATOM   1444 C CB    . MET A 1 183 ? -17.229 4.633  -11.374 1.00 15.75 ? 483 MET A CB    1 
ATOM   1445 C CG    . MET A 1 183 ? -18.460 5.224  -11.997 1.00 15.89 ? 483 MET A CG    1 
ATOM   1446 S SD    . MET A 1 183 ? -18.451 6.980  -12.287 1.00 18.58 ? 483 MET A SD    1 
ATOM   1447 C CE    . MET A 1 183 ? -18.806 7.564  -10.626 1.00 18.74 ? 483 MET A CE    1 
ATOM   1448 N N     . ALA A 1 184 ? -16.905 1.984  -13.038 1.00 15.00 ? 484 ALA A N     1 
ATOM   1449 C CA    . ALA A 1 184 ? -17.158 1.213  -14.252 1.00 15.39 ? 484 ALA A CA    1 
ATOM   1450 C C     . ALA A 1 184 ? -17.756 -0.147 -13.907 1.00 15.98 ? 484 ALA A C     1 
ATOM   1451 O O     . ALA A 1 184 ? -18.754 -0.568 -14.512 1.00 16.59 ? 484 ALA A O     1 
ATOM   1452 C CB    . ALA A 1 184 ? -15.900 1.071  -15.094 1.00 16.73 ? 484 ALA A CB    1 
ATOM   1453 N N     . LYS A 1 185 ? -17.210 -0.796 -12.864 1.00 16.45 ? 485 LYS A N     1 
ATOM   1454 C CA    . LYS A 1 185 ? -17.704 -2.115 -12.453 1.00 17.74 ? 485 LYS A CA    1 
ATOM   1455 C C     . LYS A 1 185 ? -19.154 -2.010 -11.955 1.00 16.39 ? 485 LYS A C     1 
ATOM   1456 O O     . LYS A 1 185 ? -20.018 -2.783 -12.352 1.00 16.95 ? 485 LYS A O     1 
ATOM   1457 C CB    . LYS A 1 185 ? -16.834 -2.688 -11.328 1.00 21.79 ? 485 LYS A CB    1 
ATOM   1458 C CG    . LYS A 1 185 ? -15.495 -3.250 -11.727 1.00 25.12 ? 485 LYS A CG    1 
ATOM   1459 C CD    . LYS A 1 185 ? -14.679 -3.730 -10.518 1.00 29.19 ? 485 LYS A CD    1 
ATOM   1460 C CE    . LYS A 1 185 ? -13.228 -3.810 -10.802 1.00 37.30 ? 485 LYS A CE    1 
ATOM   1461 N NZ    . LYS A 1 185 ? -12.552 -4.402 -9.651  1.00 43.86 ? 485 LYS A NZ    1 
ATOM   1462 N N     . ARG A 1 186 ? -19.413 -1.039 -11.084 1.00 15.42 ? 486 ARG A N     1 
ATOM   1463 C CA    . ARG A 1 186 ? -20.754 -0.933 -10.531 1.00 15.15 ? 486 ARG A CA    1 
ATOM   1464 C C     . ARG A 1 186 ? -21.771 -0.524 -11.602 1.00 15.17 ? 486 ARG A C     1 
ATOM   1465 O O     . ARG A 1 186 ? -22.894 -0.999 -11.591 1.00 15.94 ? 486 ARG A O     1 
ATOM   1466 C CB    . ARG A 1 186 ? -20.844 0.029  -9.350  1.00 16.80 ? 486 ARG A CB    1 
ATOM   1467 C CG    . ARG A 1 186 ? -19.844 -0.197 -8.232  1.00 16.73 ? 486 ARG A CG    1 
ATOM   1468 C CD    . ARG A 1 186 ? -19.963 -1.548 -7.600  1.00 18.03 ? 486 ARG A CD    1 
ATOM   1469 N NE    . ARG A 1 186 ? -18.926 -1.632 -6.565  1.00 18.56 ? 486 ARG A NE    1 
ATOM   1470 C CZ    . ARG A 1 186 ? -19.118 -1.563 -5.243  1.00 16.83 ? 486 ARG A CZ    1 
ATOM   1471 N NH1   . ARG A 1 186 ? -20.356 -1.558 -4.746  1.00 19.28 ? 486 ARG A NH1   1 
ATOM   1472 N NH2   . ARG A 1 186 ? -18.062 -1.582 -4.440  1.00 18.62 ? 486 ARG A NH2   1 
ATOM   1473 N N     A SER A 1 187 ? -21.364 0.377  -12.505 0.50 16.78 ? 487 SER A N     1 
ATOM   1474 N N     B SER A 1 187 ? -21.404 0.411  -12.478 0.50 13.87 ? 487 SER A N     1 
ATOM   1475 C CA    A SER A 1 187 ? -22.222 0.909  -13.556 0.50 18.61 ? 487 SER A CA    1 
ATOM   1476 C CA    B SER A 1 187 ? -22.295 0.870  -13.533 0.50 13.31 ? 487 SER A CA    1 
ATOM   1477 C C     A SER A 1 187 ? -22.619 -0.184 -14.549 0.50 17.43 ? 487 SER A C     1 
ATOM   1478 C C     B SER A 1 187 ? -22.655 -0.292 -14.465 0.50 13.11 ? 487 SER A C     1 
ATOM   1479 O O     A SER A 1 187 ? -23.763 -0.216 -15.024 0.50 19.05 ? 487 SER A O     1 
ATOM   1480 O O     B SER A 1 187 ? -23.826 -0.470 -14.837 0.50 14.85 ? 487 SER A O     1 
ATOM   1481 C CB    A SER A 1 187 ? -21.523 2.055  -14.257 0.50 20.73 ? 487 SER A CB    1 
ATOM   1482 C CB    B SER A 1 187 ? -21.629 2.010  -14.272 0.50 12.63 ? 487 SER A CB    1 
ATOM   1483 O OG    A SER A 1 187 ? -22.299 2.547  -15.346 0.50 25.55 ? 487 SER A OG    1 
ATOM   1484 O OG    B SER A 1 187 ? -21.399 3.134  -13.434 0.50 11.30 ? 487 SER A OG    1 
ATOM   1485 N N     A LYS A 1 188 ? -21.662 -1.050 -14.902 0.50 16.82 ? 488 LYS A N     1 
ATOM   1486 N N     B LYS A 1 188 ? -21.637 -1.067 -14.867 0.50 14.14 ? 488 LYS A N     1 
ATOM   1487 C CA    A LYS A 1 188 ? -21.984 -2.113 -15.836 0.50 17.39 ? 488 LYS A CA    1 
ATOM   1488 C CA    B LYS A 1 188 ? -21.884 -2.146 -15.807 0.50 16.08 ? 488 LYS A CA    1 
ATOM   1489 C C     A LYS A 1 188 ? -22.943 -3.087 -15.159 0.50 16.97 ? 488 LYS A C     1 
ATOM   1490 C C     B LYS A 1 188 ? -22.867 -3.133 -15.188 0.50 16.31 ? 488 LYS A C     1 
ATOM   1491 O O     A LYS A 1 188 ? -23.965 -3.462 -15.738 0.50 16.96 ? 488 LYS A O     1 
ATOM   1492 O O     B LYS A 1 188 ? -23.815 -3.573 -15.844 0.50 17.42 ? 488 LYS A O     1 
ATOM   1493 C CB    A LYS A 1 188 ? -20.714 -2.824 -16.324 0.50 18.38 ? 488 LYS A CB    1 
ATOM   1494 C CB    B LYS A 1 188 ? -20.575 -2.869 -16.154 0.50 17.67 ? 488 LYS A CB    1 
ATOM   1495 C CG    A LYS A 1 188 ? -19.815 -1.988 -17.235 0.50 21.42 ? 488 LYS A CG    1 
ATOM   1496 C CG    B LYS A 1 188 ? -20.708 -4.057 -17.078 0.50 21.53 ? 488 LYS A CG    1 
ATOM   1497 C CD    A LYS A 1 188 ? -18.493 -2.697 -17.526 0.50 24.90 ? 488 LYS A CD    1 
ATOM   1498 C CD    B LYS A 1 188 ? -19.428 -4.822 -17.373 0.50 25.01 ? 488 LYS A CD    1 
ATOM   1499 C CE    A LYS A 1 188 ? -17.669 -2.099 -18.617 0.50 28.78 ? 488 LYS A CE    1 
ATOM   1500 C CE    B LYS A 1 188 ? -19.762 -6.049 -18.157 0.50 27.76 ? 488 LYS A CE    1 
ATOM   1501 N NZ    A LYS A 1 188 ? -16.842 -0.979 -18.161 0.50 30.34 ? 488 LYS A NZ    1 
ATOM   1502 N NZ    B LYS A 1 188 ? -18.637 -6.395 -19.025 0.50 32.75 ? 488 LYS A NZ    1 
ATOM   1503 N N     . MET A 1 189 ? -22.639 -3.467 -13.917 1.00 16.20 ? 489 MET A N     1 
ATOM   1504 C CA    . MET A 1 189 ? -23.439 -4.479 -13.245 1.00 16.27 ? 489 MET A CA    1 
ATOM   1505 C C     . MET A 1 189 ? -24.879 -3.976 -13.100 1.00 15.93 ? 489 MET A C     1 
ATOM   1506 O O     . MET A 1 189 ? -25.814 -4.716 -13.347 1.00 17.40 ? 489 MET A O     1 
ATOM   1507 C CB    . MET A 1 189 ? -22.882 -4.780 -11.854 1.00 18.17 ? 489 MET A CB    1 
ATOM   1508 C CG    . MET A 1 189 ? -23.720 -5.733 -11.091 1.00 21.83 ? 489 MET A CG    1 
ATOM   1509 S SD    . MET A 1 189 ? -22.961 -6.315 -9.567  1.00 25.21 ? 489 MET A SD    1 
ATOM   1510 C CE    . MET A 1 189 ? -22.703 -4.794 -8.668  1.00 27.42 ? 489 MET A CE    1 
ATOM   1511 N N     . LEU A 1 190 ? -25.055 -2.716 -12.710 1.00 16.54 ? 490 LEU A N     1 
ATOM   1512 C CA    . LEU A 1 190 ? -26.386 -2.189 -12.419 1.00 16.60 ? 490 LEU A CA    1 
ATOM   1513 C C     . LEU A 1 190 ? -27.016 -1.468 -13.606 1.00 15.90 ? 490 LEU A C     1 
ATOM   1514 O O     . LEU A 1 190 ? -28.074 -0.846 -13.467 1.00 16.05 ? 490 LEU A O     1 
ATOM   1515 C CB    . LEU A 1 190 ? -26.327 -1.321 -11.180 1.00 17.33 ? 490 LEU A CB    1 
ATOM   1516 C CG    . LEU A 1 190 ? -26.050 -1.987 -9.841  1.00 20.13 ? 490 LEU A CG    1 
ATOM   1517 C CD1   . LEU A 1 190 ? -25.766 -0.936 -8.758  1.00 23.73 ? 490 LEU A CD1   1 
ATOM   1518 C CD2   . LEU A 1 190 ? -27.217 -2.845 -9.452  1.00 23.75 ? 490 LEU A CD2   1 
ATOM   1519 N N     . SER A 1 191 ? -26.402 -1.564 -14.779 1.00 15.71 ? 491 SER A N     1 
ATOM   1520 C CA    . SER A 1 191 ? -26.909 -0.959 -16.001 1.00 16.26 ? 491 SER A CA    1 
ATOM   1521 C C     . SER A 1 191 ? -27.165 0.529  -15.788 1.00 17.66 ? 491 SER A C     1 
ATOM   1522 O O     . SER A 1 191 ? -28.186 1.028  -16.210 1.00 19.90 ? 491 SER A O     1 
ATOM   1523 C CB    . SER A 1 191 ? -28.152 -1.662 -16.520 1.00 18.88 ? 491 SER A CB    1 
ATOM   1524 O OG    . SER A 1 191 ? -27.883 -2.980 -16.898 1.00 19.19 ? 491 SER A OG    1 
ATOM   1525 N N     . LEU A 1 192 ? -26.226 1.229  -15.159 1.00 15.76 ? 492 LEU A N     1 
ATOM   1526 C CA    . LEU A 1 192 ? -26.377 2.654  -14.883 1.00 16.59 ? 492 LEU A CA    1 
ATOM   1527 C C     . LEU A 1 192 ? -25.955 3.465  -16.092 1.00 17.12 ? 492 LEU A C     1 
ATOM   1528 O O     . LEU A 1 192 ? -25.001 3.130  -16.785 1.00 19.58 ? 492 LEU A O     1 
ATOM   1529 C CB    . LEU A 1 192 ? -25.565 3.063  -13.657 1.00 15.16 ? 492 LEU A CB    1 
ATOM   1530 C CG    . LEU A 1 192 ? -25.826 2.271  -12.377 1.00 17.10 ? 492 LEU A CG    1 
ATOM   1531 C CD1   . LEU A 1 192 ? -24.914 2.802  -11.301 1.00 19.58 ? 492 LEU A CD1   1 
ATOM   1532 C CD2   . LEU A 1 192 ? -27.273 2.340  -11.981 1.00 17.60 ? 492 LEU A CD2   1 
ATOM   1533 N N     . ASN A 1 193 ? -26.607 4.600  -16.248 1.00 15.49 ? 493 ASN A N     1 
ATOM   1534 C CA    . ASN A 1 193 ? -26.204 5.594  -17.238 1.00 14.82 ? 493 ASN A CA    1 
ATOM   1535 C C     . ASN A 1 193 ? -25.073 6.454  -16.676 1.00 14.80 ? 493 ASN A C     1 
ATOM   1536 O O     . ASN A 1 193 ? -25.141 6.949  -15.546 1.00 15.83 ? 493 ASN A O     1 
ATOM   1537 C CB    . ASN A 1 193 ? -27.384 6.465  -17.662 1.00 15.25 ? 493 ASN A CB    1 
ATOM   1538 C CG    . ASN A 1 193 ? -28.409 5.639  -18.407 1.00 18.09 ? 493 ASN A CG    1 
ATOM   1539 O OD1   . ASN A 1 193 ? -28.068 4.749  -19.182 1.00 20.09 ? 493 ASN A OD1   1 
ATOM   1540 N ND2   . ASN A 1 193 ? -29.669 5.928  -18.188 1.00 18.69 ? 493 ASN A ND2   1 
ATOM   1541 N N     . ASN A 1 194 ? -24.042 6.593  -17.508 1.00 15.24 ? 494 ASN A N     1 
ATOM   1542 C CA    . ASN A 1 194 ? -22.805 7.269  -17.179 1.00 15.18 ? 494 ASN A CA    1 
ATOM   1543 C C     . ASN A 1 194 ? -22.690 8.544  -18.004 1.00 15.22 ? 494 ASN A C     1 
ATOM   1544 O O     . ASN A 1 194 ? -23.184 8.627  -19.127 1.00 15.80 ? 494 ASN A O     1 
ATOM   1545 C CB    . ASN A 1 194 ? -21.577 6.412  -17.427 1.00 15.54 ? 494 ASN A CB    1 
ATOM   1546 C CG    . ASN A 1 194 ? -21.543 5.174  -16.551 1.00 18.14 ? 494 ASN A CG    1 
ATOM   1547 O OD1   . ASN A 1 194 ? -21.651 4.041  -17.031 1.00 23.95 ? 494 ASN A OD1   1 
ATOM   1548 N ND2   . ASN A 1 194 ? -21.361 5.353  -15.247 1.00 19.70 ? 494 ASN A ND2   1 
ATOM   1549 N N     . TYR A 1 195 ? -21.939 9.486  -17.449 1.00 15.17 ? 495 TYR A N     1 
ATOM   1550 C CA    . TYR A 1 195 ? -21.673 10.754 -18.096 1.00 16.26 ? 495 TYR A CA    1 
ATOM   1551 C C     . TYR A 1 195 ? -20.188 11.094 -17.956 1.00 17.21 ? 495 TYR A C     1 
ATOM   1552 O O     . TYR A 1 195 ? -19.522 10.629 -17.021 1.00 15.90 ? 495 TYR A O     1 
ATOM   1553 C CB    . TYR A 1 195 ? -22.547 11.840 -17.470 1.00 15.10 ? 495 TYR A CB    1 
ATOM   1554 C CG    . TYR A 1 195 ? -24.027 11.592 -17.689 1.00 15.32 ? 495 TYR A CG    1 
ATOM   1555 C CD1   . TYR A 1 195 ? -24.646 11.907 -18.895 1.00 15.82 ? 495 TYR A CD1   1 
ATOM   1556 C CD2   . TYR A 1 195 ? -24.801 10.940 -16.712 1.00 16.33 ? 495 TYR A CD2   1 
ATOM   1557 C CE1   . TYR A 1 195 ? -25.990 11.645 -19.093 1.00 16.18 ? 495 TYR A CE1   1 
ATOM   1558 C CE2   . TYR A 1 195 ? -26.135 10.674 -16.924 1.00 16.60 ? 495 TYR A CE2   1 
ATOM   1559 C CZ    . TYR A 1 195 ? -26.725 11.041 -18.110 1.00 16.74 ? 495 TYR A CZ    1 
ATOM   1560 O OH    . TYR A 1 195 ? -28.051 10.781 -18.346 1.00 19.69 ? 495 TYR A OH    1 
ATOM   1561 N N     A SER A 1 196 ? -19.730 11.961 -18.866 0.50 16.94 ? 496 SER A N     1 
ATOM   1562 N N     B SER A 1 196 ? -19.696 11.935 -18.881 0.50 17.70 ? 496 SER A N     1 
ATOM   1563 C CA    A SER A 1 196 ? -18.379 12.484 -18.919 0.50 18.48 ? 496 SER A CA    1 
ATOM   1564 C CA    B SER A 1 196 ? -18.339 12.465 -18.872 0.50 20.02 ? 496 SER A CA    1 
ATOM   1565 C C     A SER A 1 196 ? -18.490 13.995 -18.812 0.50 20.67 ? 496 SER A C     1 
ATOM   1566 C C     B SER A 1 196 ? -18.396 13.983 -18.833 0.50 21.57 ? 496 SER A C     1 
ATOM   1567 O O     A SER A 1 196 ? -19.004 14.621 -19.729 0.50 22.28 ? 496 SER A O     1 
ATOM   1568 O O     B SER A 1 196 ? -18.682 14.613 -19.845 0.50 22.19 ? 496 SER A O     1 
ATOM   1569 C CB    A SER A 1 196 ? -17.689 12.085 -20.209 0.50 19.71 ? 496 SER A CB    1 
ATOM   1570 C CB    B SER A 1 196 ? -17.542 12.020 -20.075 0.50 23.11 ? 496 SER A CB    1 
ATOM   1571 O OG    A SER A 1 196 ? -17.625 10.670 -20.363 0.50 20.71 ? 496 SER A OG    1 
ATOM   1572 O OG    B SER A 1 196 ? -16.282 12.683 -20.121 0.50 25.26 ? 496 SER A OG    1 
ATOM   1573 N N     . VAL A 1 197 ? -18.079 14.534 -17.655 1.00 25.21 ? 497 VAL A N     1 
ATOM   1574 C CA    . VAL A 1 197 ? -18.133 15.961 -17.382 1.00 28.23 ? 497 VAL A CA    1 
ATOM   1575 C C     . VAL A 1 197 ? -16.729 16.503 -17.094 1.00 33.24 ? 497 VAL A C     1 
ATOM   1576 O O     . VAL A 1 197 ? -15.884 15.720 -16.709 1.00 36.47 ? 497 VAL A O     1 
ATOM   1577 C CB    . VAL A 1 197 ? -19.061 16.236 -16.189 1.00 33.61 ? 497 VAL A CB    1 
ATOM   1578 C CG1   . VAL A 1 197 ? -19.005 17.683 -15.716 1.00 38.66 ? 497 VAL A CG1   1 
ATOM   1579 C CG2   . VAL A 1 197 ? -20.481 15.861 -16.537 1.00 37.83 ? 497 VAL A CG2   1 
ATOM   1580 O OXT   . VAL A 1 197 ? -16.565 17.741 -17.221 1.00 44.97 ? 497 VAL A OXT   1 
HETATM 1581 N N1    A APR B 2 .   ? -8.110  17.794 -1.453  0.50 13.32 ? 501 APR A N1    1 
HETATM 1582 C C2    A APR B 2 .   ? -8.359  16.530 -1.797  0.50 13.77 ? 501 APR A C2    1 
HETATM 1583 N N3    A APR B 2 .   ? -7.714  15.430 -1.452  0.50 12.78 ? 501 APR A N3    1 
HETATM 1584 C C4    A APR B 2 .   ? -6.617  15.713 -0.723  0.50 13.08 ? 501 APR A C4    1 
HETATM 1585 C C5    A APR B 2 .   ? -6.216  16.951 -0.304  0.50 13.35 ? 501 APR A C5    1 
HETATM 1586 C C6    A APR B 2 .   ? -7.001  18.041 -0.706  0.50 13.07 ? 501 APR A C6    1 
HETATM 1587 N N6    A APR B 2 .   ? -6.706  19.285 -0.361  0.50 12.53 ? 501 APR A N6    1 
HETATM 1588 N N7    A APR B 2 .   ? -5.062  16.868 0.462   0.50 13.57 ? 501 APR A N7    1 
HETATM 1589 C C8    A APR B 2 .   ? -4.787  15.577 0.504   0.50 12.42 ? 501 APR A C8    1 
HETATM 1590 N N9    A APR B 2 .   ? -5.705  14.836 -0.213  0.50 12.85 ? 501 APR A N9    1 
HETATM 1591 C "C1'" A APR B 2 .   ? -5.767  13.389 -0.305  0.50 12.60 ? 501 APR A "C1'" 1 
HETATM 1592 C "C2'" A APR B 2 .   ? -4.531  12.594 0.074   0.50 13.72 ? 501 APR A "C2'" 1 
HETATM 1593 O "O2'" A APR B 2 .   ? -3.535  12.614 -0.928  0.50 14.77 ? 501 APR A "O2'" 1 
HETATM 1594 C "C3'" A APR B 2 .   ? -5.192  11.242 0.334   0.50 12.62 ? 501 APR A "C3'" 1 
HETATM 1595 O "O3'" A APR B 2 .   ? -5.421  10.583 -0.905  0.50 14.47 ? 501 APR A "O3'" 1 
HETATM 1596 O "O4'" A APR B 2 .   ? -6.749  12.988 0.634   0.50 13.46 ? 501 APR A "O4'" 1 
HETATM 1597 C "C4'" A APR B 2 .   ? -6.507  11.611 1.027   0.50 12.20 ? 501 APR A "C4'" 1 
HETATM 1598 C "C5'" A APR B 2 .   ? -6.519  11.481 2.539   0.50 12.68 ? 501 APR A "C5'" 1 
HETATM 1599 O "O5'" A APR B 2 .   ? -5.207  11.822 3.082   0.50 13.67 ? 501 APR A "O5'" 1 
HETATM 1600 P PA    A APR B 2 .   ? -5.019  12.404 4.583   0.50 14.62 ? 501 APR A PA    1 
HETATM 1601 O O1A   A APR B 2 .   ? -5.274  13.875 4.566   0.50 14.32 ? 501 APR A O1A   1 
HETATM 1602 O O2A   A APR B 2 .   ? -3.663  11.972 5.046   0.50 14.85 ? 501 APR A O2A   1 
HETATM 1603 O O3A   A APR B 2 .   ? -6.188  11.708 5.450   0.50 14.04 ? 501 APR A O3A   1 
HETATM 1604 P PB    A APR B 2 .   ? -6.462  10.181 5.837   0.50 14.83 ? 501 APR A PB    1 
HETATM 1605 O O1B   A APR B 2 .   ? -5.607  9.255  5.021   0.50 14.26 ? 501 APR A O1B   1 
HETATM 1606 O O2B   A APR B 2 .   ? -7.946  10.042 5.835   0.50 12.65 ? 501 APR A O2B   1 
HETATM 1607 O O5D   A APR B 2 .   ? -5.880  10.150 7.334   0.50 14.94 ? 501 APR A O5D   1 
HETATM 1608 C C5D   A APR B 2 .   ? -6.384  11.064 8.331   0.50 17.24 ? 501 APR A C5D   1 
HETATM 1609 O O4D   A APR B 2 .   ? -4.339  12.171 8.885   0.50 19.23 ? 501 APR A O4D   1 
HETATM 1610 O O1D   A APR B 2 .   ? -5.665  13.833 9.603   0.50 19.59 ? 501 APR A O1D   1 
HETATM 1611 C C1D   A APR B 2 .   ? -4.443  13.258 9.754   0.50 19.84 ? 501 APR A C1D   1 
HETATM 1612 O O2D   A APR B 2 .   ? -3.420  11.839 11.524  0.50 21.10 ? 501 APR A O2D   1 
HETATM 1613 C C2D   A APR B 2 .   ? -4.537  12.608 11.127  0.50 18.77 ? 501 APR A C2D   1 
HETATM 1614 O O3D   A APR B 2 .   ? -6.102  10.861 11.694  0.50 21.67 ? 501 APR A O3D   1 
HETATM 1615 C C3D   A APR B 2 .   ? -5.788  11.831 10.722  0.50 19.11 ? 501 APR A C3D   1 
HETATM 1616 C C4D   A APR B 2 .   ? -5.325  11.232 9.386   0.50 18.47 ? 501 APR A C4D   1 
HETATM 1617 N N1    B AR6 C 3 .   ? -8.083  17.578 -1.676  0.50 16.82 ? 502 AR6 A N1    1 
HETATM 1618 C C2    B AR6 C 3 .   ? -8.336  16.294 -1.948  0.50 17.54 ? 502 AR6 A C2    1 
HETATM 1619 N N3    B AR6 C 3 .   ? -7.636  15.217 -1.628  0.50 17.85 ? 502 AR6 A N3    1 
HETATM 1620 C C4    B AR6 C 3 .   ? -6.506  15.542 -0.977  0.50 17.71 ? 502 AR6 A C4    1 
HETATM 1621 C C5    B AR6 C 3 .   ? -6.097  16.807 -0.630  0.50 17.01 ? 502 AR6 A C5    1 
HETATM 1622 C C6    B AR6 C 3 .   ? -6.930  17.875 -1.016  0.50 17.31 ? 502 AR6 A C6    1 
HETATM 1623 N N6    B AR6 C 3 .   ? -6.641  19.141 -0.754  0.50 17.02 ? 502 AR6 A N6    1 
HETATM 1624 N N7    B AR6 C 3 .   ? -4.875  16.756 0.032   0.50 17.76 ? 502 AR6 A N7    1 
HETATM 1625 C C8    B AR6 C 3 .   ? -4.598  15.472 0.104   0.50 17.61 ? 502 AR6 A C8    1 
HETATM 1626 N N9    B AR6 C 3 .   ? -5.549  14.689 -0.504  0.50 18.00 ? 502 AR6 A N9    1 
HETATM 1627 P PA    B AR6 C 3 .   ? -5.069  12.331 4.504   0.50 17.99 ? 502 AR6 A PA    1 
HETATM 1628 P PB    B AR6 C 3 .   ? -6.408  10.036 5.868   0.50 18.52 ? 502 AR6 A PB    1 
HETATM 1629 C "C1'" B AR6 C 3 .   ? -5.587  13.225 -0.575  0.50 18.20 ? 502 AR6 A "C1'" 1 
HETATM 1630 O O1A   B AR6 C 3 .   ? -3.727  11.707 4.707   0.50 16.44 ? 502 AR6 A O1A   1 
HETATM 1631 O O1B   B AR6 C 3 .   ? -5.719  8.954  5.100   0.50 17.85 ? 502 AR6 A O1B   1 
HETATM 1632 C C1D   B AR6 C 3 .   ? -3.665  12.732 9.741   0.50 23.53 ? 502 AR6 A C1D   1 
HETATM 1633 O O1D   B AR6 C 3 .   ? -2.576  12.232 10.406  0.50 25.87 ? 502 AR6 A O1D   1 
HETATM 1634 C "C2'" B AR6 C 3 .   ? -4.353  12.495 -0.057  0.50 19.08 ? 502 AR6 A "C2'" 1 
HETATM 1635 O "O2'" B AR6 C 3 .   ? -3.297  12.430 -0.992  0.50 18.99 ? 502 AR6 A "O2'" 1 
HETATM 1636 O O2A   B AR6 C 3 .   ? -5.202  13.739 5.000   0.50 17.02 ? 502 AR6 A O2A   1 
HETATM 1637 O O2B   B AR6 C 3 .   ? -7.864  9.913  6.203   0.50 17.75 ? 502 AR6 A O2B   1 
HETATM 1638 C C2D   B AR6 C 3 .   ? -4.832  12.929 10.707  0.50 23.92 ? 502 AR6 A C2D   1 
HETATM 1639 O O2D   B AR6 C 3 .   ? -4.389  13.453 11.943  0.50 21.00 ? 502 AR6 A O2D   1 
HETATM 1640 C "C3'" B AR6 C 3 .   ? -4.955  11.133 0.302   0.50 19.15 ? 502 AR6 A "C3'" 1 
HETATM 1641 O "O3'" B AR6 C 3 .   ? -5.070  10.242 -0.802  0.50 18.68 ? 502 AR6 A "O3'" 1 
HETATM 1642 O O3A   B AR6 C 3 .   ? -6.263  11.452 5.132   0.50 17.26 ? 502 AR6 A O3A   1 
HETATM 1643 C C3D   B AR6 C 3 .   ? -5.524  11.557 10.745  0.50 23.89 ? 502 AR6 A C3D   1 
HETATM 1644 O O3D   B AR6 C 3 .   ? -5.140  10.687 11.797  0.50 25.81 ? 502 AR6 A O3D   1 
HETATM 1645 C "C4'" B AR6 C 3 .   ? -6.347  11.493 0.831   0.50 18.44 ? 502 AR6 A "C4'" 1 
HETATM 1646 O "O4'" B AR6 C 3 .   ? -6.649  12.794 0.254   0.50 19.19 ? 502 AR6 A "O4'" 1 
HETATM 1647 C C4D   B AR6 C 3 .   ? -5.055  10.898 9.443   0.50 22.31 ? 502 AR6 A C4D   1 
HETATM 1648 O O4D   B AR6 C 3 .   ? -4.148  11.822 8.794   0.50 23.43 ? 502 AR6 A O4D   1 
HETATM 1649 C "C5'" B AR6 C 3 .   ? -6.485  11.528 2.340   0.50 19.04 ? 502 AR6 A "C5'" 1 
HETATM 1650 O "O5'" B AR6 C 3 .   ? -5.383  12.283 2.923   0.50 19.66 ? 502 AR6 A "O5'" 1 
HETATM 1651 C C5D   B AR6 C 3 .   ? -6.152  10.552 8.471   0.50 20.99 ? 502 AR6 A C5D   1 
HETATM 1652 O O5D   B AR6 C 3 .   ? -5.541  10.289 7.193   0.50 19.06 ? 502 AR6 A O5D   1 
HETATM 1653 O O     . HOH D 4 .   ? -18.473 19.649 -4.521  0.50 19.96 ? 601 HOH A O     1 
HETATM 1654 O O     . HOH D 4 .   ? -18.983 29.970 3.434   1.00 39.93 ? 602 HOH A O     1 
HETATM 1655 O O     . HOH D 4 .   ? -13.458 31.385 9.564   1.00 45.77 ? 603 HOH A O     1 
HETATM 1656 O O     . HOH D 4 .   ? -0.230  13.351 -5.107  1.00 36.73 ? 604 HOH A O     1 
HETATM 1657 O O     . HOH D 4 .   ? -16.027 -4.209 -6.526  1.00 34.48 ? 605 HOH A O     1 
HETATM 1658 O O     . HOH D 4 .   ? 1.821   12.574 7.132   1.00 35.49 ? 606 HOH A O     1 
HETATM 1659 O O     . HOH D 4 .   ? -5.975  15.060 7.073   1.00 16.30 ? 607 HOH A O     1 
HETATM 1660 O O     . HOH D 4 .   ? -38.239 12.493 -3.232  1.00 29.98 ? 608 HOH A O     1 
HETATM 1661 O O     . HOH D 4 .   ? -5.663  10.112 14.270  1.00 32.82 ? 609 HOH A O     1 
HETATM 1662 O O     . HOH D 4 .   ? -33.724 -0.955 0.753   1.00 44.44 ? 610 HOH A O     1 
HETATM 1663 O O     . HOH D 4 .   ? -20.395 22.368 15.779  1.00 28.60 ? 611 HOH A O     1 
HETATM 1664 O O     . HOH D 4 .   ? -10.804 33.645 9.301   1.00 34.65 ? 612 HOH A O     1 
HETATM 1665 O O     . HOH D 4 .   ? -8.891  19.068 18.942  1.00 28.40 ? 613 HOH A O     1 
HETATM 1666 O O     . HOH D 4 .   ? 0.859   0.255  4.881   1.00 47.96 ? 614 HOH A O     1 
HETATM 1667 O O     . HOH D 4 .   ? -29.203 9.919  -16.153 1.00 19.06 ? 615 HOH A O     1 
HETATM 1668 O O     . HOH D 4 .   ? -18.080 -2.225 2.287   1.00 26.45 ? 616 HOH A O     1 
HETATM 1669 O O     . HOH D 4 .   ? -3.568  17.270 21.188  1.00 38.25 ? 617 HOH A O     1 
HETATM 1670 O O     . HOH D 4 .   ? -13.477 29.526 0.300   1.00 40.49 ? 618 HOH A O     1 
HETATM 1671 O O     . HOH D 4 .   ? -16.389 25.219 -6.144  1.00 31.85 ? 619 HOH A O     1 
HETATM 1672 O O     . HOH D 4 .   ? -21.574 16.582 15.661  1.00 19.88 ? 620 HOH A O     1 
HETATM 1673 O O     . HOH D 4 .   ? -20.574 28.569 5.089   1.00 27.28 ? 621 HOH A O     1 
HETATM 1674 O O     . HOH D 4 .   ? -6.665  28.088 1.776   1.00 35.07 ? 622 HOH A O     1 
HETATM 1675 O O     . HOH D 4 .   ? -29.834 21.320 7.925   1.00 57.50 ? 623 HOH A O     1 
HETATM 1676 O O     . HOH D 4 .   ? -14.685 14.434 -18.726 1.00 60.35 ? 624 HOH A O     1 
HETATM 1677 O O     . HOH D 4 .   ? -26.528 21.105 -3.708  1.00 47.67 ? 625 HOH A O     1 
HETATM 1678 O O     . HOH D 4 .   ? -12.982 3.857  15.923  1.00 26.01 ? 626 HOH A O     1 
HETATM 1679 O O     . HOH D 4 .   ? -8.952  12.810 -1.960  1.00 14.88 ? 627 HOH A O     1 
HETATM 1680 O O     . HOH D 4 .   ? -0.545  16.379 17.485  1.00 44.07 ? 628 HOH A O     1 
HETATM 1681 O O     . HOH D 4 .   ? -34.295 16.418 0.726   1.00 30.33 ? 629 HOH A O     1 
HETATM 1682 O O     . HOH D 4 .   ? -28.884 5.345  -14.517 1.00 16.75 ? 630 HOH A O     1 
HETATM 1683 O O     . HOH D 4 .   ? -28.065 10.798 11.588  1.00 34.80 ? 631 HOH A O     1 
HETATM 1684 O O     . HOH D 4 .   ? -15.126 25.512 -0.488  1.00 22.52 ? 632 HOH A O     1 
HETATM 1685 O O     . HOH D 4 .   ? -20.980 1.528  -17.751 1.00 39.36 ? 633 HOH A O     1 
HETATM 1686 O O     . HOH D 4 .   ? -28.840 1.990  5.207   1.00 29.18 ? 634 HOH A O     1 
HETATM 1687 O O     . HOH D 4 .   ? -3.511  4.311  0.070   1.00 32.20 ? 635 HOH A O     1 
HETATM 1688 O O     . HOH D 4 .   ? -24.298 0.050  5.364   1.00 33.69 ? 636 HOH A O     1 
HETATM 1689 O O     . HOH D 4 .   ? -19.327 -4.744 -3.264  1.00 36.12 ? 637 HOH A O     1 
HETATM 1690 O O     . HOH D 4 .   ? -5.946  15.961 12.072  1.00 16.95 ? 638 HOH A O     1 
HETATM 1691 O O     . HOH D 4 .   ? -13.117 13.334 -13.261 1.00 31.89 ? 639 HOH A O     1 
HETATM 1692 O O     . HOH D 4 .   ? -27.455 4.242  4.229   1.00 22.78 ? 640 HOH A O     1 
HETATM 1693 O O     . HOH D 4 .   ? -10.237 -4.705 -1.063  1.00 40.13 ? 641 HOH A O     1 
HETATM 1694 O O     . HOH D 4 .   ? -32.543 16.004 -1.309  1.00 19.37 ? 642 HOH A O     1 
HETATM 1695 O O     . HOH D 4 .   ? -1.271  12.075 3.582   1.00 28.49 ? 643 HOH A O     1 
HETATM 1696 O O     . HOH D 4 .   ? -21.087 9.177  19.786  1.00 35.48 ? 644 HOH A O     1 
HETATM 1697 O O     . HOH D 4 .   ? -0.684  11.327 -2.145  1.00 36.20 ? 645 HOH A O     1 
HETATM 1698 O O     . HOH D 4 .   ? -36.781 15.282 -3.892  1.00 39.35 ? 646 HOH A O     1 
HETATM 1699 O O     . HOH D 4 .   ? -29.084 2.071  -18.578 1.00 41.51 ? 647 HOH A O     1 
HETATM 1700 O O     . HOH D 4 .   ? -4.479  0.811  7.011   1.00 36.41 ? 648 HOH A O     1 
HETATM 1701 O O     . HOH D 4 .   ? -23.806 0.887  -17.831 1.00 35.28 ? 649 HOH A O     1 
HETATM 1702 O O     . HOH D 4 .   ? -12.906 8.544  -15.192 1.00 46.89 ? 650 HOH A O     1 
HETATM 1703 O O     . HOH D 4 .   ? -2.494  12.472 14.040  1.00 25.05 ? 651 HOH A O     1 
HETATM 1704 O O     . HOH D 4 .   ? -22.170 4.016  10.967  1.00 20.93 ? 652 HOH A O     1 
HETATM 1705 O O     . HOH D 4 .   ? -0.674  6.103  2.058   1.00 38.00 ? 653 HOH A O     1 
HETATM 1706 O O     . HOH D 4 .   ? -17.807 23.741 24.583  1.00 38.13 ? 654 HOH A O     1 
HETATM 1707 O O     . HOH D 4 .   ? -21.618 13.211 23.813  1.00 37.44 ? 655 HOH A O     1 
HETATM 1708 O O     . HOH D 4 .   ? -30.423 -3.911 -17.489 1.00 29.71 ? 656 HOH A O     1 
HETATM 1709 O O     . HOH D 4 .   ? -23.010 -1.311 2.447   1.00 30.85 ? 657 HOH A O     1 
HETATM 1710 O O     . HOH D 4 .   ? -21.970 1.282  10.226  1.00 23.90 ? 658 HOH A O     1 
HETATM 1711 O O     . HOH D 4 .   ? -30.173 -1.798 5.465   1.00 39.52 ? 659 HOH A O     1 
HETATM 1712 O O     . HOH D 4 .   ? -12.952 26.720 21.175  1.00 24.60 ? 660 HOH A O     1 
HETATM 1713 O O     . HOH D 4 .   ? -10.472 -1.859 -9.650  1.00 38.03 ? 661 HOH A O     1 
HETATM 1714 O O     . HOH D 4 .   ? -23.589 27.118 7.995   1.00 38.13 ? 662 HOH A O     1 
HETATM 1715 O O     . HOH D 4 .   ? -4.848  2.403  -9.700  1.00 27.83 ? 663 HOH A O     1 
HETATM 1716 O O     . HOH D 4 .   ? -11.044 -0.267 -7.681  1.00 27.92 ? 664 HOH A O     1 
HETATM 1717 O O     . HOH D 4 .   ? -2.431  9.507  -1.334  1.00 34.35 ? 665 HOH A O     1 
HETATM 1718 O O     . HOH D 4 .   ? -31.714 6.900  -4.516  1.00 16.57 ? 666 HOH A O     1 
HETATM 1719 O O     . HOH D 4 .   ? 0.466   14.099 7.187   1.00 26.12 ? 667 HOH A O     1 
HETATM 1720 O O     . HOH D 4 .   ? 1.038   6.844  7.809   1.00 36.73 ? 668 HOH A O     1 
HETATM 1721 O O     . HOH D 4 .   ? -25.865 3.347  -20.172 1.00 30.34 ? 669 HOH A O     1 
HETATM 1722 O O     . HOH D 4 .   ? -16.196 29.958 15.957  1.00 30.49 ? 670 HOH A O     1 
HETATM 1723 O O     . HOH D 4 .   ? -16.633 32.508 8.065   1.00 46.08 ? 671 HOH A O     1 
HETATM 1724 O O     . HOH D 4 .   ? -30.885 8.337  -2.424  1.00 16.24 ? 672 HOH A O     1 
HETATM 1725 O O     . HOH D 4 .   ? -7.557  31.265 6.843   1.00 30.61 ? 673 HOH A O     1 
HETATM 1726 O O     . HOH D 4 .   ? -10.704 5.285  21.366  1.00 47.22 ? 674 HOH A O     1 
HETATM 1727 O O     . HOH D 4 .   ? -11.855 20.685 23.033  1.00 27.39 ? 675 HOH A O     1 
HETATM 1728 O O     . HOH D 4 .   ? -3.272  19.045 0.302   1.00 32.01 ? 676 HOH A O     1 
HETATM 1729 O O     . HOH D 4 .   ? 0.325   17.510 7.967   1.00 28.91 ? 677 HOH A O     1 
HETATM 1730 O O     . HOH D 4 .   ? -6.907  11.735 -3.597  1.00 19.12 ? 678 HOH A O     1 
HETATM 1731 O O     . HOH D 4 .   ? -24.772 3.867  3.549   1.00 18.95 ? 679 HOH A O     1 
HETATM 1732 O O     . HOH D 4 .   ? -6.318  25.612 2.106   1.00 35.06 ? 680 HOH A O     1 
HETATM 1733 O O     . HOH D 4 .   ? -22.325 13.695 15.364  1.00 39.62 ? 681 HOH A O     1 
HETATM 1734 O O     . HOH D 4 .   ? -3.682  -7.142 -2.273  1.00 33.89 ? 682 HOH A O     1 
HETATM 1735 O O     . HOH D 4 .   ? -25.074 24.947 0.192   1.00 32.50 ? 683 HOH A O     1 
HETATM 1736 O O     . HOH D 4 .   ? -9.518  9.494  21.773  1.00 41.32 ? 684 HOH A O     1 
HETATM 1737 O O     . HOH D 4 .   ? -30.540 9.479  9.582   1.00 35.36 ? 685 HOH A O     1 
HETATM 1738 O O     . HOH D 4 .   ? -35.106 1.056  -3.205  1.00 27.07 ? 686 HOH A O     1 
HETATM 1739 O O     . HOH D 4 .   ? -8.976  20.517 9.892   1.00 15.09 ? 687 HOH A O     1 
HETATM 1740 O O     . HOH D 4 .   ? -16.338 15.534 25.474  1.00 34.94 ? 688 HOH A O     1 
HETATM 1741 O O     . HOH D 4 .   ? -16.779 19.830 -8.379  1.00 30.78 ? 689 HOH A O     1 
HETATM 1742 O O     . HOH D 4 .   ? -20.820 12.082 20.268  1.00 30.99 ? 690 HOH A O     1 
HETATM 1743 O O     . HOH D 4 .   ? -35.286 11.910 3.220   1.00 34.24 ? 691 HOH A O     1 
HETATM 1744 O O     . HOH D 4 .   ? -36.029 13.090 -8.466  1.00 34.89 ? 692 HOH A O     1 
HETATM 1745 O O     . HOH D 4 .   ? 0.480   21.729 14.139  1.00 31.54 ? 693 HOH A O     1 
HETATM 1746 O O     . HOH D 4 .   ? -11.803 6.376  14.914  1.00 17.87 ? 694 HOH A O     1 
HETATM 1747 O O     . HOH D 4 .   ? -22.494 -2.927 -6.103  1.00 28.62 ? 695 HOH A O     1 
HETATM 1748 O O     . HOH D 4 .   ? -14.830 10.595 -18.225 1.00 54.09 ? 696 HOH A O     1 
HETATM 1749 O O     . HOH D 4 .   ? -6.090  28.092 17.696  1.00 44.27 ? 697 HOH A O     1 
HETATM 1750 O O     . HOH D 4 .   ? -8.275  2.148  27.714  1.00 23.51 ? 698 HOH A O     1 
HETATM 1751 O O     . HOH D 4 .   ? -21.674 19.503 -5.326  1.00 22.97 ? 699 HOH A O     1 
HETATM 1752 O O     . HOH D 4 .   ? -22.709 19.621 15.799  1.00 29.62 ? 700 HOH A O     1 
HETATM 1753 O O     . HOH D 4 .   ? -12.446 16.252 -12.629 1.00 32.94 ? 701 HOH A O     1 
HETATM 1754 O O     . HOH D 4 .   ? -17.213 -1.686 9.552   1.00 21.70 ? 702 HOH A O     1 
HETATM 1755 O O     . HOH D 4 .   ? -9.317  3.219  -14.290 1.00 33.98 ? 703 HOH A O     1 
HETATM 1756 O O     . HOH D 4 .   ? -3.168  1.559  -2.483  1.00 31.92 ? 704 HOH A O     1 
HETATM 1757 O O     . HOH D 4 .   ? -1.155  11.921 0.914   1.00 34.54 ? 705 HOH A O     1 
HETATM 1758 O O     . HOH D 4 .   ? -21.331 17.157 -3.969  1.00 19.62 ? 706 HOH A O     1 
HETATM 1759 O O     . HOH D 4 .   ? -23.505 4.464  -19.430 1.00 21.86 ? 707 HOH A O     1 
HETATM 1760 O O     . HOH D 4 .   ? -15.614 5.077  -14.803 1.00 32.15 ? 708 HOH A O     1 
HETATM 1761 O O     . HOH D 4 .   ? 1.502   18.473 11.144  1.00 28.50 ? 709 HOH A O     1 
HETATM 1762 O O     . HOH D 4 .   ? -30.266 7.410  -15.735 1.00 18.20 ? 710 HOH A O     1 
HETATM 1763 O O     . HOH D 4 .   ? -31.571 4.192  -19.582 1.00 30.12 ? 711 HOH A O     1 
HETATM 1764 O O     . HOH D 4 .   ? -5.936  -1.274 9.829   1.00 29.95 ? 712 HOH A O     1 
HETATM 1765 O O     . HOH D 4 .   ? -29.244 21.258 2.478   1.00 28.66 ? 713 HOH A O     1 
HETATM 1766 O O     . HOH D 4 .   ? -6.023  12.347 -9.900  1.00 25.99 ? 714 HOH A O     1 
HETATM 1767 O O     . HOH D 4 .   ? -8.562  32.399 9.449   1.00 25.86 ? 715 HOH A O     1 
HETATM 1768 O O     . HOH D 4 .   ? -0.707  8.364  -8.263  1.00 31.66 ? 716 HOH A O     1 
HETATM 1769 O O     . HOH D 4 .   ? -31.568 3.675  -11.375 1.00 26.80 ? 717 HOH A O     1 
HETATM 1770 O O     . HOH D 4 .   ? -5.927  -1.546 3.284   1.00 26.63 ? 718 HOH A O     1 
HETATM 1771 O O     . HOH D 4 .   ? -7.403  20.499 17.198  1.00 25.22 ? 719 HOH A O     1 
HETATM 1772 O O     . HOH D 4 .   ? -24.556 0.610  11.145  1.00 42.74 ? 720 HOH A O     1 
HETATM 1773 O O     . HOH D 4 .   ? -36.573 7.073  1.111   1.00 28.47 ? 721 HOH A O     1 
HETATM 1774 O O     . HOH D 4 .   ? -29.528 -2.478 2.531   1.00 37.04 ? 722 HOH A O     1 
HETATM 1775 O O     . HOH D 4 .   ? -20.955 28.704 7.967   1.00 37.30 ? 723 HOH A O     1 
HETATM 1776 O O     . HOH D 4 .   ? -35.056 14.746 -2.066  1.00 22.69 ? 724 HOH A O     1 
HETATM 1777 O O     . HOH D 4 .   ? -17.650 22.201 -6.628  1.00 30.99 ? 725 HOH A O     1 
HETATM 1778 O O     . HOH D 4 .   ? -33.221 21.554 5.382   1.00 32.44 ? 726 HOH A O     1 
HETATM 1779 O O     . HOH D 4 .   ? -10.551 21.986 -7.192  1.00 29.64 ? 727 HOH A O     1 
HETATM 1780 O O     . HOH D 4 .   ? -22.842 25.418 -1.206  1.00 28.43 ? 728 HOH A O     1 
HETATM 1781 O O     . HOH D 4 .   ? -10.169 31.515 5.367   1.00 45.40 ? 729 HOH A O     1 
HETATM 1782 O O     . HOH D 4 .   ? -1.088  7.478  -0.395  1.00 52.46 ? 730 HOH A O     1 
HETATM 1783 O O     . HOH D 4 .   ? 1.253   12.924 -10.013 1.00 29.59 ? 731 HOH A O     1 
HETATM 1784 O O     . HOH D 4 .   ? -13.470 -1.681 -14.229 1.00 31.59 ? 732 HOH A O     1 
HETATM 1785 O O     . HOH D 4 .   ? -35.189 8.321  3.815   1.00 36.23 ? 733 HOH A O     1 
HETATM 1786 O O     . HOH D 4 .   ? -26.851 0.156  6.105   1.00 30.60 ? 734 HOH A O     1 
HETATM 1787 O O     . HOH D 4 .   ? -36.087 17.644 -8.249  1.00 27.08 ? 735 HOH A O     1 
HETATM 1788 O O     . HOH D 4 .   ? -8.973  28.192 17.628  1.00 38.54 ? 736 HOH A O     1 
HETATM 1789 O O     . HOH D 4 .   ? -6.258  6.306  15.335  1.00 44.39 ? 737 HOH A O     1 
HETATM 1790 O O     . HOH D 4 .   ? -33.507 0.152  -5.406  1.00 26.26 ? 738 HOH A O     1 
HETATM 1791 O O     . HOH D 4 .   ? -20.436 22.253 -7.288  1.00 39.80 ? 739 HOH A O     1 
HETATM 1792 O O     . HOH D 4 .   ? -14.727 -2.638 5.900   1.00 31.53 ? 740 HOH A O     1 
HETATM 1793 O O     . HOH D 4 .   ? -7.964  5.338  13.732  1.00 35.06 ? 741 HOH A O     1 
HETATM 1794 O O     . HOH D 4 .   ? -0.063  22.150 11.578  1.00 34.28 ? 742 HOH A O     1 
HETATM 1795 O O     . HOH D 4 .   ? -2.623  8.063  -6.144  1.00 27.69 ? 743 HOH A O     1 
HETATM 1796 O O     . HOH D 4 .   ? -19.602 32.256 4.647   1.00 50.05 ? 744 HOH A O     1 
HETATM 1797 O O     . HOH D 4 .   ? -27.209 -2.682 2.140   1.00 49.72 ? 745 HOH A O     1 
HETATM 1798 O O     . HOH D 4 .   ? -10.811 -4.903 8.190   1.00 35.96 ? 746 HOH A O     1 
HETATM 1799 O O     . HOH D 4 .   ? -24.656 -1.889 -1.630  1.00 44.48 ? 747 HOH A O     1 
HETATM 1800 O O     . HOH D 4 .   ? -6.207  12.061 -15.548 1.00 40.33 ? 748 HOH A O     1 
HETATM 1801 O O     . HOH D 4 .   ? -15.744 -2.569 -15.576 1.00 35.21 ? 749 HOH A O     1 
HETATM 1802 O O     . HOH D 4 .   ? -11.050 8.395  22.428  1.00 39.78 ? 750 HOH A O     1 
HETATM 1803 O O     . HOH D 4 .   ? -9.396  19.333 21.947  1.00 33.52 ? 751 HOH A O     1 
HETATM 1804 O O     . HOH D 4 .   ? -26.437 19.201 -6.403  1.00 33.71 ? 752 HOH A O     1 
HETATM 1805 O O     . HOH D 4 .   ? -9.659  1.016  20.340  1.00 38.85 ? 753 HOH A O     1 
HETATM 1806 O O     . HOH D 4 .   ? -1.586  -0.191 6.120   1.00 55.93 ? 754 HOH A O     1 
HETATM 1807 O O     . HOH D 4 .   ? -21.617 0.155  7.484   1.00 35.90 ? 755 HOH A O     1 
HETATM 1808 O O     . HOH D 4 .   ? -14.760 4.738  -17.610 1.00 48.57 ? 756 HOH A O     1 
HETATM 1809 O O     . HOH D 4 .   ? -7.105  8.994  20.714  1.00 38.50 ? 757 HOH A O     1 
HETATM 1810 O O     . HOH D 4 .   ? -20.001 -1.755 8.851   1.00 30.55 ? 758 HOH A O     1 
HETATM 1811 O O     . HOH D 4 .   ? -37.565 17.980 -4.919  1.00 27.81 ? 759 HOH A O     1 
HETATM 1812 O O     . HOH D 4 .   ? -2.480  3.290  10.003  1.00 67.37 ? 760 HOH A O     1 
HETATM 1813 O O     . HOH D 4 .   ? -16.764 -3.772 11.275  1.00 26.66 ? 761 HOH A O     1 
HETATM 1814 O O     . HOH D 4 .   ? -10.453 27.954 20.618  1.00 43.31 ? 762 HOH A O     1 
HETATM 1815 O O     . HOH D 4 .   ? -36.028 14.267 0.563   1.00 37.85 ? 763 HOH A O     1 
HETATM 1816 O O     . HOH D 4 .   ? -20.330 -4.879 -6.165  1.00 37.96 ? 764 HOH A O     1 
HETATM 1817 O O     . HOH D 4 .   ? -6.792  0.833  -10.863 1.00 39.02 ? 765 HOH A O     1 
HETATM 1818 O O     . HOH D 4 .   ? -18.461 -4.642 -8.506  1.00 34.89 ? 766 HOH A O     1 
HETATM 1819 O O     . HOH D 4 .   ? -33.280 5.606  -17.338 1.00 39.55 ? 767 HOH A O     1 
HETATM 1820 O O     . HOH D 4 .   ? -22.434 -3.537 1.547   1.00 57.26 ? 768 HOH A O     1 
HETATM 1821 O O     . HOH D 4 .   ? -29.618 13.474 -12.608 1.00 45.04 ? 769 HOH A O     1 
HETATM 1822 O O     . HOH D 4 .   ? -6.345  4.425  20.433  1.00 39.90 ? 770 HOH A O     1 
HETATM 1823 O O     . HOH D 4 .   ? -24.767 4.980  10.669  1.00 27.48 ? 771 HOH A O     1 
HETATM 1824 O O     . HOH D 4 .   ? -23.518 11.336 26.098  1.00 36.87 ? 772 HOH A O     1 
HETATM 1825 O O     . HOH D 4 .   ? -1.079  16.317 -0.563  1.00 47.77 ? 773 HOH A O     1 
HETATM 1826 O O     . HOH D 4 .   ? 1.634   16.504 9.318   1.00 31.68 ? 774 HOH A O     1 
HETATM 1827 O O     . HOH D 4 .   ? -29.890 -5.863 -18.571 1.00 35.78 ? 775 HOH A O     1 
HETATM 1828 O O     . HOH D 4 .   ? -24.119 20.085 -6.257  1.00 38.06 ? 776 HOH A O     1 
HETATM 1829 O O     . HOH D 4 .   ? -30.665 3.294  -14.046 1.00 26.31 ? 777 HOH A O     1 
HETATM 1830 O O     . HOH D 4 .   ? -11.093 23.054 24.048  1.00 45.07 ? 778 HOH A O     1 
HETATM 1831 O O     . HOH D 4 .   ? -5.993  -0.824 5.826   1.00 28.42 ? 779 HOH A O     1 
HETATM 1832 O O     . HOH D 4 .   ? -40.095 13.015 -1.148  1.00 33.49 ? 780 HOH A O     1 
HETATM 1833 O O     . HOH D 4 .   ? -12.309 0.022  -16.095 1.00 41.91 ? 781 HOH A O     1 
HETATM 1834 O O     . HOH D 4 .   ? -5.736  14.428 -16.623 1.00 39.53 ? 782 HOH A O     1 
HETATM 1835 O O     . HOH D 4 .   ? -21.798 -5.526 -5.334  1.00 35.07 ? 783 HOH A O     1 
HETATM 1836 O O     . HOH D 4 .   ? -27.608 -2.499 5.617   1.00 39.42 ? 784 HOH A O     1 
HETATM 1837 O O     . HOH D 4 .   ? -38.602 13.202 -7.079  1.00 46.71 ? 785 HOH A O     1 
HETATM 1838 O O     . HOH D 4 .   ? -12.047 1.929  21.173  1.00 41.27 ? 786 HOH A O     1 
HETATM 1839 O O     . HOH D 4 .   ? -31.844 1.778  -18.489 1.00 36.48 ? 787 HOH A O     1 
HETATM 1840 O O     . HOH D 4 .   ? -12.740 -4.616 6.332   1.00 46.94 ? 788 HOH A O     1 
HETATM 1841 O O     . HOH D 4 .   ? -0.584  3.792  1.098   1.00 49.59 ? 789 HOH A O     1 
HETATM 1842 O O     . HOH D 4 .   ? -30.246 11.980 -14.619 1.00 26.27 ? 790 HOH A O     1 
HETATM 1843 O O     . HOH D 4 .   ? -16.056 -3.615 3.661   1.00 34.96 ? 791 HOH A O     1 
HETATM 1844 O O     . HOH D 4 .   ? -42.503 11.644 -1.793  1.00 32.62 ? 792 HOH A O     1 
HETATM 1845 O O     . HOH D 4 .   ? -23.929 8.482  19.273  1.00 38.56 ? 793 HOH A O     1 
HETATM 1846 O O     . HOH D 4 .   ? 3.196   12.275 4.002   1.00 33.61 ? 794 HOH A O     1 
HETATM 1847 O O     . HOH D 4 .   ? -5.919  -2.914 7.483   1.00 39.39 ? 795 HOH A O     1 
HETATM 1848 O O     . HOH D 4 .   ? -16.168 -3.862 7.836   1.00 33.91 ? 796 HOH A O     1 
HETATM 1849 O O     . HOH D 4 .   ? -25.653 6.970  12.213  1.00 38.46 ? 797 HOH A O     1 
HETATM 1850 O O     . HOH D 4 .   ? -39.311 7.336  1.813   1.00 34.22 ? 798 HOH A O     1 
HETATM 1851 O O     . HOH D 4 .   ? -6.350  33.621 10.605  1.00 25.10 ? 799 HOH A O     1 
HETATM 1852 O O     . HOH D 4 .   ? 2.278   16.301 6.766   1.00 33.30 ? 800 HOH A O     1 
HETATM 1853 O O     . HOH D 4 .   ? 2.162   13.964 10.629  1.00 34.90 ? 801 HOH A O     1 
HETATM 1854 O O     . HOH D 4 .   ? -37.856 1.131  -3.516  1.00 32.28 ? 802 HOH A O     1 
HETATM 1855 O O     . HOH D 4 .   ? -16.273 -7.670 -11.186 1.00 39.44 ? 803 HOH A O     1 
HETATM 1856 O O     . HOH D 4 .   ? -5.435  32.736 13.012  1.00 22.10 ? 804 HOH A O     1 
HETATM 1857 O O     . HOH D 4 .   ? -27.476 28.087 6.170   1.00 49.55 ? 805 HOH A O     1 
HETATM 1858 O O     . HOH D 4 .   ? -22.407 18.435 -16.836 1.00 38.16 ? 806 HOH A O     1 
HETATM 1859 O O     . HOH D 4 .   ? -7.839  23.420 23.129  1.00 37.69 ? 807 HOH A O     1 
HETATM 1860 O O     . HOH D 4 .   ? -38.093 7.422  8.290   1.00 38.94 ? 808 HOH A O     1 
HETATM 1861 O O     . HOH D 4 .   ? -9.002  24.669 29.437  1.00 36.86 ? 809 HOH A O     1 
HETATM 1862 O O     . HOH D 4 .   ? -5.023  29.443 25.734  1.00 42.34 ? 810 HOH A O     1 
HETATM 1863 O O     . HOH D 4 .   ? -4.624  34.016 24.500  1.00 40.58 ? 811 HOH A 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     . SER A 8   ? 0.4372 0.8776 0.5249 0.0928  0.0771  -0.1021 308 SER A N     
2    C CA    . SER A 8   ? 0.3051 0.8356 0.5112 0.0942  0.0759  -0.0960 308 SER A CA    
3    C C     . SER A 8   ? 0.3387 0.6938 0.4594 0.0857  0.0604  -0.0498 308 SER A C     
4    O O     . SER A 8   ? 0.5354 0.7621 0.5574 0.1087  -0.0416 -0.0202 308 SER A O     
5    C CB    . SER A 8   ? 0.3517 0.8945 0.5940 0.0648  0.0685  -0.0989 308 SER A CB    
6    O OG    . SER A 8   ? 0.3855 1.0315 0.6367 0.0259  0.0085  -0.0773 308 SER A OG    
7    N N     . PHE A 9   ? 0.2159 0.4307 0.3868 0.0511  0.0195  -0.0713 309 PHE A N     
8    C CA    . PHE A 9   ? 0.1763 0.2863 0.3574 0.0152  0.0069  -0.0521 309 PHE A CA    
9    C C     . PHE A 9   ? 0.1802 0.2498 0.3593 -0.0035 -0.0025 -0.0314 309 PHE A C     
10   O O     . PHE A 9   ? 0.1843 0.3592 0.4064 0.0399  -0.0299 -0.0494 309 PHE A O     
11   C CB    . PHE A 9   ? 0.2406 0.3382 0.4301 -0.0225 -0.0014 -0.0463 309 PHE A CB    
12   C CG    . PHE A 9   ? 0.2769 0.3415 0.4769 0.0062  -0.0184 0.0005  309 PHE A CG    
13   C CD1   . PHE A 9   ? 0.3838 0.3931 0.5065 -0.0469 -0.0496 0.0144  309 PHE A CD1   
14   C CD2   . PHE A 9   ? 0.3926 0.3492 0.4885 0.0068  -0.0081 -0.0150 309 PHE A CD2   
15   C CE1   . PHE A 9   ? 0.4285 0.3258 0.5204 -0.0609 -0.0417 -0.0094 309 PHE A CE1   
16   C CE2   . PHE A 9   ? 0.4837 0.3763 0.5286 -0.0037 -0.0117 -0.0168 309 PHE A CE2   
17   C CZ    . PHE A 9   ? 0.4813 0.3409 0.5300 0.0000  -0.0081 0.0308  309 PHE A CZ    
18   N N     . ASN A 10  ? 0.1179 0.2566 0.3191 -0.0120 -0.0079 -0.0302 310 ASN A N     
19   C CA    . ASN A 10  ? 0.1123 0.2396 0.3114 -0.0205 -0.0044 -0.0130 310 ASN A CA    
20   C C     . ASN A 10  ? 0.1143 0.2215 0.2919 -0.0205 -0.0073 -0.0205 310 ASN A C     
21   O O     . ASN A 10  ? 0.1175 0.2926 0.2993 -0.0272 -0.0114 -0.0519 310 ASN A O     
22   C CB    . ASN A 10  ? 0.1232 0.2671 0.3365 -0.0457 -0.0103 -0.0233 310 ASN A CB    
23   C CG    . ASN A 10  ? 0.1877 0.2646 0.3931 -0.0485 -0.0323 -0.0131 310 ASN A CG    
24   O OD1   . ASN A 10  ? 0.2285 0.2655 0.3677 -0.0776 -0.0217 0.0299  310 ASN A OD1   
25   N ND2   . ASN A 10  ? 0.2655 0.3434 0.4924 -0.0842 -0.0419 -0.0025 310 ASN A ND2   
26   N N     . ALA A 11  ? 0.1138 0.1435 0.2851 -0.0303 -0.0027 -0.0155 311 ALA A N     
27   C CA    . ALA A 11  ? 0.0934 0.1464 0.3036 -0.0179 0.0065  0.0051  311 ALA A CA    
28   C C     . ALA A 11  ? 0.0985 0.1563 0.2966 -0.0084 0.0014  -0.0117 311 ALA A C     
29   O O     . ALA A 11  ? 0.1104 0.2000 0.3006 -0.0218 0.0017  -0.0147 311 ALA A O     
30   C CB    . ALA A 11  ? 0.1115 0.1618 0.3316 -0.0079 0.0008  -0.0060 311 ALA A CB    
31   N N     . MET A 12  ? 0.1181 0.1746 0.2962 -0.0299 0.0071  -0.0241 312 MET A N     
32   C CA    . MET A 12  ? 0.1164 0.1732 0.3137 -0.0247 -0.0006 -0.0125 312 MET A CA    
33   C C     . MET A 12  ? 0.1135 0.1726 0.2947 -0.0385 -0.0001 -0.0215 312 MET A C     
34   O O     . MET A 12  ? 0.1013 0.1843 0.3156 -0.0232 -0.0075 -0.0279 312 MET A O     
35   C CB    . MET A 12  ? 0.1079 0.1530 0.3514 -0.0052 0.0049  -0.0275 312 MET A CB    
36   C CG    . MET A 12  ? 0.1620 0.1545 0.3735 0.0124  -0.0103 -0.0309 312 MET A CG    
37   S SD    . MET A 12  ? 0.1830 0.2143 0.4006 -0.0109 -0.0028 0.0314  312 MET A SD    
38   C CE    . MET A 12  ? 0.2581 0.2373 0.4175 -0.0305 0.0054  0.0288  312 MET A CE    
39   N N     . VAL A 13  ? 0.1046 0.1279 0.2919 -0.0218 -0.0086 -0.0029 313 VAL A N     
40   C CA    . VAL A 13  ? 0.1194 0.1571 0.2881 -0.0286 0.0015  0.0014  313 VAL A CA    
41   C C     . VAL A 13  ? 0.1178 0.1465 0.2785 -0.0106 -0.0102 -0.0068 313 VAL A C     
42   O O     . VAL A 13  ? 0.1150 0.1276 0.3006 -0.0190 0.0019  -0.0137 313 VAL A O     
43   C CB    . VAL A 13  ? 0.1326 0.1597 0.2958 -0.0195 -0.0072 0.0027  313 VAL A CB    
44   C CG1   . VAL A 13  ? 0.1269 0.1823 0.3184 -0.0102 -0.0095 0.0018  313 VAL A CG1   
45   C CG2   . VAL A 13  ? 0.1403 0.1625 0.3158 0.0116  -0.0138 0.0187  313 VAL A CG2   
46   N N     . VAL A 14  ? 0.1136 0.1328 0.2928 -0.0213 0.0046  -0.0056 314 VAL A N     
47   C CA    . VAL A 14  ? 0.1229 0.1366 0.2976 -0.0130 0.0078  0.0159  314 VAL A CA    
48   C C     . VAL A 14  ? 0.0934 0.1640 0.2853 -0.0106 0.0057  0.0213  314 VAL A C     
49   O O     . VAL A 14  ? 0.1140 0.1350 0.2937 -0.0048 -0.0028 0.0041  314 VAL A O     
50   C CB    . VAL A 14  ? 0.1397 0.1263 0.3352 0.0130  0.0182  0.0165  314 VAL A CB    
51   C CG1   . VAL A 14  ? 0.1177 0.1782 0.3462 0.0290  0.0284  0.0194  314 VAL A CG1   
52   C CG2   . VAL A 14  ? 0.1424 0.1338 0.3473 0.0279  0.0013  0.0334  314 VAL A CG2   
53   N N     . ASN A 15  ? 0.1082 0.1826 0.3098 -0.0183 -0.0049 0.0063  315 ASN A N     
54   C CA    . ASN A 15  ? 0.1098 0.1674 0.3041 -0.0097 -0.0034 -0.0092 315 ASN A CA    
55   C C     . ASN A 15  ? 0.0958 0.1768 0.2769 0.0091  -0.0061 0.0071  315 ASN A C     
56   O O     . ASN A 15  ? 0.1736 0.2140 0.2853 0.0266  -0.0063 0.0058  315 ASN A O     
57   C CB    . ASN A 15  ? 0.1069 0.1588 0.3243 -0.0263 0.0060  -0.0081 315 ASN A CB    
58   C CG    . ASN A 15  ? 0.1955 0.1718 0.3436 -0.0407 0.0017  -0.0037 315 ASN A CG    
59   O OD1   . ASN A 15  ? 0.3393 0.1362 0.3783 -0.0702 0.0329  -0.0158 315 ASN A OD1   
60   N ND2   . ASN A 15  ? 0.1949 0.1432 0.3839 -0.0098 -0.0068 -0.0201 315 ASN A ND2   
61   N N     . ASN A 16  ? 0.1025 0.1469 0.2687 0.0009  0.0003  0.0157  316 ASN A N     
62   C CA    . ASN A 16  ? 0.1120 0.1435 0.2788 0.0164  0.0013  0.0093  316 ASN A CA    
63   C C     . ASN A 16  ? 0.1357 0.1401 0.2877 0.0041  0.0063  0.0065  316 ASN A C     
64   O O     . ASN A 16  ? 0.1260 0.1845 0.3195 0.0150  -0.0047 -0.0226 316 ASN A O     
65   C CB    . ASN A 16  ? 0.1418 0.1433 0.3064 0.0331  0.0054  0.0169  316 ASN A CB    
66   C CG    . ASN A 16  ? 0.1238 0.2093 0.2811 0.0306  0.0087  -0.0005 316 ASN A CG    
67   O OD1   . ASN A 16  ? 0.1343 0.2000 0.2905 0.0381  0.0115  -0.0051 316 ASN A OD1   
68   N ND2   . ASN A 16  ? 0.1438 0.3230 0.3502 0.0471  0.0176  0.0259  316 ASN A ND2   
69   N N     . LEU A 17  ? 0.1385 0.0900 0.2921 -0.0138 -0.0015 -0.0116 317 LEU A N     
70   C CA    . LEU A 17  ? 0.1229 0.0860 0.3153 0.0021  -0.0015 -0.0046 317 LEU A CA    
71   C C     . LEU A 17  ? 0.1146 0.1020 0.3087 0.0046  -0.0093 0.0001  317 LEU A C     
72   O O     . LEU A 17  ? 0.1244 0.1053 0.3210 -0.0188 0.0095  -0.0035 317 LEU A O     
73   C CB    . LEU A 17  ? 0.1092 0.1075 0.3144 -0.0054 0.0071  0.0013  317 LEU A CB    
74   C CG    . LEU A 17  ? 0.1117 0.1324 0.3223 -0.0004 -0.0014 0.0053  317 LEU A CG    
75   C CD1   . LEU A 17  ? 0.1084 0.1296 0.3243 -0.0060 0.0002  -0.0072 317 LEU A CD1   
76   C CD2   . LEU A 17  ? 0.1195 0.1215 0.3454 0.0498  -0.0107 0.0143  317 LEU A CD2   
77   N N     . THR A 18  ? 0.1124 0.0802 0.2973 0.0054  0.0068  -0.0112 318 THR A N     
78   C CA    . THR A 18  ? 0.0948 0.1286 0.2876 0.0106  -0.0064 -0.0128 318 THR A CA    
79   C C     . THR A 18  ? 0.0957 0.1534 0.2932 -0.0044 -0.0017 -0.0130 318 THR A C     
80   O O     . THR A 18  ? 0.1158 0.1894 0.3054 0.0010  0.0099  -0.0344 318 THR A O     
81   C CB    . THR A 18  ? 0.1290 0.1525 0.3083 -0.0056 -0.0093 0.0175  318 THR A CB    
82   O OG1   . THR A 18  ? 0.1320 0.1780 0.3484 -0.0120 -0.0307 0.0107  318 THR A OG1   
83   C CG2   . THR A 18  ? 0.1504 0.1773 0.3203 -0.0163 -0.0032 0.0146  318 THR A CG2   
84   N N     . LEU A 19  ? 0.1117 0.1618 0.2867 -0.0003 -0.0075 -0.0305 319 LEU A N     
85   C CA    . LEU A 19  ? 0.1169 0.1941 0.2901 0.0086  -0.0051 -0.0315 319 LEU A CA    
86   C C     . LEU A 19  ? 0.1158 0.2079 0.2809 -0.0109 -0.0123 -0.0366 319 LEU A C     
87   O O     . LEU A 19  ? 0.1220 0.2172 0.2908 -0.0170 -0.0089 -0.0300 319 LEU A O     
88   C CB    . LEU A 19  ? 0.1457 0.1840 0.2949 0.0265  -0.0117 -0.0403 319 LEU A CB    
89   C CG    . LEU A 19  ? 0.1565 0.1755 0.3353 0.0256  -0.0154 -0.0215 319 LEU A CG    
90   C CD1   . LEU A 19  ? 0.1500 0.2251 0.3190 0.0397  -0.0152 -0.0055 319 LEU A CD1   
91   C CD2   . LEU A 19  ? 0.1766 0.1714 0.3663 0.0202  -0.0153 -0.0287 319 LEU A CD2   
92   N N     . GLN A 20  ? 0.1229 0.1766 0.2711 -0.0102 -0.0066 -0.0371 320 GLN A N     
93   C CA    . GLN A 20  ? 0.1248 0.1700 0.2906 -0.0229 -0.0086 -0.0345 320 GLN A CA    
94   C C     . GLN A 20  ? 0.1203 0.1955 0.2885 -0.0411 0.0032  -0.0155 320 GLN A C     
95   O O     . GLN A 20  ? 0.0966 0.2598 0.2898 -0.0113 -0.0021 -0.0284 320 GLN A O     
96   C CB    . GLN A 20  ? 0.1573 0.2021 0.3618 -0.0246 -0.0036 -0.0395 320 GLN A CB    
97   C CG    . GLN A 20  ? 0.2109 0.2756 0.4581 -0.0048 -0.0012 -0.0438 320 GLN A CG    
98   C CD    . GLN A 20  ? 0.3163 0.2667 0.5393 -0.0025 -0.0445 -0.0139 320 GLN A CD    
99   O OE1   . GLN A 20  ? 0.5177 0.2910 0.4851 -0.0156 0.0048  0.0531  320 GLN A OE1   
100  N NE2   . GLN A 20  ? 0.4166 0.3110 0.6226 0.0349  -0.0151 -0.0399 320 GLN A NE2   
101  N N     . ILE A 21  ? 0.1018 0.1868 0.2831 -0.0436 -0.0090 -0.0112 321 ILE A N     
102  C CA    . ILE A 21  ? 0.1005 0.2077 0.2865 0.0019  -0.0146 0.0112  321 ILE A CA    
103  C C     . ILE A 21  ? 0.1231 0.2288 0.2764 -0.0066 -0.0030 0.0070  321 ILE A C     
104  O O     . ILE A 21  ? 0.1511 0.2585 0.2921 -0.0461 0.0072  0.0118  321 ILE A O     
105  C CB    . ILE A 21  ? 0.1096 0.2241 0.3300 0.0242  0.0071  0.0060  321 ILE A CB    
106  C CG1   . ILE A 21  ? 0.1430 0.2553 0.3777 0.0326  0.0010  -0.0052 321 ILE A CG1   
107  C CG2   . ILE A 21  ? 0.1367 0.2896 0.4098 0.0226  -0.0014 0.0010  321 ILE A CG2   
108  C CD1   . ILE A 21  ? 0.1884 0.2228 0.4157 0.0283  -0.0269 -0.0006 321 ILE A CD1   
109  N N     . VAL A 22  ? 0.1461 0.1913 0.3124 -0.0135 -0.0241 0.0217  322 VAL A N     
110  C CA    . VAL A 22  ? 0.1624 0.1834 0.3488 -0.0172 -0.0304 0.0540  322 VAL A CA    
111  C C     . VAL A 22  ? 0.1638 0.2279 0.3156 -0.0548 -0.0125 0.0319  322 VAL A C     
112  O O     . VAL A 22  ? 0.1267 0.3452 0.3216 -0.0753 -0.0299 0.0385  322 VAL A O     
113  C CB    . VAL A 22  ? 0.2170 0.1831 0.4604 0.0171  -0.0202 0.0630  322 VAL A CB    
114  C CG1   . VAL A 22  ? 0.3091 0.2267 0.4709 0.0071  0.0087  0.0373  322 VAL A CG1   
115  C CG2   . VAL A 22  ? 0.2437 0.1900 0.5533 -0.0029 -0.0206 0.0387  322 VAL A CG2   
116  N N     . GLN A 23  ? 0.1641 0.2435 0.3049 -0.0597 0.0022  0.0263  323 GLN A N     
117  C CA    . GLN A 23  ? 0.1966 0.2444 0.3209 -0.0785 -0.0128 0.0062  323 GLN A CA    
118  C C     . GLN A 23  ? 0.1981 0.2163 0.3196 -0.0840 -0.0055 0.0232  323 GLN A C     
119  O O     . GLN A 23  ? 0.2703 0.2716 0.3480 -0.0743 -0.0391 0.0364  323 GLN A O     
120  C CB    . GLN A 23  ? 0.1925 0.2997 0.3368 -0.0581 -0.0001 0.0333  323 GLN A CB    
121  C CG    . GLN A 23  ? 0.1898 0.3235 0.3812 -0.0581 0.0152  0.0269  323 GLN A CG    
122  C CD    . GLN A 23  ? 0.2552 0.3825 0.4048 -0.0380 0.0405  0.0497  323 GLN A CD    
123  O OE1   . GLN A 23  ? 0.4342 0.5580 0.4372 0.0357  0.0464  0.0364  323 GLN A OE1   
124  N NE2   . GLN A 23  ? 0.1912 0.4407 0.4362 -0.0161 0.0159  0.0569  323 GLN A NE2   
125  N N     . GLY A 24  ? 0.2041 0.2052 0.3085 -0.0441 0.0079  0.0153  324 GLY A N     
126  C CA    . GLY A 24  ? 0.1280 0.2190 0.3131 -0.0470 0.0149  0.0071  324 GLY A CA    
127  C C     . GLY A 24  ? 0.1405 0.2166 0.2938 -0.0473 0.0239  0.0047  324 GLY A C     
128  O O     . GLY A 24  ? 0.1784 0.2494 0.3089 -0.0554 -0.0156 0.0199  324 GLY A O     
129  N N     . HIS A 25  ? 0.1897 0.2116 0.3062 -0.0051 0.0191  0.0246  325 HIS A N     
130  C CA    . HIS A 25  ? 0.1817 0.1793 0.3130 -0.0096 0.0132  0.0243  325 HIS A CA    
131  C C     . HIS A 25  ? 0.1459 0.1580 0.3243 -0.0100 0.0046  0.0294  325 HIS A C     
132  O O     . HIS A 25  ? 0.1480 0.1603 0.3331 -0.0056 -0.0003 0.0211  325 HIS A O     
133  C CB    . HIS A 25  ? 0.2044 0.2026 0.3414 -0.0191 0.0131  0.0220  325 HIS A CB    
134  C CG    . HIS A 25  ? 0.1929 0.2236 0.3773 -0.0107 0.0077  0.0334  325 HIS A CG    
135  N ND1   . HIS A 25  ? 0.2325 0.2119 0.4069 -0.0099 0.0048  0.0214  325 HIS A ND1   
136  C CD2   . HIS A 25  ? 0.1215 0.2682 0.3889 -0.0098 0.0104  0.0212  325 HIS A CD2   
137  C CE1   . HIS A 25  ? 0.2279 0.2899 0.4191 -0.0822 0.0242  0.0364  325 HIS A CE1   
138  N NE2   . HIS A 25  ? 0.1718 0.2984 0.4190 -0.0665 0.0412  0.0350  325 HIS A NE2   
139  N N     . ILE A 26  ? 0.1308 0.1694 0.3088 0.0008  0.0038  0.0261  326 ILE A N     
140  C CA    . ILE A 26  ? 0.1624 0.1859 0.2984 -0.0087 0.0105  0.0158  326 ILE A CA    
141  C C     . ILE A 26  ? 0.1230 0.1696 0.3076 -0.0202 0.0009  0.0198  326 ILE A C     
142  O O     . ILE A 26  ? 0.1538 0.1896 0.3173 0.0338  0.0041  0.0162  326 ILE A O     
143  C CB    . ILE A 26  ? 0.1337 0.1461 0.3127 -0.0088 0.0030  0.0245  326 ILE A CB    
144  C CG1   . ILE A 26  ? 0.1424 0.1478 0.3096 -0.0131 0.0079  0.0204  326 ILE A CG1   
145  C CG2   . ILE A 26  ? 0.1579 0.1656 0.3163 0.0074  0.0088  0.0050  326 ILE A CG2   
146  C CD1   . ILE A 26  ? 0.1698 0.1884 0.3092 0.0162  -0.0140 0.0103  326 ILE A CD1   
147  N N     . GLU A 27  ? 0.1386 0.1834 0.3076 -0.0155 -0.0088 0.0053  327 GLU A N     
148  C CA    . GLU A 27  ? 0.1695 0.1919 0.3186 0.0165  -0.0053 0.0050  327 GLU A CA    
149  C C     . GLU A 27  ? 0.1562 0.1745 0.3297 0.0286  -0.0101 0.0013  327 GLU A C     
150  O O     . GLU A 27  ? 0.2186 0.1743 0.3417 0.0526  -0.0107 -0.0093 327 GLU A O     
151  C CB    . GLU A 27  ? 0.1869 0.1292 0.3559 0.0196  -0.0235 0.0142  327 GLU A CB    
152  C CG    . GLU A 27  ? 0.1931 0.1796 0.3482 -0.0225 -0.0268 0.0157  327 GLU A CG    
153  C CD    . GLU A 27  ? 0.1593 0.1774 0.3652 -0.0703 -0.0349 -0.0131 327 GLU A CD    
154  O OE1   . GLU A 27  ? 0.1357 0.1481 0.3462 -0.0288 -0.0078 0.0042  327 GLU A OE1   
155  O OE2   . GLU A 27  ? 0.1742 0.1859 0.4526 -0.0577 0.0311  0.0120  327 GLU A OE2   
156  N N     . TRP A 28  ? 0.1743 0.1713 0.3367 0.0353  -0.0149 0.0094  328 TRP A N     
157  C CA    . TRP A 28  ? 0.2004 0.1755 0.3496 0.0150  -0.0113 0.0336  328 TRP A CA    
158  C C     . TRP A 28  ? 0.2040 0.1613 0.3381 -0.0019 -0.0110 0.0390  328 TRP A C     
159  O O     . TRP A 28  ? 0.2335 0.1953 0.3543 -0.0004 -0.0261 0.0578  328 TRP A O     
160  C CB    . TRP A 28  ? 0.2311 0.2263 0.3646 0.0229  -0.0072 0.0482  328 TRP A CB    
161  C CG    . TRP A 28  ? 0.2697 0.2255 0.4271 -0.0524 0.0205  0.0669  328 TRP A CG    
162  C CD1   . TRP A 28  ? 0.2487 0.3173 0.4434 -0.0558 0.0134  0.0389  328 TRP A CD1   
163  C CD2   . TRP A 28  ? 0.2282 0.2758 0.4535 -0.0171 0.0020  0.0619  328 TRP A CD2   
164  N NE1   . TRP A 28  ? 0.2674 0.2948 0.4710 -0.0734 0.0123  0.0528  328 TRP A NE1   
165  C CE2   . TRP A 28  ? 0.2218 0.2749 0.5120 -0.0877 0.0410  0.0539  328 TRP A CE2   
166  C CE3   . TRP A 28  ? 0.2630 0.2599 0.4977 -0.0308 -0.0102 0.0567  328 TRP A CE3   
167  C CZ2   . TRP A 28  ? 0.1937 0.3181 0.5287 -0.0230 0.0283  0.0705  328 TRP A CZ2   
168  C CZ3   . TRP A 28  ? 0.2724 0.2949 0.5138 -0.0589 0.0423  0.0780  328 TRP A CZ3   
169  C CH2   . TRP A 28  ? 0.2635 0.3098 0.5367 -0.0600 0.0344  0.0696  328 TRP A CH2   
170  N N     A GLN A 29  ? 0.1625 0.1420 0.3177 0.0314  -0.0052 0.0451  329 GLN A N     
171  N N     B GLN A 29  ? 0.1848 0.1575 0.3297 0.0147  -0.0126 0.0466  329 GLN A N     
172  C CA    A GLN A 29  ? 0.1642 0.1489 0.3120 0.0311  -0.0144 0.0290  329 GLN A CA    
173  C CA    B GLN A 29  ? 0.1931 0.1791 0.3312 0.0135  -0.0275 0.0216  329 GLN A CA    
174  C C     A GLN A 29  ? 0.1977 0.1198 0.3036 0.0283  -0.0188 0.0302  329 GLN A C     
175  C C     B GLN A 29  ? 0.2038 0.1416 0.3128 -0.0002 -0.0194 0.0220  329 GLN A C     
176  O O     A GLN A 29  ? 0.2417 0.1340 0.3209 0.0192  -0.0443 0.0383  329 GLN A O     
177  O O     B GLN A 29  ? 0.1917 0.1390 0.3238 -0.0418 -0.0156 0.0254  329 GLN A O     
178  C CB    A GLN A 29  ? 0.1237 0.1475 0.3098 0.0392  -0.0129 0.0256  329 GLN A CB    
179  C CB    B GLN A 29  ? 0.1909 0.1914 0.3409 0.0106  -0.0438 0.0215  329 GLN A CB    
180  C CG    A GLN A 29  ? 0.1104 0.1572 0.3014 0.0369  -0.0004 0.0181  329 GLN A CG    
181  C CG    B GLN A 29  ? 0.1926 0.2137 0.3554 0.0300  -0.0469 0.0150  329 GLN A CG    
182  C CD    A GLN A 29  ? 0.0873 0.1615 0.2920 0.0413  0.0071  0.0065  329 GLN A CD    
183  C CD    B GLN A 29  ? 0.1791 0.2213 0.3547 0.0403  -0.0702 -0.0119 329 GLN A CD    
184  O OE1   A GLN A 29  ? 0.1125 0.2185 0.2862 -0.0046 -0.0025 0.0192  329 GLN A OE1   
185  O OE1   B GLN A 29  ? 0.1154 0.1790 0.3705 0.0123  -0.0287 -0.0159 329 GLN A OE1   
186  N NE2   A GLN A 29  ? 0.1433 0.1640 0.2988 0.0222  0.0110  0.0042  329 GLN A NE2   
187  N NE2   B GLN A 29  ? 0.2236 0.2304 0.3548 0.0735  -0.0681 -0.0245 329 GLN A NE2   
188  N N     . THR A 30  ? 0.1831 0.1292 0.3117 0.0235  -0.0143 0.0171  330 THR A N     
189  C CA    . THR A 30  ? 0.1636 0.1736 0.3287 0.0041  0.0035  0.0256  330 THR A CA    
190  C C     . THR A 30  ? 0.1651 0.2037 0.2952 -0.0180 -0.0164 0.0223  330 THR A C     
191  O O     . THR A 30  ? 0.2172 0.2200 0.3065 -0.0608 0.0285  0.0127  330 THR A O     
192  C CB    . THR A 30  ? 0.1798 0.1850 0.3651 0.0035  -0.0020 0.0426  330 THR A CB    
193  O OG1   . THR A 30  ? 0.2134 0.2200 0.3990 -0.0365 -0.0050 0.0545  330 THR A OG1   
194  C CG2   . THR A 30  ? 0.1712 0.2318 0.3929 0.0108  -0.0142 0.0411  330 THR A CG2   
195  N N     . ALA A 31  ? 0.1768 0.1565 0.2948 0.0014  -0.0103 0.0208  331 ALA A N     
196  C CA    . ALA A 31  ? 0.1916 0.1286 0.2790 -0.0057 -0.0053 0.0269  331 ALA A CA    
197  C C     . ALA A 31  ? 0.1621 0.1353 0.2949 -0.0022 0.0067  0.0131  331 ALA A C     
198  O O     . ALA A 31  ? 0.1818 0.1585 0.3205 -0.0077 -0.0004 -0.0037 331 ALA A O     
199  C CB    . ALA A 31  ? 0.1803 0.1494 0.2836 0.0311  -0.0153 0.0129  331 ALA A CB    
200  N N     . ASP A 32  ? 0.1464 0.1161 0.2807 -0.0106 -0.0169 0.0058  332 ASP A N     
201  C CA    . ASP A 32  ? 0.1181 0.1126 0.2882 -0.0148 -0.0235 0.0061  332 ASP A CA    
202  C C     . ASP A 32  ? 0.1117 0.1217 0.2838 0.0018  -0.0178 -0.0049 332 ASP A C     
203  O O     . ASP A 32  ? 0.1303 0.1155 0.2988 0.0111  -0.0095 -0.0074 332 ASP A O     
204  C CB    . ASP A 32  ? 0.0881 0.1334 0.3253 0.0004  -0.0158 0.0000  332 ASP A CB    
205  C CG    . ASP A 32  ? 0.1266 0.1448 0.3424 -0.0145 -0.0453 0.0025  332 ASP A CG    
206  O OD1   . ASP A 32  ? 0.1842 0.1539 0.3888 0.0048  -0.0462 0.0222  332 ASP A OD1   
207  O OD2   . ASP A 32  ? 0.1642 0.1418 0.3878 -0.0306 -0.0529 0.0087  332 ASP A OD2   
208  N N     . VAL A 33  ? 0.0913 0.1197 0.3048 0.0067  -0.0280 -0.0142 333 VAL A N     
209  C CA    . VAL A 33  ? 0.0949 0.1058 0.2926 -0.0008 -0.0103 -0.0006 333 VAL A CA    
210  C C     . VAL A 33  ? 0.0636 0.1094 0.2910 0.0110  -0.0225 0.0066  333 VAL A C     
211  O O     . VAL A 33  ? 0.0637 0.1482 0.2876 0.0033  -0.0089 -0.0024 333 VAL A O     
212  C CB    . VAL A 33  ? 0.1083 0.0925 0.3013 -0.0089 -0.0107 -0.0022 333 VAL A CB    
213  C CG1   . VAL A 33  ? 0.0965 0.1214 0.3058 -0.0219 -0.0195 0.0086  333 VAL A CG1   
214  C CG2   . VAL A 33  ? 0.1269 0.1455 0.3030 0.0266  -0.0069 0.0079  333 VAL A CG2   
215  N N     . ILE A 34  ? 0.1116 0.1128 0.2811 -0.0207 -0.0165 -0.0225 334 ILE A N     
216  C CA    . ILE A 34  ? 0.1145 0.1047 0.2770 -0.0046 -0.0049 0.0018  334 ILE A CA    
217  C C     . ILE A 34  ? 0.0866 0.1224 0.2690 -0.0119 -0.0055 -0.0003 334 ILE A C     
218  O O     . ILE A 34  ? 0.1140 0.1233 0.2769 0.0026  -0.0131 -0.0062 334 ILE A O     
219  C CB    . ILE A 34  ? 0.0983 0.1332 0.3021 -0.0092 0.0068  0.0036  334 ILE A CB    
220  C CG1   . ILE A 34  ? 0.1143 0.1456 0.3176 0.0084  0.0191  0.0080  334 ILE A CG1   
221  C CG2   . ILE A 34  ? 0.0983 0.1556 0.3303 -0.0200 0.0019  0.0075  334 ILE A CG2   
222  C CD1   . ILE A 34  ? 0.1422 0.1593 0.3159 -0.0075 0.0227  0.0072  334 ILE A CD1   
223  N N     . VAL A 35  ? 0.1124 0.1323 0.2756 -0.0025 -0.0016 -0.0150 335 VAL A N     
224  C CA    . VAL A 35  ? 0.1080 0.1334 0.2897 -0.0037 -0.0156 0.0007  335 VAL A CA    
225  C C     . VAL A 35  ? 0.1120 0.0875 0.2807 -0.0154 0.0135  -0.0005 335 VAL A C     
226  O O     . VAL A 35  ? 0.0950 0.1481 0.2909 0.0084  0.0046  -0.0019 335 VAL A O     
227  C CB    . VAL A 35  ? 0.0755 0.1267 0.2877 0.0057  -0.0051 0.0013  335 VAL A CB    
228  C CG1   . VAL A 35  ? 0.0794 0.1473 0.3079 -0.0172 -0.0081 0.0170  335 VAL A CG1   
229  C CG2   . VAL A 35  ? 0.0767 0.1411 0.2961 0.0211  0.0017  0.0103  335 VAL A CG2   
230  N N     . ASN A 36  ? 0.0756 0.1007 0.2836 0.0107  -0.0001 -0.0062 336 ASN A N     
231  C CA    . ASN A 36  ? 0.0737 0.0987 0.2979 0.0169  0.0019  -0.0103 336 ASN A CA    
232  C C     . ASN A 36  ? 0.1138 0.1232 0.2843 0.0143  -0.0039 0.0059  336 ASN A C     
233  O O     . ASN A 36  ? 0.1258 0.1373 0.2850 0.0115  0.0161  0.0089  336 ASN A O     
234  C CB    . ASN A 36  ? 0.1062 0.0918 0.3003 0.0003  0.0004  -0.0001 336 ASN A CB    
235  C CG    . ASN A 36  ? 0.1171 0.1188 0.3137 0.0054  0.0027  0.0088  336 ASN A CG    
236  O OD1   . ASN A 36  ? 0.1146 0.1167 0.3110 -0.0133 0.0094  0.0041  336 ASN A OD1   
237  N ND2   . ASN A 36  ? 0.0887 0.1188 0.3174 -0.0009 -0.0118 -0.0077 336 ASN A ND2   
238  N N     . SER A 37  ? 0.1229 0.1188 0.3060 -0.0072 -0.0128 0.0080  337 SER A N     
239  C CA    . SER A 37  ? 0.1187 0.1294 0.3030 0.0070  -0.0118 0.0063  337 SER A CA    
240  C C     . SER A 37  ? 0.1459 0.1587 0.2947 -0.0019 -0.0080 0.0040  337 SER A C     
241  O O     . SER A 37  ? 0.1318 0.1689 0.3100 -0.0037 -0.0046 0.0113  337 SER A O     
242  C CB    . SER A 37  ? 0.1421 0.1430 0.3116 -0.0012 -0.0047 -0.0001 337 SER A CB    
243  O OG    . SER A 37  ? 0.1418 0.1222 0.3278 0.0295  0.0032  -0.0140 337 SER A OG    
244  N N     . VAL A 38  ? 0.1008 0.1477 0.2844 -0.0168 0.0047  0.0062  338 VAL A N     
245  C CA    . VAL A 38  ? 0.1107 0.1208 0.2948 -0.0258 0.0037  0.0057  338 VAL A CA    
246  C C     . VAL A 38  ? 0.1124 0.1713 0.2840 -0.0184 -0.0041 0.0140  338 VAL A C     
247  O O     . VAL A 38  ? 0.0940 0.1399 0.3303 -0.0120 -0.0103 0.0180  338 VAL A O     
248  C CB    . VAL A 38  ? 0.1029 0.1672 0.3183 0.0072  -0.0051 -0.0111 338 VAL A CB    
249  C CG1   . VAL A 38  ? 0.1467 0.1686 0.3125 0.0222  -0.0067 -0.0008 338 VAL A CG1   
250  C CG2   . VAL A 38  ? 0.0822 0.1615 0.3204 0.0015  -0.0125 -0.0117 338 VAL A CG2   
251  N N     . ASN A 39  ? 0.1058 0.1709 0.3057 -0.0264 -0.0035 0.0245  339 ASN A N     
252  C CA    . ASN A 39  ? 0.1209 0.1760 0.3076 -0.0072 -0.0106 0.0121  339 ASN A CA    
253  C C     . ASN A 39  ? 0.1261 0.1131 0.3035 -0.0059 -0.0111 0.0094  339 ASN A C     
254  O O     . ASN A 39  ? 0.1319 0.1203 0.3182 -0.0183 -0.0268 0.0165  339 ASN A O     
255  C CB    . ASN A 39  ? 0.1153 0.2059 0.3309 0.0040  -0.0041 0.0224  339 ASN A CB    
256  C CG    . ASN A 39  ? 0.1237 0.2700 0.3165 0.0147  -0.0106 0.0182  339 ASN A CG    
257  O OD1   . ASN A 39  ? 0.1413 0.2307 0.3383 0.0213  0.0027  0.0402  339 ASN A OD1   
258  N ND2   . ASN A 39  ? 0.1240 0.3631 0.3479 -0.0166 -0.0151 0.0289  339 ASN A ND2   
259  N N     . PRO A 40  ? 0.1213 0.1174 0.3176 -0.0036 -0.0086 0.0057  340 PRO A N     
260  C CA    . PRO A 40  ? 0.1547 0.1401 0.3003 0.0084  -0.0262 0.0006  340 PRO A CA    
261  C C     . PRO A 40  ? 0.1594 0.1301 0.3078 -0.0185 -0.0243 0.0055  340 PRO A C     
262  O O     . PRO A 40  ? 0.2355 0.1367 0.3326 -0.0087 0.0026  -0.0152 340 PRO A O     
263  C CB    . PRO A 40  ? 0.1179 0.1760 0.3180 0.0104  -0.0091 0.0017  340 PRO A CB    
264  C CG    . PRO A 40  ? 0.1579 0.1486 0.3228 0.0064  -0.0125 0.0066  340 PRO A CG    
265  C CD    . PRO A 40  ? 0.1591 0.1149 0.3187 0.0122  -0.0104 0.0058  340 PRO A CD    
266  N N     . HIS A 41  ? 0.1416 0.1864 0.2903 -0.0338 -0.0282 0.0231  341 HIS A N     
267  C CA    . HIS A 41  ? 0.1909 0.1953 0.3117 -0.0511 -0.0349 0.0274  341 HIS A CA    
268  C C     . HIS A 41  ? 0.2296 0.2085 0.3001 -0.0581 -0.0296 0.0349  341 HIS A C     
269  O O     . HIS A 41  ? 0.2075 0.2686 0.3211 -0.0387 -0.0515 0.0021  341 HIS A O     
270  C CB    . HIS A 41  ? 0.1865 0.2592 0.3273 -0.0349 -0.0483 0.0455  341 HIS A CB    
271  C CG    . HIS A 41  ? 0.2107 0.2831 0.3628 -0.0215 -0.0301 0.0686  341 HIS A CG    
272  N ND1   . HIS A 41  ? 0.2758 0.3306 0.3912 -0.0595 -0.0157 0.0737  341 HIS A ND1   
273  C CD2   . HIS A 41  ? 0.1071 0.2687 0.4231 -0.0264 -0.0371 0.0921  341 HIS A CD2   
274  C CE1   . HIS A 41  ? 0.2515 0.3733 0.4405 -0.0457 0.0000  0.0956  341 HIS A CE1   
275  N NE2   . HIS A 41  ? 0.2304 0.3583 0.3916 -0.0358 -0.0421 0.0958  341 HIS A NE2   
276  N N     . ASP A 42  ? 0.1883 0.1540 0.3100 -0.0648 -0.0256 0.0279  342 ASP A N     
277  C CA    . ASP A 42  ? 0.1569 0.1924 0.3289 -0.0573 -0.0316 0.0372  342 ASP A CA    
278  C C     . ASP A 42  ? 0.1563 0.1791 0.3015 -0.0328 -0.0206 0.0156  342 ASP A C     
279  O O     . ASP A 42  ? 0.1662 0.1458 0.3285 -0.0385 -0.0227 0.0004  342 ASP A O     
280  C CB    . ASP A 42  ? 0.1695 0.2435 0.3291 -0.0317 -0.0504 0.0387  342 ASP A CB    
281  C CG    . ASP A 42  ? 0.1799 0.2634 0.3597 -0.0361 -0.0211 0.0493  342 ASP A CG    
282  O OD1   . ASP A 42  ? 0.1831 0.2273 0.3486 -0.0573 -0.0332 0.0351  342 ASP A OD1   
283  O OD2   . ASP A 42  ? 0.1951 0.3338 0.4274 -0.0406 -0.0552 0.0360  342 ASP A OD2   
284  N N     . ILE A 43  ? 0.1683 0.1120 0.3120 -0.0331 -0.0030 0.0051  343 ILE A N     
285  C CA    . ILE A 43  ? 0.1534 0.1215 0.3103 -0.0011 -0.0034 -0.0100 343 ILE A CA    
286  C C     . ILE A 43  ? 0.1561 0.1261 0.3122 -0.0316 -0.0218 0.0023  343 ILE A C     
287  O O     . ILE A 43  ? 0.1563 0.1562 0.3156 -0.0372 -0.0266 0.0029  343 ILE A O     
288  C CB    . ILE A 43  ? 0.1421 0.1621 0.3384 -0.0090 0.0155  -0.0264 343 ILE A CB    
289  C CG1   . ILE A 43  ? 0.1757 0.1673 0.3460 0.0161  0.0040  -0.0371 343 ILE A CG1   
290  C CG2   . ILE A 43  ? 0.1475 0.1648 0.3673 -0.0050 0.0235  -0.0129 343 ILE A CG2   
291  C CD1   . ILE A 43  ? 0.1808 0.1797 0.3656 -0.0056 0.0311  -0.0323 343 ILE A CD1   
292  N N     . THR A 44  ? 0.1469 0.1121 0.3438 -0.0158 -0.0202 -0.0020 344 THR A N     
293  C CA    . THR A 44  ? 0.1599 0.1948 0.3300 -0.0371 -0.0074 0.0063  344 THR A CA    
294  C C     . THR A 44  ? 0.1824 0.1777 0.3397 -0.0248 0.0100  0.0213  344 THR A C     
295  O O     . THR A 44  ? 0.1999 0.1898 0.3651 -0.0579 0.0216  0.0280  344 THR A O     
296  C CB    . THR A 44  ? 0.1792 0.1526 0.3488 -0.0331 -0.0361 0.0092  344 THR A CB    
297  O OG1   . THR A 44  ? 0.1914 0.1940 0.3402 -0.0357 -0.0336 0.0166  344 THR A OG1   
298  C CG2   . THR A 44  ? 0.1764 0.1523 0.3429 -0.0506 -0.0330 0.0076  344 THR A CG2   
299  N N     . VAL A 45  ? 0.1355 0.1585 0.3573 -0.0228 0.0011  -0.0203 345 VAL A N     
300  C CA    . VAL A 45  ? 0.1589 0.2036 0.3315 0.0049  0.0036  -0.0095 345 VAL A CA    
301  C C     . VAL A 45  ? 0.1511 0.1701 0.3352 0.0052  -0.0080 -0.0087 345 VAL A C     
302  O O     . VAL A 45  ? 0.1307 0.2173 0.3314 0.0056  -0.0188 -0.0060 345 VAL A O     
303  C CB    . VAL A 45  ? 0.2170 0.2738 0.3722 0.0503  -0.0110 -0.0078 345 VAL A CB    
304  C CG1   . VAL A 45  ? 0.2100 0.2826 0.3941 0.0381  -0.0427 -0.0018 345 VAL A CG1   
305  C CG2   . VAL A 45  ? 0.1743 0.3082 0.4110 0.0500  -0.0197 -0.0018 345 VAL A CG2   
306  N N     . GLY A 46  ? 0.1335 0.1611 0.3441 -0.0321 0.0057  -0.0129 346 GLY A N     
307  C CA    . GLY A 46  ? 0.1229 0.1727 0.3339 -0.0064 0.0020  -0.0137 346 GLY A CA    
308  C C     . GLY A 46  ? 0.0935 0.2000 0.3196 -0.0092 0.0108  -0.0125 346 GLY A C     
309  O O     . GLY A 46  ? 0.1304 0.1918 0.3344 -0.0090 0.0116  0.0006  346 GLY A O     
310  N N     . PRO A 47  ? 0.0800 0.1891 0.3304 0.0134  -0.0047 -0.0172 347 PRO A N     
311  C CA    . PRO A 47  ? 0.0798 0.2408 0.3340 -0.0161 -0.0166 -0.0089 347 PRO A CA    
312  C C     . PRO A 47  ? 0.0639 0.2037 0.3237 -0.0383 -0.0069 0.0080  347 PRO A C     
313  O O     . PRO A 47  ? 0.1193 0.2003 0.3494 -0.0069 -0.0118 -0.0021 347 PRO A O     
314  C CB    . PRO A 47  ? 0.1049 0.2485 0.3548 -0.0288 -0.0227 -0.0303 347 PRO A CB    
315  C CG    . PRO A 47  ? 0.1104 0.2179 0.3492 -0.0117 -0.0012 -0.0486 347 PRO A CG    
316  C CD    . PRO A 47  ? 0.1167 0.2125 0.3540 -0.0002 0.0092  -0.0405 347 PRO A CD    
317  N N     . VAL A 48  ? 0.0740 0.1919 0.3266 -0.0302 -0.0047 0.0128  348 VAL A N     
318  C CA    . VAL A 48  ? 0.0757 0.1982 0.2922 -0.0236 -0.0125 0.0153  348 VAL A CA    
319  C C     . VAL A 48  ? 0.1059 0.1549 0.2941 -0.0118 -0.0139 0.0176  348 VAL A C     
320  O O     . VAL A 48  ? 0.1201 0.1502 0.3244 -0.0085 -0.0173 0.0111  348 VAL A O     
321  C CB    . VAL A 48  ? 0.0686 0.2083 0.3062 -0.0152 -0.0110 0.0080  348 VAL A CB    
322  C CG1   . VAL A 48  ? 0.0658 0.1915 0.3040 -0.0235 -0.0115 -0.0027 348 VAL A CG1   
323  C CG2   . VAL A 48  ? 0.0722 0.2164 0.3208 -0.0091 -0.0038 -0.0088 348 VAL A CG2   
324  N N     . ALA A 49  ? 0.1011 0.1606 0.3108 -0.0052 0.0005  0.0248  349 ALA A N     
325  C CA    . ALA A 49  ? 0.1014 0.1819 0.3107 -0.0365 0.0021  0.0118  349 ALA A CA    
326  C C     . ALA A 49  ? 0.0771 0.1532 0.3237 -0.0101 -0.0205 -0.0051 349 ALA A C     
327  O O     . ALA A 49  ? 0.1045 0.1574 0.3258 -0.0082 -0.0118 0.0145  349 ALA A O     
328  C CB    . ALA A 49  ? 0.1002 0.1667 0.3182 -0.0262 0.0066  -0.0007 349 ALA A CB    
329  N N     . LYS A 50  ? 0.0790 0.1428 0.3366 -0.0065 -0.0219 0.0024  350 LYS A N     
330  C CA    . LYS A 50  ? 0.1288 0.1690 0.3240 -0.0370 -0.0069 0.0006  350 LYS A CA    
331  C C     . LYS A 50  ? 0.1058 0.1943 0.3423 -0.0199 0.0086  0.0028  350 LYS A C     
332  O O     . LYS A 50  ? 0.1505 0.1898 0.3935 -0.0544 -0.0080 0.0038  350 LYS A O     
333  C CB    . LYS A 50  ? 0.1344 0.1788 0.3498 0.0129  0.0003  0.0078  350 LYS A CB    
334  C CG    . LYS A 50  ? 0.1668 0.1857 0.3527 -0.0180 0.0113  0.0072  350 LYS A CG    
335  C CD    . LYS A 50  ? 0.1551 0.1982 0.3644 -0.0113 0.0109  -0.0030 350 LYS A CD    
336  C CE    . LYS A 50  ? 0.1339 0.2129 0.4156 -0.0437 0.0230  -0.0075 350 LYS A CE    
337  N NZ    . LYS A 50  ? 0.1744 0.2540 0.4479 -0.0460 0.0187  0.0065  350 LYS A NZ    
338  N N     . SER A 51  ? 0.1350 0.1950 0.3299 -0.0381 0.0067  0.0200  351 SER A N     
339  C CA    . SER A 51  ? 0.1378 0.2244 0.3393 -0.0352 0.0005  0.0323  351 SER A CA    
340  C C     . SER A 51  ? 0.1487 0.1494 0.3491 -0.0159 -0.0175 0.0306  351 SER A C     
341  O O     . SER A 51  ? 0.1282 0.1350 0.3514 -0.0225 -0.0143 0.0262  351 SER A O     
342  C CB    . SER A 51  ? 0.1211 0.2668 0.3202 -0.0239 -0.0051 0.0365  351 SER A CB    
343  O OG    . SER A 51  ? 0.1601 0.2738 0.3359 0.0186  0.0142  0.0246  351 SER A OG    
344  N N     . ILE A 52  ? 0.1138 0.1509 0.3433 -0.0057 -0.0138 0.0348  352 ILE A N     
345  C CA    . ILE A 52  ? 0.1144 0.1401 0.3274 -0.0216 -0.0225 0.0172  352 ILE A CA    
346  C C     . ILE A 52  ? 0.1348 0.1228 0.3263 -0.0101 -0.0322 0.0128  352 ILE A C     
347  O O     . ILE A 52  ? 0.1635 0.1092 0.3419 -0.0021 -0.0258 0.0089  352 ILE A O     
348  C CB    . ILE A 52  ? 0.1629 0.1315 0.3277 -0.0215 0.0201  0.0077  352 ILE A CB    
349  C CG1   . ILE A 52  ? 0.2119 0.1489 0.3383 -0.0290 0.0423  -0.0271 352 ILE A CG1   
350  C CG2   . ILE A 52  ? 0.1346 0.1392 0.3422 -0.0178 0.0111  0.0017  352 ILE A CG2   
351  C CD1   . ILE A 52  ? 0.2525 0.1594 0.3697 0.0136  0.0354  0.0089  352 ILE A CD1   
352  N N     . LEU A 53  ? 0.1370 0.1404 0.3261 -0.0213 -0.0191 0.0041  353 LEU A N     
353  C CA    . LEU A 53  ? 0.0970 0.1471 0.3309 -0.0336 -0.0260 0.0041  353 LEU A CA    
354  C C     . LEU A 53  ? 0.1184 0.1433 0.3512 -0.0162 0.0024  0.0169  353 LEU A C     
355  O O     . LEU A 53  ? 0.1517 0.1163 0.3592 -0.0178 -0.0248 0.0113  353 LEU A O     
356  C CB    . LEU A 53  ? 0.1464 0.1700 0.3394 -0.0391 -0.0500 0.0066  353 LEU A CB    
357  C CG    . LEU A 53  ? 0.1722 0.1674 0.3593 -0.0518 -0.0481 0.0021  353 LEU A CG    
358  C CD1   . LEU A 53  ? 0.1714 0.2237 0.3515 -0.0572 -0.0398 -0.0128 353 LEU A CD1   
359  C CD2   . LEU A 53  ? 0.1741 0.1876 0.3808 -0.0857 -0.0592 -0.0008 353 LEU A CD2   
360  N N     . GLN A 54  ? 0.1112 0.1284 0.3597 -0.0181 -0.0198 0.0257  354 GLN A N     
361  C CA    . GLN A 54  ? 0.1448 0.1203 0.3833 -0.0353 -0.0013 0.0175  354 GLN A CA    
362  C C     . GLN A 54  ? 0.2066 0.1706 0.3512 -0.0471 -0.0254 0.0458  354 GLN A C     
363  O O     . GLN A 54  ? 0.2474 0.1719 0.4325 -0.0630 -0.0527 0.0550  354 GLN A O     
364  C CB    . GLN A 54  ? 0.1499 0.1411 0.4061 -0.0346 0.0185  0.0270  354 GLN A CB    
365  C CG    . GLN A 54  ? 0.1905 0.2092 0.4375 -0.0396 0.0177  0.0090  354 GLN A CG    
366  C CD    . GLN A 54  ? 0.2309 0.2151 0.4953 -0.0289 0.0848  0.0185  354 GLN A CD    
367  O OE1   . GLN A 54  ? 0.3023 0.1961 0.5992 -0.0587 0.1221  0.0098  354 GLN A OE1   
368  N NE2   . GLN A 54  ? 0.2082 0.1979 0.5147 0.0424  0.1139  -0.0005 354 GLN A NE2   
369  N N     . GLN A 55  ? 0.1781 0.1610 0.3450 -0.0450 -0.0274 0.0444  355 GLN A N     
370  C CA    . GLN A 55  ? 0.2060 0.1525 0.3363 -0.0527 -0.0287 0.0395  355 GLN A CA    
371  C C     . GLN A 55  ? 0.2058 0.1481 0.3508 -0.0160 -0.0338 0.0265  355 GLN A C     
372  O O     . GLN A 55  ? 0.2261 0.1655 0.3825 0.0203  -0.0163 0.0398  355 GLN A O     
373  C CB    . GLN A 55  ? 0.2076 0.1787 0.3344 -0.0518 -0.0402 0.0259  355 GLN A CB    
374  C CG    . GLN A 55  ? 0.3330 0.2189 0.3474 -0.0938 -0.0737 0.0451  355 GLN A CG    
375  C CD    . GLN A 55  ? 0.3859 0.2950 0.4082 -0.0973 -0.0231 0.0905  355 GLN A CD    
376  O OE1   . GLN A 55  ? 0.4776 0.3815 0.4091 -0.0674 0.0257  0.0824  355 GLN A OE1   
377  N NE2   . GLN A 55  ? 0.4860 0.3892 0.4808 -0.0320 0.0160  0.1403  355 GLN A NE2   
378  N N     . ALA A 56  ? 0.1394 0.1209 0.3508 0.0067  -0.0301 0.0012  356 ALA A N     
379  C CA    . ALA A 56  ? 0.1651 0.1066 0.3518 -0.0097 -0.0183 0.0017  356 ALA A CA    
380  C C     . ALA A 56  ? 0.1531 0.1201 0.3430 -0.0222 -0.0204 0.0182  356 ALA A C     
381  O O     . ALA A 56  ? 0.2055 0.1306 0.3747 0.0093  -0.0280 -0.0319 356 ALA A O     
382  C CB    . ALA A 56  ? 0.1622 0.1436 0.3544 0.0217  0.0004  0.0098  356 ALA A CB    
383  N N     . GLY A 57  ? 0.1448 0.1665 0.3532 -0.0395 -0.0198 -0.0254 357 GLY A N     
384  C CA    . GLY A 57  ? 0.1523 0.2037 0.3602 -0.0219 -0.0309 -0.0310 357 GLY A CA    
385  C C     . GLY A 57  ? 0.1716 0.1682 0.3543 -0.0335 -0.0228 -0.0180 357 GLY A C     
386  O O     . GLY A 57  ? 0.1575 0.1890 0.3928 -0.0338 -0.0208 -0.0142 357 GLY A O     
387  N N     . VAL A 58  ? 0.1987 0.1608 0.3551 -0.0193 -0.0444 -0.0214 358 VAL A N     
388  C CA    . VAL A 58  ? 0.1812 0.1886 0.3534 -0.0032 -0.0353 -0.0149 358 VAL A CA    
389  C C     . VAL A 58  ? 0.1558 0.1879 0.3466 -0.0394 -0.0564 -0.0131 358 VAL A C     
390  O O     . VAL A 58  ? 0.2322 0.1895 0.3679 -0.0155 -0.0622 0.0146  358 VAL A O     
391  C CB    . VAL A 58  ? 0.1769 0.1955 0.3909 -0.0062 -0.0382 -0.0243 358 VAL A CB    
392  C CG1   . VAL A 58  ? 0.1840 0.1937 0.3879 0.0026  -0.0505 -0.0230 358 VAL A CG1   
393  C CG2   . VAL A 58  ? 0.1905 0.2193 0.4046 -0.0224 -0.0508 -0.0309 358 VAL A CG2   
394  N N     . GLU A 59  ? 0.1714 0.1539 0.3673 -0.0207 -0.0339 -0.0067 359 GLU A N     
395  C CA    . GLU A 59  ? 0.1659 0.1741 0.3502 -0.0017 -0.0126 0.0125  359 GLU A CA    
396  C C     . GLU A 59  ? 0.1987 0.1711 0.3302 0.0179  -0.0086 0.0072  359 GLU A C     
397  O O     . GLU A 59  ? 0.1966 0.1677 0.3427 0.0077  0.0013  0.0084  359 GLU A O     
398  C CB    . GLU A 59  ? 0.1786 0.1921 0.3866 0.0162  -0.0102 -0.0078 359 GLU A CB    
399  C CG    . GLU A 59  ? 0.2901 0.1816 0.4329 0.0173  -0.0234 -0.0189 359 GLU A CG    
400  C CD    . GLU A 59  ? 0.3767 0.2876 0.5145 0.0069  0.0047  -0.0231 359 GLU A CD    
401  O OE1   . GLU A 59  ? 0.3679 0.2644 0.5648 0.0674  -0.0508 -0.0214 359 GLU A OE1   
402  O OE2   . GLU A 59  ? 0.5409 0.3096 0.6038 0.0048  0.0278  -0.0341 359 GLU A OE2   
403  N N     . MET A 60  ? 0.1620 0.1469 0.3445 -0.0256 -0.0130 0.0061  360 MET A N     
404  C CA    . MET A 60  ? 0.1650 0.1506 0.3492 -0.0350 -0.0230 0.0065  360 MET A CA    
405  C C     . MET A 60  ? 0.1378 0.1657 0.3428 -0.0129 -0.0129 0.0010  360 MET A C     
406  O O     . MET A 60  ? 0.1972 0.1522 0.3552 -0.0353 -0.0230 -0.0004 360 MET A O     
407  C CB    . MET A 60  ? 0.1969 0.1313 0.3737 -0.0424 -0.0094 0.0121  360 MET A CB    
408  C CG    . MET A 60  ? 0.1612 0.1129 0.3929 -0.0289 -0.0150 0.0074  360 MET A CG    
409  S SD    . MET A 60  ? 0.2209 0.1483 0.4055 -0.0225 0.0043  -0.0008 360 MET A SD    
410  C CE    . MET A 60  ? 0.2973 0.0348 0.4076 -0.0140 0.0751  0.0125  360 MET A CE    
411  N N     . LYS A 61  ? 0.1432 0.1521 0.3321 -0.0274 -0.0130 0.0083  361 LYS A N     
412  C CA    . LYS A 61  ? 0.1622 0.1489 0.3305 -0.0200 -0.0123 0.0126  361 LYS A CA    
413  C C     . LYS A 61  ? 0.1422 0.1240 0.3317 -0.0116 -0.0217 0.0139  361 LYS A C     
414  O O     . LYS A 61  ? 0.1292 0.1300 0.3302 -0.0081 0.0036  0.0003  361 LYS A O     
415  C CB    . LYS A 61  ? 0.1721 0.2005 0.3470 -0.0404 0.0005  0.0128  361 LYS A CB    
416  C CG    . LYS A 61  ? 0.1648 0.2208 0.3570 -0.0095 0.0085  0.0074  361 LYS A CG    
417  C CD    . LYS A 61  ? 0.2020 0.2748 0.3859 -0.0335 -0.0067 0.0309  361 LYS A CD    
418  C CE    . LYS A 61  ? 0.1817 0.2584 0.3903 -0.0393 0.0100  0.0454  361 LYS A CE    
419  N NZ    . LYS A 61  ? 0.1870 0.2363 0.3872 -0.0430 -0.0100 0.0352  361 LYS A NZ    
420  N N     . SER A 62  ? 0.1710 0.1241 0.3458 0.0031  -0.0265 0.0072  362 SER A N     
421  C CA    . SER A 62  ? 0.2226 0.1330 0.3369 -0.0197 -0.0283 0.0068  362 SER A CA    
422  C C     . SER A 62  ? 0.1991 0.1236 0.3340 0.0164  -0.0333 0.0066  362 SER A C     
423  O O     . SER A 62  ? 0.1759 0.1287 0.3351 0.0157  -0.0377 -0.0089 362 SER A O     
424  C CB    . SER A 62  ? 0.2745 0.1141 0.4009 -0.0417 -0.0313 0.0188  362 SER A CB    
425  O OG    . SER A 62  ? 0.3109 0.1951 0.4919 -0.0443 -0.0484 -0.0224 362 SER A OG    
426  N N     . GLU A 63  ? 0.1701 0.0915 0.3223 0.0259  -0.0292 0.0040  363 GLU A N     
427  C CA    . GLU A 63  ? 0.1495 0.1133 0.3345 0.0283  -0.0024 -0.0105 363 GLU A CA    
428  C C     . GLU A 63  ? 0.1835 0.1226 0.3019 0.0177  0.0090  -0.0001 363 GLU A C     
429  O O     . GLU A 63  ? 0.1926 0.1459 0.3088 0.0066  -0.0065 0.0075  363 GLU A O     
430  C CB    . GLU A 63  ? 0.2327 0.1392 0.3453 0.0274  0.0013  0.0152  363 GLU A CB    
431  C CG    . GLU A 63  ? 0.2561 0.1616 0.4017 0.0218  -0.0313 -0.0101 363 GLU A CG    
432  C CD    . GLU A 63  ? 0.2926 0.2695 0.4815 0.0818  -0.0375 -0.0532 363 GLU A CD    
433  O OE1   . GLU A 63  ? 0.4145 0.2918 0.6143 0.1106  -0.0181 -0.0137 363 GLU A OE1   
434  O OE2   . GLU A 63  ? 0.3989 0.2672 0.4847 0.1516  -0.0778 -0.1147 363 GLU A OE2   
435  N N     . PHE A 64  ? 0.1354 0.0982 0.3237 0.0053  -0.0014 -0.0021 364 PHE A N     
436  C CA    . PHE A 64  ? 0.1340 0.1027 0.3258 0.0002  -0.0161 -0.0091 364 PHE A CA    
437  C C     . PHE A 64  ? 0.1524 0.1061 0.3314 0.0000  -0.0161 -0.0111 364 PHE A C     
438  O O     . PHE A 64  ? 0.1550 0.1134 0.3469 -0.0168 -0.0030 -0.0072 364 PHE A O     
439  C CB    . PHE A 64  ? 0.1408 0.1005 0.3237 0.0032  -0.0112 -0.0080 364 PHE A CB    
440  C CG    . PHE A 64  ? 0.1191 0.1080 0.3097 0.0016  -0.0063 -0.0059 364 PHE A CG    
441  C CD1   . PHE A 64  ? 0.1465 0.1332 0.3054 0.0329  -0.0207 -0.0169 364 PHE A CD1   
442  C CD2   . PHE A 64  ? 0.1294 0.1312 0.3019 0.0123  -0.0129 -0.0073 364 PHE A CD2   
443  C CE1   . PHE A 64  ? 0.1084 0.1332 0.3108 0.0436  -0.0304 -0.0095 364 PHE A CE1   
444  C CE2   . PHE A 64  ? 0.1236 0.1360 0.3042 -0.0043 -0.0156 -0.0174 364 PHE A CE2   
445  C CZ    . PHE A 64  ? 0.1330 0.1430 0.3130 0.0050  -0.0231 -0.0030 364 PHE A CZ    
446  N N     . LEU A 65  ? 0.1356 0.1062 0.3192 -0.0192 -0.0056 -0.0036 365 LEU A N     
447  C CA    . LEU A 65  ? 0.1981 0.0995 0.3210 -0.0185 -0.0178 0.0080  365 LEU A CA    
448  C C     . LEU A 65  ? 0.2390 0.1229 0.3289 -0.0080 -0.0131 -0.0106 365 LEU A C     
449  O O     . LEU A 65  ? 0.2369 0.1482 0.3164 -0.0361 -0.0234 0.0037  365 LEU A O     
450  C CB    . LEU A 65  ? 0.1771 0.1846 0.3374 -0.0354 -0.0259 -0.0058 365 LEU A CB    
451  C CG    . LEU A 65  ? 0.1555 0.2267 0.3931 -0.0013 -0.0318 0.0126  365 LEU A CG    
452  C CD1   . LEU A 65  ? 0.1704 0.2824 0.4051 -0.0547 -0.0257 0.0209  365 LEU A CD1   
453  C CD2   . LEU A 65  ? 0.1339 0.2918 0.4410 0.0318  -0.0174 0.0400  365 LEU A CD2   
454  N N     . ALA A 66  ? 0.2275 0.1005 0.3365 -0.0194 0.0048  -0.0051 366 ALA A N     
455  C CA    . ALA A 66  ? 0.2720 0.1190 0.3352 -0.0054 0.0171  -0.0423 366 ALA A CA    
456  C C     . ALA A 66  ? 0.2019 0.1320 0.3314 0.0133  0.0194  -0.0269 366 ALA A C     
457  O O     . ALA A 66  ? 0.2647 0.1666 0.3633 0.0298  0.0478  -0.0233 366 ALA A O     
458  C CB    . ALA A 66  ? 0.2477 0.1503 0.3718 0.0345  0.0327  -0.0464 366 ALA A CB    
459  N N     . THR A 67  ? 0.1796 0.1094 0.3279 0.0056  0.0047  -0.0002 367 THR A N     
460  C CA    . THR A 67  ? 0.2363 0.1146 0.3484 -0.0142 0.0226  -0.0242 367 THR A CA    
461  C C     . THR A 67  ? 0.1939 0.1496 0.3316 -0.0035 0.0285  -0.0036 367 THR A C     
462  O O     . THR A 67  ? 0.2178 0.1740 0.3400 -0.0388 0.0055  0.0064  367 THR A O     
463  C CB    . THR A 67  ? 0.2129 0.1215 0.3652 0.0024  -0.0163 -0.0228 367 THR A CB    
464  O OG1   . THR A 67  ? 0.2370 0.1222 0.4529 0.0160  -0.0682 -0.0264 367 THR A OG1   
465  C CG2   . THR A 67  ? 0.2093 0.1158 0.3874 0.0094  0.0108  -0.0396 367 THR A CG2   
466  N N     . LYS A 68  ? 0.1763 0.0592 0.3544 -0.0138 0.0203  -0.0012 368 LYS A N     
467  C CA    . LYS A 68  ? 0.2195 0.0759 0.3367 -0.0175 0.0204  0.0025  368 LYS A CA    
468  C C     . LYS A 68  ? 0.2623 0.1077 0.3464 0.0029  -0.0037 -0.0036 368 LYS A C     
469  O O     . LYS A 68  ? 0.2587 0.1480 0.3324 -0.0393 -0.0086 0.0192  368 LYS A O     
470  C CB    . LYS A 68  ? 0.1927 0.1178 0.3746 -0.0353 -0.0007 0.0037  368 LYS A CB    
471  C CG    . LYS A 68  ? 0.2011 0.1521 0.4121 -0.0368 0.0005  0.0241  368 LYS A CG    
472  C CD    . LYS A 68  ? 0.2019 0.2028 0.4481 0.0253  -0.0143 0.0234  368 LYS A CD    
473  C CE    . LYS A 68  ? 0.2300 0.2289 0.4611 0.0518  -0.0162 0.0313  368 LYS A CE    
474  N NZ    . LYS A 68  ? 0.3157 0.3203 0.4994 0.0438  -0.0377 0.0403  368 LYS A NZ    
475  N N     . ALA A 69  ? 0.2932 0.0886 0.3698 -0.0090 -0.0086 -0.0065 369 ALA A N     
476  C CA    . ALA A 69  ? 0.3673 0.1347 0.3543 -0.0354 0.0095  -0.0127 369 ALA A CA    
477  C C     . ALA A 69  ? 0.3734 0.1861 0.3478 -0.0342 0.0091  -0.0113 369 ALA A C     
478  O O     . ALA A 69  ? 0.4592 0.2781 0.3617 -0.0583 0.0017  0.0086  369 ALA A O     
479  C CB    . ALA A 69  ? 0.3976 0.1441 0.3730 -0.0424 -0.0064 -0.0142 369 ALA A CB    
480  N N     . LYS A 70  ? 0.3631 0.1332 0.3716 -0.0142 0.0466  -0.0103 370 LYS A N     
481  C CA    . LYS A 70  ? 0.3329 0.2122 0.3950 -0.0016 0.0731  -0.0122 370 LYS A CA    
482  C C     . LYS A 70  ? 0.2931 0.2239 0.3661 -0.0277 0.0696  -0.0053 370 LYS A C     
483  O O     . LYS A 70  ? 0.3570 0.2284 0.4253 -0.0314 0.1129  0.0147  370 LYS A O     
484  C CB    . LYS A 70  ? 0.3669 0.1781 0.4634 -0.0072 0.0654  -0.0128 370 LYS A CB    
485  C CG    . LYS A 70  ? 0.4548 0.2375 0.5642 -0.0780 0.0325  -0.0430 370 LYS A CG    
486  C CD    . LYS A 70  ? 0.4648 0.3371 0.6899 -0.0626 0.0330  -0.0543 370 LYS A CD    
487  C CE    . LYS A 70  ? 0.5373 0.4192 0.7389 -0.0675 0.0348  -0.0629 370 LYS A CE    
488  N NZ    . LYS A 70  ? 0.5544 0.3708 0.8041 -0.0403 0.0109  -0.0440 370 LYS A NZ    
489  N N     . GLN A 71  ? 0.2430 0.1518 0.3810 -0.0063 0.0634  -0.0127 371 GLN A N     
490  C CA    . GLN A 71  ? 0.2362 0.1341 0.3727 -0.0054 0.0504  -0.0095 371 GLN A CA    
491  C C     . GLN A 71  ? 0.1863 0.1540 0.3664 -0.0063 0.0357  -0.0093 371 GLN A C     
492  O O     . GLN A 71  ? 0.2277 0.1475 0.3937 -0.0142 0.0406  0.0101  371 GLN A O     
493  C CB    . GLN A 71  ? 0.2077 0.1747 0.3959 0.0141  0.0397  -0.0326 371 GLN A CB    
494  C CG    . GLN A 71  ? 0.1855 0.2237 0.4033 0.0243  0.0445  -0.0418 371 GLN A CG    
495  C CD    . GLN A 71  ? 0.1967 0.2571 0.4069 0.0203  0.0179  -0.0486 371 GLN A CD    
496  O OE1   . GLN A 71  ? 0.1845 0.1767 0.3692 0.0116  0.0139  -0.0080 371 GLN A OE1   
497  N NE2   . GLN A 71  ? 0.2505 0.2906 0.4440 0.0338  0.0055  -0.0243 371 GLN A NE2   
498  N N     . PHE A 72  ? 0.1821 0.1248 0.3408 0.0034  0.0225  -0.0125 372 PHE A N     
499  C CA    . PHE A 72  ? 0.1349 0.1612 0.3480 0.0090  0.0174  -0.0064 372 PHE A CA    
500  C C     . PHE A 72  ? 0.1468 0.1384 0.3305 -0.0241 0.0011  -0.0218 372 PHE A C     
501  O O     . PHE A 72  ? 0.2761 0.1223 0.3339 -0.0022 0.0142  -0.0284 372 PHE A O     
502  C CB    . PHE A 72  ? 0.1616 0.1507 0.3895 0.0014  0.0200  0.0060  372 PHE A CB    
503  C CG    . PHE A 72  ? 0.1403 0.1824 0.3839 0.0091  0.0401  0.0440  372 PHE A CG    
504  C CD1   . PHE A 72  ? 0.1895 0.1609 0.4010 0.0484  0.0550  0.0892  372 PHE A CD1   
505  C CD2   . PHE A 72  ? 0.1709 0.2199 0.4221 0.0249  0.0160  0.0138  372 PHE A CD2   
506  C CE1   . PHE A 72  ? 0.1675 0.2424 0.3983 0.0684  0.0592  0.0743  372 PHE A CE1   
507  C CE2   . PHE A 72  ? 0.1635 0.2195 0.4393 0.0513  0.0274  0.0592  372 PHE A CE2   
508  C CZ    . PHE A 72  ? 0.1475 0.2716 0.4185 0.0671  0.0376  0.0689  372 PHE A CZ    
509  N N     . GLN A 73  ? 0.1831 0.1115 0.3242 -0.0100 0.0074  0.0079  373 GLN A N     
510  C CA    . GLN A 73  ? 0.1678 0.1020 0.3142 -0.0200 0.0061  0.0115  373 GLN A CA    
511  C C     . GLN A 73  ? 0.1372 0.1375 0.2873 -0.0315 0.0093  0.0106  373 GLN A C     
512  O O     . GLN A 73  ? 0.1633 0.1358 0.2850 -0.0118 -0.0042 0.0122  373 GLN A O     
513  C CB    . GLN A 73  ? 0.1764 0.1379 0.3511 -0.0106 0.0129  0.0241  373 GLN A CB    
514  C CG    . GLN A 73  ? 0.1896 0.1471 0.3647 0.0169  -0.0010 0.0160  373 GLN A CG    
515  C CD    . GLN A 73  ? 0.2160 0.1953 0.3827 0.0296  0.0175  -0.0052 373 GLN A CD    
516  O OE1   . GLN A 73  ? 0.1779 0.2016 0.4355 -0.0028 0.0185  0.0069  373 GLN A OE1   
517  N NE2   . GLN A 73  ? 0.2704 0.2820 0.4165 0.0318  0.0208  -0.0360 373 GLN A NE2   
518  N N     . ARG A 74  ? 0.1497 0.1359 0.2775 -0.0368 0.0101  0.0292  374 ARG A N     
519  C CA    . ARG A 74  ? 0.1688 0.1494 0.2970 -0.0170 0.0150  0.0187  374 ARG A CA    
520  C C     . ARG A 74  ? 0.1721 0.1354 0.2837 0.0011  0.0183  0.0248  374 ARG A C     
521  O O     . ARG A 74  ? 0.1789 0.1657 0.3007 0.0117  0.0191  0.0041  374 ARG A O     
522  C CB    . ARG A 74  ? 0.1936 0.1561 0.3262 -0.0023 0.0022  0.0277  374 ARG A CB    
523  C CG    . ARG A 74  ? 0.2372 0.1477 0.3580 0.0038  0.0042  0.0178  374 ARG A CG    
524  C CD    . ARG A 74  ? 0.1985 0.1747 0.3623 0.0129  -0.0265 0.0204  374 ARG A CD    
525  N NE    . ARG A 74  ? 0.2230 0.2357 0.3776 0.0471  -0.0438 0.0394  374 ARG A NE    
526  C CZ    . ARG A 74  ? 0.2045 0.2277 0.3965 0.0343  -0.0266 0.0440  374 ARG A CZ    
527  N NH1   . ARG A 74  ? 0.2124 0.2564 0.4130 0.0370  -0.0071 0.0285  374 ARG A NH1   
528  N NH2   . ARG A 74  ? 0.1861 0.2539 0.4294 0.0584  0.0018  0.0337  374 ARG A NH2   
529  N N     . SER A 75  ? 0.1538 0.1284 0.2971 -0.0198 0.0172  0.0018  375 SER A N     
530  C CA    . SER A 75  ? 0.2026 0.1478 0.2803 0.0081  0.0085  -0.0028 375 SER A CA    
531  C C     . SER A 75  ? 0.1936 0.1028 0.2887 0.0272  0.0225  -0.0023 375 SER A C     
532  O O     . SER A 75  ? 0.2355 0.1236 0.3043 -0.0048 -0.0033 0.0063  375 SER A O     
533  C CB    . SER A 75  ? 0.1903 0.1238 0.3044 -0.0052 -0.0060 0.0037  375 SER A CB    
534  O OG    . SER A 75  ? 0.1666 0.1363 0.3280 -0.0073 0.0065  -0.0052 375 SER A OG    
535  N N     . GLN A 76  ? 0.1601 0.1367 0.2806 0.0065  -0.0047 -0.0075 376 GLN A N     
536  C CA    . GLN A 76  ? 0.1481 0.1529 0.2734 -0.0043 -0.0161 -0.0026 376 GLN A CA    
537  C C     . GLN A 76  ? 0.1534 0.0970 0.2877 0.0166  -0.0138 0.0029  376 GLN A C     
538  O O     . GLN A 76  ? 0.1319 0.1829 0.3093 -0.0043 -0.0154 -0.0059 376 GLN A O     
539  C CB    . GLN A 76  ? 0.1393 0.1408 0.2835 0.0000  -0.0035 -0.0035 376 GLN A CB    
540  C CG    . GLN A 76  ? 0.1836 0.1493 0.2867 0.0070  0.0020  -0.0045 376 GLN A CG    
541  C CD    . GLN A 76  ? 0.1817 0.1524 0.3155 0.0117  -0.0148 -0.0209 376 GLN A CD    
542  O OE1   . GLN A 76  ? 0.2912 0.1388 0.3614 0.0476  -0.0430 -0.0310 376 GLN A OE1   
543  N NE2   . GLN A 76  ? 0.1974 0.1273 0.3288 -0.0165 -0.0192 -0.0022 376 GLN A NE2   
544  N N     . LEU A 77  ? 0.1457 0.0992 0.2916 0.0004  -0.0051 0.0173  377 LEU A N     
545  C CA    . LEU A 77  ? 0.1284 0.1027 0.2939 -0.0009 -0.0005 0.0127  377 LEU A CA    
546  C C     . LEU A 77  ? 0.1143 0.1348 0.2752 0.0019  -0.0020 0.0215  377 LEU A C     
547  O O     . LEU A 77  ? 0.1183 0.1112 0.2905 -0.0250 0.0157  0.0136  377 LEU A O     
548  C CB    . LEU A 77  ? 0.1126 0.1136 0.3172 -0.0219 0.0093  0.0116  377 LEU A CB    
549  C CG    . LEU A 77  ? 0.1471 0.1144 0.3486 -0.0035 0.0276  -0.0048 377 LEU A CG    
550  C CD1   . LEU A 77  ? 0.1523 0.1407 0.3512 0.0089  0.0168  -0.0055 377 LEU A CD1   
551  C CD2   . LEU A 77  ? 0.1908 0.1259 0.4014 -0.0083 0.0167  -0.0190 377 LEU A CD2   
552  N N     . VAL A 78  ? 0.0962 0.1463 0.2855 0.0059  -0.0041 0.0264  378 VAL A N     
553  C CA    . VAL A 78  ? 0.1082 0.1245 0.2970 0.0025  0.0080  0.0156  378 VAL A CA    
554  C C     . VAL A 78  ? 0.1385 0.1011 0.3045 0.0095  0.0216  0.0209  378 VAL A C     
555  O O     . VAL A 78  ? 0.1520 0.1116 0.3422 -0.0287 0.0298  0.0010  378 VAL A O     
556  C CB    . VAL A 78  ? 0.1155 0.1351 0.3031 0.0049  -0.0087 0.0154  378 VAL A CB    
557  C CG1   . VAL A 78  ? 0.1628 0.1251 0.3235 0.0215  -0.0127 0.0181  378 VAL A CG1   
558  C CG2   . VAL A 78  ? 0.1339 0.1705 0.2887 -0.0017 0.0014  0.0049  378 VAL A CG2   
559  N N     . LEU A 79  ? 0.1089 0.1115 0.3118 0.0180  -0.0005 0.0022  379 LEU A N     
560  C CA    . LEU A 79  ? 0.1175 0.1003 0.3006 0.0067  0.0108  0.0068  379 LEU A CA    
561  C C     . LEU A 79  ? 0.1172 0.1052 0.2854 0.0063  0.0046  0.0016  379 LEU A C     
562  O O     . LEU A 79  ? 0.1367 0.1077 0.2978 0.0153  0.0136  0.0231  379 LEU A O     
563  C CB    . LEU A 79  ? 0.1355 0.0920 0.3138 0.0122  -0.0010 -0.0030 379 LEU A CB    
564  C CG    . LEU A 79  ? 0.1311 0.1045 0.3253 0.0247  0.0000  -0.0066 379 LEU A CG    
565  C CD1   . LEU A 79  ? 0.1852 0.1229 0.3353 0.0419  -0.0088 -0.0086 379 LEU A CD1   
566  C CD2   . LEU A 79  ? 0.0904 0.1201 0.3308 0.0212  0.0119  0.0031  379 LEU A CD2   
567  N N     . VAL A 80  ? 0.1084 0.1479 0.2889 -0.0015 0.0073  -0.0018 380 VAL A N     
568  C CA    . VAL A 80  ? 0.1205 0.1067 0.2815 0.0040  -0.0054 0.0014  380 VAL A CA    
569  C C     . VAL A 80  ? 0.1241 0.1137 0.2798 0.0021  -0.0251 0.0091  380 VAL A C     
570  O O     . VAL A 80  ? 0.1665 0.1221 0.2897 0.0226  -0.0130 0.0034  380 VAL A O     
571  C CB    . VAL A 80  ? 0.1290 0.1274 0.3039 0.0223  0.0039  0.0074  380 VAL A CB    
572  C CG1   . VAL A 80  ? 0.1635 0.1537 0.3025 0.0187  -0.0014 0.0104  380 VAL A CG1   
573  C CG2   . VAL A 80  ? 0.1500 0.1333 0.3110 0.0173  -0.0191 0.0000  380 VAL A CG2   
574  N N     . THR A 81  ? 0.1770 0.1180 0.2903 0.0090  -0.0048 -0.0062 381 THR A N     
575  C CA    . THR A 81  ? 0.1655 0.1077 0.2992 0.0116  -0.0166 -0.0115 381 THR A CA    
576  C C     . THR A 81  ? 0.1616 0.1162 0.3079 0.0203  -0.0033 -0.0226 381 THR A C     
577  O O     . THR A 81  ? 0.1398 0.0942 0.3214 0.0224  -0.0134 -0.0136 381 THR A O     
578  C CB    . THR A 81  ? 0.1801 0.1049 0.2961 -0.0091 -0.0334 -0.0068 381 THR A CB    
579  O OG1   . THR A 81  ? 0.1715 0.1214 0.2954 0.0085  -0.0205 -0.0056 381 THR A OG1   
580  C CG2   . THR A 81  ? 0.1730 0.1478 0.2943 -0.0155 -0.0271 0.0144  381 THR A CG2   
581  N N     . LYS A 82  ? 0.1679 0.1017 0.3217 0.0081  -0.0113 -0.0119 382 LYS A N     
582  C CA    . LYS A 82  ? 0.2123 0.1061 0.3259 0.0177  -0.0189 0.0070  382 LYS A CA    
583  C C     . LYS A 82  ? 0.1920 0.0992 0.3062 0.0157  -0.0312 -0.0004 382 LYS A C     
584  O O     . LYS A 82  ? 0.1824 0.1287 0.3379 0.0235  -0.0377 0.0260  382 LYS A O     
585  C CB    . LYS A 82  ? 0.2898 0.1022 0.3620 0.0204  0.0038  0.0281  382 LYS A CB    
586  C CG    . LYS A 82  ? 0.3028 0.1468 0.4045 0.0604  0.0036  0.0227  382 LYS A CG    
587  C CD    . LYS A 82  ? 0.3757 0.2005 0.4490 0.1172  0.0181  0.0038  382 LYS A CD    
588  C CE    . LYS A 82  ? 0.4500 0.3795 0.4870 0.0841  0.0078  -0.0411 382 LYS A CE    
589  N NZ    . LYS A 82  ? 0.5760 0.3960 0.4918 0.0755  0.0132  -0.0510 382 LYS A NZ    
590  N N     . GLY A 83  ? 0.1722 0.1343 0.3277 0.0315  -0.0337 0.0118  383 GLY A N     
591  C CA    . GLY A 83  ? 0.1902 0.1227 0.3265 0.0205  -0.0196 0.0163  383 GLY A CA    
592  C C     . GLY A 83  ? 0.1960 0.1243 0.3372 0.0093  -0.0144 -0.0035 383 GLY A C     
593  O O     . GLY A 83  ? 0.1835 0.1106 0.3668 0.0123  -0.0145 0.0097  383 GLY A O     
594  N N     . PHE A 84  ? 0.1626 0.1401 0.3433 0.0088  -0.0257 -0.0037 384 PHE A N     
595  C CA    . PHE A 84  ? 0.2146 0.1207 0.3413 0.0166  -0.0393 -0.0093 384 PHE A CA    
596  C C     . PHE A 84  ? 0.2211 0.0977 0.3451 -0.0017 -0.0307 -0.0004 384 PHE A C     
597  O O     . PHE A 84  ? 0.2036 0.1150 0.3717 0.0152  -0.0392 0.0285  384 PHE A O     
598  C CB    . PHE A 84  ? 0.2043 0.1367 0.3392 0.0050  -0.0271 -0.0101 384 PHE A CB    
599  C CG    . PHE A 84  ? 0.1974 0.1652 0.3439 0.0056  -0.0148 -0.0060 384 PHE A CG    
600  C CD1   . PHE A 84  ? 0.2016 0.2009 0.3489 -0.0182 0.0114  -0.0276 384 PHE A CD1   
601  C CD2   . PHE A 84  ? 0.1942 0.1831 0.3457 0.0273  -0.0217 0.0185  384 PHE A CD2   
602  C CE1   . PHE A 84  ? 0.2552 0.2375 0.3614 0.0059  -0.0051 -0.0257 384 PHE A CE1   
603  C CE2   . PHE A 84  ? 0.1855 0.2349 0.3513 0.0371  -0.0189 0.0141  384 PHE A CE2   
604  C CZ    . PHE A 84  ? 0.1858 0.2615 0.3350 0.0195  0.0071  0.0096  384 PHE A CZ    
605  N N     . ASN A 85  ? 0.2184 0.0935 0.3613 0.0228  -0.0217 0.0029  385 ASN A N     
606  C CA    . ASN A 85  ? 0.2116 0.1558 0.3515 0.0013  -0.0263 0.0091  385 ASN A CA    
607  C C     . ASN A 85  ? 0.2149 0.1169 0.3397 -0.0112 0.0005  0.0229  385 ASN A C     
608  O O     . ASN A 85  ? 0.3167 0.1574 0.3473 -0.0469 0.0240  0.0279  385 ASN A O     
609  C CB    . ASN A 85  ? 0.2357 0.1487 0.3851 -0.0273 -0.0400 0.0115  385 ASN A CB    
610  C CG    . ASN A 85  ? 0.3002 0.1780 0.4721 -0.0192 -0.0241 -0.0025 385 ASN A CG    
611  O OD1   . ASN A 85  ? 0.3821 0.2357 0.5246 0.0077  -0.0018 -0.0414 385 ASN A OD1   
612  N ND2   . ASN A 85  ? 0.3646 0.2398 0.5087 -0.0027 -0.0783 -0.0344 385 ASN A ND2   
613  N N     . LEU A 86  ? 0.2019 0.1084 0.3572 -0.0204 0.0122  0.0094  386 LEU A N     
614  C CA    . LEU A 86  ? 0.2005 0.1208 0.3593 -0.0175 -0.0056 -0.0131 386 LEU A CA    
615  C C     . LEU A 86  ? 0.2209 0.1114 0.3222 -0.0004 -0.0075 -0.0003 386 LEU A C     
616  O O     . LEU A 86  ? 0.2332 0.1456 0.3617 -0.0031 0.0080  -0.0318 386 LEU A O     
617  C CB    . LEU A 86  ? 0.1874 0.1334 0.3840 0.0003  -0.0017 -0.0007 386 LEU A CB    
618  C CG    . LEU A 86  ? 0.1661 0.1739 0.3898 -0.0191 -0.0014 0.0449  386 LEU A CG    
619  C CD1   . LEU A 86  ? 0.1837 0.1668 0.4311 -0.0405 -0.0136 0.0366  386 LEU A CD1   
620  C CD2   . LEU A 86  ? 0.1652 0.2266 0.4121 -0.0114 -0.0011 0.0382  386 LEU A CD2   
621  N N     . PHE A 87  ? 0.2111 0.1249 0.3323 -0.0035 -0.0099 -0.0042 387 PHE A N     
622  C CA    . PHE A 87  ? 0.2275 0.0970 0.3495 0.0037  -0.0197 0.0060  387 PHE A CA    
623  C C     . PHE A 87  ? 0.2422 0.1100 0.3329 -0.0135 -0.0137 0.0026  387 PHE A C     
624  O O     . PHE A 87  ? 0.2321 0.1545 0.3100 -0.0258 -0.0051 0.0117  387 PHE A O     
625  C CB    . PHE A 87  ? 0.2464 0.1188 0.3655 -0.0050 -0.0008 0.0079  387 PHE A CB    
626  C CG    . PHE A 87  ? 0.3676 0.2144 0.4183 -0.0595 0.0329  0.0371  387 PHE A CG    
627  C CD1   . PHE A 87  ? 0.5109 0.2448 0.4610 -0.0669 0.0845  0.0122  387 PHE A CD1   
628  C CD2   . PHE A 87  ? 0.4413 0.3215 0.5076 -0.1070 0.0726  0.0661  387 PHE A CD2   
629  C CE1   . PHE A 87  ? 0.5723 0.3026 0.5354 -0.1038 0.0946  0.0559  387 PHE A CE1   
630  C CE2   . PHE A 87  ? 0.5050 0.3188 0.6032 -0.1404 0.1156  0.0642  387 PHE A CE2   
631  C CZ    . PHE A 87  ? 0.5972 0.3031 0.5688 -0.1141 0.1173  0.0509  387 PHE A CZ    
632  N N     . CYS A 88  ? 0.2545 0.0872 0.3190 -0.0091 -0.0228 -0.0056 388 CYS A N     
633  C CA    . CYS A 88  ? 0.2579 0.0799 0.3267 0.0090  -0.0108 0.0116  388 CYS A CA    
634  C C     . CYS A 88  ? 0.2323 0.1121 0.3131 0.0311  -0.0254 0.0021  388 CYS A C     
635  O O     . CYS A 88  ? 0.2197 0.1586 0.3660 -0.0278 0.0071  -0.0191 388 CYS A O     
636  C CB    . CYS A 88  ? 0.1880 0.0893 0.3296 0.0092  -0.0039 0.0000  388 CYS A CB    
637  S SG    . CYS A 88  ? 0.1591 0.1365 0.3550 -0.0362 -0.0104 0.0109  388 CYS A SG    
638  N N     . LYS A 89  ? 0.2341 0.0921 0.3271 0.0274  -0.0180 -0.0085 389 LYS A N     
639  C CA    . LYS A 89  ? 0.2486 0.0843 0.3278 0.0437  -0.0281 0.0007  389 LYS A CA    
640  C C     . LYS A 89  ? 0.2029 0.1037 0.3219 0.0270  -0.0275 -0.0006 389 LYS A C     
641  O O     . LYS A 89  ? 0.2084 0.1222 0.3370 0.0382  -0.0138 -0.0116 389 LYS A O     
642  C CB    . LYS A 89  ? 0.2206 0.1254 0.3705 0.0592  -0.0357 0.0007  389 LYS A CB    
643  C CG    . LYS A 89  ? 0.2035 0.2110 0.3982 0.0724  -0.0251 0.0073  389 LYS A CG    
644  C CD    . LYS A 89  ? 0.1762 0.3027 0.4544 0.0751  -0.0367 -0.0013 389 LYS A CD    
645  C CE    . LYS A 89  ? 0.2540 0.3872 0.4693 0.0429  -0.0579 0.0095  389 LYS A CE    
646  N NZ    . LYS A 89  ? 0.2311 0.4332 0.4630 0.0711  -0.0607 0.0320  389 LYS A NZ    
647  N N     . TYR A 90  ? 0.1850 0.0895 0.3198 0.0040  -0.0187 0.0029  390 TYR A N     
648  C CA    . TYR A 90  ? 0.1274 0.1385 0.2884 0.0044  -0.0027 0.0051  390 TYR A CA    
649  C C     . TYR A 90  ? 0.1258 0.1193 0.2840 0.0009  -0.0079 0.0119  390 TYR A C     
650  O O     . TYR A 90  ? 0.1419 0.1312 0.2980 -0.0076 0.0027  0.0027  390 TYR A O     
651  C CB    . TYR A 90  ? 0.1388 0.1574 0.2751 -0.0117 0.0070  -0.0059 390 TYR A CB    
652  C CG    . TYR A 90  ? 0.1454 0.1693 0.3339 0.0100  0.0135  0.0044  390 TYR A CG    
653  C CD1   . TYR A 90  ? 0.1468 0.2218 0.3746 0.0270  0.0231  -0.0178 390 TYR A CD1   
654  C CD2   . TYR A 90  ? 0.1870 0.1875 0.3537 0.0521  -0.0011 0.0012  390 TYR A CD2   
655  C CE1   . TYR A 90  ? 0.1896 0.2861 0.3949 0.0604  0.0561  -0.0197 390 TYR A CE1   
656  C CE2   . TYR A 90  ? 0.1694 0.2849 0.4217 0.0684  0.0097  -0.0005 390 TYR A CE2   
657  C CZ    . TYR A 90  ? 0.1635 0.3013 0.4302 0.0929  0.0319  -0.0004 390 TYR A CZ    
658  O OH    . TYR A 90  ? 0.1944 0.5511 0.5823 0.1309  0.0836  -0.0456 390 TYR A OH    
659  N N     . ILE A 91  ? 0.1295 0.0907 0.2844 0.0074  -0.0167 -0.0127 391 ILE A N     
660  C CA    . ILE A 91  ? 0.0895 0.1116 0.2892 0.0089  -0.0046 0.0007  391 ILE A CA    
661  C C     . ILE A 91  ? 0.1010 0.1174 0.2749 0.0085  -0.0146 -0.0062 391 ILE A C     
662  O O     . ILE A 91  ? 0.1295 0.1035 0.2871 0.0372  -0.0091 -0.0118 391 ILE A O     
663  C CB    . ILE A 91  ? 0.1118 0.0974 0.2976 -0.0027 -0.0073 -0.0107 391 ILE A CB    
664  C CG1   . ILE A 91  ? 0.1155 0.1315 0.3326 -0.0274 0.0034  0.0079  391 ILE A CG1   
665  C CG2   . ILE A 91  ? 0.0974 0.1325 0.3153 0.0027  0.0011  -0.0160 391 ILE A CG2   
666  C CD1   . ILE A 91  ? 0.1289 0.1591 0.3554 -0.0311 -0.0076 -0.0005 391 ILE A CD1   
667  N N     . TYR A 92  ? 0.0899 0.1161 0.2777 0.0193  -0.0100 -0.0126 392 TYR A N     
668  C CA    . TYR A 92  ? 0.1014 0.1410 0.2869 0.0043  -0.0097 0.0042  392 TYR A CA    
669  C C     . TYR A 92  ? 0.1056 0.1005 0.2876 -0.0046 -0.0003 0.0128  392 TYR A C     
670  O O     . TYR A 92  ? 0.0907 0.1357 0.3035 0.0051  -0.0031 0.0041  392 TYR A O     
671  C CB    . TYR A 92  ? 0.0623 0.1310 0.2934 0.0136  0.0084  -0.0051 392 TYR A CB    
672  C CG    . TYR A 92  ? 0.0653 0.1289 0.3001 0.0001  0.0044  0.0206  392 TYR A CG    
673  C CD1   . TYR A 92  ? 0.0775 0.1432 0.2936 0.0133  -0.0090 0.0141  392 TYR A CD1   
674  C CD2   . TYR A 92  ? 0.1185 0.1400 0.3022 -0.0066 -0.0153 0.0095  392 TYR A CD2   
675  C CE1   . TYR A 92  ? 0.0808 0.1059 0.2987 0.0173  -0.0159 0.0013  392 TYR A CE1   
676  C CE2   . TYR A 92  ? 0.1062 0.1133 0.3005 -0.0146 -0.0189 0.0130  392 TYR A CE2   
677  C CZ    . TYR A 92  ? 0.0745 0.1448 0.3025 -0.0162 -0.0055 0.0020  392 TYR A CZ    
678  O OH    . TYR A 92  ? 0.0781 0.1765 0.3322 -0.0243 -0.0152 -0.0020 392 TYR A OH    
679  N N     . HIS A 93  ? 0.0878 0.1164 0.2823 0.0111  0.0008  -0.0005 393 HIS A N     
680  C CA    . HIS A 93  ? 0.0784 0.1165 0.2849 0.0035  0.0009  0.0066  393 HIS A CA    
681  C C     . HIS A 93  ? 0.0978 0.1082 0.2762 0.0124  -0.0011 0.0002  393 HIS A C     
682  O O     . HIS A 93  ? 0.1361 0.1116 0.2831 0.0228  -0.0007 0.0005  393 HIS A O     
683  C CB    . HIS A 93  ? 0.0833 0.1207 0.2829 -0.0059 -0.0089 0.0114  393 HIS A CB    
684  C CG    . HIS A 93  ? 0.1144 0.1226 0.2908 0.0145  0.0054  0.0107  393 HIS A CG    
685  N ND1   . HIS A 93  ? 0.1150 0.1108 0.3004 -0.0088 -0.0104 0.0213  393 HIS A ND1   
686  C CD2   . HIS A 93  ? 0.0943 0.1062 0.3047 0.0037  0.0053  0.0222  393 HIS A CD2   
687  C CE1   . HIS A 93  ? 0.1310 0.1191 0.3140 -0.0144 -0.0026 0.0149  393 HIS A CE1   
688  N NE2   . HIS A 93  ? 0.1490 0.0924 0.2972 -0.0253 -0.0106 0.0058  393 HIS A NE2   
689  N N     . VAL A 94  ? 0.1052 0.1278 0.2858 -0.0003 0.0119  0.0108  394 VAL A N     
690  C CA    . VAL A 94  ? 0.1185 0.1172 0.2837 -0.0084 -0.0058 0.0126  394 VAL A CA    
691  C C     . VAL A 94  ? 0.0907 0.1360 0.2851 -0.0080 -0.0021 -0.0155 394 VAL A C     
692  O O     . VAL A 94  ? 0.0942 0.1479 0.3081 0.0005  0.0025  0.0064  394 VAL A O     
693  C CB    . VAL A 94  ? 0.0963 0.0984 0.3084 -0.0155 0.0000  -0.0042 394 VAL A CB    
694  C CG1   . VAL A 94  ? 0.0906 0.1106 0.3277 0.0202  0.0104  -0.0201 394 VAL A CG1   
695  C CG2   . VAL A 94  ? 0.1372 0.1116 0.3018 -0.0119 -0.0042 -0.0216 394 VAL A CG2   
696  N N     . LEU A 95  ? 0.0947 0.1096 0.2800 0.0021  -0.0148 0.0070  395 LEU A N     
697  C CA    . LEU A 95  ? 0.1217 0.0936 0.2877 0.0083  -0.0223 0.0123  395 LEU A CA    
698  C C     . LEU A 95  ? 0.1066 0.1070 0.2897 0.0068  -0.0190 0.0090  395 LEU A C     
699  O O     . LEU A 95  ? 0.1050 0.1224 0.3281 -0.0056 -0.0177 0.0106  395 LEU A O     
700  C CB    . LEU A 95  ? 0.1429 0.0935 0.2880 0.0020  -0.0243 0.0167  395 LEU A CB    
701  C CG    . LEU A 95  ? 0.1425 0.1140 0.2948 0.0124  -0.0254 0.0205  395 LEU A CG    
702  C CD1   . LEU A 95  ? 0.1619 0.0972 0.3203 0.0071  -0.0157 0.0194  395 LEU A CD1   
703  C CD2   . LEU A 95  ? 0.1101 0.1042 0.3115 0.0142  -0.0227 0.0183  395 LEU A CD2   
704  N N     . TRP A 96  ? 0.1009 0.1262 0.3050 0.0014  -0.0090 0.0204  396 TRP A N     
705  C CA    . TRP A 96  ? 0.1298 0.1292 0.3039 0.0102  -0.0023 0.0193  396 TRP A CA    
706  C C     . TRP A 96  ? 0.1313 0.1772 0.3028 0.0118  -0.0098 0.0055  396 TRP A C     
707  O O     . TRP A 96  ? 0.1171 0.1831 0.3350 0.0177  -0.0332 -0.0198 396 TRP A O     
708  C CB    . TRP A 96  ? 0.1436 0.1252 0.3069 0.0245  0.0034  0.0160  396 TRP A CB    
709  C CG    . TRP A 96  ? 0.1344 0.1437 0.2933 0.0146  0.0105  -0.0142 396 TRP A CG    
710  C CD1   . TRP A 96  ? 0.1374 0.1529 0.3108 0.0242  -0.0036 0.0010  396 TRP A CD1   
711  C CD2   . TRP A 96  ? 0.1160 0.1306 0.3060 0.0130  0.0269  -0.0076 396 TRP A CD2   
712  N NE1   . TRP A 96  ? 0.1600 0.1333 0.3073 0.0202  0.0096  0.0215  396 TRP A NE1   
713  C CE2   . TRP A 96  ? 0.1318 0.1331 0.3159 0.0312  0.0193  0.0014  396 TRP A CE2   
714  C CE3   . TRP A 96  ? 0.1634 0.1378 0.3244 0.0250  0.0136  0.0127  396 TRP A CE3   
715  C CZ2   . TRP A 96  ? 0.1713 0.1715 0.3075 0.0193  0.0121  -0.0044 396 TRP A CZ2   
716  C CZ3   . TRP A 96  ? 0.1682 0.1344 0.3403 0.0363  0.0206  -0.0036 396 TRP A CZ3   
717  C CH2   . TRP A 96  ? 0.2035 0.1734 0.3191 0.0164  0.0112  -0.0189 396 TRP A CH2   
718  N N     . HIS A 97  ? 0.1820 0.1549 0.3375 0.0253  -0.0295 0.0191  397 HIS A N     
719  C CA    . HIS A 97  ? 0.2361 0.1726 0.3311 0.0096  -0.0392 0.0212  397 HIS A CA    
720  C C     . HIS A 97  ? 0.3534 0.1843 0.3485 0.0476  -0.0063 0.0305  397 HIS A C     
721  O O     . HIS A 97  ? 0.5536 0.1989 0.3940 0.0884  0.0440  0.0678  397 HIS A O     
722  C CB    . HIS A 97  ? 0.1986 0.1851 0.3017 -0.0081 -0.0337 0.0204  397 HIS A CB    
723  C CG    . HIS A 97  ? 0.1968 0.1296 0.3360 -0.0289 -0.0079 0.0479  397 HIS A CG    
724  N ND1   . HIS A 97  ? 0.1360 0.3287 0.3916 -0.0261 -0.0127 0.0649  397 HIS A ND1   
725  C CD2   . HIS A 97  ? 0.1797 0.1654 0.2867 -0.0158 0.0162  0.0254  397 HIS A CD2   
726  C CE1   . HIS A 97  ? 0.1045 0.3549 0.3800 -0.0609 0.0467  0.0912  397 HIS A CE1   
727  N NE2   . HIS A 97  ? 0.1921 0.2618 0.3465 -0.0555 0.0446  0.0623  397 HIS A NE2   
728  N N     . SER A 98  ? 0.2452 0.1744 0.3767 0.0603  0.0175  0.0116  398 SER A N     
729  C CA    . SER A 98  ? 0.3296 0.2312 0.3919 0.0353  0.0012  0.0242  398 SER A CA    
730  C C     . SER A 98  ? 0.3414 0.1612 0.4103 0.0422  -0.0306 -0.0079 398 SER A C     
731  O O     . SER A 98  ? 0.2563 0.2109 0.4709 0.0566  0.0152  -0.0236 398 SER A O     
732  C CB    . SER A 98  ? 0.3406 0.1756 0.4258 0.0255  -0.0074 -0.0040 398 SER A CB    
733  O OG    . SER A 98  ? 0.3408 0.3321 0.3656 0.0730  0.0042  -0.0678 398 SER A OG    
734  N N     . GLU A 99  ? 0.4288 0.1523 0.4213 0.0757  -0.0635 -0.0253 399 GLU A N     
735  C CA    . GLU A 99  ? 0.3324 0.2522 0.4610 0.1229  -0.1177 -0.0468 399 GLU A CA    
736  C C     . GLU A 99  ? 0.2544 0.2003 0.4153 0.0882  -0.0917 -0.0043 399 GLU A C     
737  O O     . GLU A 99  ? 0.2278 0.2040 0.4926 0.0840  -0.0702 -0.0053 399 GLU A O     
738  C CB    . GLU A 99  ? 0.4351 0.4005 0.5097 0.1363  -0.1564 -0.0421 399 GLU A CB    
739  C CG    . GLU A 99  ? 0.4473 0.5446 0.6253 0.0980  -0.1922 -0.0362 399 GLU A CG    
740  C CD    . GLU A 99  ? 0.5300 0.6786 0.6957 0.0834  -0.1723 0.0133  399 GLU A CD    
741  O OE1   . GLU A 99  ? 0.5866 0.7999 0.6636 0.1146  -0.2121 -0.0079 399 GLU A OE1   
742  O OE2   . GLU A 99  ? 0.5484 0.7258 0.8192 0.2180  -0.1830 0.0546  399 GLU A OE2   
743  N N     . PHE A 100 ? 0.2270 0.2073 0.3259 0.1096  -0.0281 -0.0261 400 PHE A N     
744  C CA    . PHE A 100 ? 0.1984 0.1800 0.3168 0.0857  -0.0011 -0.0015 400 PHE A CA    
745  C C     . PHE A 100 ? 0.1877 0.2010 0.3127 0.0570  -0.0081 0.0093  400 PHE A C     
746  O O     . PHE A 100 ? 0.1608 0.2074 0.3165 0.0433  -0.0148 0.0101  400 PHE A O     
747  C CB    . PHE A 100 ? 0.1995 0.2413 0.3352 0.0767  -0.0140 0.0045  400 PHE A CB    
748  C CG    . PHE A 100 ? 0.1877 0.3226 0.3451 0.0407  0.0014  -0.0142 400 PHE A CG    
749  C CD1   . PHE A 100 ? 0.2565 0.3258 0.3431 -0.0101 0.0201  -0.0381 400 PHE A CD1   
750  C CD2   . PHE A 100 ? 0.1824 0.4087 0.3729 0.0318  0.0141  -0.0364 400 PHE A CD2   
751  C CE1   . PHE A 100 ? 0.2699 0.3619 0.3896 -0.0360 0.0617  -0.0244 400 PHE A CE1   
752  C CE2   . PHE A 100 ? 0.2154 0.3714 0.3746 -0.0172 0.0232  -0.0198 400 PHE A CE2   
753  C CZ    . PHE A 100 ? 0.2740 0.3240 0.3656 -0.0519 0.0756  -0.0359 400 PHE A CZ    
754  N N     . PRO A 101 ? 0.1996 0.1759 0.3204 0.0552  -0.0171 0.0151  401 PRO A N     
755  C CA    . PRO A 101 ? 0.1700 0.1675 0.3257 0.0407  -0.0049 0.0013  401 PRO A CA    
756  C C     . PRO A 101 ? 0.1561 0.1724 0.3086 0.0306  -0.0022 0.0162  401 PRO A C     
757  O O     . PRO A 101 ? 0.1542 0.1432 0.3322 0.0402  0.0074  0.0042  401 PRO A O     
758  C CB    . PRO A 101 ? 0.2523 0.1770 0.3364 0.0559  -0.0026 -0.0097 401 PRO A CB    
759  C CG    . PRO A 101 ? 0.2773 0.1634 0.3597 0.0699  -0.0081 0.0186  401 PRO A CG    
760  C CD    . PRO A 101 ? 0.2267 0.1873 0.3334 0.0719  -0.0086 0.0263  401 PRO A CD    
761  N N     . LYS A 102 ? 0.1552 0.1587 0.3274 0.0281  0.0165  0.0072  402 LYS A N     
762  C CA    . LYS A 102 ? 0.1451 0.1774 0.3285 0.0297  -0.0111 0.0176  402 LYS A CA    
763  C C     . LYS A 102 ? 0.1128 0.1656 0.2876 0.0377  0.0082  0.0085  402 LYS A C     
764  O O     . LYS A 102 ? 0.1271 0.1442 0.3252 0.0377  -0.0126 0.0199  402 LYS A O     
765  C CB    . LYS A 102 ? 0.1404 0.1856 0.3472 0.0078  -0.0005 0.0309  402 LYS A CB    
766  C CG    . LYS A 102 ? 0.1956 0.2658 0.3907 -0.0150 -0.0377 0.0376  402 LYS A CG    
767  C CD    . LYS A 102 ? 0.1788 0.2703 0.4129 -0.0111 -0.0351 0.0335  402 LYS A CD    
768  C CE    . LYS A 102 ? 0.2628 0.4247 0.4514 0.0114  -0.0558 0.0076  402 LYS A CE    
769  N NZ    . LYS A 102 ? 0.1941 0.4292 0.4485 0.0098  -0.0333 -0.0138 402 LYS A NZ    
770  N N     . PRO A 103 ? 0.1647 0.1772 0.2978 0.0583  0.0056  0.0016  403 PRO A N     
771  C CA    . PRO A 103 ? 0.1454 0.1618 0.2818 0.0501  0.0006  0.0032  403 PRO A CA    
772  C C     . PRO A 103 ? 0.1207 0.1698 0.2796 0.0237  -0.0020 0.0122  403 PRO A C     
773  O O     . PRO A 103 ? 0.1573 0.1561 0.2946 0.0261  -0.0152 0.0139  403 PRO A O     
774  C CB    . PRO A 103 ? 0.1801 0.1834 0.3061 0.0669  0.0005  -0.0107 403 PRO A CB    
775  C CG    . PRO A 103 ? 0.1899 0.1738 0.3188 0.0752  0.0197  -0.0077 403 PRO A CG    
776  C CD    . PRO A 103 ? 0.1341 0.2125 0.2951 0.0594  0.0060  -0.0091 403 PRO A CD    
777  N N     . GLN A 104 ? 0.1342 0.1545 0.2856 0.0356  -0.0087 -0.0010 404 GLN A N     
778  C CA    . GLN A 104 ? 0.1308 0.1214 0.3017 0.0355  0.0044  0.0097  404 GLN A CA    
779  C C     . GLN A 104 ? 0.1441 0.1078 0.3022 0.0440  -0.0144 0.0127  404 GLN A C     
780  O O     . GLN A 104 ? 0.1247 0.1162 0.3169 0.0319  0.0048  0.0047  404 GLN A O     
781  C CB    . GLN A 104 ? 0.1666 0.1184 0.3248 0.0120  0.0258  0.0158  404 GLN A CB    
782  C CG    . GLN A 104 ? 0.1996 0.1119 0.3463 0.0284  0.0285  0.0074  404 GLN A CG    
783  C CD    . GLN A 104 ? 0.2570 0.1430 0.3439 0.0603  0.0374  0.0144  404 GLN A CD    
784  O OE1   . GLN A 104 ? 0.2480 0.1952 0.4153 0.0758  0.0451  -0.0069 404 GLN A OE1   
785  N NE2   . GLN A 104 ? 0.2587 0.1306 0.3229 0.0800  0.0356  0.0431  404 GLN A NE2   
786  N N     . ILE A 105 ? 0.1212 0.1385 0.3089 0.0345  -0.0061 -0.0116 405 ILE A N     
787  C CA    . ILE A 105 ? 0.1294 0.1388 0.2953 0.0238  -0.0042 0.0081  405 ILE A CA    
788  C C     . ILE A 105 ? 0.1106 0.1416 0.2907 0.0218  -0.0130 -0.0066 405 ILE A C     
789  O O     . ILE A 105 ? 0.1107 0.1562 0.3126 0.0365  -0.0003 0.0090  405 ILE A O     
790  C CB    . ILE A 105 ? 0.1186 0.1345 0.3118 0.0324  -0.0182 0.0083  405 ILE A CB    
791  C CG1   . ILE A 105 ? 0.1311 0.1526 0.3336 0.0682  -0.0299 0.0100  405 ILE A CG1   
792  C CG2   . ILE A 105 ? 0.1366 0.1512 0.3089 0.0452  -0.0082 -0.0023 405 ILE A CG2   
793  C CD1   . ILE A 105 ? 0.1507 0.1867 0.3352 0.0516  -0.0253 0.0214  405 ILE A CD1   
794  N N     . LEU A 106 ? 0.1186 0.1263 0.2983 0.0313  -0.0008 -0.0108 406 LEU A N     
795  C CA    . LEU A 106 ? 0.1362 0.1445 0.2802 0.0019  0.0044  -0.0018 406 LEU A CA    
796  C C     . LEU A 106 ? 0.1466 0.1285 0.2814 0.0021  -0.0105 -0.0069 406 LEU A C     
797  O O     . LEU A 106 ? 0.1617 0.1621 0.2890 0.0335  -0.0113 0.0092  406 LEU A O     
798  C CB    . LEU A 106 ? 0.1365 0.1221 0.2998 -0.0017 0.0132  0.0089  406 LEU A CB    
799  C CG    . LEU A 106 ? 0.1419 0.1171 0.2991 -0.0106 0.0137  0.0088  406 LEU A CG    
800  C CD1   . LEU A 106 ? 0.1694 0.1159 0.3240 -0.0177 0.0005  0.0201  406 LEU A CD1   
801  C CD2   . LEU A 106 ? 0.2108 0.1685 0.3137 0.0242  0.0234  -0.0057 406 LEU A CD2   
802  N N     . LYS A 107 ? 0.1312 0.1062 0.2875 0.0173  -0.0187 0.0028  407 LYS A N     
803  C CA    . LYS A 107 ? 0.1245 0.1213 0.2822 0.0157  -0.0028 -0.0024 407 LYS A CA    
804  C C     . LYS A 107 ? 0.1298 0.1359 0.2701 0.0188  -0.0116 -0.0055 407 LYS A C     
805  O O     . LYS A 107 ? 0.1283 0.1299 0.2946 -0.0058 -0.0232 0.0143  407 LYS A O     
806  C CB    . LYS A 107 ? 0.1321 0.1188 0.3240 0.0281  -0.0155 0.0114  407 LYS A CB    
807  C CG    . LYS A 107 ? 0.1541 0.1372 0.3523 0.0183  -0.0167 0.0122  407 LYS A CG    
808  C CD    . LYS A 107 ? 0.2339 0.1661 0.4071 0.0247  -0.0248 0.0261  407 LYS A CD    
809  C CE    . LYS A 107 ? 0.2680 0.2025 0.4472 0.0148  -0.0567 0.0055  407 LYS A CE    
810  N NZ    . LYS A 107 ? 0.2952 0.2764 0.4663 0.0322  -0.0557 0.0000  407 LYS A NZ    
811  N N     . HIS A 108 ? 0.1387 0.1138 0.2701 0.0128  -0.0092 0.0004  408 HIS A N     
812  C CA    . HIS A 108 ? 0.1283 0.1111 0.2781 0.0250  0.0073  0.0027  408 HIS A CA    
813  C C     . HIS A 108 ? 0.1295 0.1162 0.2735 0.0187  -0.0128 0.0112  408 HIS A C     
814  O O     . HIS A 108 ? 0.1309 0.1247 0.3015 0.0360  0.0036  0.0086  408 HIS A O     
815  C CB    . HIS A 108 ? 0.1449 0.1212 0.2777 0.0290  0.0273  0.0069  408 HIS A CB    
816  C CG    . HIS A 108 ? 0.1689 0.1256 0.3081 0.0364  0.0105  0.0204  408 HIS A CG    
817  N ND1   . HIS A 108 ? 0.2316 0.1176 0.3406 0.0077  -0.0130 0.0282  408 HIS A ND1   
818  C CD2   . HIS A 108 ? 0.1771 0.1429 0.3100 0.0491  0.0075  0.0108  408 HIS A CD2   
819  C CE1   . HIS A 108 ? 0.2335 0.1096 0.3506 0.0128  -0.0250 0.0204  408 HIS A CE1   
820  N NE2   . HIS A 108 ? 0.2337 0.1324 0.3195 0.0438  -0.0165 0.0191  408 HIS A NE2   
821  N N     . ALA A 109 ? 0.0977 0.1033 0.3008 0.0329  -0.0011 0.0000  409 ALA A N     
822  C CA    . ALA A 109 ? 0.0973 0.0907 0.3128 0.0222  -0.0123 0.0011  409 ALA A CA    
823  C C     . ALA A 109 ? 0.1113 0.1080 0.3085 0.0077  0.0046  0.0097  409 ALA A C     
824  O O     . ALA A 109 ? 0.1362 0.0840 0.3211 0.0134  -0.0025 0.0129  409 ALA A O     
825  C CB    . ALA A 109 ? 0.1014 0.1153 0.3498 0.0225  -0.0156 0.0149  409 ALA A CB    
826  N N     . MET A 110 ? 0.1249 0.1279 0.3112 -0.0093 0.0076  0.0008  410 MET A N     
827  C CA    . MET A 110 ? 0.1506 0.1169 0.3158 0.0037  0.0144  0.0047  410 MET A CA    
828  C C     . MET A 110 ? 0.1471 0.0772 0.3062 0.0044  -0.0122 0.0015  410 MET A C     
829  O O     . MET A 110 ? 0.1516 0.1172 0.3115 0.0172  -0.0053 0.0287  410 MET A O     
830  C CB    . MET A 110 ? 0.1645 0.1249 0.3602 0.0134  0.0241  -0.0143 410 MET A CB    
831  C CG    . MET A 110 ? 0.2063 0.1314 0.3885 0.0356  0.0307  -0.0210 410 MET A CG    
832  S SD    . MET A 110 ? 0.3134 0.1353 0.3748 0.0148  0.0437  0.0027  410 MET A SD    
833  C CE    . MET A 110 ? 0.2298 0.0545 0.5036 -0.0261 0.0855  -0.0286 410 MET A CE    
834  N N     . LYS A 111 ? 0.1148 0.0896 0.3145 0.0109  -0.0207 0.0138  411 LYS A N     
835  C CA    . LYS A 111 ? 0.1153 0.0809 0.3249 -0.0075 -0.0124 -0.0100 411 LYS A CA    
836  C C     . LYS A 111 ? 0.1153 0.0855 0.3277 0.0271  -0.0221 0.0037  411 LYS A C     
837  O O     . LYS A 111 ? 0.1123 0.1426 0.3528 0.0379  -0.0376 0.0084  411 LYS A O     
838  C CB    . LYS A 111 ? 0.1463 0.0780 0.3676 -0.0142 -0.0080 -0.0096 411 LYS A CB    
839  C CG    . LYS A 111 ? 0.1616 0.1386 0.4163 -0.0079 0.0038  0.0083  411 LYS A CG    
840  C CD    . LYS A 111 ? 0.1889 0.1809 0.4581 -0.0432 0.0001  0.0058  411 LYS A CD    
841  C CE    . LYS A 111 ? 0.2003 0.2896 0.5378 -0.0357 0.0024  0.0130  411 LYS A CE    
842  N NZ    . LYS A 111 ? 0.3017 0.2673 0.5438 0.0265  0.0040  0.0152  411 LYS A NZ    
843  N N     . GLU A 112 ? 0.1176 0.0804 0.3091 0.0002  0.0062  0.0094  412 GLU A N     
844  C CA    . GLU A 112 ? 0.1473 0.1032 0.3023 -0.0011 0.0213  0.0020  412 GLU A CA    
845  C C     . GLU A 112 ? 0.1203 0.0937 0.2915 0.0246  0.0224  0.0017  412 GLU A C     
846  O O     . GLU A 112 ? 0.1264 0.1342 0.3291 0.0441  0.0145  -0.0004 412 GLU A O     
852  N N     . CYS A 113 ? 0.1008 0.1033 0.2963 0.0118  0.0095  0.0161  413 CYS A N     
853  C CA    . CYS A 113 ? 0.0887 0.0993 0.3064 0.0039  -0.0011 0.0123  413 CYS A CA    
854  C C     . CYS A 113 ? 0.1048 0.1175 0.3103 0.0093  -0.0106 -0.0032 413 CYS A C     
855  O O     . CYS A 113 ? 0.1351 0.1342 0.3224 0.0280  -0.0381 0.0088  413 CYS A O     
856  C CB    . CYS A 113 ? 0.0729 0.0585 0.3256 0.0273  0.0029  0.0353  413 CYS A CB    
857  S SG    . CYS A 113 ? 0.1078 0.1335 0.3264 0.0001  -0.0094 0.0054  413 CYS A SG    
858  N N     . LEU A 114 ? 0.0920 0.1126 0.3310 0.0053  -0.0198 -0.0138 414 LEU A N     
859  C CA    . LEU A 114 ? 0.0979 0.1046 0.3387 0.0192  -0.0204 -0.0159 414 LEU A CA    
860  C C     . LEU A 114 ? 0.1367 0.1424 0.3141 0.0173  -0.0206 -0.0074 414 LEU A C     
861  O O     . LEU A 114 ? 0.1490 0.1189 0.3451 0.0269  -0.0193 0.0027  414 LEU A O     
862  C CB    . LEU A 114 ? 0.1263 0.0854 0.3454 -0.0111 -0.0218 -0.0135 414 LEU A CB    
863  C CG    . LEU A 114 ? 0.1448 0.1042 0.3299 0.0128  -0.0217 -0.0046 414 LEU A CG    
864  C CD1   . LEU A 114 ? 0.1671 0.1076 0.3394 0.0127  0.0036  -0.0075 414 LEU A CD1   
865  C CD2   . LEU A 114 ? 0.1911 0.1493 0.3248 0.0275  -0.0142 0.0062  414 LEU A CD2   
866  N N     . GLU A 115 ? 0.1152 0.1247 0.3242 0.0279  -0.0141 -0.0006 415 GLU A N     
867  C CA    . GLU A 115 ? 0.0948 0.1222 0.3484 0.0112  0.0080  0.0139  415 GLU A CA    
868  C C     . GLU A 115 ? 0.1246 0.1422 0.3384 0.0216  0.0156  0.0155  415 GLU A C     
869  O O     . GLU A 115 ? 0.1029 0.1629 0.3685 0.0113  0.0197  0.0261  415 GLU A O     
870  C CB    . GLU A 115 ? 0.1062 0.1647 0.3724 0.0167  0.0148  0.0125  415 GLU A CB    
871  C CG    . GLU A 115 ? 0.1254 0.1768 0.4261 0.0091  0.0301  0.0215  415 GLU A CG    
872  C CD    . GLU A 115 ? 0.1281 0.2084 0.4680 0.0016  0.0430  0.0066  415 GLU A CD    
873  O OE1   . GLU A 115 ? 0.1788 0.3881 0.5212 -0.0199 0.0937  0.0080  415 GLU A OE1   
874  O OE2   . GLU A 115 ? 0.2195 0.3937 0.4776 0.0254  0.0520  -0.0467 415 GLU A OE2   
875  N N     A LYS A 116 ? 0.1049 0.1158 0.3197 0.0220  0.0158  0.0246  416 LYS A N     
876  N N     B LYS A 116 ? 0.1291 0.1238 0.3475 0.0164  0.0163  0.0251  416 LYS A N     
877  C CA    A LYS A 116 ? 0.0850 0.1282 0.2951 0.0232  0.0158  0.0114  416 LYS A CA    
878  C CA    B LYS A 116 ? 0.1533 0.1444 0.3406 0.0336  0.0209  0.0111  416 LYS A CA    
879  C C     A LYS A 116 ? 0.0971 0.1205 0.3007 0.0313  0.0185  0.0094  416 LYS A C     
880  C C     B LYS A 116 ? 0.1252 0.1287 0.3266 0.0381  0.0243  -0.0015 416 LYS A C     
881  O O     A LYS A 116 ? 0.1266 0.1070 0.3085 0.0254  0.0247  -0.0009 416 LYS A O     
882  O O     B LYS A 116 ? 0.1113 0.1150 0.3458 0.0172  0.0364  -0.0243 416 LYS A O     
883  C CB    A LYS A 116 ? 0.0695 0.1421 0.3023 0.0185  0.0198  0.0161  416 LYS A CB    
884  C CB    B LYS A 116 ? 0.1761 0.2067 0.3904 0.0211  0.0204  0.0096  416 LYS A CB    
885  C CG    A LYS A 116 ? 0.0736 0.1750 0.3057 -0.0002 0.0182  -0.0138 416 LYS A CG    
886  C CG    B LYS A 116 ? 0.2621 0.2741 0.4266 0.0195  0.0169  -0.0006 416 LYS A CG    
887  C CD    A LYS A 116 ? 0.0759 0.1777 0.3290 -0.0061 0.0092  -0.0173 416 LYS A CD    
888  C CD    B LYS A 116 ? 0.3061 0.3405 0.4608 0.0173  0.0340  0.0022  416 LYS A CD    
889  C CE    A LYS A 116 ? 0.1641 0.1840 0.3699 0.0057  0.0038  -0.0006 416 LYS A CE    
890  C CE    B LYS A 116 ? 0.2707 0.3326 0.4923 0.0282  0.0335  -0.0024 416 LYS A CE    
891  N NZ    A LYS A 116 ? 0.1896 0.2028 0.3866 -0.0098 0.0099  0.0051  416 LYS A NZ    
892  N NZ    B LYS A 116 ? 0.2505 0.2937 0.4846 0.0076  0.0481  0.0194  416 LYS A NZ    
893  N N     . CYS A 117 ? 0.1373 0.1324 0.3080 0.0460  0.0116  0.0062  417 CYS A N     
894  C CA    . CYS A 117 ? 0.1505 0.1368 0.3015 0.0279  -0.0113 -0.0033 417 CYS A CA    
895  C C     . CYS A 117 ? 0.1613 0.1658 0.3136 0.0175  -0.0005 0.0049  417 CYS A C     
896  O O     . CYS A 117 ? 0.1196 0.1893 0.3504 0.0354  0.0242  0.0256  417 CYS A O     
897  C CB    . CYS A 117 ? 0.0948 0.1968 0.3213 0.0292  -0.0088 -0.0084 417 CYS A CB    
898  S SG    . CYS A 117 ? 0.1372 0.1603 0.3219 0.0227  0.0135  0.0176  417 CYS A SG    
899  N N     . ILE A 118 ? 0.1049 0.1457 0.3360 0.0206  -0.0080 0.0134  418 ILE A N     
900  C CA    . ILE A 118 ? 0.0991 0.1632 0.3365 -0.0082 -0.0069 0.0065  418 ILE A CA    
901  C C     . ILE A 118 ? 0.1044 0.1972 0.3425 0.0196  -0.0061 -0.0031 418 ILE A C     
902  O O     . ILE A 118 ? 0.1208 0.1791 0.3428 0.0379  0.0063  -0.0057 418 ILE A O     
903  C CB    . ILE A 118 ? 0.1281 0.1883 0.3488 -0.0106 0.0041  0.0212  418 ILE A CB    
904  C CG1   . ILE A 118 ? 0.0907 0.1998 0.3912 -0.0053 -0.0028 -0.0095 418 ILE A CG1   
905  C CG2   . ILE A 118 ? 0.1471 0.1823 0.3682 -0.0151 0.0141  0.0335  418 ILE A CG2   
906  C CD1   . ILE A 118 ? 0.1990 0.1739 0.4236 0.0023  0.0081  0.0050  418 ILE A CD1   
907  N N     . GLU A 119 ? 0.1300 0.2068 0.3269 0.0114  -0.0133 0.0012  419 GLU A N     
908  C CA    . GLU A 119 ? 0.1142 0.2042 0.3393 0.0191  -0.0007 0.0079  419 GLU A CA    
909  C C     . GLU A 119 ? 0.1336 0.1943 0.3238 0.0227  0.0199  0.0042  419 GLU A C     
910  O O     . GLU A 119 ? 0.1461 0.2119 0.3636 0.0446  0.0298  -0.0001 419 GLU A O     
911  C CB    . GLU A 119 ? 0.1624 0.2265 0.3422 0.0260  -0.0013 0.0182  419 GLU A CB    
912  C CG    . GLU A 119 ? 0.1864 0.2634 0.3353 0.0174  0.0056  0.0129  419 GLU A CG    
913  C CD    . GLU A 119 ? 0.1729 0.3263 0.3882 0.0733  -0.0116 -0.0027 419 GLU A CD    
914  O OE1   . GLU A 119 ? 0.3287 0.3742 0.4485 0.1423  -0.0518 0.0110  419 GLU A OE1   
915  O OE2   . GLU A 119 ? 0.3081 0.4108 0.3801 0.0117  -0.0123 0.0206  419 GLU A OE2   
916  N N     . GLN A 120 ? 0.1149 0.1594 0.3284 0.0224  0.0167  -0.0022 420 GLN A N     
917  C CA    . GLN A 120 ? 0.1091 0.1641 0.3094 0.0079  0.0134  -0.0219 420 GLN A CA    
918  C C     . GLN A 120 ? 0.0982 0.1632 0.3309 0.0211  0.0076  0.0044  420 GLN A C     
919  O O     . GLN A 120 ? 0.1471 0.1494 0.3388 0.0012  -0.0035 -0.0051 420 GLN A O     
920  C CB    . GLN A 120 ? 0.1081 0.1806 0.3223 0.0112  0.0096  -0.0159 420 GLN A CB    
921  C CG    . GLN A 120 ? 0.1259 0.2092 0.3460 0.0042  -0.0015 -0.0485 420 GLN A CG    
922  C CD    . GLN A 120 ? 0.1172 0.2090 0.3985 -0.0003 0.0015  -0.0565 420 GLN A CD    
923  O OE1   . GLN A 120 ? 0.1750 0.2777 0.4327 0.0459  0.0115  -0.0649 420 GLN A OE1   
924  N NE2   . GLN A 120 ? 0.2045 0.3267 0.4658 -0.0064 -0.0059 -0.1224 420 GLN A NE2   
925  N N     . ASN A 121 ? 0.1162 0.1590 0.3211 0.0280  0.0131  0.0073  421 ASN A N     
926  C CA    . ASN A 121 ? 0.1276 0.1864 0.3036 0.0272  0.0116  -0.0069 421 ASN A CA    
927  C C     . ASN A 121 ? 0.1336 0.1705 0.2991 0.0204  0.0014  0.0011  421 ASN A C     
928  O O     . ASN A 121 ? 0.1251 0.1791 0.3481 0.0387  0.0210  0.0307  421 ASN A O     
929  C CB    . ASN A 121 ? 0.1414 0.1860 0.3139 0.0303  0.0196  -0.0061 421 ASN A CB    
930  C CG    . ASN A 121 ? 0.1557 0.2023 0.3275 0.0298  -0.0066 0.0018  421 ASN A CG    
931  O OD1   . ASN A 121 ? 0.2307 0.2982 0.3617 0.0703  -0.0549 -0.0442 421 ASN A OD1   
932  N ND2   . ASN A 121 ? 0.1159 0.2301 0.3357 0.0145  0.0126  0.0365  421 ASN A ND2   
933  N N     . ILE A 122 ? 0.1183 0.1459 0.2964 0.0108  0.0112  0.0086  422 ILE A N     
934  C CA    . ILE A 122 ? 0.0957 0.1360 0.3088 0.0107  0.0071  0.0135  422 ILE A CA    
935  C C     . ILE A 122 ? 0.0983 0.1178 0.3021 0.0118  -0.0031 0.0071  422 ILE A C     
936  O O     . ILE A 122 ? 0.1410 0.0924 0.3265 -0.0029 0.0011  -0.0040 422 ILE A O     
937  C CB    . ILE A 122 ? 0.0944 0.1668 0.3083 0.0213  0.0015  0.0118  422 ILE A CB    
938  C CG1   . ILE A 122 ? 0.0758 0.1783 0.3136 -0.0085 0.0057  0.0124  422 ILE A CG1   
939  C CG2   . ILE A 122 ? 0.1231 0.1463 0.3024 0.0266  0.0113  0.0113  422 ILE A CG2   
940  C CD1   . ILE A 122 ? 0.0814 0.1855 0.3144 -0.0086 0.0028  0.0016  422 ILE A CD1   
941  N N     . THR A 123 ? 0.1176 0.1304 0.2903 0.0226  0.0082  -0.0002 423 THR A N     
942  C CA    . THR A 123 ? 0.1178 0.1336 0.2878 0.0227  0.0077  0.0122  423 THR A CA    
943  C C     . THR A 123 ? 0.0940 0.1494 0.2618 0.0012  -0.0081 0.0250  423 THR A C     
944  O O     . THR A 123 ? 0.1058 0.1664 0.2773 0.0051  -0.0095 -0.0075 423 THR A O     
945  C CB    . THR A 123 ? 0.1325 0.1551 0.3138 0.0362  -0.0099 0.0063  423 THR A CB    
946  O OG1   . THR A 123 ? 0.1574 0.1658 0.3528 0.0381  -0.0036 0.0354  423 THR A OG1   
947  C CG2   . THR A 123 ? 0.1341 0.1293 0.3335 0.0252  -0.0156 -0.0040 423 THR A CG2   
948  N N     . SER A 124 ? 0.0958 0.1514 0.2750 -0.0005 -0.0114 0.0035  424 SER A N     
949  C CA    . SER A 124 ? 0.1200 0.1254 0.2733 -0.0048 -0.0040 0.0000  424 SER A CA    
950  C C     . SER A 124 ? 0.1069 0.1541 0.2673 0.0147  -0.0089 -0.0072 424 SER A C     
951  O O     . SER A 124 ? 0.1247 0.1477 0.2930 0.0311  -0.0200 -0.0085 424 SER A O     
952  C CB    . SER A 124 ? 0.1024 0.1533 0.2839 0.0086  -0.0101 0.0109  424 SER A CB    
953  O OG    . SER A 124 ? 0.1407 0.1449 0.3069 -0.0018 -0.0260 -0.0077 424 SER A OG    
954  N N     . ILE A 125 ? 0.1235 0.1297 0.2638 0.0001  -0.0091 -0.0126 425 ILE A N     
955  C CA    . ILE A 125 ? 0.1217 0.1344 0.2649 0.0217  -0.0020 0.0039  425 ILE A CA    
956  C C     . ILE A 125 ? 0.1063 0.1376 0.2635 0.0094  -0.0165 -0.0015 425 ILE A C     
957  O O     . ILE A 125 ? 0.1109 0.1518 0.2708 0.0017  -0.0104 -0.0172 425 ILE A O     
958  C CB    . ILE A 125 ? 0.1159 0.1129 0.2783 0.0124  -0.0030 -0.0033 425 ILE A CB    
959  C CG1   . ILE A 125 ? 0.1170 0.1113 0.2879 0.0099  -0.0048 0.0001  425 ILE A CG1   
960  C CG2   . ILE A 125 ? 0.1224 0.1111 0.2908 0.0099  -0.0110 0.0021  425 ILE A CG2   
961  C CD1   . ILE A 125 ? 0.1266 0.1202 0.2953 0.0078  -0.0043 -0.0011 425 ILE A CD1   
962  N N     . SER A 126 ? 0.1057 0.1247 0.2799 0.0009  -0.0047 -0.0002 426 SER A N     
963  C CA    . SER A 126 ? 0.1265 0.1027 0.2770 0.0250  0.0022  -0.0072 426 SER A CA    
964  C C     . SER A 126 ? 0.1086 0.1240 0.2800 0.0068  -0.0001 0.0049  426 SER A C     
965  O O     . SER A 126 ? 0.1167 0.1331 0.2834 0.0184  -0.0056 0.0023  426 SER A O     
966  C CB    . SER A 126 ? 0.1443 0.1414 0.2966 0.0183  0.0213  0.0115  426 SER A CB    
967  O OG    . SER A 126 ? 0.1848 0.1393 0.3043 0.0340  -0.0012 0.0261  426 SER A OG    
968  N N     . PHE A 127 ? 0.1064 0.1248 0.2814 0.0077  -0.0115 -0.0104 427 PHE A N     
969  C CA    . PHE A 127 ? 0.0771 0.1221 0.2776 0.0040  0.0047  -0.0053 427 PHE A CA    
970  C C     . PHE A 127 ? 0.0772 0.1226 0.2730 0.0149  -0.0065 0.0089  427 PHE A C     
971  O O     . PHE A 127 ? 0.1013 0.1599 0.2657 0.0241  0.0126  -0.0031 427 PHE A O     
972  C CB    . PHE A 127 ? 0.0610 0.1159 0.3030 0.0389  0.0005  -0.0189 427 PHE A CB    
973  C CG    . PHE A 127 ? 0.0747 0.1256 0.2906 0.0185  0.0026  -0.0131 427 PHE A CG    
974  C CD1   . PHE A 127 ? 0.1014 0.1269 0.2833 0.0201  -0.0035 0.0130  427 PHE A CD1   
975  C CD2   . PHE A 127 ? 0.0986 0.1351 0.2770 0.0304  -0.0067 -0.0094 427 PHE A CD2   
976  C CE1   . PHE A 127 ? 0.0943 0.1489 0.2937 0.0170  -0.0071 0.0045  427 PHE A CE1   
977  C CE2   . PHE A 127 ? 0.1251 0.1210 0.2632 0.0090  0.0065  0.0063  427 PHE A CE2   
978  C CZ    . PHE A 127 ? 0.1137 0.1045 0.2953 0.0207  0.0087  0.0008  427 PHE A CZ    
979  N N     . PRO A 128 ? 0.0722 0.1538 0.2890 -0.0026 -0.0062 -0.0028 428 PRO A N     
980  C CA    . PRO A 128 ? 0.0790 0.1502 0.3003 0.0058  0.0050  -0.0019 428 PRO A CA    
981  C C     . PRO A 128 ? 0.0760 0.1633 0.2926 -0.0100 0.0076  -0.0080 428 PRO A C     
982  O O     . PRO A 128 ? 0.0896 0.1623 0.3242 -0.0058 0.0160  0.0051  428 PRO A O     
983  C CB    . PRO A 128 ? 0.1223 0.1505 0.3225 -0.0213 -0.0037 -0.0094 428 PRO A CB    
984  C CG    . PRO A 128 ? 0.0855 0.1346 0.3164 -0.0298 -0.0084 -0.0162 428 PRO A CG    
985  C CD    . PRO A 128 ? 0.0911 0.1404 0.3034 -0.0176 -0.0044 -0.0007 428 PRO A CD    
986  N N     . ALA A 129 ? 0.0922 0.1478 0.3051 0.0186  -0.0024 0.0107  429 ALA A N     
987  C CA    . ALA A 129 ? 0.1014 0.1543 0.3117 0.0403  0.0052  0.0029  429 ALA A CA    
988  C C     . ALA A 129 ? 0.1254 0.1383 0.3126 0.0392  0.0128  0.0034  429 ALA A C     
989  O O     . ALA A 129 ? 0.1005 0.1659 0.3059 0.0074  0.0020  -0.0161 429 ALA A O     
990  C CB    . ALA A 129 ? 0.1138 0.1608 0.3205 0.0253  0.0070  0.0039  429 ALA A CB    
991  N N     . LEU A 130 ? 0.1324 0.1375 0.3178 0.0281  0.0201  0.0090  430 LEU A N     
992  C CA    . LEU A 130 ? 0.1270 0.1484 0.3083 0.0199  0.0203  -0.0091 430 LEU A CA    
993  C C     . LEU A 130 ? 0.1104 0.1763 0.3100 0.0252  0.0008  -0.0031 430 LEU A C     
994  O O     . LEU A 130 ? 0.1271 0.1740 0.3291 0.0121  -0.0037 -0.0017 430 LEU A O     
995  C CB    . LEU A 130 ? 0.1078 0.1686 0.3173 -0.0068 0.0093  0.0172  430 LEU A CB    
996  C CG    . LEU A 130 ? 0.1316 0.1850 0.3138 0.0108  -0.0091 0.0186  430 LEU A CG    
997  C CD1   . LEU A 130 ? 0.1330 0.1992 0.3096 0.0177  0.0038  0.0043  430 LEU A CD1   
998  C CD2   . LEU A 130 ? 0.1230 0.2176 0.3252 0.0514  -0.0001 -0.0066 430 LEU A CD2   
999  N N     . GLY A 131 ? 0.1095 0.1561 0.3234 -0.0048 -0.0029 0.0124  431 GLY A N     
1000 C CA    . GLY A 131 ? 0.1349 0.1492 0.3329 0.0103  0.0013  0.0012  431 GLY A CA    
1001 C C     . GLY A 131 ? 0.1326 0.1677 0.3179 0.0017  0.0024  0.0093  431 GLY A C     
1002 O O     . GLY A 131 ? 0.1864 0.1536 0.3406 0.0255  -0.0080 0.0136  431 GLY A O     
1003 N N     . THR A 132 ? 0.1225 0.1496 0.3234 0.0271  -0.0030 0.0035  432 THR A N     
1004 C CA    . THR A 132 ? 0.1441 0.1255 0.3261 0.0325  0.0130  -0.0217 432 THR A CA    
1005 C C     . THR A 132 ? 0.1421 0.1443 0.3399 0.0551  0.0031  -0.0205 432 THR A C     
1006 O O     . THR A 132 ? 0.1214 0.2460 0.3518 0.0497  0.0138  -0.0309 432 THR A O     
1007 C CB    . THR A 132 ? 0.1313 0.1431 0.3315 0.0206  0.0191  -0.0114 432 THR A CB    
1008 O OG1   . THR A 132 ? 0.1301 0.1442 0.3337 0.0082  0.0059  -0.0036 432 THR A OG1   
1009 C CG2   . THR A 132 ? 0.1630 0.1781 0.3401 0.0040  -0.0186 0.0046  432 THR A CG2   
1010 N N     . GLY A 133 ? 0.1102 0.1476 0.3494 0.0055  0.0196  -0.0266 433 GLY A N     
1011 C CA    . GLY A 133 ? 0.1198 0.1794 0.3503 0.0003  0.0096  -0.0142 433 GLY A CA    
1012 C C     . GLY A 133 ? 0.1316 0.2031 0.3510 0.0073  -0.0023 -0.0173 433 GLY A C     
1013 O O     . GLY A 133 ? 0.1284 0.2004 0.3701 0.0360  -0.0040 -0.0304 433 GLY A O     
1014 N N     . ASN A 134 ? 0.1151 0.1999 0.3493 0.0183  0.0132  -0.0060 434 ASN A N     
1015 C CA    . ASN A 134 ? 0.1142 0.2081 0.3653 0.0105  -0.0029 0.0030  434 ASN A CA    
1016 C C     . ASN A 134 ? 0.1030 0.1909 0.3550 0.0128  -0.0209 0.0136  434 ASN A C     
1017 O O     . ASN A 134 ? 0.1494 0.2355 0.3994 0.0461  -0.0543 0.0066  434 ASN A O     
1018 C CB    . ASN A 134 ? 0.1525 0.2182 0.3705 -0.0046 -0.0300 -0.0044 434 ASN A CB    
1019 C CG    . ASN A 134 ? 0.1217 0.2205 0.4207 -0.0037 -0.0060 -0.0259 434 ASN A CG    
1020 O OD1   . ASN A 134 ? 0.1430 0.2977 0.5508 -0.0005 0.0271  -0.0096 434 ASN A OD1   
1021 N ND2   . ASN A 134 ? 0.1540 0.2058 0.5163 0.0178  0.0008  -0.0099 434 ASN A ND2   
1022 N N     A MET A 135 ? 0.1034 0.1930 0.3652 0.0136  -0.0227 0.0050  435 MET A N     
1023 N N     B MET A 135 ? 0.0968 0.2057 0.3595 0.0149  -0.0192 0.0131  435 MET A N     
1024 C CA    A MET A 135 ? 0.1472 0.1831 0.3743 0.0191  -0.0171 0.0091  435 MET A CA    
1025 C CA    B MET A 135 ? 0.1253 0.2042 0.3646 0.0177  -0.0147 0.0217  435 MET A CA    
1026 C C     A MET A 135 ? 0.1408 0.2042 0.3789 0.0386  -0.0240 0.0156  435 MET A C     
1027 C C     B MET A 135 ? 0.1306 0.2163 0.3754 0.0363  -0.0256 0.0244  435 MET A C     
1028 O O     A MET A 135 ? 0.1752 0.1914 0.3935 0.0474  -0.0241 0.0235  435 MET A O     
1029 O O     B MET A 135 ? 0.1728 0.2012 0.3878 0.0394  -0.0292 0.0287  435 MET A O     
1030 C CB    A MET A 135 ? 0.1590 0.1802 0.3907 0.0409  -0.0226 0.0057  435 MET A CB    
1031 C CB    B MET A 135 ? 0.1302 0.2142 0.3761 0.0374  -0.0203 0.0305  435 MET A CB    
1032 C CG    A MET A 135 ? 0.1873 0.1758 0.4053 0.0473  -0.0119 0.0154  435 MET A CG    
1033 C CG    B MET A 135 ? 0.1426 0.2344 0.3765 0.0325  -0.0132 0.0458  435 MET A CG    
1034 S SD    A MET A 135 ? 0.3204 0.3004 0.4173 0.0103  -0.0194 0.0111  435 MET A SD    
1035 S SD    B MET A 135 ? 0.1981 0.2539 0.3814 0.0117  0.0073  0.0736  435 MET A SD    
1036 C CE    A MET A 135 ? 0.3130 0.3245 0.3960 0.0312  -0.0429 0.0225  435 MET A CE    
1037 C CE    B MET A 135 ? 0.1738 0.2692 0.4046 0.0323  0.0338  0.0564  435 MET A CE    
1038 N N     . GLU A 136 ? 0.1661 0.2238 0.3750 0.0491  -0.0290 0.0017  436 GLU A N     
1039 C CA    . GLU A 136 ? 0.1291 0.2396 0.4167 0.0463  -0.0141 -0.0101 436 GLU A CA    
1040 C C     . GLU A 136 ? 0.1463 0.1938 0.3960 0.0586  -0.0191 -0.0110 436 GLU A C     
1041 O O     . GLU A 136 ? 0.1658 0.1999 0.4648 0.0699  -0.0599 -0.0463 436 GLU A O     
1042 C CB    . GLU A 136 ? 0.1928 0.2450 0.4818 0.0802  -0.0292 -0.0190 436 GLU A CB    
1043 C CG    . GLU A 136 ? 0.2395 0.2959 0.5525 0.0940  -0.0653 -0.0360 436 GLU A CG    
1044 C CD    . GLU A 136 ? 0.2683 0.2771 0.6918 0.1233  -0.0825 -0.0305 436 GLU A CD    
1045 O OE1   . GLU A 136 ? 0.4028 0.3505 0.7718 0.1265  -0.1613 0.0265  436 GLU A OE1   
1046 O OE2   . GLU A 136 ? 0.2662 0.4724 0.8674 0.0882  -0.1784 -0.0605 436 GLU A OE2   
1047 N N     . ILE A 137 ? 0.1193 0.2048 0.3301 0.0415  -0.0046 -0.0067 437 ILE A N     
1048 C CA    . ILE A 137 ? 0.1361 0.1917 0.3361 0.0296  -0.0116 0.0178  437 ILE A CA    
1049 C C     . ILE A 137 ? 0.0965 0.2296 0.3611 0.0367  -0.0094 0.0142  437 ILE A C     
1050 O O     . ILE A 137 ? 0.1315 0.2300 0.3566 0.0504  0.0046  0.0347  437 ILE A O     
1051 C CB    . ILE A 137 ? 0.1429 0.1891 0.3331 0.0231  -0.0045 0.0365  437 ILE A CB    
1052 C CG1   . ILE A 137 ? 0.1644 0.1753 0.3454 0.0307  0.0062  0.0257  437 ILE A CG1   
1053 C CG2   . ILE A 137 ? 0.1801 0.2268 0.3552 0.0038  -0.0073 0.0317  437 ILE A CG2   
1054 C CD1   . ILE A 137 ? 0.1632 0.1932 0.3068 0.0330  0.0197  0.0286  437 ILE A CD1   
1055 N N     . LYS A 138 ? 0.1056 0.2561 0.3479 0.0517  -0.0142 -0.0032 438 LYS A N     
1056 C CA    . LYS A 138 ? 0.1386 0.2817 0.3561 0.0507  -0.0022 0.0184  438 LYS A CA    
1057 C C     . LYS A 138 ? 0.1608 0.2331 0.3283 0.0524  0.0052  -0.0065 438 LYS A C     
1058 O O     . LYS A 138 ? 0.1425 0.2174 0.3433 0.0278  0.0137  -0.0117 438 LYS A O     
1059 C CB    . LYS A 138 ? 0.1950 0.2907 0.4119 0.1126  -0.0244 0.0204  438 LYS A CB    
1060 C CG    . LYS A 138 ? 0.2909 0.3601 0.4777 0.1244  0.0029  0.0225  438 LYS A CG    
1061 C CD    . LYS A 138 ? 0.3127 0.3687 0.6583 0.0946  0.0131  0.0297  438 LYS A CD    
1062 C CE    . LYS A 138 ? 0.3850 0.3529 0.7601 0.0889  0.0121  0.0089  438 LYS A CE    
1063 N NZ    . LYS A 138 ? 0.3094 0.3638 0.8353 0.1469  0.0009  -0.0158 438 LYS A NZ    
1064 N N     . LYS A 139 ? 0.1202 0.2421 0.3418 0.0334  0.0102  0.0159  439 LYS A N     
1065 C CA    . LYS A 139 ? 0.1137 0.2259 0.3469 0.0386  0.0082  0.0202  439 LYS A CA    
1066 C C     . LYS A 139 ? 0.1298 0.2076 0.3381 0.0374  0.0224  0.0139  439 LYS A C     
1067 O O     . LYS A 139 ? 0.1284 0.2125 0.3349 0.0345  0.0088  0.0170  439 LYS A O     
1068 C CB    . LYS A 139 ? 0.1367 0.2500 0.3703 0.0650  0.0153  0.0287  439 LYS A CB    
1069 C CG    . LYS A 139 ? 0.1544 0.2885 0.3911 0.0543  0.0287  0.0112  439 LYS A CG    
1070 C CD    . LYS A 139 ? 0.2296 0.3780 0.4021 0.0506  0.0456  0.0017  439 LYS A CD    
1071 C CE    . LYS A 139 ? 0.2850 0.4398 0.4115 0.0419  0.0884  -0.0241 439 LYS A CE    
1072 N NZ    . LYS A 139 ? 0.3371 0.4376 0.4621 0.0579  0.0789  -0.0473 439 LYS A NZ    
1073 N N     . GLU A 140 ? 0.1047 0.2109 0.3661 0.0461  0.0346  0.0180  440 GLU A N     
1074 C CA    . GLU A 140 ? 0.2050 0.1839 0.3529 0.0296  0.0158  0.0012  440 GLU A CA    
1075 C C     . GLU A 140 ? 0.2021 0.1271 0.3313 0.0528  0.0136  -0.0087 440 GLU A C     
1076 O O     . GLU A 140 ? 0.1755 0.2237 0.3401 0.0797  0.0026  -0.0135 440 GLU A O     
1077 C CB    . GLU A 140 ? 0.2046 0.2154 0.4048 0.0621  0.0508  -0.0309 440 GLU A CB    
1078 C CG    . GLU A 140 ? 0.3089 0.2726 0.4373 0.0230  0.0632  -0.0364 440 GLU A CG    
1079 C CD    . GLU A 140 ? 0.2840 0.3008 0.4924 0.0388  0.1212  -0.0498 440 GLU A CD    
1080 O OE1   . GLU A 140 ? 0.2957 0.3343 0.5458 0.1388  0.1090  -0.0226 440 GLU A OE1   
1081 O OE2   . GLU A 140 ? 0.4772 0.3684 0.5107 0.0260  0.1586  -0.0759 440 GLU A OE2   
1082 N N     . THR A 141 ? 0.1615 0.1413 0.3367 0.0575  0.0115  -0.0170 441 THR A N     
1083 C CA    . THR A 141 ? 0.1717 0.1540 0.3329 0.0338  -0.0005 0.0048  441 THR A CA    
1084 C C     . THR A 141 ? 0.1418 0.1676 0.3017 0.0170  -0.0097 -0.0241 441 THR A C     
1085 O O     . THR A 141 ? 0.1251 0.1796 0.3257 0.0171  -0.0031 -0.0015 441 THR A O     
1086 C CB    . THR A 141 ? 0.2143 0.1374 0.3480 0.0750  -0.0056 0.0193  441 THR A CB    
1087 O OG1   . THR A 141 ? 0.2787 0.1583 0.3899 0.0893  0.0166  0.0174  441 THR A OG1   
1088 C CG2   . THR A 141 ? 0.2151 0.1905 0.3486 0.0460  -0.0221 0.0334  441 THR A CG2   
1089 N N     . ALA A 142 ? 0.0887 0.1640 0.3213 0.0356  -0.0064 -0.0068 442 ALA A N     
1090 C CA    . ALA A 142 ? 0.1205 0.1444 0.3112 0.0334  -0.0023 -0.0134 442 ALA A CA    
1091 C C     . ALA A 142 ? 0.1155 0.1616 0.3023 0.0229  0.0034  -0.0073 442 ALA A C     
1092 O O     . ALA A 142 ? 0.1153 0.1282 0.3267 0.0231  0.0055  -0.0077 442 ALA A O     
1093 C CB    . ALA A 142 ? 0.1117 0.1433 0.3199 0.0278  -0.0005 0.0016  442 ALA A CB    
1094 N N     . ALA A 143 ? 0.1273 0.1664 0.3252 0.0599  0.0137  -0.0068 443 ALA A N     
1095 C CA    . ALA A 143 ? 0.1756 0.1341 0.3044 0.0230  -0.0083 -0.0034 443 ALA A CA    
1096 C C     . ALA A 143 ? 0.1407 0.1307 0.2980 0.0316  0.0002  -0.0023 443 ALA A C     
1097 O O     . ALA A 143 ? 0.1259 0.1510 0.3181 0.0341  -0.0098 -0.0066 443 ALA A O     
1098 C CB    . ALA A 143 ? 0.1217 0.1509 0.3123 -0.0105 -0.0089 -0.0001 443 ALA A CB    
1099 N N     A GLU A 144 ? 0.1184 0.1194 0.3066 0.0273  -0.0066 -0.0088 444 GLU A N     
1100 N N     B GLU A 144 ? 0.1504 0.1212 0.3208 0.0407  -0.0025 -0.0087 444 GLU A N     
1101 C CA    A GLU A 144 ? 0.1358 0.1395 0.2930 0.0127  -0.0033 -0.0166 444 GLU A CA    
1102 C CA    B GLU A 144 ? 0.1898 0.1381 0.3140 0.0295  0.0132  -0.0116 444 GLU A CA    
1103 C C     A GLU A 144 ? 0.1089 0.1418 0.2970 0.0296  -0.0142 -0.0094 444 GLU A C     
1104 C C     B GLU A 144 ? 0.1400 0.1209 0.3105 0.0516  -0.0110 -0.0056 444 GLU A C     
1105 O O     A GLU A 144 ? 0.1110 0.1704 0.3158 0.0030  -0.0055 -0.0073 444 GLU A O     
1106 O O     B GLU A 144 ? 0.1405 0.0868 0.3433 0.0636  -0.0033 -0.0025 444 GLU A O     
1107 C CB    A GLU A 144 ? 0.1642 0.1357 0.3262 0.0103  -0.0074 -0.0203 444 GLU A CB    
1108 C CB    B GLU A 144 ? 0.2422 0.1416 0.3651 0.0451  0.0295  -0.0090 444 GLU A CB    
1109 C CG    A GLU A 144 ? 0.1624 0.1004 0.3480 0.0219  -0.0066 -0.0300 444 GLU A CG    
1110 C CG    B GLU A 144 ? 0.3011 0.1198 0.4083 0.0402  0.0411  0.0034  444 GLU A CG    
1111 C CD    A GLU A 144 ? 0.2073 0.1387 0.3837 0.0528  0.0013  -0.0079 444 GLU A CD    
1112 C CD    B GLU A 144 ? 0.3543 0.0969 0.4582 0.0395  0.0669  0.0223  444 GLU A CD    
1113 O OE1   A GLU A 144 ? 0.2364 0.1496 0.4212 0.0501  -0.0269 -0.0016 444 GLU A OE1   
1114 O OE1   B GLU A 144 ? 0.4006 0.2351 0.4919 0.1005  0.0801  0.0693  444 GLU A OE1   
1115 O OE2   A GLU A 144 ? 0.2343 0.2289 0.4311 0.0532  0.0090  -0.0407 444 GLU A OE2   
1116 O OE2   B GLU A 144 ? 0.3749 0.2445 0.5128 0.0426  0.0501  -0.0475 444 GLU A OE2   
1117 N N     . ILE A 145 ? 0.1179 0.1249 0.3010 0.0382  -0.0045 -0.0112 445 ILE A N     
1118 C CA    . ILE A 145 ? 0.1595 0.1456 0.2875 0.0170  -0.0012 -0.0081 445 ILE A CA    
1119 C C     . ILE A 145 ? 0.1189 0.1630 0.2807 0.0135  -0.0032 0.0017  445 ILE A C     
1120 O O     . ILE A 145 ? 0.1156 0.1683 0.2920 -0.0041 0.0038  -0.0049 445 ILE A O     
1121 C CB    . ILE A 145 ? 0.1723 0.1449 0.2903 0.0069  -0.0073 0.0111  445 ILE A CB    
1122 C CG1   . ILE A 145 ? 0.1847 0.1808 0.2922 0.0159  -0.0186 0.0248  445 ILE A CG1   
1123 C CG2   . ILE A 145 ? 0.1799 0.1527 0.3082 -0.0017 -0.0048 0.0092  445 ILE A CG2   
1124 C CD1   . ILE A 145 ? 0.1701 0.2159 0.3146 0.0232  -0.0241 0.0299  445 ILE A CD1   
1125 N N     . LEU A 146 ? 0.1198 0.1365 0.2888 0.0194  -0.0048 -0.0034 446 LEU A N     
1126 C CA    . LEU A 146 ? 0.1161 0.1279 0.3085 0.0181  0.0050  -0.0076 446 LEU A CA    
1127 C C     . LEU A 146 ? 0.0915 0.1389 0.2971 0.0070  0.0153  -0.0003 446 LEU A C     
1128 O O     . LEU A 146 ? 0.1054 0.1282 0.3134 0.0359  -0.0016 -0.0023 446 LEU A O     
1129 C CB    . LEU A 146 ? 0.1165 0.1397 0.2989 0.0242  -0.0013 0.0085  446 LEU A CB    
1130 C CG    . LEU A 146 ? 0.1338 0.1395 0.3123 0.0184  -0.0131 0.0103  446 LEU A CG    
1131 C CD1   . LEU A 146 ? 0.1202 0.1646 0.3216 0.0135  -0.0160 0.0129  446 LEU A CD1   
1132 C CD2   . LEU A 146 ? 0.1477 0.1622 0.3174 0.0082  -0.0169 0.0118  446 LEU A CD2   
1133 N N     . PHE A 147 ? 0.1026 0.1523 0.2998 0.0390  0.0066  -0.0131 447 PHE A N     
1134 C CA    . PHE A 147 ? 0.1138 0.1474 0.2906 0.0377  -0.0057 -0.0001 447 PHE A CA    
1135 C C     . PHE A 147 ? 0.0872 0.1501 0.2873 0.0379  0.0036  0.0018  447 PHE A C     
1136 O O     . PHE A 147 ? 0.1007 0.1489 0.2986 0.0438  -0.0073 -0.0058 447 PHE A O     
1137 C CB    . PHE A 147 ? 0.0932 0.1365 0.2954 0.0262  -0.0203 0.0057  447 PHE A CB    
1138 C CG    . PHE A 147 ? 0.1326 0.1476 0.2976 0.0233  0.0012  0.0147  447 PHE A CG    
1139 C CD1   . PHE A 147 ? 0.1619 0.1464 0.3009 0.0018  -0.0060 0.0052  447 PHE A CD1   
1140 C CD2   . PHE A 147 ? 0.1155 0.1611 0.3293 0.0122  -0.0119 0.0243  447 PHE A CD2   
1141 C CE1   . PHE A 147 ? 0.1811 0.1786 0.3128 0.0179  0.0055  -0.0035 447 PHE A CE1   
1142 C CE2   . PHE A 147 ? 0.1433 0.1970 0.3102 0.0288  -0.0224 0.0187  447 PHE A CE2   
1143 C CZ    . PHE A 147 ? 0.1689 0.1686 0.3028 0.0084  -0.0008 0.0028  447 PHE A CZ    
1144 N N     . ASP A 148 ? 0.1169 0.1567 0.3003 0.0269  -0.0121 -0.0023 448 ASP A N     
1145 C CA    . ASP A 148 ? 0.1643 0.1473 0.2912 0.0005  -0.0070 0.0034  448 ASP A CA    
1146 C C     . ASP A 148 ? 0.1122 0.1341 0.2965 -0.0087 -0.0138 0.0026  448 ASP A C     
1147 O O     . ASP A 148 ? 0.1125 0.1239 0.3106 -0.0077 -0.0130 0.0063  448 ASP A O     
1148 C CB    . ASP A 148 ? 0.1516 0.1421 0.2993 0.0112  0.0021  -0.0016 448 ASP A CB    
1149 C CG    . ASP A 148 ? 0.1873 0.1395 0.3216 0.0324  0.0109  0.0186  448 ASP A CG    
1150 O OD1   . ASP A 148 ? 0.2048 0.1616 0.3418 0.0293  -0.0170 -0.0043 448 ASP A OD1   
1151 O OD2   . ASP A 148 ? 0.2435 0.1858 0.3800 0.0750  -0.0187 0.0131  448 ASP A OD2   
1152 N N     . GLU A 149 ? 0.0968 0.1287 0.3126 -0.0015 0.0010  -0.0035 449 GLU A N     
1153 C CA    . GLU A 149 ? 0.1305 0.1167 0.3051 0.0097  0.0017  0.0052  449 GLU A CA    
1154 C C     . GLU A 149 ? 0.1161 0.0969 0.2895 0.0073  0.0043  0.0084  449 GLU A C     
1155 O O     . GLU A 149 ? 0.1197 0.1405 0.3188 0.0082  0.0149  -0.0031 449 GLU A O     
1156 C CB    . GLU A 149 ? 0.1484 0.1284 0.3376 -0.0002 -0.0238 -0.0050 449 GLU A CB    
1157 C CG    . GLU A 149 ? 0.1287 0.1332 0.3571 0.0268  -0.0189 -0.0095 449 GLU A CG    
1158 C CD    . GLU A 149 ? 0.1525 0.1566 0.3959 0.0212  -0.0086 0.0119  449 GLU A CD    
1159 O OE1   . GLU A 149 ? 0.1883 0.1684 0.3678 0.0089  0.0192  0.0109  449 GLU A OE1   
1160 O OE2   . GLU A 149 ? 0.2395 0.1905 0.5835 0.0167  -0.0047 0.1048  449 GLU A OE2   
1161 N N     . VAL A 150 ? 0.1073 0.1403 0.3036 0.0196  0.0130  0.0149  450 VAL A N     
1162 C CA    . VAL A 150 ? 0.1168 0.1463 0.3059 0.0240  0.0081  0.0337  450 VAL A CA    
1163 C C     . VAL A 150 ? 0.1104 0.1471 0.3005 0.0367  0.0106  0.0222  450 VAL A C     
1164 O O     . VAL A 150 ? 0.1022 0.1532 0.3131 0.0397  0.0080  0.0074  450 VAL A O     
1165 C CB    . VAL A 150 ? 0.1572 0.1858 0.3481 0.0305  0.0087  0.0502  450 VAL A CB    
1166 C CG1   . VAL A 150 ? 0.1879 0.1813 0.3613 0.0728  0.0272  0.0722  450 VAL A CG1   
1167 C CG2   . VAL A 150 ? 0.1471 0.1856 0.3487 0.0251  0.0089  0.0388  450 VAL A CG2   
1168 N N     . LEU A 151 ? 0.1064 0.1747 0.3079 0.0690  -0.0151 -0.0030 451 LEU A N     
1169 C CA    . LEU A 151 ? 0.1533 0.1830 0.3032 0.0513  -0.0191 -0.0027 451 LEU A CA    
1170 C C     . LEU A 151 ? 0.1036 0.1049 0.3206 0.0187  -0.0233 -0.0246 451 LEU A C     
1171 O O     . LEU A 151 ? 0.1062 0.1753 0.3441 0.0245  -0.0225 -0.0274 451 LEU A O     
1172 C CB    . LEU A 151 ? 0.1023 0.1954 0.3330 0.0549  -0.0130 -0.0195 451 LEU A CB    
1173 C CG    . LEU A 151 ? 0.2000 0.2223 0.3313 0.0594  -0.0138 -0.0370 451 LEU A CG    
1174 C CD1   . LEU A 151 ? 0.1316 0.2281 0.3590 0.0374  -0.0366 -0.0518 451 LEU A CD1   
1175 C CD2   . LEU A 151 ? 0.2400 0.2573 0.3307 0.0436  -0.0044 -0.0192 451 LEU A CD2   
1176 N N     . THR A 152 ? 0.1417 0.1356 0.3221 0.0078  -0.0205 -0.0190 452 THR A N     
1177 C CA    . THR A 152 ? 0.1507 0.1119 0.3302 0.0054  -0.0179 0.0001  452 THR A CA    
1178 C C     . THR A 152 ? 0.1141 0.1273 0.3175 -0.0041 -0.0237 0.0024  452 THR A C     
1179 O O     . THR A 152 ? 0.1053 0.1466 0.3735 -0.0059 -0.0043 0.0141  452 THR A O     
1180 C CB    . THR A 152 ? 0.2080 0.1064 0.3584 0.0043  -0.0151 0.0412  452 THR A CB    
1181 O OG1   . THR A 152 ? 0.2202 0.1070 0.4028 0.0191  -0.0058 0.0277  452 THR A OG1   
1182 C CG2   . THR A 152 ? 0.2176 0.1567 0.3524 0.0322  -0.0168 0.0636  452 THR A CG2   
1183 N N     . PHE A 153 ? 0.1173 0.1200 0.3245 -0.0018 0.0087  0.0027  453 PHE A N     
1184 C CA    . PHE A 153 ? 0.1586 0.1106 0.3052 -0.0014 0.0143  -0.0048 453 PHE A CA    
1185 C C     . PHE A 153 ? 0.1189 0.0959 0.3262 -0.0192 0.0171  -0.0035 453 PHE A C     
1186 O O     . PHE A 153 ? 0.0923 0.1481 0.3427 -0.0133 0.0160  0.0050  453 PHE A O     
1187 C CB    . PHE A 153 ? 0.1570 0.1319 0.3112 -0.0090 0.0053  -0.0065 453 PHE A CB    
1188 C CG    . PHE A 153 ? 0.1382 0.1488 0.3043 -0.0143 0.0048  -0.0060 453 PHE A CG    
1189 C CD1   . PHE A 153 ? 0.1466 0.1270 0.3117 0.0052  0.0138  -0.0079 453 PHE A CD1   
1190 C CD2   . PHE A 153 ? 0.1417 0.1685 0.2980 0.0029  -0.0017 -0.0081 453 PHE A CD2   
1191 C CE1   . PHE A 153 ? 0.1375 0.1055 0.3379 -0.0080 0.0055  -0.0155 453 PHE A CE1   
1192 C CE2   . PHE A 153 ? 0.1390 0.1786 0.3211 -0.0130 0.0158  -0.0260 453 PHE A CE2   
1193 C CZ    . PHE A 153 ? 0.1271 0.1631 0.3299 -0.0270 0.0110  -0.0115 453 PHE A CZ    
1194 N N     . ALA A 154 ? 0.1472 0.0935 0.3339 0.0006  -0.0022 -0.0035 454 ALA A N     
1195 C CA    . ALA A 154 ? 0.1546 0.1134 0.3294 0.0062  -0.0139 0.0033  454 ALA A CA    
1196 C C     . ALA A 154 ? 0.1287 0.1332 0.3391 0.0243  -0.0109 0.0010  454 ALA A C     
1197 O O     . ALA A 154 ? 0.1302 0.1552 0.3536 0.0140  -0.0338 0.0340  454 ALA A O     
1198 C CB    . ALA A 154 ? 0.1511 0.1222 0.3206 0.0091  -0.0163 -0.0038 454 ALA A CB    
1199 N N     . LYS A 155 ? 0.1233 0.1318 0.3767 0.0061  -0.0233 0.0195  455 LYS A N     
1200 C CA    . LYS A 155 ? 0.1909 0.1216 0.4015 -0.0090 -0.0436 0.0271  455 LYS A CA    
1201 C C     . LYS A 155 ? 0.1393 0.1196 0.4234 0.0091  -0.0461 0.0443  455 LYS A C     
1202 O O     . LYS A 155 ? 0.1348 0.2359 0.4716 -0.0773 -0.0680 0.0599  455 LYS A O     
1203 C CB    . LYS A 155 ? 0.2990 0.0994 0.4525 -0.0058 -0.0515 0.0365  455 LYS A CB    
1204 C CG    . LYS A 155 ? 0.3366 0.1768 0.4996 0.0111  -0.1009 0.0184  455 LYS A CG    
1205 C CD    . LYS A 155 ? 0.4339 0.1453 0.4995 0.0517  -0.1185 -0.0062 455 LYS A CD    
1206 C CE    . LYS A 155 ? 0.4831 0.3560 0.5472 0.0178  -0.1319 0.0008  455 LYS A CE    
1207 N NZ    . LYS A 155 ? 0.4535 0.4178 0.5701 -0.0327 -0.1492 -0.0262 455 LYS A NZ    
1208 N N     . ASP A 156 ? 0.1284 0.1827 0.4002 -0.0028 -0.0177 0.0276  456 ASP A N     
1209 C CA    . ASP A 156 ? 0.1837 0.1379 0.4211 -0.0567 -0.0085 0.0255  456 ASP A CA    
1210 C C     . ASP A 156 ? 0.1610 0.1428 0.3804 -0.0353 0.0182  0.0397  456 ASP A C     
1211 O O     . ASP A 156 ? 0.1813 0.2495 0.4184 -0.0616 0.0730  0.0263  456 ASP A O     
1212 C CB    . ASP A 156 ? 0.1832 0.1886 0.4375 -0.0444 -0.0132 0.0636  456 ASP A CB    
1213 C CG    . ASP A 156 ? 0.2414 0.2026 0.5028 -0.0573 -0.0463 0.0943  456 ASP A CG    
1214 O OD1   . ASP A 156 ? 0.2664 0.2536 0.5365 -0.0713 -0.0215 0.0403  456 ASP A OD1   
1215 O OD2   . ASP A 156 ? 0.2265 0.3319 0.5726 -0.0815 -0.0517 0.1472  456 ASP A OD2   
1216 N N     . HIS A 157 ? 0.1317 0.0948 0.3902 -0.0316 0.0314  0.0114  457 HIS A N     
1217 C CA    . HIS A 157 ? 0.1236 0.1439 0.3475 -0.0056 0.0495  0.0079  457 HIS A CA    
1218 C C     . HIS A 157 ? 0.1464 0.1663 0.3578 -0.0171 0.0294  0.0012  457 HIS A C     
1219 O O     . HIS A 157 ? 0.1358 0.1354 0.3685 -0.0063 0.0173  0.0001  457 HIS A O     
1220 C CB    . HIS A 157 ? 0.1422 0.1835 0.3497 -0.0091 0.0431  -0.0154 457 HIS A CB    
1221 C CG    . HIS A 157 ? 0.1793 0.2240 0.3621 -0.0136 0.0386  0.0005  457 HIS A CG    
1222 N ND1   . HIS A 157 ? 0.1495 0.3219 0.3581 -0.0037 0.0350  0.0090  457 HIS A ND1   
1223 C CD2   . HIS A 157 ? 0.1917 0.2623 0.3812 -0.0255 0.0229  -0.0043 457 HIS A CD2   
1224 C CE1   . HIS A 157 ? 0.2072 0.3694 0.3362 0.0241  0.0529  0.0149  457 HIS A CE1   
1225 N NE2   . HIS A 157 ? 0.1970 0.2967 0.3723 -0.0179 0.0436  0.0027  457 HIS A NE2   
1226 N N     . VAL A 158 ? 0.1147 0.1582 0.3732 -0.0085 0.0383  0.0028  458 VAL A N     
1227 C CA    . VAL A 158 ? 0.1471 0.1316 0.3629 -0.0236 0.0557  -0.0172 458 VAL A CA    
1228 C C     . VAL A 158 ? 0.1808 0.1581 0.3674 -0.0072 0.0337  -0.0024 458 VAL A C     
1229 O O     . VAL A 158 ? 0.2476 0.2009 0.3708 -0.0148 0.0323  0.0161  458 VAL A O     
1230 C CB    . VAL A 158 ? 0.2228 0.1587 0.3812 -0.0515 0.0366  -0.0422 458 VAL A CB    
1231 C CG1   . VAL A 158 ? 0.2283 0.2025 0.3958 -0.0900 0.0516  -0.0602 458 VAL A CG1   
1232 C CG2   . VAL A 158 ? 0.2713 0.1977 0.4058 -0.0863 0.0400  -0.0538 458 VAL A CG2   
1233 N N     . LYS A 159 ? 0.1307 0.1551 0.3528 -0.0233 0.0080  -0.0002 459 LYS A N     
1234 C CA    . LYS A 159 ? 0.1265 0.1875 0.3981 -0.0191 -0.0040 0.0103  459 LYS A CA    
1235 C C     . LYS A 159 ? 0.1324 0.1678 0.4136 -0.0046 0.0032  0.0082  459 LYS A C     
1236 O O     . LYS A 159 ? 0.1769 0.1565 0.4650 -0.0098 -0.0622 0.0028  459 LYS A O     
1237 C CB    . LYS A 159 ? 0.1403 0.2265 0.4523 -0.0254 0.0122  -0.0120 459 LYS A CB    
1238 C CG    . LYS A 159 ? 0.1912 0.2798 0.4745 -0.0682 0.0568  -0.0493 459 LYS A CG    
1239 C CD    . LYS A 159 ? 0.2269 0.3777 0.5375 -0.0906 0.0178  -0.0935 459 LYS A CD    
1240 C CE    . LYS A 159 ? 0.3905 0.5040 0.5770 -0.0264 0.0254  -0.1097 459 LYS A CE    
1241 N NZ    . LYS A 159 ? 0.3594 0.4931 0.6204 -0.0364 0.0235  -0.1755 459 LYS A NZ    
1242 N N     . HIS A 160 ? 0.1223 0.1414 0.3819 -0.0171 0.0054  0.0051  460 HIS A N     
1243 C CA    . HIS A 160 ? 0.1525 0.1162 0.3532 -0.0279 0.0193  0.0299  460 HIS A CA    
1244 C C     . HIS A 160 ? 0.1057 0.1052 0.3408 -0.0134 0.0179  0.0149  460 HIS A C     
1245 O O     . HIS A 160 ? 0.1268 0.1288 0.3594 0.0004  0.0175  0.0047  460 HIS A O     
1246 C CB    . HIS A 160 ? 0.1206 0.1185 0.3386 -0.0174 0.0251  0.0121  460 HIS A CB    
1247 C CG    . HIS A 160 ? 0.1636 0.1396 0.3459 -0.0108 0.0043  -0.0081 460 HIS A CG    
1248 N ND1   . HIS A 160 ? 0.1403 0.1662 0.3540 -0.0034 0.0149  -0.0155 460 HIS A ND1   
1249 C CD2   . HIS A 160 ? 0.1497 0.1236 0.3451 0.0175  0.0062  0.0065  460 HIS A CD2   
1250 C CE1   . HIS A 160 ? 0.1868 0.1614 0.4036 -0.0134 0.0216  -0.0396 460 HIS A CE1   
1251 N NE2   . HIS A 160 ? 0.1843 0.1427 0.3426 0.0185  -0.0050 0.0014  460 HIS A NE2   
1252 N N     . GLN A 161 ? 0.1214 0.1005 0.3166 -0.0067 -0.0027 0.0051  461 GLN A N     
1253 C CA    . GLN A 161 ? 0.1108 0.1067 0.3287 0.0076  -0.0040 -0.0083 461 GLN A CA    
1254 C C     . GLN A 161 ? 0.0958 0.1321 0.2921 0.0001  0.0069  -0.0107 461 GLN A C     
1255 O O     . GLN A 161 ? 0.0932 0.1707 0.3072 0.0106  0.0011  -0.0138 461 GLN A O     
1256 C CB    . GLN A 161 ? 0.1209 0.1210 0.3603 0.0116  -0.0253 0.0022  461 GLN A CB    
1257 C CG    . GLN A 161 ? 0.1239 0.1643 0.3874 0.0096  -0.0293 -0.0001 461 GLN A CG    
1258 C CD    . GLN A 161 ? 0.1445 0.1730 0.3992 0.0227  -0.0464 0.0103  461 GLN A CD    
1259 O OE1   . GLN A 161 ? 0.2008 0.1929 0.5358 0.0797  -0.0787 -0.0139 461 GLN A OE1   
1260 N NE2   . GLN A 161 ? 0.1530 0.2007 0.3743 0.0753  -0.0463 0.0581  461 GLN A NE2   
1261 N N     . LEU A 162 ? 0.1039 0.1234 0.2900 0.0192  -0.0061 -0.0206 462 LEU A N     
1262 C CA    . LEU A 162 ? 0.1000 0.0756 0.2846 -0.0096 0.0044  -0.0094 462 LEU A CA    
1263 C C     . LEU A 162 ? 0.1159 0.1082 0.2829 0.0179  -0.0055 -0.0038 462 LEU A C     
1264 O O     . LEU A 162 ? 0.1286 0.1324 0.2974 -0.0028 0.0186  -0.0191 462 LEU A O     
1265 C CB    . LEU A 162 ? 0.1040 0.1329 0.3013 0.0082  0.0003  0.0017  462 LEU A CB    
1266 C CG    . LEU A 162 ? 0.1085 0.1087 0.3060 0.0271  -0.0102 0.0041  462 LEU A CG    
1267 C CD1   . LEU A 162 ? 0.1683 0.0948 0.3002 0.0210  -0.0239 0.0036  462 LEU A CD1   
1268 C CD2   . LEU A 162 ? 0.1380 0.1141 0.3134 0.0134  -0.0134 0.0080  462 LEU A CD2   
1269 N N     . THR A 163 ? 0.1106 0.1001 0.2878 0.0145  -0.0080 -0.0081 463 THR A N     
1270 C CA    . THR A 163 ? 0.1105 0.1069 0.3028 0.0056  -0.0139 -0.0124 463 THR A CA    
1271 C C     . THR A 163 ? 0.1089 0.1537 0.2930 -0.0024 -0.0108 -0.0211 463 THR A C     
1272 O O     . THR A 163 ? 0.1080 0.1549 0.3224 0.0130  -0.0263 -0.0325 463 THR A O     
1273 C CB    . THR A 163 ? 0.1525 0.1427 0.3222 -0.0221 -0.0175 0.0194  463 THR A CB    
1274 O OG1   . THR A 163 ? 0.2133 0.1890 0.3471 -0.0126 -0.0566 0.0361  463 THR A OG1   
1275 C CG2   . THR A 163 ? 0.1828 0.1824 0.3209 -0.0306 -0.0015 0.0264  463 THR A CG2   
1276 N N     . VAL A 164 ? 0.1026 0.1343 0.2965 -0.0033 -0.0070 -0.0237 464 VAL A N     
1277 C CA    . VAL A 164 ? 0.0781 0.1296 0.3027 -0.0228 0.0060  -0.0078 464 VAL A CA    
1278 C C     . VAL A 164 ? 0.0816 0.1530 0.2787 -0.0089 0.0018  -0.0046 464 VAL A C     
1279 O O     . VAL A 164 ? 0.0976 0.2191 0.2828 -0.0067 0.0006  -0.0238 464 VAL A O     
1280 C CB    . VAL A 164 ? 0.0673 0.1088 0.3242 -0.0021 0.0089  -0.0150 464 VAL A CB    
1281 C CG1   . VAL A 164 ? 0.0807 0.1289 0.3273 -0.0264 0.0114  -0.0027 464 VAL A CG1   
1282 C CG2   . VAL A 164 ? 0.0818 0.1004 0.3341 -0.0003 -0.0023 0.0000  464 VAL A CG2   
1283 N N     . LYS A 165 ? 0.0858 0.1537 0.2825 -0.0007 0.0012  -0.0119 465 LYS A N     
1284 C CA    . LYS A 165 ? 0.0767 0.1628 0.2780 -0.0272 -0.0050 0.0015  465 LYS A CA    
1285 C C     . LYS A 165 ? 0.1114 0.1757 0.2745 -0.0079 -0.0055 -0.0050 465 LYS A C     
1286 O O     . LYS A 165 ? 0.1065 0.1822 0.2792 -0.0217 0.0010  -0.0195 465 LYS A O     
1287 C CB    . LYS A 165 ? 0.1305 0.1530 0.2785 -0.0182 0.0045  -0.0023 465 LYS A CB    
1288 C CG    . LYS A 165 ? 0.1868 0.1782 0.2976 -0.0209 -0.0156 0.0051  465 LYS A CG    
1289 C CD    . LYS A 165 ? 0.2231 0.1931 0.3221 -0.0113 -0.0079 0.0326  465 LYS A CD    
1290 C CE    . LYS A 165 ? 0.2984 0.2024 0.3323 -0.0140 -0.0237 0.0476  465 LYS A CE    
1291 N NZ    . LYS A 165 ? 0.3843 0.1874 0.3927 -0.0060 -0.0237 0.0238  465 LYS A NZ    
1292 N N     . PHE A 166 ? 0.1143 0.1422 0.2699 0.0027  -0.0177 -0.0154 466 PHE A N     
1293 C CA    . PHE A 166 ? 0.1182 0.1552 0.2697 0.0053  -0.0086 0.0063  466 PHE A CA    
1294 C C     . PHE A 166 ? 0.0935 0.1781 0.2621 0.0188  -0.0078 0.0094  466 PHE A C     
1295 O O     . PHE A 166 ? 0.1465 0.2027 0.2648 -0.0308 -0.0016 0.0064  466 PHE A O     
1296 C CB    . PHE A 166 ? 0.1067 0.1539 0.2924 0.0020  -0.0099 -0.0062 466 PHE A CB    
1297 C CG    . PHE A 166 ? 0.1257 0.1318 0.3004 0.0061  -0.0075 0.0001  466 PHE A CG    
1298 C CD1   . PHE A 166 ? 0.1219 0.1145 0.3075 0.0089  -0.0044 -0.0093 466 PHE A CD1   
1299 C CD2   . PHE A 166 ? 0.1383 0.1399 0.3106 0.0019  0.0055  -0.0129 466 PHE A CD2   
1300 C CE1   . PHE A 166 ? 0.1144 0.1622 0.3059 0.0099  0.0033  0.0047  466 PHE A CE1   
1301 C CE2   . PHE A 166 ? 0.1618 0.1329 0.3178 0.0109  0.0048  0.0026  466 PHE A CE2   
1302 C CZ    . PHE A 166 ? 0.1459 0.1676 0.3080 0.0184  0.0073  0.0112  466 PHE A CZ    
1303 N N     . VAL A 167 ? 0.1286 0.1724 0.2657 -0.0135 0.0039  0.0185  467 VAL A N     
1304 C CA    . VAL A 167 ? 0.1009 0.1667 0.2791 -0.0141 0.0014  0.0127  467 VAL A CA    
1305 C C     . VAL A 167 ? 0.1051 0.1848 0.2731 -0.0269 -0.0087 -0.0109 467 VAL A C     
1306 O O     . VAL A 167 ? 0.1091 0.2185 0.2787 -0.0077 -0.0059 -0.0036 467 VAL A O     
1307 C CB    . VAL A 167 ? 0.1085 0.1834 0.2851 -0.0111 -0.0051 -0.0017 467 VAL A CB    
1308 C CG1   . VAL A 167 ? 0.1403 0.2136 0.3207 -0.0074 0.0015  0.0138  467 VAL A CG1   
1309 C CG2   . VAL A 167 ? 0.1182 0.1590 0.3125 -0.0197 -0.0240 -0.0109 467 VAL A CG2   
1310 N N     . ILE A 168 ? 0.1105 0.2150 0.2961 -0.0333 -0.0074 -0.0079 468 ILE A N     
1311 C CA    . ILE A 168 ? 0.1002 0.2153 0.2904 -0.0452 -0.0043 -0.0114 468 ILE A CA    
1312 C C     . ILE A 168 ? 0.1168 0.2278 0.2755 -0.0582 -0.0020 -0.0026 468 ILE A C     
1313 O O     . ILE A 168 ? 0.1354 0.1793 0.3197 -0.0463 0.0123  0.0008  468 ILE A O     
1314 C CB    . ILE A 168 ? 0.1083 0.2526 0.3131 -0.0239 0.0017  -0.0350 468 ILE A CB    
1315 C CG1   . ILE A 168 ? 0.1323 0.2444 0.3173 -0.0276 0.0007  -0.0361 468 ILE A CG1   
1316 C CG2   . ILE A 168 ? 0.1132 0.2718 0.3266 -0.0168 -0.0106 -0.0519 468 ILE A CG2   
1317 C CD1   . ILE A 168 ? 0.1482 0.2719 0.3422 -0.0258 0.0175  -0.0346 468 ILE A CD1   
1318 N N     . PHE A 169 ? 0.1160 0.2439 0.2797 -0.0398 0.0190  0.0207  469 PHE A N     
1319 C CA    . PHE A 169 ? 0.1377 0.2368 0.2936 -0.0446 0.0126  0.0189  469 PHE A CA    
1320 C C     . PHE A 169 ? 0.1092 0.2703 0.2994 -0.0252 0.0097  0.0033  469 PHE A C     
1321 O O     . PHE A 169 ? 0.1307 0.2727 0.3145 -0.0258 0.0285  0.0010  469 PHE A O     
1322 C CB    . PHE A 169 ? 0.1560 0.1929 0.3142 0.0065  0.0024  0.0263  469 PHE A CB    
1323 C CG    . PHE A 169 ? 0.1253 0.2085 0.3475 0.0080  -0.0010 0.0081  469 PHE A CG    
1324 C CD1   . PHE A 169 ? 0.1914 0.2010 0.3214 0.0070  0.0179  0.0203  469 PHE A CD1   
1325 C CD2   . PHE A 169 ? 0.1311 0.2469 0.3989 -0.0105 0.0129  -0.0153 469 PHE A CD2   
1326 C CE1   . PHE A 169 ? 0.2021 0.2135 0.3681 -0.0103 -0.0036 0.0162  469 PHE A CE1   
1327 C CE2   . PHE A 169 ? 0.1821 0.2478 0.4159 -0.0242 -0.0198 -0.0214 469 PHE A CE2   
1328 C CZ    . PHE A 169 ? 0.1951 0.2458 0.4209 -0.0188 0.0014  -0.0130 469 PHE A CZ    
1329 N N     . PRO A 170 ? 0.1693 0.2605 0.3098 -0.0549 0.0151  0.0043  470 PRO A N     
1330 C CA    . PRO A 170 ? 0.2323 0.2899 0.3335 -0.0591 0.0210  0.0122  470 PRO A CA    
1331 C C     . PRO A 170 ? 0.2262 0.3210 0.3594 -0.0721 0.0206  -0.0036 470 PRO A C     
1332 O O     . PRO A 170 ? 0.2453 0.4078 0.4038 -0.1452 0.0566  -0.0305 470 PRO A O     
1333 C CB    . PRO A 170 ? 0.2246 0.3225 0.3332 -0.0615 0.0443  0.0312  470 PRO A CB    
1334 C CG    . PRO A 170 ? 0.2018 0.2905 0.3678 -0.0387 0.0049  0.0044  470 PRO A CG    
1335 C CD    . PRO A 170 ? 0.1930 0.3011 0.3234 -0.0520 0.0352  -0.0014 470 PRO A CD    
1336 N N     . THR A 171 ? 0.1467 0.2344 0.3758 -0.0679 0.0328  0.0026  471 THR A N     
1337 C CA    . THR A 171 ? 0.1252 0.3484 0.4126 -0.0646 0.0545  -0.0187 471 THR A CA    
1338 C C     . THR A 171 ? 0.1041 0.3600 0.3810 -0.0488 0.0335  -0.0065 471 THR A C     
1339 O O     . THR A 171 ? 0.1244 0.3733 0.3853 -0.0202 0.0454  -0.0151 471 THR A O     
1340 C CB    . THR A 171 ? 0.1239 0.4012 0.4841 -0.0717 0.0364  -0.0413 471 THR A CB    
1341 O OG1   . THR A 171 ? 0.2012 0.4090 0.4742 -0.0693 0.0027  -0.0784 471 THR A OG1   
1342 C CG2   . THR A 171 ? 0.1820 0.4302 0.5552 -0.0808 0.0322  -0.0466 471 THR A CG2   
1343 N N     . ASP A 172 ? 0.1287 0.2895 0.3527 -0.0492 0.0475  -0.0199 472 ASP A N     
1344 C CA    . ASP A 172 ? 0.1387 0.2916 0.3268 -0.0185 0.0215  0.0037  472 ASP A CA    
1345 C C     . ASP A 172 ? 0.1336 0.2885 0.3154 -0.0190 0.0366  -0.0012 472 ASP A C     
1346 O O     . ASP A 172 ? 0.0954 0.2693 0.3552 -0.0182 0.0368  -0.0117 472 ASP A O     
1347 C CB    . ASP A 172 ? 0.1608 0.3276 0.3244 -0.0191 0.0199  0.0025  472 ASP A CB    
1348 C CG    . ASP A 172 ? 0.1397 0.3551 0.3223 -0.0166 0.0287  -0.0096 472 ASP A CG    
1349 O OD1   . ASP A 172 ? 0.1315 0.4845 0.4160 0.0171  -0.0179 -0.0241 472 ASP A OD1   
1350 O OD2   . ASP A 172 ? 0.1231 0.3049 0.3343 -0.0089 0.0249  -0.0169 472 ASP A OD2   
1351 N N     . LEU A 173 ? 0.1193 0.2765 0.3203 -0.0129 0.0495  -0.0146 473 LEU A N     
1352 C CA    . LEU A 173 ? 0.1226 0.2950 0.3246 -0.0155 0.0323  -0.0177 473 LEU A CA    
1353 C C     . LEU A 173 ? 0.1303 0.2517 0.3313 0.0219  0.0223  -0.0391 473 LEU A C     
1354 O O     . LEU A 173 ? 0.1333 0.2481 0.3185 0.0093  0.0121  -0.0140 473 LEU A O     
1355 C CB    . LEU A 173 ? 0.1907 0.3189 0.3281 -0.0377 0.0518  -0.0433 473 LEU A CB    
1356 C CG    . LEU A 173 ? 0.2008 0.3706 0.3422 -0.0719 0.0315  -0.0287 473 LEU A CG    
1357 C CD1   . LEU A 173 ? 0.2058 0.4310 0.3904 -0.0789 0.0388  -0.0161 473 LEU A CD1   
1358 C CD2   . LEU A 173 ? 0.2438 0.3518 0.3277 -0.0711 0.0483  -0.0570 473 LEU A CD2   
1359 N N     . GLU A 174 ? 0.1052 0.2914 0.3467 -0.0151 0.0010  -0.0138 474 GLU A N     
1360 C CA    . GLU A 174 ? 0.0871 0.2650 0.3957 0.0059  0.0275  -0.0206 474 GLU A CA    
1361 C C     . GLU A 174 ? 0.1072 0.2707 0.3591 -0.0038 0.0174  -0.0126 474 GLU A C     
1362 O O     . GLU A 174 ? 0.1269 0.2303 0.3627 -0.0072 0.0498  -0.0080 474 GLU A O     
1363 C CB    . GLU A 174 ? 0.1016 0.3679 0.4678 0.0325  0.0146  -0.0236 474 GLU A CB    
1364 C CG    . GLU A 174 ? 0.2048 0.4588 0.5328 0.0282  0.0770  -0.0146 474 GLU A CG    
1365 C CD    . GLU A 174 ? 0.4213 0.4964 0.6155 -0.0167 0.1091  -0.0103 474 GLU A CD    
1366 O OE1   . GLU A 174 ? 0.6081 0.5010 0.7222 -0.0331 0.2014  0.0886  474 GLU A OE1   
1367 O OE2   . GLU A 174 ? 0.5518 0.5899 0.6891 -0.0069 0.1908  0.0359  474 GLU A OE2   
1368 N N     . ILE A 175 ? 0.1022 0.2325 0.3536 -0.0152 0.0118  -0.0155 475 ILE A N     
1369 C CA    . ILE A 175 ? 0.1131 0.2193 0.3290 -0.0249 0.0181  -0.0251 475 ILE A CA    
1370 C C     . ILE A 175 ? 0.1412 0.2039 0.3106 -0.0163 0.0118  -0.0083 475 ILE A C     
1371 O O     . ILE A 175 ? 0.1128 0.2478 0.3283 -0.0203 0.0298  0.0072  475 ILE A O     
1372 C CB    . ILE A 175 ? 0.1114 0.2351 0.3302 -0.0227 0.0112  -0.0169 475 ILE A CB    
1373 C CG1   . ILE A 175 ? 0.1279 0.2776 0.3772 -0.0091 0.0013  -0.0060 475 ILE A CG1   
1374 C CG2   . ILE A 175 ? 0.1120 0.2377 0.3579 -0.0142 0.0317  -0.0153 475 ILE A CG2   
1375 C CD1   . ILE A 175 ? 0.1037 0.2771 0.3745 -0.0209 -0.0320 -0.0079 475 ILE A CD1   
1376 N N     . TYR A 176 ? 0.1148 0.2026 0.3076 -0.0148 0.0092  -0.0132 476 TYR A N     
1377 C CA    . TYR A 176 ? 0.1342 0.1831 0.3259 -0.0041 0.0181  -0.0115 476 TYR A CA    
1378 C C     . TYR A 176 ? 0.0765 0.2058 0.3145 -0.0114 0.0378  -0.0100 476 TYR A C     
1379 O O     . TYR A 176 ? 0.0864 0.2112 0.3524 -0.0294 0.0315  -0.0063 476 TYR A O     
1380 C CB    . TYR A 176 ? 0.1314 0.1991 0.3425 -0.0364 0.0107  0.0032  476 TYR A CB    
1381 C CG    . TYR A 176 ? 0.1546 0.2190 0.3589 -0.0260 -0.0121 0.0230  476 TYR A CG    
1382 C CD1   . TYR A 176 ? 0.1631 0.2643 0.3860 -0.0163 -0.0271 0.0341  476 TYR A CD1   
1383 C CD2   . TYR A 176 ? 0.1514 0.2850 0.4159 -0.0103 -0.0378 0.0040  476 TYR A CD2   
1384 C CE1   . TYR A 176 ? 0.2341 0.3347 0.3687 0.0052  -0.0447 0.0356  476 TYR A CE1   
1385 C CE2   . TYR A 176 ? 0.2126 0.3255 0.3935 0.0117  -0.0614 0.0162  476 TYR A CE2   
1386 C CZ    . TYR A 176 ? 0.2449 0.3416 0.3875 -0.0109 -0.0753 0.0237  476 TYR A CZ    
1387 O OH    . TYR A 176 ? 0.2177 0.5119 0.4548 0.0047  -0.0778 0.0568  476 TYR A OH    
1388 N N     . LYS A 177 ? 0.1120 0.2345 0.3326 0.0167  0.0267  -0.0207 477 LYS A N     
1389 C CA    . LYS A 177 ? 0.1372 0.2218 0.3254 -0.0023 0.0195  -0.0249 477 LYS A CA    
1390 C C     . LYS A 177 ? 0.1365 0.2318 0.3181 0.0026  0.0167  -0.0132 477 LYS A C     
1391 O O     . LYS A 177 ? 0.1258 0.2392 0.3497 -0.0129 0.0170  -0.0398 477 LYS A O     
1392 C CB    . LYS A 177 ? 0.1501 0.2353 0.3607 -0.0038 0.0250  -0.0440 477 LYS A CB    
1393 C CG    . LYS A 177 ? 0.1763 0.2979 0.4030 -0.0201 0.0583  -0.0311 477 LYS A CG    
1394 C CD    . LYS A 177 ? 0.1979 0.3547 0.4795 -0.0321 0.0950  -0.0384 477 LYS A CD    
1395 C CE    . LYS A 177 ? 0.2819 0.4356 0.5537 0.0102  0.0684  -0.0250 477 LYS A CE    
1396 N NZ    . LYS A 177 ? 0.3687 0.5514 0.6630 0.0769  0.0842  -0.0535 477 LYS A NZ    
1397 N N     . ALA A 178 ? 0.1126 0.1968 0.3289 0.0136  0.0156  -0.0272 478 ALA A N     
1398 C CA    . ALA A 178 ? 0.1423 0.1501 0.3383 0.0232  0.0087  -0.0196 478 ALA A CA    
1399 C C     . ALA A 178 ? 0.1198 0.1331 0.3287 -0.0025 0.0239  -0.0097 478 ALA A C     
1400 O O     . ALA A 178 ? 0.1476 0.1341 0.3354 -0.0343 0.0156  -0.0088 478 ALA A O     
1401 C CB    . ALA A 178 ? 0.1330 0.2104 0.3495 0.0312  0.0042  -0.0310 478 ALA A CB    
1402 N N     . PHE A 179 ? 0.0999 0.1646 0.3348 0.0154  0.0113  -0.0209 479 PHE A N     
1403 C CA    . PHE A 179 ? 0.0831 0.1408 0.3185 0.0012  0.0059  0.0018  479 PHE A CA    
1404 C C     . PHE A 179 ? 0.0989 0.1513 0.3159 -0.0236 0.0067  -0.0220 479 PHE A C     
1405 O O     . PHE A 179 ? 0.0862 0.1544 0.3253 -0.0172 0.0023  0.0053  479 PHE A O     
1406 C CB    . PHE A 179 ? 0.1062 0.1466 0.3184 -0.0120 0.0045  -0.0108 479 PHE A CB    
1407 C CG    . PHE A 179 ? 0.0921 0.1484 0.3096 -0.0204 0.0038  -0.0174 479 PHE A CG    
1408 C CD1   . PHE A 179 ? 0.1110 0.2298 0.3098 0.0078  0.0099  -0.0160 479 PHE A CD1   
1409 C CD2   . PHE A 179 ? 0.1303 0.1984 0.3049 0.0291  0.0095  -0.0072 479 PHE A CD2   
1410 C CE1   . PHE A 179 ? 0.1187 0.2149 0.3221 0.0389  0.0097  -0.0059 479 PHE A CE1   
1411 C CE2   . PHE A 179 ? 0.1325 0.2018 0.2994 0.0474  0.0107  -0.0136 479 PHE A CE2   
1412 C CZ    . PHE A 179 ? 0.1359 0.2124 0.3014 0.0592  0.0001  -0.0203 479 PHE A CZ    
1413 N N     A SER A 180 ? 0.1227 0.1802 0.3183 -0.0019 0.0083  -0.0172 480 SER A N     
1414 N N     B SER A 180 ? 0.1351 0.1732 0.3188 -0.0081 0.0099  -0.0172 480 SER A N     
1415 C CA    A SER A 180 ? 0.1206 0.1817 0.3330 -0.0139 0.0038  -0.0170 480 SER A CA    
1416 C CA    B SER A 180 ? 0.1485 0.1694 0.3305 -0.0235 0.0077  -0.0163 480 SER A CA    
1417 C C     A SER A 180 ? 0.0980 0.1705 0.3284 -0.0189 0.0028  -0.0173 480 SER A C     
1418 C C     B SER A 180 ? 0.1168 0.1590 0.3300 -0.0191 0.0065  -0.0164 480 SER A C     
1419 O O     A SER A 180 ? 0.0823 0.1620 0.3352 -0.0190 0.0083  -0.0101 480 SER A O     
1420 O O     B SER A 180 ? 0.1147 0.1611 0.3386 -0.0138 0.0046  -0.0106 480 SER A O     
1421 C CB    A SER A 180 ? 0.1617 0.2165 0.3363 -0.0310 0.0007  -0.0100 480 SER A CB    
1422 C CB    B SER A 180 ? 0.1849 0.1788 0.3386 -0.0584 0.0058  -0.0135 480 SER A CB    
1423 O OG    A SER A 180 ? 0.1725 0.2478 0.3717 -0.0061 -0.0287 -0.0055 480 SER A OG    
1424 O OG    B SER A 180 ? 0.2244 0.2279 0.3413 -0.0397 0.0095  0.0072  480 SER A OG    
1425 N N     . SER A 181 ? 0.0834 0.1829 0.3405 -0.0169 0.0141  -0.0281 481 SER A N     
1426 C CA    . SER A 181 ? 0.1234 0.1836 0.3260 -0.0199 0.0015  -0.0291 481 SER A CA    
1427 C C     . SER A 181 ? 0.1431 0.1751 0.3053 0.0054  0.0071  -0.0269 481 SER A C     
1428 O O     . SER A 181 ? 0.1422 0.1747 0.3128 -0.0074 0.0063  -0.0228 481 SER A O     
1429 C CB    . SER A 181 ? 0.1229 0.1898 0.3846 -0.0266 0.0169  -0.0176 481 SER A CB    
1430 O OG    . SER A 181 ? 0.1774 0.2140 0.4579 -0.0189 0.0027  -0.0139 481 SER A OG    
1431 N N     . GLU A 182 ? 0.1111 0.1489 0.3157 0.0060  0.0178  -0.0146 482 GLU A N     
1432 C CA    . GLU A 182 ? 0.1438 0.1511 0.2971 -0.0126 0.0146  0.0020  482 GLU A CA    
1433 C C     . GLU A 182 ? 0.1452 0.1389 0.3176 -0.0060 -0.0017 -0.0088 482 GLU A C     
1434 O O     . GLU A 182 ? 0.1478 0.1640 0.3110 0.0031  0.0101  -0.0091 482 GLU A O     
1435 C CB    . GLU A 182 ? 0.1674 0.1599 0.3111 0.0035  0.0256  0.0022  482 GLU A CB    
1436 C CG    . GLU A 182 ? 0.1637 0.1806 0.3069 0.0073  0.0253  0.0030  482 GLU A CG    
1437 C CD    . GLU A 182 ? 0.1866 0.2075 0.3585 0.0555  0.0236  -0.0103 482 GLU A CD    
1438 O OE1   . GLU A 182 ? 0.1850 0.2404 0.4105 0.0710  0.0049  0.0238  482 GLU A OE1   
1439 O OE2   . GLU A 182 ? 0.2075 0.2230 0.3947 0.0066  0.0091  -0.0063 482 GLU A OE2   
1440 N N     . MET A 183 ? 0.0987 0.1442 0.3029 -0.0168 -0.0094 -0.0108 483 MET A N     
1441 C CA    . MET A 183 ? 0.0973 0.1633 0.3173 -0.0061 0.0132  -0.0070 483 MET A CA    
1442 C C     . MET A 183 ? 0.1115 0.1247 0.3035 -0.0010 0.0159  -0.0183 483 MET A C     
1443 O O     . MET A 183 ? 0.1159 0.1570 0.3078 -0.0007 0.0017  -0.0097 483 MET A O     
1444 C CB    . MET A 183 ? 0.1136 0.1584 0.3265 -0.0003 0.0157  -0.0061 483 MET A CB    
1445 C CG    . MET A 183 ? 0.1274 0.1331 0.3433 0.0117  0.0021  -0.0115 483 MET A CG    
1446 S SD    . MET A 183 ? 0.1587 0.1822 0.3652 -0.0148 -0.0042 0.0088  483 MET A SD    
1447 C CE    . MET A 183 ? 0.1417 0.1758 0.3946 -0.0475 0.0093  -0.0072 483 MET A CE    
1448 N N     . ALA A 184 ? 0.1110 0.1556 0.3033 -0.0172 0.0194  -0.0023 484 ALA A N     
1449 C CA    . ALA A 184 ? 0.1150 0.1674 0.3022 0.0062  0.0142  -0.0099 484 ALA A CA    
1450 C C     . ALA A 184 ? 0.1251 0.1600 0.3222 0.0005  0.0087  -0.0197 484 ALA A C     
1451 O O     . ALA A 184 ? 0.1318 0.1493 0.3490 -0.0241 0.0070  -0.0326 484 ALA A O     
1452 C CB    . ALA A 184 ? 0.1471 0.1956 0.2931 0.0245  0.0164  -0.0172 484 ALA A CB    
1453 N N     . LYS A 185 ? 0.1270 0.1516 0.3463 -0.0144 0.0108  -0.0186 485 LYS A N     
1454 C CA    . LYS A 185 ? 0.1571 0.1184 0.3985 0.0018  0.0112  -0.0247 485 LYS A CA    
1455 C C     . LYS A 185 ? 0.1269 0.1519 0.3438 -0.0129 -0.0086 -0.0042 485 LYS A C     
1456 O O     . LYS A 185 ? 0.1606 0.1150 0.3686 -0.0037 0.0024  -0.0214 485 LYS A O     
1457 C CB    . LYS A 185 ? 0.1676 0.2099 0.4503 -0.0213 -0.0139 0.0163  485 LYS A CB    
1458 C CG    . LYS A 185 ? 0.1777 0.2589 0.5176 -0.0325 0.0073  0.0375  485 LYS A CG    
1459 C CD    . LYS A 185 ? 0.2376 0.2934 0.5779 0.0359  -0.0082 0.0766  485 LYS A CD    
1460 C CE    . LYS A 185 ? 0.2844 0.4739 0.6590 -0.0058 -0.0489 0.0569  485 LYS A CE    
1461 N NZ    . LYS A 185 ? 0.4634 0.5168 0.6863 0.0220  -0.0620 0.0731  485 LYS A NZ    
1462 N N     . ARG A 186 ? 0.1020 0.1415 0.3423 0.0081  -0.0049 0.0088  486 ARG A N     
1463 C CA    . ARG A 186 ? 0.1235 0.1134 0.3386 -0.0099 0.0159  0.0086  486 ARG A CA    
1464 C C     . ARG A 186 ? 0.1172 0.1301 0.3291 -0.0197 0.0027  0.0106  486 ARG A C     
1465 O O     . ARG A 186 ? 0.1166 0.1480 0.3409 -0.0270 0.0166  0.0101  486 ARG A O     
1466 C CB    . ARG A 186 ? 0.1562 0.1467 0.3354 -0.0208 0.0107  0.0047  486 ARG A CB    
1467 C CG    . ARG A 186 ? 0.1388 0.1480 0.3487 -0.0010 0.0142  0.0040  486 ARG A CG    
1468 C CD    . ARG A 186 ? 0.1613 0.1694 0.3545 -0.0025 -0.0073 0.0114  486 ARG A CD    
1469 N NE    . ARG A 186 ? 0.1561 0.2062 0.3427 0.0262  0.0017  0.0112  486 ARG A NE    
1470 C CZ    . ARG A 186 ? 0.1751 0.1337 0.3307 0.0102  0.0043  0.0127  486 ARG A CZ    
1471 N NH1   . ARG A 186 ? 0.1958 0.2087 0.3282 0.0295  0.0337  -0.0203 486 ARG A NH1   
1472 N NH2   . ARG A 186 ? 0.2150 0.1624 0.3298 0.0268  -0.0207 -0.0053 486 ARG A NH2   
1473 N N     A SER A 187 ? 0.1406 0.1511 0.3457 -0.0066 0.0058  0.0138  487 SER A N     
1474 N N     B SER A 187 ? 0.1085 0.0965 0.3222 0.0022  -0.0050 0.0020  487 SER A N     
1475 C CA    A SER A 187 ? 0.1704 0.1848 0.3521 -0.0009 -0.0026 0.0071  487 SER A CA    
1476 C CA    B SER A 187 ? 0.1192 0.0787 0.3077 -0.0038 -0.0063 -0.0074 487 SER A CA    
1477 C C     A SER A 187 ? 0.1464 0.1530 0.3628 0.0139  0.0109  0.0104  487 SER A C     
1478 C C     B SER A 187 ? 0.1146 0.0570 0.3265 0.0056  -0.0025 -0.0042 487 SER A C     
1479 O O     A SER A 187 ? 0.1589 0.2059 0.3589 0.0195  -0.0010 0.0359  487 SER A O     
1480 O O     B SER A 187 ? 0.1351 0.0980 0.3312 0.0031  -0.0197 0.0012  487 SER A O     
1481 C CB    A SER A 187 ? 0.1999 0.2057 0.3822 -0.0111 -0.0173 0.0221  487 SER A CB    
1482 C CB    B SER A 187 ? 0.1189 0.0580 0.3029 0.0054  -0.0153 -0.0050 487 SER A CB    
1483 O OG    A SER A 187 ? 0.2651 0.3128 0.3930 -0.0340 -0.0386 0.0231  487 SER A OG    
1484 O OG    B SER A 187 ? 0.0935 0.0613 0.2746 -0.0113 -0.0090 -0.0043 487 SER A OG    
1485 N N     A LYS A 188 ? 0.1422 0.1564 0.3404 0.0080  0.0227  -0.0061 488 LYS A N     
1486 N N     B LYS A 188 ? 0.1074 0.1023 0.3277 0.0110  0.0031  -0.0130 488 LYS A N     
1487 C CA    A LYS A 188 ? 0.1627 0.1400 0.3582 -0.0015 0.0309  -0.0247 488 LYS A CA    
1488 C CA    B LYS A 188 ? 0.1343 0.1222 0.3545 -0.0002 0.0023  -0.0346 488 LYS A CA    
1489 C C     A LYS A 188 ? 0.1619 0.1320 0.3510 0.0061  0.0164  -0.0162 488 LYS A C     
1490 C C     B LYS A 188 ? 0.1360 0.1303 0.3534 0.0096  0.0025  -0.0216 488 LYS A C     
1491 O O     A LYS A 188 ? 0.1717 0.1141 0.3587 -0.0079 0.0048  -0.0100 488 LYS A O     
1492 O O     B LYS A 188 ? 0.1171 0.1600 0.3850 0.0101  -0.0072 -0.0256 488 LYS A O     
1493 C CB    A LYS A 188 ? 0.1686 0.1507 0.3791 -0.0120 0.0417  -0.0426 488 LYS A CB    
1494 C CB    B LYS A 188 ? 0.1387 0.1482 0.3847 -0.0003 0.0025  -0.0459 488 LYS A CB    
1495 C CG    A LYS A 188 ? 0.2251 0.1958 0.3930 -0.0158 0.0525  -0.0286 488 LYS A CG    
1496 C CG    B LYS A 188 ? 0.2153 0.1963 0.4066 0.0087  -0.0158 -0.0588 488 LYS A CG    
1497 C CD    A LYS A 188 ? 0.2601 0.2595 0.4266 0.0053  0.0714  -0.0291 488 LYS A CD    
1498 C CD    B LYS A 188 ? 0.2543 0.2432 0.4528 0.0325  -0.0067 -0.0610 488 LYS A CD    
1499 C CE    A LYS A 188 ? 0.2927 0.3230 0.4776 -0.0041 0.0628  -0.0066 488 LYS A CE    
1500 C CE    B LYS A 188 ? 0.3216 0.2440 0.4892 0.0432  -0.0128 -0.0660 488 LYS A CE    
1501 N NZ    A LYS A 188 ? 0.3216 0.3314 0.4999 -0.0074 0.0662  -0.0277 488 LYS A NZ    
1502 N NZ    B LYS A 188 ? 0.3816 0.3301 0.5327 0.0196  0.0074  -0.0447 488 LYS A NZ    
1503 N N     . MET A 189 ? 0.1390 0.1368 0.3398 -0.0132 0.0035  -0.0110 489 MET A N     
1504 C CA    . MET A 189 ? 0.1433 0.1212 0.3536 -0.0017 0.0162  0.0052  489 MET A CA    
1505 C C     . MET A 189 ? 0.1212 0.1479 0.3363 -0.0302 -0.0064 -0.0060 489 MET A C     
1506 O O     . MET A 189 ? 0.1728 0.1152 0.3731 -0.0453 -0.0055 -0.0095 489 MET A O     
1507 C CB    . MET A 189 ? 0.1568 0.1516 0.3818 -0.0254 -0.0121 0.0271  489 MET A CB    
1508 C CG    . MET A 189 ? 0.1940 0.2347 0.4006 -0.0247 0.0009  0.0605  489 MET A CG    
1509 S SD    . MET A 189 ? 0.2447 0.2767 0.4365 -0.0554 -0.0061 0.0624  489 MET A SD    
1510 C CE    . MET A 189 ? 0.3585 0.2523 0.4311 0.0126  0.0438  0.0482  489 MET A CE    
1511 N N     . LEU A 190 ? 0.1568 0.1364 0.3353 -0.0166 0.0130  0.0038  490 LEU A N     
1512 C CA    . LEU A 190 ? 0.1500 0.1490 0.3317 -0.0230 0.0155  0.0106  490 LEU A CA    
1513 C C     . LEU A 190 ? 0.1437 0.1250 0.3355 -0.0177 0.0227  0.0001  490 LEU A C     
1514 O O     . LEU A 190 ? 0.1001 0.1444 0.3652 -0.0314 0.0210  -0.0036 490 LEU A O     
1515 C CB    . LEU A 190 ? 0.1480 0.1772 0.3332 -0.0338 0.0304  -0.0024 490 LEU A CB    
1516 C CG    . LEU A 190 ? 0.2170 0.1968 0.3510 -0.0685 0.0174  -0.0013 490 LEU A CG    
1517 C CD1   . LEU A 190 ? 0.2648 0.2736 0.3632 -0.0637 0.0204  -0.0260 490 LEU A CD1   
1518 C CD2   . LEU A 190 ? 0.2936 0.2708 0.3380 -0.1199 0.0157  0.0209  490 LEU A CD2   
1519 N N     . SER A 191 ? 0.1743 0.0891 0.3335 -0.0058 0.0107  -0.0065 491 SER A N     
1520 C CA    . SER A 191 ? 0.1432 0.1304 0.3444 -0.0333 0.0023  0.0006  491 SER A CA    
1521 C C     . SER A 191 ? 0.1653 0.1300 0.3756 -0.0086 -0.0227 0.0015  491 SER A C     
1522 O O     . SER A 191 ? 0.1681 0.1672 0.4207 0.0004  -0.0480 0.0187  491 SER A O     
1523 C CB    . SER A 191 ? 0.1970 0.1500 0.3704 -0.0483 -0.0355 0.0050  491 SER A CB    
1524 O OG    . SER A 191 ? 0.1975 0.1528 0.3790 -0.0373 -0.0144 0.0091  491 SER A OG    
1525 N N     . LEU A 192 ? 0.1254 0.1085 0.3649 -0.0020 0.0042  -0.0131 492 LEU A N     
1526 C CA    . LEU A 192 ? 0.1322 0.1239 0.3742 0.0224  0.0299  -0.0116 492 LEU A CA    
1527 C C     . LEU A 192 ? 0.1439 0.1315 0.3750 -0.0197 0.0240  -0.0168 492 LEU A C     
1528 O O     . LEU A 192 ? 0.1754 0.1369 0.4319 -0.0021 0.0704  0.0224  492 LEU A O     
1529 C CB    . LEU A 192 ? 0.0843 0.1035 0.3883 0.0010  0.0350  -0.0174 492 LEU A CB    
1530 C CG    . LEU A 192 ? 0.1406 0.1351 0.3741 0.0008  0.0193  -0.0304 492 LEU A CG    
1531 C CD1   . LEU A 192 ? 0.2144 0.1685 0.3609 -0.0100 0.0113  -0.0408 492 LEU A CD1   
1532 C CD2   . LEU A 192 ? 0.1478 0.1338 0.3872 -0.0194 0.0059  -0.0331 492 LEU A CD2   
1533 N N     . ASN A 193 ? 0.1164 0.1468 0.3253 -0.0109 0.0168  0.0025  493 ASN A N     
1534 C CA    . ASN A 193 ? 0.1080 0.1320 0.3231 -0.0217 0.0042  -0.0031 493 ASN A CA    
1535 C C     . ASN A 193 ? 0.1098 0.1550 0.2974 -0.0229 0.0018  -0.0068 493 ASN A C     
1536 O O     . ASN A 193 ? 0.1316 0.1580 0.3119 -0.0234 0.0116  -0.0153 493 ASN A O     
1537 C CB    . ASN A 193 ? 0.1081 0.1437 0.3275 -0.0180 0.0137  0.0056  493 ASN A CB    
1538 C CG    . ASN A 193 ? 0.1520 0.2179 0.3176 -0.0306 0.0015  -0.0251 493 ASN A CG    
1539 O OD1   . ASN A 193 ? 0.1472 0.2417 0.3745 -0.0066 -0.0168 -0.0689 493 ASN A OD1   
1540 N ND2   . ASN A 193 ? 0.1326 0.2550 0.3224 -0.0328 -0.0024 -0.0038 493 ASN A ND2   
1541 N N     . ASN A 194 ? 0.1229 0.1783 0.2780 -0.0334 -0.0033 -0.0057 494 ASN A N     
1542 C CA    . ASN A 194 ? 0.1154 0.1746 0.2866 -0.0249 -0.0101 0.0003  494 ASN A CA    
1543 C C     . ASN A 194 ? 0.1308 0.1699 0.2776 -0.0083 -0.0060 -0.0059 494 ASN A C     
1544 O O     . ASN A 194 ? 0.1388 0.1645 0.2969 -0.0154 -0.0094 0.0008  494 ASN A O     
1545 C CB    . ASN A 194 ? 0.1092 0.1662 0.3150 -0.0142 0.0068  0.0105  494 ASN A CB    
1546 C CG    . ASN A 194 ? 0.1786 0.1771 0.3337 0.0119  -0.0040 0.0059  494 ASN A CG    
1547 O OD1   . ASN A 194 ? 0.2576 0.2112 0.4414 -0.0463 -0.0626 -0.0085 494 ASN A OD1   
1548 N ND2   . ASN A 194 ? 0.2323 0.1789 0.3374 0.0057  0.0016  0.0084  494 ASN A ND2   
1549 N N     . TYR A 195 ? 0.1305 0.1613 0.2844 -0.0152 -0.0130 0.0120  495 TYR A N     
1550 C CA    . TYR A 195 ? 0.1531 0.1613 0.3035 -0.0426 -0.0088 0.0088  495 TYR A CA    
1551 C C     . TYR A 195 ? 0.1514 0.1975 0.3048 -0.0526 -0.0202 0.0255  495 TYR A C     
1552 O O     . TYR A 195 ? 0.1282 0.1495 0.3265 -0.0533 -0.0220 0.0130  495 TYR A O     
1553 C CB    . TYR A 195 ? 0.1220 0.1633 0.2883 -0.0499 -0.0186 0.0106  495 TYR A CB    
1554 C CG    . TYR A 195 ? 0.1227 0.1634 0.2961 -0.0330 -0.0128 0.0000  495 TYR A CG    
1555 C CD1   . TYR A 195 ? 0.1387 0.1677 0.2948 -0.0091 -0.0004 0.0009  495 TYR A CD1   
1556 C CD2   . TYR A 195 ? 0.1525 0.1877 0.2803 -0.0173 -0.0188 0.0037  495 TYR A CD2   
1557 C CE1   . TYR A 195 ? 0.1362 0.1775 0.3012 0.0098  -0.0176 0.0062  495 TYR A CE1   
1558 C CE2   . TYR A 195 ? 0.1444 0.1827 0.3034 -0.0140 -0.0202 0.0125  495 TYR A CE2   
1559 C CZ    . TYR A 195 ? 0.1437 0.1866 0.3056 -0.0252 -0.0284 -0.0077 495 TYR A CZ    
1560 O OH    . TYR A 195 ? 0.1210 0.2778 0.3492 -0.0181 -0.0220 -0.0102 495 TYR A OH    
1561 N N     A SER A 196 ? 0.1170 0.1878 0.3389 -0.0488 -0.0245 0.0439  496 SER A N     
1562 N N     B SER A 196 ? 0.1052 0.2217 0.3456 -0.0571 -0.0236 0.0507  496 SER A N     
1563 C CA    A SER A 196 ? 0.1299 0.2072 0.3649 -0.0576 -0.0285 0.0412  496 SER A CA    
1564 C CA    B SER A 196 ? 0.1094 0.2738 0.3775 -0.0635 -0.0328 0.0462  496 SER A CA    
1565 C C     A SER A 196 ? 0.1757 0.2138 0.3959 -0.0793 -0.0464 0.0462  496 SER A C     
1566 C C     B SER A 196 ? 0.1446 0.2732 0.4018 -0.0738 -0.0516 0.0482  496 SER A C     
1567 O O     A SER A 196 ? 0.2373 0.2339 0.3753 -0.0764 -0.0527 0.0484  496 SER A O     
1568 O O     B SER A 196 ? 0.1402 0.3044 0.3985 -0.0483 -0.0567 0.0477  496 SER A O     
1569 C CB    A SER A 196 ? 0.1414 0.2226 0.3849 -0.0449 -0.0196 0.0349  496 SER A CB    
1570 C CB    B SER A 196 ? 0.1420 0.3324 0.4035 -0.0485 -0.0227 0.0435  496 SER A CB    
1571 O OG    A SER A 196 ? 0.1530 0.2187 0.4152 -0.0085 -0.0012 0.0384  496 SER A OG    
1572 O OG    B SER A 196 ? 0.1099 0.4112 0.4388 -0.0251 -0.0254 0.0494  496 SER A OG    
1573 N N     . VAL A 197 ? 0.2671 0.2745 0.4161 -0.0677 -0.0670 0.0440  497 VAL A N     
1574 C CA    . VAL A 197 ? 0.3212 0.2410 0.5103 -0.0788 -0.0655 0.0548  497 VAL A CA    
1575 C C     . VAL A 197 ? 0.3451 0.2359 0.6819 -0.1097 -0.0511 0.0606  497 VAL A C     
1576 O O     . VAL A 197 ? 0.2909 0.3140 0.7809 -0.1177 -0.1722 0.0192  497 VAL A O     
1577 C CB    . VAL A 197 ? 0.3904 0.2884 0.5982 -0.0581 -0.0417 0.0012  497 VAL A CB    
1578 C CG1   . VAL A 197 ? 0.5131 0.3115 0.6441 -0.0295 -0.0412 0.0212  497 VAL A CG1   
1579 C CG2   . VAL A 197 ? 0.4003 0.3867 0.6503 -0.0501 -0.0663 -0.0174 497 VAL A CG2   
1580 O OXT   . VAL A 197 ? 0.5885 0.2735 0.8468 -0.1728 -0.0204 0.0576  497 VAL A OXT   
1581 N N1    A APR B .   ? 0.0685 0.1290 0.3088 0.0082  0.0107  -0.0017 501 APR A N1    
1582 C C2    A APR B .   ? 0.0820 0.1372 0.3038 -0.0035 0.0067  -0.0023 501 APR A C2    
1583 N N3    A APR B .   ? 0.0588 0.1248 0.3021 -0.0057 0.0029  -0.0060 501 APR A N3    
1584 C C4    A APR B .   ? 0.0620 0.1339 0.3011 0.0089  0.0005  -0.0052 501 APR A C4    
1585 C C5    A APR B .   ? 0.0684 0.1423 0.2966 0.0115  -0.0112 -0.0146 501 APR A C5    
1586 C C6    A APR B .   ? 0.0759 0.1197 0.3011 0.0045  0.0048  -0.0134 501 APR A C6    
1587 N N6    A APR B .   ? 0.0618 0.1141 0.3002 -0.0139 0.0052  0.0050  501 APR A N6    
1588 N N7    A APR B .   ? 0.0709 0.1393 0.3052 0.0274  -0.0124 -0.0066 501 APR A N7    
1589 C C8    A APR B .   ? 0.0319 0.1355 0.3046 0.0333  -0.0028 -0.0174 501 APR A C8    
1590 N N9    A APR B .   ? 0.0825 0.1118 0.2938 0.0175  -0.0003 -0.0154 501 APR A N9    
1591 C "C1'" A APR B .   ? 0.0775 0.1095 0.2917 0.0097  0.0192  -0.0205 501 APR A "C1'" 
1592 C "C2'" A APR B .   ? 0.0794 0.1340 0.3076 0.0078  0.0124  -0.0172 501 APR A "C2'" 
1593 O "O2'" A APR B .   ? 0.1021 0.1425 0.3166 0.0088  0.0257  -0.0181 501 APR A "O2'" 
1594 C "C3'" A APR B .   ? 0.0507 0.1223 0.3064 0.0218  0.0182  -0.0158 501 APR A "C3'" 
1595 O "O3'" A APR B .   ? 0.0856 0.1535 0.3104 -0.0089 0.0127  -0.0292 501 APR A "O3'" 
1596 O "O4'" A APR B .   ? 0.0953 0.1195 0.2965 0.0113  0.0296  -0.0135 501 APR A "O4'" 
1597 C "C4'" A APR B .   ? 0.0338 0.1244 0.3053 0.0032  0.0154  -0.0133 501 APR A "C4'" 
1598 C "C5'" A APR B .   ? 0.0316 0.1446 0.3057 0.0054  0.0248  -0.0062 501 APR A "C5'" 
1599 O "O5'" A APR B .   ? 0.0389 0.1607 0.3197 -0.0049 0.0196  0.0080  501 APR A "O5'" 
1600 P PA    A APR B .   ? 0.0849 0.1369 0.3338 0.0146  0.0037  -0.0110 501 APR A PA    
1601 O O1A   A APR B .   ? 0.0863 0.1171 0.3406 -0.0084 -0.0052 0.0022  501 APR A O1A   
1602 O O2A   A APR B .   ? 0.0633 0.1510 0.3500 0.0163  0.0244  -0.0246 501 APR A O2A   
1603 O O3A   A APR B .   ? 0.0738 0.1433 0.3161 0.0126  0.0047  -0.0142 501 APR A O3A   
1604 P PB    A APR B .   ? 0.1014 0.1458 0.3163 0.0200  0.0035  -0.0106 501 APR A PB    
1605 O O1B   A APR B .   ? 0.1222 0.1113 0.3084 0.0051  0.0026  -0.0171 501 APR A O1B   
1606 O O2B   A APR B .   ? 0.0895 0.1218 0.2695 0.0238  0.0085  -0.0076 501 APR A O2B   
1607 O O5D   A APR B .   ? 0.1042 0.1566 0.3067 0.0081  0.0277  -0.0119 501 APR A O5D   
1608 C C5D   A APR B .   ? 0.1176 0.1998 0.3377 0.0359  0.0178  -0.0329 501 APR A C5D   
1609 O O4D   A APR B .   ? 0.1557 0.2313 0.3438 0.0152  0.0332  -0.0183 501 APR A O4D   
1610 O O1D   A APR B .   ? 0.1371 0.2301 0.3770 0.0138  0.0179  -0.0312 501 APR A O1D   
1611 C C1D   A APR B .   ? 0.1441 0.2405 0.3692 0.0220  0.0228  -0.0242 501 APR A C1D   
1612 O O2D   A APR B .   ? 0.2023 0.1953 0.4041 0.0775  -0.0286 0.0109  501 APR A O2D   
1613 C C2D   A APR B .   ? 0.1269 0.2233 0.3628 0.0491  -0.0014 -0.0301 501 APR A C2D   
1614 O O3D   A APR B .   ? 0.1769 0.2574 0.3890 -0.0249 -0.0027 -0.0221 501 APR A O3D   
1615 C C3D   A APR B .   ? 0.1389 0.2228 0.3645 0.0309  0.0097  -0.0322 501 APR A C3D   
1616 C C4D   A APR B .   ? 0.1485 0.2091 0.3441 0.0116  0.0120  -0.0313 501 APR A C4D   
1617 N N1    B AR6 C .   ? 0.1242 0.1620 0.3527 -0.0101 0.0297  -0.0125 502 AR6 A N1    
1618 C C2    B AR6 C .   ? 0.1447 0.1710 0.3506 -0.0256 0.0226  -0.0109 502 AR6 A C2    
1619 N N3    B AR6 C .   ? 0.1564 0.1695 0.3523 -0.0241 0.0060  -0.0104 502 AR6 A N3    
1620 C C4    B AR6 C .   ? 0.1382 0.1924 0.3421 -0.0144 0.0205  -0.0046 502 AR6 A C4    
1621 C C5    B AR6 C .   ? 0.1248 0.1851 0.3366 0.0109  0.0274  -0.0186 502 AR6 A C5    
1622 C C6    B AR6 C .   ? 0.1381 0.1654 0.3542 -0.0002 0.0180  -0.0159 502 AR6 A C6    
1623 N N6    B AR6 C .   ? 0.1365 0.1545 0.3554 0.0144  0.0198  -0.0054 502 AR6 A N6    
1624 N N7    B AR6 C .   ? 0.1590 0.1986 0.3171 -0.0051 0.0148  0.0048  502 AR6 A N7    
1625 C C8    B AR6 C .   ? 0.1298 0.1995 0.3398 -0.0002 0.0257  -0.0061 502 AR6 A C8    
1626 N N9    B AR6 C .   ? 0.1632 0.1898 0.3311 -0.0066 0.0181  -0.0037 502 AR6 A N9    
1627 P PA    B AR6 C .   ? 0.1032 0.2012 0.3789 -0.0169 -0.0033 -0.0071 502 AR6 A PA    
1628 P PB    B AR6 C .   ? 0.1263 0.2203 0.3569 -0.0012 0.0009  0.0016  502 AR6 A PB    
1629 C "C1'" B AR6 C .   ? 0.1622 0.1771 0.3523 -0.0090 0.0110  0.0187  502 AR6 A "C1'" 
1630 O O1A   B AR6 C .   ? 0.1164 0.1673 0.3409 0.0005  -0.0002 -0.0237 502 AR6 A O1A   
1631 O O1B   B AR6 C .   ? 0.1399 0.1998 0.3386 0.0105  0.0034  0.0073  502 AR6 A O1B   
1632 C C1D   B AR6 C .   ? 0.2239 0.2727 0.3974 -0.0191 -0.0171 -0.0232 502 AR6 A C1D   
1633 O O1D   B AR6 C .   ? 0.2174 0.3550 0.4107 -0.0128 -0.0294 -0.0611 502 AR6 A O1D   
1634 C "C2'" B AR6 C .   ? 0.1748 0.1844 0.3658 -0.0102 0.0057  0.0223  502 AR6 A "C2'" 
1635 O "O2'" B AR6 C .   ? 0.1654 0.1627 0.3934 -0.0270 0.0212  0.0356  502 AR6 A "O2'" 
1636 O O2A   B AR6 C .   ? 0.1112 0.1719 0.3635 -0.0351 -0.0039 0.0122  502 AR6 A O2A   
1637 O O2B   B AR6 C .   ? 0.0988 0.2110 0.3647 0.0379  -0.0054 0.0035  502 AR6 A O2B   
1638 C C2D   B AR6 C .   ? 0.2241 0.2859 0.3990 -0.0293 -0.0092 -0.0053 502 AR6 A C2D   
1639 O O2D   B AR6 C .   ? 0.1256 0.2701 0.4023 -0.0420 -0.0269 0.0218  502 AR6 A O2D   
1640 C "C3'" B AR6 C .   ? 0.1701 0.1842 0.3733 -0.0075 0.0004  0.0349  502 AR6 A "C3'" 
1641 O "O3'" B AR6 C .   ? 0.1189 0.2275 0.3633 0.0010  -0.0114 0.0276  502 AR6 A "O3'" 
1642 O O3A   B AR6 C .   ? 0.0794 0.2232 0.3533 -0.0149 -0.0016 0.0002  502 AR6 A O3A   
1643 C C3D   B AR6 C .   ? 0.2264 0.2873 0.3940 -0.0247 -0.0100 0.0064  502 AR6 A C3D   
1644 O O3D   B AR6 C .   ? 0.1890 0.3797 0.4120 -0.0075 -0.0098 0.0441  502 AR6 A O3D   
1645 C "C4'" B AR6 C .   ? 0.1619 0.1688 0.3698 -0.0250 0.0002  0.0240  502 AR6 A "C4'" 
1646 O "O4'" B AR6 C .   ? 0.1787 0.1859 0.3643 -0.0141 0.0060  0.0342  502 AR6 A "O4'" 
1647 C C4D   B AR6 C .   ? 0.2296 0.2381 0.3799 -0.0221 -0.0195 -0.0014 502 AR6 A C4D   
1648 O O4D   B AR6 C .   ? 0.2235 0.2967 0.3700 -0.0251 0.0078  -0.0283 502 AR6 A O4D   
1649 C "C5'" B AR6 C .   ? 0.1820 0.1769 0.3646 -0.0026 -0.0031 0.0328  502 AR6 A "C5'" 
1650 O "O5'" B AR6 C .   ? 0.1862 0.1965 0.3642 -0.0023 0.0005  0.0315  502 AR6 A "O5'" 
1651 C C5D   B AR6 C .   ? 0.2095 0.2060 0.3820 -0.0060 -0.0204 -0.0027 502 AR6 A C5D   
1652 O O5D   B AR6 C .   ? 0.1553 0.1953 0.3736 0.0035  -0.0094 -0.0006 502 AR6 A O5D   
1653 O O     . HOH D .   ? 0.2331 0.1426 0.3825 -0.0637 -0.0321 0.0688  601 HOH A O     
1654 O O     . HOH D .   ? 0.2431 0.5193 0.7546 0.0804  -0.0712 -0.2875 602 HOH A O     
1655 O O     . HOH D .   ? 0.7393 0.3932 0.6066 -0.1369 0.1756  -0.1739 603 HOH A O     
1656 O O     . HOH D .   ? 0.3843 0.4972 0.5140 0.0025  -0.0321 -0.1379 604 HOH A O     
1657 O O     . HOH D .   ? 0.4287 0.2304 0.6510 0.0392  0.1100  0.0230  605 HOH A O     
1658 O O     . HOH D .   ? 0.2494 0.4793 0.6196 0.0964  -0.0314 -0.0129 606 HOH A O     
1659 O O     . HOH D .   ? 0.1346 0.1309 0.3540 0.0125  0.0028  -0.0162 607 HOH A O     
1660 O O     . HOH D .   ? 0.2349 0.3513 0.5528 0.0481  -0.0946 0.0227  608 HOH A O     
1661 O O     . HOH D .   ? 0.2368 0.3810 0.6293 -0.1220 -0.0448 -0.0220 609 HOH A O     
1662 O O     . HOH D .   ? 0.9129 0.2361 0.5396 0.0442  -0.1837 -0.0193 610 HOH A O     
1663 O O     . HOH D .   ? 0.4399 0.2022 0.4447 0.0415  -0.0952 -0.0665 611 HOH A O     
1664 O O     . HOH D .   ? 0.4160 0.2815 0.6190 0.0302  -0.0934 0.0933  612 HOH A O     
1665 O O     . HOH D .   ? 0.4483 0.1875 0.4434 -0.0556 -0.0164 0.0095  613 HOH A O     
1666 O O     . HOH D .   ? 0.4537 0.2904 1.0782 0.0636  0.0474  -0.0432 614 HOH A O     
1667 O O     . HOH D .   ? 0.1381 0.2357 0.3505 -0.0319 0.0164  -0.0154 615 HOH A O     
1668 O O     . HOH D .   ? 0.3049 0.2973 0.4029 -0.0172 -0.0634 0.0251  616 HOH A O     
1669 O O     . HOH D .   ? 0.3666 0.5095 0.5770 -0.1553 -0.0280 0.0781  617 HOH A O     
1670 O O     . HOH D .   ? 0.5255 0.4232 0.5896 0.0524  0.1396  0.0243  618 HOH A O     
1671 O O     . HOH D .   ? 0.2350 0.4023 0.5728 -0.0103 -0.0031 0.1724  619 HOH A O     
1672 O O     . HOH D .   ? 0.1703 0.2383 0.3468 0.0297  0.0299  0.0365  620 HOH A O     
1673 O O     . HOH D .   ? 0.3553 0.1564 0.5249 -0.0149 -0.0151 -0.0417 621 HOH A O     
1674 O O     . HOH D .   ? 0.4246 0.3746 0.5333 0.0228  -0.0135 0.0292  622 HOH A O     
1675 O O     . HOH D .   ? 0.4967 0.5415 1.1463 0.2973  0.0348  0.2122  623 HOH A O     
1676 O O     . HOH D .   ? 1.0060 0.5934 0.6937 0.0718  -0.0793 -0.1980 624 HOH A O     
1677 O O     . HOH D .   ? 0.6963 0.6224 0.4924 0.1900  -0.2101 0.0908  625 HOH A O     
1678 O O     . HOH D .   ? 0.3167 0.2519 0.4197 0.0144  0.0073  0.0669  626 HOH A O     
1679 O O     . HOH D .   ? 0.0803 0.1620 0.3231 0.0004  -0.0075 -0.0050 627 HOH A O     
1680 O O     . HOH D .   ? 0.3014 0.5496 0.8235 0.0275  -0.0413 0.1916  628 HOH A O     
1681 O O     . HOH D .   ? 0.2876 0.3421 0.5225 -0.0068 -0.0348 -0.0772 629 HOH A O     
1682 O O     . HOH D .   ? 0.1025 0.2199 0.3140 0.0128  -0.0043 -0.0038 630 HOH A O     
1683 O O     . HOH D .   ? 0.4383 0.4046 0.4794 0.1338  0.0281  0.0576  631 HOH A O     
1684 O O     . HOH D .   ? 0.2161 0.2420 0.3976 -0.0163 -0.0105 -0.0610 632 HOH A O     
1685 O O     . HOH D .   ? 0.6445 0.3944 0.4566 0.2125  0.1068  0.0579  633 HOH A O     
1686 O O     . HOH D .   ? 0.1955 0.3736 0.5395 -0.0087 0.0434  0.0656  634 HOH A O     
1687 O O     . HOH D .   ? 0.4158 0.2184 0.5894 -0.0015 0.2059  -0.0295 635 HOH A O     
1688 O O     . HOH D .   ? 0.2985 0.2833 0.6980 -0.0649 0.0194  0.1390  636 HOH A O     
1689 O O     . HOH D .   ? 0.7018 0.0753 0.5952 0.0195  0.1708  -0.0514 637 HOH A O     
1690 O O     . HOH D .   ? 0.1495 0.1786 0.3160 -0.0433 -0.0171 -0.0043 638 HOH A O     
1691 O O     . HOH D .   ? 0.1712 0.4437 0.5970 -0.0187 -0.0679 0.0640  639 HOH A O     
1692 O O     . HOH D .   ? 0.2728 0.2283 0.3646 -0.0118 0.0213  -0.0113 640 HOH A O     
1693 O O     . HOH D .   ? 0.4159 0.3502 0.7586 -0.0697 -0.1239 -0.0564 641 HOH A O     
1694 O O     . HOH D .   ? 0.2248 0.1591 0.3520 0.0730  -0.0468 -0.0041 642 HOH A O     
1695 O O     . HOH D .   ? 0.2448 0.2491 0.5884 0.0414  0.1426  0.0737  643 HOH A O     
1696 O O     . HOH D .   ? 0.4651 0.4019 0.4809 0.0068  0.0376  0.1490  644 HOH A O     
1697 O O     . HOH D .   ? 0.2615 0.5362 0.5776 0.0298  -0.0853 -0.0597 645 HOH A O     
1698 O O     . HOH D .   ? 0.4583 0.4164 0.6205 0.2055  -0.0873 -0.0367 646 HOH A O     
1699 O O     . HOH D .   ? 0.7197 0.3936 0.4638 -0.0397 -0.1778 0.0434  647 HOH A O     
1700 O O     . HOH D .   ? 0.5772 0.2719 0.5344 0.1311  -0.0851 0.0559  648 HOH A O     
1701 O O     . HOH D .   ? 0.5496 0.2965 0.4945 0.0822  0.2060  -0.0172 649 HOH A O     
1702 O O     . HOH D .   ? 0.4551 0.6049 0.7215 0.0794  -0.1126 -0.1326 650 HOH A O     
1703 O O     . HOH D .   ? 0.2036 0.3339 0.4142 0.0093  0.0192  0.0161  651 HOH A O     
1704 O O     . HOH D .   ? 0.2221 0.1977 0.3754 -0.0020 0.0068  0.0165  652 HOH A O     
1705 O O     . HOH D .   ? 0.4960 0.4631 0.4846 0.2123  0.1082  -0.0091 653 HOH A O     
1706 O O     . HOH D .   ? 0.5568 0.4177 0.4744 -0.3831 0.1785  -0.2181 654 HOH A O     
1707 O O     . HOH D .   ? 0.4717 0.3104 0.6404 -0.1071 0.1976  -0.0517 655 HOH A O     
1708 O O     . HOH D .   ? 0.2648 0.4281 0.4359 -0.0652 -0.0032 -0.0989 656 HOH A O     
1709 O O     . HOH D .   ? 0.3249 0.3542 0.4931 0.0102  -0.0813 0.0174  657 HOH A O     
1710 O O     . HOH D .   ? 0.2222 0.1992 0.4865 -0.0094 -0.1031 0.0430  658 HOH A O     
1711 O O     . HOH D .   ? 0.5262 0.2681 0.7071 -0.0737 -0.0073 0.0305  659 HOH A O     
1712 O O     . HOH D .   ? 0.3173 0.1909 0.4265 0.0534  -0.0732 -0.0491 660 HOH A O     
1713 O O     . HOH D .   ? 0.4462 0.3975 0.6010 0.1536  0.0250  0.0700  661 HOH A O     
1714 O O     . HOH D .   ? 0.6060 0.2318 0.6108 0.2165  -0.2017 -0.0852 662 HOH A O     
1715 O O     . HOH D .   ? 0.3074 0.3232 0.4267 0.1122  0.0042  -0.0660 663 HOH A O     
1716 O O     . HOH D .   ? 0.3423 0.1900 0.5284 0.0847  -0.0204 0.0595  664 HOH A O     
1717 O O     . HOH D .   ? 0.2132 0.4772 0.6148 0.0805  -0.0418 -0.1207 665 HOH A O     
1718 O O     . HOH D .   ? 0.1540 0.1514 0.3241 0.0296  -0.0024 0.0089  666 HOH A O     
1719 O O     . HOH D .   ? 0.3285 0.1521 0.5119 -0.0519 -0.0165 0.0373  667 HOH A O     
1720 O O     . HOH D .   ? 0.2908 0.5053 0.5994 0.0394  -0.0585 -0.0127 668 HOH A O     
1721 O O     . HOH D .   ? 0.3289 0.3459 0.4777 -0.0443 -0.0141 -0.0209 669 HOH A O     
1722 O O     . HOH D .   ? 0.4270 0.2825 0.4488 0.1273  0.1060  0.0088  670 HOH A O     
1723 O O     . HOH D .   ? 0.5819 0.3460 0.8229 0.0441  0.2824  -0.0052 671 HOH A O     
1724 O O     . HOH D .   ? 0.1525 0.1279 0.3365 0.0025  0.0043  -0.0120 672 HOH A O     
1725 O O     . HOH D .   ? 0.4037 0.2222 0.5371 -0.0108 0.0074  -0.0182 673 HOH A O     
1726 O O     . HOH D .   ? 0.6610 0.6960 0.4372 -0.1385 0.0466  -0.1800 674 HOH A O     
1727 O O     . HOH D .   ? 0.3581 0.2152 0.4675 0.0409  -0.1354 0.0189  675 HOH A O     
1728 O O     . HOH D .   ? 0.2460 0.4356 0.5346 -0.1573 -0.0345 0.0124  676 HOH A O     
1729 O O     . HOH D .   ? 0.1654 0.3448 0.5884 -0.1233 0.0707  -0.0393 677 HOH A O     
1730 O O     . HOH D .   ? 0.1594 0.2313 0.3359 0.0027  0.0104  -0.0374 678 HOH A O     
1731 O O     . HOH D .   ? 0.1957 0.1844 0.3400 0.0344  0.0303  0.0087  679 HOH A O     
1732 O O     . HOH D .   ? 0.4232 0.4202 0.4885 -0.2261 -0.0929 0.1372  680 HOH A O     
1733 O O     . HOH D .   ? 0.2798 0.5485 0.6772 -0.0605 -0.0793 -0.1181 681 HOH A O     
1734 O O     . HOH D .   ? 0.2994 0.4703 0.5180 0.1914  -0.0139 0.0818  682 HOH A O     
1735 O O     . HOH D .   ? 0.3915 0.2101 0.6335 0.0250  -0.0287 0.0059  683 HOH A O     
1736 O O     . HOH D .   ? 0.7035 0.2690 0.5974 0.1335  -0.0331 0.0196  684 HOH A O     
1737 O O     . HOH D .   ? 0.2438 0.5497 0.5499 0.0719  0.0679  0.2188  685 HOH A O     
1738 O O     . HOH D .   ? 0.2622 0.2116 0.5548 -0.0435 -0.1060 0.0115  686 HOH A O     
1739 O O     . HOH D .   ? 0.1084 0.1227 0.3424 -0.0288 -0.0047 0.0037  687 HOH A O     
1740 O O     . HOH D .   ? 0.6735 0.1588 0.4954 -0.0808 -0.1405 -0.0033 688 HOH A O     
1741 O O     . HOH D .   ? 0.4098 0.2723 0.4875 0.0198  -0.1173 0.0538  689 HOH A O     
1742 O O     . HOH D .   ? 0.4322 0.3164 0.4289 -0.0983 -0.0292 -0.0200 690 HOH A O     
1743 O O     . HOH D .   ? 0.2107 0.5597 0.5304 -0.0567 0.0878  0.0011  691 HOH A O     
1744 O O     . HOH D .   ? 0.4270 0.2154 0.6832 0.2808  -0.2022 -0.1185 692 HOH A O     
1745 O O     . HOH D .   ? 0.3306 0.2287 0.6390 0.0540  0.1057  0.0299  693 HOH A O     
1746 O O     . HOH D .   ? 0.1802 0.1474 0.3514 -0.0074 -0.0356 0.0164  694 HOH A O     
1747 O O     . HOH D .   ? 0.1849 0.4050 0.4975 -0.0495 0.0021  -0.0360 695 HOH A O     
1748 O O     . HOH D .   ? 0.3498 1.1702 0.5353 -0.0866 0.0343  0.1307  696 HOH A O     
1749 O O     . HOH D .   ? 0.3810 0.5193 0.7816 -0.1165 0.1860  -0.2096 697 HOH A O     
1750 O O     . HOH D .   ? 0.2310 0.2755 0.3869 -0.0484 0.0215  -0.0012 698 HOH A O     
1751 O O     . HOH D .   ? 0.2178 0.2491 0.4057 0.0068  -0.0126 0.0596  699 HOH A O     
1752 O O     . HOH D .   ? 0.2374 0.4214 0.4667 0.0923  -0.0105 -0.0348 700 HOH A O     
1753 O O     . HOH D .   ? 0.3624 0.4724 0.4168 -0.1012 -0.0781 0.1145  701 HOH A O     
1754 O O     . HOH D .   ? 0.2327 0.2343 0.3573 -0.0558 0.0118  -0.0137 702 HOH A O     
1755 O O     . HOH D .   ? 0.4025 0.3485 0.5402 -0.0444 0.0862  -0.1077 703 HOH A O     
1756 O O     . HOH D .   ? 0.1671 0.5977 0.4478 0.0525  0.0185  -0.0015 704 HOH A O     
1757 O O     . HOH D .   ? 0.2173 0.5520 0.5431 0.0087  0.0101  0.0047  705 HOH A O     
1758 O O     . HOH D .   ? 0.2192 0.1960 0.3303 0.0003  0.0427  0.0321  706 HOH A O     
1759 O O     . HOH D .   ? 0.1989 0.2248 0.4070 0.0270  0.0079  -0.0286 707 HOH A O     
1760 O O     . HOH D .   ? 0.2859 0.4728 0.4629 0.0566  0.0193  0.0427  708 HOH A O     
1761 O O     . HOH D .   ? 0.2902 0.2942 0.4986 0.0119  0.0519  0.0412  709 HOH A O     
1762 O O     . HOH D .   ? 0.1070 0.2541 0.3304 -0.0132 -0.0020 -0.0138 710 HOH A O     
1763 O O     . HOH D .   ? 0.3576 0.4009 0.3860 -0.0965 -0.0522 0.0141  711 HOH A O     
1764 O O     . HOH D .   ? 0.1885 0.4035 0.5459 0.1115  0.0082  -0.0290 712 HOH A O     
1765 O O     . HOH D .   ? 0.2961 0.2768 0.5161 0.0670  -0.0581 0.0380  713 HOH A O     
1766 O O     . HOH D .   ? 0.2189 0.3064 0.4623 0.0058  -0.0296 0.0098  714 HOH A O     
1767 O O     . HOH D .   ? 0.2667 0.2009 0.5150 -0.1096 -0.0614 0.0622  715 HOH A O     
1768 O O     . HOH D .   ? 0.1626 0.5250 0.5152 0.0338  -0.0090 -0.0479 716 HOH A O     
1769 O O     . HOH D .   ? 0.4101 0.2378 0.3703 -0.0358 -0.0157 -0.0263 717 HOH A O     
1770 O O     . HOH D .   ? 0.3617 0.1684 0.4816 0.0815  0.0161  0.0466  718 HOH A O     
1771 O O     . HOH D .   ? 0.3494 0.2152 0.3938 0.0058  -0.0161 -0.0415 719 HOH A O     
1772 O O     . HOH D .   ? 0.4649 0.5503 0.6088 -0.1285 -0.0691 0.0644  720 HOH A O     
1773 O O     . HOH D .   ? 0.3559 0.3473 0.3786 -0.0058 0.0468  -0.0027 721 HOH A O     
1774 O O     . HOH D .   ? 0.3931 0.2764 0.7376 -0.0731 0.1566  0.0020  722 HOH A O     
1775 O O     . HOH D .   ? 0.3166 0.4091 0.6917 0.0835  0.1391  0.2195  723 HOH A O     
1776 O O     . HOH D .   ? 0.1671 0.1732 0.5219 0.0246  0.0604  -0.0484 724 HOH A O     
1777 O O     . HOH D .   ? 0.3964 0.3748 0.4061 0.1254  -0.0630 -0.0500 725 HOH A O     
1778 O O     . HOH D .   ? 0.5547 0.2614 0.4165 -0.0222 -0.1611 -0.0125 726 HOH A O     
1779 O O     . HOH D .   ? 0.5323 0.1708 0.4229 0.0345  -0.0206 0.0647  727 HOH A O     
1780 O O     . HOH D .   ? 0.2798 0.2444 0.5558 0.0378  0.0045  0.0693  728 HOH A O     
1781 O O     . HOH D .   ? 0.6901 0.3343 0.7004 -0.0801 -0.0736 -0.0480 729 HOH A O     
1782 O O     . HOH D .   ? 0.7007 0.4992 0.7935 0.1298  0.2605  0.0899  730 HOH A O     
1783 O O     . HOH D .   ? 0.2371 0.4118 0.4753 0.1813  0.0646  -0.0961 731 HOH A O     
1784 O O     . HOH D .   ? 0.3132 0.4098 0.4773 -0.0750 0.0047  -0.1148 732 HOH A O     
1785 O O     . HOH D .   ? 0.0694 0.4035 0.9034 -0.0657 -0.0290 -0.0380 733 HOH A O     
1786 O O     . HOH D .   ? 0.3231 0.3742 0.4652 -0.0834 -0.0161 0.0189  734 HOH A O     
1787 O O     . HOH D .   ? 0.4032 0.2080 0.4179 0.0989  0.0023  0.0002  735 HOH A O     
1788 O O     . HOH D .   ? 0.2661 0.3021 0.8961 -0.0937 -0.0050 -0.0736 736 HOH A O     
1789 O O     . HOH D .   ? 0.4055 0.3569 0.9244 0.0813  -0.1019 -0.0846 737 HOH A O     
1790 O O     . HOH D .   ? 0.2641 0.1239 0.6098 -0.0197 0.0496  0.0196  738 HOH A O     
1791 O O     . HOH D .   ? 0.6427 0.3023 0.5673 -0.1795 -0.1207 0.0255  739 HOH A O     
1792 O O     . HOH D .   ? 0.3718 0.2726 0.5534 -0.1376 0.0488  -0.0443 740 HOH A O     
1793 O O     . HOH D .   ? 0.5475 0.2595 0.5252 -0.0268 -0.0465 0.0171  741 HOH A O     
1794 O O     . HOH D .   ? 0.3219 0.2734 0.7073 -0.1013 0.0717  -0.1520 742 HOH A O     
1795 O O     . HOH D .   ? 0.2509 0.3063 0.4949 0.0598  -0.0256 -0.0606 743 HOH A O     
1796 O O     . HOH D .   ? 0.5225 0.4076 0.9714 0.0898  0.0235  -0.0158 744 HOH A O     
1797 O O     . HOH D .   ? 0.4101 0.5450 0.9341 0.1073  -0.0662 0.0280  745 HOH A O     
1798 O O     . HOH D .   ? 0.4887 0.4321 0.4453 0.0694  0.0550  -0.0704 746 HOH A O     
1799 O O     . HOH D .   ? 0.7175 0.3683 0.6042 0.0700  0.0182  0.0748  747 HOH A O     
1800 O O     . HOH D .   ? 0.2764 0.6699 0.5862 0.0954  0.0633  0.0789  748 HOH A O     
1801 O O     . HOH D .   ? 0.3646 0.3974 0.5758 -0.0007 0.0700  -0.1023 749 HOH A O     
1802 O O     . HOH D .   ? 0.3697 0.3184 0.8231 -0.0804 0.0430  0.0620  750 HOH A O     
1803 O O     . HOH D .   ? 0.3220 0.3665 0.5850 0.0756  0.0090  0.0594  751 HOH A O     
1804 O O     . HOH D .   ? 0.2369 0.4076 0.6363 0.0292  -0.0185 0.1194  752 HOH A O     
1805 O O     . HOH D .   ? 0.3654 0.6845 0.4263 -0.2297 0.0365  0.0166  753 HOH A O     
1806 O O     . HOH D .   ? 0.6859 0.2986 1.1406 0.1514  0.0397  0.1051  754 HOH A O     
1807 O O     . HOH D .   ? 0.2893 0.4304 0.6442 0.1497  0.0284  0.0623  755 HOH A O     
1808 O O     . HOH D .   ? 0.5259 0.8112 0.5084 0.1007  0.0987  0.0986  756 HOH A O     
1809 O O     . HOH D .   ? 0.3582 0.3872 0.7174 0.0022  -0.2149 0.0054  757 HOH A O     
1810 O O     . HOH D .   ? 0.3226 0.3525 0.4856 -0.0327 0.0196  -0.0333 758 HOH A O     
1811 O O     . HOH D .   ? 0.3369 0.2181 0.5015 0.0530  0.0291  0.0817  759 HOH A O     
1812 O O     . HOH D .   ? 0.7218 1.0012 0.8368 0.4164  -0.0202 0.0995  760 HOH A O     
1813 O O     . HOH D .   ? 0.3037 0.2747 0.4345 0.0239  0.0042  0.0510  761 HOH A O     
1814 O O     . HOH D .   ? 0.7756 0.4216 0.4484 -0.2186 -0.1109 -0.0281 762 HOH A O     
1815 O O     . HOH D .   ? 0.4796 0.4067 0.5520 0.1318  0.0498  -0.0412 763 HOH A O     
1816 O O     . HOH D .   ? 0.4693 0.3763 0.5966 -0.1821 0.0147  0.0183  764 HOH A O     
1817 O O     . HOH D .   ? 0.3855 0.2526 0.8445 0.0181  0.0008  -0.1032 765 HOH A O     
1818 O O     . HOH D .   ? 0.4710 0.2505 0.6041 -0.0551 0.0758  -0.0302 766 HOH A O     
1819 O O     . HOH D .   ? 0.7072 0.3598 0.4357 -0.0509 0.0050  -0.0283 767 HOH A O     
1820 O O     . HOH D .   ? 0.8047 0.3378 1.0331 0.1127  0.1438  -0.0647 768 HOH A O     
1821 O O     . HOH D .   ? 0.8840 0.3284 0.4987 0.1680  0.1638  -0.0260 769 HOH A O     
1822 O O     . HOH D .   ? 0.2517 0.5078 0.7564 0.0756  0.0452  -0.1373 770 HOH A O     
1823 O O     . HOH D .   ? 0.2461 0.3696 0.4284 0.0025  0.0267  0.0416  771 HOH A O     
1824 O O     . HOH D .   ? 0.5326 0.2188 0.6496 -0.1418 -0.0549 0.0582  772 HOH A O     
1825 O O     . HOH D .   ? 0.1132 0.9113 0.7905 0.0674  0.0321  0.2013  773 HOH A O     
1826 O O     . HOH D .   ? 0.2083 0.2106 0.7848 0.0085  0.0589  -0.0484 774 HOH A O     
1827 O O     . HOH D .   ? 0.5267 0.2701 0.5625 0.0395  0.0288  0.1069  775 HOH A O     
1828 O O     . HOH D .   ? 0.4256 0.4068 0.6138 -0.0713 -0.0426 0.1384  776 HOH A O     
1829 O O     . HOH D .   ? 0.2192 0.2376 0.5427 -0.0163 -0.0110 -0.0651 777 HOH A O     
1830 O O     . HOH D .   ? 0.8401 0.4128 0.4597 -0.0692 -0.2390 0.0352  778 HOH A O     
1831 O O     . HOH D .   ? 0.2331 0.2934 0.5531 0.0185  0.0153  0.0594  779 HOH A O     
1832 O O     . HOH D .   ? 0.2555 0.4034 0.6136 0.1030  0.0933  0.0539  780 HOH A O     
1833 O O     . HOH D .   ? 0.3964 0.5658 0.6301 -0.0046 0.0395  -0.0409 781 HOH A O     
1834 O O     . HOH D .   ? 0.3274 0.5309 0.6436 -0.0287 -0.0171 -0.0086 782 HOH A O     
1835 O O     . HOH D .   ? 0.3736 0.4436 0.5153 -0.0541 0.0226  0.0495  783 HOH A O     
1836 O O     . HOH D .   ? 0.3949 0.3649 0.7379 -0.0753 -0.0760 0.0965  784 HOH A O     
1837 O O     . HOH D .   ? 0.5011 0.3972 0.8766 0.0248  -0.0680 0.0184  785 HOH A O     
1838 O O     . HOH D .   ? 0.7051 0.3062 0.5566 -0.1369 0.2784  -0.0849 786 HOH A O     
1839 O O     . HOH D .   ? 0.3680 0.3878 0.6301 -0.1410 -0.0952 0.1518  787 HOH A O     
1840 O O     . HOH D .   ? 0.7921 0.4554 0.5360 -0.1454 0.0231  -0.0772 788 HOH A O     
1841 O O     . HOH D .   ? 0.5185 0.5232 0.8423 0.0490  0.2688  0.1150  789 HOH A O     
1842 O O     . HOH D .   ? 0.2793 0.2607 0.4580 0.0421  0.0101  0.0504  790 HOH A O     
1843 O O     . HOH D .   ? 0.3669 0.3700 0.5912 -0.0266 -0.0915 0.0497  791 HOH A O     
1844 O O     . HOH D .   ? 0.3973 0.3182 0.5237 0.0344  0.0636  0.0017  792 HOH A O     
1845 O O     . HOH D .   ? 0.3745 0.4041 0.6864 0.0587  0.1028  0.1534  793 HOH A O     
1846 O O     . HOH D .   ? 0.3566 0.4039 0.5165 0.0331  0.0071  0.0511  794 HOH A O     
1847 O O     . HOH D .   ? 0.4489 0.3324 0.7152 0.1131  -0.0754 -0.0252 795 HOH A O     
1848 O O     . HOH D .   ? 0.3660 0.4004 0.5221 -0.0325 -0.0205 0.0432  796 HOH A O     
1849 O O     . HOH D .   ? 0.3443 0.3730 0.7438 0.0984  0.0438  -0.0698 797 HOH A O     
1850 O O     . HOH D .   ? 0.3432 0.4125 0.5443 -0.0565 0.0499  0.0415  798 HOH A O     
1851 O O     . HOH D .   ? 0.2191 0.2146 0.5199 -0.0753 -0.0241 -0.0231 799 HOH A O     
1852 O O     . HOH D .   ? 0.3946 0.1556 0.7152 0.0512  0.1126  0.0650  800 HOH A O     
1853 O O     . HOH D .   ? 0.3187 0.3241 0.6830 0.1080  -0.0483 0.0280  801 HOH A O     
1854 O O     . HOH D .   ? 0.3224 0.1883 0.7156 0.0204  -0.0150 -0.0857 802 HOH A O     
1855 O O     . HOH D .   ? 0.3858 0.3906 0.7221 0.1366  0.0873  -0.0556 803 HOH A O     
1856 O O     . HOH D .   ? 0.1218 0.1848 0.5330 0.0080  0.0078  -0.0283 804 HOH A O     
1857 O O     . HOH D .   ? 0.6358 0.3473 0.8996 0.0038  0.0630  0.1622  805 HOH A O     
1858 O O     . HOH D .   ? 0.3423 0.4408 0.6669 -0.1009 -0.0205 -0.0242 806 HOH A O     
1859 O O     . HOH D .   ? 0.5613 0.3567 0.5141 0.0916  -0.1031 -0.0505 807 HOH A O     
1860 O O     . HOH D .   ? 0.5818 0.3504 0.5473 -0.0171 -0.0186 0.1375  808 HOH A O     
1861 O O     . HOH D .   ? 0.4116 0.3133 0.6756 -0.0080 -0.0817 0.0262  809 HOH A O     
1862 O O     . HOH D .   ? 0.5522 0.4447 0.6118 0.0183  -0.0121 0.0143  810 HOH A O     
1863 O O     . HOH D .   ? 0.4240 0.5041 0.6136 0.2125  0.0754  -0.0436 811 HOH A O     
# 
