data_9ODS
# 
_entry.id   9ODS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ODS         pdb_00009ods 10.2210/pdb9ods/pdb 
WWPDB D_1000295399 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ODS 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              corey@coreyandpam.net 
_pdbx_contact_author.name_first         Corey 
_pdbx_contact_author.name_last          Strickland 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0006-6944-2968 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Strickland, C.' 1 ? 
'Rice, C.'       2 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Discovery and Characterization of PVTX-321 as a Potent and Orally Bioavailable Estrogen Receptor Degrader for ER+/HER2- Breast Cancer.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.5c00223 
_citation.pdbx_database_id_PubMed   40366756 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, G.'          1  ?                   
primary 'Havens, C.G.'    2  ?                   
primary 'Deng, Q.'        3  ?                   
primary 'Lowenstein, C.'  4  ?                   
primary 'Samanta, D.'     5  ?                   
primary 'Vidal, B.'       6  ?                   
primary 'Behshad, E.'     7  ?                   
primary 'Russell, M.'     8  ?                   
primary 'Orth, P.'        9  ?                   
primary 'Rice, C.T.'      10 ?                   
primary 'Nagilla, R.'     11 ?                   
primary 'Kirchhoff, P.'   12 ?                   
primary 'Chen, Z.'        13 ?                   
primary 'Rej, R.K.'       14 0000-0003-0904-9137 
primary 'Acharyya, R.K.'  15 0000-0002-1562-0216 
primary 'Wu, D.'          16 ?                   
primary 'Wang, S.'        17 0000-0002-8782-6950 
primary 'Zhang, W.'       18 ?                   
primary 'Wu, W.'          19 0000-0002-5979-9350 
primary 'Jolivette, L.'   20 ?                   
primary 'Strickland, C.'  21 ?                   
primary 'Sui, Z.'         22 ?                   
primary 'Mohammad, H.P.'  23 ?                   
primary 'Zhang, X.'       24 0009-0003-6990-6812 
primary 'Priestley, E.S.' 25 0000-0001-8390-1143 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protein cereblon'                                                                                         
12309.062 4  ? ? 'TBD domain' ? 
2 non-polymer syn "(1P)-1-[(4S)-8H-spiro[furo[2,3-c]imidazo[1,2-a]pyridine-7,4'-piperidin]-3-yl]pyrimidine-2,4(1H,3H)-dione" 
339.349   4  ? ? ?            ? 
3 non-polymer syn 'ZINC ION'                                                                                                 
65.409    4  ? ? ?            ? 
4 water       nat water                                                                                                      
18.015    31 ? ? ?            ? 
# 
_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       
;GPSTSLSCKQCQETEITTKNEIFSLSLSGPMAAYVNPHGYVHETLTVYKASNLNLIGRPSTEHSWFPGYAWTVAQCKICA
SHIGWKFTATKKDMSPQKFWGLTRSALLPTI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPSTSLSCKQCQETEITTKNEIFSLSLSGPMAAYVNPHGYVHETLTVYKASNLNLIGRPSTEHSWFPGYAWTVAQCKICA
SHIGWKFTATKKDMSPQKFWGLTRSALLPTI
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "(1P)-1-[(4S)-8H-spiro[furo[2,3-c]imidazo[1,2-a]pyridine-7,4'-piperidin]-3-yl]pyrimidine-2,4(1H,3H)-dione" A1CAW 
3 'ZINC ION'                                                                                                 ZN    
4 water                                                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   SER n 
1 4   THR n 
1 5   SER n 
1 6   LEU n 
1 7   SER n 
1 8   CYS n 
1 9   LYS n 
1 10  GLN n 
1 11  CYS n 
1 12  GLN n 
1 13  GLU n 
1 14  THR n 
1 15  GLU n 
1 16  ILE n 
1 17  THR n 
1 18  THR n 
1 19  LYS n 
1 20  ASN n 
1 21  GLU n 
1 22  ILE n 
1 23  PHE n 
1 24  SER n 
1 25  LEU n 
1 26  SER n 
1 27  LEU n 
1 28  SER n 
1 29  GLY n 
1 30  PRO n 
1 31  MET n 
1 32  ALA n 
1 33  ALA n 
1 34  TYR n 
1 35  VAL n 
1 36  ASN n 
1 37  PRO n 
1 38  HIS n 
1 39  GLY n 
1 40  TYR n 
1 41  VAL n 
1 42  HIS n 
1 43  GLU n 
1 44  THR n 
1 45  LEU n 
1 46  THR n 
1 47  VAL n 
1 48  TYR n 
1 49  LYS n 
1 50  ALA n 
1 51  SER n 
1 52  ASN n 
1 53  LEU n 
1 54  ASN n 
1 55  LEU n 
1 56  ILE n 
1 57  GLY n 
1 58  ARG n 
1 59  PRO n 
1 60  SER n 
1 61  THR n 
1 62  GLU n 
1 63  HIS n 
1 64  SER n 
1 65  TRP n 
1 66  PHE n 
1 67  PRO n 
1 68  GLY n 
1 69  TYR n 
1 70  ALA n 
1 71  TRP n 
1 72  THR n 
1 73  VAL n 
1 74  ALA n 
1 75  GLN n 
1 76  CYS n 
1 77  LYS n 
1 78  ILE n 
1 79  CYS n 
1 80  ALA n 
1 81  SER n 
1 82  HIS n 
1 83  ILE n 
1 84  GLY n 
1 85  TRP n 
1 86  LYS n 
1 87  PHE n 
1 88  THR n 
1 89  ALA n 
1 90  THR n 
1 91  LYS n 
1 92  LYS n 
1 93  ASP n 
1 94  MET n 
1 95  SER n 
1 96  PRO n 
1 97  GLN n 
1 98  LYS n 
1 99  PHE n 
1 100 TRP n 
1 101 GLY n 
1 102 LEU n 
1 103 THR n 
1 104 ARG n 
1 105 SER n 
1 106 ALA n 
1 107 LEU n 
1 108 LEU n 
1 109 PRO n 
1 110 THR n 
1 111 ILE 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                   111 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CRBN, AD-006' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1CAW non-polymer         . 
"(1P)-1-[(4S)-8H-spiro[furo[2,3-c]imidazo[1,2-a]pyridine-7,4'-piperidin]-3-yl]pyrimidine-2,4(1H,3H)-dione" ? 'C17 H17 N5 O3'  
339.349 
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 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   316 ?   ?   ?   A . n 
A 1 2   PRO 2   317 ?   ?   ?   A . n 
A 1 3   SER 3   318 ?   ?   ?   A . n 
A 1 4   THR 4   319 319 THR THR A . n 
A 1 5   SER 5   320 320 SER SER A . n 
A 1 6   LEU 6   321 321 LEU LEU A . n 
A 1 7   SER 7   322 322 SER SER A . n 
A 1 8   CYS 8   323 323 CYS CYS A . n 
A 1 9   LYS 9   324 324 LYS LYS A . n 
A 1 10  GLN 10  325 325 GLN GLN A . n 
A 1 11  CYS 11  326 326 CYS CYS A . n 
A 1 12  GLN 12  327 327 GLN GLN A . n 
A 1 13  GLU 13  328 328 GLU GLU A . n 
A 1 14  THR 14  329 329 THR THR A . n 
A 1 15  GLU 15  330 330 GLU GLU A . n 
A 1 16  ILE 16  331 331 ILE ILE A . n 
A 1 17  THR 17  332 332 THR THR A . n 
A 1 18  THR 18  333 333 THR THR A . n 
A 1 19  LYS 19  334 334 LYS LYS A . n 
A 1 20  ASN 20  335 335 ASN ASN A . n 
A 1 21  GLU 21  336 336 GLU GLU A . n 
A 1 22  ILE 22  337 337 ILE ILE A . n 
A 1 23  PHE 23  338 338 PHE PHE A . n 
A 1 24  SER 24  339 339 SER SER A . n 
A 1 25  LEU 25  340 340 LEU LEU A . n 
A 1 26  SER 26  341 341 SER SER A . n 
A 1 27  LEU 27  342 342 LEU LEU A . n 
A 1 28  SER 28  343 343 SER SER A . n 
A 1 29  GLY 29  344 344 GLY GLY A . n 
A 1 30  PRO 30  345 345 PRO PRO A . n 
A 1 31  MET 31  346 346 MET MET A . n 
A 1 32  ALA 32  347 347 ALA ALA A . n 
A 1 33  ALA 33  348 348 ALA ALA A . n 
A 1 34  TYR 34  349 349 TYR TYR A . n 
A 1 35  VAL 35  350 350 VAL VAL A . n 
A 1 36  ASN 36  351 351 ASN ASN A . n 
A 1 37  PRO 37  352 352 PRO PRO A . n 
A 1 38  HIS 38  353 353 HIS HIS A . n 
A 1 39  GLY 39  354 354 GLY GLY A . n 
A 1 40  TYR 40  355 355 TYR TYR A . n 
A 1 41  VAL 41  356 356 VAL VAL A . n 
A 1 42  HIS 42  357 357 HIS HIS A . n 
A 1 43  GLU 43  358 358 GLU GLU A . n 
A 1 44  THR 44  359 359 THR THR A . n 
A 1 45  LEU 45  360 360 LEU LEU A . n 
A 1 46  THR 46  361 361 THR THR A . n 
A 1 47  VAL 47  362 362 VAL VAL A . n 
A 1 48  TYR 48  363 363 TYR TYR A . n 
A 1 49  LYS 49  364 364 LYS LYS A . n 
A 1 50  ALA 50  365 365 ALA ALA A . n 
A 1 51  SER 51  366 366 SER SER A . n 
A 1 52  ASN 52  367 367 ASN ASN A . n 
A 1 53  LEU 53  368 368 LEU LEU A . n 
A 1 54  ASN 54  369 369 ASN ASN A . n 
A 1 55  LEU 55  370 370 LEU LEU A . n 
A 1 56  ILE 56  371 371 ILE ILE A . n 
A 1 57  GLY 57  372 372 GLY GLY A . n 
A 1 58  ARG 58  373 373 ARG ARG A . n 
A 1 59  PRO 59  374 374 PRO PRO A . n 
A 1 60  SER 60  375 375 SER SER A . n 
A 1 61  THR 61  376 376 THR THR A . n 
A 1 62  GLU 62  377 377 GLU GLU A . n 
A 1 63  HIS 63  378 378 HIS HIS A . n 
A 1 64  SER 64  379 379 SER SER A . n 
A 1 65  TRP 65  380 380 TRP TRP A . n 
A 1 66  PHE 66  381 381 PHE PHE A . n 
A 1 67  PRO 67  382 382 PRO PRO A . n 
A 1 68  GLY 68  383 383 GLY GLY A . n 
A 1 69  TYR 69  384 384 TYR TYR A . n 
A 1 70  ALA 70  385 385 ALA ALA A . n 
A 1 71  TRP 71  386 386 TRP TRP A . n 
A 1 72  THR 72  387 387 THR THR A . n 
A 1 73  VAL 73  388 388 VAL VAL A . n 
A 1 74  ALA 74  389 389 ALA ALA A . n 
A 1 75  GLN 75  390 390 GLN GLN A . n 
A 1 76  CYS 76  391 391 CYS CYS A . n 
A 1 77  LYS 77  392 392 LYS LYS A . n 
A 1 78  ILE 78  393 393 ILE ILE A . n 
A 1 79  CYS 79  394 394 CYS CYS A . n 
A 1 80  ALA 80  395 395 ALA ALA A . n 
A 1 81  SER 81  396 396 SER SER A . n 
A 1 82  HIS 82  397 397 HIS HIS A . n 
A 1 83  ILE 83  398 398 ILE ILE A . n 
A 1 84  GLY 84  399 399 GLY GLY A . n 
A 1 85  TRP 85  400 400 TRP TRP A . n 
A 1 86  LYS 86  401 401 LYS LYS A . n 
A 1 87  PHE 87  402 402 PHE PHE A . n 
A 1 88  THR 88  403 403 THR THR A . n 
A 1 89  ALA 89  404 404 ALA ALA A . n 
A 1 90  THR 90  405 405 THR THR A . n 
A 1 91  LYS 91  406 406 LYS LYS A . n 
A 1 92  LYS 92  407 407 LYS LYS A . n 
A 1 93  ASP 93  408 408 ASP ASP A . n 
A 1 94  MET 94  409 409 MET MET A . n 
A 1 95  SER 95  410 410 SER SER A . n 
A 1 96  PRO 96  411 411 PRO PRO A . n 
A 1 97  GLN 97  412 412 GLN GLN A . n 
A 1 98  LYS 98  413 413 LYS LYS A . n 
A 1 99  PHE 99  414 414 PHE PHE A . n 
A 1 100 TRP 100 415 415 TRP TRP A . n 
A 1 101 GLY 101 416 416 GLY GLY A . n 
A 1 102 LEU 102 417 417 LEU LEU A . n 
A 1 103 THR 103 418 418 THR THR A . n 
A 1 104 ARG 104 419 419 ARG ARG A . n 
A 1 105 SER 105 420 420 SER SER A . n 
A 1 106 ALA 106 421 421 ALA ALA A . n 
A 1 107 LEU 107 422 422 LEU LEU A . n 
A 1 108 LEU 108 423 423 LEU LEU A . n 
A 1 109 PRO 109 424 424 PRO PRO A . n 
A 1 110 THR 110 425 425 THR THR A . n 
A 1 111 ILE 111 426 426 ILE ILE A . n 
B 1 1   GLY 1   316 ?   ?   ?   B . n 
B 1 2   PRO 2   317 ?   ?   ?   B . n 
B 1 3   SER 3   318 318 SER SER B . n 
B 1 4   THR 4   319 319 THR THR B . n 
B 1 5   SER 5   320 320 SER SER B . n 
B 1 6   LEU 6   321 321 LEU LEU B . n 
B 1 7   SER 7   322 322 SER SER B . n 
B 1 8   CYS 8   323 323 CYS CYS B . n 
B 1 9   LYS 9   324 324 LYS LYS B . n 
B 1 10  GLN 10  325 325 GLN GLN B . n 
B 1 11  CYS 11  326 326 CYS CYS B . n 
B 1 12  GLN 12  327 327 GLN GLN B . n 
B 1 13  GLU 13  328 328 GLU GLU B . n 
B 1 14  THR 14  329 329 THR THR B . n 
B 1 15  GLU 15  330 330 GLU GLU B . n 
B 1 16  ILE 16  331 331 ILE ILE B . n 
B 1 17  THR 17  332 332 THR THR B . n 
B 1 18  THR 18  333 333 THR THR B . n 
B 1 19  LYS 19  334 334 LYS LYS B . n 
B 1 20  ASN 20  335 335 ASN ASN B . n 
B 1 21  GLU 21  336 336 GLU GLU B . n 
B 1 22  ILE 22  337 337 ILE ILE B . n 
B 1 23  PHE 23  338 338 PHE PHE B . n 
B 1 24  SER 24  339 339 SER SER B . n 
B 1 25  LEU 25  340 340 LEU LEU B . n 
B 1 26  SER 26  341 341 SER SER B . n 
B 1 27  LEU 27  342 342 LEU LEU B . n 
B 1 28  SER 28  343 343 SER SER B . n 
B 1 29  GLY 29  344 344 GLY GLY B . n 
B 1 30  PRO 30  345 345 PRO PRO B . n 
B 1 31  MET 31  346 346 MET MET B . n 
B 1 32  ALA 32  347 347 ALA ALA B . n 
B 1 33  ALA 33  348 348 ALA ALA B . n 
B 1 34  TYR 34  349 349 TYR TYR B . n 
B 1 35  VAL 35  350 350 VAL VAL B . n 
B 1 36  ASN 36  351 351 ASN ASN B . n 
B 1 37  PRO 37  352 352 PRO PRO B . n 
B 1 38  HIS 38  353 353 HIS HIS B . n 
B 1 39  GLY 39  354 354 GLY GLY B . n 
B 1 40  TYR 40  355 355 TYR TYR B . n 
B 1 41  VAL 41  356 356 VAL VAL B . n 
B 1 42  HIS 42  357 357 HIS HIS B . n 
B 1 43  GLU 43  358 358 GLU GLU B . n 
B 1 44  THR 44  359 359 THR THR B . n 
B 1 45  LEU 45  360 360 LEU LEU B . n 
B 1 46  THR 46  361 361 THR THR B . n 
B 1 47  VAL 47  362 362 VAL VAL B . n 
B 1 48  TYR 48  363 363 TYR TYR B . n 
B 1 49  LYS 49  364 364 LYS LYS B . n 
B 1 50  ALA 50  365 365 ALA ALA B . n 
B 1 51  SER 51  366 366 SER SER B . n 
B 1 52  ASN 52  367 367 ASN ASN B . n 
B 1 53  LEU 53  368 368 LEU LEU B . n 
B 1 54  ASN 54  369 369 ASN ASN B . n 
B 1 55  LEU 55  370 370 LEU LEU B . n 
B 1 56  ILE 56  371 371 ILE ILE B . n 
B 1 57  GLY 57  372 372 GLY GLY B . n 
B 1 58  ARG 58  373 373 ARG ARG B . n 
B 1 59  PRO 59  374 374 PRO PRO B . n 
B 1 60  SER 60  375 375 SER SER B . n 
B 1 61  THR 61  376 376 THR THR B . n 
B 1 62  GLU 62  377 377 GLU GLU B . n 
B 1 63  HIS 63  378 378 HIS HIS B . n 
B 1 64  SER 64  379 379 SER SER B . n 
B 1 65  TRP 65  380 380 TRP TRP B . n 
B 1 66  PHE 66  381 381 PHE PHE B . n 
B 1 67  PRO 67  382 382 PRO PRO B . n 
B 1 68  GLY 68  383 383 GLY GLY B . n 
B 1 69  TYR 69  384 384 TYR TYR B . n 
B 1 70  ALA 70  385 385 ALA ALA B . n 
B 1 71  TRP 71  386 386 TRP TRP B . n 
B 1 72  THR 72  387 387 THR THR B . n 
B 1 73  VAL 73  388 388 VAL VAL B . n 
B 1 74  ALA 74  389 389 ALA ALA B . n 
B 1 75  GLN 75  390 390 GLN GLN B . n 
B 1 76  CYS 76  391 391 CYS CYS B . n 
B 1 77  LYS 77  392 392 LYS LYS B . n 
B 1 78  ILE 78  393 393 ILE ILE B . n 
B 1 79  CYS 79  394 394 CYS CYS B . n 
B 1 80  ALA 80  395 395 ALA ALA B . n 
B 1 81  SER 81  396 396 SER SER B . n 
B 1 82  HIS 82  397 397 HIS HIS B . n 
B 1 83  ILE 83  398 398 ILE ILE B . n 
B 1 84  GLY 84  399 399 GLY GLY B . n 
B 1 85  TRP 85  400 400 TRP TRP B . n 
B 1 86  LYS 86  401 401 LYS LYS B . n 
B 1 87  PHE 87  402 402 PHE PHE B . n 
B 1 88  THR 88  403 403 THR THR B . n 
B 1 89  ALA 89  404 404 ALA ALA B . n 
B 1 90  THR 90  405 405 THR THR B . n 
B 1 91  LYS 91  406 406 LYS LYS B . n 
B 1 92  LYS 92  407 407 LYS LYS B . n 
B 1 93  ASP 93  408 408 ASP ASP B . n 
B 1 94  MET 94  409 409 MET MET B . n 
B 1 95  SER 95  410 410 SER SER B . n 
B 1 96  PRO 96  411 411 PRO PRO B . n 
B 1 97  GLN 97  412 412 GLN GLN B . n 
B 1 98  LYS 98  413 413 LYS LYS B . n 
B 1 99  PHE 99  414 414 PHE PHE B . n 
B 1 100 TRP 100 415 415 TRP TRP B . n 
B 1 101 GLY 101 416 416 GLY GLY B . n 
B 1 102 LEU 102 417 417 LEU LEU B . n 
B 1 103 THR 103 418 418 THR THR B . n 
B 1 104 ARG 104 419 419 ARG ARG B . n 
B 1 105 SER 105 420 420 SER SER B . n 
B 1 106 ALA 106 421 421 ALA ALA B . n 
B 1 107 LEU 107 422 422 LEU LEU B . n 
B 1 108 LEU 108 423 423 LEU LEU B . n 
B 1 109 PRO 109 424 424 PRO PRO B . n 
B 1 110 THR 110 425 425 THR THR B . n 
B 1 111 ILE 111 426 ?   ?   ?   B . n 
C 1 1   GLY 1   316 ?   ?   ?   C . n 
C 1 2   PRO 2   317 ?   ?   ?   C . n 
C 1 3   SER 3   318 318 SER SER C . n 
C 1 4   THR 4   319 319 THR THR C . n 
C 1 5   SER 5   320 320 SER SER C . n 
C 1 6   LEU 6   321 321 LEU LEU C . n 
C 1 7   SER 7   322 322 SER SER C . n 
C 1 8   CYS 8   323 323 CYS CYS C . n 
C 1 9   LYS 9   324 324 LYS LYS C . n 
C 1 10  GLN 10  325 325 GLN GLN C . n 
C 1 11  CYS 11  326 326 CYS CYS C . n 
C 1 12  GLN 12  327 327 GLN GLN C . n 
C 1 13  GLU 13  328 328 GLU GLU C . n 
C 1 14  THR 14  329 329 THR THR C . n 
C 1 15  GLU 15  330 330 GLU GLU C . n 
C 1 16  ILE 16  331 331 ILE ILE C . n 
C 1 17  THR 17  332 332 THR THR C . n 
C 1 18  THR 18  333 333 THR THR C . n 
C 1 19  LYS 19  334 334 LYS LYS C . n 
C 1 20  ASN 20  335 335 ASN ASN C . n 
C 1 21  GLU 21  336 336 GLU GLU C . n 
C 1 22  ILE 22  337 337 ILE ILE C . n 
C 1 23  PHE 23  338 338 PHE PHE C . n 
C 1 24  SER 24  339 339 SER SER C . n 
C 1 25  LEU 25  340 340 LEU LEU C . n 
C 1 26  SER 26  341 341 SER SER C . n 
C 1 27  LEU 27  342 342 LEU LEU C . n 
C 1 28  SER 28  343 343 SER SER C . n 
C 1 29  GLY 29  344 344 GLY GLY C . n 
C 1 30  PRO 30  345 345 PRO PRO C . n 
C 1 31  MET 31  346 346 MET MET C . n 
C 1 32  ALA 32  347 347 ALA ALA C . n 
C 1 33  ALA 33  348 348 ALA ALA C . n 
C 1 34  TYR 34  349 349 TYR TYR C . n 
C 1 35  VAL 35  350 350 VAL VAL C . n 
C 1 36  ASN 36  351 351 ASN ASN C . n 
C 1 37  PRO 37  352 352 PRO PRO C . n 
C 1 38  HIS 38  353 353 HIS HIS C . n 
C 1 39  GLY 39  354 354 GLY GLY C . n 
C 1 40  TYR 40  355 355 TYR TYR C . n 
C 1 41  VAL 41  356 356 VAL VAL C . n 
C 1 42  HIS 42  357 357 HIS HIS C . n 
C 1 43  GLU 43  358 358 GLU GLU C . n 
C 1 44  THR 44  359 359 THR THR C . n 
C 1 45  LEU 45  360 360 LEU LEU C . n 
C 1 46  THR 46  361 361 THR THR C . n 
C 1 47  VAL 47  362 362 VAL VAL C . n 
C 1 48  TYR 48  363 363 TYR TYR C . n 
C 1 49  LYS 49  364 364 LYS LYS C . n 
C 1 50  ALA 50  365 365 ALA ALA C . n 
C 1 51  SER 51  366 366 SER SER C . n 
C 1 52  ASN 52  367 367 ASN ASN C . n 
C 1 53  LEU 53  368 368 LEU LEU C . n 
C 1 54  ASN 54  369 369 ASN ASN C . n 
C 1 55  LEU 55  370 370 LEU LEU C . n 
C 1 56  ILE 56  371 371 ILE ILE C . n 
C 1 57  GLY 57  372 372 GLY GLY C . n 
C 1 58  ARG 58  373 373 ARG ARG C . n 
C 1 59  PRO 59  374 374 PRO PRO C . n 
C 1 60  SER 60  375 375 SER SER C . n 
C 1 61  THR 61  376 376 THR THR C . n 
C 1 62  GLU 62  377 377 GLU GLU C . n 
C 1 63  HIS 63  378 378 HIS HIS C . n 
C 1 64  SER 64  379 379 SER SER C . n 
C 1 65  TRP 65  380 380 TRP TRP C . n 
C 1 66  PHE 66  381 381 PHE PHE C . n 
C 1 67  PRO 67  382 382 PRO PRO C . n 
C 1 68  GLY 68  383 383 GLY GLY C . n 
C 1 69  TYR 69  384 384 TYR TYR C . n 
C 1 70  ALA 70  385 385 ALA ALA C . n 
C 1 71  TRP 71  386 386 TRP TRP C . n 
C 1 72  THR 72  387 387 THR THR C . n 
C 1 73  VAL 73  388 388 VAL VAL C . n 
C 1 74  ALA 74  389 389 ALA ALA C . n 
C 1 75  GLN 75  390 390 GLN GLN C . n 
C 1 76  CYS 76  391 391 CYS CYS C . n 
C 1 77  LYS 77  392 392 LYS LYS C . n 
C 1 78  ILE 78  393 393 ILE ILE C . n 
C 1 79  CYS 79  394 394 CYS CYS C . n 
C 1 80  ALA 80  395 395 ALA ALA C . n 
C 1 81  SER 81  396 396 SER SER C . n 
C 1 82  HIS 82  397 397 HIS HIS C . n 
C 1 83  ILE 83  398 398 ILE ILE C . n 
C 1 84  GLY 84  399 399 GLY GLY C . n 
C 1 85  TRP 85  400 400 TRP TRP C . n 
C 1 86  LYS 86  401 401 LYS LYS C . n 
C 1 87  PHE 87  402 402 PHE PHE C . n 
C 1 88  THR 88  403 403 THR THR C . n 
C 1 89  ALA 89  404 404 ALA ALA C . n 
C 1 90  THR 90  405 405 THR THR C . n 
C 1 91  LYS 91  406 406 LYS LYS C . n 
C 1 92  LYS 92  407 407 LYS LYS C . n 
C 1 93  ASP 93  408 408 ASP ASP C . n 
C 1 94  MET 94  409 409 MET MET C . n 
C 1 95  SER 95  410 410 SER SER C . n 
C 1 96  PRO 96  411 411 PRO PRO C . n 
C 1 97  GLN 97  412 412 GLN GLN C . n 
C 1 98  LYS 98  413 413 LYS LYS C . n 
C 1 99  PHE 99  414 414 PHE PHE C . n 
C 1 100 TRP 100 415 415 TRP TRP C . n 
C 1 101 GLY 101 416 416 GLY GLY C . n 
C 1 102 LEU 102 417 417 LEU LEU C . n 
C 1 103 THR 103 418 418 THR THR C . n 
C 1 104 ARG 104 419 419 ARG ARG C . n 
C 1 105 SER 105 420 420 SER SER C . n 
C 1 106 ALA 106 421 421 ALA ALA C . n 
C 1 107 LEU 107 422 422 LEU LEU C . n 
C 1 108 LEU 108 423 423 LEU LEU C . n 
C 1 109 PRO 109 424 424 PRO PRO C . n 
C 1 110 THR 110 425 425 THR THR C . n 
C 1 111 ILE 111 426 426 ILE ILE C . n 
D 1 1   GLY 1   316 ?   ?   ?   D . n 
D 1 2   PRO 2   317 ?   ?   ?   D . n 
D 1 3   SER 3   318 318 SER SER D . n 
D 1 4   THR 4   319 319 THR THR D . n 
D 1 5   SER 5   320 320 SER SER D . n 
D 1 6   LEU 6   321 321 LEU LEU D . n 
D 1 7   SER 7   322 322 SER SER D . n 
D 1 8   CYS 8   323 323 CYS CYS D . n 
D 1 9   LYS 9   324 324 LYS LYS D . n 
D 1 10  GLN 10  325 325 GLN GLN D . n 
D 1 11  CYS 11  326 326 CYS CYS D . n 
D 1 12  GLN 12  327 327 GLN GLN D . n 
D 1 13  GLU 13  328 328 GLU GLU D . n 
D 1 14  THR 14  329 329 THR THR D . n 
D 1 15  GLU 15  330 330 GLU GLU D . n 
D 1 16  ILE 16  331 331 ILE ILE D . n 
D 1 17  THR 17  332 332 THR THR D . n 
D 1 18  THR 18  333 333 THR THR D . n 
D 1 19  LYS 19  334 334 LYS LYS D . n 
D 1 20  ASN 20  335 335 ASN ASN D . n 
D 1 21  GLU 21  336 336 GLU GLU D . n 
D 1 22  ILE 22  337 337 ILE ILE D . n 
D 1 23  PHE 23  338 338 PHE PHE D . n 
D 1 24  SER 24  339 339 SER SER D . n 
D 1 25  LEU 25  340 340 LEU LEU D . n 
D 1 26  SER 26  341 341 SER SER D . n 
D 1 27  LEU 27  342 342 LEU LEU D . n 
D 1 28  SER 28  343 343 SER SER D . n 
D 1 29  GLY 29  344 344 GLY GLY D . n 
D 1 30  PRO 30  345 345 PRO PRO D . n 
D 1 31  MET 31  346 346 MET MET D . n 
D 1 32  ALA 32  347 347 ALA ALA D . n 
D 1 33  ALA 33  348 348 ALA ALA D . n 
D 1 34  TYR 34  349 349 TYR TYR D . n 
D 1 35  VAL 35  350 350 VAL VAL D . n 
D 1 36  ASN 36  351 351 ASN ASN D . n 
D 1 37  PRO 37  352 352 PRO PRO D . n 
D 1 38  HIS 38  353 353 HIS HIS D . n 
D 1 39  GLY 39  354 354 GLY GLY D . n 
D 1 40  TYR 40  355 355 TYR TYR D . n 
D 1 41  VAL 41  356 356 VAL VAL D . n 
D 1 42  HIS 42  357 357 HIS HIS D . n 
D 1 43  GLU 43  358 358 GLU GLU D . n 
D 1 44  THR 44  359 359 THR THR D . n 
D 1 45  LEU 45  360 360 LEU LEU D . n 
D 1 46  THR 46  361 361 THR THR D . n 
D 1 47  VAL 47  362 362 VAL VAL D . n 
D 1 48  TYR 48  363 363 TYR TYR D . n 
D 1 49  LYS 49  364 364 LYS LYS D . n 
D 1 50  ALA 50  365 365 ALA ALA D . n 
D 1 51  SER 51  366 366 SER SER D . n 
D 1 52  ASN 52  367 367 ASN ASN D . n 
D 1 53  LEU 53  368 368 LEU LEU D . n 
D 1 54  ASN 54  369 369 ASN ASN D . n 
D 1 55  LEU 55  370 370 LEU LEU D . n 
D 1 56  ILE 56  371 371 ILE ILE D . n 
D 1 57  GLY 57  372 372 GLY GLY D . n 
D 1 58  ARG 58  373 373 ARG ARG D . n 
D 1 59  PRO 59  374 374 PRO PRO D . n 
D 1 60  SER 60  375 375 SER SER D . n 
D 1 61  THR 61  376 376 THR THR D . n 
D 1 62  GLU 62  377 377 GLU GLU D . n 
D 1 63  HIS 63  378 378 HIS HIS D . n 
D 1 64  SER 64  379 379 SER SER D . n 
D 1 65  TRP 65  380 380 TRP TRP D . n 
D 1 66  PHE 66  381 381 PHE PHE D . n 
D 1 67  PRO 67  382 382 PRO PRO D . n 
D 1 68  GLY 68  383 383 GLY GLY D . n 
D 1 69  TYR 69  384 384 TYR TYR D . n 
D 1 70  ALA 70  385 385 ALA ALA D . n 
D 1 71  TRP 71  386 386 TRP TRP D . n 
D 1 72  THR 72  387 387 THR THR D . n 
D 1 73  VAL 73  388 388 VAL VAL D . n 
D 1 74  ALA 74  389 389 ALA ALA D . n 
D 1 75  GLN 75  390 390 GLN GLN D . n 
D 1 76  CYS 76  391 391 CYS CYS D . n 
D 1 77  LYS 77  392 392 LYS LYS D . n 
D 1 78  ILE 78  393 393 ILE ILE D . n 
D 1 79  CYS 79  394 394 CYS CYS D . n 
D 1 80  ALA 80  395 395 ALA ALA D . n 
D 1 81  SER 81  396 396 SER SER D . n 
D 1 82  HIS 82  397 397 HIS HIS D . n 
D 1 83  ILE 83  398 398 ILE ILE D . n 
D 1 84  GLY 84  399 399 GLY GLY D . n 
D 1 85  TRP 85  400 400 TRP TRP D . n 
D 1 86  LYS 86  401 401 LYS LYS D . n 
D 1 87  PHE 87  402 402 PHE PHE D . n 
D 1 88  THR 88  403 403 THR THR D . n 
D 1 89  ALA 89  404 404 ALA ALA D . n 
D 1 90  THR 90  405 405 THR THR D . n 
D 1 91  LYS 91  406 406 LYS LYS D . n 
D 1 92  LYS 92  407 407 LYS LYS D . n 
D 1 93  ASP 93  408 408 ASP ASP D . n 
D 1 94  MET 94  409 409 MET MET D . n 
D 1 95  SER 95  410 410 SER SER D . n 
D 1 96  PRO 96  411 411 PRO PRO D . n 
D 1 97  GLN 97  412 412 GLN GLN D . n 
D 1 98  LYS 98  413 413 LYS LYS D . n 
D 1 99  PHE 99  414 414 PHE PHE D . n 
D 1 100 TRP 100 415 415 TRP TRP D . n 
D 1 101 GLY 101 416 416 GLY GLY D . n 
D 1 102 LEU 102 417 417 LEU LEU D . n 
D 1 103 THR 103 418 418 THR THR D . n 
D 1 104 ARG 104 419 419 ARG ARG D . n 
D 1 105 SER 105 420 420 SER SER D . n 
D 1 106 ALA 106 421 421 ALA ALA D . n 
D 1 107 LEU 107 422 422 LEU LEU D . n 
D 1 108 LEU 108 423 423 LEU LEU D . n 
D 1 109 PRO 109 424 424 PRO PRO D . n 
D 1 110 THR 110 425 425 THR THR D . n 
D 1 111 ILE 111 426 426 ILE ILE D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1CAW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1CAW 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
E 2 A1CAW 1  501 1  A1CAW UNL A . 
F 3 ZN    1  502 1  ZN    ZN  A . 
G 2 A1CAW 1  501 1  A1CAW UNL B . 
H 3 ZN    1  502 2  ZN    ZN  B . 
I 2 A1CAW 1  501 1  A1CAW UNL C . 
J 3 ZN    1  502 3  ZN    ZN  C . 
K 2 A1CAW 1  501 1  A1CAW UNL D . 
L 3 ZN    1  502 4  ZN    ZN  D . 
M 4 HOH   1  601 16 HOH   HOH A . 
M 4 HOH   2  602 8  HOH   HOH A . 
M 4 HOH   3  603 11 HOH   HOH A . 
M 4 HOH   4  604 6  HOH   HOH A . 
M 4 HOH   5  605 17 HOH   HOH A . 
M 4 HOH   6  606 20 HOH   HOH A . 
M 4 HOH   7  607 7  HOH   HOH A . 
M 4 HOH   8  608 10 HOH   HOH A . 
N 4 HOH   1  601 21 HOH   HOH B . 
O 4 HOH   1  601 3  HOH   HOH C . 
O 4 HOH   2  602 14 HOH   HOH C . 
O 4 HOH   3  603 4  HOH   HOH C . 
O 4 HOH   4  604 30 HOH   HOH C . 
O 4 HOH   5  605 1  HOH   HOH C . 
O 4 HOH   6  606 23 HOH   HOH C . 
O 4 HOH   7  607 13 HOH   HOH C . 
O 4 HOH   8  608 15 HOH   HOH C . 
O 4 HOH   9  609 19 HOH   HOH C . 
P 4 HOH   1  601 9  HOH   HOH D . 
P 4 HOH   2  602 28 HOH   HOH D . 
P 4 HOH   3  603 29 HOH   HOH D . 
P 4 HOH   4  604 5  HOH   HOH D . 
P 4 HOH   5  605 31 HOH   HOH D . 
P 4 HOH   6  606 24 HOH   HOH D . 
P 4 HOH   7  607 22 HOH   HOH D . 
P 4 HOH   8  608 2  HOH   HOH D . 
P 4 HOH   9  609 26 HOH   HOH D . 
P 4 HOH   10 610 27 HOH   HOH D . 
P 4 HOH   11 611 25 HOH   HOH D . 
P 4 HOH   12 612 12 HOH   HOH D . 
P 4 HOH   13 613 18 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B LYS 407 ? CG ? B LYS 92 CG 
2 1 Y 1 B LYS 407 ? CD ? B LYS 92 CD 
3 1 Y 1 B LYS 407 ? CE ? B LYS 92 CE 
4 1 Y 1 B LYS 407 ? NZ ? B LYS 92 NZ 
5 1 Y 1 D LYS 407 ? CG ? D LYS 92 CG 
6 1 Y 1 D LYS 407 ? CD ? D LYS 92 CD 
7 1 Y 1 D LYS 407 ? CE ? D LYS 92 CE 
8 1 Y 1 D LYS 407 ? NZ ? D LYS 92 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0430 ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        ? 3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .        ? 4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? FFT         ? ? ? .        ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   114.42 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ODS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.559 
_cell.length_a_esd                 ? 
_cell.length_b                     86.279 
_cell.length_b_esd                 ? 
_cell.length_c                     90.972 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9ODS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9ODS 
_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             3.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.38 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2M tri-Sodium citrate
18 % w/v PEG 3,350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_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                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ODS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.61 
_reflns.d_resolution_low                               60.36 
_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                                     12509 
_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                           62.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.61 
_reflns_shell.d_res_low                                     2.85 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3353 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.293 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            1.22 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.28 
_refine.aniso_B[2][2]                            -0.91 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.40 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               65.140 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.928 
_refine.correlation_coeff_Fo_to_Fc_free          0.903 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9ODS 
_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                            2.61 
_refine.ls_d_res_low                             60.36 
_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                     11895 
_refine.ls_number_reflns_R_free                  614 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    62.52 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21642 
_refine.ls_R_factor_R_free                       0.24802 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21484 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.419 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             13.896 
_refine.overall_SU_ML                            0.279 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.61 
_refine_hist.d_res_low                        60.36 
_refine_hist.number_atoms_solvent             31 
_refine_hist.number_atoms_total               3528 
_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        3393 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         104 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  0.012  3609 ? r_bond_refined_d       ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3265 ? r_bond_other_d         ? ? ? 
'X-RAY DIFFRACTION' ? 1.020  1.822  4935 ? r_angle_refined_deg    ? ? ? 
'X-RAY DIFFRACTION' ? 0.336  1.738  7575 ? r_angle_other_deg      ? ? ? 
'X-RAY DIFFRACTION' ? 7.240  5.000  430  ? r_dihedral_angle_1_deg ? ? ? 
'X-RAY DIFFRACTION' ? 11.962 5.000  48   ? r_dihedral_angle_2_deg ? ? ? 
'X-RAY DIFFRACTION' ? 13.696 10.000 569  ? r_dihedral_angle_3_deg ? ? ? 
'X-RAY DIFFRACTION' ? 0.047  0.200  537  ? r_chiral_restr         ? ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  4086 ? r_gen_planes_refined   ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  786  ? r_gen_planes_other     ? ? ? 
'X-RAY DIFFRACTION' ? 1.658  6.675  1732 ? r_mcbond_it            ? ? ? 
'X-RAY DIFFRACTION' ? 1.658  6.675  1732 ? r_mcbond_other         ? ? ? 
'X-RAY DIFFRACTION' ? 3.015  11.985 2158 ? r_mcangle_it           ? ? ? 
'X-RAY DIFFRACTION' ? 3.015  11.987 2159 ? r_mcangle_other        ? ? ? 
'X-RAY DIFFRACTION' ? 1.351  6.708  1877 ? r_scbond_it            ? ? ? 
'X-RAY DIFFRACTION' ? 1.351  6.708  1877 ? r_scbond_other         ? ? ? 
'X-RAY DIFFRACTION' ? 2.511  12.274 2778 ? r_scangle_other        ? ? ? 
'X-RAY DIFFRACTION' ? 5.067  62.01  3896 ? r_long_range_B_refined ? ? ? 
'X-RAY DIFFRACTION' ? 5.066  62.01  3897 ? r_long_range_B_other   ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          2.61 
_refine_ls_shell.d_res_low                           2.674 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                3 
_refine_ls_shell.number_reflns_R_work                54 
_refine_ls_shell.percent_reflns_obs                  3.94 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.357 
_refine_ls_shell.redundancy_reflns_all               ? 
_refine_ls_shell.redundancy_reflns_obs               ? 
_refine_ls_shell.wR_factor_all                       ? 
_refine_ls_shell.wR_factor_obs                       ? 
_refine_ls_shell.wR_factor_R_free                    ? 
_refine_ls_shell.wR_factor_R_work                    ? 
_refine_ls_shell.pdbx_R_complete                     ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      ? 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.R_factor_R_free                     0.307 
# 
_struct.entry_id                     9ODS 
_struct.title                        'Structure of CRBN TBD bound to compound C3' 
_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        9ODS 
_struct_keywords.text            'Protein degrader, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 2 ? 
J N N 3 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CRBN_HUMAN 
_struct_ref.pdbx_db_accession          Q96SW2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHI
GWKFTATKKDMSPQKFWGLTRSALLPTI
;
_struct_ref.pdbx_align_begin           319 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9ODS A 4 ? 111 ? Q96SW2 319 ? 426 ? 319 426 
2 1 9ODS B 4 ? 111 ? Q96SW2 319 ? 426 ? 319 426 
3 1 9ODS C 4 ? 111 ? Q96SW2 319 ? 426 ? 319 426 
4 1 9ODS D 4 ? 111 ? Q96SW2 319 ? 426 ? 319 426 
# 
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 9ODS GLY A 1  ? UNP Q96SW2 ?   ?   'expression tag' 316 1  
1 9ODS PRO A 2  ? UNP Q96SW2 ?   ?   'expression tag' 317 2  
1 9ODS SER A 3  ? UNP Q96SW2 ?   ?   'expression tag' 318 3  
1 9ODS SER A 7  ? UNP Q96SW2 CYS 322 conflict         322 4  
1 9ODS SER A 28 ? UNP Q96SW2 CYS 343 conflict         343 5  
1 9ODS SER A 51 ? UNP Q96SW2 CYS 366 conflict         366 6  
2 9ODS GLY B 1  ? UNP Q96SW2 ?   ?   'expression tag' 316 7  
2 9ODS PRO B 2  ? UNP Q96SW2 ?   ?   'expression tag' 317 8  
2 9ODS SER B 3  ? UNP Q96SW2 ?   ?   'expression tag' 318 9  
2 9ODS SER B 7  ? UNP Q96SW2 CYS 322 conflict         322 10 
2 9ODS SER B 28 ? UNP Q96SW2 CYS 343 conflict         343 11 
2 9ODS SER B 51 ? UNP Q96SW2 CYS 366 conflict         366 12 
3 9ODS GLY C 1  ? UNP Q96SW2 ?   ?   'expression tag' 316 13 
3 9ODS PRO C 2  ? UNP Q96SW2 ?   ?   'expression tag' 317 14 
3 9ODS SER C 3  ? UNP Q96SW2 ?   ?   'expression tag' 318 15 
3 9ODS SER C 7  ? UNP Q96SW2 CYS 322 conflict         322 16 
3 9ODS SER C 28 ? UNP Q96SW2 CYS 343 conflict         343 17 
3 9ODS SER C 51 ? UNP Q96SW2 CYS 366 conflict         366 18 
4 9ODS GLY D 1  ? UNP Q96SW2 ?   ?   'expression tag' 316 19 
4 9ODS PRO D 2  ? UNP Q96SW2 ?   ?   'expression tag' 317 20 
4 9ODS SER D 3  ? UNP Q96SW2 ?   ?   'expression tag' 318 21 
4 9ODS SER D 7  ? UNP Q96SW2 CYS 322 conflict         322 22 
4 9ODS SER D 28 ? UNP Q96SW2 CYS 343 conflict         343 23 
4 9ODS SER D 51 ? UNP Q96SW2 CYS 366 conflict         366 24 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,M 
2 1 B,G,H,N 
3 1 C,I,J,O 
4 1 D,K,L,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'fluorescence resonance energy transfer' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 THR A 18 ? ILE A 22 ? THR A 333 ILE A 337 5 ? 5 
HELX_P HELX_P2 AA2 THR B 18 ? ILE B 22 ? THR B 333 ILE B 337 5 ? 5 
HELX_P HELX_P3 AA3 ASN C 20 ? ILE C 22 ? ASN C 335 ILE C 337 5 ? 3 
HELX_P HELX_P4 AA4 THR D 18 ? ILE D 22 ? THR D 333 ILE D 337 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 8  SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 323 A ZN 502 1_555 ? ? ? ? ? ? ? 2.477 ? ? 
metalc2  metalc ? ? A CYS 11 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 326 A ZN 502 1_555 ? ? ? ? ? ? ? 2.420 ? ? 
metalc3  metalc ? ? A CYS 76 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 391 A ZN 502 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc4  metalc ? ? A CYS 79 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 394 A ZN 502 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc5  metalc ? ? B CYS 8  SG ? ? ? 1_555 H ZN . ZN ? ? B CYS 323 B ZN 502 1_555 ? ? ? ? ? ? ? 2.627 ? ? 
metalc6  metalc ? ? B CYS 11 SG ? ? ? 1_555 H ZN . ZN ? ? B CYS 326 B ZN 502 1_555 ? ? ? ? ? ? ? 2.398 ? ? 
metalc7  metalc ? ? B CYS 76 SG ? ? ? 1_555 H ZN . ZN ? ? B CYS 391 B ZN 502 1_555 ? ? ? ? ? ? ? 2.387 ? ? 
metalc8  metalc ? ? B CYS 79 SG ? ? ? 1_555 H ZN . ZN ? ? B CYS 394 B ZN 502 1_555 ? ? ? ? ? ? ? 2.137 ? ? 
metalc9  metalc ? ? C CYS 8  SG ? ? ? 1_555 J ZN . ZN ? ? C CYS 323 C ZN 502 1_555 ? ? ? ? ? ? ? 2.496 ? ? 
metalc10 metalc ? ? C CYS 11 SG ? ? ? 1_555 J ZN . ZN ? ? C CYS 326 C ZN 502 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc11 metalc ? ? C CYS 76 SG ? ? ? 1_555 J ZN . ZN ? ? C CYS 391 C ZN 502 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc12 metalc ? ? C CYS 79 SG ? ? ? 1_555 J ZN . ZN ? ? C CYS 394 C ZN 502 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc13 metalc ? ? D CYS 8  SG ? ? ? 1_555 L ZN . ZN ? ? D CYS 323 D ZN 502 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc14 metalc ? ? D CYS 11 SG ? ? ? 1_555 L ZN . ZN ? ? D CYS 326 D ZN 502 1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc15 metalc ? ? D CYS 76 SG ? ? ? 1_555 L ZN . ZN ? ? D CYS 391 D ZN 502 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc16 metalc ? ? D CYS 79 SG ? ? ? 1_555 L ZN . ZN ? ? D CYS 394 D ZN 502 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 8  ? A CYS 323 ? 1_555 ZN ? F ZN . ? A ZN 502 ? 1_555 SG ? A CYS 11 ? A CYS 326 ? 1_555 94.5  ? 
2  SG ? A CYS 8  ? A CYS 323 ? 1_555 ZN ? F ZN . ? A ZN 502 ? 1_555 SG ? A CYS 76 ? A CYS 391 ? 1_555 110.6 ? 
3  SG ? A CYS 11 ? A CYS 326 ? 1_555 ZN ? F ZN . ? A ZN 502 ? 1_555 SG ? A CYS 76 ? A CYS 391 ? 1_555 107.3 ? 
4  SG ? A CYS 8  ? A CYS 323 ? 1_555 ZN ? F ZN . ? A ZN 502 ? 1_555 SG ? A CYS 79 ? A CYS 394 ? 1_555 94.9  ? 
5  SG ? A CYS 11 ? A CYS 326 ? 1_555 ZN ? F ZN . ? A ZN 502 ? 1_555 SG ? A CYS 79 ? A CYS 394 ? 1_555 130.4 ? 
6  SG ? A CYS 76 ? A CYS 391 ? 1_555 ZN ? F ZN . ? A ZN 502 ? 1_555 SG ? A CYS 79 ? A CYS 394 ? 1_555 114.4 ? 
7  SG ? B CYS 8  ? B CYS 323 ? 1_555 ZN ? H ZN . ? B ZN 502 ? 1_555 SG ? B CYS 11 ? B CYS 326 ? 1_555 93.1  ? 
8  SG ? B CYS 8  ? B CYS 323 ? 1_555 ZN ? H ZN . ? B ZN 502 ? 1_555 SG ? B CYS 76 ? B CYS 391 ? 1_555 112.1 ? 
9  SG ? B CYS 11 ? B CYS 326 ? 1_555 ZN ? H ZN . ? B ZN 502 ? 1_555 SG ? B CYS 76 ? B CYS 391 ? 1_555 108.3 ? 
10 SG ? B CYS 8  ? B CYS 323 ? 1_555 ZN ? H ZN . ? B ZN 502 ? 1_555 SG ? B CYS 79 ? B CYS 394 ? 1_555 94.8  ? 
11 SG ? B CYS 11 ? B CYS 326 ? 1_555 ZN ? H ZN . ? B ZN 502 ? 1_555 SG ? B CYS 79 ? B CYS 394 ? 1_555 125.2 ? 
12 SG ? B CYS 76 ? B CYS 391 ? 1_555 ZN ? H ZN . ? B ZN 502 ? 1_555 SG ? B CYS 79 ? B CYS 394 ? 1_555 118.1 ? 
13 SG ? C CYS 8  ? C CYS 323 ? 1_555 ZN ? J ZN . ? C ZN 502 ? 1_555 SG ? C CYS 11 ? C CYS 326 ? 1_555 99.1  ? 
14 SG ? C CYS 8  ? C CYS 323 ? 1_555 ZN ? J ZN . ? C ZN 502 ? 1_555 SG ? C CYS 76 ? C CYS 391 ? 1_555 110.4 ? 
15 SG ? C CYS 11 ? C CYS 326 ? 1_555 ZN ? J ZN . ? C ZN 502 ? 1_555 SG ? C CYS 76 ? C CYS 391 ? 1_555 106.8 ? 
16 SG ? C CYS 8  ? C CYS 323 ? 1_555 ZN ? J ZN . ? C ZN 502 ? 1_555 SG ? C CYS 79 ? C CYS 394 ? 1_555 100.3 ? 
17 SG ? C CYS 11 ? C CYS 326 ? 1_555 ZN ? J ZN . ? C ZN 502 ? 1_555 SG ? C CYS 79 ? C CYS 394 ? 1_555 121.3 ? 
18 SG ? C CYS 76 ? C CYS 391 ? 1_555 ZN ? J ZN . ? C ZN 502 ? 1_555 SG ? C CYS 79 ? C CYS 394 ? 1_555 116.8 ? 
19 SG ? D CYS 8  ? D CYS 323 ? 1_555 ZN ? L ZN . ? D ZN 502 ? 1_555 SG ? D CYS 11 ? D CYS 326 ? 1_555 103.0 ? 
20 SG ? D CYS 8  ? D CYS 323 ? 1_555 ZN ? L ZN . ? D ZN 502 ? 1_555 SG ? D CYS 76 ? D CYS 391 ? 1_555 111.8 ? 
21 SG ? D CYS 11 ? D CYS 326 ? 1_555 ZN ? L ZN . ? D ZN 502 ? 1_555 SG ? D CYS 76 ? D CYS 391 ? 1_555 112.0 ? 
22 SG ? D CYS 8  ? D CYS 323 ? 1_555 ZN ? L ZN . ? D ZN 502 ? 1_555 SG ? D CYS 79 ? D CYS 394 ? 1_555 97.2  ? 
23 SG ? D CYS 11 ? D CYS 326 ? 1_555 ZN ? L ZN . ? D ZN 502 ? 1_555 SG ? D CYS 79 ? D CYS 394 ? 1_555 119.3 ? 
24 SG ? D CYS 76 ? D CYS 391 ? 1_555 ZN ? L ZN . ? D ZN 502 ? 1_555 SG ? D CYS 79 ? D CYS 394 ? 1_555 111.9 ? 
# 
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 SER 95  A . ? SER 410 A PRO 96  A ? PRO 411 A 1 4.66  
2 LEU 108 A . ? LEU 423 A PRO 109 A ? PRO 424 A 1 -4.71 
3 SER 95  B . ? SER 410 B PRO 96  B ? PRO 411 B 1 1.56  
4 LEU 108 B . ? LEU 423 B PRO 109 B ? PRO 424 B 1 -6.99 
5 SER 95  C . ? SER 410 C PRO 96  C ? PRO 411 C 1 -1.54 
6 LEU 108 C . ? LEU 423 C PRO 109 C ? PRO 424 C 1 -2.26 
7 SER 95  D . ? SER 410 D PRO 96  D ? PRO 411 D 1 3.93  
8 LEU 108 D . ? LEU 423 D PRO 109 D ? PRO 424 D 1 -2.82 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
AA4 ? 6 ? 
AA5 ? 3 ? 
AA6 ? 6 ? 
AA7 ? 3 ? 
AA8 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? 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 GLU A 15  ? THR A 17  ? GLU A 330 THR A 332 
AA1 2 LEU A 6   ? CYS A 8   ? LEU A 321 CYS A 323 
AA1 3 LEU A 107 ? LEU A 108 ? LEU A 422 LEU A 423 
AA2 1 MET A 31  ? VAL A 35  ? MET A 346 VAL A 350 
AA2 2 VAL A 41  ? VAL A 47  ? VAL A 356 VAL A 362 
AA2 3 LYS A 98  ? THR A 103 ? LYS A 413 THR A 418 
AA2 4 HIS A 82  ? ALA A 89  ? HIS A 397 ALA A 404 
AA2 5 TYR A 69  ? CYS A 76  ? TYR A 384 CYS A 391 
AA2 6 LEU A 53  ? SER A 60  ? LEU A 368 SER A 375 
AA3 1 GLU B 15  ? THR B 17  ? GLU B 330 THR B 332 
AA3 2 LEU B 6   ? CYS B 8   ? LEU B 321 CYS B 323 
AA3 3 LEU B 107 ? LEU B 108 ? LEU B 422 LEU B 423 
AA4 1 MET B 31  ? VAL B 35  ? MET B 346 VAL B 350 
AA4 2 VAL B 41  ? VAL B 47  ? VAL B 356 VAL B 362 
AA4 3 LYS B 98  ? THR B 103 ? LYS B 413 THR B 418 
AA4 4 HIS B 82  ? ALA B 89  ? HIS B 397 ALA B 404 
AA4 5 TYR B 69  ? CYS B 76  ? TYR B 384 CYS B 391 
AA4 6 LEU B 53  ? SER B 60  ? LEU B 368 SER B 375 
AA5 1 GLU C 15  ? THR C 18  ? GLU C 330 THR C 333 
AA5 2 SER C 5   ? CYS C 8   ? SER C 320 CYS C 323 
AA5 3 LEU C 107 ? LEU C 108 ? LEU C 422 LEU C 423 
AA6 1 ALA C 33  ? VAL C 35  ? ALA C 348 VAL C 350 
AA6 2 VAL C 41  ? VAL C 47  ? VAL C 356 VAL C 362 
AA6 3 LYS C 98  ? THR C 103 ? LYS C 413 THR C 418 
AA6 4 HIS C 82  ? ALA C 89  ? HIS C 397 ALA C 404 
AA6 5 TYR C 69  ? CYS C 76  ? TYR C 384 CYS C 391 
AA6 6 LEU C 53  ? SER C 60  ? LEU C 368 SER C 375 
AA7 1 GLU D 15  ? THR D 17  ? GLU D 330 THR D 332 
AA7 2 LEU D 6   ? CYS D 8   ? LEU D 321 CYS D 323 
AA7 3 LEU D 107 ? LEU D 108 ? LEU D 422 LEU D 423 
AA8 1 MET D 31  ? VAL D 35  ? MET D 346 VAL D 350 
AA8 2 VAL D 41  ? VAL D 47  ? VAL D 356 VAL D 362 
AA8 3 LYS D 98  ? THR D 103 ? LYS D 413 THR D 418 
AA8 4 HIS D 82  ? ALA D 89  ? HIS D 397 ALA D 404 
AA8 5 TYR D 69  ? CYS D 76  ? TYR D 384 CYS D 391 
AA8 6 LEU D 53  ? SER D 60  ? LEU D 368 SER D 375 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O THR A 17  ? O THR A 332 N LEU A 6   ? N LEU A 321 
AA1 2 3 N SER A 7   ? N SER A 322 O LEU A 108 ? O LEU A 423 
AA2 1 2 N TYR A 34  ? N TYR A 349 O HIS A 42  ? O HIS A 357 
AA2 2 3 N VAL A 47  ? N VAL A 362 O TRP A 100 ? O TRP A 415 
AA2 3 4 O THR A 103 ? O THR A 418 N ILE A 83  ? N ILE A 398 
AA2 4 5 O LYS A 86  ? O LYS A 401 N THR A 72  ? N THR A 387 
AA2 5 6 O TRP A 71  ? O TRP A 386 N SER A 60  ? N SER A 375 
AA3 1 2 O ILE B 16  ? O ILE B 331 N LEU B 6   ? N LEU B 321 
AA3 2 3 N SER B 7   ? N SER B 322 O LEU B 108 ? O LEU B 423 
AA4 1 2 N TYR B 34  ? N TYR B 349 O HIS B 42  ? O HIS B 357 
AA4 2 3 N VAL B 47  ? N VAL B 362 O TRP B 100 ? O TRP B 415 
AA4 3 4 O THR B 103 ? O THR B 418 N ILE B 83  ? N ILE B 398 
AA4 4 5 O GLY B 84  ? O GLY B 399 N ALA B 74  ? N ALA B 389 
AA4 5 6 O TRP B 71  ? O TRP B 386 N SER B 60  ? N SER B 375 
AA5 1 2 O ILE C 16  ? O ILE C 331 N LEU C 6   ? N LEU C 321 
AA5 2 3 N SER C 7   ? N SER C 322 O LEU C 108 ? O LEU C 423 
AA6 1 2 N TYR C 34  ? N TYR C 349 O HIS C 42  ? O HIS C 357 
AA6 2 3 N VAL C 47  ? N VAL C 362 O TRP C 100 ? O TRP C 415 
AA6 3 4 O THR C 103 ? O THR C 418 N ILE C 83  ? N ILE C 398 
AA6 4 5 O GLY C 84  ? O GLY C 399 N ALA C 74  ? N ALA C 389 
AA6 5 6 O GLN C 75  ? O GLN C 390 N ASN C 54  ? N ASN C 369 
AA7 1 2 O ILE D 16  ? O ILE D 331 N LEU D 6   ? N LEU D 321 
AA7 2 3 N SER D 7   ? N SER D 322 O LEU D 108 ? O LEU D 423 
AA8 1 2 N TYR D 34  ? N TYR D 349 O HIS D 42  ? O HIS D 357 
AA8 2 3 N VAL D 47  ? N VAL D 362 O TRP D 100 ? O TRP D 415 
AA8 3 4 O THR D 103 ? O THR D 418 N ILE D 83  ? N ILE D 398 
AA8 4 5 O GLY D 84  ? O GLY D 399 N ALA D 74  ? N ALA D 389 
AA8 5 6 O TRP D 71  ? O TRP D 386 N SER D 60  ? N SER D 375 
# 
_pdbx_entry_details.entry_id                   9ODS 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLN A 327 ? ? 87.44   -33.00  
2  1 LEU A 342 ? ? 67.00   -16.64  
3  1 SER A 343 ? ? -105.86 44.36   
4  1 GLN B 327 ? ? 87.16   -32.89  
5  1 ASN B 335 ? ? -87.04  34.17   
6  1 ASN B 367 ? ? 72.21   42.88   
7  1 GLN C 327 ? ? 78.99   -23.73  
8  1 SER C 341 ? ? 47.45   -116.32 
9  1 GLN D 327 ? ? 86.19   -27.82  
10 1 SER D 341 ? ? 39.47   -113.37 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 316 ? A GLY 1   
2  1 Y 1 A PRO 317 ? A PRO 2   
3  1 Y 1 A SER 318 ? A SER 3   
4  1 Y 1 B GLY 316 ? B GLY 1   
5  1 Y 1 B PRO 317 ? B PRO 2   
6  1 Y 1 B ILE 426 ? B ILE 111 
7  1 Y 1 C GLY 316 ? C GLY 1   
8  1 Y 1 C PRO 317 ? C PRO 2   
9  1 Y 1 D GLY 316 ? D GLY 1   
10 1 Y 1 D PRO 317 ? D PRO 2   
# 
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 
A1CAW O1   O  N N 1   
A1CAW C1   C  N N 2   
A1CAW N1   N  N N 3   
A1CAW N2   N  N N 4   
A1CAW C2   C  Y N 5   
A1CAW C3   C  Y N 6   
A1CAW N3   N  Y N 7   
A1CAW C4   C  Y N 8   
A1CAW N4   N  Y N 9   
A1CAW C5   C  Y N 10  
A1CAW C6   C  Y N 11  
A1CAW C7   C  Y N 12  
A1CAW C8   C  Y N 13  
A1CAW O2   O  N N 14  
A1CAW C9   C  N N 15  
A1CAW C10  C  N N 16  
A1CAW C11  C  N N 17  
A1CAW C12  C  N N 18  
A1CAW N5   N  N N 19  
A1CAW C13  C  N N 20  
A1CAW C14  C  N N 21  
A1CAW C15  C  N N 22  
A1CAW C16  C  N N 23  
A1CAW C17  C  N N 24  
A1CAW O3   O  N N 25  
A1CAW H1   H  N N 26  
A1CAW H2   H  N N 27  
A1CAW H3   H  N N 28  
A1CAW H4   H  N N 29  
A1CAW H5   H  N N 30  
A1CAW H6   H  N N 31  
A1CAW H7   H  N N 32  
A1CAW H8   H  N N 33  
A1CAW H9   H  N N 34  
A1CAW H10  H  N N 35  
A1CAW H11  H  N N 36  
A1CAW H13  H  N N 37  
A1CAW H14  H  N N 38  
A1CAW H15  H  N N 39  
A1CAW H16  H  N N 40  
A1CAW H17  H  N N 41  
A1CAW H18  H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TRP   N    N  N N 363 
TRP   CA   C  N S 364 
TRP   C    C  N N 365 
TRP   O    O  N N 366 
TRP   CB   C  N N 367 
TRP   CG   C  Y N 368 
TRP   CD1  C  Y N 369 
TRP   CD2  C  Y N 370 
TRP   NE1  N  Y N 371 
TRP   CE2  C  Y N 372 
TRP   CE3  C  Y N 373 
TRP   CZ2  C  Y N 374 
TRP   CZ3  C  Y N 375 
TRP   CH2  C  Y N 376 
TRP   OXT  O  N N 377 
TRP   H    H  N N 378 
TRP   H2   H  N N 379 
TRP   HA   H  N N 380 
TRP   HB2  H  N N 381 
TRP   HB3  H  N N 382 
TRP   HD1  H  N N 383 
TRP   HE1  H  N N 384 
TRP   HE3  H  N N 385 
TRP   HZ2  H  N N 386 
TRP   HZ3  H  N N 387 
TRP   HH2  H  N N 388 
TRP   HXT  H  N N 389 
TYR   N    N  N N 390 
TYR   CA   C  N S 391 
TYR   C    C  N N 392 
TYR   O    O  N N 393 
TYR   CB   C  N N 394 
TYR   CG   C  Y N 395 
TYR   CD1  C  Y N 396 
TYR   CD2  C  Y N 397 
TYR   CE1  C  Y N 398 
TYR   CE2  C  Y N 399 
TYR   CZ   C  Y N 400 
TYR   OH   O  N N 401 
TYR   OXT  O  N N 402 
TYR   H    H  N N 403 
TYR   H2   H  N N 404 
TYR   HA   H  N N 405 
TYR   HB2  H  N N 406 
TYR   HB3  H  N N 407 
TYR   HD1  H  N N 408 
TYR   HD2  H  N N 409 
TYR   HE1  H  N N 410 
TYR   HE2  H  N N 411 
TYR   HH   H  N N 412 
TYR   HXT  H  N N 413 
VAL   N    N  N N 414 
VAL   CA   C  N S 415 
VAL   C    C  N N 416 
VAL   O    O  N N 417 
VAL   CB   C  N N 418 
VAL   CG1  C  N N 419 
VAL   CG2  C  N N 420 
VAL   OXT  O  N N 421 
VAL   H    H  N N 422 
VAL   H2   H  N N 423 
VAL   HA   H  N N 424 
VAL   HB   H  N N 425 
VAL   HG11 H  N N 426 
VAL   HG12 H  N N 427 
VAL   HG13 H  N N 428 
VAL   HG21 H  N N 429 
VAL   HG22 H  N N 430 
VAL   HG23 H  N N 431 
VAL   HXT  H  N N 432 
ZN    ZN   ZN N N 433 
# 
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 
A1CAW N5  C13  sing N N 1   
A1CAW N5  C12  sing N N 2   
A1CAW C13 C14  sing N N 3   
A1CAW C14 C10  sing N N 4   
A1CAW C12 C11  sing N N 5   
A1CAW C11 C10  sing N N 6   
A1CAW C6  C7   sing Y N 7   
A1CAW C6  C5   doub Y N 8   
A1CAW C10 C7   sing N N 9   
A1CAW C10 C9   sing N N 10  
A1CAW C7  C8   doub Y N 11  
A1CAW C5  N4   sing Y N 12  
A1CAW C9  O2   sing N N 13  
A1CAW O3  C17  doub N N 14  
A1CAW C8  O2   sing N N 15  
A1CAW C8  C4   sing Y N 16  
A1CAW C17 N1   sing N N 17  
A1CAW C17 C16  sing N N 18  
A1CAW N4  C4   sing Y N 19  
A1CAW N4  C2   sing Y N 20  
A1CAW N1  C1   sing N N 21  
A1CAW C16 C15  doub N N 22  
A1CAW C1  O1   doub N N 23  
A1CAW C1  N2   sing N N 24  
A1CAW C15 N2   sing N N 25  
A1CAW C4  N3   doub Y N 26  
A1CAW N2  C2   sing N N 27  
A1CAW C2  C3   doub Y N 28  
A1CAW N3  C3   sing Y N 29  
A1CAW N1  H1   sing N N 30  
A1CAW C3  H2   sing N N 31  
A1CAW C5  H3   sing N N 32  
A1CAW C6  H4   sing N N 33  
A1CAW C9  H5   sing N N 34  
A1CAW C9  H6   sing N N 35  
A1CAW C11 H7   sing N N 36  
A1CAW C11 H8   sing N N 37  
A1CAW C12 H9   sing N N 38  
A1CAW C12 H10  sing N N 39  
A1CAW N5  H11  sing N N 40  
A1CAW C13 H13  sing N N 41  
A1CAW C13 H14  sing N N 42  
A1CAW C14 H15  sing N N 43  
A1CAW C14 H16  sing N N 44  
A1CAW C15 H17  sing N N 45  
A1CAW C16 H18  sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   7BQU 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    9ODS 
_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]   0.010804 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004905 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011590 
_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]   0.012072 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . THR   A 1 4   ? 25.518  24.671  54.140  1.00 93.09  ? 319 THR   A N   1 
ATOM   2    C  CA  . THR   A 1 4   ? 24.516  25.172  53.172  1.00 93.10  ? 319 THR   A CA  1 
ATOM   3    C  C   . THR   A 1 4   ? 24.356  24.150  52.048  1.00 94.53  ? 319 THR   A C   1 
ATOM   4    O  O   . THR   A 1 4   ? 24.794  24.387  50.925  1.00 96.92  ? 319 THR   A O   1 
ATOM   5    C  CB  . THR   A 1 4   ? 24.930  26.544  52.634  1.00 92.50  ? 319 THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 4   ? 26.215  26.391  52.040  1.00 90.07  ? 319 THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 4   ? 25.005  27.611  53.713  1.00 93.22  ? 319 THR   A CG2 1 
ATOM   8    N  N   . SER   A 1 5   ? 23.731  23.011  52.369  1.00 94.50  ? 320 SER   A N   1 
ATOM   9    C  CA  . SER   A 1 5   ? 23.569  21.929  51.412  1.00 95.25  ? 320 SER   A CA  1 
ATOM   10   C  C   . SER   A 1 5   ? 22.328  21.107  51.752  1.00 95.18  ? 320 SER   A C   1 
ATOM   11   O  O   . SER   A 1 5   ? 22.171  20.659  52.886  1.00 94.23  ? 320 SER   A O   1 
ATOM   12   C  CB  . SER   A 1 5   ? 24.802  21.062  51.365  1.00 95.82  ? 320 SER   A CB  1 
ATOM   13   O  OG  . SER   A 1 5   ? 24.670  20.035  50.393  1.00 95.71  ? 320 SER   A OG  1 
ATOM   14   N  N   . LEU   A 1 6   ? 21.465  20.910  50.746  1.00 95.19  ? 321 LEU   A N   1 
ATOM   15   C  CA  . LEU   A 1 6   ? 20.208  20.196  50.907  1.00 94.26  ? 321 LEU   A CA  1 
ATOM   16   C  C   . LEU   A 1 6   ? 20.179  19.004  49.956  1.00 91.44  ? 321 LEU   A C   1 
ATOM   17   O  O   . LEU   A 1 6   ? 20.536  19.134  48.787  1.00 90.51  ? 321 LEU   A O   1 
ATOM   18   C  CB  . LEU   A 1 6   ? 19.053  21.160  50.644  1.00 96.43  ? 321 LEU   A CB  1 
ATOM   19   C  CG  . LEU   A 1 6   ? 18.873  22.281  51.673  1.00 98.11  ? 321 LEU   A CG  1 
ATOM   20   C  CD1 . LEU   A 1 6   ? 17.954  23.368  51.144  1.00 98.06  ? 321 LEU   A CD1 1 
ATOM   21   C  CD2 . LEU   A 1 6   ? 18.340  21.728  52.985  1.00 98.90  ? 321 LEU   A CD2 1 
ATOM   22   N  N   . SER   A 1 7   ? 19.728  17.852  50.470  1.00 88.97  ? 322 SER   A N   1 
ATOM   23   C  CA  . SER   A 1 7   ? 19.866  16.584  49.772  1.00 86.64  ? 322 SER   A CA  1 
ATOM   24   C  C   . SER   A 1 7   ? 18.528  15.856  49.696  1.00 83.75  ? 322 SER   A C   1 
ATOM   25   O  O   . SER   A 1 7   ? 17.619  16.136  50.474  1.00 83.69  ? 322 SER   A O   1 
ATOM   26   C  CB  . SER   A 1 7   ? 20.905  15.723  50.444  1.00 87.26  ? 322 SER   A CB  1 
ATOM   27   O  OG  . SER   A 1 7   ? 22.165  16.379  50.476  1.00 87.84  ? 322 SER   A OG  1 
ATOM   28   N  N   . CYS   A 1 8   ? 18.432  14.915  48.748  1.00 80.56  ? 323 CYS   A N   1 
ATOM   29   C  CA  . CYS   A 1 8   ? 17.307  13.998  48.664  1.00 79.17  ? 323 CYS   A CA  1 
ATOM   30   C  C   . CYS   A 1 8   ? 17.156  13.278  50.000  1.00 78.61  ? 323 CYS   A C   1 
ATOM   31   O  O   . CYS   A 1 8   ? 18.145  12.828  50.568  1.00 77.68  ? 323 CYS   A O   1 
ATOM   32   C  CB  . CYS   A 1 8   ? 17.509  12.988  47.539  1.00 77.81  ? 323 CYS   A CB  1 
ATOM   33   S  SG  . CYS   A 1 8   ? 16.221  11.715  47.447  1.00 74.16  ? 323 CYS   A SG  1 
ATOM   34   N  N   . LYS   A 1 9   ? 15.918  13.187  50.496  1.00 80.70  ? 324 LYS   A N   1 
ATOM   35   C  CA  . LYS   A 1 9   ? 15.652  12.580  51.790  1.00 82.58  ? 324 LYS   A CA  1 
ATOM   36   C  C   . LYS   A 1 9   ? 15.773  11.061  51.700  1.00 81.86  ? 324 LYS   A C   1 
ATOM   37   O  O   . LYS   A 1 9   ? 16.155  10.414  52.674  1.00 80.57  ? 324 LYS   A O   1 
ATOM   38   C  CB  . LYS   A 1 9   ? 14.267  12.990  52.307  1.00 84.85  ? 324 LYS   A CB  1 
ATOM   39   C  CG  . LYS   A 1 9   ? 13.770  12.218  53.528  1.00 86.61  ? 324 LYS   A CG  1 
ATOM   40   C  CD  . LYS   A 1 9   ? 12.633  12.900  54.280  1.00 87.91  ? 324 LYS   A CD  1 
ATOM   41   C  CE  . LYS   A 1 9   ? 13.115  14.038  55.123  1.00 88.98  ? 324 LYS   A CE  1 
ATOM   42   N  NZ  . LYS   A 1 9   ? 12.013  14.902  55.551  1.00 90.08  ? 324 LYS   A NZ  1 
ATOM   43   N  N   . GLN   A 1 10  ? 15.447  10.502  50.530  1.00 83.28  ? 325 GLN   A N   1 
ATOM   44   C  CA  . GLN   A 1 10  ? 15.282  9.065   50.386  1.00 85.03  ? 325 GLN   A CA  1 
ATOM   45   C  C   . GLN   A 1 10  ? 16.629  8.399   50.108  1.00 83.93  ? 325 GLN   A C   1 
ATOM   46   O  O   . GLN   A 1 10  ? 16.961  7.404   50.748  1.00 84.10  ? 325 GLN   A O   1 
ATOM   47   C  CB  . GLN   A 1 10  ? 14.259  8.761   49.293  1.00 88.15  ? 325 GLN   A CB  1 
ATOM   48   C  CG  . GLN   A 1 10  ? 13.616  7.385   49.428  1.00 91.40  ? 325 GLN   A CG  1 
ATOM   49   C  CD  . GLN   A 1 10  ? 12.875  6.956   48.181  1.00 96.24  ? 325 GLN   A CD  1 
ATOM   50   O  OE1 . GLN   A 1 10  ? 11.901  7.592   47.762  1.00 99.47  ? 325 GLN   A OE1 1 
ATOM   51   N  NE2 . GLN   A 1 10  ? 13.333  5.873   47.570  1.00 98.71  ? 325 GLN   A NE2 1 
ATOM   52   N  N   . CYS   A 1 11  ? 17.392  8.942   49.149  1.00 83.65  ? 326 CYS   A N   1 
ATOM   53   C  CA  . CYS   A 1 11  ? 18.680  8.371   48.776  1.00 82.67  ? 326 CYS   A CA  1 
ATOM   54   C  C   . CYS   A 1 11  ? 19.804  9.028   49.579  1.00 84.06  ? 326 CYS   A C   1 
ATOM   55   O  O   . CYS   A 1 11  ? 20.805  8.379   49.874  1.00 83.39  ? 326 CYS   A O   1 
ATOM   56   C  CB  . CYS   A 1 11  ? 18.911  8.446   47.270  1.00 80.86  ? 326 CYS   A CB  1 
ATOM   57   S  SG  . CYS   A 1 11  ? 19.337  10.098  46.663  1.00 78.81  ? 326 CYS   A SG  1 
ATOM   58   N  N   . GLN   A 1 12  ? 19.646  10.323  49.889  1.00 87.18  ? 327 GLN   A N   1 
ATOM   59   C  CA  . GLN   A 1 12  ? 20.396  11.000  50.942  1.00 89.91  ? 327 GLN   A CA  1 
ATOM   60   C  C   . GLN   A 1 12  ? 21.725  11.559  50.430  1.00 91.40  ? 327 GLN   A C   1 
ATOM   61   O  O   . GLN   A 1 12  ? 22.170  12.601  50.906  1.00 92.01  ? 327 GLN   A O   1 
ATOM   62   C  CB  . GLN   A 1 12  ? 20.591  10.122  52.180  1.00 90.91  ? 327 GLN   A CB  1 
ATOM   63   C  CG  . GLN   A 1 12  ? 19.282  9.614   52.777  1.00 93.44  ? 327 GLN   A CG  1 
ATOM   64   C  CD  . GLN   A 1 12  ? 19.454  8.938   54.119  1.00 96.78  ? 327 GLN   A CD  1 
ATOM   65   O  OE1 . GLN   A 1 12  ? 19.153  7.751   54.287  1.00 97.70  ? 327 GLN   A OE1 1 
ATOM   66   N  NE2 . GLN   A 1 12  ? 19.934  9.694   55.096  1.00 98.44  ? 327 GLN   A NE2 1 
ATOM   67   N  N   . GLU   A 1 13  ? 22.348  10.875  49.465  1.00 92.91  ? 328 GLU   A N   1 
ATOM   68   C  CA  . GLU   A 1 13  ? 23.685  11.221  49.003  1.00 94.23  ? 328 GLU   A CA  1 
ATOM   69   C  C   . GLU   A 1 13  ? 23.661  12.435  48.073  1.00 92.90  ? 328 GLU   A C   1 
ATOM   70   O  O   . GLU   A 1 13  ? 24.658  13.145  47.964  1.00 93.19  ? 328 GLU   A O   1 
ATOM   71   C  CB  . GLU   A 1 13  ? 24.310  10.020  48.289  1.00 95.98  ? 328 GLU   A CB  1 
ATOM   72   C  CG  . GLU   A 1 13  ? 23.560  9.590   47.029  1.00 96.57  ? 328 GLU   A CG  1 
ATOM   73   C  CD  . GLU   A 1 13  ? 24.067  8.311   46.387  1.00 96.95  ? 328 GLU   A CD  1 
ATOM   74   O  OE1 . GLU   A 1 13  ? 25.102  7.774   46.838  1.00 98.32  ? 328 GLU   A OE1 1 
ATOM   75   O  OE2 . GLU   A 1 13  ? 23.410  7.845   45.433  1.00 96.64  ? 328 GLU   A OE2 1 
ATOM   76   N  N   . THR   A 1 14  ? 22.518  12.668  47.416  1.00 91.36  ? 329 THR   A N   1 
ATOM   77   C  CA  . THR   A 1 14  ? 22.433  13.563  46.272  1.00 90.83  ? 329 THR   A CA  1 
ATOM   78   C  C   . THR   A 1 14  ? 22.162  14.993  46.733  1.00 90.25  ? 329 THR   A C   1 
ATOM   79   O  O   . THR   A 1 14  ? 21.144  15.244  47.372  1.00 91.42  ? 329 THR   A O   1 
ATOM   80   C  CB  . THR   A 1 14  ? 21.315  13.054  45.362  1.00 91.91  ? 329 THR   A CB  1 
ATOM   81   O  OG1 . THR   A 1 14  ? 21.594  11.676  45.138  1.00 91.96  ? 329 THR   A OG1 1 
ATOM   82   C  CG2 . THR   A 1 14  ? 21.238  13.800  44.042  1.00 92.57  ? 329 THR   A CG2 1 
ATOM   83   N  N   . GLU   A 1 15  ? 23.058  15.926  46.379  1.00 89.99  ? 330 GLU   A N   1 
ATOM   84   C  CA  . GLU   A 1 15  ? 22.809  17.346  46.586  1.00 91.23  ? 330 GLU   A CA  1 
ATOM   85   C  C   . GLU   A 1 15  ? 21.846  17.844  45.511  1.00 90.33  ? 330 GLU   A C   1 
ATOM   86   O  O   . GLU   A 1 15  ? 22.082  17.640  44.322  1.00 90.31  ? 330 GLU   A O   1 
ATOM   87   C  CB  . GLU   A 1 15  ? 24.077  18.203  46.550  1.00 93.44  ? 330 GLU   A CB  1 
ATOM   88   C  CG  . GLU   A 1 15  ? 23.779  19.702  46.554  1.00 96.24  ? 330 GLU   A CG  1 
ATOM   89   C  CD  . GLU   A 1 15  ? 24.960  20.613  46.834  1.00 99.34  ? 330 GLU   A CD  1 
ATOM   90   O  OE1 . GLU   A 1 15  ? 25.573  20.473  47.913  1.00 101.71 ? 330 GLU   A OE1 1 
ATOM   91   O  OE2 . GLU   A 1 15  ? 25.255  21.476  45.980  1.00 101.04 ? 330 GLU   A OE2 1 
ATOM   92   N  N   . ILE   A 1 16  ? 20.771  18.512  45.949  1.00 88.88  ? 331 ILE   A N   1 
ATOM   93   C  CA  . ILE   A 1 16  ? 19.793  19.097  45.047  1.00 86.47  ? 331 ILE   A CA  1 
ATOM   94   C  C   . ILE   A 1 16  ? 20.085  20.589  44.908  1.00 86.42  ? 331 ILE   A C   1 
ATOM   95   O  O   . ILE   A 1 16  ? 20.203  21.093  43.793  1.00 86.28  ? 331 ILE   A O   1 
ATOM   96   C  CB  . ILE   A 1 16  ? 18.357  18.843  45.545  1.00 85.44  ? 331 ILE   A CB  1 
ATOM   97   C  CG1 . ILE   A 1 16  ? 18.101  17.358  45.838  1.00 85.02  ? 331 ILE   A CG1 1 
ATOM   98   C  CG2 . ILE   A 1 16  ? 17.330  19.408  44.562  1.00 85.04  ? 331 ILE   A CG2 1 
ATOM   99   C  CD1 . ILE   A 1 16  ? 18.186  16.451  44.623  1.00 84.88  ? 331 ILE   A CD1 1 
ATOM   100  N  N   . THR   A 1 17  ? 20.186  21.282  46.051  1.00 87.60  ? 332 THR   A N   1 
ATOM   101  C  CA  . THR   A 1 17  ? 20.432  22.716  46.068  1.00 88.48  ? 332 THR   A CA  1 
ATOM   102  C  C   . THR   A 1 17  ? 21.131  23.106  47.370  1.00 88.88  ? 332 THR   A C   1 
ATOM   103  O  O   . THR   A 1 17  ? 21.339  22.269  48.249  1.00 86.45  ? 332 THR   A O   1 
ATOM   104  C  CB  . THR   A 1 17  ? 19.105  23.457  45.886  1.00 87.66  ? 332 THR   A CB  1 
ATOM   105  O  OG1 . THR   A 1 17  ? 19.439  24.826  45.674  1.00 86.69  ? 332 THR   A OG1 1 
ATOM   106  C  CG2 . THR   A 1 17  ? 18.177  23.316  47.080  1.00 87.02  ? 332 THR   A CG2 1 
ATOM   107  N  N   . THR   A 1 18  ? 21.490  24.394  47.467  1.00 90.05  ? 333 THR   A N   1 
ATOM   108  C  CA  . THR   A 1 18  ? 22.103  24.965  48.656  1.00 89.68  ? 333 THR   A CA  1 
ATOM   109  C  C   . THR   A 1 18  ? 21.169  26.028  49.232  1.00 90.99  ? 333 THR   A C   1 
ATOM   110  O  O   . THR   A 1 18  ? 20.300  26.542  48.532  1.00 91.71  ? 333 THR   A O   1 
ATOM   111  C  CB  . THR   A 1 18  ? 23.473  25.543  48.299  1.00 89.34  ? 333 THR   A CB  1 
ATOM   112  O  OG1 . THR   A 1 18  ? 23.237  26.536  47.306  1.00 88.73  ? 333 THR   A OG1 1 
ATOM   113  C  CG2 . THR   A 1 18  ? 24.427  24.492  47.762  1.00 89.59  ? 333 THR   A CG2 1 
ATOM   114  N  N   . LYS   A 1 19  ? 21.378  26.356  50.512  1.00 92.45  ? 334 LYS   A N   1 
ATOM   115  C  CA  . LYS   A 1 19  ? 20.490  27.233  51.262  1.00 93.18  ? 334 LYS   A CA  1 
ATOM   116  C  C   . LYS   A 1 19  ? 20.575  28.676  50.764  1.00 90.46  ? 334 LYS   A C   1 
ATOM   117  O  O   . LYS   A 1 19  ? 19.626  29.437  50.936  1.00 89.75  ? 334 LYS   A O   1 
ATOM   118  C  CB  . LYS   A 1 19  ? 20.820  27.122  52.756  1.00 96.60  ? 334 LYS   A CB  1 
ATOM   119  C  CG  . LYS   A 1 19  ? 20.122  25.975  53.486  1.00 100.00 ? 334 LYS   A CG  1 
ATOM   120  C  CD  . LYS   A 1 19  ? 20.982  25.180  54.465  1.00 103.36 ? 334 LYS   A CD  1 
ATOM   121  C  CE  . LYS   A 1 19  ? 21.774  25.988  55.452  1.00 105.88 ? 334 LYS   A CE  1 
ATOM   122  N  NZ  . LYS   A 1 19  ? 20.930  26.664  56.441  1.00 108.20 ? 334 LYS   A NZ  1 
ATOM   123  N  N   . ASN   A 1 20  ? 21.702  29.046  50.140  1.00 88.82  ? 335 ASN   A N   1 
ATOM   124  C  CA  . ASN   A 1 20  ? 21.886  30.396  49.626  1.00 88.03  ? 335 ASN   A CA  1 
ATOM   125  C  C   . ASN   A 1 20  ? 21.394  30.487  48.178  1.00 84.48  ? 335 ASN   A C   1 
ATOM   126  O  O   . ASN   A 1 20  ? 21.785  31.398  47.451  1.00 83.23  ? 335 ASN   A O   1 
ATOM   127  C  CB  . ASN   A 1 20  ? 23.317  30.896  49.828  1.00 89.08  ? 335 ASN   A CB  1 
ATOM   128  C  CG  . ASN   A 1 20  ? 24.347  29.790  49.824  1.00 89.88  ? 335 ASN   A CG  1 
ATOM   129  O  OD1 . ASN   A 1 20  ? 24.369  28.962  50.741  1.00 88.23  ? 335 ASN   A OD1 1 
ATOM   130  N  ND2 . ASN   A 1 20  ? 25.219  29.768  48.826  1.00 90.58  ? 335 ASN   A ND2 1 
ATOM   131  N  N   . GLU   A 1 21  ? 20.523  29.550  47.774  1.00 81.88  ? 336 GLU   A N   1 
ATOM   132  C  CA  . GLU   A 1 21  ? 19.769  29.658  46.533  1.00 80.46  ? 336 GLU   A CA  1 
ATOM   133  C  C   . GLU   A 1 21  ? 18.306  29.990  46.825  1.00 79.05  ? 336 GLU   A C   1 
ATOM   134  O  O   . GLU   A 1 21  ? 17.520  30.163  45.896  1.00 77.61  ? 336 GLU   A O   1 
ATOM   135  C  CB  . GLU   A 1 21  ? 19.840  28.355  45.734  1.00 79.96  ? 336 GLU   A CB  1 
ATOM   136  C  CG  . GLU   A 1 21  ? 21.215  28.074  45.135  1.00 80.18  ? 336 GLU   A CG  1 
ATOM   137  C  CD  . GLU   A 1 21  ? 21.594  28.946  43.950  1.00 80.71  ? 336 GLU   A CD  1 
ATOM   138  O  OE1 . GLU   A 1 21  ? 20.772  29.787  43.525  1.00 80.39  ? 336 GLU   A OE1 1 
ATOM   139  O  OE2 . GLU   A 1 21  ? 22.724  28.778  43.447  1.00 81.00  ? 336 GLU   A OE2 1 
ATOM   140  N  N   . ILE   A 1 22  ? 17.947  30.080  48.113  1.00 78.78  ? 337 ILE   A N   1 
ATOM   141  C  CA  . ILE   A 1 22  ? 16.570  30.318  48.521  1.00 79.83  ? 337 ILE   A CA  1 
ATOM   142  C  C   . ILE   A 1 22  ? 16.202  31.765  48.202  1.00 80.69  ? 337 ILE   A C   1 
ATOM   143  O  O   . ILE   A 1 22  ? 17.063  32.642  48.205  1.00 80.94  ? 337 ILE   A O   1 
ATOM   144  C  CB  . ILE   A 1 22  ? 16.374  29.992  50.016  1.00 79.42  ? 337 ILE   A CB  1 
ATOM   145  C  CG1 . ILE   A 1 22  ? 16.622  28.507  50.303  1.00 80.30  ? 337 ILE   A CG1 1 
ATOM   146  C  CG2 . ILE   A 1 22  ? 14.990  30.431  50.501  1.00 79.18  ? 337 ILE   A CG2 1 
ATOM   147  C  CD1 . ILE   A 1 22  ? 16.743  28.163  51.777  1.00 80.02  ? 337 ILE   A CD1 1 
ATOM   148  N  N   . PHE   A 1 23  ? 14.914  31.992  47.916  1.00 81.90  ? 338 PHE   A N   1 
ATOM   149  C  CA  . PHE   A 1 23  ? 14.393  33.332  47.703  1.00 83.96  ? 338 PHE   A CA  1 
ATOM   150  C  C   . PHE   A 1 23  ? 12.884  33.326  47.937  1.00 86.48  ? 338 PHE   A C   1 
ATOM   151  O  O   . PHE   A 1 23  ? 12.238  32.285  47.831  1.00 86.37  ? 338 PHE   A O   1 
ATOM   152  C  CB  . PHE   A 1 23  ? 14.767  33.821  46.300  1.00 83.40  ? 338 PHE   A CB  1 
ATOM   153  C  CG  . PHE   A 1 23  ? 13.890  33.298  45.170  1.00 84.51  ? 338 PHE   A CG  1 
ATOM   154  C  CD1 . PHE   A 1 23  ? 13.948  31.964  44.776  1.00 85.91  ? 338 PHE   A CD1 1 
ATOM   155  C  CD2 . PHE   A 1 23  ? 13.028  34.149  44.486  1.00 85.15  ? 338 PHE   A CD2 1 
ATOM   156  C  CE1 . PHE   A 1 23  ? 13.152  31.496  43.741  1.00 86.56  ? 338 PHE   A CE1 1 
ATOM   157  C  CE2 . PHE   A 1 23  ? 12.237  33.676  43.449  1.00 85.92  ? 338 PHE   A CE2 1 
ATOM   158  C  CZ  . PHE   A 1 23  ? 12.301  32.352  43.079  1.00 86.51  ? 338 PHE   A CZ  1 
ATOM   159  N  N   . SER   A 1 24  ? 12.342  34.508  48.255  1.00 87.80  ? 339 SER   A N   1 
ATOM   160  C  CA  . SER   A 1 24  ? 10.931  34.668  48.562  1.00 89.03  ? 339 SER   A CA  1 
ATOM   161  C  C   . SER   A 1 24  ? 10.181  35.140  47.320  1.00 90.67  ? 339 SER   A C   1 
ATOM   162  O  O   . SER   A 1 24  ? 10.425  36.243  46.835  1.00 91.45  ? 339 SER   A O   1 
ATOM   163  C  CB  . SER   A 1 24  ? 10.741  35.627  49.710  1.00 89.52  ? 339 SER   A CB  1 
ATOM   164  O  OG  . SER   A 1 24  ? 9.362   35.867  49.959  1.00 90.16  ? 339 SER   A OG  1 
ATOM   165  N  N   . LEU   A 1 25  ? 9.282   34.289  46.807  1.00 92.78  ? 340 LEU   A N   1 
ATOM   166  C  CA  . LEU   A 1 25  ? 8.401   34.665  45.711  1.00 94.28  ? 340 LEU   A CA  1 
ATOM   167  C  C   . LEU   A 1 25  ? 6.943   34.620  46.171  1.00 96.12  ? 340 LEU   A C   1 
ATOM   168  O  O   . LEU   A 1 25  ? 6.063   35.139  45.489  1.00 96.65  ? 340 LEU   A O   1 
ATOM   169  C  CB  . LEU   A 1 25  ? 8.638   33.770  44.495  1.00 93.25  ? 340 LEU   A CB  1 
ATOM   170  C  CG  . LEU   A 1 25  ? 8.549   34.460  43.129  1.00 92.07  ? 340 LEU   A CG  1 
ATOM   171  C  CD1 . LEU   A 1 25  ? 8.812   33.453  42.027  1.00 92.75  ? 340 LEU   A CD1 1 
ATOM   172  C  CD2 . LEU   A 1 25  ? 7.225   35.168  42.881  1.00 91.15  ? 340 LEU   A CD2 1 
ATOM   173  N  N   . SER   A 1 26  ? 6.685   34.001  47.330  1.00 97.71  ? 341 SER   A N   1 
ATOM   174  C  CA  . SER   A 1 26  ? 5.437   34.233  48.036  1.00 99.77  ? 341 SER   A CA  1 
ATOM   175  C  C   . SER   A 1 26  ? 5.375   35.700  48.457  1.00 100.42 ? 341 SER   A C   1 
ATOM   176  O  O   . SER   A 1 26  ? 4.289   36.256  48.604  1.00 102.56 ? 341 SER   A O   1 
ATOM   177  C  CB  . SER   A 1 26  ? 5.292   33.318  49.227  1.00 101.14 ? 341 SER   A CB  1 
ATOM   178  O  OG  . SER   A 1 26  ? 5.787   32.018  48.937  1.00 103.07 ? 341 SER   A OG  1 
ATOM   179  N  N   . LEU   A 1 27  ? 6.561   36.297  48.665  1.00 100.20 ? 342 LEU   A N   1 
ATOM   180  C  CA  . LEU   A 1 27  ? 6.728   37.668  49.131  1.00 97.32  ? 342 LEU   A CA  1 
ATOM   181  C  C   . LEU   A 1 27  ? 6.222   37.788  50.570  1.00 96.89  ? 342 LEU   A C   1 
ATOM   182  O  O   . LEU   A 1 27  ? 6.539   38.761  51.252  1.00 96.06  ? 342 LEU   A O   1 
ATOM   183  C  CB  . LEU   A 1 27  ? 6.106   38.721  48.208  1.00 93.89  ? 342 LEU   A CB  1 
ATOM   184  C  CG  . LEU   A 1 27  ? 6.945   39.186  47.007  1.00 90.48  ? 342 LEU   A CG  1 
ATOM   185  C  CD1 . LEU   A 1 27  ? 8.424   39.341  47.344  1.00 89.73  ? 342 LEU   A CD1 1 
ATOM   186  C  CD2 . LEU   A 1 27  ? 6.783   38.285  45.796  1.00 87.86  ? 342 LEU   A CD2 1 
ATOM   187  N  N   . SER   A 1 28  ? 5.434   36.798  51.016  1.00 95.59  ? 343 SER   A N   1 
ATOM   188  C  CA  . SER   A 1 28  ? 5.215   36.532  52.428  1.00 93.26  ? 343 SER   A CA  1 
ATOM   189  C  C   . SER   A 1 28  ? 5.986   35.277  52.839  1.00 91.76  ? 343 SER   A C   1 
ATOM   190  O  O   . SER   A 1 28  ? 5.448   34.414  53.533  1.00 88.51  ? 343 SER   A O   1 
ATOM   191  C  CB  . SER   A 1 28  ? 3.743   36.398  52.725  1.00 92.03  ? 343 SER   A CB  1 
ATOM   192  O  OG  . SER   A 1 28  ? 3.172   35.330  51.983  1.00 91.53  ? 343 SER   A OG  1 
ATOM   193  N  N   . GLY   A 1 29  ? 7.244   35.183  52.385  1.00 91.43  ? 344 GLY   A N   1 
ATOM   194  C  CA  . GLY   A 1 29  ? 8.163   34.140  52.812  1.00 90.91  ? 344 GLY   A CA  1 
ATOM   195  C  C   . GLY   A 1 29  ? 8.667   33.301  51.639  1.00 89.93  ? 344 GLY   A C   1 
ATOM   196  O  O   . GLY   A 1 29  ? 8.010   33.216  50.605  1.00 90.50  ? 344 GLY   A O   1 
ATOM   197  N  N   . PRO   A 1 30  ? 9.856   32.665  51.757  1.00 88.79  ? 345 PRO   A N   1 
ATOM   198  C  CA  . PRO   A 1 30  ? 10.279  31.645  50.802  1.00 88.32  ? 345 PRO   A CA  1 
ATOM   199  C  C   . PRO   A 1 30  ? 9.511   30.335  50.962  1.00 86.55  ? 345 PRO   A C   1 
ATOM   200  O  O   . PRO   A 1 30  ? 9.387   29.566  50.010  1.00 85.08  ? 345 PRO   A O   1 
ATOM   201  C  CB  . PRO   A 1 30  ? 11.768  31.488  51.097  1.00 88.44  ? 345 PRO   A CB  1 
ATOM   202  C  CG  . PRO   A 1 30  ? 11.852  31.811  52.579  1.00 88.53  ? 345 PRO   A CG  1 
ATOM   203  C  CD  . PRO   A 1 30  ? 10.855  32.905  52.811  1.00 88.74  ? 345 PRO   A CD  1 
ATOM   204  N  N   . MET   A 1 31  ? 9.003   30.105  52.179  1.00 84.77  ? 346 MET   A N   1 
ATOM   205  C  CA  . MET   A 1 31  ? 8.257   28.907  52.522  1.00 84.37  ? 346 MET   A CA  1 
ATOM   206  C  C   . MET   A 1 31  ? 6.764   29.221  52.523  1.00 80.54  ? 346 MET   A C   1 
ATOM   207  O  O   . MET   A 1 31  ? 6.304   30.041  53.314  1.00 83.57  ? 346 MET   A O   1 
ATOM   208  C  CB  . MET   A 1 31  ? 8.642   28.422  53.923  1.00 87.74  ? 346 MET   A CB  1 
ATOM   209  C  CG  . MET   A 1 31  ? 10.113  28.101  54.089  1.00 90.84  ? 346 MET   A CG  1 
ATOM   210  S  SD  . MET   A 1 31  ? 10.599  28.084  55.826  1.00 97.22  ? 346 MET   A SD  1 
ATOM   211  C  CE  . MET   A 1 31  ? 10.450  29.829  56.238  1.00 97.66  ? 346 MET   A CE  1 
ATOM   212  N  N   . ALA   A 1 32  ? 6.019   28.555  51.635  1.00 75.48  ? 347 ALA   A N   1 
ATOM   213  C  CA  . ALA   A 1 32  ? 4.577   28.711  51.556  1.00 71.29  ? 347 ALA   A CA  1 
ATOM   214  C  C   . ALA   A 1 32  ? 3.913   27.343  51.678  1.00 67.90  ? 347 ALA   A C   1 
ATOM   215  O  O   . ALA   A 1 32  ? 4.588   26.337  51.885  1.00 69.32  ? 347 ALA   A O   1 
ATOM   216  C  CB  . ALA   A 1 32  ? 4.214   29.396  50.257  1.00 71.41  ? 347 ALA   A CB  1 
ATOM   217  N  N   . ALA   A 1 33  ? 2.580   27.328  51.576  1.00 64.16  ? 348 ALA   A N   1 
ATOM   218  C  CA  . ALA   A 1 33  ? 1.825   26.096  51.432  1.00 61.17  ? 348 ALA   A CA  1 
ATOM   219  C  C   . ALA   A 1 33  ? 0.737   26.304  50.383  1.00 58.95  ? 348 ALA   A C   1 
ATOM   220  O  O   . ALA   A 1 33  ? 0.005   27.290  50.438  1.00 58.98  ? 348 ALA   A O   1 
ATOM   221  C  CB  . ALA   A 1 33  ? 1.247   25.677  52.764  1.00 61.04  ? 348 ALA   A CB  1 
ATOM   222  N  N   . TYR   A 1 34  ? 0.658   25.374  49.425  1.00 56.69  ? 349 TYR   A N   1 
ATOM   223  C  CA  . TYR   A 1 34  ? -0.280  25.476  48.320  1.00 55.26  ? 349 TYR   A CA  1 
ATOM   224  C  C   . TYR   A 1 34  ? -1.151  24.226  48.285  1.00 54.39  ? 349 TYR   A C   1 
ATOM   225  O  O   . TYR   A 1 34  ? -0.723  23.155  48.708  1.00 54.87  ? 349 TYR   A O   1 
ATOM   226  C  CB  . TYR   A 1 34  ? 0.472   25.657  46.999  1.00 54.97  ? 349 TYR   A CB  1 
ATOM   227  C  CG  . TYR   A 1 34  ? 1.334   26.910  46.941  1.00 54.54  ? 349 TYR   A CG  1 
ATOM   228  C  CD1 . TYR   A 1 34  ? 0.798   28.133  46.553  1.00 54.31  ? 349 TYR   A CD1 1 
ATOM   229  C  CD2 . TYR   A 1 34  ? 2.682   26.871  47.281  1.00 54.59  ? 349 TYR   A CD2 1 
ATOM   230  C  CE1 . TYR   A 1 34  ? 1.578   29.277  46.496  1.00 54.22  ? 349 TYR   A CE1 1 
ATOM   231  C  CE2 . TYR   A 1 34  ? 3.471   28.009  47.230  1.00 54.85  ? 349 TYR   A CE2 1 
ATOM   232  C  CZ  . TYR   A 1 34  ? 2.917   29.216  46.840  1.00 54.73  ? 349 TYR   A CZ  1 
ATOM   233  O  OH  . TYR   A 1 34  ? 3.691   30.339  46.789  1.00 55.78  ? 349 TYR   A OH  1 
ATOM   234  N  N   . VAL   A 1 35  ? -2.372  24.382  47.767  1.00 54.23  ? 350 VAL   A N   1 
ATOM   235  C  CA  . VAL   A 1 35  ? -3.300  23.273  47.641  1.00 55.13  ? 350 VAL   A CA  1 
ATOM   236  C  C   . VAL   A 1 35  ? -3.375  22.872  46.169  1.00 54.15  ? 350 VAL   A C   1 
ATOM   237  O  O   . VAL   A 1 35  ? -3.462  23.728  45.290  1.00 52.06  ? 350 VAL   A O   1 
ATOM   238  C  CB  . VAL   A 1 35  ? -4.684  23.632  48.221  1.00 57.07  ? 350 VAL   A CB  1 
ATOM   239  C  CG1 . VAL   A 1 35  ? -5.504  24.515  47.287  1.00 58.40  ? 350 VAL   A CG1 1 
ATOM   240  C  CG2 . VAL   A 1 35  ? -5.479  22.388  48.589  1.00 58.06  ? 350 VAL   A CG2 1 
ATOM   241  N  N   . ASN   A 1 36  ? -3.324  21.558  45.913  1.00 54.23  ? 351 ASN   A N   1 
ATOM   242  C  CA  . ASN   A 1 36  ? -3.427  21.026  44.564  1.00 54.08  ? 351 ASN   A CA  1 
ATOM   243  C  C   . ASN   A 1 36  ? -4.912  20.852  44.239  1.00 54.72  ? 351 ASN   A C   1 
ATOM   244  O  O   . ASN   A 1 36  ? -5.761  21.071  45.102  1.00 55.30  ? 351 ASN   A O   1 
ATOM   245  C  CB  . ASN   A 1 36  ? -2.549  19.785  44.415  1.00 53.24  ? 351 ASN   A CB  1 
ATOM   246  C  CG  . ASN   A 1 36  ? -3.184  18.524  44.952  1.00 53.34  ? 351 ASN   A CG  1 
ATOM   247  O  OD1 . ASN   A 1 36  ? -4.397  18.471  45.179  1.00 53.23  ? 351 ASN   A OD1 1 
ATOM   248  N  ND2 . ASN   A 1 36  ? -2.385  17.482  45.129  1.00 53.77  ? 351 ASN   A ND2 1 
ATOM   249  N  N   . PRO   A 1 37  ? -5.284  20.471  42.993  1.00 54.89  ? 352 PRO   A N   1 
ATOM   250  C  CA  . PRO   A 1 37  ? -6.688  20.380  42.603  1.00 55.27  ? 352 PRO   A CA  1 
ATOM   251  C  C   . PRO   A 1 37  ? -7.535  19.454  43.473  1.00 55.98  ? 352 PRO   A C   1 
ATOM   252  O  O   . PRO   A 1 37  ? -8.717  19.720  43.681  1.00 56.87  ? 352 PRO   A O   1 
ATOM   253  C  CB  . PRO   A 1 37  ? -6.630  19.878  41.161  1.00 55.25  ? 352 PRO   A CB  1 
ATOM   254  C  CG  . PRO   A 1 37  ? -5.251  20.297  40.690  1.00 55.27  ? 352 PRO   A CG  1 
ATOM   255  C  CD  . PRO   A 1 37  ? -4.372  20.143  41.887  1.00 55.29  ? 352 PRO   A CD  1 
ATOM   256  N  N   . HIS   A 1 38  ? -6.924  18.371  43.974  1.00 56.45  ? 353 HIS   A N   1 
ATOM   257  C  CA  . HIS   A 1 38  ? -7.637  17.357  44.738  1.00 56.65  ? 353 HIS   A CA  1 
ATOM   258  C  C   . HIS   A 1 38  ? -7.750  17.745  46.214  1.00 55.24  ? 353 HIS   A C   1 
ATOM   259  O  O   . HIS   A 1 38  ? -8.376  17.026  46.988  1.00 54.92  ? 353 HIS   A O   1 
ATOM   260  C  CB  . HIS   A 1 38  ? -6.987  15.980  44.543  1.00 57.80  ? 353 HIS   A CB  1 
ATOM   261  C  CG  . HIS   A 1 38  ? -7.379  15.298  43.272  1.00 59.38  ? 353 HIS   A CG  1 
ATOM   262  N  ND1 . HIS   A 1 38  ? -7.298  13.933  43.104  1.00 60.65  ? 353 HIS   A ND1 1 
ATOM   263  C  CD2 . HIS   A 1 38  ? -7.852  15.784  42.116  1.00 60.10  ? 353 HIS   A CD2 1 
ATOM   264  C  CE1 . HIS   A 1 38  ? -7.710  13.616  41.885  1.00 61.17  ? 353 HIS   A CE1 1 
ATOM   265  N  NE2 . HIS   A 1 38  ? -8.051  14.726  41.267  1.00 60.61  ? 353 HIS   A NE2 1 
ATOM   266  N  N   . GLY   A 1 39  ? -7.141  18.871  46.605  1.00 54.21  ? 354 GLY   A N   1 
ATOM   267  C  CA  . GLY   A 1 39  ? -7.346  19.434  47.930  1.00 52.62  ? 354 GLY   A CA  1 
ATOM   268  C  C   . GLY   A 1 39  ? -6.184  19.151  48.880  1.00 51.52  ? 354 GLY   A C   1 
ATOM   269  O  O   . GLY   A 1 39  ? -6.190  19.639  50.006  1.00 50.73  ? 354 GLY   A O   1 
ATOM   270  N  N   . TYR   A 1 40  ? -5.186  18.384  48.423  1.00 51.55  ? 355 TYR   A N   1 
ATOM   271  C  CA  . TYR   A 1 40  ? -4.038  18.040  49.248  1.00 52.30  ? 355 TYR   A CA  1 
ATOM   272  C  C   . TYR   A 1 40  ? -3.100  19.242  49.337  1.00 51.57  ? 355 TYR   A C   1 
ATOM   273  O  O   . TYR   A 1 40  ? -2.879  19.938  48.349  1.00 51.15  ? 355 TYR   A O   1 
ATOM   274  C  CB  . TYR   A 1 40  ? -3.291  16.825  48.690  1.00 53.94  ? 355 TYR   A CB  1 
ATOM   275  C  CG  . TYR   A 1 40  ? -4.073  15.519  48.730  1.00 55.19  ? 355 TYR   A CG  1 
ATOM   276  C  CD1 . TYR   A 1 40  ? -5.030  15.227  47.764  1.00 55.78  ? 355 TYR   A CD1 1 
ATOM   277  C  CD2 . TYR   A 1 40  ? -3.844  14.570  49.721  1.00 55.57  ? 355 TYR   A CD2 1 
ATOM   278  C  CE1 . TYR   A 1 40  ? -5.745  14.041  47.790  1.00 56.44  ? 355 TYR   A CE1 1 
ATOM   279  C  CE2 . TYR   A 1 40  ? -4.551  13.379  49.758  1.00 55.68  ? 355 TYR   A CE2 1 
ATOM   280  C  CZ  . TYR   A 1 40  ? -5.504  13.113  48.789  1.00 55.77  ? 355 TYR   A CZ  1 
ATOM   281  O  OH  . TYR   A 1 40  ? -6.208  11.944  48.810  1.00 54.18  ? 355 TYR   A OH  1 
ATOM   282  N  N   . VAL   A 1 41  ? -2.535  19.451  50.532  1.00 51.12  ? 356 VAL   A N   1 
ATOM   283  C  CA  . VAL   A 1 41  ? -1.712  20.613  50.819  1.00 51.22  ? 356 VAL   A CA  1 
ATOM   284  C  C   . VAL   A 1 41  ? -0.243  20.232  50.656  1.00 52.24  ? 356 VAL   A C   1 
ATOM   285  O  O   . VAL   A 1 41  ? 0.197   19.219  51.195  1.00 53.27  ? 356 VAL   A O   1 
ATOM   286  C  CB  . VAL   A 1 41  ? -2.006  21.129  52.241  1.00 51.12  ? 356 VAL   A CB  1 
ATOM   287  C  CG1 . VAL   A 1 41  ? -1.179  22.362  52.590  1.00 51.12  ? 356 VAL   A CG1 1 
ATOM   288  C  CG2 . VAL   A 1 41  ? -3.492  21.408  52.443  1.00 51.12  ? 356 VAL   A CG2 1 
ATOM   289  N  N   . HIS   A 1 42  ? 0.502   21.060  49.912  1.00 53.10  ? 357 HIS   A N   1 
ATOM   290  C  CA  . HIS   A 1 42  ? 1.932   20.882  49.724  1.00 54.80  ? 357 HIS   A CA  1 
ATOM   291  C  C   . HIS   A 1 42  ? 2.669   22.074  50.327  1.00 56.07  ? 357 HIS   A C   1 
ATOM   292  O  O   . HIS   A 1 42  ? 2.356   23.216  50.000  1.00 57.90  ? 357 HIS   A O   1 
ATOM   293  C  CB  . HIS   A 1 42  ? 2.269   20.768  48.233  1.00 55.58  ? 357 HIS   A CB  1 
ATOM   294  C  CG  . HIS   A 1 42  ? 1.678   19.574  47.564  1.00 55.64  ? 357 HIS   A CG  1 
ATOM   295  N  ND1 . HIS   A 1 42  ? 2.403   18.430  47.310  1.00 55.48  ? 357 HIS   A ND1 1 
ATOM   296  C  CD2 . HIS   A 1 42  ? 0.447   19.349  47.083  1.00 55.63  ? 357 HIS   A CD2 1 
ATOM   297  C  CE1 . HIS   A 1 42  ? 1.624   17.547  46.703  1.00 55.98  ? 357 HIS   A CE1 1 
ATOM   298  N  NE2 . HIS   A 1 42  ? 0.431   18.083  46.559  1.00 55.56  ? 357 HIS   A NE2 1 
ATOM   299  N  N   . GLU   A 1 43  ? 3.650   21.796  51.194  1.00 57.47  ? 358 GLU   A N   1 
ATOM   300  C  CA  . GLU   A 1 43  ? 4.454   22.836  51.818  1.00 59.99  ? 358 GLU   A CA  1 
ATOM   301  C  C   . GLU   A 1 43  ? 5.775   22.952  51.059  1.00 59.65  ? 358 GLU   A C   1 
ATOM   302  O  O   . GLU   A 1 43  ? 6.590   22.031  51.087  1.00 57.66  ? 358 GLU   A O   1 
ATOM   303  C  CB  . GLU   A 1 43  ? 4.605   22.519  53.307  1.00 63.02  ? 358 GLU   A CB  1 
ATOM   304  C  CG  . GLU   A 1 43  ? 3.267   22.471  54.042  1.00 65.76  ? 358 GLU   A CG  1 
ATOM   305  C  CD  . GLU   A 1 43  ? 3.329   22.120  55.520  1.00 69.00  ? 358 GLU   A CD  1 
ATOM   306  O  OE1 . GLU   A 1 43  ? 3.885   21.052  55.856  1.00 70.22  ? 358 GLU   A OE1 1 
ATOM   307  O  OE2 . GLU   A 1 43  ? 2.801   22.906  56.337  1.00 71.87  ? 358 GLU   A OE2 1 
ATOM   308  N  N   . THR   A 1 44  ? 5.974   24.099  50.392  1.00 61.29  ? 359 THR   A N   1 
ATOM   309  C  CA  . THR   A 1 44  ? 6.980   24.242  49.349  1.00 62.67  ? 359 THR   A CA  1 
ATOM   310  C  C   . THR   A 1 44  ? 8.125   25.140  49.816  1.00 63.21  ? 359 THR   A C   1 
ATOM   311  O  O   . THR   A 1 44  ? 8.078   25.712  50.903  1.00 63.51  ? 359 THR   A O   1 
ATOM   312  C  CB  . THR   A 1 44  ? 6.332   24.812  48.088  1.00 63.34  ? 359 THR   A CB  1 
ATOM   313  O  OG1 . THR   A 1 44  ? 5.836   26.095  48.460  1.00 63.27  ? 359 THR   A OG1 1 
ATOM   314  C  CG2 . THR   A 1 44  ? 5.213   23.937  47.551  1.00 64.04  ? 359 THR   A CG2 1 
ATOM   315  N  N   . LEU   A 1 45  ? 9.148   25.250  48.958  1.00 64.00  ? 360 LEU   A N   1 
ATOM   316  C  CA  . LEU   A 1 45  ? 10.278  26.140  49.170  1.00 65.47  ? 360 LEU   A CA  1 
ATOM   317  C  C   . LEU   A 1 45  ? 10.819  26.584  47.812  1.00 66.30  ? 360 LEU   A C   1 
ATOM   318  O  O   . LEU   A 1 45  ? 11.321  25.759  47.051  1.00 68.18  ? 360 LEU   A O   1 
ATOM   319  C  CB  . LEU   A 1 45  ? 11.349  25.416  49.985  1.00 65.93  ? 360 LEU   A CB  1 
ATOM   320  C  CG  . LEU   A 1 45  ? 12.644  26.194  50.247  1.00 67.02  ? 360 LEU   A CG  1 
ATOM   321  C  CD1 . LEU   A 1 45  ? 12.392  27.415  51.119  1.00 67.43  ? 360 LEU   A CD1 1 
ATOM   322  C  CD2 . LEU   A 1 45  ? 13.695  25.295  50.874  1.00 66.93  ? 360 LEU   A CD2 1 
ATOM   323  N  N   . THR   A 1 46  ? 10.723  27.889  47.525  1.00 66.94  ? 361 THR   A N   1 
ATOM   324  C  CA  . THR   A 1 46  ? 11.161  28.436  46.249  1.00 68.71  ? 361 THR   A CA  1 
ATOM   325  C  C   . THR   A 1 46  ? 12.674  28.649  46.273  1.00 69.39  ? 361 THR   A C   1 
ATOM   326  O  O   . THR   A 1 46  ? 13.197  29.257  47.205  1.00 68.47  ? 361 THR   A O   1 
ATOM   327  C  CB  . THR   A 1 46  ? 10.408  29.733  45.954  1.00 69.65  ? 361 THR   A CB  1 
ATOM   328  O  OG1 . THR   A 1 46  ? 10.392  30.473  47.171  1.00 72.59  ? 361 THR   A OG1 1 
ATOM   329  C  CG2 . THR   A 1 46  ? 8.985   29.482  45.491  1.00 69.27  ? 361 THR   A CG2 1 
ATOM   330  N  N   . VAL   A 1 47  ? 13.361  28.132  45.241  1.00 71.25  ? 362 VAL   A N   1 
ATOM   331  C  CA  . VAL   A 1 47  ? 14.798  28.308  45.076  1.00 72.61  ? 362 VAL   A CA  1 
ATOM   332  C  C   . VAL   A 1 47  ? 15.083  28.655  43.615  1.00 73.29  ? 362 VAL   A C   1 
ATOM   333  O  O   . VAL   A 1 47  ? 14.342  28.249  42.722  1.00 71.38  ? 362 VAL   A O   1 
ATOM   334  C  CB  . VAL   A 1 47  ? 15.621  27.076  45.508  1.00 73.30  ? 362 VAL   A CB  1 
ATOM   335  C  CG1 . VAL   A 1 47  ? 15.344  26.681  46.954  1.00 73.43  ? 362 VAL   A CG1 1 
ATOM   336  C  CG2 . VAL   A 1 47  ? 15.410  25.882  44.583  1.00 73.35  ? 362 VAL   A CG2 1 
ATOM   337  N  N   . TYR   A 1 48  ? 16.178  29.393  43.392  1.00 75.49  ? 363 TYR   A N   1 
ATOM   338  C  CA  . TYR   A 1 48  ? 16.549  29.869  42.068  1.00 75.54  ? 363 TYR   A CA  1 
ATOM   339  C  C   . TYR   A 1 48  ? 17.059  28.712  41.214  1.00 74.23  ? 363 TYR   A C   1 
ATOM   340  O  O   . TYR   A 1 48  ? 16.691  28.601  40.046  1.00 73.77  ? 363 TYR   A O   1 
ATOM   341  C  CB  . TYR   A 1 48  ? 17.636  30.948  42.115  1.00 77.23  ? 363 TYR   A CB  1 
ATOM   342  C  CG  . TYR   A 1 48  ? 17.172  32.328  42.560  1.00 78.81  ? 363 TYR   A CG  1 
ATOM   343  C  CD1 . TYR   A 1 48  ? 16.320  33.087  41.764  1.00 79.33  ? 363 TYR   A CD1 1 
ATOM   344  C  CD2 . TYR   A 1 48  ? 17.620  32.892  43.751  1.00 78.40  ? 363 TYR   A CD2 1 
ATOM   345  C  CE1 . TYR   A 1 48  ? 15.900  34.349  42.154  1.00 79.82  ? 363 TYR   A CE1 1 
ATOM   346  C  CE2 . TYR   A 1 48  ? 17.214  34.156  44.147  1.00 79.01  ? 363 TYR   A CE2 1 
ATOM   347  C  CZ  . TYR   A 1 48  ? 16.349  34.885  43.349  1.00 79.99  ? 363 TYR   A CZ  1 
ATOM   348  O  OH  . TYR   A 1 48  ? 15.944  36.130  43.736  1.00 79.98  ? 363 TYR   A OH  1 
ATOM   349  N  N   . LYS   A 1 49  ? 17.923  27.875  41.803  1.00 74.32  ? 364 LYS   A N   1 
ATOM   350  C  CA  . LYS   A 1 49  ? 18.644  26.856  41.057  1.00 74.17  ? 364 LYS   A CA  1 
ATOM   351  C  C   . LYS   A 1 49  ? 18.623  25.528  41.807  1.00 72.84  ? 364 LYS   A C   1 
ATOM   352  O  O   . LYS   A 1 49  ? 18.709  25.494  43.033  1.00 71.44  ? 364 LYS   A O   1 
ATOM   353  C  CB  . LYS   A 1 49  ? 20.090  27.304  40.823  1.00 76.00  ? 364 LYS   A CB  1 
ATOM   354  C  CG  . LYS   A 1 49  ? 20.238  28.521  39.923  1.00 77.93  ? 364 LYS   A CG  1 
ATOM   355  C  CD  . LYS   A 1 49  ? 21.675  28.997  39.751  1.00 79.57  ? 364 LYS   A CD  1 
ATOM   356  C  CE  . LYS   A 1 49  ? 21.780  30.087  38.733  1.00 81.75  ? 364 LYS   A CE  1 
ATOM   357  N  NZ  . LYS   A 1 49  ? 23.155  30.576  38.608  1.00 83.21  ? 364 LYS   A NZ  1 
ATOM   358  N  N   . ALA   A 1 50  ? 18.512  24.441  41.034  1.00 73.36  ? 365 ALA   A N   1 
ATOM   359  C  CA  . ALA   A 1 50  ? 18.626  23.086  41.546  1.00 73.77  ? 365 ALA   A CA  1 
ATOM   360  C  C   . ALA   A 1 50  ? 19.145  22.177  40.435  1.00 73.73  ? 365 ALA   A C   1 
ATOM   361  O  O   . ALA   A 1 50  ? 18.981  22.485  39.256  1.00 73.82  ? 365 ALA   A O   1 
ATOM   362  C  CB  . ALA   A 1 50  ? 17.290  22.615  42.072  1.00 74.46  ? 365 ALA   A CB  1 
ATOM   363  N  N   . SER   A 1 51  ? 19.773  21.063  40.828  1.00 73.58  ? 366 SER   A N   1 
ATOM   364  C  CA  . SER   A 1 51  ? 20.361  20.127  39.882  1.00 74.72  ? 366 SER   A CA  1 
ATOM   365  C  C   . SER   A 1 51  ? 20.239  18.701  40.415  1.00 72.01  ? 366 SER   A C   1 
ATOM   366  O  O   . SER   A 1 51  ? 19.854  18.501  41.565  1.00 70.74  ? 366 SER   A O   1 
ATOM   367  C  CB  . SER   A 1 51  ? 21.795  20.499  39.578  1.00 76.95  ? 366 SER   A CB  1 
ATOM   368  O  OG  . SER   A 1 51  ? 22.536  20.713  40.772  1.00 78.11  ? 366 SER   A OG  1 
ATOM   369  N  N   . ASN   A 1 52  ? 20.570  17.725  39.556  1.00 70.21  ? 367 ASN   A N   1 
ATOM   370  C  CA  . ASN   A 1 52  ? 20.346  16.308  39.813  1.00 67.76  ? 367 ASN   A CA  1 
ATOM   371  C  C   . ASN   A 1 52  ? 18.845  16.026  39.791  1.00 66.37  ? 367 ASN   A C   1 
ATOM   372  O  O   . ASN   A 1 52  ? 18.335  15.303  40.644  1.00 65.17  ? 367 ASN   A O   1 
ATOM   373  C  CB  . ASN   A 1 52  ? 20.972  15.826  41.120  1.00 66.59  ? 367 ASN   A CB  1 
ATOM   374  C  CG  . ASN   A 1 52  ? 22.473  15.993  41.171  1.00 66.22  ? 367 ASN   A CG  1 
ATOM   375  O  OD1 . ASN   A 1 52  ? 23.069  15.828  42.241  1.00 66.19  ? 367 ASN   A OD1 1 
ATOM   376  N  ND2 . ASN   A 1 52  ? 23.106  16.314  40.052  1.00 65.96  ? 367 ASN   A ND2 1 
ATOM   377  N  N   . LEU   A 1 53  ? 18.154  16.604  38.800  1.00 64.79  ? 368 LEU   A N   1 
ATOM   378  C  CA  . LEU   A 1 53  ? 16.716  16.448  38.663  1.00 62.76  ? 368 LEU   A CA  1 
ATOM   379  C  C   . LEU   A 1 53  ? 16.388  16.076  37.221  1.00 60.97  ? 368 LEU   A C   1 
ATOM   380  O  O   . LEU   A 1 53  ? 16.796  16.772  36.295  1.00 60.54  ? 368 LEU   A O   1 
ATOM   381  C  CB  . LEU   A 1 53  ? 15.999  17.735  39.069  1.00 62.03  ? 368 LEU   A CB  1 
ATOM   382  C  CG  . LEU   A 1 53  ? 16.151  18.173  40.530  1.00 61.68  ? 368 LEU   A CG  1 
ATOM   383  C  CD1 . LEU   A 1 53  ? 15.519  19.539  40.729  1.00 61.30  ? 368 LEU   A CD1 1 
ATOM   384  C  CD2 . LEU   A 1 53  ? 15.546  17.166  41.494  1.00 61.54  ? 368 LEU   A CD2 1 
ATOM   385  N  N   . ASN   A 1 54  ? 15.655  14.971  37.049  1.00 59.26  ? 369 ASN   A N   1 
ATOM   386  C  CA  . ASN   A 1 54  ? 15.045  14.648  35.772  1.00 59.33  ? 369 ASN   A CA  1 
ATOM   387  C  C   . ASN   A 1 54  ? 13.656  15.275  35.727  1.00 59.17  ? 369 ASN   A C   1 
ATOM   388  O  O   . ASN   A 1 54  ? 12.842  15.038  36.616  1.00 58.87  ? 369 ASN   A O   1 
ATOM   389  C  CB  . ASN   A 1 54  ? 14.959  13.143  35.537  1.00 59.63  ? 369 ASN   A CB  1 
ATOM   390  C  CG  . ASN   A 1 54  ? 16.311  12.471  35.538  1.00 58.90  ? 369 ASN   A CG  1 
ATOM   391  O  OD1 . ASN   A 1 54  ? 16.508  11.483  36.253  1.00 58.94  ? 369 ASN   A OD1 1 
ATOM   392  N  ND2 . ASN   A 1 54  ? 17.244  12.966  34.738  1.00 58.27  ? 369 ASN   A ND2 1 
ATOM   393  N  N   . LEU   A 1 55  ? 13.404  16.087  34.693  1.00 60.50  ? 370 LEU   A N   1 
ATOM   394  C  CA  . LEU   A 1 55  ? 12.079  16.632  34.447  1.00 60.80  ? 370 LEU   A CA  1 
ATOM   395  C  C   . LEU   A 1 55  ? 11.246  15.584  33.716  1.00 60.27  ? 370 LEU   A C   1 
ATOM   396  O  O   . LEU   A 1 55  ? 11.790  14.642  33.143  1.00 61.94  ? 370 LEU   A O   1 
ATOM   397  C  CB  . LEU   A 1 55  ? 12.167  17.933  33.651  1.00 61.15  ? 370 LEU   A CB  1 
ATOM   398  C  CG  . LEU   A 1 55  ? 12.903  19.092  34.330  1.00 61.41  ? 370 LEU   A CG  1 
ATOM   399  C  CD1 . LEU   A 1 55  ? 12.844  20.325  33.445  1.00 61.92  ? 370 LEU   A CD1 1 
ATOM   400  C  CD2 . LEU   A 1 55  ? 12.343  19.396  35.712  1.00 61.74  ? 370 LEU   A CD2 1 
ATOM   401  N  N   . ILE   A 1 56  ? 9.922   15.767  33.746  1.00 58.88  ? 371 ILE   A N   1 
ATOM   402  C  CA  . ILE   A 1 56  ? 8.994   14.748  33.286  1.00 58.91  ? 371 ILE   A CA  1 
ATOM   403  C  C   . ILE   A 1 56  ? 7.674   15.413  32.899  1.00 59.09  ? 371 ILE   A C   1 
ATOM   404  O  O   . ILE   A 1 56  ? 7.026   16.041  33.734  1.00 58.70  ? 371 ILE   A O   1 
ATOM   405  C  CB  . ILE   A 1 56  ? 8.835   13.649  34.357  1.00 58.63  ? 371 ILE   A CB  1 
ATOM   406  C  CG1 . ILE   A 1 56  ? 7.478   12.940  34.271  1.00 58.01  ? 371 ILE   A CG1 1 
ATOM   407  C  CG2 . ILE   A 1 56  ? 9.089   14.204  35.761  1.00 59.92  ? 371 ILE   A CG2 1 
ATOM   408  C  CD1 . ILE   A 1 56  ? 7.207   11.978  35.414  1.00 57.96  ? 371 ILE   A CD1 1 
ATOM   409  N  N   . GLY   A 1 57  ? 7.300   15.268  31.620  1.00 61.31  ? 372 GLY   A N   1 
ATOM   410  C  CA  . GLY   A 1 57  ? 6.084   15.856  31.078  1.00 62.84  ? 372 GLY   A CA  1 
ATOM   411  C  C   . GLY   A 1 57  ? 6.347   17.234  30.474  1.00 64.82  ? 372 GLY   A C   1 
ATOM   412  O  O   . GLY   A 1 57  ? 7.444   17.774  30.603  1.00 64.87  ? 372 GLY   A O   1 
ATOM   413  N  N   . ARG   A 1 58  ? 5.327   17.785  29.806  1.00 68.62  ? 373 ARG   A N   1 
ATOM   414  C  CA  . ARG   A 1 58  ? 5.371   19.151  29.308  1.00 71.50  ? 373 ARG   A CA  1 
ATOM   415  C  C   . ARG   A 1 58  ? 5.133   20.120  30.461  1.00 67.94  ? 373 ARG   A C   1 
ATOM   416  O  O   . ARG   A 1 58  ? 4.542   19.746  31.472  1.00 69.21  ? 373 ARG   A O   1 
ATOM   417  C  CB  . ARG   A 1 58  ? 4.260   19.436  28.291  1.00 78.40  ? 373 ARG   A CB  1 
ATOM   418  C  CG  . ARG   A 1 58  ? 4.311   18.647  26.992  1.00 85.08  ? 373 ARG   A CG  1 
ATOM   419  C  CD  . ARG   A 1 58  ? 3.139   19.044  26.109  1.00 92.54  ? 373 ARG   A CD  1 
ATOM   420  N  NE  . ARG   A 1 58  ? 3.108   18.340  24.822  1.00 99.76  ? 373 ARG   A NE  1 
ATOM   421  C  CZ  . ARG   A 1 58  ? 2.187   18.508  23.873  1.00 104.76 ? 373 ARG   A CZ  1 
ATOM   422  N  NH1 . ARG   A 1 58  ? 1.183   19.355  24.048  1.00 106.35 ? 373 ARG   A NH1 1 
ATOM   423  N  NH2 . ARG   A 1 58  ? 2.271   17.822  22.745  1.00 105.08 ? 373 ARG   A NH2 1 
ATOM   424  N  N   . PRO   A 1 59  ? 5.575   21.393  30.350  1.00 64.53  ? 374 PRO   A N   1 
ATOM   425  C  CA  . PRO   A 1 59  ? 5.074   22.442  31.228  1.00 62.73  ? 374 PRO   A CA  1 
ATOM   426  C  C   . PRO   A 1 59  ? 3.565   22.638  31.090  1.00 60.62  ? 374 PRO   A C   1 
ATOM   427  O  O   . PRO   A 1 59  ? 3.045   22.677  29.977  1.00 59.76  ? 374 PRO   A O   1 
ATOM   428  C  CB  . PRO   A 1 59  ? 5.873   23.679  30.813  1.00 62.17  ? 374 PRO   A CB  1 
ATOM   429  C  CG  . PRO   A 1 59  ? 7.085   23.122  30.086  1.00 62.58  ? 374 PRO   A CG  1 
ATOM   430  C  CD  . PRO   A 1 59  ? 6.613   21.867  29.422  1.00 63.43  ? 374 PRO   A CD  1 
ATOM   431  N  N   . SER   A 1 60  ? 2.874   22.728  32.233  1.00 59.46  ? 375 SER   A N   1 
ATOM   432  C  CA  . SER   A 1 60  ? 1.443   22.984  32.274  1.00 58.52  ? 375 SER   A CA  1 
ATOM   433  C  C   . SER   A 1 60  ? 1.167   24.184  33.174  1.00 57.48  ? 375 SER   A C   1 
ATOM   434  O  O   . SER   A 1 60  ? 1.948   24.469  34.078  1.00 56.72  ? 375 SER   A O   1 
ATOM   435  C  CB  . SER   A 1 60  ? 0.684   21.767  32.745  1.00 58.43  ? 375 SER   A CB  1 
ATOM   436  O  OG  . SER   A 1 60  ? -0.680  22.078  33.000  1.00 57.61  ? 375 SER   A OG  1 
ATOM   437  N  N   . THR   A 1 61  ? 0.053   24.877  32.908  1.00 58.43  ? 376 THR   A N   1 
ATOM   438  C  CA  . THR   A 1 61  ? -0.382  26.004  33.721  1.00 59.54  ? 376 THR   A CA  1 
ATOM   439  C  C   . THR   A 1 61  ? -1.732  25.698  34.369  1.00 60.76  ? 376 THR   A C   1 
ATOM   440  O  O   . THR   A 1 61  ? -2.381  26.603  34.890  1.00 59.97  ? 376 THR   A O   1 
ATOM   441  C  CB  . THR   A 1 61  ? -0.448  27.266  32.859  1.00 58.74  ? 376 THR   A CB  1 
ATOM   442  O  OG1 . THR   A 1 61  ? -1.247  26.942  31.726  1.00 58.86  ? 376 THR   A OG1 1 
ATOM   443  C  CG2 . THR   A 1 61  ? 0.921   27.730  32.397  1.00 58.38  ? 376 THR   A CG2 1 
ATOM   444  N  N   . GLU   A 1 62  ? -2.148  24.423  34.340  1.00 63.07  ? 377 GLU   A N   1 
ATOM   445  C  CA  . GLU   A 1 62  ? -3.374  23.996  34.994  1.00 64.58  ? 377 GLU   A CA  1 
ATOM   446  C  C   . GLU   A 1 62  ? -3.201  24.127  36.505  1.00 63.74  ? 377 GLU   A C   1 
ATOM   447  O  O   . GLU   A 1 62  ? -2.433  23.380  37.109  1.00 61.80  ? 377 GLU   A O   1 
ATOM   448  C  CB  . GLU   A 1 62  ? -3.725  22.548  34.646  1.00 67.25  ? 377 GLU   A CB  1 
ATOM   449  C  CG  . GLU   A 1 62  ? -4.995  22.046  35.331  1.00 70.04  ? 377 GLU   A CG  1 
ATOM   450  C  CD  . GLU   A 1 62  ? -5.003  20.559  35.645  1.00 72.35  ? 377 GLU   A CD  1 
ATOM   451  O  OE1 . GLU   A 1 62  ? -4.950  19.746  34.697  1.00 73.88  ? 377 GLU   A OE1 1 
ATOM   452  O  OE2 . GLU   A 1 62  ? -5.056  20.211  36.846  1.00 72.09  ? 377 GLU   A OE2 1 
ATOM   453  N  N   . HIS   A 1 63  ? -3.927  25.085  37.096  1.00 63.85  ? 378 HIS   A N   1 
ATOM   454  C  CA  . HIS   A 1 63  ? -3.920  25.307  38.533  1.00 63.31  ? 378 HIS   A CA  1 
ATOM   455  C  C   . HIS   A 1 63  ? -2.494  25.602  38.992  1.00 61.87  ? 378 HIS   A C   1 
ATOM   456  O  O   . HIS   A 1 63  ? -1.997  24.976  39.925  1.00 62.26  ? 378 HIS   A O   1 
ATOM   457  C  CB  . HIS   A 1 63  ? -4.569  24.118  39.254  1.00 63.75  ? 378 HIS   A CB  1 
ATOM   458  C  CG  . HIS   A 1 63  ? -4.967  24.391  40.669  1.00 64.78  ? 378 HIS   A CG  1 
ATOM   459  N  ND1 . HIS   A 1 63  ? -4.198  25.109  41.559  1.00 64.97  ? 378 HIS   A ND1 1 
ATOM   460  C  CD2 . HIS   A 1 63  ? -6.059  24.016  41.345  1.00 64.84  ? 378 HIS   A CD2 1 
ATOM   461  C  CE1 . HIS   A 1 63  ? -4.820  25.166  42.727  1.00 64.76  ? 378 HIS   A CE1 1 
ATOM   462  N  NE2 . HIS   A 1 63  ? -5.952  24.508  42.619  1.00 65.37  ? 378 HIS   A NE2 1 
ATOM   463  N  N   . SER   A 1 64  ? -1.846  26.563  38.323  1.00 60.26  ? 379 SER   A N   1 
ATOM   464  C  CA  . SER   A 1 64  ? -0.494  26.967  38.672  1.00 59.25  ? 379 SER   A CA  1 
ATOM   465  C  C   . SER   A 1 64  ? -0.533  27.828  39.931  1.00 58.47  ? 379 SER   A C   1 
ATOM   466  O  O   . SER   A 1 64  ? -1.402  28.686  40.072  1.00 58.61  ? 379 SER   A O   1 
ATOM   467  C  CB  . SER   A 1 64  ? 0.179   27.692  37.535  1.00 59.55  ? 379 SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 64  ? 1.541   27.960  37.844  1.00 59.01  ? 379 SER   A OG  1 
ATOM   469  N  N   . TRP   A 1 65  ? 0.424   27.584  40.833  1.00 57.67  ? 380 TRP   A N   1 
ATOM   470  C  CA  . TRP   A 1 65  ? 0.479   28.256  42.122  1.00 56.61  ? 380 TRP   A CA  1 
ATOM   471  C  C   . TRP   A 1 65  ? 1.128   29.631  41.991  1.00 56.64  ? 380 TRP   A C   1 
ATOM   472  O  O   . TRP   A 1 65  ? 0.976   30.471  42.876  1.00 56.96  ? 380 TRP   A O   1 
ATOM   473  C  CB  . TRP   A 1 65  ? 1.236   27.385  43.133  1.00 55.85  ? 380 TRP   A CB  1 
ATOM   474  C  CG  . TRP   A 1 65  ? 0.562   26.072  43.428  1.00 54.56  ? 380 TRP   A CG  1 
ATOM   475  C  CD1 . TRP   A 1 65  ? -0.771  25.793  43.343  1.00 54.56  ? 380 TRP   A CD1 1 
ATOM   476  C  CD2 . TRP   A 1 65  ? 1.200   24.852  43.862  1.00 53.93  ? 380 TRP   A CD2 1 
ATOM   477  N  NE1 . TRP   A 1 65  ? -1.008  24.490  43.690  1.00 55.35  ? 380 TRP   A NE1 1 
ATOM   478  C  CE2 . TRP   A 1 65  ? 0.179   23.888  44.014  1.00 54.73  ? 380 TRP   A CE2 1 
ATOM   479  C  CE3 . TRP   A 1 65  ? 2.522   24.482  44.134  1.00 53.48  ? 380 TRP   A CE3 1 
ATOM   480  C  CZ2 . TRP   A 1 65  ? 0.444   22.583  44.424  1.00 54.47  ? 380 TRP   A CZ2 1 
ATOM   481  C  CZ3 . TRP   A 1 65  ? 2.782   23.192  44.542  1.00 53.45  ? 380 TRP   A CZ3 1 
ATOM   482  C  CH2 . TRP   A 1 65  ? 1.756   22.257  44.683  1.00 54.00  ? 380 TRP   A CH2 1 
ATOM   483  N  N   . PHE   A 1 66  ? 1.863   29.840  40.891  1.00 56.74  ? 381 PHE   A N   1 
ATOM   484  C  CA  . PHE   A 1 66  ? 2.452   31.130  40.576  1.00 56.56  ? 381 PHE   A CA  1 
ATOM   485  C  C   . PHE   A 1 66  ? 1.926   31.577  39.215  1.00 57.55  ? 381 PHE   A C   1 
ATOM   486  O  O   . PHE   A 1 66  ? 2.505   31.232  38.188  1.00 59.56  ? 381 PHE   A O   1 
ATOM   487  C  CB  . PHE   A 1 66  ? 3.978   31.005  40.613  1.00 55.60  ? 381 PHE   A CB  1 
ATOM   488  C  CG  . PHE   A 1 66  ? 4.517   30.421  41.910  1.00 55.20  ? 381 PHE   A CG  1 
ATOM   489  C  CD1 . PHE   A 1 66  ? 4.827   31.241  42.989  1.00 55.76  ? 381 PHE   A CD1 1 
ATOM   490  C  CD2 . PHE   A 1 66  ? 4.704   29.051  42.050  1.00 55.85  ? 381 PHE   A CD2 1 
ATOM   491  C  CE1 . PHE   A 1 66  ? 5.314   30.703  44.171  1.00 56.54  ? 381 PHE   A CE1 1 
ATOM   492  C  CE2 . PHE   A 1 66  ? 5.190   28.517  43.235  1.00 56.41  ? 381 PHE   A CE2 1 
ATOM   493  C  CZ  . PHE   A 1 66  ? 5.494   29.344  44.292  1.00 56.39  ? 381 PHE   A CZ  1 
ATOM   494  N  N   . PRO   A 1 67  ? 0.802   32.331  39.155  1.00 57.58  ? 382 PRO   A N   1 
ATOM   495  C  CA  . PRO   A 1 67  ? 0.268   32.797  37.881  1.00 57.03  ? 382 PRO   A CA  1 
ATOM   496  C  C   . PRO   A 1 67  ? 1.313   33.542  37.057  1.00 56.44  ? 382 PRO   A C   1 
ATOM   497  O  O   . PRO   A 1 67  ? 2.035   34.383  37.588  1.00 55.42  ? 382 PRO   A O   1 
ATOM   498  C  CB  . PRO   A 1 67  ? -0.916  33.675  38.279  1.00 57.63  ? 382 PRO   A CB  1 
ATOM   499  C  CG  . PRO   A 1 67  ? -1.300  33.156  39.654  1.00 58.24  ? 382 PRO   A CG  1 
ATOM   500  C  CD  . PRO   A 1 67  ? -0.011  32.759  40.303  1.00 58.30  ? 382 PRO   A CD  1 
ATOM   501  N  N   . GLY   A 1 68  ? 1.386   33.201  35.764  1.00 56.54  ? 383 GLY   A N   1 
ATOM   502  C  CA  . GLY   A 1 68  ? 2.465   33.639  34.893  1.00 56.12  ? 383 GLY   A CA  1 
ATOM   503  C  C   . GLY   A 1 68  ? 3.391   32.481  34.521  1.00 55.90  ? 383 GLY   A C   1 
ATOM   504  O  O   . GLY   A 1 68  ? 3.970   32.479  33.436  1.00 55.49  ? 383 GLY   A O   1 
ATOM   505  N  N   . TYR   A 1 69  ? 3.518   31.502  35.428  1.00 55.66  ? 384 TYR   A N   1 
ATOM   506  C  CA  . TYR   A 1 69  ? 4.467   30.412  35.277  1.00 55.01  ? 384 TYR   A CA  1 
ATOM   507  C  C   . TYR   A 1 69  ? 3.743   29.105  34.967  1.00 54.43  ? 384 TYR   A C   1 
ATOM   508  O  O   . TYR   A 1 69  ? 2.574   28.938  35.310  1.00 55.77  ? 384 TYR   A O   1 
ATOM   509  C  CB  . TYR   A 1 69  ? 5.289   30.237  36.556  1.00 55.05  ? 384 TYR   A CB  1 
ATOM   510  C  CG  . TYR   A 1 69  ? 6.230   31.390  36.872  1.00 56.03  ? 384 TYR   A CG  1 
ATOM   511  C  CD1 . TYR   A 1 69  ? 5.788   32.511  37.566  1.00 56.15  ? 384 TYR   A CD1 1 
ATOM   512  C  CD2 . TYR   A 1 69  ? 7.565   31.348  36.485  1.00 56.35  ? 384 TYR   A CD2 1 
ATOM   513  C  CE1 . TYR   A 1 69  ? 6.646   33.558  37.864  1.00 56.24  ? 384 TYR   A CE1 1 
ATOM   514  C  CE2 . TYR   A 1 69  ? 8.432   32.388  36.776  1.00 56.75  ? 384 TYR   A CE2 1 
ATOM   515  C  CZ  . TYR   A 1 69  ? 7.971   33.495  37.467  1.00 56.94  ? 384 TYR   A CZ  1 
ATOM   516  O  OH  . TYR   A 1 69  ? 8.815   34.527  37.759  1.00 57.23  ? 384 TYR   A OH  1 
ATOM   517  N  N   . ALA   A 1 70  ? 4.475   28.187  34.323  1.00 53.16  ? 385 ALA   A N   1 
ATOM   518  C  CA  . ALA   A 1 70  ? 4.028   26.825  34.085  1.00 52.03  ? 385 ALA   A CA  1 
ATOM   519  C  C   . ALA   A 1 70  ? 4.923   25.867  34.865  1.00 51.50  ? 385 ALA   A C   1 
ATOM   520  O  O   . ALA   A 1 70  ? 6.101   26.153  35.064  1.00 52.49  ? 385 ALA   A O   1 
ATOM   521  C  CB  . ALA   A 1 70  ? 4.065   26.524  32.604  1.00 51.95  ? 385 ALA   A CB  1 
ATOM   522  N  N   . TRP   A 1 71  ? 4.360   24.725  35.273  1.00 50.07  ? 386 TRP   A N   1 
ATOM   523  C  CA  . TRP   A 1 71  ? 5.054   23.786  36.139  1.00 49.66  ? 386 TRP   A CA  1 
ATOM   524  C  C   . TRP   A 1 71  ? 5.345   22.487  35.394  1.00 50.45  ? 386 TRP   A C   1 
ATOM   525  O  O   . TRP   A 1 71  ? 4.504   21.993  34.646  1.00 49.82  ? 386 TRP   A O   1 
ATOM   526  C  CB  . TRP   A 1 71  ? 4.238   23.521  37.412  1.00 50.00  ? 386 TRP   A CB  1 
ATOM   527  C  CG  . TRP   A 1 71  ? 2.811   23.109  37.160  1.00 49.90  ? 386 TRP   A CG  1 
ATOM   528  C  CD1 . TRP   A 1 71  ? 1.726   23.932  37.071  1.00 49.80  ? 386 TRP   A CD1 1 
ATOM   529  C  CD2 . TRP   A 1 71  ? 2.313   21.767  36.970  1.00 49.56  ? 386 TRP   A CD2 1 
ATOM   530  N  NE1 . TRP   A 1 71  ? 0.593   23.202  36.833  1.00 49.73  ? 386 TRP   A NE1 1 
ATOM   531  C  CE2 . TRP   A 1 71  ? 0.919   21.873  36.768  1.00 49.79  ? 386 TRP   A CE2 1 
ATOM   532  C  CE3 . TRP   A 1 71  ? 2.904   20.498  36.950  1.00 49.07  ? 386 TRP   A CE3 1 
ATOM   533  C  CZ2 . TRP   A 1 71  ? 0.114   20.756  36.550  1.00 49.70  ? 386 TRP   A CZ2 1 
ATOM   534  C  CZ3 . TRP   A 1 71  ? 2.105   19.396  36.736  1.00 49.07  ? 386 TRP   A CZ3 1 
ATOM   535  C  CH2 . TRP   A 1 71  ? 0.730   19.526  36.538  1.00 49.60  ? 386 TRP   A CH2 1 
ATOM   536  N  N   . THR   A 1 72  ? 6.556   21.957  35.608  1.00 52.50  ? 387 THR   A N   1 
ATOM   537  C  CA  . THR   A 1 72  ? 6.932   20.622  35.169  1.00 54.01  ? 387 THR   A CA  1 
ATOM   538  C  C   . THR   A 1 72  ? 7.358   19.830  36.403  1.00 54.13  ? 387 THR   A C   1 
ATOM   539  O  O   . THR   A 1 72  ? 8.025   20.373  37.281  1.00 55.06  ? 387 THR   A O   1 
ATOM   540  C  CB  . THR   A 1 72  ? 8.058   20.708  34.137  1.00 54.16  ? 387 THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 72  ? 7.637   21.643  33.149  1.00 55.82  ? 387 THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 72  ? 8.357   19.372  33.481  1.00 53.58  ? 387 THR   A CG2 1 
ATOM   543  N  N   . VAL   A 1 73  ? 6.974   18.549  36.463  1.00 53.35  ? 388 VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 73  ? 7.276   17.716  37.617  1.00 53.91  ? 388 VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 73  ? 8.779   17.438  37.627  1.00 53.60  ? 388 VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 73  ? 9.401   17.364  36.570  1.00 53.96  ? 388 VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 73  ? 6.450   16.413  37.622  1.00 54.36  ? 388 VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 73  ? 6.788   15.521  38.812  1.00 54.43  ? 388 VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 73  ? 4.951   16.689  37.589  1.00 54.55  ? 388 VAL   A CG2 1 
ATOM   550  N  N   . ALA   A 1 74  ? 9.348   17.304  38.832  1.00 53.67  ? 389 ALA   A N   1 
ATOM   551  C  CA  . ALA   A 1 74  ? 10.773  17.071  39.007  1.00 54.56  ? 389 ALA   A CA  1 
ATOM   552  C  C   . ALA   A 1 74  ? 10.995  15.890  39.949  1.00 57.60  ? 389 ALA   A C   1 
ATOM   553  O  O   . ALA   A 1 74  ? 10.282  15.743  40.940  1.00 59.14  ? 389 ALA   A O   1 
ATOM   554  C  CB  . ALA   A 1 74  ? 11.434  18.324  39.534  1.00 54.26  ? 389 ALA   A CB  1 
ATOM   555  N  N   . GLN   A 1 75  ? 11.999  15.063  39.626  1.00 60.52  ? 390 GLN   A N   1 
ATOM   556  C  CA  . GLN   A 1 75  ? 12.326  13.875  40.400  1.00 62.55  ? 390 GLN   A CA  1 
ATOM   557  C  C   . GLN   A 1 75  ? 13.834  13.778  40.596  1.00 62.87  ? 390 GLN   A C   1 
ATOM   558  O  O   . GLN   A 1 75  ? 14.601  14.342  39.819  1.00 63.57  ? 390 GLN   A O   1 
ATOM   559  C  CB  . GLN   A 1 75  ? 11.911  12.594  39.679  1.00 64.74  ? 390 GLN   A CB  1 
ATOM   560  C  CG  . GLN   A 1 75  ? 10.406  12.393  39.565  1.00 66.70  ? 390 GLN   A CG  1 
ATOM   561  C  CD  . GLN   A 1 75  ? 10.041  11.197  38.713  1.00 68.35  ? 390 GLN   A CD  1 
ATOM   562  O  OE1 . GLN   A 1 75  ? 10.877  10.640  37.991  1.00 70.97  ? 390 GLN   A OE1 1 
ATOM   563  N  NE2 . GLN   A 1 75  ? 8.780   10.796  38.779  1.00 68.06  ? 390 GLN   A NE2 1 
ATOM   564  N  N   . CYS   A 1 76  ? 14.240  13.025  41.623  1.00 63.52  ? 391 CYS   A N   1 
ATOM   565  C  CA  . CYS   A 1 76  ? 15.643  12.731  41.863  1.00 65.73  ? 391 CYS   A CA  1 
ATOM   566  C  C   . CYS   A 1 76  ? 16.190  11.919  40.691  1.00 66.64  ? 391 CYS   A C   1 
ATOM   567  O  O   . CYS   A 1 76  ? 15.514  11.018  40.198  1.00 67.87  ? 391 CYS   A O   1 
ATOM   568  C  CB  . CYS   A 1 76  ? 15.816  11.966  43.172  1.00 67.05  ? 391 CYS   A CB  1 
ATOM   569  S  SG  . CYS   A 1 76  ? 17.542  11.771  43.690  1.00 68.03  ? 391 CYS   A SG  1 
ATOM   570  N  N   . LYS   A 1 77  ? 17.405  12.264  40.241  1.00 66.21  ? 392 LYS   A N   1 
ATOM   571  C  CA  . LYS   A 1 77  ? 18.111  11.484  39.235  1.00 65.82  ? 392 LYS   A CA  1 
ATOM   572  C  C   . LYS   A 1 77  ? 18.247  10.034  39.692  1.00 65.36  ? 392 LYS   A C   1 
ATOM   573  O  O   . LYS   A 1 77  ? 18.063  9.115   38.901  1.00 65.77  ? 392 LYS   A O   1 
ATOM   574  C  CB  . LYS   A 1 77  ? 19.531  11.989  38.951  1.00 66.93  ? 392 LYS   A CB  1 
ATOM   575  C  CG  . LYS   A 1 77  ? 19.730  12.803  37.681  1.00 68.88  ? 392 LYS   A CG  1 
ATOM   576  C  CD  . LYS   A 1 77  ? 21.205  12.988  37.339  1.00 70.95  ? 392 LYS   A CD  1 
ATOM   577  C  CE  . LYS   A 1 77  ? 21.448  13.512  35.955  1.00 73.16  ? 392 LYS   A CE  1 
ATOM   578  N  NZ  . LYS   A 1 77  ? 20.937  14.873  35.768  1.00 73.98  ? 392 LYS   A NZ  1 
ATOM   579  N  N   . ILE   A 1 78  ? 18.569  9.846   40.975  1.00 65.32  ? 393 ILE   A N   1 
ATOM   580  C  CA  . ILE   A 1 78  ? 19.045  8.565   41.467  1.00 65.02  ? 393 ILE   A CA  1 
ATOM   581  C  C   . ILE   A 1 78  ? 17.862  7.659   41.799  1.00 63.76  ? 393 ILE   A C   1 
ATOM   582  O  O   . ILE   A 1 78  ? 17.766  6.561   41.255  1.00 64.02  ? 393 ILE   A O   1 
ATOM   583  C  CB  . ILE   A 1 78  ? 19.985  8.764   42.672  1.00 65.58  ? 393 ILE   A CB  1 
ATOM   584  C  CG1 . ILE   A 1 78  ? 21.053  9.824   42.382  1.00 65.04  ? 393 ILE   A CG1 1 
ATOM   585  C  CG2 . ILE   A 1 78  ? 20.608  7.439   43.114  1.00 65.95  ? 393 ILE   A CG2 1 
ATOM   586  C  CD1 . ILE   A 1 78  ? 21.712  9.684   41.022  1.00 64.16  ? 393 ILE   A CD1 1 
ATOM   587  N  N   . CYS   A 1 79  ? 16.970  8.122   42.686  1.00 62.20  ? 394 CYS   A N   1 
ATOM   588  C  CA  . CYS   A 1 79  ? 15.964  7.256   43.284  1.00 60.47  ? 394 CYS   A CA  1 
ATOM   589  C  C   . CYS   A 1 79  ? 14.567  7.508   42.714  1.00 59.23  ? 394 CYS   A C   1 
ATOM   590  O  O   . CYS   A 1 79  ? 13.628  6.808   43.087  1.00 59.46  ? 394 CYS   A O   1 
ATOM   591  C  CB  . CYS   A 1 79  ? 15.963  7.389   44.804  1.00 60.69  ? 394 CYS   A CB  1 
ATOM   592  S  SG  . CYS   A 1 79  ? 15.475  9.026   45.410  1.00 60.29  ? 394 CYS   A SG  1 
ATOM   593  N  N   . ALA   A 1 80  ? 14.429  8.498   41.820  1.00 58.74  ? 395 ALA   A N   1 
ATOM   594  C  CA  . ALA   A 1 80  ? 13.156  8.824   41.187  1.00 59.00  ? 395 ALA   A CA  1 
ATOM   595  C  C   . ALA   A 1 80  ? 12.118  9.276   42.214  1.00 60.55  ? 395 ALA   A C   1 
ATOM   596  O  O   . ALA   A 1 80  ? 10.918  9.153   41.975  1.00 60.02  ? 395 ALA   A O   1 
ATOM   597  C  CB  . ALA   A 1 80  ? 12.646  7.643   40.392  1.00 57.98  ? 395 ALA   A CB  1 
ATOM   598  N  N   . SER   A 1 81  ? 12.583  9.809   43.349  1.00 61.79  ? 396 SER   A N   1 
ATOM   599  C  CA  . SER   A 1 81  ? 11.686  10.330  44.364  1.00 63.89  ? 396 SER   A CA  1 
ATOM   600  C  C   . SER   A 1 81  ? 11.244  11.731  43.949  1.00 64.81  ? 396 SER   A C   1 
ATOM   601  O  O   . SER   A 1 81  ? 12.068  12.533  43.516  1.00 64.31  ? 396 SER   A O   1 
ATOM   602  C  CB  . SER   A 1 81  ? 12.344  10.323  45.722  1.00 65.13  ? 396 SER   A CB  1 
ATOM   603  O  OG  . SER   A 1 81  ? 11.421  10.677  46.742  1.00 66.99  ? 396 SER   A OG  1 
ATOM   604  N  N   . HIS   A 1 82  ? 9.937   12.001  44.060  1.00 66.44  ? 397 HIS   A N   1 
ATOM   605  C  CA  . HIS   A 1 82  ? 9.367   13.276  43.651  1.00 68.05  ? 397 HIS   A CA  1 
ATOM   606  C  C   . HIS   A 1 82  ? 9.831   14.370  44.609  1.00 65.91  ? 397 HIS   A C   1 
ATOM   607  O  O   . HIS   A 1 82  ? 9.456   14.367  45.779  1.00 65.37  ? 397 HIS   A O   1 
ATOM   608  C  CB  . HIS   A 1 82  ? 7.837   13.186  43.583  1.00 70.83  ? 397 HIS   A CB  1 
ATOM   609  C  CG  . HIS   A 1 82  ? 7.135   14.480  43.306  1.00 74.07  ? 397 HIS   A CG  1 
ATOM   610  N  ND1 . HIS   A 1 82  ? 5.993   14.525  42.535  1.00 76.35  ? 397 HIS   A ND1 1 
ATOM   611  C  CD2 . HIS   A 1 82  ? 7.376   15.749  43.676  1.00 74.66  ? 397 HIS   A CD2 1 
ATOM   612  C  CE1 . HIS   A 1 82  ? 5.570   15.778  42.448  1.00 76.88  ? 397 HIS   A CE1 1 
ATOM   613  N  NE2 . HIS   A 1 82  ? 6.395   16.537  43.134  1.00 76.39  ? 397 HIS   A NE2 1 
ATOM   614  N  N   . ILE   A 1 83  ? 10.619  15.318  44.085  1.00 64.10  ? 398 ILE   A N   1 
ATOM   615  C  CA  . ILE   A 1 83  ? 11.195  16.384  44.887  1.00 62.15  ? 398 ILE   A CA  1 
ATOM   616  C  C   . ILE   A 1 83  ? 10.289  17.612  44.824  1.00 61.61  ? 398 ILE   A C   1 
ATOM   617  O  O   . ILE   A 1 83  ? 9.949   18.182  45.858  1.00 62.98  ? 398 ILE   A O   1 
ATOM   618  C  CB  . ILE   A 1 83  ? 12.634  16.697  44.433  1.00 61.34  ? 398 ILE   A CB  1 
ATOM   619  C  CG1 . ILE   A 1 83  ? 13.560  15.486  44.591  1.00 60.59  ? 398 ILE   A CG1 1 
ATOM   620  C  CG2 . ILE   A 1 83  ? 13.191  17.920  45.163  1.00 62.15  ? 398 ILE   A CG2 1 
ATOM   621  C  CD1 . ILE   A 1 83  ? 13.717  14.993  46.020  1.00 60.38  ? 398 ILE   A CD1 1 
ATOM   622  N  N   . GLY   A 1 84  ? 9.906   18.025  43.611  1.00 59.82  ? 399 GLY   A N   1 
ATOM   623  C  CA  . GLY   A 1 84  ? 9.053   19.191  43.465  1.00 58.49  ? 399 GLY   A CA  1 
ATOM   624  C  C   . GLY   A 1 84  ? 8.642   19.432  42.017  1.00 57.24  ? 399 GLY   A C   1 
ATOM   625  O  O   . GLY   A 1 84  ? 8.413   18.488  41.264  1.00 57.76  ? 399 GLY   A O   1 
ATOM   626  N  N   . TRP   A 1 85  ? 8.523   20.718  41.665  1.00 56.52  ? 400 TRP   A N   1 
ATOM   627  C  CA  . TRP   A 1 85  ? 8.163   21.148  40.325  1.00 56.32  ? 400 TRP   A CA  1 
ATOM   628  C  C   . TRP   A 1 85  ? 9.123   22.250  39.886  1.00 55.58  ? 400 TRP   A C   1 
ATOM   629  O  O   . TRP   A 1 85  ? 9.688   22.948  40.724  1.00 55.17  ? 400 TRP   A O   1 
ATOM   630  C  CB  . TRP   A 1 85  ? 6.709   21.643  40.290  1.00 56.81  ? 400 TRP   A CB  1 
ATOM   631  C  CG  . TRP   A 1 85  ? 5.705   20.648  40.811  1.00 58.19  ? 400 TRP   A CG  1 
ATOM   632  C  CD1 . TRP   A 1 85  ? 4.881   19.847  40.077  1.00 59.39  ? 400 TRP   A CD1 1 
ATOM   633  C  CD2 . TRP   A 1 85  ? 5.432   20.339  42.196  1.00 58.74  ? 400 TRP   A CD2 1 
ATOM   634  N  NE1 . TRP   A 1 85  ? 4.111   19.070  40.902  1.00 59.70  ? 400 TRP   A NE1 1 
ATOM   635  C  CE2 . TRP   A 1 85  ? 4.428   19.346  42.205  1.00 58.91  ? 400 TRP   A CE2 1 
ATOM   636  C  CE3 . TRP   A 1 85  ? 5.934   20.801  43.418  1.00 59.12  ? 400 TRP   A CE3 1 
ATOM   637  C  CZ2 . TRP   A 1 85  ? 3.921   18.815  43.390  1.00 59.58  ? 400 TRP   A CZ2 1 
ATOM   638  C  CZ3 . TRP   A 1 85  ? 5.435   20.271  44.588  1.00 59.54  ? 400 TRP   A CZ3 1 
ATOM   639  C  CH2 . TRP   A 1 85  ? 4.442   19.291  44.572  1.00 59.52  ? 400 TRP   A CH2 1 
ATOM   640  N  N   . LYS   A 1 86  ? 9.306   22.385  38.568  1.00 55.89  ? 401 LYS   A N   1 
ATOM   641  C  CA  . LYS   A 1 86  ? 10.090  23.469  38.001  1.00 56.00  ? 401 LYS   A CA  1 
ATOM   642  C  C   . LYS   A 1 86  ? 9.139   24.448  37.321  1.00 55.31  ? 401 LYS   A C   1 
ATOM   643  O  O   . LYS   A 1 86  ? 8.295   24.036  36.528  1.00 54.11  ? 401 LYS   A O   1 
ATOM   644  C  CB  . LYS   A 1 86  ? 11.113  22.952  36.985  1.00 56.92  ? 401 LYS   A CB  1 
ATOM   645  C  CG  . LYS   A 1 86  ? 12.062  24.017  36.449  1.00 57.87  ? 401 LYS   A CG  1 
ATOM   646  C  CD  . LYS   A 1 86  ? 12.811  23.613  35.186  1.00 58.82  ? 401 LYS   A CD  1 
ATOM   647  C  CE  . LYS   A 1 86  ? 13.561  24.763  34.595  1.00 60.45  ? 401 LYS   A CE  1 
ATOM   648  N  NZ  . LYS   A 1 86  ? 14.145  24.424  33.294  1.00 61.64  ? 401 LYS   A NZ  1 
ATOM   649  N  N   . PHE   A 1 87  ? 9.307   25.742  37.627  1.00 55.57  ? 402 PHE   A N   1 
ATOM   650  C  CA  . PHE   A 1 87  ? 8.425   26.782  37.125  1.00 55.70  ? 402 PHE   A CA  1 
ATOM   651  C  C   . PHE   A 1 87  ? 9.134   27.570  36.029  1.00 56.15  ? 402 PHE   A C   1 
ATOM   652  O  O   . PHE   A 1 87  ? 10.279  27.979  36.199  1.00 55.95  ? 402 PHE   A O   1 
ATOM   653  C  CB  . PHE   A 1 87  ? 7.961   27.650  38.297  1.00 55.97  ? 402 PHE   A CB  1 
ATOM   654  C  CG  . PHE   A 1 87  ? 6.946   26.939  39.181  1.00 56.85  ? 402 PHE   A CG  1 
ATOM   655  C  CD1 . PHE   A 1 87  ? 5.589   26.974  38.872  1.00 56.95  ? 402 PHE   A CD1 1 
ATOM   656  C  CD2 . PHE   A 1 87  ? 7.350   26.214  40.299  1.00 56.58  ? 402 PHE   A CD2 1 
ATOM   657  C  CE1 . PHE   A 1 87  ? 4.663   26.318  39.667  1.00 56.26  ? 402 PHE   A CE1 1 
ATOM   658  C  CE2 . PHE   A 1 87  ? 6.419   25.558  41.091  1.00 56.58  ? 402 PHE   A CE2 1 
ATOM   659  C  CZ  . PHE   A 1 87  ? 5.079   25.612  40.774  1.00 56.64  ? 402 PHE   A CZ  1 
ATOM   660  N  N   . THR   A 1 88  ? 8.427   27.772  34.909  1.00 57.64  ? 403 THR   A N   1 
ATOM   661  C  CA  . THR   A 1 88  ? 8.962   28.463  33.747  1.00 59.48  ? 403 THR   A CA  1 
ATOM   662  C  C   . THR   A 1 88  ? 7.980   29.549  33.316  1.00 61.84  ? 403 THR   A C   1 
ATOM   663  O  O   . THR   A 1 88  ? 6.785   29.292  33.201  1.00 62.73  ? 403 THR   A O   1 
ATOM   664  C  CB  . THR   A 1 88  ? 9.208   27.456  32.624  1.00 60.04  ? 403 THR   A CB  1 
ATOM   665  O  OG1 . THR   A 1 88  ? 8.005   26.701  32.509  1.00 60.58  ? 403 THR   A OG1 1 
ATOM   666  C  CG2 . THR   A 1 88  ? 10.372  26.527  32.917  1.00 60.11  ? 403 THR   A CG2 1 
ATOM   667  N  N   . ALA   A 1 89  ? 8.507   30.755  33.063  1.00 64.84  ? 404 ALA   A N   1 
ATOM   668  C  CA  . ALA   A 1 89  ? 7.701   31.894  32.650  1.00 66.18  ? 404 ALA   A CA  1 
ATOM   669  C  C   . ALA   A 1 89  ? 7.094   31.642  31.271  1.00 68.33  ? 404 ALA   A C   1 
ATOM   670  O  O   . ALA   A 1 89  ? 7.644   30.884  30.474  1.00 67.88  ? 404 ALA   A O   1 
ATOM   671  C  CB  . ALA   A 1 89  ? 8.549   33.146  32.651  1.00 65.87  ? 404 ALA   A CB  1 
ATOM   672  N  N   . THR   A 1 90  ? 5.957   32.296  31.004  1.00 71.84  ? 405 THR   A N   1 
ATOM   673  C  CA  . THR   A 1 90  ? 5.234   32.121  29.754  1.00 75.21  ? 405 THR   A CA  1 
ATOM   674  C  C   . THR   A 1 90  ? 5.436   33.330  28.838  1.00 81.49  ? 405 THR   A C   1 
ATOM   675  O  O   . THR   A 1 90  ? 4.963   33.315  27.704  1.00 82.66  ? 405 THR   A O   1 
ATOM   676  C  CB  . THR   A 1 90  ? 3.757   31.870  30.055  1.00 73.06  ? 405 THR   A CB  1 
ATOM   677  O  OG1 . THR   A 1 90  ? 3.323   32.972  30.846  1.00 73.28  ? 405 THR   A OG1 1 
ATOM   678  C  CG2 . THR   A 1 90  ? 3.533   30.567  30.802  1.00 71.72  ? 405 THR   A CG2 1 
ATOM   679  N  N   . LYS   A 1 91  ? 6.132   34.368  29.328  1.00 87.08  ? 406 LYS   A N   1 
ATOM   680  C  CA  . LYS   A 1 91  ? 6.507   35.514  28.512  1.00 91.74  ? 406 LYS   A CA  1 
ATOM   681  C  C   . LYS   A 1 91  ? 7.908   35.984  28.899  1.00 95.19  ? 406 LYS   A C   1 
ATOM   682  O  O   . LYS   A 1 91  ? 8.421   35.624  29.957  1.00 94.22  ? 406 LYS   A O   1 
ATOM   683  C  CB  . LYS   A 1 91  ? 5.501   36.662  28.660  1.00 93.48  ? 406 LYS   A CB  1 
ATOM   684  C  CG  . LYS   A 1 91  ? 4.120   36.419  28.059  1.00 94.95  ? 406 LYS   A CG  1 
ATOM   685  C  CD  . LYS   A 1 91  ? 2.992   37.020  28.887  1.00 96.56  ? 406 LYS   A CD  1 
ATOM   686  C  CE  . LYS   A 1 91  ? 2.767   36.252  30.155  1.00 97.44  ? 406 LYS   A CE  1 
ATOM   687  N  NZ  . LYS   A 1 91  ? 2.119   37.074  31.179  1.00 98.16  ? 406 LYS   A NZ  1 
ATOM   688  N  N   . LYS   A 1 92  ? 8.500   36.814  28.030  1.00 98.86  ? 407 LYS   A N   1 
ATOM   689  C  CA  . LYS   A 1 92  ? 9.889   37.239  28.145  1.00 101.18 ? 407 LYS   A CA  1 
ATOM   690  C  C   . LYS   A 1 92  ? 10.077  38.264  29.265  1.00 99.45  ? 407 LYS   A C   1 
ATOM   691  O  O   . LYS   A 1 92  ? 11.173  38.380  29.810  1.00 98.10  ? 407 LYS   A O   1 
ATOM   692  C  CB  . LYS   A 1 92  ? 10.368  37.830  26.811  1.00 103.65 ? 407 LYS   A CB  1 
ATOM   693  C  CG  . LYS   A 1 92  ? 11.089  36.873  25.864  1.00 105.42 ? 407 LYS   A CG  1 
ATOM   694  C  CD  . LYS   A 1 92  ? 12.612  36.963  25.916  1.00 107.08 ? 407 LYS   A CD  1 
ATOM   695  C  CE  . LYS   A 1 92  ? 13.230  36.523  27.209  1.00 107.85 ? 407 LYS   A CE  1 
ATOM   696  N  NZ  . LYS   A 1 92  ? 13.250  35.065  27.352  1.00 108.17 ? 407 LYS   A NZ  1 
ATOM   697  N  N   . ASP   A 1 93  ? 9.013   39.001  29.606  1.00 99.17  ? 408 ASP   A N   1 
ATOM   698  C  CA  . ASP   A 1 93  ? 9.132   40.192  30.435  1.00 99.17  ? 408 ASP   A CA  1 
ATOM   699  C  C   . ASP   A 1 93  ? 9.242   39.846  31.922  1.00 97.19  ? 408 ASP   A C   1 
ATOM   700  O  O   . ASP   A 1 93  ? 9.678   40.683  32.710  1.00 96.57  ? 408 ASP   A O   1 
ATOM   701  C  CB  . ASP   A 1 93  ? 7.994   41.167  30.169  1.00 100.44 ? 408 ASP   A CB  1 
ATOM   702  C  CG  . ASP   A 1 93  ? 6.587   40.616  30.355  1.00 101.19 ? 408 ASP   A CG  1 
ATOM   703  O  OD1 . ASP   A 1 93  ? 6.236   39.652  29.641  1.00 101.03 ? 408 ASP   A OD1 1 
ATOM   704  O  OD2 . ASP   A 1 93  ? 5.853   41.159  31.208  1.00 100.93 ? 408 ASP   A OD2 1 
ATOM   705  N  N   . MET   A 1 94  ? 8.851   38.623  32.306  1.00 94.30  ? 409 MET   A N   1 
ATOM   706  C  CA  . MET   A 1 94  ? 8.804   38.235  33.708  1.00 90.74  ? 409 MET   A CA  1 
ATOM   707  C  C   . MET   A 1 94  ? 10.218  38.035  34.250  1.00 86.21  ? 409 MET   A C   1 
ATOM   708  O  O   . MET   A 1 94  ? 11.172  37.907  33.487  1.00 86.07  ? 409 MET   A O   1 
ATOM   709  C  CB  . MET   A 1 94  ? 7.999   36.945  33.891  1.00 91.52  ? 409 MET   A CB  1 
ATOM   710  C  CG  . MET   A 1 94  ? 6.543   37.071  33.484  1.00 93.44  ? 409 MET   A CG  1 
ATOM   711  S  SD  . MET   A 1 94  ? 5.707   35.479  33.338  1.00 95.50  ? 409 MET   A SD  1 
ATOM   712  C  CE  . MET   A 1 94  ? 5.900   34.855  35.013  1.00 94.86  ? 409 MET   A CE  1 
ATOM   713  N  N   . SER   A 1 95  ? 10.330  38.017  35.583  1.00 81.41  ? 410 SER   A N   1 
ATOM   714  C  CA  . SER   A 1 95  ? 11.599  37.828  36.265  1.00 79.19  ? 410 SER   A CA  1 
ATOM   715  C  C   . SER   A 1 95  ? 11.419  37.361  37.708  1.00 78.95  ? 410 SER   A C   1 
ATOM   716  O  O   . SER   A 1 95  ? 10.783  38.059  38.495  1.00 79.11  ? 410 SER   A O   1 
ATOM   717  C  CB  . SER   A 1 95  ? 12.414  39.091  36.218  1.00 79.05  ? 410 SER   A CB  1 
ATOM   718  O  OG  . SER   A 1 95  ? 13.679  38.902  36.838  1.00 79.16  ? 410 SER   A OG  1 
ATOM   719  N  N   . PRO   A 1 96  ? 11.972  36.195  38.126  1.00 78.26  ? 411 PRO   A N   1 
ATOM   720  C  CA  . PRO   A 1 96  ? 12.839  35.373  37.284  1.00 77.86  ? 411 PRO   A CA  1 
ATOM   721  C  C   . PRO   A 1 96  ? 12.091  34.581  36.213  1.00 77.49  ? 411 PRO   A C   1 
ATOM   722  O  O   . PRO   A 1 96  ? 10.877  34.403  36.297  1.00 77.01  ? 411 PRO   A O   1 
ATOM   723  C  CB  . PRO   A 1 96  ? 13.532  34.454  38.287  1.00 77.12  ? 411 PRO   A CB  1 
ATOM   724  C  CG  . PRO   A 1 96  ? 12.502  34.309  39.392  1.00 77.44  ? 411 PRO   A CG  1 
ATOM   725  C  CD  . PRO   A 1 96  ? 11.775  35.618  39.466  1.00 77.91  ? 411 PRO   A CD  1 
ATOM   726  N  N   . GLN   A 1 97  ? 12.840  34.112  35.207  1.00 75.99  ? 412 GLN   A N   1 
ATOM   727  C  CA  . GLN   A 1 97  ? 12.279  33.378  34.082  1.00 74.43  ? 412 GLN   A CA  1 
ATOM   728  C  C   . GLN   A 1 97  ? 12.021  31.925  34.474  1.00 72.29  ? 412 GLN   A C   1 
ATOM   729  O  O   . GLN   A 1 97  ? 11.100  31.300  33.952  1.00 68.89  ? 412 GLN   A O   1 
ATOM   730  C  CB  . GLN   A 1 97  ? 13.201  33.465  32.864  1.00 74.29  ? 412 GLN   A CB  1 
ATOM   731  C  CG  . GLN   A 1 97  ? 13.100  34.782  32.101  1.00 74.54  ? 412 GLN   A CG  1 
ATOM   732  C  CD  . GLN   A 1 97  ? 11.854  34.885  31.248  1.00 74.51  ? 412 GLN   A CD  1 
ATOM   733  O  OE1 . GLN   A 1 97  ? 10.955  35.691  31.512  1.00 75.21  ? 412 GLN   A OE1 1 
ATOM   734  N  NE2 . GLN   A 1 97  ? 11.785  34.062  30.210  1.00 72.69  ? 412 GLN   A NE2 1 
ATOM   735  N  N   . LYS   A 1 98  ? 12.845  31.390  35.384  1.00 72.83  ? 413 LYS   A N   1 
ATOM   736  C  CA  . LYS   A 1 98  ? 12.674  30.026  35.857  1.00 73.65  ? 413 LYS   A CA  1 
ATOM   737  C  C   . LYS   A 1 98  ? 13.162  29.913  37.301  1.00 71.87  ? 413 LYS   A C   1 
ATOM   738  O  O   . LYS   A 1 98  ? 14.106  30.592  37.703  1.00 71.70  ? 413 LYS   A O   1 
ATOM   739  C  CB  . LYS   A 1 98  ? 13.372  29.051  34.899  1.00 76.20  ? 413 LYS   A CB  1 
ATOM   740  C  CG  . LYS   A 1 98  ? 14.890  29.172  34.791  1.00 78.26  ? 413 LYS   A CG  1 
ATOM   741  C  CD  . LYS   A 1 98  ? 15.668  28.361  35.822  1.00 80.21  ? 413 LYS   A CD  1 
ATOM   742  C  CE  . LYS   A 1 98  ? 17.108  28.756  35.908  1.00 81.28  ? 413 LYS   A CE  1 
ATOM   743  N  NZ  . LYS   A 1 98  ? 17.793  28.040  36.987  1.00 81.67  ? 413 LYS   A NZ  1 
ATOM   744  N  N   . PHE   A 1 99  ? 12.486  29.050  38.069  1.00 69.34  ? 414 PHE   A N   1 
ATOM   745  C  CA  . PHE   A 1 99  ? 12.855  28.739  39.441  1.00 66.88  ? 414 PHE   A CA  1 
ATOM   746  C  C   . PHE   A 1 99  ? 12.266  27.371  39.784  1.00 66.97  ? 414 PHE   A C   1 
ATOM   747  O  O   . PHE   A 1 99  ? 11.687  26.717  38.918  1.00 67.64  ? 414 PHE   A O   1 
ATOM   748  C  CB  . PHE   A 1 99  ? 12.375  29.856  40.375  1.00 65.42  ? 414 PHE   A CB  1 
ATOM   749  C  CG  . PHE   A 1 99  ? 10.864  29.910  40.558  1.00 64.69  ? 414 PHE   A CG  1 
ATOM   750  C  CD1 . PHE   A 1 99  ? 10.065  30.644  39.686  1.00 63.22  ? 414 PHE   A CD1 1 
ATOM   751  C  CD2 . PHE   A 1 99  ? 10.246  29.222  41.598  1.00 63.68  ? 414 PHE   A CD2 1 
ATOM   752  C  CE1 . PHE   A 1 99  ? 8.689   30.685  39.852  1.00 62.39  ? 414 PHE   A CE1 1 
ATOM   753  C  CE2 . PHE   A 1 99  ? 8.869   29.268  41.758  1.00 62.89  ? 414 PHE   A CE2 1 
ATOM   754  C  CZ  . PHE   A 1 99  ? 8.095   29.999  40.887  1.00 62.39  ? 414 PHE   A CZ  1 
ATOM   755  N  N   . TRP   A 1 100 ? 12.417  26.947  41.045  1.00 66.28  ? 415 TRP   A N   1 
ATOM   756  C  CA  . TRP   A 1 100 ? 11.975  25.628  41.474  1.00 66.44  ? 415 TRP   A CA  1 
ATOM   757  C  C   . TRP   A 1 100 ? 11.168  25.737  42.766  1.00 67.01  ? 415 TRP   A C   1 
ATOM   758  O  O   . TRP   A 1 100 ? 11.528  26.499  43.660  1.00 67.65  ? 415 TRP   A O   1 
ATOM   759  C  CB  . TRP   A 1 100 ? 13.183  24.700  41.667  1.00 65.91  ? 415 TRP   A CB  1 
ATOM   760  C  CG  . TRP   A 1 100 ? 14.140  24.675  40.504  1.00 66.54  ? 415 TRP   A CG  1 
ATOM   761  C  CD1 . TRP   A 1 100 ? 15.028  25.651  40.156  1.00 66.88  ? 415 TRP   A CD1 1 
ATOM   762  C  CD2 . TRP   A 1 100 ? 14.332  23.604  39.553  1.00 65.95  ? 415 TRP   A CD2 1 
ATOM   763  N  NE1 . TRP   A 1 100 ? 15.741  25.277  39.049  1.00 66.93  ? 415 TRP   A NE1 1 
ATOM   764  C  CE2 . TRP   A 1 100 ? 15.342  24.025  38.660  1.00 66.55  ? 415 TRP   A CE2 1 
ATOM   765  C  CE3 . TRP   A 1 100 ? 13.752  22.343  39.368  1.00 65.68  ? 415 TRP   A CE3 1 
ATOM   766  C  CZ2 . TRP   A 1 100 ? 15.779  23.230  37.603  1.00 66.26  ? 415 TRP   A CZ2 1 
ATOM   767  C  CZ3 . TRP   A 1 100 ? 14.190  21.556  38.325  1.00 65.76  ? 415 TRP   A CZ3 1 
ATOM   768  C  CH2 . TRP   A 1 100 ? 15.190  21.995  37.457  1.00 66.14  ? 415 TRP   A CH2 1 
ATOM   769  N  N   . GLY   A 1 101 ? 10.077  24.963  42.846  1.00 66.37  ? 416 GLY   A N   1 
ATOM   770  C  CA  . GLY   A 1 101 ? 9.295   24.820  44.064  1.00 65.70  ? 416 GLY   A CA  1 
ATOM   771  C  C   . GLY   A 1 101 ? 9.402   23.396  44.604  1.00 65.85  ? 416 GLY   A C   1 
ATOM   772  O  O   . GLY   A 1 101 ? 8.868   22.467  44.004  1.00 65.30  ? 416 GLY   A O   1 
ATOM   773  N  N   . LEU   A 1 102 ? 10.093  23.243  45.742  1.00 65.66  ? 417 LEU   A N   1 
ATOM   774  C  CA  . LEU   A 1 102 ? 10.470  21.938  46.261  1.00 64.74  ? 417 LEU   A CA  1 
ATOM   775  C  C   . LEU   A 1 102 ? 9.648   21.609  47.503  1.00 62.86  ? 417 LEU   A C   1 
ATOM   776  O  O   . LEU   A 1 102 ? 9.364   22.491  48.308  1.00 62.36  ? 417 LEU   A O   1 
ATOM   777  C  CB  . LEU   A 1 102 ? 11.961  21.935  46.590  1.00 65.97  ? 417 LEU   A CB  1 
ATOM   778  C  CG  . LEU   A 1 102 ? 12.899  22.473  45.505  1.00 67.48  ? 417 LEU   A CG  1 
ATOM   779  C  CD1 . LEU   A 1 102 ? 14.342  22.250  45.921  1.00 68.16  ? 417 LEU   A CD1 1 
ATOM   780  C  CD2 . LEU   A 1 102 ? 12.630  21.848  44.145  1.00 68.07  ? 417 LEU   A CD2 1 
ATOM   781  N  N   . THR   A 1 103 ? 9.303   20.324  47.652  1.00 62.20  ? 418 THR   A N   1 
ATOM   782  C  CA  . THR   A 1 103 ? 8.645   19.821  48.847  1.00 61.19  ? 418 THR   A CA  1 
ATOM   783  C  C   . THR   A 1 103 ? 9.675   19.768  49.975  1.00 61.82  ? 418 THR   A C   1 
ATOM   784  O  O   . THR   A 1 103 ? 10.709  19.117  49.840  1.00 60.15  ? 418 THR   A O   1 
ATOM   785  C  CB  . THR   A 1 103 ? 8.038   18.449  48.549  1.00 60.28  ? 418 THR   A CB  1 
ATOM   786  O  OG1 . THR   A 1 103 ? 7.179   18.643  47.428  1.00 58.32  ? 418 THR   A OG1 1 
ATOM   787  C  CG2 . THR   A 1 103 ? 7.247   17.883  49.716  1.00 59.82  ? 418 THR   A CG2 1 
ATOM   788  N  N   . ARG   A 1 104 ? 9.385   20.466  51.080  1.00 64.11  ? 419 ARG   A N   1 
ATOM   789  C  CA  . ARG   A 1 104 ? 10.324  20.595  52.184  1.00 66.63  ? 419 ARG   A CA  1 
ATOM   790  C  C   . ARG   A 1 104 ? 10.521  19.244  52.867  1.00 67.23  ? 419 ARG   A C   1 
ATOM   791  O  O   . ARG   A 1 104 ? 11.615  18.944  53.344  1.00 68.26  ? 419 ARG   A O   1 
ATOM   792  C  CB  . ARG   A 1 104 ? 9.860   21.643  53.202  1.00 68.44  ? 419 ARG   A CB  1 
ATOM   793  C  CG  . ARG   A 1 104 ? 9.802   23.058  52.644  1.00 70.73  ? 419 ARG   A CG  1 
ATOM   794  C  CD  . ARG   A 1 104 ? 9.732   24.128  53.727  1.00 72.74  ? 419 ARG   A CD  1 
ATOM   795  N  NE  . ARG   A 1 104 ? 8.560   23.995  54.601  1.00 73.84  ? 419 ARG   A NE  1 
ATOM   796  C  CZ  . ARG   A 1 104 ? 7.417   24.670  54.490  1.00 74.60  ? 419 ARG   A CZ  1 
ATOM   797  N  NH1 . ARG   A 1 104 ? 7.187   25.447  53.445  1.00 75.00  ? 419 ARG   A NH1 1 
ATOM   798  N  NH2 . ARG   A 1 104 ? 6.479   24.530  55.412  1.00 75.02  ? 419 ARG   A NH2 1 
ATOM   799  N  N   . SER   A 1 105 ? 9.459   18.430  52.892  1.00 66.72  ? 420 SER   A N   1 
ATOM   800  C  CA  . SER   A 1 105 ? 9.501   17.115  53.511  1.00 66.50  ? 420 SER   A CA  1 
ATOM   801  C  C   . SER   A 1 105 ? 10.136  16.086  52.574  1.00 65.90  ? 420 SER   A C   1 
ATOM   802  O  O   . SER   A 1 105 ? 10.030  14.886  52.818  1.00 66.00  ? 420 SER   A O   1 
ATOM   803  C  CB  . SER   A 1 105 ? 8.117   16.689  53.936  1.00 66.94  ? 420 SER   A CB  1 
ATOM   804  O  OG  . SER   A 1 105 ? 7.223   16.677  52.831  1.00 67.40  ? 420 SER   A OG  1 
ATOM   805  N  N   . ALA   A 1 106 ? 10.801  16.558  51.510  1.00 65.97  ? 421 ALA   A N   1 
ATOM   806  C  CA  . ALA   A 1 106 ? 11.492  15.686  50.574  1.00 66.08  ? 421 ALA   A CA  1 
ATOM   807  C  C   . ALA   A 1 106 ? 12.994  15.971  50.570  1.00 68.16  ? 421 ALA   A C   1 
ATOM   808  O  O   . ALA   A 1 106 ? 13.712  15.456  49.717  1.00 69.28  ? 421 ALA   A O   1 
ATOM   809  C  CB  . ALA   A 1 106 ? 10.900  15.866  49.194  1.00 65.17  ? 421 ALA   A CB  1 
ATOM   810  N  N   . LEU   A 1 107 ? 13.468  16.775  51.532  1.00 71.17  ? 422 LEU   A N   1 
ATOM   811  C  CA  . LEU   A 1 107 ? 14.848  17.237  51.541  1.00 73.01  ? 422 LEU   A CA  1 
ATOM   812  C  C   . LEU   A 1 107 ? 15.449  17.083  52.935  1.00 75.73  ? 422 LEU   A C   1 
ATOM   813  O  O   . LEU   A 1 107 ? 14.726  16.901  53.913  1.00 77.25  ? 422 LEU   A O   1 
ATOM   814  C  CB  . LEU   A 1 107 ? 14.890  18.690  51.069  1.00 73.31  ? 422 LEU   A CB  1 
ATOM   815  C  CG  . LEU   A 1 107 ? 14.571  18.928  49.590  1.00 73.52  ? 422 LEU   A CG  1 
ATOM   816  C  CD1 . LEU   A 1 107 ? 14.407  20.410  49.305  1.00 73.76  ? 422 LEU   A CD1 1 
ATOM   817  C  CD2 . LEU   A 1 107 ? 15.647  18.336  48.696  1.00 73.49  ? 422 LEU   A CD2 1 
ATOM   818  N  N   . LEU   A 1 108 ? 16.784  17.168  53.005  1.00 77.94  ? 423 LEU   A N   1 
ATOM   819  C  CA  . LEU   A 1 108 ? 17.519  17.038  54.254  1.00 80.83  ? 423 LEU   A CA  1 
ATOM   820  C  C   . LEU   A 1 108 ? 18.634  18.070  54.413  1.00 85.20  ? 423 LEU   A C   1 
ATOM   821  O  O   . LEU   A 1 108 ? 19.446  18.236  53.507  1.00 85.59  ? 423 LEU   A O   1 
ATOM   822  C  CB  . LEU   A 1 108 ? 18.085  15.623  54.348  1.00 79.23  ? 423 LEU   A CB  1 
ATOM   823  C  CG  . LEU   A 1 108 ? 17.107  14.527  54.781  1.00 78.79  ? 423 LEU   A CG  1 
ATOM   824  C  CD1 . LEU   A 1 108 ? 17.816  13.186  54.771  1.00 79.22  ? 423 LEU   A CD1 1 
ATOM   825  C  CD2 . LEU   A 1 108 ? 16.506  14.798  56.151  1.00 78.47  ? 423 LEU   A CD2 1 
ATOM   826  N  N   . PRO   A 1 109 ? 18.725  18.785  55.562  1.00 90.92  ? 424 PRO   A N   1 
ATOM   827  C  CA  . PRO   A 1 109 ? 17.739  18.689  56.634  1.00 94.79  ? 424 PRO   A CA  1 
ATOM   828  C  C   . PRO   A 1 109 ? 16.408  19.349  56.279  1.00 101.49 ? 424 PRO   A C   1 
ATOM   829  O  O   . PRO   A 1 109 ? 16.379  20.305  55.506  1.00 105.18 ? 424 PRO   A O   1 
ATOM   830  C  CB  . PRO   A 1 109 ? 18.414  19.407  57.800  1.00 93.33  ? 424 PRO   A CB  1 
ATOM   831  C  CG  . PRO   A 1 109 ? 19.286  20.430  57.094  1.00 92.30  ? 424 PRO   A CG  1 
ATOM   832  C  CD  . PRO   A 1 109 ? 19.813  19.723  55.884  1.00 90.89  ? 424 PRO   A CD  1 
ATOM   833  N  N   . THR   A 1 110 ? 15.313  18.827  56.844  1.00 105.51 ? 425 THR   A N   1 
ATOM   834  C  CA  . THR   A 1 110 ? 14.002  19.426  56.654  1.00 108.19 ? 425 THR   A CA  1 
ATOM   835  C  C   . THR   A 1 110 ? 13.900  20.667  57.538  1.00 110.63 ? 425 THR   A C   1 
ATOM   836  O  O   . THR   A 1 110 ? 14.161  20.599  58.738  1.00 109.33 ? 425 THR   A O   1 
ATOM   837  C  CB  . THR   A 1 110 ? 12.898  18.417  56.965  1.00 108.55 ? 425 THR   A CB  1 
ATOM   838  O  OG1 . THR   A 1 110 ? 13.083  17.370  56.018  1.00 109.64 ? 425 THR   A OG1 1 
ATOM   839  C  CG2 . THR   A 1 110 ? 11.505  19.005  56.815  1.00 108.10 ? 425 THR   A CG2 1 
ATOM   840  N  N   . ILE   A 1 111 ? 13.523  21.793  56.920  1.00 114.10 ? 426 ILE   A N   1 
ATOM   841  C  CA  . ILE   A 1 111 ? 13.334  23.052  57.623  1.00 117.18 ? 426 ILE   A CA  1 
ATOM   842  C  C   . ILE   A 1 111 ? 12.123  23.777  57.006  1.00 118.32 ? 426 ILE   A C   1 
ATOM   843  O  O   . ILE   A 1 111 ? 10.990  23.434  57.414  1.00 116.98 ? 426 ILE   A O   1 
ATOM   844  C  CB  . ILE   A 1 111 ? 14.619  23.907  57.598  1.00 116.67 ? 426 ILE   A CB  1 
ATOM   845  C  CG1 . ILE   A 1 111 ? 15.344  23.821  56.247  1.00 114.74 ? 426 ILE   A CG1 1 
ATOM   846  C  CG2 . ILE   A 1 111 ? 15.549  23.525  58.753  1.00 116.09 ? 426 ILE   A CG2 1 
ATOM   847  C  CD1 . ILE   A 1 111 ? 16.438  24.858  56.058  1.00 113.35 ? 426 ILE   A CD1 1 
ATOM   848  O  OXT . ILE   A 1 111 ? 12.348  24.649  56.139  1.00 119.62 ? 426 ILE   A OXT 1 
ATOM   849  N  N   . SER   B 1 3   ? 49.248  -53.031 7.709   1.00 112.57 ? 318 SER   B N   1 
ATOM   850  C  CA  . SER   B 1 3   ? 47.939  -52.360 7.933   1.00 112.80 ? 318 SER   B CA  1 
ATOM   851  C  C   . SER   B 1 3   ? 46.798  -53.255 7.451   1.00 111.68 ? 318 SER   B C   1 
ATOM   852  O  O   . SER   B 1 3   ? 46.433  -53.225 6.276   1.00 109.83 ? 318 SER   B O   1 
ATOM   853  C  CB  . SER   B 1 3   ? 47.897  -51.004 7.262   1.00 112.31 ? 318 SER   B CB  1 
ATOM   854  O  OG  . SER   B 1 3   ? 46.672  -50.333 7.530   1.00 111.56 ? 318 SER   B OG  1 
ATOM   855  N  N   . THR   B 1 4   ? 46.254  -54.061 8.372   1.00 109.33 ? 319 THR   B N   1 
ATOM   856  C  CA  . THR   B 1 4   ? 44.963  -54.701 8.175   1.00 106.05 ? 319 THR   B CA  1 
ATOM   857  C  C   . THR   B 1 4   ? 43.889  -53.718 8.633   1.00 104.77 ? 319 THR   B C   1 
ATOM   858  O  O   . THR   B 1 4   ? 43.200  -53.966 9.618   1.00 104.96 ? 319 THR   B O   1 
ATOM   859  C  CB  . THR   B 1 4   ? 44.883  -56.027 8.934   1.00 104.18 ? 319 THR   B CB  1 
ATOM   860  O  OG1 . THR   B 1 4   ? 45.150  -55.741 10.303  1.00 104.21 ? 319 THR   B OG1 1 
ATOM   861  C  CG2 . THR   B 1 4   ? 45.873  -57.065 8.434   1.00 102.06 ? 319 THR   B CG2 1 
ATOM   862  N  N   . SER   B 1 5   ? 43.772  -52.594 7.915   1.00 103.75 ? 320 SER   B N   1 
ATOM   863  C  CA  . SER   B 1 5   ? 42.925  -51.492 8.339   1.00 104.07 ? 320 SER   B CA  1 
ATOM   864  C  C   . SER   B 1 5   ? 42.418  -50.725 7.121   1.00 102.98 ? 320 SER   B C   1 
ATOM   865  O  O   . SER   B 1 5   ? 43.168  -50.497 6.174   1.00 101.50 ? 320 SER   B O   1 
ATOM   866  C  CB  . SER   B 1 5   ? 43.663  -50.582 9.292   1.00 104.42 ? 320 SER   B CB  1 
ATOM   867  O  OG  . SER   B 1 5   ? 42.799  -49.593 9.833   1.00 104.27 ? 320 SER   B OG  1 
ATOM   868  N  N   . LEU   B 1 6   ? 41.138  -50.332 7.173   1.00 102.82 ? 321 LEU   B N   1 
ATOM   869  C  CA  . LEU   B 1 6   ? 40.477  -49.615 6.093   1.00 101.82 ? 321 LEU   B CA  1 
ATOM   870  C  C   . LEU   B 1 6   ? 39.779  -48.385 6.665   1.00 99.48  ? 321 LEU   B C   1 
ATOM   871  O  O   . LEU   B 1 6   ? 39.191  -48.453 7.743   1.00 98.68  ? 321 LEU   B O   1 
ATOM   872  C  CB  . LEU   B 1 6   ? 39.488  -50.550 5.399   1.00 102.85 ? 321 LEU   B CB  1 
ATOM   873  C  CG  . LEU   B 1 6   ? 40.102  -51.671 4.553   1.00 103.52 ? 321 LEU   B CG  1 
ATOM   874  C  CD1 . LEU   B 1 6   ? 39.055  -52.708 4.189   1.00 103.11 ? 321 LEU   B CD1 1 
ATOM   875  C  CD2 . LEU   B 1 6   ? 40.751  -51.112 3.299   1.00 104.02 ? 321 LEU   B CD2 1 
ATOM   876  N  N   . SER   B 1 7   ? 39.834  -47.273 5.919   1.00 96.91  ? 322 SER   B N   1 
ATOM   877  C  CA  . SER   B 1 7   ? 39.414  -45.979 6.432   1.00 95.58  ? 322 SER   B CA  1 
ATOM   878  C  C   . SER   B 1 7   ? 38.534  -45.246 5.424   1.00 93.81  ? 322 SER   B C   1 
ATOM   879  O  O   . SER   B 1 7   ? 38.525  -45.577 4.241   1.00 94.75  ? 322 SER   B O   1 
ATOM   880  C  CB  . SER   B 1 7   ? 40.610  -45.140 6.809   1.00 95.55  ? 322 SER   B CB  1 
ATOM   881  O  OG  . SER   B 1 7   ? 41.285  -45.688 7.933   1.00 96.14  ? 322 SER   B OG  1 
ATOM   882  N  N   . CYS   B 1 8   ? 37.799  -44.245 5.927   1.00 91.67  ? 323 CYS   B N   1 
ATOM   883  C  CA  . CYS   B 1 8   ? 37.036  -43.323 5.102   1.00 90.18  ? 323 CYS   B CA  1 
ATOM   884  C  C   . CYS   B 1 8   ? 37.984  -42.624 4.132   1.00 89.30  ? 323 CYS   B C   1 
ATOM   885  O  O   . CYS   B 1 8   ? 39.085  -42.243 4.516   1.00 88.32  ? 323 CYS   B O   1 
ATOM   886  C  CB  . CYS   B 1 8   ? 36.310  -42.302 5.973   1.00 89.25  ? 323 CYS   B CB  1 
ATOM   887  S  SG  . CYS   B 1 8   ? 35.452  -41.005 5.040   1.00 86.41  ? 323 CYS   B SG  1 
ATOM   888  N  N   . LYS   B 1 9   ? 37.554  -42.473 2.874   1.00 89.49  ? 324 LYS   B N   1 
ATOM   889  C  CA  . LYS   B 1 9   ? 38.378  -41.842 1.855   1.00 90.33  ? 324 LYS   B CA  1 
ATOM   890  C  C   . LYS   B 1 9   ? 38.382  -40.328 2.049   1.00 87.52  ? 324 LYS   B C   1 
ATOM   891  O  O   . LYS   B 1 9   ? 39.390  -39.675 1.787   1.00 84.81  ? 324 LYS   B O   1 
ATOM   892  C  CB  . LYS   B 1 9   ? 37.895  -42.208 0.446   1.00 93.48  ? 324 LYS   B CB  1 
ATOM   893  C  CG  . LYS   B 1 9   ? 38.614  -41.491 -0.696  1.00 96.00  ? 324 LYS   B CG  1 
ATOM   894  C  CD  . LYS   B 1 9   ? 38.460  -42.162 -2.056  1.00 98.20  ? 324 LYS   B CD  1 
ATOM   895  C  CE  . LYS   B 1 9   ? 39.338  -43.367 -2.201  1.00 99.80  ? 324 LYS   B CE  1 
ATOM   896  N  NZ  . LYS   B 1 9   ? 38.905  -44.249 -3.289  1.00 100.41 ? 324 LYS   B NZ  1 
ATOM   897  N  N   . GLN   B 1 10  ? 37.253  -39.779 2.511   1.00 87.80  ? 325 GLN   B N   1 
ATOM   898  C  CA  . GLN   B 1 10  ? 37.046  -38.340 2.497   1.00 88.62  ? 325 GLN   B CA  1 
ATOM   899  C  C   . GLN   B 1 10  ? 37.743  -37.690 3.692   1.00 86.55  ? 325 GLN   B C   1 
ATOM   900  O  O   . GLN   B 1 10  ? 38.436  -36.691 3.522   1.00 88.77  ? 325 GLN   B O   1 
ATOM   901  C  CB  . GLN   B 1 10  ? 35.558  -37.998 2.456   1.00 90.77  ? 325 GLN   B CB  1 
ATOM   902  C  CG  . GLN   B 1 10  ? 35.274  -36.628 1.850   1.00 93.86  ? 325 GLN   B CG  1 
ATOM   903  C  CD  . GLN   B 1 10  ? 33.864  -36.141 2.104   1.00 97.90  ? 325 GLN   B CD  1 
ATOM   904  O  OE1 . GLN   B 1 10  ? 32.883  -36.759 1.675   1.00 101.33 ? 325 GLN   B OE1 1 
ATOM   905  N  NE2 . GLN   B 1 10  ? 33.747  -35.024 2.808   1.00 98.98  ? 325 GLN   B NE2 1 
ATOM   906  N  N   . CYS   B 1 11  ? 37.553  -38.251 4.895   1.00 84.35  ? 326 CYS   B N   1 
ATOM   907  C  CA  . CYS   B 1 11  ? 38.128  -37.675 6.103   1.00 83.81  ? 326 CYS   B CA  1 
ATOM   908  C  C   . CYS   B 1 11  ? 39.442  -38.370 6.457   1.00 85.00  ? 326 CYS   B C   1 
ATOM   909  O  O   . CYS   B 1 11  ? 40.338  -37.736 7.008   1.00 84.97  ? 326 CYS   B O   1 
ATOM   910  C  CB  . CYS   B 1 11  ? 37.134  -37.685 7.259   1.00 82.35  ? 326 CYS   B CB  1 
ATOM   911  S  SG  . CYS   B 1 11  ? 36.845  -39.325 7.968   1.00 81.98  ? 326 CYS   B SG  1 
ATOM   912  N  N   . GLN   B 1 12  ? 39.528  -39.680 6.179   1.00 86.81  ? 327 GLN   B N   1 
ATOM   913  C  CA  . GLN   B 1 12  ? 40.791  -40.407 6.096   1.00 88.49  ? 327 GLN   B CA  1 
ATOM   914  C  C   . GLN   B 1 12  ? 41.243  -40.933 7.459   1.00 90.76  ? 327 GLN   B C   1 
ATOM   915  O  O   . GLN   B 1 12  ? 41.864  -41.992 7.525   1.00 91.01  ? 327 GLN   B O   1 
ATOM   916  C  CB  . GLN   B 1 12  ? 41.912  -39.596 5.443   1.00 88.24  ? 327 GLN   B CB  1 
ATOM   917  C  CG  . GLN   B 1 12  ? 41.580  -39.112 4.036   1.00 88.53  ? 327 GLN   B CG  1 
ATOM   918  C  CD  . GLN   B 1 12  ? 42.778  -38.552 3.304   1.00 89.91  ? 327 GLN   B CD  1 
ATOM   919  O  OE1 . GLN   B 1 12  ? 42.847  -37.356 2.997   1.00 90.58  ? 327 GLN   B OE1 1 
ATOM   920  N  NE2 . GLN   B 1 12  ? 43.742  -39.416 3.020   1.00 90.31  ? 327 GLN   B NE2 1 
ATOM   921  N  N   . GLU   B 1 13  ? 40.937  -40.201 8.536   1.00 93.96  ? 328 GLU   B N   1 
ATOM   922  C  CA  . GLU   B 1 13  ? 41.442  -40.521 9.863   1.00 96.59  ? 328 GLU   B CA  1 
ATOM   923  C  C   . GLU   B 1 13  ? 40.706  -41.721 10.463  1.00 95.52  ? 328 GLU   B C   1 
ATOM   924  O  O   . GLU   B 1 13  ? 41.236  -42.387 11.350  1.00 95.28  ? 328 GLU   B O   1 
ATOM   925  C  CB  . GLU   B 1 13  ? 41.292  -39.298 10.770  1.00 98.67  ? 328 GLU   B CB  1 
ATOM   926  C  CG  . GLU   B 1 13  ? 39.847  -39.004 11.166  1.00 100.10 ? 328 GLU   B CG  1 
ATOM   927  C  CD  . GLU   B 1 13  ? 39.596  -37.612 11.720  1.00 101.66 ? 328 GLU   B CD  1 
ATOM   928  O  OE1 . GLU   B 1 13  ? 40.528  -36.780 11.718  1.00 101.98 ? 328 GLU   B OE1 1 
ATOM   929  O  OE2 . GLU   B 1 13  ? 38.453  -37.362 12.159  1.00 102.20 ? 328 GLU   B OE2 1 
ATOM   930  N  N   . THR   B 1 14  ? 39.492  -41.990 9.967   1.00 93.77  ? 329 THR   B N   1 
ATOM   931  C  CA  . THR   B 1 14  ? 38.547  -42.873 10.632  1.00 91.76  ? 329 THR   B CA  1 
ATOM   932  C  C   . THR   B 1 14  ? 38.719  -44.307 10.137  1.00 89.78  ? 329 THR   B C   1 
ATOM   933  O  O   . THR   B 1 14  ? 38.500  -44.577 8.960   1.00 89.79  ? 329 THR   B O   1 
ATOM   934  C  CB  . THR   B 1 14  ? 37.136  -42.360 10.344  1.00 91.88  ? 329 THR   B CB  1 
ATOM   935  O  OG1 . THR   B 1 14  ? 37.149  -40.980 10.697  1.00 92.13  ? 329 THR   B OG1 1 
ATOM   936  C  CG2 . THR   B 1 14  ? 36.065  -43.094 11.132  1.00 91.97  ? 329 THR   B CG2 1 
ATOM   937  N  N   . GLU   B 1 15  ? 39.083  -45.222 11.046  1.00 87.99  ? 330 GLU   B N   1 
ATOM   938  C  CA  . GLU   B 1 15  ? 39.031  -46.646 10.756  1.00 88.09  ? 330 GLU   B CA  1 
ATOM   939  C  C   . GLU   B 1 15  ? 37.569  -47.083 10.725  1.00 87.37  ? 330 GLU   B C   1 
ATOM   940  O  O   . GLU   B 1 15  ? 36.823  -46.821 11.666  1.00 87.19  ? 330 GLU   B O   1 
ATOM   941  C  CB  . GLU   B 1 15  ? 39.793  -47.498 11.774  1.00 89.12  ? 330 GLU   B CB  1 
ATOM   942  C  CG  . GLU   B 1 15  ? 39.578  -48.999 11.581  1.00 89.90  ? 330 GLU   B CG  1 
ATOM   943  C  CD  . GLU   B 1 15  ? 40.490  -49.902 12.391  1.00 90.62  ? 330 GLU   B CD  1 
ATOM   944  O  OE1 . GLU   B 1 15  ? 41.724  -49.778 12.242  1.00 92.61  ? 330 GLU   B OE1 1 
ATOM   945  O  OE2 . GLU   B 1 15  ? 39.970  -50.740 13.158  1.00 88.66  ? 330 GLU   B OE2 1 
ATOM   946  N  N   . ILE   B 1 16  ? 37.176  -47.750 9.634   1.00 86.27  ? 331 ILE   B N   1 
ATOM   947  C  CA  . ILE   B 1 16  ? 35.836  -48.296 9.499   1.00 85.41  ? 331 ILE   B CA  1 
ATOM   948  C  C   . ILE   B 1 16  ? 35.875  -49.769 9.897   1.00 87.59  ? 331 ILE   B C   1 
ATOM   949  O  O   . ILE   B 1 16  ? 35.128  -50.191 10.778  1.00 89.64  ? 331 ILE   B O   1 
ATOM   950  C  CB  . ILE   B 1 16  ? 35.299  -48.101 8.068   1.00 84.22  ? 331 ILE   B CB  1 
ATOM   951  C  CG1 . ILE   B 1 16  ? 35.406  -46.641 7.607   1.00 83.71  ? 331 ILE   B CG1 1 
ATOM   952  C  CG2 . ILE   B 1 16  ? 33.869  -48.628 7.941   1.00 83.78  ? 331 ILE   B CG2 1 
ATOM   953  C  CD1 . ILE   B 1 16  ? 34.609  -45.655 8.444   1.00 83.53  ? 331 ILE   B CD1 1 
ATOM   954  N  N   . THR   B 1 17  ? 36.753  -50.535 9.237   1.00 89.21  ? 332 THR   B N   1 
ATOM   955  C  CA  . THR   B 1 17  ? 36.894  -51.959 9.498   1.00 88.83  ? 332 THR   B CA  1 
ATOM   956  C  C   . THR   B 1 17  ? 38.333  -52.388 9.210   1.00 90.14  ? 332 THR   B C   1 
ATOM   957  O  O   . THR   B 1 17  ? 39.168  -51.568 8.830   1.00 86.53  ? 332 THR   B O   1 
ATOM   958  C  CB  . THR   B 1 17  ? 35.876  -52.729 8.654   1.00 87.11  ? 332 THR   B CB  1 
ATOM   959  O  OG1 . THR   B 1 17  ? 35.877  -54.067 9.145   1.00 85.30  ? 332 THR   B OG1 1 
ATOM   960  C  CG2 . THR   B 1 17  ? 36.196  -52.709 7.169   1.00 86.53  ? 332 THR   B CG2 1 
ATOM   961  N  N   . THR   B 1 18  ? 38.602  -53.685 9.410   1.00 93.68  ? 333 THR   B N   1 
ATOM   962  C  CA  . THR   B 1 18  ? 39.910  -54.274 9.167   1.00 93.87  ? 333 THR   B CA  1 
ATOM   963  C  C   . THR   B 1 18  ? 39.782  -55.349 8.088   1.00 94.88  ? 333 THR   B C   1 
ATOM   964  O  O   . THR   B 1 18  ? 38.719  -55.941 7.918   1.00 95.13  ? 333 THR   B O   1 
ATOM   965  C  CB  . THR   B 1 18  ? 40.463  -54.840 10.475  1.00 93.67  ? 333 THR   B CB  1 
ATOM   966  O  OG1 . THR   B 1 18  ? 39.479  -55.744 10.966  1.00 93.37  ? 333 THR   B OG1 1 
ATOM   967  C  CG2 . THR   B 1 18  ? 40.726  -53.761 11.511  1.00 93.81  ? 333 THR   B CG2 1 
ATOM   968  N  N   . LYS   B 1 19  ? 40.888  -55.591 7.374   1.00 96.44  ? 334 LYS   B N   1 
ATOM   969  C  CA  . LYS   B 1 19  ? 40.933  -56.518 6.251   1.00 97.54  ? 334 LYS   B CA  1 
ATOM   970  C  C   . LYS   B 1 19  ? 40.450  -57.911 6.656   1.00 95.50  ? 334 LYS   B C   1 
ATOM   971  O  O   . LYS   B 1 19  ? 39.774  -58.576 5.874   1.00 94.26  ? 334 LYS   B O   1 
ATOM   972  C  CB  . LYS   B 1 19  ? 42.357  -56.570 5.685   1.00 100.12 ? 334 LYS   B CB  1 
ATOM   973  C  CG  . LYS   B 1 19  ? 42.669  -55.517 4.625   1.00 102.43 ? 334 LYS   B CG  1 
ATOM   974  C  CD  . LYS   B 1 19  ? 44.104  -54.995 4.596   1.00 105.40 ? 334 LYS   B CD  1 
ATOM   975  C  CE  . LYS   B 1 19  ? 45.187  -56.022 4.784   1.00 107.90 ? 334 LYS   B CE  1 
ATOM   976  N  NZ  . LYS   B 1 19  ? 45.273  -56.988 3.686   1.00 109.40 ? 334 LYS   B NZ  1 
ATOM   977  N  N   . ASN   B 1 20  ? 40.790  -58.346 7.876   1.00 94.12  ? 335 ASN   B N   1 
ATOM   978  C  CA  . ASN   B 1 20  ? 40.405  -59.668 8.350   1.00 93.16  ? 335 ASN   B CA  1 
ATOM   979  C  C   . ASN   B 1 20  ? 39.015  -59.616 8.991   1.00 90.07  ? 335 ASN   B C   1 
ATOM   980  O  O   . ASN   B 1 20  ? 38.749  -60.339 9.949   1.00 89.80  ? 335 ASN   B O   1 
ATOM   981  C  CB  . ASN   B 1 20  ? 41.483  -60.291 9.237   1.00 94.72  ? 335 ASN   B CB  1 
ATOM   982  C  CG  . ASN   B 1 20  ? 42.117  -59.306 10.192  1.00 96.44  ? 335 ASN   B CG  1 
ATOM   983  O  OD1 . ASN   B 1 20  ? 42.826  -58.391 9.758   1.00 96.97  ? 335 ASN   B OD1 1 
ATOM   984  N  ND2 . ASN   B 1 20  ? 41.900  -59.482 11.488  1.00 96.87  ? 335 ASN   B ND2 1 
ATOM   985  N  N   . GLU   B 1 21  ? 38.136  -58.756 8.454   1.00 87.28  ? 336 GLU   B N   1 
ATOM   986  C  CA  . GLU   B 1 21  ? 36.703  -58.830 8.699   1.00 85.82  ? 336 GLU   B CA  1 
ATOM   987  C  C   . GLU   B 1 21  ? 35.964  -59.196 7.412   1.00 83.20  ? 336 GLU   B C   1 
ATOM   988  O  O   . GLU   B 1 21  ? 34.753  -59.407 7.438   1.00 81.17  ? 336 GLU   B O   1 
ATOM   989  C  CB  . GLU   B 1 21  ? 36.151  -57.500 9.213   1.00 87.32  ? 336 GLU   B CB  1 
ATOM   990  C  CG  . GLU   B 1 21  ? 36.520  -57.197 10.662  1.00 88.34  ? 336 GLU   B CG  1 
ATOM   991  C  CD  . GLU   B 1 21  ? 35.785  -58.026 11.702  1.00 89.11  ? 336 GLU   B CD  1 
ATOM   992  O  OE1 . GLU   B 1 21  ? 34.995  -58.922 11.330  1.00 88.57  ? 336 GLU   B OE1 1 
ATOM   993  O  OE2 . GLU   B 1 21  ? 36.001  -57.760 12.902  1.00 90.79  ? 336 GLU   B OE2 1 
ATOM   994  N  N   . ILE   B 1 22  ? 36.698  -59.273 6.295   1.00 83.74  ? 337 ILE   B N   1 
ATOM   995  C  CA  . ILE   B 1 22  ? 36.106  -59.506 4.987   1.00 84.50  ? 337 ILE   B CA  1 
ATOM   996  C  C   . ILE   B 1 22  ? 35.615  -60.949 4.912   1.00 85.55  ? 337 ILE   B C   1 
ATOM   997  O  O   . ILE   B 1 22  ? 36.168  -61.832 5.565   1.00 85.32  ? 337 ILE   B O   1 
ATOM   998  C  CB  . ILE   B 1 22  ? 37.117  -59.183 3.868   1.00 83.72  ? 337 ILE   B CB  1 
ATOM   999  C  CG1 . ILE   B 1 22  ? 37.515  -57.704 3.878   1.00 84.30  ? 337 ILE   B CG1 1 
ATOM   1000 C  CG2 . ILE   B 1 22  ? 36.583  -59.605 2.497   1.00 83.50  ? 337 ILE   B CG2 1 
ATOM   1001 C  CD1 . ILE   B 1 22  ? 38.753  -57.384 3.060   1.00 84.22  ? 337 ILE   B CD1 1 
ATOM   1002 N  N   . PHE   B 1 23  ? 34.562  -61.166 4.115   1.00 87.88  ? 338 PHE   B N   1 
ATOM   1003 C  CA  . PHE   B 1 23  ? 34.062  -62.501 3.826   1.00 89.68  ? 338 PHE   B CA  1 
ATOM   1004 C  C   . PHE   B 1 23  ? 33.284  -62.462 2.512   1.00 92.08  ? 338 PHE   B C   1 
ATOM   1005 O  O   . PHE   B 1 23  ? 32.760  -61.418 2.128   1.00 94.10  ? 338 PHE   B O   1 
ATOM   1006 C  CB  . PHE   B 1 23  ? 33.212  -62.991 5.002   1.00 88.59  ? 338 PHE   B CB  1 
ATOM   1007 C  CG  . PHE   B 1 23  ? 31.782  -62.469 5.023   1.00 88.19  ? 338 PHE   B CG  1 
ATOM   1008 C  CD1 . PHE   B 1 23  ? 31.513  -61.124 5.259   1.00 87.79  ? 338 PHE   B CD1 1 
ATOM   1009 C  CD2 . PHE   B 1 23  ? 30.707  -63.331 4.825   1.00 88.06  ? 338 PHE   B CD2 1 
ATOM   1010 C  CE1 . PHE   B 1 23  ? 30.207  -60.656 5.278   1.00 88.45  ? 338 PHE   B CE1 1 
ATOM   1011 C  CE2 . PHE   B 1 23  ? 29.404  -62.858 4.852   1.00 88.44  ? 338 PHE   B CE2 1 
ATOM   1012 C  CZ  . PHE   B 1 23  ? 29.156  -61.523 5.077   1.00 88.66  ? 338 PHE   B CZ  1 
ATOM   1013 N  N   . SER   B 1 24  ? 33.219  -63.613 1.831   1.00 92.67  ? 339 SER   B N   1 
ATOM   1014 C  CA  . SER   B 1 24  ? 32.510  -63.729 0.567   1.00 93.27  ? 339 SER   B CA  1 
ATOM   1015 C  C   . SER   B 1 24  ? 31.039  -64.043 0.825   1.00 95.19  ? 339 SER   B C   1 
ATOM   1016 O  O   . SER   B 1 24  ? 30.721  -64.808 1.732   1.00 93.44  ? 339 SER   B O   1 
ATOM   1017 C  CB  . SER   B 1 24  ? 33.142  -64.777 -0.314  1.00 92.22  ? 339 SER   B CB  1 
ATOM   1018 O  OG  . SER   B 1 24  ? 32.301  -65.095 -1.414  1.00 92.29  ? 339 SER   B OG  1 
ATOM   1019 N  N   . LEU   B 1 25  ? 30.153  -63.441 0.021   1.00 99.47  ? 340 LEU   B N   1 
ATOM   1020 C  CA  . LEU   B 1 25  ? 28.734  -63.755 0.088   1.00 103.07 ? 340 LEU   B CA  1 
ATOM   1021 C  C   . LEU   B 1 25  ? 28.151  -63.856 -1.322  1.00 106.58 ? 340 LEU   B C   1 
ATOM   1022 O  O   . LEU   B 1 25  ? 26.941  -63.732 -1.499  1.00 107.48 ? 340 LEU   B O   1 
ATOM   1023 C  CB  . LEU   B 1 25  ? 28.013  -62.687 0.915   1.00 103.49 ? 340 LEU   B CB  1 
ATOM   1024 C  CG  . LEU   B 1 25  ? 27.124  -63.170 2.072   1.00 103.15 ? 340 LEU   B CG  1 
ATOM   1025 C  CD1 . LEU   B 1 25  ? 25.714  -62.615 1.924   1.00 102.95 ? 340 LEU   B CD1 1 
ATOM   1026 C  CD2 . LEU   B 1 25  ? 27.078  -64.676 2.281   1.00 102.62 ? 340 LEU   B CD2 1 
ATOM   1027 N  N   . SER   B 1 26  ? 29.012  -64.111 -2.317  1.00 108.84 ? 341 SER   B N   1 
ATOM   1028 C  CA  . SER   B 1 26  ? 28.612  -64.087 -3.715  1.00 109.47 ? 341 SER   B CA  1 
ATOM   1029 C  C   . SER   B 1 26  ? 29.491  -65.041 -4.525  1.00 108.71 ? 341 SER   B C   1 
ATOM   1030 O  O   . SER   B 1 26  ? 30.283  -65.792 -3.958  1.00 108.61 ? 341 SER   B O   1 
ATOM   1031 C  CB  . SER   B 1 26  ? 28.666  -62.676 -4.260  1.00 111.25 ? 341 SER   B CB  1 
ATOM   1032 O  OG  . SER   B 1 26  ? 27.829  -61.802 -3.514  1.00 113.35 ? 341 SER   B OG  1 
ATOM   1033 N  N   . LEU   B 1 27  ? 29.327  -65.006 -5.855  1.00 107.79 ? 342 LEU   B N   1 
ATOM   1034 C  CA  . LEU   B 1 27  ? 30.103  -65.829 -6.770  1.00 106.54 ? 342 LEU   B CA  1 
ATOM   1035 C  C   . LEU   B 1 27  ? 31.447  -65.166 -7.057  1.00 106.31 ? 342 LEU   B C   1 
ATOM   1036 O  O   . LEU   B 1 27  ? 32.470  -65.844 -7.122  1.00 107.21 ? 342 LEU   B O   1 
ATOM   1037 C  CB  . LEU   B 1 27  ? 29.306  -66.060 -8.053  1.00 104.75 ? 342 LEU   B CB  1 
ATOM   1038 C  CG  . LEU   B 1 27  ? 28.321  -67.232 -8.021  1.00 103.61 ? 342 LEU   B CG  1 
ATOM   1039 C  CD1 . LEU   B 1 27  ? 27.168  -67.015 -8.980  1.00 102.68 ? 342 LEU   B CD1 1 
ATOM   1040 C  CD2 . LEU   B 1 27  ? 29.042  -68.530 -8.346  1.00 103.57 ? 342 LEU   B CD2 1 
ATOM   1041 N  N   . SER   B 1 28  ? 31.431  -63.837 -7.219  1.00 104.42 ? 343 SER   B N   1 
ATOM   1042 C  CA  . SER   B 1 28  ? 32.642  -63.069 -7.459  1.00 103.14 ? 343 SER   B CA  1 
ATOM   1043 C  C   . SER   B 1 28  ? 33.470  -62.948 -6.179  1.00 103.13 ? 343 SER   B C   1 
ATOM   1044 O  O   . SER   B 1 28  ? 34.486  -62.257 -6.169  1.00 106.16 ? 343 SER   B O   1 
ATOM   1045 C  CB  . SER   B 1 28  ? 32.305  -61.713 -8.032  1.00 102.16 ? 343 SER   B CB  1 
ATOM   1046 O  OG  . SER   B 1 28  ? 33.477  -60.949 -8.280  1.00 103.09 ? 343 SER   B OG  1 
ATOM   1047 N  N   . GLY   B 1 29  ? 33.032  -63.625 -5.107  1.00 100.34 ? 344 GLY   B N   1 
ATOM   1048 C  CA  . GLY   B 1 29  ? 33.749  -63.635 -3.843  1.00 97.34  ? 344 GLY   B CA  1 
ATOM   1049 C  C   . GLY   B 1 29  ? 33.230  -62.540 -2.916  1.00 94.30  ? 344 GLY   B C   1 
ATOM   1050 O  O   . GLY   B 1 29  ? 32.022  -62.317 -2.838  1.00 92.79  ? 344 GLY   B O   1 
ATOM   1051 N  N   . PRO   B 1 30  ? 34.117  -61.830 -2.180  1.00 91.33  ? 345 PRO   B N   1 
ATOM   1052 C  CA  . PRO   B 1 30  ? 33.693  -60.702 -1.358  1.00 90.80  ? 345 PRO   B CA  1 
ATOM   1053 C  C   . PRO   B 1 30  ? 33.296  -59.482 -2.186  1.00 89.79  ? 345 PRO   B C   1 
ATOM   1054 O  O   . PRO   B 1 30  ? 32.341  -58.782 -1.847  1.00 90.04  ? 345 PRO   B O   1 
ATOM   1055 C  CB  . PRO   B 1 30  ? 34.900  -60.460 -0.455  1.00 90.05  ? 345 PRO   B CB  1 
ATOM   1056 C  CG  . PRO   B 1 30  ? 36.072  -60.927 -1.299  1.00 89.07  ? 345 PRO   B CG  1 
ATOM   1057 C  CD  . PRO   B 1 30  ? 35.566  -62.084 -2.104  1.00 89.33  ? 345 PRO   B CD  1 
ATOM   1058 N  N   . MET   B 1 31  ? 34.030  -59.257 -3.283  1.00 87.42  ? 346 MET   B N   1 
ATOM   1059 C  CA  . MET   B 1 31  ? 33.797  -58.132 -4.173  1.00 86.02  ? 346 MET   B CA  1 
ATOM   1060 C  C   . MET   B 1 31  ? 32.717  -58.492 -5.188  1.00 81.30  ? 346 MET   B C   1 
ATOM   1061 O  O   . MET   B 1 31  ? 32.860  -59.462 -5.928  1.00 84.63  ? 346 MET   B O   1 
ATOM   1062 C  CB  . MET   B 1 31  ? 35.063  -57.780 -4.958  1.00 89.31  ? 346 MET   B CB  1 
ATOM   1063 C  CG  . MET   B 1 31  ? 36.218  -57.289 -4.113  1.00 91.77  ? 346 MET   B CG  1 
ATOM   1064 S  SD  . MET   B 1 31  ? 37.542  -56.619 -5.139  1.00 97.13  ? 346 MET   B SD  1 
ATOM   1065 C  CE  . MET   B 1 31  ? 37.771  -57.923 -6.358  1.00 95.74  ? 346 MET   B CE  1 
ATOM   1066 N  N   . ALA   B 1 32  ? 31.650  -57.689 -5.224  1.00 75.16  ? 347 ALA   B N   1 
ATOM   1067 C  CA  . ALA   B 1 32  ? 30.613  -57.822 -6.232  1.00 70.26  ? 347 ALA   B CA  1 
ATOM   1068 C  C   . ALA   B 1 32  ? 30.352  -56.458 -6.861  1.00 66.05  ? 347 ALA   B C   1 
ATOM   1069 O  O   . ALA   B 1 32  ? 31.014  -55.479 -6.524  1.00 65.86  ? 347 ALA   B O   1 
ATOM   1070 C  CB  . ALA   B 1 32  ? 29.366  -58.399 -5.599  1.00 70.29  ? 347 ALA   B CB  1 
ATOM   1071 N  N   . ALA   B 1 33  ? 29.403  -56.416 -7.801  1.00 62.58  ? 348 ALA   B N   1 
ATOM   1072 C  CA  . ALA   B 1 33  ? 28.882  -55.164 -8.320  1.00 60.01  ? 348 ALA   B CA  1 
ATOM   1073 C  C   . ALA   B 1 33  ? 27.377  -55.305 -8.517  1.00 58.33  ? 348 ALA   B C   1 
ATOM   1074 O  O   . ALA   B 1 33  ? 26.924  -56.224 -9.196  1.00 58.45  ? 348 ALA   B O   1 
ATOM   1075 C  CB  . ALA   B 1 33  ? 29.584  -54.792 -9.605  1.00 59.66  ? 348 ALA   B CB  1 
ATOM   1076 N  N   . TYR   B 1 34  ? 26.615  -54.396 -7.898  1.00 55.82  ? 349 TYR   B N   1 
ATOM   1077 C  CA  . TYR   B 1 34  ? 25.164  -54.447 -7.939  1.00 53.41  ? 349 TYR   B CA  1 
ATOM   1078 C  C   . TYR   B 1 34  ? 24.632  -53.184 -8.603  1.00 52.13  ? 349 TYR   B C   1 
ATOM   1079 O  O   . TYR   B 1 34  ? 25.292  -52.149 -8.596  1.00 51.72  ? 349 TYR   B O   1 
ATOM   1080 C  CB  . TYR   B 1 34  ? 24.598  -54.601 -6.526  1.00 52.21  ? 349 TYR   B CB  1 
ATOM   1081 C  CG  . TYR   B 1 34  ? 25.086  -55.848 -5.806  1.00 51.34  ? 349 TYR   B CG  1 
ATOM   1082 C  CD1 . TYR   B 1 34  ? 24.427  -57.064 -5.950  1.00 51.76  ? 349 TYR   B CD1 1 
ATOM   1083 C  CD2 . TYR   B 1 34  ? 26.213  -55.812 -4.994  1.00 50.82  ? 349 TYR   B CD2 1 
ATOM   1084 C  CE1 . TYR   B 1 34  ? 24.867  -58.206 -5.300  1.00 51.65  ? 349 TYR   B CE1 1 
ATOM   1085 C  CE2 . TYR   B 1 34  ? 26.663  -56.947 -4.338  1.00 52.00  ? 349 TYR   B CE2 1 
ATOM   1086 C  CZ  . TYR   B 1 34  ? 25.990  -58.147 -4.492  1.00 52.14  ? 349 TYR   B CZ  1 
ATOM   1087 O  OH  . TYR   B 1 34  ? 26.437  -59.264 -3.845  1.00 51.78  ? 349 TYR   B OH  1 
ATOM   1088 N  N   . VAL   B 1 35  ? 23.428  -53.293 -9.170  1.00 51.91  ? 350 VAL   B N   1 
ATOM   1089 C  CA  . VAL   B 1 35  ? 22.756  -52.162 -9.780  1.00 52.45  ? 350 VAL   B CA  1 
ATOM   1090 C  C   . VAL   B 1 35  ? 21.565  -51.786 -8.901  1.00 52.07  ? 350 VAL   B C   1 
ATOM   1091 O  O   . VAL   B 1 35  ? 20.855  -52.660 -8.405  1.00 51.80  ? 350 VAL   B O   1 
ATOM   1092 C  CB  . VAL   B 1 35  ? 22.326  -52.475 -11.227 1.00 53.95  ? 350 VAL   B CB  1 
ATOM   1093 C  CG1 . VAL   B 1 35  ? 21.103  -53.383 -11.289 1.00 54.97  ? 350 VAL   B CG1 1 
ATOM   1094 C  CG2 . VAL   B 1 35  ? 22.073  -51.204 -12.023 1.00 54.73  ? 350 VAL   B CG2 1 
ATOM   1095 N  N   . ASN   B 1 36  ? 21.367  -50.476 -8.709  1.00 51.46  ? 351 ASN   B N   1 
ATOM   1096 C  CA  . ASN   B 1 36  ? 20.261  -49.970 -7.913  1.00 50.91  ? 351 ASN   B CA  1 
ATOM   1097 C  C   . ASN   B 1 36  ? 19.060  -49.781 -8.842  1.00 51.58  ? 351 ASN   B C   1 
ATOM   1098 O  O   . ASN   B 1 36  ? 19.172  -50.010 -10.045 1.00 52.16  ? 351 ASN   B O   1 
ATOM   1099 C  CB  . ASN   B 1 36  ? 20.707  -48.751 -7.109  1.00 49.53  ? 351 ASN   B CB  1 
ATOM   1100 C  CG  . ASN   B 1 36  ? 20.839  -47.499 -7.941  1.00 48.17  ? 351 ASN   B CG  1 
ATOM   1101 O  OD1 . ASN   B 1 36  ? 20.294  -47.416 -9.046  1.00 47.48  ? 351 ASN   B OD1 1 
ATOM   1102 N  ND2 . ASN   B 1 36  ? 21.530  -46.501 -7.413  1.00 48.48  ? 351 ASN   B ND2 1 
ATOM   1103 N  N   . PRO   B 1 37  ? 17.870  -49.387 -8.329  1.00 52.14  ? 352 PRO   B N   1 
ATOM   1104 C  CA  . PRO   B 1 37  ? 16.682  -49.262 -9.167  1.00 53.41  ? 352 PRO   B CA  1 
ATOM   1105 C  C   . PRO   B 1 37  ? 16.815  -48.244 -10.299 1.00 56.72  ? 352 PRO   B C   1 
ATOM   1106 O  O   . PRO   B 1 37  ? 16.209  -48.417 -11.354 1.00 58.50  ? 352 PRO   B O   1 
ATOM   1107 C  CB  . PRO   B 1 37  ? 15.580  -48.866 -8.187  1.00 53.17  ? 352 PRO   B CB  1 
ATOM   1108 C  CG  . PRO   B 1 37  ? 16.119  -49.267 -6.826  1.00 52.98  ? 352 PRO   B CG  1 
ATOM   1109 C  CD  . PRO   B 1 37  ? 17.598  -49.082 -6.916  1.00 52.61  ? 352 PRO   B CD  1 
ATOM   1110 N  N   . HIS   B 1 38  ? 17.610  -47.189 -10.070 1.00 58.90  ? 353 HIS   B N   1 
ATOM   1111 C  CA  . HIS   B 1 38  ? 17.810  -46.136 -11.055 1.00 59.78  ? 353 HIS   B CA  1 
ATOM   1112 C  C   . HIS   B 1 38  ? 18.836  -46.553 -12.109 1.00 59.90  ? 353 HIS   B C   1 
ATOM   1113 O  O   . HIS   B 1 38  ? 19.033  -45.835 -13.087 1.00 62.99  ? 353 HIS   B O   1 
ATOM   1114 C  CB  . HIS   B 1 38  ? 18.200  -44.820 -10.369 1.00 61.30  ? 353 HIS   B CB  1 
ATOM   1115 C  CG  . HIS   B 1 38  ? 17.071  -44.158 -9.651  1.00 63.56  ? 353 HIS   B CG  1 
ATOM   1116 N  ND1 . HIS   B 1 38  ? 15.752  -44.315 -10.023 1.00 64.28  ? 353 HIS   B ND1 1 
ATOM   1117 C  CD2 . HIS   B 1 38  ? 17.062  -43.338 -8.594  1.00 64.41  ? 353 HIS   B CD2 1 
ATOM   1118 C  CE1 . HIS   B 1 38  ? 14.981  -43.611 -9.209  1.00 64.62  ? 353 HIS   B CE1 1 
ATOM   1119 N  NE2 . HIS   B 1 38  ? 15.757  -43.010 -8.332  1.00 65.50  ? 353 HIS   B NE2 1 
ATOM   1120 N  N   . GLY   B 1 39  ? 19.500  -47.697 -11.902 1.00 57.54  ? 354 GLY   B N   1 
ATOM   1121 C  CA  . GLY   B 1 39  ? 20.342  -48.291 -12.927 1.00 56.32  ? 354 GLY   B CA  1 
ATOM   1122 C  C   . GLY   B 1 39  ? 21.830  -48.028 -12.700 1.00 55.20  ? 354 GLY   B C   1 
ATOM   1123 O  O   . GLY   B 1 39  ? 22.655  -48.520 -13.464 1.00 54.43  ? 354 GLY   B O   1 
ATOM   1124 N  N   . TYR   B 1 40  ? 22.172  -47.269 -11.650 1.00 54.81  ? 355 TYR   B N   1 
ATOM   1125 C  CA  . TYR   B 1 40  ? 23.563  -46.968 -11.346 1.00 55.98  ? 355 TYR   B CA  1 
ATOM   1126 C  C   . TYR   B 1 40  ? 24.211  -48.192 -10.707 1.00 54.27  ? 355 TYR   B C   1 
ATOM   1127 O  O   . TYR   B 1 40  ? 23.588  -48.882 -9.903  1.00 52.96  ? 355 TYR   B O   1 
ATOM   1128 C  CB  . TYR   B 1 40  ? 23.699  -45.755 -10.421 1.00 58.82  ? 355 TYR   B CB  1 
ATOM   1129 C  CG  . TYR   B 1 40  ? 23.234  -44.435 -11.023 1.00 62.24  ? 355 TYR   B CG  1 
ATOM   1130 C  CD1 . TYR   B 1 40  ? 21.882  -44.113 -11.086 1.00 62.80  ? 355 TYR   B CD1 1 
ATOM   1131 C  CD2 . TYR   B 1 40  ? 24.146  -43.503 -11.512 1.00 63.28  ? 355 TYR   B CD2 1 
ATOM   1132 C  CE1 . TYR   B 1 40  ? 21.449  -42.914 -11.629 1.00 62.95  ? 355 TYR   B CE1 1 
ATOM   1133 C  CE2 . TYR   B 1 40  ? 23.724  -42.299 -12.055 1.00 63.36  ? 355 TYR   B CE2 1 
ATOM   1134 C  CZ  . TYR   B 1 40  ? 22.373  -42.004 -12.113 1.00 62.72  ? 355 TYR   B CZ  1 
ATOM   1135 O  OH  . TYR   B 1 40  ? 21.940  -40.823 -12.644 1.00 61.41  ? 355 TYR   B OH  1 
ATOM   1136 N  N   . VAL   B 1 41  ? 25.478  -48.431 -11.062 1.00 53.42  ? 356 VAL   B N   1 
ATOM   1137 C  CA  . VAL   B 1 41  ? 26.198  -49.620 -10.641 1.00 53.64  ? 356 VAL   B CA  1 
ATOM   1138 C  C   . VAL   B 1 41  ? 27.024  -49.287 -9.400  1.00 54.39  ? 356 VAL   B C   1 
ATOM   1139 O  O   . VAL   B 1 41  ? 27.750  -48.297 -9.384  1.00 55.94  ? 356 VAL   B O   1 
ATOM   1140 C  CB  . VAL   B 1 41  ? 27.074  -50.140 -11.799 1.00 53.32  ? 356 VAL   B CB  1 
ATOM   1141 C  CG1 . VAL   B 1 41  ? 27.936  -51.330 -11.388 1.00 53.21  ? 356 VAL   B CG1 1 
ATOM   1142 C  CG2 . VAL   B 1 41  ? 26.231  -50.491 -13.019 1.00 53.24  ? 356 VAL   B CG2 1 
ATOM   1143 N  N   . HIS   B 1 42  ? 26.894  -50.130 -8.368  1.00 54.70  ? 357 HIS   B N   1 
ATOM   1144 C  CA  . HIS   B 1 42  ? 27.633  -49.986 -7.125  1.00 55.28  ? 357 HIS   B CA  1 
ATOM   1145 C  C   . HIS   B 1 42  ? 28.578  -51.173 -6.962  1.00 56.43  ? 357 HIS   B C   1 
ATOM   1146 O  O   . HIS   B 1 42  ? 28.138  -52.319 -7.003  1.00 56.82  ? 357 HIS   B O   1 
ATOM   1147 C  CB  . HIS   B 1 42  ? 26.671  -49.915 -5.935  1.00 54.76  ? 357 HIS   B CB  1 
ATOM   1148 C  CG  . HIS   B 1 42  ? 25.815  -48.694 -5.927  1.00 53.73  ? 357 HIS   B CG  1 
ATOM   1149 N  ND1 . HIS   B 1 42  ? 26.174  -47.541 -5.264  1.00 52.83  ? 357 HIS   B ND1 1 
ATOM   1150 C  CD2 . HIS   B 1 42  ? 24.627  -48.443 -6.493  1.00 53.12  ? 357 HIS   B CD2 1 
ATOM   1151 C  CE1 . HIS   B 1 42  ? 25.228  -46.629 -5.432  1.00 52.70  ? 357 HIS   B CE1 1 
ATOM   1152 N  NE2 . HIS   B 1 42  ? 24.280  -47.155 -6.176  1.00 52.35  ? 357 HIS   B NE2 1 
ATOM   1153 N  N   . GLU   B 1 43  ? 29.869  -50.883 -6.765  1.00 58.43  ? 358 GLU   B N   1 
ATOM   1154 C  CA  . GLU   B 1 43  ? 30.881  -51.911 -6.585  1.00 61.55  ? 358 GLU   B CA  1 
ATOM   1155 C  C   . GLU   B 1 43  ? 31.180  -52.032 -5.092  1.00 60.72  ? 358 GLU   B C   1 
ATOM   1156 O  O   . GLU   B 1 43  ? 31.698  -51.096 -4.486  1.00 59.35  ? 358 GLU   B O   1 
ATOM   1157 C  CB  . GLU   B 1 43  ? 32.087  -51.559 -7.458  1.00 65.39  ? 358 GLU   B CB  1 
ATOM   1158 C  CG  . GLU   B 1 43  ? 31.739  -51.481 -8.944  1.00 68.86  ? 358 GLU   B CG  1 
ATOM   1159 C  CD  . GLU   B 1 43  ? 32.867  -51.061 -9.870  1.00 72.81  ? 358 GLU   B CD  1 
ATOM   1160 O  OE1 . GLU   B 1 43  ? 33.443  -49.975 -9.646  1.00 74.69  ? 358 GLU   B OE1 1 
ATOM   1161 O  OE2 . GLU   B 1 43  ? 33.156  -51.807 -10.831 1.00 76.00  ? 358 GLU   B OE2 1 
ATOM   1162 N  N   . THR   B 1 44  ? 30.849  -53.196 -4.515  1.00 62.10  ? 359 THR   B N   1 
ATOM   1163 C  CA  . THR   B 1 44  ? 30.711  -53.338 -3.072  1.00 62.76  ? 359 THR   B CA  1 
ATOM   1164 C  C   . THR   B 1 44  ? 31.749  -54.312 -2.516  1.00 64.05  ? 359 THR   B C   1 
ATOM   1165 O  O   . THR   B 1 44  ? 32.506  -54.929 -3.263  1.00 63.87  ? 359 THR   B O   1 
ATOM   1166 C  CB  . THR   B 1 44  ? 29.291  -53.799 -2.736  1.00 61.69  ? 359 THR   B CB  1 
ATOM   1167 O  OG1 . THR   B 1 44  ? 29.176  -55.124 -3.246  1.00 60.41  ? 359 THR   B OG1 1 
ATOM   1168 C  CG2 . THR   B 1 44  ? 28.223  -52.896 -3.328  1.00 61.56  ? 359 THR   B CG2 1 
ATOM   1169 N  N   . LEU   B 1 45  ? 31.756  -54.426 -1.181  1.00 65.80  ? 360 LEU   B N   1 
ATOM   1170 C  CA  . LEU   B 1 45  ? 32.627  -55.334 -0.453  1.00 67.28  ? 360 LEU   B CA  1 
ATOM   1171 C  C   . LEU   B 1 45  ? 31.934  -55.732 0.849   1.00 70.03  ? 360 LEU   B C   1 
ATOM   1172 O  O   . LEU   B 1 45  ? 31.623  -54.869 1.668   1.00 71.49  ? 360 LEU   B O   1 
ATOM   1173 C  CB  . LEU   B 1 45  ? 33.963  -54.641 -0.187  1.00 66.41  ? 360 LEU   B CB  1 
ATOM   1174 C  CG  . LEU   B 1 45  ? 34.982  -55.423 0.648   1.00 66.55  ? 360 LEU   B CG  1 
ATOM   1175 C  CD1 . LEU   B 1 45  ? 35.462  -56.664 -0.085  1.00 66.30  ? 360 LEU   B CD1 1 
ATOM   1176 C  CD2 . LEU   B 1 45  ? 36.156  -54.539 1.030   1.00 66.65  ? 360 LEU   B CD2 1 
ATOM   1177 N  N   . THR   B 1 46  ? 31.700  -57.038 1.029   1.00 71.32  ? 361 THR   B N   1 
ATOM   1178 C  CA  . THR   B 1 46  ? 31.003  -57.546 2.201   1.00 71.85  ? 361 THR   B CA  1 
ATOM   1179 C  C   . THR   B 1 46  ? 32.001  -57.759 3.338   1.00 72.78  ? 361 THR   B C   1 
ATOM   1180 O  O   . THR   B 1 46  ? 33.062  -58.345 3.128   1.00 70.59  ? 361 THR   B O   1 
ATOM   1181 C  CB  . THR   B 1 46  ? 30.256  -58.831 1.839   1.00 72.19  ? 361 THR   B CB  1 
ATOM   1182 O  OG1 . THR   B 1 46  ? 31.138  -59.600 1.027   1.00 74.02  ? 361 THR   B OG1 1 
ATOM   1183 C  CG2 . THR   B 1 46  ? 28.985  -58.561 1.055   1.00 72.08  ? 361 THR   B CG2 1 
ATOM   1184 N  N   . VAL   B 1 47  ? 31.652  -57.255 4.533   1.00 75.10  ? 362 VAL   B N   1 
ATOM   1185 C  CA  . VAL   B 1 47  ? 32.426  -57.477 5.747   1.00 75.60  ? 362 VAL   B CA  1 
ATOM   1186 C  C   . VAL   B 1 47  ? 31.464  -57.842 6.876   1.00 75.62  ? 362 VAL   B C   1 
ATOM   1187 O  O   . VAL   B 1 47  ? 30.295  -57.461 6.852   1.00 73.89  ? 362 VAL   B O   1 
ATOM   1188 C  CB  . VAL   B 1 47  ? 33.302  -56.275 6.159   1.00 75.46  ? 362 VAL   B CB  1 
ATOM   1189 C  CG1 . VAL   B 1 47  ? 34.313  -55.905 5.080   1.00 75.19  ? 362 VAL   B CG1 1 
ATOM   1190 C  CG2 . VAL   B 1 47  ? 32.470  -55.057 6.548   1.00 75.78  ? 362 VAL   B CG2 1 
ATOM   1191 N  N   . TYR   B 1 48  ? 31.987  -58.570 7.870   1.00 76.88  ? 363 TYR   B N   1 
ATOM   1192 C  CA  . TYR   B 1 48  ? 31.212  -59.011 9.018   1.00 78.60  ? 363 TYR   B CA  1 
ATOM   1193 C  C   . TYR   B 1 48  ? 30.878  -57.826 9.918   1.00 78.27  ? 363 TYR   B C   1 
ATOM   1194 O  O   . TYR   B 1 48  ? 29.741  -57.692 10.367  1.00 76.32  ? 363 TYR   B O   1 
ATOM   1195 C  CB  . TYR   B 1 48  ? 31.998  -60.062 9.809   1.00 81.42  ? 363 TYR   B CB  1 
ATOM   1196 C  CG  . TYR   B 1 48  ? 31.996  -61.460 9.205   1.00 84.51  ? 363 TYR   B CG  1 
ATOM   1197 C  CD1 . TYR   B 1 48  ? 30.803  -62.124 8.936   1.00 85.85  ? 363 TYR   B CD1 1 
ATOM   1198 C  CD2 . TYR   B 1 48  ? 33.184  -62.107 8.886   1.00 85.81  ? 363 TYR   B CD2 1 
ATOM   1199 C  CE1 . TYR   B 1 48  ? 30.793  -63.395 8.384   1.00 86.98  ? 363 TYR   B CE1 1 
ATOM   1200 C  CE2 . TYR   B 1 48  ? 33.188  -63.378 8.334   1.00 86.43  ? 363 TYR   B CE2 1 
ATOM   1201 C  CZ  . TYR   B 1 48  ? 31.989  -64.022 8.079   1.00 87.02  ? 363 TYR   B CZ  1 
ATOM   1202 O  OH  . TYR   B 1 48  ? 31.987  -65.273 7.533   1.00 85.48  ? 363 TYR   B OH  1 
ATOM   1203 N  N   . LYS   B 1 49  ? 31.887  -56.985 10.184  1.00 77.60  ? 364 LYS   B N   1 
ATOM   1204 C  CA  . LYS   B 1 49  ? 31.800  -55.979 11.231  1.00 76.78  ? 364 LYS   B CA  1 
ATOM   1205 C  C   . LYS   B 1 49  ? 32.437  -54.672 10.765  1.00 73.78  ? 364 LYS   B C   1 
ATOM   1206 O  O   . LYS   B 1 49  ? 33.404  -54.677 10.004  1.00 73.28  ? 364 LYS   B O   1 
ATOM   1207 C  CB  . LYS   B 1 49  ? 32.469  -56.510 12.505  1.00 78.76  ? 364 LYS   B CB  1 
ATOM   1208 C  CG  . LYS   B 1 49  ? 31.865  -57.805 13.040  1.00 79.99  ? 364 LYS   B CG  1 
ATOM   1209 C  CD  . LYS   B 1 49  ? 32.421  -58.283 14.376  1.00 80.81  ? 364 LYS   B CD  1 
ATOM   1210 C  CE  . LYS   B 1 49  ? 31.636  -59.440 14.910  1.00 81.43  ? 364 LYS   B CE  1 
ATOM   1211 N  NZ  . LYS   B 1 49  ? 32.102  -59.853 16.236  1.00 82.22  ? 364 LYS   B NZ  1 
ATOM   1212 N  N   . ALA   B 1 50  ? 31.866  -53.559 11.241  1.00 71.19  ? 365 ALA   B N   1 
ATOM   1213 C  CA  . ALA   B 1 50  ? 32.364  -52.222 10.964  1.00 69.97  ? 365 ALA   B CA  1 
ATOM   1214 C  C   . ALA   B 1 50  ? 31.874  -51.274 12.055  1.00 70.08  ? 365 ALA   B C   1 
ATOM   1215 O  O   . ALA   B 1 50  ? 30.850  -51.531 12.686  1.00 70.96  ? 365 ALA   B O   1 
ATOM   1216 C  CB  . ALA   B 1 50  ? 31.908  -51.772 9.594   1.00 69.09  ? 365 ALA   B CB  1 
ATOM   1217 N  N   . SER   B 1 51  ? 32.613  -50.179 12.266  1.00 69.24  ? 366 SER   B N   1 
ATOM   1218 C  CA  . SER   B 1 51  ? 32.296  -49.225 13.317  1.00 69.32  ? 366 SER   B CA  1 
ATOM   1219 C  C   . SER   B 1 51  ? 32.660  -47.810 12.872  1.00 66.71  ? 366 SER   B C   1 
ATOM   1220 O  O   . SER   B 1 51  ? 33.336  -47.632 11.862  1.00 66.21  ? 366 SER   B O   1 
ATOM   1221 C  CB  . SER   B 1 51  ? 32.973  -49.611 14.613  1.00 70.77  ? 366 SER   B CB  1 
ATOM   1222 O  OG  . SER   B 1 51  ? 34.291  -50.090 14.383  1.00 71.14  ? 366 SER   B OG  1 
ATOM   1223 N  N   . ASN   B 1 52  ? 32.187  -46.820 13.643  1.00 65.35  ? 367 ASN   B N   1 
ATOM   1224 C  CA  . ASN   B 1 52  ? 32.271  -45.406 13.301  1.00 63.71  ? 367 ASN   B CA  1 
ATOM   1225 C  C   . ASN   B 1 52  ? 31.295  -45.095 12.169  1.00 63.34  ? 367 ASN   B C   1 
ATOM   1226 O  O   . ASN   B 1 52  ? 31.632  -44.357 11.247  1.00 62.42  ? 367 ASN   B O   1 
ATOM   1227 C  CB  . ASN   B 1 52  ? 33.682  -44.953 12.932  1.00 62.32  ? 367 ASN   B CB  1 
ATOM   1228 C  CG  . ASN   B 1 52  ? 34.703  -45.203 14.018  1.00 62.18  ? 367 ASN   B CG  1 
ATOM   1229 O  OD1 . ASN   B 1 52  ? 35.905  -45.059 13.772  1.00 62.63  ? 367 ASN   B OD1 1 
ATOM   1230 N  ND2 . ASN   B 1 52  ? 34.266  -45.575 15.213  1.00 62.22  ? 367 ASN   B ND2 1 
ATOM   1231 N  N   . LEU   B 1 53  ? 30.079  -45.650 12.265  1.00 63.55  ? 368 LEU   B N   1 
ATOM   1232 C  CA  . LEU   B 1 53  ? 29.064  -45.473 11.239  1.00 62.61  ? 368 LEU   B CA  1 
ATOM   1233 C  C   . LEU   B 1 53  ? 27.734  -45.102 11.889  1.00 60.84  ? 368 LEU   B C   1 
ATOM   1234 O  O   . LEU   B 1 53  ? 27.282  -45.782 12.807  1.00 61.55  ? 368 LEU   B O   1 
ATOM   1235 C  CB  . LEU   B 1 53  ? 28.928  -46.750 10.410  1.00 62.84  ? 368 LEU   B CB  1 
ATOM   1236 C  CG  . LEU   B 1 53  ? 30.160  -47.179 9.606   1.00 62.88  ? 368 LEU   B CG  1 
ATOM   1237 C  CD1 . LEU   B 1 53  ? 29.891  -48.513 8.934   1.00 63.40  ? 368 LEU   B CD1 1 
ATOM   1238 C  CD2 . LEU   B 1 53  ? 30.565  -46.141 8.571   1.00 62.76  ? 368 LEU   B CD2 1 
ATOM   1239 N  N   . ASN   B 1 54  ? 27.119  -44.020 11.397  1.00 58.87  ? 369 ASN   B N   1 
ATOM   1240 C  CA  . ASN   B 1 54  ? 25.768  -43.654 11.785  1.00 58.41  ? 369 ASN   B CA  1 
ATOM   1241 C  C   . ASN   B 1 54  ? 24.780  -44.310 10.824  1.00 56.88  ? 369 ASN   B C   1 
ATOM   1242 O  O   . ASN   B 1 54  ? 24.838  -44.075 9.620   1.00 56.33  ? 369 ASN   B O   1 
ATOM   1243 C  CB  . ASN   B 1 54  ? 25.561  -42.143 11.809  1.00 58.71  ? 369 ASN   B CB  1 
ATOM   1244 C  CG  . ASN   B 1 54  ? 26.407  -41.449 12.850  1.00 58.91  ? 369 ASN   B CG  1 
ATOM   1245 O  OD1 . ASN   B 1 54  ? 27.129  -40.500 12.523  1.00 59.31  ? 369 ASN   B OD1 1 
ATOM   1246 N  ND2 . ASN   B 1 54  ? 26.322  -41.879 14.101  1.00 58.86  ? 369 ASN   B ND2 1 
ATOM   1247 N  N   . LEU   B 1 55  ? 23.882  -45.135 11.374  1.00 56.27  ? 370 LEU   B N   1 
ATOM   1248 C  CA  . LEU   B 1 55  ? 22.784  -45.705 10.613  1.00 55.74  ? 370 LEU   B CA  1 
ATOM   1249 C  C   . LEU   B 1 55  ? 21.671  -44.669 10.502  1.00 55.54  ? 370 LEU   B C   1 
ATOM   1250 O  O   . LEU   B 1 55  ? 21.503  -43.835 11.389  1.00 55.85  ? 370 LEU   B O   1 
ATOM   1251 C  CB  . LEU   B 1 55  ? 22.281  -46.986 11.275  1.00 55.68  ? 370 LEU   B CB  1 
ATOM   1252 C  CG  . LEU   B 1 55  ? 23.304  -48.116 11.421  1.00 55.75  ? 370 LEU   B CG  1 
ATOM   1253 C  CD1 . LEU   B 1 55  ? 22.699  -49.260 12.215  1.00 56.21  ? 370 LEU   B CD1 1 
ATOM   1254 C  CD2 . LEU   B 1 55  ? 23.803  -48.602 10.070  1.00 55.48  ? 370 LEU   B CD2 1 
ATOM   1255 N  N   . ILE   B 1 56  ? 20.906  -44.759 9.408   1.00 55.38  ? 371 ILE   B N   1 
ATOM   1256 C  CA  . ILE   B 1 56  ? 19.955  -43.725 9.036   1.00 56.46  ? 371 ILE   B CA  1 
ATOM   1257 C  C   . ILE   B 1 56  ? 18.788  -44.370 8.288   1.00 57.19  ? 371 ILE   B C   1 
ATOM   1258 O  O   . ILE   B 1 56  ? 18.994  -45.072 7.301   1.00 55.83  ? 371 ILE   B O   1 
ATOM   1259 C  CB  . ILE   B 1 56  ? 20.659  -42.613 8.231   1.00 56.91  ? 371 ILE   B CB  1 
ATOM   1260 C  CG1 . ILE   B 1 56  ? 19.716  -41.930 7.228   1.00 56.72  ? 371 ILE   B CG1 1 
ATOM   1261 C  CG2 . ILE   B 1 56  ? 21.921  -43.143 7.544   1.00 58.09  ? 371 ILE   B CG2 1 
ATOM   1262 C  CD1 . ILE   B 1 56  ? 20.410  -40.981 6.267   1.00 56.65  ? 371 ILE   B CD1 1 
ATOM   1263 N  N   . GLY   B 1 57  ? 17.568  -44.120 8.786   1.00 60.01  ? 372 GLY   B N   1 
ATOM   1264 C  CA  . GLY   B 1 57  ? 16.350  -44.687 8.226   1.00 61.55  ? 372 GLY   B CA  1 
ATOM   1265 C  C   . GLY   B 1 57  ? 16.057  -46.071 8.803   1.00 63.32  ? 372 GLY   B C   1 
ATOM   1266 O  O   . GLY   B 1 57  ? 16.853  -46.611 9.568   1.00 63.38  ? 372 GLY   B O   1 
ATOM   1267 N  N   . ARG   B 1 58  ? 14.899  -46.629 8.430   1.00 66.40  ? 373 ARG   B N   1 
ATOM   1268 C  CA  . ARG   B 1 58  ? 14.545  -47.996 8.780   1.00 70.22  ? 373 ARG   B CA  1 
ATOM   1269 C  C   . ARG   B 1 58  ? 15.265  -48.966 7.847   1.00 68.73  ? 373 ARG   B C   1 
ATOM   1270 O  O   . ARG   B 1 58  ? 15.714  -48.574 6.772   1.00 68.23  ? 373 ARG   B O   1 
ATOM   1271 C  CB  . ARG   B 1 58  ? 13.040  -48.249 8.625   1.00 74.98  ? 373 ARG   B CB  1 
ATOM   1272 C  CG  . ARG   B 1 58  ? 12.148  -47.569 9.654   1.00 79.37  ? 373 ARG   B CG  1 
ATOM   1273 C  CD  . ARG   B 1 58  ? 12.258  -48.233 11.022  1.00 83.84  ? 373 ARG   B CD  1 
ATOM   1274 N  NE  . ARG   B 1 58  ? 11.425  -47.602 12.053  1.00 87.96  ? 373 ARG   B NE  1 
ATOM   1275 C  CZ  . ARG   B 1 58  ? 11.574  -46.362 12.512  1.00 90.88  ? 373 ARG   B CZ  1 
ATOM   1276 N  NH1 . ARG   B 1 58  ? 12.504  -45.573 12.008  1.00 91.81  ? 373 ARG   B NH1 1 
ATOM   1277 N  NH2 . ARG   B 1 58  ? 10.787  -45.905 13.471  1.00 91.97  ? 373 ARG   B NH2 1 
ATOM   1278 N  N   . PRO   B 1 59  ? 15.408  -50.257 8.227   1.00 68.76  ? 374 PRO   B N   1 
ATOM   1279 C  CA  . PRO   B 1 59  ? 15.716  -51.301 7.255   1.00 68.26  ? 374 PRO   B CA  1 
ATOM   1280 C  C   . PRO   B 1 59  ? 14.619  -51.452 6.202   1.00 68.23  ? 374 PRO   B C   1 
ATOM   1281 O  O   . PRO   B 1 59  ? 13.435  -51.440 6.535   1.00 69.94  ? 374 PRO   B O   1 
ATOM   1282 C  CB  . PRO   B 1 59  ? 15.887  -52.561 8.107   1.00 67.48  ? 374 PRO   B CB  1 
ATOM   1283 C  CG  . PRO   B 1 59  ? 16.124  -52.040 9.514   1.00 67.71  ? 374 PRO   B CG  1 
ATOM   1284 C  CD  . PRO   B 1 59  ? 15.347  -50.763 9.607   1.00 68.56  ? 374 PRO   B CD  1 
ATOM   1285 N  N   . SER   B 1 60  ? 15.031  -51.576 4.934   1.00 67.72  ? 375 SER   B N   1 
ATOM   1286 C  CA  . SER   B 1 60  ? 14.117  -51.742 3.814   1.00 66.37  ? 375 SER   B CA  1 
ATOM   1287 C  C   . SER   B 1 60  ? 14.565  -52.930 2.966   1.00 65.22  ? 375 SER   B C   1 
ATOM   1288 O  O   . SER   B 1 60  ? 15.758  -53.208 2.877   1.00 64.27  ? 375 SER   B O   1 
ATOM   1289 C  CB  . SER   B 1 60  ? 14.035  -50.477 2.993   1.00 66.32  ? 375 SER   B CB  1 
ATOM   1290 O  OG  . SER   B 1 60  ? 13.310  -50.685 1.788   1.00 65.91  ? 375 SER   B OG  1 
ATOM   1291 N  N   . THR   B 1 61  ? 13.593  -53.626 2.358   1.00 64.83  ? 376 THR   B N   1 
ATOM   1292 C  CA  . THR   B 1 61  ? 13.866  -54.783 1.516   1.00 64.76  ? 376 THR   B CA  1 
ATOM   1293 C  C   . THR   B 1 61  ? 13.536  -54.473 0.055   1.00 64.63  ? 376 THR   B C   1 
ATOM   1294 O  O   . THR   B 1 61  ? 13.574  -55.369 -0.786  1.00 64.29  ? 376 THR   B O   1 
ATOM   1295 C  CB  . THR   B 1 61  ? 13.076  -55.993 2.021   1.00 63.53  ? 376 THR   B CB  1 
ATOM   1296 O  OG1 . THR   B 1 61  ? 11.717  -55.580 2.132   1.00 62.56  ? 376 THR   B OG1 1 
ATOM   1297 C  CG2 . THR   B 1 61  ? 13.570  -56.495 3.365   1.00 62.20  ? 376 THR   B CG2 1 
ATOM   1298 N  N   . GLU   B 1 62  ? 13.221  -53.206 -0.245  1.00 64.88  ? 377 GLU   B N   1 
ATOM   1299 C  CA  . GLU   B 1 62  ? 12.981  -52.776 -1.612  1.00 65.75  ? 377 GLU   B CA  1 
ATOM   1300 C  C   . GLU   B 1 62  ? 14.258  -52.973 -2.426  1.00 65.21  ? 377 GLU   B C   1 
ATOM   1301 O  O   . GLU   B 1 62  ? 15.240  -52.263 -2.215  1.00 64.75  ? 377 GLU   B O   1 
ATOM   1302 C  CB  . GLU   B 1 62  ? 12.549  -51.308 -1.634  1.00 68.35  ? 377 GLU   B CB  1 
ATOM   1303 C  CG  . GLU   B 1 62  ? 12.276  -50.765 -3.036  1.00 71.16  ? 377 GLU   B CG  1 
ATOM   1304 C  CD  . GLU   B 1 62  ? 12.415  -49.256 -3.164  1.00 73.54  ? 377 GLU   B CD  1 
ATOM   1305 O  OE1 . GLU   B 1 62  ? 11.721  -48.526 -2.425  1.00 76.40  ? 377 GLU   B OE1 1 
ATOM   1306 O  OE2 . GLU   B 1 62  ? 13.220  -48.810 -4.009  1.00 73.37  ? 377 GLU   B OE2 1 
ATOM   1307 N  N   . HIS   B 1 63  ? 14.234  -53.955 -3.337  1.00 64.42  ? 378 HIS   B N   1 
ATOM   1308 C  CA  . HIS   B 1 63  ? 15.322  -54.194 -4.274  1.00 62.99  ? 378 HIS   B CA  1 
ATOM   1309 C  C   . HIS   B 1 63  ? 16.599  -54.536 -3.507  1.00 60.45  ? 378 HIS   B C   1 
ATOM   1310 O  O   . HIS   B 1 63  ? 17.658  -53.975 -3.777  1.00 59.83  ? 378 HIS   B O   1 
ATOM   1311 C  CB  . HIS   B 1 63  ? 15.470  -52.993 -5.219  1.00 64.19  ? 378 HIS   B CB  1 
ATOM   1312 C  CG  . HIS   B 1 63  ? 16.315  -53.234 -6.430  1.00 65.86  ? 378 HIS   B CG  1 
ATOM   1313 N  ND1 . HIS   B 1 63  ? 17.501  -53.936 -6.424  1.00 66.35  ? 378 HIS   B ND1 1 
ATOM   1314 C  CD2 . HIS   B 1 63  ? 16.136  -52.826 -7.693  1.00 66.30  ? 378 HIS   B CD2 1 
ATOM   1315 C  CE1 . HIS   B 1 63  ? 18.006  -53.955 -7.649  1.00 66.01  ? 378 HIS   B CE1 1 
ATOM   1316 N  NE2 . HIS   B 1 63  ? 17.193  -53.287 -8.436  1.00 66.44  ? 378 HIS   B NE2 1 
ATOM   1317 N  N   . SER   B 1 64  ? 16.489  -55.469 -2.554  1.00 58.52  ? 379 SER   B N   1 
ATOM   1318 C  CA  . SER   B 1 64  ? 17.629  -55.895 -1.758  1.00 57.47  ? 379 SER   B CA  1 
ATOM   1319 C  C   . SER   B 1 64  ? 18.537  -56.790 -2.599  1.00 56.66  ? 379 SER   B C   1 
ATOM   1320 O  O   . SER   B 1 64  ? 18.060  -57.709 -3.263  1.00 55.31  ? 379 SER   B O   1 
ATOM   1321 C  CB  . SER   B 1 64  ? 17.186  -56.596 -0.498  1.00 57.43  ? 379 SER   B CB  1 
ATOM   1322 O  OG  . SER   B 1 64  ? 18.306  -56.999 0.279   1.00 57.06  ? 379 SER   B OG  1 
ATOM   1323 N  N   . TRP   B 1 65  ? 19.848  -56.515 -2.542  1.00 55.94  ? 380 TRP   B N   1 
ATOM   1324 C  CA  . TRP   B 1 65  ? 20.837  -57.228 -3.337  1.00 54.96  ? 380 TRP   B CA  1 
ATOM   1325 C  C   . TRP   B 1 65  ? 21.134  -58.603 -2.742  1.00 56.00  ? 380 TRP   B C   1 
ATOM   1326 O  O   . TRP   B 1 65  ? 21.686  -59.463 -3.425  1.00 57.15  ? 380 TRP   B O   1 
ATOM   1327 C  CB  . TRP   B 1 65  ? 22.123  -56.400 -3.455  1.00 53.15  ? 380 TRP   B CB  1 
ATOM   1328 C  CG  . TRP   B 1 65  ? 21.946  -55.092 -4.179  1.00 51.26  ? 380 TRP   B CG  1 
ATOM   1329 C  CD1 . TRP   B 1 65  ? 21.054  -54.812 -5.173  1.00 50.95  ? 380 TRP   B CD1 1 
ATOM   1330 C  CD2 . TRP   B 1 65  ? 22.689  -53.875 -3.953  1.00 50.36  ? 380 TRP   B CD2 1 
ATOM   1331 N  NE1 . TRP   B 1 65  ? 21.187  -53.512 -5.580  1.00 51.18  ? 380 TRP   B NE1 1 
ATOM   1332 C  CE2 . TRP   B 1 65  ? 22.180  -52.912 -4.852  1.00 50.78  ? 380 TRP   B CE2 1 
ATOM   1333 C  CE3 . TRP   B 1 65  ? 23.726  -53.509 -3.087  1.00 49.67  ? 380 TRP   B CE3 1 
ATOM   1334 C  CZ2 . TRP   B 1 65  ? 22.677  -51.611 -4.906  1.00 50.67  ? 380 TRP   B CZ2 1 
ATOM   1335 C  CZ3 . TRP   B 1 65  ? 24.215  -52.222 -3.142  1.00 49.91  ? 380 TRP   B CZ3 1 
ATOM   1336 C  CH2 . TRP   B 1 65  ? 23.696  -51.287 -4.039  1.00 50.24  ? 380 TRP   B CH2 1 
ATOM   1337 N  N   . PHE   B 1 66  ? 20.792  -58.784 -1.460  1.00 55.64  ? 381 PHE   B N   1 
ATOM   1338 C  CA  . PHE   B 1 66  ? 20.878  -60.078 -0.805  1.00 55.45  ? 381 PHE   B CA  1 
ATOM   1339 C  C   . PHE   B 1 66  ? 19.477  -60.467 -0.346  1.00 57.93  ? 381 PHE   B C   1 
ATOM   1340 O  O   . PHE   B 1 66  ? 19.019  -59.996 0.692   1.00 59.44  ? 381 PHE   B O   1 
ATOM   1341 C  CB  . PHE   B 1 66  ? 21.884  -59.987 0.346   1.00 53.76  ? 381 PHE   B CB  1 
ATOM   1342 C  CG  . PHE   B 1 66  ? 23.237  -59.438 -0.080  1.00 52.57  ? 381 PHE   B CG  1 
ATOM   1343 C  CD1 . PHE   B 1 66  ? 23.472  -58.068 -0.102  1.00 52.22  ? 381 PHE   B CD1 1 
ATOM   1344 C  CD2 . PHE   B 1 66  ? 24.264  -60.289 -0.471  1.00 52.16  ? 381 PHE   B CD2 1 
ATOM   1345 C  CE1 . PHE   B 1 66  ? 24.703  -57.566 -0.498  1.00 52.66  ? 381 PHE   B CE1 1 
ATOM   1346 C  CE2 . PHE   B 1 66  ? 25.494  -59.782 -0.865  1.00 52.35  ? 381 PHE   B CE2 1 
ATOM   1347 C  CZ  . PHE   B 1 66  ? 25.711  -58.423 -0.878  1.00 52.37  ? 381 PHE   B CZ  1 
ATOM   1348 N  N   . PRO   B 1 67  ? 18.736  -61.297 -1.119  1.00 60.06  ? 382 PRO   B N   1 
ATOM   1349 C  CA  . PRO   B 1 67  ? 17.411  -61.744 -0.704  1.00 60.53  ? 382 PRO   B CA  1 
ATOM   1350 C  C   . PRO   B 1 67  ? 17.422  -62.396 0.676   1.00 61.29  ? 382 PRO   B C   1 
ATOM   1351 O  O   . PRO   B 1 67  ? 18.282  -63.227 0.961   1.00 61.75  ? 382 PRO   B O   1 
ATOM   1352 C  CB  . PRO   B 1 67  ? 16.986  -62.709 -1.809  1.00 60.42  ? 382 PRO   B CB  1 
ATOM   1353 C  CG  . PRO   B 1 67  ? 17.818  -62.276 -3.003  1.00 60.90  ? 382 PRO   B CG  1 
ATOM   1354 C  CD  . PRO   B 1 67  ? 19.127  -61.826 -2.435  1.00 60.80  ? 382 PRO   B CD  1 
ATOM   1355 N  N   . GLY   B 1 68  ? 16.470  -61.986 1.525   1.00 61.63  ? 383 GLY   B N   1 
ATOM   1356 C  CA  . GLY   B 1 68  ? 16.416  -62.418 2.912   1.00 61.10  ? 383 GLY   B CA  1 
ATOM   1357 C  C   . GLY   B 1 68  ? 16.827  -61.303 3.871   1.00 61.12  ? 383 GLY   B C   1 
ATOM   1358 O  O   . GLY   B 1 68  ? 16.466  -61.339 5.045   1.00 61.34  ? 383 GLY   B O   1 
ATOM   1359 N  N   . TYR   B 1 69  ? 17.585  -60.321 3.362   1.00 61.04  ? 384 TYR   B N   1 
ATOM   1360 C  CA  . TYR   B 1 69  ? 18.116  -59.240 4.178   1.00 61.35  ? 384 TYR   B CA  1 
ATOM   1361 C  C   . TYR   B 1 69  ? 17.402  -57.931 3.848   1.00 61.35  ? 384 TYR   B C   1 
ATOM   1362 O  O   . TYR   B 1 69  ? 16.822  -57.785 2.773   1.00 63.00  ? 384 TYR   B O   1 
ATOM   1363 C  CB  . TYR   B 1 69  ? 19.620  -59.074 3.944   1.00 61.90  ? 384 TYR   B CB  1 
ATOM   1364 C  CG  . TYR   B 1 69  ? 20.491  -60.193 4.498   1.00 63.38  ? 384 TYR   B CG  1 
ATOM   1365 C  CD1 . TYR   B 1 69  ? 20.746  -61.342 3.758   1.00 64.43  ? 384 TYR   B CD1 1 
ATOM   1366 C  CD2 . TYR   B 1 69  ? 21.074  -60.088 5.756   1.00 64.37  ? 384 TYR   B CD2 1 
ATOM   1367 C  CE1 . TYR   B 1 69  ? 21.546  -62.357 4.257   1.00 64.91  ? 384 TYR   B CE1 1 
ATOM   1368 C  CE2 . TYR   B 1 69  ? 21.874  -61.097 6.266   1.00 65.66  ? 384 TYR   B CE2 1 
ATOM   1369 C  CZ  . TYR   B 1 69  ? 22.111  -62.234 5.514   1.00 65.67  ? 384 TYR   B CZ  1 
ATOM   1370 O  OH  . TYR   B 1 69  ? 22.901  -63.230 6.011   1.00 65.66  ? 384 TYR   B OH  1 
ATOM   1371 N  N   . ALA   B 1 70  ? 17.463  -56.991 4.799   1.00 60.16  ? 385 ALA   B N   1 
ATOM   1372 C  CA  . ALA   B 1 70  ? 17.045  -55.613 4.590   1.00 58.81  ? 385 ALA   B CA  1 
ATOM   1373 C  C   . ALA   B 1 70  ? 18.264  -54.706 4.714   1.00 56.48  ? 385 ALA   B C   1 
ATOM   1374 O  O   . ALA   B 1 70  ? 19.235  -55.066 5.375   1.00 55.45  ? 385 ALA   B O   1 
ATOM   1375 C  CB  . ALA   B 1 70  ? 15.979  -55.237 5.594   1.00 59.34  ? 385 ALA   B CB  1 
ATOM   1376 N  N   . TRP   B 1 71  ? 18.197  -53.525 4.090   1.00 55.34  ? 386 TRP   B N   1 
ATOM   1377 C  CA  . TRP   B 1 71  ? 19.327  -52.612 4.064   1.00 55.47  ? 386 TRP   B CA  1 
ATOM   1378 C  C   . TRP   B 1 71  ? 18.977  -51.306 4.772   1.00 56.88  ? 386 TRP   B C   1 
ATOM   1379 O  O   . TRP   B 1 71  ? 17.897  -50.755 4.572   1.00 56.70  ? 386 TRP   B O   1 
ATOM   1380 C  CB  . TRP   B 1 71  ? 19.790  -52.356 2.623   1.00 55.40  ? 386 TRP   B CB  1 
ATOM   1381 C  CG  . TRP   B 1 71  ? 18.701  -51.916 1.679   1.00 55.44  ? 386 TRP   B CG  1 
ATOM   1382 C  CD1 . TRP   B 1 71  ? 17.962  -52.713 0.856   1.00 55.19  ? 386 TRP   B CD1 1 
ATOM   1383 C  CD2 . TRP   B 1 71  ? 18.238  -50.566 1.453   1.00 55.69  ? 386 TRP   B CD2 1 
ATOM   1384 N  NE1 . TRP   B 1 71  ? 17.069  -51.962 0.140   1.00 55.09  ? 386 TRP   B NE1 1 
ATOM   1385 C  CE2 . TRP   B 1 71  ? 17.214  -50.643 0.482   1.00 55.44  ? 386 TRP   B CE2 1 
ATOM   1386 C  CE3 . TRP   B 1 71  ? 18.582  -49.311 1.972   1.00 55.54  ? 386 TRP   B CE3 1 
ATOM   1387 C  CZ2 . TRP   B 1 71  ? 16.538  -49.512 0.026   1.00 55.14  ? 386 TRP   B CZ2 1 
ATOM   1388 C  CZ3 . TRP   B 1 71  ? 17.912  -48.196 1.520   1.00 55.39  ? 386 TRP   B CZ3 1 
ATOM   1389 C  CH2 . TRP   B 1 71  ? 16.905  -48.297 0.559   1.00 55.46  ? 386 TRP   B CH2 1 
ATOM   1390 N  N   . THR   B 1 72  ? 19.909  -50.844 5.616   1.00 58.87  ? 387 THR   B N   1 
ATOM   1391 C  CA  . THR   B 1 72  ? 19.876  -49.506 6.186   1.00 60.53  ? 387 THR   B CA  1 
ATOM   1392 C  C   . THR   B 1 72  ? 21.115  -48.759 5.697   1.00 61.65  ? 387 THR   B C   1 
ATOM   1393 O  O   . THR   B 1 72  ? 22.191  -49.346 5.608   1.00 62.58  ? 387 THR   B O   1 
ATOM   1394 C  CB  . THR   B 1 72  ? 19.839  -49.595 7.711   1.00 60.91  ? 387 THR   B CB  1 
ATOM   1395 O  OG1 . THR   B 1 72  ? 18.821  -50.541 8.021   1.00 62.44  ? 387 THR   B OG1 1 
ATOM   1396 C  CG2 . THR   B 1 72  ? 19.543  -48.258 8.367   1.00 60.91  ? 387 THR   B CG2 1 
ATOM   1397 N  N   . VAL   B 1 73  ? 20.954  -47.468 5.383   1.00 61.24  ? 388 VAL   B N   1 
ATOM   1398 C  CA  . VAL   B 1 73  ? 22.045  -46.664 4.851   1.00 60.33  ? 388 VAL   B CA  1 
ATOM   1399 C  C   . VAL   B 1 73  ? 23.054  -46.403 5.969   1.00 60.23  ? 388 VAL   B C   1 
ATOM   1400 O  O   . VAL   B 1 73  ? 22.673  -46.280 7.131   1.00 60.16  ? 388 VAL   B O   1 
ATOM   1401 C  CB  . VAL   B 1 73  ? 21.516  -45.355 4.232   1.00 59.42  ? 388 VAL   B CB  1 
ATOM   1402 C  CG1 . VAL   B 1 73  ? 22.643  -44.441 3.765   1.00 59.26  ? 388 VAL   B CG1 1 
ATOM   1403 C  CG2 . VAL   B 1 73  ? 20.548  -45.627 3.085   1.00 59.58  ? 388 VAL   B CG2 1 
ATOM   1404 N  N   . ALA   B 1 74  ? 24.341  -46.332 5.603   1.00 59.91  ? 389 ALA   B N   1 
ATOM   1405 C  CA  . ALA   B 1 74  ? 25.419  -46.173 6.566   1.00 59.93  ? 389 ALA   B CA  1 
ATOM   1406 C  C   . ALA   B 1 74  ? 26.343  -45.036 6.137   1.00 60.76  ? 389 ALA   B C   1 
ATOM   1407 O  O   . ALA   B 1 74  ? 26.775  -44.987 4.987   1.00 60.29  ? 389 ALA   B O   1 
ATOM   1408 C  CB  . ALA   B 1 74  ? 26.178  -47.475 6.708   1.00 59.68  ? 389 ALA   B CB  1 
ATOM   1409 N  N   . GLN   B 1 75  ? 26.646  -44.141 7.088   1.00 62.59  ? 390 GLN   B N   1 
ATOM   1410 C  CA  . GLN   B 1 75  ? 27.449  -42.953 6.841   1.00 64.29  ? 390 GLN   B CA  1 
ATOM   1411 C  C   . GLN   B 1 75  ? 28.607  -42.886 7.829   1.00 63.98  ? 390 GLN   B C   1 
ATOM   1412 O  O   . GLN   B 1 75  ? 28.538  -43.466 8.908   1.00 64.14  ? 390 GLN   B O   1 
ATOM   1413 C  CB  . GLN   B 1 75  ? 26.634  -41.682 7.063   1.00 66.63  ? 390 GLN   B CB  1 
ATOM   1414 C  CG  . GLN   B 1 75  ? 25.618  -41.382 5.968   1.00 69.43  ? 390 GLN   B CG  1 
ATOM   1415 C  CD  . GLN   B 1 75  ? 24.808  -40.139 6.261   1.00 72.07  ? 390 GLN   B CD  1 
ATOM   1416 O  OE1 . GLN   B 1 75  ? 24.836  -39.601 7.374   1.00 72.90  ? 390 GLN   B OE1 1 
ATOM   1417 N  NE2 . GLN   B 1 75  ? 24.071  -39.672 5.263   1.00 73.51  ? 390 GLN   B NE2 1 
ATOM   1418 N  N   . CYS   B 1 76  ? 29.652  -42.138 7.457   1.00 64.16  ? 391 CYS   B N   1 
ATOM   1419 C  CA  . CYS   B 1 76  ? 30.765  -41.871 8.352   1.00 65.05  ? 391 CYS   B CA  1 
ATOM   1420 C  C   . CYS   B 1 76  ? 30.285  -40.984 9.499   1.00 65.68  ? 391 CYS   B C   1 
ATOM   1421 O  O   . CYS   B 1 76  ? 29.550  -40.024 9.271   1.00 65.82  ? 391 CYS   B O   1 
ATOM   1422 C  CB  . CYS   B 1 76  ? 31.920  -41.204 7.613   1.00 65.81  ? 391 CYS   B CB  1 
ATOM   1423 S  SG  . CYS   B 1 76  ? 33.382  -40.933 8.649   1.00 66.34  ? 391 CYS   B SG  1 
ATOM   1424 N  N   . LYS   B 1 77  ? 30.696  -41.331 10.726  1.00 65.63  ? 392 LYS   B N   1 
ATOM   1425 C  CA  . LYS   B 1 77  ? 30.425  -40.518 11.903  1.00 64.41  ? 392 LYS   B CA  1 
ATOM   1426 C  C   . LYS   B 1 77  ? 30.915  -39.089 11.685  1.00 62.87  ? 392 LYS   B C   1 
ATOM   1427 O  O   . LYS   B 1 77  ? 30.203  -38.138 11.988  1.00 61.34  ? 392 LYS   B O   1 
ATOM   1428 C  CB  . LYS   B 1 77  ? 31.115  -41.052 13.164  1.00 65.26  ? 392 LYS   B CB  1 
ATOM   1429 C  CG  . LYS   B 1 77  ? 30.275  -41.938 14.071  1.00 66.72  ? 392 LYS   B CG  1 
ATOM   1430 C  CD  . LYS   B 1 77  ? 30.975  -42.251 15.389  1.00 68.90  ? 392 LYS   B CD  1 
ATOM   1431 C  CE  . LYS   B 1 77  ? 30.077  -42.858 16.424  1.00 71.45  ? 392 LYS   B CE  1 
ATOM   1432 N  NZ  . LYS   B 1 77  ? 29.534  -44.157 16.018  1.00 73.22  ? 392 LYS   B NZ  1 
ATOM   1433 N  N   . ILE   B 1 78  ? 32.135  -38.958 11.151  1.00 63.65  ? 393 ILE   B N   1 
ATOM   1434 C  CA  . ILE   B 1 78  ? 32.851  -37.693 11.153  1.00 64.15  ? 393 ILE   B CA  1 
ATOM   1435 C  C   . ILE   B 1 78  ? 32.329  -36.787 10.039  1.00 64.16  ? 393 ILE   B C   1 
ATOM   1436 O  O   . ILE   B 1 78  ? 31.785  -35.722 10.324  1.00 64.19  ? 393 ILE   B O   1 
ATOM   1437 C  CB  . ILE   B 1 78  ? 34.370  -37.932 11.045  1.00 63.52  ? 393 ILE   B CB  1 
ATOM   1438 C  CG1 . ILE   B 1 78  ? 34.863  -38.921 12.109  1.00 62.79  ? 393 ILE   B CG1 1 
ATOM   1439 C  CG2 . ILE   B 1 78  ? 35.146  -36.614 11.094  1.00 63.32  ? 393 ILE   B CG2 1 
ATOM   1440 C  CD1 . ILE   B 1 78  ? 34.346  -38.647 13.511  1.00 62.33  ? 393 ILE   B CD1 1 
ATOM   1441 N  N   . CYS   B 1 79  ? 32.497  -37.215 8.781   1.00 63.81  ? 394 CYS   B N   1 
ATOM   1442 C  CA  . CYS   B 1 79  ? 32.312  -36.330 7.639   1.00 63.68  ? 394 CYS   B CA  1 
ATOM   1443 C  C   . CYS   B 1 79  ? 30.954  -36.533 6.963   1.00 62.12  ? 394 CYS   B C   1 
ATOM   1444 O  O   . CYS   B 1 79  ? 30.632  -35.809 6.023   1.00 61.39  ? 394 CYS   B O   1 
ATOM   1445 C  CB  . CYS   B 1 79  ? 33.444  -36.500 6.632   1.00 65.20  ? 394 CYS   B CB  1 
ATOM   1446 S  SG  . CYS   B 1 79  ? 33.567  -38.166 5.932   1.00 66.39  ? 394 CYS   B SG  1 
ATOM   1447 N  N   . ALA   B 1 80  ? 30.171  -37.514 7.434   1.00 60.91  ? 395 ALA   B N   1 
ATOM   1448 C  CA  . ALA   B 1 80  ? 28.855  -37.808 6.882   1.00 60.52  ? 395 ALA   B CA  1 
ATOM   1449 C  C   . ALA   B 1 80  ? 28.957  -38.301 5.440   1.00 61.60  ? 395 ALA   B C   1 
ATOM   1450 O  O   . ALA   B 1 80  ? 28.007  -38.165 4.672   1.00 61.76  ? 395 ALA   B O   1 
ATOM   1451 C  CB  . ALA   B 1 80  ? 27.960  -36.592 6.976   1.00 59.24  ? 395 ALA   B CB  1 
ATOM   1452 N  N   . SER   B 1 81  ? 30.109  -38.881 5.084   1.00 62.48  ? 396 SER   B N   1 
ATOM   1453 C  CA  . SER   B 1 81  ? 30.294  -39.485 3.777   1.00 63.55  ? 396 SER   B CA  1 
ATOM   1454 C  C   . SER   B 1 81  ? 29.581  -40.835 3.753   1.00 62.89  ? 396 SER   B C   1 
ATOM   1455 O  O   . SER   B 1 81  ? 29.721  -41.620 4.687   1.00 61.96  ? 396 SER   B O   1 
ATOM   1456 C  CB  . SER   B 1 81  ? 31.761  -39.624 3.450   1.00 65.38  ? 396 SER   B CB  1 
ATOM   1457 O  OG  . SER   B 1 81  ? 31.956  -40.289 2.209   1.00 68.06  ? 396 SER   B OG  1 
ATOM   1458 N  N   . HIS   B 1 82  ? 28.804  -41.078 2.689   1.00 62.96  ? 397 HIS   B N   1 
ATOM   1459 C  CA  . HIS   B 1 82  ? 28.102  -42.339 2.507   1.00 63.18  ? 397 HIS   B CA  1 
ATOM   1460 C  C   . HIS   B 1 82  ? 29.128  -43.435 2.241   1.00 60.38  ? 397 HIS   B C   1 
ATOM   1461 O  O   . HIS   B 1 82  ? 29.849  -43.375 1.249   1.00 60.83  ? 397 HIS   B O   1 
ATOM   1462 C  CB  . HIS   B 1 82  ? 27.071  -42.223 1.377   1.00 65.68  ? 397 HIS   B CB  1 
ATOM   1463 C  CG  . HIS   B 1 82  ? 26.344  -43.488 1.040   1.00 69.35  ? 397 HIS   B CG  1 
ATOM   1464 N  ND1 . HIS   B 1 82  ? 25.022  -43.469 0.649   1.00 72.34  ? 397 HIS   B ND1 1 
ATOM   1465 C  CD2 . HIS   B 1 82  ? 26.711  -44.779 1.019   1.00 70.49  ? 397 HIS   B CD2 1 
ATOM   1466 C  CE1 . HIS   B 1 82  ? 24.617  -44.708 0.407   1.00 72.51  ? 397 HIS   B CE1 1 
ATOM   1467 N  NE2 . HIS   B 1 82  ? 25.627  -45.519 0.625   1.00 72.00  ? 397 HIS   B NE2 1 
ATOM   1468 N  N   . ILE   B 1 83  ? 29.172  -44.437 3.129   1.00 58.37  ? 398 ILE   B N   1 
ATOM   1469 C  CA  . ILE   B 1 83  ? 30.141  -45.517 3.033   1.00 56.56  ? 398 ILE   B CA  1 
ATOM   1470 C  C   . ILE   B 1 83  ? 29.473  -46.754 2.435   1.00 56.08  ? 398 ILE   B C   1 
ATOM   1471 O  O   . ILE   B 1 83  ? 30.045  -47.399 1.559   1.00 57.31  ? 398 ILE   B O   1 
ATOM   1472 C  CB  . ILE   B 1 83  ? 30.781  -45.802 4.405   1.00 55.82  ? 398 ILE   B CB  1 
ATOM   1473 C  CG1 . ILE   B 1 83  ? 31.467  -44.556 4.983   1.00 55.79  ? 398 ILE   B CG1 1 
ATOM   1474 C  CG2 . ILE   B 1 83  ? 31.743  -46.988 4.331   1.00 55.96  ? 398 ILE   B CG2 1 
ATOM   1475 C  CD1 . ILE   B 1 83  ? 32.528  -43.939 4.087   1.00 55.71  ? 398 ILE   B CD1 1 
ATOM   1476 N  N   . GLY   B 1 84  ? 28.267  -47.088 2.906   1.00 55.14  ? 399 GLY   B N   1 
ATOM   1477 C  CA  . GLY   B 1 84  ? 27.543  -48.213 2.339   1.00 54.76  ? 399 GLY   B CA  1 
ATOM   1478 C  C   . GLY   B 1 84  ? 26.201  -48.450 3.023   1.00 54.53  ? 399 GLY   B C   1 
ATOM   1479 O  O   . GLY   B 1 84  ? 25.504  -47.502 3.381   1.00 53.98  ? 399 GLY   B O   1 
ATOM   1480 N  N   . TRP   B 1 85  ? 25.853  -49.736 3.162   1.00 55.51  ? 400 TRP   B N   1 
ATOM   1481 C  CA  . TRP   B 1 85  ? 24.607  -50.171 3.773   1.00 55.76  ? 400 TRP   B CA  1 
ATOM   1482 C  C   . TRP   B 1 85  ? 24.903  -51.268 4.791   1.00 55.88  ? 400 TRP   B C   1 
ATOM   1483 O  O   . TRP   B 1 85  ? 25.903  -51.972 4.674   1.00 54.63  ? 400 TRP   B O   1 
ATOM   1484 C  CB  . TRP   B 1 85  ? 23.627  -50.679 2.706   1.00 55.98  ? 400 TRP   B CB  1 
ATOM   1485 C  CG  . TRP   B 1 85  ? 23.338  -49.681 1.618   1.00 57.18  ? 400 TRP   B CG  1 
ATOM   1486 C  CD1 . TRP   B 1 85  ? 22.232  -48.893 1.493   1.00 57.82  ? 400 TRP   B CD1 1 
ATOM   1487 C  CD2 . TRP   B 1 85  ? 24.194  -49.350 0.503   1.00 58.29  ? 400 TRP   B CD2 1 
ATOM   1488 N  NE1 . TRP   B 1 85  ? 22.332  -48.104 0.378   1.00 58.55  ? 400 TRP   B NE1 1 
ATOM   1489 C  CE2 . TRP   B 1 85  ? 23.526  -48.358 -0.247  1.00 58.63  ? 400 TRP   B CE2 1 
ATOM   1490 C  CE3 . TRP   B 1 85  ? 25.451  -49.791 0.071   1.00 58.22  ? 400 TRP   B CE3 1 
ATOM   1491 C  CZ2 . TRP   B 1 85  ? 24.074  -47.807 -1.404  1.00 58.66  ? 400 TRP   B CZ2 1 
ATOM   1492 C  CZ3 . TRP   B 1 85  ? 25.994  -49.240 -1.069  1.00 58.60  ? 400 TRP   B CZ3 1 
ATOM   1493 C  CH2 . TRP   B 1 85  ? 25.314  -48.261 -1.794  1.00 58.78  ? 400 TRP   B CH2 1 
ATOM   1494 N  N   . LYS   B 1 86  ? 24.020  -51.394 5.787   1.00 57.47  ? 401 LYS   B N   1 
ATOM   1495 C  CA  . LYS   B 1 86  ? 24.084  -52.477 6.753   1.00 57.33  ? 401 LYS   B CA  1 
ATOM   1496 C  C   . LYS   B 1 86  ? 22.936  -53.436 6.462   1.00 56.51  ? 401 LYS   B C   1 
ATOM   1497 O  O   . LYS   B 1 86  ? 21.790  -53.008 6.340   1.00 56.62  ? 401 LYS   B O   1 
ATOM   1498 C  CB  . LYS   B 1 86  ? 23.992  -51.951 8.189   1.00 58.87  ? 401 LYS   B CB  1 
ATOM   1499 C  CG  . LYS   B 1 86  ? 24.201  -53.005 9.271   1.00 60.50  ? 401 LYS   B CG  1 
ATOM   1500 C  CD  . LYS   B 1 86  ? 23.721  -52.583 10.654  1.00 61.22  ? 401 LYS   B CD  1 
ATOM   1501 C  CE  . LYS   B 1 86  ? 23.750  -53.710 11.636  1.00 61.88  ? 401 LYS   B CE  1 
ATOM   1502 N  NZ  . LYS   B 1 86  ? 23.116  -53.338 12.903  1.00 62.65  ? 401 LYS   B NZ  1 
ATOM   1503 N  N   . PHE   B 1 87  ? 23.261  -54.730 6.361   1.00 56.19  ? 402 PHE   B N   1 
ATOM   1504 C  CA  . PHE   B 1 87  ? 22.286  -55.747 6.008   1.00 55.06  ? 402 PHE   B CA  1 
ATOM   1505 C  C   . PHE   B 1 87  ? 21.905  -56.533 7.258   1.00 54.20  ? 402 PHE   B C   1 
ATOM   1506 O  O   . PHE   B 1 87  ? 22.776  -57.002 7.986   1.00 51.30  ? 402 PHE   B O   1 
ATOM   1507 C  CB  . PHE   B 1 87  ? 22.870  -56.597 4.875   1.00 54.96  ? 402 PHE   B CB  1 
ATOM   1508 C  CG  . PHE   B 1 87  ? 22.930  -55.850 3.550   1.00 54.48  ? 402 PHE   B CG  1 
ATOM   1509 C  CD1 . PHE   B 1 87  ? 21.823  -55.814 2.707   1.00 54.27  ? 402 PHE   B CD1 1 
ATOM   1510 C  CD2 . PHE   B 1 87  ? 24.078  -55.167 3.160   1.00 54.13  ? 402 PHE   B CD2 1 
ATOM   1511 C  CE1 . PHE   B 1 87  ? 21.869  -55.124 1.505   1.00 53.92  ? 402 PHE   B CE1 1 
ATOM   1512 C  CE2 . PHE   B 1 87  ? 24.119  -54.479 1.955   1.00 53.75  ? 402 PHE   B CE2 1 
ATOM   1513 C  CZ  . PHE   B 1 87  ? 23.015  -54.458 1.132   1.00 53.52  ? 402 PHE   B CZ  1 
ATOM   1514 N  N   . THR   B 1 88  ? 20.591  -56.654 7.489   1.00 56.59  ? 403 THR   B N   1 
ATOM   1515 C  CA  . THR   B 1 88  ? 20.046  -57.343 8.648   1.00 59.40  ? 403 THR   B CA  1 
ATOM   1516 C  C   . THR   B 1 88  ? 19.044  -58.393 8.176   1.00 60.54  ? 403 THR   B C   1 
ATOM   1517 O  O   . THR   B 1 88  ? 18.231  -58.122 7.295   1.00 59.80  ? 403 THR   B O   1 
ATOM   1518 C  CB  . THR   B 1 88  ? 19.397  -56.331 9.591   1.00 61.13  ? 403 THR   B CB  1 
ATOM   1519 O  OG1 . THR   B 1 88  ? 18.516  -55.542 8.795   1.00 62.52  ? 403 THR   B OG1 1 
ATOM   1520 C  CG2 . THR   B 1 88  ? 20.414  -55.432 10.270  1.00 61.54  ? 403 THR   B CG2 1 
ATOM   1521 N  N   . ALA   B 1 89  ? 19.106  -59.583 8.785   1.00 63.55  ? 404 ALA   B N   1 
ATOM   1522 C  CA  . ALA   B 1 89  ? 18.251  -60.701 8.416   1.00 66.47  ? 404 ALA   B CA  1 
ATOM   1523 C  C   . ALA   B 1 89  ? 16.801  -60.410 8.797   1.00 68.63  ? 404 ALA   B C   1 
ATOM   1524 O  O   . ALA   B 1 89  ? 16.539  -59.594 9.679   1.00 66.64  ? 404 ALA   B O   1 
ATOM   1525 C  CB  . ALA   B 1 89  ? 18.754  -61.965 9.079   1.00 66.79  ? 404 ALA   B CB  1 
ATOM   1526 N  N   . THR   B 1 90  ? 15.866  -61.090 8.119   1.00 73.27  ? 405 THR   B N   1 
ATOM   1527 C  CA  . THR   B 1 90  ? 14.441  -60.875 8.324   1.00 77.83  ? 405 THR   B CA  1 
ATOM   1528 C  C   . THR   B 1 90  ? 13.801  -62.081 9.015   1.00 85.83  ? 405 THR   B C   1 
ATOM   1529 O  O   . THR   B 1 90  ? 12.605  -62.052 9.301   1.00 87.97  ? 405 THR   B O   1 
ATOM   1530 C  CB  . THR   B 1 90  ? 13.777  -60.568 6.981   1.00 75.50  ? 405 THR   B CB  1 
ATOM   1531 O  OG1 . THR   B 1 90  ? 14.070  -61.664 6.122   1.00 75.75  ? 405 THR   B OG1 1 
ATOM   1532 C  CG2 . THR   B 1 90  ? 14.289  -59.279 6.364   1.00 74.68  ? 405 THR   B CG2 1 
ATOM   1533 N  N   . LYS   B 1 91  ? 14.592  -63.133 9.278   1.00 92.60  ? 406 LYS   B N   1 
ATOM   1534 C  CA  . LYS   B 1 91  ? 14.156  -64.262 10.089  1.00 97.34  ? 406 LYS   B CA  1 
ATOM   1535 C  C   . LYS   B 1 91  ? 15.322  -64.738 10.952  1.00 99.69  ? 406 LYS   B C   1 
ATOM   1536 O  O   . LYS   B 1 91  ? 16.476  -64.416 10.676  1.00 100.79 ? 406 LYS   B O   1 
ATOM   1537 C  CB  . LYS   B 1 91  ? 13.638  -65.422 9.230   1.00 98.98  ? 406 LYS   B CB  1 
ATOM   1538 C  CG  . LYS   B 1 91  ? 12.303  -65.182 8.537   1.00 100.81 ? 406 LYS   B CG  1 
ATOM   1539 C  CD  . LYS   B 1 91  ? 12.144  -65.840 7.170   1.00 102.26 ? 406 LYS   B CD  1 
ATOM   1540 C  CE  . LYS   B 1 91  ? 13.062  -65.281 6.120   1.00 102.53 ? 406 LYS   B CE  1 
ATOM   1541 N  NZ  . LYS   B 1 91  ? 14.315  -66.028 5.977   1.00 102.34 ? 406 LYS   B NZ  1 
ATOM   1542 N  N   . LYS   B 1 92  ? 14.998  -65.532 11.980  1.00 99.83  ? 407 LYS   B N   1 
ATOM   1543 C  CA  . LYS   B 1 92  ? 15.955  -65.922 13.005  1.00 98.93  ? 407 LYS   B CA  1 
ATOM   1544 C  C   . LYS   B 1 92  ? 16.951  -66.955 12.476  1.00 98.39  ? 407 LYS   B C   1 
ATOM   1545 O  O   . LYS   B 1 92  ? 18.057  -67.069 13.001  1.00 97.16  ? 407 LYS   B O   1 
ATOM   1546 C  CB  . LYS   B 1 92  ? 15.206  -66.481 14.221  1.00 96.49  ? 407 LYS   B CB  1 
ATOM   1547 N  N   . ASP   B 1 93  ? 16.565  -67.694 11.428  1.00 98.59  ? 408 ASP   B N   1 
ATOM   1548 C  CA  . ASP   B 1 93  ? 17.271  -68.906 11.039  1.00 99.47  ? 408 ASP   B CA  1 
ATOM   1549 C  C   . ASP   B 1 93  ? 18.467  -68.608 10.132  1.00 98.27  ? 408 ASP   B C   1 
ATOM   1550 O  O   . ASP   B 1 93  ? 19.282  -69.498 9.898   1.00 98.54  ? 408 ASP   B O   1 
ATOM   1551 C  CB  . ASP   B 1 93  ? 16.322  -69.918 10.414  1.00 100.75 ? 408 ASP   B CB  1 
ATOM   1552 C  CG  . ASP   B 1 93  ? 15.478  -69.411 9.254   1.00 101.67 ? 408 ASP   B CG  1 
ATOM   1553 O  OD1 . ASP   B 1 93  ? 14.740  -68.424 9.455   1.00 102.80 ? 408 ASP   B OD1 1 
ATOM   1554 O  OD2 . ASP   B 1 93  ? 15.557  -70.012 8.162   1.00 101.24 ? 408 ASP   B OD2 1 
ATOM   1555 N  N   . MET   B 1 94  ? 18.581  -67.371 9.627   1.00 96.43  ? 409 MET   B N   1 
ATOM   1556 C  CA  . MET   B 1 94  ? 19.621  -67.028 8.667   1.00 94.15  ? 409 MET   B CA  1 
ATOM   1557 C  C   . MET   B 1 94  ? 20.969  -66.884 9.373   1.00 90.74  ? 409 MET   B C   1 
ATOM   1558 O  O   . MET   B 1 94  ? 21.029  -66.799 10.598  1.00 89.88  ? 409 MET   B O   1 
ATOM   1559 C  CB  . MET   B 1 94  ? 19.273  -65.732 7.928   1.00 94.25  ? 409 MET   B CB  1 
ATOM   1560 C  CG  . MET   B 1 94  ? 18.030  -65.842 7.064   1.00 95.15  ? 409 MET   B CG  1 
ATOM   1561 S  SD  . MET   B 1 94  ? 17.446  -64.254 6.439   1.00 96.86  ? 409 MET   B SD  1 
ATOM   1562 C  CE  . MET   B 1 94  ? 18.901  -63.658 5.567   1.00 96.09  ? 409 MET   B CE  1 
ATOM   1563 N  N   . SER   B 1 95  ? 22.047  -66.870 8.577   1.00 86.72  ? 410 SER   B N   1 
ATOM   1564 C  CA  . SER   B 1 95  ? 23.407  -66.776 9.084   1.00 85.72  ? 410 SER   B CA  1 
ATOM   1565 C  C   . SER   B 1 95  ? 24.409  -66.364 8.006   1.00 83.60  ? 410 SER   B C   1 
ATOM   1566 O  O   . SER   B 1 95  ? 24.552  -67.069 7.010   1.00 83.02  ? 410 SER   B O   1 
ATOM   1567 C  CB  . SER   B 1 95  ? 23.829  -68.078 9.720   1.00 86.07  ? 410 SER   B CB  1 
ATOM   1568 O  OG  . SER   B 1 95  ? 25.144  -67.987 10.251  1.00 85.82  ? 410 SER   B OG  1 
ATOM   1569 N  N   . PRO   B 1 96  ? 25.151  -65.236 8.153   1.00 82.66  ? 411 PRO   B N   1 
ATOM   1570 C  CA  . PRO   B 1 96  ? 25.075  -64.376 9.331   1.00 82.78  ? 411 PRO   B CA  1 
ATOM   1571 C  C   . PRO   B 1 96  ? 23.769  -63.593 9.438   1.00 82.94  ? 411 PRO   B C   1 
ATOM   1572 O  O   . PRO   B 1 96  ? 23.020  -63.490 8.468   1.00 84.31  ? 411 PRO   B O   1 
ATOM   1573 C  CB  . PRO   B 1 96  ? 26.272  -63.441 9.171   1.00 81.63  ? 411 PRO   B CB  1 
ATOM   1574 C  CG  . PRO   B 1 96  ? 26.463  -63.379 7.668   1.00 82.16  ? 411 PRO   B CG  1 
ATOM   1575 C  CD  . PRO   B 1 96  ? 26.119  -64.745 7.159   1.00 82.69  ? 411 PRO   B CD  1 
ATOM   1576 N  N   . GLN   B 1 97  ? 23.512  -63.048 10.634  1.00 81.12  ? 412 GLN   B N   1 
ATOM   1577 C  CA  . GLN   B 1 97  ? 22.291  -62.308 10.912  1.00 79.14  ? 412 GLN   B CA  1 
ATOM   1578 C  C   . GLN   B 1 97  ? 22.446  -60.852 10.478  1.00 77.34  ? 412 GLN   B C   1 
ATOM   1579 O  O   . GLN   B 1 97  ? 21.468  -60.228 10.067  1.00 74.58  ? 412 GLN   B O   1 
ATOM   1580 C  CB  . GLN   B 1 97  ? 21.915  -62.429 12.390  1.00 78.85  ? 412 GLN   B CB  1 
ATOM   1581 C  CG  . GLN   B 1 97  ? 21.181  -63.721 12.733  1.00 78.19  ? 412 GLN   B CG  1 
ATOM   1582 C  CD  . GLN   B 1 97  ? 19.753  -63.739 12.232  1.00 77.94  ? 412 GLN   B CD  1 
ATOM   1583 O  OE1 . GLN   B 1 97  ? 19.402  -64.471 11.300  1.00 78.30  ? 412 GLN   B OE1 1 
ATOM   1584 N  NE2 . GLN   B 1 97  ? 18.912  -62.915 12.842  1.00 77.22  ? 412 GLN   B NE2 1 
ATOM   1585 N  N   . LYS   B 1 98  ? 23.670  -60.316 10.580  1.00 77.32  ? 413 LYS   B N   1 
ATOM   1586 C  CA  . LYS   B 1 98  ? 23.958  -58.978 10.089  1.00 77.18  ? 413 LYS   B CA  1 
ATOM   1587 C  C   . LYS   B 1 98  ? 25.361  -58.935 9.485   1.00 75.42  ? 413 LYS   B C   1 
ATOM   1588 O  O   . LYS   B 1 98  ? 26.243  -59.697 9.879   1.00 74.65  ? 413 LYS   B O   1 
ATOM   1589 C  CB  . LYS   B 1 98  ? 23.728  -57.933 11.191  1.00 79.45  ? 413 LYS   B CB  1 
ATOM   1590 C  CG  . LYS   B 1 98  ? 24.542  -58.068 12.476  1.00 81.70  ? 413 LYS   B CG  1 
ATOM   1591 C  CD  . LYS   B 1 98  ? 25.960  -57.509 12.411  1.00 83.74  ? 413 LYS   B CD  1 
ATOM   1592 C  CE  . LYS   B 1 98  ? 26.680  -57.606 13.718  1.00 85.14  ? 413 LYS   B CE  1 
ATOM   1593 N  NZ  . LYS   B 1 98  ? 28.128  -57.471 13.540  1.00 85.52  ? 413 LYS   B NZ  1 
ATOM   1594 N  N   . PHE   B 1 99  ? 25.533  -58.041 8.502   1.00 73.11  ? 414 PHE   B N   1 
ATOM   1595 C  CA  . PHE   B 1 99  ? 26.819  -57.770 7.878   1.00 69.60  ? 414 PHE   B CA  1 
ATOM   1596 C  C   . PHE   B 1 99  ? 26.740  -56.390 7.228   1.00 68.12  ? 414 PHE   B C   1 
ATOM   1597 O  O   . PHE   B 1 99  ? 25.714  -55.720 7.325   1.00 66.18  ? 414 PHE   B O   1 
ATOM   1598 C  CB  . PHE   B 1 99  ? 27.178  -58.877 6.879   1.00 68.37  ? 414 PHE   B CB  1 
ATOM   1599 C  CG  . PHE   B 1 99  ? 26.353  -58.882 5.599   1.00 67.63  ? 414 PHE   B CG  1 
ATOM   1600 C  CD1 . PHE   B 1 99  ? 25.150  -59.578 5.526   1.00 67.07  ? 414 PHE   B CD1 1 
ATOM   1601 C  CD2 . PHE   B 1 99  ? 26.783  -58.191 4.469   1.00 67.26  ? 414 PHE   B CD2 1 
ATOM   1602 C  CE1 . PHE   B 1 99  ? 24.400  -59.577 4.359   1.00 66.45  ? 414 PHE   B CE1 1 
ATOM   1603 C  CE2 . PHE   B 1 99  ? 26.029  -58.194 3.305   1.00 66.40  ? 414 PHE   B CE2 1 
ATOM   1604 C  CZ  . PHE   B 1 99  ? 24.841  -58.886 3.252   1.00 66.55  ? 414 PHE   B CZ  1 
ATOM   1605 N  N   . TRP   B 1 100 ? 27.829  -55.977 6.566   1.00 69.11  ? 415 TRP   B N   1 
ATOM   1606 C  CA  . TRP   B 1 100 ? 27.905  -54.670 5.932   1.00 70.10  ? 415 TRP   B CA  1 
ATOM   1607 C  C   . TRP   B 1 100 ? 28.352  -54.820 4.479   1.00 71.17  ? 415 TRP   B C   1 
ATOM   1608 O  O   . TRP   B 1 100 ? 29.220  -55.637 4.181   1.00 72.33  ? 415 TRP   B O   1 
ATOM   1609 C  CB  . TRP   B 1 100 ? 28.876  -53.759 6.697   1.00 70.09  ? 415 TRP   B CB  1 
ATOM   1610 C  CG  . TRP   B 1 100 ? 28.654  -53.716 8.186   1.00 69.90  ? 415 TRP   B CG  1 
ATOM   1611 C  CD1 . TRP   B 1 100 ? 28.993  -54.680 9.089   1.00 71.01  ? 415 TRP   B CD1 1 
ATOM   1612 C  CD2 . TRP   B 1 100 ? 28.074  -52.637 8.952   1.00 68.82  ? 415 TRP   B CD2 1 
ATOM   1613 N  NE1 . TRP   B 1 100 ? 28.649  -54.291 10.355  1.00 71.48  ? 415 TRP   B NE1 1 
ATOM   1614 C  CE2 . TRP   B 1 100 ? 28.089  -53.043 10.305  1.00 69.96  ? 415 TRP   B CE2 1 
ATOM   1615 C  CE3 . TRP   B 1 100 ? 27.545  -51.383 8.632   1.00 69.08  ? 415 TRP   B CE3 1 
ATOM   1616 C  CZ2 . TRP   B 1 100 ? 27.595  -52.238 11.329  1.00 70.57  ? 415 TRP   B CZ2 1 
ATOM   1617 C  CZ3 . TRP   B 1 100 ? 27.061  -50.586 9.646   1.00 69.97  ? 415 TRP   B CZ3 1 
ATOM   1618 C  CH2 . TRP   B 1 100 ? 27.087  -51.009 10.976  1.00 70.43  ? 415 TRP   B CH2 1 
ATOM   1619 N  N   . GLY   B 1 101 ? 27.750  -54.019 3.590   1.00 70.41  ? 416 GLY   B N   1 
ATOM   1620 C  CA  . GLY   B 1 101 ? 28.198  -53.887 2.212   1.00 68.62  ? 416 GLY   B CA  1 
ATOM   1621 C  C   . GLY   B 1 101 ? 28.687  -52.466 1.942   1.00 67.71  ? 416 GLY   B C   1 
ATOM   1622 O  O   . GLY   B 1 101 ? 27.898  -51.524 1.987   1.00 65.70  ? 416 GLY   B O   1 
ATOM   1623 N  N   . LEU   B 1 102 ? 29.988  -52.329 1.655   1.00 67.90  ? 417 LEU   B N   1 
ATOM   1624 C  CA  . LEU   B 1 102 ? 30.647  -51.033 1.596   1.00 68.52  ? 417 LEU   B CA  1 
ATOM   1625 C  C   . LEU   B 1 102 ? 31.012  -50.691 0.155   1.00 67.92  ? 417 LEU   B C   1 
ATOM   1626 O  O   . LEU   B 1 102 ? 31.430  -51.562 -0.603  1.00 67.19  ? 417 LEU   B O   1 
ATOM   1627 C  CB  . LEU   B 1 102 ? 31.902  -51.064 2.466   1.00 69.53  ? 417 LEU   B CB  1 
ATOM   1628 C  CG  . LEU   B 1 102 ? 31.748  -51.665 3.866   1.00 71.08  ? 417 LEU   B CG  1 
ATOM   1629 C  CD1 . LEU   B 1 102 ? 33.066  -51.553 4.615   1.00 71.33  ? 417 LEU   B CD1 1 
ATOM   1630 C  CD2 . LEU   B 1 102 ? 30.623  -51.010 4.649   1.00 72.05  ? 417 LEU   B CD2 1 
ATOM   1631 N  N   . THR   B 1 103 ? 30.881  -49.406 -0.196  1.00 68.88  ? 418 THR   B N   1 
ATOM   1632 C  CA  . THR   B 1 103 ? 31.363  -48.897 -1.470  1.00 69.92  ? 418 THR   B CA  1 
ATOM   1633 C  C   . THR   B 1 103 ? 32.890  -48.876 -1.430  1.00 72.08  ? 418 THR   B C   1 
ATOM   1634 O  O   . THR   B 1 103 ? 33.476  -48.199 -0.586  1.00 72.30  ? 418 THR   B O   1 
ATOM   1635 C  CB  . THR   B 1 103 ? 30.773  -47.507 -1.716  1.00 68.23  ? 418 THR   B CB  1 
ATOM   1636 O  OG1 . THR   B 1 103 ? 29.359  -47.670 -1.651  1.00 66.67  ? 418 THR   B OG1 1 
ATOM   1637 C  CG2 . THR   B 1 103 ? 31.170  -46.926 -3.062  1.00 67.43  ? 418 THR   B CG2 1 
ATOM   1638 N  N   . ARG   B 1 104 ? 33.524  -49.626 -2.343  1.00 73.88  ? 419 ARG   B N   1 
ATOM   1639 C  CA  . ARG   B 1 104 ? 34.971  -49.786 -2.352  1.00 74.61  ? 419 ARG   B CA  1 
ATOM   1640 C  C   . ARG   B 1 104 ? 35.654  -48.452 -2.646  1.00 71.83  ? 419 ARG   B C   1 
ATOM   1641 O  O   . ARG   B 1 104 ? 36.732  -48.179 -2.119  1.00 70.11  ? 419 ARG   B O   1 
ATOM   1642 C  CB  . ARG   B 1 104 ? 35.419  -50.841 -3.371  1.00 76.95  ? 419 ARG   B CB  1 
ATOM   1643 C  CG  . ARG   B 1 104 ? 34.972  -52.257 -3.035  1.00 79.04  ? 419 ARG   B CG  1 
ATOM   1644 C  CD  . ARG   B 1 104 ? 35.706  -53.313 -3.849  1.00 81.33  ? 419 ARG   B CD  1 
ATOM   1645 N  NE  . ARG   B 1 104 ? 35.589  -53.100 -5.296  1.00 83.91  ? 419 ARG   B NE  1 
ATOM   1646 C  CZ  . ARG   B 1 104 ? 34.797  -53.770 -6.131  1.00 84.85  ? 419 ARG   B CZ  1 
ATOM   1647 N  NH1 . ARG   B 1 104 ? 33.906  -54.634 -5.672  1.00 85.43  ? 419 ARG   B NH1 1 
ATOM   1648 N  NH2 . ARG   B 1 104 ? 34.872  -53.544 -7.432  1.00 84.55  ? 419 ARG   B NH2 1 
ATOM   1649 N  N   . SER   B 1 105 ? 35.007  -47.622 -3.474  1.00 70.04  ? 420 SER   B N   1 
ATOM   1650 C  CA  . SER   B 1 105 ? 35.548  -46.331 -3.865  1.00 69.86  ? 420 SER   B CA  1 
ATOM   1651 C  C   . SER   B 1 105 ? 35.391  -45.297 -2.749  1.00 69.04  ? 420 SER   B C   1 
ATOM   1652 O  O   . SER   B 1 105 ? 35.749  -44.138 -2.943  1.00 68.96  ? 420 SER   B O   1 
ATOM   1653 C  CB  . SER   B 1 105 ? 34.897  -45.845 -5.136  1.00 70.06  ? 420 SER   B CB  1 
ATOM   1654 O  OG  . SER   B 1 105 ? 33.510  -45.608 -4.940  1.00 69.66  ? 420 SER   B OG  1 
ATOM   1655 N  N   . ALA   B 1 106 ? 34.857  -45.713 -1.592  1.00 68.32  ? 421 ALA   B N   1 
ATOM   1656 C  CA  . ALA   B 1 106 ? 34.669  -44.821 -0.459  1.00 67.48  ? 421 ALA   B CA  1 
ATOM   1657 C  C   . ALA   B 1 106 ? 35.650  -45.152 0.666   1.00 67.60  ? 421 ALA   B C   1 
ATOM   1658 O  O   . ALA   B 1 106 ? 35.465  -44.696 1.792   1.00 67.94  ? 421 ALA   B O   1 
ATOM   1659 C  CB  . ALA   B 1 106 ? 33.235  -44.912 0.020   1.00 66.65  ? 421 ALA   B CB  1 
ATOM   1660 N  N   . LEU   B 1 107 ? 36.700  -45.923 0.354   1.00 68.27  ? 422 LEU   B N   1 
ATOM   1661 C  CA  . LEU   B 1 107 ? 37.611  -46.425 1.371   1.00 69.72  ? 422 LEU   B CA  1 
ATOM   1662 C  C   . LEU   B 1 107 ? 39.059  -46.272 0.911   1.00 72.04  ? 422 LEU   B C   1 
ATOM   1663 O  O   . LEU   B 1 107 ? 39.320  -46.043 -0.268  1.00 71.43  ? 422 LEU   B O   1 
ATOM   1664 C  CB  . LEU   B 1 107 ? 37.272  -47.885 1.666   1.00 69.78  ? 422 LEU   B CB  1 
ATOM   1665 C  CG  . LEU   B 1 107 ? 35.932  -48.142 2.362   1.00 70.10  ? 422 LEU   B CG  1 
ATOM   1666 C  CD1 . LEU   B 1 107 ? 35.644  -49.631 2.413   1.00 70.72  ? 422 LEU   B CD1 1 
ATOM   1667 C  CD2 . LEU   B 1 107 ? 35.906  -47.549 3.762   1.00 70.15  ? 422 LEU   B CD2 1 
ATOM   1668 N  N   . LEU   B 1 108 ? 39.987  -46.415 1.868   1.00 76.32  ? 423 LEU   B N   1 
ATOM   1669 C  CA  . LEU   B 1 108 ? 41.418  -46.336 1.613   1.00 81.11  ? 423 LEU   B CA  1 
ATOM   1670 C  C   . LEU   B 1 108 ? 42.229  -47.402 2.350   1.00 85.84  ? 423 LEU   B C   1 
ATOM   1671 O  O   . LEU   B 1 108 ? 42.131  -47.511 3.570   1.00 86.00  ? 423 LEU   B O   1 
ATOM   1672 C  CB  . LEU   B 1 108 ? 41.907  -44.937 1.987   1.00 80.42  ? 423 LEU   B CB  1 
ATOM   1673 C  CG  . LEU   B 1 108 ? 41.643  -43.831 0.961   1.00 80.73  ? 423 LEU   B CG  1 
ATOM   1674 C  CD1 . LEU   B 1 108 ? 42.129  -42.498 1.503   1.00 80.32  ? 423 LEU   B CD1 1 
ATOM   1675 C  CD2 . LEU   B 1 108 ? 42.301  -44.129 -0.379  1.00 81.08  ? 423 LEU   B CD2 1 
ATOM   1676 N  N   . PRO   B 1 109 ? 43.058  -48.217 1.650   1.00 91.88  ? 424 PRO   B N   1 
ATOM   1677 C  CA  . PRO   B 1 109 ? 43.110  -48.229 0.190   1.00 95.91  ? 424 PRO   B CA  1 
ATOM   1678 C  C   . PRO   B 1 109 ? 41.841  -48.795 -0.448  1.00 101.27 ? 424 PRO   B C   1 
ATOM   1679 O  O   . PRO   B 1 109 ? 41.195  -49.668 0.129   1.00 106.47 ? 424 PRO   B O   1 
ATOM   1680 C  CB  . PRO   B 1 109 ? 44.343  -49.078 -0.119  1.00 95.04  ? 424 PRO   B CB  1 
ATOM   1681 C  CG  . PRO   B 1 109 ? 44.466  -49.981 1.094   1.00 94.34  ? 424 PRO   B CG  1 
ATOM   1682 C  CD  . PRO   B 1 109 ? 44.014  -49.156 2.260   1.00 92.66  ? 424 PRO   B CD  1 
ATOM   1683 N  N   . THR   B 1 110 ? 41.498  -48.283 -1.638  1.00 101.33 ? 425 THR   B N   1 
ATOM   1684 C  CA  . THR   B 1 110 ? 40.263  -48.637 -2.326  1.00 99.78  ? 425 THR   B CA  1 
ATOM   1685 C  C   . THR   B 1 110 ? 40.119  -50.147 -2.374  1.00 98.21  ? 425 THR   B C   1 
ATOM   1686 O  O   . THR   B 1 110 ? 40.911  -50.776 -3.111  1.00 96.89  ? 425 THR   B O   1 
ATOM   1687 C  CB  . THR   B 1 110 ? 40.267  -48.020 -3.725  1.00 98.28  ? 425 THR   B CB  1 
ATOM   1688 O  OG1 . THR   B 1 110 ? 40.263  -46.611 -3.516  1.00 97.85  ? 425 THR   B OG1 1 
ATOM   1689 C  CG2 . THR   B 1 110 ? 39.059  -48.411 -4.559  1.00 97.39  ? 425 THR   B CG2 1 
ATOM   1690 N  N   . SER   C 1 3   ? 6.726   3.908   8.323   1.00 105.11 ? 318 SER   C N   1 
ATOM   1691 C  CA  . SER   C 1 3   ? 7.166   4.176   9.719   1.00 104.25 ? 318 SER   C CA  1 
ATOM   1692 C  C   . SER   C 1 3   ? 8.286   3.213   10.111  1.00 101.48 ? 318 SER   C C   1 
ATOM   1693 O  O   . SER   C 1 3   ? 8.033   2.048   10.416  1.00 100.73 ? 318 SER   C O   1 
ATOM   1694 C  CB  . SER   C 1 3   ? 6.004   4.091   10.688  1.00 103.06 ? 318 SER   C CB  1 
ATOM   1695 O  OG  . SER   C 1 3   ? 6.403   4.443   12.007  1.00 101.01 ? 318 SER   C OG  1 
ATOM   1696 N  N   . THR   C 1 4   ? 9.526   3.718   10.089  1.00 95.57  ? 319 THR   C N   1 
ATOM   1697 C  CA  . THR   C 1 4   ? 10.650  3.044   10.720  1.00 89.52  ? 319 THR   C CA  1 
ATOM   1698 C  C   . THR   C 1 4   ? 10.772  3.537   12.162  1.00 83.28  ? 319 THR   C C   1 
ATOM   1699 O  O   . THR   C 1 4   ? 11.863  3.532   12.721  1.00 83.03  ? 319 THR   C O   1 
ATOM   1700 C  CB  . THR   C 1 4   ? 11.935  3.294   9.925   1.00 89.26  ? 319 THR   C CB  1 
ATOM   1701 O  OG1 . THR   C 1 4   ? 12.021  4.698   9.703   1.00 87.95  ? 319 THR   C OG1 1 
ATOM   1702 C  CG2 . THR   C 1 4   ? 11.960  2.569   8.591   1.00 88.65  ? 319 THR   C CG2 1 
ATOM   1703 N  N   . SER   C 1 5   ? 9.644   3.928   12.770  1.00 77.15  ? 320 SER   C N   1 
ATOM   1704 C  CA  . SER   C 1 5   ? 9.649   4.645   14.035  1.00 74.27  ? 320 SER   C CA  1 
ATOM   1705 C  C   . SER   C 1 5   ? 8.993   3.802   15.124  1.00 72.59  ? 320 SER   C C   1 
ATOM   1706 O  O   . SER   C 1 5   ? 8.075   3.034   14.845  1.00 73.75  ? 320 SER   C O   1 
ATOM   1707 C  CB  . SER   C 1 5   ? 8.959   5.975   13.894  1.00 73.98  ? 320 SER   C CB  1 
ATOM   1708 O  OG  . SER   C 1 5   ? 8.962   6.681   15.127  1.00 73.21  ? 320 SER   C OG  1 
ATOM   1709 N  N   . LEU   C 1 6   ? 9.467   3.976   16.365  1.00 70.77  ? 321 LEU   C N   1 
ATOM   1710 C  CA  . LEU   C 1 6   ? 8.987   3.209   17.504  1.00 69.57  ? 321 LEU   C CA  1 
ATOM   1711 C  C   . LEU   C 1 6   ? 8.669   4.154   18.659  1.00 67.49  ? 321 LEU   C C   1 
ATOM   1712 O  O   . LEU   C 1 6   ? 9.525   4.926   19.083  1.00 66.12  ? 321 LEU   C O   1 
ATOM   1713 C  CB  . LEU   C 1 6   ? 10.035  2.171   17.902  1.00 70.54  ? 321 LEU   C CB  1 
ATOM   1714 C  CG  . LEU   C 1 6   ? 10.194  0.980   16.953  1.00 71.70  ? 321 LEU   C CG  1 
ATOM   1715 C  CD1 . LEU   C 1 6   ? 11.424  0.169   17.316  1.00 72.44  ? 321 LEU   C CD1 1 
ATOM   1716 C  CD2 . LEU   C 1 6   ? 8.958   0.096   16.964  1.00 71.96  ? 321 LEU   C CD2 1 
ATOM   1717 N  N   . SER   C 1 7   ? 7.438   4.052   19.177  1.00 67.31  ? 322 SER   C N   1 
ATOM   1718 C  CA  . SER   C 1 7   ? 6.903   5.020   20.122  1.00 67.47  ? 322 SER   C CA  1 
ATOM   1719 C  C   . SER   C 1 7   ? 6.620   4.363   21.471  1.00 66.65  ? 322 SER   C C   1 
ATOM   1720 O  O   . SER   C 1 7   ? 6.440   3.151   21.547  1.00 65.27  ? 322 SER   C O   1 
ATOM   1721 C  CB  . SER   C 1 7   ? 5.654   5.665   19.577  1.00 68.02  ? 322 SER   C CB  1 
ATOM   1722 O  OG  . SER   C 1 7   ? 5.913   6.347   18.359  1.00 68.96  ? 322 SER   C OG  1 
ATOM   1723 N  N   . CYS   C 1 8   ? 6.572   5.194   22.521  1.00 66.02  ? 323 CYS   C N   1 
ATOM   1724 C  CA  . CYS   C 1 8   ? 6.151   4.772   23.849  1.00 65.33  ? 323 CYS   C CA  1 
ATOM   1725 C  C   . CYS   C 1 8   ? 4.704   4.294   23.791  1.00 64.97  ? 323 CYS   C C   1 
ATOM   1726 O  O   . CYS   C 1 8   ? 3.837   5.001   23.288  1.00 62.05  ? 323 CYS   C O   1 
ATOM   1727 C  CB  . CYS   C 1 8   ? 6.285   5.913   24.853  1.00 65.62  ? 323 CYS   C CB  1 
ATOM   1728 S  SG  . CYS   C 1 8   ? 5.612   5.541   26.495  1.00 63.88  ? 323 CYS   C SG  1 
ATOM   1729 N  N   . LYS   C 1 9   ? 4.455   3.090   24.315  1.00 67.03  ? 324 LYS   C N   1 
ATOM   1730 C  CA  . LYS   C 1 9   ? 3.140   2.476   24.238  1.00 69.22  ? 324 LYS   C CA  1 
ATOM   1731 C  C   . LYS   C 1 9   ? 2.121   3.287   25.037  1.00 70.81  ? 324 LYS   C C   1 
ATOM   1732 O  O   . LYS   C 1 9   ? 0.965   3.385   24.633  1.00 70.98  ? 324 LYS   C O   1 
ATOM   1733 C  CB  . LYS   C 1 9   ? 3.204   1.024   24.725  1.00 70.12  ? 324 LYS   C CB  1 
ATOM   1734 C  CG  . LYS   C 1 9   ? 1.857   0.323   24.867  1.00 70.97  ? 324 LYS   C CG  1 
ATOM   1735 C  CD  . LYS   C 1 9   ? 1.960   -1.196  24.919  1.00 71.36  ? 324 LYS   C CD  1 
ATOM   1736 C  CE  . LYS   C 1 9   ? 2.226   -1.788  23.572  1.00 71.87  ? 324 LYS   C CE  1 
ATOM   1737 N  NZ  . LYS   C 1 9   ? 2.702   -3.169  23.670  1.00 73.06  ? 324 LYS   C NZ  1 
ATOM   1738 N  N   . GLN   C 1 10  ? 2.560   3.866   26.164  1.00 72.98  ? 325 GLN   C N   1 
ATOM   1739 C  CA  . GLN   C 1 10  ? 1.651   4.494   27.110  1.00 73.62  ? 325 GLN   C CA  1 
ATOM   1740 C  C   . GLN   C 1 10  ? 1.146   5.822   26.547  1.00 72.51  ? 325 GLN   C C   1 
ATOM   1741 O  O   . GLN   C 1 10  ? -0.057  5.992   26.363  1.00 73.81  ? 325 GLN   C O   1 
ATOM   1742 C  CB  . GLN   C 1 10  ? 2.310   4.667   28.479  1.00 75.21  ? 325 GLN   C CB  1 
ATOM   1743 C  CG  . GLN   C 1 10  ? 1.310   4.810   29.622  1.00 78.16  ? 325 GLN   C CG  1 
ATOM   1744 C  CD  . GLN   C 1 10  ? 1.960   5.095   30.959  1.00 81.09  ? 325 GLN   C CD  1 
ATOM   1745 O  OE1 . GLN   C 1 10  ? 2.663   4.252   31.528  1.00 81.76  ? 325 GLN   C OE1 1 
ATOM   1746 N  NE2 . GLN   C 1 10  ? 1.719   6.287   31.488  1.00 82.35  ? 325 GLN   C NE2 1 
ATOM   1747 N  N   . CYS   C 1 11  ? 2.069   6.752   26.267  1.00 70.69  ? 326 CYS   C N   1 
ATOM   1748 C  CA  . CYS   C 1 11  ? 1.704   8.098   25.845  1.00 69.73  ? 326 CYS   C CA  1 
ATOM   1749 C  C   . CYS   C 1 11  ? 1.585   8.185   24.323  1.00 71.42  ? 326 CYS   C C   1 
ATOM   1750 O  O   . CYS   C 1 11  ? 0.905   9.072   23.814  1.00 70.95  ? 326 CYS   C O   1 
ATOM   1751 C  CB  . CYS   C 1 11  ? 2.674   9.135   26.399  1.00 68.06  ? 326 CYS   C CB  1 
ATOM   1752 S  SG  . CYS   C 1 11  ? 4.385   8.897   25.858  1.00 65.65  ? 326 CYS   C SG  1 
ATOM   1753 N  N   . GLN   C 1 12  ? 2.285   7.296   23.603  1.00 75.42  ? 327 GLN   C N   1 
ATOM   1754 C  CA  . GLN   C 1 12  ? 2.033   7.034   22.189  1.00 78.06  ? 327 GLN   C CA  1 
ATOM   1755 C  C   . GLN   C 1 12  ? 2.640   8.106   21.282  1.00 79.92  ? 327 GLN   C C   1 
ATOM   1756 O  O   . GLN   C 1 12  ? 2.907   7.830   20.114  1.00 81.04  ? 327 GLN   C O   1 
ATOM   1757 C  CB  . GLN   C 1 12  ? 0.542   6.885   21.880  1.00 79.11  ? 327 GLN   C CB  1 
ATOM   1758 C  CG  . GLN   C 1 12  ? -0.162  5.836   22.734  1.00 80.51  ? 327 GLN   C CG  1 
ATOM   1759 C  CD  . GLN   C 1 12  ? -1.580  5.558   22.287  1.00 81.12  ? 327 GLN   C CD  1 
ATOM   1760 O  OE1 . GLN   C 1 12  ? -2.546  5.807   23.017  1.00 81.20  ? 327 GLN   C OE1 1 
ATOM   1761 N  NE2 . GLN   C 1 12  ? -1.718  5.036   21.077  1.00 81.62  ? 327 GLN   C NE2 1 
ATOM   1762 N  N   . GLU   C 1 13  ? 2.861   9.316   21.812  1.00 80.97  ? 328 GLU   C N   1 
ATOM   1763 C  CA  . GLU   C 1 13  ? 3.239   10.461  20.998  1.00 82.61  ? 328 GLU   C CA  1 
ATOM   1764 C  C   . GLU   C 1 13  ? 4.755   10.524  20.806  1.00 80.31  ? 328 GLU   C C   1 
ATOM   1765 O  O   . GLU   C 1 13  ? 5.234   11.160  19.869  1.00 80.37  ? 328 GLU   C O   1 
ATOM   1766 C  CB  . GLU   C 1 13  ? 2.716   11.737  21.660  1.00 85.12  ? 328 GLU   C CB  1 
ATOM   1767 C  CG  . GLU   C 1 13  ? 3.503   12.154  22.901  1.00 86.38  ? 328 GLU   C CG  1 
ATOM   1768 C  CD  . GLU   C 1 13  ? 2.781   13.113  23.832  1.00 88.09  ? 328 GLU   C CD  1 
ATOM   1769 O  OE1 . GLU   C 1 13  ? 1.560   13.315  23.671  1.00 89.32  ? 328 GLU   C OE1 1 
ATOM   1770 O  OE2 . GLU   C 1 13  ? 3.454   13.671  24.724  1.00 89.77  ? 328 GLU   C OE2 1 
ATOM   1771 N  N   . THR   C 1 14  ? 5.503   9.860   21.696  1.00 76.25  ? 329 THR   C N   1 
ATOM   1772 C  CA  . THR   C 1 14  ? 6.938   10.062  21.814  1.00 72.37  ? 329 THR   C CA  1 
ATOM   1773 C  C   . THR   C 1 14  ? 7.683   9.012   20.994  1.00 69.66  ? 329 THR   C C   1 
ATOM   1774 O  O   . THR   C 1 14  ? 7.500   7.817   21.211  1.00 68.82  ? 329 THR   C O   1 
ATOM   1775 C  CB  . THR   C 1 14  ? 7.307   9.988   23.294  1.00 72.02  ? 329 THR   C CB  1 
ATOM   1776 O  OG1 . THR   C 1 14  ? 6.523   11.010  23.901  1.00 71.90  ? 329 THR   C OG1 1 
ATOM   1777 C  CG2 . THR   C 1 14  ? 8.784   10.224  23.553  1.00 71.70  ? 329 THR   C CG2 1 
ATOM   1778 N  N   . GLU   C 1 15  ? 8.528   9.477   20.064  1.00 66.91  ? 330 GLU   C N   1 
ATOM   1779 C  CA  . GLU   C 1 15  ? 9.443   8.609   19.339  1.00 66.31  ? 330 GLU   C CA  1 
ATOM   1780 C  C   . GLU   C 1 15  ? 10.641  8.299   20.232  1.00 64.70  ? 330 GLU   C C   1 
ATOM   1781 O  O   . GLU   C 1 15  ? 11.276  9.213   20.753  1.00 63.90  ? 330 GLU   C O   1 
ATOM   1782 C  CB  . GLU   C 1 15  ? 9.911   9.252   18.033  1.00 67.97  ? 330 GLU   C CB  1 
ATOM   1783 C  CG  . GLU   C 1 15  ? 11.086  8.524   17.383  1.00 69.89  ? 330 GLU   C CG  1 
ATOM   1784 C  CD  . GLU   C 1 15  ? 11.467  9.035   16.007  1.00 71.18  ? 330 GLU   C CD  1 
ATOM   1785 O  OE1 . GLU   C 1 15  ? 10.621  8.948   15.093  1.00 72.36  ? 330 GLU   C OE1 1 
ATOM   1786 O  OE2 . GLU   C 1 15  ? 12.609  9.517   15.850  1.00 73.04  ? 330 GLU   C OE2 1 
ATOM   1787 N  N   . ILE   C 1 16  ? 10.945  7.004   20.386  1.00 63.68  ? 331 ILE   C N   1 
ATOM   1788 C  CA  . ILE   C 1 16  ? 12.065  6.556   21.200  1.00 62.46  ? 331 ILE   C CA  1 
ATOM   1789 C  C   . ILE   C 1 16  ? 13.251  6.247   20.289  1.00 62.69  ? 331 ILE   C C   1 
ATOM   1790 O  O   . ILE   C 1 16  ? 14.346  6.757   20.514  1.00 62.35  ? 331 ILE   C O   1 
ATOM   1791 C  CB  . ILE   C 1 16  ? 11.677  5.339   22.060  1.00 60.99  ? 331 ILE   C CB  1 
ATOM   1792 C  CG1 . ILE   C 1 16  ? 10.365  5.563   22.820  1.00 61.04  ? 331 ILE   C CG1 1 
ATOM   1793 C  CG2 . ILE   C 1 16  ? 12.817  4.956   23.005  1.00 60.50  ? 331 ILE   C CG2 1 
ATOM   1794 C  CD1 . ILE   C 1 16  ? 10.411  6.688   23.840  1.00 60.77  ? 331 ILE   C CD1 1 
ATOM   1795 N  N   . THR   C 1 17  ? 13.024  5.400   19.276  1.00 62.99  ? 332 THR   C N   1 
ATOM   1796 C  CA  . THR   C 1 17  ? 14.069  5.007   18.343  1.00 64.01  ? 332 THR   C CA  1 
ATOM   1797 C  C   . THR   C 1 17  ? 13.451  4.649   16.993  1.00 64.87  ? 332 THR   C C   1 
ATOM   1798 O  O   . THR   C 1 17  ? 12.231  4.661   16.840  1.00 65.94  ? 332 THR   C O   1 
ATOM   1799 C  CB  . THR   C 1 17  ? 14.859  3.834   18.925  1.00 64.22  ? 332 THR   C CB  1 
ATOM   1800 O  OG1 . THR   C 1 17  ? 15.998  3.687   18.083  1.00 63.48  ? 332 THR   C OG1 1 
ATOM   1801 C  CG2 . THR   C 1 17  ? 14.057  2.545   18.968  1.00 64.76  ? 332 THR   C CG2 1 
ATOM   1802 N  N   . THR   C 1 18  ? 14.323  4.324   16.026  1.00 64.73  ? 333 THR   C N   1 
ATOM   1803 C  CA  . THR   C 1 18  ? 13.909  3.926   14.691  1.00 64.75  ? 333 THR   C CA  1 
ATOM   1804 C  C   . THR   C 1 18  ? 14.426  2.517   14.402  1.00 63.73  ? 333 THR   C C   1 
ATOM   1805 O  O   . THR   C 1 18  ? 15.436  2.094   14.959  1.00 61.94  ? 333 THR   C O   1 
ATOM   1806 C  CB  . THR   C 1 18  ? 14.412  4.938   13.658  1.00 65.84  ? 333 THR   C CB  1 
ATOM   1807 O  OG1 . THR   C 1 18  ? 15.834  4.889   13.697  1.00 67.21  ? 333 THR   C OG1 1 
ATOM   1808 C  CG2 . THR   C 1 18  ? 13.935  6.352   13.939  1.00 65.12  ? 333 THR   C CG2 1 
ATOM   1809 N  N   . LYS   C 1 19  ? 13.725  1.815   13.502  1.00 64.48  ? 334 LYS   C N   1 
ATOM   1810 C  CA  . LYS   C 1 19  ? 13.987  0.417   13.189  1.00 66.29  ? 334 LYS   C CA  1 
ATOM   1811 C  C   . LYS   C 1 19  ? 15.407  0.218   12.663  1.00 66.18  ? 334 LYS   C C   1 
ATOM   1812 O  O   . LYS   C 1 19  ? 15.989  -0.846  12.865  1.00 65.32  ? 334 LYS   C O   1 
ATOM   1813 C  CB  . LYS   C 1 19  ? 12.969  -0.091  12.161  1.00 69.35  ? 334 LYS   C CB  1 
ATOM   1814 C  CG  . LYS   C 1 19  ? 11.714  -0.741  12.736  1.00 72.32  ? 334 LYS   C CG  1 
ATOM   1815 C  CD  . LYS   C 1 19  ? 10.427  -0.500  11.952  1.00 76.47  ? 334 LYS   C CD  1 
ATOM   1816 C  CE  . LYS   C 1 19  ? 10.525  -0.629  10.456  1.00 80.17  ? 334 LYS   C CE  1 
ATOM   1817 N  NZ  . LYS   C 1 19  ? 10.769  -2.000  9.999   1.00 81.80  ? 334 LYS   C NZ  1 
ATOM   1818 N  N   . ASN   C 1 20  ? 15.959  1.237   11.992  1.00 66.06  ? 335 ASN   C N   1 
ATOM   1819 C  CA  . ASN   C 1 20  ? 17.278  1.134   11.385  1.00 66.53  ? 335 ASN   C CA  1 
ATOM   1820 C  C   . ASN   C 1 20  ? 18.361  1.564   12.378  1.00 63.73  ? 335 ASN   C C   1 
ATOM   1821 O  O   . ASN   C 1 20  ? 19.463  1.921   11.968  1.00 64.56  ? 335 ASN   C O   1 
ATOM   1822 C  CB  . ASN   C 1 20  ? 17.336  1.870   10.047  1.00 69.18  ? 335 ASN   C CB  1 
ATOM   1823 C  CG  . ASN   C 1 20  ? 16.495  3.124   10.031  1.00 72.41  ? 335 ASN   C CG  1 
ATOM   1824 O  OD1 . ASN   C 1 20  ? 15.262  3.043   10.066  1.00 75.79  ? 335 ASN   C OD1 1 
ATOM   1825 N  ND2 . ASN   C 1 20  ? 17.130  4.286   9.970   1.00 72.97  ? 335 ASN   C ND2 1 
ATOM   1826 N  N   . GLU   C 1 21  ? 18.045  1.520   13.680  1.00 61.83  ? 336 GLU   C N   1 
ATOM   1827 C  CA  . GLU   C 1 21  ? 19.048  1.578   14.733  1.00 60.78  ? 336 GLU   C CA  1 
ATOM   1828 C  C   . GLU   C 1 21  ? 19.202  0.210   15.398  1.00 57.43  ? 336 GLU   C C   1 
ATOM   1829 O  O   . GLU   C 1 21  ? 20.020  0.057   16.303  1.00 55.80  ? 336 GLU   C O   1 
ATOM   1830 C  CB  . GLU   C 1 21  ? 18.674  2.611   15.797  1.00 63.04  ? 336 GLU   C CB  1 
ATOM   1831 C  CG  . GLU   C 1 21  ? 18.702  4.051   15.294  1.00 66.14  ? 336 GLU   C CG  1 
ATOM   1832 C  CD  . GLU   C 1 21  ? 20.080  4.614   14.991  1.00 68.71  ? 336 GLU   C CD  1 
ATOM   1833 O  OE1 . GLU   C 1 21  ? 21.091  3.894   15.140  1.00 70.10  ? 336 GLU   C OE1 1 
ATOM   1834 O  OE2 . GLU   C 1 21  ? 20.136  5.800   14.604  1.00 71.04  ? 336 GLU   C OE2 1 
ATOM   1835 N  N   . ILE   C 1 22  ? 18.415  -0.779  14.949  1.00 54.62  ? 337 ILE   C N   1 
ATOM   1836 C  CA  . ILE   C 1 22  ? 18.462  -2.124  15.501  1.00 52.59  ? 337 ILE   C CA  1 
ATOM   1837 C  C   . ILE   C 1 22  ? 19.768  -2.780  15.066  1.00 51.02  ? 337 ILE   C C   1 
ATOM   1838 O  O   . ILE   C 1 22  ? 20.238  -2.546  13.955  1.00 49.95  ? 337 ILE   C O   1 
ATOM   1839 C  CB  . ILE   C 1 22  ? 17.243  -2.953  15.052  1.00 52.22  ? 337 ILE   C CB  1 
ATOM   1840 C  CG1 . ILE   C 1 22  ? 15.932  -2.360  15.568  1.00 52.71  ? 337 ILE   C CG1 1 
ATOM   1841 C  CG2 . ILE   C 1 22  ? 17.394  -4.418  15.467  1.00 52.02  ? 337 ILE   C CG2 1 
ATOM   1842 C  CD1 . ILE   C 1 22  ? 14.688  -2.942  14.920  1.00 52.65  ? 337 ILE   C CD1 1 
ATOM   1843 N  N   . PHE   C 1 23  ? 20.333  -3.615  15.946  1.00 50.39  ? 338 PHE   C N   1 
ATOM   1844 C  CA  . PHE   C 1 23  ? 21.577  -4.300  15.640  1.00 50.30  ? 338 PHE   C CA  1 
ATOM   1845 C  C   . PHE   C 1 23  ? 21.695  -5.580  16.464  1.00 50.68  ? 338 PHE   C C   1 
ATOM   1846 O  O   . PHE   C 1 23  ? 20.940  -5.799  17.410  1.00 49.84  ? 338 PHE   C O   1 
ATOM   1847 C  CB  . PHE   C 1 23  ? 22.748  -3.348  15.899  1.00 49.77  ? 338 PHE   C CB  1 
ATOM   1848 C  CG  . PHE   C 1 23  ? 23.170  -3.252  17.357  1.00 49.77  ? 338 PHE   C CG  1 
ATOM   1849 C  CD1 . PHE   C 1 23  ? 22.361  -2.621  18.295  1.00 49.38  ? 338 PHE   C CD1 1 
ATOM   1850 C  CD2 . PHE   C 1 23  ? 24.381  -3.787  17.784  1.00 50.75  ? 338 PHE   C CD2 1 
ATOM   1851 C  CE1 . PHE   C 1 23  ? 22.752  -2.538  19.624  1.00 49.73  ? 338 PHE   C CE1 1 
ATOM   1852 C  CE2 . PHE   C 1 23  ? 24.767  -3.699  19.113  1.00 50.35  ? 338 PHE   C CE2 1 
ATOM   1853 C  CZ  . PHE   C 1 23  ? 23.953  -3.075  20.030  1.00 49.59  ? 338 PHE   C CZ  1 
ATOM   1854 N  N   . SER   C 1 24  ? 22.661  -6.415  16.066  1.00 52.42  ? 339 SER   C N   1 
ATOM   1855 C  CA  . SER   C 1 24  ? 23.043  -7.613  16.794  1.00 54.40  ? 339 SER   C CA  1 
ATOM   1856 C  C   . SER   C 1 24  ? 24.302  -7.330  17.610  1.00 55.19  ? 339 SER   C C   1 
ATOM   1857 O  O   . SER   C 1 24  ? 25.286  -6.825  17.075  1.00 55.36  ? 339 SER   C O   1 
ATOM   1858 C  CB  . SER   C 1 24  ? 23.259  -8.768  15.844  1.00 55.31  ? 339 SER   C CB  1 
ATOM   1859 O  OG  . SER   C 1 24  ? 24.069  -9.780  16.427  1.00 56.33  ? 339 SER   C OG  1 
ATOM   1860 N  N   . LEU   C 1 25  ? 24.256  -7.657  18.906  1.00 56.85  ? 340 LEU   C N   1 
ATOM   1861 C  CA  . LEU   C 1 25  ? 25.433  -7.589  19.757  1.00 57.27  ? 340 LEU   C CA  1 
ATOM   1862 C  C   . LEU   C 1 25  ? 26.095  -8.964  19.780  1.00 57.69  ? 340 LEU   C C   1 
ATOM   1863 O  O   . LEU   C 1 25  ? 25.411  -9.977  19.917  1.00 57.11  ? 340 LEU   C O   1 
ATOM   1864 C  CB  . LEU   C 1 25  ? 25.065  -7.137  21.170  1.00 56.41  ? 340 LEU   C CB  1 
ATOM   1865 C  CG  . LEU   C 1 25  ? 26.244  -6.699  22.046  1.00 56.30  ? 340 LEU   C CG  1 
ATOM   1866 C  CD1 . LEU   C 1 25  ? 26.402  -5.188  22.049  1.00 56.69  ? 340 LEU   C CD1 1 
ATOM   1867 C  CD2 . LEU   C 1 25  ? 26.127  -7.222  23.462  1.00 56.66  ? 340 LEU   C CD2 1 
ATOM   1868 N  N   . SER   C 1 26  ? 27.429  -8.979  19.661  1.00 58.86  ? 341 SER   C N   1 
ATOM   1869 C  CA  . SER   C 1 26  ? 28.208  -10.207 19.625  1.00 60.36  ? 341 SER   C CA  1 
ATOM   1870 C  C   . SER   C 1 26  ? 27.572  -11.192 18.644  1.00 61.33  ? 341 SER   C C   1 
ATOM   1871 O  O   . SER   C 1 26  ? 27.503  -10.902 17.451  1.00 64.21  ? 341 SER   C O   1 
ATOM   1872 C  CB  . SER   C 1 26  ? 28.381  -10.789 21.011  1.00 61.47  ? 341 SER   C CB  1 
ATOM   1873 O  OG  . SER   C 1 26  ? 29.150  -9.922  21.830  1.00 63.45  ? 341 SER   C OG  1 
ATOM   1874 N  N   . LEU   C 1 27  ? 27.099  -12.341 19.146  1.00 60.72  ? 342 LEU   C N   1 
ATOM   1875 C  CA  . LEU   C 1 27  ? 26.449  -13.335 18.310  1.00 60.27  ? 342 LEU   C CA  1 
ATOM   1876 C  C   . LEU   C 1 27  ? 24.968  -13.435 18.667  1.00 60.34  ? 342 LEU   C C   1 
ATOM   1877 O  O   . LEU   C 1 27  ? 24.280  -14.331 18.184  1.00 61.50  ? 342 LEU   C O   1 
ATOM   1878 C  CB  . LEU   C 1 27  ? 27.161  -14.678 18.466  1.00 59.98  ? 342 LEU   C CB  1 
ATOM   1879 C  CG  . LEU   C 1 27  ? 28.634  -14.717 18.044  1.00 58.90  ? 342 LEU   C CG  1 
ATOM   1880 C  CD1 . LEU   C 1 27  ? 29.121  -16.155 18.005  1.00 58.94  ? 342 LEU   C CD1 1 
ATOM   1881 C  CD2 . LEU   C 1 27  ? 28.880  -14.044 16.704  1.00 58.41  ? 342 LEU   C CD2 1 
ATOM   1882 N  N   . SER   C 1 28  ? 24.485  -12.507 19.503  1.00 60.21  ? 343 SER   C N   1 
ATOM   1883 C  CA  . SER   C 1 28  ? 23.077  -12.442 19.857  1.00 60.50  ? 343 SER   C CA  1 
ATOM   1884 C  C   . SER   C 1 28  ? 22.296  -11.807 18.711  1.00 59.16  ? 343 SER   C C   1 
ATOM   1885 O  O   . SER   C 1 28  ? 22.749  -10.829 18.124  1.00 59.13  ? 343 SER   C O   1 
ATOM   1886 C  CB  . SER   C 1 28  ? 22.873  -11.664 21.132  1.00 61.33  ? 343 SER   C CB  1 
ATOM   1887 O  OG  . SER   C 1 28  ? 23.755  -12.113 22.152  1.00 63.07  ? 343 SER   C OG  1 
ATOM   1888 N  N   . GLY   C 1 29  ? 21.121  -12.367 18.406  1.00 58.08  ? 344 GLY   C N   1 
ATOM   1889 C  CA  . GLY   C 1 29  ? 20.191  -11.730 17.490  1.00 57.36  ? 344 GLY   C CA  1 
ATOM   1890 C  C   . GLY   C 1 29  ? 19.699  -10.406 18.069  1.00 56.99  ? 344 GLY   C C   1 
ATOM   1891 O  O   . GLY   C 1 29  ? 19.946  -10.111 19.237  1.00 57.33  ? 344 GLY   C O   1 
ATOM   1892 N  N   . PRO   C 1 30  ? 18.989  -9.569  17.281  1.00 56.72  ? 345 PRO   C N   1 
ATOM   1893 C  CA  . PRO   C 1 30  ? 18.536  -8.271  17.767  1.00 56.60  ? 345 PRO   C CA  1 
ATOM   1894 C  C   . PRO   C 1 30  ? 17.426  -8.378  18.810  1.00 56.34  ? 345 PRO   C C   1 
ATOM   1895 O  O   . PRO   C 1 30  ? 17.392  -7.599  19.760  1.00 55.82  ? 345 PRO   C O   1 
ATOM   1896 C  CB  . PRO   C 1 30  ? 18.088  -7.562  16.493  1.00 56.62  ? 345 PRO   C CB  1 
ATOM   1897 C  CG  . PRO   C 1 30  ? 17.625  -8.711  15.613  1.00 56.67  ? 345 PRO   C CG  1 
ATOM   1898 C  CD  . PRO   C 1 30  ? 18.565  -9.843  15.899  1.00 56.90  ? 345 PRO   C CD  1 
ATOM   1899 N  N   . MET   C 1 31  ? 16.535  -9.361  18.625  1.00 56.82  ? 346 MET   C N   1 
ATOM   1900 C  CA  . MET   C 1 31  ? 15.402  -9.572  19.511  1.00 57.73  ? 346 MET   C CA  1 
ATOM   1901 C  C   . MET   C 1 31  ? 15.670  -10.780 20.400  1.00 55.89  ? 346 MET   C C   1 
ATOM   1902 O  O   . MET   C 1 31  ? 15.339  -11.907 20.038  1.00 55.44  ? 346 MET   C O   1 
ATOM   1903 C  CB  . MET   C 1 31  ? 14.120  -9.818  18.712  1.00 59.51  ? 346 MET   C CB  1 
ATOM   1904 C  CG  . MET   C 1 31  ? 13.592  -8.585  18.017  1.00 61.66  ? 346 MET   C CG  1 
ATOM   1905 S  SD  . MET   C 1 31  ? 12.506  -9.004  16.641  1.00 65.97  ? 346 MET   C SD  1 
ATOM   1906 C  CE  . MET   C 1 31  ? 13.687  -9.708  15.480  1.00 65.39  ? 346 MET   C CE  1 
ATOM   1907 N  N   . ALA   C 1 32  ? 16.261  -10.521 21.568  1.00 55.65  ? 347 ALA   C N   1 
ATOM   1908 C  CA  . ALA   C 1 32  ? 16.562  -11.566 22.528  1.00 55.62  ? 347 ALA   C CA  1 
ATOM   1909 C  C   . ALA   C 1 32  ? 15.502  -11.582 23.625  1.00 56.37  ? 347 ALA   C C   1 
ATOM   1910 O  O   . ALA   C 1 32  ? 14.600  -10.746 23.643  1.00 57.02  ? 347 ALA   C O   1 
ATOM   1911 C  CB  . ALA   C 1 32  ? 17.942  -11.343 23.099  1.00 55.22  ? 347 ALA   C CB  1 
ATOM   1912 N  N   . ALA   C 1 33  ? 15.621  -12.569 24.517  1.00 57.05  ? 348 ALA   C N   1 
ATOM   1913 C  CA  . ALA   C 1 33  ? 14.886  -12.596 25.769  1.00 56.34  ? 348 ALA   C CA  1 
ATOM   1914 C  C   . ALA   C 1 33  ? 15.835  -13.039 26.878  1.00 55.72  ? 348 ALA   C C   1 
ATOM   1915 O  O   . ALA   C 1 33  ? 16.560  -14.018 26.717  1.00 55.00  ? 348 ALA   C O   1 
ATOM   1916 C  CB  . ALA   C 1 33  ? 13.686  -13.513 25.656  1.00 56.58  ? 348 ALA   C CB  1 
ATOM   1917 N  N   . TYR   C 1 34  ? 15.838  -12.294 27.987  1.00 55.63  ? 349 TYR   C N   1 
ATOM   1918 C  CA  . TYR   C 1 34  ? 16.687  -12.606 29.124  1.00 55.05  ? 349 TYR   C CA  1 
ATOM   1919 C  C   . TYR   C 1 34  ? 15.817  -12.748 30.366  1.00 54.19  ? 349 TYR   C C   1 
ATOM   1920 O  O   . TYR   C 1 34  ? 14.673  -12.300 30.384  1.00 53.42  ? 349 TYR   C O   1 
ATOM   1921 C  CB  . TYR   C 1 34  ? 17.753  -11.522 29.297  1.00 55.54  ? 349 TYR   C CB  1 
ATOM   1922 C  CG  . TYR   C 1 34  ? 18.620  -11.330 28.063  1.00 55.77  ? 349 TYR   C CG  1 
ATOM   1923 C  CD1 . TYR   C 1 34  ? 19.762  -12.095 27.861  1.00 56.22  ? 349 TYR   C CD1 1 
ATOM   1924 C  CD2 . TYR   C 1 34  ? 18.283  -10.395 27.092  1.00 56.43  ? 349 TYR   C CD2 1 
ATOM   1925 C  CE1 . TYR   C 1 34  ? 20.551  -11.928 26.734  1.00 56.68  ? 349 TYR   C CE1 1 
ATOM   1926 C  CE2 . TYR   C 1 34  ? 19.065  -10.216 25.963  1.00 57.08  ? 349 TYR   C CE2 1 
ATOM   1927 C  CZ  . TYR   C 1 34  ? 20.201  -10.987 25.781  1.00 57.14  ? 349 TYR   C CZ  1 
ATOM   1928 O  OH  . TYR   C 1 34  ? 20.973  -10.822 24.668  1.00 58.01  ? 349 TYR   C OH  1 
ATOM   1929 N  N   . VAL   C 1 35  ? 16.386  -13.375 31.399  1.00 53.93  ? 350 VAL   C N   1 
ATOM   1930 C  CA  . VAL   C 1 35  ? 15.666  -13.634 32.633  1.00 54.24  ? 350 VAL   C CA  1 
ATOM   1931 C  C   . VAL   C 1 35  ? 16.285  -12.778 33.737  1.00 53.99  ? 350 VAL   C C   1 
ATOM   1932 O  O   . VAL   C 1 35  ? 17.506  -12.661 33.825  1.00 53.15  ? 350 VAL   C O   1 
ATOM   1933 C  CB  . VAL   C 1 35  ? 15.648  -15.139 32.972  1.00 54.75  ? 350 VAL   C CB  1 
ATOM   1934 C  CG1 . VAL   C 1 35  ? 17.043  -15.726 33.161  1.00 55.26  ? 350 VAL   C CG1 1 
ATOM   1935 C  CG2 . VAL   C 1 35  ? 14.773  -15.441 34.180  1.00 54.68  ? 350 VAL   C CG2 1 
ATOM   1936 N  N   . ASN   C 1 36  ? 15.422  -12.163 34.555  1.00 52.97  ? 351 ASN   C N   1 
ATOM   1937 C  CA  . ASN   C 1 36  ? 15.849  -11.239 35.593  1.00 52.37  ? 351 ASN   C CA  1 
ATOM   1938 C  C   . ASN   C 1 36  ? 16.086  -12.036 36.876  1.00 53.16  ? 351 ASN   C C   1 
ATOM   1939 O  O   . ASN   C 1 36  ? 15.827  -13.237 36.909  1.00 51.87  ? 351 ASN   C O   1 
ATOM   1940 C  CB  . ASN   C 1 36  ? 14.866  -10.076 35.710  1.00 52.19  ? 351 ASN   C CB  1 
ATOM   1941 C  CG  . ASN   C 1 36  ? 13.564  -10.441 36.386  1.00 51.92  ? 351 ASN   C CG  1 
ATOM   1942 O  OD1 . ASN   C 1 36  ? 13.456  -11.486 37.037  1.00 52.15  ? 351 ASN   C OD1 1 
ATOM   1943 N  ND2 . ASN   C 1 36  ? 12.568  -9.578  36.261  1.00 51.78  ? 351 ASN   C ND2 1 
ATOM   1944 N  N   . PRO   C 1 37  ? 16.590  -11.405 37.965  1.00 54.69  ? 352 PRO   C N   1 
ATOM   1945 C  CA  . PRO   C 1 37  ? 16.913  -12.127 39.193  1.00 55.10  ? 352 PRO   C CA  1 
ATOM   1946 C  C   . PRO   C 1 37  ? 15.757  -12.926 39.790  1.00 55.86  ? 352 PRO   C C   1 
ATOM   1947 O  O   . PRO   C 1 37  ? 15.981  -14.004 40.335  1.00 56.83  ? 352 PRO   C O   1 
ATOM   1948 C  CB  . PRO   C 1 37  ? 17.372  -11.031 40.151  1.00 54.46  ? 352 PRO   C CB  1 
ATOM   1949 C  CG  . PRO   C 1 37  ? 17.841  -9.927  39.225  1.00 54.30  ? 352 PRO   C CG  1 
ATOM   1950 C  CD  . PRO   C 1 37  ? 16.909  -9.972  38.059  1.00 54.00  ? 352 PRO   C CD  1 
ATOM   1951 N  N   . HIS   C 1 38  ? 14.530  -12.398 39.688  1.00 56.87  ? 353 HIS   C N   1 
ATOM   1952 C  CA  . HIS   C 1 38  ? 13.377  -13.044 40.298  1.00 57.95  ? 353 HIS   C CA  1 
ATOM   1953 C  C   . HIS   C 1 38  ? 12.616  -13.894 39.276  1.00 56.49  ? 353 HIS   C C   1 
ATOM   1954 O  O   . HIS   C 1 38  ? 11.437  -14.179 39.472  1.00 57.67  ? 353 HIS   C O   1 
ATOM   1955 C  CB  . HIS   C 1 38  ? 12.510  -12.026 41.053  1.00 60.39  ? 353 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   C 1 38  ? 11.804  -11.017 40.210  1.00 64.10  ? 353 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   C 1 38  ? 12.213  -9.704  40.125  1.00 66.74  ? 353 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   C 1 38  ? 10.692  -11.107 39.466  1.00 66.34  ? 353 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   C 1 38  ? 11.384  -9.039  39.331  1.00 68.24  ? 353 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   C 1 38  ? 10.454  -9.873  38.917  1.00 67.79  ? 353 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   C 1 39  ? 13.289  -14.298 38.191  1.00 54.27  ? 354 GLY   C N   1 
ATOM   1962 C  CA  . GLY   C 1 39  ? 12.863  -15.445 37.402  1.00 52.46  ? 354 GLY   C CA  1 
ATOM   1963 C  C   . GLY   C 1 39  ? 12.009  -15.088 36.185  1.00 51.41  ? 354 GLY   C C   1 
ATOM   1964 O  O   . GLY   C 1 39  ? 11.613  -15.984 35.443  1.00 50.25  ? 354 GLY   C O   1 
ATOM   1965 N  N   . TYR   C 1 40  ? 11.736  -13.795 35.967  1.00 51.00  ? 355 TYR   C N   1 
ATOM   1966 C  CA  . TYR   C 1 40  ? 10.859  -13.371 34.885  1.00 50.97  ? 355 TYR   C CA  1 
ATOM   1967 C  C   . TYR   C 1 40  ? 11.654  -13.244 33.586  1.00 52.37  ? 355 TYR   C C   1 
ATOM   1968 O  O   . TYR   C 1 40  ? 12.799  -12.800 33.600  1.00 51.76  ? 355 TYR   C O   1 
ATOM   1969 C  CB  . TYR   C 1 40  ? 10.167  -12.054 35.249  1.00 50.68  ? 355 TYR   C CB  1 
ATOM   1970 C  CG  . TYR   C 1 40  ? 9.385   -11.426 34.104  1.00 50.98  ? 355 TYR   C CG  1 
ATOM   1971 C  CD1 . TYR   C 1 40  ? 8.187   -11.977 33.666  1.00 51.67  ? 355 TYR   C CD1 1 
ATOM   1972 C  CD2 . TYR   C 1 40  ? 9.845   -10.283 33.462  1.00 51.20  ? 355 TYR   C CD2 1 
ATOM   1973 C  CE1 . TYR   C 1 40  ? 7.471   -11.413 32.622  1.00 52.48  ? 355 TYR   C CE1 1 
ATOM   1974 C  CE2 . TYR   C 1 40  ? 9.138   -9.707  32.418  1.00 51.69  ? 355 TYR   C CE2 1 
ATOM   1975 C  CZ  . TYR   C 1 40  ? 7.948   -10.274 31.997  1.00 52.73  ? 355 TYR   C CZ  1 
ATOM   1976 O  OH  . TYR   C 1 40  ? 7.242   -9.716  30.971  1.00 53.90  ? 355 TYR   C OH  1 
ATOM   1977 N  N   . VAL   C 1 41  ? 11.012  -13.610 32.467  1.00 53.59  ? 356 VAL   C N   1 
ATOM   1978 C  CA  . VAL   C 1 41  ? 11.644  -13.631 31.156  1.00 54.11  ? 356 VAL   C CA  1 
ATOM   1979 C  C   . VAL   C 1 41  ? 11.297  -12.348 30.401  1.00 55.38  ? 356 VAL   C C   1 
ATOM   1980 O  O   . VAL   C 1 41  ? 10.219  -12.239 29.819  1.00 53.07  ? 356 VAL   C O   1 
ATOM   1981 C  CB  . VAL   C 1 41  ? 11.207  -14.881 30.363  1.00 54.53  ? 356 VAL   C CB  1 
ATOM   1982 C  CG1 . VAL   C 1 41  ? 11.801  -14.909 28.959  1.00 54.85  ? 356 VAL   C CG1 1 
ATOM   1983 C  CG2 . VAL   C 1 41  ? 11.550  -16.170 31.100  1.00 54.56  ? 356 VAL   C CG2 1 
ATOM   1984 N  N   . HIS   C 1 42  ? 12.232  -11.387 30.413  1.00 59.10  ? 357 HIS   C N   1 
ATOM   1985 C  CA  . HIS   C 1 42  ? 12.112  -10.155 29.648  1.00 61.80  ? 357 HIS   C CA  1 
ATOM   1986 C  C   . HIS   C 1 42  ? 12.408  -10.423 28.175  1.00 60.96  ? 357 HIS   C C   1 
ATOM   1987 O  O   . HIS   C 1 42  ? 13.297  -11.209 27.861  1.00 61.85  ? 357 HIS   C O   1 
ATOM   1988 C  CB  . HIS   C 1 42  ? 13.105  -9.094  30.137  1.00 65.38  ? 357 HIS   C CB  1 
ATOM   1989 C  CG  . HIS   C 1 42  ? 12.664  -8.323  31.335  1.00 69.63  ? 357 HIS   C CG  1 
ATOM   1990 N  ND1 . HIS   C 1 42  ? 12.027  -7.105  31.237  1.00 71.66  ? 357 HIS   C ND1 1 
ATOM   1991 C  CD2 . HIS   C 1 42  ? 12.790  -8.573  32.645  1.00 72.07  ? 357 HIS   C CD2 1 
ATOM   1992 C  CE1 . HIS   C 1 42  ? 11.765  -6.651  32.456  1.00 73.05  ? 357 HIS   C CE1 1 
ATOM   1993 N  NE2 . HIS   C 1 42  ? 12.222  -7.526  33.326  1.00 73.08  ? 357 HIS   C NE2 1 
ATOM   1994 N  N   . GLU   C 1 43  ? 11.670  -9.740  27.290  1.00 59.74  ? 358 GLU   C N   1 
ATOM   1995 C  CA  . GLU   C 1 43  ? 11.916  -9.785  25.857  1.00 58.56  ? 358 GLU   C CA  1 
ATOM   1996 C  C   . GLU   C 1 43  ? 12.378  -8.404  25.397  1.00 56.84  ? 358 GLU   C C   1 
ATOM   1997 O  O   . GLU   C 1 43  ? 11.650  -7.423  25.548  1.00 55.23  ? 358 GLU   C O   1 
ATOM   1998 C  CB  . GLU   C 1 43  ? 10.661  -10.266 25.131  1.00 59.92  ? 358 GLU   C CB  1 
ATOM   1999 C  CG  . GLU   C 1 43  ? 10.307  -11.714 25.455  1.00 62.60  ? 358 GLU   C CG  1 
ATOM   2000 C  CD  . GLU   C 1 43  ? 9.176   -12.286 24.621  1.00 65.90  ? 358 GLU   C CD  1 
ATOM   2001 O  OE1 . GLU   C 1 43  ? 8.085   -11.679 24.621  1.00 68.00  ? 358 GLU   C OE1 1 
ATOM   2002 O  OE2 . GLU   C 1 43  ? 9.382   -13.337 23.975  1.00 69.22  ? 358 GLU   C OE2 1 
ATOM   2003 N  N   . THR   C 1 44  ? 13.589  -8.351  24.824  1.00 55.21  ? 359 THR   C N   1 
ATOM   2004 C  CA  . THR   C 1 44  ? 14.317  -7.104  24.651  1.00 54.11  ? 359 THR   C CA  1 
ATOM   2005 C  C   . THR   C 1 44  ? 14.619  -6.859  23.174  1.00 53.04  ? 359 THR   C C   1 
ATOM   2006 O  O   . THR   C 1 44  ? 14.475  -7.752  22.343  1.00 52.61  ? 359 THR   C O   1 
ATOM   2007 C  CB  . THR   C 1 44  ? 15.608  -7.150  25.468  1.00 54.06  ? 359 THR   C CB  1 
ATOM   2008 O  OG1 . THR   C 1 44  ? 16.396  -8.187  24.892  1.00 54.46  ? 359 THR   C OG1 1 
ATOM   2009 C  CG2 . THR   C 1 44  ? 15.363  -7.432  26.940  1.00 54.09  ? 359 THR   C CG2 1 
ATOM   2010 N  N   . LEU   C 1 45  ? 15.062  -5.629  22.885  1.00 52.01  ? 360 LEU   C N   1 
ATOM   2011 C  CA  . LEU   C 1 45  ? 15.476  -5.208  21.556  1.00 50.24  ? 360 LEU   C CA  1 
ATOM   2012 C  C   . LEU   C 1 45  ? 16.692  -4.295  21.691  1.00 49.35  ? 360 LEU   C C   1 
ATOM   2013 O  O   . LEU   C 1 45  ? 16.598  -3.230  22.297  1.00 50.92  ? 360 LEU   C O   1 
ATOM   2014 C  CB  . LEU   C 1 45  ? 14.311  -4.487  20.879  1.00 49.68  ? 360 LEU   C CB  1 
ATOM   2015 C  CG  . LEU   C 1 45  ? 14.611  -3.818  19.534  1.00 49.44  ? 360 LEU   C CG  1 
ATOM   2016 C  CD1 . LEU   C 1 45  ? 14.995  -4.848  18.489  1.00 49.79  ? 360 LEU   C CD1 1 
ATOM   2017 C  CD2 . LEU   C 1 45  ? 13.425  -2.992  19.066  1.00 49.43  ? 360 LEU   C CD2 1 
ATOM   2018 N  N   . THR   C 1 46  ? 17.830  -4.716  21.128  1.00 48.38  ? 361 THR   C N   1 
ATOM   2019 C  CA  . THR   C 1 46  ? 19.048  -3.924  21.187  1.00 48.00  ? 361 THR   C CA  1 
ATOM   2020 C  C   . THR   C 1 46  ? 19.060  -2.932  20.027  1.00 48.04  ? 361 THR   C C   1 
ATOM   2021 O  O   . THR   C 1 46  ? 18.899  -3.324  18.873  1.00 47.53  ? 361 THR   C O   1 
ATOM   2022 C  CB  . THR   C 1 46  ? 20.272  -4.837  21.164  1.00 48.25  ? 361 THR   C CB  1 
ATOM   2023 O  OG1 . THR   C 1 46  ? 20.074  -5.730  20.073  1.00 48.85  ? 361 THR   C OG1 1 
ATOM   2024 C  CG2 . THR   C 1 46  ? 20.434  -5.607  22.461  1.00 48.73  ? 361 THR   C CG2 1 
ATOM   2025 N  N   . VAL   C 1 47  ? 19.244  -1.647  20.359  1.00 49.13  ? 362 VAL   C N   1 
ATOM   2026 C  CA  . VAL   C 1 47  ? 19.393  -0.594  19.366  1.00 49.96  ? 362 VAL   C CA  1 
ATOM   2027 C  C   . VAL   C 1 47  ? 20.610  0.251   19.732  1.00 50.32  ? 362 VAL   C C   1 
ATOM   2028 O  O   . VAL   C 1 47  ? 20.990  0.334   20.899  1.00 49.94  ? 362 VAL   C O   1 
ATOM   2029 C  CB  . VAL   C 1 47  ? 18.138  0.292   19.227  1.00 50.46  ? 362 VAL   C CB  1 
ATOM   2030 C  CG1 . VAL   C 1 47  ? 16.919  -0.515  18.796  1.00 51.28  ? 362 VAL   C CG1 1 
ATOM   2031 C  CG2 . VAL   C 1 47  ? 17.840  1.073   20.501  1.00 50.58  ? 362 VAL   C CG2 1 
ATOM   2032 N  N   . TYR   C 1 48  ? 21.199  0.888   18.715  1.00 51.96  ? 363 TYR   C N   1 
ATOM   2033 C  CA  . TYR   C 1 48  ? 22.387  1.706   18.891  1.00 53.20  ? 363 TYR   C CA  1 
ATOM   2034 C  C   . TYR   C 1 48  ? 22.028  3.007   19.602  1.00 55.09  ? 363 TYR   C C   1 
ATOM   2035 O  O   . TYR   C 1 48  ? 22.784  3.468   20.456  1.00 55.44  ? 363 TYR   C O   1 
ATOM   2036 C  CB  . TYR   C 1 48  ? 23.048  1.993   17.539  1.00 52.77  ? 363 TYR   C CB  1 
ATOM   2037 C  CG  . TYR   C 1 48  ? 23.968  0.892   17.028  1.00 52.01  ? 363 TYR   C CG  1 
ATOM   2038 C  CD1 . TYR   C 1 48  ? 24.979  0.372   17.829  1.00 52.06  ? 363 TYR   C CD1 1 
ATOM   2039 C  CD2 . TYR   C 1 48  ? 23.820  0.365   15.749  1.00 51.76  ? 363 TYR   C CD2 1 
ATOM   2040 C  CE1 . TYR   C 1 48  ? 25.821  -0.629  17.373  1.00 52.18  ? 363 TYR   C CE1 1 
ATOM   2041 C  CE2 . TYR   C 1 48  ? 24.655  -0.637  15.281  1.00 51.96  ? 363 TYR   C CE2 1 
ATOM   2042 C  CZ  . TYR   C 1 48  ? 25.657  -1.136  16.096  1.00 52.17  ? 363 TYR   C CZ  1 
ATOM   2043 O  OH  . TYR   C 1 48  ? 26.486  -2.124  15.651  1.00 53.10  ? 363 TYR   C OH  1 
ATOM   2044 N  N   . LYS   C 1 49  ? 20.884  3.596   19.232  1.00 57.34  ? 364 LYS   C N   1 
ATOM   2045 C  CA  . LYS   C 1 49  ? 20.542  4.935   19.684  1.00 59.58  ? 364 LYS   C CA  1 
ATOM   2046 C  C   . LYS   C 1 49  ? 19.053  5.034   20.005  1.00 60.58  ? 364 LYS   C C   1 
ATOM   2047 O  O   . LYS   C 1 49  ? 18.215  4.471   19.302  1.00 58.78  ? 364 LYS   C O   1 
ATOM   2048 C  CB  . LYS   C 1 49  ? 20.988  5.952   18.627  1.00 60.14  ? 364 LYS   C CB  1 
ATOM   2049 C  CG  . LYS   C 1 49  ? 22.495  5.971   18.414  1.00 61.08  ? 364 LYS   C CG  1 
ATOM   2050 C  CD  . LYS   C 1 49  ? 23.038  7.115   17.570  1.00 62.14  ? 364 LYS   C CD  1 
ATOM   2051 C  CE  . LYS   C 1 49  ? 24.534  7.127   17.614  1.00 63.88  ? 364 LYS   C CE  1 
ATOM   2052 N  NZ  . LYS   C 1 49  ? 25.109  8.169   16.760  1.00 65.19  ? 364 LYS   C NZ  1 
ATOM   2053 N  N   . ALA   C 1 50  ? 18.760  5.753   21.097  1.00 62.52  ? 365 ALA   C N   1 
ATOM   2054 C  CA  . ALA   C 1 50  ? 17.410  6.149   21.466  1.00 63.06  ? 365 ALA   C CA  1 
ATOM   2055 C  C   . ALA   C 1 50  ? 17.451  7.557   22.054  1.00 63.72  ? 365 ALA   C C   1 
ATOM   2056 O  O   . ALA   C 1 50  ? 18.522  8.060   22.392  1.00 63.99  ? 365 ALA   C O   1 
ATOM   2057 C  CB  . ALA   C 1 50  ? 16.825  5.154   22.444  1.00 62.47  ? 365 ALA   C CB  1 
ATOM   2058 N  N   . SER   C 1 51  ? 16.278  8.189   22.164  1.00 64.87  ? 366 SER   C N   1 
ATOM   2059 C  CA  . SER   C 1 51  ? 16.167  9.521   22.738  1.00 65.79  ? 366 SER   C CA  1 
ATOM   2060 C  C   . SER   C 1 51  ? 14.786  9.698   23.366  1.00 64.28  ? 366 SER   C C   1 
ATOM   2061 O  O   . SER   C 1 51  ? 13.941  8.812   23.259  1.00 64.31  ? 366 SER   C O   1 
ATOM   2062 C  CB  . SER   C 1 51  ? 16.464  10.581  21.702  1.00 66.95  ? 366 SER   C CB  1 
ATOM   2063 O  OG  . SER   C 1 51  ? 15.629  10.431  20.563  1.00 67.86  ? 366 SER   C OG  1 
ATOM   2064 N  N   . ASN   C 1 52  ? 14.581  10.847  24.026  1.00 62.69  ? 367 ASN   C N   1 
ATOM   2065 C  CA  . ASN   C 1 52  ? 13.395  11.107  24.829  1.00 60.98  ? 367 ASN   C CA  1 
ATOM   2066 C  C   . ASN   C 1 52  ? 13.353  10.125  25.996  1.00 57.67  ? 367 ASN   C C   1 
ATOM   2067 O  O   . ASN   C 1 52  ? 12.293  9.599   26.327  1.00 55.85  ? 367 ASN   C O   1 
ATOM   2068 C  CB  . ASN   C 1 52  ? 12.104  11.050  24.014  1.00 62.20  ? 367 ASN   C CB  1 
ATOM   2069 C  CG  . ASN   C 1 52  ? 12.041  12.073  22.903  1.00 63.99  ? 367 ASN   C CG  1 
ATOM   2070 O  OD1 . ASN   C 1 52  ? 11.222  11.930  21.988  1.00 65.36  ? 367 ASN   C OD1 1 
ATOM   2071 N  ND2 . ASN   C 1 52  ? 12.878  13.100  22.944  1.00 65.43  ? 367 ASN   C ND2 1 
ATOM   2072 N  N   . LEU   C 1 53  ? 14.517  9.896   26.615  1.00 56.36  ? 368 LEU   C N   1 
ATOM   2073 C  CA  . LEU   C 1 53  ? 14.626  8.983   27.740  1.00 56.32  ? 368 LEU   C CA  1 
ATOM   2074 C  C   . LEU   C 1 53  ? 15.355  9.678   28.886  1.00 55.53  ? 368 LEU   C C   1 
ATOM   2075 O  O   . LEU   C 1 53  ? 16.426  10.250  28.688  1.00 53.87  ? 368 LEU   C O   1 
ATOM   2076 C  CB  . LEU   C 1 53  ? 15.344  7.697   27.331  1.00 57.02  ? 368 LEU   C CB  1 
ATOM   2077 C  CG  . LEU   C 1 53  ? 14.657  6.834   26.267  1.00 57.15  ? 368 LEU   C CG  1 
ATOM   2078 C  CD1 . LEU   C 1 53  ? 15.521  5.630   25.926  1.00 56.53  ? 368 LEU   C CD1 1 
ATOM   2079 C  CD2 . LEU   C 1 53  ? 13.275  6.376   26.704  1.00 57.18  ? 368 LEU   C CD2 1 
ATOM   2080 N  N   . ASN   C 1 54  ? 14.746  9.629   30.078  1.00 54.84  ? 369 ASN   C N   1 
ATOM   2081 C  CA  . ASN   C 1 54  ? 15.417  9.995   31.312  1.00 54.50  ? 369 ASN   C CA  1 
ATOM   2082 C  C   . ASN   C 1 54  ? 16.140  8.768   31.858  1.00 54.99  ? 369 ASN   C C   1 
ATOM   2083 O  O   . ASN   C 1 54  ? 15.538  7.705   31.997  1.00 53.79  ? 369 ASN   C O   1 
ATOM   2084 C  CB  . ASN   C 1 54  ? 14.446  10.523  32.363  1.00 54.86  ? 369 ASN   C CB  1 
ATOM   2085 C  CG  . ASN   C 1 54  ? 13.971  11.926  32.071  1.00 54.66  ? 369 ASN   C CG  1 
ATOM   2086 O  OD1 . ASN   C 1 54  ? 12.764  12.161  31.961  1.00 55.11  ? 369 ASN   C OD1 1 
ATOM   2087 N  ND2 . ASN   C 1 54  ? 14.893  12.871  31.970  1.00 54.85  ? 369 ASN   C ND2 1 
ATOM   2088 N  N   . LEU   C 1 55  ? 17.436  8.925   32.150  1.00 55.81  ? 370 LEU   C N   1 
ATOM   2089 C  CA  . LEU   C 1 55  ? 18.184  7.915   32.880  1.00 55.44  ? 370 LEU   C CA  1 
ATOM   2090 C  C   . LEU   C 1 55  ? 17.962  8.146   34.369  1.00 54.49  ? 370 LEU   C C   1 
ATOM   2091 O  O   . LEU   C 1 55  ? 17.604  9.245   34.783  1.00 53.86  ? 370 LEU   C O   1 
ATOM   2092 C  CB  . LEU   C 1 55  ? 19.671  7.943   32.533  1.00 56.02  ? 370 LEU   C CB  1 
ATOM   2093 C  CG  . LEU   C 1 55  ? 20.036  7.643   31.076  1.00 56.21  ? 370 LEU   C CG  1 
ATOM   2094 C  CD1 . LEU   C 1 55  ? 21.548  7.618   30.934  1.00 56.19  ? 370 LEU   C CD1 1 
ATOM   2095 C  CD2 . LEU   C 1 55  ? 19.428  6.340   30.578  1.00 56.96  ? 370 LEU   C CD2 1 
ATOM   2096 N  N   . ILE   C 1 56  ? 18.183  7.090   35.158  1.00 54.71  ? 371 ILE   C N   1 
ATOM   2097 C  CA  . ILE   C 1 56  ? 17.805  7.082   36.561  1.00 54.05  ? 371 ILE   C CA  1 
ATOM   2098 C  C   . ILE   C 1 56  ? 18.650  6.041   37.293  1.00 53.88  ? 371 ILE   C C   1 
ATOM   2099 O  O   . ILE   C 1 56  ? 18.610  4.859   36.963  1.00 53.19  ? 371 ILE   C O   1 
ATOM   2100 C  CB  . ILE   C 1 56  ? 16.282  6.866   36.700  1.00 53.44  ? 371 ILE   C CB  1 
ATOM   2101 C  CG1 . ILE   C 1 56  ? 15.906  6.131   37.990  1.00 53.17  ? 371 ILE   C CG1 1 
ATOM   2102 C  CG2 . ILE   C 1 56  ? 15.704  6.155   35.473  1.00 53.77  ? 371 ILE   C CG2 1 
ATOM   2103 C  CD1 . ILE   C 1 56  ? 14.419  5.868   38.135  1.00 53.56  ? 371 ILE   C CD1 1 
ATOM   2104 N  N   . GLY   C 1 57  ? 19.433  6.509   38.274  1.00 56.06  ? 372 GLY   C N   1 
ATOM   2105 C  CA  . GLY   C 1 57  ? 20.324  5.659   39.048  1.00 58.26  ? 372 GLY   C CA  1 
ATOM   2106 C  C   . GLY   C 1 57  ? 21.717  5.596   38.425  1.00 60.93  ? 372 GLY   C C   1 
ATOM   2107 O  O   . GLY   C 1 57  ? 21.938  6.124   37.336  1.00 60.38  ? 372 GLY   C O   1 
ATOM   2108 N  N   . ARG   C 1 58  ? 22.649  4.949   39.139  1.00 63.38  ? 373 ARG   C N   1 
ATOM   2109 C  CA  . ARG   C 1 58  ? 23.988  4.700   38.626  1.00 63.66  ? 373 ARG   C CA  1 
ATOM   2110 C  C   . ARG   C 1 58  ? 23.976  3.469   37.728  1.00 61.36  ? 373 ARG   C C   1 
ATOM   2111 O  O   . ARG   C 1 58  ? 23.092  2.621   37.841  1.00 62.21  ? 373 ARG   C O   1 
ATOM   2112 C  CB  . ARG   C 1 58  ? 25.019  4.420   39.728  1.00 66.39  ? 373 ARG   C CB  1 
ATOM   2113 C  CG  . ARG   C 1 58  ? 25.444  5.609   40.577  1.00 68.40  ? 373 ARG   C CG  1 
ATOM   2114 C  CD  . ARG   C 1 58  ? 25.873  6.800   39.724  1.00 70.54  ? 373 ARG   C CD  1 
ATOM   2115 N  NE  . ARG   C 1 58  ? 26.207  8.016   40.476  1.00 73.62  ? 373 ARG   C NE  1 
ATOM   2116 C  CZ  . ARG   C 1 58  ? 25.419  8.643   41.350  1.00 75.98  ? 373 ARG   C CZ  1 
ATOM   2117 N  NH1 . ARG   C 1 58  ? 24.248  8.132   41.687  1.00 77.41  ? 373 ARG   C NH1 1 
ATOM   2118 N  NH2 . ARG   C 1 58  ? 25.807  9.780   41.905  1.00 75.44  ? 373 ARG   C NH2 1 
ATOM   2119 N  N   . PRO   C 1 59  ? 24.954  3.338   36.803  1.00 58.29  ? 374 PRO   C N   1 
ATOM   2120 C  CA  . PRO   C 1 59  ? 25.236  2.057   36.169  1.00 56.96  ? 374 PRO   C CA  1 
ATOM   2121 C  C   . PRO   C 1 59  ? 25.583  0.968   37.180  1.00 55.91  ? 374 PRO   C C   1 
ATOM   2122 O  O   . PRO   C 1 59  ? 26.298  1.224   38.147  1.00 56.31  ? 374 PRO   C O   1 
ATOM   2123 C  CB  . PRO   C 1 59  ? 26.396  2.371   35.227  1.00 57.04  ? 374 PRO   C CB  1 
ATOM   2124 C  CG  . PRO   C 1 59  ? 26.285  3.866   34.993  1.00 57.16  ? 374 PRO   C CG  1 
ATOM   2125 C  CD  . PRO   C 1 59  ? 25.798  4.428   36.287  1.00 57.65  ? 374 PRO   C CD  1 
ATOM   2126 N  N   . SER   C 1 60  ? 25.045  -0.236  36.950  1.00 54.03  ? 375 SER   C N   1 
ATOM   2127 C  CA  . SER   C 1 60  ? 25.317  -1.398  37.778  1.00 53.03  ? 375 SER   C CA  1 
ATOM   2128 C  C   . SER   C 1 60  ? 25.634  -2.593  36.886  1.00 52.98  ? 375 SER   C C   1 
ATOM   2129 O  O   . SER   C 1 60  ? 25.084  -2.712  35.795  1.00 52.53  ? 375 SER   C O   1 
ATOM   2130 C  CB  . SER   C 1 60  ? 24.153  -1.700  38.681  1.00 53.36  ? 375 SER   C CB  1 
ATOM   2131 O  OG  . SER   C 1 60  ? 24.260  -3.007  39.229  1.00 53.31  ? 375 SER   C OG  1 
ATOM   2132 N  N   . THR   C 1 61  ? 26.516  -3.477  37.369  1.00 54.18  ? 376 THR   C N   1 
ATOM   2133 C  CA  . THR   C 1 61  ? 26.877  -4.687  36.647  1.00 55.20  ? 376 THR   C CA  1 
ATOM   2134 C  C   . THR   C 1 61  ? 26.252  -5.910  37.316  1.00 55.38  ? 376 THR   C C   1 
ATOM   2135 O  O   . THR   C 1 61  ? 26.507  -7.037  36.899  1.00 54.78  ? 376 THR   C O   1 
ATOM   2136 C  CB  . THR   C 1 61  ? 28.399  -4.805  36.568  1.00 55.11  ? 376 THR   C CB  1 
ATOM   2137 O  OG1 . THR   C 1 61  ? 28.883  -4.645  37.897  1.00 55.32  ? 376 THR   C OG1 1 
ATOM   2138 C  CG2 . THR   C 1 61  ? 29.011  -3.751  35.663  1.00 55.36  ? 376 THR   C CG2 1 
ATOM   2139 N  N   . GLU   C 1 62  ? 25.433  -5.680  38.349  1.00 57.11  ? 377 GLU   C N   1 
ATOM   2140 C  CA  . GLU   C 1 62  ? 24.722  -6.752  39.023  1.00 58.32  ? 377 GLU   C CA  1 
ATOM   2141 C  C   . GLU   C 1 62  ? 23.786  -7.427  38.023  1.00 56.55  ? 377 GLU   C C   1 
ATOM   2142 O  O   . GLU   C 1 62  ? 22.843  -6.804  37.541  1.00 56.15  ? 377 GLU   C O   1 
ATOM   2143 C  CB  . GLU   C 1 62  ? 23.956  -6.188  40.222  1.00 60.93  ? 377 GLU   C CB  1 
ATOM   2144 C  CG  . GLU   C 1 62  ? 23.104  -7.218  40.962  1.00 63.49  ? 377 GLU   C CG  1 
ATOM   2145 C  CD  . GLU   C 1 62  ? 22.282  -6.649  42.107  1.00 65.32  ? 377 GLU   C CD  1 
ATOM   2146 O  OE1 . GLU   C 1 62  ? 22.462  -5.459  42.447  1.00 66.51  ? 377 GLU   C OE1 1 
ATOM   2147 O  OE2 . GLU   C 1 62  ? 21.444  -7.398  42.651  1.00 67.05  ? 377 GLU   C OE2 1 
ATOM   2148 N  N   . HIS   C 1 63  ? 24.086  -8.692  37.700  1.00 55.05  ? 378 HIS   C N   1 
ATOM   2149 C  CA  . HIS   C 1 63  ? 23.181  -9.546  36.948  1.00 54.06  ? 378 HIS   C CA  1 
ATOM   2150 C  C   . HIS   C 1 63  ? 23.026  -9.017  35.521  1.00 53.63  ? 378 HIS   C C   1 
ATOM   2151 O  O   . HIS   C 1 63  ? 21.953  -9.127  34.932  1.00 53.48  ? 378 HIS   C O   1 
ATOM   2152 C  CB  . HIS   C 1 63  ? 21.843  -9.658  37.693  1.00 53.51  ? 378 HIS   C CB  1 
ATOM   2153 C  CG  . HIS   C 1 63  ? 21.057  -10.893 37.399  1.00 52.77  ? 378 HIS   C CG  1 
ATOM   2154 N  ND1 . HIS   C 1 63  ? 20.298  -11.058 36.261  1.00 52.83  ? 378 HIS   C ND1 1 
ATOM   2155 C  CD2 . HIS   C 1 63  ? 20.913  -12.020 38.107  1.00 51.77  ? 378 HIS   C CD2 1 
ATOM   2156 C  CE1 . HIS   C 1 63  ? 19.719  -12.249 36.292  1.00 51.78  ? 378 HIS   C CE1 1 
ATOM   2157 N  NE2 . HIS   C 1 63  ? 20.078  -12.849 37.404  1.00 51.74  ? 378 HIS   C NE2 1 
ATOM   2158 N  N   . SER   C 1 64  ? 24.112  -8.462  34.966  1.00 53.21  ? 379 SER   C N   1 
ATOM   2159 C  CA  . SER   C 1 64  ? 24.089  -7.869  33.638  1.00 52.52  ? 379 SER   C CA  1 
ATOM   2160 C  C   . SER   C 1 64  ? 23.892  -8.954  32.582  1.00 52.56  ? 379 SER   C C   1 
ATOM   2161 O  O   . SER   C 1 64  ? 24.524  -10.005 32.649  1.00 53.45  ? 379 SER   C O   1 
ATOM   2162 C  CB  . SER   C 1 64  ? 25.347  -7.085  33.372  1.00 52.51  ? 379 SER   C CB  1 
ATOM   2163 O  OG  . SER   C 1 64  ? 25.336  -6.539  32.059  1.00 52.69  ? 379 SER   C OG  1 
ATOM   2164 N  N   . TRP   C 1 65  ? 23.024  -8.670  31.602  1.00 52.54  ? 380 TRP   C N   1 
ATOM   2165 C  CA  . TRP   C 1 65  ? 22.677  -9.622  30.558  1.00 52.66  ? 380 TRP   C CA  1 
ATOM   2166 C  C   . TRP   C 1 65  ? 23.715  -9.619  29.437  1.00 53.42  ? 380 TRP   C C   1 
ATOM   2167 O  O   . TRP   C 1 65  ? 23.736  -10.531 28.612  1.00 53.80  ? 380 TRP   C O   1 
ATOM   2168 C  CB  . TRP   C 1 65  ? 21.281  -9.308  30.003  1.00 51.95  ? 380 TRP   C CB  1 
ATOM   2169 C  CG  . TRP   C 1 65  ? 20.171  -9.497  31.001  1.00 51.78  ? 380 TRP   C CG  1 
ATOM   2170 C  CD1 . TRP   C 1 65  ? 20.175  -10.312 32.095  1.00 52.81  ? 380 TRP   C CD1 1 
ATOM   2171 C  CD2 . TRP   C 1 65  ? 18.876  -8.859  30.982  1.00 52.07  ? 380 TRP   C CD2 1 
ATOM   2172 N  NE1 . TRP   C 1 65  ? 18.981  -10.224 32.759  1.00 53.67  ? 380 TRP   C NE1 1 
ATOM   2173 C  CE2 . TRP   C 1 65  ? 18.164  -9.343  32.101  1.00 53.17  ? 380 TRP   C CE2 1 
ATOM   2174 C  CE3 . TRP   C 1 65  ? 18.254  -7.934  30.137  1.00 52.89  ? 380 TRP   C CE3 1 
ATOM   2175 C  CZ2 . TRP   C 1 65  ? 16.866  -8.931  32.391  1.00 53.42  ? 380 TRP   C CZ2 1 
ATOM   2176 C  CZ3 . TRP   C 1 65  ? 16.969  -7.528  30.425  1.00 52.96  ? 380 TRP   C CZ3 1 
ATOM   2177 C  CH2 . TRP   C 1 65  ? 16.286  -8.022  31.535  1.00 53.21  ? 380 TRP   C CH2 1 
ATOM   2178 N  N   . PHE   C 1 66  ? 24.554  -8.578  29.400  1.00 53.81  ? 381 PHE   C N   1 
ATOM   2179 C  CA  . PHE   C 1 66  ? 25.621  -8.473  28.419  1.00 53.37  ? 381 PHE   C CA  1 
ATOM   2180 C  C   . PHE   C 1 66  ? 26.940  -8.311  29.166  1.00 52.85  ? 381 PHE   C C   1 
ATOM   2181 O  O   . PHE   C 1 66  ? 27.319  -7.196  29.516  1.00 53.03  ? 381 PHE   C O   1 
ATOM   2182 C  CB  . PHE   C 1 66  ? 25.309  -7.308  27.476  1.00 53.82  ? 381 PHE   C CB  1 
ATOM   2183 C  CG  . PHE   C 1 66  ? 23.961  -7.416  26.776  1.00 54.77  ? 381 PHE   C CG  1 
ATOM   2184 C  CD1 . PHE   C 1 66  ? 23.820  -8.155  25.607  1.00 55.64  ? 381 PHE   C CD1 1 
ATOM   2185 C  CD2 . PHE   C 1 66  ? 22.837  -6.777  27.288  1.00 55.72  ? 381 PHE   C CD2 1 
ATOM   2186 C  CE1 . PHE   C 1 66  ? 22.593  -8.247  24.968  1.00 56.14  ? 381 PHE   C CE1 1 
ATOM   2187 C  CE2 . PHE   C 1 66  ? 21.610  -6.874  26.647  1.00 56.09  ? 381 PHE   C CE2 1 
ATOM   2188 C  CZ  . PHE   C 1 66  ? 21.491  -7.608  25.489  1.00 56.24  ? 381 PHE   C CZ  1 
ATOM   2189 N  N   . PRO   C 1 67  ? 27.669  -9.414  29.453  1.00 53.49  ? 382 PRO   C N   1 
ATOM   2190 C  CA  . PRO   C 1 67  ? 28.891  -9.332  30.245  1.00 53.86  ? 382 PRO   C CA  1 
ATOM   2191 C  C   . PRO   C 1 67  ? 29.879  -8.309  29.695  1.00 54.34  ? 382 PRO   C C   1 
ATOM   2192 O  O   . PRO   C 1 67  ? 30.199  -8.333  28.509  1.00 54.16  ? 382 PRO   C O   1 
ATOM   2193 C  CB  . PRO   C 1 67  ? 29.448  -10.753 30.211  1.00 54.12  ? 382 PRO   C CB  1 
ATOM   2194 C  CG  . PRO   C 1 67  ? 28.242  -11.618 29.893  1.00 54.10  ? 382 PRO   C CG  1 
ATOM   2195 C  CD  . PRO   C 1 67  ? 27.353  -10.786 29.025  1.00 53.92  ? 382 PRO   C CD  1 
ATOM   2196 N  N   . GLY   C 1 68  ? 30.335  -7.407  30.574  1.00 55.81  ? 383 GLY   C N   1 
ATOM   2197 C  CA  . GLY   C 1 68  ? 31.227  -6.323  30.197  1.00 56.88  ? 383 GLY   C CA  1 
ATOM   2198 C  C   . GLY   C 1 68  ? 30.536  -4.963  30.275  1.00 58.34  ? 383 GLY   C C   1 
ATOM   2199 O  O   . GLY   C 1 68  ? 31.209  -3.933  30.281  1.00 60.56  ? 383 GLY   C O   1 
ATOM   2200 N  N   . TYR   C 1 69  ? 29.196  -4.970  30.328  1.00 58.37  ? 384 TYR   C N   1 
ATOM   2201 C  CA  . TYR   C 1 69  ? 28.407  -3.747  30.317  1.00 57.66  ? 384 TYR   C CA  1 
ATOM   2202 C  C   . TYR   C 1 69  ? 27.704  -3.561  31.657  1.00 58.05  ? 384 TYR   C C   1 
ATOM   2203 O  O   . TYR   C 1 69  ? 27.377  -4.534  32.334  1.00 58.76  ? 384 TYR   C O   1 
ATOM   2204 C  CB  . TYR   C 1 69  ? 27.353  -3.771  29.207  1.00 56.77  ? 384 TYR   C CB  1 
ATOM   2205 C  CG  . TYR   C 1 69  ? 27.918  -3.671  27.798  1.00 56.45  ? 384 TYR   C CG  1 
ATOM   2206 C  CD1 . TYR   C 1 69  ? 28.375  -4.799  27.128  1.00 55.77  ? 384 TYR   C CD1 1 
ATOM   2207 C  CD2 . TYR   C 1 69  ? 27.990  -2.448  27.139  1.00 56.54  ? 384 TYR   C CD2 1 
ATOM   2208 C  CE1 . TYR   C 1 69  ? 28.890  -4.715  25.846  1.00 56.54  ? 384 TYR   C CE1 1 
ATOM   2209 C  CE2 . TYR   C 1 69  ? 28.504  -2.351  25.856  1.00 56.54  ? 384 TYR   C CE2 1 
ATOM   2210 C  CZ  . TYR   C 1 69  ? 28.955  -3.488  25.209  1.00 57.03  ? 384 TYR   C CZ  1 
ATOM   2211 O  OH  . TYR   C 1 69  ? 29.464  -3.419  23.945  1.00 58.28  ? 384 TYR   C OH  1 
ATOM   2212 N  N   . ALA   C 1 70  ? 27.474  -2.291  32.011  1.00 57.03  ? 385 ALA   C N   1 
ATOM   2213 C  CA  . ALA   C 1 70  ? 26.618  -1.920  33.124  1.00 56.60  ? 385 ALA   C CA  1 
ATOM   2214 C  C   . ALA   C 1 70  ? 25.289  -1.408  32.574  1.00 56.24  ? 385 ALA   C C   1 
ATOM   2215 O  O   . ALA   C 1 70  ? 25.233  -0.946  31.438  1.00 55.54  ? 385 ALA   C O   1 
ATOM   2216 C  CB  . ALA   C 1 70  ? 27.305  -0.876  33.976  1.00 56.46  ? 385 ALA   C CB  1 
ATOM   2217 N  N   . TRP   C 1 71  ? 24.232  -1.488  33.393  1.00 55.65  ? 386 TRP   C N   1 
ATOM   2218 C  CA  . TRP   C 1 71  ? 22.898  -1.072  32.986  1.00 53.95  ? 386 TRP   C CA  1 
ATOM   2219 C  C   . TRP   C 1 71  ? 22.392  0.054   33.885  1.00 52.77  ? 386 TRP   C C   1 
ATOM   2220 O  O   . TRP   C 1 71  ? 22.582  0.022   35.099  1.00 53.15  ? 386 TRP   C O   1 
ATOM   2221 C  CB  . TRP   C 1 71  ? 21.927  -2.263  32.998  1.00 54.00  ? 386 TRP   C CB  1 
ATOM   2222 C  CG  . TRP   C 1 71  ? 21.893  -3.039  34.289  1.00 53.30  ? 386 TRP   C CG  1 
ATOM   2223 C  CD1 . TRP   C 1 71  ? 22.624  -4.150  34.592  1.00 53.49  ? 386 TRP   C CD1 1 
ATOM   2224 C  CD2 . TRP   C 1 71  ? 21.078  -2.766  35.450  1.00 52.25  ? 386 TRP   C CD2 1 
ATOM   2225 N  NE1 . TRP   C 1 71  ? 22.329  -4.584  35.857  1.00 54.11  ? 386 TRP   C NE1 1 
ATOM   2226 C  CE2 . TRP   C 1 71  ? 21.385  -3.758  36.408  1.00 52.59  ? 386 TRP   C CE2 1 
ATOM   2227 C  CE3 . TRP   C 1 71  ? 20.129  -1.790  35.774  1.00 51.85  ? 386 TRP   C CE3 1 
ATOM   2228 C  CZ2 . TRP   C 1 71  ? 20.776  -3.795  37.660  1.00 51.87  ? 386 TRP   C CZ2 1 
ATOM   2229 C  CZ3 . TRP   C 1 71  ? 19.527  -1.830  37.013  1.00 51.37  ? 386 TRP   C CZ3 1 
ATOM   2230 C  CH2 . TRP   C 1 71  ? 19.848  -2.819  37.941  1.00 51.28  ? 386 TRP   C CH2 1 
ATOM   2231 N  N   . THR   C 1 72  ? 21.758  1.054   33.261  1.00 51.54  ? 387 THR   C N   1 
ATOM   2232 C  CA  . THR   C 1 72  ? 21.005  2.077   33.967  1.00 50.43  ? 387 THR   C CA  1 
ATOM   2233 C  C   . THR   C 1 72  ? 19.587  2.083   33.404  1.00 51.17  ? 387 THR   C C   1 
ATOM   2234 O  O   . THR   C 1 72  ? 19.407  1.946   32.197  1.00 52.08  ? 387 THR   C O   1 
ATOM   2235 C  CB  . THR   C 1 72  ? 21.683  3.437   33.805  1.00 49.71  ? 387 THR   C CB  1 
ATOM   2236 O  OG1 . THR   C 1 72  ? 23.019  3.262   34.261  1.00 49.25  ? 387 THR   C OG1 1 
ATOM   2237 C  CG2 . THR   C 1 72  ? 21.015  4.528   34.623  1.00 50.29  ? 387 THR   C CG2 1 
ATOM   2238 N  N   . VAL   C 1 73  ? 18.594  2.247   34.286  1.00 51.06  ? 388 VAL   C N   1 
ATOM   2239 C  CA  . VAL   C 1 73  ? 17.191  2.177   33.905  1.00 50.98  ? 388 VAL   C CA  1 
ATOM   2240 C  C   . VAL   C 1 73  ? 16.846  3.406   33.065  1.00 50.98  ? 388 VAL   C C   1 
ATOM   2241 O  O   . VAL   C 1 73  ? 17.415  4.476   33.268  1.00 50.33  ? 388 VAL   C O   1 
ATOM   2242 C  CB  . VAL   C 1 73  ? 16.282  2.059   35.146  1.00 51.71  ? 388 VAL   C CB  1 
ATOM   2243 C  CG1 . VAL   C 1 73  ? 14.800  2.053   34.783  1.00 51.39  ? 388 VAL   C CG1 1 
ATOM   2244 C  CG2 . VAL   C 1 73  ? 16.623  0.830   35.983  1.00 52.43  ? 388 VAL   C CG2 1 
ATOM   2245 N  N   . ALA   C 1 74  ? 15.907  3.233   32.123  1.00 52.21  ? 389 ALA   C N   1 
ATOM   2246 C  CA  . ALA   C 1 74  ? 15.548  4.273   31.171  1.00 53.13  ? 389 ALA   C CA  1 
ATOM   2247 C  C   . ALA   C 1 74  ? 14.031  4.462   31.141  1.00 54.33  ? 389 ALA   C C   1 
ATOM   2248 O  O   . ALA   C 1 74  ? 13.290  3.495   30.971  1.00 54.25  ? 389 ALA   C O   1 
ATOM   2249 C  CB  . ALA   C 1 74  ? 16.085  3.913   29.804  1.00 52.75  ? 389 ALA   C CB  1 
ATOM   2250 N  N   . GLN   C 1 75  ? 13.592  5.722   31.284  1.00 56.06  ? 390 GLN   C N   1 
ATOM   2251 C  CA  . GLN   C 1 75  ? 12.181  6.073   31.344  1.00 57.90  ? 390 GLN   C CA  1 
ATOM   2252 C  C   . GLN   C 1 75  ? 11.820  7.059   30.239  1.00 56.84  ? 390 GLN   C C   1 
ATOM   2253 O  O   . GLN   C 1 75  ? 12.641  7.887   29.854  1.00 58.04  ? 390 GLN   C O   1 
ATOM   2254 C  CB  . GLN   C 1 75  ? 11.813  6.818   32.627  1.00 60.65  ? 390 GLN   C CB  1 
ATOM   2255 C  CG  . GLN   C 1 75  ? 11.699  5.944   33.869  1.00 63.14  ? 390 GLN   C CG  1 
ATOM   2256 C  CD  . GLN   C 1 75  ? 11.219  6.722   35.076  1.00 64.78  ? 390 GLN   C CD  1 
ATOM   2257 O  OE1 . GLN   C 1 75  ? 11.072  7.949   35.035  1.00 65.02  ? 390 GLN   C OE1 1 
ATOM   2258 N  NE2 . GLN   C 1 75  ? 10.972  6.012   36.167  1.00 65.57  ? 390 GLN   C NE2 1 
ATOM   2259 N  N   . CYS   C 1 76  ? 10.563  6.993   29.788  1.00 55.98  ? 391 CYS   C N   1 
ATOM   2260 C  CA  . CYS   C 1 76  ? 10.007  7.979   28.876  1.00 56.30  ? 391 CYS   C CA  1 
ATOM   2261 C  C   . CYS   C 1 76  ? 10.009  9.352   29.543  1.00 56.97  ? 391 CYS   C C   1 
ATOM   2262 O  O   . CYS   C 1 76  ? 9.542   9.487   30.670  1.00 58.82  ? 391 CYS   C O   1 
ATOM   2263 C  CB  . CYS   C 1 76  ? 8.587   7.598   28.475  1.00 56.48  ? 391 CYS   C CB  1 
ATOM   2264 S  SG  . CYS   C 1 76  ? 7.808   8.781   27.346  1.00 57.32  ? 391 CYS   C SG  1 
ATOM   2265 N  N   . LYS   C 1 77  ? 10.532  10.361  28.832  1.00 58.37  ? 392 LYS   C N   1 
ATOM   2266 C  CA  . LYS   C 1 77  ? 10.569  11.736  29.312  1.00 58.83  ? 392 LYS   C CA  1 
ATOM   2267 C  C   . LYS   C 1 77  ? 9.184   12.219  29.735  1.00 57.46  ? 392 LYS   C C   1 
ATOM   2268 O  O   . LYS   C 1 77  ? 9.063   13.005  30.670  1.00 55.67  ? 392 LYS   C O   1 
ATOM   2269 C  CB  . LYS   C 1 77  ? 11.052  12.721  28.239  1.00 61.40  ? 392 LYS   C CB  1 
ATOM   2270 C  CG  . LYS   C 1 77  ? 12.523  13.103  28.274  1.00 64.08  ? 392 LYS   C CG  1 
ATOM   2271 C  CD  . LYS   C 1 77  ? 12.852  14.226  27.295  1.00 67.38  ? 392 LYS   C CD  1 
ATOM   2272 C  CE  . LYS   C 1 77  ? 14.161  14.901  27.568  1.00 69.79  ? 392 LYS   C CE  1 
ATOM   2273 N  NZ  . LYS   C 1 77  ? 15.286  13.962  27.564  1.00 71.21  ? 392 LYS   C NZ  1 
ATOM   2274 N  N   . ILE   C 1 78  ? 8.148   11.762  29.024  1.00 57.49  ? 393 ILE   C N   1 
ATOM   2275 C  CA  . ILE   C 1 78  ? 6.821   12.341  29.135  1.00 57.80  ? 393 ILE   C CA  1 
ATOM   2276 C  C   . ILE   C 1 78  ? 6.059   11.690  30.288  1.00 56.85  ? 393 ILE   C C   1 
ATOM   2277 O  O   . ILE   C 1 78  ? 5.688   12.376  31.237  1.00 57.76  ? 393 ILE   C O   1 
ATOM   2278 C  CB  . ILE   C 1 78  ? 6.073   12.213  27.794  1.00 58.61  ? 393 ILE   C CB  1 
ATOM   2279 C  CG1 . ILE   C 1 78  ? 6.912   12.752  26.629  1.00 58.71  ? 393 ILE   C CG1 1 
ATOM   2280 C  CG2 . ILE   C 1 78  ? 4.700   12.883  27.859  1.00 59.71  ? 393 ILE   C CG2 1 
ATOM   2281 C  CD1 . ILE   C 1 78  ? 7.515   14.126  26.870  1.00 58.53  ? 393 ILE   C CD1 1 
ATOM   2282 N  N   . CYS   C 1 79  ? 5.830   10.374  30.195  1.00 56.32  ? 394 CYS   C N   1 
ATOM   2283 C  CA  . CYS   C 1 79  ? 4.918   9.682   31.096  1.00 55.43  ? 394 CYS   C CA  1 
ATOM   2284 C  C   . CYS   C 1 79  ? 5.664   8.882   32.167  1.00 55.52  ? 394 CYS   C C   1 
ATOM   2285 O  O   . CYS   C 1 79  ? 5.025   8.240   32.997  1.00 55.99  ? 394 CYS   C O   1 
ATOM   2286 C  CB  . CYS   C 1 79  ? 3.978   8.776   30.310  1.00 55.01  ? 394 CYS   C CB  1 
ATOM   2287 S  SG  . CYS   C 1 79  ? 4.827   7.461   29.398  1.00 54.04  ? 394 CYS   C SG  1 
ATOM   2288 N  N   . ALA   C 1 80  ? 7.006   8.911   32.137  1.00 55.57  ? 395 ALA   C N   1 
ATOM   2289 C  CA  . ALA   C 1 80  ? 7.849   8.230   33.114  1.00 55.26  ? 395 ALA   C CA  1 
ATOM   2290 C  C   . ALA   C 1 80  ? 7.656   6.715   33.069  1.00 55.77  ? 395 ALA   C C   1 
ATOM   2291 O  O   . ALA   C 1 80  ? 7.971   6.024   34.036  1.00 54.29  ? 395 ALA   C O   1 
ATOM   2292 C  CB  . ALA   C 1 80  ? 7.589   8.768   34.504  1.00 54.75  ? 395 ALA   C CB  1 
ATOM   2293 N  N   . SER   C 1 81  ? 7.160   6.205   31.936  1.00 57.08  ? 396 SER   C N   1 
ATOM   2294 C  CA  . SER   C 1 81  ? 6.977   4.776   31.753  1.00 58.36  ? 396 SER   C CA  1 
ATOM   2295 C  C   . SER   C 1 81  ? 8.336   4.130   31.495  1.00 58.70  ? 396 SER   C C   1 
ATOM   2296 O  O   . SER   C 1 81  ? 9.089   4.601   30.647  1.00 58.72  ? 396 SER   C O   1 
ATOM   2297 C  CB  . SER   C 1 81  ? 6.010   4.500   30.630  1.00 59.67  ? 396 SER   C CB  1 
ATOM   2298 O  OG  . SER   C 1 81  ? 5.845   3.104   30.424  1.00 61.97  ? 396 SER   C OG  1 
ATOM   2299 N  N   . HIS   C 1 82  ? 8.643   3.069   32.251  1.00 59.81  ? 397 HIS   C N   1 
ATOM   2300 C  CA  . HIS   C 1 82  ? 9.879   2.320   32.079  1.00 61.24  ? 397 HIS   C CA  1 
ATOM   2301 C  C   . HIS   C 1 82  ? 9.868   1.685   30.691  1.00 60.08  ? 397 HIS   C C   1 
ATOM   2302 O  O   . HIS   C 1 82  ? 8.952   0.935   30.363  1.00 61.06  ? 397 HIS   C O   1 
ATOM   2303 C  CB  . HIS   C 1 82  ? 10.042  1.309   33.224  1.00 64.19  ? 397 HIS   C CB  1 
ATOM   2304 C  CG  . HIS   C 1 82  ? 11.128  0.289   33.061  1.00 67.77  ? 397 HIS   C CG  1 
ATOM   2305 N  ND1 . HIS   C 1 82  ? 11.802  -0.203  34.159  1.00 69.61  ? 397 HIS   C ND1 1 
ATOM   2306 C  CD2 . HIS   C 1 82  ? 11.648  -0.353  31.999  1.00 68.75  ? 397 HIS   C CD2 1 
ATOM   2307 C  CE1 . HIS   C 1 82  ? 12.698  -1.097  33.764  1.00 69.30  ? 397 HIS   C CE1 1 
ATOM   2308 N  NE2 . HIS   C 1 82  ? 12.621  -1.203  32.456  1.00 68.82  ? 397 HIS   C NE2 1 
ATOM   2309 N  N   . ILE   C 1 83  ? 10.893  2.000   29.887  1.00 58.43  ? 398 ILE   C N   1 
ATOM   2310 C  CA  . ILE   C 1 83  ? 11.002  1.500   28.525  1.00 57.68  ? 398 ILE   C CA  1 
ATOM   2311 C  C   . ILE   C 1 83  ? 12.060  0.400   28.467  1.00 57.41  ? 398 ILE   C C   1 
ATOM   2312 O  O   . ILE   C 1 83  ? 11.851  -0.620  27.814  1.00 58.31  ? 398 ILE   C O   1 
ATOM   2313 C  CB  . ILE   C 1 83  ? 11.320  2.642   27.540  1.00 57.74  ? 398 ILE   C CB  1 
ATOM   2314 C  CG1 . ILE   C 1 83  ? 10.307  3.787   27.631  1.00 57.96  ? 398 ILE   C CG1 1 
ATOM   2315 C  CG2 . ILE   C 1 83  ? 11.435  2.114   26.110  1.00 58.21  ? 398 ILE   C CG2 1 
ATOM   2316 C  CD1 . ILE   C 1 83  ? 8.892   3.411   27.223  1.00 58.52  ? 398 ILE   C CD1 1 
ATOM   2317 N  N   . GLY   C 1 84  ? 13.205  0.623   29.125  1.00 55.80  ? 399 GLY   C N   1 
ATOM   2318 C  CA  . GLY   C 1 84  ? 14.282  -0.353  29.135  1.00 53.42  ? 399 GLY   C CA  1 
ATOM   2319 C  C   . GLY   C 1 84  ? 15.480  0.133   29.948  1.00 51.89  ? 399 GLY   C C   1 
ATOM   2320 O  O   . GLY   C 1 84  ? 15.312  0.812   30.958  1.00 50.34  ? 399 GLY   C O   1 
ATOM   2321 N  N   . TRP   C 1 85  ? 16.684  -0.240  29.494  1.00 51.89  ? 400 TRP   C N   1 
ATOM   2322 C  CA  . TRP   C 1 85  ? 17.927  0.137   30.148  1.00 51.77  ? 400 TRP   C CA  1 
ATOM   2323 C  C   . TRP   C 1 85  ? 18.914  0.669   29.113  1.00 52.24  ? 400 TRP   C C   1 
ATOM   2324 O  O   . TRP   C 1 85  ? 18.755  0.433   27.916  1.00 52.88  ? 400 TRP   C O   1 
ATOM   2325 C  CB  . TRP   C 1 85  ? 18.539  -1.057  30.896  1.00 51.86  ? 400 TRP   C CB  1 
ATOM   2326 C  CG  . TRP   C 1 85  ? 17.600  -1.737  31.856  1.00 52.27  ? 400 TRP   C CG  1 
ATOM   2327 C  CD1 . TRP   C 1 85  ? 17.547  -1.588  33.210  1.00 52.77  ? 400 TRP   C CD1 1 
ATOM   2328 C  CD2 . TRP   C 1 85  ? 16.561  -2.679  31.515  1.00 52.96  ? 400 TRP   C CD2 1 
ATOM   2329 N  NE1 . TRP   C 1 85  ? 16.556  -2.373  33.738  1.00 53.11  ? 400 TRP   C NE1 1 
ATOM   2330 C  CE2 . TRP   C 1 85  ? 15.932  -3.051  32.723  1.00 53.50  ? 400 TRP   C CE2 1 
ATOM   2331 C  CE3 . TRP   C 1 85  ? 16.104  -3.237  30.315  1.00 53.48  ? 400 TRP   C CE3 1 
ATOM   2332 C  CZ2 . TRP   C 1 85  ? 14.872  -3.956  32.758  1.00 53.89  ? 400 TRP   C CZ2 1 
ATOM   2333 C  CZ3 . TRP   C 1 85  ? 15.055  -4.130  30.351  1.00 54.35  ? 400 TRP   C CZ3 1 
ATOM   2334 C  CH2 . TRP   C 1 85  ? 14.449  -4.482  31.558  1.00 54.12  ? 400 TRP   C CH2 1 
ATOM   2335 N  N   . LYS   C 1 86  ? 19.937  1.380   29.601  1.00 52.16  ? 401 LYS   C N   1 
ATOM   2336 C  CA  . LYS   C 1 86  ? 21.039  1.845   28.776  1.00 51.54  ? 401 LYS   C CA  1 
ATOM   2337 C  C   . LYS   C 1 86  ? 22.317  1.148   29.225  1.00 50.20  ? 401 LYS   C C   1 
ATOM   2338 O  O   . LYS   C 1 86  ? 22.697  1.245   30.390  1.00 48.79  ? 401 LYS   C O   1 
ATOM   2339 C  CB  . LYS   C 1 86  ? 21.242  3.358   28.901  1.00 52.88  ? 401 LYS   C CB  1 
ATOM   2340 C  CG  . LYS   C 1 86  ? 22.371  3.916   28.043  1.00 54.24  ? 401 LYS   C CG  1 
ATOM   2341 C  CD  . LYS   C 1 86  ? 22.710  5.370   28.340  1.00 55.00  ? 401 LYS   C CD  1 
ATOM   2342 C  CE  . LYS   C 1 86  ? 23.873  5.853   27.538  1.00 56.35  ? 401 LYS   C CE  1 
ATOM   2343 N  NZ  . LYS   C 1 86  ? 24.232  7.223   27.911  1.00 57.40  ? 401 LYS   C NZ  1 
ATOM   2344 N  N   . PHE   C 1 87  ? 22.983  0.476   28.280  1.00 50.23  ? 402 PHE   C N   1 
ATOM   2345 C  CA  . PHE   C 1 87  ? 24.178  -0.293  28.581  1.00 51.01  ? 402 PHE   C CA  1 
ATOM   2346 C  C   . PHE   C 1 87  ? 25.412  0.547   28.268  1.00 51.48  ? 402 PHE   C C   1 
ATOM   2347 O  O   . PHE   C 1 87  ? 25.495  1.156   27.206  1.00 51.29  ? 402 PHE   C O   1 
ATOM   2348 C  CB  . PHE   C 1 87  ? 24.124  -1.620  27.821  1.00 51.07  ? 402 PHE   C CB  1 
ATOM   2349 C  CG  . PHE   C 1 87  ? 23.081  -2.571  28.390  1.00 50.67  ? 402 PHE   C CG  1 
ATOM   2350 C  CD1 . PHE   C 1 87  ? 23.399  -3.427  29.439  1.00 50.40  ? 402 PHE   C CD1 1 
ATOM   2351 C  CD2 . PHE   C 1 87  ? 21.779  -2.582  27.900  1.00 50.55  ? 402 PHE   C CD2 1 
ATOM   2352 C  CE1 . PHE   C 1 87  ? 22.446  -4.283  29.967  1.00 50.16  ? 402 PHE   C CE1 1 
ATOM   2353 C  CE2 . PHE   C 1 87  ? 20.829  -3.440  28.433  1.00 49.96  ? 402 PHE   C CE2 1 
ATOM   2354 C  CZ  . PHE   C 1 87  ? 21.164  -4.288  29.465  1.00 50.02  ? 402 PHE   C CZ  1 
ATOM   2355 N  N   . THR   C 1 88  ? 26.351  0.570   29.221  1.00 53.10  ? 403 THR   C N   1 
ATOM   2356 C  CA  . THR   C 1 88  ? 27.593  1.315   29.096  1.00 55.56  ? 403 THR   C CA  1 
ATOM   2357 C  C   . THR   C 1 88  ? 28.758  0.367   29.372  1.00 57.38  ? 403 THR   C C   1 
ATOM   2358 O  O   . THR   C 1 88  ? 28.726  -0.386  30.343  1.00 57.63  ? 403 THR   C O   1 
ATOM   2359 C  CB  . THR   C 1 88  ? 27.579  2.500   30.062  1.00 56.12  ? 403 THR   C CB  1 
ATOM   2360 O  OG1 . THR   C 1 88  ? 27.256  1.983   31.349  1.00 55.91  ? 403 THR   C OG1 1 
ATOM   2361 C  CG2 . THR   C 1 88  ? 26.553  3.552   29.678  1.00 56.19  ? 403 THR   C CG2 1 
ATOM   2362 N  N   . ALA   C 1 89  ? 29.777  0.413   28.504  1.00 59.12  ? 404 ALA   C N   1 
ATOM   2363 C  CA  . ALA   C 1 89  ? 30.927  -0.473  28.609  1.00 60.69  ? 404 ALA   C CA  1 
ATOM   2364 C  C   . ALA   C 1 89  ? 31.744  -0.120  29.850  1.00 62.46  ? 404 ALA   C C   1 
ATOM   2365 O  O   . ALA   C 1 89  ? 31.709  1.017   30.315  1.00 61.96  ? 404 ALA   C O   1 
ATOM   2366 C  CB  . ALA   C 1 89  ? 31.764  -0.385  27.353  1.00 60.71  ? 404 ALA   C CB  1 
ATOM   2367 N  N   . THR   C 1 90  ? 32.474  -1.111  30.375  1.00 64.61  ? 405 THR   C N   1 
ATOM   2368 C  CA  . THR   C 1 90  ? 33.233  -0.944  31.605  1.00 67.08  ? 405 THR   C CA  1 
ATOM   2369 C  C   . THR   C 1 90  ? 34.717  -0.731  31.302  1.00 71.03  ? 405 THR   C C   1 
ATOM   2370 O  O   . THR   C 1 90  ? 35.485  -0.439  32.216  1.00 71.40  ? 405 THR   C O   1 
ATOM   2371 C  CB  . THR   C 1 90  ? 33.008  -2.155  32.510  1.00 66.36  ? 405 THR   C CB  1 
ATOM   2372 O  OG1 . THR   C 1 90  ? 33.323  -3.300  31.725  1.00 66.48  ? 405 THR   C OG1 1 
ATOM   2373 C  CG2 . THR   C 1 90  ? 31.576  -2.249  33.008  1.00 66.09  ? 405 THR   C CG2 1 
ATOM   2374 N  N   . LYS   C 1 91  ? 35.114  -0.881  30.029  1.00 75.96  ? 406 LYS   C N   1 
ATOM   2375 C  CA  . LYS   C 1 91  ? 36.487  -0.649  29.605  1.00 79.53  ? 406 LYS   C CA  1 
ATOM   2376 C  C   . LYS   C 1 91  ? 36.489  0.093   28.271  1.00 82.15  ? 406 LYS   C C   1 
ATOM   2377 O  O   . LYS   C 1 91  ? 35.489  0.096   27.555  1.00 81.27  ? 406 LYS   C O   1 
ATOM   2378 C  CB  . LYS   C 1 91  ? 37.262  -1.963  29.455  1.00 80.86  ? 406 LYS   C CB  1 
ATOM   2379 C  CG  . LYS   C 1 91  ? 37.440  -2.778  30.730  1.00 83.02  ? 406 LYS   C CG  1 
ATOM   2380 C  CD  . LYS   C 1 91  ? 37.456  -4.282  30.483  1.00 85.65  ? 406 LYS   C CD  1 
ATOM   2381 C  CE  . LYS   C 1 91  ? 36.092  -4.807  30.148  1.00 87.28  ? 406 LYS   C CE  1 
ATOM   2382 N  NZ  . LYS   C 1 91  ? 36.149  -6.064  29.397  1.00 88.20  ? 406 LYS   C NZ  1 
ATOM   2383 N  N   . LYS   C 1 92  ? 37.639  0.694   27.944  1.00 84.70  ? 407 LYS   C N   1 
ATOM   2384 C  CA  . LYS   C 1 92  ? 37.769  1.582   26.798  1.00 87.41  ? 407 LYS   C CA  1 
ATOM   2385 C  C   . LYS   C 1 92  ? 37.777  0.795   25.488  1.00 87.07  ? 407 LYS   C C   1 
ATOM   2386 O  O   . LYS   C 1 92  ? 37.357  1.315   24.455  1.00 87.46  ? 407 LYS   C O   1 
ATOM   2387 C  CB  . LYS   C 1 92  ? 39.052  2.415   26.923  1.00 90.08  ? 407 LYS   C CB  1 
ATOM   2388 C  CG  . LYS   C 1 92  ? 38.992  3.607   27.875  1.00 92.43  ? 407 LYS   C CG  1 
ATOM   2389 C  CD  . LYS   C 1 92  ? 38.610  4.932   27.221  1.00 95.28  ? 407 LYS   C CD  1 
ATOM   2390 C  CE  . LYS   C 1 92  ? 37.238  4.970   26.620  1.00 97.17  ? 407 LYS   C CE  1 
ATOM   2391 N  NZ  . LYS   C 1 92  ? 36.184  4.835   27.629  1.00 99.17  ? 407 LYS   C NZ  1 
ATOM   2392 N  N   . ASP   C 1 93  ? 38.250  -0.456  25.537  1.00 85.62  ? 408 ASP   C N   1 
ATOM   2393 C  CA  . ASP   C 1 93  ? 38.577  -1.209  24.335  1.00 84.85  ? 408 ASP   C CA  1 
ATOM   2394 C  C   . ASP   C 1 93  ? 37.337  -1.854  23.714  1.00 81.93  ? 408 ASP   C C   1 
ATOM   2395 O  O   . ASP   C 1 93  ? 37.372  -2.234  22.547  1.00 83.30  ? 408 ASP   C O   1 
ATOM   2396 C  CB  . ASP   C 1 93  ? 39.645  -2.254  24.617  1.00 87.03  ? 408 ASP   C CB  1 
ATOM   2397 C  CG  . ASP   C 1 93  ? 39.286  -3.279  25.683  1.00 89.46  ? 408 ASP   C CG  1 
ATOM   2398 O  OD1 . ASP   C 1 93  ? 39.095  -2.870  26.848  1.00 91.35  ? 408 ASP   C OD1 1 
ATOM   2399 O  OD2 . ASP   C 1 93  ? 39.191  -4.475  25.337  1.00 92.85  ? 408 ASP   C OD2 1 
ATOM   2400 N  N   . MET   C 1 94  ? 36.253  -1.983  24.489  1.00 78.96  ? 409 MET   C N   1 
ATOM   2401 C  CA  . MET   C 1 94  ? 35.053  -2.665  24.027  1.00 76.41  ? 409 MET   C CA  1 
ATOM   2402 C  C   . MET   C 1 94  ? 34.351  -1.845  22.947  1.00 73.29  ? 409 MET   C C   1 
ATOM   2403 O  O   . MET   C 1 94  ? 34.612  -0.654  22.788  1.00 72.24  ? 409 MET   C O   1 
ATOM   2404 C  CB  . MET   C 1 94  ? 34.071  -2.898  25.180  1.00 77.84  ? 409 MET   C CB  1 
ATOM   2405 C  CG  . MET   C 1 94  ? 34.584  -3.841  26.250  1.00 78.74  ? 409 MET   C CG  1 
ATOM   2406 S  SD  . MET   C 1 94  ? 33.509  -3.888  27.698  1.00 79.90  ? 409 MET   C SD  1 
ATOM   2407 C  CE  . MET   C 1 94  ? 31.939  -4.347  26.950  1.00 79.51  ? 409 MET   C CE  1 
ATOM   2408 N  N   . SER   C 1 95  ? 33.447  -2.509  22.219  1.00 70.55  ? 410 SER   C N   1 
ATOM   2409 C  CA  . SER   C 1 95  ? 32.689  -1.898  21.140  1.00 69.80  ? 410 SER   C CA  1 
ATOM   2410 C  C   . SER   C 1 95  ? 31.379  -2.637  20.868  1.00 69.70  ? 410 SER   C C   1 
ATOM   2411 O  O   . SER   C 1 95  ? 31.395  -3.854  20.698  1.00 70.36  ? 410 SER   C O   1 
ATOM   2412 C  CB  . SER   C 1 95  ? 33.528  -1.825  19.891  1.00 70.08  ? 410 SER   C CB  1 
ATOM   2413 O  OG  . SER   C 1 95  ? 32.792  -1.275  18.807  1.00 71.53  ? 410 SER   C OG  1 
ATOM   2414 N  N   . PRO   C 1 96  ? 30.205  -1.958  20.818  1.00 68.31  ? 411 PRO   C N   1 
ATOM   2415 C  CA  . PRO   C 1 96  ? 30.100  -0.519  21.046  1.00 66.90  ? 411 PRO   C CA  1 
ATOM   2416 C  C   . PRO   C 1 96  ? 30.286  -0.124  22.508  1.00 66.11  ? 411 PRO   C C   1 
ATOM   2417 O  O   . PRO   C 1 96  ? 30.241  -0.975  23.393  1.00 67.81  ? 411 PRO   C O   1 
ATOM   2418 C  CB  . PRO   C 1 96  ? 28.695  -0.183  20.553  1.00 66.58  ? 411 PRO   C CB  1 
ATOM   2419 C  CG  . PRO   C 1 96  ? 27.930  -1.471  20.793  1.00 66.79  ? 411 PRO   C CG  1 
ATOM   2420 C  CD  . PRO   C 1 96  ? 28.902  -2.579  20.528  1.00 67.27  ? 411 PRO   C CD  1 
ATOM   2421 N  N   . GLN   C 1 97  ? 30.490  1.177   22.746  1.00 64.69  ? 412 GLN   C N   1 
ATOM   2422 C  CA  . GLN   C 1 97  ? 30.752  1.682   24.085  1.00 64.26  ? 412 GLN   C CA  1 
ATOM   2423 C  C   . GLN   C 1 97  ? 29.441  1.863   24.849  1.00 63.70  ? 412 GLN   C C   1 
ATOM   2424 O  O   . GLN   C 1 97  ? 29.430  1.776   26.076  1.00 63.52  ? 412 GLN   C O   1 
ATOM   2425 C  CB  . GLN   C 1 97  ? 31.590  2.960   24.024  1.00 64.45  ? 412 GLN   C CB  1 
ATOM   2426 C  CG  . GLN   C 1 97  ? 33.080  2.704   23.818  1.00 65.05  ? 412 GLN   C CG  1 
ATOM   2427 C  CD  . GLN   C 1 97  ? 33.759  2.133   25.045  1.00 65.34  ? 412 GLN   C CD  1 
ATOM   2428 O  OE1 . GLN   C 1 97  ? 34.092  0.943   25.105  1.00 65.74  ? 412 GLN   C OE1 1 
ATOM   2429 N  NE2 . GLN   C 1 97  ? 33.954  2.975   26.049  1.00 64.69  ? 412 GLN   C NE2 1 
ATOM   2430 N  N   . LYS   C 1 98  ? 28.344  2.114   24.124  1.00 62.69  ? 413 LYS   C N   1 
ATOM   2431 C  CA  . LYS   C 1 98  ? 27.028  2.170   24.738  1.00 62.36  ? 413 LYS   C CA  1 
ATOM   2432 C  C   . LYS   C 1 98  ? 25.970  1.724   23.731  1.00 59.53  ? 413 LYS   C C   1 
ATOM   2433 O  O   . LYS   C 1 98  ? 26.179  1.811   22.522  1.00 58.95  ? 413 LYS   C O   1 
ATOM   2434 C  CB  . LYS   C 1 98  ? 26.759  3.565   25.324  1.00 64.48  ? 413 LYS   C CB  1 
ATOM   2435 C  CG  . LYS   C 1 98  ? 26.810  4.749   24.359  1.00 66.27  ? 413 LYS   C CG  1 
ATOM   2436 C  CD  . LYS   C 1 98  ? 25.523  5.011   23.582  1.00 68.01  ? 413 LYS   C CD  1 
ATOM   2437 C  CE  . LYS   C 1 98  ? 25.664  6.112   22.576  1.00 68.78  ? 413 LYS   C CE  1 
ATOM   2438 N  NZ  . LYS   C 1 98  ? 24.477  6.212   21.723  1.00 69.28  ? 413 LYS   C NZ  1 
ATOM   2439 N  N   . PHE   C 1 99  ? 24.843  1.227   24.256  1.00 56.37  ? 414 PHE   C N   1 
ATOM   2440 C  CA  . PHE   C 1 99  ? 23.686  0.871   23.450  1.00 53.70  ? 414 PHE   C CA  1 
ATOM   2441 C  C   . PHE   C 1 99  ? 22.470  0.799   24.370  1.00 52.03  ? 414 PHE   C C   1 
ATOM   2442 O  O   . PHE   C 1 99  ? 22.574  1.116   25.553  1.00 51.74  ? 414 PHE   C O   1 
ATOM   2443 C  CB  . PHE   C 1 99  ? 23.939  -0.437  22.692  1.00 53.04  ? 414 PHE   C CB  1 
ATOM   2444 C  CG  . PHE   C 1 99  ? 23.979  -1.686  23.562  1.00 52.77  ? 414 PHE   C CG  1 
ATOM   2445 C  CD1 . PHE   C 1 99  ? 25.171  -2.118  24.137  1.00 52.78  ? 414 PHE   C CD1 1 
ATOM   2446 C  CD2 . PHE   C 1 99  ? 22.827  -2.430  23.796  1.00 52.03  ? 414 PHE   C CD2 1 
ATOM   2447 C  CE1 . PHE   C 1 99  ? 25.205  -3.258  24.927  1.00 52.23  ? 414 PHE   C CE1 1 
ATOM   2448 C  CE2 . PHE   C 1 99  ? 22.867  -3.568  24.588  1.00 52.23  ? 414 PHE   C CE2 1 
ATOM   2449 C  CZ  . PHE   C 1 99  ? 24.055  -3.979  25.151  1.00 52.07  ? 414 PHE   C CZ  1 
ATOM   2450 N  N   . TRP   C 1 100 ? 21.326  0.382   23.814  1.00 51.42  ? 415 TRP   C N   1 
ATOM   2451 C  CA  . TRP   C 1 100 ? 20.070  0.357   24.545  1.00 51.88  ? 415 TRP   C CA  1 
ATOM   2452 C  C   . TRP   C 1 100 ? 19.373  -0.987  24.355  1.00 51.66  ? 415 TRP   C C   1 
ATOM   2453 O  O   . TRP   C 1 100 ? 19.169  -1.419  23.224  1.00 51.74  ? 415 TRP   C O   1 
ATOM   2454 C  CB  . TRP   C 1 100 ? 19.163  1.498   24.065  1.00 52.41  ? 415 TRP   C CB  1 
ATOM   2455 C  CG  . TRP   C 1 100 ? 19.810  2.857   24.106  1.00 54.26  ? 415 TRP   C CG  1 
ATOM   2456 C  CD1 . TRP   C 1 100 ? 20.719  3.360   23.221  1.00 55.18  ? 415 TRP   C CD1 1 
ATOM   2457 C  CD2 . TRP   C 1 100 ? 19.577  3.900   25.078  1.00 53.80  ? 415 TRP   C CD2 1 
ATOM   2458 N  NE1 . TRP   C 1 100 ? 21.081  4.632   23.579  1.00 54.64  ? 415 TRP   C NE1 1 
ATOM   2459 C  CE2 . TRP   C 1 100 ? 20.394  4.992   24.709  1.00 53.85  ? 415 TRP   C CE2 1 
ATOM   2460 C  CE3 . TRP   C 1 100 ? 18.766  4.017   26.214  1.00 53.05  ? 415 TRP   C CE3 1 
ATOM   2461 C  CZ2 . TRP   C 1 100 ? 20.420  6.179   25.439  1.00 53.10  ? 415 TRP   C CZ2 1 
ATOM   2462 C  CZ3 . TRP   C 1 100 ? 18.791  5.193   26.931  1.00 52.97  ? 415 TRP   C CZ3 1 
ATOM   2463 C  CH2 . TRP   C 1 100 ? 19.607  6.257   26.547  1.00 53.41  ? 415 TRP   C CH2 1 
ATOM   2464 N  N   . GLY   C 1 101 ? 19.013  -1.629  25.473  1.00 51.11  ? 416 GLY   C N   1 
ATOM   2465 C  CA  . GLY   C 1 101 ? 18.122  -2.779  25.466  1.00 51.37  ? 416 GLY   C CA  1 
ATOM   2466 C  C   . GLY   C 1 101 ? 16.725  -2.369  25.928  1.00 52.08  ? 416 GLY   C C   1 
ATOM   2467 O  O   . GLY   C 1 101 ? 16.562  -1.906  27.055  1.00 52.56  ? 416 GLY   C O   1 
ATOM   2468 N  N   . LEU   C 1 102 ? 15.729  -2.543  25.050  1.00 51.86  ? 417 LEU   C N   1 
ATOM   2469 C  CA  . LEU   C 1 102 ? 14.398  -1.995  25.266  1.00 51.80  ? 417 LEU   C CA  1 
ATOM   2470 C  C   . LEU   C 1 102 ? 13.379  -3.119  25.425  1.00 51.06  ? 417 LEU   C C   1 
ATOM   2471 O  O   . LEU   C 1 102 ? 13.442  -4.122  24.719  1.00 51.55  ? 417 LEU   C O   1 
ATOM   2472 C  CB  . LEU   C 1 102 ? 14.035  -1.093  24.087  1.00 52.06  ? 417 LEU   C CB  1 
ATOM   2473 C  CG  . LEU   C 1 102 ? 15.051  -0.004  23.726  1.00 52.03  ? 417 LEU   C CG  1 
ATOM   2474 C  CD1 . LEU   C 1 102 ? 14.549  0.823   22.554  1.00 52.30  ? 417 LEU   C CD1 1 
ATOM   2475 C  CD2 . LEU   C 1 102 ? 15.371  0.889   24.912  1.00 51.32  ? 417 LEU   C CD2 1 
ATOM   2476 N  N   . THR   C 1 103 ? 12.431  -2.921  26.348  1.00 50.18  ? 418 THR   C N   1 
ATOM   2477 C  CA  . THR   C 1 103 ? 11.290  -3.809  26.494  1.00 50.64  ? 418 THR   C CA  1 
ATOM   2478 C  C   . THR   C 1 103 ? 10.403  -3.653  25.262  1.00 50.90  ? 418 THR   C C   1 
ATOM   2479 O  O   . THR   C 1 103 ? 9.954   -2.550  24.962  1.00 49.37  ? 418 THR   C O   1 
ATOM   2480 C  CB  . THR   C 1 103 ? 10.536  -3.469  27.780  1.00 51.87  ? 418 THR   C CB  1 
ATOM   2481 O  OG1 . THR   C 1 103 ? 11.498  -3.514  28.831  1.00 51.71  ? 418 THR   C OG1 1 
ATOM   2482 C  CG2 . THR   C 1 103 ? 9.400   -4.433  28.070  1.00 52.59  ? 418 THR   C CG2 1 
ATOM   2483 N  N   . ARG   C 1 104 ? 10.158  -4.767  24.559  1.00 52.89  ? 419 ARG   C N   1 
ATOM   2484 C  CA  . ARG   C 1 104 ? 9.419   -4.747  23.306  1.00 54.32  ? 419 ARG   C CA  1 
ATOM   2485 C  C   . ARG   C 1 104 ? 7.941   -4.454  23.563  1.00 54.74  ? 419 ARG   C C   1 
ATOM   2486 O  O   . ARG   C 1 104 ? 7.278   -3.838  22.731  1.00 54.23  ? 419 ARG   C O   1 
ATOM   2487 C  CB  . ARG   C 1 104 ? 9.601   -6.064  22.543  1.00 55.19  ? 419 ARG   C CB  1 
ATOM   2488 C  CG  . ARG   C 1 104 ? 11.048  -6.340  22.158  1.00 55.92  ? 419 ARG   C CG  1 
ATOM   2489 C  CD  . ARG   C 1 104 ? 11.177  -7.265  20.958  1.00 57.07  ? 419 ARG   C CD  1 
ATOM   2490 N  NE  . ARG   C 1 104 ? 10.610  -8.599  21.187  1.00 58.50  ? 419 ARG   C NE  1 
ATOM   2491 C  CZ  . ARG   C 1 104 ? 11.305  -9.693  21.491  1.00 61.10  ? 419 ARG   C CZ  1 
ATOM   2492 N  NH1 . ARG   C 1 104 ? 12.593  -9.619  21.778  1.00 62.52  ? 419 ARG   C NH1 1 
ATOM   2493 N  NH2 . ARG   C 1 104 ? 10.698  -10.866 21.554  1.00 62.11  ? 419 ARG   C NH2 1 
ATOM   2494 N  N   . SER   C 1 105 ? 7.442   -4.883  24.729  1.00 55.08  ? 420 SER   C N   1 
ATOM   2495 C  CA  . SER   C 1 105 ? 6.053   -4.673  25.108  1.00 55.18  ? 420 SER   C CA  1 
ATOM   2496 C  C   . SER   C 1 105 ? 5.842   -3.270  25.679  1.00 55.49  ? 420 SER   C C   1 
ATOM   2497 O  O   . SER   C 1 105 ? 4.784   -2.992  26.241  1.00 56.00  ? 420 SER   C O   1 
ATOM   2498 C  CB  . SER   C 1 105 ? 5.610   -5.725  26.091  1.00 55.64  ? 420 SER   C CB  1 
ATOM   2499 O  OG  . SER   C 1 105 ? 6.374   -5.652  27.287  1.00 56.31  ? 420 SER   C OG  1 
ATOM   2500 N  N   . ALA   C 1 106 ? 6.846   -2.393  25.541  1.00 55.41  ? 421 ALA   C N   1 
ATOM   2501 C  CA  . ALA   C 1 106 ? 6.732   -1.009  25.969  1.00 55.75  ? 421 ALA   C CA  1 
ATOM   2502 C  C   . ALA   C 1 106 ? 6.689   -0.065  24.767  1.00 57.34  ? 421 ALA   C C   1 
ATOM   2503 O  O   . ALA   C 1 106 ? 6.626   1.150   24.946  1.00 58.15  ? 421 ALA   C O   1 
ATOM   2504 C  CB  . ALA   C 1 106 ? 7.886   -0.668  26.886  1.00 55.15  ? 421 ALA   C CB  1 
ATOM   2505 N  N   . LEU   C 1 107 ? 6.697   -0.623  23.548  1.00 58.13  ? 422 LEU   C N   1 
ATOM   2506 C  CA  . LEU   C 1 107 ? 6.878   0.170   22.342  1.00 59.15  ? 422 LEU   C CA  1 
ATOM   2507 C  C   . LEU   C 1 107 ? 5.743   -0.089  21.355  1.00 60.69  ? 422 LEU   C C   1 
ATOM   2508 O  O   . LEU   C 1 107 ? 4.981   -1.040  21.512  1.00 60.56  ? 422 LEU   C O   1 
ATOM   2509 C  CB  . LEU   C 1 107 ? 8.240   -0.158  21.730  1.00 59.19  ? 422 LEU   C CB  1 
ATOM   2510 C  CG  . LEU   C 1 107 ? 9.465   0.249   22.557  1.00 58.21  ? 422 LEU   C CG  1 
ATOM   2511 C  CD1 . LEU   C 1 107 ? 10.733  -0.327  21.953  1.00 57.49  ? 422 LEU   C CD1 1 
ATOM   2512 C  CD2 . LEU   C 1 107 ? 9.577   1.760   22.683  1.00 57.51  ? 422 LEU   C CD2 1 
ATOM   2513 N  N   . LEU   C 1 108 ? 5.655   0.777   20.337  1.00 63.85  ? 423 LEU   C N   1 
ATOM   2514 C  CA  . LEU   C 1 108 ? 4.639   0.694   19.299  1.00 66.73  ? 423 LEU   C CA  1 
ATOM   2515 C  C   . LEU   C 1 108 ? 5.184   0.995   17.905  1.00 70.08  ? 423 LEU   C C   1 
ATOM   2516 O  O   . LEU   C 1 108 ? 5.786   2.046   17.696  1.00 71.51  ? 423 LEU   C O   1 
ATOM   2517 C  CB  . LEU   C 1 108 ? 3.494   1.645   19.642  1.00 66.06  ? 423 LEU   C CB  1 
ATOM   2518 C  CG  . LEU   C 1 108 ? 2.485   1.149   20.682  1.00 65.33  ? 423 LEU   C CG  1 
ATOM   2519 C  CD1 . LEU   C 1 108 ? 1.450   2.227   20.947  1.00 65.70  ? 423 LEU   C CD1 1 
ATOM   2520 C  CD2 . LEU   C 1 108 ? 1.806   -0.139  20.248  1.00 64.60  ? 423 LEU   C CD2 1 
ATOM   2521 N  N   . PRO   C 1 109 ? 4.986   0.105   16.904  1.00 74.81  ? 424 PRO   C N   1 
ATOM   2522 C  CA  . PRO   C 1 109 ? 4.307   -1.172  17.103  1.00 79.00  ? 424 PRO   C CA  1 
ATOM   2523 C  C   . PRO   C 1 109 ? 5.136   -2.178  17.896  1.00 84.53  ? 424 PRO   C C   1 
ATOM   2524 O  O   . PRO   C 1 109 ? 6.363   -2.093  17.916  1.00 87.25  ? 424 PRO   C O   1 
ATOM   2525 C  CB  . PRO   C 1 109 ? 4.063   -1.664  15.679  1.00 78.30  ? 424 PRO   C CB  1 
ATOM   2526 C  CG  . PRO   C 1 109 ? 5.239   -1.067  14.925  1.00 76.84  ? 424 PRO   C CG  1 
ATOM   2527 C  CD  . PRO   C 1 109 ? 5.415   0.299   15.510  1.00 75.34  ? 424 PRO   C CD  1 
ATOM   2528 N  N   . THR   C 1 110 ? 4.451   -3.122  18.553  1.00 88.64  ? 425 THR   C N   1 
ATOM   2529 C  CA  . THR   C 1 110 ? 5.118   -4.215  19.243  1.00 91.29  ? 425 THR   C CA  1 
ATOM   2530 C  C   . THR   C 1 110 ? 5.606   -5.215  18.198  1.00 91.67  ? 425 THR   C C   1 
ATOM   2531 O  O   . THR   C 1 110 ? 4.965   -5.405  17.165  1.00 90.85  ? 425 THR   C O   1 
ATOM   2532 C  CB  . THR   C 1 110 ? 4.179   -4.861  20.264  1.00 93.23  ? 425 THR   C CB  1 
ATOM   2533 O  OG1 . THR   C 1 110 ? 3.854   -3.831  21.192  1.00 93.71  ? 425 THR   C OG1 1 
ATOM   2534 C  CG2 . THR   C 1 110 ? 4.822   -6.020  21.006  1.00 93.28  ? 425 THR   C CG2 1 
ATOM   2535 N  N   . ILE   C 1 111 ? 6.748   -5.847  18.492  1.00 92.44  ? 426 ILE   C N   1 
ATOM   2536 C  CA  . ILE   C 1 111 ? 7.433   -6.717  17.550  1.00 92.79  ? 426 ILE   C CA  1 
ATOM   2537 C  C   . ILE   C 1 111 ? 8.175   -7.816  18.333  1.00 92.73  ? 426 ILE   C C   1 
ATOM   2538 O  O   . ILE   C 1 111 ? 8.243   -7.691  19.578  1.00 91.36  ? 426 ILE   C O   1 
ATOM   2539 C  CB  . ILE   C 1 111 ? 8.383   -5.898  16.654  1.00 92.45  ? 426 ILE   C CB  1 
ATOM   2540 C  CG1 . ILE   C 1 111 ? 9.120   -4.818  17.457  1.00 91.60  ? 426 ILE   C CG1 1 
ATOM   2541 C  CG2 . ILE   C 1 111 ? 7.633   -5.297  15.463  1.00 91.91  ? 426 ILE   C CG2 1 
ATOM   2542 C  CD1 . ILE   C 1 111 ? 10.260  -4.146  16.712  1.00 91.03  ? 426 ILE   C CD1 1 
ATOM   2543 O  OXT . ILE   C 1 111 ? 8.653   -8.764  17.671  1.00 92.61  ? 426 ILE   C OXT 1 
ATOM   2544 N  N   . SER   D 1 3   ? -0.309  -32.713 23.780  1.00 98.89  ? 318 SER   D N   1 
ATOM   2545 C  CA  . SER   D 1 3   ? 0.975   -33.289 23.299  1.00 98.64  ? 318 SER   D CA  1 
ATOM   2546 C  C   . SER   D 1 3   ? 2.137   -32.375 23.686  1.00 98.95  ? 318 SER   D C   1 
ATOM   2547 O  O   . SER   D 1 3   ? 2.324   -31.312 23.094  1.00 98.19  ? 318 SER   D O   1 
ATOM   2548 C  CB  . SER   D 1 3   ? 0.943   -33.535 21.807  1.00 96.71  ? 318 SER   D CB  1 
ATOM   2549 O  OG  . SER   D 1 3   ? 2.076   -34.282 21.388  1.00 93.93  ? 318 SER   D OG  1 
ATOM   2550 N  N   . THR   D 1 4   ? 2.902   -32.800 24.699  1.00 95.94  ? 319 THR   D N   1 
ATOM   2551 C  CA  . THR   D 1 4   ? 4.162   -32.166 25.049  1.00 91.89  ? 319 THR   D CA  1 
ATOM   2552 C  C   . THR   D 1 4   ? 5.264   -32.805 24.206  1.00 88.06  ? 319 THR   D C   1 
ATOM   2553 O  O   . THR   D 1 4   ? 6.180   -33.415 24.749  1.00 89.95  ? 319 THR   D O   1 
ATOM   2554 C  CB  . THR   D 1 4   ? 4.428   -32.327 26.548  1.00 91.42  ? 319 THR   D CB  1 
ATOM   2555 O  OG1 . THR   D 1 4   ? 4.419   -33.726 26.820  1.00 91.23  ? 319 THR   D OG1 1 
ATOM   2556 C  CG2 . THR   D 1 4   ? 3.385   -31.654 27.421  1.00 90.71  ? 319 THR   D CG2 1 
ATOM   2557 N  N   . SER   D 1 5   ? 5.163   -32.675 22.877  1.00 81.58  ? 320 SER   D N   1 
ATOM   2558 C  CA  . SER   D 1 5   ? 5.995   -33.457 21.976  1.00 78.42  ? 320 SER   D CA  1 
ATOM   2559 C  C   . SER   D 1 5   ? 6.373   -32.642 20.741  1.00 75.28  ? 320 SER   D C   1 
ATOM   2560 O  O   . SER   D 1 5   ? 5.532   -31.958 20.163  1.00 76.48  ? 320 SER   D O   1 
ATOM   2561 C  CB  . SER   D 1 5   ? 5.300   -34.735 21.588  1.00 77.74  ? 320 SER   D CB  1 
ATOM   2562 O  OG  . SER   D 1 5   ? 6.174   -35.586 20.860  1.00 78.70  ? 320 SER   D OG  1 
ATOM   2563 N  N   . LEU   D 1 6   ? 7.647   -32.751 20.340  1.00 71.25  ? 321 LEU   D N   1 
ATOM   2564 C  CA  . LEU   D 1 6   ? 8.181   -32.026 19.197  1.00 68.25  ? 321 LEU   D CA  1 
ATOM   2565 C  C   . LEU   D 1 6   ? 8.815   -33.013 18.222  1.00 65.90  ? 321 LEU   D C   1 
ATOM   2566 O  O   . LEU   D 1 6   ? 9.623   -33.847 18.623  1.00 63.82  ? 321 LEU   D O   1 
ATOM   2567 C  CB  . LEU   D 1 6   ? 9.192   -30.986 19.678  1.00 68.16  ? 321 LEU   D CB  1 
ATOM   2568 C  CG  . LEU   D 1 6   ? 8.612   -29.776 20.417  1.00 68.48  ? 321 LEU   D CG  1 
ATOM   2569 C  CD1 . LEU   D 1 6   ? 9.725   -28.917 20.987  1.00 68.52  ? 321 LEU   D CD1 1 
ATOM   2570 C  CD2 . LEU   D 1 6   ? 7.717   -28.944 19.512  1.00 68.74  ? 321 LEU   D CD2 1 
ATOM   2571 N  N   . SER   D 1 7   ? 8.455   -32.881 16.937  1.00 66.23  ? 322 SER   D N   1 
ATOM   2572 C  CA  . SER   D 1 7   ? 8.794   -33.865 15.921  1.00 66.64  ? 322 SER   D CA  1 
ATOM   2573 C  C   . SER   D 1 7   ? 9.618   -33.230 14.804  1.00 66.87  ? 322 SER   D C   1 
ATOM   2574 O  O   . SER   D 1 7   ? 9.595   -32.015 14.629  1.00 69.99  ? 322 SER   D O   1 
ATOM   2575 C  CB  . SER   D 1 7   ? 7.549   -34.500 15.358  1.00 66.33  ? 322 SER   D CB  1 
ATOM   2576 O  OG  . SER   D 1 7   ? 6.796   -35.140 16.377  1.00 66.51  ? 322 SER   D OG  1 
ATOM   2577 N  N   . CYS   D 1 8   ? 10.333  -34.074 14.049  1.00 65.24  ? 323 CYS   D N   1 
ATOM   2578 C  CA  . CYS   D 1 8   ? 11.065  -33.643 12.867  1.00 64.21  ? 323 CYS   D CA  1 
ATOM   2579 C  C   . CYS   D 1 8   ? 10.073  -33.157 11.815  1.00 63.65  ? 323 CYS   D C   1 
ATOM   2580 O  O   . CYS   D 1 8   ? 9.197   -33.909 11.404  1.00 62.18  ? 323 CYS   D O   1 
ATOM   2581 C  CB  . CYS   D 1 8   ? 11.911  -34.779 12.302  1.00 63.89  ? 323 CYS   D CB  1 
ATOM   2582 S  SG  . CYS   D 1 8   ? 12.703  -34.392 10.717  1.00 62.89  ? 323 CYS   D SG  1 
ATOM   2583 N  N   . LYS   D 1 9   ? 10.224  -31.901 11.382  1.00 64.76  ? 324 LYS   D N   1 
ATOM   2584 C  CA  . LYS   D 1 9   ? 9.287   -31.295 10.450  1.00 66.49  ? 324 LYS   D CA  1 
ATOM   2585 C  C   . LYS   D 1 9   ? 9.267   -32.073 9.136   1.00 68.83  ? 324 LYS   D C   1 
ATOM   2586 O  O   . LYS   D 1 9   ? 8.211   -32.220 8.527   1.00 69.34  ? 324 LYS   D O   1 
ATOM   2587 C  CB  . LYS   D 1 9   ? 9.620   -29.819 10.200  1.00 67.17  ? 324 LYS   D CB  1 
ATOM   2588 C  CG  . LYS   D 1 9   ? 8.752   -29.130 9.149   1.00 68.26  ? 324 LYS   D CG  1 
ATOM   2589 C  CD  . LYS   D 1 9   ? 8.855   -27.609 9.129   1.00 69.68  ? 324 LYS   D CD  1 
ATOM   2590 C  CE  . LYS   D 1 9   ? 8.104   -26.961 10.250  1.00 70.33  ? 324 LYS   D CE  1 
ATOM   2591 N  NZ  . LYS   D 1 9   ? 8.425   -25.537 10.379  1.00 70.50  ? 324 LYS   D NZ  1 
ATOM   2592 N  N   . GLN   D 1 10  ? 10.436  -32.569 8.710   1.00 72.04  ? 325 GLN   D N   1 
ATOM   2593 C  CA  . GLN   D 1 10  ? 10.577  -33.177 7.397   1.00 73.43  ? 325 GLN   D CA  1 
ATOM   2594 C  C   . GLN   D 1 10  ? 9.798   -34.491 7.348   1.00 72.60  ? 325 GLN   D C   1 
ATOM   2595 O  O   . GLN   D 1 10  ? 8.876   -34.627 6.547   1.00 74.26  ? 325 GLN   D O   1 
ATOM   2596 C  CB  . GLN   D 1 10  ? 12.049  -33.374 7.029   1.00 75.40  ? 325 GLN   D CB  1 
ATOM   2597 C  CG  . GLN   D 1 10  ? 12.293  -33.492 5.528   1.00 77.65  ? 325 GLN   D CG  1 
ATOM   2598 C  CD  . GLN   D 1 10  ? 13.687  -33.972 5.182   1.00 80.48  ? 325 GLN   D CD  1 
ATOM   2599 O  OE1 . GLN   D 1 10  ? 14.682  -33.268 5.387   1.00 81.03  ? 325 GLN   D OE1 1 
ATOM   2600 N  NE2 . GLN   D 1 10  ? 13.773  -35.176 4.634   1.00 81.75  ? 325 GLN   D NE2 1 
ATOM   2601 N  N   . CYS   D 1 11  ? 10.164  -35.445 8.215   1.00 70.90  ? 326 CYS   D N   1 
ATOM   2602 C  CA  . CYS   D 1 11  ? 9.606   -36.789 8.160   1.00 70.30  ? 326 CYS   D CA  1 
ATOM   2603 C  C   . CYS   D 1 11  ? 8.394   -36.920 9.085   1.00 73.79  ? 326 CYS   D C   1 
ATOM   2604 O  O   . CYS   D 1 11  ? 7.536   -37.765 8.844   1.00 74.46  ? 326 CYS   D O   1 
ATOM   2605 C  CB  . CYS   D 1 11  ? 10.667  -37.841 8.459   1.00 68.41  ? 326 CYS   D CB  1 
ATOM   2606 S  SG  . CYS   D 1 11  ? 11.353  -37.734 10.130  1.00 67.13  ? 326 CYS   D SG  1 
ATOM   2607 N  N   . GLN   D 1 12  ? 8.356   -36.120 10.160  1.00 77.71  ? 327 GLN   D N   1 
ATOM   2608 C  CA  . GLN   D 1 12  ? 7.137   -35.839 10.914  1.00 81.19  ? 327 GLN   D CA  1 
ATOM   2609 C  C   . GLN   D 1 12  ? 6.859   -36.889 11.992  1.00 84.00  ? 327 GLN   D C   1 
ATOM   2610 O  O   . GLN   D 1 12  ? 6.230   -36.571 12.999  1.00 85.67  ? 327 GLN   D O   1 
ATOM   2611 C  CB  . GLN   D 1 12  ? 5.902   -35.676 10.025  1.00 81.44  ? 327 GLN   D CB  1 
ATOM   2612 C  CG  . GLN   D 1 12  ? 6.063   -34.627 8.931   1.00 82.18  ? 327 GLN   D CG  1 
ATOM   2613 C  CD  . GLN   D 1 12  ? 4.754   -34.251 8.274   1.00 82.81  ? 327 GLN   D CD  1 
ATOM   2614 O  OE1 . GLN   D 1 12  ? 4.495   -34.589 7.114   1.00 82.98  ? 327 GLN   D OE1 1 
ATOM   2615 N  NE2 . GLN   D 1 12  ? 3.911   -33.551 9.020   1.00 82.57  ? 327 GLN   D NE2 1 
ATOM   2616 N  N   . GLU   D 1 13  ? 7.320   -38.128 11.788  1.00 85.96  ? 328 GLU   D N   1 
ATOM   2617 C  CA  . GLU   D 1 13  ? 6.945   -39.243 12.647  1.00 87.51  ? 328 GLU   D CA  1 
ATOM   2618 C  C   . GLU   D 1 13  ? 7.826   -39.307 13.896  1.00 84.79  ? 328 GLU   D C   1 
ATOM   2619 O  O   . GLU   D 1 13  ? 7.455   -39.951 14.875  1.00 84.73  ? 328 GLU   D O   1 
ATOM   2620 C  CB  . GLU   D 1 13  ? 7.045   -40.544 11.851  1.00 90.14  ? 328 GLU   D CB  1 
ATOM   2621 C  CG  . GLU   D 1 13  ? 8.480   -40.958 11.534  1.00 91.89  ? 328 GLU   D CG  1 
ATOM   2622 C  CD  . GLU   D 1 13  ? 8.639   -41.848 10.314  1.00 95.78  ? 328 GLU   D CD  1 
ATOM   2623 O  OE1 . GLU   D 1 13  ? 7.633   -42.149 9.638   1.00 98.67  ? 328 GLU   D OE1 1 
ATOM   2624 O  OE2 . GLU   D 1 13  ? 9.791   -42.241 10.037  1.00 98.97  ? 328 GLU   D OE2 1 
ATOM   2625 N  N   . THR   D 1 14  ? 8.983   -38.634 13.854  1.00 81.06  ? 329 THR   D N   1 
ATOM   2626 C  CA  . THR   D 1 14  ? 10.047  -38.843 14.823  1.00 76.83  ? 329 THR   D CA  1 
ATOM   2627 C  C   . THR   D 1 14  ? 9.967   -37.790 15.926  1.00 73.24  ? 329 THR   D C   1 
ATOM   2628 O  O   . THR   D 1 14  ? 10.135  -36.605 15.655  1.00 72.97  ? 329 THR   D O   1 
ATOM   2629 C  CB  . THR   D 1 14  ? 11.385  -38.779 14.089  1.00 76.67  ? 329 THR   D CB  1 
ATOM   2630 O  OG1 . THR   D 1 14  ? 11.308  -39.784 13.082  1.00 76.45  ? 329 THR   D OG1 1 
ATOM   2631 C  CG2 . THR   D 1 14  ? 12.573  -39.035 15.000  1.00 76.43  ? 329 THR   D CG2 1 
ATOM   2632 N  N   . GLU   D 1 15  ? 9.734   -38.244 17.165  1.00 69.81  ? 330 GLU   D N   1 
ATOM   2633 C  CA  . GLU   D 1 15  ? 9.782   -37.382 18.336  1.00 68.14  ? 330 GLU   D CA  1 
ATOM   2634 C  C   . GLU   D 1 15  ? 11.241  -37.105 18.689  1.00 65.61  ? 330 GLU   D C   1 
ATOM   2635 O  O   . GLU   D 1 15  ? 12.012  -38.039 18.897  1.00 65.23  ? 330 GLU   D O   1 
ATOM   2636 C  CB  . GLU   D 1 15  ? 9.068   -38.029 19.524  1.00 69.81  ? 330 GLU   D CB  1 
ATOM   2637 C  CG  . GLU   D 1 15  ? 9.278   -37.292 20.845  1.00 71.36  ? 330 GLU   D CG  1 
ATOM   2638 C  CD  . GLU   D 1 15  ? 8.464   -37.844 22.000  1.00 73.26  ? 330 GLU   D CD  1 
ATOM   2639 O  OE1 . GLU   D 1 15  ? 7.220   -37.819 21.905  1.00 74.48  ? 330 GLU   D OE1 1 
ATOM   2640 O  OE2 . GLU   D 1 15  ? 9.072   -38.299 22.992  1.00 75.41  ? 330 GLU   D OE2 1 
ATOM   2641 N  N   . ILE   D 1 16  ? 11.599  -35.818 18.768  1.00 63.82  ? 331 ILE   D N   1 
ATOM   2642 C  CA  . ILE   D 1 16  ? 12.952  -35.408 19.107  1.00 63.11  ? 331 ILE   D CA  1 
ATOM   2643 C  C   . ILE   D 1 16  ? 13.018  -35.136 20.608  1.00 63.21  ? 331 ILE   D C   1 
ATOM   2644 O  O   . ILE   D 1 16  ? 13.794  -35.774 21.318  1.00 63.66  ? 331 ILE   D O   1 
ATOM   2645 C  CB  . ILE   D 1 16  ? 13.391  -34.182 18.280  1.00 62.52  ? 331 ILE   D CB  1 
ATOM   2646 C  CG1 . ILE   D 1 16  ? 13.093  -34.353 16.784  1.00 62.24  ? 331 ILE   D CG1 1 
ATOM   2647 C  CG2 . ILE   D 1 16  ? 14.866  -33.859 18.526  1.00 62.01  ? 331 ILE   D CG2 1 
ATOM   2648 C  CD1 . ILE   D 1 16  ? 13.842  -35.493 16.117  1.00 62.06  ? 331 ILE   D CD1 1 
ATOM   2649 N  N   . THR   D 1 17  ? 12.191  -34.190 21.077  1.00 62.33  ? 332 THR   D N   1 
ATOM   2650 C  CA  . THR   D 1 17  ? 12.166  -33.800 22.479  1.00 62.71  ? 332 THR   D CA  1 
ATOM   2651 C  C   . THR   D 1 17  ? 10.726  -33.525 22.911  1.00 62.66  ? 332 THR   D C   1 
ATOM   2652 O  O   . THR   D 1 17  ? 9.798   -33.636 22.111  1.00 61.51  ? 332 THR   D O   1 
ATOM   2653 C  CB  . THR   D 1 17  ? 13.062  -32.578 22.687  1.00 62.58  ? 332 THR   D CB  1 
ATOM   2654 O  OG1 . THR   D 1 17  ? 13.165  -32.394 24.096  1.00 62.53  ? 332 THR   D OG1 1 
ATOM   2655 C  CG2 . THR   D 1 17  ? 12.507  -31.317 22.049  1.00 62.97  ? 332 THR   D CG2 1 
ATOM   2656 N  N   . THR   D 1 18  ? 10.571  -33.168 24.194  1.00 62.75  ? 333 THR   D N   1 
ATOM   2657 C  CA  . THR   D 1 18  ? 9.291   -32.782 24.768  1.00 61.95  ? 333 THR   D CA  1 
ATOM   2658 C  C   . THR   D 1 18  ? 9.408   -31.366 25.329  1.00 61.19  ? 333 THR   D C   1 
ATOM   2659 O  O   . THR   D 1 18  ? 10.500  -30.914 25.667  1.00 59.53  ? 333 THR   D O   1 
ATOM   2660 C  CB  . THR   D 1 18  ? 8.880   -33.792 25.842  1.00 61.31  ? 333 THR   D CB  1 
ATOM   2661 O  OG1 . THR   D 1 18  ? 9.887   -33.750 26.846  1.00 61.87  ? 333 THR   D OG1 1 
ATOM   2662 C  CG2 . THR   D 1 18  ? 8.761   -35.207 25.303  1.00 60.64  ? 333 THR   D CG2 1 
ATOM   2663 N  N   . LYS   D 1 19  ? 8.262   -30.682 25.429  1.00 62.70  ? 334 LYS   D N   1 
ATOM   2664 C  CA  . LYS   D 1 19  ? 8.195   -29.288 25.845  1.00 64.70  ? 334 LYS   D CA  1 
ATOM   2665 C  C   . LYS   D 1 19  ? 8.767   -29.090 27.248  1.00 63.75  ? 334 LYS   D C   1 
ATOM   2666 O  O   . LYS   D 1 19  ? 9.334   -28.039 27.534  1.00 62.53  ? 334 LYS   D O   1 
ATOM   2667 C  CB  . LYS   D 1 19  ? 6.741   -28.801 25.805  1.00 68.17  ? 334 LYS   D CB  1 
ATOM   2668 C  CG  . LYS   D 1 19  ? 6.266   -28.225 24.472  1.00 70.78  ? 334 LYS   D CG  1 
ATOM   2669 C  CD  . LYS   D 1 19  ? 4.822   -28.535 24.080  1.00 74.33  ? 334 LYS   D CD  1 
ATOM   2670 C  CE  . LYS   D 1 19  ? 3.795   -28.498 25.183  1.00 77.78  ? 334 LYS   D CE  1 
ATOM   2671 N  NZ  . LYS   D 1 19  ? 3.576   -27.169 25.762  1.00 78.71  ? 334 LYS   D NZ  1 
ATOM   2672 N  N   . ASN   D 1 20  ? 8.618   -30.095 28.120  1.00 64.01  ? 335 ASN   D N   1 
ATOM   2673 C  CA  . ASN   D 1 20  ? 9.036   -29.968 29.510  1.00 64.70  ? 335 ASN   D CA  1 
ATOM   2674 C  C   . ASN   D 1 20  ? 10.512  -30.339 29.669  1.00 62.30  ? 335 ASN   D C   1 
ATOM   2675 O  O   . ASN   D 1 20  ? 10.967  -30.572 30.787  1.00 62.40  ? 335 ASN   D O   1 
ATOM   2676 C  CB  . ASN   D 1 20  ? 8.100   -30.721 30.455  1.00 67.28  ? 335 ASN   D CB  1 
ATOM   2677 C  CG  . ASN   D 1 20  ? 7.502   -31.960 29.831  1.00 70.34  ? 335 ASN   D CG  1 
ATOM   2678 O  OD1 . ASN   D 1 20  ? 6.732   -31.856 28.869  1.00 72.45  ? 335 ASN   D OD1 1 
ATOM   2679 N  ND2 . ASN   D 1 20  ? 7.823   -33.130 30.362  1.00 72.35  ? 335 ASN   D ND2 1 
ATOM   2680 N  N   . GLU   D 1 21  ? 11.255  -30.374 28.553  1.00 60.64  ? 336 GLU   D N   1 
ATOM   2681 C  CA  . GLU   D 1 21  ? 12.708  -30.441 28.579  1.00 58.63  ? 336 GLU   D CA  1 
ATOM   2682 C  C   . GLU   D 1 21  ? 13.312  -29.082 28.222  1.00 55.55  ? 336 GLU   D C   1 
ATOM   2683 O  O   . GLU   D 1 21  ? 14.533  -28.942 28.199  1.00 55.05  ? 336 GLU   D O   1 
ATOM   2684 C  CB  . GLU   D 1 21  ? 13.216  -31.511 27.612  1.00 60.24  ? 336 GLU   D CB  1 
ATOM   2685 C  CG  . GLU   D 1 21  ? 12.817  -32.929 28.007  1.00 62.40  ? 336 GLU   D CG  1 
ATOM   2686 C  CD  . GLU   D 1 21  ? 13.480  -33.468 29.263  1.00 64.96  ? 336 GLU   D CD  1 
ATOM   2687 O  OE1 . GLU   D 1 21  ? 14.330  -32.769 29.858  1.00 66.11  ? 336 GLU   D OE1 1 
ATOM   2688 O  OE2 . GLU   D 1 21  ? 13.136  -34.605 29.650  1.00 67.07  ? 336 GLU   D OE2 1 
ATOM   2689 N  N   . ILE   D 1 22  ? 12.455  -28.089 27.946  1.00 51.87  ? 337 ILE   D N   1 
ATOM   2690 C  CA  . ILE   D 1 22  ? 12.896  -26.733 27.658  1.00 48.73  ? 337 ILE   D CA  1 
ATOM   2691 C  C   . ILE   D 1 22  ? 13.480  -26.130 28.931  1.00 47.74  ? 337 ILE   D C   1 
ATOM   2692 O  O   . ILE   D 1 22  ? 12.994  -26.407 30.026  1.00 47.64  ? 337 ILE   D O   1 
ATOM   2693 C  CB  . ILE   D 1 22  ? 11.734  -25.878 27.116  1.00 47.96  ? 337 ILE   D CB  1 
ATOM   2694 C  CG1 . ILE   D 1 22  ? 11.232  -26.392 25.766  1.00 47.64  ? 337 ILE   D CG1 1 
ATOM   2695 C  CG2 . ILE   D 1 22  ? 12.128  -24.401 27.040  1.00 48.48  ? 337 ILE   D CG2 1 
ATOM   2696 C  CD1 . ILE   D 1 22  ? 9.908   -25.794 25.324  1.00 47.03  ? 337 ILE   D CD1 1 
ATOM   2697 N  N   . PHE   D 1 23  ? 14.510  -25.290 28.774  1.00 47.19  ? 338 PHE   D N   1 
ATOM   2698 C  CA  . PHE   D 1 23  ? 15.116  -24.612 29.907  1.00 46.37  ? 338 PHE   D CA  1 
ATOM   2699 C  C   . PHE   D 1 23  ? 15.843  -23.352 29.442  1.00 46.16  ? 338 PHE   D C   1 
ATOM   2700 O  O   . PHE   D 1 23  ? 16.095  -23.170 28.254  1.00 44.68  ? 338 PHE   D O   1 
ATOM   2701 C  CB  . PHE   D 1 23  ? 16.069  -25.570 30.628  1.00 45.89  ? 338 PHE   D CB  1 
ATOM   2702 C  CG  . PHE   D 1 23  ? 17.443  -25.679 29.983  1.00 46.59  ? 338 PHE   D CG  1 
ATOM   2703 C  CD1 . PHE   D 1 23  ? 17.613  -26.340 28.771  1.00 47.17  ? 338 PHE   D CD1 1 
ATOM   2704 C  CD2 . PHE   D 1 23  ? 18.561  -25.120 30.592  1.00 47.38  ? 338 PHE   D CD2 1 
ATOM   2705 C  CE1 . PHE   D 1 23  ? 18.866  -26.430 28.185  1.00 47.73  ? 338 PHE   D CE1 1 
ATOM   2706 C  CE2 . PHE   D 1 23  ? 19.811  -25.215 30.002  1.00 47.59  ? 338 PHE   D CE2 1 
ATOM   2707 C  CZ  . PHE   D 1 23  ? 19.962  -25.870 28.802  1.00 47.73  ? 338 PHE   D CZ  1 
ATOM   2708 N  N   . SER   D 1 24  ? 16.172  -22.499 30.420  1.00 47.86  ? 339 SER   D N   1 
ATOM   2709 C  CA  . SER   D 1 24  ? 16.970  -21.301 30.219  1.00 49.96  ? 339 SER   D CA  1 
ATOM   2710 C  C   . SER   D 1 24  ? 18.417  -21.573 30.623  1.00 51.54  ? 339 SER   D C   1 
ATOM   2711 O  O   . SER   D 1 24  ? 18.670  -22.027 31.736  1.00 51.98  ? 339 SER   D O   1 
ATOM   2712 C  CB  . SER   D 1 24  ? 16.394  -20.149 31.011  1.00 50.69  ? 339 SER   D CB  1 
ATOM   2713 O  OG  . SER   D 1 24  ? 17.358  -19.130 31.239  1.00 51.97  ? 339 SER   D OG  1 
ATOM   2714 N  N   . LEU   D 1 25  ? 19.363  -21.285 29.720  1.00 53.45  ? 340 LEU   D N   1 
ATOM   2715 C  CA  . LEU   D 1 25  ? 20.777  -21.353 30.054  1.00 54.73  ? 340 LEU   D CA  1 
ATOM   2716 C  C   . LEU   D 1 25  ? 21.221  -19.998 30.602  1.00 56.41  ? 340 LEU   D C   1 
ATOM   2717 O  O   . LEU   D 1 25  ? 20.905  -18.962 30.021  1.00 56.54  ? 340 LEU   D O   1 
ATOM   2718 C  CB  . LEU   D 1 25  ? 21.622  -21.750 28.846  1.00 54.26  ? 340 LEU   D CB  1 
ATOM   2719 C  CG  . LEU   D 1 25  ? 23.047  -22.211 29.173  1.00 54.20  ? 340 LEU   D CG  1 
ATOM   2720 C  CD1 . LEU   D 1 25  ? 23.139  -23.727 29.227  1.00 54.00  ? 340 LEU   D CD1 1 
ATOM   2721 C  CD2 . LEU   D 1 25  ? 24.065  -21.648 28.201  1.00 55.14  ? 340 LEU   D CD2 1 
ATOM   2722 N  N   . SER   D 1 26  ? 21.978  -20.032 31.708  1.00 58.18  ? 341 SER   D N   1 
ATOM   2723 C  CA  . SER   D 1 26  ? 22.400  -18.844 32.437  1.00 59.57  ? 341 SER   D CA  1 
ATOM   2724 C  C   . SER   D 1 26  ? 21.265  -17.819 32.489  1.00 60.89  ? 341 SER   D C   1 
ATOM   2725 O  O   . SER   D 1 26  ? 20.240  -18.081 33.116  1.00 63.14  ? 341 SER   D O   1 
ATOM   2726 C  CB  . SER   D 1 26  ? 23.684  -18.275 31.873  1.00 59.70  ? 341 SER   D CB  1 
ATOM   2727 O  OG  . SER   D 1 26  ? 23.474  -17.656 30.612  1.00 61.00  ? 341 SER   D OG  1 
ATOM   2728 N  N   . LEU   D 1 27  ? 21.441  -16.666 31.824  1.00 60.48  ? 342 LEU   D N   1 
ATOM   2729 C  CA  . LEU   D 1 27  ? 20.480  -15.574 31.903  1.00 60.21  ? 342 LEU   D CA  1 
ATOM   2730 C  C   . LEU   D 1 27  ? 19.729  -15.405 30.582  1.00 59.52  ? 342 LEU   D C   1 
ATOM   2731 O  O   . LEU   D 1 27  ? 18.927  -14.482 30.454  1.00 59.38  ? 342 LEU   D O   1 
ATOM   2732 C  CB  . LEU   D 1 27  ? 21.170  -14.266 32.295  1.00 60.68  ? 342 LEU   D CB  1 
ATOM   2733 C  CG  . LEU   D 1 27  ? 21.827  -14.210 33.680  1.00 60.64  ? 342 LEU   D CG  1 
ATOM   2734 C  CD1 . LEU   D 1 27  ? 20.964  -14.871 34.741  1.00 60.29  ? 342 LEU   D CD1 1 
ATOM   2735 C  CD2 . LEU   D 1 27  ? 23.222  -14.816 33.668  1.00 61.72  ? 342 LEU   D CD2 1 
ATOM   2736 N  N   . SER   D 1 28  ? 19.982  -16.285 29.605  1.00 58.03  ? 343 SER   D N   1 
ATOM   2737 C  CA  . SER   D 1 28  ? 19.292  -16.213 28.327  1.00 57.76  ? 343 SER   D CA  1 
ATOM   2738 C  C   . SER   D 1 28  ? 17.997  -17.017 28.404  1.00 56.10  ? 343 SER   D C   1 
ATOM   2739 O  O   . SER   D 1 28  ? 17.955  -18.063 29.045  1.00 55.72  ? 343 SER   D O   1 
ATOM   2740 C  CB  . SER   D 1 28  ? 20.170  -16.687 27.194  1.00 58.36  ? 343 SER   D CB  1 
ATOM   2741 O  OG  . SER   D 1 28  ? 20.326  -18.099 27.219  1.00 60.69  ? 343 SER   D OG  1 
ATOM   2742 N  N   . GLY   D 1 29  ? 16.947  -16.514 27.744  1.00 55.71  ? 344 GLY   D N   1 
ATOM   2743 C  CA  . GLY   D 1 29  ? 15.661  -17.191 27.702  1.00 55.72  ? 344 GLY   D CA  1 
ATOM   2744 C  C   . GLY   D 1 29  ? 15.736  -18.482 26.890  1.00 55.76  ? 344 GLY   D C   1 
ATOM   2745 O  O   . GLY   D 1 29  ? 16.760  -18.776 26.276  1.00 56.06  ? 344 GLY   D O   1 
ATOM   2746 N  N   . PRO   D 1 30  ? 14.648  -19.284 26.848  1.00 55.84  ? 345 PRO   D N   1 
ATOM   2747 C  CA  . PRO   D 1 30  ? 14.680  -20.582 26.186  1.00 56.11  ? 345 PRO   D CA  1 
ATOM   2748 C  C   . PRO   D 1 30  ? 14.745  -20.479 24.664  1.00 56.34  ? 345 PRO   D C   1 
ATOM   2749 O  O   . PRO   D 1 30  ? 15.379  -21.308 24.016  1.00 54.79  ? 345 PRO   D O   1 
ATOM   2750 C  CB  . PRO   D 1 30  ? 13.395  -21.249 26.666  1.00 55.86  ? 345 PRO   D CB  1 
ATOM   2751 C  CG  . PRO   D 1 30  ? 12.463  -20.068 26.878  1.00 55.93  ? 345 PRO   D CG  1 
ATOM   2752 C  CD  . PRO   D 1 30  ? 13.325  -18.959 27.405  1.00 55.99  ? 345 PRO   D CD  1 
ATOM   2753 N  N   . MET   D 1 31  ? 14.088  -19.448 24.118  1.00 58.21  ? 346 MET   D N   1 
ATOM   2754 C  CA  . MET   D 1 31  ? 13.985  -19.248 22.682  1.00 60.43  ? 346 MET   D CA  1 
ATOM   2755 C  C   . MET   D 1 31  ? 14.809  -18.030 22.280  1.00 60.42  ? 346 MET   D C   1 
ATOM   2756 O  O   . MET   D 1 31  ? 14.310  -16.906 22.289  1.00 61.47  ? 346 MET   D O   1 
ATOM   2757 C  CB  . MET   D 1 31  ? 12.526  -19.043 22.267  1.00 62.70  ? 346 MET   D CB  1 
ATOM   2758 C  CG  . MET   D 1 31  ? 11.698  -20.309 22.328  1.00 65.85  ? 346 MET   D CG  1 
ATOM   2759 S  SD  . MET   D 1 31  ? 9.925   -19.981 22.316  1.00 70.43  ? 346 MET   D SD  1 
ATOM   2760 C  CE  . MET   D 1 31  ? 9.749   -19.213 23.934  1.00 70.92  ? 346 MET   D CE  1 
ATOM   2761 N  N   . ALA   D 1 32  ? 16.071  -18.282 21.920  1.00 60.03  ? 347 ALA   D N   1 
ATOM   2762 C  CA  . ALA   D 1 32  ? 16.994  -17.234 21.522  1.00 59.08  ? 347 ALA   D CA  1 
ATOM   2763 C  C   . ALA   D 1 32  ? 17.144  -17.223 20.004  1.00 59.08  ? 347 ALA   D C   1 
ATOM   2764 O  O   . ALA   D 1 32  ? 16.553  -18.044 19.306  1.00 60.63  ? 347 ALA   D O   1 
ATOM   2765 C  CB  . ALA   D 1 32  ? 18.325  -17.452 22.204  1.00 58.73  ? 347 ALA   D CB  1 
ATOM   2766 N  N   . ALA   D 1 33  ? 17.929  -16.259 19.514  1.00 58.37  ? 348 ALA   D N   1 
ATOM   2767 C  CA  . ALA   D 1 33  ? 18.375  -16.233 18.133  1.00 56.55  ? 348 ALA   D CA  1 
ATOM   2768 C  C   . ALA   D 1 33  ? 19.847  -15.833 18.105  1.00 56.03  ? 348 ALA   D C   1 
ATOM   2769 O  O   . ALA   D 1 33  ? 20.235  -14.862 18.749  1.00 56.15  ? 348 ALA   D O   1 
ATOM   2770 C  CB  . ALA   D 1 33  ? 17.522  -15.283 17.323  1.00 56.07  ? 348 ALA   D CB  1 
ATOM   2771 N  N   . TYR   D 1 34  ? 20.657  -16.605 17.374  1.00 55.99  ? 349 TYR   D N   1 
ATOM   2772 C  CA  . TYR   D 1 34  ? 22.079  -16.333 17.256  1.00 55.60  ? 349 TYR   D CA  1 
ATOM   2773 C  C   . TYR   D 1 34  ? 22.441  -16.227 15.780  1.00 54.82  ? 349 TYR   D C   1 
ATOM   2774 O  O   . TYR   D 1 34  ? 21.712  -16.716 14.920  1.00 54.43  ? 349 TYR   D O   1 
ATOM   2775 C  CB  . TYR   D 1 34  ? 22.891  -17.427 17.952  1.00 56.76  ? 349 TYR   D CB  1 
ATOM   2776 C  CG  . TYR   D 1 34  ? 22.522  -17.639 19.412  1.00 57.22  ? 349 TYR   D CG  1 
ATOM   2777 C  CD1 . TYR   D 1 34  ? 21.553  -18.566 19.776  1.00 58.49  ? 349 TYR   D CD1 1 
ATOM   2778 C  CD2 . TYR   D 1 34  ? 23.132  -16.907 20.424  1.00 57.43  ? 349 TYR   D CD2 1 
ATOM   2779 C  CE1 . TYR   D 1 34  ? 21.209  -18.767 21.103  1.00 58.55  ? 349 TYR   D CE1 1 
ATOM   2780 C  CE2 . TYR   D 1 34  ? 22.795  -17.096 21.754  1.00 58.21  ? 349 TYR   D CE2 1 
ATOM   2781 C  CZ  . TYR   D 1 34  ? 21.830  -18.028 22.094  1.00 58.70  ? 349 TYR   D CZ  1 
ATOM   2782 O  OH  . TYR   D 1 34  ? 21.489  -18.220 23.402  1.00 59.28  ? 349 TYR   D OH  1 
ATOM   2783 N  N   . VAL   D 1 35  ? 23.583  -15.590 15.509  1.00 54.68  ? 350 VAL   D N   1 
ATOM   2784 C  CA  . VAL   D 1 35  ? 24.029  -15.367 14.145  1.00 55.97  ? 350 VAL   D CA  1 
ATOM   2785 C  C   . VAL   D 1 35  ? 25.265  -16.230 13.894  1.00 55.76  ? 350 VAL   D C   1 
ATOM   2786 O  O   . VAL   D 1 35  ? 26.140  -16.327 14.752  1.00 55.74  ? 350 VAL   D O   1 
ATOM   2787 C  CB  . VAL   D 1 35  ? 24.281  -13.869 13.876  1.00 56.76  ? 350 VAL   D CB  1 
ATOM   2788 C  CG1 . VAL   D 1 35  ? 25.406  -13.293 14.730  1.00 57.32  ? 350 VAL   D CG1 1 
ATOM   2789 C  CG2 . VAL   D 1 35  ? 24.532  -13.596 12.400  1.00 56.65  ? 350 VAL   D CG2 1 
ATOM   2790 N  N   . ASN   D 1 36  ? 25.306  -16.869 12.718  1.00 54.96  ? 351 ASN   D N   1 
ATOM   2791 C  CA  . ASN   D 1 36  ? 26.381  -17.783 12.363  1.00 54.67  ? 351 ASN   D CA  1 
ATOM   2792 C  C   . ASN   D 1 36  ? 27.489  -16.984 11.676  1.00 54.79  ? 351 ASN   D C   1 
ATOM   2793 O  O   . ASN   D 1 36  ? 27.308  -15.800 11.395  1.00 53.16  ? 351 ASN   D O   1 
ATOM   2794 C  CB  . ASN   D 1 36  ? 25.833  -18.968 11.569  1.00 54.61  ? 351 ASN   D CB  1 
ATOM   2795 C  CG  . ASN   D 1 36  ? 25.399  -18.612 10.166  1.00 54.21  ? 351 ASN   D CG  1 
ATOM   2796 O  OD1 . ASN   D 1 36  ? 25.677  -17.513 9.673   1.00 53.59  ? 351 ASN   D OD1 1 
ATOM   2797 N  ND2 . ASN   D 1 36  ? 24.725  -19.538 9.501   1.00 54.50  ? 351 ASN   D ND2 1 
ATOM   2798 N  N   . PRO   D 1 37  ? 28.668  -17.589 11.390  1.00 56.15  ? 352 PRO   D N   1 
ATOM   2799 C  CA  . PRO   D 1 37  ? 29.803  -16.855 10.836  1.00 56.18  ? 352 PRO   D CA  1 
ATOM   2800 C  C   . PRO   D 1 37  ? 29.504  -16.057 9.570   1.00 55.87  ? 352 PRO   D C   1 
ATOM   2801 O  O   . PRO   D 1 37  ? 30.064  -14.979 9.387   1.00 56.22  ? 352 PRO   D O   1 
ATOM   2802 C  CB  . PRO   D 1 37  ? 30.839  -17.940 10.554  1.00 55.92  ? 352 PRO   D CB  1 
ATOM   2803 C  CG  . PRO   D 1 37  ? 30.477  -19.025 11.548  1.00 56.20  ? 352 PRO   D CG  1 
ATOM   2804 C  CD  . PRO   D 1 37  ? 28.983  -19.008 11.618  1.00 56.22  ? 352 PRO   D CD  1 
ATOM   2805 N  N   . HIS   D 1 38  ? 28.632  -16.584 8.700   1.00 56.32  ? 353 HIS   D N   1 
ATOM   2806 C  CA  . HIS   D 1 38  ? 28.338  -15.918 7.440   1.00 56.91  ? 353 HIS   D CA  1 
ATOM   2807 C  C   . HIS   D 1 38  ? 27.095  -15.033 7.555   1.00 56.83  ? 353 HIS   D C   1 
ATOM   2808 O  O   . HIS   D 1 38  ? 26.554  -14.604 6.540   1.00 58.80  ? 353 HIS   D O   1 
ATOM   2809 C  CB  . HIS   D 1 38  ? 28.294  -16.915 6.274   1.00 57.52  ? 353 HIS   D CB  1 
ATOM   2810 C  CG  . HIS   D 1 38  ? 27.162  -17.888 6.292   1.00 59.52  ? 353 HIS   D CG  1 
ATOM   2811 N  ND1 . HIS   D 1 38  ? 27.340  -19.229 6.551   1.00 61.02  ? 353 HIS   D ND1 1 
ATOM   2812 C  CD2 . HIS   D 1 38  ? 25.857  -17.731 6.028   1.00 60.62  ? 353 HIS   D CD2 1 
ATOM   2813 C  CE1 . HIS   D 1 38  ? 26.168  -19.848 6.473   1.00 62.03  ? 353 HIS   D CE1 1 
ATOM   2814 N  NE2 . HIS   D 1 38  ? 25.253  -18.955 6.158   1.00 61.63  ? 353 HIS   D NE2 1 
ATOM   2815 N  N   . GLY   D 1 39  ? 26.644  -14.753 8.786   1.00 55.89  ? 354 GLY   D N   1 
ATOM   2816 C  CA  . GLY   D 1 39  ? 25.760  -13.626 9.040   1.00 55.30  ? 354 GLY   D CA  1 
ATOM   2817 C  C   . GLY   D 1 39  ? 24.280  -14.003 9.118   1.00 55.75  ? 354 GLY   D C   1 
ATOM   2818 O  O   . GLY   D 1 39  ? 23.445  -13.122 9.313   1.00 54.49  ? 354 GLY   D O   1 
ATOM   2819 N  N   . TYR   D 1 40  ? 23.955  -15.297 8.987   1.00 56.56  ? 355 TYR   D N   1 
ATOM   2820 C  CA  . TYR   D 1 40  ? 22.568  -15.743 9.042   1.00 57.10  ? 355 TYR   D CA  1 
ATOM   2821 C  C   . TYR   D 1 40  ? 22.124  -15.859 10.499  1.00 57.40  ? 355 TYR   D C   1 
ATOM   2822 O  O   . TYR   D 1 40  ? 22.860  -16.384 11.332  1.00 56.06  ? 355 TYR   D O   1 
ATOM   2823 C  CB  . TYR   D 1 40  ? 22.347  -17.076 8.320   1.00 57.04  ? 355 TYR   D CB  1 
ATOM   2824 C  CG  . TYR   D 1 40  ? 20.946  -17.652 8.494   1.00 57.07  ? 355 TYR   D CG  1 
ATOM   2825 C  CD1 . TYR   D 1 40  ? 19.833  -16.997 7.978   1.00 57.74  ? 355 TYR   D CD1 1 
ATOM   2826 C  CD2 . TYR   D 1 40  ? 20.735  -18.851 9.166   1.00 57.34  ? 355 TYR   D CD2 1 
ATOM   2827 C  CE1 . TYR   D 1 40  ? 18.555  -17.510 8.134   1.00 58.33  ? 355 TYR   D CE1 1 
ATOM   2828 C  CE2 . TYR   D 1 40  ? 19.462  -19.377 9.324   1.00 57.93  ? 355 TYR   D CE2 1 
ATOM   2829 C  CZ  . TYR   D 1 40  ? 18.368  -18.704 8.806   1.00 58.67  ? 355 TYR   D CZ  1 
ATOM   2830 O  OH  . TYR   D 1 40  ? 17.109  -19.211 8.956   1.00 59.87  ? 355 TYR   D OH  1 
ATOM   2831 N  N   . VAL   D 1 41  ? 20.899  -15.387 10.773  1.00 58.45  ? 356 VAL   D N   1 
ATOM   2832 C  CA  . VAL   D 1 41  ? 20.335  -15.374 12.114  1.00 59.15  ? 356 VAL   D CA  1 
ATOM   2833 C  C   . VAL   D 1 41  ? 19.510  -16.642 12.326  1.00 60.20  ? 356 VAL   D C   1 
ATOM   2834 O  O   . VAL   D 1 41  ? 18.402  -16.757 11.804  1.00 58.46  ? 356 VAL   D O   1 
ATOM   2835 C  CB  . VAL   D 1 41  ? 19.488  -14.105 12.338  1.00 59.45  ? 356 VAL   D CB  1 
ATOM   2836 C  CG1 . VAL   D 1 41  ? 18.763  -14.124 13.678  1.00 60.36  ? 356 VAL   D CG1 1 
ATOM   2837 C  CG2 . VAL   D 1 41  ? 20.326  -12.838 12.216  1.00 59.55  ? 356 VAL   D CG2 1 
ATOM   2838 N  N   . HIS   D 1 42  ? 20.077  -17.583 13.095  1.00 62.77  ? 357 HIS   D N   1 
ATOM   2839 C  CA  . HIS   D 1 42  ? 19.391  -18.792 13.526  1.00 64.50  ? 357 HIS   D CA  1 
ATOM   2840 C  C   . HIS   D 1 42  ? 18.461  -18.479 14.693  1.00 63.15  ? 357 HIS   D C   1 
ATOM   2841 O  O   . HIS   D 1 42  ? 18.776  -17.630 15.520  1.00 64.46  ? 357 HIS   D O   1 
ATOM   2842 C  CB  . HIS   D 1 42  ? 20.386  -19.856 14.005  1.00 67.06  ? 357 HIS   D CB  1 
ATOM   2843 C  CG  . HIS   D 1 42  ? 20.762  -20.863 12.976  1.00 70.21  ? 357 HIS   D CG  1 
ATOM   2844 N  ND1 . HIS   D 1 42  ? 20.076  -22.050 12.838  1.00 71.08  ? 357 HIS   D ND1 1 
ATOM   2845 C  CD2 . HIS   D 1 42  ? 21.736  -20.882 12.057  1.00 72.86  ? 357 HIS   D CD2 1 
ATOM   2846 C  CE1 . HIS   D 1 42  ? 20.618  -22.752 11.855  1.00 74.05  ? 357 HIS   D CE1 1 
ATOM   2847 N  NE2 . HIS   D 1 42  ? 21.632  -22.064 11.369  1.00 74.92  ? 357 HIS   D NE2 1 
ATOM   2848 N  N   . GLU   D 1 43  ? 17.333  -19.197 14.761  1.00 61.64  ? 358 GLU   D N   1 
ATOM   2849 C  CA  . GLU   D 1 43  ? 16.424  -19.117 15.892  1.00 61.40  ? 358 GLU   D CA  1 
ATOM   2850 C  C   . GLU   D 1 43  ? 16.357  -20.485 16.565  1.00 59.22  ? 358 GLU   D C   1 
ATOM   2851 O  O   . GLU   D 1 43  ? 15.857  -21.443 15.980  1.00 59.12  ? 358 GLU   D O   1 
ATOM   2852 C  CB  . GLU   D 1 43  ? 15.058  -18.604 15.437  1.00 63.45  ? 358 GLU   D CB  1 
ATOM   2853 C  CG  . GLU   D 1 43  ? 15.097  -17.147 14.986  1.00 65.96  ? 358 GLU   D CG  1 
ATOM   2854 C  CD  . GLU   D 1 43  ? 13.746  -16.459 14.973  1.00 68.80  ? 358 GLU   D CD  1 
ATOM   2855 O  OE1 . GLU   D 1 43  ? 12.886  -16.852 14.155  1.00 70.05  ? 358 GLU   D OE1 1 
ATOM   2856 O  OE2 . GLU   D 1 43  ? 13.554  -15.533 15.792  1.00 71.88  ? 358 GLU   D OE2 1 
ATOM   2857 N  N   . THR   D 1 44  ? 16.857  -20.546 17.807  1.00 57.20  ? 359 THR   D N   1 
ATOM   2858 C  CA  . THR   D 1 44  ? 17.161  -21.805 18.467  1.00 55.16  ? 359 THR   D CA  1 
ATOM   2859 C  C   . THR   D 1 44  ? 16.247  -22.015 19.672  1.00 53.01  ? 359 THR   D C   1 
ATOM   2860 O  O   . THR   D 1 44  ? 15.607  -21.081 20.151  1.00 50.08  ? 359 THR   D O   1 
ATOM   2861 C  CB  . THR   D 1 44  ? 18.629  -21.811 18.892  1.00 55.43  ? 359 THR   D CB  1 
ATOM   2862 O  OG1 . THR   D 1 44  ? 18.768  -20.737 19.818  1.00 56.33  ? 359 THR   D OG1 1 
ATOM   2863 C  CG2 . THR   D 1 44  ? 19.578  -21.626 17.722  1.00 55.59  ? 359 THR   D CG2 1 
ATOM   2864 N  N   . LEU   D 1 45  ? 16.228  -23.265 20.150  1.00 52.16  ? 360 LEU   D N   1 
ATOM   2865 C  CA  . LEU   D 1 45  ? 15.506  -23.667 21.346  1.00 51.23  ? 360 LEU   D CA  1 
ATOM   2866 C  C   . LEU   D 1 45  ? 16.412  -24.574 22.175  1.00 51.07  ? 360 LEU   D C   1 
ATOM   2867 O  O   . LEU   D 1 45  ? 16.831  -25.625 21.697  1.00 51.28  ? 360 LEU   D O   1 
ATOM   2868 C  CB  . LEU   D 1 45  ? 14.224  -24.391 20.936  1.00 51.21  ? 360 LEU   D CB  1 
ATOM   2869 C  CG  . LEU   D 1 45  ? 13.403  -25.015 22.070  1.00 52.24  ? 360 LEU   D CG  1 
ATOM   2870 C  CD1 . LEU   D 1 45  ? 12.864  -23.947 23.003  1.00 52.85  ? 360 LEU   D CD1 1 
ATOM   2871 C  CD2 . LEU   D 1 45  ? 12.273  -25.864 21.512  1.00 52.44  ? 360 LEU   D CD2 1 
ATOM   2872 N  N   . THR   D 1 46  ? 16.709  -24.159 23.412  1.00 51.50  ? 361 THR   D N   1 
ATOM   2873 C  CA  . THR   D 1 46  ? 17.544  -24.945 24.308  1.00 51.50  ? 361 THR   D CA  1 
ATOM   2874 C  C   . THR   D 1 46  ? 16.680  -25.970 25.038  1.00 50.45  ? 361 THR   D C   1 
ATOM   2875 O  O   . THR   D 1 46  ? 15.660  -25.619 25.628  1.00 48.72  ? 361 THR   D O   1 
ATOM   2876 C  CB  . THR   D 1 46  ? 18.277  -24.027 25.286  1.00 51.97  ? 361 THR   D CB  1 
ATOM   2877 O  OG1 . THR   D 1 46  ? 17.294  -23.136 25.806  1.00 52.11  ? 361 THR   D OG1 1 
ATOM   2878 C  CG2 . THR   D 1 46  ? 19.394  -23.249 24.616  1.00 52.24  ? 361 THR   D CG2 1 
ATOM   2879 N  N   . VAL   D 1 47  ? 17.100  -27.241 24.982  1.00 51.09  ? 362 VAL   D N   1 
ATOM   2880 C  CA  . VAL   D 1 47  ? 16.450  -28.307 25.727  1.00 51.95  ? 362 VAL   D CA  1 
ATOM   2881 C  C   . VAL   D 1 47  ? 17.524  -29.155 26.407  1.00 51.54  ? 362 VAL   D C   1 
ATOM   2882 O  O   . VAL   D 1 47  ? 18.631  -29.298 25.891  1.00 50.49  ? 362 VAL   D O   1 
ATOM   2883 C  CB  . VAL   D 1 47  ? 15.527  -29.173 24.846  1.00 52.63  ? 362 VAL   D CB  1 
ATOM   2884 C  CG1 . VAL   D 1 47  ? 14.410  -28.348 24.217  1.00 53.21  ? 362 VAL   D CG1 1 
ATOM   2885 C  CG2 . VAL   D 1 47  ? 16.296  -29.933 23.770  1.00 52.57  ? 362 VAL   D CG2 1 
ATOM   2886 N  N   . TYR   D 1 48  ? 17.170  -29.711 27.571  1.00 52.54  ? 363 TYR   D N   1 
ATOM   2887 C  CA  . TYR   D 1 48  ? 18.070  -30.543 28.354  1.00 53.92  ? 363 TYR   D CA  1 
ATOM   2888 C  C   . TYR   D 1 48  ? 18.336  -31.865 27.641  1.00 55.80  ? 363 TYR   D C   1 
ATOM   2889 O  O   . TYR   D 1 48  ? 19.447  -32.388 27.708  1.00 56.91  ? 363 TYR   D O   1 
ATOM   2890 C  CB  . TYR   D 1 48  ? 17.488  -30.833 29.743  1.00 52.82  ? 363 TYR   D CB  1 
ATOM   2891 C  CG  . TYR   D 1 48  ? 17.736  -29.754 30.788  1.00 51.22  ? 363 TYR   D CG  1 
ATOM   2892 C  CD1 . TYR   D 1 48  ? 19.014  -29.252 31.010  1.00 51.07  ? 363 TYR   D CD1 1 
ATOM   2893 C  CD2 . TYR   D 1 48  ? 16.693  -29.231 31.546  1.00 50.86  ? 363 TYR   D CD2 1 
ATOM   2894 C  CE1 . TYR   D 1 48  ? 19.249  -28.269 31.956  1.00 51.18  ? 363 TYR   D CE1 1 
ATOM   2895 C  CE2 . TYR   D 1 48  ? 16.915  -28.248 32.497  1.00 50.75  ? 363 TYR   D CE2 1 
ATOM   2896 C  CZ  . TYR   D 1 48  ? 18.197  -27.765 32.700  1.00 50.96  ? 363 TYR   D CZ  1 
ATOM   2897 O  OH  . TYR   D 1 48  ? 18.444  -26.795 33.627  1.00 51.06  ? 363 TYR   D OH  1 
ATOM   2898 N  N   . LYS   D 1 49  ? 17.304  -32.406 26.982  1.00 57.38  ? 364 LYS   D N   1 
ATOM   2899 C  CA  . LYS   D 1 49  ? 17.364  -33.754 26.444  1.00 58.79  ? 364 LYS   D CA  1 
ATOM   2900 C  C   . LYS   D 1 49  ? 16.657  -33.833 25.094  1.00 58.57  ? 364 LYS   D C   1 
ATOM   2901 O  O   . LYS   D 1 49  ? 15.645  -33.172 24.870  1.00 58.62  ? 364 LYS   D O   1 
ATOM   2902 C  CB  . LYS   D 1 49  ? 16.732  -34.736 27.436  1.00 60.52  ? 364 LYS   D CB  1 
ATOM   2903 C  CG  . LYS   D 1 49  ? 17.564  -34.986 28.682  1.00 61.87  ? 364 LYS   D CG  1 
ATOM   2904 C  CD  . LYS   D 1 49  ? 16.889  -35.870 29.722  1.00 62.23  ? 364 LYS   D CD  1 
ATOM   2905 C  CE  . LYS   D 1 49  ? 17.821  -36.203 30.841  1.00 63.24  ? 364 LYS   D CE  1 
ATOM   2906 N  NZ  . LYS   D 1 49  ? 17.115  -36.826 31.961  1.00 64.41  ? 364 LYS   D NZ  1 
ATOM   2907 N  N   . ALA   D 1 50  ? 17.224  -34.665 24.213  1.00 58.28  ? 365 ALA   D N   1 
ATOM   2908 C  CA  . ALA   D 1 50  ? 16.623  -35.020 22.940  1.00 58.01  ? 365 ALA   D CA  1 
ATOM   2909 C  C   . ALA   D 1 50  ? 17.068  -36.433 22.573  1.00 58.60  ? 365 ALA   D C   1 
ATOM   2910 O  O   . ALA   D 1 50  ? 18.054  -36.933 23.110  1.00 59.13  ? 365 ALA   D O   1 
ATOM   2911 C  CB  . ALA   D 1 50  ? 17.021  -34.018 21.878  1.00 57.90  ? 365 ALA   D CB  1 
ATOM   2912 N  N   . SER   D 1 51  ? 16.325  -37.070 21.663  1.00 59.33  ? 366 SER   D N   1 
ATOM   2913 C  CA  . SER   D 1 51  ? 16.665  -38.402 21.194  1.00 60.35  ? 366 SER   D CA  1 
ATOM   2914 C  C   . SER   D 1 51  ? 16.305  -38.533 19.716  1.00 59.53  ? 366 SER   D C   1 
ATOM   2915 O  O   . SER   D 1 51  ? 15.735  -37.612 19.134  1.00 58.79  ? 366 SER   D O   1 
ATOM   2916 C  CB  . SER   D 1 51  ? 15.997  -39.457 22.043  1.00 61.37  ? 366 SER   D CB  1 
ATOM   2917 O  OG  . SER   D 1 51  ? 14.615  -39.175 22.213  1.00 61.81  ? 366 SER   D OG  1 
ATOM   2918 N  N   . ASN   D 1 52  ? 16.671  -39.678 19.125  1.00 58.97  ? 367 ASN   D N   1 
ATOM   2919 C  CA  . ASN   D 1 52  ? 16.500  -39.936 17.703  1.00 58.70  ? 367 ASN   D CA  1 
ATOM   2920 C  C   . ASN   D 1 52  ? 17.365  -38.968 16.900  1.00 55.97  ? 367 ASN   D C   1 
ATOM   2921 O  O   . ASN   D 1 52  ? 16.939  -38.467 15.862  1.00 53.96  ? 367 ASN   D O   1 
ATOM   2922 C  CB  . ASN   D 1 52  ? 15.036  -39.880 17.269  1.00 60.03  ? 367 ASN   D CB  1 
ATOM   2923 C  CG  . ASN   D 1 52  ? 14.167  -40.918 17.941  1.00 61.54  ? 367 ASN   D CG  1 
ATOM   2924 O  OD1 . ASN   D 1 52  ? 12.937  -40.835 17.852  1.00 62.89  ? 367 ASN   D OD1 1 
ATOM   2925 N  ND2 . ASN   D 1 52  ? 14.759  -41.895 18.613  1.00 62.25  ? 367 ASN   D ND2 1 
ATOM   2926 N  N   . LEU   D 1 53  ? 18.587  -38.727 17.390  1.00 55.17  ? 368 LEU   D N   1 
ATOM   2927 C  CA  . LEU   D 1 53  ? 19.512  -37.816 16.740  1.00 55.75  ? 368 LEU   D CA  1 
ATOM   2928 C  C   . LEU   D 1 53  ? 20.854  -38.516 16.552  1.00 55.23  ? 368 LEU   D C   1 
ATOM   2929 O  O   . LEU   D 1 53  ? 21.438  -39.009 17.516  1.00 54.64  ? 368 LEU   D O   1 
ATOM   2930 C  CB  . LEU   D 1 53  ? 19.672  -36.529 17.549  1.00 56.63  ? 368 LEU   D CB  1 
ATOM   2931 C  CG  . LEU   D 1 53  ? 18.432  -35.636 17.676  1.00 56.68  ? 368 LEU   D CG  1 
ATOM   2932 C  CD1 . LEU   D 1 53  ? 18.741  -34.445 18.570  1.00 56.70  ? 368 LEU   D CD1 1 
ATOM   2933 C  CD2 . LEU   D 1 53  ? 17.918  -35.157 16.328  1.00 56.44  ? 368 LEU   D CD2 1 
ATOM   2934 N  N   . ASN   D 1 54  ? 21.318  -38.564 15.297  1.00 54.76  ? 369 ASN   D N   1 
ATOM   2935 C  CA  . ASN   D 1 54  ? 22.690  -38.928 14.994  1.00 53.91  ? 369 ASN   D CA  1 
ATOM   2936 C  C   . ASN   D 1 54  ? 23.567  -37.693 15.172  1.00 53.35  ? 369 ASN   D C   1 
ATOM   2937 O  O   . ASN   D 1 54  ? 23.249  -36.626 14.648  1.00 51.74  ? 369 ASN   D O   1 
ATOM   2938 C  CB  . ASN   D 1 54  ? 22.838  -39.496 13.585  1.00 53.93  ? 369 ASN   D CB  1 
ATOM   2939 C  CG  . ASN   D 1 54  ? 22.309  -40.905 13.465  1.00 54.28  ? 369 ASN   D CG  1 
ATOM   2940 O  OD1 . ASN   D 1 54  ? 21.389  -41.158 12.680  1.00 55.09  ? 369 ASN   D OD1 1 
ATOM   2941 N  ND2 . ASN   D 1 54  ? 22.881  -41.836 14.213  1.00 54.59  ? 369 ASN   D ND2 1 
ATOM   2942 N  N   . LEU   D 1 55  ? 24.652  -37.849 15.938  1.00 53.57  ? 370 LEU   D N   1 
ATOM   2943 C  CA  . LEU   D 1 55  ? 25.689  -36.835 16.025  1.00 53.79  ? 370 LEU   D CA  1 
ATOM   2944 C  C   . LEU   D 1 55  ? 26.707  -37.100 14.922  1.00 54.23  ? 370 LEU   D C   1 
ATOM   2945 O  O   . LEU   D 1 55  ? 26.867  -38.234 14.476  1.00 54.27  ? 370 LEU   D O   1 
ATOM   2946 C  CB  . LEU   D 1 55  ? 26.345  -36.839 17.405  1.00 54.21  ? 370 LEU   D CB  1 
ATOM   2947 C  CG  . LEU   D 1 55  ? 25.412  -36.583 18.593  1.00 55.32  ? 370 LEU   D CG  1 
ATOM   2948 C  CD1 . LEU   D 1 55  ? 26.202  -36.656 19.887  1.00 55.89  ? 370 LEU   D CD1 1 
ATOM   2949 C  CD2 . LEU   D 1 55  ? 24.689  -35.249 18.482  1.00 55.64  ? 370 LEU   D CD2 1 
ATOM   2950 N  N   . ILE   D 1 56  ? 27.391  -36.033 14.498  1.00 55.09  ? 371 ILE   D N   1 
ATOM   2951 C  CA  . ILE   D 1 56  ? 28.207  -36.065 13.297  1.00 55.88  ? 371 ILE   D CA  1 
ATOM   2952 C  C   . ILE   D 1 56  ? 29.353  -35.067 13.454  1.00 56.10  ? 371 ILE   D C   1 
ATOM   2953 O  O   . ILE   D 1 56  ? 29.133  -33.858 13.476  1.00 54.74  ? 371 ILE   D O   1 
ATOM   2954 C  CB  . ILE   D 1 56  ? 27.332  -35.818 12.048  1.00 56.01  ? 371 ILE   D CB  1 
ATOM   2955 C  CG1 . ILE   D 1 56  ? 28.098  -35.125 10.915  1.00 56.55  ? 371 ILE   D CG1 1 
ATOM   2956 C  CG2 . ILE   D 1 56  ? 26.058  -35.047 12.404  1.00 56.99  ? 371 ILE   D CG2 1 
ATOM   2957 C  CD1 . ILE   D 1 56  ? 27.236  -34.748 9.724   1.00 57.42  ? 371 ILE   D CD1 1 
ATOM   2958 N  N   . GLY   D 1 57  ? 30.573  -35.602 13.596  1.00 58.43  ? 372 GLY   D N   1 
ATOM   2959 C  CA  . GLY   D 1 57  ? 31.785  -34.801 13.664  1.00 60.67  ? 372 GLY   D CA  1 
ATOM   2960 C  C   . GLY   D 1 57  ? 32.328  -34.708 15.088  1.00 62.29  ? 372 GLY   D C   1 
ATOM   2961 O  O   . GLY   D 1 57  ? 31.786  -35.315 16.009  1.00 59.51  ? 372 GLY   D O   1 
ATOM   2962 N  N   . ARG   D 1 58  ? 33.421  -33.948 15.238  1.00 66.43  ? 373 ARG   D N   1 
ATOM   2963 C  CA  . ARG   D 1 58  ? 33.974  -33.605 16.537  1.00 68.93  ? 373 ARG   D CA  1 
ATOM   2964 C  C   . ARG   D 1 58  ? 33.170  -32.465 17.154  1.00 65.52  ? 373 ARG   D C   1 
ATOM   2965 O  O   . ARG   D 1 58  ? 32.553  -31.680 16.437  1.00 65.80  ? 373 ARG   D O   1 
ATOM   2966 C  CB  . ARG   D 1 58  ? 35.413  -33.085 16.429  1.00 74.08  ? 373 ARG   D CB  1 
ATOM   2967 C  CG  . ARG   D 1 58  ? 36.465  -34.122 16.061  1.00 78.68  ? 373 ARG   D CG  1 
ATOM   2968 C  CD  . ARG   D 1 58  ? 36.635  -35.176 17.148  1.00 82.10  ? 373 ARG   D CD  1 
ATOM   2969 N  NE  . ARG   D 1 58  ? 37.744  -36.098 16.873  1.00 86.02  ? 373 ARG   D NE  1 
ATOM   2970 C  CZ  . ARG   D 1 58  ? 37.811  -36.951 15.854  1.00 88.60  ? 373 ARG   D CZ  1 
ATOM   2971 N  NH1 . ARG   D 1 58  ? 36.821  -37.041 14.982  1.00 89.83  ? 373 ARG   D NH1 1 
ATOM   2972 N  NH2 . ARG   D 1 58  ? 38.873  -37.725 15.710  1.00 89.02  ? 373 ARG   D NH2 1 
ATOM   2973 N  N   . PRO   D 1 59  ? 33.150  -32.335 18.500  1.00 61.60  ? 374 PRO   D N   1 
ATOM   2974 C  CA  . PRO   D 1 59  ? 32.790  -31.071 19.130  1.00 59.39  ? 374 PRO   D CA  1 
ATOM   2975 C  C   . PRO   D 1 59  ? 33.792  -29.965 18.804  1.00 57.47  ? 374 PRO   D C   1 
ATOM   2976 O  O   . PRO   D 1 59  ? 34.998  -30.201 18.812  1.00 55.96  ? 374 PRO   D O   1 
ATOM   2977 C  CB  . PRO   D 1 59  ? 32.738  -31.403 20.620  1.00 59.33  ? 374 PRO   D CB  1 
ATOM   2978 C  CG  . PRO   D 1 59  ? 32.673  -32.920 20.678  1.00 60.06  ? 374 PRO   D CG  1 
ATOM   2979 C  CD  . PRO   D 1 59  ? 33.411  -33.405 19.474  1.00 60.68  ? 374 PRO   D CD  1 
ATOM   2980 N  N   . SER   D 1 60  ? 33.272  -28.769 18.502  1.00 56.47  ? 375 SER   D N   1 
ATOM   2981 C  CA  . SER   D 1 60  ? 34.091  -27.621 18.151  1.00 55.27  ? 375 SER   D CA  1 
ATOM   2982 C  C   . SER   D 1 60  ? 33.616  -26.395 18.924  1.00 55.06  ? 375 SER   D C   1 
ATOM   2983 O  O   . SER   D 1 60  ? 32.422  -26.241 19.165  1.00 54.35  ? 375 SER   D O   1 
ATOM   2984 C  CB  . SER   D 1 60  ? 34.053  -27.368 16.668  1.00 55.49  ? 375 SER   D CB  1 
ATOM   2985 O  OG  . SER   D 1 60  ? 34.710  -26.151 16.340  1.00 55.65  ? 375 SER   D OG  1 
ATOM   2986 N  N   . THR   D 1 61  ? 34.567  -25.526 19.292  1.00 55.87  ? 376 THR   D N   1 
ATOM   2987 C  CA  . THR   D 1 61  ? 34.270  -24.300 20.018  1.00 56.46  ? 376 THR   D CA  1 
ATOM   2988 C  C   . THR   D 1 61  ? 34.428  -23.088 19.100  1.00 56.83  ? 376 THR   D C   1 
ATOM   2989 O  O   . THR   D 1 61  ? 34.363  -21.950 19.563  1.00 57.06  ? 376 THR   D O   1 
ATOM   2990 C  CB  . THR   D 1 61  ? 35.180  -24.202 21.242  1.00 56.63  ? 376 THR   D CB  1 
ATOM   2991 O  OG1 . THR   D 1 61  ? 36.507  -24.395 20.762  1.00 56.84  ? 376 THR   D OG1 1 
ATOM   2992 C  CG2 . THR   D 1 61  ? 34.855  -25.250 22.291  1.00 56.96  ? 376 THR   D CG2 1 
ATOM   2993 N  N   . GLU   D 1 62  ? 34.631  -23.338 17.801  1.00 57.73  ? 377 GLU   D N   1 
ATOM   2994 C  CA  . GLU   D 1 62  ? 34.700  -22.278 16.809  1.00 59.57  ? 377 GLU   D CA  1 
ATOM   2995 C  C   . GLU   D 1 62  ? 33.360  -21.549 16.771  1.00 56.88  ? 377 GLU   D C   1 
ATOM   2996 O  O   . GLU   D 1 62  ? 32.344  -22.144 16.417  1.00 55.29  ? 377 GLU   D O   1 
ATOM   2997 C  CB  . GLU   D 1 62  ? 35.058  -22.879 15.446  1.00 63.64  ? 377 GLU   D CB  1 
ATOM   2998 C  CG  . GLU   D 1 62  ? 35.010  -21.891 14.282  1.00 66.44  ? 377 GLU   D CG  1 
ATOM   2999 C  CD  . GLU   D 1 62  ? 35.200  -22.522 12.910  1.00 70.38  ? 377 GLU   D CD  1 
ATOM   3000 O  OE1 . GLU   D 1 62  ? 35.472  -23.741 12.832  1.00 72.50  ? 377 GLU   D OE1 1 
ATOM   3001 O  OE2 . GLU   D 1 62  ? 35.062  -21.787 11.909  1.00 73.16  ? 377 GLU   D OE2 1 
ATOM   3002 N  N   . HIS   D 1 63  ? 33.373  -20.269 17.168  1.00 54.78  ? 378 HIS   D N   1 
ATOM   3003 C  CA  . HIS   D 1 63  ? 32.233  -19.382 16.992  1.00 53.83  ? 378 HIS   D CA  1 
ATOM   3004 C  C   . HIS   D 1 63  ? 31.054  -19.891 17.823  1.00 53.25  ? 378 HIS   D C   1 
ATOM   3005 O  O   . HIS   D 1 63  ? 29.912  -19.858 17.369  1.00 52.96  ? 378 HIS   D O   1 
ATOM   3006 C  CB  . HIS   D 1 63  ? 31.913  -19.258 15.496  1.00 54.03  ? 378 HIS   D CB  1 
ATOM   3007 C  CG  . HIS   D 1 63  ? 31.216  -18.003 15.089  1.00 54.01  ? 378 HIS   D CG  1 
ATOM   3008 N  ND1 . HIS   D 1 63  ? 29.845  -17.879 15.016  1.00 54.08  ? 378 HIS   D ND1 1 
ATOM   3009 C  CD2 . HIS   D 1 63  ? 31.715  -16.824 14.695  1.00 53.40  ? 378 HIS   D CD2 1 
ATOM   3010 C  CE1 . HIS   D 1 63  ? 29.540  -16.656 14.607  1.00 53.98  ? 378 HIS   D CE1 1 
ATOM   3011 N  NE2 . HIS   D 1 63  ? 30.661  -15.999 14.404  1.00 53.36  ? 378 HIS   D NE2 1 
ATOM   3012 N  N   . SER   D 1 64  ? 31.344  -20.346 19.049  1.00 52.19  ? 379 SER   D N   1 
ATOM   3013 C  CA  . SER   D 1 64  ? 30.342  -20.955 19.911  1.00 51.76  ? 379 SER   D CA  1 
ATOM   3014 C  C   . SER   D 1 64  ? 29.375  -19.894 20.431  1.00 51.46  ? 379 SER   D C   1 
ATOM   3015 O  O   . SER   D 1 64  ? 29.798  -18.835 20.888  1.00 51.72  ? 379 SER   D O   1 
ATOM   3016 C  CB  . SER   D 1 64  ? 30.989  -21.700 21.052  1.00 51.63  ? 379 SER   D CB  1 
ATOM   3017 O  OG  . SER   D 1 64  ? 30.011  -22.217 21.944  1.00 51.67  ? 379 SER   D OG  1 
ATOM   3018 N  N   . TRP   D 1 65  ? 28.074  -20.206 20.374  1.00 51.03  ? 380 TRP   D N   1 
ATOM   3019 C  CA  . TRP   D 1 65  ? 27.033  -19.315 20.862  1.00 50.70  ? 380 TRP   D CA  1 
ATOM   3020 C  C   . TRP   D 1 65  ? 26.920  -19.388 22.384  1.00 51.05  ? 380 TRP   D C   1 
ATOM   3021 O  O   . TRP   D 1 65  ? 26.309  -18.516 22.999  1.00 51.37  ? 380 TRP   D O   1 
ATOM   3022 C  CB  . TRP   D 1 65  ? 25.692  -19.659 20.200  1.00 49.82  ? 380 TRP   D CB  1 
ATOM   3023 C  CG  . TRP   D 1 65  ? 25.695  -19.489 18.704  1.00 49.13  ? 380 TRP   D CG  1 
ATOM   3024 C  CD1 . TRP   D 1 65  ? 26.517  -18.681 17.977  1.00 49.11  ? 380 TRP   D CD1 1 
ATOM   3025 C  CD2 . TRP   D 1 65  ? 24.825  -20.139 17.753  1.00 49.11  ? 380 TRP   D CD2 1 
ATOM   3026 N  NE1 . TRP   D 1 65  ? 26.224  -18.782 16.644  1.00 50.12  ? 380 TRP   D NE1 1 
ATOM   3027 C  CE2 . TRP   D 1 65  ? 25.192  -19.666 16.475  1.00 49.87  ? 380 TRP   D CE2 1 
ATOM   3028 C  CE3 . TRP   D 1 65  ? 23.780  -21.065 17.854  1.00 49.72  ? 380 TRP   D CE3 1 
ATOM   3029 C  CZ2 . TRP   D 1 65  ? 24.551  -20.091 15.313  1.00 50.61  ? 380 TRP   D CZ2 1 
ATOM   3030 C  CZ3 . TRP   D 1 65  ? 23.147  -21.484 16.704  1.00 50.12  ? 380 TRP   D CZ3 1 
ATOM   3031 C  CH2 . TRP   D 1 65  ? 23.529  -21.003 15.451  1.00 50.64  ? 380 TRP   D CH2 1 
ATOM   3032 N  N   . PHE   D 1 66  ? 27.492  -20.441 22.979  1.00 51.24  ? 381 PHE   D N   1 
ATOM   3033 C  CA  . PHE   D 1 66  ? 27.479  -20.616 24.422  1.00 50.61  ? 381 PHE   D CA  1 
ATOM   3034 C  C   . PHE   D 1 66  ? 28.916  -20.750 24.914  1.00 50.28  ? 381 PHE   D C   1 
ATOM   3035 O  O   . PHE   D 1 66  ? 29.458  -21.852 24.952  1.00 48.53  ? 381 PHE   D O   1 
ATOM   3036 C  CB  . PHE   D 1 66  ? 26.596  -21.821 24.758  1.00 50.41  ? 381 PHE   D CB  1 
ATOM   3037 C  CG  . PHE   D 1 66  ? 25.170  -21.678 24.247  1.00 50.38  ? 381 PHE   D CG  1 
ATOM   3038 C  CD1 . PHE   D 1 66  ? 24.246  -20.889 24.923  1.00 50.91  ? 381 PHE   D CD1 1 
ATOM   3039 C  CD2 . PHE   D 1 66  ? 24.758  -22.323 23.086  1.00 50.48  ? 381 PHE   D CD2 1 
ATOM   3040 C  CE1 . PHE   D 1 66  ? 22.948  -20.758 24.454  1.00 51.30  ? 381 PHE   D CE1 1 
ATOM   3041 C  CE2 . PHE   D 1 66  ? 23.459  -22.187 22.621  1.00 50.71  ? 381 PHE   D CE2 1 
ATOM   3042 C  CZ  . PHE   D 1 66  ? 22.557  -21.405 23.305  1.00 51.03  ? 381 PHE   D CZ  1 
ATOM   3043 N  N   . PRO   D 1 67  ? 29.575  -19.630 25.295  1.00 51.92  ? 382 PRO   D N   1 
ATOM   3044 C  CA  . PRO   D 1 67  ? 30.950  -19.677 25.777  1.00 53.45  ? 382 PRO   D CA  1 
ATOM   3045 C  C   . PRO   D 1 67  ? 31.168  -20.744 26.846  1.00 54.82  ? 382 PRO   D C   1 
ATOM   3046 O  O   . PRO   D 1 67  ? 30.475  -20.755 27.861  1.00 55.85  ? 382 PRO   D O   1 
ATOM   3047 C  CB  . PRO   D 1 67  ? 31.190  -18.265 26.309  1.00 53.38  ? 382 PRO   D CB  1 
ATOM   3048 C  CG  . PRO   D 1 67  ? 30.226  -17.409 25.508  1.00 52.76  ? 382 PRO   D CG  1 
ATOM   3049 C  CD  . PRO   D 1 67  ? 29.021  -18.267 25.274  1.00 52.36  ? 382 PRO   D CD  1 
ATOM   3050 N  N   . GLY   D 1 68  ? 32.122  -21.648 26.588  1.00 55.78  ? 383 GLY   D N   1 
ATOM   3051 C  CA  . GLY   D 1 68  ? 32.426  -22.743 27.496  1.00 56.43  ? 383 GLY   D CA  1 
ATOM   3052 C  C   . GLY   D 1 68  ? 31.985  -24.094 26.934  1.00 57.33  ? 383 GLY   D C   1 
ATOM   3053 O  O   . GLY   D 1 68  ? 32.452  -25.131 27.399  1.00 58.52  ? 383 GLY   D O   1 
ATOM   3054 N  N   . TYR   D 1 69  ? 31.080  -24.069 25.943  1.00 57.10  ? 384 TYR   D N   1 
ATOM   3055 C  CA  . TYR   D 1 69  ? 30.535  -25.280 25.349  1.00 55.61  ? 384 TYR   D CA  1 
ATOM   3056 C  C   . TYR   D 1 69  ? 31.065  -25.450 23.927  1.00 54.33  ? 384 TYR   D C   1 
ATOM   3057 O  O   . TYR   D 1 69  ? 31.321  -24.468 23.234  1.00 54.40  ? 384 TYR   D O   1 
ATOM   3058 C  CB  . TYR   D 1 69  ? 29.005  -25.234 25.315  1.00 54.91  ? 384 TYR   D CB  1 
ATOM   3059 C  CG  . TYR   D 1 69  ? 28.332  -25.352 26.675  1.00 55.21  ? 384 TYR   D CG  1 
ATOM   3060 C  CD1 . TYR   D 1 69  ? 28.123  -24.233 27.472  1.00 55.16  ? 384 TYR   D CD1 1 
ATOM   3061 C  CD2 . TYR   D 1 69  ? 27.898  -26.582 27.157  1.00 55.68  ? 384 TYR   D CD2 1 
ATOM   3062 C  CE1 . TYR   D 1 69  ? 27.508  -24.333 28.709  1.00 54.48  ? 384 TYR   D CE1 1 
ATOM   3063 C  CE2 . TYR   D 1 69  ? 27.281  -26.696 28.393  1.00 55.15  ? 384 TYR   D CE2 1 
ATOM   3064 C  CZ  . TYR   D 1 69  ? 27.086  -25.567 29.170  1.00 55.15  ? 384 TYR   D CZ  1 
ATOM   3065 O  OH  . TYR   D 1 69  ? 26.480  -25.655 30.389  1.00 57.63  ? 384 TYR   D OH  1 
ATOM   3066 N  N   . ALA   D 1 70  ? 31.216  -26.713 23.512  1.00 53.27  ? 385 ALA   D N   1 
ATOM   3067 C  CA  . ALA   D 1 70  ? 31.482  -27.059 22.126  1.00 53.05  ? 385 ALA   D CA  1 
ATOM   3068 C  C   . ALA   D 1 70  ? 30.186  -27.537 21.480  1.00 52.37  ? 385 ALA   D C   1 
ATOM   3069 O  O   . ALA   D 1 70  ? 29.277  -27.972 22.181  1.00 51.85  ? 385 ALA   D O   1 
ATOM   3070 C  CB  . ALA   D 1 70  ? 32.560  -28.119 22.056  1.00 53.07  ? 385 ALA   D CB  1 
ATOM   3071 N  N   . TRP   D 1 71  ? 30.114  -27.452 20.146  1.00 51.81  ? 386 TRP   D N   1 
ATOM   3072 C  CA  . TRP   D 1 71  ? 28.943  -27.898 19.407  1.00 51.95  ? 386 TRP   D CA  1 
ATOM   3073 C  C   . TRP   D 1 71  ? 29.316  -29.047 18.476  1.00 51.46  ? 386 TRP   D C   1 
ATOM   3074 O  O   . TRP   D 1 71  ? 30.350  -29.007 17.814  1.00 52.25  ? 386 TRP   D O   1 
ATOM   3075 C  CB  . TRP   D 1 71  ? 28.309  -26.743 18.619  1.00 52.90  ? 386 TRP   D CB  1 
ATOM   3076 C  CG  . TRP   D 1 71  ? 29.263  -25.994 17.725  1.00 54.05  ? 386 TRP   D CG  1 
ATOM   3077 C  CD1 . TRP   D 1 71  ? 29.933  -24.846 18.032  1.00 54.59  ? 386 TRP   D CD1 1 
ATOM   3078 C  CD2 . TRP   D 1 71  ? 29.653  -26.338 16.377  1.00 54.44  ? 386 TRP   D CD2 1 
ATOM   3079 N  NE1 . TRP   D 1 71  ? 30.712  -24.453 16.977  1.00 55.06  ? 386 TRP   D NE1 1 
ATOM   3080 C  CE2 . TRP   D 1 71  ? 30.563  -25.346 15.949  1.00 54.74  ? 386 TRP   D CE2 1 
ATOM   3081 C  CE3 . TRP   D 1 71  ? 29.329  -27.378 15.497  1.00 54.86  ? 386 TRP   D CE3 1 
ATOM   3082 C  CZ2 . TRP   D 1 71  ? 31.146  -25.369 14.683  1.00 54.25  ? 386 TRP   D CZ2 1 
ATOM   3083 C  CZ3 . TRP   D 1 71  ? 29.906  -27.399 14.246  1.00 54.16  ? 386 TRP   D CZ3 1 
ATOM   3084 C  CH2 . TRP   D 1 71  ? 30.802  -26.407 13.847  1.00 54.01  ? 386 TRP   D CH2 1 
ATOM   3085 N  N   . THR   D 1 72  ? 28.459  -30.073 18.456  1.00 50.91  ? 387 THR   D N   1 
ATOM   3086 C  CA  . THR   D 1 72  ? 28.487  -31.097 17.427  1.00 50.68  ? 387 THR   D CA  1 
ATOM   3087 C  C   . THR   D 1 72  ? 27.144  -31.047 16.705  1.00 51.15  ? 387 THR   D C   1 
ATOM   3088 O  O   . THR   D 1 72  ? 26.118  -30.825 17.340  1.00 50.51  ? 387 THR   D O   1 
ATOM   3089 C  CB  . THR   D 1 72  ? 28.751  -32.463 18.058  1.00 50.73  ? 387 THR   D CB  1 
ATOM   3090 O  OG1 . THR   D 1 72  ? 29.865  -32.290 18.929  1.00 50.80  ? 387 THR   D OG1 1 
ATOM   3091 C  CG2 . THR   D 1 72  ? 29.070  -33.532 17.029  1.00 50.98  ? 387 THR   D CG2 1 
ATOM   3092 N  N   . VAL   D 1 73  ? 27.163  -31.239 15.382  1.00 53.05  ? 388 VAL   D N   1 
ATOM   3093 C  CA  . VAL   D 1 73  ? 25.958  -31.141 14.572  1.00 54.90  ? 388 VAL   D CA  1 
ATOM   3094 C  C   . VAL   D 1 73  ? 25.064  -32.345 14.872  1.00 56.31  ? 388 VAL   D C   1 
ATOM   3095 O  O   . VAL   D 1 73  ? 25.561  -33.438 15.135  1.00 56.30  ? 388 VAL   D O   1 
ATOM   3096 C  CB  . VAL   D 1 73  ? 26.300  -31.034 13.071  1.00 55.84  ? 388 VAL   D CB  1 
ATOM   3097 C  CG1 . VAL   D 1 73  ? 25.054  -31.035 12.190  1.00 55.88  ? 388 VAL   D CG1 1 
ATOM   3098 C  CG2 . VAL   D 1 73  ? 27.153  -29.804 12.774  1.00 56.13  ? 388 VAL   D CG2 1 
ATOM   3099 N  N   . ALA   D 1 74  ? 23.742  -32.121 14.832  1.00 57.35  ? 389 ALA   D N   1 
ATOM   3100 C  CA  . ALA   D 1 74  ? 22.759  -33.131 15.193  1.00 57.53  ? 389 ALA   D CA  1 
ATOM   3101 C  C   . ALA   D 1 74  ? 21.754  -33.315 14.057  1.00 58.40  ? 389 ALA   D C   1 
ATOM   3102 O  O   . ALA   D 1 74  ? 21.240  -32.336 13.518  1.00 58.00  ? 389 ALA   D O   1 
ATOM   3103 C  CB  . ALA   D 1 74  ? 22.069  -32.732 16.478  1.00 57.54  ? 389 ALA   D CB  1 
ATOM   3104 N  N   . GLN   D 1 75  ? 21.471  -34.584 13.724  1.00 58.94  ? 390 GLN   D N   1 
ATOM   3105 C  CA  . GLN   D 1 75  ? 20.649  -34.938 12.578  1.00 59.51  ? 390 GLN   D CA  1 
ATOM   3106 C  C   . GLN   D 1 75  ? 19.561  -35.927 12.977  1.00 57.22  ? 390 GLN   D C   1 
ATOM   3107 O  O   . GLN   D 1 75  ? 19.785  -36.782 13.828  1.00 57.81  ? 390 GLN   D O   1 
ATOM   3108 C  CB  . GLN   D 1 75  ? 21.455  -35.657 11.498  1.00 62.91  ? 390 GLN   D CB  1 
ATOM   3109 C  CG  . GLN   D 1 75  ? 22.260  -34.737 10.588  1.00 65.79  ? 390 GLN   D CG  1 
ATOM   3110 C  CD  . GLN   D 1 75  ? 22.889  -35.478 9.428   1.00 68.79  ? 390 GLN   D CD  1 
ATOM   3111 O  OE1 . GLN   D 1 75  ? 22.819  -36.709 9.335   1.00 70.28  ? 390 GLN   D OE1 1 
ATOM   3112 N  NE2 . GLN   D 1 75  ? 23.512  -34.731 8.528   1.00 70.21  ? 390 GLN   D NE2 1 
ATOM   3113 N  N   . CYS   D 1 76  ? 18.407  -35.827 12.308  1.00 55.27  ? 391 CYS   D N   1 
ATOM   3114 C  CA  . CYS   D 1 76  ? 17.341  -36.805 12.441  1.00 54.90  ? 391 CYS   D CA  1 
ATOM   3115 C  C   . CYS   D 1 76  ? 17.868  -38.187 12.060  1.00 56.52  ? 391 CYS   D C   1 
ATOM   3116 O  O   . CYS   D 1 76  ? 18.506  -38.334 11.022  1.00 57.62  ? 391 CYS   D O   1 
ATOM   3117 C  CB  . CYS   D 1 76  ? 16.154  -36.435 11.559  1.00 53.50  ? 391 CYS   D CB  1 
ATOM   3118 S  SG  . CYS   D 1 76  ? 14.760  -37.584 11.693  1.00 51.77  ? 391 CYS   D SG  1 
ATOM   3119 N  N   . LYS   D 1 77  ? 17.603  -39.183 12.917  1.00 59.55  ? 392 LYS   D N   1 
ATOM   3120 C  CA  . LYS   D 1 77  ? 17.973  -40.571 12.672  1.00 60.44  ? 392 LYS   D CA  1 
ATOM   3121 C  C   . LYS   D 1 77  ? 17.415  -41.067 11.341  1.00 60.59  ? 392 LYS   D C   1 
ATOM   3122 O  O   . LYS   D 1 77  ? 18.071  -41.837 10.647  1.00 60.87  ? 392 LYS   D O   1 
ATOM   3123 C  CB  . LYS   D 1 77  ? 17.386  -41.531 13.712  1.00 62.75  ? 392 LYS   D CB  1 
ATOM   3124 C  CG  . LYS   D 1 77  ? 18.286  -42.012 14.837  1.00 64.79  ? 392 LYS   D CG  1 
ATOM   3125 C  CD  . LYS   D 1 77  ? 17.511  -42.964 15.742  1.00 67.44  ? 392 LYS   D CD  1 
ATOM   3126 C  CE  . LYS   D 1 77  ? 18.350  -43.802 16.648  1.00 69.80  ? 392 LYS   D CE  1 
ATOM   3127 N  NZ  . LYS   D 1 77  ? 17.502  -44.726 17.408  1.00 71.11  ? 392 LYS   D NZ  1 
ATOM   3128 N  N   . ILE   D 1 78  ? 16.187  -40.648 11.019  1.00 61.21  ? 393 ILE   D N   1 
ATOM   3129 C  CA  . ILE   D 1 78  ? 15.426  -41.248 9.936   1.00 61.33  ? 393 ILE   D CA  1 
ATOM   3130 C  C   . ILE   D 1 78  ? 15.784  -40.571 8.616   1.00 60.01  ? 393 ILE   D C   1 
ATOM   3131 O  O   . ILE   D 1 78  ? 16.304  -41.225 7.715   1.00 61.94  ? 393 ILE   D O   1 
ATOM   3132 C  CB  . ILE   D 1 78  ? 13.917  -41.181 10.236  1.00 61.83  ? 393 ILE   D CB  1 
ATOM   3133 C  CG1 . ILE   D 1 78  ? 13.599  -41.700 11.643  1.00 61.22  ? 393 ILE   D CG1 1 
ATOM   3134 C  CG2 . ILE   D 1 78  ? 13.109  -41.914 9.164   1.00 62.38  ? 393 ILE   D CG2 1 
ATOM   3135 C  CD1 . ILE   D 1 78  ? 14.293  -43.003 12.000  1.00 61.07  ? 393 ILE   D CD1 1 
ATOM   3136 N  N   . CYS   D 1 79  ? 15.505  -39.264 8.516   1.00 58.57  ? 394 CYS   D N   1 
ATOM   3137 C  CA  . CYS   D 1 79  ? 15.568  -38.556 7.246   1.00 57.86  ? 394 CYS   D CA  1 
ATOM   3138 C  C   . CYS   D 1 79  ? 16.866  -37.760 7.097   1.00 57.43  ? 394 CYS   D C   1 
ATOM   3139 O  O   . CYS   D 1 79  ? 17.068  -37.122 6.066   1.00 58.89  ? 394 CYS   D O   1 
ATOM   3140 C  CB  . CYS   D 1 79  ? 14.357  -37.645 7.075   1.00 57.83  ? 394 CYS   D CB  1 
ATOM   3141 S  SG  . CYS   D 1 79  ? 14.346  -36.225 8.200   1.00 58.83  ? 394 CYS   D SG  1 
ATOM   3142 N  N   . ALA   D 1 80  ? 17.725  -37.780 8.129   1.00 56.54  ? 395 ALA   D N   1 
ATOM   3143 C  CA  . ALA   D 1 80  ? 19.031  -37.132 8.102   1.00 55.89  ? 395 ALA   D CA  1 
ATOM   3144 C  C   . ALA   D 1 80  ? 18.913  -35.611 8.009   1.00 55.60  ? 395 ALA   D C   1 
ATOM   3145 O  O   . ALA   D 1 80  ? 19.882  -34.942 7.657   1.00 53.02  ? 395 ALA   D O   1 
ATOM   3146 C  CB  . ALA   D 1 80  ? 19.868  -37.677 6.966   1.00 55.64  ? 395 ALA   D CB  1 
ATOM   3147 N  N   . SER   D 1 81  ? 17.736  -35.069 8.342   1.00 57.38  ? 396 SER   D N   1 
ATOM   3148 C  CA  . SER   D 1 81  ? 17.530  -33.631 8.354   1.00 58.84  ? 396 SER   D CA  1 
ATOM   3149 C  C   . SER   D 1 81  ? 18.302  -33.023 9.521   1.00 60.75  ? 396 SER   D C   1 
ATOM   3150 O  O   . SER   D 1 81  ? 18.250  -33.547 10.632  1.00 61.63  ? 396 SER   D O   1 
ATOM   3151 C  CB  . SER   D 1 81  ? 16.063  -33.297 8.434   1.00 58.66  ? 396 SER   D CB  1 
ATOM   3152 O  OG  . SER   D 1 81  ? 15.856  -31.892 8.451   1.00 59.02  ? 396 SER   D OG  1 
ATOM   3153 N  N   . HIS   D 1 82  ? 19.031  -31.932 9.251   1.00 62.29  ? 397 HIS   D N   1 
ATOM   3154 C  CA  . HIS   D 1 82  ? 19.735  -31.195 10.288  1.00 64.23  ? 397 HIS   D CA  1 
ATOM   3155 C  C   . HIS   D 1 82  ? 18.701  -30.527 11.192  1.00 63.23  ? 397 HIS   D C   1 
ATOM   3156 O  O   . HIS   D 1 82  ? 17.927  -29.691 10.733  1.00 63.92  ? 397 HIS   D O   1 
ATOM   3157 C  CB  . HIS   D 1 82  ? 20.725  -30.204 9.661   1.00 67.33  ? 397 HIS   D CB  1 
ATOM   3158 C  CG  . HIS   D 1 82  ? 21.316  -29.196 10.600  1.00 71.92  ? 397 HIS   D CG  1 
ATOM   3159 N  ND1 . HIS   D 1 82  ? 22.641  -28.826 10.510  1.00 73.63  ? 397 HIS   D ND1 1 
ATOM   3160 C  CD2 . HIS   D 1 82  ? 20.805  -28.477 11.617  1.00 73.55  ? 397 HIS   D CD2 1 
ATOM   3161 C  CE1 . HIS   D 1 82  ? 22.911  -27.924 11.443  1.00 74.20  ? 397 HIS   D CE1 1 
ATOM   3162 N  NE2 . HIS   D 1 82  ? 21.810  -27.696 12.125  1.00 74.26  ? 397 HIS   D NE2 1 
ATOM   3163 N  N   . ILE   D 1 83  ? 18.707  -30.905 12.477  1.00 61.67  ? 398 ILE   D N   1 
ATOM   3164 C  CA  . ILE   D 1 83  ? 17.749  -30.390 13.443  1.00 61.36  ? 398 ILE   D CA  1 
ATOM   3165 C  C   . ILE   D 1 83  ? 18.418  -29.326 14.312  1.00 61.04  ? 398 ILE   D C   1 
ATOM   3166 O  O   . ILE   D 1 83  ? 17.802  -28.308 14.616  1.00 60.99  ? 398 ILE   D O   1 
ATOM   3167 C  CB  . ILE   D 1 83  ? 17.148  -31.529 14.291  1.00 62.20  ? 398 ILE   D CB  1 
ATOM   3168 C  CG1 . ILE   D 1 83  ? 16.472  -32.605 13.427  1.00 62.96  ? 398 ILE   D CG1 1 
ATOM   3169 C  CG2 . ILE   D 1 83  ? 16.185  -30.978 15.345  1.00 62.52  ? 398 ILE   D CG2 1 
ATOM   3170 C  CD1 . ILE   D 1 83  ? 15.221  -32.143 12.698  1.00 63.13  ? 398 ILE   D CD1 1 
ATOM   3171 N  N   . GLY   D 1 84  ? 19.667  -29.570 14.730  1.00 60.25  ? 399 GLY   D N   1 
ATOM   3172 C  CA  . GLY   D 1 84  ? 20.379  -28.619 15.569  1.00 58.99  ? 399 GLY   D CA  1 
ATOM   3173 C  C   . GLY   D 1 84  ? 21.780  -29.105 15.933  1.00 57.98  ? 399 GLY   D C   1 
ATOM   3174 O  O   . GLY   D 1 84  ? 22.430  -29.778 15.136  1.00 58.70  ? 399 GLY   D O   1 
ATOM   3175 N  N   . TRP   D 1 85  ? 22.231  -28.738 17.140  1.00 57.36  ? 400 TRP   D N   1 
ATOM   3176 C  CA  . TRP   D 1 85  ? 23.540  -29.118 17.648  1.00 57.22  ? 400 TRP   D CA  1 
ATOM   3177 C  C   . TRP   D 1 85  ? 23.413  -29.648 19.074  1.00 56.95  ? 400 TRP   D C   1 
ATOM   3178 O  O   . TRP   D 1 85  ? 22.440  -29.355 19.768  1.00 56.64  ? 400 TRP   D O   1 
ATOM   3179 C  CB  . TRP   D 1 85  ? 24.510  -27.928 17.625  1.00 57.39  ? 400 TRP   D CB  1 
ATOM   3180 C  CG  . TRP   D 1 85  ? 24.620  -27.233 16.295  1.00 58.23  ? 400 TRP   D CG  1 
ATOM   3181 C  CD1 . TRP   D 1 85  ? 25.622  -27.352 15.376  1.00 58.46  ? 400 TRP   D CD1 1 
ATOM   3182 C  CD2 . TRP   D 1 85  ? 23.671  -26.300 15.738  1.00 59.05  ? 400 TRP   D CD2 1 
ATOM   3183 N  NE1 . TRP   D 1 85  ? 25.367  -26.557 14.291  1.00 58.76  ? 400 TRP   D NE1 1 
ATOM   3184 C  CE2 . TRP   D 1 85  ? 24.178  -25.902 14.481  1.00 59.32  ? 400 TRP   D CE2 1 
ATOM   3185 C  CE3 . TRP   D 1 85  ? 22.452  -25.769 16.175  1.00 59.12  ? 400 TRP   D CE3 1 
ATOM   3186 C  CZ2 . TRP   D 1 85  ? 23.503  -24.997 13.665  1.00 59.68  ? 400 TRP   D CZ2 1 
ATOM   3187 C  CZ3 . TRP   D 1 85  ? 21.786  -24.877 15.364  1.00 60.07  ? 400 TRP   D CZ3 1 
ATOM   3188 C  CH2 . TRP   D 1 85  ? 22.307  -24.497 14.128  1.00 59.79  ? 400 TRP   D CH2 1 
ATOM   3189 N  N   . LYS   D 1 86  ? 24.424  -30.416 19.496  1.00 56.14  ? 401 LYS   D N   1 
ATOM   3190 C  CA  . LYS   D 1 86  ? 24.562  -30.846 20.877  1.00 55.56  ? 401 LYS   D CA  1 
ATOM   3191 C  C   . LYS   D 1 86  ? 25.730  -30.093 21.505  1.00 55.76  ? 401 LYS   D C   1 
ATOM   3192 O  O   . LYS   D 1 86  ? 26.833  -30.110 20.963  1.00 57.72  ? 401 LYS   D O   1 
ATOM   3193 C  CB  . LYS   D 1 86  ? 24.826  -32.351 20.966  1.00 55.57  ? 401 LYS   D CB  1 
ATOM   3194 C  CG  . LYS   D 1 86  ? 24.928  -32.895 22.385  1.00 56.26  ? 401 LYS   D CG  1 
ATOM   3195 C  CD  . LYS   D 1 86  ? 25.264  -34.378 22.457  1.00 56.55  ? 401 LYS   D CD  1 
ATOM   3196 C  CE  . LYS   D 1 86  ? 25.348  -34.876 23.863  1.00 57.40  ? 401 LYS   D CE  1 
ATOM   3197 N  NZ  . LYS   D 1 86  ? 25.722  -36.292 23.900  1.00 58.13  ? 401 LYS   D NZ  1 
ATOM   3198 N  N   . PHE   D 1 87  ? 25.475  -29.451 22.651  1.00 54.29  ? 402 PHE   D N   1 
ATOM   3199 C  CA  . PHE   D 1 87  ? 26.487  -28.660 23.331  1.00 53.10  ? 402 PHE   D CA  1 
ATOM   3200 C  C   . PHE   D 1 87  ? 27.049  -29.456 24.505  1.00 53.78  ? 402 PHE   D C   1 
ATOM   3201 O  O   . PHE   D 1 87  ? 26.294  -30.027 25.286  1.00 53.67  ? 402 PHE   D O   1 
ATOM   3202 C  CB  . PHE   D 1 87  ? 25.894  -27.309 23.741  1.00 52.06  ? 402 PHE   D CB  1 
ATOM   3203 C  CG  . PHE   D 1 87  ? 25.684  -26.381 22.553  1.00 50.66  ? 402 PHE   D CG  1 
ATOM   3204 C  CD1 . PHE   D 1 87  ? 26.730  -25.604 22.067  1.00 49.77  ? 402 PHE   D CD1 1 
ATOM   3205 C  CD2 . PHE   D 1 87  ? 24.452  -26.309 21.910  1.00 49.68  ? 402 PHE   D CD2 1 
ATOM   3206 C  CE1 . PHE   D 1 87  ? 26.543  -24.767 20.978  1.00 49.25  ? 402 PHE   D CE1 1 
ATOM   3207 C  CE2 . PHE   D 1 87  ? 24.271  -25.472 20.820  1.00 48.92  ? 402 PHE   D CE2 1 
ATOM   3208 C  CZ  . PHE   D 1 87  ? 25.316  -24.703 20.356  1.00 49.11  ? 402 PHE   D CZ  1 
ATOM   3209 N  N   . THR   D 1 88  ? 28.385  -29.475 24.604  1.00 54.59  ? 403 THR   D N   1 
ATOM   3210 C  CA  . THR   D 1 88  ? 29.096  -30.225 25.626  1.00 55.60  ? 403 THR   D CA  1 
ATOM   3211 C  C   . THR   D 1 88  ? 30.111  -29.305 26.301  1.00 56.55  ? 403 THR   D C   1 
ATOM   3212 O  O   . THR   D 1 88  ? 30.891  -28.638 25.626  1.00 56.46  ? 403 THR   D O   1 
ATOM   3213 C  CB  . THR   D 1 88  ? 29.771  -31.438 24.986  1.00 56.47  ? 403 THR   D CB  1 
ATOM   3214 O  OG1 . THR   D 1 88  ? 30.499  -30.941 23.867  1.00 57.37  ? 403 THR   D OG1 1 
ATOM   3215 C  CG2 . THR   D 1 88  ? 28.773  -32.480 24.516  1.00 56.70  ? 403 THR   D CG2 1 
ATOM   3216 N  N   . ALA   D 1 89  ? 30.091  -29.289 27.640  1.00 58.62  ? 404 ALA   D N   1 
ATOM   3217 C  CA  . ALA   D 1 89  ? 30.968  -28.439 28.429  1.00 60.08  ? 404 ALA   D CA  1 
ATOM   3218 C  C   . ALA   D 1 89  ? 32.422  -28.864 28.239  1.00 61.70  ? 404 ALA   D C   1 
ATOM   3219 O  O   . ALA   D 1 89  ? 32.701  -30.028 27.961  1.00 61.77  ? 404 ALA   D O   1 
ATOM   3220 C  CB  . ALA   D 1 89  ? 30.559  -28.498 29.886  1.00 60.28  ? 404 ALA   D CB  1 
ATOM   3221 N  N   . THR   D 1 90  ? 33.341  -27.905 28.402  1.00 64.26  ? 405 THR   D N   1 
ATOM   3222 C  CA  . THR   D 1 90  ? 34.751  -28.127 28.122  1.00 67.03  ? 405 THR   D CA  1 
ATOM   3223 C  C   . THR   D 1 90  ? 35.534  -28.370 29.413  1.00 70.65  ? 405 THR   D C   1 
ATOM   3224 O  O   . THR   D 1 90  ? 36.708  -28.730 29.350  1.00 71.13  ? 405 THR   D O   1 
ATOM   3225 C  CB  . THR   D 1 90  ? 35.305  -26.939 27.336  1.00 67.18  ? 405 THR   D CB  1 
ATOM   3226 O  OG1 . THR   D 1 90  ? 34.988  -25.771 28.087  1.00 67.52  ? 405 THR   D OG1 1 
ATOM   3227 C  CG2 . THR   D 1 90  ? 34.708  -26.842 25.943  1.00 66.96  ? 405 THR   D CG2 1 
ATOM   3228 N  N   . LYS   D 1 91  ? 34.890  -28.167 30.573  1.00 75.05  ? 406 LYS   D N   1 
ATOM   3229 C  CA  . LYS   D 1 91  ? 35.486  -28.494 31.861  1.00 78.74  ? 406 LYS   D CA  1 
ATOM   3230 C  C   . LYS   D 1 91  ? 34.441  -29.154 32.756  1.00 77.90  ? 406 LYS   D C   1 
ATOM   3231 O  O   . LYS   D 1 91  ? 33.245  -28.906 32.612  1.00 76.71  ? 406 LYS   D O   1 
ATOM   3232 C  CB  . LYS   D 1 91  ? 36.065  -27.250 32.544  1.00 82.03  ? 406 LYS   D CB  1 
ATOM   3233 C  CG  . LYS   D 1 91  ? 37.306  -26.666 31.881  1.00 85.52  ? 406 LYS   D CG  1 
ATOM   3234 C  CD  . LYS   D 1 91  ? 37.436  -25.149 31.955  1.00 88.33  ? 406 LYS   D CD  1 
ATOM   3235 C  CE  . LYS   D 1 91  ? 36.355  -24.423 31.208  1.00 91.44  ? 406 LYS   D CE  1 
ATOM   3236 N  NZ  . LYS   D 1 91  ? 35.222  -24.028 32.052  1.00 93.34  ? 406 LYS   D NZ  1 
ATOM   3237 N  N   . LYS   D 1 92  ? 34.924  -29.961 33.710  1.00 76.93  ? 407 LYS   D N   1 
ATOM   3238 C  CA  . LYS   D 1 92  ? 34.088  -30.882 34.463  1.00 75.56  ? 407 LYS   D CA  1 
ATOM   3239 C  C   . LYS   D 1 92  ? 33.275  -30.159 35.538  1.00 76.69  ? 407 LYS   D C   1 
ATOM   3240 O  O   . LYS   D 1 92  ? 32.439  -30.784 36.186  1.00 78.40  ? 407 LYS   D O   1 
ATOM   3241 C  CB  . LYS   D 1 92  ? 34.960  -31.965 35.110  1.00 73.47  ? 407 LYS   D CB  1 
ATOM   3242 N  N   . ASP   D 1 93  ? 33.515  -28.854 35.721  1.00 76.71  ? 408 ASP   D N   1 
ATOM   3243 C  CA  . ASP   D 1 93  ? 32.901  -28.097 36.803  1.00 77.21  ? 408 ASP   D CA  1 
ATOM   3244 C  C   . ASP   D 1 93  ? 31.633  -27.382 36.339  1.00 73.83  ? 408 ASP   D C   1 
ATOM   3245 O  O   . ASP   D 1 93  ? 30.846  -26.941 37.173  1.00 74.03  ? 408 ASP   D O   1 
ATOM   3246 C  CB  . ASP   D 1 93  ? 33.879  -27.102 37.408  1.00 80.91  ? 408 ASP   D CB  1 
ATOM   3247 C  CG  . ASP   D 1 93  ? 34.500  -26.117 36.429  1.00 85.47  ? 408 ASP   D CG  1 
ATOM   3248 O  OD1 . ASP   D 1 93  ? 35.266  -26.569 35.553  1.00 89.04  ? 408 ASP   D OD1 1 
ATOM   3249 O  OD2 . ASP   D 1 93  ? 34.205  -24.908 36.544  1.00 88.53  ? 408 ASP   D OD2 1 
ATOM   3250 N  N   . MET   D 1 94  ? 31.438  -27.258 35.020  1.00 71.43  ? 409 MET   D N   1 
ATOM   3251 C  CA  . MET   D 1 94  ? 30.315  -26.508 34.475  1.00 69.45  ? 409 MET   D CA  1 
ATOM   3252 C  C   . MET   D 1 94  ? 29.010  -27.267 34.709  1.00 67.39  ? 409 MET   D C   1 
ATOM   3253 O  O   . MET   D 1 94  ? 29.020  -28.453 35.028  1.00 68.09  ? 409 MET   D O   1 
ATOM   3254 C  CB  . MET   D 1 94  ? 30.498  -26.258 32.975  1.00 69.61  ? 409 MET   D CB  1 
ATOM   3255 C  CG  . MET   D 1 94  ? 31.656  -25.335 32.644  1.00 69.82  ? 409 MET   D CG  1 
ATOM   3256 S  SD  . MET   D 1 94  ? 31.977  -25.210 30.874  1.00 70.20  ? 409 MET   D SD  1 
ATOM   3257 C  CE  . MET   D 1 94  ? 30.387  -24.651 30.248  1.00 68.55  ? 409 MET   D CE  1 
ATOM   3258 N  N   . SER   D 1 95  ? 27.888  -26.558 34.550  1.00 63.81  ? 410 SER   D N   1 
ATOM   3259 C  CA  . SER   D 1 95  ? 26.569  -27.141 34.732  1.00 62.47  ? 410 SER   D CA  1 
ATOM   3260 C  C   . SER   D 1 95  ? 25.484  -26.346 34.009  1.00 61.35  ? 410 SER   D C   1 
ATOM   3261 O  O   . SER   D 1 95  ? 25.339  -25.152 34.260  1.00 61.17  ? 410 SER   D O   1 
ATOM   3262 C  CB  . SER   D 1 95  ? 26.249  -27.271 36.199  1.00 63.72  ? 410 SER   D CB  1 
ATOM   3263 O  OG  . SER   D 1 95  ? 25.096  -28.077 36.400  1.00 64.93  ? 410 SER   D OG  1 
ATOM   3264 N  N   . PRO   D 1 96  ? 24.685  -26.956 33.098  1.00 59.92  ? 411 PRO   D N   1 
ATOM   3265 C  CA  . PRO   D 1 96  ? 24.750  -28.388 32.819  1.00 58.77  ? 411 PRO   D CA  1 
ATOM   3266 C  C   . PRO   D 1 96  ? 25.995  -28.792 32.037  1.00 58.99  ? 411 PRO   D C   1 
ATOM   3267 O  O   . PRO   D 1 96  ? 26.708  -27.939 31.513  1.00 58.73  ? 411 PRO   D O   1 
ATOM   3268 C  CB  . PRO   D 1 96  ? 23.473  -28.660 32.029  1.00 57.91  ? 411 PRO   D CB  1 
ATOM   3269 C  CG  . PRO   D 1 96  ? 23.193  -27.335 31.346  1.00 58.59  ? 411 PRO   D CG  1 
ATOM   3270 C  CD  . PRO   D 1 96  ? 23.679  -26.263 32.277  1.00 59.05  ? 411 PRO   D CD  1 
ATOM   3271 N  N   . GLN   D 1 97  ? 26.248  -30.103 31.981  1.00 59.44  ? 412 GLN   D N   1 
ATOM   3272 C  CA  . GLN   D 1 97  ? 27.394  -30.636 31.263  1.00 59.82  ? 412 GLN   D CA  1 
ATOM   3273 C  C   . GLN   D 1 97  ? 27.063  -30.754 29.777  1.00 59.53  ? 412 GLN   D C   1 
ATOM   3274 O  O   . GLN   D 1 97  ? 27.951  -30.609 28.940  1.00 58.40  ? 412 GLN   D O   1 
ATOM   3275 C  CB  . GLN   D 1 97  ? 27.852  -31.964 31.868  1.00 59.96  ? 412 GLN   D CB  1 
ATOM   3276 C  CG  . GLN   D 1 97  ? 28.699  -31.803 33.125  1.00 60.12  ? 412 GLN   D CG  1 
ATOM   3277 C  CD  . GLN   D 1 97  ? 30.062  -31.205 32.848  1.00 60.05  ? 412 GLN   D CD  1 
ATOM   3278 O  OE1 . GLN   D 1 97  ? 30.366  -30.075 33.246  1.00 60.88  ? 412 GLN   D OE1 1 
ATOM   3279 N  NE2 . GLN   D 1 97  ? 30.897  -31.957 32.144  1.00 59.04  ? 412 GLN   D NE2 1 
ATOM   3280 N  N   . LYS   D 1 98  ? 25.790  -31.019 29.455  1.00 60.12  ? 413 LYS   D N   1 
ATOM   3281 C  CA  . LYS   D 1 98  ? 25.368  -31.060 28.065  1.00 61.07  ? 413 LYS   D CA  1 
ATOM   3282 C  C   . LYS   D 1 98  ? 23.898  -30.666 27.938  1.00 57.59  ? 413 LYS   D C   1 
ATOM   3283 O  O   . LYS   D 1 98  ? 23.114  -30.812 28.873  1.00 56.60  ? 413 LYS   D O   1 
ATOM   3284 C  CB  . LYS   D 1 98  ? 25.682  -32.420 27.427  1.00 63.94  ? 413 LYS   D CB  1 
ATOM   3285 C  CG  . LYS   D 1 98  ? 24.961  -33.645 27.987  1.00 66.93  ? 413 LYS   D CG  1 
ATOM   3286 C  CD  . LYS   D 1 98  ? 23.591  -33.937 27.383  1.00 69.44  ? 413 LYS   D CD  1 
ATOM   3287 C  CE  . LYS   D 1 98  ? 23.114  -35.323 27.703  1.00 70.86  ? 413 LYS   D CE  1 
ATOM   3288 N  NZ  . LYS   D 1 98  ? 21.744  -35.561 27.241  1.00 71.25  ? 413 LYS   D NZ  1 
ATOM   3289 N  N   . PHE   D 1 99  ? 23.562  -30.145 26.753  1.00 54.89  ? 414 PHE   D N   1 
ATOM   3290 C  CA  . PHE   D 1 99  ? 22.203  -29.789 26.386  1.00 53.06  ? 414 PHE   D CA  1 
ATOM   3291 C  C   . PHE   D 1 99  ? 22.146  -29.705 24.863  1.00 51.76  ? 414 PHE   D C   1 
ATOM   3292 O  O   . PHE   D 1 99  ? 23.149  -29.945 24.194  1.00 50.48  ? 414 PHE   D O   1 
ATOM   3293 C  CB  . PHE   D 1 99  ? 21.805  -28.474 27.062  1.00 52.56  ? 414 PHE   D CB  1 
ATOM   3294 C  CG  . PHE   D 1 99  ? 22.529  -27.248 26.521  1.00 52.45  ? 414 PHE   D CG  1 
ATOM   3295 C  CD1 . PHE   D 1 99  ? 23.745  -26.841 27.061  1.00 52.09  ? 414 PHE   D CD1 1 
ATOM   3296 C  CD2 . PHE   D 1 99  ? 21.994  -26.508 25.472  1.00 52.13  ? 414 PHE   D CD2 1 
ATOM   3297 C  CE1 . PHE   D 1 99  ? 24.403  -25.725 26.565  1.00 51.52  ? 414 PHE   D CE1 1 
ATOM   3298 C  CE2 . PHE   D 1 99  ? 22.657  -25.394 24.979  1.00 51.94  ? 414 PHE   D CE2 1 
ATOM   3299 C  CZ  . PHE   D 1 99  ? 23.859  -25.005 25.526  1.00 51.63  ? 414 PHE   D CZ  1 
ATOM   3300 N  N   . TRP   D 1 100 ? 20.974  -29.348 24.328  1.00 51.28  ? 415 TRP   D N   1 
ATOM   3301 C  CA  . TRP   D 1 100 ? 20.775  -29.288 22.890  1.00 51.82  ? 415 TRP   D CA  1 
ATOM   3302 C  C   . TRP   D 1 100 ? 20.206  -27.927 22.502  1.00 52.03  ? 415 TRP   D C   1 
ATOM   3303 O  O   . TRP   D 1 100 ? 19.285  -27.436 23.151  1.00 51.31  ? 415 TRP   D O   1 
ATOM   3304 C  CB  . TRP   D 1 100 ? 19.839  -30.420 22.443  1.00 52.83  ? 415 TRP   D CB  1 
ATOM   3305 C  CG  . TRP   D 1 100 ? 20.240  -31.785 22.939  1.00 54.45  ? 415 TRP   D CG  1 
ATOM   3306 C  CD1 . TRP   D 1 100 ? 20.115  -32.260 24.212  1.00 54.92  ? 415 TRP   D CD1 1 
ATOM   3307 C  CD2 . TRP   D 1 100 ? 20.805  -32.866 22.162  1.00 53.95  ? 415 TRP   D CD2 1 
ATOM   3308 N  NE1 . TRP   D 1 100 ? 20.579  -33.546 24.290  1.00 54.47  ? 415 TRP   D NE1 1 
ATOM   3309 C  CE2 . TRP   D 1 100 ? 21.002  -33.948 23.050  1.00 53.90  ? 415 TRP   D CE2 1 
ATOM   3310 C  CE3 . TRP   D 1 100 ? 21.164  -33.025 20.818  1.00 53.65  ? 415 TRP   D CE3 1 
ATOM   3311 C  CZ2 . TRP   D 1 100 ? 21.541  -35.164 22.633  1.00 53.41  ? 415 TRP   D CZ2 1 
ATOM   3312 C  CZ3 . TRP   D 1 100 ? 21.692  -34.231 20.407  1.00 53.52  ? 415 TRP   D CZ3 1 
ATOM   3313 C  CH2 . TRP   D 1 100 ? 21.877  -35.283 21.304  1.00 53.26  ? 415 TRP   D CH2 1 
ATOM   3314 N  N   . GLY   D 1 101 ? 20.783  -27.327 21.451  1.00 52.15  ? 416 GLY   D N   1 
ATOM   3315 C  CA  . GLY   D 1 101 ? 20.212  -26.161 20.795  1.00 52.03  ? 416 GLY   D CA  1 
ATOM   3316 C  C   . GLY   D 1 101 ? 19.624  -26.555 19.441  1.00 51.96  ? 416 GLY   D C   1 
ATOM   3317 O  O   . GLY   D 1 101 ? 20.345  -27.057 18.583  1.00 53.39  ? 416 GLY   D O   1 
ATOM   3318 N  N   . LEU   D 1 102 ? 18.316  -26.329 19.266  1.00 51.19  ? 417 LEU   D N   1 
ATOM   3319 C  CA  . LEU   D 1 102 ? 17.579  -26.876 18.136  1.00 50.63  ? 417 LEU   D CA  1 
ATOM   3320 C  C   . LEU   D 1 102 ? 17.027  -25.754 17.262  1.00 50.66  ? 417 LEU   D C   1 
ATOM   3321 O  O   . LEU   D 1 102 ? 16.579  -24.730 17.769  1.00 52.05  ? 417 LEU   D O   1 
ATOM   3322 C  CB  . LEU   D 1 102 ? 16.450  -27.761 18.660  1.00 50.88  ? 417 LEU   D CB  1 
ATOM   3323 C  CG  . LEU   D 1 102 ? 16.848  -28.862 19.650  1.00 50.92  ? 417 LEU   D CG  1 
ATOM   3324 C  CD1 . LEU   D 1 102 ? 15.629  -29.694 20.009  1.00 50.83  ? 417 LEU   D CD1 1 
ATOM   3325 C  CD2 . LEU   D 1 102 ? 17.960  -29.754 19.118  1.00 50.94  ? 417 LEU   D CD2 1 
ATOM   3326 N  N   . THR   D 1 103 ? 17.043  -25.980 15.943  1.00 50.96  ? 418 THR   D N   1 
ATOM   3327 C  CA  . THR   D 1 103 ? 16.417  -25.086 14.983  1.00 51.40  ? 418 THR   D CA  1 
ATOM   3328 C  C   . THR   D 1 103 ? 14.901  -25.219 15.119  1.00 50.69  ? 418 THR   D C   1 
ATOM   3329 O  O   . THR   D 1 103 ? 14.354  -26.296 14.897  1.00 49.00  ? 418 THR   D O   1 
ATOM   3330 C  CB  . THR   D 1 103 ? 16.894  -25.444 13.573  1.00 53.02  ? 418 THR   D CB  1 
ATOM   3331 O  OG1 . THR   D 1 103 ? 18.316  -25.346 13.572  1.00 53.23  ? 418 THR   D OG1 1 
ATOM   3332 C  CG2 . THR   D 1 103 ? 16.324  -24.531 12.503  1.00 53.48  ? 418 THR   D CG2 1 
ATOM   3333 N  N   . ARG   D 1 104 ? 14.232  -24.115 15.477  1.00 52.13  ? 419 ARG   D N   1 
ATOM   3334 C  CA  . ARG   D 1 104 ? 12.799  -24.124 15.728  1.00 53.73  ? 419 ARG   D CA  1 
ATOM   3335 C  C   . ARG   D 1 104 ? 12.031  -24.406 14.437  1.00 54.50  ? 419 ARG   D C   1 
ATOM   3336 O  O   . ARG   D 1 104 ? 10.948  -24.986 14.477  1.00 53.86  ? 419 ARG   D O   1 
ATOM   3337 C  CB  . ARG   D 1 104 ? 12.332  -22.802 16.348  1.00 54.96  ? 419 ARG   D CB  1 
ATOM   3338 C  CG  . ARG   D 1 104 ? 12.946  -22.520 17.711  1.00 56.51  ? 419 ARG   D CG  1 
ATOM   3339 C  CD  . ARG   D 1 104 ? 12.118  -21.560 18.554  1.00 58.68  ? 419 ARG   D CD  1 
ATOM   3340 N  NE  . ARG   D 1 104 ? 12.006  -20.216 17.975  1.00 61.18  ? 419 ARG   D NE  1 
ATOM   3341 C  CZ  . ARG   D 1 104 ? 12.727  -19.150 18.325  1.00 63.07  ? 419 ARG   D CZ  1 
ATOM   3342 N  NH1 . ARG   D 1 104 ? 13.752  -19.268 19.153  1.00 64.44  ? 419 ARG   D NH1 1 
ATOM   3343 N  NH2 . ARG   D 1 104 ? 12.448  -17.965 17.807  1.00 62.58  ? 419 ARG   D NH2 1 
ATOM   3344 N  N   . SER   D 1 105 ? 12.608  -24.003 13.298  1.00 55.89  ? 420 SER   D N   1 
ATOM   3345 C  CA  . SER   D 1 105 ? 11.975  -24.180 12.001  1.00 56.47  ? 420 SER   D CA  1 
ATOM   3346 C  C   . SER   D 1 105 ? 12.117  -25.619 11.505  1.00 56.71  ? 420 SER   D C   1 
ATOM   3347 O  O   . SER   D 1 105 ? 11.617  -25.940 10.430  1.00 58.18  ? 420 SER   D O   1 
ATOM   3348 C  CB  . SER   D 1 105 ? 12.540  -23.211 10.991  1.00 57.53  ? 420 SER   D CB  1 
ATOM   3349 O  OG  . SER   D 1 105 ? 13.863  -23.571 10.615  1.00 58.81  ? 420 SER   D OG  1 
ATOM   3350 N  N   . ALA   D 1 106 ? 12.801  -26.475 12.279  1.00 56.78  ? 421 ALA   D N   1 
ATOM   3351 C  CA  . ALA   D 1 106 ? 13.027  -27.860 11.894  1.00 56.71  ? 421 ALA   D CA  1 
ATOM   3352 C  C   . ALA   D 1 106 ? 12.153  -28.811 12.712  1.00 57.89  ? 421 ALA   D C   1 
ATOM   3353 O  O   . ALA   D 1 106 ? 12.356  -30.023 12.659  1.00 58.28  ? 421 ALA   D O   1 
ATOM   3354 C  CB  . ALA   D 1 106 ? 14.493  -28.195 12.063  1.00 55.89  ? 421 ALA   D CB  1 
ATOM   3355 N  N   . LEU   D 1 107 ? 11.178  -28.264 13.451  1.00 59.41  ? 422 LEU   D N   1 
ATOM   3356 C  CA  . LEU   D 1 107 ? 10.400  -29.044 14.402  1.00 60.75  ? 422 LEU   D CA  1 
ATOM   3357 C  C   . LEU   D 1 107 ? 8.911   -28.765 14.221  1.00 61.92  ? 422 LEU   D C   1 
ATOM   3358 O  O   . LEU   D 1 107 ? 8.530   -27.812 13.545  1.00 62.44  ? 422 LEU   D O   1 
ATOM   3359 C  CB  . LEU   D 1 107 ? 10.868  -28.718 15.820  1.00 60.95  ? 422 LEU   D CB  1 
ATOM   3360 C  CG  . LEU   D 1 107 ? 12.291  -29.163 16.177  1.00 60.63  ? 422 LEU   D CG  1 
ATOM   3361 C  CD1 . LEU   D 1 107 ? 12.742  -28.543 17.489  1.00 60.34  ? 422 LEU   D CD1 1 
ATOM   3362 C  CD2 . LEU   D 1 107 ? 12.391  -30.679 16.246  1.00 60.62  ? 422 LEU   D CD2 1 
ATOM   3363 N  N   . LEU   D 1 108 ? 8.081   -29.613 14.842  1.00 64.35  ? 423 LEU   D N   1 
ATOM   3364 C  CA  . LEU   D 1 108 ? 6.634   -29.509 14.749  1.00 68.30  ? 423 LEU   D CA  1 
ATOM   3365 C  C   . LEU   D 1 108 ? 5.919   -29.798 16.067  1.00 72.06  ? 423 LEU   D C   1 
ATOM   3366 O  O   . LEU   D 1 108 ? 6.144   -30.842 16.675  1.00 71.51  ? 423 LEU   D O   1 
ATOM   3367 C  CB  . LEU   D 1 108 ? 6.129   -30.445 13.652  1.00 68.01  ? 423 LEU   D CB  1 
ATOM   3368 C  CG  . LEU   D 1 108 ? 6.107   -29.879 12.229  1.00 67.49  ? 423 LEU   D CG  1 
ATOM   3369 C  CD1 . LEU   D 1 108 ? 5.659   -30.958 11.260  1.00 68.15  ? 423 LEU   D CD1 1 
ATOM   3370 C  CD2 . LEU   D 1 108 ? 5.204   -28.661 12.116  1.00 67.36  ? 423 LEU   D CD2 1 
ATOM   3371 N  N   . PRO   D 1 109 ? 5.021   -28.904 16.543  1.00 77.04  ? 424 PRO   D N   1 
ATOM   3372 C  CA  . PRO   D 1 109 ? 4.745   -27.634 15.877  1.00 81.37  ? 424 PRO   D CA  1 
ATOM   3373 C  C   . PRO   D 1 109 ? 5.866   -26.609 16.044  1.00 85.45  ? 424 PRO   D C   1 
ATOM   3374 O  O   . PRO   D 1 109 ? 6.625   -26.669 17.010  1.00 87.14  ? 424 PRO   D O   1 
ATOM   3375 C  CB  . PRO   D 1 109 ? 3.453   -27.166 16.539  1.00 81.20  ? 424 PRO   D CB  1 
ATOM   3376 C  CG  . PRO   D 1 109 ? 3.571   -27.750 17.937  1.00 79.96  ? 424 PRO   D CG  1 
ATOM   3377 C  CD  . PRO   D 1 109 ? 4.209   -29.094 17.755  1.00 77.60  ? 424 PRO   D CD  1 
ATOM   3378 N  N   . THR   D 1 110 ? 5.962   -25.675 15.090  1.00 89.28  ? 425 THR   D N   1 
ATOM   3379 C  CA  . THR   D 1 110 ? 6.911   -24.577 15.184  1.00 92.95  ? 425 THR   D CA  1 
ATOM   3380 C  C   . THR   D 1 110 ? 6.375   -23.560 16.188  1.00 94.31  ? 425 THR   D C   1 
ATOM   3381 O  O   . THR   D 1 110 ? 5.164   -23.382 16.311  1.00 94.58  ? 425 THR   D O   1 
ATOM   3382 C  CB  . THR   D 1 110 ? 7.146   -23.957 13.805  1.00 95.10  ? 425 THR   D CB  1 
ATOM   3383 O  OG1 . THR   D 1 110 ? 7.707   -24.995 13.008  1.00 96.67  ? 425 THR   D OG1 1 
ATOM   3384 C  CG2 . THR   D 1 110 ? 8.104   -22.778 13.840  1.00 95.14  ? 425 THR   D CG2 1 
ATOM   3385 N  N   . ILE   D 1 111 ? 7.298   -22.899 16.895  1.00 95.68  ? 426 ILE   D N   1 
ATOM   3386 C  CA  . ILE   D 1 111 ? 6.962   -22.014 17.998  1.00 96.14  ? 426 ILE   D CA  1 
ATOM   3387 C  C   . ILE   D 1 111 ? 7.975   -20.854 18.037  1.00 96.16  ? 426 ILE   D C   1 
ATOM   3388 O  O   . ILE   D 1 111 ? 8.808   -20.789 17.104  1.00 95.60  ? 426 ILE   D O   1 
ATOM   3389 C  CB  . ILE   D 1 111 ? 6.927   -22.798 19.326  1.00 95.53  ? 426 ILE   D CB  1 
ATOM   3390 C  CG1 . ILE   D 1 111 ? 8.083   -23.800 19.415  1.00 94.40  ? 426 ILE   D CG1 1 
ATOM   3391 C  CG2 . ILE   D 1 111 ? 5.575   -23.488 19.518  1.00 94.48  ? 426 ILE   D CG2 1 
ATOM   3392 C  CD1 . ILE   D 1 111 ? 8.368   -24.305 20.818  1.00 93.82  ? 426 ILE   D CD1 1 
ATOM   3393 O  OXT . ILE   D 1 111 ? 7.890   -20.052 18.993  1.00 95.70  ? 426 ILE   D OXT 1 
HETATM 3394 O  O1  . A1CAW E 2 .   ? -1.595  22.198  41.187  1.00 49.85  ? 501 A1CAW A O1  1 
HETATM 3395 C  C1  . A1CAW E 2 .   ? -0.386  22.347  41.082  1.00 51.11  ? 501 A1CAW A C1  1 
HETATM 3396 N  N1  . A1CAW E 2 .   ? 0.155   23.579  40.791  1.00 50.96  ? 501 A1CAW A N1  1 
HETATM 3397 N  N2  . A1CAW E 2 .   ? 0.463   21.302  41.295  1.00 52.07  ? 501 A1CAW A N2  1 
HETATM 3398 C  C2  . A1CAW E 2 .   ? -0.011  20.039  41.572  1.00 54.30  ? 501 A1CAW A C2  1 
HETATM 3399 C  C3  . A1CAW E 2 .   ? 0.413   19.082  42.496  1.00 55.01  ? 501 A1CAW A C3  1 
HETATM 3400 N  N3  . A1CAW E 2 .   ? -0.254  17.874  42.393  1.00 55.79  ? 501 A1CAW A N3  1 
HETATM 3401 C  C4  . A1CAW E 2 .   ? -1.042  18.029  41.293  1.00 57.14  ? 501 A1CAW A C4  1 
HETATM 3402 N  N4  . A1CAW E 2 .   ? -0.883  19.299  40.757  1.00 56.57  ? 501 A1CAW A N4  1 
HETATM 3403 C  C5  . A1CAW E 2 .   ? -1.578  19.707  39.634  1.00 58.51  ? 501 A1CAW A C5  1 
HETATM 3404 C  C6  . A1CAW E 2 .   ? -2.441  18.875  39.009  1.00 60.19  ? 501 A1CAW A C6  1 
HETATM 3405 C  C7  . A1CAW E 2 .   ? -2.641  17.535  39.530  1.00 61.41  ? 501 A1CAW A C7  1 
HETATM 3406 C  C8  . A1CAW E 2 .   ? -1.963  17.122  40.623  1.00 59.65  ? 501 A1CAW A C8  1 
HETATM 3407 O  O2  . A1CAW E 2 .   ? -2.223  15.864  41.026  1.00 61.20  ? 501 A1CAW A O2  1 
HETATM 3408 C  C9  . A1CAW E 2 .   ? -3.275  15.345  40.159  1.00 62.94  ? 501 A1CAW A C9  1 
HETATM 3409 C  C10 . A1CAW E 2 .   ? -3.518  16.392  39.042  1.00 64.32  ? 501 A1CAW A C10 1 
HETATM 3410 C  C11 . A1CAW E 2 .   ? -4.991  16.800  38.908  1.00 65.60  ? 501 A1CAW A C11 1 
HETATM 3411 C  C12 . A1CAW E 2 .   ? -5.833  15.697  38.302  1.00 66.67  ? 501 A1CAW A C12 1 
HETATM 3412 N  N5  . A1CAW E 2 .   ? -5.313  15.282  36.994  1.00 67.93  ? 501 A1CAW A N5  1 
HETATM 3413 C  C13 . A1CAW E 2 .   ? -3.926  14.814  37.102  1.00 67.05  ? 501 A1CAW A C13 1 
HETATM 3414 C  C14 . A1CAW E 2 .   ? -3.020  15.881  37.683  1.00 66.18  ? 501 A1CAW A C14 1 
HETATM 3415 C  C15 . A1CAW E 2 .   ? 1.917   21.379  41.089  1.00 51.14  ? 501 A1CAW A C15 1 
HETATM 3416 C  C16 . A1CAW E 2 .   ? 2.442   22.793  40.920  1.00 51.28  ? 501 A1CAW A C16 1 
HETATM 3417 C  C17 . A1CAW E 2 .   ? 1.453   23.887  40.694  1.00 51.58  ? 501 A1CAW A C17 1 
HETATM 3418 O  O3  . A1CAW E 2 .   ? 1.801   25.029  40.440  1.00 53.32  ? 501 A1CAW A O3  1 
HETATM 3419 ZN ZN  . ZN    F 3 .   ? 17.191  10.399  45.586  1.00 59.66  ? 502 ZN    A ZN  1 
HETATM 3420 O  O1  . A1CAW G 2 .   ? 18.783  -51.118 -4.219  1.00 55.87  ? 501 A1CAW B O1  1 
HETATM 3421 C  C1  . A1CAW G 2 .   ? 19.514  -51.285 -3.255  1.00 56.02  ? 501 A1CAW B C1  1 
HETATM 3422 N  N1  . A1CAW G 2 .   ? 19.665  -52.530 -2.688  1.00 55.38  ? 501 A1CAW B N1  1 
HETATM 3423 N  N2  . A1CAW G 2 .   ? 20.230  -50.240 -2.749  1.00 57.44  ? 501 A1CAW B N2  1 
HETATM 3424 C  C2  . A1CAW G 2 .   ? 20.097  -48.971 -3.285  1.00 60.57  ? 501 A1CAW B C2  1 
HETATM 3425 C  C3  . A1CAW G 2 .   ? 21.062  -48.000 -3.567  1.00 61.40  ? 501 A1CAW B C3  1 
HETATM 3426 N  N3  . A1CAW G 2 .   ? 20.538  -46.801 -4.016  1.00 62.65  ? 501 A1CAW B N3  1 
HETATM 3427 C  C4  . A1CAW G 2 .   ? 19.191  -46.975 -3.914  1.00 64.38  ? 501 A1CAW B C4  1 
HETATM 3428 N  N4  . A1CAW G 2 .   ? 18.901  -48.248 -3.441  1.00 63.46  ? 501 A1CAW B N4  1 
HETATM 3429 C  C5  . A1CAW G 2 .   ? 17.596  -48.670 -3.251  1.00 64.96  ? 501 A1CAW B C5  1 
HETATM 3430 C  C6  . A1CAW G 2 .   ? 16.551  -47.852 -3.516  1.00 66.64  ? 501 A1CAW B C6  1 
HETATM 3431 C  C7  . A1CAW G 2 .   ? 16.804  -46.510 -4.011  1.00 68.91  ? 501 A1CAW B C7  1 
HETATM 3432 C  C8  . A1CAW G 2 .   ? 18.074  -46.081 -4.192  1.00 67.04  ? 501 A1CAW B C8  1 
HETATM 3433 O  O2  . A1CAW G 2 .   ? 18.198  -44.828 -4.665  1.00 68.54  ? 501 A1CAW B O2  1 
HETATM 3434 C  C9  . A1CAW G 2 .   ? 16.853  -44.365 -4.992  1.00 70.47  ? 501 A1CAW B C9  1 
HETATM 3435 C  C10 . A1CAW G 2 .   ? 15.852  -45.377 -4.376  1.00 71.92  ? 501 A1CAW B C10 1 
HETATM 3436 C  C11 . A1CAW G 2 .   ? 14.756  -45.839 -5.345  1.00 73.14  ? 501 A1CAW B C11 1 
HETATM 3437 C  C12 . A1CAW G 2 .   ? 13.731  -44.756 -5.609  1.00 73.81  ? 501 A1CAW B C12 1 
HETATM 3438 N  N5  . A1CAW G 2 .   ? 13.125  -44.268 -4.365  1.00 74.58  ? 501 A1CAW B N5  1 
HETATM 3439 C  C13 . A1CAW G 2 .   ? 14.147  -43.744 -3.453  1.00 73.76  ? 501 A1CAW B C13 1 
HETATM 3440 C  C14 . A1CAW G 2 .   ? 15.188  -44.793 -3.120  1.00 73.25  ? 501 A1CAW B C14 1 
HETATM 3441 C  C15 . A1CAW G 2 .   ? 21.074  -50.344 -1.549  1.00 56.32  ? 501 A1CAW B C15 1 
HETATM 3442 C  C16 . A1CAW G 2 .   ? 21.298  -51.771 -1.071  1.00 56.28  ? 501 A1CAW B C16 1 
HETATM 3443 C  C17 . A1CAW G 2 .   ? 20.457  -52.856 -1.661  1.00 55.88  ? 501 A1CAW B C17 1 
HETATM 3444 O  O3  . A1CAW G 2 .   ? 20.488  -54.003 -1.244  1.00 54.81  ? 501 A1CAW B O3  1 
HETATM 3445 ZN ZN  . ZN    H 3 .   ? 34.626  -39.606 7.104   1.00 58.70  ? 502 ZN    B ZN  1 
HETATM 3446 O  O1  . A1CAW I 2 .   ? 19.168  -8.380  35.766  1.00 51.25  ? 501 A1CAW C O1  1 
HETATM 3447 C  C1  . A1CAW I 2 .   ? 19.140  -7.514  34.905  1.00 52.74  ? 501 A1CAW C C1  1 
HETATM 3448 N  N1  . A1CAW I 2 .   ? 20.134  -7.430  33.956  1.00 52.61  ? 501 A1CAW C N1  1 
HETATM 3449 N  N2  . A1CAW I 2 .   ? 18.106  -6.619  34.863  1.00 54.19  ? 501 A1CAW C N2  1 
HETATM 3450 C  C2  . A1CAW I 2 .   ? 17.167  -6.541  35.888  1.00 57.28  ? 501 A1CAW C C2  1 
HETATM 3451 C  C3  . A1CAW I 2 .   ? 15.787  -6.310  35.833  1.00 57.47  ? 501 A1CAW C C3  1 
HETATM 3452 N  N3  . A1CAW I 2 .   ? 15.181  -6.210  37.074  1.00 58.25  ? 501 A1CAW C N3  1 
HETATM 3453 C  C4  . A1CAW I 2 .   ? 16.221  -6.277  37.953  1.00 59.88  ? 501 A1CAW C C4  1 
HETATM 3454 N  N4  . A1CAW I 2 .   ? 17.421  -6.436  37.268  1.00 59.69  ? 501 A1CAW C N4  1 
HETATM 3455 C  C5  . A1CAW I 2 .   ? 18.627  -6.535  37.942  1.00 60.91  ? 501 A1CAW C C5  1 
HETATM 3456 C  C6  . A1CAW I 2 .   ? 18.686  -6.474  39.292  1.00 61.63  ? 501 A1CAW C C6  1 
HETATM 3457 C  C7  . A1CAW I 2 .   ? 17.461  -6.305  40.050  1.00 62.96  ? 501 A1CAW C C7  1 
HETATM 3458 C  C8  . A1CAW I 2 .   ? 16.271  -6.212  39.413  1.00 62.08  ? 501 A1CAW C C8  1 
HETATM 3459 O  O2  . A1CAW I 2 .   ? 15.201  -6.053  40.214  1.00 62.78  ? 501 A1CAW C O2  1 
HETATM 3460 C  C9  . A1CAW I 2 .   ? 15.693  -5.978  41.586  1.00 64.10  ? 501 A1CAW C C9  1 
HETATM 3461 C  C10 . A1CAW I 2 .   ? 17.230  -6.197  41.550  1.00 64.62  ? 501 A1CAW C C10 1 
HETATM 3462 C  C11 . A1CAW I 2 .   ? 17.676  -7.458  42.302  1.00 65.79  ? 501 A1CAW C C11 1 
HETATM 3463 C  C12 . A1CAW I 2 .   ? 17.663  -7.270  43.805  1.00 66.45  ? 501 A1CAW C C12 1 
HETATM 3464 N  N5  . A1CAW I 2 .   ? 18.485  -6.126  44.209  1.00 66.37  ? 501 A1CAW C N5  1 
HETATM 3465 C  C13 . A1CAW I 2 .   ? 17.984  -4.895  43.594  1.00 66.17  ? 501 A1CAW C C13 1 
HETATM 3466 C  C14 . A1CAW I 2 .   ? 18.016  -4.989  42.083  1.00 65.37  ? 501 A1CAW C C14 1 
HETATM 3467 C  C15 . A1CAW I 2 .   ? 17.949  -5.629  33.785  1.00 53.77  ? 501 A1CAW C C15 1 
HETATM 3468 C  C16 . A1CAW I 2 .   ? 19.162  -5.503  32.871  1.00 53.18  ? 501 A1CAW C C16 1 
HETATM 3469 C  C17 . A1CAW I 2 .   ? 20.233  -6.535  32.970  1.00 52.63  ? 501 A1CAW C C17 1 
HETATM 3470 O  O3  . A1CAW I 2 .   ? 21.171  -6.575  32.191  1.00 52.90  ? 501 A1CAW C O3  1 
HETATM 3471 ZN ZN  . ZN    J 3 .   ? 5.621   7.848   27.448  1.00 56.42  ? 502 ZN    C ZN  1 
HETATM 3472 O  O1  . A1CAW K 2 .   ? 28.787  -20.584 14.703  1.00 65.88  ? 501 A1CAW D O1  1 
HETATM 3473 C  C1  . A1CAW K 2 .   ? 28.117  -21.474 15.206  1.00 64.72  ? 501 A1CAW D C1  1 
HETATM 3474 N  N1  . A1CAW K 2 .   ? 27.969  -21.566 16.573  1.00 64.24  ? 501 A1CAW D N1  1 
HETATM 3475 N  N2  . A1CAW K 2 .   ? 27.504  -22.410 14.414  1.00 65.16  ? 501 A1CAW D N2  1 
HETATM 3476 C  C2  . A1CAW K 2 .   ? 27.683  -22.478 13.035  1.00 64.64  ? 501 A1CAW D C2  1 
HETATM 3477 C  C3  . A1CAW K 2 .   ? 26.742  -22.757 12.039  1.00 64.11  ? 501 A1CAW D C3  1 
HETATM 3478 N  N3  . A1CAW K 2 .   ? 27.273  -22.848 10.767  1.00 64.93  ? 501 A1CAW D N3  1 
HETATM 3479 C  C4  . A1CAW K 2 .   ? 28.614  -22.731 10.962  1.00 66.03  ? 501 A1CAW D C4  1 
HETATM 3480 N  N4  . A1CAW K 2 .   ? 28.890  -22.551 12.313  1.00 65.37  ? 501 A1CAW D N4  1 
HETATM 3481 C  C5  . A1CAW K 2 .   ? 30.192  -22.401 12.762  1.00 66.46  ? 501 A1CAW D C5  1 
HETATM 3482 C  C6  . A1CAW K 2 .   ? 31.241  -22.434 11.905  1.00 67.49  ? 501 A1CAW D C6  1 
HETATM 3483 C  C7  . A1CAW K 2 .   ? 30.999  -22.623 10.482  1.00 69.10  ? 501 A1CAW D C7  1 
HETATM 3484 C  C8  . A1CAW K 2 .   ? 29.735  -22.771 10.025  1.00 67.91  ? 501 A1CAW D C8  1 
HETATM 3485 O  O2  . A1CAW K 2 .   ? 29.615  -22.936 8.695   1.00 69.00  ? 501 A1CAW D O2  1 
HETATM 3486 C  C9  . A1CAW K 2 .   ? 30.954  -22.846 8.123   1.00 70.51  ? 501 A1CAW D C9  1 
HETATM 3487 C  C10 . A1CAW K 2 .   ? 31.957  -22.709 9.299   1.00 72.17  ? 501 A1CAW D C10 1 
HETATM 3488 C  C11 . A1CAW K 2 .   ? 32.852  -21.466 9.186   1.00 73.93  ? 501 A1CAW D C11 1 
HETATM 3489 C  C12 . A1CAW K 2 .   ? 33.930  -21.619 8.132   1.00 75.12  ? 501 A1CAW D C12 1 
HETATM 3490 N  N5  . A1CAW K 2 .   ? 34.744  -22.819 8.351   1.00 75.82  ? 501 A1CAW D N5  1 
HETATM 3491 C  C13 . A1CAW K 2 .   ? 33.903  -24.019 8.339   1.00 75.04  ? 501 A1CAW D C13 1 
HETATM 3492 C  C14 . A1CAW K 2 .   ? 32.847  -23.955 9.422   1.00 73.97  ? 501 A1CAW D C14 1 
HETATM 3493 C  C15 . A1CAW K 2 .   ? 26.723  -23.523 14.979  1.00 65.62  ? 501 A1CAW D C15 1 
HETATM 3494 C  C16 . A1CAW K 2 .   ? 26.310  -23.310 16.425  1.00 64.56  ? 501 A1CAW D C16 1 
HETATM 3495 C  C17 . A1CAW K 2 .   ? 27.199  -22.436 17.239  1.00 64.50  ? 501 A1CAW D C17 1 
HETATM 3496 O  O3  . A1CAW K 2 .   ? 27.210  -22.475 18.459  1.00 64.89  ? 501 A1CAW D O3  1 
HETATM 3497 ZN ZN  . ZN    L 3 .   ? 13.316  -36.681 10.152  1.00 59.47  ? 502 ZN    D ZN  1 
HETATM 3498 O  O   . HOH   M 4 .   ? -10.267 14.721  39.796  1.00 46.83  ? 601 HOH   A O   1 
HETATM 3499 O  O   . HOH   M 4 .   ? 7.200   29.220  48.344  1.00 51.99  ? 602 HOH   A O   1 
HETATM 3500 O  O   . HOH   M 4 .   ? 3.807   19.057  34.205  1.00 37.76  ? 603 HOH   A O   1 
HETATM 3501 O  O   . HOH   M 4 .   ? 13.696  20.981  53.734  1.00 52.45  ? 604 HOH   A O   1 
HETATM 3502 O  O   . HOH   M 4 .   ? -4.540  13.549  44.132  1.00 44.06  ? 605 HOH   A O   1 
HETATM 3503 O  O   . HOH   M 4 .   ? 7.746   9.006   44.133  1.00 43.07  ? 606 HOH   A O   1 
HETATM 3504 O  O   . HOH   M 4 .   ? 1.236   15.969  39.321  1.00 32.40  ? 607 HOH   A O   1 
HETATM 3505 O  O   . HOH   M 4 .   ? 2.467   15.115  44.058  1.00 41.62  ? 608 HOH   A O   1 
HETATM 3506 O  O   . HOH   N 4 .   ? 19.328  -44.836 -0.900  1.00 35.67  ? 601 HOH   B O   1 
HETATM 3507 O  O   . HOH   O 4 .   ? 21.455  -7.945  20.443  1.00 41.42  ? 601 HOH   C O   1 
HETATM 3508 O  O   . HOH   O 4 .   ? 20.990  1.010   37.350  1.00 46.63  ? 602 HOH   C O   1 
HETATM 3509 O  O   . HOH   O 4 .   ? 8.335   -3.379  20.282  1.00 64.45  ? 603 HOH   C O   1 
HETATM 3510 O  O   . HOH   O 4 .   ? 17.805  9.843   25.981  1.00 37.00  ? 604 HOH   C O   1 
HETATM 3511 O  O   . HOH   O 4 .   ? 19.253  -8.550  22.604  1.00 38.20  ? 605 HOH   C O   1 
HETATM 3512 O  O   . HOH   O 4 .   ? 27.213  -13.762 22.377  1.00 49.16  ? 606 HOH   C O   1 
HETATM 3513 O  O   . HOH   O 4 .   ? 15.934  -2.737  37.219  1.00 36.66  ? 607 HOH   C O   1 
HETATM 3514 O  O   . HOH   O 4 .   ? 1.848   1.568   29.188  1.00 41.09  ? 608 HOH   C O   1 
HETATM 3515 O  O   . HOH   O 4 .   ? 3.260   10.803  36.408  1.00 39.95  ? 609 HOH   C O   1 
HETATM 3516 O  O   . HOH   P 4 .   ? 18.337  -20.981 26.654  1.00 42.05  ? 601 HOH   D O   1 
HETATM 3517 O  O   . HOH   P 4 .   ? 23.455  -44.474 14.351  1.00 39.32  ? 602 HOH   D O   1 
HETATM 3518 O  O   . HOH   P 4 .   ? 19.874  -38.935 20.032  1.00 36.58  ? 603 HOH   D O   1 
HETATM 3519 O  O   . HOH   P 4 .   ? 9.886   -25.184 17.291  1.00 58.39  ? 604 HOH   D O   1 
HETATM 3520 O  O   . HOH   P 4 .   ? 34.602  -32.846 12.651  1.00 50.75  ? 605 HOH   D O   1 
HETATM 3521 O  O   . HOH   P 4 .   ? 23.105  -26.158 9.029   1.00 40.53  ? 606 HOH   D O   1 
HETATM 3522 O  O   . HOH   P 4 .   ? 23.742  -14.682 29.633  1.00 31.87  ? 607 HOH   D O   1 
HETATM 3523 O  O   . HOH   P 4 .   ? 18.434  -20.462 23.169  1.00 30.59  ? 608 HOH   D O   1 
HETATM 3524 O  O   . HOH   P 4 .   ? 13.956  -15.167 19.051  1.00 41.57  ? 609 HOH   D O   1 
HETATM 3525 O  O   . HOH   P 4 .   ? 12.519  -14.025 21.556  1.00 39.86  ? 610 HOH   D O   1 
HETATM 3526 O  O   . HOH   P 4 .   ? 27.450  -26.308 11.448  1.00 28.29  ? 611 HOH   D O   1 
HETATM 3527 O  O   . HOH   P 4 .   ? 35.296  -31.711 30.659  1.00 42.43  ? 612 HOH   D O   1 
HETATM 3528 O  O   . HOH   P 4 .   ? 11.389  -32.851 33.706  1.00 43.55  ? 613 HOH   D O   1 
# 
