data_9DPU
# 
_entry.id   9DPU 
# 
_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   9DPU         pdb_00009dpu 10.2210/pdb9dpu/pdb 
WWPDB D_1000287387 ?            ?                   
# 
_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                        9DPU 
_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' 12148.996 1   ? 'A321S, G389S' ? ? 
2 non-polymer syn 'CHLORIDE ION'                    35.453    5   ? ?              ? ? 
3 non-polymer syn 'SODIUM ION'                      22.990    1   ? ?              ? ? 
4 non-polymer syn GLYCEROL                          92.094    2   ? ?              ? ? 
5 water       nat water                             18.015    106 ? ?              ? ? 
# 
_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       
;SSGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVSKACCVPTKLS
PISVLYKDDMGVPTLKYHYEGMSVAECGCR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SSGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVSKACCVPTKLS
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 'CHLORIDE ION' CL  
3 'SODIUM ION'   NA  
4 GLYCEROL       GOL 
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  LYS 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  LYS 38  357 357 LYS LYS 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 CL  1   501 1   CL  CL  A . 
C 2 CL  1   502 2   CL  CL  A . 
D 2 CL  1   503 3   CL  CL  A . 
E 2 CL  1   504 4   CL  CL  A . 
F 2 CL  1   505 5   CL  CL  A . 
G 3 NA  1   506 1   NA  NA  A . 
H 4 GOL 1   507 1   GOL GOL A . 
I 4 GOL 1   508 2   GOL GOL A . 
J 5 HOH 1   601 94  HOH HOH A . 
J 5 HOH 2   602 38  HOH HOH A . 
J 5 HOH 3   603 2   HOH HOH A . 
J 5 HOH 4   604 109 HOH HOH A . 
J 5 HOH 5   605 106 HOH HOH A . 
J 5 HOH 6   606 118 HOH HOH A . 
J 5 HOH 7   607 112 HOH HOH A . 
J 5 HOH 8   608 86  HOH HOH A . 
J 5 HOH 9   609 10  HOH HOH A . 
J 5 HOH 10  610 1   HOH HOH A . 
J 5 HOH 11  611 28  HOH HOH A . 
J 5 HOH 12  612 14  HOH HOH A . 
J 5 HOH 13  613 121 HOH HOH A . 
J 5 HOH 14  614 12  HOH HOH A . 
J 5 HOH 15  615 74  HOH HOH A . 
J 5 HOH 16  616 43  HOH HOH A . 
J 5 HOH 17  617 26  HOH HOH A . 
J 5 HOH 18  618 73  HOH HOH A . 
J 5 HOH 19  619 71  HOH HOH A . 
J 5 HOH 20  620 61  HOH HOH A . 
J 5 HOH 21  621 5   HOH HOH A . 
J 5 HOH 22  622 57  HOH HOH A . 
J 5 HOH 23  623 60  HOH HOH A . 
J 5 HOH 24  624 50  HOH HOH A . 
J 5 HOH 25  625 88  HOH HOH A . 
J 5 HOH 26  626 22  HOH HOH A . 
J 5 HOH 27  627 92  HOH HOH A . 
J 5 HOH 28  628 7   HOH HOH A . 
J 5 HOH 29  629 41  HOH HOH A . 
J 5 HOH 30  630 36  HOH HOH A . 
J 5 HOH 31  631 33  HOH HOH A . 
J 5 HOH 32  632 46  HOH HOH A . 
J 5 HOH 33  633 100 HOH HOH A . 
J 5 HOH 34  634 18  HOH HOH A . 
J 5 HOH 35  635 117 HOH HOH A . 
J 5 HOH 36  636 45  HOH HOH A . 
J 5 HOH 37  637 40  HOH HOH A . 
J 5 HOH 38  638 17  HOH HOH A . 
J 5 HOH 39  639 48  HOH HOH A . 
J 5 HOH 40  640 15  HOH HOH A . 
J 5 HOH 41  641 16  HOH HOH A . 
J 5 HOH 42  642 8   HOH HOH A . 
J 5 HOH 43  643 25  HOH HOH A . 
J 5 HOH 44  644 20  HOH HOH A . 
J 5 HOH 45  645 75  HOH HOH A . 
J 5 HOH 46  646 69  HOH HOH A . 
J 5 HOH 47  647 21  HOH HOH A . 
J 5 HOH 48  648 85  HOH HOH A . 
J 5 HOH 49  649 47  HOH HOH A . 
J 5 HOH 50  650 31  HOH HOH A . 
J 5 HOH 51  651 90  HOH HOH A . 
J 5 HOH 52  652 23  HOH HOH A . 
J 5 HOH 53  653 68  HOH HOH A . 
J 5 HOH 54  654 107 HOH HOH A . 
J 5 HOH 55  655 67  HOH HOH A . 
J 5 HOH 56  656 37  HOH HOH A . 
J 5 HOH 57  657 59  HOH HOH A . 
J 5 HOH 58  658 99  HOH HOH A . 
J 5 HOH 59  659 11  HOH HOH A . 
J 5 HOH 60  660 54  HOH HOH A . 
J 5 HOH 61  661 116 HOH HOH A . 
J 5 HOH 62  662 53  HOH HOH A . 
J 5 HOH 63  663 113 HOH HOH A . 
J 5 HOH 64  664 49  HOH HOH A . 
J 5 HOH 65  665 83  HOH HOH A . 
J 5 HOH 66  666 115 HOH HOH A . 
J 5 HOH 67  667 93  HOH HOH A . 
J 5 HOH 68  668 72  HOH HOH A . 
J 5 HOH 69  669 97  HOH HOH A . 
J 5 HOH 70  670 105 HOH HOH A . 
J 5 HOH 71  671 58  HOH HOH A . 
J 5 HOH 72  672 108 HOH HOH A . 
J 5 HOH 73  673 95  HOH HOH A . 
J 5 HOH 74  674 84  HOH HOH A . 
J 5 HOH 75  675 120 HOH HOH A . 
J 5 HOH 76  676 65  HOH HOH A . 
J 5 HOH 77  677 64  HOH HOH A . 
J 5 HOH 78  678 9   HOH HOH A . 
J 5 HOH 79  679 119 HOH HOH A . 
J 5 HOH 80  680 76  HOH HOH A . 
J 5 HOH 81  681 42  HOH HOH A . 
J 5 HOH 82  682 80  HOH HOH A . 
J 5 HOH 83  683 32  HOH HOH A . 
J 5 HOH 84  684 103 HOH HOH A . 
J 5 HOH 85  685 51  HOH HOH A . 
J 5 HOH 86  686 91  HOH HOH A . 
J 5 HOH 87  687 102 HOH HOH A . 
J 5 HOH 88  688 114 HOH HOH A . 
J 5 HOH 89  689 3   HOH HOH A . 
J 5 HOH 90  690 87  HOH HOH A . 
J 5 HOH 91  691 70  HOH HOH A . 
J 5 HOH 92  692 81  HOH HOH A . 
J 5 HOH 93  693 98  HOH HOH A . 
J 5 HOH 94  694 77  HOH HOH A . 
J 5 HOH 95  695 111 HOH HOH A . 
J 5 HOH 96  696 4   HOH HOH A . 
J 5 HOH 97  697 62  HOH HOH A . 
J 5 HOH 98  698 89  HOH HOH A . 
J 5 HOH 99  699 82  HOH HOH A . 
J 5 HOH 100 700 78  HOH HOH A . 
J 5 HOH 101 701 66  HOH HOH A . 
J 5 HOH 102 702 104 HOH HOH A . 
J 5 HOH 103 703 101 HOH HOH A . 
J 5 HOH 104 704 96  HOH HOH A . 
J 5 HOH 105 705 55  HOH HOH A . 
J 5 HOH 106 706 56  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                     9DPU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.589 
_cell.length_a_esd                 ? 
_cell.length_b                     71.589 
_cell.length_b_esd                 ? 
_cell.length_c                     146.719 
_cell.length_c_esd                 ? 
_cell.volume                       751932.663 
_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                         9DPU 
_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                   9DPU 
_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             3.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          69.14 
_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              4 
_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, 0.1M Acetic Acid pH 4, 27% Glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2022-10-18 
_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                          40.28 
_reflns.entry_id                                       9DPU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               41.66 
_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                                     11543 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.89 
_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                                0.162 
_reflns.pdbx_Rpim_I_all                                0.043 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.156 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             929 
_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                               26.9 
_reflns_shell.pdbx_chi_squared                              0.85 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.498 
_reflns_shell.pdbx_Rpim_I_all                               0.399 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.970 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.444 
_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                               66.01 
_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                                 9DPU 
_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                            2.10 
_refine.ls_d_res_low                             41.66 
_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                     11501 
_refine.ls_number_reflns_R_free                  584 
_refine.ls_number_reflns_R_work                  10917 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.73 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1933 
_refine.ls_R_factor_R_free                       0.2236 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1916 
_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                          1.37 
_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                 27.6425 
_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                            0.2262 
_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                       2.10 
_refine_hist.d_res_low                        41.66 
_refine_hist.number_atoms_solvent             106 
_refine_hist.number_atoms_total               948 
_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        824 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_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' ? 0.0079  ? 861  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0292  ? 1167 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0616  ? 128  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0074  ? 145  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.7777 ? 316  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.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' 2.10 2.31  . . 144 2667 99.54 . . . . 0.2141 . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 2.31 2.65  . . 145 2665 99.65 . . . . 0.2124 . . . . . . . . . . . 0.2566 
'X-RAY DIFFRACTION' 2.65 3.33  . . 135 2734 99.90 . . . . 0.1987 . . . . . . . . . . . 0.2301 
'X-RAY DIFFRACTION' 3.34 41.66 . . 160 2851 99.83 . . . . 0.1812 . . . . . . . . . . . 0.2078 
# 
_struct.entry_id                     9DPU 
_struct.title                        'BMP-9 G389S Dimer in Acidic 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        9DPU 
_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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J 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              9DPU 
_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 9DPU SER A 2  ? UNP Q9UK05 ALA 321 'engineered mutation' 321 1 
1 9DPU SER A 70 ? UNP Q9UK05 GLY 389 'engineered mutation' 389 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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 
1 2 A,B,C,D,E,F,G,H,I,J 
# 
_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 dimers observed on 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' 5_554 -x+1/2,y,-z-1/4 -1.0000000000 0.0000000000 0.0000000000 35.7945000000 0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -36.6797500000 
# 
_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 ? ? ? ? ? ? ? 2.025 ? ? 
disulf2 disulf ? ? A CYS 37 SG  ? ? ? 1_555 A CYS 107 SG ? ? A CYS 356 A CYS 426 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf3 disulf ? ? A CYS 41 SG  ? ? ? 1_555 A CYS 109 SG ? ? A CYS 360 A CYS 428 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf4 disulf ? ? A CYS 73 SG  A ? ? 1_555 A CYS 73  SG A ? A CYS 392 A CYS 392 5_554 ? ? ? ? ? ? ? 2.047 ? ? 
metalc1 metalc ? ? A THR 67 OG1 ? ? ? 1_555 G NA  .   NA ? ? A THR 386 A NA  506 1_555 ? ? ? ? ? ? ? 2.512 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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 A CYS A 73  A CYS A 392 ? 1_555 CYS A 392 ? 5_554 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 0.02 
2 PHE 43 A . ? PHE 362 A PRO 44 A ? PRO 363 A 1 0.74 
# 
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 ? LYS A 38  ? GLU A 355 LYS 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 ILE A 82 ? N ILE A 401 O TYR A 99 ? O TYR A 418 
# 
_pdbx_entry_details.entry_id                   9DPU 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    TYR 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     354 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             66.34 
_pdbx_validate_torsion.psi             160.71 
# 
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  502 ? C CL  . 
2 1 A HOH 701 ? J 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 4.91826626721 22.4465189059 -6.12269745122 0.554739488621 ? 0.229191218692  ? 0.0277247094899  ? 
0.5416777168   ? 0.0364662017572  ? 0.318638350997  ? 1.65654363991 ? 0.335276109029   ? -2.51374536344 ? 0.899938105168 ? 
-0.906529068791 ? 4.02274487419 ? -0.567458172572 ? 0.0518748644425 ? -0.170205139871 ? 0.527152620365   ? 0.466679045874 ? 
0.363734470169  ? 0.34173908939   ? -0.734428107192 ? -0.943681482185 ? 
2 'X-RAY DIFFRACTION' ? refined 17.3704467138 21.1250855553 -30.7114620532 0.34518384288  ? -0.107418421488 ? -0.0423947072173 ? 
0.462090162359 ? -0.0951616707755 ? 0.0746023342444 ? 1.1432613853  ? 0.506376954646   ? 0.662937368027 ? 2.51381103536  ? 
1.80798629498   ? 4.16486227348 ? -0.132023089315 ? -0.178194939571 ? 0.253631927378  ? -0.0159813145806 ? -0.29526953522 ? 
0.340065634365  ? -0.449144457212 ? -0.649296091087 ? -0.220830574479 ? 
3 'X-RAY DIFFRACTION' ? refined 11.7269003242 28.4273261225 -9.26928539004 0.50061291901  ? 0.150144423293  ? -0.0579516643788 ? 
0.558273804608 ? 0.00775571085308 ? 0.293899776105  ? 1.66847374288 ? -0.0727710470856 ? -1.396009029   ? 0.679607506521 ? 
0.411674030764  ? 4.28079652922 ? -0.254605125357 ? -0.143517871624 ? 0.126175077384  ? 0.12546744274    ? 0.397167810372 ? 
-0.121138885145 ? -0.519409466624 ? 0.109799754164  ? 0.0413604004633 ? 
# 
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 33  A 357 ? ? 
;chain 'A' and (resid  325  through  357 )
;
2 'X-RAY DIFFRACTION' 2 A 34 A 358 ? A 59  A 383 ? ? 
;chain 'A' and (resid  358  through  383 )
;
3 'X-RAY DIFFRACTION' 3 A 60 A 384 ? A 105 A 429 ? ? 
;chain 'A' and (resid  384  through  429 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       706 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.91 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 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          ? 
# 
_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                    9DPU 
_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]   0.013969 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013969 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006816 
_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 ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . SER A 1 6   ? 5.47100  14.57900 -26.10200 1.000 121.56104 ? 325 SER A N    1 
ATOM   2    C  CA   . SER A 1 6   ? 6.04500  15.08700 -27.34400 1.000 71.72804  ? 325 SER A CA   1 
ATOM   3    C  C    . SER A 1 6   ? 7.12600  16.13100 -27.08000 1.000 121.55014 ? 325 SER A C    1 
ATOM   4    O  O    . SER A 1 6   ? 8.23400  15.79700 -26.66100 1.000 69.70477  ? 325 SER A O    1 
ATOM   5    C  CB   . SER A 1 6   ? 4.95700  15.69000 -28.23500 1.000 94.71299  ? 325 SER A CB   1 
ATOM   6    O  OG   . SER A 1 6   ? 3.97400  14.73700 -28.58900 1.000 112.43651 ? 325 SER A OG   1 
ATOM   7    H  HA   . SER A 1 6   ? 6.45300  14.33400 -27.79900 1.000 86.17269  ? 325 SER A HA   1 
ATOM   8    H  HB2  . SER A 1 6   ? 4.53600  16.43200 -27.77300 1.000 113.75461 ? 325 SER A HB2  1 
ATOM   9    H  HB3  . SER A 1 6   ? 5.36200  16.05000 -29.04000 1.000 113.75461 ? 325 SER A HB3  1 
ATOM   10   H  HG   . SER A 1 6   ? 3.83600  14.22200 -27.94000 1.000 135.02284 ? 325 SER A HG   1 
ATOM   11   N  N    . HIS A 1 7   ? 6.79600  17.39600 -27.32400 1.000 52.13414  ? 326 HIS A N    1 
ATOM   12   C  CA   . HIS A 1 7   ? 7.76900  18.46900 -27.20400 1.000 61.42964  ? 326 HIS A CA   1 
ATOM   13   C  C    . HIS A 1 7   ? 7.73000  19.10000 -25.81100 1.000 51.06131  ? 326 HIS A C    1 
ATOM   14   O  O    . HIS A 1 7   ? 6.82200  18.87000 -25.00700 1.000 58.94394  ? 326 HIS A O    1 
ATOM   15   C  CB   . HIS A 1 7   ? 7.53900  19.53400 -28.28000 1.000 54.52056  ? 326 HIS A CB   1 
ATOM   16   C  CG   . HIS A 1 7   ? 8.04900  19.14900 -29.63500 1.000 109.74263 ? 326 HIS A CG   1 
ATOM   17   N  ND1  . HIS A 1 7   ? 7.27400  18.48500 -30.56200 1.000 100.34853 ? 326 HIS A ND1  1 
ATOM   18   C  CD2  . HIS A 1 7   ? 9.25600  19.33600 -30.22100 1.000 84.77768  ? 326 HIS A CD2  1 
ATOM   19   C  CE1  . HIS A 1 7   ? 7.97900  18.28500 -31.66200 1.000 103.80683 ? 326 HIS A CE1  1 
ATOM   20   N  NE2  . HIS A 1 7   ? 9.18600  18.79000 -31.48000 1.000 131.89583 ? 326 HIS A NE2  1 
ATOM   21   H  H    . HIS A 1 7   ? 6.01000  17.65200 -27.56100 1.000 62.66000  ? 326 HIS A H    1 
ATOM   22   H  HA   . HIS A 1 7   ? 8.65000  18.08400 -27.33500 1.000 73.81460  ? 326 HIS A HA   1 
ATOM   23   H  HB2  . HIS A 1 7   ? 6.58900  19.71800 -28.34200 1.000 65.52370  ? 326 HIS A HB2  1 
ATOM   24   H  HB3  . HIS A 1 7   ? 7.97000  20.35800 -28.00400 1.000 65.52370  ? 326 HIS A HB3  1 
ATOM   25   H  HD2  . HIS A 1 7   ? 9.99400  19.75600 -29.84200 1.000 101.83225 ? 326 HIS A HD2  1 
ATOM   26   H  HE1  . HIS A 1 7   ? 7.67700  17.86100 -32.43300 1.000 124.66723 ? 326 HIS A HE1  1 
ATOM   27   H  HE2  . HIS A 1 7   ? 9.82400  18.77900 -32.05600 1.000 158.37403 ? 326 HIS A HE2  1 
ATOM   28   N  N    . CYS A 1 8   ? 8.74300  19.92100 -25.54500 1.000 51.26153  ? 327 CYS A N    1 
ATOM   29   C  CA   . CYS A 1 8   ? 8.95000  20.52900 -24.23600 1.000 51.47707  ? 327 CYS A CA   1 
ATOM   30   C  C    . CYS A 1 8   ? 7.82900  21.51400 -23.92200 1.000 53.46791  ? 327 CYS A C    1 
ATOM   31   O  O    . CYS A 1 8   ? 7.62800  22.48700 -24.65600 1.000 59.08636  ? 327 CYS A O    1 
ATOM   32   C  CB   . CYS A 1 8   ? 10.30900 21.22500 -24.22700 1.000 47.32923  ? 327 CYS A CB   1 
ATOM   33   S  SG   . CYS A 1 8   ? 10.78400 22.03700 -22.69900 1.000 47.49964  ? 327 CYS A SG   1 
ATOM   34   H  H    . CYS A 1 8   ? 9.33600  20.14200 -26.12700 1.000 61.61287  ? 327 CYS A H    1 
ATOM   35   H  HA   . CYS A 1 8   ? 8.93700  19.84400 -23.55000 1.000 61.87151  ? 327 CYS A HA   1 
ATOM   36   H  HB2  . CYS A 1 8   ? 10.98800 20.56800 -24.44500 1.000 56.89411  ? 327 CYS A HB2  1 
ATOM   37   H  HB3  . CYS A 1 8   ? 10.31600 21.88600 -24.93700 1.000 56.89411  ? 327 CYS A HB3  1 
ATOM   38   N  N    . GLN A 1 9   ? 7.10500  21.27200 -22.82800 1.000 39.61027  ? 328 GLN A N    1 
ATOM   39   C  CA   . GLN A 1 9   ? 5.96100  22.10700 -22.49500 1.000 46.18406  ? 328 GLN A CA   1 
ATOM   40   C  C    . GLN A 1 9   ? 5.71000  22.07900 -20.99400 1.000 53.01968  ? 328 GLN A C    1 
ATOM   41   O  O    . GLN A 1 9   ? 6.17400  21.18500 -20.28000 1.000 37.35020  ? 328 GLN A O    1 
ATOM   42   C  CB   . GLN A 1 9   ? 4.70700  21.65700 -23.24900 1.000 39.84101  ? 328 GLN A CB   1 
ATOM   43   C  CG   . GLN A 1 9   ? 4.29500  20.22400 -22.95400 1.000 68.99238  ? 328 GLN A CG   1 
ATOM   44   C  CD   . GLN A 1 9   ? 3.18800  19.75100 -23.87600 1.000 87.73815  ? 328 GLN A CD   1 
ATOM   45   O  OE1  . GLN A 1 9   ? 2.12000  20.36100 -23.94500 1.000 80.50640  ? 328 GLN A OE1  1 
ATOM   46   N  NE2  . GLN A 1 9   ? 3.43900  18.66200 -24.59600 1.000 113.30763 ? 328 GLN A NE2  1 
ATOM   47   H  H    . GLN A 1 9   ? 7.26100  20.63400 -22.27300 1.000 47.63135  ? 328 GLN A H    1 
ATOM   48   H  HA   . GLN A 1 9   ? 6.16400  23.01600 -22.76600 1.000 55.51990  ? 328 GLN A HA   1 
ATOM   49   H  HB2  . GLN A 1 9   ? 3.97300  22.24900 -23.02100 1.000 47.90824  ? 328 GLN A HB2  1 
ATOM   50   H  HB3  . GLN A 1 9   ? 4.86200  21.75000 -24.20200 1.000 47.90824  ? 328 GLN A HB3  1 
ATOM   51   H  HG2  . GLN A 1 9   ? 5.06500  19.64100 -23.04800 1.000 82.88989  ? 328 GLN A HG2  1 
ATOM   52   H  HG3  . GLN A 1 9   ? 3.99900  20.15600 -22.03300 1.000 82.88989  ? 328 GLN A HG3  1 
ATOM   53   H  HE21 . GLN A 1 9   ? 4.19700  18.26200 -24.52100 1.000 136.06819 ? 328 GLN A HE21 1 
ATOM   54   H  HE22 . GLN A 1 9   ? 2.84400  18.35700 -25.13700 1.000 136.06819 ? 328 GLN A HE22 1 
ATOM   55   N  N    . LYS A 1 10  ? 4.95500  23.07300 -20.52900 1.000 47.91646  ? 329 LYS A N    1 
ATOM   56   C  CA   . LYS A 1 10  ? 4.62600  23.18500 -19.11500 1.000 61.64528  ? 329 LYS A CA   1 
ATOM   57   C  C    . LYS A 1 10  ? 3.49300  22.23000 -18.75800 1.000 46.68432  ? 329 LYS A C    1 
ATOM   58   O  O    . LYS A 1 10  ? 2.47200  22.17400 -19.45000 1.000 49.36574  ? 329 LYS A O    1 
ATOM   59   C  CB   . LYS A 1 10  ? 4.23800  24.62900 -18.78100 1.000 47.60719  ? 329 LYS A CB   1 
ATOM   60   C  CG   . LYS A 1 10  ? 3.98700  24.89200 -17.30100 1.000 68.73200  ? 329 LYS A CG   1 
ATOM   61   C  CD   . LYS A 1 10  ? 3.82500  26.38500 -16.98200 1.000 55.11940  ? 329 LYS A CD   1 
ATOM   62   C  CE   . LYS A 1 10  ? 2.47000  26.92100 -17.42600 1.000 51.89218  ? 329 LYS A CE   1 
ATOM   63   N  NZ   . LYS A 1 10  ? 2.17300  28.27900 -16.87400 1.000 115.52374 ? 329 LYS A NZ   1 
ATOM   64   H  H    . LYS A 1 10  ? 4.62300  23.69500 -21.02200 1.000 57.59878  ? 329 LYS A H    1 
ATOM   65   H  HA   . LYS A 1 10  ? 5.40500  22.94300 -18.59000 1.000 74.07337  ? 329 LYS A HA   1 
ATOM   66   H  HB2  . LYS A 1 10  ? 4.94300  25.22000 -19.08700 1.000 57.22766  ? 329 LYS A HB2  1 
ATOM   67   H  HB3  . LYS A 1 10  ? 3.43800  24.86000 -19.27900 1.000 57.22766  ? 329 LYS A HB3  1 
ATOM   68   H  HG2  . LYS A 1 10  ? 3.18800  24.41800 -17.02300 1.000 82.57743  ? 329 LYS A HG2  1 
ATOM   69   H  HG3  . LYS A 1 10  ? 4.72400  24.53300 -16.78300 1.000 82.57743  ? 329 LYS A HG3  1 
ATOM   70   H  HD2  . LYS A 1 10  ? 3.93000  26.52400 -16.02800 1.000 66.24231  ? 329 LYS A HD2  1 
ATOM   71   H  HD3  . LYS A 1 10  ? 4.53000  26.88700 -17.42100 1.000 66.24231  ? 329 LYS A HD3  1 
ATOM   72   H  HE2  . LYS A 1 10  ? 2.44300  26.95800 -18.39500 1.000 62.36965  ? 329 LYS A HE2  1 
ATOM   73   H  HE3  . LYS A 1 10  ? 1.77600  26.30400 -17.14600 1.000 62.36965  ? 329 LYS A HE3  1 
ATOM   74   H  HZ1  . LYS A 1 10  ? 1.36900  28.27500 -16.49100 1.000 138.72752 ? 329 LYS A HZ1  1 
ATOM   75   H  HZ2  . LYS A 1 10  ? 2.78800  28.49500 -16.26800 1.000 138.72752 ? 329 LYS A HZ2  1 
ATOM   76   H  HZ3  . LYS A 1 10  ? 2.18400  28.87700 -17.53300 1.000 138.72752 ? 329 LYS A HZ3  1 
ATOM   77   N  N    . THR A 1 11  ? 3.68100  21.46500 -17.68600 1.000 44.14099  ? 330 THR A N    1 
ATOM   78   C  CA   . THR A 1 11  ? 2.67100  20.54600 -17.18500 1.000 54.07106  ? 330 THR A CA   1 
ATOM   79   C  C    . THR A 1 11  ? 2.46400  20.80500 -15.69900 1.000 45.11091  ? 330 THR A C    1 
ATOM   80   O  O    . THR A 1 11  ? 3.25400  21.49500 -15.04800 1.000 41.85767  ? 330 THR A O    1 
ATOM   81   C  CB   . THR A 1 11  ? 3.06300  19.07900 -17.42800 1.000 58.03961  ? 330 THR A CB   1 
ATOM   82   O  OG1  . THR A 1 11  ? 4.17400  18.73300 -16.59400 1.000 66.65424  ? 330 THR A OG1  1 
ATOM   83   C  CG2  . THR A 1 11  ? 3.45000  18.85300 -18.88200 1.000 83.70414  ? 330 THR A CG2  1 
ATOM   84   H  H    . THR A 1 11  ? 4.40800  21.46700 -17.22600 1.000 53.06822  ? 330 THR A H    1 
ATOM   85   H  HA   . THR A 1 11  ? 1.84300  20.70100 -17.66700 1.000 64.98430  ? 330 THR A HA   1 
ATOM   86   H  HB   . THR A 1 11  ? 2.29700  18.52200 -17.21600 1.000 69.74656  ? 330 THR A HB   1 
ATOM   87   H  HG1  . THR A 1 11  ? 4.47200  17.98200 -16.82200 1.000 80.08412  ? 330 THR A HG1  1 
ATOM   88   H  HG21 . THR A 1 11  ? 3.69300  17.92300 -19.01200 1.000 100.54399 ? 330 THR A HG21 1 
ATOM   89   H  HG22 . THR A 1 11  ? 2.69900  19.07300 -19.45500 1.000 100.54399 ? 330 THR A HG22 1 
ATOM   90   H  HG23 . THR A 1 11  ? 4.20500  19.41800 -19.10800 1.000 100.54399 ? 330 THR A HG23 1 
ATOM   91   N  N    . SER A 1 12  ? 1.38600  20.24000 -15.16300 1.000 49.58993  ? 331 SER A N    1 
ATOM   92   C  CA   . SER A 1 12  ? 1.00000  20.49200 -13.78200 1.000 52.35129  ? 331 SER A CA   1 
ATOM   93   C  C    . SER A 1 12  ? 1.90000  19.74300 -12.80700 1.000 57.15710  ? 331 SER A C    1 
ATOM   94   O  O    . SER A 1 12  ? 2.21800  18.56700 -13.00600 1.000 60.60127  ? 331 SER A O    1 
ATOM   95   C  CB   . SER A 1 12  ? -0.45700 20.08700 -13.55600 1.000 50.32052  ? 331 SER A CB   1 
ATOM   96   O  OG   . SER A 1 12  ? -0.81400 20.21400 -12.18800 1.000 81.13303  ? 331 SER A OG   1 
ATOM   97   H  H    . SER A 1 12  ? 0.86300  19.70500 -15.58700 1.000 59.60695  ? 331 SER A H    1 
ATOM   98   H  HA   . SER A 1 12  ? 1.09900  21.44300 -13.61700 1.000 62.92058  ? 331 SER A HA   1 
ATOM   99   H  HB2  . SER A 1 12  ? -1.03800 20.64300 -14.09800 1.000 60.48366  ? 331 SER A HB2  1 
ATOM   100  H  HB3  . SER A 1 12  ? -0.59000 19.17100 -13.84500 1.000 60.48366  ? 331 SER A HB3  1 
ATOM   101  H  HG   . SER A 1 12  ? -0.35600 20.82300 -11.83400 1.000 97.45867  ? 331 SER A HG   1 
ATOM   102  N  N    . LEU A 1 13  ? 2.30700  20.44000 -11.74400 1.000 48.60084  ? 332 LEU A N    1 
ATOM   103  C  CA   . LEU A 1 13  ? 3.02900  19.82000 -10.63200 1.000 41.09541  ? 332 LEU A CA   1 
ATOM   104  C  C    . LEU A 1 13  ? 2.59400  20.53900 -9.35800  1.000 42.76533  ? 332 LEU A C    1 
ATOM   105  O  O    . LEU A 1 13  ? 3.04500  21.65700 -9.08800  1.000 43.79125  ? 332 LEU A O    1 
ATOM   106  C  CB   . LEU A 1 13  ? 4.53700  19.89500 -10.82600 1.000 48.46893  ? 332 LEU A CB   1 
ATOM   107  C  CG   . LEU A 1 13  ? 5.33400  19.42100 -9.60600  1.000 55.33493  ? 332 LEU A CG   1 
ATOM   108  C  CD1  . LEU A 1 13  ? 5.13400  17.93100 -9.37000  1.000 57.01175  ? 332 LEU A CD1  1 
ATOM   109  C  CD2  . LEU A 1 13  ? 6.80900  19.76500 -9.73700  1.000 54.27990  ? 332 LEU A CD2  1 
ATOM   110  H  H    . LEU A 1 13  ? 2.17200  21.28400 -11.64800 1.000 58.42004  ? 332 LEU A H    1 
ATOM   111  H  HA   . LEU A 1 13  ? 2.81600  18.87500 -10.58000 1.000 49.41353  ? 332 LEU A HA   1 
ATOM   112  H  HB2  . LEU A 1 13  ? 4.78400  19.35700 -11.59400 1.000 58.26175  ? 332 LEU A HB2  1 
ATOM   113  H  HB3  . LEU A 1 13  ? 4.78500  20.81000 -11.03000 1.000 58.26175  ? 332 LEU A HB3  1 
ATOM   114  H  HG   . LEU A 1 13  ? 4.99400  19.89400 -8.83000  1.000 66.50095  ? 332 LEU A HG   1 
ATOM   115  H  HD11 . LEU A 1 13  ? 5.64700  17.65400 -8.59500  1.000 68.51314  ? 332 LEU A HD11 1 
ATOM   116  H  HD12 . LEU A 1 13  ? 4.19300  17.75100 -9.21600  1.000 68.51314  ? 332 LEU A HD12 1 
ATOM   117  H  HD13 . LEU A 1 13  ? 5.43400  17.43700 -10.14900 1.000 68.51314  ? 332 LEU A HD13 1 
ATOM   118  H  HD21 . LEU A 1 13  ? 7.28500  19.45300 -8.95200  1.000 65.23491  ? 332 LEU A HD21 1 
ATOM   119  H  HD22 . LEU A 1 13  ? 7.17300  19.33600 -10.52700 1.000 65.23491  ? 332 LEU A HD22 1 
ATOM   120  H  HD23 . LEU A 1 13  ? 6.91200  20.72600 -9.81600  1.000 65.23491  ? 332 LEU A HD23 1 
ATOM   121  N  N    . ARG A 1 14  ? 1.72100  19.89900 -8.58600  1.000 49.57424  ? 333 ARG A N    1 
ATOM   122  C  CA   . ARG A 1 14  ? 1.24900  20.45500 -7.32600  1.000 53.83419  ? 333 ARG A CA   1 
ATOM   123  C  C    . ARG A 1 14  ? 2.18500  20.00900 -6.20800  1.000 46.41373  ? 333 ARG A C    1 
ATOM   124  O  O    . ARG A 1 14  ? 2.36500  18.80700 -5.98600  1.000 59.89606  ? 333 ARG A O    1 
ATOM   125  C  CB   . ARG A 1 14  ? -0.18900 20.02000 -7.04700  1.000 59.34851  ? 333 ARG A CB   1 
ATOM   126  C  CG   . ARG A 1 14  ? -0.83700 20.76100 -5.89500  1.000 127.76749 ? 333 ARG A CG   1 
ATOM   127  C  CD   . ARG A 1 14  ? -2.35500 20.68300 -5.95100  1.000 99.03763  ? 333 ARG A CD   1 
ATOM   128  N  NE   . ARG A 1 14  ? -2.96300 21.57300 -4.96900  1.000 117.62685 ? 333 ARG A NE   1 
ATOM   129  C  CZ   . ARG A 1 14  ? -3.13800 22.87500 -5.14900  1.000 128.89556 ? 333 ARG A CZ   1 
ATOM   130  N  NH1  . ARG A 1 14  ? -2.77600 23.47100 -6.27500  1.000 74.31679  ? 333 ARG A NH1  1 
ATOM   131  N  NH2  . ARG A 1 14  ? -3.68800 23.59700 -4.17600  1.000 124.76192 ? 333 ARG A NH2  1 
ATOM   132  H  H    . ARG A 1 14  ? 1.38700  19.13100 -8.77900  1.000 59.58812  ? 333 ARG A H    1 
ATOM   133  H  HA   . ARG A 1 14  ? 1.25200  21.42400 -7.37700  1.000 64.70006  ? 333 ARG A HA   1 
ATOM   134  H  HB2  . ARG A 1 14  ? -0.72000 20.15500 -7.84700  1.000 71.31724  ? 333 ARG A HB2  1 
ATOM   135  H  HB3  . ARG A 1 14  ? -0.20000 19.06900 -6.85600  1.000 71.31724  ? 333 ARG A HB3  1 
ATOM   136  H  HG2  . ARG A 1 14  ? -0.52500 20.38800 -5.05500  1.000 153.42002 ? 333 ARG A HG2  1 
ATOM   137  H  HG3  . ARG A 1 14  ? -0.56100 21.69100 -5.91300  1.000 153.42002 ? 333 ARG A HG3  1 
ATOM   138  H  HD2  . ARG A 1 14  ? -2.66100 20.92000 -6.84000  1.000 118.94419 ? 333 ARG A HD2  1 
ATOM   139  H  HD3  . ARG A 1 14  ? -2.64100 19.77100 -5.78600  1.000 118.94419 ? 333 ARG A HD3  1 
ATOM   140  H  HE   . ARG A 1 14  ? -3.22500 21.23100 -4.22500  1.000 141.25126 ? 333 ARG A HE   1 
ATOM   141  H  HH11 . ARG A 1 14  ? -2.41900 23.01200 -6.90900  1.000 89.27918  ? 333 ARG A HH11 1 
ATOM   142  H  HH12 . ARG A 1 14  ? -2.89800 24.31700 -6.37200  1.000 89.27918  ? 333 ARG A HH12 1 
ATOM   143  H  HH21 . ARG A 1 14  ? -3.92500 23.21800 -3.44100  1.000 149.81333 ? 333 ARG A HH21 1 
ATOM   144  H  HH22 . ARG A 1 14  ? -3.80600 24.44200 -4.28200  1.000 149.81333 ? 333 ARG A HH22 1 
ATOM   145  N  N    . VAL A 1 15  ? 2.77800  20.97500 -5.50900  1.000 44.07466  ? 334 VAL A N    1 
ATOM   146  C  CA   . VAL A 1 15  ? 3.83300  20.72300 -4.53400  1.000 40.78677  ? 334 VAL A CA   1 
ATOM   147  C  C    . VAL A 1 15  ? 3.28400  20.94800 -3.13100  1.000 46.68030  ? 334 VAL A C    1 
ATOM   148  O  O    . VAL A 1 15  ? 2.64200  21.97100 -2.86600  1.000 51.31535  ? 334 VAL A O    1 
ATOM   149  C  CB   . VAL A 1 15  ? 5.05600  21.61900 -4.79800  1.000 43.83122  ? 334 VAL A CB   1 
ATOM   150  C  CG1  . VAL A 1 15  ? 6.06400  21.49200 -3.67200  1.000 47.16585  ? 334 VAL A CG1  1 
ATOM   151  C  CG2  . VAL A 1 15  ? 5.69200  21.25600 -6.12800  1.000 52.85924  ? 334 VAL A CG2  1 
ATOM   152  H  H    . VAL A 1 15  ? 2.57500  21.80700 -5.59000  1.000 52.98862  ? 334 VAL A H    1 
ATOM   153  H  HA   . VAL A 1 15  ? 4.12800  19.80300 -4.61700  1.000 49.04315  ? 334 VAL A HA   1 
ATOM   154  H  HB   . VAL A 1 15  ? 4.76100  22.54200 -4.83700  1.000 52.69650  ? 334 VAL A HB   1 
ATOM   155  H  HG11 . VAL A 1 15  ? 6.82700  22.06200 -3.85500  1.000 56.69805  ? 334 VAL A HG11 1 
ATOM   156  H  HG12 . VAL A 1 15  ? 5.65200  21.76200 -2.83600  1.000 56.69805  ? 334 VAL A HG12 1 
ATOM   157  H  HG13 . VAL A 1 15  ? 6.35900  20.57000 -3.60400  1.000 56.69805  ? 334 VAL A HG13 1 
ATOM   158  H  HG21 . VAL A 1 15  ? 6.46100  21.82600 -6.28500  1.000 63.53012  ? 334 VAL A HG21 1 
ATOM   159  H  HG22 . VAL A 1 15  ? 5.97600  20.32900 -6.10900  1.000 63.53012  ? 334 VAL A HG22 1 
ATOM   160  H  HG23 . VAL A 1 15  ? 5.04600  21.38200 -6.84100  1.000 63.53012  ? 334 VAL A HG23 1 
ATOM   161  N  N    . ASN A 1 16  ? 3.54900  20.00000 -2.23600  1.000 51.88610  ? 335 ASN A N    1 
ATOM   162  C  CA   . ASN A 1 16  ? 3.15100  20.08600 -0.83600  1.000 73.23459  ? 335 ASN A CA   1 
ATOM   163  C  C    . ASN A 1 16  ? 4.38600  20.39900 0.00500   1.000 43.72931  ? 335 ASN A C    1 
ATOM   164  O  O    . ASN A 1 16  ? 5.38200  19.67000 -0.05800  1.000 45.55734  ? 335 ASN A O    1 
ATOM   165  C  CB   . ASN A 1 16  ? 2.49800  18.77800 -0.38800  1.000 55.61879  ? 335 ASN A CB   1 
ATOM   166  C  CG   . ASN A 1 16  ? 2.07300  18.80000 1.07100   1.000 115.76121 ? 335 ASN A CG   1 
ATOM   167  O  OD1  . ASN A 1 16  ? 2.91400  18.89400 1.97200   1.000 58.66338  ? 335 ASN A OD1  1 
ATOM   168  N  ND2  . ASN A 1 16  ? 0.77300  18.68900 1.31800   1.000 60.47151  ? 335 ASN A ND2  1 
ATOM   169  H  H    . ASN A 1 16  ? 3.97200  19.27700 -2.43000  1.000 62.36235  ? 335 ASN A H    1 
ATOM   170  H  HA   . ASN A 1 16  ? 2.49800  20.79400 -0.72000  1.000 87.98054  ? 335 ASN A HA   1 
ATOM   171  H  HB2  . ASN A 1 16  ? 1.72300  18.60200 -0.94400  1.000 66.84158  ? 335 ASN A HB2  1 
ATOM   172  H  HB3  . ASN A 1 16  ? 3.12000  18.04700 -0.52800  1.000 66.84158  ? 335 ASN A HB3  1 
ATOM   173  H  HD21 . ASN A 1 16  ? 0.48900  18.68100 2.13000   1.000 72.66485  ? 335 ASN A HD21 1 
ATOM   174  H  HD22 . ASN A 1 16  ? 0.21500  18.62600 0.66600   1.000 72.66485  ? 335 ASN A HD22 1 
ATOM   175  N  N    . PHE A 1 17  ? 4.31700  21.47900 0.79200   1.000 54.63348  ? 336 PHE A N    1 
ATOM   176  C  CA   . PHE A 1 17  ? 5.49400  21.91900 1.53900   1.000 52.41873  ? 336 PHE A CA   1 
ATOM   177  C  C    . PHE A 1 17  ? 5.85700  20.94900 2.65700   1.000 52.74328  ? 336 PHE A C    1 
ATOM   178  O  O    . PHE A 1 17  ? 7.03200  20.85500 3.03000   1.000 57.05900  ? 336 PHE A O    1 
ATOM   179  C  CB   . PHE A 1 17  ? 5.27500  23.32500 2.10600   1.000 57.70341  ? 336 PHE A CB   1 
ATOM   180  C  CG   . PHE A 1 17  ? 5.19400  24.40200 1.05500   1.000 59.15881  ? 336 PHE A CG   1 
ATOM   181  C  CD1  . PHE A 1 17  ? 6.31500  24.76100 0.31700   1.000 62.15656  ? 336 PHE A CD1  1 
ATOM   182  C  CD2  . PHE A 1 17  ? 3.99600  25.06300 0.81400   1.000 51.67750  ? 336 PHE A CD2  1 
ATOM   183  C  CE1  . PHE A 1 17  ? 6.24200  25.75300 -0.66100  1.000 57.86564  ? 336 PHE A CE1  1 
ATOM   184  C  CE2  . PHE A 1 17  ? 3.91800  26.05900 -0.15300  1.000 58.55668  ? 336 PHE A CE2  1 
ATOM   185  C  CZ   . PHE A 1 17  ? 5.04200  26.40400 -0.88900  1.000 46.38903  ? 336 PHE A CZ   1 
ATOM   186  H  H    . PHE A 1 17  ? 3.61300  21.96000 0.90400   1.000 65.65920  ? 336 PHE A H    1 
ATOM   187  H  HA   . PHE A 1 17  ? 6.23800  21.94000 0.91700   1.000 63.00151  ? 336 PHE A HA   1 
ATOM   188  H  HB2  . PHE A 1 17  ? 4.45600  23.33100 2.62600   1.000 69.34312  ? 336 PHE A HB2  1 
ATOM   189  H  HB3  . PHE A 1 17  ? 6.00000  23.53500 2.71600   1.000 69.34312  ? 336 PHE A HB3  1 
ATOM   190  H  HD1  . PHE A 1 17  ? 7.12500  24.33400 0.47700   1.000 74.68691  ? 336 PHE A HD1  1 
ATOM   191  H  HD2  . PHE A 1 17  ? 3.23900  24.83700 1.30400   1.000 62.11203  ? 336 PHE A HD2  1 
ATOM   192  H  HE1  . PHE A 1 17  ? 6.99600  25.97600 -1.15800  1.000 69.53780  ? 336 PHE A HE1  1 
ATOM   193  H  HE2  . PHE A 1 17  ? 3.11100  26.49500 -0.30700  1.000 70.36705  ? 336 PHE A HE2  1 
ATOM   194  H  HZ   . PHE A 1 17  ? 4.98900  27.07100 -1.53400  1.000 55.76587  ? 336 PHE A HZ   1 
ATOM   195  N  N    . GLU A 1 18  ? 4.87900  20.22700 3.20800   1.000 67.04394  ? 337 GLU A N    1 
ATOM   196  C  CA   . GLU A 1 18  ? 5.20000  19.21400 4.20900   1.000 71.09169  ? 337 GLU A CA   1 
ATOM   197  C  C    . GLU A 1 18  ? 6.02000  18.08500 3.59500   1.000 59.97407  ? 337 GLU A C    1 
ATOM   198  O  O    . GLU A 1 18  ? 6.99200  17.61400 4.19700   1.000 56.53502  ? 337 GLU A O    1 
ATOM   199  C  CB   . GLU A 1 18  ? 3.91900  18.67200 4.85000   1.000 71.71479  ? 337 GLU A CB   1 
ATOM   200  C  CG   . GLU A 1 18  ? 4.14000  17.54300 5.85200   1.000 123.78750 ? 337 GLU A CG   1 
ATOM   201  C  CD   . GLU A 1 18  ? 2.84700  17.12900 6.58200   1.000 136.13058 ? 337 GLU A CD   1 
ATOM   202  O  OE1  . GLU A 1 18  ? 2.03600  18.01500 6.93500   1.000 91.65882  ? 337 GLU A OE1  1 
ATOM   203  O  OE2  . GLU A 1 18  ? 2.64100  15.91100 6.80400   1.000 84.82704  ? 337 GLU A OE2  1 
ATOM   204  H  H    . GLU A 1 18  ? 4.04300  20.30600 3.02100   1.000 80.55176  ? 337 GLU A H    1 
ATOM   205  H  HA   . GLU A 1 18  ? 5.73700  19.62900 4.90200   1.000 85.40906  ? 337 GLU A HA   1 
ATOM   206  H  HB2  . GLU A 1 18  ? 3.46200  19.40100 5.29700   1.000 86.15678  ? 337 GLU A HB2  1 
ATOM   207  H  HB3  . GLU A 1 18  ? 3.32900  18.35500 4.14800   1.000 86.15678  ? 337 GLU A HB3  1 
ATOM   208  H  HG2  . GLU A 1 18  ? 4.50600  16.77300 5.38900   1.000 148.64403 ? 337 GLU A HG2  1 
ATOM   209  H  HG3  . GLU A 1 18  ? 4.80000  17.82100 6.50600   1.000 148.64403 ? 337 GLU A HG3  1 
ATOM   210  N  N    . ASP A 1 19  ? 5.66100  17.66200 2.37700   1.000 71.27921  ? 338 ASP A N    1 
ATOM   211  C  CA   . ASP A 1 19  ? 6.35300  16.55700 1.71900   1.000 65.06831  ? 338 ASP A CA   1 
ATOM   212  C  C    . ASP A 1 19  ? 7.81700  16.86900 1.42600   1.000 57.09111  ? 338 ASP A C    1 
ATOM   213  O  O    . ASP A 1 19  ? 8.61400  15.93800 1.27000   1.000 55.34437  ? 338 ASP A O    1 
ATOM   214  C  CB   . ASP A 1 19  ? 5.64600  16.18400 0.40900   1.000 57.48939  ? 338 ASP A CB   1 
ATOM   215  C  CG   . ASP A 1 19  ? 4.24600  15.61400 0.62600   1.000 122.97326 ? 338 ASP A CG   1 
ATOM   216  O  OD1  . ASP A 1 19  ? 3.83400  15.45100 1.79200   1.000 94.61650  ? 338 ASP A OD1  1 
ATOM   217  O  OD2  . ASP A 1 19  ? 3.56000  15.32500 -0.37700  1.000 71.60106  ? 338 ASP A OD2  1 
ATOM   218  H  H    . ASP A 1 19  ? 5.01900  18.00400 1.91800   1.000 85.63408  ? 338 ASP A H    1 
ATOM   219  H  HA   . ASP A 1 19  ? 6.32700  15.81000 2.33800   1.000 78.18100  ? 338 ASP A HA   1 
ATOM   220  H  HB2  . ASP A 1 19  ? 5.58500  16.97100 -0.15500  1.000 69.08629  ? 338 ASP A HB2  1 
ATOM   221  H  HB3  . ASP A 1 19  ? 6.18400  15.53300 -0.06900  1.000 69.08629  ? 338 ASP A HB3  1 
ATOM   222  N  N    . ILE A 1 20  ? 8.19100  18.14600 1.33500   1.000 55.06368  ? 339 ILE A N    1 
ATOM   223  C  CA   . ILE A 1 20  ? 9.56000  18.54000 1.02400   1.000 77.71585  ? 339 ILE A CA   1 
ATOM   224  C  C    . ILE A 1 20  ? 10.25700 19.17600 2.22100   1.000 59.47862  ? 339 ILE A C    1 
ATOM   225  O  O    . ILE A 1 20  ? 11.34300 19.74700 2.07400   1.000 54.52553  ? 339 ILE A O    1 
ATOM   226  C  CB   . ILE A 1 20  ? 9.60900  19.46900 -0.20200  1.000 55.83017  ? 339 ILE A CB   1 
ATOM   227  C  CG1  . ILE A 1 20  ? 9.00400  20.83800 0.12200   1.000 53.49011  ? 339 ILE A CG1  1 
ATOM   228  C  CG2  . ILE A 1 20  ? 8.86500  18.83300 -1.37100  1.000 60.74323  ? 339 ILE A CG2  1 
ATOM   229  C  CD1  . ILE A 1 20  ? 9.34600  21.90800 -0.88300  1.000 55.44941  ? 339 ILE A CD1  1 
ATOM   230  H  H    . ILE A 1 20  ? 7.65400  18.80800 1.45300   1.000 66.17545  ? 339 ILE A H    1 
ATOM   231  H  HA   . ILE A 1 20  ? 10.04600 17.72900 0.80600   1.000 93.35806  ? 339 ILE A HA   1 
ATOM   232  H  HB   . ILE A 1 20  ? 10.53900 19.59800 -0.44700  1.000 67.09524  ? 339 ILE A HB   1 
ATOM   233  H  HG12 . ILE A 1 20  ? 8.03900  20.75200 0.17400   1.000 64.28717  ? 339 ILE A HG12 1 
ATOM   234  H  HG13 . ILE A 1 20  ? 9.31100  21.11900 0.99800   1.000 64.28717  ? 339 ILE A HG13 1 
ATOM   235  H  HG21 . ILE A 1 20  ? 8.90100  19.42500 -2.13800  1.000 72.99091  ? 339 ILE A HG21 1 
ATOM   236  H  HG22 . ILE A 1 20  ? 9.28000  17.98600 -1.59700  1.000 72.99091  ? 339 ILE A HG22 1 
ATOM   237  H  HG23 . ILE A 1 20  ? 7.93900  18.68300 -1.12200  1.000 72.99091  ? 339 ILE A HG23 1 
ATOM   238  H  HD11 . ILE A 1 20  ? 8.93300  22.74500 -0.61800  1.000 66.63833  ? 339 ILE A HD11 1 
ATOM   239  H  HD12 . ILE A 1 20  ? 10.30900 22.02100 -0.92100  1.000 66.63833  ? 339 ILE A HD12 1 
ATOM   240  H  HD13 . ILE A 1 20  ? 9.01700  21.64800 -1.75800  1.000 66.63833  ? 339 ILE A HD13 1 
ATOM   241  N  N    . GLY A 1 21  ? 9.66300  19.08700 3.41000   1.000 65.81429  ? 340 GLY A N    1 
ATOM   242  C  CA   . GLY A 1 21  ? 10.32300 19.54700 4.61600   1.000 52.11061  ? 340 GLY A CA   1 
ATOM   243  C  C    . GLY A 1 21  ? 10.37500 21.04500 4.79800   1.000 96.81136  ? 340 GLY A C    1 
ATOM   244  O  O    . GLY A 1 21  ? 11.25700 21.54100 5.50700   1.000 57.60781  ? 340 GLY A O    1 
ATOM   245  H  H    . GLY A 1 21  ? 8.87700  18.76200 3.53400   1.000 79.07618  ? 340 GLY A H    1 
ATOM   246  H  HA2  . GLY A 1 21  ? 9.87000  19.15900 5.38100   1.000 62.63177  ? 340 GLY A HA2  1 
ATOM   247  H  HA3  . GLY A 1 21  ? 11.23100 19.20500 4.62000   1.000 62.63177  ? 340 GLY A HA3  1 
ATOM   248  N  N    . TRP A 1 22  ? 9.45900  21.78700 4.17800   1.000 49.78874  ? 341 TRP A N    1 
ATOM   249  C  CA   . TRP A 1 22  ? 9.40600  23.23500 4.31200   1.000 42.47880  ? 341 TRP A CA   1 
ATOM   250  C  C    . TRP A 1 22  ? 8.28700  23.71600 5.22200   1.000 53.63263  ? 341 TRP A C    1 
ATOM   251  O  O    . TRP A 1 22  ? 8.21700  24.91600 5.50800   1.000 52.83591  ? 341 TRP A O    1 
ATOM   252  C  CB   . TRP A 1 22  ? 9.25500  23.89400 2.93300   1.000 54.51145  ? 341 TRP A CB   1 
ATOM   253  C  CG   . TRP A 1 22  ? 10.53800 23.94900 2.17700   1.000 63.23712  ? 341 TRP A CG   1 
ATOM   254  C  CD1  . TRP A 1 22  ? 11.68900 23.27900 2.47200   1.000 73.96817  ? 341 TRP A CD1  1 
ATOM   255  C  CD2  . TRP A 1 22  ? 10.81600 24.73300 1.01100   1.000 50.67842  ? 341 TRP A CD2  1 
ATOM   256  N  NE1  . TRP A 1 22  ? 12.66500 23.59000 1.55800   1.000 52.58881  ? 341 TRP A NE1  1 
ATOM   257  C  CE2  . TRP A 1 22  ? 12.15500 24.48000 0.65100   1.000 58.02171  ? 341 TRP A CE2  1 
ATOM   258  C  CE3  . TRP A 1 22  ? 10.06400 25.62000 0.23500   1.000 48.78339  ? 341 TRP A CE3  1 
ATOM   259  C  CZ2  . TRP A 1 22  ? 12.75800 25.08500 -0.45200  1.000 46.35286  ? 341 TRP A CZ2  1 
ATOM   260  C  CZ3  . TRP A 1 22  ? 10.66500 26.21800 -0.86000  1.000 57.82346  ? 341 TRP A CZ3  1 
ATOM   261  C  CH2  . TRP A 1 22  ? 11.99800 25.94800 -1.19300  1.000 59.16662  ? 341 TRP A CH2  1 
ATOM   262  H  H    . TRP A 1 22  ? 8.85000  21.46000 3.66600   1.000 59.84552  ? 341 TRP A H    1 
ATOM   263  H  HA   . TRP A 1 22  ? 10.24400 23.49700 4.72300   1.000 51.07360  ? 341 TRP A HA   1 
ATOM   264  H  HB2  . TRP A 1 22  ? 8.59900  23.40200 2.41400   1.000 65.51277  ? 341 TRP A HB2  1 
ATOM   265  H  HB3  . TRP A 1 22  ? 8.91100  24.79400 3.04500   1.000 65.51277  ? 341 TRP A HB3  1 
ATOM   266  H  HD1  . TRP A 1 22  ? 11.79700 22.69600 3.18800   1.000 88.86083  ? 341 TRP A HD1  1 
ATOM   267  H  HE1  . TRP A 1 22  ? 13.46600 23.27700 1.55600   1.000 63.20560  ? 341 TRP A HE1  1 
ATOM   268  H  HE3  . TRP A 1 22  ? 9.17800  25.80500 0.45000   1.000 58.63910  ? 341 TRP A HE3  1 
ATOM   269  H  HZ2  . TRP A 1 22  ? 13.64300 24.90800 -0.67500  1.000 55.72247  ? 341 TRP A HZ2  1 
ATOM   270  H  HZ3  . TRP A 1 22  ? 10.17400 26.81000 -1.38400  1.000 69.48718  ? 341 TRP A HZ3  1 
ATOM   271  H  HH2  . TRP A 1 22  ? 12.37500 26.36400 -1.93400  1.000 71.09898  ? 341 TRP A HH2  1 
ATOM   272  N  N    . ASP A 1 23  ? 7.42500  22.82500 5.66300   1.000 62.85570  ? 342 ASP A N    1 
ATOM   273  C  CA   . ASP A 1 23  ? 6.31800  23.21600 6.52300   1.000 61.49003  ? 342 ASP A CA   1 
ATOM   274  C  C    . ASP A 1 23  ? 6.77200  23.73100 7.88000   1.000 70.98620  ? 342 ASP A C    1 
ATOM   275  O  O    . ASP A 1 23  ? 5.95200  24.30700 8.60300   1.000 68.58899  ? 342 ASP A O    1 
ATOM   276  C  CB   . ASP A 1 23  ? 5.37600  22.03500 6.71900   1.000 93.11071  ? 342 ASP A CB   1 
ATOM   277  C  CG   . ASP A 1 23  ? 6.08900  20.82700 7.26800   1.000 90.65067  ? 342 ASP A CG   1 
ATOM   278  O  OD1  . ASP A 1 23  ? 7.32100  20.90200 7.45100   1.000 105.04051 ? 342 ASP A OD1  1 
ATOM   279  O  OD2  . ASP A 1 23  ? 5.42900  19.80100 7.52100   1.000 96.55766  ? 342 ASP A OD2  1 
ATOM   280  H  H    . ASP A 1 23  ? 7.46300  21.98300 5.49000   1.000 75.52587  ? 342 ASP A H    1 
ATOM   281  H  HA   . ASP A 1 23  ? 5.86100  23.94700 6.07800   1.000 73.88707  ? 342 ASP A HA   1 
ATOM   282  H  HB2  . ASP A 1 23  ? 4.66100  22.28900 7.32300   1.000 111.83188 ? 342 ASP A HB2  1 
ATOM   283  H  HB3  . ASP A 1 23  ? 4.96300  21.80700 5.87100   1.000 111.83188 ? 342 ASP A HB3  1 
ATOM   284  N  N    . SER A 1 24  ? 8.03600  23.52900 8.27700   1.000 70.27092  ? 343 SER A N    1 
ATOM   285  C  CA   . SER A 1 24  ? 8.49200  24.09500 9.54000   1.000 107.68932 ? 343 SER A CA   1 
ATOM   286  C  C    . SER A 1 24  ? 8.50900  25.60900 9.46600   1.000 97.50021  ? 343 SER A C    1 
ATOM   287  O  O    . SER A 1 24  ? 8.40600  26.25900 10.51600  1.000 93.44315  ? 343 SER A O    1 
ATOM   288  C  CB   . SER A 1 24  ? 9.79300  23.38100 9.96400   1.000 113.25760 ? 343 SER A CB   1 
ATOM   289  O  OG   . SER A 1 24  ? 10.78200 23.43000 8.93700   1.000 122.00266 ? 343 SER A OG   1 
ATOM   290  H  H    . SER A 1 24  ? 8.62500  23.09000 7.83000   1.000 84.42413  ? 343 SER A H    1 
ATOM   291  H  HA   . SER A 1 24  ? 7.87600  23.92700 10.27000  1.000 129.32621 ? 343 SER A HA   1 
ATOM   292  H  HB2  . SER A 1 24  ? 10.14200 23.79500 10.76900  1.000 136.00816 ? 343 SER A HB2  1 
ATOM   293  H  HB3  . SER A 1 24  ? 9.59800  22.45600 10.18200  1.000 136.00816 ? 343 SER A HB3  1 
ATOM   294  H  HG   . SER A 1 24  ? 11.47600 23.03600 9.19700   1.000 146.50222 ? 343 SER A HG   1 
ATOM   295  N  N    . TRP A 1 25  ? 8.60700  26.16400 8.25600   1.000 55.02118  ? 344 TRP A N    1 
ATOM   296  C  CA   . TRP A 1 25  ? 8.81600  27.62800 8.10200   1.000 71.44959  ? 344 TRP A CA   1 
ATOM   297  C  C    . TRP A 1 25  ? 7.78200  28.26400 7.17000   1.000 97.36758  ? 344 TRP A C    1 
ATOM   298  O  O    . TRP A 1 25  ? 7.56400  29.46500 7.31400   1.000 81.94020  ? 344 TRP A O    1 
ATOM   299  C  CB   . TRP A 1 25  ? 10.25700 27.94500 7.68800   1.000 63.28931  ? 344 TRP A CB   1 
ATOM   300  C  CG   . TRP A 1 25  ? 10.59400 27.77800 6.24200   1.000 75.19290  ? 344 TRP A CG   1 
ATOM   301  C  CD1  . TRP A 1 25  ? 10.90500 26.62100 5.58900   1.000 142.43420 ? 344 TRP A CD1  1 
ATOM   302  C  CD2  . TRP A 1 25  ? 10.73000 28.83100 5.27500   1.000 88.72318  ? 344 TRP A CD2  1 
ATOM   303  N  NE1  . TRP A 1 25  ? 11.19200 26.87800 4.27600   1.000 111.60293 ? 344 TRP A NE1  1 
ATOM   304  C  CE2  . TRP A 1 25  ? 11.09900 28.22600 4.05700   1.000 122.76351 ? 344 TRP A CE2  1 
ATOM   305  C  CE3  . TRP A 1 25  ? 10.56300 30.21700 5.32200   1.000 81.26937  ? 344 TRP A CE3  1 
ATOM   306  C  CZ2  . TRP A 1 25  ? 11.30300 28.96600 2.89500   1.000 96.31780  ? 344 TRP A CZ2  1 
ATOM   307  C  CZ3  . TRP A 1 25  ? 10.75700 30.94500 4.17200   1.000 94.52642  ? 344 TRP A CZ3  1 
ATOM   308  C  CH2  . TRP A 1 25  ? 11.12100 30.32600 2.97900   1.000 111.41947 ? 344 TRP A CH2  1 
ATOM   309  H  H    . TRP A 1 25  ? 8.55700  25.72700 7.51700   1.000 66.12445  ? 344 TRP A H    1 
ATOM   310  H  HA   . TRP A 1 25  ? 8.67700  28.03400 8.97200   1.000 85.83854  ? 344 TRP A HA   1 
ATOM   311  H  HB2  . TRP A 1 25  ? 10.44900 28.86200 7.93900   1.000 76.04620  ? 344 TRP A HB2  1 
ATOM   312  H  HB3  . TRP A 1 25  ? 10.85200 27.37900 8.20400   1.000 76.04620  ? 344 TRP A HB3  1 
ATOM   313  H  HD1  . TRP A 1 25  ? 10.92000 25.77800 5.98100   1.000 171.02007 ? 344 TRP A HD1  1 
ATOM   314  H  HE1  . TRP A 1 25  ? 11.39700 26.28800 3.68500   1.000 134.02254 ? 344 TRP A HE1  1 
ATOM   315  H  HE3  . TRP A 1 25  ? 10.32500 30.63900 6.11600   1.000 97.62228  ? 344 TRP A HE3  1 
ATOM   316  H  HZ2  . TRP A 1 25  ? 11.55100 28.55800 2.09700   1.000 115.68039 ? 344 TRP A HZ2  1 
ATOM   317  H  HZ3  . TRP A 1 25  ? 10.64300 31.86800 4.19100   1.000 113.53073 ? 344 TRP A HZ3  1 
ATOM   318  H  HH2  . TRP A 1 25  ? 11.24400 30.84700 2.21800   1.000 133.80239 ? 344 TRP A HH2  1 
ATOM   319  N  N    . ILE A 1 26  ? 7.14400  27.52200 6.27300   1.000 58.16291  ? 345 ILE A N    1 
ATOM   320  C  CA   . ILE A 1 26  ? 6.08200  28.05200 5.42600   1.000 68.43805  ? 345 ILE A CA   1 
ATOM   321  C  C    . ILE A 1 26  ? 4.75200  27.62700 6.03600   1.000 63.34362  ? 345 ILE A C    1 
ATOM   322  O  O    . ILE A 1 26  ? 4.39100  26.44600 6.00700   1.000 62.69675  ? 345 ILE A O    1 
ATOM   323  C  CB   . ILE A 1 26  ? 6.21800  27.57100 3.97600   1.000 60.23801  ? 345 ILE A CB   1 
ATOM   324  C  CG1  . ILE A 1 26  ? 7.50500  28.12300 3.35700   1.000 60.64773  ? 345 ILE A CG1  1 
ATOM   325  C  CG2  . ILE A 1 26  ? 5.00700  27.99200 3.15800   1.000 66.54292  ? 345 ILE A CG2  1 
ATOM   326  C  CD1  . ILE A 1 26  ? 7.70000  27.74500 1.90900   1.000 70.95080  ? 345 ILE A CD1  1 
ATOM   327  H  H    . ILE A 1 26  ? 7.31600  26.69000 6.13700   1.000 69.89452  ? 345 ILE A H    1 
ATOM   328  H  HA   . ILE A 1 26  ? 6.13900  29.02000 5.39000   1.000 82.22469  ? 345 ILE A HA   1 
ATOM   329  H  HB   . ILE A 1 26  ? 6.26300  26.60200 3.97300   1.000 72.38465  ? 345 ILE A HB   1 
ATOM   330  H  HG12 . ILE A 1 26  ? 7.50000  29.09000 3.43100   1.000 72.87631  ? 345 ILE A HG12 1 
ATOM   331  H  HG13 . ILE A 1 26  ? 8.26300  27.80300 3.87000   1.000 72.87631  ? 345 ILE A HG13 1 
ATOM   332  H  HG21 . ILE A 1 26  ? 5.10900  27.68000 2.24500   1.000 79.95053  ? 345 ILE A HG21 1 
ATOM   333  H  HG22 . ILE A 1 26  ? 4.20500  27.60500 3.54400   1.000 79.95053  ? 345 ILE A HG22 1 
ATOM   334  H  HG23 . ILE A 1 26  ? 4.93300  28.95900 3.16300   1.000 79.95053  ? 345 ILE A HG23 1 
ATOM   335  H  HD11 . ILE A 1 26  ? 8.53000  28.12600 1.58400   1.000 85.23999  ? 345 ILE A HD11 1 
ATOM   336  H  HD12 . ILE A 1 26  ? 7.73500  26.77900 1.82800   1.000 85.23999  ? 345 ILE A HD12 1 
ATOM   337  H  HD13 . ILE A 1 26  ? 6.96000  28.08600 1.38300   1.000 85.23999  ? 345 ILE A HD13 1 
ATOM   338  N  N    . ILE A 1 27  ? 4.02300  28.59200 6.59600   1.000 70.98411  ? 346 ILE A N    1 
ATOM   339  C  CA   . ILE A 1 27  ? 2.74700  28.29200 7.24000   1.000 65.20931  ? 346 ILE A CA   1 
ATOM   340  C  C    . ILE A 1 27  ? 1.66700  28.03600 6.19900   1.000 75.62336  ? 346 ILE A C    1 
ATOM   341  O  O    . ILE A 1 27  ? 1.01700  26.98300 6.19400   1.000 75.42459  ? 346 ILE A O    1 
ATOM   342  C  CB   . ILE A 1 27  ? 2.34200  29.43400 8.19000   1.000 67.41447  ? 346 ILE A CB   1 
ATOM   343  C  CG1  . ILE A 1 27  ? 3.51900  29.84300 9.07400   1.000 91.78815  ? 346 ILE A CG1  1 
ATOM   344  C  CG2  . ILE A 1 27  ? 1.15300  29.02000 9.04400   1.000 93.88044  ? 346 ILE A CG2  1 
ATOM   345  C  CD1  . ILE A 1 27  ? 3.22100  31.02900 9.96300   1.000 74.34409  ? 346 ILE A CD1  1 
ATOM   346  H  H    . ILE A 1 27  ? 4.24900  29.42200 6.61300   1.000 85.27997  ? 346 ILE A H    1 
ATOM   347  H  HA   . ILE A 1 27  ? 2.85000  27.48400 7.76700   1.000 78.35020  ? 346 ILE A HA   1 
ATOM   348  H  HB   . ILE A 1 27  ? 2.08400  30.20000 7.65300   1.000 80.99640  ? 346 ILE A HB   1 
ATOM   349  H  HG12 . ILE A 1 27  ? 3.77600  29.08900 9.62800   1.000 110.24481 ? 346 ILE A HG12 1 
ATOM   350  H  HG13 . ILE A 1 27  ? 4.28000  30.05300 8.51000   1.000 110.24481 ? 346 ILE A HG13 1 
ATOM   351  H  HG21 . ILE A 1 27  ? 0.91000  29.74900 9.63600   1.000 112.75556 ? 346 ILE A HG21 1 
ATOM   352  H  HG22 . ILE A 1 27  ? 0.40100  28.80600 8.47000   1.000 112.75556 ? 346 ILE A HG22 1 
ATOM   353  H  HG23 . ILE A 1 27  ? 1.38900  28.24100 9.57100   1.000 112.75556 ? 346 ILE A HG23 1 
ATOM   354  H  HD11 . ILE A 1 27  ? 4.00300  31.23800 10.49700  1.000 89.31194  ? 346 ILE A HD11 1 
ATOM   355  H  HD12 . ILE A 1 27  ? 2.99000  31.79500 9.41400   1.000 89.31194  ? 346 ILE A HD12 1 
ATOM   356  H  HD13 . ILE A 1 27  ? 2.47800  30.81600 10.54900  1.000 89.31194  ? 346 ILE A HD13 1 
ATOM   357  N  N    . ALA A 1 28  ? 1.45700  28.99700 5.30600   1.000 59.02389  ? 347 ALA A N    1 
ATOM   358  C  CA   . ALA A 1 28  ? 0.42200  28.92500 4.29000   1.000 64.06732  ? 347 ALA A CA   1 
ATOM   359  C  C    . ALA A 1 28  ? 0.98300  29.42000 2.96600   1.000 61.79645  ? 347 ALA A C    1 
ATOM   360  O  O    . ALA A 1 28  ? 1.84600  30.30700 2.94900   1.000 57.34917  ? 347 ALA A O    1 
ATOM   361  C  CB   . ALA A 1 28  ? -0.80800 29.76100 4.68000   1.000 54.65188  ? 347 ALA A CB   1 
ATOM   362  H  H    . ALA A 1 28  ? 1.92100  29.72000 5.27500   1.000 70.92769  ? 347 ALA A H    1 
ATOM   363  H  HA   . ALA A 1 28  ? 0.13900  28.00100 4.20700   1.000 76.97981  ? 347 ALA A HA   1 
ATOM   364  H  HB1  . ALA A 1 28  ? -1.48000 29.69300 3.98400   1.000 65.68129  ? 347 ALA A HB1  1 
ATOM   365  H  HB2  . ALA A 1 28  ? -1.17400 29.42900 5.51500   1.000 65.68129  ? 347 ALA A HB2  1 
ATOM   366  H  HB3  . ALA A 1 28  ? -0.54800 30.68900 4.78800   1.000 65.68129  ? 347 ALA A HB3  1 
ATOM   367  N  N    . PRO A 1 29  ? 0.51600  28.86600 1.83900   1.000 57.81538  ? 348 PRO A N    1 
ATOM   368  C  CA   . PRO A 1 29  ? -0.49900 27.81000 1.70400   1.000 55.52977  ? 348 PRO A CA   1 
ATOM   369  C  C    . PRO A 1 29  ? 0.06400  26.42000 1.97400   1.000 53.53909  ? 348 PRO A C    1 
ATOM   370  O  O    . PRO A 1 29  ? 1.27500  26.24100 2.06900   1.000 54.40890  ? 348 PRO A O    1 
ATOM   371  C  CB   . PRO A 1 29  ? -0.95400 27.96900 0.24900   1.000 59.04041  ? 348 PRO A CB   1 
ATOM   372  C  CG   . PRO A 1 29  ? 0.28700  28.42400 -0.45900  1.000 57.06933  ? 348 PRO A CG   1 
ATOM   373  C  CD   . PRO A 1 29  ? 0.99100  29.33300 0.52300   1.000 64.22541  ? 348 PRO A CD   1 
ATOM   374  H  HA   . PRO A 1 29  ? -1.22000 27.89600 2.34700   1.000 66.73475  ? 348 PRO A HA   1 
ATOM   375  H  HB2  . PRO A 1 29  ? -1.28600 27.13300 -0.11400  1.000 70.94752  ? 348 PRO A HB2  1 
ATOM   376  H  HB3  . PRO A 1 29  ? -1.67000 28.61800 0.16800   1.000 70.94752  ? 348 PRO A HB3  1 
ATOM   377  H  HG2  . PRO A 1 29  ? 0.84700  27.67100 -0.70400  1.000 68.58223  ? 348 PRO A HG2  1 
ATOM   378  H  HG3  . PRO A 1 29  ? 0.07000  28.89400 -1.27900  1.000 68.58223  ? 348 PRO A HG3  1 
ATOM   379  H  HD2  . PRO A 1 29  ? 1.95500  29.26100 0.44700   1.000 77.16953  ? 348 PRO A HD2  1 
ATOM   380  H  HD3  . PRO A 1 29  ? 0.76400  30.26400 0.37200   1.000 77.16953  ? 348 PRO A HD3  1 
ATOM   381  N  N    . LYS A 1 30  ? -0.80200 25.41300 2.10900   1.000 54.60081  ? 349 LYS A N    1 
ATOM   382  C  CA   . LYS A 1 30  ? -0.32000 24.04900 2.29800   1.000 65.78021  ? 349 LYS A CA   1 
ATOM   383  C  C    . LYS A 1 30  ? 0.30300  23.50400 1.02000   1.000 66.28564  ? 349 LYS A C    1 
ATOM   384  O  O    . LYS A 1 30  ? 1.35100  22.84900 1.06300   1.000 57.28994  ? 349 LYS A O    1 
ATOM   385  C  CB   . LYS A 1 30  ? -1.46200 23.14800 2.76600   1.000 61.79450  ? 349 LYS A CB   1 
ATOM   386  C  CG   . LYS A 1 30  ? -1.97700 23.46400 4.18300   1.000 97.58767  ? 349 LYS A CG   1 
ATOM   387  C  CD   . LYS A 1 30  ? -0.88600 23.29200 5.24900   1.000 107.29491 ? 349 LYS A CD   1 
ATOM   388  C  CE   . LYS A 1 30  ? -1.39600 23.66100 6.64000   1.000 141.22036 ? 349 LYS A CE   1 
ATOM   389  N  NZ   . LYS A 1 30  ? -0.35600 23.50100 7.70300   1.000 98.02292  ? 349 LYS A NZ   1 
ATOM   390  H  H    . LYS A 1 30  ? -1.65800 25.49800 2.09400   1.000 65.62001  ? 349 LYS A H    1 
ATOM   391  H  HA   . LYS A 1 30  ? 0.36900  24.06200 2.98100   1.000 79.03528  ? 349 LYS A HA   1 
ATOM   392  H  HB2  . LYS A 1 30  ? -2.19900 23.22600 2.14000   1.000 74.25243  ? 349 LYS A HB2  1 
ATOM   393  H  HB3  . LYS A 1 30  ? -1.16400 22.22500 2.74000   1.000 74.25243  ? 349 LYS A HB3  1 
ATOM   394  H  HG2  . LYS A 1 30  ? -2.31100 24.37400 4.20800   1.000 117.20424 ? 349 LYS A HG2  1 
ATOM   395  H  HG3  . LYS A 1 30  ? -2.72500 22.88200 4.39100   1.000 117.20424 ? 349 LYS A HG3  1 
ATOM   396  H  HD2  . LYS A 1 30  ? -0.57600 22.37300 5.25100   1.000 128.85292 ? 349 LYS A HD2  1 
ATOM   397  H  HD3  . LYS A 1 30  ? -0.12300 23.84800 5.02500   1.000 128.85292 ? 349 LYS A HD3  1 
ATOM   398  H  HE2  . LYS A 1 30  ? -1.70500 24.58000 6.63300   1.000 169.56347 ? 349 LYS A HE2  1 
ATOM   399  H  HE3  . LYS A 1 30  ? -2.16100 23.10600 6.85700   1.000 169.56347 ? 349 LYS A HE3  1 
ATOM   400  H  HZ1  . LYS A 1 30  ? -0.45100 24.14400 8.31100   1.000 117.72654 ? 349 LYS A HZ1  1 
ATOM   401  H  HZ2  . LYS A 1 30  ? -0.45100 22.70700 8.09400   1.000 117.72654 ? 349 LYS A HZ2  1 
ATOM   402  H  HZ3  . LYS A 1 30  ? 0.45400  23.55600 7.33700   1.000 117.72654 ? 349 LYS A HZ3  1 
ATOM   403  N  N    . GLU A 1 31  ? -0.32500 23.76200 -0.12500  1.000 48.76886  ? 350 GLU A N    1 
ATOM   404  C  CA   . GLU A 1 31  ? 0.18200  23.33800 -1.42000  1.000 48.37624  ? 350 GLU A CA   1 
ATOM   405  C  C    . GLU A 1 31  ? 0.13400  24.51000 -2.38900  1.000 48.44106  ? 350 GLU A C    1 
ATOM   406  O  O    . GLU A 1 31  ? -0.52200 25.52600 -2.14200  1.000 53.16571  ? 350 GLU A O    1 
ATOM   407  C  CB   . GLU A 1 31  ? -0.62100 22.15900 -1.98600  1.000 55.56142  ? 350 GLU A CB   1 
ATOM   408  C  CG   . GLU A 1 31  ? -0.74900 20.98500 -1.04300  1.000 95.06174  ? 350 GLU A CG   1 
ATOM   409  C  CD   . GLU A 1 31  ? -1.34500 19.75700 -1.70500  1.000 113.57273 ? 350 GLU A CD   1 
ATOM   410  O  OE1  . GLU A 1 31  ? -1.85800 19.87800 -2.84200  1.000 146.09592 ? 350 GLU A OE1  1 
ATOM   411  O  OE2  . GLU A 1 31  ? -1.29400 18.66900 -1.08500  1.000 107.34226 ? 350 GLU A OE2  1 
ATOM   412  H  H    . GLU A 1 31  ? -1.06700 24.19400 -0.16800  1.000 58.62166  ? 350 GLU A H    1 
ATOM   413  H  HA   . GLU A 1 31  ? 1.09800  23.04000 -1.30300  1.000 58.15052  ? 350 GLU A HA   1 
ATOM   414  H  HB2  . GLU A 1 31  ? -1.50900 22.47000 -2.22200  1.000 66.77273  ? 350 GLU A HB2  1 
ATOM   415  H  HB3  . GLU A 1 31  ? -0.19900 21.85800 -2.80600  1.000 66.77273  ? 350 GLU A HB3  1 
ATOM   416  H  HG2  . GLU A 1 31  ? 0.12700  20.76300 -0.69000  1.000 114.17312 ? 350 GLU A HG2  1 
ATOM   417  H  HG3  . GLU A 1 31  ? -1.30300 21.24100 -0.28900  1.000 114.17312 ? 350 GLU A HG3  1 
ATOM   418  N  N    . TYR A 1 32  ? 0.83800  24.35700 -3.50700  1.000 44.72159  ? 351 TYR A N    1 
ATOM   419  C  CA   . TYR A 1 32  ? 0.79500  25.35700 -4.56300  1.000 45.49179  ? 351 TYR A CA   1 
ATOM   420  C  C    . TYR A 1 32  ? 1.15200  24.69600 -5.88300  1.000 49.81606  ? 351 TYR A C    1 
ATOM   421  O  O    . TYR A 1 32  ? 1.74900  23.61800 -5.92000  1.000 42.32738  ? 351 TYR A O    1 
ATOM   422  C  CB   . TYR A 1 32  ? 1.73300  26.53300 -4.27200  1.000 40.51581  ? 351 TYR A CB   1 
ATOM   423  C  CG   . TYR A 1 32  ? 3.16800  26.33700 -4.70100  1.000 48.78649  ? 351 TYR A CG   1 
ATOM   424  C  CD1  . TYR A 1 32  ? 4.00800  25.47600 -4.01000  1.000 51.56504  ? 351 TYR A CD1  1 
ATOM   425  C  CD2  . TYR A 1 32  ? 3.68700  27.02500 -5.79200  1.000 43.73461  ? 351 TYR A CD2  1 
ATOM   426  C  CE1  . TYR A 1 32  ? 5.32200  25.29900 -4.39500  1.000 51.71888  ? 351 TYR A CE1  1 
ATOM   427  C  CE2  . TYR A 1 32  ? 5.00000  26.85600 -6.18200  1.000 38.53094  ? 351 TYR A CE2  1 
ATOM   428  C  CZ   . TYR A 1 32  ? 5.81300  25.99100 -5.47900  1.000 43.56548  ? 351 TYR A CZ   1 
ATOM   429  O  OH   . TYR A 1 32  ? 7.12200  25.81400 -5.86200  1.000 46.09571  ? 351 TYR A OH   1 
ATOM   430  H  H    . TYR A 1 32  ? 1.34500  23.68200 -3.67100  1.000 53.76494  ? 351 TYR A H    1 
ATOM   431  H  HA   . TYR A 1 32  ? -0.10300 25.72100 -4.61100  1.000 54.68918  ? 351 TYR A HA   1 
ATOM   432  H  HB2  . TYR A 1 32  ? 1.38400  27.32300 -4.71400  1.000 48.70533  ? 351 TYR A HB2  1 
ATOM   433  H  HB3  . TYR A 1 32  ? 1.71800  26.71100 -3.31900  1.000 48.70533  ? 351 TYR A HB3  1 
ATOM   434  H  HD1  . TYR A 1 32  ? 3.68000  25.01000 -3.27500  1.000 61.97708  ? 351 TYR A HD1  1 
ATOM   435  H  HD2  . TYR A 1 32  ? 3.14000  27.60900 -6.26700  1.000 52.58057  ? 351 TYR A HD2  1 
ATOM   436  H  HE1  . TYR A 1 32  ? 5.87200  24.71500 -3.92500  1.000 62.16169  ? 351 TYR A HE1  1 
ATOM   437  H  HE2  . TYR A 1 32  ? 5.33500  27.32200 -6.91400  1.000 46.33616  ? 351 TYR A HE2  1 
ATOM   438  H  HH   . TYR A 1 32  ? 7.58800  25.62800 -5.18900  1.000 55.41388  ? 351 TYR A HH   1 
ATOM   439  N  N    . GLU A 1 33  ? 0.76900  25.36300 -6.96700  1.000 43.65548  ? 352 GLU A N    1 
ATOM   440  C  CA   . GLU A 1 33  ? 1.00700  24.86500 -8.31800  1.000 40.38146  ? 352 GLU A CA   1 
ATOM   441  C  C    . GLU A 1 33  ? 2.36100  25.38300 -8.78600  1.000 38.27614  ? 352 GLU A C    1 
ATOM   442  O  O    . GLU A 1 33  ? 2.48700  26.53300 -9.21200  1.000 49.98522  ? 352 GLU A O    1 
ATOM   443  C  CB   . GLU A 1 33  ? -0.11600 25.30000 -9.25100  1.000 46.48141  ? 352 GLU A CB   1 
ATOM   444  C  CG   . GLU A 1 33  ? 0.08100  24.87500 -10.69200 1.000 58.58521  ? 352 GLU A CG   1 
ATOM   445  C  CD   . GLU A 1 33  ? 0.06300  23.37200 -10.86500 1.000 63.14022  ? 352 GLU A CD   1 
ATOM   446  O  OE1  . GLU A 1 33  ? -0.90300 22.73100 -10.40000 1.000 85.55592  ? 352 GLU A OE1  1 
ATOM   447  O  OE2  . GLU A 1 33  ? 1.02000  22.83200 -11.45700 1.000 58.29976  ? 352 GLU A OE2  1 
ATOM   448  H  H    . GLU A 1 33  ? 0.36200  26.12000 -6.94000  1.000 52.48560  ? 352 GLU A H    1 
ATOM   449  H  HA   . GLU A 1 33  ? 1.01800  23.89500 -8.32400  1.000 47.96260  ? 352 GLU A HA   1 
ATOM   450  H  HB2  . GLU A 1 33  ? -0.95400 24.93300 -8.92700  1.000 55.87673  ? 352 GLU A HB2  1 
ATOM   451  H  HB3  . GLU A 1 33  ? -0.19700 26.26600 -9.21600  1.000 55.87673  ? 352 GLU A HB3  1 
ATOM   452  H  HG2  . GLU A 1 33  ? -0.61700 25.26800 -11.24000 1.000 70.40129  ? 352 GLU A HG2  1 
ATOM   453  H  HG3  . GLU A 1 33  ? 0.92600  25.22400 -11.01600 1.000 70.40129  ? 352 GLU A HG3  1 
ATOM   454  N  N    . ALA A 1 34  ? 3.38000  24.53100 -8.70100  1.000 37.21506  ? 353 ALA A N    1 
ATOM   455  C  CA   . ALA A 1 34  ? 4.72100  24.90100 -9.13400  1.000 39.82739  ? 353 ALA A CA   1 
ATOM   456  C  C    . ALA A 1 34  ? 4.94200  24.68100 -10.61900 1.000 46.47049  ? 353 ALA A C    1 
ATOM   457  O  O    . ALA A 1 34  ? 5.77300  25.37300 -11.22000 1.000 39.08032  ? 353 ALA A O    1 
ATOM   458  C  CB   . ALA A 1 34  ? 5.77100  24.10600 -8.35700  1.000 36.11471  ? 353 ALA A CB   1 
ATOM   459  H  H    . ALA A 1 34  ? 3.31300  23.73100 -8.39400  1.000 44.16292  ? 353 ALA A H    1 
ATOM   460  H  HA   . ALA A 1 34  ? 4.81200  25.85000 -8.95500  1.000 47.89189  ? 353 ALA A HA   1 
ATOM   461  H  HB1  . ALA A 1 34  ? 6.65800  24.36200 -8.65500  1.000 43.43668  ? 353 ALA A HB1  1 
ATOM   462  H  HB2  . ALA A 1 34  ? 5.68300  24.29300 -7.40900  1.000 43.43668  ? 353 ALA A HB2  1 
ATOM   463  H  HB3  . ALA A 1 34  ? 5.64000  23.15800 -8.51300  1.000 43.43668  ? 353 ALA A HB3  1 
ATOM   464  N  N    . TYR A 1 35  ? 4.23100  23.72000 -11.21200 1.000 41.53058  ? 354 TYR A N    1 
ATOM   465  C  CA   . TYR A 1 35  ? 4.41800  23.32400 -12.62500 1.000 37.12300  ? 354 TYR A CA   1 
ATOM   466  C  C    . TYR A 1 35  ? 5.79300  22.68900 -12.81900 1.000 38.81060  ? 354 TYR A C    1 
ATOM   467  O  O    . TYR A 1 35  ? 6.66600  22.80100 -11.95900 1.000 40.43420  ? 354 TYR A O    1 
ATOM   468  C  CB   . TYR A 1 35  ? 4.22500  24.47800 -13.61200 1.000 40.16220  ? 354 TYR A CB   1 
ATOM   469  C  CG   . TYR A 1 35  ? 2.86800  25.12800 -13.62900 1.000 41.29857  ? 354 TYR A CG   1 
ATOM   470  C  CD1  . TYR A 1 35  ? 1.78700  24.50600 -14.22500 1.000 51.42605  ? 354 TYR A CD1  1 
ATOM   471  C  CD2  . TYR A 1 35  ? 2.67700  26.38400 -13.08200 1.000 63.56486  ? 354 TYR A CD2  1 
ATOM   472  C  CE1  . TYR A 1 35  ? 0.54200  25.10700 -14.25700 1.000 53.22455  ? 354 TYR A CE1  1 
ATOM   473  C  CE2  . TYR A 1 35  ? 1.44000  27.00000 -13.10700 1.000 54.76656  ? 354 TYR A CE2  1 
ATOM   474  C  CZ   . TYR A 1 35  ? 0.36900  26.35800 -13.69700 1.000 51.28588  ? 354 TYR A CZ   1 
ATOM   475  O  OH   . TYR A 1 35  ? -0.86200 26.95800 -13.72100 1.000 76.92715  ? 354 TYR A OH   1 
ATOM   476  H  H    . TYR A 1 35  ? 3.61900  23.27100 -10.80700 1.000 49.93573  ? 354 TYR A H    1 
ATOM   477  H  HA   . TYR A 1 35  ? 3.72400  22.67500 -12.82100 1.000 44.64663  ? 354 TYR A HA   1 
ATOM   478  H  HB2  . TYR A 1 35  ? 4.88600  25.16000 -13.41400 1.000 48.29367  ? 354 TYR A HB2  1 
ATOM   479  H  HB3  . TYR A 1 35  ? 4.41500  24.14900 -14.50400 1.000 48.29367  ? 354 TYR A HB3  1 
ATOM   480  H  HD1  . TYR A 1 35  ? 1.89900  23.66800 -14.61200 1.000 61.81029  ? 354 TYR A HD1  1 
ATOM   481  H  HD2  . TYR A 1 35  ? 3.39600  26.82300 -12.68900 1.000 76.37686  ? 354 TYR A HD2  1 
ATOM   482  H  HE1  . TYR A 1 35  ? -0.17700 24.67000 -14.65400 1.000 63.96849  ? 354 TYR A HE1  1 
ATOM   483  H  HE2  . TYR A 1 35  ? 1.32900  27.84200 -12.72900 1.000 65.81890  ? 354 TYR A HE2  1 
ATOM   484  H  HH   . TYR A 1 35  ? -0.81600 27.70800 -13.34600 1.000 92.41161  ? 354 TYR A HH   1 
ATOM   485  N  N    . GLU A 1 36  ? 5.93600  21.95200 -13.89800 1.000 39.57003  ? 355 GLU A N    1 
ATOM   486  C  CA   . GLU A 1 36  ? 7.22400  21.40000 -14.29700 1.000 35.50341  ? 355 GLU A CA   1 
ATOM   487  C  C    . GLU A 1 36  ? 7.30900  21.42200 -15.81300 1.000 39.81108  ? 355 GLU A C    1 
ATOM   488  O  O    . GLU A 1 36  ? 6.29600  21.53900 -16.50700 1.000 46.81186  ? 355 GLU A O    1 
ATOM   489  C  CB   . GLU A 1 36  ? 7.41600  19.96700 -13.81900 1.000 35.97774  ? 355 GLU A CB   1 
ATOM   490  C  CG   . GLU A 1 36  ? 6.28700  19.07100 -14.23500 1.000 43.56583  ? 355 GLU A CG   1 
ATOM   491  C  CD   . GLU A 1 36  ? 6.52500  17.63100 -13.86100 1.000 53.68025  ? 355 GLU A CD   1 
ATOM   492  O  OE1  . GLU A 1 36  ? 7.68700  17.28500 -13.55200 1.000 74.79498  ? 355 GLU A OE1  1 
ATOM   493  O  OE2  . GLU A 1 36  ? 5.55200  16.84300 -13.87500 1.000 93.97554  ? 355 GLU A OE2  1 
ATOM   494  H  H    . GLU A 1 36  ? 5.28900  21.75200 -14.42800 1.000 47.58306  ? 355 GLU A H    1 
ATOM   495  H  HA   . GLU A 1 36  ? 7.91800  21.94200 -13.89100 1.000 42.70312  ? 355 GLU A HA   1 
ATOM   496  H  HB2  . GLU A 1 36  ? 8.24900  19.61900 -14.17300 1.000 43.27232  ? 355 GLU A HB2  1 
ATOM   497  H  HB3  . GLU A 1 36  ? 7.49300  19.95900 -12.85200 1.000 43.27232  ? 355 GLU A HB3  1 
ATOM   498  H  HG2  . GLU A 1 36  ? 5.46500  19.37800 -13.82100 1.000 52.37803  ? 355 GLU A HG2  1 
ATOM   499  H  HG3  . GLU A 1 36  ? 6.16300  19.13600 -15.19500 1.000 52.37803  ? 355 GLU A HG3  1 
ATOM   500  N  N    . CYS A 1 37  ? 8.52400  21.29500 -16.32500 1.000 39.01661  ? 356 CYS A N    1 
ATOM   501  C  CA   . CYS A 1 37  ? 8.74500  21.23000 -17.76100 1.000 41.31160  ? 356 CYS A CA   1 
ATOM   502  C  C    . CYS A 1 37  ? 9.04400  19.78900 -18.13000 1.000 45.07214  ? 356 CYS A C    1 
ATOM   503  O  O    . CYS A 1 37  ? 9.96200  19.18300 -17.57300 1.000 50.93244  ? 356 CYS A O    1 
ATOM   504  C  CB   . CYS A 1 37  ? 9.87400  22.15600 -18.18700 1.000 35.59969  ? 356 CYS A CB   1 
ATOM   505  S  SG   . CYS A 1 37  ? 9.48600  23.85200 -17.83300 1.000 45.22325  ? 356 CYS A SG   1 
ATOM   506  H  H    . CYS A 1 37  ? 9.24100  21.24400 -15.85300 1.000 46.91897  ? 356 CYS A H    1 
ATOM   507  H  HA   . CYS A 1 37  ? 7.95000  21.52900 -18.23000 1.000 49.67295  ? 356 CYS A HA   1 
ATOM   508  H  HB2  . CYS A 1 37  ? 10.69100 21.90600 -17.72700 1.000 42.81866  ? 356 CYS A HB2  1 
ATOM   509  H  HB3  . CYS A 1 37  ? 10.04000 22.05100 -19.13700 1.000 42.81866  ? 356 CYS A HB3  1 
ATOM   510  N  N    . LYS A 1 38  ? 8.24400  19.24100 -19.04600 1.000 40.88949  ? 357 LYS A N    1 
ATOM   511  C  CA   . LYS A 1 38  ? 8.32500  17.84700 -19.45900 1.000 51.39482  ? 357 LYS A CA   1 
ATOM   512  C  C    . LYS A 1 38  ? 8.25400  17.75800 -20.98000 1.000 51.30462  ? 357 LYS A C    1 
ATOM   513  O  O    . LYS A 1 38  ? 7.54600  18.53200 -21.62900 1.000 41.65535  ? 357 LYS A O    1 
ATOM   514  C  CB   . LYS A 1 38  ? 7.17800  17.06300 -18.81300 1.000 47.27522  ? 357 LYS A CB   1 
ATOM   515  C  CG   . LYS A 1 38  ? 7.17000  15.58400 -19.04000 1.000 108.12253 ? 357 LYS A CG   1 
ATOM   516  C  CD   . LYS A 1 38  ? 5.98400  14.97400 -18.31600 1.000 91.17748  ? 357 LYS A CD   1 
ATOM   517  C  CE   . LYS A 1 38  ? 6.18400  15.05200 -16.82300 1.000 84.67248  ? 357 LYS A CE   1 
ATOM   518  N  NZ   . LYS A 1 38  ? 7.44700  14.36200 -16.43000 1.000 152.44824 ? 357 LYS A NZ   1 
ATOM   519  H  H    . LYS A 1 38  ? 7.62700  19.68200 -19.45100 1.000 49.16642  ? 357 LYS A H    1 
ATOM   520  H  HA   . LYS A 1 38  ? 9.16800  17.46300 -19.17000 1.000 61.77281  ? 357 LYS A HA   1 
ATOM   521  H  HB2  . LYS A 1 38  ? 7.20100  17.22300 -17.85700 1.000 56.82929  ? 357 LYS A HB2  1 
ATOM   522  H  HB3  . LYS A 1 38  ? 6.34000  17.42500 -19.14100 1.000 56.82929  ? 357 LYS A HB3  1 
ATOM   523  H  HG2  . LYS A 1 38  ? 7.11700  15.39200 -19.98900 1.000 129.84607 ? 357 LYS A HG2  1 
ATOM   524  H  HG3  . LYS A 1 38  ? 7.99600  15.19200 -18.71700 1.000 129.84607 ? 357 LYS A HG3  1 
ATOM   525  H  HD2  . LYS A 1 38  ? 5.17100  15.44100 -18.56400 1.000 109.51201 ? 357 LYS A HD2  1 
ATOM   526  H  HD3  . LYS A 1 38  ? 5.87400  14.04900 -18.58600 1.000 109.51201 ? 357 LYS A HD3  1 
ATOM   527  H  HE2  . LYS A 1 38  ? 6.21500  15.98000 -16.54300 1.000 101.70601 ? 357 LYS A HE2  1 
ATOM   528  H  HE3  . LYS A 1 38  ? 5.43100  14.64400 -16.36800 1.000 101.70601 ? 357 LYS A HE3  1 
ATOM   529  H  HZ1  . LYS A 1 38  ? 7.38200  14.08100 -15.58800 1.000 183.03692 ? 357 LYS A HZ1  1 
ATOM   530  H  HZ2  . LYS A 1 38  ? 7.58400  13.66400 -16.96600 1.000 183.03692 ? 357 LYS A HZ2  1 
ATOM   531  H  HZ3  . LYS A 1 38  ? 8.13000  14.92800 -16.50200 1.000 183.03692 ? 357 LYS A HZ3  1 
ATOM   532  N  N    . GLY A 1 39  ? 8.98500  16.81100 -21.55000 1.000 49.07266  ? 358 GLY A N    1 
ATOM   533  C  CA   . GLY A 1 39  ? 8.93100  16.59400 -22.97800 1.000 52.18403  ? 358 GLY A CA   1 
ATOM   534  C  C    . GLY A 1 39  ? 10.31100 16.52500 -23.57900 1.000 55.36239  ? 358 GLY A C    1 
ATOM   535  O  O    . GLY A 1 39  ? 11.32600 16.70500 -22.90900 1.000 57.45924  ? 358 GLY A O    1 
ATOM   536  H  H    . GLY A 1 39  ? 9.51700  16.28600 -21.12500 1.000 58.98622  ? 358 GLY A H    1 
ATOM   537  H  HA2  . GLY A 1 39  ? 8.45500  15.77000 -23.16300 1.000 62.71986  ? 358 GLY A HA2  1 
ATOM   538  H  HA3  . GLY A 1 39  ? 8.43000  17.31100 -23.39700 1.000 62.71986  ? 358 GLY A HA3  1 
ATOM   539  N  N    . GLY A 1 40  ? 10.34000 16.22100 -24.87300 1.000 56.02529  ? 359 GLY A N    1 
ATOM   540  C  CA   . GLY A 1 40  ? 11.59000 15.96600 -25.54800 1.000 69.24647  ? 359 GLY A CA   1 
ATOM   541  C  C    . GLY A 1 40  ? 12.15500 17.18300 -26.25200 1.000 52.44275  ? 359 GLY A C    1 
ATOM   542  O  O    . GLY A 1 40  ? 11.45000 18.14300 -26.55800 1.000 47.36103  ? 359 GLY A O    1 
ATOM   543  H  H    . GLY A 1 40  ? 9.64200  16.15900 -25.37200 1.000 67.32938  ? 359 GLY A H    1 
ATOM   544  H  HA2  . GLY A 1 40  ? 12.23800 15.64400 -24.90200 1.000 83.19479  ? 359 GLY A HA2  1 
ATOM   545  H  HA3  . GLY A 1 40  ? 11.46000 15.25700 -26.19700 1.000 83.19479  ? 359 GLY A HA3  1 
ATOM   546  N  N    . CYS A 1 41  ? 13.45900 17.12500 -26.50100 1.000 48.23328  ? 360 CYS A N    1 
ATOM   547  C  CA   . CYS A 1 41  ? 14.19000 18.14700 -27.24500 1.000 48.49568  ? 360 CYS A CA   1 
ATOM   548  C  C    . CYS A 1 41  ? 14.76000 17.45800 -28.47900 1.000 44.05130  ? 360 CYS A C    1 
ATOM   549  O  O    . CYS A 1 41  ? 15.89500 16.97500 -28.47100 1.000 73.25087  ? 360 CYS A O    1 
ATOM   550  C  CB   . CYS A 1 41  ? 15.26900 18.78100 -26.38500 1.000 44.82268  ? 360 CYS A CB   1 
ATOM   551  S  SG   . CYS A 1 41  ? 14.59500 19.65100 -24.95700 1.000 47.15588  ? 360 CYS A SG   1 
ATOM   552  H  H    . CYS A 1 41  ? 13.95600 16.47500 -26.23600 1.000 57.97897  ? 360 CYS A H    1 
ATOM   553  H  HA   . CYS A 1 41  ? 13.60900 18.87700 -27.51000 1.000 58.29384  ? 360 CYS A HA   1 
ATOM   554  H  HB2  . CYS A 1 41  ? 15.88100 18.09300 -26.08100 1.000 53.88625  ? 360 CYS A HB2  1 
ATOM   555  H  HB3  . CYS A 1 41  ? 15.78400 19.40100 -26.92400 1.000 53.88625  ? 360 CYS A HB3  1 
ATOM   556  N  N    . PHE A 1 42  ? 13.95900 17.41400 -29.53900 1.000 39.42859  ? 361 PHE A N    1 
ATOM   557  C  CA   . PHE A 1 42  ? 14.26900 16.62500 -30.71900 1.000 51.08495  ? 361 PHE A CA   1 
ATOM   558  C  C    . PHE A 1 42  ? 13.82400 17.37800 -31.96400 1.000 45.62819  ? 361 PHE A C    1 
ATOM   559  O  O    . PHE A 1 42  ? 12.90600 18.20000 -31.91500 1.000 47.78857  ? 361 PHE A O    1 
ATOM   560  C  CB   . PHE A 1 42  ? 13.60300 15.24500 -30.65100 1.000 62.64891  ? 361 PHE A CB   1 
ATOM   561  C  CG   . PHE A 1 42  ? 12.09900 15.29300 -30.64100 1.000 80.50985  ? 361 PHE A CG   1 
ATOM   562  C  CD1  . PHE A 1 42  ? 11.40600 15.53500 -29.46400 1.000 79.44593  ? 361 PHE A CD1  1 
ATOM   563  C  CD2  . PHE A 1 42  ? 11.38000 15.09300 -31.81100 1.000 91.51330  ? 361 PHE A CD2  1 
ATOM   564  C  CE1  . PHE A 1 42  ? 10.02400 15.58200 -29.44900 1.000 71.80393  ? 361 PHE A CE1  1 
ATOM   565  C  CE2  . PHE A 1 42  ? 9.99600  15.13700 -31.80200 1.000 99.32689  ? 361 PHE A CE2  1 
ATOM   566  C  CZ   . PHE A 1 42  ? 9.31900  15.38100 -30.61500 1.000 114.54870 ? 361 PHE A CZ   1 
ATOM   567  H  H    . PHE A 1 42  ? 13.21600 17.84500 -29.59100 1.000 47.41334  ? 361 PHE A H    1 
ATOM   568  H  HA   . PHE A 1 42  ? 15.22800 16.48400 -30.75800 1.000 61.40097  ? 361 PHE A HA   1 
ATOM   569  H  HB2  . PHE A 1 42  ? 13.89600 14.71700 -31.41000 1.000 75.27772  ? 361 PHE A HB2  1 
ATOM   570  H  HB3  . PHE A 1 42  ? 13.90800 14.78700 -29.85200 1.000 75.27772  ? 361 PHE A HB3  1 
ATOM   571  H  HD1  . PHE A 1 42  ? 11.87800 15.66800 -28.67400 1.000 95.43415  ? 361 PHE A HD1  1 
ATOM   572  H  HD2  . PHE A 1 42  ? 11.83100 14.92800 -32.60700 1.000 109.91500 ? 361 PHE A HD2  1 
ATOM   573  H  HE1  . PHE A 1 42  ? 9.57200  15.74900 -28.65400 1.000 86.26375  ? 361 PHE A HE1  1 
ATOM   574  H  HE2  . PHE A 1 42  ? 9.52100  15.00300 -32.59000 1.000 119.29130 ? 361 PHE A HE2  1 
ATOM   575  H  HZ   . PHE A 1 42  ? 8.38900  15.40900 -30.60700 1.000 137.55747 ? 361 PHE A HZ   1 
ATOM   576  N  N    . PHE A 1 43  ? 14.47500 17.07600 -33.08600 1.000 47.97228  ? 362 PHE A N    1 
ATOM   577  C  CA   . PHE A 1 43  ? 14.01800 17.69600 -34.32000 1.000 40.65901  ? 362 PHE A CA   1 
ATOM   578  C  C    . PHE A 1 43  ? 12.92900 16.84900 -34.97200 1.000 47.85810  ? 362 PHE A C    1 
ATOM   579  O  O    . PHE A 1 43  ? 12.95600 15.61700 -34.88500 1.000 50.03336  ? 362 PHE A O    1 
ATOM   580  C  CB   . PHE A 1 43  ? 15.18200 17.87300 -35.29100 1.000 46.67127  ? 362 PHE A CB   1 
ATOM   581  C  CG   . PHE A 1 43  ? 16.24000 18.81800 -34.79900 1.000 38.11872  ? 362 PHE A CG   1 
ATOM   582  C  CD1  . PHE A 1 43  ? 16.04700 20.18800 -34.86400 1.000 50.01615  ? 362 PHE A CD1  1 
ATOM   583  C  CD2  . PHE A 1 43  ? 17.42800 18.33700 -34.27400 1.000 45.40340  ? 362 PHE A CD2  1 
ATOM   584  C  CE1  . PHE A 1 43  ? 17.01700 21.06100 -34.41200 1.000 42.00813  ? 362 PHE A CE1  1 
ATOM   585  C  CE2  . PHE A 1 43  ? 18.40300 19.20600 -33.82100 1.000 49.09840  ? 362 PHE A CE2  1 
ATOM   586  C  CZ   . PHE A 1 43  ? 18.19700 20.57000 -33.89000 1.000 42.05001  ? 362 PHE A CZ   1 
ATOM   587  H  H    . PHE A 1 43  ? 15.14700 16.54400 -33.15300 1.000 57.66576  ? 362 PHE A H    1 
ATOM   588  H  HA   . PHE A 1 43  ? 13.65200 18.56800 -34.10300 1.000 48.88984  ? 362 PHE A HA   1 
ATOM   589  H  HB2  . PHE A 1 43  ? 15.58600 17.00800 -35.46000 1.000 56.10455  ? 362 PHE A HB2  1 
ATOM   590  H  HB3  . PHE A 1 43  ? 14.83900 18.19700 -36.13900 1.000 56.10455  ? 362 PHE A HB3  1 
ATOM   591  H  HD1  . PHE A 1 43  ? 15.25500 20.52400 -35.21600 1.000 60.11841  ? 362 PHE A HD1  1 
ATOM   592  H  HD2  . PHE A 1 43  ? 17.57100 17.41900 -34.22600 1.000 54.58311  ? 362 PHE A HD2  1 
ATOM   593  H  HE1  . PHE A 1 43  ? 16.87500 21.97900 -34.45900 1.000 50.50879  ? 362 PHE A HE1  1 
ATOM   594  H  HE2  . PHE A 1 43  ? 19.19700 18.87200 -33.47000 1.000 59.01711  ? 362 PHE A HE2  1 
ATOM   595  H  HZ   . PHE A 1 43  ? 18.85200 21.15600 -33.58600 1.000 50.55904  ? 362 PHE A HZ   1 
ATOM   596  N  N    . PRO A 1 44  ? 11.94700 17.48000 -35.63200 1.000 39.58985  ? 363 PRO A N    1 
ATOM   597  C  CA   . PRO A 1 44  ? 11.77400 18.92700 -35.83500 1.000 51.12233  ? 363 PRO A CA   1 
ATOM   598  C  C    . PRO A 1 44  ? 11.23100 19.63000 -34.59500 1.000 64.88170  ? 363 PRO A C    1 
ATOM   599  O  O    . PRO A 1 44  ? 10.53800 19.02500 -33.78200 1.000 55.15534  ? 363 PRO A O    1 
ATOM   600  C  CB   . PRO A 1 44  ? 10.78300 18.98400 -37.00300 1.000 46.16791  ? 363 PRO A CB   1 
ATOM   601  C  CG   . PRO A 1 44  ? 9.92600  17.77000 -36.79800 1.000 53.37159  ? 363 PRO A CG   1 
ATOM   602  C  CD   . PRO A 1 44  ? 10.86800 16.70900 -36.27700 1.000 48.94744  ? 363 PRO A CD   1 
ATOM   603  H  HA   . PRO A 1 44  ? 12.61000 19.38600 -36.01300 1.000 61.44583  ? 363 PRO A HA   1 
ATOM   604  H  HB2  . PRO A 1 44  ? 10.25700 19.79900 -36.98500 1.000 55.50053  ? 363 PRO A HB2  1 
ATOM   605  H  HB3  . PRO A 1 44  ? 11.23900 18.95900 -37.85900 1.000 55.50053  ? 363 PRO A HB3  1 
ATOM   606  H  HG2  . PRO A 1 44  ? 9.21200  17.94700 -36.16600 1.000 64.14494  ? 363 PRO A HG2  1 
ATOM   607  H  HG3  . PRO A 1 44  ? 9.50800  17.49100 -37.62800 1.000 64.14494  ? 363 PRO A HG3  1 
ATOM   608  H  HD2  . PRO A 1 44  ? 10.42600 16.12000 -35.64600 1.000 58.83595  ? 363 PRO A HD2  1 
ATOM   609  H  HD3  . PRO A 1 44  ? 11.20900 16.15200 -36.99500 1.000 58.83595  ? 363 PRO A HD3  1 
ATOM   610  N  N    . LEU A 1 45  ? 11.53500 20.91300 -34.42800 1.000 56.50443  ? 364 LEU A N    1 
ATOM   611  C  CA   . LEU A 1 45  ? 11.08000 21.69600 -33.24500 1.000 106.56496 ? 364 LEU A CA   1 
ATOM   612  C  C    . LEU A 1 45  ? 9.78200  22.47100 -33.53600 1.000 102.58298 ? 364 LEU A C    1 
ATOM   613  O  O    . LEU A 1 45  ? 9.61100  22.91100 -34.68400 1.000 82.69657  ? 364 LEU A O    1 
ATOM   614  C  CB   . LEU A 1 45  ? 12.21000 22.64500 -32.84800 1.000 59.19354  ? 364 LEU A CB   1 
ATOM   615  C  CG   . LEU A 1 45  ? 13.46900 21.96600 -32.31000 1.000 81.99768  ? 364 LEU A CG   1 
ATOM   616  C  CD1  . LEU A 1 45  ? 14.58100 22.97800 -32.10000 1.000 75.46373  ? 364 LEU A CD1  1 
ATOM   617  C  CD2  . LEU A 1 45  ? 13.18000 21.22500 -31.01600 1.000 91.43431  ? 364 LEU A CD2  1 
ATOM   618  H  H    . LEU A 1 45  ? 12.00800 21.36500 -34.98600 1.000 67.90435  ? 364 LEU A H    1 
ATOM   619  H  HA   . LEU A 1 45  ? 10.87600 21.09100 -32.51500 1.000 127.97698 ? 364 LEU A HA   1 
ATOM   620  H  HB2  . LEU A 1 45  ? 12.45200 23.17800 -33.62100 1.000 71.13129  ? 364 LEU A HB2  1 
ATOM   621  H  HB3  . LEU A 1 45  ? 11.87700 23.25800 -32.17400 1.000 71.13129  ? 364 LEU A HB3  1 
ATOM   622  H  HG   . LEU A 1 45  ? 13.76100 21.32000 -32.97200 1.000 98.49625  ? 364 LEU A HG   1 
ATOM   623  H  HD11 . LEU A 1 45  ? 15.36900 22.52700 -31.75900 1.000 90.65551  ? 364 LEU A HD11 1 
ATOM   624  H  HD12 . LEU A 1 45  ? 14.79400 23.40500 -32.94400 1.000 90.65551  ? 364 LEU A HD12 1 
ATOM   625  H  HD13 . LEU A 1 45  ? 14.29200 23.64900 -31.46200 1.000 90.65551  ? 364 LEU A HD13 1 
ATOM   626  H  HD21 . LEU A 1 45  ? 13.99300 20.80400 -30.69600 1.000 109.82020 ? 364 LEU A HD21 1 
ATOM   627  H  HD22 . LEU A 1 45  ? 12.85700 21.85100 -30.35000 1.000 109.82020 ? 364 LEU A HD22 1 
ATOM   628  H  HD23 . LEU A 1 45  ? 12.50600 20.54600 -31.17500 1.000 109.82020 ? 364 LEU A HD23 1 
ATOM   629  N  N    . ALA A 1 46  ? 8.91300  22.64400 -32.53000 1.000 104.46134 ? 365 ALA A N    1 
ATOM   630  C  CA   . ALA A 1 46  ? 7.63600  23.39100 -32.68400 1.000 140.42626 ? 365 ALA A CA   1 
ATOM   631  C  C    . ALA A 1 46  ? 7.95500  24.87500 -32.88300 1.000 61.31709  ? 365 ALA A C    1 
ATOM   632  O  O    . ALA A 1 46  ? 8.90900  25.34800 -32.23200 1.000 101.23729 ? 365 ALA A O    1 
ATOM   633  C  CB   . ALA A 1 46  ? 6.81000  23.18800 -31.45100 1.000 94.42173  ? 365 ALA A CB   1 
ATOM   634  H  H    . ALA A 1 46  ? 9.04100  22.33500 -31.73800 1.000 125.45264 ? 365 ALA A H    1 
ATOM   635  H  HA   . ALA A 1 46  ? 7.13900  23.07100 -33.45300 1.000 168.61054 ? 365 ALA A HA   1 
ATOM   636  H  HB1  . ALA A 1 46  ? 5.97300  23.67100 -31.53900 1.000 113.40511 ? 365 ALA A HB1  1 
ATOM   637  H  HB2  . ALA A 1 46  ? 6.62700  22.24200 -31.33600 1.000 113.40511 ? 365 ALA A HB2  1 
ATOM   638  H  HB3  . ALA A 1 46  ? 7.29400  23.51900 -30.67900 1.000 113.40511 ? 365 ALA A HB3  1 
ATOM   639  N  N    . ASP A 1 47  ? 7.20400  25.56800 -33.74600 1.000 131.60456 ? 366 ASP A N    1 
ATOM   640  C  CA   . ASP A 1 47  ? 7.43700  27.01200 -34.05900 1.000 137.51345 ? 366 ASP A CA   1 
ATOM   641  C  C    . ASP A 1 47  ? 6.85900  27.99000 -33.02400 1.000 122.32074 ? 366 ASP A C    1 
ATOM   642  O  O    . ASP A 1 47  ? 6.91000  29.19900 -33.29300 1.000 115.57628 ? 366 ASP A O    1 
ATOM   643  C  CB   . ASP A 1 47  ? 6.83900  27.37800 -35.41600 1.000 155.76079 ? 366 ASP A CB   1 
ATOM   644  C  CG   . ASP A 1 47  ? 5.33600  27.17000 -35.47200 1.000 175.13673 ? 366 ASP A CG   1 
ATOM   645  O  OD1  . ASP A 1 47  ? 4.77600  26.66700 -34.47700 1.000 177.49753 ? 366 ASP A OD1  1 
ATOM   646  O  OD2  . ASP A 1 47  ? 4.74000  27.50600 -36.51400 1.000 184.34791 ? 366 ASP A OD2  1 
ATOM   647  H  H    . ASP A 1 47  ? 6.54100  25.22500 -34.17300 1.000 158.02450 ? 366 ASP A H    1 
ATOM   648  H  HA   . ASP A 1 47  ? 8.40200  27.10500 -34.05300 1.000 165.11517 ? 366 ASP A HA   1 
ATOM   649  H  HB2  . ASP A 1 47  ? 7.04000  28.30600 -35.61400 1.000 187.01198 ? 366 ASP A HB2  1 
ATOM   650  H  HB3  . ASP A 1 47  ? 7.26100  26.84300 -36.10600 1.000 187.01198 ? 366 ASP A HB3  1 
ATOM   651  N  N    . ASP A 1 48  ? 6.30600  27.51500 -31.91300 1.000 144.94178 ? 367 ASP A N    1 
ATOM   652  C  CA   . ASP A 1 48  ? 5.83600  28.39000 -30.84600 1.000 150.61439 ? 367 ASP A CA   1 
ATOM   653  C  C    . ASP A 1 48  ? 6.77400  28.38600 -29.64200 1.000 154.04548 ? 367 ASP A C    1 
ATOM   654  O  O    . ASP A 1 48  ? 6.33700  28.63600 -28.51300 1.000 158.88075 ? 367 ASP A O    1 
ATOM   655  C  CB   . ASP A 1 48  ? 4.42100  27.99700 -30.42100 1.000 181.18037 ? 367 ASP A CB   1 
ATOM   656  C  CG   . ASP A 1 48  ? 4.32900  26.55500 -29.96300 1.000 186.55177 ? 367 ASP A CG   1 
ATOM   657  O  OD1  . ASP A 1 48  ? 5.08400  25.71300 -30.49100 1.000 193.24899 ? 367 ASP A OD1  1 
ATOM   658  O  OD2  . ASP A 1 48  ? 3.50100  26.26400 -29.07400 1.000 218.11207 ? 367 ASP A OD2  1 
ATOM   659  H  H    . ASP A 1 48  ? 6.19300  26.67700 -31.75700 1.000 174.02917 ? 367 ASP A H    1 
ATOM   660  H  HA   . ASP A 1 48  ? 5.82400  29.29400 -31.19800 1.000 180.83630 ? 367 ASP A HA   1 
ATOM   661  H  HB2  . ASP A 1 48  ? 4.12900  28.58000 -29.70300 1.000 217.51548 ? 367 ASP A HB2  1 
ATOM   662  H  HB3  . ASP A 1 48  ? 3.81300  28.13600 -31.16400 1.000 217.51548 ? 367 ASP A HB3  1 
ATOM   663  N  N    . VAL A 1 49  ? 8.06000  28.10500 -29.86200 1.000 82.42959  ? 368 VAL A N    1 
ATOM   664  C  CA   . VAL A 1 49  ? 9.05700  28.07800 -28.80000 1.000 136.46693 ? 368 VAL A CA   1 
ATOM   665  C  C    . VAL A 1 49  ? 10.36800 28.61800 -29.35600 1.000 85.35875  ? 368 VAL A C    1 
ATOM   666  O  O    . VAL A 1 49  ? 10.60500 28.62000 -30.56700 1.000 96.14557  ? 368 VAL A O    1 
ATOM   667  C  CB   . VAL A 1 49  ? 9.25200  26.65700 -28.21800 1.000 129.96246 ? 368 VAL A CB   1 
ATOM   668  C  CG1  . VAL A 1 49  ? 9.78300  25.70400 -29.28200 1.000 88.61636  ? 368 VAL A CG1  1 
ATOM   669  C  CG2  . VAL A 1 49  ? 10.16400 26.68900 -26.99600 1.000 130.78969 ? 368 VAL A CG2  1 
ATOM   670  H  H    . VAL A 1 49  ? 8.37700  27.92400 -30.64100 1.000 99.01453  ? 368 VAL A H    1 
ATOM   671  H  HA   . VAL A 1 49  ? 8.74800  28.63400 -28.06700 1.000 163.85934 ? 368 VAL A HA   1 
ATOM   672  H  HB   . VAL A 1 49  ? 8.38700  26.32600 -27.93000 1.000 156.05399 ? 368 VAL A HB   1 
ATOM   673  H  HG11 . VAL A 1 49  ? 9.89800  24.82100 -28.89700 1.000 106.43867 ? 368 VAL A HG11 1 
ATOM   674  H  HG12 . VAL A 1 49  ? 9.15300  25.65600 -30.01800 1.000 106.43867 ? 368 VAL A HG12 1 
ATOM   675  H  HG13 . VAL A 1 49  ? 10.63700 26.02700 -29.60900 1.000 106.43867 ? 368 VAL A HG13 1 
ATOM   676  H  HG21 . VAL A 1 49  ? 10.27200 25.79000 -26.64900 1.000 157.04665 ? 368 VAL A HG21 1 
ATOM   677  H  HG22 . VAL A 1 49  ? 11.03100 27.04400 -27.24800 1.000 157.04665 ? 368 VAL A HG22 1 
ATOM   678  H  HG23 . VAL A 1 49  ? 9.77000  27.25400 -26.31300 1.000 157.04665 ? 368 VAL A HG23 1 
ATOM   679  N  N    . THR A 1 50  ? 11.18900 29.17000 -28.46400 1.000 149.73415 ? 369 THR A N    1 
ATOM   680  C  CA   . THR A 1 50  ? 12.41600 29.85200 -28.86000 1.000 145.47176 ? 369 THR A CA   1 
ATOM   681  C  C    . THR A 1 50  ? 13.62800 29.06200 -28.39000 1.000 56.64256  ? 369 THR A C    1 
ATOM   682  O  O    . THR A 1 50  ? 13.94100 29.07300 -27.18800 1.000 93.42480  ? 369 THR A O    1 
ATOM   683  C  CB   . THR A 1 50  ? 12.45300 31.27000 -28.28700 1.000 166.77732 ? 369 THR A CB   1 
ATOM   684  O  OG1  . THR A 1 50  ? 12.36200 31.21300 -26.85800 1.000 128.95868 ? 369 THR A OG1  1 
ATOM   685  C  CG2  . THR A 1 50  ? 11.29600 32.09500 -28.83300 1.000 119.64190 ? 369 THR A CG2  1 
ATOM   686  H  H    . THR A 1 50  ? 11.05000 29.15900 -27.61500 1.000 179.78002 ? 369 THR A H    1 
ATOM   687  H  HA   . THR A 1 50  ? 12.43700 29.91300 -29.82800 1.000 174.66514 ? 369 THR A HA   1 
ATOM   688  H  HB   . THR A 1 50  ? 13.28800 31.68900 -28.54700 1.000 200.23181 ? 369 THR A HB   1 
ATOM   689  H  HG1  . THR A 1 50  ? 12.50600 30.42700 -26.59900 1.000 154.84945 ? 369 THR A HG1  1 
ATOM   690  H  HG21 . THR A 1 50  ? 11.33300 32.99000 -28.46100 1.000 143.66931 ? 369 THR A HG21 1 
ATOM   691  H  HG22 . THR A 1 50  ? 11.36100 32.14400 -29.80000 1.000 143.66931 ? 369 THR A HG22 1 
ATOM   692  H  HG23 . THR A 1 50  ? 10.45600 31.67700 -28.58700 1.000 143.66931 ? 369 THR A HG23 1 
ATOM   693  N  N    . PRO A 1 51  ? 14.33300 28.37100 -29.27900 1.000 79.18396  ? 370 PRO A N    1 
ATOM   694  C  CA   . PRO A 1 51  ? 15.52500 27.62400 -28.87500 1.000 52.88222  ? 370 PRO A CA   1 
ATOM   695  C  C    . PRO A 1 51  ? 16.78500 28.47900 -28.92000 1.000 61.78465  ? 370 PRO A C    1 
ATOM   696  O  O    . PRO A 1 51  ? 16.86300 29.49600 -29.61200 1.000 79.95490  ? 370 PRO A O    1 
ATOM   697  C  CB   . PRO A 1 51  ? 15.59300 26.50700 -29.92500 1.000 46.67495  ? 370 PRO A CB   1 
ATOM   698  C  CG   . PRO A 1 51  ? 15.04100 27.15000 -31.15400 1.000 64.36568  ? 370 PRO A CG   1 
ATOM   699  C  CD   . PRO A 1 51  ? 13.97900 28.12400 -30.68800 1.000 94.36068  ? 370 PRO A CD   1 
ATOM   700  H  HA   . PRO A 1 51  ? 15.47200 27.30600 -27.96000 1.000 63.55769  ? 370 PRO A HA   1 
ATOM   701  H  HB2  . PRO A 1 51  ? 16.50300 26.19900 -30.06100 1.000 56.10897  ? 370 PRO A HB2  1 
ATOM   702  H  HB3  . PRO A 1 51  ? 15.06900 25.73500 -29.66000 1.000 56.10897  ? 370 PRO A HB3  1 
ATOM   703  H  HG2  . PRO A 1 51  ? 15.73900 27.61000 -31.64700 1.000 77.33785  ? 370 PRO A HG2  1 
ATOM   704  H  HG3  . PRO A 1 51  ? 14.66300 26.48600 -31.75100 1.000 77.33785  ? 370 PRO A HG3  1 
ATOM   705  H  HD2  . PRO A 1 51  ? 13.99200 28.94300 -31.20800 1.000 113.33185 ? 370 PRO A HD2  1 
ATOM   706  H  HD3  . PRO A 1 51  ? 13.08900 27.74900 -30.77200 1.000 113.33185 ? 370 PRO A HD3  1 
ATOM   707  N  N    . THR A 1 52  ? 17.78000 28.04100 -28.15500 1.000 46.83068  ? 371 THR A N    1 
ATOM   708  C  CA   . THR A 1 52  ? 19.10800 28.63000 -28.21900 1.000 31.91044  ? 371 THR A CA   1 
ATOM   709  C  C    . THR A 1 52  ? 19.95400 27.87500 -29.23600 1.000 29.40323  ? 371 THR A C    1 
ATOM   710  O  O    . THR A 1 52  ? 19.70400 26.70300 -29.53000 1.000 35.70871  ? 371 THR A O    1 
ATOM   711  C  CB   . THR A 1 52  ? 19.79600 28.59700 -26.85200 1.000 43.40755  ? 371 THR A CB   1 
ATOM   712  O  OG1  . THR A 1 52  ? 20.02000 27.23800 -26.46000 1.000 41.03137  ? 371 THR A OG1  1 
ATOM   713  C  CG2  . THR A 1 52  ? 18.93700 29.28900 -25.80400 1.000 50.13672  ? 371 THR A CG2  1 
ATOM   714  H  H    . THR A 1 52  ? 17.70300 27.39800 -27.58900 1.000 56.29585  ? 371 THR A H    1 
ATOM   715  H  HA   . THR A 1 52  ? 19.01600 29.55700 -28.49000 1.000 38.39156  ? 371 THR A HA   1 
ATOM   716  H  HB   . THR A 1 52  ? 20.64300 29.06400 -26.92100 1.000 52.18809  ? 371 THR A HB   1 
ATOM   717  H  HG1  . THR A 1 52  ? 19.88900 26.73100 -27.11700 1.000 49.33667  ? 371 THR A HG1  1 
ATOM   718  H  HG21 . THR A 1 52  ? 19.38700 29.25900 -24.94500 1.000 60.26310  ? 371 THR A HG21 1 
ATOM   719  H  HG22 . THR A 1 52  ? 18.79400 30.21300 -26.06100 1.000 60.26310  ? 371 THR A HG22 1 
ATOM   720  H  HG23 . THR A 1 52  ? 18.08200 28.83700 -25.73600 1.000 60.26310  ? 371 THR A HG23 1 
ATOM   721  N  N    . LYS A 1 53  ? 20.95900 28.56400 -29.78200 1.000 39.81771  ? 372 LYS A N    1 
ATOM   722  C  CA   . LYS A 1 53  ? 21.84500 27.91400 -30.74500 1.000 28.17920  ? 372 LYS A CA   1 
ATOM   723  C  C    . LYS A 1 53  ? 22.62700 26.77500 -30.09600 1.000 37.01724  ? 372 LYS A C    1 
ATOM   724  O  O    . LYS A 1 53  ? 22.83600 25.72700 -30.71700 1.000 38.15234  ? 372 LYS A O    1 
ATOM   725  C  CB   . LYS A 1 53  ? 22.79000 28.93800 -31.37700 1.000 45.36018  ? 372 LYS A CB   1 
ATOM   726  C  CG   . LYS A 1 53  ? 22.04200 30.03700 -32.18100 1.000 45.38794  ? 372 LYS A CG   1 
ATOM   727  C  CD   . LYS A 1 53  ? 23.00600 30.92800 -32.95200 1.000 84.55310  ? 372 LYS A CD   1 
ATOM   728  C  CE   . LYS A 1 53  ? 22.30500 32.15800 -33.54300 1.000 81.38640  ? 372 LYS A CE   1 
ATOM   729  N  NZ   . LYS A 1 53  ? 22.37400 33.37200 -32.66800 1.000 55.65393  ? 372 LYS A NZ   1 
ATOM   730  H  H    . LYS A 1 53  ? 21.14100 29.38700 -29.61300 1.000 47.88028  ? 372 LYS A H    1 
ATOM   731  H  HA   . LYS A 1 53  ? 21.29700 27.52900 -31.44700 1.000 33.91407  ? 372 LYS A HA   1 
ATOM   732  H  HB2  . LYS A 1 53  ? 23.31800 29.35700 -30.68000 1.000 54.53125  ? 372 LYS A HB2  1 
ATOM   733  H  HB3  . LYS A 1 53  ? 23.41000 28.47900 -31.96500 1.000 54.53125  ? 372 LYS A HB3  1 
ATOM   734  H  HG2  . LYS A 1 53  ? 21.42200 29.62000 -32.79900 1.000 54.56456  ? 372 LYS A HG2  1 
ATOM   735  H  HG3  . LYS A 1 53  ? 21.51500 30.58000 -31.57400 1.000 54.56456  ? 372 LYS A HG3  1 
ATOM   736  H  HD2  . LYS A 1 53  ? 23.72000 31.21600 -32.36300 1.000 101.56275 ? 372 LYS A HD2  1 
ATOM   737  H  HD3  . LYS A 1 53  ? 23.41700 30.41600 -33.66700 1.000 101.56275 ? 372 LYS A HD3  1 
ATOM   738  H  HE2  . LYS A 1 53  ? 22.70400 32.36600 -34.40200 1.000 97.76271  ? 372 LYS A HE2  1 
ATOM   739  H  HE3  . LYS A 1 53  ? 21.37400 31.94100 -33.70800 1.000 97.76271  ? 372 LYS A HE3  1 
ATOM   740  H  HZ1  . LYS A 1 53  ? 22.28000 34.10300 -33.16700 1.000 66.88375  ? 372 LYS A HZ1  1 
ATOM   741  H  HZ2  . LYS A 1 53  ? 21.72200 33.34000 -32.06400 1.000 66.88375  ? 372 LYS A HZ2  1 
ATOM   742  H  HZ3  . LYS A 1 53  ? 23.16100 33.39500 -32.25300 1.000 66.88375  ? 372 LYS A HZ3  1 
ATOM   743  N  N    . HIS A 1 54  ? 23.05100 26.94300 -28.84300 1.000 32.66513  ? 373 HIS A N    1 
ATOM   744  C  CA   . HIS A 1 54  ? 23.81900 25.87400 -28.21100 1.000 32.49701  ? 373 HIS A CA   1 
ATOM   745  C  C    . HIS A 1 54  ? 22.98100 24.61300 -28.03700 1.000 24.59947  ? 373 HIS A C    1 
ATOM   746  O  O    . HIS A 1 54  ? 23.48700 23.50000 -28.21200 1.000 32.23734  ? 373 HIS A O    1 
ATOM   747  C  CB   . HIS A 1 54  ? 24.39000 26.31600 -26.86300 1.000 38.21434  ? 373 HIS A CB   1 
ATOM   748  C  CG   . HIS A 1 54  ? 25.32500 25.30600 -26.27900 1.000 28.14179  ? 373 HIS A CG   1 
ATOM   749  N  ND1  . HIS A 1 54  ? 24.88300 24.18800 -25.60700 1.000 35.18552  ? 373 HIS A ND1  1 
ATOM   750  C  CD2  . HIS A 1 54  ? 26.67200 25.19300 -26.35000 1.000 36.74289  ? 373 HIS A CD2  1 
ATOM   751  C  CE1  . HIS A 1 54  ? 25.92200 23.45600 -25.24200 1.000 31.76885  ? 373 HIS A CE1  1 
ATOM   752  N  NE2  . HIS A 1 54  ? 27.01900 24.04100 -25.68800 1.000 36.73963  ? 373 HIS A NE2  1 
ATOM   753  H  H    . HIS A 1 54  ? 22.91100 27.64000 -28.35900 1.000 39.29719  ? 373 HIS A H    1 
ATOM   754  H  HA   . HIS A 1 54  ? 24.55900 25.67000 -28.80400 1.000 39.09544  ? 373 HIS A HA   1 
ATOM   755  H  HB2  . HIS A 1 54  ? 24.85700 27.15900 -26.97400 1.000 45.95623  ? 373 HIS A HB2  1 
ATOM   756  H  HB3  . HIS A 1 54  ? 23.66100 26.47500 -26.24300 1.000 45.95623  ? 373 HIS A HB3  1 
ATOM   757  H  HD1  . HIS A 1 54  ? 24.06000 23.99600 -25.44900 1.000 42.32165  ? 373 HIS A HD1  1 
ATOM   758  H  HD2  . HIS A 1 54  ? 27.25400 25.78500 -26.76900 1.000 44.19050  ? 373 HIS A HD2  1 
ATOM   759  H  HE1  . HIS A 1 54  ? 25.88600 22.66500 -24.75500 1.000 38.22166  ? 373 HIS A HE1  1 
ATOM   760  N  N    . ALA A 1 55  ? 21.70000 24.76400 -27.68500 1.000 35.92537  ? 374 ALA A N    1 
ATOM   761  C  CA   . ALA A 1 55  ? 20.82300 23.60200 -27.55900 1.000 37.54153  ? 374 ALA A CA   1 
ATOM   762  C  C    . ALA A 1 55  ? 20.61500 22.91800 -28.90300 1.000 36.51999  ? 374 ALA A C    1 
ATOM   763  O  O    . ALA A 1 55  ? 20.56200 21.68300 -28.97700 1.000 30.26147  ? 374 ALA A O    1 
ATOM   764  C  CB   . ALA A 1 55  ? 19.47600 24.01500 -26.97300 1.000 36.20033  ? 374 ALA A CB   1 
ATOM   765  H  H    . ALA A 1 55  ? 21.32600 25.52000 -27.51800 1.000 43.20947  ? 374 ALA A H    1 
ATOM   766  H  HA   . ALA A 1 55  ? 21.25200 22.97100 -26.96000 1.000 45.14887  ? 374 ALA A HA   1 
ATOM   767  H  HB1  . ALA A 1 55  ? 18.90400 23.23500 -26.89500 1.000 43.53942  ? 374 ALA A HB1  1 
ATOM   768  H  HB2  . ALA A 1 55  ? 19.61100 24.40600 -26.09600 1.000 43.53942  ? 374 ALA A HB2  1 
ATOM   769  H  HB3  . ALA A 1 55  ? 19.05600 24.66700 -27.55600 1.000 43.53942  ? 374 ALA A HB3  1 
ATOM   770  N  N    . ILE A 1 56  ? 20.46500 23.70400 -29.97100 1.000 36.29108  ? 375 ILE A N    1 
ATOM   771  C  CA   . ILE A 1 56  ? 20.36500 23.12000 -31.30800 1.000 43.60887  ? 375 ILE A CA   1 
ATOM   772  C  C    . ILE A 1 56  ? 21.63700 22.35600 -31.64700 1.000 28.77033  ? 375 ILE A C    1 
ATOM   773  O  O    . ILE A 1 56  ? 21.60000 21.20400 -32.09200 1.000 33.18643  ? 375 ILE A O    1 
ATOM   774  C  CB   . ILE A 1 56  ? 20.07600 24.21600 -32.35300 1.000 37.85687  ? 375 ILE A CB   1 
ATOM   775  C  CG1  . ILE A 1 56  ? 18.67200 24.78700 -32.15100 1.000 40.32979  ? 375 ILE A CG1  1 
ATOM   776  C  CG2  . ILE A 1 56  ? 20.23500 23.65500 -33.75100 1.000 41.89924  ? 375 ILE A CG2  1 
ATOM   777  C  CD1  . ILE A 1 56  ? 18.48400 26.17800 -32.73900 1.000 49.09349  ? 375 ILE A CD1  1 
ATOM   778  H  H    . ILE A 1 56  ? 20.42000 24.56200 -29.94400 1.000 43.64832  ? 375 ILE A H    1 
ATOM   779  H  HA   . ILE A 1 56  ? 19.62600 22.49200 -31.32200 1.000 52.42967  ? 375 ILE A HA   1 
ATOM   780  H  HB   . ILE A 1 56  ? 20.71400 24.93800 -32.23800 1.000 45.52728  ? 375 ILE A HB   1 
ATOM   781  H  HG12 . ILE A 1 56  ? 18.02600 24.18500 -32.55300 1.000 48.49478  ? 375 ILE A HG12 1 
ATOM   782  H  HG13 . ILE A 1 56  ? 18.47800 24.81800 -31.20100 1.000 48.49478  ? 375 ILE A HG13 1 
ATOM   783  H  HG21 . ILE A 1 56  ? 20.05200 24.35000 -34.40200 1.000 50.37812  ? 375 ILE A HG21 1 
ATOM   784  H  HG22 . ILE A 1 56  ? 21.14200 23.33300 -33.86900 1.000 50.37812  ? 375 ILE A HG22 1 
ATOM   785  H  HG23 . ILE A 1 56  ? 19.61300 22.92200 -33.87800 1.000 50.37812  ? 375 ILE A HG23 1 
ATOM   786  H  HD11 . ILE A 1 56  ? 17.57600 26.47800 -32.57600 1.000 59.01122  ? 375 ILE A HD11 1 
ATOM   787  H  HD12 . ILE A 1 56  ? 19.10700 26.79300 -32.32200 1.000 59.01122  ? 375 ILE A HD12 1 
ATOM   788  H  HD13 . ILE A 1 56  ? 18.64900 26.15100 -33.69500 1.000 59.01122  ? 375 ILE A HD13 1 
ATOM   789  N  N    . VAL A 1 57  ? 22.78500 22.98100 -31.43600 1.000 31.54049  ? 376 VAL A N    1 
ATOM   790  C  CA   . VAL A 1 57  ? 24.08500 22.33100 -31.76900 1.000 40.58957  ? 376 VAL A CA   1 
ATOM   791  C  C    . VAL A 1 57  ? 24.23800 21.05800 -30.93100 1.000 35.79227  ? 376 VAL A C    1 
ATOM   792  O  O    . VAL A 1 57  ? 24.60200 20.03200 -31.49300 1.000 35.44818  ? 376 VAL A O    1 
ATOM   793  C  CB   . VAL A 1 57  ? 25.26800 23.29800 -31.57100 1.000 42.65514  ? 376 VAL A CB   1 
ATOM   794  C  CG1  . VAL A 1 57  ? 26.59400 22.57100 -31.42500 1.000 43.78852  ? 376 VAL A CG1  1 
ATOM   795  C  CG2  . VAL A 1 57  ? 25.34000 24.32200 -32.69000 1.000 44.05454  ? 376 VAL A CG2  1 
ATOM   796  H  H    . VAL A 1 57  ? 22.85200 23.77200 -31.10600 1.000 37.94762  ? 376 VAL A H    1 
ATOM   797  H  HA   . VAL A 1 57  ? 24.08900 22.08800 -32.70800 1.000 48.80651  ? 376 VAL A HA   1 
ATOM   798  H  HB   . VAL A 1 57  ? 25.10300 23.76600 -30.73700 1.000 51.28520  ? 376 VAL A HB   1 
ATOM   799  H  HG11 . VAL A 1 57  ? 27.30600 23.21800 -31.30300 1.000 52.64526  ? 376 VAL A HG11 1 
ATOM   800  H  HG12 . VAL A 1 57  ? 26.55700 21.98200 -30.65500 1.000 52.64526  ? 376 VAL A HG12 1 
ATOM   801  H  HG13 . VAL A 1 57  ? 26.76600 22.04800 -32.22400 1.000 52.64526  ? 376 VAL A HG13 1 
ATOM   802  H  HG21 . VAL A 1 57  ? 26.09200 24.91500 -32.53800 1.000 52.96448  ? 376 VAL A HG21 1 
ATOM   803  H  HG22 . VAL A 1 57  ? 25.45400 23.86700 -33.53900 1.000 52.96448  ? 376 VAL A HG22 1 
ATOM   804  H  HG23 . VAL A 1 57  ? 24.52000 24.83900 -32.70900 1.000 52.96448  ? 376 VAL A HG23 1 
ATOM   805  N  N    . GLN A 1 58  ? 23.97300 21.14300 -29.63400 1.000 33.79941  ? 377 GLN A N    1 
ATOM   806  C  CA   . GLN A 1 58  ? 24.16100 19.95300 -28.81300 1.000 35.44252  ? 377 GLN A CA   1 
ATOM   807  C  C    . GLN A 1 58  ? 23.23600 18.82500 -29.25600 1.000 24.86089  ? 377 GLN A C    1 
ATOM   808  O  O    . GLN A 1 58  ? 23.64600 17.66100 -29.29300 1.000 33.85116  ? 377 GLN A O    1 
ATOM   809  C  CB   . GLN A 1 58  ? 23.94200 20.27200 -27.32500 1.000 34.67376  ? 377 GLN A CB   1 
ATOM   810  C  CG   . GLN A 1 58  ? 24.28500 19.08400 -26.42900 1.000 40.24004  ? 377 GLN A CG   1 
ATOM   811  C  CD   . GLN A 1 58  ? 24.43800 19.45900 -24.96300 1.000 37.77832  ? 377 GLN A CD   1 
ATOM   812  O  OE1  . GLN A 1 58  ? 24.85600 20.56600 -24.64100 1.000 38.62480  ? 377 GLN A OE1  1 
ATOM   813  N  NE2  . GLN A 1 58  ? 24.08600 18.53900 -24.07100 1.000 45.67296  ? 377 GLN A NE2  1 
ATOM   814  H  H    . GLN A 1 58  ? 23.69600 21.84600 -29.22300 1.000 40.65833  ? 377 GLN A H    1 
ATOM   815  H  HA   . GLN A 1 58  ? 25.07700 19.65700 -28.93200 1.000 42.63006  ? 377 GLN A HA   1 
ATOM   816  H  HB2  . GLN A 1 58  ? 24.48800 21.03300 -27.07400 1.000 41.70754  ? 377 GLN A HB2  1 
ATOM   817  H  HB3  . GLN A 1 58  ? 23.01700 20.52700 -27.18200 1.000 41.70754  ? 377 GLN A HB3  1 
ATOM   818  H  HG2  . GLN A 1 58  ? 23.59000 18.41200 -26.51400 1.000 48.38708  ? 377 GLN A HG2  1 
ATOM   819  H  HG3  . GLN A 1 58  ? 25.11000 18.68000 -26.74100 1.000 48.38708  ? 377 GLN A HG3  1 
ATOM   820  H  HE21 . GLN A 1 58  ? 23.79700 17.77300 -24.33400 1.000 54.90658  ? 377 GLN A HE21 1 
ATOM   821  H  HE22 . GLN A 1 58  ? 24.14700 18.71000 -23.23000 1.000 54.90658  ? 377 GLN A HE22 1 
ATOM   822  N  N    . THR A 1 59  ? 21.98500 19.14300 -29.59000 1.000 28.20310  ? 378 THR A N    1 
ATOM   823  C  CA   . THR A 1 59  ? 21.06200 18.09100 -30.02300 1.000 28.20653  ? 378 THR A CA   1 
ATOM   824  C  C    . THR A 1 59  ? 21.57600 17.40000 -31.28400 1.000 40.88222  ? 378 THR A C    1 
ATOM   825  O  O    . THR A 1 59  ? 21.57200 16.16500 -31.37500 1.000 33.75478  ? 378 THR A O    1 
ATOM   826  C  CB   . THR A 1 59  ? 19.67400 18.67800 -30.26400 1.000 38.20500  ? 378 THR A CB   1 
ATOM   827  O  OG1  . THR A 1 59  ? 19.23800 19.35900 -29.09000 1.000 43.13791  ? 378 THR A OG1  1 
ATOM   828  C  CG2  . THR A 1 59  ? 18.67100 17.56800 -30.59400 1.000 41.33610  ? 378 THR A CG2  1 
ATOM   829  H  H    . THR A 1 59  ? 21.65700 19.93800 -29.57400 1.000 33.94275  ? 378 THR A H    1 
ATOM   830  H  HA   . THR A 1 59  ? 21.00400 17.42600 -29.31900 1.000 33.94687  ? 378 THR A HA   1 
ATOM   831  H  HB   . THR A 1 59  ? 19.72400 19.29400 -31.01200 1.000 45.94503  ? 378 THR A HB   1 
ATOM   832  H  HG1  . THR A 1 59  ? 19.63900 20.09400 -29.02700 1.000 51.86452  ? 378 THR A HG1  1 
ATOM   833  H  HG21 . THR A 1 59  ? 17.79500 17.95700 -30.74400 1.000 49.70236  ? 378 THR A HG21 1 
ATOM   834  H  HG22 . THR A 1 59  ? 18.95800 17.10000 -31.39400 1.000 49.70236  ? 378 THR A HG22 1 
ATOM   835  H  HG23 . THR A 1 59  ? 18.62400 16.94300 -29.85300 1.000 49.70236  ? 378 THR A HG23 1 
ATOM   836  N  N    . LEU A 1 60  ? 22.06800 18.18400 -32.24700 1.000 37.19918  ? 379 LEU A N    1 
ATOM   837  C  CA   . LEU A 1 60  ? 22.67800 17.61100 -33.44700 1.000 34.62484  ? 379 LEU A CA   1 
ATOM   838  C  C    . LEU A 1 60  ? 23.90000 16.75800 -33.11200 1.000 39.98532  ? 379 LEU A C    1 
ATOM   839  O  O    . LEU A 1 60  ? 24.06300 15.65900 -33.65300 1.000 37.04478  ? 379 LEU A O    1 
ATOM   840  C  CB   . LEU A 1 60  ? 23.04400 18.73100 -34.41900 1.000 40.43386  ? 379 LEU A CB   1 
ATOM   841  C  CG   . LEU A 1 60  ? 21.88000 19.44700 -35.11400 1.000 41.79447  ? 379 LEU A CG   1 
ATOM   842  C  CD1  . LEU A 1 60  ? 22.35100 20.72600 -35.78400 1.000 70.16088  ? 379 LEU A CD1  1 
ATOM   843  C  CD2  . LEU A 1 60  ? 21.21500 18.54100 -36.15200 1.000 45.66409  ? 379 LEU A CD2  1 
ATOM   844  H  H    . LEU A 1 60  ? 22.05800 19.04400 -32.22400 1.000 44.73805  ? 379 LEU A H    1 
ATOM   845  H  HA   . LEU A 1 60  ? 22.03100 17.02200 -33.86600 1.000 41.64884  ? 379 LEU A HA   1 
ATOM   846  H  HB2  . LEU A 1 60  ? 23.56200 19.39400 -33.93600 1.000 48.61966  ? 379 LEU A HB2  1 
ATOM   847  H  HB3  . LEU A 1 60  ? 23.62400 18.36100 -35.10300 1.000 48.61966  ? 379 LEU A HB3  1 
ATOM   848  H  HG   . LEU A 1 60  ? 21.22900 19.67000 -34.43000 1.000 50.25240  ? 379 LEU A HG   1 
ATOM   849  H  HD11 . LEU A 1 60  ? 21.59900 21.16100 -36.21600 1.000 84.29208  ? 379 LEU A HD11 1 
ATOM   850  H  HD12 . LEU A 1 60  ? 22.72800 21.32100 -35.11700 1.000 84.29208  ? 379 LEU A HD12 1 
ATOM   851  H  HD13 . LEU A 1 60  ? 23.02600 20.51400 -36.44700 1.000 84.29208  ? 379 LEU A HD13 1 
ATOM   852  H  HD21 . LEU A 1 60  ? 20.48400 19.01700 -36.57600 1.000 54.89594  ? 379 LEU A HD21 1 
ATOM   853  H  HD22 . LEU A 1 60  ? 21.86700 18.28600 -36.82400 1.000 54.89594  ? 379 LEU A HD22 1 
ATOM   854  H  HD23 . LEU A 1 60  ? 20.87300 17.74500 -35.71500 1.000 54.89594  ? 379 LEU A HD23 1 
ATOM   855  N  N    . VAL A 1 61  ? 24.77200 17.23500 -32.21800 1.000 37.59318  ? 380 VAL A N    1 
ATOM   856  C  CA   . VAL A 1 61  ? 25.94000 16.43600 -31.84200 1.000 41.06629  ? 380 VAL A CA   1 
ATOM   857  C  C    . VAL A 1 61  ? 25.51000 15.15100 -31.14600 1.000 40.45513  ? 380 VAL A C    1 
ATOM   858  O  O    . VAL A 1 61  ? 26.11700 14.08600 -31.33500 1.000 36.94870  ? 380 VAL A O    1 
ATOM   859  C  CB   . VAL A 1 61  ? 26.90000 17.24700 -30.95200 1.000 40.15083  ? 380 VAL A CB   1 
ATOM   860  C  CG1  . VAL A 1 61  ? 28.02700 16.36100 -30.46900 1.000 45.40951  ? 380 VAL A CG1  1 
ATOM   861  C  CG2  . VAL A 1 61  ? 27.45100 18.44700 -31.70500 1.000 48.60802  ? 380 VAL A CG2  1 
ATOM   862  H  H    . VAL A 1 61  ? 24.70800 17.99800 -31.82700 1.000 45.21085  ? 380 VAL A H    1 
ATOM   863  H  HA   . VAL A 1 61  ? 26.41600 16.19800 -32.65300 1.000 49.37858  ? 380 VAL A HA   1 
ATOM   864  H  HB   . VAL A 1 61  ? 26.40700 17.57600 -30.18400 1.000 48.28003  ? 380 VAL A HB   1 
ATOM   865  H  HG11 . VAL A 1 61  ? 28.62800 16.87700 -29.90900 1.000 54.59044  ? 380 VAL A HG11 1 
ATOM   866  H  HG12 . VAL A 1 61  ? 27.66200 15.62300 -29.95600 1.000 54.59044  ? 380 VAL A HG12 1 
ATOM   867  H  HG13 . VAL A 1 61  ? 28.51500 16.01300 -31.23200 1.000 54.59044  ? 380 VAL A HG13 1 
ATOM   868  H  HG21 . VAL A 1 61  ? 28.05200 18.94300 -31.12800 1.000 58.42866  ? 380 VAL A HG21 1 
ATOM   869  H  HG22 . VAL A 1 61  ? 27.93400 18.14300 -32.48900 1.000 58.42866  ? 380 VAL A HG22 1 
ATOM   870  H  HG23 . VAL A 1 61  ? 26.71900 19.02100 -31.97900 1.000 58.42866  ? 380 VAL A HG23 1 
ATOM   871  N  N    . HIS A 1 62  ? 24.46300 15.21300 -30.33600 1.000 32.43232  ? 381 HIS A N    1 
ATOM   872  C  CA   . HIS A 1 62  ? 23.96300 13.98800 -29.66000 1.000 37.08336  ? 381 HIS A CA   1 
ATOM   873  C  C    . HIS A 1 62  ? 23.52800 12.96600 -30.71400 1.000 44.02605  ? 381 HIS A C    1 
ATOM   874  O  O    . HIS A 1 62  ? 23.80600 11.78400 -30.55900 1.000 39.75689  ? 381 HIS A O    1 
ATOM   875  C  CB   . HIS A 1 62  ? 22.81300 14.27100 -28.69300 1.000 40.13955  ? 381 HIS A CB   1 
ATOM   876  C  CG   . HIS A 1 62  ? 22.01900 13.06500 -28.32700 1.000 47.93149  ? 381 HIS A CG   1 
ATOM   877  N  ND1  . HIS A 1 62  ? 22.41900 12.17100 -27.36200 1.000 43.64295  ? 381 HIS A ND1  1 
ATOM   878  C  CD2  . HIS A 1 62  ? 20.86200 12.60000 -28.79900 1.000 43.35093  ? 381 HIS A CD2  1 
ATOM   879  C  CE1  . HIS A 1 62  ? 21.52600 11.20500 -27.26300 1.000 46.85144  ? 381 HIS A CE1  1 
ATOM   880  N  NE2  . HIS A 1 62  ? 20.57400 11.44600 -28.12800 1.000 47.47627  ? 381 HIS A NE2  1 
ATOM   881  H  H    . HIS A 1 62  ? 24.02600 15.93200 -30.15700 1.000 39.01782  ? 381 HIS A H    1 
ATOM   882  H  HA   . HIS A 1 62  ? 24.69200 13.63200 -29.12800 1.000 44.59906  ? 381 HIS A HA   1 
ATOM   883  H  HB2  . HIS A 1 62  ? 23.17300 14.66800 -27.88400 1.000 48.26649  ? 381 HIS A HB2  1 
ATOM   884  H  HB3  . HIS A 1 62  ? 22.22100 14.92800 -29.09200 1.000 48.26649  ? 381 HIS A HB3  1 
ATOM   885  H  HD1  . HIS A 1 62  ? 23.13900 12.23200 -26.89600 1.000 52.47057  ? 381 HIS A HD1  1 
ATOM   886  H  HD2  . HIS A 1 62  ? 20.34400 12.99100 -29.46500 1.000 52.12014  ? 381 HIS A HD2  1 
ATOM   887  H  HE1  . HIS A 1 62  ? 21.56600 10.48100 -26.68100 1.000 56.32076  ? 381 HIS A HE1  1 
ATOM   888  N  N    . LEU A 1 63  ? 22.86200 13.43300 -31.75900 1.000 35.97936  ? 382 LEU A N    1 
ATOM   889  C  CA   . LEU A 1 63  ? 22.42600 12.48100 -32.78000 1.000 44.45150  ? 382 LEU A CA   1 
ATOM   890  C  C    . LEU A 1 63  ? 23.61200 11.74600 -33.38600 1.000 38.46616  ? 382 LEU A C    1 
ATOM   891  O  O    . LEU A 1 63  ? 23.57700 10.52100 -33.55100 1.000 43.54696  ? 382 LEU A O    1 
ATOM   892  C  CB   . LEU A 1 63  ? 21.63600 13.19000 -33.87700 1.000 55.22787  ? 382 LEU A CB   1 
ATOM   893  C  CG   . LEU A 1 63  ? 20.24000 13.66500 -33.47400 1.000 81.94478  ? 382 LEU A CG   1 
ATOM   894  C  CD1  . LEU A 1 63  ? 19.66300 14.47400 -34.62200 1.000 73.35092  ? 382 LEU A CD1  1 
ATOM   895  C  CD2  . LEU A 1 63  ? 19.31700 12.49700 -33.13900 1.000 84.90583  ? 382 LEU A CD2  1 
ATOM   896  H  H    . LEU A 1 63  ? 22.65700 14.25700 -31.89800 1.000 43.27427  ? 382 LEU A H    1 
ATOM   897  H  HA   . LEU A 1 63  ? 21.85000 11.83100 -32.34900 1.000 53.44083  ? 382 LEU A HA   1 
ATOM   898  H  HB2  . LEU A 1 63  ? 22.14800 13.95700 -34.17900 1.000 66.37248  ? 382 LEU A HB2  1 
ATOM   899  H  HB3  . LEU A 1 63  ? 21.55100 12.58900 -34.63400 1.000 66.37248  ? 382 LEU A HB3  1 
ATOM   900  H  HG   . LEU A 1 63  ? 20.31200 14.20800 -32.67400 1.000 98.43277  ? 382 LEU A HG   1 
ATOM   901  H  HD11 . LEU A 1 63  ? 18.77500 14.78500 -34.38500 1.000 88.12013  ? 382 LEU A HD11 1 
ATOM   902  H  HD12 . LEU A 1 63  ? 20.23500 15.23700 -34.80100 1.000 88.12013  ? 382 LEU A HD12 1 
ATOM   903  H  HD13 . LEU A 1 63  ? 19.60900 13.91800 -35.41500 1.000 88.12013  ? 382 LEU A HD13 1 
ATOM   904  H  HD21 . LEU A 1 63  ? 18.44300 12.83600 -32.88900 1.000 101.98603 ? 382 LEU A HD21 1 
ATOM   905  H  HD22 . LEU A 1 63  ? 19.23000 11.92100 -33.91400 1.000 101.98603 ? 382 LEU A HD22 1 
ATOM   906  H  HD23 . LEU A 1 63  ? 19.69000 11.99100 -32.40100 1.000 101.98603 ? 382 LEU A HD23 1 
ATOM   907  N  N    . LYS A 1 64  ? 24.68400 12.47300 -33.68700 1.000 40.08871  ? 383 LYS A N    1 
ATOM   908  C  CA   . LYS A 1 64  ? 25.85400 11.85500 -34.30000 1.000 48.26527  ? 383 LYS A CA   1 
ATOM   909  C  C    . LYS A 1 64  ? 26.60600 10.96900 -33.31200 1.000 48.01844  ? 383 LYS A C    1 
ATOM   910  O  O    . LYS A 1 64  ? 27.08600 9.89300  -33.68600 1.000 58.66006  ? 383 LYS A O    1 
ATOM   911  C  CB   . LYS A 1 64  ? 26.75900 12.94800 -34.87900 1.000 51.10477  ? 383 LYS A CB   1 
ATOM   912  C  CG   . LYS A 1 64  ? 27.80700 12.48000 -35.89700 1.000 73.58940  ? 383 LYS A CG   1 
ATOM   913  C  CD   . LYS A 1 64  ? 27.18100 11.85100 -37.13100 1.000 86.19536  ? 383 LYS A CD   1 
ATOM   914  C  CE   . LYS A 1 64  ? 28.19900 11.67900 -38.26600 1.000 94.16233  ? 383 LYS A CE   1 
ATOM   915  N  NZ   . LYS A 1 64  ? 28.65900 12.99700 -38.79800 1.000 103.84355 ? 383 LYS A NZ   1 
ATOM   916  H  H    . LYS A 1 64  ? 24.75400 13.31800 -33.54600 1.000 48.20548  ? 383 LYS A H    1 
ATOM   917  H  HA   . LYS A 1 64  ? 25.56100 11.27500 -35.02000 1.000 58.01736  ? 383 LYS A HA   1 
ATOM   918  H  HB2  . LYS A 1 64  ? 26.19900 13.61700 -35.30200 1.000 61.42476  ? 383 LYS A HB2  1 
ATOM   919  H  HB3  . LYS A 1 64  ? 27.21900 13.38500 -34.14500 1.000 61.42476  ? 383 LYS A HB3  1 
ATOM   920  H  HG2  . LYS A 1 64  ? 28.35300 13.23600 -36.16500 1.000 88.40631  ? 383 LYS A HG2  1 
ATOM   921  H  HG3  . LYS A 1 64  ? 28.39900 11.83800 -35.47500 1.000 88.40631  ? 383 LYS A HG3  1 
ATOM   922  H  HD2  . LYS A 1 64  ? 26.80800 10.98600 -36.89900 1.000 103.53347 ? 383 LYS A HD2  1 
ATOM   923  H  HD3  . LYS A 1 64  ? 26.44600 12.40400 -37.43800 1.000 103.53347 ? 383 LYS A HD3  1 
ATOM   924  H  HE2  . LYS A 1 64  ? 28.96300 11.17600 -37.94300 1.000 113.09383 ? 383 LYS A HE2  1 
ATOM   925  H  HE3  . LYS A 1 64  ? 27.80100 11.16100 -38.98300 1.000 113.09383 ? 383 LYS A HE3  1 
ATOM   926  H  HZ1  . LYS A 1 64  ? 29.08100 12.87400 -39.57200 1.000 124.71129 ? 383 LYS A HZ1  1 
ATOM   927  H  HZ2  . LYS A 1 64  ? 27.95600 13.52800 -38.92500 1.000 124.71129 ? 383 LYS A HZ2  1 
ATOM   928  H  HZ3  . LYS A 1 64  ? 29.21500 13.37500 -38.21500 1.000 124.71129 ? 383 LYS A HZ3  1 
ATOM   929  N  N    . PHE A 1 65  ? 26.71300 11.38700 -32.04800 1.000 52.52486  ? 384 PHE A N    1 
ATOM   930  C  CA   . PHE A 1 65  ? 27.47400 10.65800 -31.02800 1.000 51.30297  ? 384 PHE A CA   1 
ATOM   931  C  C    . PHE A 1 65  ? 26.61900 10.44900 -29.77800 1.000 53.57537  ? 384 PHE A C    1 
ATOM   932  O  O    . PHE A 1 65  ? 26.87500 11.05000 -28.72800 1.000 57.37914  ? 384 PHE A O    1 
ATOM   933  C  CB   . PHE A 1 65  ? 28.76800 11.40200 -30.67600 1.000 52.68726  ? 384 PHE A CB   1 
ATOM   934  C  CG   . PHE A 1 65  ? 29.59400 11.78300 -31.87900 1.000 72.30218  ? 384 PHE A CG   1 
ATOM   935  C  CD1  . PHE A 1 65  ? 30.48200 10.88500 -32.44100 1.000 66.57072  ? 384 PHE A CD1  1 
ATOM   936  C  CD2  . PHE A 1 65  ? 29.47000 13.03400 -32.45300 1.000 61.71246  ? 384 PHE A CD2  1 
ATOM   937  C  CE1  . PHE A 1 65  ? 31.22600 11.22900 -33.55400 1.000 103.62756 ? 384 PHE A CE1  1 
ATOM   938  C  CE2  . PHE A 1 65  ? 30.21900 13.38500 -33.56100 1.000 63.96500  ? 384 PHE A CE2  1 
ATOM   939  C  CZ   . PHE A 1 65  ? 31.09200 12.48300 -34.11500 1.000 60.67535  ? 384 PHE A CZ   1 
ATOM   940  H  H    . PHE A 1 65  ? 26.34300 12.10700 -31.75600 1.000 63.12886  ? 384 PHE A H    1 
ATOM   941  H  HA   . PHE A 1 65  ? 27.71500 9.79000  -31.38900 1.000 61.66260  ? 384 PHE A HA   1 
ATOM   942  H  HB2  . PHE A 1 65  ? 28.54500 12.20500 -30.17900 1.000 63.32374  ? 384 PHE A HB2  1 
ATOM   943  H  HB3  . PHE A 1 65  ? 29.30300 10.84500 -30.09000 1.000 63.32374  ? 384 PHE A HB3  1 
ATOM   944  H  HD1  . PHE A 1 65  ? 30.58000 10.04000 -32.06600 1.000 79.98390  ? 384 PHE A HD1  1 
ATOM   945  H  HD2  . PHE A 1 65  ? 28.87400 13.64800 -32.08900 1.000 74.15398  ? 384 PHE A HD2  1 
ATOM   946  H  HE1  . PHE A 1 65  ? 31.81800 10.61500 -33.92500 1.000 124.45210 ? 384 PHE A HE1  1 
ATOM   947  H  HE2  . PHE A 1 65  ? 30.13100 14.23400 -33.93100 1.000 76.85703  ? 384 PHE A HE2  1 
ATOM   948  H  HZ   . PHE A 1 65  ? 31.59100 12.71500 -34.86500 1.000 72.90945  ? 384 PHE A HZ   1 
ATOM   949  N  N    . PRO A 1 66  ? 25.61400 9.56700  -29.84500 1.000 45.62186  ? 385 PRO A N    1 
ATOM   950  C  CA   . PRO A 1 66  ? 24.64400 9.48500  -28.73700 1.000 44.83450  ? 385 PRO A CA   1 
ATOM   951  C  C    . PRO A 1 66  ? 25.22900 8.99400  -27.42900 1.000 45.80190  ? 385 PRO A C    1 
ATOM   952  O  O    . PRO A 1 66  ? 24.70300 9.35300  -26.36300 1.000 46.44225  ? 385 PRO A O    1 
ATOM   953  C  CB   . PRO A 1 66  ? 23.56000 8.54200  -29.27800 1.000 45.14082  ? 385 PRO A CB   1 
ATOM   954  C  CG   . PRO A 1 66  ? 24.18300 7.83200  -30.44300 1.000 52.04681  ? 385 PRO A CG   1 
ATOM   955  C  CD   . PRO A 1 66  ? 25.19500 8.77600  -31.01700 1.000 59.66685  ? 385 PRO A CD   1 
ATOM   956  H  HA   . PRO A 1 66  ? 24.30800 10.36300 -28.49800 1.000 53.30625  ? 385 PRO A HA   1 
ATOM   957  H  HB2  . PRO A 1 66  ? 23.27500 7.91200  -28.59800 1.000 53.67383  ? 385 PRO A HB2  1 
ATOM   958  H  HB3  . PRO A 1 66  ? 22.77300 9.03800  -29.55300 1.000 53.67383  ? 385 PRO A HB3  1 
ATOM   959  H  HG2  . PRO A 1 66  ? 24.60300 7.00500  -30.16000 1.000 62.55521  ? 385 PRO A HG2  1 
ATOM   960  H  HG3  . PRO A 1 66  ? 23.51300 7.59800  -31.10500 1.000 62.55521  ? 385 PRO A HG3  1 
ATOM   961  H  HD2  . PRO A 1 66  ? 25.94200 8.30300  -31.41600 1.000 71.69925  ? 385 PRO A HD2  1 
ATOM   962  H  HD3  . PRO A 1 66  ? 24.81100 9.33600  -31.71000 1.000 71.69925  ? 385 PRO A HD3  1 
ATOM   963  N  N    . THR A 1 67  ? 26.30600 8.20900  -27.47200 1.000 55.65371  ? 386 THR A N    1 
ATOM   964  C  CA   . THR A 1 67  ? 26.88400 7.66700  -26.24700 1.000 88.57030  ? 386 THR A CA   1 
ATOM   965  C  C    . THR A 1 67  ? 27.74500 8.69200  -25.51900 1.000 67.38972  ? 386 THR A C    1 
ATOM   966  O  O    . THR A 1 67  ? 27.90600 8.60900  -24.29400 1.000 83.26309  ? 386 THR A O    1 
ATOM   967  C  CB   . THR A 1 67  ? 27.71400 6.42800  -26.57800 1.000 69.31627  ? 386 THR A CB   1 
ATOM   968  O  OG1  . THR A 1 67  ? 28.74200 6.79600  -27.50900 1.000 81.80369  ? 386 THR A OG1  1 
ATOM   969  C  CG2  . THR A 1 67  ? 26.83000 5.36300  -27.22000 1.000 83.97482  ? 386 THR A CG2  1 
ATOM   970  H  H    . THR A 1 67  ? 26.71300 7.98100  -28.19500 1.000 66.88348  ? 386 THR A H    1 
ATOM   971  H  HA   . THR A 1 67  ? 26.15400 7.42800  -25.65400 1.000 106.38339 ? 386 THR A HA   1 
ATOM   972  H  HB   . THR A 1 67  ? 28.10300 6.07500  -25.76200 1.000 83.27856  ? 386 THR A HB   1 
ATOM   973  H  HG21 . THR A 1 67  ? 27.36400 4.58000  -27.42700 1.000 100.86882 ? 386 THR A HG21 1 
ATOM   974  H  HG22 . THR A 1 67  ? 26.12100 5.11700  -26.60500 1.000 100.86882 ? 386 THR A HG22 1 
ATOM   975  H  HG23 . THR A 1 67  ? 26.44200 5.71400  -28.03700 1.000 100.86882 ? 386 THR A HG23 1 
ATOM   976  N  N    . LYS A 1 68  ? 28.28200 9.66900  -26.25200 1.000 75.07557  ? 387 LYS A N    1 
ATOM   977  C  CA   . LYS A 1 68  ? 29.26500 10.61000 -25.73400 1.000 67.58020  ? 387 LYS A CA   1 
ATOM   978  C  C    . LYS A 1 68  ? 28.68000 11.95800 -25.32800 1.000 63.53102  ? 387 LYS A C    1 
ATOM   979  O  O    . LYS A 1 68  ? 29.24200 12.63000 -24.46100 1.000 66.09732  ? 387 LYS A O    1 
ATOM   980  C  CB   . LYS A 1 68  ? 30.35700 10.84100 -26.78500 1.000 69.19369  ? 387 LYS A CB   1 
ATOM   981  C  CG   . LYS A 1 68  ? 31.04300 9.56500  -27.26100 1.000 81.41273  ? 387 LYS A CG   1 
ATOM   982  C  CD   . LYS A 1 68  ? 32.07200 9.86900  -28.35000 1.000 145.84416 ? 387 LYS A CD   1 
ATOM   983  C  CE   . LYS A 1 68  ? 32.65700 8.58900  -28.96100 1.000 146.65012 ? 387 LYS A CE   1 
ATOM   984  N  NZ   . LYS A 1 68  ? 33.46500 8.85500  -30.20100 1.000 110.48498 ? 387 LYS A NZ   1 
ATOM   985  H  H    . LYS A 1 68  ? 28.07900 9.80200  -27.07700 1.000 90.18972  ? 387 LYS A H    1 
ATOM   986  H  HA   . LYS A 1 68  ? 29.62500 10.20600 -24.92900 1.000 81.19527  ? 387 LYS A HA   1 
ATOM   987  H  HB2  . LYS A 1 68  ? 29.96600 11.29100 -27.55000 1.000 83.13146  ? 387 LYS A HB2  1 
ATOM   988  H  HB3  . LYS A 1 68  ? 31.02600 11.43800 -26.41600 1.000 83.13146  ? 387 LYS A HB3  1 
ATOM   989  H  HG2  . LYS A 1 68  ? 31.47900 9.13000  -26.51200 1.000 97.79431  ? 387 LYS A HG2  1 
ATOM   990  H  HG3  . LYS A 1 68  ? 30.38000 8.94500  -27.60200 1.000 97.79431  ? 387 LYS A HG3  1 
ATOM   991  H  HD2  . LYS A 1 68  ? 31.65600 10.39900 -29.04800 1.000 175.11202 ? 387 LYS A HD2  1 
ATOM   992  H  HD3  . LYS A 1 68  ? 32.78900 10.40500 -27.97600 1.000 175.11202 ? 387 LYS A HD3  1 
ATOM   993  H  HE2  . LYS A 1 68  ? 33.21700 8.14800  -28.30300 1.000 176.07918 ? 387 LYS A HE2  1 
ATOM   994  H  HE3  . LYS A 1 68  ? 31.93500 7.97800  -29.17500 1.000 176.07918 ? 387 LYS A HE3  1 
ATOM   995  H  HZ1  . LYS A 1 68  ? 33.35900 8.18300  -30.77500 1.000 132.68101 ? 387 LYS A HZ1  1 
ATOM   996  H  HZ2  . LYS A 1 68  ? 33.19000 9.61300  -30.57800 1.000 132.68101 ? 387 LYS A HZ2  1 
ATOM   997  H  HZ3  . LYS A 1 68  ? 34.32500 8.92700  -29.98500 1.000 132.68101 ? 387 LYS A HZ3  1 
ATOM   998  N  N    . VAL A 1 69  ? 27.58700 12.39000 -25.94400 1.000 59.58747  ? 388 VAL A N    1 
ATOM   999  C  CA   . VAL A 1 69  ? 27.02000 13.70700 -25.70200 1.000 43.29217  ? 388 VAL A CA   1 
ATOM   1000 C  C    . VAL A 1 69  ? 25.53100 13.53600 -25.46700 1.000 43.54230  ? 388 VAL A C    1 
ATOM   1001 O  O    . VAL A 1 69  ? 24.83800 12.93500 -26.29200 1.000 48.64441  ? 388 VAL A O    1 
ATOM   1002 C  CB   . VAL A 1 69  ? 27.26500 14.65500 -26.89000 1.000 54.26026  ? 388 VAL A CB   1 
ATOM   1003 C  CG1  . VAL A 1 69  ? 26.67700 16.02500 -26.60800 1.000 56.96067  ? 388 VAL A CG1  1 
ATOM   1004 C  CG2  . VAL A 1 69  ? 28.75100 14.74500 -27.20400 1.000 66.93785  ? 388 VAL A CG2  1 
ATOM   1005 H  H    . VAL A 1 69  ? 27.15100 11.92200 -26.51900 1.000 71.60400  ? 388 VAL A H    1 
ATOM   1006 H  HA   . VAL A 1 69  ? 27.44800 14.10500 -24.92800 1.000 51.45544  ? 388 VAL A HA   1 
ATOM   1007 H  HB   . VAL A 1 69  ? 26.81800 14.29500 -27.67200 1.000 65.21135  ? 388 VAL A HB   1 
ATOM   1008 H  HG11 . VAL A 1 69  ? 26.84000 16.60900 -27.36500 1.000 68.45184  ? 388 VAL A HG11 1 
ATOM   1009 H  HG12 . VAL A 1 69  ? 25.72100 15.94400 -26.46200 1.000 68.45184  ? 388 VAL A HG12 1 
ATOM   1010 H  HG13 . VAL A 1 69  ? 27.09300 16.39900 -25.81600 1.000 68.45184  ? 388 VAL A HG13 1 
ATOM   1011 H  HG21 . VAL A 1 69  ? 28.88800 15.34500 -27.95400 1.000 80.42445  ? 388 VAL A HG21 1 
ATOM   1012 H  HG22 . VAL A 1 69  ? 29.22600 15.08300 -26.42900 1.000 80.42445  ? 388 VAL A HG22 1 
ATOM   1013 H  HG23 . VAL A 1 69  ? 29.08800 13.86400 -27.43000 1.000 80.42445  ? 388 VAL A HG23 1 
ATOM   1014 N  N    . SER A 1 70  ? 25.09200 14.07200 -24.33900 1.000 41.24909  ? 389 SER A N    1 
ATOM   1015 C  CA   . SER A 1 70  ? 23.66700 14.01600 -23.97300 1.000 49.50202  ? 389 SER A CA   1 
ATOM   1016 C  C    . SER A 1 70  ? 22.89300 15.02600 -24.80500 1.000 56.65810  ? 389 SER A C    1 
ATOM   1017 O  O    . SER A 1 70  ? 23.49200 15.96000 -25.33800 1.000 38.78864  ? 389 SER A O    1 
ATOM   1018 C  CB   . SER A 1 70  ? 23.49900 14.31600 -22.51600 1.000 51.15068  ? 389 SER A CB   1 
ATOM   1019 O  OG   . SER A 1 70  ? 23.90700 15.64100 -22.22600 1.000 107.35114 ? 389 SER A OG   1 
ATOM   1020 H  H    . SER A 1 70  ? 25.59400 14.47300 -23.76700 1.000 49.00376  ? 389 SER A H    1 
ATOM   1021 H  HA   . SER A 1 70  ? 23.32500 13.12500 -24.14800 1.000 59.50145  ? 389 SER A HA   1 
ATOM   1022 H  HB2  . SER A 1 70  ? 22.57100 14.19600 -22.26100 1.000 61.47984  ? 389 SER A HB2  1 
ATOM   1023 H  HB3  . SER A 1 70  ? 24.02100 13.69000 -21.99000 1.000 61.47984  ? 389 SER A HB3  1 
ATOM   1024 H  HG   . SER A 1 70  ? 24.02300 16.06200 -22.94400 1.000 128.92039 ? 389 SER A HG   1 
ATOM   1025 N  N    . LYS A 1 71  ? 21.58000 14.84500 -24.81700 1.000 43.98885  ? 390 LYS A N    1 
ATOM   1026 C  CA   . LYS A 1 71  ? 20.68800 15.77400 -25.53100 1.000 54.90310  ? 390 LYS A CA   1 
ATOM   1027 C  C    . LYS A 1 71  ? 20.37400 16.98800 -24.66600 1.000 41.62784  ? 390 LYS A C    1 
ATOM   1028 O  O    . LYS A 1 71  ? 20.62900 16.96400 -23.46000 1.000 48.35588  ? 390 LYS A O    1 
ATOM   1029 C  CB   . LYS A 1 71  ? 19.36300 15.07500 -25.81800 1.000 71.68082  ? 390 LYS A CB   1 
ATOM   1030 C  CG   . LYS A 1 71  ? 18.89500 14.11200 -24.73900 1.000 115.62545 ? 390 LYS A CG   1 
ATOM   1031 C  CD   . LYS A 1 71  ? 18.80200 12.68300 -25.22200 1.000 105.92396 ? 390 LYS A CD   1 
ATOM   1032 C  CE   . LYS A 1 71  ? 19.36800 11.68700 -24.23200 1.000 172.07695 ? 390 LYS A CE   1 
ATOM   1033 N  NZ   . LYS A 1 71  ? 20.76000 12.01400 -23.84800 1.000 57.86733  ? 390 LYS A NZ   1 
ATOM   1034 H  H    . LYS A 1 71  ? 21.17800 14.19500 -24.42200 1.000 52.88566  ? 390 LYS A H    1 
ATOM   1035 H  HA   . LYS A 1 71  ? 21.13100 16.05000 -26.34800 1.000 65.98275  ? 390 LYS A HA   1 
ATOM   1036 H  HB2  . LYS A 1 71  ? 18.67900 15.75000 -25.94800 1.000 86.11602  ? 390 LYS A HB2  1 
ATOM   1037 H  HB3  . LYS A 1 71  ? 19.44400 14.58800 -26.65300 1.000 86.11602  ? 390 LYS A HB3  1 
ATOM   1038 H  HG2  . LYS A 1 71  ? 19.50600 14.15500 -23.98700 1.000 138.84957 ? 390 LYS A HG2  1 
ATOM   1039 H  HG3  . LYS A 1 71  ? 18.02600 14.39600 -24.41400 1.000 138.84957 ? 390 LYS A HG3  1 
ATOM   1040 H  HD2  . LYS A 1 71  ? 17.87300 12.46600 -25.39700 1.000 127.20779 ? 390 LYS A HD2  1 
ATOM   1041 H  HD3  . LYS A 1 71  ? 19.27600 12.60000 -26.06400 1.000 127.20779 ? 390 LYS A HD3  1 
ATOM   1042 H  HE2  . LYS A 1 71  ? 18.81000 11.66900 -23.43800 1.000 206.59137 ? 390 LYS A HE2  1 
ATOM   1043 H  HE3  . LYS A 1 71  ? 19.34100 10.79800 -24.61800 1.000 206.59137 ? 390 LYS A HE3  1 
ATOM   1044 H  HZ1  . LYS A 1 71  ? 21.18100 11.27100 -23.59700 1.000 69.53983  ? 390 LYS A HZ1  1 
ATOM   1045 H  HZ2  . LYS A 1 71  ? 21.18300 12.37400 -24.54300 1.000 69.53983  ? 390 LYS A HZ2  1 
ATOM   1046 H  HZ3  . LYS A 1 71  ? 20.75400 12.59400 -23.17300 1.000 69.53983  ? 390 LYS A HZ3  1 
ATOM   1047 N  N    . ALA A 1 72  ? 19.90900 18.01700 -25.34400 1.000 43.67141  ? 391 ALA A N    1 
ATOM   1048 C  CA   . ALA A 1 72  ? 19.49100 19.20000 -24.58300 1.000 41.59154  ? 391 ALA A CA   1 
ATOM   1049 C  C    . ALA A 1 72  ? 18.32700 18.79400 -23.67800 1.000 48.31663  ? 391 ALA A C    1 
ATOM   1050 O  O    . ALA A 1 72  ? 17.66200 17.79700 -23.96100 1.000 40.03051  ? 391 ALA A O    1 
ATOM   1051 C  CB   . ALA A 1 72  ? 19.08900 20.26400 -25.54800 1.000 37.22868  ? 391 ALA A CB   1 
ATOM   1052 H  H    . ALA A 1 72  ? 19.82500 18.06400 -26.19900 1.000 52.50472  ? 391 ALA A H    1 
ATOM   1053 H  HA   . ALA A 1 72  ? 20.20900 19.54500 -24.03000 1.000 50.00888  ? 391 ALA A HA   1 
ATOM   1054 H  HB1  . ALA A 1 72  ? 18.80900 21.05500 -25.06000 1.000 44.77344  ? 391 ALA A HB1  1 
ATOM   1055 H  HB2  . ALA A 1 72  ? 19.84200 20.48600 -26.11800 1.000 44.77344  ? 391 ALA A HB2  1 
ATOM   1056 H  HB3  . ALA A 1 72  ? 18.35400 19.94500 -26.09400 1.000 44.77344  ? 391 ALA A HB3  1 
ATOM   1057 N  N    . CYS A 1 73  ? 18.10900 19.56700 -22.62900 1.000 41.27428  ? 392 CYS A N    1 
ATOM   1058 C  CA   A CYS A 1 73  ? 17.15800 19.22300 -21.58600 0.500 34.01915  ? 392 CYS A CA   1 
ATOM   1059 C  CA   B CYS A 1 73  ? 17.15200 19.22400 -21.58900 0.500 68.38555  ? 392 CYS A CA   1 
ATOM   1060 C  C    . CYS A 1 73  ? 16.01900 20.23300 -21.58400 1.000 36.34541  ? 392 CYS A C    1 
ATOM   1061 O  O    . CYS A 1 73  ? 16.24300 21.43000 -21.77100 1.000 43.35181  ? 392 CYS A O    1 
ATOM   1062 C  CB   A CYS A 1 73  ? 17.84700 19.19200 -20.21600 0.500 38.97246  ? 392 CYS A CB   1 
ATOM   1063 C  CB   B CYS A 1 73  ? 17.80700 19.20300 -20.20800 0.500 48.07878  ? 392 CYS A CB   1 
ATOM   1064 S  SG   A CYS A 1 73  ? 17.17400 17.98600 -19.06400 0.500 46.61463  ? 392 CYS A SG   1 
ATOM   1065 S  SG   B CYS A 1 73  ? 18.96200 17.86900 -19.96900 0.500 46.23802  ? 392 CYS A SG   1 
ATOM   1066 H  H    A CYS A 1 73  ? 18.51300 20.31500 -22.50000 0.500 49.62817  ? 392 CYS A H    1 
ATOM   1067 H  H    B CYS A 1 73  ? 18.51500 20.31300 -22.49700 0.500 49.62817  ? 392 CYS A H    1 
ATOM   1068 H  HA   A CYS A 1 73  ? 16.80100 18.33900 -21.76300 0.500 40.32783  ? 392 CYS A HA   1 
ATOM   1069 H  HA   B CYS A 1 73  ? 16.81200 18.33600 -21.78100 0.500 82.16169  ? 392 CYS A HA   1 
ATOM   1070 H  HB2  A CYS A 1 73  ? 18.79000 19.00600 -20.34600 0.500 46.86598  ? 392 CYS A HB2  1 
ATOM   1071 H  HB2  B CYS A 1 73  ? 18.26700 20.04500 -20.06600 0.500 57.79357  ? 392 CYS A HB2  1 
ATOM   1072 H  HB3  A CYS A 1 73  ? 17.78400 20.07300 -19.81600 0.500 46.86598  ? 392 CYS A HB3  1 
ATOM   1073 H  HB3  B CYS A 1 73  ? 17.11300 19.14200 -19.53300 0.500 57.79357  ? 392 CYS A HB3  1 
ATOM   1074 N  N    . CYS A 1 74  ? 14.80900 19.73700 -21.37800 1.000 37.26361  ? 393 CYS A N    1 
ATOM   1075 C  CA   . CYS A 1 74  ? 13.61400 20.56200 -21.25000 1.000 46.60041  ? 393 CYS A CA   1 
ATOM   1076 C  C    . CYS A 1 74  ? 13.55300 21.09600 -19.82400 1.000 39.10320  ? 393 CYS A C    1 
ATOM   1077 O  O    . CYS A 1 74  ? 13.37000 20.32300 -18.88300 1.000 46.84763  ? 393 CYS A O    1 
ATOM   1078 C  CB   . CYS A 1 74  ? 12.38500 19.71800 -21.57700 1.000 44.22231  ? 393 CYS A CB   1 
ATOM   1079 S  SG   . CYS A 1 74  ? 10.81000 20.53500 -21.34100 1.000 47.04036  ? 393 CYS A SG   1 
ATOM   1080 H  H    . CYS A 1 74  ? 14.65400 18.89400 -21.30700 1.000 44.81536  ? 393 CYS A H    1 
ATOM   1081 H  HA   . CYS A 1 74  ? 13.63900 21.31000 -21.86700 1.000 56.01952  ? 393 CYS A HA   1 
ATOM   1082 H  HB2  . CYS A 1 74  ? 12.44700 19.42800 -22.50100 1.000 53.16581  ? 393 CYS A HB2  1 
ATOM   1083 H  HB3  . CYS A 1 74  ? 12.40400 18.91900 -21.02700 1.000 53.16581  ? 393 CYS A HB3  1 
ATOM   1084 N  N    . VAL A 1 75  ? 13.71300 22.40700 -19.66000 1.000 41.68614  ? 394 VAL A N    1 
ATOM   1085 C  CA   . VAL A 1 75  ? 13.82400 23.03600 -18.34200 1.000 32.95816  ? 394 VAL A CA   1 
ATOM   1086 C  C    . VAL A 1 75  ? 12.99000 24.30700 -18.32000 1.000 37.11015  ? 394 VAL A C    1 
ATOM   1087 O  O    . VAL A 1 75  ? 12.60500 24.83200 -19.37100 1.000 33.28781  ? 394 VAL A O    1 
ATOM   1088 C  CB   . VAL A 1 75  ? 15.28800 23.37800 -17.99500 1.000 40.44803  ? 394 VAL A CB   1 
ATOM   1089 C  CG1  . VAL A 1 75  ? 16.10000 22.10100 -17.78600 1.000 41.86250  ? 394 VAL A CG1  1 
ATOM   1090 C  CG2  . VAL A 1 75  ? 15.88600 24.24300 -19.10200 1.000 42.30123  ? 394 VAL A CG2  1 
ATOM   1091 H  H    . VAL A 1 75  ? 13.76100 22.96200 -20.31500 1.000 50.12240  ? 394 VAL A H    1 
ATOM   1092 H  HA   . VAL A 1 75  ? 13.49900 22.40600 -17.68000 1.000 39.31994  ? 394 VAL A HA   1 
ATOM   1093 H  HB   . VAL A 1 75  ? 15.31400 23.87900 -17.16500 1.000 48.63667  ? 394 VAL A HB   1 
ATOM   1094 H  HG11 . VAL A 1 75  ? 17.01700 22.33200 -17.56900 1.000 50.33404  ? 394 VAL A HG11 1 
ATOM   1095 H  HG12 . VAL A 1 75  ? 15.71500 21.58800 -17.05800 1.000 50.33404  ? 394 VAL A HG12 1 
ATOM   1096 H  HG13 . VAL A 1 75  ? 16.08400 21.57100 -18.59800 1.000 50.33404  ? 394 VAL A HG13 1 
ATOM   1097 H  HG21 . VAL A 1 75  ? 16.80600 24.45800 -18.88400 1.000 50.86051  ? 394 VAL A HG21 1 
ATOM   1098 H  HG22 . VAL A 1 75  ? 15.85800 23.75900 -19.94200 1.000 50.86051  ? 394 VAL A HG22 1 
ATOM   1099 H  HG23 . VAL A 1 75  ? 15.37400 25.06300 -19.18500 1.000 50.86051  ? 394 VAL A HG23 1 
ATOM   1100 N  N    . PRO A 1 76  ? 12.71100 24.83900 -17.12600 1.000 34.60790  ? 395 PRO A N    1 
ATOM   1101 C  CA   . PRO A 1 76  ? 12.07800 26.16200 -17.04600 1.000 35.18783  ? 395 PRO A CA   1 
ATOM   1102 C  C    . PRO A 1 76  ? 13.03700 27.25700 -17.48500 1.000 42.26041  ? 395 PRO A C    1 
ATOM   1103 O  O    . PRO A 1 76  ? 14.19800 27.28800 -17.07300 1.000 35.01207  ? 395 PRO A O    1 
ATOM   1104 C  CB   . PRO A 1 76  ? 11.71100 26.29200 -15.56500 1.000 42.79849  ? 395 PRO A CB   1 
ATOM   1105 C  CG   . PRO A 1 76  ? 11.65900 24.88800 -15.07100 1.000 35.66912  ? 395 PRO A CG   1 
ATOM   1106 C  CD   . PRO A 1 76  ? 12.73200 24.17000 -15.81400 1.000 33.04974  ? 395 PRO A CD   1 
ATOM   1107 H  HA   . PRO A 1 76  ? 11.30900 26.25100 -17.63000 1.000 42.32442  ? 395 PRO A HA   1 
ATOM   1108 H  HB2  . PRO A 1 76  ? 12.37100 26.81300 -15.08200 1.000 51.45722  ? 395 PRO A HB2  1 
ATOM   1109 H  HB3  . PRO A 1 76  ? 10.85800 26.73900 -15.45000 1.000 51.45722  ? 395 PRO A HB3  1 
ATOM   1110 H  HG2  . PRO A 1 76  ? 11.80900 24.84800 -14.11400 1.000 42.90197  ? 395 PRO A HG2  1 
ATOM   1111 H  HG3  . PRO A 1 76  ? 10.79100 24.49000 -15.23900 1.000 42.90197  ? 395 PRO A HG3  1 
ATOM   1112 H  HD2  . PRO A 1 76  ? 13.59400 24.25700 -15.37800 1.000 39.16453  ? 395 PRO A HD2  1 
ATOM   1113 H  HD3  . PRO A 1 76  ? 12.54700 23.22100 -15.88900 1.000 39.16453  ? 395 PRO A HD3  1 
ATOM   1114 N  N    . THR A 1 77  ? 12.54400 28.15400 -18.34200 1.000 34.77032  ? 396 THR A N    1 
ATOM   1115 C  CA   . THR A 1 77  ? 13.32400 29.28900 -18.82300 1.000 43.67598  ? 396 THR A CA   1 
ATOM   1116 C  C    . THR A 1 77  ? 12.85100 30.60900 -18.24000 1.000 47.68876  ? 396 THR A C    1 
ATOM   1117 O  O    . THR A 1 77  ? 13.55900 31.61400 -18.36600 1.000 47.06023  ? 396 THR A O    1 
ATOM   1118 C  CB   . THR A 1 77  ? 13.27600 29.36500 -20.35400 1.000 38.64311  ? 396 THR A CB   1 
ATOM   1119 O  OG1  . THR A 1 77  ? 11.91000 29.38700 -20.76200 1.000 39.32527  ? 396 THR A OG1  1 
ATOM   1120 C  CG2  . THR A 1 77  ? 13.95600 28.13800 -20.96800 1.000 37.19653  ? 396 THR A CG2  1 
ATOM   1121 H  H    . THR A 1 77  ? 11.74600 28.11800 -18.66000 1.000 41.22923  ? 396 THR A H    1 
ATOM   1122 H  HA   . THR A 1 77  ? 14.23600 29.14300 -18.52700 1.000 52.51021  ? 396 THR A HA   1 
ATOM   1123 H  HB   . THR A 1 77  ? 13.73800 30.16400 -20.65200 1.000 46.47076  ? 396 THR A HB   1 
ATOM   1124 H  HG1  . THR A 1 77  ? 11.42100 29.16600 -20.11600 1.000 47.28936  ? 396 THR A HG1  1 
ATOM   1125 H  HG21 . THR A 1 77  ? 13.91900 28.19800 -21.93500 1.000 44.73487  ? 396 THR A HG21 1 
ATOM   1126 H  HG22 . THR A 1 77  ? 14.88200 28.10400 -20.68200 1.000 44.73487  ? 396 THR A HG22 1 
ATOM   1127 H  HG23 . THR A 1 77  ? 13.49800 27.33400 -20.67600 1.000 44.73487  ? 396 THR A HG23 1 
ATOM   1128 N  N    . LYS A 1 78  ? 11.69100 30.62700 -17.59000 1.000 40.41977  ? 397 LYS A N    1 
ATOM   1129 C  CA   . LYS A 1 78  ? 11.21500 31.79800 -16.87000 1.000 54.14291  ? 397 LYS A CA   1 
ATOM   1130 C  C    . LYS A 1 78  ? 10.38200 31.33100 -15.68700 1.000 42.31620  ? 397 LYS A C    1 
ATOM   1131 O  O    . LYS A 1 78  ? 9.59200  30.39400 -15.82200 1.000 37.38982  ? 397 LYS A O    1 
ATOM   1132 C  CB   . LYS A 1 78  ? 10.37400 32.71600 -17.77100 1.000 47.86193  ? 397 LYS A CB   1 
ATOM   1133 C  CG   . LYS A 1 78  ? 9.91900  34.01100 -17.08000 1.000 64.07825  ? 397 LYS A CG   1 
ATOM   1134 C  CD   . LYS A 1 78  ? 9.02700  34.83300 -18.00100 1.000 110.07586 ? 397 LYS A CD   1 
ATOM   1135 C  CE   . LYS A 1 78  ? 8.66100  36.17300 -17.38900 1.000 70.34143  ? 397 LYS A CE   1 
ATOM   1136 N  NZ   . LYS A 1 78  ? 7.86700  36.99600 -18.35500 1.000 124.58636 ? 397 LYS A NZ   1 
ATOM   1137 H  H    . LYS A 1 78  ? 11.15600 29.95400 -17.55600 1.000 48.60275  ? 397 LYS A H    1 
ATOM   1138 H  HA   . LYS A 1 78  ? 11.98100 32.31100 -16.56800 1.000 65.07052  ? 397 LYS A HA   1 
ATOM   1139 H  HB2  . LYS A 1 78  ? 10.89100 32.94400 -18.55900 1.000 57.53335  ? 397 LYS A HB2  1 
ATOM   1140 H  HB3  . LYS A 1 78  ? 9.59200  32.22900 -18.07500 1.000 57.53335  ? 397 LYS A HB3  1 
ATOM   1141 H  HG2  . LYS A 1 78  ? 9.43800  33.79600 -16.26500 1.000 76.99294  ? 397 LYS A HG2  1 
ATOM   1142 H  HG3  . LYS A 1 78  ? 10.69400 34.53400 -16.82200 1.000 76.99294  ? 397 LYS A HG3  1 
ATOM   1143 H  HD2  . LYS A 1 78  ? 9.48100  34.97700 -18.84600 1.000 132.19007 ? 397 LYS A HD2  1 
ATOM   1144 H  HD3  . LYS A 1 78  ? 8.21800  34.33500 -18.19500 1.000 132.19007 ? 397 LYS A HD3  1 
ATOM   1145 H  HE2  . LYS A 1 78  ? 8.14800  36.03400 -16.57700 1.000 84.50875  ? 397 LYS A HE2  1 
ATOM   1146 H  HE3  . LYS A 1 78  ? 9.46700  36.65000 -17.13700 1.000 84.50875  ? 397 LYS A HE3  1 
ATOM   1147 H  HZ1  . LYS A 1 78  ? 8.18600  37.82700 -18.37000 1.000 149.60266 ? 397 LYS A HZ1  1 
ATOM   1148 H  HZ2  . LYS A 1 78  ? 7.92800  36.64000 -19.16900 1.000 149.60266 ? 397 LYS A HZ2  1 
ATOM   1149 H  HZ3  . LYS A 1 78  ? 7.01400  37.01100 -18.10100 1.000 149.60266 ? 397 LYS A HZ3  1 
ATOM   1150 N  N    . LEU A 1 79  ? 10.51900 32.02000 -14.54800 1.000 37.66803  ? 398 LEU A N    1 
ATOM   1151 C  CA   . LEU A 1 79  ? 9.83700  31.64800 -13.31500 1.000 40.21771  ? 398 LEU A CA   1 
ATOM   1152 C  C    . LEU A 1 79  ? 8.99700  32.80500 -12.78500 1.000 38.49801  ? 398 LEU A C    1 
ATOM   1153 O  O    . LEU A 1 79  ? 9.29500  33.97600 -13.03000 1.000 49.36778  ? 398 LEU A O    1 
ATOM   1154 C  CB   . LEU A 1 79  ? 10.85200 31.21400 -12.24500 1.000 46.99733  ? 398 LEU A CB   1 
ATOM   1155 C  CG   . LEU A 1 79  ? 11.80800 30.08100 -12.64100 1.000 41.41425  ? 398 LEU A CG   1 
ATOM   1156 C  CD1  . LEU A 1 79  ? 12.83200 29.92800 -11.55000 1.000 43.66517  ? 398 LEU A CD1  1 
ATOM   1157 C  CD2  . LEU A 1 79  ? 11.06400 28.76800 -12.86300 1.000 35.10461  ? 398 LEU A CD2  1 
ATOM   1158 H  H    . LEU A 1 79  ? 11.01400 32.71900 -14.47500 1.000 45.30067  ? 398 LEU A H    1 
ATOM   1159 H  HA   . LEU A 1 79  ? 9.24900  30.90300 -13.51600 1.000 48.36029  ? 398 LEU A HA   1 
ATOM   1160 H  HB2  . LEU A 1 79  ? 11.38200 31.98700 -11.99500 1.000 56.49583  ? 398 LEU A HB2  1 
ATOM   1161 H  HB3  . LEU A 1 79  ? 10.36300 30.93800 -11.45400 1.000 56.49583  ? 398 LEU A HB3  1 
ATOM   1162 H  HG   . LEU A 1 79  ? 12.23900 30.30600 -13.48100 1.000 49.79614  ? 398 LEU A HG   1 
ATOM   1163 H  HD11 . LEU A 1 79  ? 13.44800 29.21500 -11.78100 1.000 52.49723  ? 398 LEU A HD11 1 
ATOM   1164 H  HD12 . LEU A 1 79  ? 13.32300 30.75800 -11.44800 1.000 52.49723  ? 398 LEU A HD12 1 
ATOM   1165 H  HD13 . LEU A 1 79  ? 12.38700 29.71200 -10.71600 1.000 52.49723  ? 398 LEU A HD13 1 
ATOM   1166 H  HD21 . LEU A 1 79  ? 11.69600 28.07600 -13.11100 1.000 41.63037  ? 398 LEU A HD21 1 
ATOM   1167 H  HD22 . LEU A 1 79  ? 10.60900 28.51200 -12.04600 1.000 41.63037  ? 398 LEU A HD22 1 
ATOM   1168 H  HD23 . LEU A 1 79  ? 10.41300 28.88100 -13.57300 1.000 41.63037  ? 398 LEU A HD23 1 
ATOM   1169 N  N    . SER A 1 80  ? 7.94000  32.46500 -12.05200 1.000 44.52191  ? 399 SER A N    1 
ATOM   1170 C  CA   . SER A 1 80  ? 7.03200  33.43200 -11.45300 1.000 47.29415  ? 399 SER A CA   1 
ATOM   1171 C  C    . SER A 1 80  ? 7.02300  33.29600 -9.93200  1.000 45.52260  ? 399 SER A C    1 
ATOM   1172 O  O    . SER A 1 80  ? 7.28000  32.21200 -9.40700  1.000 39.76199  ? 399 SER A O    1 
ATOM   1173 C  CB   . SER A 1 80  ? 5.60300  33.24800 -11.97700 1.000 48.16263  ? 399 SER A CB   1 
ATOM   1174 O  OG   . SER A 1 80  ? 5.53500  33.54700 -13.36400 1.000 58.68798  ? 399 SER A OG   1 
ATOM   1175 H  H    . SER A 1 80  ? 7.72800  31.64800 -11.88700 1.000 53.52533  ? 399 SER A H    1 
ATOM   1176 H  HA   . SER A 1 80  ? 7.35000  34.31500 -11.69800 1.000 56.85202  ? 399 SER A HA   1 
ATOM   1177 H  HB2  . SER A 1 80  ? 5.31200  32.33500 -11.82300 1.000 57.89418  ? 399 SER A HB2  1 
ATOM   1178 H  HB3  . SER A 1 80  ? 4.99700  33.82500 -11.48700 1.000 57.89418  ? 399 SER A HB3  1 
ATOM   1179 H  HG   . SER A 1 80  ? 4.74700  33.44000 -13.63600 1.000 70.52461  ? 399 SER A HG   1 
ATOM   1180 N  N    . PRO A 1 81  ? 6.71700  34.36800 -9.20200  1.000 43.91920  ? 400 PRO A N    1 
ATOM   1181 C  CA   . PRO A 1 81  ? 6.64700  34.27900 -7.73700  1.000 48.57568  ? 400 PRO A CA   1 
ATOM   1182 C  C    . PRO A 1 81  ? 5.29200  33.78100 -7.25300  1.000 51.49236  ? 400 PRO A C    1 
ATOM   1183 O  O    . PRO A 1 81  ? 4.33100  33.63100 -8.00700  1.000 48.62622  ? 400 PRO A O    1 
ATOM   1184 C  CB   . PRO A 1 81  ? 6.88700  35.71600 -7.28100  1.000 47.25903  ? 400 PRO A CB   1 
ATOM   1185 C  CG   . PRO A 1 81  ? 6.32000  36.54300 -8.43700  1.000 49.28395  ? 400 PRO A CG   1 
ATOM   1186 C  CD   . PRO A 1 81  ? 6.65900  35.76400 -9.67900  1.000 53.50879  ? 400 PRO A CD   1 
ATOM   1187 H  HA   . PRO A 1 81  ? 7.29000  33.64600 -7.38000  1.000 58.38985  ? 400 PRO A HA   1 
ATOM   1188 H  HB2  . PRO A 1 81  ? 6.43300  35.90800 -6.44500  1.000 56.80986  ? 400 PRO A HB2  1 
ATOM   1189 H  HB3  . PRO A 1 81  ? 7.83000  35.89500 -7.14000  1.000 56.80986  ? 400 PRO A HB3  1 
ATOM   1190 H  HG2  . PRO A 1 81  ? 5.36100  36.66000 -8.34700  1.000 59.23977  ? 400 PRO A HG2  1 
ATOM   1191 H  HG3  . PRO A 1 81  ? 6.71300  37.42900 -8.46000  1.000 59.23977  ? 400 PRO A HG3  1 
ATOM   1192 H  HD2  . PRO A 1 81  ? 5.98600  35.87900 -10.36800 1.000 64.30957  ? 400 PRO A HD2  1 
ATOM   1193 H  HD3  . PRO A 1 81  ? 7.50500  36.04700 -10.05900 1.000 64.30957  ? 400 PRO A HD3  1 
ATOM   1194 N  N    . ILE A 1 82  ? 5.25000  33.48600 -5.95400  1.000 45.98935  ? 401 ILE A N    1 
ATOM   1195 C  CA   . ILE A 1 82  ? 4.01900  33.23000 -5.22700  1.000 46.71618  ? 401 ILE A CA   1 
ATOM   1196 C  C    . ILE A 1 82  ? 4.11500  33.96800 -3.90100  1.000 56.76478  ? 401 ILE A C    1 
ATOM   1197 O  O    . ILE A 1 82  ? 5.15200  34.52900 -3.54400  1.000 56.26178  ? 401 ILE A O    1 
ATOM   1198 C  CB   . ILE A 1 82  ? 3.75000  31.73200 -4.97200  1.000 47.88331  ? 401 ILE A CB   1 
ATOM   1199 C  CG1  . ILE A 1 82  ? 4.74800  31.17800 -3.93800  1.000 51.90526  ? 401 ILE A CG1  1 
ATOM   1200 C  CG2  . ILE A 1 82  ? 3.77600  30.95100 -6.26700  1.000 52.09379  ? 401 ILE A CG2  1 
ATOM   1201 C  CD1  . ILE A 1 82  ? 4.36500  29.81600 -3.37500  1.000 46.45134  ? 401 ILE A CD1  1 
ATOM   1202 H  H    . ILE A 1 82  ? 5.95500  33.42900 -5.46500  1.000 55.28625  ? 401 ILE A H    1 
ATOM   1203 H  HA   . ILE A 1 82  ? 3.27700  33.54200 -5.76800  1.000 56.15845  ? 401 ILE A HA   1 
ATOM   1204 H  HB   . ILE A 1 82  ? 2.86000  31.63200 -4.60100  1.000 57.55901  ? 401 ILE A HB   1 
ATOM   1205 H  HG12 . ILE A 1 82  ? 5.62400  31.11300 -4.35000  1.000 62.38534  ? 401 ILE A HG12 1 
ATOM   1206 H  HG13 . ILE A 1 82  ? 4.82500  31.81000 -3.20600  1.000 62.38534  ? 401 ILE A HG13 1 
ATOM   1207 H  HG21 . ILE A 1 82  ? 3.60500  30.01400 -6.08400  1.000 62.61158  ? 401 ILE A HG21 1 
ATOM   1208 H  HG22 . ILE A 1 82  ? 3.09300  31.29300 -6.86500  1.000 62.61158  ? 401 ILE A HG22 1 
ATOM   1209 H  HG23 . ILE A 1 82  ? 4.64700  31.04500 -6.68400  1.000 62.61158  ? 401 ILE A HG23 1 
ATOM   1210 H  HD11 . ILE A 1 82  ? 5.03500  29.53100 -2.73400  1.000 55.84064  ? 401 ILE A HD11 1 
ATOM   1211 H  HD12 . ILE A 1 82  ? 3.50300  29.87800 -2.93500  1.000 55.84064  ? 401 ILE A HD12 1 
ATOM   1212 H  HD13 . ILE A 1 82  ? 4.31300  29.17000 -4.09700  1.000 55.84064  ? 401 ILE A HD13 1 
ATOM   1213 N  N    . SER A 1 83  ? 3.01200  33.97200 -3.17600  1.000 55.29704  ? 402 SER A N    1 
ATOM   1214 C  CA   . SER A 1 83  ? 2.95600  34.58100 -1.86100  1.000 50.56341  ? 402 SER A CA   1 
ATOM   1215 C  C    . SER A 1 83  ? 2.93600  33.46700 -0.83800  1.000 44.24863  ? 402 SER A C    1 
ATOM   1216 O  O    . SER A 1 83  ? 2.17400  32.50000 -0.97600  1.000 53.56753  ? 402 SER A O    1 
ATOM   1217 C  CB   . SER A 1 83  ? 1.73200  35.48500 -1.73500  1.000 57.42864  ? 402 SER A CB   1 
ATOM   1218 O  OG   . SER A 1 83  ? 1.84100  36.57300 -2.63000  1.000 56.80495  ? 402 SER A OG   1 
ATOM   1219 H  H    . SER A 1 83  ? 2.27100  33.62000 -3.43300  1.000 66.45548  ? 402 SER A H    1 
ATOM   1220 H  HA   . SER A 1 83  ? 3.73100  35.14500 -1.71300  1.000 60.77512  ? 402 SER A HA   1 
ATOM   1221 H  HB2  . SER A 1 83  ? 0.92600  34.98000 -1.92500  1.000 69.01340  ? 402 SER A HB2  1 
ATOM   1222 H  HB3  . SER A 1 83  ? 1.65400  35.81200 -0.82500  1.000 69.01340  ? 402 SER A HB3  1 
ATOM   1223 H  HG   . SER A 1 83  ? 2.45100  37.08900 -2.37100  1.000 68.26497  ? 402 SER A HG   1 
ATOM   1224 N  N    . VAL A 1 84  ? 3.78600  33.59800 0.16900   1.000 51.80578  ? 403 VAL A N    1 
ATOM   1225 C  CA   . VAL A 1 84  ? 3.84300  32.63500 1.25800   1.000 49.17753  ? 403 VAL A CA   1 
ATOM   1226 C  C    . VAL A 1 84  ? 3.71900  33.37100 2.58500   1.000 75.78759  ? 403 VAL A C    1 
ATOM   1227 O  O    . VAL A 1 84  ? 4.23500  34.48700 2.75100   1.000 47.54208  ? 403 VAL A O    1 
ATOM   1228 C  CB   . VAL A 1 84  ? 5.13600  31.79600 1.20700   1.000 43.09673  ? 403 VAL A CB   1 
ATOM   1229 C  CG1  . VAL A 1 84  ? 5.26000  31.10100 -0.18500  1.000 51.89813  ? 403 VAL A CG1  1 
ATOM   1230 C  CG2  . VAL A 1 84  ? 6.34300  32.66400 1.47100   1.000 61.06061  ? 403 VAL A CG2  1 
ATOM   1231 H  H    . VAL A 1 84  ? 4.34600  34.24700 0.24100   1.000 62.26596  ? 403 VAL A H    1 
ATOM   1232 H  HA   . VAL A 1 84  ? 3.10300  32.01500 1.16500   1.000 59.11207  ? 403 VAL A HA   1 
ATOM   1233 H  HB   . VAL A 1 84  ? 5.09500  31.11600 1.89700   1.000 51.81510  ? 403 VAL A HB   1 
ATOM   1234 H  HG11 . VAL A 1 84  ? 6.07400  30.57500 -0.21300  1.000 62.37679  ? 403 VAL A HG11 1 
ATOM   1235 H  HG12 . VAL A 1 84  ? 4.49600  30.52100 -0.32700  1.000 62.37679  ? 403 VAL A HG12 1 
ATOM   1236 H  HG13 . VAL A 1 84  ? 5.28700  31.77500 -0.88200  1.000 62.37679  ? 403 VAL A HG13 1 
ATOM   1237 H  HG21 . VAL A 1 84  ? 7.14600  32.12100 1.43500   1.000 73.37176  ? 403 VAL A HG21 1 
ATOM   1238 H  HG22 . VAL A 1 84  ? 6.39400  33.36100 0.79800   1.000 73.37176  ? 403 VAL A HG22 1 
ATOM   1239 H  HG23 . VAL A 1 84  ? 6.26500  33.06800 2.34900   1.000 73.37176  ? 403 VAL A HG23 1 
ATOM   1240 N  N    . LEU A 1 85  ? 3.05900  32.69000 3.52500   1.000 55.42863  ? 404 LEU A N    1 
ATOM   1241 C  CA   . LEU A 1 85  ? 2.99000  33.17800 4.92000   1.000 59.72520  ? 404 LEU A CA   1 
ATOM   1242 C  C    . LEU A 1 85  ? 4.00700  32.33200 5.67800   1.000 71.25870  ? 404 LEU A C    1 
ATOM   1243 O  O    . LEU A 1 85  ? 3.81300  31.11500 5.75100   1.000 61.52331  ? 404 LEU A O    1 
ATOM   1244 C  CB   . LEU A 1 85  ? 1.58400  33.03400 5.49700   1.000 56.54661  ? 404 LEU A CB   1 
ATOM   1245 C  CG   . LEU A 1 85  ? 1.39100  33.43400 6.96100   1.000 71.43580  ? 404 LEU A CG   1 
ATOM   1246 C  CD1  . LEU A 1 85  ? 1.66500  34.91600 7.15700   1.000 65.06889  ? 404 LEU A CD1  1 
ATOM   1247 C  CD2  . LEU A 1 85  ? -0.01000 33.07700 7.43500   1.000 49.11174  ? 404 LEU A CD2  1 
ATOM   1248 H  H    . LEU A 1 85  ? 2.64600  31.94900 3.38400   1.000 66.61339  ? 404 LEU A H    1 
ATOM   1249 H  HA   . LEU A 1 85  ? 3.19000  34.12500 4.98600   1.000 71.76927  ? 404 LEU A HA   1 
ATOM   1250 H  HB2  . LEU A 1 85  ? 0.98000  33.56700 4.95700   1.000 67.95496  ? 404 LEU A HB2  1 
ATOM   1251 H  HB3  . LEU A 1 85  ? 1.31100  32.10800 5.39900   1.000 67.95496  ? 404 LEU A HB3  1 
ATOM   1252 H  HG   . LEU A 1 85  ? 2.02900  32.93700 7.49700   1.000 85.82199  ? 404 LEU A HG   1 
ATOM   1253 H  HD11 . LEU A 1 85  ? 1.53700  35.14800 8.09000   1.000 78.18170  ? 404 LEU A HD11 1 
ATOM   1254 H  HD12 . LEU A 1 85  ? 2.57800  35.11400 6.89700   1.000 78.18170  ? 404 LEU A HD12 1 
ATOM   1255 H  HD13 . LEU A 1 85  ? 1.05400  35.43300 6.60900   1.000 78.18170  ? 404 LEU A HD13 1 
ATOM   1256 H  HD21 . LEU A 1 85  ? -0.11400 33.33700 8.36400   1.000 59.03312  ? 404 LEU A HD21 1 
ATOM   1257 H  HD22 . LEU A 1 85  ? -0.66400 33.54500 6.89300   1.000 59.03312  ? 404 LEU A HD22 1 
ATOM   1258 H  HD23 . LEU A 1 85  ? -0.14600 32.12000 7.35100   1.000 59.03312  ? 404 LEU A HD23 1 
ATOM   1259 N  N    . TYR A 1 86  ? 5.10400  32.96900 6.07500   1.000 74.75296  ? 405 TYR A N    1 
ATOM   1260 C  CA   . TYR A 1 86  ? 6.23400  32.20000 6.62900   1.000 74.40203  ? 405 TYR A CA   1 
ATOM   1261 C  C    . TYR A 1 86  ? 6.61300  32.55300 8.05900   1.000 83.88433  ? 405 TYR A C    1 
ATOM   1262 O  O    . TYR A 1 86  ? 6.19400  33.60600 8.57600   1.000 75.27361  ? 405 TYR A O    1 
ATOM   1263 C  CB   . TYR A 1 86  ? 7.49200  32.49600 5.81800   1.000 85.35075  ? 405 TYR A CB   1 
ATOM   1264 C  CG   . TYR A 1 86  ? 8.05900  33.88500 5.94400   1.000 71.39647  ? 405 TYR A CG   1 
ATOM   1265 C  CD1  . TYR A 1 86  ? 7.61600  34.91000 5.13000   1.000 67.58814  ? 405 TYR A CD1  1 
ATOM   1266 C  CD2  . TYR A 1 86  ? 9.07900  34.16100 6.83700   1.000 71.14670  ? 405 TYR A CD2  1 
ATOM   1267 C  CE1  . TYR A 1 86  ? 8.14600  36.18400 5.22300   1.000 81.45299  ? 405 TYR A CE1  1 
ATOM   1268 C  CE2  . TYR A 1 86  ? 9.61900  35.42900 6.94500   1.000 92.18252  ? 405 TYR A CE2  1 
ATOM   1269 C  CZ   . TYR A 1 86  ? 9.15200  36.44400 6.13300   1.000 69.02114  ? 405 TYR A CZ   1 
ATOM   1270 O  OH   . TYR A 1 86  ? 9.68600  37.70200 6.22900   1.000 104.81141 ? 405 TYR A OH   1 
ATOM   1271 H  H    . TYR A 1 86  ? 5.22100  33.82000 6.03800   1.000 89.80258  ? 405 TYR A H    1 
ATOM   1272 H  HA   . TYR A 1 86  ? 5.93500  31.27800 6.59700   1.000 89.38147  ? 405 TYR A HA   1 
ATOM   1273 H  HB2  . TYR A 1 86  ? 8.17800  31.86300 6.08000   1.000 102.51993 ? 405 TYR A HB2  1 
ATOM   1274 H  HB3  . TYR A 1 86  ? 7.29600  32.33100 4.88200   1.000 102.51993 ? 405 TYR A HB3  1 
ATOM   1275 H  HD1  . TYR A 1 86  ? 6.94700  34.74000 4.50600   1.000 81.20480  ? 405 TYR A HD1  1 
ATOM   1276 H  HD2  . TYR A 1 86  ? 9.40900  33.47900 7.37600   1.000 85.47507  ? 405 TYR A HD2  1 
ATOM   1277 H  HE1  . TYR A 1 86  ? 7.82600  36.86400 4.67500   1.000 97.84262  ? 405 TYR A HE1  1 
ATOM   1278 H  HE2  . TYR A 1 86  ? 10.29400 35.59800 7.56200   1.000 110.71806 ? 405 TYR A HE2  1 
ATOM   1279 H  HH   . TYR A 1 86  ? 9.07300  38.27300 6.16100   1.000 125.87273 ? 405 TYR A HH   1 
ATOM   1280 N  N    . LYS A 1 87  ? 7.43500  31.67800 8.64100   1.000 186.33899 ? 406 LYS A N    1 
ATOM   1281 C  CA   . LYS A 1 87  ? 7.88900  31.86600 10.03900  1.000 84.10656  ? 406 LYS A CA   1 
ATOM   1282 C  C    . LYS A 1 87  ? 9.23700  32.58900 10.03400  1.000 155.09759 ? 406 LYS A C    1 
ATOM   1283 O  O    . LYS A 1 87  ? 10.22700 31.98200 9.60100   1.000 88.89907  ? 406 LYS A O    1 
ATOM   1284 C  CB   . LYS A 1 87  ? 7.88000  30.53100 10.78400  1.000 149.35563 ? 406 LYS A CB   1 
ATOM   1285 C  CG   . LYS A 1 87  ? 6.50000  29.95200 11.05600  1.000 129.71914 ? 406 LYS A CG   1 
ATOM   1286 C  CD   . LYS A 1 87  ? 6.56000  28.57000 11.66200  1.000 88.77131  ? 406 LYS A CD   1 
ATOM   1287 C  CE   . LYS A 1 87  ? 7.37300  28.52300 12.93800  1.000 131.68166 ? 406 LYS A CE   1 
ATOM   1288 N  NZ   . LYS A 1 87  ? 8.12600  27.25300 13.06300  1.000 114.24514 ? 406 LYS A NZ   1 
ATOM   1289 H  H    . LYS A 1 87  ? 7.74300  30.97400 8.25500   1.000 223.70581 ? 406 LYS A H    1 
ATOM   1290 H  HA   . LYS A 1 87  ? 7.27700  32.43300 10.53300  1.000 101.02690 ? 406 LYS A HA   1 
ATOM   1291 H  HB2  . LYS A 1 87  ? 8.39000  29.88600 10.26900  1.000 179.32578 ? 406 LYS A HB2  1 
ATOM   1292 H  HB3  . LYS A 1 87  ? 8.34000  30.64600 11.63000  1.000 179.32578 ? 406 LYS A HB3  1 
ATOM   1293 H  HG2  . LYS A 1 87  ? 6.01700  30.54300 11.65400  1.000 155.76200 ? 406 LYS A HG2  1 
ATOM   1294 H  HG3  . LYS A 1 87  ? 5.99900  29.91600 10.22600  1.000 155.76200 ? 406 LYS A HG3  1 
ATOM   1295 H  HD2  . LYS A 1 87  ? 5.65900  28.26300 11.84600  1.000 106.62460 ? 406 LYS A HD2  1 
ATOM   1296 H  HD3  . LYS A 1 87  ? 6.94300  27.95500 11.01700  1.000 106.62460 ? 406 LYS A HD3  1 
ATOM   1297 H  HE2  . LYS A 1 87  ? 7.99200  29.26900 12.95500  1.000 158.11703 ? 406 LYS A HE2  1 
ATOM   1298 H  HE3  . LYS A 1 87  ? 6.78300  28.62600 13.70100  1.000 158.11703 ? 406 LYS A HE3  1 
ATOM   1299 H  HZ1  . LYS A 1 87  ? 8.92000  27.41300 13.43200  1.000 137.19320 ? 406 LYS A HZ1  1 
ATOM   1300 H  HZ2  . LYS A 1 87  ? 7.67000  26.68600 13.57600  1.000 137.19320 ? 406 LYS A HZ2  1 
ATOM   1301 H  HZ3  . LYS A 1 87  ? 8.24100  26.89500 12.25600  1.000 137.19320 ? 406 LYS A HZ3  1 
ATOM   1302 N  N    . ASP A 1 88  ? 9.27600  33.85600 10.46200  1.000 74.14211  ? 407 ASP A N    1 
ATOM   1303 C  CA   . ASP A 1 88  ? 10.54100 34.64200 10.39100  1.000 174.96867 ? 407 ASP A CA   1 
ATOM   1304 C  C    . ASP A 1 88  ? 11.51200 34.16000 11.48100  1.000 135.65817 ? 407 ASP A C    1 
ATOM   1305 O  O    . ASP A 1 88  ? 11.09600 33.33300 12.31300  1.000 101.86122 ? 407 ASP A O    1 
ATOM   1306 C  CB   . ASP A 1 88  ? 10.26200 36.14700 10.44700  1.000 72.89209  ? 407 ASP A CB   1 
ATOM   1307 C  CG   . ASP A 1 88  ? 9.57600  36.59800 11.72400  1.000 125.69175 ? 407 ASP A CG   1 
ATOM   1308 O  OD1  . ASP A 1 88  ? 9.24200  35.72800 12.54900  1.000 114.15124 ? 407 ASP A OD1  1 
ATOM   1309 O  OD2  . ASP A 1 88  ? 9.37900  37.81800 11.87500  1.000 111.94629 ? 407 ASP A OD2  1 
ATOM   1310 H  H    . ASP A 1 88  ? 8.60400  34.28000 10.79100  1.000 89.06956  ? 407 ASP A H    1 
ATOM   1311 H  HA   . ASP A 1 88  ? 10.97100 34.48900 9.53500   1.000 210.06143 ? 407 ASP A HA   1 
ATOM   1312 H  HB2  . ASP A 1 88  ? 11.10000 36.62600 10.35400  1.000 87.56954  ? 407 ASP A HB2  1 
ATOM   1313 H  HB3  . ASP A 1 88  ? 9.70900  36.39300 9.68900   1.000 87.56954  ? 407 ASP A HB3  1 
ATOM   1314 N  N    . ASP A 1 89  ? 12.75600 34.65300 11.48200  1.000 178.84849 ? 408 ASP A N    1 
ATOM   1315 C  CA   . ASP A 1 89  ? 13.67800 34.22800 12.53500  1.000 161.49638 ? 408 ASP A CA   1 
ATOM   1316 C  C    . ASP A 1 89  ? 13.06300 34.44100 13.90900  1.000 130.09115 ? 408 ASP A C    1 
ATOM   1317 O  O    . ASP A 1 89  ? 13.18300 33.58200 14.78900  1.000 122.66494 ? 408 ASP A O    1 
ATOM   1318 C  CB   . ASP A 1 89  ? 15.01100 34.97100 12.41800  1.000 107.18649 ? 408 ASP A CB   1 
ATOM   1319 C  CG   . ASP A 1 89  ? 15.98900 34.27400 11.47500  1.000 167.30731 ? 408 ASP A CG   1 
ATOM   1320 O  OD1  . ASP A 1 89  ? 15.74300 33.09600 11.11900  1.000 144.38537 ? 408 ASP A OD1  1 
ATOM   1321 O  OD2  . ASP A 1 89  ? 17.00500 34.90300 11.09100  1.000 168.67485 ? 408 ASP A OD2  1 
ATOM   1322 H  H    . ASP A 1 89  ? 13.07300 35.21000 10.90800  1.000 214.71721 ? 408 ASP A H    1 
ATOM   1323 H  HA   . ASP A 1 89  ? 13.84800 33.27900 12.42400  1.000 193.89469 ? 408 ASP A HA   1 
ATOM   1324 H  HB2  . ASP A 1 89  ? 14.84800 35.87300 12.10100  1.000 128.72282 ? 408 ASP A HB2  1 
ATOM   1325 H  HB3  . ASP A 1 89  ? 15.41300 35.04800 13.29700  1.000 128.72282 ? 408 ASP A HB3  1 
ATOM   1326 N  N    . MET A 1 90  ? 12.36400 35.56600 14.09500  1.000 101.65319 ? 409 MET A N    1 
ATOM   1327 C  CA   . MET A 1 90  ? 11.66600 35.85200 15.34300  1.000 132.12319 ? 409 MET A CA   1 
ATOM   1328 C  C    . MET A 1 90  ? 10.45400 34.94700 15.56800  1.000 146.66340 ? 409 MET A C    1 
ATOM   1329 O  O    . MET A 1 90  ? 9.95600  34.87200 16.69900  1.000 113.22260 ? 409 MET A O    1 
ATOM   1330 C  CB   . MET A 1 90  ? 11.24500 37.32100 15.35500  1.000 120.46718 ? 409 MET A CB   1 
ATOM   1331 C  CG   . MET A 1 90  ? 10.72400 37.82500 16.68500  1.000 155.12826 ? 409 MET A CG   1 
ATOM   1332 S  SD   . MET A 1 90  ? 10.30300 39.57200 16.58900  1.000 206.65995 ? 409 MET A SD   1 
ATOM   1333 C  CE   . MET A 1 90  ? 11.86600 40.28000 16.05400  1.000 154.89910 ? 409 MET A CE   1 
ATOM   1334 H  H    . MET A 1 90  ? 12.28400 36.18100 13.49900  1.000 122.08286 ? 409 MET A H    1 
ATOM   1335 H  HA   . MET A 1 90  ? 12.27900 35.67200 16.07200  1.000 158.64686 ? 409 MET A HA   1 
ATOM   1336 H  HB2  . MET A 1 90  ? 12.00500 37.86400 15.09400  1.000 144.65965 ? 409 MET A HB2  1 
ATOM   1337 H  HB3  . MET A 1 90  ? 10.55800 37.45200 14.68300  1.000 144.65965 ? 409 MET A HB3  1 
ATOM   1338 H  HG2  . MET A 1 90  ? 9.94200  37.31400 16.94500  1.000 186.25294 ? 409 MET A HG2  1 
ATOM   1339 H  HG3  . MET A 1 90  ? 11.39400 37.68700 17.37200  1.000 186.25294 ? 409 MET A HG3  1 
ATOM   1340 H  HE1  . MET A 1 90  ? 11.77200 41.24100 15.96200  1.000 185.97796 ? 409 MET A HE1  1 
ATOM   1341 H  HE2  . MET A 1 90  ? 12.55200 40.08400 16.71100  1.000 185.97796 ? 409 MET A HE2  1 
ATOM   1342 H  HE3  . MET A 1 90  ? 12.11900 39.89700 15.19900  1.000 185.97796 ? 409 MET A HE3  1 
ATOM   1343 N  N    . GLY A 1 91  ? 9.96000  34.27600 14.52600  1.000 126.23289 ? 410 GLY A N    1 
ATOM   1344 C  CA   . GLY A 1 91  ? 8.90400  33.28600 14.66300  1.000 118.53328 ? 410 GLY A CA   1 
ATOM   1345 C  C    . GLY A 1 91  ? 7.48200  33.76400 14.43800  1.000 141.52039 ? 410 GLY A C    1 
ATOM   1346 O  O    . GLY A 1 91  ? 6.54500  32.98500 14.66400  1.000 101.71148 ? 410 GLY A O    1 
ATOM   1347 H  H    . GLY A 1 91  ? 10.23300 34.38700 13.71800  1.000 151.57850 ? 410 GLY A H    1 
ATOM   1348 H  HA2  . GLY A 1 91  ? 9.08300  32.56600 14.03900  1.000 142.33896 ? 410 GLY A HA2  1 
ATOM   1349 H  HA3  . GLY A 1 91  ? 8.95800  32.90800 15.55500  1.000 142.33896 ? 410 GLY A HA3  1 
ATOM   1350 N  N    . VAL A 1 92  ? 7.28900  35.00600 13.99800  1.000 102.52467 ? 411 VAL A N    1 
ATOM   1351 C  CA   . VAL A 1 92  ? 5.95200  35.57700 13.82700  1.000 134.29984 ? 411 VAL A CA   1 
ATOM   1352 C  C    . VAL A 1 92  ? 5.49200  35.39500 12.38400  1.000 125.44426 ? 411 VAL A C    1 
ATOM   1353 O  O    . VAL A 1 92  ? 6.29800  35.56200 11.45400  1.000 83.82472  ? 411 VAL A O    1 
ATOM   1354 C  CB   . VAL A 1 92  ? 5.93000  37.05600 14.24200  1.000 85.44091  ? 411 VAL A CB   1 
ATOM   1355 C  CG1  . VAL A 1 92  ? 4.66000  37.73800 13.76100  1.000 72.29575  ? 411 VAL A CG1  1 
ATOM   1356 C  CG2  . VAL A 1 92  ? 6.03700  37.15600 15.74400  1.000 97.72615  ? 411 VAL A CG2  1 
ATOM   1357 H  H    . VAL A 1 92  ? 7.92900  35.54200 13.79000  1.000 123.12863 ? 411 VAL A H    1 
ATOM   1358 H  HA   . VAL A 1 92  ? 5.33200  35.10700 14.40700  1.000 161.25884 ? 411 VAL A HA   1 
ATOM   1359 H  HB   . VAL A 1 92  ? 6.68500  37.50600 13.83100  1.000 102.62812 ? 411 VAL A HB   1 
ATOM   1360 H  HG11 . VAL A 1 92  ? 4.66900  38.66900 14.03400  1.000 86.85393  ? 411 VAL A HG11 1 
ATOM   1361 H  HG12 . VAL A 1 92  ? 4.61100  37.68600 12.79400  1.000 86.85393  ? 411 VAL A HG12 1 
ATOM   1362 H  HG13 . VAL A 1 92  ? 3.88800  37.29500 14.14800  1.000 86.85393  ? 411 VAL A HG13 1 
ATOM   1363 H  HG21 . VAL A 1 92  ? 6.02300  38.08900 16.00800  1.000 117.37041 ? 411 VAL A HG21 1 
ATOM   1364 H  HG22 . VAL A 1 92  ? 5.28900  36.69300 16.15300  1.000 117.37041 ? 411 VAL A HG22 1 
ATOM   1365 H  HG23 . VAL A 1 92  ? 6.86800  36.75000 16.03700  1.000 117.37041 ? 411 VAL A HG23 1 
ATOM   1366 N  N    . PRO A 1 93  ? 4.22900  35.02000 12.16100  1.000 75.71426  ? 412 PRO A N    1 
ATOM   1367 C  CA   . PRO A 1 93  ? 3.70600  34.88600 10.78900  1.000 140.36746 ? 412 PRO A CA   1 
ATOM   1368 C  C    . PRO A 1 93  ? 3.80200  36.19300 10.01900  1.000 78.92019  ? 412 PRO A C    1 
ATOM   1369 O  O    . PRO A 1 93  ? 3.22100  37.21000 10.40500  1.000 87.33321  ? 412 PRO A O    1 
ATOM   1370 C  CB   . PRO A 1 93  ? 2.25000  34.46200 11.01100  1.000 86.87666  ? 412 PRO A CB   1 
ATOM   1371 C  CG   . PRO A 1 93  ? 2.28400  33.73200 12.32300  1.000 104.12893 ? 412 PRO A CG   1 
ATOM   1372 C  CD   . PRO A 1 93  ? 3.29000  34.47600 13.16000  1.000 121.21520 ? 412 PRO A CD   1 
ATOM   1373 H  HA   . PRO A 1 93  ? 4.20700  34.25100 10.25300  1.000 168.53999 ? 412 PRO A HA   1 
ATOM   1374 H  HB2  . PRO A 1 93  ? 1.65700  35.22900 11.04600  1.000 104.35102 ? 412 PRO A HB2  1 
ATOM   1375 H  HB3  . PRO A 1 93  ? 1.93300  33.89100 10.29400  1.000 104.35102 ? 412 PRO A HB3  1 
ATOM   1376 H  HG2  . PRO A 1 93  ? 1.41100  33.72800 12.74500  1.000 125.05375 ? 412 PRO A HG2  1 
ATOM   1377 H  HG3  . PRO A 1 93  ? 2.54500  32.80600 12.20200  1.000 125.05375 ? 412 PRO A HG3  1 
ATOM   1378 H  HD2  . PRO A 1 93  ? 2.87200  35.18100 13.67900  1.000 145.55727 ? 412 PRO A HD2  1 
ATOM   1379 H  HD3  . PRO A 1 93  ? 3.73700  33.88800 13.78800  1.000 145.55727 ? 412 PRO A HD3  1 
ATOM   1380 N  N    . THR A 1 94  ? 4.55000  36.15400 8.92100   1.000 73.49427  ? 413 THR A N    1 
ATOM   1381 C  CA   . THR A 1 94  ? 4.79100  37.31100 8.07400   1.000 85.34326  ? 413 THR A CA   1 
ATOM   1382 C  C    . THR A 1 94  ? 4.47000  36.94100 6.63300   1.000 79.98938  ? 413 THR A C    1 
ATOM   1383 O  O    . THR A 1 94  ? 4.72700  35.81100 6.20000   1.000 64.56811  ? 413 THR A O    1 
ATOM   1384 C  CB   . THR A 1 94  ? 6.24600  37.77900 8.19100   1.000 75.22098  ? 413 THR A CB   1 
ATOM   1385 O  OG1  . THR A 1 94  ? 6.56000  38.01900 9.56700   1.000 130.67398 ? 413 THR A OG1  1 
ATOM   1386 C  CG2  . THR A 1 94  ? 6.48100  39.04600 7.39000   1.000 111.88431 ? 413 THR A CG2  1 
ATOM   1387 H  H    . THR A 1 94  ? 4.93800  35.43900 8.64400   1.000 88.29215  ? 413 THR A H    1 
ATOM   1388 H  HA   . THR A 1 94  ? 4.22100  38.04100 8.36100   1.000 102.51094 ? 413 THR A HA   1 
ATOM   1389 H  HB   . THR A 1 94  ? 6.82000  37.08300 7.83500   1.000 90.36421  ? 413 THR A HB   1 
ATOM   1390 H  HG1  . THR A 1 94  ? 6.57000  37.29000 9.98400   1.000 156.90781 ? 413 THR A HG1  1 
ATOM   1391 H  HG21 . THR A 1 94  ? 7.40700  39.32000 7.48100   1.000 134.36020 ? 413 THR A HG21 1 
ATOM   1392 H  HG22 . THR A 1 94  ? 6.28400  38.87900 6.45500   1.000 134.36020 ? 413 THR A HG22 1 
ATOM   1393 H  HG23 . THR A 1 94  ? 5.90200  39.75000 7.72100   1.000 134.36020 ? 413 THR A HG23 1 
ATOM   1394 N  N    . LEU A 1 95  ? 3.88900  37.88000 5.89300   1.000 61.62530  ? 414 LEU A N    1 
ATOM   1395 C  CA   . LEU A 1 95  ? 3.59500  37.64900 4.48800   1.000 52.95513  ? 414 LEU A CA   1 
ATOM   1396 C  C    . LEU A 1 95  ? 4.80600  38.01000 3.63300   1.000 72.46697  ? 414 LEU A C    1 
ATOM   1397 O  O    . LEU A 1 95  ? 5.38600  39.09100 3.78000   1.000 58.73440  ? 414 LEU A O    1 
ATOM   1398 C  CB   . LEU A 1 95  ? 2.37700  38.45400 4.04000   1.000 60.61511  ? 414 LEU A CB   1 
ATOM   1399 C  CG   . LEU A 1 95  ? 2.08900  38.26400 2.54500   1.000 56.06336  ? 414 LEU A CG   1 
ATOM   1400 C  CD1  . LEU A 1 95  ? 1.36400  36.94000 2.28200   1.000 57.77072  ? 414 LEU A CD1  1 
ATOM   1401 C  CD2  . LEU A 1 95  ? 1.30600  39.44500 1.96600   1.000 60.00870  ? 414 LEU A CD2  1 
ATOM   1402 H  H    . LEU A 1 95  ? 3.65800  38.65500 6.18600   1.000 74.04939  ? 414 LEU A H    1 
ATOM   1403 H  HA   . LEU A 1 95  ? 3.39300  36.70700 4.37300   1.000 63.64519  ? 414 LEU A HA   1 
ATOM   1404 H  HB2  . LEU A 1 95  ? 1.60200  38.18300 4.55600   1.000 72.83717  ? 414 LEU A HB2  1 
ATOM   1405 H  HB3  . LEU A 1 95  ? 2.52500  39.39500 4.22400   1.000 72.83717  ? 414 LEU A HB3  1 
ATOM   1406 H  HG   . LEU A 1 95  ? 2.94500  38.23000 2.08900   1.000 67.37507  ? 414 LEU A HG   1 
ATOM   1407 H  HD11 . LEU A 1 95  ? 1.19500  36.84700 1.33100   1.000 69.42389  ? 414 LEU A HD11 1 
ATOM   1408 H  HD12 . LEU A 1 95  ? 1.91600  36.20300 2.58600   1.000 69.42389  ? 414 LEU A HD12 1 
ATOM   1409 H  HD13 . LEU A 1 95  ? 0.52100  36.93100 2.76200   1.000 69.42389  ? 414 LEU A HD13 1 
ATOM   1410 H  HD21 . LEU A 1 95  ? 1.14100  39.29300 1.02200   1.000 72.10947  ? 414 LEU A HD21 1 
ATOM   1411 H  HD22 . LEU A 1 95  ? 0.45900  39.53200 2.43200   1.000 72.10947  ? 414 LEU A HD22 1 
ATOM   1412 H  HD23 . LEU A 1 95  ? 1.82000  40.26000 2.07700   1.000 72.10947  ? 414 LEU A HD23 1 
ATOM   1413 N  N    . LYS A 1 96  ? 5.20200  37.08900 2.75200   1.000 54.07680  ? 415 LYS A N    1 
ATOM   1414 C  CA   . LYS A 1 96  ? 6.16700  37.37700 1.69900   1.000 60.62669  ? 415 LYS A CA   1 
ATOM   1415 C  C    . LYS A 1 96  ? 5.36400  37.50900 0.41500   1.000 53.72827  ? 415 LYS A C    1 
ATOM   1416 O  O    . LYS A 1 96  ? 4.85600  36.51600 -0.10100  1.000 62.03857  ? 415 LYS A O    1 
ATOM   1417 C  CB   . LYS A 1 96  ? 7.21900  36.27400 1.59000   1.000 56.00909  ? 415 LYS A CB   1 
ATOM   1418 C  CG   . LYS A 1 96  ? 8.23400  36.47900 0.47400   1.000 57.24277  ? 415 LYS A CG   1 
ATOM   1419 C  CD   . LYS A 1 96  ? 8.96300  37.80200 0.63000   1.000 57.54377  ? 415 LYS A CD   1 
ATOM   1420 C  CE   . LYS A 1 96  ? 9.91400  38.05600 -0.53100  1.000 50.20609  ? 415 LYS A CE   1 
ATOM   1421 N  NZ   . LYS A 1 96  ? 10.63100 39.35600 -0.39200  1.000 74.38848  ? 415 LYS A NZ   1 
ATOM   1422 H  H    . LYS A 1 96  ? 4.91500  36.27800 2.75200   1.000 64.99119  ? 415 LYS A H    1 
ATOM   1423 H  HA   . LYS A 1 96  ? 6.65800  38.19200 1.88800   1.000 72.85106  ? 415 LYS A HA   1 
ATOM   1424 H  HB2  . LYS A 1 96  ? 7.69200  36.20900 2.43400   1.000 67.30994  ? 415 LYS A HB2  1 
ATOM   1425 H  HB3  . LYS A 1 96  ? 6.76900  35.42600 1.45100   1.000 67.30994  ? 415 LYS A HB3  1 
ATOM   1426 H  HG2  . LYS A 1 96  ? 8.87500  35.75100 0.47900   1.000 68.79035  ? 415 LYS A HG2  1 
ATOM   1427 H  HG3  . LYS A 1 96  ? 7.78400  36.45400 -0.38500  1.000 68.79035  ? 415 LYS A HG3  1 
ATOM   1428 H  HD2  . LYS A 1 96  ? 8.31700  38.52400 0.68500   1.000 69.15156  ? 415 LYS A HD2  1 
ATOM   1429 H  HD3  . LYS A 1 96  ? 9.46000  37.80200 1.46300   1.000 69.15156  ? 415 LYS A HD3  1 
ATOM   1430 H  HE2  . LYS A 1 96  ? 10.56100 37.33500 -0.58200  1.000 60.34634  ? 415 LYS A HE2  1 
ATOM   1431 H  HE3  . LYS A 1 96  ? 9.41600  38.05000 -1.36300  1.000 60.34634  ? 415 LYS A HE3  1 
ATOM   1432 H  HZ1  . LYS A 1 96  ? 10.45300 39.87000 -1.09600  1.000 89.36521  ? 415 LYS A HZ1  1 
ATOM   1433 H  HZ2  . LYS A 1 96  ? 10.36100 39.76600 0.35000   1.000 89.36521  ? 415 LYS A HZ2  1 
ATOM   1434 H  HZ3  . LYS A 1 96  ? 11.50800 39.20800 -0.34700  1.000 89.36521  ? 415 LYS A HZ3  1 
ATOM   1435 N  N    . TYR A 1 97  ? 5.22100  38.73500 -0.08700  1.000 58.15384  ? 416 TYR A N    1 
ATOM   1436 C  CA   . TYR A 1 97  ? 4.25900  38.96200 -1.16200  1.000 51.53567  ? 416 TYR A CA   1 
ATOM   1437 C  C    . TYR A 1 97  ? 4.71500  38.31900 -2.46500  1.000 53.50447  ? 416 TYR A C    1 
ATOM   1438 O  O    . TYR A 1 97  ? 3.95500  37.58000 -3.10200  1.000 59.87547  ? 416 TYR A O    1 
ATOM   1439 C  CB   . TYR A 1 97  ? 4.01700  40.45800 -1.35300  1.000 56.24821  ? 416 TYR A CB   1 
ATOM   1440 C  CG   . TYR A 1 97  ? 2.82400  40.74200 -2.23300  1.000 55.97040  ? 416 TYR A CG   1 
ATOM   1441 C  CD1  . TYR A 1 97  ? 1.58900  40.17000 -1.95600  1.000 56.48317  ? 416 TYR A CD1  1 
ATOM   1442 C  CD2  . TYR A 1 97  ? 2.92900  41.57300 -3.33900  1.000 58.45194  ? 416 TYR A CD2  1 
ATOM   1443 C  CE1  . TYR A 1 97  ? 0.49100  40.41900 -2.75500  1.000 54.13858  ? 416 TYR A CE1  1 
ATOM   1444 C  CE2  . TYR A 1 97  ? 1.83400  41.82900 -4.14500  1.000 88.53017  ? 416 TYR A CE2  1 
ATOM   1445 C  CZ   . TYR A 1 97  ? 0.61800  41.24900 -3.84700  1.000 55.59335  ? 416 TYR A CZ   1 
ATOM   1446 O  OH   . TYR A 1 97  ? -0.47600 41.49800 -4.64400  1.000 55.34781  ? 416 TYR A OH   1 
ATOM   1447 H  H    . TYR A 1 97  ? 5.65700  39.42900 0.17200   1.000 69.88364  ? 416 TYR A H    1 
ATOM   1448 H  HA   . TYR A 1 97  ? 3.42300  38.54200 -0.90600  1.000 61.94184  ? 416 TYR A HA   1 
ATOM   1449 H  HB2  . TYR A 1 97  ? 3.88300  40.87400 -0.48700  1.000 67.59688  ? 416 TYR A HB2  1 
ATOM   1450 H  HB3  . TYR A 1 97  ? 4.80700  40.86300 -1.74300  1.000 67.59688  ? 416 TYR A HB3  1 
ATOM   1451 H  HD1  . TYR A 1 97  ? 1.50000  39.60900 -1.21900  1.000 67.87884  ? 416 TYR A HD1  1 
ATOM   1452 H  HD2  . TYR A 1 97  ? 3.74800  41.96400 -3.54200  1.000 70.24135  ? 416 TYR A HD2  1 
ATOM   1453 H  HE1  . TYR A 1 97  ? -0.33000 40.02900 -2.55700  1.000 65.06533  ? 416 TYR A HE1  1 
ATOM   1454 H  HE2  . TYR A 1 97  ? 1.91700  42.38900 -4.88300  1.000 106.33523 ? 416 TYR A HE2  1 
ATOM   1455 H  HH   . TYR A 1 97  ? -0.21900 41.72200 -5.41100  1.000 66.51640  ? 416 TYR A HH   1 
ATOM   1456 N  N    . HIS A 1 98  ? 5.94700  38.59100 -2.88300  1.000 60.93185  ? 417 HIS A N    1 
ATOM   1457 C  CA   . HIS A 1 98  ? 6.51500  38.00500 -4.09300  1.000 53.94557  ? 417 HIS A CA   1 
ATOM   1458 C  C    . HIS A 1 98  ? 7.74200  37.17700 -3.68700  1.000 59.32051  ? 417 HIS A C    1 
ATOM   1459 O  O    . HIS A 1 98  ? 8.86900  37.67400 -3.62900  1.000 52.71990  ? 417 HIS A O    1 
ATOM   1460 C  CB   . HIS A 1 98  ? 6.88200  39.07300 -5.12100  1.000 56.29744  ? 417 HIS A CB   1 
ATOM   1461 C  CG   . HIS A 1 98  ? 5.69700  39.78800 -5.71200  1.000 85.05825  ? 417 HIS A CG   1 
ATOM   1462 N  ND1  . HIS A 1 98  ? 5.63700  41.16400 -5.83500  1.000 78.58083  ? 417 HIS A ND1  1 
ATOM   1463 C  CD2  . HIS A 1 98  ? 4.53400  39.31700 -6.22500  1.000 63.55854  ? 417 HIS A CD2  1 
ATOM   1464 C  CE1  . HIS A 1 98  ? 4.48800  41.50900 -6.38800  1.000 58.00827  ? 417 HIS A CE1  1 
ATOM   1465 N  NE2  . HIS A 1 98  ? 3.80200  40.40700 -6.64000  1.000 111.74024 ? 417 HIS A NE2  1 
ATOM   1466 H  H    . HIS A 1 98  ? 6.48100  39.12400 -2.47000  1.000 73.21725  ? 417 HIS A H    1 
ATOM   1467 H  HA   . HIS A 1 98  ? 5.85500  37.43600 -4.51900  1.000 64.83371  ? 417 HIS A HA   1 
ATOM   1468 H  HB2  . HIS A 1 98  ? 7.46500  39.72500 -4.70200  1.000 67.65596  ? 417 HIS A HB2  1 
ATOM   1469 H  HB3  . HIS A 1 98  ? 7.38800  38.65900 -5.83700  1.000 67.65596  ? 417 HIS A HB3  1 
ATOM   1470 H  HD1  . HIS A 1 98  ? 6.25300  41.71100 -5.58900  1.000 94.39603  ? 417 HIS A HD1  1 
ATOM   1471 H  HD2  . HIS A 1 98  ? 4.27800  38.42500 -6.28500  1.000 76.36928  ? 417 HIS A HD2  1 
ATOM   1472 H  HE1  . HIS A 1 98  ? 4.20900  42.37800 -6.56900  1.000 69.70895  ? 417 HIS A HE1  1 
ATOM   1473 N  N    . TYR A 1 99  ? 7.51100  35.90900 -3.37600  1.000 51.31433  ? 418 TYR A N    1 
ATOM   1474 C  CA   . TYR A 1 99  ? 8.59300  34.93800 -3.18500  1.000 60.89983  ? 418 TYR A CA   1 
ATOM   1475 C  C    . TYR A 1 99  ? 9.01400  34.42700 -4.56400  1.000 50.10190  ? 418 TYR A C    1 
ATOM   1476 O  O    . TYR A 1 99  ? 8.35700  33.56600 -5.14000  1.000 44.38644  ? 418 TYR A O    1 
ATOM   1477 C  CB   . TYR A 1 99  ? 8.10200  33.80500 -2.29600  1.000 43.18430  ? 418 TYR A CB   1 
ATOM   1478 C  CG   . TYR A 1 99  ? 9.20700  32.98900 -1.65900  1.000 66.83814  ? 418 TYR A CG   1 
ATOM   1479 C  CD1  . TYR A 1 99  ? 10.33500 33.60700 -1.12700  1.000 59.74553  ? 418 TYR A CD1  1 
ATOM   1480 C  CD2  . TYR A 1 99  ? 9.10900  31.60400 -1.56000  1.000 60.20721  ? 418 TYR A CD2  1 
ATOM   1481 C  CE1  . TYR A 1 99  ? 11.34300 32.86500 -0.53000  1.000 77.67938  ? 418 TYR A CE1  1 
ATOM   1482 C  CE2  . TYR A 1 99  ? 10.11200 30.85000 -0.96500  1.000 62.20807  ? 418 TYR A CE2  1 
ATOM   1483 C  CZ   . TYR A 1 99  ? 11.22600 31.48500 -0.45500  1.000 64.04093  ? 418 TYR A CZ   1 
ATOM   1484 O  OH   . TYR A 1 99  ? 12.22900 30.74700 0.13700   1.000 100.82079 ? 418 TYR A OH   1 
ATOM   1485 H  H    . TYR A 1 99  ? 6.72300  35.58200 -3.26800  1.000 61.67623  ? 418 TYR A H    1 
ATOM   1486 H  HA   . TYR A 1 99  ? 9.35800  35.34400 -2.74900  1.000 73.17883  ? 418 TYR A HA   1 
ATOM   1487 H  HB2  . TYR A 1 99  ? 7.54400  34.17700 -1.59500  1.000 51.92019  ? 418 TYR A HB2  1 
ATOM   1488 H  HB3  . TYR A 1 99  ? 7.54100  33.21500 -2.82300  1.000 51.92019  ? 418 TYR A HB3  1 
ATOM   1489 H  HD1  . TYR A 1 99  ? 10.41400 34.53300 -1.17300  1.000 71.79367  ? 418 TYR A HD1  1 
ATOM   1490 H  HD2  . TYR A 1 99  ? 8.35700  31.17500 -1.89900  1.000 72.34769  ? 418 TYR A HD2  1 
ATOM   1491 H  HE1  . TYR A 1 99  ? 12.09300 33.29000 -0.18200  1.000 93.31428  ? 418 TYR A HE1  1 
ATOM   1492 H  HE2  . TYR A 1 99  ? 10.03400 29.92500 -0.91100  1.000 74.74872  ? 418 TYR A HE2  1 
ATOM   1493 H  HH   . TYR A 1 99  ? 11.93600 29.98600 0.33800   1.000 121.08398 ? 418 TYR A HH   1 
ATOM   1494 N  N    . GLU A 1 100 ? 10.12300 34.94800 -5.08200  1.000 46.25681  ? 419 GLU A N    1 
ATOM   1495 C  CA   . GLU A 1 100 ? 10.51300 34.74100 -6.47100  1.000 48.06258  ? 419 GLU A CA   1 
ATOM   1496 C  C    . GLU A 1 100 ? 10.88500 33.29300 -6.78300  1.000 48.94065  ? 419 GLU A C    1 
ATOM   1497 O  O    . GLU A 1 100 ? 11.32900 32.53100 -5.91900  1.000 42.01565  ? 419 GLU A O    1 
ATOM   1498 C  CB   . GLU A 1 100 ? 11.70400 35.63200 -6.81300  1.000 42.95036  ? 419 GLU A CB   1 
ATOM   1499 C  CG   . GLU A 1 100 ? 11.39600 37.10300 -6.69100  1.000 52.61917  ? 419 GLU A CG   1 
ATOM   1500 C  CD   . GLU A 1 100 ? 10.26400 37.52500 -7.61200  1.000 80.20503  ? 419 GLU A CD   1 
ATOM   1501 O  OE1  . GLU A 1 100 ? 10.13200 36.93000 -8.71300  1.000 61.74484  ? 419 GLU A OE1  1 
ATOM   1502 O  OE2  . GLU A 1 100 ? 9.50600  38.44700 -7.22900  1.000 79.79438  ? 419 GLU A OE2  1 
ATOM   1503 H  H    . GLU A 1 100 ? 10.67300 35.43400 -4.63400  1.000 55.60720  ? 419 GLU A H    1 
ATOM   1504 H  HA   . GLU A 1 100 ? 9.73800  34.96900 -7.00800  1.000 57.77413  ? 419 GLU A HA   1 
ATOM   1505 H  HB2  . GLU A 1 100 ? 12.44400 35.41200 -6.22600  1.000 51.04528  ? 419 GLU A HB2  1 
ATOM   1506 H  HB3  . GLU A 1 100 ? 11.99400 35.44200 -7.71900  1.000 51.04528  ? 419 GLU A HB3  1 
ATOM   1507 H  HG2  . GLU A 1 100 ? 11.15900 37.30800 -5.77300  1.000 63.24203  ? 419 GLU A HG2  1 
ATOM   1508 H  HG3  . GLU A 1 100 ? 12.19100 37.61800 -6.90000  1.000 63.24203  ? 419 GLU A HG3  1 
ATOM   1509 N  N    . GLY A 1 101 ? 10.71700 32.92900 -8.05400  1.000 49.12561  ? 420 GLY A N    1 
ATOM   1510 C  CA   . GLY A 1 101 ? 11.29600 31.72100 -8.59900  1.000 44.63990  ? 420 GLY A CA   1 
ATOM   1511 C  C    . GLY A 1 101 ? 10.60100 30.44000 -8.22800  1.000 41.35303  ? 420 GLY A C    1 
ATOM   1512 O  O    . GLY A 1 101 ? 11.20600 29.37000 -8.36000  1.000 41.82971  ? 420 GLY A O    1 
ATOM   1513 H  H    . GLY A 1 101 ? 10.25900 33.38500 -8.62200  1.000 59.04976  ? 420 GLY A H    1 
ATOM   1514 H  HA2  . GLY A 1 101 ? 11.30700 31.79500 -9.56600  1.000 53.66691  ? 420 GLY A HA2  1 
ATOM   1515 H  HA3  . GLY A 1 101 ? 12.22000 31.66500 -8.30800  1.000 53.66691  ? 420 GLY A HA3  1 
ATOM   1516 N  N    . MET A 1 102 ? 9.33800  30.50400 -7.80600  1.000 37.06687  ? 421 MET A N    1 
ATOM   1517 C  CA   . MET A 1 102 ? 8.64600  29.33700 -7.27700  1.000 38.53592  ? 421 MET A CA   1 
ATOM   1518 C  C    . MET A 1 102 ? 7.81500  28.56900 -8.30000  1.000 40.12686  ? 421 MET A C    1 
ATOM   1519 O  O    . MET A 1 102 ? 7.58200  27.37000 -8.08500  1.000 36.19216  ? 421 MET A O    1 
ATOM   1520 C  CB   . MET A 1 102 ? 7.75600  29.75800 -6.11000  1.000 42.79830  ? 421 MET A CB   1 
ATOM   1521 C  CG   . MET A 1 102 ? 8.55700  30.15800 -4.89500  1.000 39.92710  ? 421 MET A CG   1 
ATOM   1522 S  SD   . MET A 1 102 ? 9.44200  28.73800 -4.19200  1.000 44.73812  ? 421 MET A SD   1 
ATOM   1523 C  CE   . MET A 1 102 ? 8.06300  27.87400 -3.45200  1.000 47.14546  ? 421 MET A CE   1 
ATOM   1524 H  H    . MET A 1 102 ? 8.86400  31.22100 -7.81900  1.000 44.57927  ? 421 MET A H    1 
ATOM   1525 H  HA   . MET A 1 102 ? 9.34200  28.72500 -6.99000  1.000 46.34213  ? 421 MET A HA   1 
ATOM   1526 H  HB2  . MET A 1 102 ? 7.19600  30.50100 -6.38500  1.000 51.45699  ? 421 MET A HB2  1 
ATOM   1527 H  HB3  . MET A 1 102 ? 7.16300  29.02600 -5.87800  1.000 51.45699  ? 421 MET A HB3  1 
ATOM   1528 H  HG2  . MET A 1 102 ? 9.19200  30.85000 -5.13700  1.000 48.01156  ? 421 MET A HG2  1 
ATOM   1529 H  HG3  . MET A 1 102 ? 7.96600  30.53700 -4.22600  1.000 48.01156  ? 421 MET A HG3  1 
ATOM   1530 H  HE1  . MET A 1 102 ? 8.38100  27.06500 -3.02100  1.000 56.67358  ? 421 MET A HE1  1 
ATOM   1531 H  HE2  . MET A 1 102 ? 7.63900  28.44500 -2.79300  1.000 56.67358  ? 421 MET A HE2  1 
ATOM   1532 H  HE3  . MET A 1 102 ? 7.42000  27.64200 -4.14000  1.000 56.67358  ? 421 MET A HE3  1 
ATOM   1533 N  N    . SER A 1 103 ? 7.36400  29.20500 -9.40000  1.000 35.90291  ? 422 SER A N    1 
ATOM   1534 C  CA   . SER A 1 103 ? 6.47100  28.57200 -10.37000 1.000 40.62633  ? 422 SER A CA   1 
ATOM   1535 C  C    . SER A 1 103 ? 6.98600  28.76800 -11.78900 1.000 40.64501  ? 422 SER A C    1 
ATOM   1536 O  O    . SER A 1 103 ? 7.52000  29.82700 -12.12200 1.000 43.58363  ? 422 SER A O    1 
ATOM   1537 C  CB   . SER A 1 103 ? 5.04300  29.14800 -10.31400 1.000 44.16485  ? 422 SER A CB   1 
ATOM   1538 O  OG   . SER A 1 103 ? 4.44900  28.91500 -9.05500  1.000 85.96054  ? 422 SER A OG   1 
ATOM   1539 H  H    . SER A 1 103 ? 7.57300  30.01600 -9.59600  1.000 42.58834  ? 422 SER A H    1 
ATOM   1540 H  HA   . SER A 1 103 ? 6.44900  27.63100 -10.13600 1.000 48.85063  ? 422 SER A HA   1 
ATOM   1541 H  HB2  . SER A 1 103 ? 5.06900  30.10100 -10.49100 1.000 53.09685  ? 422 SER A HB2  1 
ATOM   1542 H  HB3  . SER A 1 103 ? 4.50100  28.74500 -11.01000 1.000 53.09685  ? 422 SER A HB3  1 
ATOM   1543 H  HG   . SER A 1 103 ? 4.86300  28.30100 -8.65900  1.000 103.25168 ? 422 SER A HG   1 
ATOM   1544 N  N    . VAL A 1 104 ? 6.74100  27.76400 -12.62100 1.000 39.10876  ? 423 VAL A N    1 
ATOM   1545 C  CA   . VAL A 1 104 ? 7.20800  27.81700 -14.03300 1.000 37.92566  ? 423 VAL A CA   1 
ATOM   1546 C  C    . VAL A 1 104 ? 6.31800  28.74100 -14.86700 1.000 37.68348  ? 423 VAL A C    1 
ATOM   1547 O  O    . VAL A 1 104 ? 5.10200  28.52700 -14.88500 1.000 40.79575  ? 423 VAL A O    1 
ATOM   1548 C  CB   . VAL A 1 104 ? 7.28100  26.42200 -14.67600 1.000 40.79931  ? 423 VAL A CB   1 
ATOM   1549 C  CG1  . VAL A 1 104 ? 7.70400  26.50300 -16.13200 1.000 46.38785  ? 423 VAL A CG1  1 
ATOM   1550 C  CG2  . VAL A 1 104 ? 8.17800  25.47500 -13.89900 1.000 40.08751  ? 423 VAL A CG2  1 
ATOM   1551 H  H    . VAL A 1 104 ? 6.31500  27.04800 -12.40800 1.000 47.02954  ? 423 VAL A H    1 
ATOM   1552 H  HA   . VAL A 1 104 ? 8.10900  28.17700 -14.01800 1.000 45.60982  ? 423 VAL A HA   1 
ATOM   1553 H  HB   . VAL A 1 104 ? 6.38400  26.05400 -14.64400 1.000 49.05820  ? 423 VAL A HB   1 
ATOM   1554 H  HG11 . VAL A 1 104 ? 7.74100  25.61000 -16.50900 1.000 55.76445  ? 423 VAL A HG11 1 
ATOM   1555 H  HG12 . VAL A 1 104 ? 7.06200  27.03600 -16.62700 1.000 55.76445  ? 423 VAL A HG12 1 
ATOM   1556 H  HG13 . VAL A 1 104 ? 8.58000  26.91500 -16.19200 1.000 55.76445  ? 423 VAL A HG13 1 
ATOM   1557 H  HG21 . VAL A 1 104 ? 8.19400  24.61100 -14.33900 1.000 48.20404  ? 423 VAL A HG21 1 
ATOM   1558 H  HG22 . VAL A 1 104 ? 9.07700  25.83700 -13.86400 1.000 48.20404  ? 423 VAL A HG22 1 
ATOM   1559 H  HG23 . VAL A 1 104 ? 7.83600  25.37200 -12.99700 1.000 48.20404  ? 423 VAL A HG23 1 
ATOM   1560 N  N    . ALA A 1 105 ? 6.91400  29.75400 -15.47400 1.000 40.97636  ? 424 ALA A N    1 
ATOM   1561 C  CA   . ALA A 1 105 ? 6.21800  30.61700 -16.43500 1.000 51.45105  ? 424 ALA A CA   1 
ATOM   1562 C  C    . ALA A 1 105 ? 6.36300  30.10900 -17.86800 1.000 52.36751  ? 424 ALA A C    1 
ATOM   1563 O  O    . ALA A 1 105 ? 5.37400  30.02400 -18.59800 1.000 50.32272  ? 424 ALA A O    1 
ATOM   1564 C  CB   . ALA A 1 105 ? 6.73500  32.06400 -16.35400 1.000 38.45827  ? 424 ALA A CB   1 
ATOM   1565 H  H    . ALA A 1 105 ? 7.73700  29.96700 -15.34500 1.000 49.27067  ? 424 ALA A H    1 
ATOM   1566 H  HA   . ALA A 1 105 ? 5.27800  30.59700 -16.19600 1.000 61.84029  ? 424 ALA A HA   1 
ATOM   1567 H  HB1  . ALA A 1 105 ? 6.26100  32.61400 -16.99700 1.000 45.67758  ? 424 ALA A HB1  1 
ATOM   1568 H  HB2  . ALA A 1 105 ? 6.58600  32.41100 -15.46100 1.000 45.67758  ? 424 ALA A HB2  1 
ATOM   1569 H  HB3  . ALA A 1 105 ? 7.68400  32.08000 -16.55300 1.000 45.67758  ? 424 ALA A HB3  1 
ATOM   1570 N  N    . GLU A 1 106 ? 7.58900  29.78900 -18.29200 1.000 46.92512  ? 425 GLU A N    1 
ATOM   1571 C  CA   . GLU A 1 106 ? 7.85100  29.25400 -19.62500 1.000 39.60909  ? 425 GLU A CA   1 
ATOM   1572 C  C    . GLU A 1 106 ? 8.86500  28.11700 -19.54800 1.000 44.58968  ? 425 GLU A C    1 
ATOM   1573 O  O    . GLU A 1 106 ? 9.71900  28.09100 -18.65300 1.000 43.48034  ? 425 GLU A O    1 
ATOM   1574 C  CB   . GLU A 1 106 ? 8.37400  30.34500 -20.57100 1.000 45.01825  ? 425 GLU A CB   1 
ATOM   1575 C  CG   . GLU A 1 106 ? 7.39100  31.47800 -20.79900 1.000 83.52417  ? 425 GLU A CG   1 
ATOM   1576 C  CD   . GLU A 1 106 ? 8.03300  32.69400 -21.45100 1.000 145.11359 ? 425 GLU A CD   1 
ATOM   1577 O  OE1  . GLU A 1 106 ? 9.21000  32.60000 -21.87600 1.000 82.44843  ? 425 GLU A OE1  1 
ATOM   1578 O  OE2  . GLU A 1 106 ? 7.35600  33.74500 -21.53200 1.000 116.88195 ? 425 GLU A OE2  1 
ATOM   1579 H  H    . GLU A 1 106 ? 8.29500  29.87800 -17.80800 1.000 56.40918  ? 425 GLU A H    1 
ATOM   1580 H  HA   . GLU A 1 106 ? 7.01200  28.91700 -19.97800 1.000 47.62994  ? 425 GLU A HA   1 
ATOM   1581 H  HB2  . GLU A 1 106 ? 9.19600  30.70900 -20.20800 1.000 54.12093  ? 425 GLU A HB2  1 
ATOM   1582 H  HB3  . GLU A 1 106 ? 8.59500  29.94200 -21.42500 1.000 54.12093  ? 425 GLU A HB3  1 
ATOM   1583 H  HG2  . GLU A 1 106 ? 6.66400  31.16200 -21.35800 1.000 100.32803 ? 425 GLU A HG2  1 
ATOM   1584 H  HG3  . GLU A 1 106 ? 7.00200  31.73900 -19.95000 1.000 100.32803 ? 425 GLU A HG3  1 
ATOM   1585 N  N    . CYS A 1 107 ? 8.75700  27.18000 -20.49800 1.000 39.89066  ? 426 CYS A N    1 
ATOM   1586 C  CA   . CYS A 1 107 ? 9.66300  26.05100 -20.67100 1.000 38.53057  ? 426 CYS A CA   1 
ATOM   1587 C  C    . CYS A 1 107 ? 10.45800 26.19600 -21.96200 1.000 41.49295  ? 426 CYS A C    1 
ATOM   1588 O  O    . CYS A 1 107 ? 10.05500 26.88900 -22.89800 1.000 40.79347  ? 426 CYS A O    1 
ATOM   1589 C  CB   . CYS A 1 107 ? 8.91000  24.71500 -20.71800 1.000 40.22218  ? 426 CYS A CB   1 
ATOM   1590 S  SG   . CYS A 1 107 ? 8.02900  24.26100 -19.21000 1.000 50.44454  ? 426 CYS A SG   1 
ATOM   1591 H  H    . CYS A 1 107 ? 8.12500  27.19100 -21.08100 1.000 47.96782  ? 426 CYS A H    1 
ATOM   1592 H  HA   . CYS A 1 107 ? 10.25800 26.05200 -19.90500 1.000 46.33571  ? 426 CYS A HA   1 
ATOM   1593 H  HB2  . CYS A 1 107 ? 8.27200  24.74700 -21.44800 1.000 48.36565  ? 426 CYS A HB2  1 
ATOM   1594 H  HB3  . CYS A 1 107 ? 9.54500  24.01200 -20.92600 1.000 48.36565  ? 426 CYS A HB3  1 
ATOM   1595 N  N    . GLY A 1 108 ? 11.58000 25.50200 -22.02200 1.000 33.95314  ? 427 GLY A N    1 
ATOM   1596 C  CA   . GLY A 1 108 ? 12.39900 25.55500 -23.21500 1.000 41.53384  ? 427 GLY A CA   1 
ATOM   1597 C  C    . GLY A 1 108 ? 13.51400 24.54400 -23.13600 1.000 45.00455  ? 427 GLY A C    1 
ATOM   1598 O  O    . GLY A 1 108 ? 13.89200 24.09200 -22.05200 1.000 38.34723  ? 427 GLY A O    1 
ATOM   1599 H  H    . GLY A 1 108 ? 11.88200 25.00100 -21.39200 1.000 40.24861  ? 427 GLY A H    1 
ATOM   1600 H  HA2  . GLY A 1 108 ? 11.85200 25.38100 -23.99700 1.000 49.93964  ? 427 GLY A HA2  1 
ATOM   1601 H  HA3  . GLY A 1 108 ? 12.76900 26.44500 -23.32000 1.000 49.93964  ? 427 GLY A HA3  1 
ATOM   1602 N  N    . CYS A 1 109 ? 14.04100 24.20200 -24.30500 1.000 41.17057  ? 428 CYS A N    1 
ATOM   1603 C  CA   . CYS A 1 109 ? 15.16100 23.27800 -24.42000 1.000 36.36022  ? 428 CYS A CA   1 
ATOM   1604 C  C    . CYS A 1 109 ? 16.45600 24.06600 -24.28700 1.000 38.15612  ? 428 CYS A C    1 
ATOM   1605 O  O    . CYS A 1 109 ? 16.61500 25.11700 -24.91600 1.000 39.32162  ? 428 CYS A O    1 
ATOM   1606 C  CB   . CYS A 1 109 ? 15.09400 22.53100 -25.75700 1.000 37.47600  ? 428 CYS A CB   1 
ATOM   1607 S  SG   . CYS A 1 109 ? 13.72900 21.29400 -25.77600 1.000 48.49014  ? 428 CYS A SG   1 
ATOM   1608 H  H    . CYS A 1 109 ? 13.75700 24.50200 -25.05900 1.000 49.50372  ? 428 CYS A H    1 
ATOM   1609 H  HA   . CYS A 1 109 ? 15.12300 22.61300 -23.71500 1.000 43.73130  ? 428 CYS A HA   1 
ATOM   1610 H  HB2  . CYS A 1 109 ? 14.96500 23.16700 -26.47800 1.000 45.07024  ? 428 CYS A HB2  1 
ATOM   1611 H  HB3  . CYS A 1 109 ? 15.93900 22.08400 -25.92100 1.000 45.07024  ? 428 CYS A HB3  1 
ATOM   1612 N  N    . ARG A 1 110 ? 17.34400 23.59900 -23.41500 1.000 41.00288  ? 429 ARG A N    1 
ATOM   1613 C  CA   . ARG A 1 110 ? 18.56600 24.35000 -23.12600 1.000 43.05470  ? 429 ARG A CA   1 
ATOM   1614 C  C    . ARG A 1 110 ? 19.80800 23.45000 -23.08700 1.000 43.79722  ? 429 ARG A C    1 
ATOM   1615 O  O    . ARG A 1 110 ? 20.88000 23.83000 -23.60100 1.000 36.45127  ? 429 ARG A O    1 
ATOM   1616 C  CB   . ARG A 1 110 ? 18.39900 25.11800 -21.81800 1.000 36.88224  ? 429 ARG A CB   1 
ATOM   1617 C  CG   . ARG A 1 110 ? 17.39600 26.26600 -21.90100 1.000 36.11484  ? 429 ARG A CG   1 
ATOM   1618 C  CD   . ARG A 1 110 ? 17.85900 27.34500 -22.88700 1.000 35.96590  ? 429 ARG A CD   1 
ATOM   1619 N  NE   . ARG A 1 110 ? 16.91600 28.45900 -22.97400 1.000 40.19909  ? 429 ARG A NE   1 
ATOM   1620 C  CZ   . ARG A 1 110 ? 15.88800 28.51700 -23.82000 1.000 48.49562  ? 429 ARG A CZ   1 
ATOM   1621 N  NH1  . ARG A 1 110 ? 15.61300 27.52400 -24.65700 1.000 37.00031  ? 429 ARG A NH1  1 
ATOM   1622 N  NH2  . ARG A 1 110 ? 15.11200 29.59300 -23.82300 1.000 36.93874  ? 429 ARG A NH2  1 
ATOM   1623 O  OXT  . ARG A 1 110 ? 19.75900 22.31400 -22.59100 1.000 38.61707  ? 429 ARG A OXT  1 
ATOM   1624 H  H    . ARG A 1 110 ? 17.26200 22.85900 -22.98400 1.000 49.30249  ? 429 ARG A H    1 
ATOM   1625 H  HA   . ARG A 1 110 ? 18.70900 24.98000 -23.85000 1.000 51.76468  ? 429 ARG A HA   1 
ATOM   1626 H  HB2  . ARG A 1 110 ? 18.11600 24.50200 -21.12500 1.000 44.35772  ? 429 ARG A HB2  1 
ATOM   1627 H  HB3  . ARG A 1 110 ? 19.26100 25.47200 -21.54800 1.000 44.35772  ? 429 ARG A HB3  1 
ATOM   1628 H  HG2  . ARG A 1 110 ? 16.53200 25.92300 -22.17700 1.000 43.43684  ? 429 ARG A HG2  1 
ATOM   1629 H  HG3  . ARG A 1 110 ? 17.27800 26.65800 -21.02200 1.000 43.43684  ? 429 ARG A HG3  1 
ATOM   1630 H  HD2  . ARG A 1 110 ? 18.72700 27.68000 -22.61300 1.000 42.94768  ? 429 ARG A HD2  1 
ATOM   1631 H  HD3  . ARG A 1 110 ? 17.97200 26.95000 -23.76600 1.000 42.94768  ? 429 ARG A HD3  1 
ATOM   1632 H  HE   . ARG A 1 110 ? 17.03300 29.12400 -22.44100 1.000 48.33794  ? 429 ARG A HE   1 
ATOM   1633 H  HH11 . ARG A 1 110 ? 16.10400 26.81800 -24.66300 1.000 44.49940  ? 429 ARG A HH11 1 
ATOM   1634 H  HH12 . ARG A 1 110 ? 14.94300 27.58600 -25.19300 1.000 44.49940  ? 429 ARG A HH12 1 
ATOM   1635 H  HH21 . ARG A 1 110 ? 15.27500 30.24200 -23.28300 1.000 43.83134  ? 429 ARG A HH21 1 
ATOM   1636 H  HH22 . ARG A 1 110 ? 14.44600 29.64100 -24.36500 1.000 43.83134  ? 429 ARG A HH22 1 
HETATM 1637 CL CL   . CL  B 2 .   ? 20.78900 31.62800 -28.78300 0.660 45.43269  ? 501 CL  A CL   1 
HETATM 1638 CL CL   . CL  C 2 .   ? 13.42900 22.36600 -36.68000 0.430 56.81409  ? 502 CL  A CL   1 
HETATM 1639 CL CL   . CL  D 2 .   ? 7.79300  40.55900 -1.69400  0.660 77.10057  ? 503 CL  A CL   1 
HETATM 1640 CL CL   . CL  E 2 .   ? 0.48400  43.24400 -6.74500  0.520 50.63528  ? 504 CL  A CL   1 
HETATM 1641 CL CL   . CL  F 2 .   ? 13.20800 25.69500 -26.88100 0.600 46.09706  ? 505 CL  A CL   1 
HETATM 1642 NA NA   . NA  G 3 .   ? 28.55500 7.44500  -29.92900 0.990 57.60580  ? 506 NA  A NA   1 
HETATM 1643 C  C1   . GOL H 4 .   ? 0.56200  38.15600 -5.54500  0.960 114.67029 ? 507 GOL A C1   1 
HETATM 1644 O  O1   . GOL H 4 .   ? -0.16400 37.65300 -4.42900  0.960 114.35351 ? 507 GOL A O1   1 
HETATM 1645 C  C2   . GOL H 4 .   ? 0.21600  37.40400 -6.81200  0.960 114.66038 ? 507 GOL A C2   1 
HETATM 1646 O  O2   . GOL H 4 .   ? 1.08900  36.28700 -6.97600  0.960 114.60664 ? 507 GOL A O2   1 
HETATM 1647 C  C3   . GOL H 4 .   ? 0.23700  38.27400 -8.04900  0.960 114.53427 ? 507 GOL A C3   1 
HETATM 1648 O  O3   . GOL H 4 .   ? 1.32800  39.18800 -8.02500  0.960 114.47587 ? 507 GOL A O3   1 
HETATM 1649 H  H11  . GOL H 4 .   ? 1.51400  38.08300 -5.37300  0.960 137.70337 ? 507 GOL A H11  1 
HETATM 1650 H  H12  . GOL H 4 .   ? 0.36600  39.09900 -5.66200  0.960 137.70337 ? 507 GOL A H12  1 
HETATM 1651 H  HO1  . GOL H 4 .   ? -0.34100 38.28300 -3.90200  0.960 137.32324 ? 507 GOL A HO1  1 
HETATM 1652 H  H2   . GOL H 4 .   ? -0.69800 37.09400 -6.71000  0.960 137.69148 ? 507 GOL A H2   1 
HETATM 1653 H  HO2  . GOL H 4 .   ? 0.96200  35.94100 -7.73100  0.960 137.62699 ? 507 GOL A HO2  1 
HETATM 1654 H  H31  . GOL H 4 .   ? -0.59700 38.76500 -8.11500  0.960 137.54016 ? 507 GOL A H31  1 
HETATM 1655 H  H32  . GOL H 4 .   ? 0.30000  37.71400 -8.83900  0.960 137.54016 ? 507 GOL A H32  1 
HETATM 1656 H  HO3  . GOL H 4 .   ? 1.97900  38.83700 -7.62800  0.960 137.47008 ? 507 GOL A HO3  1 
HETATM 1657 C  C1   . GOL I 4 .   ? 10.40800 34.51900 3.11200   0.790 90.06580  ? 508 GOL A C1   1 
HETATM 1658 O  O1   . GOL I 4 .   ? 9.80000  33.57900 2.23200   0.790 90.50501  ? 508 GOL A O1   1 
HETATM 1659 C  C2   . GOL I 4 .   ? 11.81300 34.87500 2.67900   0.790 90.04652  ? 508 GOL A C2   1 
HETATM 1660 O  O2   . GOL I 4 .   ? 12.75400 34.32900 3.60000   0.790 90.37682  ? 508 GOL A O2   1 
HETATM 1661 C  C3   . GOL I 4 .   ? 12.04600 36.36500 2.57300   0.790 90.24725  ? 508 GOL A C3   1 
HETATM 1662 O  O3   . GOL I 4 .   ? 13.07500 36.77600 3.46700   0.790 90.28635  ? 508 GOL A O3   1 
HETATM 1663 H  H11  . GOL I 4 .   ? 10.43000 34.15300 4.01000   0.790 108.17799 ? 508 GOL A H11  1 
HETATM 1664 H  H12  . GOL I 4 .   ? 9.86800  35.32400 3.14700   0.790 108.17799 ? 508 GOL A H12  1 
HETATM 1665 H  HO1  . GOL I 4 .   ? 9.98600  32.79900 2.48300   0.790 108.70504 ? 508 GOL A HO1  1 
HETATM 1666 H  H2   . GOL I 4 .   ? 11.93100 34.49800 1.79300   0.790 108.15486 ? 508 GOL A H2   1 
HETATM 1667 H  HO2  . GOL I 4 .   ? 13.23900 34.94400 3.90300   0.790 108.55121 ? 508 GOL A HO2  1 
HETATM 1668 H  H31  . GOL I 4 .   ? 11.22500 36.84100 2.77600   0.790 108.39573 ? 508 GOL A H31  1 
HETATM 1669 H  H32  . GOL I 4 .   ? 12.29000 36.59500 1.66300   0.790 108.39573 ? 508 GOL A H32  1 
HETATM 1670 H  HO3  . GOL I 4 .   ? 13.19400 37.60500 3.39600   0.790 108.44265 ? 508 GOL A HO3  1 
HETATM 1671 O  O    . HOH J 5 .   ? 3.60100  32.81000 -14.33600 0.460 47.56769  ? 601 HOH A O    1 
HETATM 1672 O  O    . HOH J 5 .   ? 9.26400  16.07500 -14.91200 0.920 71.80228  ? 602 HOH A O    1 
HETATM 1673 O  O    . HOH J 5 .   ? 22.76000 22.77700 -24.72600 0.990 39.81475  ? 603 HOH A O    1 
HETATM 1674 O  O    . HOH J 5 .   ? -2.86100 23.20100 -9.02700  0.840 75.01270  ? 604 HOH A O    1 
HETATM 1675 O  O    . HOH J 5 .   ? 16.37200 24.88400 -27.36000 0.770 59.82175  ? 605 HOH A O    1 
HETATM 1676 O  O    . HOH J 5 .   ? 12.94200 32.73400 5.47400   0.990 85.58000  ? 606 HOH A O    1 
HETATM 1677 O  O    . HOH J 5 .   ? 30.32700 14.53100 -23.30800 0.560 62.65716  ? 607 HOH A O    1 
HETATM 1678 O  O    . HOH J 5 .   ? 7.53500  34.82300 17.28900  0.960 78.20079  ? 608 HOH A O    1 
HETATM 1679 O  O    . HOH J 5 .   ? 10.11500 34.81400 -10.09600 0.800 43.68101  ? 609 HOH A O    1 
HETATM 1680 O  O    . HOH J 5 .   ? 21.39100 26.25200 -24.11800 0.680 26.21678  ? 610 HOH A O    1 
HETATM 1681 O  O    . HOH J 5 .   ? 15.77800 14.86800 -33.25100 0.990 67.97967  ? 611 HOH A O    1 
HETATM 1682 O  O    . HOH J 5 .   ? 21.68100 8.78000  -33.29700 0.610 39.18134  ? 612 HOH A O    1 
HETATM 1683 O  O    . HOH J 5 .   ? 11.27500 31.17800 -22.69500 0.290 40.41982  ? 613 HOH A O    1 
HETATM 1684 O  O    . HOH J 5 .   ? 15.72400 16.04200 -23.59500 0.770 48.93766  ? 614 HOH A O    1 
HETATM 1685 O  O    . HOH J 5 .   ? 22.37900 10.21000 -22.78400 0.340 42.64898  ? 615 HOH A O    1 
HETATM 1686 O  O    . HOH J 5 .   ? 11.06500 20.22300 -28.15400 0.930 63.88158  ? 616 HOH A O    1 
HETATM 1687 O  O    . HOH J 5 .   ? 3.44200  36.59100 -5.78600  0.470 38.43852  ? 617 HOH A O    1 
HETATM 1688 O  O    . HOH J 5 .   ? 24.78900 17.94500 -21.23900 0.700 47.52780  ? 618 HOH A O    1 
HETATM 1689 O  O    . HOH J 5 .   ? 22.02000 20.93500 -22.11600 0.910 48.51813  ? 619 HOH A O    1 
HETATM 1690 O  O    . HOH J 5 .   ? 3.71400  16.47600 -5.65000  0.990 65.81236  ? 620 HOH A O    1 
HETATM 1691 O  O    . HOH J 5 .   ? 25.05800 21.24000 -22.01300 0.970 37.33957  ? 621 HOH A O    1 
HETATM 1692 O  O    . HOH J 5 .   ? 20.13400 33.47100 -31.12100 0.820 57.20928  ? 622 HOH A O    1 
HETATM 1693 O  O    . HOH J 5 .   ? 4.53200  17.54400 -2.90500  0.880 52.54425  ? 623 HOH A O    1 
HETATM 1694 O  O    . HOH J 5 .   ? 12.60500 22.20200 10.55800  0.990 98.36692  ? 624 HOH A O    1 
HETATM 1695 O  O    . HOH J 5 .   ? 14.40400 32.12300 1.14200   0.910 64.35650  ? 625 HOH A O    1 
HETATM 1696 O  O    . HOH J 5 .   ? 16.78800 28.08700 -17.74500 0.900 46.93547  ? 626 HOH A O    1 
HETATM 1697 O  O    . HOH J 5 .   ? 8.58300  38.25400 -10.64800 0.640 70.08201  ? 627 HOH A O    1 
HETATM 1698 O  O    . HOH J 5 .   ? 14.44800 16.94800 -21.17600 0.990 57.95512  ? 628 HOH A O    1 
HETATM 1699 O  O    . HOH J 5 .   ? 17.35700 14.56000 -28.48400 0.560 41.95238  ? 629 HOH A O    1 
HETATM 1700 O  O    . HOH J 5 .   ? 12.36700 17.69900 -18.41900 0.990 66.41506  ? 630 HOH A O    1 
HETATM 1701 O  O    . HOH J 5 .   ? 3.08900  40.48000 6.74900   0.920 64.35350  ? 631 HOH A O    1 
HETATM 1702 O  O    . HOH J 5 .   ? 4.23600  25.20500 -22.30200 0.990 62.10213  ? 632 HOH A O    1 
HETATM 1703 O  O    . HOH J 5 .   ? 13.64900 37.90300 6.04200   0.990 86.44164  ? 633 HOH A O    1 
HETATM 1704 O  O    . HOH J 5 .   ? -3.01900 26.31100 -3.32200  0.690 52.82184  ? 634 HOH A O    1 
HETATM 1705 O  O    . HOH J 5 .   ? 5.16300  27.41300 -26.14500 0.890 83.55108  ? 635 HOH A O    1 
HETATM 1706 O  O    . HOH J 5 .   ? 6.54300  27.35200 -22.38900 0.990 65.71409  ? 636 HOH A O    1 
HETATM 1707 O  O    . HOH J 5 .   ? 14.58200 14.42500 -26.25000 0.520 41.95347  ? 637 HOH A O    1 
HETATM 1708 O  O    . HOH J 5 .   ? 1.02100  29.08100 -9.33200  0.760 54.81036  ? 638 HOH A O    1 
HETATM 1709 O  O    . HOH J 5 .   ? 0.71900  21.83900 -21.82100 0.990 74.98021  ? 639 HOH A O    1 
HETATM 1710 O  O    . HOH J 5 .   ? 6.45200  41.10100 1.15700   0.700 50.27069  ? 640 HOH A O    1 
HETATM 1711 O  O    . HOH J 5 .   ? 7.88500  39.98600 -9.19700  0.810 68.08770  ? 641 HOH A O    1 
HETATM 1712 O  O    . HOH J 5 .   ? 12.78500 33.95000 -14.32200 0.970 49.24980  ? 642 HOH A O    1 
HETATM 1713 O  O    . HOH J 5 .   ? 1.86800  21.32700 3.58700   0.940 65.49844  ? 643 HOH A O    1 
HETATM 1714 O  O    . HOH J 5 .   ? 16.31100 31.77100 -19.53600 0.740 46.61166  ? 644 HOH A O    1 
HETATM 1715 O  O    . HOH J 5 .   ? 24.59800 10.51100 -23.56600 0.660 69.07280  ? 645 HOH A O    1 
HETATM 1716 O  O    . HOH J 5 .   ? 0.45100  19.46900 4.25800   0.820 68.28648  ? 646 HOH A O    1 
HETATM 1717 O  O    . HOH J 5 .   ? 18.10100 30.24800 -20.79200 0.990 62.48195  ? 647 HOH A O    1 
HETATM 1718 O  O    . HOH J 5 .   ? 9.78100  24.73300 13.85100  0.990 86.36207  ? 648 HOH A O    1 
HETATM 1719 O  O    . HOH J 5 .   ? 11.34400 29.61200 -23.82700 0.710 56.72003  ? 649 HOH A O    1 
HETATM 1720 O  O    . HOH J 5 .   ? 12.14300 35.97200 -2.92800  0.990 53.66726  ? 650 HOH A O    1 
HETATM 1721 O  O    . HOH J 5 .   ? -0.96900 20.73600 -24.33700 0.990 81.20074  ? 651 HOH A O    1 
HETATM 1722 O  O    . HOH J 5 .   ? -0.90600 19.59700 -17.21300 0.990 60.68427  ? 652 HOH A O    1 
HETATM 1723 O  O    . HOH J 5 .   ? -3.40400 24.43000 -0.03700  0.890 74.16874  ? 653 HOH A O    1 
HETATM 1724 O  O    . HOH J 5 .   ? 16.21800 32.19100 -22.41100 0.990 77.94227  ? 654 HOH A O    1 
HETATM 1725 O  O    . HOH J 5 .   ? 10.89200 39.96900 -4.47200  0.760 67.18989  ? 655 HOH A O    1 
HETATM 1726 O  O    . HOH J 5 .   ? 11.26900 15.57800 -19.71400 0.660 51.34400  ? 656 HOH A O    1 
HETATM 1727 O  O    . HOH J 5 .   ? 0.33700  17.23100 -9.69400  0.850 69.29804  ? 657 HOH A O    1 
HETATM 1728 O  O    . HOH J 5 .   ? 12.95700 32.88600 8.17500   0.990 99.97307  ? 658 HOH A O    1 
HETATM 1729 O  O    . HOH J 5 .   ? 4.23200  18.62300 -28.84100 0.990 67.32387  ? 659 HOH A O    1 
HETATM 1730 O  O    . HOH J 5 .   ? 3.10400  30.68800 -13.56900 0.990 71.92203  ? 660 HOH A O    1 
HETATM 1731 O  O    . HOH J 5 .   ? 10.43600 28.77900 -33.78600 0.680 66.15121  ? 661 HOH A O    1 
HETATM 1732 O  O    . HOH J 5 .   ? -1.13200 28.76300 -11.05700 0.670 49.82851  ? 662 HOH A O    1 
HETATM 1733 O  O    . HOH J 5 .   ? 25.17800 14.67900 -19.40600 0.990 73.96578  ? 663 HOH A O    1 
HETATM 1734 O  O    . HOH J 5 .   ? 5.06800  16.63500 -22.61600 0.990 71.21407  ? 664 HOH A O    1 
HETATM 1735 O  O    . HOH J 5 .   ? -1.02000 27.57300 -17.19500 0.990 92.64562  ? 665 HOH A O    1 
HETATM 1736 O  O    . HOH J 5 .   ? 9.84800  13.95200 -20.14000 0.340 53.69562  ? 666 HOH A O    1 
HETATM 1737 O  O    . HOH J 5 .   ? 5.47700  34.63900 -18.94300 0.970 77.03260  ? 667 HOH A O    1 
HETATM 1738 O  O    . HOH J 5 .   ? 22.22100 18.37600 -20.90500 0.990 74.19600  ? 668 HOH A O    1 
HETATM 1739 O  O    . HOH J 5 .   ? 2.52800  35.25200 -10.30200 0.990 81.54968  ? 669 HOH A O    1 
HETATM 1740 O  O    . HOH J 5 .   ? 19.81900 8.91800  -30.28400 0.990 83.45691  ? 670 HOH A O    1 
HETATM 1741 O  O    . HOH J 5 .   ? 2.26200  31.37900 -10.08100 0.990 77.87833  ? 671 HOH A O    1 
HETATM 1742 O  O    . HOH J 5 .   ? -2.68300 26.96300 -6.44200  0.880 76.69648  ? 672 HOH A O    1 
HETATM 1743 O  O    . HOH J 5 .   ? -0.27100 23.30700 -17.56400 0.990 83.36991  ? 673 HOH A O    1 
HETATM 1744 O  O    . HOH J 5 .   ? 0.52300  29.12300 -19.89700 0.990 78.02808  ? 674 HOH A O    1 
HETATM 1745 O  O    . HOH J 5 .   ? 26.39300 11.07100 -22.19600 0.620 63.83766  ? 675 HOH A O    1 
HETATM 1746 O  O    . HOH J 5 .   ? 17.60000 32.27000 -27.32700 0.960 74.17540  ? 676 HOH A O    1 
HETATM 1747 O  O    . HOH J 5 .   ? 7.54100  28.98900 -25.05700 0.990 75.20361  ? 677 HOH A O    1 
HETATM 1748 O  O    . HOH J 5 .   ? 12.66300 34.72400 -11.34800 0.820 48.01291  ? 678 HOH A O    1 
HETATM 1749 O  O    . HOH J 5 .   ? 15.63700 29.01900 -0.26800  0.990 80.17622  ? 679 HOH A O    1 
HETATM 1750 O  O    . HOH J 5 .   ? 20.63300 8.35200  -25.80800 0.980 82.24659  ? 680 HOH A O    1 
HETATM 1751 O  O    . HOH J 5 .   ? 16.33700 21.98700 -29.10800 0.990 54.48202  ? 681 HOH A O    1 
HETATM 1752 O  O    . HOH J 5 .   ? 22.37700 11.78800 -20.20600 0.990 90.58666  ? 682 HOH A O    1 
HETATM 1753 O  O    . HOH J 5 .   ? 3.87100  42.36400 2.03400   0.990 55.02101  ? 683 HOH A O    1 
HETATM 1754 O  O    . HOH J 5 .   ? 6.44000  13.68300 -22.30300 0.990 78.17085  ? 684 HOH A O    1 
HETATM 1755 O  O    . HOH J 5 .   ? 12.72100 26.88800 9.82400   0.990 84.00780  ? 685 HOH A O    1 
HETATM 1756 O  O    . HOH J 5 .   ? 5.06700  39.32700 -10.42100 0.990 76.63723  ? 686 HOH A O    1 
HETATM 1757 O  O    . HOH J 5 .   ? 10.41100 12.42700 -23.02800 0.990 85.14775  ? 687 HOH A O    1 
HETATM 1758 O  O    . HOH J 5 .   ? 21.71300 15.87900 -18.62300 0.990 89.81653  ? 688 HOH A O    1 
HETATM 1759 O  O    . HOH J 5 .   ? 21.17100 28.52700 -22.24700 0.910 44.49123  ? 689 HOH A O    1 
HETATM 1760 O  O    . HOH J 5 .   ? 15.59700 31.34600 5.07900   0.990 89.46323  ? 690 HOH A O    1 
HETATM 1761 O  O    . HOH J 5 .   ? 13.90500 38.89500 10.80500  0.990 82.00518  ? 691 HOH A O    1 
HETATM 1762 O  O    . HOH J 5 .   ? 6.66000  16.86100 -34.78100 0.560 62.68359  ? 692 HOH A O    1 
HETATM 1763 O  O    . HOH J 5 .   ? 0.30800  37.88200 -12.28100 0.990 71.68618  ? 693 HOH A O    1 
HETATM 1764 O  O    . HOH J 5 .   ? 20.23400 6.87600  -28.58400 0.930 65.74702  ? 694 HOH A O    1 
HETATM 1765 O  O    . HOH J 5 .   ? 1.62600  26.22800 -21.61700 0.890 76.77017  ? 695 HOH A O    1 
HETATM 1766 O  O    . HOH J 5 .   ? 20.54700 31.27200 -22.01100 0.990 50.63033  ? 696 HOH A O    1 
HETATM 1767 O  O    . HOH J 5 .   ? 2.90300  14.07900 -6.74900  0.990 67.75966  ? 697 HOH A O    1 
HETATM 1768 O  O    . HOH J 5 .   ? 7.69000  15.12300 -34.26500 0.440 42.39281  ? 698 HOH A O    1 
HETATM 1769 O  O    . HOH J 5 .   ? 2.45400  17.12900 -32.55500 0.990 72.55504  ? 699 HOH A O    1 
HETATM 1770 O  O    . HOH J 5 .   ? 26.55000 5.11100  -31.60500 0.910 68.71760  ? 700 HOH A O    1 
HETATM 1771 O  O    . HOH J 5 .   ? 17.89700 33.96700 -18.34000 0.790 105.02006 ? 701 HOH A O    1 
HETATM 1772 O  O    . HOH J 5 .   ? 16.47100 10.84300 -21.68600 0.990 78.02189  ? 702 HOH A O    1 
HETATM 1773 O  O    . HOH J 5 .   ? 12.72700 12.55000 -20.60500 0.990 86.51722  ? 703 HOH A O    1 
HETATM 1774 O  O    . HOH J 5 .   ? -1.37900 24.23700 -23.47700 0.970 83.76642  ? 704 HOH A O    1 
HETATM 1775 O  O    . HOH J 5 .   ? 4.95500  43.98300 -0.66200  0.990 80.24181  ? 705 HOH A O    1 
HETATM 1776 O  O    . HOH J 5 .   ? 21.20200 33.56200 -26.63100 0.710 52.53301  ? 706 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   ? 1.53107 1.72151 1.36619 -0.37063 0.05575  -0.10749 325 SER A N    
2    C  CA   . SER A 6   ? 0.89422 1.09296 0.73816 -0.35629 0.03885  -0.10386 325 SER A CA   
3    C  C    . SER A 6   ? 1.52284 1.70735 1.38816 -0.31631 0.01230  -0.09830 325 SER A C    
4    O  O    . SER A 6   ? 0.89664 1.01024 0.74159 -0.30545 0.01763  -0.10616 325 SER A O    
5    C  CB   . SER A 6   ? 1.15052 1.43284 1.01530 -0.36064 0.02558  -0.09315 325 SER A CB   
6    O  OG   . SER A 6   ? 1.37902 1.67579 1.21726 -0.39689 0.04551  -0.10113 325 SER A OG   
7    H  HA   . SER A 6   ? 1.09139 1.09139 1.09139 0.00000  0.00000  0.00000  325 SER A HA   
8    H  HB2  . SER A 6   ? 1.44072 1.44072 1.44072 -0.00000 0.00000  0.00000  325 SER A HB2  
9    H  HB3  . SER A 6   ? 1.44072 1.44072 1.44072 -0.00000 0.00000  0.00000  325 SER A HB3  
10   H  HG   . SER A 6   ? 1.71008 1.71008 1.71008 -0.00000 0.00000  0.00000  325 SER A HG   
11   N  N    . HIS A 7   ? 0.61102 0.85783 0.51202 -0.29068 -0.01445 -0.08430 326 HIS A N    
12   C  CA   . HIS A 7   ? 0.72748 0.96096 0.64561 -0.24883 -0.03933 -0.07869 326 HIS A CA   
13   C  C    . HIS A 7   ? 0.59309 0.83010 0.51690 -0.21551 -0.05102 -0.07252 326 HIS A C    
14   O  O    . HIS A 7   ? 0.68665 0.94240 0.61055 -0.21601 -0.03953 -0.06657 326 HIS A O    
15   C  CB   . HIS A 7   ? 0.61564 0.89275 0.56314 -0.23017 -0.05455 -0.06509 326 HIS A CB   
16   C  CG   . HIS A 7   ? 1.32585 1.57900 1.26488 -0.24184 -0.04726 -0.06885 326 HIS A CG   
17   N  ND1  . HIS A 7   ? 1.20302 1.48036 1.12940 -0.27376 -0.03213 -0.07037 326 HIS A ND1  
18   C  CD2  . HIS A 7   ? 1.02401 1.23374 0.96341 -0.22471 -0.05341 -0.07129 326 HIS A CD2  
19   C  CE1  . HIS A 7   ? 1.25853 1.50826 1.17740 -0.27531 -0.02943 -0.07351 326 HIS A CE1  
20   N  NE2  . HIS A 7   ? 1.62434 1.83380 1.55330 -0.24581 -0.04182 -0.07351 326 HIS A NE2  
21   H  H    . HIS A 7   ? 0.79360 0.79360 0.79360 0.00000  0.00000  0.00000  326 HIS A H    
22   H  HA   . HIS A 7   ? 0.93487 0.93487 0.93487 -0.00000 0.00000  0.00000  326 HIS A HA   
23   H  HB2  . HIS A 7   ? 0.82987 0.82987 0.82987 0.00000  0.00000  -0.00000 326 HIS A HB2  
24   H  HB3  . HIS A 7   ? 0.82987 0.82987 0.82987 0.00000  0.00000  -0.00000 326 HIS A HB3  
25   H  HD2  . HIS A 7   ? 1.28972 1.28972 1.28972 0.00000  0.00000  -0.00000 326 HIS A HD2  
26   H  HE1  . HIS A 7   ? 1.57893 1.57893 1.57893 0.00000  -0.00000 -0.00000 326 HIS A HE1  
27   H  HE2  . HIS A 7   ? 2.00583 2.00583 2.00583 0.00000  -0.00000 0.00000  326 HIS A HE2  
28   N  N    . CYS A 8   ? 0.60390 0.81142 0.53239 -0.17466 -0.06838 -0.06884 327 CYS A N    
29   C  CA   . CYS A 8   ? 0.61343 0.80025 0.54222 -0.12873 -0.07348 -0.05940 327 CYS A CA   
30   C  C    . CYS A 8   ? 0.60721 0.86199 0.56233 -0.11410 -0.08386 -0.04509 327 CYS A C    
31   O  O    . CYS A 8   ? 0.65393 0.95814 0.63294 -0.10941 -0.10167 -0.03866 327 CYS A O    
32   C  CB   . CYS A 8   ? 0.57437 0.72211 0.50182 -0.09647 -0.09059 -0.06091 327 CYS A CB   
33   S  SG   . CYS A 8   ? 0.58757 0.70691 0.51029 -0.04373 -0.09856 -0.05262 327 CYS A SG   
34   H  H    . CYS A 8   ? 0.78034 0.78034 0.78034 0.00000  -0.00000 0.00000  327 CYS A H    
35   H  HA   . CYS A 8   ? 0.78361 0.78361 0.78361 0.00000  0.00000  0.00000  327 CYS A HA   
36   H  HB2  . CYS A 8   ? 0.72057 0.72057 0.72057 0.00000  -0.00000 0.00000  327 CYS A HB2  
37   H  HB3  . CYS A 8   ? 0.72057 0.72057 0.72057 0.00000  -0.00000 0.00000  327 CYS A HB3  
38   N  N    . GLN A 9   ? 0.43293 0.68915 0.38293 -0.10463 -0.07096 -0.03853 328 GLN A N    
39   C  CA   . GLN A 9   ? 0.48678 0.80760 0.46041 -0.09093 -0.07641 -0.02311 328 GLN A CA   
40   C  C    . GLN A 9   ? 0.58646 0.87981 0.54824 -0.06238 -0.06571 -0.01666 328 GLN A C    
41   O  O    . GLN A 9   ? 0.41617 0.65109 0.35188 -0.06231 -0.05064 -0.02393 328 GLN A O    
42   C  CB   . GLN A 9   ? 0.37702 0.77108 0.36567 -0.13282 -0.06903 -0.02034 328 GLN A CB   
43   C  CG   . GLN A 9   ? 0.76117 1.13289 0.72733 -0.16898 -0.04313 -0.03032 328 GLN A CG   
44   C  CD   . GLN A 9   ? 0.96982 1.41581 0.94803 -0.21914 -0.03688 -0.03142 328 GLN A CD   
45   O  OE1  . GLN A 9   ? 0.84214 1.36948 0.84725 -0.21773 -0.04351 -0.01646 328 GLN A OE1  
46   N  NE2  . GLN A 9   ? 1.30938 1.72950 1.26630 -0.26436 -0.02273 -0.04856 328 GLN A NE2  
47   H  H    . GLN A 9   ? 0.60326 0.60326 0.60326 0.00000  -0.00000 -0.00000 328 GLN A H    
48   H  HA   . GLN A 9   ? 0.70317 0.70317 0.70317 0.00000  0.00000  -0.00000 328 GLN A HA   
49   H  HB2  . GLN A 9   ? 0.60676 0.60676 0.60676 0.00000  -0.00000 0.00000  328 GLN A HB2  
50   H  HB3  . GLN A 9   ? 0.60676 0.60676 0.60676 0.00000  -0.00000 0.00000  328 GLN A HB3  
51   H  HG2  . GLN A 9   ? 1.04981 1.04981 1.04981 0.00000  0.00000  -0.00000 328 GLN A HG2  
52   H  HG3  . GLN A 9   ? 1.04981 1.04981 1.04981 0.00000  0.00000  -0.00000 328 GLN A HG3  
53   H  HE21 . GLN A 9   ? 1.72332 1.72332 1.72332 0.00000  -0.00000 -0.00000 328 GLN A HE21 
54   H  HE22 . GLN A 9   ? 1.72332 1.72332 1.72332 0.00000  -0.00000 -0.00000 328 GLN A HE22 
55   N  N    . LYS A 10  ? 0.50145 0.83763 0.48153 -0.03675 -0.07186 -0.00151 329 LYS A N    
56   C  CA   . LYS A 10  ? 0.68571 1.00101 0.65552 -0.00826 -0.06222 0.00582  329 LYS A CA   
57   C  C    . LYS A 10  ? 0.48794 0.82952 0.45633 -0.03389 -0.04156 0.00862  329 LYS A C    
58   O  O    . LYS A 10  ? 0.49149 0.90337 0.48081 -0.06018 -0.03989 0.01489  329 LYS A O    
59   C  CB   . LYS A 10  ? 0.49188 0.83824 0.47874 0.02887  -0.07295 0.02127  329 LYS A CB   
60   C  CG   . LYS A 10  ? 0.77291 1.09240 0.74620 0.06131  -0.06363 0.02826  329 LYS A CG   
61   C  CD   . LYS A 10  ? 0.59297 0.92584 0.57547 0.09986  -0.07165 0.04118  329 LYS A CD   
62   C  CE   . LYS A 10  ? 0.51514 0.92925 0.52727 0.09939  -0.06809 0.06097  329 LYS A CE   
63   N  NZ   . LYS A 10  ? 1.31863 1.73685 1.33390 0.14121  -0.06732 0.07634  329 LYS A NZ   
64   H  H    . LYS A 10  ? 0.72950 0.72950 0.72950 0.00000  -0.00000 0.00000  329 LYS A H    
65   H  HA   . LYS A 10  ? 0.93815 0.93815 0.93815 -0.00000 0.00000  0.00000  329 LYS A HA   
66   H  HB2  . LYS A 10  ? 0.72480 0.72480 0.72480 -0.00000 0.00000  0.00000  329 LYS A HB2  
67   H  HB3  . LYS A 10  ? 0.72480 0.72480 0.72480 -0.00000 0.00000  0.00000  329 LYS A HB3  
68   H  HG2  . LYS A 10  ? 1.04586 1.04586 1.04586 0.00000  -0.00000 0.00000  329 LYS A HG2  
69   H  HG3  . LYS A 10  ? 1.04586 1.04586 1.04586 0.00000  -0.00000 0.00000  329 LYS A HG3  
70   H  HD2  . LYS A 10  ? 0.83897 0.83897 0.83897 -0.00000 0.00000  0.00000  329 LYS A HD2  
71   H  HD3  . LYS A 10  ? 0.83897 0.83897 0.83897 -0.00000 0.00000  0.00000  329 LYS A HD3  
72   H  HE2  . LYS A 10  ? 0.78992 0.78992 0.78992 0.00000  -0.00000 -0.00000 329 LYS A HE2  
73   H  HE3  . LYS A 10  ? 0.78992 0.78992 0.78992 0.00000  -0.00000 -0.00000 329 LYS A HE3  
74   H  HZ1  . LYS A 10  ? 1.75700 1.75700 1.75700 0.00000  -0.00000 0.00000  329 LYS A HZ1  
75   H  HZ2  . LYS A 10  ? 1.75700 1.75700 1.75700 0.00000  -0.00000 0.00000  329 LYS A HZ2  
76   H  HZ3  . LYS A 10  ? 1.75700 1.75700 1.75700 0.00000  -0.00000 0.00000  329 LYS A HZ3  
77   N  N    . THR A 11  ? 0.48209 0.76991 0.42515 -0.02726 -0.02521 0.00436  330 THR A N    
78   C  CA   . THR A 11  ? 0.60507 0.90696 0.54243 -0.04893 -0.00274 0.00629  330 THR A CA   
79   C  C    . THR A 11  ? 0.50371 0.78007 0.43022 -0.01216 0.00477  0.01525  330 THR A C    
80   O  O    . THR A 11  ? 0.47874 0.71609 0.39556 0.02529  -0.00548 0.01650  330 THR A O    
81   C  CB   . THR A 11  ? 0.68026 0.93397 0.59101 -0.08474 0.01740  -0.00922 330 THR A CB   
82   O  OG1  . THR A 11  ? 0.82592 0.99880 0.70783 -0.05836 0.02304  -0.01404 330 THR A OG1  
83   C  CG2  . THR A 11  ? 0.99900 1.26631 0.91506 -0.11930 0.01012  -0.01998 330 THR A CG2  
84   H  H    . THR A 11  ? 0.67212 0.67212 0.67212 0.00000  0.00000  -0.00000 330 THR A H    
85   H  HA   . THR A 11  ? 0.82304 0.82304 0.82304 -0.00000 -0.00000 0.00000  330 THR A HA   
86   H  HB   . THR A 11  ? 0.88335 0.88335 0.88335 0.00000  0.00000  0.00000  330 THR A HB   
87   H  HG1  . THR A 11  ? 1.01428 1.01428 1.01428 -0.00000 -0.00000 0.00000  330 THR A HG1  
88   H  HG21 . THR A 11  ? 1.27340 1.27340 1.27340 0.00000  0.00000  0.00000  330 THR A HG21 
89   H  HG22 . THR A 11  ? 1.27340 1.27340 1.27340 0.00000  0.00000  0.00000  330 THR A HG22 
90   H  HG23 . THR A 11  ? 1.27340 1.27340 1.27340 0.00000  0.00000  0.00000  330 THR A HG23 
91   N  N    . SER A 12  ? 0.55249 0.85243 0.47927 -0.02532 0.02343  0.02084  331 SER A N    
92   C  CA   . SER A 12  ? 0.59549 0.87971 0.51391 0.00740  0.03206  0.03085  331 SER A CA   
93   C  C    . SER A 12  ? 0.69625 0.89684 0.57862 0.02192  0.04425  0.02265  331 SER A C    
94   O  O    . SER A 12  ? 0.75852 0.92265 0.62140 -0.00414 0.06038  0.01217  331 SER A O    
95   C  CB   . SER A 12  ? 0.54700 0.88666 0.47829 -0.01293 0.04911  0.04007  331 SER A CB   
96   O  OG   . SER A 12  ? 0.94809 1.26635 0.86825 0.01750  0.06013  0.04903  331 SER A OG   
97   H  H    . SER A 12  ? 0.75493 0.75493 0.75493 0.00000  -0.00000 0.00000  331 SER A H    
98   H  HA   . SER A 12  ? 0.79690 0.79690 0.79690 -0.00000 -0.00000 -0.00000 331 SER A HA   
99   H  HB2  . SER A 12  ? 0.76603 0.76603 0.76603 0.00000  -0.00000 -0.00000 331 SER A HB2  
100  H  HB3  . SER A 12  ? 0.76603 0.76603 0.76603 0.00000  -0.00000 -0.00000 331 SER A HB3  
101  H  HG   . SER A 12  ? 1.23433 1.23433 1.23433 0.00000  0.00000  -0.00000 331 SER A HG   
102  N  N    . LEU A 13  ? 0.60154 0.77205 0.47302 0.06410  0.03823  0.02830  332 LEU A N    
103  C  CA   . LEU A 13  ? 0.54038 0.64267 0.37839 0.08329  0.04990  0.02484  332 LEU A CA   
104  C  C    . LEU A 13  ? 0.56328 0.66513 0.39648 0.11918  0.05095  0.03572  332 LEU A C    
105  O  O    . LEU A 13  ? 0.57720 0.67545 0.41122 0.14834  0.03413  0.03813  332 LEU A O    
106  C  CB   . LEU A 13  ? 0.65479 0.70955 0.47726 0.09619  0.03658  0.01604  332 LEU A CB   
107  C  CG   . LEU A 13  ? 0.77299 0.76734 0.56215 0.12265  0.04590  0.01627  332 LEU A CG   
108  C  CD1  . LEU A 13  ? 0.81209 0.77360 0.58049 0.10307  0.07536  0.01464  332 LEU A CD1  
109  C  CD2  . LEU A 13  ? 0.77395 0.73624 0.55219 0.14021  0.02843  0.01051  332 LEU A CD2  
110  H  H    . LEU A 13  ? 0.73990 0.73990 0.73990 0.00000  -0.00000 0.00000  332 LEU A H    
111  H  HA   . LEU A 13  ? 0.62583 0.62583 0.62583 -0.00000 0.00000  -0.00000 332 LEU A HA   
112  H  HB2  . LEU A 13  ? 0.73789 0.73789 0.73789 -0.00000 -0.00000 0.00000  332 LEU A HB2  
113  H  HB3  . LEU A 13  ? 0.73789 0.73789 0.73789 -0.00000 -0.00000 0.00000  332 LEU A HB3  
114  H  HG   . LEU A 13  ? 0.84224 0.84224 0.84224 0.00000  0.00000  0.00000  332 LEU A HG   
115  H  HD11 . LEU A 13  ? 0.86773 0.86773 0.86773 -0.00000 0.00000  -0.00000 332 LEU A HD11 
116  H  HD12 . LEU A 13  ? 0.86773 0.86773 0.86773 -0.00000 0.00000  -0.00000 332 LEU A HD12 
117  H  HD13 . LEU A 13  ? 0.86773 0.86773 0.86773 -0.00000 0.00000  -0.00000 332 LEU A HD13 
118  H  HD21 . LEU A 13  ? 0.82621 0.82621 0.82621 0.00000  -0.00000 -0.00000 332 LEU A HD21 
119  H  HD22 . LEU A 13  ? 0.82621 0.82621 0.82621 0.00000  -0.00000 -0.00000 332 LEU A HD22 
120  H  HD23 . LEU A 13  ? 0.82621 0.82621 0.82621 0.00000  -0.00000 -0.00000 332 LEU A HD23 
121  N  N    . ARG A 14  ? 0.65161 0.75448 0.47751 0.11543  0.07242  0.04148  333 ARG A N    
122  C  CA   . ARG A 14  ? 0.70938 0.80836 0.52771 0.14790  0.07713  0.05189  333 ARG A CA   
123  C  C    . ARG A 14  ? 0.64996 0.68173 0.43182 0.17172  0.08343  0.04834  333 ARG A C    
124  O  O    . ARG A 14  ? 0.83848 0.83620 0.60110 0.15887  0.10215  0.04478  333 ARG A O    
125  C  CB   . ARG A 14  ? 0.76210 0.90064 0.59223 0.13265  0.09717  0.06120  333 ARG A CB   
126  C  CG   . ARG A 14  ? 1.62718 1.77228 1.45512 0.16613  0.10160  0.07415  333 ARG A CG   
127  C  CD   . ARG A 14  ? 1.23416 1.44233 1.08649 0.15116  0.11545  0.08664  333 ARG A CD   
128  N  NE   . ARG A 14  ? 1.46638 1.68375 1.31915 0.18652  0.11882  0.10089  333 ARG A NE   
129  C  CZ   . ARG A 14  ? 1.59418 1.84037 1.46289 0.21019  0.10632  0.11075  333 ARG A CZ   
130  N  NH1  . ARG A 14  ? 0.88779 1.16043 0.77548 0.20313  0.08824  0.10866  333 ARG A NH1  
131  N  NH2  . ARG A 14  ? 1.54399 1.78906 1.40733 0.24240  0.11442  0.12345  333 ARG A NH2  
132  H  H    . ARG A 14  ? 0.75469 0.75469 0.75469 -0.00000 0.00000  0.00000  333 ARG A H    
133  H  HA   . ARG A 14  ? 0.81944 0.81944 0.81944 -0.00000 0.00000  0.00000  333 ARG A HA   
134  H  HB2  . ARG A 14  ? 0.90324 0.90324 0.90324 0.00000  0.00000  -0.00000 333 ARG A HB2  
135  H  HB3  . ARG A 14  ? 0.90324 0.90324 0.90324 0.00000  0.00000  -0.00000 333 ARG A HB3  
136  H  HG2  . ARG A 14  ? 1.94309 1.94309 1.94309 -0.00000 0.00000  0.00000  333 ARG A HG2  
137  H  HG3  . ARG A 14  ? 1.94309 1.94309 1.94309 -0.00000 0.00000  0.00000  333 ARG A HG3  
138  H  HD2  . ARG A 14  ? 1.50645 1.50645 1.50645 -0.00000 0.00000  0.00000  333 ARG A HD2  
139  H  HD3  . ARG A 14  ? 1.50645 1.50645 1.50645 -0.00000 0.00000  0.00000  333 ARG A HD3  
140  H  HE   . ARG A 14  ? 1.78897 1.78897 1.78897 0.00000  -0.00000 -0.00000 333 ARG A HE   
141  H  HH11 . ARG A 14  ? 1.13073 1.13073 1.13073 0.00000  0.00000  0.00000  333 ARG A HH11 
142  H  HH12 . ARG A 14  ? 1.13073 1.13073 1.13073 0.00000  0.00000  0.00000  333 ARG A HH12 
143  H  HH21 . ARG A 14  ? 1.89741 1.89741 1.89741 0.00000  -0.00000 0.00000  333 ARG A HH21 
144  H  HH22 . ARG A 14  ? 1.89741 1.89741 1.89741 0.00000  -0.00000 0.00000  333 ARG A HH22 
145  N  N    . VAL A 15  ? 0.63028 0.64366 0.40070 0.20580  0.06953  0.04980  334 VAL A N    
146  C  CA   . VAL A 15  ? 0.61787 0.57722 0.35462 0.22932  0.06985  0.04665  334 VAL A CA   
147  C  C    . VAL A 15  ? 0.70210 0.65017 0.42137 0.25510  0.08116  0.05506  334 VAL A C    
148  O  O    . VAL A 15  ? 0.74964 0.72146 0.47865 0.26912  0.07664  0.06087  334 VAL A O    
149  C  CB   . VAL A 15  ? 0.66189 0.60913 0.39437 0.24406  0.04491  0.03944  334 VAL A CB   
150  C  CG1  . VAL A 15  ? 0.72995 0.63407 0.42807 0.26977  0.04386  0.03823  334 VAL A CG1  
151  C  CG2  . VAL A 15  ? 0.77001 0.72201 0.51639 0.21958  0.03580  0.03130  334 VAL A CG2  
152  H  H    . VAL A 15  ? 0.67111 0.67111 0.67111 0.00000  -0.00000 0.00000  334 VAL A H    
153  H  HA   . VAL A 15  ? 0.62114 0.62114 0.62114 0.00000  -0.00000 -0.00000 334 VAL A HA   
154  H  HB   . VAL A 15  ? 0.66741 0.66741 0.66741 0.00000  0.00000  0.00000  334 VAL A HB   
155  H  HG11 . VAL A 15  ? 0.71809 0.71809 0.71809 0.00000  -0.00000 0.00000  334 VAL A HG11 
156  H  HG12 . VAL A 15  ? 0.71809 0.71809 0.71809 0.00000  -0.00000 0.00000  334 VAL A HG12 
157  H  HG13 . VAL A 15  ? 0.71809 0.71809 0.71809 0.00000  -0.00000 0.00000  334 VAL A HG13 
158  H  HG21 . VAL A 15  ? 0.80462 0.80462 0.80462 0.00000  0.00000  -0.00000 334 VAL A HG21 
159  H  HG22 . VAL A 15  ? 0.80462 0.80462 0.80462 0.00000  0.00000  -0.00000 334 VAL A HG22 
160  H  HG23 . VAL A 15  ? 0.80462 0.80462 0.80462 0.00000  0.00000  -0.00000 334 VAL A HG23 
161  N  N    . ASN A 16  ? 0.78995 0.69979 0.48169 0.26292  0.09768  0.05675  335 ASN A N    
162  C  CA   . ASN A 16  ? 1.07306 0.96632 0.74320 0.28798  0.10948  0.06433  335 ASN A CA   
163  C  C    . ASN A 16  ? 0.72143 0.57954 0.36054 0.31571  0.09792  0.06146  335 ASN A C    
164  O  O    . ASN A 16  ? 0.75832 0.59057 0.38209 0.31577  0.09811  0.05884  335 ASN A O    
165  C  CB   . ASN A 16  ? 0.85849 0.73644 0.51833 0.27694  0.13869  0.06965  335 ASN A CB   
166  C  CG   . ASN A 16  ? 1.63403 1.49371 1.27066 0.30306  0.15235  0.07814  335 ASN A CG   
167  O  OD1  . ASN A 16  ? 0.93114 0.75907 0.53873 0.32888  0.14819  0.07861  335 ASN A OD1  
168  N  ND2  . ASN A 16  ? 0.92207 0.80478 0.57080 0.29579  0.16903  0.08542  335 ASN A ND2  
169  H  H    . ASN A 16  ? 0.78983 0.78983 0.78983 -0.00000 0.00000  0.00000  335 ASN A H    
170  H  HA   . ASN A 16  ? 1.11429 1.11429 1.11429 -0.00000 -0.00000 0.00000  335 ASN A HA   
171  H  HB2  . ASN A 16  ? 0.84656 0.84656 0.84656 -0.00000 -0.00000 0.00000  335 ASN A HB2  
172  H  HB3  . ASN A 16  ? 0.84656 0.84656 0.84656 -0.00000 -0.00000 0.00000  335 ASN A HB3  
173  H  HD21 . ASN A 16  ? 0.92031 0.92031 0.92031 0.00000  -0.00000 -0.00000 335 ASN A HD21 
174  H  HD22 . ASN A 16  ? 0.92031 0.92031 0.92031 0.00000  -0.00000 -0.00000 335 ASN A HD22 
175  N  N    . PHE A 17  ? 0.86291 0.72161 0.49131 0.33868  0.08945  0.06258  336 PHE A N    
176  C  CA   . PHE A 17  ? 0.85317 0.68679 0.45171 0.36040  0.07589  0.05789  336 PHE A CA   
177  C  C    . PHE A 17  ? 0.87785 0.68167 0.44449 0.37510  0.09067  0.06400  336 PHE A C    
178  O  O    . PHE A 17  ? 0.94208 0.73665 0.48926 0.37616  0.07973  0.06087  336 PHE A O    
179  C  CB   . PHE A 17  ? 0.92056 0.76020 0.51171 0.37206  0.06647  0.05533  336 PHE A CB   
180  C  CG   . PHE A 17  ? 0.92304 0.78548 0.53924 0.36382  0.05158  0.04984  336 PHE A CG   
181  C  CD1  . PHE A 17  ? 0.95931 0.82268 0.57969 0.35201  0.03168  0.03829  336 PHE A CD1  
182  C  CD2  . PHE A 17  ? 0.81393 0.69944 0.45014 0.36834  0.05925  0.05760  336 PHE A CD2  
183  C  CE1  . PHE A 17  ? 0.89118 0.77361 0.53384 0.34384  0.01980  0.03369  336 PHE A CE1  
184  C  CE2  . PHE A 17  ? 0.88621 0.79396 0.54471 0.36199  0.04755  0.05518  336 PHE A CE2  
185  C  CZ   . PHE A 17  ? 0.73263 0.63650 0.39344 0.34916  0.02800  0.04260  336 PHE A CZ   
186  H  H    . PHE A 17  ? 0.83158 0.83158 0.83158 -0.00000 0.00000  0.00000  336 PHE A H    
187  H  HA   . PHE A 17  ? 0.79792 0.79792 0.79792 -0.00000 -0.00000 -0.00000 336 PHE A HA   
188  H  HB2  . PHE A 17  ? 0.87824 0.87824 0.87824 0.00000  -0.00000 0.00000  336 PHE A HB2  
189  H  HB3  . PHE A 17  ? 0.87824 0.87824 0.87824 0.00000  -0.00000 0.00000  336 PHE A HB3  
190  H  HD1  . PHE A 17  ? 0.94592 0.94592 0.94592 0.00000  -0.00000 -0.00000 336 PHE A HD1  
191  H  HD2  . PHE A 17  ? 0.78666 0.78666 0.78666 0.00000  0.00000  0.00000  336 PHE A HD2  
192  H  HE1  . PHE A 17  ? 0.88071 0.88071 0.88071 -0.00000 0.00000  0.00000  336 PHE A HE1  
193  H  HE2  . PHE A 17  ? 0.89121 0.89121 0.89121 0.00000  -0.00000 -0.00000 336 PHE A HE2  
194  H  HZ   . PHE A 17  ? 0.70628 0.70628 0.70628 0.00000  -0.00000 0.00000  336 PHE A HZ   
195  N  N    . GLU A 18  ? 1.06205 0.85984 0.62547 0.37588  0.11494  0.07277  337 GLU A N    
196  C  CA   . GLU A 18  ? 1.13260 0.90153 0.66703 0.38683  0.13066  0.08104  337 GLU A CA   
197  C  C    . GLU A 18  ? 0.99899 0.74980 0.52995 0.37929  0.13794  0.08121  337 GLU A C    
198  O  O    . GLU A 18  ? 0.96805 0.70368 0.47635 0.38738  0.13529  0.08753  337 GLU A O    
199  C  CB   . GLU A 18  ? 1.14274 0.90681 0.67528 0.38869  0.15797  0.08970  337 GLU A CB   
200  C  CG   . GLU A 18  ? 1.82106 1.55388 1.32842 0.39567  0.17482  0.10121  337 GLU A CG   
201  C  CD   . GLU A 18  ? 1.97913 1.70727 1.48594 0.39638  0.19955  0.10947  337 GLU A CD   
202  O  OE1  . GLU A 18  ? 1.40725 1.15402 0.92135 0.40211  0.19635  0.11008  337 GLU A OE1  
203  O  OE2  . GLU A 18  ? 1.33994 1.04426 0.83884 0.39058  0.22348  0.11596  337 GLU A OE2  
204  H  H    . GLU A 18  ? 1.02020 1.02020 1.02020 0.00000  0.00000  -0.00000 337 GLU A H    
205  H  HA   . GLU A 18  ? 1.08172 1.08172 1.08172 0.00000  -0.00000 -0.00000 337 GLU A HA   
206  H  HB2  . GLU A 18  ? 1.09119 1.09119 1.09119 0.00000  0.00000  -0.00000 337 GLU A HB2  
207  H  HB3  . GLU A 18  ? 1.09119 1.09119 1.09119 0.00000  0.00000  -0.00000 337 GLU A HB3  
208  H  HG2  . GLU A 18  ? 1.88260 1.88260 1.88260 -0.00000 -0.00000 0.00000  337 GLU A HG2  
209  H  HG3  . GLU A 18  ? 1.88260 1.88260 1.88260 -0.00000 -0.00000 0.00000  337 GLU A HG3  
210  N  N    . ASP A 19  ? 1.13047 0.89090 0.68692 0.35208  0.14328  0.07668  338 ASP A N    
211  C  CA   . ASP A 19  ? 1.06064 0.79897 0.61270 0.34012  0.15409  0.07676  338 ASP A CA   
212  C  C    . ASP A 19  ? 0.96267 0.69826 0.50828 0.35142  0.13201  0.07351  338 ASP A C    
213  O  O    . ASP A 19  ? 0.95339 0.66436 0.48508 0.35443  0.14324  0.07819  338 ASP A O    
214  C  CB   . ASP A 19  ? 0.94994 0.70379 0.53061 0.30239  0.16134  0.07031  338 ASP A CB   
215  C  CG   . ASP A 19  ? 1.77598 1.53461 1.36184 0.28569  0.18745  0.07403  338 ASP A CG   
216  O  OD1  . ASP A 19  ? 1.42776 1.17242 0.99481 0.30498  0.20161  0.08215  338 ASP A OD1  
217  O  OD2  . ASP A 19  ? 1.11106 0.89010 0.71936 0.25177  0.19388  0.06871  338 ASP A OD2  
218  H  H    . ASP A 19  ? 1.08457 1.08457 1.08457 0.00000  0.00000  0.00000  338 ASP A H    
219  H  HA   . ASP A 19  ? 0.99017 0.99017 0.99017 -0.00000 0.00000  0.00000  338 ASP A HA   
220  H  HB2  . ASP A 19  ? 0.87499 0.87499 0.87499 -0.00000 0.00000  0.00000  338 ASP A HB2  
221  H  HB3  . ASP A 19  ? 0.87499 0.87499 0.87499 -0.00000 0.00000  0.00000  338 ASP A HB3  
222  N  N    . ILE A 20  ? 0.92616 0.68553 0.48047 0.35758  0.10320  0.06624  339 ILE A N    
223  C  CA   . ILE A 20  ? 1.21096 0.97853 0.76337 0.35757  0.08012  0.06076  339 ILE A CA   
224  C  C    . ILE A 20  ? 0.98261 0.76223 0.51507 0.36823  0.06882  0.05678  339 ILE A C    
225  O  O    . ILE A 20  ? 0.91342 0.70835 0.44995 0.36519  0.05059  0.04595  339 ILE A O    
226  C  CB   . ILE A 20  ? 0.91738 0.70600 0.49792 0.34417  0.05810  0.04971  339 ILE A CB   
227  C  CG1  . ILE A 20  ? 0.87790 0.68848 0.46600 0.34540  0.04456  0.04365  339 ILE A CG1  
228  C  CG2  . ILE A 20  ? 0.96969 0.76280 0.57547 0.31532  0.07076  0.04791  339 ILE A CG2  
229  C  CD1  . ILE A 20  ? 0.88826 0.71994 0.49863 0.33265  0.02165  0.03245  339 ILE A CD1  
230  H  H    . ILE A 20  ? 0.83812 0.83812 0.83812 -0.00000 -0.00000 0.00000  339 ILE A H    
231  H  HA   . ILE A 20  ? 1.18239 1.18239 1.18239 0.00000  0.00000  -0.00000 339 ILE A HA   
232  H  HB   . ILE A 20  ? 0.84977 0.84977 0.84977 -0.00000 0.00000  0.00000  339 ILE A HB   
233  H  HG12 . ILE A 20  ? 0.81421 0.81421 0.81421 -0.00000 0.00000  -0.00000 339 ILE A HG12 
234  H  HG13 . ILE A 20  ? 0.81421 0.81421 0.81421 -0.00000 0.00000  -0.00000 339 ILE A HG13 
235  H  HG21 . ILE A 20  ? 0.92444 0.92444 0.92444 0.00000  0.00000  0.00000  339 ILE A HG21 
236  H  HG22 . ILE A 20  ? 0.92444 0.92444 0.92444 0.00000  0.00000  0.00000  339 ILE A HG22 
237  H  HG23 . ILE A 20  ? 0.92444 0.92444 0.92444 0.00000  0.00000  0.00000  339 ILE A HG23 
238  H  HD11 . ILE A 20  ? 0.84398 0.84398 0.84398 0.00000  -0.00000 -0.00000 339 ILE A HD11 
239  H  HD12 . ILE A 20  ? 0.84398 0.84398 0.84398 0.00000  -0.00000 -0.00000 339 ILE A HD12 
240  H  HD13 . ILE A 20  ? 0.84398 0.84398 0.84398 0.00000  -0.00000 -0.00000 339 ILE A HD13 
241  N  N    . GLY A 21  ? 1.07200 0.84432 0.58432 0.38109  0.08144  0.06349  340 GLY A N    
242  C  CA   . GLY A 21  ? 0.90281 0.68286 0.39429 0.39461  0.07602  0.05772  340 GLY A CA   
243  C  C    . GLY A 21  ? 1.46187 1.25712 0.95940 0.39290  0.05604  0.04310  340 GLY A C    
244  O  O    . GLY A 21  ? 0.96389 0.76716 0.45778 0.39951  0.04540  0.03482  340 GLY A O    
245  H  H    . GLY A 21  ? 1.00151 1.00151 1.00151 -0.00000 0.00000  0.00000  340 GLY A H    
246  H  HA2  . GLY A 21  ? 0.79324 0.79324 0.79324 -0.00000 0.00000  0.00000  340 GLY A HA2  
247  H  HA3  . GLY A 21  ? 0.79324 0.79324 0.79324 -0.00000 0.00000  0.00000  340 GLY A HA3  
248  N  N    . TRP A 22  ? 0.86084 0.65986 0.37105 0.38475  0.05160  0.04146  341 TRP A N    
249  C  CA   . TRP A 22  ? 0.76631 0.57229 0.27540 0.38487  0.03789  0.02959  341 TRP A CA   
250  C  C    . TRP A 22  ? 0.91413 0.71284 0.41083 0.39376  0.04788  0.03688  341 TRP A C    
251  O  O    . TRP A 22  ? 0.90579 0.70349 0.39824 0.39499  0.03949  0.02997  341 TRP A O    
252  C  CB   . TRP A 22  ? 0.90446 0.72331 0.44342 0.36865  0.02490  0.02413  341 TRP A CB   
253  C  CG   . TRP A 22  ? 1.00833 0.83483 0.55957 0.35810  0.00877  0.01334  341 TRP A CG   
254  C  CD1  . TRP A 22  ? 1.14624 0.97259 0.69163 0.36098  0.00714  0.01176  341 TRP A CD1  
255  C  CD2  . TRP A 22  ? 0.83788 0.67557 0.41210 0.34354  -0.00680 0.00419  341 TRP A CD2  
256  N  NE1  . TRP A 22  ? 0.86558 0.70274 0.42981 0.34806  -0.00873 0.00264  341 TRP A NE1  
257  C  CE2  . TRP A 22  ? 0.92718 0.76948 0.50790 0.33676  -0.01759 -0.00304 341 TRP A CE2  
258  C  CE3  . TRP A 22  ? 0.80510 0.65138 0.39707 0.33651  -0.01112 0.00290  341 TRP A CE3  
259  C  CZ2  . TRP A 22  ? 0.76901 0.62099 0.37120 0.32174  -0.03285 -0.01257 341 TRP A CZ2  
260  C  CZ3  . TRP A 22  ? 0.90980 0.76562 0.52161 0.32270  -0.02612 -0.00658 341 TRP A CZ3  
261  C  CH2  . TRP A 22  ? 0.92505 0.78203 0.54098 0.31474  -0.03699 -0.01487 341 TRP A CH2  
262  H  H    . TRP A 22  ? 0.75795 0.75795 0.75795 0.00000  0.00000  0.00000  341 TRP A H    
263  H  HA   . TRP A 22  ? 0.64685 0.64685 0.64685 0.00000  0.00000  0.00000  341 TRP A HA   
264  H  HB2  . TRP A 22  ? 0.82973 0.82973 0.82973 0.00000  0.00000  0.00000  341 TRP A HB2  
265  H  HB3  . TRP A 22  ? 0.82973 0.82973 0.82973 0.00000  0.00000  0.00000  341 TRP A HB3  
266  H  HD1  . TRP A 22  ? 1.12544 1.12544 1.12544 0.00000  0.00000  0.00000  341 TRP A HD1  
267  H  HE1  . TRP A 22  ? 0.80051 0.80051 0.80051 0.00000  -0.00000 -0.00000 341 TRP A HE1  
268  H  HE3  . TRP A 22  ? 0.74267 0.74267 0.74267 -0.00000 -0.00000 0.00000  341 TRP A HE3  
269  H  HZ2  . TRP A 22  ? 0.70573 0.70573 0.70573 -0.00000 0.00000  0.00000  341 TRP A HZ2  
270  H  HZ3  . TRP A 22  ? 0.88007 0.88007 0.88007 0.00000  0.00000  0.00000  341 TRP A HZ3  
271  H  HH2  . TRP A 22  ? 0.90048 0.90048 0.90048 0.00000  0.00000  0.00000  341 TRP A HH2  
272  N  N    . ASP A 23  ? 1.03603 0.82637 0.52582 0.40026  0.06695  0.05163  342 ASP A N    
273  C  CA   . ASP A 23  ? 1.02434 0.80813 0.50388 0.40949  0.07828  0.06031  342 ASP A CA   
274  C  C    . ASP A 23  ? 1.15424 0.92854 0.61437 0.41812  0.07327  0.05630  342 ASP A C    
275  O  O    . ASP A 23  ? 1.13035 0.89608 0.57964 0.42603  0.07996  0.06196  342 ASP A O    
276  C  CB   . ASP A 23  ? 1.42548 1.20183 0.91047 0.41250  0.10073  0.07590  342 ASP A CB   
277  C  CG   . ASP A 23  ? 1.40499 1.16668 0.87263 0.41719  0.10845  0.08193  342 ASP A CG   
278  O  OD1  . ASP A 23  ? 1.58675 1.35315 1.05116 0.41633  0.09533  0.07211  342 ASP A OD1  
279  O  OD2  . ASP A 23  ? 1.48529 1.23267 0.95079 0.42058  0.12913  0.09535  342 ASP A OD2  
280  H  H    . ASP A 23  ? 0.95655 0.95655 0.95655 0.00000  0.00000  0.00000  342 ASP A H    
281  H  HA   . ASP A 23  ? 0.93579 0.93579 0.93579 0.00000  -0.00000 -0.00000 342 ASP A HA   
282  H  HB2  . ASP A 23  ? 1.41637 1.41637 1.41637 -0.00000 -0.00000 -0.00000 342 ASP A HB2  
283  H  HB3  . ASP A 23  ? 1.41637 1.41637 1.41637 -0.00000 -0.00000 -0.00000 342 ASP A HB3  
284  N  N    . SER A 24  ? 1.14579 0.92202 0.60217 0.42005  0.06431  0.04656  343 SER A N    
285  C  CA   . SER A 24  ? 1.62655 1.39385 1.07130 0.43533  0.05839  0.04247  343 SER A CA   
286  C  C    . SER A 24  ? 1.50172 1.26249 0.94036 0.43469  0.04457  0.03407  343 SER A C    
287  O  O    . SER A 24  ? 1.46344 1.20867 0.87830 0.44690  0.04461  0.03431  343 SER A O    
288  C  CB   . SER A 24  ? 1.69588 1.47188 1.13551 0.44322  0.05384  0.03995  343 SER A CB   
289  O  OG   . SER A 24  ? 1.79705 1.58738 1.25112 0.43363  0.04075  0.03052  343 SER A OG   
290  H  H    . SER A 24  ? 1.06924 1.06924 1.06924 0.00000  0.00000  -0.00000 343 SER A H    
291  H  HA   . SER A 24  ? 1.63794 1.63794 1.63794 0.00000  -0.00000 0.00000  343 SER A HA   
292  H  HB2  . SER A 24  ? 1.72256 1.72256 1.72256 0.00000  0.00000  0.00000  343 SER A HB2  
293  H  HB3  . SER A 24  ? 1.72256 1.72256 1.72256 0.00000  0.00000  0.00000  343 SER A HB3  
294  H  HG   . SER A 24  ? 1.85547 1.85547 1.85547 -0.00000 -0.00000 0.00000  343 SER A HG   
295  N  N    . TRP A 25  ? 0.95538 0.72435 0.41083 0.42162  0.03541  0.02675  344 TRP A N    
296  C  CA   . TRP A 25  ? 1.16985 0.92882 0.61608 0.42090  0.02281  0.01808  344 TRP A CA   
297  C  C    . TRP A 25  ? 1.49491 1.25654 0.94807 0.41208  0.02764  0.02351  344 TRP A C    
298  O  O    . TRP A 25  ? 1.31000 1.05504 0.74831 0.41665  0.02674  0.02127  344 TRP A O    
299  C  CB   . TRP A 25  ? 1.06264 0.82866 0.51340 0.41709  0.00393  0.00299  344 TRP A CB   
300  C  CG   . TRP A 25  ? 1.19837 0.98149 0.67713 0.40041  -0.00329 -0.00291 344 TRP A CG   
301  C  CD1  . TRP A 25  ? 2.03903 1.83821 1.53461 0.39290  -0.00039 -0.00142 344 TRP A CD1  
302  C  CD2  . TRP A 25  ? 1.36699 1.14906 0.85503 0.39032  -0.01425 -0.01100 344 TRP A CD2  
303  N  NE1  . TRP A 25  ? 1.63880 1.44777 1.15383 0.37854  -0.00968 -0.00854 344 TRP A NE1  
304  C  CE2  . TRP A 25  ? 1.78334 1.58424 1.29688 0.37624  -0.01833 -0.01509 344 TRP A CE2  
305  C  CE3  . TRP A 25  ? 1.28424 1.04728 0.75635 0.39287  -0.01904 -0.01409 344 TRP A CE3  
306  C  CZ2  . TRP A 25  ? 1.44165 1.24723 0.97076 0.36402  -0.02843 -0.02288 344 TRP A CZ2  
307  C  CZ3  . TRP A 25  ? 1.44633 1.21265 0.93259 0.38137  -0.02777 -0.02040 344 TRP A CZ3  
308  C  CH2  . TRP A 25  ? 1.64203 1.43160 1.15980 0.36678  -0.03301 -0.02508 344 TRP A CH2  
309  H  H    . TRP A 25  ? 0.83748 0.83748 0.83748 -0.00000 0.00000  0.00000  344 TRP A H    
310  H  HA   . TRP A 25  ? 1.08716 1.08716 1.08716 0.00000  -0.00000 -0.00000 344 TRP A HA   
311  H  HB2  . TRP A 25  ? 0.96314 0.96314 0.96314 0.00000  0.00000  0.00000  344 TRP A HB2  
312  H  HB3  . TRP A 25  ? 0.96314 0.96314 0.96314 0.00000  0.00000  0.00000  344 TRP A HB3  
313  H  HD1  . TRP A 25  ? 2.16599 2.16599 2.16599 -0.00000 0.00000  0.00000  344 TRP A HD1  
314  H  HE1  . TRP A 25  ? 1.69742 1.69742 1.69742 -0.00000 -0.00000 0.00000  344 TRP A HE1  
315  H  HE3  . TRP A 25  ? 1.23640 1.23640 1.23640 0.00000  0.00000  -0.00000 344 TRP A HE3  
316  H  HZ2  . TRP A 25  ? 1.46511 1.46511 1.46511 0.00000  0.00000  0.00000  344 TRP A HZ2  
317  H  HZ3  . TRP A 25  ? 1.43788 1.43788 1.43788 0.00000  0.00000  0.00000  344 TRP A HZ3  
318  H  HH2  . TRP A 25  ? 1.69463 1.69463 1.69463 -0.00000 -0.00000 0.00000  344 TRP A HH2  
319  N  N    . ILE A 26  ? 0.98678 0.76612 0.45702 0.40461  0.03695  0.02879  345 ILE A N    
320  C  CA   . ILE A 26  ? 1.10899 0.89782 0.59353 0.40299  0.04516  0.03443  345 ILE A CA   
321  C  C    . ILE A 26  ? 1.04225 0.83266 0.53186 0.41094  0.06638  0.04950  345 ILE A C    
322  O  O    . ILE A 26  ? 1.02705 0.82586 0.52928 0.40995  0.07579  0.05712  345 ILE A O    
323  C  CB   . ILE A 26  ? 0.98392 0.79663 0.50822 0.38780  0.03891  0.03114  345 ILE A CB   
324  C  CG1  . ILE A 26  ? 0.99075 0.80184 0.51175 0.37948  0.01878  0.01549  345 ILE A CG1  
325  C  CG2  . ILE A 26  ? 1.04567 0.87890 0.60375 0.38502  0.04794  0.03970  345 ILE A CG2  
326  C  CD1  . ILE A 26  ? 1.10125 0.93342 0.66114 0.36339  0.01062  0.01316  345 ILE A CD1  
327  H  H    . ILE A 26  ? 0.88522 0.88522 0.88522 -0.00000 0.00000  -0.00000 345 ILE A H    
328  H  HA   . ILE A 26  ? 1.04139 1.04139 1.04139 0.00000  0.00000  0.00000  345 ILE A HA   
329  H  HB   . ILE A 26  ? 0.91676 0.91676 0.91676 -0.00000 0.00000  0.00000  345 ILE A HB   
330  H  HG12 . ILE A 26  ? 0.92299 0.92299 0.92299 0.00000  0.00000  0.00000  345 ILE A HG12 
331  H  HG13 . ILE A 26  ? 0.92299 0.92299 0.92299 0.00000  0.00000  0.00000  345 ILE A HG13 
332  H  HG21 . ILE A 26  ? 1.01259 1.01259 1.01259 0.00000  0.00000  -0.00000 345 ILE A HG21 
333  H  HG22 . ILE A 26  ? 1.01259 1.01259 1.01259 0.00000  0.00000  -0.00000 345 ILE A HG22 
334  H  HG23 . ILE A 26  ? 1.01259 1.01259 1.01259 0.00000  0.00000  -0.00000 345 ILE A HG23 
335  H  HD11 . ILE A 26  ? 1.07958 1.07958 1.07958 0.00000  0.00000  0.00000  345 ILE A HD11 
336  H  HD12 . ILE A 26  ? 1.07958 1.07958 1.07958 0.00000  0.00000  0.00000  345 ILE A HD12 
337  H  HD13 . ILE A 26  ? 1.07958 1.07958 1.07958 0.00000  0.00000  0.00000  345 ILE A HD13 
338  N  N    . ILE A 27  ? 1.14636 0.92586 0.62485 0.41940  0.07561  0.05449  346 ILE A N    
339  C  CA   . ILE A 27  ? 1.07138 0.85302 0.55326 0.42835  0.09644  0.06914  346 ILE A CA   
340  C  C    . ILE A 27  ? 1.17756 0.99287 0.70292 0.42406  0.10672  0.07852  346 ILE A C    
341  O  O    . ILE A 27  ? 1.16521 0.99419 0.70639 0.42495  0.11830  0.08791  346 ILE A O    
342  C  CB   . ILE A 27  ? 1.11658 0.87351 0.57135 0.43968  0.10449  0.07240  346 ILE A CB   
343  C  CG1  . ILE A 27  ? 1.44861 1.17408 0.86484 0.44401  0.09041  0.06213  346 ILE A CG1  
344  C  CG2  . ILE A 27  ? 1.45255 1.20881 0.90567 0.45010  0.12536  0.08761  346 ILE A CG2  
345  C  CD1  . ILE A 27  ? 1.24669 0.94126 0.63679 0.45284  0.09889  0.06248  346 ILE A CD1  
346  H  H    . ILE A 27  ? 1.08008 1.08008 1.08008 0.00000  -0.00000 -0.00000 346 ILE A H    
347  H  HA   . ILE A 27  ? 0.99232 0.99232 0.99232 0.00000  0.00000  0.00000  346 ILE A HA   
348  H  HB   . ILE A 27  ? 1.02583 1.02583 1.02583 0.00000  0.00000  -0.00000 346 ILE A HB   
349  H  HG12 . ILE A 27  ? 1.39627 1.39627 1.39627 0.00000  0.00000  0.00000  346 ILE A HG12 
350  H  HG13 . ILE A 27  ? 1.39627 1.39627 1.39627 0.00000  0.00000  0.00000  346 ILE A HG13 
351  H  HG21 . ILE A 27  ? 1.42807 1.42807 1.42807 0.00000  0.00000  0.00000  346 ILE A HG21 
352  H  HG22 . ILE A 27  ? 1.42807 1.42807 1.42807 0.00000  0.00000  0.00000  346 ILE A HG22 
353  H  HG23 . ILE A 27  ? 1.42807 1.42807 1.42807 0.00000  0.00000  0.00000  346 ILE A HG23 
354  H  HD11 . ILE A 27  ? 1.13115 1.13115 1.13115 -0.00000 0.00000  0.00000  346 ILE A HD11 
355  H  HD12 . ILE A 27  ? 1.13115 1.13115 1.13115 -0.00000 0.00000  0.00000  346 ILE A HD12 
356  H  HD13 . ILE A 27  ? 1.13115 1.13115 1.13115 -0.00000 0.00000  0.00000  346 ILE A HD13 
357  N  N    . ALA A 28  ? 0.95609 0.78592 0.50063 0.42080  0.10348  0.07754  347 ALA A N    
358  C  CA   . ALA A 28  ? 0.99272 0.86222 0.57932 0.41976  0.11172  0.08925  347 ALA A CA   
359  C  C    . ALA A 28  ? 0.95096 0.83696 0.56006 0.40857  0.09610  0.08139  347 ALA A C    
360  O  O    . ALA A 28  ? 0.90851 0.77192 0.49858 0.40535  0.08498  0.06947  347 ALA A O    
361  C  CB   . ALA A 28  ? 0.87024 0.74735 0.45893 0.43287  0.13036  0.10457  347 ALA A CB   
362  H  H    . ALA A 28  ? 0.89831 0.89831 0.89831 0.00000  0.00000  -0.00000 347 ALA A H    
363  H  HA   . ALA A 28  ? 0.97496 0.97496 0.97496 0.00000  0.00000  -0.00000 347 ALA A HA   
364  H  HB1  . ALA A 28  ? 0.83186 0.83186 0.83186 0.00000  -0.00000 -0.00000 347 ALA A HB1  
365  H  HB2  . ALA A 28  ? 0.83186 0.83186 0.83186 0.00000  -0.00000 -0.00000 347 ALA A HB2  
366  H  HB3  . ALA A 28  ? 0.83186 0.83186 0.83186 0.00000  -0.00000 -0.00000 347 ALA A HB3  
367  N  N    . PRO A 29  ? 0.87397 0.80005 0.52270 0.40285  0.09520  0.08845  348 PRO A N    
368  C  CA   . PRO A 29  ? 0.82559 0.78476 0.49953 0.40702  0.10933  0.10288  348 PRO A CA   
369  C  C    . PRO A 29  ? 0.80960 0.75142 0.47322 0.40047  0.10892  0.09614  348 PRO A C    
370  O  O    . PRO A 29  ? 0.83744 0.74951 0.48035 0.39467  0.09465  0.08266  348 PRO A O    
371  C  CB   . PRO A 29  ? 0.83779 0.84987 0.55560 0.39894  0.10395  0.11067  348 PRO A CB   
372  C  CG   . PRO A 29  ? 0.82070 0.81443 0.53324 0.38808  0.08202  0.09474  348 PRO A CG   
373  C  CD   . PRO A 29  ? 0.94109 0.88600 0.61318 0.39164  0.07989  0.08281  348 PRO A CD   
374  H  HA   . PRO A 29  ? 0.84521 0.84521 0.84521 0.00000  -0.00000 -0.00000 348 PRO A HA   
375  H  HB2  . PRO A 29  ? 0.89856 0.89856 0.89856 0.00000  -0.00000 0.00000  348 PRO A HB2  
376  H  HB3  . PRO A 29  ? 0.89856 0.89856 0.89856 0.00000  -0.00000 0.00000  348 PRO A HB3  
377  H  HG2  . PRO A 29  ? 0.86860 0.86860 0.86860 0.00000  0.00000  -0.00000 348 PRO A HG2  
378  H  HG3  . PRO A 29  ? 0.86860 0.86860 0.86860 0.00000  0.00000  -0.00000 348 PRO A HG3  
379  H  HD2  . PRO A 29  ? 0.97736 0.97736 0.97736 -0.00000 -0.00000 -0.00000 348 PRO A HD2  
380  H  HD3  . PRO A 29  ? 0.97736 0.97736 0.97736 -0.00000 -0.00000 -0.00000 348 PRO A HD3  
381  N  N    . LYS A 30  ? 0.81194 0.77386 0.48878 0.38985  0.12484  0.10503  349 LYS A N    
382  C  CA   . LYS A 30  ? 0.96395 0.90591 0.62949 0.37537  0.12844  0.09908  349 LYS A CA   
383  C  C    . LYS A 30  ? 0.95932 0.91465 0.64458 0.34823  0.11521  0.09056  349 LYS A C    
384  O  O    . LYS A 30  ? 0.86169 0.78609 0.52898 0.34412  0.10931  0.08149  349 LYS A O    
385  C  CB   . LYS A 30  ? 0.90645 0.86286 0.57861 0.36886  0.15247  0.10998  349 LYS A CB   
386  C  CG   . LYS A 30  ? 1.37559 1.30999 1.02231 0.39646  0.16800  0.11799  349 LYS A CG   
387  C  CD   . LYS A 30  ? 1.53152 1.41132 1.13388 0.41433  0.16444  0.10955  349 LYS A CD   
388  C  CE   . LYS A 30  ? 1.97619 1.83546 1.55408 0.42991  0.17381  0.11810  349 LYS A CE   
389  N  NZ   . LYS A 30  ? 1.45623 1.27415 0.99405 0.43346  0.16393  0.11275  349 LYS A NZ   
390  H  H    . LYS A 30  ? 0.83109 0.83109 0.83109 0.00000  -0.00000 0.00000  349 LYS A H    
391  H  HA   . LYS A 30  ? 1.00099 1.00099 1.00099 -0.00000 -0.00000 0.00000  349 LYS A HA   
392  H  HB2  . LYS A 30  ? 0.94042 0.94042 0.94042 0.00000  0.00000  0.00000  349 LYS A HB2  
393  H  HB3  . LYS A 30  ? 0.94042 0.94042 0.94042 0.00000  0.00000  0.00000  349 LYS A HB3  
394  H  HG2  . LYS A 30  ? 1.48441 1.48441 1.48441 -0.00000 -0.00000 -0.00000 349 LYS A HG2  
395  H  HG3  . LYS A 30  ? 1.48441 1.48441 1.48441 -0.00000 -0.00000 -0.00000 349 LYS A HG3  
396  H  HD2  . LYS A 30  ? 1.63194 1.63194 1.63194 0.00000  -0.00000 -0.00000 349 LYS A HD2  
397  H  HD3  . LYS A 30  ? 1.63194 1.63194 1.63194 0.00000  -0.00000 -0.00000 349 LYS A HD3  
398  H  HE2  . LYS A 30  ? 2.14755 2.14755 2.14755 0.00000  -0.00000 0.00000  349 LYS A HE2  
399  H  HE3  . LYS A 30  ? 2.14755 2.14755 2.14755 0.00000  -0.00000 0.00000  349 LYS A HE3  
400  H  HZ1  . LYS A 30  ? 1.49102 1.49102 1.49102 -0.00000 -0.00000 0.00000  349 LYS A HZ1  
401  H  HZ2  . LYS A 30  ? 1.49102 1.49102 1.49102 -0.00000 -0.00000 0.00000  349 LYS A HZ2  
402  H  HZ3  . LYS A 30  ? 1.49102 1.49102 1.49102 -0.00000 -0.00000 0.00000  349 LYS A HZ3  
403  N  N    . GLU A 31  ? 0.70946 0.71262 0.43092 0.33045  0.11136  0.09464  350 GLU A N    
404  C  CA   . GLU A 31  ? 0.69268 0.71181 0.43358 0.30310  0.09907  0.08653  350 GLU A CA   
405  C  C    . GLU A 31  ? 0.67398 0.72715 0.43942 0.30420  0.08305  0.08815  350 GLU A C    
406  O  O    . GLU A 31  ? 0.72575 0.79680 0.49750 0.32357  0.08621  0.09843  350 GLU A O    
407  C  CB   . GLU A 31  ? 0.76726 0.81617 0.52764 0.27067  0.11409  0.08938  350 GLU A CB   
408  C  CG   . GLU A 31  ? 1.28695 1.30177 1.02318 0.26919  0.13564  0.08976  350 GLU A CG   
409  C  CD   . GLU A 31  ? 1.51063 1.54465 1.25997 0.23120  0.15202  0.08826  350 GLU A CD   
410  O  OE1  . GLU A 31  ? 1.89528 1.98026 1.67544 0.20523  0.14633  0.08849  350 GLU A OE1  
411  O  OE2  . GLU A 31  ? 1.45149 1.44904 1.17800 0.22651  0.17200  0.08678  350 GLU A OE2  
412  H  H    . GLU A 31  ? 0.74245 0.74245 0.74245 0.00000  -0.00000 0.00000  350 GLU A H    
413  H  HA   . GLU A 31  ? 0.73648 0.73648 0.73648 0.00000  0.00000  0.00000  350 GLU A HA   
414  H  HB2  . GLU A 31  ? 0.84569 0.84569 0.84569 -0.00000 -0.00000 0.00000  350 GLU A HB2  
415  H  HB3  . GLU A 31  ? 0.84569 0.84569 0.84569 -0.00000 -0.00000 0.00000  350 GLU A HB3  
416  H  HG2  . GLU A 31  ? 1.44602 1.44602 1.44602 0.00000  -0.00000 -0.00000 350 GLU A HG2  
417  H  HG3  . GLU A 31  ? 1.44602 1.44602 1.44602 0.00000  -0.00000 -0.00000 350 GLU A HG3  
418  N  N    . TYR A 32  ? 0.62048 0.68035 0.39839 0.28453  0.06797  0.07898  351 TYR A N    
419  C  CA   . TYR A 32  ? 0.61039 0.70489 0.41320 0.28281  0.05364  0.08100  351 TYR A CA   
420  C  C    . TYR A 32  ? 0.65178 0.76678 0.47422 0.25010  0.04418  0.07331  351 TYR A C    
421  O  O    . TYR A 32  ? 0.57029 0.65787 0.38009 0.23350  0.04678  0.06380  351 TYR A O    
422  C  CB   . TYR A 32  ? 0.56563 0.62512 0.34867 0.30741  0.03989  0.07436  351 TYR A CB   
423  C  CG   . TYR A 32  ? 0.68480 0.71309 0.45577 0.29887  0.02220  0.05840  351 TYR A CG   
424  C  CD1  . TYR A 32  ? 0.74236 0.73039 0.48649 0.29928  0.02315  0.05021  351 TYR A CD1  
425  C  CD2  . TYR A 32  ? 0.61136 0.65254 0.39782 0.29235  0.00563  0.05339  351 TYR A CD2  
426  C  CE1  . TYR A 32  ? 0.75522 0.72018 0.48968 0.29366  0.00793  0.03835  351 TYR A CE1  
427  C  CE2  . TYR A 32  ? 0.55754 0.57250 0.33395 0.28489  -0.01007 0.03962  351 TYR A CE2  
428  C  CZ   . TYR A 32  ? 0.64188 0.62046 0.39294 0.28575  -0.00894 0.03257  351 TYR A CZ   
429  O  OH   . TYR A 32  ? 0.68373 0.64154 0.42615 0.28027  -0.02360 0.02149  351 TYR A OH   
430  H  H    . TYR A 32  ? 0.68094 0.68094 0.68094 0.00000  0.00000  -0.00000 351 TYR A H    
431  H  HA   . TYR A 32  ? 0.69265 0.69265 0.69265 -0.00000 0.00000  0.00000  351 TYR A HA   
432  H  HB2  . TYR A 32  ? 0.61686 0.61686 0.61686 -0.00000 0.00000  0.00000  351 TYR A HB2  
433  H  HB3  . TYR A 32  ? 0.61686 0.61686 0.61686 -0.00000 0.00000  0.00000  351 TYR A HB3  
434  H  HD1  . TYR A 32  ? 0.78495 0.78495 0.78495 -0.00000 -0.00000 -0.00000 351 TYR A HD1  
435  H  HD2  . TYR A 32  ? 0.66594 0.66594 0.66594 0.00000  0.00000  0.00000  351 TYR A HD2  
436  H  HE1  . TYR A 32  ? 0.78729 0.78729 0.78729 -0.00000 0.00000  0.00000  351 TYR A HE1  
437  H  HE2  . TYR A 32  ? 0.58685 0.58685 0.58685 0.00000  -0.00000 0.00000  351 TYR A HE2  
438  H  HH   . TYR A 32  ? 0.70182 0.70182 0.70182 -0.00000 0.00000  -0.00000 351 TYR A HH   
439  N  N    . GLU A 33  ? 0.54806 0.71079 0.39986 0.24226  0.03517  0.07872  352 GLU A N    
440  C  CA   . GLU A 33  ? 0.49105 0.68025 0.36301 0.21003  0.02576  0.07214  352 GLU A CA   
441  C  C    . GLU A 33  ? 0.47890 0.63408 0.34134 0.21609  0.00611  0.05974  352 GLU A C    
442  O  O    . GLU A 33  ? 0.61975 0.78766 0.49180 0.23010  -0.00500 0.06289  352 GLU A O    
443  C  CB   . GLU A 33  ? 0.53057 0.79622 0.43930 0.19837  0.02588  0.08602  352 GLU A CB   
444  C  CG   . GLU A 33  ? 0.66619 0.96469 0.59509 0.16365  0.01547  0.07930  352 GLU A CG   
445  C  CD   . GLU A 33  ? 0.72955 1.01856 0.65093 0.12671  0.02663  0.06874  352 GLU A CD   
446  O  OE1  . GLU A 33  ? 1.00561 1.31607 0.92905 0.11513  0.04438  0.07498  352 GLU A OE1  
447  O  OE2  . GLU A 33  ? 0.68210 0.93937 0.59366 0.10937  0.01985  0.05437  352 GLU A OE2  
448  H  H    . GLU A 33  ? 0.66474 0.66474 0.66474 0.00000  -0.00000 -0.00000 352 GLU A H    
449  H  HA   . GLU A 33  ? 0.60745 0.60745 0.60745 0.00000  0.00000  0.00000  352 GLU A HA   
450  H  HB2  . GLU A 33  ? 0.70769 0.70769 0.70769 -0.00000 0.00000  0.00000  352 GLU A HB2  
451  H  HB3  . GLU A 33  ? 0.70769 0.70769 0.70769 -0.00000 0.00000  0.00000  352 GLU A HB3  
452  H  HG2  . GLU A 33  ? 0.89164 0.89164 0.89164 0.00000  0.00000  0.00000  352 GLU A HG2  
453  H  HG3  . GLU A 33  ? 0.89164 0.89164 0.89164 0.00000  0.00000  0.00000  352 GLU A HG3  
454  N  N    . ALA A 34  ? 0.48661 0.59811 0.32928 0.20647  0.00377  0.04674  353 ALA A N    
455  C  CA   . ALA A 34  ? 0.53250 0.61439 0.36637 0.21029  -0.01437 0.03517  353 ALA A CA   
456  C  C    . ALA A 34  ? 0.60059 0.70838 0.45670 0.18241  -0.02429 0.03000  353 ALA A C    
457  O  O    . ALA A 34  ? 0.50832 0.60924 0.36732 0.18671  -0.04109 0.02388  353 ALA A O    
458  C  CB   . ALA A 34  ? 0.51388 0.54171 0.31661 0.21634  -0.01180 0.02668  353 ALA A CB   
459  H  H    . ALA A 34  ? 0.55933 0.55933 0.55933 0.00000  0.00000  -0.00000 353 ALA A H    
460  H  HA   . ALA A 34  ? 0.60656 0.60656 0.60656 -0.00000 -0.00000 -0.00000 353 ALA A HA   
461  H  HB1  . ALA A 34  ? 0.55013 0.55013 0.55013 0.00000  -0.00000 0.00000  353 ALA A HB1  
462  H  HB2  . ALA A 34  ? 0.55013 0.55013 0.55013 0.00000  -0.00000 0.00000  353 ALA A HB2  
463  H  HB3  . ALA A 34  ? 0.55013 0.55013 0.55013 0.00000  -0.00000 0.00000  353 ALA A HB3  
464  N  N    . TYR A 35  ? 0.52412 0.66023 0.39363 0.15198  -0.01325 0.03132  354 TYR A N    
465  C  CA   . TYR A 35  ? 0.45510 0.61399 0.34142 0.11978  -0.01995 0.02476  354 TYR A CA   
466  C  C    . TYR A 35  ? 0.50085 0.60673 0.36704 0.11468  -0.02424 0.01148  354 TYR A C    
467  O  O    . TYR A 35  ? 0.54379 0.60508 0.38744 0.13898  -0.02703 0.00866  354 TYR A O    
468  C  CB   . TYR A 35  ? 0.46923 0.67436 0.38238 0.12213  -0.03656 0.02990  354 TYR A CB   
469  C  CG   . TYR A 35  ? 0.45502 0.72224 0.39190 0.12800  -0.03159 0.04679  354 TYR A CG   
470  C  CD1  . TYR A 35  ? 0.55705 0.88261 0.51430 0.09764  -0.02255 0.05292  354 TYR A CD1  
471  C  CD2  . TYR A 35  ? 0.73599 1.00535 0.67384 0.16323  -0.03452 0.05724  354 TYR A CD2  
472  C  CE1  . TYR A 35  ? 0.54970 0.94149 0.53111 0.10463  -0.01801 0.07142  354 TYR A CE1  
473  C  CE2  . TYR A 35  ? 0.59807 0.92509 0.55772 0.17282  -0.02738 0.07605  354 TYR A CE2  
474  C  CZ   . TYR A 35  ? 0.52433 0.91661 0.50770 0.14460  -0.01997 0.08437  354 TYR A CZ   
475  O  OH   . TYR A 35  ? 0.81927 1.27729 0.82631 0.15558  -0.01270 0.10587  354 TYR A OH   
476  H  H    . TYR A 35  ? 0.63244 0.63244 0.63244 -0.00000 0.00000  -0.00000 354 TYR A H    
477  H  HA   . TYR A 35  ? 0.56546 0.56546 0.56546 0.00000  -0.00000 -0.00000 354 TYR A HA   
478  H  HB2  . TYR A 35  ? 0.61165 0.61165 0.61165 0.00000  0.00000  0.00000  354 TYR A HB2  
479  H  HB3  . TYR A 35  ? 0.61165 0.61165 0.61165 0.00000  0.00000  0.00000  354 TYR A HB3  
480  H  HD1  . TYR A 35  ? 0.78284 0.78284 0.78284 -0.00000 0.00000  0.00000  354 TYR A HD1  
481  H  HD2  . TYR A 35  ? 0.96732 0.96732 0.96732 0.00000  0.00000  0.00000  354 TYR A HD2  
482  H  HE1  . TYR A 35  ? 0.81017 0.81017 0.81017 0.00000  0.00000  0.00000  354 TYR A HE1  
483  H  HE2  . TYR A 35  ? 0.83361 0.83361 0.83361 0.00000  0.00000  0.00000  354 TYR A HE2  
484  H  HH   . TYR A 35  ? 1.17041 1.17041 1.17041 0.00000  0.00000  0.00000  354 TYR A HH   
485  N  N    . GLU A 36  ? 0.50604 0.61880 0.37864 0.08227  -0.02234 0.00434  355 GLU A N    
486  C  CA   . GLU A 36  ? 0.47484 0.54239 0.33174 0.07678  -0.02563 -0.00641 355 GLU A CA   
487  C  C    . GLU A 36  ? 0.51372 0.60940 0.38952 0.04762  -0.03500 -0.01244 355 GLU A C    
488  O  O    . GLU A 36  ? 0.57714 0.72688 0.47462 0.02560  -0.03443 -0.00874 355 GLU A O    
489  C  CB   . GLU A 36  ? 0.50453 0.52720 0.33526 0.06563  -0.00156 -0.00972 355 GLU A CB   
490  C  CG   . GLU A 36  ? 0.59091 0.63783 0.42657 0.02871  0.01884  -0.01033 355 GLU A CG   
491  C  CD   . GLU A 36  ? 0.74678 0.74041 0.55241 0.01564  0.04709  -0.01458 355 GLU A CD   
492  O  OE1  . GLU A 36  ? 1.03883 0.98016 0.82288 0.03364  0.04919  -0.01635 355 GLU A OE1  
493  O  OE2  . GLU A 36  ? 1.25436 1.25924 1.05704 -0.01247 0.06884  -0.01528 355 GLU A OE2  
494  H  H    . GLU A 36  ? 0.60265 0.60265 0.60265 0.00000  -0.00000 -0.00000 355 GLU A H    
495  H  HA   . GLU A 36  ? 0.54084 0.54084 0.54084 0.00000  0.00000  0.00000  355 GLU A HA   
496  H  HB2  . GLU A 36  ? 0.54805 0.54805 0.54805 0.00000  -0.00000 -0.00000 355 GLU A HB2  
497  H  HB3  . GLU A 36  ? 0.54805 0.54805 0.54805 0.00000  -0.00000 -0.00000 355 GLU A HB3  
498  H  HG2  . GLU A 36  ? 0.66338 0.66338 0.66338 -0.00000 0.00000  0.00000  355 GLU A HG2  
499  H  HG3  . GLU A 36  ? 0.66338 0.66338 0.66338 -0.00000 0.00000  0.00000  355 GLU A HG3  
500  N  N    . CYS A 37  ? 0.51754 0.57998 0.38493 0.04741  -0.04334 -0.02083 356 CYS A N    
501  C  CA   . CYS A 37  ? 0.53588 0.61676 0.41701 0.01969  -0.05111 -0.02773 356 CYS A CA   
502  C  C    . CYS A 37  ? 0.60241 0.64651 0.46362 -0.00903 -0.03019 -0.03602 356 CYS A C    
503  O  O    . CYS A 37  ? 0.70290 0.69230 0.54000 0.00489  -0.02096 -0.03784 356 CYS A O    
504  C  CB   . CYS A 37  ? 0.46532 0.53562 0.35168 0.03800  -0.07386 -0.03127 356 CYS A CB   
505  S  SG   . CYS A 37  ? 0.56959 0.67481 0.47388 0.06859  -0.09231 -0.02253 356 CYS A SG   
506  H  H    . CYS A 37  ? 0.59424 0.59424 0.59424 0.00000  0.00000  -0.00000 356 CYS A H    
507  H  HA   . CYS A 37  ? 0.62912 0.62912 0.62912 0.00000  0.00000  -0.00000 356 CYS A HA   
508  H  HB2  . CYS A 37  ? 0.54230 0.54230 0.54230 -0.00000 0.00000  -0.00000 356 CYS A HB2  
509  H  HB3  . CYS A 37  ? 0.54230 0.54230 0.54230 -0.00000 0.00000  -0.00000 356 CYS A HB3  
510  N  N    . LYS A 38  ? 0.53626 0.61166 0.40569 -0.04916 -0.02070 -0.04014 357 LYS A N    
511  C  CA   . LYS A 38  ? 0.68855 0.72867 0.53555 -0.08354 0.00461  -0.04946 357 LYS A CA   
512  C  C    . LYS A 38  ? 0.67402 0.74301 0.53230 -0.12221 -0.00075 -0.05838 357 LYS A C    
513  O  O    . LYS A 38  ? 0.52044 0.65590 0.40638 -0.13237 -0.01729 -0.05493 357 LYS A O    
514  C  CB   . LYS A 38  ? 0.63705 0.68454 0.47465 -0.10132 0.02955  -0.04721 357 LYS A CB   
515  C  CG   . LYS A 38  ? 1.43282 1.43471 1.24063 -0.13644 0.06240  -0.05697 357 LYS A CG   
516  C  CD   . LYS A 38  ? 1.21660 1.23053 1.01720 -0.15192 0.08549  -0.05422 357 LYS A CD   
517  C  CE   . LYS A 38  ? 1.14980 1.12926 0.93810 -0.10825 0.09064  -0.04380 357 LYS A CE   
518  N  NZ   . LYS A 38  ? 2.04511 1.94540 1.80183 -0.08780 0.10466  -0.04491 357 LYS A NZ   
519  H  H    . LYS A 38  ? 0.62270 0.62270 0.62270 -0.00000 0.00000  -0.00000 357 LYS A H    
520  H  HA   . LYS A 38  ? 0.78236 0.78236 0.78236 0.00000  -0.00000 0.00000  357 LYS A HA   
521  H  HB2  . LYS A 38  ? 0.71975 0.71975 0.71975 -0.00000 0.00000  0.00000  357 LYS A HB2  
522  H  HB3  . LYS A 38  ? 0.71975 0.71975 0.71975 -0.00000 0.00000  0.00000  357 LYS A HB3  
523  H  HG2  . LYS A 38  ? 1.64452 1.64452 1.64452 -0.00000 -0.00000 0.00000  357 LYS A HG2  
524  H  HG3  . LYS A 38  ? 1.64452 1.64452 1.64452 -0.00000 -0.00000 0.00000  357 LYS A HG3  
525  H  HD2  . LYS A 38  ? 1.38699 1.38699 1.38699 0.00000  0.00000  0.00000  357 LYS A HD2  
526  H  HD3  . LYS A 38  ? 1.38699 1.38699 1.38699 0.00000  0.00000  0.00000  357 LYS A HD3  
527  H  HE2  . LYS A 38  ? 1.28812 1.28812 1.28812 0.00000  0.00000  0.00000  357 LYS A HE2  
528  H  HE3  . LYS A 38  ? 1.28812 1.28812 1.28812 0.00000  0.00000  0.00000  357 LYS A HE3  
529  H  HZ1  . LYS A 38  ? 2.31819 2.31819 2.31819 0.00000  -0.00000 -0.00000 357 LYS A HZ1  
530  H  HZ2  . LYS A 38  ? 2.31819 2.31819 2.31819 0.00000  -0.00000 -0.00000 357 LYS A HZ2  
531  H  HZ3  . LYS A 38  ? 2.31819 2.31819 2.31819 0.00000  -0.00000 -0.00000 357 LYS A HZ3  
532  N  N    . GLY A 39  ? 0.52849 0.90256 0.43349 -0.18818 0.08257  -0.18541 358 GLY A N    
533  C  CA   . GLY A 39  ? 0.56013 0.94292 0.47971 -0.18102 0.07532  -0.18249 358 GLY A CA   
534  C  C    . GLY A 39  ? 0.62575 0.95373 0.52404 -0.17135 0.06518  -0.15594 358 GLY A C    
535  O  O    . GLY A 39  ? 0.67358 0.96056 0.54905 -0.16849 0.06240  -0.14127 358 GLY A O    
536  H  H    . GLY A 39  ? 0.74707 0.74707 0.74707 0.00000  0.00000  0.00000  358 GLY A H    
537  H  HA2  . GLY A 39  ? 0.79436 0.79436 0.79436 -0.00000 0.00000  0.00000  358 GLY A HA2  
538  H  HA3  . GLY A 39  ? 0.79436 0.79436 0.79436 -0.00000 0.00000  0.00000  358 GLY A HA3  
539  N  N    . GLY A 40  ? 0.63044 0.96057 0.53770 -0.16698 0.05954  -0.15111 359 GLY A N    
540  C  CA   . GLY A 40  ? 0.81905 1.10226 0.70974 -0.16147 0.05124  -0.12771 359 GLY A CA   
541  C  C    . GLY A 40  ? 0.61405 0.87922 0.49932 -0.13551 0.03728  -0.12437 359 GLY A C    
542  O  O    . GLY A 40  ? 0.53853 0.82730 0.43368 -0.11911 0.03114  -0.14075 359 GLY A O    
543  H  H    . GLY A 40  ? 0.85274 0.85274 0.85274 0.00000  0.00000  0.00000  359 GLY A H    
544  H  HA2  . GLY A 40  ? 1.05367 1.05367 1.05367 -0.00000 0.00000  0.00000  359 GLY A HA2  
545  H  HA3  . GLY A 40  ? 1.05367 1.05367 1.05367 -0.00000 0.00000  0.00000  359 GLY A HA3  
546  N  N    . CYS A 41  ? 0.58079 0.80225 0.44960 -0.13203 0.03073  -0.10443 360 CYS A N    
547  C  CA   . CYS A 41  ? 0.59615 0.79133 0.45513 -0.11304 0.01692  -0.09826 360 CYS A CA   
548  C  C    . CYS A 41  ? 0.54461 0.72451 0.40463 -0.11533 0.01384  -0.08481 360 CYS A C    
549  O  O    . CYS A 41  ? 0.92573 1.07866 0.77880 -0.11996 0.01371  -0.06961 360 CYS A O    
550  C  CB   . CYS A 41  ? 0.56609 0.72918 0.40779 -0.10857 0.01293  -0.08975 360 CYS A CB   
551  S  SG   . CYS A 41  ? 0.59182 0.77032 0.42956 -0.10476 0.01635  -0.10659 360 CYS A SG   
552  H  H    . CYS A 41  ? 0.73431 0.73431 0.73431 -0.00000 0.00000  0.00000  360 CYS A H    
553  H  HA   . CYS A 41  ? 0.73830 0.73830 0.73830 -0.00000 0.00000  0.00000  360 CYS A HA   
554  H  HB2  . CYS A 41  ? 0.68248 0.68248 0.68248 0.00000  0.00000  0.00000  360 CYS A HB2  
555  H  HB3  . CYS A 41  ? 0.68248 0.68248 0.68248 0.00000  0.00000  0.00000  360 CYS A HB3  
556  N  N    . PHE A 42  ? 0.47605 0.67591 0.34615 -0.11106 0.01085  -0.09243 361 PHE A N    
557  C  CA   . PHE A 42  ? 0.62584 0.81704 0.49811 -0.11522 0.00998  -0.08235 361 PHE A CA   
558  C  C    . PHE A 42  ? 0.55668 0.74920 0.42777 -0.09945 -0.00272 -0.08833 361 PHE A C    
559  O  O    . PHE A 42  ? 0.57583 0.78861 0.45131 -0.08762 -0.00944 -0.10459 361 PHE A O    
560  C  CB   . PHE A 42  ? 0.75990 0.97559 0.64488 -0.13455 0.02212  -0.08520 361 PHE A CB   
561  C  CG   . PHE A 42  ? 0.96414 1.22796 0.86691 -0.13667 0.02660  -0.10598 361 PHE A CG   
562  C  CD1  . PHE A 42  ? 0.93907 1.23004 0.84948 -0.14206 0.03391  -0.12018 361 PHE A CD1  
563  C  CD2  . PHE A 42  ? 1.09276 1.37789 1.00644 -0.13306 0.02343  -0.11321 361 PHE A CD2  
564  C  CE1  . PHE A 42  ? 0.81682 1.16135 0.75005 -0.14411 0.03885  -0.14322 361 PHE A CE1  
565  C  CE2  . PHE A 42  ? 1.16711 1.50433 1.10253 -0.13368 0.02723  -0.13574 361 PHE A CE2  
566  C  CZ   . PHE A 42  ? 1.34486 1.71503 1.29244 -0.13941 0.03551  -0.15178 361 PHE A CZ   
567  H  H    . PHE A 42  ? 0.60050 0.60050 0.60050 0.00000  0.00000  0.00000  361 PHE A H    
568  H  HA   . PHE A 42  ? 0.77765 0.77765 0.77765 0.00000  -0.00000 0.00000  361 PHE A HA   
569  H  HB2  . PHE A 42  ? 0.95340 0.95340 0.95340 0.00000  -0.00000 0.00000  361 PHE A HB2  
570  H  HB3  . PHE A 42  ? 0.95340 0.95340 0.95340 0.00000  -0.00000 0.00000  361 PHE A HB3  
571  H  HD1  . PHE A 42  ? 1.20869 1.20869 1.20869 -0.00000 0.00000  0.00000  361 PHE A HD1  
572  H  HD2  . PHE A 42  ? 1.39209 1.39209 1.39209 0.00000  0.00000  0.00000  361 PHE A HD2  
573  H  HE1  . PHE A 42  ? 1.09254 1.09254 1.09254 -0.00000 -0.00000 -0.00000 361 PHE A HE1  
574  H  HE2  . PHE A 42  ? 1.51084 1.51084 1.51084 -0.00000 -0.00000 0.00000  361 PHE A HE2  
575  H  HZ   . PHE A 42  ? 1.74219 1.74219 1.74219 0.00000  0.00000  0.00000  361 PHE A HZ   
576  N  N    . PHE A 43  ? 0.59570 0.76628 0.46074 -0.09873 -0.00714 -0.07639 362 PHE A N    
577  C  CA   . PHE A 43  ? 0.50608 0.67304 0.36574 -0.08529 -0.02080 -0.08128 362 PHE A CA   
578  C  C    . PHE A 43  ? 0.58045 0.78126 0.45669 -0.09048 -0.01704 -0.09056 362 PHE A C    
579  O  O    . PHE A 43  ? 0.60116 0.81317 0.48670 -0.10700 -0.00403 -0.08603 362 PHE A O    
580  C  CB   . PHE A 43  ? 0.60013 0.72915 0.44401 -0.08245 -0.02718 -0.06606 362 PHE A CB   
581  C  CG   . PHE A 43  ? 0.50650 0.60637 0.33547 -0.07766 -0.03160 -0.05919 362 PHE A CG   
582  C  CD1  . PHE A 43  ? 0.66917 0.75138 0.47984 -0.06317 -0.04678 -0.06568 362 PHE A CD1  
583  C  CD2  . PHE A 43  ? 0.60093 0.69076 0.43343 -0.08783 -0.02214 -0.04754 362 PHE A CD2  
584  C  CE1  . PHE A 43  ? 0.58075 0.63795 0.37743 -0.06058 -0.05016 -0.06035 362 PHE A CE1  
585  C  CE2  . PHE A 43  ? 0.65821 0.72708 0.48022 -0.08520 -0.02559 -0.04274 362 PHE A CE2  
586  C  CZ   . PHE A 43  ? 0.57987 0.63345 0.38439 -0.07270 -0.03838 -0.04883 362 PHE A CZ   
587  H  H    . PHE A 43  ? 0.73035 0.73035 0.73035 -0.00000 0.00000  0.00000  362 PHE A H    
588  H  HA   . PHE A 43  ? 0.61920 0.61920 0.61920 -0.00000 -0.00000 0.00000  362 PHE A HA   
589  H  HB2  . PHE A 43  ? 0.71057 0.71057 0.71057 0.00000  0.00000  0.00000  362 PHE A HB2  
590  H  HB3  . PHE A 43  ? 0.71057 0.71057 0.71057 0.00000  0.00000  0.00000  362 PHE A HB3  
591  H  HD1  . PHE A 43  ? 0.76141 0.76141 0.76141 0.00000  -0.00000 0.00000  362 PHE A HD1  
592  H  HD2  . PHE A 43  ? 0.69130 0.69130 0.69130 0.00000  0.00000  0.00000  362 PHE A HD2  
593  H  HE1  . PHE A 43  ? 0.63970 0.63970 0.63970 -0.00000 0.00000  0.00000  362 PHE A HE1  
594  H  HE2  . PHE A 43  ? 0.74746 0.74746 0.74746 0.00000  0.00000  0.00000  362 PHE A HE2  
595  H  HZ   . PHE A 43  ? 0.64034 0.64034 0.64034 0.00000  0.00000  0.00000  362 PHE A HZ   
596  N  N    . PRO A 44  ? 0.46916 0.68616 0.34891 -0.07657 -0.02969 -0.10458 363 PRO A N    
597  C  CA   . PRO A 44  ? 0.62543 0.82587 0.49111 -0.05613 -0.04899 -0.11154 363 PRO A CA   
598  C  C    . PRO A 44  ? 0.78850 1.01282 0.66388 -0.04925 -0.04753 -0.12729 363 PRO A C    
599  O  O    . PRO A 44  ? 0.64297 0.91088 0.54180 -0.05827 -0.03306 -0.13931 363 PRO A O    
600  C  CB   . PRO A 44  ? 0.55481 0.77226 0.42711 -0.04539 -0.06198 -0.12227 363 PRO A CB   
601  C  CG   . PRO A 44  ? 0.61898 0.88764 0.52126 -0.05871 -0.04573 -0.13279 363 PRO A CG   
602  C  CD   . PRO A 44  ? 0.56886 0.82334 0.46757 -0.08063 -0.02685 -0.11587 363 PRO A CD   
603  H  HA   . PRO A 44  ? 0.77822 0.77822 0.77822 -0.00000 0.00000  0.00000  363 PRO A HA   
604  H  HB2  . PRO A 44  ? 0.70292 0.70292 0.70292 0.00000  -0.00000 -0.00000 363 PRO A HB2  
605  H  HB3  . PRO A 44  ? 0.70292 0.70292 0.70292 0.00000  -0.00000 -0.00000 363 PRO A HB3  
606  H  HG2  . PRO A 44  ? 0.81241 0.81241 0.81241 -0.00000 0.00000  0.00000  363 PRO A HG2  
607  H  HG3  . PRO A 44  ? 0.81241 0.81241 0.81241 -0.00000 0.00000  0.00000  363 PRO A HG3  
608  H  HD2  . PRO A 44  ? 0.74517 0.74517 0.74517 0.00000  0.00000  0.00000  363 PRO A HD2  
609  H  HD3  . PRO A 44  ? 0.74517 0.74517 0.74517 0.00000  0.00000  0.00000  363 PRO A HD3  
610  N  N    . LEU A 45  ? 0.69855 0.89407 0.55429 -0.03469 -0.06184 -0.12825 364 LEU A N    
611  C  CA   . LEU A 45  ? 1.32375 1.53840 1.18684 -0.02519 -0.06157 -0.14452 364 LEU A CA   
612  C  C    . LEU A 45  ? 1.25643 1.50476 1.13650 -0.00032 -0.07649 -0.17000 364 LEU A C    
613  O  O    . LEU A 45  ? 1.01422 1.24423 0.88364 0.01333  -0.09456 -0.16878 364 LEU A O    
614  C  CB   . LEU A 45  ? 0.75194 0.91398 0.58316 -0.02343 -0.06863 -0.13187 364 LEU A CB   
615  C  CG   . LEU A 45  ? 1.05127 1.18992 0.87435 -0.04188 -0.05456 -0.11210 364 LEU A CG   
616  C  CD1  . LEU A 45  ? 0.99492 1.08430 0.78806 -0.03853 -0.06390 -0.10199 364 LEU A CD1  
617  C  CD2  . LEU A 45  ? 1.15244 1.32575 0.99590 -0.05374 -0.03573 -0.11782 364 LEU A CD2  
618  H  H    . LEU A 45  ? 0.86002 0.86002 0.86002 -0.00000 0.00000  0.00000  364 LEU A H    
619  H  HA   . LEU A 45  ? 1.62085 1.62085 1.62085 -0.00000 -0.00000 0.00000  364 LEU A HA   
620  H  HB2  . LEU A 45  ? 0.90089 0.90089 0.90089 -0.00000 -0.00000 0.00000  364 LEU A HB2  
621  H  HB3  . LEU A 45  ? 0.90089 0.90089 0.90089 -0.00000 -0.00000 0.00000  364 LEU A HB3  
622  H  HG   . LEU A 45  ? 1.24747 1.24747 1.24747 0.00000  -0.00000 0.00000  364 LEU A HG   
623  H  HD11 . LEU A 45  ? 1.14817 1.14817 1.14817 0.00000  0.00000  0.00000  364 LEU A HD11 
624  H  HD12 . LEU A 45  ? 1.14817 1.14817 1.14817 0.00000  0.00000  0.00000  364 LEU A HD12 
625  H  HD13 . LEU A 45  ? 1.14817 1.14817 1.14817 0.00000  0.00000  0.00000  364 LEU A HD13 
626  H  HD21 . LEU A 45  ? 1.39089 1.39089 1.39089 0.00000  0.00000  0.00000  364 LEU A HD21 
627  H  HD22 . LEU A 45  ? 1.39089 1.39089 1.39089 0.00000  0.00000  0.00000  364 LEU A HD22 
628  H  HD23 . LEU A 45  ? 1.39089 1.39089 1.39089 0.00000  0.00000  0.00000  364 LEU A HD23 
629  N  N    . ALA A 46  ? 1.25575 1.55169 1.16162 0.00668  -0.06976 -0.19318 365 ALA A N    
630  C  CA   . ALA A 46  ? 1.68964 2.02639 1.61953 0.03580  -0.08430 -0.22296 365 ALA A CA   
631  C  C    . ALA A 46  ? 0.71313 1.00139 0.61525 0.06247  -0.10858 -0.22292 365 ALA A C    
632  O  O    . ALA A 46  ? 1.24142 1.48807 1.11707 0.05493  -0.10590 -0.20959 365 ALA A O    
633  C  CB   . ALA A 46  ? 1.07542 1.47387 1.03830 0.03288  -0.06803 -0.24728 365 ALA A CB   
634  H  H    . ALA A 46  ? 1.58888 1.58888 1.58888 0.00000  -0.00000 0.00000  365 ALA A H    
635  H  HA   . ALA A 46  ? 2.13548 2.13548 2.13548 -0.00000 0.00000  0.00000  365 ALA A HA   
636  H  HB1  . ALA A 46  ? 1.43629 1.43629 1.43629 0.00000  0.00000  0.00000  365 ALA A HB1  
637  H  HB2  . ALA A 46  ? 1.43629 1.43629 1.43629 0.00000  0.00000  0.00000  365 ALA A HB2  
638  H  HB3  . ALA A 46  ? 1.43629 1.43629 1.43629 0.00000  0.00000  0.00000  365 ALA A HB3  
639  N  N    . ASP A 47  ? 1.60138 1.89160 1.50740 0.09232  -0.13187 -0.23694 366 ASP A N    
640  C  CA   . ASP A 47  ? 1.70504 1.94023 1.57961 0.12064  -0.15820 -0.23650 366 ASP A CA   
641  C  C    . ASP A 47  ? 1.50279 1.75564 1.38920 0.14735  -0.16543 -0.26265 366 ASP A C    
642  O  O    . ASP A 47  ? 1.44163 1.64752 1.30221 0.17513  -0.18960 -0.26522 366 ASP A O    
643  C  CB   . ASP A 47  ? 1.94217 2.16430 1.81174 0.14539  -0.18294 -0.24055 366 ASP A CB   
644  C  CG   . ASP A 47  ? 2.14737 2.44263 2.06440 0.16896  -0.18804 -0.27430 366 ASP A CG   
645  O  OD1  . ASP A 47  ? 2.14299 2.50319 2.09792 0.16159  -0.16927 -0.29413 366 ASP A OD1  
646  O  OD2  . ASP A 47  ? 2.26724 2.55467 2.18247 0.19320  -0.20992 -0.28113 366 ASP A OD2  
647  H  H    . ASP A 47  ? 2.00140 2.00140 2.00140 0.00000  -0.00000 -0.00000 366 ASP A H    
648  H  HA   . ASP A 47  ? 2.09121 2.09121 2.09121 0.00000  -0.00000 0.00000  366 ASP A HA   
649  H  HB2  . ASP A 47  ? 2.36853 2.36853 2.36853 0.00000  -0.00000 -0.00000 366 ASP A HB2  
650  H  HB3  . ASP A 47  ? 2.36853 2.36853 2.36853 0.00000  -0.00000 -0.00000 366 ASP A HB3  
651  N  N    . ASP A 48  ? 1.75677 2.07187 1.67849 0.13978  -0.14590 -0.28183 367 ASP A N    
652  C  CA   . ASP A 48  ? 1.81867 2.15238 1.75162 0.16150  -0.14952 -0.30643 367 ASP A CA   
653  C  C    . ASP A 48  ? 1.87659 2.18618 1.79025 0.13679  -0.13048 -0.29221 367 ASP A C    
654  O  O    . ASP A 48  ? 1.92050 2.26405 1.85220 0.14130  -0.12142 -0.31182 367 ASP A O    
655  C  CB   . ASP A 48  ? 2.15570 2.58343 2.14490 0.17251  -0.14176 -0.34325 367 ASP A CB   
656  C  CG   . ASP A 48  ? 2.19784 2.67782 2.21246 0.13251  -0.10937 -0.33922 367 ASP A CG   
657  O  OD1  . ASP A 48  ? 2.29906 2.74894 2.29458 0.10510  -0.09989 -0.31075 367 ASP A OD1  
658  O  OD2  . ASP A 48  ? 2.56172 3.11124 2.61430 0.12776  -0.09379 -0.36458 367 ASP A OD2  
659  H  H    . ASP A 48  ? 2.20411 2.20411 2.20411 -0.00000 0.00000  -0.00000 367 ASP A H    
660  H  HA   . ASP A 48  ? 2.29032 2.29032 2.29032 -0.00000 -0.00000 0.00000  367 ASP A HA   
661  H  HB2  . ASP A 48  ? 2.75487 2.75487 2.75487 -0.00000 -0.00000 0.00000  367 ASP A HB2  
662  H  HB3  . ASP A 48  ? 2.75487 2.75487 2.75487 -0.00000 -0.00000 0.00000  367 ASP A HB3  
663  N  N    . VAL A 49  ? 1.00027 1.25335 0.87833 0.11067  -0.12437 -0.25927 368 VAL A N    
664  C  CA   . VAL A 49  ? 1.70057 1.92640 1.55815 0.08756  -0.10856 -0.24417 368 VAL A CA   
665  C  C    . VAL A 49  ? 1.09407 1.24313 0.90604 0.07957  -0.11923 -0.21669 368 VAL A C    
666  O  O    . VAL A 49  ? 1.24458 1.36637 1.04215 0.08101  -0.13121 -0.20388 368 VAL A O    
667  C  CB   . VAL A 49  ? 1.60168 1.86074 1.47556 0.05315  -0.08023 -0.23422 368 VAL A CB   
668  C  CG1  . VAL A 49  ? 1.08564 1.32882 0.95256 0.03456  -0.07749 -0.21125 368 VAL A CG1  
669  C  CG2  . VAL A 49  ? 1.62750 1.86036 1.48155 0.03467  -0.06664 -0.22203 368 VAL A CG2  
670  H  H    . VAL A 49  ? 1.25403 1.25403 1.25403 -0.00000 0.00000  0.00000  368 VAL A H    
671  H  HA   . VAL A 49  ? 2.07530 2.07530 2.07530 -0.00000 -0.00000 0.00000  368 VAL A HA   
672  H  HB   . VAL A 49  ? 1.97645 1.97645 1.97645 0.00000  0.00000  0.00000  368 VAL A HB   
673  H  HG11 . VAL A 49  ? 1.34806 1.34806 1.34806 0.00000  0.00000  0.00000  368 VAL A HG11 
674  H  HG12 . VAL A 49  ? 1.34806 1.34806 1.34806 0.00000  0.00000  0.00000  368 VAL A HG12 
675  H  HG13 . VAL A 49  ? 1.34806 1.34806 1.34806 0.00000  0.00000  0.00000  368 VAL A HG13 
676  H  HG21 . VAL A 49  ? 1.98902 1.98902 1.98902 -0.00000 -0.00000 0.00000  368 VAL A HG21 
677  H  HG22 . VAL A 49  ? 1.98902 1.98902 1.98902 -0.00000 -0.00000 0.00000  368 VAL A HG22 
678  H  HG23 . VAL A 49  ? 1.98902 1.98902 1.98902 -0.00000 -0.00000 0.00000  368 VAL A HG23 
679  N  N    . THR A 50  ? 1.92834 2.04355 1.71732 0.07134  -0.11535 -0.20951 369 THR A N    
680  C  CA   . THR A 50  ? 1.91025 1.95841 1.65860 0.06293  -0.12477 -0.18789 369 THR A CA   
681  C  C    . THR A 50  ? 0.79246 0.82921 0.53049 0.02751  -0.10590 -0.16561 369 THR A C    
682  O  O    . THR A 50  ? 1.25810 1.29715 0.99447 0.01866  -0.09508 -0.16744 369 THR A O    
683  C  CB   . THR A 50  ? 2.19888 2.21130 1.92660 0.08389  -0.13918 -0.19852 369 THR A CB   
684  O  OG1  . THR A 50  ? 1.70785 1.74511 1.44688 0.07831  -0.12441 -0.20965 369 THR A OG1  
685  C  CG2  . THR A 50  ? 1.59911 1.61367 1.33307 0.12436  -0.16284 -0.22042 369 THR A CG2  
686  H  H    . THR A 50  ? 2.27694 2.27694 2.27694 0.00000  0.00000  0.00000  369 THR A H    
687  H  HA   . THR A 50  ? 2.21216 2.21216 2.21216 -0.00000 0.00000  0.00000  369 THR A HA   
688  H  HB   . THR A 50  ? 2.53597 2.53597 2.53597 0.00000  0.00000  -0.00000 369 THR A HB   
689  H  HG1  . THR A 50  ? 1.96119 1.96119 1.96119 0.00000  0.00000  0.00000  369 THR A HG1  
690  H  HG21 . THR A 50  ? 1.81959 1.81959 1.81959 -0.00000 -0.00000 0.00000  369 THR A HG21 
691  H  HG22 . THR A 50  ? 1.81959 1.81959 1.81959 -0.00000 -0.00000 0.00000  369 THR A HG22 
692  H  HG23 . THR A 50  ? 1.81959 1.81959 1.81959 -0.00000 -0.00000 0.00000  369 THR A HG23 
693  N  N    . PRO A 51  ? 1.08503 1.10824 0.81536 0.00849  -0.10260 -0.14524 370 PRO A N    
694  C  CA   . PRO A 51  ? 0.76093 0.76759 0.48077 -0.01895 -0.08901 -0.12528 370 PRO A CA   
695  C  C    . PRO A 51  ? 0.88737 0.87118 0.58898 -0.03201 -0.09068 -0.11577 370 PRO A C    
696  O  O    . PRO A 51  ? 1.13102 1.08693 0.81997 -0.01559 -0.10569 -0.11627 370 PRO A O    
697  C  CB   . PRO A 51  ? 0.67746 0.68961 0.40636 -0.02531 -0.08613 -0.11313 370 PRO A CB   
698  C  CG   . PRO A 51  ? 0.90314 0.91459 0.62788 -0.01470 -0.10023 -0.11780 370 PRO A CG   
699  C  CD   . PRO A 51  ? 1.27609 1.30016 1.00902 0.01441  -0.11189 -0.14120 370 PRO A CD   
700  H  HA   . PRO A 51  ? 0.80497 0.80497 0.80497 0.00000  0.00000  -0.00000 370 PRO A HA   
701  H  HB2  . PRO A 51  ? 0.71063 0.71063 0.71063 0.00000  0.00000  0.00000  370 PRO A HB2  
702  H  HB3  . PRO A 51  ? 0.71063 0.71063 0.71063 0.00000  0.00000  0.00000  370 PRO A HB3  
703  H  HG2  . PRO A 51  ? 0.97950 0.97950 0.97950 -0.00000 -0.00000 -0.00000 370 PRO A HG2  
704  H  HG3  . PRO A 51  ? 0.97950 0.97950 0.97950 -0.00000 -0.00000 -0.00000 370 PRO A HG3  
705  H  HD2  . PRO A 51  ? 1.43536 1.43536 1.43536 0.00000  -0.00000 0.00000  370 PRO A HD2  
706  H  HD3  . PRO A 51  ? 1.43536 1.43536 1.43536 0.00000  -0.00000 0.00000  370 PRO A HD3  
707  N  N    . THR A 52  ? 0.68394 0.68518 0.41023 -0.02091 -0.08368 -0.11277 371 THR A N    
708  C  CA   . THR A 52  ? 0.51118 0.48088 0.22038 -0.03459 -0.08466 -0.09957 371 THR A CA   
709  C  C    . THR A 52  ? 0.48101 0.44039 0.19578 -0.04576 -0.07932 -0.07992 371 THR A C    
710  O  O    . THR A 52  ? 0.54895 0.52755 0.28026 -0.04622 -0.07237 -0.07616 371 THR A O    
711  C  CB   . THR A 52  ? 0.65715 0.62379 0.36835 -0.03924 -0.07835 -0.09811 371 THR A CB   
712  O  OG1  . THR A 52  ? 0.61693 0.59736 0.34471 -0.04636 -0.06636 -0.08823 371 THR A OG1  
713  C  CG2  . THR A 52  ? 0.73919 0.71921 0.44657 -0.02916 -0.08098 -0.11903 371 THR A CG2  
714  H  H    . THR A 52  ? 0.71300 0.71300 0.71300 -0.00000 0.00000  0.00000  371 THR A H    
715  H  HA   . THR A 52  ? 0.48623 0.48623 0.48623 0.00000  0.00000  0.00000  371 THR A HA   
716  H  HB   . THR A 52  ? 0.66097 0.66097 0.66097 0.00000  0.00000  -0.00000 371 THR A HB   
717  H  HG1  . THR A 52  ? 0.62486 0.62486 0.62486 0.00000  0.00000  0.00000  371 THR A HG1  
718  H  HG21 . THR A 52  ? 0.76324 0.76324 0.76324 0.00000  0.00000  0.00000  371 THR A HG21 
719  H  HG22 . THR A 52  ? 0.76324 0.76324 0.76324 0.00000  0.00000  0.00000  371 THR A HG22 
720  H  HG23 . THR A 52  ? 0.76324 0.76324 0.76324 0.00000  0.00000  0.00000  371 THR A HG23 
721  N  N    . LYS A 53  ? 0.63076 0.55388 0.32826 -0.05746 -0.08196 -0.06727 372 LYS A N    
722  C  CA   . LYS A 53  ? 0.48359 0.40077 0.18632 -0.07167 -0.07491 -0.05123 372 LYS A CA   
723  C  C    . LYS A 53  ? 0.57974 0.52001 0.30673 -0.08236 -0.06125 -0.04435 372 LYS A C    
724  O  O    . LYS A 53  ? 0.58436 0.53862 0.32664 -0.08802 -0.05363 -0.03715 372 LYS A O    
725  C  CB   . LYS A 53  ? 0.72585 0.59689 0.40073 -0.08487 -0.07997 -0.04100 372 LYS A CB   
726  C  CG   . LYS A 53  ? 0.75002 0.58202 0.39250 -0.07403 -0.09593 -0.04413 372 LYS A CG   
727  C  CD   . LYS A 53  ? 1.27584 1.05285 0.88394 -0.09054 -0.10000 -0.03138 372 LYS A CD   
728  C  CE   . LYS A 53  ? 1.26782 0.98984 0.83465 -0.07723 -0.11916 -0.03362 372 LYS A CE   
729  N  NZ   . LYS A 53  ? 0.96340 0.64672 0.50447 -0.07277 -0.12917 -0.03906 372 LYS A NZ   
730  H  H    . LYS A 53  ? 0.60641 0.60641 0.60641 0.00000  -0.00000 -0.00000 372 LYS A H    
731  H  HA   . LYS A 53  ? 0.42953 0.42953 0.42953 0.00000  0.00000  0.00000  372 LYS A HA   
732  H  HB2  . LYS A 53  ? 0.69065 0.69065 0.69065 0.00000  0.00000  0.00000  372 LYS A HB2  
733  H  HB3  . LYS A 53  ? 0.69065 0.69065 0.69065 0.00000  0.00000  0.00000  372 LYS A HB3  
734  H  HG2  . LYS A 53  ? 0.69107 0.69107 0.69107 -0.00000 -0.00000 0.00000  372 LYS A HG2  
735  H  HG3  . LYS A 53  ? 0.69107 0.69107 0.69107 -0.00000 -0.00000 0.00000  372 LYS A HG3  
736  H  HD2  . LYS A 53  ? 1.28631 1.28631 1.28631 0.00000  0.00000  -0.00000 372 LYS A HD2  
737  H  HD3  . LYS A 53  ? 1.28631 1.28631 1.28631 0.00000  0.00000  -0.00000 372 LYS A HD3  
738  H  HE2  . LYS A 53  ? 1.23818 1.23818 1.23818 0.00000  -0.00000 0.00000  372 LYS A HE2  
739  H  HE3  . LYS A 53  ? 1.23818 1.23818 1.23818 0.00000  -0.00000 0.00000  372 LYS A HE3  
740  H  HZ1  . LYS A 53  ? 0.84709 0.84709 0.84709 0.00000  -0.00000 0.00000  372 LYS A HZ1  
741  H  HZ2  . LYS A 53  ? 0.84709 0.84709 0.84709 0.00000  -0.00000 0.00000  372 LYS A HZ2  
742  H  HZ3  . LYS A 53  ? 0.84709 0.84709 0.84709 0.00000  -0.00000 0.00000  372 LYS A HZ3  
743  N  N    . HIS A 54  ? 0.52306 0.46573 0.25234 -0.08488 -0.05891 -0.04685 373 HIS A N    
744  C  CA   . HIS A 54  ? 0.50853 0.46905 0.25716 -0.09437 -0.04837 -0.04014 373 HIS A CA   
745  C  C    . HIS A 54  ? 0.39418 0.38039 0.16009 -0.08869 -0.04161 -0.04215 373 HIS A C    
746  O  O    . HIS A 54  ? 0.48227 0.47964 0.26297 -0.09671 -0.03382 -0.03439 373 HIS A O    
747  C  CB   . HIS A 54  ? 0.58348 0.54021 0.32828 -0.09729 -0.04882 -0.04292 373 HIS A CB   
748  C  CG   . HIS A 54  ? 0.44610 0.41688 0.20629 -0.10664 -0.04121 -0.03606 373 HIS A CG   
749  N  ND1  . HIS A 54  ? 0.52517 0.51436 0.29736 -0.10317 -0.03522 -0.03673 373 HIS A ND1  
750  C  CD2  . HIS A 54  ? 0.55457 0.52334 0.31816 -0.11958 -0.03951 -0.02920 373 HIS A CD2  
751  C  CE1  . HIS A 54  ? 0.47734 0.47201 0.25772 -0.11123 -0.03200 -0.03062 373 HIS A CE1  
752  N  NE2  . HIS A 54  ? 0.54433 0.53010 0.32151 -0.12023 -0.03472 -0.02698 373 HIS A NE2  
753  H  H    . HIS A 54  ? 0.49770 0.49770 0.49770 -0.00000 0.00000  -0.00000 373 HIS A H    
754  H  HA   . HIS A 54  ? 0.49515 0.49515 0.49515 -0.00000 0.00000  0.00000  373 HIS A HA   
755  H  HB2  . HIS A 54  ? 0.58204 0.58204 0.58204 0.00000  -0.00000 0.00000  373 HIS A HB2  
756  H  HB3  . HIS A 54  ? 0.58204 0.58204 0.58204 0.00000  -0.00000 0.00000  373 HIS A HB3  
757  H  HD1  . HIS A 54  ? 0.53601 0.53601 0.53601 0.00000  0.00000  -0.00000 373 HIS A HD1  
758  H  HD2  . HIS A 54  ? 0.55968 0.55968 0.55968 -0.00000 0.00000  0.00000  373 HIS A HD2  
759  H  HE1  . HIS A 54  ? 0.48408 0.48408 0.48408 0.00000  -0.00000 -0.00000 373 HIS A HE1  
760  N  N    . ALA A 55  ? 0.53590 0.53066 0.29844 -0.07622 -0.04472 -0.05368 374 ALA A N    
761  C  CA   . ALA A 55  ? 0.54439 0.56150 0.32052 -0.07583 -0.03697 -0.05569 374 ALA A CA   
762  C  C    . ALA A 55  ? 0.52677 0.54953 0.31129 -0.07759 -0.03546 -0.05041 374 ALA A C    
763  O  O    . ALA A 55  ? 0.43769 0.47524 0.23686 -0.08514 -0.02635 -0.04545 374 ALA A O    
764  C  CB   . ALA A 55  ? 0.52663 0.55265 0.29617 -0.06505 -0.04015 -0.07130 374 ALA A CB   
765  H  H    . ALA A 55  ? 0.54725 0.54725 0.54725 -0.00000 0.00000  0.00000  374 ALA A H    
766  H  HA   . ALA A 55  ? 0.57182 0.57182 0.57182 -0.00000 -0.00000 -0.00000 374 ALA A HA   
767  H  HB1  . ALA A 55  ? 0.55143 0.55143 0.55143 0.00000  0.00000  0.00000  374 ALA A HB1  
768  H  HB2  . ALA A 55  ? 0.55143 0.55143 0.55143 0.00000  0.00000  0.00000  374 ALA A HB2  
769  H  HB3  . ALA A 55  ? 0.55143 0.55143 0.55143 0.00000  0.00000  0.00000  374 ALA A HB3  
770  N  N    . ILE A 56  ? 0.53215 0.54163 0.30512 -0.07077 -0.04511 -0.05203 375 ILE A N    
771  C  CA   . ILE A 56  ? 0.62233 0.63425 0.40036 -0.07279 -0.04428 -0.04646 375 ILE A CA   
772  C  C    . ILE A 56  ? 0.43134 0.44166 0.22014 -0.08766 -0.03509 -0.03305 375 ILE A C    
773  O  O    . ILE A 56  ? 0.47843 0.50146 0.28104 -0.09278 -0.02808 -0.02892 375 ILE A O    
774  C  CB   . ILE A 56  ? 0.56211 0.55574 0.32054 -0.06350 -0.05764 -0.05002 375 ILE A CB   
775  C  CG1  . ILE A 56  ? 0.59415 0.59437 0.34383 -0.04491 -0.06999 -0.06755 375 ILE A CG1  
776  C  CG2  . ILE A 56  ? 0.61318 0.60491 0.37389 -0.06843 -0.05582 -0.04185 375 ILE A CG2  
777  C  CD1  . ILE A 56  ? 0.71700 0.70248 0.44585 -0.03634 -0.08447 -0.07390 375 ILE A CD1  
778  H  H    . ILE A 56  ? 0.55281 0.55281 0.55281 -0.00000 0.00000  0.00000  375 ILE A H    
779  H  HA   . ILE A 56  ? 0.66403 0.66403 0.66403 0.00000  0.00000  0.00000  375 ILE A HA   
780  H  HB   . ILE A 56  ? 0.57661 0.57661 0.57661 0.00000  0.00000  0.00000  375 ILE A HB   
781  H  HG12 . ILE A 56  ? 0.61419 0.61419 0.61419 0.00000  0.00000  0.00000  375 ILE A HG12 
782  H  HG13 . ILE A 56  ? 0.61419 0.61419 0.61419 0.00000  0.00000  0.00000  375 ILE A HG13 
783  H  HG21 . ILE A 56  ? 0.63805 0.63805 0.63805 0.00000  0.00000  0.00000  375 ILE A HG21 
784  H  HG22 . ILE A 56  ? 0.63805 0.63805 0.63805 0.00000  0.00000  0.00000  375 ILE A HG22 
785  H  HG23 . ILE A 56  ? 0.63805 0.63805 0.63805 0.00000  0.00000  0.00000  375 ILE A HG23 
786  H  HD11 . ILE A 56  ? 0.74739 0.74739 0.74739 0.00000  -0.00000 0.00000  375 ILE A HD11 
787  H  HD12 . ILE A 56  ? 0.74739 0.74739 0.74739 0.00000  -0.00000 0.00000  375 ILE A HD12 
788  H  HD13 . ILE A 56  ? 0.74739 0.74739 0.74739 0.00000  -0.00000 0.00000  375 ILE A HD13 
789  N  N    . VAL A 57  ? 0.47374 0.46887 0.25579 -0.09545 -0.03568 -0.02777 376 VAL A N    
790  C  CA   . VAL A 57  ? 0.58478 0.58095 0.37649 -0.10962 -0.02865 -0.01832 376 VAL A CA   
791  C  C    . VAL A 57  ? 0.51206 0.52666 0.32123 -0.11180 -0.02132 -0.01742 376 VAL A C    
792  O  O    . VAL A 57  ? 0.50131 0.52405 0.32151 -0.11697 -0.01650 -0.01333 376 VAL A O    
793  C  CB   . VAL A 57  ? 0.62058 0.59956 0.40056 -0.11999 -0.03093 -0.01509 376 VAL A CB   
794  C  CG1  . VAL A 57  ? 0.62715 0.61685 0.41977 -0.13270 -0.02445 -0.01009 376 VAL A CG1  
795  C  CG2  . VAL A 57  ? 0.65379 0.60765 0.41243 -0.12437 -0.03663 -0.01262 376 VAL A CG2  
796  H  H    . VAL A 57  ? 0.48061 0.48061 0.48061 0.00000  0.00000  0.00000  376 VAL A H    
797  H  HA   . VAL A 57  ? 0.61814 0.61814 0.61814 0.00000  0.00000  0.00000  376 VAL A HA   
798  H  HB   . VAL A 57  ? 0.64953 0.64953 0.64953 0.00000  0.00000  0.00000  376 VAL A HB   
799  H  HG11 . VAL A 57  ? 0.66676 0.66676 0.66676 0.00000  0.00000  0.00000  376 VAL A HG11 
800  H  HG12 . VAL A 57  ? 0.66676 0.66676 0.66676 0.00000  0.00000  0.00000  376 VAL A HG12 
801  H  HG13 . VAL A 57  ? 0.66676 0.66676 0.66676 0.00000  0.00000  0.00000  376 VAL A HG13 
802  H  HG21 . VAL A 57  ? 0.67080 0.67080 0.67080 0.00000  0.00000  0.00000  376 VAL A HG21 
803  H  HG22 . VAL A 57  ? 0.67080 0.67080 0.67080 0.00000  0.00000  0.00000  376 VAL A HG22 
804  H  HG23 . VAL A 57  ? 0.67080 0.67080 0.67080 0.00000  0.00000  0.00000  376 VAL A HG23 
805  N  N    . GLN A 58  ? 0.48601 0.50401 0.29420 -0.10816 -0.02140 -0.02164 377 GLN A N    
806  C  CA   . GLN A 58  ? 0.49986 0.52873 0.31806 -0.11150 -0.01577 -0.01998 377 GLN A CA   
807  C  C    . GLN A 58  ? 0.35899 0.39974 0.18587 -0.11133 -0.01086 -0.02056 377 GLN A C    
808  O  O    . GLN A 58  ? 0.46928 0.51362 0.30328 -0.11640 -0.00725 -0.01673 377 GLN A O    
809  C  CB   . GLN A 58  ? 0.49259 0.52079 0.30406 -0.10877 -0.01650 -0.02462 377 GLN A CB   
810  C  CG   . GLN A 58  ? 0.56051 0.59300 0.37542 -0.11312 -0.01252 -0.02194 377 GLN A CG   
811  C  CD   . GLN A 58  ? 0.53426 0.56208 0.33907 -0.11212 -0.01417 -0.02501 377 GLN A CD   
812  O  OE1  . GLN A 58  ? 0.54969 0.57024 0.34764 -0.11016 -0.01899 -0.02731 377 GLN A OE1  
813  N  NE2  . GLN A 58  ? 0.63485 0.66456 0.43595 -0.11466 -0.01038 -0.02528 377 GLN A NE2  
814  H  H    . GLN A 58  ? 0.51494 0.51494 0.51494 0.00000  -0.00000 -0.00000 377 GLN A H    
815  H  HA   . GLN A 58  ? 0.53992 0.53992 0.53992 0.00000  0.00000  0.00000  377 GLN A HA   
816  H  HB2  . GLN A 58  ? 0.52823 0.52823 0.52823 -0.00000 0.00000  0.00000  377 GLN A HB2  
817  H  HB3  . GLN A 58  ? 0.52823 0.52823 0.52823 -0.00000 0.00000  0.00000  377 GLN A HB3  
818  H  HG2  . GLN A 58  ? 0.61283 0.61283 0.61283 0.00000  0.00000  -0.00000 377 GLN A HG2  
819  H  HG3  . GLN A 58  ? 0.61283 0.61283 0.61283 0.00000  0.00000  -0.00000 377 GLN A HG3  
820  H  HE21 . GLN A 58  ? 0.69540 0.69540 0.69540 0.00000  0.00000  0.00000  377 GLN A HE21 
821  H  HE22 . GLN A 58  ? 0.69540 0.69540 0.69540 0.00000  0.00000  0.00000  377 GLN A HE22 
822  N  N    . THR A 59  ? 0.40002 0.44686 0.22470 -0.10551 -0.01179 -0.02665 378 THR A N    
823  C  CA   . THR A 59  ? 0.39244 0.45356 0.22571 -0.10811 -0.00674 -0.02833 378 THR A CA   
824  C  C    . THR A 59  ? 0.55148 0.61048 0.39137 -0.11194 -0.00579 -0.02202 378 THR A C    
825  O  O    . THR A 59  ? 0.45703 0.52135 0.30415 -0.11816 -0.00113 -0.01985 378 THR A O    
826  C  CB   . THR A 59  ? 0.51652 0.58853 0.34656 -0.10056 -0.00958 -0.03847 378 THR A CB   
827  O  OG1  . THR A 59  ? 0.58021 0.65516 0.40368 -0.09670 -0.01044 -0.04648 378 THR A OG1  
828  C  CG2  . THR A 59  ? 0.54574 0.63833 0.38651 -0.10671 -0.00304 -0.04193 378 THR A CG2  
829  H  H    . THR A 59  ? 0.42989 0.42989 0.42989 -0.00000 -0.00000 0.00000  378 THR A H    
830  H  HA   . THR A 59  ? 0.42994 0.42994 0.42994 -0.00000 -0.00000 0.00000  378 THR A HA   
831  H  HB   . THR A 59  ? 0.58190 0.58190 0.58190 0.00000  -0.00000 0.00000  378 THR A HB   
832  H  HG1  . THR A 59  ? 0.65687 0.65687 0.65687 0.00000  0.00000  0.00000  378 THR A HG1  
833  H  HG21 . THR A 59  ? 0.62949 0.62949 0.62949 0.00000  -0.00000 -0.00000 378 THR A HG21 
834  H  HG22 . THR A 59  ? 0.62949 0.62949 0.62949 0.00000  -0.00000 -0.00000 378 THR A HG22 
835  H  HG23 . THR A 59  ? 0.62949 0.62949 0.62949 0.00000  -0.00000 -0.00000 378 THR A HG23 
836  N  N    . LEU A 60  ? 0.51002 0.55872 0.34465 -0.10938 -0.01052 -0.01948 379 LEU A N    
837  C  CA   . LEU A 60  ? 0.47657 0.52317 0.31585 -0.11436 -0.00896 -0.01422 379 LEU A CA   
838  C  C    . LEU A 60  ? 0.54185 0.58898 0.38843 -0.12154 -0.00554 -0.00999 379 LEU A C    
839  O  O    . LEU A 60  ? 0.50102 0.55258 0.35394 -0.12531 -0.00274 -0.00862 379 LEU A O    
840  C  CB   . LEU A 60  ? 0.55879 0.59132 0.38619 -0.11334 -0.01427 -0.01239 379 LEU A CB   
841  C  CG   . LEU A 60  ? 0.58146 0.60960 0.39694 -0.10339 -0.02141 -0.01721 379 LEU A CG   
842  C  CD1  . LEU A 60  ? 0.95470 0.96039 0.75070 -0.10337 -0.02858 -0.01493 379 LEU A CD1  
843  C  CD2  . LEU A 60  ? 0.62537 0.66289 0.44677 -0.10306 -0.01965 -0.01761 379 LEU A CD2  
844  H  H    . LEU A 60  ? 0.56661 0.56661 0.56661 0.00000  -0.00000 -0.00000 379 LEU A H    
845  H  HA   . LEU A 60  ? 0.52749 0.52749 0.52749 -0.00000 0.00000  0.00000  379 LEU A HA   
846  H  HB2  . LEU A 60  ? 0.61578 0.61578 0.61578 0.00000  -0.00000 -0.00000 379 LEU A HB2  
847  H  HB3  . LEU A 60  ? 0.61578 0.61578 0.61578 0.00000  -0.00000 -0.00000 379 LEU A HB3  
848  H  HG   . LEU A 60  ? 0.63645 0.63645 0.63645 0.00000  0.00000  0.00000  379 LEU A HG   
849  H  HD11 . LEU A 60  ? 1.06757 1.06757 1.06757 0.00000  -0.00000 0.00000  379 LEU A HD11 
850  H  HD12 . LEU A 60  ? 1.06757 1.06757 1.06757 0.00000  -0.00000 0.00000  379 LEU A HD12 
851  H  HD13 . LEU A 60  ? 1.06757 1.06757 1.06757 0.00000  -0.00000 0.00000  379 LEU A HD13 
852  H  HD21 . LEU A 60  ? 0.69527 0.69527 0.69527 0.00000  0.00000  -0.00000 379 LEU A HD21 
853  H  HD22 . LEU A 60  ? 0.69527 0.69527 0.69527 0.00000  0.00000  -0.00000 379 LEU A HD22 
854  H  HD23 . LEU A 60  ? 0.69527 0.69527 0.69527 0.00000  0.00000  -0.00000 379 LEU A HD23 
855  N  N    . VAL A 61  ? 0.51403 0.55680 0.35754 -0.12304 -0.00697 -0.00911 380 VAL A N    
856  C  CA   . VAL A 61  ? 0.55588 0.60105 0.40340 -0.12728 -0.00593 -0.00695 380 VAL A CA   
857  C  C    . VAL A 61  ? 0.54710 0.59433 0.39568 -0.12617 -0.00400 -0.00759 380 VAL A C    
858  O  O    . VAL A 61  ? 0.50247 0.54962 0.35180 -0.12704 -0.00367 -0.00636 380 VAL A O    
859  C  CB   . VAL A 61  ? 0.54719 0.58895 0.38940 -0.12909 -0.00885 -0.00686 380 VAL A CB   
860  C  CG1  . VAL A 61  ? 0.61163 0.65838 0.45534 -0.13050 -0.00963 -0.00625 380 VAL A CG1  
861  C  CG2  . VAL A 61  ? 0.65782 0.69424 0.49483 -0.13513 -0.01026 -0.00586 380 VAL A CG2  
862  H  H    . VAL A 61  ? 0.57260 0.57260 0.57260 0.00000  0.00000  -0.00000 380 VAL A H    
863  H  HA   . VAL A 61  ? 0.62539 0.62539 0.62539 0.00000  0.00000  -0.00000 380 VAL A HA   
864  H  HB   . VAL A 61  ? 0.61147 0.61147 0.61147 0.00000  -0.00000 0.00000  380 VAL A HB   
865  H  HG11 . VAL A 61  ? 0.69140 0.69140 0.69140 0.00000  -0.00000 0.00000  380 VAL A HG11 
866  H  HG12 . VAL A 61  ? 0.69140 0.69140 0.69140 0.00000  -0.00000 0.00000  380 VAL A HG12 
867  H  HG13 . VAL A 61  ? 0.69140 0.69140 0.69140 0.00000  -0.00000 0.00000  380 VAL A HG13 
868  H  HG21 . VAL A 61  ? 0.74001 0.74001 0.74001 -0.00000 -0.00000 0.00000  380 VAL A HG21 
869  H  HG22 . VAL A 61  ? 0.74001 0.74001 0.74001 -0.00000 -0.00000 0.00000  380 VAL A HG22 
870  H  HG23 . VAL A 61  ? 0.74001 0.74001 0.74001 -0.00000 -0.00000 0.00000  380 VAL A HG23 
871  N  N    . HIS A 62  ? 0.44636 0.49434 0.29158 -0.12515 -0.00274 -0.01020 381 HIS A N    
872  C  CA   . HIS A 62  ? 0.50683 0.55382 0.34835 -0.12873 0.00001  -0.01082 381 HIS A CA   
873  C  C    . HIS A 62  ? 0.59224 0.64214 0.43841 -0.13232 0.00256  -0.01061 381 HIS A C    
874  O  O    . HIS A 62  ? 0.54268 0.58498 0.38292 -0.13490 0.00292  -0.00924 381 HIS A O    
875  C  CB   . HIS A 62  ? 0.54558 0.59673 0.38281 -0.12992 0.00276  -0.01527 381 HIS A CB   
876  C  CG   . HIS A 62  ? 0.64559 0.69700 0.47859 -0.13788 0.00733  -0.01688 381 HIS A CG   
877  N  ND1  . HIS A 62  ? 0.60055 0.63787 0.41981 -0.14208 0.00722  -0.01466 381 HIS A ND1  
878  C  CD2  . HIS A 62  ? 0.58235 0.64463 0.42016 -0.14335 0.01177  -0.02087 381 HIS A CD2  
879  C  CE1  . HIS A 62  ? 0.64316 0.67967 0.45731 -0.15160 0.01196  -0.01690 381 HIS A CE1  
880  N  NE2  . HIS A 62  ? 0.64082 0.69491 0.46815 -0.15325 0.01508  -0.02117 381 HIS A NE2  
881  H  H    . HIS A 62  ? 0.49417 0.49417 0.49417 0.00000  0.00000  -0.00000 381 HIS A H    
882  H  HA   . HIS A 62  ? 0.56485 0.56485 0.56485 0.00000  0.00000  0.00000  381 HIS A HA   
883  H  HB2  . HIS A 62  ? 0.61130 0.61130 0.61130 0.00000  0.00000  -0.00000 381 HIS A HB2  
884  H  HB3  . HIS A 62  ? 0.61130 0.61130 0.61130 0.00000  0.00000  -0.00000 381 HIS A HB3  
885  H  HD1  . HIS A 62  ? 0.66455 0.66455 0.66455 -0.00000 -0.00000 0.00000  381 HIS A HD1  
886  H  HD2  . HIS A 62  ? 0.66011 0.66011 0.66011 -0.00000 0.00000  -0.00000 381 HIS A HD2  
887  H  HE1  . HIS A 62  ? 0.71331 0.71331 0.71331 -0.00000 0.00000  0.00000  381 HIS A HE1  
888  N  N    . LEU A 63  ? 0.48537 0.54335 0.33834 -0.13133 0.00335  -0.01217 382 LEU A N    
889  C  CA   . LEU A 63  ? 0.59039 0.65151 0.44706 -0.13506 0.00544  -0.01249 382 LEU A CA   
890  C  C    . LEU A 63  ? 0.51728 0.57108 0.37318 -0.13509 0.00414  -0.00933 382 LEU A C    
891  O  O    . LEU A 63  ? 0.58472 0.63333 0.43654 -0.13798 0.00538  -0.00940 382 LEU A O    
892  C  CB   . LEU A 63  ? 0.72267 0.79217 0.58357 -0.13171 0.00495  -0.01449 382 LEU A CB   
893  C  CG   . LEU A 63  ? 1.05683 1.13878 0.91792 -0.12949 0.00613  -0.02065 382 LEU A CG   
894  C  CD1  . LEU A 63  ? 0.94713 1.03328 0.80659 -0.12251 0.00220  -0.02303 382 LEU A CD1  
895  C  CD2  . LEU A 63  ? 1.09009 1.18229 0.95366 -0.13959 0.01162  -0.02456 382 LEU A CD2  
896  H  H    . LEU A 63  ? 0.54807 0.54807 0.54807 0.00000  0.00000  0.00000  382 LEU A H    
897  H  HA   . LEU A 63  ? 0.67684 0.67684 0.67684 0.00000  -0.00000 -0.00000 382 LEU A HA   
898  H  HB2  . LEU A 63  ? 0.84062 0.84062 0.84062 -0.00000 0.00000  0.00000  382 LEU A HB2  
899  H  HB3  . LEU A 63  ? 0.84062 0.84062 0.84062 -0.00000 0.00000  0.00000  382 LEU A HB3  
900  H  HG   . LEU A 63  ? 1.24667 1.24667 1.24667 0.00000  0.00000  -0.00000 382 LEU A HG   
901  H  HD11 . LEU A 63  ? 1.11605 1.11605 1.11605 0.00000  0.00000  -0.00000 382 LEU A HD11 
902  H  HD12 . LEU A 63  ? 1.11605 1.11605 1.11605 0.00000  0.00000  -0.00000 382 LEU A HD12 
903  H  HD13 . LEU A 63  ? 1.11605 1.11605 1.11605 0.00000  0.00000  -0.00000 382 LEU A HD13 
904  H  HD21 . LEU A 63  ? 1.29167 1.29167 1.29167 0.00000  0.00000  -0.00000 382 LEU A HD21 
905  H  HD22 . LEU A 63  ? 1.29167 1.29167 1.29167 0.00000  0.00000  -0.00000 382 LEU A HD22 
906  H  HD23 . LEU A 63  ? 1.29167 1.29167 1.29167 0.00000  0.00000  -0.00000 382 LEU A HD23 
907  N  N    . LYS A 64  ? 0.53747 0.59064 0.39508 -0.13202 0.00183  -0.00748 383 LYS A N    
908  C  CA   . LYS A 64  ? 0.64145 0.69347 0.49894 -0.13114 0.00134  -0.00656 383 LYS A CA   
909  C  C    . LYS A 64  ? 0.64362 0.68910 0.49176 -0.12863 -0.00057 -0.00613 383 LYS A C    
910  O  O    . LYS A 64  ? 0.78169 0.82354 0.62358 -0.12734 -0.00082 -0.00664 383 LYS A O    
911  C  CB   . LYS A 64  ? 0.67484 0.73167 0.53524 -0.13335 0.00056  -0.00600 383 LYS A CB   
912  C  CG   . LYS A 64  ? 0.95712 1.02035 0.81859 -0.13684 0.00204  -0.00716 383 LYS A CG   
913  C  CD   . LYS A 64  ? 1.11671 1.17892 0.97940 -0.13752 0.00408  -0.00794 383 LYS A CD   
914  C  CE   . LYS A 64  ? 1.21501 1.28495 1.07778 -0.14245 0.00646  -0.01026 383 LYS A CE   
915  N  NZ   . LYS A 64  ? 1.33711 1.40918 1.19929 -0.15041 0.00685  -0.00989 383 LYS A NZ   
916  H  H    . LYS A 64  ? 0.61053 0.61053 0.61053 -0.00000 0.00000  0.00000  383 LYS A H    
917  H  HA   . LYS A 64  ? 0.73480 0.73480 0.73480 0.00000  0.00000  -0.00000 383 LYS A HA   
918  H  HB2  . LYS A 64  ? 0.77795 0.77795 0.77795 0.00000  0.00000  -0.00000 383 LYS A HB2  
919  H  HB3  . LYS A 64  ? 0.77795 0.77795 0.77795 0.00000  0.00000  -0.00000 383 LYS A HB3  
920  H  HG2  . LYS A 64  ? 1.11968 1.11968 1.11968 -0.00000 0.00000  -0.00000 383 LYS A HG2  
921  H  HG3  . LYS A 64  ? 1.11968 1.11968 1.11968 -0.00000 0.00000  -0.00000 383 LYS A HG3  
922  H  HD2  . LYS A 64  ? 1.31127 1.31127 1.31127 0.00000  0.00000  0.00000  383 LYS A HD2  
923  H  HD3  . LYS A 64  ? 1.31127 1.31127 1.31127 0.00000  0.00000  0.00000  383 LYS A HD3  
924  H  HE2  . LYS A 64  ? 1.43235 1.43235 1.43235 -0.00000 0.00000  0.00000  383 LYS A HE2  
925  H  HE3  . LYS A 64  ? 1.43235 1.43235 1.43235 -0.00000 0.00000  0.00000  383 LYS A HE3  
926  H  HZ1  . LYS A 64  ? 1.57949 1.57949 1.57949 -0.00000 0.00000  -0.00000 383 LYS A HZ1  
927  H  HZ2  . LYS A 64  ? 1.57949 1.57949 1.57949 -0.00000 0.00000  -0.00000 383 LYS A HZ2  
928  H  HZ3  . LYS A 64  ? 1.57949 1.57949 1.57949 -0.00000 0.00000  -0.00000 383 LYS A HZ3  
929  N  N    . PHE A 65  ? 0.57470 0.86193 0.55907 -0.07554 0.14424  -0.14985 384 PHE A N    
930  C  CA   . PHE A 65  ? 0.55910 0.84537 0.54481 -0.03808 0.14986  -0.14917 384 PHE A CA   
931  C  C    . PHE A 65  ? 0.60187 0.85678 0.57697 -0.02035 0.14688  -0.13692 384 PHE A C    
932  O  O    . PHE A 65  ? 0.64165 0.91379 0.62470 -0.00434 0.13293  -0.13072 384 PHE A O    
933  C  CB   . PHE A 65  ? 0.55263 0.89069 0.55856 -0.02747 0.13761  -0.15317 384 PHE A CB   
934  C  CG   . PHE A 65  ? 0.78544 1.15893 0.80278 -0.04870 0.13908  -0.16495 384 PHE A CG   
935  C  CD1  . PHE A 65  ? 0.70863 1.09310 0.72765 -0.03628 0.15484  -0.17511 384 PHE A CD1  
936  C  CD2  . PHE A 65  ? 0.64255 1.03580 0.66644 -0.08021 0.12607  -0.16537 384 PHE A CD2  
937  C  CE1  . PHE A 65  ? 1.16313 1.58181 1.19244 -0.05653 0.15682  -0.18622 384 PHE A CE1  
938  C  CE2  . PHE A 65  ? 0.65799 1.08216 0.69023 -0.10091 0.12856  -0.17562 384 PHE A CE2  
939  C  CZ   . PHE A 65  ? 0.61014 1.04905 0.64619 -0.08997 0.14356  -0.18641 384 PHE A CZ   
940  H  H    . PHE A 65  ? 0.79954 0.79954 0.79954 0.00000  -0.00000 -0.00000 384 PHE A H    
941  H  HA   . PHE A 65  ? 0.78097 0.78097 0.78097 0.00000  -0.00000 0.00000  384 PHE A HA   
942  H  HB2  . PHE A 65  ? 0.80200 0.80200 0.80200 0.00000  0.00000  -0.00000 384 PHE A HB2  
943  H  HB3  . PHE A 65  ? 0.80200 0.80200 0.80200 0.00000  0.00000  -0.00000 384 PHE A HB3  
944  H  HD1  . PHE A 65  ? 1.01301 1.01301 1.01301 0.00000  -0.00000 -0.00000 384 PHE A HD1  
945  H  HD2  . PHE A 65  ? 0.93917 0.93917 0.93917 -0.00000 -0.00000 -0.00000 384 PHE A HD2  
946  H  HE1  . PHE A 65  ? 1.57620 1.57620 1.57620 0.00000  -0.00000 0.00000  384 PHE A HE1  
947  H  HE2  . PHE A 65  ? 0.97341 0.97341 0.97341 0.00000  0.00000  -0.00000 384 PHE A HE2  
948  H  HZ   . PHE A 65  ? 0.92341 0.92341 0.92341 0.00000  0.00000  -0.00000 384 PHE A HZ   
949  N  N    . PRO A 66  ? 0.52271 0.73205 0.47866 -0.02360 0.16099  -0.13421 385 PRO A N    
950  C  CA   . PRO A 66  ? 0.52578 0.70658 0.47115 -0.01300 0.15775  -0.12233 385 PRO A CA   
951  C  C    . PRO A 66  ? 0.54096 0.71585 0.48345 0.02706  0.15951  -0.11597 385 PRO A C    
952  O  O    . PRO A 66  ? 0.55179 0.72052 0.49228 0.03738  0.14944  -0.10572 385 PRO A O    
953  C  CB   . PRO A 66  ? 0.55117 0.68809 0.47588 -0.02981 0.17617  -0.12431 385 PRO A CB   
954  C  CG   . PRO A 66  ? 0.64053 0.77532 0.56169 -0.03822 0.19295  -0.13752 385 PRO A CG   
955  C  CD   . PRO A 66  ? 0.71289 0.89827 0.65591 -0.04454 0.17916  -0.14291 385 PRO A CD   
956  H  HA   . PRO A 66  ? 0.67513 0.67513 0.67513 0.00000  0.00000  -0.00000 385 PRO A HA   
957  H  HB2  . PRO A 66  ? 0.67979 0.67979 0.67979 0.00000  -0.00000 0.00000  385 PRO A HB2  
958  H  HB3  . PRO A 66  ? 0.67979 0.67979 0.67979 0.00000  -0.00000 0.00000  385 PRO A HB3  
959  H  HG2  . PRO A 66  ? 0.79227 0.79227 0.79227 -0.00000 0.00000  0.00000  385 PRO A HG2  
960  H  HG3  . PRO A 66  ? 0.79227 0.79227 0.79227 -0.00000 0.00000  0.00000  385 PRO A HG3  
961  H  HD2  . PRO A 66  ? 0.90808 0.90808 0.90808 -0.00000 -0.00000 -0.00000 385 PRO A HD2  
962  H  HD3  . PRO A 66  ? 0.90808 0.90808 0.90808 -0.00000 -0.00000 -0.00000 385 PRO A HD3  
963  N  N    . THR A 67  ? 0.66463 0.84379 0.60616 0.05160  0.17180  -0.12132 386 THR A N    
964  C  CA   . THR A 67  ? 1.08460 1.25999 1.02068 0.09395  0.17463  -0.11407 386 THR A CA   
965  C  C    . THR A 67  ? 0.79019 1.02211 0.74821 0.10697  0.15268  -0.11288 386 THR A C    
966  O  O    . THR A 67  ? 0.99136 1.22599 0.94627 0.13655  0.14768  -0.10435 386 THR A O    
967  C  CB   . THR A 67  ? 0.84996 1.00944 0.77430 0.11912  0.19720  -0.11951 386 THR A CB   
968  O  OG1  . THR A 67  ? 0.98621 1.19236 0.92960 0.11049  0.19398  -0.13162 386 THR A OG1  
969  C  CG2  . THR A 67  ? 1.06540 1.16190 0.96336 0.10455  0.22151  -0.12210 386 THR A CG2  
970  H  H    . THR A 67  ? 0.84709 0.84709 0.84709 0.00000  0.00000  0.00000  386 THR A H    
971  H  HA   . THR A 67  ? 1.34736 1.34736 1.34736 0.00000  0.00000  0.00000  386 THR A HA   
972  H  HB   . THR A 67  ? 1.05474 1.05474 1.05474 0.00000  -0.00000 -0.00000 386 THR A HB   
973  H  HG21 . THR A 67  ? 1.27752 1.27752 1.27752 0.00000  0.00000  0.00000  386 THR A HG21 
974  H  HG22 . THR A 67  ? 1.27752 1.27752 1.27752 0.00000  0.00000  0.00000  386 THR A HG22 
975  H  HG23 . THR A 67  ? 1.27752 1.27752 1.27752 0.00000  0.00000  0.00000  386 THR A HG23 
976  N  N    . LYS A 68  ? 0.86583 1.14255 0.84414 0.08344  0.14022  -0.12180 387 LYS A N    
977  C  CA   . LYS A 68  ? 0.74488 1.07920 0.74366 0.09053  0.12238  -0.12495 387 LYS A CA   
978  C  C    . LYS A 68  ? 0.68787 1.03255 0.69347 0.06854  0.10191  -0.12102 387 LYS A C    
979  O  O    . LYS A 68  ? 0.70531 1.08498 0.72111 0.07932  0.08789  -0.12110 387 LYS A O    
980  C  CB   . LYS A 68  ? 0.74520 1.12351 0.76033 0.07783  0.12384  -0.13864 387 LYS A CB   
981  C  CG   . LYS A 68  ? 0.90419 1.27618 0.91294 0.10091  0.14471  -0.14396 387 LYS A CG   
982  C  CD   . LYS A 68  ? 1.69880 2.11786 1.72475 0.08538  0.14576  -0.15811 387 LYS A CD   
983  C  CE   . LYS A 68  ? 1.71581 2.12326 1.73296 0.10665  0.16860  -0.16413 387 LYS A CE   
984  N  NZ   . LYS A 68  ? 1.23972 1.68678 1.27143 0.08572  0.17164  -0.17836 387 LYS A NZ   
985  H  H    . LYS A 68  ? 1.14227 1.14227 1.14227 0.00000  -0.00000 0.00000  387 LYS A H    
986  H  HA   . LYS A 68  ? 1.02835 1.02835 1.02835 0.00000  0.00000  -0.00000 387 LYS A HA   
987  H  HB2  . LYS A 68  ? 1.05287 1.05287 1.05287 -0.00000 -0.00000 0.00000  387 LYS A HB2  
988  H  HB3  . LYS A 68  ? 1.05287 1.05287 1.05287 -0.00000 -0.00000 0.00000  387 LYS A HB3  
989  H  HG2  . LYS A 68  ? 1.23858 1.23858 1.23858 0.00000  0.00000  0.00000  387 LYS A HG2  
990  H  HG3  . LYS A 68  ? 1.23858 1.23858 1.23858 0.00000  0.00000  0.00000  387 LYS A HG3  
991  H  HD2  . LYS A 68  ? 2.21782 2.21782 2.21782 0.00000  0.00000  -0.00000 387 LYS A HD2  
992  H  HD3  . LYS A 68  ? 2.21782 2.21782 2.21782 0.00000  0.00000  -0.00000 387 LYS A HD3  
993  H  HE2  . LYS A 68  ? 2.23007 2.23007 2.23007 0.00000  0.00000  0.00000  387 LYS A HE2  
994  H  HE3  . LYS A 68  ? 2.23007 2.23007 2.23007 0.00000  0.00000  0.00000  387 LYS A HE3  
995  H  HZ1  . LYS A 68  ? 1.68042 1.68042 1.68042 0.00000  -0.00000 -0.00000 387 LYS A HZ1  
996  H  HZ2  . LYS A 68  ? 1.68042 1.68042 1.68042 0.00000  -0.00000 -0.00000 387 LYS A HZ2  
997  H  HZ3  . LYS A 68  ? 1.68042 1.68042 1.68042 0.00000  -0.00000 -0.00000 387 LYS A HZ3  
998  N  N    . VAL A 69  ? 0.64922 0.96646 0.64838 0.03837  0.10023  -0.11819 388 VAL A N    
999  C  CA   . VAL A 69  ? 0.43955 0.76305 0.44230 0.01795  0.08267  -0.11422 388 VAL A CA   
1000 C  C    . VAL A 69  ? 0.46277 0.74180 0.44983 0.01254  0.08465  -0.10343 388 VAL A C    
1001 O  O    . VAL A 69  ? 0.53924 0.79211 0.51692 -0.00151 0.09657  -0.10373 388 VAL A O    
1002 C  CB   . VAL A 69  ? 0.56848 0.91332 0.57984 -0.01637 0.07733  -0.12186 388 VAL A CB   
1003 C  CG1  . VAL A 69  ? 0.60347 0.94727 0.61350 -0.03436 0.06128  -0.11655 388 VAL A CG1  
1004 C  CG2  . VAL A 69  ? 0.70793 1.10018 0.73522 -0.01375 0.07761  -0.13409 388 VAL A CG2  
1005 H  H    . VAL A 69  ? 0.90688 0.90688 0.90688 -0.00000 0.00000  0.00000  388 VAL A H    
1006 H  HA   . VAL A 69  ? 0.65169 0.65169 0.65169 0.00000  0.00000  0.00000  388 VAL A HA   
1007 H  HB   . VAL A 69  ? 0.82591 0.82591 0.82591 0.00000  -0.00000 -0.00000 388 VAL A HB   
1008 H  HG11 . VAL A 69  ? 0.86695 0.86695 0.86695 -0.00000 -0.00000 -0.00000 388 VAL A HG11 
1009 H  HG12 . VAL A 69  ? 0.86695 0.86695 0.86695 -0.00000 -0.00000 -0.00000 388 VAL A HG12 
1010 H  HG13 . VAL A 69  ? 0.86695 0.86695 0.86695 -0.00000 -0.00000 -0.00000 388 VAL A HG13 
1011 H  HG21 . VAL A 69  ? 1.01859 1.01859 1.01859 0.00000  -0.00000 0.00000  388 VAL A HG21 
1012 H  HG22 . VAL A 69  ? 1.01859 1.01859 1.01859 0.00000  -0.00000 0.00000  388 VAL A HG22 
1013 H  HG23 . VAL A 69  ? 1.01859 1.01859 1.01859 0.00000  -0.00000 0.00000  388 VAL A HG23 
1014 N  N    . SER A 70  ? 0.43582 0.71106 0.42040 0.02304  0.07319  -0.09530 389 SER A N    
1015 C  CA   . SER A 70  ? 0.55679 0.79628 0.52779 0.01931  0.07356  -0.08475 389 SER A CA   
1016 C  C    . SER A 70  ? 0.64744 0.88686 0.61845 -0.01193 0.06555  -0.08362 389 SER A C    
1017 O  O    . SER A 70  ? 0.41009 0.67381 0.38989 -0.02731 0.05704  -0.08907 389 SER A O    
1018 C  CB   . SER A 70  ? 0.57895 0.81739 0.54715 0.04124  0.06386  -0.07691 389 SER A CB   
1019 O  OG   . SER A 70  ? 1.27838 1.54455 1.25593 0.03340  0.04677  -0.07950 389 SER A OG   
1020 H  H    . SER A 70  ? 0.62064 0.62064 0.62064 0.00000  0.00000  0.00000  389 SER A H    
1021 H  HA   . SER A 70  ? 0.75359 0.75359 0.75359 0.00000  0.00000  0.00000  389 SER A HA   
1022 H  HB2  . SER A 70  ? 0.77865 0.77865 0.77865 0.00000  -0.00000 0.00000  389 SER A HB2  
1023 H  HB3  . SER A 70  ? 0.77865 0.77865 0.77865 0.00000  -0.00000 0.00000  389 SER A HB3  
1024 H  HG   . SER A 70  ? 1.63280 1.63280 1.63280 0.00000  0.00000  0.00000  389 SER A HG   
1025 N  N    . LYS A 71  ? 0.49940 0.71281 0.45917 -0.01915 0.06860  -0.07600 390 LYS A N    
1026 C  CA   . LYS A 71  ? 0.63816 0.85260 0.59530 -0.04388 0.06102  -0.07235 390 LYS A CA   
1027 C  C    . LYS A 71  ? 0.46919 0.68691 0.42556 -0.03882 0.04494  -0.06502 390 LYS A C    
1028 O  O    . LYS A 71  ? 0.55459 0.77127 0.51144 -0.01750 0.04060  -0.06256 390 LYS A O    
1029 C  CB   . LYS A 71  ? 0.86174 1.05432 0.80748 -0.05253 0.07072  -0.06774 390 LYS A CB   
1030 C  CG   . LYS A 71  ? 1.42945 1.59748 1.36631 -0.03235 0.07938  -0.06275 390 LYS A CG   
1031 C  CD   . LYS A 71  ? 1.31703 1.46291 1.24469 -0.03536 0.10031  -0.06838 390 LYS A CD   
1032 C  CE   . LYS A 71  ? 2.16419 2.28895 2.08499 -0.00634 0.11093  -0.06704 390 LYS A CE   
1033 N  NZ   . LYS A 71  ? 0.70609 0.85392 0.63868 0.01365  0.10311  -0.07000 390 LYS A NZ   
1034 H  H    . LYS A 71  ? 0.66980 0.66980 0.66980 0.00000  -0.00000 -0.00000 390 LYS A H    
1035 H  HA   . LYS A 71  ? 0.83568 0.83568 0.83568 0.00000  0.00000  0.00000  390 LYS A HA   
1036 H  HB2  . LYS A 71  ? 1.09067 1.09067 1.09067 0.00000  -0.00000 -0.00000 390 LYS A HB2  
1037 H  HB3  . LYS A 71  ? 1.09067 1.09067 1.09067 0.00000  -0.00000 -0.00000 390 LYS A HB3  
1038 H  HG2  . LYS A 71  ? 1.75855 1.75855 1.75855 0.00000  0.00000  0.00000  390 LYS A HG2  
1039 H  HG3  . LYS A 71  ? 1.75855 1.75855 1.75855 0.00000  0.00000  0.00000  390 LYS A HG3  
1040 H  HD2  . LYS A 71  ? 1.61111 1.61111 1.61111 0.00000  -0.00000 0.00000  390 LYS A HD2  
1041 H  HD3  . LYS A 71  ? 1.61111 1.61111 1.61111 0.00000  -0.00000 0.00000  390 LYS A HD3  
1042 H  HE2  . LYS A 71  ? 2.61651 2.61651 2.61651 0.00000  -0.00000 0.00000  390 LYS A HE2  
1043 H  HE3  . LYS A 71  ? 2.61651 2.61651 2.61651 0.00000  -0.00000 0.00000  390 LYS A HE3  
1044 H  HZ1  . LYS A 71  ? 0.88073 0.88073 0.88073 0.00000  0.00000  0.00000  390 LYS A HZ1  
1045 H  HZ2  . LYS A 71  ? 0.88073 0.88073 0.88073 0.00000  0.00000  0.00000  390 LYS A HZ2  
1046 H  HZ3  . LYS A 71  ? 0.88073 0.88073 0.88073 0.00000  0.00000  0.00000  390 LYS A HZ3  
1047 N  N    . ALA A 72  ? 0.49475 0.71631 0.44825 -0.05779 0.03740  -0.06215 391 ALA A N    
1048 C  CA   . ALA A 72  ? 0.47147 0.68907 0.41975 -0.05314 0.02417  -0.05482 391 ALA A CA   
1049 C  C    . ALA A 72  ? 0.56477 0.76556 0.50548 -0.03857 0.02500  -0.04542 391 ALA A C    
1050 O  O    . ALA A 72  ? 0.46359 0.65609 0.40130 -0.04071 0.03563  -0.04420 391 ALA A O    
1051 C  CB   . ALA A 72  ? 0.41804 0.63667 0.35980 -0.07343 0.01897  -0.05142 391 ALA A CB   
1052 H  H    . ALA A 72  ? 0.66498 0.66498 0.66498 0.00000  0.00000  0.00000  391 ALA A H    
1053 H  HA   . ALA A 72  ? 0.63337 0.63337 0.63337 0.00000  0.00000  0.00000  391 ALA A HA   
1054 H  HB1  . ALA A 72  ? 0.56706 0.56706 0.56706 0.00000  -0.00000 -0.00000 391 ALA A HB1  
1055 H  HB2  . ALA A 72  ? 0.56706 0.56706 0.56706 0.00000  -0.00000 -0.00000 391 ALA A HB2  
1056 H  HB3  . ALA A 72  ? 0.56706 0.56706 0.56706 0.00000  -0.00000 -0.00000 391 ALA A HB3  
1057 N  N    . CYS A 73  ? 0.47854 0.67456 0.41513 -0.02604 0.01497  -0.04008 392 CYS A N    
1058 C  CA   A CYS A 73  ? 0.39324 0.57606 0.32328 -0.00961 0.01529  -0.03180 392 CYS A CA   
1059 C  CA   B CYS A 73  ? 0.82851 1.01131 0.75852 -0.00967 0.01529  -0.03177 392 CYS A CA   
1060 C  C    . CYS A 73  ? 0.42765 0.60507 0.34824 -0.01346 0.00756  -0.02250 392 CYS A C    
1061 O  O    . CYS A 73  ? 0.51761 0.69532 0.43424 -0.01921 -0.00112 -0.02206 392 CYS A O    
1062 C  CB   A CYS A 73  ? 0.45507 0.63883 0.38687 0.01280  0.01066  -0.03321 392 CYS A CB   
1063 C  CB   B CYS A 73  ? 0.57064 0.75399 0.50215 0.01281  0.01058  -0.03292 392 CYS A CB   
1064 S  SG   A CYS A 73  ? 0.55952 0.72690 0.48472 0.03546  0.01925  -0.02616 392 CYS A SG   
1065 S  SG   B CYS A 73  ? 0.54261 0.73256 0.48166 0.02748  0.02082  -0.04017 392 CYS A SG   
1066 H  H    A CYS A 73  ? 0.62855 0.62855 0.62855 0.00000  0.00000  0.00000  392 CYS A H    
1067 H  H    B CYS A 73  ? 0.62855 0.62855 0.62855 0.00000  0.00000  0.00000  392 CYS A H    
1068 H  HA   A CYS A 73  ? 0.51076 0.51076 0.51076 0.00000  0.00000  -0.00000 392 CYS A HA   
1069 H  HA   B CYS A 73  ? 1.04059 1.04059 1.04059 0.00000  0.00000  0.00000  392 CYS A HA   
1070 H  HB2  A CYS A 73  ? 0.59356 0.59356 0.59356 0.00000  0.00000  0.00000  392 CYS A HB2  
1071 H  HB2  B CYS A 73  ? 0.73196 0.73196 0.73196 0.00000  0.00000  0.00000  392 CYS A HB2  
1072 H  HB3  A CYS A 73  ? 0.59356 0.59356 0.59356 0.00000  0.00000  0.00000  392 CYS A HB3  
1073 H  HB3  B CYS A 73  ? 0.73196 0.73196 0.73196 0.00000  0.00000  0.00000  392 CYS A HB3  
1074 N  N    . CYS A 74  ? 0.44279 0.61492 0.35815 -0.01014 0.01204  -0.01530 393 CYS A N    
1075 C  CA   . CYS A 74  ? 0.56419 0.73575 0.47066 -0.00855 0.00566  -0.00546 393 CYS A CA   
1076 C  C    . CYS A 74  ? 0.47415 0.63591 0.37569 0.01218  -0.00185 -0.00146 393 CYS A C    
1077 O  O    . CYS A 74  ? 0.57388 0.73054 0.47557 0.02572  0.00243  -0.00018 393 CYS A O    
1078 C  CB   . CYS A 74  ? 0.53270 0.71032 0.43723 -0.01491 0.01450  -0.00144 393 CYS A CB   
1079 S  SG   . CYS A 74  ? 0.56845 0.75516 0.46371 -0.00907 0.00800  0.01090  393 CYS A SG   
1080 H  H    . CYS A 74  ? 0.56759 0.56759 0.56759 -0.00000 -0.00000 0.00000  393 CYS A H    
1081 H  HA   . CYS A 74  ? 0.70950 0.70950 0.70950 -0.00000 0.00000  0.00000  393 CYS A HA   
1082 H  HB2  . CYS A 74  ? 0.67335 0.67335 0.67335 0.00000  -0.00000 0.00000  393 CYS A HB2  
1083 H  HB3  . CYS A 74  ? 0.67335 0.67335 0.67335 0.00000  -0.00000 0.00000  393 CYS A HB3  
1084 N  N    . VAL A 75  ? 0.51095 0.66737 0.40556 0.01427  -0.01176 0.00026  394 VAL A N    
1085 C  CA   . VAL A 75  ? 0.40581 0.55225 0.29421 0.03164  -0.01902 0.00130  394 VAL A CA   
1086 C  C    . VAL A 75  ? 0.46682 0.60257 0.34063 0.03494  -0.02542 0.00942  394 VAL A C    
1087 O  O    . VAL A 75  ? 0.42006 0.55636 0.28837 0.02398  -0.02535 0.01372  394 VAL A O    
1088 C  CB   . VAL A 75  ? 0.49865 0.64685 0.39134 0.03078  -0.02338 -0.00957 394 VAL A CB   
1089 C  CG1  . VAL A 75  ? 0.50836 0.66856 0.41366 0.03584  -0.01708 -0.01603 394 VAL A CG1  
1090 C  CG2  . VAL A 75  ? 0.52301 0.67067 0.41357 0.01082  -0.02527 -0.01406 394 VAL A CG2  
1091 H  H    . VAL A 75  ? 0.63481 0.63481 0.63481 0.00000  0.00000  -0.00000 394 VAL A H    
1092 H  HA   . VAL A 75  ? 0.49799 0.49799 0.49799 0.00000  0.00000  0.00000  394 VAL A HA   
1093 H  HB   . VAL A 75  ? 0.61599 0.61599 0.61599 0.00000  0.00000  0.00000  394 VAL A HB   
1094 H  HG11 . VAL A 75  ? 0.63749 0.63749 0.63749 0.00000  0.00000  -0.00000 394 VAL A HG11 
1095 H  HG12 . VAL A 75  ? 0.63749 0.63749 0.63749 0.00000  0.00000  -0.00000 394 VAL A HG12 
1096 H  HG13 . VAL A 75  ? 0.63749 0.63749 0.63749 0.00000  0.00000  -0.00000 394 VAL A HG13 
1097 H  HG21 . VAL A 75  ? 0.64416 0.64416 0.64416 0.00000  -0.00000 -0.00000 394 VAL A HG21 
1098 H  HG22 . VAL A 75  ? 0.64416 0.64416 0.64416 0.00000  -0.00000 -0.00000 394 VAL A HG22 
1099 H  HG23 . VAL A 75  ? 0.64416 0.64416 0.64416 0.00000  -0.00000 -0.00000 394 VAL A HG23 
1100 N  N    . PRO A 76  ? 0.44155 0.56665 0.30675 0.05174  -0.03047 0.01200  395 PRO A N    
1101 C  CA   . PRO A 76  ? 0.46010 0.56906 0.30783 0.05738  -0.03559 0.01868  395 PRO A CA   
1102 C  C    . PRO A 76  ? 0.55814 0.65091 0.39665 0.04511  -0.03876 0.01223  395 PRO A C    
1103 O  O    . PRO A 76  ? 0.46457 0.55788 0.30785 0.03998  -0.04064 0.00086  395 PRO A O    
1104 C  CB   . PRO A 76  ? 0.56090 0.66270 0.40254 0.07789  -0.03881 0.02027  395 PRO A CB   
1105 C  CG   . PRO A 76  ? 0.46095 0.57816 0.31616 0.08329  -0.03379 0.01949  395 PRO A CG   
1106 C  CD   . PRO A 76  ? 0.42028 0.54683 0.28863 0.06860  -0.03007 0.01104  395 PRO A CD   
1107 H  HA   . PRO A 76  ? 0.53605 0.53605 0.53605 -0.00000 0.00000  0.00000  395 PRO A HA   
1108 H  HB2  . PRO A 76  ? 0.65171 0.65171 0.65171 -0.00000 0.00000  0.00000  395 PRO A HB2  
1109 H  HB3  . PRO A 76  ? 0.65171 0.65171 0.65171 -0.00000 0.00000  0.00000  395 PRO A HB3  
1110 H  HG2  . PRO A 76  ? 0.54336 0.54336 0.54336 0.00000  -0.00000 -0.00000 395 PRO A HG2  
1111 H  HG3  . PRO A 76  ? 0.54336 0.54336 0.54336 0.00000  -0.00000 -0.00000 395 PRO A HG3  
1112 H  HD2  . PRO A 76  ? 0.49602 0.49602 0.49602 0.00000  -0.00000 0.00000  395 PRO A HD2  
1113 H  HD3  . PRO A 76  ? 0.49602 0.49602 0.49602 0.00000  -0.00000 0.00000  395 PRO A HD3  
1114 N  N    . THR A 77  ? 0.47244 0.55236 0.29632 0.04019  -0.03854 0.01964  396 THR A N    
1115 C  CA   . THR A 77  ? 0.59782 0.65477 0.40691 0.02715  -0.03911 0.01521  396 THR A CA   
1116 C  C    . THR A 77  ? 0.66887 0.69183 0.45126 0.03937  -0.04086 0.02043  396 THR A C    
1117 O  O    . THR A 77  ? 0.67556 0.67135 0.44116 0.02841  -0.03982 0.01475  396 THR A O    
1118 C  CB   . THR A 77  ? 0.53318 0.59457 0.34051 0.01131  -0.03540 0.01997  396 THR A CB   
1119 O  OG1  . THR A 77  ? 0.54200 0.60979 0.34239 0.02303  -0.03484 0.03451  396 THR A OG1  
1120 C  CG2  . THR A 77  ? 0.49719 0.58754 0.32856 -0.00342 -0.03225 0.01175  396 THR A CG2  
1121 H  H    . THR A 77  ? 0.52217 0.52217 0.52217 0.00000  -0.00000 -0.00000 396 THR A H    
1122 H  HA   . THR A 77  ? 0.66505 0.66505 0.66505 -0.00000 -0.00000 -0.00000 396 THR A HA   
1123 H  HB   . THR A 77  ? 0.58856 0.58856 0.58856 0.00000  -0.00000 -0.00000 396 THR A HB   
1124 H  HG1  . THR A 77  ? 0.59893 0.59893 0.59893 0.00000  0.00000  -0.00000 396 THR A HG1  
1125 H  HG21 . THR A 77  ? 0.56657 0.56657 0.56657 0.00000  0.00000  -0.00000 396 THR A HG21 
1126 H  HG22 . THR A 77  ? 0.56657 0.56657 0.56657 0.00000  0.00000  -0.00000 396 THR A HG22 
1127 H  HG23 . THR A 77  ? 0.56657 0.56657 0.56657 0.00000  0.00000  -0.00000 396 THR A HG23 
1128 N  N    . LYS A 78  ? 0.57885 0.60146 0.35546 0.06106  -0.04219 0.03024  397 LYS A N    
1129 C  CA   . LYS A 78  ? 0.77229 0.76190 0.52299 0.07678  -0.04297 0.03451  397 LYS A CA   
1130 C  C    . LYS A 78  ? 0.61648 0.61873 0.37262 0.09878  -0.04539 0.03800  397 LYS A C    
1131 O  O    . LYS A 78  ? 0.53898 0.57117 0.31050 0.10485  -0.04476 0.04482  397 LYS A O    
1132 C  CB   . LYS A 78  ? 0.70702 0.67719 0.43433 0.08359  -0.03988 0.04899  397 LYS A CB   
1133 C  CG   . LYS A 78  ? 0.93733 0.86496 0.63239 0.10181  -0.03836 0.05374  397 LYS A CG   
1134 C  CD   . LYS A 78  ? 1.53375 1.44441 1.20422 0.11400  -0.03446 0.07072  397 LYS A CD   
1135 C  CE   . LYS A 78  ? 1.05991 0.91955 0.69320 0.13302  -0.03044 0.07545  397 LYS A CE   
1136 N  NZ   . LYS A 78  ? 1.76245 1.60309 1.36817 0.14782  -0.02550 0.09365  397 LYS A NZ   
1137 H  H    . LYS A 78  ? 0.61556 0.61556 0.61556 0.00000  -0.00000 -0.00000 397 LYS A H    
1138 H  HA   . LYS A 78  ? 0.82413 0.82413 0.82413 0.00000  -0.00000 -0.00000 397 LYS A HA   
1139 H  HB2  . LYS A 78  ? 0.72867 0.72867 0.72867 0.00000  0.00000  -0.00000 397 LYS A HB2  
1140 H  HB3  . LYS A 78  ? 0.72867 0.72867 0.72867 0.00000  0.00000  -0.00000 397 LYS A HB3  
1141 H  HG2  . LYS A 78  ? 0.97513 0.97513 0.97513 -0.00000 -0.00000 -0.00000 397 LYS A HG2  
1142 H  HG3  . LYS A 78  ? 0.97513 0.97513 0.97513 -0.00000 -0.00000 -0.00000 397 LYS A HG3  
1143 H  HD2  . LYS A 78  ? 1.67421 1.67421 1.67421 0.00000  0.00000  0.00000  397 LYS A HD2  
1144 H  HD3  . LYS A 78  ? 1.67421 1.67421 1.67421 0.00000  0.00000  0.00000  397 LYS A HD3  
1145 H  HE2  . LYS A 78  ? 1.07032 1.07032 1.07032 0.00000  0.00000  0.00000  397 LYS A HE2  
1146 H  HE3  . LYS A 78  ? 1.07032 1.07032 1.07032 0.00000  0.00000  0.00000  397 LYS A HE3  
1147 H  HZ1  . LYS A 78  ? 1.89474 1.89474 1.89474 -0.00000 0.00000  -0.00000 397 LYS A HZ1  
1148 H  HZ2  . LYS A 78  ? 1.89474 1.89474 1.89474 -0.00000 0.00000  -0.00000 397 LYS A HZ2  
1149 H  HZ3  . LYS A 78  ? 1.89474 1.89474 1.89474 -0.00000 0.00000  -0.00000 397 LYS A HZ3  
1150 N  N    . LEU A 79  ? 0.57041 0.54910 0.31170 0.10930  -0.04713 0.03292  398 LEU A N    
1151 C  CA   . LEU A 79  ? 0.59832 0.58709 0.34268 0.12988  -0.04920 0.03499  398 LEU A CA   
1152 C  C    . LEU A 79  ? 0.59600 0.55436 0.31239 0.15012  -0.04810 0.04201  398 LEU A C    
1153 O  O    . LEU A 79  ? 0.75491 0.67465 0.44619 0.14671  -0.04556 0.04045  398 LEU A O    
1154 C  CB   . LEU A 79  ? 0.67859 0.67417 0.43292 0.12611  -0.05255 0.02067  398 LEU A CB   
1155 C  CG   . LEU A 79  ? 0.58989 0.61399 0.36967 0.11030  -0.05287 0.01306  398 LEU A CG   
1156 C  CD1  . LEU A 79  ? 0.61489 0.64536 0.39883 0.11040  -0.05672 -0.00045 398 LEU A CD1  
1157 C  CD2  . LEU A 79  ? 0.49418 0.54689 0.29274 0.11602  -0.05001 0.02167  398 LEU A CD2  
1158 H  H    . LEU A 79  ? 0.57374 0.57374 0.57374 0.00000  0.00000  0.00000  398 LEU A H    
1159 H  HA   . LEU A 79  ? 0.61249 0.61249 0.61249 0.00000  0.00000  0.00000  398 LEU A HA   
1160 H  HB2  . LEU A 79  ? 0.71553 0.71553 0.71553 0.00000  -0.00000 -0.00000 398 LEU A HB2  
1161 H  HB3  . LEU A 79  ? 0.71553 0.71553 0.71553 0.00000  -0.00000 -0.00000 398 LEU A HB3  
1162 H  HG   . LEU A 79  ? 0.63068 0.63068 0.63068 0.00000  0.00000  -0.00000 398 LEU A HG   
1163 H  HD11 . LEU A 79  ? 0.66489 0.66489 0.66489 0.00000  0.00000  -0.00000 398 LEU A HD11 
1164 H  HD12 . LEU A 79  ? 0.66489 0.66489 0.66489 0.00000  0.00000  -0.00000 398 LEU A HD12 
1165 H  HD13 . LEU A 79  ? 0.66489 0.66489 0.66489 0.00000  0.00000  -0.00000 398 LEU A HD13 
1166 H  HD21 . LEU A 79  ? 0.52725 0.52725 0.52725 0.00000  -0.00000 -0.00000 398 LEU A HD21 
1167 H  HD22 . LEU A 79  ? 0.52725 0.52725 0.52725 0.00000  -0.00000 -0.00000 398 LEU A HD22 
1168 H  HD23 . LEU A 79  ? 0.52725 0.52725 0.52725 0.00000  -0.00000 -0.00000 398 LEU A HD23 
1169 N  N    . SER A 80  ? 0.66620 0.64030 0.38513 0.17129  -0.04859 0.04962  399 SER A N    
1170 C  CA   . SER A 80  ? 0.71725 0.66830 0.41141 0.19495  -0.04702 0.05681  399 SER A CA   
1171 C  C    . SER A 80  ? 0.69517 0.64603 0.38845 0.20756  -0.04914 0.04987  399 SER A C    
1172 O  O    . SER A 80  ? 0.60547 0.58488 0.32042 0.20388  -0.05146 0.04540  399 SER A O    
1173 C  CB   . SER A 80  ? 0.71900 0.69572 0.41525 0.21191  -0.04521 0.07345  399 SER A CB   
1174 O  OG   . SER A 80  ? 0.85416 0.82985 0.54586 0.20369  -0.04336 0.08104  399 SER A OG   
1175 H  H    . SER A 80  ? 0.67791 0.67791 0.67791 0.00000  0.00000  0.00000  399 SER A H    
1176 H  HA   . SER A 80  ? 0.72004 0.72004 0.72004 0.00000  -0.00000 0.00000  399 SER A HA   
1177 H  HB2  . SER A 80  ? 0.73324 0.73324 0.73324 0.00000  -0.00000 -0.00000 399 SER A HB2  
1178 H  HB3  . SER A 80  ? 0.73324 0.73324 0.73324 0.00000  -0.00000 -0.00000 399 SER A HB3  
1179 H  HG   . SER A 80  ? 0.89320 0.89320 0.89320 -0.00000 0.00000  0.00000  399 SER A HG   
1180 N  N    . PRO A 81  ? 0.69509 0.61240 0.36124 0.22354  -0.04740 0.04923  400 PRO A N    
1181 C  CA   . PRO A 81  ? 0.75465 0.67304 0.41796 0.23644  -0.04926 0.04260  400 PRO A CA   
1182 C  C    . PRO A 81  ? 0.77996 0.72668 0.44983 0.25995  -0.04828 0.05478  400 PRO A C    
1183 O  O    . PRO A 81  ? 0.73572 0.70169 0.41016 0.26784  -0.04612 0.06799  400 PRO A O    
1184 C  CB   . PRO A 81  ? 0.76720 0.63333 0.39510 0.24139  -0.04597 0.03562  400 PRO A CB   
1185 C  CG   . PRO A 81  ? 0.80777 0.64840 0.41640 0.24687  -0.04045 0.04819  400 PRO A CG   
1186 C  CD   . PRO A 81  ? 0.84359 0.71291 0.47658 0.22739  -0.04247 0.05209  400 PRO A CD   
1187 H  HA   . PRO A 81  ? 0.73952 0.73952 0.73952 0.00000  0.00000  0.00000  400 PRO A HA   
1188 H  HB2  . PRO A 81  ? 0.71951 0.71951 0.71951 0.00000  0.00000  0.00000  400 PRO A HB2  
1189 H  HB3  . PRO A 81  ? 0.71951 0.71951 0.71951 0.00000  0.00000  0.00000  400 PRO A HB3  
1190 H  HG2  . PRO A 81  ? 0.75028 0.75028 0.75028 0.00000  0.00000  0.00000  400 PRO A HG2  
1191 H  HG3  . PRO A 81  ? 0.75028 0.75028 0.75028 0.00000  0.00000  0.00000  400 PRO A HG3  
1192 H  HD2  . PRO A 81  ? 0.81449 0.81449 0.81449 0.00000  0.00000  0.00000  400 PRO A HD2  
1193 H  HD3  . PRO A 81  ? 0.81449 0.81449 0.81449 0.00000  0.00000  0.00000  400 PRO A HD3  
1194 N  N    . ILE A 82  ? 0.70762 0.66141 0.37836 0.27002  -0.04982 0.04942  401 ILE A N    
1195 C  CA   . ILE A 82  ? 0.70996 0.68423 0.38081 0.29327  -0.04782 0.05855  401 ILE A CA   
1196 C  C    . ILE A 82  ? 0.85325 0.80157 0.50198 0.30746  -0.04790 0.05022  401 ILE A C    
1197 O  O    . ILE A 82  ? 0.86054 0.78043 0.49672 0.29665  -0.04977 0.03652  401 ILE A O    
1198 C  CB   . ILE A 82  ? 0.70078 0.71936 0.39921 0.28946  -0.04791 0.06193  401 ILE A CB   
1199 C  CG1  . ILE A 82  ? 0.74995 0.76859 0.45362 0.28355  -0.05113 0.05029  401 ILE A CG1  
1200 C  CG2  . ILE A 82  ? 0.73951 0.78127 0.45855 0.27169  -0.04686 0.06700  401 ILE A CG2  
1201 C  CD1  . ILE A 82  ? 0.66347 0.71496 0.38652 0.28490  -0.04790 0.05424  401 ILE A CD1  
1202 H  H    . ILE A 82  ? 0.70021 0.70021 0.70021 0.00000  -0.00000 0.00000  401 ILE A H    
1203 H  HA   . ILE A 82  ? 0.71126 0.71126 0.71126 -0.00000 0.00000  -0.00000 401 ILE A HA   
1204 H  HB   . ILE A 82  ? 0.72899 0.72899 0.72899 0.00000  -0.00000 0.00000  401 ILE A HB   
1205 H  HG12 . ILE A 82  ? 0.79012 0.79012 0.79012 0.00000  -0.00000 -0.00000 401 ILE A HG12 
1206 H  HG13 . ILE A 82  ? 0.79012 0.79012 0.79012 0.00000  -0.00000 -0.00000 401 ILE A HG13 
1207 H  HG21 . ILE A 82  ? 0.79298 0.79298 0.79298 0.00000  0.00000  0.00000  401 ILE A HG21 
1208 H  HG22 . ILE A 82  ? 0.79298 0.79298 0.79298 0.00000  0.00000  0.00000  401 ILE A HG22 
1209 H  HG23 . ILE A 82  ? 0.79298 0.79298 0.79298 0.00000  0.00000  0.00000  401 ILE A HG23 
1210 H  HD11 . ILE A 82  ? 0.70723 0.70723 0.70723 0.00000  0.00000  0.00000  401 ILE A HD11 
1211 H  HD12 . ILE A 82  ? 0.70723 0.70723 0.70723 0.00000  0.00000  0.00000  401 ILE A HD12 
1212 H  HD13 . ILE A 82  ? 0.70723 0.70723 0.70723 0.00000  0.00000  0.00000  401 ILE A HD13 
1213 N  N    . SER A 83  ? 0.83111 0.79245 0.47748 0.32813  -0.04420 0.05630  402 SER A N    
1214 C  CA   . SER A 83  ? 0.78503 0.72616 0.40999 0.34418  -0.04376 0.04923  402 SER A CA   
1215 C  C    . SER A 83  ? 0.68623 0.66137 0.33365 0.34065  -0.04331 0.04501  402 SER A C    
1216 O  O    . SER A 83  ? 0.78313 0.79443 0.45776 0.33470  -0.03726 0.05096  402 SER A O    
1217 C  CB   . SER A 83  ? 0.88014 0.81025 0.49164 0.36321  -0.03452 0.05431  402 SER A CB   
1218 O  OG   . SER A 83  ? 0.89444 0.78447 0.47942 0.36862  -0.03344 0.05882  402 SER A OG   
1219 H  H    . SER A 83  ? 0.84167 0.84167 0.84167 0.00000  0.00000  -0.00000 402 SER A H    
1220 H  HA   . SER A 83  ? 0.76973 0.76973 0.76973 -0.00000 0.00000  0.00000  402 SER A HA   
1221 H  HB2  . SER A 83  ? 0.87406 0.87406 0.87406 -0.00000 -0.00000 0.00000  402 SER A HB2  
1222 H  HB3  . SER A 83  ? 0.87406 0.87406 0.87406 -0.00000 -0.00000 0.00000  402 SER A HB3  
1223 H  HG   . SER A 83  ? 0.86459 0.86459 0.86459 0.00000  0.00000  0.00000  402 SER A HG   
1224 N  N    . VAL A 84  ? 0.79151 0.75367 0.42320 0.34446  -0.04973 0.03501  403 VAL A N    
1225 C  CA   . VAL A 84  ? 0.74367 0.73340 0.39146 0.34383  -0.04864 0.03124  403 VAL A CA   
1226 C  C    . VAL A 84  ? 1.09477 1.06783 0.71698 0.36144  -0.04905 0.02375  403 VAL A C    
1227 O  O    . VAL A 84  ? 0.75823 0.69539 0.35276 0.36332  -0.05186 0.01392  403 VAL A O    
1228 C  CB   . VAL A 84  ? 0.65863 0.66158 0.31727 0.33013  -0.05659 0.02583  403 VAL A CB   
1229 C  CG1  . VAL A 84  ? 0.75830 0.77462 0.43897 0.31367  -0.05573 0.03304  403 VAL A CG1  
1230 C  CG2  . VAL A 84  ? 0.89937 0.87772 0.54293 0.31871  -0.06142 0.00843  403 VAL A CG2  
1231 H  H    . VAL A 84  ? 0.78861 0.78861 0.78861 -0.00000 0.00000  0.00000  403 VAL A H    
1232 H  HA   . VAL A 84  ? 0.74866 0.74866 0.74866 -0.00000 0.00000  0.00000  403 VAL A HA   
1233 H  HB   . VAL A 84  ? 0.65625 0.65625 0.65625 0.00000  0.00000  0.00000  403 VAL A HB   
1234 H  HG11 . VAL A 84  ? 0.79001 0.79001 0.79001 0.00000  0.00000  0.00000  403 VAL A HG11 
1235 H  HG12 . VAL A 84  ? 0.79001 0.79001 0.79001 0.00000  0.00000  0.00000  403 VAL A HG12 
1236 H  HG13 . VAL A 84  ? 0.79001 0.79001 0.79001 0.00000  0.00000  0.00000  403 VAL A HG13 
1237 H  HG21 . VAL A 84  ? 0.92926 0.92926 0.92926 -0.00000 0.00000  0.00000  403 VAL A HG21 
1238 H  HG22 . VAL A 84  ? 0.92926 0.92926 0.92926 -0.00000 0.00000  0.00000  403 VAL A HG22 
1239 H  HG23 . VAL A 84  ? 0.92926 0.92926 0.92926 -0.00000 0.00000  0.00000  403 VAL A HG23 
1240 N  N    . LEU A 85  ? 0.82420 0.82218 0.45965 0.36611  -0.04232 0.02505  404 LEU A N    
1241 C  CA   . LEU A 85  ? 0.88878 0.87801 0.50250 0.38230  -0.04269 0.01743  404 LEU A CA   
1242 C  C    . LEU A 85  ? 1.02609 1.03371 0.64771 0.37587  -0.04865 0.01095  404 LEU A C    
1243 O  O    . LEU A 85  ? 0.88529 0.92012 0.53220 0.36784  -0.04288 0.01699  404 LEU A O    
1244 C  CB   . LEU A 85  ? 0.84120 0.84701 0.46030 0.39273  -0.03104 0.02326  404 LEU A CB   
1245 C  CG   . LEU A 85  ? 1.03851 1.03928 0.63645 0.41006  -0.02994 0.01630  404 LEU A CG   
1246 C  CD1  . LEU A 85  ? 0.98557 0.94298 0.54377 0.42648  -0.03496 0.00841  404 LEU A CD1  
1247 C  CD2  . LEU A 85  ? 0.74487 0.76983 0.35132 0.41743  -0.01807 0.02334  404 LEU A CD2  
1248 H  H    . LEU A 85  ? 0.84367 0.84367 0.84367 0.00000  0.00000  0.00000  404 LEU A H    
1249 H  HA   . LEU A 85  ? 0.90897 0.90897 0.90897 0.00000  0.00000  -0.00000 404 LEU A HA   
1250 H  HB2  . LEU A 85  ? 0.86066 0.86066 0.86066 -0.00000 -0.00000 -0.00000 404 LEU A HB2  
1251 H  HB3  . LEU A 85  ? 0.86066 0.86066 0.86066 -0.00000 -0.00000 -0.00000 404 LEU A HB3  
1252 H  HG   . LEU A 85  ? 1.08695 1.08695 1.08695 0.00000  0.00000  -0.00000 404 LEU A HG   
1253 H  HD11 . LEU A 85  ? 0.99018 0.99018 0.99018 0.00000  0.00000  0.00000  404 LEU A HD11 
1254 H  HD12 . LEU A 85  ? 0.99018 0.99018 0.99018 0.00000  0.00000  0.00000  404 LEU A HD12 
1255 H  HD13 . LEU A 85  ? 0.99018 0.99018 0.99018 0.00000  0.00000  0.00000  404 LEU A HD13 
1256 H  HD21 . LEU A 85  ? 0.74766 0.74766 0.74766 -0.00000 0.00000  0.00000  404 LEU A HD21 
1257 H  HD22 . LEU A 85  ? 0.74766 0.74766 0.74766 -0.00000 0.00000  0.00000  404 LEU A HD22 
1258 H  HD23 . LEU A 85  ? 0.74766 0.74766 0.74766 -0.00000 0.00000  0.00000  404 LEU A HD23 
1259 N  N    . TYR A 86  ? 1.08402 1.07588 0.68037 0.37770  -0.06005 -0.00106 405 TYR A N    
1260 C  CA   . TYR A 86  ? 1.06855 1.08447 0.67392 0.36973  -0.06671 -0.00848 405 TYR A CA   
1261 C  C    . TYR A 86  ? 1.19409 1.21319 0.77994 0.37837  -0.07010 -0.02124 405 TYR A C    
1262 O  O    . TYR A 86  ? 1.10151 1.09540 0.66314 0.38612  -0.06749 -0.02883 405 TYR A O    
1263 C  CB   . TYR A 86  ? 1.20762 1.21621 0.81912 0.34576  -0.07179 -0.02047 405 TYR A CB   
1264 C  CG   . TYR A 86  ? 1.04979 1.02581 0.63713 0.33493  -0.07289 -0.03900 405 TYR A CG   
1265 C  CD1  . TYR A 86  ? 1.01954 0.95574 0.59276 0.33102  -0.06736 -0.03838 405 TYR A CD1  
1266 C  CD2  . TYR A 86  ? 1.04711 1.03212 0.62403 0.32731  -0.07856 -0.05754 405 TYR A CD2  
1267 C  CE1  . TYR A 86  ? 1.21679 1.11481 0.76325 0.31917  -0.06557 -0.05563 405 TYR A CE1  
1268 C  CE2  . TYR A 86  ? 1.33221 1.28553 0.88477 0.31279  -0.07775 -0.07686 405 TYR A CE2  
1269 C  CZ   . TYR A 86  ? 1.06024 0.96593 0.59632 0.30803  -0.07034 -0.07592 405 TYR A CZ   
1270 O  OH   . TYR A 86  ? 1.53626 1.40247 1.04363 0.29209  -0.06682 -0.09521 405 TYR A OH   
1271 H  H    . TYR A 86  ? 1.13736 1.13736 1.13736 0.00000  0.00000  0.00000  405 TYR A H    
1272 H  HA   . TYR A 86  ? 1.13203 1.13203 1.13203 -0.00000 0.00000  0.00000  405 TYR A HA   
1273 H  HB2  . TYR A 86  ? 1.29843 1.29843 1.29843 0.00000  0.00000  0.00000  405 TYR A HB2  
1274 H  HB3  . TYR A 86  ? 1.29843 1.29843 1.29843 0.00000  0.00000  0.00000  405 TYR A HB3  
1275 H  HD1  . TYR A 86  ? 1.02847 1.02847 1.02847 -0.00000 -0.00000 -0.00000 405 TYR A HD1  
1276 H  HD2  . TYR A 86  ? 1.08255 1.08255 1.08255 0.00000  -0.00000 0.00000  405 TYR A HD2  
1277 H  HE1  . TYR A 86  ? 1.23919 1.23919 1.23919 0.00000  0.00000  0.00000  405 TYR A HE1  
1278 H  HE2  . TYR A 86  ? 1.40226 1.40226 1.40226 -0.00000 -0.00000 0.00000  405 TYR A HE2  
1279 H  HH   . TYR A 86  ? 1.59420 1.59420 1.59420 0.00000  -0.00000 0.00000  405 TYR A HH   
1280 N  N    . LYS A 87  ? 2.47718 2.52631 2.07654 0.37517  -0.07388 -0.02430 406 LYS A N    
1281 C  CA   . LYS A 87  ? 1.18307 1.24472 0.76787 0.38271  -0.07772 -0.03616 406 LYS A CA   
1282 C  C    . LYS A 87  ? 2.08667 2.14851 1.65782 0.36591  -0.08721 -0.05786 406 LYS A C    
1283 O  O    . LYS A 87  ? 1.23438 1.32021 0.82317 0.35436  -0.09244 -0.06005 406 LYS A O    
1284 C  CB   . LYS A 87  ? 1.99062 2.08332 1.60089 0.38804  -0.07143 -0.02711 406 LYS A CB   
1285 C  CG   . LYS A 87  ? 1.73950 1.83002 1.35921 0.39657  -0.05703 -0.01312 406 LYS A CG   
1286 C  CD   . LYS A 87  ? 1.20821 1.32107 0.84363 0.39785  -0.04887 -0.00498 406 LYS A CD   
1287 C  CE   . LYS A 87  ? 1.74824 1.87999 1.37507 0.40729  -0.05440 -0.01343 406 LYS A CE   
1288 N  NZ   . LYS A 87  ? 1.51589 1.66803 1.15687 0.40554  -0.05129 -0.00788 406 LYS A NZ   
1289 H  H    . LYS A 87  ? 2.83327 2.83327 2.83327 0.00000  0.00000  0.00000  406 LYS A H    
1290 H  HA   . LYS A 87  ? 1.27952 1.27952 1.27952 0.00000  0.00000  0.00000  406 LYS A HA   
1291 H  HB2  . LYS A 87  ? 2.27119 2.27119 2.27119 0.00000  0.00000  0.00000  406 LYS A HB2  
1292 H  HB3  . LYS A 87  ? 2.27119 2.27119 2.27119 0.00000  0.00000  0.00000  406 LYS A HB3  
1293 H  HG2  . LYS A 87  ? 1.97275 1.97275 1.97275 0.00000  -0.00000 0.00000  406 LYS A HG2  
1294 H  HG3  . LYS A 87  ? 1.97275 1.97275 1.97275 0.00000  -0.00000 0.00000  406 LYS A HG3  
1295 H  HD2  . LYS A 87  ? 1.35042 1.35042 1.35042 0.00000  0.00000  0.00000  406 LYS A HD2  
1296 H  HD3  . LYS A 87  ? 1.35042 1.35042 1.35042 0.00000  0.00000  0.00000  406 LYS A HD3  
1297 H  HE2  . LYS A 87  ? 2.00258 2.00258 2.00258 -0.00000 -0.00000 0.00000  406 LYS A HE2  
1298 H  HE3  . LYS A 87  ? 2.00258 2.00258 2.00258 -0.00000 -0.00000 0.00000  406 LYS A HE3  
1299 H  HZ1  . LYS A 87  ? 1.73757 1.73757 1.73757 0.00000  0.00000  -0.00000 406 LYS A HZ1  
1300 H  HZ2  . LYS A 87  ? 1.73757 1.73757 1.73757 0.00000  0.00000  -0.00000 406 LYS A HZ2  
1301 H  HZ3  . LYS A 87  ? 1.73757 1.73757 1.73757 0.00000  0.00000  -0.00000 406 LYS A HZ3  
1302 N  N    . ASP A 88  ? 1.07897 1.11366 0.62443 0.36078  -0.08642 -0.07467 407 ASP A N    
1303 C  CA   . ASP A 88  ? 2.35992 2.39146 1.89663 0.33593  -0.09146 -0.09856 407 ASP A CA   
1304 C  C    . ASP A 88  ? 1.84605 1.92498 1.38336 0.33716  -0.10046 -0.11012 407 ASP A C    
1305 O  O    . ASP A 88  ? 1.40759 1.51146 0.95121 0.35822  -0.10074 -0.09782 407 ASP A O    
1306 C  CB   . ASP A 88  ? 1.09476 1.07506 0.59975 0.32793  -0.08500 -0.11338 407 ASP A CB   
1307 C  CG   . ASP A 88  ? 1.77531 1.74616 1.25424 0.34688  -0.08187 -0.11796 407 ASP A CG   
1308 O  OD1  . ASP A 88  ? 1.61515 1.62045 1.10162 0.36655  -0.08483 -0.10799 407 ASP A OD1  
1309 O  OD2  . ASP A 88  ? 1.62606 1.55223 1.07515 0.34196  -0.07527 -0.13134 407 ASP A OD2  
1310 H  H    . ASP A 88  ? 1.12808 1.12808 1.12808 0.00000  -0.00000 0.00000  407 ASP A H    
1311 H  HA   . ASP A 88  ? 2.66046 2.66046 2.66046 0.00000  0.00000  -0.00000 407 ASP A HA   
1312 H  HB2  . ASP A 88  ? 1.10908 1.10908 1.10908 0.00000  -0.00000 -0.00000 407 ASP A HB2  
1313 H  HB3  . ASP A 88  ? 1.10908 1.10908 1.10908 0.00000  -0.00000 -0.00000 407 ASP A HB3  
1314 N  N    . ASP A 89  ? 2.38943 2.48235 1.92365 0.31387  -0.10625 -0.13222 408 ASP A N    
1315 C  CA   . ASP A 89  ? 2.15100 2.29632 1.68881 0.31545  -0.11486 -0.14283 408 ASP A CA   
1316 C  C    . ASP A 89  ? 1.75791 1.90244 1.28252 0.33129  -0.11224 -0.14283 408 ASP A C    
1317 O  O    . ASP A 89  ? 1.64527 1.82813 1.18731 0.34560  -0.11435 -0.13340 408 ASP A O    
1318 C  CB   . ASP A 89  ? 1.45994 1.62087 0.99179 0.28477  -0.12034 -0.17088 408 ASP A CB   
1319 C  CG   . ASP A 89  ? 2.20066 2.39596 1.76030 0.27268  -0.12581 -0.16907 408 ASP A CG   
1320 O  OD1  . ASP A 89  ? 1.89659 2.10837 1.48103 0.29023  -0.12569 -0.14612 408 ASP A OD1  
1321 O  OD2  . ASP A 89  ? 2.21529 2.41958 1.77400 0.24352  -0.12827 -0.19044 408 ASP A OD2  
1322 H  H    . ASP A 89  ? 2.71943 2.71943 2.71943 0.00000  0.00000  -0.00000 408 ASP A H    
1323 H  HA   . ASP A 89  ? 2.45570 2.45570 2.45570 -0.00000 -0.00000 0.00000  408 ASP A HA   
1324 H  HB2  . ASP A 89  ? 1.63029 1.63029 1.63029 -0.00000 -0.00000 -0.00000 408 ASP A HB2  
1325 H  HB3  . ASP A 89  ? 1.63029 1.63029 1.63029 -0.00000 -0.00000 -0.00000 408 ASP A HB3  
1326 N  N    . MET A 90  ? 1.42405 1.52170 0.91662 0.33066  -0.10601 -0.15253 409 MET A N    
1327 C  CA   . MET A 90  ? 1.81672 1.90882 1.29454 0.34628  -0.10237 -0.15260 409 MET A CA   
1328 C  C    . MET A 90  ? 1.99525 2.08985 1.48745 0.37526  -0.09738 -0.12488 409 MET A C    
1329 O  O    . MET A 90  ? 1.57026 1.67365 1.05803 0.39013  -0.09524 -0.12189 409 MET A O    
1330 C  CB   . MET A 90  ? 1.70128 1.73591 1.14002 0.33805  -0.09449 -0.17029 409 MET A CB   
1331 C  CG   . MET A 90  ? 2.14892 2.17683 1.56842 0.34884  -0.09067 -0.17662 409 MET A CG   
1332 S  SD   . MET A 90  ? 2.84316 2.79407 2.21491 0.33831  -0.07817 -0.19771 409 MET A SD   
1333 C  CE   . MET A 90  ? 2.19181 2.14028 1.55338 0.29522  -0.08142 -0.22858 409 MET A CE   
1334 H  H    . MET A 90  ? 1.54620 1.54620 1.54620 -0.00000 0.00000  0.00000  409 MET A H    
1335 H  HA   . MET A 90  ? 2.00929 2.00929 2.00929 -0.00000 -0.00000 -0.00000 409 MET A HA   
1336 H  HB2  . MET A 90  ? 1.83214 1.83214 1.83214 0.00000  -0.00000 -0.00000 409 MET A HB2  
1337 H  HB3  . MET A 90  ? 1.83214 1.83214 1.83214 0.00000  -0.00000 -0.00000 409 MET A HB3  
1338 H  HG2  . MET A 90  ? 2.35892 2.35892 2.35892 -0.00000 0.00000  -0.00000 409 MET A HG2  
1339 H  HG3  . MET A 90  ? 2.35892 2.35892 2.35892 -0.00000 0.00000  -0.00000 409 MET A HG3  
1340 H  HE1  . MET A 90  ? 2.35544 2.35544 2.35544 0.00000  -0.00000 -0.00000 409 MET A HE1  
1341 H  HE2  . MET A 90  ? 2.35544 2.35544 2.35544 0.00000  -0.00000 -0.00000 409 MET A HE2  
1342 H  HE3  . MET A 90  ? 2.35544 2.35544 2.35544 0.00000  -0.00000 -0.00000 409 MET A HE3  
1343 N  N    . GLY A 91  ? 1.73312 1.82076 1.24239 0.38126  -0.09449 -0.10569 410 GLY A N    
1344 C  CA   . GLY A 91  ? 1.62667 1.72183 1.15523 0.40222  -0.08779 -0.08092 410 GLY A CA   
1345 C  C    . GLY A 91  ? 1.93397 1.99402 1.44914 0.41620  -0.07871 -0.07094 410 GLY A C    
1346 O  O    . GLY A 91  ? 1.42074 1.49070 0.95313 0.43044  -0.07098 -0.05342 410 GLY A O    
1347 H  H    . GLY A 91  ? 1.91976 1.91976 1.91976 -0.00000 0.00000  0.00000  410 GLY A H    
1348 H  HA2  . GLY A 91  ? 1.80274 1.80274 1.80274 0.00000  0.00000  0.00000  410 GLY A HA2  
1349 H  HA3  . GLY A 91  ? 1.80274 1.80274 1.80274 0.00000  0.00000  0.00000  410 GLY A HA3  
1350 N  N    . VAL A 92  ? 1.46381 1.48263 0.94903 0.41171  -0.07673 -0.08267 411 VAL A N    
1351 C  CA   . VAL A 92  ? 1.88244 1.86846 1.35189 0.42875  -0.06727 -0.07367 411 VAL A CA   
1352 C  C    . VAL A 92  ? 1.76963 1.74234 1.25434 0.42559  -0.06390 -0.05874 411 VAL A C    
1353 O  O    . VAL A 92  ? 1.24263 1.20600 0.73632 0.40447  -0.06703 -0.06449 411 VAL A O    
1354 C  CB   . VAL A 92  ? 1.29143 1.23350 0.72144 0.42748  -0.06272 -0.09392 411 VAL A CB   
1355 C  CG1  . VAL A 92  ? 1.14209 1.04558 0.55924 0.44431  -0.05182 -0.08337 411 VAL A CG1  
1356 C  CG2  . VAL A 92  ? 1.44337 1.40266 0.86712 0.43228  -0.06439 -0.10326 411 VAL A CG2  
1357 H  H    . VAL A 92  ? 1.55944 1.55944 1.55944 -0.00000 -0.00000 -0.00000 411 VAL A H    
1358 H  HA   . VAL A 92  ? 2.04237 2.04237 2.04237 0.00000  0.00000  0.00000  411 VAL A HA   
1359 H  HB   . VAL A 92  ? 1.29980 1.29980 1.29980 0.00000  0.00000  0.00000  411 VAL A HB   
1360 H  HG11 . VAL A 92  ? 1.10002 1.10002 1.10002 0.00000  0.00000  -0.00000 411 VAL A HG11 
1361 H  HG12 . VAL A 92  ? 1.10002 1.10002 1.10002 0.00000  0.00000  -0.00000 411 VAL A HG12 
1362 H  HG13 . VAL A 92  ? 1.10002 1.10002 1.10002 0.00000  0.00000  -0.00000 411 VAL A HG13 
1363 H  HG21 . VAL A 92  ? 1.48651 1.48651 1.48651 0.00000  -0.00000 -0.00000 411 VAL A HG21 
1364 H  HG22 . VAL A 92  ? 1.48651 1.48651 1.48651 0.00000  -0.00000 -0.00000 411 VAL A HG22 
1365 H  HG23 . VAL A 92  ? 1.48651 1.48651 1.48651 0.00000  -0.00000 -0.00000 411 VAL A HG23 
1366 N  N    . PRO A 93  ? 1.13538 1.11203 0.62939 0.44311  -0.05706 -0.03963 412 PRO A N    
1367 C  CA   . PRO A 93  ? 1.95140 1.92021 1.46172 0.43967  -0.05364 -0.02541 412 PRO A CA   
1368 C  C    . PRO A 93  ? 1.19518 1.11671 0.68672 0.43215  -0.05031 -0.03396 412 PRO A C    
1369 O  O    . PRO A 93  ? 1.32153 1.21112 0.78562 0.44576  -0.04385 -0.03886 412 PRO A O    
1370 C  CB   . PRO A 93  ? 1.26178 1.24700 0.79214 0.45148  -0.04011 -0.01252 412 PRO A CB   
1371 C  CG   . PRO A 93  ? 1.46854 1.48139 1.00649 0.45583  -0.03828 -0.01478 412 PRO A CG   
1372 C  CD   . PRO A 93  ? 1.69959 1.69868 1.20736 0.45904  -0.04949 -0.03102 412 PRO A CD   
1373 H  HA   . PRO A 93  ? 2.13458 2.13458 2.13458 0.00000  -0.00000 -0.00000 412 PRO A HA   
1374 H  HB2  . PRO A 93  ? 1.32162 1.32162 1.32162 0.00000  0.00000  -0.00000 412 PRO A HB2  
1375 H  HB3  . PRO A 93  ? 1.32162 1.32162 1.32162 0.00000  0.00000  -0.00000 412 PRO A HB3  
1376 H  HG2  . PRO A 93  ? 1.58382 1.58382 1.58382 0.00000  -0.00000 -0.00000 412 PRO A HG2  
1377 H  HG3  . PRO A 93  ? 1.58382 1.58382 1.58382 0.00000  -0.00000 -0.00000 412 PRO A HG3  
1378 H  HD2  . PRO A 93  ? 1.84350 1.84350 1.84350 0.00000  0.00000  0.00000  412 PRO A HD2  
1379 H  HD3  . PRO A 93  ? 1.84350 1.84350 1.84350 0.00000  0.00000  0.00000  412 PRO A HD3  
1380 N  N    . THR A 94  ? 1.12435 1.03908 0.62901 0.41083  -0.05346 -0.03547 413 THR A N    
1381 C  CA   . THR A 94  ? 1.29603 1.16373 0.78289 0.39970  -0.04948 -0.04282 413 THR A CA   
1382 C  C    . THR A 94  ? 1.21980 1.09145 0.72798 0.39464  -0.04837 -0.02681 413 THR A C    
1383 O  O    . THR A 94  ? 1.00233 0.91047 0.54049 0.38597  -0.05318 -0.01868 413 THR A O    
1384 C  CB   . THR A 94  ? 1.17532 1.02995 0.65279 0.37269  -0.05420 -0.06533 413 THR A CB   
1385 O  OG1  . THR A 94  ? 1.88189 1.74197 1.34115 0.37633  -0.05617 -0.08102 413 THR A OG1  
1386 C  CG2  . THR A 94  ? 1.66676 1.46478 1.11956 0.35947  -0.04732 -0.07385 413 THR A CG2  
1387 H  H    . THR A 94  ? 1.11823 1.11823 1.11823 0.00000  -0.00000 -0.00000 413 THR A H    
1388 H  HA   . THR A 94  ? 1.29832 1.29832 1.29832 0.00000  0.00000  -0.00000 413 THR A HA   
1389 H  HB   . THR A 94  ? 1.14448 1.14448 1.14448 0.00000  0.00000  0.00000  413 THR A HB   
1390 H  HG1  . THR A 94  ? 1.98726 1.98726 1.98726 0.00000  -0.00000 0.00000  413 THR A HG1  
1391 H  HG21 . THR A 94  ? 1.70169 1.70169 1.70169 0.00000  -0.00000 -0.00000 413 THR A HG21 
1392 H  HG22 . THR A 94  ? 1.70169 1.70169 1.70169 0.00000  -0.00000 -0.00000 413 THR A HG22 
1393 H  HG23 . THR A 94  ? 1.70169 1.70169 1.70169 0.00000  -0.00000 -0.00000 413 THR A HG23 
1394 N  N    . LEU A 95  ? 1.00577 0.83927 0.49644 0.40142  -0.04120 -0.02189 414 LEU A N    
1395 C  CA   . LEU A 95  ? 0.88922 0.72621 0.39662 0.39669  -0.04016 -0.00744 414 LEU A CA   
1396 C  C    . LEU A 95  ? 1.14451 0.95796 0.65094 0.36769  -0.04234 -0.01813 414 LEU A C    
1397 O  O    . LEU A 95  ? 0.99533 0.76354 0.47277 0.35803  -0.03859 -0.03314 414 LEU A O    
1398 C  CB   . LEU A 95  ? 1.00074 0.81305 0.48931 0.42091  -0.03142 0.00525  414 LEU A CB   
1399 C  CG   . LEU A 95  ? 0.93566 0.75478 0.43971 0.41608  -0.03081 0.02002  414 LEU A CG   
1400 C  CD1  . LEU A 95  ? 0.92239 0.80403 0.46861 0.41269  -0.03091 0.03187  414 LEU A CD1  
1401 C  CD2  . LEU A 95  ? 1.00924 0.78709 0.48373 0.43650  -0.02171 0.02847  414 LEU A CD2  
1402 H  H    . LEU A 95  ? 0.93785 0.93785 0.93785 -0.00000 -0.00000 -0.00000 414 LEU A H    
1403 H  HA   . LEU A 95  ? 0.80608 0.80608 0.80608 -0.00000 0.00000  0.00000  414 LEU A HA   
1404 H  HB2  . LEU A 95  ? 0.92249 0.92249 0.92249 0.00000  0.00000  0.00000  414 LEU A HB2  
1405 H  HB3  . LEU A 95  ? 0.92249 0.92249 0.92249 0.00000  0.00000  0.00000  414 LEU A HB3  
1406 H  HG   . LEU A 95  ? 0.85332 0.85332 0.85332 0.00000  0.00000  0.00000  414 LEU A HG   
1407 H  HD11 . LEU A 95  ? 0.87926 0.87926 0.87926 0.00000  -0.00000 0.00000  414 LEU A HD11 
1408 H  HD12 . LEU A 95  ? 0.87926 0.87926 0.87926 0.00000  -0.00000 0.00000  414 LEU A HD12 
1409 H  HD13 . LEU A 95  ? 0.87926 0.87926 0.87926 0.00000  -0.00000 0.00000  414 LEU A HD13 
1410 H  HD21 . LEU A 95  ? 0.91328 0.91328 0.91328 0.00000  0.00000  0.00000  414 LEU A HD21 
1411 H  HD22 . LEU A 95  ? 0.91328 0.91328 0.91328 0.00000  0.00000  0.00000  414 LEU A HD22 
1412 H  HD23 . LEU A 95  ? 0.91328 0.91328 0.91328 0.00000  0.00000  0.00000  414 LEU A HD23 
1413 N  N    . LYS A 96  ? 0.89130 0.73511 0.42826 0.35223  -0.04727 -0.01144 415 LYS A N    
1414 C  CA   . LYS A 96  ? 0.97954 0.80539 0.51860 0.32633  -0.04820 -0.01770 415 LYS A CA   
1415 C  C    . LYS A 96  ? 0.89381 0.71167 0.43595 0.33289  -0.04362 -0.00022 415 LYS A C    
1416 O  O    . LYS A 96  ? 0.97688 0.83392 0.54638 0.33613  -0.04586 0.01345  415 LYS A O    
1417 C  CB   . LYS A 96  ? 0.89737 0.76380 0.46693 0.30587  -0.05639 -0.02308 415 LYS A CB   
1418 C  CG   . LYS A 96  ? 0.91493 0.77006 0.48997 0.27836  -0.05730 -0.02965 415 LYS A CG   
1419 C  CD   . LYS A 96  ? 0.94504 0.75326 0.48809 0.26291  -0.05343 -0.04799 415 LYS A CD   
1420 C  CE   . LYS A 96  ? 0.85511 0.65077 0.40172 0.23422  -0.05264 -0.05393 415 LYS A CE   
1421 N  NZ   . LYS A 96  ? 1.18915 0.93567 0.70160 0.21501  -0.04654 -0.07300 415 LYS A NZ   
1422 H  H    . LYS A 96  ? 0.82312 0.82312 0.82312 0.00000  0.00000  0.00000  415 LYS A H    
1423 H  HA   . LYS A 96  ? 0.92267 0.92267 0.92267 0.00000  0.00000  -0.00000 415 LYS A HA   
1424 H  HB2  . LYS A 96  ? 0.85249 0.85249 0.85249 -0.00000 0.00000  0.00000  415 LYS A HB2  
1425 H  HB3  . LYS A 96  ? 0.85249 0.85249 0.85249 -0.00000 0.00000  0.00000  415 LYS A HB3  
1426 H  HG2  . LYS A 96  ? 0.87124 0.87124 0.87124 0.00000  0.00000  0.00000  415 LYS A HG2  
1427 H  HG3  . LYS A 96  ? 0.87124 0.87124 0.87124 0.00000  0.00000  0.00000  415 LYS A HG3  
1428 H  HD2  . LYS A 96  ? 0.87581 0.87581 0.87581 -0.00000 -0.00000 0.00000  415 LYS A HD2  
1429 H  HD3  . LYS A 96  ? 0.87581 0.87581 0.87581 -0.00000 -0.00000 0.00000  415 LYS A HD3  
1430 H  HE2  . LYS A 96  ? 0.76430 0.76430 0.76430 -0.00000 0.00000  -0.00000 415 LYS A HE2  
1431 H  HE3  . LYS A 96  ? 0.76430 0.76430 0.76430 -0.00000 0.00000  -0.00000 415 LYS A HE3  
1432 H  HZ1  . LYS A 96  ? 1.13182 1.13182 1.13182 0.00000  0.00000  0.00000  415 LYS A HZ1  
1433 H  HZ2  . LYS A 96  ? 1.13182 1.13182 1.13182 0.00000  0.00000  0.00000  415 LYS A HZ2  
1434 H  HZ3  . LYS A 96  ? 1.13182 1.13182 1.13182 0.00000  0.00000  0.00000  415 LYS A HZ3  
1435 N  N    . TYR A 97  ? 0.97713 0.74373 0.48873 0.33540  -0.03623 -0.00057 416 TYR A N    
1436 C  CA   . TYR A 97  ? 0.89603 0.65691 0.40519 0.35001  -0.03137 0.01826  416 TYR A CA   
1437 C  C    . TYR A 97  ? 0.90528 0.68778 0.43987 0.32902  -0.03503 0.02423  416 TYR A C    
1438 O  O    . TYR A 97  ? 0.96602 0.78621 0.52277 0.33680  -0.03650 0.03951  416 TYR A O    
1439 C  CB   . TYR A 97  ? 0.99259 0.68719 0.45740 0.36122  -0.02089 0.01775  416 TYR A CB   
1440 C  CG   . TYR A 97  ? 0.99160 0.68527 0.44974 0.38666  -0.01563 0.03931  416 TYR A CG   
1441 C  CD1  . TYR A 97  ? 0.97762 0.71693 0.45156 0.41334  -0.01702 0.05347  416 TYR A CD1  
1442 C  CD2  . TYR A 97  ? 1.04496 0.69566 0.48028 0.38407  -0.00887 0.04566  416 TYR A CD2  
1443 C  CE1  . TYR A 97  ? 0.94100 0.69605 0.41997 0.42665  -0.00965 0.06718  416 TYR A CE1  
1444 C  CE2  . TYR A 97  ? 1.42667 1.08210 0.85497 0.41035  -0.00461 0.06642  416 TYR A CE2  
1445 C  CZ   . TYR A 97  ? 0.98117 0.69509 0.43603 0.42842  -0.00468 0.07480  416 TYR A CZ   
1446 O  OH   . TYR A 97  ? 0.96668 0.70519 0.43109 0.43848  0.00335  0.08582  416 TYR A OH   
1447 H  H    . TYR A 97  ? 0.88509 0.88509 0.88509 0.00000  -0.00000 -0.00000 416 TYR A H    
1448 H  HA   . TYR A 97  ? 0.78450 0.78450 0.78450 0.00000  -0.00000 0.00000  416 TYR A HA   
1449 H  HB2  . TYR A 97  ? 0.85612 0.85612 0.85612 0.00000  -0.00000 -0.00000 416 TYR A HB2  
1450 H  HB3  . TYR A 97  ? 0.85612 0.85612 0.85612 0.00000  -0.00000 -0.00000 416 TYR A HB3  
1451 H  HD1  . TYR A 97  ? 0.85970 0.85970 0.85970 0.00000  -0.00000 0.00000  416 TYR A HD1  
1452 H  HD2  . TYR A 97  ? 0.88962 0.88962 0.88962 -0.00000 0.00000  0.00000  416 TYR A HD2  
1453 H  HE1  . TYR A 97  ? 0.82406 0.82406 0.82406 0.00000  0.00000  -0.00000 416 TYR A HE1  
1454 H  HE2  . TYR A 97  ? 1.34675 1.34675 1.34675 0.00000  0.00000  0.00000  416 TYR A HE2  
1455 H  HH   . TYR A 97  ? 0.84244 0.84244 0.84244 0.00000  0.00000  -0.00000 416 TYR A HH   
1456 N  N    . HIS A 98  ? 1.00751 0.76880 0.53882 0.30099  -0.03591 0.01130  417 HIS A N    
1457 C  CA   . HIS A 98  ? 0.90487 0.68553 0.45928 0.27914  -0.03898 0.01468  417 HIS A CA   
1458 C  C    . HIS A 98  ? 0.95485 0.76571 0.53335 0.25560  -0.04643 -0.00041 417 HIS A C    
1459 O  O    . HIS A 98  ? 0.88128 0.67200 0.44983 0.23346  -0.04647 -0.01684 417 HIS A O    
1460 C  CB   . HIS A 98  ? 0.95999 0.69067 0.48839 0.26719  -0.03202 0.01458  417 HIS A CB   
1461 C  CG   . HIS A 98  ? 1.34021 1.04584 0.84578 0.29324  -0.02465 0.03277  417 HIS A CG   
1462 N  ND1  . HIS A 98  ? 1.29509 0.93420 0.75643 0.30019  -0.01417 0.03222  417 HIS A ND1  
1463 C  CD2  . HIS A 98  ? 1.05191 0.79179 0.57124 0.31462  -0.02553 0.05199  417 HIS A CD2  
1464 C  CE1  . HIS A 98  ? 1.04047 0.67441 0.48917 0.32850  -0.00939 0.05184  417 HIS A CE1  
1465 N  NE2  . HIS A 98  ? 1.68733 1.38609 1.17221 0.33688  -0.01684 0.06356  417 HIS A NE2  
1466 H  H    . HIS A 98  ? 0.92731 0.92731 0.92731 0.00000  -0.00000 -0.00000 417 HIS A H    
1467 H  HA   . HIS A 98  ? 0.82113 0.82113 0.82113 0.00000  0.00000  0.00000  417 HIS A HA   
1468 H  HB2  . HIS A 98  ? 0.85687 0.85687 0.85687 0.00000  0.00000  -0.00000 417 HIS A HB2  
1469 H  HB3  . HIS A 98  ? 0.85687 0.85687 0.85687 0.00000  0.00000  -0.00000 417 HIS A HB3  
1470 H  HD1  . HIS A 98  ? 1.19554 1.19554 1.19554 0.00000  0.00000  0.00000  417 HIS A HD1  
1471 H  HD2  . HIS A 98  ? 0.96723 0.96723 0.96723 0.00000  0.00000  0.00000  417 HIS A HD2  
1472 H  HE1  . HIS A 98  ? 0.88287 0.88287 0.88287 0.00000  -0.00000 0.00000  417 HIS A HE1  
1473 N  N    . TYR A 99  ? 0.82700 0.68714 0.43556 0.26110  -0.05180 0.00508  418 TYR A N    
1474 C  CA   . TYR A 99  ? 0.92880 0.82264 0.56248 0.24348  -0.05815 -0.00469 418 TYR A CA   
1475 C  C    . TYR A 99  ? 0.78105 0.68805 0.43455 0.22488  -0.05841 -0.00015 418 TYR A C    
1476 O  O    . TYR A 99  ? 0.69351 0.62669 0.36629 0.23001  -0.05788 0.01300  418 TYR A O    
1477 C  CB   . TYR A 99  ? 0.68546 0.61810 0.33725 0.25941  -0.06102 0.00122  418 TYR A CB   
1478 C  CG   . TYR A 99  ? 0.97027 0.93135 0.63792 0.24992  -0.06684 -0.00982 418 TYR A CG   
1479 C  CD1  . TYR A 99  ? 0.88728 0.83927 0.54351 0.23697  -0.07033 -0.02840 418 TYR A CD1  
1480 C  CD2  . TYR A 99  ? 0.86612 0.86366 0.55782 0.25470  -0.06785 -0.00184 418 TYR A CD2  
1481 C  CE1  . TYR A 99  ? 1.09839 1.08402 0.76906 0.23154  -0.07627 -0.03792 418 TYR A CE1  
1482 C  CE2  . TYR A 99  ? 0.87913 0.90207 0.58243 0.25100  -0.07237 -0.00998 418 TYR A CE2  
1483 C  CZ   . TYR A 99  ? 0.90635 0.92675 0.60016 0.24080  -0.07737 -0.02758 418 TYR A CZ   
1484 O  OH   . TYR A 99  ? 1.35749 1.41040 1.06284 0.23991  -0.08250 -0.03522 418 TYR A OH   
1485 H  H    . TYR A 99  ? 0.78114 0.78114 0.78114 0.00000  -0.00000 0.00000  418 TYR A H    
1486 H  HA   . TYR A 99  ? 0.92682 0.92682 0.92682 0.00000  0.00000  0.00000  418 TYR A HA   
1487 H  HB2  . TYR A 99  ? 0.65758 0.65758 0.65758 0.00000  0.00000  0.00000  418 TYR A HB2  
1488 H  HB3  . TYR A 99  ? 0.65758 0.65758 0.65758 0.00000  0.00000  0.00000  418 TYR A HB3  
1489 H  HD1  . TYR A 99  ? 0.90928 0.90928 0.90928 -0.00000 -0.00000 0.00000  418 TYR A HD1  
1490 H  HD2  . TYR A 99  ? 0.91629 0.91629 0.91629 -0.00000 -0.00000 0.00000  418 TYR A HD2  
1491 H  HE1  . TYR A 99  ? 1.18184 1.18184 1.18184 -0.00000 0.00000  -0.00000 418 TYR A HE1  
1492 H  HE2  . TYR A 99  ? 0.94670 0.94670 0.94670 -0.00000 -0.00000 -0.00000 418 TYR A HE2  
1493 H  HH   . TYR A 99  ? 1.53355 1.53355 1.53355 -0.00000 0.00000  -0.00000 418 TYR A HH   
1494 N  N    . GLU A 100 ? 0.73973 0.62998 0.38784 0.20139  -0.05849 -0.01229 419 GLU A N    
1495 C  CA   . GLU A 100 ? 0.75724 0.65138 0.41753 0.18311  -0.05725 -0.00862 419 GLU A CA   
1496 C  C    . GLU A 100 ? 0.74121 0.68216 0.43614 0.17681  -0.06116 -0.00643 419 GLU A C    
1497 O  O    . GLU A 100 ? 0.64011 0.60790 0.34840 0.18036  -0.06526 -0.01244 419 GLU A O    
1498 C  CB   . GLU A 100 ? 0.70650 0.57351 0.35191 0.15730  -0.05551 -0.02441 419 GLU A CB   
1499 C  CG   . GLU A 100 ? 0.86131 0.67092 0.46706 0.16012  -0.04832 -0.02668 419 GLU A CG   
1500 C  CD   . GLU A 100 ? 1.22323 1.00879 0.81540 0.17552  -0.04235 -0.00712 419 GLU A CD   
1501 O  OE1  . GLU A 100 ? 0.97593 0.78324 0.58685 0.17020  -0.04314 0.00332  419 GLU A OE1  
1502 O  OE2  . GLU A 100 ? 1.24106 0.98787 0.80289 0.19413  -0.03661 -0.00236 419 GLU A OE2  
1503 H  H    . GLU A 100 ? 0.70427 0.70427 0.70427 -0.00000 0.00000  0.00000  419 GLU A H    
1504 H  HA   . GLU A 100 ? 0.73172 0.73172 0.73172 -0.00000 0.00000  -0.00000 419 GLU A HA   
1505 H  HB2  . GLU A 100 ? 0.64650 0.64650 0.64650 -0.00000 -0.00000 -0.00000 419 GLU A HB2  
1506 H  HB3  . GLU A 100 ? 0.64650 0.64650 0.64650 -0.00000 -0.00000 -0.00000 419 GLU A HB3  
1507 H  HG2  . GLU A 100 ? 0.80097 0.80097 0.80097 0.00000  0.00000  0.00000  419 GLU A HG2  
1508 H  HG3  . GLU A 100 ? 0.80097 0.80097 0.80097 0.00000  0.00000  0.00000  419 GLU A HG3  
1509 N  N    . GLY A 101 ? 0.73703 0.68564 0.44388 0.16798  -0.05893 0.00237  420 GLY A N    
1510 C  CA   . GLY A 101 ? 0.65925 0.64250 0.39437 0.15625  -0.06042 0.00155  420 GLY A CA   
1511 C  C    . GLY A 101 ? 0.60130 0.61504 0.35488 0.17028  -0.05999 0.01079  420 GLY A C    
1512 O  O    . GLY A 101 ? 0.59247 0.63087 0.36600 0.16364  -0.06018 0.00805  420 GLY A O    
1513 H  H    . GLY A 101 ? 0.74787 0.74787 0.74787 0.00000  -0.00000 0.00000  420 GLY A H    
1514 H  HA2  . GLY A 101 ? 0.67970 0.67970 0.67970 0.00000  0.00000  0.00000  420 GLY A HA2  
1515 H  HA3  . GLY A 101 ? 0.67970 0.67970 0.67970 0.00000  0.00000  0.00000  420 GLY A HA3  
1516 N  N    . MET A 102 ? 0.55008 0.56210 0.29619 0.18925  -0.05801 0.02176  421 MET A N    
1517 C  CA   . MET A 102 ? 0.55533 0.59367 0.31519 0.20120  -0.05597 0.02933  421 MET A CA   
1518 C  C    . MET A 102 ? 0.56446 0.62219 0.33798 0.19657  -0.05099 0.04045  421 MET A C    
1519 O  O    . MET A 102 ? 0.50307 0.58164 0.29042 0.19745  -0.04724 0.04357  421 MET A O    
1520 C  CB   . MET A 102 ? 0.61640 0.64835 0.36140 0.22328  -0.05594 0.03328  421 MET A CB   
1521 C  CG   . MET A 102 ? 0.58691 0.60887 0.32127 0.22794  -0.06035 0.02118  421 MET A CG   
1522 S  SD   . MET A 102 ? 0.63175 0.68319 0.38490 0.22739  -0.06197 0.01642  421 MET A SD   
1523 C  CE   . MET A 102 ? 0.65697 0.72265 0.41169 0.24740  -0.05628 0.03041  421 MET A CE   
1524 H  H    . MET A 102 ? 0.56460 0.56460 0.56460 0.00000  0.00000  -0.00000 421 MET A H    
1525 H  HA   . MET A 102 ? 0.58693 0.58693 0.58693 0.00000  0.00000  0.00000  421 MET A HA   
1526 H  HB2  . MET A 102 ? 0.65171 0.65171 0.65171 0.00000  0.00000  0.00000  421 MET A HB2  
1527 H  HB3  . MET A 102 ? 0.65171 0.65171 0.65171 0.00000  0.00000  0.00000  421 MET A HB3  
1528 H  HG2  . MET A 102 ? 0.60807 0.60807 0.60807 0.00000  0.00000  0.00000  421 MET A HG2  
1529 H  HG3  . MET A 102 ? 0.60807 0.60807 0.60807 0.00000  0.00000  0.00000  421 MET A HG3  
1530 H  HE1  . MET A 102 ? 0.71778 0.71778 0.71778 0.00000  -0.00000 -0.00000 421 MET A HE1  
1531 H  HE2  . MET A 102 ? 0.71778 0.71778 0.71778 0.00000  -0.00000 -0.00000 421 MET A HE2  
1532 H  HE3  . MET A 102 ? 0.71778 0.71778 0.71778 0.00000  -0.00000 -0.00000 421 MET A HE3  
1533 N  N    . SER A 103 ? 0.51496 0.56621 0.28297 0.19126  -0.04993 0.04629  422 SER A N    
1534 C  CA   . SER A 103 ? 0.56297 0.63841 0.34224 0.18680  -0.04568 0.05614  422 SER A CA   
1535 C  C    . SER A 103 ? 0.56301 0.63575 0.34557 0.16792  -0.04552 0.05515  422 SER A C    
1536 O  O    . SER A 103 ? 0.61383 0.66038 0.38177 0.16421  -0.04775 0.05221  422 SER A O    
1537 C  CB   . SER A 103 ? 0.60939 0.69137 0.37730 0.20497  -0.04433 0.06789  422 SER A CB   
1538 O  OG   . SER A 103 ? 1.13735 1.22589 0.90287 0.22201  -0.04344 0.06947  422 SER A OG   
1539 H  H    . SER A 103 ? 0.53939 0.53939 0.53939 -0.00000 0.00000  0.00000  422 SER A H    
1540 H  HA   . SER A 103 ? 0.61870 0.61870 0.61870 0.00000  -0.00000 0.00000  422 SER A HA   
1541 H  HB2  . SER A 103 ? 0.67248 0.67248 0.67248 0.00000  0.00000  0.00000  422 SER A HB2  
1542 H  HB3  . SER A 103 ? 0.67248 0.67248 0.67248 0.00000  0.00000  0.00000  422 SER A HB3  
1543 H  HG   . SER A 103 ? 1.30770 1.30770 1.30770 0.00000  0.00000  -0.00000 422 SER A HG   
1544 N  N    . VAL A 104 ? 0.52944 0.62791 0.32861 0.15557  -0.04156 0.05774  423 VAL A N    
1545 C  CA   . VAL A 104 ? 0.51236 0.61278 0.31586 0.13646  -0.04081 0.05665  423 VAL A CA   
1546 C  C    . VAL A 104 ? 0.51390 0.61439 0.30351 0.14235  -0.04129 0.06752  423 VAL A C    
1547 O  O    . VAL A 104 ? 0.54468 0.66982 0.33556 0.15259  -0.03953 0.07652  423 VAL A O    
1548 C  CB   . VAL A 104 ? 0.53349 0.65956 0.35714 0.12021  -0.03525 0.05425  423 VAL A CB   
1549 C  CG1  . VAL A 104 ? 0.60180 0.73187 0.42886 0.10103  -0.03433 0.05294  423 VAL A CG1  
1550 C  CG2  . VAL A 104 ? 0.52178 0.64537 0.35599 0.11837  -0.03330 0.04543  423 VAL A CG2  
1551 H  H    . VAL A 104 ? 0.59564 0.59564 0.59564 0.00000  0.00000  -0.00000 423 VAL A H    
1552 H  HA   . VAL A 104 ? 0.57766 0.57766 0.57766 0.00000  0.00000  0.00000  423 VAL A HA   
1553 H  HB   . VAL A 104 ? 0.62133 0.62133 0.62133 0.00000  0.00000  0.00000  423 VAL A HB   
1554 H  HG11 . VAL A 104 ? 0.70627 0.70627 0.70627 -0.00000 0.00000  0.00000  423 VAL A HG11 
1555 H  HG12 . VAL A 104 ? 0.70627 0.70627 0.70627 -0.00000 0.00000  0.00000  423 VAL A HG12 
1556 H  HG13 . VAL A 104 ? 0.70627 0.70627 0.70627 -0.00000 0.00000  0.00000  423 VAL A HG13 
1557 H  HG21 . VAL A 104 ? 0.61051 0.61051 0.61051 0.00000  -0.00000 -0.00000 423 VAL A HG21 
1558 H  HG22 . VAL A 104 ? 0.61051 0.61051 0.61051 0.00000  -0.00000 -0.00000 423 VAL A HG22 
1559 H  HG23 . VAL A 104 ? 0.61051 0.61051 0.61051 0.00000  -0.00000 -0.00000 423 VAL A HG23 
1560 N  N    . ALA A 105 ? 0.56928 0.64337 0.34426 0.13708  -0.04294 0.06677  424 ALA A N    
1561 C  CA   . ALA A 105 ? 0.70849 0.77925 0.46717 0.14287  -0.04232 0.07837  424 ALA A CA   
1562 C  C    . ALA A 105 ? 0.70909 0.80199 0.47865 0.12307  -0.04047 0.07956  424 ALA A C    
1563 O  O    . ALA A 105 ? 0.67396 0.79463 0.44345 0.12748  -0.03957 0.08965  424 ALA A O    
1564 C  CB   . ALA A 105 ? 0.56962 0.59173 0.29989 0.14801  -0.04256 0.07818  424 ALA A CB   
1565 H  H    . ALA A 105 ? 0.62402 0.62402 0.62402 0.00000  -0.00000 -0.00000 424 ALA A H    
1566 H  HA   . ALA A 105 ? 0.78322 0.78322 0.78322 -0.00000 0.00000  0.00000  424 ALA A HA   
1567 H  HB1  . ALA A 105 ? 0.57851 0.57851 0.57851 0.00000  0.00000  0.00000  424 ALA A HB1  
1568 H  HB2  . ALA A 105 ? 0.57851 0.57851 0.57851 0.00000  0.00000  0.00000  424 ALA A HB2  
1569 H  HB3  . ALA A 105 ? 0.57851 0.57851 0.57851 0.00000  0.00000  0.00000  424 ALA A HB3  
1570 N  N    . GLU A 106 ? 0.63997 0.72450 0.41847 0.10147  -0.03985 0.06886  425 GLU A N    
1571 C  CA   . GLU A 106 ? 0.53723 0.64152 0.32621 0.08112  -0.03742 0.06794  425 GLU A CA   
1572 C  C    . GLU A 106 ? 0.58971 0.70375 0.40075 0.06327  -0.03535 0.05445  425 GLU A C    
1573 O  O    . GLU A 106 ? 0.57987 0.67847 0.39372 0.06434  -0.03690 0.04536  425 GLU A O    
1574 C  CB   . GLU A 106 ? 0.62097 0.69902 0.39049 0.07349  -0.03707 0.07092  425 GLU A CB   
1575 C  CG   . GLU A 106 ? 1.12194 1.18653 0.86507 0.09387  -0.03732 0.08639  425 GLU A CG   
1576 C  CD   . GLU A 106 ? 1.92495 1.94741 1.64129 0.08847  -0.03485 0.08910  425 GLU A CD   
1577 O  OE1  . GLU A 106 ? 1.13318 1.14482 0.85466 0.06512  -0.03326 0.07848  425 GLU A OE1  
1578 O  OE2  . GLU A 106 ? 1.58440 1.58373 1.27285 0.10818  -0.03339 0.10206  425 GLU A OE2  
1579 H  H    . GLU A 106 ? 0.71443 0.71443 0.71443 0.00000  0.00000  0.00000  425 GLU A H    
1580 H  HA   . GLU A 106 ? 0.60324 0.60324 0.60324 0.00000  0.00000  -0.00000 425 GLU A HA   
1581 H  HB2  . GLU A 106 ? 0.68545 0.68545 0.68545 0.00000  0.00000  0.00000  425 GLU A HB2  
1582 H  HB3  . GLU A 106 ? 0.68545 0.68545 0.68545 0.00000  0.00000  0.00000  425 GLU A HB3  
1583 H  HG2  . GLU A 106 ? 1.27067 1.27067 1.27067 0.00000  0.00000  -0.00000 425 GLU A HG2  
1584 H  HG3  . GLU A 106 ? 1.27067 1.27067 1.27067 0.00000  0.00000  -0.00000 425 GLU A HG3  
1585 N  N    . CYS A 107 ? 0.51644 0.65759 0.34163 0.04792  -0.03136 0.05305  426 CYS A N    
1586 C  CA   . CYS A 107 ? 0.49019 0.64000 0.33379 0.03162  -0.02713 0.04135  426 CYS A CA   
1587 C  C    . CYS A 107 ? 0.52732 0.67751 0.37171 0.01139  -0.02546 0.03709  426 CYS A C    
1588 O  O    . CYS A 107 ? 0.52187 0.67358 0.35451 0.00792  -0.02632 0.04477  426 CYS A O    
1589 C  CB   . CYS A 107 ? 0.49807 0.67498 0.35521 0.02780  -0.02076 0.04104  426 CYS A CB   
1590 S  SG   . CYS A 107 ? 0.62643 0.80580 0.48443 0.04767  -0.01990 0.04479  426 CYS A SG   
1591 H  H    . CYS A 107 ? 0.60752 0.60752 0.60752 0.00000  0.00000  0.00000  426 CYS A H    
1592 H  HA   . CYS A 107 ? 0.58685 0.58685 0.58685 0.00000  -0.00000 0.00000  426 CYS A HA   
1593 H  HB2  . CYS A 107 ? 0.61256 0.61256 0.61256 0.00000  0.00000  -0.00000 426 CYS A HB2  
1594 H  HB3  . CYS A 107 ? 0.61256 0.61256 0.61256 0.00000  0.00000  -0.00000 426 CYS A HB3  
1595 N  N    . GLY A 108 ? 0.42719 0.57810 0.28477 -0.00057 -0.02247 0.02536  427 GLY A N    
1596 C  CA   . GLY A 108 ? 0.52141 0.67542 0.38127 -0.02047 -0.02000 0.01994  427 GLY A CA   
1597 C  C    . GLY A 108 ? 0.55734 0.71837 0.43427 -0.02905 -0.01547 0.00692  427 GLY A C    
1598 O  O    . GLY A 108 ? 0.47191 0.62960 0.35551 -0.01776 -0.01587 0.00222  427 GLY A O    
1599 H  H    . GLY A 108 ? 0.50975 0.50975 0.50975 0.00000  -0.00000 0.00000  427 GLY A H    
1600 H  HA2  . GLY A 108 ? 0.63249 0.63249 0.63249 0.00000  -0.00000 0.00000  427 GLY A HA2  
1601 H  HA3  . GLY A 108 ? 0.63249 0.63249 0.63249 0.00000  -0.00000 0.00000  427 GLY A HA3  
1602 N  N    . CYS A 109 ? 0.50332 0.67513 0.38584 -0.04739 -0.01081 0.00162  428 CYS A N    
1603 C  CA   . CYS A 109 ? 0.43472 0.61463 0.33217 -0.05502 -0.00527 -0.01079 428 CYS A CA   
1604 C  C    . CYS A 109 ? 0.45960 0.63332 0.35684 -0.06007 -0.00927 -0.01854 428 CYS A C    
1605 O  O    . CYS A 109 ? 0.48106 0.64618 0.36680 -0.07090 -0.01178 -0.01629 428 CYS A O    
1606 C  CB   . CYS A 109 ? 0.44192 0.63750 0.34450 -0.07303 0.00270  -0.01404 428 CYS A CB   
1607 S  SG   . CYS A 109 ? 0.57699 0.78363 0.48178 -0.07166 0.01059  -0.01043 428 CYS A SG   
1608 H  H    . CYS A 109 ? 0.62697 0.62697 0.62697 0.00000  -0.00000 -0.00000 428 CYS A H    
1609 H  HA   . CYS A 109 ? 0.55386 0.55386 0.55386 0.00000  -0.00000 -0.00000 428 CYS A HA   
1610 H  HB2  . CYS A 109 ? 0.57082 0.57082 0.57082 0.00000  -0.00000 -0.00000 428 CYS A HB2  
1611 H  HB3  . CYS A 109 ? 0.57082 0.57082 0.57082 0.00000  -0.00000 -0.00000 428 CYS A HB3  
1612 N  N    . ARG A 110 ? 0.49059 0.66898 0.39835 -0.05165 -0.00945 -0.02729 429 ARG A N    
1613 C  CA   . ARG A 110 ? 0.51586 0.69565 0.42436 -0.05696 -0.01372 -0.03656 429 ARG A CA   
1614 C  C    . ARG A 110 ? 0.51175 0.71456 0.43779 -0.05733 -0.00962 -0.04904 429 ARG A C    
1615 O  O    . ARG A 110 ? 0.41296 0.62854 0.34348 -0.07210 -0.00930 -0.05858 429 ARG A O    
1616 C  CB   . ARG A 110 ? 0.44547 0.61120 0.34469 -0.04262 -0.02126 -0.03462 429 ARG A CB   
1617 C  CG   . ARG A 110 ? 0.45110 0.59154 0.32956 -0.04187 -0.02476 -0.02352 429 ARG A CG   
1618 C  CD   . ARG A 110 ? 0.45757 0.58582 0.32315 -0.06225 -0.02385 -0.02484 429 ARG A CD   
1619 N  NE   . ARG A 110 ? 0.52885 0.62828 0.37025 -0.05764 -0.02565 -0.01267 429 ARG A NE   
1620 C  CZ   . ARG A 110 ? 0.63749 0.73482 0.47030 -0.05610 -0.02386 0.00005  429 ARG A CZ   
1621 N  NH1  . ARG A 110 ? 0.47924 0.60106 0.32554 -0.06198 -0.02018 0.00116  429 ARG A NH1  
1622 N  NH2  . ARG A 110 ? 0.50788 0.57903 0.31659 -0.04775 -0.02523 0.01160  429 ARG A NH2  
1623 O  OXT  . ARG A 110 ? 0.44116 0.65032 0.37579 -0.04258 -0.00534 -0.04949 429 ARG A OXT  
1624 H  H    . ARG A 110 ? 0.62442 0.62442 0.62442 0.00000  0.00000  0.00000  429 ARG A H    
1625 H  HA   . ARG A 110 ? 0.65561 0.65561 0.65561 0.00000  0.00000  0.00000  429 ARG A HA   
1626 H  HB2  . ARG A 110 ? 0.56180 0.56180 0.56180 0.00000  0.00000  -0.00000 429 ARG A HB2  
1627 H  HB3  . ARG A 110 ? 0.56180 0.56180 0.56180 0.00000  0.00000  -0.00000 429 ARG A HB3  
1628 H  HG2  . ARG A 110 ? 0.55013 0.55013 0.55013 0.00000  -0.00000 0.00000  429 ARG A HG2  
1629 H  HG3  . ARG A 110 ? 0.55013 0.55013 0.55013 0.00000  -0.00000 0.00000  429 ARG A HG3  
1630 H  HD2  . ARG A 110 ? 0.54394 0.54394 0.54394 -0.00000 0.00000  -0.00000 429 ARG A HD2  
1631 H  HD3  . ARG A 110 ? 0.54394 0.54394 0.54394 -0.00000 0.00000  -0.00000 429 ARG A HD3  
1632 H  HE   . ARG A 110 ? 0.61221 0.61221 0.61221 0.00000  0.00000  0.00000  429 ARG A HE   
1633 H  HH11 . ARG A 110 ? 0.56359 0.56359 0.56359 0.00000  -0.00000 0.00000  429 ARG A HH11 
1634 H  HH12 . ARG A 110 ? 0.56359 0.56359 0.56359 0.00000  -0.00000 0.00000  429 ARG A HH12 
1635 H  HH21 . ARG A 110 ? 0.55513 0.55513 0.55513 -0.00000 0.00000  0.00000  429 ARG A HH21 
1636 H  HH22 . ARG A 110 ? 0.55513 0.55513 0.55513 -0.00000 0.00000  0.00000  429 ARG A HH22 
1637 CL CL   . CL  B .   ? 0.64514 0.62213 0.45896 -0.26903 -0.10145 0.05290  501 CL  A CL   
1638 CL CL   . CL  C .   ? 0.89549 0.89528 0.36790 0.17928  -0.15281 -0.15287 502 CL  A CL   
1639 CL CL   . CL  D .   ? 1.15281 1.18130 0.59536 0.23639  -0.34888 -0.20286 503 CL  A CL   
1640 CL CL   . CL  E .   ? 0.60810 0.91078 0.40503 0.39581  0.05033  0.15828  504 CL  A CL   
1641 CL CL   . CL  F .   ? 0.70745 0.79162 0.25241 -0.01333 -0.12043 -0.00280 505 CL  A CL   
1642 NA NA   . NA  G .   ? 0.74870 0.78872 0.65134 0.10638  0.07925  -0.02091 506 NA  A NA   
1643 C  C1   . GOL H .   ? 1.46178 1.10387 1.79130 -0.02452 0.05722  -0.05599 507 GOL A C1   
1644 O  O1   . GOL H .   ? 1.45797 1.10005 1.78690 -0.02032 0.05739  -0.05648 507 GOL A O1   
1645 C  C2   . GOL H .   ? 1.46202 1.10333 1.79122 -0.02425 0.05712  -0.05510 507 GOL A C2   
1646 O  O2   . GOL H .   ? 1.46010 1.10053 1.79390 -0.02328 0.05734  -0.05527 507 GOL A O2   
1647 C  C3   . GOL H .   ? 1.46126 1.10187 1.78865 -0.02267 0.05712  -0.05480 507 GOL A C3   
1648 O  O3   . GOL H .   ? 1.46055 1.10062 1.78839 -0.02237 0.05697  -0.05468 507 GOL A O3   
1649 H  H11  . GOL H .   ? 1.74403 1.74403 1.74403 0.00000  -0.00000 -0.00000 507 GOL A H11  
1650 H  H12  . GOL H .   ? 1.74403 1.74403 1.74403 0.00000  -0.00000 -0.00000 507 GOL A H12  
1651 H  HO1  . GOL H .   ? 1.73922 1.73922 1.73922 -0.00000 -0.00000 0.00000  507 GOL A HO1  
1652 H  H2   . GOL H .   ? 1.74388 1.74388 1.74388 0.00000  -0.00000 0.00000  507 GOL A H2   
1653 H  HO2  . GOL H .   ? 1.74307 1.74307 1.74307 -0.00000 0.00000  0.00000  507 GOL A HO2  
1654 H  H31  . GOL H .   ? 1.74197 1.74197 1.74197 0.00000  -0.00000 0.00000  507 GOL A H31  
1655 H  H32  . GOL H .   ? 1.74197 1.74197 1.74197 0.00000  -0.00000 0.00000  507 GOL A H32  
1656 H  HO3  . GOL H .   ? 1.74108 1.74108 1.74108 0.00000  0.00000  0.00000  507 GOL A HO3  
1657 C  C1   . GOL I .   ? 1.02078 0.97143 1.42987 0.12560  0.10524  -0.26831 508 GOL A C1   
1658 O  O1   . GOL I .   ? 1.02824 0.97914 1.43140 0.12862  0.10611  -0.26727 508 GOL A O1   
1659 C  C2   . GOL I .   ? 1.02224 0.97262 1.42650 0.12500  0.10492  -0.26773 508 GOL A C2   
1660 O  O2   . GOL I .   ? 1.02787 0.97658 1.42946 0.12428  0.10446  -0.26769 508 GOL A O2   
1661 C  C3   . GOL I .   ? 1.02295 0.97384 1.43220 0.12678  0.10445  -0.26734 508 GOL A C3   
1662 O  O3   . GOL I .   ? 1.02512 0.97514 1.43021 0.12660  0.10465  -0.26613 508 GOL A O3   
1663 H  H11  . GOL I .   ? 1.37009 1.37009 1.37009 0.00000  0.00000  0.00000  508 GOL A H11  
1664 H  H12  . GOL I .   ? 1.37009 1.37009 1.37009 0.00000  0.00000  0.00000  508 GOL A H12  
1665 H  HO1  . GOL I .   ? 1.37677 1.37677 1.37677 -0.00000 -0.00000 -0.00000 508 GOL A HO1  
1666 H  H2   . GOL I .   ? 1.36980 1.36980 1.36980 0.00000  0.00000  0.00000  508 GOL A H2   
1667 H  HO2  . GOL I .   ? 1.37482 1.37482 1.37482 0.00000  0.00000  0.00000  508 GOL A HO2  
1668 H  H31  . GOL I .   ? 1.37285 1.37285 1.37285 0.00000  -0.00000 0.00000  508 GOL A H31  
1669 H  H32  . GOL I .   ? 1.37285 1.37285 1.37285 0.00000  -0.00000 0.00000  508 GOL A H32  
1670 H  HO3  . GOL I .   ? 1.37344 1.37344 1.37344 0.00000  -0.00000 0.00000  508 GOL A HO3  
1671 O  O    . HOH J .   ? 0.54996 0.82165 0.43574 -0.07293 -0.04348 -0.30627 601 HOH A O    
1672 O  O    . HOH J .   ? 0.81047 1.09400 0.82368 0.35900  -0.02401 -0.12719 602 HOH A O    
1673 O  O    . HOH J .   ? 0.41970 0.85171 0.24137 -0.15394 -0.05397 0.03673  603 HOH A O    
1674 O  O    . HOH J .   ? 0.97361 0.73427 1.14226 0.15645  -0.06768 -0.01683 604 HOH A O    
1675 O  O    . HOH J .   ? 0.56861 1.14809 0.55625 -0.04290 -0.15115 -0.31549 605 HOH A O    
1676 O  O    . HOH J .   ? 1.14740 0.93600 1.16824 0.26810  -0.34952 -0.06806 606 HOH A O    
1677 O  O    . HOH J .   ? 0.85807 0.68782 0.83480 0.22295  -0.22203 -0.35798 607 HOH A O    
1678 O  O    . HOH J .   ? 1.26262 1.05696 0.65169 0.12121  -0.03638 -0.16060 608 HOH A O    
1679 O  O    . HOH J .   ? 0.80538 0.60616 0.24814 0.20091  -0.00742 0.06535  609 HOH A O    
1680 O  O    . HOH J .   ? 0.31876 0.52455 0.15281 -0.08595 -0.03454 0.05638  610 HOH A O    
1681 O  O    . HOH J .   ? 0.91221 0.94542 0.72529 0.15674  0.27996  0.42587  611 HOH A O    
1682 O  O    . HOH J .   ? 0.64974 0.58176 0.25721 -0.28788 -0.09818 0.08307  612 HOH A O    
1683 O  O    . HOH J .   ? 0.48118 0.28604 0.76855 0.05148  0.09035  0.15371  613 HOH A O    
1684 O  O    . HOH J .   ? 0.62605 0.67344 0.55992 -0.22855 0.07682  -0.14770 614 HOH A O    
1685 O  O    . HOH J .   ? 0.60253 0.63798 0.37995 0.09599  0.19542  -0.17242 615 HOH A O    
1686 O  O    . HOH J .   ? 0.58858 1.11555 0.72309 -0.03359 -0.09907 0.49807  616 HOH A O    
1687 O  O    . HOH J .   ? 0.49514 0.66997 0.29537 0.24052  0.03446  0.02108  617 HOH A O    
1688 O  O    . HOH J .   ? 0.65542 0.71862 0.43180 0.03072  -0.25568 -0.17603 618 HOH A O    
1689 O  O    . HOH J .   ? 0.74173 0.54114 0.56059 -0.10164 0.27666  -0.13460 619 HOH A O    
1690 O  O    . HOH J .   ? 0.71511 0.92825 0.85721 0.36236  0.19039  0.31202  620 HOH A O    
1691 O  O    . HOH J .   ? 0.50417 0.70959 0.20497 -0.15969 0.03804  -0.02935 621 HOH A O    
1692 O  O    . HOH J .   ? 0.70951 0.96667 0.49751 0.05178  -0.03025 0.16509  622 HOH A O    
1693 O  O    . HOH J .   ? 0.64969 0.85839 0.48837 0.35982  0.04340  0.22793  623 HOH A O    
1694 O  O    . HOH J .   ? 1.03049 1.38514 1.32187 0.37961  -0.02336 0.57726  624 HOH A O    
1695 O  O    . HOH J .   ? 0.67269 1.18920 0.58336 0.21566  -0.09346 -0.13652 625 HOH A O    
1696 O  O    . HOH J .   ? 0.62490 0.70957 0.44886 0.01168  0.02348  -0.01088 626 HOH A O    
1697 O  O    . HOH J .   ? 1.21512 0.68836 0.75932 -0.12075 -0.22953 -0.29166 627 HOH A O    
1698 O  O    . HOH J .   ? 0.61738 0.65624 0.92841 -0.02161 0.42490  0.08450  628 HOH A O    
1699 O  O    . HOH J .   ? 0.53081 0.49187 0.57132 -0.12442 -0.16443 -0.00855 629 HOH A O    
1700 O  O    . HOH J .   ? 0.87557 0.87831 0.76959 0.11586  0.24501  0.17701  630 HOH A O    
1701 O  O    . HOH J .   ? 1.05418 0.95079 0.44017 0.50123  -0.04032 -0.13691 631 HOH A O    
1702 O  O    . HOH J .   ? 0.89871 0.92820 0.53269 0.19652  -0.21646 0.25478  632 HOH A O    
1703 O  O    . HOH J .   ? 1.02528 1.17504 1.08407 -0.31420 -0.08641 0.06415  633 HOH A O    
1704 O  O    . HOH J .   ? 0.68952 0.58625 0.73122 0.34497  0.08314  -0.11704 634 HOH A O    
1705 O  O    . HOH J .   ? 1.10173 1.12215 0.95068 0.28014  -0.13687 -0.26590 635 HOH A O    
1706 O  O    . HOH J .   ? 0.67238 1.21356 0.61090 0.39662  -0.20525 -0.40552 636 HOH A O    
1707 O  O    . HOH J .   ? 0.58562 0.67665 0.33177 0.24601  0.16109  0.17494  637 HOH A O    
1708 O  O    . HOH J .   ? 0.77861 0.69036 0.61357 0.21684  0.06017  -0.00729 638 HOH A O    
1709 O  O    . HOH J .   ? 0.78929 1.26764 0.79198 0.12950  -0.02369 -0.30918 639 HOH A O    
1710 O  O    . HOH J .   ? 0.85492 0.61638 0.43876 0.39261  -0.24648 -0.19156 640 HOH A O    
1711 O  O    . HOH J .   ? 1.13373 0.47746 0.97583 -0.05307 -0.27623 0.05760  641 HOH A O    
1712 O  O    . HOH J .   ? 0.83617 0.65467 0.38042 -0.02726 -0.03798 0.15006  642 HOH A O    
1713 O  O    . HOH J .   ? 0.99059 0.91109 0.58696 0.55711  0.17890  0.15271  643 HOH A O    
1714 O  O    . HOH J .   ? 0.72786 0.57895 0.46423 0.02480  -0.09737 0.01112  644 HOH A O    
1715 O  O    . HOH J .   ? 1.17650 0.77564 0.67231 0.14991  0.06886  0.17443  645 HOH A O    
1716 O  O    . HOH J .   ? 1.00713 0.94746 0.63998 0.10450  0.22188  0.17442  646 HOH A O    
1717 O  O    . HOH J .   ? 1.22068 0.57409 0.57926 0.05955  -0.10769 0.19024  647 HOH A O    
1718 O  O    . HOH J .   ? 1.19455 1.27268 0.81414 -0.04538 0.28026  0.00627  648 HOH A O    
1719 O  O    . HOH J .   ? 0.69907 0.74599 0.71004 0.02045  -0.23340 0.35632  649 HOH A O    
1720 O  O    . HOH J .   ? 0.93165 0.61524 0.49222 0.30735  -0.22812 -0.23263 650 HOH A O    
1721 O  O    . HOH J .   ? 0.99276 1.18700 0.90549 0.04904  0.16867  0.01060  651 HOH A O    
1722 O  O    . HOH J .   ? 0.60840 1.08943 0.60789 -0.16030 -0.08298 0.04427  652 HOH A O    
1723 O  O    . HOH J .   ? 0.93626 1.44686 0.43495 0.34454  -0.10362 -0.12609 653 HOH A O    
1724 O  O    . HOH J .   ? 1.26126 0.64607 1.05412 0.22292  -0.42734 -0.12846 654 HOH A O    
1725 O  O    . HOH J .   ? 1.00139 0.62226 0.92925 0.18929  0.00342  -0.26175 655 HOH A O    
1726 O  O    . HOH J .   ? 0.78340 0.62432 0.54312 0.16994  -0.11111 -0.03977 656 HOH A O    
1727 O  O    . HOH J .   ? 1.09726 0.93731 0.59843 -0.34999 0.38529  -0.16391 657 HOH A O    
1728 O  O    . HOH J .   ? 1.10296 1.34604 1.34952 0.41157  0.03030  -0.05220 658 HOH A O    
1729 O  O    . HOH J .   ? 0.77444 1.10231 0.68125 -0.02328 0.06950  0.08319  659 HOH A O    
1730 O  O    . HOH J .   ? 0.78651 0.98815 0.95805 0.13452  -0.03928 -0.04073 660 HOH A O    
1731 O  O    . HOH J .   ? 0.90038 0.95753 0.65554 0.20666  0.14213  0.07211  661 HOH A O    
1732 O  O    . HOH J .   ? 0.55231 0.81730 0.52365 0.38456  0.00485  0.05850  662 HOH A O    
1733 O  O    . HOH J .   ? 0.91675 1.26388 0.62974 -0.25327 -0.24148 -0.09918 663 HOH A O    
1734 O  O    . HOH J .   ? 0.76760 1.12063 0.81758 0.05967  -0.20066 -0.33009 664 HOH A O    
1735 O  O    . HOH J .   ? 0.99058 1.33682 1.19271 0.27389  -0.18892 0.15970  665 HOH A O    
1736 O  O    . HOH J .   ? 0.72685 0.60216 0.71118 0.05389  0.05989  0.37776  666 HOH A O    
1737 O  O    . HOH J .   ? 0.99436 1.06433 0.86820 0.34424  -0.39283 0.14485  667 HOH A O    
1738 O  O    . HOH J .   ? 0.91251 1.11582 0.79078 0.06692  -0.03345 0.23634  668 HOH A O    
1739 O  O    . HOH J .   ? 1.31346 1.12735 0.65770 0.18462  0.13024  0.03382  669 HOH A O    
1740 O  O    . HOH J .   ? 0.84431 0.99797 1.32870 -0.34834 -0.35879 0.34873  670 HOH A O    
1741 O  O    . HOH J .   ? 0.76230 1.15329 1.04343 0.32365  0.15880  0.06920  671 HOH A O    
1742 O  O    . HOH J .   ? 0.90543 0.99521 1.01347 -0.07972 0.01404  -0.43797 672 HOH A O    
1743 O  O    . HOH J .   ? 0.80298 1.48398 0.88072 0.18477  -0.22436 -0.27323 673 HOH A O    
1744 O  O    . HOH J .   ? 0.79630 1.24632 0.92209 0.18075  -0.22432 0.01001  674 HOH A O    
1745 O  O    . HOH J .   ? 0.74154 0.87697 0.80702 0.02432  0.04336  0.05043  675 HOH A O    
1746 O  O    . HOH J .   ? 1.03834 0.86944 0.91055 0.29289  -0.21369 -0.12939 676 HOH A O    
1747 O  O    . HOH J .   ? 0.88676 1.41567 0.55497 0.02613  0.14350  -0.32420 677 HOH A O    
1748 O  O    . HOH J .   ? 0.77214 0.76192 0.29022 0.10797  -0.10208 0.03281  678 HOH A O    
1749 O  O    . HOH J .   ? 1.02713 1.01673 1.00247 0.30238  -0.16876 -0.04579 679 HOH A O    
1750 O  O    . HOH J .   ? 1.04723 1.11123 0.96654 -0.56067 0.18154  0.16382  680 HOH A O    
1751 O  O    . HOH J .   ? 0.68211 1.09239 0.29557 -0.03265 -0.08689 0.04998  681 HOH A O    
1752 O  O    . HOH J .   ? 0.89006 1.33210 1.21972 -0.18036 0.14423  0.57278  682 HOH A O    
1753 O  O    . HOH J .   ? 0.80243 0.70097 0.58715 0.27858  -0.06513 -0.14953 683 HOH A O    
1754 O  O    . HOH J .   ? 1.22312 1.03782 0.70919 -0.63635 0.15206  -0.16883 684 HOH A O    
1755 O  O    . HOH J .   ? 0.90513 1.40763 0.87915 0.30714  -0.12801 -0.34332 685 HOH A O    
1756 O  O    . HOH J .   ? 0.93633 0.83132 1.14421 0.02171  -0.13492 0.30385  686 HOH A O    
1757 O  O    . HOH J .   ? 0.75546 0.83727 1.64249 -0.01141 0.10040  0.17483  687 HOH A O    
1758 O  O    . HOH J .   ? 0.83909 1.30115 1.27239 -0.17344 0.15869  0.01675  688 HOH A O    
1759 O  O    . HOH J .   ? 0.54831 0.84746 0.29469 -0.19339 -0.08040 -0.08622 689 HOH A O    
1760 O  O    . HOH J .   ? 0.95827 1.25463 1.18629 -0.05209 -0.20381 0.39374  690 HOH A O    
1761 O  O    . HOH J .   ? 0.97228 1.10807 1.03547 0.09431  0.03053  -0.28738 691 HOH A O    
1762 O  O    . HOH J .   ? 0.78502 0.87607 0.72060 0.31074  -0.19053 0.25403  692 HOH A O    
1763 O  O    . HOH J .   ? 0.97346 1.03028 0.72001 0.13144  -0.05215 0.15743  693 HOH A O    
1764 O  O    . HOH J .   ? 0.75273 1.10471 0.64065 0.02251  -0.11695 -0.13726 694 HOH A O    
1765 O  O    . HOH J .   ? 0.93925 1.28709 0.69058 0.25081  -0.36332 0.14356  695 HOH A O    
1766 O  O    . HOH J .   ? 0.93617 0.50906 0.47849 0.12632  0.08404  0.04116  696 HOH A O    
1767 O  O    . HOH J .   ? 0.90170 1.03373 0.63913 0.11089  -0.00985 0.15394  697 HOH A O    
1768 O  O    . HOH J .   ? 0.66122 0.70606 0.24346 -0.02124 -0.16899 -0.00397 698 HOH A O    
1769 O  O    . HOH J .   ? 0.95432 1.12760 0.67485 0.09515  0.03408  0.02798  699 HOH A O    
1770 O  O    . HOH J .   ? 0.95036 0.76650 0.89410 0.13379  0.11450  -0.09790 700 HOH A O    
1771 O  O    . HOH J .   ? 1.30259 1.19118 1.49651 -0.00040 0.22345  -0.00001 701 HOH A O    
1772 O  O    . HOH J .   ? 0.74910 1.06591 1.14946 -0.12634 0.02676  0.24518  702 HOH A O    
1773 O  O    . HOH J .   ? 0.89987 0.94589 1.44150 0.08391  0.08834  -0.02810 703 HOH A O    
1774 O  O    . HOH J .   ? 0.86555 1.34019 0.97700 -0.36787 0.00828  -0.18951 704 HOH A O    
1775 O  O    . HOH J .   ? 1.14464 0.91016 0.99402 0.10205  -0.04332 -0.21700 705 HOH A O    
1776 O  O    . HOH J .   ? 1.02753 0.60860 0.35988 0.07007  0.04203  -0.00956 706 HOH A O    
# 
