data_9QY1
# 
_entry.id   9QY1 
# 
_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   9QY1         pdb_00009qy1 10.2210/pdb9qy1/pdb 
WWPDB D_1292147205 ?            ?                   
# 
_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                        9QY1 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-16 
_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                 2 
_pdbx_contact_author.email              k.drickamer@imperial.ac.uk 
_pdbx_contact_author.name_first         Kurt 
_pdbx_contact_author.name_last          Drickamer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5026-5996 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Drickamer, K.'   1 0000-0001-5026-5996 
'Feinberg, H.'    2 0000-0002-9937-4699 
'Weis, W.I.'      3 0000-0002-5583-6150 
'Taylor, M.E.'    4 0000-0001-8300-4987 
'Jegouzo, S.A.F.' 5 0000-0001-7768-0102 
# 
_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                     'Sugar binding activity of the endothelial receptor Endo180' 
_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 'Jegouzo, S.A.F.' 1 0000-0001-7768-0102 
primary 'Feinberg, H.'    2 0000-0002-9937-4699 
primary 'Lasanajak, Y.'   3 0000-0003-1450-8107 
primary 'Smith, D.H.'     4 ?                   
primary 'Weis, W.I.'      5 0000-0002-5583-6150 
primary 'Drickamer, K.'   6 0000-0001-5026-5996 
primary 'Taylor, M.E.'    7 0000-0001-8300-4987 
# 
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 'Mannose receptor C type 2'     14961.853 1  ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'                   40.078    2  ? ? ? ? 
3 non-polymer syn 'methyl alpha-L-fucopyranoside' 178.183   1  ? ? ? ? 
4 water       nat water                           18.015    67 ? ? ? ? 
# 
_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       
;AVECEPSWQPFQGHCYRLQAEKRSWQESKKMCLRGGGDLLSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDG
SLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AVECEPSWQPFQGHCYRLQAEKRSWQESKKMCLRGGGDLLSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDG
SLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKK
;
_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 'CALCIUM ION'                   CA  
3 'methyl alpha-L-fucopyranoside' MFU 
4 water                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   VAL n 
1 3   GLU n 
1 4   CYS n 
1 5   GLU n 
1 6   PRO n 
1 7   SER n 
1 8   TRP n 
1 9   GLN n 
1 10  PRO n 
1 11  PHE n 
1 12  GLN n 
1 13  GLY n 
1 14  HIS n 
1 15  CYS n 
1 16  TYR n 
1 17  ARG n 
1 18  LEU n 
1 19  GLN n 
1 20  ALA n 
1 21  GLU n 
1 22  LYS n 
1 23  ARG n 
1 24  SER n 
1 25  TRP n 
1 26  GLN n 
1 27  GLU n 
1 28  SER n 
1 29  LYS n 
1 30  LYS n 
1 31  MET n 
1 32  CYS n 
1 33  LEU n 
1 34  ARG n 
1 35  GLY n 
1 36  GLY n 
1 37  GLY n 
1 38  ASP n 
1 39  LEU n 
1 40  LEU n 
1 41  SER n 
1 42  ILE n 
1 43  HIS n 
1 44  SER n 
1 45  MET n 
1 46  ALA n 
1 47  GLU n 
1 48  LEU n 
1 49  GLU n 
1 50  PHE n 
1 51  ILE n 
1 52  THR n 
1 53  LYS n 
1 54  GLN n 
1 55  ILE n 
1 56  LYS n 
1 57  GLN n 
1 58  GLU n 
1 59  VAL n 
1 60  GLU n 
1 61  GLU n 
1 62  LEU n 
1 63  TRP n 
1 64  ILE n 
1 65  GLY n 
1 66  LEU n 
1 67  ASN n 
1 68  ASP n 
1 69  LEU n 
1 70  LYS n 
1 71  LEU n 
1 72  GLN n 
1 73  MET n 
1 74  ASN n 
1 75  PHE n 
1 76  GLU n 
1 77  TRP n 
1 78  SER n 
1 79  ASP n 
1 80  GLY n 
1 81  SER n 
1 82  LEU n 
1 83  VAL n 
1 84  SER n 
1 85  PHE n 
1 86  THR n 
1 87  HIS n 
1 88  TRP n 
1 89  HIS n 
1 90  PRO n 
1 91  PHE n 
1 92  GLU n 
1 93  PRO n 
1 94  ASN n 
1 95  ASN n 
1 96  PHE n 
1 97  ARG n 
1 98  ASP n 
1 99  SER n 
1 100 LEU n 
1 101 GLU n 
1 102 ASP n 
1 103 CYS n 
1 104 VAL n 
1 105 THR n 
1 106 ILE n 
1 107 TRP n 
1 108 GLY n 
1 109 PRO n 
1 110 GLU n 
1 111 GLY n 
1 112 ARG n 
1 113 TRP n 
1 114 ASN n 
1 115 ASP n 
1 116 SER n 
1 117 PRO n 
1 118 CYS n 
1 119 ASN n 
1 120 GLN n 
1 121 SER n 
1 122 LEU n 
1 123 PRO n 
1 124 SER n 
1 125 ILE n 
1 126 CYS n 
1 127 LYS n 
1 128 LYS 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                   128 
_entity_src_gen.gene_src_common_name               'domestic cattle' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MRC2 
_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      'Bos taurus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9913 
_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  
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 
CA  non-polymer         . 'CALCIUM ION'                   ? 'Ca 2'           40.078  
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 
MFU L-saccharide        n 'methyl alpha-L-fucopyranoside' 
'ALPHA-L-METHYL-FUCOSE; methyl 6-deoxy-alpha-L-galactopyranoside; methyl alpha-L-fucoside; methyl L-fucoside; methyl fucoside' 
'C7 H14 O5'      178.183 
PHE 'L-peptide linking' y PHENYLALANINE                   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
MFU 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 'LFucp[1Me]a'             
MFU 'COMMON NAME'                         GMML     1.0 1-methyl-a-L-fucopyranose 
MFU 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 o1-methyl-a-L-fucose      
# 
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   ALA 1   380 380 ALA ALA A . n 
A 1 2   VAL 2   381 381 VAL VAL A . n 
A 1 3   GLU 3   382 382 GLU GLU A . n 
A 1 4   CYS 4   383 383 CYS CYS A . n 
A 1 5   GLU 5   384 384 GLU GLU A . n 
A 1 6   PRO 6   385 385 PRO PRO A . n 
A 1 7   SER 7   386 386 SER SER A . n 
A 1 8   TRP 8   387 387 TRP TRP A . n 
A 1 9   GLN 9   388 388 GLN GLN A . n 
A 1 10  PRO 10  389 389 PRO PRO A . n 
A 1 11  PHE 11  390 390 PHE PHE A . n 
A 1 12  GLN 12  391 391 GLN GLN A . n 
A 1 13  GLY 13  392 392 GLY GLY A . n 
A 1 14  HIS 14  393 393 HIS HIS A . n 
A 1 15  CYS 15  394 394 CYS CYS A . n 
A 1 16  TYR 16  395 395 TYR TYR A . n 
A 1 17  ARG 17  396 396 ARG ARG A . n 
A 1 18  LEU 18  397 397 LEU LEU A . n 
A 1 19  GLN 19  398 398 GLN GLN A . n 
A 1 20  ALA 20  399 399 ALA ALA A . n 
A 1 21  GLU 21  400 400 GLU GLU A . n 
A 1 22  LYS 22  401 401 LYS LYS A . n 
A 1 23  ARG 23  402 402 ARG ARG A . n 
A 1 24  SER 24  403 403 SER SER A . n 
A 1 25  TRP 25  404 404 TRP TRP A . n 
A 1 26  GLN 26  405 405 GLN GLN A . n 
A 1 27  GLU 27  406 406 GLU GLU A . n 
A 1 28  SER 28  407 407 SER SER A . n 
A 1 29  LYS 29  408 408 LYS LYS A . n 
A 1 30  LYS 30  409 409 LYS LYS A . n 
A 1 31  MET 31  410 410 MET MET A . n 
A 1 32  CYS 32  411 411 CYS CYS A . n 
A 1 33  LEU 33  412 412 LEU LEU A . n 
A 1 34  ARG 34  413 413 ARG ARG A . n 
A 1 35  GLY 35  414 414 GLY GLY A . n 
A 1 36  GLY 36  415 415 GLY GLY A . n 
A 1 37  GLY 37  416 416 GLY GLY A . n 
A 1 38  ASP 38  417 417 ASP ASP A . n 
A 1 39  LEU 39  418 418 LEU LEU A . n 
A 1 40  LEU 40  419 419 LEU LEU A . n 
A 1 41  SER 41  420 420 SER SER A . n 
A 1 42  ILE 42  421 421 ILE ILE A . n 
A 1 43  HIS 43  422 422 HIS HIS A . n 
A 1 44  SER 44  423 423 SER SER A . n 
A 1 45  MET 45  424 424 MET MET A . n 
A 1 46  ALA 46  425 425 ALA ALA A . n 
A 1 47  GLU 47  426 426 GLU GLU A . n 
A 1 48  LEU 48  427 427 LEU LEU A . n 
A 1 49  GLU 49  428 428 GLU GLU A . n 
A 1 50  PHE 50  429 429 PHE PHE A . n 
A 1 51  ILE 51  430 430 ILE ILE A . n 
A 1 52  THR 52  431 431 THR THR A . n 
A 1 53  LYS 53  432 432 LYS LYS A . n 
A 1 54  GLN 54  433 433 GLN GLN A . n 
A 1 55  ILE 55  434 434 ILE ILE A . n 
A 1 56  LYS 56  435 435 LYS LYS A . n 
A 1 57  GLN 57  436 436 GLN GLN A . n 
A 1 58  GLU 58  437 437 GLU GLU A . n 
A 1 59  VAL 59  438 438 VAL VAL A . n 
A 1 60  GLU 60  439 439 GLU GLU A . n 
A 1 61  GLU 61  440 440 GLU GLU A . n 
A 1 62  LEU 62  441 441 LEU LEU A . n 
A 1 63  TRP 63  442 442 TRP TRP A . n 
A 1 64  ILE 64  443 443 ILE ILE A . n 
A 1 65  GLY 65  444 444 GLY GLY A . n 
A 1 66  LEU 66  445 445 LEU LEU A . n 
A 1 67  ASN 67  446 446 ASN ASN A . n 
A 1 68  ASP 68  447 447 ASP ASP A . n 
A 1 69  LEU 69  448 448 LEU LEU A . n 
A 1 70  LYS 70  449 449 LYS LYS A . n 
A 1 71  LEU 71  450 450 LEU LEU A . n 
A 1 72  GLN 72  451 451 GLN GLN A . n 
A 1 73  MET 73  452 452 MET MET A . n 
A 1 74  ASN 74  453 453 ASN ASN A . n 
A 1 75  PHE 75  454 454 PHE PHE A . n 
A 1 76  GLU 76  455 455 GLU GLU A . n 
A 1 77  TRP 77  456 456 TRP TRP A . n 
A 1 78  SER 78  457 457 SER SER A . n 
A 1 79  ASP 79  458 458 ASP ASP A . n 
A 1 80  GLY 80  459 459 GLY GLY A . n 
A 1 81  SER 81  460 460 SER SER A . n 
A 1 82  LEU 82  461 461 LEU LEU A . n 
A 1 83  VAL 83  462 462 VAL VAL A . n 
A 1 84  SER 84  463 463 SER SER A . n 
A 1 85  PHE 85  464 464 PHE PHE A . n 
A 1 86  THR 86  465 465 THR THR A . n 
A 1 87  HIS 87  466 466 HIS HIS A . n 
A 1 88  TRP 88  467 467 TRP TRP A . n 
A 1 89  HIS 89  468 468 HIS HIS A . n 
A 1 90  PRO 90  469 469 PRO PRO A . n 
A 1 91  PHE 91  470 470 PHE PHE A . n 
A 1 92  GLU 92  471 471 GLU GLU A . n 
A 1 93  PRO 93  472 472 PRO PRO A . n 
A 1 94  ASN 94  473 473 ASN ASN A . n 
A 1 95  ASN 95  474 474 ASN ASN A . n 
A 1 96  PHE 96  475 475 PHE PHE A . n 
A 1 97  ARG 97  476 476 ARG ARG A . n 
A 1 98  ASP 98  477 477 ASP ASP A . n 
A 1 99  SER 99  478 ?   ?   ?   A . n 
A 1 100 LEU 100 479 ?   ?   ?   A . n 
A 1 101 GLU 101 480 480 GLU GLU A . n 
A 1 102 ASP 102 481 481 ASP ASP A . n 
A 1 103 CYS 103 482 482 CYS CYS A . n 
A 1 104 VAL 104 483 483 VAL VAL A . n 
A 1 105 THR 105 484 484 THR THR A . n 
A 1 106 ILE 106 485 485 ILE ILE A . n 
A 1 107 TRP 107 486 486 TRP TRP A . n 
A 1 108 GLY 108 487 487 GLY GLY A . n 
A 1 109 PRO 109 488 488 PRO PRO A . n 
A 1 110 GLU 110 489 489 GLU GLU A . n 
A 1 111 GLY 111 490 490 GLY GLY A . n 
A 1 112 ARG 112 491 491 ARG ARG A . n 
A 1 113 TRP 113 492 492 TRP TRP A . n 
A 1 114 ASN 114 493 493 ASN ASN A . n 
A 1 115 ASP 115 494 494 ASP ASP A . n 
A 1 116 SER 116 495 495 SER SER A . n 
A 1 117 PRO 117 496 496 PRO PRO A . n 
A 1 118 CYS 118 497 497 CYS CYS A . n 
A 1 119 ASN 119 498 498 ASN ASN A . n 
A 1 120 GLN 120 499 499 GLN GLN A . n 
A 1 121 SER 121 500 500 SER SER A . n 
A 1 122 LEU 122 501 501 LEU LEU A . n 
A 1 123 PRO 123 502 502 PRO PRO A . n 
A 1 124 SER 124 503 503 SER SER A . n 
A 1 125 ILE 125 504 504 ILE ILE A . n 
A 1 126 CYS 126 505 505 CYS CYS A . n 
A 1 127 LYS 127 506 506 LYS LYS A . n 
A 1 128 LYS 128 507 507 LYS LYS 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 CA  ? ? CA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MFU ? ? MFU ? ? '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 CA  1  601 601 CA  CA  A . 
C 2 CA  1  602 602 CA  CA  A . 
D 3 MFU 1  603 603 MFU MFU A . 
E 4 HOH 1  701 32  HOH HOH A . 
E 4 HOH 2  702 60  HOH HOH A . 
E 4 HOH 3  703 31  HOH HOH A . 
E 4 HOH 4  704 27  HOH HOH A . 
E 4 HOH 5  705 10  HOH HOH A . 
E 4 HOH 6  706 19  HOH HOH A . 
E 4 HOH 7  707 3   HOH HOH A . 
E 4 HOH 8  708 22  HOH HOH A . 
E 4 HOH 9  709 7   HOH HOH A . 
E 4 HOH 10 710 29  HOH HOH A . 
E 4 HOH 11 711 54  HOH HOH A . 
E 4 HOH 12 712 21  HOH HOH A . 
E 4 HOH 13 713 2   HOH HOH A . 
E 4 HOH 14 714 38  HOH HOH A . 
E 4 HOH 15 715 52  HOH HOH A . 
E 4 HOH 16 716 28  HOH HOH A . 
E 4 HOH 17 717 44  HOH HOH A . 
E 4 HOH 18 718 49  HOH HOH A . 
E 4 HOH 19 719 62  HOH HOH A . 
E 4 HOH 20 720 43  HOH HOH A . 
E 4 HOH 21 721 57  HOH HOH A . 
E 4 HOH 22 722 11  HOH HOH A . 
E 4 HOH 23 723 63  HOH HOH A . 
E 4 HOH 24 724 66  HOH HOH A . 
E 4 HOH 25 725 8   HOH HOH A . 
E 4 HOH 26 726 55  HOH HOH A . 
E 4 HOH 27 727 14  HOH HOH A . 
E 4 HOH 28 728 18  HOH HOH A . 
E 4 HOH 29 729 12  HOH HOH A . 
E 4 HOH 30 730 24  HOH HOH A . 
E 4 HOH 31 731 9   HOH HOH A . 
E 4 HOH 32 732 56  HOH HOH A . 
E 4 HOH 33 733 4   HOH HOH A . 
E 4 HOH 34 734 59  HOH HOH A . 
E 4 HOH 35 735 6   HOH HOH A . 
E 4 HOH 36 736 20  HOH HOH A . 
E 4 HOH 37 737 35  HOH HOH A . 
E 4 HOH 38 738 41  HOH HOH A . 
E 4 HOH 39 739 46  HOH HOH A . 
E 4 HOH 40 740 1   HOH HOH A . 
E 4 HOH 41 741 25  HOH HOH A . 
E 4 HOH 42 742 16  HOH HOH A . 
E 4 HOH 43 743 5   HOH HOH A . 
E 4 HOH 44 744 23  HOH HOH A . 
E 4 HOH 45 745 64  HOH HOH A . 
E 4 HOH 46 746 58  HOH HOH A . 
E 4 HOH 47 747 30  HOH HOH A . 
E 4 HOH 48 748 51  HOH HOH A . 
E 4 HOH 49 749 61  HOH HOH A . 
E 4 HOH 50 750 15  HOH HOH A . 
E 4 HOH 51 751 40  HOH HOH A . 
E 4 HOH 52 752 26  HOH HOH A . 
E 4 HOH 53 753 17  HOH HOH A . 
E 4 HOH 54 754 39  HOH HOH A . 
E 4 HOH 55 755 34  HOH HOH A . 
E 4 HOH 56 756 53  HOH HOH A . 
E 4 HOH 57 757 13  HOH HOH A . 
E 4 HOH 58 758 37  HOH HOH A . 
E 4 HOH 59 759 67  HOH HOH A . 
E 4 HOH 60 760 33  HOH HOH A . 
E 4 HOH 61 761 65  HOH HOH A . 
E 4 HOH 62 762 42  HOH HOH A . 
E 4 HOH 63 763 50  HOH HOH A . 
E 4 HOH 64 764 36  HOH HOH A . 
E 4 HOH 65 765 48  HOH HOH A . 
E 4 HOH 66 766 47  HOH HOH A . 
E 4 HOH 67 767 45  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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 ? 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           ? 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           ? 4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           ? 5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9QY1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.650 
_cell.length_a_esd                 ? 
_cell.length_b                     66.560 
_cell.length_b_esd                 ? 
_cell.length_c                     37.230 
_cell.length_c_esd                 ? 
_cell.volume                       113122.015 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9QY1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab' 
_symmetry.space_group_name_H-M             'P 21 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                   9QY1 
_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             1.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          34.93 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_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    
;Drop:
5.2 mg/ml protein
5 mM CaCl2
10 mM Tris-Cl, pH 8.0
25mM NaCl
50mM alpha-Methyl-Fucoside

Reservoir
26% polyethylene glycol 8K
0.1 M Tris-Cl, pH 8.0.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.5 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-23 
_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   0.97946 
_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                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          24.00 
_reflns.entry_id                                       9QY1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.9 
_reflns.d_resolution_low                               40 
_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                                     9435 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                24.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.08 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.125 
_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                                    1.90 
_reflns_shell.d_res_low                                     1.97 
_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                             922 
_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                               22.4 
_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                                  0.992 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.92 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9QY1 
_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                            1.90 
_refine.ls_d_res_low                             37.65 
_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                     9385 
_refine.ls_number_reflns_R_free                  472 
_refine.ls_number_reflns_R_work                  8913 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1865 
_refine.ls_R_factor_R_free                       0.2386 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1837 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.2236 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1898 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        37.65 
_refine_hist.number_atoms_solvent             67 
_refine_hist.number_atoms_total               1117 
_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        1036 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_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' ? 0.0058  ? 1096 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.8054  ? 1485 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0564  ? 154  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0062  ? 189  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 13.4640 ? 398  ? f_dihedral_angle_d ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.90 2.17  . . 154 2907 99.71 . . . . 0.1839 . . . . . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 2.18 2.74  . . 155 2917 99.64 . . . . 0.2120 . . . . . . . . . . . . . . . 0.2722 
'X-RAY DIFFRACTION' 2.74 37.65 . . 163 3089 99.97 . . . . 0.1736 . . . . . . . . . . . . . . . 0.2248 
# 
_struct.entry_id                     9QY1 
_struct.title                        'Endo180 (uPARAP) carbohydrate-recognition domain 2 with bound methyl fucoside' 
_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        9QY1 
_struct_keywords.text            'Lectin Endocytosis Endothelial cells, SUGAR BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'SUGAR BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3Q1M5H7_BOVIN 
_struct_ref.pdbx_db_accession          A0A3Q1M5H7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VECEPSWQPFQGHCYRLQAEKRSWQESKKMCLRGGGDLLSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGS
LVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKK
;
_struct_ref.pdbx_align_begin           381 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9QY1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 128 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A3Q1M5H7 
_struct_ref_seq.db_align_beg                  381 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  507 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       381 
_struct_ref_seq.pdbx_auth_seq_align_end       507 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9QY1 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   A0A3Q1M5H7 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            380 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_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)' 450  ? 
1 MORE         -23  ? 
1 'SSA (A^2)'  7210 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                
'This is a fragment constituting one folded domain from a larger polypeptide' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 24 ? GLY A 35 ? SER A 403 GLY A 414 1 ? 12 
HELX_P HELX_P2 AA2 SER A 44 ? ILE A 55 ? SER A 423 ILE A 434 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 4   SG  ? ? ? 1_555 A CYS 15  SG ? ? A CYS 383 A CYS 394 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf2  disulf ? ? A CYS 32  SG  ? ? ? 1_555 A CYS 126 SG ? ? A CYS 411 A CYS 505 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf3  disulf ? ? A CYS 103 SG  ? ? ? 1_555 A CYS 118 SG ? ? A CYS 482 A CYS 497 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc1  metalc ? ? A ASP 68  OD1 ? ? ? 1_555 B CA  .   CA ? ? A ASP 447 A CA  601 1_555 ? ? ? ? ? ? ? 2.529 ? ? 
metalc2  metalc ? ? A ASP 68  OD2 ? ? ? 1_555 B CA  .   CA ? ? A ASP 447 A CA  601 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc3  metalc ? ? A GLN 72  OE1 ? ? ? 1_555 B CA  .   CA ? ? A GLN 451 A CA  601 1_555 ? ? ? ? ? ? ? 2.385 ? ? 
metalc4  metalc ? ? A GLU 92  OE1 ? ? ? 1_555 C CA  .   CA ? ? A GLU 471 A CA  602 1_555 ? ? ? ? ? ? ? 2.603 ? ? 
metalc5  metalc ? ? A ASN 94  OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASN 473 A CA  602 1_555 ? ? ? ? ? ? ? 2.440 ? ? 
metalc6  metalc ? ? A ASN 95  OD1 ? ? ? 1_555 B CA  .   CA ? ? A ASN 474 A CA  601 1_555 ? ? ? ? ? ? ? 2.426 ? ? 
metalc7  metalc ? ? A GLU 101 O   ? ? ? 1_555 B CA  .   CA ? ? A GLU 480 A CA  601 1_555 ? ? ? ? ? ? ? 2.449 ? ? 
metalc8  metalc ? ? A GLU 101 OE1 ? ? ? 1_555 C CA  .   CA ? ? A GLU 480 A CA  602 1_555 ? ? ? ? ? ? ? 2.516 ? ? 
metalc9  metalc ? ? A ASP 102 OD1 ? ? ? 1_555 B CA  .   CA ? ? A ASP 481 A CA  601 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc10 metalc ? ? A ASN 114 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASN 493 A CA  602 1_555 ? ? ? ? ? ? ? 2.351 ? ? 
metalc11 metalc ? ? A ASP 115 O   ? ? ? 1_555 C CA  .   CA ? ? A ASP 494 A CA  602 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc12 metalc ? ? A ASP 115 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASP 494 A CA  602 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc13 metalc ? ? B CA  .   CA  ? ? ? 1_555 E HOH .   O  ? ? A CA  601 A HOH 740 1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc14 metalc ? ? C CA  .   CA  ? ? ? 1_555 D MFU .   O3 A ? A CA  602 A MFU 603 1_555 ? ? ? ? ? ? ? 2.585 ? ? 
metalc15 metalc ? ? C CA  .   CA  ? ? ? 1_555 D MFU .   O3 B ? A CA  602 A MFU 603 1_555 ? ? ? ? ? ? ? 2.472 ? ? 
metalc16 metalc ? ? C CA  .   CA  ? ? ? 1_555 D MFU .   O2 A ? A CA  602 A MFU 603 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc17 metalc ? ? C CA  .   CA  ? ? ? 1_555 D MFU .   O4 B ? A CA  602 A MFU 603 1_555 ? ? ? ? ? ? ? 2.603 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD2 ? A ASP 68  ? A ASP 447 ? 1_555 52.5  ? 
2  OD1 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OE1 ? A GLN 72  ? A GLN 451 ? 1_555 109.4 ? 
3  OD2 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OE1 ? A GLN 72  ? A GLN 451 ? 1_555 73.7  ? 
4  OD1 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASN 95  ? A ASN 474 ? 1_555 171.1 ? 
5  OD2 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASN 95  ? A ASN 474 ? 1_555 136.3 ? 
6  OE1 ? A GLN 72  ? A GLN 451 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASN 95  ? A ASN 474 ? 1_555 75.8  ? 
7  OD1 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? A GLU 101 ? A GLU 480 ? 1_555 95.8  ? 
8  OD2 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? A GLU 101 ? A GLU 480 ? 1_555 138.4 ? 
9  OE1 ? A GLN 72  ? A GLN 451 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? A GLU 101 ? A GLU 480 ? 1_555 147.9 ? 
10 OD1 ? A ASN 95  ? A ASN 474 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? A GLU 101 ? A GLU 480 ? 1_555 76.9  ? 
11 OD1 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASP 102 ? A ASP 481 ? 1_555 75.9  ? 
12 OD2 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASP 102 ? A ASP 481 ? 1_555 113.3 ? 
13 OE1 ? A GLN 72  ? A GLN 451 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASP 102 ? A ASP 481 ? 1_555 90.2  ? 
14 OD1 ? A ASN 95  ? A ASN 474 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASP 102 ? A ASP 481 ? 1_555 97.2  ? 
15 O   ? A GLU 101 ? A GLU 480 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 OD1 ? A ASP 102 ? A ASP 481 ? 1_555 76.8  ? 
16 OD1 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? E HOH .   ? A HOH 740 ? 1_555 95.9  ? 
17 OD2 ? A ASP 68  ? A ASP 447 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? E HOH .   ? A HOH 740 ? 1_555 76.5  ? 
18 OE1 ? A GLN 72  ? A GLN 451 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? E HOH .   ? A HOH 740 ? 1_555 113.8 ? 
19 OD1 ? A ASN 95  ? A ASN 474 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? E HOH .   ? A HOH 740 ? 1_555 88.2  ? 
20 O   ? A GLU 101 ? A GLU 480 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? E HOH .   ? A HOH 740 ? 1_555 81.8  ? 
21 OD1 ? A ASP 102 ? A ASP 481 ? 1_555 CA ? B CA . ? A CA 601 ? 1_555 O   ? E HOH .   ? A HOH 740 ? 1_555 156.0 ? 
22 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 72.3  ? 
23 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 142.5 ? 
24 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 75.4  ? 
25 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 68.3  ? 
26 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 140.1 ? 
27 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 143.8 ? 
28 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O   ? A ASP 115 ? A ASP 494 ? 1_555 126.8 ? 
29 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O   ? A ASP 115 ? A ASP 494 ? 1_555 141.4 ? 
30 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O   ? A ASP 115 ? A ASP 494 ? 1_555 72.1  ? 
31 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O   ? A ASP 115 ? A ASP 494 ? 1_555 72.2  ? 
32 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 70.1  ? 
33 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 82.1  ? 
34 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 87.3  ? 
35 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 90.6  ? 
36 O   ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 76.1  ? 
37 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  A D MFU .   ? A MFU 603 ? 1_555 135.7 ? 
38 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  A D MFU .   ? A MFU 603 ? 1_555 120.9 ? 
39 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  A D MFU .   ? A MFU 603 ? 1_555 77.9  ? 
40 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  A D MFU .   ? A MFU 603 ? 1_555 84.8  ? 
41 O   ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  A D MFU .   ? A MFU 603 ? 1_555 71.7  ? 
42 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  A D MFU .   ? A MFU 603 ? 1_555 147.3 ? 
43 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 130.2 ? 
44 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 120.5 ? 
45 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 82.9  ? 
46 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 82.0  ? 
47 O   ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 75.6  ? 
48 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 151.6 ? 
49 O3  A D MFU .   ? A MFU 603 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O3  B D MFU .   ? A MFU 603 ? 1_555 5.6   ? 
50 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 72.2  ? 
51 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 77.5  ? 
52 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 118.4 ? 
53 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 84.4  ? 
54 O   ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 137.1 ? 
55 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 141.1 ? 
56 O3  A D MFU .   ? A MFU 603 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 70.7  ? 
57 O3  B D MFU .   ? A MFU 603 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O2  A D MFU .   ? A MFU 603 ? 1_555 65.7  ? 
58 OE1 ? A GLU 92  ? A GLU 471 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 74.6  ? 
59 OD1 ? A ASN 94  ? A ASN 473 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 74.2  ? 
60 OE1 ? A GLU 101 ? A GLU 480 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 113.9 ? 
61 OD1 ? A ASN 114 ? A ASN 493 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 89.1  ? 
62 O   ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 138.9 ? 
63 OD1 ? A ASP 115 ? A ASP 494 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 142.1 ? 
64 O3  A D MFU .   ? A MFU 603 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 70.3  ? 
65 O3  B D MFU .   ? A MFU 603 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 65.5  ? 
66 O2  A D MFU .   ? A MFU 603 ? 1_555 CA ? C CA . ? A CA 602 ? 1_555 O4  B D MFU .   ? A MFU 603 ? 1_555 4.7   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 4   ? CYS A 15  ? CYS A 383 ? 1_555 CYS A 394 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 32  ? CYS A 126 ? CYS A 411 ? 1_555 CYS A 505 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 103 ? CYS A 118 ? CYS A 482 ? 1_555 CYS A 497 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           92 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            471 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    93 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     472 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.50 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 9   ? PHE A 11  ? GLN A 388 PHE A 390 
AA1 2 HIS A 14  ? ARG A 23  ? HIS A 393 ARG A 402 
AA1 3 LEU A 122 ? LYS A 128 ? LEU A 501 LYS A 507 
AA1 4 ASP A 38  ? LEU A 39  ? ASP A 417 LEU A 418 
AA2 1 GLU A 76  ? TRP A 77  ? GLU A 455 TRP A 456 
AA2 2 GLU A 61  ? ASN A 67  ? GLU A 440 ASN A 446 
AA2 3 CYS A 103 ? TRP A 107 ? CYS A 482 TRP A 486 
AA2 4 ARG A 112 ? SER A 116 ? ARG A 491 SER 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 GLN A 9   ? N GLN A 388 O TYR A 16  ? O TYR A 395 
AA1 2 3 N CYS A 15  ? N CYS A 394 O LYS A 128 ? O LYS A 507 
AA1 3 4 O LYS A 127 ? O LYS A 506 N ASP A 38  ? N ASP A 417 
AA2 1 2 O GLU A 76  ? O GLU A 455 N ASN A 67  ? N ASN A 446 
AA2 2 3 N ILE A 64  ? N ILE A 443 O VAL A 104 ? O VAL A 483 
AA2 3 4 N CYS A 103 ? N CYS A 482 O SER A 116 ? O SER A 495 
# 
_pdbx_entry_details.entry_id                   9QY1 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 GLN A 391 ? ? 38.69   56.88   
2 1 GLN A 436 ? ? 53.96   -126.94 
3 1 MET A 452 ? ? 75.48   -4.11   
4 1 HIS A 466 ? ? -149.24 59.80   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         9.77750118094 
_pdbx_refine_tls.origin_y         11.4569054019 
_pdbx_refine_tls.origin_z         11.1400383382 
_pdbx_refine_tls.T[1][1]          0.153199167465 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0214478960848 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.000212805574231 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.181901508825 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.00824081621446 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.223642881584 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.2569426406 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.713088153415 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.234645138704 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          4.1269059069 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.19061457131 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.10513826244 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0411010200323 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.18351715735 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0189591627724 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0467080784318 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.031689806186 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.269511239709 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0775211944767 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0259281201237 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0260886120554 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     380 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   E 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     67 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       767 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.39 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 478 ? A SER 99  
2 1 Y 1 A LEU 479 ? A LEU 100 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MFU C1   C  N R 251 
MFU C2   C  N S 252 
MFU C3   C  N R 253 
MFU C4   C  N S 254 
MFU C5   C  N S 255 
MFU C6   C  N N 256 
MFU O1   O  N N 257 
MFU O2   O  N N 258 
MFU O3   O  N N 259 
MFU O4   O  N N 260 
MFU O5   O  N N 261 
MFU CM   C  N N 262 
MFU H1   H  N N 263 
MFU H2   H  N N 264 
MFU H3   H  N N 265 
MFU H4   H  N N 266 
MFU H5   H  N N 267 
MFU H61  H  N N 268 
MFU H62  H  N N 269 
MFU H63  H  N N 270 
MFU HO2  H  N N 271 
MFU HO3  H  N N 272 
MFU HO4  H  N N 273 
MFU HM1  H  N N 274 
MFU HM2  H  N N 275 
MFU HM3  H  N N 276 
PHE N    N  N N 277 
PHE CA   C  N S 278 
PHE C    C  N N 279 
PHE O    O  N N 280 
PHE CB   C  N N 281 
PHE CG   C  Y N 282 
PHE CD1  C  Y N 283 
PHE CD2  C  Y N 284 
PHE CE1  C  Y N 285 
PHE CE2  C  Y N 286 
PHE CZ   C  Y N 287 
PHE OXT  O  N N 288 
PHE H    H  N N 289 
PHE H2   H  N N 290 
PHE HA   H  N N 291 
PHE HB2  H  N N 292 
PHE HB3  H  N N 293 
PHE HD1  H  N N 294 
PHE HD2  H  N N 295 
PHE HE1  H  N N 296 
PHE HE2  H  N N 297 
PHE HZ   H  N N 298 
PHE HXT  H  N N 299 
PRO N    N  N N 300 
PRO CA   C  N S 301 
PRO C    C  N N 302 
PRO O    O  N N 303 
PRO CB   C  N N 304 
PRO CG   C  N N 305 
PRO CD   C  N N 306 
PRO OXT  O  N N 307 
PRO H    H  N N 308 
PRO HA   H  N N 309 
PRO HB2  H  N N 310 
PRO HB3  H  N N 311 
PRO HG2  H  N N 312 
PRO HG3  H  N N 313 
PRO HD2  H  N N 314 
PRO HD3  H  N N 315 
PRO HXT  H  N N 316 
SER N    N  N N 317 
SER CA   C  N S 318 
SER C    C  N N 319 
SER O    O  N N 320 
SER CB   C  N N 321 
SER OG   O  N N 322 
SER OXT  O  N N 323 
SER H    H  N N 324 
SER H2   H  N N 325 
SER HA   H  N N 326 
SER HB2  H  N N 327 
SER HB3  H  N N 328 
SER HG   H  N N 329 
SER HXT  H  N N 330 
THR N    N  N N 331 
THR CA   C  N S 332 
THR C    C  N N 333 
THR O    O  N N 334 
THR CB   C  N R 335 
THR OG1  O  N N 336 
THR CG2  C  N N 337 
THR OXT  O  N N 338 
THR H    H  N N 339 
THR H2   H  N N 340 
THR HA   H  N N 341 
THR HB   H  N N 342 
THR HG1  H  N N 343 
THR HG21 H  N N 344 
THR HG22 H  N N 345 
THR HG23 H  N N 346 
THR HXT  H  N N 347 
TRP N    N  N N 348 
TRP CA   C  N S 349 
TRP C    C  N N 350 
TRP O    O  N N 351 
TRP CB   C  N N 352 
TRP CG   C  Y N 353 
TRP CD1  C  Y N 354 
TRP CD2  C  Y N 355 
TRP NE1  N  Y N 356 
TRP CE2  C  Y N 357 
TRP CE3  C  Y N 358 
TRP CZ2  C  Y N 359 
TRP CZ3  C  Y N 360 
TRP CH2  C  Y N 361 
TRP OXT  O  N N 362 
TRP H    H  N N 363 
TRP H2   H  N N 364 
TRP HA   H  N N 365 
TRP HB2  H  N N 366 
TRP HB3  H  N N 367 
TRP HD1  H  N N 368 
TRP HE1  H  N N 369 
TRP HE3  H  N N 370 
TRP HZ2  H  N N 371 
TRP HZ3  H  N N 372 
TRP HH2  H  N N 373 
TRP HXT  H  N N 374 
TYR N    N  N N 375 
TYR CA   C  N S 376 
TYR C    C  N N 377 
TYR O    O  N N 378 
TYR CB   C  N N 379 
TYR CG   C  Y N 380 
TYR CD1  C  Y N 381 
TYR CD2  C  Y N 382 
TYR CE1  C  Y N 383 
TYR CE2  C  Y N 384 
TYR CZ   C  Y N 385 
TYR OH   O  N N 386 
TYR OXT  O  N N 387 
TYR H    H  N N 388 
TYR H2   H  N N 389 
TYR HA   H  N N 390 
TYR HB2  H  N N 391 
TYR HB3  H  N N 392 
TYR HD1  H  N N 393 
TYR HD2  H  N N 394 
TYR HE1  H  N N 395 
TYR HE2  H  N N 396 
TYR HH   H  N N 397 
TYR HXT  H  N N 398 
VAL N    N  N N 399 
VAL CA   C  N S 400 
VAL C    C  N N 401 
VAL O    O  N N 402 
VAL CB   C  N N 403 
VAL CG1  C  N N 404 
VAL CG2  C  N N 405 
VAL OXT  O  N N 406 
VAL H    H  N N 407 
VAL H2   H  N N 408 
VAL HA   H  N N 409 
VAL HB   H  N N 410 
VAL HG11 H  N N 411 
VAL HG12 H  N N 412 
VAL HG13 H  N N 413 
VAL HG21 H  N N 414 
VAL HG22 H  N N 415 
VAL HG23 H  N N 416 
VAL HXT  H  N N 417 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
MFU C1  C2   sing N N 237 
MFU C1  O1   sing N N 238 
MFU C1  O5   sing N N 239 
MFU C1  H1   sing N N 240 
MFU C2  C3   sing N N 241 
MFU C2  O2   sing N N 242 
MFU C2  H2   sing N N 243 
MFU C3  C4   sing N N 244 
MFU C3  O3   sing N N 245 
MFU C3  H3   sing N N 246 
MFU C4  C5   sing N N 247 
MFU C4  O4   sing N N 248 
MFU C4  H4   sing N N 249 
MFU C5  C6   sing N N 250 
MFU C5  O5   sing N N 251 
MFU C5  H5   sing N N 252 
MFU C6  H61  sing N N 253 
MFU C6  H62  sing N N 254 
MFU C6  H63  sing N N 255 
MFU O1  CM   sing N N 256 
MFU O2  HO2  sing N N 257 
MFU O3  HO3  sing N N 258 
MFU O4  HO4  sing N N 259 
MFU CM  HM1  sing N N 260 
MFU CM  HM2  sing N N 261 
MFU CM  HM3  sing N N 262 
PHE N   CA   sing N N 263 
PHE N   H    sing N N 264 
PHE N   H2   sing N N 265 
PHE CA  C    sing N N 266 
PHE CA  CB   sing N N 267 
PHE CA  HA   sing N N 268 
PHE C   O    doub N N 269 
PHE C   OXT  sing N N 270 
PHE CB  CG   sing N N 271 
PHE CB  HB2  sing N N 272 
PHE CB  HB3  sing N N 273 
PHE CG  CD1  doub Y N 274 
PHE CG  CD2  sing Y N 275 
PHE CD1 CE1  sing Y N 276 
PHE CD1 HD1  sing N N 277 
PHE CD2 CE2  doub Y N 278 
PHE CD2 HD2  sing N N 279 
PHE CE1 CZ   doub Y N 280 
PHE CE1 HE1  sing N N 281 
PHE CE2 CZ   sing Y N 282 
PHE CE2 HE2  sing N N 283 
PHE CZ  HZ   sing N N 284 
PHE OXT HXT  sing N N 285 
PRO N   CA   sing N N 286 
PRO N   CD   sing N N 287 
PRO N   H    sing N N 288 
PRO CA  C    sing N N 289 
PRO CA  CB   sing N N 290 
PRO CA  HA   sing N N 291 
PRO C   O    doub N N 292 
PRO C   OXT  sing N N 293 
PRO CB  CG   sing N N 294 
PRO CB  HB2  sing N N 295 
PRO CB  HB3  sing N N 296 
PRO CG  CD   sing N N 297 
PRO CG  HG2  sing N N 298 
PRO CG  HG3  sing N N 299 
PRO CD  HD2  sing N N 300 
PRO CD  HD3  sing N N 301 
PRO OXT HXT  sing N N 302 
SER N   CA   sing N N 303 
SER N   H    sing N N 304 
SER N   H2   sing N N 305 
SER CA  C    sing N N 306 
SER CA  CB   sing N N 307 
SER CA  HA   sing N N 308 
SER C   O    doub N N 309 
SER C   OXT  sing N N 310 
SER CB  OG   sing N N 311 
SER CB  HB2  sing N N 312 
SER CB  HB3  sing N N 313 
SER OG  HG   sing N N 314 
SER OXT HXT  sing N N 315 
THR N   CA   sing N N 316 
THR N   H    sing N N 317 
THR N   H2   sing N N 318 
THR CA  C    sing N N 319 
THR CA  CB   sing N N 320 
THR CA  HA   sing N N 321 
THR C   O    doub N N 322 
THR C   OXT  sing N N 323 
THR CB  OG1  sing N N 324 
THR CB  CG2  sing N N 325 
THR CB  HB   sing N N 326 
THR OG1 HG1  sing N N 327 
THR CG2 HG21 sing N N 328 
THR CG2 HG22 sing N N 329 
THR CG2 HG23 sing N N 330 
THR OXT HXT  sing N N 331 
TRP N   CA   sing N N 332 
TRP N   H    sing N N 333 
TRP N   H2   sing N N 334 
TRP CA  C    sing N N 335 
TRP CA  CB   sing N N 336 
TRP CA  HA   sing N N 337 
TRP C   O    doub N N 338 
TRP C   OXT  sing N N 339 
TRP CB  CG   sing N N 340 
TRP CB  HB2  sing N N 341 
TRP CB  HB3  sing N N 342 
TRP CG  CD1  doub Y N 343 
TRP CG  CD2  sing Y N 344 
TRP CD1 NE1  sing Y N 345 
TRP CD1 HD1  sing N N 346 
TRP CD2 CE2  doub Y N 347 
TRP CD2 CE3  sing Y N 348 
TRP NE1 CE2  sing Y N 349 
TRP NE1 HE1  sing N N 350 
TRP CE2 CZ2  sing Y N 351 
TRP CE3 CZ3  doub Y N 352 
TRP CE3 HE3  sing N N 353 
TRP CZ2 CH2  doub Y N 354 
TRP CZ2 HZ2  sing N N 355 
TRP CZ3 CH2  sing Y N 356 
TRP CZ3 HZ3  sing N N 357 
TRP CH2 HH2  sing N N 358 
TRP OXT HXT  sing N N 359 
TYR N   CA   sing N N 360 
TYR N   H    sing N N 361 
TYR N   H2   sing N N 362 
TYR CA  C    sing N N 363 
TYR CA  CB   sing N N 364 
TYR CA  HA   sing N N 365 
TYR C   O    doub N N 366 
TYR C   OXT  sing N N 367 
TYR CB  CG   sing N N 368 
TYR CB  HB2  sing N N 369 
TYR CB  HB3  sing N N 370 
TYR CG  CD1  doub Y N 371 
TYR CG  CD2  sing Y N 372 
TYR CD1 CE1  sing Y N 373 
TYR CD1 HD1  sing N N 374 
TYR CD2 CE2  doub Y N 375 
TYR CD2 HD2  sing N N 376 
TYR CE1 CZ   doub Y N 377 
TYR CE1 HE1  sing N N 378 
TYR CE2 CZ   sing Y N 379 
TYR CE2 HE2  sing N N 380 
TYR CZ  OH   sing N N 381 
TYR OH  HH   sing N N 382 
TYR OXT HXT  sing N N 383 
VAL N   CA   sing N N 384 
VAL N   H    sing N N 385 
VAL N   H2   sing N N 386 
VAL CA  C    sing N N 387 
VAL CA  CB   sing N N 388 
VAL CA  HA   sing N N 389 
VAL C   O    doub N N 390 
VAL C   OXT  sing N N 391 
VAL CB  CG1  sing N N 392 
VAL CB  CG2  sing N N 393 
VAL CB  HB   sing N N 394 
VAL CG1 HG11 sing N N 395 
VAL CG1 HG12 sing N N 396 
VAL CG1 HG13 sing N N 397 
VAL CG2 HG21 sing N N 398 
VAL CG2 HG22 sing N N 399 
VAL CG2 HG23 sing N N 400 
VAL OXT HXT  sing N N 401 
# 
_pdbx_audit_support.funding_organization   'UK Research and Innovation (UKRI)' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           BB/V014137/1 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5E4K 
_pdbx_initial_refinement_model.details          'Chain A residues 380-506 and two Ca2+ ions' 
# 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.name_Hall        'P 2 2ab' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9QY1 
_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]   0.021906 
_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]   0.015024 
_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]   0.026860 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CA ? ? 16.26893 3.65395 ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 7.30273  -17.61773 7.57900  1.000 70.98941 ? 380 ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 6.42733  -16.54700 7.11023  1.000 73.53324 ? 380 ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 7.23960  -15.38047 6.54713  1.000 66.10672 ? 380 ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 8.43512  -15.51988 6.29128  1.000 70.04914 ? 380 ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 5.52115  -16.07596 8.23528  1.000 73.36209 ? 380 ALA A CB  1 
ATOM   6    N  N   . VAL A 1 2   ? 6.59527  -14.22891 6.34803  1.000 60.28588 ? 381 VAL A N   1 
ATOM   7    C  CA  . VAL A 1 2   ? 7.28429  -13.07962 5.77000  1.000 54.82682 ? 381 VAL A CA  1 
ATOM   8    C  C   . VAL A 1 2   ? 8.04030  -12.33188 6.86298  1.000 53.56032 ? 381 VAL A C   1 
ATOM   9    O  O   . VAL A 1 2   ? 7.62688  -12.27508 8.02808  1.000 52.16759 ? 381 VAL A O   1 
ATOM   10   C  CB  . VAL A 1 2   ? 6.30729  -12.15153 5.01112  1.000 53.00121 ? 381 VAL A CB  1 
ATOM   11   C  CG1 . VAL A 1 2   ? 5.24720  -12.96383 4.28478  1.000 52.37791 ? 381 VAL A CG1 1 
ATOM   12   C  CG2 . VAL A 1 2   ? 5.68155  -11.10496 5.92663  1.000 44.19328 ? 381 VAL A CG2 1 
ATOM   13   N  N   . GLU A 1 3   ? 9.17696  -11.76590 6.48162  1.000 53.89812 ? 382 GLU A N   1 
ATOM   14   C  CA  . GLU A 1 3   ? 10.07002 -11.08221 7.39969  1.000 52.65028 ? 382 GLU A CA  1 
ATOM   15   C  C   . GLU A 1 3   ? 10.52230 -9.78080  6.75962  1.000 50.86976 ? 382 GLU A C   1 
ATOM   16   O  O   . GLU A 1 3   ? 10.35230 -9.56646  5.55651  1.000 51.57785 ? 382 GLU A O   1 
ATOM   17   C  CB  . GLU A 1 3   ? 11.27699 -11.96442 7.75237  1.000 55.93042 ? 382 GLU A CB  1 
ATOM   18   C  CG  . GLU A 1 3   ? 11.91000 -12.63749 6.54097  1.000 59.82884 ? 382 GLU A CG  1 
ATOM   19   C  CD  . GLU A 1 3   ? 12.62171 -13.94212 6.88373  1.000 66.89022 ? 382 GLU A CD  1 
ATOM   20   O  OE1 . GLU A 1 3   ? 12.97935 -14.13887 8.06456  1.000 69.53420 ? 382 GLU A OE1 1 
ATOM   21   O  OE2 . GLU A 1 3   ? 12.81585 -14.77688 5.97058  1.000 75.18013 ? 382 GLU A OE2 1 
ATOM   22   N  N   . CYS A 1 4   ? 11.08123 -8.89730  7.58428  1.000 49.85209 ? 383 CYS A N   1 
ATOM   23   C  CA  . CYS A 1 4   ? 11.75117 -7.71440  7.06499  1.000 47.63150 ? 383 CYS A CA  1 
ATOM   24   C  C   . CYS A 1 4   ? 13.01576 -8.11677  6.32263  1.000 46.75092 ? 383 CYS A C   1 
ATOM   25   O  O   . CYS A 1 4   ? 13.60820 -9.16939  6.58166  1.000 46.33972 ? 383 CYS A O   1 
ATOM   26   C  CB  . CYS A 1 4   ? 12.11389 -6.75546  8.19518  1.000 39.88617 ? 383 CYS A CB  1 
ATOM   27   S  SG  . CYS A 1 4   ? 10.69146 -6.23528  9.15287  1.000 43.50368 ? 383 CYS A SG  1 
ATOM   28   N  N   . GLU A 1 5   ? 13.43375 -7.26480  5.38803  1.000 45.38297 ? 384 GLU A N   1 
ATOM   29   C  CA  . GLU A 1 5   ? 14.72565 -7.47417  4.75946  1.000 47.17824 ? 384 GLU A CA  1 
ATOM   30   C  C   . GLU A 1 5   ? 15.81264 -7.32198  5.81823  1.000 43.26131 ? 384 GLU A C   1 
ATOM   31   O  O   . GLU A 1 5   ? 15.56473 -6.76951  6.89190  1.000 41.53542 ? 384 GLU A O   1 
ATOM   32   C  CB  . GLU A 1 5   ? 14.93798 -6.47278  3.62785  1.000 49.83926 ? 384 GLU A CB  1 
ATOM   33   C  CG  . GLU A 1 5   ? 13.68005 -6.15305  2.84151  1.000 53.44087 ? 384 GLU A CG  1 
ATOM   34   C  CD  . GLU A 1 5   ? 13.78366 -4.82235  2.12510  1.000 57.05109 ? 384 GLU A CD  1 
ATOM   35   O  OE1 . GLU A 1 5   ? 14.82387 -4.57560  1.47559  1.000 60.90886 ? 384 GLU A OE1 1 
ATOM   36   O  OE2 . GLU A 1 5   ? 12.83622 -4.01363  2.22986  1.000 60.17504 ? 384 GLU A OE2 1 
ATOM   37   N  N   . PRO A 1 6   ? 17.01658 -7.82538  5.55643  1.000 45.32842 ? 385 PRO A N   1 
ATOM   38   C  CA  . PRO A 1 6   ? 18.11607 -7.58797  6.49528  1.000 46.27977 ? 385 PRO A CA  1 
ATOM   39   C  C   . PRO A 1 6   ? 18.30598 -6.09991  6.74092  1.000 45.31232 ? 385 PRO A C   1 
ATOM   40   O  O   . PRO A 1 6   ? 18.09627 -5.27080  5.85058  1.000 45.96706 ? 385 PRO A O   1 
ATOM   41   C  CB  . PRO A 1 6   ? 19.32269 -8.20778  5.78668  1.000 45.61184 ? 385 PRO A CB  1 
ATOM   42   C  CG  . PRO A 1 6   ? 18.73108 -9.26418  4.92326  1.000 49.58938 ? 385 PRO A CG  1 
ATOM   43   C  CD  . PRO A 1 6   ? 17.43088 -8.68772  4.43859  1.000 46.99967 ? 385 PRO A CD  1 
ATOM   44   N  N   . SER A 1 7   ? 18.66871 -5.76736  7.97949  1.000 44.39458 ? 386 SER A N   1 
ATOM   45   C  CA  . SER A 1 7   ? 18.88308 -4.41290  8.49521  1.000 43.96641 ? 386 SER A CA  1 
ATOM   46   C  C   . SER A 1 7   ? 17.60085 -3.60406  8.66330  1.000 39.68098 ? 386 SER A C   1 
ATOM   47   O  O   . SER A 1 7   ? 17.68762 -2.42213  9.02825  1.000 39.99554 ? 386 SER A O   1 
ATOM   48   C  CB  . SER A 1 7   ? 19.85917 -3.59413  7.63658  1.000 50.64296 ? 386 SER A CB  1 
ATOM   49   O  OG  . SER A 1 7   ? 19.24021 -3.19809  6.42804  1.000 52.08749 ? 386 SER A OG  1 
ATOM   50   N  N   . TRP A 1 8   ? 16.42312 -4.18042  8.39990  1.000 36.74792 ? 387 TRP A N   1 
ATOM   51   C  CA  . TRP A 1 8   ? 15.14236 -3.59064  8.78255  1.000 36.00380 ? 387 TRP A CA  1 
ATOM   52   C  C   . TRP A 1 8   ? 14.63406 -4.28192  10.04093 1.000 32.16872 ? 387 TRP A C   1 
ATOM   53   O  O   . TRP A 1 8   ? 14.65567 -5.51605  10.12494 1.000 34.77841 ? 387 TRP A O   1 
ATOM   54   C  CB  . TRP A 1 8   ? 14.10259 -3.72395  7.66692  1.000 34.77253 ? 387 TRP A CB  1 
ATOM   55   C  CG  . TRP A 1 8   ? 14.40099 -2.91162  6.45306  1.000 36.79797 ? 387 TRP A CG  1 
ATOM   56   C  CD1 . TRP A 1 8   ? 15.39004 -3.13784  5.54060  1.000 42.96374 ? 387 TRP A CD1 1 
ATOM   57   C  CD2 . TRP A 1 8   ? 13.70068 -1.74717  6.00473  1.000 35.38412 ? 387 TRP A CD2 1 
ATOM   58   N  NE1 . TRP A 1 8   ? 15.35404 -2.17997  4.55566  1.000 44.56057 ? 387 TRP A NE1 1 
ATOM   59   C  CE2 . TRP A 1 8   ? 14.32631 -1.31439  4.81820  1.000 39.67993 ? 387 TRP A CE2 1 
ATOM   60   C  CE3 . TRP A 1 8   ? 12.61025 -1.01930  6.49675  1.000 33.23320 ? 387 TRP A CE3 1 
ATOM   61   C  CZ2 . TRP A 1 8   ? 13.89632 -0.19436  4.11319  1.000 36.99762 ? 387 TRP A CZ2 1 
ATOM   62   C  CZ3 . TRP A 1 8   ? 12.18334 0.08712   5.79608  1.000 31.10034 ? 387 TRP A CZ3 1 
ATOM   63   C  CH2 . TRP A 1 8   ? 12.82490 0.49167   4.61604  1.000 32.87436 ? 387 TRP A CH2 1 
ATOM   64   N  N   . GLN A 1 9   ? 14.18696 -3.49176  11.01341 1.000 26.52132 ? 388 GLN A N   1 
ATOM   65   C  CA  . GLN A 1 9   ? 13.78280 -4.03190  12.30587 1.000 28.53342 ? 388 GLN A CA  1 
ATOM   66   C  C   . GLN A 1 9   ? 12.27092 -4.15115  12.34836 1.000 27.21151 ? 388 GLN A C   1 
ATOM   67   O  O   . GLN A 1 9   ? 11.58546 -3.18290  11.98749 1.000 25.85847 ? 388 GLN A O   1 
ATOM   68   C  CB  . GLN A 1 9   ? 14.26309 -3.12643  13.44062 1.000 25.28934 ? 388 GLN A CB  1 
ATOM   69   C  CG  . GLN A 1 9   ? 15.79347 -2.97040  13.43120 1.000 34.53410 ? 388 GLN A CG  1 
ATOM   70   C  CD  . GLN A 1 9   ? 16.34298 -2.21530  14.62400 1.000 36.30537 ? 388 GLN A CD  1 
ATOM   71   O  OE1 . GLN A 1 9   ? 15.97291 -2.47450  15.77262 1.000 36.60423 ? 388 GLN A OE1 1 
ATOM   72   N  NE2 . GLN A 1 9   ? 17.24408 -1.26912  14.35354 1.000 38.69603 ? 388 GLN A NE2 1 
ATOM   73   N  N   . PRO A 1 10  ? 11.73331 -5.29527  12.77334 1.000 27.56343 ? 389 PRO A N   1 
ATOM   74   C  CA  . PRO A 1 10  ? 10.27071 -5.46298  12.82734 1.000 28.77790 ? 389 PRO A CA  1 
ATOM   75   C  C   . PRO A 1 10  ? 9.65603  -4.88744  14.09570 1.000 29.66480 ? 389 PRO A C   1 
ATOM   76   O  O   . PRO A 1 10  ? 10.23800 -4.95182  15.18133 1.000 29.30301 ? 389 PRO A O   1 
ATOM   77   C  CB  . PRO A 1 10  ? 10.09281 -6.98197  12.78524 1.000 30.69011 ? 389 PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 10  ? 11.37080 -7.52922  13.38167 1.000 32.29224 ? 389 PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 10  ? 12.45759 -6.56694  12.98663 1.000 28.52700 ? 389 PRO A CD  1 
ATOM   80   N  N   . PHE A 1 11  ? 8.45285  -4.32943  13.95334 1.000 27.23326 ? 390 PHE A N   1 
ATOM   81   C  CA  . PHE A 1 11  ? 7.68767  -3.87990  15.11044 1.000 25.77267 ? 390 PHE A CA  1 
ATOM   82   C  C   . PHE A 1 11  ? 6.22368  -3.75915  14.72507 1.000 25.44580 ? 390 PHE A C   1 
ATOM   83   O  O   . PHE A 1 11  ? 5.88998  -3.02416  13.79017 1.000 25.28465 ? 390 PHE A O   1 
ATOM   84   C  CB  . PHE A 1 11  ? 8.18077  -2.54365  15.64625 1.000 25.54423 ? 390 PHE A CB  1 
ATOM   85   C  CG  . PHE A 1 11  ? 7.31282  -1.97023  16.73317 1.000 25.99234 ? 390 PHE A CG  1 
ATOM   86   C  CD1 . PHE A 1 11  ? 7.38504  -2.45810  18.02690 1.000 27.04030 ? 390 PHE A CD1 1 
ATOM   87   C  CD2 . PHE A 1 11  ? 6.42333  -0.93870  16.45809 1.000 26.29555 ? 390 PHE A CD2 1 
ATOM   88   C  CE1 . PHE A 1 11  ? 6.58902  -1.92233  19.02133 1.000 27.42583 ? 390 PHE A CE1 1 
ATOM   89   C  CE2 . PHE A 1 11  ? 5.62579  -0.40750  17.44387 1.000 25.33433 ? 390 PHE A CE2 1 
ATOM   90   C  CZ  . PHE A 1 11  ? 5.70718  -0.90202  18.73018 1.000 25.06451 ? 390 PHE A CZ  1 
ATOM   91   N  N   . GLN A 1 12  ? 5.36606  -4.43839  15.47565 1.000 25.88135 ? 391 GLN A N   1 
ATOM   92   C  CA  . GLN A 1 12  ? 3.90576  -4.35092  15.33160 1.000 23.82913 ? 391 GLN A CA  1 
ATOM   93   C  C   . GLN A 1 12  ? 3.49230  -4.25846  13.86377 1.000 25.71478 ? 391 GLN A C   1 
ATOM   94   O  O   . GLN A 1 12  ? 2.81197  -3.33166  13.42134 1.000 28.89496 ? 391 GLN A O   1 
ATOM   95   C  CB  . GLN A 1 12  ? 3.33906  -3.18492  16.14145 1.000 25.54980 ? 391 GLN A CB  1 
ATOM   96   C  CG  . GLN A 1 12  ? 3.50220  -3.37943  17.64535 1.000 26.58113 ? 391 GLN A CG  1 
ATOM   97   C  CD  . GLN A 1 12  ? 2.70231  -2.40268  18.48079 1.000 27.78377 ? 391 GLN A CD  1 
ATOM   98   O  OE1 . GLN A 1 12  ? 2.11830  -1.44821  17.96677 1.000 27.90651 ? 391 GLN A OE1 1 
ATOM   99   N  NE2 . GLN A 1 12  ? 2.67636  -2.63890  19.78821 1.000 28.66208 ? 391 GLN A NE2 1 
ATOM   100  N  N   . GLY A 1 13  ? 3.92013  -5.25705  13.10847 1.000 25.37014 ? 392 GLY A N   1 
ATOM   101  C  CA  . GLY A 1 13  ? 3.44789  -5.45968  11.76649 1.000 26.03228 ? 392 GLY A CA  1 
ATOM   102  C  C   . GLY A 1 13  ? 4.26294  -4.80014  10.67982 1.000 26.55021 ? 392 GLY A C   1 
ATOM   103  O  O   . GLY A 1 13  ? 4.05844  -5.11894  9.50408  1.000 26.23532 ? 392 GLY A O   1 
ATOM   104  N  N   . HIS A 1 14  ? 5.20069  -3.91656  11.02877 1.000 25.99102 ? 393 HIS A N   1 
ATOM   105  C  CA  . HIS A 1 14  ? 5.90978  -3.12922  10.03497 1.000 24.69902 ? 393 HIS A CA  1 
ATOM   106  C  C   . HIS A 1 14  ? 7.41337  -3.25320  10.23954 1.000 27.30474 ? 393 HIS A C   1 
ATOM   107  O  O   . HIS A 1 14  ? 7.88335  -3.75605  11.26483 1.000 22.60979 ? 393 HIS A O   1 
ATOM   108  C  CB  . HIS A 1 14  ? 5.47470  -1.65822  10.08324 1.000 27.38439 ? 393 HIS A CB  1 
ATOM   109  C  CG  . HIS A 1 14  ? 4.03050  -1.45312  9.73018  1.000 31.22630 ? 393 HIS A CG  1 
ATOM   110  N  ND1 . HIS A 1 14  ? 3.61271  -1.12250  8.45860  1.000 34.58766 ? 393 HIS A ND1 1 
ATOM   111  C  CD2 . HIS A 1 14  ? 2.90712  -1.55259  10.47955 1.000 35.66673 ? 393 HIS A CD2 1 
ATOM   112  C  CE1 . HIS A 1 14  ? 2.29545  -1.01190  8.44366  1.000 38.69504 ? 393 HIS A CE1 1 
ATOM   113  N  NE2 . HIS A 1 14  ? 1.84196  -1.27198  9.65672  1.000 38.10357 ? 393 HIS A NE2 1 
ATOM   114  N  N   . CYS A 1 15  ? 8.15403  -2.80358  9.22765  1.000 24.53001 ? 394 CYS A N   1 
ATOM   115  C  CA  . CYS A 1 15  ? 9.61139  -2.83772  9.21053  1.000 27.32670 ? 394 CYS A CA  1 
ATOM   116  C  C   . CYS A 1 15  ? 10.15261 -1.41666  9.24039  1.000 25.72845 ? 394 CYS A C   1 
ATOM   117  O  O   . CYS A 1 15  ? 9.57504  -0.51410  8.63438  1.000 23.35890 ? 394 CYS A O   1 
ATOM   118  C  CB  . CYS A 1 15  ? 10.12342 -3.55064  7.96364  1.000 28.32293 ? 394 CYS A CB  1 
ATOM   119  S  SG  . CYS A 1 15  ? 9.53034  -5.22117  7.81371  1.000 36.19353 ? 394 CYS A SG  1 
ATOM   120  N  N   . TYR A 1 16  ? 11.28252 -1.22475  9.92936  1.000 26.97178 ? 395 TYR A N   1 
ATOM   121  C  CA  . TYR A 1 16  ? 11.81163 0.11343   10.19201 1.000 24.06138 ? 395 TYR A CA  1 
ATOM   122  C  C   . TYR A 1 16  ? 13.31548 0.15717   9.94778  1.000 25.56393 ? 395 TYR A C   1 
ATOM   123  O  O   . TYR A 1 16  ? 14.03228 -0.76865  10.32169 1.000 24.31313 ? 395 TYR A O   1 
ATOM   124  C  CB  . TYR A 1 16  ? 11.53974 0.54662   11.63569 1.000 21.75921 ? 395 TYR A CB  1 
ATOM   125  C  CG  . TYR A 1 16  ? 10.07440 0.63052   12.00673 1.000 21.74169 ? 395 TYR A CG  1 
ATOM   126  C  CD1 . TYR A 1 16  ? 9.36996  -0.50781  12.38692 1.000 24.77675 ? 395 TYR A CD1 1 
ATOM   127  C  CD2 . TYR A 1 16  ? 9.40518  1.84096   11.98833 1.000 21.90875 ? 395 TYR A CD2 1 
ATOM   128  C  CE1 . TYR A 1 16  ? 8.01112  -0.43628  12.73593 1.000 24.65271 ? 395 TYR A CE1 1 
ATOM   129  C  CE2 . TYR A 1 16  ? 8.05742  1.92654   12.33078 1.000 23.82437 ? 395 TYR A CE2 1 
ATOM   130  C  CZ  . TYR A 1 16  ? 7.37218  0.78858   12.70873 1.000 24.01758 ? 395 TYR A CZ  1 
ATOM   131  O  OH  . TYR A 1 16  ? 6.03707  0.86151   13.05125 1.000 26.07892 ? 395 TYR A OH  1 
ATOM   132  N  N   . ARG A 1 17  ? 13.79836 1.25284   9.36149  1.000 26.20094 ? 396 ARG A N   1 
ATOM   133  C  CA  . ARG A 1 17  ? 15.23255 1.37741   9.12552  1.000 27.65564 ? 396 ARG A CA  1 
ATOM   134  C  C   . ARG A 1 17  ? 15.68944 2.81651   9.32241  1.000 26.16287 ? 396 ARG A C   1 
ATOM   135  O  O   . ARG A 1 17  ? 15.10110 3.74273   8.76074  1.000 25.50774 ? 396 ARG A O   1 
ATOM   136  C  CB  . ARG A 1 17  ? 15.60092 0.89709   7.71713  1.000 30.07423 ? 396 ARG A CB  1 
ATOM   137  C  CG  . ARG A 1 17  ? 17.09316 0.79465   7.50815  1.000 35.94816 ? 396 ARG A CG  1 
ATOM   138  C  CD  . ARG A 1 17  ? 17.46857 0.60562   6.05215  1.000 40.99030 ? 396 ARG A CD  1 
ATOM   139  N  NE  . ARG A 1 17  ? 18.90408 0.80922   5.89215  1.000 51.97131 ? 396 ARG A NE  1 
ATOM   140  C  CZ  . ARG A 1 17  ? 19.76648 -0.13943  5.55765  1.000 55.04639 ? 396 ARG A CZ  1 
ATOM   141  N  NH1 . ARG A 1 17  ? 19.36177 -1.35605  5.23348  1.000 59.79244 ? 396 ARG A NH1 1 
ATOM   142  N  NH2 . ARG A 1 17  ? 21.06757 0.14213   5.53831  1.000 57.77483 ? 396 ARG A NH2 1 
ATOM   143  N  N   . LEU A 1 18  ? 16.74004 3.00283   10.11829 1.000 26.66293 ? 397 LEU A N   1 
ATOM   144  C  CA  . LEU A 1 18  ? 17.38342 4.31121   10.19546 1.000 27.97500 ? 397 LEU A CA  1 
ATOM   145  C  C   . LEU A 1 18  ? 18.24857 4.52743   8.96426  1.000 30.18458 ? 397 LEU A C   1 
ATOM   146  O  O   . LEU A 1 18  ? 19.09901 3.69581   8.64146  1.000 28.45786 ? 397 LEU A O   1 
ATOM   147  C  CB  . LEU A 1 18  ? 18.24051 4.42435   11.45781 1.000 28.43544 ? 397 LEU A CB  1 
ATOM   148  C  CG  . LEU A 1 18  ? 19.17258 5.63587   11.50458 1.000 28.26723 ? 397 LEU A CG  1 
ATOM   149  C  CD1 . LEU A 1 18  ? 18.36942 6.90156   11.71796 1.000 25.56266 ? 397 LEU A CD1 1 
ATOM   150  C  CD2 . LEU A 1 18  ? 20.24076 5.46671   12.58453 1.000 30.38484 ? 397 LEU A CD2 1 
ATOM   151  N  N   . GLN A 1 19  ? 18.02712 5.63479   8.26777  1.000 28.92126 ? 398 GLN A N   1 
ATOM   152  C  CA  . GLN A 1 19  ? 18.89353 6.05214   7.17165  1.000 31.00838 ? 398 GLN A CA  1 
ATOM   153  C  C   . GLN A 1 19  ? 19.86577 7.09079   7.71349  1.000 30.96997 ? 398 GLN A C   1 
ATOM   154  O  O   . GLN A 1 19  ? 19.46382 8.20841   8.04152  1.000 29.24167 ? 398 GLN A O   1 
ATOM   155  C  CB  . GLN A 1 19  ? 18.07573 6.61304   6.01576  1.000 32.46963 ? 398 GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 19  ? 17.02350 5.65723   5.53321  1.000 32.86318 ? 398 GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 19  ? 16.40046 6.09954   4.24092  1.000 37.94751 ? 398 GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 19  ? 16.43337 5.37023   3.25087  1.000 42.30688 ? 398 GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 19  ? 15.78825 7.28410   4.24517  1.000 34.43819 ? 398 GLN A NE2 1 
ATOM   160  N  N   . ALA A 1 20  ? 21.14825 6.72417   7.79885  1.000 30.97388 ? 399 ALA A N   1 
ATOM   161  C  CA  . ALA A 1 20  ? 22.11115 7.55577   8.50392  1.000 30.70420 ? 399 ALA A CA  1 
ATOM   162  C  C   . ALA A 1 20  ? 22.53307 8.77158   7.69217  1.000 33.15278 ? 399 ALA A C   1 
ATOM   163  O  O   . ALA A 1 20  ? 22.94466 9.78464   8.27142  1.000 35.22641 ? 399 ALA A O   1 
ATOM   164  C  CB  . ALA A 1 20  ? 23.34705 6.72631   8.86678  1.000 38.56297 ? 399 ALA A CB  1 
ATOM   165  N  N   . GLU A 1 21  ? 22.45346 8.68542   6.36603  1.000 34.04100 ? 400 GLU A N   1 
ATOM   166  C  CA  . GLU A 1 21  ? 22.95035 9.74387   5.49782  1.000 36.41193 ? 400 GLU A CA  1 
ATOM   167  C  C   . GLU A 1 21  ? 22.10775 11.00165  5.66760  1.000 32.05326 ? 400 GLU A C   1 
ATOM   168  O  O   . GLU A 1 21  ? 20.87901 10.93060  5.69410  1.000 34.39361 ? 400 GLU A O   1 
ATOM   169  C  CB  . GLU A 1 21  ? 22.90908 9.26793   4.04930  1.000 38.44304 ? 400 GLU A CB  1 
ATOM   170  C  CG  . GLU A 1 21  ? 23.97438 9.83153   3.13885  1.000 45.47270 ? 400 GLU A CG  1 
ATOM   171  C  CD  . GLU A 1 21  ? 24.32734 8.85013   2.02932  1.000 50.05361 ? 400 GLU A CD  1 
ATOM   172  O  OE1 . GLU A 1 21  ? 23.42301 8.08489   1.62452  1.000 58.96197 ? 400 GLU A OE1 1 
ATOM   173  O  OE2 . GLU A 1 21  ? 25.49723 8.82293   1.58191  1.000 54.41493 ? 400 GLU A OE2 1 
ATOM   174  N  N   . LYS A 1 22  ? 22.75921 12.15717  5.77501  1.000 33.18596 ? 401 LYS A N   1 
ATOM   175  C  CA  . LYS A 1 22  ? 22.02486 13.40690  5.96314  1.000 32.49903 ? 401 LYS A CA  1 
ATOM   176  C  C   . LYS A 1 22  ? 21.51785 13.91958  4.61984  1.000 33.29288 ? 401 LYS A C   1 
ATOM   177  O  O   . LYS A 1 22  ? 22.31305 14.19730  3.71822  1.000 32.73630 ? 401 LYS A O   1 
ATOM   178  C  CB  . LYS A 1 22  ? 22.89901 14.46063  6.64122  1.000 35.92466 ? 401 LYS A CB  1 
ATOM   179  C  CG  . LYS A 1 22  ? 23.28871 14.11978  8.07738  1.000 35.83527 ? 401 LYS A CG  1 
ATOM   180  C  CD  . LYS A 1 22  ? 24.17226 15.19018  8.68513  1.000 40.16497 ? 401 LYS A CD  1 
ATOM   181  C  CE  . LYS A 1 22  ? 24.71798 14.72409  10.02977 1.000 46.10148 ? 401 LYS A CE  1 
ATOM   182  N  NZ  . LYS A 1 22  ? 25.44648 15.79780  10.75811 1.000 46.82087 ? 401 LYS A NZ  1 
ATOM   183  N  N   . ARG A 1 23  ? 20.19612 14.06337  4.49969  1.000 32.63904 ? 402 ARG A N   1 
ATOM   184  C  CA  . ARG A 1 23  ? 19.54617 14.53787  3.28444  1.000 32.82675 ? 402 ARG A CA  1 
ATOM   185  C  C   . ARG A 1 23  ? 18.40621 15.48161  3.64744  1.000 31.74849 ? 402 ARG A C   1 
ATOM   186  O  O   . ARG A 1 23  ? 17.92933 15.50589  4.78616  1.000 29.79823 ? 402 ARG A O   1 
ATOM   187  C  CB  . ARG A 1 23  ? 18.95301 13.39869  2.44703  1.000 32.07414 ? 402 ARG A CB  1 
ATOM   188  C  CG  . ARG A 1 23  ? 19.87673 12.26268  2.09556  1.000 35.86183 ? 402 ARG A CG  1 
ATOM   189  C  CD  . ARG A 1 23  ? 19.06584 11.17667  1.40864  1.000 35.78895 ? 402 ARG A CD  1 
ATOM   190  N  NE  . ARG A 1 23  ? 19.86769 10.00497  1.08816  1.000 36.93502 ? 402 ARG A NE  1 
ATOM   191  C  CZ  . ARG A 1 23  ? 19.93977 8.92087   1.84746  1.000 39.97236 ? 402 ARG A CZ  1 
ATOM   192  N  NH1 . ARG A 1 23  ? 19.26979 8.82733   2.98579  1.000 38.37949 ? 402 ARG A NH1 1 
ATOM   193  N  NH2 . ARG A 1 23  ? 20.69950 7.90377   1.45359  1.000 42.65422 ? 402 ARG A NH2 1 
ATOM   194  N  N   . SER A 1 24  ? 17.94760 16.23625  2.64613  1.000 32.56019 ? 403 SER A N   1 
ATOM   195  C  CA  . SER A 1 24  ? 16.71229 17.00652  2.77743  1.000 28.81478 ? 403 SER A CA  1 
ATOM   196  C  C   . SER A 1 24  ? 15.51792 16.08252  3.02620  1.000 29.59666 ? 403 SER A C   1 
ATOM   197  O  O   . SER A 1 24  ? 15.58767 14.86268  2.85282  1.000 30.35196 ? 403 SER A O   1 
ATOM   198  C  CB  . SER A 1 24  ? 16.45791 17.82307  1.51535  1.000 31.88256 ? 403 SER A CB  1 
ATOM   199  O  OG  . SER A 1 24  ? 16.10775 16.96431  0.44580  1.000 34.02705 ? 403 SER A OG  1 
ATOM   200  N  N   . TRP A 1 25  ? 14.38953 16.68324  3.41771  1.000 26.34156 ? 404 TRP A N   1 
ATOM   201  C  CA  . TRP A 1 25  ? 13.19525 15.87348  3.66890  1.000 29.09971 ? 404 TRP A CA  1 
ATOM   202  C  C   . TRP A 1 25  ? 12.75213 15.15440  2.40113  1.000 28.17739 ? 404 TRP A C   1 
ATOM   203  O  O   . TRP A 1 25  ? 12.53142 13.93810  2.41137  1.000 27.95714 ? 404 TRP A O   1 
ATOM   204  C  CB  . TRP A 1 25  ? 12.07360 16.74499  4.22916  1.000 25.61783 ? 404 TRP A CB  1 
ATOM   205  C  CG  . TRP A 1 25  ? 10.82106 15.99744  4.65211  1.000 26.67178 ? 404 TRP A CG  1 
ATOM   206  C  CD1 . TRP A 1 25  ? 10.53808 15.48431  5.88932  1.000 23.90279 ? 404 TRP A CD1 1 
ATOM   207  C  CD2 . TRP A 1 25  ? 9.67510  15.73862  3.84029  1.000 25.67528 ? 404 TRP A CD2 1 
ATOM   208  N  NE1 . TRP A 1 25  ? 9.28970  14.89488  5.88899  1.000 24.57290 ? 404 TRP A NE1 1 
ATOM   209  C  CE2 . TRP A 1 25  ? 8.74114  15.04032  4.63991  1.000 26.99122 ? 404 TRP A CE2 1 
ATOM   210  C  CE3 . TRP A 1 25  ? 9.35256  16.01637  2.50851  1.000 27.29992 ? 404 TRP A CE3 1 
ATOM   211  C  CZ2 . TRP A 1 25  ? 7.50681  14.62320  4.14846  1.000 25.19493 ? 404 TRP A CZ2 1 
ATOM   212  C  CZ3 . TRP A 1 25  ? 8.12587  15.59526  2.02250  1.000 27.69786 ? 404 TRP A CZ3 1 
ATOM   213  C  CH2 . TRP A 1 25  ? 7.22119  14.90840  2.83937  1.000 27.01871 ? 404 TRP A CH2 1 
ATOM   214  N  N   . GLN A 1 26  ? 12.65192 15.88250  1.28711  1.000 28.09951 ? 405 GLN A N   1 
ATOM   215  C  CA  . GLN A 1 26  ? 12.21430 15.25835  0.03992  1.000 32.38783 ? 405 GLN A CA  1 
ATOM   216  C  C   . GLN A 1 26  ? 13.18898 14.18326  -0.42439 1.000 31.47942 ? 405 GLN A C   1 
ATOM   217  O  O   . GLN A 1 26  ? 12.76808 13.11415  -0.87780 1.000 32.87206 ? 405 GLN A O   1 
ATOM   218  C  CB  . GLN A 1 26  ? 12.03218 16.30971  -1.05442 1.000 32.42486 ? 405 GLN A CB  1 
ATOM   219  C  CG  . GLN A 1 26  ? 10.84929 17.23078  -0.84210 1.000 35.27013 ? 405 GLN A CG  1 
ATOM   220  C  CD  . GLN A 1 26  ? 11.20910 18.48555  -0.05477 1.000 40.03657 ? 405 GLN A CD  1 
ATOM   221  O  OE1 . GLN A 1 26  ? 12.30329 18.59368  0.50754  1.000 40.39410 ? 405 GLN A OE1 1 
ATOM   222  N  NE2 . GLN A 1 26  ? 10.28311 19.44580  -0.01541 1.000 35.08370 ? 405 GLN A NE2 1 
ATOM   223  N  N   . GLU A 1 27  ? 14.49449 14.44920  -0.33282 1.000 30.99539 ? 406 GLU A N   1 
ATOM   224  C  CA  . GLU A 1 27  ? 15.47824 13.43646  -0.70438 1.000 32.20652 ? 406 GLU A CA  1 
ATOM   225  C  C   . GLU A 1 27  ? 15.37766 12.20970  0.19616  1.000 30.45170 ? 406 GLU A C   1 
ATOM   226  O  O   . GLU A 1 27  ? 15.52420 11.07784  -0.27244 1.000 32.19784 ? 406 GLU A O   1 
ATOM   227  C  CB  . GLU A 1 27  ? 16.89106 14.02526  -0.65483 1.000 33.69753 ? 406 GLU A CB  1 
ATOM   228  C  CG  . GLU A 1 27  ? 17.26850 14.87970  -1.86302 1.000 36.04962 ? 406 GLU A CG  1 
ATOM   229  C  CD  . GLU A 1 27  ? 18.41489 15.85284  -1.58268 1.000 45.39537 ? 406 GLU A CD  1 
ATOM   230  O  OE1 . GLU A 1 27  ? 18.82598 15.98022  -0.40654 1.000 42.91024 ? 406 GLU A OE1 1 
ATOM   231  O  OE2 . GLU A 1 27  ? 18.90542 16.49556  -2.54133 1.000 47.42721 ? 406 GLU A OE2 1 
ATOM   232  N  N   . SER A 1 28  ? 15.15121 12.41216  1.49530  1.000 29.21802 ? 407 SER A N   1 
ATOM   233  C  CA  . SER A 1 28  ? 14.98759 11.27519  2.39351  1.000 30.04230 ? 407 SER A CA  1 
ATOM   234  C  C   . SER A 1 28  ? 13.77478 10.44910  2.00170  1.000 29.29317 ? 407 SER A C   1 
ATOM   235  O  O   . SER A 1 28  ? 13.82587 9.21446   2.01077  1.000 29.95388 ? 407 SER A O   1 
ATOM   236  C  CB  . SER A 1 28  ? 14.84723 11.75276  3.83963  1.000 28.74860 ? 407 SER A CB  1 
ATOM   237  O  OG  . SER A 1 28  ? 15.96823 12.52742  4.24100  1.000 29.12369 ? 407 SER A OG  1 
ATOM   238  N  N   . LYS A 1 29  ? 12.67063 11.11976  1.66467  1.000 29.18062 ? 408 LYS A N   1 
ATOM   239  C  CA  . LYS A 1 29  ? 11.46294 10.41452  1.24147  1.000 29.36312 ? 408 LYS A CA  1 
ATOM   240  C  C   . LYS A 1 29  ? 11.72013 9.60020   -0.01743 1.000 31.07503 ? 408 LYS A C   1 
ATOM   241  O  O   . LYS A 1 29  ? 11.29395 8.44417   -0.11418 1.000 31.66070 ? 408 LYS A O   1 
ATOM   242  C  CB  . LYS A 1 29  ? 10.32797 11.41380  1.00498  1.000 28.69449 ? 408 LYS A CB  1 
ATOM   243  C  CG  . LYS A 1 29  ? 8.95535  10.76580  0.78570  1.000 30.25988 ? 408 LYS A CG  1 
ATOM   244  C  CD  . LYS A 1 29  ? 7.89349  11.78660  0.40330  1.000 31.83981 ? 408 LYS A CD  1 
ATOM   245  C  CE  . LYS A 1 29  ? 8.14687  12.33036  -0.99329 1.000 35.06387 ? 408 LYS A CE  1 
ATOM   246  N  NZ  . LYS A 1 29  ? 6.99792  13.12803  -1.51131 1.000 44.72706 ? 408 LYS A NZ  1 
ATOM   247  N  N   . LYS A 1 30  ? 12.42077 10.18647  -0.99336 1.000 31.50740 ? 409 LYS A N   1 
ATOM   248  C  CA  . LYS A 1 30  ? 12.69262 9.47287   -2.23707 1.000 33.07488 ? 409 LYS A CA  1 
ATOM   249  C  C   . LYS A 1 30  ? 13.51968 8.22341   -1.97985 1.000 33.65394 ? 409 LYS A C   1 
ATOM   250  O  O   . LYS A 1 30  ? 13.29117 7.17927   -2.60091 1.000 37.31643 ? 409 LYS A O   1 
ATOM   251  C  CB  . LYS A 1 30  ? 13.40339 10.39212  -3.23219 1.000 34.71723 ? 409 LYS A CB  1 
ATOM   252  C  CG  . LYS A 1 30  ? 12.56548 11.59132  -3.66439 1.000 38.37023 ? 409 LYS A CG  1 
ATOM   253  C  CD  . LYS A 1 30  ? 13.33260 12.52554  -4.60030 1.000 43.42531 ? 409 LYS A CD  1 
ATOM   254  C  CE  . LYS A 1 30  ? 13.05087 12.20098  -6.05829 1.000 49.53816 ? 409 LYS A CE  1 
ATOM   255  N  NZ  . LYS A 1 30  ? 11.57643 12.16727  -6.30884 1.000 53.23855 ? 409 LYS A NZ  1 
ATOM   256  N  N   . MET A 1 31  ? 14.47891 8.30650   -1.05752 1.000 34.51770 ? 410 MET A N   1 
ATOM   257  C  CA  . MET A 1 31  ? 15.26177 7.12795   -0.70451 1.000 34.00735 ? 410 MET A CA  1 
ATOM   258  C  C   . MET A 1 31  ? 14.39081 6.04629   -0.07373 1.000 35.42668 ? 410 MET A C   1 
ATOM   259  O  O   . MET A 1 31  ? 14.55320 4.85863   -0.37900 1.000 35.84138 ? 410 MET A O   1 
ATOM   260  C  CB  . MET A 1 31  ? 16.39833 7.51597   0.24095  1.000 35.84862 ? 410 MET A CB  1 
ATOM   261  C  CG  . MET A 1 31  ? 17.33304 6.37119   0.59868  1.000 37.35586 ? 410 MET A CG  1 
ATOM   262  S  SD  . MET A 1 31  ? 18.73353 6.14787   -0.50840 1.000 48.14491 ? 410 MET A SD  1 
ATOM   263  C  CE  . MET A 1 31  ? 18.00052 5.32993   -1.91254 1.000 43.00701 ? 410 MET A CE  1 
ATOM   264  N  N   . CYS A 1 32  ? 13.46265 6.43031   0.80986  1.000 33.70090 ? 411 CYS A N   1 
ATOM   265  C  CA  . CYS A 1 32  ? 12.54318 5.44349   1.37514  1.000 33.68439 ? 411 CYS A CA  1 
ATOM   266  C  C   . CYS A 1 32  ? 11.69992 4.79608   0.28845  1.000 34.55443 ? 411 CYS A C   1 
ATOM   267  O  O   . CYS A 1 32  ? 11.50755 3.57467   0.28546  1.000 37.06704 ? 411 CYS A O   1 
ATOM   268  C  CB  . CYS A 1 32  ? 11.63111 6.08283   2.42253  1.000 32.01727 ? 411 CYS A CB  1 
ATOM   269  S  SG  . CYS A 1 32  ? 12.46579 6.66503   3.91059  1.000 34.42188 ? 411 CYS A SG  1 
ATOM   270  N  N   . LEU A 1 33  ? 11.17931 5.60352   -0.63671 1.000 36.09961 ? 412 LEU A N   1 
ATOM   271  C  CA  . LEU A 1 33  ? 10.38462 5.06862   -1.73590 1.000 35.92369 ? 412 LEU A CA  1 
ATOM   272  C  C   . LEU A 1 33  ? 11.19347 4.09560   -2.58243 1.000 38.35307 ? 412 LEU A C   1 
ATOM   273  O  O   . LEU A 1 33  ? 10.67601 3.05557   -3.01163 1.000 39.08907 ? 412 LEU A O   1 
ATOM   274  C  CB  . LEU A 1 33  ? 9.84958  6.21436   -2.59032 1.000 34.36884 ? 412 LEU A CB  1 
ATOM   275  C  CG  . LEU A 1 33  ? 8.78391  7.04125   -1.87303 1.000 35.50498 ? 412 LEU A CG  1 
ATOM   276  C  CD1 . LEU A 1 33  ? 8.49929  8.31447   -2.63425 1.000 39.39264 ? 412 LEU A CD1 1 
ATOM   277  C  CD2 . LEU A 1 33  ? 7.51601  6.21789   -1.71160 1.000 34.87602 ? 412 LEU A CD2 1 
ATOM   278  N  N   . ARG A 1 34  ? 12.46662 4.41028   -2.83068 1.000 38.98848 ? 413 ARG A N   1 
ATOM   279  C  CA  . ARG A 1 34  ? 13.31570 3.49522   -3.58722 1.000 40.89399 ? 413 ARG A CA  1 
ATOM   280  C  C   . ARG A 1 34  ? 13.45960 2.15041   -2.89184 1.000 44.48367 ? 413 ARG A C   1 
ATOM   281  O  O   . ARG A 1 34  ? 13.69454 1.13346   -3.55249 1.000 50.50759 ? 413 ARG A O   1 
ATOM   282  C  CB  . ARG A 1 34  ? 14.69883 4.10415   -3.80198 1.000 42.21410 ? 413 ARG A CB  1 
ATOM   283  C  CG  . ARG A 1 34  ? 14.73184 5.27094   -4.75436 1.000 43.52201 ? 413 ARG A CG  1 
ATOM   284  C  CD  . ARG A 1 34  ? 16.16297 5.74439   -4.93949 1.000 44.62589 ? 413 ARG A CD  1 
ATOM   285  N  NE  . ARG A 1 34  ? 16.27993 6.74818   -5.98694 1.000 45.91620 ? 413 ARG A NE  1 
ATOM   286  C  CZ  . ARG A 1 34  ? 17.43211 7.23530   -6.42678 1.000 46.13802 ? 413 ARG A CZ  1 
ATOM   287  N  NH1 . ARG A 1 34  ? 18.58914 6.83453   -5.92223 1.000 43.27746 ? 413 ARG A NH1 1 
ATOM   288  N  NH2 . ARG A 1 34  ? 17.42375 8.14093   -7.40237 1.000 45.58581 ? 413 ARG A NH2 1 
ATOM   289  N  N   . GLY A 1 35  ? 13.37009 2.13003   -1.56914 1.000 42.81022 ? 414 GLY A N   1 
ATOM   290  C  CA  . GLY A 1 35  ? 13.45688 0.90636   -0.80789 1.000 45.09102 ? 414 GLY A CA  1 
ATOM   291  C  C   . GLY A 1 35  ? 12.12453 0.24665   -0.55716 1.000 44.43418 ? 414 GLY A C   1 
ATOM   292  O  O   . GLY A 1 35  ? 12.04967 -0.67511  0.26081  1.000 46.95930 ? 414 GLY A O   1 
ATOM   293  N  N   . GLY A 1 36  ? 11.06875 0.69952   -1.23064 1.000 43.12298 ? 415 GLY A N   1 
ATOM   294  C  CA  . GLY A 1 36  ? 9.74946  0.12305   -1.08015 1.000 41.76143 ? 415 GLY A CA  1 
ATOM   295  C  C   . GLY A 1 36  ? 8.94949  0.61577   0.10355  1.000 39.83758 ? 415 GLY A C   1 
ATOM   296  O  O   . GLY A 1 36  ? 7.89529  0.04286   0.39918  1.000 38.23089 ? 415 GLY A O   1 
ATOM   297  N  N   . GLY A 1 37  ? 9.40177  1.65532   0.79109  1.000 35.04008 ? 416 GLY A N   1 
ATOM   298  C  CA  . GLY A 1 37  ? 8.71180  2.15873   1.95559  1.000 33.42676 ? 416 GLY A CA  1 
ATOM   299  C  C   . GLY A 1 37  ? 8.35584  3.62372   1.79208  1.000 32.27490 ? 416 GLY A C   1 
ATOM   300  O  O   . GLY A 1 37  ? 8.17885  4.12659   0.68841  1.000 32.36686 ? 416 GLY A O   1 
ATOM   301  N  N   . ASP A 1 38  ? 8.23564  4.29729   2.92904  1.000 29.98389 ? 417 ASP A N   1 
ATOM   302  C  CA  . ASP A 1 38  ? 7.99733  5.73430   2.97975  1.000 28.76804 ? 417 ASP A CA  1 
ATOM   303  C  C   . ASP A 1 38  ? 8.65293  6.24876   4.25080  1.000 25.98431 ? 417 ASP A C   1 
ATOM   304  O  O   . ASP A 1 38  ? 9.10374  5.46982   5.09307  1.000 26.53270 ? 417 ASP A O   1 
ATOM   305  C  CB  . ASP A 1 38  ? 6.49192  6.06107   2.96876  1.000 27.91832 ? 417 ASP A CB  1 
ATOM   306  C  CG  . ASP A 1 38  ? 6.16530  7.41482   2.31642  1.000 30.59687 ? 417 ASP A CG  1 
ATOM   307  O  OD1 . ASP A 1 38  ? 6.90191  8.40453   2.53458  1.000 26.80021 ? 417 ASP A OD1 1 
ATOM   308  O  OD2 . ASP A 1 38  ? 5.14834  7.48820   1.58385  1.000 31.33776 ? 417 ASP A OD2 1 
ATOM   309  N  N   . LEU A 1 39  ? 8.69147  7.57020   4.39957  1.000 24.34732 ? 418 LEU A N   1 
ATOM   310  C  CA  . LEU A 1 39  ? 9.12368  8.13909   5.66816  1.000 22.62982 ? 418 LEU A CA  1 
ATOM   311  C  C   . LEU A 1 39  ? 8.23290  7.66112   6.81091  1.000 24.26310 ? 418 LEU A C   1 
ATOM   312  O  O   . LEU A 1 39  ? 7.03507  7.40276   6.63796  1.000 24.50320 ? 418 LEU A O   1 
ATOM   313  C  CB  . LEU A 1 39  ? 9.10469  9.66833   5.60503  1.000 24.62869 ? 418 LEU A CB  1 
ATOM   314  C  CG  . LEU A 1 39  ? 10.26413 10.32116  4.87713  1.000 24.88595 ? 418 LEU A CG  1 
ATOM   315  C  CD1 . LEU A 1 39  ? 10.04964 11.83504  4.76149  1.000 23.66604 ? 418 LEU A CD1 1 
ATOM   316  C  CD2 . LEU A 1 39  ? 11.54948 10.02861  5.62265  1.000 24.08551 ? 418 LEU A CD2 1 
ATOM   317  N  N   . LEU A 1 40  ? 8.83101  7.59938   7.99858  1.000 21.48683 ? 419 LEU A N   1 
ATOM   318  C  CA  . LEU A 1 40  ? 8.17880  7.05635   9.18011  1.000 22.63405 ? 419 LEU A CA  1 
ATOM   319  C  C   . LEU A 1 40  ? 6.89299  7.80387   9.52676  1.000 21.52637 ? 419 LEU A C   1 
ATOM   320  O  O   . LEU A 1 40  ? 6.86421  9.03634   9.56349  1.000 21.20641 ? 419 LEU A O   1 
ATOM   321  C  CB  . LEU A 1 40  ? 9.14951  7.13497   10.35415 1.000 21.76362 ? 419 LEU A CB  1 
ATOM   322  C  CG  . LEU A 1 40  ? 8.57668  6.86292   11.73820 1.000 21.24201 ? 419 LEU A CG  1 
ATOM   323  C  CD1 . LEU A 1 40  ? 8.18790  5.40697   11.82244 1.000 19.95113 ? 419 LEU A CD1 1 
ATOM   324  C  CD2 . LEU A 1 40  ? 9.62188  7.19671   12.77710 1.000 24.11286 ? 419 LEU A CD2 1 
ATOM   325  N  N   . SER A 1 41  ? 5.82419  7.05567   9.78970  1.000 20.62056 ? 420 SER A N   1 
ATOM   326  C  CA  . SER A 1 41  ? 4.66266  7.59746   10.47758 1.000 19.61315 ? 420 SER A CA  1 
ATOM   327  C  C   . SER A 1 41  ? 4.54190  6.93359   11.84419 1.000 22.82472 ? 420 SER A C   1 
ATOM   328  O  O   . SER A 1 41  ? 4.97957  5.79328   12.03821 1.000 22.68391 ? 420 SER A O   1 
ATOM   329  C  CB  . SER A 1 41  ? 3.37695  7.40837   9.65792  1.000 23.26338 ? 420 SER A CB  1 
ATOM   330  O  OG  . SER A 1 41  ? 3.13382  6.04481   9.35555  1.000 22.58776 ? 420 SER A OG  1 
ATOM   331  N  N   . ILE A 1 42  ? 3.96363  7.66526   12.79759 1.000 21.64585 ? 421 ILE A N   1 
ATOM   332  C  CA  . ILE A 1 42  ? 3.94314  7.28108   14.20790 1.000 19.48158 ? 421 ILE A CA  1 
ATOM   333  C  C   . ILE A 1 42  ? 2.51249  7.43247   14.69796 1.000 22.46323 ? 421 ILE A C   1 
ATOM   334  O  O   . ILE A 1 42  ? 1.97315  8.54265   14.69786 1.000 22.53514 ? 421 ILE A O   1 
ATOM   335  C  CB  . ILE A 1 42  ? 4.89214  8.14567   15.05974 1.000 21.55095 ? 421 ILE A CB  1 
ATOM   336  C  CG1 . ILE A 1 42  ? 6.31852  8.09663   14.50091 1.000 19.72631 ? 421 ILE A CG1 1 
ATOM   337  C  CG2 . ILE A 1 42  ? 4.90058  7.66997   16.50317 1.000 21.78478 ? 421 ILE A CG2 1 
ATOM   338  C  CD1 . ILE A 1 42  ? 7.26839  9.00842   15.26498 1.000 22.53087 ? 421 ILE A CD1 1 
ATOM   339  N  N   . HIS A 1 43  ? 1.89432  6.33043   15.11744 1.000 21.89538 ? 422 HIS A N   1 
ATOM   340  C  CA  . HIS A 1 43  ? 0.46481  6.35654   15.39995 1.000 21.42111 ? 422 HIS A CA  1 
ATOM   341  C  C   . HIS A 1 43  ? 0.12372  6.04323   16.84447 1.000 22.92093 ? 422 HIS A C   1 
ATOM   342  O  O   . HIS A 1 43  ? -1.06386 5.93426   17.17202 1.000 23.23202 ? 422 HIS A O   1 
ATOM   343  C  CB  . HIS A 1 43  ? -0.25801 5.39114   14.46321 1.000 24.35106 ? 422 HIS A CB  1 
ATOM   344  C  CG  . HIS A 1 43  ? -0.11089 5.74717   13.01806 1.000 24.55406 ? 422 HIS A CG  1 
ATOM   345  N  ND1 . HIS A 1 43  ? 0.36394  4.86187   12.07491 1.000 26.23656 ? 422 HIS A ND1 1 
ATOM   346  C  CD2 . HIS A 1 43  ? -0.37853 6.89571   12.35586 1.000 24.25473 ? 422 HIS A CD2 1 
ATOM   347  C  CE1 . HIS A 1 43  ? 0.38973  5.45357   10.89377 1.000 25.51809 ? 422 HIS A CE1 1 
ATOM   348  N  NE2 . HIS A 1 43  ? -0.05794 6.68830   11.03694 1.000 25.59343 ? 422 HIS A NE2 1 
ATOM   349  N  N   . SER A 1 44  ? 1.11776  5.89475   17.71344 1.000 21.96082 ? 423 SER A N   1 
ATOM   350  C  CA  . SER A 1 44  ? 0.85902  5.52977   19.09903 1.000 23.36240 ? 423 SER A CA  1 
ATOM   351  C  C   . SER A 1 44  ? 2.10918  5.81489   19.90951 1.000 24.26302 ? 423 SER A C   1 
ATOM   352  O  O   . SER A 1 44  ? 3.21393  5.84567   19.36451 1.000 24.59675 ? 423 SER A O   1 
ATOM   353  C  CB  . SER A 1 44  ? 0.46927  4.05083   19.23086 1.000 25.75152 ? 423 SER A CB  1 
ATOM   354  O  OG  . SER A 1 44  ? 1.58391  3.20533   18.97580 1.000 22.29279 ? 423 SER A OG  1 
ATOM   355  N  N   . MET A 1 45  ? 1.92054  6.02742   21.21518 1.000 24.21602 ? 424 MET A N   1 
ATOM   356  C  CA  . MET A 1 45  ? 3.06209  6.17940   22.11071 1.000 27.63057 ? 424 MET A CA  1 
ATOM   357  C  C   . MET A 1 45  ? 3.96049  4.94554   22.07395 1.000 26.96777 ? 424 MET A C   1 
ATOM   358  O  O   . MET A 1 45  ? 5.19062  5.05742   22.16840 1.000 25.76873 ? 424 MET A O   1 
ATOM   359  C  CB  . MET A 1 45  ? 2.57718  6.44838   23.53789 1.000 27.73655 ? 424 MET A CB  1 
ATOM   360  C  CG  . MET A 1 45  ? 3.70478  6.77402   24.53638 1.000 35.76730 ? 424 MET A CG  1 
ATOM   361  S  SD  . MET A 1 45  ? 4.47622  8.39765   24.27793 1.000 46.91621 ? 424 MET A SD  1 
ATOM   362  C  CE  . MET A 1 45  ? 3.12850  9.46930   24.77283 1.000 41.51740 ? 424 MET A CE  1 
ATOM   363  N  N   . ALA A 1 46  ? 3.36573  3.75799   21.94250 1.000 26.70122 ? 425 ALA A N   1 
ATOM   364  C  CA  . ALA A 1 46  ? 4.17137  2.53678   21.86800 1.000 24.57529 ? 425 ALA A CA  1 
ATOM   365  C  C   . ALA A 1 46  ? 5.10078  2.55646   20.65895 1.000 26.37692 ? 425 ALA A C   1 
ATOM   366  O  O   . ALA A 1 46  ? 6.27289  2.16271   20.75486 1.000 25.64609 ? 425 ALA A O   1 
ATOM   367  C  CB  . ALA A 1 46  ? 3.25817  1.31211   21.82038 1.000 28.64734 ? 425 ALA A CB  1 
ATOM   368  N  N   . GLU A 1 47  ? 4.59828  3.01062   19.50789 1.000 22.83189 ? 426 GLU A N   1 
ATOM   369  C  CA  . GLU A 1 47  ? 5.45030  3.10983   18.32806 1.000 23.73299 ? 426 GLU A CA  1 
ATOM   370  C  C   . GLU A 1 47  ? 6.48931  4.20684   18.50008 1.000 25.20630 ? 426 GLU A C   1 
ATOM   371  O  O   . GLU A 1 47  ? 7.62851  4.06651   18.04478 1.000 24.23297 ? 426 GLU A O   1 
ATOM   372  C  CB  . GLU A 1 47  ? 4.60196  3.36759   17.08571 1.000 24.39432 ? 426 GLU A CB  1 
ATOM   373  C  CG  . GLU A 1 47  ? 5.37601  3.34896   15.78993 1.000 23.50553 ? 426 GLU A CG  1 
ATOM   374  C  CD  . GLU A 1 47  ? 4.46552  3.37415   14.57125 1.000 26.82238 ? 426 GLU A CD  1 
ATOM   375  O  OE1 . GLU A 1 47  ? 3.27029  3.73220   14.72303 1.000 25.09561 ? 426 GLU A OE1 1 
ATOM   376  O  OE2 . GLU A 1 47  ? 4.94199  3.02083   13.46370 1.000 25.36631 ? 426 GLU A OE2 1 
ATOM   377  N  N   . LEU A 1 48  ? 6.11715  5.30892   19.15413 1.000 23.44446 ? 427 LEU A N   1 
ATOM   378  C  CA  . LEU A 1 48  ? 7.10028  6.35627   19.40883 1.000 25.35582 ? 427 LEU A CA  1 
ATOM   379  C  C   . LEU A 1 48  ? 8.24188  5.83442   20.27099 1.000 25.08913 ? 427 LEU A C   1 
ATOM   380  O  O   . LEU A 1 48  ? 9.41634  6.10045   19.99029 1.000 24.15554 ? 427 LEU A O   1 
ATOM   381  C  CB  . LEU A 1 48  ? 6.43681  7.55058   20.08161 1.000 25.51949 ? 427 LEU A CB  1 
ATOM   382  C  CG  . LEU A 1 48  ? 7.47218  8.57929   20.53331 1.000 27.95595 ? 427 LEU A CG  1 
ATOM   383  C  CD1 . LEU A 1 48  ? 8.09904  9.25751   19.32565 1.000 25.55078 ? 427 LEU A CD1 1 
ATOM   384  C  CD2 . LEU A 1 48  ? 6.80392  9.56014   21.43411 1.000 29.61489 ? 427 LEU A CD2 1 
ATOM   385  N  N   . GLU A 1 49  ? 7.91568  5.08082   21.32317 1.000 24.48125 ? 428 GLU A N   1 
ATOM   386  C  CA  . GLU A 1 49  ? 8.95040  4.58385   22.22009 1.000 28.79472 ? 428 GLU A CA  1 
ATOM   387  C  C   . GLU A 1 49  ? 9.82970  3.53895   21.54468 1.000 28.07917 ? 428 GLU A C   1 
ATOM   388  O  O   . GLU A 1 49  ? 11.03217 3.47787   21.82034 1.000 27.60223 ? 428 GLU A O   1 
ATOM   389  C  CB  . GLU A 1 49  ? 8.31823  4.02723   23.49405 1.000 34.07310 ? 428 GLU A CB  1 
ATOM   390  C  CG  . GLU A 1 49  ? 7.69292  5.11451   24.36657 1.000 39.77353 ? 428 GLU A CG  1 
ATOM   391  C  CD  . GLU A 1 49  ? 7.08959  4.57760   25.65801 1.000 52.49495 ? 428 GLU A CD  1 
ATOM   392  O  OE1 . GLU A 1 49  ? 6.84326  3.35279   25.74110 1.000 52.76029 ? 428 GLU A OE1 1 
ATOM   393  O  OE2 . GLU A 1 49  ? 6.86716  5.38584   26.59106 1.000 55.12093 ? 428 GLU A OE2 1 
ATOM   394  N  N   . PHE A 1 50  ? 9.26753  2.71641   20.65944 1.000 24.34715 ? 429 PHE A N   1 
ATOM   395  C  CA  . PHE A 1 50  ? 10.11189 1.81734   19.87565 1.000 27.93768 ? 429 PHE A CA  1 
ATOM   396  C  C   . PHE A 1 50  ? 11.10030 2.61444   19.03780 1.000 27.57896 ? 429 PHE A C   1 
ATOM   397  O  O   . PHE A 1 50  ? 12.29986 2.30240   18.99185 1.000 24.52102 ? 429 PHE A O   1 
ATOM   398  C  CB  . PHE A 1 50  ? 9.25346  0.92048   18.97753 1.000 26.14009 ? 429 PHE A CB  1 
ATOM   399  C  CG  . PHE A 1 50  ? 10.06173 0.12525   17.98687 1.000 27.40311 ? 429 PHE A CG  1 
ATOM   400  C  CD1 . PHE A 1 50  ? 10.76732 -0.99048  18.39726 1.000 26.23602 ? 429 PHE A CD1 1 
ATOM   401  C  CD2 . PHE A 1 50  ? 10.13482 0.51022   16.65678 1.000 27.30624 ? 429 PHE A CD2 1 
ATOM   402  C  CE1 . PHE A 1 50  ? 11.53065 -1.72821  17.50161 1.000 28.31866 ? 429 PHE A CE1 1 
ATOM   403  C  CE2 . PHE A 1 50  ? 10.89545 -0.22165  15.75364 1.000 25.50714 ? 429 PHE A CE2 1 
ATOM   404  C  CZ  . PHE A 1 50  ? 11.59119 -1.34196  16.17945 1.000 28.00641 ? 429 PHE A CZ  1 
ATOM   405  N  N   . ILE A 1 51  ? 10.60438 3.66788   18.38581 1.000 23.96395 ? 430 ILE A N   1 
ATOM   406  C  CA  . ILE A 1 51  ? 11.43296 4.48913   17.50477 1.000 26.12552 ? 430 ILE A CA  1 
ATOM   407  C  C   . ILE A 1 51  ? 12.58276 5.11217   18.28042 1.000 27.50546 ? 430 ILE A C   1 
ATOM   408  O  O   . ILE A 1 51  ? 13.75238 4.99509   17.90022 1.000 26.76867 ? 430 ILE A O   1 
ATOM   409  C  CB  . ILE A 1 51  ? 10.57201 5.57456   16.82538 1.000 25.87935 ? 430 ILE A CB  1 
ATOM   410  C  CG1 . ILE A 1 51  ? 9.61611  4.95076   15.81213 1.000 26.45954 ? 430 ILE A CG1 1 
ATOM   411  C  CG2 . ILE A 1 51  ? 11.44402 6.63167   16.18021 1.000 30.74203 ? 430 ILE A CG2 1 
ATOM   412  C  CD1 . ILE A 1 51  ? 10.25952 3.99588   14.86306 1.000 24.97363 ? 430 ILE A CD1 1 
ATOM   413  N  N   . THR A 1 52  ? 12.26714 5.80564   19.37051 1.000 27.14259 ? 431 THR A N   1 
ATOM   414  C  CA  . THR A 1 52  ? 13.31529 6.48749   20.11589 1.000 29.64069 ? 431 THR A CA  1 
ATOM   415  C  C   . THR A 1 52  ? 14.28105 5.48855   20.74431 1.000 28.32022 ? 431 THR A C   1 
ATOM   416  O  O   . THR A 1 52  ? 15.49764 5.70609   20.73634 1.000 29.88139 ? 431 THR A O   1 
ATOM   417  C  CB  . THR A 1 52  ? 12.69235 7.40592   21.17045 1.000 29.60950 ? 431 THR A CB  1 
ATOM   418  O  OG1 . THR A 1 52  ? 12.10287 6.61375   22.20640 1.000 32.04858 ? 431 THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 52  ? 11.61144 8.26297   20.53827 1.000 27.87050 ? 431 THR A CG2 1 
ATOM   420  N  N   . LYS A 1 53  ? 13.77111 4.35915   21.24180 1.000 26.47533 ? 432 LYS A N   1 
ATOM   421  C  CA  . LYS A 1 53  ? 14.61524 3.43589   21.98672 1.000 31.72015 ? 432 LYS A CA  1 
ATOM   422  C  C   . LYS A 1 53  ? 15.47979 2.55585   21.09267 1.000 32.90189 ? 432 LYS A C   1 
ATOM   423  O  O   . LYS A 1 53  ? 16.60652 2.22558   21.47047 1.000 34.62233 ? 432 LYS A O   1 
ATOM   424  C  CB  . LYS A 1 53  ? 13.76856 2.53644   22.88615 1.000 34.79728 ? 432 LYS A CB  1 
ATOM   425  C  CG  . LYS A 1 53  ? 13.76334 2.94464   24.34342 1.000 41.48041 ? 432 LYS A CG  1 
ATOM   426  C  CD  . LYS A 1 53  ? 13.86959 1.72441   25.26278 1.000 44.75393 ? 432 LYS A CD  1 
ATOM   427  C  CE  . LYS A 1 53  ? 15.23501 1.03954   25.14737 1.000 48.95572 ? 432 LYS A CE  1 
ATOM   428  N  NZ  . LYS A 1 53  ? 15.46833 0.03951   26.23300 1.000 50.47798 ? 432 LYS A NZ  1 
ATOM   429  N  N   . GLN A 1 54  ? 14.97873 2.14427   19.93457 1.000 30.56935 ? 433 GLN A N   1 
ATOM   430  C  CA  . GLN A 1 54  ? 15.65992 1.13982   19.13497 1.000 31.65337 ? 433 GLN A CA  1 
ATOM   431  C  C   . GLN A 1 54  ? 16.14391 1.62544   17.78207 1.000 31.14732 ? 433 GLN A C   1 
ATOM   432  O  O   . GLN A 1 54  ? 17.07761 1.03212   17.23905 1.000 28.61799 ? 433 GLN A O   1 
ATOM   433  C  CB  . GLN A 1 54  ? 14.74540 -0.07646  18.91628 1.000 30.86581 ? 433 GLN A CB  1 
ATOM   434  C  CG  . GLN A 1 54  ? 14.56007 -0.92293  20.14956 1.000 34.83777 ? 433 GLN A CG  1 
ATOM   435  C  CD  . GLN A 1 54  ? 15.81670 -1.66787  20.51782 1.000 38.27324 ? 433 GLN A CD  1 
ATOM   436  O  OE1 . GLN A 1 54  ? 16.52180 -2.18649  19.64845 1.000 40.33097 ? 433 GLN A OE1 1 
ATOM   437  N  NE2 . GLN A 1 54  ? 16.11489 -1.72391  21.81167 1.000 39.13041 ? 433 GLN A NE2 1 
ATOM   438  N  N   . ILE A 1 55  ? 15.54366 2.66821   17.21965 1.000 28.75546 ? 434 ILE A N   1 
ATOM   439  C  CA  . ILE A 1 55  ? 15.86867 3.07314   15.85940 1.000 27.18278 ? 434 ILE A CA  1 
ATOM   440  C  C   . ILE A 1 55  ? 16.66526 4.36741   15.89448 1.000 29.21893 ? 434 ILE A C   1 
ATOM   441  O  O   . ILE A 1 55  ? 17.78142 4.43573   15.36775 1.000 29.45508 ? 434 ILE A O   1 
ATOM   442  C  CB  . ILE A 1 55  ? 14.60151 3.22166   14.99946 1.000 27.39484 ? 434 ILE A CB  1 
ATOM   443  C  CG1 . ILE A 1 55  ? 13.79538 1.92199   15.01257 1.000 26.10886 ? 434 ILE A CG1 1 
ATOM   444  C  CG2 . ILE A 1 55  ? 14.98808 3.54390   13.57791 1.000 29.37506 ? 434 ILE A CG2 1 
ATOM   445  C  CD1 . ILE A 1 55  ? 14.49429 0.76287   14.35284 1.000 28.74481 ? 434 ILE A CD1 1 
ATOM   446  N  N   . LYS A 1 56  ? 16.10891 5.39474   16.53150 1.000 27.10607 ? 435 LYS A N   1 
ATOM   447  C  CA  . LYS A 1 56  ? 16.80352 6.67912   16.62027 1.000 28.95250 ? 435 LYS A CA  1 
ATOM   448  C  C   . LYS A 1 56  ? 18.02289 6.58344   17.52363 1.000 31.51576 ? 435 LYS A C   1 
ATOM   449  O  O   . LYS A 1 56  ? 19.12972 6.98859   17.13902 1.000 28.70066 ? 435 LYS A O   1 
ATOM   450  C  CB  . LYS A 1 56  ? 15.83680 7.75312   17.11656 1.000 28.05389 ? 435 LYS A CB  1 
ATOM   451  C  CG  . LYS A 1 56  ? 16.47111 9.03455   17.66730 1.000 26.97524 ? 435 LYS A CG  1 
ATOM   452  C  CD  . LYS A 1 56  ? 15.34924 9.97278   18.16250 1.000 27.09400 ? 435 LYS A CD  1 
ATOM   453  C  CE  . LYS A 1 56  ? 15.87004 11.35969  18.58668 1.000 29.86708 ? 435 LYS A CE  1 
ATOM   454  N  NZ  . LYS A 1 56  ? 16.88603 11.22526  19.67135 1.000 30.42224 ? 435 LYS A NZ  1 
ATOM   455  N  N   . GLN A 1 57  ? 17.82997 6.07209   18.73666 1.000 29.97197 ? 436 GLN A N   1 
ATOM   456  C  CA  . GLN A 1 57  ? 18.90406 5.86374   19.70765 1.000 32.34951 ? 436 GLN A CA  1 
ATOM   457  C  C   . GLN A 1 57  ? 19.65102 7.18519   19.90035 1.000 32.43718 ? 436 GLN A C   1 
ATOM   458  O  O   . GLN A 1 57  ? 19.01080 8.21133   20.16409 1.000 33.43247 ? 436 GLN A O   1 
ATOM   459  C  CB  . GLN A 1 57  ? 19.76276 4.69999   19.25106 1.000 32.95759 ? 436 GLN A CB  1 
ATOM   460  C  CG  . GLN A 1 57  ? 18.99108 3.41356   19.07858 1.000 34.00287 ? 436 GLN A CG  1 
ATOM   461  C  CD  . GLN A 1 57  ? 19.87876 2.19596   19.17239 1.000 38.66712 ? 436 GLN A CD  1 
ATOM   462  O  OE1 . GLN A 1 57  ? 20.92738 2.12311   18.53619 1.000 41.09344 ? 436 GLN A OE1 1 
ATOM   463  N  NE2 . GLN A 1 57  ? 19.46675 1.23212   19.98661 1.000 40.06298 ? 436 GLN A NE2 1 
ATOM   464  N  N   . GLU A 1 58  ? 20.97909 7.21249   19.75180 1.000 31.67846 ? 437 GLU A N   1 
ATOM   465  C  CA  . GLU A 1 58  ? 21.73816 8.40654   20.08718 1.000 32.85695 ? 437 GLU A CA  1 
ATOM   466  C  C   . GLU A 1 58  ? 21.61616 9.51024   19.04688 1.000 33.10459 ? 437 GLU A C   1 
ATOM   467  O  O   . GLU A 1 58  ? 22.09421 10.61619  19.30519 1.000 33.66435 ? 437 GLU A O   1 
ATOM   468  C  CB  . GLU A 1 58  ? 23.20914 8.05010   20.28675 1.000 33.65599 ? 437 GLU A CB  1 
ATOM   469  C  CG  . GLU A 1 58  ? 24.04969 8.03158   19.00426 1.000 36.64857 ? 437 GLU A CG  1 
ATOM   470  C  CD  . GLU A 1 58  ? 23.68692 6.90050   18.04032 1.000 42.29128 ? 437 GLU A CD  1 
ATOM   471  O  OE1 . GLU A 1 58  ? 22.91827 5.98622   18.42616 1.000 37.10214 ? 437 GLU A OE1 1 
ATOM   472  O  OE2 . GLU A 1 58  ? 24.17127 6.93741   16.88358 1.000 39.04321 ? 437 GLU A OE2 1 
ATOM   473  N  N   . VAL A 1 59  ? 21.01952 9.24485   17.88274 1.000 28.72622 ? 438 VAL A N   1 
ATOM   474  C  CA  . VAL A 1 59  ? 20.91281 10.28333  16.86660 1.000 32.13429 ? 438 VAL A CA  1 
ATOM   475  C  C   . VAL A 1 59  ? 20.01765 11.38310  17.40270 1.000 32.11425 ? 438 VAL A C   1 
ATOM   476  O  O   . VAL A 1 59  ? 18.95706 11.10866  17.97198 1.000 29.89492 ? 438 VAL A O   1 
ATOM   477  C  CB  . VAL A 1 59  ? 20.36485 9.70839   15.55352 1.000 32.10322 ? 438 VAL A CB  1 
ATOM   478  C  CG1 . VAL A 1 59  ? 20.10293 10.83859  14.55030 1.000 32.61261 ? 438 VAL A CG1 1 
ATOM   479  C  CG2 . VAL A 1 59  ? 21.32661 8.69356   14.98019 1.000 36.12438 ? 438 VAL A CG2 1 
ATOM   480  N  N   . GLU A 1 60  ? 20.44355 12.63503  17.24049 1.000 29.87735 ? 439 GLU A N   1 
ATOM   481  C  CA  . GLU A 1 60  ? 19.75615 13.70852  17.94484 1.000 31.93490 ? 439 GLU A CA  1 
ATOM   482  C  C   . GLU A 1 60  ? 18.51867 14.18579  17.19771 1.000 30.24340 ? 439 GLU A C   1 
ATOM   483  O  O   . GLU A 1 60  ? 17.51228 14.51311  17.82880 1.000 31.64884 ? 439 GLU A O   1 
ATOM   484  C  CB  . GLU A 1 60  ? 20.70871 14.86940  18.19801 1.000 35.47557 ? 439 GLU A CB  1 
ATOM   485  C  CG  . GLU A 1 60  ? 20.03108 16.11652  18.75577 1.000 39.99945 ? 439 GLU A CG  1 
ATOM   486  C  CD  . GLU A 1 60  ? 19.64307 15.98378  20.21910 1.000 42.30403 ? 439 GLU A CD  1 
ATOM   487  O  OE1 . GLU A 1 60  ? 20.04855 14.98765  20.86714 1.000 38.19614 ? 439 GLU A OE1 1 
ATOM   488  O  OE2 . GLU A 1 60  ? 18.93455 16.88848  20.71817 1.000 41.97571 ? 439 GLU A OE2 1 
ATOM   489  N  N   . GLU A 1 61  ? 18.56634 14.23557  15.86863 1.000 29.59348 ? 440 GLU A N   1 
ATOM   490  C  CA  . GLU A 1 61  ? 17.50173 14.86570  15.09164 1.000 29.26854 ? 440 GLU A CA  1 
ATOM   491  C  C   . GLU A 1 61  ? 17.39761 14.17057  13.74150 1.000 28.77131 ? 440 GLU A C   1 
ATOM   492  O  O   . GLU A 1 61  ? 18.41944 13.95956  13.08071 1.000 27.10830 ? 440 GLU A O   1 
ATOM   493  C  CB  . GLU A 1 61  ? 17.78957 16.36442  14.91071 1.000 30.74046 ? 440 GLU A CB  1 
ATOM   494  C  CG  . GLU A 1 61  ? 16.72264 17.14084  14.13164 1.000 31.26662 ? 440 GLU A CG  1 
ATOM   495  C  CD  . GLU A 1 61  ? 16.95922 18.64612  14.14041 1.000 39.17868 ? 440 GLU A CD  1 
ATOM   496  O  OE1 . GLU A 1 61  ? 18.11451 19.07266  14.35534 1.000 38.87807 ? 440 GLU A OE1 1 
ATOM   497  O  OE2 . GLU A 1 61  ? 15.97829 19.39847  13.93925 1.000 51.11259 ? 440 GLU A OE2 1 
ATOM   498  N  N   . LEU A 1 62  ? 16.18021 13.80395  13.33571 1.000 23.54241 ? 441 LEU A N   1 
ATOM   499  C  CA  . LEU A 1 62  ? 16.01298 13.14616  12.04700 1.000 25.42773 ? 441 LEU A CA  1 
ATOM   500  C  C   . LEU A 1 62  ? 14.63070 13.43782  11.48684 1.000 23.13989 ? 441 LEU A C   1 
ATOM   501  O  O   . LEU A 1 62  ? 13.71346 13.83370  12.21455 1.000 23.31403 ? 441 LEU A O   1 
ATOM   502  C  CB  . LEU A 1 62  ? 16.25003 11.63350  12.15168 1.000 27.40715 ? 441 LEU A CB  1 
ATOM   503  C  CG  . LEU A 1 62  ? 15.47744 10.85558  13.20918 1.000 24.78708 ? 441 LEU A CG  1 
ATOM   504  C  CD1 . LEU A 1 62  ? 14.09862 10.47284  12.70574 1.000 25.85665 ? 441 LEU A CD1 1 
ATOM   505  C  CD2 . LEU A 1 62  ? 16.26985 9.61569   13.58801 1.000 28.88857 ? 441 LEU A CD2 1 
ATOM   506  N  N   . TRP A 1 63  ? 14.49217 13.24610  10.17495 1.000 23.47902 ? 442 TRP A N   1 
ATOM   507  C  CA  . TRP A 1 63  ? 13.20930 13.47922  9.50081  1.000 20.55490 ? 442 TRP A CA  1 
ATOM   508  C  C   . TRP A 1 63  ? 12.23214 12.34782  9.76447  1.000 23.36723 ? 442 TRP A C   1 
ATOM   509  O  O   . TRP A 1 63  ? 12.61281 11.17463  9.75328  1.000 22.39127 ? 442 TRP A O   1 
ATOM   510  C  CB  . TRP A 1 63  ? 13.39000 13.57264  7.98384  1.000 21.59652 ? 442 TRP A CB  1 
ATOM   511  C  CG  . TRP A 1 63  ? 14.14475 14.76077  7.46270  1.000 24.76343 ? 442 TRP A CG  1 
ATOM   512  C  CD1 . TRP A 1 63  ? 15.29218 14.74924  6.71648  1.000 25.55256 ? 442 TRP A CD1 1 
ATOM   513  C  CD2 . TRP A 1 63  ? 13.77818 16.13376  7.61018  1.000 26.74330 ? 442 TRP A CD2 1 
ATOM   514  N  NE1 . TRP A 1 63  ? 15.66310 16.03202  6.40563  1.000 26.82412 ? 442 TRP A NE1 1 
ATOM   515  C  CE2 . TRP A 1 63  ? 14.75787 16.90140  6.94957  1.000 27.07410 ? 442 TRP A CE2 1 
ATOM   516  C  CE3 . TRP A 1 63  ? 12.73097 16.78866  8.25578  1.000 24.77532 ? 442 TRP A CE3 1 
ATOM   517  C  CZ2 . TRP A 1 63  ? 14.71550 18.28988  6.91296  1.000 28.65453 ? 442 TRP A CZ2 1 
ATOM   518  C  CZ3 . TRP A 1 63  ? 12.69126 18.17016  8.21849  1.000 27.30621 ? 442 TRP A CZ3 1 
ATOM   519  C  CH2 . TRP A 1 63  ? 13.67168 18.90214  7.55089  1.000 29.37053 ? 442 TRP A CH2 1 
ATOM   520  N  N   . ILE A 1 64  ? 10.95140 12.69957  9.94154  1.000 21.69318 ? 443 ILE A N   1 
ATOM   521  C  CA  . ILE A 1 64  ? 9.86318  11.72887  9.84625  1.000 21.98793 ? 443 ILE A CA  1 
ATOM   522  C  C   . ILE A 1 64  ? 8.88460  12.23009  8.78565  1.000 20.76147 ? 443 ILE A C   1 
ATOM   523  O  O   . ILE A 1 64  ? 9.11717  13.26828  8.15901  1.000 21.17165 ? 443 ILE A O   1 
ATOM   524  C  CB  . ILE A 1 64  ? 9.17021  11.49165  11.20302 1.000 21.29316 ? 443 ILE A CB  1 
ATOM   525  C  CG1 . ILE A 1 64  ? 8.55187  12.77917  11.74716 1.000 21.09196 ? 443 ILE A CG1 1 
ATOM   526  C  CG2 . ILE A 1 64  ? 10.16362 10.91101  12.20980 1.000 22.21395 ? 443 ILE A CG2 1 
ATOM   527  C  CD1 . ILE A 1 64  ? 7.76804  12.57190  13.03586 1.000 21.06734 ? 443 ILE A CD1 1 
ATOM   528  N  N   . GLY A 1 65  ? 7.79459  11.50067  8.56180  1.000 20.33302 ? 444 GLY A N   1 
ATOM   529  C  CA  . GLY A 1 65  ? 6.95608  11.76828  7.40814  1.000 20.88664 ? 444 GLY A CA  1 
ATOM   530  C  C   . GLY A 1 65  ? 5.92537  12.86157  7.54433  1.000 22.41758 ? 444 GLY A C   1 
ATOM   531  O  O   . GLY A 1 65  ? 5.20391  13.14508  6.58228  1.000 23.66870 ? 444 GLY A O   1 
ATOM   532  N  N   . LEU A 1 66  ? 5.81545  13.48327  8.70836  1.000 22.51424 ? 445 LEU A N   1 
ATOM   533  C  CA  . LEU A 1 66  ? 4.79082  14.49363  8.92273  1.000 21.29120 ? 445 LEU A CA  1 
ATOM   534  C  C   . LEU A 1 66  ? 5.19242  15.79326  8.23430  1.000 23.33281 ? 445 LEU A C   1 
ATOM   535  O  O   . LEU A 1 66  ? 6.36671  16.17474  8.22213  1.000 22.54710 ? 445 LEU A O   1 
ATOM   536  C  CB  . LEU A 1 66  ? 4.58412  14.71548  10.42019 1.000 22.11057 ? 445 LEU A CB  1 
ATOM   537  C  CG  . LEU A 1 66  ? 3.29659  15.39890  10.85934 1.000 22.16904 ? 445 LEU A CG  1 
ATOM   538  C  CD1 . LEU A 1 66  ? 2.10505  14.50141  10.53103 1.000 23.24101 ? 445 LEU A CD1 1 
ATOM   539  C  CD2 . LEU A 1 66  ? 3.36072  15.68823  12.34213 1.000 23.56751 ? 445 LEU A CD2 1 
ATOM   540  N  N   . ASN A 1 67  ? 4.21619  16.47007  7.64548  1.000 22.34314 ? 446 ASN A N   1 
ATOM   541  C  CA  . ASN A 1 67  ? 4.51233  17.66214  6.86637  1.000 24.76241 ? 446 ASN A CA  1 
ATOM   542  C  C   . ASN A 1 67  ? 3.21923  18.42732  6.63155  1.000 27.76419 ? 446 ASN A C   1 
ATOM   543  O  O   . ASN A 1 67  ? 2.13749  17.83084  6.58374  1.000 27.37856 ? 446 ASN A O   1 
ATOM   544  C  CB  . ASN A 1 67  ? 5.14727  17.30326  5.52197  1.000 24.92468 ? 446 ASN A CB  1 
ATOM   545  C  CG  . ASN A 1 67  ? 4.13314  16.75534  4.53620  1.000 28.86710 ? 446 ASN A CG  1 
ATOM   546  O  OD1 . ASN A 1 67  ? 3.53151  17.50600  3.76916  1.000 27.38908 ? 446 ASN A OD1 1 
ATOM   547  N  ND2 . ASN A 1 67  ? 3.91954  15.44347  4.56814  1.000 25.05597 ? 446 ASN A ND2 1 
ATOM   548  N  N   . ASP A 1 68  ? 3.33867  19.74314  6.48216  1.000 28.27332 ? 447 ASP A N   1 
ATOM   549  C  CA  . ASP A 1 68  ? 2.21386  20.56410  6.04984  1.000 28.48246 ? 447 ASP A CA  1 
ATOM   550  C  C   . ASP A 1 68  ? 2.53650  21.25842  4.72964  1.000 32.04211 ? 447 ASP A C   1 
ATOM   551  O  O   . ASP A 1 68  ? 2.17555  22.41351  4.49902  1.000 31.48798 ? 447 ASP A O   1 
ATOM   552  C  CB  . ASP A 1 68  ? 1.78522  21.54751  7.14344  1.000 27.75101 ? 447 ASP A CB  1 
ATOM   553  C  CG  . ASP A 1 68  ? 2.75514  22.70287  7.34221  1.000 32.43845 ? 447 ASP A CG  1 
ATOM   554  O  OD1 . ASP A 1 68  ? 3.93213  22.55117  6.99073  1.000 30.36883 ? 447 ASP A OD1 1 
ATOM   555  O  OD2 . ASP A 1 68  ? 2.32810  23.76241  7.85572  1.000 31.87719 ? 447 ASP A OD2 1 
ATOM   556  N  N   . LEU A 1 69  ? 3.20232  20.52716  3.82900  1.000 29.46613 ? 448 LEU A N   1 
ATOM   557  C  CA  . LEU A 1 69  ? 3.51572  21.06984  2.50947  1.000 32.24577 ? 448 LEU A CA  1 
ATOM   558  C  C   . LEU A 1 69  ? 2.25690  21.43281  1.73002  1.000 37.44446 ? 448 LEU A C   1 
ATOM   559  O  O   . LEU A 1 69  ? 2.21901  22.45345  1.03487  1.000 39.92824 ? 448 LEU A O   1 
ATOM   560  C  CB  . LEU A 1 69  ? 4.34840  20.06289  1.72251  1.000 34.16664 ? 448 LEU A CB  1 
ATOM   561  C  CG  . LEU A 1 69  ? 5.80500  19.98592  2.16245  1.000 33.45349 ? 448 LEU A CG  1 
ATOM   562  C  CD1 . LEU A 1 69  ? 6.47935  18.75775  1.58328  1.000 35.58625 ? 448 LEU A CD1 1 
ATOM   563  C  CD2 . LEU A 1 69  ? 6.53534  21.24523  1.72997  1.000 35.54846 ? 448 LEU A CD2 1 
ATOM   564  N  N   . LYS A 1 70  ? 1.21985  20.60405  1.81415  1.000 36.49206 ? 449 LYS A N   1 
ATOM   565  C  CA  . LYS A 1 70  ? 0.05082  20.85212  0.97932  1.000 39.36698 ? 449 LYS A CA  1 
ATOM   566  C  C   . LYS A 1 70  ? -0.81780 21.96676  1.54681  1.000 37.03649 ? 449 LYS A C   1 
ATOM   567  O  O   . LYS A 1 70  ? -1.32366 22.80428  0.79461  1.000 38.00770 ? 449 LYS A O   1 
ATOM   568  C  CB  . LYS A 1 70  ? -0.75520 19.56190  0.80769  1.000 40.10109 ? 449 LYS A CB  1 
ATOM   569  C  CG  . LYS A 1 70  ? 0.03400  18.43968  0.13608  1.000 43.89398 ? 449 LYS A CG  1 
ATOM   570  C  CD  . LYS A 1 70  ? 0.90100  19.01036  -0.97686 1.000 45.60057 ? 449 LYS A CD  1 
ATOM   571  C  CE  . LYS A 1 70  ? 1.73714  17.95408  -1.66397 1.000 46.00027 ? 449 LYS A CE  1 
ATOM   572  N  NZ  . LYS A 1 70  ? 2.24666  18.49874  -2.95284 1.000 47.31784 ? 449 LYS A NZ  1 
ATOM   573  N  N   . LEU A 1 71  ? -0.98000 22.01064  2.86580  1.000 36.30605 ? 450 LEU A N   1 
ATOM   574  C  CA  . LEU A 1 71  ? -1.91351 22.94243  3.49286  1.000 38.53182 ? 450 LEU A CA  1 
ATOM   575  C  C   . LEU A 1 71  ? -1.30257 23.41015  4.80759  1.000 37.84402 ? 450 LEU A C   1 
ATOM   576  O  O   . LEU A 1 71  ? -1.17424 22.61010  5.73621  1.000 35.83571 ? 450 LEU A O   1 
ATOM   577  C  CB  . LEU A 1 71  ? -3.25618 22.25934  3.71676  1.000 36.54655 ? 450 LEU A CB  1 
ATOM   578  C  CG  . LEU A 1 71  ? -4.46972 23.12407  3.98149  1.000 39.62210 ? 450 LEU A CG  1 
ATOM   579  C  CD1 . LEU A 1 71  ? -4.82815 23.90213  2.73411  1.000 38.35258 ? 450 LEU A CD1 1 
ATOM   580  C  CD2 . LEU A 1 71  ? -5.60982 22.22275  4.40063  1.000 41.79872 ? 450 LEU A CD2 1 
ATOM   581  N  N   . GLN A 1 72  ? -0.93549 24.69270  4.89296  1.000 36.23070 ? 451 GLN A N   1 
ATOM   582  C  CA  . GLN A 1 72  ? -0.21617 25.17954  6.06717  1.000 35.26263 ? 451 GLN A CA  1 
ATOM   583  C  C   . GLN A 1 72  ? -1.02031 24.96050  7.34022  1.000 37.15096 ? 451 GLN A C   1 
ATOM   584  O  O   . GLN A 1 72  ? -2.22113 25.23722  7.38801  1.000 33.35955 ? 451 GLN A O   1 
ATOM   585  C  CB  . GLN A 1 72  ? 0.10426  26.66666  5.92587  1.000 35.95687 ? 451 GLN A CB  1 
ATOM   586  C  CG  . GLN A 1 72  ? 1.27679  26.96753  5.03598  1.000 36.97816 ? 451 GLN A CG  1 
ATOM   587  C  CD  . GLN A 1 72  ? 2.59039  26.44107  5.59100  1.000 38.19839 ? 451 GLN A CD  1 
ATOM   588  O  OE1 . GLN A 1 72  ? 2.80218  26.39587  6.80510  1.000 37.79041 ? 451 GLN A OE1 1 
ATOM   589  N  NE2 . GLN A 1 72  ? 3.47968  26.03720  4.69664  1.000 41.31300 ? 451 GLN A NE2 1 
ATOM   590  N  N   . MET A 1 73  ? -0.33688 24.48114  8.37852  1.000 35.20501 ? 452 MET A N   1 
ATOM   591  C  CA  . MET A 1 73  ? -0.82444 24.19028  9.72189  1.000 36.41894 ? 452 MET A CA  1 
ATOM   592  C  C   . MET A 1 73  ? -1.65324 22.90086  9.78003  1.000 37.21130 ? 452 MET A C   1 
ATOM   593  O  O   . MET A 1 73  ? -2.04679 22.49349  10.87568 1.000 35.52724 ? 452 MET A O   1 
ATOM   594  C  CB  . MET A 1 73  ? -1.64462 25.34494  10.33325 1.000 39.57521 ? 452 MET A CB  1 
ATOM   595  C  CG  . MET A 1 73  ? -0.94981 26.69470  10.27516 1.000 46.65672 ? 452 MET A CG  1 
ATOM   596  S  SD  . MET A 1 73  ? -2.09788 28.08223  10.47233 1.000 65.03451 ? 452 MET A SD  1 
ATOM   597  C  CE  . MET A 1 73  ? -0.97886 29.46969  10.27099 1.000 54.40878 ? 452 MET A CE  1 
ATOM   598  N  N   . ASN A 1 74  ? -1.91975 22.23587  8.65588  1.000 36.21022 ? 453 ASN A N   1 
ATOM   599  C  CA  . ASN A 1 74  ? -2.60011 20.94393  8.64989  1.000 33.77212 ? 453 ASN A CA  1 
ATOM   600  C  C   . ASN A 1 74  ? -1.57556 19.88210  8.28176  1.000 32.54786 ? 453 ASN A C   1 
ATOM   601  O  O   . ASN A 1 74  ? -1.29345 19.65632  7.10325  1.000 33.92302 ? 453 ASN A O   1 
ATOM   602  C  CB  . ASN A 1 74  ? -3.77246 20.93895  7.68633  1.000 37.11053 ? 453 ASN A CB  1 
ATOM   603  C  CG  . ASN A 1 74  ? -4.93473 21.73261  8.20498  1.000 42.69822 ? 453 ASN A CG  1 
ATOM   604  O  OD1 . ASN A 1 74  ? -4.76933 22.85696  8.68026  1.000 44.52530 ? 453 ASN A OD1 1 
ATOM   605  N  ND2 . ASN A 1 74  ? -6.12154 21.14658  8.14417  1.000 43.65962 ? 453 ASN A ND2 1 
ATOM   606  N  N   . PHE A 1 75  ? -1.01238 19.24300  9.29378  1.000 28.45158 ? 454 PHE A N   1 
ATOM   607  C  CA  . PHE A 1 75  ? 0.02361  18.25215  9.05932  1.000 28.59562 ? 454 PHE A CA  1 
ATOM   608  C  C   . PHE A 1 75  ? -0.58925 16.90621  8.71271  1.000 28.89945 ? 454 PHE A C   1 
ATOM   609  O  O   . PHE A 1 75  ? -1.63480 16.52413  9.24410  1.000 28.68344 ? 454 PHE A O   1 
ATOM   610  C  CB  . PHE A 1 75  ? 0.93061  18.15171  10.28192 1.000 26.09891 ? 454 PHE A CB  1 
ATOM   611  C  CG  . PHE A 1 75  ? 1.87752  19.30660  10.39825 1.000 27.14928 ? 454 PHE A CG  1 
ATOM   612  C  CD1 . PHE A 1 75  ? 1.49532  20.47348  11.03213 1.000 31.82809 ? 454 PHE A CD1 1 
ATOM   613  C  CD2 . PHE A 1 75  ? 3.13709  19.24390  9.82441  1.000 27.31826 ? 454 PHE A CD2 1 
ATOM   614  C  CE1 . PHE A 1 75  ? 2.36048  21.54548  11.10742 1.000 30.08068 ? 454 PHE A CE1 1 
ATOM   615  C  CE2 . PHE A 1 75  ? 4.00793  20.31846  9.89935  1.000 25.52512 ? 454 PHE A CE2 1 
ATOM   616  C  CZ  . PHE A 1 75  ? 3.61921  21.46231  10.54334 1.000 27.30055 ? 454 PHE A CZ  1 
ATOM   617  N  N   . GLU A 1 76  ? 0.06160  16.20480  7.78826  1.000 27.79032 ? 455 GLU A N   1 
ATOM   618  C  CA  . GLU A 1 76  ? -0.35040 14.88623  7.35249  1.000 30.12901 ? 455 GLU A CA  1 
ATOM   619  C  C   . GLU A 1 76  ? 0.88595  14.01910  7.16558  1.000 25.38978 ? 455 GLU A C   1 
ATOM   620  O  O   . GLU A 1 76  ? 2.00606  14.51823  7.02132  1.000 24.89612 ? 455 GLU A O   1 
ATOM   621  C  CB  . GLU A 1 76  ? -1.16242 14.94669  6.05141  1.000 31.88967 ? 455 GLU A CB  1 
ATOM   622  C  CG  . GLU A 1 76  ? -2.64970 14.66591  6.24299  1.000 46.79797 ? 455 GLU A CG  1 
ATOM   623  C  CD  . GLU A 1 76  ? -2.93699 13.35021  6.98732  1.000 49.97209 ? 455 GLU A CD  1 
ATOM   624  O  OE1 . GLU A 1 76  ? -2.13344 12.36594  6.89963  1.000 32.73073 ? 455 GLU A OE1 1 
ATOM   625  O  OE2 . GLU A 1 76  ? -3.98727 13.31973  7.67047  1.000 49.45800 ? 455 GLU A OE2 1 
ATOM   626  N  N   . TRP A 1 77  ? 0.67571  12.70751  7.18235  1.000 25.08366 ? 456 TRP A N   1 
ATOM   627  C  CA  . TRP A 1 77  ? 1.77234  11.77750  6.94031  1.000 23.53789 ? 456 TRP A CA  1 
ATOM   628  C  C   . TRP A 1 77  ? 1.95331  11.58416  5.44504  1.000 24.25568 ? 456 TRP A C   1 
ATOM   629  O  O   . TRP A 1 77  ? 0.97751  11.42093  4.70722  1.000 20.98728 ? 456 TRP A O   1 
ATOM   630  C  CB  . TRP A 1 77  ? 1.50395  10.41971  7.59145  1.000 24.82523 ? 456 TRP A CB  1 
ATOM   631  C  CG  . TRP A 1 77  ? 1.43710  10.45313  9.06675  1.000 23.78091 ? 456 TRP A CG  1 
ATOM   632  C  CD1 . TRP A 1 77  ? 0.33321  10.25005  9.84105  1.000 22.81290 ? 456 TRP A CD1 1 
ATOM   633  C  CD2 . TRP A 1 77  ? 2.51866  10.70811  9.96027  1.000 21.29485 ? 456 TRP A CD2 1 
ATOM   634  N  NE1 . TRP A 1 77  ? 0.66381  10.36268  11.16758 1.000 24.31138 ? 456 TRP A NE1 1 
ATOM   635  C  CE2 . TRP A 1 77  ? 2.00390  10.63758  11.26706 1.000 21.21979 ? 456 TRP A CE2 1 
ATOM   636  C  CE3 . TRP A 1 77  ? 3.88120  10.98217  9.78151  1.000 21.63020 ? 456 TRP A CE3 1 
ATOM   637  C  CZ2 . TRP A 1 77  ? 2.79357  10.84673  12.39030 1.000 22.29555 ? 456 TRP A CZ2 1 
ATOM   638  C  CZ3 . TRP A 1 77  ? 4.66703  11.18087  10.89665 1.000 21.30077 ? 456 TRP A CZ3 1 
ATOM   639  C  CH2 . TRP A 1 77  ? 4.12543  11.11695  12.18576 1.000 21.91562 ? 456 TRP A CH2 1 
ATOM   640  N  N   . SER A 1 78  ? 3.21038  11.58545  4.99881  1.000 22.10651 ? 457 SER A N   1 
ATOM   641  C  CA  . SER A 1 78  ? 3.47026  11.39377  3.57663  1.000 23.00395 ? 457 SER A CA  1 
ATOM   642  C  C   . SER A 1 78  ? 2.93101  10.06058  3.08750  1.000 25.39895 ? 457 SER A C   1 
ATOM   643  O  O   . SER A 1 78  ? 2.57772  9.93293   1.91083  1.000 24.67325 ? 457 SER A O   1 
ATOM   644  C  CB  . SER A 1 78  ? 4.97082  11.49120  3.29244  1.000 24.84446 ? 457 SER A CB  1 
ATOM   645  O  OG  . SER A 1 78  ? 5.69327  10.52655  4.03117  1.000 25.52132 ? 457 SER A OG  1 
ATOM   646  N  N   . ASP A 1 79  ? 2.84308  9.06377   3.96929  1.000 24.44083 ? 458 ASP A N   1 
ATOM   647  C  CA  . ASP A 1 79  ? 2.37590  7.74692   3.54958  1.000 26.48921 ? 458 ASP A CA  1 
ATOM   648  C  C   . ASP A 1 79  ? 0.85573  7.64606   3.46987  1.000 26.91464 ? 458 ASP A C   1 
ATOM   649  O  O   . ASP A 1 79  ? 0.34465  6.58244   3.10098  1.000 27.19037 ? 458 ASP A O   1 
ATOM   650  C  CB  . ASP A 1 79  ? 2.94671  6.64645   4.47007  1.000 26.87528 ? 458 ASP A CB  1 
ATOM   651  C  CG  . ASP A 1 79  ? 2.33297  6.63228   5.88265  1.000 27.37212 ? 458 ASP A CG  1 
ATOM   652  O  OD1 . ASP A 1 79  ? 1.39667  7.40430   6.17858  1.000 26.84288 ? 458 ASP A OD1 1 
ATOM   653  O  OD2 . ASP A 1 79  ? 2.81117  5.82120   6.71529  1.000 27.21690 ? 458 ASP A OD2 1 
ATOM   654  N  N   . GLY A 1 80  ? 0.12334  8.71413   3.79064  1.000 26.67295 ? 459 GLY A N   1 
ATOM   655  C  CA  . GLY A 1 80  ? -1.31749 8.71260   3.63124  1.000 25.99494 ? 459 GLY A CA  1 
ATOM   656  C  C   . GLY A 1 80  ? -2.10815 8.17243   4.80175  1.000 25.95669 ? 459 GLY A C   1 
ATOM   657  O  O   . GLY A 1 80  ? -3.34812 8.12851   4.72457  1.000 28.63259 ? 459 GLY A O   1 
ATOM   658  N  N   . SER A 1 81  ? -1.44969 7.75368   5.87423  1.000 27.08123 ? 460 SER A N   1 
ATOM   659  C  CA  . SER A 1 81  ? -2.16614 7.26222   7.03773  1.000 27.37360 ? 460 SER A CA  1 
ATOM   660  C  C   . SER A 1 81  ? -2.72613 8.42807   7.84467  1.000 29.47941 ? 460 SER A C   1 
ATOM   661  O  O   . SER A 1 81  ? -2.34352 9.58547   7.65452  1.000 28.17339 ? 460 SER A O   1 
ATOM   662  C  CB  . SER A 1 81  ? -1.25347 6.40205   7.90607  1.000 24.59903 ? 460 SER A CB  1 
ATOM   663  O  OG  . SER A 1 81  ? -0.13538 7.15033   8.34530  1.000 24.95795 ? 460 SER A OG  1 
ATOM   664  N  N   . LEU A 1 82  ? -3.66078 8.10922   8.74061  1.000 27.82583 ? 461 LEU A N   1 
ATOM   665  C  CA  . LEU A 1 82  ? -4.30887 9.11977   9.56759  1.000 30.02615 ? 461 LEU A CA  1 
ATOM   666  C  C   . LEU A 1 82  ? -3.36438 9.64713   10.63536 1.000 29.67970 ? 461 LEU A C   1 
ATOM   667  O  O   . LEU A 1 82  ? -2.52506 8.91557   11.16211 1.000 27.08175 ? 461 LEU A O   1 
ATOM   668  C  CB  . LEU A 1 82  ? -5.53169 8.53674   10.26351 1.000 30.18667 ? 461 LEU A CB  1 
ATOM   669  C  CG  . LEU A 1 82  ? -6.60445 7.93918   9.37550  1.000 34.99148 ? 461 LEU A CG  1 
ATOM   670  C  CD1 . LEU A 1 82  ? -7.66981 7.34412   10.26230 1.000 31.54922 ? 461 LEU A CD1 1 
ATOM   671  C  CD2 . LEU A 1 82  ? -7.18776 9.00792   8.48014  1.000 38.66222 ? 461 LEU A CD2 1 
ATOM   672  N  N   . VAL A 1 83  ? -3.52432 10.92484  10.98012 1.000 29.69243 ? 462 VAL A N   1 
ATOM   673  C  CA  . VAL A 1 83  ? -2.79849 11.50359  12.11620 1.000 28.81943 ? 462 VAL A CA  1 
ATOM   674  C  C   . VAL A 1 83  ? -3.64880 11.20445  13.34593 1.000 29.56533 ? 462 VAL A C   1 
ATOM   675  O  O   . VAL A 1 83  ? -4.56695 11.94259  13.69206 1.000 34.73652 ? 462 VAL A O   1 
ATOM   676  C  CB  . VAL A 1 83  ? -2.53100 12.99685  11.94462 1.000 31.06472 ? 462 VAL A CB  1 
ATOM   677  C  CG1 . VAL A 1 83  ? -1.74952 13.53023  13.14347 1.000 27.91636 ? 462 VAL A CG1 1 
ATOM   678  C  CG2 . VAL A 1 83  ? -1.76058 13.26057  10.66738 1.000 27.44257 ? 462 VAL A CG2 1 
ATOM   679  N  N   . SER A 1 84  ? -3.35257 10.08785  13.99940 1.000 26.90113 ? 463 SER A N   1 
ATOM   680  C  CA  . SER A 1 84  ? -4.07031 9.68585   15.19737 1.000 29.51572 ? 463 SER A CA  1 
ATOM   681  C  C   . SER A 1 84  ? -3.31215 10.01500  16.47147 1.000 28.86162 ? 463 SER A C   1 
ATOM   682  O  O   . SER A 1 84  ? -3.87599 9.87565   17.56424 1.000 30.32695 ? 463 SER A O   1 
ATOM   683  C  CB  . SER A 1 84  ? -4.34936 8.18086   15.15716 1.000 30.29825 ? 463 SER A CB  1 
ATOM   684  O  OG  . SER A 1 84  ? -4.88376 7.80524   13.90192 1.000 30.01840 ? 463 SER A OG  1 
ATOM   685  N  N   . PHE A 1 85  ? -2.06209 10.45210  16.34717 1.000 25.84414 ? 464 PHE A N   1 
ATOM   686  C  CA  . PHE A 1 85  ? -1.14040 10.63239  17.45664 1.000 26.67286 ? 464 PHE A CA  1 
ATOM   687  C  C   . PHE A 1 85  ? -0.15756 11.73506  17.08660 1.000 23.65186 ? 464 PHE A C   1 
ATOM   688  O  O   . PHE A 1 85  ? 0.34398  11.76563  15.96197 1.000 23.17572 ? 464 PHE A O   1 
ATOM   689  C  CB  . PHE A 1 85  ? -0.38391 9.32645   17.75002 1.000 24.62630 ? 464 PHE A CB  1 
ATOM   690  C  CG  . PHE A 1 85  ? 0.72650  9.47789   18.73183 1.000 23.32336 ? 464 PHE A CG  1 
ATOM   691  C  CD1 . PHE A 1 85  ? 0.47235  9.42769   20.08683 1.000 24.48720 ? 464 PHE A CD1 1 
ATOM   692  C  CD2 . PHE A 1 85  ? 2.03258  9.67624   18.30344 1.000 24.29623 ? 464 PHE A CD2 1 
ATOM   693  C  CE1 . PHE A 1 85  ? 1.50660  9.56503   21.00030 1.000 25.08679 ? 464 PHE A CE1 1 
ATOM   694  C  CE2 . PHE A 1 85  ? 3.06847  9.80556   19.21133 1.000 23.30542 ? 464 PHE A CE2 1 
ATOM   695  C  CZ  . PHE A 1 85  ? 2.80195  9.75686   20.56009 1.000 25.87945 ? 464 PHE A CZ  1 
ATOM   696  N  N   . THR A 1 86  ? 0.10492  12.64384  18.02091 1.000 25.09711 ? 465 THR A N   1 
ATOM   697  C  CA  . THR A 1 86  ? 1.17176  13.62306  17.84819 1.000 24.30295 ? 465 THR A CA  1 
ATOM   698  C  C   . THR A 1 86  ? 1.99985  13.71266  19.11818 1.000 24.00545 ? 465 THR A C   1 
ATOM   699  O  O   . THR A 1 86  ? 1.56416  13.31931  20.20115 1.000 25.57505 ? 465 THR A O   1 
ATOM   700  C  CB  . THR A 1 86  ? 0.64704  15.03086  17.50529 1.000 26.38727 ? 465 THR A CB  1 
ATOM   701  O  OG1 . THR A 1 86  ? -0.10985 15.53829  18.60463 1.000 25.05379 ? 465 THR A OG1 1 
ATOM   702  C  CG2 . THR A 1 86  ? -0.19814 15.01225  16.25346 1.000 26.07195 ? 465 THR A CG2 1 
ATOM   703  N  N   . HIS A 1 87  ? 3.20416  14.25575  18.97524 1.000 21.06529 ? 466 HIS A N   1 
ATOM   704  C  CA  . HIS A 1 87  ? 4.11142  14.37262  20.09825 1.000 23.98814 ? 466 HIS A CA  1 
ATOM   705  C  C   . HIS A 1 87  ? 4.97712  15.61467  19.88551 1.000 24.99313 ? 466 HIS A C   1 
ATOM   706  O  O   . HIS A 1 87  ? 6.19673  15.55677  19.80373 1.000 23.65820 ? 466 HIS A O   1 
ATOM   707  C  CB  . HIS A 1 87  ? 4.93819  13.09322  20.23812 1.000 24.22872 ? 466 HIS A CB  1 
ATOM   708  C  CG  . HIS A 1 87  ? 5.45001  12.85232  21.62424 1.000 28.34138 ? 466 HIS A CG  1 
ATOM   709  N  ND1 . HIS A 1 87  ? 6.77950  12.60501  21.89537 1.000 29.27471 ? 466 HIS A ND1 1 
ATOM   710  C  CD2 . HIS A 1 87  ? 4.81150  12.82005  22.81747 1.000 28.95429 ? 466 HIS A CD2 1 
ATOM   711  C  CE1 . HIS A 1 87  ? 6.93759  12.42940  23.19543 1.000 30.81465 ? 466 HIS A CE1 1 
ATOM   712  N  NE2 . HIS A 1 87  ? 5.75764  12.55202  23.77705 1.000 32.69501 ? 466 HIS A NE2 1 
ATOM   713  N  N   . TRP A 1 88  ? 4.33494  16.77857  19.78807 1.000 23.82481 ? 467 TRP A N   1 
ATOM   714  C  CA  . TRP A 1 88  ? 5.05695  18.00737  19.47928 1.000 24.06707 ? 467 TRP A CA  1 
ATOM   715  C  C   . TRP A 1 88  ? 5.84929  18.50276  20.67944 1.000 25.05926 ? 467 TRP A C   1 
ATOM   716  O  O   . TRP A 1 88  ? 5.39518  18.42318  21.82414 1.000 26.18814 ? 467 TRP A O   1 
ATOM   717  C  CB  . TRP A 1 88  ? 4.08084  19.10292  19.05793 1.000 26.02219 ? 467 TRP A CB  1 
ATOM   718  C  CG  . TRP A 1 88  ? 3.36310  18.88735  17.76486 1.000 24.85510 ? 467 TRP A CG  1 
ATOM   719  C  CD1 . TRP A 1 88  ? 2.04833  18.53480  17.59611 1.000 25.97725 ? 467 TRP A CD1 1 
ATOM   720  C  CD2 . TRP A 1 88  ? 3.90853  19.04727  16.45699 1.000 24.49518 ? 467 TRP A CD2 1 
ATOM   721  N  NE1 . TRP A 1 88  ? 1.75111  18.45911  16.25506 1.000 25.91040 ? 467 TRP A NE1 1 
ATOM   722  C  CE2 . TRP A 1 88  ? 2.88068  18.76470  15.53696 1.000 25.01629 ? 467 TRP A CE2 1 
ATOM   723  C  CE3 . TRP A 1 88  ? 5.17698  19.39388  15.97210 1.000 24.40029 ? 467 TRP A CE3 1 
ATOM   724  C  CZ2 . TRP A 1 88  ? 3.07567  18.83148  14.16340 1.000 23.24650 ? 467 TRP A CZ2 1 
ATOM   725  C  CZ3 . TRP A 1 88  ? 5.36867  19.45205  14.60826 1.000 25.08192 ? 467 TRP A CZ3 1 
ATOM   726  C  CH2 . TRP A 1 88  ? 4.32100  19.18632  13.71933 1.000 22.93674 ? 467 TRP A CH2 1 
ATOM   727  N  N   . HIS A 1 89  ? 7.01977  19.07371  20.41037 1.000 23.93617 ? 468 HIS A N   1 
ATOM   728  C  CA  . HIS A 1 89  ? 7.63618  19.93209  21.39975 1.000 27.07762 ? 468 HIS A CA  1 
ATOM   729  C  C   . HIS A 1 89  ? 6.65674  21.04952  21.74954 1.000 28.27658 ? 468 HIS A C   1 
ATOM   730  O  O   . HIS A 1 89  ? 5.87613  21.47705  20.89928 1.000 27.63551 ? 468 HIS A O   1 
ATOM   731  C  CB  . HIS A 1 89  ? 8.93629  20.53754  20.86749 1.000 26.35255 ? 468 HIS A CB  1 
ATOM   732  C  CG  . HIS A 1 89  ? 10.10240 19.59961  20.89879 1.000 28.07429 ? 468 HIS A CG  1 
ATOM   733  N  ND1 . HIS A 1 89  ? 10.87216 19.41204  22.02624 1.000 29.38858 ? 468 HIS A ND1 1 
ATOM   734  C  CD2 . HIS A 1 89  ? 10.64021 18.81234  19.94028 1.000 26.75313 ? 468 HIS A CD2 1 
ATOM   735  C  CE1 . HIS A 1 89  ? 11.82852 18.54115  21.76238 1.000 28.44942 ? 468 HIS A CE1 1 
ATOM   736  N  NE2 . HIS A 1 89  ? 11.71242 18.16456  20.50270 1.000 27.57983 ? 468 HIS A NE2 1 
ATOM   737  N  N   . PRO A 1 90  ? 6.68394  21.54245  22.98333 1.000 30.66281 ? 469 PRO A N   1 
ATOM   738  C  CA  . PRO A 1 90  ? 5.84747  22.70056  23.31362 1.000 32.92608 ? 469 PRO A CA  1 
ATOM   739  C  C   . PRO A 1 90  ? 6.13366  23.84284  22.35509 1.000 31.83958 ? 469 PRO A C   1 
ATOM   740  O  O   . PRO A 1 90  ? 7.28445  24.10486  21.99837 1.000 31.32949 ? 469 PRO A O   1 
ATOM   741  C  CB  . PRO A 1 90  ? 6.26794  23.05232  24.74416 1.000 36.39293 ? 469 PRO A CB  1 
ATOM   742  C  CG  . PRO A 1 90  ? 6.99037  21.85839  25.24889 1.000 40.24415 ? 469 PRO A CG  1 
ATOM   743  C  CD  . PRO A 1 90  ? 7.62684  21.21757  24.06266 1.000 34.06280 ? 469 PRO A CD  1 
ATOM   744  N  N   . PHE A 1 91  ? 5.05825  24.48146  21.90259 1.000 31.89172 ? 470 PHE A N   1 
ATOM   745  C  CA  . PHE A 1 91  ? 5.01185  25.62128  20.99574 1.000 32.90079 ? 470 PHE A CA  1 
ATOM   746  C  C   . PHE A 1 91  ? 5.34662  25.25156  19.56026 1.000 31.30287 ? 470 PHE A C   1 
ATOM   747  O  O   . PHE A 1 91  ? 5.35651  26.14087  18.69316 1.000 33.72219 ? 470 PHE A O   1 
ATOM   748  C  CB  . PHE A 1 91  ? 5.89906  26.77056  21.48310 1.000 32.70894 ? 470 PHE A CB  1 
ATOM   749  C  CG  . PHE A 1 91  ? 5.45821  27.31135  22.80416 1.000 34.09998 ? 470 PHE A CG  1 
ATOM   750  C  CD1 . PHE A 1 91  ? 4.42746  28.22580  22.87105 1.000 35.31455 ? 470 PHE A CD1 1 
ATOM   751  C  CD2 . PHE A 1 91  ? 6.02257  26.85642  23.97950 1.000 34.23180 ? 470 PHE A CD2 1 
ATOM   752  C  CE1 . PHE A 1 91  ? 3.99554  28.70621  24.07744 1.000 37.83933 ? 470 PHE A CE1 1 
ATOM   753  C  CE2 . PHE A 1 91  ? 5.59249  27.33979  25.19220 1.000 36.63541 ? 470 PHE A CE2 1 
ATOM   754  C  CZ  . PHE A 1 91  ? 4.58040  28.26038  25.24193 1.000 38.50879 ? 470 PHE A CZ  1 
ATOM   755  N  N   . GLU A 1 92  ? 5.57911  24.02096  19.27861 1.000 27.84920 ? 471 GLU A N   1 
ATOM   756  C  CA  . GLU A 1 92  ? 5.62837  23.53693  17.91362 1.000 27.71919 ? 471 GLU A CA  1 
ATOM   757  C  C   . GLU A 1 92  ? 4.29354  22.91261  17.54208 1.000 27.13583 ? 471 GLU A C   1 
ATOM   758  O  O   . GLU A 1 92  ? 3.61641  22.34009  18.39869 1.000 28.33277 ? 471 GLU A O   1 
ATOM   759  C  CB  . GLU A 1 92  ? 6.72409  22.48566  17.73275 1.000 26.07497 ? 471 GLU A CB  1 
ATOM   760  C  CG  . GLU A 1 92  ? 8.08300  22.89587  18.24127 1.000 26.44252 ? 471 GLU A CG  1 
ATOM   761  C  CD  . GLU A 1 92  ? 8.69248  24.04400  17.46253 1.000 31.67789 ? 471 GLU A CD  1 
ATOM   762  O  OE1 . GLU A 1 92  ? 8.18585  24.37385  16.36051 1.000 30.46044 ? 471 GLU A OE1 1 
ATOM   763  O  OE2 . GLU A 1 92  ? 9.68355  24.62352  17.96492 1.000 30.73184 ? 471 GLU A OE2 1 
ATOM   764  N  N   . PRO A 1 93  ? 3.89894  22.97642  16.26992 1.000 27.27558 ? 472 PRO A N   1 
ATOM   765  C  CA  . PRO A 1 93  ? 4.61171  23.58270  15.13655 1.000 28.40035 ? 472 PRO A CA  1 
ATOM   766  C  C   . PRO A 1 93  ? 4.51018  25.10450  15.14464 1.000 30.00358 ? 472 PRO A C   1 
ATOM   767  O  O   . PRO A 1 93  ? 3.47058  25.64097  15.49009 1.000 27.40926 ? 472 PRO A O   1 
ATOM   768  C  CB  . PRO A 1 93  ? 3.90786  22.95712  13.93101 1.000 27.11669 ? 472 PRO A CB  1 
ATOM   769  C  CG  . PRO A 1 93  ? 2.49371  22.74193  14.40884 1.000 27.27967 ? 472 PRO A CG  1 
ATOM   770  C  CD  . PRO A 1 93  ? 2.60991  22.38220  15.86137 1.000 25.52018 ? 472 PRO A CD  1 
ATOM   771  N  N   . ASN A 1 94  ? 5.56930  25.83363  14.78831 1.000 29.77948 ? 473 ASN A N   1 
ATOM   772  C  CA  . ASN A 1 94  ? 5.53675  27.28666  14.84132 1.000 32.43337 ? 473 ASN A CA  1 
ATOM   773  C  C   . ASN A 1 94  ? 5.82297  27.95875  13.50484 1.000 32.19990 ? 473 ASN A C   1 
ATOM   774  O  O   . ASN A 1 94  ? 5.81793  29.19219  13.44798 1.000 34.36431 ? 473 ASN A O   1 
ATOM   775  C  CB  . ASN A 1 94  ? 6.50550  27.81401  15.91748 1.000 32.75900 ? 473 ASN A CB  1 
ATOM   776  C  CG  . ASN A 1 94  ? 7.97293  27.52724  15.60491 1.000 31.35088 ? 473 ASN A CG  1 
ATOM   777  O  OD1 . ASN A 1 94  ? 8.29272  26.81422  14.65917 1.000 29.70104 ? 473 ASN A OD1 1 
ATOM   778  N  ND2 . ASN A 1 94  ? 8.87179  28.09092  16.41648 1.000 32.03400 ? 473 ASN A ND2 1 
ATOM   779  N  N   . ASN A 1 95  ? 6.05046  27.19231  12.43519 1.000 33.28684 ? 474 ASN A N   1 
ATOM   780  C  CA  . ASN A 1 95  ? 6.22289  27.71765  11.07448 1.000 35.18521 ? 474 ASN A CA  1 
ATOM   781  C  C   . ASN A 1 95  ? 7.15099  28.93363  11.04875 1.000 41.29312 ? 474 ASN A C   1 
ATOM   782  O  O   . ASN A 1 95  ? 6.87772  29.95413  10.41245 1.000 45.46269 ? 474 ASN A O   1 
ATOM   783  C  CB  . ASN A 1 95  ? 4.86886  28.04679  10.45011 1.000 39.71467 ? 474 ASN A CB  1 
ATOM   784  C  CG  . ASN A 1 95  ? 4.92890  28.11788  8.93880  1.000 39.88061 ? 474 ASN A CG  1 
ATOM   785  O  OD1 . ASN A 1 95  ? 5.26153  27.13342  8.27247  1.000 37.99667 ? 474 ASN A OD1 1 
ATOM   786  N  ND2 . ASN A 1 95  ? 4.59720  29.27724  8.38725  1.000 46.84996 ? 474 ASN A ND2 1 
ATOM   787  N  N   . PHE A 1 96  ? 8.28304  28.80469  11.73945 1.000 38.45501 ? 475 PHE A N   1 
ATOM   788  C  CA  . PHE A 1 96  ? 9.12258  29.96671  12.01058 1.000 43.28538 ? 475 PHE A CA  1 
ATOM   789  C  C   . PHE A 1 96  ? 9.78114  30.49953  10.74450 1.000 50.71894 ? 475 PHE A C   1 
ATOM   790  O  O   . PHE A 1 96  ? 9.65853  31.68694  10.41362 1.000 55.96525 ? 475 PHE A O   1 
ATOM   791  C  CB  . PHE A 1 96  ? 10.18133 29.60304  13.04273 1.000 38.63600 ? 475 PHE A CB  1 
ATOM   792  C  CG  . PHE A 1 96  ? 11.03456 30.75500  13.44191 1.000 42.23723 ? 475 PHE A CG  1 
ATOM   793  C  CD1 . PHE A 1 96  ? 10.57354 31.66975  14.36353 1.000 41.16380 ? 475 PHE A CD1 1 
ATOM   794  C  CD2 . PHE A 1 96  ? 12.28572 30.93822  12.88108 1.000 47.14111 ? 475 PHE A CD2 1 
ATOM   795  C  CE1 . PHE A 1 96  ? 11.33763 32.73088  14.73867 1.000 40.56134 ? 475 PHE A CE1 1 
ATOM   796  C  CE2 . PHE A 1 96  ? 13.06170 32.00407  13.25201 1.000 46.93436 ? 475 PHE A CE2 1 
ATOM   797  C  CZ  . PHE A 1 96  ? 12.58669 32.90863  14.18192 1.000 44.23280 ? 475 PHE A CZ  1 
ATOM   798  N  N   . ARG A 1 97  ? 10.51540 29.64141  10.04377 1.000 60.83683 ? 476 ARG A N   1 
ATOM   799  C  CA  . ARG A 1 97  ? 11.29151 30.05188  8.88171  1.000 58.94986 ? 476 ARG A CA  1 
ATOM   800  C  C   . ARG A 1 97  ? 10.37756 30.17791  7.66579  1.000 65.97525 ? 476 ARG A C   1 
ATOM   801  O  O   . ARG A 1 97  ? 9.66550  29.23066  7.30880  1.000 60.92751 ? 476 ARG A O   1 
ATOM   802  C  CB  . ARG A 1 97  ? 12.41531 29.04877  8.62657  1.000 56.83362 ? 476 ARG A CB  1 
ATOM   803  C  CG  . ARG A 1 97  ? 13.52369 29.53758  7.70908  1.000 63.53105 ? 476 ARG A CG  1 
ATOM   804  C  CD  . ARG A 1 97  ? 14.55333 30.36880  8.45848  1.000 68.95732 ? 476 ARG A CD  1 
ATOM   805  N  NE  . ARG A 1 97  ? 13.99988 31.62122  8.96102  1.000 68.86123 ? 476 ARG A NE  1 
ATOM   806  C  CZ  . ARG A 1 97  ? 14.70851 32.56945  9.55810  1.000 69.67679 ? 476 ARG A CZ  1 
ATOM   807  N  NH1 . ARG A 1 97  ? 16.01278 32.44671  9.73975  1.000 69.48639 ? 476 ARG A NH1 1 
ATOM   808  N  NH2 . ARG A 1 97  ? 14.09294 33.66937  9.98250  1.000 69.85984 ? 476 ARG A NH2 1 
ATOM   809  N  N   . ASP A 1 98  ? 10.38622 31.35131  7.04044  1.000 73.50910 ? 477 ASP A N   1 
ATOM   810  C  CA  . ASP A 1 98  ? 9.57346  31.58329  5.85507  1.000 73.55341 ? 477 ASP A CA  1 
ATOM   811  C  C   . ASP A 1 98  ? 10.44131 32.04413  4.69733  1.000 69.01551 ? 477 ASP A C   1 
ATOM   812  O  O   . ASP A 1 98  ? 11.08368 31.22898  4.04092  1.000 76.56091 ? 477 ASP A O   1 
ATOM   813  C  CB  . ASP A 1 98  ? 8.47638  32.60639  6.14788  1.000 75.87890 ? 477 ASP A CB  1 
ATOM   814  C  CG  . ASP A 1 98  ? 7.41170  32.05930  7.07474  1.000 76.30345 ? 477 ASP A CG  1 
ATOM   815  O  OD1 . ASP A 1 98  ? 7.22324  30.82230  7.08399  1.000 71.63766 ? 477 ASP A OD1 1 
ATOM   816  O  OD2 . ASP A 1 98  ? 6.76903  32.86007  7.79009  1.000 76.66554 ? 477 ASP A OD2 1 
ATOM   817  N  N   . GLU A 1 101 ? 9.00404  26.40426  7.07902  1.000 36.10538 ? 480 GLU A N   1 
ATOM   818  C  CA  . GLU A 1 101 ? 9.04360  25.19708  7.90697  1.000 31.05679 ? 480 GLU A CA  1 
ATOM   819  C  C   . GLU A 1 101 ? 7.83760  24.31832  7.65992  1.000 32.96943 ? 480 GLU A C   1 
ATOM   820  O  O   . GLU A 1 101 ? 6.78725  24.51429  8.27485  1.000 32.74134 ? 480 GLU A O   1 
ATOM   821  C  CB  . GLU A 1 101 ? 9.09383  25.53865  9.39334  1.000 31.77114 ? 480 GLU A CB  1 
ATOM   822  C  CG  . GLU A 1 101 ? 10.20338 26.46280  9.78416  1.000 35.83194 ? 480 GLU A CG  1 
ATOM   823  C  CD  . GLU A 1 101 ? 10.60686 26.29827  11.22823 1.000 34.59228 ? 480 GLU A CD  1 
ATOM   824  O  OE1 . GLU A 1 101 ? 9.73044  26.08187  12.09403 1.000 28.50984 ? 480 GLU A OE1 1 
ATOM   825  O  OE2 . GLU A 1 101 ? 11.82031 26.36836  11.49536 1.000 38.72962 ? 480 GLU A OE2 1 
ATOM   826  N  N   . ASP A 1 102 ? 7.98411  23.32826  6.78823  1.000 29.46986 ? 481 ASP A N   1 
ATOM   827  C  CA  . ASP A 1 102 ? 6.85790  22.48598  6.43369  1.000 30.28751 ? 481 ASP A CA  1 
ATOM   828  C  C   . ASP A 1 102 ? 7.10881  20.99676  6.59127  1.000 29.03952 ? 481 ASP A C   1 
ATOM   829  O  O   . ASP A 1 102 ? 6.23358  20.20444  6.22455  1.000 25.67582 ? 481 ASP A O   1 
ATOM   830  C  CB  . ASP A 1 102 ? 6.42568  22.75624  4.99100  1.000 31.78843 ? 481 ASP A CB  1 
ATOM   831  C  CG  . ASP A 1 102 ? 5.90817  24.15522  4.79413  1.000 33.89888 ? 481 ASP A CG  1 
ATOM   832  O  OD1 . ASP A 1 102 ? 5.38826  24.75102  5.76654  1.000 33.63271 ? 481 ASP A OD1 1 
ATOM   833  O  OD2 . ASP A 1 102 ? 6.01239  24.65260  3.65531  1.000 34.80364 ? 481 ASP A OD2 1 
ATOM   834  N  N   . CYS A 1 103 ? 8.26498  20.59317  7.11246  1.000 27.64745 ? 482 CYS A N   1 
ATOM   835  C  CA  . CYS A 1 103 ? 8.61303  19.19329  7.29621  1.000 24.37261 ? 482 CYS A CA  1 
ATOM   836  C  C   . CYS A 1 103 ? 8.97935  18.97709  8.75781  1.000 23.93493 ? 482 CYS A C   1 
ATOM   837  O  O   . CYS A 1 103 ? 9.44035  19.89872  9.43131  1.000 27.17695 ? 482 CYS A O   1 
ATOM   838  C  CB  . CYS A 1 103 ? 9.77240  18.80108  6.37641  1.000 27.77072 ? 482 CYS A CB  1 
ATOM   839  S  SG  . CYS A 1 103 ? 9.40619  19.00769  4.61380  1.000 29.90171 ? 482 CYS A SG  1 
ATOM   840  N  N   . VAL A 1 104 ? 8.80406  17.75737  9.25324  1.000 21.58449 ? 483 VAL A N   1 
ATOM   841  C  CA  . VAL A 1 104 ? 8.83025  17.51147  10.69259 1.000 21.14880 ? 483 VAL A CA  1 
ATOM   842  C  C   . VAL A 1 104 ? 10.00650 16.61418  11.06122 1.000 20.69705 ? 483 VAL A C   1 
ATOM   843  O  O   . VAL A 1 104 ? 10.25588 15.59428  10.40483 1.000 21.66601 ? 483 VAL A O   1 
ATOM   844  C  CB  . VAL A 1 104 ? 7.50420  16.90577  11.17915 1.000 20.52772 ? 483 VAL A CB  1 
ATOM   845  C  CG1 . VAL A 1 104 ? 7.59482  16.54385  12.65893 1.000 19.93268 ? 483 VAL A CG1 1 
ATOM   846  C  CG2 . VAL A 1 104 ? 6.36952  17.91394  10.95036 1.000 21.02547 ? 483 VAL A CG2 1 
ATOM   847  N  N   . THR A 1 105 ? 10.70966 16.98879  12.12776 1.000 23.30870 ? 484 THR A N   1 
ATOM   848  C  CA  . THR A 1 105 ? 11.78893 16.20272  12.70483 1.000 21.65889 ? 484 THR A CA  1 
ATOM   849  C  C   . THR A 1 105 ? 11.39409 15.71128  14.08936 1.000 24.43406 ? 484 THR A C   1 
ATOM   850  O  O   . THR A 1 105 ? 10.51531 16.27057  14.74370 1.000 24.46606 ? 484 THR A O   1 
ATOM   851  C  CB  . THR A 1 105 ? 13.08897 17.01217  12.84139 1.000 26.10489 ? 484 THR A CB  1 
ATOM   852  O  OG1 . THR A 1 105 ? 12.92199 18.03576  13.83129 1.000 25.04958 ? 484 THR A OG1 1 
ATOM   853  C  CG2 . THR A 1 105 ? 13.48408 17.64819  11.53592 1.000 26.41239 ? 484 THR A CG2 1 
ATOM   854  N  N   . ILE A 1 106 ? 12.04178 14.63809  14.52563 1.000 24.23352 ? 485 ILE A N   1 
ATOM   855  C  CA  A ILE A 1 106 ? 12.07577 14.22463  15.92383 0.500 26.70213 ? 485 ILE A CA  1 
ATOM   856  C  CA  B ILE A 1 106 ? 12.04903 14.28902  15.93536 0.500 26.52140 ? 485 ILE A CA  1 
ATOM   857  C  C   . ILE A 1 106 ? 13.41381 14.67916  16.47884 1.000 25.85429 ? 485 ILE A C   1 
ATOM   858  O  O   . ILE A 1 106 ? 14.44507 14.46856  15.82808 1.000 26.89742 ? 485 ILE A O   1 
ATOM   859  C  CB  A ILE A 1 106 ? 11.94081 12.69768  16.06053 0.500 25.72837 ? 485 ILE A CB  1 
ATOM   860  C  CB  B ILE A 1 106 ? 11.72040 12.80319  16.19813 0.500 25.55200 ? 485 ILE A CB  1 
ATOM   861  C  CG1 A ILE A 1 106 ? 10.53200 12.21370  15.73753 0.500 24.96942 ? 485 ILE A CG1 1 
ATOM   862  C  CG1 B ILE A 1 106 ? 12.80495 11.86899  15.67637 0.500 25.38956 ? 485 ILE A CG1 1 
ATOM   863  C  CG2 A ILE A 1 106 ? 12.34487 12.24745  17.44478 0.500 26.22598 ? 485 ILE A CG2 1 
ATOM   864  C  CG2 B ILE A 1 106 ? 10.39673 12.43118  15.55400 0.500 24.82868 ? 485 ILE A CG2 1 
ATOM   865  C  CD1 A ILE A 1 106 ? 10.39496 10.71746  15.91308 0.500 26.42984 ? 485 ILE A CD1 1 
ATOM   866  C  CD1 B ILE A 1 106 ? 12.46586 10.39224  15.90200 0.500 28.20185 ? 485 ILE A CD1 1 
ATOM   867  N  N   . TRP A 1 107 ? 13.41548 15.30462  17.65172 1.000 26.56185 ? 486 TRP A N   1 
ATOM   868  C  CA  . TRP A 1 107 ? 14.70453 15.61357  18.24849 1.000 28.25084 ? 486 TRP A CA  1 
ATOM   869  C  C   . TRP A 1 107 ? 14.59115 15.59944  19.76223 1.000 29.52916 ? 486 TRP A C   1 
ATOM   870  O  O   . TRP A 1 107 ? 13.52180 15.83948  20.32368 1.000 26.21343 ? 486 TRP A O   1 
ATOM   871  C  CB  . TRP A 1 107 ? 15.27736 16.94076  17.73355 1.000 29.01862 ? 486 TRP A CB  1 
ATOM   872  C  CG  . TRP A 1 107 ? 14.66272 18.19419  18.26716 1.000 30.50663 ? 486 TRP A CG  1 
ATOM   873  C  CD1 . TRP A 1 107 ? 13.66905 18.92648  17.69324 1.000 30.45964 ? 486 TRP A CD1 1 
ATOM   874  C  CD2 . TRP A 1 107 ? 15.04303 18.89233  19.45829 1.000 32.32978 ? 486 TRP A CD2 1 
ATOM   875  N  NE1 . TRP A 1 107 ? 13.39077 20.03603  18.46444 1.000 33.45917 ? 486 TRP A NE1 1 
ATOM   876  C  CE2 . TRP A 1 107 ? 14.21999 20.03478  19.55528 1.000 33.59933 ? 486 TRP A CE2 1 
ATOM   877  C  CE3 . TRP A 1 107 ? 15.99003 18.65611  20.45880 1.000 35.03072 ? 486 TRP A CE3 1 
ATOM   878  C  CZ2 . TRP A 1 107 ? 14.31524 20.93981  20.61519 1.000 36.88151 ? 486 TRP A CZ2 1 
ATOM   879  C  CZ3 . TRP A 1 107 ? 16.08744 19.55584  21.50915 1.000 36.25173 ? 486 TRP A CZ3 1 
ATOM   880  C  CH2 . TRP A 1 107 ? 15.25530 20.68436  21.58005 1.000 38.10202 ? 486 TRP A CH2 1 
ATOM   881  N  N   . GLY A 1 108 ? 15.70434 15.26836  20.41302 1.000 29.34891 ? 487 GLY A N   1 
ATOM   882  C  CA  . GLY A 1 108 ? 15.75136 15.21042  21.85016 1.000 30.71664 ? 487 GLY A CA  1 
ATOM   883  C  C   . GLY A 1 108 ? 15.46976 13.81222  22.34223 1.000 31.09356 ? 487 GLY A C   1 
ATOM   884  O  O   . GLY A 1 108 ? 15.02100 12.94200  21.59180 1.000 29.94011 ? 487 GLY A O   1 
ATOM   885  N  N   . PRO A 1 109 ? 15.72759 13.57032  23.62723 1.000 30.86437 ? 488 PRO A N   1 
ATOM   886  C  CA  . PRO A 1 109 ? 15.61113 12.19974  24.15248 1.000 33.37235 ? 488 PRO A CA  1 
ATOM   887  C  C   . PRO A 1 109 ? 14.17964 11.71472  24.31442 1.000 34.64261 ? 488 PRO A C   1 
ATOM   888  O  O   . PRO A 1 109 ? 13.96031 10.49652  24.32471 1.000 34.19851 ? 488 PRO A O   1 
ATOM   889  C  CB  . PRO A 1 109 ? 16.33766 12.27957  25.50353 1.000 38.30567 ? 488 PRO A CB  1 
ATOM   890  C  CG  . PRO A 1 109 ? 16.25723 13.71863  25.89172 1.000 40.81190 ? 488 PRO A CG  1 
ATOM   891  C  CD  . PRO A 1 109 ? 16.26968 14.51499  24.61836 1.000 35.83059 ? 488 PRO A CD  1 
ATOM   892  N  N   . GLU A 1 110 ? 13.20081 12.60570  24.43244 1.000 32.72643 ? 489 GLU A N   1 
ATOM   893  C  CA  . GLU A 1 110 ? 11.81171 12.17551  24.53289 1.000 34.69935 ? 489 GLU A CA  1 
ATOM   894  C  C   . GLU A 1 110 ? 11.15814 11.96306  23.17558 1.000 28.84915 ? 489 GLU A C   1 
ATOM   895  O  O   . GLU A 1 110 ? 9.98755  11.56830  23.11919 1.000 30.32925 ? 489 GLU A O   1 
ATOM   896  C  CB  . GLU A 1 110 ? 11.00154 13.18369  25.35266 1.000 37.10020 ? 489 GLU A CB  1 
ATOM   897  C  CG  . GLU A 1 110 ? 11.15494 13.00347  26.85705 1.000 47.15024 ? 489 GLU A CG  1 
ATOM   898  C  CD  . GLU A 1 110 ? 11.34269 14.31984  27.59530 1.000 58.84839 ? 489 GLU A CD  1 
ATOM   899  O  OE1 . GLU A 1 110 ? 11.67273 15.33309  26.93841 1.000 60.57740 ? 489 GLU A OE1 1 
ATOM   900  O  OE2 . GLU A 1 110 ? 11.16278 14.34363  28.83478 1.000 63.88416 ? 489 GLU A OE2 1 
ATOM   901  N  N   . GLY A 1 111 ? 11.87631 12.20587  22.08389 1.000 29.15562 ? 490 GLY A N   1 
ATOM   902  C  CA  . GLY A 1 111 ? 11.29937 11.95820  20.78120 1.000 27.08576 ? 490 GLY A CA  1 
ATOM   903  C  C   . GLY A 1 111 ? 10.23798 12.94490  20.35679 1.000 26.35009 ? 490 GLY A C   1 
ATOM   904  O  O   . GLY A 1 111 ? 9.43122  12.62483  19.48885 1.000 24.40727 ? 490 GLY A O   1 
ATOM   905  N  N   . ARG A 1 112 ? 10.22091 14.14461  20.93251 1.000 25.54623 ? 491 ARG A N   1 
ATOM   906  C  CA  . ARG A 1 112 ? 9.20935  15.12257  20.55864 1.000 25.16114 ? 491 ARG A CA  1 
ATOM   907  C  C   . ARG A 1 112 ? 9.54953  15.75405  19.20651 1.000 24.64658 ? 491 ARG A C   1 
ATOM   908  O  O   . ARG A 1 112 ? 10.68303 15.66720  18.71862 1.000 24.34601 ? 491 ARG A O   1 
ATOM   909  C  CB  . ARG A 1 112 ? 9.05776  16.16791  21.66038 1.000 26.38092 ? 491 ARG A CB  1 
ATOM   910  C  CG  . ARG A 1 112 ? 8.45592  15.57122  22.92501 1.000 28.65740 ? 491 ARG A CG  1 
ATOM   911  C  CD  . ARG A 1 112 ? 7.76511  16.60300  23.80410 1.000 31.59281 ? 491 ARG A CD  1 
ATOM   912  N  NE  . ARG A 1 112 ? 7.01056  15.96229  24.87698 1.000 35.94199 ? 491 ARG A NE  1 
ATOM   913  C  CZ  . ARG A 1 112 ? 5.70215  15.73555  24.84869 1.000 39.08607 ? 491 ARG A CZ  1 
ATOM   914  N  NH1 . ARG A 1 112 ? 4.94956  16.13139  23.83094 1.000 36.85352 ? 491 ARG A NH1 1 
ATOM   915  N  NH2 . ARG A 1 112 ? 5.13133  15.10418  25.87090 1.000 40.28291 ? 491 ARG A NH2 1 
ATOM   916  N  N   . TRP A 1 113 ? 8.54003  16.37081  18.58665 1.000 23.23014 ? 492 TRP A N   1 
ATOM   917  C  CA  . TRP A 1 113 ? 8.58257  16.75708  17.18110 1.000 23.25720 ? 492 TRP A CA  1 
ATOM   918  C  C   . TRP A 1 113 ? 8.66820  18.27390  17.00559 1.000 23.08767 ? 492 TRP A C   1 
ATOM   919  O  O   . TRP A 1 113 ? 8.21637  19.05286  17.85135 1.000 23.34707 ? 492 TRP A O   1 
ATOM   920  C  CB  . TRP A 1 113 ? 7.34161  16.24656  16.43328 1.000 22.03457 ? 492 TRP A CB  1 
ATOM   921  C  CG  . TRP A 1 113 ? 7.03713  14.77343  16.61639 1.000 21.62297 ? 492 TRP A CG  1 
ATOM   922  C  CD1 . TRP A 1 113 ? 7.84327  13.81786  17.17474 1.000 23.64796 ? 492 TRP A CD1 1 
ATOM   923  C  CD2 . TRP A 1 113 ? 5.82843  14.10633  16.24363 1.000 21.01181 ? 492 TRP A CD2 1 
ATOM   924  N  NE1 . TRP A 1 113 ? 7.20726  12.59153  17.16763 1.000 19.96043 ? 492 TRP A NE1 1 
ATOM   925  C  CE2 . TRP A 1 113 ? 5.96946  12.74466  16.60021 1.000 22.64541 ? 492 TRP A CE2 1 
ATOM   926  C  CE3 . TRP A 1 113 ? 4.63356  14.52791  15.64194 1.000 22.95772 ? 492 TRP A CE3 1 
ATOM   927  C  CZ2 . TRP A 1 113 ? 4.95954  11.79949  16.37253 1.000 23.63490 ? 492 TRP A CZ2 1 
ATOM   928  C  CZ3 . TRP A 1 113 ? 3.63062  13.58417  15.41686 1.000 21.52987 ? 492 TRP A CZ3 1 
ATOM   929  C  CH2 . TRP A 1 113 ? 3.80312  12.23887  15.78379 1.000 22.87759 ? 492 TRP A CH2 1 
ATOM   930  N  N   . ASN A 1 114 ? 9.21731  18.67725  15.85690 1.000 22.11967 ? 493 ASN A N   1 
ATOM   931  C  CA  . ASN A 1 114 ? 9.40153  20.07895  15.50510 1.000 25.72376 ? 493 ASN A CA  1 
ATOM   932  C  C   . ASN A 1 114 ? 9.23393  20.24840  14.00163 1.000 24.63100 ? 493 ASN A C   1 
ATOM   933  O  O   . ASN A 1 114 ? 9.69485  19.40894  13.23203 1.000 25.32823 ? 493 ASN A O   1 
ATOM   934  C  CB  . ASN A 1 114 ? 10.79116 20.56576  15.93237 1.000 25.72475 ? 493 ASN A CB  1 
ATOM   935  C  CG  . ASN A 1 114 ? 11.12056 21.93675  15.38657 1.000 28.30969 ? 493 ASN A CG  1 
ATOM   936  O  OD1 . ASN A 1 114 ? 10.26679 22.82361  15.33373 1.000 30.57195 ? 493 ASN A OD1 1 
ATOM   937  N  ND2 . ASN A 1 114 ? 12.36249 22.11768  14.96684 1.000 29.34589 ? 493 ASN A ND2 1 
ATOM   938  N  N   . ASP A 1 115 ? 8.60158  21.33916  13.57504 1.000 24.86339 ? 494 ASP A N   1 
ATOM   939  C  CA  . ASP A 1 115 ? 8.58121  21.64174  12.14950 1.000 24.59393 ? 494 ASP A CA  1 
ATOM   940  C  C   . ASP A 1 115 ? 9.84082  22.41411  11.78442 1.000 27.83298 ? 494 ASP A C   1 
ATOM   941  O  O   . ASP A 1 115 ? 10.30622 23.26217  12.54832 1.000 26.64856 ? 494 ASP A O   1 
ATOM   942  C  CB  . ASP A 1 115 ? 7.30241  22.39652  11.73939 1.000 26.21739 ? 494 ASP A CB  1 
ATOM   943  C  CG  . ASP A 1 115 ? 7.10567  23.72249  12.46216 1.000 27.29713 ? 494 ASP A CG  1 
ATOM   944  O  OD1 . ASP A 1 115 ? 7.60555  23.91218  13.58751 1.000 29.44193 ? 494 ASP A OD1 1 
ATOM   945  O  OD2 . ASP A 1 115 ? 6.41079  24.58953  11.88575 1.000 30.74142 ? 494 ASP A OD2 1 
ATOM   946  N  N   . SER A 1 116 ? 10.41745 22.07704  10.63623 1.000 26.41979 ? 495 SER A N   1 
ATOM   947  C  CA  . SER A 1 116 ? 11.75398 22.50929  10.25467 1.000 31.36641 ? 495 SER A CA  1 
ATOM   948  C  C   . SER A 1 116 ? 11.78296 22.85332  8.77140  1.000 30.52284 ? 495 SER A C   1 
ATOM   949  O  O   . SER A 1 116 ? 10.95002 22.36673  8.00064  1.000 27.67654 ? 495 SER A O   1 
ATOM   950  C  CB  . SER A 1 116 ? 12.79065 21.41225  10.53762 1.000 31.89382 ? 495 SER A CB  1 
ATOM   951  O  OG  . SER A 1 116 ? 12.96871 21.20336  11.92605 1.000 35.86949 ? 495 SER A OG  1 
ATOM   952  N  N   . PRO A 1 117 ? 12.74311 23.67106  8.34286  1.000 29.19555 ? 496 PRO A N   1 
ATOM   953  C  CA  . PRO A 1 117 ? 12.90492 23.90392  6.90038  1.000 31.03907 ? 496 PRO A CA  1 
ATOM   954  C  C   . PRO A 1 117 ? 13.21763 22.59976  6.18248  1.000 32.24481 ? 496 PRO A C   1 
ATOM   955  O  O   . PRO A 1 117 ? 14.08671 21.83496  6.60165  1.000 32.19536 ? 496 PRO A O   1 
ATOM   956  C  CB  . PRO A 1 117 ? 14.07557 24.89121  6.82665  1.000 33.22164 ? 496 PRO A CB  1 
ATOM   957  C  CG  . PRO A 1 117 ? 14.09933 25.54254  8.16372  1.000 37.44322 ? 496 PRO A CG  1 
ATOM   958  C  CD  . PRO A 1 117 ? 13.68056 24.48266  9.13610  1.000 32.72125 ? 496 PRO A CD  1 
ATOM   959  N  N   . CYS A 1 118 ? 12.49237 22.34905  5.09057  1.000 31.62408 ? 497 CYS A N   1 
ATOM   960  C  CA  . CYS A 1 118 ? 12.57358 21.05292  4.43109  1.000 33.38120 ? 497 CYS A CA  1 
ATOM   961  C  C   . CYS A 1 118 ? 13.92529 20.80121  3.77435  1.000 31.89389 ? 497 CYS A C   1 
ATOM   962  O  O   . CYS A 1 118 ? 14.26030 19.64207  3.50795  1.000 32.32139 ? 497 CYS A O   1 
ATOM   963  C  CB  . CYS A 1 118 ? 11.45911 20.93092  3.39900  1.000 31.18564 ? 497 CYS A CB  1 
ATOM   964  S  SG  . CYS A 1 118 ? 9.79084  20.96278  4.14257  1.000 42.33317 ? 497 CYS A SG  1 
ATOM   965  N  N   . ASN A 1 119 ? 14.71155 21.84178  3.52287  1.000 33.54565 ? 498 ASN A N   1 
ATOM   966  C  CA  . ASN A 1 119 ? 15.99116 21.68273  2.84274  1.000 32.18755 ? 498 ASN A CA  1 
ATOM   967  C  C   . ASN A 1 119 ? 17.13841 21.36888  3.79123  1.000 33.05575 ? 498 ASN A C   1 
ATOM   968  O  O   . ASN A 1 119 ? 18.28578 21.28482  3.34375  1.000 35.15744 ? 498 ASN A O   1 
ATOM   969  C  CB  . ASN A 1 119 ? 16.32623 22.93976  2.02653  1.000 35.69074 ? 498 ASN A CB  1 
ATOM   970  C  CG  . ASN A 1 119 ? 16.59386 24.16198  2.89825  1.000 38.12811 ? 498 ASN A CG  1 
ATOM   971  O  OD1 . ASN A 1 119 ? 16.03903 24.30100  3.98849  1.000 37.63183 ? 498 ASN A OD1 1 
ATOM   972  N  ND2 . ASN A 1 119 ? 17.44305 25.05804  2.41157  1.000 43.85459 ? 498 ASN A ND2 1 
ATOM   973  N  N   . GLN A 1 120 ? 16.86885 21.20305  5.07887  1.000 31.16850 ? 499 GLN A N   1 
ATOM   974  C  CA  . GLN A 1 120 ? 17.92593 20.85334  6.01738  1.000 35.63310 ? 499 GLN A CA  1 
ATOM   975  C  C   . GLN A 1 120 ? 18.38621 19.41588  5.77960  1.000 33.66793 ? 499 GLN A C   1 
ATOM   976  O  O   . GLN A 1 120 ? 17.57053 18.53370  5.51074  1.000 31.49808 ? 499 GLN A O   1 
ATOM   977  C  CB  . GLN A 1 120 ? 17.41788 21.01316  7.45181  1.000 34.27363 ? 499 GLN A CB  1 
ATOM   978  C  CG  . GLN A 1 120 ? 18.53863 21.22082  8.46549  1.000 40.81772 ? 499 GLN A CG  1 
ATOM   979  C  CD  . GLN A 1 120 ? 18.01667 21.41466  9.87524  1.000 47.04073 ? 499 GLN A CD  1 
ATOM   980  O  OE1 . GLN A 1 120 ? 16.82705 21.66949  10.07919 1.000 45.61344 ? 499 GLN A OE1 1 
ATOM   981  N  NE2 . GLN A 1 120 ? 18.90222 21.28449  10.86020 1.000 46.76034 ? 499 GLN A NE2 1 
ATOM   982  N  N   . SER A 1 121 ? 19.69530 19.16856  5.87835  1.000 33.46968 ? 500 SER A N   1 
ATOM   983  C  CA  . SER A 1 121 ? 20.21263 17.80729  5.72615  1.000 33.32836 ? 500 SER A CA  1 
ATOM   984  C  C   . SER A 1 121 ? 20.21334 17.10491  7.07818  1.000 32.41408 ? 500 SER A C   1 
ATOM   985  O  O   . SER A 1 121 ? 20.91940 17.52793  7.99767  1.000 30.27385 ? 500 SER A O   1 
ATOM   986  C  CB  . SER A 1 121 ? 21.61993 17.79693  5.13310  1.000 36.75688 ? 500 SER A CB  1 
ATOM   987  O  OG  . SER A 1 121 ? 21.61628 18.19515  3.77550  1.000 41.87203 ? 500 SER A OG  1 
ATOM   988  N  N   . LEU A 1 122 ? 19.46270 16.01140  7.18212  1.000 28.18056 ? 501 LEU A N   1 
ATOM   989  C  CA  . LEU A 1 122 ? 19.32592 15.26019  8.41989  1.000 29.04875 ? 501 LEU A CA  1 
ATOM   990  C  C   . LEU A 1 122 ? 19.18966 13.78520  8.08350  1.000 28.24066 ? 501 LEU A C   1 
ATOM   991  O  O   . LEU A 1 122 ? 18.78125 13.43473  6.97087  1.000 27.06603 ? 501 LEU A O   1 
ATOM   992  C  CB  . LEU A 1 122 ? 18.09527 15.70985  9.22112  1.000 29.57251 ? 501 LEU A CB  1 
ATOM   993  C  CG  . LEU A 1 122 ? 18.09325 17.11205  9.81537  1.000 31.02330 ? 501 LEU A CG  1 
ATOM   994  C  CD1 . LEU A 1 122 ? 16.71317 17.43529  10.34428 1.000 30.39388 ? 501 LEU A CD1 1 
ATOM   995  C  CD2 . LEU A 1 122 ? 19.14036 17.24309  10.90935 1.000 32.03539 ? 501 LEU A CD2 1 
ATOM   996  N  N   . PRO A 1 123 ? 19.50526 12.89629  9.02272  1.000 29.55431 ? 502 PRO A N   1 
ATOM   997  C  CA  . PRO A 1 123 ? 19.14170 11.48580  8.85844  1.000 27.12276 ? 502 PRO A CA  1 
ATOM   998  C  C   . PRO A 1 123 ? 17.62652 11.34088  8.84442  1.000 26.41355 ? 502 PRO A C   1 
ATOM   999  O  O   . PRO A 1 123 ? 16.88415 12.28304  9.11897  1.000 24.46422 ? 502 PRO A O   1 
ATOM   1000 C  CB  . PRO A 1 123 ? 19.76200 10.81144  10.08636 1.000 26.62419 ? 502 PRO A CB  1 
ATOM   1001 C  CG  . PRO A 1 123 ? 20.75477 11.79543  10.61866 1.000 31.86470 ? 502 PRO A CG  1 
ATOM   1002 C  CD  . PRO A 1 123 ? 20.18652 13.13566  10.30438 1.000 29.24247 ? 502 PRO A CD  1 
ATOM   1003 N  N   . SER A 1 124 ? 17.15600 10.13807  8.53736  1.000 25.44533 ? 503 SER A N   1 
ATOM   1004 C  CA  . SER A 1 124 ? 15.71793 9.91168   8.48709  1.000 25.25366 ? 503 SER A CA  1 
ATOM   1005 C  C   . SER A 1 124 ? 15.40634 8.48732   8.92528  1.000 23.99701 ? 503 SER A C   1 
ATOM   1006 O  O   . SER A 1 124 ? 16.30228 7.69236   9.21318  1.000 23.42481 ? 503 SER A O   1 
ATOM   1007 C  CB  . SER A 1 124 ? 15.16725 10.17098  7.08282  1.000 26.94322 ? 503 SER A CB  1 
ATOM   1008 O  OG  . SER A 1 124 ? 15.85789 9.38410   6.12215  1.000 27.71208 ? 503 SER A OG  1 
ATOM   1009 N  N   . ILE A 1 125 ? 14.11505 8.17082   8.98456  1.000 22.30818 ? 504 ILE A N   1 
ATOM   1010 C  CA  . ILE A 1 125 ? 13.65487 6.80982   9.25990  1.000 24.03350 ? 504 ILE A CA  1 
ATOM   1011 C  C   . ILE A 1 125 ? 12.61379 6.42995   8.22096  1.000 24.38807 ? 504 ILE A C   1 
ATOM   1012 O  O   . ILE A 1 125 ? 11.65345 7.18036   8.00242  1.000 23.93446 ? 504 ILE A O   1 
ATOM   1013 C  CB  . ILE A 1 125 ? 13.06234 6.66937   10.67369 1.000 24.89542 ? 504 ILE A CB  1 
ATOM   1014 C  CG1 . ILE A 1 125 ? 14.13583 6.87995   11.73640 1.000 24.91498 ? 504 ILE A CG1 1 
ATOM   1015 C  CG2 . ILE A 1 125 ? 12.40241 5.30007   10.84760 1.000 23.79057 ? 504 ILE A CG2 1 
ATOM   1016 C  CD1 . ILE A 1 125 ? 13.56771 6.84360   13.14949 1.000 27.04285 ? 504 ILE A CD1 1 
ATOM   1017 N  N   . CYS A 1 126 ? 12.79878 5.26536   7.58728  1.000 27.91483 ? 505 CYS A N   1 
ATOM   1018 C  CA  . CYS A 1 126 ? 11.78826 4.68280   6.71355  1.000 23.13531 ? 505 CYS A CA  1 
ATOM   1019 C  C   . CYS A 1 126 ? 10.99781 3.60885   7.43513  1.000 26.21080 ? 505 CYS A C   1 
ATOM   1020 O  O   . CYS A 1 126 ? 11.48821 2.94724   8.35558  1.000 24.55816 ? 505 CYS A O   1 
ATOM   1021 C  CB  . CYS A 1 126 ? 12.36587 4.05078   5.45112  1.000 28.64182 ? 505 CYS A CB  1 
ATOM   1022 S  SG  . CYS A 1 126 ? 13.52793 5.04553   4.53997  1.000 39.71397 ? 505 CYS A SG  1 
ATOM   1023 N  N   . LYS A 1 127 ? 9.77150  3.41641   6.95638  1.000 24.06399 ? 506 LYS A N   1 
ATOM   1024 C  CA  . LYS A 1 127 ? 8.84939  2.41874   7.46512  1.000 26.55944 ? 506 LYS A CA  1 
ATOM   1025 C  C   . LYS A 1 127 ? 8.28034  1.63431   6.29483  1.000 29.14508 ? 506 LYS A C   1 
ATOM   1026 O  O   . LYS A 1 127 ? 7.98815  2.20058   5.23531  1.000 26.85612 ? 506 LYS A O   1 
ATOM   1027 C  CB  . LYS A 1 127 ? 7.73039  3.08340   8.26279  1.000 23.29350 ? 506 LYS A CB  1 
ATOM   1028 C  CG  . LYS A 1 127 ? 6.71541  2.14518   8.86218  1.000 26.74354 ? 506 LYS A CG  1 
ATOM   1029 C  CD  . LYS A 1 127 ? 5.73134  2.97938   9.66728  1.000 25.70968 ? 506 LYS A CD  1 
ATOM   1030 C  CE  . LYS A 1 127 ? 4.40335  2.30147   9.86005  1.000 30.39675 ? 506 LYS A CE  1 
ATOM   1031 N  NZ  . LYS A 1 127 ? 3.55439  3.14372   10.76584 1.000 27.41952 ? 506 LYS A NZ  1 
ATOM   1032 N  N   . LYS A 1 128 ? 8.10885  0.33454   6.49847  1.000 27.12885 ? 507 LYS A N   1 
ATOM   1033 C  CA  . LYS A 1 128 ? 7.66326  -0.54750  5.43937  1.000 31.46891 ? 507 LYS A CA  1 
ATOM   1034 C  C   . LYS A 1 128 ? 6.62990  -1.54735  5.97507  1.000 34.71545 ? 507 LYS A C   1 
ATOM   1035 O  O   . LYS A 1 128 ? 6.67714  -1.93858  7.14126  1.000 33.72632 ? 507 LYS A O   1 
ATOM   1036 C  CB  . LYS A 1 128 ? 8.87512  -1.26877  4.84062  1.000 36.40114 ? 507 LYS A CB  1 
ATOM   1037 C  CG  . LYS A 1 128 ? 8.60588  -2.03474  3.57524  1.000 42.16558 ? 507 LYS A CG  1 
ATOM   1038 C  CD  . LYS A 1 128 ? 9.91349  -2.43344  2.90981  1.000 44.23293 ? 507 LYS A CD  1 
ATOM   1039 C  CE  . LYS A 1 128 ? 9.63841  -3.29990  1.69408  1.000 52.33618 ? 507 LYS A CE  1 
ATOM   1040 N  NZ  . LYS A 1 128 ? 10.87711 -3.67999  0.96607  1.000 55.95419 ? 507 LYS A NZ  1 
ATOM   1041 O  OXT . LYS A 1 128 ? 5.72016  -1.98524  5.27029  1.000 37.63505 ? 507 LYS A OXT 1 
HETATM 1042 CA CA  . CA  B 2 .   ? 4.43616  24.91948  7.72032  1.000 30.61405 ? 601 CA  A CA  1 
HETATM 1043 CA CA  . CA  C 2 .   ? 9.68454  24.84577  14.28465 1.000 29.47116 ? 602 CA  A CA  1 
HETATM 1044 C  C1  A MFU D 3 .   ? 12.51219 26.90136  17.09290 0.500 32.73081 ? 603 MFU A C1  1 
HETATM 1045 C  C1  B MFU D 3 .   ? 13.07178 28.54565  15.16522 0.500 34.36043 ? 603 MFU A C1  1 
HETATM 1046 C  C2  A MFU D 3 .   ? 12.09883 25.81011  16.12409 0.500 32.34169 ? 603 MFU A C2  1 
HETATM 1047 C  C2  B MFU D 3 .   ? 12.56851 27.38873  14.30984 0.500 33.40194 ? 603 MFU A C2  1 
HETATM 1048 C  C3  A MFU D 3 .   ? 12.63569 26.11131  14.77756 0.500 32.72320 ? 603 MFU A C3  1 
HETATM 1049 C  C3  B MFU D 3 .   ? 12.78729 26.06176  14.93456 0.500 32.62480 ? 603 MFU A C3  1 
HETATM 1050 C  C4  A MFU D 3 .   ? 14.13467 26.21920  14.79077 0.500 32.77980 ? 603 MFU A C4  1 
HETATM 1051 C  C4  B MFU D 3 .   ? 12.22282 26.00817  16.31869 0.500 32.71270 ? 603 MFU A C4  1 
HETATM 1052 C  C5  A MFU D 3 .   ? 14.61488 27.26527  15.79400 0.500 33.84226 ? 603 MFU A C5  1 
HETATM 1053 C  C5  B MFU D 3 .   ? 12.79785 27.13610  17.18203 0.500 32.30062 ? 603 MFU A C5  1 
HETATM 1054 C  C6  A MFU D 3 .   ? 16.11082 27.18918  15.92140 0.500 33.82415 ? 603 MFU A C6  1 
HETATM 1055 C  C6  B MFU D 3 .   ? 12.16246 27.10615  18.53816 0.500 32.70643 ? 603 MFU A C6  1 
HETATM 1056 O  O1  A MFU D 3 .   ? 11.90949 28.03752  16.65715 0.500 32.29474 ? 603 MFU A O1  1 
HETATM 1057 O  O1  B MFU D 3 .   ? 14.43633 28.59037  15.14510 0.500 33.50247 ? 603 MFU A O1  1 
HETATM 1058 O  O2  A MFU D 3 .   ? 10.65909 25.79728  16.06411 0.500 30.75508 ? 603 MFU A O2  1 
HETATM 1059 O  O2  B MFU D 3 .   ? 13.21583 27.41642  13.01853 0.500 35.32383 ? 603 MFU A O2  1 
HETATM 1060 O  O3  A MFU D 3 .   ? 12.22157 25.07622  13.84765 0.500 31.89373 ? 603 MFU A O3  1 
HETATM 1061 O  O3  B MFU D 3 .   ? 12.14044 25.06060  14.10730 0.500 31.86832 ? 603 MFU A O3  1 
HETATM 1062 O  O4  A MFU D 3 .   ? 14.69817 24.96068  15.15354 0.500 31.66678 ? 603 MFU A O4  1 
HETATM 1063 O  O4  B MFU D 3 .   ? 10.79952 26.13795  16.25022 0.500 30.94590 ? 603 MFU A O4  1 
HETATM 1064 O  O5  A MFU D 3 .   ? 14.00243 27.08519  17.12576 0.500 34.07401 ? 603 MFU A O5  1 
HETATM 1065 O  O5  B MFU D 3 .   ? 12.57362 28.46233  16.58125 0.500 33.25652 ? 603 MFU A O5  1 
HETATM 1066 C  CM  A MFU D 3 .   ? 12.16344 29.18190  17.43882 0.500 32.92069 ? 603 MFU A CM  1 
HETATM 1067 C  CM  B MFU D 3 .   ? 14.95388 29.89276  15.30165 0.500 34.30220 ? 603 MFU A CM  1 
HETATM 1068 O  O   . HOH E 4 .   ? 7.50966  1.22892   25.03976 1.000 45.60210 ? 701 HOH A O   1 
HETATM 1069 O  O   . HOH E 4 .   ? 1.38008  12.83572  22.61545 1.000 44.19902 ? 702 HOH A O   1 
HETATM 1070 O  O   . HOH E 4 .   ? -1.10337 19.60983  4.63566  1.000 33.57258 ? 703 HOH A O   1 
HETATM 1071 O  O   . HOH E 4 .   ? 14.50254 23.77041  12.88009 1.000 33.83554 ? 704 HOH A O   1 
HETATM 1072 O  O   . HOH E 4 .   ? 1.36819  21.68237  19.47929 1.000 32.22494 ? 705 HOH A O   1 
HETATM 1073 O  O   . HOH E 4 .   ? 3.66977  5.47441   0.86282  1.000 35.97496 ? 706 HOH A O   1 
HETATM 1074 O  O   . HOH E 4 .   ? -0.23853 9.67001   13.92105 1.000 27.68960 ? 707 HOH A O   1 
HETATM 1075 O  O   . HOH E 4 .   ? 4.24886  28.49446  18.57156 1.000 37.82864 ? 708 HOH A O   1 
HETATM 1076 O  O   . HOH E 4 .   ? 9.49871  25.23922  20.49824 1.000 31.22404 ? 709 HOH A O   1 
HETATM 1077 O  O   . HOH E 4 .   ? 2.03828  -0.08779  15.73451 1.000 36.32453 ? 710 HOH A O   1 
HETATM 1078 O  O   . HOH E 4 .   ? 18.02214 -5.24044  3.21439  1.000 62.70362 ? 711 HOH A O   1 
HETATM 1079 O  O   . HOH E 4 .   ? 16.60733 8.63278   21.16498 1.000 39.44232 ? 712 HOH A O   1 
HETATM 1080 O  O   . HOH E 4 .   ? 5.40445  5.31327   6.56010  1.000 27.35952 ? 713 HOH A O   1 
HETATM 1081 O  O   . HOH E 4 .   ? 18.96702 2.30747   14.27589 1.000 35.25041 ? 714 HOH A O   1 
HETATM 1082 O  O   . HOH E 4 .   ? 18.18780 12.82965  21.37863 1.000 33.90130 ? 715 HOH A O   1 
HETATM 1083 O  O   . HOH E 4 .   ? 14.51461 -3.93262  17.49505 1.000 40.83187 ? 716 HOH A O   1 
HETATM 1084 O  O   . HOH E 4 .   ? 14.07367 20.61011  0.35826  1.000 36.90568 ? 717 HOH A O   1 
HETATM 1085 O  O   . HOH E 4 .   ? 20.94747 14.67233  13.65125 1.000 32.38605 ? 718 HOH A O   1 
HETATM 1086 O  O   . HOH E 4 .   ? 12.70284 -5.33407  16.19361 1.000 33.50070 ? 719 HOH A O   1 
HETATM 1087 O  O   . HOH E 4 .   ? 0.91756  18.14050  3.64062  1.000 31.91655 ? 720 HOH A O   1 
HETATM 1088 O  O   . HOH E 4 .   ? -2.84135 6.58520   19.08852 1.000 30.66861 ? 721 HOH A O   1 
HETATM 1089 O  O   . HOH E 4 .   ? 1.30250  2.56218   16.34644 1.000 29.73409 ? 722 HOH A O   1 
HETATM 1090 O  O   . HOH E 4 .   ? 12.48558 15.18494  22.77451 1.000 30.93337 ? 723 HOH A O   1 
HETATM 1091 O  O   . HOH E 4 .   ? 25.41952 12.21198  5.11894  1.000 40.53234 ? 724 HOH A O   1 
HETATM 1092 O  O   . HOH E 4 .   ? 5.38052  -12.75839 9.60761  1.000 42.69484 ? 725 HOH A O   1 
HETATM 1093 O  O   . HOH E 4 .   ? 5.35729  3.10628   4.96945  1.000 29.46081 ? 726 HOH A O   1 
HETATM 1094 O  O   . HOH E 4 .   ? 21.93535 11.68063  21.90131 1.000 37.88713 ? 727 HOH A O   1 
HETATM 1095 O  O   . HOH E 4 .   ? 20.39183 1.47131   9.78943  1.000 44.09372 ? 728 HOH A O   1 
HETATM 1096 O  O   . HOH E 4 .   ? 3.66983  -0.57404  13.58955 1.000 30.58376 ? 729 HOH A O   1 
HETATM 1097 O  O   . HOH E 4 .   ? 0.57440  -1.60447  13.57021 1.000 38.42455 ? 730 HOH A O   1 
HETATM 1098 O  O   . HOH E 4 .   ? 4.71557  9.19449   6.33829  1.000 22.25828 ? 731 HOH A O   1 
HETATM 1099 O  O   . HOH E 4 .   ? -0.75458 6.39850   22.10804 1.000 28.38387 ? 732 HOH A O   1 
HETATM 1100 O  O   . HOH E 4 .   ? 18.11130 10.62349  4.90478  1.000 31.22433 ? 733 HOH A O   1 
HETATM 1101 O  O   . HOH E 4 .   ? 4.93110  9.39350   -0.54219 1.000 41.85379 ? 734 HOH A O   1 
HETATM 1102 O  O   . HOH E 4 .   ? 5.96424  -6.16154  17.69412 1.000 32.23626 ? 735 HOH A O   1 
HETATM 1103 O  O   . HOH E 4 .   ? 6.72536  0.15823   22.76505 1.000 33.02794 ? 736 HOH A O   1 
HETATM 1104 O  O   . HOH E 4 .   ? 11.68779 -4.98718  5.18468  1.000 45.75963 ? 737 HOH A O   1 
HETATM 1105 O  O   . HOH E 4 .   ? -0.51421 23.48783  13.10330 1.000 36.63249 ? 738 HOH A O   1 
HETATM 1106 O  O   . HOH E 4 .   ? 11.51572 21.95762  23.22287 1.000 33.53530 ? 739 HOH A O   1 
HETATM 1107 O  O   . HOH E 4 .   ? 4.18401  24.53765  9.94202  1.000 31.56863 ? 740 HOH A O   1 
HETATM 1108 O  O   . HOH E 4 .   ? 20.77765 4.85232   16.02751 1.000 43.88667 ? 741 HOH A O   1 
HETATM 1109 O  O   . HOH E 4 .   ? 1.92431  14.26777  2.79266  1.000 31.19120 ? 742 HOH A O   1 
HETATM 1110 O  O   . HOH E 4 .   ? 1.37591  16.96316  20.70182 1.000 28.17115 ? 743 HOH A O   1 
HETATM 1111 O  O   . HOH E 4 .   ? 17.98916 0.92403   11.81272 1.000 34.49734 ? 744 HOH A O   1 
HETATM 1112 O  O   . HOH E 4 .   ? -0.98169 18.96916  15.18384 1.000 31.51846 ? 745 HOH A O   1 
HETATM 1113 O  O   . HOH E 4 .   ? 1.67483  1.36123   12.24998 1.000 44.49243 ? 746 HOH A O   1 
HETATM 1114 O  O   . HOH E 4 .   ? 11.84081 22.58935  18.35887 1.000 29.03124 ? 747 HOH A O   1 
HETATM 1115 O  O   . HOH E 4 .   ? 22.13620 3.99235   7.00596  1.000 43.42855 ? 748 HOH A O   1 
HETATM 1116 O  O   . HOH E 4 .   ? 8.13113  -7.58382  5.04916  1.000 64.27761 ? 749 HOH A O   1 
HETATM 1117 O  O   . HOH E 4 .   ? -1.93021 19.71046  12.17671 1.000 35.22592 ? 750 HOH A O   1 
HETATM 1118 O  O   . HOH E 4 .   ? 0.56572  -1.02647  21.32257 1.000 38.15883 ? 751 HOH A O   1 
HETATM 1119 O  O   . HOH E 4 .   ? 3.05492  19.46816  23.54361 1.000 43.30587 ? 752 HOH A O   1 
HETATM 1120 O  O   . HOH E 4 .   ? 23.36074 13.53460  16.59858 1.000 38.80033 ? 753 HOH A O   1 
HETATM 1121 O  O   . HOH E 4 .   ? -1.38645 12.18953  20.92310 1.000 33.05230 ? 754 HOH A O   1 
HETATM 1122 O  O   . HOH E 4 .   ? 1.80644  15.80167  23.09765 1.000 38.75825 ? 755 HOH A O   1 
HETATM 1123 O  O   . HOH E 4 .   ? 21.45306 6.37143   4.29814  1.000 37.64727 ? 756 HOH A O   1 
HETATM 1124 O  O   . HOH E 4 .   ? 18.76304 14.93659  -5.46983 1.000 58.09610 ? 757 HOH A O   1 
HETATM 1125 O  O   . HOH E 4 .   ? 2.03015  23.01800  22.18038 1.000 55.10176 ? 758 HOH A O   1 
HETATM 1126 O  O   . HOH E 4 .   ? 15.69985 23.52189  18.06995 1.000 57.02449 ? 759 HOH A O   1 
HETATM 1127 O  O   . HOH E 4 .   ? 11.77545 23.51695  20.90067 1.000 33.27541 ? 760 HOH A O   1 
HETATM 1128 O  O   . HOH E 4 .   ? 1.86172  25.52717  11.44508 1.000 37.47223 ? 761 HOH A O   1 
HETATM 1129 O  O   . HOH E 4 .   ? 14.07701 25.31751  20.77035 1.000 45.68504 ? 762 HOH A O   1 
HETATM 1130 O  O   . HOH E 4 .   ? 23.09421 13.17444  14.07153 1.000 47.05832 ? 763 HOH A O   1 
HETATM 1131 O  O   . HOH E 4 .   ? 3.96322  3.20969   2.73163  1.000 36.09034 ? 764 HOH A O   1 
HETATM 1132 O  O   . HOH E 4 .   ? -0.58958 -3.37262  22.80686 1.000 29.62074 ? 765 HOH A O   1 
HETATM 1133 O  O   . HOH E 4 .   ? 13.82998 22.73577  24.52147 1.000 44.22863 ? 766 HOH A O   1 
HETATM 1134 O  O   . HOH E 4 .   ? 15.40276 24.11811  22.94908 1.000 36.48809 ? 767 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   . ALA A 1   ? 0.92207 0.56515 1.21005 -0.05507 0.08977  -0.15654 380 ALA A N   
2    C  CA  . ALA A 1   ? 0.95563 0.62469 1.21360 -0.06940 0.08372  -0.16428 380 ALA A CA  
3    C  C   . ALA A 1   ? 0.85651 0.55144 1.10380 -0.06000 0.08928  -0.17240 380 ALA A C   
4    O  O   . ALA A 1   ? 0.90217 0.59461 1.16476 -0.04448 0.10020  -0.17756 380 ALA A O   
5    C  CB  . ALA A 1   ? 0.95035 0.63017 1.20691 -0.07778 0.07131  -0.13860 380 ALA A CB  
6    N  N   . VAL A 2   ? 0.78222 0.50295 1.00543 -0.06968 0.08225  -0.17302 381 VAL A N   
7    C  CA  . VAL A 2   ? 0.70982 0.45395 0.91940 -0.06298 0.08765  -0.18071 381 VAL A CA  
8    C  C   . VAL A 2   ? 0.68291 0.43928 0.91285 -0.04828 0.08459  -0.15605 381 VAL A C   
9    O  O   . VAL A 2   ? 0.66231 0.41758 0.90223 -0.04896 0.07416  -0.13241 381 VAL A O   
10   C  CB  . VAL A 2   ? 0.69137 0.45740 0.86503 -0.07948 0.08017  -0.19207 381 VAL A CB  
11   C  CG1 . VAL A 2   ? 0.69281 0.44710 0.85021 -0.09702 0.07500  -0.20861 381 VAL A CG1 
12   C  CG2 . VAL A 2   ? 0.57258 0.36016 0.74640 -0.08333 0.06774  -0.17070 381 VAL A CG2 
13   N  N   . GLU A 3   ? 0.68142 0.44972 0.91675 -0.03543 0.09401  -0.16116 382 GLU A N   
14   C  CA  . GLU A 3   ? 0.65401 0.43479 0.91167 -0.02047 0.09046  -0.13986 382 GLU A CA  
15   C  C   . GLU A 3   ? 0.62827 0.43396 0.87059 -0.01877 0.09621  -0.14859 382 GLU A C   
16   O  O   . GLU A 3   ? 0.64450 0.45558 0.85964 -0.02677 0.10552  -0.17103 382 GLU A O   
17   C  CB  . GLU A 3   ? 0.68685 0.45608 0.98216 -0.00299 0.09612  -0.13284 382 GLU A CB  
18   C  CG  . GLU A 3   ? 0.73759 0.49948 1.03615 0.00026  0.11455  -0.15854 382 GLU A CG  
19   C  CD  . GLU A 3   ? 0.82191 0.56271 1.15690 0.01220  0.11849  -0.15385 382 GLU A CD  
20   O  OE1 . GLU A 3   ? 0.84746 0.58579 1.20874 0.02191  0.10678  -0.12812 382 GLU A OE1 
21   O  OE2 . GLU A 3   ? 0.93178 0.65753 1.26719 0.01152  0.13266  -0.17570 382 GLU A OE2 
22   N  N   . CYS A 4   ? 0.60532 0.43026 0.85857 -0.00915 0.08822  -0.12710 383 CYS A N   
23   C  CA  . CYS A 4   ? 0.57129 0.42530 0.81319 -0.00508 0.09301  -0.12891 383 CYS A CA  
24   C  C   . CYS A 4   ? 0.55297 0.40229 0.82106 0.00668  0.11350  -0.14592 383 CYS A C   
25   O  O   . CYS A 4   ? 0.54214 0.37674 0.84182 0.01606  0.11697  -0.14391 383 CYS A O   
26   C  CB  . CYS A 4   ? 0.46353 0.33898 0.71298 0.00186  0.07808  -0.10137 383 CYS A CB  
27   S  SG  . CYS A 4   ? 0.51693 0.39825 0.73775 -0.01010 0.05871  -0.08220 383 CYS A SG  
28   N  N   . GLU A 5   ? 0.53517 0.40484 0.78433 0.00500  0.12519  -0.15698 384 GLU A N   
29   C  CA  . GLU A 5   ? 0.54797 0.42240 0.82219 0.01583  0.14548  -0.16798 384 GLU A CA  
30   C  C   . GLU A 5   ? 0.47756 0.36503 0.80114 0.03174  0.13766  -0.14526 384 GLU A C   
31   O  O   . GLU A 5   ? 0.45181 0.34652 0.77983 0.03319  0.11815  -0.12366 384 GLU A O   
32   C  CB  . GLU A 5   ? 0.58596 0.47947 0.82823 0.00950  0.16060  -0.18145 384 GLU A CB  
33   C  CG  . GLU A 5   ? 0.65202 0.54259 0.83591 -0.00876 0.15614  -0.19316 384 GLU A CG  
34   C  CD  . GLU A 5   ? 0.70088 0.61692 0.84988 -0.01518 0.15982  -0.19033 384 GLU A CD  
35   O  OE1 . GLU A 5   ? 0.74427 0.66885 0.90114 -0.00995 0.18153  -0.19893 384 GLU A OE1 
36   O  OE2 . GLU A 5   ? 0.74737 0.67484 0.86417 -0.02508 0.14189  -0.17831 384 GLU A OE2 
37   N  N   . PRO A 6   ? 0.49070 0.38335 0.84822 0.04191  0.14958  -0.14750 385 PRO A N   
38   C  CA  . PRO A 6   ? 0.48137 0.39152 0.88553 0.05498  0.13934  -0.12580 385 PRO A CA  
39   C  C   . PRO A 6   ? 0.46154 0.39946 0.86067 0.05362  0.13309  -0.11524 385 PRO A C   
40   O  O   . PRO A 6   ? 0.47617 0.42526 0.84511 0.04553  0.14624  -0.12768 385 PRO A O   
41   C  CB  . PRO A 6   ? 0.46139 0.37538 0.89628 0.06253  0.15878  -0.13665 385 PRO A CB  
42   C  CG  . PRO A 6   ? 0.52827 0.41543 0.94047 0.05677  0.17293  -0.15898 385 PRO A CG  
43   C  CD  . PRO A 6   ? 0.51591 0.39774 0.87212 0.04146  0.17136  -0.16959 385 PRO A CD  
44   N  N   . SER A 7   ? 0.43771 0.38597 0.86312 0.06053  0.11139  -0.09113 386 SER A N   
45   C  CA  . SER A 7   ? 0.42352 0.39754 0.84946 0.05960  0.09943  -0.07699 386 SER A CA  
46   C  C   . SER A 7   ? 0.38927 0.36269 0.75573 0.04432  0.08661  -0.07146 386 SER A C   
47   O  O   . SER A 7   ? 0.39060 0.38373 0.74532 0.03975  0.07591  -0.05982 386 SER A O   
48   C  CB  . SER A 7   ? 0.49583 0.49638 0.93200 0.05829  0.11687  -0.08461 386 SER A CB  
49   O  OG  . SER A 7   ? 0.52875 0.52760 0.92273 0.04815  0.13704  -0.10390 386 SER A OG  
50   N  N   . TRP A 8   ? 0.37056 0.32262 0.70307 0.03616  0.08759  -0.08000 387 TRP A N   
51   C  CA  . TRP A 8   ? 0.37639 0.32778 0.66381 0.02387  0.07299  -0.07176 387 TRP A CA  
52   C  C   . TRP A 8   ? 0.33180 0.26592 0.62455 0.02553  0.05540  -0.05518 387 TRP A C   
53   O  O   . TRP A 8   ? 0.36565 0.27708 0.67869 0.03027  0.05887  -0.05855 387 TRP A O   
54   C  CB  . TRP A 8   ? 0.37669 0.31971 0.62480 0.01175  0.08366  -0.09071 387 TRP A CB  
55   C  CG  . TRP A 8   ? 0.40367 0.36240 0.63208 0.00712  0.09876  -0.10356 387 TRP A CG  
56   C  CD1 . TRP A 8   ? 0.47538 0.43671 0.72034 0.01215  0.12081  -0.11906 387 TRP A CD1 
57   C  CD2 . TRP A 8   ? 0.39454 0.36738 0.58251 -0.00349 0.09431  -0.10093 387 TRP A CD2 
58   N  NE1 . TRP A 8   ? 0.50166 0.47728 0.71416 0.00388  0.13070  -0.12524 387 TRP A NE1 
59   C  CE2 . TRP A 8   ? 0.44920 0.43136 0.62710 -0.00538 0.11321  -0.11334 387 TRP A CE2 
60   C  CE3 . TRP A 8   ? 0.37442 0.35263 0.53567 -0.01093 0.07723  -0.08862 387 TRP A CE3 
61   C  CZ2 . TRP A 8   ? 0.42378 0.41840 0.56356 -0.01480 0.11313  -0.11145 387 TRP A CZ2 
62   C  CZ3 . TRP A 8   ? 0.35366 0.34518 0.48283 -0.01861 0.07710  -0.08813 387 TRP A CZ3 
63   C  CH2 . TRP A 8   ? 0.37764 0.37635 0.49509 -0.02067 0.09369  -0.09827 387 TRP A CH2 
64   N  N   . GLN A 9   ? 0.26385 0.20647 0.53737 0.02135  0.03807  -0.03747 388 GLN A N   
65   C  CA  . GLN A 9   ? 0.29442 0.22194 0.56778 0.02213  0.02218  -0.01902 388 GLN A CA  
66   C  C   . GLN A 9   ? 0.29272 0.21015 0.53105 0.00959  0.02168  -0.02061 388 GLN A C   
67   O  O   . GLN A 9   ? 0.28012 0.21216 0.49023 0.00142  0.02242  -0.02491 388 GLN A O   
68   C  CB  . GLN A 9   ? 0.24912 0.19085 0.52090 0.02460  0.00422  0.00040  388 GLN A CB  
69   C  CG  . GLN A 9   ? 0.34733 0.30373 0.66108 0.03593  0.00204  0.00303  388 GLN A CG  
70   C  CD  . GLN A 9   ? 0.36540 0.33376 0.68028 0.03728  -0.01972 0.02189  388 GLN A CD  
71   O  OE1 . GLN A 9   ? 0.37857 0.33452 0.67770 0.03599  -0.03589 0.03834  388 GLN A OE1 
72   N  NE2 . GLN A 9   ? 0.38216 0.37405 0.71406 0.03851  -0.01998 0.01933  388 GLN A NE2 
73   N  N   . PRO A 10  ? 0.30359 0.19702 0.54667 0.00776  0.02047  -0.01631 389 PRO A N   
74   C  CA  . PRO A 10  ? 0.33025 0.21638 0.54679 -0.00559 0.02087  -0.01759 389 PRO A CA  
75   C  C   . PRO A 10  ? 0.34714 0.23780 0.54219 -0.00983 0.00913  0.00267  389 PRO A C   
76   O  O   . PRO A 10  ? 0.34265 0.22799 0.54274 -0.00358 -0.00144 0.02091  389 PRO A O   
77   C  CB  . PRO A 10  ? 0.35810 0.21404 0.59394 -0.00616 0.02596  -0.02085 389 PRO A CB  
78   C  CG  . PRO A 10  ? 0.37074 0.21615 0.64007 0.00898  0.02107  -0.00862 389 PRO A CG  
79   C  CD  . PRO A 10  ? 0.31126 0.18229 0.59034 0.01776  0.02175  -0.01318 389 PRO A CD  
80   N  N   . PHE A 11  ? 0.32117 0.22180 0.49177 -0.02068 0.01103  -0.00088 390 PHE A N   
81   C  CA  . PHE A 11  ? 0.30875 0.21178 0.45871 -0.02578 0.00508  0.01519  390 PHE A CA  
82   C  C   . PHE A 11  ? 0.30626 0.21654 0.44402 -0.03803 0.01102  0.00792  390 PHE A C   
83   O  O   . PHE A 11  ? 0.30037 0.22842 0.43191 -0.04055 0.01325  -0.00482 390 PHE A O   
84   C  CB  . PHE A 11  ? 0.30488 0.22535 0.44033 -0.02105 -0.00231 0.02211  390 PHE A CB  
85   C  CG  . PHE A 11  ? 0.31834 0.24118 0.42807 -0.02678 -0.00471 0.03384  390 PHE A CG  
86   C  CD1 . PHE A 11  ? 0.34020 0.24722 0.43999 -0.02701 -0.01049 0.05177  390 PHE A CD1 
87   C  CD2 . PHE A 11  ? 0.32134 0.26144 0.41633 -0.03160 -0.00036 0.02729  390 PHE A CD2 
88   C  CE1 . PHE A 11  ? 0.35396 0.26227 0.42582 -0.03292 -0.00909 0.06072  390 PHE A CE1 
89   C  CE2 . PHE A 11  ? 0.31538 0.25753 0.38968 -0.03581 0.00107  0.03576  390 PHE A CE2 
90   C  CZ  . PHE A 11  ? 0.32180 0.24790 0.38263 -0.03698 -0.00188 0.05145  390 PHE A CZ  
91   N  N   . GLN A 12  ? 0.31669 0.21446 0.45222 -0.04579 0.01287  0.01795  391 GLN A N   
92   C  CA  . GLN A 12  ? 0.28907 0.19660 0.41972 -0.05820 0.01824  0.01426  391 GLN A CA  
93   C  C   . GLN A 12  ? 0.30669 0.22674 0.44362 -0.06327 0.01985  -0.00657 391 GLN A C   
94   O  O   . GLN A 12  ? 0.34200 0.28466 0.47122 -0.06629 0.01871  -0.01170 391 GLN A O   
95   C  CB  . GLN A 12  ? 0.31146 0.23645 0.42286 -0.05854 0.01834  0.02352  391 GLN A CB  
96   C  CG  . GLN A 12  ? 0.33432 0.24468 0.43096 -0.05761 0.01783  0.04353  391 GLN A CG  
97   C  CD  . GLN A 12  ? 0.35197 0.27574 0.42795 -0.06058 0.02294  0.04972  391 GLN A CD  
98   O  OE1 . GLN A 12  ? 0.34607 0.29139 0.42286 -0.06075 0.02557  0.04001  391 GLN A OE1 
99   N  NE2 . GLN A 12  ? 0.37437 0.28397 0.43068 -0.06263 0.02486  0.06637  391 GLN A NE2 
100  N  N   . GLY A 13  ? 0.30348 0.20671 0.45376 -0.06406 0.02212  -0.01854 392 GLY A N   
101  C  CA  . GLY A 13  ? 0.30971 0.21821 0.46120 -0.07219 0.02351  -0.03936 392 GLY A CA  
102  C  C   . GLY A 13  ? 0.31583 0.23519 0.45776 -0.06543 0.02391  -0.05305 392 GLY A C   
103  O  O   . GLY A 13  ? 0.31356 0.23202 0.45124 -0.07214 0.02570  -0.07183 392 GLY A O   
104  N  N   . HIS A 14  ? 0.30733 0.23577 0.44444 -0.05371 0.02267  -0.04458 393 HIS A N   
105  C  CA  . HIS A 14  ? 0.28977 0.23130 0.41738 -0.04886 0.02475  -0.05484 393 HIS A CA  
106  C  C   . HIS A 14  ? 0.32044 0.25449 0.46253 -0.03628 0.02871  -0.05250 393 HIS A C   
107  O  O   . HIS A 14  ? 0.26004 0.18167 0.41736 -0.03017 0.02582  -0.03981 393 HIS A O   
108  C  CB  . HIS A 14  ? 0.32123 0.28689 0.43237 -0.04872 0.01912  -0.04747 393 HIS A CB  
109  C  CG  . HIS A 14  ? 0.36828 0.34627 0.47190 -0.05940 0.01449  -0.05009 393 HIS A CG  
110  N  ND1 . HIS A 14  ? 0.41144 0.40085 0.50188 -0.06548 0.01182  -0.06198 393 HIS A ND1 
111  C  CD2 . HIS A 14  ? 0.42113 0.40324 0.53080 -0.06539 0.01183  -0.04173 393 HIS A CD2 
112  C  CE1 . HIS A 14  ? 0.45865 0.46045 0.55114 -0.07409 0.00500  -0.06029 393 HIS A CE1 
113  N  NE2 . HIS A 14  ? 0.44759 0.44602 0.55415 -0.07412 0.00654  -0.04869 393 HIS A NE2 
114  N  N   . CYS A 15  ? 0.28381 0.22636 0.42186 -0.03300 0.03524  -0.06406 394 CYS A N   
115  C  CA  . CYS A 15  ? 0.31308 0.25437 0.47085 -0.02153 0.04139  -0.06430 394 CYS A CA  
116  C  C   . CYS A 15  ? 0.28815 0.25102 0.43839 -0.01794 0.03871  -0.05657 394 CYS A C   
117  O  O   . CYS A 15  ? 0.26159 0.23752 0.38842 -0.02403 0.03794  -0.05901 394 CYS A O   
118  C  CB  . CYS A 15  ? 0.32722 0.25930 0.48963 -0.02137 0.05638  -0.08607 394 CYS A CB  
119  S  SG  . CYS A 15  ? 0.43366 0.33556 0.60597 -0.02685 0.06060  -0.09913 394 CYS A SG  
120  N  N   . TYR A 16  ? 0.29542 0.26147 0.46791 -0.00835 0.03612  -0.04670 395 TYR A N   
121  C  CA  . TYR A 16  ? 0.25362 0.23776 0.42284 -0.00633 0.03120  -0.03777 395 TYR A CA  
122  C  C   . TYR A 16  ? 0.26003 0.25181 0.45947 0.00197  0.03792  -0.03963 395 TYR A C   
123  O  O   . TYR A 16  ? 0.23680 0.22027 0.46672 0.00999  0.03814  -0.03821 395 TYR A O   
124  C  CB  . TYR A 16  ? 0.22616 0.20996 0.39063 -0.00565 0.01586  -0.02044 395 TYR A CB  
125  C  CG  . TYR A 16  ? 0.23553 0.21548 0.37508 -0.01330 0.01170  -0.01724 395 TYR A CG  
126  C  CD1 . TYR A 16  ? 0.27863 0.24294 0.41983 -0.01627 0.01149  -0.01598 395 TYR A CD1 
127  C  CD2 . TYR A 16  ? 0.24050 0.23234 0.35959 -0.01737 0.00900  -0.01492 395 TYR A CD2 
128  C  CE1 . TYR A 16  ? 0.28281 0.24690 0.40698 -0.02415 0.00964  -0.01280 395 TYR A CE1 
129  C  CE2 . TYR A 16  ? 0.26999 0.26154 0.37368 -0.02319 0.00684  -0.01220 395 TYR A CE2 
130  C  CZ  . TYR A 16  ? 0.27536 0.25474 0.38245 -0.02695 0.00761  -0.01123 395 TYR A CZ  
131  O  OH  . TYR A 16  ? 0.30371 0.28591 0.40126 -0.03351 0.00740  -0.00836 395 TYR A OH  
132  N  N   . ARG A 17  ? 0.26420 0.27228 0.45903 0.00021  0.04318  -0.04110 396 ARG A N   
133  C  CA  . ARG A 17  ? 0.26759 0.28705 0.49615 0.00674  0.05128  -0.04237 396 ARG A CA  
134  C  C   . ARG A 17  ? 0.24352 0.27993 0.47062 0.00369  0.04600  -0.03337 396 ARG A C   
135  O  O   . ARG A 17  ? 0.24378 0.28411 0.44129 -0.00365 0.04867  -0.03413 396 ARG A O   
136  C  CB  . ARG A 17  ? 0.29764 0.31662 0.52842 0.00657  0.07440  -0.06054 396 ARG A CB  
137  C  CG  . ARG A 17  ? 0.35320 0.38435 0.62832 0.01479  0.08670  -0.06306 396 ARG A CG  
138  C  CD  . ARG A 17  ? 0.41830 0.45118 0.68796 0.01281  0.11400  -0.08170 396 ARG A CD  
139  N  NE  . ARG A 17  ? 0.53622 0.58713 0.85133 0.01948  0.12739  -0.08173 396 ARG A NE  
140  C  CZ  . ARG A 17  ? 0.56215 0.61194 0.91742 0.02932  0.14491  -0.09320 396 ARG A CZ  
141  N  NH1 . ARG A 17  ? 0.63104 0.65880 0.98200 0.03293  0.15315  -0.10784 396 ARG A NH1 
142  N  NH2 . ARG A 17  ? 0.57460 0.64467 0.97592 0.03486  0.15385  -0.08990 396 ARG A NH2 
143  N  N   . LEU A 18  ? 0.23551 0.28122 0.49634 0.00897  0.03707  -0.02430 397 LEU A N   
144  C  CA  . LEU A 18  ? 0.24459 0.30633 0.51200 0.00489  0.03403  -0.01830 397 LEU A CA  
145  C  C   . LEU A 18  ? 0.26206 0.33715 0.54767 0.00407  0.05632  -0.02713 397 LEU A C   
146  O  O   . LEU A 18  ? 0.22657 0.30650 0.54820 0.01128  0.06798  -0.03350 397 LEU A O   
147  C  CB  . LEU A 18  ? 0.23779 0.30650 0.53613 0.00884  0.01452  -0.00647 397 LEU A CB  
148  C  CG  . LEU A 18  ? 0.22307 0.30986 0.54109 0.00393  0.01169  -0.00229 397 LEU A CG  
149  C  CD1 . LEU A 18  ? 0.20392 0.28492 0.48242 -0.00535 0.00503  0.00089  397 LEU A CD1 
150  C  CD2 . LEU A 18  ? 0.23263 0.32992 0.59194 0.00842  -0.00787 0.00721  397 LEU A CD2 
151  N  N   . GLN A 19  ? 0.25252 0.33255 0.51380 -0.00444 0.06379  -0.02702 398 GLN A N   
152  C  CA  . GLN A 19  ? 0.27010 0.36335 0.54472 -0.00764 0.08574  -0.03209 398 GLN A CA  
153  C  C   . GLN A 19  ? 0.25383 0.36309 0.55979 -0.01084 0.07860  -0.02183 398 GLN A C   
154  O  O   . GLN A 19  ? 0.23979 0.34624 0.52503 -0.01790 0.06762  -0.01371 398 GLN A O   
155  C  CB  . GLN A 19  ? 0.30676 0.39375 0.53319 -0.01623 0.09778  -0.03580 398 GLN A CB  
156  C  CG  . GLN A 19  ? 0.32755 0.39946 0.52164 -0.01560 0.10016  -0.04633 398 GLN A CG  
157  C  CD  . GLN A 19  ? 0.40815 0.47658 0.55710 -0.02432 0.11194  -0.05072 398 GLN A CD  
158  O  OE1 . GLN A 19  ? 0.46947 0.53342 0.60458 -0.02565 0.12913  -0.06481 398 GLN A OE1 
159  N  NE2 . GLN A 19  ? 0.37213 0.44063 0.49573 -0.03034 0.10185  -0.03884 398 GLN A NE2 
160  N  N   . ALA A 20  ? 0.23041 0.35649 0.58996 -0.00578 0.08487  -0.02282 399 ALA A N   
161  C  CA  . ALA A 20  ? 0.20860 0.35172 0.60630 -0.00922 0.07267  -0.01317 399 ALA A CA  
162  C  C   . ALA A 20  ? 0.23674 0.38992 0.63299 -0.02060 0.08857  -0.01102 399 ALA A C   
163  O  O   . ALA A 20  ? 0.25590 0.41599 0.66655 -0.02797 0.07549  -0.00261 399 ALA A O   
164  C  CB  . ALA A 20  ? 0.28403 0.44145 0.73974 0.00048  0.07094  -0.01334 399 ALA A CB  
165  N  N   . GLU A 21  ? 0.25457 0.40693 0.63191 -0.02326 0.11656  -0.01842 400 GLU A N   
166  C  CA  . GLU A 21  ? 0.28357 0.44329 0.65663 -0.03415 0.13439  -0.01444 400 GLU A CA  
167  C  C   . GLU A 21  ? 0.24567 0.39239 0.57982 -0.04404 0.12169  -0.00410 400 GLU A C   
168  O  O   . GLU A 21  ? 0.29719 0.42539 0.58422 -0.04254 0.11190  -0.00436 400 GLU A O   
169  C  CB  . GLU A 21  ? 0.31952 0.47553 0.66561 -0.03473 0.16501  -0.02467 400 GLU A CB  
170  C  CG  . GLU A 21  ? 0.40267 0.56830 0.75679 -0.04089 0.18580  -0.02277 400 GLU A CG  
171  C  CD  . GLU A 21  ? 0.46417 0.62821 0.80943 -0.03609 0.21259  -0.03714 400 GLU A CD  
172  O  OE1 . GLU A 21  ? 0.59328 0.74346 0.90354 -0.03329 0.21798  -0.04779 400 GLU A OE1 
173  O  OE2 . GLU A 21  ? 0.50602 0.68192 0.87958 -0.03554 0.22796  -0.03893 400 GLU A OE2 
174  N  N   . LYS A 22  ? 0.25047 0.40525 0.60519 -0.05391 0.12124  0.00495  401 LYS A N   
175  C  CA  . LYS A 22  ? 0.25886 0.39685 0.57910 -0.06221 0.10880  0.01468  401 LYS A CA  
176  C  C   . LYS A 22  ? 0.28684 0.41480 0.56334 -0.06891 0.12936  0.01896  401 LYS A C   
177  O  O   . LYS A 22  ? 0.27210 0.41059 0.56114 -0.07622 0.15358  0.02124  401 LYS A O   
178  C  CB  . LYS A 22  ? 0.28695 0.43293 0.64509 -0.07138 0.09838  0.02196  401 LYS A CB  
179  C  CG  . LYS A 22  ? 0.27421 0.42559 0.66178 -0.06606 0.07060  0.01941  401 LYS A CG  
180  C  CD  . LYS A 22  ? 0.32057 0.47474 0.73077 -0.07512 0.05735  0.02388  401 LYS A CD  
181  C  CE  . LYS A 22  ? 0.38465 0.54600 0.82100 -0.06997 0.03032  0.02138  401 LYS A CE  
182  N  NZ  . LYS A 22  ? 0.38837 0.54992 0.84069 -0.08028 0.01377  0.02380  401 LYS A NZ  
183  N  N   . ARG A 23  ? 0.30191 0.41039 0.52784 -0.06690 0.11934  0.02124  402 ARG A N   
184  C  CA  . ARG A 23  ? 0.32375 0.42107 0.50244 -0.07256 0.13213  0.02764  402 ARG A CA  
185  C  C   . ARG A 23  ? 0.32662 0.40476 0.47492 -0.07302 0.11238  0.03797  402 ARG A C   
186  O  O   . ARG A 23  ? 0.30135 0.37381 0.45704 -0.06747 0.09153  0.03591  402 ARG A O   
187  C  CB  . ARG A 23  ? 0.32610 0.42147 0.47110 -0.06779 0.14229  0.01681  402 ARG A CB  
188  C  CG  . ARG A 23  ? 0.36022 0.47017 0.53220 -0.06413 0.16267  0.00262  402 ARG A CG  
189  C  CD  . ARG A 23  ? 0.37525 0.47653 0.50803 -0.06010 0.16776  -0.01019 402 ARG A CD  
190  N  NE  . ARG A 23  ? 0.37810 0.48883 0.53643 -0.05492 0.18825  -0.02656 402 ARG A NE  
191  C  CZ  . ARG A 23  ? 0.40619 0.51831 0.59426 -0.04429 0.17981  -0.03681 402 ARG A CZ  
192  N  NH1 . ARG A 23  ? 0.38681 0.49233 0.57910 -0.03894 0.15211  -0.03225 402 ARG A NH1 
193  N  NH2 . ARG A 23  ? 0.42927 0.54815 0.64324 -0.03874 0.20102  -0.05161 402 ARG A NH2 
194  N  N   . SER A 24  ? 0.35230 0.41986 0.46497 -0.07924 0.11998  0.04947  403 SER A N   
195  C  CA  . SER A 24  ? 0.32085 0.37040 0.40357 -0.07715 0.10267  0.05957  403 SER A CA  
196  C  C   . SER A 24  ? 0.33866 0.38646 0.39942 -0.06756 0.08894  0.05064  403 SER A C   
197  O  O   . SER A 24  ? 0.34568 0.40240 0.40516 -0.06417 0.09458  0.03772  403 SER A O   
198  C  CB  . SER A 24  ? 0.37494 0.41443 0.42203 -0.08488 0.11284  0.07559  403 SER A CB  
199  O  OG  . SER A 24  ? 0.41298 0.45668 0.42322 -0.08515 0.12285  0.07052  403 SER A OG  
200  N  N   . TRP A 25  ? 0.30640 0.34193 0.35253 -0.06332 0.07182  0.05756  404 TRP A N   
201  C  CA  . TRP A 25  ? 0.34658 0.38248 0.37660 -0.05553 0.05927  0.05032  404 TRP A CA  
202  C  C   . TRP A 25  ? 0.34509 0.38492 0.34060 -0.05807 0.06606  0.04796  404 TRP A C   
203  O  O   . TRP A 25  ? 0.34126 0.38722 0.33376 -0.05537 0.06646  0.03422  404 TRP A O   
204  C  CB  . TRP A 25  ? 0.30793 0.33217 0.33326 -0.05035 0.04281  0.05882  404 TRP A CB  
205  C  CG  . TRP A 25  ? 0.32295 0.35007 0.34040 -0.04284 0.03046  0.05201  404 TRP A CG  
206  C  CD1 . TRP A 25  ? 0.28213 0.31025 0.31582 -0.03718 0.02296  0.04251  404 TRP A CD1 
207  C  CD2 . TRP A 25  ? 0.31790 0.34765 0.31000 -0.04162 0.02387  0.05561  404 TRP A CD2 
208  N  NE1 . TRP A 25  ? 0.29301 0.32477 0.31588 -0.03279 0.01486  0.03978  404 TRP A NE1 
209  C  CE2 . TRP A 25  ? 0.33056 0.36459 0.33039 -0.03545 0.01396  0.04717  404 TRP A CE2 
210  C  CE3 . TRP A 25  ? 0.34854 0.37787 0.31086 -0.04624 0.02446  0.06586  404 TRP A CE3 
211  C  CZ2 . TRP A 25  ? 0.31054 0.35077 0.29599 -0.03404 0.00440  0.04780  404 TRP A CZ2 
212  C  CZ3 . TRP A 25  ? 0.35790 0.39272 0.30177 -0.04452 0.01217  0.06651  404 TRP A CZ3 
213  C  CH2 . TRP A 25  ? 0.34217 0.38351 0.30091 -0.03859 0.00217  0.05708  404 TRP A CH2 
214  N  N   . GLN A 26  ? 0.35537 0.38978 0.32250 -0.06434 0.07137  0.06124  405 GLN A N   
215  C  CA  . GLN A 26  ? 0.42267 0.45923 0.34869 -0.06868 0.07597  0.05881  405 GLN A CA  
216  C  C   . GLN A 26  ? 0.40810 0.45302 0.33495 -0.07246 0.09730  0.04220  405 GLN A C   
217  O  O   . GLN A 26  ? 0.43180 0.47899 0.33820 -0.07255 0.09806  0.02848  405 GLN A O   
218  C  CB  . GLN A 26  ? 0.43759 0.46513 0.32928 -0.07568 0.07747  0.07919  405 GLN A CB  
219  C  CG  . GLN A 26  ? 0.47805 0.49683 0.36523 -0.07020 0.05507  0.09576  405 GLN A CG  
220  C  CD  . GLN A 26  ? 0.53169 0.53940 0.45011 -0.06791 0.05342  0.10788  405 GLN A CD  
221  O  OE1 . GLN A 26  ? 0.52629 0.53518 0.47332 -0.07074 0.06544  0.10217  405 GLN A OE1 
222  N  NE2 . GLN A 26  ? 0.47362 0.47024 0.38917 -0.06284 0.03769  0.12424  405 GLN A NE2 
223  N  N   . GLU A 27  ? 0.39154 0.44110 0.34504 -0.07581 0.11536  0.04237  406 GLU A N   
224  C  CA  . GLU A 27  ? 0.40000 0.45929 0.36441 -0.07722 0.13782  0.02596  406 GLU A CA  
225  C  C   . GLU A 27  ? 0.36696 0.43116 0.35890 -0.06784 0.13022  0.00848  406 GLU A C   
226  O  O   . GLU A 27  ? 0.39077 0.45689 0.37572 -0.06695 0.14201  -0.00790 406 GLU A O   
227  C  CB  . GLU A 27  ? 0.40449 0.47188 0.40399 -0.08212 0.15711  0.03107  406 GLU A CB  
228  C  CG  . GLU A 27  ? 0.44588 0.50911 0.41473 -0.09398 0.17617  0.04502  406 GLU A CG  
229  C  CD  . GLU A 27  ? 0.54902 0.61774 0.55807 -0.10042 0.18797  0.05641  406 GLU A CD  
230  O  OE1 . GLU A 27  ? 0.49905 0.57402 0.55733 -0.09581 0.17657  0.05398  406 GLU A OE1 
231  O  OE2 . GLU A 27  ? 0.58186 0.64822 0.57194 -0.11143 0.20830  0.06817  406 GLU A OE2 
232  N  N   . SER A 28  ? 0.34144 0.40542 0.36329 -0.06123 0.11161  0.01159  407 SER A N   
233  C  CA  . SER A 28  ? 0.34387 0.40996 0.38763 -0.05300 0.10303  -0.00130 407 SER A CA  
234  C  C   . SER A 28  ? 0.34726 0.40713 0.35862 -0.05210 0.09515  -0.00937 407 SER A C   
235  O  O   . SER A 28  ? 0.35372 0.41329 0.37111 -0.04911 0.09980  -0.02423 407 SER A O   
236  C  CB  . SER A 28  ? 0.31904 0.38366 0.38961 -0.04795 0.08398  0.00512  407 SER A CB  
237  O  OG  . SER A 28  ? 0.31142 0.38176 0.41339 -0.05065 0.08813  0.01135  407 SER A OG  
238  N  N   . LYS A 29  ? 0.35780 0.41249 0.33844 -0.05476 0.08223  0.00060  408 LYS A N   
239  C  CA  . LYS A 29  ? 0.37038 0.42227 0.32301 -0.05576 0.07204  -0.00605 408 LYS A CA  
240  C  C   . LYS A 29  ? 0.40243 0.45291 0.32537 -0.06236 0.08769  -0.01955 408 LYS A C   
241  O  O   . LYS A 29  ? 0.41262 0.46030 0.33004 -0.06245 0.08635  -0.03516 408 LYS A O   
242  C  CB  . LYS A 29  ? 0.37001 0.41985 0.30040 -0.05705 0.05506  0.00962  408 LYS A CB  
243  C  CG  . LYS A 29  ? 0.39532 0.44670 0.30772 -0.05784 0.03929  0.00452  408 LYS A CG  
244  C  CD  . LYS A 29  ? 0.42088 0.47321 0.31568 -0.05825 0.02231  0.02174  408 LYS A CD  
245  C  CE  . LYS A 29  ? 0.47643 0.52549 0.33035 -0.06651 0.02772  0.03076  408 LYS A CE  
246  N  NZ  . LYS A 29  ? 0.60497 0.65528 0.43917 -0.06684 0.00723  0.04826  408 LYS A NZ  
247  N  N   . LYS A 30  ? 0.41484 0.46538 0.31692 -0.06893 0.10411  -0.01446 409 LYS A N   
248  C  CA  . LYS A 30  ? 0.44754 0.49497 0.31418 -0.07628 0.12224  -0.02872 409 LYS A CA  
249  C  C   . LYS A 30  ? 0.44480 0.49301 0.34088 -0.07153 0.13979  -0.05031 409 LYS A C   
250  O  O   . LYS A 30  ? 0.50075 0.54224 0.37487 -0.07450 0.14670  -0.06929 409 LYS A O   
251  C  CB  . LYS A 30  ? 0.47714 0.52437 0.31759 -0.08459 0.14043  -0.01729 409 LYS A CB  
252  C  CG  . LYS A 30  ? 0.53618 0.57896 0.34276 -0.08940 0.12301  0.00592  409 LYS A CG  
253  C  CD  . LYS A 30  ? 0.60964 0.64951 0.39081 -0.09854 0.14234  0.02049  409 LYS A CD  
254  C  CE  . LYS A 30  ? 0.71165 0.74500 0.42558 -0.10969 0.15059  0.01596  409 LYS A CE  
255  N  NZ  . LYS A 30  ? 0.77107 0.80083 0.45092 -0.11062 0.11943  0.02117  409 LYS A NZ  
256  N  N   . MET A 31  ? 0.43621 0.49166 0.38364 -0.06412 0.14578  -0.04788 410 MET A N   
257  C  CA  . MET A 31  ? 0.41712 0.47392 0.40108 -0.05710 0.15931  -0.06538 410 MET A CA  
258  C  C   . MET A 31  ? 0.43617 0.48435 0.42553 -0.05213 0.14282  -0.07559 410 MET A C   
259  O  O   . MET A 31  ? 0.44299 0.48374 0.43508 -0.05041 0.15429  -0.09472 410 MET A O   
260  C  CB  . MET A 31  ? 0.41757 0.48635 0.45816 -0.05042 0.16260  -0.05723 410 MET A CB  
261  C  CG  . MET A 31  ? 0.42013 0.49274 0.50648 -0.04147 0.17586  -0.07193 410 MET A CG  
262  S  SD  . MET A 31  ? 0.54900 0.63111 0.64918 -0.04331 0.21592  -0.08435 410 MET A SD  
263  C  CE  . MET A 31  ? 0.51129 0.57585 0.54693 -0.05057 0.23120  -0.10539 410 MET A CE  
264  N  N   . CYS A 32  ? 0.41347 0.46119 0.40582 -0.05009 0.11783  -0.06355 411 CYS A N   
265  C  CA  . CYS A 32  ? 0.41477 0.45465 0.41044 -0.04755 0.10353  -0.07136 411 CYS A CA  
266  C  C   . CYS A 32  ? 0.44250 0.47412 0.39629 -0.05614 0.10411  -0.08536 411 CYS A C   
267  O  O   . CYS A 32  ? 0.47605 0.49772 0.43462 -0.05589 0.10663  -0.10190 411 CYS A O   
268  C  CB  . CYS A 32  ? 0.39057 0.43292 0.39303 -0.04513 0.08017  -0.05589 411 CYS A CB  
269  S  SG  . CYS A 32  ? 0.40441 0.45230 0.45117 -0.03654 0.07456  -0.04301 411 CYS A SG  
270  N  N   . LEU A 33  ? 0.47510 0.50932 0.38720 -0.06449 0.10014  -0.07843 412 LEU A N   
271  C  CA  . LEU A 33  ? 0.49024 0.51773 0.35696 -0.07469 0.09732  -0.09120 412 LEU A CA  
272  C  C   . LEU A 33  ? 0.52855 0.54611 0.38259 -0.07778 0.12283  -0.11493 412 LEU A C   
273  O  O   . LEU A 33  ? 0.54744 0.55383 0.38393 -0.08326 0.12179  -0.13447 412 LEU A O   
274  C  CB  . LEU A 33  ? 0.48317 0.51561 0.30708 -0.08241 0.08792  -0.07564 412 LEU A CB  
275  C  CG  . LEU A 33  ? 0.49106 0.53138 0.32659 -0.07909 0.06145  -0.05567 412 LEU A CG  
276  C  CD1 . LEU A 33  ? 0.55012 0.59388 0.35274 -0.08370 0.05405  -0.03608 412 LEU A CD1 
277  C  CD2 . LEU A 33  ? 0.48343 0.52388 0.31782 -0.08232 0.04238  -0.06444 412 LEU A CD2 
278  N  N   . ARG A 34  ? 0.53163 0.55282 0.39694 -0.07475 0.14717  -0.11481 413 ARG A N   
279  C  CA  . ARG A 34  ? 0.56041 0.57303 0.42034 -0.07575 0.17611  -0.13867 413 ARG A CA  
280  C  C   . ARG A 34  ? 0.59555 0.59821 0.49642 -0.06717 0.17850  -0.15590 413 ARG A C   
281  O  O   . ARG A 34  ? 0.68019 0.66898 0.56989 -0.06920 0.19646  -0.18069 413 ARG A O   
282  C  CB  . ARG A 34  ? 0.56733 0.59017 0.44645 -0.07264 0.20284  -0.13326 413 ARG A CB  
283  C  CG  . ARG A 34  ? 0.59795 0.62536 0.43033 -0.08322 0.20891  -0.11928 413 ARG A CG  
284  C  CD  . ARG A 34  ? 0.59950 0.63751 0.45857 -0.08117 0.23873  -0.11548 413 ARG A CD  
285  N  NE  . ARG A 34  ? 0.63073 0.66886 0.44502 -0.09073 0.24425  -0.10054 413 ARG A NE  
286  C  CZ  . ARG A 34  ? 0.62594 0.67142 0.45568 -0.09020 0.26515  -0.09371 413 ARG A CZ  
287  N  NH1 . ARG A 34  ? 0.56608 0.62159 0.45667 -0.08067 0.28075  -0.10023 413 ARG A NH1 
288  N  NH2 . ARG A 34  ? 0.63469 0.67801 0.41935 -0.09939 0.26901  -0.07884 413 ARG A NH2 
289  N  N   . GLY A 35  ? 0.55741 0.56470 0.50448 -0.05765 0.16203  -0.14320 414 GLY A N   
290  C  CA  . GLY A 35  ? 0.57703 0.57321 0.56301 -0.04940 0.16115  -0.15408 414 GLY A CA  
291  C  C   . GLY A 35  ? 0.57739 0.56194 0.54897 -0.05504 0.14011  -0.15857 414 GLY A C   
292  O  O   . GLY A 35  ? 0.60171 0.57595 0.60658 -0.04888 0.13538  -0.16195 414 GLY A O   
293  N  N   . GLY A 36  ? 0.57551 0.56214 0.50082 -0.06696 0.12658  -0.15703 415 GLY A N   
294  C  CA  . GLY A 36  ? 0.56416 0.54388 0.47870 -0.07437 0.10606  -0.16137 415 GLY A CA  
295  C  C   . GLY A 36  ? 0.52848 0.51868 0.46648 -0.07074 0.08297  -0.13983 415 GLY A C   
296  O  O   . GLY A 36  ? 0.50883 0.49482 0.44895 -0.07615 0.06812  -0.14260 415 GLY A O   
297  N  N   . GLY A 37  ? 0.45741 0.46060 0.41335 -0.06275 0.08060  -0.11963 416 GLY A N   
298  C  CA  . GLY A 37  ? 0.42765 0.43882 0.40359 -0.05882 0.06217  -0.10133 416 GLY A CA  
299  C  C   . GLY A 37  ? 0.41405 0.43949 0.37276 -0.05998 0.05244  -0.08364 416 GLY A C   
300  O  O   . GLY A 37  ? 0.42565 0.45438 0.34976 -0.06694 0.05291  -0.08423 416 GLY A O   
301  N  N   . ASP A 38  ? 0.37527 0.40693 0.35705 -0.05321 0.04334  -0.06760 417 ASP A N   
302  C  CA  . ASP A 38  ? 0.35916 0.40074 0.33316 -0.05200 0.03540  -0.05041 417 ASP A CA  
303  C  C   . ASP A 38  ? 0.31361 0.35606 0.31761 -0.04340 0.03552  -0.03998 417 ASP A C   
304  O  O   . ASP A 38  ? 0.31442 0.35158 0.34212 -0.03886 0.03803  -0.04397 417 ASP A O   
305  C  CB  . ASP A 38  ? 0.34929 0.39792 0.31356 -0.05552 0.01718  -0.04361 417 ASP A CB  
306  C  CG  . ASP A 38  ? 0.38742 0.44360 0.33153 -0.05662 0.00991  -0.02913 417 ASP A CG  
307  O  OD1 . ASP A 38  ? 0.33778 0.39342 0.28708 -0.05214 0.01537  -0.01840 417 ASP A OD1 
308  O  OD2 . ASP A 38  ? 0.40125 0.46349 0.32595 -0.06243 -0.00285 -0.02760 417 ASP A OD2 
309  N  N   . LEU A 39  ? 0.29189 0.33934 0.29386 -0.04166 0.03136  -0.02619 418 LEU A N   
310  C  CA  . LEU A 39  ? 0.26235 0.30926 0.28822 -0.03541 0.02802  -0.01769 418 LEU A CA  
311  C  C   . LEU A 39  ? 0.28020 0.32483 0.31686 -0.03253 0.01809  -0.01701 418 LEU A C   
312  O  O   . LEU A 39  ? 0.28513 0.33237 0.31351 -0.03518 0.01128  -0.01797 418 LEU A O   
313  C  CB  . LEU A 39  ? 0.28889 0.33775 0.30914 -0.03511 0.02448  -0.00447 418 LEU A CB  
314  C  CG  . LEU A 39  ? 0.29259 0.34238 0.31058 -0.03805 0.03615  -0.00118 418 LEU A CG  
315  C  CD1 . LEU A 39  ? 0.28018 0.32777 0.29124 -0.03872 0.03134  0.01347  418 LEU A CD1 
316  C  CD2 . LEU A 39  ? 0.27223 0.32307 0.31984 -0.03519 0.04274  -0.00478 418 LEU A CD2 
317  N  N   . LEU A 40  ? 0.24014 0.28086 0.29539 -0.02794 0.01694  -0.01429 419 LEU A N   
318  C  CA  . LEU A 40  ? 0.25383 0.29000 0.31616 -0.02593 0.01049  -0.01281 419 LEU A CA  
319  C  C   . LEU A 40  ? 0.24113 0.28088 0.29589 -0.02596 0.00402  -0.00691 419 LEU A C   
320  O  O   . LEU A 40  ? 0.23762 0.27900 0.28913 -0.02402 0.00203  -0.00066 419 LEU A O   
321  C  CB  . LEU A 40  ? 0.23959 0.27096 0.31638 -0.02179 0.00808  -0.00853 419 LEU A CB  
322  C  CG  . LEU A 40  ? 0.23540 0.26010 0.31160 -0.02036 0.00154  -0.00394 419 LEU A CG  
323  C  CD1 . LEU A 40  ? 0.21954 0.23827 0.30024 -0.02160 0.00314  -0.00743 419 LEU A CD1 
324  C  CD2 . LEU A 40  ? 0.27052 0.29123 0.35443 -0.01772 -0.00422 0.00093  419 LEU A CD2 
325  N  N   . SER A 41  ? 0.22895 0.26963 0.28490 -0.02811 0.00175  -0.00895 420 SER A N   
326  C  CA  . SER A 41  ? 0.21414 0.25911 0.27196 -0.02676 -0.00165 -0.00361 420 SER A CA  
327  C  C   . SER A 41  ? 0.25585 0.29286 0.31853 -0.02628 0.00022  -0.00219 420 SER A C   
328  O  O   . SER A 41  ? 0.25541 0.28476 0.32172 -0.02824 0.00167  -0.00483 420 SER A O   
329  C  CB  . SER A 41  ? 0.25617 0.31295 0.31479 -0.03091 -0.00584 -0.00511 420 SER A CB  
330  O  OG  . SER A 41  ? 0.24734 0.30244 0.30845 -0.03740 -0.00526 -0.01293 420 SER A OG  
331  N  N   . ILE A 42  ? 0.24138 0.27825 0.30282 -0.02348 0.00109  0.00234  421 ILE A N   
332  C  CA  . ILE A 42  ? 0.21866 0.24581 0.27574 -0.02348 0.00383  0.00518  421 ILE A CA  
333  C  C   . ILE A 42  ? 0.25273 0.28683 0.31394 -0.02425 0.00952  0.00656  421 ILE A C   
334  O  O   . ILE A 42  ? 0.25082 0.29085 0.31456 -0.02003 0.01120  0.00693  421 ILE A O   
335  C  CB  . ILE A 42  ? 0.25156 0.26906 0.29822 -0.02003 0.00138  0.00718  421 ILE A CB  
336  C  CG1 . ILE A 42  ? 0.22750 0.24320 0.27881 -0.01940 -0.00359 0.00625  421 ILE A CG1 
337  C  CG2 . ILE A 42  ? 0.26253 0.26851 0.29669 -0.02144 0.00234  0.01076  421 ILE A CG2 
338  C  CD1 . ILE A 42  ? 0.26721 0.27595 0.31291 -0.01802 -0.00861 0.00771  421 ILE A CD1 
339  N  N   . HIS A 43  ? 0.24442 0.27756 0.30994 -0.02948 0.01369  0.00771  422 HIS A N   
340  C  CA  . HIS A 43  ? 0.23059 0.27530 0.30802 -0.03167 0.02091  0.00870  422 HIS A CA  
341  C  C   . HIS A 43  ? 0.25602 0.29145 0.32342 -0.03387 0.03144  0.01312  422 HIS A C   
342  O  O   . HIS A 43  ? 0.25228 0.29800 0.33243 -0.03674 0.04112  0.01416  422 HIS A O   
343  C  CB  . HIS A 43  ? 0.25802 0.31382 0.35340 -0.03896 0.01796  0.00587  422 HIS A CB  
344  C  CG  . HIS A 43  ? 0.25615 0.32184 0.35495 -0.03823 0.00799  0.00142  422 HIS A CG  
345  N  ND1 . HIS A 43  ? 0.27965 0.34137 0.37585 -0.04359 0.00276  -0.00462 422 HIS A ND1 
346  C  CD2 . HIS A 43  ? 0.24747 0.32480 0.34930 -0.03301 0.00293  0.00268  422 HIS A CD2 
347  C  CE1 . HIS A 43  ? 0.26857 0.33974 0.36127 -0.04274 -0.00470 -0.00713 422 HIS A CE1 
348  N  NE2 . HIS A 43  ? 0.26502 0.34575 0.36166 -0.03629 -0.00581 -0.00118 422 HIS A NE2 
349  N  N   . SER A 44  ? 0.25726 0.27469 0.30245 -0.03322 0.02974  0.01644  423 SER A N   
350  C  CA  . SER A 44  ? 0.28505 0.29073 0.31188 -0.03675 0.03873  0.02231  423 SER A CA  
351  C  C   . SER A 44  ? 0.31140 0.29959 0.31089 -0.03439 0.03081  0.02505  423 SER A C   
352  O  O   . SER A 44  ? 0.31521 0.30103 0.31832 -0.03146 0.01865  0.02403  423 SER A O   
353  C  CB  . SER A 44  ? 0.31448 0.31539 0.34857 -0.04499 0.04225  0.02865  423 SER A CB  
354  O  OG  . SER A 44  ? 0.27571 0.26336 0.30795 -0.04502 0.03113  0.03167  423 SER A OG  
355  N  N   . MET A 45  ? 0.32363 0.30062 0.29584 -0.03646 0.03804  0.02818  424 MET A N   
356  C  CA  . MET A 45  ? 0.38251 0.34238 0.32494 -0.03649 0.02733  0.03184  424 MET A CA  
357  C  C   . MET A 45  ? 0.37600 0.32685 0.32180 -0.03822 0.01468  0.04210  424 MET A C   
358  O  O   . MET A 45  ? 0.36407 0.30924 0.30579 -0.03560 -0.00070 0.04403  424 MET A O   
359  C  CB  . MET A 45  ? 0.40033 0.34774 0.30578 -0.04058 0.03845  0.03354  424 MET A CB  
360  C  CG  . MET A 45  ? 0.52043 0.45002 0.38854 -0.04210 0.02451  0.03585  424 MET A CG  
361  S  SD  . MET A 45  ? 0.66156 0.59199 0.52905 -0.03718 0.01492  0.02138  424 MET A SD  
362  C  CE  . MET A 45  ? 0.59762 0.52733 0.45253 -0.03588 0.03957  0.00876  424 MET A CE  
363  N  N   . ALA A 46  ? 0.36924 0.31857 0.32671 -0.04260 0.02091  0.04883  425 ALA A N   
364  C  CA  . ALA A 46  ? 0.34350 0.28118 0.30906 -0.04293 0.01022  0.05843  425 ALA A CA  
365  C  C   . ALA A 46  ? 0.35437 0.30016 0.34767 -0.03673 -0.00015 0.05108  425 ALA A C   
366  O  O   . ALA A 46  ? 0.34607 0.28438 0.34398 -0.03291 -0.01287 0.05638  425 ALA A O   
367  C  CB  . ALA A 46  ? 0.39277 0.32568 0.37002 -0.04987 0.02069  0.06486  425 ALA A CB  
368  N  N   . GLU A 47  ? 0.29771 0.25953 0.31027 -0.03568 0.00534  0.03957  426 GLU A N   
369  C  CA  . GLU A 47  ? 0.29991 0.26911 0.33273 -0.03097 -0.00124 0.03208  426 GLU A CA  
370  C  C   . GLU A 47  ? 0.31994 0.29174 0.34604 -0.02620 -0.00992 0.03047  426 GLU A C   
371  O  O   . GLU A 47  ? 0.30240 0.27529 0.34305 -0.02246 -0.01738 0.02966  426 GLU A O   
372  C  CB  . GLU A 47  ? 0.29825 0.28280 0.34582 -0.03253 0.00522  0.02197  426 GLU A CB  
373  C  CG  . GLU A 47  ? 0.28012 0.27056 0.34242 -0.02961 0.00164  0.01398  426 GLU A CG  
374  C  CD  . GLU A 47  ? 0.31510 0.31818 0.38585 -0.03329 0.00551  0.00541  426 GLU A CD  
375  O  OE1 . GLU A 47  ? 0.29043 0.30240 0.36069 -0.03629 0.00908  0.00610  426 GLU A OE1 
376  O  OE2 . GLU A 47  ? 0.29368 0.29833 0.37179 -0.03341 0.00494  -0.00222 426 GLU A OE2 
377  N  N   . LEU A 48  ? 0.30374 0.27635 0.31069 -0.02669 -0.00790 0.02900  427 LEU A N   
378  C  CA  . LEU A 48  ? 0.33032 0.30244 0.33064 -0.02432 -0.01706 0.02668  427 LEU A CA  
379  C  C   . LEU A 48  ? 0.33247 0.29450 0.32630 -0.02439 -0.03122 0.03522  427 LEU A C   
380  O  O   . LEU A 48  ? 0.31412 0.28070 0.32298 -0.02197 -0.04176 0.03450  427 LEU A O   
381  C  CB  . LEU A 48  ? 0.34042 0.30994 0.31926 -0.02530 -0.01125 0.02195  427 LEU A CB  
382  C  CG  . LEU A 48  ? 0.37634 0.34064 0.34522 -0.02532 -0.02218 0.01876  427 LEU A CG  
383  C  CD1 . LEU A 48  ? 0.33390 0.30902 0.32789 -0.02262 -0.02465 0.01392  427 LEU A CD1 
384  C  CD2 . LEU A 48  ? 0.40932 0.36448 0.35143 -0.02695 -0.01522 0.01275  427 LEU A CD2 
385  N  N   . GLU A 49  ? 0.33594 0.28508 0.30915 -0.02750 -0.03206 0.04482  428 GLU A N   
386  C  CA  . GLU A 49  ? 0.39701 0.33580 0.36126 -0.02748 -0.04892 0.05608  428 GLU A CA  
387  C  C   . GLU A 49  ? 0.37530 0.31654 0.37504 -0.02211 -0.05620 0.06130  428 GLU A C   
388  O  O   . GLU A 49  ? 0.36514 0.30734 0.37628 -0.01901 -0.07262 0.06693  428 GLU A O   
389  C  CB  . GLU A 49  ? 0.48145 0.40355 0.40963 -0.03291 -0.04692 0.06742  428 GLU A CB  
390  C  CG  . GLU A 49  ? 0.56832 0.48556 0.45733 -0.03784 -0.03999 0.06091  428 GLU A CG  
391  C  CD  . GLU A 49  ? 0.74913 0.64913 0.59631 -0.04449 -0.03496 0.07216  428 GLU A CD  
392  O  OE1 . GLU A 49  ? 0.75313 0.64591 0.60561 -0.04587 -0.03267 0.08548  428 GLU A OE1 
393  O  OE2 . GLU A 49  ? 0.79843 0.69014 0.60578 -0.04901 -0.03215 0.06734  428 GLU A OE2 
394  N  N   . PHE A 50  ? 0.32085 0.26341 0.34082 -0.02102 -0.04447 0.05848  429 PHE A N   
395  C  CA  . PHE A 50  ? 0.35405 0.29788 0.40958 -0.01510 -0.04767 0.05876  429 PHE A CA  
396  C  C   . PHE A 50  ? 0.33649 0.29665 0.41474 -0.01087 -0.05052 0.04928  429 PHE A C   
397  O  O   . PHE A 50  ? 0.28809 0.25153 0.39206 -0.00534 -0.06020 0.05298  429 PHE A O   
398  C  CB  . PHE A 50  ? 0.32770 0.26872 0.39679 -0.01676 -0.03338 0.05276  429 PHE A CB  
399  C  CG  . PHE A 50  ? 0.33187 0.27337 0.43595 -0.01069 -0.03213 0.04720  429 PHE A CG  
400  C  CD1 . PHE A 50  ? 0.31571 0.24317 0.43797 -0.00543 -0.03943 0.05771  429 PHE A CD1 
401  C  CD2 . PHE A 50  ? 0.32164 0.27641 0.43947 -0.00987 -0.02302 0.03184  429 PHE A CD2 
402  C  CE1 . PHE A 50  ? 0.33042 0.25711 0.48845 0.00161  -0.03556 0.05069  429 PHE A CE1 
403  C  CE2 . PHE A 50  ? 0.28941 0.24339 0.43636 -0.00451 -0.01839 0.02446  429 PHE A CE2 
404  C  CZ  . PHE A 50  ? 0.31831 0.25835 0.48745 0.00174  -0.02360 0.03270  429 PHE A CZ  
405  N  N   . ILE A 51  ? 0.28937 0.26033 0.36083 -0.01342 -0.04184 0.03837  430 ILE A N   
406  C  CA  . ILE A 51  ? 0.30570 0.29090 0.39605 -0.01129 -0.04140 0.03044  430 ILE A CA  
407  C  C   . ILE A 51  ? 0.32085 0.30901 0.41522 -0.01089 -0.05703 0.03549  430 ILE A C   
408  O  O   . ILE A 51  ? 0.29802 0.29568 0.42338 -0.00721 -0.06187 0.03569  430 ILE A O   
409  C  CB  . ILE A 51  ? 0.30450 0.29687 0.38193 -0.01453 -0.03132 0.02174  430 ILE A CB  
410  C  CG1 . ILE A 51  ? 0.31021 0.30457 0.39057 -0.01555 -0.01928 0.01584  430 ILE A CG1 
411  C  CG2 . ILE A 51  ? 0.35816 0.36150 0.44840 -0.01423 -0.03202 0.01716  430 ILE A CG2 
412  C  CD1 . ILE A 51  ? 0.28320 0.27901 0.38668 -0.01282 -0.01486 0.01114  430 ILE A CD1 
413  N  N   . THR A 52  ? 0.32876 0.30958 0.39295 -0.01536 -0.06468 0.03841  431 THR A N   
414  C  CA  . THR A 52  ? 0.35957 0.34262 0.42402 -0.01746 -0.08199 0.04111  431 THR A CA  
415  C  C   . THR A 52  ? 0.33779 0.31941 0.41883 -0.01385 -0.09918 0.05356  431 THR A C   
416  O  O   . THR A 52  ? 0.34426 0.33750 0.45359 -0.01254 -0.11234 0.05535  431 THR A O   
417  C  CB  . THR A 52  ? 0.37705 0.34861 0.39936 -0.02389 -0.08517 0.03881  431 THR A CB  
418  O  OG1 . THR A 52  ? 0.42277 0.37971 0.41522 -0.02539 -0.08776 0.04804  431 THR A OG1 
419  C  CG2 . THR A 52  ? 0.35811 0.33039 0.37046 -0.02483 -0.06723 0.02833  431 THR A CG2 
420  N  N   . LYS A 53  ? 0.32287 0.29113 0.39195 -0.01201 -0.09926 0.06346  432 LYS A N   
421  C  CA  . LYS A 53  ? 0.38699 0.35015 0.46808 -0.00808 -0.11823 0.07893  432 LYS A CA  
422  C  C   . LYS A 53  ? 0.38084 0.35345 0.51584 0.00158  -0.11651 0.07996  432 LYS A C   
423  O  O   . LYS A 53  ? 0.39120 0.36986 0.55443 0.00658  -0.13475 0.08975  432 LYS A O   
424  C  CB  . LYS A 53  ? 0.44426 0.38611 0.49177 -0.01026 -0.11829 0.09184  432 LYS A CB  
425  C  CG  . LYS A 53  ? 0.54826 0.47865 0.54916 -0.01735 -0.13499 0.10134  432 LYS A CG  
426  C  CD  . LYS A 53  ? 0.59970 0.51237 0.58838 -0.01595 -0.14815 0.12354  432 LYS A CD  
427  C  CE  . LYS A 53  ? 0.63445 0.55477 0.67087 -0.00649 -0.16921 0.13529  432 LYS A CE  
428  N  NZ  . LYS A 53  ? 0.66531 0.56707 0.68555 -0.00529 -0.18882 0.16061  432 LYS A NZ  
429  N  N   . GLN A 54  ? 0.34570 0.31959 0.49621 0.00436  -0.09541 0.06970  433 GLN A N   
430  C  CA  . GLN A 54  ? 0.34309 0.32015 0.53944 0.01362  -0.08984 0.06866  433 GLN A CA  
431  C  C   . GLN A 54  ? 0.32091 0.31620 0.54635 0.01559  -0.07440 0.05288  433 GLN A C   
432  O  O   . GLN A 54  ? 0.27180 0.27457 0.54098 0.02382  -0.07136 0.05128  433 GLN A O   
433  C  CB  . GLN A 54  ? 0.34154 0.29925 0.53196 0.01470  -0.07779 0.06969  433 GLN A CB  
434  C  CG  . GLN A 54  ? 0.40386 0.34136 0.57846 0.01494  -0.09178 0.08933  433 GLN A CG  
435  C  CD  . GLN A 54  ? 0.43449 0.37140 0.64833 0.02547  -0.10885 0.10295  433 GLN A CD  
436  O  OE1 . GLN A 54  ? 0.44280 0.38620 0.70340 0.03466  -0.10141 0.09596  433 GLN A OE1 
437  N  NE2 . GLN A 54  ? 0.45405 0.38336 0.64936 0.02446  -0.13193 0.12257  433 GLN A NE2 
438  N  N   . ILE A 55  ? 0.29582 0.29771 0.49905 0.00870  -0.06357 0.04202  434 ILE A N   
439  C  CA  . ILE A 55  ? 0.26476 0.28064 0.48742 0.00917  -0.04680 0.02876  434 ILE A CA  
440  C  C   . ILE A 55  ? 0.28217 0.31438 0.51364 0.00539  -0.05277 0.02808  434 ILE A C   
441  O  O   . ILE A 55  ? 0.26706 0.31483 0.53727 0.00858  -0.04958 0.02578  434 ILE A O   
442  C  CB  . ILE A 55  ? 0.27863 0.28939 0.47286 0.00409  -0.03033 0.01848  434 ILE A CB  
443  C  CG1 . ILE A 55  ? 0.26982 0.26406 0.45814 0.00540  -0.02561 0.01855  434 ILE A CG1 
444  C  CG2 . ILE A 55  ? 0.29493 0.31786 0.50333 0.00397  -0.01375 0.00648  434 ILE A CG2 
445  C  CD1 . ILE A 55  ? 0.29277 0.28369 0.51571 0.01277  -0.01746 0.01337  434 ILE A CD1 
446  N  N   . LYS A 56  ? 0.26777 0.29597 0.46617 -0.00177 -0.06022 0.02949  435 LYS A N   
447  C  CA  . LYS A 56  ? 0.28515 0.32458 0.49033 -0.00719 -0.06656 0.02800  435 LYS A CA  
448  C  C   . LYS A 56  ? 0.30595 0.35352 0.53798 -0.00620 -0.08812 0.03643  435 LYS A C   
449  O  O   . LYS A 56  ? 0.25156 0.31705 0.52189 -0.00682 -0.08937 0.03515  435 LYS A O   
450  C  CB  . LYS A 56  ? 0.29136 0.32005 0.45451 -0.01427 -0.06817 0.02561  435 LYS A CB  
451  C  CG  . LYS A 56  ? 0.27677 0.30868 0.43949 -0.02138 -0.08032 0.02466  435 LYS A CG  
452  C  CD  . LYS A 56  ? 0.29768 0.31414 0.41763 -0.02633 -0.07821 0.02023  435 LYS A CD  
453  C  CE  . LYS A 56  ? 0.33428 0.34886 0.45167 -0.03443 -0.08735 0.01587  435 LYS A CE  
454  N  NZ  . LYS A 56  ? 0.33807 0.35507 0.46276 -0.03826 -0.11091 0.02010  435 LYS A NZ  
455  N  N   . GLN A 57  ? 0.29700 0.33247 0.50932 -0.00561 -0.10583 0.04608  436 GLN A N   
456  C  CA  . GLN A 57  ? 0.31815 0.35998 0.55101 -0.00471 -0.13165 0.05695  436 GLN A CA  
457  C  C   . GLN A 57  ? 0.31214 0.36669 0.55364 -0.01372 -0.14272 0.05241  436 GLN A C   
458  O  O   . GLN A 57  ? 0.34077 0.38517 0.54435 -0.02222 -0.14089 0.04552  436 GLN A O   
459  C  CB  . GLN A 57  ? 0.30468 0.35713 0.59043 0.00659  -0.13081 0.06261  436 GLN A CB  
460  C  CG  . GLN A 57  ? 0.32688 0.36189 0.60319 0.01396  -0.11984 0.06573  436 GLN A CG  
461  C  CD  . GLN A 57  ? 0.36901 0.40713 0.69304 0.02586  -0.12819 0.07603  436 GLN A CD  
462  O  OE1 . GLN A 57  ? 0.37523 0.43312 0.75302 0.03209  -0.12408 0.07262  436 GLN A OE1 
463  N  NE2 . GLN A 57  ? 0.39912 0.41719 0.70590 0.02933  -0.13909 0.08969  436 GLN A NE2 
464  N  N   . GLU A 58  ? 0.27763 0.35412 0.57190 -0.01235 -0.15301 0.05534  437 GLU A N   
465  C  CA  . GLU A 58  ? 0.28502 0.37310 0.59030 -0.02314 -0.16753 0.05210  437 GLU A CA  
466  C  C   . GLU A 58  ? 0.28515 0.37812 0.59456 -0.02968 -0.14545 0.04018  437 GLU A C   
467  O  O   . GLU A 58  ? 0.28928 0.38674 0.60307 -0.04055 -0.15510 0.03626  437 GLU A O   
468  C  CB  . GLU A 58  ? 0.27389 0.37903 0.62586 -0.01967 -0.17890 0.05841  437 GLU A CB  
469  C  CG  . GLU A 58  ? 0.28716 0.41277 0.69255 -0.01529 -0.15583 0.05300  437 GLU A CG  
470  C  CD  . GLU A 58  ? 0.35227 0.47832 0.77628 -0.00282 -0.13339 0.05188  437 GLU A CD  
471  O  OE1 . GLU A 58  ? 0.29800 0.40952 0.70220 0.00386  -0.13830 0.05758  437 GLU A OE1 
472  O  OE2 . GLU A 58  ? 0.29610 0.43527 0.75209 -0.00041 -0.10958 0.04471  437 GLU A OE2 
473  N  N   . VAL A 59  ? 0.23089 0.32198 0.53859 -0.02436 -0.11755 0.03493  438 VAL A N   
474  C  CA  . VAL A 59  ? 0.27266 0.36711 0.58119 -0.03067 -0.09780 0.02691  438 VAL A CA  
475  C  C   . VAL A 59  ? 0.29527 0.36960 0.55532 -0.03904 -0.10193 0.02248  438 VAL A C   
476  O  O   . VAL A 59  ? 0.28737 0.34352 0.50498 -0.03659 -0.10372 0.02240  438 VAL A O   
477  C  CB  . VAL A 59  ? 0.27275 0.36702 0.58000 -0.02390 -0.06993 0.02270  438 VAL A CB  
478  C  CG1 . VAL A 59  ? 0.28280 0.37656 0.57977 -0.03113 -0.05162 0.01750  438 VAL A CG1 
479  C  CG2 . VAL A 59  ? 0.30068 0.41328 0.65860 -0.01550 -0.06209 0.02382  438 VAL A CG2 
480  N  N   . GLU A 60  ? 0.26325 0.33995 0.53200 -0.04910 -0.10212 0.01856  439 GLU A N   
481  C  CA  . GLU A 60  ? 0.30999 0.36539 0.53800 -0.05683 -0.10905 0.01305  439 GLU A CA  
482  C  C   . GLU A 60  ? 0.30381 0.34426 0.50104 -0.05434 -0.08782 0.00941  439 GLU A C   
483  O  O   . GLU A 60  ? 0.34134 0.36237 0.49881 -0.05414 -0.08937 0.00555  439 GLU A O   
484  C  CB  . GLU A 60  ? 0.34586 0.40570 0.59635 -0.06976 -0.12060 0.00972  439 GLU A CB  
485  C  CG  . GLU A 60  ? 0.42461 0.45878 0.63640 -0.07806 -0.12347 0.00110  439 GLU A CG  
486  C  CD  . GLU A 60  ? 0.47311 0.49059 0.64366 -0.07999 -0.14367 -0.00296 439 GLU A CD  
487  O  OE1 . GLU A 60  ? 0.41680 0.44367 0.59082 -0.07665 -0.16006 0.00350  439 GLU A OE1 
488  O  OE2 . GLU A 60  ? 0.48914 0.48272 0.62302 -0.08476 -0.14233 -0.01234 439 GLU A OE2 
489  N  N   . GLU A 61  ? 0.28669 0.33632 0.50141 -0.05246 -0.06800 0.01089  440 GLU A N   
490  C  CA  . GLU A 61  ? 0.29532 0.33239 0.48436 -0.05143 -0.05165 0.00970  440 GLU A CA  
491  C  C   . GLU A 61  ? 0.28217 0.33074 0.48027 -0.04607 -0.03269 0.01230  440 GLU A C   
492  O  O   . GLU A 61  ? 0.24454 0.30973 0.47572 -0.04782 -0.02534 0.01387  440 GLU A O   
493  C  CB  . GLU A 61  ? 0.31508 0.34387 0.50906 -0.06110 -0.05027 0.00872  440 GLU A CB  
494  C  CG  . GLU A 61  ? 0.33440 0.34856 0.50504 -0.05930 -0.03604 0.01038  440 GLU A CG  
495  C  CD  . GLU A 61  ? 0.43805 0.43759 0.61297 -0.06846 -0.03652 0.01007  440 GLU A CD  
496  O  OE1 . GLU A 61  ? 0.42281 0.42872 0.62566 -0.07836 -0.04318 0.00935  440 GLU A OE1 
497  O  OE2 . GLU A 61  ? 0.60227 0.58376 0.75602 -0.06575 -0.03067 0.01077  440 GLU A OE2 
498  N  N   . LEU A 62  ? 0.22807 0.26862 0.39781 -0.04025 -0.02442 0.01179  441 LEU A N   
499  C  CA  . LEU A 62  ? 0.24865 0.29761 0.41987 -0.03687 -0.00807 0.01214  441 LEU A CA  
500  C  C   . LEU A 62  ? 0.23374 0.27253 0.37294 -0.03481 -0.00188 0.01295  441 LEU A C   
501  O  O   . LEU A 62  ? 0.24627 0.27328 0.36628 -0.03316 -0.00906 0.01258  441 LEU A O   
502  C  CB  . LEU A 62  ? 0.26704 0.32378 0.45053 -0.03035 -0.00811 0.00955  441 LEU A CB  
503  C  CG  . LEU A 62  ? 0.24300 0.28991 0.40889 -0.02559 -0.01964 0.00934  441 LEU A CG  
504  C  CD1 . LEU A 62  ? 0.26812 0.30777 0.40654 -0.02295 -0.01171 0.00728  441 LEU A CD1 
505  C  CD2 . LEU A 62  ? 0.28402 0.33795 0.47566 -0.02053 -0.02483 0.01023  441 LEU A CD2 
506  N  N   . TRP A 63  ? 0.23795 0.28219 0.37195 -0.03509 0.01168  0.01387  442 TRP A N   
507  C  CA  . TRP A 63  ? 0.21229 0.25025 0.31845 -0.03356 0.01475  0.01618  442 TRP A CA  
508  C  C   . TRP A 63  ? 0.25204 0.28963 0.34618 -0.02845 0.01138  0.01127  442 TRP A C   
509  O  O   . TRP A 63  ? 0.23489 0.27753 0.33834 -0.02662 0.01395  0.00597  442 TRP A O   
510  C  CB  . TRP A 63  ? 0.22646 0.26978 0.32433 -0.03723 0.02847  0.01902  442 TRP A CB  
511  C  CG  . TRP A 63  ? 0.26471 0.30675 0.36944 -0.04391 0.03523  0.02698  442 TRP A CG  
512  C  CD1 . TRP A 63  ? 0.26659 0.31807 0.38621 -0.04945 0.04941  0.02772  442 TRP A CD1 
513  C  CD2 . TRP A 63  ? 0.29603 0.32538 0.39471 -0.04617 0.03017  0.03574  442 TRP A CD2 
514  N  NE1 . TRP A 63  ? 0.28376 0.32940 0.40603 -0.05647 0.05308  0.03770  442 TRP A NE1 
515  C  CE2 . TRP A 63  ? 0.29619 0.32659 0.40591 -0.05433 0.04058  0.04273  442 TRP A CE2 
516  C  CE3 . TRP A 63  ? 0.27895 0.29540 0.36700 -0.04183 0.01955  0.03791  442 TRP A CE3 
517  C  CZ2 . TRP A 63  ? 0.32108 0.33728 0.43039 -0.05883 0.03902  0.05273  442 TRP A CZ2 
518  C  CZ3 . TRP A 63  ? 0.31538 0.31785 0.40428 -0.04464 0.01851  0.04628  442 TRP A CZ3 
519  C  CH2 . TRP A 63  ? 0.33867 0.33976 0.43751 -0.05331 0.02733  0.05404  442 TRP A CH2 
520  N  N   . ILE A 64  ? 0.23854 0.27015 0.31554 -0.02618 0.00676  0.01331  443 ILE A N   
521  C  CA  . ILE A 64  ? 0.24504 0.27881 0.31159 -0.02368 0.00577  0.00983  443 ILE A CA  
522  C  C   . ILE A 64  ? 0.23375 0.26996 0.28513 -0.02433 0.00650  0.01420  443 ILE A C   
523  O  O   . ILE A 64  ? 0.24097 0.27514 0.28831 -0.02605 0.00833  0.02118  443 ILE A O   
524  C  CB  . ILE A 64  ? 0.23861 0.26660 0.30384 -0.02055 -0.00098 0.00858  443 ILE A CB  
525  C  CG1 . ILE A 64  ? 0.24030 0.26096 0.30015 -0.01867 -0.00390 0.01200  443 ILE A CG1 
526  C  CG2 . ILE A 64  ? 0.24764 0.27279 0.32359 -0.02046 -0.00506 0.00668  443 ILE A CG2 
527  C  CD1 . ILE A 64  ? 0.24384 0.25870 0.29792 -0.01610 -0.00628 0.00944  443 ILE A CD1 
528  N  N   . GLY A 65  ? 0.22927 0.26988 0.27341 -0.02374 0.00381  0.01146  444 GLY A N   
529  C  CA  . GLY A 65  ? 0.23908 0.28520 0.26931 -0.02550 0.00134  0.01554  444 GLY A CA  
530  C  C   . GLY A 65  ? 0.25810 0.30407 0.28960 -0.02122 -0.00573 0.02470  444 GLY A C   
531  O  O   . GLY A 65  ? 0.27521 0.32692 0.29717 -0.02204 -0.01122 0.03086  444 GLY A O   
532  N  N   . LEU A 66  ? 0.25784 0.29690 0.30070 -0.01644 -0.00621 0.02554  445 LEU A N   
533  C  CA  . LEU A 66  ? 0.24064 0.27830 0.29003 -0.01041 -0.01035 0.03225  445 LEU A CA  
534  C  C   . LEU A 66  ? 0.27036 0.29961 0.31658 -0.00986 -0.01109 0.04291  445 LEU A C   
535  O  O   . LEU A 66  ? 0.26389 0.28463 0.30817 -0.01380 -0.00640 0.04329  445 LEU A O   
536  C  CB  . LEU A 66  ? 0.25066 0.28043 0.30901 -0.00612 -0.00740 0.02685  445 LEU A CB  
537  C  CG  . LEU A 66  ? 0.24704 0.27789 0.31738 0.00152  -0.00758 0.02924  445 LEU A CG  
538  C  CD1 . LEU A 66  ? 0.25195 0.30096 0.33014 0.00154  -0.01054 0.02912  445 LEU A CD1 
539  C  CD2 . LEU A 66  ? 0.26870 0.28725 0.33952 0.00403  -0.00117 0.02150  445 LEU A CD2 
540  N  N   . ASN A 67  ? 0.25606 0.28815 0.30473 -0.00528 -0.01755 0.05301  446 ASN A N   
541  C  CA  . ASN A 67  ? 0.29161 0.31371 0.33554 -0.00499 -0.01927 0.06672  446 ASN A CA  
542  C  C   . ASN A 67  ? 0.32478 0.34913 0.38100 0.00397  -0.02837 0.07797  446 ASN A C   
543  O  O   . ASN A 67  ? 0.31185 0.35238 0.37603 0.00699  -0.03497 0.07638  446 ASN A O   
544  C  CB  . ASN A 67  ? 0.29996 0.32648 0.32058 -0.01363 -0.01854 0.07204  446 ASN A CB  
545  C  CG  . ASN A 67  ? 0.34930 0.39035 0.35717 -0.01456 -0.02914 0.07639  446 ASN A CG  
546  O  OD1 . ASN A 67  ? 0.33246 0.37326 0.33494 -0.01216 -0.03872 0.09169  446 ASN A OD1 
547  N  ND2 . ASN A 67  ? 0.29834 0.35125 0.30242 -0.01844 -0.02919 0.06348  446 ASN A ND2 
548  N  N   . ASP A 68  ? 0.33468 0.34296 0.39662 0.00811  -0.02894 0.08985  447 ASP A N   
549  C  CA  . ASP A 68  ? 0.33235 0.34139 0.40847 0.01782  -0.03901 0.10464  447 ASP A CA  
550  C  C   . ASP A 68  ? 0.38608 0.38737 0.44400 0.01415  -0.04562 0.12511  447 ASP A C   
551  O  O   . ASP A 68  ? 0.37960 0.36754 0.44926 0.02154  -0.05069 0.14095  447 ASP A O   
552  C  CB  . ASP A 68  ? 0.31890 0.31283 0.42268 0.02900  -0.03378 0.10141  447 ASP A CB  
553  C  CG  . ASP A 68  ? 0.38810 0.35362 0.49080 0.02715  -0.02717 0.10492  447 ASP A CG  
554  O  OD1 . ASP A 68  ? 0.36981 0.33024 0.45383 0.01590  -0.02317 0.10498  447 ASP A OD1 
555  O  OD2 . ASP A 68  ? 0.37978 0.32794 0.50348 0.03680  -0.02508 0.10682  447 ASP A OD2 
556  N  N   . LEU A 69  ? 0.36111 0.36961 0.38886 0.00264  -0.04467 0.12527  448 LEU A N   
557  C  CA  . LEU A 69  ? 0.40726 0.40900 0.40893 -0.00308 -0.04906 0.14495  448 LEU A CA  
558  C  C   . LEU A 69  ? 0.47024 0.48008 0.47240 0.00373  -0.06876 0.16338  448 LEU A C   
559  O  O   . LEU A 69  ? 0.50853 0.50475 0.50381 0.00559  -0.07522 0.18584  448 LEU A O   
560  C  CB  . LEU A 69  ? 0.44013 0.45023 0.40781 -0.01644 -0.04180 0.13760  448 LEU A CB  
561  C  CG  . LEU A 69  ? 0.43381 0.43481 0.40246 -0.02372 -0.02304 0.12713  448 LEU A CG  
562  C  CD1 . LEU A 69  ? 0.46476 0.47756 0.40979 -0.03367 -0.01396 0.11449  448 LEU A CD1 
563  C  CD2 . LEU A 69  ? 0.46833 0.44944 0.43291 -0.02752 -0.01689 0.14486  448 LEU A CD2 
564  N  N   . LYS A 70  ? 0.44740 0.47971 0.45943 0.00691  -0.07972 0.15577  449 LYS A N   
565  C  CA  . LYS A 70  ? 0.47893 0.52384 0.49300 0.01181  -0.10199 0.17368  449 LYS A CA  
566  C  C   . LYS A 70  ? 0.43660 0.47610 0.49452 0.02867  -0.10831 0.18578  449 LYS A C   
567  O  O   . LYS A 70  ? 0.44959 0.48509 0.50944 0.03455  -0.12396 0.20990  449 LYS A O   
568  C  CB  . LYS A 70  ? 0.47934 0.55192 0.49240 0.00723  -0.11269 0.16098  449 LYS A CB  
569  C  CG  . LYS A 70  ? 0.54106 0.61637 0.51034 -0.00881 -0.10659 0.14793  449 LYS A CG  
570  C  CD  . LYS A 70  ? 0.58250 0.64163 0.50849 -0.01685 -0.10423 0.16343  449 LYS A CD  
571  C  CE  . LYS A 70  ? 0.60150 0.66181 0.48449 -0.03192 -0.09371 0.14880  449 LYS A CE  
572  N  NZ  . LYS A 70  ? 0.63776 0.68653 0.47357 -0.04055 -0.09462 0.16698  449 LYS A NZ  
573  N  N   . LEU A 71  ? 0.41663 0.45406 0.50877 0.03682  -0.09568 0.16977  450 LEU A N   
574  C  CA  . LEU A 71  ? 0.43077 0.46486 0.56840 0.05395  -0.09814 0.17620  450 LEU A CA  
575  C  C   . LEU A 71  ? 0.42473 0.43660 0.57656 0.05765  -0.07674 0.15986  450 LEU A C   
576  O  O   . LEU A 71  ? 0.39624 0.41552 0.54983 0.05431  -0.06506 0.13836  450 LEU A O   
577  C  CB  . LEU A 71  ? 0.38450 0.45027 0.55384 0.06030  -0.10798 0.17087  450 LEU A CB  
578  C  CG  . LEU A 71  ? 0.40405 0.47605 0.62537 0.07896  -0.11541 0.18220  450 LEU A CG  
579  C  CD1 . LEU A 71  ? 0.39213 0.46051 0.60458 0.08139  -0.13518 0.20646  450 LEU A CD1 
580  C  CD2 . LEU A 71  ? 0.40910 0.51565 0.66340 0.08147  -0.11877 0.17104  450 LEU A CD2 
581  N  N   . GLN A 72  ? 0.41106 0.39417 0.57137 0.06360  -0.07257 0.17024  451 GLN A N   
582  C  CA  . GLN A 72  ? 0.40474 0.36329 0.57178 0.06380  -0.05403 0.15344  451 GLN A CA  
583  C  C   . GLN A 72  ? 0.41615 0.38251 0.61291 0.07387  -0.04427 0.13396  451 GLN A C   
584  O  O   . GLN A 72  ? 0.35292 0.33065 0.58395 0.08784  -0.04915 0.13954  451 GLN A O   
585  C  CB  . GLN A 72  ? 0.42135 0.34591 0.59894 0.06931  -0.05254 0.16803  451 GLN A CB  
586  C  CG  . GLN A 72  ? 0.45024 0.35903 0.59574 0.05549  -0.05305 0.18207  451 GLN A CG  
587  C  CD  . GLN A 72  ? 0.47409 0.37858 0.59869 0.04044  -0.03908 0.16272  451 GLN A CD  
588  O  OE1 . GLN A 72  ? 0.46746 0.36508 0.60332 0.04134  -0.02876 0.14133  451 GLN A OE1 
589  N  NE2 . GLN A 72  ? 0.52221 0.43135 0.61615 0.02651  -0.03879 0.17041  451 GLN A NE2 
590  N  N   . MET A 73  ? 0.39769 0.35815 0.58179 0.06660  -0.03010 0.11191  452 MET A N   
591  C  CA  . MET A 73  ? 0.40725 0.37049 0.60602 0.07188  -0.01681 0.09097  452 MET A CA  
592  C  C   . MET A 73  ? 0.40427 0.40150 0.60809 0.07080  -0.01919 0.08555  452 MET A C   
593  O  O   . MET A 73  ? 0.37883 0.38055 0.59049 0.07292  -0.00662 0.06930  452 MET A O   
594  C  CB  . MET A 73  ? 0.44075 0.38781 0.67512 0.08854  -0.00899 0.08946  452 MET A CB  
595  C  CG  . MET A 73  ? 0.54287 0.45231 0.77756 0.09013  -0.00676 0.09496  452 MET A CG  
596  S  SD  . MET A 73  ? 0.76498 0.65663 1.04940 0.11309  -0.00257 0.10137  452 MET A SD  
597  C  CE  . MET A 73  ? 0.64949 0.49295 0.92484 0.10851  -0.00148 0.10853  452 MET A CE  
598  N  N   . ASN A 74  ? 0.38631 0.40599 0.58353 0.06608  -0.03429 0.09797  453 ASN A N   
599  C  CA  . ASN A 74  ? 0.34425 0.39400 0.54493 0.06170  -0.03758 0.09169  453 ASN A CA  
600  C  C   . ASN A 74  ? 0.34074 0.39242 0.50351 0.04587  -0.03885 0.08585  453 ASN A C   
601  O  O   . ASN A 74  ? 0.36278 0.41995 0.50619 0.03913  -0.05077 0.09630  453 ASN A O   
602  C  CB  . ASN A 74  ? 0.37014 0.44482 0.59507 0.06763  -0.05543 0.10752  453 ASN A CB  
603  C  CG  . ASN A 74  ? 0.42284 0.50292 0.69658 0.08480  -0.05197 0.11052  453 ASN A CG  
604  O  OD1 . ASN A 74  ? 0.45020 0.50576 0.73579 0.09491  -0.04271 0.11096  453 ASN A OD1 
605  N  ND2 . ASN A 74  ? 0.41362 0.52571 0.71953 0.08802  -0.05815 0.11129  453 ASN A ND2 
606  N  N   . PHE A 75  ? 0.29448 0.34056 0.44600 0.04029  -0.02614 0.06934  454 PHE A N   
607  C  CA  . PHE A 75  ? 0.30603 0.35225 0.42823 0.02743  -0.02580 0.06318  454 PHE A CA  
608  C  C   . PHE A 75  ? 0.30214 0.37175 0.42415 0.02146  -0.03115 0.05940  454 PHE A C   
609  O  O   . PHE A 75  ? 0.28724 0.37127 0.43133 0.02502  -0.02916 0.05546  454 PHE A O   
610  C  CB  . PHE A 75  ? 0.28341 0.31309 0.39513 0.02419  -0.01344 0.04953  454 PHE A CB  
611  C  CG  . PHE A 75  ? 0.30665 0.31238 0.41252 0.02447  -0.01071 0.05181  454 PHE A CG  
612  C  CD1 . PHE A 75  ? 0.36623 0.35564 0.48745 0.03344  -0.00559 0.05086  454 PHE A CD1 
613  C  CD2 . PHE A 75  ? 0.31687 0.31614 0.40496 0.01535  -0.01217 0.05452  454 PHE A CD2 
614  C  CE1 . PHE A 75  ? 0.35353 0.31846 0.47094 0.03197  -0.00376 0.05237  454 PHE A CE1 
615  C  CE2 . PHE A 75  ? 0.30152 0.27982 0.38850 0.01359  -0.00970 0.05733  454 PHE A CE2 
616  C  CZ  . PHE A 75  ? 0.32542 0.28557 0.42631 0.02125  -0.00643 0.05621  454 PHE A CZ  
617  N  N   . GLU A 76  ? 0.29501 0.36768 0.39322 0.01168  -0.03666 0.05998  455 GLU A N   
618  C  CA  . GLU A 76  ? 0.32046 0.41023 0.41408 0.00375  -0.04186 0.05407  455 GLU A CA  
619  C  C   . GLU A 76  ? 0.27182 0.35306 0.33981 -0.00577 -0.03587 0.04522  455 GLU A C   
620  O  O   . GLU A 76  ? 0.27486 0.34218 0.32890 -0.00694 -0.03080 0.04710  455 GLU A O   
621  C  CB  . GLU A 76  ? 0.33766 0.44342 0.43058 0.00220  -0.05902 0.06475  455 GLU A CB  
622  C  CG  . GLU A 76  ? 0.50787 0.63662 0.63362 0.00565  -0.06700 0.06560  455 GLU A CG  
623  C  CD  . GLU A 76  ? 0.54240 0.67956 0.67676 -0.00119 -0.05914 0.05100  455 GLU A CD  
624  O  OE1 . GLU A 76  ? 0.33458 0.46365 0.44539 -0.01075 -0.05442 0.04099  455 GLU A OE1 
625  O  OE2 . GLU A 76  ? 0.52003 0.67147 0.68768 0.00344  -0.05646 0.05033  455 GLU A OE2 
626  N  N   . TRP A 77  ? 0.26569 0.35536 0.33202 -0.01257 -0.03571 0.03545  456 TRP A N   
627  C  CA  . TRP A 77  ? 0.25502 0.33698 0.30234 -0.02014 -0.02967 0.02631  456 TRP A CA  
628  C  C   . TRP A 77  ? 0.27068 0.35625 0.29468 -0.02710 -0.03603 0.02760  456 TRP A C   
629  O  O   . TRP A 77  ? 0.22557 0.32388 0.24797 -0.03019 -0.04823 0.03022  456 TRP A O   
630  C  CB  . TRP A 77  ? 0.26775 0.35236 0.32314 -0.02450 -0.02588 0.01540  456 TRP A CB  
631  C  CG  . TRP A 77  ? 0.25186 0.33068 0.32103 -0.01980 -0.01807 0.01409  456 TRP A CG  
632  C  CD1 . TRP A 77  ? 0.23082 0.31783 0.31814 -0.01827 -0.01638 0.01395  456 TRP A CD1 
633  C  CD2 . TRP A 77  ? 0.22705 0.29102 0.29103 -0.01713 -0.01077 0.01271  456 TRP A CD2 
634  N  NE1 . TRP A 77  ? 0.25349 0.32924 0.34099 -0.01497 -0.00699 0.01236  456 TRP A NE1 
635  C  CE2 . TRP A 77  ? 0.22406 0.28552 0.29668 -0.01442 -0.00553 0.01154  456 TRP A CE2 
636  C  CE3 . TRP A 77  ? 0.23803 0.29189 0.29193 -0.01769 -0.00829 0.01238  456 TRP A CE3 
637  C  CZ2 . TRP A 77  ? 0.24462 0.29215 0.31036 -0.01264 -0.00066 0.00998  456 TRP A CZ2 
638  C  CZ3 . TRP A 77  ? 0.23727 0.28010 0.29196 -0.01571 -0.00462 0.01104  456 TRP A CZ3 
639  C  CH2 . TRP A 77  ? 0.24539 0.28422 0.30309 -0.01342 -0.00219 0.00979  456 TRP A CH2 
640  N  N   . SER A 78  ? 0.25302 0.32826 0.25867 -0.03036 -0.02761 0.02535  457 SER A N   
641  C  CA  . SER A 78  ? 0.27363 0.35002 0.25040 -0.03798 -0.02961 0.02516  457 SER A CA  
642  C  C   . SER A 78  ? 0.30457 0.38751 0.27296 -0.04600 -0.03397 0.01195  457 SER A C   
643  O  O   . SER A 78  ? 0.30225 0.38968 0.24553 -0.05314 -0.04228 0.01192  457 SER A O   
644  C  CB  . SER A 78  ? 0.30475 0.37040 0.26883 -0.04037 -0.01472 0.02263  457 SER A CB  
645  O  OG  . SER A 78  ? 0.31014 0.37175 0.28780 -0.04010 -0.00450 0.00964  457 SER A OG  
646  N  N   . ASP A 79  ? 0.28661 0.36840 0.27363 -0.04602 -0.02936 0.00103  458 ASP A N   
647  C  CA  . ASP A 79  ? 0.31343 0.39752 0.29552 -0.05480 -0.03239 -0.01277 458 ASP A CA  
648  C  C   . ASP A 79  ? 0.30924 0.40933 0.30407 -0.05804 -0.04866 -0.00990 458 ASP A C   
649  O  O   . ASP A 79  ? 0.31247 0.41520 0.30545 -0.06742 -0.05358 -0.02157 458 ASP A O   
650  C  CB  . ASP A 79  ? 0.31656 0.39003 0.31455 -0.05418 -0.02073 -0.02388 458 ASP A CB  
651  C  CG  . ASP A 79  ? 0.31257 0.38863 0.33881 -0.04899 -0.02141 -0.01859 458 ASP A CG  
652  O  OD1 . ASP A 79  ? 0.29824 0.38561 0.33606 -0.04556 -0.02884 -0.00910 458 ASP A OD1 
653  O  OD2 . ASP A 79  ? 0.31049 0.37634 0.34729 -0.04809 -0.01345 -0.02367 458 ASP A OD2 
654  N  N   . GLY A 80  ? 0.29708 0.40799 0.30838 -0.05076 -0.05691 0.00457  459 GLY A N   
655  C  CA  . GLY A 80  ? 0.27558 0.40621 0.30590 -0.05282 -0.07300 0.00887  459 GLY A CA  
656  C  C   . GLY A 80  ? 0.26042 0.39890 0.32692 -0.05156 -0.06887 0.00556  459 GLY A C   
657  O  O   . GLY A 80  ? 0.27961 0.43811 0.37019 -0.05370 -0.08077 0.00879  459 GLY A O   
658  N  N   . SER A 81  ? 0.27750 0.40208 0.34939 -0.04878 -0.05285 0.00033  460 SER A N   
659  C  CA  . SER A 81  ? 0.26998 0.39956 0.37053 -0.04846 -0.04646 -0.00092 460 SER A CA  
660  C  C   . SER A 81  ? 0.28680 0.42435 0.40893 -0.03710 -0.04341 0.00991  460 SER A C   
661  O  O   . SER A 81  ? 0.27413 0.40760 0.38873 -0.02873 -0.04481 0.01773  460 SER A O   
662  C  CB  . SER A 81  ? 0.24345 0.35336 0.33784 -0.04961 -0.03224 -0.00798 460 SER A CB  
663  O  OG  . SER A 81  ? 0.25675 0.35309 0.33845 -0.04118 -0.02472 -0.00404 460 SER A OG  
664  N  N   . LEU A 82  ? 0.25308 0.40091 0.40327 -0.03734 -0.03753 0.00984  461 LEU A N   
665  C  CA  . LEU A 82  ? 0.27053 0.42614 0.44419 -0.02653 -0.03081 0.01709  461 LEU A CA  
666  C  C   . LEU A 82  ? 0.27899 0.41253 0.43618 -0.01925 -0.01624 0.01658  461 LEU A C   
667  O  O   . LEU A 82  ? 0.25762 0.37484 0.39652 -0.02365 -0.00913 0.01143  461 LEU A O   
668  C  CB  . LEU A 82  ? 0.25529 0.42847 0.46319 -0.03032 -0.02430 0.01592  461 LEU A CB  
669  C  CG  . LEU A 82  ? 0.29942 0.49799 0.53211 -0.03969 -0.03962 0.01551  461 LEU A CG  
670  C  CD1 . LEU A 82  ? 0.23841 0.45257 0.50775 -0.04443 -0.02811 0.01443  461 LEU A CD1 
671  C  CD2 . LEU A 82  ? 0.33468 0.55190 0.58242 -0.03203 -0.05667 0.02496  461 LEU A CD2 
672  N  N   . VAL A 83  ? 0.27673 0.40917 0.44228 -0.00809 -0.01288 0.02191  462 VAL A N   
673  C  CA  . VAL A 83  ? 0.27719 0.38913 0.42869 -0.00233 0.00038  0.01947  462 VAL A CA  
674  C  C   . VAL A 83  ? 0.27973 0.39653 0.44709 -0.00184 0.01561  0.01627  462 VAL A C   
675  O  O   . VAL A 83  ? 0.33360 0.46051 0.52571 0.00607  0.02237  0.01779  462 VAL A O   
676  C  CB  . VAL A 83  ? 0.30850 0.41195 0.45987 0.00803  -0.00140 0.02446  462 VAL A CB  
677  C  CG1 . VAL A 83  ? 0.28186 0.36255 0.41629 0.01125  0.01077  0.01899  462 VAL A CG1 
678  C  CG2 . VAL A 83  ? 0.26939 0.36912 0.40418 0.00579  -0.01459 0.02991  462 VAL A CG2 
679  N  N   . SER A 84  ? 0.25295 0.36209 0.40708 -0.01027 0.02228  0.01247  463 SER A N   
680  C  CA  . SER A 84  ? 0.28281 0.39379 0.44486 -0.01228 0.03885  0.01092  463 SER A CA  
681  C  C   . SER A 84  ? 0.29245 0.37968 0.42448 -0.00999 0.05042  0.00802  463 SER A C   
682  O  O   . SER A 84  ? 0.31195 0.39754 0.44280 -0.01109 0.06682  0.00667  463 SER A O   
683  C  CB  . SER A 84  ? 0.28960 0.40543 0.45617 -0.02470 0.03883  0.01092  463 SER A CB  
684  O  OG  . SER A 84  ? 0.27269 0.40747 0.46040 -0.02937 0.02462  0.01120  463 SER A OG  
685  N  N   . PHE A 85  ? 0.26825 0.33794 0.37578 -0.00792 0.04227  0.00699  464 PHE A N   
686  C  CA  . PHE A 85  ? 0.29668 0.34374 0.37302 -0.00834 0.04699  0.00422  464 PHE A CA  
687  C  C   . PHE A 85  ? 0.26536 0.30116 0.33214 -0.00317 0.03827  0.00248  464 PHE A C   
688  O  O   . PHE A 85  ? 0.25580 0.29627 0.32850 -0.00335 0.02683  0.00532  464 PHE A O   
689  C  CB  . PHE A 85  ? 0.27985 0.31731 0.33853 -0.01680 0.04273  0.00701  464 PHE A CB  
690  C  CG  . PHE A 85  ? 0.28077 0.29705 0.30836 -0.01760 0.04080  0.00637  464 PHE A CG  
691  C  CD1 . PHE A 85  ? 0.30676 0.31168 0.31197 -0.01994 0.05182  0.00601  464 PHE A CD1 
692  C  CD2 . PHE A 85  ? 0.29802 0.30671 0.31842 -0.01692 0.02775  0.00628  464 PHE A CD2 
693  C  CE1 . PHE A 85  ? 0.33155 0.31711 0.30452 -0.02196 0.04615  0.00578  464 PHE A CE1 
694  C  CE2 . PHE A 85  ? 0.29902 0.29123 0.29526 -0.01853 0.02254  0.00617  464 PHE A CE2 
695  C  CZ  . PHE A 85  ? 0.34400 0.32431 0.31499 -0.02119 0.02993  0.00598  464 PHE A CZ  
696  N  N   . THR A 86  ? 0.29425 0.31421 0.34512 0.00020  0.04470  -0.00278 465 THR A N   
697  C  CA  . THR A 86  ? 0.29240 0.29803 0.33298 0.00223  0.03645  -0.00502 465 THR A CA  
698  C  C   . THR A 86  ? 0.30597 0.29113 0.31499 -0.00207 0.03723  -0.01072 465 THR A C   
699  O  O   . THR A 86  ? 0.33349 0.31312 0.32512 -0.00458 0.04719  -0.01350 465 THR A O   
700  C  CB  . THR A 86  ? 0.31371 0.31767 0.37122 0.01125  0.04006  -0.00689 465 THR A CB  
701  O  OG1 . THR A 86  ? 0.30059 0.29681 0.35453 0.01545  0.05595  -0.01501 465 THR A OG1 
702  C  CG2 . THR A 86  ? 0.29266 0.31767 0.38029 0.01566  0.03551  0.00101  465 THR A CG2 
703  N  N   . HIS A 87  ? 0.27504 0.24931 0.27604 -0.00398 0.02624  -0.01195 466 HIS A N   
704  C  CA  . HIS A 87  ? 0.32752 0.28401 0.29991 -0.00948 0.02151  -0.01708 466 HIS A CA  
705  C  C   . HIS A 87  ? 0.34357 0.28811 0.31795 -0.00970 0.01414  -0.02190 466 HIS A C   
706  O  O   . HIS A 87  ? 0.32817 0.27015 0.30058 -0.01508 0.00127  -0.02029 466 HIS A O   
707  C  CB  . HIS A 87  ? 0.33212 0.29191 0.29656 -0.01549 0.01084  -0.01005 466 HIS A CB  
708  C  CG  . HIS A 87  ? 0.40050 0.34489 0.33145 -0.02132 0.00642  -0.01193 466 HIS A CG  
709  N  ND1 . HIS A 87  ? 0.41625 0.35598 0.34008 -0.02618 -0.01075 -0.00896 466 HIS A ND1 
710  C  CD2 . HIS A 87  ? 0.42191 0.35501 0.32321 -0.02356 0.01649  -0.01580 466 HIS A CD2 
711  C  CE1 . HIS A 87  ? 0.45203 0.37776 0.34103 -0.03138 -0.01428 -0.00993 466 HIS A CE1 
712  N  NE2 . HIS A 87  ? 0.48361 0.40377 0.35489 -0.03036 0.00331  -0.01438 466 HIS A NE2 
713  N  N   . TRP A 88  ? 0.32845 0.26547 0.31131 -0.00373 0.02285  -0.02755 467 TRP A N   
714  C  CA  . TRP A 88  ? 0.33407 0.25732 0.32304 -0.00433 0.01715  -0.03094 467 TRP A CA  
715  C  C   . TRP A 88  ? 0.36319 0.26449 0.32446 -0.01185 0.01236  -0.04277 467 TRP A C   
716  O  O   . TRP A 88  ? 0.38996 0.28043 0.32464 -0.01292 0.02009  -0.05199 467 TRP A O   
717  C  CB  . TRP A 88  ? 0.35398 0.27225 0.36250 0.00546  0.02772  -0.03254 467 TRP A CB  
718  C  CG  . TRP A 88  ? 0.32302 0.26173 0.35964 0.01226  0.02767  -0.01993 467 TRP A CG  
719  C  CD1 . TRP A 88  ? 0.32669 0.28111 0.37922 0.01967  0.03629  -0.01702 467 TRP A CD1 
720  C  CD2 . TRP A 88  ? 0.31124 0.25720 0.36226 0.01117  0.01800  -0.00856 467 TRP A CD2 
721  N  NE1 . TRP A 88  ? 0.31300 0.28397 0.38751 0.02292  0.02917  -0.00460 467 TRP A NE1 
722  C  CE2 . TRP A 88  ? 0.30519 0.26994 0.37537 0.01775  0.01889  0.00077  467 TRP A CE2 
723  C  CE3 . TRP A 88  ? 0.31272 0.25207 0.36231 0.00422  0.00921  -0.00519 467 TRP A CE3 
724  C  CZ2 . TRP A 88  ? 0.27627 0.25053 0.35646 0.01741  0.01067  0.01309  467 TRP A CZ2 
725  C  CZ3 . TRP A 88  ? 0.31383 0.26322 0.37594 0.00420  0.00469  0.00723  467 TRP A CZ3 
726  C  CH2 . TRP A 88  ? 0.27757 0.24279 0.35112 0.01071  0.00513  0.01617  467 TRP A CH2 
727  N  N   . HIS A 89  ? 0.34942 0.24378 0.31626 -0.01815 0.00006  -0.04302 468 HIS A N   
728  C  CA  . HIS A 89  ? 0.40404 0.27462 0.35017 -0.02552 -0.00500 -0.05665 468 HIS A CA  
729  C  C   . HIS A 89  ? 0.42710 0.27721 0.37008 -0.01869 0.01093  -0.06879 468 HIS A C   
730  O  O   . HIS A 89  ? 0.40860 0.26339 0.37803 -0.00870 0.02042  -0.06299 468 HIS A O   
731  C  CB  . HIS A 89  ? 0.38984 0.25783 0.35360 -0.03355 -0.01885 -0.05439 468 HIS A CB  
732  C  CG  . HIS A 89  ? 0.40558 0.28947 0.37164 -0.04142 -0.03517 -0.04736 468 HIS A CG  
733  N  ND1 . HIS A 89  ? 0.43230 0.30891 0.37542 -0.05091 -0.04969 -0.05419 468 HIS A ND1 
734  C  CD2 . HIS A 89  ? 0.37332 0.27970 0.36348 -0.04072 -0.03937 -0.03443 468 HIS A CD2 
735  C  CE1 . HIS A 89  ? 0.40891 0.30456 0.36748 -0.05440 -0.06305 -0.04410 468 HIS A CE1 
736  N  NE2 . HIS A 89  ? 0.38238 0.29559 0.36994 -0.04811 -0.05526 -0.03321 468 HIS A NE2 
737  N  N   . PRO A 90  ? 0.47575 0.30244 0.38686 -0.02365 0.01375  -0.08585 469 PRO A N   
738  C  CA  . PRO A 90  ? 0.51217 0.31559 0.42328 -0.01661 0.03089  -0.10038 469 PRO A CA  
739  C  C   . PRO A 90  ? 0.49053 0.28369 0.43554 -0.01381 0.02828  -0.09708 469 PRO A C   
740  O  O   . PRO A 90  ? 0.48245 0.27316 0.43476 -0.02364 0.01266  -0.09339 469 PRO A O   
741  C  CB  . PRO A 90  ? 0.58028 0.35695 0.44554 -0.02727 0.02897  -0.12101 469 PRO A CB  
742  C  CG  . PRO A 90  ? 0.63308 0.42393 0.47208 -0.03731 0.01271  -0.11364 469 PRO A CG  
743  C  CD  . PRO A 90  ? 0.53383 0.35146 0.40894 -0.03675 -0.00099 -0.09334 469 PRO A CD  
744  N  N   . PHE A 91  ? 0.48446 0.27352 0.45376 -0.00010 0.04383  -0.09619 470 PHE A N   
745  C  CA  . PHE A 91  ? 0.49039 0.26663 0.49306 0.00605  0.04468  -0.09036 470 PHE A CA  
746  C  C   . PHE A 91  ? 0.45320 0.25330 0.48287 0.00666  0.03369  -0.06647 470 PHE A C   
747  O  O   . PHE A 91  ? 0.47864 0.26903 0.53362 0.01073  0.03296  -0.05702 470 PHE A O   
748  C  CB  . PHE A 91  ? 0.50267 0.24382 0.49630 -0.00413 0.03952  -0.10536 470 PHE A CB  
749  C  CG  . PHE A 91  ? 0.53937 0.25160 0.50467 -0.00389 0.05287  -0.13159 470 PHE A CG  
750  C  CD1 . PHE A 91  ? 0.55562 0.24783 0.53835 0.01033  0.07240  -0.14058 470 PHE A CD1 
751  C  CD2 . PHE A 91  ? 0.55816 0.26391 0.47858 -0.01709 0.04662  -0.14691 470 PHE A CD2 
752  C  CE1 . PHE A 91  ? 0.60591 0.27060 0.56121 0.01100  0.08858  -0.16712 470 PHE A CE1 
753  C  CE2 . PHE A 91  ? 0.60919 0.28683 0.49596 -0.01793 0.06058  -0.17235 470 PHE A CE2 
754  C  CZ  . PHE A 91  ? 0.63426 0.29100 0.53790 -0.00398 0.08326  -0.18379 470 PHE A CZ  
755  N  N   . GLU A 92  ? 0.40216 0.22997 0.42601 0.00300  0.02652  -0.05665 471 GLU A N   
756  C  CA  . GLU A 92  ? 0.38544 0.23713 0.43063 0.00526  0.02034  -0.03640 471 GLU A CA  
757  C  C   . GLU A 92  ? 0.36705 0.23995 0.42403 0.01710  0.02820  -0.02920 471 GLU A C   
758  O  O   . GLU A 92  ? 0.38453 0.26240 0.42959 0.01969  0.03677  -0.03800 471 GLU A O   
759  C  CB  . GLU A 92  ? 0.36170 0.23146 0.39757 -0.00581 0.00831  -0.03099 471 GLU A CB  
760  C  CG  . GLU A 92  ? 0.37372 0.22944 0.40153 -0.01894 -0.00183 -0.03846 471 GLU A CG  
761  C  CD  . GLU A 92  ? 0.43783 0.27964 0.48615 -0.02286 -0.00391 -0.03251 471 GLU A CD  
762  O  OE1 . GLU A 92  ? 0.41515 0.26092 0.48129 -0.01558 0.00076  -0.01858 471 GLU A OE1 
763  O  OE2 . GLU A 92  ? 0.43172 0.25808 0.47787 -0.03432 -0.01121 -0.04101 471 GLU A OE2 
764  N  N   . PRO A 93  ? 0.35676 0.24339 0.43619 0.02305  0.02487  -0.01261 472 PRO A N   
765  C  CA  . PRO A 93  ? 0.36891 0.25105 0.45912 0.01957  0.01671  0.00123  472 PRO A CA  
766  C  C   . PRO A 93  ? 0.39430 0.24692 0.49877 0.02452  0.02050  0.00062  472 PRO A C   
767  O  O   . PRO A 93  ? 0.35983 0.20406 0.47754 0.03663  0.02915  -0.00379 472 PRO A O   
768  C  CB  . PRO A 93  ? 0.34014 0.24824 0.44193 0.02509  0.01267  0.01786  472 PRO A CB  
769  C  CG  . PRO A 93  ? 0.33505 0.25285 0.44860 0.03659  0.02034  0.01332  472 PRO A CG  
770  C  CD  . PRO A 93  ? 0.32168 0.23145 0.41652 0.03296  0.02893  -0.00549 472 PRO A CD  
771  N  N   . ASN A 94  ? 0.39675 0.23232 0.50241 0.01542  0.01550  0.00470  473 ASN A N   
772  C  CA  . ASN A 94  ? 0.43664 0.23916 0.55653 0.01862  0.01923  0.00367  473 ASN A CA  
773  C  C   . ASN A 94  ? 0.43029 0.22752 0.56564 0.01783  0.01438  0.02668  473 ASN A C   
774  O  O   . ASN A 94  ? 0.46296 0.22994 0.61279 0.02030  0.01701  0.02916  473 ASN A O   
775  C  CB  . ASN A 94  ? 0.45375 0.23035 0.56059 0.00633  0.01908  -0.01615 473 ASN A CB  
776  C  CG  . ASN A 94  ? 0.43514 0.21911 0.53694 -0.01100 0.00900  -0.01174 473 ASN A CG  
777  O  OD1 . ASN A 94  ? 0.40508 0.21394 0.50948 -0.01355 0.00497  0.00385  473 ASN A OD1 
778  N  ND2 . ASN A 94  ? 0.45288 0.21540 0.54887 -0.02343 0.00529  -0.02687 473 ASN A ND2 
779  N  N   . ASN A 95  ? 0.43696 0.26016 0.56763 0.01419  0.00838  0.04339  474 ASN A N   
780  C  CA  . ASN A 95  ? 0.45961 0.28011 0.59715 0.01305  0.00459  0.06770  474 ASN A CA  
781  C  C   . ASN A 95  ? 0.54496 0.33321 0.69078 0.00362  0.00652  0.07059  474 ASN A C   
782  O  O   . ASN A 95  ? 0.60039 0.36760 0.75938 0.00830  0.00653  0.08699  474 ASN A O   
783  C  CB  . ASN A 95  ? 0.51116 0.33447 0.66335 0.02955  0.00206  0.08283  474 ASN A CB  
784  C  CG  . ASN A 95  ? 0.51219 0.34350 0.65959 0.02753  -0.00535 0.11006  474 ASN A CG  
785  O  OD1 . ASN A 95  ? 0.48623 0.34250 0.61497 0.02000  -0.00859 0.11481  474 ASN A OD1 
786  N  ND2 . ASN A 95  ? 0.60321 0.41144 0.76543 0.03423  -0.00772 0.12817  474 ASN A ND2 
787  N  N   . PHE A 96  ? 0.51222 0.29678 0.65212 -0.01066 0.00686  0.05566  475 PHE A N   
788  C  CA  . PHE A 96  ? 0.58044 0.33272 0.73149 -0.02134 0.00825  0.05227  475 PHE A CA  
789  C  C   . PHE A 96  ? 0.67365 0.42101 0.83243 -0.03011 0.00914  0.07683  475 PHE A C   
790  O  O   . PHE A 96  ? 0.74582 0.46229 0.91831 -0.02889 0.01136  0.08810  475 PHE A O   
791  C  CB  . PHE A 96  ? 0.52293 0.27789 0.66717 -0.03579 0.00481  0.03097  475 PHE A CB  
792  C  CG  . PHE A 96  ? 0.57509 0.29777 0.73196 -0.04901 0.00419  0.02372  475 PHE A CG  
793  C  CD1 . PHE A 96  ? 0.57262 0.26041 0.73101 -0.04496 0.00665  0.00641  475 PHE A CD1 
794  C  CD2 . PHE A 96  ? 0.63184 0.35832 0.80098 -0.06612 0.00264  0.03326  475 PHE A CD2 
795  C  CE1 . PHE A 96  ? 0.57220 0.23251 0.73643 -0.05764 0.00519  -0.00232 475 PHE A CE1 
796  C  CE2 . PHE A 96  ? 0.63421 0.33520 0.81388 -0.07918 0.00140  0.02585  475 PHE A CE2 
797  C  CZ  . PHE A 96  ? 0.61273 0.28163 0.78629 -0.07485 0.00162  0.00782  475 PHE A CZ  
798  N  N   . ARG A 97  ? 0.79528 0.57086 0.94539 -0.03946 0.00906  0.08524  476 ARG A N   
799  C  CA  . ARG A 97  ? 0.77103 0.54434 0.92446 -0.05074 0.01351  0.10700  476 ARG A CA  
800  C  C   . ARG A 97  ? 0.86299 0.63771 1.00606 -0.04020 0.01301  0.13241  476 ARG A C   
801  O  O   . ARG A 97  ? 0.79556 0.59587 0.92354 -0.03128 0.00941  0.13428  476 ARG A O   
802  C  CB  . ARG A 97  ? 0.73528 0.53929 0.88484 -0.06375 0.01641  0.10391  476 ARG A CB  
803  C  CG  . ARG A 97  ? 0.81809 0.61925 0.97655 -0.07987 0.02516  0.12056  476 ARG A CG  
804  C  CD  . ARG A 97  ? 0.88486 0.66838 1.06682 -0.09433 0.02485  0.10926  476 ARG A CD  
805  N  NE  . ARG A 97  ? 0.89479 0.64284 1.07878 -0.08867 0.02126  0.10483  476 ARG A NE  
806  C  CZ  . ARG A 97  ? 0.90772 0.63638 1.10330 -0.09921 0.01997  0.09363  476 ARG A CZ  
807  N  NH1 . ARG A 97  ? 0.89608 0.63928 1.10481 -0.11601 0.02027  0.08666  476 ARG A NH1 
808  N  NH2 . ARG A 97  ? 0.92129 0.61612 1.11694 -0.09250 0.01825  0.08902  476 ARG A NH2 
809  N  N   . ASP A 98  ? 0.96527 0.71290 1.11485 -0.04166 0.01494  0.15141  477 ASP A N   
810  C  CA  . ASP A 98  ? 0.97009 0.71907 1.10554 -0.03229 0.01127  0.17656  477 ASP A CA  
811  C  C   . ASP A 98  ? 0.91860 0.66426 1.03941 -0.04608 0.01790  0.19592  477 ASP A C   
812  O  O   . ASP A 98  ? 1.01194 0.77988 1.11715 -0.05653 0.02381  0.20160  477 ASP A O   
813  C  CB  . ASP A 98  ? 1.00313 0.72849 1.15143 -0.01558 0.00580  0.17760  477 ASP A CB  
814  C  CG  . ASP A 98  ? 1.00177 0.73547 1.16194 0.00035  0.00165  0.16143  477 ASP A CG  
815  O  OD1 . ASP A 98  ? 0.93623 0.69953 1.08615 0.00125  -0.00070 0.15670  477 ASP A OD1 
816  O  OD2 . ASP A 98  ? 1.00761 0.72096 1.18437 0.01161  0.00228  0.15072  477 ASP A OD2 
817  N  N   . GLU A 101 ? 0.46939 0.33658 0.56587 -0.02434 0.00459  0.11953  480 GLU A N   
818  C  CA  . GLU A 101 ? 0.39941 0.28771 0.49290 -0.02355 0.00373  0.09895  480 GLU A CA  
819  C  C   . GLU A 101 ? 0.42027 0.32833 0.50408 -0.01289 -0.00170 0.09922  480 GLU A C   
820  O  O   . GLU A 101 ? 0.41563 0.31977 0.50862 -0.00152 -0.00513 0.09446  480 GLU A O   
821  C  CB  . GLU A 101 ? 0.40925 0.28292 0.51499 -0.02191 0.00292  0.07957  480 GLU A CB  
822  C  CG  . GLU A 101 ? 0.46364 0.31610 0.58171 -0.03355 0.00531  0.07620  480 GLU A CG  
823  C  CD  . GLU A 101 ? 0.44858 0.29650 0.56927 -0.03717 0.00219  0.05330  480 GLU A CD  
824  O  OE1 . GLU A 101 ? 0.37450 0.22000 0.48874 -0.02754 0.00078  0.04098  480 GLU A OE1 
825  O  OE2 . GLU A 101 ? 0.49816 0.34621 0.62717 -0.05049 0.00100  0.04806  480 GLU A OE2 
826  N  N   . ASP A 102 ? 0.37435 0.30388 0.44149 -0.01714 -0.00139 0.10306  481 ASP A N   
827  C  CA  . ASP A 102 ? 0.38140 0.32967 0.43972 -0.00972 -0.00816 0.10354  481 ASP A CA  
828  C  C   . ASP A 102 ? 0.36143 0.33112 0.41082 -0.01370 -0.00611 0.08926  481 ASP A C   
829  O  O   . ASP A 102 ? 0.31609 0.30145 0.35802 -0.01016 -0.01166 0.08865  481 ASP A O   
830  C  CB  . ASP A 102 ? 0.40511 0.35590 0.44681 -0.01000 -0.01366 0.12454  481 ASP A CB  
831  C  CG  . ASP A 102 ? 0.43508 0.36462 0.48830 -0.00293 -0.01871 0.14218  481 ASP A CG  
832  O  OD1 . ASP A 102 ? 0.42788 0.34534 0.50467 0.00653  -0.01938 0.13559  481 ASP A OD1 
833  O  OD2 . ASP A 102 ? 0.45386 0.37727 0.49125 -0.00672 -0.02126 0.16293  481 ASP A OD2 
834  N  N   . CYS A 103 ? 0.34228 0.31291 0.39529 -0.02104 0.00056  0.07838  482 CYS A N   
835  C  CA  . CYS A 103 ? 0.29647 0.28421 0.34537 -0.02382 0.00281  0.06594  482 CYS A CA  
836  C  C   . CYS A 103 ? 0.28785 0.27185 0.34972 -0.02301 0.00182  0.05208  482 CYS A C   
837  O  O   . CYS A 103 ? 0.33064 0.29971 0.40225 -0.02479 0.00151  0.05062  482 CYS A O   
838  C  CB  . CYS A 103 ? 0.33934 0.33438 0.38144 -0.03322 0.01194  0.06806  482 CYS A CB  
839  S  SG  . CYS A 103 ? 0.37476 0.37217 0.38921 -0.03673 0.01401  0.08435  482 CYS A SG  
840  N  N   . VAL A 104 ? 0.25482 0.25045 0.31484 -0.02148 0.00062  0.04211  483 VAL A N   
841  C  CA  . VAL A 104 ? 0.24920 0.24019 0.31417 -0.01967 -0.00239 0.03139  483 VAL A CA  
842  C  C   . VAL A 104 ? 0.23906 0.23741 0.30992 -0.02492 -0.00244 0.02501  483 VAL A C   
843  O  O   . VAL A 104 ? 0.24734 0.25812 0.31774 -0.02605 0.00088  0.02436  483 VAL A O   
844  C  CB  . VAL A 104 ? 0.24125 0.23720 0.30150 -0.01286 -0.00405 0.02752  483 VAL A CB  
845  C  CG1 . VAL A 104 ? 0.23636 0.22655 0.29444 -0.01261 -0.00528 0.01756  483 VAL A CG1 
846  C  CG2 . VAL A 104 ? 0.24837 0.23836 0.31213 -0.00585 -0.00461 0.03391  483 VAL A CG2 
847  N  N   . THR A 105 ? 0.27278 0.26281 0.35003 -0.02792 -0.00706 0.01973  484 THR A N   
848  C  CA  . THR A 105 ? 0.24617 0.24347 0.33329 -0.03170 -0.01141 0.01501  484 THR A CA  
849  C  C   . THR A 105 ? 0.28694 0.27849 0.36296 -0.02929 -0.01889 0.00851  484 THR A C   
850  O  O   . THR A 105 ? 0.29590 0.27545 0.35825 -0.02654 -0.01893 0.00532  484 THR A O   
851  C  CB  . THR A 105 ? 0.29741 0.29214 0.40231 -0.03971 -0.01431 0.01535  484 THR A CB  
852  O  OG1 . THR A 105 ? 0.29221 0.26892 0.39064 -0.04186 -0.02101 0.01057  484 THR A OG1 
853  C  CG2 . THR A 105 ? 0.29748 0.29501 0.41106 -0.04377 -0.00442 0.02354  484 THR A CG2 
854  N  N   . ILE A 106 ? 0.27974 0.27932 0.36171 -0.02997 -0.02409 0.00719  485 ILE A N   
855  C  CA  A ILE A 106 ? 0.31707 0.30996 0.38753 -0.03037 -0.03405 0.00373  485 ILE A CA  
856  C  CA  B ILE A 106 ? 0.31519 0.30744 0.38506 -0.03043 -0.03396 0.00357  485 ILE A CA  
857  C  C   . ILE A 106 ? 0.30180 0.29463 0.38592 -0.03711 -0.04581 0.00246  485 ILE A C   
858  O  O   . ILE A 106 ? 0.30158 0.30779 0.41262 -0.03924 -0.04572 0.00553  485 ILE A O   
859  C  CB  A ILE A 106 ? 0.30232 0.30253 0.37271 -0.02672 -0.03479 0.00608  485 ILE A CB  
860  C  CB  B ILE A 106 ? 0.30253 0.30029 0.36804 -0.02655 -0.03451 0.00553  485 ILE A CB  
861  C  CG1 A ILE A 106 ? 0.29722 0.29709 0.35441 -0.02238 -0.02549 0.00614  485 ILE A CG1 
862  C  CG1 B ILE A 106 ? 0.28784 0.29857 0.37828 -0.02617 -0.03637 0.00845  485 ILE A CG1 
863  C  CG2 A ILE A 106 ? 0.31411 0.30791 0.37444 -0.02850 -0.04781 0.00650  485 ILE A CG2 
864  C  CG2 B ILE A 106 ? 0.29548 0.29539 0.35251 -0.02220 -0.02380 0.00597  485 ILE A CG2 
865  C  CD1 A ILE A 106 ? 0.31429 0.31745 0.37248 -0.02046 -0.02592 0.00825  485 ILE A CD1 
866  C  CD1 B ILE A 106 ? 0.32382 0.33541 0.41231 -0.02202 -0.03643 0.01064  485 ILE A CD1 
867  N  N   . TRP A 107 ? 0.32118 0.29990 0.38814 -0.04119 -0.05536 -0.00295 486 TRP A N   
868  C  CA  . TRP A 107 ? 0.33738 0.31802 0.41800 -0.04922 -0.07086 -0.00447 486 TRP A CA  
869  C  C   . TRP A 107 ? 0.36839 0.33500 0.41859 -0.05278 -0.08485 -0.00972 486 TRP A C   
870  O  O   . TRP A 107 ? 0.34228 0.29322 0.36050 -0.05055 -0.07829 -0.01504 486 TRP A O   
871  C  CB  . TRP A 107 ? 0.34243 0.31936 0.44078 -0.05647 -0.06891 -0.00691 486 TRP A CB  
872  C  CG  . TRP A 107 ? 0.37656 0.32955 0.45300 -0.05965 -0.06770 -0.01548 486 TRP A CG  
873  C  CD1 . TRP A 107 ? 0.38244 0.32367 0.45122 -0.05472 -0.05358 -0.01574 486 TRP A CD1 
874  C  CD2 . TRP A 107 ? 0.41009 0.34678 0.47151 -0.06847 -0.08155 -0.02578 486 TRP A CD2 
875  N  NE1 . TRP A 107 ? 0.43373 0.35096 0.48661 -0.05847 -0.05544 -0.02616 486 TRP A NE1 
876  C  CE2 . TRP A 107 ? 0.43951 0.35251 0.48460 -0.06780 -0.07201 -0.03387 486 TRP A CE2 
877  C  CE3 . TRP A 107 ? 0.44400 0.38333 0.50368 -0.07697 -0.10243 -0.02914 486 TRP A CE3 
878  C  CZ2 . TRP A 107 ? 0.49578 0.38513 0.52042 -0.07586 -0.08005 -0.04797 486 TRP A CZ2 
879  C  CZ3 . TRP A 107 ? 0.47458 0.39214 0.51068 -0.08640 -0.11327 -0.04215 486 TRP A CZ3 
880  C  CH2 . TRP A 107 ? 0.51285 0.40443 0.53042 -0.08607 -0.10081 -0.05281 486 TRP A CH2 
881  N  N   . GLY A 108 ? 0.36024 0.33388 0.42101 -0.05829 -0.10405 -0.00763 487 GLY A N   
882  C  CA  . GLY A 108 ? 0.39291 0.35364 0.42054 -0.06351 -0.12103 -0.01112 487 GLY A CA  
883  C  C   . GLY A 108 ? 0.40131 0.36531 0.41479 -0.05743 -0.12515 -0.00154 487 GLY A C   
884  O  O   . GLY A 108 ? 0.37939 0.35221 0.40599 -0.04895 -0.11223 0.00504  487 GLY A O   
885  N  N   . PRO A 109 ? 0.41131 0.36611 0.39529 -0.06273 -0.14405 -0.00032 488 PRO A N   
886  C  CA  . PRO A 109 ? 0.44657 0.40273 0.41870 -0.05780 -0.15086 0.01261  488 PRO A CA  
887  C  C   . PRO A 109 ? 0.47826 0.42162 0.41638 -0.05282 -0.13105 0.01327  488 PRO A C   
888  O  O   . PRO A 109 ? 0.47103 0.41707 0.41129 -0.04740 -0.12976 0.02502  488 PRO A O   
889  C  CB  . PRO A 109 ? 0.52062 0.46903 0.46578 -0.06704 -0.17931 0.01443  488 PRO A CB  
890  C  CG  . PRO A 109 ? 0.56510 0.49887 0.48670 -0.07710 -0.17972 -0.00286 488 PRO A CG  
891  C  CD  . PRO A 109 ? 0.48571 0.42826 0.44743 -0.07471 -0.16255 -0.00981 488 PRO A CD  
892  N  N   . GLU A 110 ? 0.46737 0.39716 0.37893 -0.05435 -0.11498 0.00132  489 GLU A N   
893  C  CA  . GLU A 110 ? 0.50271 0.42491 0.39080 -0.04968 -0.09439 0.00183  489 GLU A CA  
894  C  C   . GLU A 110 ? 0.41310 0.34854 0.33449 -0.04157 -0.07574 0.00297  489 GLU A C   
895  O  O   . GLU A 110 ? 0.43586 0.36944 0.34708 -0.03799 -0.05936 0.00378  489 GLU A O   
896  C  CB  . GLU A 110 ? 0.55346 0.45588 0.40029 -0.05383 -0.08404 -0.01204 489 GLU A CB  
897  C  CG  . GLU A 110 ? 0.70383 0.58903 0.49863 -0.06206 -0.09627 -0.01200 489 GLU A CG  
898  C  CD  . GLU A 110 ? 0.86838 0.73493 0.63266 -0.07051 -0.10068 -0.02997 489 GLU A CD  
899  O  OE1 . GLU A 110 ? 0.88055 0.74873 0.67238 -0.07074 -0.10009 -0.03988 489 GLU A OE1 
900  O  OE2 . GLU A 110 ? 0.95623 0.80436 0.66671 -0.07780 -0.10422 -0.03443 489 GLU A OE2 
901  N  N   . GLY A 111 ? 0.39946 0.34883 0.35949 -0.03967 -0.07779 0.00320  490 GLY A N   
902  C  CA  . GLY A 111 ? 0.36117 0.32208 0.34588 -0.03336 -0.06219 0.00454  490 GLY A CA  
903  C  C   . GLY A 111 ? 0.35525 0.31155 0.33438 -0.03115 -0.04674 -0.00294 490 GLY A C   
904  O  O   . GLY A 111 ? 0.32412 0.28866 0.31458 -0.02631 -0.03492 -0.00091 490 GLY A O   
905  N  N   . ARG A 112 ? 0.35473 0.29744 0.31847 -0.03455 -0.04758 -0.01181 491 ARG A N   
906  C  CA  . ARG A 112 ? 0.35198 0.28858 0.31544 -0.03046 -0.03290 -0.01816 491 ARG A CA  
907  C  C   . ARG A 112 ? 0.33255 0.27755 0.32636 -0.02871 -0.03091 -0.01529 491 ARG A C   
908  O  O   . ARG A 112 ? 0.31983 0.27298 0.33223 -0.03255 -0.03949 -0.01152 491 ARG A O   
909  C  CB  . ARG A 112 ? 0.38372 0.29871 0.31993 -0.03421 -0.03237 -0.03041 491 ARG A CB  
910  C  CG  . ARG A 112 ? 0.42802 0.33372 0.32711 -0.03579 -0.02871 -0.03297 491 ARG A CG  
911  C  CD  . ARG A 112 ? 0.48156 0.36594 0.35289 -0.03634 -0.01727 -0.04790 491 ARG A CD  
912  N  NE  . ARG A 112 ? 0.55087 0.42854 0.38622 -0.03750 -0.00766 -0.04912 491 ARG A NE  
913  C  CZ  . ARG A 112 ? 0.58843 0.47071 0.42595 -0.03104 0.01350  -0.04912 491 ARG A CZ  
914  N  NH1 . ARG A 112 ? 0.54434 0.43802 0.41791 -0.02210 0.02482  -0.04831 491 ARG A NH1 
915  N  NH2 . ARG A 112 ? 0.61703 0.49309 0.42045 -0.03423 0.02314  -0.04885 491 ARG A NH2 
916  N  N   . TRP A 113 ? 0.31290 0.25686 0.31288 -0.02276 -0.01897 -0.01578 492 TRP A N   
917  C  CA  . TRP A 113 ? 0.30258 0.25549 0.32560 -0.02029 -0.01587 -0.00912 492 TRP A CA  
918  C  C   . TRP A 113 ? 0.30360 0.24114 0.33248 -0.02068 -0.01409 -0.01191 492 TRP A C   
919  O  O   . TRP A 113 ? 0.31670 0.23659 0.33379 -0.01946 -0.01069 -0.02091 492 TRP A O   
920  C  CB  . TRP A 113 ? 0.28110 0.24624 0.30988 -0.01326 -0.00729 -0.00400 492 TRP A CB  
921  C  CG  . TRP A 113 ? 0.27356 0.25021 0.29781 -0.01340 -0.00701 -0.00208 492 TRP A CG  
922  C  CD1 . TRP A 113 ? 0.30082 0.27841 0.31928 -0.01756 -0.01383 -0.00157 492 TRP A CD1 
923  C  CD2 . TRP A 113 ? 0.26071 0.24844 0.28920 -0.00956 -0.00039 0.00043  492 TRP A CD2 
924  N  NE1 . TRP A 113 ? 0.25193 0.23722 0.26925 -0.01644 -0.01044 0.00132  492 TRP A NE1 
925  C  CE2 . TRP A 113 ? 0.28155 0.27379 0.30508 -0.01257 -0.00207 0.00174  492 TRP A CE2 
926  C  CE3 . TRP A 113 ? 0.27932 0.27419 0.31878 -0.00407 0.00542  0.00251  492 TRP A CE3 
927  C  CZ2 . TRP A 113 ? 0.28920 0.29137 0.31746 -0.01199 0.00313  0.00369  492 TRP A CZ2 
928  C  CZ3 . TRP A 113 ? 0.25449 0.26311 0.30044 -0.00337 0.00889  0.00442  492 TRP A CZ3 
929  C  CH2 . TRP A 113 ? 0.27268 0.28408 0.31248 -0.00816 0.00836  0.00431  492 TRP A CH2 
930  N  N   . ASN A 114 ? 0.28372 0.22639 0.33034 -0.02248 -0.01454 -0.00403 493 ASN A N   
931  C  CA  . ASN A 114 ? 0.33156 0.25851 0.38731 -0.02395 -0.01291 -0.00290 493 ASN A CA  
932  C  C   . ASN A 114 ? 0.31047 0.24654 0.37885 -0.02148 -0.00864 0.01073  493 ASN A C   
933  O  O   . ASN A 114 ? 0.31234 0.26580 0.38421 -0.02399 -0.00874 0.01656  493 ASN A O   
934  C  CB  . ASN A 114 ? 0.33224 0.25132 0.39386 -0.03517 -0.02119 -0.00742 493 ASN A CB  
935  C  CG  . ASN A 114 ? 0.36578 0.26865 0.44121 -0.03907 -0.01880 -0.00393 493 ASN A CG  
936  O  OD1 . ASN A 114 ? 0.40054 0.28630 0.47476 -0.03284 -0.01287 -0.00416 493 ASN A OD1 
937  N  ND2 . ASN A 114 ? 0.37151 0.27963 0.46387 -0.04925 -0.02256 0.00021  493 ASN A ND2 
938  N  N   . ASP A 115 ? 0.31600 0.23875 0.38995 -0.01663 -0.00486 0.01596  494 ASP A N   
939  C  CA  . ASP A 115 ? 0.30848 0.23648 0.38950 -0.01623 -0.00304 0.03149  494 ASP A CA  
940  C  C   . ASP A 115 ? 0.34974 0.26786 0.43992 -0.02672 -0.00283 0.03605  494 ASP A C   
941  O  O   . ASP A 115 ? 0.33929 0.23826 0.43498 -0.03138 -0.00454 0.02862  494 ASP A O   
942  C  CB  . ASP A 115 ? 0.33000 0.25012 0.41602 -0.00539 -0.00128 0.03951  494 ASP A CB  
943  C  CG  . ASP A 115 ? 0.35028 0.24231 0.44458 -0.00202 0.00120  0.03403  494 ASP A CG  
944  O  OD1 . ASP A 115 ? 0.38336 0.26236 0.47294 -0.00686 0.00149  0.01898  494 ASP A OD1 
945  O  OD2 . ASP A 115 ? 0.39372 0.27531 0.49900 0.00579  0.00214  0.04492  494 ASP A OD2 
946  N  N   . SER A 116 ? 0.32702 0.25842 0.41839 -0.03177 0.00023  0.04695  495 SER A N   
947  C  CA  . SER A 116 ? 0.38623 0.31589 0.48966 -0.04363 0.00336  0.05116  495 SER A CA  
948  C  C   . SER A 116 ? 0.37652 0.30777 0.47545 -0.04600 0.01058  0.06910  495 SER A C   
949  O  O   . SER A 116 ? 0.34246 0.28309 0.42603 -0.03964 0.01084  0.07611  495 SER A O   
950  C  CB  . SER A 116 ? 0.38366 0.33364 0.49452 -0.04958 0.00262  0.04309  495 SER A CB  
951  O  OG  . SER A 116 ? 0.43457 0.38096 0.54735 -0.04995 -0.00641 0.02927  495 SER A OG  
952  N  N   . PRO A 117 ? 0.35877 0.28115 0.46938 -0.05655 0.01616  0.07715  496 PRO A N   
953  C  CA  . PRO A 117 ? 0.38469 0.30918 0.48547 -0.06102 0.02533  0.09556  496 PRO A CA  
954  C  C   . PRO A 117 ? 0.39504 0.34581 0.48430 -0.06242 0.03218  0.09328  496 PRO A C   
955  O  O   . PRO A 117 ? 0.38446 0.35071 0.48811 -0.06639 0.03495  0.08167  496 PRO A O   
956  C  CB  . PRO A 117 ? 0.40966 0.32176 0.53085 -0.07467 0.03200  0.10144  496 PRO A CB  
957  C  CG  . PRO A 117 ? 0.46357 0.35771 0.60140 -0.07467 0.02260  0.08819  496 PRO A CG  
958  C  CD  . PRO A 117 ? 0.40101 0.30939 0.53286 -0.06632 0.01425  0.07056  496 PRO A CD  
959  N  N   . CYS A 118 ? 0.39440 0.34923 0.45794 -0.05898 0.03395  0.10419  497 CYS A N   
960  C  CA  . CYS A 118 ? 0.41488 0.39101 0.46244 -0.05939 0.03979  0.09844  497 CYS A CA  
961  C  C   . CYS A 118 ? 0.39054 0.37717 0.44411 -0.07059 0.05702  0.09887  497 CYS A C   
962  O  O   . CYS A 118 ? 0.39129 0.39520 0.44158 -0.07064 0.06422  0.08833  497 CYS A O   
963  C  CB  . CYS A 118 ? 0.39758 0.37417 0.41317 -0.05508 0.03514  0.10945  497 CYS A CB  
964  S  SG  . CYS A 118 ? 0.53924 0.51244 0.55679 -0.04062 0.01645  0.10696  497 CYS A SG  
965  N  N   . ASN A 119 ? 0.41087 0.38720 0.47651 -0.08013 0.06528  0.11017  498 ASN A N   
966  C  CA  . ASN A 119 ? 0.38645 0.37468 0.46185 -0.09167 0.08503  0.11200  498 ASN A CA  
967  C  C   . ASN A 119 ? 0.37842 0.38022 0.49733 -0.09540 0.08658  0.09801  498 ASN A C   
968  O  O   . ASN A 119 ? 0.39408 0.40892 0.53282 -0.10481 0.10353  0.09883  498 ASN A O   
969  C  CB  . ASN A 119 ? 0.43849 0.41013 0.50746 -0.10240 0.09523  0.13347  498 ASN A CB  
970  C  CG  . ASN A 119 ? 0.46569 0.41796 0.56504 -0.10643 0.08730  0.13720  498 ASN A CG  
971  O  OD1 . ASN A 119 ? 0.45866 0.40249 0.56869 -0.09833 0.07067  0.12724  498 ASN A OD1 
972  N  ND2 . ASN A 119 ? 0.53688 0.48049 0.64890 -0.12010 0.10060  0.15092  498 ASN A ND2 
973  N  N   . GLN A 120 ? 0.34990 0.34991 0.48445 -0.08874 0.06947  0.08596  499 GLN A N   
974  C  CA  . GLN A 120 ? 0.38894 0.40268 0.56227 -0.09217 0.06613  0.07394  499 GLN A CA  
975  C  C   . GLN A 120 ? 0.35338 0.39158 0.53426 -0.08796 0.07430  0.06387  499 GLN A C   
976  O  O   . GLN A 120 ? 0.33388 0.37416 0.48874 -0.07920 0.07325  0.05932  499 GLN A O   
977  C  CB  . GLN A 120 ? 0.37402 0.37673 0.55149 -0.08642 0.04500  0.06412  499 GLN A CB  
978  C  CG  . GLN A 120 ? 0.44222 0.45108 0.65759 -0.09430 0.03653  0.05615  499 GLN A CG  
979  C  CD  . GLN A 120 ? 0.52770 0.52245 0.73718 -0.09016 0.01636  0.04566  499 GLN A CD  
980  O  OE1 . GLN A 120 ? 0.52464 0.50203 0.70643 -0.08216 0.01184  0.04543  499 GLN A OE1 
981  N  NE2 . GLN A 120 ? 0.51268 0.51577 0.74823 -0.09577 0.00419  0.03686  499 GLN A NE2 
982  N  N   . SER A 121 ? 0.33143 0.38823 0.55204 -0.09417 0.08242  0.05999  500 SER A N   
983  C  CA  . SER A 121 ? 0.31706 0.39600 0.55327 -0.08844 0.09075  0.04974  500 SER A CA  
984  C  C   . SER A 121 ? 0.29761 0.38149 0.55249 -0.08056 0.06958  0.03928  500 SER A C   
985  O  O   . SER A 121 ? 0.25840 0.34633 0.54554 -0.08539 0.05688  0.03809  500 SER A O   
986  C  CB  . SER A 121 ? 0.34028 0.44008 0.61623 -0.09710 0.11178  0.05104  500 SER A CB  
987  O  OG  . SER A 121 ? 0.41461 0.51065 0.66569 -0.10420 0.13558  0.06039  500 SER A OG  
988  N  N   . LEU A 122 ? 0.25105 0.33440 0.48528 -0.06982 0.06548  0.03222  501 LEU A N   
989  C  CA  . LEU A 122 ? 0.25836 0.34312 0.50224 -0.06219 0.04634  0.02493  501 LEU A CA  
990  C  C   . LEU A 122 ? 0.24595 0.33904 0.48803 -0.05302 0.05352  0.01744  501 LEU A C   
991  O  O   . LEU A 122 ? 0.23918 0.33106 0.45815 -0.05225 0.06964  0.01592  501 LEU A O   
992  C  CB  . LEU A 122 ? 0.28271 0.34705 0.49385 -0.05904 0.02938  0.02538  501 LEU A CB  
993  C  CG  . LEU A 122 ? 0.30583 0.35575 0.51717 -0.06630 0.01959  0.02925  501 LEU A CG  
994  C  CD1 . LEU A 122 ? 0.31592 0.34605 0.49285 -0.06061 0.00997  0.02831  501 LEU A CD1 
995  C  CD2 . LEU A 122 ? 0.30506 0.36226 0.54988 -0.07156 0.00508  0.02528  501 LEU A CD2 
996  N  N   . PRO A 123 ? 0.25325 0.35255 0.51714 -0.04649 0.04097  0.01281  502 PRO A N   
997  C  CA  . PRO A 123 ? 0.22413 0.32393 0.48248 -0.03709 0.04496  0.00594  502 PRO A CA  
998  C  C   . PRO A 123 ? 0.23635 0.31893 0.44832 -0.03447 0.03985  0.00504  502 PRO A C   
999  O  O   . PRO A 123 ? 0.22314 0.29470 0.41169 -0.03770 0.03176  0.00984  502 PRO A O   
1000 C  CB  . PRO A 123 ? 0.20484 0.31114 0.49561 -0.03155 0.02723  0.00593  502 PRO A CB  
1001 C  CG  . PRO A 123 ? 0.25747 0.37401 0.57923 -0.03921 0.01784  0.01089  502 PRO A CG  
1002 C  CD  . PRO A 123 ? 0.23821 0.34219 0.53068 -0.04810 0.02054  0.01439  502 PRO A CD  
1003 N  N   . SER A 124 ? 0.22797 0.30820 0.43064 -0.02850 0.04478  -0.00171 503 SER A N   
1004 C  CA  . SER A 124 ? 0.24235 0.30979 0.40738 -0.02718 0.03988  -0.00293 503 SER A CA  
1005 C  C   . SER A 124 ? 0.22648 0.28971 0.39559 -0.02063 0.03611  -0.00893 503 SER A C   
1006 O  O   . SER A 124 ? 0.20714 0.27572 0.40717 -0.01586 0.03731  -0.01142 503 SER A O   
1007 C  CB  . SER A 124 ? 0.27395 0.33985 0.40992 -0.03155 0.05354  -0.00438 503 SER A CB  
1008 O  OG  . SER A 124 ? 0.27871 0.35120 0.42302 -0.03147 0.07183  -0.01300 503 SER A OG  
1009 N  N   . ILE A 125 ? 0.21754 0.27110 0.35896 -0.02040 0.03125  -0.01020 504 ILE A N   
1010 C  CA  . ILE A 125 ? 0.24147 0.28803 0.38367 -0.01639 0.02954  -0.01562 504 ILE A CA  
1011 C  C   . ILE A 125 ? 0.25620 0.29883 0.37161 -0.02000 0.03649  -0.02287 504 ILE A C   
1012 O  O   . ILE A 125 ? 0.25827 0.30075 0.35038 -0.02365 0.03193  -0.01896 504 ILE A O   
1013 C  CB  . ILE A 125 ? 0.25636 0.29491 0.39464 -0.01435 0.01384  -0.00901 504 ILE A CB  
1014 C  CG1 . ILE A 125 ? 0.24786 0.28939 0.40940 -0.01176 0.00337  -0.00251 504 ILE A CG1 
1015 C  CG2 . ILE A 125 ? 0.24637 0.27528 0.38229 -0.01232 0.01373  -0.01280 504 ILE A CG2 
1016 C  CD1 . ILE A 125 ? 0.28263 0.31431 0.43056 -0.01138 -0.01156 0.00426  504 ILE A CD1 
1017 N  N   . CYS A 126 ? 0.30043 0.33942 0.42079 -0.01894 0.04652  -0.03388 505 CYS A N   
1018 C  CA  . CYS A 126 ? 0.25028 0.28349 0.34526 -0.02387 0.04999  -0.04325 505 CYS A CA  
1019 C  C   . CYS A 126 ? 0.29147 0.31401 0.39041 -0.02291 0.04209  -0.04520 505 CYS A C   
1020 O  O   . CYS A 126 ? 0.26475 0.28128 0.38706 -0.01722 0.03894  -0.04209 505 CYS A O   
1021 C  CB  . CYS A 126 ? 0.32179 0.35360 0.41287 -0.02572 0.06788  -0.05785 505 CYS A CB  
1022 S  SG  . CYS A 126 ? 0.45812 0.50175 0.54907 -0.02764 0.08419  -0.05639 505 CYS A SG  
1023 N  N   . LYS A 127 ? 0.27238 0.29281 0.34913 -0.02936 0.03844  -0.04950 506 LYS A N   
1024 C  CA  . LYS A 127 ? 0.30620 0.31729 0.38566 -0.03166 0.03256  -0.05189 506 LYS A CA  
1025 C  C   . LYS A 127 ? 0.34589 0.35181 0.40967 -0.03949 0.03728  -0.06760 506 LYS A C   
1026 O  O   . LYS A 127 ? 0.32248 0.33584 0.36209 -0.04505 0.03802  -0.07169 506 LYS A O   
1027 C  CB  . LYS A 127 ? 0.26513 0.28196 0.33796 -0.03340 0.02088  -0.04044 506 LYS A CB  
1028 C  CG  . LYS A 127 ? 0.30959 0.31916 0.38738 -0.03732 0.01660  -0.04066 506 LYS A CG  
1029 C  CD  . LYS A 127 ? 0.29486 0.31311 0.36888 -0.03771 0.00926  -0.02945 506 LYS A CD  
1030 C  CE  . LYS A 127 ? 0.35294 0.37162 0.43038 -0.04480 0.00653  -0.03054 506 LYS A CE  
1031 N  NZ  . LYS A 127 ? 0.31194 0.33974 0.39014 -0.04330 0.00349  -0.01987 506 LYS A NZ  
1032 N  N   . LYS A 128 ? 0.32126 0.31258 0.39694 -0.04077 0.03931  -0.07590 507 LYS A N   
1033 C  CA  . LYS A 128 ? 0.38380 0.36592 0.44595 -0.04932 0.04400  -0.09433 507 LYS A CA  
1034 C  C   . LYS A 128 ? 0.42543 0.39650 0.49710 -0.05565 0.03684  -0.09593 507 LYS A C   
1035 O  O   . LYS A 128 ? 0.40833 0.37198 0.50114 -0.05093 0.03434  -0.08500 507 LYS A O   
1036 C  CB  . LYS A 128 ? 0.44722 0.41728 0.51857 -0.04451 0.06108  -0.10916 507 LYS A CB  
1037 C  CG  . LYS A 128 ? 0.53127 0.48995 0.58087 -0.05374 0.06943  -0.13240 507 LYS A CG  
1038 C  CD  . LYS A 128 ? 0.55774 0.50836 0.61455 -0.04741 0.09100  -0.14711 507 LYS A CD  
1039 C  CE  . LYS A 128 ? 0.67437 0.60871 0.70545 -0.05732 0.10119  -0.17400 507 LYS A CE  
1040 N  NZ  . LYS A 128 ? 0.72118 0.64736 0.75746 -0.05118 0.12675  -0.19126 507 LYS A NZ  
1041 O  OXT . LYS A 128 ? 0.46754 0.43677 0.52565 -0.06681 0.03289  -0.10734 507 LYS A OXT 
1042 CA CA  . CA  B .   ? 0.38135 0.29205 0.48979 0.02114  -0.01618 0.11101  601 CA  A CA  
1043 CA CA  . CA  C .   ? 0.39048 0.24535 0.48394 -0.02773 -0.00449 0.00838  602 CA  A CA  
1044 C  C1  A MFU D .   ? 0.45158 0.24663 0.54541 -0.06687 -0.02550 -0.03559 603 MFU A C1  
1045 C  C1  B MFU D .   ? 0.46455 0.24008 0.60091 -0.07383 -0.01565 -0.00839 603 MFU A C1  
1046 C  C2  A MFU D .   ? 0.43548 0.26176 0.53160 -0.05730 -0.02063 -0.01887 603 MFU A C2  
1047 C  C2  B MFU D .   ? 0.44361 0.25156 0.57395 -0.06323 -0.01148 0.00623  603 MFU A C2  
1048 C  C3  A MFU D .   ? 0.43062 0.26420 0.54852 -0.06147 -0.01649 -0.00028 603 MFU A C3  
1049 C  C3  B MFU D .   ? 0.42924 0.26343 0.54692 -0.06325 -0.01811 -0.00252 603 MFU A C3  
1050 C  C4  A MFU D .   ? 0.42291 0.26308 0.55949 -0.07830 -0.02330 -0.00089 603 MFU A C4  
1051 C  C4  B MFU D .   ? 0.44203 0.26284 0.53806 -0.05953 -0.02189 -0.02202 603 MFU A C4  
1052 C  C5  A MFU D .   ? 0.44492 0.25668 0.58425 -0.08954 -0.03100 -0.01676 603 MFU A C5  
1053 C  C5  B MFU D .   ? 0.44669 0.23698 0.54360 -0.07108 -0.02754 -0.03759 603 MFU A C5  
1054 C  C6  A MFU D .   ? 0.43248 0.25805 0.59464 -0.10706 -0.04123 -0.01826 603 MFU A C6  
1055 C  C6  B MFU D .   ? 0.46692 0.24128 0.53449 -0.06748 -0.02856 -0.05838 603 MFU A C6  
1056 O  O1  A MFU D .   ? 0.45150 0.22053 0.55503 -0.06133 -0.01636 -0.03177 603 MFU A O1  
1057 O  O1  B MFU D .   ? 0.44538 0.22893 0.59863 -0.09108 -0.02256 -0.00849 603 MFU A O1  
1058 O  O2  A MFU D .   ? 0.42012 0.24192 0.50652 -0.04155 -0.01145 -0.01777 603 MFU A O2  
1059 O  O2  B MFU D .   ? 0.45868 0.27909 0.60438 -0.06941 -0.00690 0.02582  603 MFU A O2  
1060 O  O3  A MFU D .   ? 0.41215 0.27288 0.52679 -0.05344 -0.01195 0.01284  603 MFU A O3  
1061 O  O3  B MFU D .   ? 0.41339 0.27214 0.52532 -0.05285 -0.01292 0.00941  603 MFU A O3  
1062 O  O4  A MFU D .   ? 0.40007 0.26837 0.53475 -0.08025 -0.03086 -0.00457 603 MFU A O4  
1063 O  O4  B MFU D .   ? 0.42516 0.23823 0.51242 -0.04394 -0.01209 -0.02113 603 MFU A O4  
1064 O  O5  A MFU D .   ? 0.46113 0.26086 0.57267 -0.08491 -0.03655 -0.03632 603 MFU A O5  
1065 O  O5  B MFU D .   ? 0.46256 0.22495 0.57609 -0.07043 -0.01964 -0.03162 603 MFU A O5  
1066 C  CM  A MFU D .   ? 0.47136 0.20502 0.57446 -0.06929 -0.01816 -0.04819 603 MFU A CM  
1067 C  CM  B MFU D .   ? 0.46062 0.21305 0.62965 -0.10320 -0.02348 -0.01280 603 MFU A CM  
1068 O  O   . HOH E .   ? 0.64943 0.53440 0.54884 -0.04094 -0.04355 0.10460  701 HOH A O   
1069 O  O   . HOH E .   ? 0.59633 0.55239 0.53063 -0.01285 0.06313  -0.01958 702 HOH A O   
1070 O  O   . HOH E .   ? 0.36830 0.43452 0.47278 0.02870  -0.07626 0.12194  703 HOH A O   
1071 O  O   . HOH E .   ? 0.41234 0.31866 0.55460 -0.07118 -0.01362 0.02293  704 HOH A O   
1072 O  O   . HOH E .   ? 0.42707 0.32061 0.47671 0.03391  0.06384  -0.04808 705 HOH A O   
1073 O  O   . HOH E .   ? 0.46384 0.52709 0.37595 -0.07795 -0.01669 -0.05296 706 HOH A O   
1074 O  O   . HOH E .   ? 0.29645 0.36447 0.39116 -0.01474 0.01324  0.00892  707 HOH A O   
1075 O  O   . HOH E .   ? 0.53473 0.27508 0.62751 0.02951  0.05067  -0.06353 708 HOH A O   
1076 O  O   . HOH E .   ? 0.46733 0.25347 0.46557 -0.04105 -0.01151 -0.07885 709 HOH A O   
1077 O  O   . HOH E .   ? 0.43638 0.41581 0.52798 -0.05594 0.01956  0.01474  710 HOH A O   
1078 O  O   . HOH E .   ? 0.71002 0.65590 1.01653 0.02958  0.18873  -0.16910 711 HOH A O   
1079 O  O   . HOH E .   ? 0.46305 0.46894 0.56663 -0.02809 -0.12984 0.04027  712 HOH A O   
1080 O  O   . HOH E .   ? 0.32128 0.36661 0.35165 -0.04353 0.00525  -0.03260 713 HOH A O   
1081 O  O   . HOH E .   ? 0.31450 0.36662 0.65824 0.02640  -0.03100 0.01996  714 HOH A O   
1082 O  O   . HOH E .   ? 0.38758 0.39833 0.50218 -0.05662 -0.14846 0.01402  715 HOH A O   
1083 O  O   . HOH E .   ? 0.45976 0.37152 0.72015 0.03040  -0.05060 0.06509  716 HOH A O   
1084 O  O   . HOH E .   ? 0.47846 0.46992 0.45387 -0.08582 0.08643  0.12557  717 HOH A O   
1085 O  O   . HOH E .   ? 0.27619 0.36909 0.58525 -0.06143 -0.04061 0.01612  718 HOH A O   
1086 O  O   . HOH E .   ? 0.38034 0.26289 0.62964 0.01977  -0.02081 0.04305  719 HOH A O   
1087 O  O   . HOH E .   ? 0.37192 0.43244 0.40832 0.00347  -0.06584 0.10853  720 HOH A O   
1088 O  O   . HOH E .   ? 0.34364 0.39646 0.42516 -0.03663 0.07221  0.01640  721 HOH A O   
1089 O  O   . HOH E .   ? 0.34944 0.35689 0.42343 -0.04770 0.02292  0.01647  722 HOH A O   
1090 O  O   . HOH E .   ? 0.43622 0.36111 0.37800 -0.05282 -0.08580 -0.02121 723 HOH A O   
1091 O  O   . HOH E .   ? 0.31066 0.49557 0.73381 -0.05481 0.14320  0.00355  724 HOH A O   
1092 O  O   . HOH E .   ? 0.54621 0.29369 0.78231 -0.07323 0.05615  -0.10185 725 HOH A O   
1093 O  O   . HOH E .   ? 0.35732 0.38972 0.37233 -0.05674 0.01232  -0.06145 726 HOH A O   
1094 O  O   . HOH E .   ? 0.37805 0.44638 0.61510 -0.05806 -0.20217 0.03478  727 HOH A O   
1095 O  O   . HOH E .   ? 0.39735 0.47334 0.80467 0.03443  0.05783  -0.02980 728 HOH A O   
1096 O  O   . HOH E .   ? 0.36134 0.33616 0.46454 -0.05008 0.01238  -0.00583 729 HOH A O   
1097 O  O   . HOH E .   ? 0.44904 0.43699 0.57393 -0.07480 0.01880  -0.00786 730 HOH A O   
1098 O  O   . HOH E .   ? 0.25496 0.31739 0.27337 -0.03422 -0.00825 -0.00028 731 HOH A O   
1099 O  O   . HOH E .   ? 0.36838 0.36163 0.34845 -0.04060 0.07597  0.02509  732 HOH A O   
1100 O  O   . HOH E .   ? 0.30362 0.39766 0.48510 -0.04161 0.10355  -0.00752 733 HOH A O   
1101 O  O   . HOH E .   ? 0.55359 0.62074 0.41592 -0.06987 -0.01361 -0.00359 734 HOH A O   
1102 O  O   . HOH E .   ? 0.41193 0.26228 0.55061 -0.04270 0.00600  0.05630  735 HOH A O   
1103 O  O   . HOH E .   ? 0.46159 0.36107 0.43225 -0.03746 -0.02423 0.09007  736 HOH A O   
1104 O  O   . HOH E .   ? 0.55309 0.46300 0.72256 -0.01806 0.10058  -0.14037 737 HOH A O   
1105 O  O   . HOH E .   ? 0.42120 0.36710 0.60357 0.06757  0.01962  0.03731  738 HOH A O   
1106 O  O   . HOH E .   ? 0.50930 0.33427 0.43062 -0.06691 -0.05691 -0.08525 739 HOH A O   
1107 O  O   . HOH E .   ? 0.39082 0.29752 0.51112 0.02602  -0.00602 0.07676  740 HOH A O   
1108 O  O   . HOH E .   ? 0.40382 0.49174 0.77193 0.01345  -0.07567 0.03711  741 HOH A O   
1109 O  O   . HOH E .   ? 0.37364 0.45561 0.35587 -0.02581 -0.05549 0.06574  742 HOH A O   
1110 O  O   . HOH E .   ? 0.37723 0.32176 0.37139 0.01028  0.06039  -0.03630 743 HOH A O   
1111 O  O   . HOH E .   ? 0.31463 0.34964 0.64647 0.02861  0.01707  -0.01058 744 HOH A O   
1112 O  O   . HOH E .   ? 0.35248 0.35577 0.48930 0.04348  0.03539  0.00806  745 HOH A O   
1113 O  O   . HOH E .   ? 0.52384 0.54366 0.62301 -0.05591 0.00827  -0.01418 746 HOH A O   
1114 O  O   . HOH E .   ? 0.39732 0.26554 0.44020 -0.05276 -0.03605 -0.03718 747 HOH A O   
1115 O  O   . HOH E .   ? 0.36722 0.49385 0.78902 0.01616  0.11616  -0.04536 748 HOH A O   
1116 O  O   . HOH E .   ? 0.81541 0.67061 0.95624 -0.05537 0.08056  -0.16506 749 HOH A O   
1117 O  O   . HOH E .   ? 0.37514 0.40717 0.55611 0.05380  0.00569  0.04263  750 HOH A O   
1118 O  O   . HOH E .   ? 0.49809 0.43197 0.51980 -0.07213 0.05015  0.07091  751 HOH A O   
1119 O  O   . HOH E .   ? 0.62377 0.48907 0.53259 -0.00136 0.06302  -0.07781 752 HOH A O   
1120 O  O   . HOH E .   ? 0.32594 0.44766 0.70064 -0.06144 -0.10579 0.02101  753 HOH A O   
1121 O  O   . HOH E .   ? 0.40968 0.41734 0.42882 -0.00396 0.08339  -0.01132 754 HOH A O   
1122 O  O   . HOH E .   ? 0.54236 0.46608 0.46419 -0.00447 0.06768  -0.04478 755 HOH A O   
1123 O  O   . HOH E .   ? 0.32629 0.45496 0.64917 -0.01358 0.15925  -0.05004 756 HOH A O   
1124 O  O   . HOH E .   ? 0.75491 0.81903 0.63345 -0.11803 0.24698  0.04886  757 HOH A O   
1125 O  O   . HOH E .   ? 0.75912 0.59023 0.74426 0.02463  0.08135  -0.09070 758 HOH A O   
1126 O  O   . HOH E .   ? 0.72631 0.60721 0.83315 -0.09073 -0.06580 -0.03482 759 HOH A O   
1127 O  O   . HOH E .   ? 0.48241 0.30684 0.47506 -0.06290 -0.04508 -0.07118 760 HOH A O   
1128 O  O   . HOH E .   ? 0.45523 0.34960 0.61894 0.05452  0.00408  0.06310  761 HOH A O   
1129 O  O   . HOH E .   ? 0.63377 0.43736 0.66469 -0.09161 -0.06701 -0.07884 762 HOH A O   
1130 O  O   . HOH E .   ? 0.41868 0.55404 0.81529 -0.05517 -0.05336 0.01963  763 HOH A O   
1131 O  O   . HOH E .   ? 0.45320 0.49737 0.42069 -0.07443 -0.00245 -0.07278 764 HOH A O   
1132 O  O   . HOH E .   ? 0.40346 0.30182 0.42017 -0.09465 0.07079  0.10154  765 HOH A O   
1133 O  O   . HOH E .   ? 0.65356 0.46324 0.56368 -0.09718 -0.09875 -0.10191 766 HOH A O   
1134 O  O   . HOH E .   ? 0.52714 0.34295 0.51629 -0.11029 -0.10605 -0.09446 767 HOH A O   
# 
