data_9DPV
# 
_entry.id   9DPV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9DPV         pdb_00009dpv 10.2210/pdb9dpv/pdb 
WWPDB D_1000287389 ?            ?                   
# 
_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       2025-03-05 
_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                        9DPV 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ahinck@pitt.edu 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Hinck 
_pdbx_contact_author.name_mi            P 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3320-8054 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Schwartze, T.A.' 1 0000-0003-0306-3288 
'Hinck, A.P.'     2 0000-0003-3320-8054 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_id_ASTM           JMOBAK 
_citation.journal_id_CSD            0070 
_citation.journal_id_ISSN           1089-8638 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            437 
_citation.language                  ? 
_citation.page_first                168935 
_citation.page_last                 168935 
_citation.title                     'Molecular Basis of Interchain Disulfide Bond Formation in BMP-9 and BMP-10.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2025.168935 
_citation.pdbx_database_id_PubMed   39793884 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Schwartze, T.A.' 1  ? 
primary 'Morosky, S.A.'   2  ? 
primary 'Rosato, T.L.'    3  ? 
primary 'Henrickson, A.'  4  ? 
primary 'Lin, G.'         5  ? 
primary 'Hinck, C.S.'     6  ? 
primary 'Taylor, A.B.'    7  ? 
primary 'Olsen, S.K.'     8  ? 
primary 'Calero, G.'      9  ? 
primary 'Demeler, B.'     10 ? 
primary 'Roman, B.L.'     11 ? 
primary 'Hinck, A.P.'     12 ? 
# 
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 'Growth/differentiation factor 2' 12177.011 1  ? 'A321S, K357R, G389S' ? ? 
2 non-polymer syn GLYCEROL                          92.094    1  ? ?                     ? ? 
3 non-polymer syn 'CHLORIDE ION'                    35.453    5  ? ?                     ? ? 
4 non-polymer syn 'SODIUM ION'                      22.990    4  ? ?                     ? ? 
5 water       nat water                             18.015    87 ? ?                     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'GDF-2,Bone morphogenetic protein 9,BMP-9' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SSGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECRGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVSKACCVPTKLS
PISVLYKDDMGVPTLKYHYEGMSVAECGCR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECRGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVSKACCVPTKLS
PISVLYKDDMGVPTLKYHYEGMSVAECGCR
;
_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 GLYCEROL       GOL 
3 'CHLORIDE ION' CL  
4 'SODIUM ION'   NA  
5 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   SER n 
1 3   GLY n 
1 4   ALA n 
1 5   GLY n 
1 6   SER n 
1 7   HIS n 
1 8   CYS n 
1 9   GLN n 
1 10  LYS n 
1 11  THR n 
1 12  SER n 
1 13  LEU n 
1 14  ARG n 
1 15  VAL n 
1 16  ASN n 
1 17  PHE n 
1 18  GLU n 
1 19  ASP n 
1 20  ILE n 
1 21  GLY n 
1 22  TRP n 
1 23  ASP n 
1 24  SER n 
1 25  TRP n 
1 26  ILE n 
1 27  ILE n 
1 28  ALA n 
1 29  PRO n 
1 30  LYS n 
1 31  GLU n 
1 32  TYR n 
1 33  GLU n 
1 34  ALA n 
1 35  TYR n 
1 36  GLU n 
1 37  CYS n 
1 38  ARG n 
1 39  GLY n 
1 40  GLY n 
1 41  CYS n 
1 42  PHE n 
1 43  PHE n 
1 44  PRO n 
1 45  LEU n 
1 46  ALA n 
1 47  ASP n 
1 48  ASP n 
1 49  VAL n 
1 50  THR n 
1 51  PRO n 
1 52  THR n 
1 53  LYS n 
1 54  HIS n 
1 55  ALA n 
1 56  ILE n 
1 57  VAL n 
1 58  GLN n 
1 59  THR n 
1 60  LEU n 
1 61  VAL n 
1 62  HIS n 
1 63  LEU n 
1 64  LYS n 
1 65  PHE n 
1 66  PRO n 
1 67  THR n 
1 68  LYS n 
1 69  VAL n 
1 70  SER n 
1 71  LYS n 
1 72  ALA n 
1 73  CYS n 
1 74  CYS n 
1 75  VAL n 
1 76  PRO n 
1 77  THR n 
1 78  LYS n 
1 79  LEU n 
1 80  SER n 
1 81  PRO n 
1 82  ILE n 
1 83  SER n 
1 84  VAL n 
1 85  LEU n 
1 86  TYR n 
1 87  LYS n 
1 88  ASP n 
1 89  ASP n 
1 90  MET n 
1 91  GLY n 
1 92  VAL n 
1 93  PRO n 
1 94  THR n 
1 95  LEU n 
1 96  LYS n 
1 97  TYR n 
1 98  HIS n 
1 99  TYR n 
1 100 GLU n 
1 101 GLY n 
1 102 MET n 
1 103 SER n 
1 104 VAL n 
1 105 ALA n 
1 106 GLU n 
1 107 CYS n 
1 108 GLY n 
1 109 CYS n 
1 110 ARG 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                   110 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'GDF2, BMP9' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                kidney 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               embryonic 
_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            'expi293 (Invitrogen)' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pcdna3.1 
_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 
CL  non-polymer         . 'CHLORIDE ION'  ?                               'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ?                               'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   320 ?   ?   ?   A . n 
A 1 2   SER 2   321 ?   ?   ?   A . n 
A 1 3   GLY 3   322 ?   ?   ?   A . n 
A 1 4   ALA 4   323 ?   ?   ?   A . n 
A 1 5   GLY 5   324 ?   ?   ?   A . n 
A 1 6   SER 6   325 325 SER SER A . n 
A 1 7   HIS 7   326 326 HIS HIS A . n 
A 1 8   CYS 8   327 327 CYS CYS A . n 
A 1 9   GLN 9   328 328 GLN GLN A . n 
A 1 10  LYS 10  329 329 LYS LYS A . n 
A 1 11  THR 11  330 330 THR THR A . n 
A 1 12  SER 12  331 331 SER SER A . n 
A 1 13  LEU 13  332 332 LEU LEU A . n 
A 1 14  ARG 14  333 333 ARG ARG A . n 
A 1 15  VAL 15  334 334 VAL VAL A . n 
A 1 16  ASN 16  335 335 ASN ASN A . n 
A 1 17  PHE 17  336 336 PHE PHE A . n 
A 1 18  GLU 18  337 337 GLU GLU A . n 
A 1 19  ASP 19  338 338 ASP ASP A . n 
A 1 20  ILE 20  339 339 ILE ILE A . n 
A 1 21  GLY 21  340 340 GLY GLY A . n 
A 1 22  TRP 22  341 341 TRP TRP A . n 
A 1 23  ASP 23  342 342 ASP ASP A . n 
A 1 24  SER 24  343 343 SER SER A . n 
A 1 25  TRP 25  344 344 TRP TRP A . n 
A 1 26  ILE 26  345 345 ILE ILE A . n 
A 1 27  ILE 27  346 346 ILE ILE A . n 
A 1 28  ALA 28  347 347 ALA ALA A . n 
A 1 29  PRO 29  348 348 PRO PRO A . n 
A 1 30  LYS 30  349 349 LYS LYS A . n 
A 1 31  GLU 31  350 350 GLU GLU A . n 
A 1 32  TYR 32  351 351 TYR TYR A . n 
A 1 33  GLU 33  352 352 GLU GLU A . n 
A 1 34  ALA 34  353 353 ALA ALA A . n 
A 1 35  TYR 35  354 354 TYR TYR A . n 
A 1 36  GLU 36  355 355 GLU GLU A . n 
A 1 37  CYS 37  356 356 CYS CYS A . n 
A 1 38  ARG 38  357 357 ARG ARG A . n 
A 1 39  GLY 39  358 358 GLY GLY A . n 
A 1 40  GLY 40  359 359 GLY GLY A . n 
A 1 41  CYS 41  360 360 CYS CYS A . n 
A 1 42  PHE 42  361 361 PHE PHE A . n 
A 1 43  PHE 43  362 362 PHE PHE A . n 
A 1 44  PRO 44  363 363 PRO PRO A . n 
A 1 45  LEU 45  364 364 LEU LEU A . n 
A 1 46  ALA 46  365 365 ALA ALA A . n 
A 1 47  ASP 47  366 366 ASP ASP A . n 
A 1 48  ASP 48  367 367 ASP ASP A . n 
A 1 49  VAL 49  368 368 VAL VAL A . n 
A 1 50  THR 50  369 369 THR THR A . n 
A 1 51  PRO 51  370 370 PRO PRO A . n 
A 1 52  THR 52  371 371 THR THR A . n 
A 1 53  LYS 53  372 372 LYS LYS A . n 
A 1 54  HIS 54  373 373 HIS HIS A . n 
A 1 55  ALA 55  374 374 ALA ALA A . n 
A 1 56  ILE 56  375 375 ILE ILE A . n 
A 1 57  VAL 57  376 376 VAL VAL A . n 
A 1 58  GLN 58  377 377 GLN GLN A . n 
A 1 59  THR 59  378 378 THR THR A . n 
A 1 60  LEU 60  379 379 LEU LEU A . n 
A 1 61  VAL 61  380 380 VAL VAL A . n 
A 1 62  HIS 62  381 381 HIS HIS A . n 
A 1 63  LEU 63  382 382 LEU LEU A . n 
A 1 64  LYS 64  383 383 LYS LYS A . n 
A 1 65  PHE 65  384 384 PHE PHE A . n 
A 1 66  PRO 66  385 385 PRO PRO A . n 
A 1 67  THR 67  386 386 THR THR A . n 
A 1 68  LYS 68  387 387 LYS LYS A . n 
A 1 69  VAL 69  388 388 VAL VAL A . n 
A 1 70  SER 70  389 389 SER SER A . n 
A 1 71  LYS 71  390 390 LYS LYS A . n 
A 1 72  ALA 72  391 391 ALA ALA A . n 
A 1 73  CYS 73  392 392 CYS CYS A . n 
A 1 74  CYS 74  393 393 CYS CYS A . n 
A 1 75  VAL 75  394 394 VAL VAL A . n 
A 1 76  PRO 76  395 395 PRO PRO A . n 
A 1 77  THR 77  396 396 THR THR A . n 
A 1 78  LYS 78  397 397 LYS LYS A . n 
A 1 79  LEU 79  398 398 LEU LEU A . n 
A 1 80  SER 80  399 399 SER SER A . n 
A 1 81  PRO 81  400 400 PRO PRO A . n 
A 1 82  ILE 82  401 401 ILE ILE A . n 
A 1 83  SER 83  402 402 SER SER A . n 
A 1 84  VAL 84  403 403 VAL VAL A . n 
A 1 85  LEU 85  404 404 LEU LEU A . n 
A 1 86  TYR 86  405 405 TYR TYR A . n 
A 1 87  LYS 87  406 406 LYS LYS A . n 
A 1 88  ASP 88  407 407 ASP ASP A . n 
A 1 89  ASP 89  408 408 ASP ASP A . n 
A 1 90  MET 90  409 409 MET MET A . n 
A 1 91  GLY 91  410 410 GLY GLY A . n 
A 1 92  VAL 92  411 411 VAL VAL A . n 
A 1 93  PRO 93  412 412 PRO PRO A . n 
A 1 94  THR 94  413 413 THR THR A . n 
A 1 95  LEU 95  414 414 LEU LEU A . n 
A 1 96  LYS 96  415 415 LYS LYS A . n 
A 1 97  TYR 97  416 416 TYR TYR A . n 
A 1 98  HIS 98  417 417 HIS HIS A . n 
A 1 99  TYR 99  418 418 TYR TYR A . n 
A 1 100 GLU 100 419 419 GLU GLU A . n 
A 1 101 GLY 101 420 420 GLY GLY A . n 
A 1 102 MET 102 421 421 MET MET A . n 
A 1 103 SER 103 422 422 SER SER A . n 
A 1 104 VAL 104 423 423 VAL VAL A . n 
A 1 105 ALA 105 424 424 ALA ALA A . n 
A 1 106 GLU 106 425 425 GLU GLU A . n 
A 1 107 CYS 107 426 426 CYS CYS A . n 
A 1 108 GLY 108 427 427 GLY GLY A . n 
A 1 109 CYS 109 428 428 CYS CYS A . n 
A 1 110 ARG 110 429 429 ARG ARG A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GOL 1  501 1   GOL GOL A . 
C 3 CL  1  502 1   CL  CL  A . 
D 3 CL  1  503 2   CL  CL  A . 
E 3 CL  1  504 3   CL  CL  A . 
F 3 CL  1  505 4   CL  CL  A . 
G 3 CL  1  506 5   CL  CL  A . 
H 4 NA  1  507 1   NA  NA  A . 
I 4 NA  1  508 2   NA  NA  A . 
J 4 NA  1  509 3   NA  NA  A . 
K 4 NA  1  510 4   NA  NA  A . 
L 5 HOH 1  601 9   HOH HOH A . 
L 5 HOH 2  602 117 HOH HOH A . 
L 5 HOH 3  603 36  HOH HOH A . 
L 5 HOH 4  604 112 HOH HOH A . 
L 5 HOH 5  605 38  HOH HOH A . 
L 5 HOH 6  606 1   HOH HOH A . 
L 5 HOH 7  607 123 HOH HOH A . 
L 5 HOH 8  608 30  HOH HOH A . 
L 5 HOH 9  609 76  HOH HOH A . 
L 5 HOH 10 610 66  HOH HOH A . 
L 5 HOH 11 611 22  HOH HOH A . 
L 5 HOH 12 612 2   HOH HOH A . 
L 5 HOH 13 613 27  HOH HOH A . 
L 5 HOH 14 614 57  HOH HOH A . 
L 5 HOH 15 615 32  HOH HOH A . 
L 5 HOH 16 616 31  HOH HOH A . 
L 5 HOH 17 617 116 HOH HOH A . 
L 5 HOH 18 618 29  HOH HOH A . 
L 5 HOH 19 619 79  HOH HOH A . 
L 5 HOH 20 620 43  HOH HOH A . 
L 5 HOH 21 621 47  HOH HOH A . 
L 5 HOH 22 622 7   HOH HOH A . 
L 5 HOH 23 623 58  HOH HOH A . 
L 5 HOH 24 624 16  HOH HOH A . 
L 5 HOH 25 625 4   HOH HOH A . 
L 5 HOH 26 626 8   HOH HOH A . 
L 5 HOH 27 627 34  HOH HOH A . 
L 5 HOH 28 628 61  HOH HOH A . 
L 5 HOH 29 629 68  HOH HOH A . 
L 5 HOH 30 630 103 HOH HOH A . 
L 5 HOH 31 631 107 HOH HOH A . 
L 5 HOH 32 632 6   HOH HOH A . 
L 5 HOH 33 633 102 HOH HOH A . 
L 5 HOH 34 634 12  HOH HOH A . 
L 5 HOH 35 635 119 HOH HOH A . 
L 5 HOH 36 636 120 HOH HOH A . 
L 5 HOH 37 637 41  HOH HOH A . 
L 5 HOH 38 638 51  HOH HOH A . 
L 5 HOH 39 639 19  HOH HOH A . 
L 5 HOH 40 640 18  HOH HOH A . 
L 5 HOH 41 641 28  HOH HOH A . 
L 5 HOH 42 642 104 HOH HOH A . 
L 5 HOH 43 643 80  HOH HOH A . 
L 5 HOH 44 644 122 HOH HOH A . 
L 5 HOH 45 645 35  HOH HOH A . 
L 5 HOH 46 646 77  HOH HOH A . 
L 5 HOH 47 647 124 HOH HOH A . 
L 5 HOH 48 648 25  HOH HOH A . 
L 5 HOH 49 649 118 HOH HOH A . 
L 5 HOH 50 650 101 HOH HOH A . 
L 5 HOH 51 651 21  HOH HOH A . 
L 5 HOH 52 652 39  HOH HOH A . 
L 5 HOH 53 653 40  HOH HOH A . 
L 5 HOH 54 654 20  HOH HOH A . 
L 5 HOH 55 655 78  HOH HOH A . 
L 5 HOH 56 656 62  HOH HOH A . 
L 5 HOH 57 657 70  HOH HOH A . 
L 5 HOH 58 658 67  HOH HOH A . 
L 5 HOH 59 659 93  HOH HOH A . 
L 5 HOH 60 660 54  HOH HOH A . 
L 5 HOH 61 661 13  HOH HOH A . 
L 5 HOH 62 662 114 HOH HOH A . 
L 5 HOH 63 663 49  HOH HOH A . 
L 5 HOH 64 664 48  HOH HOH A . 
L 5 HOH 65 665 64  HOH HOH A . 
L 5 HOH 66 666 85  HOH HOH A . 
L 5 HOH 67 667 26  HOH HOH A . 
L 5 HOH 68 668 84  HOH HOH A . 
L 5 HOH 69 669 23  HOH HOH A . 
L 5 HOH 70 670 109 HOH HOH A . 
L 5 HOH 71 671 73  HOH HOH A . 
L 5 HOH 72 672 106 HOH HOH A . 
L 5 HOH 73 673 59  HOH HOH A . 
L 5 HOH 74 674 105 HOH HOH A . 
L 5 HOH 75 675 110 HOH HOH A . 
L 5 HOH 76 676 121 HOH HOH A . 
L 5 HOH 77 677 83  HOH HOH A . 
L 5 HOH 78 678 98  HOH HOH A . 
L 5 HOH 79 679 81  HOH HOH A . 
L 5 HOH 80 680 113 HOH HOH A . 
L 5 HOH 81 681 115 HOH HOH A . 
L 5 HOH 82 682 69  HOH HOH A . 
L 5 HOH 83 683 5   HOH HOH A . 
L 5 HOH 84 684 100 HOH HOH A . 
L 5 HOH 85 685 3   HOH HOH A . 
L 5 HOH 86 686 90  HOH HOH A . 
L 5 HOH 87 687 86  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_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .           4 
# 
_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                     9DPV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.105 
_cell.length_a_esd                 ? 
_cell.length_b                     71.105 
_cell.length_b_esd                 ? 
_cell.length_c                     145.553 
_cell.length_c_esd                 ? 
_cell.volume                       735904.473 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9DPV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                98 
_symmetry.space_group_name_Hall            'I 4bw 2bw' 
_symmetry.space_group_name_H-M             'I 41 2 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                   9DPV 
_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             3.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.44 
_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              7.5 
_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    '1M NaCl, 22-26% glycerol, 0.1 M HEPES pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-17 
_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   1 
_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                        'APS BEAMLINE 22-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          36.87 
_reflns.entry_id                                       9DPV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.99 
_reflns.d_resolution_low                               41.37 
_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                                     13055 
_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                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.168 
_reflns.pdbx_Rpim_I_all                                0.081 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.146 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.99 
_reflns_shell.d_res_low                                     2.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             832 
_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                               5.6 
_reflns_shell.pdbx_chi_squared                              0.95 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.723 
_reflns_shell.pdbx_Rpim_I_all                               0.877 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.645 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          86.7 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.467 
_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                               53.46 
_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                                 9DPV 
_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                            1.99 
_refine.ls_d_res_low                             35.55 
_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                     12997 
_refine.ls_number_reflns_R_free                  649 
_refine.ls_number_reflns_R_work                  12348 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.28 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2259 
_refine.ls_R_factor_R_free                       0.2649 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2238 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.01 
_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                 28.1713 
_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                            0.2480 
_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                       1.99 
_refine_hist.d_res_low                        35.55 
_refine_hist.number_atoms_solvent             87 
_refine_hist.number_atoms_total               928 
_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        826 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0094  ? 854  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2478  ? 1158 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0653  ? 127  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0143  ? 145  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.0951 ? 312  ? 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.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' 1.99 2.14  . . 122 2313 94.02 . . . . 0.3031 . . . . . . . . . . . 0.3203 
'X-RAY DIFFRACTION' 2.14 2.36  . . 136 2441 99.38 . . . . 0.2311 . . . . . . . . . . . 0.2589 
'X-RAY DIFFRACTION' 2.36 2.70  . . 123 2474 99.16 . . . . 0.2328 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 2.70 3.40  . . 125 2507 99.51 . . . . 0.1957 . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 3.41 35.55 . . 143 2613 99.21 . . . . 0.2240 . . . . . . . . . . . 0.2707 
# 
_struct.entry_id                     9DPV 
_struct.title                        'BMP-9 K357R G389S Dimer Without Radiation Damage in Neutral pH' 
_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        9DPV 
_struct_keywords.text            'SIGNALING PROTEIN, BMP, bone morphogenetic protein, TGF-beta family' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    GDF2_HUMAN 
_struct_ref.pdbx_db_accession          Q9UK05 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLS
PISVLYKDDMGVPTLKYHYEGMSVAECGCR
;
_struct_ref.pdbx_align_begin           320 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DPV 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 110 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9UK05 
_struct_ref_seq.db_align_beg                  320 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  429 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       320 
_struct_ref_seq.pdbx_auth_seq_align_end       429 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DPV SER A 2  ? UNP Q9UK05 ALA 321 'engineered mutation' 321 1 
1 9DPV ARG A 38 ? UNP Q9UK05 LYS 357 'engineered mutation' 357 2 
1 9DPV SER A 70 ? UNP Q9UK05 GLY 389 'engineered mutation' 389 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L 
1 2 A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                'Covalent Homodimer observed by SDS gel.' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z           1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 6_555 x,-y+1/2,-z+1/4 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
-1.0000000000 0.0000000000 35.5525000000 0.0000000000 0.0000000000 -1.0000000000 36.3882500000 
# 
_struct_conf.conf_type_id            HELX_P 
_struct_conf.id                      HELX_P1 
_struct_conf.pdbx_PDB_helix_id       AA1 
_struct_conf.beg_label_comp_id       THR 
_struct_conf.beg_label_asym_id       A 
_struct_conf.beg_label_seq_id        52 
_struct_conf.pdbx_beg_PDB_ins_code   ? 
_struct_conf.end_label_comp_id       PHE 
_struct_conf.end_label_asym_id       A 
_struct_conf.end_label_seq_id        65 
_struct_conf.pdbx_end_PDB_ins_code   ? 
_struct_conf.beg_auth_comp_id        THR 
_struct_conf.beg_auth_asym_id        A 
_struct_conf.beg_auth_seq_id         371 
_struct_conf.end_auth_comp_id        PHE 
_struct_conf.end_auth_asym_id        A 
_struct_conf.end_auth_seq_id         384 
_struct_conf.pdbx_PDB_helix_class    1 
_struct_conf.details                 ? 
_struct_conf.pdbx_PDB_helix_length   14 
# 
_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 8  SG  ? ? ? 1_555 A CYS 74  SG ? ? A CYS 327 A CYS 393 1_555  ? ? ? ? ? ? ? 2.030 ? ? 
disulf2 disulf ? ? A CYS 37 SG  ? ? ? 1_555 A CYS 107 SG ? ? A CYS 356 A CYS 426 1_555  ? ? ? ? ? ? ? 2.031 ? ? 
disulf3 disulf ? ? A CYS 41 SG  ? ? ? 1_555 A CYS 109 SG ? ? A CYS 360 A CYS 428 1_555  ? ? ? ? ? ? ? 2.033 ? ? 
disulf4 disulf ? ? A CYS 73 SG  ? ? ? 1_555 A CYS 73  SG ? ? A CYS 392 A CYS 392 6_555  ? ? ? ? ? ? ? 2.103 ? ? 
metalc1 metalc ? ? A ASP 19 OD2 ? ? ? 1_555 K NA  .   NA ? ? A ASP 338 A NA  510 1_555  ? ? ? ? ? ? ? 2.988 ? ? 
metalc2 metalc ? ? A THR 67 OG1 ? ? ? 1_555 J NA  .   NA ? ? A THR 386 A NA  509 1_555  ? ? ? ? ? ? ? 2.626 ? ? 
metalc3 metalc ? ? A TYR 97 OH  ? ? ? 1_555 H NA  .   NA ? ? A TYR 416 A NA  507 1_555  ? ? ? ? ? ? ? 2.932 ? ? 
metalc4 metalc ? ? H NA  .  NA  ? ? ? 1_555 L HOH .   O  ? ? A NA  507 A HOH 646 10_655 ? ? ? ? ? ? ? 2.954 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OH 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   TYR 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    97 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    TYR 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     416 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   H 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    NA 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     507 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   L 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     646 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        10_655 
_pdbx_struct_conn_angle.value                 109.4 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 8  ? CYS A 74  ? CYS A 327 ? 1_555 CYS A 393 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 37 ? CYS A 107 ? CYS A 356 ? 1_555 CYS A 426 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 41 ? CYS A 109 ? CYS A 360 ? 1_555 CYS A 428 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 73 ? CYS A 73  ? CYS A 392 ? 1_555 CYS A 392 ? 6_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 28 A . ? ALA 347 A PRO 29 A ? PRO 348 A 1 -1.19 
2 PHE 43 A . ? PHE 362 A PRO 44 A ? PRO 363 A 1 -0.70 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? 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  ? THR A 11  ? GLN A 328 THR A 330 
AA1 2 GLU A 36 ? ARG A 38  ? GLU A 355 ARG A 357 
AA2 1 ARG A 14 ? ASN A 16  ? ARG A 333 ASN A 335 
AA2 2 GLU A 31 ? GLU A 33  ? GLU A 350 GLU A 352 
AA3 1 ILE A 26 ? ALA A 28  ? ILE A 345 ALA A 347 
AA3 2 CYS A 74 ? LYS A 87  ? CYS A 393 LYS A 406 
AA3 3 PRO A 93 ? CYS A 109 ? PRO A 412 CYS A 428 
# 
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 THR A 11 ? N THR A 330 O GLU A 36  ? O GLU A 355 
AA2 1 2 N VAL A 15 ? N VAL A 334 O TYR A 32  ? O TYR A 351 
AA3 1 2 N ALA A 28 ? N ALA A 347 O LEU A 85  ? O LEU A 404 
AA3 2 3 N SER A 80 ? N SER A 399 O SER A 103 ? O SER A 422 
# 
_pdbx_entry_details.entry_id                   9DPV 
_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     N 
_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 TYR A 354 ? ? 59.88 170.51 
2 1 THR A 369 ? ? 38.85 55.23  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A CL  504 ? E CL  . 
2 1 A HOH 621 ? L HOH . 
3 1 A HOH 656 ? L HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                
2  -y+1/2,x,z+3/4       
3  y+1/2,-x,z+3/4       
4  x+1/2,-y,-z+3/4      
5  -x+1/2,y,-z+3/4      
6  -x,-y,z              
7  y,x,-z               
8  -y,-x,-z             
9  x+1/2,y+1/2,z+1/2    
10 -y+1,x+1/2,z+5/4     
11 y+1,-x+1/2,z+5/4     
12 x+1,-y+1/2,-z+5/4    
13 -x+1,y+1/2,-z+5/4    
14 -x+1/2,-y+1/2,z+1/2  
15 y+1/2,x+1/2,-z+1/2   
16 -y+1/2,-x+1/2,-z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 20.2910570484 4.05618233953 15.3896947138 0.559353072358 ? -0.000455770105152 ? -0.0334385800731 ? 
0.42513581736  ? 0.0219164076099   ? 0.3395083513   ? 4.46411851473 ? 0.555400342677  ? 2.35824147939   ? 6.83553823375 ? 
4.13681896152   ? 3.46153339041 ? 0.542873456449 ? 0.0974408182245 ? -0.689481571533  ? 0.682054256171  ? -0.629459287413  ? 
0.312864074634  ? 1.08238858485    ? -1.12217922279   ? 0.296894570259   ? 
2 'X-RAY DIFFRACTION' ? refined 23.2066508718 5.26082819866 1.6958395929  0.651259197314 ? 0.309262115294     ? -0.137635800146  ? 
0.726527684558 ? -0.0311096621095  ? 0.250349164364 ? 1.81245487457 ? -0.36204160894  ? 0.740707143114  ? 3.69344032823 ? 
1.61839652156   ? 2.63750095092 ? 0.651124636266 ? 0.909889864666  ? -0.336829195217  ? -0.659575184989 ? -0.693606087637  ? 
0.477444062394  ? 0.204181732278   ? -0.544178084197  ? -0.0765953273368 ? 
3 'X-RAY DIFFRACTION' ? refined 22.5273884641 12.2029351014 29.841701487  0.767941397548 ? -0.0805453336673   ? 0.135064218399   ? 
0.365162232824 ? -0.00290457339791 ? 0.412009730371 ? 7.19068099657 ? 4.82363331231   ? -3.70473202815  ? 5.03800980664 ? 
0.136145425917  ? 7.10296763069 ? -0.61757333311 ? 0.277005276924  ? -1.36730415684   ? 0.844047073091  ? -0.161416168774  ? 
-0.455409683722 ? 1.63170937135    ? -0.0481692162187 ? 0.587388751983   ? 
4 'X-RAY DIFFRACTION' ? refined 16.7878277626 23.72571359   28.6515954363 0.406321368008 ? -0.0902911316412   ? 0.0317830104869  ? 
0.416851776037 ? 0.0275025490613   ? 0.225363206952 ? 2.23597832492 ? 0.138918662442  ? -2.09317220567  ? 4.32015112436 ? 
-0.115832977592 ? 4.97088007046 ? 0.222834169222 ? 0.290712370193  ? -0.174284519827  ? 0.18241636987   ? -0.250777607652  ? 
0.373800739522  ? -0.0249529786204 ? -0.363796504112  ? 0.085060020232   ? 
5 'X-RAY DIFFRACTION' ? refined 32.0908938336 8.48556691092 1.15566158278 0.420716348282 ? 0.227334996915     ? 0.0471221602865  ? 
0.632547387836 ? 0.0832385473297   ? 0.26693643241  ? 3.64266322366 ? -0.577542048531 ? 0.0417633886845 ? 4.14454105218 ? 
2.05504589098   ? 1.96226971837 ? 0.329275675947 ? 0.951657122524  ? 0.147974029361   ? -0.420273162075 ? -0.0234203082548 ? 
-0.480501142241 ? 0.400919566104   ? 0.569814567219   ? -0.29746530541   ? 
6 'X-RAY DIFFRACTION' ? refined 32.3578595655 8.24336647025 8.3170819313  0.382116669125 ? 0.144716581622     ? -0.020679603605  ? 
0.412843117074 ? 0.0767708968869   ? 0.274664053027 ? 4.27480277861 ? -1.55567358875  ? -3.19698470713  ? 4.43389152712 ? 
3.3221388097    ? 6.17923528838 ? 0.386179705    ? 0.429292567203  ? -0.0132680585282 ? -0.107526524398 ? -0.277491446036  ? 
-0.587861247982 ? 0.125355491069   ? 0.216955768234   ? -0.064390083295  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1  A 325 ? A 11  A 335 ? ? 
;chain 'A' and (resid  325  through  335 )
;
2 'X-RAY DIFFRACTION' 2 A 12 A 336 ? A 33  A 357 ? ? 
;chain 'A' and (resid  336  through  357 )
;
3 'X-RAY DIFFRACTION' 3 A 34 A 358 ? A 47  A 371 ? ? 
;chain 'A' and (resid  358  through  371 )
;
4 'X-RAY DIFFRACTION' 4 A 48 A 372 ? A 68  A 392 ? ? 
;chain 'A' and (resid  372  through  392 )
;
5 'X-RAY DIFFRACTION' 5 A 69 A 393 ? A 87  A 411 ? ? 
;chain 'A' and (resid  393  through  411 )
;
6 'X-RAY DIFFRACTION' 6 A 88 A 412 ? A 105 A 429 ? ? 
;chain 'A' and (resid  412  through  429 )
;
# 
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 320 ? A SER 1 
2 1 Y 1 A SER 321 ? A SER 2 
3 1 Y 1 A GLY 322 ? A GLY 3 
4 1 Y 1 A ALA 323 ? A ALA 4 
5 1 Y 1 A GLY 324 ? A GLY 5 
# 
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  
CL  CL   CL 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 
GOL C1   C  N N 138 
GOL O1   O  N N 139 
GOL C2   C  N N 140 
GOL O2   O  N N 141 
GOL C3   C  N N 142 
GOL O3   O  N N 143 
GOL H11  H  N N 144 
GOL H12  H  N N 145 
GOL HO1  H  N N 146 
GOL H2   H  N N 147 
GOL HO2  H  N N 148 
GOL H31  H  N N 149 
GOL H32  H  N N 150 
GOL HO3  H  N N 151 
HIS N    N  N N 152 
HIS CA   C  N S 153 
HIS C    C  N N 154 
HIS O    O  N N 155 
HIS CB   C  N N 156 
HIS CG   C  Y N 157 
HIS ND1  N  Y N 158 
HIS CD2  C  Y N 159 
HIS CE1  C  Y N 160 
HIS NE2  N  Y N 161 
HIS OXT  O  N N 162 
HIS H    H  N N 163 
HIS H2   H  N N 164 
HIS HA   H  N N 165 
HIS HB2  H  N N 166 
HIS HB3  H  N N 167 
HIS HD1  H  N N 168 
HIS HD2  H  N N 169 
HIS HE1  H  N N 170 
HIS HE2  H  N N 171 
HIS HXT  H  N N 172 
HOH O    O  N N 173 
HOH H1   H  N N 174 
HOH H2   H  N N 175 
ILE N    N  N N 176 
ILE CA   C  N S 177 
ILE C    C  N N 178 
ILE O    O  N N 179 
ILE CB   C  N S 180 
ILE CG1  C  N N 181 
ILE CG2  C  N N 182 
ILE CD1  C  N N 183 
ILE OXT  O  N N 184 
ILE H    H  N N 185 
ILE H2   H  N N 186 
ILE HA   H  N N 187 
ILE HB   H  N N 188 
ILE HG12 H  N N 189 
ILE HG13 H  N N 190 
ILE HG21 H  N N 191 
ILE HG22 H  N N 192 
ILE HG23 H  N N 193 
ILE HD11 H  N N 194 
ILE HD12 H  N N 195 
ILE HD13 H  N N 196 
ILE HXT  H  N N 197 
LEU N    N  N N 198 
LEU CA   C  N S 199 
LEU C    C  N N 200 
LEU O    O  N N 201 
LEU CB   C  N N 202 
LEU CG   C  N N 203 
LEU CD1  C  N N 204 
LEU CD2  C  N N 205 
LEU OXT  O  N N 206 
LEU H    H  N N 207 
LEU H2   H  N N 208 
LEU HA   H  N N 209 
LEU HB2  H  N N 210 
LEU HB3  H  N N 211 
LEU HG   H  N N 212 
LEU HD11 H  N N 213 
LEU HD12 H  N N 214 
LEU HD13 H  N N 215 
LEU HD21 H  N N 216 
LEU HD22 H  N N 217 
LEU HD23 H  N N 218 
LEU HXT  H  N N 219 
LYS N    N  N N 220 
LYS CA   C  N S 221 
LYS C    C  N N 222 
LYS O    O  N N 223 
LYS CB   C  N N 224 
LYS CG   C  N N 225 
LYS CD   C  N N 226 
LYS CE   C  N N 227 
LYS NZ   N  N N 228 
LYS OXT  O  N N 229 
LYS H    H  N N 230 
LYS H2   H  N N 231 
LYS HA   H  N N 232 
LYS HB2  H  N N 233 
LYS HB3  H  N N 234 
LYS HG2  H  N N 235 
LYS HG3  H  N N 236 
LYS HD2  H  N N 237 
LYS HD3  H  N N 238 
LYS HE2  H  N N 239 
LYS HE3  H  N N 240 
LYS HZ1  H  N N 241 
LYS HZ2  H  N N 242 
LYS HZ3  H  N N 243 
LYS HXT  H  N N 244 
MET N    N  N N 245 
MET CA   C  N S 246 
MET C    C  N N 247 
MET O    O  N N 248 
MET CB   C  N N 249 
MET CG   C  N N 250 
MET SD   S  N N 251 
MET CE   C  N N 252 
MET OXT  O  N N 253 
MET H    H  N N 254 
MET H2   H  N N 255 
MET HA   H  N N 256 
MET HB2  H  N N 257 
MET HB3  H  N N 258 
MET HG2  H  N N 259 
MET HG3  H  N N 260 
MET HE1  H  N N 261 
MET HE2  H  N N 262 
MET HE3  H  N N 263 
MET HXT  H  N N 264 
NA  NA   NA N N 265 
PHE N    N  N N 266 
PHE CA   C  N S 267 
PHE C    C  N N 268 
PHE O    O  N N 269 
PHE CB   C  N N 270 
PHE CG   C  Y N 271 
PHE CD1  C  Y N 272 
PHE CD2  C  Y N 273 
PHE CE1  C  Y N 274 
PHE CE2  C  Y N 275 
PHE CZ   C  Y N 276 
PHE OXT  O  N N 277 
PHE H    H  N N 278 
PHE H2   H  N N 279 
PHE HA   H  N N 280 
PHE HB2  H  N N 281 
PHE HB3  H  N N 282 
PHE HD1  H  N N 283 
PHE HD2  H  N N 284 
PHE HE1  H  N N 285 
PHE HE2  H  N N 286 
PHE HZ   H  N N 287 
PHE HXT  H  N N 288 
PRO N    N  N N 289 
PRO CA   C  N S 290 
PRO C    C  N N 291 
PRO O    O  N N 292 
PRO CB   C  N N 293 
PRO CG   C  N N 294 
PRO CD   C  N N 295 
PRO OXT  O  N N 296 
PRO H    H  N N 297 
PRO HA   H  N N 298 
PRO HB2  H  N N 299 
PRO HB3  H  N N 300 
PRO HG2  H  N N 301 
PRO HG3  H  N N 302 
PRO HD2  H  N N 303 
PRO HD3  H  N N 304 
PRO HXT  H  N N 305 
SER N    N  N N 306 
SER CA   C  N S 307 
SER C    C  N N 308 
SER O    O  N N 309 
SER CB   C  N N 310 
SER OG   O  N N 311 
SER OXT  O  N N 312 
SER H    H  N N 313 
SER H2   H  N N 314 
SER HA   H  N N 315 
SER HB2  H  N N 316 
SER HB3  H  N N 317 
SER HG   H  N N 318 
SER HXT  H  N N 319 
THR N    N  N N 320 
THR CA   C  N S 321 
THR C    C  N N 322 
THR O    O  N N 323 
THR CB   C  N R 324 
THR OG1  O  N N 325 
THR CG2  C  N N 326 
THR OXT  O  N N 327 
THR H    H  N N 328 
THR H2   H  N N 329 
THR HA   H  N N 330 
THR HB   H  N N 331 
THR HG1  H  N N 332 
THR HG21 H  N N 333 
THR HG22 H  N N 334 
THR HG23 H  N N 335 
THR HXT  H  N N 336 
TRP N    N  N N 337 
TRP CA   C  N S 338 
TRP C    C  N N 339 
TRP O    O  N N 340 
TRP CB   C  N N 341 
TRP CG   C  Y N 342 
TRP CD1  C  Y N 343 
TRP CD2  C  Y N 344 
TRP NE1  N  Y N 345 
TRP CE2  C  Y N 346 
TRP CE3  C  Y N 347 
TRP CZ2  C  Y N 348 
TRP CZ3  C  Y N 349 
TRP CH2  C  Y N 350 
TRP OXT  O  N N 351 
TRP H    H  N N 352 
TRP H2   H  N N 353 
TRP HA   H  N N 354 
TRP HB2  H  N N 355 
TRP HB3  H  N N 356 
TRP HD1  H  N N 357 
TRP HE1  H  N N 358 
TRP HE3  H  N N 359 
TRP HZ2  H  N N 360 
TRP HZ3  H  N N 361 
TRP HH2  H  N N 362 
TRP HXT  H  N N 363 
TYR N    N  N N 364 
TYR CA   C  N S 365 
TYR C    C  N N 366 
TYR O    O  N N 367 
TYR CB   C  N N 368 
TYR CG   C  Y N 369 
TYR CD1  C  Y N 370 
TYR CD2  C  Y N 371 
TYR CE1  C  Y N 372 
TYR CE2  C  Y N 373 
TYR CZ   C  Y N 374 
TYR OH   O  N N 375 
TYR OXT  O  N N 376 
TYR H    H  N N 377 
TYR H2   H  N N 378 
TYR HA   H  N N 379 
TYR HB2  H  N N 380 
TYR HB3  H  N N 381 
TYR HD1  H  N N 382 
TYR HD2  H  N N 383 
TYR HE1  H  N N 384 
TYR HE2  H  N N 385 
TYR HH   H  N N 386 
TYR HXT  H  N N 387 
VAL N    N  N N 388 
VAL CA   C  N S 389 
VAL C    C  N N 390 
VAL O    O  N N 391 
VAL CB   C  N N 392 
VAL CG1  C  N N 393 
VAL CG2  C  N N 394 
VAL OXT  O  N N 395 
VAL H    H  N N 396 
VAL H2   H  N N 397 
VAL HA   H  N N 398 
VAL HB   H  N N 399 
VAL HG11 H  N N 400 
VAL HG12 H  N N 401 
VAL HG13 H  N N 402 
VAL HG21 H  N N 403 
VAL HG22 H  N N 404 
VAL HG23 H  N N 405 
VAL HXT  H  N N 406 
# 
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 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM58670          1 
'Department of Defense (DOD, United States)'                                               'United States' W81XWH-17-1-0429 2 
# 
_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   1ZKZ 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_space_group.name_H-M_alt     'I 41 2 2' 
_space_group.name_Hall        'I 4bw 2bw' 
_space_group.IT_number        98 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DPV 
_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]   0.014064 
_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]   0.014064 
_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]   0.006870 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C    ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL   ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H    ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
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.
;
? 
NA   ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
NA1+ ? ? 9.95753 ?       ? ? 4.19129  ?        ? ? 0.0 
;1-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    . SER A 1 6   ? 15.56400 4.75900  28.19700  1.000 93.78602  ? 325 SER A N    1 
ATOM   2    C  CA   . SER A 1 6   ? 15.11300 5.48900  27.01000  1.000 79.10218  ? 325 SER A CA   1 
ATOM   3    C  C    . SER A 1 6   ? 15.99200 6.70400  26.71700  1.000 138.33544 ? 325 SER A C    1 
ATOM   4    O  O    . SER A 1 6   ? 15.51000 7.73400  26.24200  1.000 77.53646  ? 325 SER A O    1 
ATOM   5    C  CB   . SER A 1 6   ? 13.65900 5.91800  27.18200  1.000 130.81190 ? 325 SER A CB   1 
ATOM   6    O  OG   . SER A 1 6   ? 12.84300 4.81600  27.54700  1.000 146.29270 ? 325 SER A OG   1 
ATOM   7    H  HA   . SER A 1 6   ? 15.18500 4.88900  26.25100  1.000 94.99962  ? 325 SER A HA   1 
ATOM   8    H  HB2  . SER A 1 6   ? 13.60000 6.60700  27.86200  1.000 157.05128 ? 325 SER A HB2  1 
ATOM   9    H  HB3  . SER A 1 6   ? 13.33300 6.30600  26.35500  1.000 157.05128 ? 325 SER A HB3  1 
ATOM   10   H  HG   . SER A 1 6   ? 13.20500 4.39500  28.17700  1.000 175.62824 ? 325 SER A HG   1 
ATOM   11   N  N    . HIS A 1 7   ? 17.29700 6.56000  26.97900  1.000 59.70265  ? 326 HIS A N    1 
ATOM   12   C  CA   . HIS A 1 7   ? 18.23400 7.66500  26.87100  1.000 60.01532  ? 326 HIS A CA   1 
ATOM   13   C  C    . HIS A 1 7   ? 19.04600 7.62200  25.57500  1.000 44.59751  ? 326 HIS A C    1 
ATOM   14   O  O    . HIS A 1 7   ? 18.92400 6.69500  24.78000  1.000 44.97242  ? 326 HIS A O    1 
ATOM   15   C  CB   . HIS A 1 7   ? 19.12500 7.68000  28.12000  1.000 62.08312  ? 326 HIS A CB   1 
ATOM   16   C  CG   . HIS A 1 7   ? 18.46000 8.31900  29.30500  1.000 129.05726 ? 326 HIS A CG   1 
ATOM   17   N  ND1  . HIS A 1 7   ? 18.23300 9.68900  29.35900  1.000 86.93883  ? 326 HIS A ND1  1 
ATOM   18   C  CD2  . HIS A 1 7   ? 17.99100 7.76000  30.44300  1.000 92.95020  ? 326 HIS A CD2  1 
ATOM   19   C  CE1  . HIS A 1 7   ? 17.63600 9.91500  30.51900  1.000 98.59294  ? 326 HIS A CE1  1 
ATOM   20   N  NE2  . HIS A 1 7   ? 17.47000 8.77900  31.20500  1.000 83.86511  ? 326 HIS A NE2  1 
ATOM   21   H  H    . HIS A 1 7   ? 17.65500 5.81700  27.22300  1.000 71.72017  ? 326 HIS A H    1 
ATOM   22   H  HA   . HIS A 1 7   ? 17.73600 8.49600  26.82700  1.000 72.09538  ? 326 HIS A HA   1 
ATOM   23   H  HB2  . HIS A 1 7   ? 19.37300 6.77000  28.34600  1.000 74.57674  ? 326 HIS A HB2  1 
ATOM   24   H  HB3  . HIS A 1 7   ? 19.94600 8.15600  27.92000  1.000 74.57674  ? 326 HIS A HB3  1 
ATOM   25   H  HD2  . HIS A 1 7   ? 18.01600 6.85800  30.66800  1.000 111.61723 ? 326 HIS A HD2  1 
ATOM   26   H  HE1  . HIS A 1 7   ? 17.36700 10.75400 30.81800  1.000 118.38852 ? 326 HIS A HE1  1 
ATOM   27   H  HE2  . HIS A 1 7   ? 17.10500 8.70000  31.98000  1.000 100.71513 ? 326 HIS A HE2  1 
ATOM   28   N  N    . CYS A 1 8   ? 19.88300 8.64100  25.39700  1.000 44.89273  ? 327 CYS A N    1 
ATOM   29   C  CA   . CYS A 1 8   ? 20.62100 8.88200  24.17100  1.000 50.47883  ? 327 CYS A CA   1 
ATOM   30   C  C    . CYS A 1 8   ? 21.59500 7.75800  23.83200  1.000 54.52000  ? 327 CYS A C    1 
ATOM   31   O  O    . CYS A 1 8   ? 22.55300 7.52900  24.56300  1.000 53.31336  ? 327 CYS A O    1 
ATOM   32   C  CB   . CYS A 1 8   ? 21.35000 10.21600 24.30400  1.000 40.85494  ? 327 CYS A CB   1 
ATOM   33   S  SG   . CYS A 1 8   ? 22.35900 10.65500 22.87900  1.000 38.27665  ? 327 CYS A SG   1 
ATOM   34   H  H    . CYS A 1 8   ? 20.03900 9.22600  26.00800  1.000 53.94828  ? 327 CYS A H    1 
ATOM   35   H  HA   . CYS A 1 8   ? 19.99000 8.91200  23.43400  1.000 60.65160  ? 327 CYS A HA   1 
ATOM   36   H  HB2  . CYS A 1 8   ? 20.69600 10.91700 24.45200  1.000 49.10293  ? 327 CYS A HB2  1 
ATOM   37   H  HB3  . CYS A 1 8   ? 21.91600 10.18600 25.09100  1.000 49.10293  ? 327 CYS A HB3  1 
ATOM   38   N  N    . GLN A 1 9   ? 21.35900 7.08000  22.70300  1.000 36.17341  ? 328 GLN A N    1 
ATOM   39   C  CA   . GLN A 1 9   ? 22.21500 5.98100  22.29400  1.000 38.26450  ? 328 GLN A CA   1 
ATOM   40   C  C    . GLN A 1 9   ? 22.17000 5.71400  20.79400  1.000 36.00654  ? 328 GLN A C    1 
ATOM   41   O  O    . GLN A 1 9   ? 21.30100 6.22300  20.09200  1.000 36.78272  ? 328 GLN A O    1 
ATOM   42   C  CB   . GLN A 1 9   ? 21.82000 4.70800  23.05000  1.000 40.63674  ? 328 GLN A CB   1 
ATOM   43   C  CG   . GLN A 1 9   ? 20.41500 4.22600  22.74800  1.000 46.23019  ? 328 GLN A CG   1 
ATOM   44   C  CD   . GLN A 1 9   ? 20.10300 2.95600  23.49900  1.000 77.39080  ? 328 GLN A CD   1 
ATOM   45   O  OE1  . GLN A 1 9   ? 20.88100 2.48800  24.33500  1.000 60.30426  ? 328 GLN A OE1  1 
ATOM   46   N  NE2  . GLN A 1 9   ? 18.95600 2.36800  23.21200  1.000 60.39975  ? 328 GLN A NE2  1 
ATOM   47   H  H    . GLN A 1 9   ? 20.70800 7.24600  22.16600  1.000 43.02311  ? 328 GLN A H    1 
ATOM   48   H  HA   . GLN A 1 9   ? 23.12500 6.23900  22.51100  1.000 45.99440  ? 328 GLN A HA   1 
ATOM   49   H  HB2  . GLN A 1 9   ? 22.44900 4.00300  22.82900  1.000 48.37911  ? 328 GLN A HB2  1 
ATOM   50   H  HB3  . GLN A 1 9   ? 21.89900 4.87100  24.00300  1.000 48.37911  ? 328 GLN A HB3  1 
ATOM   51   H  HG2  . GLN A 1 9   ? 19.77500 4.91400  22.99000  1.000 55.55323  ? 328 GLN A HG2  1 
ATOM   52   H  HG3  . GLN A 1 9   ? 20.32000 4.07300  21.79500  1.000 55.55323  ? 328 GLN A HG3  1 
ATOM   53   H  HE21 . GLN A 1 9   ? 18.43100 2.71400  22.62500  1.000 72.55670  ? 328 GLN A HE21 1 
ATOM   54   H  HE22 . GLN A 1 9   ? 18.73400 1.63900  23.61200  1.000 72.55670  ? 328 GLN A HE22 1 
ATOM   55   N  N    . LYS A 1 10  ? 23.12500 4.89500  20.34200  1.000 39.07644  ? 329 LYS A N    1 
ATOM   56   C  CA   . LYS A 1 10  ? 23.25600 4.49900  18.95500  1.000 47.80493  ? 329 LYS A CA   1 
ATOM   57   C  C    . LYS A 1 10  ? 22.27600 3.37600  18.62800  1.000 48.45320  ? 329 LYS A C    1 
ATOM   58   O  O    . LYS A 1 10  ? 22.22400 2.37400  19.33300  1.000 49.42358  ? 329 LYS A O    1 
ATOM   59   C  CB   . LYS A 1 10  ? 24.68800 4.04300  18.70600  1.000 49.43567  ? 329 LYS A CB   1 
ATOM   60   C  CG   . LYS A 1 10  ? 25.01200 3.84900  17.24700  1.000 48.23925  ? 329 LYS A CG   1 
ATOM   61   C  CD   . LYS A 1 10  ? 26.48000 3.66700  17.00100  1.000 38.15921  ? 329 LYS A CD   1 
ATOM   62   C  CE   . LYS A 1 10  ? 26.95900 2.29600  17.35000  1.000 47.01308  ? 329 LYS A CE   1 
ATOM   63   N  NZ   . LYS A 1 10  ? 28.40200 2.15100  17.04500  1.000 81.27732  ? 329 LYS A NZ   1 
ATOM   64   H  H    . LYS A 1 10  ? 23.72500 4.55100  20.85300  1.000 46.96873  ? 329 LYS A H    1 
ATOM   65   H  HA   . LYS A 1 10  ? 23.05100 5.25300  18.38100  1.000 57.44292  ? 329 LYS A HA   1 
ATOM   66   H  HB2  . LYS A 1 10  ? 25.29800 4.69700  19.08100  1.000 59.39980  ? 329 LYS A HB2  1 
ATOM   67   H  HB3  . LYS A 1 10  ? 24.84100 3.20900  19.17800  1.000 59.39980  ? 329 LYS A HB3  1 
ATOM   68   H  HG2  . LYS A 1 10  ? 24.53300 3.07400  16.91300  1.000 57.96409  ? 329 LYS A HG2  1 
ATOM   69   H  HG3  . LYS A 1 10  ? 24.69600 4.61600  16.74400  1.000 57.96409  ? 329 LYS A HG3  1 
ATOM   70   H  HD2  . LYS A 1 10  ? 26.67200 3.84400  16.06700  1.000 45.86805  ? 329 LYS A HD2  1 
ATOM   71   H  HD3  . LYS A 1 10  ? 26.97400 4.32000  17.52100  1.000 45.86805  ? 329 LYS A HD3  1 
ATOM   72   H  HE2  . LYS A 1 10  ? 26.80400 2.12400  18.29200  1.000 56.49269  ? 329 LYS A HE2  1 
ATOM   73   H  HE3  . LYS A 1 10  ? 26.45100 1.63500  16.85400  1.000 56.49269  ? 329 LYS A HE3  1 
ATOM   74   H  HZ1  . LYS A 1 10  ? 28.58300 1.29900  16.86300  1.000 97.60979  ? 329 LYS A HZ1  1 
ATOM   75   H  HZ2  . LYS A 1 10  ? 28.60900 2.65400  16.34100  1.000 97.60979  ? 329 LYS A HZ2  1 
ATOM   76   H  HZ3  . LYS A 1 10  ? 28.88200 2.41300  17.74700  1.000 97.60979  ? 329 LYS A HZ3  1 
ATOM   77   N  N    . THR A 1 11  ? 21.49700 3.56200  17.55800  1.000 35.76441  ? 330 THR A N    1 
ATOM   78   C  CA   . THR A 1 11  ? 20.56100 2.55300  17.09100  1.000 38.41875  ? 330 THR A CA   1 
ATOM   79   C  C    . THR A 1 11  ? 20.79500 2.37000  15.59700  1.000 37.58163  ? 330 THR A C    1 
ATOM   80   O  O    . THR A 1 11  ? 21.45300 3.18900  14.96400  1.000 34.67624  ? 330 THR A O    1 
ATOM   81   C  CB   . THR A 1 11  ? 19.11300 2.94100  17.39800  1.000 47.75967  ? 330 THR A CB   1 
ATOM   82   O  OG1  . THR A 1 11  ? 18.76900 4.09600  16.63500  1.000 45.05659  ? 330 THR A OG1  1 
ATOM   83   C  CG2  . THR A 1 11  ? 18.89100 3.22700  18.86300  1.000 75.53193  ? 330 THR A CG2  1 
ATOM   84   H  H    . THR A 1 11  ? 21.50200 4.28100  17.08600  1.000 42.53231  ? 330 THR A H    1 
ATOM   85   H  HA   . THR A 1 11  ? 20.71200 1.71500  17.55600  1.000 45.71752  ? 330 THR A HA   1 
ATOM   86   H  HB   . THR A 1 11  ? 18.55000 2.18800  17.16000  1.000 57.38860  ? 330 THR A HB   1 
ATOM   87   H  HG1  . THR A 1 11  ? 17.97000 4.30500  16.78800  1.000 54.14490  ? 330 THR A HG1  1 
ATOM   88   H  HG21 . THR A 1 11  ? 17.96300 3.46800  19.00900  1.000 90.71532  ? 330 THR A HG21 1 
ATOM   89   H  HG22 . THR A 1 11  ? 19.10500 2.43700  19.38300  1.000 90.71532  ? 330 THR A HG22 1 
ATOM   90   H  HG23 . THR A 1 11  ? 19.46200 3.96100  19.14000  1.000 90.71532  ? 330 THR A HG23 1 
ATOM   91   N  N    . SER A 1 12  ? 20.25300 1.28400  15.05300  1.000 39.66363  ? 331 SER A N    1 
ATOM   92   C  CA   . SER A 1 12  ? 20.50200 0.92800  13.67100  1.000 39.29325  ? 331 SER A CA   1 
ATOM   93   C  C    . SER A 1 12  ? 19.81900 1.91500  12.72600  1.000 41.75490  ? 331 SER A C    1 
ATOM   94   O  O    . SER A 1 12  ? 18.73300 2.41200  13.01400  1.000 45.28967  ? 331 SER A O    1 
ATOM   95   C  CB   . SER A 1 12  ? 20.01800 -0.48500 13.38900  1.000 43.09915  ? 331 SER A CB   1 
ATOM   96   O  OG   . SER A 1 12  ? 20.27400 -0.80000 12.02800  1.000 58.91741  ? 331 SER A OG   1 
ATOM   97   H  H    . SER A 1 12  ? 19.73600 0.74100  15.47400  1.000 47.21137  ? 331 SER A H    1 
ATOM   98   H  HA   . SER A 1 12  ? 21.45900 0.96700  13.51800  1.000 46.76692  ? 331 SER A HA   1 
ATOM   99   H  HB2  . SER A 1 12  ? 20.47100 -1.11600 13.97000  1.000 51.79597  ? 331 SER A HB2  1 
ATOM   100  H  HB3  . SER A 1 12  ? 19.06900 -0.55800 13.57700  1.000 51.79597  ? 331 SER A HB3  1 
ATOM   101  H  HG   . SER A 1 12  ? 20.99500 -0.44100 11.78800  1.000 70.77789  ? 331 SER A HG   1 
ATOM   102  N  N    . LEU A 1 13  ? 20.49300 2.21900  11.61400  1.000 37.72770  ? 332 LEU A N    1 
ATOM   103  C  CA   . LEU A 1 13  ? 19.87500 2.94700  10.51900  1.000 41.02666  ? 332 LEU A CA   1 
ATOM   104  C  C    . LEU A 1 13  ? 20.56000 2.51400  9.22800   1.000 41.92967  ? 332 LEU A C    1 
ATOM   105  O  O    . LEU A 1 13  ? 21.68500 2.92100  8.94500   1.000 43.60982  ? 332 LEU A O    1 
ATOM   106  C  CB   . LEU A 1 13  ? 19.96400 4.46800  10.68700  1.000 36.73286  ? 332 LEU A CB   1 
ATOM   107  C  CG   . LEU A 1 13  ? 19.35300 5.28500  9.50200   1.000 38.17987  ? 332 LEU A CG   1 
ATOM   108  C  CD1  . LEU A 1 13  ? 17.87000 5.09100  9.41400   1.000 37.77249  ? 332 LEU A CD1  1 
ATOM   109  C  CD2  . LEU A 1 13  ? 19.66100 6.77600  9.62700   1.000 34.14201  ? 332 LEU A CD2  1 
ATOM   110  H  H    . LEU A 1 13  ? 21.31600 2.00800  11.47900  1.000 45.35023  ? 332 LEU A H    1 
ATOM   111  H  HA   . LEU A 1 13  ? 18.92800 2.73700  10.50200  1.000 49.30899  ? 332 LEU A HA   1 
ATOM   112  H  HB2  . LEU A 1 13  ? 19.51000 4.71900  11.50700  1.000 44.15643  ? 332 LEU A HB2  1 
ATOM   113  H  HB3  . LEU A 1 13  ? 20.89600 4.71700  10.79100  1.000 44.15643  ? 332 LEU A HB3  1 
ATOM   114  H  HG   . LEU A 1 13  ? 19.76600 4.94900  8.69100   1.000 45.89284  ? 332 LEU A HG   1 
ATOM   115  H  HD11 . LEU A 1 13  ? 17.51900 5.60800  8.67200   1.000 45.40398  ? 332 LEU A HD11 1 
ATOM   116  H  HD12 . LEU A 1 13  ? 17.67400 4.15100  9.27400   1.000 45.40398  ? 332 LEU A HD12 1 
ATOM   117  H  HD13 . LEU A 1 13  ? 17.45500 5.38800  10.23900  1.000 45.40398  ? 332 LEU A HD13 1 
ATOM   118  H  HD21 . LEU A 1 13  ? 19.26900 7.25200  8.87800   1.000 41.04741  ? 332 LEU A HD21 1 
ATOM   119  H  HD22 . LEU A 1 13  ? 19.28800 7.11500  10.45600  1.000 41.04741  ? 332 LEU A HD22 1 
ATOM   120  H  HD23 . LEU A 1 13  ? 20.62200 6.90900  9.62600   1.000 41.04741  ? 332 LEU A HD23 1 
ATOM   121  N  N    . ARG A 1 14  ? 19.86700 1.66400  8.47000   1.000 40.23473  ? 333 ARG A N    1 
ATOM   122  C  CA   . ARG A 1 14  ? 20.36800 1.19200  7.19400   1.000 41.35021  ? 333 ARG A CA   1 
ATOM   123  C  C    . ARG A 1 14  ? 19.91500 2.14900  6.09500   1.000 44.02843  ? 333 ARG A C    1 
ATOM   124  O  O    . ARG A 1 14  ? 18.71900 2.36400  5.92500   1.000 42.76452  ? 333 ARG A O    1 
ATOM   125  C  CB   . ARG A 1 14  ? 19.87900 -0.22700 6.92800   1.000 55.69235  ? 333 ARG A CB   1 
ATOM   126  C  CG   . ARG A 1 14  ? 20.66200 -0.89300 5.82200   1.000 69.45497  ? 333 ARG A CG   1 
ATOM   127  C  CD   . ARG A 1 14  ? 20.46000 -2.39000 5.77800   1.000 80.52618  ? 333 ARG A CD   1 
ATOM   128  N  NE   . ARG A 1 14  ? 21.30600 -3.00200 4.76200   1.000 97.53504  ? 333 ARG A NE   1 
ATOM   129  C  CZ   . ARG A 1 14  ? 22.63200 -3.04200 4.81200   1.000 78.32271  ? 333 ARG A CZ   1 
ATOM   130  N  NH1  . ARG A 1 14  ? 23.29200 -2.74000 5.91900   1.000 65.58627  ? 333 ARG A NH1  1 
ATOM   131  N  NH2  . ARG A 1 14  ? 23.31300 -3.40800 3.72800   1.000 94.39119  ? 333 ARG A NH2  1 
ATOM   132  H  H    . ARG A 1 14  ? 19.09600 1.34900  8.68600   1.000 48.35867  ? 333 ARG A H    1 
ATOM   133  H  HA   . ARG A 1 14  ? 21.33800 1.17000  7.20900   1.000 49.69725  ? 333 ARG A HA   1 
ATOM   134  H  HB2  . ARG A 1 14  ? 19.95500 -0.75300 7.74000   1.000 66.90781  ? 333 ARG A HB2  1 
ATOM   135  H  HB3  . ARG A 1 14  ? 18.93900 -0.20600 6.69100   1.000 66.90781  ? 333 ARG A HB3  1 
ATOM   136  H  HG2  . ARG A 1 14  ? 20.39900 -0.51100 4.97000   1.000 83.42296  ? 333 ARG A HG2  1 
ATOM   137  H  HG3  . ARG A 1 14  ? 21.60600 -0.70200 5.94000   1.000 83.42296  ? 333 ARG A HG3  1 
ATOM   138  H  HD2  . ARG A 1 14  ? 20.66300 -2.77300 6.64600   1.000 96.70841  ? 333 ARG A HD2  1 
ATOM   139  H  HD3  . ARG A 1 14  ? 19.52900 -2.58900 5.59100   1.000 96.70841  ? 333 ARG A HD3  1 
ATOM   140  H  HE   . ARG A 1 14  ? 20.92000 -3.36200 4.08300   1.000 117.11905 ? 333 ARG A HE   1 
ATOM   141  H  HH11 . ARG A 1 14  ? 22.86100 -2.51100 6.62800   1.000 78.78052  ? 333 ARG A HH11 1 
ATOM   142  H  HH12 . ARG A 1 14  ? 24.15100 -2.77200 5.93000   1.000 78.78052  ? 333 ARG A HH12 1 
ATOM   143  H  HH21 . ARG A 1 14  ? 22.89400 -3.61500 3.00600   1.000 113.34642 ? 333 ARG A HH21 1 
ATOM   144  H  HH22 . ARG A 1 14  ? 24.17200 -3.43700 3.75000   1.000 113.34642 ? 333 ARG A HH22 1 
ATOM   145  N  N    . VAL A 1 15  ? 20.89000 2.71900  5.37600   1.000 42.32000  ? 334 VAL A N    1 
ATOM   146  C  CA   . VAL A 1 15  ? 20.65000 3.71400  4.34400   1.000 39.96882  ? 334 VAL A CA   1 
ATOM   147  C  C    . VAL A 1 15  ? 20.84900 3.11000  2.93700   1.000 42.57922  ? 334 VAL A C    1 
ATOM   148  O  O    . VAL A 1 15  ? 21.96500 2.64500  2.64300   1.000 42.80221  ? 334 VAL A O    1 
ATOM   149  C  CB   . VAL A 1 15  ? 21.58400 4.91600  4.54800   1.000 37.89096  ? 334 VAL A CB   1 
ATOM   150  C  CG1  . VAL A 1 15  ? 21.53200 5.86900  3.35100   1.000 39.25138  ? 334 VAL A CG1  1 
ATOM   151  C  CG2  . VAL A 1 15  ? 21.27700 5.63600  5.85600   1.000 39.11134  ? 334 VAL A CG2  1 
ATOM   152  H  H    . VAL A 1 15  ? 21.72200 2.52900  5.48300   1.000 50.86100  ? 334 VAL A H    1 
ATOM   153  H  HA   . VAL A 1 15  ? 19.73000 4.01300  4.41400   1.000 47.57760  ? 334 VAL A HA   1 
ATOM   154  H  HB   . VAL A 1 15  ? 22.49200 4.58000  4.60900   1.000 45.08417  ? 334 VAL A HB   1 
ATOM   155  H  HG11 . VAL A 1 15  ? 22.13000 6.61700  3.50600   1.000 46.71667  ? 334 VAL A HG11 1 
ATOM   156  H  HG12 . VAL A 1 15  ? 21.80700 5.39700  2.54900   1.000 46.71667  ? 334 VAL A HG12 1 
ATOM   157  H  HG13 . VAL A 1 15  ? 20.62600 6.19800  3.23800   1.000 46.71667  ? 334 VAL A HG13 1 
ATOM   158  H  HG21 . VAL A 1 15  ? 21.87900 6.38900  5.96000   1.000 47.01061  ? 334 VAL A HG21 1 
ATOM   159  H  HG22 . VAL A 1 15  ? 20.36100 5.95500  5.84300   1.000 47.01061  ? 334 VAL A HG22 1 
ATOM   160  H  HG23 . VAL A 1 15  ? 21.39500 5.02300  6.59800   1.000 47.01061  ? 334 VAL A HG23 1 
ATOM   161  N  N    . ASN A 1 16  ? 19.84200 3.24600  2.06700   1.000 45.21101  ? 335 ASN A N    1 
ATOM   162  C  CA   . ASN A 1 16  ? 19.92400 2.97900  0.59800   1.000 47.77934  ? 335 ASN A CA   1 
ATOM   163  C  C    . ASN A 1 16  ? 20.24700 4.26400  -0.17800  1.000 48.35171  ? 335 ASN A C    1 
ATOM   164  O  O    . ASN A 1 16  ? 19.46500 5.21500  -0.07800  1.000 48.27151  ? 335 ASN A O    1 
ATOM   165  C  CB   . ASN A 1 16  ? 18.64500 2.29400  0.12800   1.000 51.24308  ? 335 ASN A CB   1 
ATOM   166  C  CG   . ASN A 1 16  ? 18.70900 1.82000  -1.30600  1.000 66.46196  ? 335 ASN A CG   1 
ATOM   167  O  OD1  . ASN A 1 16  ? 18.82600 2.62600  -2.22200  1.000 55.38795  ? 335 ASN A OD1  1 
ATOM   168  N  ND2  . ASN A 1 16  ? 18.62200 0.51800  -1.50900  1.000 56.13816  ? 335 ASN A ND2  1 
ATOM   169  H  H    . ASN A 1 16  ? 19.06000 3.50500  2.31300   1.000 54.33021  ? 335 ASN A H    1 
ATOM   170  H  HA   . ASN A 1 16  ? 20.65800 2.37100  0.41700   1.000 57.34350  ? 335 ASN A HA   1 
ATOM   171  H  HB2  . ASN A 1 16  ? 18.46200 1.53600  0.70400   1.000 61.56870  ? 335 ASN A HB2  1 
ATOM   172  H  HB3  . ASN A 1 16  ? 17.90200 2.91000  0.22500   1.000 61.56870  ? 335 ASN A HB3  1 
ATOM   173  H  HD21 . ASN A 1 16  ? 18.64700 0.20500  -2.31000  1.000 67.44279  ? 335 ASN A HD21 1 
ATOM   174  H  HD22 . ASN A 1 16  ? 18.54100 -0.01700 -0.84100  1.000 67.44279  ? 335 ASN A HD22 1 
ATOM   175  N  N    . PHE A 1 17  ? 21.35400 4.29000  -0.92100  1.000 49.24248  ? 336 PHE A N    1 
ATOM   176  C  CA   . PHE A 1 17  ? 21.80000 5.46200  -1.65300  1.000 49.45656  ? 336 PHE A CA   1 
ATOM   177  C  C    . PHE A 1 17  ? 20.84100 5.89600  -2.76200  1.000 52.29833  ? 336 PHE A C    1 
ATOM   178  O  O    . PHE A 1 17  ? 20.72800 7.08300  -3.04100  1.000 52.58059  ? 336 PHE A O    1 
ATOM   179  C  CB   . PHE A 1 17  ? 23.18700 5.19400  -2.23700  1.000 49.24842  ? 336 PHE A CB   1 
ATOM   180  C  CG   . PHE A 1 17  ? 24.27400 5.16400  -1.19500  1.000 46.52131  ? 336 PHE A CG   1 
ATOM   181  C  CD1  . PHE A 1 17  ? 24.51000 6.26400  -0.38300  1.000 44.53321  ? 336 PHE A CD1  1 
ATOM   182  C  CD2  . PHE A 1 17  ? 25.04500 4.03100  -1.00500  1.000 46.13815  ? 336 PHE A CD2  1 
ATOM   183  C  CE1  . PHE A 1 17  ? 25.50700 6.23600  0.57800   1.000 42.24848  ? 336 PHE A CE1  1 
ATOM   184  C  CE2  . PHE A 1 17  ? 26.04100 4.00800  -0.03800  1.000 43.89118  ? 336 PHE A CE2  1 
ATOM   185  C  CZ   . PHE A 1 17  ? 26.27400 5.11300  0.73600   1.000 41.97708  ? 336 PHE A CZ   1 
ATOM   186  H  H    . PHE A 1 17  ? 21.87300 3.61000  -1.01200  1.000 58.70599  ? 336 PHE A H    1 
ATOM   187  H  HA   . PHE A 1 17  ? 21.82800 6.19600  -1.01900  1.000 58.96289  ? 336 PHE A HA   1 
ATOM   188  H  HB2  . PHE A 1 17  ? 23.17500 4.34600  -2.70800  1.000 58.71312  ? 336 PHE A HB2  1 
ATOM   189  H  HB3  . PHE A 1 17  ? 23.39400 5.87900  -2.89200  1.000 58.71312  ? 336 PHE A HB3  1 
ATOM   190  H  HD1  . PHE A 1 17  ? 23.99200 7.03000  -0.48500  1.000 53.05487  ? 336 PHE A HD1  1 
ATOM   191  H  HD2  . PHE A 1 17  ? 24.89500 3.27800  -1.53000  1.000 54.98080  ? 336 PHE A HD2  1 
ATOM   192  H  HE1  . PHE A 1 17  ? 25.65500 6.98000  1.11600   1.000 50.31319  ? 336 PHE A HE1  1 
ATOM   193  H  HE2  . PHE A 1 17  ? 26.55100 3.24000  0.08400   1.000 52.28442  ? 336 PHE A HE2  1 
ATOM   194  H  HZ   . PHE A 1 17  ? 26.95400 5.10100  1.37000   1.000 49.98751  ? 336 PHE A HZ   1 
ATOM   195  N  N    . GLU A 1 18  ? 20.16800 4.93500  -3.40300  1.000 54.61539  ? 337 GLU A N    1 
ATOM   196  C  CA   . GLU A 1 18  ? 19.10200 5.25500  -4.33800  1.000 57.57365  ? 337 GLU A CA   1 
ATOM   197  C  C    . GLU A 1 18  ? 17.98800 6.04400  -3.65500  1.000 57.49637  ? 337 GLU A C    1 
ATOM   198  O  O    . GLU A 1 18  ? 17.51800 7.04600  -4.19800  1.000 58.90645  ? 337 GLU A O    1 
ATOM   199  C  CB   . GLU A 1 18  ? 18.54900 3.98100  -5.00600  1.000 60.10520  ? 337 GLU A CB   1 
ATOM   200  C  CG   . GLU A 1 18  ? 17.50700 4.28200  -6.07100  1.000 63.54094  ? 337 GLU A CG   1 
ATOM   201  C  CD   . GLU A 1 18  ? 17.10300 3.11900  -6.95600  1.000 75.29119  ? 337 GLU A CD   1 
ATOM   202  O  OE1  . GLU A 1 18  ? 17.79900 2.07900  -6.94000  1.000 65.92925  ? 337 GLU A OE1  1 
ATOM   203  O  OE2  . GLU A 1 18  ? 16.07800 3.24900  -7.66400  1.000 116.00432 ? 337 GLU A OE2  1 
ATOM   204  H  H    . GLU A 1 18  ? 20.31800 4.09400  -3.30600  1.000 65.15348  ? 337 GLU A H    1 
ATOM   205  H  HA   . GLU A 1 18  ? 19.47800 5.81600  -5.03400  1.000 68.70340  ? 337 GLU A HA   1 
ATOM   206  H  HB2  . GLU A 1 18  ? 19.28100 3.48600  -5.40600  1.000 71.74125  ? 337 GLU A HB2  1 
ATOM   207  H  HB3  . GLU A 1 18  ? 18.15700 3.40900  -4.32800  1.000 71.74125  ? 337 GLU A HB3  1 
ATOM   208  H  HG2  . GLU A 1 18  ? 16.71200 4.62300  -5.63200  1.000 75.86414  ? 337 GLU A HG2  1 
ATOM   209  H  HG3  . GLU A 1 18  ? 17.84600 4.99300  -6.63700  1.000 75.86414  ? 337 GLU A HG3  1 
ATOM   210  N  N    . ASP A 1 19  ? 17.58200 5.60900  -2.45400  1.000 56.05969  ? 338 ASP A N    1 
ATOM   211  C  CA   . ASP A 1 19  ? 16.51100 6.27800  -1.73200  1.000 57.74806  ? 338 ASP A CA   1 
ATOM   212  C  C    . ASP A 1 19  ? 16.80800 7.75500  -1.49300  1.000 54.83503  ? 338 ASP A C    1 
ATOM   213  O  O    . ASP A 1 19  ? 15.88100 8.55900  -1.47100  1.000 56.06331  ? 338 ASP A O    1 
ATOM   214  C  CB   . ASP A 1 19  ? 16.24000 5.61200  -0.37500  1.000 60.09902  ? 338 ASP A CB   1 
ATOM   215  C  CG   . ASP A 1 19  ? 15.49600 4.29600  -0.40400  1.000 61.70665  ? 338 ASP A CG   1 
ATOM   216  O  OD1  . ASP A 1 19  ? 15.05300 3.89100  -1.49200  1.000 59.31371  ? 338 ASP A OD1  1 
ATOM   217  O  OD2  . ASP A 1 19  ? 15.37500 3.65900  0.67000   1.000 60.12752  ? 338 ASP A OD2  1 
ATOM   218  H  H    . ASP A 1 19  ? 17.91800 4.92900  -2.04800  1.000 66.88665  ? 338 ASP A H    1 
ATOM   219  H  HA   . ASP A 1 19  ? 15.72700 6.20000  -2.29700  1.000 69.37467  ? 338 ASP A HA   1 
ATOM   220  H  HB2  . ASP A 1 19  ? 17.09100 5.47000  0.06800   1.000 72.19582  ? 338 ASP A HB2  1 
ATOM   221  H  HB3  . ASP A 1 19  ? 15.73500 6.23400  0.17300   1.000 72.19582  ? 338 ASP A HB3  1 
ATOM   222  N  N    . ILE A 1 20  ? 18.09000 8.09400  -1.27500  1.000 54.76887  ? 339 ILE A N    1 
ATOM   223  C  CA   . ILE A 1 20  ? 18.49300 9.47000  -1.01200  1.000 51.98035  ? 339 ILE A CA   1 
ATOM   224  C  C    . ILE A 1 20  ? 19.08400 10.18800 -2.23000  1.000 55.90399  ? 339 ILE A C    1 
ATOM   225  O  O    . ILE A 1 20  ? 19.62800 11.28200 -2.09400  1.000 51.56494  ? 339 ILE A O    1 
ATOM   226  C  CB   . ILE A 1 20  ? 19.48000 9.54300  0.18100   1.000 51.14789  ? 339 ILE A CB   1 
ATOM   227  C  CG1  . ILE A 1 20  ? 20.82300 8.86500  -0.12800  1.000 46.89422  ? 339 ILE A CG1  1 
ATOM   228  C  CG2  . ILE A 1 20  ? 18.85400 8.97100  1.45100   1.000 50.57540  ? 339 ILE A CG2  1 
ATOM   229  C  CD1  . ILE A 1 20  ? 21.91600 9.30000  0.75700   1.000 46.14201  ? 339 ILE A CD1  1 
ATOM   230  H  H    . ILE A 1 20  ? 18.74000 7.53100  -1.27700  1.000 65.79965  ? 339 ILE A H    1 
ATOM   231  H  HA   . ILE A 1 20  ? 17.67500 9.94000  -0.78600  1.000 62.45342  ? 339 ILE A HA   1 
ATOM   232  H  HB   . ILE A 1 20  ? 19.66700 10.48300 0.33300   1.000 61.45446  ? 339 ILE A HB   1 
ATOM   233  H  HG12 . ILE A 1 20  ? 20.71700 7.90400  -0.05200  1.000 56.06377  ? 339 ILE A HG12 1 
ATOM   234  H  HG13 . ILE A 1 20  ? 21.06700 9.05100  -1.04800  1.000 56.06377  ? 339 ILE A HG13 1 
ATOM   235  H  HG21 . ILE A 1 20  ? 19.49100 9.02900  2.18000   1.000 60.76747  ? 339 ILE A HG21 1 
ATOM   236  H  HG22 . ILE A 1 20  ? 18.05800 9.47800  1.67600   1.000 60.76747  ? 339 ILE A HG22 1 
ATOM   237  H  HG23 . ILE A 1 20  ? 18.61500 8.04300  1.30400   1.000 60.76747  ? 339 ILE A HG23 1 
ATOM   238  H  HD11 . ILE A 1 20  ? 22.73300 8.83900  0.51300   1.000 55.44741  ? 339 ILE A HD11 1 
ATOM   239  H  HD12 . ILE A 1 20  ? 22.04600 10.25700 0.66500   1.000 55.44741  ? 339 ILE A HD12 1 
ATOM   240  H  HD13 . ILE A 1 20  ? 21.69000 9.09200  1.67700   1.000 55.44741  ? 339 ILE A HD13 1 
ATOM   241  N  N    . GLY A 1 21  ? 18.97000 9.57800  -3.41500  1.000 54.98894  ? 340 GLY A N    1 
ATOM   242  C  CA   . GLY A 1 21  ? 19.38300 10.22000 -4.65300  1.000 56.94642  ? 340 GLY A CA   1 
ATOM   243  C  C    . GLY A 1 21  ? 20.88500 10.23700 -4.94200  1.000 59.05143  ? 340 GLY A C    1 
ATOM   244  O  O    . GLY A 1 21  ? 21.33500 11.00400 -5.79500  1.000 57.34557  ? 340 GLY A O    1 
ATOM   245  H  H    . GLY A 1 21  ? 18.65200 8.78500  -3.51700  1.000 65.60174  ? 340 GLY A H    1 
ATOM   246  H  HA2  . GLY A 1 21  ? 18.93700 9.77500  -5.39000  1.000 67.95071  ? 340 GLY A HA2  1 
ATOM   247  H  HA3  . GLY A 1 21  ? 19.06500 11.13600 -4.64100  1.000 67.95071  ? 340 GLY A HA3  1 
ATOM   248  N  N    . TRP A 1 22  ? 21.64600 9.37500  -4.25400  1.000 53.62755  ? 341 TRP A N    1 
ATOM   249  C  CA   . TRP A 1 22  ? 23.09400 9.31000  -4.41000  1.000 52.60994  ? 341 TRP A CA   1 
ATOM   250  C  C    . TRP A 1 22  ? 23.59000 8.16400  -5.29600  1.000 56.18338  ? 341 TRP A C    1 
ATOM   251  O  O    . TRP A 1 22  ? 24.79400 8.04500  -5.54900  1.000 53.83042  ? 341 TRP A O    1 
ATOM   252  C  CB   . TRP A 1 22  ? 23.77000 9.21800  -3.02500  1.000 49.25002  ? 341 TRP A CB   1 
ATOM   253  C  CG   . TRP A 1 22  ? 23.82600 10.50800 -2.26300  1.000 47.65034  ? 341 TRP A CG   1 
ATOM   254  C  CD1  . TRP A 1 22  ? 23.13500 11.65700 -2.51900  1.000 48.99960  ? 341 TRP A CD1  1 
ATOM   255  C  CD2  . TRP A 1 22  ? 24.63700 10.77400 -1.11200  1.000 44.84819  ? 341 TRP A CD2  1 
ATOM   256  N  NE1  . TRP A 1 22  ? 23.45700 12.62200 -1.58400  1.000 47.54401  ? 341 TRP A NE1  1 
ATOM   257  C  CE2  . TRP A 1 22  ? 24.38100 12.10500 -0.71400  1.000 44.32742  ? 341 TRP A CE2  1 
ATOM   258  C  CE3  . TRP A 1 22  ? 25.54900 10.01100 -0.37100  1.000 44.06211  ? 341 TRP A CE3  1 
ATOM   259  C  CZ2  . TRP A 1 22  ? 25.01200 12.68500 0.38600   1.000 42.92391  ? 341 TRP A CZ2  1 
ATOM   260  C  CZ3  . TRP A 1 22  ? 26.17700 10.59000 0.71200   1.000 40.74558  ? 341 TRP A CZ3  1 
ATOM   261  C  CH2  . TRP A 1 22  ? 25.90300 11.90700 1.08700   1.000 45.50961  ? 341 TRP A CH2  1 
ATOM   262  H  H    . TRP A 1 22  ? 21.33000 8.81300  -3.68400  1.000 63.96807  ? 341 TRP A H    1 
ATOM   263  H  HA   . TRP A 1 22  ? 23.34200 10.12900 -4.86600  1.000 62.74695  ? 341 TRP A HA   1 
ATOM   264  H  HB2  . TRP A 1 22  ? 23.29500 8.56200  -2.49100  1.000 58.71504  ? 341 TRP A HB2  1 
ATOM   265  H  HB3  . TRP A 1 22  ? 24.67400 8.88700  -3.14200  1.000 58.71504  ? 341 TRP A HB3  1 
ATOM   266  H  HD1  . TRP A 1 22  ? 22.53500 11.77300 -3.22000  1.000 58.87652  ? 341 TRP A HD1  1 
ATOM   267  H  HE1  . TRP A 1 22  ? 23.13100 13.41700 -1.55300  1.000 57.12981  ? 341 TRP A HE1  1 
ATOM   268  H  HE3  . TRP A 1 22  ? 25.72800 9.12900  -0.60500  1.000 52.95153  ? 341 TRP A HE3  1 
ATOM   269  H  HZ2  . TRP A 1 22  ? 24.83700 13.56400 0.63600   1.000 51.58569  ? 341 TRP A HZ2  1 
ATOM   270  H  HZ3  . TRP A 1 22  ? 26.79400 10.09500 1.20100   1.000 48.97169  ? 341 TRP A HZ3  1 
ATOM   271  H  HH2  . TRP A 1 22  ? 26.33400 12.26700 1.82900   1.000 54.68853  ? 341 TRP A HH2  1 
ATOM   272  N  N    . ASP A 1 23  ? 22.66100 7.33100  -5.78600  1.000 56.10784  ? 342 ASP A N    1 
ATOM   273  C  CA   . ASP A 1 23  ? 23.00200 6.23500  -6.67900  1.000 59.32958  ? 342 ASP A CA   1 
ATOM   274  C  C    . ASP A 1 23  ? 23.44000 6.74400  -8.05300  1.000 65.58808  ? 342 ASP A C    1 
ATOM   275  O  O    . ASP A 1 23  ? 23.98800 5.99000  -8.84900  1.000 66.63084  ? 342 ASP A O    1 
ATOM   276  C  CB   . ASP A 1 23  ? 21.80700 5.28500  -6.83300  1.000 69.20343  ? 342 ASP A CB   1 
ATOM   277  C  CG   . ASP A 1 23  ? 20.62800 5.93200  -7.52000  1.000 71.67423  ? 342 ASP A CG   1 
ATOM   278  O  OD1  . ASP A 1 23  ? 20.26700 7.06200  -7.13100  1.000 63.21789  ? 342 ASP A OD1  1 
ATOM   279  O  OD2  . ASP A 1 23  ? 20.06500 5.30900  -8.43800  1.000 83.72601  ? 342 ASP A OD2  1 
ATOM   280  H  H    . ASP A 1 23  ? 21.82200 7.39200  -5.60600  1.000 66.94442  ? 342 ASP A H    1 
ATOM   281  H  HA   . ASP A 1 23  ? 23.74700 5.75600  -6.28400  1.000 71.27250  ? 342 ASP A HA   1 
ATOM   282  H  HB2  . ASP A 1 23  ? 22.08300 4.50500  -7.33900  1.000 83.12112  ? 342 ASP A HB2  1 
ATOM   283  H  HB3  . ASP A 1 23  ? 21.53300 4.97200  -5.95700  1.000 83.12112  ? 342 ASP A HB3  1 
ATOM   284  N  N    . SER A 1 24  ? 23.18000 8.02600  -8.32700  1.000 67.04297  ? 343 SER A N    1 
ATOM   285  C  CA   . SER A 1 24  ? 23.72400 8.68800  -9.49900  1.000 101.02541 ? 343 SER A CA   1 
ATOM   286  C  C    . SER A 1 24  ? 25.25200 8.70000  -9.52900  1.000 82.64291  ? 343 SER A C    1 
ATOM   287  O  O    . SER A 1 24  ? 25.83800 8.67800  -10.60800 1.000 85.76912  ? 343 SER A O    1 
ATOM   288  C  CB   . SER A 1 24  ? 23.18300 10.11400 -9.59900  1.000 119.63891 ? 343 SER A CB   1 
ATOM   289  O  OG   . SER A 1 24  ? 23.36200 10.82300 -8.38400  1.000 84.21276  ? 343 SER A OG   1 
ATOM   290  H  H    . SER A 1 24  ? 22.68400 8.52900  -7.83600  1.000 80.52856  ? 343 SER A H    1 
ATOM   291  H  HA   . SER A 1 24  ? 23.43500 8.17200  -10.26800 1.000 121.30749 ? 343 SER A HA   1 
ATOM   292  H  HB2  . SER A 1 24  ? 23.63400 10.58300 -10.31800 1.000 143.64369 ? 343 SER A HB2  1 
ATOM   293  H  HB3  . SER A 1 24  ? 22.24000 10.08900 -9.82500  1.000 143.64369 ? 343 SER A HB3  1 
ATOM   294  H  HG   . SER A 1 24  ? 22.74900 10.61800 -7.84700  1.000 101.13231 ? 343 SER A HG   1 
ATOM   295  N  N    . TRP A 1 25  ? 25.89500 8.73700  -8.35300  1.000 59.62603  ? 344 TRP A N    1 
ATOM   296  C  CA   . TRP A 1 25  ? 27.34900 8.80200  -8.29600  1.000 58.83015  ? 344 TRP A CA   1 
ATOM   297  C  C    . TRP A 1 25  ? 28.01000 7.67100  -7.50700  1.000 57.20369  ? 344 TRP A C    1 
ATOM   298  O  O    . TRP A 1 25  ? 29.14000 7.30400  -7.81400  1.000 59.11622  ? 344 TRP A O    1 
ATOM   299  C  CB   . TRP A 1 25  ? 27.81900 10.18000 -7.78200  1.000 58.75976  ? 344 TRP A CB   1 
ATOM   300  C  CG   . TRP A 1 25  ? 27.70000 10.41000 -6.30900  1.000 75.84568  ? 344 TRP A CG   1 
ATOM   301  C  CD1  . TRP A 1 25  ? 26.56500 10.66900 -5.59700  1.000 133.78766 ? 344 TRP A CD1  1 
ATOM   302  C  CD2  . TRP A 1 25  ? 28.77500 10.41000 -5.36600  1.000 70.44911  ? 344 TRP A CD2  1 
ATOM   303  N  NE1  . TRP A 1 25  ? 26.87100 10.82900 -4.26300  1.000 74.59352  ? 344 TRP A NE1  1 
ATOM   304  C  CE2  . TRP A 1 25  ? 28.22200 10.67500 -4.09500  1.000 75.84254  ? 344 TRP A CE2  1 
ATOM   305  C  CE3  . TRP A 1 25  ? 30.15600 10.21100 -5.47300  1.000 74.83296  ? 344 TRP A CE3  1 
ATOM   306  C  CZ2  . TRP A 1 25  ? 29.00500 10.74100 -2.94400  1.000 70.84879  ? 344 TRP A CZ2  1 
ATOM   307  C  CZ3  . TRP A 1 25  ? 30.92800 10.27600 -4.33200  1.000 97.00160  ? 344 TRP A CZ3  1 
ATOM   308  C  CH2  . TRP A 1 25  ? 30.35500 10.53800 -3.08700  1.000 74.32192  ? 344 TRP A CH2  1 
ATOM   309  H  H    . TRP A 1 25  ? 25.50500 8.72500  -7.58700  1.000 71.16625  ? 344 TRP A H    1 
ATOM   310  H  HA   . TRP A 1 25  ? 27.64500 8.68000  -9.21200  1.000 70.21120  ? 344 TRP A HA   1 
ATOM   311  H  HB2  . TRP A 1 25  ? 28.74800 10.30000 -8.03500  1.000 70.58871  ? 344 TRP A HB2  1 
ATOM   312  H  HB3  . TRP A 1 25  ? 27.30900 10.86700 -8.24000  1.000 70.58871  ? 344 TRP A HB3  1 
ATOM   313  H  HD1  . TRP A 1 25  ? 25.71000 10.72900 -5.95900  1.000 160.62218 ? 344 TRP A HD1  1 
ATOM   314  H  HE1  . TRP A 1 25  ? 26.30600 10.99800 -3.63700  1.000 89.58922  ? 344 TRP A HE1  1 
ATOM   315  H  HE3  . TRP A 1 25  ? 30.54600 10.03800 -6.29900  1.000 89.87655  ? 344 TRP A HE3  1 
ATOM   316  H  HZ2  . TRP A 1 25  ? 28.62800 10.91600 -2.11200  1.000 85.09554  ? 344 TRP A HZ2  1 
ATOM   317  H  HZ3  . TRP A 1 25  ? 31.84600 10.14300 -4.39300  1.000 116.47891 ? 344 TRP A HZ3  1 
ATOM   318  H  HH2  . TRP A 1 25  ? 30.90100 10.57600 -2.33500  1.000 89.26330  ? 344 TRP A HH2  1 
ATOM   319  N  N    . ILE A 1 26  ? 27.31200 7.11100  -6.51100  1.000 58.50498  ? 345 ILE A N    1 
ATOM   320  C  CA   . ILE A 1 26  ? 27.79500 5.92500  -5.81900  1.000 54.94370  ? 345 ILE A CA   1 
ATOM   321  C  C    . ILE A 1 26  ? 27.32900 4.65700  -6.53000  1.000 59.04875  ? 345 ILE A C    1 
ATOM   322  O  O    . ILE A 1 26  ? 26.13500 4.38100  -6.59700  1.000 58.03250  ? 345 ILE A O    1 
ATOM   323  C  CB   . ILE A 1 26  ? 27.36800 5.90900  -4.33500  1.000 54.57221  ? 345 ILE A CB   1 
ATOM   324  C  CG1  . ILE A 1 26  ? 28.00600 7.07900  -3.57900  1.000 52.81285  ? 345 ILE A CG1  1 
ATOM   325  C  CG2  . ILE A 1 26  ? 27.71400 4.55900  -3.68200  1.000 57.60812  ? 345 ILE A CG2  1 
ATOM   326  C  CD1  . ILE A 1 26  ? 27.43200 7.35100  -2.31200  1.000 46.63276  ? 345 ILE A CD1  1 
ATOM   327  H  H    . ILE A 1 26  ? 26.55700 7.40800  -6.22600  1.000 70.28297  ? 345 ILE A H    1 
ATOM   328  H  HA   . ILE A 1 26  ? 28.76400 5.95300  -5.84000  1.000 66.00944  ? 345 ILE A HA   1 
ATOM   329  H  HB   . ILE A 1 26  ? 26.40500 6.01700  -4.29000  1.000 65.56365  ? 345 ILE A HB   1 
ATOM   330  H  HG12 . ILE A 1 26  ? 28.95100 6.89400  -3.45900  1.000 63.45242  ? 345 ILE A HG12 1 
ATOM   331  H  HG13 . ILE A 1 26  ? 27.94100 7.87600  -4.12800  1.000 63.45242  ? 345 ILE A HG13 1 
ATOM   332  H  HG21 . ILE A 1 26  ? 27.43800 4.56900  -2.75200  1.000 69.20674  ? 345 ILE A HG21 1 
ATOM   333  H  HG22 . ILE A 1 26  ? 27.25100 3.84600  -4.14800  1.000 69.20674  ? 345 ILE A HG22 1 
ATOM   334  H  HG23 . ILE A 1 26  ? 28.67100 4.41000  -3.73400  1.000 69.20674  ? 345 ILE A HG23 1 
ATOM   335  H  HD11 . ILE A 1 26  ? 27.89100 8.10100  -1.90300  1.000 56.03631  ? 345 ILE A HD11 1 
ATOM   336  H  HD12 . ILE A 1 26  ? 26.49300 7.56800  -2.42200  1.000 56.03631  ? 345 ILE A HD12 1 
ATOM   337  H  HD13 . ILE A 1 26  ? 27.51900 6.57000  -1.74300  1.000 56.03631  ? 345 ILE A HD13 1 
ATOM   338  N  N    . ILE A 1 27  ? 28.30200 3.88000  -7.01900  1.000 62.09534  ? 346 ILE A N    1 
ATOM   339  C  CA   . ILE A 1 27  ? 28.05500 2.62700  -7.71400  1.000 69.69000  ? 346 ILE A CA   1 
ATOM   340  C  C    . ILE A 1 27  ? 27.82800 1.49900  -6.71400  1.000 66.52895  ? 346 ILE A C    1 
ATOM   341  O  O    . ILE A 1 27  ? 26.94400 0.66300  -6.89900  1.000 67.84281  ? 346 ILE A O    1 
ATOM   342  C  CB   . ILE A 1 27  ? 29.24900 2.30200  -8.63500  1.000 70.64514  ? 346 ILE A CB   1 
ATOM   343  C  CG1  . ILE A 1 27  ? 29.51600 3.44400  -9.63700  1.000 80.40232  ? 346 ILE A CG1  1 
ATOM   344  C  CG2  . ILE A 1 27  ? 29.04300 0.96500  -9.35100  1.000 79.34213  ? 346 ILE A CG2  1 
ATOM   345  C  CD1  . ILE A 1 27  ? 30.92900 3.42900  -10.20300 1.000 79.84196  ? 346 ILE A CD1  1 
ATOM   346  H  H    . ILE A 1 27  ? 29.13700 4.07600  -6.95100  1.000 74.59140  ? 346 ILE A H    1 
ATOM   347  H  HA   . ILE A 1 27  ? 27.25500 2.71600  -8.25500  1.000 83.70499  ? 346 ILE A HA   1 
ATOM   348  H  HB   . ILE A 1 27  ? 30.03800 2.21900  -8.07700  1.000 84.85117  ? 346 ILE A HB   1 
ATOM   349  H  HG12 . ILE A 1 27  ? 28.88100 3.38000  -10.36700 1.000 96.55978  ? 346 ILE A HG12 1 
ATOM   350  H  HG13 . ILE A 1 27  ? 29.35900 4.29500  -9.19800  1.000 96.55978  ? 346 ILE A HG13 1 
ATOM   351  H  HG21 . ILE A 1 27  ? 29.80500 0.78300  -9.92300  1.000 95.28756  ? 346 ILE A HG21 1 
ATOM   352  H  HG22 . ILE A 1 27  ? 28.95500 0.25600  -8.69500  1.000 95.28756  ? 346 ILE A HG22 1 
ATOM   353  H  HG23 . ILE A 1 27  ? 28.23800 1.00700  -9.89000  1.000 95.28756  ? 346 ILE A HG23 1 
ATOM   354  H  HD11 . ILE A 1 27  ? 31.03700 4.16600  -10.82400 1.000 95.88735  ? 346 ILE A HD11 1 
ATOM   355  H  HD12 . ILE A 1 27  ? 31.56900 3.52000  -9.47900  1.000 95.88735  ? 346 ILE A HD12 1 
ATOM   356  H  HD13 . ILE A 1 27  ? 31.08300 2.59100  -10.66700 1.000 95.88735  ? 346 ILE A HD13 1 
ATOM   357  N  N    . ALA A 1 28  ? 28.67400 1.47500  -5.67700  1.000 54.76701  ? 347 ALA A N    1 
ATOM   358  C  CA   . ALA A 1 28  ? 28.59100 0.48200  -4.62300  1.000 53.27625  ? 347 ALA A CA   1 
ATOM   359  C  C    . ALA A 1 28  ? 29.17100 1.04700  -3.32700  1.000 52.96453  ? 347 ALA A C    1 
ATOM   360  O  O    . ALA A 1 28  ? 30.05100 1.90800  -3.35800  1.000 49.59745  ? 347 ALA A O    1 
ATOM   361  C  CB   . ALA A 1 28  ? 29.33200 -0.78100 -5.02700  1.000 54.69316  ? 347 ALA A CB   1 
ATOM   362  H  H    . ALA A 1 28  ? 29.31300 2.04200  -5.57300  1.000 65.79741  ? 347 ALA A H    1 
ATOM   363  H  HA   . ALA A 1 28  ? 27.65900 0.25700  -4.47700  1.000 64.00850  ? 347 ALA A HA   1 
ATOM   364  H  HB1  . ALA A 1 28  ? 29.26900 -1.43600 -4.31400  1.000 65.70879  ? 347 ALA A HB1  1 
ATOM   365  H  HB2  . ALA A 1 28  ? 28.93700 -1.14400 -5.83500  1.000 65.70879  ? 347 ALA A HB2  1 
ATOM   366  H  HB3  . ALA A 1 28  ? 30.26500 -0.57100 -5.19000  1.000 65.70879  ? 347 ALA A HB3  1 
ATOM   367  N  N    . PRO A 1 29  ? 28.68900 0.60100  -2.14600  1.000 48.14989  ? 348 PRO A N    1 
ATOM   368  C  CA   . PRO A 1 29  ? 27.61600 -0.38300 -2.05500  1.000 49.17267  ? 348 PRO A CA   1 
ATOM   369  C  C    . PRO A 1 29  ? 26.24600 0.23600  -2.31800  1.000 49.89688  ? 348 PRO A C    1 
ATOM   370  O  O    . PRO A 1 29  ? 26.13300 1.45400  -2.38200  1.000 49.23608  ? 348 PRO A O    1 
ATOM   371  C  CB   . PRO A 1 29  ? 27.72400 -0.84400 -0.60800  1.000 47.16539  ? 348 PRO A CB   1 
ATOM   372  C  CG   . PRO A 1 29  ? 28.13800 0.42000  0.11800   1.000 44.83942  ? 348 PRO A CG   1 
ATOM   373  C  CD   . PRO A 1 29  ? 29.11600 1.09300  -0.82400  1.000 45.44318  ? 348 PRO A CD   1 
ATOM   374  H  HA   . PRO A 1 29  ? 27.69900 -1.09400 -2.71000  1.000 58.62222  ? 348 PRO A HA   1 
ATOM   375  H  HB2  . PRO A 1 29  ? 26.88000 -1.18900 -0.27700  1.000 56.21348  ? 348 PRO A HB2  1 
ATOM   376  H  HB3  . PRO A 1 29  ? 28.38000 -1.55000 -0.50300  1.000 56.21348  ? 348 PRO A HB3  1 
ATOM   377  H  HG2  . PRO A 1 29  ? 27.37400 0.98900  0.30000   1.000 53.42232  ? 348 PRO A HG2  1 
ATOM   378  H  HG3  . PRO A 1 29  ? 28.55200 0.21800  0.97200   1.000 53.42232  ? 348 PRO A HG3  1 
ATOM   379  H  HD2  . PRO A 1 29  ? 29.06400 2.06000  -0.76600  1.000 54.14683  ? 348 PRO A HD2  1 
ATOM   380  H  HD3  . PRO A 1 29  ? 30.03300 0.84600  -0.62700  1.000 54.14683  ? 348 PRO A HD3  1 
ATOM   381  N  N    . LYS A 1 30  ? 25.21500 -0.60700 -2.42700  1.000 51.41259  ? 349 LYS A N    1 
ATOM   382  C  CA   . LYS A 1 30  ? 23.85000 -0.14100 -2.61200  1.000 52.43338  ? 349 LYS A CA   1 
ATOM   383  C  C    . LYS A 1 30  ? 23.23300 0.38400  -1.31600  1.000 50.46079  ? 349 LYS A C    1 
ATOM   384  O  O    . LYS A 1 30  ? 22.38300 1.27400  -1.35100  1.000 50.68400  ? 349 LYS A O    1 
ATOM   385  C  CB   . LYS A 1 30  ? 22.98700 -1.27000 -3.19000  1.000 55.09322  ? 349 LYS A CB   1 
ATOM   386  C  CG   . LYS A 1 30  ? 23.34400 -1.63500 -4.64500  1.000 69.18884  ? 349 LYS A CG   1 
ATOM   387  C  CD   . LYS A 1 30  ? 23.10600 -0.48200 -5.62400  1.000 72.36109  ? 349 LYS A CD   1 
ATOM   388  C  CE   . LYS A 1 30  ? 23.18900 -0.89100 -7.08300  1.000 78.68325  ? 349 LYS A CE   1 
ATOM   389  N  NZ   . LYS A 1 30  ? 22.80200 0.22900  -7.99100  1.000 78.07663  ? 349 LYS A NZ   1 
ATOM   390  H  H    . LYS A 1 30  ? 25.29300 -1.46300 -2.39500  1.000 61.31013  ? 349 LYS A H    1 
ATOM   391  H  HA   . LYS A 1 30  ? 23.87900 0.60200  -3.23500  1.000 62.53507  ? 349 LYS A HA   1 
ATOM   392  H  HB2  . LYS A 1 30  ? 23.08400 -2.05900 -2.63300  1.000 65.72688  ? 349 LYS A HB2  1 
ATOM   393  H  HB3  . LYS A 1 30  ? 22.05400 -1.00700 -3.15000  1.000 65.72688  ? 349 LYS A HB3  1 
ATOM   394  H  HG2  . LYS A 1 30  ? 24.27600 -1.90200 -4.68700  1.000 83.10360  ? 349 LYS A HG2  1 
ATOM   395  H  HG3  . LYS A 1 30  ? 22.81600 -2.40100 -4.92000  1.000 83.10360  ? 349 LYS A HG3  1 
ATOM   396  H  HD2  . LYS A 1 30  ? 22.23100 -0.09900 -5.45300  1.000 86.91030  ? 349 LYS A HD2  1 
ATOM   397  H  HD3  . LYS A 1 30  ? 23.75900 0.21500  -5.45500  1.000 86.91030  ? 349 LYS A HD3  1 
ATOM   398  H  HE2  . LYS A 1 30  ? 24.09300 -1.17800 -7.28800  1.000 94.49690  ? 349 LYS A HE2  1 
ATOM   399  H  HE3  . LYS A 1 30  ? 22.60800 -1.65100 -7.24000  1.000 94.49690  ? 349 LYS A HE3  1 
ATOM   400  H  HZ1  . LYS A 1 30  ? 22.45600 -0.10300 -8.74100  1.000 93.76895  ? 349 LYS A HZ1  1 
ATOM   401  H  HZ2  . LYS A 1 30  ? 22.19700 0.74300  -7.58800  1.000 93.76895  ? 349 LYS A HZ2  1 
ATOM   402  H  HZ3  . LYS A 1 30  ? 23.52100 0.71500  -8.18600  1.000 93.76895  ? 349 LYS A HZ3  1 
ATOM   403  N  N    . GLU A 1 31  ? 23.66100 -0.19100 -0.18600  1.000 48.80428  ? 350 GLU A N    1 
ATOM   404  C  CA   . GLU A 1 31  ? 23.15200 0.16000  1.13100   1.000 47.12084  ? 350 GLU A CA   1 
ATOM   405  C  C    . GLU A 1 31  ? 24.28800 0.09600  2.14600   1.000 44.79608  ? 350 GLU A C    1 
ATOM   406  O  O    . GLU A 1 31  ? 25.26600 -0.61500 1.93600   1.000 44.90227  ? 350 GLU A O    1 
ATOM   407  C  CB   . GLU A 1 31  ? 22.05300 -0.81400 1.59400   1.000 49.55700  ? 350 GLU A CB   1 
ATOM   408  C  CG   . GLU A 1 31  ? 20.83800 -0.90000 0.69500   1.000 62.06523  ? 350 GLU A CG   1 
ATOM   409  C  CD   . GLU A 1 31  ? 19.65400 -1.64200 1.29000   1.000 81.90047  ? 350 GLU A CD   1 
ATOM   410  O  OE1  . GLU A 1 31  ? 19.73700 -2.06800 2.46400   1.000 73.17642  ? 350 GLU A OE1  1 
ATOM   411  O  OE2  . GLU A 1 31  ? 18.63800 -1.79900 0.57600   1.000 73.82213  ? 350 GLU A OE2  1 
ATOM   412  H  H    . GLU A 1 31  ? 24.26400 -0.80400 -0.17000  1.000 58.18015  ? 350 GLU A H    1 
ATOM   413  H  HA   . GLU A 1 31  ? 22.78000 1.05400  1.07100   1.000 56.16003  ? 350 GLU A HA   1 
ATOM   414  H  HB2  . GLU A 1 31  ? 22.44000 -1.70000 1.67400   1.000 59.54540  ? 350 GLU A HB2  1 
ATOM   415  H  HB3  . GLU A 1 31  ? 21.76200 -0.55100 2.48100   1.000 59.54540  ? 350 GLU A HB3  1 
ATOM   416  H  HG2  . GLU A 1 31  ? 20.55700 0.00000  0.46600   1.000 74.55528  ? 350 GLU A HG2  1 
ATOM   417  H  HG3  . GLU A 1 31  ? 21.09400 -1.33700 -0.13200  1.000 74.55528  ? 350 GLU A HG3  1 
ATOM   418  N  N    . TYR A 1 32  ? 24.14600 0.82100  3.25900   1.000 42.91645  ? 351 TYR A N    1 
ATOM   419  C  CA   . TYR A 1 32  ? 25.10200 0.68900  4.34500   1.000 43.17776  ? 351 TYR A CA   1 
ATOM   420  C  C    . TYR A 1 32  ? 24.43500 1.01000  5.67800   1.000 43.23478  ? 351 TYR A C    1 
ATOM   421  O  O    . TYR A 1 32  ? 23.33900 1.56000  5.71400   1.000 40.54719  ? 351 TYR A O    1 
ATOM   422  C  CB   . TYR A 1 32  ? 26.34600 1.56400  4.10500   1.000 39.58605  ? 351 TYR A CB   1 
ATOM   423  C  CG   . TYR A 1 32  ? 26.22500 3.00100  4.55400   1.000 38.05082  ? 351 TYR A CG   1 
ATOM   424  C  CD1  . TYR A 1 32  ? 25.38100 3.88300  3.90200   1.000 38.84100  ? 351 TYR A CD1  1 
ATOM   425  C  CD2  . TYR A 1 32  ? 26.95400 3.47800  5.63900   1.000 38.97184  ? 351 TYR A CD2  1 
ATOM   426  C  CE1  . TYR A 1 32  ? 25.27400 5.20800  4.30000   1.000 37.63732  ? 351 TYR A CE1  1 
ATOM   427  C  CE2  . TYR A 1 32  ? 26.85800 4.80300  6.04400   1.000 34.75405  ? 351 TYR A CE2  1 
ATOM   428  C  CZ   . TYR A 1 32  ? 26.01900 5.66800  5.36900   1.000 35.56376  ? 351 TYR A CZ   1 
ATOM   429  O  OH   . TYR A 1 32  ? 25.88800 6.98500  5.74700   1.000 34.54804  ? 351 TYR A OH   1 
ATOM   430  H  H    . TYR A 1 32  ? 23.51200 1.38500  3.39800   1.000 51.11475  ? 351 TYR A H    1 
ATOM   431  H  HA   . TYR A 1 32  ? 25.40600 -0.23200 4.37600   1.000 51.89031  ? 351 TYR A HA   1 
ATOM   432  H  HB2  . TYR A 1 32  ? 27.10000 1.16000  4.56300   1.000 47.11828  ? 351 TYR A HB2  1 
ATOM   433  H  HB3  . TYR A 1 32  ? 26.55200 1.55400  3.15700   1.000 47.11828  ? 351 TYR A HB3  1 
ATOM   434  H  HD1  . TYR A 1 32  ? 24.87500 3.58100  3.18200   1.000 46.22421  ? 351 TYR A HD1  1 
ATOM   435  H  HD2  . TYR A 1 32  ? 27.51600 2.89900  6.10100   1.000 46.84321  ? 351 TYR A HD2  1 
ATOM   436  H  HE1  . TYR A 1 32  ? 24.70200 5.78500  3.84800   1.000 44.77979  ? 351 TYR A HE1  1 
ATOM   437  H  HE2  . TYR A 1 32  ? 27.35700 5.10700  6.76700   1.000 41.31988  ? 351 TYR A HE2  1 
ATOM   438  H  HH   . TYR A 1 32  ? 26.38800 7.13900  6.40400   1.000 41.07266  ? 351 TYR A HH   1 
ATOM   439  N  N    . GLU A 1 33  ? 25.10700 0.59900  6.75700   1.000 38.62276  ? 352 GLU A N    1 
ATOM   440  C  CA   . GLU A 1 33  ? 24.69600 0.87400  8.12000   1.000 37.81163  ? 352 GLU A CA   1 
ATOM   441  C  C    . GLU A 1 33  ? 25.27300 2.21000  8.58400   1.000 35.47883  ? 352 GLU A C    1 
ATOM   442  O  O    . GLU A 1 33  ? 26.44700 2.30900  8.91400   1.000 34.23234  ? 352 GLU A O    1 
ATOM   443  C  CB   . GLU A 1 33  ? 25.15300 -0.29000 9.00900   1.000 38.50658  ? 352 GLU A CB   1 
ATOM   444  C  CG   . GLU A 1 33  ? 24.82700 -0.11100 10.47000  1.000 44.56705  ? 352 GLU A CG   1 
ATOM   445  C  CD   . GLU A 1 33  ? 23.35600 0.07800  10.75300  1.000 50.84865  ? 352 GLU A CD   1 
ATOM   446  O  OE1  . GLU A 1 33  ? 22.58300 -0.89500 10.59200  1.000 57.92803  ? 352 GLU A OE1  1 
ATOM   447  O  OE2  . GLU A 1 33  ? 22.97300 1.21700  11.09200  1.000 43.99304  ? 352 GLU A OE2  1 
ATOM   448  H  H    . GLU A 1 33  ? 25.83300 0.14100  6.70600   1.000 45.96233  ? 352 GLU A H    1 
ATOM   449  H  HA   . GLU A 1 33  ? 23.73100 0.94800  8.17700   1.000 45.45095  ? 352 GLU A HA   1 
ATOM   450  H  HB2  . GLU A 1 33  ? 24.73900 -1.10800 8.69300   1.000 46.28489  ? 352 GLU A HB2  1 
ATOM   451  H  HB3  . GLU A 1 33  ? 26.11200 -0.40100 8.91200   1.000 46.28489  ? 352 GLU A HB3  1 
ATOM   452  H  HG2  . GLU A 1 33  ? 25.14400 -0.88600 10.96000  1.000 53.55746  ? 352 GLU A HG2  1 
ATOM   453  H  HG3  . GLU A 1 33  ? 25.31300 0.65700  10.80900  1.000 53.55746  ? 352 GLU A HG3  1 
ATOM   454  N  N    . ALA A 1 34  ? 24.42500 3.24200  8.60000   1.000 35.32828  ? 353 ALA A N    1 
ATOM   455  C  CA   . ALA A 1 34  ? 24.83300 4.58100  8.98700   1.000 33.62816  ? 353 ALA A CA   1 
ATOM   456  C  C    . ALA A 1 34  ? 24.70300 4.76800  10.49400  1.000 32.49669  ? 353 ALA A C    1 
ATOM   457  O  O    . ALA A 1 34  ? 25.38200 5.61200  11.06800  1.000 33.46068  ? 353 ALA A O    1 
ATOM   458  C  CB   . ALA A 1 34  ? 23.97400 5.61800  8.26200   1.000 34.30407  ? 353 ALA A CB   1 
ATOM   459  H  H    . ALA A 1 34  ? 23.59500 3.17800  8.38500   1.000 42.00894  ? 353 ALA A H    1 
ATOM   460  H  HA   . ALA A 1 34  ? 25.76300 4.70200  8.73800   1.000 39.96881  ? 353 ALA A HA   1 
ATOM   461  H  HB1  . ALA A 1 34  ? 24.25200 6.50900  8.52500   1.000 40.77990  ? 353 ALA A HB1  1 
ATOM   462  H  HB2  . ALA A 1 34  ? 24.08300 5.51500  7.30400   1.000 40.77990  ? 353 ALA A HB2  1 
ATOM   463  H  HB3  . ALA A 1 34  ? 23.04200 5.48800  8.49700   1.000 40.77990  ? 353 ALA A HB3  1 
ATOM   464  N  N    . TYR A 1 35  ? 23.81000 3.98100  11.10400  1.000 34.47963  ? 354 TYR A N    1 
ATOM   465  C  CA   . TYR A 1 35  ? 23.36500 4.18600  12.47500  1.000 36.22390  ? 354 TYR A CA   1 
ATOM   466  C  C    . TYR A 1 35  ? 22.71200 5.55300  12.64700  1.000 41.36673  ? 354 TYR A C    1 
ATOM   467  O  O    . TYR A 1 35  ? 22.72400 6.38500  11.74300  1.000 33.43225  ? 354 TYR A O    1 
ATOM   468  C  CB   . TYR A 1 35  ? 24.51600 4.02200  13.46300  1.000 37.01279  ? 354 TYR A CB   1 
ATOM   469  C  CG   . TYR A 1 35  ? 25.12100 2.64200  13.45700  1.000 38.87709  ? 354 TYR A CG   1 
ATOM   470  C  CD1  . TYR A 1 35  ? 24.46800 1.57100  14.05400  1.000 41.43119  ? 354 TYR A CD1  1 
ATOM   471  C  CD2  . TYR A 1 35  ? 26.34500 2.40100  12.85200  1.000 40.02939  ? 354 TYR A CD2  1 
ATOM   472  C  CE1  . TYR A 1 35  ? 25.02100 0.29700  14.04800  1.000 45.12295  ? 354 TYR A CE1  1 
ATOM   473  C  CE2  . TYR A 1 35  ? 26.90900 1.13100  12.84000  1.000 36.53804  ? 354 TYR A CE2  1 
ATOM   474  C  CZ   . TYR A 1 35  ? 26.24200 0.08000  13.43700  1.000 41.52476  ? 354 TYR A CZ   1 
ATOM   475  O  OH   . TYR A 1 35  ? 26.79100 -1.17600 13.42500  1.000 48.89277  ? 354 TYR A OH   1 
ATOM   476  H  H    . TYR A 1 35  ? 23.44300 3.30400  10.72100  1.000 41.45255  ? 354 TYR A H    1 
ATOM   477  H  HA   . TYR A 1 35  ? 22.70100 3.50500  12.66600  1.000 43.54567  ? 354 TYR A HA   1 
ATOM   478  H  HB2  . TYR A 1 35  ? 25.20600 4.67100  13.25500  1.000 44.49235  ? 354 TYR A HB2  1 
ATOM   479  H  HB3  . TYR A 1 35  ? 24.19700 4.22400  14.35700  1.000 44.49235  ? 354 TYR A HB3  1 
ATOM   480  H  HD1  . TYR A 1 35  ? 23.64500 1.71000  14.46500  1.000 49.79443  ? 354 TYR A HD1  1 
ATOM   481  H  HD2  . TYR A 1 35  ? 26.79800 3.10400  12.44600  1.000 48.11226  ? 354 TYR A HD2  1 
ATOM   482  H  HE1  . TYR A 1 35  ? 24.57100 -0.40800 14.45400  1.000 54.22454  ? 354 TYR A HE1  1 
ATOM   483  H  HE2  . TYR A 1 35  ? 27.73200 0.99000  12.43100  1.000 43.92265  ? 354 TYR A HE2  1 
ATOM   484  H  HH   . TYR A 1 35  ? 27.54000 -1.15100 13.04500  1.000 58.74832  ? 354 TYR A HH   1 
ATOM   485  N  N    . GLU A 1 36  ? 22.09900 5.75300  13.81300  1.000 32.72802  ? 355 GLU A N    1 
ATOM   486  C  CA   . GLU A 1 36  ? 21.57400 7.04800  14.21000  1.000 32.25853  ? 355 GLU A CA   1 
ATOM   487  C  C    . GLU A 1 36  ? 21.59400 7.15600  15.72800  1.000 38.20322  ? 355 GLU A C    1 
ATOM   488  O  O    . GLU A 1 36  ? 21.66100 6.13700  16.41800  1.000 37.39060  ? 355 GLU A O    1 
ATOM   489  C  CB   . GLU A 1 36  ? 20.14300 7.23300  13.73000  1.000 40.53653  ? 355 GLU A CB   1 
ATOM   490  C  CG   . GLU A 1 36  ? 19.24500 6.09200  14.13600  1.000 45.45519  ? 355 GLU A CG   1 
ATOM   491  C  CD   . GLU A 1 36  ? 17.79600 6.26700  13.75600  1.000 54.89798  ? 355 GLU A CD   1 
ATOM   492  O  OE1  . GLU A 1 36  ? 17.43400 7.34900  13.23800  1.000 54.21144  ? 355 GLU A OE1  1 
ATOM   493  O  OE2  . GLU A 1 36  ? 17.02000 5.31000  13.97800  1.000 70.77008  ? 355 GLU A OE2  1 
ATOM   494  H  H    . GLU A 1 36  ? 21.97800 5.13300  14.39700  1.000 38.88864  ? 355 GLU A H    1 
ATOM   495  H  HA   . GLU A 1 36  ? 22.13000 7.73400  13.80900  1.000 38.32525  ? 355 GLU A HA   1 
ATOM   496  H  HB2  . GLU A 1 36  ? 19.79000 8.06200  14.08900  1.000 48.72083  ? 355 GLU A HB2  1 
ATOM   497  H  HB3  . GLU A 1 36  ? 20.13800 7.31700  12.76400  1.000 48.72083  ? 355 GLU A HB3  1 
ATOM   498  H  HG2  . GLU A 1 36  ? 19.57700 5.27500  13.73100  1.000 54.62322  ? 355 GLU A HG2  1 
ATOM   499  H  HG3  . GLU A 1 36  ? 19.30300 5.97600  15.09700  1.000 54.62322  ? 355 GLU A HG3  1 
ATOM   500  N  N    . CYS A 1 37  ? 21.47900 8.39000  16.22200  1.000 39.13817  ? 356 CYS A N    1 
ATOM   501  C  CA   . CYS A 1 37  ? 21.44500 8.65500  17.65100  1.000 40.47787  ? 356 CYS A CA   1 
ATOM   502  C  C    . CYS A 1 37  ? 20.02200 9.00600  18.06400  1.000 41.58940  ? 356 CYS A C    1 
ATOM   503  O  O    . CYS A 1 37  ? 19.44500 9.96900  17.56200  1.000 39.14074  ? 356 CYS A O    1 
ATOM   504  C  CB   . CYS A 1 37  ? 22.43300 9.75800  18.00700  1.000 30.74773  ? 356 CYS A CB   1 
ATOM   505  S  SG   . CYS A 1 37  ? 24.14500 9.32800  17.64700  1.000 30.43888  ? 356 CYS A SG   1 
ATOM   506  H  H    . CYS A 1 37  ? 21.41900 9.09500  15.73300  1.000 47.04280  ? 356 CYS A H    1 
ATOM   507  H  HA   . CYS A 1 37  ? 21.71400 7.86300  18.14100  1.000 48.65044  ? 356 CYS A HA   1 
ATOM   508  H  HB2  . CYS A 1 37  ? 22.19900 10.56300 17.51900  1.000 36.97427  ? 356 CYS A HB2  1 
ATOM   509  H  HB3  . CYS A 1 37  ? 22.35000 9.96500  18.95100  1.000 36.97427  ? 356 CYS A HB3  1 
ATOM   510  N  N    . ARG A 1 38  ? 19.45300 8.18700  18.95400  1.000 36.17243  ? 357 ARG A N    1 
ATOM   511  C  CA   . ARG A 1 38  ? 18.08500 8.37100  19.39700  1.000 40.20503  ? 357 ARG A CA   1 
ATOM   512  C  C    . ARG A 1 38  ? 17.97200 8.26300  20.91500  1.000 40.06688  ? 357 ARG A C    1 
ATOM   513  O  O    . ARG A 1 38  ? 18.69300 7.50100  21.55500  1.000 37.64337  ? 357 ARG A O    1 
ATOM   514  C  CB   . ARG A 1 38  ? 17.16500 7.33500  18.74600  1.000 44.93945  ? 357 ARG A CB   1 
ATOM   515  C  CG   . ARG A 1 38  ? 17.02300 7.51100  17.23600  1.000 59.85006  ? 357 ARG A CG   1 
ATOM   516  C  CD   . ARG A 1 38  ? 15.96100 6.60600  16.63600  1.000 82.52828  ? 357 ARG A CD   1 
ATOM   517  N  NE   . ARG A 1 38  ? 14.64300 6.83600  17.21800  1.000 124.41511 ? 357 ARG A NE   1 
ATOM   518  C  CZ   . ARG A 1 38  ? 13.63900 7.45000  16.60100  1.000 91.25420  ? 357 ARG A CZ   1 
ATOM   519  N  NH1  . ARG A 1 38  ? 13.82700 8.13400  15.48400  1.000 69.89373  ? 357 ARG A NH1  1 
ATOM   520  N  NH2  . ARG A 1 38  ? 12.41900 7.38900  17.12900  1.000 87.19174  ? 357 ARG A NH2  1 
ATOM   521  H  H    . ARG A 1 38  ? 19.85400 7.51500  19.31100  1.000 43.48391  ? 357 ARG A H    1 
ATOM   522  H  HA   . ARG A 1 38  ? 17.81100 9.26200  19.12800  1.000 48.32303  ? 357 ARG A HA   1 
ATOM   523  H  HB2  . ARG A 1 38  ? 17.50900 6.44700  18.93000  1.000 54.00433  ? 357 ARG A HB2  1 
ATOM   524  H  HB3  . ARG A 1 38  ? 16.28700 7.39000  19.15500  1.000 54.00433  ? 357 ARG A HB3  1 
ATOM   525  H  HG2  . ARG A 1 38  ? 16.80200 8.43500  17.04200  1.000 71.89706  ? 357 ARG A HG2  1 
ATOM   526  H  HG3  . ARG A 1 38  ? 17.87600 7.32800  16.81100  1.000 71.89706  ? 357 ARG A HG3  1 
ATOM   527  H  HD2  . ARG A 1 38  ? 15.91900 6.75200  15.67800  1.000 99.11093  ? 357 ARG A HD2  1 
ATOM   528  H  HD3  . ARG A 1 38  ? 16.21500 5.68000  16.77100  1.000 99.11093  ? 357 ARG A HD3  1 
ATOM   529  H  HE   . ARG A 1 38  ? 14.50600 6.55400  18.01900  1.000 149.37513 ? 357 ARG A HE   1 
ATOM   530  H  HH11 . ARG A 1 38  ? 14.61400 8.18900  15.14100  1.000 83.94948  ? 357 ARG A HH11 1 
ATOM   531  H  HH12 . ARG A 1 38  ? 13.16300 8.52400  15.10100  1.000 83.94948  ? 357 ARG A HH12 1 
ATOM   532  H  HH21 . ARG A 1 38  ? 12.28800 6.95600  17.86100  1.000 104.70709 ? 357 ARG A HH21 1 
ATOM   533  H  HH22 . ARG A 1 38  ? 11.76100 7.78200  16.73900  1.000 104.70709 ? 357 ARG A HH22 1 
ATOM   534  N  N    . GLY A 1 39  ? 17.01800 9.01100  21.46300  1.000 57.10434  ? 358 GLY A N    1 
ATOM   535  C  CA   . GLY A 1 39  ? 16.71200 8.95700  22.88000  1.000 57.18846  ? 358 GLY A CA   1 
ATOM   536  C  C    . GLY A 1 39  ? 16.70700 10.35400 23.48100  1.000 58.86064  ? 358 GLY A C    1 
ATOM   537  O  O    . GLY A 1 39  ? 17.07700 11.32400 22.82100  1.000 64.94671  ? 358 GLY A O    1 
ATOM   538  H  H    . GLY A 1 39  ? 16.53100 9.56400  21.01900  1.000 68.60221  ? 358 GLY A H    1 
ATOM   539  H  HA2  . GLY A 1 39  ? 15.84700 8.53900  23.01300  1.000 68.70315  ? 358 GLY A HA2  1 
ATOM   540  H  HA3  . GLY A 1 39  ? 17.36700 8.40600  23.33600  1.000 68.70315  ? 358 GLY A HA3  1 
ATOM   541  N  N    . GLY A 1 40  ? 16.26500 10.38100 24.72700  1.000 61.63663  ? 359 GLY A N    1 
ATOM   542  C  CA   . GLY A 1 40  ? 16.11200 11.69000 25.34900  1.000 55.48652  ? 359 GLY A CA   1 
ATOM   543  C  C    . GLY A 1 40  ? 17.35800 12.19400 26.02200  1.000 45.85712  ? 359 GLY A C    1 
ATOM   544  O  O    . GLY A 1 40  ? 18.32200 11.39500 26.29600  1.000 59.80076  ? 359 GLY A O    1 
ATOM   545  H  H    . GLY A 1 40  ? 16.05800 9.69900  25.20900  1.000 74.04095  ? 359 GLY A H    1 
ATOM   546  H  HA2  . GLY A 1 40  ? 15.83900 12.33000 24.67300  1.000 66.66082  ? 359 GLY A HA2  1 
ATOM   547  H  HA3  . GLY A 1 40  ? 15.39700 11.64600 26.00300  1.000 66.66082  ? 359 GLY A HA3  1 
ATOM   548  N  N    . CYS A 1 41  ? 17.39800 13.51200 26.14700  1.000 40.93567  ? 360 CYS A N    1 
ATOM   549  C  CA   . CYS A 1 41  ? 18.46300 14.13400 26.94900  1.000 41.81465  ? 360 CYS A CA   1 
ATOM   550  C  C    . CYS A 1 41  ? 17.62800 14.75500 28.06000  1.000 48.16712  ? 360 CYS A C    1 
ATOM   551  O  O    . CYS A 1 41  ? 16.96100 15.76700 27.77200  1.000 65.94859  ? 360 CYS A O    1 
ATOM   552  C  CB   . CYS A 1 41  ? 19.24300 15.13800 26.11600  1.000 42.21567  ? 360 CYS A CB   1 
ATOM   553  S  SG   . CYS A 1 41  ? 20.20700 14.31000 24.82700  1.000 40.43455  ? 360 CYS A SG   1 
ATOM   554  H  H    . CYS A 1 41  ? 16.83800 14.05900 25.79000  1.000 49.19981  ? 360 CYS A H    1 
ATOM   555  H  HA   . CYS A 1 41  ? 19.15700 13.54400 27.28100  1.000 50.25458  ? 360 CYS A HA   1 
ATOM   556  H  HB2  . CYS A 1 41  ? 18.63000 15.77000 25.70900  1.000 50.73580  ? 360 CYS A HB2  1 
ATOM   557  H  HB3  . CYS A 1 41  ? 19.83600 15.64700 26.69000  1.000 50.73580  ? 360 CYS A HB3  1 
ATOM   558  N  N    . PHE A 1 42  ? 17.47000 14.02400 29.16300  1.000 37.23643  ? 361 PHE A N    1 
ATOM   559  C  CA   . PHE A 1 42  ? 16.64200 14.49900 30.30200  1.000 37.25594  ? 361 PHE A CA   1 
ATOM   560  C  C    . PHE A 1 42  ? 17.21600 13.88900 31.57800  1.000 41.38529  ? 361 PHE A C    1 
ATOM   561  O  O    . PHE A 1 42  ? 17.85800 12.83800 31.53700  1.000 40.25928  ? 361 PHE A O    1 
ATOM   562  C  CB   . PHE A 1 42  ? 15.14400 14.17900 30.17500  1.000 42.72789  ? 361 PHE A CB   1 
ATOM   563  C  CG   . PHE A 1 42  ? 14.75300 12.72200 30.09900  1.000 42.93023  ? 361 PHE A CG   1 
ATOM   564  C  CD1  . PHE A 1 42  ? 14.61900 12.12800 28.85700  1.000 58.01381  ? 361 PHE A CD1  1 
ATOM   565  C  CD2  . PHE A 1 42  ? 14.44500 11.96600 31.23100  1.000 53.21538  ? 361 PHE A CD2  1 
ATOM   566  C  CE1  . PHE A 1 42  ? 14.27500 10.79000 28.74300  1.000 63.94803  ? 361 PHE A CE1  1 
ATOM   567  C  CE2  . PHE A 1 42  ? 14.09900 10.62800 31.11100  1.000 57.82536  ? 361 PHE A CE2  1 
ATOM   568  C  CZ   . PHE A 1 42  ? 14.01300 10.04100 29.86800  1.000 64.51638  ? 361 PHE A CZ   1 
ATOM   569  H  H    . PHE A 1 42  ? 17.82800 13.25100 29.28200  1.000 44.29873  ? 361 PHE A H    1 
ATOM   570  H  HA   . PHE A 1 42  ? 16.68500 15.46800 30.31600  1.000 44.32214  ? 361 PHE A HA   1 
ATOM   571  H  HB2  . PHE A 1 42  ? 14.68700 14.57400 30.93400  1.000 51.35046  ? 361 PHE A HB2  1 
ATOM   572  H  HB3  . PHE A 1 42  ? 14.80800 14.62200 29.38000  1.000 51.35046  ? 361 PHE A HB3  1 
ATOM   573  H  HD1  . PHE A 1 42  ? 14.76100 12.63300 28.08900  1.000 69.69356  ? 361 PHE A HD1  1 
ATOM   574  H  HD2  . PHE A 1 42  ? 14.47200 12.36200 32.07200  1.000 63.93545  ? 361 PHE A HD2  1 
ATOM   575  H  HE1  . PHE A 1 42  ? 14.22100 10.39600 27.90200  1.000 76.81464  ? 361 PHE A HE1  1 
ATOM   576  H  HE2  . PHE A 1 42  ? 13.92400 10.12500 31.87300  1.000 69.46743  ? 361 PHE A HE2  1 
ATOM   577  H  HZ   . PHE A 1 42  ? 13.77900 9.14400  29.78900  1.000 77.49665  ? 361 PHE A HZ   1 
ATOM   578  N  N    . PHE A 1 43  ? 16.99500 14.56200 32.69000  1.000 38.05111  ? 362 PHE A N    1 
ATOM   579  C  CA   . PHE A 1 43  ? 17.49800 14.08100 33.96500  1.000 46.85792  ? 362 PHE A CA   1 
ATOM   580  C  C    . PHE A 1 43  ? 16.61900 12.96000 34.50500  1.000 48.90117  ? 362 PHE A C    1 
ATOM   581  O  O    . PHE A 1 43  ? 15.40100 12.99300 34.34800  1.000 49.88484  ? 362 PHE A O    1 
ATOM   582  C  CB   . PHE A 1 43  ? 17.58700 15.21800 34.97600  1.000 38.79844  ? 362 PHE A CB   1 
ATOM   583  C  CG   . PHE A 1 43  ? 18.57800 16.25500 34.51800  1.000 38.34636  ? 362 PHE A CG   1 
ATOM   584  C  CD1  . PHE A 1 43  ? 19.93400 15.98300 34.50900  1.000 38.15823  ? 362 PHE A CD1  1 
ATOM   585  C  CD2  . PHE A 1 43  ? 18.15000 17.47800 34.03600  1.000 34.13708  ? 362 PHE A CD2  1 
ATOM   586  C  CE1  . PHE A 1 43  ? 20.84900 16.93700 34.08000  1.000 34.36272  ? 362 PHE A CE1  1 
ATOM   587  C  CE2  . PHE A 1 43  ? 19.06700 18.42700 33.59200  1.000 39.98292  ? 362 PHE A CE2  1 
ATOM   588  C  CZ   . PHE A 1 43  ? 20.40900 18.14900 33.61400  1.000 36.67795  ? 362 PHE A CZ   1 
ATOM   589  H  H    . PHE A 1 43  ? 16.55600 15.30000 32.73100  1.000 45.37500  ? 362 PHE A H    1 
ATOM   590  H  HA   . PHE A 1 43  ? 18.39000 13.72900 33.82100  1.000 56.30650  ? 362 PHE A HA   1 
ATOM   591  H  HB2  . PHE A 1 43  ? 16.71400 15.62500 35.09000  1.000 46.27179  ? 362 PHE A HB2  1 
ATOM   592  H  HB3  . PHE A 1 43  ? 17.85300 14.86900 35.84100  1.000 46.27179  ? 362 PHE A HB3  1 
ATOM   593  H  HD1  . PHE A 1 43  ? 20.23700 15.15100 34.79400  1.000 45.86687  ? 362 PHE A HD1  1 
ATOM   594  H  HD2  . PHE A 1 43  ? 17.24000 17.66900 34.00800  1.000 41.04149  ? 362 PHE A HD2  1 
ATOM   595  H  HE1  . PHE A 1 43  ? 21.76000 16.75300 34.10900  1.000 41.31226  ? 362 PHE A HE1  1 
ATOM   596  H  HE2  . PHE A 1 43  ? 18.76900 19.25100 33.28000  1.000 48.05651  ? 362 PHE A HE2  1 
ATOM   597  H  HZ   . PHE A 1 43  ? 21.02000 18.78200 33.31300  1.000 44.09054  ? 362 PHE A HZ   1 
ATOM   598  N  N    . PRO A 1 44  ? 17.20700 11.93100 35.15300  1.000 49.58787  ? 363 PRO A N    1 
ATOM   599  C  CA   . PRO A 1 44  ? 18.65100 11.84500 35.34200  1.000 46.14084  ? 363 PRO A CA   1 
ATOM   600  C  C    . PRO A 1 44  ? 19.37800 11.29300 34.11700  1.000 48.71491  ? 363 PRO A C    1 
ATOM   601  O  O    . PRO A 1 44  ? 18.85100 10.43900 33.40700  1.000 53.08261  ? 363 PRO A O    1 
ATOM   602  C  CB   . PRO A 1 44  ? 18.75700 10.90000 36.53500  1.000 50.44233  ? 363 PRO A CB   1 
ATOM   603  C  CG   . PRO A 1 44  ? 17.59700 9.96400  36.34400  1.000 53.11901  ? 363 PRO A CG   1 
ATOM   604  C  CD   . PRO A 1 44  ? 16.48800 10.79600 35.74500  1.000 49.90036  ? 363 PRO A CD   1 
ATOM   605  H  HA   . PRO A 1 44  ? 19.06800 12.71000 35.48200  1.000 54.98402  ? 363 PRO A HA   1 
ATOM   606  H  HB2  . PRO A 1 44  ? 19.60300 10.42500 36.54000  1.000 60.14581  ? 363 PRO A HB2  1 
ATOM   607  H  HB3  . PRO A 1 44  ? 18.69500 11.37900 37.37700  1.000 60.14581  ? 363 PRO A HB3  1 
ATOM   608  H  HG2  . PRO A 1 44  ? 17.83600 9.22900  35.75700  1.000 63.81981  ? 363 PRO A HG2  1 
ATOM   609  H  HG3  . PRO A 1 44  ? 17.32200 9.57500  37.18900  1.000 63.81981  ? 363 PRO A HG3  1 
ATOM   610  H  HD2  . PRO A 1 44  ? 15.98800 10.30000 35.07800  1.000 59.95743  ? 363 PRO A HD2  1 
ATOM   611  H  HD3  . PRO A 1 44  ? 15.85300 11.08500 36.41800  1.000 59.95743  ? 363 PRO A HD3  1 
ATOM   612  N  N    . LEU A 1 45  ? 20.59700 11.78000 33.88000  1.000 56.65948  ? 364 LEU A N    1 
ATOM   613  C  CA   . LEU A 1 45  ? 21.35300 11.38600 32.70100  1.000 67.67929  ? 364 LEU A CA   1 
ATOM   614  C  C    . LEU A 1 45  ? 22.03500 10.03100 32.89000  1.000 83.41964  ? 364 LEU A C    1 
ATOM   615  O  O    . LEU A 1 45  ? 22.25100 9.59100  34.01800  1.000 72.58367  ? 364 LEU A O    1 
ATOM   616  C  CB   . LEU A 1 45  ? 22.38100 12.47200 32.37400  1.000 59.28595  ? 364 LEU A CB   1 
ATOM   617  C  CG   . LEU A 1 45  ? 21.79300 13.81700 31.91400  1.000 50.60030  ? 364 LEU A CG   1 
ATOM   618  C  CD1  . LEU A 1 45  ? 22.86000 14.83500 31.72900  1.000 45.94389  ? 364 LEU A CD1  1 
ATOM   619  C  CD2  . LEU A 1 45  ? 21.01300 13.68700 30.61700  1.000 49.62167  ? 364 LEU A CD2  1 
ATOM   620  H  H    . LEU A 1 45  ? 21.00100 12.34000 34.39300  1.000 68.06838  ? 364 LEU A H    1 
ATOM   621  H  HA   . LEU A 1 45  ? 20.73600 11.28900 31.95800  1.000 81.29215  ? 364 LEU A HA   1 
ATOM   622  H  HB2  . LEU A 1 45  ? 22.92700 12.62700 33.16000  1.000 71.22014  ? 364 LEU A HB2  1 
ATOM   623  H  HB3  . LEU A 1 45  ? 22.97100 12.13900 31.68000  1.000 71.22014  ? 364 LEU A HB3  1 
ATOM   624  H  HG   . LEU A 1 45  ? 21.18700 14.10100 32.61600  1.000 60.79735  ? 364 LEU A HG   1 
ATOM   625  H  HD11 . LEU A 1 45  ? 22.46300 15.67100 31.44000  1.000 55.20967  ? 364 LEU A HD11 1 
ATOM   626  H  HD12 . LEU A 1 45  ? 23.32600 14.97200 32.56900  1.000 55.20967  ? 364 LEU A HD12 1 
ATOM   627  H  HD13 . LEU A 1 45  ? 23.48900 14.52700 31.05800  1.000 55.20967  ? 364 LEU A HD13 1 
ATOM   628  H  HD21 . LEU A 1 45  ? 20.66000 14.55400 30.36300  1.000 59.62300  ? 364 LEU A HD21 1 
ATOM   629  H  HD22 . LEU A 1 45  ? 21.60000 13.36000 29.91800  1.000 59.62300  ? 364 LEU A HD22 1 
ATOM   630  H  HD23 . LEU A 1 45  ? 20.28000 13.06400 30.74100  1.000 59.62300  ? 364 LEU A HD23 1 
ATOM   631  N  N    . ALA A 1 46  ? 22.36700 9.38800  31.77300  1.000 96.42055  ? 365 ALA A N    1 
ATOM   632  C  CA   . ALA A 1 46  ? 23.12400 8.14900  31.79900  1.000 134.06145 ? 365 ALA A CA   1 
ATOM   633  C  C    . ALA A 1 46  ? 24.60900 8.44300  31.99700  1.000 111.48113 ? 365 ALA A C    1 
ATOM   634  O  O    . ALA A 1 46  ? 25.07000 9.58200  31.87400  1.000 105.60778 ? 365 ALA A O    1 
ATOM   635  C  CB   . ALA A 1 46  ? 22.89700 7.35400  30.51500  1.000 84.64539  ? 365 ALA A CB   1 
ATOM   636  H  H    . ALA A 1 46  ? 22.15900 9.66000  30.98400  1.000 115.78166 ? 365 ALA A H    1 
ATOM   637  H  HA   . ALA A 1 46  ? 22.81400 7.61200  32.54500  1.000 160.95074 ? 365 ALA A HA   1 
ATOM   638  H  HB1  . ALA A 1 46  ? 23.40900 6.53100  30.54900  1.000 101.65146 ? 365 ALA A HB1  1 
ATOM   639  H  HB2  . ALA A 1 46  ? 21.95400 7.14400  30.42600  1.000 101.65146 ? 365 ALA A HB2  1 
ATOM   640  H  HB3  . ALA A 1 46  ? 23.18300 7.88100  29.75300  1.000 101.65146 ? 365 ALA A HB3  1 
ATOM   641  N  N    . ASP A 1 47  ? 25.36800 7.38800  32.30200  1.000 85.21275  ? 366 ASP A N    1 
ATOM   642  C  CA   . ASP A 1 47  ? 26.77600 7.56800  32.64000  1.000 121.23496 ? 366 ASP A CA   1 
ATOM   643  C  C    . ASP A 1 47  ? 27.60900 8.01900  31.44300  1.000 136.60306 ? 366 ASP A C    1 
ATOM   644  O  O    . ASP A 1 47  ? 28.60200 8.73300  31.62400  1.000 112.04680 ? 366 ASP A O    1 
ATOM   645  C  CB   . ASP A 1 47  ? 27.35300 6.27100  33.21900  1.000 81.03490  ? 366 ASP A CB   1 
ATOM   646  C  CG   . ASP A 1 47  ? 26.85800 5.97400  34.63200  1.000 146.80722 ? 366 ASP A CG   1 
ATOM   647  O  OD1  . ASP A 1 47  ? 26.28000 6.87700  35.26800  1.000 161.78436 ? 366 ASP A OD1  1 
ATOM   648  O  OD2  . ASP A 1 47  ? 27.05300 4.82200  35.07100  1.000 163.11389 ? 366 ASP A OD2  1 
ATOM   649  H  H    . ASP A 1 47  ? 25.09000 6.57400  32.31800  1.000 102.33229 ? 366 ASP A H    1 
ATOM   650  H  HA   . ASP A 1 47  ? 26.82100 8.27200  33.30600  1.000 145.55895 ? 366 ASP A HA   1 
ATOM   651  H  HB2  . ASP A 1 47  ? 27.11800 5.53100  32.63800  1.000 97.31888  ? 366 ASP A HB2  1 
ATOM   652  H  HB3  . ASP A 1 47  ? 28.32100 6.32900  33.22700  1.000 97.31888  ? 366 ASP A HB3  1 
ATOM   653  N  N    . ASP A 1 48  ? 27.23300 7.63200  30.22300  1.000 81.74732  ? 367 ASP A N    1 
ATOM   654  C  CA   . ASP A 1 48  ? 28.10100 7.79500  29.06000  1.000 102.30101 ? 367 ASP A CA   1 
ATOM   655  C  C    . ASP A 1 48  ? 27.44300 8.58100  27.92900  1.000 134.11708 ? 367 ASP A C    1 
ATOM   656  O  O    . ASP A 1 48  ? 27.69600 8.31700  26.75300  1.000 75.10813  ? 367 ASP A O    1 
ATOM   657  C  CB   . ASP A 1 48  ? 28.56200 6.43800  28.53400  1.000 118.47718 ? 367 ASP A CB   1 
ATOM   658  C  CG   . ASP A 1 48  ? 27.40900 5.58500  28.03500  1.000 131.77922 ? 367 ASP A CG   1 
ATOM   659  O  OD1  . ASP A 1 48  ? 26.25100 5.99700  28.24900  1.000 109.02110 ? 367 ASP A OD1  1 
ATOM   660  O  OD2  . ASP A 1 48  ? 27.67300 4.50200  27.47800  1.000 168.17861 ? 367 ASP A OD2  1 
ATOM   661  H  H    . ASP A 1 48  ? 26.47200 7.27000  30.04900  1.000 98.17379  ? 367 ASP A H    1 
ATOM   662  H  HA   . ASP A 1 48  ? 28.86500 8.30800  29.36500  1.000 122.83821 ? 367 ASP A HA   1 
ATOM   663  H  HB2  . ASP A 1 48  ? 29.19600 6.57300  27.81300  1.000 142.24961 ? 367 ASP A HB2  1 
ATOM   664  H  HB3  . ASP A 1 48  ? 29.03000 5.96300  29.23900  1.000 142.24961 ? 367 ASP A HB3  1 
ATOM   665  N  N    . VAL A 1 49  ? 26.58800 9.55400  28.24400  1.000 84.89727  ? 368 VAL A N    1 
ATOM   666  C  CA   . VAL A 1 49  ? 26.13600 10.48500 27.21500  1.000 73.06660  ? 368 VAL A CA   1 
ATOM   667  C  C    . VAL A 1 49  ? 27.05100 11.70000 27.12600  1.000 127.88322 ? 368 VAL A C    1 
ATOM   668  O  O    . VAL A 1 49  ? 26.75000 12.64600 26.38900  1.000 58.48492  ? 368 VAL A O    1 
ATOM   669  C  CB   . VAL A 1 49  ? 24.66100 10.88600 27.41000  1.000 97.41411  ? 368 VAL A CB   1 
ATOM   670  C  CG1  . VAL A 1 49  ? 23.79500 9.64000  27.37400  1.000 74.46320  ? 368 VAL A CG1  1 
ATOM   671  C  CG2  . VAL A 1 49  ? 24.44200 11.68000 28.70000  1.000 60.59252  ? 368 VAL A CG2  1 
ATOM   672  H  H    . VAL A 1 49  ? 26.26500 9.69000  29.02900  1.000 101.95372 ? 368 VAL A H    1 
ATOM   673  H  HA   . VAL A 1 49  ? 26.18800 10.02300 26.36400  1.000 87.75691  ? 368 VAL A HA   1 
ATOM   674  H  HB   . VAL A 1 49  ? 24.40600 11.47600 26.68400  1.000 116.97393 ? 368 VAL A HB   1 
ATOM   675  H  HG11 . VAL A 1 49  ? 22.86500 9.88800  27.49600  1.000 89.43283  ? 368 VAL A HG11 1 
ATOM   676  H  HG12 . VAL A 1 49  ? 23.90100 9.19700  26.51800  1.000 89.43283  ? 368 VAL A HG12 1 
ATOM   677  H  HG13 . VAL A 1 49  ? 24.06500 9.03800  28.08500  1.000 89.43283  ? 368 VAL A HG13 1 
ATOM   678  H  HG21 . VAL A 1 49  ? 23.50400 11.91100 28.78300  1.000 72.78803  ? 368 VAL A HG21 1 
ATOM   679  H  HG22 . VAL A 1 49  ? 24.71000 11.14200 29.46100  1.000 72.78803  ? 368 VAL A HG22 1 
ATOM   680  H  HG23 . VAL A 1 49  ? 24.97300 12.49100 28.67500  1.000 72.78803  ? 368 VAL A HG23 1 
ATOM   681  N  N    . THR A 1 50  ? 28.17600 11.67500 27.84800  1.000 52.88679  ? 369 THR A N    1 
ATOM   682  C  CA   . THR A 1 50  ? 29.25100 12.66500 27.80600  1.000 57.68246  ? 369 THR A CA   1 
ATOM   683  C  C    . THR A 1 50  ? 28.70800 14.09300 27.67000  1.000 47.75303  ? 369 THR A C    1 
ATOM   684  O  O    . THR A 1 50  ? 29.08900 14.81600 26.74400  1.000 54.27322  ? 369 THR A O    1 
ATOM   685  C  CB   . THR A 1 50  ? 30.23600 12.35200 26.68600  1.000 144.13694 ? 369 THR A CB   1 
ATOM   686  O  OG1  . THR A 1 50  ? 29.58600 12.55400 25.42900  1.000 65.15436  ? 369 THR A OG1  1 
ATOM   687  C  CG2  . THR A 1 50  ? 30.72300 10.89900 26.77900  1.000 98.86015  ? 369 THR A CG2  1 
ATOM   688  H  H    . THR A 1 50  ? 28.33900 11.04200 28.40700  1.000 63.54115  ? 369 THR A H    1 
ATOM   689  H  HA   . THR A 1 50  ? 29.72300 12.61300 28.65200  1.000 69.29595  ? 369 THR A HA   1 
ATOM   690  H  HB   . THR A 1 50  ? 31.00400 12.93900 26.76800  1.000 173.04133 ? 369 THR A HB   1 
ATOM   691  H  HG1  . THR A 1 50  ? 28.99900 13.14900 25.50900  1.000 78.26223  ? 369 THR A HG1  1 
ATOM   692  H  HG21 . THR A 1 50  ? 31.34800 10.72000 26.05900  1.000 118.70918 ? 369 THR A HG21 1 
ATOM   693  H  HG22 . THR A 1 50  ? 31.16400 10.75900 27.63100  1.000 118.70918 ? 369 THR A HG22 1 
ATOM   694  H  HG23 . THR A 1 50  ? 29.96500 10.29800 26.70600  1.000 118.70918 ? 369 THR A HG23 1 
ATOM   695  N  N    . PRO A 1 51  ? 27.82400 14.52200 28.57100  1.000 52.72656  ? 370 PRO A N    1 
ATOM   696  C  CA   . PRO A 1 51  ? 27.13200 15.79700 28.35300  1.000 41.25906  ? 370 PRO A CA   1 
ATOM   697  C  C    . PRO A 1 51  ? 28.05200 16.98000 28.62400  1.000 34.31748  ? 370 PRO A C    1 
ATOM   698  O  O    . PRO A 1 51  ? 28.70500 17.05500 29.66800  1.000 45.04310  ? 370 PRO A O    1 
ATOM   699  C  CB   . PRO A 1 51  ? 25.97300 15.74600 29.35400  1.000 38.62554  ? 370 PRO A CB   1 
ATOM   700  C  CG   . PRO A 1 51  ? 26.49500 14.91900 30.47000  1.000 44.13598  ? 370 PRO A CG   1 
ATOM   701  C  CD   . PRO A 1 51  ? 27.44200 13.90700 29.85700  1.000 44.66485  ? 370 PRO A CD   1 
ATOM   702  H  HA   . PRO A 1 51  ? 26.83400 15.91400 27.43800  1.000 49.58787  ? 370 PRO A HA   1 
ATOM   703  H  HB2  . PRO A 1 51  ? 25.72600 16.63400 29.65600  1.000 46.42765  ? 370 PRO A HB2  1 
ATOM   704  H  HB3  . PRO A 1 51  ? 25.18000 15.35000 28.95900  1.000 46.42765  ? 370 PRO A HB3  1 
ATOM   705  H  HG2  . PRO A 1 51  ? 26.95500 15.47100 31.12100  1.000 53.04018  ? 370 PRO A HG2  1 
ATOM   706  H  HG3  . PRO A 1 51  ? 25.77100 14.47400 30.93700  1.000 53.04018  ? 370 PRO A HG3  1 
ATOM   707  H  HD2  . PRO A 1 51  ? 28.21500 13.75400 30.42300  1.000 53.67482  ? 370 PRO A HD2  1 
ATOM   708  H  HD3  . PRO A 1 51  ? 27.01100 13.04800 29.72700  1.000 53.67482  ? 370 PRO A HD3  1 
ATOM   709  N  N    . THR A 1 52  ? 28.11000 17.89700 27.66300  1.000 41.76970  ? 371 THR A N    1 
ATOM   710  C  CA   . THR A 1 52  ? 28.73400 19.18800 27.89700  1.000 36.93854  ? 371 THR A CA   1 
ATOM   711  C  C    . THR A 1 52  ? 27.97400 19.93700 28.99300  1.000 30.43945  ? 371 THR A C    1 
ATOM   712  O  O    . THR A 1 52  ? 26.81800 19.63500 29.30200  1.000 29.95103  ? 371 THR A O    1 
ATOM   713  C  CB   . THR A 1 52  ? 28.73700 20.02400 26.61600  1.000 34.71243  ? 371 THR A CB   1 
ATOM   714  O  OG1  . THR A 1 52  ? 27.38300 20.22100 26.20300  1.000 30.29030  ? 371 THR A OG1  1 
ATOM   715  C  CG2  . THR A 1 52  ? 29.52900 19.34500 25.46600  1.000 33.97213  ? 371 THR A CG2  1 
ATOM   716  H  H    . THR A 1 52  ? 27.79400 17.78900 26.87100  1.000 50.20063  ? 371 THR A H    1 
ATOM   717  H  HA   . THR A 1 52  ? 29.65100 19.04200 28.17700  1.000 44.40325  ? 371 THR A HA   1 
ATOM   718  H  HB   . THR A 1 52  ? 29.17500 20.86800 26.80800  1.000 41.73192  ? 371 THR A HB   1 
ATOM   719  H  HG1  . THR A 1 52  ? 27.37100 20.55500 25.43200  1.000 36.42536  ? 371 THR A HG1  1 
ATOM   720  H  HG21 . THR A 1 52  ? 29.50300 19.91000 24.67800  1.000 40.84355  ? 371 THR A HG21 1 
ATOM   721  H  HG22 . THR A 1 52  ? 30.45000 19.21500 25.74000  1.000 40.84355  ? 371 THR A HG22 1 
ATOM   722  H  HG23 . THR A 1 52  ? 29.12900 18.48500 25.26100  1.000 40.84355  ? 371 THR A HG23 1 
ATOM   723  N  N    . LYS A 1 53  ? 28.64100 20.93000 29.58700  1.000 36.35379  ? 372 LYS A N    1 
ATOM   724  C  CA   . LYS A 1 53  ? 27.97900 21.77900 30.55600  1.000 35.39073  ? 372 LYS A CA   1 
ATOM   725  C  C    . LYS A 1 53  ? 26.82800 22.55300 29.91200  1.000 29.97466  ? 372 LYS A C    1 
ATOM   726  O  O    . LYS A 1 53  ? 25.79000 22.74800 30.53600  1.000 31.05567  ? 372 LYS A O    1 
ATOM   727  C  CB   . LYS A 1 53  ? 28.98000 22.73700 31.22500  1.000 35.41980  ? 372 LYS A CB   1 
ATOM   728  C  CG   . LYS A 1 53  ? 30.07700 22.03700 32.05100  1.000 39.72174  ? 372 LYS A CG   1 
ATOM   729  C  CD   . LYS A 1 53  ? 30.86300 22.99500 32.94400  1.000 40.73017  ? 372 LYS A CD   1 
ATOM   730  C  CE   . LYS A 1 53  ? 32.19700 22.43900 33.45300  1.000 48.12879  ? 372 LYS A CE   1 
ATOM   731  N  NZ   . LYS A 1 53  ? 33.25500 22.36400 32.40400  1.000 44.69136  ? 372 LYS A NZ   1 
ATOM   732  H  H    . LYS A 1 53  ? 29.46700 21.12100 29.44000  1.000 43.70154  ? 372 LYS A H    1 
ATOM   733  H  HA   . LYS A 1 53  ? 27.60600 21.20800 31.24600  1.000 42.54587  ? 372 LYS A HA   1 
ATOM   734  H  HB2  . LYS A 1 53  ? 29.40200 23.27700 30.53900  1.000 42.58076  ? 372 LYS A HB2  1 
ATOM   735  H  HB3  . LYS A 1 53  ? 28.49300 23.34400 31.80400  1.000 42.58076  ? 372 LYS A HB3  1 
ATOM   736  H  HG2  . LYS A 1 53  ? 29.67000 21.35100 32.60300  1.000 47.74309  ? 372 LYS A HG2  1 
ATOM   737  H  HG3  . LYS A 1 53  ? 30.69100 21.58900 31.44800  1.000 47.74309  ? 372 LYS A HG3  1 
ATOM   738  H  HD2  . LYS A 1 53  ? 31.03300 23.81300 32.45100  1.000 48.95320  ? 372 LYS A HD2  1 
ATOM   739  H  HD3  . LYS A 1 53  ? 30.31300 23.23300 33.70700  1.000 48.95320  ? 372 LYS A HD3  1 
ATOM   740  H  HE2  . LYS A 1 53  ? 32.51400 22.99600 34.18100  1.000 57.83155  ? 372 LYS A HE2  1 
ATOM   741  H  HE3  . LYS A 1 53  ? 32.05100 21.55200 33.81700  1.000 57.83155  ? 372 LYS A HE3  1 
ATOM   742  H  HZ1  . LYS A 1 53  ? 33.90600 21.82200 32.67700  1.000 53.70662  ? 372 LYS A HZ1  1 
ATOM   743  H  HZ2  . LYS A 1 53  ? 32.90300 22.04900 31.64900  1.000 53.70662  ? 372 LYS A HZ2  1 
ATOM   744  H  HZ3  . LYS A 1 53  ? 33.58800 23.17700 32.25900  1.000 53.70662  ? 372 LYS A HZ3  1 
ATOM   745  N  N    . HIS A 1 54  ? 26.99800 22.99400 28.65800  1.000 28.59241  ? 373 HIS A N    1 
ATOM   746  C  CA   . HIS A 1 54  ? 25.93000 23.72500 27.98700  1.000 27.51260  ? 373 HIS A CA   1 
ATOM   747  C  C    . HIS A 1 54  ? 24.67100 22.87000 27.84000  1.000 26.96022  ? 373 HIS A C    1 
ATOM   748  O  O    . HIS A 1 54  ? 23.57500 23.33000 28.13600  1.000 27.86008  ? 373 HIS A O    1 
ATOM   749  C  CB   . HIS A 1 54  ? 26.36600 24.28900 26.62100  1.000 27.63249  ? 373 HIS A CB   1 
ATOM   750  C  CG   . HIS A 1 54  ? 25.38400 25.29700 26.10500  1.000 27.02471  ? 373 HIS A CG   1 
ATOM   751  N  ND1  . HIS A 1 54  ? 24.19800 24.91000 25.49700  1.000 29.06360  ? 373 HIS A ND1  1 
ATOM   752  C  CD2  . HIS A 1 54  ? 25.42100 26.64500 26.16600  1.000 27.71140  ? 373 HIS A CD2  1 
ATOM   753  C  CE1  . HIS A 1 54  ? 23.54900 26.03200 25.22300  1.000 26.54243  ? 373 HIS A CE1  1 
ATOM   754  N  NE2  . HIS A 1 54  ? 24.25700 27.10200 25.60700  1.000 26.83775  ? 373 HIS A NE2  1 
ATOM   755  H  H    . HIS A 1 54  ? 27.71100 22.88000 28.19100  1.000 33.92591  ? 373 HIS A H    1 
ATOM   756  H  HA   . HIS A 1 54  ? 25.72100 24.48200 28.55600  1.000 32.63013  ? 373 HIS A HA   1 
ATOM   757  H  HB2  . HIS A 1 54  ? 27.24100 24.70000 26.70400  1.000 32.77401  ? 373 HIS A HB2  1 
ATOM   758  H  HB3  . HIS A 1 54  ? 26.45300 23.56400 25.98300  1.000 32.77401  ? 373 HIS A HB3  1 
ATOM   759  H  HD1  . HIS A 1 54  ? 23.93800 24.10700 25.33200  1.000 34.95332  ? 373 HIS A HD1  1 
ATOM   760  H  HD2  . HIS A 1 54  ? 26.10600 27.16400 26.52000  1.000 33.33068  ? 373 HIS A HD2  1 
ATOM   761  H  HE1  . HIS A 1 54  ? 22.71300 26.07100 24.81800  1.000 31.46593  ? 373 HIS A HE1  1 
ATOM   762  N  N    . ALA A 1 55  ? 24.83200 21.60900 27.42900  1.000 27.42761  ? 374 ALA A N    1 
ATOM   763  C  CA   . ALA A 1 55  ? 23.70400 20.68500 27.33900  1.000 27.39494  ? 374 ALA A CA   1 
ATOM   764  C  C    . ALA A 1 55  ? 22.96600 20.49400 28.66800  1.000 27.34607  ? 374 ALA A C    1 
ATOM   765  O  O    . ALA A 1 55  ? 21.73900 20.40400 28.71200  1.000 27.20109  ? 374 ALA A O    1 
ATOM   766  C  CB   . ALA A 1 55  ? 24.19200 19.34700 26.82400  1.000 28.36153  ? 374 ALA A CB   1 
ATOM   767  H  H    . ALA A 1 55  ? 25.58800 21.27100 27.19800  1.000 32.52814  ? 374 ALA A H    1 
ATOM   768  H  HA   . ALA A 1 55  ? 23.06400 21.07700 26.72400  1.000 32.48894  ? 374 ALA A HA   1 
ATOM   769  H  HB1  . ALA A 1 55  ? 23.44500 18.73100 26.76300  1.000 33.99503  ? 374 ALA A HB1  1 
ATOM   770  H  HB2  . ALA A 1 55  ? 24.58700 19.46300 25.94600  1.000 33.99503  ? 374 ALA A HB2  1 
ATOM   771  H  HB3  . ALA A 1 55  ? 24.85700 18.98900 27.43300  1.000 33.99503  ? 374 ALA A HB3  1 
ATOM   772  N  N    . ILE A 1 56  ? 23.72600 20.45000 29.76600  1.000 27.80777  ? 375 ILE A N    1 
ATOM   773  C  CA   . ILE A 1 56  ? 23.14600 20.32900 31.09300  1.000 28.05594  ? 375 ILE A CA   1 
ATOM   774  C  C    . ILE A 1 56  ? 22.35200 21.58300 31.44900  1.000 27.36221  ? 375 ILE A C    1 
ATOM   775  O  O    . ILE A 1 56  ? 21.19700 21.49800 31.86100  1.000 27.35475  ? 375 ILE A O    1 
ATOM   776  C  CB   . ILE A 1 56  ? 24.27700 20.00800 32.11200  1.000 29.20106  ? 375 ILE A CB   1 
ATOM   777  C  CG1  . ILE A 1 56  ? 24.86400 18.60900 31.81800  1.000 39.55248  ? 375 ILE A CG1  1 
ATOM   778  C  CG2  . ILE A 1 56  ? 23.79900 20.11300 33.52100  1.000 29.68819  ? 375 ILE A CG2  1 
ATOM   779  C  CD1  . ILE A 1 56  ? 26.14500 18.28000 32.55400  1.000 34.52652  ? 375 ILE A CD1  1 
ATOM   780  H  H    . ILE A 1 56  ? 24.58500 20.49000 29.75700  1.000 33.31560  ? 375 ILE A H    1 
ATOM   781  H  HA   . ILE A 1 56  ? 22.51100 19.59600 31.11900  1.000 33.28214  ? 375 ILE A HA   1 
ATOM   782  H  HB   . ILE A 1 56  ? 24.97900 20.66900 32.00700  1.000 34.93293  ? 375 ILE A HB   1 
ATOM   783  H  HG12 . ILE A 1 56  ? 24.19800 17.94100 32.04300  1.000 47.53998  ? 375 ILE A HG12 1 
ATOM   784  H  HG13 . ILE A 1 56  ? 25.02800 18.53700 30.86500  1.000 47.53998  ? 375 ILE A HG13 1 
ATOM   785  H  HG21 . ILE A 1 56  ? 24.52800 19.90700 34.12700  1.000 35.24084  ? 375 ILE A HG21 1 
ATOM   786  H  HG22 . ILE A 1 56  ? 23.48400 21.01500 33.69000  1.000 35.24084  ? 375 ILE A HG22 1 
ATOM   787  H  HG23 . ILE A 1 56  ? 23.07300 19.48600 33.66400  1.000 35.24084  ? 375 ILE A HG23 1 
ATOM   788  H  HD11 . ILE A 1 56  ? 26.43900 17.38800 32.31000  1.000 41.50882  ? 375 ILE A HD11 1 
ATOM   789  H  HD12 . ILE A 1 56  ? 26.83100 18.92300 32.31400  1.000 41.50882  ? 375 ILE A HD12 1 
ATOM   790  H  HD13 . ILE A 1 56  ? 25.98800 18.31800 33.51000  1.000 41.50882  ? 375 ILE A HD13 1 
ATOM   791  N  N    . VAL A 1 57  ? 22.98200 22.75000 31.28200  1.000 28.11616  ? 376 VAL A N    1 
ATOM   792  C  CA   . VAL A 1 57  ? 22.33400 24.02300 31.56000  1.000 33.49601  ? 376 VAL A CA   1 
ATOM   793  C  C    . VAL A 1 57  ? 21.07200 24.22900 30.72600  1.000 35.06583  ? 376 VAL A C    1 
ATOM   794  O  O    . VAL A 1 57  ? 20.03200 24.62700 31.23800  1.000 27.49182  ? 376 VAL A O    1 
ATOM   795  C  CB   . VAL A 1 57  ? 23.33600 25.16200 31.34000  1.000 38.66243  ? 376 VAL A CB   1 
ATOM   796  C  CG1  . VAL A 1 57  ? 22.64100 26.50600 31.19300  1.000 36.63826  ? 376 VAL A CG1  1 
ATOM   797  C  CG2  . VAL A 1 57  ? 24.35500 25.18800 32.46400  1.000 32.74459  ? 376 VAL A CG2  1 
ATOM   798  H  H    . VAL A 1 57  ? 23.79300 22.82000 31.00500  1.000 33.81639  ? 376 VAL A H    1 
ATOM   799  H  HA   . VAL A 1 57  ? 22.04800 24.02000 32.48700  1.000 40.27220  ? 376 VAL A HA   1 
ATOM   800  H  HB   . VAL A 1 57  ? 23.80100 24.99400 30.50600  1.000 46.47192  ? 376 VAL A HB   1 
ATOM   801  H  HG11 . VAL A 1 57  ? 23.30400 27.20000 31.05600  1.000 44.04290  ? 376 VAL A HG11 1 
ATOM   802  H  HG12 . VAL A 1 57  ? 22.04000 26.47800 30.43200  1.000 44.04290  ? 376 VAL A HG12 1 
ATOM   803  H  HG13 . VAL A 1 57  ? 22.13400 26.69800 31.99700  1.000 44.04290  ? 376 VAL A HG13 1 
ATOM   804  H  HG21 . VAL A 1 57  ? 24.98300 25.91200 32.31500  1.000 39.37051  ? 376 VAL A HG21 1 
ATOM   805  H  HG22 . VAL A 1 57  ? 23.90000 25.32400 33.31000  1.000 39.37051  ? 376 VAL A HG22 1 
ATOM   806  H  HG23 . VAL A 1 57  ? 24.83400 24.34500 32.48700  1.000 39.37051  ? 376 VAL A HG23 1 
ATOM   807  N  N    . GLN A 1 58  ? 21.16700 23.94800 29.42600  1.000 26.78843  ? 377 GLN A N    1 
ATOM   808  C  CA   . GLN A 1 58  ? 20.01900 24.12500 28.55800  1.000 26.82788  ? 377 GLN A CA   1 
ATOM   809  C  C    . GLN A 1 58  ? 18.86900 23.20000 28.94600  1.000 27.28705  ? 377 GLN A C    1 
ATOM   810  O  O    . GLN A 1 58  ? 17.71400 23.61500 28.96300  1.000 32.34403  ? 377 GLN A O    1 
ATOM   811  C  CB   . GLN A 1 58  ? 20.42800 23.92300 27.08300  1.000 27.82508  ? 377 GLN A CB   1 
ATOM   812  C  CG   . GLN A 1 58  ? 19.27100 24.25000 26.17500  1.000 27.72003  ? 377 GLN A CG   1 
ATOM   813  C  CD   . GLN A 1 58  ? 19.64800 24.38700 24.74200  1.000 31.67266  ? 377 GLN A CD   1 
ATOM   814  O  OE1  . GLN A 1 58  ? 20.76600 24.74800 24.40700  1.000 27.47729  ? 377 GLN A OE1  1 
ATOM   815  N  NE2  . GLN A 1 58  ? 18.68400 24.10400 23.88100  1.000 28.86162  ? 377 GLN A NE2  1 
ATOM   816  H  H    . GLN A 1 58  ? 21.87800 23.65900 29.03800  1.000 32.22311  ? 377 GLN A H    1 
ATOM   817  H  HA   . GLN A 1 58  ? 19.69800 25.03400 28.66600  1.000 32.27045  ? 377 GLN A HA   1 
ATOM   818  H  HB2  . GLN A 1 58  ? 21.18600 24.49000 26.87000  1.000 33.46709  ? 377 GLN A HB2  1 
ATOM   819  H  HB3  . GLN A 1 58  ? 20.71100 23.00600 26.94100  1.000 33.46709  ? 377 GLN A HB3  1 
ATOM   820  H  HG2  . GLN A 1 58  ? 18.60000 23.55500 26.25800  1.000 33.34103  ? 377 GLN A HG2  1 
ATOM   821  H  HG3  . GLN A 1 58  ? 18.86100 25.07700 26.47300  1.000 33.34103  ? 377 GLN A HG3  1 
ATOM   822  H  HE21 . GLN A 1 58  ? 17.91200 23.85300 24.16600  1.000 34.71094  ? 377 GLN A HE21 1 
ATOM   823  H  HE22 . GLN A 1 58  ? 18.82900 24.17100 23.03600  1.000 34.71094  ? 377 GLN A HE22 1 
ATOM   824  N  N    . THR A 1 59  ? 19.18800 21.95100 29.29400  1.000 27.43713  ? 378 THR A N    1 
ATOM   825  C  CA   . THR A 1 59  ? 18.17700 21.00700 29.74600  1.000 29.18286  ? 378 THR A CA   1 
ATOM   826  C  C    . THR A 1 59  ? 17.44500 21.49400 30.99600  1.000 30.81632  ? 378 THR A C    1 
ATOM   827  O  O    . THR A 1 59  ? 16.22600 21.35300 31.09600  1.000 29.25815  ? 378 THR A O    1 
ATOM   828  C  CB   . THR A 1 59  ? 18.81300 19.63700 29.95300  1.000 30.53925  ? 378 THR A CB   1 
ATOM   829  O  OG1  . THR A 1 59  ? 19.47000 19.25300 28.73300  1.000 31.86402  ? 378 THR A OG1  1 
ATOM   830  C  CG2  . THR A 1 59  ? 17.78500 18.56900 30.37100  1.000 34.03762  ? 378 THR A CG2  1 
ATOM   831  H  H    . THR A 1 59  ? 19.98700 21.63500 29.27400  1.000 33.00155  ? 378 THR A H    1 
ATOM   832  H  HA   . THR A 1 59  ? 17.49900 20.93300 29.05700  1.000 35.09643  ? 378 THR A HA   1 
ATOM   833  H  HB   . THR A 1 59  ? 19.45300 19.70000 30.67900  1.000 36.72410  ? 378 THR A HB   1 
ATOM   834  H  HG1  . THR A 1 59  ? 20.30200 19.28800 28.84000  1.000 38.31382  ? 378 THR A HG1  1 
ATOM   835  H  HG21 . THR A 1 59  ? 18.23300 17.71700 30.49100  1.000 40.92214  ? 378 THR A HG21 1 
ATOM   836  H  HG22 . THR A 1 59  ? 17.36500 18.83300 31.20500  1.000 40.92214  ? 378 THR A HG22 1 
ATOM   837  H  HG23 . THR A 1 59  ? 17.10800 18.48300 29.68100  1.000 40.92214  ? 378 THR A HG23 1 
ATOM   838  N  N    . LEU A 1 60  ? 18.19300 22.07700 31.94100  1.000 30.22075  ? 379 LEU A N    1 
ATOM   839  C  CA   . LEU A 1 60  ? 17.59900 22.65600 33.13600  1.000 36.09757  ? 379 LEU A CA   1 
ATOM   840  C  C    . LEU A 1 60  ? 16.74000 23.87800 32.82000  1.000 35.67172  ? 379 LEU A C    1 
ATOM   841  O  O    . LEU A 1 60  ? 15.66700 24.04900 33.38900  1.000 31.59946  ? 379 LEU A O    1 
ATOM   842  C  CB   . LEU A 1 60  ? 18.70300 23.04300 34.13500  1.000 30.73024  ? 379 LEU A CB   1 
ATOM   843  C  CG   . LEU A 1 60  ? 19.45800 21.86200 34.76900  1.000 32.73547  ? 379 LEU A CG   1 
ATOM   844  C  CD1  . LEU A 1 60  ? 20.65800 22.34700 35.57200  1.000 37.81376  ? 379 LEU A CD1  1 
ATOM   845  C  CD2  . LEU A 1 60  ? 18.54700 21.05000 35.65200  1.000 32.33849  ? 379 LEU A CD2  1 
ATOM   846  H  H    . LEU A 1 60  ? 19.04900 22.14400 31.90200  1.000 36.34189  ? 379 LEU A H    1 
ATOM   847  H  HA   . LEU A 1 60  ? 17.01900 21.98300 33.52600  1.000 43.39409  ? 379 LEU A HA   1 
ATOM   848  H  HB2  . LEU A 1 60  ? 19.34400 23.61200 33.68100  1.000 36.95328  ? 379 LEU A HB2  1 
ATOM   849  H  HB3  . LEU A 1 60  ? 18.30600 23.57200 34.84400  1.000 36.95328  ? 379 LEU A HB3  1 
ATOM   850  H  HG   . LEU A 1 60  ? 19.77500 21.29800 34.04600  1.000 39.35956  ? 379 LEU A HG   1 
ATOM   851  H  HD11 . LEU A 1 60  ? 21.11600 21.58600 35.96100  1.000 45.45351  ? 379 LEU A HD11 1 
ATOM   852  H  HD12 . LEU A 1 60  ? 21.26600 22.82600 34.98800  1.000 45.45351  ? 379 LEU A HD12 1 
ATOM   853  H  HD13 . LEU A 1 60  ? 20.35700 22.93800 36.27900  1.000 45.45351  ? 379 LEU A HD13 1 
ATOM   854  H  HD21 . LEU A 1 60  ? 19.04400 20.31300 36.04000  1.000 38.88318  ? 379 LEU A HD21 1 
ATOM   855  H  HD22 . LEU A 1 60  ? 18.19800 21.61200 36.36100  1.000 38.88318  ? 379 LEU A HD22 1 
ATOM   856  H  HD23 . LEU A 1 60  ? 17.81100 20.70100 35.12500  1.000 38.88318  ? 379 LEU A HD23 1 
ATOM   857  N  N    . VAL A 1 61  ? 17.21000 24.72600 31.89900  1.000 29.13889  ? 380 VAL A N    1 
ATOM   858  C  CA   . VAL A 1 61  ? 16.43200 25.88200 31.48700  1.000 30.28902  ? 380 VAL A CA   1 
ATOM   859  C  C    . VAL A 1 61  ? 15.14600 25.44300 30.79000  1.000 40.27770  ? 380 VAL A C    1 
ATOM   860  O  O    . VAL A 1 61  ? 14.08600 26.01800 31.03000  1.000 34.13619  ? 380 VAL A O    1 
ATOM   861  C  CB   . VAL A 1 61  ? 17.25300 26.83800 30.58500  1.000 30.72496  ? 380 VAL A CB   1 
ATOM   862  C  CG1  . VAL A 1 61  ? 16.37800 27.96900 30.05600  1.000 30.42929  ? 380 VAL A CG1  1 
ATOM   863  C  CG2  . VAL A 1 61  ? 18.45300 27.38700 31.32400  1.000 33.93744  ? 380 VAL A CG2  1 
ATOM   864  H  H    . VAL A 1 61  ? 17.97100 24.64500 31.50800  1.000 35.04367  ? 380 VAL A H    1 
ATOM   865  H  HA   . VAL A 1 61  ? 16.19500 26.37600 32.28700  1.000 36.42382  ? 380 VAL A HA   1 
ATOM   866  H  HB   . VAL A 1 61  ? 17.57800 26.32700 29.82700  1.000 36.94695  ? 380 VAL A HB   1 
ATOM   867  H  HG11 . VAL A 1 61  ? 16.91000 28.55500 29.49500  1.000 36.59214  ? 380 VAL A HG11 1 
ATOM   868  H  HG12 . VAL A 1 61  ? 15.64900 27.59800 29.53500  1.000 36.59214  ? 380 VAL A HG12 1 
ATOM   869  H  HG13 . VAL A 1 61  ? 16.01800 28.47500 30.80100  1.000 36.59214  ? 380 VAL A HG13 1 
ATOM   870  H  HG21 . VAL A 1 61  ? 18.94900 27.98100 30.73900  1.000 40.80192  ? 380 VAL A HG21 1 
ATOM   871  H  HG22 . VAL A 1 61  ? 18.15500 27.87800 32.10600  1.000 40.80192  ? 380 VAL A HG22 1 
ATOM   872  H  HG23 . VAL A 1 61  ? 19.02500 26.65500 31.60100  1.000 40.80192  ? 380 VAL A HG23 1 
ATOM   873  N  N    . HIS A 1 62  ? 15.25000 24.43100 29.92300  1.000 30.58967  ? 381 HIS A N    1 
ATOM   874  C  CA   . HIS A 1 62  ? 14.07700 23.85000 29.28600  1.000 32.54054  ? 381 HIS A CA   1 
ATOM   875  C  C    . HIS A 1 62  ? 13.03800 23.39700 30.31300  1.000 31.24547  ? 381 HIS A C    1 
ATOM   876  O  O    . HIS A 1 62  ? 11.84400 23.65500 30.15600  1.000 38.51882  ? 381 HIS A O    1 
ATOM   877  C  CB   . HIS A 1 62  ? 14.45700 22.66600 28.39400  1.000 29.83512  ? 381 HIS A CB   1 
ATOM   878  C  CG   . HIS A 1 62  ? 13.25900 21.90200 27.91300  1.000 34.08581  ? 381 HIS A CG   1 
ATOM   879  N  ND1  . HIS A 1 62  ? 12.45400 22.38000 26.88900  1.000 35.08688  ? 381 HIS A ND1  1 
ATOM   880  C  CD2  . HIS A 1 62  ? 12.74800 20.73100 28.35200  1.000 32.52853  ? 381 HIS A CD2  1 
ATOM   881  C  CE1  . HIS A 1 62  ? 11.48500 21.48500 26.73200  1.000 37.21208  ? 381 HIS A CE1  1 
ATOM   882  N  NE2  . HIS A 1 62  ? 11.62400 20.47200 27.59300  1.000 35.18231  ? 381 HIS A NE2  1 
ATOM   883  H  H    . HIS A 1 62  ? 15.99600 24.06900 29.69300  1.000 36.78460  ? 381 HIS A H    1 
ATOM   884  H  HA   . HIS A 1 62  ? 13.68700 24.54900 28.73800  1.000 39.12564  ? 381 HIS A HA   1 
ATOM   885  H  HB2  . HIS A 1 62  ? 14.95900 22.98900 27.63000  1.000 35.41715  ? 381 HIS A HB2  1 
ATOM   886  H  HB3  . HIS A 1 62  ? 15.04200 22.06900 28.88600  1.000 35.41715  ? 381 HIS A HB3  1 
ATOM   887  H  HD1  . HIS A 1 62  ? 12.56100 23.10900 26.44500  1.000 42.18125  ? 381 HIS A HD1  1 
ATOM   888  H  HD2  . HIS A 1 62  ? 13.08900 20.20000 29.03600  1.000 38.64925  ? 381 HIS A HD2  1 
ATOM   889  H  HE1  . HIS A 1 62  ? 10.80100 21.55400 26.10600  1.000 44.73149  ? 381 HIS A HE1  1 
ATOM   890  N  N    . LEU A 1 63  ? 13.48800 22.74000 31.38700  1.000 30.64092  ? 382 LEU A N    1 
ATOM   891  C  CA   . LEU A 1 63  ? 12.55000 22.28000 32.40800  1.000 31.93492  ? 382 LEU A CA   1 
ATOM   892  C  C    . LEU A 1 63  ? 11.76900 23.44400 33.00400  1.000 33.53869  ? 382 LEU A C    1 
ATOM   893  O  O    . LEU A 1 63  ? 10.56600 23.34000 33.22100  1.000 37.47695  ? 382 LEU A O    1 
ATOM   894  C  CB   . LEU A 1 63  ? 13.26200 21.52500 33.53100  1.000 36.23226  ? 382 LEU A CB   1 
ATOM   895  C  CG   . LEU A 1 63  ? 13.78500 20.13700 33.20400  1.000 49.77337  ? 382 LEU A CG   1 
ATOM   896  C  CD1  . LEU A 1 63  ? 14.33300 19.47200 34.44700  1.000 55.88044  ? 382 LEU A CD1  1 
ATOM   897  C  CD2  . LEU A 1 63  ? 12.70200 19.25400 32.58300  1.000 64.35420  ? 382 LEU A CD2  1 
ATOM   898  H  H    . LEU A 1 63  ? 14.31400 22.55500 31.53900  1.000 36.38412  ? 382 LEU A H    1 
ATOM   899  H  HA   . LEU A 1 63  ? 11.93400 21.67400 31.96600  1.000 37.93692  ? 382 LEU A HA   1 
ATOM   900  H  HB2  . LEU A 1 63  ? 14.00900 22.06600 33.83200  1.000 43.55571  ? 382 LEU A HB2  1 
ATOM   901  H  HB3  . LEU A 1 63  ? 12.64900 21.44800 34.27900  1.000 43.55571  ? 382 LEU A HB3  1 
ATOM   902  H  HG   . LEU A 1 63  ? 14.49700 20.24300 32.55300  1.000 59.80504  ? 382 LEU A HG   1 
ATOM   903  H  HD11 . LEU A 1 63  ? 14.66300 18.58800 34.22300  1.000 67.13353  ? 382 LEU A HD11 1 
ATOM   904  H  HD12 . LEU A 1 63  ? 15.05900 20.00600 34.80700  1.000 67.13353  ? 382 LEU A HD12 1 
ATOM   905  H  HD13 . LEU A 1 63  ? 13.62900 19.39500 35.11000  1.000 67.13353  ? 382 LEU A HD13 1 
ATOM   906  H  HD21 . LEU A 1 63  ? 13.07100 18.37800 32.38800  1.000 77.30204  ? 382 LEU A HD21 1 
ATOM   907  H  HD22 . LEU A 1 63  ? 11.96300 19.16200 33.20500  1.000 77.30204  ? 382 LEU A HD22 1 
ATOM   908  H  HD23 . LEU A 1 63  ? 12.38400 19.66100 31.76200  1.000 77.30204  ? 382 LEU A HD23 1 
ATOM   909  N  N    . LYS A 1 64  ? 12.46500 24.55200 33.27300  1.000 38.60413  ? 383 LYS A N    1 
ATOM   910  C  CA   . LYS A 1 64  ? 11.83800 25.70800 33.88800  1.000 44.58079  ? 383 LYS A CA   1 
ATOM   911  C  C    . LYS A 1 64  ? 10.98600 26.48900 32.89200  1.000 44.23153  ? 383 LYS A C    1 
ATOM   912  O  O    . LYS A 1 64  ? 9.96500  27.04800 33.27300  1.000 48.35864  ? 383 LYS A O    1 
ATOM   913  C  CB   . LYS A 1 64  ? 12.91100 26.62000 34.50800  1.000 40.49808  ? 383 LYS A CB   1 
ATOM   914  C  CG   . LYS A 1 64  ? 12.40000 27.56100 35.59600  1.000 57.23675  ? 383 LYS A CG   1 
ATOM   915  C  CD   . LYS A 1 64  ? 12.06300 26.84000 36.90400  1.000 62.10036  ? 383 LYS A CD   1 
ATOM   916  C  CE   . LYS A 1 64  ? 11.50100 27.75900 37.96800  1.000 67.71380  ? 383 LYS A CE   1 
ATOM   917  N  NZ   . LYS A 1 64  ? 12.54700 28.63300 38.55900  1.000 68.96633  ? 383 LYS A NZ   1 
ATOM   918  H  H    . LYS A 1 64  ? 13.30300 24.64800 33.10400  1.000 46.40195  ? 383 LYS A H    1 
ATOM   919  H  HA   . LYS A 1 64  ? 11.24600 25.38800 34.58700  1.000 53.57395  ? 383 LYS A HA   1 
ATOM   920  H  HB2  . LYS A 1 64  ? 13.61300 26.06500 34.88200  1.000 48.67469  ? 383 LYS A HB2  1 
ATOM   921  H  HB3  . LYS A 1 64  ? 13.31400 27.15000 33.80300  1.000 48.67469  ? 383 LYS A HB3  1 
ATOM   922  H  HG2  . LYS A 1 64  ? 13.07100 28.23900 35.77100  1.000 68.76109  ? 383 LYS A HG2  1 
ATOM   923  H  HG3  . LYS A 1 64  ? 11.60900 28.02100 35.27300  1.000 68.76109  ? 383 LYS A HG3  1 
ATOM   924  H  HD2  . LYS A 1 64  ? 11.42100 26.13600 36.72200  1.000 74.59743  ? 383 LYS A HD2  1 
ATOM   925  H  HD3  . LYS A 1 64  ? 12.86400 26.41200 37.24500  1.000 74.59743  ? 383 LYS A HD3  1 
ATOM   926  H  HE2  . LYS A 1 64  ? 10.80100 28.30900 37.58200  1.000 81.33356  ? 383 LYS A HE2  1 
ATOM   927  H  HE3  . LYS A 1 64  ? 11.09100 27.22800 38.66900  1.000 81.33356  ? 383 LYS A HE3  1 
ATOM   928  H  HZ1  . LYS A 1 64  ? 12.16000 29.28800 39.02200  1.000 82.83659  ? 383 LYS A HZ1  1 
ATOM   929  H  HZ2  . LYS A 1 64  ? 13.06400 28.15200 39.10100  1.000 82.83659  ? 383 LYS A HZ2  1 
ATOM   930  H  HZ3  . LYS A 1 64  ? 13.04400 28.98300 37.90900  1.000 82.83659  ? 383 LYS A HZ3  1 
ATOM   931  N  N    . PHE A 1 65  ? 11.40600 26.50800 31.61800  1.000 44.18361  ? 384 PHE A N    1 
ATOM   932  C  CA   . PHE A 1 65  ? 10.75600 27.30400 30.58800  1.000 39.37472  ? 384 PHE A CA   1 
ATOM   933  C  C    . PHE A 1 65  ? 10.52100 26.48700 29.31900  1.000 44.22827  ? 384 PHE A C    1 
ATOM   934  O  O    . PHE A 1 65  ? 11.10100 26.78500 28.27500  1.000 43.24076  ? 384 PHE A O    1 
ATOM   935  C  CB   . PHE A 1 65  ? 11.63400 28.52300 30.24900  1.000 44.86431  ? 384 PHE A CB   1 
ATOM   936  C  CG   . PHE A 1 65  ? 11.91700 29.43700 31.40700  1.000 46.14499  ? 384 PHE A CG   1 
ATOM   937  C  CD1  . PHE A 1 65  ? 10.97800 30.36200 31.82600  1.000 63.17900  ? 384 PHE A CD1  1 
ATOM   938  C  CD2  . PHE A 1 65  ? 13.11400 29.36300 32.09200  1.000 44.10417  ? 384 PHE A CD2  1 
ATOM   939  C  CE1  . PHE A 1 65  ? 11.24000 31.20100 32.90200  1.000 87.00399  ? 384 PHE A CE1  1 
ATOM   940  C  CE2  . PHE A 1 65  ? 13.37200 30.20400 33.16700  1.000 50.92047  ? 384 PHE A CE2  1 
ATOM   941  C  CZ   . PHE A 1 65  ? 12.43700 31.11800 33.56500  1.000 54.20756  ? 384 PHE A CZ   1 
ATOM   942  H  H    . PHE A 1 65  ? 12.08000 26.05500 31.33500  1.000 53.09733  ? 384 PHE A H    1 
ATOM   943  H  HA   . PHE A 1 65  ? 9.89600  27.59400 30.93000  1.000 47.32666  ? 384 PHE A HA   1 
ATOM   944  H  HB2  . PHE A 1 65  ? 12.47800 28.20800 29.88800  1.000 53.91417  ? 384 PHE A HB2  1 
ATOM   945  H  HB3  . PHE A 1 65  ? 11.19900 29.03400 29.54900  1.000 53.91417  ? 384 PHE A HB3  1 
ATOM   946  H  HD1  . PHE A 1 65  ? 10.16300 30.42300 31.38300  1.000 75.89180  ? 384 PHE A HD1  1 
ATOM   947  H  HD2  . PHE A 1 65  ? 13.75500 28.74200 31.83000  1.000 53.00200  ? 384 PHE A HD2  1 
ATOM   948  H  HE1  . PHE A 1 65  ? 10.60200 31.82100 33.17300  1.000 104.48178 ? 384 PHE A HE1  1 
ATOM   949  H  HE2  . PHE A 1 65  ? 14.18400 30.14500 33.61700  1.000 61.18156  ? 384 PHE A HE2  1 
ATOM   950  H  HZ   . PHE A 1 65  ? 12.61200 31.68200 34.28300  1.000 65.12606  ? 384 PHE A HZ   1 
ATOM   951  N  N    . PRO A 1 66  ? 9.67800  25.42900 29.36100  1.000 42.66321  ? 385 PRO A N    1 
ATOM   952  C  CA   . PRO A 1 66  ? 9.58500  24.47100 28.26800  1.000 37.75408  ? 385 PRO A CA   1 
ATOM   953  C  C    . PRO A 1 66  ? 9.03600  25.01100 26.94700  1.000 48.09163  ? 385 PRO A C    1 
ATOM   954  O  O    . PRO A 1 66  ? 9.33600  24.44800 25.89900  1.000 45.90415  ? 385 PRO A O    1 
ATOM   955  C  CB   . PRO A 1 66  ? 8.66800  23.38700 28.85100  1.000 37.98460  ? 385 PRO A CB   1 
ATOM   956  C  CG   . PRO A 1 66  ? 7.90600  24.05900 29.89600  1.000 39.04590  ? 385 PRO A CG   1 
ATOM   957  C  CD   . PRO A 1 66  ? 8.81600  25.06200 30.49200  1.000 37.18281  ? 385 PRO A CD   1 
ATOM   958  H  HA   . PRO A 1 66  ? 10.46800 24.16900 28.00400  1.000 45.38189  ? 385 PRO A HA   1 
ATOM   959  H  HB2  . PRO A 1 66  ? 8.08200  23.01900 28.17100  1.000 45.19653  ? 385 PRO A HB2  1 
ATOM   960  H  HB3  . PRO A 1 66  ? 9.18300  22.64800 29.21200  1.000 45.19653  ? 385 PRO A HB3  1 
ATOM   961  H  HG2  . PRO A 1 66  ? 7.11500  24.48400 29.52900  1.000 46.47010  ? 385 PRO A HG2  1 
ATOM   962  H  HG3  . PRO A 1 66  ? 7.60300  23.42600 30.56500  1.000 46.47010  ? 385 PRO A HG3  1 
ATOM   963  H  HD2  . PRO A 1 66  ? 8.33100  25.82700 30.83900  1.000 44.23439  ? 385 PRO A HD2  1 
ATOM   964  H  HD3  . PRO A 1 66  ? 9.32700  24.69200 31.22900  1.000 44.23439  ? 385 PRO A HD3  1 
ATOM   965  N  N    . THR A 1 67  ? 8.21300  26.06600 26.98700  1.000 45.20715  ? 386 THR A N    1 
ATOM   966  C  CA   . THR A 1 67  ? 7.68700  26.64600 25.75800  1.000 50.28426  ? 386 THR A CA   1 
ATOM   967  C  C    . THR A 1 67  ? 8.64700  27.60000 25.04800  1.000 52.04959  ? 386 THR A C    1 
ATOM   968  O  O    . THR A 1 67  ? 8.41200  27.94800 23.89500  1.000 60.98543  ? 386 THR A O    1 
ATOM   969  C  CB   . THR A 1 67  ? 6.37400  27.37200 26.00600  1.000 48.86498  ? 386 THR A CB   1 
ATOM   970  O  OG1  . THR A 1 67  ? 6.62100  28.49300 26.84800  1.000 56.73290  ? 386 THR A OG1  1 
ATOM   971  C  CG2  . THR A 1 67  ? 5.32500  26.46300 26.62300  1.000 52.90246  ? 386 THR A CG2  1 
ATOM   972  H  H    . THR A 1 67  ? 7.95300  26.45300 27.71000  1.000 54.32558  ? 386 THR A H    1 
ATOM   973  H  HA   . THR A 1 67  ? 7.55100  25.88500 25.17200  1.000 60.41810  ? 386 THR A HA   1 
ATOM   974  H  HB   . THR A 1 67  ? 6.02000  27.66700 25.15200  1.000 58.71498  ? 386 THR A HB   1 
ATOM   975  H  HG1  . THR A 1 67  ? 5.89000  28.82000 27.10100  1.000 68.15648  ? 386 THR A HG1  1 
ATOM   976  H  HG21 . THR A 1 67  ? 4.50600  26.96300 26.76400  1.000 63.55995  ? 386 THR A HG21 1 
ATOM   977  H  HG22 . THR A 1 67  ? 5.15000  25.71900 26.02600  1.000 63.55995  ? 386 THR A HG22 1 
ATOM   978  H  HG23 . THR A 1 67  ? 5.64800  26.12600 27.47300  1.000 63.55995  ? 386 THR A HG23 1 
ATOM   979  N  N    . LYS A 1 68  ? 9.71800  28.01800 25.73500  1.000 53.36416  ? 387 LYS A N    1 
ATOM   980  C  CA   . LYS A 1 68  ? 10.63700 29.01600 25.20600  1.000 49.85019  ? 387 LYS A CA   1 
ATOM   981  C  C    . LYS A 1 68  ? 12.00700 28.45900 24.82400  1.000 49.93697  ? 387 LYS A C    1 
ATOM   982  O  O    . LYS A 1 68  ? 12.62300 28.92100 23.86500  1.000 53.65711  ? 387 LYS A O    1 
ATOM   983  C  CB   . LYS A 1 68  ? 10.81700 30.13600 26.23500  1.000 55.36045  ? 387 LYS A CB   1 
ATOM   984  C  CG   . LYS A 1 68  ? 9.55000  30.95100 26.47100  1.000 70.81786  ? 387 LYS A CG   1 
ATOM   985  C  CD   . LYS A 1 68  ? 9.79600  32.17800 27.33800  1.000 89.39872  ? 387 LYS A CD   1 
ATOM   986  C  CE   . LYS A 1 68  ? 8.57400  33.05500 27.47000  1.000 129.88633 ? 387 LYS A CE   1 
ATOM   987  N  NZ   . LYS A 1 68  ? 7.50000  32.40000 28.26400  1.000 102.38106 ? 387 LYS A NZ   1 
ATOM   988  H  H    . LYS A 1 68  ? 9.92600  27.72800 26.51800  1.000 64.11399  ? 387 LYS A H    1 
ATOM   989  H  HA   . LYS A 1 68  ? 10.23700 29.34800 24.38700  1.000 59.89722  ? 387 LYS A HA   1 
ATOM   990  H  HB2  . LYS A 1 68  ? 11.10600 29.75000 27.07600  1.000 66.50954  ? 387 LYS A HB2  1 
ATOM   991  H  HB3  . LYS A 1 68  ? 11.52400 30.72900 25.93700  1.000 66.50954  ? 387 LYS A HB3  1 
ATOM   992  H  HG2  . LYS A 1 68  ? 9.18600  31.23100 25.61700  1.000 85.05843  ? 387 LYS A HG2  1 
ATOM   993  H  HG3  . LYS A 1 68  ? 8.88200  30.38900 26.89400  1.000 85.05843  ? 387 LYS A HG3  1 
ATOM   994  H  HD2  . LYS A 1 68  ? 10.08200 31.89400 28.22000  1.000 107.35547 ? 387 LYS A HD2  1 
ATOM   995  H  HD3  . LYS A 1 68  ? 10.52200 32.69700 26.95800  1.000 107.35547 ? 387 LYS A HD3  1 
ATOM   996  H  HE2  . LYS A 1 68  ? 8.82200  33.89200 27.89200  1.000 155.94060 ? 387 LYS A HE2  1 
ATOM   997  H  HE3  . LYS A 1 68  ? 8.23600  33.27200 26.58700  1.000 155.94060 ? 387 LYS A HE3  1 
ATOM   998  H  HZ1  . LYS A 1 68  ? 6.75200  32.37000 27.78300  1.000 122.93427 ? 387 LYS A HZ1  1 
ATOM   999  H  HZ2  . LYS A 1 68  ? 7.75000  31.57200 28.47600  1.000 122.93427 ? 387 LYS A HZ2  1 
ATOM   1000 H  HZ3  . LYS A 1 68  ? 7.35500  32.86500 29.00900  1.000 122.93427 ? 387 LYS A HZ3  1 
ATOM   1001 N  N    . VAL A 1 69  ? 12.48600 27.47200 25.58400  1.000 38.93716  ? 388 VAL A N    1 
ATOM   1002 C  CA   . VAL A 1 69  ? 13.80200 26.90300 25.35900  1.000 42.76662  ? 388 VAL A CA   1 
ATOM   1003 C  C    . VAL A 1 69  ? 13.68300 25.40800 25.11000  1.000 36.61310  ? 388 VAL A C    1 
ATOM   1004 O  O    . VAL A 1 69  ? 12.99900 24.70900 25.85000  1.000 42.13877  ? 388 VAL A O    1 
ATOM   1005 C  CB   . VAL A 1 69  ? 14.71900 27.17200 26.55500  1.000 38.43692  ? 388 VAL A CB   1 
ATOM   1006 C  CG1  . VAL A 1 69  ? 16.09900 26.55400 26.32200  1.000 38.89449  ? 388 VAL A CG1  1 
ATOM   1007 C  CG2  . VAL A 1 69  ? 14.80500 28.66200 26.83500  1.000 48.77082  ? 388 VAL A CG2  1 
ATOM   1008 H  H    . VAL A 1 69  ? 12.05500 27.12000 26.23900  1.000 46.80159  ? 388 VAL A H    1 
ATOM   1009 H  HA   . VAL A 1 69  ? 14.19300 27.32400 24.57700  1.000 51.39694  ? 388 VAL A HA   1 
ATOM   1010 H  HB   . VAL A 1 69  ? 14.34100 26.75000 27.34200  1.000 46.20130  ? 388 VAL A HB   1 
ATOM   1011 H  HG11 . VAL A 1 69  ? 16.66700 26.73300 27.08700  1.000 46.75038  ? 388 VAL A HG11 1 
ATOM   1012 H  HG12 . VAL A 1 69  ? 16.00900 25.59500 26.20400  1.000 46.75038  ? 388 VAL A HG12 1 
ATOM   1013 H  HG13 . VAL A 1 69  ? 16.49700 26.94100 25.52700  1.000 46.75038  ? 388 VAL A HG13 1 
ATOM   1014 H  HG21 . VAL A 1 69  ? 15.38900 28.81600 27.59400  1.000 58.60198  ? 388 VAL A HG21 1 
ATOM   1015 H  HG22 . VAL A 1 69  ? 15.16100 29.11800 26.05600  1.000 58.60198  ? 388 VAL A HG22 1 
ATOM   1016 H  HG23 . VAL A 1 69  ? 13.92000 29.00600 27.03300  1.000 58.60198  ? 388 VAL A HG23 1 
ATOM   1017 N  N    . SER A 1 70  ? 14.38500 24.92300 24.08800  1.000 36.40312  ? 389 SER A N    1 
ATOM   1018 C  CA   . SER A 1 70  ? 14.33800 23.51100 23.76000  1.000 37.71942  ? 389 SER A CA   1 
ATOM   1019 C  C    . SER A 1 70  ? 15.33400 22.70200 24.58600  1.000 35.96510  ? 389 SER A C    1 
ATOM   1020 O  O    . SER A 1 70  ? 16.28400 23.23900 25.15700  1.000 34.95010  ? 389 SER A O    1 
ATOM   1021 C  CB   . SER A 1 70  ? 14.59700 23.30200 22.27600  1.000 45.06080  ? 389 SER A CB   1 
ATOM   1022 O  OG   . SER A 1 70  ? 15.92300 23.68800 21.96700  1.000 58.13395  ? 389 SER A OG   1 
ATOM   1023 H  H    . SER A 1 70  ? 14.89100 25.39600 23.57800  1.000 43.76074  ? 389 SER A H    1 
ATOM   1024 H  HA   . SER A 1 70  ? 13.44800 23.19300 23.97700  1.000 45.34030  ? 389 SER A HA   1 
ATOM   1025 H  HB2  . SER A 1 70  ? 14.45900 22.37100 22.04200  1.000 54.14996  ? 389 SER A HB2  1 
ATOM   1026 H  HB3  . SER A 1 70  ? 13.96800 23.82300 21.75200  1.000 54.14996  ? 389 SER A HB3  1 
ATOM   1027 H  HG   . SER A 1 70  ? 16.35300 23.80700 22.67800  1.000 69.83773  ? 389 SER A HG   1 
ATOM   1028 N  N    . LYS A 1 71  ? 15.08700 21.41000 24.61900  1.000 41.08690  ? 390 LYS A N    1 
ATOM   1029 C  CA   . LYS A 1 71  ? 16.01000 20.51300 25.32800  1.000 43.87617  ? 390 LYS A CA   1 
ATOM   1030 C  C    . LYS A 1 71  ? 17.26600 20.28500 24.50900  1.000 43.83552  ? 390 LYS A C    1 
ATOM   1031 O  O    . LYS A 1 71  ? 17.28100 20.62100 23.32800  1.000 36.47399  ? 390 LYS A O    1 
ATOM   1032 C  CB   . LYS A 1 71  ? 15.38400 19.12500 25.44500  1.000 48.92831  ? 390 LYS A CB   1 
ATOM   1033 C  CG   . LYS A 1 71  ? 13.86300 19.07800 25.44300  1.000 76.53325  ? 390 LYS A CG   1 
ATOM   1034 C  CD   . LYS A 1 71  ? 13.25600 18.80700 24.08800  1.000 115.67825 ? 390 LYS A CD   1 
ATOM   1035 C  CE   . LYS A 1 71  ? 12.01300 19.63200 23.83700  1.000 62.06013  ? 390 LYS A CE   1 
ATOM   1036 N  NZ   . LYS A 1 71  ? 12.30900 20.85100 23.05400  1.000 49.24831  ? 390 LYS A NZ   1 
ATOM   1037 H  H    . LYS A 1 71  ? 14.41100 21.02700 24.25100  1.000 49.38128  ? 390 LYS A H    1 
ATOM   1038 H  HA   . LYS A 1 71  ? 16.20100 20.92100 26.18700  1.000 52.72840  ? 390 LYS A HA   1 
ATOM   1039 H  HB2  . LYS A 1 71  ? 15.70800 18.58000 24.71000  1.000 58.79097  ? 390 LYS A HB2  1 
ATOM   1040 H  HB3  . LYS A 1 71  ? 15.70200 18.71400 26.26400  1.000 58.79097  ? 390 LYS A HB3  1 
ATOM   1041 H  HG2  . LYS A 1 71  ? 13.57000 18.39100 26.06100  1.000 91.91690  ? 390 LYS A HG2  1 
ATOM   1042 H  HG3  . LYS A 1 71  ? 13.52300 19.92300 25.77600  1.000 91.91690  ? 390 LYS A HG3  1 
ATOM   1043 H  HD2  . LYS A 1 71  ? 13.91200 18.99700 23.39900  1.000 138.89089 ? 390 LYS A HD2  1 
ATOM   1044 H  HD3  . LYS A 1 71  ? 13.03500 17.86500 24.01800  1.000 138.89089 ? 390 LYS A HD3  1 
ATOM   1045 H  HE2  . LYS A 1 71  ? 11.35900 19.09500 23.36300  1.000 74.54916  ? 390 LYS A HE2  1 
ATOM   1046 H  HE3  . LYS A 1 71  ? 11.61400 19.88200 24.68500  1.000 74.54916  ? 390 LYS A HE3  1 
ATOM   1047 H  HZ1  . LYS A 1 71  ? 12.16400 21.57000 23.55800  1.000 59.17497  ? 390 LYS A HZ1  1 
ATOM   1048 H  HZ2  . LYS A 1 71  ? 13.16000 20.83800 22.79400  1.000 59.17497  ? 390 LYS A HZ2  1 
ATOM   1049 H  HZ3  . LYS A 1 71  ? 11.78100 20.88000 22.33800  1.000 59.17497  ? 390 LYS A HZ3  1 
ATOM   1050 N  N    . ALA A 1 72  ? 18.28500 19.75400 25.15200  1.000 33.59359  ? 391 ALA A N    1 
ATOM   1051 C  CA   . ALA A 1 72  ? 19.48200 19.31400 24.46900  1.000 32.24265  ? 391 ALA A CA   1 
ATOM   1052 C  C    . ALA A 1 72  ? 19.10600 18.20200 23.49900  1.000 40.32731  ? 391 ALA A C    1 
ATOM   1053 O  O    . ALA A 1 72  ? 18.07000 17.56100 23.66500  1.000 38.67661  ? 391 ALA A O    1 
ATOM   1054 C  CB   . ALA A 1 72  ? 20.51500 18.82000 25.45400  1.000 36.80166  ? 391 ALA A CB   1 
ATOM   1055 H  H    . ALA A 1 72  ? 18.30300 19.63700 26.00400  1.000 40.38930  ? 391 ALA A H    1 
ATOM   1056 H  HA   . ALA A 1 72  ? 19.86900 20.06100 23.98600  1.000 38.76818  ? 391 ALA A HA   1 
ATOM   1057 H  HB1  . ALA A 1 72  ? 21.30700 18.53100 24.97500  1.000 44.23898  ? 391 ALA A HB1  1 
ATOM   1058 H  HB2  . ALA A 1 72  ? 20.75000 19.53700 26.06300  1.000 44.23898  ? 391 ALA A HB2  1 
ATOM   1059 H  HB3  . ALA A 1 72  ? 20.15200 18.07400 25.95700  1.000 44.23898  ? 391 ALA A HB3  1 
ATOM   1060 N  N    . CYS A 1 73  ? 19.98600 17.96400 22.52100  1.000 34.02860  ? 392 CYS A N    1 
ATOM   1061 C  CA   . CYS A 1 73  ? 19.72700 16.99700 21.47000  1.000 39.65138  ? 392 CYS A CA   1 
ATOM   1062 C  C    . CYS A 1 73  ? 20.70800 15.83000 21.48900  1.000 41.12287  ? 392 CYS A C    1 
ATOM   1063 O  O    . CYS A 1 73  ? 21.90400 16.03600 21.67100  1.000 35.34061  ? 392 CYS A O    1 
ATOM   1064 C  CB   . CYS A 1 73  ? 19.76400 17.70100 20.12700  1.000 43.62658  ? 392 CYS A CB   1 
ATOM   1065 S  SG   . CYS A 1 73  ? 18.58100 17.03600 18.94100  1.000 52.89258  ? 392 CYS A SG   1 
ATOM   1066 H  H    . CYS A 1 73  ? 20.74600 18.36100 22.45500  1.000 40.91131  ? 392 CYS A H    1 
ATOM   1067 H  HA   . CYS A 1 73  ? 18.84800 16.61800 21.62500  1.000 47.65865  ? 392 CYS A HA   1 
ATOM   1068 H  HB2  . CYS A 1 73  ? 19.58500 18.64500 20.25900  1.000 52.42890  ? 392 CYS A HB2  1 
ATOM   1069 H  HB3  . CYS A 1 73  ? 20.65800 17.63100 19.75700  1.000 52.42890  ? 392 CYS A HB3  1 
ATOM   1070 N  N    . CYS A 1 74  ? 20.17000 14.61800 21.30200  1.000 40.28111  ? 393 CYS A N    1 
ATOM   1071 C  CA   . CYS A 1 74  ? 20.95200 13.40600 21.13900  1.000 38.40221  ? 393 CYS A CA   1 
ATOM   1072 C  C    . CYS A 1 74  ? 21.49800 13.33100 19.71600  1.000 37.47632  ? 393 CYS A C    1 
ATOM   1073 O  O    . CYS A 1 74  ? 20.75100 13.05400 18.78300  1.000 29.15115  ? 393 CYS A O    1 
ATOM   1074 C  CB   . CYS A 1 74  ? 20.10100 12.18100 21.46900  1.000 39.07820  ? 393 CYS A CB   1 
ATOM   1075 S  SG   . CYS A 1 74  ? 20.99700 10.61300 21.37400  1.000 35.05718  ? 393 CYS A SG   1 
ATOM   1076 H  H    . CYS A 1 74  ? 19.32100 14.48400 21.26700  1.000 48.41433  ? 393 CYS A H    1 
ATOM   1077 H  HA   . CYS A 1 74  ? 21.70200 13.42200 21.75300  1.000 46.15965  ? 393 CYS A HA   1 
ATOM   1078 H  HB2  . CYS A 1 74  ? 19.73900 12.28200 22.36300  1.000 46.97084  ? 393 CYS A HB2  1 
ATOM   1079 H  HB3  . CYS A 1 74  ? 19.34700 12.14900 20.86000  1.000 46.97084  ? 393 CYS A HB3  1 
ATOM   1080 N  N    . VAL A 1 75  ? 22.80300 13.56500 19.56700  1.000 27.72881  ? 394 VAL A N    1 
ATOM   1081 C  CA   . VAL A 1 75  ? 23.43700 13.64000 18.26100  1.000 25.88296  ? 394 VAL A CA   1 
ATOM   1082 C  C    . VAL A 1 75  ? 24.69200 12.78000 18.19900  1.000 33.50807  ? 394 VAL A C    1 
ATOM   1083 O  O    . VAL A 1 75  ? 25.25100 12.41000 19.23400  1.000 27.07649  ? 394 VAL A O    1 
ATOM   1084 C  CB   . VAL A 1 75  ? 23.81500 15.10700 17.91900  1.000 31.77133  ? 394 VAL A CB   1 
ATOM   1085 C  CG1  . VAL A 1 75  ? 22.58400 15.95100 17.61400  1.000 36.37310  ? 394 VAL A CG1  1 
ATOM   1086 C  CG2  . VAL A 1 75  ? 24.65800 15.72500 19.02900  1.000 34.58941  ? 394 VAL A CG2  1 
ATOM   1087 H  H    . VAL A 1 75  ? 23.34300 13.68400 20.22600  1.000 33.35157  ? 394 VAL A H    1 
ATOM   1088 H  HA   . VAL A 1 75  ? 22.79600 13.30700 17.61400  1.000 31.13655  ? 394 VAL A HA   1 
ATOM   1089 H  HB   . VAL A 1 75  ? 24.35300 15.09100 17.11200  1.000 38.20259  ? 394 VAL A HB   1 
ATOM   1090 H  HG11 . VAL A 1 75  ? 22.85700 16.85800 17.40500  1.000 43.72471  ? 394 VAL A HG11 1 
ATOM   1091 H  HG12 . VAL A 1 75  ? 22.11200 15.57300 16.85500  1.000 43.72471  ? 394 VAL A HG12 1 
ATOM   1092 H  HG13 . VAL A 1 75  ? 21.99800 15.96000 18.38700  1.000 43.72471  ? 394 VAL A HG13 1 
ATOM   1093 H  HG21 . VAL A 1 75  ? 24.88200 16.63900 18.79500  1.000 41.58429  ? 394 VAL A HG21 1 
ATOM   1094 H  HG22 . VAL A 1 75  ? 24.15600 15.71800 19.85900  1.000 41.58429  ? 394 VAL A HG22 1 
ATOM   1095 H  HG23 . VAL A 1 75  ? 25.47300 15.21100 19.14100  1.000 41.58429  ? 394 VAL A HG23 1 
ATOM   1096 N  N    . PRO A 1 76  ? 25.19100 12.44300 16.98600  1.000 29.92195  ? 395 PRO A N    1 
ATOM   1097 C  CA   . PRO A 1 76  ? 26.52200 11.87200 16.85400  1.000 34.69286  ? 395 PRO A CA   1 
ATOM   1098 C  C    . PRO A 1 76  ? 27.60900 12.81100 17.36200  1.000 36.37670  ? 395 PRO A C    1 
ATOM   1099 O  O    . PRO A 1 76  ? 27.61900 13.99000 17.01500  1.000 34.09207  ? 395 PRO A O    1 
ATOM   1100 C  CB   . PRO A 1 76  ? 26.65700 11.61000 15.34700  1.000 31.24141  ? 395 PRO A CB   1 
ATOM   1101 C  CG   . PRO A 1 76  ? 25.28900 11.65400 14.81900  1.000 33.49004  ? 395 PRO A CG   1 
ATOM   1102 C  CD   . PRO A 1 76  ? 24.49200 12.55800 15.70100  1.000 25.64771  ? 395 PRO A CD   1 
ATOM   1103 H  HA   . PRO A 1 76  ? 26.63100 11.06900 17.38800  1.000 41.70843  ? 395 PRO A HA   1 
ATOM   1104 H  HB2  . PRO A 1 76  ? 27.21600 12.28000 14.92400  1.000 37.56669  ? 395 PRO A HB2  1 
ATOM   1105 H  HB3  . PRO A 1 76  ? 27.06900 10.74900 15.17800  1.000 37.56669  ? 395 PRO A HB3  1 
ATOM   1106 H  HG2  . PRO A 1 76  ? 25.28700 11.98100 13.90600  1.000 40.26505  ? 395 PRO A HG2  1 
ATOM   1107 H  HG3  . PRO A 1 76  ? 24.90100 10.76500 14.80300  1.000 40.26505  ? 395 PRO A HG3  1 
ATOM   1108 H  HD2  . PRO A 1 76  ? 24.48700 13.47100 15.37300  1.000 30.85425  ? 395 PRO A HD2  1 
ATOM   1109 H  HD3  . PRO A 1 76  ? 23.56600 12.27500 15.76700  1.000 30.85425  ? 395 PRO A HD3  1 
ATOM   1110 N  N    . THR A 1 77  ? 28.50300 12.26600 18.18900  1.000 29.28857  ? 396 THR A N    1 
ATOM   1111 C  CA   . THR A 1 77  ? 29.64200 13.00100 18.70600  1.000 35.77706  ? 396 THR A CA   1 
ATOM   1112 C  C    . THR A 1 77  ? 30.95900 12.47700 18.13900  1.000 41.02405  ? 396 THR A C    1 
ATOM   1113 O  O    . THR A 1 77  ? 32.01200 13.05900 18.37800  1.000 43.11281  ? 396 THR A O    1 
ATOM   1114 C  CB   . THR A 1 77  ? 29.59700 12.93300 20.22400  1.000 32.16172  ? 396 THR A CB   1 
ATOM   1115 O  OG1  . THR A 1 77  ? 29.59800 11.55900 20.61300  1.000 29.45828  ? 396 THR A OG1  1 
ATOM   1116 C  CG2  . THR A 1 77  ? 28.36600 13.61500 20.77600  1.000 36.79148  ? 396 THR A CG2  1 
ATOM   1117 H  H    . THR A 1 77  ? 28.45900 11.45200 18.46400  1.000 35.22328  ? 396 THR A H    1 
ATOM   1118 H  HA   . THR A 1 77  ? 29.59200 13.92800 18.42500  1.000 43.00947  ? 396 THR A HA   1 
ATOM   1119 H  HB   . THR A 1 77  ? 30.37200 13.39400 20.58100  1.000 38.67106  ? 396 THR A HB   1 
ATOM   1120 H  HG1  . THR A 1 77  ? 29.45100 11.50100 21.43800  1.000 34.96495  ? 396 THR A HG1  1 
ATOM   1121 H  HG21 . THR A 1 77  ? 28.36800 13.55400 21.74400  1.000 44.22677  ? 396 THR A HG21 1 
ATOM   1122 H  HG22 . THR A 1 77  ? 28.36700 14.54800 20.51200  1.000 44.22677  ? 396 THR A HG22 1 
ATOM   1123 H  HG23 . THR A 1 77  ? 27.57200 13.18100 20.42700  1.000 44.22677  ? 396 THR A HG23 1 
ATOM   1124 N  N    . LYS A 1 78  ? 30.88600 11.36700 17.39800  1.000 34.95910  ? 397 LYS A N    1 
ATOM   1125 C  CA   . LYS A 1 78  ? 32.04000 10.80100 16.72300  1.000 34.83212  ? 397 LYS A CA   1 
ATOM   1126 C  C    . LYS A 1 78  ? 31.52200 10.01000 15.53100  1.000 35.67433  ? 397 LYS A C    1 
ATOM   1127 O  O    . LYS A 1 78  ? 30.55800 9.26800  15.67600  1.000 32.93604  ? 397 LYS A O    1 
ATOM   1128 C  CB   . LYS A 1 78  ? 32.83200 9.88300  17.64100  1.000 42.18991  ? 397 LYS A CB   1 
ATOM   1129 C  CG   . LYS A 1 78  ? 34.12800 9.38000  17.03200  1.000 52.90715  ? 397 LYS A CG   1 
ATOM   1130 C  CD   . LYS A 1 78  ? 34.77500 8.28600  17.86900  1.000 59.71908  ? 397 LYS A CD   1 
ATOM   1131 C  CE   . LYS A 1 78  ? 36.03400 7.75000  17.23600  1.000 61.24502  ? 397 LYS A CE   1 
ATOM   1132 N  NZ   . LYS A 1 78  ? 36.43500 6.45100  17.83900  1.000 95.01170  ? 397 LYS A NZ   1 
ATOM   1133 H  H    . LYS A 1 78  ? 30.15900 10.92500 17.27700  1.000 42.02791  ? 397 LYS A H    1 
ATOM   1134 H  HA   . LYS A 1 78  ? 32.63700 11.51400 16.44600  1.000 41.87554  ? 397 LYS A HA   1 
ATOM   1135 H  HB2  . LYS A 1 78  ? 33.03300 10.35600 18.46300  1.000 50.70488  ? 397 LYS A HB2  1 
ATOM   1136 H  HB3  . LYS A 1 78  ? 32.27900 9.12200  17.87900  1.000 50.70488  ? 397 LYS A HB3  1 
ATOM   1137 H  HG2  . LYS A 1 78  ? 33.95300 9.04100  16.14000  1.000 63.56557  ? 397 LYS A HG2  1 
ATOM   1138 H  HG3  . LYS A 1 78  ? 34.74700 10.12100 16.93800  1.000 63.56557  ? 397 LYS A HG3  1 
ATOM   1139 H  HD2  . LYS A 1 78  ? 34.98200 8.63500  18.75000  1.000 71.73989  ? 397 LYS A HD2  1 
ATOM   1140 H  HD3  . LYS A 1 78  ? 34.14300 7.56000  17.99300  1.000 71.73989  ? 397 LYS A HD3  1 
ATOM   1141 H  HE2  . LYS A 1 78  ? 35.89600 7.63700  16.28300  1.000 73.57102  ? 397 LYS A HE2  1 
ATOM   1142 H  HE3  . LYS A 1 78  ? 36.75200 8.39400  17.34400  1.000 73.57102  ? 397 LYS A HE3  1 
ATOM   1143 H  HZ1  . LYS A 1 78  ? 36.88500 5.97100  17.23900  1.000 114.09103 ? 397 LYS A HZ1  1 
ATOM   1144 H  HZ2  . LYS A 1 78  ? 36.95200 6.60000  18.54800  1.000 114.09103 ? 397 LYS A HZ2  1 
ATOM   1145 H  HZ3  . LYS A 1 78  ? 35.70800 6.00300  18.09100  1.000 114.09103 ? 397 LYS A HZ3  1 
ATOM   1146 N  N    . LEU A 1 79  ? 32.17300 10.18200 14.37300  1.000 35.89866  ? 398 LEU A N    1 
ATOM   1147 C  CA   . LEU A 1 79  ? 31.76100 9.53900  13.13400  1.000 27.97973  ? 398 LEU A CA   1 
ATOM   1148 C  C    . LEU A 1 79  ? 32.90200 8.68200  12.59000  1.000 36.10368  ? 398 LEU A C    1 
ATOM   1149 O  O    . LEU A 1 79  ? 34.05700 8.92300  12.91400  1.000 37.02674  ? 398 LEU A O    1 
ATOM   1150 C  CB   . LEU A 1 79  ? 31.37300 10.59700 12.11500  1.000 29.52887  ? 398 LEU A CB   1 
ATOM   1151 C  CG   . LEU A 1 79  ? 30.19900 11.49400 12.49500  1.000 34.31833  ? 398 LEU A CG   1 
ATOM   1152 C  CD1  . LEU A 1 79  ? 30.02900 12.61000 11.50100  1.000 31.16972  ? 398 LEU A CD1  1 
ATOM   1153 C  CD2  . LEU A 1 79  ? 28.91500 10.70700 12.60700  1.000 25.46545  ? 398 LEU A CD2  1 
ATOM   1154 H  H    . LEU A 1 79  ? 32.87000 10.68000 14.29200  1.000 43.15539  ? 398 LEU A H    1 
ATOM   1155 H  HA   . LEU A 1 79  ? 30.99600 8.96900  13.30800  1.000 33.65267  ? 398 LEU A HA   1 
ATOM   1156 H  HB2  . LEU A 1 79  ? 32.14600 11.15900 11.94900  1.000 35.51164  ? 398 LEU A HB2  1 
ATOM   1157 H  HB3  . LEU A 1 79  ? 31.16000 10.15300 11.27900  1.000 35.51164  ? 398 LEU A HB3  1 
ATOM   1158 H  HG   . LEU A 1 79  ? 30.40000 11.87600 13.36400  1.000 41.25899  ? 398 LEU A HG   1 
ATOM   1159 H  HD11 . LEU A 1 79  ? 29.27800 13.16600 11.76300  1.000 37.48067  ? 398 LEU A HD11 1 
ATOM   1160 H  HD12 . LEU A 1 79  ? 30.83600 13.14800 11.47700  1.000 37.48067  ? 398 LEU A HD12 1 
ATOM   1161 H  HD13 . LEU A 1 79  ? 29.86300 12.23700 10.62100  1.000 37.48067  ? 398 LEU A HD13 1 
ATOM   1162 H  HD21 . LEU A 1 79  ? 28.19000 11.30400 12.84900  1.000 30.63553  ? 398 LEU A HD21 1 
ATOM   1163 H  HD22 . LEU A 1 79  ? 28.71700 10.28700 11.75500  1.000 30.63553  ? 398 LEU A HD22 1 
ATOM   1164 H  HD23 . LEU A 1 79  ? 29.01200 10.02400 13.28900  1.000 30.63553  ? 398 LEU A HD23 1 
ATOM   1165 N  N    . SER A 1 80  ? 32.55300 7.66600  11.79600  1.000 31.52189  ? 399 SER A N    1 
ATOM   1166 C  CA   . SER A 1 80  ? 33.51900 6.77500  11.17500  1.000 40.47576  ? 399 SER A CA   1 
ATOM   1167 C  C    . SER A 1 80  ? 33.35100 6.78100  9.66200   1.000 38.82273  ? 399 SER A C    1 
ATOM   1168 O  O    . SER A 1 80  ? 32.26300 7.05700  9.16500   1.000 33.52618  ? 399 SER A O    1 
ATOM   1169 C  CB   . SER A 1 80  ? 33.34900 5.34500  11.68100  1.000 36.70007  ? 399 SER A CB   1 
ATOM   1170 O  OG   . SER A 1 80  ? 33.67000 5.25500  13.05500  1.000 44.21067  ? 399 SER A OG   1 
ATOM   1171 H  H    . SER A 1 80  ? 31.73600 7.47800  11.60400  1.000 37.90326  ? 399 SER A H    1 
ATOM   1172 H  HA   . SER A 1 80  ? 34.40400 7.09500  11.41000  1.000 48.64791  ? 399 SER A HA   1 
ATOM   1173 H  HB2  . SER A 1 80  ? 32.43500 5.05400  11.53900  1.000 44.11708  ? 399 SER A HB2  1 
ATOM   1174 H  HB3  . SER A 1 80  ? 33.91900 4.74800  11.17200  1.000 44.11708  ? 399 SER A HB3  1 
ATOM   1175 H  HG   . SER A 1 80  ? 33.56900 4.46300  13.31500  1.000 53.12980  ? 399 SER A HG   1 
ATOM   1176 N  N    . PRO A 1 81  ? 34.41000 6.43800  8.89200   1.000 35.75578  ? 400 PRO A N    1 
ATOM   1177 C  CA   . PRO A 1 81  ? 34.30500 6.36000  7.44100   1.000 42.37470  ? 400 PRO A CA   1 
ATOM   1178 C  C    . PRO A 1 81  ? 33.73400 5.03800  6.94100   1.000 41.54749  ? 400 PRO A C    1 
ATOM   1179 O  O    . PRO A 1 81  ? 33.66900 4.05600  7.67800   1.000 37.70643  ? 400 PRO A O    1 
ATOM   1180 C  CB   . PRO A 1 81  ? 35.75500 6.51900  6.99600   1.000 42.94156  ? 400 PRO A CB   1 
ATOM   1181 C  CG   . PRO A 1 81  ? 36.53600 5.84000  8.11000   1.000 42.14758  ? 400 PRO A CG   1 
ATOM   1182 C  CD   . PRO A 1 81  ? 35.76700 6.15200  9.38200   1.000 41.93080  ? 400 PRO A CD   1 
ATOM   1183 H  HA   . PRO A 1 81  ? 33.69600 7.02700  7.08700   1.000 50.92664  ? 400 PRO A HA   1 
ATOM   1184 H  HB2  . PRO A 1 81  ? 35.91500 6.09700  6.13700   1.000 51.60687  ? 400 PRO A HB2  1 
ATOM   1185 H  HB3  . PRO A 1 81  ? 36.00100 7.45300  6.90300   1.000 51.60687  ? 400 PRO A HB3  1 
ATOM   1186 H  HG2  . PRO A 1 81  ? 36.59700 4.88300  7.96300   1.000 50.65409  ? 400 PRO A HG2  1 
ATOM   1187 H  HG3  . PRO A 1 81  ? 37.44400 6.17800  8.15800   1.000 50.65409  ? 400 PRO A HG3  1 
ATOM   1188 H  HD2  . PRO A 1 81  ? 35.77500 5.40300  9.99900   1.000 50.39396  ? 400 PRO A HD2  1 
ATOM   1189 H  HD3  . PRO A 1 81  ? 36.14600 6.91100  9.85300   1.000 50.39396  ? 400 PRO A HD3  1 
ATOM   1190 N  N    . ILE A 1 82  ? 33.32600 5.04300  5.67000   1.000 39.95166  ? 401 ILE A N    1 
ATOM   1191 C  CA   . ILE A 1 82  ? 33.05900 3.83200  4.91700   1.000 40.12679  ? 401 ILE A CA   1 
ATOM   1192 C  C    . ILE A 1 82  ? 33.79900 3.98000  3.59300   1.000 39.53628  ? 401 ILE A C    1 
ATOM   1193 O  O    . ILE A 1 82  ? 34.26100 5.06700  3.24900   1.000 42.55354  ? 401 ILE A O    1 
ATOM   1194 C  CB   . ILE A 1 82  ? 31.55600 3.58100  4.69100   1.000 43.37089  ? 401 ILE A CB   1 
ATOM   1195 C  CG1  . ILE A 1 82  ? 30.92700 4.65000  3.74900   1.000 41.71146  ? 401 ILE A CG1  1 
ATOM   1196 C  CG2  . ILE A 1 82  ? 30.79700 3.49700  6.01100   1.000 38.95520  ? 401 ILE A CG2  1 
ATOM   1197 C  CD1  . ILE A 1 82  ? 29.63900 4.22500  3.14200   1.000 37.58163  ? 401 ILE A CD1  1 
ATOM   1198 H  H    . ILE A 1 82  ? 33.19700 5.76500  5.22000   1.000 48.01900  ? 401 ILE A H    1 
ATOM   1199 H  HA   . ILE A 1 82  ? 33.36700 3.05900  5.41600   1.000 48.22915  ? 401 ILE A HA   1 
ATOM   1200 H  HB   . ILE A 1 82  ? 31.47600 2.72100  4.25000   1.000 52.12207  ? 401 ILE A HB   1 
ATOM   1201 H  HG12 . ILE A 1 82  ? 30.78500 5.46800  4.25000   1.000 50.13075  ? 401 ILE A HG12 1 
ATOM   1202 H  HG13 . ILE A 1 82  ? 31.55700 4.85700  3.04100   1.000 50.13075  ? 401 ILE A HG13 1 
ATOM   1203 H  HG21 . ILE A 1 82  ? 29.85600 3.33900  5.83400   1.000 46.82324  ? 401 ILE A HG21 1 
ATOM   1204 H  HG22 . ILE A 1 82  ? 31.15300 2.76800  6.54300   1.000 46.82324  ? 401 ILE A HG22 1 
ATOM   1205 H  HG23 . ILE A 1 82  ? 30.89900 4.33100  6.49700   1.000 46.82324  ? 401 ILE A HG23 1 
ATOM   1206 H  HD11 . ILE A 1 82  ? 29.30200 4.93200  2.57000   1.000 45.17495  ? 401 ILE A HD11 1 
ATOM   1207 H  HD12 . ILE A 1 82  ? 29.77800 3.42200  2.61600   1.000 45.17495  ? 401 ILE A HD12 1 
ATOM   1208 H  HD13 . ILE A 1 82  ? 28.99500 4.04300  3.84400   1.000 45.17495  ? 401 ILE A HD13 1 
ATOM   1209 N  N    . SER A 1 83  ? 33.90700 2.87100  2.86400   1.000 37.90575  ? 402 SER A N    1 
ATOM   1210 C  CA   . SER A 1 83  ? 34.43300 2.89700  1.51100   1.000 39.48070  ? 402 SER A CA   1 
ATOM   1211 C  C    . SER A 1 83  ? 33.26100 2.98200  0.54400   1.000 41.18871  ? 402 SER A C    1 
ATOM   1212 O  O    . SER A 1 83  ? 32.24500 2.31700  0.74100   1.000 38.47988  ? 402 SER A O    1 
ATOM   1213 C  CB   . SER A 1 83  ? 35.25500 1.65700  1.21500   1.000 41.71040  ? 402 SER A CB   1 
ATOM   1214 O  OG   . SER A 1 83  ? 36.33600 1.49200  2.12000   1.000 43.36567  ? 402 SER A OG   1 
ATOM   1215 H  H    . SER A 1 83  ? 33.67800 2.09000  3.14100   1.000 45.56390  ? 402 SER A H    1 
ATOM   1216 H  HA   . SER A 1 83  ? 35.01600 3.66600  1.41100   1.000 46.99185  ? 402 SER A HA   1 
ATOM   1217 H  HB2  . SER A 1 83  ? 34.68200 0.87600  1.25500   1.000 49.66749  ? 402 SER A HB2  1 
ATOM   1218 H  HB3  . SER A 1 83  ? 35.60000 1.71000  0.31000   1.000 49.66749  ? 402 SER A HB3  1 
ATOM   1219 H  HG   . SER A 1 83  ? 37.06100 1.63200  1.71900   1.000 52.11580  ? 402 SER A HG   1 
ATOM   1220 N  N    . VAL A 1 84  ? 33.42100 3.80000  -0.50000  1.000 44.77451  ? 403 VAL A N    1 
ATOM   1221 C  CA   . VAL A 1 84  ? 32.47100 3.83500  -1.59600  1.000 44.30026  ? 403 VAL A CA   1 
ATOM   1222 C  C    . VAL A 1 84  ? 33.20400 3.71100  -2.93100  1.000 47.12442  ? 403 VAL A C    1 
ATOM   1223 O  O    . VAL A 1 84  ? 34.31900 4.21100  -3.08700  1.000 49.22861  ? 403 VAL A O    1 
ATOM   1224 C  CB   . VAL A 1 84  ? 31.60500 5.10400  -1.52100  1.000 44.06017  ? 403 VAL A CB   1 
ATOM   1225 C  CG1  . VAL A 1 84  ? 30.75200 5.10400  -0.25000  1.000 43.78924  ? 403 VAL A CG1  1 
ATOM   1226 C  CG2  . VAL A 1 84  ? 32.45000 6.37200  -1.61400  1.000 45.40727  ? 403 VAL A CG2  1 
ATOM   1227 H  H    . VAL A 1 84  ? 34.08100 4.34400  -0.58600  1.000 53.80641  ? 403 VAL A H    1 
ATOM   1228 H  HA   . VAL A 1 84  ? 31.87000 3.07800  -1.52300  1.000 53.23731  ? 403 VAL A HA   1 
ATOM   1229 H  HB   . VAL A 1 84  ? 31.01000 5.09800  -2.28700  1.000 52.94921  ? 403 VAL A HB   1 
ATOM   1230 H  HG11 . VAL A 1 84  ? 30.21400 5.91100  -0.22100  1.000 52.62408  ? 403 VAL A HG11 1 
ATOM   1231 H  HG12 . VAL A 1 84  ? 30.17000 4.32800  -0.25000  1.000 52.62408  ? 403 VAL A HG12 1 
ATOM   1232 H  HG13 . VAL A 1 84  ? 31.33000 5.07400  0.52800   1.000 52.62408  ? 403 VAL A HG13 1 
ATOM   1233 H  HG21 . VAL A 1 84  ? 31.87300 7.15000  -1.56400  1.000 54.56572  ? 403 VAL A HG21 1 
ATOM   1234 H  HG22 . VAL A 1 84  ? 33.08500 6.39300  -0.88100  1.000 54.56572  ? 403 VAL A HG22 1 
ATOM   1235 H  HG23 . VAL A 1 84  ? 32.93000 6.38000  -2.45700  1.000 54.56572  ? 403 VAL A HG23 1 
ATOM   1236 N  N    . LEU A 1 85  ? 32.56800 2.99900  -3.86800  1.000 44.82208  ? 404 LEU A N    1 
ATOM   1237 C  CA   . LEU A 1 85  ? 32.97400 2.97900  -5.26300  1.000 48.74442  ? 404 LEU A CA   1 
ATOM   1238 C  C    . LEU A 1 85  ? 32.11400 4.01100  -5.98300  1.000 59.95059  ? 404 LEU A C    1 
ATOM   1239 O  O    . LEU A 1 85  ? 30.89100 3.88200  -6.00900  1.000 48.97636  ? 404 LEU A O    1 
ATOM   1240 C  CB   . LEU A 1 85  ? 32.77400 1.58200  -5.86000  1.000 49.45321  ? 404 LEU A CB   1 
ATOM   1241 C  CG   . LEU A 1 85  ? 33.16000 1.41400  -7.33000  1.000 52.87389  ? 404 LEU A CG   1 
ATOM   1242 C  CD1  . LEU A 1 85  ? 34.60900 1.79300  -7.56400  1.000 55.29153  ? 404 LEU A CD1  1 
ATOM   1243 C  CD2  . LEU A 1 85  ? 32.91100 -0.01500 -7.79700  1.000 54.51355  ? 404 LEU A CD2  1 
ATOM   1244 H  H    . LEU A 1 85  ? 31.88000 2.51000  -3.70100  1.000 53.40151  ? 404 LEU A H    1 
ATOM   1245 H  HA   . LEU A 1 85  ? 33.91500 3.19200  -5.35800  1.000 58.57030  ? 404 LEU A HA   1 
ATOM   1246 H  HB2  . LEU A 1 85  ? 33.29000 0.95000  -5.33500  1.000 58.95886  ? 404 LEU A HB2  1 
ATOM   1247 H  HB3  . LEU A 1 85  ? 31.84000 1.33900  -5.76000  1.000 58.95886  ? 404 LEU A HB3  1 
ATOM   1248 H  HG   . LEU A 1 85  ? 32.60000 2.01300  -7.84900  1.000 63.06368  ? 404 LEU A HG   1 
ATOM   1249 H  HD11 . LEU A 1 85  ? 34.82600 1.67700  -8.50200  1.000 66.42684  ? 404 LEU A HD11 1 
ATOM   1250 H  HD12 . LEU A 1 85  ? 34.74600 2.72000  -7.31300  1.000 66.42684  ? 404 LEU A HD12 1 
ATOM   1251 H  HD13 . LEU A 1 85  ? 35.18300 1.22500  -7.02700  1.000 66.42684  ? 404 LEU A HD13 1 
ATOM   1252 H  HD21 . LEU A 1 85  ? 33.16200 -0.09900 -8.73000  1.000 65.03128  ? 404 LEU A HD21 1 
ATOM   1253 H  HD22 . LEU A 1 85  ? 33.44200 -0.62700 -7.26300  1.000 65.03128  ? 404 LEU A HD22 1 
ATOM   1254 H  HD23 . LEU A 1 85  ? 31.97100 -0.23000 -7.69500  1.000 65.03128  ? 404 LEU A HD23 1 
ATOM   1255 N  N    . TYR A 1 86  ? 32.76300 5.04200  -6.53800  1.000 70.11856  ? 405 TYR A N    1 
ATOM   1256 C  CA   . TYR A 1 86  ? 32.05700 6.18100  -7.09900  1.000 79.37115  ? 405 TYR A CA   1 
ATOM   1257 C  C    . TYR A 1 86  ? 32.46800 6.45400  -8.54300  1.000 90.72925  ? 405 TYR A C    1 
ATOM   1258 O  O    . TYR A 1 86  ? 33.55600 6.06800  -8.97100  1.000 86.54062  ? 405 TYR A O    1 
ATOM   1259 C  CB   . TYR A 1 86  ? 32.29200 7.43900  -6.24700  1.000 72.80659  ? 405 TYR A CB   1 
ATOM   1260 C  CG   . TYR A 1 86  ? 33.67200 8.03500  -6.40200  1.000 96.87210  ? 405 TYR A CG   1 
ATOM   1261 C  CD1  . TYR A 1 86  ? 34.76900 7.47100  -5.76800  1.000 75.90999  ? 405 TYR A CD1  1 
ATOM   1262 C  CD2  . TYR A 1 86  ? 33.88400 9.14800  -7.20300  1.000 84.34887  ? 405 TYR A CD2  1 
ATOM   1263 C  CE1  . TYR A 1 86  ? 36.04300 8.00900  -5.91500  1.000 78.47801  ? 405 TYR A CE1  1 
ATOM   1264 C  CE2  . TYR A 1 86  ? 35.15100 9.69600  -7.35700  1.000 84.46882  ? 405 TYR A CE2  1 
ATOM   1265 C  CZ   . TYR A 1 86  ? 36.23000 9.12300  -6.71100  1.000 83.90900  ? 405 TYR A CZ   1 
ATOM   1266 O  OH   . TYR A 1 86  ? 37.48500 9.65700  -6.86100  1.000 91.97682  ? 405 TYR A OH   1 
ATOM   1267 H  H    . TYR A 1 86  ? 33.62000 5.09300  -6.59600  1.000 84.21927  ? 405 TYR A H    1 
ATOM   1268 H  HA   . TYR A 1 86  ? 31.11300 5.95900  -7.09300  1.000 95.32238  ? 405 TYR A HA   1 
ATOM   1269 H  HB2  . TYR A 1 86  ? 31.63200 8.10800  -6.48600  1.000 87.44490  ? 405 TYR A HB2  1 
ATOM   1270 H  HB3  . TYR A 1 86  ? 32.14800 7.21800  -5.31400  1.000 87.44490  ? 405 TYR A HB3  1 
ATOM   1271 H  HD1  . TYR A 1 86  ? 34.65000 6.71900  -5.23400  1.000 91.16899  ? 405 TYR A HD1  1 
ATOM   1272 H  HD2  . TYR A 1 86  ? 33.16300 9.53500  -7.64600  1.000 101.29564 ? 405 TYR A HD2  1 
ATOM   1273 H  HE1  . TYR A 1 86  ? 36.76700 7.62000  -5.47900  1.000 94.25061  ? 405 TYR A HE1  1 
ATOM   1274 H  HE2  . TYR A 1 86  ? 35.27300 10.44600 -7.89300  1.000 101.43958 ? 405 TYR A HE2  1 
ATOM   1275 H  HH   . TYR A 1 86  ? 38.06100 9.07700  -6.67000  1.000 110.44918 ? 405 TYR A HH   1 
ATOM   1276 N  N    . LYS A 1 87  ? 31.57000 7.12700  -9.27500  1.000 93.11202  ? 406 LYS A N    1 
ATOM   1277 C  CA   . LYS A 1 87  ? 31.81400 7.53100  -10.65000 1.000 100.75833 ? 406 LYS A CA   1 
ATOM   1278 C  C    . LYS A 1 87  ? 32.72400 8.75700  -10.70500 1.000 145.28929 ? 406 LYS A C    1 
ATOM   1279 O  O    . LYS A 1 87  ? 32.38500 9.80500  -10.15600 1.000 90.03772  ? 406 LYS A O    1 
ATOM   1280 C  CB   . LYS A 1 87  ? 30.49100 7.86400  -11.35900 1.000 81.67234  ? 406 LYS A CB   1 
ATOM   1281 C  CG   . LYS A 1 87  ? 29.56500 6.68100  -11.60000 1.000 113.32550 ? 406 LYS A CG   1 
ATOM   1282 C  CD   . LYS A 1 87  ? 28.35500 7.08600  -12.44600 1.000 87.14940  ? 406 LYS A CD   1 
ATOM   1283 C  CE   . LYS A 1 87  ? 27.40900 5.94500  -12.72300 1.000 124.73136 ? 406 LYS A CE   1 
ATOM   1284 N  NZ   . LYS A 1 87  ? 28.05100 4.87600  -13.53400 1.000 134.70404 ? 406 LYS A NZ   1 
ATOM   1285 H  H    . LYS A 1 87  ? 30.79800 7.36000  -8.97700  1.000 111.81142 ? 406 LYS A H    1 
ATOM   1286 H  HA   . LYS A 1 87  ? 32.24700 6.78900  -11.09900 1.000 120.98700 ? 406 LYS A HA   1 
ATOM   1287 H  HB2  . LYS A 1 87  ? 30.01600 8.52500  -10.83100 1.000 98.08380  ? 406 LYS A HB2  1 
ATOM   1288 H  HB3  . LYS A 1 87  ? 30.69400 8.27600  -12.21300 1.000 98.08380  ? 406 LYS A HB3  1 
ATOM   1289 H  HG2  . LYS A 1 87  ? 30.05200 5.97200  -12.04700 1.000 136.06760 ? 406 LYS A HG2  1 
ATOM   1290 H  HG3  . LYS A 1 87  ? 29.26300 6.32500  -10.75000 1.000 136.06760 ? 406 LYS A HG3  1 
ATOM   1291 H  HD2  . LYS A 1 87  ? 27.87300 7.79400  -11.99100 1.000 104.65628 ? 406 LYS A HD2  1 
ATOM   1292 H  HD3  . LYS A 1 87  ? 28.66600 7.45100  -13.28900 1.000 104.65628 ? 406 LYS A HD3  1 
ATOM   1293 H  HE2  . LYS A 1 87  ? 27.09900 5.57100  -11.88300 1.000 149.75463 ? 406 LYS A HE2  1 
ATOM   1294 H  HE3  . LYS A 1 87  ? 26.62700 6.28000  -13.19000 1.000 149.75463 ? 406 LYS A HE3  1 
ATOM   1295 H  HZ1  . LYS A 1 87  ? 27.54800 4.70100  -14.24700 1.000 161.72184 ? 406 LYS A HZ1  1 
ATOM   1296 H  HZ2  . LYS A 1 87  ? 28.85600 5.14700  -13.79900 1.000 161.72184 ? 406 LYS A HZ2  1 
ATOM   1297 H  HZ3  . LYS A 1 87  ? 28.13400 4.13900  -13.04200 1.000 161.72184 ? 406 LYS A HZ3  1 
ATOM   1298 N  N    . ASP A 1 88  ? 33.87200 8.61000  -11.38000 1.000 97.87127  ? 407 ASP A N    1 
ATOM   1299 C  CA   . ASP A 1 88  ? 34.79100 9.71300  -11.61800 1.000 116.56951 ? 407 ASP A CA   1 
ATOM   1300 C  C    . ASP A 1 88  ? 34.24000 10.63100 -12.70900 1.000 146.69904 ? 407 ASP A C    1 
ATOM   1301 O  O    . ASP A 1 88  ? 33.36000 10.23100 -13.46900 1.000 155.61622 ? 407 ASP A O    1 
ATOM   1302 C  CB   . ASP A 1 88  ? 36.16700 9.14700  -12.01600 1.000 105.75695 ? 407 ASP A CB   1 
ATOM   1303 C  CG   . ASP A 1 88  ? 37.29800 10.14900 -12.10800 1.000 132.85804 ? 407 ASP A CG   1 
ATOM   1304 O  OD1  . ASP A 1 88  ? 37.28000 10.98100 -13.03900 1.000 117.32368 ? 407 ASP A OD1  1 
ATOM   1305 O  OD2  . ASP A 1 88  ? 38.20600 10.09700 -11.25200 1.000 147.10187 ? 407 ASP A OD2  1 
ATOM   1306 H  H    . ASP A 1 88  ? 34.13400 7.86100  -11.71100 1.000 117.52252 ? 407 ASP A H    1 
ATOM   1307 H  HA   . ASP A 1 88  ? 34.89000 10.23800 -10.80900 1.000 139.96041 ? 407 ASP A HA   1 
ATOM   1308 H  HB2  . ASP A 1 88  ? 36.41500 8.46500  -11.37200 1.000 126.98534 ? 407 ASP A HB2  1 
ATOM   1309 H  HB3  . ASP A 1 88  ? 36.07900 8.70600  -12.87600 1.000 126.98534 ? 407 ASP A HB3  1 
ATOM   1310 N  N    . ASP A 1 89  ? 34.76900 11.86200 -12.78200 1.000 158.49811 ? 408 ASP A N    1 
ATOM   1311 C  CA   . ASP A 1 89  ? 34.45000 12.78500 -13.86300 1.000 124.22633 ? 408 ASP A CA   1 
ATOM   1312 C  C    . ASP A 1 89  ? 34.82800 12.22400 -15.23200 1.000 135.16734 ? 408 ASP A C    1 
ATOM   1313 O  O    . ASP A 1 89  ? 34.24900 12.61600 -16.24300 1.000 157.52963 ? 408 ASP A O    1 
ATOM   1314 C  CB   . ASP A 1 89  ? 35.15800 14.13800 -13.66300 1.000 111.59450 ? 408 ASP A CB   1 
ATOM   1315 C  CG   . ASP A 1 89  ? 34.66300 14.95800 -12.48900 1.000 148.33413 ? 408 ASP A CG   1 
ATOM   1316 O  OD1  . ASP A 1 89  ? 33.77400 14.47200 -11.75400 1.000 109.33942 ? 408 ASP A OD1  1 
ATOM   1317 O  OD2  . ASP A 1 89  ? 35.16400 16.08800 -12.30400 1.000 127.63115 ? 408 ASP A OD2  1 
ATOM   1318 H  H    . ASP A 1 89  ? 35.32100 12.17700 -12.20300 1.000 190.27473 ? 408 ASP A H    1 
ATOM   1319 H  HA   . ASP A 1 89  ? 33.48900 12.91200 -13.83700 1.000 149.14859 ? 408 ASP A HA   1 
ATOM   1320 H  HB2  . ASP A 1 89  ? 36.10800 13.97600 -13.54800 1.000 133.99040 ? 408 ASP A HB2  1 
ATOM   1321 H  HB3  . ASP A 1 89  ? 35.05500 14.66300 -14.47200 1.000 133.99040 ? 408 ASP A HB3  1 
ATOM   1322 N  N    . MET A 1 90  ? 35.80600 11.30900 -15.25000 1.000 136.43338 ? 409 MET A N    1 
ATOM   1323 C  CA   . MET A 1 90  ? 36.19900 10.59700 -16.45500 1.000 171.77423 ? 409 MET A CA   1 
ATOM   1324 C  C    . MET A 1 90  ? 35.27300 9.40600  -16.71700 1.000 194.16694 ? 409 MET A C    1 
ATOM   1325 O  O    . MET A 1 90  ? 35.47500 8.65700  -17.67100 1.000 194.36938 ? 409 MET A O    1 
ATOM   1326 C  CB   . MET A 1 90  ? 37.66900 10.14800 -16.29900 1.000 134.88749 ? 409 MET A CB   1 
ATOM   1327 C  CG   . MET A 1 90  ? 38.29100 9.51800  -17.54000 1.000 108.48862 ? 409 MET A CG   1 
ATOM   1328 S  SD   . MET A 1 90  ? 38.55900 10.71300 -18.87100 1.000 204.04597 ? 409 MET A SD   1 
ATOM   1329 C  CE   . MET A 1 90  ? 40.17300 11.31400 -18.42700 1.000 145.29811 ? 409 MET A CE   1 
ATOM   1330 H  H    . MET A 1 90  ? 36.25900 11.08800 -14.55300 1.000 163.79706 ? 409 MET A H    1 
ATOM   1331 H  HA   . MET A 1 90  ? 36.12200 11.18300 -17.22400 1.000 206.20607 ? 409 MET A HA   1 
ATOM   1332 H  HB2  . MET A 1 90  ? 38.20200 10.91700 -16.04300 1.000 161.94199 ? 409 MET A HB2  1 
ATOM   1333 H  HB3  . MET A 1 90  ? 37.72200 9.51100  -15.56900 1.000 161.94199 ? 409 MET A HB3  1 
ATOM   1334 H  HG2  . MET A 1 90  ? 39.13800 9.11100  -17.30100 1.000 130.26335 ? 409 MET A HG2  1 
ATOM   1335 H  HG3  . MET A 1 90  ? 37.71500 8.80700  -17.86000 1.000 130.26335 ? 409 MET A HG3  1 
ATOM   1336 H  HE1  . MET A 1 90  ? 40.45800 11.98200 -19.07000 1.000 174.43473 ? 409 MET A HE1  1 
ATOM   1337 H  HE2  . MET A 1 90  ? 40.13900 11.71100 -17.54200 1.000 174.43473 ? 409 MET A HE2  1 
ATOM   1338 H  HE3  . MET A 1 90  ? 40.80400 10.57700 -18.42600 1.000 174.43473 ? 409 MET A HE3  1 
ATOM   1339 N  N    . GLY A 1 91  ? 34.24500 9.24400  -15.87200 1.000 179.43213 ? 410 GLY A N    1 
ATOM   1340 C  CA   . GLY A 1 91  ? 33.26200 8.18500  -16.03200 1.000 160.69728 ? 410 GLY A CA   1 
ATOM   1341 C  C    . GLY A 1 91  ? 33.82100 6.79600  -15.73500 1.000 145.68211 ? 410 GLY A C    1 
ATOM   1342 O  O    . GLY A 1 91  ? 33.43600 5.82100  -16.37800 1.000 167.58637 ? 410 GLY A O    1 
ATOM   1343 H  H    . GLY A 1 91  ? 34.10600 9.75100  -15.19100 1.000 215.39555 ? 410 GLY A H    1 
ATOM   1344 H  HA2  . GLY A 1 91  ? 32.51100 8.35800  -15.44300 1.000 192.91373 ? 410 GLY A HA2  1 
ATOM   1345 H  HA3  . GLY A 1 91  ? 32.92100 8.20300  -16.94000 1.000 192.91373 ? 410 GLY A HA3  1 
ATOM   1346 N  N    . VAL A 1 92  ? 34.72700 6.72600  -14.75200 1.000 117.39218 ? 411 VAL A N    1 
ATOM   1347 C  CA   . VAL A 1 92  ? 35.38100 5.48200  -14.37800 1.000 132.03698 ? 411 VAL A CA   1 
ATOM   1348 C  C    . VAL A 1 92  ? 35.14200 5.22500  -12.89200 1.000 125.95866 ? 411 VAL A C    1 
ATOM   1349 O  O    . VAL A 1 92  ? 35.29300 6.13000  -12.07400 1.000 95.21202  ? 411 VAL A O    1 
ATOM   1350 C  CB   . VAL A 1 92  ? 36.89600 5.48200  -14.73600 1.000 99.06683  ? 411 VAL A CB   1 
ATOM   1351 C  CG1  . VAL A 1 92  ? 37.12500 5.56900  -16.24200 1.000 133.84050 ? 411 VAL A CG1  1 
ATOM   1352 C  CG2  . VAL A 1 92  ? 37.64400 6.59800  -14.00600 1.000 93.57134  ? 411 VAL A CG2  1 
ATOM   1353 H  H    . VAL A 1 92  ? 34.97500 7.40500  -14.28600 1.000 140.94761 ? 411 VAL A H    1 
ATOM   1354 H  HA   . VAL A 1 92  ? 34.99300 4.75600  -14.89200 1.000 158.52137 ? 411 VAL A HA   1 
ATOM   1355 H  HB   . VAL A 1 92  ? 37.25600 4.63300  -14.43400 1.000 118.95719 ? 411 VAL A HB   1 
ATOM   1356 H  HG11 . VAL A 1 92  ? 38.07800 5.56700  -16.42500 1.000 160.68559 ? 411 VAL A HG11 1 
ATOM   1357 H  HG12 . VAL A 1 92  ? 36.71000 4.80800  -16.67700 1.000 160.68559 ? 411 VAL A HG12 1 
ATOM   1358 H  HG13 . VAL A 1 92  ? 36.73300 6.38800  -16.58200 1.000 160.68559 ? 411 VAL A HG13 1 
ATOM   1359 H  HG21 . VAL A 1 92  ? 38.58300 6.57200  -14.24900 1.000 112.36260 ? 411 VAL A HG21 1 
ATOM   1360 H  HG22 . VAL A 1 92  ? 37.26900 7.45700  -14.25700 1.000 112.36260 ? 411 VAL A HG22 1 
ATOM   1361 H  HG23 . VAL A 1 92  ? 37.55500 6.47500  -13.04800 1.000 112.36260 ? 411 VAL A HG23 1 
ATOM   1362 N  N    . PRO A 1 93  ? 34.72900 3.99400  -12.50300 1.000 112.03696 ? 412 PRO A N    1 
ATOM   1363 C  CA   . PRO A 1 93  ? 34.63900 3.63200  -11.09300 1.000 113.68217 ? 412 PRO A CA   1 
ATOM   1364 C  C    . PRO A 1 93  ? 35.96500 3.78200  -10.35300 1.000 99.96508  ? 412 PRO A C    1 
ATOM   1365 O  O    . PRO A 1 93  ? 36.97000 3.20100  -10.75900 1.000 79.36654  ? 412 PRO A O    1 
ATOM   1366 C  CB   . PRO A 1 93  ? 34.18200 2.16600  -11.12700 1.000 102.33636 ? 412 PRO A CB   1 
ATOM   1367 C  CG   . PRO A 1 93  ? 33.57100 1.97500  -12.48600 1.000 148.90485 ? 412 PRO A CG   1 
ATOM   1368 C  CD   . PRO A 1 93  ? 34.29600 2.91200  -13.40400 1.000 133.60052 ? 412 PRO A CD   1 
ATOM   1369 H  HA   . PRO A 1 93  ? 34.03200 4.21500  -10.61000 1.000 136.49561 ? 412 PRO A HA   1 
ATOM   1370 H  HB2  . PRO A 1 93  ? 34.92900 1.56300  -10.99100 1.000 122.88063 ? 412 PRO A HB2  1 
ATOM   1371 H  HB3  . PRO A 1 93  ? 33.53800 1.98300  -10.42500 1.000 122.88063 ? 412 PRO A HB3  1 
ATOM   1372 H  HG2  . PRO A 1 93  ? 33.66600 1.05600  -12.78300 1.000 178.76282 ? 412 PRO A HG2  1 
ATOM   1373 H  HG3  . PRO A 1 93  ? 32.62100 2.17100  -12.47000 1.000 178.76282 ? 412 PRO A HG3  1 
ATOM   1374 H  HD2  . PRO A 1 93  ? 35.05000 2.48000  -13.83500 1.000 160.39762 ? 412 PRO A HD2  1 
ATOM   1375 H  HD3  . PRO A 1 93  ? 33.71800 3.24200  -14.10900 1.000 160.39762 ? 412 PRO A HD3  1 
ATOM   1376 N  N    . THR A 1 94  ? 35.94700 4.58200  -9.28000  1.000 88.06003  ? 413 THR A N    1 
ATOM   1377 C  CA   . THR A 1 94  ? 37.11400 4.79900  -8.44100  1.000 74.40930  ? 413 THR A CA   1 
ATOM   1378 C  C    . THR A 1 94  ? 36.74800 4.50300  -6.98900  1.000 65.86575  ? 413 THR A C    1 
ATOM   1379 O  O    . THR A 1 94  ? 35.64400 4.81600  -6.55400  1.000 64.22007  ? 413 THR A O    1 
ATOM   1380 C  CB   . THR A 1 94  ? 37.62200 6.22800  -8.61900  1.000 77.55620  ? 413 THR A CB   1 
ATOM   1381 O  OG1  . THR A 1 94  ? 37.99600 6.41600  -9.98200  1.000 133.56991 ? 413 THR A OG1  1 
ATOM   1382 C  CG2  . THR A 1 94  ? 38.80400 6.54400  -7.72100  1.000 72.91879  ? 413 THR A CG2  1 
ATOM   1383 H  H    . THR A 1 94  ? 35.24900 5.01300  -9.02300  1.000 105.74903 ? 413 THR A H    1 
ATOM   1384 H  HA   . THR A 1 94  ? 37.83100 4.20000  -8.70100  1.000 89.36815  ? 413 THR A HA   1 
ATOM   1385 H  HB   . THR A 1 94  ? 36.90500 6.83100  -8.36800  1.000 93.14443  ? 413 THR A HB   1 
ATOM   1386 H  HG1  . THR A 1 94  ? 37.30600 6.46300  -10.45800 1.000 160.36088 ? 413 THR A HG1  1 
ATOM   1387 H  HG21 . THR A 1 94  ? 39.08900 7.45900  -7.87100  1.000 87.57955  ? 413 THR A HG21 1 
ATOM   1388 H  HG22 . THR A 1 94  ? 38.54400 6.43400  -6.79300  1.000 87.57955  ? 413 THR A HG22 1 
ATOM   1389 H  HG23 . THR A 1 94  ? 39.53600 5.94100  -7.92500  1.000 87.57955  ? 413 THR A HG23 1 
ATOM   1390 N  N    . LEU A 1 95  ? 37.67900 3.88500  -6.25400  1.000 55.04256  ? 414 LEU A N    1 
ATOM   1391 C  CA   . LEU A 1 95  ? 37.48800 3.62400  -4.83800  1.000 54.03116  ? 414 LEU A CA   1 
ATOM   1392 C  C    . LEU A 1 95  ? 37.82300 4.86500  -4.01700  1.000 50.00516  ? 414 LEU A C    1 
ATOM   1393 O  O    . LEU A 1 95  ? 38.87300 5.47200  -4.20600  1.000 57.91749  ? 414 LEU A O    1 
ATOM   1394 C  CB   . LEU A 1 95  ? 38.36800 2.45800  -4.36800  1.000 48.93301  ? 414 LEU A CB   1 
ATOM   1395 C  CG   . LEU A 1 95  ? 38.21500 2.10000  -2.88100  1.000 51.07362  ? 414 LEU A CG   1 
ATOM   1396 C  CD1  . LEU A 1 95  ? 36.87400 1.46200  -2.61800  1.000 46.67790  ? 414 LEU A CD1  1 
ATOM   1397 C  CD2  . LEU A 1 95  ? 39.33900 1.18900  -2.41600  1.000 50.94192  ? 414 LEU A CD2  1 
ATOM   1398 H  H    . LEU A 1 95  ? 38.43100 3.61000  -6.56700  1.000 66.12807  ? 414 LEU A H    1 
ATOM   1399 H  HA   . LEU A 1 95  ? 36.55600 3.38900  -4.70700  1.000 64.91438  ? 414 LEU A HA   1 
ATOM   1400 H  HB2  . LEU A 1 95  ? 38.15800 1.67500  -4.90000  1.000 58.79661  ? 414 LEU A HB2  1 
ATOM   1401 H  HB3  . LEU A 1 95  ? 39.29700 2.67900  -4.54200  1.000 58.79661  ? 414 LEU A HB3  1 
ATOM   1402 H  HG   . LEU A 1 95  ? 38.26700 2.92400  -2.37300  1.000 61.36534  ? 414 LEU A HG   1 
ATOM   1403 H  HD11 . LEU A 1 95  ? 36.79800 1.24400  -1.67600  1.000 56.09047  ? 414 LEU A HD11 1 
ATOM   1404 H  HD12 . LEU A 1 95  ? 36.16800 2.07900  -2.86500  1.000 56.09047  ? 414 LEU A HD12 1 
ATOM   1405 H  HD13 . LEU A 1 95  ? 36.79200 0.65100  -3.14400  1.000 56.09047  ? 414 LEU A HD13 1 
ATOM   1406 H  HD21 . LEU A 1 95  ? 39.21800 0.97900  -1.47700  1.000 61.20730  ? 414 LEU A HD21 1 
ATOM   1407 H  HD22 . LEU A 1 95  ? 39.32700 0.36900  -2.93400  1.000 61.20730  ? 414 LEU A HD22 1 
ATOM   1408 H  HD23 . LEU A 1 95  ? 40.19100 1.63600  -2.54000  1.000 61.20730  ? 414 LEU A HD23 1 
ATOM   1409 N  N    . LYS A 1 96  ? 36.91500 5.23000  -3.10800  1.000 51.20446  ? 415 LYS A N    1 
ATOM   1410 C  CA   . LYS A 1 96  ? 37.20200 6.22300  -2.08800  1.000 44.81483  ? 415 LYS A CA   1 
ATOM   1411 C  C    . LYS A 1 96  ? 37.31400 5.47200  -0.76100  1.000 46.27377  ? 415 LYS A C    1 
ATOM   1412 O  O    . LYS A 1 96  ? 36.31300 5.12000  -0.15100  1.000 49.93144  ? 415 LYS A O    1 
ATOM   1413 C  CB   . LYS A 1 96  ? 36.11600 7.30200  -2.08800  1.000 46.50136  ? 415 LYS A CB   1 
ATOM   1414 C  CG   . LYS A 1 96  ? 36.21900 8.31000  -0.96300  1.000 54.29396  ? 415 LYS A CG   1 
ATOM   1415 C  CD   . LYS A 1 96  ? 37.57700 8.97600  -0.86900  1.000 58.47827  ? 415 LYS A CD   1 
ATOM   1416 C  CE   . LYS A 1 96  ? 37.61800 9.94800  0.27500   1.000 57.08760  ? 415 LYS A CE   1 
ATOM   1417 N  NZ   . LYS A 1 96  ? 39.00200 10.37000 0.58100   1.000 68.19183  ? 415 LYS A NZ   1 
ATOM   1418 H  H    . LYS A 1 96  ? 36.11900 4.90600  -3.07100  1.000 61.52235  ? 415 LYS A H    1 
ATOM   1419 H  HA   . LYS A 1 96  ? 38.03500 6.69300  -2.25300  1.000 53.85479  ? 415 LYS A HA   1 
ATOM   1420 H  HB2  . LYS A 1 96  ? 36.14900 7.77600  -2.93400  1.000 55.87863  ? 415 LYS A HB2  1 
ATOM   1421 H  HB3  . LYS A 1 96  ? 35.24900 6.87000  -2.03900  1.000 55.87863  ? 415 LYS A HB3  1 
ATOM   1422 H  HG2  . LYS A 1 96  ? 35.54000 8.99200  -1.08700  1.000 65.22974  ? 415 LYS A HG2  1 
ATOM   1423 H  HG3  . LYS A 1 96  ? 36.02600 7.86600  -0.12200  1.000 65.22974  ? 415 LYS A HG3  1 
ATOM   1424 H  HD2  . LYS A 1 96  ? 38.26500 8.30200  -0.75100  1.000 70.25092  ? 415 LYS A HD2  1 
ATOM   1425 H  HD3  . LYS A 1 96  ? 37.77300 9.43900  -1.69900  1.000 70.25092  ? 415 LYS A HD3  1 
ATOM   1426 H  HE2  . LYS A 1 96  ? 37.08200 10.72700 0.05800   1.000 68.58212  ? 415 LYS A HE2  1 
ATOM   1427 H  HE3  . LYS A 1 96  ? 37.22200 9.54100  1.06100   1.000 68.58212  ? 415 LYS A HE3  1 
ATOM   1428 H  HZ1  . LYS A 1 96  ? 39.04300 10.66900 1.41800   1.000 81.90719  ? 415 LYS A HZ1  1 
ATOM   1429 H  HZ2  . LYS A 1 96  ? 39.55200 9.67600  0.48700   1.000 81.90719  ? 415 LYS A HZ2  1 
ATOM   1430 H  HZ3  . LYS A 1 96  ? 39.24500 11.01900 0.02200   1.000 81.90719  ? 415 LYS A HZ3  1 
ATOM   1431 N  N    . TYR A 1 97  ? 38.54800 5.20500  -0.33100  1.000 42.02319  ? 416 TYR A N    1 
ATOM   1432 C  CA   . TYR A 1 97  ? 38.77900 4.19000  0.68200   1.000 44.12881  ? 416 TYR A CA   1 
ATOM   1433 C  C    . TYR A 1 97  ? 38.22500 4.61300  2.04100   1.000 39.19826  ? 416 TYR A C    1 
ATOM   1434 O  O    . TYR A 1 97  ? 37.48000 3.85600  2.65000   1.000 42.70594  ? 416 TYR A O    1 
ATOM   1435 C  CB   . TYR A 1 97  ? 40.25700 3.84100  0.76000   1.000 43.50083  ? 416 TYR A CB   1 
ATOM   1436 C  CG   . TYR A 1 97  ? 40.54800 2.68700  1.68800   1.000 43.66700  ? 416 TYR A CG   1 
ATOM   1437 C  CD1  . TYR A 1 97  ? 39.94700 1.44700  1.50200   1.000 43.59896  ? 416 TYR A CD1  1 
ATOM   1438 C  CD2  . TYR A 1 97  ? 41.42700 2.82900  2.74700   1.000 44.49436  ? 416 TYR A CD2  1 
ATOM   1439 C  CE1  . TYR A 1 97  ? 40.21600 0.37900  2.34900   1.000 44.38543  ? 416 TYR A CE1  1 
ATOM   1440 C  CE2  . TYR A 1 97  ? 41.70400 1.77100  3.60000   1.000 47.49139  ? 416 TYR A CE2  1 
ATOM   1441 C  CZ   . TYR A 1 97  ? 41.09900 0.54300  3.39700   1.000 45.28109  ? 416 TYR A CZ   1 
ATOM   1442 O  OH   . TYR A 1 97  ? 41.35700 -0.49800 4.25100   1.000 46.64189  ? 416 TYR A OH   1 
ATOM   1443 H  H    . TYR A 1 97  ? 39.25700 5.60000  -0.61400  1.000 50.04284  ? 416 TYR A H    1 
ATOM   1444 H  HA   . TYR A 1 97  ? 38.29600 3.39000  0.42100   1.000 53.03157  ? 416 TYR A HA   1 
ATOM   1445 H  HB2  . TYR A 1 97  ? 40.57900 3.62300  -0.12900  1.000 51.81601  ? 416 TYR A HB2  1 
ATOM   1446 H  HB3  . TYR A 1 97  ? 40.75200 4.62000  1.05800   1.000 51.81601  ? 416 TYR A HB3  1 
ATOM   1447 H  HD1  . TYR A 1 97  ? 39.35300 1.33000  0.79600   1.000 51.93376  ? 416 TYR A HD1  1 
ATOM   1448 H  HD2  . TYR A 1 97  ? 41.84000 3.65000  2.89000   1.000 53.00825  ? 416 TYR A HD2  1 
ATOM   1449 H  HE1  . TYR A 1 97  ? 39.80300 -0.44300 2.21000   1.000 52.87753  ? 416 TYR A HE1  1 
ATOM   1450 H  HE2  . TYR A 1 97  ? 42.29600 1.88700  4.30800   1.000 57.06667  ? 416 TYR A HE2  1 
ATOM   1451 H  HH   . TYR A 1 97  ? 41.83000 -0.22600 4.89000   1.000 55.58528  ? 416 TYR A HH   1 
ATOM   1452 N  N    . HIS A 1 98  ? 38.55800 5.83100  2.48100   1.000 42.00103  ? 417 HIS A N    1 
ATOM   1453 C  CA   . HIS A 1 98  ? 37.95600 6.41400  3.67200   1.000 39.35398  ? 417 HIS A CA   1 
ATOM   1454 C  C    . HIS A 1 98  ? 37.08500 7.62900  3.34700   1.000 45.09833  ? 417 HIS A C    1 
ATOM   1455 O  O    . HIS A 1 98  ? 37.54600 8.76800  3.40300   1.000 48.57721  ? 417 HIS A O    1 
ATOM   1456 C  CB   . HIS A 1 98  ? 39.03100 6.81500  4.69800   1.000 40.30269  ? 417 HIS A CB   1 
ATOM   1457 C  CG   . HIS A 1 98  ? 39.86700 5.67900  5.20800   1.000 45.68581  ? 417 HIS A CG   1 
ATOM   1458 N  ND1  . HIS A 1 98  ? 39.29700 4.53600  5.73300   1.000 40.79987  ? 417 HIS A ND1  1 
ATOM   1459 C  CD2  . HIS A 1 98  ? 41.21200 5.55100  5.24900   1.000 46.10078  ? 417 HIS A CD2  1 
ATOM   1460 C  CE1  . HIS A 1 98  ? 40.30900 3.75200  6.07900   1.000 47.87573  ? 417 HIS A CE1  1 
ATOM   1461 N  NE2  . HIS A 1 98  ? 41.48100 4.32900  5.80200   1.000 44.97935  ? 417 HIS A NE2  1 
ATOM   1462 H  H    . HIS A 1 98  ? 39.13700 6.33600  2.09500   1.000 50.47823  ? 417 HIS A H    1 
ATOM   1463 H  HA   . HIS A 1 98  ? 37.38700 5.72700  4.05400   1.000 47.30178  ? 417 HIS A HA   1 
ATOM   1464 H  HB2  . HIS A 1 98  ? 39.61600 7.47500  4.29400   1.000 48.44023  ? 417 HIS A HB2  1 
ATOM   1465 H  HB3  . HIS A 1 98  ? 38.59700 7.24500  5.45200   1.000 48.44023  ? 417 HIS A HB3  1 
ATOM   1466 H  HD1  . HIS A 1 98  ? 38.45800 4.36700  5.81800   1.000 49.03684  ? 417 HIS A HD1  1 
ATOM   1467 H  HD2  . HIS A 1 98  ? 41.83600 6.17500  4.95700   1.000 55.39794  ? 417 HIS A HD2  1 
ATOM   1468 H  HE1  . HIS A 1 98  ? 40.21500 2.91100  6.46400   1.000 57.52788  ? 417 HIS A HE1  1 
ATOM   1469 N  N    . TYR A 1 99  ? 35.80900 7.37300  3.04500   1.000 39.14858  ? 418 TYR A N    1 
ATOM   1470 C  CA   . TYR A 1 99  ? 34.83200 8.43400  2.85300   1.000 41.07109  ? 418 TYR A CA   1 
ATOM   1471 C  C    . TYR A 1 99  ? 34.31000 8.84300  4.22700   1.000 35.70675  ? 418 TYR A C    1 
ATOM   1472 O  O    . TYR A 1 99  ? 33.44300 8.17500  4.78600   1.000 35.71043  ? 418 TYR A O    1 
ATOM   1473 C  CB   . TYR A 1 99  ? 33.70500 7.96000  1.92300   1.000 35.52091  ? 418 TYR A CB   1 
ATOM   1474 C  CG   . TYR A 1 99  ? 32.88800 9.07600  1.30800   1.000 46.16058  ? 418 TYR A CG   1 
ATOM   1475 C  CD1  . TYR A 1 99  ? 33.49800 10.10000 0.59600   1.000 58.23708  ? 418 TYR A CD1  1 
ATOM   1476 C  CD2  . TYR A 1 99  ? 31.50400 9.09100  1.41100   1.000 46.23881  ? 418 TYR A CD2  1 
ATOM   1477 C  CE1  . TYR A 1 99  ? 32.75200 11.11900 0.01300   1.000 131.47701 ? 418 TYR A CE1  1 
ATOM   1478 C  CE2  . TYR A 1 99  ? 30.74700 10.10800 0.83800   1.000 48.91882  ? 418 TYR A CE2  1 
ATOM   1479 C  CZ   . TYR A 1 99  ? 31.37500 11.12200 0.14100   1.000 57.45168  ? 418 TYR A CZ   1 
ATOM   1480 O  OH   . TYR A 1 99  ? 30.64400 12.13200 -0.43600  1.000 62.89372  ? 418 TYR A OH   1 
ATOM   1481 H  H    . TYR A 1 99  ? 35.49200 6.58000  2.94700   1.000 47.05530  ? 418 TYR A H    1 
ATOM   1482 H  HA   . TYR A 1 99  ? 35.23700 9.20500  2.42500   1.000 49.36231  ? 418 TYR A HA   1 
ATOM   1483 H  HB2  . TYR A 1 99  ? 34.09200 7.42700  1.21100   1.000 42.70209  ? 418 TYR A HB2  1 
ATOM   1484 H  HB3  . TYR A 1 99  ? 33.11200 7.37800  2.42300   1.000 42.70209  ? 418 TYR A HB3  1 
ATOM   1485 H  HD1  . TYR A 1 99  ? 34.42400 10.10500 0.50700   1.000 69.96150  ? 418 TYR A HD1  1 
ATOM   1486 H  HD2  . TYR A 1 99  ? 31.07400 8.40700  1.87200   1.000 55.56357  ? 418 TYR A HD2  1 
ATOM   1487 H  HE1  . TYR A 1 99  ? 33.17800 11.79600 -0.46100  1.000 157.84940 ? 418 TYR A HE1  1 
ATOM   1488 H  HE2  . TYR A 1 99  ? 29.82100 10.10500 0.92400   1.000 58.77959  ? 418 TYR A HE2  1 
ATOM   1489 H  HH   . TYR A 1 99  ? 29.87600 11.84900 -0.62600  1.000 75.54946  ? 418 TYR A HH   1 
ATOM   1490 N  N    . GLU A 1 100 ? 34.85300 9.94600  4.75600   1.000 44.93721  ? 419 GLU A N    1 
ATOM   1491 C  CA   . GLU A 1 100 ? 34.72100 10.27900 6.16400   1.000 43.84773  ? 419 GLU A CA   1 
ATOM   1492 C  C    . GLU A 1 100 ? 33.33300 10.77700 6.56300   1.000 37.60817  ? 419 GLU A C    1 
ATOM   1493 O  O    . GLU A 1 100 ? 32.63100 11.42600 5.79000   1.000 34.98307  ? 419 GLU A O    1 
ATOM   1494 C  CB   . GLU A 1 100 ? 35.76300 11.34400 6.54600   1.000 52.85333  ? 419 GLU A CB   1 
ATOM   1495 C  CG   . GLU A 1 100 ? 37.20700 10.91200 6.33000   1.000 56.88522  ? 419 GLU A CG   1 
ATOM   1496 C  CD   . GLU A 1 100 ? 37.74600 9.87700  7.30300   1.000 69.44903  ? 419 GLU A CD   1 
ATOM   1497 O  OE1  . GLU A 1 100 ? 37.08100 9.60200  8.32900   1.000 54.97623  ? 419 GLU A OE1  1 
ATOM   1498 O  OE2  . GLU A 1 100 ? 38.84500 9.33900  7.03400   1.000 60.72460  ? 419 GLU A OE2  1 
ATOM   1499 H  H    . GLU A 1 100 ? 35.30700 10.51800 4.30100   1.000 54.00165  ? 419 GLU A H    1 
ATOM   1500 H  HA   . GLU A 1 100 ? 34.86800 9.45100  6.64600   1.000 52.69427  ? 419 GLU A HA   1 
ATOM   1501 H  HB2  . GLU A 1 100 ? 35.59500 12.14600 6.02700   1.000 63.50099  ? 419 GLU A HB2  1 
ATOM   1502 H  HB3  . GLU A 1 100 ? 35.64300 11.57900 7.47900   1.000 63.50099  ? 419 GLU A HB3  1 
ATOM   1503 H  HG2  . GLU A 1 100 ? 37.28900 10.55800 5.43100   1.000 68.33926  ? 419 GLU A HG2  1 
ATOM   1504 H  HG3  . GLU A 1 100 ? 37.77200 11.69900 6.37700   1.000 68.33926  ? 419 GLU A HG3  1 
ATOM   1505 N  N    . GLY A 1 101 ? 32.94500 10.44000 7.79200   1.000 30.86052  ? 420 GLY A N    1 
ATOM   1506 C  CA   . GLY A 1 101 ? 31.80600 11.05700 8.44500   1.000 36.23396  ? 420 GLY A CA   1 
ATOM   1507 C  C    . GLY A 1 101 ? 30.47800 10.38900 8.11600   1.000 30.78315  ? 420 GLY A C    1 
ATOM   1508 O  O    . GLY A 1 101 ? 29.43100 11.00900 8.26900   1.000 35.95693  ? 420 GLY A O    1 
ATOM   1509 H  H    . GLY A 1 101 ? 33.34100 9.84300  8.26800   1.000 37.10962  ? 420 GLY A H    1 
ATOM   1510 H  HA2  . GLY A 1 101 ? 31.94200 11.03400 9.40500   1.000 43.55775  ? 420 GLY A HA2  1 
ATOM   1511 H  HA3  . GLY A 1 101 ? 31.76200 11.99100 8.18700   1.000 43.55775  ? 420 GLY A HA3  1 
ATOM   1512 N  N    . MET A 1 102 ? 30.53000 9.12500  7.68200   1.000 32.42769  ? 421 MET A N    1 
ATOM   1513 C  CA   . MET A 1 102 ? 29.35600 8.46300  7.14000   1.000 32.15441  ? 421 MET A CA   1 
ATOM   1514 C  C    . MET A 1 102 ? 28.56000 7.61900  8.13600   1.000 34.12642  ? 421 MET A C    1 
ATOM   1515 O  O    . MET A 1 102 ? 27.37100 7.38700  7.92800   1.000 32.35811  ? 421 MET A O    1 
ATOM   1516 C  CB   . MET A 1 102 ? 29.79100 7.60400  5.95400   1.000 28.75655  ? 421 MET A CB   1 
ATOM   1517 C  CG   . MET A 1 102 ? 30.14300 8.43900  4.74400   1.000 29.99516  ? 421 MET A CG   1 
ATOM   1518 S  SD   . MET A 1 102 ? 28.74000 9.30400  4.05500   1.000 34.51778  ? 421 MET A SD   1 
ATOM   1519 C  CE   . MET A 1 102 ? 27.91700 7.99100  3.21500   1.000 32.10470  ? 421 MET A CE   1 
ATOM   1520 H  H    . MET A 1 102 ? 31.24000 8.63900  7.69600   1.000 38.99022  ? 421 MET A H    1 
ATOM   1521 H  HA   . MET A 1 102 ? 28.74400 9.16700  6.87500   1.000 38.66229  ? 421 MET A HA   1 
ATOM   1522 H  HB2  . MET A 1 102 ? 30.55800 7.06800  6.20900   1.000 34.24765  ? 421 MET A HB2  1 
ATOM   1523 H  HB3  . MET A 1 102 ? 29.07800 6.98800  5.72400   1.000 34.24765  ? 421 MET A HB3  1 
ATOM   1524 H  HG2  . MET A 1 102 ? 30.82400 9.08400  4.99000   1.000 35.81444  ? 421 MET A HG2  1 
ATOM   1525 H  HG3  . MET A 1 102 ? 30.52800 7.86500  4.06300   1.000 35.81444  ? 421 MET A HG3  1 
ATOM   1526 H  HE1  . MET A 1 102 ? 27.11700 8.33200  2.78600   1.000 38.60264  ? 421 MET A HE1  1 
ATOM   1527 H  HE2  . MET A 1 102 ? 28.50800 7.61500  2.54400   1.000 38.60264  ? 421 MET A HE2  1 
ATOM   1528 H  HE3  . MET A 1 102 ? 27.67200 7.30200  3.85200   1.000 38.60264  ? 421 MET A HE3  1 
ATOM   1529 N  N    . SER A 1 103 ? 29.20600 7.18800  9.22300   1.000 33.65054  ? 422 SER A N    1 
ATOM   1530 C  CA   . SER A 1 103 ? 28.60800 6.24400  10.15200  1.000 34.33878  ? 422 SER A CA   1 
ATOM   1531 C  C    . SER A 1 103 ? 28.85300 6.68300  11.59500  1.000 34.38100  ? 422 SER A C    1 
ATOM   1532 O  O    . SER A 1 103 ? 29.93800 7.16100  11.91300  1.000 32.35582  ? 422 SER A O    1 
ATOM   1533 C  CB   . SER A 1 103 ? 29.19500 4.85700  9.90900   1.000 36.94044  ? 422 SER A CB   1 
ATOM   1534 O  OG   . SER A 1 103 ? 28.46500 3.85400  10.59500  1.000 37.51912  ? 422 SER A OG   1 
ATOM   1535 H  H    . SER A 1 103 ? 30.00100 7.43800  9.43700   1.000 40.45765  ? 422 SER A H    1 
ATOM   1536 H  HA   . SER A 1 103 ? 27.64900 6.21600  10.00600  1.000 41.28353  ? 422 SER A HA   1 
ATOM   1537 H  HB2  . SER A 1 103 ? 29.19300 4.66600  8.95800   1.000 44.40553  ? 422 SER A HB2  1 
ATOM   1538 H  HB3  . SER A 1 103 ? 30.12000 4.84100  10.20000  1.000 44.40553  ? 422 SER A HB3  1 
ATOM   1539 H  HG   . SER A 1 103 ? 28.01800 4.20600  11.21300  1.000 45.09994  ? 422 SER A HG   1 
ATOM   1540 N  N    . VAL A 1 104 ? 27.84700 6.51300  12.46200  1.000 30.35659  ? 423 VAL A N    1 
ATOM   1541 C  CA   . VAL A 1 104 ? 27.95300 6.94500  13.84900  1.000 31.37227  ? 423 VAL A CA   1 
ATOM   1542 C  C    . VAL A 1 104 ? 28.84100 5.98400  14.62800  1.000 28.95773  ? 423 VAL A C    1 
ATOM   1543 O  O    . VAL A 1 104 ? 28.60200 4.78000  14.59600  1.000 36.87925  ? 423 VAL A O    1 
ATOM   1544 C  CB   . VAL A 1 104 ? 26.58400 7.04300  14.54500  1.000 35.22758  ? 423 VAL A CB   1 
ATOM   1545 C  CG1  . VAL A 1 104 ? 26.73800 7.43000  16.02400  1.000 28.86943  ? 423 VAL A CG1  1 
ATOM   1546 C  CG2  . VAL A 1 104 ? 25.66600 8.01600  13.81800  1.000 28.76486  ? 423 VAL A CG2  1 
ATOM   1547 H  H    . VAL A 1 104 ? 27.09500 6.14800  12.26000  1.000 36.50491  ? 423 VAL A H    1 
ATOM   1548 H  HA   . VAL A 1 104 ? 28.34300 7.83300  13.83700  1.000 37.72372  ? 423 VAL A HA   1 
ATOM   1549 H  HB   . VAL A 1 104 ? 26.17300 6.16500  14.51000  1.000 42.35010  ? 423 VAL A HB   1 
ATOM   1550 H  HG11 . VAL A 1 104 ? 25.86200 7.48500  16.43700  1.000 34.72031  ? 423 VAL A HG11 1 
ATOM   1551 H  HG12 . VAL A 1 104 ? 27.26900 6.75900  16.48100  1.000 34.72031  ? 423 VAL A HG12 1 
ATOM   1552 H  HG13 . VAL A 1 104 ? 27.18000 8.29100  16.08900  1.000 34.72031  ? 423 VAL A HG13 1 
ATOM   1553 H  HG21 . VAL A 1 104 ? 24.81200 8.05900  14.27600  1.000 34.59483  ? 423 VAL A HG21 1 
ATOM   1554 H  HG22 . VAL A 1 104 ? 26.07100 8.89700  13.80700  1.000 34.59483  ? 423 VAL A HG22 1 
ATOM   1555 H  HG23 . VAL A 1 104 ? 25.52900 7.71300  12.90700  1.000 34.59483  ? 423 VAL A HG23 1 
ATOM   1556 N  N    . ALA A 1 105 ? 29.84800 6.53600  15.32000  1.000 32.03083  ? 424 ALA A N    1 
ATOM   1557 C  CA   . ALA A 1 105 ? 30.65600 5.79100  16.27100  1.000 37.15556  ? 424 ALA A CA   1 
ATOM   1558 C  C    . ALA A 1 105 ? 30.14500 5.97400  17.70000  1.000 30.59030  ? 424 ALA A C    1 
ATOM   1559 O  O    . ALA A 1 105 ? 30.09000 5.01300  18.46100  1.000 38.42339  ? 424 ALA A O    1 
ATOM   1560 C  CB   . ALA A 1 105 ? 32.11600 6.21300  16.18200  1.000 39.88277  ? 424 ALA A CB   1 
ATOM   1561 H  H    . ALA A 1 105 ? 30.07600 7.36200  15.24300  1.000 38.51400  ? 424 ALA A H    1 
ATOM   1562 H  HA   . ALA A 1 105 ? 30.58500 4.85100  16.04200  1.000 44.66367  ? 424 ALA A HA   1 
ATOM   1563 H  HB1  . ALA A 1 105 ? 32.63900 5.70600  16.82300  1.000 47.93632  ? 424 ALA A HB1  1 
ATOM   1564 H  HB2  . ALA A 1 105 ? 32.44800 6.04200  15.28700  1.000 47.93632  ? 424 ALA A HB2  1 
ATOM   1565 H  HB3  . ALA A 1 105 ? 32.19200 7.16000  16.38000  1.000 47.93632  ? 424 ALA A HB3  1 
ATOM   1566 N  N    . GLU A 1 106 ? 29.78500 7.21400  18.05800  1.000 35.93831  ? 425 GLU A N    1 
ATOM   1567 C  CA   . GLU A 1 106 ? 29.29300 7.52400  19.39300  1.000 39.06082  ? 425 GLU A CA   1 
ATOM   1568 C  C    . GLU A 1 106 ? 28.21800 8.60800  19.35900  1.000 33.03344  ? 425 GLU A C    1 
ATOM   1569 O  O    . GLU A 1 106 ? 28.25300 9.48200  18.50300  1.000 30.42616  ? 425 GLU A O    1 
ATOM   1570 C  CB   . GLU A 1 106 ? 30.45800 7.99400  20.29000  1.000 37.00573  ? 425 GLU A CB   1 
ATOM   1571 C  CG   . GLU A 1 106 ? 31.23800 6.86900  20.93000  1.000 62.80540  ? 425 GLU A CG   1 
ATOM   1572 C  CD   . GLU A 1 106 ? 32.66800 7.23200  21.26300  1.000 80.96296  ? 425 GLU A CD   1 
ATOM   1573 O  OE1  . GLU A 1 106 ? 32.89700 8.37000  21.73300  1.000 65.18999  ? 425 GLU A OE1  1 
ATOM   1574 O  OE2  . GLU A 1 106 ? 33.56000 6.37600  21.06100  1.000 126.98279 ? 425 GLU A OE2  1 
ATOM   1575 H  H    . GLU A 1 106 ? 29.82200 7.89200  17.53000  1.000 43.20297  ? 425 GLU A H    1 
ATOM   1576 H  HA   . GLU A 1 106 ? 28.90000 6.71400  19.75500  1.000 46.94998  ? 425 GLU A HA   1 
ATOM   1577 H  HB2  . GLU A 1 106 ? 31.06400 8.53400  19.75900  1.000 44.48387  ? 425 GLU A HB2  1 
ATOM   1578 H  HB3  . GLU A 1 106 ? 30.10500 8.56700  20.98800  1.000 44.48387  ? 425 GLU A HB3  1 
ATOM   1579 H  HG2  . GLU A 1 106 ? 30.78500 6.59400  21.74200  1.000 75.44348  ? 425 GLU A HG2  1 
ATOM   1580 H  HG3  . GLU A 1 106 ? 31.23800 6.10500  20.33200  1.000 75.44348  ? 425 GLU A HG3  1 
ATOM   1581 N  N    . CYS A 1 107 ? 27.29900 8.54300  20.33000  1.000 39.92035  ? 426 CYS A N    1 
ATOM   1582 C  CA   . CYS A 1 107 ? 26.22100 9.49900  20.50600  1.000 32.07257  ? 426 CYS A CA   1 
ATOM   1583 C  C    . CYS A 1 107 ? 26.41300 10.24900 21.82100  1.000 33.16437  ? 426 CYS A C    1 
ATOM   1584 O  O    . CYS A 1 107 ? 26.98000 9.71400  22.76500  1.000 30.49610  ? 426 CYS A O    1 
ATOM   1585 C  CB   . CYS A 1 107 ? 24.86800 8.79600  20.51000  1.000 37.37156  ? 426 CYS A CB   1 
ATOM   1586 S  SG   . CYS A 1 107 ? 24.49900 7.86500  19.01000  1.000 34.40043  ? 426 CYS A SG   1 
ATOM   1587 H  H    . CYS A 1 107 ? 27.29400 7.91700  20.92000  1.000 47.98142  ? 426 CYS A H    1 
ATOM   1588 H  HA   . CYS A 1 107 ? 26.24000 10.12500 19.76500  1.000 38.56408  ? 426 CYS A HA   1 
ATOM   1589 H  HB2  . CYS A 1 107 ? 24.83300 8.19200  21.26800  1.000 44.92287  ? 426 CYS A HB2  1 
ATOM   1590 H  HB3  . CYS A 1 107 ? 24.17300 9.45900  20.64400  1.000 44.92287  ? 426 CYS A HB3  1 
ATOM   1591 N  N    . GLY A 1 108 ? 25.89200 11.47300 21.89100  1.000 27.10348  ? 427 GLY A N    1 
ATOM   1592 C  CA   . GLY A 1 108 ? 25.81500 12.18400 23.15600  1.000 33.36775  ? 427 GLY A CA   1 
ATOM   1593 C  C    . GLY A 1 108 ? 24.83200 13.34300 23.09500  1.000 36.98669  ? 427 GLY A C    1 
ATOM   1594 O  O    . GLY A 1 108 ? 24.34000 13.69200 22.02800  1.000 30.75154  ? 427 GLY A O    1 
ATOM   1595 H  H    . GLY A 1 108 ? 25.57900 11.90500 21.21600  1.000 32.60117  ? 427 GLY A H    1 
ATOM   1596 H  HA2  . GLY A 1 108 ? 25.54700 11.56900 23.85700  1.000 40.11830  ? 427 GLY A HA2  1 
ATOM   1597 H  HA3  . GLY A 1 108 ? 26.69400 12.51800 23.39300  1.000 40.11830  ? 427 GLY A HA3  1 
ATOM   1598 N  N    . CYS A 1 109 ? 24.56300 13.92500 24.26300  1.000 34.60364  ? 428 CYS A N    1 
ATOM   1599 C  CA   . CYS A 1 109 ? 23.68100 15.07100 24.39300  1.000 34.55389  ? 428 CYS A CA   1 
ATOM   1600 C  C    . CYS A 1 109 ? 24.49300 16.35400 24.25100  1.000 35.76475  ? 428 CYS A C    1 
ATOM   1601 O  O    . CYS A 1 109 ? 25.52100 16.50200 24.90700  1.000 34.61849  ? 428 CYS A O    1 
ATOM   1602 C  CB   . CYS A 1 109 ? 22.95200 14.99500 25.73200  1.000 36.66251  ? 428 CYS A CB   1 
ATOM   1603 S  SG   . CYS A 1 109 ? 21.81500 13.58800 25.84000  1.000 37.13520  ? 428 CYS A SG   1 
ATOM   1604 H  H    . CYS A 1 109 ? 24.89500 13.65800 25.01000  1.000 41.60137  ? 428 CYS A H    1 
ATOM   1605 H  HA   . CYS A 1 109 ? 23.01200 15.06900 23.69100  1.000 41.54166  ? 428 CYS A HA   1 
ATOM   1606 H  HB2  . CYS A 1 109 ? 23.60500 14.93300 26.44700  1.000 44.07201  ? 428 CYS A HB2  1 
ATOM   1607 H  HB3  . CYS A 1 109 ? 22.45600 15.81700 25.87200  1.000 44.07201  ? 428 CYS A HB3  1 
ATOM   1608 N  N    . ARG A 1 110 ? 24.03200 17.24600 23.36300  1.000 28.11683  ? 429 ARG A N    1 
ATOM   1609 C  CA   . ARG A 1 110 ? 24.74100 18.46400 23.01200  1.000 34.05609  ? 429 ARG A CA   1 
ATOM   1610 C  C    . ARG A 1 110 ? 23.77100 19.64700 22.94000  1.000 29.54330  ? 429 ARG A C    1 
ATOM   1611 O  O    . ARG A 1 110 ? 24.16000 20.79000 23.20900  1.000 29.94213  ? 429 ARG A O    1 
ATOM   1612 C  CB   . ARG A 1 110 ? 25.48000 18.27900 21.68000  1.000 31.81815  ? 429 ARG A CB   1 
ATOM   1613 C  CG   . ARG A 1 110 ? 26.60900 17.27200 21.74700  1.000 35.58330  ? 429 ARG A CG   1 
ATOM   1614 C  CD   . ARG A 1 110 ? 27.71300 17.73000 22.67300  1.000 35.67989  ? 429 ARG A CD   1 
ATOM   1615 N  NE   . ARG A 1 110 ? 28.83100 16.79700 22.71500  1.000 36.56922  ? 429 ARG A NE   1 
ATOM   1616 C  CZ   . ARG A 1 110 ? 28.92800 15.75900 23.53600  1.000 42.35900  ? 429 ARG A CZ   1 
ATOM   1617 N  NH1  . ARG A 1 110 ? 27.92000 15.38200 24.30800  1.000 30.84012  ? 429 ARG A NH1  1 
ATOM   1618 N  NH2  . ARG A 1 110 ? 30.06600 15.07500 23.57600  1.000 35.69304  ? 429 ARG A NH2  1 
ATOM   1619 O  OXT  . ARG A 1 110 ? 22.59600 19.45900 22.63300  1.000 27.84830  ? 429 ARG A OXT  1 
ATOM   1620 H  H    . ARG A 1 110 ? 23.28600 17.15000 22.94600  1.000 33.81719  ? 429 ARG A H    1 
ATOM   1621 H  HA   . ARG A 1 110 ? 25.39600 18.65500 23.70100  1.000 40.94430  ? 429 ARG A HA   1 
ATOM   1622 H  HB2  . ARG A 1 110 ? 24.84500 17.99700 21.00300  1.000 38.25878  ? 429 ARG A HB2  1 
ATOM   1623 H  HB3  . ARG A 1 110 ? 25.83700 19.13500 21.39500  1.000 38.25878  ? 429 ARG A HB3  1 
ATOM   1624 H  HG2  . ARG A 1 110 ? 26.26400 16.41800 22.05200  1.000 42.77695  ? 429 ARG A HG2  1 
ATOM   1625 H  HG3  . ARG A 1 110 ? 26.97000 17.13100 20.85800  1.000 42.77695  ? 429 ARG A HG3  1 
ATOM   1626 H  HD2  . ARG A 1 110 ? 28.03200 18.60000 22.38500  1.000 42.89287  ? 429 ARG A HD2  1 
ATOM   1627 H  HD3  . ARG A 1 110 ? 27.35500 17.84100 23.56800  1.000 42.89287  ? 429 ARG A HD3  1 
ATOM   1628 H  HE   . ARG A 1 110 ? 29.47900 16.92900 22.16500  1.000 43.96006  ? 429 ARG A HE   1 
ATOM   1629 H  HH11 . ARG A 1 110 ? 27.17700 15.81400 24.28600  1.000 37.08514  ? 429 ARG A HH11 1 
ATOM   1630 H  HH12 . ARG A 1 110 ? 28.00900 14.70500 24.83100  1.000 37.08514  ? 429 ARG A HH12 1 
ATOM   1631 H  HH21 . ARG A 1 110 ? 30.72500 15.30700 23.07500  1.000 42.90865  ? 429 ARG A HH21 1 
ATOM   1632 H  HH22 . ARG A 1 110 ? 30.14400 14.40000 24.10300  1.000 42.90865  ? 429 ARG A HH22 1 
HETATM 1633 C  C1   . GOL B 2 .   ? 38.04800 0.74200  4.92300   0.910 43.48345  ? 501 GOL A C1   1 
HETATM 1634 O  O1   . GOL B 2 .   ? 37.23600 -0.08100 4.09300   0.910 43.33258  ? 501 GOL A O1   1 
HETATM 1635 C  C2   . GOL B 2 .   ? 37.31400 1.17700  6.17100   0.910 43.90848  ? 501 GOL A C2   1 
HETATM 1636 O  O2   . GOL B 2 .   ? 38.25400 1.62600  7.14300   0.910 47.13276  ? 501 GOL A O2   1 
HETATM 1637 C  C3   . GOL B 2 .   ? 36.27200 2.24300  5.91400   0.910 43.83580  ? 501 GOL A C3   1 
HETATM 1638 O  O3   . GOL B 2 .   ? 36.82200 3.36200  5.22800   0.910 43.83107  ? 501 GOL A O3   1 
HETATM 1639 H  H11  . GOL B 2 .   ? 38.33100 1.52500  4.42500   0.910 52.25714  ? 501 GOL A H11  1 
HETATM 1640 H  H12  . GOL B 2 .   ? 38.85100 0.25800  5.17200   0.910 52.25714  ? 501 GOL A H12  1 
HETATM 1641 H  HO1  . GOL B 2 .   ? 37.61000 -0.18400 3.34800   0.910 52.07609  ? 501 GOL A HO1  1 
HETATM 1642 H  H2   . GOL B 2 .   ? 36.83200 0.40300  6.50200   0.910 52.76718  ? 501 GOL A H2   1 
HETATM 1643 H  HO2  . GOL B 2 .   ? 38.23900 2.46500  7.18100   0.910 56.63631  ? 501 GOL A HO2  1 
HETATM 1644 H  H31  . GOL B 2 .   ? 35.89200 2.53500  6.75800   0.910 52.67995  ? 501 GOL A H31  1 
HETATM 1645 H  H32  . GOL B 2 .   ? 35.54600 1.86700  5.39100   0.910 52.67995  ? 501 GOL A H32  1 
HETATM 1646 H  HO3  . GOL B 2 .   ? 36.20400 3.88400  5.00200   0.910 52.67428  ? 501 GOL A HO3  1 
HETATM 1647 CL CL   . CL  C 3 .   ? 36.09700 12.13500 2.76100   0.990 55.43455  ? 502 CL  A CL   1 
HETATM 1648 CL CL   . CL  D 3 .   ? 31.81500 20.67800 28.67000  0.750 36.23883  ? 503 CL  A CL   1 
HETATM 1649 CL CL   . CL  E 3 .   ? 22.07900 13.47300 36.38900  0.450 67.71750  ? 504 CL  A CL   1 
HETATM 1650 CL CL   . CL  F 3 .   ? 40.52900 7.74700  1.32300   0.990 68.65831  ? 505 CL  A CL   1 
HETATM 1651 CL CL   . CL  G 3 .   ? 44.15200 2.42800  6.30400   0.580 63.13053  ? 506 CL  A CL   1 
HETATM 1652 NA NA   . NA  H 4 .   ? 42.90300 0.45600  6.55300   0.800 38.37563  1 507 NA  A NA   1 
HETATM 1653 NA NA   . NA  I 4 .   ? 23.80100 -0.54800 17.57800  0.840 94.95182  1 508 NA  A NA   1 
HETATM 1654 NA NA   . NA  J 4 .   ? 7.54600  28.41500 29.30400  0.930 46.95383  1 509 NA  A NA   1 
HETATM 1655 NA NA   . NA  K 4 .   ? 17.28100 4.43600  2.83600   0.990 59.84125  1 510 NA  A NA   1 
HETATM 1656 O  O    . HOH L 5 .   ? 16.32900 9.30600  14.21000  0.930 43.42506  ? 601 HOH A O    1 
HETATM 1657 O  O    . HOH L 5 .   ? 29.04300 10.42900 24.32700  0.260 27.76298  ? 602 HOH A O    1 
HETATM 1658 O  O    . HOH L 5 .   ? 17.98700 24.49000 20.88000  0.580 36.91067  ? 603 HOH A O    1 
HETATM 1659 O  O    . HOH L 5 .   ? 37.73400 2.47300  9.46400   0.140 15.49328  ? 604 HOH A O    1 
HETATM 1660 O  O    . HOH L 5 .   ? 40.19700 7.63800  8.32400   0.240 34.43800  ? 605 HOH A O    1 
HETATM 1661 O  O    . HOH L 5 .   ? 22.99600 22.72500 24.51800  0.850 28.05514  ? 606 HOH A O    1 
HETATM 1662 O  O    . HOH L 5 .   ? 25.80100 -3.47000 2.93900   0.150 24.79097  ? 607 HOH A O    1 
HETATM 1663 O  O    . HOH L 5 .   ? 10.56100 29.89000 39.71000  0.510 48.38935  ? 608 HOH A O    1 
HETATM 1664 O  O    . HOH L 5 .   ? 14.11800 1.41700  1.17000   0.260 35.28149  ? 609 HOH A O    1 
HETATM 1665 O  O    . HOH L 5 .   ? 33.89400 20.21500 31.03200  0.220 27.73249  ? 610 HOH A O    1 
HETATM 1666 O  O    . HOH L 5 .   ? 34.88600 9.68000  9.79000   0.910 39.22275  ? 611 HOH A O    1 
HETATM 1667 O  O    . HOH L 5 .   ? 26.74800 21.39500 23.89800  0.840 30.88892  ? 612 HOH A O    1 
HETATM 1668 O  O    . HOH L 5 .   ? 20.95000 1.99200  -3.74900  0.790 44.91960  ? 613 HOH A O    1 
HETATM 1669 O  O    . HOH L 5 .   ? 19.838   12.147   -7.723    0.240 16.70442  ? 614 HOH A O    1 
HETATM 1670 O  O    . HOH L 5 .   ? 20.462   13.711   -2.963    0.730 33.67932  ? 615 HOH A O    1 
HETATM 1671 O  O    . HOH L 5 .   ? 16.17300 15.64800 23.25200  0.510 36.31057  ? 616 HOH A O    1 
HETATM 1672 O  O    . HOH L 5 .   ? 20.58900 10.51500 28.25600  0.450 26.43261  ? 617 HOH A O    1 
HETATM 1673 O  O    . HOH L 5 .   ? 8.741    21.374   32.681    0.550 24.73108  ? 618 HOH A O    1 
HETATM 1674 O  O    . HOH L 5 .   ? 24.79700 2.82500  -4.74300  0.250 22.94777  ? 619 HOH A O    1 
HETATM 1675 O  O    . HOH L 5 .   ? 30.82300 10.94500 23.04400  0.340 37.11432  ? 620 HOH A O    1 
HETATM 1676 O  O    . HOH L 5 .   ? 26.113   9.438    36.387    0.400 78.05326  ? 621 HOH A O    1 
HETATM 1677 O  O    . HOH L 5 .   ? 15.21700 16.75700 32.47100  0.970 44.32784  ? 622 HOH A O    1 
HETATM 1678 O  O    . HOH L 5 .   ? 9.95500  18.56400 28.87400  0.230 32.61584  ? 623 HOH A O    1 
HETATM 1679 O  O    . HOH L 5 .   ? 28.51800 16.64700 17.67400  0.870 35.51524  ? 624 HOH A O    1 
HETATM 1680 O  O    . HOH L 5 .   ? 21.58200 10.75000 14.51400  0.940 26.26018  ? 625 HOH A O    1 
HETATM 1681 O  O    . HOH L 5 .   ? 21.09700 21.84100 21.86300  0.930 43.09975  ? 626 HOH A O    1 
HETATM 1682 O  O    . HOH L 5 .   ? 31.19300 2.34300  17.93400  0.450 50.15276  ? 627 HOH A O    1 
HETATM 1683 O  O    . HOH L 5 .   ? 13.783   5.075    -7.412    0.110 14.03125  ? 628 HOH A O    1 
HETATM 1684 O  O    . HOH L 5 .   ? 32.26800 16.27800 22.02700  0.240 18.81226  ? 629 HOH A O    1 
HETATM 1685 O  O    . HOH L 5 .   ? 36.61200 5.57800  13.21700  0.180 17.89726  ? 630 HOH A O    1 
HETATM 1686 O  O    . HOH L 5 .   ? 22.97700 1.13600  21.92400  0.230 23.45675  ? 631 HOH A O    1 
HETATM 1687 O  O    . HOH L 5 .   ? 34.17500 12.38100 14.25800  0.820 34.44514  ? 632 HOH A O    1 
HETATM 1688 O  O    . HOH L 5 .   ? 29.51700 7.91600  24.43100  0.220 29.17583  ? 633 HOH A O    1 
HETATM 1689 O  O    . HOH L 5 .   ? 17.18400 14.33800 21.00300  0.890 45.43684  ? 634 HOH A O    1 
HETATM 1690 O  O    . HOH L 5 .   ? 32.09600 15.92900 19.33700  0.240 31.85710  ? 635 HOH A O    1 
HETATM 1691 O  O    . HOH L 5 .   ? 34.98900 13.37100 17.65000  0.300 35.06127  ? 636 HOH A O    1 
HETATM 1692 O  O    . HOH L 5 .   ? 34.54700 2.09800  9.89800   0.170 30.30703  ? 637 HOH A O    1 
HETATM 1693 O  O    . HOH L 5 .   ? 15.47700 10.98100 19.62300  0.300 42.84122  ? 638 HOH A O    1 
HETATM 1694 O  O    . HOH L 5 .   ? 25.45200 4.11000  22.24400  0.720 44.74866  ? 639 HOH A O    1 
HETATM 1695 O  O    . HOH L 5 .   ? 27.23100 6.04600  22.19300  0.640 38.30942  ? 640 HOH A O    1 
HETATM 1696 O  O    . HOH L 5 .   ? 17.05300 0.71800  9.42000   0.540 40.12564  ? 641 HOH A O    1 
HETATM 1697 O  O    . HOH L 5 .   ? 13.45700 30.13500 41.16300  0.250 31.27855  ? 642 HOH A O    1 
HETATM 1698 O  O    . HOH L 5 .   ? 24.69600 -3.16800 -0.21000  0.210 18.89632  ? 643 HOH A O    1 
HETATM 1699 O  O    . HOH L 5 .   ? 40.54000 3.12400  -7.34800  0.200 20.38029  ? 644 HOH A O    1 
HETATM 1700 O  O    . HOH L 5 .   ? 31.44200 3.08300  13.73200  0.580 52.12601  ? 645 HOH A O    1 
HETATM 1701 O  O    . HOH L 5 .   ? 29.24700 0.78500  9.02200   0.270 25.37437  ? 646 HOH A O    1 
HETATM 1702 O  O    . HOH L 5 .   ? 17.72000 12.87300 17.79800  0.200 22.95893  ? 647 HOH A O    1 
HETATM 1703 O  O    . HOH L 5 .   ? 41.08900 6.67000  -1.64200  0.790 40.64069  ? 648 HOH A O    1 
HETATM 1704 O  O    . HOH L 5 .   ? 19.129   13.241   15.991    1.000 80.36831  ? 649 HOH A O    1 
HETATM 1705 O  O    . HOH L 5 .   ? 15.00200 6.29900  -7.98500  0.150 9.58099   ? 650 HOH A O    1 
HETATM 1706 O  O    . HOH L 5 .   ? 19.06500 -1.02400 17.02400  0.780 50.94925  ? 651 HOH A O    1 
HETATM 1707 O  O    . HOH L 5 .   ? 39.98300 10.95300 3.91200   0.280 34.33666  ? 652 HOH A O    1 
HETATM 1708 O  O    . HOH L 5 .   ? 38.14800 9.21200  11.48200  0.180 32.47806  ? 653 HOH A O    1 
HETATM 1709 O  O    . HOH L 5 .   ? 31.77900 1.80100  9.34000   0.990 78.04032  ? 654 HOH A O    1 
HETATM 1710 O  O    . HOH L 5 .   ? 22.46600 2.51200  -5.50600  0.200 23.81787  ? 655 HOH A O    1 
HETATM 1711 O  O    . HOH L 5 .   ? 8.551    27.003   36.387    0.120 37.82576  ? 656 HOH A O    1 
HETATM 1712 O  O    . HOH L 5 .   ? 36.72400 10.22200 14.72700  0.260 38.62125  ? 657 HOH A O    1 
HETATM 1713 O  O    . HOH L 5 .   ? 32.14100 16.59500 26.82000  0.290 39.96536  ? 658 HOH A O    1 
HETATM 1714 O  O    . HOH L 5 .   ? 21.788   13.020   -10.737   0.120 3.05618   ? 659 HOH A O    1 
HETATM 1715 O  O    . HOH L 5 .   ? 15.38400 18.74200 20.89000  0.290 30.50660  ? 660 HOH A O    1 
HETATM 1716 O  O    . HOH L 5 .   ? 10.795   9.912    14.631    0.750 61.08164  ? 661 HOH A O    1 
HETATM 1717 O  O    . HOH L 5 .   ? 14.63200 3.77200  31.55000  0.280 42.68155  ? 662 HOH A O    1 
HETATM 1718 O  O    . HOH L 5 .   ? 15.36900 7.53900  33.89400  0.160 25.91036  ? 663 HOH A O    1 
HETATM 1719 O  O    . HOH L 5 .   ? 20.64200 6.40800  34.74800  0.120 18.97911  ? 664 HOH A O    1 
HETATM 1720 O  O    . HOH L 5 .   ? 29.298   15.519   -0.304    0.160 31.57062  ? 665 HOH A O    1 
HETATM 1721 O  O    . HOH L 5 .   ? 12.22700 1.92300  -0.11300  0.110 18.95785  ? 666 HOH A O    1 
HETATM 1722 O  O    . HOH L 5 .   ? 42.02100 3.87100  -2.80800  0.920 47.47219  ? 667 HOH A O    1 
HETATM 1723 O  O    . HOH L 5 .   ? 27.59100 0.81000  20.50700  0.170 32.87426  ? 668 HOH A O    1 
HETATM 1724 O  O    . HOH L 5 .   ? 34.61900 12.26300 11.12300  0.610 35.75545  ? 669 HOH A O    1 
HETATM 1725 O  O    . HOH L 5 .   ? 27.52400 -1.71500 17.18000  0.450 64.21574  ? 670 HOH A O    1 
HETATM 1726 O  O    . HOH L 5 .   ? 19.73000 -0.57700 19.67600  0.170 36.32797  ? 671 HOH A O    1 
HETATM 1727 O  O    . HOH L 5 .   ? 42.31800 7.01600  -5.16900  0.110 23.47202  ? 672 HOH A O    1 
HETATM 1728 O  O    . HOH L 5 .   ? 8.14600  20.69800 25.55800  0.170 21.04675  ? 673 HOH A O    1 
HETATM 1729 O  O    . HOH L 5 .   ? 10.81400 32.17500 38.05400  0.130 24.67468  ? 674 HOH A O    1 
HETATM 1730 O  O    . HOH L 5 .   ? 15.08200 2.11400  11.37800  0.110 32.32516  ? 675 HOH A O    1 
HETATM 1731 O  O    . HOH L 5 .   ? 15.23300 0.71900  -4.00100  0.450 67.69022  ? 676 HOH A O    1 
HETATM 1732 O  O    . HOH L 5 .   ? 33.55500 13.70300 25.15800  0.240 31.83143  ? 677 HOH A O    1 
HETATM 1733 O  O    . HOH L 5 .   ? 43.046   3.310    9.432     0.210 35.60211  ? 678 HOH A O    1 
HETATM 1734 O  O    . HOH L 5 .   ? 22.11000 -4.65100 -0.03000  0.110 23.22039  ? 679 HOH A O    1 
HETATM 1735 O  O    . HOH L 5 .   ? 39.11200 4.30300  10.18000  0.110 26.94692  ? 680 HOH A O    1 
HETATM 1736 O  O    . HOH L 5 .   ? 12.86700 2.98500  31.27400  0.170 32.81752  ? 681 HOH A O    1 
HETATM 1737 O  O    . HOH L 5 .   ? 33.25900 12.51100 22.55600  0.200 29.93662  ? 682 HOH A O    1 
HETATM 1738 O  O    . HOH L 5 .   ? 31.69500 15.05000 14.63600  0.880 52.85955  ? 683 HOH A O    1 
HETATM 1739 O  O    . HOH L 5 .   ? 33.674   14.041   9.979     0.160 18.52008  ? 684 HOH A O    1 
HETATM 1740 O  O    . HOH L 5 .   ? 28.79600 21.12200 21.93700  0.920 30.44583  ? 685 HOH A O    1 
HETATM 1741 O  O    . HOH L 5 .   ? 16.49200 -1.61600 5.42200   0.210 25.64678  ? 686 HOH A O    1 
HETATM 1742 O  O    . HOH L 5 .   ? 26.940   -5.080   0.513     0.180 44.72271  ? 687 HOH A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 6   ? 1.48408 1.24851 0.83084 -0.39019 0.19110  0.04895  325 SER A N   
2    C CA  . SER A 6   ? 1.23303 1.10183 0.67066 -0.36571 0.20345  0.02154  325 SER A CA  
3    C C   . SER A 6   ? 1.96589 1.85927 1.43095 -0.30226 0.18073  0.02629  325 SER A C   
4    O O   . SER A 6   ? 1.13720 1.13383 0.67500 -0.27872 0.19479  -0.00549 325 SER A O   
5    C CB  . SER A 6   ? 1.82915 1.81116 1.32995 -0.39655 0.24823  -0.02731 325 SER A CB  
6    O OG  . SER A 6   ? 2.04319 1.99972 1.51555 -0.45760 0.27131  -0.03342 325 SER A OG  
11   N N   . HIS A 7   ? 1.01818 0.81690 0.43335 -0.27176 0.14117  0.06181  326 HIS A N   
12   C CA  . HIS A 7   ? 1.01257 0.82012 0.44762 -0.21417 0.11753  0.06793  326 HIS A CA  
13   C C   . HIS A 7   ? 0.80501 0.60019 0.28931 -0.16530 0.08322  0.07831  326 HIS A C   
14   O O   . HIS A 7   ? 0.81320 0.58855 0.30699 -0.17622 0.07650  0.08151  326 HIS A O   
15   C CB  . HIS A 7   ? 1.08314 0.81374 0.46200 -0.20470 0.09422  0.08802  326 HIS A CB  
16   C CG  . HIS A 7   ? 1.92267 1.69641 1.28451 -0.22649 0.12358  0.06947  326 HIS A CG  
17   N ND1 . HIS A 7   ? 1.34473 1.20469 0.75386 -0.19939 0.13697  0.04473  326 HIS A ND1 
18   C CD2 . HIS A 7   ? 1.49598 1.23684 0.79887 -0.27179 0.14045  0.06992  326 HIS A CD2 
19   C CE1 . HIS A 7   ? 1.49399 1.37455 0.87755 -0.22730 0.16142  0.02923  326 HIS A CE1 
20   N NE2 . HIS A 7   ? 1.35384 1.16324 0.66940 -0.27265 0.16593  0.04521  326 HIS A NE2 
28   N N   . CYS A 8   ? 0.79070 0.60057 0.31445 -0.11028 0.06138  0.08040  327 CYS A N   
29   C CA  . CYS A 8   ? 0.83750 0.65625 0.42421 -0.06001 0.03543  0.08379  327 CYS A CA  
30   C C   . CYS A 8   ? 0.93190 0.65557 0.48404 -0.05688 0.00522  0.10679  327 CYS A C   
31   O O   . CYS A 8   ? 0.95356 0.60399 0.46812 -0.04959 -0.01872 0.12238  327 CYS A O   
32   C CB  . CYS A 8   ? 0.69458 0.53766 0.32006 -0.01118 0.02228  0.08310  327 CYS A CB  
33   S SG  . CYS A 8   ? 0.63617 0.48687 0.33129 0.04575  -0.00258 0.08894  327 CYS A SG  
38   N N   . GLN A 9   ? 0.68450 0.42114 0.26879 -0.05742 0.00284  0.10054  328 GLN A N   
39   C CA  . GLN A 9   ? 0.74521 0.40046 0.30820 -0.05336 -0.02672 0.11449  328 GLN A CA  
40   C C   . GLN A 9   ? 0.68333 0.37882 0.30594 -0.03206 -0.03077 0.10057  328 GLN A C   
41   O O   . GLN A 9   ? 0.64969 0.42884 0.31904 -0.02790 -0.01131 0.08204  328 GLN A O   
42   C CB  . GLN A 9   ? 0.82715 0.40462 0.31223 -0.10818 -0.02721 0.12728  328 GLN A CB  
43   C CG  . GLN A 9   ? 0.87677 0.50661 0.37316 -0.15248 0.00494  0.11075  328 GLN A CG  
44   C CD  . GLN A 9   ? 1.32786 0.86976 0.74288 -0.21116 0.00538  0.12726  328 GLN A CD  
45   O OE1 . GLN A 9   ? 1.14824 0.61733 0.52571 -0.20732 -0.02122 0.13887  328 GLN A OE1 
46   N NE2 . GLN A 9   ? 1.09620 0.67405 0.52467 -0.25417 0.03203  0.11206  328 GLN A NE2 
55   N N   . LYS A 10  ? 0.74478 0.37682 0.36313 -0.01781 -0.05948 0.10667  329 LYS A N   
56   C CA  . LYS A 10  ? 0.83131 0.48935 0.49571 0.00220  -0.06597 0.09213  329 LYS A CA  
57   C C   . LYS A 10  ? 0.84400 0.49953 0.49747 -0.03637 -0.06059 0.08268  329 LYS A C   
58   O O   . LYS A 10  ? 0.89795 0.47922 0.50069 -0.07193 -0.07144 0.09393  329 LYS A O   
59   C CB  . LYS A 10  ? 0.87129 0.46549 0.54156 0.03104  -0.09822 0.09487  329 LYS A CB  
60   C CG  . LYS A 10  ? 0.82762 0.45750 0.54775 0.05789  -0.10073 0.07613  329 LYS A CG  
61   C CD  . LYS A 10  ? 0.68952 0.30962 0.45074 0.08237  -0.11592 0.06340  329 LYS A CD  
62   C CE  . LYS A 10  ? 0.82591 0.38689 0.57348 0.06561  -0.14313 0.05625  329 LYS A CE  
63   N NZ  . LYS A 10  ? 1.23513 0.81772 1.03531 0.08571  -0.15100 0.03644  329 LYS A NZ  
77   N N   . THR A 11  ? 0.64240 0.37469 0.34179 -0.02936 -0.04644 0.06188  330 THR A N   
78   C CA  . THR A 11  ? 0.67151 0.41213 0.37610 -0.06093 -0.04286 0.04638  330 THR A CA  
79   C C   . THR A 11  ? 0.63591 0.40881 0.38321 -0.02743 -0.05512 0.02740  330 THR A C   
80   O O   . THR A 11  ? 0.58222 0.38345 0.35187 0.01389  -0.05722 0.02683  330 THR A O   
81   C CB  . THR A 11  ? 0.76194 0.57208 0.48063 -0.09230 -0.01202 0.03130  330 THR A CB  
82   O OG1 . THR A 11  ? 0.68178 0.57897 0.45119 -0.05646 -0.00433 0.01460  330 THR A OG1 
83   C CG2 . THR A 11  ? 1.13661 0.92375 0.80951 -0.12567 0.00620  0.04626  330 THR A CG2 
91   N N   . SER A 12  ? 0.66206 0.42791 0.41706 -0.04802 -0.06216 0.01148  331 SER A N   
92   C CA  . SER A 12  ? 0.63954 0.42730 0.42612 -0.01897 -0.07644 -0.00935 331 SER A CA  
93   C C   . SER A 12  ? 0.62911 0.50780 0.44959 0.00661  -0.06309 -0.02678 331 SER A C   
94   O O   . SER A 12  ? 0.65234 0.58183 0.48663 -0.00967 -0.04672 -0.03484 331 SER A O   
95   C CB  . SER A 12  ? 0.69720 0.45409 0.48628 -0.04839 -0.09013 -0.02476 331 SER A CB  
96   O OG  . SER A 12  ? 0.87919 0.66166 0.69775 -0.01731 -0.10446 -0.04914 331 SER A OG  
102  N N   . LEU A 13  ? 0.56861 0.46457 0.40030 0.04663  -0.07122 -0.03400 332 LEU A N   
103  C CA  . LEU A 13  ? 0.58114 0.54630 0.43139 0.07155  -0.06752 -0.05067 332 LEU A CA  
104  C C   . LEU A 13  ? 0.59445 0.55556 0.44313 0.09925  -0.07974 -0.06508 332 LEU A C   
105  O O   . LEU A 13  ? 0.62386 0.56953 0.46358 0.12409  -0.07724 -0.05520 332 LEU A O   
106  C CB  . LEU A 13  ? 0.51532 0.51430 0.36605 0.09460  -0.05577 -0.03540 332 LEU A CB  
107  C CG  . LEU A 13  ? 0.51123 0.56851 0.37092 0.12347  -0.05990 -0.04973 332 LEU A CG  
108  C CD1 . LEU A 13  ? 0.48116 0.58636 0.36766 0.10673  -0.06410 -0.07682 332 LEU A CD1 
109  C CD2 . LEU A 13  ? 0.45558 0.52952 0.31214 0.14833  -0.05343 -0.03048 332 LEU A CD2 
121  N N   . ARG A 14  ? 0.56362 0.54098 0.42414 0.09268  -0.09137 -0.09223 333 ARG A N   
122  C CA  . ARG A 14  ? 0.57787 0.55833 0.43492 0.11753  -0.10280 -0.11281 333 ARG A CA  
123  C C   . ARG A 14  ? 0.59754 0.63246 0.44288 0.14703  -0.10089 -0.12105 333 ARG A C   
124  O O   . ARG A 14  ? 0.56387 0.63870 0.42229 0.14266  -0.10686 -0.13497 333 ARG A O   
125  C CB  . ARG A 14  ? 0.75843 0.72421 0.63341 0.09746  -0.12093 -0.13998 333 ARG A CB  
126  C CG  . ARG A 14  ? 0.93620 0.89343 0.80934 0.12138  -0.13402 -0.16348 333 ARG A CG  
127  C CD  . ARG A 14  ? 1.07963 1.00473 0.97527 0.10113  -0.15663 -0.18795 333 ARG A CD  
128  N NE  . ARG A 14  ? 1.29563 1.21567 1.19458 0.12667  -0.16943 -0.21557 333 ARG A NE  
129  C CZ  . ARG A 14  ? 1.06260 0.95295 0.96035 0.14250  -0.16846 -0.21332 333 ARG A CZ  
130  N NH1 . ARG A 14  ? 0.91630 0.76450 0.81117 0.13366  -0.16381 -0.18444 333 ARG A NH1 
131  N NH2 . ARG A 14  ? 1.25960 1.16495 1.16189 0.16795  -0.17287 -0.24539 333 ARG A NH2 
145  N N   . VAL A 15  ? 0.58503 0.61771 0.40523 0.17550  -0.09344 -0.11363 334 VAL A N   
146  C CA  . VAL A 15  ? 0.55395 0.62039 0.34429 0.20284  -0.09210 -0.11316 334 VAL A CA  
147  C C   . VAL A 15  ? 0.59277 0.66682 0.35823 0.22038  -0.10046 -0.14054 334 VAL A C   
148  O O   . VAL A 15  ? 0.60428 0.65748 0.36453 0.22537  -0.09114 -0.14625 334 VAL A O   
149  C CB  . VAL A 15  ? 0.53777 0.59311 0.30881 0.21722  -0.07270 -0.08193 334 VAL A CB  
150  C CG1 . VAL A 15  ? 0.56449 0.63765 0.28924 0.24342  -0.07162 -0.07754 334 VAL A CG1 
151  C CG2 . VAL A 15  ? 0.54614 0.60068 0.33922 0.20450  -0.06746 -0.05902 334 VAL A CG2 
161  N N   . ASN A 16  ? 0.62113 0.72630 0.37038 0.23267  -0.11794 -0.15905 335 ASN A N   
162  C CA  . ASN A 16  ? 0.66453 0.77969 0.37117 0.25502  -0.12736 -0.18314 335 ASN A CA  
163  C C   . ASN A 16  ? 0.69370 0.80839 0.33505 0.27886  -0.11828 -0.16111 335 ASN A C   
164  O O   . ASN A 16  ? 0.69182 0.81740 0.32487 0.28655  -0.13039 -0.14732 335 ASN A O   
165  C CB  . ASN A 16  ? 0.69311 0.83507 0.41883 0.25472  -0.15755 -0.21896 335 ASN A CB  
166  C CG  . ASN A 16  ? 0.89736 1.04706 0.58084 0.27669  -0.17140 -0.24948 335 ASN A CG  
167  O OD1 . ASN A 16  ? 0.77331 0.92113 0.41005 0.29346  -0.16606 -0.23304 335 ASN A OD1 
168  N ND2 . ASN A 16  ? 0.75540 0.90631 0.47129 0.26843  -0.18419 -0.28412 335 ASN A ND2 
175  N N   . PHE A 17  ? 0.70867 0.81484 0.34748 0.32270  -0.16175 -0.08535 336 PHE A N   
176  C CA  . PHE A 17  ? 0.71830 0.82075 0.34007 0.34153  -0.14282 -0.06734 336 PHE A CA  
177  C C   . PHE A 17  ? 0.75119 0.87077 0.36513 0.36409  -0.15604 -0.07991 336 PHE A C   
178  O O   . PHE A 17  ? 0.75713 0.87734 0.36336 0.37489  -0.14536 -0.06663 336 PHE A O   
179  C CB  . PHE A 17  ? 0.73057 0.81109 0.32956 0.34988  -0.12758 -0.05821 336 PHE A CB  
180  C CG  . PHE A 17  ? 0.69974 0.76192 0.30594 0.33179  -0.11023 -0.04127 336 PHE A CG  
181  C CD1 . PHE A 17  ? 0.67158 0.73075 0.28972 0.32093  -0.09134 -0.01957 336 PHE A CD1 
182  C CD2 . PHE A 17  ? 0.70170 0.74790 0.30344 0.32611  -0.11476 -0.04868 336 PHE A CD2 
183  C CE1 . PHE A 17  ? 0.64581 0.68733 0.27210 0.30461  -0.07706 -0.00551 336 PHE A CE1 
184  C CE2 . PHE A 17  ? 0.67744 0.70502 0.28521 0.31129  -0.10129 -0.03448 336 PHE A CE2 
185  C CZ  . PHE A 17  ? 0.64955 0.67543 0.26995 0.30060  -0.08233 -0.01286 336 PHE A CZ  
195  N N   . GLU A 18  ? 0.77651 0.90689 0.39174 0.37111  -0.18039 -0.10630 337 GLU A N   
196  C CA  . GLU A 18  ? 0.80895 0.95701 0.42157 0.39129  -0.19788 -0.12232 337 GLU A CA  
197  C C   . GLU A 18  ? 0.79020 0.96324 0.43115 0.38586  -0.20465 -0.12498 337 GLU A C   
198  O O   . GLU A 18  ? 0.80964 0.98721 0.44133 0.40366  -0.20482 -0.12144 337 GLU A O   
199  C CB  . GLU A 18  ? 0.83688 0.99317 0.45367 0.39600  -0.22460 -0.15296 337 GLU A CB  
200  C CG  . GLU A 18  ? 0.87671 1.04873 0.48883 0.41954  -0.24407 -0.17082 337 GLU A CG  
201  C CD  . GLU A 18  ? 1.02488 1.20039 0.63545 0.42880  -0.26861 -0.19948 337 GLU A CD  
202  O OE1 . GLU A 18  ? 0.91290 1.07384 0.51827 0.42064  -0.26848 -0.20377 337 GLU A OE1 
203  O OE2 . GLU A 18  ? 1.53344 1.72532 1.14888 0.44486  -0.28918 -0.21876 337 GLU A OE2 
210  N N   . ASP A 19  ? 0.75572 0.94427 0.43002 0.36156  -0.21053 -0.13182 338 ASP A N   
211  C CA  . ASP A 19  ? 0.75593 0.97507 0.46316 0.35589  -0.21750 -0.13784 338 ASP A CA  
212  C C   . ASP A 19  ? 0.72578 0.93568 0.42202 0.36369  -0.19606 -0.11082 338 ASP A C   
213  O O   . ASP A 19  ? 0.72873 0.96025 0.44117 0.37283  -0.20368 -0.11701 338 ASP A O   
214  C CB  . ASP A 19  ? 0.76918 1.00427 0.51004 0.32531  -0.22241 -0.14654 338 ASP A CB  
215  C CG  . ASP A 19  ? 0.77415 1.02846 0.54196 0.31056  -0.24795 -0.18091 338 ASP A CG  
216  O OD1 . ASP A 19  ? 0.74288 1.00249 0.50828 0.32654  -0.26448 -0.19980 338 ASP A OD1 
217  O OD2 . ASP A 19  ? 0.74452 1.00543 0.53462 0.28083  -0.25091 -0.18982 338 ASP A OD2 
222  N N   . ILE A 20  ? 0.74308 0.92151 0.41637 0.35856  -0.17009 -0.08313 339 ILE A N   
223  C CA  . ILE A 20  ? 0.71477 0.88022 0.38003 0.36151  -0.14819 -0.05756 339 ILE A CA  
224  C C   . ILE A 20  ? 0.78388 0.92688 0.41334 0.38218  -0.13710 -0.04553 339 ILE A C   
225  O O   . ILE A 20  ? 0.73728 0.86409 0.35786 0.38205  -0.11729 -0.02374 339 ILE A O   
226  C CB  . ILE A 20  ? 0.70789 0.85578 0.37971 0.33871  -0.12600 -0.03558 339 ILE A CB  
227  C CG1 . ILE A 20  ? 0.66961 0.79039 0.32177 0.33442  -0.11329 -0.02688 339 ILE A CG1 
228  C CG2 . ILE A 20  ? 0.68382 0.85234 0.38547 0.31847  -0.13647 -0.04542 339 ILE A CG2 
229  C CD1 . ILE A 20  ? 0.66582 0.76560 0.32177 0.31799  -0.08913 -0.00345 339 ILE A CD1 
241  N N   . GLY A 21  ? 0.77949 0.92136 0.38848 0.39934  -0.15056 -0.06057 340 GLY A N   
242  C CA  . GLY A 21  ? 0.82310 0.94601 0.39460 0.42135  -0.14354 -0.05182 340 GLY A CA  
243  C C   . GLY A 21  ? 0.86569 0.96322 0.41478 0.41917  -0.11873 -0.03197 340 GLY A C   
244  O O   . GLY A 21  ? 0.85937 0.94044 0.37907 0.43391  -0.10798 -0.01953 340 GLY A O   
248  N N   . TRP A 22  ? 0.79335 0.88802 0.35623 0.40148  -0.11127 -0.03038 341 TRP A N   
249  C CA  . TRP A 22  ? 0.79133 0.86693 0.34067 0.39888  -0.08926 -0.01469 341 TRP A CA  
250  C C   . TRP A 22  ? 0.84428 0.91629 0.37414 0.41078  -0.09645 -0.02812 341 TRP A C   
251  O O   . TRP A 22  ? 0.82265 0.88237 0.34029 0.41261  -0.07987 -0.01789 341 TRP A O   
252  C CB  . TRP A 22  ? 0.74150 0.81232 0.31746 0.37298  -0.07518 -0.00262 341 TRP A CB  
253  C CG  . TRP A 22  ? 0.71804 0.78466 0.30780 0.36228  -0.05911 0.01681  341 TRP A CG  
254  C CD1 . TRP A 22  ? 0.73596 0.80494 0.32086 0.37142  -0.05966 0.02198  341 TRP A CD1 
255  C CD2 . TRP A 22  ? 0.67884 0.73598 0.28921 0.34086  -0.04172 0.03226  341 TRP A CD2 
256  N NE1 . TRP A 22  ? 0.71406 0.77611 0.31629 0.35637  -0.04336 0.03941  341 TRP A NE1 
257  C CE2 . TRP A 22  ? 0.67006 0.72527 0.28891 0.33721  -0.03200 0.04578  341 TRP A CE2 
258  C CE3 . TRP A 22  ? 0.66805 0.71638 0.28972 0.32518  -0.03527 0.03472  341 TRP A CE3 
259  C CZ2 . TRP A 22  ? 0.64824 0.69434 0.28834 0.31764  -0.01580 0.06079  341 TRP A CZ2 
260  C CZ3 . TRP A 22  ? 0.62262 0.66134 0.26419 0.30649  -0.01956 0.05014  341 TRP A CZ3 
261  C CH2 . TRP A 22  ? 0.67964 0.71806 0.33146 0.30226  -0.00993 0.06252  341 TRP A CH2 
272  N N   . ASP A 23  ? 0.83973 0.92386 0.36826 0.41980  -0.12207 -0.05253 342 ASP A N   
273  C CA  . ASP A 23  ? 0.88787 0.96852 0.39787 0.43273  -0.13215 -0.06834 342 ASP A CA  
274  C C   . ASP A 23  ? 0.98395 1.05387 0.45422 0.45826  -0.12437 -0.06168 342 ASP A C   
275  O O   . ASP A 23  ? 1.00572 1.07042 0.45553 0.47095  -0.12681 -0.07001 342 ASP A O   
276  C CB  . ASP A 23  ? 1.00330 1.09988 0.52623 0.43433  -0.16327 -0.09767 342 ASP A CB  
277  C CG  . ASP A 23  ? 1.03293 1.14113 0.54923 0.45148  -0.17887 -0.10698 342 ASP A CG  
278  O OD1 . ASP A 23  ? 0.92286 1.03403 0.44510 0.44948  -0.17116 -0.09364 342 ASP A OD1 
279  O OD2 . ASP A 23  ? 1.18746 1.30076 0.69298 0.46756  -0.20001 -0.12863 342 ASP A OD2 
284  N N   . SER A 24  ? 1.00825 1.07334 0.46574 0.46589  -0.11596 -0.04695 343 SER A N   
285  C CA  . SER A 24  ? 1.45753 1.50680 0.87417 0.48625  -0.10451 -0.03480 343 SER A CA  
286  C C   . SER A 24  ? 1.23166 1.26924 0.63916 0.48203  -0.07830 -0.01706 343 SER A C   
287  O O   . SER A 24  ? 1.28627 1.31401 0.65856 0.49924  -0.07208 -0.01387 343 SER A O   
288  C CB  . SER A 24  ? 1.69902 1.74102 1.10570 0.49128  -0.10060 -0.02092 343 SER A CB  
289  O OG  . SER A 24  ? 1.23983 1.28307 0.67680 0.46944  -0.08580 -0.00521 343 SER A OG  
295  N N   . TRP A 25  ? 0.92936 0.96837 0.36778 0.45970  -0.06358 -0.00617 344 TRP A N   
296  C CA  . TRP A 25  ? 0.92321 0.95377 0.35830 0.45549  -0.03963 0.00962  344 TRP A CA  
297  C C   . TRP A 25  ? 0.89324 0.92873 0.35151 0.44289  -0.04038 0.00127  344 TRP A C   
298  O O   . TRP A 25  ? 0.92195 0.95403 0.37016 0.44811  -0.02839 0.00493  344 TRP A O   
299  C CB  . TRP A 25  ? 0.92248 0.94377 0.36635 0.44364  -0.01697 0.03503  344 TRP A CB  
300  C CG  . TRP A 25  ? 1.12385 1.14963 0.60831 0.41918  -0.01360 0.04011  344 TRP A CG  
301  C CD1 . TRP A 25  ? 1.84862 1.88187 1.35284 0.40978  -0.02642 0.03461  344 TRP A CD1 
302  C CD2 . TRP A 25  ? 1.04843 1.07130 0.55701 0.40172  0.00347  0.05147  344 TRP A CD2 
303  N NE1 . TRP A 25  ? 1.08783 1.12147 0.62491 0.38658  -0.01748 0.04280  344 TRP A NE1 
304  C CE2 . TRP A 25  ? 1.10499 1.13125 0.64543 0.38131  0.00015  0.05283  344 TRP A CE2 
305  C CE3 . TRP A 25  ? 1.10635 1.12479 0.61217 0.40232  0.02061  0.06000  344 TRP A CE3 
306  C CZ2 . TRP A 25  ? 1.03395 1.05634 0.60165 0.36144  0.01253  0.06225  344 TRP A CZ2 
307  C CZ3 . TRP A 25  ? 1.37792 1.39463 0.91307 0.38392  0.03217  0.06855  344 TRP A CZ3 
308  C CH2 . TRP A 25  ? 1.08057 1.09782 0.64550 0.36360  0.02771  0.06952  344 TRP A CH2 
319  N N   . ILE A 26  ? 0.89797 0.94038 0.38457 0.42686  -0.05520 -0.01031 345 ILE A N   
320  C CA  . ILE A 26  ? 0.84781 0.88955 0.35025 0.41597  -0.06132 -0.02126 345 ILE A CA  
321  C C   . ILE A 26  ? 0.90256 0.94819 0.39283 0.42842  -0.08537 -0.04755 345 ILE A C   
322  O O   . ILE A 26  ? 0.88518 0.93871 0.38107 0.42798  -0.10630 -0.06295 345 ILE A O   
323  C CB  . ILE A 26  ? 0.83204 0.87405 0.36741 0.38978  -0.06496 -0.01920 345 ILE A CB  
324  C CG1 . ILE A 26  ? 0.80695 0.84319 0.35651 0.37688  -0.04095 0.00554  345 ILE A CG1 
325  C CG2 . ILE A 26  ? 0.86937 0.90475 0.41473 0.37917  -0.07706 -0.03344 345 ILE A CG2 
326  C CD1 . ILE A 26  ? 0.71955 0.75654 0.29575 0.35476  -0.04348 0.00974  345 ILE A CD1 
338  N N   . ILE A 27  ? 0.94737 0.98841 0.42356 0.43918  -0.08286 -0.05372 346 ILE A N   
339  C CA  . ILE A 27  ? 1.04703 1.08911 0.51176 0.45154  -0.10477 -0.07934 346 ILE A CA  
340  C C   . ILE A 27  ? 1.00058 1.03733 0.48989 0.43299  -0.12271 -0.09577 346 ILE A C   
341  O O   . ILE A 27  ? 1.01500 1.05391 0.50880 0.43231  -0.14724 -0.11784 346 ILE A O   
342  C CB  . ILE A 27  ? 1.06862 1.10819 0.50738 0.47112  -0.09392 -0.07907 346 ILE A CB  
343  C CG1 . ILE A 27  ? 1.20167 1.24196 0.61130 0.48669  -0.07497 -0.06059 346 ILE A CG1 
344  C CG2 . ILE A 27  ? 1.18248 1.22195 0.61020 0.48440  -0.11738 -0.10714 346 ILE A CG2 
345  C CD1 . ILE A 27  ? 1.20164 1.24076 0.59123 0.49752  -0.05463 -0.05173 346 ILE A CD1 
357  N N   . ALA A 28  ? 0.84992 0.87724 0.35374 0.41800  -0.11095 -0.08506 347 ALA A N   
358  C CA  . ALA A 28  ? 0.82909 0.84354 0.35163 0.39857  -0.12666 -0.09713 347 ALA A CA  
359  C C   . ALA A 28  ? 0.82278 0.82777 0.36186 0.37904  -0.11076 -0.07719 347 ALA A C   
360  O O   . ALA A 28  ? 0.78041 0.78783 0.31624 0.38448  -0.08714 -0.05804 347 ALA A O   
361  C CB  . ALA A 28  ? 0.85399 0.85764 0.36646 0.40992  -0.13836 -0.11647 347 ALA A CB  
367  N N   . PRO A 29  ? 0.75988 0.75273 0.31687 0.35489  -0.12346 -0.08058 348 PRO A N   
368  C CA  . PRO A 29  ? 0.77161 0.76166 0.33507 0.34492  -0.15104 -0.10267 348 PRO A CA  
369  C C   . PRO A 29  ? 0.77068 0.78320 0.34198 0.34324  -0.15693 -0.10419 348 PRO A C   
370  O O   . PRO A 29  ? 0.75783 0.78295 0.32996 0.34713  -0.13987 -0.08622 348 PRO A O   
371  C CB  . PRO A 29  ? 0.74973 0.71611 0.32623 0.31825  -0.15771 -0.09988 348 PRO A CB  
372  C CG  . PRO A 29  ? 0.71662 0.68629 0.30078 0.31090  -0.13300 -0.07210 348 PRO A CG  
373  C CD  . PRO A 29  ? 0.72476 0.70533 0.29655 0.33460  -0.11156 -0.06211 348 PRO A CD  
381  N N   . LYS A 30  ? 0.78586 0.80239 0.36519 0.33679  -0.18221 -0.12696 349 LYS A N   
382  C CA  . LYS A 30  ? 0.78665 0.82754 0.37804 0.33555  -0.19238 -0.13364 349 LYS A CA  
383  C C   . LYS A 30  ? 0.75276 0.79921 0.36531 0.31114  -0.19020 -0.12379 349 LYS A C   
384  O O   . LYS A 30  ? 0.74459 0.81411 0.36706 0.31398  -0.18872 -0.11999 349 LYS A O   
385  C CB  . LYS A 30  ? 0.81666 0.86251 0.41412 0.33636  -0.22094 -0.16430 349 LYS A CB  
386  C CG  . LYS A 30  ? 1.00267 1.04873 0.57746 0.36515  -0.22485 -0.17544 349 LYS A CG  
387  C CD  . LYS A 30  ? 1.04235 1.10614 0.60089 0.38937  -0.21402 -0.16539 349 LYS A CD  
388  C CE  . LYS A 30  ? 1.13032 1.19497 0.66431 0.41705  -0.22276 -0.17984 349 LYS A CE  
389  N NZ  . LYS A 30  ? 1.12493 1.20170 0.63993 0.43873  -0.21586 -0.17105 349 LYS A NZ  
403  N N   . GLU A 31  ? 0.73792 0.76125 0.35517 0.28851  -0.19145 -0.12102 350 GLU A N   
404  C CA  . GLU A 31  ? 0.71166 0.73510 0.34362 0.26364  -0.19019 -0.11302 350 GLU A CA  
405  C C   . GLU A 31  ? 0.69628 0.68612 0.31965 0.25070  -0.17720 -0.09469 350 GLU A C   
406  O O   . GLU A 31  ? 0.70966 0.67538 0.32104 0.25618  -0.17839 -0.09746 350 GLU A O   
407  C CB  . GLU A 31  ? 0.73656 0.76209 0.38429 0.24063  -0.21596 -0.13983 350 GLU A CB  
408  C CG  . GLU A 31  ? 0.87775 0.93800 0.54244 0.25005  -0.23321 -0.16307 350 GLU A CG  
409  C CD  . GLU A 31  ? 1.11620 1.18682 0.80883 0.22159  -0.25471 -0.19045 350 GLU A CD  
410  O OE1 . GLU A 31  ? 1.00944 1.05351 0.71742 0.18631  -0.24499 -0.18435 350 GLU A OE1 
411  O OE2 . GLU A 31  ? 0.99686 1.09755 0.71050 0.22765  -0.27062 -0.21261 350 GLU A OE2 
418  N N   . TYR A 32  ? 0.67094 0.65882 0.30087 0.23470  -0.16631 -0.07755 351 TYR A N   
419  C CA  . TYR A 32  ? 0.68749 0.63888 0.31419 0.21790  -0.15561 -0.06138 351 TYR A CA  
420  C C   . TYR A 32  ? 0.68190 0.62746 0.33336 0.18434  -0.14576 -0.05254 351 TYR A C   
421  O O   . TYR A 32  ? 0.63144 0.60756 0.30161 0.17936  -0.14423 -0.05653 351 TYR A O   
422  C CB  . TYR A 32  ? 0.64397 0.59399 0.26613 0.23499  -0.13196 -0.03865 351 TYR A CB  
423  C CG  . TYR A 32  ? 0.61485 0.58029 0.25062 0.23226  -0.10989 -0.01586 351 TYR A CG  
424  C CD1 . TYR A 32  ? 0.61140 0.60930 0.25508 0.24374  -0.10577 -0.01568 351 TYR A CD1 
425  C CD2 . TYR A 32  ? 0.63147 0.57590 0.27338 0.21823  -0.09489 0.00393  351 TYR A CD2 
426  C CE1 . TYR A 32  ? 0.58850 0.59648 0.24507 0.24156  -0.08728 0.00322  351 TYR A CE1 
427  C CE2 . TYR A 32  ? 0.56853 0.52555 0.22642 0.21444  -0.07522 0.02236  351 TYR A CE2 
428  C CZ  . TYR A 32  ? 0.56618 0.55421 0.23087 0.22619  -0.07153 0.02183  351 TYR A CZ  
429  O OH  . TYR A 32  ? 0.54523 0.54233 0.22511 0.22321  -0.05469 0.03759  351 TYR A OH  
439  N N   . GLU A 33  ? 0.63750 0.54239 0.28760 0.16233  -0.14060 -0.04279 352 GLU A N   
440  C CA  . GLU A 33  ? 0.62734 0.51749 0.29183 0.13029  -0.12878 -0.03194 352 GLU A CA  
441  C C   . GLU A 33  ? 0.59599 0.49170 0.26033 0.13856  -0.10776 -0.00601 352 GLU A C   
442  O O   . GLU A 33  ? 0.59274 0.46237 0.24557 0.14352  -0.10219 0.00793  352 GLU A O   
443  C CB  . GLU A 33  ? 0.65746 0.49349 0.31213 0.10427  -0.13707 -0.03473 352 GLU A CB  
444  C CG  . GLU A 33  ? 0.74074 0.55220 0.40040 0.06994  -0.12453 -0.02282 352 GLU A CG  
445  C CD  . GLU A 33  ? 0.80249 0.64338 0.48614 0.04774  -0.11829 -0.03267 352 GLU A CD  
446  O OE1 . GLU A 33  ? 0.89031 0.72885 0.58184 0.03033  -0.13045 -0.05306 352 GLU A OE1 
447  O OE2 . GLU A 33  ? 0.70183 0.57046 0.39924 0.04882  -0.10155 -0.02169 352 GLU A OE2 
454  N N   . ALA A 34  ? 0.57734 0.50782 0.25716 0.14062  -0.09758 -0.00145 353 ALA A N   
455  C CA  . ALA A 34  ? 0.55331 0.49018 0.23423 0.14896  -0.07882 0.02173  353 ALA A CA  
456  C C   . ALA A 34  ? 0.54377 0.45726 0.23370 0.11806  -0.06708 0.03168  353 ALA A C   
457  O O   . ALA A 34  ? 0.56083 0.46281 0.24771 0.12025  -0.05372 0.05128  353 ALA A O   
458  C CB  . ALA A 34  ? 0.54384 0.52541 0.23416 0.16883  -0.07611 0.02094  353 ALA A CB  
464  N N   . TYR A 35  ? 0.56794 0.47425 0.26788 0.08891  -0.07170 0.01729  354 TYR A N   
465  C CA  . TYR A 35  ? 0.59282 0.48356 0.29997 0.05781  -0.05840 0.02338  354 TYR A CA  
466  C C   . TYR A 35  ? 0.63904 0.56711 0.36560 0.06464  -0.04332 0.03023  354 TYR A C   
467  O O   . TYR A 35  ? 0.52677 0.48609 0.25741 0.09414  -0.04387 0.03367  354 TYR A O   
468  C CB  . TYR A 35  ? 0.62771 0.46594 0.31266 0.04687  -0.05454 0.04035  354 TYR A CB  
469  C CG  . TYR A 35  ? 0.67221 0.46734 0.33760 0.03861  -0.07137 0.03262  354 TYR A CG  
470  C CD1 . TYR A 35  ? 0.71537 0.48323 0.37560 0.00664  -0.07721 0.02077  354 TYR A CD1 
471  C CD2 . TYR A 35  ? 0.69598 0.47654 0.34842 0.06245  -0.08107 0.03625  354 TYR A CD2 
472  C CE1 . TYR A 35  ? 0.78416 0.50651 0.42379 -0.00005 -0.09500 0.01371  354 TYR A CE1 
473  C CE2 . TYR A 35  ? 0.67075 0.41104 0.30649 0.05762  -0.09875 0.02704  354 TYR A CE2 
474  C CZ  . TYR A 35  ? 0.74699 0.45588 0.37488 0.02699  -0.10709 0.01620  354 TYR A CZ  
475  O OH  . TYR A 35  ? 0.86172 0.52533 0.47065 0.02302  -0.12671 0.00718  354 TYR A OH  
485  N N   . GLU A 36  ? 0.52828 0.45082 0.26442 0.03696  -0.03007 0.03117  355 GLU A N   
486  C CA  . GLU A 36  ? 0.50711 0.45790 0.26067 0.04130  -0.01480 0.03780  355 GLU A CA  
487  C C   . GLU A 36  ? 0.59521 0.51483 0.34151 0.01120  0.00107  0.04660  355 GLU A C   
488  O O   . GLU A 36  ? 0.60251 0.48485 0.33332 -0.01677 -0.00010 0.04340  355 GLU A O   
489  C CB  . GLU A 36  ? 0.58319 0.58703 0.36999 0.04264  -0.01667 0.01657  355 GLU A CB  
490  C CG  . GLU A 36  ? 0.64100 0.64457 0.44152 0.00882  -0.01822 -0.00443 355 GLU A CG  
491  C CD  . GLU A 36  ? 0.72773 0.78834 0.56980 0.00747  -0.01957 -0.02891 355 GLU A CD  
492  O OE1 . GLU A 36  ? 0.70036 0.80008 0.55935 0.03460  -0.02035 -0.02936 355 GLU A OE1 
493  O OE2 . GLU A 36  ? 0.92177 0.98679 0.78038 -0.02102 -0.02071 -0.04850 355 GLU A OE2 
500  N N   . CYS A 37  ? 0.59963 0.53286 0.35458 0.01739  0.01511  0.05676  356 CYS A N   
501  C CA  . CYS A 37  ? 0.62822 0.53519 0.37456 -0.00801 0.03120  0.06428  356 CYS A CA  
502  C C   . CYS A 37  ? 0.61916 0.56593 0.39511 -0.02341 0.04472  0.04789  356 CYS A C   
503  O O   . CYS A 37  ? 0.56449 0.55604 0.36664 -0.00238 0.04646  0.04297  356 CYS A O   
504  C CB  . CYS A 37  ? 0.51482 0.40412 0.24933 0.00886  0.03698  0.08607  356 CYS A CB  
505  S SG  . CYS A 37  ? 0.53447 0.38036 0.24171 0.02387  0.02345  0.10227  356 CYS A SG  
510  N N   . ARG A 38  ? 0.55785 0.48728 0.32926 -0.06024 0.05402  0.03843  357 ARG A N   
511  C CA  . ARG A 38  ? 0.58522 0.55425 0.38814 -0.07981 0.06984  0.01962  357 ARG A CA  
512  C C   . ARG A 38  ? 0.60248 0.53607 0.38381 -0.11517 0.09119  0.02449  357 ARG A C   
513  O O   . ARG A 38  ? 0.60513 0.47926 0.34588 -0.13417 0.08951  0.03622  357 ARG A O   
514  C CB  . ARG A 38  ? 0.62775 0.62424 0.45550 -0.09341 0.06177  -0.00454 357 ARG A CB  
515  C CG  . ARG A 38  ? 0.79465 0.83376 0.64562 -0.05780 0.04083  -0.01416 357 ARG A CG  
516  C CD  . ARG A 38  ? 1.05984 1.13328 0.94258 -0.07081 0.03210  -0.04224 357 ARG A CD  
517  N NE  . ARG A 38  ? 1.56229 1.67879 1.48612 -0.09321 0.04951  -0.06290 357 ARG A NE  
518  C CZ  . ARG A 38  ? 1.10499 1.28630 1.07595 -0.07548 0.04512  -0.08378 357 ARG A CZ  
519  N NH1 . ARG A 38  ? 0.82466 1.03064 0.80035 -0.03268 0.02579  -0.08199 357 ARG A NH1 
520  N NH2 . ARG A 38  ? 1.02600 1.24740 1.03949 -0.10114 0.06074  -0.10750 357 ARG A NH2 
534  N N   . GLY A 39  ? 0.82733 0.77928 0.56309 -0.43089 0.28995  -0.27453 358 GLY A N   
535  C CA  . GLY A 39  ? 0.86098 0.73909 0.57283 -0.41327 0.29999  -0.25898 358 GLY A CA  
536  C C   . GLY A 39  ? 0.86391 0.78946 0.58307 -0.37889 0.25598  -0.22864 358 GLY A C   
537  O O   . GLY A 39  ? 0.90571 0.91254 0.64943 -0.36731 0.22232  -0.21653 358 GLY A O   
541  N N   . GLY A 40  ? 0.92479 0.79667 0.62045 -0.36245 0.26088  -0.21342 359 GLY A N   
542  C CA  . GLY A 40  ? 0.82695 0.74686 0.53443 -0.33079 0.22619  -0.18185 359 GLY A CA  
543  C C   . GLY A 40  ? 0.72756 0.59440 0.42040 -0.27894 0.21154  -0.15117 359 GLY A C   
544  O O   . GLY A 40  ? 0.94127 0.71728 0.61361 -0.25766 0.22709  -0.14938 359 GLY A O   
548  N N   . CYS A 41  ? 0.63452 0.56405 0.35679 -0.25422 0.17355  -0.12401 360 CYS A N   
549  C CA  . CYS A 41  ? 0.66152 0.54800 0.37924 -0.20622 0.14849  -0.09163 360 CYS A CA  
550  C C   . CYS A 41  ? 0.74653 0.62632 0.45727 -0.20423 0.14595  -0.07760 360 CYS A C   
551  O O   . CYS A 41  ? 0.93299 0.89131 0.68145 -0.20712 0.13164  -0.07224 360 CYS A O   
552  C CB  . CYS A 41  ? 0.63205 0.58828 0.38367 -0.18797 0.11600  -0.07917 360 CYS A CB  
553  S SG  . CYS A 41  ? 0.60579 0.56709 0.36345 -0.19874 0.12917  -0.10494 360 CYS A SG  
558  N N   . PHE A 42  ? 0.65221 0.44433 0.31828 -0.20766 0.16685  -0.07622 361 PHE A N   
559  C CA  . PHE A 42  ? 0.66237 0.43990 0.31328 -0.21494 0.17324  -0.06990 361 PHE A CA  
560  C C   . PHE A 42  ? 0.77086 0.44139 0.36020 -0.20531 0.17970  -0.05152 361 PHE A C   
561  O O   . PHE A 42  ? 0.78691 0.39223 0.35053 -0.19884 0.18896  -0.04756 361 PHE A O   
562  C CB  . PHE A 42  ? 0.71620 0.52942 0.37784 -0.25594 0.20156  -0.09744 361 PHE A CB  
563  C CG  . PHE A 42  ? 0.74816 0.50479 0.37821 -0.28700 0.23227  -0.12274 361 PHE A CG  
564  C CD1 . PHE A 42  ? 0.91771 0.71654 0.57001 -0.30929 0.23889  -0.14717 361 PHE A CD1 
565  C CD2 . PHE A 42  ? 0.92592 0.59013 0.50589 -0.29794 0.25298  -0.12496 361 PHE A CD2 
566  C CE1 . PHE A 42  ? 1.02170 0.76122 0.64681 -0.34130 0.27030  -0.17442 361 PHE A CE1 
567  C CE2 . PHE A 42  ? 1.01489 0.61914 0.56307 -0.32574 0.28352  -0.15000 361 PHE A CE2 
568  C CZ  . PHE A 42  ? 1.08031 0.71849 0.65253 -0.34850 0.29466  -0.17587 361 PHE A CZ  
578  N N   . PHE A 43  ? 0.74143 0.39535 0.30899 -0.20536 0.17622  -0.03874 362 PHE A N   
579  C CA  . PHE A 43  ? 0.90427 0.46884 0.40728 -0.20274 0.17654  -0.01624 362 PHE A CA  
580  C C   . PHE A 43  ? 0.95932 0.46789 0.43081 -0.22901 0.20465  -0.03473 362 PHE A C   
581  O O   . PHE A 43  ? 0.95269 0.49623 0.44648 -0.25574 0.22406  -0.06531 362 PHE A O   
582  C CB  . PHE A 43  ? 0.79673 0.37851 0.29892 -0.19607 0.15754  -0.00633 362 PHE A CB  
583  C CG  . PHE A 43  ? 0.76798 0.39522 0.29378 -0.17027 0.12950  0.01111  362 PHE A CG  
584  C CD1 . PHE A 43  ? 0.77859 0.38490 0.28635 -0.14527 0.10425  0.03854  362 PHE A CD1 
585  C CD2 . PHE A 43  ? 0.67684 0.37093 0.24928 -0.16900 0.12877  0.00067  362 PHE A CD2 
586  C CE1 . PHE A 43  ? 0.70274 0.36156 0.24132 -0.12276 0.07607  0.04803  362 PHE A CE1 
587  C CE2 . PHE A 43  ? 0.72845 0.46320 0.32752 -0.14495 0.10156  0.01350  362 PHE A CE2 
588  C CZ  . PHE A 43  ? 0.69880 0.41700 0.27780 -0.12514 0.07595  0.03425  362 PHE A CZ  
598  N N   . PRO A 44  ? 1.01145 0.43792 0.43474 -0.21978 0.20574  -0.01511 363 PRO A N   
599  C CA  . PRO A 44  ? 0.98082 0.37854 0.39378 -0.18368 0.17797  0.02565  363 PRO A CA  
600  C C   . PRO A 44  ? 1.00951 0.39384 0.44760 -0.16619 0.18566  0.02812  363 PRO A C   
601  O O   . PRO A 44  ? 1.06890 0.43306 0.51494 -0.18450 0.21853  -0.00005 363 PRO A O   
602  C CB  . PRO A 44  ? 1.07454 0.40240 0.43964 -0.18297 0.17865  0.04605  363 PRO A CB  
603  C CG  . PRO A 44  ? 1.12560 0.41900 0.47368 -0.21378 0.21966  0.01177  363 PRO A CG  
604  C CD  . PRO A 44  ? 1.04939 0.41517 0.43143 -0.24134 0.23256  -0.02891 363 PRO A CD  
612  N N   . LEU A 45  ? 1.08839 0.50737 0.55704 -0.12785 0.15140  0.05095  364 LEU A N   
613  C CA  . LEU A 45  ? 1.20380 0.64371 0.72399 -0.10350 0.15206  0.04115  364 LEU A CA  
614  C C   . LEU A 45  ? 1.43770 0.78523 0.94663 -0.08068 0.16897  0.06234  364 LEU A C   
615  O O   . LEU A 45  ? 1.33867 0.61749 0.80170 -0.07229 0.16308  0.10097  364 LEU A O   
616  C CB  . LEU A 45  ? 1.05853 0.57555 0.61852 -0.07445 0.11218  0.05443  364 LEU A CB  
617  C CG  . LEU A 45  ? 0.91126 0.51575 0.49557 -0.09119 0.10021  0.03405  364 LEU A CG  
618  C CD1 . LEU A 45  ? 0.82425 0.48639 0.43502 -0.06654 0.06520  0.04937  364 LEU A CD1 
619  C CD2 . LEU A 45  ? 0.87107 0.52306 0.49127 -0.11362 0.12092  -0.00389 364 LEU A CD2 
631  N N   . ALA A 46  ? 1.58879 0.93458 1.14017 -0.07244 0.19214  0.03788  365 ALA A N   
632  C CA  . ALA A 46  ? 2.09176 1.35018 1.65178 -0.04277 0.21453  0.05581  365 ALA A CA  
633  C C   . ALA A 46  ? 1.78269 1.06920 1.38388 0.01217  0.17575  0.09751  365 ALA A C   
634  O O   . ALA A 46  ? 1.67070 1.04789 1.29403 0.02042  0.13706  0.10117  365 ALA A O   
635  C CB  . ALA A 46  ? 1.46052 0.70460 1.05101 -0.06183 0.26374  0.00532  365 ALA A CB  
641  N N   . ASP A 47  ? 1.47150 0.67948 1.08672 0.05025  0.18849  0.13047  366 ASP A N   
642  C CA  . ASP A 47  ? 1.90230 1.14234 1.56173 0.10506  0.14933  0.17855  366 ASP A CA  
643  C C   . ASP A 47  ? 2.04265 1.36785 1.77979 0.12354  0.14600  0.14804  366 ASP A C   
644  O O   . ASP A 47  ? 1.69608 1.09550 1.46569 0.15209  0.10300  0.17427  366 ASP A O   
645  C CB  . ASP A 47  ? 1.41884 0.56770 1.09242 0.14492  0.16295  0.22411  366 ASP A CB  
646  C CG  . ASP A 47  ? 2.28013 1.40274 1.89513 0.12549  0.14019  0.26181  366 ASP A CG  
647  O OD1 . ASP A 47  ? 2.47473 1.63709 2.03525 0.09161  0.11459  0.26239  366 ASP A OD1 
648  O OD2 . ASP A 47  ? 2.50270 1.56465 2.13024 0.14262  0.15161  0.28785  366 ASP A OD2 
653  N N   . ASP A 48  ? 1.34082 0.66156 1.10365 0.10102  0.19150  0.09114  367 ASP A N   
654  C CA  . ASP A 48  ? 1.55627 0.93967 1.39103 0.11645  0.19927  0.06110  367 ASP A CA  
655  C C   . ASP A 48  ? 1.93428 1.39743 1.76413 0.06611  0.20481  0.00472  367 ASP A C   
656  O O   . ASP A 48  ? 1.16707 0.65148 1.03522 0.05402  0.23654  -0.03876 367 ASP A O   
657  C CB  . ASP A 48  ? 1.77285 1.07356 1.65518 0.13998  0.25633  0.04671  367 ASP A CB  
658  C CG  . ASP A 48  ? 1.98058 1.20337 1.82306 0.08977  0.31801  -0.00157 367 ASP A CG  
659  O OD1 . ASP A 48  ? 1.70889 0.94447 1.48894 0.04247  0.31027  -0.01466 367 ASP A OD1 
660  O OD2 . ASP A 48  ? 2.45495 1.60408 2.33099 0.09718  0.37645  -0.02621 367 ASP A OD2 
665  N N   . VAL A 49  ? 1.31034 0.82025 1.09512 0.03463  0.17616  0.00546  368 VAL A N   
666  C CA  . VAL A 49  ? 1.12793 0.72931 0.91896 -0.00234 0.16891  -0.03202 368 VAL A CA  
667  C C   . VAL A 49  ? 1.78418 1.47237 1.60242 0.01827  0.12332  -0.01522 368 VAL A C   
668  O O   . VAL A 49  ? 0.87943 0.64284 0.69989 -0.00785 0.10993  -0.03477 368 VAL A O   
669  C CB  . VAL A 49  ? 1.44834 1.06065 1.19230 -0.04669 0.16957  -0.04394 368 VAL A CB  
670  C CG1 . VAL A 49  ? 1.19341 0.72581 0.91005 -0.07543 0.21985  -0.06823 368 VAL A CG1 
671  C CG2 . VAL A 49  ? 0.99337 0.60557 0.70331 -0.03606 0.13318  -0.00480 368 VAL A CG2 
681  N N   . THR A 50  ? 0.82954 0.51092 0.66900 0.06296  0.09959  0.02287  369 THR A N   
682  C CA  . THR A 50  ? 0.85389 0.61488 0.72290 0.08280  0.06093  0.03767  369 THR A CA  
683  C C   . THR A 50  ? 0.71566 0.54251 0.55622 0.05164  0.03429  0.03035  369 THR A C   
684  O O   . THR A 50  ? 0.76784 0.66221 0.63208 0.04095  0.02705  0.01023  369 THR A O   
685  C CB  . THR A 50  ? 1.91558 1.71193 1.84904 0.09639  0.07967  0.01056  369 THR A CB  
686  O OG1 . THR A 50  ? 0.90632 0.73422 0.83502 0.05212  0.10336  -0.03789 369 THR A OG1 
687  C CG2 . THR A 50  ? 1.35424 1.07474 1.32726 0.13117  0.11632  0.01586  369 THR A CG2 
695  N N   . PRO A 51  ? 0.80236 0.60717 0.59384 0.03623  0.02319  0.04646  370 PRO A N   
696  C CA  . PRO A 51  ? 0.64568 0.50159 0.42039 0.00845  0.00938  0.03661  370 PRO A CA  
697  C C   . PRO A 51  ? 0.53842 0.44807 0.31742 0.01811  -0.02446 0.05362  370 PRO A C   
698  O O   . PRO A 51  ? 0.68304 0.58219 0.44620 0.03409  -0.04461 0.08266  370 PRO A O   
699  C CB  . PRO A 51  ? 0.64415 0.45121 0.37223 -0.00821 0.01653  0.04619  370 PRO A CB  
700  C CG  . PRO A 51  ? 0.74209 0.48687 0.44801 0.01401  0.01287  0.07745  370 PRO A CG  
701  C CD  . PRO A 51  ? 0.73850 0.47006 0.48850 0.04282  0.02455  0.07596  370 PRO A CD  
709  N N   . THR A 52  ? 0.60707 0.57639 0.40359 0.00362  -0.03030 0.03640  371 THR A N   
710  C CA  . THR A 52  ? 0.53343 0.54606 0.32401 0.00207  -0.05575 0.04782  371 THR A CA  
711  C C   . THR A 52  ? 0.47393 0.45998 0.22265 -0.01067 -0.06024 0.06245  371 THR A C   
712  O O   . THR A 52  ? 0.48554 0.43492 0.21754 -0.02140 -0.04369 0.05920  371 THR A O   
713  C CB  . THR A 52  ? 0.47994 0.54901 0.28997 -0.01554 -0.05669 0.02927  371 THR A CB  
714  O OG1 . THR A 52  ? 0.42708 0.49351 0.23030 -0.03599 -0.04457 0.02175  371 THR A OG1 
715  C CG2 . THR A 52  ? 0.44764 0.54763 0.29552 -0.01231 -0.04665 0.00709  371 THR A CG2 
723  N N   . LYS A 53  ? 0.48717 0.54884 0.34526 -0.06952 -0.01791 0.10216  372 LYS A N   
724  C CA  . LYS A 53  ? 0.48785 0.53556 0.32128 -0.08882 -0.02306 0.09960  372 LYS A CA  
725  C C   . LYS A 53  ? 0.43039 0.45942 0.24908 -0.09427 -0.01137 0.08683  372 LYS A C   
726  O O   . LYS A 53  ? 0.45828 0.46499 0.25671 -0.10224 -0.00939 0.08251  372 LYS A O   
727  C CB  . LYS A 53  ? 0.47813 0.55179 0.31587 -0.10466 -0.03396 0.10562  372 LYS A CB  
728  C CG  . LYS A 53  ? 0.51850 0.61937 0.37137 -0.09934 -0.05118 0.12028  372 LYS A CG  
729  C CD  . LYS A 53  ? 0.52368 0.64996 0.37393 -0.12188 -0.06645 0.12356  372 LYS A CD  
730  C CE  . LYS A 53  ? 0.59186 0.76572 0.47109 -0.11448 -0.08620 0.13890  372 LYS A CE  
731  N NZ  . LYS A 53  ? 0.51688 0.73552 0.44567 -0.10269 -0.08036 0.14207  372 LYS A NZ  
745  N N   . HIS A 54  ? 0.40654 0.44507 0.23478 -0.08812 -0.00265 0.08193  373 HIS A N   
746  C CA  . HIS A 54  ? 0.40267 0.42661 0.21607 -0.08858 0.00633  0.07265  373 HIS A CA  
747  C C   . HIS A 54  ? 0.40243 0.41137 0.21056 -0.08248 0.00763  0.06479  373 HIS A C   
748  O O   . HIS A 54  ? 0.42120 0.41928 0.21808 -0.08745 0.01027  0.05999  373 HIS A O   
749  C CB  . HIS A 54  ? 0.39971 0.43275 0.21745 -0.08103 0.01552  0.07053  373 HIS A CB  
750  C CG  . HIS A 54  ? 0.40347 0.42193 0.20142 -0.08041 0.02288  0.06534  373 HIS A CG  
751  N ND1 . HIS A 54  ? 0.43330 0.44596 0.22502 -0.07043 0.02283  0.05786  373 HIS A ND1 
752  C CD2 . HIS A 54  ? 0.42039 0.42897 0.20354 -0.08801 0.03049  0.06735  373 HIS A CD2 
753  C CE1 . HIS A 54  ? 0.40947 0.41345 0.18557 -0.06850 0.02875  0.05774  373 HIS A CE1 
754  N NE2 . HIS A 54  ? 0.41861 0.41469 0.18641 -0.07816 0.03549  0.06364  373 HIS A NE2 
762  N N   . ALA A 55  ? 0.40563 0.41357 0.22293 -0.07271 0.00751  0.06314  374 ALA A N   
763  C CA  . ALA A 55  ? 0.41187 0.40437 0.22465 -0.07221 0.00961  0.05372  374 ALA A CA  
764  C C   . ALA A 55  ? 0.41942 0.39616 0.22345 -0.08337 0.00846  0.05533  374 ALA A C   
765  O O   . ALA A 55  ? 0.42051 0.39087 0.22214 -0.08902 0.01233  0.04642  374 ALA A O   
766  C CB  . ALA A 55  ? 0.42486 0.40940 0.24334 -0.06189 0.01291  0.05233  374 ALA A CB  
772  N N   . ILE A 56  ? 0.42819 0.40103 0.22734 -0.08691 0.00314  0.06703  375 ILE A N   
773  C CA  . ILE A 56  ? 0.44364 0.39641 0.22595 -0.09762 0.00325  0.07013  375 ILE A CA  
774  C C   . ILE A 56  ? 0.43910 0.38987 0.21068 -0.10845 0.00764  0.06564  375 ILE A C   
775  O O   . ILE A 56  ? 0.44538 0.38279 0.21118 -0.11439 0.01569  0.05983  375 ILE A O   
776  C CB  . ILE A 56  ? 0.46090 0.41277 0.23584 -0.09682 -0.00698 0.08519  375 ILE A CB  
777  C CG1 . ILE A 56  ? 0.59054 0.53718 0.37509 -0.08089 -0.00686 0.09123  375 ILE A CG1 
778  C CG2 . ILE A 56  ? 0.48391 0.41253 0.23158 -0.10917 -0.00752 0.08940  375 ILE A CG2 
779  C CD1 . ILE A 56  ? 0.52251 0.48058 0.30877 -0.07242 -0.01932 0.10886  375 ILE A CD1 
791  N N   . VAL A 57  ? 0.44541 0.40792 0.21496 -0.11101 0.00517  0.06833  376 VAL A N   
792  C CA  . VAL A 57  ? 0.52138 0.47477 0.27654 -0.11884 0.01292  0.06497  376 VAL A CA  
793  C C   . VAL A 57  ? 0.53684 0.49420 0.30130 -0.11053 0.02182  0.05614  376 VAL A C   
794  O O   . VAL A 57  ? 0.44660 0.39343 0.20453 -0.11385 0.03087  0.05300  376 VAL A O   
795  C CB  . VAL A 57  ? 0.58575 0.54687 0.33637 -0.12388 0.01134  0.06845  376 VAL A CB  
796  C CG1 . VAL A 57  ? 0.57011 0.51646 0.30553 -0.12614 0.02426  0.06446  376 VAL A CG1 
797  C CG2 . VAL A 57  ? 0.51478 0.47561 0.25375 -0.13776 0.00078  0.07572  376 VAL A CG2 
807  N N   . GLN A 58  ? 0.42109 0.39592 0.20083 -0.09892 0.01919  0.05237  377 GLN A N   
808  C CA  . GLN A 58  ? 0.41509 0.40097 0.20328 -0.09031 0.02270  0.04452  377 GLN A CA  
809  C C   . GLN A 58  ? 0.41703 0.40360 0.21615 -0.09524 0.02469  0.03684  377 GLN A C   
810  O O   . GLN A 58  ? 0.47562 0.47093 0.28237 -0.09381 0.03012  0.03252  377 GLN A O   
811  C CB  . GLN A 58  ? 0.42057 0.42179 0.21486 -0.07845 0.01813  0.04142  377 GLN A CB  
812  C CG  . GLN A 58  ? 0.41265 0.42937 0.21121 -0.06876 0.01767  0.03472  377 GLN A CG  
813  C CD  . GLN A 58  ? 0.46165 0.48779 0.25397 -0.05649 0.01424  0.03325  377 GLN A CD  
814  O OE1 . GLN A 58  ? 0.41394 0.43288 0.19720 -0.05400 0.01746  0.03934  377 GLN A OE1 
815  N NE2 . GLN A 58  ? 0.41852 0.46280 0.21529 -0.04986 0.00780  0.02465  377 GLN A NE2 
824  N N   . THR A 59  ? 0.42164 0.39837 0.22247 -0.10081 0.02238  0.03589  378 THR A N   
825  C CA  . THR A 59  ? 0.44344 0.41374 0.25163 -0.10969 0.02797  0.02836  378 THR A CA  
826  C C   . THR A 59  ? 0.47092 0.42829 0.27166 -0.11886 0.03837  0.03109  378 THR A C   
827  O O   . THR A 59  ? 0.44334 0.40952 0.25881 -0.12384 0.04655  0.02322  378 THR A O   
828  C CB  . THR A 59  ? 0.46894 0.41938 0.27203 -0.11213 0.02718  0.02973  378 THR A CB  
829  O OG1 . THR A 59  ? 0.48077 0.44069 0.28923 -0.10214 0.02144  0.02626  378 THR A OG1 
830  C CG2 . THR A 59  ? 0.51662 0.45276 0.32389 -0.12443 0.03679  0.02084  378 THR A CG2 
838  N N   . LEU A 60  ? 0.47742 0.41550 0.25533 -0.12222 0.03866  0.04141  379 LEU A N   
839  C CA  . LEU A 60  ? 0.56392 0.48250 0.32513 -0.13111 0.05059  0.04366  379 LEU A CA  
840  C C   . LEU A 60  ? 0.55181 0.48261 0.32095 -0.12488 0.05995  0.04029  379 LEU A C   
841  O O   . LEU A 60  ? 0.50019 0.42705 0.27340 -0.12810 0.07449  0.03711  379 LEU A O   
842  C CB  . LEU A 60  ? 0.51427 0.40993 0.24340 -0.13806 0.04550  0.05399  379 LEU A CB  
843  C CG  . LEU A 60  ? 0.54883 0.42946 0.26551 -0.14121 0.03726  0.06153  379 LEU A CG  
844  C CD1 . LEU A 60  ? 0.62465 0.49716 0.31494 -0.14674 0.02567  0.07195  379 LEU A CD1 
845  C CD2 . LEU A 60  ? 0.55620 0.41086 0.26166 -0.14935 0.05048  0.06017  379 LEU A CD2 
857  N N   . VAL A 61  ? 0.46391 0.40816 0.23507 -0.11417 0.05398  0.04209  380 VAL A N   
858  C CA  . VAL A 61  ? 0.47406 0.42674 0.25004 -0.10292 0.06333  0.04162  380 VAL A CA  
859  C C   . VAL A 61  ? 0.57796 0.56450 0.38791 -0.09449 0.06356  0.03398  380 VAL A C   
860  O O   . VAL A 61  ? 0.49380 0.48829 0.31493 -0.08833 0.07596  0.03345  380 VAL A O   
861  C CB  . VAL A 61  ? 0.48255 0.43654 0.24832 -0.09293 0.05870  0.04646  380 VAL A CB  
862  C CG1 . VAL A 61  ? 0.47615 0.43558 0.24444 -0.07601 0.06924  0.04834  380 VAL A CG1 
863  C CG2 . VAL A 61  ? 0.54212 0.46853 0.27883 -0.10579 0.05926  0.05204  380 VAL A CG2 
873  N N   . HIS A 62  ? 0.44262 0.45032 0.26933 -0.09458 0.05034  0.02755  381 HIS A N   
874  C CA  . HIS A 62  ? 0.44490 0.48792 0.30356 -0.09306 0.04726  0.01722  381 HIS A CA  
875  C C   . HIS A 62  ? 0.42344 0.46591 0.29784 -0.10589 0.06164  0.01247  381 HIS A C   
876  O O   . HIS A 62  ? 0.49510 0.56972 0.39872 -0.10132 0.06687  0.00807  381 HIS A O   
877  C CB  . HIS A 62  ? 0.40557 0.45810 0.26993 -0.09781 0.03377  0.00846  381 HIS A CB  
878  C CG  . HIS A 62  ? 0.43818 0.52401 0.33291 -0.10495 0.03052  -0.00563 381 HIS A CG  
879  N ND1 . HIS A 62  ? 0.42979 0.55893 0.34442 -0.09312 0.02050  -0.01012 381 HIS A ND1 
880  C CD2 . HIS A 62  ? 0.41557 0.49751 0.32286 -0.12401 0.03624  -0.01595 381 HIS A CD2 
881  C CE1 . HIS A 62  ? 0.43811 0.59495 0.38082 -0.10759 0.01809  -0.02458 381 HIS A CE1 
882  N NE2 . HIS A 62  ? 0.42369 0.55047 0.36261 -0.12783 0.02936  -0.02923 381 HIS A NE2 
890  N N   . LEU A 63  ? 0.43401 0.44107 0.28913 -0.12093 0.06905  0.01453  382 LEU A N   
891  C CA  . LEU A 63  ? 0.45033 0.44905 0.31399 -0.13453 0.08670  0.01073  382 LEU A CA  
892  C C   . LEU A 63  ? 0.46886 0.46971 0.33575 -0.12726 0.10389  0.01480  382 LEU A C   
893  O O   . LEU A 63  ? 0.50115 0.52457 0.39823 -0.13019 0.11744  0.00901  382 LEU A O   
894  C CB  . LEU A 63  ? 0.53148 0.48331 0.36186 -0.14837 0.09236  0.01610  382 LEU A CB  
895  C CG  . LEU A 63  ? 0.70718 0.64850 0.53548 -0.15570 0.08397  0.01253  382 LEU A CG  
896  C CD1 . LEU A 63  ? 0.81208 0.70578 0.60535 -0.16515 0.09179  0.02135  382 LEU A CD1 
897  C CD2 . LEU A 63  ? 0.87159 0.83891 0.73467 -0.16595 0.08773  -0.00287 382 LEU A CD2 
909  N N   . LYS A 64  ? 0.55141 0.52775 0.38763 -0.11859 0.10552  0.02421  383 LYS A N   
910  C CA  . LYS A 64  ? 0.63308 0.59822 0.46256 -0.11084 0.12585  0.02836  383 LYS A CA  
911  C C   . LYS A 64  ? 0.60324 0.61080 0.46656 -0.08836 0.12562  0.02859  383 LYS A C   
912  O O   . LYS A 64  ? 0.64673 0.66361 0.52706 -0.07968 0.14494  0.02953  383 LYS A O   
913  C CB  . LYS A 64  ? 0.61348 0.53215 0.39311 -0.11310 0.12851  0.03632  383 LYS A CB  
914  C CG  . LYS A 64  ? 0.84547 0.72922 0.60004 -0.11390 0.15530  0.03872  383 LYS A CG  
915  C CD  . LYS A 64  ? 0.92202 0.77789 0.65962 -0.13229 0.17036  0.03644  383 LYS A CD  
916  C CE  . LYS A 64  ? 1.01225 0.83320 0.72737 -0.13011 0.19617  0.03638  383 LYS A CE  
917  N NZ  . LYS A 64  ? 1.05309 0.83678 0.73053 -0.13028 0.18357  0.03586  383 LYS A NZ  
931  N N   . PHE A 65  ? 0.59130 0.62437 0.46310 -0.07720 0.10456  0.02873  384 PHE A N   
932  C CA  . PHE A 65  ? 0.51065 0.58062 0.40479 -0.05243 0.10038  0.03204  384 PHE A CA  
933  C C   . PHE A 65  ? 0.54606 0.66492 0.46950 -0.05039 0.07654  0.02404  384 PHE A C   
934  O O   . PHE A 65  ? 0.53621 0.66003 0.44671 -0.03828 0.06155  0.02732  384 PHE A O   
935  C CB  . PHE A 65  ? 0.60326 0.64139 0.45999 -0.03806 0.10164  0.04277  384 PHE A CB  
936  C CG  . PHE A 65  ? 0.64909 0.63448 0.46972 -0.04244 0.12480  0.04846  384 PHE A CG  
937  C CD1 . PHE A 65  ? 0.86555 0.84468 0.69028 -0.02669 0.14817  0.05321  384 PHE A CD1 
938  C CD2 . PHE A 65  ? 0.65034 0.59311 0.43230 -0.06240 0.12355  0.04864  384 PHE A CD2 
939  C CE1 . PHE A 65  ? 1.19982 1.12230 0.98364 -0.03294 0.17207  0.05626  384 PHE A CE1 
940  C CE2 . PHE A 65  ? 0.76615 0.65928 0.50932 -0.07046 0.14323  0.05144  384 PHE A CE2 
941  C CZ  . PHE A 65  ? 0.81326 0.69223 0.55415 -0.05680 0.16848  0.05432  384 PHE A CZ  
951  N N   . PRO A 66  ? 0.50275 0.65568 0.46258 -0.06452 0.07381  0.01219  385 PRO A N   
952  C CA  . PRO A 66  ? 0.42242 0.61127 0.40080 -0.07104 0.05164  0.00064  385 PRO A CA  
953  C C   . PRO A 66  ? 0.53021 0.76986 0.52719 -0.04877 0.03364  0.00165  385 PRO A C   
954  O O   . PRO A 66  ? 0.49911 0.75388 0.49116 -0.05133 0.01345  -0.00584 385 PRO A O   
955  C CB  . PRO A 66  ? 0.40752 0.61574 0.41998 -0.09462 0.05989  -0.01256 385 PRO A CB  
956  C CG  . PRO A 66  ? 0.41677 0.62343 0.44337 -0.09005 0.08405  -0.00631 385 PRO A CG  
957  C CD  . PRO A 66  ? 0.42654 0.57924 0.40700 -0.07861 0.09464  0.00784  385 PRO A CD  
965  N N   . THR A 67  ? 0.47908 0.74372 0.49486 -0.02569 0.04144  0.01125  386 THR A N   
966  C CA  . THR A 67  ? 0.52275 0.83546 0.55237 0.00048  0.02318  0.01598  386 THR A CA  
967  C C   . THR A 67  ? 0.57243 0.85025 0.55497 0.02272  0.01886  0.02980  386 THR A C   
968  O O   . THR A 67  ? 0.67565 0.98451 0.65701 0.04348  0.00111  0.03410  386 THR A O   
969  C CB  . THR A 67  ? 0.47506 0.83380 0.54779 0.02164  0.03323  0.02307  386 THR A CB  
970  O OG1 . THR A 67  ? 0.59958 0.90888 0.64713 0.03740  0.06031  0.03793  386 THR A OG1 
971  C CG2 . THR A 67  ? 0.49366 0.89593 0.62046 -0.00109 0.03940  0.00887  386 THR A CG2 
979  N N   . LYS A 68  ? 0.62353 0.83784 0.56623 0.01700  0.03502  0.03653  387 LYS A N   
980  C CA  . LYS A 68  ? 0.60604 0.78266 0.50538 0.03410  0.03721  0.04934  387 LYS A CA  
981  C C   . LYS A 68  ? 0.62761 0.77394 0.49582 0.01804  0.02837  0.04497  387 LYS A C   
982  O O   . LYS A 68  ? 0.68708 0.82305 0.52859 0.03102  0.02217  0.05123  387 LYS A O   
983  C CB  . LYS A 68  ? 0.69938 0.82760 0.57646 0.04006  0.06474  0.06046  387 LYS A CB  
984  C CG  . LYS A 68  ? 0.87942 1.03007 0.78126 0.06524  0.07887  0.06891  387 LYS A CG  
985  C CD  . LYS A 68  ? 1.14589 1.23679 1.01407 0.07345  0.10930  0.07974  387 LYS A CD  
986  C CE  . LYS A 68  ? 1.64522 1.75408 1.53578 0.10495  0.12692  0.09045  387 LYS A CE  
987  N NZ  . LYS A 68  ? 1.26707 1.41581 1.20714 0.09604  0.13427  0.08201  387 LYS A NZ  
1001 N N   . VAL A 69  ? 0.49245 0.62344 0.36355 -0.00841 0.02987  0.03557  388 VAL A N   
1002 C CA  . VAL A 69  ? 0.55760 0.66227 0.40507 -0.02137 0.02401  0.03299  388 VAL A CA  
1003 C C   . VAL A 69  ? 0.46742 0.59120 0.33251 -0.03819 0.01155  0.01836  388 VAL A C   
1004 O O   . VAL A 69  ? 0.52675 0.65983 0.41450 -0.05255 0.01558  0.01075  388 VAL A O   
1005 C CB  . VAL A 69  ? 0.52459 0.58476 0.35107 -0.03511 0.03822  0.03835  388 VAL A CB  
1006 C CG1 . VAL A 69  ? 0.54140 0.58436 0.35205 -0.04591 0.03118  0.03723  388 VAL A CG1 
1007 C CG2 . VAL A 69  ? 0.67178 0.70538 0.47592 -0.02280 0.05380  0.05002  388 VAL A CG2 
1017 N N   . SER A 70  ? 0.46977 0.59286 0.32052 -0.03735 0.00009  0.01423  389 SER A N   
1018 C CA  . SER A 70  ? 0.48054 0.61219 0.34044 -0.05305 -0.00878 -0.00072 389 SER A CA  
1019 C C   . SER A 70  ? 0.47345 0.56885 0.32421 -0.06837 -0.00058 -0.00059 389 SER A C   
1020 O O   . SER A 70  ? 0.47443 0.54390 0.30961 -0.06631 0.00683  0.01072  389 SER A O   
1021 C CB  . SER A 70  ? 0.57523 0.71806 0.41881 -0.04467 -0.02246 -0.00637 389 SER A CB  
1022 O OG  . SER A 70  ? 0.76048 0.87254 0.57580 -0.03720 -0.01680 0.00285  389 SER A OG  
1028 N N   . LYS A 71  ? 0.53546 0.63023 0.39542 -0.08377 -0.00234 -0.01327 390 LYS A N   
1029 C CA  . LYS A 71  ? 0.58626 0.64518 0.43566 -0.09403 0.00519  -0.01143 390 LYS A CA  
1030 C C   . LYS A 71  ? 0.59720 0.64106 0.42729 -0.08536 0.00235  -0.00897 390 LYS A C   
1031 O O   . LYS A 71  ? 0.50188 0.56004 0.32393 -0.07554 -0.00472 -0.01243 390 LYS A O   
1032 C CB  . LYS A 71  ? 0.64834 0.70276 0.50795 -0.11217 0.00765  -0.02633 390 LYS A CB  
1033 C CG  . LYS A 71  ? 0.97704 1.06637 0.86451 -0.12286 0.00593  -0.03819 390 LYS A CG  
1034 C CD  . LYS A 71  ? 1.45934 1.58238 1.35353 -0.12433 -0.00892 -0.05376 390 LYS A CD  
1035 C CE  . LYS A 71  ? 0.75281 0.92941 0.67578 -0.11836 -0.01777 -0.05525 390 LYS A CE  
1036 N NZ  . LYS A 71  ? 0.59029 0.78145 0.49947 -0.09229 -0.02775 -0.04330 390 LYS A NZ  
1050 N N   . ALA A 72  ? 0.47898 0.49582 0.30160 -0.08743 0.00843  -0.00183 391 ALA A N   
1051 C CA  . ALA A 72  ? 0.46996 0.47394 0.28118 -0.07901 0.00935  0.00029  391 ALA A CA  
1052 C C   . ALA A 72  ? 0.57587 0.57471 0.38168 -0.08324 0.00883  -0.01646 391 ALA A C   
1053 O O   . ALA A 72  ? 0.55184 0.55264 0.36505 -0.09723 0.00842  -0.02882 391 ALA A O   
1054 C CB  . ALA A 72  ? 0.53537 0.51745 0.34548 -0.07896 0.01471  0.01198  391 ALA A CB  
1060 N N   . CYS A 73  ? 0.50368 0.49373 0.29551 -0.07311 0.01112  -0.01760 392 CYS A N   
1061 C CA  . CYS A 73  ? 0.58340 0.56252 0.36065 -0.07723 0.01207  -0.03508 392 CYS A CA  
1062 C C   . CYS A 73  ? 0.61742 0.55984 0.38523 -0.07330 0.02590  -0.03471 392 CYS A C   
1063 O O   . CYS A 73  ? 0.54487 0.48224 0.31568 -0.05910 0.03216  -0.01992 392 CYS A O   
1064 C CB  . CYS A 73  ? 0.63415 0.62925 0.39421 -0.06715 0.00554  -0.03883 392 CYS A CB  
1065 S SG  . CYS A 73  ? 0.75399 0.75840 0.49728 -0.07991 -0.00541 -0.06448 392 CYS A SG  
1070 N N   . CYS A 74  ? 0.60264 0.45070 0.47717 -0.07475 0.09393  0.00710  393 CYS A N   
1071 C CA  . CYS A 74  ? 0.60923 0.42511 0.42476 -0.05763 0.08148  0.01995  393 CYS A CA  
1072 C C   . CYS A 74  ? 0.57810 0.42075 0.42508 -0.03988 0.06745  0.03190  393 CYS A C   
1073 O O   . CYS A 74  ? 0.46536 0.31140 0.33085 -0.04443 0.07226  0.03414  393 CYS A O   
1074 C CB  . CYS A 74  ? 0.65393 0.41707 0.41379 -0.07079 0.09616  0.02026  393 CYS A CB  
1075 S SG  . CYS A 74  ? 0.64450 0.35834 0.32917 -0.04975 0.08055  0.03543  393 CYS A SG  
1080 N N   . VAL A 75  ? 0.44621 0.30864 0.29872 -0.01953 0.05047  0.03755  394 VAL A N   
1081 C CA  . VAL A 75  ? 0.40212 0.29498 0.28633 -0.00318 0.04044  0.04809  394 VAL A CA  
1082 C C   . VAL A 75  ? 0.51522 0.39599 0.36194 0.02003  0.02373  0.05332  394 VAL A C   
1083 O O   . VAL A 75  ? 0.45568 0.31182 0.26129 0.02620  0.01547  0.04885  394 VAL A O   
1084 C CB  . VAL A 75  ? 0.43664 0.37986 0.39067 -0.00286 0.03999  0.04839  394 VAL A CB  
1085 C CG1 . VAL A 75  ? 0.47407 0.43311 0.47483 -0.02105 0.05290  0.04530  394 VAL A CG1 
1086 C CG2 . VAL A 75  ? 0.46781 0.41982 0.42661 0.00015  0.03357  0.03849  394 VAL A CG2 
1096 N N   . PRO A 76  ? 0.45981 0.35815 0.31893 0.03508  0.01721  0.06165  395 PRO A N   
1097 C CA  . PRO A 76  ? 0.52543 0.42549 0.36725 0.05863  0.00123  0.06313  395 PRO A CA  
1098 C C   . PRO A 76  ? 0.52443 0.45732 0.40040 0.06641  -0.00672 0.05749  395 PRO A C   
1099 O O   . PRO A 76  ? 0.46331 0.43554 0.39650 0.05935  0.00072  0.05853  395 PRO A O   
1100 C CB  . PRO A 76  ? 0.46787 0.39061 0.32856 0.06875  0.00169  0.07094  395 PRO A CB  
1101 C CG  . PRO A 76  ? 0.49586 0.41298 0.36362 0.05222  0.01386  0.07318  395 PRO A CG  
1102 C CD  . PRO A 76  ? 0.38988 0.30699 0.27762 0.03141  0.02408  0.06795  395 PRO A CD  
1110 N N   . THR A 77  ? 0.45232 0.36672 0.29380 0.08149  -0.02298 0.05079  396 THR A N   
1111 C CA  . THR A 77  ? 0.51346 0.45885 0.38705 0.09216  -0.03483 0.04072  396 THR A CA  
1112 C C   . THR A 77  ? 0.57143 0.53409 0.45320 0.11745  -0.05005 0.03856  396 THR A C   
1113 O O   . THR A 77  ? 0.57419 0.56980 0.49410 0.12783  -0.05983 0.02794  396 THR A O   
1114 C CB  . THR A 77  ? 0.49233 0.40679 0.32287 0.09018  -0.04386 0.03039  396 THR A CB  
1115 O OG1 . THR A 77  ? 0.50100 0.36165 0.25663 0.10113  -0.05447 0.03451  396 THR A OG1 
1116 C CG2 . THR A 77  ? 0.55221 0.45938 0.38632 0.06416  -0.02562 0.02838  396 THR A CG2 
1124 N N   . LYS A 78  ? 0.51227 0.45385 0.36216 0.12710  -0.05179 0.04565  397 LYS A N   
1125 C CA  . LYS A 78  ? 0.50137 0.46073 0.36136 0.15079  -0.06362 0.04188  397 LYS A CA  
1126 C C   . LYS A 78  ? 0.52026 0.47032 0.36487 0.15174  -0.05481 0.05115  397 LYS A C   
1127 O O   . LYS A 78  ? 0.51515 0.42170 0.31457 0.14347  -0.05188 0.05611  397 LYS A O   
1128 C CB  . LYS A 78  ? 0.62049 0.54698 0.43555 0.17228  -0.08906 0.03218  397 LYS A CB  
1129 C CG  . LYS A 78  ? 0.74105 0.69185 0.57733 0.19865  -0.10336 0.02303  397 LYS A CG  
1130 C CD  . LYS A 78  ? 0.85856 0.76723 0.64326 0.22272  -0.13195 0.01482  397 LYS A CD  
1131 C CE  . LYS A 78  ? 0.85840 0.79426 0.67437 0.24248  -0.14163 0.00078  397 LYS A CE  
1132 N NZ  . LYS A 78  ? 1.31776 1.20603 1.08623 0.25320  -0.15884 -0.00670 397 LYS A NZ  
1146 N N   . LEU A 79  ? 0.49642 0.48809 0.37948 0.16129  -0.04958 0.05180  398 LEU A N   
1147 C CA  . LEU A 79  ? 0.40003 0.39122 0.27186 0.16395  -0.04154 0.05805  398 LEU A CA  
1148 C C   . LEU A 79  ? 0.50007 0.50165 0.37006 0.18941  -0.05265 0.04844  398 LEU A C   
1149 O O   . LEU A 79  ? 0.49458 0.52045 0.39182 0.20271  -0.06177 0.03826  398 LEU A O   
1150 C CB  . LEU A 79  ? 0.39152 0.42379 0.30666 0.15126  -0.02179 0.06891  398 LEU A CB  
1151 C CG  . LEU A 79  ? 0.45054 0.47684 0.37655 0.12740  -0.01110 0.07686  398 LEU A CG  
1152 C CD1 . LEU A 79  ? 0.38196 0.44858 0.35377 0.11931  0.00484  0.08883  398 LEU A CD1 
1153 C CD2 . LEU A 79  ? 0.36728 0.35043 0.24986 0.11737  -0.01062 0.07798  398 LEU A CD2 
1165 N N   . SER A 80  ? 0.45771 0.44127 0.29870 0.19633  -0.05273 0.04854  399 SER A N   
1166 C CA  . SER A 80  ? 0.56858 0.56133 0.40798 0.22052  -0.06201 0.03710  399 SER A CA  
1167 C C   . SER A 80  ? 0.53246 0.55744 0.38518 0.22128  -0.04623 0.03993  399 SER A C   
1168 O O   . SER A 80  ? 0.46920 0.49053 0.31412 0.20559  -0.03453 0.05041  399 SER A O   
1169 C CB  . SER A 80  ? 0.55797 0.49215 0.34432 0.23177  -0.07997 0.03082  399 SER A CB  
1170 O OG  . SER A 80  ? 0.66842 0.57283 0.43855 0.23038  -0.09384 0.02676  399 SER A OG  
1176 N N   . PRO A 81  ? 0.47674 0.53382 0.34800 0.24070  -0.04633 0.02881  400 PRO A N   
1177 C CA  . PRO A 81  ? 0.54944 0.63609 0.42452 0.24358  -0.03113 0.03003  400 PRO A CA  
1178 C C   . PRO A 81  ? 0.56420 0.61734 0.39707 0.25248  -0.03975 0.02163  400 PRO A C   
1179 O O   . PRO A 81  ? 0.54042 0.54749 0.34477 0.26002  -0.05764 0.01364  400 PRO A O   
1180 C CB  . PRO A 81  ? 0.52751 0.66194 0.44214 0.26014  -0.02634 0.01791  400 PRO A CB  
1181 C CG  . PRO A 81  ? 0.52612 0.63676 0.43853 0.27660  -0.05116 0.00188  400 PRO A CG  
1182 C CD  . PRO A 81  ? 0.54420 0.61357 0.43541 0.26135  -0.06101 0.01252  400 PRO A CD  
1190 N N   . ILE A 82  ? 0.53796 0.61355 0.36647 0.25184  -0.02696 0.02357  401 ILE A N   
1191 C CA  . ILE A 82  ? 0.55520 0.61484 0.35459 0.26447  -0.03352 0.00960  401 ILE A CA  
1192 C C   . ILE A 82  ? 0.52513 0.63752 0.33955 0.27720  -0.01913 0.00322  401 ILE A C   
1193 O O   . ILE A 82  ? 0.53993 0.69433 0.38258 0.27159  -0.00168 0.01445  401 ILE A O   
1194 C CB  . ILE A 82  ? 0.61582 0.64501 0.38707 0.24983  -0.03404 0.01471  401 ILE A CB  
1195 C CG1 . ILE A 82  ? 0.57940 0.64492 0.36053 0.23787  -0.01751 0.02935  401 ILE A CG1 
1196 C CG2 . ILE A 82  ? 0.58145 0.56002 0.33865 0.23405  -0.04247 0.02123  401 ILE A CG2 
1197 C CD1 . ILE A 82  ? 0.54070 0.58896 0.29828 0.23162  -0.02080 0.02605  401 ILE A CD1 
1209 N N   . SER A 83  ? 0.51226 0.62054 0.30744 0.29379  -0.02513 -0.01548 402 SER A N   
1210 C CA  . SER A 83  ? 0.51503 0.67073 0.31433 0.30546  -0.00992 -0.02359 402 SER A CA  
1211 C C   . SER A 83  ? 0.54618 0.70250 0.31631 0.29753  -0.00428 -0.01691 402 SER A C   
1212 O O   . SER A 83  ? 0.53289 0.64959 0.27958 0.29290  -0.01810 -0.02176 402 SER A O   
1213 C CB  . SER A 83  ? 0.54379 0.69950 0.34151 0.33005  -0.02015 -0.05206 402 SER A CB  
1214 O OG  . SER A 83  ? 0.55635 0.70970 0.38165 0.34104  -0.03054 -0.06123 402 SER A OG  
1220 N N   . VAL A 84  ? 0.57617 0.77688 0.34817 0.29636  0.01606  -0.00627 403 VAL A N   
1221 C CA  . VAL A 84  ? 0.57853 0.78593 0.31875 0.29508  0.01912  -0.00290 403 VAL A CA  
1222 C C   . VAL A 84  ? 0.60343 0.85549 0.33159 0.31128  0.03533  -0.01269 403 VAL A C   
1223 O O   . VAL A 84  ? 0.61050 0.89776 0.36220 0.31473  0.05421  -0.00948 403 VAL A O   
1224 C CB  . VAL A 84  ? 0.57435 0.78235 0.31738 0.27525  0.02617  0.02598  403 VAL A CB  
1225 C CG1 . VAL A 84  ? 0.58283 0.74662 0.33435 0.25913  0.01108  0.03063  403 VAL A CG1 
1226 C CG2 . VAL A 84  ? 0.56999 0.81435 0.34093 0.26917  0.04925  0.04711  403 VAL A CG2 
1236 N N   . LEU A 85  ? 0.58655 0.83712 0.27937 0.32102  0.02809  -0.02761 404 LEU A N   
1237 C CA  . LEU A 85  ? 0.62756 0.91246 0.31204 0.32683  0.03949  -0.03169 404 LEU A CA  
1238 C C   . LEU A 85  ? 0.77201 1.06256 0.44328 0.31289  0.04543  -0.00549 404 LEU A C   
1239 O O   . LEU A 85  ? 0.64541 0.91175 0.30372 0.30720  0.02925  -0.00560 404 LEU A O   
1240 C CB  . LEU A 85  ? 0.64537 0.92024 0.31338 0.34098  0.02278  -0.06377 404 LEU A CB  
1241 C CG  . LEU A 85  ? 0.68202 0.99063 0.33631 0.34798  0.03266  -0.07224 404 LEU A CG  
1242 C CD1 . LEU A 85  ? 0.69375 1.03936 0.36771 0.35088  0.05632  -0.07073 404 LEU A CD1 
1243 C CD2 . LEU A 85  ? 0.71027 1.00725 0.35374 0.36157  0.01393  -0.10631 404 LEU A CD2 
1255 N N   . TYR A 86  ? 0.88864 1.20861 0.56693 0.30696  0.06857  0.01568  405 TYR A N   
1256 C CA  . TYR A 86  ? 1.00884 1.32879 0.67811 0.29402  0.07469  0.04382  405 TYR A CA  
1257 C C   . TYR A 86  ? 1.15193 1.49691 0.79846 0.29766  0.09051  0.04880  405 TYR A C   
1258 O O   . TYR A 86  ? 1.09027 1.45947 0.73842 0.30526  0.10507  0.03618  405 TYR A O   
1259 C CB  . TYR A 86  ? 0.91546 1.23580 0.61506 0.27875  0.08819  0.07200  405 TYR A CB  
1260 C CG  . TYR A 86  ? 1.20236 1.55390 0.92444 0.27680  0.11599  0.08076  405 TYR A CG  
1261 C CD1 . TYR A 86  ? 0.92324 1.28960 0.67139 0.28478  0.12151  0.06138  405 TYR A CD1 
1262 C CD2 . TYR A 86  ? 1.04019 1.40411 0.76056 0.26661  0.13649  0.10590  405 TYR A CD2 
1263 C CE1 . TYR A 86  ? 0.93530 1.33176 0.71475 0.28046  0.14716  0.06466  405 TYR A CE1 
1264 C CE2 . TYR A 86  ? 1.02468 1.41453 0.77022 0.26120  0.16440  0.11199  405 TYR A CE2 
1265 C CZ  . TYR A 86  ? 1.00060 1.40863 0.77893 0.26718  0.17005  0.09006  405 TYR A CZ  
1266 O OH  . TYR A 86  ? 1.08248 1.51724 0.89499 0.25967  0.19760  0.09133  405 TYR A OH  
1276 N N   . LYS A 87  ? 1.19192 1.52906 0.81685 0.29202  0.08722  0.06604  406 LYS A N   
1277 C CA  . LYS A 87  ? 1.29346 1.64720 0.88770 0.29459  0.10159  0.07543  406 LYS A CA  
1278 C C   . LYS A 87  ? 1.84805 2.21519 1.45709 0.28253  0.13131  0.10378  406 LYS A C   
1279 O O   . LYS A 87  ? 1.14608 1.50037 0.77457 0.26955  0.13374  0.12870  406 LYS A O   
1280 C CB  . LYS A 87  ? 1.06706 1.40418 0.63193 0.29437  0.08499  0.08372  406 LYS A CB  
1281 C CG  . LYS A 87  ? 1.47674 1.80405 1.02506 0.30601  0.05792  0.05369  406 LYS A CG  
1282 C CD  . LYS A 87  ? 1.15840 1.47533 0.67755 0.30741  0.04294  0.06058  406 LYS A CD  
1283 C CE  . LYS A 87  ? 1.64075 1.95052 1.14795 0.31854  0.01636  0.02874  406 LYS A CE  
1284 N NZ  . LYS A 87  ? 1.76737 2.09664 1.25413 0.33374  0.01859  0.00255  406 LYS A NZ  
1298 N N   . ASP A 88  ? 1.24119 1.63362 0.84386 0.28577  0.15466  0.09774  407 ASP A N   
1299 C CA  . ASP A 88  ? 1.46951 1.87477 1.08483 0.27280  0.18695  0.12148  407 ASP A CA  
1300 C C   . ASP A 88  ? 1.86829 2.26217 1.44343 0.26779  0.19371  0.14801  407 ASP A C   
1301 O O   . ASP A 88  ? 1.99802 2.38261 1.53208 0.27767  0.17544  0.14186  407 ASP A O   
1302 C CB  . ASP A 88  ? 1.31975 1.75567 0.94286 0.27700  0.21061  0.10070  407 ASP A CB  
1303 C CG  . ASP A 88  ? 1.64890 2.10089 1.29821 0.26131  0.24761  0.11766  407 ASP A CG  
1304 O OD1 . ASP A 88  ? 1.46326 1.91114 1.08337 0.25293  0.26635  0.14061  407 ASP A OD1 
1305 O OD2 . ASP A 88  ? 1.80715 2.27467 1.50738 0.25719  0.25770  0.10652  407 ASP A OD2 
1310 N N   . ASP A 89  ? 2.01356 2.40695 1.60170 0.25261  0.21954  0.17633  408 ASP A N   
1311 C CA  . ASP A 89  ? 1.59745 1.97814 1.14445 0.24766  0.23039  0.20315  408 ASP A CA  
1312 C C   . ASP A 89  ? 1.74910 2.14386 1.24278 0.25694  0.24269  0.19168  408 ASP A C   
1313 O O   . ASP A 89  ? 2.05376 2.43503 1.49662 0.25971  0.24027  0.20669  408 ASP A O   
1314 C CB  . ASP A 89  ? 1.42888 1.80657 1.00464 0.22826  0.26036  0.23265  408 ASP A CB  
1315 C CG  . ASP A 89  ? 1.88440 2.24447 1.50715 0.21776  0.24910  0.24926  408 ASP A CG  
1316 O OD1 . ASP A 89  ? 1.39028 1.74061 1.02351 0.22440  0.21926  0.23799  408 ASP A OD1 
1317 O OD2 . ASP A 89  ? 1.61452 1.97000 1.26489 0.20183  0.27112  0.27216  408 ASP A OD2 
1322 N N   . MET A 90  ? 1.75212 2.17396 1.25776 0.26214  0.25542  0.16376  409 MET A N   
1323 C CA  . MET A 90  ? 2.20926 2.64792 1.66947 0.27193  0.26620  0.14560  409 MET A CA  
1324 C C   . MET A 90  ? 2.50288 2.93859 1.93598 0.29149  0.23097  0.11863  409 MET A C   
1325 O O   . MET A 90  ? 2.51276 2.96268 1.90971 0.30227  0.23395  0.09825  409 MET A O   
1326 C CB  . MET A 90  ? 1.72014 2.19028 1.21469 0.26835  0.29546  0.12356  409 MET A CB  
1327 C CG  . MET A 90  ? 1.39240 1.88349 0.84618 0.27511  0.31517  0.10383  409 MET A CG  
1328 S SD  . MET A 90  ? 2.62384 3.10719 2.02179 0.26057  0.35251  0.13750  409 MET A SD  
1329 C CE  . MET A 90  ? 1.85178 2.35870 1.31019 0.23885  0.40073  0.13759  409 MET A CE  
1339 N N   . GLY A 91  ? 2.31607 2.73299 1.76854 0.29484  0.19881  0.11717  410 GLY A N   
1340 C CA  . GLY A 91  ? 2.08696 2.49754 1.52127 0.31046  0.16526  0.09156  410 GLY A CA  
1341 C C   . GLY A 91  ? 1.88445 2.31284 1.33797 0.32191  0.15915  0.05265  410 GLY A C   
1342 O O   . GLY A 91  ? 2.16889 2.60154 1.59708 0.33592  0.14304  0.02681  410 GLY A O   
1346 N N   . VAL A 92  ? 1.50735 1.94538 1.00764 0.31642  0.17092  0.04768  411 VAL A N   
1347 C CA  . VAL A 92  ? 1.68014 2.13306 1.20360 0.32739  0.16565  0.01154  411 VAL A CA  
1348 C C   . VAL A 92  ? 1.59430 2.03109 1.16046 0.32621  0.14672  0.00673  411 VAL A C   
1349 O O   . VAL A 92  ? 1.19760 1.62851 0.79151 0.31373  0.15541  0.02958  411 VAL A O   
1350 C CB  . VAL A 92  ? 1.24753 1.73130 0.78526 0.32477  0.19976  0.00232  411 VAL A CB  
1351 C CG1 . VAL A 92  ? 1.69965 2.19756 1.18812 0.32663  0.21947  0.00267  411 VAL A CG1 
1352 C CG2 . VAL A 92  ? 1.16313 1.65133 0.74082 0.30770  0.22450  0.02651  411 VAL A CG2 
1362 N N   . PRO A 93  ? 1.48621 1.73907 1.03162 0.42058  0.14021  -0.01953 412 PRO A N   
1363 C CA  . PRO A 93  ? 1.49188 1.74272 1.08480 0.39779  0.12838  -0.02724 412 PRO A CA  
1364 C C   . PRO A 93  ? 1.31557 1.53813 0.94452 0.38199  0.15626  -0.01161 412 PRO A C   
1365 O O   . PRO A 93  ? 1.04908 1.27118 0.69530 0.37764  0.17656  -0.02155 412 PRO A O   
1366 C CB  . PRO A 93  ? 1.33057 1.61145 0.94630 0.38587  0.10909  -0.07214 412 PRO A CB  
1367 C CG  . PRO A 93  ? 1.92232 2.23439 1.50099 0.40408  0.09981  -0.08885 412 PRO A CG  
1368 C CD  . PRO A 93  ? 1.74963 2.03991 1.28667 0.42501  0.12559  -0.05659 412 PRO A CD  
1376 N N   . THR A 94  ? 1.16568 1.36975 0.81045 0.37415  0.15722  0.01031  413 THR A N   
1377 C CA  . THR A 94  ? 0.98324 1.17127 0.67271 0.35874  0.18033  0.02177  413 THR A CA  
1378 C C   . THR A 94  ? 0.86148 1.05285 0.58827 0.34657  0.15931  0.01526  413 THR A C   
1379 O O   . THR A 94  ? 0.84656 1.03856 0.55495 0.34763  0.13758  0.01768  413 THR A O   
1380 C CB  . THR A 94  ? 1.03912 1.19627 0.71139 0.35894  0.21136  0.05559  413 THR A CB  
1381 O OG1 . THR A 94  ? 1.76415 1.91240 1.39850 0.37121  0.23343  0.06052  413 THR A OG1 
1382 C CG2 . THR A 94  ? 0.96320 1.11438 0.69301 0.33873  0.23624  0.06190  413 THR A CG2 
1390 N N   . LEU A 95  ? 0.70498 0.89984 0.48655 0.33748  0.16485  0.00589  414 LEU A N   
1391 C CA  . LEU A 95  ? 0.68098 0.87064 0.50132 0.32495  0.14318  0.00352  414 LEU A CA  
1392 C C   . LEU A 95  ? 0.62781 0.80408 0.46807 0.31039  0.15067  0.03014  414 LEU A C   
1393 O O   . LEU A 95  ? 0.72008 0.89785 0.58266 0.30646  0.17906  0.04040  414 LEU A O   
1394 C CB  . LEU A 95  ? 0.59845 0.78909 0.47170 0.31979  0.13638  -0.01394 414 LEU A CB  
1395 C CG  . LEU A 95  ? 0.62026 0.79318 0.52713 0.30429  0.10847  -0.01277 414 LEU A CG  
1396 C CD1 . LEU A 95  ? 0.57916 0.73717 0.45723 0.29906  0.08677  -0.02724 414 LEU A CD1 
1397 C CD2 . LEU A 95  ? 0.60222 0.77528 0.55806 0.30875  0.10556  -0.02245 414 LEU A CD2 
1409 N N   . LYS A 96  ? 0.64889 0.81322 0.48343 0.29993  0.12802  0.03717  415 LYS A N   
1410 C CA  . LYS A 96  ? 0.56345 0.71450 0.42481 0.28174  0.12990  0.05579  415 LYS A CA  
1411 C C   . LYS A 96  ? 0.56813 0.71729 0.47277 0.26608  0.10025  0.04558  415 LYS A C   
1412 O O   . LYS A 96  ? 0.62300 0.76103 0.51314 0.26087  0.07635  0.04069  415 LYS A O   
1413 C CB  . LYS A 96  ? 0.60528 0.74055 0.42101 0.28588  0.13046  0.07331  415 LYS A CB  
1414 C CG  . LYS A 96  ? 0.70186 0.81919 0.54188 0.26507  0.13131  0.08894  415 LYS A CG  
1415 C CD  . LYS A 96  ? 0.74185 0.85766 0.62240 0.25059  0.16203  0.09570  415 LYS A CD  
1416 C CE  . LYS A 96  ? 0.72044 0.82213 0.62650 0.22724  0.16196  0.10434  415 LYS A CE  
1417 N NZ  . LYS A 96  ? 0.83701 0.95252 0.80144 0.20658  0.18545  0.09784  415 LYS A NZ  
1431 N N   . TYR A 97  ? 0.49308 0.65456 0.44904 0.26102  0.10323  0.04093  416 TYR A N   
1432 C CA  . TYR A 97  ? 0.51104 0.66942 0.49623 0.25942  0.07591  0.03011  416 TYR A CA  
1433 C C   . TYR A 97  ? 0.45345 0.59569 0.44021 0.24330  0.05359  0.03909  416 TYR A C   
1434 O O   . TYR A 97  ? 0.51138 0.63073 0.48052 0.24211  0.03261  0.03439  416 TYR A O   
1435 C CB  . TYR A 97  ? 0.47603 0.66146 0.51535 0.26592  0.08220  0.02100  416 TYR A CB  
1436 C CG  . TYR A 97  ? 0.47423 0.65195 0.53297 0.27613  0.05460  0.01193  416 TYR A CG  
1437 C CD1 . TYR A 97  ? 0.49337 0.64060 0.52260 0.28765  0.04548  0.00277  416 TYR A CD1 
1438 C CD2 . TYR A 97  ? 0.46276 0.66182 0.56600 0.27622  0.03952  0.01088  416 TYR A CD2 
1439 C CE1 . TYR A 97  ? 0.50846 0.63306 0.54493 0.30085  0.02617  -0.00158 416 TYR A CE1 
1440 C CE2 . TYR A 97  ? 0.50283 0.68941 0.61222 0.29437  0.01401  0.00637  416 TYR A CE2 
1441 C CZ  . TYR A 97  ? 0.50191 0.64435 0.57422 0.30774  0.00946  0.00296  416 TYR A CZ  
1442 O OH  . TYR A 97  ? 0.52985 0.64462 0.59770 0.32887  -0.01019 0.00256  416 TYR A OH  
1452 N N   . HIS A 98  ? 0.48004 0.63048 0.48533 0.22898  0.06273  0.05009  417 HIS A N   
1453 C CA  . HIS A 98  ? 0.45274 0.58823 0.45431 0.21261  0.04568  0.05800  417 HIS A CA  
1454 C C   . HIS A 98  ? 0.54159 0.66183 0.51011 0.20538  0.06159  0.07232  417 HIS A C   
1455 O O   . HIS A 98  ? 0.58018 0.70179 0.56374 0.19403  0.08269  0.08040  417 HIS A O   
1456 C CB  . HIS A 98  ? 0.43996 0.59839 0.49297 0.20132  0.03915  0.05382  417 HIS A CB  
1457 C CG  . HIS A 98  ? 0.49283 0.66808 0.57494 0.21631  0.01784  0.04133  417 HIS A CG  
1458 N ND1 . HIS A 98  ? 0.45048 0.59546 0.50427 0.22798  -0.00613 0.04119  417 HIS A ND1 
1459 C CD2 . HIS A 98  ? 0.46620 0.68394 0.60148 0.22362  0.01987  0.02797  417 HIS A CD2 
1460 C CE1 . HIS A 98  ? 0.52434 0.68723 0.60749 0.24684  -0.01881 0.03217  417 HIS A CE1 
1461 N NE2 . HIS A 98  ? 0.45308 0.66678 0.58915 0.24604  -0.00645 0.02234  417 HIS A NE2 
1469 N N   . TYR A 99  ? 0.48566 0.59143 0.41038 0.21257  0.05247  0.07272  418 TYR A N   
1470 C CA  . TYR A 99  ? 0.52582 0.61906 0.41564 0.21329  0.06094  0.08533  418 TYR A CA  
1471 C C   . TYR A 99  ? 0.45979 0.53903 0.35788 0.19413  0.04361  0.08805  418 TYR A C   
1472 O O   . TYR A 99  ? 0.46581 0.53875 0.35227 0.19019  0.02199  0.07902  418 TYR A O   
1473 C CB  . TYR A 99  ? 0.46813 0.56781 0.31370 0.23241  0.05547  0.07739  418 TYR A CB  
1474 C CG  . TYR A 99  ? 0.61879 0.71370 0.42140 0.24828  0.06833  0.09159  418 TYR A CG  
1475 C CD1 . TYR A 99  ? 0.78172 0.86284 0.56818 0.25893  0.10090  0.11171  418 TYR A CD1 
1476 C CD2 . TYR A 99  ? 0.62598 0.72886 0.40202 0.25527  0.05067  0.08380  418 TYR A CD2 
1477 C CE1 . TYR A 99  ? 1.73118 1.79743 1.46692 0.28137  0.11503  0.12894  418 TYR A CE1 
1478 C CE2 . TYR A 99  ? 0.67452 0.77608 0.40810 0.27870  0.05982  0.09701  418 TYR A CE2 
1479 C CZ  . TYR A 99  ? 0.79665 0.87509 0.51116 0.29239  0.09098  0.12030  418 TYR A CZ  
1480 O OH  . TYR A 99  ? 0.87622 0.94208 0.57137 0.31077  0.09831  0.12649  418 TYR A OH  
1490 N N   . GLU A 100 ? 0.57196 0.64510 0.49035 0.17990  0.05724  0.09772  419 GLU A N   
1491 C CA  . GLU A 100 ? 0.55504 0.62045 0.49052 0.15938  0.04128  0.09627  419 GLU A CA  
1492 C C   . GLU A 100 ? 0.49339 0.53952 0.39603 0.15698  0.03420  0.10145  419 GLU A C   
1493 O O   . GLU A 100 ? 0.47323 0.51148 0.34449 0.17106  0.04874  0.11071  419 GLU A O   
1494 C CB  . GLU A 100 ? 0.65495 0.72564 0.62759 0.14180  0.06146  0.09762  419 GLU A CB  
1495 C CG  . GLU A 100 ? 0.67997 0.78258 0.69883 0.14116  0.06742  0.08567  419 GLU A CG  
1496 C CD  . GLU A 100 ? 0.82205 0.94769 0.86901 0.14207  0.03362  0.07145  419 GLU A CD  
1497 O OE1 . GLU A 100 ? 0.64929 0.76026 0.67929 0.13773  0.00800  0.07200  419 GLU A OE1 
1498 O OE2 . GLU A 100 ? 0.68915 0.84602 0.77209 0.14997  0.03439  0.06006  419 GLU A OE2 
1505 N N   . GLY A 101 ? 0.40862 0.44792 0.31602 0.14228  0.01175  0.09488  420 GLY A N   
1506 C CA  . GLY A 101 ? 0.48843 0.51211 0.37619 0.13388  0.00734  0.09702  420 GLY A CA  
1507 C C   . GLY A 101 ? 0.42822 0.45421 0.28719 0.14322  -0.00352 0.08800  420 GLY A C   
1508 O O   . GLY A 101 ? 0.50032 0.52325 0.34263 0.14391  -0.00266 0.08818  420 GLY A O   
1512 N N   . MET A 102 ? 0.44711 0.48092 0.30407 0.14968  -0.01216 0.07621  421 MET A N   
1513 C CA  . MET A 102 ? 0.44662 0.49196 0.28314 0.15668  -0.01761 0.05949  421 MET A CA  
1514 C C   . MET A 102 ? 0.47807 0.50732 0.31125 0.13701  -0.02954 0.04348  421 MET A C   
1515 O O   . MET A 102 ? 0.45431 0.49776 0.27739 0.13523  -0.03119 0.02489  421 MET A O   
1516 C CB  . MET A 102 ? 0.39904 0.46030 0.23328 0.17312  -0.01362 0.05076  421 MET A CB  
1517 C CG  . MET A 102 ? 0.41340 0.49089 0.23539 0.19607  0.00275  0.06350  421 MET A CG  
1518 S SD  . MET A 102 ? 0.47566 0.57403 0.26183 0.21799  0.00395  0.06214  421 MET A SD  
1519 C CE  . MET A 102 ? 0.43589 0.57166 0.21228 0.22696  -0.00886 0.02715  421 MET A CE  
1529 N N   . SER A 103 ? 0.47914 0.48027 0.31916 0.12349  -0.03624 0.04909  422 SER A N   
1530 C CA  . SER A 103 ? 0.50244 0.47336 0.32891 0.10692  -0.04130 0.03767  422 SER A CA  
1531 C C   . SER A 103 ? 0.51272 0.45855 0.33505 0.09314  -0.04852 0.04986  422 SER A C   
1532 O O   . SER A 103 ? 0.48074 0.43138 0.31726 0.09805  -0.05408 0.06308  422 SER A O   
1533 C CB  . SER A 103 ? 0.54335 0.49383 0.36639 0.11337  -0.04084 0.03130  422 SER A CB  
1534 O OG  . SER A 103 ? 0.57077 0.48173 0.37306 0.09749  -0.03650 0.01819  422 SER A OG  
1540 N N   . VAL A 104 ? 0.47529 0.39863 0.27949 0.07490  -0.04715 0.04148  423 VAL A N   
1541 C CA  . VAL A 104 ? 0.49999 0.39941 0.29261 0.06199  -0.05317 0.05104  423 VAL A CA  
1542 C C   . VAL A 104 ? 0.48781 0.35079 0.26166 0.06782  -0.06180 0.05977  423 VAL A C   
1543 O O   . VAL A 104 ? 0.60662 0.43535 0.35928 0.06839  -0.05506 0.05376  423 VAL A O   
1544 C CB  . VAL A 104 ? 0.55924 0.44403 0.33523 0.04072  -0.04525 0.03850  423 VAL A CB  
1545 C CG1 . VAL A 104 ? 0.49464 0.35096 0.25131 0.02805  -0.05059 0.04818  423 VAL A CG1 
1546 C CG2 . VAL A 104 ? 0.45790 0.38366 0.25138 0.04266  -0.03974 0.02890  423 VAL A CG2 
1556 N N   . ALA A 105 ? 0.52159 0.39275 0.30269 0.07360  -0.07541 0.07156  424 ALA A N   
1557 C CA  . ALA A 105 ? 0.60381 0.44680 0.36114 0.08557  -0.08906 0.08004  424 ALA A CA  
1558 C C   . ALA A 105 ? 0.54402 0.35439 0.26388 0.07178  -0.09247 0.08314  424 ALA A C   
1559 O O   . ALA A 105 ? 0.67551 0.43491 0.34949 0.07809  -0.09274 0.08947  424 ALA A O   
1560 C CB  . ALA A 105 ? 0.61297 0.49797 0.40442 0.10279  -0.10472 0.08383  424 ALA A CB  
1566 N N   . GLU A 106 ? 0.59891 0.43300 0.33358 0.05454  -0.09203 0.07939  425 GLU A N   
1567 C CA  . GLU A 106 ? 0.65819 0.46668 0.35926 0.03983  -0.09392 0.07973  425 GLU A CA  
1568 C C   . GLU A 106 ? 0.57246 0.39462 0.28804 0.01682  -0.08016 0.07041  425 GLU A C   
1569 O O   . GLU A 106 ? 0.51455 0.37311 0.26840 0.01720  -0.07535 0.06760  425 GLU A O   
1570 C CB  . GLU A 106 ? 0.62425 0.45440 0.32740 0.04975  -0.11656 0.08263  425 GLU A CB  
1571 C CG  . GLU A 106 ? 0.97047 0.77680 0.63905 0.07534  -0.13147 0.09150  425 GLU A CG  
1572 C CD  . GLU A 106 ? 1.17449 1.03224 0.86949 0.09450  -0.15773 0.08748  425 GLU A CD  
1573 O OE1 . GLU A 106 ? 0.95589 0.84989 0.67114 0.08085  -0.16671 0.07641  425 GLU A OE1 
1574 O OE2 . GLU A 106 ? 1.75139 1.61860 1.45478 0.12033  -0.16571 0.09068  425 GLU A OE2 
1581 N N   . CYS A 107 ? 0.68254 0.47127 0.36299 -0.00040 -0.07191 0.06658  426 CYS A N   
1582 C CA  . CYS A 107 ? 0.57651 0.37536 0.26675 -0.02035 -0.05890 0.05583  426 CYS A CA  
1583 C C   . CYS A 107 ? 0.59900 0.39038 0.27071 -0.03106 -0.06562 0.05603  426 CYS A C   
1584 O O   . CYS A 107 ? 0.58636 0.35244 0.21991 -0.02549 -0.07733 0.06288  426 CYS A O   
1585 C CB  . CYS A 107 ? 0.65853 0.43159 0.32983 -0.03573 -0.03880 0.04343  426 CYS A CB  
1586 S SG  . CYS A 107 ? 0.60852 0.39655 0.30199 -0.02742 -0.02984 0.03295  426 CYS A SG  
1591 N N   . GLY A 108 ? 0.50817 0.31952 0.20212 -0.04378 -0.05740 0.04760  427 GLY A N   
1592 C CA  . GLY A 108 ? 0.59714 0.39882 0.27186 -0.05872 -0.05872 0.04211  427 GLY A CA  
1593 C C   . GLY A 108 ? 0.63204 0.44510 0.32818 -0.07244 -0.04139 0.03086  427 GLY A C   
1594 O O   . GLY A 108 ? 0.53639 0.36934 0.26269 -0.06496 -0.03156 0.02945  427 GLY A O   
1598 N N   . CYS A 109 ? 0.61293 0.41294 0.28891 -0.08871 -0.03828 0.02264  428 CYS A N   
1599 C CA  . CYS A 109 ? 0.60450 0.41074 0.29764 -0.10040 -0.02110 0.01076  428 CYS A CA  
1600 C C   . CYS A 109 ? 0.60238 0.42786 0.32866 -0.10006 -0.02134 0.00868  428 CYS A C   
1601 O O   . CYS A 109 ? 0.58716 0.41857 0.30962 -0.10518 -0.03485 0.00537  428 CYS A O   
1602 C CB  . CYS A 109 ? 0.65403 0.43243 0.30656 -0.12016 -0.01305 0.00051  428 CYS A CB  
1603 S SG  . CYS A 109 ? 0.68178 0.42954 0.29965 -0.12815 0.00184  -0.00220 428 CYS A SG  
1608 N N   . ARG A 110 ? 0.49192 0.32711 0.24928 -0.09219 -0.00484 0.00900  429 ARG A N   
1609 C CA  . ARG A 110 ? 0.55516 0.39596 0.34285 -0.09153 0.00548  0.00888  429 ARG A CA  
1610 C C   . ARG A 110 ? 0.49956 0.32750 0.29545 -0.09045 0.02979  0.00340  429 ARG A C   
1611 O O   . ARG A 110 ? 0.50388 0.31999 0.31379 -0.10003 0.04507  -0.00322 429 ARG A O   
1612 C CB  . ARG A 110 ? 0.51404 0.36973 0.32517 -0.07218 0.00480  0.02307  429 ARG A CB  
1613 C CG  . ARG A 110 ? 0.55694 0.42786 0.36721 -0.07066 -0.01760 0.02639  429 ARG A CG  
1614 C CD  . ARG A 110 ? 0.55073 0.43353 0.37141 -0.08716 -0.02618 0.01283  429 ARG A CD  
1615 N NE  . ARG A 110 ? 0.55367 0.45941 0.37639 -0.07847 -0.05020 0.01429  429 ARG A NE  
1616 C CZ  . ARG A 110 ? 0.64075 0.54189 0.42681 -0.07346 -0.07313 0.01549  429 ARG A CZ  
1617 N NH1 . ARG A 110 ? 0.51978 0.39011 0.26190 -0.07943 -0.07210 0.01679  429 ARG A NH1 
1618 N NH2 . ARG A 110 ? 0.54649 0.47199 0.33770 -0.06001 -0.09509 0.01550  429 ARG A NH2 
1619 O OXT . ARG A 110 ? 0.47920 0.30973 0.26918 -0.07952 0.03536  0.00269  429 ARG A OXT 
1661 O O   . HOH L .   ? 0.50385 0.40329 0.15883 -0.15434 0.03726  -0.01711 606 HOH A O   
1667 O O   . HOH L .   ? 0.53242 0.44416 0.19706 -0.06142 -0.06727 0.11213  612 HOH A O   
1680 O O   . HOH L .   ? 0.52551 0.28019 0.19207 0.00981  -0.01181 -0.02954 625 HOH A O   
1738 O O   . HOH L .   ? 0.61955 0.75470 0.63417 -0.09897 0.11168  -0.15247 683 HOH A O   
1740 O O   . HOH L .   ? 0.59713 0.38956 0.17011 -0.11873 0.04899  -0.00132 685 HOH A O   
# 
