data_9DDU
# 
_entry.id   9DDU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DDU         pdb_00009ddu 10.2210/pdb9ddu/pdb 
WWPDB D_1000287545 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9DDU 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              geigerj@msu.edu 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_last          Geiger 
_pdbx_contact_author.name_mi            H. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9443-4488 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bingham, C.'  1 0000-0001-5920-5543 
'Geiger, J.H.' 2 0000-0002-9443-4488 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Photoswitching fluorescence via a novel Trp-flap mechanism' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bingham, C.'   1 0000-0001-5920-5543 
primary 'Ehyeai, N.'    2 ?                   
primary 'Maity, S.'     3 ?                   
primary 'Cantrell, J.'  4 ?                   
primary 'Gwasdacus, J.' 5 ?                   
primary 'Sheng, W.'     6 ?                   
primary 'Vasileiou, C.' 7 ?                   
primary 'Borhan, B.'    8 0000-0002-3193-0732 
primary 'Geiger, J.H.'  9 0000-0002-9443-4488 
# 
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 'Retinol-binding protein 2'                                                 15553.569 2   ? ? ? ? 
2 non-polymer syn '(4aP)-N,N-diethyl-9,9-dimethyl-7-[(1E)-prop-1-en-1-yl]-9H-fluoren-2-amine' 305.456   2   ? ? ? ? 
3 non-polymer syn 'ACETIC ACID'                                                               60.052    3   ? ? ? ? 
4 non-polymer syn GLYCEROL                                                                    92.094    8   ? ? ? ? 
5 water       nat water                                                                       18.015    110 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cellular retinol-binding protein II,CRBP-II' 
# 
_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       
;TRDANGTWEMESNENFEGWMKALDIDFALRKIAVRLTLTLVIDQDGDNFKTKCTSTFYNYDVDFTVGVEFDEYTKSLDNR
HVKALVTWEGDVLVCVQKGEKENRGWKKWIEGDKLYLELTCGDQVCRQVFKKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TRDANGTWEMESNENFEGWMKALDIDFALRKIAVRLTLTLVIDQDGDNFKTKCTSTFYNYDVDFTVGVEFDEYTKSLDNR
HVKALVTWEGDVLVCVQKGEKENRGWKKWIEGDKLYLELTCGDQVCRQVFKKK
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(4aP)-N,N-diethyl-9,9-dimethyl-7-[(1E)-prop-1-en-1-yl]-9H-fluoren-2-amine' ZFJ 
3 'ACETIC ACID'                                                               ACY 
4 GLYCEROL                                                                    GOL 
5 water                                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ARG n 
1 3   ASP n 
1 4   ALA n 
1 5   ASN n 
1 6   GLY n 
1 7   THR n 
1 8   TRP n 
1 9   GLU n 
1 10  MET n 
1 11  GLU n 
1 12  SER n 
1 13  ASN n 
1 14  GLU n 
1 15  ASN n 
1 16  PHE n 
1 17  GLU n 
1 18  GLY n 
1 19  TRP n 
1 20  MET n 
1 21  LYS n 
1 22  ALA n 
1 23  LEU n 
1 24  ASP n 
1 25  ILE n 
1 26  ASP n 
1 27  PHE n 
1 28  ALA n 
1 29  LEU n 
1 30  ARG n 
1 31  LYS n 
1 32  ILE n 
1 33  ALA n 
1 34  VAL n 
1 35  ARG n 
1 36  LEU n 
1 37  THR n 
1 38  LEU n 
1 39  THR n 
1 40  LEU n 
1 41  VAL n 
1 42  ILE n 
1 43  ASP n 
1 44  GLN n 
1 45  ASP n 
1 46  GLY n 
1 47  ASP n 
1 48  ASN n 
1 49  PHE n 
1 50  LYS n 
1 51  THR n 
1 52  LYS n 
1 53  CYS n 
1 54  THR n 
1 55  SER n 
1 56  THR n 
1 57  PHE n 
1 58  TYR n 
1 59  ASN n 
1 60  TYR n 
1 61  ASP n 
1 62  VAL n 
1 63  ASP n 
1 64  PHE n 
1 65  THR n 
1 66  VAL n 
1 67  GLY n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  GLU n 
1 73  TYR n 
1 74  THR n 
1 75  LYS n 
1 76  SER n 
1 77  LEU n 
1 78  ASP n 
1 79  ASN n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  LYS n 
1 84  ALA n 
1 85  LEU n 
1 86  VAL n 
1 87  THR n 
1 88  TRP n 
1 89  GLU n 
1 90  GLY n 
1 91  ASP n 
1 92  VAL n 
1 93  LEU n 
1 94  VAL n 
1 95  CYS n 
1 96  VAL n 
1 97  GLN n 
1 98  LYS n 
1 99  GLY n 
1 100 GLU n 
1 101 LYS n 
1 102 GLU n 
1 103 ASN n 
1 104 ARG n 
1 105 GLY n 
1 106 TRP n 
1 107 LYS n 
1 108 LYS n 
1 109 TRP n 
1 110 ILE n 
1 111 GLU n 
1 112 GLY n 
1 113 ASP n 
1 114 LYS n 
1 115 LEU n 
1 116 TYR n 
1 117 LEU n 
1 118 GLU n 
1 119 LEU n 
1 120 THR n 
1 121 CYS n 
1 122 GLY n 
1 123 ASP n 
1 124 GLN n 
1 125 VAL n 
1 126 CYS n 
1 127 ARG n 
1 128 GLN n 
1 129 VAL n 
1 130 PHE n 
1 131 LYS n 
1 132 LYS n 
1 133 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   133 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'RBP2, CRBP2' 
_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 
ACY non-polymer         . 'ACETIC ACID'                                                               ? 'C2 H4 O2'       60.052  
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  
GOL non-polymer         . GLYCEROL                                                                    
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE                                                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                       ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                  ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                                     ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                                      ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                  ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                               ? 'C9 H11 N O2'    165.189 
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 
ZFJ non-polymer         . '(4aP)-N,N-diethyl-9,9-dimethyl-7-[(1E)-prop-1-en-1-yl]-9H-fluoren-2-amine' ? 'C22 H27 N'      305.456 
# 
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   THR 1   1   1   THR THR B . n 
A 1 2   ARG 2   2   2   ARG ARG B . n 
A 1 3   ASP 3   3   3   ASP ASP B . n 
A 1 4   ALA 4   4   4   ALA ALA B . n 
A 1 5   ASN 5   5   5   ASN ASN B . n 
A 1 6   GLY 6   6   6   GLY GLY B . n 
A 1 7   THR 7   7   7   THR THR B . n 
A 1 8   TRP 8   8   8   TRP TRP B . n 
A 1 9   GLU 9   9   9   GLU GLU B . n 
A 1 10  MET 10  10  10  MET MET B . n 
A 1 11  GLU 11  11  11  GLU GLU B . n 
A 1 12  SER 12  12  12  SER SER B . n 
A 1 13  ASN 13  13  13  ASN ASN B . n 
A 1 14  GLU 14  14  14  GLU GLU B . n 
A 1 15  ASN 15  15  15  ASN ASN B . n 
A 1 16  PHE 16  16  16  PHE PHE B . n 
A 1 17  GLU 17  17  17  GLU GLU B . n 
A 1 18  GLY 18  18  18  GLY GLY B . n 
A 1 19  TRP 19  19  19  TRP TRP B . n 
A 1 20  MET 20  20  20  MET MET B . n 
A 1 21  LYS 21  21  21  LYS LYS B . n 
A 1 22  ALA 22  22  22  ALA ALA B . n 
A 1 23  LEU 23  23  23  LEU LEU B . n 
A 1 24  ASP 24  24  24  ASP ASP B . n 
A 1 25  ILE 25  25  25  ILE ILE B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  PHE 27  27  27  PHE PHE B . n 
A 1 28  ALA 28  28  28  ALA ALA B . n 
A 1 29  LEU 29  29  29  LEU LEU B . n 
A 1 30  ARG 30  30  30  ARG ARG B . n 
A 1 31  LYS 31  31  31  LYS LYS B . n 
A 1 32  ILE 32  32  32  ILE ILE B . n 
A 1 33  ALA 33  33  33  ALA ALA B . n 
A 1 34  VAL 34  34  34  VAL VAL B . n 
A 1 35  ARG 35  35  35  ARG ARG B . n 
A 1 36  LEU 36  36  36  LEU LEU B . n 
A 1 37  THR 37  37  37  THR THR B . n 
A 1 38  LEU 38  38  38  LEU LEU B . n 
A 1 39  THR 39  39  39  THR THR B . n 
A 1 40  LEU 40  40  40  LEU LEU B . n 
A 1 41  VAL 41  41  41  VAL VAL B . n 
A 1 42  ILE 42  42  42  ILE ILE B . n 
A 1 43  ASP 43  43  43  ASP ASP B . n 
A 1 44  GLN 44  44  44  GLN GLN B . n 
A 1 45  ASP 45  45  45  ASP ASP B . n 
A 1 46  GLY 46  46  46  GLY GLY B . n 
A 1 47  ASP 47  47  47  ASP ASP B . n 
A 1 48  ASN 48  48  48  ASN ASN B . n 
A 1 49  PHE 49  49  49  PHE PHE B . n 
A 1 50  LYS 50  50  50  LYS LYS B . n 
A 1 51  THR 51  51  51  THR THR B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  CYS 53  53  53  CYS CYS B . n 
A 1 54  THR 54  54  54  THR THR B . n 
A 1 55  SER 55  55  55  SER SER B . n 
A 1 56  THR 56  56  56  THR THR B . n 
A 1 57  PHE 57  57  57  PHE PHE B . n 
A 1 58  TYR 58  58  58  TYR TYR B . n 
A 1 59  ASN 59  59  59  ASN ASN B . n 
A 1 60  TYR 60  60  60  TYR TYR B . n 
A 1 61  ASP 61  61  61  ASP ASP B . n 
A 1 62  VAL 62  62  62  VAL VAL B . n 
A 1 63  ASP 63  63  63  ASP ASP B . n 
A 1 64  PHE 64  64  64  PHE PHE B . n 
A 1 65  THR 65  65  65  THR THR B . n 
A 1 66  VAL 66  66  66  VAL VAL B . n 
A 1 67  GLY 67  67  67  GLY GLY B . n 
A 1 68  VAL 68  68  68  VAL VAL B . n 
A 1 69  GLU 69  69  69  GLU GLU B . n 
A 1 70  PHE 70  70  70  PHE PHE B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  GLU 72  72  72  GLU GLU B . n 
A 1 73  TYR 73  73  73  TYR TYR B . n 
A 1 74  THR 74  74  74  THR THR B . n 
A 1 75  LYS 75  75  75  LYS LYS B . n 
A 1 76  SER 76  76  76  SER SER B . n 
A 1 77  LEU 77  77  77  LEU LEU B . n 
A 1 78  ASP 78  78  78  ASP ASP B . n 
A 1 79  ASN 79  79  79  ASN ASN B . n 
A 1 80  ARG 80  80  80  ARG ARG B . n 
A 1 81  HIS 81  81  81  HIS HIS B . n 
A 1 82  VAL 82  82  82  VAL VAL B . n 
A 1 83  LYS 83  83  83  LYS LYS B . n 
A 1 84  ALA 84  84  84  ALA ALA B . n 
A 1 85  LEU 85  85  85  LEU LEU B . n 
A 1 86  VAL 86  86  86  VAL VAL B . n 
A 1 87  THR 87  87  87  THR THR B . n 
A 1 88  TRP 88  88  88  TRP TRP B . n 
A 1 89  GLU 89  89  89  GLU GLU B . n 
A 1 90  GLY 90  90  90  GLY GLY B . n 
A 1 91  ASP 91  91  91  ASP ASP B . n 
A 1 92  VAL 92  92  92  VAL VAL B . n 
A 1 93  LEU 93  93  93  LEU LEU B . n 
A 1 94  VAL 94  94  94  VAL VAL B . n 
A 1 95  CYS 95  95  95  CYS CYS B . n 
A 1 96  VAL 96  96  96  VAL VAL B . n 
A 1 97  GLN 97  97  97  GLN GLN B . n 
A 1 98  LYS 98  98  98  LYS LYS B . n 
A 1 99  GLY 99  99  99  GLY GLY B . n 
A 1 100 GLU 100 100 100 GLU GLU B . n 
A 1 101 LYS 101 101 101 LYS LYS B . n 
A 1 102 GLU 102 102 102 GLU GLU B . n 
A 1 103 ASN 103 103 103 ASN ASN B . n 
A 1 104 ARG 104 104 104 ARG ARG B . n 
A 1 105 GLY 105 105 105 GLY GLY B . n 
A 1 106 TRP 106 106 106 TRP TRP B . n 
A 1 107 LYS 107 107 107 LYS LYS B . n 
A 1 108 LYS 108 108 108 LYS LYS B . n 
A 1 109 TRP 109 109 109 TRP TRP B . n 
A 1 110 ILE 110 110 110 ILE ILE B . n 
A 1 111 GLU 111 111 111 GLU GLU B . n 
A 1 112 GLY 112 112 112 GLY GLY B . n 
A 1 113 ASP 113 113 113 ASP ASP B . n 
A 1 114 LYS 114 114 114 LYS LYS B . n 
A 1 115 LEU 115 115 115 LEU LEU B . n 
A 1 116 TYR 116 116 116 TYR TYR B . n 
A 1 117 LEU 117 117 117 LEU LEU B . n 
A 1 118 GLU 118 118 118 GLU GLU B . n 
A 1 119 LEU 119 119 119 LEU LEU B . n 
A 1 120 THR 120 120 120 THR THR B . n 
A 1 121 CYS 121 121 121 CYS CYS B . n 
A 1 122 GLY 122 122 122 GLY GLY B . n 
A 1 123 ASP 123 123 123 ASP ASP B . n 
A 1 124 GLN 124 124 124 GLN GLN B . n 
A 1 125 VAL 125 125 125 VAL VAL B . n 
A 1 126 CYS 126 126 126 CYS CYS B . n 
A 1 127 ARG 127 127 127 ARG ARG B . n 
A 1 128 GLN 128 128 128 GLN GLN B . n 
A 1 129 VAL 129 129 129 VAL VAL B . n 
A 1 130 PHE 130 130 130 PHE PHE B . n 
A 1 131 LYS 131 131 131 LYS LYS B . n 
A 1 132 LYS 132 132 132 LYS LYS B . n 
A 1 133 LYS 133 133 133 LYS LYS B . n 
B 1 1   THR 1   1   1   THR THR A . n 
B 1 2   ARG 2   2   2   ARG ARG A . n 
B 1 3   ASP 3   3   3   ASP ASP A . n 
B 1 4   ALA 4   4   4   ALA ALA A . n 
B 1 5   ASN 5   5   5   ASN ASN A . n 
B 1 6   GLY 6   6   6   GLY GLY A . n 
B 1 7   THR 7   7   7   THR THR A . n 
B 1 8   TRP 8   8   8   TRP TRP A . n 
B 1 9   GLU 9   9   9   GLU GLU A . n 
B 1 10  MET 10  10  10  MET MET A . n 
B 1 11  GLU 11  11  11  GLU GLU A . n 
B 1 12  SER 12  12  12  SER SER A . n 
B 1 13  ASN 13  13  13  ASN ASN A . n 
B 1 14  GLU 14  14  14  GLU GLU A . n 
B 1 15  ASN 15  15  15  ASN ASN A . n 
B 1 16  PHE 16  16  16  PHE PHE A . n 
B 1 17  GLU 17  17  17  GLU GLU A . n 
B 1 18  GLY 18  18  18  GLY GLY A . n 
B 1 19  TRP 19  19  19  TRP TRP A . n 
B 1 20  MET 20  20  20  MET MET A . n 
B 1 21  LYS 21  21  21  LYS LYS A . n 
B 1 22  ALA 22  22  22  ALA ALA A . n 
B 1 23  LEU 23  23  23  LEU LEU A . n 
B 1 24  ASP 24  24  24  ASP ASP A . n 
B 1 25  ILE 25  25  25  ILE ILE A . n 
B 1 26  ASP 26  26  26  ASP ASP A . n 
B 1 27  PHE 27  27  27  PHE PHE A . n 
B 1 28  ALA 28  28  28  ALA ALA A . n 
B 1 29  LEU 29  29  29  LEU LEU A . n 
B 1 30  ARG 30  30  30  ARG ARG A . n 
B 1 31  LYS 31  31  31  LYS LYS A . n 
B 1 32  ILE 32  32  32  ILE ILE A . n 
B 1 33  ALA 33  33  33  ALA ALA A . n 
B 1 34  VAL 34  34  34  VAL VAL A . n 
B 1 35  ARG 35  35  35  ARG ARG A . n 
B 1 36  LEU 36  36  36  LEU LEU A . n 
B 1 37  THR 37  37  37  THR THR A . n 
B 1 38  LEU 38  38  38  LEU LEU A . n 
B 1 39  THR 39  39  39  THR THR A . n 
B 1 40  LEU 40  40  40  LEU LEU A . n 
B 1 41  VAL 41  41  41  VAL VAL A . n 
B 1 42  ILE 42  42  42  ILE ILE A . n 
B 1 43  ASP 43  43  43  ASP ASP A . n 
B 1 44  GLN 44  44  44  GLN GLN A . n 
B 1 45  ASP 45  45  45  ASP ASP A . n 
B 1 46  GLY 46  46  46  GLY GLY A . n 
B 1 47  ASP 47  47  47  ASP ASP A . n 
B 1 48  ASN 48  48  48  ASN ASN A . n 
B 1 49  PHE 49  49  49  PHE PHE A . n 
B 1 50  LYS 50  50  50  LYS LYS A . n 
B 1 51  THR 51  51  51  THR THR A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  CYS 53  53  53  CYS CYS A . n 
B 1 54  THR 54  54  54  THR THR A . n 
B 1 55  SER 55  55  55  SER SER A . n 
B 1 56  THR 56  56  56  THR THR A . n 
B 1 57  PHE 57  57  57  PHE PHE A . n 
B 1 58  TYR 58  58  58  TYR TYR A . n 
B 1 59  ASN 59  59  59  ASN ASN A . n 
B 1 60  TYR 60  60  60  TYR TYR A . n 
B 1 61  ASP 61  61  61  ASP ASP A . n 
B 1 62  VAL 62  62  62  VAL VAL A . n 
B 1 63  ASP 63  63  63  ASP ASP A . n 
B 1 64  PHE 64  64  64  PHE PHE A . n 
B 1 65  THR 65  65  65  THR THR A . n 
B 1 66  VAL 66  66  66  VAL VAL A . n 
B 1 67  GLY 67  67  67  GLY GLY A . n 
B 1 68  VAL 68  68  68  VAL VAL A . n 
B 1 69  GLU 69  69  69  GLU GLU A . n 
B 1 70  PHE 70  70  70  PHE PHE A . n 
B 1 71  ASP 71  71  71  ASP ASP A . n 
B 1 72  GLU 72  72  72  GLU GLU A . n 
B 1 73  TYR 73  73  73  TYR TYR A . n 
B 1 74  THR 74  74  74  THR THR A . n 
B 1 75  LYS 75  75  75  LYS LYS A . n 
B 1 76  SER 76  76  76  SER SER A . n 
B 1 77  LEU 77  77  77  LEU LEU A . n 
B 1 78  ASP 78  78  78  ASP ASP A . n 
B 1 79  ASN 79  79  79  ASN ASN A . n 
B 1 80  ARG 80  80  80  ARG ARG A . n 
B 1 81  HIS 81  81  81  HIS HIS A . n 
B 1 82  VAL 82  82  82  VAL VAL A . n 
B 1 83  LYS 83  83  83  LYS LYS A . n 
B 1 84  ALA 84  84  84  ALA ALA A . n 
B 1 85  LEU 85  85  85  LEU LEU A . n 
B 1 86  VAL 86  86  86  VAL VAL A . n 
B 1 87  THR 87  87  87  THR THR A . n 
B 1 88  TRP 88  88  88  TRP TRP A . n 
B 1 89  GLU 89  89  89  GLU GLU A . n 
B 1 90  GLY 90  90  90  GLY GLY A . n 
B 1 91  ASP 91  91  91  ASP ASP A . n 
B 1 92  VAL 92  92  92  VAL VAL A . n 
B 1 93  LEU 93  93  93  LEU LEU A . n 
B 1 94  VAL 94  94  94  VAL VAL A . n 
B 1 95  CYS 95  95  95  CYS CYS A . n 
B 1 96  VAL 96  96  96  VAL VAL A . n 
B 1 97  GLN 97  97  97  GLN GLN A . n 
B 1 98  LYS 98  98  98  LYS LYS A . n 
B 1 99  GLY 99  99  99  GLY GLY A . n 
B 1 100 GLU 100 100 100 GLU GLU A . n 
B 1 101 LYS 101 101 101 LYS LYS A . n 
B 1 102 GLU 102 102 102 GLU GLU A . n 
B 1 103 ASN 103 103 103 ASN ASN A . n 
B 1 104 ARG 104 104 104 ARG ARG A . n 
B 1 105 GLY 105 105 105 GLY GLY A . n 
B 1 106 TRP 106 106 106 TRP TRP A . n 
B 1 107 LYS 107 107 107 LYS LYS A . n 
B 1 108 LYS 108 108 108 LYS LYS A . n 
B 1 109 TRP 109 109 109 TRP TRP A . n 
B 1 110 ILE 110 110 110 ILE ILE A . n 
B 1 111 GLU 111 111 111 GLU GLU A . n 
B 1 112 GLY 112 112 112 GLY GLY A . n 
B 1 113 ASP 113 113 113 ASP ASP A . n 
B 1 114 LYS 114 114 114 LYS LYS A . n 
B 1 115 LEU 115 115 115 LEU LEU A . n 
B 1 116 TYR 116 116 116 TYR TYR A . n 
B 1 117 LEU 117 117 117 LEU LEU A . n 
B 1 118 GLU 118 118 118 GLU GLU A . n 
B 1 119 LEU 119 119 119 LEU LEU A . n 
B 1 120 THR 120 120 120 THR THR A . n 
B 1 121 CYS 121 121 121 CYS CYS A . n 
B 1 122 GLY 122 122 122 GLY GLY A . n 
B 1 123 ASP 123 123 123 ASP ASP A . n 
B 1 124 GLN 124 124 124 GLN GLN A . n 
B 1 125 VAL 125 125 125 VAL VAL A . n 
B 1 126 CYS 126 126 126 CYS CYS A . n 
B 1 127 ARG 127 127 127 ARG ARG A . n 
B 1 128 GLN 128 128 128 GLN GLN A . n 
B 1 129 VAL 129 129 129 VAL VAL A . n 
B 1 130 PHE 130 130 130 PHE PHE A . n 
B 1 131 LYS 131 131 131 LYS LYS A . n 
B 1 132 LYS 132 132 132 LYS LYS A . n 
B 1 133 LYS 133 133 133 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZFJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZFJ 
_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 
C 2 ZFJ 1  201 201 ZFJ LIG B . 
D 3 ACY 1  202 301 ACY ACT B . 
E 4 GOL 1  203 401 GOL GOL B . 
F 4 GOL 1  204 501 GOL GOL B . 
G 4 GOL 1  205 601 GOL GOL B . 
H 4 GOL 1  206 701 GOL GOL B . 
I 4 GOL 1  207 801 GOL GOL B . 
J 2 ZFJ 1  201 211 ZFJ LIG A . 
K 4 GOL 1  202 311 GOL GOL A . 
L 4 GOL 1  203 411 GOL GOL A . 
M 3 ACY 1  204 511 ACY ACT A . 
N 3 ACY 1  205 611 ACY ACT A . 
O 4 GOL 1  206 711 GOL GOL A . 
P 5 HOH 1  301 46  HOH HOH B . 
P 5 HOH 2  302 39  HOH HOH B . 
P 5 HOH 3  303 82  HOH HOH B . 
P 5 HOH 4  304 2   HOH HOH B . 
P 5 HOH 5  305 21  HOH HOH B . 
P 5 HOH 6  306 68  HOH HOH B . 
P 5 HOH 7  307 49  HOH HOH B . 
P 5 HOH 8  308 40  HOH HOH B . 
P 5 HOH 9  309 19  HOH HOH B . 
P 5 HOH 10 310 61  HOH HOH B . 
P 5 HOH 11 311 67  HOH HOH B . 
P 5 HOH 12 312 8   HOH HOH B . 
P 5 HOH 13 313 69  HOH HOH B . 
P 5 HOH 14 314 117 HOH HOH B . 
P 5 HOH 15 315 48  HOH HOH B . 
P 5 HOH 16 316 54  HOH HOH B . 
P 5 HOH 17 317 15  HOH HOH B . 
P 5 HOH 18 318 123 HOH HOH B . 
P 5 HOH 19 319 11  HOH HOH B . 
P 5 HOH 20 320 27  HOH HOH B . 
P 5 HOH 21 321 52  HOH HOH B . 
P 5 HOH 22 322 10  HOH HOH B . 
P 5 HOH 23 323 65  HOH HOH B . 
P 5 HOH 24 324 111 HOH HOH B . 
P 5 HOH 25 325 5   HOH HOH B . 
P 5 HOH 26 326 85  HOH HOH B . 
P 5 HOH 27 327 74  HOH HOH B . 
P 5 HOH 28 328 32  HOH HOH B . 
P 5 HOH 29 329 4   HOH HOH B . 
P 5 HOH 30 330 59  HOH HOH B . 
P 5 HOH 31 331 26  HOH HOH B . 
P 5 HOH 32 332 16  HOH HOH B . 
P 5 HOH 33 333 107 HOH HOH B . 
P 5 HOH 34 334 102 HOH HOH B . 
P 5 HOH 35 335 106 HOH HOH B . 
P 5 HOH 36 336 7   HOH HOH B . 
P 5 HOH 37 337 124 HOH HOH B . 
P 5 HOH 38 338 31  HOH HOH B . 
P 5 HOH 39 339 127 HOH HOH B . 
P 5 HOH 40 340 90  HOH HOH B . 
P 5 HOH 41 341 33  HOH HOH B . 
P 5 HOH 42 342 70  HOH HOH B . 
P 5 HOH 43 343 128 HOH HOH B . 
P 5 HOH 44 344 24  HOH HOH B . 
P 5 HOH 45 345 66  HOH HOH B . 
P 5 HOH 46 346 13  HOH HOH B . 
P 5 HOH 47 347 53  HOH HOH B . 
P 5 HOH 48 348 105 HOH HOH B . 
P 5 HOH 49 349 64  HOH HOH B . 
P 5 HOH 50 350 45  HOH HOH B . 
P 5 HOH 51 351 126 HOH HOH B . 
P 5 HOH 52 352 22  HOH HOH B . 
P 5 HOH 53 353 94  HOH HOH B . 
P 5 HOH 54 354 114 HOH HOH B . 
P 5 HOH 55 355 75  HOH HOH B . 
P 5 HOH 56 356 41  HOH HOH B . 
P 5 HOH 57 357 37  HOH HOH B . 
Q 5 HOH 1  301 89  HOH HOH A . 
Q 5 HOH 2  302 28  HOH HOH A . 
Q 5 HOH 3  303 36  HOH HOH A . 
Q 5 HOH 4  304 101 HOH HOH A . 
Q 5 HOH 5  305 71  HOH HOH A . 
Q 5 HOH 6  306 83  HOH HOH A . 
Q 5 HOH 7  307 80  HOH HOH A . 
Q 5 HOH 8  308 12  HOH HOH A . 
Q 5 HOH 9  309 18  HOH HOH A . 
Q 5 HOH 10 310 1   HOH HOH A . 
Q 5 HOH 11 311 103 HOH HOH A . 
Q 5 HOH 12 312 14  HOH HOH A . 
Q 5 HOH 13 313 35  HOH HOH A . 
Q 5 HOH 14 314 81  HOH HOH A . 
Q 5 HOH 15 315 9   HOH HOH A . 
Q 5 HOH 16 316 17  HOH HOH A . 
Q 5 HOH 17 317 47  HOH HOH A . 
Q 5 HOH 18 318 42  HOH HOH A . 
Q 5 HOH 19 319 38  HOH HOH A . 
Q 5 HOH 20 320 63  HOH HOH A . 
Q 5 HOH 21 321 56  HOH HOH A . 
Q 5 HOH 22 322 73  HOH HOH A . 
Q 5 HOH 23 323 3   HOH HOH A . 
Q 5 HOH 24 324 84  HOH HOH A . 
Q 5 HOH 25 325 57  HOH HOH A . 
Q 5 HOH 26 326 62  HOH HOH A . 
Q 5 HOH 27 327 58  HOH HOH A . 
Q 5 HOH 28 328 6   HOH HOH A . 
Q 5 HOH 29 329 20  HOH HOH A . 
Q 5 HOH 30 330 93  HOH HOH A . 
Q 5 HOH 31 331 23  HOH HOH A . 
Q 5 HOH 32 332 29  HOH HOH A . 
Q 5 HOH 33 333 25  HOH HOH A . 
Q 5 HOH 34 334 60  HOH HOH A . 
Q 5 HOH 35 335 30  HOH HOH A . 
Q 5 HOH 36 336 34  HOH HOH A . 
Q 5 HOH 37 337 50  HOH HOH A . 
Q 5 HOH 38 338 77  HOH HOH A . 
Q 5 HOH 39 339 79  HOH HOH A . 
Q 5 HOH 40 340 130 HOH HOH A . 
Q 5 HOH 41 341 86  HOH HOH A . 
Q 5 HOH 42 342 99  HOH HOH A . 
Q 5 HOH 43 343 104 HOH HOH A . 
Q 5 HOH 44 344 44  HOH HOH A . 
Q 5 HOH 45 345 129 HOH HOH A . 
Q 5 HOH 46 346 115 HOH HOH A . 
Q 5 HOH 47 347 118 HOH HOH A . 
Q 5 HOH 48 348 76  HOH HOH A . 
Q 5 HOH 49 349 55  HOH HOH A . 
Q 5 HOH 50 350 108 HOH HOH A . 
Q 5 HOH 51 351 43  HOH HOH A . 
Q 5 HOH 52 352 72  HOH HOH A . 
Q 5 HOH 53 353 120 HOH HOH A . 
# 
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 ASP 61 ? CG  ? A ASP 61 CG  
2 1 Y 1 B ASP 61 ? OD1 ? A ASP 61 OD1 
3 1 Y 1 B ASP 61 ? OD2 ? A ASP 61 OD2 
4 1 Y 1 A LYS 52 ? CG  ? B LYS 52 CG  
5 1 Y 1 A LYS 52 ? CD  ? B LYS 52 CD  
6 1 Y 1 A LYS 52 ? CE  ? B LYS 52 CE  
7 1 Y 1 A LYS 52 ? NZ  ? B LYS 52 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_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.16 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .    4 
# 
_cell.angle_alpha                  86.010 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   86.510 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  65.280 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DDU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     31.021 
_cell.length_a_esd                 ? 
_cell.length_b                     35.939 
_cell.length_b_esd                 ? 
_cell.length_c                     64.043 
_cell.length_c_esd                 ? 
_cell.volume                       64659.364 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9DDU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            'P 1' 
_symmetry.space_group_name_H-M             'P 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                   9DDU 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.83 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    'PEG4000, ammonium acetate, sodium acetate, pH 4.0-4.8' 
_exptl_crystal_grow.pdbx_pH_range   '4.0 - 4.8' 
_exptl_crystal_grow.temp            298 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.272 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.272 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DDU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.599 
_reflns.d_resolution_low                               29.63 
_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                                     29102 
_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                           87.82 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          88.1 
_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                                0.097 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.599 
_reflns_shell.d_res_low                                     1.657 
_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                             2868 
_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                               0.447 
_reflns_shell.pdbx_Rpim_I_all                               0.192 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.928 
_reflns_shell.pdbx_CC_star                                  0.981 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          85.63 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.96 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DDU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.599 
_refine.ls_d_res_low                             29.63 
_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                     29102 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.82 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2179 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1928 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.599 
_refine_hist.d_res_low                        29.63 
_refine_hist.number_atoms_solvent             110 
_refine_hist.number_atoms_total               2393 
_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        2177 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         106 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0174  ? 2337 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1510  ? 3147 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0747  ? 329  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0089  ? 391  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 19.7140 ? 1346 ? f_dihedral_angle_d ? ? 
# 
_struct.entry_id                     9DDU 
_struct.title                        
'Q108K:K40L:T51V:T53C:R58Y:Y19W:Q38L:Q4A:T29L mutant of hCRBPII bound to FR1V and irradiated with UV light at pH 3.0' 
_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        9DDU 
_struct_keywords.text            
'human cellular retinol binding protein II, hCRBPII, protein engineering, fluorescent protein, FR1V, RETINOL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RETINOL BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 2 ? 
K N N 4 ? 
L N N 4 ? 
M N N 3 ? 
N N N 3 ? 
O N N 4 ? 
P N N 5 ? 
Q N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RET2_HUMAN 
_struct_ref.pdbx_db_accession          P50120 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;TRDQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNR
HVKALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCGDQVCRQVFKKK
;
_struct_ref.pdbx_align_begin           2 
# 
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 9DDU B 1 ? 133 ? P50120 2 ? 134 ? 1 133 
2 1 9DDU A 1 ? 133 ? P50120 2 ? 134 ? 1 133 
# 
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 9DDU ALA B 4   ? UNP P50120 GLN 5   'engineered mutation' 4   1  
1 9DDU TRP B 19  ? UNP P50120 TYR 20  'engineered mutation' 19  2  
1 9DDU LEU B 29  ? UNP P50120 THR 30  'engineered mutation' 29  3  
1 9DDU LEU B 38  ? UNP P50120 GLN 39  'engineered mutation' 38  4  
1 9DDU LEU B 40  ? UNP P50120 LYS 41  'engineered mutation' 40  5  
1 9DDU CYS B 53  ? UNP P50120 THR 54  'engineered mutation' 53  6  
1 9DDU TYR B 58  ? UNP P50120 ARG 59  'engineered mutation' 58  7  
1 9DDU LYS B 108 ? UNP P50120 GLN 109 'engineered mutation' 108 8  
2 9DDU ALA A 4   ? UNP P50120 GLN 5   'engineered mutation' 4   9  
2 9DDU TRP A 19  ? UNP P50120 TYR 20  'engineered mutation' 19  10 
2 9DDU LEU A 29  ? UNP P50120 THR 30  'engineered mutation' 29  11 
2 9DDU LEU A 38  ? UNP P50120 GLN 39  'engineered mutation' 38  12 
2 9DDU LEU A 40  ? UNP P50120 LYS 41  'engineered mutation' 40  13 
2 9DDU CYS A 53  ? UNP P50120 THR 54  'engineered mutation' 53  14 
2 9DDU TYR A 58  ? UNP P50120 ARG 59  'engineered mutation' 58  15 
2 9DDU LYS A 108 ? UNP P50120 GLN 109 'engineered mutation' 108 16 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? 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,C,D,E,F,G,H,I,P 
2 1 B,J,K,L,M,N,O,Q   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASN A 15 ? LEU A 23 ? ASN B 15 LEU B 23 1 ? 9 
HELX_P HELX_P2 AA2 ASP A 26 ? VAL A 34 ? ASP B 26 VAL B 34 1 ? 9 
HELX_P HELX_P3 AA3 ASN B 15 ? LEU B 23 ? ASN A 15 LEU A 23 1 ? 9 
HELX_P HELX_P4 AA4 ASP B 26 ? VAL B 34 ? ASP A 26 VAL A 34 1 ? 9 
# 
_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 
covale1 covale one ? A LYS 108 NZ ? ? ? 1_555 C ZFJ . C23 ? ? B LYS 108 B ZFJ 201 1_555 ? ? ? ? ? ? ? 1.420 doub ? 
covale2 covale one ? B LYS 108 NZ ? ? ? 1_555 J ZFJ . C23 ? ? A LYS 108 A ZFJ 201 1_555 ? ? ? ? ? ? ? 1.294 doub ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 ZFJ C . ? LYS A 108 ? ZFJ B 201 ? 1_555 LYS B 108 ? 1_555 C23 NZ LYS 1 ZFJ None 'Covalent chemical modification' 
2 ZFJ J . ? LYS B 108 ? ZFJ A 201 ? 1_555 LYS A 108 ? 1_555 C23 NZ LYS 1 ZFJ None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 10 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? 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 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? 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  ASN A 59  ? THR A 65  ? ASN B 59  THR B 65  
AA1 2  ASN A 48  ? THR A 54  ? ASN B 48  THR B 54  
AA1 3  THR A 39  ? ASP A 45  ? THR B 39  ASP B 45  
AA1 4  GLY A 6   ? GLU A 14  ? GLY B 6   GLU B 14  
AA1 5  GLN A 124 ? LYS A 132 ? GLN B 124 LYS B 132 
AA1 6  LYS A 114 ? CYS A 121 ? LYS B 114 CYS B 121 
AA1 7  GLY A 105 ? GLU A 111 ? GLY B 105 GLU B 111 
AA1 8  VAL A 92  ? LYS A 98  ? VAL B 92  LYS B 98  
AA1 9  HIS A 81  ? GLU A 89  ? HIS B 81  GLU B 89  
AA1 10 PHE A 70  ? TYR A 73  ? PHE B 70  TYR B 73  
AA2 1  ASN B 59  ? THR B 65  ? ASN A 59  THR A 65  
AA2 2  ASN B 48  ? THR B 54  ? ASN A 48  THR A 54  
AA2 3  THR B 39  ? ASP B 45  ? THR A 39  ASP A 45  
AA2 4  GLY B 6   ? GLU B 14  ? GLY A 6   GLU A 14  
AA2 5  GLN B 124 ? LYS B 132 ? GLN A 124 LYS A 132 
AA2 6  LYS B 114 ? CYS B 121 ? LYS A 114 CYS A 121 
AA2 7  GLY B 105 ? GLU B 111 ? GLY A 105 GLU A 111 
AA2 8  VAL B 92  ? LYS B 98  ? VAL A 92  LYS A 98  
AA2 9  HIS B 81  ? GLU B 89  ? HIS A 81  GLU A 89  
AA2 10 PHE B 70  ? TYR B 73  ? PHE A 70  TYR A 73  
# 
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 VAL A 62  ? O VAL B 62  N THR A 51  ? N THR B 51  
AA1 2 3  O LYS A 52  ? O LYS B 52  N VAL A 41  ? N VAL B 41  
AA1 3 4  O LEU A 40  ? O LEU B 40  N TRP A 8   ? N TRP B 8   
AA1 4 5  N GLU A 11  ? N GLU B 11  O VAL A 129 ? O VAL B 129 
AA1 5 6  O GLN A 128 ? O GLN B 128 N LEU A 117 ? N LEU B 117 
AA1 6 7  O TYR A 116 ? O TYR B 116 N TRP A 109 ? N TRP B 109 
AA1 7 8  O TRP A 106 ? O TRP B 106 N CYS A 95  ? N CYS B 95  
AA1 8 9  O VAL A 94  ? O VAL B 94  N THR A 87  ? N THR B 87  
AA1 9 10 O VAL A 82  ? O VAL B 82  N GLU A 72  ? N GLU B 72  
AA2 1 2  O VAL B 62  ? O VAL A 62  N THR B 51  ? N THR A 51  
AA2 2 3  O THR B 54  ? O THR A 54  N THR B 39  ? N THR A 39  
AA2 3 4  O LEU B 40  ? O LEU A 40  N TRP B 8   ? N TRP A 8   
AA2 4 5  N GLU B 11  ? N GLU A 11  O VAL B 129 ? O VAL A 129 
AA2 5 6  O GLN B 128 ? O GLN A 128 N LEU B 117 ? N LEU A 117 
AA2 6 7  O TYR B 116 ? O TYR A 116 N TRP B 109 ? N TRP A 109 
AA2 7 8  O TRP B 106 ? O TRP A 106 N CYS B 95  ? N CYS A 95  
AA2 8 9  O VAL B 94  ? O VAL A 94  N THR B 87  ? N THR A 87  
AA2 9 10 O ALA B 84  ? O ALA A 84  N PHE B 70  ? N PHE A 70  
# 
_pdbx_entry_details.entry_id                   9DDU 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 72  ? ? OXT A ACY 205 ? ? 1.69 
2 1 O2  A GOL 206 ? ? O   A HOH 301 ? ? 1.84 
3 1 OD1 A ASP 47  ? ? O   A HOH 302 ? ? 1.93 
4 1 N   A THR 1   ? ? OD1 A ASP 91  ? ? 2.03 
5 1 O   A HOH 339 ? ? O   A HOH 352 ? ? 2.12 
6 1 OG  B SER 12  ? ? O   B HOH 301 ? ? 2.12 
7 1 OE2 B GLU 72  ? ? O   B ACY 202 ? ? 2.18 
8 1 O   B HOH 340 ? ? O   B HOH 349 ? ? 2.19 
# 
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 PHE B 57 ? ? -97.20  -70.78  
2 1 LEU B 77 ? ? -119.41 -104.41 
3 1 LEU A 77 ? ? -124.56 -109.13 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 GLU A 102 ? ? -11.36 
2 1 GLU A 102 ? ? -11.36 
3 1 ASN A 103 ? A -11.16 
4 1 ASN A 103 ? B -11.16 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
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 
ACY C    C N N 1   
ACY O    O N N 2   
ACY OXT  O N N 3   
ACY CH3  C N N 4   
ACY HXT  H N N 5   
ACY H1   H N N 6   
ACY H2   H N N 7   
ACY H3   H N N 8   
ALA N    N N N 9   
ALA CA   C N S 10  
ALA C    C N N 11  
ALA O    O N N 12  
ALA CB   C N N 13  
ALA OXT  O N N 14  
ALA H    H N N 15  
ALA H2   H N N 16  
ALA HA   H N N 17  
ALA HB1  H N N 18  
ALA HB2  H N N 19  
ALA HB3  H N N 20  
ALA HXT  H N N 21  
ARG N    N N N 22  
ARG CA   C N S 23  
ARG C    C N N 24  
ARG O    O N N 25  
ARG CB   C N N 26  
ARG CG   C N N 27  
ARG CD   C N N 28  
ARG NE   N N N 29  
ARG CZ   C N N 30  
ARG NH1  N N N 31  
ARG NH2  N N N 32  
ARG OXT  O N N 33  
ARG H    H N N 34  
ARG H2   H N N 35  
ARG HA   H N N 36  
ARG HB2  H N N 37  
ARG HB3  H N N 38  
ARG HG2  H N N 39  
ARG HG3  H N N 40  
ARG HD2  H N N 41  
ARG HD3  H N N 42  
ARG HE   H N N 43  
ARG HH11 H N N 44  
ARG HH12 H N N 45  
ARG HH21 H N N 46  
ARG HH22 H N N 47  
ARG HXT  H N N 48  
ASN N    N N N 49  
ASN CA   C N S 50  
ASN C    C N N 51  
ASN O    O N N 52  
ASN CB   C N N 53  
ASN CG   C N N 54  
ASN OD1  O N N 55  
ASN ND2  N N N 56  
ASN OXT  O N N 57  
ASN H    H N N 58  
ASN H2   H N N 59  
ASN HA   H N N 60  
ASN HB2  H N N 61  
ASN HB3  H N N 62  
ASN HD21 H N N 63  
ASN HD22 H N N 64  
ASN HXT  H N N 65  
ASP N    N N N 66  
ASP CA   C N S 67  
ASP C    C N N 68  
ASP O    O N N 69  
ASP CB   C N N 70  
ASP CG   C N N 71  
ASP OD1  O N N 72  
ASP OD2  O N N 73  
ASP OXT  O N N 74  
ASP H    H N N 75  
ASP H2   H N N 76  
ASP HA   H N N 77  
ASP HB2  H N N 78  
ASP HB3  H N N 79  
ASP HD2  H N N 80  
ASP HXT  H N N 81  
CYS N    N N N 82  
CYS CA   C N R 83  
CYS C    C N N 84  
CYS O    O N N 85  
CYS CB   C N N 86  
CYS SG   S N N 87  
CYS OXT  O N N 88  
CYS H    H N N 89  
CYS H2   H N N 90  
CYS HA   H N N 91  
CYS HB2  H N N 92  
CYS HB3  H N N 93  
CYS HG   H N N 94  
CYS HXT  H N N 95  
GLN N    N N N 96  
GLN CA   C N S 97  
GLN C    C N N 98  
GLN O    O N N 99  
GLN CB   C N N 100 
GLN CG   C N N 101 
GLN CD   C N N 102 
GLN OE1  O N N 103 
GLN NE2  N N N 104 
GLN OXT  O N N 105 
GLN H    H N N 106 
GLN H2   H N N 107 
GLN HA   H N N 108 
GLN HB2  H N N 109 
GLN HB3  H N N 110 
GLN HG2  H N N 111 
GLN HG3  H N N 112 
GLN HE21 H N N 113 
GLN HE22 H N N 114 
GLN HXT  H N N 115 
GLU N    N N N 116 
GLU CA   C N S 117 
GLU C    C N N 118 
GLU O    O N N 119 
GLU CB   C N N 120 
GLU CG   C N N 121 
GLU CD   C N N 122 
GLU OE1  O N N 123 
GLU OE2  O N N 124 
GLU OXT  O N N 125 
GLU H    H N N 126 
GLU H2   H N N 127 
GLU HA   H N N 128 
GLU HB2  H N N 129 
GLU HB3  H N N 130 
GLU HG2  H N N 131 
GLU HG3  H N N 132 
GLU HE2  H N N 133 
GLU HXT  H N N 134 
GLY N    N N N 135 
GLY CA   C N N 136 
GLY C    C N N 137 
GLY O    O N N 138 
GLY OXT  O N N 139 
GLY H    H N N 140 
GLY H2   H N N 141 
GLY HA2  H N N 142 
GLY HA3  H N N 143 
GLY HXT  H N N 144 
GOL C1   C N N 145 
GOL O1   O N N 146 
GOL C2   C N N 147 
GOL O2   O N N 148 
GOL C3   C N N 149 
GOL O3   O N N 150 
GOL H11  H N N 151 
GOL H12  H N N 152 
GOL HO1  H N N 153 
GOL H2   H N N 154 
GOL HO2  H N N 155 
GOL H31  H N N 156 
GOL H32  H N N 157 
GOL HO3  H N N 158 
HIS N    N N N 159 
HIS CA   C N S 160 
HIS C    C N N 161 
HIS O    O N N 162 
HIS CB   C N N 163 
HIS CG   C Y N 164 
HIS ND1  N Y N 165 
HIS CD2  C Y N 166 
HIS CE1  C Y N 167 
HIS NE2  N Y N 168 
HIS OXT  O N N 169 
HIS H    H N N 170 
HIS H2   H N N 171 
HIS HA   H N N 172 
HIS HB2  H N N 173 
HIS HB3  H N N 174 
HIS HD1  H N N 175 
HIS HD2  H N N 176 
HIS HE1  H N N 177 
HIS HE2  H N N 178 
HIS HXT  H N N 179 
HOH O    O N N 180 
HOH H1   H N N 181 
HOH H2   H N N 182 
ILE N    N N N 183 
ILE CA   C N S 184 
ILE C    C N N 185 
ILE O    O N N 186 
ILE CB   C N S 187 
ILE CG1  C N N 188 
ILE CG2  C N N 189 
ILE CD1  C N N 190 
ILE OXT  O N N 191 
ILE H    H N N 192 
ILE H2   H N N 193 
ILE HA   H N N 194 
ILE HB   H N N 195 
ILE HG12 H N N 196 
ILE HG13 H N N 197 
ILE HG21 H N N 198 
ILE HG22 H N N 199 
ILE HG23 H N N 200 
ILE HD11 H N N 201 
ILE HD12 H N N 202 
ILE HD13 H N N 203 
ILE HXT  H N N 204 
LEU N    N N N 205 
LEU CA   C N S 206 
LEU C    C N N 207 
LEU O    O N N 208 
LEU CB   C N N 209 
LEU CG   C N N 210 
LEU CD1  C N N 211 
LEU CD2  C N N 212 
LEU OXT  O N N 213 
LEU H    H N N 214 
LEU H2   H N N 215 
LEU HA   H N N 216 
LEU HB2  H N N 217 
LEU HB3  H N N 218 
LEU HG   H N N 219 
LEU HD11 H N N 220 
LEU HD12 H N N 221 
LEU HD13 H N N 222 
LEU HD21 H N N 223 
LEU HD22 H N N 224 
LEU HD23 H N N 225 
LEU HXT  H N N 226 
LYS N    N N N 227 
LYS CA   C N S 228 
LYS C    C N N 229 
LYS O    O N N 230 
LYS CB   C N N 231 
LYS CG   C N N 232 
LYS CD   C N N 233 
LYS CE   C N N 234 
LYS NZ   N N N 235 
LYS OXT  O N N 236 
LYS H    H N N 237 
LYS H2   H N N 238 
LYS HA   H N N 239 
LYS HB2  H N N 240 
LYS HB3  H N N 241 
LYS HG2  H N N 242 
LYS HG3  H N N 243 
LYS HD2  H N N 244 
LYS HD3  H N N 245 
LYS HE2  H N N 246 
LYS HE3  H N N 247 
LYS HZ1  H N N 248 
LYS HZ2  H N N 249 
LYS HZ3  H N N 250 
LYS HXT  H N N 251 
MET N    N N N 252 
MET CA   C N S 253 
MET C    C N N 254 
MET O    O N N 255 
MET CB   C N N 256 
MET CG   C N N 257 
MET SD   S N N 258 
MET CE   C N N 259 
MET OXT  O N N 260 
MET H    H N N 261 
MET H2   H N N 262 
MET HA   H N N 263 
MET HB2  H N N 264 
MET HB3  H N N 265 
MET HG2  H N N 266 
MET HG3  H N N 267 
MET HE1  H N N 268 
MET HE2  H N N 269 
MET HE3  H N N 270 
MET HXT  H N N 271 
PHE N    N N N 272 
PHE CA   C N S 273 
PHE C    C N N 274 
PHE O    O N N 275 
PHE CB   C N N 276 
PHE CG   C Y N 277 
PHE CD1  C Y N 278 
PHE CD2  C Y N 279 
PHE CE1  C Y N 280 
PHE CE2  C Y N 281 
PHE CZ   C Y N 282 
PHE OXT  O N N 283 
PHE H    H N N 284 
PHE H2   H N N 285 
PHE HA   H N N 286 
PHE HB2  H N N 287 
PHE HB3  H N N 288 
PHE HD1  H N N 289 
PHE HD2  H N N 290 
PHE HE1  H N N 291 
PHE HE2  H N N 292 
PHE HZ   H N N 293 
PHE HXT  H N N 294 
SER N    N N N 295 
SER CA   C N S 296 
SER C    C N N 297 
SER O    O N N 298 
SER CB   C N N 299 
SER OG   O N N 300 
SER OXT  O N N 301 
SER H    H N N 302 
SER H2   H N N 303 
SER HA   H N N 304 
SER HB2  H N N 305 
SER HB3  H N N 306 
SER HG   H N N 307 
SER HXT  H N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
ZFJ C10  C Y N 396 
ZFJ C13  C Y N 397 
ZFJ C15  C N N 398 
ZFJ C17  C N N 399 
ZFJ C20  C N N 400 
ZFJ C21  C N N 401 
ZFJ C22  C N N 402 
ZFJ C01  C Y N 403 
ZFJ C02  C Y N 404 
ZFJ C03  C Y N 405 
ZFJ C04  C Y N 406 
ZFJ C05  C Y N 407 
ZFJ C06  C Y N 408 
ZFJ C07  C Y N 409 
ZFJ C08  C Y N 410 
ZFJ C09  C N N 411 
ZFJ C11  C Y N 412 
ZFJ C12  C Y N 413 
ZFJ C14  C N N 414 
ZFJ C18  C N N 415 
ZFJ C19  C N N 416 
ZFJ C23  C N N 417 
ZFJ N16  N N N 418 
ZFJ H1   H N N 419 
ZFJ H2   H N N 420 
ZFJ H3   H N N 421 
ZFJ H4   H N N 422 
ZFJ H5   H N N 423 
ZFJ H6   H N N 424 
ZFJ H7   H N N 425 
ZFJ H8   H N N 426 
ZFJ H9   H N N 427 
ZFJ H10  H N N 428 
ZFJ H11  H N N 429 
ZFJ H12  H N N 430 
ZFJ H13  H N N 431 
ZFJ H14  H N N 432 
ZFJ H15  H N N 433 
ZFJ H16  H N N 434 
ZFJ H17  H N N 435 
ZFJ H18  H N N 436 
ZFJ H19  H N N 437 
ZFJ H20  H N N 438 
ZFJ H21  H N N 439 
ZFJ H22  H N N 440 
ZFJ H23  H N N 441 
ZFJ H24  H N N 442 
ZFJ H25  H N N 443 
ZFJ H26  H N N 444 
ZFJ H27  H N N 445 
# 
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 
ACY C   O    doub N N 1   
ACY C   OXT  sing N N 2   
ACY C   CH3  sing N N 3   
ACY OXT HXT  sing N N 4   
ACY CH3 H1   sing N N 5   
ACY CH3 H2   sing N N 6   
ACY CH3 H3   sing N N 7   
ALA N   CA   sing N N 8   
ALA N   H    sing N N 9   
ALA N   H2   sing N N 10  
ALA CA  C    sing N N 11  
ALA CA  CB   sing N N 12  
ALA CA  HA   sing N N 13  
ALA C   O    doub N N 14  
ALA C   OXT  sing N N 15  
ALA CB  HB1  sing N N 16  
ALA CB  HB2  sing N N 17  
ALA CB  HB3  sing N N 18  
ALA OXT HXT  sing N N 19  
ARG N   CA   sing N N 20  
ARG N   H    sing N N 21  
ARG N   H2   sing N N 22  
ARG CA  C    sing N N 23  
ARG CA  CB   sing N N 24  
ARG CA  HA   sing N N 25  
ARG C   O    doub N N 26  
ARG C   OXT  sing N N 27  
ARG CB  CG   sing N N 28  
ARG CB  HB2  sing N N 29  
ARG CB  HB3  sing N N 30  
ARG CG  CD   sing N N 31  
ARG CG  HG2  sing N N 32  
ARG CG  HG3  sing N N 33  
ARG CD  NE   sing N N 34  
ARG CD  HD2  sing N N 35  
ARG CD  HD3  sing N N 36  
ARG NE  CZ   sing N N 37  
ARG NE  HE   sing N N 38  
ARG CZ  NH1  sing N N 39  
ARG CZ  NH2  doub N N 40  
ARG NH1 HH11 sing N N 41  
ARG NH1 HH12 sing N N 42  
ARG NH2 HH21 sing N N 43  
ARG NH2 HH22 sing N N 44  
ARG OXT HXT  sing N N 45  
ASN N   CA   sing N N 46  
ASN N   H    sing N N 47  
ASN N   H2   sing N N 48  
ASN CA  C    sing N N 49  
ASN CA  CB   sing N N 50  
ASN CA  HA   sing N N 51  
ASN C   O    doub N N 52  
ASN C   OXT  sing N N 53  
ASN CB  CG   sing N N 54  
ASN CB  HB2  sing N N 55  
ASN CB  HB3  sing N N 56  
ASN CG  OD1  doub N N 57  
ASN CG  ND2  sing N N 58  
ASN ND2 HD21 sing N N 59  
ASN ND2 HD22 sing N N 60  
ASN OXT HXT  sing N N 61  
ASP N   CA   sing N N 62  
ASP N   H    sing N N 63  
ASP N   H2   sing N N 64  
ASP CA  C    sing N N 65  
ASP CA  CB   sing N N 66  
ASP CA  HA   sing N N 67  
ASP C   O    doub N N 68  
ASP C   OXT  sing N N 69  
ASP CB  CG   sing N N 70  
ASP CB  HB2  sing N N 71  
ASP CB  HB3  sing N N 72  
ASP CG  OD1  doub N N 73  
ASP CG  OD2  sing N N 74  
ASP OD2 HD2  sing N N 75  
ASP OXT HXT  sing N N 76  
CYS N   CA   sing N N 77  
CYS N   H    sing N N 78  
CYS N   H2   sing N N 79  
CYS CA  C    sing N N 80  
CYS CA  CB   sing N N 81  
CYS CA  HA   sing N N 82  
CYS C   O    doub N N 83  
CYS C   OXT  sing N N 84  
CYS CB  SG   sing N N 85  
CYS CB  HB2  sing N N 86  
CYS CB  HB3  sing N N 87  
CYS SG  HG   sing N N 88  
CYS OXT HXT  sing N N 89  
GLN N   CA   sing N N 90  
GLN N   H    sing N N 91  
GLN N   H2   sing N N 92  
GLN CA  C    sing N N 93  
GLN CA  CB   sing N N 94  
GLN CA  HA   sing N N 95  
GLN C   O    doub N N 96  
GLN C   OXT  sing N N 97  
GLN CB  CG   sing N N 98  
GLN CB  HB2  sing N N 99  
GLN CB  HB3  sing N N 100 
GLN CG  CD   sing N N 101 
GLN CG  HG2  sing N N 102 
GLN CG  HG3  sing N N 103 
GLN CD  OE1  doub N N 104 
GLN CD  NE2  sing N N 105 
GLN NE2 HE21 sing N N 106 
GLN NE2 HE22 sing N N 107 
GLN OXT HXT  sing N N 108 
GLU N   CA   sing N N 109 
GLU N   H    sing N N 110 
GLU N   H2   sing N N 111 
GLU CA  C    sing N N 112 
GLU CA  CB   sing N N 113 
GLU CA  HA   sing N N 114 
GLU C   O    doub N N 115 
GLU C   OXT  sing N N 116 
GLU CB  CG   sing N N 117 
GLU CB  HB2  sing N N 118 
GLU CB  HB3  sing N N 119 
GLU CG  CD   sing N N 120 
GLU CG  HG2  sing N N 121 
GLU CG  HG3  sing N N 122 
GLU CD  OE1  doub N N 123 
GLU CD  OE2  sing N N 124 
GLU OE2 HE2  sing N N 125 
GLU OXT HXT  sing N N 126 
GLY N   CA   sing N N 127 
GLY N   H    sing N N 128 
GLY N   H2   sing N N 129 
GLY CA  C    sing N N 130 
GLY CA  HA2  sing N N 131 
GLY CA  HA3  sing N N 132 
GLY C   O    doub N N 133 
GLY C   OXT  sing N N 134 
GLY OXT HXT  sing N N 135 
GOL C1  O1   sing N N 136 
GOL C1  C2   sing N N 137 
GOL C1  H11  sing N N 138 
GOL C1  H12  sing N N 139 
GOL O1  HO1  sing N N 140 
GOL C2  O2   sing N N 141 
GOL C2  C3   sing N N 142 
GOL C2  H2   sing N N 143 
GOL O2  HO2  sing N N 144 
GOL C3  O3   sing N N 145 
GOL C3  H31  sing N N 146 
GOL C3  H32  sing N N 147 
GOL O3  HO3  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
SER N   CA   sing N N 280 
SER N   H    sing N N 281 
SER N   H2   sing N N 282 
SER CA  C    sing N N 283 
SER CA  CB   sing N N 284 
SER CA  HA   sing N N 285 
SER C   O    doub N N 286 
SER C   OXT  sing N N 287 
SER CB  OG   sing N N 288 
SER CB  HB2  sing N N 289 
SER CB  HB3  sing N N 290 
SER OG  HG   sing N N 291 
SER OXT HXT  sing N N 292 
THR N   CA   sing N N 293 
THR N   H    sing N N 294 
THR N   H2   sing N N 295 
THR CA  C    sing N N 296 
THR CA  CB   sing N N 297 
THR CA  HA   sing N N 298 
THR C   O    doub N N 299 
THR C   OXT  sing N N 300 
THR CB  OG1  sing N N 301 
THR CB  CG2  sing N N 302 
THR CB  HB   sing N N 303 
THR OG1 HG1  sing N N 304 
THR CG2 HG21 sing N N 305 
THR CG2 HG22 sing N N 306 
THR CG2 HG23 sing N N 307 
THR OXT HXT  sing N N 308 
TRP N   CA   sing N N 309 
TRP N   H    sing N N 310 
TRP N   H2   sing N N 311 
TRP CA  C    sing N N 312 
TRP CA  CB   sing N N 313 
TRP CA  HA   sing N N 314 
TRP C   O    doub N N 315 
TRP C   OXT  sing N N 316 
TRP CB  CG   sing N N 317 
TRP CB  HB2  sing N N 318 
TRP CB  HB3  sing N N 319 
TRP CG  CD1  doub Y N 320 
TRP CG  CD2  sing Y N 321 
TRP CD1 NE1  sing Y N 322 
TRP CD1 HD1  sing N N 323 
TRP CD2 CE2  doub Y N 324 
TRP CD2 CE3  sing Y N 325 
TRP NE1 CE2  sing Y N 326 
TRP NE1 HE1  sing N N 327 
TRP CE2 CZ2  sing Y N 328 
TRP CE3 CZ3  doub Y N 329 
TRP CE3 HE3  sing N N 330 
TRP CZ2 CH2  doub Y N 331 
TRP CZ2 HZ2  sing N N 332 
TRP CZ3 CH2  sing Y N 333 
TRP CZ3 HZ3  sing N N 334 
TRP CH2 HH2  sing N N 335 
TRP OXT HXT  sing N N 336 
TYR N   CA   sing N N 337 
TYR N   H    sing N N 338 
TYR N   H2   sing N N 339 
TYR CA  C    sing N N 340 
TYR CA  CB   sing N N 341 
TYR CA  HA   sing N N 342 
TYR C   O    doub N N 343 
TYR C   OXT  sing N N 344 
TYR CB  CG   sing N N 345 
TYR CB  HB2  sing N N 346 
TYR CB  HB3  sing N N 347 
TYR CG  CD1  doub Y N 348 
TYR CG  CD2  sing Y N 349 
TYR CD1 CE1  sing Y N 350 
TYR CD1 HD1  sing N N 351 
TYR CD2 CE2  doub Y N 352 
TYR CD2 HD2  sing N N 353 
TYR CE1 CZ   doub Y N 354 
TYR CE1 HE1  sing N N 355 
TYR CE2 CZ   sing Y N 356 
TYR CE2 HE2  sing N N 357 
TYR CZ  OH   sing N N 358 
TYR OH  HH   sing N N 359 
TYR OXT HXT  sing N N 360 
VAL N   CA   sing N N 361 
VAL N   H    sing N N 362 
VAL N   H2   sing N N 363 
VAL CA  C    sing N N 364 
VAL CA  CB   sing N N 365 
VAL CA  HA   sing N N 366 
VAL C   O    doub N N 367 
VAL C   OXT  sing N N 368 
VAL CB  CG1  sing N N 369 
VAL CB  CG2  sing N N 370 
VAL CB  HB   sing N N 371 
VAL CG1 HG11 sing N N 372 
VAL CG1 HG12 sing N N 373 
VAL CG1 HG13 sing N N 374 
VAL CG2 HG21 sing N N 375 
VAL CG2 HG22 sing N N 376 
VAL CG2 HG23 sing N N 377 
VAL OXT HXT  sing N N 378 
ZFJ C23 C22  sing N N 379 
ZFJ C21 C22  doub N E 380 
ZFJ C21 C12  sing N N 381 
ZFJ C11 C12  doub Y N 382 
ZFJ C11 C10  sing Y N 383 
ZFJ C12 C13  sing Y N 384 
ZFJ C10 C07  doub Y N 385 
ZFJ C13 C08  doub Y N 386 
ZFJ C07 C08  sing Y N 387 
ZFJ C07 C06  sing N N 388 
ZFJ C08 C09  sing N N 389 
ZFJ C06 C05  doub Y N 390 
ZFJ C06 C01  sing Y N 391 
ZFJ C05 C04  sing Y N 392 
ZFJ C14 C09  sing N N 393 
ZFJ C09 C01  sing N N 394 
ZFJ C09 C15  sing N N 395 
ZFJ C01 C02  doub Y N 396 
ZFJ C04 C03  doub Y N 397 
ZFJ C02 C03  sing Y N 398 
ZFJ C03 N16  sing N N 399 
ZFJ C18 C17  sing N N 400 
ZFJ N16 C17  sing N N 401 
ZFJ N16 C19  sing N N 402 
ZFJ C20 C19  sing N N 403 
ZFJ C10 H1   sing N N 404 
ZFJ C13 H2   sing N N 405 
ZFJ C15 H3   sing N N 406 
ZFJ C15 H4   sing N N 407 
ZFJ C15 H5   sing N N 408 
ZFJ C17 H6   sing N N 409 
ZFJ C17 H7   sing N N 410 
ZFJ C20 H8   sing N N 411 
ZFJ C20 H9   sing N N 412 
ZFJ C20 H10  sing N N 413 
ZFJ C21 H11  sing N N 414 
ZFJ C22 H12  sing N N 415 
ZFJ C02 H13  sing N N 416 
ZFJ C04 H14  sing N N 417 
ZFJ C05 H15  sing N N 418 
ZFJ C11 H16  sing N N 419 
ZFJ C14 H17  sing N N 420 
ZFJ C14 H18  sing N N 421 
ZFJ C14 H19  sing N N 422 
ZFJ C18 H20  sing N N 423 
ZFJ C18 H21  sing N N 424 
ZFJ C18 H22  sing N N 425 
ZFJ C19 H23  sing N N 426 
ZFJ C19 H24  sing N N 427 
ZFJ C23 H25  sing N N 428 
ZFJ C23 H26  sing N N 429 
ZFJ C23 H27  sing N N 430 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Biomedical Imaging and Bioengineering (NIH/NIBIB)' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4QYP 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DDU 
_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]   0.032236 
_atom_sites.fract_transf_matrix[1][2]   -0.014841 
_atom_sites.fract_transf_matrix[1][3]   -0.001245 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.030632 
_atom_sites.fract_transf_matrix[2][3]   -0.001493 
_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]   0.015662 
_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 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . THR A 1 1   ? -7.82900  -5.37900  35.29700  1.000 35.89000 ? 1   THR B N   1 
ATOM   2    C CA  . THR A 1 1   ? -7.17800  -6.48100  36.00000  1.000 38.67000 ? 1   THR B CA  1 
ATOM   3    C C   . THR A 1 1   ? -5.75000  -6.11800  36.38900  1.000 38.13000 ? 1   THR B C   1 
ATOM   4    O O   . THR A 1 1   ? -5.20700  -5.12200  35.91400  1.000 39.25000 ? 1   THR B O   1 
ATOM   5    C CB  . THR A 1 1   ? -7.15400  -7.76900  35.14600  1.000 45.54000 ? 1   THR B CB  1 
ATOM   6    O OG1 . THR A 1 1   ? -6.52700  -8.82100  35.88700  1.000 44.16000 ? 1   THR B OG1 1 
ATOM   7    C CG2 . THR A 1 1   ? -6.37800  -7.54900  33.85200  1.000 36.82000 ? 1   THR B CG2 1 
ATOM   8    N N   . ARG A 1 2   ? -5.14200  -6.92500  37.25600  1.000 28.74000 ? 2   ARG B N   1 
ATOM   9    C CA  . ARG A 1 2   ? -3.76500  -6.71100  37.67800  1.000 31.27000 ? 2   ARG B CA  1 
ATOM   10   C C   . ARG A 1 2   ? -2.76400  -7.55800  36.89500  1.000 35.43000 ? 2   ARG B C   1 
ATOM   11   O O   . ARG A 1 2   ? -1.57400  -7.53700  37.21900  1.000 42.39000 ? 2   ARG B O   1 
ATOM   12   C CB  . ARG A 1 2   ? -3.62200  -6.98400  39.17800  1.000 36.64000 ? 2   ARG B CB  1 
ATOM   13   C CG  . ARG A 1 2   ? -4.02100  -5.80500  40.07500  1.000 34.22000 ? 2   ARG B CG  1 
ATOM   14   C CD  . ARG A 1 2   ? -3.61800  -6.03000  41.53500  1.000 30.74000 ? 2   ARG B CD  1 
ATOM   15   N NE  . ARG A 1 2   ? -4.00900  -4.90200  42.38500  1.000 34.08000 ? 2   ARG B NE  1 
ATOM   16   C CZ  . ARG A 1 2   ? -4.07300  -4.93700  43.71600  1.000 38.07000 ? 2   ARG B CZ  1 
ATOM   17   N NH1 . ARG A 1 2   ? -3.77000  -6.05100  44.36700  1.000 35.94000 ? 2   ARG B NH1 1 
ATOM   18   N NH2 . ARG A 1 2   ? -4.44400  -3.85100  44.39700  1.000 32.28000 ? 2   ARG B NH2 1 
ATOM   19   N N   . ASP A 1 3   ? -3.20600  -8.29200  35.87100  1.000 34.46000 ? 3   ASP B N   1 
ATOM   20   C CA  . ASP A 1 3   ? -2.32000  -9.14900  35.07700  1.000 33.41000 ? 3   ASP B CA  1 
ATOM   21   C C   . ASP A 1 3   ? -1.98700  -8.45300  33.75800  1.000 28.50000 ? 3   ASP B C   1 
ATOM   22   O O   . ASP A 1 3   ? -2.83200  -8.35400  32.86200  1.000 27.73000 ? 3   ASP B O   1 
ATOM   23   C CB  . ASP A 1 3   ? -2.96100  -10.51500 34.82800  1.000 32.71000 ? 3   ASP B CB  1 
ATOM   24   C CG  . ASP A 1 3   ? -2.03600  -11.47300 34.07600  1.000 37.05000 ? 3   ASP B CG  1 
ATOM   25   O OD1 . ASP A 1 3   ? -0.97300  -11.03400 33.58000  1.000 33.32000 ? 3   ASP B OD1 1 
ATOM   26   O OD2 . ASP A 1 3   ? -2.37700  -12.67300 33.98300  1.000 39.35000 ? 3   ASP B OD2 1 
ATOM   27   N N   . ALA A 1 4   ? -0.74700  -7.98500  33.63600  1.000 27.51000 ? 4   ALA B N   1 
ATOM   28   C CA  . ALA A 1 4   ? -0.30700  -7.20700  32.49000  1.000 23.83000 ? 4   ALA B CA  1 
ATOM   29   C C   . ALA A 1 4   ? 0.52500   -8.02400  31.51400  1.000 25.00000 ? 4   ALA B C   1 
ATOM   30   O O   . ALA A 1 4   ? 1.05500   -7.46800  30.54700  1.000 21.34000 ? 4   ALA B O   1 
ATOM   31   C CB  . ALA A 1 4   ? 0.48800   -5.98900  32.97000  1.000 24.67000 ? 4   ALA B CB  1 
ATOM   32   N N   . ASN A 1 5   ? 0.66100   -9.32800  31.75800  1.000 21.73000 ? 5   ASN B N   1 
ATOM   33   C CA  . ASN A 1 5   ? 1.44600   -10.20400 30.89000  1.000 23.43000 ? 5   ASN B CA  1 
ATOM   34   C C   . ASN A 1 5   ? 1.01600   -10.08100 29.43300  1.000 24.86000 ? 5   ASN B C   1 
ATOM   35   O O   . ASN A 1 5   ? -0.17600  -10.07100 29.12300  1.000 25.61000 ? 5   ASN B O   1 
ATOM   36   C CB  . ASN A 1 5   ? 1.26500   -11.66200 31.32800  1.000 26.06000 ? 5   ASN B CB  1 
ATOM   37   C CG  . ASN A 1 5   ? 2.21300   -12.06700 32.42400  1.000 23.07000 ? 5   ASN B CG  1 
ATOM   38   O OD1 . ASN A 1 5   ? 3.40600   -12.21400 32.19000  1.000 23.88000 ? 5   ASN B OD1 1 
ATOM   39   N ND2 . ASN A 1 5   ? 1.68400   -12.27100 33.62600  1.000 24.77000 ? 5   ASN B ND2 1 
ATOM   40   N N   . GLY A 1 6   ? 1.98200   -10.04400 28.53400  1.000 22.17000 ? 6   GLY B N   1 
ATOM   41   C CA  . GLY A 1 6   ? 1.65900   -10.20600 27.12800  1.000 26.26000 ? 6   GLY B CA  1 
ATOM   42   C C   . GLY A 1 6   ? 2.61000   -9.44000  26.23100  1.000 24.48000 ? 6   GLY B C   1 
ATOM   43   O O   . GLY A 1 6   ? 3.50100   -8.72400  26.68400  1.000 22.23000 ? 6   GLY B O   1 
ATOM   44   N N   . THR A 1 7   ? 2.41000   -9.64200  24.93000  1.000 20.93000 ? 7   THR B N   1 
ATOM   45   C CA  . THR A 1 7   ? 2.99600   -8.81100  23.88900  1.000 20.94000 ? 7   THR B CA  1 
ATOM   46   C C   . THR A 1 7   ? 1.94000   -7.82400  23.42500  1.000 21.34000 ? 7   THR B C   1 
ATOM   47   O O   . THR A 1 7   ? 0.82800   -8.22500  23.06100  1.000 23.66000 ? 7   THR B O   1 
ATOM   48   C CB  . THR A 1 7   ? 3.48400   -9.64300  22.70300  1.000 26.31000 ? 7   THR B CB  1 
ATOM   49   O OG1 . THR A 1 7   ? 4.44600   -10.59100 23.15900  1.000 25.98000 ? 7   THR B OG1 1 
ATOM   50   C CG2 . THR A 1 7   ? 4.11900   -8.73900  21.65000  1.000 28.13000 ? 7   THR B CG2 1 
ATOM   51   N N   . TRP A 1 8   ? 2.27800   -6.54000  23.46700  1.000 19.03000 ? 8   TRP B N   1 
ATOM   52   C CA  . TRP A 1 8   ? 1.30800   -5.47100  23.31300  1.000 18.74000 ? 8   TRP B CA  1 
ATOM   53   C C   . TRP A 1 8   ? 1.71900   -4.60100  22.13700  1.000 19.60000 ? 8   TRP B C   1 
ATOM   54   O O   . TRP A 1 8   ? 2.86600   -4.13900  22.07500  1.000 21.30000 ? 8   TRP B O   1 
ATOM   55   C CB  . TRP A 1 8   ? 1.23100   -4.64500  24.60300  1.000 18.55000 ? 8   TRP B CB  1 
ATOM   56   C CG  . TRP A 1 8   ? 0.79000   -5.41500  25.82000  1.000 19.61000 ? 8   TRP B CG  1 
ATOM   57   C CD1 . TRP A 1 8   ? 1.59300   -6.04600  26.73400  1.000 19.99000 ? 8   TRP B CD1 1 
ATOM   58   C CD2 . TRP A 1 8   ? -0.55800  -5.61100  26.26800  1.000 16.66000 ? 8   TRP B CD2 1 
ATOM   59   N NE1 . TRP A 1 8   ? 0.82300   -6.62000  27.72500  1.000 21.34000 ? 8   TRP B NE1 1 
ATOM   60   C CE2 . TRP A 1 8   ? -0.49800  -6.37000  27.46100  1.000 19.39000 ? 8   TRP B CE2 1 
ATOM   61   C CE3 . TRP A 1 8   ? -1.81300  -5.21200  25.77900  1.000 17.42000 ? 8   TRP B CE3 1 
ATOM   62   C CZ2 . TRP A 1 8   ? -1.64000  -6.74200  28.16900  1.000 20.03000 ? 8   TRP B CZ2 1 
ATOM   63   C CZ3 . TRP A 1 8   ? -2.94800  -5.58300  26.48000  1.000 17.85000 ? 8   TRP B CZ3 1 
ATOM   64   C CH2 . TRP A 1 8   ? -2.84900  -6.34000  27.67200  1.000 21.83000 ? 8   TRP B CH2 1 
ATOM   65   N N   . GLU A 1 9   ? 0.80400   -4.41500  21.19300  1.000 21.99000 ? 9   GLU B N   1 
ATOM   66   C CA  . GLU A 1 9   ? 1.07100   -3.63700  19.99200  1.000 19.96000 ? 9   GLU B CA  1 
ATOM   67   C C   . GLU A 1 9   ? 0.38900   -2.28000  20.09600  1.000 22.21000 ? 9   GLU B C   1 
ATOM   68   O O   . GLU A 1 9   ? -0.78800  -2.18700  20.46200  1.000 20.49000 ? 9   GLU B O   1 
ATOM   69   C CB  . GLU A 1 9   ? 0.58800   -4.37700  18.73900  1.000 29.65000 ? 9   GLU B CB  1 
ATOM   70   C CG  . GLU A 1 9   ? 1.18700   -5.76800  18.57300  1.000 31.77000 ? 9   GLU B CG  1 
ATOM   71   C CD  . GLU A 1 9   ? 2.68300   -5.73800  18.29600  1.000 42.39000 ? 9   GLU B CD  1 
ATOM   72   O OE1 . GLU A 1 9   ? 3.22700   -4.63900  18.04800  1.000 45.36000 ? 9   GLU B OE1 1 
ATOM   73   O OE2 . GLU A 1 9   ? 3.32000   -6.81500  18.33500  1.000 46.85000 ? 9   GLU B OE2 1 
ATOM   74   N N   . MET A 1 10  ? 1.12400   -1.23100  19.74900  1.000 24.31000 ? 10  MET B N   1 
ATOM   75   C CA  . MET A 1 10  ? 0.58200   0.11200   19.87600  1.000 27.49000 ? 10  MET B CA  1 
ATOM   76   C C   . MET A 1 10  ? -0.56400  0.33300   18.89500  1.000 28.02000 ? 10  MET B C   1 
ATOM   77   O O   . MET A 1 10  ? -0.51300  -0.08500  17.73400  1.000 31.27000 ? 10  MET B O   1 
ATOM   78   C CB  . MET A 1 10  ? 1.67800   1.14800   19.65400  1.000 27.04000 ? 10  MET B CB  1 
ATOM   79   C CG  . MET A 1 10  ? 1.14000   2.55300   19.50600  1.000 26.95000 ? 10  MET B CG  1 
ATOM   80   S SD  . MET A 1 10  ? 2.49200   3.73000   19.57100  1.000 39.20000 ? 10  MET B SD  1 
ATOM   81   C CE  . MET A 1 10  ? 3.00900   3.55700   21.26100  1.000 19.62000 ? 10  MET B CE  1 
ATOM   82   N N   . GLU A 1 11  ? -1.60300  0.99500   19.37700  1.000 25.32000 ? 11  GLU B N   1 
ATOM   83   C CA  . GLU A 1 11  ? -2.76100  1.38300   18.58500  1.000 26.97000 ? 11  GLU B CA  1 
ATOM   84   C C   . GLU A 1 11  ? -2.91700  2.88600   18.46800  1.000 27.90000 ? 11  GLU B C   1 
ATOM   85   O O   . GLU A 1 11  ? -3.44100  3.37300   17.46100  1.000 23.33000 ? 11  GLU B O   1 
ATOM   86   C CB  . GLU A 1 11  ? -4.04400  0.82200   19.21500  1.000 33.32000 ? 11  GLU B CB  1 
ATOM   87   C CG  . GLU A 1 11  ? -4.58500  -0.43700  18.58200  1.000 47.24000 ? 11  GLU B CG  1 
ATOM   88   C CD  . GLU A 1 11  ? -6.05400  -0.65000  18.91700  1.000 52.14000 ? 11  GLU B CD  1 
ATOM   89   O OE1 . GLU A 1 11  ? -6.68600  0.29200   19.44600  1.000 54.57000 ? 11  GLU B OE1 1 
ATOM   90   O OE2 . GLU A 1 11  ? -6.57300  -1.75600  18.66100  1.000 49.56000 ? 11  GLU B OE2 1 
ATOM   91   N N   . SER A 1 12  ? -2.49900  3.62800   19.48800  1.000 21.75000 ? 12  SER B N   1 
ATOM   92   C CA  . SER A 1 12  ? -2.69100  5.06400   19.55900  1.000 21.73000 ? 12  SER B CA  1 
ATOM   93   C C   . SER A 1 12  ? -1.53300  5.63100   20.36200  1.000 20.85000 ? 12  SER B C   1 
ATOM   94   O O   . SER A 1 12  ? -0.98500  4.95600   21.23800  1.000 18.54000 ? 12  SER B O   1 
ATOM   95   C CB  . SER A 1 12  ? -4.03600  5.41600   20.21100  1.000 25.27000 ? 12  SER B CB  1 
ATOM   96   O OG  . SER A 1 12  ? -4.15900  6.81200   20.43500  1.000 32.80000 ? 12  SER B OG  1 
ATOM   97   N N   . ASN A 1 13  ? -1.15800  6.87400   20.05200  1.000 21.75000 ? 13  ASN B N   1 
ATOM   98   C CA  . ASN A 1 13  ? 0.01200   7.49600   20.68500  1.000 20.55000 ? 13  ASN B CA  1 
ATOM   99   C C   . ASN A 1 13  ? -0.16100  9.00700   20.54400  1.000 20.40000 ? 13  ASN B C   1 
ATOM   100  O O   . ASN A 1 13  ? 0.10000   9.55800   19.47100  1.000 28.81000 ? 13  ASN B O   1 
ATOM   101  C CB  . ASN A 1 13  ? 1.28800   7.01000   20.02500  1.000 22.95000 ? 13  ASN B CB  1 
ATOM   102  C CG  . ASN A 1 13  ? 2.55600   7.43400   20.76000  1.000 24.95000 ? 13  ASN B CG  1 
ATOM   103  O OD1 . ASN A 1 13  ? 2.51700   7.92900   21.89200  1.000 20.66000 ? 13  ASN B OD1 1 
ATOM   104  N ND2 . ASN A 1 13  ? 3.69300   7.22900   20.11000  1.000 26.56000 ? 13  ASN B ND2 1 
ATOM   105  N N   . GLU A 1 14  ? -0.63500  9.64800   21.61000  1.000 19.79000 ? 14  GLU B N   1 
ATOM   106  C CA  . GLU A 1 14  ? -0.96800  11.06600  21.61700  1.000 20.31000 ? 14  GLU B CA  1 
ATOM   107  C C   . GLU A 1 14  ? 0.07400   11.83600  22.41800  1.000 20.43000 ? 14  GLU B C   1 
ATOM   108  O O   . GLU A 1 14  ? 0.41700   11.43900  23.53500  1.000 17.73000 ? 14  GLU B O   1 
ATOM   109  C CB  . GLU A 1 14  ? -2.35900  11.28900  22.21500  1.000 24.05000 ? 14  GLU B CB  1 
ATOM   110  C CG  . GLU A 1 14  ? -3.44300  10.48600  21.52300  1.000 35.05000 ? 14  GLU B CG  1 
ATOM   111  C CD  . GLU A 1 14  ? -4.67800  10.29600  22.38600  1.000 41.24000 ? 14  GLU B CD  1 
ATOM   112  O OE1 . GLU A 1 14  ? -4.79200  10.97100  23.43300  1.000 42.84000 ? 14  GLU B OE1 1 
ATOM   113  O OE2 . GLU A 1 14  ? -5.54300  9.47400   22.00800  1.000 49.40000 ? 14  GLU B OE2 1 
ATOM   114  N N   . ASN A 1 15  ? 0.57300   12.93000  21.83700  1.000 21.09000 ? 15  ASN B N   1 
ATOM   115  C CA  . ASN A 1 15  ? 1.54300   13.83200  22.47400  1.000 19.39000 ? 15  ASN B CA  1 
ATOM   116  C C   . ASN A 1 15  ? 2.85200   13.13400  22.83900  1.000 20.22000 ? 15  ASN B C   1 
ATOM   117  O O   . ASN A 1 15  ? 3.49900   13.49200  23.82000  1.000 19.45000 ? 15  ASN B O   1 
ATOM   118  C CB  . ASN A 1 15  ? 0.95400   14.52300  23.70700  1.000 22.26000 ? 15  ASN B CB  1 
ATOM   119  C CG  . ASN A 1 15  ? 1.80100   15.70900  24.16400  1.000 21.52000 ? 15  ASN B CG  1 
ATOM   120  O OD1 . ASN A 1 15  ? 2.41100   16.38600  23.34200  1.000 25.64000 ? 15  ASN B OD1 1 
ATOM   121  N ND2 . ASN A 1 15  ? 1.87400   15.93700  25.47300  1.000 18.19000 ? 15  ASN B ND2 1 
ATOM   122  N N   . PHE A 1 16  ? 3.28300   12.17900  22.00800  1.000 18.99000 ? 16  PHE B N   1 
ATOM   123  C CA  . PHE A 1 16  ? 4.59100   11.54700  22.18600  1.000 17.62000 ? 16  PHE B CA  1 
ATOM   124  C C   . PHE A 1 16  ? 5.71400   12.57200  22.07200  1.000 22.10000 ? 16  PHE B C   1 
ATOM   125  O O   . PHE A 1 16  ? 6.65400   12.57500  22.87600  1.000 18.94000 ? 16  PHE B O   1 
ATOM   126  C CB  . PHE A 1 16  ? 4.75000   10.44300  21.13300  1.000 23.20000 ? 16  PHE B CB  1 
ATOM   127  C CG  . PHE A 1 16  ? 5.88600   9.47700   21.37000  1.000 20.85000 ? 16  PHE B CG  1 
ATOM   128  C CD1 . PHE A 1 16  ? 6.07100   8.86200   22.59800  1.000 22.01000 ? 16  PHE B CD1 1 
ATOM   129  C CD2 . PHE A 1 16  ? 6.71000   9.10900   20.31700  1.000 28.43000 ? 16  PHE B CD2 1 
ATOM   130  C CE1 . PHE A 1 16  ? 7.09300   7.93600   22.78900  1.000 27.84000 ? 16  PHE B CE1 1 
ATOM   131  C CE2 . PHE A 1 16  ? 7.73200   8.19100   20.50400  1.000 27.14000 ? 16  PHE B CE2 1 
ATOM   132  C CZ  . PHE A 1 16  ? 7.92400   7.60400   21.73900  1.000 28.60000 ? 16  PHE B CZ  1 
ATOM   133  N N   . GLU A 1 17  ? 5.62800   13.46300  21.08500  1.000 22.57000 ? 17  GLU B N   1 
ATOM   134  C CA  . GLU A 1 17  ? 6.71700   14.40700  20.86800  1.000 22.45000 ? 17  GLU B CA  1 
ATOM   135  C C   . GLU A 1 17  ? 6.80000   15.42000  22.00400  1.000 21.31000 ? 17  GLU B C   1 
ATOM   136  O O   . GLU A 1 17  ? 7.89900   15.81500  22.40500  1.000 21.25000 ? 17  GLU B O   1 
ATOM   137  C CB  . GLU A 1 17  ? 6.54200   15.10600  19.51700  1.000 28.28000 ? 17  GLU B CB  1 
ATOM   138  C CG  . GLU A 1 17  ? 7.15300   14.34100  18.35200  1.000 36.00000 ? 17  GLU B CG  1 
ATOM   139  C CD  . GLU A 1 17  ? 7.96800   15.23400  17.43000  1.000 50.40000 ? 17  GLU B CD  1 
ATOM   140  O OE1 . GLU A 1 17  ? 7.38400   16.18700  16.87000  1.000 60.90000 ? 17  GLU B OE1 1 
ATOM   141  O OE2 . GLU A 1 17  ? 9.18300   14.98300  17.26000  1.000 48.79000 ? 17  GLU B OE2 1 
ATOM   142  N N   . GLY A 1 18  ? 5.65100   15.84800  22.53600  1.000 22.35000 ? 18  GLY B N   1 
ATOM   143  C CA  . GLY A 1 18  ? 5.65800   16.76000  23.67500  1.000 20.72000 ? 18  GLY B CA  1 
ATOM   144  C C   . GLY A 1 18  ? 6.25200   16.14000  24.92800  1.000 21.22000 ? 18  GLY B C   1 
ATOM   145  O O   . GLY A 1 18  ? 7.01900   16.78300  25.65200  1.000 19.14000 ? 18  GLY B O   1 
ATOM   146  N N   . TRP A 1 19  ? 5.92300   14.87700  25.19300  1.000 16.41000 ? 19  TRP B N   1 
ATOM   147  C CA  . TRP A 1 19  ? 6.52800   14.17400  26.32500  1.000 18.02000 ? 19  TRP B CA  1 
ATOM   148  C C   . TRP A 1 19  ? 8.04000   14.02200  26.14700  1.000 18.19000 ? 19  TRP B C   1 
ATOM   149  O O   . TRP A 1 19  ? 8.81500   14.22300  27.09000  1.000 17.78000 ? 19  TRP B O   1 
ATOM   150  C CB  . TRP A 1 19  ? 5.84300   12.81100  26.46800  1.000 18.44000 ? 19  TRP B CB  1 
ATOM   151  C CG  . TRP A 1 19  ? 6.49200   11.88700  27.43300  1.000 17.97000 ? 19  TRP B CG  1 
ATOM   152  C CD1 . TRP A 1 19  ? 6.45400   11.95700  28.80200  1.000 17.83000 ? 19  TRP B CD1 1 
ATOM   153  C CD2 . TRP A 1 19  ? 7.27700   10.73700  27.11000  1.000 18.48000 ? 19  TRP B CD2 1 
ATOM   154  N NE1 . TRP A 1 19  ? 7.17700   10.91700  29.34000  1.000 17.12000 ? 19  TRP B NE1 1 
ATOM   155  C CE2 . TRP A 1 19  ? 7.68800   10.15500  28.32200  1.000 17.63000 ? 19  TRP B CE2 1 
ATOM   156  C CE3 . TRP A 1 19  ? 7.66900   10.13800  25.90400  1.000 22.28000 ? 19  TRP B CE3 1 
ATOM   157  C CZ2 . TRP A 1 19  ? 8.47700   9.00000   28.36600  1.000 19.71000 ? 19  TRP B CZ2 1 
ATOM   158  C CZ3 . TRP A 1 19  ? 8.45000   9.00100   25.95000  1.000 21.47000 ? 19  TRP B CZ3 1 
ATOM   159  C CH2 . TRP A 1 19  ? 8.85000   8.44700   27.16700  1.000 22.28000 ? 19  TRP B CH2 1 
ATOM   160  N N   . MET A 1 20  ? 8.48200   13.64900  24.94100  1.000 16.31000 ? 20  MET B N   1 
ATOM   161  C CA  . MET A 1 20  ? 9.91400   13.49700  24.69000  1.000 16.24000 ? 20  MET B CA  1 
ATOM   162  C C   . MET A 1 20  ? 10.64000  14.83000  24.80500  1.000 17.57000 ? 20  MET B C   1 
ATOM   163  O O   . MET A 1 20  ? 11.78100  14.88500  25.29400  1.000 19.67000 ? 20  MET B O   1 
ATOM   164  C CB  . MET A 1 20  ? 10.14300  12.88900  23.30300  1.000 19.67000 ? 20  MET B CB  1 
ATOM   165  C CG  . MET A 1 20  ? 9.82600   11.41600  23.20400  1.000 18.57000 ? 20  MET B CG  1 
ATOM   166  S SD  . MET A 1 20  ? 10.40000  10.72400  21.63700  1.000 21.94000 ? 20  MET B SD  1 
ATOM   167  C CE  . MET A 1 20  ? 9.27300   11.48400  20.47600  1.000 25.17000 ? 20  MET B CE  1 
ATOM   168  N N   . LYS A 1 21  ? 10.00400  15.90300  24.34000  1.000 17.20000 ? 21  LYS B N   1 
ATOM   169  C CA  . LYS A 1 21  ? 10.58100  17.23900  24.47300  1.000 20.48000 ? 21  LYS B CA  1 
ATOM   170  C C   . LYS A 1 21  ? 10.71100  17.64200  25.93700  1.000 19.56000 ? 21  LYS B C   1 
ATOM   171  O O   . LYS A 1 21  ? 11.72900  18.21600  26.34400  1.000 20.99000 ? 21  LYS B O   1 
ATOM   172  C CB  . LYS A 1 21  ? 9.72000   18.24500  23.70400  1.000 22.57000 ? 21  LYS B CB  1 
ATOM   173  C CG  . LYS A 1 21  ? 10.29100  19.64800  23.64800  1.000 24.28000 ? 21  LYS B CG  1 
ATOM   174  C CD  . LYS A 1 21  ? 9.55200   20.49100  22.60900  1.000 33.84000 ? 21  LYS B CD  1 
ATOM   175  C CE  . LYS A 1 21  ? 8.05800   20.52300  22.86700  1.000 37.22000 ? 21  LYS B CE  1 
ATOM   176  N NZ  . LYS A 1 21  ? 7.38900   21.52400  21.98400  1.000 42.33000 ? 21  LYS B NZ  1 
ATOM   177  N N   . ALA A 1 22  ? 9.69900   17.32700  26.75000  1.000 18.13000 ? 22  ALA B N   1 
ATOM   178  C CA  . ALA A 1 22  ? 9.77900   17.58800  28.18500  1.000 19.59000 ? 22  ALA B CA  1 
ATOM   179  C C   . ALA A 1 22  ? 10.96700  16.87400  28.82800  1.000 21.67000 ? 22  ALA B C   1 
ATOM   180  O O   . ALA A 1 22  ? 11.54500  17.38100  29.80000  1.000 21.54000 ? 22  ALA B O   1 
ATOM   181  C CB  . ALA A 1 22  ? 8.46300   17.17500  28.86200  1.000 19.88000 ? 22  ALA B CB  1 
ATOM   182  N N   . LEU A 1 23  ? 11.34800  15.70500  28.30500  1.000 18.72000 ? 23  LEU B N   1 
ATOM   183  C CA  . LEU A 1 23  ? 12.49100  14.94600  28.80800  1.000 19.57000 ? 23  LEU B CA  1 
ATOM   184  C C   . LEU A 1 23  ? 13.81900  15.40400  28.21900  1.000 22.66000 ? 23  LEU B C   1 
ATOM   185  O O   . LEU A 1 23  ? 14.86300  14.86100  28.59200  1.000 24.71000 ? 23  LEU B O   1 
ATOM   186  C CB  . LEU A 1 23  ? 12.29900  13.44900  28.51100  1.000 20.86000 ? 23  LEU B CB  1 
ATOM   187  C CG  . LEU A 1 23  ? 11.25100  12.76200  29.37900  1.000 19.72000 ? 23  LEU B CG  1 
ATOM   188  C CD1 . LEU A 1 23  ? 10.82500  11.44200  28.78600  1.000 24.04000 ? 23  LEU B CD1 1 
ATOM   189  C CD2 . LEU A 1 23  ? 11.79900  12.55900  30.78300  1.000 22.39000 ? 23  LEU B CD2 1 
ATOM   190  N N   . ASP A 1 24  ? 13.80200  16.35400  27.28400  1.000 20.16000 ? 24  ASP B N   1 
ATOM   191  C CA  . ASP A 1 24  ? 15.00500  16.86900  26.64400  1.000 21.95000 ? 24  ASP B CA  1 
ATOM   192  C C   . ASP A 1 24  ? 15.67700  15.83500  25.74700  1.000 23.87000 ? 24  ASP B C   1 
ATOM   193  O O   . ASP A 1 24  ? 16.89300  15.87300  25.54200  1.000 31.17000 ? 24  ASP B O   1 
ATOM   194  C CB  . ASP A 1 24  ? 15.98500  17.40800  27.68600  1.000 22.58000 ? 24  ASP B CB  1 
ATOM   195  C CG  . ASP A 1 24  ? 15.30700  18.33400  28.67000  1.000 24.26000 ? 24  ASP B CG  1 
ATOM   196  O OD1 . ASP A 1 24  ? 14.75400  19.34200  28.19900  1.000 29.43000 ? 24  ASP B OD1 1 
ATOM   197  O OD2 . ASP A 1 24  ? 15.30100  18.04800  29.89000  1.000 27.61000 ? 24  ASP B OD2 1 
ATOM   198  N N   . ILE A 1 25  ? 14.88800  14.90600  25.20100  1.000 22.87000 ? 25  ILE B N   1 
ATOM   199  C CA  . ILE A 1 25  ? 15.37000  14.08100  24.10200  1.000 25.67000 ? 25  ILE B CA  1 
ATOM   200  C C   . ILE A 1 25  ? 15.64800  14.96000  22.88900  1.000 27.86000 ? 25  ILE B C   1 
ATOM   201  O O   . ILE A 1 25  ? 14.83600  15.81700  22.51400  1.000 26.69000 ? 25  ILE B O   1 
ATOM   202  C CB  . ILE A 1 25  ? 14.35000  12.98200  23.74800  1.000 27.27000 ? 25  ILE B CB  1 
ATOM   203  C CG1 . ILE A 1 25  ? 13.96200  12.15400  24.97400  1.000 29.89000 ? 25  ILE B CG1 1 
ATOM   204  C CG2 . ILE A 1 25  ? 14.90700  12.09900  22.65100  1.000 25.39000 ? 25  ILE B CG2 1 
ATOM   205  C CD1 . ILE A 1 25  ? 15.12100  11.49400  25.65700  1.000 29.40000 ? 25  ILE B CD1 1 
ATOM   206  N N   . ASP A 1 26  ? 16.78600  14.71600  22.24300  1.000 40.25000 ? 26  ASP B N   1 
ATOM   207  C CA  . ASP A 1 26  ? 17.19700  15.47000  21.06300  1.000 42.50000 ? 26  ASP B CA  1 
ATOM   208  C C   . ASP A 1 26  ? 16.08300  15.54700  20.01600  1.000 43.66000 ? 26  ASP B C   1 
ATOM   209  O O   . ASP A 1 26  ? 15.29700  14.61200  19.84200  1.000 41.12000 ? 26  ASP B O   1 
ATOM   210  C CB  . ASP A 1 26  ? 18.43900  14.81000  20.46500  1.000 50.16000 ? 26  ASP B CB  1 
ATOM   211  C CG  . ASP A 1 26  ? 19.36600  15.79600  19.78600  1.000 66.55000 ? 26  ASP B CG  1 
ATOM   212  O OD1 . ASP A 1 26  ? 18.96000  16.96100  19.57600  1.000 66.45000 ? 26  ASP B OD1 1 
ATOM   213  O OD2 . ASP A 1 26  ? 20.50100  15.38900  19.44900  1.000 69.18000 ? 26  ASP B OD2 1 
ATOM   214  N N   . PHE A 1 27  ? 16.03800  16.67400  19.29100  1.000 37.68000 ? 27  PHE B N   1 
ATOM   215  C CA  . PHE A 1 27  ? 15.01800  16.86300  18.25700  1.000 38.65000 ? 27  PHE B CA  1 
ATOM   216  C C   . PHE A 1 27  ? 15.18100  15.87100  17.10900  1.000 43.20000 ? 27  PHE B C   1 
ATOM   217  O O   . PHE A 1 27  ? 14.19100  15.49500  16.46900  1.000 39.45000 ? 27  PHE B O   1 
ATOM   218  C CB  . PHE A 1 27  ? 15.06500  18.29800  17.71900  1.000 40.79000 ? 27  PHE B CB  1 
ATOM   219  C CG  . PHE A 1 27  ? 14.12200  18.55500  16.56400  1.000 40.31000 ? 27  PHE B CG  1 
ATOM   220  C CD1 . PHE A 1 27  ? 12.83300  19.01900  16.78600  1.000 43.07000 ? 27  PHE B CD1 1 
ATOM   221  C CD2 . PHE A 1 27  ? 14.53100  18.34100  15.25500  1.000 45.52000 ? 27  PHE B CD2 1 
ATOM   222  C CE1 . PHE A 1 27  ? 11.96800  19.25700  15.72600  1.000 48.39000 ? 27  PHE B CE1 1 
ATOM   223  C CE2 . PHE A 1 27  ? 13.67300  18.57500  14.19400  1.000 50.33000 ? 27  PHE B CE2 1 
ATOM   224  C CZ  . PHE A 1 27  ? 12.38900  19.03300  14.42900  1.000 51.83000 ? 27  PHE B CZ  1 
ATOM   225  N N   . ALA A 1 28  ? 16.41800  15.45600  16.82000  1.000 48.11000 ? 28  ALA B N   1 
ATOM   226  C CA  . ALA A 1 28  ? 16.65300  14.47700  15.75900  1.000 47.09000 ? 28  ALA B CA  1 
ATOM   227  C C   . ALA A 1 28  ? 16.15300  13.09000  16.15900  1.000 42.48000 ? 28  ALA B C   1 
ATOM   228  O O   . ALA A 1 28  ? 15.52700  12.39600  15.34900  1.000 49.60000 ? 28  ALA B O   1 
ATOM   229  C CB  . ALA A 1 28  ? 18.14300  14.42900  15.41600  1.000 47.04000 ? 28  ALA B CB  1 
ATOM   230  N N   . LEU A 1 29  ? 16.43100  12.66000  17.39700  1.000 40.20000 ? 29  LEU B N   1 
ATOM   231  C CA  . LEU A 1 29  ? 15.96200  11.34800  17.83800  1.000 42.74000 ? 29  LEU B CA  1 
ATOM   232  C C   . LEU A 1 29  ? 14.45100  11.32900  18.03200  1.000 40.25000 ? 29  LEU B C   1 
ATOM   233  O O   . LEU A 1 29  ? 13.82000  10.28300  17.84600  1.000 31.63000 ? 29  LEU B O   1 
ATOM   234  C CB  . LEU A 1 29  ? 16.65900  10.92400  19.13100  1.000 43.45000 ? 29  LEU B CB  1 
ATOM   235  C CG  . LEU A 1 29  ? 18.15400  11.20900  19.28200  1.000 49.17000 ? 29  LEU B CG  1 
ATOM   236  C CD1 . LEU A 1 29  ? 18.56600  11.10700  20.74000  1.000 52.54000 ? 29  LEU B CD1 1 
ATOM   237  C CD2 . LEU A 1 29  ? 18.96900  10.25200  18.42800  1.000 53.78000 ? 29  LEU B CD2 1 
ATOM   238  N N   . ARG A 1 30  ? 13.85700  12.46300  18.42000  1.000 35.48000 ? 30  ARG B N   1 
ATOM   239  C CA  . ARG A 1 30  ? 12.40200  12.55400  18.44000  1.000 33.10000 ? 30  ARG B CA  1 
ATOM   240  C C   . ARG A 1 30  ? 11.83200  12.33800  17.05000  1.000 33.76000 ? 30  ARG B C   1 
ATOM   241  O O   . ARG A 1 30  ? 10.83200  11.63100  16.88300  1.000 33.69000 ? 30  ARG B O   1 
ATOM   242  C CB  . ARG A 1 30  ? 11.95800  13.91300  18.97700  1.000 34.88000 ? 30  ARG B CB  1 
ATOM   243  C CG  . ARG A 1 30  ? 12.49500  14.23200  20.34600  1.000 34.69000 ? 30  ARG B CG  1 
ATOM   244  C CD  . ARG A 1 30  ? 11.63800  15.26900  21.04600  1.000 35.04000 ? 30  ARG B CD  1 
ATOM   245  N NE  . ARG A 1 30  ? 11.30700  16.40500  20.19300  1.000 37.47000 ? 30  ARG B NE  1 
ATOM   246  C CZ  . ARG A 1 30  ? 11.87200  17.60500  20.29700  1.000 31.84000 ? 30  ARG B CZ  1 
ATOM   247  N NH1 . ARG A 1 30  ? 12.80400  17.82100  21.21100  1.000 34.46000 ? 30  ARG B NH1 1 
ATOM   248  N NH2 . ARG A 1 30  ? 11.49800  18.58400  19.48700  1.000 36.52000 ? 30  ARG B NH2 1 
ATOM   249  N N   . LYS A 1 31  ? 12.44700  12.97100  16.04400  1.000 36.85000 ? 31  LYS B N   1 
ATOM   250  C CA  . LYS A 1 31  ? 12.07400  12.74900  14.65100  1.000 42.45000 ? 31  LYS B CA  1 
ATOM   251  C C   . LYS A 1 31  ? 11.96300  11.26100  14.34100  1.000 35.40000 ? 31  LYS B C   1 
ATOM   252  O O   . LYS A 1 31  ? 10.96100  10.80000  13.78100  1.000 42.98000 ? 31  LYS B O   1 
ATOM   253  C CB  . LYS A 1 31  ? 13.11000  13.41500  13.73900  1.000 44.69000 ? 31  LYS B CB  1 
ATOM   254  C CG  . LYS A 1 31  ? 12.95700  13.13100  12.24700  1.000 50.71000 ? 31  LYS B CG  1 
ATOM   255  C CD  . LYS A 1 31  ? 12.62000  14.39900  11.47300  1.000 57.06000 ? 31  LYS B CD  1 
ATOM   256  C CE  . LYS A 1 31  ? 13.88500  15.10400  11.00100  1.000 57.04000 ? 31  LYS B CE  1 
ATOM   257  N NZ  . LYS A 1 31  ? 13.61300  16.49400  10.53800  1.000 61.66000 ? 31  LYS B NZ  1 
ATOM   258  N N   . ILE A 1 32  ? 12.98900  10.49300  14.70300  1.000 32.55000 ? 32  ILE B N   1 
ATOM   259  C CA  . ILE A 1 32  ? 13.01400  9.07500   14.35700  1.000 36.05000 ? 32  ILE B CA  1 
ATOM   260  C C   . ILE A 1 32  ? 12.03100  8.29100   15.21400  1.000 30.50000 ? 32  ILE B C   1 
ATOM   261  O O   . ILE A 1 32  ? 11.33700  7.39100   14.72100  1.000 29.16000 ? 32  ILE B O   1 
ATOM   262  C CB  . ILE A 1 32  ? 14.43900  8.51900   14.50200  1.000 35.04000 ? 32  ILE B CB  1 
ATOM   263  C CG1 . ILE A 1 32  ? 15.35300  9.10800   13.42800  1.000 36.91000 ? 32  ILE B CG1 1 
ATOM   264  C CG2 . ILE A 1 32  ? 14.41800  6.99700   14.45300  1.000 39.70000 ? 32  ILE B CG2 1 
ATOM   265  C CD1 . ILE A 1 32  ? 16.65900  8.36000   13.28100  1.000 44.07000 ? 32  ILE B CD1 1 
ATOM   266  N N   . ALA A 1 33  ? 11.96300  8.60500   16.50800  1.000 25.55000 ? 33  ALA B N   1 
ATOM   267  C CA  . ALA A 1 33  ? 11.12900  7.81400   17.40600  1.000 22.83000 ? 33  ALA B CA  1 
ATOM   268  C C   . ALA A 1 33  ? 9.65800   7.86600   17.01100  1.000 20.15000 ? 33  ALA B C   1 
ATOM   269  O O   . ALA A 1 33  ? 8.93900   6.87800   17.18300  1.000 22.95000 ? 33  ALA B O   1 
ATOM   270  C CB  . ALA A 1 33  ? 11.30400  8.29400   18.84500  1.000 26.36000 ? 33  ALA B CB  1 
ATOM   271  N N   . VAL A 1 34  ? 9.18300   9.01200   16.52000  1.000 22.44000 ? 34  VAL B N   1 
ATOM   272  C CA  . VAL A 1 34  ? 7.78100   9.13100   16.14300  1.000 21.87000 ? 34  VAL B CA  1 
ATOM   273  C C   . VAL A 1 34  ? 7.40100   8.20700   14.99200  1.000 24.49000 ? 34  VAL B C   1 
ATOM   274  O O   . VAL A 1 34  ? 6.21500   7.90900   14.81100  1.000 32.31000 ? 34  VAL B O   1 
ATOM   275  C CB  . VAL A 1 34  ? 7.44600   10.59600  15.78200  1.000 31.96000 ? 34  VAL B CB  1 
ATOM   276  C CG1 . VAL A 1 34  ? 7.63600   11.49900  16.98800  1.000 31.41000 ? 34  VAL B CG1 1 
ATOM   277  C CG2 . VAL A 1 34  ? 8.30700   11.07500  14.63100  1.000 34.86000 ? 34  VAL B CG2 1 
ATOM   278  N N   . ARG A 1 35  ? 8.37400   7.74300   14.20600  1.000 25.75000 ? 35  ARG B N   1 
ATOM   279  C CA  . ARG A 1 35  ? 8.09000   6.90700   13.04000  1.000 25.88000 ? 35  ARG B CA  1 
ATOM   280  C C   . ARG A 1 35  ? 8.15100   5.41700   13.33800  1.000 28.18000 ? 35  ARG B C   1 
ATOM   281  O O   . ARG A 1 35  ? 7.62400   4.61400   12.55600  1.000 22.74000 ? 35  ARG B O   1 
ATOM   282  C CB  . ARG A 1 35  ? 9.09400   7.21600   11.92500  1.000 26.04000 ? 35  ARG B CB  1 
ATOM   283  C CG  . ARG A 1 35  ? 8.93800   8.60600   11.34100  1.000 32.17000 ? 35  ARG B CG  1 
ATOM   284  C CD  . ARG A 1 35  ? 10.10200  8.98200   10.43900  1.000 38.77000 ? 35  ARG B CD  1 
ATOM   285  N NE  . ARG A 1 35  ? 10.54200  10.36300  10.65200  1.000 44.69000 ? 35  ARG B NE  1 
ATOM   286  C CZ  . ARG A 1 35  ? 9.75500   11.43200  10.52400  1.000 48.14000 ? 35  ARG B CZ  1 
ATOM   287  N NH1 . ARG A 1 35  ? 8.47400   11.28800  10.20000  1.000 45.94000 ? 35  ARG B NH1 1 
ATOM   288  N NH2 . ARG A 1 35  ? 10.24300  12.64900  10.72700  1.000 49.23000 ? 35  ARG B NH2 1 
ATOM   289  N N   . LEU A 1 36  ? 8.78100   5.03000   14.43800  1.000 25.74000 ? 36  LEU B N   1 
ATOM   290  C CA  . LEU A 1 36  ? 9.03800   3.62600   14.70700  1.000 26.00000 ? 36  LEU B CA  1 
ATOM   291  C C   . LEU A 1 36  ? 7.81200   2.92700   15.26800  1.000 31.93000 ? 36  LEU B C   1 
ATOM   292  O O   . LEU A 1 36  ? 7.03400   3.50000   16.03800  1.000 29.23000 ? 36  LEU B O   1 
ATOM   293  C CB  . LEU A 1 36  ? 10.19800  3.47900   15.68600  1.000 26.89000 ? 36  LEU B CB  1 
ATOM   294  C CG  . LEU A 1 36  ? 11.54600  4.04100   15.25100  1.000 32.49000 ? 36  LEU B CG  1 
ATOM   295  C CD1 . LEU A 1 36  ? 12.62000  3.49900   16.16200  1.000 42.42000 ? 36  LEU B CD1 1 
ATOM   296  C CD2 . LEU A 1 36  ? 11.84300  3.68400   13.80800  1.000 34.76000 ? 36  LEU B CD2 1 
ATOM   297  N N   . THR A 1 37  ? 7.64200   1.67700   14.87100  1.000 23.34000 ? 37  THR B N   1 
ATOM   298  C CA  . THR A 1 37  ? 6.67400   0.81700   15.51000  1.000 24.87000 ? 37  THR B CA  1 
ATOM   299  C C   . THR A 1 37  ? 7.22300   0.37600   16.86100  1.000 21.98000 ? 37  THR B C   1 
ATOM   300  O O   . THR A 1 37  ? 8.38800   -0.01000  16.97500  1.000 25.83000 ? 37  THR B O   1 
ATOM   301  C CB  . THR A 1 37  ? 6.39300   -0.39500  14.62700  1.000 24.09000 ? 37  THR B CB  1 
ATOM   302  O OG1 . THR A 1 37  ? 5.96100   0.06800   13.33700  1.000 28.58000 ? 37  THR B OG1 1 
ATOM   303  C CG2 . THR A 1 37  ? 5.30600   -1.23900  15.24300  1.000 27.24000 ? 37  THR B CG2 1 
ATOM   304  N N   . LEU A 1 38  ? 6.37800   0.44100   17.88300  1.000 24.41000 ? 38  LEU B N   1 
ATOM   305  C CA  . LEU A 1 38  ? 6.76300   0.11700   19.25300  1.000 24.14000 ? 38  LEU B CA  1 
ATOM   306  C C   . LEU A 1 38  ? 6.02100   -1.12900  19.70300  1.000 22.43000 ? 38  LEU B C   1 
ATOM   307  O O   . LEU A 1 38  ? 4.79500   -1.20600  19.57100  1.000 24.74000 ? 38  LEU B O   1 
ATOM   308  C CB  . LEU A 1 38  ? 6.44200   1.26500   20.21400  1.000 25.91000 ? 38  LEU B CB  1 
ATOM   309  C CG  . LEU A 1 38  ? 7.21700   2.58200   20.16700  1.000 38.75000 ? 38  LEU B CG  1 
ATOM   310  C CD1 . LEU A 1 38  ? 7.18000   3.21000   18.78800  1.000 38.12000 ? 38  LEU B CD1 1 
ATOM   311  C CD2 . LEU A 1 38  ? 6.67900   3.55400   21.22200  1.000 37.96000 ? 38  LEU B CD2 1 
ATOM   312  N N   . THR A 1 39  ? 6.75500   -2.06700  20.28000  1.000 22.38000 ? 39  THR B N   1 
ATOM   313  C CA  . THR A 1 39  ? 6.18500   -3.27800  20.83100  1.000 23.41000 ? 39  THR B CA  1 
ATOM   314  C C   . THR A 1 39  ? 6.55100   -3.32300  22.31100  1.000 25.90000 ? 39  THR B C   1 
ATOM   315  O O   . THR A 1 39  ? 7.70000   -3.15100  22.67500  1.000 23.54000 ? 39  THR B O   1 
ATOM   316  C CB  . THR A 1 39  ? 6.71900   -4.52400  20.12000  1.000 30.23000 ? 39  THR B CB  1 
ATOM   317  O OG1 . THR A 1 39  ? 6.37600   -4.44900  18.73700  1.000 32.92000 ? 39  THR B OG1 1 
ATOM   318  C CG2 . THR A 1 39  ? 6.11900   -5.78800  20.71700  1.000 32.59000 ? 39  THR B CG2 1 
ATOM   319  N N   . LEU A 1 40  ? 5.55100   -3.54800  23.14600  1.000 20.14000 ? 40  LEU B N   1 
ATOM   320  C CA  . LEU A 1 40  ? 5.71600   -3.59400  24.58600  1.000 17.32000 ? 40  LEU B CA  1 
ATOM   321  C C   . LEU A 1 40  ? 5.51100   -5.03400  25.03700  1.000 22.97000 ? 40  LEU B C   1 
ATOM   322  O O   . LEU A 1 40  ? 4.43700   -5.60800  24.82200  1.000 27.01000 ? 40  LEU B O   1 
ATOM   323  C CB  . LEU A 1 40  ? 4.72000   -2.64100  25.25500  1.000 20.49000 ? 40  LEU B CB  1 
ATOM   324  C CG  . LEU A 1 40  ? 4.57500   -2.60800  26.76900  1.000 22.45000 ? 40  LEU B CG  1 
ATOM   325  C CD1 . LEU A 1 40  ? 5.84400   -2.14200  27.48100  1.000 24.83000 ? 40  LEU B CD1 1 
ATOM   326  C CD2 . LEU A 1 40  ? 3.41100   -1.69200  27.12000  1.000 23.66000 ? 40  LEU B CD2 1 
ATOM   327  N N   . VAL A 1 41  ? 6.55100   -5.62500  25.61400  1.000 17.80000 ? 41  VAL B N   1 
ATOM   328  C CA  . VAL A 1 41  ? 6.51900   -6.99800  26.10600  1.000 18.77000 ? 41  VAL B CA  1 
ATOM   329  C C   . VAL A 1 41  ? 6.61700   -6.96100  27.62400  1.000 21.59000 ? 41  VAL B C   1 
ATOM   330  O O   . VAL A 1 41  ? 7.58200   -6.42200  28.17500  1.000 22.31000 ? 41  VAL B O   1 
ATOM   331  C CB  . VAL A 1 41  ? 7.65300   -7.83800  25.50500  1.000 22.31000 ? 41  VAL B CB  1 
ATOM   332  C CG1 . VAL A 1 41  ? 7.70500   -9.20100  26.16100  1.000 26.38000 ? 41  VAL B CG1 1 
ATOM   333  C CG2 . VAL A 1 41  ? 7.45900   -7.95800  23.99600  1.000 24.72000 ? 41  VAL B CG2 1 
ATOM   334  N N   . ILE A 1 42  ? 5.63700   -7.54600  28.30200  1.000 17.83000 ? 42  ILE B N   1 
ATOM   335  C CA  . ILE A 1 42  ? 5.59200   -7.53400  29.76300  1.000 18.97000 ? 42  ILE B CA  1 
ATOM   336  C C   . ILE A 1 42  ? 5.57600   -8.96500  30.27800  1.000 22.79000 ? 42  ILE B C   1 
ATOM   337  O O   . ILE A 1 42  ? 4.73500   -9.77100  29.86000  1.000 21.77000 ? 42  ILE B O   1 
ATOM   338  C CB  . ILE A 1 42  ? 4.37400   -6.75200  30.29000  1.000 21.57000 ? 42  ILE B CB  1 
ATOM   339  C CG1 . ILE A 1 42  ? 4.44500   -5.29000  29.83300  1.000 22.10000 ? 42  ILE B CG1 1 
ATOM   340  C CG2 . ILE A 1 42  ? 4.31900   -6.84300  31.81500  1.000 16.74000 ? 42  ILE B CG2 1 
ATOM   341  C CD1 . ILE A 1 42  ? 3.18500   -4.49600  30.11200  1.000 23.68000 ? 42  ILE B CD1 1 
ATOM   342  N N   . ASP A 1 43  ? 6.50500   -9.27100  31.18400  1.000 20.06000 ? 43  ASP B N   1 
ATOM   343  C CA  . ASP A 1 43  ? 6.54700   -10.53800 31.90200  1.000 23.62000 ? 43  ASP B CA  1 
ATOM   344  C C   . ASP A 1 43  ? 6.33300   -10.25900 33.38100  1.000 23.89000 ? 43  ASP B C   1 
ATOM   345  O O   . ASP A 1 43  ? 7.15900   -9.59500  34.01500  1.000 26.28000 ? 43  ASP B O   1 
ATOM   346  C CB  . ASP A 1 43  ? 7.87700   -11.25300 31.67500  1.000 29.94000 ? 43  ASP B CB  1 
ATOM   347  C CG  . ASP A 1 43  ? 8.23000   -11.36500 30.20300  1.000 44.42000 ? 43  ASP B CG  1 
ATOM   348  O OD1 . ASP A 1 43  ? 9.25700   -10.78800 29.78900  1.000 47.05000 ? 43  ASP B OD1 1 
ATOM   349  O OD2 . ASP A 1 43  ? 7.46500   -12.01000 29.45600  1.000 40.92000 ? 43  ASP B OD2 1 
ATOM   350  N N   . GLN A 1 44  ? 5.23800   -10.77400 33.92600  1.000 23.46000 ? 44  GLN B N   1 
ATOM   351  C CA  . GLN A 1 44  ? 4.82400   -10.47500 35.28900  1.000 21.70000 ? 44  GLN B CA  1 
ATOM   352  C C   . GLN A 1 44  ? 4.61600   -11.76800 36.05600  1.000 27.26000 ? 44  GLN B C   1 
ATOM   353  O O   . GLN A 1 44  ? 3.87200   -12.64700 35.60700  1.000 26.39000 ? 44  GLN B O   1 
ATOM   354  C CB  . GLN A 1 44  ? 3.54000   -9.64700  35.29500  1.000 22.39000 ? 44  GLN B CB  1 
ATOM   355  C CG  . GLN A 1 44  ? 2.91800   -9.48700  36.67900  1.000 25.32000 ? 44  GLN B CG  1 
ATOM   356  C CD  . GLN A 1 44  ? 1.61200   -8.74700  36.63300  1.000 24.13000 ? 44  GLN B CD  1 
ATOM   357  O OE1 . GLN A 1 44  ? 1.11400   -8.40600  35.56100  1.000 28.45000 ? 44  GLN B OE1 1 
ATOM   358  N NE2 . GLN A 1 44  ? 1.03700   -8.49100  37.80500  1.000 32.78000 ? 44  GLN B NE2 1 
ATOM   359  N N   . ASP A 1 45  ? 5.26800   -11.87900 37.21100  1.000 23.87000 ? 45  ASP B N   1 
ATOM   360  C CA  . ASP A 1 45  ? 5.10000   -13.03300 38.09500  1.000 28.33000 ? 45  ASP B CA  1 
ATOM   361  C C   . ASP A 1 45  ? 5.02200   -12.50000 39.52300  1.000 26.75000 ? 45  ASP B C   1 
ATOM   362  O O   . ASP A 1 45  ? 6.03900   -12.09500 40.09100  1.000 28.96000 ? 45  ASP B O   1 
ATOM   363  C CB  . ASP A 1 45  ? 6.23800   -14.03100 37.93500  1.000 33.44000 ? 45  ASP B CB  1 
ATOM   364  C CG  . ASP A 1 45  ? 6.15000   -15.17400 38.93000  1.000 42.17000 ? 45  ASP B CG  1 
ATOM   365  O OD1 . ASP A 1 45  ? 5.04800   -15.74200 39.08700  1.000 43.35000 ? 45  ASP B OD1 1 
ATOM   366  O OD2 . ASP A 1 45  ? 7.18000   -15.50200 39.55200  1.000 49.90000 ? 45  ASP B OD2 1 
ATOM   367  N N   . GLY A 1 46  ? 3.81900   -12.48800 40.08700  1.000 30.94000 ? 46  GLY B N   1 
ATOM   368  C CA  . GLY A 1 46  ? 3.66000   -11.91700 41.41800  1.000 31.80000 ? 46  GLY B CA  1 
ATOM   369  C C   . GLY A 1 46  ? 3.99400   -10.44000 41.38300  1.000 26.52000 ? 46  GLY B C   1 
ATOM   370  O O   . GLY A 1 46  ? 3.45000   -9.67500  40.58100  1.000 27.07000 ? 46  GLY B O   1 
ATOM   371  N N   . ASP A 1 47  ? 4.91200   -10.02500 42.24800  1.000 25.46000 ? 47  ASP B N   1 
ATOM   372  C CA  . ASP A 1 47  ? 5.36200   -8.63900  42.26500  1.000 24.08000 ? 47  ASP B CA  1 
ATOM   373  C C   . ASP A 1 47  ? 6.54300   -8.37100  41.34200  1.000 25.33000 ? 47  ASP B C   1 
ATOM   374  O O   . ASP A 1 47  ? 7.00600   -7.23100  41.28000  1.000 23.61000 ? 47  ASP B O   1 
ATOM   375  C CB  . ASP A 1 47  ? 5.73500   -8.22000  43.69100  1.000 26.36000 ? 47  ASP B CB  1 
ATOM   376  C CG  . ASP A 1 47  ? 4.66900   -8.58400  44.69300  1.000 41.85000 ? 47  ASP B CG  1 
ATOM   377  O OD1 . ASP A 1 47  ? 4.97100   -9.34800  45.63500  1.000 49.07000 ? 47  ASP B OD1 1 
ATOM   378  O OD2 . ASP A 1 47  ? 3.51800   -8.12600  44.51700  1.000 50.09000 ? 47  ASP B OD2 1 
ATOM   379  N N   . ASN A 1 48  ? 7.03500   -9.37100  40.62000  1.000 22.41000 ? 48  ASN B N   1 
ATOM   380  C CA  . ASN A 1 48  ? 8.21500   -9.21000  39.78200  1.000 22.20000 ? 48  ASN B CA  1 
ATOM   381  C C   . ASN A 1 48  ? 7.80600   -8.93200  38.33900  1.000 21.05000 ? 48  ASN B C   1 
ATOM   382  O O   . ASN A 1 48  ? 6.99100   -9.66200  37.76500  1.000 23.57000 ? 48  ASN B O   1 
ATOM   383  C CB  . ASN A 1 48  ? 9.10200   -10.45000 39.86800  1.000 23.44000 ? 48  ASN B CB  1 
ATOM   384  C CG  . ASN A 1 48  ? 9.69500   -10.64000 41.26400  1.000 31.40000 ? 48  ASN B CG  1 
ATOM   385  O OD1 . ASN A 1 48  ? 10.12100  -9.67700  41.90500  1.000 31.72000 ? 48  ASN B OD1 1 
ATOM   386  N ND2 . ASN A 1 48  ? 9.71600   -11.88000 41.73700  1.000 33.93000 ? 48  ASN B ND2 1 
ATOM   387  N N   . PHE A 1 49  ? 8.36700   -7.87100  37.76500  1.000 16.94000 ? 49  PHE B N   1 
ATOM   388  C CA  . PHE A 1 49  ? 8.06200   -7.43200  36.41100  1.000 14.47000 ? 49  PHE B CA  1 
ATOM   389  C C   . PHE A 1 49  ? 9.33200   -7.34800  35.59400  1.000 19.18000 ? 49  PHE B C   1 
ATOM   390  O O   . PHE A 1 49  ? 10.37200  -6.90200  36.08400  1.000 19.04000 ? 49  PHE B O   1 
ATOM   391  C CB  . PHE A 1 49  ? 7.42100   -6.03600  36.40000  1.000 17.68000 ? 49  PHE B CB  1 
ATOM   392  C CG  . PHE A 1 49  ? 5.96000   -6.02300  36.73300  1.000 18.39000 ? 49  PHE B CG  1 
ATOM   393  C CD1 . PHE A 1 49  ? 5.52200   -6.17100  38.03500  1.000 19.14000 ? 49  PHE B CD1 1 
ATOM   394  C CD2 . PHE A 1 49  ? 5.01900   -5.83700  35.72800  1.000 16.49000 ? 49  PHE B CD2 1 
ATOM   395  C CE1 . PHE A 1 49  ? 4.14700   -6.14200  38.33400  1.000 16.97000 ? 49  PHE B CE1 1 
ATOM   396  C CE2 . PHE A 1 49  ? 3.66600   -5.79500  36.03100  1.000 16.00000 ? 49  PHE B CE2 1 
ATOM   397  C CZ  . PHE A 1 49  ? 3.23800   -5.95800  37.32100  1.000 19.02000 ? 49  PHE B CZ  1 
ATOM   398  N N   . LYS A 1 50  ? 9.23500   -7.75200  34.33800  1.000 19.14000 ? 50  LYS B N   1 
ATOM   399  C CA  . LYS A 1 50  ? 10.26800  -7.46700  33.35700  1.000 21.90000 ? 50  LYS B CA  1 
ATOM   400  C C   . LYS A 1 50  ? 9.57000   -6.83200  32.17100  1.000 25.04000 ? 50  LYS B C   1 
ATOM   401  O O   . LYS A 1 50  ? 8.66100   -7.43100  31.58900  1.000 25.68000 ? 50  LYS B O   1 
ATOM   402  C CB  . LYS A 1 50  ? 11.03400  -8.73400  32.97300  1.000 28.75000 ? 50  LYS B CB  1 
ATOM   403  C CG  . LYS A 1 50  ? 11.54000  -9.49800  34.20200  1.000 30.78000 ? 50  LYS B CG  1 
ATOM   404  C CD  . LYS A 1 50  ? 12.62500  -10.52000 33.86700  1.000 40.62000 ? 50  LYS B CD  1 
ATOM   405  C CE  . LYS A 1 50  ? 12.05700  -11.70200 33.10800  1.000 46.25000 ? 50  LYS B CE  1 
ATOM   406  N NZ  . LYS A 1 50  ? 11.24200  -12.59000 33.98900  1.000 51.13000 ? 50  LYS B NZ  1 
ATOM   407  N N   . THR A 1 51  ? 9.93500   -5.59500  31.86500  1.000 20.63000 ? 51  THR B N   1 
ATOM   408  C CA  . THR A 1 51  ? 9.27000   -4.82200  30.83000  1.000 19.28000 ? 51  THR B CA  1 
ATOM   409  C C   . THR A 1 51  ? 10.29000  -4.52700  29.74400  1.000 25.99000 ? 51  THR B C   1 
ATOM   410  O O   . THR A 1 51  ? 11.43000  -4.14800  30.04500  1.000 25.52000 ? 51  THR B O   1 
ATOM   411  C CB  . THR A 1 51  ? 8.66700   -3.53400  31.39500  1.000 21.66000 ? 51  THR B CB  1 
ATOM   412  O OG1 . THR A 1 51  ? 7.71800   -3.85600  32.43000  1.000 27.59000 ? 51  THR B OG1 1 
ATOM   413  C CG2 . THR A 1 51  ? 7.97900   -2.74400  30.30600  1.000 26.17000 ? 51  THR B CG2 1 
ATOM   414  N N   . LYS A 1 52  ? 9.90600   -4.76500  28.49100  1.000 21.09000 ? 52  LYS B N   1 
ATOM   415  C CA  . LYS A 1 52  ? 10.80400  -4.56700  27.36000  1.000 22.68000 ? 52  LYS B CA  1 
ATOM   416  C C   . LYS A 1 52  ? 10.04400  -3.79100  26.30300  1.000 27.55000 ? 52  LYS B C   1 
ATOM   417  O O   . LYS A 1 52  ? 8.95100   -4.20000  25.89800  1.000 25.25000 ? 52  LYS B O   1 
ATOM   418  C CB  . LYS A 1 52  ? 11.31200  -5.90000  26.80200  1.000 27.37000 ? 52  LYS B CB  1 
ATOM   419  C CG  . LYS A 1 52  ? 12.23600  -6.64900  27.74500  1.000 31.25000 ? 52  LYS B CG  1 
ATOM   420  C CD  . LYS A 1 52  ? 11.82500  -8.10800  27.89700  1.000 41.89000 ? 52  LYS B CD  1 
ATOM   421  C CE  . LYS A 1 52  ? 12.36700  -8.71700  29.18600  1.000 41.40000 ? 52  LYS B CE  1 
ATOM   422  N NZ  . LYS A 1 52  ? 11.66200  -9.98500  29.54200  1.000 44.33000 ? 52  LYS B NZ  1 
ATOM   423  N N   . CYS A 1 53  ? 10.59600  -2.65500  25.89700  1.000 23.25000 ? 53  CYS B N   1 
ATOM   424  C CA  . CYS A 1 53  ? 10.03200  -1.83600  24.83800  1.000 29.47000 ? 53  CYS B CA  1 
ATOM   425  C C   . CYS A 1 53  ? 11.01800  -1.88500  23.68800  1.000 36.12000 ? 53  CYS B C   1 
ATOM   426  O O   . CYS A 1 53  ? 12.19500  -1.56000  23.86900  1.000 32.34000 ? 53  CYS B O   1 
ATOM   427  C CB  . CYS A 1 53  ? 9.81000   -0.40000  25.30800  1.000 35.05000 ? 53  CYS B CB  1 
ATOM   428  S SG  . CYS A 1 53  ? 9.15300   -0.27300  26.99800  1.000 42.97000 ? 53  CYS B SG  1 
ATOM   429  N N   . THR A 1 54  ? 10.56000  -2.31600  22.52000  1.000 31.44000 ? 54  THR B N   1 
ATOM   430  C CA  . THR A 1 54  ? 11.47700  -2.52400  21.41200  1.000 34.33000 ? 54  THR B CA  1 
ATOM   431  C C   . THR A 1 54  ? 10.96200  -1.83800  20.15700  1.000 28.82000 ? 54  THR B C   1 
ATOM   432  O O   . THR A 1 54  ? 9.75500   -1.83500  19.88200  1.000 27.33000 ? 54  THR B O   1 
ATOM   433  C CB  . THR A 1 54  ? 11.69500  -4.01400  21.14300  1.000 38.77000 ? 54  THR B CB  1 
ATOM   434  O OG1 . THR A 1 54  ? 10.56000  -4.54400  20.45100  1.000 40.37000 ? 54  THR B OG1 1 
ATOM   435  C CG2 . THR A 1 54  ? 11.89300  -4.76900  22.46600  1.000 40.63000 ? 54  THR B CG2 1 
ATOM   436  N N   . SER A 1 55  ? 11.88300  -1.31800  19.39600  1.000 27.73000 ? 55  SER B N   1 
ATOM   437  C CA  . SER A 1 55  ? 11.64800  -0.74700  18.07300  1.000 28.88000 ? 55  SER B CA  1 
ATOM   438  C C   . SER A 1 55  ? 12.83300  -1.18500  17.19400  1.000 36.82000 ? 55  SER B C   1 
ATOM   439  O O   . SER A 1 55  ? 13.67200  -1.94800  17.60900  1.000 38.32000 ? 55  SER B O   1 
ATOM   440  C CB  . SER A 1 55  ? 11.54600  0.75300   18.09900  1.000 30.63000 ? 55  SER B CB  1 
ATOM   441  O OG  . SER A 1 55  ? 12.73900  1.32100   18.49000  1.000 32.62000 ? 55  SER B OG  1 
ATOM   442  N N   . THR A 1 56  ? 12.91400  -0.67300  15.98000  1.000 35.06000 ? 56  THR B N   1 
ATOM   443  C CA  . THR A 1 56  ? 13.99500  -1.07300  15.11400  1.000 43.67000 ? 56  THR B CA  1 
ATOM   444  C C   . THR A 1 56  ? 15.32300  -0.60800  15.60900  1.000 46.28000 ? 56  THR B C   1 
ATOM   445  O O   . THR A 1 56  ? 16.32500  -1.26500  15.47300  1.000 50.05000 ? 56  THR B O   1 
ATOM   446  C CB  . THR A 1 56  ? 13.77700  -0.60200  13.63600  1.000 44.76000 ? 56  THR B CB  1 
ATOM   447  O OG1 . THR A 1 56  ? 14.73200  0.38800   13.26300  1.000 53.67000 ? 56  THR B OG1 1 
ATOM   448  C CG2 . THR A 1 56  ? 12.43800  -0.02100  13.43400  1.000 34.83000 ? 56  THR B CG2 1 
ATOM   449  N N   . PHE A 1 57  ? 15.33900  0.57500   16.15000  1.000 47.07000 ? 57  PHE B N   1 
ATOM   450  C CA  . PHE A 1 57  ? 16.57000  1.12300   16.56200  1.000 52.04000 ? 57  PHE B CA  1 
ATOM   451  C C   . PHE A 1 57  ? 16.81600  0.92300   18.00600  1.000 56.36000 ? 57  PHE B C   1 
ATOM   452  O O   . PHE A 1 57  ? 17.67200  0.16400   18.38400  1.000 59.22000 ? 57  PHE B O   1 
ATOM   453  C CB  . PHE A 1 57  ? 16.58400  2.60600   16.22500  1.000 54.54000 ? 57  PHE B CB  1 
ATOM   454  C CG  . PHE A 1 57  ? 16.55900  2.87500   14.76300  1.000 54.67000 ? 57  PHE B CG  1 
ATOM   455  C CD1 . PHE A 1 57  ? 17.65200  2.59800   13.98900  1.000 54.63000 ? 57  PHE B CD1 1 
ATOM   456  C CD2 . PHE A 1 57  ? 15.45200  3.38400   14.17000  1.000 52.25000 ? 57  PHE B CD2 1 
ATOM   457  C CE1 . PHE A 1 57  ? 17.63900  2.82700   12.64200  1.000 60.79000 ? 57  PHE B CE1 1 
ATOM   458  C CE2 . PHE A 1 57  ? 15.43000  3.61500   12.82400  1.000 54.23000 ? 57  PHE B CE2 1 
ATOM   459  C CZ  . PHE A 1 57  ? 16.52300  3.34100   12.05700  1.000 58.85000 ? 57  PHE B CZ  1 
ATOM   460  N N   . TYR A 1 58  ? 16.06400  1.63200   18.84000  1.000 53.04000 ? 58  TYR B N   1 
ATOM   461  C CA  . TYR A 1 58  ? 16.27400  1.57300   20.28500  1.000 51.91000 ? 58  TYR B CA  1 
ATOM   462  C C   . TYR A 1 58  ? 15.46000  0.56300   21.09300  1.000 50.20000 ? 58  TYR B C   1 
ATOM   463  O O   . TYR A 1 58  ? 14.38900  0.11200   20.68600  1.000 44.66000 ? 58  TYR B O   1 
ATOM   464  C CB  . TYR A 1 58  ? 16.09900  2.97000   20.89400  1.000 53.29000 ? 58  TYR B CB  1 
ATOM   465  C CG  . TYR A 1 58  ? 16.78100  4.06900   20.11100  1.000 64.44000 ? 58  TYR B CG  1 
ATOM   466  C CD1 . TYR A 1 58  ? 16.04200  4.98200   19.37100  1.000 65.81000 ? 58  TYR B CD1 1 
ATOM   467  C CD2 . TYR A 1 58  ? 18.16400  4.19400   20.11300  1.000 65.57000 ? 58  TYR B CD2 1 
ATOM   468  C CE1 . TYR A 1 58  ? 16.66100  5.98900   18.65400  1.000 65.44000 ? 58  TYR B CE1 1 
ATOM   469  C CE2 . TYR A 1 58  ? 18.79200  5.19800   19.40000  1.000 68.30000 ? 58  TYR B CE2 1 
ATOM   470  C CZ  . TYR A 1 58  ? 18.03600  6.09200   18.67200  1.000 70.57000 ? 58  TYR B CZ  1 
ATOM   471  O OH  . TYR A 1 58  ? 18.65700  7.09200   17.96100  1.000 72.98000 ? 58  TYR B OH  1 
ATOM   472  N N   . ASN A 1 59  ? 16.01500  0.23200   22.25500  1.000 45.71000 ? 59  ASN B N   1 
ATOM   473  C CA  . ASN A 1 59  ? 15.43900  -0.66200  23.21600  1.000 43.12000 ? 59  ASN B CA  1 
ATOM   474  C C   . ASN A 1 59  ? 15.39100  -0.03700  24.61500  1.000 40.46000 ? 59  ASN B C   1 
ATOM   475  O O   . ASN A 1 59  ? 16.26700  0.68900   24.97200  1.000 41.17000 ? 59  ASN B O   1 
ATOM   476  C CB  . ASN A 1 59  ? 16.29800  -1.89800  23.33100  1.000 47.17000 ? 59  ASN B CB  1 
ATOM   477  C CG  . ASN A 1 59  ? 16.03000  -2.89200  22.25900  1.000 53.86000 ? 59  ASN B CG  1 
ATOM   478  O OD1 . ASN A 1 59  ? 15.00500  -2.84800  21.58500  1.000 52.09000 ? 59  ASN B OD1 1 
ATOM   479  N ND2 . ASN A 1 59  ? 16.95600  -3.83700  22.09700  1.000 57.17000 ? 59  ASN B ND2 1 
ATOM   480  N N   . TYR A 1 60  ? 14.36500  -0.35100  25.39000  1.000 32.44000 ? 60  TYR B N   1 
ATOM   481  C CA  . TYR A 1 60  ? 14.24600  0.11200   26.76100  1.000 29.77000 ? 60  TYR B CA  1 
ATOM   482  C C   . TYR A 1 60  ? 13.71700  -1.04300  27.61800  1.000 28.75000 ? 60  TYR B C   1 
ATOM   483  O O   . TYR A 1 60  ? 12.60000  -1.39500  27.51900  1.000 29.17000 ? 60  TYR B O   1 
ATOM   484  C CB  . TYR A 1 60  ? 13.31500  1.27900   26.84000  1.000 28.80000 ? 60  TYR B CB  1 
ATOM   485  C CG  . TYR A 1 60  ? 13.28200  2.00000   28.15600  1.000 29.86000 ? 60  TYR B CG  1 
ATOM   486  C CD1 . TYR A 1 60  ? 14.11100  3.08700   28.40000  1.000 30.82000 ? 60  TYR B CD1 1 
ATOM   487  C CD2 . TYR A 1 60  ? 12.39700  1.63800   29.13500  1.000 30.65000 ? 60  TYR B CD2 1 
ATOM   488  C CE1 . TYR A 1 60  ? 14.08500  3.77900   29.58200  1.000 28.80000 ? 60  TYR B CE1 1 
ATOM   489  C CE2 . TYR A 1 60  ? 12.34300  2.34300   30.31900  1.000 32.67000 ? 60  TYR B CE2 1 
ATOM   490  C CZ  . TYR A 1 60  ? 13.19300  3.41300   30.54300  1.000 38.23000 ? 60  TYR B CZ  1 
ATOM   491  O OH  . TYR A 1 60  ? 13.12500  4.09700   31.73800  1.000 35.56000 ? 60  TYR B OH  1 
ATOM   492  N N   . ASP A 1 61  ? 14.58300  -1.59900  28.43800  1.000 24.40000 ? 61  ASP B N   1 
ATOM   493  C CA  . ASP A 1 61  ? 14.28900  -2.75600  29.27000  1.000 24.17000 ? 61  ASP B CA  1 
ATOM   494  C C   . ASP A 1 61  ? 14.48100  -2.37400  30.72800  1.000 28.98000 ? 61  ASP B C   1 
ATOM   495  O O   . ASP A 1 61  ? 15.50400  -1.77700  31.09000  1.000 27.45000 ? 61  ASP B O   1 
ATOM   496  C CB  . ASP A 1 61  ? 15.19900  -3.94100  28.92200  1.000 28.52000 ? 61  ASP B CB  1 
ATOM   497  N N   . VAL A 1 62  ? 13.50800  -2.72700  31.56200  1.000 22.10000 ? 62  VAL B N   1 
ATOM   498  C CA  . VAL A 1 62  ? 13.58200  -2.45800  32.99200  1.000 24.00000 ? 62  VAL B CA  1 
ATOM   499  C C   . VAL A 1 62  ? 12.95400  -3.62500  33.73300  1.000 25.07000 ? 62  VAL B C   1 
ATOM   500  O O   . VAL A 1 62  ? 11.94400  -4.19000  33.29500  1.000 22.43000 ? 62  VAL B O   1 
ATOM   501  C CB  . VAL A 1 62  ? 12.88600  -1.13100  33.35700  1.000 25.64000 ? 62  VAL B CB  1 
ATOM   502  C CG1 . VAL A 1 62  ? 11.39900  -1.21800  33.11000  1.000 23.04000 ? 62  VAL B CG1 1 
ATOM   503  C CG2 . VAL A 1 62  ? 13.18100  -0.75200  34.81700  1.000 28.76000 ? 62  VAL B CG2 1 
ATOM   504  N N   . ASP A 1 63  ? 13.56000  -3.99300  34.85200  1.000 21.54000 ? 63  ASP B N   1 
ATOM   505  C CA  . ASP A 1 63  ? 13.01800  -4.99700  35.74800  1.000 23.35000 ? 63  ASP B CA  1 
ATOM   506  C C   . ASP A 1 63  ? 12.76800  -4.33300  37.09300  1.000 20.51000 ? 63  ASP B C   1 
ATOM   507  O O   . ASP A 1 63  ? 13.54000  -3.46500  37.51800  1.000 21.56000 ? 63  ASP B O   1 
ATOM   508  C CB  . ASP A 1 63  ? 13.97900  -6.17400  35.91000  1.000 22.43000 ? 63  ASP B CB  1 
ATOM   509  C CG  . ASP A 1 63  ? 14.28900  -6.85500  34.59200  1.000 29.92000 ? 63  ASP B CG  1 
ATOM   510  O OD1 . ASP A 1 63  ? 13.50000  -6.68500  33.64100  1.000 30.93000 ? 63  ASP B OD1 1 
ATOM   511  O OD2 . ASP A 1 63  ? 15.31700  -7.56100  34.51100  1.000 41.61000 ? 63  ASP B OD2 1 
ATOM   512  N N   . PHE A 1 64  ? 11.67400  -4.70700  37.74800  1.000 16.15000 ? 64  PHE B N   1 
ATOM   513  C CA  . PHE A 1 64  ? 11.40400  -4.12600  39.05500  1.000 16.89000 ? 64  PHE B CA  1 
ATOM   514  C C   . PHE A 1 64  ? 10.52000  -5.06900  39.85300  1.000 16.19000 ? 64  PHE B C   1 
ATOM   515  O O   . PHE A 1 64  ? 9.89100   -5.98400  39.31100  1.000 17.76000 ? 64  PHE B O   1 
ATOM   516  C CB  . PHE A 1 64  ? 10.76100  -2.73300  38.94000  1.000 17.58000 ? 64  PHE B CB  1 
ATOM   517  C CG  . PHE A 1 64  ? 9.48800   -2.70100  38.14500  1.000 16.42000 ? 64  PHE B CG  1 
ATOM   518  C CD1 . PHE A 1 64  ? 8.26300   -2.97100  38.74200  1.000 17.20000 ? 64  PHE B CD1 1 
ATOM   519  C CD2 . PHE A 1 64  ? 9.50500   -2.35800  36.80000  1.000 17.55000 ? 64  PHE B CD2 1 
ATOM   520  C CE1 . PHE A 1 64  ? 7.08900   -2.93200  37.99400  1.000 17.16000 ? 64  PHE B CE1 1 
ATOM   521  C CE2 . PHE A 1 64  ? 8.33400   -2.30900  36.05500  1.000 15.17000 ? 64  PHE B CE2 1 
ATOM   522  C CZ  . PHE A 1 64  ? 7.12800   -2.59300  36.65300  1.000 16.42000 ? 64  PHE B CZ  1 
ATOM   523  N N   . THR A 1 65  ? 10.47800  -4.82100  41.15600  1.000 16.63000 ? 65  THR B N   1 
ATOM   524  C CA  . THR A 1 65  ? 9.57700   -5.49500  42.07800  1.000 16.14000 ? 65  THR B CA  1 
ATOM   525  C C   . THR A 1 65  ? 8.61500   -4.45200  42.62800  1.000 16.70000 ? 65  THR B C   1 
ATOM   526  O O   . THR A 1 65  ? 9.05100   -3.40000  43.10700  1.000 15.53000 ? 65  THR B O   1 
ATOM   527  C CB  . THR A 1 65  ? 10.36600  -6.14500  43.21800  1.000 23.02000 ? 65  THR B CB  1 
ATOM   528  O OG1 . THR A 1 65  ? 11.23400  -7.15100  42.67600  1.000 24.07000 ? 65  THR B OG1 1 
ATOM   529  C CG2 . THR A 1 65  ? 9.43600   -6.75900  44.24200  1.000 20.89000 ? 65  THR B CG2 1 
ATOM   530  N N   . VAL A 1 66  ? 7.31300   -4.72500  42.52400  1.000 14.54000 ? 66  VAL B N   1 
ATOM   531  C CA  . VAL A 1 66  ? 6.33100   -3.79500  43.05800  1.000 13.10000 ? 66  VAL B CA  1 
ATOM   532  C C   . VAL A 1 66  ? 6.64000   -3.52600  44.52600  1.000 16.57000 ? 66  VAL B C   1 
ATOM   533  O O   . VAL A 1 66  ? 6.89400   -4.44600  45.31500  1.000 15.77000 ? 66  VAL B O   1 
ATOM   534  C CB  . VAL A 1 66  ? 4.91700   -4.36400  42.86300  1.000 15.38000 ? 66  VAL B CB  1 
ATOM   535  C CG1 . VAL A 1 66  ? 3.90400   -3.52700  43.63300  1.000 16.06000 ? 66  VAL B CG1 1 
ATOM   536  C CG2 . VAL A 1 66  ? 4.56400   -4.38700  41.37200  1.000 18.84000 ? 66  VAL B CG2 1 
ATOM   537  N N   . GLY A 1 67  ? 6.64700   -2.25200  44.88900  1.000 12.16000 ? 67  GLY B N   1 
ATOM   538  C CA  . GLY A 1 67  ? 6.81200   -1.87900  46.27800  1.000 12.53000 ? 67  GLY B CA  1 
ATOM   539  C C   . GLY A 1 67  ? 8.24300   -1.72600  46.73600  1.000 12.87000 ? 67  GLY B C   1 
ATOM   540  O O   . GLY A 1 67  ? 8.45800   -1.41600  47.91600  1.000 14.64000 ? 67  GLY B O   1 
ATOM   541  N N   . VAL A 1 68  ? 9.22300   -1.91200  45.85400  1.000 12.00000 ? 68  VAL B N   1 
ATOM   542  C CA  . VAL A 1 68  ? 10.64000  -1.85000  46.22300  1.000 15.30000 ? 68  VAL B CA  1 
ATOM   543  C C   . VAL A 1 68  ? 11.29500  -0.75800  45.39200  1.000 15.91000 ? 68  VAL B C   1 
ATOM   544  O O   . VAL A 1 68  ? 11.39300  -0.87200  44.16300  1.000 13.51000 ? 68  VAL B O   1 
ATOM   545  C CB  . VAL A 1 68  ? 11.34800  -3.19700  46.01000  1.000 15.24000 ? 68  VAL B CB  1 
ATOM   546  C CG1 . VAL A 1 68  ? 12.82600  -3.11400  46.39800  1.000 17.12000 ? 68  VAL B CG1 1 
ATOM   547  C CG2 . VAL A 1 68  ? 10.64100  -4.29800  46.79200  1.000 19.82000 ? 68  VAL B CG2 1 
ATOM   548  N N   . GLU A 1 69  ? 11.76800  0.29300   46.04600  1.000 13.65000 ? 69  GLU B N   1 
ATOM   549  C CA  . GLU A 1 69  ? 12.43100  1.35900   45.30100  1.000 13.28000 ? 69  GLU B CA  1 
ATOM   550  C C   . GLU A 1 69  ? 13.66200  0.79400   44.61200  1.000 19.03000 ? 69  GLU B C   1 
ATOM   551  O O   . GLU A 1 69  ? 14.36600  -0.06300  45.16400  1.000 18.67000 ? 69  GLU B O   1 
ATOM   552  C CB  . GLU A 1 69  ? 12.89600  2.50200   46.19800  1.000 17.00000 ? 69  GLU B CB  1 
ATOM   553  C CG  . GLU A 1 69  ? 13.16200  3.77900   45.40300  1.000 22.30000 ? 69  GLU B CG  1 
ATOM   554  C CD  . GLU A 1 69  ? 14.00600  4.76400   46.14400  1.000 40.86000 ? 69  GLU B CD  1 
ATOM   555  O OE1 . GLU A 1 69  ? 13.68500  6.02000   46.05600  1.000 50.47000 ? 69  GLU B OE1 1 
ATOM   556  O OE2 . GLU A 1 69  ? 14.97700  4.34800   46.80600  1.000 50.54000 ? 69  GLU B OE2 1 
ATOM   557  N N   . PHE A 1 70  ? 13.96500  1.33300   43.43600  1.000 16.63000 ? 70  PHE B N   1 
ATOM   558  C CA  . PHE A 1 70  ? 15.15500  0.91400   42.70100  1.000 16.04000 ? 70  PHE B CA  1 
ATOM   559  C C   . PHE A 1 70  ? 15.78500  2.11500   42.01400  1.000 18.94000 ? 70  PHE B C   1 
ATOM   560  O O   . PHE A 1 70  ? 15.08700  3.02800   41.55900  1.000 17.80000 ? 70  PHE B O   1 
ATOM   561  C CB  . PHE A 1 70  ? 14.84600  -0.21000  41.67600  1.000 20.96000 ? 70  PHE B CB  1 
ATOM   562  C CG  . PHE A 1 70  ? 13.78200  0.12500   40.65900  1.000 18.77000 ? 70  PHE B CG  1 
ATOM   563  C CD1 . PHE A 1 70  ? 12.44400  0.13300   41.02400  1.000 17.18000 ? 70  PHE B CD1 1 
ATOM   564  C CD2 . PHE A 1 70  ? 14.11500  0.37400   39.32700  1.000 19.90000 ? 70  PHE B CD2 1 
ATOM   565  C CE1 . PHE A 1 70  ? 11.43800  0.41700   40.10000  1.000 18.23000 ? 70  PHE B CE1 1 
ATOM   566  C CE2 . PHE A 1 70  ? 13.11900  0.65900   38.39700  1.000 18.94000 ? 70  PHE B CE2 1 
ATOM   567  C CZ  . PHE A 1 70  ? 11.78300  0.68400   38.78300  1.000 19.26000 ? 70  PHE B CZ  1 
ATOM   568  N N   . ASP A 1 71  ? 17.12200  2.12500   41.97300  1.000 20.38000 ? 71  ASP B N   1 
ATOM   569  C CA  . ASP A 1 71  ? 17.83100  3.14000   41.20700  1.000 23.05000 ? 71  ASP B CA  1 
ATOM   570  C C   . ASP A 1 71  ? 17.70900  2.83200   39.72900  1.000 19.23000 ? 71  ASP B C   1 
ATOM   571  O O   . ASP A 1 71  ? 17.83900  1.68300   39.29300  1.000 23.79000 ? 71  ASP B O   1 
ATOM   572  C CB  . ASP A 1 71  ? 19.30800  3.19000   41.59900  1.000 21.19000 ? 71  ASP B CB  1 
ATOM   573  C CG  . ASP A 1 71  ? 19.51500  3.82000   42.94300  1.000 30.39000 ? 71  ASP B CG  1 
ATOM   574  O OD1 . ASP A 1 71  ? 19.75700  3.06600   43.90700  1.000 41.63000 ? 71  ASP B OD1 1 
ATOM   575  O OD2 . ASP A 1 71  ? 19.41900  5.06500   43.05600  1.000 30.84000 ? 71  ASP B OD2 1 
ATOM   576  N N   . GLU A 1 72  ? 17.46100  3.86200   38.95300  1.000 19.83000 ? 72  GLU B N   1 
ATOM   577  C CA  . GLU A 1 72  ? 17.24400  3.68900   37.53700  1.000 18.46000 ? 72  GLU B CA  1 
ATOM   578  C C   . GLU A 1 72  ? 18.12100  4.67800   36.79200  1.000 16.18000 ? 72  GLU B C   1 
ATOM   579  O O   . GLU A 1 72  ? 18.22500  5.84200   37.18200  1.000 19.67000 ? 72  GLU B O   1 
ATOM   580  C CB  . GLU A 1 72  ? 15.78200  3.91100   37.22300  1.000 25.55000 ? 72  GLU B CB  1 
ATOM   581  C CG  . GLU A 1 72  ? 15.41400  3.79100   35.80700  1.000 27.32000 ? 72  GLU B CG  1 
ATOM   582  C CD  . GLU A 1 72  ? 13.96000  3.42800   35.69000  1.000 33.12000 ? 72  GLU B CD  1 
ATOM   583  O OE1 . GLU A 1 72  ? 13.11400  4.14100   36.29100  1.000 24.94000 ? 72  GLU B OE1 1 
ATOM   584  O OE2 . GLU A 1 72  ? 13.67900  2.40800   35.03500  1.000 35.29000 ? 72  GLU B OE2 1 
ATOM   585  N N   . TYR A 1 73  ? 18.78200  4.20300   35.74500  1.000 19.08000 ? 73  TYR B N   1 
ATOM   586  C CA  . TYR A 1 73  ? 19.53800  5.07500   34.86100  1.000 19.70000 ? 73  TYR B CA  1 
ATOM   587  C C   . TYR A 1 73  ? 18.92400  4.92000   33.48400  1.000 20.02000 ? 73  TYR B C   1 
ATOM   588  O O   . TYR A 1 73  ? 18.95400  3.82900   32.90400  1.000 21.14000 ? 73  TYR B O   1 
ATOM   589  C CB  . TYR A 1 73  ? 21.02400  4.71800   34.89500  1.000 18.70000 ? 73  TYR B CB  1 
ATOM   590  C CG  . TYR A 1 73  ? 21.60600  4.87300   36.28100  1.000 20.76000 ? 73  TYR B CG  1 
ATOM   591  C CD1 . TYR A 1 73  ? 21.55500  3.82700   37.18600  1.000 23.92000 ? 73  TYR B CD1 1 
ATOM   592  C CD2 . TYR A 1 73  ? 22.15700  6.07500   36.69700  1.000 17.79000 ? 73  TYR B CD2 1 
ATOM   593  C CE1 . TYR A 1 73  ? 22.07100  3.96500   38.46300  1.000 19.73000 ? 73  TYR B CE1 1 
ATOM   594  C CE2 . TYR A 1 73  ? 22.67600  6.22000   37.97700  1.000 25.52000 ? 73  TYR B CE2 1 
ATOM   595  C CZ  . TYR A 1 73  ? 22.62000  5.16200   38.84900  1.000 22.04000 ? 73  TYR B CZ  1 
ATOM   596  O OH  . TYR A 1 73  ? 23.13800  5.30200   40.13100  1.000 32.89000 ? 73  TYR B OH  1 
ATOM   597  N N   . THR A 1 74  ? 18.30800  5.99100   32.98800  1.000 18.49000 ? 74  THR B N   1 
ATOM   598  C CA  . THR A 1 74  ? 17.50400  5.89300   31.77200  1.000 19.66000 ? 74  THR B CA  1 
ATOM   599  C C   . THR A 1 74  ? 18.40700  5.98600   30.53600  1.000 19.50000 ? 74  THR B C   1 
ATOM   600  O O   . THR A 1 74  ? 18.24600  6.83900   29.66800  1.000 18.35000 ? 74  THR B O   1 
ATOM   601  C CB  . THR A 1 74  ? 16.41700  6.96000   31.79300  1.000 20.42000 ? 74  THR B CB  1 
ATOM   602  O OG1 . THR A 1 74  ? 16.99200  8.25400   32.04000  1.000 17.37000 ? 74  THR B OG1 1 
ATOM   603  C CG2 . THR A 1 74  ? 15.41800  6.65500   32.90000  1.000 20.24000 ? 74  THR B CG2 1 
ATOM   604  N N   . LYS A 1 75  ? 19.34800  5.03500   30.46200  1.000 23.00000 ? 75  LYS B N   1 
ATOM   605  C CA  . LYS A 1 75  ? 20.49200  5.15500   29.55500  1.000 23.23000 ? 75  LYS B CA  1 
ATOM   606  C C   . LYS A 1 75  ? 20.06400  5.32900   28.10400  1.000 25.41000 ? 75  LYS B C   1 
ATOM   607  O O   . LYS A 1 75  ? 20.72900  6.04000   27.34100  1.000 27.20000 ? 75  LYS B O   1 
ATOM   608  C CB  . LYS A 1 75  ? 21.39800  3.92500   29.68200  1.000 24.43000 ? 75  LYS B CB  1 
ATOM   609  C CG  . LYS A 1 75  ? 22.02800  3.71100   31.05400  1.000 24.91000 ? 75  LYS B CG  1 
ATOM   610  C CD  . LYS A 1 75  ? 22.70600  4.96300   31.57200  1.000 24.76000 ? 75  LYS B CD  1 
ATOM   611  C CE  . LYS A 1 75  ? 24.03400  5.23200   30.90100  1.000 21.83000 ? 75  LYS B CE  1 
ATOM   612  N NZ  . LYS A 1 75  ? 24.58700  6.52900   31.37500  1.000 22.04000 ? 75  LYS B NZ  1 
ATOM   613  N N   . SER A 1 76  ? 18.98100  4.67200   27.69000  1.000 22.39000 ? 76  SER B N   1 
ATOM   614  C CA  . SER A 1 76  ? 18.56500  4.68700   26.29200  1.000 29.11000 ? 76  SER B CA  1 
ATOM   615  C C   . SER A 1 76  ? 17.49100  5.72900   26.00000  1.000 28.11000 ? 76  SER B C   1 
ATOM   616  O O   . SER A 1 76  ? 17.00000  5.79200   24.87000  1.000 29.05000 ? 76  SER B O   1 
ATOM   617  C CB  . SER A 1 76  ? 18.08500  3.29600   25.86400  1.000 32.58000 ? 76  SER B CB  1 
ATOM   618  O OG  . SER A 1 76  ? 17.06500  2.80900   26.71700  1.000 32.41000 ? 76  SER B OG  1 
ATOM   619  N N   . LEU A 1 77  ? 17.14300  6.56800   26.98300  1.000 23.03000 ? 77  LEU B N   1 
ATOM   620  C CA  . LEU A 1 77  ? 16.13600  7.60800   26.82000  1.000 19.93000 ? 77  LEU B CA  1 
ATOM   621  C C   . LEU A 1 77  ? 16.81900  8.94100   27.07200  1.000 23.17000 ? 77  LEU B C   1 
ATOM   622  O O   . LEU A 1 77  ? 17.59900  9.40700   26.22600  1.000 26.14000 ? 77  LEU B O   1 
ATOM   623  C CB  . LEU A 1 77  ? 14.94700  7.32000   27.74600  1.000 24.82000 ? 77  LEU B CB  1 
ATOM   624  C CG  . LEU A 1 77  ? 13.69800  8.20300   27.74800  1.000 25.08000 ? 77  LEU B CG  1 
ATOM   625  C CD1 . LEU A 1 77  ? 12.94000  8.13700   26.41100  1.000 26.31000 ? 77  LEU B CD1 1 
ATOM   626  C CD2 . LEU A 1 77  ? 12.77200  7.78900   28.88600  1.000 28.65000 ? 77  LEU B CD2 1 
ATOM   627  N N   . ASP A 1 78  ? 16.60500  9.57300   28.22700  1.000 18.03000 ? 78  ASP B N   1 
ATOM   628  C CA  . ASP A 1 78  ? 17.18300  10.88400  28.52300  1.000 15.66000 ? 78  ASP B CA  1 
ATOM   629  C C   . ASP A 1 78  ? 18.46000  10.81500  29.36900  1.000 18.02000 ? 78  ASP B C   1 
ATOM   630  O O   . ASP A 1 78  ? 19.06400  11.86200  29.64700  1.000 20.36000 ? 78  ASP B O   1 
ATOM   631  C CB  . ASP A 1 78  ? 16.14700  11.78200  29.22000  1.000 18.02000 ? 78  ASP B CB  1 
ATOM   632  C CG  . ASP A 1 78  ? 15.69000  11.22700  30.55400  1.000 16.96000 ? 78  ASP B CG  1 
ATOM   633  O OD1 . ASP A 1 78  ? 15.39200  10.02000  30.64000  1.000 16.61000 ? 78  ASP B OD1 1 
ATOM   634  O OD2 . ASP A 1 78  ? 15.60300  12.02000  31.51400  1.000 16.69000 ? 78  ASP B OD2 1 
ATOM   635  N N   . ASN A 1 79  ? 18.89300  9.61400   29.76100  1.000 17.16000 ? 79  ASN B N   1 
ATOM   636  C CA  . ASN A 1 79  ? 20.19100  9.39400   30.41800  1.000 16.11000 ? 79  ASN B CA  1 
ATOM   637  C C   . ASN A 1 79  ? 20.29400  10.14000  31.75000  1.000 21.31000 ? 79  ASN B C   1 
ATOM   638  O O   . ASN A 1 79  ? 21.23500  10.90300  32.01100  1.000 20.26000 ? 79  ASN B O   1 
ATOM   639  C CB  . ASN A 1 79  ? 21.35400  9.77600   29.49100  1.000 20.34000 ? 79  ASN B CB  1 
ATOM   640  C CG  . ASN A 1 79  ? 22.68000  9.25500   29.99700  1.000 28.54000 ? 79  ASN B CG  1 
ATOM   641  O OD1 . ASN A 1 79  ? 22.73700  8.20200   30.64400  1.000 26.18000 ? 79  ASN B OD1 1 
ATOM   642  N ND2 . ASN A 1 79  ? 23.75300  9.99000   29.72100  1.000 32.21000 ? 79  ASN B ND2 1 
ATOM   643  N N   . ARG A 1 80  ? 19.33000  9.86900   32.62400  1.000 17.05000 ? 80  ARG B N   1 
ATOM   644  C CA  . ARG A 1 80  ? 19.28100  10.48900  33.93800  1.000 16.69000 ? 80  ARG B CA  1 
ATOM   645  C C   . ARG A 1 80  ? 19.16300  9.41800   35.00800  1.000 15.68000 ? 80  ARG B C   1 
ATOM   646  O O   . ARG A 1 80  ? 18.67300  8.31400   34.76400  1.000 17.88000 ? 80  ARG B O   1 
ATOM   647  C CB  . ARG A 1 80  ? 18.09900  11.46300  34.07600  1.000 17.21000 ? 80  ARG B CB  1 
ATOM   648  C CG  . ARG A 1 80  ? 18.22900  12.75000  33.27000  1.000 17.61000 ? 80  ARG B CG  1 
ATOM   649  C CD  . ARG A 1 80  ? 17.24500  13.78400  33.75500  1.000 17.92000 ? 80  ARG B CD  1 
ATOM   650  N NE  . ARG A 1 80  ? 17.49600  15.09800  33.16300  1.000 23.73000 ? 80  ARG B NE  1 
ATOM   651  C CZ  . ARG A 1 80  ? 16.97000  15.51200  32.01500  1.000 25.33000 ? 80  ARG B CZ  1 
ATOM   652  N NH1 . ARG A 1 80  ? 16.12400  14.73300  31.33600  1.000 20.43000 ? 80  ARG B NH1 1 
ATOM   653  N NH2 . ARG A 1 80  ? 17.26900  16.71900  31.55300  1.000 31.15000 ? 80  ARG B NH2 1 
ATOM   654  N N   . HIS A 1 81  ? 19.62100  9.76000   36.20300  1.000 15.51000 ? 81  HIS B N   1 
ATOM   655  C CA  . HIS A 1 81  ? 19.44700  8.91700   37.37700  1.000 15.74000 ? 81  HIS B CA  1 
ATOM   656  C C   . HIS A 1 81  ? 18.14400  9.28600   38.07500  1.000 16.41000 ? 81  HIS B C   1 
ATOM   657  O O   . HIS A 1 81  ? 17.91800  10.45300  38.40900  1.000 16.96000 ? 81  HIS B O   1 
ATOM   658  C CB  . HIS A 1 81  ? 20.64300  9.12100   38.31200  1.000 18.59000 ? 81  HIS B CB  1 
ATOM   659  C CG  . HIS A 1 81  ? 20.58400  8.32100   39.56900  1.000 18.91000 ? 81  HIS B CG  1 
ATOM   660  N ND1 . HIS A 1 81  ? 21.36500  8.61400   40.66800  1.000 29.05000 ? 81  HIS B ND1 1 
ATOM   661  C CD2 . HIS A 1 81  ? 19.88100  7.21200   39.89100  1.000 20.85000 ? 81  HIS B CD2 1 
ATOM   662  C CE1 . HIS A 1 81  ? 21.11900  7.73700   41.62500  1.000 29.93000 ? 81  HIS B CE1 1 
ATOM   663  N NE2 . HIS A 1 81  ? 20.21100  6.88500   41.18500  1.000 26.43000 ? 81  HIS B NE2 1 
ATOM   664  N N   . VAL A 1 82  ? 17.26600  8.29800   38.26900  1.000 14.95000 ? 82  VAL B N   1 
ATOM   665  C CA  . VAL A 1 82  ? 16.06200  8.51900   39.05500  1.000 14.28000 ? 82  VAL B CA  1 
ATOM   666  C C   . VAL A 1 82  ? 15.94000  7.41700   40.09500  1.000 13.07000 ? 82  VAL B C   1 
ATOM   667  O O   . VAL A 1 82  ? 16.47700  6.31800   39.94600  1.000 16.29000 ? 82  VAL B O   1 
ATOM   668  C CB  . VAL A 1 82  ? 14.78100  8.56900   38.18100  1.000 14.82000 ? 82  VAL B CB  1 
ATOM   669  C CG1 . VAL A 1 82  ? 14.77900  9.79600   37.29900  1.000 15.21000 ? 82  VAL B CG1 1 
ATOM   670  C CG2 . VAL A 1 82  ? 14.60100  7.27800   37.37000  1.000 16.40000 ? 82  VAL B CG2 1 
ATOM   671  N N   . LYS A 1 83  ? 15.19300  7.72400   41.15900  1.000 16.29000 ? 83  LYS B N   1 
ATOM   672  C CA  . LYS A 1 83  ? 14.78200  6.73600   42.14300  1.000 16.26000 ? 83  LYS B CA  1 
ATOM   673  C C   . LYS A 1 83  ? 13.34600  6.37500   41.80000  1.000 13.54000 ? 83  LYS B C   1 
ATOM   674  O O   . LYS A 1 83  ? 12.45600  7.22100   41.91000  1.000 15.53000 ? 83  LYS B O   1 
ATOM   675  C CB  . LYS A 1 83  ? 14.88300  7.28800   43.56200  1.000 21.25000 ? 83  LYS B CB  1 
ATOM   676  C CG  . LYS A 1 83  ? 16.29600  7.64200   43.97500  1.000 30.16000 ? 83  LYS B CG  1 
ATOM   677  C CD  . LYS A 1 83  ? 17.04700  6.38500   44.30000  1.000 30.91000 ? 83  LYS B CD  1 
ATOM   678  C CE  . LYS A 1 83  ? 16.80900  6.01400   45.74800  1.000 44.21000 ? 83  LYS B CE  1 
ATOM   679  N NZ  . LYS A 1 83  ? 17.90400  6.46900   46.63800  1.000 48.75000 ? 83  LYS B NZ  1 
ATOM   680  N N   . ALA A 1 84  ? 13.13400  5.14100   41.35800  1.000 15.11000 ? 84  ALA B N   1 
ATOM   681  C CA  . ALA A 1 84  ? 11.83400  4.72900   40.85100  1.000 12.83000 ? 84  ALA B CA  1 
ATOM   682  C C   . ALA A 1 84  ? 11.10700  3.82700   41.83600  1.000 14.07000 ? 84  ALA B C   1 
ATOM   683  O O   . ALA A 1 84  ? 11.71500  3.11200   42.63300  1.000 13.75000 ? 84  ALA B O   1 
ATOM   684  C CB  . ALA A 1 84  ? 11.98600  4.00400   39.51000  1.000 15.66000 ? 84  ALA B CB  1 
ATOM   685  N N   . LEU A 1 85  ? 9.78500   3.84500   41.75800  1.000 12.54000 ? 85  LEU B N   1 
ATOM   686  C CA  . LEU A 1 85  ? 8.97300   3.02400   42.64000  1.000 12.51000 ? 85  LEU B CA  1 
ATOM   687  C C   . LEU A 1 85  ? 7.68400   2.72600   41.90400  1.000 10.09000 ? 85  LEU B C   1 
ATOM   688  O O   . LEU A 1 85  ? 7.04300   3.66400   41.43900  1.000 13.19000 ? 85  LEU B O   1 
ATOM   689  C CB  . LEU A 1 85  ? 8.68900   3.76100   43.94500  1.000 14.25000 ? 85  LEU B CB  1 
ATOM   690  C CG  . LEU A 1 85  ? 7.70200   3.06400   44.88000  1.000 18.38000 ? 85  LEU B CG  1 
ATOM   691  C CD1 . LEU A 1 85  ? 8.32800   1.78300   45.39200  1.000 18.07000 ? 85  LEU B CD1 1 
ATOM   692  C CD2 . LEU A 1 85  ? 7.28700   3.97200   46.05300  1.000 21.44000 ? 85  LEU B CD2 1 
ATOM   693  N N   . VAL A 1 86  ? 7.34700   1.44300   41.77700  1.000 10.57000 ? 86  VAL B N   1 
ATOM   694  C CA  . VAL A 1 86  ? 6.11300   0.99900   41.13800  1.000 11.91000 ? 86  VAL B CA  1 
ATOM   695  C C   . VAL A 1 86  ? 5.18900   0.40400   42.20000  1.000 15.13000 ? 86  VAL B C   1 
ATOM   696  O O   . VAL A 1 86  ? 5.60800   -0.45600  42.99100  1.000 13.34000 ? 86  VAL B O   1 
ATOM   697  C CB  . VAL A 1 86  ? 6.40200   -0.01500  40.02300  1.000 12.68000 ? 86  VAL B CB  1 
ATOM   698  C CG1 . VAL A 1 86  ? 5.08800   -0.37200  39.31500  1.000 14.01000 ? 86  VAL B CG1 1 
ATOM   699  C CG2 . VAL A 1 86  ? 7.38700   0.58800   39.02600  1.000 13.29000 ? 86  VAL B CG2 1 
ATOM   700  N N   . THR A 1 87  ? 3.93300   0.87300   42.23400  1.000 10.96000 ? 87  THR B N   1 
ATOM   701  C CA  . THR A 1 87  ? 2.96100   0.39700   43.21400  1.000 11.64000 ? 87  THR B CA  1 
ATOM   702  C C   . THR A 1 87  ? 1.61200   0.19800   42.54100  1.000 11.31000 ? 87  THR B C   1 
ATOM   703  O O   . THR A 1 87  ? 1.38600   0.63600   41.40900  1.000 13.96000 ? 87  THR B O   1 
ATOM   704  C CB  . THR A 1 87  ? 2.80900   1.38000   44.36800  1.000 13.77000 ? 87  THR B CB  1 
ATOM   705  O OG1 . THR A 1 87  ? 2.46800   2.66400   43.84400  1.000 16.82000 ? 87  THR B OG1 1 
ATOM   706  C CG2 . THR A 1 87  ? 4.12300   1.49200   45.12200  1.000 14.78000 ? 87  THR B CG2 1 
ATOM   707  N N   . TRP A 1 88  ? 0.71700   -0.50400  43.23900  1.000 12.28000 ? 88  TRP B N   1 
ATOM   708  C CA  . TRP A 1 88  ? -0.66700  -0.65800  42.81900  1.000 12.37000 ? 88  TRP B CA  1 
ATOM   709  C C   . TRP A 1 88  ? -1.54200  0.34600   43.55500  1.000 17.94000 ? 88  TRP B C   1 
ATOM   710  O O   . TRP A 1 88  ? -1.53100  0.40900   44.79600  1.000 14.45000 ? 88  TRP B O   1 
ATOM   711  C CB  . TRP A 1 88  ? -1.17800  -2.06300  43.12200  1.000 13.47000 ? 88  TRP B CB  1 
ATOM   712  C CG  . TRP A 1 88  ? -0.61600  -3.15900  42.30000  1.000 16.57000 ? 88  TRP B CG  1 
ATOM   713  C CD1 . TRP A 1 88  ? 0.25600   -4.13100  42.71700  1.000 20.39000 ? 88  TRP B CD1 1 
ATOM   714  C CD2 . TRP A 1 88  ? -0.89800  -3.43300  40.92700  1.000 19.03000 ? 88  TRP B CD2 1 
ATOM   715  N NE1 . TRP A 1 88  ? 0.53500   -4.98600  41.67800  1.000 21.45000 ? 88  TRP B NE1 1 
ATOM   716  C CE2 . TRP A 1 88  ? -0.16200  -4.58400  40.57100  1.000 19.75000 ? 88  TRP B CE2 1 
ATOM   717  C CE3 . TRP A 1 88  ? -1.70400  -2.82200  39.96700  1.000 18.28000 ? 88  TRP B CE3 1 
ATOM   718  C CZ2 . TRP A 1 88  ? -0.20200  -5.13000  39.28500  1.000 22.11000 ? 88  TRP B CZ2 1 
ATOM   719  C CZ3 . TRP A 1 88  ? -1.74400  -3.36500  38.68300  1.000 21.78000 ? 88  TRP B CZ3 1 
ATOM   720  C CH2 . TRP A 1 88  ? -0.99000  -4.50600  38.35800  1.000 22.44000 ? 88  TRP B CH2 1 
ATOM   721  N N   . GLU A 1 89  ? -2.32100  1.10700   42.79700  1.000 14.09000 ? 89  GLU B N   1 
ATOM   722  C CA  . GLU A 1 89  ? -3.33500  1.98400   43.36200  1.000 14.26000 ? 89  GLU B CA  1 
ATOM   723  C C   . GLU A 1 89  ? -4.64200  1.42700   42.82400  1.000 18.11000 ? 89  GLU B C   1 
ATOM   724  O O   . GLU A 1 89  ? -5.06400  1.76500   41.71100  1.000 20.75000 ? 89  GLU B O   1 
ATOM   725  C CB  . GLU A 1 89  ? -3.10700  3.43800   42.97400  1.000 19.61000 ? 89  GLU B CB  1 
ATOM   726  C CG  . GLU A 1 89  ? -2.16400  4.17100   43.92300  1.000 33.33000 ? 89  GLU B CG  1 
ATOM   727  C CD  . GLU A 1 89  ? -1.48700  5.37700   43.28900  1.000 36.75000 ? 89  GLU B CD  1 
ATOM   728  O OE1 . GLU A 1 89  ? -0.36200  5.72200   43.70600  1.000 45.01000 ? 89  GLU B OE1 1 
ATOM   729  O OE2 . GLU A 1 89  ? -2.08600  5.97700   42.37000  1.000 50.80000 ? 89  GLU B OE2 1 
ATOM   730  N N   . GLY A 1 90  ? -5.24800  0.52200   43.58700  1.000 17.36000 ? 90  GLY B N   1 
ATOM   731  C CA  . GLY A 1 90  ? -6.35200  -0.25700  43.05600  1.000 21.10000 ? 90  GLY B CA  1 
ATOM   732  C C   . GLY A 1 90  ? -5.83600  -1.21200  42.00500  1.000 23.33000 ? 90  GLY B C   1 
ATOM   733  O O   . GLY A 1 90  ? -4.91400  -1.99100  42.26500  1.000 22.75000 ? 90  GLY B O   1 
ATOM   734  N N   . ASP A 1 91  ? -6.39500  -1.16200  40.80000  1.000 22.62000 ? 91  ASP B N   1 
ATOM   735  C CA  . ASP A 1 91  ? -5.85300  -1.96200  39.71800  1.000 24.57000 ? 91  ASP B CA  1 
ATOM   736  C C   . ASP A 1 91  ? -5.02000  -1.13700  38.74000  1.000 22.41000 ? 91  ASP B C   1 
ATOM   737  O O   . ASP A 1 91  ? -4.70700  -1.62900  37.65300  1.000 24.68000 ? 91  ASP B O   1 
ATOM   738  C CB  . ASP A 1 91  ? -6.98700  -2.68700  38.98700  1.000 28.53000 ? 91  ASP B CB  1 
ATOM   739  C CG  . ASP A 1 91  ? -7.35400  -4.01700  39.64700  1.000 31.49000 ? 91  ASP B CG  1 
ATOM   740  O OD1 . ASP A 1 91  ? -6.98000  -4.23600  40.81900  1.000 38.59000 ? 91  ASP B OD1 1 
ATOM   741  O OD2 . ASP A 1 91  ? -8.03500  -4.84000  38.99800  1.000 47.72000 ? 91  ASP B OD2 1 
ATOM   742  N N   . VAL A 1 92  ? -4.66800  0.10400   39.09400  1.000 17.39000 ? 92  VAL B N   1 
ATOM   743  C CA  . VAL A 1 92  ? -3.76300  0.92800   38.28800  1.000 14.52000 ? 92  VAL B CA  1 
ATOM   744  C C   . VAL A 1 92  ? -2.33800  0.69700   38.75800  1.000 14.48000 ? 92  VAL B C   1 
ATOM   745  O O   . VAL A 1 92  ? -2.05100  0.81600   39.95000  1.000 13.00000 ? 92  VAL B O   1 
ATOM   746  C CB  . VAL A 1 92  ? -4.11700  2.41600   38.40700  1.000 16.04000 ? 92  VAL B CB  1 
ATOM   747  C CG1 . VAL A 1 92  ? -3.30500  3.25000   37.41800  1.000 17.35000 ? 92  VAL B CG1 1 
ATOM   748  C CG2 . VAL A 1 92  ? -5.62200  2.62200   38.17000  1.000 16.93000 ? 92  VAL B CG2 1 
ATOM   749  N N   . LEU A 1 93  ? -1.43900  0.40300   37.82200  1.000 10.17000 ? 93  LEU B N   1 
ATOM   750  C CA  . LEU A 1 93  ? -0.01300  0.26400   38.12200  1.000 10.91000 ? 93  LEU B CA  1 
ATOM   751  C C   . LEU A 1 93  ? 0.65000   1.62600   37.95400  1.000 12.06000 ? 93  LEU B C   1 
ATOM   752  O O   . LEU A 1 93  ? 0.56000   2.23500   36.88700  1.000 12.81000 ? 93  LEU B O   1 
ATOM   753  C CB  . LEU A 1 93  ? 0.61400   -0.77900  37.19900  1.000 13.49000 ? 93  LEU B CB  1 
ATOM   754  C CG  . LEU A 1 93  ? 1.99600   -1.26800  37.64300  1.000 13.94000 ? 93  LEU B CG  1 
ATOM   755  C CD1 . LEU A 1 93  ? 1.93900   -2.04400  38.94700  1.000 12.69000 ? 93  LEU B CD1 1 
ATOM   756  C CD2 . LEU A 1 93  ? 2.57800   -2.15300  36.53500  1.000 13.64000 ? 93  LEU B CD2 1 
ATOM   757  N N   . VAL A 1 94  ? 1.28900   2.12600   39.01100  1.000 8.72000  ? 94  VAL B N   1 
ATOM   758  C CA  . VAL A 1 94  ? 1.72800   3.51600   39.05600  1.000 8.48000  ? 94  VAL B CA  1 
ATOM   759  C C   . VAL A 1 94  ? 3.23000   3.53700   39.29500  1.000 12.47000 ? 94  VAL B C   1 
ATOM   760  O O   . VAL A 1 94  ? 3.71900   2.94800   40.26100  1.000 13.00000 ? 94  VAL B O   1 
ATOM   761  C CB  . VAL A 1 94  ? 1.00100   4.30300   40.15500  1.000 14.54000 ? 94  VAL B CB  1 
ATOM   762  C CG1 . VAL A 1 94  ? 1.54600   5.71800   40.23500  1.000 14.91000 ? 94  VAL B CG1 1 
ATOM   763  C CG2 . VAL A 1 94  ? -0.54500  4.30000   39.86600  1.000 13.34000 ? 94  VAL B CG2 1 
ATOM   764  N N   . CYS A 1 95  ? 3.95100   4.24300   38.44100  1.000 11.43000 ? 95  CYS B N   1 
ATOM   765  C CA  . CYS A 1 95  ? 5.38300   4.42500   38.61800  1.000 11.99000 ? 95  CYS B CA  1 
ATOM   766  C C   . CYS A 1 95  ? 5.69400   5.89300   38.87800  1.000 12.04000 ? 95  CYS B C   1 
ATOM   767  O O   . CYS A 1 95  ? 5.25600   6.76300   38.12200  1.000 12.23000 ? 95  CYS B O   1 
ATOM   768  C CB  . CYS A 1 95  ? 6.12300   3.94700   37.37300  1.000 8.62000  ? 95  CYS B CB  1 
ATOM   769  S SG  . CYS A 1 95  ? 7.91800   4.21400   37.48900  1.000 16.22000 ? 95  CYS B SG  1 
ATOM   770  N N   . VAL A 1 96  ? 6.44000   6.17700   39.94700  1.000 11.35000 ? 96  VAL B N   1 
ATOM   771  C CA  A VAL A 1 96  ? 6.96000   7.51600   40.20000  0.270 10.84000 ? 96  VAL B CA  1 
ATOM   772  C CA  B VAL A 1 96  ? 6.95900   7.51400   40.20400  0.730 11.00000 ? 96  VAL B CA  1 
ATOM   773  C C   . VAL A 1 96  ? 8.47500   7.44600   40.09800  1.000 11.96000 ? 96  VAL B C   1 
ATOM   774  O O   . VAL A 1 96  ? 9.09800   6.55100   40.67500  1.000 15.37000 ? 96  VAL B O   1 
ATOM   775  C CB  A VAL A 1 96  ? 6.52800   8.05900   41.57300  0.270 13.79000 ? 96  VAL B CB  1 
ATOM   776  C CB  B VAL A 1 96  ? 6.54100   8.04300   41.58500  0.730 13.66000 ? 96  VAL B CB  1 
ATOM   777  C CG1 A VAL A 1 96  ? 5.03300   8.34600   41.59100  0.270 17.80000 ? 96  VAL B CG1 1 
ATOM   778  C CG1 B VAL A 1 96  ? 7.13500   9.43500   41.80400  0.730 14.27000 ? 96  VAL B CG1 1 
ATOM   779  C CG2 A VAL A 1 96  ? 6.91900   7.09300   42.67300  0.270 13.69000 ? 96  VAL B CG2 1 
ATOM   780  C CG2 B VAL A 1 96  ? 5.02900   8.07700   41.69800  0.730 18.36000 ? 96  VAL B CG2 1 
ATOM   781  N N   . GLN A 1 97  ? 9.06000   8.36700   39.34200  1.000 14.64000 ? 97  GLN B N   1 
ATOM   782  C CA  . GLN A 1 97  ? 10.51300  8.43400   39.16700  1.000 13.68000 ? 97  GLN B CA  1 
ATOM   783  C C   . GLN A 1 97  ? 10.98800  9.75200   39.76400  1.000 14.62000 ? 97  GLN B C   1 
ATOM   784  O O   . GLN A 1 97  ? 10.83400  10.81000  39.14300  1.000 14.96000 ? 97  GLN B O   1 
ATOM   785  C CB  . GLN A 1 97  ? 10.87800  8.32100   37.69300  1.000 12.57000 ? 97  GLN B CB  1 
ATOM   786  C CG  . GLN A 1 97  ? 10.60200  6.93900   37.11600  1.000 11.54000 ? 97  GLN B CG  1 
ATOM   787  C CD  . GLN A 1 97  ? 10.60600  6.95400   35.60400  1.000 21.21000 ? 97  GLN B CD  1 
ATOM   788  O OE1 . GLN A 1 97  ? 10.05600  7.86100   34.98500  1.000 20.69000 ? 97  GLN B OE1 1 
ATOM   789  N NE2 . GLN A 1 97  ? 11.20400  5.93800   35.00300  1.000 24.20000 ? 97  GLN B NE2 1 
ATOM   790  N N   . LYS A 1 98  ? 11.53400  9.69900   40.97100  1.000 17.31000 ? 98  LYS B N   1 
ATOM   791  C CA  . LYS A 1 98  ? 11.99500  10.90100  41.64800  1.000 17.91000 ? 98  LYS B CA  1 
ATOM   792  C C   . LYS A 1 98  ? 13.35300  11.32800  41.12200  1.000 17.24000 ? 98  LYS B C   1 
ATOM   793  O O   . LYS A 1 98  ? 14.24100  10.51400  40.97800  1.000 19.11000 ? 98  LYS B O   1 
ATOM   794  C CB  . LYS A 1 98  ? 12.09300  10.64800  43.14200  1.000 21.35000 ? 98  LYS B CB  1 
ATOM   795  C CG  . LYS A 1 98  ? 10.78600  10.28100  43.80200  1.000 27.04000 ? 98  LYS B CG  1 
ATOM   796  C CD  . LYS A 1 98  ? 10.91900  10.42600  45.30700  1.000 34.83000 ? 98  LYS B CD  1 
ATOM   797  C CE  . LYS A 1 98  ? 9.76800   9.78500   46.05300  1.000 42.91000 ? 98  LYS B CE  1 
ATOM   798  N NZ  . LYS A 1 98  ? 10.10400  9.67600   47.49700  1.000 48.68000 ? 98  LYS B NZ  1 
ATOM   799  N N   . GLY A 1 99  ? 13.51000  12.61700  40.86400  1.000 17.90000 ? 99  GLY B N   1 
ATOM   800  C CA  . GLY A 1 99  ? 14.76700  13.11500  40.32200  1.000 21.41000 ? 99  GLY B CA  1 
ATOM   801  C C   . GLY A 1 99  ? 14.63600  14.56000  39.89200  1.000 19.35000 ? 99  GLY B C   1 
ATOM   802  O O   . GLY A 1 99  ? 13.86800  15.33000  40.48000  1.000 26.15000 ? 99  GLY B O   1 
ATOM   803  N N   . GLU A 1 100 ? 15.38800  14.93600  38.86300  1.000 17.96000 ? 100 GLU B N   1 
ATOM   804  C CA  . GLU A 1 100 ? 15.35800  16.30200  38.35100  1.000 26.63000 ? 100 GLU B CA  1 
ATOM   805  C C   . GLU A 1 100 ? 13.97300  16.67700  37.83300  1.000 26.24000 ? 100 GLU B C   1 
ATOM   806  O O   . GLU A 1 100 ? 13.29200  17.52400  38.41100  1.000 28.44000 ? 100 GLU B O   1 
ATOM   807  C CB  . GLU A 1 100 ? 16.39900  16.48300  37.24500  1.000 24.80000 ? 100 GLU B CB  1 
ATOM   808  C CG  . GLU A 1 100 ? 16.39600  17.86400  36.61000  1.000 30.24000 ? 100 GLU B CG  1 
ATOM   809  C CD  . GLU A 1 100 ? 16.38100  18.97800  37.63900  1.000 36.28000 ? 100 GLU B CD  1 
ATOM   810  O OE1 . GLU A 1 100 ? 15.92800  20.09300  37.30400  1.000 36.98000 ? 100 GLU B OE1 1 
ATOM   811  O OE2 . GLU A 1 100 ? 16.82300  18.73900  38.78200  1.000 35.05000 ? 100 GLU B OE2 1 
ATOM   812  N N   . LYS A 1 101 ? 13.57000  16.02800  36.73500  1.000 24.10000 ? 101 LYS B N   1 
ATOM   813  C CA  . LYS A 1 101 ? 12.24400  16.27700  36.10700  1.000 28.35000 ? 101 LYS B CA  1 
ATOM   814  C C   . LYS A 1 101 ? 11.14500  16.07700  37.15600  1.000 29.93000 ? 101 LYS B C   1 
ATOM   815  O O   . LYS A 1 101 ? 11.19000  15.05900  37.87500  1.000 29.25000 ? 101 LYS B O   1 
ATOM   816  C CB  . LYS A 1 101 ? 12.03800  15.34300  34.91000  1.000 20.11000 ? 101 LYS B CB  1 
ATOM   817  C CG  . LYS A 1 101 ? 12.90400  15.64300  33.69400  1.000 25.53000 ? 101 LYS B CG  1 
ATOM   818  C CD  . LYS A 1 101 ? 12.79800  17.07700  33.22000  1.000 27.06000 ? 101 LYS B CD  1 
ATOM   819  C CE  . LYS A 1 101 ? 13.48600  17.31600  31.89300  1.000 30.43000 ? 101 LYS B CE  1 
ATOM   820  N NZ  . LYS A 1 101 ? 13.25900  18.69400  31.39700  1.000 32.83000 ? 101 LYS B NZ  1 
ATOM   821  N N   . GLU A 1 102 ? 10.19700  17.01600  37.23000  1.000 27.51000 ? 102 GLU B N   1 
ATOM   822  C CA  . GLU A 1 102 ? 9.08200   16.93700  38.21200  1.000 27.27000 ? 102 GLU B CA  1 
ATOM   823  C C   . GLU A 1 102 ? 7.89400   16.20500  37.57900  1.000 25.07000 ? 102 GLU B C   1 
ATOM   824  O O   . GLU A 1 102 ? 7.76900   16.24100  36.33800  1.000 22.30000 ? 102 GLU B O   1 
ATOM   825  C CB  . GLU A 1 102 ? 8.68100   18.34100  38.67000  1.000 41.24000 ? 102 GLU B CB  1 
ATOM   826  C CG  . GLU A 1 102 ? 9.40300   19.44700  37.92200  1.000 44.16000 ? 102 GLU B CG  1 
ATOM   827  C CD  . GLU A 1 102 ? 9.03300   20.85500  38.35500  1.000 60.40000 ? 102 GLU B CD  1 
ATOM   828  O OE1 . GLU A 1 102 ? 9.94100   21.60200  38.77100  1.000 66.72000 ? 102 GLU B OE1 1 
ATOM   829  O OE2 . GLU A 1 102 ? 7.83800   21.20200  38.27500  1.000 56.89000 ? 102 GLU B OE2 1 
ATOM   830  N N   . ASN A 1 103 ? 7.06600   15.56500  38.41100  1.000 25.38000 ? 103 ASN B N   1 
ATOM   831  C CA  . ASN A 1 103 ? 5.86400   14.82100  37.94500  1.000 26.38000 ? 103 ASN B CA  1 
ATOM   832  C C   . ASN A 1 103 ? 6.26500   13.78200  36.89000  1.000 23.28000 ? 103 ASN B C   1 
ATOM   833  O O   . ASN A 1 103 ? 5.52900   13.64500  35.89200  1.000 23.00000 ? 103 ASN B O   1 
ATOM   834  C CB  . ASN A 1 103 ? 4.77600   15.76400  37.42200  1.000 26.67000 ? 103 ASN B CB  1 
ATOM   835  C CG  . ASN A 1 103 ? 4.42600   16.86400  38.40100  1.000 42.02000 ? 103 ASN B CG  1 
ATOM   836  O OD1 . ASN A 1 103 ? 4.47000   16.66100  39.61200  1.000 46.52000 ? 103 ASN B OD1 1 
ATOM   837  N ND2 . ASN A 1 103 ? 4.07600   18.03100  37.88600  1.000 48.68000 ? 103 ASN B ND2 1 
ATOM   838  N N   . ARG A 1 104 ? 7.38400   13.08200  37.10600  1.000 18.41000 ? 104 ARG B N   1 
ATOM   839  C CA  . ARG A 1 104 ? 7.83000   12.05900  36.16800  1.000 12.71000 ? 104 ARG B CA  1 
ATOM   840  C C   . ARG A 1 104 ? 7.33000   10.67700  36.57700  1.000 14.48000 ? 104 ARG B C   1 
ATOM   841  O O   . ARG A 1 104 ? 7.21700   10.37400  37.76400  1.000 19.62000 ? 104 ARG B O   1 
ATOM   842  C CB  . ARG A 1 104 ? 9.35700   12.05500  36.06800  1.000 14.09000 ? 104 ARG B CB  1 
ATOM   843  C CG  . ARG A 1 104 ? 9.90100   11.22100  34.91900  1.000 15.41000 ? 104 ARG B CG  1 
ATOM   844  C CD  . ARG A 1 104 ? 11.42000  11.17700  34.93800  1.000 19.41000 ? 104 ARG B CD  1 
ATOM   845  N NE  . ARG A 1 104 ? 11.95300  10.29800  33.90100  1.000 18.11000 ? 104 ARG B NE  1 
ATOM   846  C CZ  . ARG A 1 104 ? 13.11300  10.49100  33.28100  1.000 19.60000 ? 104 ARG B CZ  1 
ATOM   847  N NH1 . ARG A 1 104 ? 13.86800  11.53500  33.59300  1.000 16.62000 ? 104 ARG B NH1 1 
ATOM   848  N NH2 . ARG A 1 104 ? 13.51800  9.63900   32.35000  1.000 18.02000 ? 104 ARG B NH2 1 
ATOM   849  N N   . GLY A 1 105 ? 7.03300   9.84400   35.58500  1.000 14.45000 ? 105 GLY B N   1 
ATOM   850  C CA  . GLY A 1 105 ? 6.54800   8.50000   35.84000  1.000 13.21000 ? 105 GLY B CA  1 
ATOM   851  C C   . GLY A 1 105 ? 5.58200   8.01100   34.78000  1.000 12.45000 ? 105 GLY B C   1 
ATOM   852  O O   . GLY A 1 105 ? 5.60600   8.47500   33.64000  1.000 15.43000 ? 105 GLY B O   1 
ATOM   853  N N   . TRP A 1 106 ? 4.72700   7.06700   35.16100  1.000 12.98000 ? 106 TRP B N   1 
ATOM   854  C CA  . TRP A 1 106 ? 3.75100   6.50800   34.25400  1.000 11.39000 ? 106 TRP B CA  1 
ATOM   855  C C   . TRP A 1 106 ? 2.67700   5.76400   35.02400  1.000 12.79000 ? 106 TRP B C   1 
ATOM   856  O O   . TRP A 1 106 ? 2.83100   5.48000   36.19100  1.000 11.47000 ? 106 TRP B O   1 
ATOM   857  C CB  . TRP A 1 106 ? 4.39400   5.61600   33.17600  1.000 12.56000 ? 106 TRP B CB  1 
ATOM   858  C CG  . TRP A 1 106 ? 5.31400   4.50900   33.64000  1.000 13.08000 ? 106 TRP B CG  1 
ATOM   859  C CD1 . TRP A 1 106 ? 6.67200   4.47300   33.52200  1.000 13.83000 ? 106 TRP B CD1 1 
ATOM   860  C CD2 . TRP A 1 106 ? 4.94100   3.25500   34.23400  1.000 12.54000 ? 106 TRP B CD2 1 
ATOM   861  N NE1 . TRP A 1 106 ? 7.16300   3.29700   34.01700  1.000 15.28000 ? 106 TRP B NE1 1 
ATOM   862  C CE2 . TRP A 1 106 ? 6.12300   2.53600   34.46700  1.000 14.83000 ? 106 TRP B CE2 1 
ATOM   863  C CE3 . TRP A 1 106 ? 3.72800   2.68300   34.60700  1.000 14.48000 ? 106 TRP B CE3 1 
ATOM   864  C CZ2 . TRP A 1 106 ? 6.12700   1.28500   35.04800  1.000 14.08000 ? 106 TRP B CZ2 1 
ATOM   865  C CZ3 . TRP A 1 106 ? 3.73900   1.43900   35.19100  1.000 13.46000 ? 106 TRP B CZ3 1 
ATOM   866  C CH2 . TRP A 1 106 ? 4.92700   0.75500   35.40400  1.000 13.31000 ? 106 TRP B CH2 1 
ATOM   867  N N   . LYS A 1 107 ? 1.56800   5.50600   34.35500  1.000 11.88000 ? 107 LYS B N   1 
ATOM   868  C CA  . LYS A 1 107 ? 0.46500   4.78600   34.94600  1.000 12.38000 ? 107 LYS B CA  1 
ATOM   869  C C   . LYS A 1 107 ? -0.04600  3.83600   33.88800  1.000 13.79000 ? 107 LYS B C   1 
ATOM   870  O O   . LYS A 1 107 ? -0.14500  4.20500   32.72800  1.000 14.99000 ? 107 LYS B O   1 
ATOM   871  C CB  . LYS A 1 107 ? -0.65400  5.72900   35.37400  1.000 16.97000 ? 107 LYS B CB  1 
ATOM   872  C CG  . LYS A 1 107 ? -0.28100  6.66800   36.50700  1.000 15.17000 ? 107 LYS B CG  1 
ATOM   873  C CD  . LYS A 1 107 ? -1.48700  7.44900   37.00300  1.000 20.18000 ? 107 LYS B CD  1 
ATOM   874  C CE  . LYS A 1 107 ? -1.12300  8.41000   38.12800  1.000 31.99000 ? 107 LYS B CE  1 
ATOM   875  N NZ  . LYS A 1 107 ? -2.31700  9.11200   38.67100  1.000 39.25000 ? 107 LYS B NZ  1 
ATOM   876  N N   . LYS A 1 108 ? -0.39100  2.62900   34.30400  1.000 13.10000 ? 108 LYS B N   1 
ATOM   877  C CA  . LYS A 1 108 ? -0.86300  1.61700   33.38500  1.000 13.97000 ? 108 LYS B CA  1 
ATOM   878  C C   . LYS A 1 108 ? -2.20600  1.04500   33.82200  1.000 17.42000 ? 108 LYS B C   1 
ATOM   879  O O   . LYS A 1 108 ? -2.35500  0.58500   34.93600  1.000 16.28000 ? 108 LYS B O   1 
ATOM   880  C CB  . LYS A 1 108 ? 0.17800   0.49500   33.31000  1.000 18.81000 ? 108 LYS B CB  1 
ATOM   881  C CG  . LYS A 1 108 ? 0.10900   -0.38300  32.08200  1.000 26.99000 ? 108 LYS B CG  1 
ATOM   882  C CD  . LYS A 1 108 ? 1.09000   -1.54800  32.15200  1.000 29.23000 ? 108 LYS B CD  1 
ATOM   883  C CE  . LYS A 1 108 ? 2.51900   -1.11800  32.45400  1.000 27.42000 ? 108 LYS B CE  1 
ATOM   884  N NZ  . LYS A 1 108 ? 3.28600   -0.47500  31.34900  1.000 28.66000 ? 108 LYS B NZ  1 
ATOM   885  N N   . TRP A 1 109 ? -3.17500  1.09500   32.92100  1.000 13.59000 ? 109 TRP B N   1 
ATOM   886  C CA  . TRP A 1 109 ? -4.49500  0.54700   33.16800  1.000 12.90000 ? 109 TRP B CA  1 
ATOM   887  C C   . TRP A 1 109 ? -4.67400  -0.62000  32.21700  1.000 16.21000 ? 109 TRP B C   1 
ATOM   888  O O   . TRP A 1 109 ? -4.55800  -0.44500  31.02300  1.000 19.92000 ? 109 TRP B O   1 
ATOM   889  C CB  . TRP A 1 109 ? -5.57600  1.56800   32.82000  1.000 15.40000 ? 109 TRP B CB  1 
ATOM   890  C CG  . TRP A 1 109 ? -5.67900  2.75800   33.69700  1.000 17.27000 ? 109 TRP B CG  1 
ATOM   891  C CD1 . TRP A 1 109 ? -6.53900  2.93400   34.73300  1.000 14.47000 ? 109 TRP B CD1 1 
ATOM   892  C CD2 . TRP A 1 109 ? -4.93000  3.96700   33.59100  1.000 14.64000 ? 109 TRP B CD2 1 
ATOM   893  N NE1 . TRP A 1 109 ? -6.36300  4.16800   35.29100  1.000 14.96000 ? 109 TRP B NE1 1 
ATOM   894  C CE2 . TRP A 1 109 ? -5.37900  4.82500   34.60500  1.000 14.61000 ? 109 TRP B CE2 1 
ATOM   895  C CE3 . TRP A 1 109 ? -3.91400  4.40300   32.74500  1.000 14.60000 ? 109 TRP B CE3 1 
ATOM   896  C CZ2 . TRP A 1 109 ? -4.84600  6.08700   34.79400  1.000 18.52000 ? 109 TRP B CZ2 1 
ATOM   897  C CZ3 . TRP A 1 109 ? -3.39800  5.65200   32.93000  1.000 16.36000 ? 109 TRP B CZ3 1 
ATOM   898  C CH2 . TRP A 1 109 ? -3.85700  6.48100   33.94800  1.000 19.29000 ? 109 TRP B CH2 1 
ATOM   899  N N   . ILE A 1 110 ? -4.96900  -1.79600  32.74100  1.000 16.63000 ? 110 ILE B N   1 
ATOM   900  C CA  . ILE A 1 110 ? -5.19000  -2.95200  31.89700  1.000 22.45000 ? 110 ILE B CA  1 
ATOM   901  C C   . ILE A 1 110 ? -6.67400  -3.26800  31.86600  1.000 31.11000 ? 110 ILE B C   1 
ATOM   902  O O   . ILE A 1 110 ? -7.26800  -3.52500  32.89500  1.000 30.43000 ? 110 ILE B O   1 
ATOM   903  C CB  . ILE A 1 110 ? -4.42200  -4.18000  32.39400  1.000 31.13000 ? 110 ILE B CB  1 
ATOM   904  C CG1 . ILE A 1 110 ? -2.93200  -3.87500  32.45800  1.000 28.05000 ? 110 ILE B CG1 1 
ATOM   905  C CG2 . ILE A 1 110 ? -4.66400  -5.35800  31.47100  1.000 35.11000 ? 110 ILE B CG2 1 
ATOM   906  C CD1 . ILE A 1 110 ? -2.26000  -3.94500  31.11400  1.000 32.16000 ? 110 ILE B CD1 1 
ATOM   907  N N   . GLU A 1 111 ? -7.26000  -3.24600  30.67300  1.000 26.48000 ? 111 GLU B N   1 
ATOM   908  C CA  . GLU A 1 111 ? -8.68000  -3.53200  30.51200  1.000 29.34000 ? 111 GLU B CA  1 
ATOM   909  C C   . GLU A 1 111 ? -8.90700  -4.58300  29.43000  1.000 29.42000 ? 111 GLU B C   1 
ATOM   910  O O   . GLU A 1 111 ? -8.98900  -4.25900  28.24500  1.000 29.51000 ? 111 GLU B O   1 
ATOM   911  C CB  . GLU A 1 111 ? -9.45000  -2.25400  30.17300  1.000 31.75000 ? 111 GLU B CB  1 
ATOM   912  C CG  . GLU A 1 111 ? -10.14200 -1.61200  31.36400  1.000 44.56000 ? 111 GLU B CG  1 
ATOM   913  C CD  . GLU A 1 111 ? -9.86400  -0.12500  31.46700  1.000 42.96000 ? 111 GLU B CD  1 
ATOM   914  O OE1 . GLU A 1 111 ? -9.20800  0.29100   32.44500  1.000 39.24000 ? 111 GLU B OE1 1 
ATOM   915  O OE2 . GLU A 1 111 ? -10.30000 0.62600   30.57100  1.000 45.17000 ? 111 GLU B OE2 1 
ATOM   916  N N   . GLY A 1 112 ? -9.00700  -5.84100  29.84500  1.000 38.20000 ? 112 GLY B N   1 
ATOM   917  C CA  . GLY A 1 112 ? -9.22200  -6.93500  28.91600  1.000 37.62000 ? 112 GLY B CA  1 
ATOM   918  C C   . GLY A 1 112 ? -8.02200  -7.17600  28.02200  1.000 37.36000 ? 112 GLY B C   1 
ATOM   919  O O   . GLY A 1 112 ? -6.97000  -7.61700  28.48400  1.000 38.24000 ? 112 GLY B O   1 
ATOM   920  N N   . ASP A 1 113 ? -8.18100  -6.88500  26.73500  1.000 29.99000 ? 113 ASP B N   1 
ATOM   921  C CA  . ASP A 1 113 ? -7.10500  -7.07000  25.76900  1.000 31.68000 ? 113 ASP B CA  1 
ATOM   922  C C   . ASP A 1 113 ? -6.48500  -5.73300  25.37600  1.000 28.15000 ? 113 ASP B C   1 
ATOM   923  O O   . ASP A 1 113 ? -5.76900  -5.63800  24.38000  1.000 27.46000 ? 113 ASP B O   1 
ATOM   924  C CB  . ASP A 1 113 ? -7.62000  -7.79600  24.52500  1.000 33.79000 ? 113 ASP B CB  1 
ATOM   925  C CG  . ASP A 1 113 ? -8.39800  -6.88300  23.59700  1.000 40.19000 ? 113 ASP B CG  1 
ATOM   926  O OD1 . ASP A 1 113 ? -8.35000  -7.10100  22.36800  1.000 48.68000 ? 113 ASP B OD1 1 
ATOM   927  O OD2 . ASP A 1 113 ? -9.05900  -5.94900  24.09700  1.000 45.41000 ? 113 ASP B OD2 1 
ATOM   928  N N   . LYS A 1 114 ? -6.76600  -4.70200  26.16600  1.000 24.63000 ? 114 LYS B N   1 
ATOM   929  C CA  . LYS A 1 114 ? -6.23800  -3.36900  25.90100  1.000 19.42000 ? 114 LYS B CA  1 
ATOM   930  C C   . LYS A 1 114 ? -5.40800  -2.85500  27.07200  1.000 21.67000 ? 114 LYS B C   1 
ATOM   931  O O   . LYS A 1 114 ? -5.70600  -3.14300  28.23200  1.000 21.81000 ? 114 LYS B O   1 
ATOM   932  C CB  . LYS A 1 114 ? -7.37700  -2.39200  25.60000  1.000 22.64000 ? 114 LYS B CB  1 
ATOM   933  C CG  . LYS A 1 114 ? -8.14100  -2.70200  24.32300  1.000 35.26000 ? 114 LYS B CG  1 
ATOM   934  C CD  . LYS A 1 114 ? -7.88200  -1.65100  23.25500  1.000 34.83000 ? 114 LYS B CD  1 
ATOM   935  C CE  . LYS A 1 114 ? -8.81500  -0.46200  23.41300  1.000 35.18000 ? 114 LYS B CE  1 
ATOM   936  N NZ  . LYS A 1 114 ? -8.98400  0.28400   22.13600  1.000 46.19000 ? 114 LYS B NZ  1 
ATOM   937  N N   . LEU A 1 115 ? -4.36400  -2.09400  26.76100  1.000 14.74000 ? 115 LEU B N   1 
ATOM   938  C CA  . LEU A 1 115 ? -3.50000  -1.53800  27.77400  1.000 16.92000 ? 115 LEU B CA  1 
ATOM   939  C C   . LEU A 1 115 ? -3.41600  -0.04600  27.52400  1.000 17.71000 ? 115 LEU B C   1 
ATOM   940  O O   . LEU A 1 115 ? -3.08600  0.37700   26.43100  1.000 16.96000 ? 115 LEU B O   1 
ATOM   941  C CB  . LEU A 1 115 ? -2.11400  -2.17400  27.70500  1.000 15.36000 ? 115 LEU B CB  1 
ATOM   942  C CG  . LEU A 1 115 ? -1.10100  -1.81000  28.79500  1.000 19.34000 ? 115 LEU B CG  1 
ATOM   943  C CD1 . LEU A 1 115 ? -0.06600  -2.91100  28.93500  1.000 21.59000 ? 115 LEU B CD1 1 
ATOM   944  C CD2 . LEU A 1 115 ? -0.41600  -0.50800  28.44800  1.000 19.83000 ? 115 LEU B CD2 1 
ATOM   945  N N   . TYR A 1 116 ? -3.77000  0.74000   28.53200  1.000 14.10000 ? 116 TYR B N   1 
ATOM   946  C CA  . TYR A 1 116 ? -3.71000  2.18700   28.43500  1.000 12.67000 ? 116 TYR B CA  1 
ATOM   947  C C   . TYR A 1 116 ? -2.50700  2.65200   29.22100  1.000 13.97000 ? 116 TYR B C   1 
ATOM   948  O O   . TYR A 1 116 ? -2.36200  2.31400   30.37500  1.000 13.53000 ? 116 TYR B O   1 
ATOM   949  C CB  . TYR A 1 116 ? -4.97700  2.83600   28.99100  1.000 14.96000 ? 116 TYR B CB  1 
ATOM   950  C CG  . TYR A 1 116 ? -6.20500  2.51700   28.18600  1.000 14.24000 ? 116 TYR B CG  1 
ATOM   951  C CD1 . TYR A 1 116 ? -6.92000  1.36400   28.41900  1.000 19.08000 ? 116 TYR B CD1 1 
ATOM   952  C CD2 . TYR A 1 116 ? -6.63400  3.36000   27.18400  1.000 15.15000 ? 116 TYR B CD2 1 
ATOM   953  C CE1 . TYR A 1 116 ? -8.03500  1.05600   27.67200  1.000 19.26000 ? 116 TYR B CE1 1 
ATOM   954  C CE2 . TYR A 1 116 ? -7.74700  3.06100   26.43500  1.000 21.93000 ? 116 TYR B CE2 1 
ATOM   955  C CZ  . TYR A 1 116 ? -8.44000  1.90900   26.68900  1.000 20.90000 ? 116 TYR B CZ  1 
ATOM   956  O OH  . TYR A 1 116 ? -9.54400  1.61200   25.94500  1.000 25.48000 ? 116 TYR B OH  1 
ATOM   957  N N   . LEU A 1 117 ? -1.65400  3.43800   28.58500  1.000 13.04000 ? 117 LEU B N   1 
ATOM   958  C CA  . LEU A 1 117 ? -0.45700  3.91800   29.24300  1.000 13.90000 ? 117 LEU B CA  1 
ATOM   959  C C   . LEU A 1 117 ? -0.37200  5.42800   29.20000  1.000 17.07000 ? 117 LEU B C   1 
ATOM   960  O O   . LEU A 1 117 ? -0.52900  6.02700   28.15400  1.000 17.00000 ? 117 LEU B O   1 
ATOM   961  C CB  . LEU A 1 117 ? 0.76900   3.32700   28.55800  1.000 17.01000 ? 117 LEU B CB  1 
ATOM   962  C CG  . LEU A 1 117 ? 2.13300   3.76900   29.07400  1.000 18.11000 ? 117 LEU B CG  1 
ATOM   963  C CD1 . LEU A 1 117 ? 2.32800   3.30500   30.50500  1.000 16.60000 ? 117 LEU B CD1 1 
ATOM   964  C CD2 . LEU A 1 117 ? 3.22900   3.21900   28.18000  1.000 19.85000 ? 117 LEU B CD2 1 
ATOM   965  N N   . GLU A 1 118 ? -0.15100  6.04200   30.35300  1.000 12.83000 ? 118 GLU B N   1 
ATOM   966  C CA  . GLU A 1 118 ? 0.00800   7.48000   30.40800  1.000 14.68000 ? 118 GLU B CA  1 
ATOM   967  C C   . GLU A 1 118 ? 1.40200   7.78600   30.94000  1.000 16.50000 ? 118 GLU B C   1 
ATOM   968  O O   . GLU A 1 118 ? 1.74500   7.39500   32.03500  1.000 15.99000 ? 118 GLU B O   1 
ATOM   969  C CB  . GLU A 1 118 ? -1.07200  8.13300   31.26400  1.000 16.44000 ? 118 GLU B CB  1 
ATOM   970  C CG  . GLU A 1 118 ? -2.37200  8.33500   30.50400  1.000 20.19000 ? 118 GLU B CG  1 
ATOM   971  C CD  . GLU A 1 118 ? -3.44200  9.06200   31.30000  1.000 29.53000 ? 118 GLU B CD  1 
ATOM   972  O OE1 . GLU A 1 118 ? -4.62400  8.88200   30.96900  1.000 34.25000 ? 118 GLU B OE1 1 
ATOM   973  O OE2 . GLU A 1 118 ? -3.11200  9.80400   32.24400  1.000 35.32000 ? 118 GLU B OE2 1 
ATOM   974  N N   . LEU A 1 119 ? 2.20700   8.44600   30.12000  1.000 12.85000 ? 119 LEU B N   1 
ATOM   975  C CA  . LEU A 1 119 ? 3.55900   8.81400   30.49400  1.000 13.42000 ? 119 LEU B CA  1 
ATOM   976  C C   . LEU A 1 119 ? 3.57000   10.29900  30.80900  1.000 17.53000 ? 119 LEU B C   1 
ATOM   977  O O   . LEU A 1 119 ? 3.06500   11.10200  30.04900  1.000 19.03000 ? 119 LEU B O   1 
ATOM   978  C CB  . LEU A 1 119 ? 4.54000   8.47800   29.37600  1.000 16.79000 ? 119 LEU B CB  1 
ATOM   979  C CG  . LEU A 1 119 ? 4.49900   7.01200   28.96800  1.000 18.27000 ? 119 LEU B CG  1 
ATOM   980  C CD1 . LEU A 1 119 ? 4.55900   6.87700   27.46200  1.000 27.10000 ? 119 LEU B CD1 1 
ATOM   981  C CD2 . LEU A 1 119 ? 5.62200   6.23500   29.62300  1.000 24.57000 ? 119 LEU B CD2 1 
ATOM   982  N N   . THR A 1 120 ? 4.15400   10.64500  31.94300  1.000 14.56000 ? 120 THR B N   1 
ATOM   983  C CA  . THR A 1 120 ? 4.15600   12.03000  32.38300  1.000 15.57000 ? 120 THR B CA  1 
ATOM   984  C C   . THR A 1 120 ? 5.57300   12.54100  32.61100  1.000 16.44000 ? 120 THR B C   1 
ATOM   985  O O   . THR A 1 120 ? 6.47700   11.80400  33.03500  1.000 15.69000 ? 120 THR B O   1 
ATOM   986  C CB  . THR A 1 120 ? 3.34700   12.22600  33.67400  1.000 17.14000 ? 120 THR B CB  1 
ATOM   987  O OG1 . THR A 1 120 ? 3.92700   11.45700  34.73800  1.000 20.70000 ? 120 THR B OG1 1 
ATOM   988  C CG2 . THR A 1 120 ? 1.89900   11.81000  33.47300  1.000 19.09000 ? 120 THR B CG2 1 
ATOM   989  N N   . CYS A 1 121 ? 5.74700   13.82500  32.31500  1.000 16.55000 ? 121 CYS B N   1 
ATOM   990  C CA  . CYS A 1 121 ? 6.98300   14.51700  32.66600  1.000 16.41000 ? 121 CYS B CA  1 
ATOM   991  C C   . CYS A 1 121 ? 6.67500   16.00100  32.67100  1.000 19.94000 ? 121 CYS B C   1 
ATOM   992  O O   . CYS A 1 121 ? 6.22800   16.53600  31.65200  1.000 21.07000 ? 121 CYS B O   1 
ATOM   993  C CB  . CYS A 1 121 ? 8.07500   14.19800  31.66400  1.000 15.01000 ? 121 CYS B CB  1 
ATOM   994  S SG  . CYS A 1 121 ? 9.63300   15.04100  32.06100  1.000 24.21000 ? 121 CYS B SG  1 
ATOM   995  N N   . GLY A 1 122 ? 6.91500   16.66100  33.79800  1.000 22.56000 ? 122 GLY B N   1 
ATOM   996  C CA  . GLY A 1 122 ? 6.61800   18.08100  33.86700  1.000 27.12000 ? 122 GLY B CA  1 
ATOM   997  C C   . GLY A 1 122 ? 5.13600   18.30400  33.66100  1.000 23.25000 ? 122 GLY B C   1 
ATOM   998  O O   . GLY A 1 122 ? 4.29700   17.68000  34.32100  1.000 30.45000 ? 122 GLY B O   1 
ATOM   999  N N   . ASP A 1 123 ? 4.79500   19.18300  32.72100  1.000 25.74000 ? 123 ASP B N   1 
ATOM   1000 C CA  . ASP A 1 123 ? 3.39900   19.45100  32.40600  1.000 29.73000 ? 123 ASP B CA  1 
ATOM   1001 C C   . ASP A 1 123 ? 2.91700   18.71600  31.15800  1.000 30.95000 ? 123 ASP B C   1 
ATOM   1002 O O   . ASP A 1 123 ? 1.83500   19.03000  30.64900  1.000 32.75000 ? 123 ASP B O   1 
ATOM   1003 C CB  . ASP A 1 123 ? 3.15900   20.96200  32.25800  1.000 34.24000 ? 123 ASP B CB  1 
ATOM   1004 C CG  . ASP A 1 123 ? 3.96000   21.59300  31.11900  1.000 41.38000 ? 123 ASP B CG  1 
ATOM   1005 O OD1 . ASP A 1 123 ? 4.70900   20.88200  30.41000  1.000 37.89000 ? 123 ASP B OD1 1 
ATOM   1006 O OD2 . ASP A 1 123 ? 3.83900   22.82500  30.93300  1.000 53.09000 ? 123 ASP B OD2 1 
ATOM   1007 N N   . GLN A 1 124 ? 3.67300   17.73100  30.66700  1.000 24.94000 ? 124 GLN B N   1 
ATOM   1008 C CA  . GLN A 1 124 ? 3.31500   17.00700  29.45200  1.000 21.63000 ? 124 GLN B CA  1 
ATOM   1009 C C   . GLN A 1 124 ? 2.82700   15.60500  29.78700  1.000 23.59000 ? 124 GLN B C   1 
ATOM   1010 O O   . GLN A 1 124 ? 3.40800   14.92000  30.63700  1.000 19.91000 ? 124 GLN B O   1 
ATOM   1011 C CB  . GLN A 1 124 ? 4.51200   16.90500  28.49700  1.000 23.20000 ? 124 GLN B CB  1 
ATOM   1012 C CG  . GLN A 1 124 ? 4.98700   18.24100  27.96600  1.000 26.91000 ? 124 GLN B CG  1 
ATOM   1013 C CD  . GLN A 1 124 ? 3.93900   18.93300  27.13900  1.000 26.30000 ? 124 GLN B CD  1 
ATOM   1014 O OE1 . GLN A 1 124 ? 3.35300   18.33800  26.23800  1.000 26.59000 ? 124 GLN B OE1 1 
ATOM   1015 N NE2 . GLN A 1 124 ? 3.68900   20.20000  27.44300  1.000 33.50000 ? 124 GLN B NE2 1 
ATOM   1016 N N   . VAL A 1 125 ? 1.77700   15.16800  29.09600  1.000 17.57000 ? 125 VAL B N   1 
ATOM   1017 C CA  . VAL A 1 125 ? 1.26800   13.80900  29.22300  1.000 17.17000 ? 125 VAL B CA  1 
ATOM   1018 C C   . VAL A 1 125 ? 1.20900   13.19200  27.83100  1.000 17.81000 ? 125 VAL B C   1 
ATOM   1019 O O   . VAL A 1 125 ? 0.65300   13.79100  26.90500  1.000 19.26000 ? 125 VAL B O   1 
ATOM   1020 C CB  . VAL A 1 125 ? -0.12400  13.78300  29.88600  1.000 22.11000 ? 125 VAL B CB  1 
ATOM   1021 C CG1 . VAL A 1 125 ? -0.64100  12.35600  30.01700  1.000 22.46000 ? 125 VAL B CG1 1 
ATOM   1022 C CG2 . VAL A 1 125 ? -0.07000  14.47700  31.24400  1.000 28.17000 ? 125 VAL B CG2 1 
ATOM   1023 N N   . CYS A 1 126 ? 1.79900   12.01000  27.67800  1.000 15.14000 ? 126 CYS B N   1 
ATOM   1024 C CA  . CYS A 1 126 ? 1.66600   11.21500  26.46900  1.000 15.53000 ? 126 CYS B CA  1 
ATOM   1025 C C   . CYS A 1 126 ? 0.72700   10.06100  26.78900  1.000 16.62000 ? 126 CYS B C   1 
ATOM   1026 O O   . CYS A 1 126 ? 0.87200   9.41300   27.83000  1.000 17.13000 ? 126 CYS B O   1 
ATOM   1027 C CB  . CYS A 1 126 ? 3.02900   10.70900  25.99400  1.000 16.46000 ? 126 CYS B CB  1 
ATOM   1028 S SG  . CYS A 1 126 ? 2.93100   9.40400   24.76900  1.000 18.59000 ? 126 CYS B SG  1 
ATOM   1029 N N   . ARG A 1 127 ? -0.27700  9.84300   25.94400  1.000 15.06000 ? 127 ARG B N   1 
ATOM   1030 C CA  . ARG A 1 127 ? -1.25200  8.79500   26.18700  1.000 15.33000 ? 127 ARG B CA  1 
ATOM   1031 C C   . ARG A 1 127 ? -1.15800  7.77000   25.07200  1.000 17.43000 ? 127 ARG B C   1 
ATOM   1032 O O   . ARG A 1 127 ? -1.22300  8.12700   23.88800  1.000 19.57000 ? 127 ARG B O   1 
ATOM   1033 C CB  . ARG A 1 127 ? -2.66800  9.37200   26.28400  1.000 16.21000 ? 127 ARG B CB  1 
ATOM   1034 C CG  . ARG A 1 127 ? -2.78000  10.48300  27.32200  1.000 23.68000 ? 127 ARG B CG  1 
ATOM   1035 C CD  . ARG A 1 127 ? -4.18800  11.02500  27.44700  1.000 33.60000 ? 127 ARG B CD  1 
ATOM   1036 N NE  . ARG A 1 127 ? -4.28300  11.90300  28.61300  1.000 37.37000 ? 127 ARG B NE  1 
ATOM   1037 C CZ  . ARG A 1 127 ? -4.16000  13.22700  28.55700  1.000 36.40000 ? 127 ARG B CZ  1 
ATOM   1038 N NH1 . ARG A 1 127 ? -3.93600  13.82500  27.39500  1.000 44.51000 ? 127 ARG B NH1 1 
ATOM   1039 N NH2 . ARG A 1 127 ? -4.25400  13.95400  29.66300  1.000 51.05000 ? 127 ARG B NH2 1 
ATOM   1040 N N   . GLN A 1 128 ? -0.97300  6.51200   25.45000  1.000 14.93000 ? 128 GLN B N   1 
ATOM   1041 C CA  . GLN A 1 128 ? -0.77300  5.43900   24.48700  1.000 16.48000 ? 128 GLN B CA  1 
ATOM   1042 C C   . GLN A 1 128 ? -1.78500  4.34000   24.75900  1.000 17.59000 ? 128 GLN B C   1 
ATOM   1043 O O   . GLN A 1 128 ? -2.20800  4.12500   25.89800  1.000 16.29000 ? 128 GLN B O   1 
ATOM   1044 C CB  . GLN A 1 128 ? 0.65500   4.87500   24.55600  1.000 15.23000 ? 128 GLN B CB  1 
ATOM   1045 C CG  . GLN A 1 128 ? 1.73100   5.91200   24.23400  1.000 18.21000 ? 128 GLN B CG  1 
ATOM   1046 C CD  . GLN A 1 128 ? 3.14000   5.36200   24.26700  1.000 20.24000 ? 128 GLN B CD  1 
ATOM   1047 O OE1 . GLN A 1 128 ? 3.39300   4.29300   24.80800  1.000 19.48000 ? 128 GLN B OE1 1 
ATOM   1048 N NE2 . GLN A 1 128 ? 4.07500   6.11000   23.69500  1.000 22.75000 ? 128 GLN B NE2 1 
ATOM   1049 N N   . VAL A 1 129 ? -2.20000  3.65700   23.69900  1.000 17.02000 ? 129 VAL B N   1 
ATOM   1050 C CA  . VAL A 1 129 ? -3.08800  2.51200   23.83500  1.000 15.32000 ? 129 VAL B CA  1 
ATOM   1051 C C   . VAL A 1 129 ? -2.46900  1.34700   23.08100  1.000 18.26000 ? 129 VAL B C   1 
ATOM   1052 O O   . VAL A 1 129 ? -2.01800  1.51300   21.94200  1.000 18.08000 ? 129 VAL B O   1 
ATOM   1053 C CB  . VAL A 1 129 ? -4.50200  2.81100   23.30600  1.000 15.15000 ? 129 VAL B CB  1 
ATOM   1054 C CG1 . VAL A 1 129 ? -5.41000  1.60800   23.57800  1.000 19.61000 ? 129 VAL B CG1 1 
ATOM   1055 C CG2 . VAL A 1 129 ? -5.05700  4.07200   23.96000  1.000 18.28000 ? 129 VAL B CG2 1 
ATOM   1056 N N   . PHE A 1 130 ? -2.43800  0.18100   23.71700  1.000 15.53000 ? 130 PHE B N   1 
ATOM   1057 C CA  . PHE A 1 130 ? -1.90100  -1.04200  23.13900  1.000 17.46000 ? 130 PHE B CA  1 
ATOM   1058 C C   . PHE A 1 130 ? -2.98900  -2.10900  23.10400  1.000 19.76000 ? 130 PHE B C   1 
ATOM   1059 O O   . PHE A 1 130 ? -3.89500  -2.12500  23.94200  1.000 20.59000 ? 130 PHE B O   1 
ATOM   1060 C CB  . PHE A 1 130 ? -0.71000  -1.59000  23.93700  1.000 17.53000 ? 130 PHE B CB  1 
ATOM   1061 C CG  . PHE A 1 130 ? 0.47500   -0.66000  23.99800  1.000 16.05000 ? 130 PHE B CG  1 
ATOM   1062 C CD1 . PHE A 1 130 ? 0.49000   0.41100   24.88400  1.000 18.71000 ? 130 PHE B CD1 1 
ATOM   1063 C CD2 . PHE A 1 130 ? 1.58000   -0.86900  23.19200  1.000 18.92000 ? 130 PHE B CD2 1 
ATOM   1064 C CE1 . PHE A 1 130 ? 1.57700   1.25500   24.94300  1.000 20.86000 ? 130 PHE B CE1 1 
ATOM   1065 C CE2 . PHE A 1 130 ? 2.67900   -0.02900  23.25800  1.000 23.41000 ? 130 PHE B CE2 1 
ATOM   1066 C CZ  . PHE A 1 130 ? 2.68100   1.03100   24.13800  1.000 18.63000 ? 130 PHE B CZ  1 
ATOM   1067 N N   . LYS A 1 131 ? -2.90100  -2.99200  22.11400  1.000 20.96000 ? 131 LYS B N   1 
ATOM   1068 C CA  . LYS A 1 131 ? -3.76100  -4.16100  22.02400  1.000 20.39000 ? 131 LYS B CA  1 
ATOM   1069 C C   . LYS A 1 131 ? -2.90000  -5.40200  22.20500  1.000 18.52000 ? 131 LYS B C   1 
ATOM   1070 O O   . LYS A 1 131 ? -1.78000  -5.46100  21.69800  1.000 19.77000 ? 131 LYS B O   1 
ATOM   1071 C CB  . LYS A 1 131 ? -4.47900  -4.20500  20.67100  1.000 23.82000 ? 131 LYS B CB  1 
ATOM   1072 C CG  . LYS A 1 131 ? -5.16900  -5.52400  20.36000  1.000 36.47000 ? 131 LYS B CG  1 
ATOM   1073 C CD  . LYS A 1 131 ? -6.12300  -5.35300  19.19100  1.000 41.43000 ? 131 LYS B CD  1 
ATOM   1074 C CE  . LYS A 1 131 ? -7.57100  -5.45000  19.62600  1.000 50.39000 ? 131 LYS B CE  1 
ATOM   1075 N NZ  . LYS A 1 131 ? -7.87600  -6.77000  20.24200  1.000 50.12000 ? 131 LYS B NZ  1 
ATOM   1076 N N   . LYS A 1 132 ? -3.40000  -6.38100  22.95200  1.000 19.64000 ? 132 LYS B N   1 
ATOM   1077 C CA  . LYS A 1 132 ? -2.62800  -7.59800  23.17000  1.000 18.85000 ? 132 LYS B CA  1 
ATOM   1078 C C   . LYS A 1 132 ? -2.53400  -8.39000  21.87000  1.000 21.42000 ? 132 LYS B C   1 
ATOM   1079 O O   . LYS A 1 132 ? -3.54500  -8.60400  21.19300  1.000 25.28000 ? 132 LYS B O   1 
ATOM   1080 C CB  . LYS A 1 132 ? -3.27000  -8.45300  24.26600  1.000 25.80000 ? 132 LYS B CB  1 
ATOM   1081 C CG  . LYS A 1 132 ? -2.34600  -9.52400  24.83500  1.000 26.38000 ? 132 LYS B CG  1 
ATOM   1082 C CD  . LYS A 1 132 ? -2.95600  -10.21300 26.05400  1.000 25.35000 ? 132 LYS B CD  1 
ATOM   1083 C CE  . LYS A 1 132 ? -2.04400  -11.32400 26.56400  1.000 31.18000 ? 132 LYS B CE  1 
ATOM   1084 N NZ  . LYS A 1 132 ? -2.63900  -12.04600 27.73500  1.000 30.12000 ? 132 LYS B NZ  1 
ATOM   1085 N N   . LYS A 1 133 ? -1.32500  -8.82400  21.53000  1.000 23.85000 ? 133 LYS B N   1 
ATOM   1086 C CA  . LYS A 1 133 ? -1.10000  -9.58000  20.29800  1.000 28.91000 ? 133 LYS B CA  1 
ATOM   1087 C C   . LYS A 1 133 ? -1.59800  -11.01500 20.44900  1.000 40.40000 ? 133 LYS B C   1 
ATOM   1088 O O   . LYS A 1 133 ? -1.29100  -11.68600 21.44000  1.000 33.78000 ? 133 LYS B O   1 
ATOM   1089 C CB  . LYS A 1 133 ? 0.38100   -9.56500  19.92600  1.000 29.20000 ? 133 LYS B CB  1 
ATOM   1090 C CG  . LYS A 1 133 ? 0.72600   -10.43000 18.72500  1.000 42.36000 ? 133 LYS B CG  1 
ATOM   1091 C CD  . LYS A 1 133 ? 1.77700   -9.76100  17.85700  1.000 50.44000 ? 133 LYS B CD  1 
ATOM   1092 C CE  . LYS A 1 133 ? 3.15900   -10.35100 18.10100  1.000 50.19000 ? 133 LYS B CE  1 
ATOM   1093 N NZ  . LYS A 1 133 ? 4.23900   -9.33400  17.94800  1.000 44.89000 ? 133 LYS B NZ  1 
ATOM   1094 N N   . THR B 1 1   ? 14.34200  -9.03100  -7.18000  1.000 49.98000 ? 1   THR A N   1 
ATOM   1095 C CA  . THR B 1 1   ? 13.49900  -9.16200  -5.99700  1.000 40.19000 ? 1   THR A CA  1 
ATOM   1096 C C   . THR B 1 1   ? 12.03500  -8.89600  -6.33100  1.000 40.42000 ? 1   THR A C   1 
ATOM   1097 O O   . THR B 1 1   ? 11.40600  -8.01500  -5.74600  1.000 41.14000 ? 1   THR A O   1 
ATOM   1098 C CB  . THR B 1 1   ? 13.94300  -8.20000  -4.87900  1.000 37.00000 ? 1   THR A CB  1 
ATOM   1099 O OG1 . THR B 1 1   ? 13.24400  -6.95600  -5.01000  1.000 48.00000 ? 1   THR A OG1 1 
ATOM   1100 C CG2 . THR B 1 1   ? 15.44000  -7.94600  -4.95800  1.000 39.39000 ? 1   THR A CG2 1 
ATOM   1101 N N   . ARG B 1 2   ? 11.49900  -9.66400  -7.27400  1.000 37.61000 ? 2   ARG A N   1 
ATOM   1102 C CA  . ARG B 1 2   ? 10.13300  -9.51400  -7.67800  1.000 35.89000 ? 2   ARG A CA  1 
ATOM   1103 C C   . ARG B 1 2   ? 9.18200   -10.37700 -6.81700  1.000 40.77000 ? 2   ARG A C   1 
ATOM   1104 O O   . ARG B 1 2   ? 8.01200   -10.39700 -7.03300  1.000 40.44000 ? 2   ARG A O   1 
ATOM   1105 C CB  . ARG B 1 2   ? 9.99700   -9.84900  -9.15900  1.000 38.96000 ? 2   ARG A CB  1 
ATOM   1106 C CG  . ARG B 1 2   ? 10.52300  -8.81500  -10.13900 1.000 39.42000 ? 2   ARG A CG  1 
ATOM   1107 C CD  . ARG B 1 2   ? 9.86200   -8.89700  -11.52000 1.000 33.24000 ? 2   ARG A CD  1 
ATOM   1108 N NE  . ARG B 1 2   ? 10.30500  -7.82100  -12.39400 1.000 33.39000 ? 2   ARG A NE  1 
ATOM   1109 C CZ  . ARG B 1 2   ? 10.23500  -7.82100  -13.71100 1.000 34.15000 ? 2   ARG A CZ  1 
ATOM   1110 N NH1 . ARG B 1 2   ? 9.73700   -8.87500  -14.31400 1.000 36.29000 ? 2   ARG A NH1 1 
ATOM   1111 N NH2 . ARG B 1 2   ? 10.69000  -6.79200  -14.40700 1.000 32.13000 ? 2   ARG A NH2 1 
ATOM   1112 N N   . ASP B 1 3   ? 9.68100   -11.06800 -5.82300  1.000 38.65000 ? 3   ASP A N   1 
ATOM   1113 C CA  . ASP B 1 3   ? 8.79900   -11.88000 -4.99900  1.000 37.50000 ? 3   ASP A CA  1 
ATOM   1114 C C   . ASP B 1 3   ? 8.33000   -11.28600 -3.68800  1.000 35.12000 ? 3   ASP A C   1 
ATOM   1115 O O   . ASP B 1 3   ? 9.03000   -11.28800 -2.71700  1.000 35.59000 ? 3   ASP A O   1 
ATOM   1116 C CB  . ASP B 1 3   ? 9.42800   -13.21600 -4.74300  1.000 40.65000 ? 3   ASP A CB  1 
ATOM   1117 C CG  . ASP B 1 3   ? 8.42000   -14.22500 -4.44800  1.000 47.02000 ? 3   ASP A CG  1 
ATOM   1118 O OD1 . ASP B 1 3   ? 7.49500   -13.89300 -3.70800  1.000 40.35000 ? 3   ASP A OD1 1 
ATOM   1119 O OD2 . ASP B 1 3   ? 8.56700   -15.34600 -4.98100  1.000 50.63000 ? 3   ASP A OD2 1 
ATOM   1120 N N   . ALA B 1 4   ? 7.11100   -10.76400 -3.69300  1.000 28.89000 ? 4   ALA A N   1 
ATOM   1121 C CA  . ALA B 1 4   ? 6.54900   -10.08600 -2.53600  1.000 26.96000 ? 4   ALA A CA  1 
ATOM   1122 C C   . ALA B 1 4   ? 5.74500   -10.97200 -1.62000  1.000 26.53000 ? 4   ALA A C   1 
ATOM   1123 O O   . ALA B 1 4   ? 5.13700   -10.49900 -0.68800  1.000 24.86000 ? 4   ALA A O   1 
ATOM   1124 C CB  . ALA B 1 4   ? 5.68800   -8.92300  -2.99500  1.000 27.59000 ? 4   ALA A CB  1 
ATOM   1125 N N   . ASN B 1 5   ? 5.75100   -12.27200 -1.87500  1.000 25.75000 ? 5   ASN A N   1 
ATOM   1126 C CA  . ASN B 1 5   ? 5.00100   -13.18800 -1.04100  1.000 25.53000 ? 5   ASN A CA  1 
ATOM   1127 C C   . ASN B 1 5   ? 5.38200   -13.10400 0.42500   1.000 27.96000 ? 5   ASN A C   1 
ATOM   1128 O O   . ASN B 1 5   ? 6.54700   -12.96800 0.76200   1.000 28.81000 ? 5   ASN A O   1 
ATOM   1129 C CB  . ASN B 1 5   ? 5.24200   -14.62900 -1.48400  1.000 27.64000 ? 5   ASN A CB  1 
ATOM   1130 C CG  . ASN B 1 5   ? 4.32600   -15.06400 -2.59900  1.000 23.77000 ? 5   ASN A CG  1 
ATOM   1131 O OD1 . ASN B 1 5   ? 3.13500   -15.22100 -2.40600  1.000 27.70000 ? 5   ASN A OD1 1 
ATOM   1132 N ND2 . ASN B 1 5   ? 4.89100   -15.28600 -3.76600  1.000 30.93000 ? 5   ASN A ND2 1 
ATOM   1133 N N   . GLY B 1 6   ? 4.38900   -13.21500 1.29300   1.000 30.69000 ? 6   GLY A N   1 
ATOM   1134 C CA  . GLY B 1 6   ? 4.64400   -13.23000 2.71700   1.000 36.47000 ? 6   GLY A CA  1 
ATOM   1135 C C   . GLY B 1 6   ? 3.74700   -12.40200 3.60200   1.000 29.56000 ? 6   GLY A C   1 
ATOM   1136 O O   . GLY B 1 6   ? 2.83000   -11.74700 3.13800   1.000 26.99000 ? 6   GLY A O   1 
ATOM   1137 N N   . THR B 1 7   ? 4.01500   -12.48400 4.89700   1.000 26.72000 ? 7   THR A N   1 
ATOM   1138 C CA  . THR B 1 7   ? 3.31500   -11.72100 5.90300   1.000 24.63000 ? 7   THR A CA  1 
ATOM   1139 C C   . THR B 1 7   ? 4.34500   -10.67700 6.29500   1.000 24.16000 ? 7   THR A C   1 
ATOM   1140 O O   . THR B 1 7   ? 5.46400   -11.00800 6.64300   1.000 25.29000 ? 7   THR A O   1 
ATOM   1141 C CB  . THR B 1 7   ? 2.91000   -12.58500 7.09100   1.000 35.48000 ? 7   THR A CB  1 
ATOM   1142 O OG1 . THR B 1 7   ? 2.02900   -13.61800 6.63200   1.000 32.28000 ? 7   THR A OG1 1 
ATOM   1143 C CG2 . THR B 1 7   ? 2.22000   -11.74300 8.13700   1.000 31.00000 ? 7   THR A CG2 1 
ATOM   1144 N N   . TRP B 1 8   ? 3.95000   -9.41600  6.25400   1.000 17.02000 ? 8   TRP A N   1 
ATOM   1145 C CA  . TRP B 1 8   ? 4.89200   -8.31800  6.44500   1.000 20.95000 ? 8   TRP A CA  1 
ATOM   1146 C C   . TRP B 1 8   ? 4.43700   -7.45800  7.61500   1.000 20.24000 ? 8   TRP A C   1 
ATOM   1147 O O   . TRP B 1 8   ? 3.29800   -6.97900  7.62900   1.000 24.29000 ? 8   TRP A O   1 
ATOM   1148 C CB  . TRP B 1 8   ? 5.00700   -7.49000  5.16300   1.000 20.88000 ? 8   TRP A CB  1 
ATOM   1149 C CG  . TRP B 1 8   ? 5.50000   -8.26100  3.98900   1.000 18.02000 ? 8   TRP A CG  1 
ATOM   1150 C CD1 . TRP B 1 8   ? 4.74200   -8.94600  3.07200   1.000 22.28000 ? 8   TRP A CD1 1 
ATOM   1151 C CD2 . TRP B 1 8   ? 6.86100   -8.39800  3.56100   1.000 15.60000 ? 8   TRP A CD2 1 
ATOM   1152 N NE1 . TRP B 1 8   ? 5.55400   -9.50800  2.11800   1.000 21.69000 ? 8   TRP A NE1 1 
ATOM   1153 C CE2 . TRP B 1 8   ? 6.86000   -9.20100  2.40300   1.000 20.02000 ? 8   TRP A CE2 1 
ATOM   1154 C CE3 . TRP B 1 8   ? 8.09200   -7.95400  4.07600   1.000 18.21000 ? 8   TRP A CE3 1 
ATOM   1155 C CZ2 . TRP B 1 8   ? 8.03100   -9.53000  1.72100   1.000 19.88000 ? 8   TRP A CZ2 1 
ATOM   1156 C CZ3 . TRP B 1 8   ? 9.24900   -8.28700  3.40600   1.000 20.18000 ? 8   TRP A CZ3 1 
ATOM   1157 C CH2 . TRP B 1 8   ? 9.21500   -9.06800  2.23700   1.000 20.04000 ? 8   TRP A CH2 1 
ATOM   1158 N N   . GLU B 1 9   ? 5.32500   -7.26900  8.59400   1.000 17.20000 ? 9   GLU A N   1 
ATOM   1159 C CA  . GLU B 1 9   ? 5.00200   -6.54000  9.81700   1.000 18.73000 ? 9   GLU A CA  1 
ATOM   1160 C C   . GLU B 1 9   ? 5.61200   -5.14100  9.78500   1.000 18.42000 ? 9   GLU A C   1 
ATOM   1161 O O   . GLU B 1 9   ? 6.81700   -4.98000  9.55400   1.000 18.05000 ? 9   GLU A O   1 
ATOM   1162 C CB  . GLU B 1 9   ? 5.51100   -7.29900  11.04700  1.000 22.95000 ? 9   GLU A CB  1 
ATOM   1163 C CG  . GLU B 1 9   ? 4.65100   -8.48800  11.44400  1.000 40.85000 ? 9   GLU A CG  1 
ATOM   1164 C CD  . GLU B 1 9   ? 4.97100   -8.97900  12.84500  1.000 57.90000 ? 9   GLU A CD  1 
ATOM   1165 O OE1 . GLU B 1 9   ? 4.13500   -8.77900  13.75300  1.000 64.18000 ? 9   GLU A OE1 1 
ATOM   1166 O OE2 . GLU B 1 9   ? 6.06000   -9.56200  13.03700  1.000 60.69000 ? 9   GLU A OE2 1 
ATOM   1167 N N   . MET B 1 10  ? 4.78600   -4.13400  10.04300  1.000 19.46000 ? 10  MET A N   1 
ATOM   1168 C CA  . MET B 1 10  ? 5.26100   -2.76400  9.91500   1.000 19.12000 ? 10  MET A CA  1 
ATOM   1169 C C   . MET B 1 10  ? 6.30000   -2.45200  10.97900  1.000 19.63000 ? 10  MET A C   1 
ATOM   1170 O O   . MET B 1 10  ? 6.09700   -2.74000  12.16400  1.000 21.77000 ? 10  MET A O   1 
ATOM   1171 C CB  . MET B 1 10  ? 4.10400   -1.78000  10.02800  1.000 22.55000 ? 10  MET A CB  1 
ATOM   1172 C CG  . MET B 1 10  ? 4.53800   -0.37400  10.38600  1.000 21.46000 ? 10  MET A CG  1 
ATOM   1173 S SD  . MET B 1 10  ? 3.11800   0.73700   10.31500  1.000 26.33000 ? 10  MET A SD  1 
ATOM   1174 C CE  . MET B 1 10  ? 3.05300   0.88100   8.54400   1.000 16.81000 ? 10  MET A CE  1 
ATOM   1175 N N   . GLU B 1 11  ? 7.39800   -1.81900  10.54900  1.000 16.34000 ? 11  GLU A N   1 
ATOM   1176 C CA  . GLU B 1 11  ? 8.48200   -1.37600  11.41800  1.000 17.40000 ? 11  GLU A CA  1 
ATOM   1177 C C   . GLU B 1 11  ? 8.57600   0.13200   11.54400  1.000 21.41000 ? 11  GLU A C   1 
ATOM   1178 O O   . GLU B 1 11  ? 9.02400   0.62900   12.58100  1.000 19.90000 ? 11  GLU A O   1 
ATOM   1179 C CB  . GLU B 1 11  ? 9.83200   -1.87000  10.89000  1.000 22.62000 ? 11  GLU A CB  1 
ATOM   1180 C CG  . GLU B 1 11  ? 10.12300  -3.34200  11.06500  1.000 25.97000 ? 11  GLU A CG  1 
ATOM   1181 C CD  . GLU B 1 11  ? 11.55300  -3.68300  10.67700  1.000 38.74000 ? 11  GLU A CD  1 
ATOM   1182 O OE1 . GLU B 1 11  ? 12.23700  -2.81600  10.08400  1.000 39.12000 ? 11  GLU A OE1 1 
ATOM   1183 O OE2 . GLU B 1 11  ? 11.99700  -4.80900  10.98400  1.000 44.65000 ? 11  GLU A OE2 1 
ATOM   1184 N N   . SER B 1 12  ? 8.20700   0.84200   10.48600  1.000 16.09000 ? 12  SER A N   1 
ATOM   1185 C CA  . SER B 1 12  ? 8.31500   2.29000   10.44100  1.000 17.35000 ? 12  SER A CA  1 
ATOM   1186 C C   . SER B 1 12  ? 7.20500   2.88100   9.58300   1.000 16.53000 ? 12  SER A C   1 
ATOM   1187 O O   . SER B 1 12  ? 6.81600   2.27000   8.61300   1.000 15.48000 ? 12  SER A O   1 
ATOM   1188 C CB  . SER B 1 12  ? 9.66200   2.65000   9.81700   1.000 19.66000 ? 12  SER A CB  1 
ATOM   1189 O OG  . SER B 1 12  ? 9.90300   4.02800   9.91700   1.000 25.93000 ? 12  SER A OG  1 
ATOM   1190 N N   . ASN B 1 13  ? 6.73800   4.08600   9.92300   1.000 15.13000 ? 13  ASN A N   1 
ATOM   1191 C CA  . ASN B 1 13  ? 5.65400   4.71700   9.17600   1.000 16.15000 ? 13  ASN A CA  1 
ATOM   1192 C C   . ASN B 1 13  ? 5.91200   6.21300   9.25700   1.000 18.44000 ? 13  ASN A C   1 
ATOM   1193 O O   . ASN B 1 13  ? 5.86500   6.79000   10.34600  1.000 24.49000 ? 13  ASN A O   1 
ATOM   1194 C CB  . ASN B 1 13  ? 4.30100   4.34200   9.77200   1.000 16.75000 ? 13  ASN A CB  1 
ATOM   1195 C CG  . ASN B 1 13  ? 3.12800   4.70800   8.88400   1.000 17.76000 ? 13  ASN A CG  1 
ATOM   1196 O OD1 . ASN B 1 13  ? 3.29100   5.21900   7.77400   1.000 17.27000 ? 13  ASN A OD1 1 
ATOM   1197 N ND2 . ASN B 1 13  ? 1.92600   4.45400   9.38300   1.000 21.84000 ? 13  ASN A ND2 1 
ATOM   1198 N N   . GLU B 1 14  ? 6.20100   6.83600   8.12300   1.000 16.74000 ? 14  GLU A N   1 
ATOM   1199 C CA  . GLU B 1 14  ? 6.60300   8.23900   8.08200   1.000 17.83000 ? 14  GLU A CA  1 
ATOM   1200 C C   . GLU B 1 14  ? 5.60200   9.03800   7.25100   1.000 22.16000 ? 14  GLU A C   1 
ATOM   1201 O O   . GLU B 1 14  ? 5.33500   8.69200   6.09600   1.000 16.53000 ? 14  GLU A O   1 
ATOM   1202 C CB  . GLU B 1 14  ? 8.00300   8.37700   7.48900   1.000 19.94000 ? 14  GLU A CB  1 
ATOM   1203 C CG  . GLU B 1 14  ? 8.44100   9.82000   7.33100   1.000 25.40000 ? 14  GLU A CG  1 
ATOM   1204 C CD  . GLU B 1 14  ? 9.77200   9.97000   6.61400   1.000 38.38000 ? 14  GLU A CD  1 
ATOM   1205 O OE1 . GLU B 1 14  ? 10.39900  8.94200   6.27200   1.000 37.17000 ? 14  GLU A OE1 1 
ATOM   1206 O OE2 . GLU B 1 14  ? 10.18600  11.12700  6.38200   1.000 42.34000 ? 14  GLU A OE2 1 
ATOM   1207 N N   . ASN B 1 15  ? 5.06500   10.11300  7.83400   1.000 16.45000 ? 15  ASN A N   1 
ATOM   1208 C CA  . ASN B 1 15  ? 4.13600   11.03400  7.16500   1.000 17.07000 ? 15  ASN A CA  1 
ATOM   1209 C C   . ASN B 1 15  ? 2.82800   10.35800  6.76300   1.000 19.55000 ? 15  ASN A C   1 
ATOM   1210 O O   . ASN B 1 15  ? 2.21900   10.72600  5.75700   1.000 19.15000 ? 15  ASN A O   1 
ATOM   1211 C CB  . ASN B 1 15  ? 4.77100   11.70900  5.94700   1.000 18.45000 ? 15  ASN A CB  1 
ATOM   1212 C CG  . ASN B 1 15  ? 3.95700   12.88700  5.45100   1.000 25.43000 ? 15  ASN A CG  1 
ATOM   1213 O OD1 . ASN B 1 15  ? 3.30800   13.58000  6.24200   1.000 24.17000 ? 15  ASN A OD1 1 
ATOM   1214 N ND2 . ASN B 1 15  ? 3.96300   13.10700  4.13600   1.000 20.88000 ? 15  ASN A ND2 1 
ATOM   1215 N N   . PHE B 1 16  ? 2.36600   9.41900   7.57300   1.000 21.27000 ? 16  PHE A N   1 
ATOM   1216 C CA  . PHE B 1 16  ? 1.10300   8.75100   7.30500   1.000 18.61000 ? 16  PHE A CA  1 
ATOM   1217 C C   . PHE B 1 16  ? -0.01500  9.78500   7.37800   1.000 20.25000 ? 16  PHE A C   1 
ATOM   1218 O O   . PHE B 1 16  ? -0.91700  9.79700   6.57000   1.000 19.44000 ? 16  PHE A O   1 
ATOM   1219 C CB  . PHE B 1 16  ? 0.86700   7.64700   8.32900   1.000 19.04000 ? 16  PHE A CB  1 
ATOM   1220 C CG  . PHE B 1 16  ? -0.20400  6.66900   7.94200   1.000 23.94000 ? 16  PHE A CG  1 
ATOM   1221 C CD1 . PHE B 1 16  ? -0.34100  6.24400   6.63700   1.000 24.63000 ? 16  PHE A CD1 1 
ATOM   1222 C CD2 . PHE B 1 16  ? -1.05900  6.16100   8.89500   1.000 32.27000 ? 16  PHE A CD2 1 
ATOM   1223 C CE1 . PHE B 1 16  ? -1.31900  5.34100   6.28600   1.000 26.09000 ? 16  PHE A CE1 1 
ATOM   1224 C CE2 . PHE B 1 16  ? -2.03700  5.25300   8.55400   1.000 31.07000 ? 16  PHE A CE2 1 
ATOM   1225 C CZ  . PHE B 1 16  ? -2.17100  4.84700   7.24500   1.000 32.96000 ? 16  PHE A CZ  1 
ATOM   1226 N N   . GLU B 1 17  ? 0.07400   10.66500  8.36500   1.000 23.35000 ? 17  GLU A N   1 
ATOM   1227 C CA  . GLU B 1 17  ? -0.92000  11.71000  8.55100   1.000 24.67000 ? 17  GLU A CA  1 
ATOM   1228 C C   . GLU B 1 17  ? -1.01200  12.64900  7.36100   1.000 23.01000 ? 17  GLU A C   1 
ATOM   1229 O O   . GLU B 1 17  ? -2.09500  12.98900  6.91100   1.000 23.43000 ? 17  GLU A O   1 
ATOM   1230 C CB  . GLU B 1 17  ? -0.59600  12.52400  9.80000   1.000 28.77000 ? 17  GLU A CB  1 
ATOM   1231 C CG  . GLU B 1 17  ? -1.28100  13.87200  9.82700   1.000 35.09000 ? 17  GLU A CG  1 
ATOM   1232 C CD  . GLU B 1 17  ? -2.72500  13.76100  10.25900  1.000 44.52000 ? 17  GLU A CD  1 
ATOM   1233 O OE1 . GLU B 1 17  ? -3.16200  12.63500  10.58700  1.000 47.82000 ? 17  GLU A OE1 1 
ATOM   1234 O OE2 . GLU B 1 17  ? -3.41800  14.79500  10.27300  1.000 44.22000 ? 17  GLU A OE2 1 
ATOM   1235 N N   . GLY B 1 18  ? 0.13100   13.09400  6.86800   1.000 22.99000 ? 18  GLY A N   1 
ATOM   1236 C CA  . GLY B 1 18  ? 0.13700   13.99200  5.72500   1.000 21.50000 ? 18  GLY A CA  1 
ATOM   1237 C C   . GLY B 1 18  ? -0.49000  13.37000  4.49200   1.000 21.73000 ? 18  GLY A C   1 
ATOM   1238 O O   . GLY B 1 18  ? -1.26000  14.01700  3.77500   1.000 21.70000 ? 18  GLY A O   1 
ATOM   1239 N N   . TRP B 1 19  ? -0.17500  12.09600  4.23500   1.000 19.91000 ? 19  TRP A N   1 
ATOM   1240 C CA  . TRP B 1 19  ? -0.76700  11.38300  3.10800   1.000 17.84000 ? 19  TRP A CA  1 
ATOM   1241 C C   . TRP B 1 19  ? -2.28500  11.23100  3.26800   1.000 18.58000 ? 19  TRP A C   1 
ATOM   1242 O O   . TRP B 1 19  ? -3.04700  11.47800  2.32400   1.000 20.90000 ? 19  TRP A O   1 
ATOM   1243 C CB  . TRP B 1 19  ? -0.06400  10.02400  2.97100   1.000 16.54000 ? 19  TRP A CB  1 
ATOM   1244 C CG  . TRP B 1 19  ? -0.66700  9.11300   1.95600   1.000 14.25000 ? 19  TRP A CG  1 
ATOM   1245 C CD1 . TRP B 1 19  ? -0.49700  9.16700   0.60900   1.000 16.58000 ? 19  TRP A CD1 1 
ATOM   1246 C CD2 . TRP B 1 19  ? -1.51300  7.98400   2.21100   1.000 16.62000 ? 19  TRP A CD2 1 
ATOM   1247 N NE1 . TRP B 1 19  ? -1.20000  8.16400   0.00500   1.000 17.25000 ? 19  TRP A NE1 1 
ATOM   1248 C CE2 . TRP B 1 19  ? -1.83300  7.41800   0.96300   1.000 17.72000 ? 19  TRP A CE2 1 
ATOM   1249 C CE3 . TRP B 1 19  ? -2.04700  7.41400   3.37400   1.000 20.22000 ? 19  TRP A CE3 1 
ATOM   1250 C CZ2 . TRP B 1 19  ? -2.65200  6.29700   0.83600   1.000 19.11000 ? 19  TRP A CZ2 1 
ATOM   1251 C CZ3 . TRP B 1 19  ? -2.86300  6.29900   3.25100   1.000 24.24000 ? 19  TRP A CZ3 1 
ATOM   1252 C CH2 . TRP B 1 19  ? -3.16300  5.75500   1.98500   1.000 23.32000 ? 19  TRP A CH2 1 
ATOM   1253 N N   . MET B 1 20  ? -2.74800  10.82100  4.45400   1.000 16.77000 ? 20  MET A N   1 
ATOM   1254 C CA  . MET B 1 20  ? -4.19200  10.70100  4.66900   1.000 17.46000 ? 20  MET A CA  1 
ATOM   1255 C C   . MET B 1 20  ? -4.88500  12.04900  4.51500   1.000 19.88000 ? 20  MET A C   1 
ATOM   1256 O O   . MET B 1 20  ? -5.99100  12.13300  3.95800   1.000 19.92000 ? 20  MET A O   1 
ATOM   1257 C CB  . MET B 1 20  ? -4.47600  10.12000  6.04900   1.000 19.87000 ? 20  MET A CB  1 
ATOM   1258 C CG  . MET B 1 20  ? -4.12400  8.66100   6.18300   1.000 23.93000 ? 20  MET A CG  1 
ATOM   1259 S SD  . MET B 1 20  ? -4.78800  7.95400   7.70900   1.000 24.97000 ? 20  MET A SD  1 
ATOM   1260 C CE  . MET B 1 20  ? -3.68300  8.69200   8.91500   1.000 26.96000 ? 20  MET A CE  1 
ATOM   1261 N N   . LYS B 1 21  ? -4.26400  13.11200  5.02100   1.000 19.94000 ? 21  LYS A N   1 
ATOM   1262 C CA  . LYS B 1 21  ? -4.84400  14.44300  4.87600   1.000 23.37000 ? 21  LYS A CA  1 
ATOM   1263 C C   . LYS B 1 21  ? -4.95000  14.84000  3.40800   1.000 23.12000 ? 21  LYS A C   1 
ATOM   1264 O O   . LYS B 1 21  ? -5.94700  15.44500  2.98800   1.000 23.01000 ? 21  LYS A O   1 
ATOM   1265 C CB  . LYS B 1 21  ? -4.00800  15.45900  5.66600   1.000 22.79000 ? 21  LYS A CB  1 
ATOM   1266 C CG  . LYS B 1 21  ? -4.66300  16.81600  5.81200   1.000 22.38000 ? 21  LYS A CG  1 
ATOM   1267 C CD  . LYS B 1 21  ? -4.21900  17.47900  7.09900   1.000 30.27000 ? 21  LYS A CD  1 
ATOM   1268 C CE  . LYS B 1 21  ? -2.72700  17.70500  7.10800   1.000 38.40000 ? 21  LYS A CE  1 
ATOM   1269 N NZ  . LYS B 1 21  ? -2.36500  18.84300  8.01300   1.000 44.19000 ? 21  LYS A NZ  1 
ATOM   1270 N N   . ALA B 1 22  ? -3.93300  14.49800  2.60700   1.000 19.54000 ? 22  ALA A N   1 
ATOM   1271 C CA  . ALA B 1 22  ? -3.97500  14.78000  1.17500   1.000 20.57000 ? 22  ALA A CA  1 
ATOM   1272 C C   . ALA B 1 22  ? -5.12300  14.05200  0.48500   1.000 25.78000 ? 22  ALA A C   1 
ATOM   1273 O O   . ALA B 1 22  ? -5.67500  14.56100  -0.50000  1.000 25.51000 ? 22  ALA A O   1 
ATOM   1274 C CB  . ALA B 1 22  ? -2.64300  14.40900  0.52100   1.000 25.33000 ? 22  ALA A CB  1 
ATOM   1275 N N   . LEU B 1 23  ? -5.49500  12.86300  0.97600   1.000 19.82000 ? 23  LEU A N   1 
ATOM   1276 C CA  . LEU B 1 23  ? -6.63000  12.12300  0.43300   1.000 20.03000 ? 23  LEU A CA  1 
ATOM   1277 C C   . LEU B 1 23  ? -7.96500  12.64000  0.94900   1.000 22.33000 ? 23  LEU A C   1 
ATOM   1278 O O   . LEU B 1 23  ? -9.00900  12.15400  0.50200   1.000 24.03000 ? 23  LEU A O   1 
ATOM   1279 C CB  . LEU B 1 23  ? -6.51000  10.62600  0.77500   1.000 20.31000 ? 23  LEU A CB  1 
ATOM   1280 C CG  . LEU B 1 23  ? -5.45900  9.82600   0.00200   1.000 20.69000 ? 23  LEU A CG  1 
ATOM   1281 C CD1 . LEU B 1 23  ? -5.26900  8.44600   0.61200   1.000 22.51000 ? 23  LEU A CD1 1 
ATOM   1282 C CD2 . LEU B 1 23  ? -5.88800  9.71400   -1.44800  1.000 26.46000 ? 23  LEU A CD2 1 
ATOM   1283 N N   . ASP B 1 24  ? -7.95100  13.58900  1.88900   1.000 27.07000 ? 24  ASP A N   1 
ATOM   1284 C CA  . ASP B 1 24  ? -9.15700  14.16500  2.48000   1.000 27.93000 ? 24  ASP A CA  1 
ATOM   1285 C C   . ASP B 1 24  ? -9.90400  13.16800  3.36100   1.000 32.85000 ? 24  ASP A C   1 
ATOM   1286 O O   . ASP B 1 24  ? -11.12700 13.24300  3.50300   1.000 33.41000 ? 24  ASP A O   1 
ATOM   1287 C CB  . ASP B 1 24  ? -10.07200 14.73700  1.39200   1.000 28.26000 ? 24  ASP A CB  1 
ATOM   1288 C CG  . ASP B 1 24  ? -9.29600  15.53500  0.35900   1.000 28.65000 ? 24  ASP A CG  1 
ATOM   1289 O OD1 . ASP B 1 24  ? -8.48500  16.40100  0.76000   1.000 33.94000 ? 24  ASP A OD1 1 
ATOM   1290 O OD2 . ASP B 1 24  ? -9.44800  15.28700  -0.85500  1.000 27.77000 ? 24  ASP A OD2 1 
ATOM   1291 N N   . ILE B 1 25  ? -9.17500  12.22300  3.96100   1.000 25.77000 ? 25  ILE A N   1 
ATOM   1292 C CA  . ILE B 1 25  ? -9.76200  11.37200  4.98500   1.000 27.90000 ? 25  ILE A CA  1 
ATOM   1293 C C   . ILE B 1 25  ? -10.26400 12.24100  6.12600   1.000 34.39000 ? 25  ILE A C   1 
ATOM   1294 O O   . ILE B 1 25  ? -9.57200  13.16400  6.57400   1.000 29.76000 ? 25  ILE A O   1 
ATOM   1295 C CB  . ILE B 1 25  ? -8.73400  10.34700  5.48900   1.000 31.27000 ? 25  ILE A CB  1 
ATOM   1296 C CG1 . ILE B 1 25  ? -8.07900  9.60300   4.31900   1.000 31.37000 ? 25  ILE A CG1 1 
ATOM   1297 C CG2 . ILE B 1 25  ? -9.38600  9.39000   6.46900   1.000 27.68000 ? 25  ILE A CG2 1 
ATOM   1298 C CD1 . ILE B 1 25  ? -8.97300  8.64000   3.63700   1.000 34.93000 ? 25  ILE A CD1 1 
ATOM   1299 N N   . ASP B 1 26  ? -11.47600 11.95000  6.60000   1.000 36.89000 ? 26  ASP A N   1 
ATOM   1300 C CA  . ASP B 1 26  ? -12.02800 12.66400  7.74500   1.000 38.87000 ? 26  ASP A CA  1 
ATOM   1301 C C   . ASP B 1 26  ? -11.02300 12.69500  8.88700   1.000 36.23000 ? 26  ASP A C   1 
ATOM   1302 O O   . ASP B 1 26  ? -10.31200 11.71600  9.13100   1.000 38.06000 ? 26  ASP A O   1 
ATOM   1303 C CB  . ASP B 1 26  ? -13.32400 11.99600  8.20600   1.000 42.61000 ? 26  ASP A CB  1 
ATOM   1304 C CG  . ASP B 1 26  ? -14.31700 12.98400  8.78800   1.000 56.64000 ? 26  ASP A CG  1 
ATOM   1305 O OD1 . ASP B 1 26  ? -14.55900 12.92300  10.01300  1.000 56.21000 ? 26  ASP A OD1 1 
ATOM   1306 O OD2 . ASP B 1 26  ? -14.85600 13.81800  8.02600   1.000 64.49000 ? 26  ASP A OD2 1 
ATOM   1307 N N   . PHE B 1 27  ? -10.97600 13.82900  9.59600   1.000 35.56000 ? 27  PHE A N   1 
ATOM   1308 C CA  . PHE B 1 27  ? -10.02000 13.98700  10.69100  1.000 36.77000 ? 27  PHE A CA  1 
ATOM   1309 C C   . PHE B 1 27  ? -10.21300 12.91700  11.75700  1.000 35.51000 ? 27  PHE A C   1 
ATOM   1310 O O   . PHE B 1 27  ? -9.23900  12.43000  12.34400  1.000 35.08000 ? 27  PHE A O   1 
ATOM   1311 C CB  . PHE B 1 27  ? -10.14900 15.38500  11.30200  1.000 40.27000 ? 27  PHE A CB  1 
ATOM   1312 C CG  . PHE B 1 27  ? -9.18200  15.65600  12.42300  1.000 42.99000 ? 27  PHE A CG  1 
ATOM   1313 C CD1 . PHE B 1 27  ? -7.93100  16.19600  12.16400  1.000 45.14000 ? 27  PHE A CD1 1 
ATOM   1314 C CD2 . PHE B 1 27  ? -9.52900  15.38400  13.73700  1.000 47.16000 ? 27  PHE A CD2 1 
ATOM   1315 C CE1 . PHE B 1 27  ? -7.03800  16.45300  13.19600  1.000 44.05000 ? 27  PHE A CE1 1 
ATOM   1316 C CE2 . PHE B 1 27  ? -8.64000  15.63800  14.77500  1.000 46.56000 ? 27  PHE A CE2 1 
ATOM   1317 C CZ  . PHE B 1 27  ? -7.39500  16.17300  14.50300  1.000 49.36000 ? 27  PHE A CZ  1 
ATOM   1318 N N   . ALA B 1 28  ? -11.46400 12.53500  12.01900  1.000 40.57000 ? 28  ALA A N   1 
ATOM   1319 C CA  . ALA B 1 28  ? -11.73300 11.54200  13.05500  1.000 39.33000 ? 28  ALA A CA  1 
ATOM   1320 C C   . ALA B 1 28  ? -11.14800 10.18100  12.69300  1.000 34.77000 ? 28  ALA A C   1 
ATOM   1321 O O   . ALA B 1 28  ? -10.54700 9.51400   13.54300  1.000 39.24000 ? 28  ALA A O   1 
ATOM   1322 C CB  . ALA B 1 28  ? -13.23800 11.43300  13.29500  1.000 44.29000 ? 28  ALA A CB  1 
ATOM   1323 N N   . LEU B 1 29  ? -11.32300 9.74700   11.44200  1.000 36.99000 ? 29  LEU A N   1 
ATOM   1324 C CA  . LEU B 1 29  ? -10.72900 8.48400   11.01500  1.000 32.24000 ? 29  LEU A CA  1 
ATOM   1325 C C   . LEU B 1 29  ? -9.21100  8.57800   10.94100  1.000 32.06000 ? 29  LEU A C   1 
ATOM   1326 O O   . LEU B 1 29  ? -8.51800  7.59700   11.23800  1.000 32.28000 ? 29  LEU A O   1 
ATOM   1327 C CB  . LEU B 1 29  ? -11.30400 8.05300   9.66400   1.000 42.97000 ? 29  LEU A CB  1 
ATOM   1328 C CG  . LEU B 1 29  ? -12.75900 7.57200   9.63700   1.000 42.66000 ? 29  LEU A CG  1 
ATOM   1329 C CD1 . LEU B 1 29  ? -13.72300 8.69700   9.99300   1.000 44.46000 ? 29  LEU A CD1 1 
ATOM   1330 C CD2 . LEU B 1 29  ? -13.10400 6.98500   8.27600   1.000 44.84000 ? 29  LEU A CD2 1 
ATOM   1331 N N   . ARG B 1 30  ? -8.67900  9.73900   10.55200  1.000 28.32000 ? 30  ARG A N   1 
ATOM   1332 C CA  . ARG B 1 30  ? -7.23100  9.91000   10.52000  1.000 30.68000 ? 30  ARG A CA  1 
ATOM   1333 C C   . ARG B 1 30  ? -6.64000  9.73900   11.90700  1.000 36.22000 ? 30  ARG A C   1 
ATOM   1334 O O   . ARG B 1 30  ? -5.57900  9.12200   12.07300  1.000 32.67000 ? 30  ARG A O   1 
ATOM   1335 C CB  . ARG B 1 30  ? -6.86700  11.28700  9.96600   1.000 29.46000 ? 30  ARG A CB  1 
ATOM   1336 C CG  . ARG B 1 30  ? -7.42400  11.58400  8.58400   1.000 35.16000 ? 30  ARG A CG  1 
ATOM   1337 C CD  . ARG B 1 30  ? -6.53400  12.56700  7.83500   1.000 34.57000 ? 30  ARG A CD  1 
ATOM   1338 N NE  . ARG B 1 30  ? -6.05300  13.63300  8.70900   1.000 44.37000 ? 30  ARG A NE  1 
ATOM   1339 C CZ  . ARG B 1 30  ? -6.60600  14.84000  8.78100   1.000 35.03000 ? 30  ARG A CZ  1 
ATOM   1340 N NH1 . ARG B 1 30  ? -7.65600  15.13000  8.02700   1.000 31.41000 ? 30  ARG A NH1 1 
ATOM   1341 N NH2 . ARG B 1 30  ? -6.11300  15.75100  9.60300   1.000 38.37000 ? 30  ARG A NH2 1 
ATOM   1342 N N   . LYS B 1 31  ? -7.30800  10.29300  12.91900  1.000 31.42000 ? 31  LYS A N   1 
ATOM   1343 C CA  . LYS B 1 31  ? -6.79000  10.18300  14.27600  1.000 36.58000 ? 31  LYS A CA  1 
ATOM   1344 C C   . LYS B 1 31  ? -6.73500  8.72900   14.71600  1.000 39.25000 ? 31  LYS A C   1 
ATOM   1345 O O   . LYS B 1 31  ? -5.79100  8.31200   15.39600  1.000 42.21000 ? 31  LYS A O   1 
ATOM   1346 C CB  . LYS B 1 31  ? -7.64900  11.01300  15.23100  1.000 45.79000 ? 31  LYS A CB  1 
ATOM   1347 C CG  . LYS B 1 31  ? -6.83500  11.84500  16.21000  1.000 48.73000 ? 31  LYS A CG  1 
ATOM   1348 C CD  . LYS B 1 31  ? -7.71400  12.80300  16.99900  1.000 56.45000 ? 31  LYS A CD  1 
ATOM   1349 C CE  . LYS B 1 31  ? -8.40100  12.09800  18.15600  1.000 54.24000 ? 31  LYS A CE  1 
ATOM   1350 N NZ  . LYS B 1 31  ? -7.44400  11.76700  19.24900  1.000 57.94000 ? 31  LYS A NZ  1 
ATOM   1351 N N   . ILE B 1 32  ? -7.72400  7.93000   14.30900  1.000 39.70000 ? 32  ILE A N   1 
ATOM   1352 C CA  . ILE B 1 32  ? -7.78800  6.55000   14.77300  1.000 37.96000 ? 32  ILE A CA  1 
ATOM   1353 C C   . ILE B 1 32  ? -6.71700  5.68700   14.11300  1.000 41.01000 ? 32  ILE A C   1 
ATOM   1354 O O   . ILE B 1 32  ? -6.20400  4.74800   14.73100  1.000 39.22000 ? 32  ILE A O   1 
ATOM   1355 C CB  . ILE B 1 32  ? -9.20000  5.98200   14.54300  1.000 42.63000 ? 32  ILE A CB  1 
ATOM   1356 C CG1 . ILE B 1 32  ? -10.20600 6.78800   15.36100  1.000 47.99000 ? 32  ILE A CG1 1 
ATOM   1357 C CG2 . ILE B 1 32  ? -9.25600  4.51300   14.93100  1.000 48.72000 ? 32  ILE A CG2 1 
ATOM   1358 C CD1 . ILE B 1 32  ? -9.96300  6.68400   16.85200  1.000 51.56000 ? 32  ILE A CD1 1 
ATOM   1359 N N   . ALA B 1 33  ? -6.34100  5.98800   12.87100  1.000 34.58000 ? 33  ALA A N   1 
ATOM   1360 C CA  . ALA B 1 33  ? -5.44500  5.10300   12.14300  1.000 34.83000 ? 33  ALA A CA  1 
ATOM   1361 C C   . ALA B 1 33  ? -3.98700  5.54200   12.15200  1.000 28.61000 ? 33  ALA A C   1 
ATOM   1362 O O   . ALA B 1 33  ? -3.12500  4.72200   11.82700  1.000 27.14000 ? 33  ALA A O   1 
ATOM   1363 C CB  . ALA B 1 33  ? -5.90500  4.96100   10.68700  1.000 35.43000 ? 33  ALA A CB  1 
ATOM   1364 N N   . VAL B 1 34  ? -3.68300  6.78900   12.53400  1.000 28.97000 ? 34  VAL A N   1 
ATOM   1365 C CA  . VAL B 1 34  ? -2.36300  7.35300   12.23600  1.000 33.55000 ? 34  VAL A CA  1 
ATOM   1366 C C   . VAL B 1 34  ? -1.25600  6.55800   12.91200  1.000 33.77000 ? 34  VAL A C   1 
ATOM   1367 O O   . VAL B 1 34  ? -0.15100  6.42300   12.37200  1.000 26.05000 ? 34  VAL A O   1 
ATOM   1368 C CB  . VAL B 1 34  ? -2.29500  8.84100   12.63100  1.000 30.06000 ? 34  VAL A CB  1 
ATOM   1369 C CG1 . VAL B 1 34  ? -2.50500  9.00900   14.12900  1.000 30.91000 ? 34  VAL A CG1 1 
ATOM   1370 C CG2 . VAL B 1 34  ? -0.94200  9.42900   12.22200  1.000 34.06000 ? 34  VAL A CG2 1 
ATOM   1371 N N   . ARG B 1 35  ? -1.51300  6.03900   14.11100  1.000 30.64000 ? 35  ARG A N   1 
ATOM   1372 C CA  . ARG B 1 35  ? -0.47300  5.33500   14.85200  1.000 30.92000 ? 35  ARG A CA  1 
ATOM   1373 C C   . ARG B 1 35  ? -0.80000  3.85800   15.03300  1.000 29.99000 ? 35  ARG A C   1 
ATOM   1374 O O   . ARG B 1 35  ? -0.25800  3.21500   15.93700  1.000 36.26000 ? 35  ARG A O   1 
ATOM   1375 C CB  . ARG B 1 35  ? -0.23100  6.00600   16.20700  1.000 34.09000 ? 35  ARG A CB  1 
ATOM   1376 C CG  . ARG B 1 35  ? 0.19900   7.46900   16.10200  1.000 35.45000 ? 35  ARG A CG  1 
ATOM   1377 C CD  . ARG B 1 35  ? 1.69600   7.59300   15.85100  1.000 41.73000 ? 35  ARG A CD  1 
ATOM   1378 N NE  . ARG B 1 35  ? 2.15900   8.98000   15.88000  1.000 41.61000 ? 35  ARG A NE  1 
ATOM   1379 C CZ  . ARG B 1 35  ? 2.46200   9.68800   14.79400  1.000 48.25000 ? 35  ARG A CZ  1 
ATOM   1380 N NH1 . ARG B 1 35  ? 2.87900   10.94500  14.91000  1.000 49.82000 ? 35  ARG A NH1 1 
ATOM   1381 N NH2 . ARG B 1 35  ? 2.35000   9.14000   13.58900  1.000 43.74000 ? 35  ARG A NH2 1 
ATOM   1382 N N   . LEU B 1 36  ? -1.66800  3.30600   14.18900  1.000 30.90000 ? 36  LEU A N   1 
ATOM   1383 C CA  . LEU B 1 36  ? -1.95000  1.88000   14.22600  1.000 30.13000 ? 36  LEU A CA  1 
ATOM   1384 C C   . LEU B 1 36  ? -0.79800  1.10400   13.60700  1.000 32.32000 ? 36  LEU A C   1 
ATOM   1385 O O   . LEU B 1 36  ? -0.21900  1.52400   12.60300  1.000 33.34000 ? 36  LEU A O   1 
ATOM   1386 C CB  . LEU B 1 36  ? -3.24400  1.56200   13.47200  1.000 33.40000 ? 36  LEU A CB  1 
ATOM   1387 C CG  . LEU B 1 36  ? -4.49100  1.22700   14.29100  1.000 39.84000 ? 36  LEU A CG  1 
ATOM   1388 C CD1 . LEU B 1 36  ? -4.29600  -0.05900  15.08900  1.000 43.39000 ? 36  LEU A CD1 1 
ATOM   1389 C CD2 . LEU B 1 36  ? -4.86500  2.37300   15.21200  1.000 39.03000 ? 36  LEU A CD2 1 
ATOM   1390 N N   . THR B 1 37  ? -0.46300  -0.03100  14.21200  1.000 33.24000 ? 37  THR A N   1 
ATOM   1391 C CA  . THR B 1 37  ? 0.50200   -0.94200  13.60900  1.000 34.35000 ? 37  THR A CA  1 
ATOM   1392 C C   . THR B 1 37  ? -0.20300  -1.81500  12.57800  1.000 38.21000 ? 37  THR A C   1 
ATOM   1393 O O   . THR B 1 37  ? -1.22000  -2.44800  12.88000  1.000 39.69000 ? 37  THR A O   1 
ATOM   1394 C CB  . THR B 1 37  ? 1.17200   -1.80700  14.67500  1.000 35.13000 ? 37  THR A CB  1 
ATOM   1395 O OG1 . THR B 1 37  ? 1.70800   -0.96400  15.70200  1.000 35.05000 ? 37  THR A OG1 1 
ATOM   1396 C CG2 . THR B 1 37  ? 2.30400   -2.61700  14.05900  1.000 34.83000 ? 37  THR A CG2 1 
ATOM   1397 N N   . LEU B 1 38  ? 0.33200   -1.83700  11.35900  1.000 35.24000 ? 38  LEU A N   1 
ATOM   1398 C CA  . LEU B 1 38  ? -0.29800  -2.49300  10.22100  1.000 28.19000 ? 38  LEU A CA  1 
ATOM   1399 C C   . LEU B 1 38  ? 0.42400   -3.78400  9.85600   1.000 30.29000 ? 38  LEU A C   1 
ATOM   1400 O O   . LEU B 1 38  ? 1.64400   -3.89400  9.99200   1.000 26.52000 ? 38  LEU A O   1 
ATOM   1401 C CB  . LEU B 1 38  ? -0.33100  -1.55300  9.00800   1.000 30.99000 ? 38  LEU A CB  1 
ATOM   1402 C CG  . LEU B 1 38  ? -0.71000  -0.09600  9.31700   1.000 28.90000 ? 38  LEU A CG  1 
ATOM   1403 C CD1 . LEU B 1 38  ? -0.49600  0.80500   8.10600   1.000 34.40000 ? 38  LEU A CD1 1 
ATOM   1404 C CD2 . LEU B 1 38  ? -2.15000  0.01600   9.82700   1.000 29.70000 ? 38  LEU A CD2 1 
ATOM   1405 N N   . THR B 1 39  ? -0.33800  -4.76700  9.38500   1.000 25.32000 ? 39  THR A N   1 
ATOM   1406 C CA  . THR B 1 39  ? 0.22100   -6.00800  8.86800   1.000 26.93000 ? 39  THR A CA  1 
ATOM   1407 C C   . THR B 1 39  ? -0.24700  -6.19800  7.43300   1.000 28.17000 ? 39  THR A C   1 
ATOM   1408 O O   . THR B 1 39  ? -1.42900  -6.01400  7.13000   1.000 31.12000 ? 39  THR A O   1 
ATOM   1409 C CB  . THR B 1 39  ? -0.17500  -7.20800  9.73100   1.000 32.99000 ? 39  THR A CB  1 
ATOM   1410 O OG1 . THR B 1 39  ? 0.46800   -7.10500  11.00400  1.000 33.61000 ? 39  THR A OG1 1 
ATOM   1411 C CG2 . THR B 1 39  ? 0.26100   -8.50600  9.07500   1.000 28.34000 ? 39  THR A CG2 1 
ATOM   1412 N N   . LEU B 1 40  ? 0.68100   -6.58000  6.56100   1.000 20.54000 ? 40  LEU A N   1 
ATOM   1413 C CA  . LEU B 1 40  ? 0.46000   -6.65200  5.12200   1.000 22.27000 ? 40  LEU A CA  1 
ATOM   1414 C C   . LEU B 1 40  ? 0.71500   -8.08300  4.67200   1.000 28.42000 ? 40  LEU A C   1 
ATOM   1415 O O   . LEU B 1 40  ? 1.82500   -8.59900  4.83500   1.000 31.28000 ? 40  LEU A O   1 
ATOM   1416 C CB  . LEU B 1 40  ? 1.38600   -5.66200  4.40900   1.000 27.07000 ? 40  LEU A CB  1 
ATOM   1417 C CG  . LEU B 1 40  ? 1.46600   -5.48300  2.89600   1.000 30.98000 ? 40  LEU A CG  1 
ATOM   1418 C CD1 . LEU B 1 40  ? 0.15700   -4.94700  2.30600   1.000 29.90000 ? 40  LEU A CD1 1 
ATOM   1419 C CD2 . LEU B 1 40  ? 2.63500   -4.54500  2.58900   1.000 26.80000 ? 40  LEU A CD2 1 
ATOM   1420 N N   . VAL B 1 41  ? -0.31400  -8.72400  4.13000   1.000 24.52000 ? 41  VAL A N   1 
ATOM   1421 C CA  . VAL B 1 41  ? -0.24600  -10.10500 3.66800   1.000 23.20000 ? 41  VAL A CA  1 
ATOM   1422 C C   . VAL B 1 41  ? -0.36400  -10.08500 2.15400   1.000 27.63000 ? 41  VAL A C   1 
ATOM   1423 O O   . VAL B 1 41  ? -1.35500  -9.58400  1.61000   1.000 27.24000 ? 41  VAL A O   1 
ATOM   1424 C CB  . VAL B 1 41  ? -1.35400  -10.97200 4.28500   1.000 28.60000 ? 41  VAL A CB  1 
ATOM   1425 C CG1 . VAL B 1 41  ? -1.24900  -12.41000 3.77500   1.000 31.14000 ? 41  VAL A CG1 1 
ATOM   1426 C CG2 . VAL B 1 41  ? -1.30100  -10.92600 5.80700   1.000 31.62000 ? 41  VAL A CG2 1 
ATOM   1427 N N   . ILE B 1 42  ? 0.63400   -10.63400 1.47500   1.000 23.45000 ? 42  ILE A N   1 
ATOM   1428 C CA  . ILE B 1 42  ? 0.69900   -10.61200 0.02000   1.000 24.96000 ? 42  ILE A CA  1 
ATOM   1429 C C   . ILE B 1 42  ? 0.76800   -12.04500 -0.48500  1.000 28.21000 ? 42  ILE A C   1 
ATOM   1430 O O   . ILE B 1 42  ? 1.65400   -12.81000 -0.08100  1.000 23.54000 ? 42  ILE A O   1 
ATOM   1431 C CB  . ILE B 1 42  ? 1.90000   -9.79800  -0.48000  1.000 23.81000 ? 42  ILE A CB  1 
ATOM   1432 C CG1 . ILE B 1 42  ? 1.76100   -8.33800  -0.04100  1.000 21.09000 ? 42  ILE A CG1 1 
ATOM   1433 C CG2 . ILE B 1 42  ? 2.02400   -9.92900  -1.99300  1.000 23.50000 ? 42  ILE A CG2 1 
ATOM   1434 C CD1 . ILE B 1 42  ? 3.00500   -7.51300  -0.28500  1.000 18.07000 ? 42  ILE A CD1 1 
ATOM   1435 N N   . ASP B 1 43  ? -0.16500  -12.41100 -1.36400  1.000 22.86000 ? 43  ASP A N   1 
ATOM   1436 C CA  . ASP B 1 43  ? -0.09100  -13.66200 -2.10500  1.000 28.10000 ? 43  ASP A CA  1 
ATOM   1437 C C   . ASP B 1 43  ? 0.15400   -13.32100 -3.56700  1.000 27.67000 ? 43  ASP A C   1 
ATOM   1438 O O   . ASP B 1 43  ? -0.66000  -12.63400 -4.18900  1.000 28.19000 ? 43  ASP A O   1 
ATOM   1439 C CB  . ASP B 1 43  ? -1.36900  -14.49000 -1.95100  1.000 27.58000 ? 43  ASP A CB  1 
ATOM   1440 C CG  . ASP B 1 43  ? -1.26500  -15.85100 -2.63200  1.000 40.90000 ? 43  ASP A CG  1 
ATOM   1441 O OD1 . ASP B 1 43  ? -0.16400  -16.20100 -3.11500  1.000 45.06000 ? 43  ASP A OD1 1 
ATOM   1442 O OD2 . ASP B 1 43  ? -2.28000  -16.58000 -2.67100  1.000 51.81000 ? 43  ASP A OD2 1 
ATOM   1443 N N   . GLN B 1 44  ? 1.27000   -13.79100 -4.10500  1.000 24.88000 ? 44  GLN A N   1 
ATOM   1444 C CA  . GLN B 1 44  ? 1.68000   -13.49400 -5.47000  1.000 27.40000 ? 44  GLN A CA  1 
ATOM   1445 C C   . GLN B 1 44  ? 1.91200   -14.80000 -6.21400  1.000 31.17000 ? 44  GLN A C   1 
ATOM   1446 O O   . GLN B 1 44  ? 2.61400   -15.68800 -5.71900  1.000 25.46000 ? 44  GLN A O   1 
ATOM   1447 C CB  . GLN B 1 44  ? 2.94900   -12.63100 -5.48500  1.000 23.15000 ? 44  GLN A CB  1 
ATOM   1448 C CG  . GLN B 1 44  ? 3.60900   -12.47400 -6.84200  1.000 28.16000 ? 44  GLN A CG  1 
ATOM   1449 C CD  . GLN B 1 44  ? 4.91200   -11.71700 -6.75400  1.000 25.29000 ? 44  GLN A CD  1 
ATOM   1450 O OE1 . GLN B 1 44  ? 5.33400   -11.31000 -5.67200  1.000 34.38000 ? 44  GLN A OE1 1 
ATOM   1451 N NE2 . GLN B 1 44  ? 5.56100   -11.52100 -7.89600  1.000 34.00000 ? 44  GLN A NE2 1 
ATOM   1452 N N   . ASP B 1 45  ? 1.32300   -14.91800 -7.39800  1.000 25.60000 ? 45  ASP A N   1 
ATOM   1453 C CA  . ASP B 1 45  ? 1.50300   -16.10400 -8.23000  1.000 31.36000 ? 45  ASP A CA  1 
ATOM   1454 C C   . ASP B 1 45  ? 1.51700   -15.62200 -9.67600  1.000 28.92000 ? 45  ASP A C   1 
ATOM   1455 O O   . ASP B 1 45  ? 0.46800   -15.29100 -10.23500 1.000 30.05000 ? 45  ASP A O   1 
ATOM   1456 C CB  . ASP B 1 45  ? 0.40100   -17.12300 -7.97700  1.000 37.62000 ? 45  ASP A CB  1 
ATOM   1457 C CG  . ASP B 1 45  ? 0.41700   -18.25400 -8.97800  1.000 44.82000 ? 45  ASP A CG  1 
ATOM   1458 O OD1 . ASP B 1 45  ? -0.66400  -18.82400 -9.23300  1.000 54.96000 ? 45  ASP A OD1 1 
ATOM   1459 O OD2 . ASP B 1 45  ? 1.50600   -18.57000 -9.50500  1.000 39.52000 ? 45  ASP A OD2 1 
ATOM   1460 N N   . GLY B 1 46  ? 2.70500   -15.57300 -10.26800 1.000 30.80000 ? 46  GLY A N   1 
ATOM   1461 C CA  . GLY B 1 46  ? 2.83100   -14.98500 -11.59200 1.000 31.67000 ? 46  GLY A CA  1 
ATOM   1462 C C   . GLY B 1 46  ? 2.42600   -13.52100 -11.56200 1.000 28.86000 ? 46  GLY A C   1 
ATOM   1463 O O   . GLY B 1 46  ? 2.89200   -12.73400 -10.73200 1.000 33.18000 ? 46  GLY A O   1 
ATOM   1464 N N   . ASP B 1 47  ? 1.53800   -13.14600 -12.47600 1.000 29.90000 ? 47  ASP A N   1 
ATOM   1465 C CA  . ASP B 1 47  ? 1.02000   -11.78300 -12.53100 1.000 29.46000 ? 47  ASP A CA  1 
ATOM   1466 C C   . ASP B 1 47  ? -0.08000  -11.51300 -11.50500 1.000 30.20000 ? 47  ASP A C   1 
ATOM   1467 O O   . ASP B 1 47  ? -0.46300  -10.35400 -11.31700 1.000 24.15000 ? 47  ASP A O   1 
ATOM   1468 C CB  . ASP B 1 47  ? 0.49100   -11.48700 -13.94000 1.000 26.70000 ? 47  ASP A CB  1 
ATOM   1469 C CG  . ASP B 1 47  ? -0.50500  -12.53300 -14.42200 1.000 43.41000 ? 47  ASP A CG  1 
ATOM   1470 O OD1 . ASP B 1 47  ? -0.06300  -13.60700 -14.88500 1.000 48.51000 ? 47  ASP A OD1 1 
ATOM   1471 O OD2 . ASP B 1 47  ? -1.72700  -12.28500 -14.33900 1.000 52.01000 ? 47  ASP A OD2 1 
ATOM   1472 N N   . ASN B 1 48  ? -0.58300  -12.53300 -10.82100 1.000 25.71000 ? 48  ASN A N   1 
ATOM   1473 C CA  . ASN B 1 48  ? -1.75400  -12.37100 -9.97000  1.000 22.13000 ? 48  ASN A CA  1 
ATOM   1474 C C   . ASN B 1 48  ? -1.34400  -12.07700 -8.53100  1.000 26.35000 ? 48  ASN A C   1 
ATOM   1475 O O   . ASN B 1 48  ? -0.50400  -12.77800 -7.96000  1.000 27.13000 ? 48  ASN A O   1 
ATOM   1476 C CB  . ASN B 1 48  ? -2.63000  -13.62000 -10.04100 1.000 25.58000 ? 48  ASN A CB  1 
ATOM   1477 C CG  . ASN B 1 48  ? -3.20900  -13.83900 -11.43200 1.000 39.25000 ? 48  ASN A CG  1 
ATOM   1478 O OD1 . ASN B 1 48  ? -3.45900  -12.88300 -12.16600 1.000 36.39000 ? 48  ASN A OD1 1 
ATOM   1479 N ND2 . ASN B 1 48  ? -3.42100  -15.09900 -11.80000 1.000 43.35000 ? 48  ASN A ND2 1 
ATOM   1480 N N   . PHE B 1 49  ? -1.95100  -11.04000 -7.95300  1.000 19.67000 ? 49  PHE A N   1 
ATOM   1481 C CA  . PHE B 1 49  ? -1.67900  -10.57100 -6.60600  1.000 18.28000 ? 49  PHE A CA  1 
ATOM   1482 C C   . PHE B 1 49  ? -2.96600  -10.52200 -5.80200  1.000 25.22000 ? 49  PHE A C   1 
ATOM   1483 O O   . PHE B 1 49  ? -4.01200  -10.11500 -6.31600  1.000 21.08000 ? 49  PHE A O   1 
ATOM   1484 C CB  . PHE B 1 49  ? -1.08100  -9.15500  -6.62000  1.000 19.93000 ? 49  PHE A CB  1 
ATOM   1485 C CG  . PHE B 1 49  ? 0.37100   -9.11100  -6.94000  1.000 20.74000 ? 49  PHE A CG  1 
ATOM   1486 C CD1 . PHE B 1 49  ? 0.82100   -9.24200  -8.25000  1.000 20.43000 ? 49  PHE A CD1 1 
ATOM   1487 C CD2 . PHE B 1 49  ? 1.29100   -8.91100  -5.92800  1.000 19.75000 ? 49  PHE A CD2 1 
ATOM   1488 C CE1 . PHE B 1 49  ? 2.17500   -9.17900  -8.53800  1.000 20.29000 ? 49  PHE A CE1 1 
ATOM   1489 C CE2 . PHE B 1 49  ? 2.62900   -8.85000  -6.20600  1.000 20.39000 ? 49  PHE A CE2 1 
ATOM   1490 C CZ  . PHE B 1 49  ? 3.07600   -8.98200  -7.50900  1.000 17.73000 ? 49  PHE A CZ  1 
ATOM   1491 N N   . LYS B 1 50  ? -2.82000  -10.74700 -4.50500  1.000 21.88000 ? 50  LYS A N   1 
ATOM   1492 C CA  . LYS B 1 50  ? -3.88300  -10.59400 -3.53000  1.000 26.35000 ? 50  LYS A CA  1 
ATOM   1493 C C   . LYS B 1 50  ? -3.17100  -9.88400  -2.37900  1.000 27.12000 ? 50  LYS A C   1 
ATOM   1494 O O   . LYS B 1 50  ? -2.21600  -10.41200 -1.84200  1.000 27.55000 ? 50  LYS A O   1 
ATOM   1495 C CB  . LYS B 1 50  ? -4.44700  -11.93600 -3.10400  1.000 31.54000 ? 50  LYS A CB  1 
ATOM   1496 C CG  . LYS B 1 50  ? -4.37800  -12.98100 -4.19800  1.000 41.55000 ? 50  LYS A CG  1 
ATOM   1497 C CD  . LYS B 1 50  ? -5.76000  -13.42600 -4.62300  1.000 41.26000 ? 50  LYS A CD  1 
ATOM   1498 C CE  . LYS B 1 50  ? -6.32000  -14.40400 -3.61100  1.000 48.89000 ? 50  LYS A CE  1 
ATOM   1499 N NZ  . LYS B 1 50  ? -6.61700  -13.70800 -2.33200  1.000 50.18000 ? 50  LYS A NZ  1 
ATOM   1500 N N   . THR B 1 51  ? -3.61100  -8.68300  -2.02700  1.000 25.41000 ? 51  THR A N   1 
ATOM   1501 C CA  . THR B 1 51  ? -2.96100  -7.89400  -0.98500  1.000 25.75000 ? 51  THR A CA  1 
ATOM   1502 C C   . THR B 1 51  ? -3.99000  -7.55000  0.08200   1.000 35.87000 ? 51  THR A C   1 
ATOM   1503 O O   . THR B 1 51  ? -5.00400  -6.90100  -0.20800  1.000 35.53000 ? 51  THR A O   1 
ATOM   1504 C CB  . THR B 1 51  ? -2.32800  -6.61800  -1.55100  1.000 21.88000 ? 51  THR A CB  1 
ATOM   1505 O OG1 . THR B 1 51  ? -1.34500  -6.95300  -2.54200  1.000 29.88000 ? 51  THR A OG1 1 
ATOM   1506 C CG2 . THR B 1 51  ? -1.66900  -5.80700  -0.42900  1.000 26.88000 ? 51  THR A CG2 1 
ATOM   1507 N N   . LYS B 1 52  ? -3.73600  -8.00000  1.30700   1.000 26.28000 ? 52  LYS A N   1 
ATOM   1508 C CA  . LYS B 1 52  ? -4.59900  -7.72000  2.44400   1.000 29.21000 ? 52  LYS A CA  1 
ATOM   1509 C C   . LYS B 1 52  ? -3.82300  -6.89000  3.45200   1.000 36.61000 ? 52  LYS A C   1 
ATOM   1510 O O   . LYS B 1 52  ? -2.68300  -7.22700  3.79900   1.000 27.99000 ? 52  LYS A O   1 
ATOM   1511 C CB  . LYS B 1 52  ? -5.10100  -9.00600  3.10000   1.000 34.74000 ? 52  LYS A CB  1 
ATOM   1512 N N   . CYS B 1 53  ? -4.46500  -5.83900  3.93500   1.000 37.56000 ? 53  CYS A N   1 
ATOM   1513 C CA  . CYS B 1 53  ? -3.89700  -4.95900  4.93300   1.000 37.13000 ? 53  CYS A CA  1 
ATOM   1514 C C   . CYS B 1 53  ? -4.76900  -5.13400  6.15400   1.000 47.87000 ? 53  CYS A C   1 
ATOM   1515 O O   . CYS B 1 53  ? -5.95300  -4.82600  6.12100   1.000 44.95000 ? 53  CYS A O   1 
ATOM   1516 C CB  . CYS B 1 53  ? -3.93400  -3.51500  4.46000   1.000 46.14000 ? 53  CYS A CB  1 
ATOM   1517 S SG  . CYS B 1 53  ? -3.12700  -3.25800  2.86200   1.000 70.79000 ? 53  CYS A SG  1 
ATOM   1518 N N   . THR B 1 54  ? -4.18100  -5.59100  7.21800   1.000 44.39000 ? 54  THR A N   1 
ATOM   1519 C CA  . THR B 1 54  ? -4.91800  -5.79800  8.39900   1.000 44.20000 ? 54  THR A CA  1 
ATOM   1520 C C   . THR B 1 54  ? -4.43000  -4.91900  9.52500   1.000 49.26000 ? 54  THR A C   1 
ATOM   1521 O O   . THR B 1 54  ? -3.27900  -4.71600  9.72500   1.000 33.38000 ? 54  THR A O   1 
ATOM   1522 C CB  . THR B 1 54  ? -4.79200  -7.23900  8.86200   1.000 53.60000 ? 54  THR A CB  1 
ATOM   1523 O OG1 . THR B 1 54  ? -4.72600  -8.12000  7.72400   1.000 59.50000 ? 54  THR A OG1 1 
ATOM   1524 C CG2 . THR B 1 54  ? -5.98200  -7.59400  9.69600   1.000 57.21000 ? 54  THR A CG2 1 
ATOM   1525 N N   . SER B 1 55  ? -5.40300  -4.42000  10.25100  1.000 52.85000 ? 55  SER A N   1 
ATOM   1526 C CA  . SER B 1 55  ? -5.23500  -3.61400  11.43000  1.000 52.96000 ? 55  SER A CA  1 
ATOM   1527 C C   . SER B 1 55  ? -6.43800  -3.85700  12.30700  1.000 61.07000 ? 55  SER A C   1 
ATOM   1528 O O   . SER B 1 55  ? -7.44000  -4.41300  11.87000  1.000 65.49000 ? 55  SER A O   1 
ATOM   1529 C CB  . SER B 1 55  ? -5.16100  -2.14300  11.06500  1.000 49.48000 ? 55  SER A CB  1 
ATOM   1530 O OG  . SER B 1 55  ? -6.42700  -1.67300  10.71700  1.000 59.52000 ? 55  SER A OG  1 
ATOM   1531 N N   . THR B 1 56  ? -6.38700  -3.41400  13.54500  1.000 60.11000 ? 56  THR A N   1 
ATOM   1532 C CA  . THR B 1 56  ? -7.52400  -3.61900  14.44500  1.000 63.79000 ? 56  THR A CA  1 
ATOM   1533 C C   . THR B 1 56  ? -8.86900  -3.12600  13.93900  1.000 67.07000 ? 56  THR A C   1 
ATOM   1534 O O   . THR B 1 56  ? -9.86900  -3.77900  14.14500  1.000 69.33000 ? 56  THR A O   1 
ATOM   1535 C CB  . THR B 1 56  ? -7.32500  -2.94200  15.79800  1.000 60.43000 ? 56  THR A CB  1 
ATOM   1536 O OG1 . THR B 1 56  ? -5.95800  -3.01100  16.15700  1.000 62.33000 ? 56  THR A OG1 1 
ATOM   1537 C CG2 . THR B 1 56  ? -8.14300  -3.59300  16.87100  1.000 52.33000 ? 56  THR A CG2 1 
ATOM   1538 N N   . PHE B 1 57  ? -8.90700  -2.00500  13.25200  1.000 65.64000 ? 57  PHE A N   1 
ATOM   1539 C CA  . PHE B 1 57  ? -10.19100 -1.50300  12.84400  1.000 67.70000 ? 57  PHE A CA  1 
ATOM   1540 C C   . PHE B 1 57  ? -10.55500 -1.64800  11.39400  1.000 74.47000 ? 57  PHE A C   1 
ATOM   1541 O O   . PHE B 1 57  ? -11.64700 -2.09800  11.09200  1.000 72.79000 ? 57  PHE A O   1 
ATOM   1542 C CB  . PHE B 1 57  ? -10.38700 -0.11300  13.35900  1.000 67.86000 ? 57  PHE A CB  1 
ATOM   1543 C CG  . PHE B 1 57  ? -10.59400 -0.10000  14.82800  1.000 64.58000 ? 57  PHE A CG  1 
ATOM   1544 C CD1 . PHE B 1 57  ? -10.08600 0.88000   15.61000  1.000 63.95000 ? 57  PHE A CD1 1 
ATOM   1545 C CD2 . PHE B 1 57  ? -11.23300 -1.15700  15.41900  1.000 65.49000 ? 57  PHE A CD2 1 
ATOM   1546 C CE1 . PHE B 1 57  ? -10.25100 0.85200   16.96900  1.000 64.51000 ? 57  PHE A CE1 1 
ATOM   1547 C CE2 . PHE B 1 57  ? -11.40200 -1.21400  16.78500  1.000 62.85000 ? 57  PHE A CE2 1 
ATOM   1548 C CZ  . PHE B 1 57  ? -10.92600 -0.19600  17.55900  1.000 64.61000 ? 57  PHE A CZ  1 
ATOM   1549 N N   . TYR B 1 58  ? -9.64400  -1.29600  10.49200  1.000 75.49000 ? 58  TYR A N   1 
ATOM   1550 C CA  . TYR B 1 58  ? -9.93200  -1.37600  9.06000   1.000 73.35000 ? 58  TYR A CA  1 
ATOM   1551 C C   . TYR B 1 58  ? -9.31700  -2.57200  8.32600   1.000 69.68000 ? 58  TYR A C   1 
ATOM   1552 O O   . TYR B 1 58  ? -8.39200  -3.22000  8.81700   1.000 68.61000 ? 58  TYR A O   1 
ATOM   1553 C CB  . TYR B 1 58  ? -9.52700  -0.07300  8.36400   1.000 71.86000 ? 58  TYR A CB  1 
ATOM   1554 C CG  . TYR B 1 58  ? -10.57000 1.01700   8.45900   1.000 73.99000 ? 58  TYR A CG  1 
ATOM   1555 C CD1 . TYR B 1 58  ? -11.92400 0.71000   8.46500   1.000 77.24000 ? 58  TYR A CD1 1 
ATOM   1556 C CD2 . TYR B 1 58  ? -10.20200 2.35300   8.54500   1.000 72.85000 ? 58  TYR A CD2 1 
ATOM   1557 C CE1 . TYR B 1 58  ? -12.88200 1.70200   8.55300   1.000 73.63000 ? 58  TYR A CE1 1 
ATOM   1558 C CE2 . TYR B 1 58  ? -11.15300 3.35200   8.63300   1.000 71.30000 ? 58  TYR A CE2 1 
ATOM   1559 C CZ  . TYR B 1 58  ? -12.49100 3.02100   8.63700   1.000 74.77000 ? 58  TYR A CZ  1 
ATOM   1560 O OH  . TYR B 1 58  ? -13.44100 4.01300   8.72400   1.000 79.34000 ? 58  TYR A OH  1 
ATOM   1561 N N   . ASN B 1 59  ? -9.85700  -2.84300  7.14100   1.000 62.80000 ? 59  ASN A N   1 
ATOM   1562 C CA  . ASN B 1 59  ? -9.41500  -3.92600  6.27500   1.000 60.82000 ? 59  ASN A CA  1 
ATOM   1563 C C   . ASN B 1 59  ? -9.39300  -3.35300  4.85300   1.000 57.12000 ? 59  ASN A C   1 
ATOM   1564 O O   . ASN B 1 59  ? -10.34600 -2.77900  4.42200   1.000 53.27000 ? 59  ASN A O   1 
ATOM   1565 C CB  . ASN B 1 59  ? -10.38200 -5.12900  6.28400   1.000 62.77000 ? 59  ASN A CB  1 
ATOM   1566 C CG  . ASN B 1 59  ? -10.03100 -6.20900  7.29700   1.000 68.25000 ? 59  ASN A CG  1 
ATOM   1567 O OD1 . ASN B 1 59  ? -10.07000 -5.98100  8.49700   1.000 70.81000 ? 59  ASN A OD1 1 
ATOM   1568 N ND2 . ASN B 1 59  ? -9.81700  -7.44100  6.80900   1.000 63.90000 ? 59  ASN A ND2 1 
ATOM   1569 N N   . TYR B 1 60  ? -8.27200  -3.48900  4.15300   1.000 49.12000 ? 60  TYR A N   1 
ATOM   1570 C CA  . TYR B 1 60  ? -8.15100  -3.02700  2.79300   1.000 41.19000 ? 60  TYR A CA  1 
ATOM   1571 C C   . TYR B 1 60  ? -7.67400  -4.25200  2.09100   1.000 42.79000 ? 60  TYR A C   1 
ATOM   1572 O O   . TYR B 1 60  ? -6.60000  -4.69400  2.36800   1.000 41.79000 ? 60  TYR A O   1 
ATOM   1573 C CB  . TYR B 1 60  ? -7.10200  -1.95000  2.70700   1.000 45.80000 ? 60  TYR A CB  1 
ATOM   1574 C CG  . TYR B 1 60  ? -7.06700  -1.15700  1.41000   1.000 51.02000 ? 60  TYR A CG  1 
ATOM   1575 C CD1 . TYR B 1 60  ? -7.88300  -0.03200  1.21500   1.000 51.16000 ? 60  TYR A CD1 1 
ATOM   1576 C CD2 . TYR B 1 60  ? -6.18400  -1.48700  0.41300   1.000 47.56000 ? 60  TYR A CD2 1 
ATOM   1577 C CE1 . TYR B 1 60  ? -7.81600  0.71400   0.03500   1.000 49.00000 ? 60  TYR A CE1 1 
ATOM   1578 C CE2 . TYR B 1 60  ? -6.12400  -0.77400  -0.75100  1.000 47.57000 ? 60  TYR A CE2 1 
ATOM   1579 C CZ  . TYR B 1 60  ? -6.91200  0.33100   -0.93800  1.000 49.12000 ? 60  TYR A CZ  1 
ATOM   1580 O OH  . TYR B 1 60  ? -6.80400  1.02000   -2.12000  1.000 47.59000 ? 60  TYR A OH  1 
ATOM   1581 N N   . ASP B 1 61  ? -8.48300  -4.83700  1.22800   1.000 36.82000 ? 61  ASP A N   1 
ATOM   1582 C CA  . ASP B 1 61  ? -8.12700  -6.04600  0.50600   1.000 30.97000 ? 61  ASP A CA  1 
ATOM   1583 C C   . ASP B 1 61  ? -8.29500  -5.82100  -0.99300  1.000 39.10000 ? 61  ASP A C   1 
ATOM   1584 O O   . ASP B 1 61  ? -9.35400  -5.46300  -1.41800  1.000 36.30000 ? 61  ASP A O   1 
ATOM   1585 C CB  . ASP B 1 61  ? -8.98600  -7.21900  0.96800   1.000 36.27000 ? 61  ASP A CB  1 
ATOM   1586 C CG  . ASP B 1 61  ? -8.87100  -8.43100  0.06400   1.000 45.16000 ? 61  ASP A CG  1 
ATOM   1587 O OD1 . ASP B 1 61  ? -9.90200  -9.04000  -0.23600  1.000 56.88000 ? 61  ASP A OD1 1 
ATOM   1588 O OD2 . ASP B 1 61  ? -7.77300  -8.83100  -0.34200  1.000 45.85000 ? 61  ASP A OD2 1 
ATOM   1589 N N   . VAL B 1 62  ? -7.24900  -6.05900  -1.77200  1.000 29.93000 ? 62  VAL A N   1 
ATOM   1590 C CA  . VAL B 1 62  ? -7.26300  -5.78700  -3.20700  1.000 31.40000 ? 62  VAL A CA  1 
ATOM   1591 C C   . VAL B 1 62  ? -6.63500  -6.96200  -3.94300  1.000 30.92000 ? 62  VAL A C   1 
ATOM   1592 O O   . VAL B 1 62  ? -5.59300  -7.48300  -3.52400  1.000 30.60000 ? 62  VAL A O   1 
ATOM   1593 C CB  . VAL B 1 62  ? -6.52900  -4.47300  -3.53800  1.000 26.16000 ? 62  VAL A CB  1 
ATOM   1594 C CG1 . VAL B 1 62  ? -5.04600  -4.59600  -3.23100  1.000 27.45000 ? 62  VAL A CG1 1 
ATOM   1595 C CG2 . VAL B 1 62  ? -6.74400  -4.09000  -4.99800  1.000 28.37000 ? 62  VAL A CG2 1 
ATOM   1596 N N   . ASP B 1 63  ? -7.27300  -7.38500  -5.03400  1.000 22.79000 ? 63  ASP A N   1 
ATOM   1597 C CA  . ASP B 1 63  ? -6.72900  -8.37600  -5.94800  1.000 26.01000 ? 63  ASP A CA  1 
ATOM   1598 C C   . ASP B 1 63  ? -6.53500  -7.71000  -7.29900  1.000 22.33000 ? 63  ASP A C   1 
ATOM   1599 O O   . ASP B 1 63  ? -7.39100  -6.93700  -7.74400  1.000 25.70000 ? 63  ASP A O   1 
ATOM   1600 C CB  . ASP B 1 63  ? -7.65700  -9.58900  -6.11100  1.000 31.15000 ? 63  ASP A CB  1 
ATOM   1601 C CG  . ASP B 1 63  ? -8.10200  -10.17100 -4.78500  1.000 43.97000 ? 63  ASP A CG  1 
ATOM   1602 O OD1 . ASP B 1 63  ? -9.09500  -10.93200 -4.77300  1.000 46.68000 ? 63  ASP A OD1 1 
ATOM   1603 O OD2 . ASP B 1 63  ? -7.46100  -9.86700  -3.75900  1.000 41.31000 ? 63  ASP A OD2 1 
ATOM   1604 N N   . PHE B 1 64  ? -5.41400  -8.00100  -7.94800  1.000 19.95000 ? 64  PHE A N   1 
ATOM   1605 C CA  . PHE B 1 64  ? -5.15200  -7.43000  -9.25500  1.000 17.57000 ? 64  PHE A CA  1 
ATOM   1606 C C   . PHE B 1 64  ? -4.22300  -8.34200  -10.02400 1.000 17.71000 ? 64  PHE A C   1 
ATOM   1607 O O   . PHE B 1 64  ? -3.57700  -9.23700  -9.46600  1.000 20.31000 ? 64  PHE A O   1 
ATOM   1608 C CB  . PHE B 1 64  ? -4.54500  -6.02000  -9.16200  1.000 17.85000 ? 64  PHE A CB  1 
ATOM   1609 C CG  . PHE B 1 64  ? -3.27200  -5.94200  -8.36000  1.000 19.06000 ? 64  PHE A CG  1 
ATOM   1610 C CD1 . PHE B 1 64  ? -2.04000  -6.17200  -8.95700  1.000 17.94000 ? 64  PHE A CD1 1 
ATOM   1611 C CD2 . PHE B 1 64  ? -3.30100  -5.59700  -7.02500  1.000 18.11000 ? 64  PHE A CD2 1 
ATOM   1612 C CE1 . PHE B 1 64  ? -0.86800  -6.07500  -8.21800  1.000 16.43000 ? 64  PHE A CE1 1 
ATOM   1613 C CE2 . PHE B 1 64  ? -2.12800  -5.49700  -6.27800  1.000 18.99000 ? 64  PHE A CE2 1 
ATOM   1614 C CZ  . PHE B 1 64  ? -0.91600  -5.74600  -6.87300  1.000 18.56000 ? 64  PHE A CZ  1 
ATOM   1615 N N   . THR B 1 65  ? -4.16100  -8.09100  -11.32400 1.000 17.32000 ? 65  THR A N   1 
ATOM   1616 C CA  . THR B 1 65  ? -3.21900  -8.73800  -12.21800 1.000 18.02000 ? 65  THR A CA  1 
ATOM   1617 C C   . THR B 1 65  ? -2.29800  -7.66700  -12.78100 1.000 17.58000 ? 65  THR A C   1 
ATOM   1618 O O   . THR B 1 65  ? -2.76900  -6.64600  -13.28900 1.000 15.63000 ? 65  THR A O   1 
ATOM   1619 C CB  . THR B 1 65  ? -3.95300  -9.46800  -13.33700 1.000 22.46000 ? 65  THR A CB  1 
ATOM   1620 O OG1 . THR B 1 65  ? -4.78700  -10.48700 -12.76200 1.000 24.42000 ? 65  THR A OG1 1 
ATOM   1621 C CG2 . THR B 1 65  ? -2.96900  -10.08500 -14.31600 1.000 24.41000 ? 65  THR A CG2 1 
ATOM   1622 N N   . VAL B 1 66  ? -0.98600  -7.89500  -12.68500 1.000 16.79000 ? 66  VAL A N   1 
ATOM   1623 C CA  . VAL B 1 66  ? -0.03700  -6.92400  -13.21800 1.000 14.15000 ? 66  VAL A CA  1 
ATOM   1624 C C   . VAL B 1 66  ? -0.36000  -6.65300  -14.68200 1.000 18.67000 ? 66  VAL A C   1 
ATOM   1625 O O   . VAL B 1 66  ? -0.61100  -7.58100  -15.45300 1.000 17.70000 ? 66  VAL A O   1 
ATOM   1626 C CB  . VAL B 1 66  ? 1.39900   -7.44400  -13.03600 1.000 18.08000 ? 66  VAL A CB  1 
ATOM   1627 C CG1 . VAL B 1 66  ? 2.37000   -6.55300  -13.77600 1.000 19.79000 ? 66  VAL A CG1 1 
ATOM   1628 C CG2 . VAL B 1 66  ? 1.74500   -7.50100  -11.55300 1.000 22.45000 ? 66  VAL A CG2 1 
ATOM   1629 N N   . GLY B 1 67  ? -0.38200  -5.37200  -15.06200 1.000 12.57000 ? 67  GLY A N   1 
ATOM   1630 C CA  . GLY B 1 67  ? -0.56500  -4.97600  -16.44000 1.000 12.96000 ? 67  GLY A CA  1 
ATOM   1631 C C   . GLY B 1 67  ? -2.00500  -4.88600  -16.90200 1.000 13.97000 ? 67  GLY A C   1 
ATOM   1632 O O   . GLY B 1 67  ? -2.22800  -4.57800  -18.07400 1.000 15.85000 ? 67  GLY A O   1 
ATOM   1633 N N   . VAL B 1 68  ? -2.97300  -5.15000  -16.03100 1.000 12.11000 ? 68  VAL A N   1 
ATOM   1634 C CA  . VAL B 1 68  ? -4.39700  -5.10500  -16.38400 1.000 12.51000 ? 68  VAL A CA  1 
ATOM   1635 C C   . VAL B 1 68  ? -5.08200  -4.01900  -15.55800 1.000 14.05000 ? 68  VAL A C   1 
ATOM   1636 O O   . VAL B 1 68  ? -5.13700  -4.10700  -14.32200 1.000 12.86000 ? 68  VAL A O   1 
ATOM   1637 C CB  . VAL B 1 68  ? -5.07900  -6.46900  -16.17800 1.000 15.92000 ? 68  VAL A CB  1 
ATOM   1638 C CG1 . VAL B 1 68  ? -6.54800  -6.40000  -16.57800 1.000 16.63000 ? 68  VAL A CG1 1 
ATOM   1639 C CG2 . VAL B 1 68  ? -4.36600  -7.55500  -16.97800 1.000 18.67000 ? 68  VAL A CG2 1 
ATOM   1640 N N   . GLU B 1 69  ? -5.59300  -3.00100  -16.20600 1.000 12.93000 ? 69  GLU A N   1 
ATOM   1641 C CA  . GLU B 1 69  ? -6.27400  -1.92200  -15.50300 1.000 14.06000 ? 69  GLU A CA  1 
ATOM   1642 C C   . GLU B 1 69  ? -7.51400  -2.44100  -14.78400 1.000 17.13000 ? 69  GLU A C   1 
ATOM   1643 O O   . GLU B 1 69  ? -8.14500  -3.32800  -15.23800 1.000 16.82000 ? 69  GLU A O   1 
ATOM   1644 C CB  . GLU B 1 69  ? -6.67900  -0.83400  -16.47400 1.000 17.00000 ? 69  GLU A CB  1 
ATOM   1645 C CG  . GLU B 1 69  ? -7.14000  0.45600   -15.83900 1.000 20.63000 ? 69  GLU A CG  1 
ATOM   1646 C CD  . GLU B 1 69  ? -7.05700  1.61600   -16.82000 1.000 34.25000 ? 69  GLU A CD  1 
ATOM   1647 O OE1 . GLU B 1 69  ? -7.82800  1.64300   -17.74100 1.000 42.50000 ? 69  GLU A OE1 1 
ATOM   1648 O OE2 . GLU B 1 69  ? -6.19500  2.46300   -16.69600 1.000 44.97000 ? 69  GLU A OE2 1 
ATOM   1649 N N   . PHE B 1 70  ? -7.80300  -1.85000  -13.64000 1.000 16.25000 ? 70  PHE A N   1 
ATOM   1650 C CA  . PHE B 1 70  ? -8.95700  -2.26500  -12.87300 1.000 16.49000 ? 70  PHE A CA  1 
ATOM   1651 C C   . PHE B 1 70  ? -9.62900  -1.13600  -12.14200 1.000 20.57000 ? 70  PHE A C   1 
ATOM   1652 O O   . PHE B 1 70  ? -9.03400  -0.19700  -11.81500 1.000 15.72000 ? 70  PHE A O   1 
ATOM   1653 C CB  . PHE B 1 70  ? -8.65100  -3.39700  -11.90800 1.000 19.66000 ? 70  PHE A CB  1 
ATOM   1654 C CG  . PHE B 1 70  ? -7.63400  -3.08700  -10.84600 1.000 20.35000 ? 70  PHE A CG  1 
ATOM   1655 C CD1 . PHE B 1 70  ? -6.30300  -3.12100  -11.13000 1.000 17.87000 ? 70  PHE A CD1 1 
ATOM   1656 C CD2 . PHE B 1 70  ? -8.00900  -2.85000  -9.54100  1.000 21.50000 ? 70  PHE A CD2 1 
ATOM   1657 C CE1 . PHE B 1 70  ? -5.36300  -2.87400  -10.18800 1.000 18.87000 ? 70  PHE A CE1 1 
ATOM   1658 C CE2 . PHE B 1 70  ? -7.05800  -2.61800  -8.59700  1.000 23.15000 ? 70  PHE A CE2 1 
ATOM   1659 C CZ  . PHE B 1 70  ? -5.73800  -2.63900  -8.91600  1.000 19.27000 ? 70  PHE A CZ  1 
ATOM   1660 N N   . ASP B 1 71  ? -10.92000 -1.29600  -11.92900 1.000 18.86000 ? 71  ASP A N   1 
ATOM   1661 C CA  . ASP B 1 71  ? -11.66200 -0.29400  -11.21800 1.000 24.08000 ? 71  ASP A CA  1 
ATOM   1662 C C   . ASP B 1 71  ? -11.53500 -0.55800  -9.75200  1.000 24.00000 ? 71  ASP A C   1 
ATOM   1663 O O   . ASP B 1 71  ? -11.69100 -1.62900  -9.32100  1.000 24.77000 ? 71  ASP A O   1 
ATOM   1664 C CB  . ASP B 1 71  ? -13.13000 -0.35000  -11.57300 1.000 20.73000 ? 71  ASP A CB  1 
ATOM   1665 C CG  . ASP B 1 71  ? -13.42700 0.24800   -12.87100 1.000 27.73000 ? 71  ASP A CG  1 
ATOM   1666 O OD1 . ASP B 1 71  ? -13.93900 -0.45100  -13.70300 1.000 39.97000 ? 71  ASP A OD1 1 
ATOM   1667 O OD2 . ASP B 1 71  ? -13.20200 1.39600   -13.10300 1.000 29.23000 ? 71  ASP A OD2 1 
ATOM   1668 N N   . GLU B 1 72  ? -11.29100 0.47900   -9.00400  1.000 21.64000 ? 72  GLU A N   1 
ATOM   1669 C CA  . GLU B 1 72  ? -11.13900 0.35600   -7.60600  1.000 22.29000 ? 72  GLU A CA  1 
ATOM   1670 C C   . GLU B 1 72  ? -12.00100 1.42300   -6.91500  1.000 21.64000 ? 72  GLU A C   1 
ATOM   1671 O O   . GLU B 1 72  ? -12.09000 2.47800   -7.40000  1.000 19.16000 ? 72  GLU A O   1 
ATOM   1672 C CB  . GLU B 1 72  ? -9.67700  0.53900   -7.30000  1.000 24.91000 ? 72  GLU A CB  1 
ATOM   1673 C CG  . GLU B 1 72  ? -9.31500  0.32500   -5.90200  1.000 31.81000 ? 72  GLU A CG  1 
ATOM   1674 C CD  . GLU B 1 72  ? -7.83700  0.32600   -5.71500  1.000 35.08000 ? 72  GLU A CD  1 
ATOM   1675 O OE1 . GLU B 1 72  ? -7.11900  0.90500   -6.52200  1.000 29.10000 ? 72  GLU A OE1 1 
ATOM   1676 O OE2 . GLU B 1 72  ? -7.42600  -0.20200  -4.70200  1.000 37.21000 ? 72  GLU A OE2 1 
ATOM   1677 N N   . TYR B 1 73  ? -12.65200 1.06700   -5.82200  1.000 20.22000 ? 73  TYR A N   1 
ATOM   1678 C CA  . TYR B 1 73  ? -13.47400 1.99500   -5.03900  1.000 20.04000 ? 73  TYR A CA  1 
ATOM   1679 C C   . TYR B 1 73  ? -12.90600 1.91500   -3.64100  1.000 22.46000 ? 73  TYR A C   1 
ATOM   1680 O O   . TYR B 1 73  ? -12.99600 0.94700   -3.00900  1.000 21.98000 ? 73  TYR A O   1 
ATOM   1681 C CB  . TYR B 1 73  ? -14.91100 1.56100   -5.07900  1.000 18.01000 ? 73  TYR A CB  1 
ATOM   1682 C CG  . TYR B 1 73  ? -15.47700 1.63700   -6.44900  1.000 22.12000 ? 73  TYR A CG  1 
ATOM   1683 C CD1 . TYR B 1 73  ? -15.43700 0.58400   -7.26400  1.000 25.21000 ? 73  TYR A CD1 1 
ATOM   1684 C CD2 . TYR B 1 73  ? -16.00100 2.79000   -6.91700  1.000 20.74000 ? 73  TYR A CD2 1 
ATOM   1685 C CE1 . TYR B 1 73  ? -15.93400 0.65900   -8.53500  1.000 22.76000 ? 73  TYR A CE1 1 
ATOM   1686 C CE2 . TYR B 1 73  ? -16.52200 2.86800   -8.17100  1.000 27.68000 ? 73  TYR A CE2 1 
ATOM   1687 C CZ  . TYR B 1 73  ? -16.46900 1.78400   -8.97300  1.000 21.90000 ? 73  TYR A CZ  1 
ATOM   1688 O OH  . TYR B 1 73  ? -16.95700 1.88500   -10.23600 1.000 36.38000 ? 73  TYR A OH  1 
ATOM   1689 N N   . THR B 1 74  ? -12.31200 2.99300   -3.20300  1.000 16.54000 ? 74  THR A N   1 
ATOM   1690 C CA  . THR B 1 74  ? -11.54800 2.97700   -1.96100  1.000 18.09000 ? 74  THR A CA  1 
ATOM   1691 C C   . THR B 1 74  ? -12.48200 3.14100   -0.76200  1.000 19.57000 ? 74  THR A C   1 
ATOM   1692 O O   . THR B 1 74  ? -12.35300 4.04900   0.05400   1.000 22.67000 ? 74  THR A O   1 
ATOM   1693 C CB  . THR B 1 74  ? -10.46800 4.04600   -2.01200  1.000 20.50000 ? 74  THR A CB  1 
ATOM   1694 O OG1 . THR B 1 74  ? -11.05800 5.31000   -2.33900  1.000 18.09000 ? 74  THR A OG1 1 
ATOM   1695 C CG2 . THR B 1 74  ? -9.45300  3.68300   -3.10400  1.000 19.18000 ? 74  THR A CG2 1 
ATOM   1696 N N   . LYS B 1 75  ? -13.43800 2.20700   -0.67000  1.000 22.58000 ? 75  LYS A N   1 
ATOM   1697 C CA  . LYS B 1 75  ? -14.55100 2.35400   0.26600   1.000 21.61000 ? 75  LYS A CA  1 
ATOM   1698 C C   . LYS B 1 75  ? -14.07200 2.52400   1.70200   1.000 26.78000 ? 75  LYS A C   1 
ATOM   1699 O O   . LYS B 1 75  ? -14.67900 3.27000   2.47900   1.000 29.07000 ? 75  LYS A O   1 
ATOM   1700 C CB  . LYS B 1 75  ? -15.47400 1.13300   0.18400   1.000 20.84000 ? 75  LYS A CB  1 
ATOM   1701 C CG  . LYS B 1 75  ? -16.03400 0.84400   -1.19200  1.000 22.57000 ? 75  LYS A CG  1 
ATOM   1702 C CD  . LYS B 1 75  ? -16.75000 2.06100   -1.81000  1.000 22.41000 ? 75  LYS A CD  1 
ATOM   1703 C CE  . LYS B 1 75  ? -18.02400 2.42500   -1.07000  1.000 16.21000 ? 75  LYS A CE  1 
ATOM   1704 N NZ  . LYS B 1 75  ? -18.61900 3.63500   -1.69800  1.000 18.61000 ? 75  LYS A NZ  1 
ATOM   1705 N N   . SER B 1 76  ? -13.01700 1.81800   2.07800   1.000 26.73000 ? 76  SER A N   1 
ATOM   1706 C CA  . SER B 1 76  ? -12.52000 1.88700   3.44800   1.000 34.90000 ? 76  SER A CA  1 
ATOM   1707 C C   . SER B 1 76  ? -11.49800 2.98500   3.68200   1.000 32.53000 ? 76  SER A C   1 
ATOM   1708 O O   . SER B 1 76  ? -10.93200 3.07700   4.75800   1.000 38.14000 ? 76  SER A O   1 
ATOM   1709 C CB  . SER B 1 76  ? -11.94000 0.53800   3.88500   1.000 33.26000 ? 76  SER A CB  1 
ATOM   1710 O OG  . SER B 1 76  ? -11.07100 0.01700   2.90600   1.000 43.84000 ? 76  SER A OG  1 
ATOM   1711 N N   . LEU B 1 77  ? -11.27900 3.82100   2.67700   1.000 30.56000 ? 77  LEU A N   1 
ATOM   1712 C CA  . LEU B 1 77  ? -10.32000 4.90800   2.77400   1.000 21.34000 ? 77  LEU A CA  1 
ATOM   1713 C C   . LEU B 1 77  ? -10.99000 6.25100   2.45600   1.000 26.15000 ? 77  LEU A C   1 
ATOM   1714 O O   . LEU B 1 77  ? -11.79900 6.73800   3.23900   1.000 30.87000 ? 77  LEU A O   1 
ATOM   1715 C CB  . LEU B 1 77  ? -9.14500  4.63900   1.83700   1.000 29.21000 ? 77  LEU A CB  1 
ATOM   1716 C CG  . LEU B 1 77  ? -7.81900  5.38000   1.98900   1.000 32.23000 ? 77  LEU A CG  1 
ATOM   1717 C CD1 . LEU B 1 77  ? -7.17600  5.09800   3.33600   1.000 33.85000 ? 77  LEU A CD1 1 
ATOM   1718 C CD2 . LEU B 1 77  ? -6.88300  4.96300   0.87100   1.000 28.03000 ? 77  LEU A CD2 1 
ATOM   1719 N N   . ASP B 1 78  ? -10.66500 6.83900   1.30800   1.000 21.35000 ? 78  ASP A N   1 
ATOM   1720 C CA  . ASP B 1 78  ? -11.25700 8.12000   0.92600   1.000 19.71000 ? 78  ASP A CA  1 
ATOM   1721 C C   . ASP B 1 78  ? -12.55300 7.98200   0.12400   1.000 16.15000 ? 78  ASP A C   1 
ATOM   1722 O O   . ASP B 1 78  ? -13.13900 8.97300   -0.26100  1.000 20.96000 ? 78  ASP A O   1 
ATOM   1723 C CB  . ASP B 1 78  ? -10.26200 9.01000   0.19300   1.000 19.20000 ? 78  ASP A CB  1 
ATOM   1724 C CG  . ASP B 1 78  ? -9.77500  8.39300   -1.08400  1.000 17.90000 ? 78  ASP A CG  1 
ATOM   1725 O OD1 . ASP B 1 78  ? -9.49500  7.19100   -1.06700  1.000 18.63000 ? 78  ASP A OD1 1 
ATOM   1726 O OD2 . ASP B 1 78  ? -9.67500  9.10800   -2.08800  1.000 19.41000 ? 78  ASP A OD2 1 
ATOM   1727 N N   . ASN B 1 79  ? -12.95100 6.74700   -0.16400  1.000 18.62000 ? 79  ASN A N   1 
ATOM   1728 C CA  . ASN B 1 79  ? -14.23800 6.48600   -0.82300  1.000 18.01000 ? 79  ASN A CA  1 
ATOM   1729 C C   . ASN B 1 79  ? -14.33500 7.17100   -2.18700  1.000 18.84000 ? 79  ASN A C   1 
ATOM   1730 O O   . ASN B 1 79  ? -15.28900 7.90100   -2.48300  1.000 20.06000 ? 79  ASN A O   1 
ATOM   1731 C CB  . ASN B 1 79  ? -15.41500 6.89800   0.06900   1.000 18.56000 ? 79  ASN A CB  1 
ATOM   1732 C CG  . ASN B 1 79  ? -16.74200 6.41000   -0.48400  1.000 22.71000 ? 79  ASN A CG  1 
ATOM   1733 O OD1 . ASN B 1 79  ? -16.79100 5.39500   -1.17900  1.000 22.01000 ? 79  ASN A OD1 1 
ATOM   1734 N ND2 . ASN B 1 79  ? -17.82200 7.13400   -0.18600  1.000 27.63000 ? 79  ASN A ND2 1 
ATOM   1735 N N   . ARG B 1 80  ? -13.35000 6.90900   -3.03600  1.000 18.00000 ? 80  ARG A N   1 
ATOM   1736 C CA  . ARG B 1 80  ? -13.30500 7.44100   -4.39000  1.000 17.23000 ? 80  ARG A CA  1 
ATOM   1737 C C   . ARG B 1 80  ? -13.20600 6.30400   -5.39400  1.000 14.98000 ? 80  ARG A C   1 
ATOM   1738 O O   . ARG B 1 80  ? -12.75900 5.19900   -5.07800  1.000 17.78000 ? 80  ARG A O   1 
ATOM   1739 C CB  . ARG B 1 80  ? -12.11400 8.39500   -4.58600  1.000 17.63000 ? 80  ARG A CB  1 
ATOM   1740 C CG  . ARG B 1 80  ? -12.26900 9.72400   -3.84300  1.000 19.62000 ? 80  ARG A CG  1 
ATOM   1741 C CD  . ARG B 1 80  ? -11.24800 10.72300  -4.33900  1.000 20.00000 ? 80  ARG A CD  1 
ATOM   1742 N NE  . ARG B 1 80  ? -11.51200 12.08300  -3.85400  1.000 24.29000 ? 80  ARG A NE  1 
ATOM   1743 C CZ  . ARG B 1 80  ? -11.01900 12.59700  -2.73200  1.000 28.67000 ? 80  ARG A CZ  1 
ATOM   1744 N NH1 . ARG B 1 80  ? -10.21900 11.87700  -1.94100  1.000 25.64000 ? 80  ARG A NH1 1 
ATOM   1745 N NH2 . ARG B 1 80  ? -11.32000 13.84400  -2.39800  1.000 28.32000 ? 80  ARG A NH2 1 
ATOM   1746 N N   . HIS B 1 81  ? -13.63800 6.59500   -6.61600  1.000 16.57000 ? 81  HIS A N   1 
ATOM   1747 C CA  . HIS B 1 81  ? -13.46100 5.69700   -7.75100  1.000 18.05000 ? 81  HIS A CA  1 
ATOM   1748 C C   . HIS B 1 81  ? -12.16700 6.06300   -8.47300  1.000 20.02000 ? 81  HIS A C   1 
ATOM   1749 O O   . HIS B 1 81  ? -11.97500 7.22100   -8.85900  1.000 17.74000 ? 81  HIS A O   1 
ATOM   1750 C CB  . HIS B 1 81  ? -14.66100 5.81800   -8.69400  1.000 19.15000 ? 81  HIS A CB  1 
ATOM   1751 C CG  . HIS B 1 81  ? -14.55900 4.97000   -9.92000  1.000 23.41000 ? 81  HIS A CG  1 
ATOM   1752 N ND1 . HIS B 1 81  ? -15.20400 5.28600   -11.09600 1.000 32.34000 ? 81  HIS A ND1 1 
ATOM   1753 C CD2 . HIS B 1 81  ? -13.90200 3.80900   -10.14900 1.000 20.54000 ? 81  HIS A CD2 1 
ATOM   1754 C CE1 . HIS B 1 81  ? -14.94300 4.35900   -12.00100 1.000 34.48000 ? 81  HIS A CE1 1 
ATOM   1755 N NE2 . HIS B 1 81  ? -14.15000 3.45500   -11.45400 1.000 28.71000 ? 81  HIS A NE2 1 
ATOM   1756 N N   . VAL B 1 82  ? -11.26100 5.09200   -8.62100  1.000 15.56000 ? 82  VAL A N   1 
ATOM   1757 C CA  . VAL B 1 82  ? -10.04500 5.30000   -9.39500  1.000 16.45000 ? 82  VAL A CA  1 
ATOM   1758 C C   . VAL B 1 82  ? -9.89100  4.15600   -10.38700 1.000 16.77000 ? 82  VAL A C   1 
ATOM   1759 O O   . VAL B 1 82  ? -10.45600 3.07200   -10.22600 1.000 17.24000 ? 82  VAL A O   1 
ATOM   1760 C CB  . VAL B 1 82  ? -8.78100  5.41800   -8.50800  1.000 16.66000 ? 82  VAL A CB  1 
ATOM   1761 C CG1 . VAL B 1 82  ? -8.85200  6.66000   -7.63700  1.000 17.32000 ? 82  VAL A CG1 1 
ATOM   1762 C CG2 . VAL B 1 82  ? -8.57700  4.16800   -7.66400  1.000 17.91000 ? 82  VAL A CG2 1 
ATOM   1763 N N   . LYS B 1 83  ? -9.11900  4.41900   -11.44300 1.000 17.16000 ? 83  LYS A N   1 
ATOM   1764 C CA  . LYS B 1 83  ? -8.72900  3.39300   -12.39400 1.000 16.46000 ? 83  LYS A CA  1 
ATOM   1765 C C   . LYS B 1 83  ? -7.28000  3.04800   -12.07400 1.000 13.19000 ? 83  LYS A C   1 
ATOM   1766 O O   . LYS B 1 83  ? -6.40300  3.89600   -12.20300 1.000 18.18000 ? 83  LYS A O   1 
ATOM   1767 C CB  . LYS B 1 83  ? -8.88500  3.88800   -13.83200 1.000 18.84000 ? 83  LYS A CB  1 
ATOM   1768 C CG  . LYS B 1 83  ? -10.31100 4.24700   -14.20900 1.000 24.38000 ? 83  LYS A CG  1 
ATOM   1769 C CD  . LYS B 1 83  ? -11.09900 3.00500   -14.52700 1.000 28.64000 ? 83  LYS A CD  1 
ATOM   1770 C CE  . LYS B 1 83  ? -12.41000 3.32500   -15.25400 1.000 28.44000 ? 83  LYS A CE  1 
ATOM   1771 N NZ  . LYS B 1 83  ? -13.18000 2.07100   -15.45700 1.000 30.46000 ? 83  LYS A NZ  1 
ATOM   1772 N N   . ALA B 1 84  ? -7.05100  1.83200   -11.60600 1.000 12.86000 ? 84  ALA A N   1 
ATOM   1773 C CA  . ALA B 1 84  ? -5.76200  1.45700   -11.04400 1.000 14.41000 ? 84  ALA A CA  1 
ATOM   1774 C C   . ALA B 1 84  ? -5.01800  0.56900   -12.02400 1.000 14.28000 ? 84  ALA A C   1 
ATOM   1775 O O   . ALA B 1 84  ? -5.61800  -0.19700  -12.77800 1.000 15.09000 ? 84  ALA A O   1 
ATOM   1776 C CB  . ALA B 1 84  ? -5.91500  0.72800   -9.70700  1.000 14.11000 ? 84  ALA A CB  1 
ATOM   1777 N N   . LEU B 1 85  ? -3.69300  0.67300   -11.99900 1.000 12.29000 ? 85  LEU A N   1 
ATOM   1778 C CA  . LEU B 1 85  ? -2.86400  -0.13000  -12.88900 1.000 12.51000 ? 85  LEU A CA  1 
ATOM   1779 C C   . LEU B 1 85  ? -1.57500  -0.42100  -12.14700 1.000 10.34000 ? 85  LEU A C   1 
ATOM   1780 O O   . LEU B 1 85  ? -0.93700  0.52600   -11.68300 1.000 14.25000 ? 85  LEU A O   1 
ATOM   1781 C CB  . LEU B 1 85  ? -2.57700  0.62700   -14.18200 1.000 13.16000 ? 85  LEU A CB  1 
ATOM   1782 C CG  . LEU B 1 85  ? -1.59500  -0.04400  -15.13800 1.000 17.90000 ? 85  LEU A CG  1 
ATOM   1783 C CD1 . LEU B 1 85  ? -2.21600  -1.30300  -15.74500 1.000 18.16000 ? 85  LEU A CD1 1 
ATOM   1784 C CD2 . LEU B 1 85  ? -1.20900  0.93500   -16.23000 1.000 23.23000 ? 85  LEU A CD2 1 
ATOM   1785 N N   . VAL B 1 86  ? -1.22900  -1.70100  -11.99500 1.000 10.07000 ? 86  VAL A N   1 
ATOM   1786 C CA  . VAL B 1 86  ? 0.01800   -2.10800  -11.33000 1.000 10.85000 ? 86  VAL A CA  1 
ATOM   1787 C C   . VAL B 1 86  ? 0.95700   -2.69700  -12.37800 1.000 12.54000 ? 86  VAL A C   1 
ATOM   1788 O O   . VAL B 1 86  ? 0.55900   -3.57100  -13.16000 1.000 13.51000 ? 86  VAL A O   1 
ATOM   1789 C CB  . VAL B 1 86  ? -0.23100  -3.11300  -10.19500 1.000 13.19000 ? 86  VAL A CB  1 
ATOM   1790 C CG1 . VAL B 1 86  ? 1.10000   -3.43800  -9.48800  1.000 15.31000 ? 86  VAL A CG1 1 
ATOM   1791 C CG2 . VAL B 1 86  ? -1.22800  -2.55500  -9.17400  1.000 13.92000 ? 86  VAL A CG2 1 
ATOM   1792 N N   . THR B 1 87  ? 2.20800   -2.23900  -12.38400 1.000 11.24000 ? 87  THR A N   1 
ATOM   1793 C CA  . THR B 1 87  ? 3.18600   -2.67700  -13.37800 1.000 10.27000 ? 87  THR A CA  1 
ATOM   1794 C C   . THR B 1 87  ? 4.54100   -2.86300  -12.71200 1.000 10.02000 ? 87  THR A C   1 
ATOM   1795 O O   . THR B 1 87  ? 4.77200   -2.43100  -11.57800 1.000 14.23000 ? 87  THR A O   1 
ATOM   1796 C CB  . THR B 1 87  ? 3.33500   -1.67900  -14.52200 1.000 13.69000 ? 87  THR A CB  1 
ATOM   1797 O OG1 . THR B 1 87  ? 3.64400   -0.38800  -13.98800 1.000 17.12000 ? 87  THR A OG1 1 
ATOM   1798 C CG2 . THR B 1 87  ? 2.03400   -1.58600  -15.33000 1.000 14.73000 ? 87  THR A CG2 1 
ATOM   1799 N N   . TRP B 1 88  ? 5.43900   -3.52500  -13.43200 1.000 12.30000 ? 88  TRP A N   1 
ATOM   1800 C CA  . TRP B 1 88  ? 6.82300   -3.68100  -13.01000 1.000 13.01000 ? 88  TRP A CA  1 
ATOM   1801 C C   . TRP B 1 88  ? 7.69500   -2.65800  -13.71400 1.000 15.58000 ? 88  TRP A C   1 
ATOM   1802 O O   . TRP B 1 88  ? 7.68600   -2.53500  -14.95300 1.000 15.17000 ? 88  TRP A O   1 
ATOM   1803 C CB  . TRP B 1 88  ? 7.36300   -5.08000  -13.29600 1.000 13.38000 ? 88  TRP A CB  1 
ATOM   1804 C CG  . TRP B 1 88  ? 6.83900   -6.15600  -12.41200 1.000 14.51000 ? 88  TRP A CG  1 
ATOM   1805 C CD1 . TRP B 1 88  ? 5.96100   -7.15300  -12.76300 1.000 19.40000 ? 88  TRP A CD1 1 
ATOM   1806 C CD2 . TRP B 1 88  ? 7.16000   -6.36800  -11.03400 1.000 16.19000 ? 88  TRP A CD2 1 
ATOM   1807 N NE1 . TRP B 1 88  ? 5.72300   -7.96800  -11.67500 1.000 23.85000 ? 88  TRP A NE1 1 
ATOM   1808 C CE2 . TRP B 1 88  ? 6.45000   -7.51000  -10.60900 1.000 17.85000 ? 88  TRP A CE2 1 
ATOM   1809 C CE3 . TRP B 1 88  ? 7.99400   -5.71400  -10.12900 1.000 16.16000 ? 88  TRP A CE3 1 
ATOM   1810 C CZ2 . TRP B 1 88  ? 6.53200   -7.99900  -9.30100  1.000 21.68000 ? 88  TRP A CZ2 1 
ATOM   1811 C CZ3 . TRP B 1 88  ? 8.07600   -6.20400  -8.82300  1.000 24.39000 ? 88  TRP A CZ3 1 
ATOM   1812 C CH2 . TRP B 1 88  ? 7.34800   -7.33600  -8.43200  1.000 21.79000 ? 88  TRP A CH2 1 
ATOM   1813 N N   . GLU B 1 89  ? 8.48900   -1.91600  -12.94800 1.000 14.92000 ? 89  GLU A N   1 
ATOM   1814 C CA  . GLU B 1 89  ? 9.45500   -0.95500  -13.49200 1.000 18.60000 ? 89  GLU A CA  1 
ATOM   1815 C C   . GLU B 1 89  ? 10.74400  -1.53700  -12.94400 1.000 16.84000 ? 89  GLU A C   1 
ATOM   1816 O O   . GLU B 1 89  ? 11.16600  -1.20100  -11.85600 1.000 21.14000 ? 89  GLU A O   1 
ATOM   1817 C CB  . GLU B 1 89  ? 9.20500   0.44500   -12.95500 1.000 21.25000 ? 89  GLU A CB  1 
ATOM   1818 C CG  . GLU B 1 89  ? 8.07000   1.15100   -13.65400 1.000 29.93000 ? 89  GLU A CG  1 
ATOM   1819 C CD  . GLU B 1 89  ? 7.88800   2.58600   -13.19800 1.000 43.69000 ? 89  GLU A CD  1 
ATOM   1820 O OE1 . GLU B 1 89  ? 6.88200   3.18700   -13.59500 1.000 42.25000 ? 89  GLU A OE1 1 
ATOM   1821 O OE2 . GLU B 1 89  ? 8.74000   3.11100   -12.45300 1.000 43.19000 ? 89  GLU A OE2 1 
ATOM   1822 N N   . GLY B 1 90  ? 11.37800  -2.39500  -13.72700 1.000 21.19000 ? 90  GLY A N   1 
ATOM   1823 C CA  . GLY B 1 90  ? 12.48800  -3.18700  -13.20100 1.000 26.23000 ? 90  GLY A CA  1 
ATOM   1824 C C   . GLY B 1 90  ? 11.97500  -4.12300  -12.11600 1.000 22.33000 ? 90  GLY A C   1 
ATOM   1825 O O   . GLY B 1 90  ? 11.05500  -4.91800  -12.34300 1.000 22.96000 ? 90  GLY A O   1 
ATOM   1826 N N   . ASP B 1 91  ? 12.55400  -4.04700  -10.91500 1.000 22.75000 ? 91  ASP A N   1 
ATOM   1827 C CA  . ASP B 1 91  ? 12.07900  -4.85300  -9.79900  1.000 21.30000 ? 91  ASP A CA  1 
ATOM   1828 C C   . ASP B 1 91  ? 11.17200  -4.06600  -8.85000  1.000 21.02000 ? 91  ASP A C   1 
ATOM   1829 O O   . ASP B 1 91  ? 10.83000  -4.57700  -7.77800  1.000 24.82000 ? 91  ASP A O   1 
ATOM   1830 C CB  . ASP B 1 91  ? 13.25900  -5.43100  -9.01400  1.000 24.65000 ? 91  ASP A CB  1 
ATOM   1831 C CG  . ASP B 1 91  ? 13.62700  -6.83800  -9.45500  1.000 36.87000 ? 91  ASP A CG  1 
ATOM   1832 O OD1 . ASP B 1 91  ? 14.14200  -7.61000  -8.61500  1.000 46.96000 ? 91  ASP A OD1 1 
ATOM   1833 O OD2 . ASP B 1 91  ? 13.40600  -7.17500  -10.63600 1.000 33.28000 ? 91  ASP A OD2 1 
ATOM   1834 N N   . VAL B 1 92  ? 10.79900  -2.82800  -9.21300  1.000 16.70000 ? 92  VAL A N   1 
ATOM   1835 C CA  . VAL B 1 92  ? 9.86900   -2.01300  -8.43200  1.000 13.65000 ? 92  VAL A CA  1 
ATOM   1836 C C   . VAL B 1 92  ? 8.44300   -2.27200  -8.90000  1.000 13.20000 ? 92  VAL A C   1 
ATOM   1837 O O   . VAL B 1 92  ? 8.14800   -2.19400  -10.10100 1.000 14.21000 ? 92  VAL A O   1 
ATOM   1838 C CB  . VAL B 1 92  ? 10.19900  -0.51700  -8.56300  1.000 15.85000 ? 92  VAL A CB  1 
ATOM   1839 C CG1 . VAL B 1 92  ? 9.37500   0.30400   -7.58300  1.000 14.73000 ? 92  VAL A CG1 1 
ATOM   1840 C CG2 . VAL B 1 92  ? 11.69900  -0.27900  -8.33400  1.000 18.87000 ? 92  VAL A CG2 1 
ATOM   1841 N N   . LEU B 1 93  ? 7.55300   -2.54800  -7.95800  1.000 12.30000 ? 93  LEU A N   1 
ATOM   1842 C CA  . LEU B 1 93  ? 6.14300   -2.73500  -8.26900  1.000 10.68000 ? 93  LEU A CA  1 
ATOM   1843 C C   . LEU B 1 93  ? 5.45000   -1.39100  -8.10500  1.000 11.86000 ? 93  LEU A C   1 
ATOM   1844 O O   . LEU B 1 93  ? 5.49200   -0.78700  -7.02300  1.000 12.88000 ? 93  LEU A O   1 
ATOM   1845 C CB  . LEU B 1 93  ? 5.52300   -3.80400  -7.37300  1.000 14.42000 ? 93  LEU A CB  1 
ATOM   1846 C CG  . LEU B 1 93  ? 4.14700   -4.31900  -7.79900  1.000 15.49000 ? 93  LEU A CG  1 
ATOM   1847 C CD1 . LEU B 1 93  ? 4.20400   -5.05500  -9.13700  1.000 12.40000 ? 93  LEU A CD1 1 
ATOM   1848 C CD2 . LEU B 1 93  ? 3.57800   -5.21500  -6.69500  1.000 15.88000 ? 93  LEU A CD2 1 
ATOM   1849 N N   . VAL B 1 94  ? 4.82200   -0.92500  -9.17600  1.000 10.98000 ? 94  VAL A N   1 
ATOM   1850 C CA  . VAL B 1 94  ? 4.35200   0.44700   -9.27100  1.000 10.78000 ? 94  VAL A CA  1 
ATOM   1851 C C   . VAL B 1 94  ? 2.85600   0.44600   -9.54600  1.000 11.29000 ? 94  VAL A C   1 
ATOM   1852 O O   . VAL B 1 94  ? 2.39700   -0.19600  -10.49400 1.000 12.67000 ? 94  VAL A O   1 
ATOM   1853 C CB  . VAL B 1 94  ? 5.09000   1.21300   -10.37500 1.000 14.94000 ? 94  VAL A CB  1 
ATOM   1854 C CG1 . VAL B 1 94  ? 4.52000   2.62700   -10.50900 1.000 16.27000 ? 94  VAL A CG1 1 
ATOM   1855 C CG2 . VAL B 1 94  ? 6.62200   1.22500   -10.08200 1.000 12.95000 ? 94  VAL A CG2 1 
ATOM   1856 N N   . CYS B 1 95  ? 2.10700   1.19500   -8.74100  1.000 11.25000 ? 95  CYS A N   1 
ATOM   1857 C CA  . CYS B 1 95  ? 0.67500   1.37500   -8.91800  1.000 11.30000 ? 95  CYS A CA  1 
ATOM   1858 C C   . CYS B 1 95  ? 0.35400   2.83700   -9.18700  1.000 12.83000 ? 95  CYS A C   1 
ATOM   1859 O O   . CYS B 1 95  ? 0.78200   3.71300   -8.43800  1.000 14.39000 ? 95  CYS A O   1 
ATOM   1860 C CB  . CYS B 1 95  ? -0.06200  0.92800   -7.67300  1.000 10.74000 ? 95  CYS A CB  1 
ATOM   1861 S SG  . CYS B 1 95  ? -1.90100  1.07600   -7.87900  1.000 16.01000 ? 95  CYS A SG  1 
ATOM   1862 N N   . VAL B 1 96  ? -0.38400  3.10300   -10.26500 1.000 11.69000 ? 96  VAL A N   1 
ATOM   1863 C CA  A VAL B 1 96  ? -0.92200  4.42900   -10.53400 0.330 15.53000 ? 96  VAL A CA  1 
ATOM   1864 C CA  B VAL B 1 96  ? -0.92100  4.42800   -10.54600 0.670 15.55000 ? 96  VAL A CA  1 
ATOM   1865 C C   . VAL B 1 96  ? -2.43300  4.33200   -10.42500 1.000 11.99000 ? 96  VAL A C   1 
ATOM   1866 O O   . VAL B 1 96  ? -3.04300  3.41300   -10.97900 1.000 14.96000 ? 96  VAL A O   1 
ATOM   1867 C CB  A VAL B 1 96  ? -0.49800  4.96300   -11.91500 0.330 16.44000 ? 96  VAL A CB  1 
ATOM   1868 C CB  B VAL B 1 96  ? -0.51700  4.92700   -11.94600 0.670 16.41000 ? 96  VAL A CB  1 
ATOM   1869 C CG1 A VAL B 1 96  ? 0.92200   5.50900   -11.85900 0.330 19.40000 ? 96  VAL A CG1 1 
ATOM   1870 C CG1 B VAL B 1 96  ? -1.07700  6.32800   -12.19900 0.670 15.72000 ? 96  VAL A CG1 1 
ATOM   1871 C CG2 A VAL B 1 96  ? -0.62700  3.88400   -12.96800 0.330 18.47000 ? 96  VAL A CG2 1 
ATOM   1872 C CG2 B VAL B 1 96  ? 0.98800   4.92400   -12.08700 0.670 21.11000 ? 96  VAL A CG2 1 
ATOM   1873 N N   . GLN B 1 97  ? -3.02700  5.25700   -9.68300  1.000 13.79000 ? 97  GLN A N   1 
ATOM   1874 C CA  . GLN B 1 97  ? -4.47800  5.28200   -9.48900  1.000 14.85000 ? 97  GLN A CA  1 
ATOM   1875 C C   . GLN B 1 97  ? -4.99100  6.57100   -10.11600 1.000 14.18000 ? 97  GLN A C   1 
ATOM   1876 O O   . GLN B 1 97  ? -4.85600  7.64400   -9.52800  1.000 17.31000 ? 97  GLN A O   1 
ATOM   1877 C CB  . GLN B 1 97  ? -4.82000  5.19500   -8.01100  1.000 15.14000 ? 97  GLN A CB  1 
ATOM   1878 C CG  . GLN B 1 97  ? -4.55800  3.82100   -7.41700  1.000 15.22000 ? 97  GLN A CG  1 
ATOM   1879 C CD  . GLN B 1 97  ? -4.59700  3.85000   -5.91400  1.000 25.60000 ? 97  GLN A CD  1 
ATOM   1880 O OE1 . GLN B 1 97  ? -4.06500  4.76600   -5.30300  1.000 23.79000 ? 97  GLN A OE1 1 
ATOM   1881 N NE2 . GLN B 1 97  ? -5.25100  2.86600   -5.31000  1.000 26.63000 ? 97  GLN A NE2 1 
ATOM   1882 N N   . LYS B 1 98  ? -5.56700  6.45400   -11.31600 1.000 19.22000 ? 98  LYS A N   1 
ATOM   1883 C CA  . LYS B 1 98  ? -6.00700  7.62100   -12.06500 1.000 20.94000 ? 98  LYS A CA  1 
ATOM   1884 C C   . LYS B 1 98  ? -7.39000  8.04500   -11.58600 1.000 19.16000 ? 98  LYS A C   1 
ATOM   1885 O O   . LYS B 1 98  ? -8.27800  7.20500   -11.41800 1.000 20.58000 ? 98  LYS A O   1 
ATOM   1886 C CB  . LYS B 1 98  ? -6.03400  7.30500   -13.55800 1.000 22.23000 ? 98  LYS A CB  1 
ATOM   1887 C CG  . LYS B 1 98  ? -4.65600  7.27600   -14.18300 1.000 30.46000 ? 98  LYS A CG  1 
ATOM   1888 C CD  . LYS B 1 98  ? -4.71500  7.00700   -15.67300 1.000 36.18000 ? 98  LYS A CD  1 
ATOM   1889 C CE  . LYS B 1 98  ? -3.42600  7.45500   -16.33700 1.000 44.91000 ? 98  LYS A CE  1 
ATOM   1890 N NZ  . LYS B 1 98  ? -2.44800  6.33700   -16.38400 1.000 55.01000 ? 98  LYS A NZ  1 
ATOM   1891 N N   . GLY B 1 99  ? -7.57000  9.34300   -11.36600 1.000 20.21000 ? 99  GLY A N   1 
ATOM   1892 C CA  . GLY B 1 99  ? -8.84500  9.86400   -10.90800 1.000 23.15000 ? 99  GLY A CA  1 
ATOM   1893 C C   . GLY B 1 99  ? -8.79500  11.34200  -10.57700 1.000 28.96000 ? 99  GLY A C   1 
ATOM   1894 O O   . GLY B 1 99  ? -8.19400  12.13200  -11.30600 1.000 34.93000 ? 99  GLY A O   1 
ATOM   1895 N N   . GLU B 1 100 ? -9.43800  11.71100  -9.46400  1.000 25.07000 ? 100 GLU A N   1 
ATOM   1896 C CA  . GLU B 1 100 ? -9.48200  13.12700  -9.00800  1.000 26.89000 ? 100 GLU A CA  1 
ATOM   1897 C C   . GLU B 1 100 ? -8.12200  13.51200  -8.41500  1.000 30.33000 ? 100 GLU A C   1 
ATOM   1898 O O   . GLU B 1 100 ? -7.55000  14.52700  -8.86000  1.000 28.68000 ? 100 GLU A O   1 
ATOM   1899 C CB  . GLU B 1 100 ? -10.60300 13.32200  -7.98500  1.000 27.66000 ? 100 GLU A CB  1 
ATOM   1900 C CG  . GLU B 1 100 ? -10.54200 14.66000  -7.27000  1.000 37.28000 ? 100 GLU A CG  1 
ATOM   1901 C CD  . GLU B 1 100 ? -10.80900 15.86500  -8.15500  1.000 40.71000 ? 100 GLU A CD  1 
ATOM   1902 O OE1 . GLU B 1 100 ? -10.42700 16.98400  -7.75900  1.000 35.85000 ? 100 GLU A OE1 1 
ATOM   1903 O OE2 . GLU B 1 100 ? -11.39800 15.68100  -9.23900  1.000 37.43000 ? 100 GLU A OE2 1 
ATOM   1904 N N   . LYS B 1 101 ? -7.63300  12.72600  -7.45000  1.000 26.90000 ? 101 LYS A N   1 
ATOM   1905 C CA  . LYS B 1 101 ? -6.32500  12.99700  -6.79600  1.000 27.69000 ? 101 LYS A CA  1 
ATOM   1906 C C   . LYS B 1 101 ? -5.20700  12.91000  -7.84200  1.000 24.58000 ? 101 LYS A C   1 
ATOM   1907 O O   . LYS B 1 101 ? -5.28300  12.02300  -8.71600  1.000 29.51000 ? 101 LYS A O   1 
ATOM   1908 C CB  . LYS B 1 101 ? -6.08600  12.00600  -5.65200  1.000 23.30000 ? 101 LYS A CB  1 
ATOM   1909 C CG  . LYS B 1 101 ? -6.67800  12.40800  -4.30800  1.000 26.37000 ? 101 LYS A CG  1 
ATOM   1910 C CD  . LYS B 1 101 ? -6.68700  13.90500  -4.08200  1.000 28.87000 ? 101 LYS A CD  1 
ATOM   1911 C CE  . LYS B 1 101 ? -7.71100  14.34600  -3.05800  1.000 32.70000 ? 101 LYS A CE  1 
ATOM   1912 N NZ  . LYS B 1 101 ? -7.47000  15.73600  -2.60300  1.000 38.19000 ? 101 LYS A NZ  1 
ATOM   1913 N N   . GLU B 1 102 ? -4.21400  13.80100  -7.74700  1.000 24.14000 ? 102 GLU A N   1 
ATOM   1914 C CA  . GLU B 1 102 ? -3.07400  13.82000  -8.70200  1.000 30.46000 ? 102 GLU A CA  1 
ATOM   1915 C C   . GLU B 1 102 ? -1.90500  13.02300  -8.11100  1.000 29.97000 ? 102 GLU A C   1 
ATOM   1916 O O   . GLU B 1 102 ? -1.62500  13.23000  -6.91400  1.000 24.29000 ? 102 GLU A O   1 
ATOM   1917 C CB  . GLU B 1 102 ? -2.65500  15.26100  -9.00000  1.000 35.60000 ? 102 GLU A CB  1 
ATOM   1918 C CG  . GLU B 1 102 ? -2.67300  15.60300  -10.47900 1.000 40.02000 ? 102 GLU A CG  1 
ATOM   1919 C CD  . GLU B 1 102 ? -2.09100  16.96400  -10.82000 1.000 44.83000 ? 102 GLU A CD  1 
ATOM   1920 O OE1 . GLU B 1 102 ? -2.39700  17.48000  -11.91300 1.000 54.91000 ? 102 GLU A OE1 1 
ATOM   1921 O OE2 . GLU B 1 102 ? -1.33300  17.50500  -9.99000  1.000 42.90000 ? 102 GLU A OE2 1 
ATOM   1922 N N   A ASN B 1 103 ? -1.03800  12.51700  -8.99400  0.510 24.26000 ? 103 ASN A N   1 
ATOM   1923 N N   B ASN B 1 103 ? -1.03800  12.51700  -8.99400  0.490 24.05000 ? 103 ASN A N   1 
ATOM   1924 C CA  A ASN B 1 103 ? 0.14600   11.72000  -8.57200  0.510 25.51000 ? 103 ASN A CA  1 
ATOM   1925 C CA  B ASN B 1 103 ? 0.14600   11.72000  -8.57200  0.490 25.47000 ? 103 ASN A CA  1 
ATOM   1926 C C   A ASN B 1 103 ? -0.25700  10.77900  -7.43100  0.510 23.32000 ? 103 ASN A C   1 
ATOM   1927 C C   B ASN B 1 103 ? -0.25800  10.78000  -7.43100  0.490 23.31000 ? 103 ASN A C   1 
ATOM   1928 O O   A ASN B 1 103 ? 0.60800   10.52800  -6.56900  0.510 22.15000 ? 103 ASN A O   1 
ATOM   1929 O O   B ASN B 1 103 ? 0.60600   10.53000  -6.56700  0.490 22.14000 ? 103 ASN A O   1 
ATOM   1930 C CB  A ASN B 1 103 ? 1.32000   12.61800  -8.17100  0.510 26.78000 ? 103 ASN A CB  1 
ATOM   1931 C CB  B ASN B 1 103 ? 1.32100   12.61800  -8.17400  0.490 26.76000 ? 103 ASN A CB  1 
ATOM   1932 C CG  A ASN B 1 103 ? 2.58500   11.84000  -7.87600  0.510 27.27000 ? 103 ASN A CG  1 
ATOM   1933 C CG  B ASN B 1 103 ? 1.61000   13.69900  -9.19300  0.490 25.60000 ? 103 ASN A CG  1 
ATOM   1934 O OD1 A ASN B 1 103 ? 2.96000   10.94500  -8.63000  0.510 27.15000 ? 103 ASN A OD1 1 
ATOM   1935 O OD1 B ASN B 1 103 ? 1.43600   13.49200  -10.39200 0.490 34.22000 ? 103 ASN A OD1 1 
ATOM   1936 N ND2 A ASN B 1 103 ? 3.24900   12.17400  -6.78100  0.510 25.99000 ? 103 ASN A ND2 1 
ATOM   1937 N ND2 B ASN B 1 103 ? 2.05300   14.85600  -8.72700  0.490 31.10000 ? 103 ASN A ND2 1 
ATOM   1938 N N   . ARG B 1 104 ? -1.31400  9.99500   -7.66600  1.000 18.48000 ? 104 ARG A N   1 
ATOM   1939 C CA  . ARG B 1 104 ? -1.81200  9.05000   -6.67400  1.000 14.05000 ? 104 ARG A CA  1 
ATOM   1940 C C   . ARG B 1 104 ? -1.40300  7.62200   -7.02000  1.000 14.05000 ? 104 ARG A C   1 
ATOM   1941 O O   . ARG B 1 104 ? -1.61300  7.16100   -8.14100  1.000 14.59000 ? 104 ARG A O   1 
ATOM   1942 C CB  . ARG B 1 104 ? -3.33500  9.14800   -6.55800  1.000 14.61000 ? 104 ARG A CB  1 
ATOM   1943 C CG  . ARG B 1 104 ? -3.91400  8.42100   -5.35600  1.000 16.72000 ? 104 ARG A CG  1 
ATOM   1944 C CD  . ARG B 1 104 ? -5.38800  8.10800   -5.55800  1.000 18.91000 ? 104 ARG A CD  1 
ATOM   1945 N NE  . ARG B 1 104 ? -5.91400  7.24700   -4.50300  1.000 17.10000 ? 104 ARG A NE  1 
ATOM   1946 C CZ  . ARG B 1 104 ? -7.05200  7.47200   -3.85300  1.000 19.30000 ? 104 ARG A CZ  1 
ATOM   1947 N NH1 . ARG B 1 104 ? -7.78800  8.53400   -4.15000  1.000 17.44000 ? 104 ARG A NH1 1 
ATOM   1948 N NH2 . ARG B 1 104 ? -7.45400  6.63400   -2.90700  1.000 21.81000 ? 104 ARG A NH2 1 
ATOM   1949 N N   . GLY B 1 105 ? -0.81900  6.92800   -6.04900  1.000 12.36000 ? 105 GLY A N   1 
ATOM   1950 C CA  . GLY B 1 105 ? -0.38000  5.55500   -6.24900  1.000 13.09000 ? 105 GLY A CA  1 
ATOM   1951 C C   . GLY B 1 105 ? 0.57700   5.06600   -5.16700  1.000 12.59000 ? 105 GLY A C   1 
ATOM   1952 O O   . GLY B 1 105 ? 0.55900   5.58900   -4.07000  1.000 14.77000 ? 105 GLY A O   1 
ATOM   1953 N N   . TRP B 1 106 ? 1.32000   4.03500   -5.47900  1.000 13.17000 ? 106 TRP A N   1 
ATOM   1954 C CA  . TRP B 1 106 ? 2.27900   3.54000   -4.53800  1.000 11.03000 ? 106 TRP A CA  1 
ATOM   1955 C C   . TRP B 1 106 ? 3.35900   2.80300   -5.28600  1.000 12.47000 ? 106 TRP A C   1 
ATOM   1956 O O   . TRP B 1 106 ? 3.20700   2.47600   -6.44700  1.000 11.89000 ? 106 TRP A O   1 
ATOM   1957 C CB  . TRP B 1 106 ? 1.62600   2.65500   -3.46900  1.000 15.30000 ? 106 TRP A CB  1 
ATOM   1958 C CG  . TRP B 1 106 ? 0.71600   1.54800   -3.94000  1.000 15.34000 ? 106 TRP A CG  1 
ATOM   1959 C CD1 . TRP B 1 106 ? -0.64100  1.51500   -3.84600  1.000 14.91000 ? 106 TRP A CD1 1 
ATOM   1960 C CD2 . TRP B 1 106 ? 1.10300   0.29200   -4.51800  1.000 13.24000 ? 106 TRP A CD2 1 
ATOM   1961 N NE1 . TRP B 1 106 ? -1.12400  0.33800   -4.34200  1.000 16.47000 ? 106 TRP A NE1 1 
ATOM   1962 C CE2 . TRP B 1 106 ? -0.07500  -0.43200  -4.76300  1.000 16.79000 ? 106 TRP A CE2 1 
ATOM   1963 C CE3 . TRP B 1 106 ? 2.32500   -0.27700  -4.86600  1.000 13.96000 ? 106 TRP A CE3 1 
ATOM   1964 C CZ2 . TRP B 1 106 ? -0.06700  -1.69400  -5.34100  1.000 17.16000 ? 106 TRP A CZ2 1 
ATOM   1965 C CZ3 . TRP B 1 106 ? 2.33000   -1.52800  -5.44000  1.000 12.82000 ? 106 TRP A CZ3 1 
ATOM   1966 C CH2 . TRP B 1 106 ? 1.14400   -2.22400  -5.66600  1.000 13.14000 ? 106 TRP A CH2 1 
ATOM   1967 N N   . LYS B 1 107 ? 4.46600   2.58100   -4.60000  1.000 11.57000 ? 107 LYS A N   1 
ATOM   1968 C CA  . LYS B 1 107 ? 5.58400   1.85500   -5.15800  1.000 11.39000 ? 107 LYS A CA  1 
ATOM   1969 C C   . LYS B 1 107 ? 6.07800   0.92300   -4.07100  1.000 13.58000 ? 107 LYS A C   1 
ATOM   1970 O O   . LYS B 1 107 ? 6.12000   1.30500   -2.91500  1.000 12.13000 ? 107 LYS A O   1 
ATOM   1971 C CB  . LYS B 1 107 ? 6.69800   2.80100   -5.57800  1.000 15.32000 ? 107 LYS A CB  1 
ATOM   1972 C CG  . LYS B 1 107 ? 6.33600   3.70400   -6.74200  1.000 18.48000 ? 107 LYS A CG  1 
ATOM   1973 C CD  . LYS B 1 107 ? 7.54300   4.49100   -7.22000  1.000 18.55000 ? 107 LYS A CD  1 
ATOM   1974 C CE  . LYS B 1 107 ? 7.18700   5.43400   -8.35400  1.000 27.09000 ? 107 LYS A CE  1 
ATOM   1975 N NZ  . LYS B 1 107 ? 8.39600   6.09800   -8.90800  1.000 35.56000 ? 107 LYS A NZ  1 
ATOM   1976 N N   . LYS B 1 108 ? 6.43600   -0.29400  -4.46000  1.000 12.37000 ? 108 LYS A N   1 
ATOM   1977 C CA  . LYS B 1 108 ? 6.91400   -1.29700  -3.52500  1.000 12.15000 ? 108 LYS A CA  1 
ATOM   1978 C C   . LYS B 1 108 ? 8.28600   -1.80000  -3.93900  1.000 12.84000 ? 108 LYS A C   1 
ATOM   1979 O O   . LYS B 1 108 ? 8.48400   -2.16700  -5.07800  1.000 12.94000 ? 108 LYS A O   1 
ATOM   1980 C CB  . LYS B 1 108 ? 5.98100   -2.51000  -3.53300  1.000 17.94000 ? 108 LYS A CB  1 
ATOM   1981 C CG  . LYS B 1 108 ? 5.16500   -2.76500  -2.27600  1.000 35.67000 ? 108 LYS A CG  1 
ATOM   1982 C CD  . LYS B 1 108 ? 4.64600   -4.20200  -2.26300  1.000 31.59000 ? 108 LYS A CD  1 
ATOM   1983 C CE  . LYS B 1 108 ? 3.13000   -4.29900  -2.29300  1.000 31.38000 ? 108 LYS A CE  1 
ATOM   1984 N NZ  . LYS B 1 108 ? 2.44000   -3.50600  -1.24300  1.000 31.73000 ? 108 LYS A NZ  1 
ATOM   1985 N N   . TRP B 1 109 ? 9.22100   -1.81800  -2.99700  1.000 12.30000 ? 109 TRP A N   1 
ATOM   1986 C CA  . TRP B 1 109 ? 10.55200  -2.35300  -3.24400  1.000 13.29000 ? 109 TRP A CA  1 
ATOM   1987 C C   . TRP B 1 109 ? 10.75100  -3.46800  -2.23500  1.000 16.78000 ? 109 TRP A C   1 
ATOM   1988 O O   . TRP B 1 109 ? 10.56500  -3.25300  -1.05900  1.000 17.85000 ? 109 TRP A O   1 
ATOM   1989 C CB  . TRP B 1 109 ? 11.64700  -1.32600  -2.96400  1.000 13.55000 ? 109 TRP A CB  1 
ATOM   1990 C CG  . TRP B 1 109 ? 11.71700  -0.13400  -3.84700  1.000 15.91000 ? 109 TRP A CG  1 
ATOM   1991 C CD1 . TRP B 1 109 ? 12.56800  0.06500   -4.88900  1.000 15.46000 ? 109 TRP A CD1 1 
ATOM   1992 C CD2 . TRP B 1 109 ? 10.95400  1.06200   -3.72300  1.000 14.09000 ? 109 TRP A CD2 1 
ATOM   1993 N NE1 . TRP B 1 109 ? 12.36400  1.30100   -5.43800  1.000 15.85000 ? 109 TRP A NE1 1 
ATOM   1994 C CE2 . TRP B 1 109 ? 11.37500  1.93400   -4.73800  1.000 14.64000 ? 109 TRP A CE2 1 
ATOM   1995 C CE3 . TRP B 1 109 ? 9.94000   1.47500   -2.86000  1.000 14.72000 ? 109 TRP A CE3 1 
ATOM   1996 C CZ2 . TRP B 1 109 ? 10.81600  3.19300   -4.91000  1.000 18.76000 ? 109 TRP A CZ2 1 
ATOM   1997 C CZ3 . TRP B 1 109 ? 9.39300   2.72100   -3.03100  1.000 17.22000 ? 109 TRP A CZ3 1 
ATOM   1998 C CH2 . TRP B 1 109 ? 9.82900   3.56500   -4.04600  1.000 22.24000 ? 109 TRP A CH2 1 
ATOM   1999 N N   . ILE B 1 110 ? 11.11700  -4.65100  -2.69800  1.000 16.29000 ? 110 ILE A N   1 
ATOM   2000 C CA  . ILE B 1 110 ? 11.38400  -5.77800  -1.80300  1.000 19.21000 ? 110 ILE A CA  1 
ATOM   2001 C C   . ILE B 1 110 ? 12.89100  -5.97400  -1.78200  1.000 25.45000 ? 110 ILE A C   1 
ATOM   2002 O O   . ILE B 1 110 ? 13.50900  -6.21100  -2.82700  1.000 27.03000 ? 110 ILE A O   1 
ATOM   2003 C CB  . ILE B 1 110 ? 10.64300  -7.05600  -2.23400  1.000 28.52000 ? 110 ILE A CB  1 
ATOM   2004 C CG1 . ILE B 1 110 ? 9.12500   -6.87000  -2.13500  1.000 28.66000 ? 110 ILE A CG1 1 
ATOM   2005 C CG2 . ILE B 1 110 ? 11.04600  -8.23700  -1.36400  1.000 34.94000 ? 110 ILE A CG2 1 
ATOM   2006 C CD1 . ILE B 1 110 ? 8.52200   -6.04400  -3.23600  1.000 32.42000 ? 110 ILE A CD1 1 
ATOM   2007 N N   . GLU B 1 111 ? 13.48300  -5.87200  -0.59700  1.000 23.56000 ? 111 GLU A N   1 
ATOM   2008 C CA  . GLU B 1 111 ? 14.92400  -6.03700  -0.44400  1.000 28.21000 ? 111 GLU A CA  1 
ATOM   2009 C C   . GLU B 1 111 ? 15.25100  -7.06500  0.63400   1.000 31.61000 ? 111 GLU A C   1 
ATOM   2010 O O   . GLU B 1 111 ? 15.45100  -6.71600  1.79700   1.000 28.04000 ? 111 GLU A O   1 
ATOM   2011 C CB  . GLU B 1 111 ? 15.58400  -4.69800  -0.11200  1.000 25.03000 ? 111 GLU A CB  1 
ATOM   2012 C CG  . GLU B 1 111 ? 15.12300  -3.54400  -0.98800  1.000 31.78000 ? 111 GLU A CG  1 
ATOM   2013 C CD  . GLU B 1 111 ? 16.04500  -3.30200  -2.16600  1.000 44.44000 ? 111 GLU A CD  1 
ATOM   2014 O OE1 . GLU B 1 111 ? 16.46400  -4.28800  -2.80700  1.000 44.98000 ? 111 GLU A OE1 1 
ATOM   2015 O OE2 . GLU B 1 111 ? 16.35200  -2.12500  -2.45100  1.000 49.64000 ? 111 GLU A OE2 1 
ATOM   2016 N N   . GLY B 1 112 ? 15.30600  -8.33200  0.23900   1.000 35.67000 ? 112 GLY A N   1 
ATOM   2017 C CA  . GLY B 1 112 ? 15.60800  -9.40700  1.16600   1.000 43.06000 ? 112 GLY A CA  1 
ATOM   2018 C C   . GLY B 1 112 ? 14.45100  -9.71000  2.09800   1.000 35.98000 ? 112 GLY A C   1 
ATOM   2019 O O   . GLY B 1 112 ? 13.49200  -10.37800 1.71400   1.000 44.86000 ? 112 GLY A O   1 
ATOM   2020 N N   . ASP B 1 113 ? 14.54300  -9.21600  3.32800   1.000 34.35000 ? 113 ASP A N   1 
ATOM   2021 C CA  . ASP B 1 113 ? 13.49900  -9.43600  4.32200   1.000 33.19000 ? 113 ASP A CA  1 
ATOM   2022 C C   . ASP B 1 113 ? 12.80200  -8.13100  4.69500   1.000 24.47000 ? 113 ASP A C   1 
ATOM   2023 O O   . ASP B 1 113 ? 12.11800  -8.05200  5.71500   1.000 25.15000 ? 113 ASP A O   1 
ATOM   2024 C CB  . ASP B 1 113 ? 14.07800  -10.10100 5.57100   1.000 43.37000 ? 113 ASP A CB  1 
ATOM   2025 C CG  . ASP B 1 113 ? 13.98400  -11.61400 5.52300   1.000 51.36000 ? 113 ASP A CG  1 
ATOM   2026 O OD1 . ASP B 1 113 ? 13.67700  -12.15700 4.44100   1.000 49.68000 ? 113 ASP A OD1 1 
ATOM   2027 O OD2 . ASP B 1 113 ? 14.21800  -12.26000 6.56600   1.000 60.51000 ? 113 ASP A OD2 1 
ATOM   2028 N N   . LYS B 1 114 ? 12.98200  -7.11100  3.86300   1.000 21.28000 ? 114 LYS A N   1 
ATOM   2029 C CA  . LYS B 1 114 ? 12.38500  -5.84300  4.09400   1.000 19.28000 ? 114 LYS A CA  1 
ATOM   2030 C C   . LYS B 1 114 ? 11.60500  -5.41400  2.88600   1.000 18.65000 ? 114 LYS A C   1 
ATOM   2031 O O   . LYS B 1 114 ? 12.00600  -5.60400  1.81500   1.000 20.65000 ? 114 LYS A O   1 
ATOM   2032 C CB  . LYS B 1 114 ? 13.41600  -4.79300  4.39800   1.000 20.96000 ? 114 LYS A CB  1 
ATOM   2033 C CG  . LYS B 1 114 ? 14.05900  -4.98400  5.74800   1.000 27.20000 ? 114 LYS A CG  1 
ATOM   2034 C CD  . LYS B 1 114 ? 15.27700  -4.13700  5.89800   1.000 36.60000 ? 114 LYS A CD  1 
ATOM   2035 C CE  . LYS B 1 114 ? 16.41400  -4.83000  6.64600   1.000 46.39000 ? 114 LYS A CE  1 
ATOM   2036 N NZ  . LYS B 1 114 ? 17.74300  -4.22400  6.36100   1.000 51.24000 ? 114 LYS A NZ  1 
ATOM   2037 N N   . LEU B 1 115 ? 10.46600  -4.83900  3.16400   1.000 15.29000 ? 115 LEU A N   1 
ATOM   2038 C CA  . LEU B 1 115 ? 9.59700   -4.31100  2.12400   1.000 14.73000 ? 115 LEU A CA  1 
ATOM   2039 C C   . LEU B 1 115 ? 9.44900   -2.81800  2.37700   1.000 15.20000 ? 115 LEU A C   1 
ATOM   2040 O O   . LEU B 1 115 ? 9.08400   -2.40600  3.48300   1.000 16.27000 ? 115 LEU A O   1 
ATOM   2041 C CB  . LEU B 1 115 ? 8.25300   -5.03300  2.14000   1.000 15.04000 ? 115 LEU A CB  1 
ATOM   2042 C CG  . LEU B 1 115 ? 7.25400   -4.66800  1.04100   1.000 16.89000 ? 115 LEU A CG  1 
ATOM   2043 C CD1 . LEU B 1 115 ? 6.32800   -5.85800  0.81300   1.000 20.89000 ? 115 LEU A CD1 1 
ATOM   2044 C CD2 . LEU B 1 115 ? 6.46900   -3.45700  1.45000   1.000 17.56000 ? 115 LEU A CD2 1 
ATOM   2045 N N   . TYR B 1 116 ? 9.78600   -2.01700  1.37300   1.000 12.91000 ? 116 TYR A N   1 
ATOM   2046 C CA  . TYR B 1 116 ? 9.66000   -0.57000  1.42700   1.000 12.70000 ? 116 TYR A CA  1 
ATOM   2047 C C   . TYR B 1 116 ? 8.44200   -0.16800  0.61400   1.000 12.72000 ? 116 TYR A C   1 
ATOM   2048 O O   . TYR B 1 116 ? 8.30700   -0.56000  -0.54900  1.000 11.93000 ? 116 TYR A O   1 
ATOM   2049 C CB  . TYR B 1 116 ? 10.91800  0.11300   0.88000   1.000 12.54000 ? 116 TYR A CB  1 
ATOM   2050 C CG  . TYR B 1 116 ? 12.14500  -0.19900  1.68100   1.000 13.14000 ? 116 TYR A CG  1 
ATOM   2051 C CD1 . TYR B 1 116 ? 12.85900  -1.35900  1.45300   1.000 20.67000 ? 116 TYR A CD1 1 
ATOM   2052 C CD2 . TYR B 1 116 ? 12.55000  0.63600   2.70400   1.000 15.29000 ? 116 TYR A CD2 1 
ATOM   2053 C CE1 . TYR B 1 116 ? 13.98900  -1.66600  2.21000   1.000 17.49000 ? 116 TYR A CE1 1 
ATOM   2054 C CE2 . TYR B 1 116 ? 13.67600  0.33600   3.47800   1.000 18.19000 ? 116 TYR A CE2 1 
ATOM   2055 C CZ  . TYR B 1 116 ? 14.37500  -0.81200  3.22000   1.000 16.60000 ? 116 TYR A CZ  1 
ATOM   2056 O OH  . TYR B 1 116 ? 15.49200  -1.11400  3.97600   1.000 25.11000 ? 116 TYR A OH  1 
ATOM   2057 N N   . LEU B 1 117 ? 7.54100   0.58100   1.23000   1.000 9.67000  ? 117 LEU A N   1 
ATOM   2058 C CA  . LEU B 1 117 ? 6.32000   1.01900   0.57000   1.000 11.70000 ? 117 LEU A CA  1 
ATOM   2059 C C   . LEU B 1 117 ? 6.25700   2.53600   0.57400   1.000 13.51000 ? 117 LEU A C   1 
ATOM   2060 O O   . LEU B 1 117 ? 6.40500   3.16600   1.62500   1.000 15.72000 ? 117 LEU A O   1 
ATOM   2061 C CB  . LEU B 1 117 ? 5.10600   0.41400   1.27000   1.000 14.76000 ? 117 LEU A CB  1 
ATOM   2062 C CG  . LEU B 1 117 ? 3.77000   0.86700   0.71600   1.000 16.63000 ? 117 LEU A CG  1 
ATOM   2063 C CD1 . LEU B 1 117 ? 3.59300   0.41600   -0.73200  1.000 14.87000 ? 117 LEU A CD1 1 
ATOM   2064 C CD2 . LEU B 1 117 ? 2.65600   0.30900   1.61000   1.000 18.60000 ? 117 LEU A CD2 1 
ATOM   2065 N N   . GLU B 1 118 ? 6.04900   3.13000   -0.59600  1.000 11.85000 ? 118 GLU A N   1 
ATOM   2066 C CA  . GLU B 1 118 ? 5.89900   4.57700   -0.70800  1.000 11.17000 ? 118 GLU A CA  1 
ATOM   2067 C C   . GLU B 1 118 ? 4.50100   4.85200   -1.22800  1.000 12.24000 ? 118 GLU A C   1 
ATOM   2068 O O   . GLU B 1 118 ? 4.15400   4.39500   -2.32200  1.000 13.97000 ? 118 GLU A O   1 
ATOM   2069 C CB  . GLU B 1 118 ? 6.94600   5.15300   -1.65500  1.000 14.68000 ? 118 GLU A CB  1 
ATOM   2070 C CG  . GLU B 1 118 ? 6.80500   6.62600   -1.94900  1.000 21.22000 ? 118 GLU A CG  1 
ATOM   2071 C CD  . GLU B 1 118 ? 7.88300   7.09300   -2.91100  1.000 31.11000 ? 118 GLU A CD  1 
ATOM   2072 O OE1 . GLU B 1 118 ? 9.06100   7.16700   -2.48900  1.000 40.50000 ? 118 GLU A OE1 1 
ATOM   2073 O OE2 . GLU B 1 118 ? 7.55900   7.32800   -4.09600  1.000 36.55000 ? 118 GLU A OE2 1 
ATOM   2074 N N   . LEU B 1 119 ? 3.69300   5.56000   -0.44000  1.000 11.08000 ? 119 LEU A N   1 
ATOM   2075 C CA  . LEU B 1 119 ? 2.34500   5.94600   -0.85300  1.000 11.81000 ? 119 LEU A CA  1 
ATOM   2076 C C   . LEU B 1 119 ? 2.34500   7.42200   -1.21600  1.000 16.62000 ? 119 LEU A C   1 
ATOM   2077 O O   . LEU B 1 119 ? 2.86400   8.24700   -0.45700  1.000 18.75000 ? 119 LEU A O   1 
ATOM   2078 C CB  . LEU B 1 119 ? 1.34300   5.68400   0.27100   1.000 13.55000 ? 119 LEU A CB  1 
ATOM   2079 C CG  . LEU B 1 119 ? 1.25800   4.24400   0.75200   1.000 17.59000 ? 119 LEU A CG  1 
ATOM   2080 C CD1 . LEU B 1 119 ? 0.92200   4.27900   2.22900   1.000 23.57000 ? 119 LEU A CD1 1 
ATOM   2081 C CD2 . LEU B 1 119 ? 0.18000   3.48800   -0.01900  1.000 22.84000 ? 119 LEU A CD2 1 
ATOM   2082 N N   . THR B 1 120 ? 1.77200   7.76000   -2.36400  1.000 14.09000 ? 120 THR A N   1 
ATOM   2083 C CA  . THR B 1 120 ? 1.80200   9.14300   -2.81500  1.000 15.78000 ? 120 THR A CA  1 
ATOM   2084 C C   . THR B 1 120 ? 0.39600   9.64000   -3.11400  1.000 17.91000 ? 120 THR A C   1 
ATOM   2085 O O   . THR B 1 120 ? -0.47300  8.88600   -3.56100  1.000 17.63000 ? 120 THR A O   1 
ATOM   2086 C CB  . THR B 1 120 ? 2.66200   9.32100   -4.06000  1.000 18.27000 ? 120 THR A CB  1 
ATOM   2087 O OG1 . THR B 1 120 ? 2.07800   8.58700   -5.14600  1.000 20.01000 ? 120 THR A OG1 1 
ATOM   2088 C CG2 . THR B 1 120 ? 4.09300   8.81600   -3.80700  1.000 19.28000 ? 120 THR A CG2 1 
ATOM   2089 N N   . CYS B 1 121 ? 0.19500   10.93100  -2.84700  1.000 17.91000 ? 121 CYS A N   1 
ATOM   2090 C CA  . CYS B 1 121 ? -1.02400  11.63500  -3.22400  1.000 16.57000 ? 121 CYS A CA  1 
ATOM   2091 C C   . CYS B 1 121 ? -0.68300  13.11000  -3.30800  1.000 20.17000 ? 121 CYS A C   1 
ATOM   2092 O O   . CYS B 1 121 ? -0.22900  13.68800  -2.31800  1.000 23.00000 ? 121 CYS A O   1 
ATOM   2093 C CB  . CYS B 1 121 ? -2.12700  11.39000  -2.21300  1.000 17.51000 ? 121 CYS A CB  1 
ATOM   2094 S SG  . CYS B 1 121 ? -3.71500  12.14700  -2.67100  1.000 26.08000 ? 121 CYS A SG  1 
ATOM   2095 N N   . GLY B 1 122 ? -0.91200  13.71700  -4.47000  1.000 27.55000 ? 122 GLY A N   1 
ATOM   2096 C CA  . GLY B 1 122 ? -0.47200  15.08900  -4.65700  1.000 31.24000 ? 122 GLY A CA  1 
ATOM   2097 C C   . GLY B 1 122 ? 1.00300   15.20300  -4.34100  1.000 26.36000 ? 122 GLY A C   1 
ATOM   2098 O O   . GLY B 1 122 ? 1.83400   14.43100  -4.83700  1.000 34.04000 ? 122 GLY A O   1 
ATOM   2099 N N   . ASP B 1 123 ? 1.35000   16.15800  -3.48300  1.000 29.54000 ? 123 ASP A N   1 
ATOM   2100 C CA  . ASP B 1 123 ? 2.74100   16.36900  -3.11700  1.000 31.36000 ? 123 ASP A CA  1 
ATOM   2101 C C   . ASP B 1 123 ? 3.12500   15.66600  -1.81800  1.000 31.03000 ? 123 ASP A C   1 
ATOM   2102 O O   . ASP B 1 123 ? 4.23700   15.87100  -1.32000  1.000 33.25000 ? 123 ASP A O   1 
ATOM   2103 C CB  . ASP B 1 123 ? 3.03700   17.86700  -3.01800  1.000 38.98000 ? 123 ASP A CB  1 
ATOM   2104 C CG  . ASP B 1 123 ? 2.26600   18.54200  -1.90100  1.000 36.72000 ? 123 ASP A CG  1 
ATOM   2105 O OD1 . ASP B 1 123 ? 2.88000   19.31400  -1.13200  1.000 53.69000 ? 123 ASP A OD1 1 
ATOM   2106 O OD2 . ASP B 1 123 ? 1.04500   18.30100  -1.79400  1.000 45.00000 ? 123 ASP A OD2 1 
ATOM   2107 N N   . GLN B 1 124 ? 2.24900   14.83300  -1.26400  1.000 24.81000 ? 124 GLN A N   1 
ATOM   2108 C CA  . GLN B 1 124 ? 2.53000   14.13700  -0.01600  1.000 24.75000 ? 124 GLN A CA  1 
ATOM   2109 C C   . GLN B 1 124 ? 3.02200   12.72200  -0.29100  1.000 23.60000 ? 124 GLN A C   1 
ATOM   2110 O O   . GLN B 1 124 ? 2.45000   12.00800  -1.11500  1.000 20.15000 ? 124 GLN A O   1 
ATOM   2111 C CB  . GLN B 1 124 ? 1.28100   14.08400  0.86700   1.000 24.57000 ? 124 GLN A CB  1 
ATOM   2112 C CG  . GLN B 1 124 ? 0.86900   15.44700  1.39400   1.000 20.95000 ? 124 GLN A CG  1 
ATOM   2113 C CD  . GLN B 1 124 ? 1.94800   16.08300  2.22900   1.000 30.50000 ? 124 GLN A CD  1 
ATOM   2114 O OE1 . GLN B 1 124 ? 2.37400   15.52700  3.24300   1.000 27.24000 ? 124 GLN A OE1 1 
ATOM   2115 N NE2 . GLN B 1 124 ? 2.40900   17.25300  1.80300   1.000 34.96000 ? 124 GLN A NE2 1 
ATOM   2116 N N   . VAL B 1 125 ? 4.07500   12.32200  0.41500   1.000 20.13000 ? 125 VAL A N   1 
ATOM   2117 C CA  . VAL B 1 125 ? 4.62400   10.97500  0.33800   1.000 22.11000 ? 125 VAL A CA  1 
ATOM   2118 C C   . VAL B 1 125 ? 4.63400   10.38800  1.74200   1.000 19.94000 ? 125 VAL A C   1 
ATOM   2119 O O   . VAL B 1 125 ? 5.18000   11.00500  2.66400   1.000 19.13000 ? 125 VAL A O   1 
ATOM   2120 C CB  . VAL B 1 125 ? 6.05300   10.98600  -0.24100  1.000 21.07000 ? 125 VAL A CB  1 
ATOM   2121 C CG1 . VAL B 1 125 ? 6.65100   9.59300   -0.21000  1.000 29.22000 ? 125 VAL A CG1 1 
ATOM   2122 C CG2 . VAL B 1 125 ? 6.07200   11.59200  -1.63400  1.000 27.49000 ? 125 VAL A CG2 1 
ATOM   2123 N N   . CYS B 1 126 ? 4.04300   9.20300   1.91100   1.000 17.09000 ? 126 CYS A N   1 
ATOM   2124 C CA  . CYS B 1 126 ? 4.18800   8.43500   3.14400   1.000 17.32000 ? 126 CYS A CA  1 
ATOM   2125 C C   . CYS B 1 126 ? 5.12500   7.26700   2.86300   1.000 14.64000 ? 126 CYS A C   1 
ATOM   2126 O O   . CYS B 1 126 ? 4.99400   6.60500   1.83100   1.000 16.46000 ? 126 CYS A O   1 
ATOM   2127 C CB  . CYS B 1 126 ? 2.83100   7.94100   3.65300   1.000 16.27000 ? 126 CYS A CB  1 
ATOM   2128 S SG  . CYS B 1 126 ? 2.84500   6.56800   4.83300   1.000 18.08000 ? 126 CYS A SG  1 
ATOM   2129 N N   . ARG B 1 127 ? 6.07700   7.04200   3.75000   1.000 13.71000 ? 127 ARG A N   1 
ATOM   2130 C CA  . ARG B 1 127 ? 7.02300   5.96700   3.60000   1.000 13.79000 ? 127 ARG A CA  1 
ATOM   2131 C C   . ARG B 1 127 ? 6.90200   4.94700   4.71300   1.000 17.01000 ? 127 ARG A C   1 
ATOM   2132 O O   . ARG B 1 127 ? 6.96200   5.28800   5.82900   1.000 15.61000 ? 127 ARG A O   1 
ATOM   2133 C CB  . ARG B 1 127 ? 8.45200   6.48500   3.51800   1.000 16.24000 ? 127 ARG A CB  1 
ATOM   2134 C CG  . ARG B 1 127 ? 8.63800   7.56800   2.49900   1.000 22.62000 ? 127 ARG A CG  1 
ATOM   2135 C CD  . ARG B 1 127 ? 10.08700  7.95400   2.33200   1.000 30.25000 ? 127 ARG A CD  1 
ATOM   2136 N NE  . ARG B 1 127 ? 10.32600  8.32200   0.96600   1.000 37.93000 ? 127 ARG A NE  1 
ATOM   2137 C CZ  . ARG B 1 127 ? 10.23600  9.52700   0.45600   1.000 40.32000 ? 127 ARG A CZ  1 
ATOM   2138 N NH1 . ARG B 1 127 ? 9.98300   10.58300  1.22500   1.000 40.99000 ? 127 ARG A NH1 1 
ATOM   2139 N NH2 . ARG B 1 127 ? 10.46800  9.68700   -0.84200  1.000 38.53000 ? 127 ARG A NH2 1 
ATOM   2140 N N   . GLN B 1 128 ? 6.76100   3.68600   4.32700   1.000 13.43000 ? 128 GLN A N   1 
ATOM   2141 C CA  . GLN B 1 128 ? 6.57600   2.62800   5.31200   1.000 15.60000 ? 128 GLN A CA  1 
ATOM   2142 C C   . GLN B 1 128 ? 7.62700   1.54800   5.09600   1.000 15.65000 ? 128 GLN A C   1 
ATOM   2143 O O   . GLN B 1 128 ? 8.08800   1.32800   3.97600   1.000 14.96000 ? 128 GLN A O   1 
ATOM   2144 C CB  . GLN B 1 128 ? 5.15300   2.03100   5.22900   1.000 12.68000 ? 128 GLN A CB  1 
ATOM   2145 C CG  . GLN B 1 128 ? 4.04200   3.07600   5.49400   1.000 12.67000 ? 128 GLN A CG  1 
ATOM   2146 C CD  . GLN B 1 128 ? 2.64700   2.49700   5.46500   1.000 17.59000 ? 128 GLN A CD  1 
ATOM   2147 O OE1 . GLN B 1 128 ? 2.43500   1.38800   5.00300   1.000 19.58000 ? 128 GLN A OE1 1 
ATOM   2148 N NE2 . GLN B 1 128 ? 1.68300   3.24900   5.98500   1.000 22.76000 ? 128 GLN A NE2 1 
ATOM   2149 N N   . VAL B 1 129 ? 8.05000   0.90700   6.18600   1.000 13.02000 ? 129 VAL A N   1 
ATOM   2150 C CA  . VAL B 1 129 ? 8.98300   -0.20500  6.10300   1.000 13.15000 ? 129 VAL A CA  1 
ATOM   2151 C C   . VAL B 1 129 ? 8.39400   -1.37100  6.87200   1.000 15.95000 ? 129 VAL A C   1 
ATOM   2152 O O   . VAL B 1 129 ? 7.89800   -1.18500  7.99200   1.000 15.84000 ? 129 VAL A O   1 
ATOM   2153 C CB  . VAL B 1 129 ? 10.37700  0.13700   6.65600   1.000 13.66000 ? 129 VAL A CB  1 
ATOM   2154 C CG1 . VAL B 1 129 ? 11.33700  -1.00700  6.33100   1.000 18.89000 ? 129 VAL A CG1 1 
ATOM   2155 C CG2 . VAL B 1 129 ? 10.87400  1.44600   6.07400   1.000 15.36000 ? 129 VAL A CG2 1 
ATOM   2156 N N   . PHE B 1 130 ? 8.44200   -2.56300  6.26200   1.000 14.17000 ? 130 PHE A N   1 
ATOM   2157 C CA  . PHE B 1 130 ? 7.92200   -3.80800  6.82100   1.000 15.76000 ? 130 PHE A CA  1 
ATOM   2158 C C   . PHE B 1 130 ? 9.02400   -4.86100  6.83500   1.000 16.13000 ? 130 PHE A C   1 
ATOM   2159 O O   . PHE B 1 130 ? 9.91600   -4.86100  5.98300   1.000 16.39000 ? 130 PHE A O   1 
ATOM   2160 C CB  . PHE B 1 130 ? 6.74300   -4.37300  5.99300   1.000 16.63000 ? 130 PHE A CB  1 
ATOM   2161 C CG  . PHE B 1 130 ? 5.54700   -3.45500  5.89300   1.000 15.81000 ? 130 PHE A CG  1 
ATOM   2162 C CD1 . PHE B 1 130 ? 5.55400   -2.36800  5.02800   1.000 17.29000 ? 130 PHE A CD1 1 
ATOM   2163 C CD2 . PHE B 1 130 ? 4.40700   -3.69600  6.63700   1.000 18.01000 ? 130 PHE A CD2 1 
ATOM   2164 C CE1 . PHE B 1 130 ? 4.45400   -1.54600  4.94200   1.000 16.76000 ? 130 PHE A CE1 1 
ATOM   2165 C CE2 . PHE B 1 130 ? 3.31300   -2.87900  6.54800   1.000 22.62000 ? 130 PHE A CE2 1 
ATOM   2166 C CZ  . PHE B 1 130 ? 3.33100   -1.79800  5.68600   1.000 21.82000 ? 130 PHE A CZ  1 
ATOM   2167 N N   . LYS B 1 131 ? 8.97300   -5.77300  7.80900   1.000 17.36000 ? 131 LYS A N   1 
ATOM   2168 C CA  . LYS B 1 131 ? 9.90600   -6.89300  7.82300   1.000 18.45000 ? 131 LYS A CA  1 
ATOM   2169 C C   . LYS B 1 131 ? 9.11000   -8.18200  7.69400   1.000 16.05000 ? 131 LYS A C   1 
ATOM   2170 O O   . LYS B 1 131 ? 8.01000   -8.29300  8.23500   1.000 19.53000 ? 131 LYS A O   1 
ATOM   2171 C CB  . LYS B 1 131 ? 10.75600  -6.90600  9.09500   1.000 24.14000 ? 131 LYS A CB  1 
ATOM   2172 C CG  . LYS B 1 131 ? 9.96500   -7.12400  10.36200  1.000 31.77000 ? 131 LYS A CG  1 
ATOM   2173 C CD  . LYS B 1 131 ? 10.75100  -7.96900  11.35000  1.000 37.98000 ? 131 LYS A CD  1 
ATOM   2174 C CE  . LYS B 1 131 ? 10.68100  -9.43700  10.97900  1.000 42.96000 ? 131 LYS A CE  1 
ATOM   2175 N NZ  . LYS B 1 131 ? 10.69600  -10.31200 12.18600  1.000 40.38000 ? 131 LYS A NZ  1 
ATOM   2176 N N   . LYS B 1 132 ? 9.65400   -9.13800  6.94200   1.000 19.77000 ? 132 LYS A N   1 
ATOM   2177 C CA  . LYS B 1 132 ? 8.93200   -10.37500 6.68300   1.000 20.34000 ? 132 LYS A CA  1 
ATOM   2178 C C   . LYS B 1 132 ? 8.90400   -11.23000 7.93500   1.000 23.48000 ? 132 LYS A C   1 
ATOM   2179 O O   . LYS B 1 132 ? 9.94000   -11.43300 8.57800   1.000 26.86000 ? 132 LYS A O   1 
ATOM   2180 C CB  . LYS B 1 132 ? 9.59400   -11.15300 5.55200   1.000 24.39000 ? 132 LYS A CB  1 
ATOM   2181 C CG  . LYS B 1 132 ? 8.69300   -12.20900 4.94400   1.000 29.50000 ? 132 LYS A CG  1 
ATOM   2182 C CD  . LYS B 1 132 ? 9.34300   -12.84700 3.73900   1.000 31.37000 ? 132 LYS A CD  1 
ATOM   2183 C CE  . LYS B 1 132 ? 8.41800   -13.87700 3.12400   1.000 34.12000 ? 132 LYS A CE  1 
ATOM   2184 N NZ  . LYS B 1 132 ? 9.11900   -14.65500 2.06200   1.000 32.17000 ? 132 LYS A NZ  1 
ATOM   2185 N N   . LYS B 1 133 ? 7.72300   -11.72800 8.27400   1.000 24.41000 ? 133 LYS A N   1 
ATOM   2186 C CA  . LYS B 1 133 ? 7.56900   -12.60400 9.42800   1.000 32.48000 ? 133 LYS A CA  1 
ATOM   2187 C C   . LYS B 1 133 ? 7.92500   -14.04700 9.06500   1.000 41.10000 ? 133 LYS A C   1 
ATOM   2188 O O   . LYS B 1 133 ? 7.58500   -14.53400 7.97900   1.000 34.67000 ? 133 LYS A O   1 
ATOM   2189 C CB  . LYS B 1 133 ? 6.14400   -12.52900 9.97600   1.000 32.73000 ? 133 LYS A CB  1 
ATOM   2190 C CG  . LYS B 1 133 ? 5.90900   -13.40500 11.19100  1.000 41.98000 ? 133 LYS A CG  1 
ATOM   2191 C CD  . LYS B 1 133 ? 4.79600   -12.85800 12.06800  1.000 49.54000 ? 133 LYS A CD  1 
ATOM   2192 C CE  . LYS B 1 133 ? 3.56500   -12.50300 11.25200  1.000 54.29000 ? 133 LYS A CE  1 
ATOM   2193 N NZ  . LYS B 1 133 ? 2.31100   -12.65500 12.04700  1.000 56.63000 ? 133 LYS A NZ  1 
HETATM 2194 C C10 . ZFJ C 2 .   ? 9.60900   3.29900   29.30500  1.000 42.69000 ? 201 ZFJ B C10 1 
HETATM 2195 C C13 . ZFJ C 2 .   ? 6.76800   2.45300   28.51100  1.000 28.73000 ? 201 ZFJ B C13 1 
HETATM 2196 C C15 . ZFJ C 2 .   ? 6.43900   4.27000   25.72700  1.000 31.57000 ? 201 ZFJ B C15 1 
HETATM 2197 C C17 . ZFJ C 2 .   ? 11.09200  4.31800   21.35100  1.000 51.53000 ? 201 ZFJ B C17 1 
HETATM 2198 C C20 . ZFJ C 2 .   ? 10.50100  7.60600   22.67400  1.000 43.98000 ? 201 ZFJ B C20 1 
HETATM 2199 C C21 . ZFJ C 2 .   ? 6.27300   1.75400   31.02400  1.000 27.32000 ? 201 ZFJ B C21 1 
HETATM 2200 C C22 . ZFJ C 2 .   ? 5.21600   1.06000   30.65900  1.000 31.18000 ? 201 ZFJ B C22 1 
HETATM 2201 C C01 . ZFJ C 2 .   ? 8.88700   3.84900   25.42200  1.000 36.19000 ? 201 ZFJ B C01 1 
HETATM 2202 C C02 . ZFJ C 2 .   ? 9.31100   4.29400   24.01300  1.000 46.33000 ? 201 ZFJ B C02 1 
HETATM 2203 C C03 . ZFJ C 2 .   ? 10.72500  4.84600   23.77900  1.000 45.57000 ? 201 ZFJ B C03 1 
HETATM 2204 C C04 . ZFJ C 2 .   ? 11.71100  4.95100   24.96100  1.000 49.51000 ? 201 ZFJ B C04 1 
HETATM 2205 C C05 . ZFJ C 2 .   ? 11.27100  4.50200   26.36200  1.000 43.67000 ? 201 ZFJ B C05 1 
HETATM 2206 C C06 . ZFJ C 2 .   ? 9.85300   3.95300   26.57800  1.000 44.69000 ? 201 ZFJ B C06 1 
HETATM 2207 C C07 . ZFJ C 2 .   ? 9.13600   3.43400   27.84900  1.000 38.12000 ? 201 ZFJ B C07 1 
HETATM 2208 C C08 . ZFJ C 2 .   ? 7.73700   3.01700   27.45700  1.000 35.36000 ? 201 ZFJ B C08 1 
HETATM 2209 C C09 . ZFJ C 2 .   ? 7.57000   3.27000   25.95400  1.000 38.97000 ? 201 ZFJ B C09 1 
HETATM 2210 C C11 . ZFJ C 2 .   ? 8.65500   2.73800   30.36900  1.000 37.23000 ? 201 ZFJ B C11 1 
HETATM 2211 C C12 . ZFJ C 2 .   ? 7.22600   2.31200   29.96900  1.000 30.52000 ? 201 ZFJ B C12 1 
HETATM 2212 C C14 . ZFJ C 2 .   ? 7.26200   1.95600   25.23800  1.000 41.83000 ? 201 ZFJ B C14 1 
HETATM 2213 C C18 . ZFJ C 2 .   ? 12.03300  3.15300   21.65000  1.000 52.61000 ? 201 ZFJ B C18 1 
HETATM 2214 C C19 . ZFJ C 2 .   ? 11.58000  6.62700   22.21700  1.000 47.74000 ? 201 ZFJ B C19 1 
HETATM 2215 C C23 . ZFJ C 2 .   ? 4.31100   0.43600   31.71800  1.000 24.42000 ? 201 ZFJ B C23 1 
HETATM 2216 N N16 . ZFJ C 2 .   ? 11.13100  5.26600   22.44900  1.000 49.14000 ? 201 ZFJ B N16 1 
HETATM 2217 H H1  . ZFJ C 2 .   ? 10.47000  3.55700   29.54100  1.000 51.25000 ? 201 ZFJ B H1  1 
HETATM 2218 H H2  . ZFJ C 2 .   ? 5.90800   2.19800   28.26600  1.000 34.50000 ? 201 ZFJ B H2  1 
HETATM 2219 H H3  . ZFJ C 2 .   ? 5.58800   3.84600   25.92600  1.000 37.91000 ? 201 ZFJ B H3  1 
HETATM 2220 H H4  . ZFJ C 2 .   ? 6.44600   4.56100   24.80100  1.000 37.91000 ? 201 ZFJ B H4  1 
HETATM 2221 H H5  . ZFJ C 2 .   ? 6.56300   5.03500   26.30800  1.000 37.91000 ? 201 ZFJ B H5  1 
HETATM 2222 H H6  . ZFJ C 2 .   ? 10.18700  3.98400   21.24500  1.000 61.86000 ? 201 ZFJ B H6  1 
HETATM 2223 H H7  . ZFJ C 2 .   ? 11.37200  4.75900   20.53400  1.000 61.86000 ? 201 ZFJ B H7  1 
HETATM 2224 H H8  . ZFJ C 2 .   ? 9.89200   7.15600   23.28000  1.000 52.80000 ? 201 ZFJ B H8  1 
HETATM 2225 H H9  . ZFJ C 2 .   ? 10.91600  8.35600   23.12900  1.000 52.80000 ? 201 ZFJ B H9  1 
HETATM 2226 H H10 . ZFJ C 2 .   ? 10.01000  7.92900   21.90300  1.000 52.80000 ? 201 ZFJ B H10 1 
HETATM 2227 H H11 . ZFJ C 2 .   ? 6.44100   1.90500   31.92600  1.000 32.81000 ? 201 ZFJ B H11 1 
HETATM 2228 H H12 . ZFJ C 2 .   ? 5.02000   0.95000   29.75600  1.000 37.44000 ? 201 ZFJ B H12 1 
HETATM 2229 H H13 . ZFJ C 2 .   ? 8.71400   4.22800   23.30400  1.000 55.62000 ? 201 ZFJ B H13 1 
HETATM 2230 H H14 . ZFJ C 2 .   ? 12.56800  5.28400   24.82500  1.000 59.43000 ? 201 ZFJ B H14 1 
HETATM 2231 H H15 . ZFJ C 2 .   ? 11.86200  4.56300   27.07800  1.000 52.43000 ? 201 ZFJ B H15 1 
HETATM 2232 H H16 . ZFJ C 2 .   ? 8.93700   2.65500   31.25100  1.000 44.70000 ? 201 ZFJ B H16 1 
HETATM 2233 H H17 . ZFJ C 2 .   ? 8.05600   1.64300   24.77900  1.000 50.22000 ? 201 ZFJ B H17 1 
HETATM 2234 H H18 . ZFJ C 2 .   ? 6.55000   2.09800   24.59300  1.000 50.22000 ? 201 ZFJ B H18 1 
HETATM 2235 H H19 . ZFJ C 2 .   ? 6.98000   1.29200   25.88700  1.000 50.22000 ? 201 ZFJ B H19 1 
HETATM 2236 H H20 . ZFJ C 2 .   ? 12.92400  3.49400   21.82900  1.000 63.16000 ? 201 ZFJ B H20 1 
HETATM 2237 H H21 . ZFJ C 2 .   ? 11.71200  2.66900   22.42800  1.000 63.16000 ? 201 ZFJ B H21 1 
HETATM 2238 H H22 . ZFJ C 2 .   ? 12.06200  2.55600   20.88600  1.000 63.16000 ? 201 ZFJ B H22 1 
HETATM 2239 H H23 . ZFJ C 2 .   ? 12.39500  6.78800   22.71600  1.000 57.31000 ? 201 ZFJ B H23 1 
HETATM 2240 H H24 . ZFJ C 2 .   ? 11.75000  6.75300   21.27000  1.000 57.31000 ? 201 ZFJ B H24 1 
HETATM 2241 H H27 . ZFJ C 2 .   ? 4.66600   0.16900   32.53500  1.000 29.33000 ? 201 ZFJ B H27 1 
HETATM 2242 C C   . ACY D 3 .   ? 10.66600  2.70400   34.12600  1.000 29.51000 ? 202 ACY B C   1 
HETATM 2243 O O   . ACY D 3 .   ? 11.87800  2.92700   33.92100  1.000 31.94000 ? 202 ACY B O   1 
HETATM 2244 O OXT . ACY D 3 .   ? 10.26700  2.09300   35.14100  1.000 32.25000 ? 202 ACY B OXT 1 
HETATM 2245 C CH3 . ACY D 3 .   ? 9.65900   3.18200   33.12200  1.000 24.40000 ? 202 ACY B CH3 1 
HETATM 2246 C C1  . GOL E 4 .   ? 9.38300   6.76900   31.43100  1.000 33.84000 ? 203 GOL B C1  1 
HETATM 2247 O O1  . GOL E 4 .   ? 9.80100   5.53100   32.01700  1.000 34.13000 ? 203 GOL B O1  1 
HETATM 2248 C C2  . GOL E 4 .   ? 9.72400   7.91800   32.37300  1.000 33.54000 ? 203 GOL B C2  1 
HETATM 2249 O O2  . GOL E 4 .   ? 11.14500  8.00300   32.52800  1.000 35.30000 ? 203 GOL B O2  1 
HETATM 2250 C C3  . GOL E 4 .   ? 9.19800   9.22400   31.79100  1.000 36.67000 ? 203 GOL B C3  1 
HETATM 2251 O O3  . GOL E 4 .   ? 7.77100   9.25800   31.90500  1.000 24.80000 ? 203 GOL B O3  1 
HETATM 2252 C C1  . GOL F 4 .   ? 17.02100  2.59300   30.19200  1.000 35.36000 ? 204 GOL B C1  1 
HETATM 2253 O O1  . GOL F 4 .   ? 16.95400  3.29500   28.99600  1.000 34.04000 ? 204 GOL B O1  1 
HETATM 2254 C C2  . GOL F 4 .   ? 17.63500  1.24500   29.84000  1.000 40.23000 ? 204 GOL B C2  1 
HETATM 2255 O O2  . GOL F 4 .   ? 16.74900  0.40700   29.18600  1.000 36.82000 ? 204 GOL B O2  1 
HETATM 2256 C C3  . GOL F 4 .   ? 18.05300  0.65500   31.16300  1.000 42.85000 ? 204 GOL B C3  1 
HETATM 2257 O O3  . GOL F 4 .   ? 18.66300  -0.52800  30.81400  1.000 52.32000 ? 204 GOL B O3  1 
HETATM 2258 C C1  . GOL G 4 .   ? -2.27700  17.09800  33.14800  1.000 48.60000 ? 205 GOL B C1  1 
HETATM 2259 O O1  . GOL G 4 .   ? -3.32700  17.62300  32.40500  1.000 54.42000 ? 205 GOL B O1  1 
HETATM 2260 C C2  . GOL G 4 .   ? -0.99300  17.62700  32.49700  1.000 45.94000 ? 205 GOL B C2  1 
HETATM 2261 O O2  . GOL G 4 .   ? -1.02100  19.00300  32.32400  1.000 49.34000 ? 205 GOL B O2  1 
HETATM 2262 C C3  . GOL G 4 .   ? 0.13400   17.19000  33.43900  1.000 44.43000 ? 205 GOL B C3  1 
HETATM 2263 O O3  . GOL G 4 .   ? 1.03100   18.25200  33.47600  1.000 52.85000 ? 205 GOL B O3  1 
HETATM 2264 C C1  . GOL H 4 .   ? 3.07900   14.55900  19.33300  1.000 30.13000 ? 206 GOL B C1  1 
HETATM 2265 O O1  . GOL H 4 .   ? 2.16800   15.23400  18.46300  1.000 49.41000 ? 206 GOL B O1  1 
HETATM 2266 C C2  . GOL H 4 .   ? 3.58000   13.24600  18.74900  1.000 29.05000 ? 206 GOL B C2  1 
HETATM 2267 O O2  . GOL H 4 .   ? 3.17800   13.04700  17.39100  1.000 48.10000 ? 206 GOL B O2  1 
HETATM 2268 C C3  . GOL H 4 .   ? 3.19800   12.06600  19.63200  1.000 37.48000 ? 206 GOL B C3  1 
HETATM 2269 O O3  . GOL H 4 .   ? 2.11900   11.31400  19.07600  1.000 31.73000 ? 206 GOL B O3  1 
HETATM 2270 C C1  . GOL I 4 .   ? 6.73500   -9.56400  19.64600  1.000 46.57000 ? 207 GOL B C1  1 
HETATM 2271 O O1  . GOL I 4 .   ? 6.54000   -9.14200  18.30100  1.000 55.14000 ? 207 GOL B O1  1 
HETATM 2272 C C2  . GOL I 4 .   ? 8.20700   -9.46200  20.00700  1.000 49.85000 ? 207 GOL B C2  1 
HETATM 2273 O O2  . GOL I 4 .   ? 8.47600   -10.39000 21.06400  1.000 56.32000 ? 207 GOL B O2  1 
HETATM 2274 C C3  . GOL I 4 .   ? 8.49300   -8.04200  20.46800  1.000 47.70000 ? 207 GOL B C3  1 
HETATM 2275 O O3  . GOL I 4 .   ? 9.89200   -7.75200  20.41200  1.000 55.61000 ? 207 GOL B O3  1 
HETATM 2276 C C10 . ZFJ J 2 .   ? -3.69100  0.58800   0.37000   1.000 52.03000 ? 201 ZFJ A C10 1 
HETATM 2277 C C13 . ZFJ J 2 .   ? -1.04800  -0.47400  1.46800   1.000 38.90000 ? 201 ZFJ A C13 1 
HETATM 2278 C C15 . ZFJ J 2 .   ? -1.00700  1.29500   4.31200   1.000 37.90000 ? 201 ZFJ A C15 1 
HETATM 2279 C C17 . ZFJ J 2 .   ? -6.34000  3.76800   7.21700   1.000 58.13000 ? 201 ZFJ A C17 1 
HETATM 2280 C C20 . ZFJ J 2 .   ? -7.13000  0.36600   7.67000   1.000 68.90000 ? 201 ZFJ A C20 1 
HETATM 2281 C C21 . ZFJ J 2 .   ? -0.29100  -1.09700  -0.99600  1.000 26.28000 ? 201 ZFJ A C21 1 
HETATM 2282 C C22 . ZFJ J 2 .   ? 0.66400   -1.88800  -0.57700  1.000 30.30000 ? 201 ZFJ A C22 1 
HETATM 2283 C C01 . ZFJ J 2 .   ? -3.44900  0.93500   4.32000   1.000 46.50000 ? 201 ZFJ A C01 1 
HETATM 2284 C C02 . ZFJ J 2 .   ? -4.01300  1.35300   5.67800   1.000 54.39000 ? 201 ZFJ A C02 1 
HETATM 2285 C C03 . ZFJ J 2 .   ? -5.40400  1.98000   5.75600   1.000 57.90000 ? 201 ZFJ A C03 1 
HETATM 2286 C C04 . ZFJ J 2 .   ? -6.22600  2.20000   4.46800   1.000 57.44000 ? 201 ZFJ A C04 1 
HETATM 2287 C C05 . ZFJ J 2 .   ? -5.64500  1.78100   3.11300   1.000 52.13000 ? 201 ZFJ A C05 1 
HETATM 2288 C C06 . ZFJ J 2 .   ? -4.24600  1.14800   3.05700   1.000 55.28000 ? 201 ZFJ A C06 1 
HETATM 2289 C C07 . ZFJ J 2 .   ? -3.40400  0.63300   1.87200   1.000 52.20000 ? 201 ZFJ A C07 1 
HETATM 2290 C C08 . ZFJ J 2 .   ? -2.10100  0.11200   2.41300   1.000 46.87000 ? 201 ZFJ A C08 1 
HETATM 2291 C C09 . ZFJ J 2 .   ? -2.11000  0.30600   3.93400   1.000 54.55000 ? 201 ZFJ A C09 1 
HETATM 2292 C C11 . ZFJ J 2 .   ? -2.64800  0.00900   -0.58700  1.000 44.19000 ? 201 ZFJ A C11 1 
HETATM 2293 C C12 . ZFJ J 2 .   ? -1.31800  -0.52900  -0.03500  1.000 39.91000 ? 201 ZFJ A C12 1 
HETATM 2294 C C14 . ZFJ J 2 .   ? -1.90600  -1.01900  4.66800   1.000 48.60000 ? 201 ZFJ A C14 1 
HETATM 2295 C C18 . ZFJ J 2 .   ? -7.85500  3.85600   7.37200   1.000 63.28000 ? 201 ZFJ A C18 1 
HETATM 2296 C C19 . ZFJ J 2 .   ? -6.10800  1.41700   8.09700   1.000 64.96000 ? 201 ZFJ A C19 1 
HETATM 2297 C C23 . ZFJ J 2 .   ? 1.49900   -2.68400  -1.58000  1.000 29.87000 ? 201 ZFJ A C23 1 
HETATM 2298 N N16 . ZFJ J 2 .   ? -5.95000  2.38500   7.03200   1.000 61.76000 ? 201 ZFJ A N16 1 
HETATM 2299 H H1  . ZFJ J 2 .   ? -4.50000  0.90800   0.04100   1.000 62.46000 ? 201 ZFJ A H1  1 
HETATM 2300 H H2  . ZFJ J 2 .   ? -0.24200  -0.79000  1.80700   1.000 46.71000 ? 201 ZFJ A H2  1 
HETATM 2301 H H3  . ZFJ J 2 .   ? -0.14000  0.89300   4.14300   1.000 45.50000 ? 201 ZFJ A H3  1 
HETATM 2302 H H4  . ZFJ J 2 .   ? -1.08100  1.51800   5.25300   1.000 45.50000 ? 201 ZFJ A H4  1 
HETATM 2303 H H5  . ZFJ J 2 .   ? -1.09800  2.10100   3.77900   1.000 45.50000 ? 201 ZFJ A H5  1 
HETATM 2304 H H6  . ZFJ J 2 .   ? -5.91300  4.12000   8.01400   1.000 69.79000 ? 201 ZFJ A H6  1 
HETATM 2305 H H7  . ZFJ J 2 .   ? -6.06300  4.28700   6.44600   1.000 69.79000 ? 201 ZFJ A H7  1 
HETATM 2306 H H8  . ZFJ J 2 .   ? -7.58500  0.02100   8.45400   1.000 82.71000 ? 201 ZFJ A H8  1 
HETATM 2307 H H9  . ZFJ J 2 .   ? -7.77800  0.76900   7.07100   1.000 82.71000 ? 201 ZFJ A H9  1 
HETATM 2308 H H10 . ZFJ J 2 .   ? -6.67600  -0.36000  7.21400   1.000 82.71000 ? 201 ZFJ A H10 1 
HETATM 2309 H H11 . ZFJ J 2 .   ? -0.34000  -0.87900  -1.89800  1.000 31.56000 ? 201 ZFJ A H11 1 
HETATM 2310 H H12 . ZFJ J 2 .   ? 0.83600   -1.96500  0.33400   1.000 36.38000 ? 201 ZFJ A H12 1 
HETATM 2311 H H13 . ZFJ J 2 .   ? -3.51500  1.22200   6.45200   1.000 65.29000 ? 201 ZFJ A H13 1 
HETATM 2312 H H14 . ZFJ J 2 .   ? -7.07100  2.58500   4.51400   1.000 68.95000 ? 201 ZFJ A H14 1 
HETATM 2313 H H15 . ZFJ J 2 .   ? -6.13400  1.90900   2.33300   1.000 62.59000 ? 201 ZFJ A H15 1 
HETATM 2314 H H16 . ZFJ J 2 .   ? -2.82100  -0.02500  -1.50000  1.000 53.06000 ? 201 ZFJ A H16 1 
HETATM 2315 H H17 . ZFJ J 2 .   ? -2.77000  -1.40700  4.88100   1.000 58.34000 ? 201 ZFJ A H17 1 
HETATM 2316 H H18 . ZFJ J 2 .   ? -1.41200  -0.86300  5.48800   1.000 58.34000 ? 201 ZFJ A H18 1 
HETATM 2317 H H19 . ZFJ J 2 .   ? -1.40800  -1.62900  4.10200   1.000 58.34000 ? 201 ZFJ A H19 1 
HETATM 2318 H H20 . ZFJ J 2 .   ? -8.27700  3.18300   6.81700   1.000 75.96000 ? 201 ZFJ A H20 1 
HETATM 2319 H H21 . ZFJ J 2 .   ? -8.09500  3.70600   8.30000   1.000 75.96000 ? 201 ZFJ A H21 1 
HETATM 2320 H H22 . ZFJ J 2 .   ? -8.15800  4.73700   7.09900   1.000 75.96000 ? 201 ZFJ A H22 1 
HETATM 2321 H H23 . ZFJ J 2 .   ? -5.25600  0.98800   8.27500   1.000 77.98000 ? 201 ZFJ A H23 1 
HETATM 2322 H H24 . ZFJ J 2 .   ? -6.41900  1.86500   8.89900   1.000 77.98000 ? 201 ZFJ A H24 1 
HETATM 2323 H H27 . ZFJ J 2 .   ? 1.20700   -2.77500  -2.45800  1.000 35.86000 ? 201 ZFJ A H27 1 
HETATM 2324 C C1  . GOL K 4 .   ? -3.44500  3.04300   -2.57000  1.000 37.47000 ? 202 GOL A C1  1 
HETATM 2325 O O1  . GOL K 4 .   ? -4.75900  2.57900   -2.44500  1.000 44.79000 ? 202 GOL A O1  1 
HETATM 2326 C C2  . GOL K 4 .   ? -3.44700  4.54900   -2.19000  1.000 40.50000 ? 202 GOL A C2  1 
HETATM 2327 O O2  . GOL K 4 .   ? -4.68900  5.13000   -2.41900  1.000 31.12000 ? 202 GOL A O2  1 
HETATM 2328 C C3  . GOL K 4 .   ? -2.33900  5.17800   -3.07500  1.000 29.84000 ? 202 GOL A C3  1 
HETATM 2329 O O3  . GOL K 4 .   ? -1.82700  6.31500   -2.40800  1.000 28.07000 ? 202 GOL A O3  1 
HETATM 2330 C C1  . GOL L 4 .   ? 2.56600   2.78700   -15.05000 1.000 40.85000 ? 203 GOL A C1  1 
HETATM 2331 O O1  . GOL L 4 .   ? 1.18700   3.07100   -14.81600 1.000 40.02000 ? 203 GOL A O1  1 
HETATM 2332 C C2  . GOL L 4 .   ? 3.36900   4.07700   -14.99700 1.000 40.92000 ? 203 GOL A C2  1 
HETATM 2333 O O2  . GOL L 4 .   ? 4.07700   4.23400   -16.22300 1.000 45.68000 ? 203 GOL A O2  1 
HETATM 2334 C C3  . GOL L 4 .   ? 4.37200   3.98700   -13.85900 1.000 40.80000 ? 203 GOL A C3  1 
HETATM 2335 O O3  . GOL L 4 .   ? 4.38900   5.21600   -13.12800 1.000 49.16000 ? 203 GOL A O3  1 
HETATM 2336 C C   . ACY M 3 .   ? -5.79100  -12.45400 7.36600   1.000 55.57000 ? 204 ACY A C   1 
HETATM 2337 O O   . ACY M 3 .   ? -5.02200  -13.21800 6.75500   1.000 51.15000 ? 204 ACY A O   1 
HETATM 2338 O OXT . ACY M 3 .   ? -5.55300  -12.05200 8.52100   1.000 62.10000 ? 204 ACY A OXT 1 
HETATM 2339 C CH3 . ACY M 3 .   ? -7.02900  -11.97500 6.67400   1.000 49.40000 ? 204 ACY A CH3 1 
HETATM 2340 C C   . ACY N 3 .   ? -4.62000  -0.40200  -4.31700  1.000 38.94000 ? 205 ACY A C   1 
HETATM 2341 O O   . ACY N 3 .   ? -3.75300  -0.09900  -3.46800  1.000 35.41000 ? 205 ACY A O   1 
HETATM 2342 O OXT . ACY N 3 .   ? -5.83500  -0.17000  -4.13400  1.000 39.92000 ? 205 ACY A OXT 1 
HETATM 2343 C CH3 . ACY N 3 .   ? -4.18900  -1.06200  -5.59200  1.000 32.65000 ? 205 ACY A CH3 1 
HETATM 2344 C C1  . GOL O 4 .   ? -18.81800 6.82700   -4.21300  1.000 38.05000 ? 206 GOL A C1  1 
HETATM 2345 O O1  . GOL O 4 .   ? -19.16500 8.18800   -3.94000  1.000 47.16000 ? 206 GOL A O1  1 
HETATM 2346 C C2  . GOL O 4 .   ? -17.71500 6.77300   -5.26500  1.000 38.77000 ? 206 GOL A C2  1 
HETATM 2347 O O2  . GOL O 4 .   ? -18.23300 6.28500   -6.50300  1.000 44.36000 ? 206 GOL A O2  1 
HETATM 2348 C C3  . GOL O 4 .   ? -16.57600 5.87500   -4.81600  1.000 36.26000 ? 206 GOL A C3  1 
HETATM 2349 O O3  . GOL O 4 .   ? -17.02200 4.93100   -3.84600  1.000 37.61000 ? 206 GOL A O3  1 
HETATM 2350 O O   . HOH P 5 .   ? -3.58900  7.40900   22.38500  1.000 27.75000 ? 301 HOH B O   1 
HETATM 2351 O O   . HOH P 5 .   ? -10.91000 -0.06900  26.48500  1.000 39.63000 ? 302 HOH B O   1 
HETATM 2352 O O   . HOH P 5 .   ? 18.59800  7.45700   48.51800  1.000 49.07000 ? 303 HOH B O   1 
HETATM 2353 O O   . HOH P 5 .   ? 6.27700   10.93400  10.44600  1.000 25.21000 ? 304 HOH B O   1 
HETATM 2354 O O   . HOH P 5 .   ? -4.443    7.114     29.494    1.000 26.65000 ? 305 HOH B O   1 
HETATM 2355 O O   . HOH P 5 .   ? -5.50300  -2.23400  35.42700  1.000 32.15000 ? 306 HOH B O   1 
HETATM 2356 O O   . HOH P 5 .   ? 6.66600   -6.53900  46.55200  1.000 38.66000 ? 307 HOH B O   1 
HETATM 2357 O O   . HOH P 5 .   ? 3.34800   -1.75600  17.67700  1.000 31.21000 ? 308 HOH B O   1 
HETATM 2358 O O   . HOH P 5 .   ? 12.36900  12.85300  38.01200  1.000 17.37000 ? 309 HOH B O   1 
HETATM 2359 O O   . HOH P 5 .   ? 2.42100   9.87900   36.06400  1.000 27.16000 ? 310 HOH B O   1 
HETATM 2360 O O   . HOH P 5 .   ? 6.55400   5.85100   17.51400  1.000 36.02000 ? 311 HOH B O   1 
HETATM 2361 O O   . HOH P 5 .   ? -4.865    -0.754    45.846    1.000 23.95000 ? 312 HOH B O   1 
HETATM 2362 O O   . HOH P 5 .   ? 21.00500  0.75400   43.81600  1.000 40.72000 ? 313 HOH B O   1 
HETATM 2363 O O   . HOH P 5 .   ? 0.13400   3.26300   44.91600  1.000 32.32000 ? 314 HOH B O   1 
HETATM 2364 O O   . HOH P 5 .   ? 8.95100   17.49700  19.60900  1.000 41.96000 ? 315 HOH B O   1 
HETATM 2365 O O   . HOH P 5 .   ? 13.99600  -6.40800  31.01600  1.000 35.47000 ? 316 HOH B O   1 
HETATM 2366 O O   . HOH P 5 .   ? 16.87900  12.73600  37.36800  1.000 19.27000 ? 317 HOH B O   1 
HETATM 2367 O O   . HOH P 5 .   ? 10.11000  -0.33600  14.89800  1.000 25.51000 ? 318 HOH B O   1 
HETATM 2368 O O   . HOH P 5 .   ? 9.17100   -0.68900  42.43800  1.000 14.52000 ? 319 HOH B O   1 
HETATM 2369 O O   . HOH P 5 .   ? 1.71300   -7.55500  41.80100  1.000 35.89000 ? 320 HOH B O   1 
HETATM 2370 O O   . HOH P 5 .   ? -3.68300  5.86500   16.14400  1.000 32.15000 ? 321 HOH B O   1 
HETATM 2371 O O   . HOH P 5 .   ? 4.49900   4.37100   42.86100  1.000 17.35000 ? 322 HOH B O   1 
HETATM 2372 O O   . HOH P 5 .   ? -4.77700  -13.40500 35.36400  1.000 36.73000 ? 323 HOH B O   1 
HETATM 2373 O O   . HOH P 5 .   ? 13.08500  -7.05300  40.47300  1.000 36.94000 ? 324 HOH B O   1 
HETATM 2374 O O   . HOH P 5 .   ? 12.34700  -2.95700  42.41900  1.000 17.30000 ? 325 HOH B O   1 
HETATM 2375 O O   . HOH P 5 .   ? 0.13000   -11.43200 23.93700  1.000 32.11000 ? 326 HOH B O   1 
HETATM 2376 O O   . HOH P 5 .   ? 1.10500   8.20600   43.58500  1.000 41.63000 ? 327 HOH B O   1 
HETATM 2377 O O   . HOH P 5 .   ? 8.54400   12.67300  39.72000  1.000 22.47000 ? 328 HOH B O   1 
HETATM 2378 O O   . HOH P 5 .   ? 3.30600   8.90300   38.31100  1.000 27.12000 ? 329 HOH B O   1 
HETATM 2379 O O   . HOH P 5 .   ? 21.29800  12.12800  36.33500  1.000 27.72000 ? 330 HOH B O   1 
HETATM 2380 O O   . HOH P 5 .   ? 6.78300   15.66100  41.30800  1.000 38.95000 ? 331 HOH B O   1 
HETATM 2381 O O   . HOH P 5 .   ? 18.45500  -0.31000  42.88000  1.000 36.21000 ? 332 HOH B O   1 
HETATM 2382 O O   . HOH P 5 .   ? -2.00100  -2.33900  16.59400  1.000 43.37000 ? 333 HOH B O   1 
HETATM 2383 O O   . HOH P 5 .   ? -0.31400  13.77900  19.08200  1.000 28.59000 ? 334 HOH B O   1 
HETATM 2384 O O   . HOH P 5 .   ? 0.77500   -7.53200  45.40400  1.000 47.94000 ? 335 HOH B O   1 
HETATM 2385 O O   . HOH P 5 .   ? 14.35800  13.06800  36.07100  1.000 17.22000 ? 336 HOH B O   1 
HETATM 2386 O O   . HOH P 5 .   ? 16.14700  -2.61600  35.33700  1.000 33.29000 ? 337 HOH B O   1 
HETATM 2387 O O   . HOH P 5 .   ? 16.42700  -2.15200  44.64100  1.000 33.06000 ? 338 HOH B O   1 
HETATM 2388 O O   . HOH P 5 .   ? -5.74600  10.24300  33.57100  1.000 44.73000 ? 339 HOH B O   1 
HETATM 2389 O O   . HOH P 5 .   ? -7.96300  2.34300   41.30400  1.000 39.17000 ? 340 HOH B O   1 
HETATM 2390 O O   . HOH P 5 .   ? 7.05400   19.77800  25.61400  1.000 28.16000 ? 341 HOH B O   1 
HETATM 2391 O O   . HOH P 5 .   ? 23.17900  12.46500  28.13200  1.000 40.56000 ? 342 HOH B O   1 
HETATM 2392 O O   . HOH P 5 .   ? 21.972    13.738    31.281    1.000 41.27000 ? 343 HOH B O   1 
HETATM 2393 O O   . HOH P 5 .   ? -4.23500  6.11900   26.93600  1.000 22.79000 ? 344 HOH B O   1 
HETATM 2394 O O   . HOH P 5 .   ? 4.09500   6.61600   17.17000  1.000 37.97000 ? 345 HOH B O   1 
HETATM 2395 O O   . HOH P 5 .   ? -0.05300  17.19500  27.78300  1.000 32.86000 ? 346 HOH B O   1 
HETATM 2396 O O   . HOH P 5 .   ? -2.43600  8.10100   17.58900  1.000 31.32000 ? 347 HOH B O   1 
HETATM 2397 O O   . HOH P 5 .   ? 8.80100   -11.54600 35.71800  1.000 35.16000 ? 348 HOH B O   1 
HETATM 2398 O O   . HOH P 5 .   ? -8.94300  0.53800   40.53400  1.000 30.19000 ? 349 HOH B O   1 
HETATM 2399 O O   . HOH P 5 .   ? 12.06900  -8.34400  38.22900  1.000 31.32000 ? 350 HOH B O   1 
HETATM 2400 O O   . HOH P 5 .   ? 0.40900   9.23900   34.19000  1.000 34.75000 ? 351 HOH B O   1 
HETATM 2401 O O   . HOH P 5 .   ? 10.66000  14.06600  40.87800  1.000 28.96000 ? 352 HOH B O   1 
HETATM 2402 O O   . HOH P 5 .   ? 18.24000  0.93900   34.89200  1.000 39.88000 ? 353 HOH B O   1 
HETATM 2403 O O   . HOH P 5 .   ? 4.194     -18.439   36.981    1.000 32.13000 ? 354 HOH B O   1 
HETATM 2404 O O   . HOH P 5 .   ? 8.41700   20.86500  27.46400  1.000 29.31000 ? 355 HOH B O   1 
HETATM 2405 O O   . HOH P 5 .   ? 1.50600   9.44000   41.13800  1.000 39.87000 ? 356 HOH B O   1 
HETATM 2406 O O   . HOH P 5 .   ? 14.70300  -3.96300  42.74900  1.000 36.70000 ? 357 HOH B O   1 
HETATM 2407 O O   . HOH Q 5 .   ? -18.28800 4.64500   -7.34200  1.000 31.90000 ? 301 HOH A O   1 
HETATM 2408 O O   . HOH Q 5 .   ? 0.65900   -15.20800 -14.07400 1.000 38.33000 ? 302 HOH A O   1 
HETATM 2409 O O   . HOH Q 5 .   ? 11.79200  -5.25100  -5.48600  1.000 29.05000 ? 303 HOH A O   1 
HETATM 2410 O O   . HOH Q 5 .   ? 9.79000   13.45300  6.59400   1.000 50.73000 ? 304 HOH A O   1 
HETATM 2411 O O   . HOH Q 5 .   ? 3.06800   -18.08400 -5.28100  1.000 38.01000 ? 305 HOH A O   1 
HETATM 2412 O O   . HOH Q 5 .   ? 5.83800   0.03400   -15.07000 1.000 31.29000 ? 306 HOH A O   1 
HETATM 2413 O O   . HOH Q 5 .   ? 0.58300   3.66100   11.62000  1.000 34.77000 ? 307 HOH A O   1 
HETATM 2414 O O   . HOH Q 5 .   ? -6.33700  9.74600   -8.48400  1.000 19.97000 ? 308 HOH A O   1 
HETATM 2415 O O   . HOH Q 5 .   ? 10.98500  -3.66400  -15.90900 1.000 25.25000 ? 309 HOH A O   1 
HETATM 2416 O O   . HOH Q 5 .   ? 1.56700   1.21700   -13.03800 1.000 18.79000 ? 310 HOH A O   1 
HETATM 2417 O O   . HOH Q 5 .   ? 17.17500  -2.91100  3.06700   1.000 34.48000 ? 311 HOH A O   1 
HETATM 2418 O O   . HOH Q 5 .   ? 9.31200   4.83200   7.40200   1.000 21.56000 ? 312 HOH A O   1 
HETATM 2419 O O   . HOH Q 5 .   ? 6.19200   -14.35900 5.65200   1.000 33.14000 ? 313 HOH A O   1 
HETATM 2420 O O   . HOH Q 5 .   ? -1.07500  -16.44400 -12.22600 1.000 42.21000 ? 314 HOH A O   1 
HETATM 2421 O O   . HOH Q 5 .   ? -2.95100  -3.89200  -12.66700 1.000 14.04000 ? 315 HOH A O   1 
HETATM 2422 O O   . HOH Q 5 .   ? -10.98800 9.56400   -7.77500  1.000 21.04000 ? 316 HOH A O   1 
HETATM 2423 O O   . HOH Q 5 .   ? 4.71700   -10.52700 -12.00500 1.000 36.54000 ? 317 HOH A O   1 
HETATM 2424 O O   . HOH Q 5 .   ? 3.62200   6.66000   -6.41700  1.000 28.69000 ? 318 HOH A O   1 
HETATM 2425 O O   . HOH Q 5 .   ? 9.95300   3.20300   3.00100   1.000 24.39000 ? 319 HOH A O   1 
HETATM 2426 O O   . HOH Q 5 .   ? -4.34600  3.86800   -14.13100 1.000 36.11000 ? 320 HOH A O   1 
HETATM 2427 O O   . HOH Q 5 .   ? -20.700   4.230     0.175     1.000 25.46000 ? 321 HOH A O   1 
HETATM 2428 O O   . HOH Q 5 .   ? 4.90400   -4.67500  13.92100  1.000 40.79000 ? 322 HOH A O   1 
HETATM 2429 O O   . HOH Q 5 .   ? -8.42600  9.88800   -6.60600  1.000 18.37000 ? 323 HOH A O   1 
HETATM 2430 O O   . HOH Q 5 .   ? -0.91500  12.65400  -11.89200 1.000 40.26000 ? 324 HOH A O   1 
HETATM 2431 O O   . HOH Q 5 .   ? 2.18200   10.87400  10.37900  1.000 31.76000 ? 325 HOH A O   1 
HETATM 2432 O O   . HOH Q 5 .   ? -5.84700  -11.40300 -8.22300  1.000 33.74000 ? 326 HOH A O   1 
HETATM 2433 O O   . HOH Q 5 .   ? -15.25500 9.03300   -6.95100  1.000 25.97000 ? 327 HOH A O   1 
HETATM 2434 O O   . HOH Q 5 .   ? -6.14900  -6.26400  -12.58500 1.000 18.67000 ? 328 HOH A O   1 
HETATM 2435 O O   . HOH Q 5 .   ? -2.62900  9.51300   -10.26500 1.000 25.74000 ? 329 HOH A O   1 
HETATM 2436 O O   . HOH Q 5 .   ? 1.77600   -15.53100 11.59900  1.000 54.38000 ? 330 HOH A O   1 
HETATM 2437 O O   . HOH Q 5 .   ? 5.78000   14.41500  1.63400   1.000 30.75000 ? 331 HOH A O   1 
HETATM 2438 O O   . HOH Q 5 .   ? -4.81300  10.75200  -11.37100 1.000 34.54000 ? 332 HOH A O   1 
HETATM 2439 O O   . HOH Q 5 .   ? 2.78800   5.89800   -8.75600  1.000 28.04000 ? 333 HOH A O   1 
HETATM 2440 O O   . HOH Q 5 .   ? -4.48800  16.44400  -6.38200  1.000 39.06000 ? 334 HOH A O   1 
HETATM 2441 O O   . HOH Q 5 .   ? -12.23700 -3.82900  -12.81900 1.000 35.41000 ? 335 HOH A O   1 
HETATM 2442 O O   . HOH Q 5 .   ? -10.32500 -5.37000  -14.77400 1.000 31.30000 ? 336 HOH A O   1 
HETATM 2443 O O   . HOH Q 5 .   ? 3.45600   8.73000   10.31700  1.000 28.55000 ? 337 HOH A O   1 
HETATM 2444 O O   . HOH Q 5 .   ? 15.06800  -2.45400  -10.33300 1.000 29.38000 ? 338 HOH A O   1 
HETATM 2445 O O   . HOH Q 5 .   ? 11.13600  6.00400   6.43100   1.000 37.49000 ? 339 HOH A O   1 
HETATM 2446 O O   . HOH Q 5 .   ? -17.282   9.615     1.632     1.000 38.69000 ? 340 HOH A O   1 
HETATM 2447 O O   . HOH Q 5 .   ? 13.11100  -14.53200 2.47000   1.000 35.89000 ? 341 HOH A O   1 
HETATM 2448 O O   . HOH Q 5 .   ? 10.770    4.198     -9.742    1.000 46.30000 ? 342 HOH A O   1 
HETATM 2449 O O   . HOH Q 5 .   ? -12.82000 8.47600   -11.65200 1.000 39.35000 ? 343 HOH A O   1 
HETATM 2450 O O   . HOH Q 5 .   ? -12.20100 -2.05800  -5.06500  1.000 35.38000 ? 344 HOH A O   1 
HETATM 2451 O O   . HOH Q 5 .   ? 12.33100  -10.67500 -3.90000  1.000 41.70000 ? 345 HOH A O   1 
HETATM 2452 O O   . HOH Q 5 .   ? -10.05100 -5.78200  -5.80800  1.000 38.25000 ? 346 HOH A O   1 
HETATM 2453 O O   . HOH Q 5 .   ? -8.99000  14.70000  -13.61300 1.000 53.05000 ? 347 HOH A O   1 
HETATM 2454 O O   . HOH Q 5 .   ? 2.58700   3.65200   13.30100  1.000 42.45000 ? 348 HOH A O   1 
HETATM 2455 O O   . HOH Q 5 .   ? 2.601     -21.739   -7.501    1.000 35.30000 ? 349 HOH A O   1 
HETATM 2456 O O   . HOH Q 5 .   ? 1.212     3.240     -19.177   1.000 36.19000 ? 350 HOH A O   1 
HETATM 2457 O O   . HOH Q 5 .   ? -8.40700  -7.28300  -13.03400 1.000 33.82000 ? 351 HOH A O   1 
HETATM 2458 O O   . HOH Q 5 .   ? 11.75000  4.79800   4.80300   1.000 32.08000 ? 352 HOH A O   1 
HETATM 2459 O O   . HOH Q 5 .   ? -0.61300  -19.45000 -14.42500 1.000 52.37000 ? 353 HOH A O   1 
# 
