data_9D8M
# 
_entry.id   9D8M 
# 
_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   9D8M         pdb_00009d8m 10.2210/pdb9d8m/pdb 
WWPDB D_1000287534 ?            ?                   
# 
_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                        9D8M 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-19 
_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 
'Ehyaei, N.'   1 ?                   
'Bingham, C.'  2 0000-0001-5920-5543 
'Geiger, J.H.' 3 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 'Maity, S.'     2 ?                   
primary 'Ehyaei, N.'    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'                                                 15558.567 2   ? 
Q108K:K40L:T51V:T53C:R58W:Y19W:Q38L:Q4A:T29L ? ? 
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    2   ? ? ? ? 
4 water       nat water                                                                       18.015    305 ? ? ? ? 
# 
_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       
;TRDANGTWEMESNENFEGWMKALDIDFALRKIAVRLTLTLVIDQDGDNFKVKCTSTFWNYDVDFTVGVEFDEYTKSLDNR
HVKALVTWEGDVLVSVQKGEKENRGWKKWIEGDKLYLELTCGDQVCRQVFKKK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TRDANGTWEMESNENFEGWMKALDIDFALRKIAVRLTLTLVIDQDGDNFKVKCTSTFWNYDVDFTVGVEFDEYTKSLDNR
HVKALVTWEGDVLVSVQKGEKENRGWKKWIEGDKLYLELTCGDQVCRQVFKKK
;
_entity_poly.pdbx_strand_id                 A,B 
_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 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  VAL 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  TRP 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  SER 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  
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 A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   ASN 5   5   5   ASN ASN A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   TRP 8   8   8   TRP TRP A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  MET 10  10  10  MET MET A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  TRP 19  19  19  TRP TRP A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  CYS 53  53  53  CYS CYS A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  TRP 58  58  58  TRP TRP A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TRP 88  88  88  TRP TRP A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 TRP 106 106 106 TRP TRP A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 TRP 109 109 109 TRP TRP A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 CYS 121 121 121 CYS CYS A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 CYS 126 126 126 CYS CYS A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
B 1 1   THR 1   1   1   THR THR B . n 
B 1 2   ARG 2   2   2   ARG ARG B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   ASN 5   5   5   ASN ASN B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   THR 7   7   7   THR THR B . n 
B 1 8   TRP 8   8   8   TRP TRP B . n 
B 1 9   GLU 9   9   9   GLU GLU B . n 
B 1 10  MET 10  10  10  MET MET B . n 
B 1 11  GLU 11  11  11  GLU GLU B . n 
B 1 12  SER 12  12  12  SER SER B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  PHE 16  16  16  PHE PHE B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  TRP 19  19  19  TRP TRP B . n 
B 1 20  MET 20  20  20  MET MET B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  ASP 24  24  24  ASP ASP B . n 
B 1 25  ILE 25  25  25  ILE ILE B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  ARG 30  30  30  ARG ARG B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  ILE 32  32  32  ILE ILE B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  LEU 40  40  40  LEU LEU B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  ILE 42  42  42  ILE ILE B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  ASP 45  45  45  ASP ASP B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  ASN 48  48  48  ASN ASN B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  CYS 53  53  53  CYS CYS B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  SER 55  55  55  SER SER B . n 
B 1 56  THR 56  56  56  THR THR B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  TRP 58  58  58  TRP TRP B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  TYR 60  60  60  TYR TYR B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  VAL 62  62  62  VAL VAL B . n 
B 1 63  ASP 63  63  63  ASP ASP B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  TYR 73  73  73  TYR TYR B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  ASN 79  79  79  ASN ASN B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  HIS 81  81  81  HIS HIS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LYS 83  83  83  LYS LYS B . n 
B 1 84  ALA 84  84  84  ALA ALA B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  TRP 88  88  88  TRP TRP B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  ASP 91  91  91  ASP ASP B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  SER 95  95  95  SER SER B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  LYS 98  98  98  LYS LYS B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 GLY 105 105 105 GLY GLY B . n 
B 1 106 TRP 106 106 106 TRP TRP B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 TRP 109 109 109 TRP TRP B . n 
B 1 110 ILE 110 110 110 ILE ILE B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 ASP 113 113 113 ASP ASP B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 CYS 121 121 121 CYS CYS B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 ASP 123 123 123 ASP ASP B . n 
B 1 124 GLN 124 124 124 GLN GLN B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 CYS 126 126 126 CYS CYS B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 PHE 130 130 130 PHE PHE B . n 
B 1 131 LYS 131 131 131 LYS LYS B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 LYS 133 133 133 LYS LYS B . 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 A . 
D 3 ACY 1   202 1   ACY ACT A . 
E 2 ZFJ 1   301 301 ZFJ LIG B . 
F 3 ACY 1   302 2   ACY ACT B . 
G 4 HOH 1   301 272 HOH HOH A . 
G 4 HOH 2   302 283 HOH HOH A . 
G 4 HOH 3   303 195 HOH HOH A . 
G 4 HOH 4   304 180 HOH HOH A . 
G 4 HOH 5   305 232 HOH HOH A . 
G 4 HOH 6   306 279 HOH HOH A . 
G 4 HOH 7   307 238 HOH HOH A . 
G 4 HOH 8   308 270 HOH HOH A . 
G 4 HOH 9   309 240 HOH HOH A . 
G 4 HOH 10  310 196 HOH HOH A . 
G 4 HOH 11  311 88  HOH HOH A . 
G 4 HOH 12  312 44  HOH HOH A . 
G 4 HOH 13  313 170 HOH HOH A . 
G 4 HOH 14  314 303 HOH HOH A . 
G 4 HOH 15  315 91  HOH HOH A . 
G 4 HOH 16  316 308 HOH HOH A . 
G 4 HOH 17  317 72  HOH HOH A . 
G 4 HOH 18  318 206 HOH HOH A . 
G 4 HOH 19  319 36  HOH HOH A . 
G 4 HOH 20  320 152 HOH HOH A . 
G 4 HOH 21  321 178 HOH HOH A . 
G 4 HOH 22  322 154 HOH HOH A . 
G 4 HOH 23  323 105 HOH HOH A . 
G 4 HOH 24  324 74  HOH HOH A . 
G 4 HOH 25  325 265 HOH HOH A . 
G 4 HOH 26  326 179 HOH HOH A . 
G 4 HOH 27  327 135 HOH HOH A . 
G 4 HOH 28  328 245 HOH HOH A . 
G 4 HOH 29  329 193 HOH HOH A . 
G 4 HOH 30  330 222 HOH HOH A . 
G 4 HOH 31  331 77  HOH HOH A . 
G 4 HOH 32  332 69  HOH HOH A . 
G 4 HOH 33  333 226 HOH HOH A . 
G 4 HOH 34  334 86  HOH HOH A . 
G 4 HOH 35  335 1   HOH HOH A . 
G 4 HOH 36  336 18  HOH HOH A . 
G 4 HOH 37  337 127 HOH HOH A . 
G 4 HOH 38  338 23  HOH HOH A . 
G 4 HOH 39  339 95  HOH HOH A . 
G 4 HOH 40  340 22  HOH HOH A . 
G 4 HOH 41  341 42  HOH HOH A . 
G 4 HOH 42  342 124 HOH HOH A . 
G 4 HOH 43  343 11  HOH HOH A . 
G 4 HOH 44  344 4   HOH HOH A . 
G 4 HOH 45  345 39  HOH HOH A . 
G 4 HOH 46  346 311 HOH HOH A . 
G 4 HOH 47  347 144 HOH HOH A . 
G 4 HOH 48  348 19  HOH HOH A . 
G 4 HOH 49  349 14  HOH HOH A . 
G 4 HOH 50  350 54  HOH HOH A . 
G 4 HOH 51  351 291 HOH HOH A . 
G 4 HOH 52  352 217 HOH HOH A . 
G 4 HOH 53  353 160 HOH HOH A . 
G 4 HOH 54  354 239 HOH HOH A . 
G 4 HOH 55  355 51  HOH HOH A . 
G 4 HOH 56  356 106 HOH HOH A . 
G 4 HOH 57  357 27  HOH HOH A . 
G 4 HOH 58  358 126 HOH HOH A . 
G 4 HOH 59  359 30  HOH HOH A . 
G 4 HOH 60  360 165 HOH HOH A . 
G 4 HOH 61  361 295 HOH HOH A . 
G 4 HOH 62  362 66  HOH HOH A . 
G 4 HOH 63  363 46  HOH HOH A . 
G 4 HOH 64  364 62  HOH HOH A . 
G 4 HOH 65  365 192 HOH HOH A . 
G 4 HOH 66  366 53  HOH HOH A . 
G 4 HOH 67  367 57  HOH HOH A . 
G 4 HOH 68  368 34  HOH HOH A . 
G 4 HOH 69  369 17  HOH HOH A . 
G 4 HOH 70  370 5   HOH HOH A . 
G 4 HOH 71  371 33  HOH HOH A . 
G 4 HOH 72  372 28  HOH HOH A . 
G 4 HOH 73  373 264 HOH HOH A . 
G 4 HOH 74  374 313 HOH HOH A . 
G 4 HOH 75  375 78  HOH HOH A . 
G 4 HOH 76  376 43  HOH HOH A . 
G 4 HOH 77  377 136 HOH HOH A . 
G 4 HOH 78  378 271 HOH HOH A . 
G 4 HOH 79  379 294 HOH HOH A . 
G 4 HOH 80  380 25  HOH HOH A . 
G 4 HOH 81  381 138 HOH HOH A . 
G 4 HOH 82  382 207 HOH HOH A . 
G 4 HOH 83  383 104 HOH HOH A . 
G 4 HOH 84  384 212 HOH HOH A . 
G 4 HOH 85  385 225 HOH HOH A . 
G 4 HOH 86  386 63  HOH HOH A . 
G 4 HOH 87  387 244 HOH HOH A . 
G 4 HOH 88  388 87  HOH HOH A . 
G 4 HOH 89  389 173 HOH HOH A . 
G 4 HOH 90  390 157 HOH HOH A . 
G 4 HOH 91  391 58  HOH HOH A . 
G 4 HOH 92  392 83  HOH HOH A . 
G 4 HOH 93  393 61  HOH HOH A . 
G 4 HOH 94  394 65  HOH HOH A . 
G 4 HOH 95  395 146 HOH HOH A . 
G 4 HOH 96  396 297 HOH HOH A . 
G 4 HOH 97  397 94  HOH HOH A . 
G 4 HOH 98  398 107 HOH HOH A . 
G 4 HOH 99  399 49  HOH HOH A . 
G 4 HOH 100 400 9   HOH HOH A . 
G 4 HOH 101 401 139 HOH HOH A . 
G 4 HOH 102 402 140 HOH HOH A . 
G 4 HOH 103 403 252 HOH HOH A . 
G 4 HOH 104 404 102 HOH HOH A . 
G 4 HOH 105 405 64  HOH HOH A . 
G 4 HOH 106 406 200 HOH HOH A . 
G 4 HOH 107 407 151 HOH HOH A . 
G 4 HOH 108 408 158 HOH HOH A . 
G 4 HOH 109 409 132 HOH HOH A . 
G 4 HOH 110 410 181 HOH HOH A . 
G 4 HOH 111 411 209 HOH HOH A . 
G 4 HOH 112 412 185 HOH HOH A . 
G 4 HOH 113 413 267 HOH HOH A . 
G 4 HOH 114 414 227 HOH HOH A . 
G 4 HOH 115 415 150 HOH HOH A . 
G 4 HOH 116 416 310 HOH HOH A . 
G 4 HOH 117 417 98  HOH HOH A . 
G 4 HOH 118 418 108 HOH HOH A . 
G 4 HOH 119 419 213 HOH HOH A . 
G 4 HOH 120 420 236 HOH HOH A . 
G 4 HOH 121 421 286 HOH HOH A . 
G 4 HOH 122 422 257 HOH HOH A . 
G 4 HOH 123 423 288 HOH HOH A . 
G 4 HOH 124 424 314 HOH HOH A . 
G 4 HOH 125 425 111 HOH HOH A . 
G 4 HOH 126 426 129 HOH HOH A . 
G 4 HOH 127 427 301 HOH HOH A . 
G 4 HOH 128 428 249 HOH HOH A . 
G 4 HOH 129 429 191 HOH HOH A . 
G 4 HOH 130 430 82  HOH HOH A . 
G 4 HOH 131 431 56  HOH HOH A . 
G 4 HOH 132 432 85  HOH HOH A . 
G 4 HOH 133 433 93  HOH HOH A . 
G 4 HOH 134 434 253 HOH HOH A . 
G 4 HOH 135 435 282 HOH HOH A . 
G 4 HOH 136 436 285 HOH HOH A . 
G 4 HOH 137 437 312 HOH HOH A . 
G 4 HOH 138 438 233 HOH HOH A . 
G 4 HOH 139 439 275 HOH HOH A . 
G 4 HOH 140 440 130 HOH HOH A . 
G 4 HOH 141 441 118 HOH HOH A . 
G 4 HOH 142 442 290 HOH HOH A . 
G 4 HOH 143 443 235 HOH HOH A . 
G 4 HOH 144 444 92  HOH HOH A . 
G 4 HOH 145 445 208 HOH HOH A . 
G 4 HOH 146 446 155 HOH HOH A . 
H 4 HOH 1   401 220 HOH HOH B . 
H 4 HOH 2   402 147 HOH HOH B . 
H 4 HOH 3   403 246 HOH HOH B . 
H 4 HOH 4   404 119 HOH HOH B . 
H 4 HOH 5   405 266 HOH HOH B . 
H 4 HOH 6   406 273 HOH HOH B . 
H 4 HOH 7   407 174 HOH HOH B . 
H 4 HOH 8   408 205 HOH HOH B . 
H 4 HOH 9   409 198 HOH HOH B . 
H 4 HOH 10  410 231 HOH HOH B . 
H 4 HOH 11  411 117 HOH HOH B . 
H 4 HOH 12  412 90  HOH HOH B . 
H 4 HOH 13  413 164 HOH HOH B . 
H 4 HOH 14  414 250 HOH HOH B . 
H 4 HOH 15  415 194 HOH HOH B . 
H 4 HOH 16  416 109 HOH HOH B . 
H 4 HOH 17  417 214 HOH HOH B . 
H 4 HOH 18  418 242 HOH HOH B . 
H 4 HOH 19  419 41  HOH HOH B . 
H 4 HOH 20  420 52  HOH HOH B . 
H 4 HOH 21  421 110 HOH HOH B . 
H 4 HOH 22  422 141 HOH HOH B . 
H 4 HOH 23  423 162 HOH HOH B . 
H 4 HOH 24  424 48  HOH HOH B . 
H 4 HOH 25  425 37  HOH HOH B . 
H 4 HOH 26  426 223 HOH HOH B . 
H 4 HOH 27  427 67  HOH HOH B . 
H 4 HOH 28  428 112 HOH HOH B . 
H 4 HOH 29  429 182 HOH HOH B . 
H 4 HOH 30  430 76  HOH HOH B . 
H 4 HOH 31  431 31  HOH HOH B . 
H 4 HOH 32  432 188 HOH HOH B . 
H 4 HOH 33  433 167 HOH HOH B . 
H 4 HOH 34  434 171 HOH HOH B . 
H 4 HOH 35  435 201 HOH HOH B . 
H 4 HOH 36  436 122 HOH HOH B . 
H 4 HOH 37  437 10  HOH HOH B . 
H 4 HOH 38  438 218 HOH HOH B . 
H 4 HOH 39  439 197 HOH HOH B . 
H 4 HOH 40  440 121 HOH HOH B . 
H 4 HOH 41  441 300 HOH HOH B . 
H 4 HOH 42  442 6   HOH HOH B . 
H 4 HOH 43  443 89  HOH HOH B . 
H 4 HOH 44  444 100 HOH HOH B . 
H 4 HOH 45  445 302 HOH HOH B . 
H 4 HOH 46  446 13  HOH HOH B . 
H 4 HOH 47  447 169 HOH HOH B . 
H 4 HOH 48  448 307 HOH HOH B . 
H 4 HOH 49  449 137 HOH HOH B . 
H 4 HOH 50  450 70  HOH HOH B . 
H 4 HOH 51  451 68  HOH HOH B . 
H 4 HOH 52  452 199 HOH HOH B . 
H 4 HOH 53  453 166 HOH HOH B . 
H 4 HOH 54  454 186 HOH HOH B . 
H 4 HOH 55  455 24  HOH HOH B . 
H 4 HOH 56  456 8   HOH HOH B . 
H 4 HOH 57  457 73  HOH HOH B . 
H 4 HOH 58  458 131 HOH HOH B . 
H 4 HOH 59  459 168 HOH HOH B . 
H 4 HOH 60  460 276 HOH HOH B . 
H 4 HOH 61  461 79  HOH HOH B . 
H 4 HOH 62  462 3   HOH HOH B . 
H 4 HOH 63  463 21  HOH HOH B . 
H 4 HOH 64  464 163 HOH HOH B . 
H 4 HOH 65  465 20  HOH HOH B . 
H 4 HOH 66  466 304 HOH HOH B . 
H 4 HOH 67  467 306 HOH HOH B . 
H 4 HOH 68  468 32  HOH HOH B . 
H 4 HOH 69  469 115 HOH HOH B . 
H 4 HOH 70  470 26  HOH HOH B . 
H 4 HOH 71  471 55  HOH HOH B . 
H 4 HOH 72  472 184 HOH HOH B . 
H 4 HOH 73  473 116 HOH HOH B . 
H 4 HOH 74  474 12  HOH HOH B . 
H 4 HOH 75  475 2   HOH HOH B . 
H 4 HOH 76  476 60  HOH HOH B . 
H 4 HOH 77  477 269 HOH HOH B . 
H 4 HOH 78  478 75  HOH HOH B . 
H 4 HOH 79  479 190 HOH HOH B . 
H 4 HOH 80  480 80  HOH HOH B . 
H 4 HOH 81  481 40  HOH HOH B . 
H 4 HOH 82  482 216 HOH HOH B . 
H 4 HOH 83  483 15  HOH HOH B . 
H 4 HOH 84  484 16  HOH HOH B . 
H 4 HOH 85  485 305 HOH HOH B . 
H 4 HOH 86  486 211 HOH HOH B . 
H 4 HOH 87  487 38  HOH HOH B . 
H 4 HOH 88  488 280 HOH HOH B . 
H 4 HOH 89  489 153 HOH HOH B . 
H 4 HOH 90  490 259 HOH HOH B . 
H 4 HOH 91  491 161 HOH HOH B . 
H 4 HOH 92  492 35  HOH HOH B . 
H 4 HOH 93  493 29  HOH HOH B . 
H 4 HOH 94  494 284 HOH HOH B . 
H 4 HOH 95  495 204 HOH HOH B . 
H 4 HOH 96  496 228 HOH HOH B . 
H 4 HOH 97  497 84  HOH HOH B . 
H 4 HOH 98  498 274 HOH HOH B . 
H 4 HOH 99  499 101 HOH HOH B . 
H 4 HOH 100 500 99  HOH HOH B . 
H 4 HOH 101 501 298 HOH HOH B . 
H 4 HOH 102 502 148 HOH HOH B . 
H 4 HOH 103 503 50  HOH HOH B . 
H 4 HOH 104 504 149 HOH HOH B . 
H 4 HOH 105 505 81  HOH HOH B . 
H 4 HOH 106 506 134 HOH HOH B . 
H 4 HOH 107 507 254 HOH HOH B . 
H 4 HOH 108 508 47  HOH HOH B . 
H 4 HOH 109 509 114 HOH HOH B . 
H 4 HOH 110 510 7   HOH HOH B . 
H 4 HOH 111 511 175 HOH HOH B . 
H 4 HOH 112 512 187 HOH HOH B . 
H 4 HOH 113 513 287 HOH HOH B . 
H 4 HOH 114 514 255 HOH HOH B . 
H 4 HOH 115 515 262 HOH HOH B . 
H 4 HOH 116 516 183 HOH HOH B . 
H 4 HOH 117 517 120 HOH HOH B . 
H 4 HOH 118 518 123 HOH HOH B . 
H 4 HOH 119 519 219 HOH HOH B . 
H 4 HOH 120 520 142 HOH HOH B . 
H 4 HOH 121 521 299 HOH HOH B . 
H 4 HOH 122 522 125 HOH HOH B . 
H 4 HOH 123 523 260 HOH HOH B . 
H 4 HOH 124 524 113 HOH HOH B . 
H 4 HOH 125 525 221 HOH HOH B . 
H 4 HOH 126 526 293 HOH HOH B . 
H 4 HOH 127 527 281 HOH HOH B . 
H 4 HOH 128 528 261 HOH HOH B . 
H 4 HOH 129 529 234 HOH HOH B . 
H 4 HOH 130 530 251 HOH HOH B . 
H 4 HOH 131 531 143 HOH HOH B . 
H 4 HOH 132 532 96  HOH HOH B . 
H 4 HOH 133 533 156 HOH HOH B . 
H 4 HOH 134 534 241 HOH HOH B . 
H 4 HOH 135 535 277 HOH HOH B . 
H 4 HOH 136 536 237 HOH HOH B . 
H 4 HOH 137 537 229 HOH HOH B . 
H 4 HOH 138 538 278 HOH HOH B . 
H 4 HOH 139 539 247 HOH HOH B . 
H 4 HOH 140 540 243 HOH HOH B . 
H 4 HOH 141 541 176 HOH HOH B . 
H 4 HOH 142 542 224 HOH HOH B . 
H 4 HOH 143 543 309 HOH HOH B . 
H 4 HOH 144 544 189 HOH HOH B . 
H 4 HOH 145 545 59  HOH HOH B . 
H 4 HOH 146 546 97  HOH HOH B . 
H 4 HOH 147 547 71  HOH HOH B . 
H 4 HOH 148 548 45  HOH HOH B . 
H 4 HOH 149 549 215 HOH HOH B . 
H 4 HOH 150 550 203 HOH HOH B . 
H 4 HOH 151 551 296 HOH HOH B . 
H 4 HOH 152 552 177 HOH HOH B . 
H 4 HOH 153 553 263 HOH HOH B . 
H 4 HOH 154 554 133 HOH HOH B . 
H 4 HOH 155 555 128 HOH HOH B . 
H 4 HOH 156 556 159 HOH HOH B . 
H 4 HOH 157 557 292 HOH HOH B . 
H 4 HOH 158 558 258 HOH HOH B . 
H 4 HOH 159 559 289 HOH HOH B . 
# 
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 0 A ASP 47  ? OD1 ? A ASP 47  OD1 
2  1 Y 0 A ASN 59  ? ND2 ? A ASN 59  ND2 
3  1 Y 0 A SER 76  ? CB  ? A SER 76  CB  
4  1 Y 0 A LYS 83  ? CD  ? A LYS 83  CD  
5  1 Y 0 A LYS 83  ? CE  ? A LYS 83  CE  
6  1 Y 0 A ASP 113 ? CG  ? A ASP 113 CG  
7  1 Y 0 A ASP 113 ? OD1 ? A ASP 113 OD1 
8  1 Y 0 A ASP 113 ? OD2 ? A ASP 113 OD2 
9  1 Y 1 A LYS 133 ? O   ? A LYS 133 O   
10 1 Y 0 B ASP 47  ? OD1 ? B ASP 47  OD1 
11 1 Y 0 B ASN 59  ? ND2 ? B ASN 59  ND2 
12 1 Y 0 B SER 76  ? CB  ? B SER 76  CB  
13 1 Y 0 B LYS 83  ? CD  ? B LYS 83  CD  
14 1 Y 0 B LYS 83  ? CE  ? B LYS 83  CE  
15 1 Y 0 B ASP 113 ? CG  ? B ASP 113 CG  
16 1 Y 0 B ASP 113 ? OD1 ? B ASP 113 OD1 
17 1 Y 0 B ASP 113 ? OD2 ? B ASP 113 OD2 
18 1 Y 1 B LYS 131 ? CG  ? B LYS 131 CG  
19 1 Y 1 B LYS 131 ? CD  ? B LYS 131 CD  
20 1 Y 1 B LYS 131 ? CE  ? B LYS 131 CE  
21 1 Y 1 B LYS 131 ? NZ  ? B LYS 131 NZ  
22 1 Y 1 B LYS 133 ? O   ? B LYS 133 O   
# 
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   ? ? ? 1.16-3549 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .         4 
# 
_cell.angle_alpha                  85.660 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   86.040 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  65.170 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D8M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     31.171 
_cell.length_a_esd                 ? 
_cell.length_b                     35.859 
_cell.length_b_esd                 ? 
_cell.length_c                     64.046 
_cell.length_c_esd                 ? 
_cell.volume                       64729.046 
_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                         9D8M 
_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                   9D8M 
_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          40.87 
_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   ? 
_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         2021-01-27 
_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   1.00 
_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 23-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D8M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.201 
_reflns.d_resolution_low                               28.27 
_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                                     74135 
_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                           94.79 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.8780 
_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                                    1.201 
_reflns_shell.d_res_low                                     1.244 
_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                             7114 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.8780 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                               17.49 
_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                                 9D8M 
_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                            1.201 
_refine.ls_d_res_low                             28.27 
_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                     74133 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.79 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2039 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1929 
_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.pdbx_number_atoms_protein        2182 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             305 
_refine_hist.number_atoms_total               2541 
_refine_hist.d_res_high                       1.201 
_refine_hist.d_res_low                        28.27 
# 
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' ? 0.0072  ? 2282 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8757  ? 3084 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0793  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0043  ? 386  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.1438 ? 1314 ? f_dihedral_angle_d ? ? 
# 
_struct.entry_id                     9D8M 
_struct.title                        
'Q108K:K40L:T51V:T53C:R58W:Y19W:Q38L:Q4A:T29L mutant of hCRBPII bound to FR1V fluorophore in the dark state at pH 4' 
_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        9D8M 
_struct_keywords.text            
;human cellular retinol binding protein II, hCRBPII, retinal binding protein, protein engineering, fluorescent protein, 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 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_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 9D8M A 1 ? 133 ? P50120 2 ? 134 ? 1 133 
2 1 9D8M B 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 9D8M ALA A 4   ? UNP P50120 GLN 5   'engineered mutation' 4   1  
1 9D8M TRP A 19  ? UNP P50120 TYR 20  'engineered mutation' 19  2  
1 9D8M LEU A 29  ? UNP P50120 THR 30  'engineered mutation' 29  3  
1 9D8M LEU A 38  ? UNP P50120 GLN 39  'engineered mutation' 38  4  
1 9D8M LEU A 40  ? UNP P50120 LYS 41  'engineered mutation' 40  5  
1 9D8M VAL A 51  ? UNP P50120 THR 52  'engineered mutation' 51  6  
1 9D8M CYS A 53  ? UNP P50120 THR 54  'engineered mutation' 53  7  
1 9D8M TRP A 58  ? UNP P50120 ARG 59  'engineered mutation' 58  8  
1 9D8M SER A 95  ? UNP P50120 CYS 96  conflict              95  9  
1 9D8M LYS A 108 ? UNP P50120 GLN 109 'engineered mutation' 108 10 
2 9D8M ALA B 4   ? UNP P50120 GLN 5   'engineered mutation' 4   11 
2 9D8M TRP B 19  ? UNP P50120 TYR 20  'engineered mutation' 19  12 
2 9D8M LEU B 29  ? UNP P50120 THR 30  'engineered mutation' 29  13 
2 9D8M LEU B 38  ? UNP P50120 GLN 39  'engineered mutation' 38  14 
2 9D8M LEU B 40  ? UNP P50120 LYS 41  'engineered mutation' 40  15 
2 9D8M VAL B 51  ? UNP P50120 THR 52  'engineered mutation' 51  16 
2 9D8M CYS B 53  ? UNP P50120 THR 54  'engineered mutation' 53  17 
2 9D8M TRP B 58  ? UNP P50120 ARG 59  'engineered mutation' 58  18 
2 9D8M SER B 95  ? UNP P50120 CYS 96  conflict              95  19 
2 9D8M LYS B 108 ? UNP P50120 GLN 109 'engineered mutation' 108 20 
# 
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,G 
2 1 B,E,F,H 
# 
_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 A 15 LEU A 23 1 ? 9 
HELX_P HELX_P2 AA2 ASP A 26 ? VAL A 34 ? ASP A 26 VAL A 34 1 ? 9 
HELX_P HELX_P3 AA3 ASN B 15 ? LEU B 23 ? ASN B 15 LEU B 23 1 ? 9 
HELX_P HELX_P4 AA4 ASP B 26 ? VAL B 34 ? ASP B 26 VAL B 34 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           LYS 
_struct_conn.ptnr1_label_seq_id            108 
_struct_conn.ptnr1_label_atom_id           NZ 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           C 
_struct_conn.ptnr2_label_comp_id           ZFJ 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C23 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            LYS 
_struct_conn.ptnr1_auth_seq_id             108 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            ZFJ 
_struct_conn.ptnr2_auth_seq_id             201 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.415 
_struct_conn.pdbx_value_order              doub 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      ZFJ 
_pdbx_modification_feature.label_asym_id                      C 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     LYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      108 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       ZFJ 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        201 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      LYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       108 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C23 
_pdbx_modification_feature.modified_residue_id_linking_atom   NZ 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        ZFJ 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           '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 A 59  THR A 65  
AA1 2  ASN A 48  ? THR A 54  ? ASN A 48  THR A 54  
AA1 3  THR A 39  ? ASP A 45  ? THR A 39  ASP A 45  
AA1 4  GLY A 6   ? GLU A 14  ? GLY A 6   GLU A 14  
AA1 5  GLN A 124 ? LYS A 132 ? GLN A 124 LYS A 132 
AA1 6  LYS A 114 ? CYS A 121 ? LYS A 114 CYS A 121 
AA1 7  GLY A 105 ? GLU A 111 ? GLY A 105 GLU A 111 
AA1 8  VAL A 92  ? LYS A 98  ? VAL A 92  LYS A 98  
AA1 9  HIS A 81  ? GLU A 89  ? HIS A 81  GLU A 89  
AA1 10 PHE A 70  ? TYR A 73  ? PHE A 70  TYR A 73  
AA2 1  ASN B 59  ? THR B 65  ? ASN B 59  THR B 65  
AA2 2  ASN B 48  ? THR B 54  ? ASN B 48  THR B 54  
AA2 3  THR B 39  ? ASP B 45  ? THR B 39  ASP B 45  
AA2 4  GLY B 6   ? GLU B 14  ? GLY B 6   GLU B 14  
AA2 5  GLN B 124 ? LYS B 132 ? GLN B 124 LYS B 132 
AA2 6  LYS B 114 ? CYS B 121 ? LYS B 114 CYS B 121 
AA2 7  GLY B 105 ? GLU B 111 ? GLY B 105 GLU B 111 
AA2 8  VAL B 92  ? LYS B 98  ? VAL B 92  LYS B 98  
AA2 9  HIS B 81  ? GLU B 89  ? HIS B 81  GLU B 89  
AA2 10 PHE B 70  ? TYR B 73  ? PHE B 70  TYR B 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 PHE A 64  ? O PHE A 64  N PHE A 49  ? N PHE A 49  
AA1 2 3  O ASN A 48  ? O ASN A 48  N ASP A 45  ? N ASP A 45  
AA1 3 4  O LEU A 40  ? O LEU A 40  N TRP A 8   ? N TRP A 8   
AA1 4 5  N GLU A 11  ? N GLU A 11  O VAL A 129 ? O VAL A 129 
AA1 5 6  O GLN A 128 ? O GLN A 128 N LEU A 117 ? N LEU A 117 
AA1 6 7  O LYS A 114 ? O LYS A 114 N GLU A 111 ? N GLU A 111 
AA1 7 8  O TRP A 106 ? O TRP A 106 N SER A 95  ? N SER A 95  
AA1 8 9  O VAL A 94  ? O VAL A 94  N THR A 87  ? N THR A 87  
AA1 9 10 O VAL A 82  ? O VAL A 82  N GLU A 72  ? N GLU A 72  
AA2 1 2  O PHE B 64  ? O PHE B 64  N PHE B 49  ? N PHE B 49  
AA2 2 3  O LYS B 52  ? O LYS B 52  N VAL B 41  ? N VAL B 41  
AA2 3 4  O LEU B 40  ? O LEU B 40  N TRP B 8   ? N TRP B 8   
AA2 4 5  N GLU B 11  ? N GLU B 11  O VAL B 129 ? O VAL B 129 
AA2 5 6  O GLN B 128 ? O GLN B 128 N LEU B 117 ? N LEU B 117 
AA2 6 7  O LYS B 114 ? O LYS B 114 N GLU B 111 ? N GLU B 111 
AA2 7 8  O TRP B 106 ? O TRP B 106 N SER B 95  ? N SER B 95  
AA2 8 9  O VAL B 94  ? O VAL B 94  N THR B 87  ? N THR B 87  
AA2 9 10 O ALA B 84  ? O ALA B 84  N PHE B 70  ? N PHE B 70  
# 
_pdbx_entry_details.entry_id                   9D8M 
_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 NZ  B LYS 108 ? ? C23 B ZFJ 301 ? ? 1.16 
2  1 O   B HOH 445 ? ? O   B HOH 467 ? ? 1.78 
3  1 O   B HOH 413 ? ? O   B HOH 485 ? ? 1.91 
4  1 O   A HOH 368 ? ? O   A HOH 414 ? ? 1.93 
5  1 O   B HOH 441 ? ? O   B HOH 537 ? ? 1.93 
6  1 O   A HOH 377 ? ? O   A HOH 428 ? ? 1.99 
7  1 OH  B TYR 73  ? ? O   B HOH 401 ? ? 1.99 
8  1 O   B HOH 444 ? ? O   B HOH 537 ? ? 2.02 
9  1 O   B HOH 501 ? ? O   B HOH 513 ? ? 2.04 
10 1 O   B HOH 504 ? ? O   B HOH 523 ? ? 2.07 
11 1 O   B HOH 440 ? ? O   B HOH 490 ? ? 2.08 
12 1 OD1 B ASN 59  ? ? O   B HOH 402 ? ? 2.10 
13 1 NZ  A LYS 21  ? ? O   A HOH 301 ? ? 2.11 
14 1 O   B HOH 526 ? ? O   B HOH 536 ? ? 2.14 
15 1 NH2 A ARG 35  ? ? O   A HOH 302 ? ? 2.14 
16 1 O   B HOH 413 ? ? O   B HOH 445 ? ? 2.15 
17 1 NZ  B LYS 52  ? ? O   B HOH 403 ? ? 2.15 
18 1 O   A HOH 306 ? ? O   B HOH 477 ? ? 2.16 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 395 ? ? 1_555 O A HOH 437 ? ? 1_655 1.95 
2 1 O A HOH 421 ? ? 1_555 O A HOH 437 ? ? 1_655 2.04 
3 1 O A HOH 346 ? ? 1_555 O A HOH 412 ? ? 1_455 2.04 
4 1 O A HOH 320 ? ? 1_555 O A HOH 346 ? ? 1_655 2.08 
5 1 O A HOH 435 ? ? 1_555 O B HOH 537 ? ? 1_656 2.12 
6 1 O A HOH 435 ? ? 1_555 O B HOH 441 ? ? 1_656 2.13 
7 1 O B HOH 488 ? ? 1_555 O B HOH 543 ? ? 1_655 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A SER 95 ? ? OG A SER 95 ? ? 1.555 1.418 0.137 0.013 N 
2 1 CB B SER 95 ? ? OG B SER 95 ? ? 1.568 1.418 0.150 0.013 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 13 ? ? -161.23 102.21  
2 1 LEU A 77 ? ? -112.63 -107.69 
3 1 LEU B 77 ? ? -108.09 -108.35 
# 
_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 
HIS N    N N N 145 
HIS CA   C N S 146 
HIS C    C N N 147 
HIS O    O N N 148 
HIS CB   C N N 149 
HIS CG   C Y N 150 
HIS ND1  N Y N 151 
HIS CD2  C Y N 152 
HIS CE1  C Y N 153 
HIS NE2  N Y N 154 
HIS OXT  O N N 155 
HIS H    H N N 156 
HIS H2   H N N 157 
HIS HA   H N N 158 
HIS HB2  H N N 159 
HIS HB3  H N N 160 
HIS HD1  H N N 161 
HIS HD2  H N N 162 
HIS HE1  H N N 163 
HIS HE2  H N N 164 
HIS HXT  H N N 165 
HOH O    O N N 166 
HOH H1   H N N 167 
HOH H2   H N N 168 
ILE N    N N N 169 
ILE CA   C N S 170 
ILE C    C N N 171 
ILE O    O N N 172 
ILE CB   C N S 173 
ILE CG1  C N N 174 
ILE CG2  C N N 175 
ILE CD1  C N N 176 
ILE OXT  O N N 177 
ILE H    H N N 178 
ILE H2   H N N 179 
ILE HA   H N N 180 
ILE HB   H N N 181 
ILE HG12 H N N 182 
ILE HG13 H N N 183 
ILE HG21 H N N 184 
ILE HG22 H N N 185 
ILE HG23 H N N 186 
ILE HD11 H N N 187 
ILE HD12 H N N 188 
ILE HD13 H N N 189 
ILE HXT  H N N 190 
LEU N    N N N 191 
LEU CA   C N S 192 
LEU C    C N N 193 
LEU O    O N N 194 
LEU CB   C N N 195 
LEU CG   C N N 196 
LEU CD1  C N N 197 
LEU CD2  C N N 198 
LEU OXT  O N N 199 
LEU H    H N N 200 
LEU H2   H N N 201 
LEU HA   H N N 202 
LEU HB2  H N N 203 
LEU HB3  H N N 204 
LEU HG   H N N 205 
LEU HD11 H N N 206 
LEU HD12 H N N 207 
LEU HD13 H N N 208 
LEU HD21 H N N 209 
LEU HD22 H N N 210 
LEU HD23 H N N 211 
LEU HXT  H N N 212 
LYS N    N N N 213 
LYS CA   C N S 214 
LYS C    C N N 215 
LYS O    O N N 216 
LYS CB   C N N 217 
LYS CG   C N N 218 
LYS CD   C N N 219 
LYS CE   C N N 220 
LYS NZ   N N N 221 
LYS OXT  O N N 222 
LYS H    H N N 223 
LYS H2   H N N 224 
LYS HA   H N N 225 
LYS HB2  H N N 226 
LYS HB3  H N N 227 
LYS HG2  H N N 228 
LYS HG3  H N N 229 
LYS HD2  H N N 230 
LYS HD3  H N N 231 
LYS HE2  H N N 232 
LYS HE3  H N N 233 
LYS HZ1  H N N 234 
LYS HZ2  H N N 235 
LYS HZ3  H N N 236 
LYS HXT  H N N 237 
MET N    N N N 238 
MET CA   C N S 239 
MET C    C N N 240 
MET O    O N N 241 
MET CB   C N N 242 
MET CG   C N N 243 
MET SD   S N N 244 
MET CE   C N N 245 
MET OXT  O N N 246 
MET H    H N N 247 
MET H2   H N N 248 
MET HA   H N N 249 
MET HB2  H N N 250 
MET HB3  H N N 251 
MET HG2  H N N 252 
MET HG3  H N N 253 
MET HE1  H N N 254 
MET HE2  H N N 255 
MET HE3  H N N 256 
MET HXT  H N N 257 
PHE N    N N N 258 
PHE CA   C N S 259 
PHE C    C N N 260 
PHE O    O N N 261 
PHE CB   C N N 262 
PHE CG   C Y N 263 
PHE CD1  C Y N 264 
PHE CD2  C Y N 265 
PHE CE1  C Y N 266 
PHE CE2  C Y N 267 
PHE CZ   C Y N 268 
PHE OXT  O N N 269 
PHE H    H N N 270 
PHE H2   H N N 271 
PHE HA   H N N 272 
PHE HB2  H N N 273 
PHE HB3  H N N 274 
PHE HD1  H N N 275 
PHE HD2  H N N 276 
PHE HE1  H N N 277 
PHE HE2  H N N 278 
PHE HZ   H N N 279 
PHE HXT  H N N 280 
SER N    N N N 281 
SER CA   C N S 282 
SER C    C N N 283 
SER O    O N N 284 
SER CB   C N N 285 
SER OG   O N N 286 
SER OXT  O N N 287 
SER H    H N N 288 
SER H2   H N N 289 
SER HA   H N N 290 
SER HB2  H N N 291 
SER HB3  H N N 292 
SER HG   H N N 293 
SER HXT  H N N 294 
THR N    N N N 295 
THR CA   C N S 296 
THR C    C N N 297 
THR O    O N N 298 
THR CB   C N R 299 
THR OG1  O N N 300 
THR CG2  C N N 301 
THR OXT  O N N 302 
THR H    H N N 303 
THR H2   H N N 304 
THR HA   H N N 305 
THR HB   H N N 306 
THR HG1  H N N 307 
THR HG21 H N N 308 
THR HG22 H N N 309 
THR HG23 H N N 310 
THR HXT  H N N 311 
TRP N    N N N 312 
TRP CA   C N S 313 
TRP C    C N N 314 
TRP O    O N N 315 
TRP CB   C N N 316 
TRP CG   C Y N 317 
TRP CD1  C Y N 318 
TRP CD2  C Y N 319 
TRP NE1  N Y N 320 
TRP CE2  C Y N 321 
TRP CE3  C Y N 322 
TRP CZ2  C Y N 323 
TRP CZ3  C Y N 324 
TRP CH2  C Y N 325 
TRP OXT  O N N 326 
TRP H    H N N 327 
TRP H2   H N N 328 
TRP HA   H N N 329 
TRP HB2  H N N 330 
TRP HB3  H N N 331 
TRP HD1  H N N 332 
TRP HE1  H N N 333 
TRP HE3  H N N 334 
TRP HZ2  H N N 335 
TRP HZ3  H N N 336 
TRP HH2  H N N 337 
TRP HXT  H N N 338 
TYR N    N N N 339 
TYR CA   C N S 340 
TYR C    C N N 341 
TYR O    O N N 342 
TYR CB   C N N 343 
TYR CG   C Y N 344 
TYR CD1  C Y N 345 
TYR CD2  C Y N 346 
TYR CE1  C Y N 347 
TYR CE2  C Y N 348 
TYR CZ   C Y N 349 
TYR OH   O N N 350 
TYR OXT  O N N 351 
TYR H    H N N 352 
TYR H2   H N N 353 
TYR HA   H N N 354 
TYR HB2  H N N 355 
TYR HB3  H N N 356 
TYR HD1  H N N 357 
TYR HD2  H N N 358 
TYR HE1  H N N 359 
TYR HE2  H N N 360 
TYR HH   H N N 361 
TYR HXT  H N N 362 
VAL N    N N N 363 
VAL CA   C N S 364 
VAL C    C N N 365 
VAL O    O N N 366 
VAL CB   C N N 367 
VAL CG1  C N N 368 
VAL CG2  C N N 369 
VAL OXT  O N N 370 
VAL H    H N N 371 
VAL H2   H N N 372 
VAL HA   H N N 373 
VAL HB   H N N 374 
VAL HG11 H N N 375 
VAL HG12 H N N 376 
VAL HG13 H N N 377 
VAL HG21 H N N 378 
VAL HG22 H N N 379 
VAL HG23 H N N 380 
VAL HXT  H N N 381 
ZFJ C10  C Y N 382 
ZFJ C13  C Y N 383 
ZFJ C15  C N N 384 
ZFJ C17  C N N 385 
ZFJ C20  C N N 386 
ZFJ C21  C N N 387 
ZFJ C22  C N N 388 
ZFJ C01  C Y N 389 
ZFJ C02  C Y N 390 
ZFJ C03  C Y N 391 
ZFJ C04  C Y N 392 
ZFJ C05  C Y N 393 
ZFJ C06  C Y N 394 
ZFJ C07  C Y N 395 
ZFJ C08  C Y N 396 
ZFJ C09  C N N 397 
ZFJ C11  C Y N 398 
ZFJ C12  C Y N 399 
ZFJ C14  C N N 400 
ZFJ C18  C N N 401 
ZFJ C19  C N N 402 
ZFJ C23  C N N 403 
ZFJ N16  N N N 404 
ZFJ H1   H N N 405 
ZFJ H2   H N N 406 
ZFJ H3   H N N 407 
ZFJ H4   H N N 408 
ZFJ H5   H N N 409 
ZFJ H6   H N N 410 
ZFJ H7   H N N 411 
ZFJ H8   H N N 412 
ZFJ H9   H N N 413 
ZFJ H10  H N N 414 
ZFJ H11  H N N 415 
ZFJ H12  H N N 416 
ZFJ H13  H N N 417 
ZFJ H14  H N N 418 
ZFJ H15  H N N 419 
ZFJ H16  H N N 420 
ZFJ H17  H N N 421 
ZFJ H18  H N N 422 
ZFJ H19  H N N 423 
ZFJ H20  H N N 424 
ZFJ H21  H N N 425 
ZFJ H22  H N N 426 
ZFJ H23  H N N 427 
ZFJ H24  H N N 428 
ZFJ H25  H N N 429 
ZFJ H26  H N N 430 
ZFJ H27  H N N 431 
# 
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 
HIS N   CA   sing N N 136 
HIS N   H    sing N N 137 
HIS N   H2   sing N N 138 
HIS CA  C    sing N N 139 
HIS CA  CB   sing N N 140 
HIS CA  HA   sing N N 141 
HIS C   O    doub N N 142 
HIS C   OXT  sing N N 143 
HIS CB  CG   sing N N 144 
HIS CB  HB2  sing N N 145 
HIS CB  HB3  sing N N 146 
HIS CG  ND1  sing Y N 147 
HIS CG  CD2  doub Y N 148 
HIS ND1 CE1  doub Y N 149 
HIS ND1 HD1  sing N N 150 
HIS CD2 NE2  sing Y N 151 
HIS CD2 HD2  sing N N 152 
HIS CE1 NE2  sing Y N 153 
HIS CE1 HE1  sing N N 154 
HIS NE2 HE2  sing N N 155 
HIS OXT HXT  sing N N 156 
HOH O   H1   sing N N 157 
HOH O   H2   sing N N 158 
ILE N   CA   sing N N 159 
ILE N   H    sing N N 160 
ILE N   H2   sing N N 161 
ILE CA  C    sing N N 162 
ILE CA  CB   sing N N 163 
ILE CA  HA   sing N N 164 
ILE C   O    doub N N 165 
ILE C   OXT  sing N N 166 
ILE CB  CG1  sing N N 167 
ILE CB  CG2  sing N N 168 
ILE CB  HB   sing N N 169 
ILE CG1 CD1  sing N N 170 
ILE CG1 HG12 sing N N 171 
ILE CG1 HG13 sing N N 172 
ILE CG2 HG21 sing N N 173 
ILE CG2 HG22 sing N N 174 
ILE CG2 HG23 sing N N 175 
ILE CD1 HD11 sing N N 176 
ILE CD1 HD12 sing N N 177 
ILE CD1 HD13 sing N N 178 
ILE OXT HXT  sing N N 179 
LEU N   CA   sing N N 180 
LEU N   H    sing N N 181 
LEU N   H2   sing N N 182 
LEU CA  C    sing N N 183 
LEU CA  CB   sing N N 184 
LEU CA  HA   sing N N 185 
LEU C   O    doub N N 186 
LEU C   OXT  sing N N 187 
LEU CB  CG   sing N N 188 
LEU CB  HB2  sing N N 189 
LEU CB  HB3  sing N N 190 
LEU CG  CD1  sing N N 191 
LEU CG  CD2  sing N N 192 
LEU CG  HG   sing N N 193 
LEU CD1 HD11 sing N N 194 
LEU CD1 HD12 sing N N 195 
LEU CD1 HD13 sing N N 196 
LEU CD2 HD21 sing N N 197 
LEU CD2 HD22 sing N N 198 
LEU CD2 HD23 sing N N 199 
LEU OXT HXT  sing N N 200 
LYS N   CA   sing N N 201 
LYS N   H    sing N N 202 
LYS N   H2   sing N N 203 
LYS CA  C    sing N N 204 
LYS CA  CB   sing N N 205 
LYS CA  HA   sing N N 206 
LYS C   O    doub N N 207 
LYS C   OXT  sing N N 208 
LYS CB  CG   sing N N 209 
LYS CB  HB2  sing N N 210 
LYS CB  HB3  sing N N 211 
LYS CG  CD   sing N N 212 
LYS CG  HG2  sing N N 213 
LYS CG  HG3  sing N N 214 
LYS CD  CE   sing N N 215 
LYS CD  HD2  sing N N 216 
LYS CD  HD3  sing N N 217 
LYS CE  NZ   sing N N 218 
LYS CE  HE2  sing N N 219 
LYS CE  HE3  sing N N 220 
LYS NZ  HZ1  sing N N 221 
LYS NZ  HZ2  sing N N 222 
LYS NZ  HZ3  sing N N 223 
LYS OXT HXT  sing N N 224 
MET N   CA   sing N N 225 
MET N   H    sing N N 226 
MET N   H2   sing N N 227 
MET CA  C    sing N N 228 
MET CA  CB   sing N N 229 
MET CA  HA   sing N N 230 
MET C   O    doub N N 231 
MET C   OXT  sing N N 232 
MET CB  CG   sing N N 233 
MET CB  HB2  sing N N 234 
MET CB  HB3  sing N N 235 
MET CG  SD   sing N N 236 
MET CG  HG2  sing N N 237 
MET CG  HG3  sing N N 238 
MET SD  CE   sing N N 239 
MET CE  HE1  sing N N 240 
MET CE  HE2  sing N N 241 
MET CE  HE3  sing N N 242 
MET OXT HXT  sing N N 243 
PHE N   CA   sing N N 244 
PHE N   H    sing N N 245 
PHE N   H2   sing N N 246 
PHE CA  C    sing N N 247 
PHE CA  CB   sing N N 248 
PHE CA  HA   sing N N 249 
PHE C   O    doub N N 250 
PHE C   OXT  sing N N 251 
PHE CB  CG   sing N N 252 
PHE CB  HB2  sing N N 253 
PHE CB  HB3  sing N N 254 
PHE CG  CD1  doub Y N 255 
PHE CG  CD2  sing Y N 256 
PHE CD1 CE1  sing Y N 257 
PHE CD1 HD1  sing N N 258 
PHE CD2 CE2  doub Y N 259 
PHE CD2 HD2  sing N N 260 
PHE CE1 CZ   doub Y N 261 
PHE CE1 HE1  sing N N 262 
PHE CE2 CZ   sing Y N 263 
PHE CE2 HE2  sing N N 264 
PHE CZ  HZ   sing N N 265 
PHE OXT HXT  sing N N 266 
SER N   CA   sing N N 267 
SER N   H    sing N N 268 
SER N   H2   sing N N 269 
SER CA  C    sing N N 270 
SER CA  CB   sing N N 271 
SER CA  HA   sing N N 272 
SER C   O    doub N N 273 
SER C   OXT  sing N N 274 
SER CB  OG   sing N N 275 
SER CB  HB2  sing N N 276 
SER CB  HB3  sing N N 277 
SER OG  HG   sing N N 278 
SER OXT HXT  sing N N 279 
THR N   CA   sing N N 280 
THR N   H    sing N N 281 
THR N   H2   sing N N 282 
THR CA  C    sing N N 283 
THR CA  CB   sing N N 284 
THR CA  HA   sing N N 285 
THR C   O    doub N N 286 
THR C   OXT  sing N N 287 
THR CB  OG1  sing N N 288 
THR CB  CG2  sing N N 289 
THR CB  HB   sing N N 290 
THR OG1 HG1  sing N N 291 
THR CG2 HG21 sing N N 292 
THR CG2 HG22 sing N N 293 
THR CG2 HG23 sing N N 294 
THR OXT HXT  sing N N 295 
TRP N   CA   sing N N 296 
TRP N   H    sing N N 297 
TRP N   H2   sing N N 298 
TRP CA  C    sing N N 299 
TRP CA  CB   sing N N 300 
TRP CA  HA   sing N N 301 
TRP C   O    doub N N 302 
TRP C   OXT  sing N N 303 
TRP CB  CG   sing N N 304 
TRP CB  HB2  sing N N 305 
TRP CB  HB3  sing N N 306 
TRP CG  CD1  doub Y N 307 
TRP CG  CD2  sing Y N 308 
TRP CD1 NE1  sing Y N 309 
TRP CD1 HD1  sing N N 310 
TRP CD2 CE2  doub Y N 311 
TRP CD2 CE3  sing Y N 312 
TRP NE1 CE2  sing Y N 313 
TRP NE1 HE1  sing N N 314 
TRP CE2 CZ2  sing Y N 315 
TRP CE3 CZ3  doub Y N 316 
TRP CE3 HE3  sing N N 317 
TRP CZ2 CH2  doub Y N 318 
TRP CZ2 HZ2  sing N N 319 
TRP CZ3 CH2  sing Y N 320 
TRP CZ3 HZ3  sing N N 321 
TRP CH2 HH2  sing N N 322 
TRP OXT HXT  sing N N 323 
TYR N   CA   sing N N 324 
TYR N   H    sing N N 325 
TYR N   H2   sing N N 326 
TYR CA  C    sing N N 327 
TYR CA  CB   sing N N 328 
TYR CA  HA   sing N N 329 
TYR C   O    doub N N 330 
TYR C   OXT  sing N N 331 
TYR CB  CG   sing N N 332 
TYR CB  HB2  sing N N 333 
TYR CB  HB3  sing N N 334 
TYR CG  CD1  doub Y N 335 
TYR CG  CD2  sing Y N 336 
TYR CD1 CE1  sing Y N 337 
TYR CD1 HD1  sing N N 338 
TYR CD2 CE2  doub Y N 339 
TYR CD2 HD2  sing N N 340 
TYR CE1 CZ   doub Y N 341 
TYR CE1 HE1  sing N N 342 
TYR CE2 CZ   sing Y N 343 
TYR CE2 HE2  sing N N 344 
TYR CZ  OH   sing N N 345 
TYR OH  HH   sing N N 346 
TYR OXT HXT  sing N N 347 
VAL N   CA   sing N N 348 
VAL N   H    sing N N 349 
VAL N   H2   sing N N 350 
VAL CA  C    sing N N 351 
VAL CA  CB   sing N N 352 
VAL CA  HA   sing N N 353 
VAL C   O    doub N N 354 
VAL C   OXT  sing N N 355 
VAL CB  CG1  sing N N 356 
VAL CB  CG2  sing N N 357 
VAL CB  HB   sing N N 358 
VAL CG1 HG11 sing N N 359 
VAL CG1 HG12 sing N N 360 
VAL CG1 HG13 sing N N 361 
VAL CG2 HG21 sing N N 362 
VAL CG2 HG22 sing N N 363 
VAL CG2 HG23 sing N N 364 
VAL OXT HXT  sing N N 365 
ZFJ C23 C22  sing N N 366 
ZFJ C21 C22  doub N E 367 
ZFJ C21 C12  sing N N 368 
ZFJ C11 C12  doub Y N 369 
ZFJ C11 C10  sing Y N 370 
ZFJ C12 C13  sing Y N 371 
ZFJ C10 C07  doub Y N 372 
ZFJ C13 C08  doub Y N 373 
ZFJ C07 C08  sing Y N 374 
ZFJ C07 C06  sing N N 375 
ZFJ C08 C09  sing N N 376 
ZFJ C06 C05  doub Y N 377 
ZFJ C06 C01  sing Y N 378 
ZFJ C05 C04  sing Y N 379 
ZFJ C14 C09  sing N N 380 
ZFJ C09 C01  sing N N 381 
ZFJ C09 C15  sing N N 382 
ZFJ C01 C02  doub Y N 383 
ZFJ C04 C03  doub Y N 384 
ZFJ C02 C03  sing Y N 385 
ZFJ C03 N16  sing N N 386 
ZFJ C18 C17  sing N N 387 
ZFJ N16 C17  sing N N 388 
ZFJ N16 C19  sing N N 389 
ZFJ C20 C19  sing N N 390 
ZFJ C10 H1   sing N N 391 
ZFJ C13 H2   sing N N 392 
ZFJ C15 H3   sing N N 393 
ZFJ C15 H4   sing N N 394 
ZFJ C15 H5   sing N N 395 
ZFJ C17 H6   sing N N 396 
ZFJ C17 H7   sing N N 397 
ZFJ C20 H8   sing N N 398 
ZFJ C20 H9   sing N N 399 
ZFJ C20 H10  sing N N 400 
ZFJ C21 H11  sing N N 401 
ZFJ C22 H12  sing N N 402 
ZFJ C02 H13  sing N N 403 
ZFJ C04 H14  sing N N 404 
ZFJ C05 H15  sing N N 405 
ZFJ C11 H16  sing N N 406 
ZFJ C14 H17  sing N N 407 
ZFJ C14 H18  sing N N 408 
ZFJ C14 H19  sing N N 409 
ZFJ C18 H20  sing N N 410 
ZFJ C18 H21  sing N N 411 
ZFJ C18 H22  sing N N 412 
ZFJ C19 H23  sing N N 413 
ZFJ C19 H24  sing N N 414 
ZFJ C23 H25  sing N N 415 
ZFJ C23 H26  sing N N 416 
ZFJ C23 H27  sing N N 417 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Biomedical Imaging and Bioengineering (NIH/NIBIB)' 
_pdbx_audit_support.country                'United States' 
_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   4QYN 
_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                    9D8M 
_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]   0.032081 
_atom_sites.fract_transf_matrix[1][2]   -0.014844 
_atom_sites.fract_transf_matrix[1][3]   -0.001458 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.030728 
_atom_sites.fract_transf_matrix[2][3]   -0.001586 
_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]   0.015672 
_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   ? -27.59800 -23.25300 24.07100  1.000 39.03000 ? 1   THR A N    1 
ATOM   2    C CA   . THR A 1 1   ? -27.00700 -22.16900 23.29300  1.000 32.93000 ? 1   THR A CA   1 
ATOM   3    C C    . THR A 1 1   ? -25.65200 -21.74700 23.85400  1.000 30.21000 ? 1   THR A C    1 
ATOM   4    O O    . THR A 1 1   ? -25.19800 -20.63000 23.61300  1.000 30.13000 ? 1   THR A O    1 
ATOM   5    C CB   . THR A 1 1   ? -27.93100 -20.93400 23.23300  1.000 32.12000 ? 1   THR A CB   1 
ATOM   6    O OG1  . THR A 1 1   ? -28.55700 -20.73400 24.50800  1.000 37.92000 ? 1   THR A OG1  1 
ATOM   7    C CG2  . THR A 1 1   ? -29.00000 -21.11400 22.16500  1.000 32.83000 ? 1   THR A CG2  1 
ATOM   8    N N    . ARG A 1 2   ? -25.01400 -22.63800 24.61100  1.000 31.53000 ? 2   ARG A N    1 
ATOM   9    C CA   . ARG A 1 2   ? -23.66500 -22.40900 25.11100  1.000 24.87000 ? 2   ARG A CA   1 
ATOM   10   C C    . ARG A 1 2   ? -22.60600 -23.18800 24.32900  1.000 21.28000 ? 2   ARG A C    1 
ATOM   11   O O    . ARG A 1 2   ? -21.43100 -23.14600 24.70200  1.000 23.50000 ? 2   ARG A O    1 
ATOM   12   C CB   . ARG A 1 2   ? -23.57400 -22.71900 26.61500  1.000 27.87000 ? 2   ARG A CB   1 
ATOM   13   C CG   . ARG A 1 2   ? -23.80400 -21.51600 27.56200  1.000 28.35000 ? 2   ARG A CG   1 
ATOM   14   C CD   . ARG A 1 2   ? -23.25400 -21.75900 28.98800  1.000 26.80000 ? 2   ARG A CD   1 
ATOM   15   N NE   . ARG A 1 2   ? -23.71700 -20.75700 29.95900  1.000 24.59000 ? 2   ARG A NE   1 
ATOM   16   C CZ   . ARG A 1 2   ? -23.45900 -20.78700 31.26900  1.000 25.96000 ? 2   ARG A CZ   1 
ATOM   17   N NH1  . ARG A 1 2   ? -22.73600 -21.77000 31.78900  1.000 28.19000 ? 2   ARG A NH1  1 
ATOM   18   N NH2  . ARG A 1 2   ? -23.92600 -19.83000 32.06700  1.000 25.46000 ? 2   ARG A NH2  1 
ATOM   19   N N    . ASP A 1 3   ? -22.98600 -23.88100 23.24700  1.000 18.41000 ? 3   ASP A N    1 
ATOM   20   C CA   . ASP A 1 3   ? -22.05700 -24.73200 22.49900  1.000 18.37000 ? 3   ASP A CA   1 
ATOM   21   C C    . ASP A 1 3   ? -21.60200 -24.02700 21.22400  1.000 18.30000 ? 3   ASP A C    1 
ATOM   22   O O    . ASP A 1 3   ? -22.35600 -23.94100 20.24800  1.000 20.67000 ? 3   ASP A O    1 
ATOM   23   C CB   . ASP A 1 3   ? -22.68500 -26.08700 22.17400  1.000 20.14000 ? 3   ASP A CB   1 
ATOM   24   C CG   . ASP A 1 3   ? -21.68800 -27.06100 21.57100  1.000 21.19000 ? 3   ASP A CG   1 
ATOM   25   O OD1  . ASP A 1 3   ? -20.50500 -26.68800 21.41000  1.000 19.34000 ? 3   ASP A OD1  1 
ATOM   26   O OD2  . ASP A 1 3   ? -22.09000 -28.20500 21.25900  1.000 25.02000 ? 3   ASP A OD2  1 
ATOM   27   N N    . ALA A 1 4   ? -20.35100 -23.56900 21.21600  1.000 15.51000 ? 4   ALA A N    1 
ATOM   28   C CA   . ALA A 1 4   ? -19.76900 -22.88700 20.06700  1.000 15.22000 ? 4   ALA A CA   1 
ATOM   29   C C    . ALA A 1 4   ? -18.89200 -23.79300 19.20800  1.000 14.18000 ? 4   ALA A C    1 
ATOM   30   O O    . ALA A 1 4   ? -18.26400 -23.30600 18.26000  1.000 13.56000 ? 4   ALA A O    1 
ATOM   31   C CB   . ALA A 1 4   ? -18.98700 -21.64800 20.51400  1.000 17.47000 ? 4   ALA A CB   1 
ATOM   32   N N    . ASN A 1 5   ? -18.84100 -25.09500 19.49800  1.000 14.06000 ? 5   ASN A N    1 
ATOM   33   C CA   . ASN A 1 5   ? -18.02600 -25.99900 18.69600  1.000 13.05000 ? 5   ASN A CA   1 
ATOM   34   C C    . ASN A 1 5   ? -18.41800 -25.92700 17.22900  1.000 14.79000 ? 5   ASN A C    1 
ATOM   35   O O    . ASN A 1 5   ? -19.60100 -25.83300 16.89100  1.000 16.06000 ? 5   ASN A O    1 
ATOM   36   C CB   . ASN A 1 5   ? -18.22100 -27.44200 19.15800  1.000 14.91000 ? 5   ASN A CB   1 
ATOM   37   C CG   . ASN A 1 5   ? -17.28900 -27.82800 20.27800  1.000 14.92000 ? 5   ASN A CG   1 
ATOM   38   O OD1  . ASN A 1 5   ? -16.08500 -27.97100 20.08000  1.000 15.61000 ? 5   ASN A OD1  1 
ATOM   39   N ND2  . ASN A 1 5   ? -17.84400 -27.98700 21.47800  1.000 16.40000 ? 5   ASN A ND2  1 
ATOM   40   N N    . GLY A 1 6   ? -17.41300 -25.99200 16.35700  1.000 14.88000 ? 6   GLY A N    1 
ATOM   41   C CA   . GLY A 1 6   ? -17.67900 -26.18000 14.94500  1.000 18.38000 ? 6   GLY A CA   1 
ATOM   42   C C    . GLY A 1 6   ? -16.83500 -25.34500 14.01000  1.000 15.06000 ? 6   GLY A C    1 
ATOM   43   O O    . GLY A 1 6   ? -15.93700 -24.60400 14.42800  1.000 13.75000 ? 6   GLY A O    1 
ATOM   44   N N    . THR A 1 7   ? -17.11500 -25.49400 12.71900  1.000 13.48000 ? 7   THR A N    1 
ATOM   45   C CA   . THR A 1 7   ? -16.53600 -24.67200 11.66700  1.000 13.75000 ? 7   THR A CA   1 
ATOM   46   C C    . THR A 1 7   ? -17.60700 -23.69100 11.22500  1.000 13.82000 ? 7   THR A C    1 
ATOM   47   O O    . THR A 1 7   ? -18.71200 -24.09800 10.85400  1.000 16.90000 ? 7   THR A O    1 
ATOM   48   C CB   . THR A 1 7   ? -16.09900 -25.54000 10.48600  1.000 16.78000 ? 7   THR A CB   1 
ATOM   49   O OG1  . THR A 1 7   ? -15.07300 -26.43300 10.92400  1.000 18.84000 ? 7   THR A OG1  1 
ATOM   50   C CG2  . THR A 1 7   ? -15.56800 -24.67700 9.33700   1.000 19.29000 ? 7   THR A CG2  1 
ATOM   51   N N    . TRP A 1 8   ? -17.28900 -22.40600 11.29100  1.000 12.78000 ? 8   TRP A N    1 
ATOM   52   C CA   . TRP A 1 8   ? -18.27500 -21.34500 11.13500  1.000 13.85000 ? 8   TRP A CA   1 
ATOM   53   C C    . TRP A 1 8   ? -17.93500 -20.50300 9.90700   1.000 14.39000 ? 8   TRP A C    1 
ATOM   54   O O    . TRP A 1 8   ? -16.82500 -19.97300 9.80300   1.000 14.71000 ? 8   TRP A O    1 
ATOM   55   C CB   . TRP A 1 8   ? -18.30500 -20.49100 12.40700  1.000 13.43000 ? 8   TRP A CB   1 
ATOM   56   C CG   . TRP A 1 8   ? -18.75100 -21.25700 13.64200  1.000 12.37000 ? 8   TRP A CG   1 
ATOM   57   C CD1  . TRP A 1 8   ? -17.95500 -21.92400 14.53000  1.000 12.77000 ? 8   TRP A CD1  1 
ATOM   58   C CD2  . TRP A 1 8   ? -20.09700 -21.42800 14.10400  1.000 12.33000 ? 8   TRP A CD2  1 
ATOM   59   N NE1  . TRP A 1 8   ? -18.72600 -22.50000 15.51300  1.000 14.07000 ? 8   TRP A NE1  1 
ATOM   60   C CE2  . TRP A 1 8   ? -20.04200 -22.20900 15.27700  1.000 12.98000 ? 8   TRP A CE2  1 
ATOM   61   C CE3  . TRP A 1 8   ? -21.33800 -20.99400 13.64100  1.000 13.68000 ? 8   TRP A CE3  1 
ATOM   62   C CZ2  . TRP A 1 8   ? -21.18700 -22.56000 15.99900  1.000 13.70000 ? 8   TRP A CZ2  1 
ATOM   63   C CZ3  . TRP A 1 8   ? -22.47000 -21.33900 14.35500  1.000 15.08000 ? 8   TRP A CZ3  1 
ATOM   64   C CH2  . TRP A 1 8   ? -22.38700 -22.11800 15.52100  1.000 14.88000 ? 8   TRP A CH2  1 
ATOM   65   N N    . GLU A 1 9   ? -18.88900 -20.38500 8.98600   1.000 12.89000 ? 9   GLU A N    1 
ATOM   66   C CA   . GLU A 1 9   ? -18.71000 -19.65700 7.73400   1.000 13.56000 ? 9   GLU A CA   1 
ATOM   67   C C    . GLU A 1 9   ? -19.38500 -18.29800 7.84000   1.000 14.42000 ? 9   GLU A C    1 
ATOM   68   O O    . GLU A 1 9   ? -20.48700 -18.18300 8.37700   1.000 14.44000 ? 9   GLU A O    1 
ATOM   69   C CB   . GLU A 1 9   ? -19.35300 -20.42000 6.57600   1.000 21.25000 ? 9   GLU A CB   1 
ATOM   70   C CG   . GLU A 1 9   ? -18.50400 -21.52200 5.98600   1.000 28.94000 ? 9   GLU A CG   1 
ATOM   71   C CD   . GLU A 1 9   ? -19.17600 -22.17300 4.79100   1.000 31.95000 ? 9   GLU A CD   1 
ATOM   72   O OE1  . GLU A 1 9   ? -20.09400 -22.99600 5.00100   1.000 35.17000 ? 9   GLU A OE1  1 
ATOM   73   O OE2  . GLU A 1 9   ? -18.79900 -21.85200 3.64400   1.000 33.36000 ? 9   GLU A OE2  1 
ATOM   74   N N    . MET A 1 10  ? -18.73600 -17.27200 7.29700   1.000 13.30000 ? 10  MET A N    1 
ATOM   75   C CA   . MET A 1 10  ? -19.23400 -15.91100 7.45800   1.000 13.56000 ? 10  MET A CA   1 
ATOM   76   C C    . MET A 1 10  ? -20.45700 -15.64900 6.58800   1.000 13.10000 ? 10  MET A C    1 
ATOM   77   O O    . MET A 1 10  ? -20.47500 -15.96200 5.38600   1.000 14.09000 ? 10  MET A O    1 
ATOM   78   C CB   . MET A 1 10  ? -18.13600 -14.89700 7.13800   1.000 16.86000 ? 10  MET A CB   1 
ATOM   79   C CG   . MET A 1 10  ? -18.58400 -13.45600 7.30500   1.000 15.62000 ? 10  MET A CG   1 
ATOM   80   S SD   . MET A 1 10  ? -17.22300 -12.27500 7.34500   1.000 18.73000 ? 10  MET A SD   1 
ATOM   81   C CE   . MET A 1 10  ? -16.69200 -12.38800 9.05000   1.000 16.40000 ? 10  MET A CE   1 
ATOM   82   N N    . GLU A 1 11  ? -21.46900 -15.04100 7.19600   0.910 12.43000 ? 11  GLU A N    1 
ATOM   83   C CA   . GLU A 1 11  ? -22.64900 -14.54300 6.50000   0.910 13.89000 ? 11  GLU A CA   1 
ATOM   84   C C    . GLU A 1 11  ? -22.63500 -13.03300 6.34100   0.910 12.71000 ? 11  GLU A C    1 
ATOM   85   O O    . GLU A 1 11  ? -23.07700 -12.52100 5.31000   0.910 13.23000 ? 11  GLU A O    1 
ATOM   86   C CB   . GLU A 1 11  ? -23.91900 -14.93300 7.26000   0.910 14.72000 ? 11  GLU A CB   1 
ATOM   87   C CG   . GLU A 1 11  ? -24.21600 -16.42300 7.26400   0.910 23.01000 ? 11  GLU A CG   1 
ATOM   88   C CD   . GLU A 1 11  ? -25.70500 -16.71600 7.35400   0.910 24.66000 ? 11  GLU A CD   1 
ATOM   89   O OE1  . GLU A 1 11  ? -26.44100 -15.89400 7.94500   0.910 30.41000 ? 11  GLU A OE1  1 
ATOM   90   O OE2  . GLU A 1 11  ? -26.13700 -17.77000 6.83800   0.910 30.30000 ? 11  GLU A OE2  1 
ATOM   91   N N    . SER A 1 12  ? -22.16300 -12.30300 7.35000   1.000 12.83000 ? 12  SER A N    1 
ATOM   92   C CA   . SER A 1 12  ? -22.15600 -10.84800 7.29000   1.000 12.81000 ? 12  SER A CA   1 
ATOM   93   C C    . SER A 1 12  ? -21.08100 -10.31500 8.22700   1.000 12.05000 ? 12  SER A C    1 
ATOM   94   O O    . SER A 1 12  ? -20.63900 -10.99500 9.16100   1.000 12.84000 ? 12  SER A O    1 
ATOM   95   C CB   . SER A 1 12  ? -23.53400 -10.25100 7.58800   1.000 16.86000 ? 12  SER A CB   1 
ATOM   96   O OG   . SER A 1 12  ? -23.94400 -10.53600 8.90900   1.000 17.71000 ? 12  SER A OG   1 
ATOM   97   N N    . ASN A 1 13  ? -20.67200 -9.07200  7.96600   1.000 13.55000 ? 13  ASN A N    1 
ATOM   98   C CA   . ASN A 1 13  ? -19.54000 -8.46700  8.66400   1.000 13.28000 ? 13  ASN A CA   1 
ATOM   99   C C    . ASN A 1 13  ? -19.69100 -6.96000  8.45200   1.000 13.46000 ? 13  ASN A C    1 
ATOM   100  O O    . ASN A 1 13  ? -19.38800 -6.46300  7.36600   1.000 15.79000 ? 13  ASN A O    1 
ATOM   101  C CB   . ASN A 1 13  ? -18.24500 -8.98500  8.06200   1.000 13.57000 ? 13  ASN A CB   1 
ATOM   102  C CG   . ASN A 1 13  ? -17.01100 -8.49200  8.79200   1.000 14.41000 ? 13  ASN A CG   1 
ATOM   103  O OD1  . ASN A 1 13  ? -17.10400 -7.85900  9.85000   1.000 13.35000 ? 13  ASN A OD1  1 
ATOM   104  N ND2  . ASN A 1 13  ? -15.84100 -8.78900  8.23200   1.000 16.55000 ? 13  ASN A ND2  1 
ATOM   105  N N    . GLU A 1 14  ? -20.17600 -6.26000  9.46900   1.000 12.11000 ? 14  GLU A N    1 
ATOM   106  C CA   . GLU A 1 14  ? -20.45900 -4.83500  9.36800   1.000 13.94000 ? 14  GLU A CA   1 
ATOM   107  C C    . GLU A 1 14  ? -19.52500 -4.01900  10.25800  1.000 11.99000 ? 14  GLU A C    1 
ATOM   108  O O    . GLU A 1 14  ? -19.26800 -4.37800  11.41500  1.000 11.18000 ? 14  GLU A O    1 
ATOM   109  C CB   . GLU A 1 14  ? -21.92400 -4.55200  9.71000   1.000 15.82000 ? 14  GLU A CB   1 
ATOM   110  C CG   . GLU A 1 14  ? -22.90900 -5.06700  8.65100   1.000 18.67000 ? 14  GLU A CG   1 
ATOM   111  C CD   . GLU A 1 14  ? -22.69100 -4.44400  7.27400   1.000 20.29000 ? 14  GLU A CD   1 
ATOM   112  O OE1  . GLU A 1 14  ? -22.66700 -3.19800  7.17800   1.000 24.23000 ? 14  GLU A OE1  1 
ATOM   113  O OE2  . GLU A 1 14  ? -22.54800 -5.19400  6.28500   1.000 22.93000 ? 14  GLU A OE2  1 
ATOM   114  N N    . ASN A 1 15  ? -19.03500 -2.90900  9.70500   1.000 12.76000 ? 15  ASN A N    1 
ATOM   115  C CA   . ASN A 1 15  ? -18.07700 -2.01700  10.36500  1.000 13.25000 ? 15  ASN A CA   1 
ATOM   116  C C    . ASN A 1 15  ? -16.75000 -2.70200  10.68600  1.000 12.97000 ? 15  ASN A C    1 
ATOM   117  O O    . ASN A 1 15  ? -16.06900 -2.35300  11.65000  1.000 12.23000 ? 15  ASN A O    1 
ATOM   118  C CB   . ASN A 1 15  ? -18.66000 -1.29500  11.58000  1.000 13.07000 ? 15  ASN A CB   1 
ATOM   119  C CG   . ASN A 1 15  ? -17.79300 -0.13100  12.02200  1.000 13.85000 ? 15  ASN A CG   1 
ATOM   120  O OD1  . ASN A 1 15  ? -17.19200 0.55900   11.19300  1.000 14.25000 ? 15  ASN A OD1  1 
ATOM   121  N ND2  . ASN A 1 15  ? -17.71700 0.09200   13.32400  1.000 13.09000 ? 15  ASN A ND2  1 
ATOM   122  N N    . PHE A 1 16  ? -16.36100 -3.66500  9.85700   1.000 12.52000 ? 16  PHE A N    1 
ATOM   123  C CA   . PHE A 1 16  ? -15.05900 -4.30400  9.99800   1.000 12.08000 ? 16  PHE A CA   1 
ATOM   124  C C    . PHE A 1 16  ? -13.93000 -3.28400  9.88400   1.000 12.90000 ? 16  PHE A C    1 
ATOM   125  O O    . PHE A 1 16  ? -12.95400 -3.33100  10.64000  1.000 12.06000 ? 16  PHE A O    1 
ATOM   126  C CB   . PHE A 1 16  ? -14.96300 -5.35100  8.88900   1.000 15.13000 ? 16  PHE A CB   1 
ATOM   127  C CG   . PHE A 1 16  ? -13.82100 -6.30600  9.01200   1.000 16.29000 ? 16  PHE A CG   1 
ATOM   128  C CD1  . PHE A 1 16  ? -13.50000 -6.89700  10.21800  1.000 16.94000 ? 16  PHE A CD1  1 
ATOM   129  C CD2  . PHE A 1 16  ? -13.11800 -6.67900  7.87400   1.000 18.29000 ? 16  PHE A CD2  1 
ATOM   130  C CE1  . PHE A 1 16  ? -12.46300 -7.80300  10.29600  1.000 22.48000 ? 16  PHE A CE1  1 
ATOM   131  C CE2  . PHE A 1 16  ? -12.09000 -7.58300  7.95000   1.000 20.35000 ? 16  PHE A CE2  1 
ATOM   132  C CZ   . PHE A 1 16  ? -11.76800 -8.14800  9.15200   1.000 19.69000 ? 16  PHE A CZ   1 
ATOM   133  N N    . GLU A 1 17  ? -14.04900 -2.35100  8.93400   1.000 13.84000 ? 17  GLU A N    1 
ATOM   134  C CA   . GLU A 1 17  ? -12.99700 -1.36000  8.72800   1.000 14.02000 ? 17  GLU A CA   1 
ATOM   135  C C    . GLU A 1 17  ? -12.88900 -0.40300  9.90900   1.000 14.07000 ? 17  GLU A C    1 
ATOM   136  O O    . GLU A 1 17  ? -11.78000 -0.04100  10.32200  1.000 13.77000 ? 17  GLU A O    1 
ATOM   137  C CB   . GLU A 1 17  ? -13.25200 -0.59900  7.42800   1.000 18.45000 ? 17  GLU A CB   1 
ATOM   138  C CG   . GLU A 1 17  ? -13.05600 -1.45500  6.19400   1.000 24.69000 ? 17  GLU A CG   1 
ATOM   139  C CD   . GLU A 1 17  ? -12.96000 -0.64400  4.91900   1.000 29.61000 ? 17  GLU A CD   1 
ATOM   140  O OE1  . GLU A 1 17  ? -11.94200 0.05700   4.73200   1.000 31.47000 ? 17  GLU A OE1  1 
ATOM   141  O OE2  . GLU A 1 17  ? -13.90300 -0.71400  4.10300   1.000 33.03000 ? 17  GLU A OE2  1 
ATOM   142  N N    . GLY A 1 18  ? -14.02400 0.02900   10.45500  1.000 13.61000 ? 18  GLY A N    1 
ATOM   143  C CA   . GLY A 1 18  ? -13.99200 0.93000   11.59400  1.000 15.14000 ? 18  GLY A CA   1 
ATOM   144  C C    . GLY A 1 18  ? -13.34700 0.29400   12.80900  1.000 11.88000 ? 18  GLY A C    1 
ATOM   145  O O    . GLY A 1 18  ? -12.57300 0.93600   13.52400  1.000 12.27000 ? 18  GLY A O    1 
ATOM   146  N N    . TRP A 1 19  ? -13.65300 -0.98300  13.05300  1.000 11.83000 ? 19  TRP A N    1 
ATOM   147  C CA   . TRP A 1 19  ? -13.04000 -1.69100  14.17100  1.000 12.21000 ? 19  TRP A CA   1 
ATOM   148  C C    . TRP A 1 19  ? -11.53700 -1.86700  13.95000  1.000 10.80000 ? 19  TRP A C    1 
ATOM   149  O O    . TRP A 1 19  ? -10.74000 -1.62200  14.86000  1.000 10.51000 ? 19  TRP A O    1 
ATOM   150  C CB   . TRP A 1 19  ? -13.77600 -3.01800  14.38900  1.000 11.79000 ? 19  TRP A CB   1 
ATOM   151  C CG   . TRP A 1 19  ? -13.09700 -3.97300  15.30200  1.000 11.11000 ? 19  TRP A CG   1 
ATOM   152  C CD1  . TRP A 1 19  ? -13.11400 -3.96500  16.67200  1.000 11.52000 ? 19  TRP A CD1  1 
ATOM   153  C CD2  . TRP A 1 19  ? -12.30200 -5.09800  14.91600  1.000 12.96000 ? 19  TRP A CD2  1 
ATOM   154  N NE1  . TRP A 1 19  ? -12.37100 -5.01500  17.15600  1.000 12.82000 ? 19  TRP A NE1  1 
ATOM   155  C CE2  . TRP A 1 19  ? -11.86300 -5.72500  16.09600  1.000 12.70000 ? 19  TRP A CE2  1 
ATOM   156  C CE3  . TRP A 1 19  ? -11.91500 -5.63200  13.68200  1.000 16.16000 ? 19  TRP A CE3  1 
ATOM   157  C CZ2  . TRP A 1 19  ? -11.05300 -6.86300  16.07600  1.000 15.15000 ? 19  TRP A CZ2  1 
ATOM   158  C CZ3  . TRP A 1 19  ? -11.12000 -6.74800  13.66300  1.000 17.50000 ? 19  TRP A CZ3  1 
ATOM   159  C CH2  . TRP A 1 19  ? -10.69300 -7.35400  14.84700  1.000 15.38000 ? 19  TRP A CH2  1 
ATOM   160  N N    . MET A 1 20  ? -11.12300 -2.27300  12.74300  1.000 10.59000 ? 20  MET A N    1 
ATOM   161  C CA   . MET A 1 20  ? -9.69200  -2.39500  12.46900  1.000 10.51000 ? 20  MET A CA   1 
ATOM   162  C C    . MET A 1 20  ? -8.97900  -1.05800  12.61200  1.000 9.37000  ? 20  MET A C    1 
ATOM   163  O O    . MET A 1 20  ? -7.84900  -0.99900  13.11200  1.000 10.38000 ? 20  MET A O    1 
ATOM   164  C CB   . MET A 1 20  ? -9.44800  -2.97600  11.07400  1.000 11.10000 ? 20  MET A CB   1 
ATOM   165  C CG   . MET A 1 20  ? -9.70000  -4.47900  10.96100  1.000 11.40000 ? 20  MET A CG   1 
ATOM   166  S SD   . MET A 1 20  ? -9.14700  -5.16200  9.38600   1.000 13.55000 ? 20  MET A SD   1 
ATOM   167  C CE   . MET A 1 20  ? -10.28000 -4.35100  8.24600   1.000 15.74000 ? 20  MET A CE   1 
ATOM   168  N N    . LYS A 1 21  ? -9.61600  0.02200   12.16000  1.000 10.26000 ? 21  LYS A N    1 
ATOM   169  C CA   . LYS A 1 21  ? -9.01700  1.34600   12.29500  1.000 11.78000 ? 21  LYS A CA   1 
ATOM   170  C C    . LYS A 1 21  ? -8.87400  1.73500   13.76100  1.000 11.04000 ? 21  LYS A C    1 
ATOM   171  O O    . LYS A 1 21  ? -7.86200  2.32600   14.16100  1.000 11.77000 ? 21  LYS A O    1 
ATOM   172  C CB   . LYS A 1 21  ? -9.85700  2.36500   11.52500  1.000 13.37000 ? 21  LYS A CB   1 
ATOM   173  C CG   . LYS A 1 21  ? -9.28100  3.76700   11.51600  1.000 15.13000 ? 21  LYS A CG   1 
ATOM   174  C CD   . LYS A 1 21  ? -10.27700 4.78100   10.99200  1.000 24.14000 ? 21  LYS A CD   1 
ATOM   175  C CE   . LYS A 1 21  ? -10.11700 4.96200   9.50500   1.000 25.19000 ? 21  LYS A CE   1 
ATOM   176  N NZ   . LYS A 1 21  ? -10.89600 6.13100   9.00700   1.000 29.78000 ? 21  LYS A NZ   1 
ATOM   177  N N    . ALA A 1 22  ? -9.86600  1.39100   14.59000  1.000 11.17000 ? 22  ALA A N    1 
ATOM   178  C CA   . ALA A 1 22  ? -9.76500  1.68500   16.01800  1.000 11.30000 ? 22  ALA A CA   1 
ATOM   179  C C    . ALA A 1 22  ? -8.58000  0.97300   16.65500  1.000 12.17000 ? 22  ALA A C    1 
ATOM   180  O O    . ALA A 1 22  ? -8.02100  1.46000   17.64500  1.000 13.43000 ? 22  ALA A O    1 
ATOM   181  C CB   . ALA A 1 22  ? -11.05800 1.30600   16.74200  1.000 12.35000 ? 22  ALA A CB   1 
ATOM   182  N N    . LEU A 1 23  ? -8.20200  -0.19400  16.12700  1.000 10.88000 ? 23  LEU A N    1 
ATOM   183  C CA   . LEU A 1 23  ? -7.02700  -0.92900  16.59200  1.000 12.44000 ? 23  LEU A CA   1 
ATOM   184  C C    . LEU A 1 23  ? -5.72800  -0.43400  15.96700  1.000 12.73000 ? 23  LEU A C    1 
ATOM   185  O O    . LEU A 1 23  ? -4.65100  -0.93700  16.32100  1.000 15.24000 ? 23  LEU A O    1 
ATOM   186  C CB   . LEU A 1 23  ? -7.19000  -2.42300  16.28800  1.000 13.57000 ? 23  LEU A CB   1 
ATOM   187  C CG   . LEU A 1 23  ? -8.24900  -3.13100  17.13600  1.000 12.60000 ? 23  LEU A CG   1 
ATOM   188  C CD1  . LEU A 1 23  ? -8.61100  -4.48500  16.55000  1.000 16.86000 ? 23  LEU A CD1  1 
ATOM   189  C CD2  . LEU A 1 23  ? -7.74700  -3.28100  18.56700  1.000 14.91000 ? 23  LEU A CD2  1 
ATOM   190  N N    . ASP A 1 24  ? -5.79600  0.50800   15.03500  1.000 12.53000 ? 24  ASP A N    1 
ATOM   191  C CA   . ASP A 1 24  ? -4.62700  1.06500   14.36100  1.000 14.65000 ? 24  ASP A CA   1 
ATOM   192  C C    . ASP A 1 24  ? -4.02300  0.12900   13.31700  1.000 12.85000 ? 24  ASP A C    1 
ATOM   193  O O    . ASP A 1 24  ? -2.83700  0.26900   12.97800  1.000 16.97000 ? 24  ASP A O    1 
ATOM   194  C CB   . ASP A 1 24  ? -3.56200  1.54100   15.35800  1.000 17.59000 ? 24  ASP A CB   1 
ATOM   195  C CG   . ASP A 1 24  ? -4.13500  2.48800   16.40200  1.000 16.76000 ? 24  ASP A CG   1 
ATOM   196  O OD1  . ASP A 1 24  ? -4.76200  3.47400   15.98700  1.000 23.53000 ? 24  ASP A OD1  1 
ATOM   197  O OD2  . ASP A 1 24  ? -3.98200  2.22900   17.61300  1.000 18.76000 ? 24  ASP A OD2  1 
ATOM   198  N N    . ILE A 1 25  ? -4.79200  -0.82900  12.78600  1.000 13.77000 ? 25  ILE A N    1 
ATOM   199  C CA   . ILE A 1 25  ? -4.29900  -1.67200  11.70100  1.000 15.73000 ? 25  ILE A CA   1 
ATOM   200  C C    . ILE A 1 25  ? -3.96500  -0.80200  10.49400  1.000 14.95000 ? 25  ILE A C    1 
ATOM   201  O O    . ILE A 1 25  ? -4.72500  0.10700   10.13100  1.000 14.84000 ? 25  ILE A O    1 
ATOM   202  C CB   . ILE A 1 25  ? -5.34000  -2.74700  11.33600  1.000 13.58000 ? 25  ILE A CB   1 
ATOM   203  C CG1  . ILE A 1 25  ? -5.70500  -3.60800  12.54900  1.000 15.61000 ? 25  ILE A CG1  1 
ATOM   204  C CG2  . ILE A 1 25  ? -4.84100  -3.59900  10.16800  1.000 16.32000 ? 25  ILE A CG2  1 
ATOM   205  C CD1  . ILE A 1 25  ? -4.51600  -4.26900  13.20500  1.000 17.55000 ? 25  ILE A CD1  1 
ATOM   206  N N    . ASP A 1 26  ? -2.81400  -1.08000  9.87000   1.000 15.99000 ? 26  ASP A N    1 
ATOM   207  C CA   . ASP A 1 26  ? -2.35300  -0.32100  8.70600   1.000 16.95000 ? 26  ASP A CA   1 
ATOM   208  C C    . ASP A 1 26  ? -3.45100  -0.19900  7.65600   1.000 16.95000 ? 26  ASP A C    1 
ATOM   209  O O    . ASP A 1 26  ? -4.10300  -1.18200  7.30000   1.000 15.46000 ? 26  ASP A O    1 
ATOM   210  C CB   . ASP A 1 26  ? -1.12400  -0.99700  8.09100   1.000 19.60000 ? 26  ASP A CB   1 
ATOM   211  C CG   . ASP A 1 26  ? -0.81900  -0.48900  6.68100   1.000 23.45000 ? 26  ASP A CG   1 
ATOM   212  O OD1  . ASP A 1 26  ? -0.26500  0.62200   6.55100   1.000 26.56000 ? 26  ASP A OD1  1 
ATOM   213  O OD2  . ASP A 1 26  ? -1.13600  -1.19400  5.69900   1.000 24.67000 ? 26  ASP A OD2  1 
ATOM   214  N N    . PHE A 1 27  ? -3.63900  1.02300   7.14900   1.000 17.18000 ? 27  PHE A N    1 
ATOM   215  C CA   . PHE A 1 27  ? -4.72800  1.29700   6.21600   1.000 17.37000 ? 27  PHE A CA   1 
ATOM   216  C C    . PHE A 1 27  ? -4.65700  0.40700   4.97800   1.000 16.90000 ? 27  PHE A C    1 
ATOM   217  O O    . PHE A 1 27  ? -5.68600  -0.10300  4.51400   1.000 17.81000 ? 27  PHE A O    1 
ATOM   218  C CB   . PHE A 1 27  ? -4.71000  2.77900   5.82900   1.000 20.86000 ? 27  PHE A CB   1 
ATOM   219  C CG   . PHE A 1 27  ? -5.57100  3.12000   4.64200   1.000 24.72000 ? 27  PHE A CG   1 
ATOM   220  C CD1  . PHE A 1 27  ? -6.92100  3.39900   4.79800   1.000 27.59000 ? 27  PHE A CD1  1 
ATOM   221  C CD2  . PHE A 1 27  ? -5.02300  3.18100   3.36900   1.000 27.22000 ? 27  PHE A CD2  1 
ATOM   222  C CE1  . PHE A 1 27  ? -7.71000  3.72000   3.70500   1.000 30.96000 ? 27  PHE A CE1  1 
ATOM   223  C CE2  . PHE A 1 27  ? -5.80600  3.49900   2.27400   1.000 28.95000 ? 27  PHE A CE2  1 
ATOM   224  C CZ   . PHE A 1 27  ? -7.14900  3.77100   2.44100   1.000 31.39000 ? 27  PHE A CZ   1 
ATOM   225  N N    . ALA A 1 28  ? -3.46100  0.22200   4.41400   1.000 18.86000 ? 28  ALA A N    1 
ATOM   226  C CA   . ALA A 1 28  ? -3.35000  -0.61300  3.21900   1.000 21.97000 ? 28  ALA A CA   1 
ATOM   227  C C    . ALA A 1 28  ? -3.71700  -2.05600  3.53300   1.000 20.78000 ? 28  ALA A C    1 
ATOM   228  O O    . ALA A 1 28  ? -4.39300  -2.72700  2.73900   1.000 21.58000 ? 28  ALA A O    1 
ATOM   229  C CB   . ALA A 1 28  ? -1.94100  -0.51700  2.63400   1.000 23.20000 ? 28  ALA A CB   1 
ATOM   230  N N    . LEU A 1 29  ? -3.31600  -2.54000  4.70800   1.000 16.97000 ? 29  LEU A N    1 
ATOM   231  C CA   . LEU A 1 29  ? -3.66900  -3.89700  5.10500   1.000 17.78000 ? 29  LEU A CA   1 
ATOM   232  C C    . LEU A 1 29  ? -5.17200  -4.04300  5.30300   1.000 16.57000 ? 29  LEU A C    1 
ATOM   233  O O    . LEU A 1 29  ? -5.75500  -5.07400  4.94700   1.000 18.22000 ? 29  LEU A O    1 
ATOM   234  C CB   . LEU A 1 29  ? -2.91100  -4.27400  6.37500   1.000 17.43000 ? 29  LEU A CB   1 
ATOM   235  C CG   . LEU A 1 29  ? -2.94900  -5.74900  6.76300   1.000 20.06000 ? 29  LEU A CG   1 
ATOM   236  C CD1  . LEU A 1 29  ? -2.39100  -6.61100  5.63600   1.000 24.87000 ? 29  LEU A CD1  1 
ATOM   237  C CD2  . LEU A 1 29  ? -2.17800  -5.96800  8.06000   1.000 21.82000 ? 29  LEU A CD2  1 
ATOM   238  N N    . ARG A 1 30  ? -5.82200  -3.02200  5.87100   1.000 17.22000 ? 30  ARG A N    1 
ATOM   239  C CA   . ARG A 1 30  ? -7.26400  -3.08500  6.08100   1.000 17.43000 ? 30  ARG A CA   1 
ATOM   240  C C    . ARG A 1 30  ? -8.00700  -3.32000  4.77700   1.000 21.62000 ? 30  ARG A C    1 
ATOM   241  O O    . ARG A 1 30  ? -8.97800  -4.08100  4.73600   1.000 21.23000 ? 30  ARG A O    1 
ATOM   242  C CB   . ARG A 1 30  ? -7.75900  -1.78400  6.71200   1.000 17.71000 ? 30  ARG A CB   1 
ATOM   243  C CG   . ARG A 1 30  ? -7.19600  -1.49700  8.08500   1.000 15.61000 ? 30  ARG A CG   1 
ATOM   244  C CD   . ARG A 1 30  ? -8.07200  -0.52100  8.87200   1.000 18.12000 ? 30  ARG A CD   1 
ATOM   245  N NE   . ARG A 1 30  ? -8.34000  0.73100   8.17600   1.000 19.91000 ? 30  ARG A NE   1 
ATOM   246  C CZ   . ARG A 1 30  ? -7.67900  1.87100   8.38900   1.000 18.68000 ? 30  ARG A CZ   1 
ATOM   247  N NH1  . ARG A 1 30  ? -6.68400  1.92500   9.26000   1.000 18.24000 ? 30  ARG A NH1  1 
ATOM   248  N NH2  . ARG A 1 30  ? -8.01200  2.95600   7.71400   1.000 24.31000 ? 30  ARG A NH2  1 
ATOM   249  N N    . LYS A 1 31  ? -7.58500  -2.65000  3.70600   1.000 20.54000 ? 31  LYS A N    1 
ATOM   250  C CA   . LYS A 1 31  ? -8.28500  -2.78200  2.43500   1.000 24.94000 ? 31  LYS A CA   1 
ATOM   251  C C    . LYS A 1 31  ? -8.11800  -4.17300  1.83300   1.000 23.77000 ? 31  LYS A C    1 
ATOM   252  O O    . LYS A 1 31  ? -9.00700  -4.63900  1.11200   1.000 27.54000 ? 31  LYS A O    1 
ATOM   253  C CB   . LYS A 1 31  ? -7.82900  -1.69300  1.46700   1.000 26.30000 ? 31  LYS A CB   1 
ATOM   254  C CG   . LYS A 1 31  ? -8.03300  -0.28300  2.00400   1.000 30.01000 ? 31  LYS A CG   1 
ATOM   255  C CD   . LYS A 1 31  ? -9.36100  0.27800   1.51900   1.000 32.40000 ? 31  LYS A CD   1 
ATOM   256  C CE   . LYS A 1 31  ? -9.27200  1.75300   1.17200   1.000 35.55000 ? 31  LYS A CE   1 
ATOM   257  N NZ   . LYS A 1 31  ? -9.67900  2.03500   -0.23600  1.000 37.04000 ? 31  LYS A NZ   1 
ATOM   258  N N    . ILE A 1 32  ? -6.99800  -4.84100  2.11300   1.000 21.88000 ? 32  ILE A N    1 
ATOM   259  C CA   . ILE A 1 32  ? -6.85400  -6.24600  1.73100   1.000 21.12000 ? 32  ILE A CA   1 
ATOM   260  C C    . ILE A 1 32  ? -7.70200  -7.13000  2.63600   1.000 20.98000 ? 32  ILE A C    1 
ATOM   261  O O    . ILE A 1 32  ? -8.42400  -8.01900  2.17000   1.000 21.41000 ? 32  ILE A O    1 
ATOM   262  C CB   . ILE A 1 32  ? -5.37500  -6.66800  1.75700   1.000 21.48000 ? 32  ILE A CB   1 
ATOM   263  C CG1  . ILE A 1 32  ? -4.57000  -5.88700  0.71600   1.000 25.40000 ? 32  ILE A CG1  1 
ATOM   264  C CG2  . ILE A 1 32  ? -5.24700  -8.17000  1.53100   1.000 25.81000 ? 32  ILE A CG2  1 
ATOM   265  C CD1  . ILE A 1 32  ? -5.08600  -6.03000  -0.70300  1.000 26.57000 ? 32  ILE A CD1  1 
ATOM   266  N N    . ALA A 1 33  ? -7.63400  -6.89600  3.95000   1.000 18.08000 ? 33  ALA A N    1 
ATOM   267  C CA   . ALA A 1 33  ? -8.38600  -7.73100  4.87500   1.000 15.84000 ? 33  ALA A CA   1 
ATOM   268  C C    . ALA A 1 33  ? -9.87700  -7.67800  4.58100   1.000 13.92000 ? 33  ALA A C    1 
ATOM   269  O O    . ALA A 1 33  ? -10.58200 -8.67000  4.77900   1.000 15.27000 ? 33  ALA A O    1 
ATOM   270  C CB   . ALA A 1 33  ? -8.09600  -7.32300  6.31800   1.000 16.27000 ? 33  ALA A CB   1 
ATOM   271  N N    . VAL A 1 34  ? -10.37400 -6.54000  4.08600   1.000 16.76000 ? 34  VAL A N    1 
ATOM   272  C CA   . VAL A 1 34  ? -11.79100 -6.45300  3.74600   1.000 19.64000 ? 34  VAL A CA   1 
ATOM   273  C C    . VAL A 1 34  ? -12.17600 -7.39400  2.60700   1.000 18.55000 ? 34  VAL A C    1 
ATOM   274  O O    . VAL A 1 34  ? -13.34900 -7.75600  2.48300   1.000 23.19000 ? 34  VAL A O    1 
ATOM   275  C CB   . VAL A 1 34  ? -12.23300 -4.99700  3.47300   1.000 23.51000 ? 34  VAL A CB   1 
ATOM   276  C CG1  . VAL A 1 34  ? -11.94700 -4.11400  4.68200   1.000 24.05000 ? 34  VAL A CG1  1 
ATOM   277  C CG2  . VAL A 1 34  ? -11.55700 -4.44800  2.22900   1.000 24.30000 ? 34  VAL A CG2  1 
ATOM   278  N N    . ARG A 1 35  ? -11.22200 -7.80500  1.77400   1.000 17.75000 ? 35  ARG A N    1 
ATOM   279  C CA   . ARG A 1 35  ? -11.52400 -8.71400  0.67100   1.000 18.43000 ? 35  ARG A CA   1 
ATOM   280  C C    . ARG A 1 35  ? -11.47600 -10.18800 1.06500   1.000 18.66000 ? 35  ARG A C    1 
ATOM   281  O O    . ARG A 1 35  ? -12.10000 -11.01700 0.39200   1.000 16.72000 ? 35  ARG A O    1 
ATOM   282  C CB   . ARG A 1 35  ? -10.57000 -8.45900  -0.50200  1.000 20.28000 ? 35  ARG A CB   1 
ATOM   283  C CG   . ARG A 1 35  ? -10.70700 -7.07000  -1.08900  1.000 23.67000 ? 35  ARG A CG   1 
ATOM   284  C CD   . ARG A 1 35  ? -12.16100 -6.63800  -1.03900  1.000 26.12000 ? 35  ARG A CD   1 
ATOM   285  N NE   . ARG A 1 35  ? -12.38800 -5.35700  -1.70400  1.000 28.74000 ? 35  ARG A NE   1 
ATOM   286  C CZ   . ARG A 1 35  ? -13.58700 -4.81300  -1.87500  1.000 16.78000 ? 35  ARG A CZ   1 
ATOM   287  N NH1  . ARG A 1 35  ? -13.71000 -3.64300  -2.48700  1.000 29.24000 ? 35  ARG A NH1  1 
ATOM   288  N NH2  . ARG A 1 35  ? -14.66500 -5.43700  -1.42400  1.000 26.69000 ? 35  ARG A NH2  1 
ATOM   289  N N    . LEU A 1 36  ? -10.76600 -10.53700 2.13500   1.000 16.04000 ? 36  LEU A N    1 
ATOM   290  C CA   . LEU A 1 36  ? -10.46400 -11.93400 2.42200   1.000 17.90000 ? 36  LEU A CA   1 
ATOM   291  C C    . LEU A 1 36  ? -11.62800 -12.64700 3.09800   1.000 17.09000 ? 36  LEU A C    1 
ATOM   292  O O    . LEU A 1 36  ? -12.23200 -12.13400 4.04600   1.000 21.57000 ? 36  LEU A O    1 
ATOM   293  C CB   . LEU A 1 36  ? -9.25100  -12.02200 3.34400   1.000 21.17000 ? 36  LEU A CB   1 
ATOM   294  C CG   . LEU A 1 36  ? -7.93400  -11.44200 2.84400   1.000 25.50000 ? 36  LEU A CG   1 
ATOM   295  C CD1  . LEU A 1 36  ? -6.84700  -11.72200 3.85800   1.000 26.11000 ? 36  LEU A CD1  1 
ATOM   296  C CD2  . LEU A 1 36  ? -7.56300  -12.00900 1.48000   1.000 25.81000 ? 36  LEU A CD2  1 
ATOM   297  N N    . THR A 1 37  ? -11.90100 -13.86900 2.64400   1.000 15.01000 ? 37  THR A N    1 
ATOM   298  C CA   . THR A 1 37  ? -12.88400 -14.71400 3.30700   1.000 17.08000 ? 37  THR A CA   1 
ATOM   299  C C    . THR A 1 37  ? -12.32500 -15.21200 4.63800   1.000 14.63000 ? 37  THR A C    1 
ATOM   300  O O    . THR A 1 37  ? -11.20100 -15.71500 4.70200   1.000 15.72000 ? 37  THR A O    1 
ATOM   301  C CB   . THR A 1 37  ? -13.23800 -15.90000 2.40800   1.000 17.11000 ? 37  THR A CB   1 
ATOM   302  O OG1  . THR A 1 37  ? -13.63300 -15.42400 1.11200   1.000 16.74000 ? 37  THR A OG1  1 
ATOM   303  C CG2  . THR A 1 37  ? -14.36800 -16.71900 3.01500   1.000 19.03000 ? 37  THR A CG2  1 
ATOM   304  N N    . LEU A 1 38  ? -13.11400 -15.07300 5.70100   1.000 14.94000 ? 38  LEU A N    1 
ATOM   305  C CA   . LEU A 1 38  ? -12.71400 -15.46300 7.05000   1.000 14.86000 ? 38  LEU A CA   1 
ATOM   306  C C    . LEU A 1 38  ? -13.47000 -16.71600 7.46500   1.000 15.46000 ? 38  LEU A C    1 
ATOM   307  O O    . LEU A 1 38  ? -14.69100 -16.78800 7.30200   1.000 16.54000 ? 38  LEU A O    1 
ATOM   308  C CB   . LEU A 1 38  ? -13.00900 -14.33400 8.04100   1.000 16.43000 ? 38  LEU A CB   1 
ATOM   309  C CG   . LEU A 1 38  ? -12.35000 -12.98400 7.76000   1.000 21.76000 ? 38  LEU A CG   1 
ATOM   310  C CD1  . LEU A 1 38  ? -12.75100 -11.95500 8.81400   1.000 24.97000 ? 38  LEU A CD1  1 
ATOM   311  C CD2  . LEU A 1 38  ? -10.84300 -13.13300 7.69600   1.000 25.33000 ? 38  LEU A CD2  1 
ATOM   312  N N    . THR A 1 39  ? -12.75000 -17.69100 8.01000   1.000 16.45000 ? 39  THR A N    1 
ATOM   313  C CA   . THR A 1 39  ? -13.35800 -18.89100 8.56800   1.000 15.49000 ? 39  THR A CA   1 
ATOM   314  C C    . THR A 1 39  ? -12.98100 -19.00800 10.03700  1.000 15.20000 ? 39  THR A C    1 
ATOM   315  O O    . THR A 1 39  ? -11.82000 -18.81300 10.40700  1.000 17.22000 ? 39  THR A O    1 
ATOM   316  C CB   . THR A 1 39  ? -12.89000 -20.15100 7.83000   1.000 17.45000 ? 39  THR A CB   1 
ATOM   317  O OG1  . THR A 1 39  ? -13.17700 -20.03000 6.43100   1.000 20.42000 ? 39  THR A OG1  1 
ATOM   318  C CG2  . THR A 1 39  ? -13.58800 -21.39200 8.37800   1.000 20.53000 ? 39  THR A CG2  1 
ATOM   319  N N    . LEU A 1 40  ? -13.96400 -19.35000 10.86500  1.000 14.93000 ? 40  LEU A N    1 
ATOM   320  C CA   . LEU A 1 40  ? -13.80900 -19.39600 12.31200  1.000 13.49000 ? 40  LEU A CA   1 
ATOM   321  C C    . LEU A 1 40  ? -14.03600 -20.82900 12.77100  1.000 15.18000 ? 40  LEU A C    1 
ATOM   322  O O    . LEU A 1 40  ? -15.12200 -21.37800 12.57400  1.000 17.20000 ? 40  LEU A O    1 
ATOM   323  C CB   . LEU A 1 40  ? -14.82200 -18.44500 12.95600  1.000 15.41000 ? 40  LEU A CB   1 
ATOM   324  C CG   . LEU A 1 40  ? -14.96900 -18.45200 14.47400  1.000 15.26000 ? 40  LEU A CG   1 
ATOM   325  C CD1  . LEU A 1 40  ? -13.66000 -18.08600 15.16300  1.000 17.96000 ? 40  LEU A CD1  1 
ATOM   326  C CD2  . LEU A 1 40  ? -16.07100 -17.48600 14.87500  1.000 15.82000 ? 40  LEU A CD2  1 
ATOM   327  N N    . VAL A 1 41  ? -13.00900 -21.44200 13.35600  1.000 12.44000 ? 41  VAL A N    1 
ATOM   328  C CA   . VAL A 1 41  ? -13.08000 -22.81300 13.84500  1.000 13.42000 ? 41  VAL A CA   1 
ATOM   329  C C    . VAL A 1 41  ? -12.89000 -22.77900 15.35300  1.000 13.58000 ? 41  VAL A C    1 
ATOM   330  O O    . VAL A 1 41  ? -11.90600 -22.21900 15.84400  1.000 13.86000 ? 41  VAL A O    1 
ATOM   331  C CB   . VAL A 1 41  ? -12.02300 -23.71500 13.17700  1.000 16.87000 ? 41  VAL A CB   1 
ATOM   332  C CG1  . VAL A 1 41  ? -12.05700 -25.10500 13.78500  1.000 17.32000 ? 41  VAL A CG1  1 
ATOM   333  C CG2  . VAL A 1 41  ? -12.25900 -23.80100 11.67800  1.000 17.54000 ? 41  VAL A CG2  1 
ATOM   334  N N    . ILE A 1 42  ? -13.82600 -23.38400 16.07800  1.000 12.52000 ? 42  ILE A N    1 
ATOM   335  C CA   . ILE A 1 42  ? -13.84300 -23.34600 17.53500  1.000 12.81000 ? 42  ILE A CA   1 
ATOM   336  C C    . ILE A 1 42  ? -13.87000 -24.77000 18.06600  1.000 12.73000 ? 42  ILE A C    1 
ATOM   337  O O    . ILE A 1 42  ? -14.71200 -25.57900 17.65800  1.000 12.94000 ? 42  ILE A O    1 
ATOM   338  C CB   . ILE A 1 42  ? -15.03800 -22.53100 18.06800  1.000 11.79000 ? 42  ILE A CB   1 
ATOM   339  C CG1  . ILE A 1 42  ? -14.94300 -21.07100 17.60500  1.000 14.97000 ? 42  ILE A CG1  1 
ATOM   340  C CG2  . ILE A 1 42  ? -15.12800 -22.62900 19.59400  1.000 14.16000 ? 42  ILE A CG2  1 
ATOM   341  C CD1  . ILE A 1 42  ? -16.19100 -20.25800 17.87400  1.000 14.96000 ? 42  ILE A CD1  1 
ATOM   342  N N    . ASP A 1 43  ? -12.95400 -25.06400 18.98100  1.000 12.35000 ? 43  ASP A N    1 
ATOM   343  C CA   . ASP A 1 43  ? -12.94300 -26.30000 19.75000  1.000 13.68000 ? 43  ASP A CA   1 
ATOM   344  C C    . ASP A 1 43  ? -13.21000 -25.92800 21.20400  1.000 13.75000 ? 43  ASP A C    1 
ATOM   345  O O    . ASP A 1 43  ? -12.45400 -25.14500 21.79100  1.000 15.90000 ? 43  ASP A O    1 
ATOM   346  C CB   . ASP A 1 43  ? -11.58100 -26.97900 19.61800  1.000 17.88000 ? 43  ASP A CB   1 
ATOM   347  C CG   . ASP A 1 43  ? -11.55000 -28.36800 20.22000  1.000 22.84000 ? 43  ASP A CG   1 
ATOM   348  O OD1  . ASP A 1 43  ? -11.69700 -28.50000 21.45100  1.000 23.83000 ? 43  ASP A OD1  1 
ATOM   349  O OD2  . ASP A 1 43  ? -11.36300 -29.33400 19.45200  1.000 29.77000 ? 43  ASP A OD2  1 
ATOM   350  N N    . GLN A 1 44  ? -14.28000 -26.47600 21.77600  1.000 13.13000 ? 44  GLN A N    1 
ATOM   351  C CA   . GLN A 1 44  ? -14.72800 -26.12300 23.12000  1.000 13.36000 ? 44  GLN A CA   1 
ATOM   352  C C    . GLN A 1 44  ? -14.89800 -27.40200 23.92600  1.000 13.69000 ? 44  GLN A C    1 
ATOM   353  O O    . GLN A 1 44  ? -15.69600 -28.27000 23.55500  1.000 14.71000 ? 44  GLN A O    1 
ATOM   354  C CB   . GLN A 1 44  ? -16.04600 -25.34100 23.04500  1.000 12.93000 ? 44  GLN A CB   1 
ATOM   355  C CG   . GLN A 1 44  ? -16.73200 -25.04500 24.38200  1.000 14.75000 ? 44  GLN A CG   1 
ATOM   356  C CD   . GLN A 1 44  ? -18.05100 -24.32100 24.18100  1.000 14.11000 ? 44  GLN A CD   1 
ATOM   357  O OE1  . GLN A 1 44  ? -18.33500 -23.82100 23.08900  1.000 16.94000 ? 44  GLN A OE1  1 
ATOM   358  N NE2  . GLN A 1 44  ? -18.85700 -24.24300 25.23200  1.000 16.77000 ? 44  GLN A NE2  1 
ATOM   359  N N    . ASP A 1 45  ? -14.15200 -27.50500 25.03000  1.000 14.37000 ? 45  ASP A N    1 
ATOM   360  C CA   . ASP A 1 45  ? -14.09900 -28.69600 25.88300  1.000 15.05000 ? 45  ASP A CA   1 
ATOM   361  C C    . ASP A 1 45  ? -14.16500 -28.20100 27.32700  1.000 14.28000 ? 45  ASP A C    1 
ATOM   362  O O    . ASP A 1 45  ? -13.15000 -27.78700 27.89000  1.000 15.40000 ? 45  ASP A O    1 
ATOM   363  C CB   . ASP A 1 45  ? -12.80300 -29.45600 25.60700  1.000 21.86000 ? 45  ASP A CB   1 
ATOM   364  C CG   . ASP A 1 45  ? -12.55700 -30.60700 26.57500  1.000 24.92000 ? 45  ASP A CG   1 
ATOM   365  O OD1  . ASP A 1 45  ? -13.49100 -31.01800 27.29100  1.000 26.20000 ? 45  ASP A OD1  1 
ATOM   366  O OD2  . ASP A 1 45  ? -11.41100 -31.10400 26.60700  1.000 31.81000 ? 45  ASP A OD2  1 
ATOM   367  N N    . GLY A 1 46  ? -15.35300 -28.22800 27.91500  1.000 15.19000 ? 46  GLY A N    1 
ATOM   368  C CA   . GLY A 1 46  ? -15.49900 -27.65800 29.25100  1.000 16.62000 ? 46  GLY A CA   1 
ATOM   369  C C    . GLY A 1 46  ? -15.20300 -26.16600 29.23000  1.000 15.49000 ? 46  GLY A C    1 
ATOM   370  O O    . GLY A 1 46  ? -15.77000 -25.41000 28.43200  1.000 16.86000 ? 46  GLY A O    1 
ATOM   371  N N    . ASP A 1 47  ? -14.28700 -25.72800 30.09800  1.000 14.71000 ? 47  ASP A N    1 
ATOM   372  C CA   . ASP A 1 47  ? -13.85500 -24.33700 30.10700  1.000 12.99000 ? 47  ASP A CA   1 
ATOM   373  C C    . ASP A 1 47  ? -12.82900 -24.02900 29.02900  1.000 12.93000 ? 47  ASP A C    1 
ATOM   374  O O    . ASP A 1 47  ? -12.48900 -22.85600 28.84400  1.000 13.02000 ? 47  ASP A O    1 
ATOM   375  C CB   . ASP A 1 47  ? -13.17700 -23.99700 31.43700  1.000 13.35000 ? 47  ASP A CB   1 
ATOM   376  C CG   . ASP A 1 47  ? -14.14300 -23.89100 32.59000  1.000 16.71000 ? 47  ASP A CG   1 
ATOM   377  O OD1  . ASP A 1 47  ? -15.33900 -23.61700 32.36100  0.000 16.28000 ? 47  ASP A OD1  1 
ATOM   378  O OD2  . ASP A 1 47  ? -13.68300 -24.07800 33.74200  1.000 19.56000 ? 47  ASP A OD2  1 
ATOM   379  N N    . ASN A 1 48  ? -12.27900 -25.04200 28.35900  1.000 12.86000 ? 48  ASN A N    1 
ATOM   380  C CA   . ASN A 1 48  ? -11.11100 -24.84600 27.51200  1.000 12.42000 ? 48  ASN A CA   1 
ATOM   381  C C    . ASN A 1 48  ? -11.53900 -24.61400 26.07100  1.000 12.79000 ? 48  ASN A C    1 
ATOM   382  O O    . ASN A 1 48  ? -12.23200 -25.44700 25.47500  1.000 13.45000 ? 48  ASN A O    1 
ATOM   383  C CB   . ASN A 1 48  ? -10.16200 -26.03700 27.61100  1.000 15.08000 ? 48  ASN A CB   1 
ATOM   384  C CG   . ASN A 1 48  ? -9.59600  -26.20500 29.00800  1.000 18.58000 ? 48  ASN A CG   1 
ATOM   385  O OD1  . ASN A 1 48  ? -9.38100  -25.22400 29.72700  1.000 18.44000 ? 48  ASN A OD1  1 
ATOM   386  N ND2  . ASN A 1 48  ? -9.35600  -27.45100 29.40400  1.000 24.30000 ? 48  ASN A ND2  1 
ATOM   387  N N    . PHE A 1 49  ? -11.10600 -23.49300 25.51500  1.000 11.39000 ? 49  PHE A N    1 
ATOM   388  C CA   . PHE A 1 49  ? -11.41100 -23.11900 24.14700  1.000 11.50000 ? 49  PHE A CA   1 
ATOM   389  C C    . PHE A 1 49  ? -10.12100 -23.02800 23.34900  1.000 12.05000 ? 49  PHE A C    1 
ATOM   390  O O    . PHE A 1 49  ? -9.10400  -22.53200 23.84300  1.000 12.64000 ? 49  PHE A O    1 
ATOM   391  C CB   . PHE A 1 49  ? -12.06400 -21.73500 24.10600  1.000 11.31000 ? 49  PHE A CB   1 
ATOM   392  C CG   . PHE A 1 49  ? -13.53000 -21.72900 24.45400  1.000 11.30000 ? 49  PHE A CG   1 
ATOM   393  C CD1  . PHE A 1 49  ? -13.95800 -21.91200 25.76000  1.000 11.26000 ? 49  PHE A CD1  1 
ATOM   394  C CD2  . PHE A 1 49  ? -14.47700 -21.49600 23.47400  1.000 11.99000 ? 49  PHE A CD2  1 
ATOM   395  C CE1  . PHE A 1 49  ? -15.30500 -21.88800 26.07300  1.000 11.81000 ? 49  PHE A CE1  1 
ATOM   396  C CE2  . PHE A 1 49  ? -15.82200 -21.47000 23.78300  1.000 14.45000 ? 49  PHE A CE2  1 
ATOM   397  C CZ   . PHE A 1 49  ? -16.23400 -21.66400 25.09000  1.000 13.15000 ? 49  PHE A CZ   1 
ATOM   398  N N    . LYS A 1 50  ? -10.18600 -23.48800 22.10100  1.000 12.34000 ? 50  LYS A N    1 
ATOM   399  C CA   . LYS A 1 50  ? -9.16000  -23.22700 21.10100  1.000 14.42000 ? 50  LYS A CA   1 
ATOM   400  C C    . LYS A 1 50  ? -9.85800  -22.60000 19.90600  1.000 13.87000 ? 50  LYS A C    1 
ATOM   401  O O    . LYS A 1 50  ? -10.74400 -23.21700 19.30400  1.000 15.75000 ? 50  LYS A O    1 
ATOM   402  C CB   . LYS A 1 50  ? -8.43900  -24.51600 20.70500  1.000 17.90000 ? 50  LYS A CB   1 
ATOM   403  C CG   . LYS A 1 50  ? -7.71000  -25.15300 21.87100  1.000 17.85000 ? 50  LYS A CG   1 
ATOM   404  C CD   . LYS A 1 50  ? -6.94100  -26.39400 21.45500  1.000 23.31000 ? 50  LYS A CD   1 
ATOM   405  C CE   . LYS A 1 50  ? -7.85400  -27.41600 20.80500  0.670 23.47000 ? 50  LYS A CE   1 
ATOM   406  N NZ   . LYS A 1 50  ? -7.14700  -28.70500 20.55400  1.000 32.74000 ? 50  LYS A NZ   1 
ATOM   407  N N    . VAL A 1 51  ? -9.49900  -21.35900 19.59300  1.000 14.07000 ? 51  VAL A N    1 
ATOM   408  C CA   . VAL A 1 51  ? -10.15600 -20.58800 18.54500  1.000 14.88000 ? 51  VAL A CA   1 
ATOM   409  C C    . VAL A 1 51  ? -9.14000  -20.34400 17.44000  1.000 15.66000 ? 51  VAL A C    1 
ATOM   410  O O    . VAL A 1 51  ? -7.99800  -19.95600 17.71500  1.000 16.56000 ? 51  VAL A O    1 
ATOM   411  C CB   . VAL A 1 51  ? -10.70800 -19.26200 19.09600  1.000 15.18000 ? 51  VAL A CB   1 
ATOM   412  C CG1  . VAL A 1 51  ? -11.32100 -18.43600 17.97800  1.000 16.68000 ? 51  VAL A CG1  1 
ATOM   413  C CG2  . VAL A 1 51  ? -11.73900 -19.53100 20.18900  1.000 17.72000 ? 51  VAL A CG2  1 
ATOM   414  N N    . LYS A 1 52  ? -9.54500  -20.58400 16.19500  1.000 14.59000 ? 52  LYS A N    1 
ATOM   415  C CA   . LYS A 1 52  ? -8.67000  -20.39100 15.04400  1.000 15.00000 ? 52  LYS A CA   1 
ATOM   416  C C    . LYS A 1 52  ? -9.44000  -19.64300 13.97300  1.000 16.30000 ? 52  LYS A C    1 
ATOM   417  O O    . LYS A 1 52  ? -10.46200 -20.13500 13.48400  1.000 15.88000 ? 52  LYS A O    1 
ATOM   418  C CB   . LYS A 1 52  ? -8.16500  -21.73100 14.50400  1.000 18.78000 ? 52  LYS A CB   1 
ATOM   419  C CG   . LYS A 1 52  ? -7.22400  -22.45200 15.46300  1.000 19.62000 ? 52  LYS A CG   1 
ATOM   420  C CD   . LYS A 1 52  ? -6.91500  -23.87200 15.02200  1.000 24.71000 ? 52  LYS A CD   1 
ATOM   421  C CE   . LYS A 1 52  ? -6.50800  -24.72200 16.22000  1.000 28.08000 ? 52  LYS A CE   1 
ATOM   422  N NZ   . LYS A 1 52  ? -5.41400  -24.08100 17.00200  1.000 28.88000 ? 52  LYS A NZ   1 
ATOM   423  N N    . CYS A 1 53  ? -8.96100  -18.45200 13.62900  1.000 15.79000 ? 53  CYS A N    1 
ATOM   424  C CA   . CYS A 1 53  ? -9.55000  -17.63200 12.58300  1.000 16.87000 ? 53  CYS A CA   1 
ATOM   425  C C    . CYS A 1 53  ? -8.56200  -17.59000 11.43200  1.000 18.57000 ? 53  CYS A C    1 
ATOM   426  O O    . CYS A 1 53  ? -7.38300  -17.28200 11.63600  1.000 21.34000 ? 53  CYS A O    1 
ATOM   427  C CB   . CYS A 1 53  ? -9.80000  -16.21800 13.10400  1.000 21.70000 ? 53  CYS A CB   1 
ATOM   428  S SG   . CYS A 1 53  ? -10.24900 -16.14500 14.86400  1.000 30.18000 ? 53  CYS A SG   1 
ATOM   429  N N    . THR A 1 54  ? -9.03000  -17.91600 10.23000  1.000 16.57000 ? 54  THR A N    1 
ATOM   430  C CA   . THR A 1 54  ? -8.11900  -18.12200 9.11500   1.000 19.25000 ? 54  THR A CA   1 
ATOM   431  C C    . THR A 1 54  ? -8.61200  -17.42000 7.85900   1.000 18.28000 ? 54  THR A C    1 
ATOM   432  O O    . THR A 1 54  ? -9.81000  -17.42000 7.55800   1.000 16.60000 ? 54  THR A O    1 
ATOM   433  C CB   . THR A 1 54  ? -7.93300  -19.61300 8.82900   1.000 21.22000 ? 54  THR A CB   1 
ATOM   434  O OG1  . THR A 1 54  ? -9.20800  -20.22500 8.60300   1.000 24.99000 ? 54  THR A OG1  1 
ATOM   435  C CG2  . THR A 1 54  ? -7.25700  -20.29700 10.00900  1.000 24.28000 ? 54  THR A CG2  1 
ATOM   436  N N    . SER A 1 55  ? -7.66400  -16.83500 7.12900   1.000 18.90000 ? 55  SER A N    1 
ATOM   437  C CA   . SER A 1 55  ? -7.86900  -16.31700 5.78500   1.000 17.93000 ? 55  SER A CA   1 
ATOM   438  C C    . SER A 1 55  ? -6.62500  -16.66300 4.97600   1.000 17.29000 ? 55  SER A C    1 
ATOM   439  O O    . SER A 1 55  ? -5.66000  -17.22800 5.50100   1.000 20.16000 ? 55  SER A O    1 
ATOM   440  C CB   . SER A 1 55  ? -8.05900  -14.80100 5.80700   1.000 19.08000 ? 55  SER A CB   1 
ATOM   441  O OG   . SER A 1 55  ? -6.80700  -14.15700 5.95700   1.000 21.32000 ? 55  SER A OG   1 
ATOM   442  N N    . THR A 1 56  ? -6.64100  -16.30400 3.68700   1.000 18.10000 ? 56  THR A N    1 
ATOM   443  C CA   . THR A 1 56  ? -5.50800  -16.58900 2.80800   1.000 20.33000 ? 56  THR A CA   1 
ATOM   444  C C    . THR A 1 56  ? -4.20200  -16.03800 3.36500   1.000 19.97000 ? 56  THR A C    1 
ATOM   445  O O    . THR A 1 56  ? -3.17900  -16.73400 3.37200   1.000 24.80000 ? 56  THR A O    1 
ATOM   446  C CB   . THR A 1 56  ? -5.77100  -16.01000 1.41600   1.000 23.57000 ? 56  THR A CB   1 
ATOM   447  O OG1  . THR A 1 56  ? -6.02200  -14.60300 1.52100   1.000 30.96000 ? 56  THR A OG1  1 
ATOM   448  C CG2  . THR A 1 56  ? -6.97800  -16.68200 0.78700   1.000 25.34000 ? 56  THR A CG2  1 
ATOM   449  N N    . PHE A 1 57  ? -4.20400  -14.78400 3.81300   1.000 20.76000 ? 57  PHE A N    1 
ATOM   450  C CA   . PHE A 1 57  ? -2.97700  -14.10600 4.20800   1.000 27.79000 ? 57  PHE A CA   1 
ATOM   451  C C    . PHE A 1 57  ? -2.82400  -13.93500 5.71100   1.000 25.88000 ? 57  PHE A C    1 
ATOM   452  O O    . PHE A 1 57  ? -1.77500  -13.45900 6.15700   1.000 28.63000 ? 57  PHE A O    1 
ATOM   453  C CB   . PHE A 1 57  ? -2.89300  -12.72000 3.54700   1.000 26.90000 ? 57  PHE A CB   1 
ATOM   454  C CG   . PHE A 1 57  ? -2.79900  -12.76400 2.04900   1.000 28.21000 ? 57  PHE A CG   1 
ATOM   455  C CD1  . PHE A 1 57  ? -1.81400  -13.51000 1.42100   1.000 27.97000 ? 57  PHE A CD1  1 
ATOM   456  C CD2  . PHE A 1 57  ? -3.70100  -12.06000 1.26800   1.000 28.18000 ? 57  PHE A CD2  1 
ATOM   457  C CE1  . PHE A 1 57  ? -1.73000  -13.54900 0.03700   1.000 32.89000 ? 57  PHE A CE1  1 
ATOM   458  C CE2  . PHE A 1 57  ? -3.62300  -12.09500 -0.11000  1.000 31.34000 ? 57  PHE A CE2  1 
ATOM   459  C CZ   . PHE A 1 57  ? -2.63600  -12.84100 -0.72700  1.000 30.85000 ? 57  PHE A CZ   1 
ATOM   460  N N    . TRP A 1 58  ? -3.82300  -14.31900 6.49800   1.000 23.37000 ? 58  TRP A N    1 
ATOM   461  C CA   . TRP A 1 58  ? -3.90700  -13.90000 7.88600   1.000 21.66000 ? 58  TRP A CA   1 
ATOM   462  C C    . TRP A 1 58  ? -4.42400  -15.05500 8.72800   1.000 22.39000 ? 58  TRP A C    1 
ATOM   463  O O    . TRP A 1 58  ? -5.30000  -15.80700 8.29600   1.000 27.99000 ? 58  TRP A O    1 
ATOM   464  C CB   . TRP A 1 58  ? -4.88200  -12.71900 7.99600   1.000 26.86000 ? 58  TRP A CB   1 
ATOM   465  C CG   . TRP A 1 58  ? -4.52100  -11.69700 9.02500   1.000 27.88000 ? 58  TRP A CG   1 
ATOM   466  C CD1  . TRP A 1 58  ? -3.96900  -11.92700 10.24800  1.000 25.17000 ? 58  TRP A CD1  1 
ATOM   467  C CD2  . TRP A 1 58  ? -4.70100  -10.27500 8.92700   1.000 27.94000 ? 58  TRP A CD2  1 
ATOM   468  N NE1  . TRP A 1 58  ? -3.78800  -10.74200 10.91800  1.000 26.06000 ? 58  TRP A NE1  1 
ATOM   469  C CE2  . TRP A 1 58  ? -4.22700  -9.71100  10.12800  1.000 29.67000 ? 58  TRP A CE2  1 
ATOM   470  C CE3  . TRP A 1 58  ? -5.21100  -9.42500  7.93900   1.000 30.00000 ? 58  TRP A CE3  1 
ATOM   471  C CZ2  . TRP A 1 58  ? -4.25300  -8.33700  10.37200  1.000 27.06000 ? 58  TRP A CZ2  1 
ATOM   472  C CZ3  . TRP A 1 58  ? -5.23300  -8.06100  8.18300   1.000 30.46000 ? 58  TRP A CZ3  1 
ATOM   473  C CH2  . TRP A 1 58  ? -4.75500  -7.53200  9.38900   1.000 30.00000 ? 58  TRP A CH2  1 
ATOM   474  N N    . ASN A 1 59  ? -3.87500  -15.19600 9.92900   1.000 19.92000 ? 59  ASN A N    1 
ATOM   475  C CA   . ASN A 1 59  ? -4.38500  -16.16000 10.88800  1.000 21.52000 ? 59  ASN A CA   1 
ATOM   476  C C    . ASN A 1 59  ? -4.37500  -15.52300 12.26600  1.000 21.02000 ? 59  ASN A C    1 
ATOM   477  O O    . ASN A 1 59  ? -3.52900  -14.67900 12.57400  1.000 20.80000 ? 59  ASN A O    1 
ATOM   478  C CB   . ASN A 1 59  ? -3.55300  -17.44500 10.91400  1.000 23.14000 ? 59  ASN A CB   1 
ATOM   479  C CG   . ASN A 1 59  ? -3.64200  -18.22200 9.61600   1.000 28.64000 ? 59  ASN A CG   1 
ATOM   480  O OD1  . ASN A 1 59  ? -2.67300  -18.84800 9.18700   1.000 34.31000 ? 59  ASN A OD1  1 
ATOM   481  N ND2  . ASN A 1 59  ? -4.80800  -18.18800 8.98400   0.000 23.79000 ? 59  ASN A ND2  1 
ATOM   482  N N    . TYR A 1 60  ? -5.34100  -15.92400 13.08600  1.000 18.91000 ? 60  TYR A N    1 
ATOM   483  C CA   . TYR A 1 60  ? -5.43200  -15.46200 14.46700  1.000 19.18000 ? 60  TYR A CA   1 
ATOM   484  C C    . TYR A 1 60  ? -5.87100  -16.65200 15.30300  1.000 18.04000 ? 60  TYR A C    1 
ATOM   485  O O    . TYR A 1 60  ? -6.99800  -17.13300 15.15300  1.000 19.87000 ? 60  TYR A O    1 
ATOM   486  C CB   . TYR A 1 60  ? -6.43400  -14.31700 14.58500  1.000 18.20000 ? 60  TYR A CB   1 
ATOM   487  C CG   . TYR A 1 60  ? -6.44200  -13.63700 15.93200  1.000 21.48000 ? 60  TYR A CG   1 
ATOM   488  C CD1  . TYR A 1 60  ? -7.20200  -14.14000 16.98000  1.000 21.04000 ? 60  TYR A CD1  1 
ATOM   489  C CD2  . TYR A 1 60  ? -5.69900  -12.48800 16.15400  1.000 22.92000 ? 60  TYR A CD2  1 
ATOM   490  C CE1  . TYR A 1 60  ? -7.21500  -13.52100 18.21600  1.000 22.20000 ? 60  TYR A CE1  1 
ATOM   491  C CE2  . TYR A 1 60  ? -5.70400  -11.86300 17.38500  1.000 21.22000 ? 60  TYR A CE2  1 
ATOM   492  C CZ   . TYR A 1 60  ? -6.46600  -12.38200 18.41000  1.000 20.56000 ? 60  TYR A CZ   1 
ATOM   493  O OH   . TYR A 1 60  ? -6.47700  -11.76000 19.63700  1.000 21.68000 ? 60  TYR A OH   1 
ATOM   494  N N    . ASP A 1 61  ? -4.98600  -17.13500 16.16600  1.000 17.53000 ? 61  ASP A N    1 
ATOM   495  C CA   . ASP A 1 61  ? -5.25400  -18.29300 17.00100  1.000 17.31000 ? 61  ASP A CA   1 
ATOM   496  C C    . ASP A 1 61  ? -5.14700  -17.87300 18.45800  1.000 18.87000 ? 61  ASP A C    1 
ATOM   497  O O    . ASP A 1 61  ? -4.22100  -17.14600 18.83400  1.000 22.82000 ? 61  ASP A O    1 
ATOM   498  C CB   . ASP A 1 61  ? -4.24300  -19.41700 16.72800  1.000 22.94000 ? 61  ASP A CB   1 
ATOM   499  C CG   . ASP A 1 61  ? -4.40600  -20.04000 15.34800  1.000 25.88000 ? 61  ASP A CG   1 
ATOM   500  O OD1  . ASP A 1 61  ? -5.34900  -19.66700 14.62200  1.000 25.69000 ? 61  ASP A OD1  1 
ATOM   501  O OD2  . ASP A 1 61  ? -3.58600  -20.91500 14.99300  1.000 30.61000 ? 61  ASP A OD2  1 
ATOM   502  N N    . VAL A 1 62  ? -6.09600  -18.31600 19.27800  1.000 15.70000 ? 62  VAL A N    1 
ATOM   503  C CA   . VAL A 1 62  ? -6.05200  -18.02600 20.70800  1.000 15.72000 ? 62  VAL A CA   1 
ATOM   504  C C    . VAL A 1 62  ? -6.64700  -19.20300 21.46000  1.000 15.71000 ? 62  VAL A C    1 
ATOM   505  O O    . VAL A 1 62  ? -7.68600  -19.74500 21.07300  1.000 16.22000 ? 62  VAL A O    1 
ATOM   506  C CB   . VAL A 1 62  ? -6.76200  -16.69900 21.06000  1.000 18.01000 ? 62  VAL A CB   1 
ATOM   507  C CG1  . VAL A 1 62  ? -8.25600  -16.80200 20.80500  1.000 20.14000 ? 62  VAL A CG1  1 
ATOM   508  C CG2  . VAL A 1 62  ? -6.49000  -16.30900 22.51800  1.000 18.22000 ? 62  VAL A CG2  1 
ATOM   509  N N    . ASP A 1 63  ? -5.97300  -19.60000 22.53600  1.000 15.31000 ? 63  ASP A N    1 
ATOM   510  C CA   . ASP A 1 63  ? -6.47500  -20.61000 23.45100  1.000 15.00000 ? 63  ASP A CA   1 
ATOM   511  C C    . ASP A 1 63  ? -6.70200  -19.95700 24.80400  1.000 15.19000 ? 63  ASP A C    1 
ATOM   512  O O    . ASP A 1 63  ? -5.90300  -19.12300 25.23600  1.000 16.46000 ? 63  ASP A O    1 
ATOM   513  C CB   . ASP A 1 63  ? -5.47300  -21.74400 23.64000  1.000 17.82000 ? 63  ASP A CB   1 
ATOM   514  C CG   . ASP A 1 63  ? -5.12900  -22.44600 22.34500  1.000 19.20000 ? 63  ASP A CG   1 
ATOM   515  O OD1  . ASP A 1 63  ? -5.85800  -22.27900 21.34800  1.000 19.00000 ? 63  ASP A OD1  1 
ATOM   516  O OD2  . ASP A 1 63  ? -4.12100  -23.18600 22.33600  1.000 28.21000 ? 63  ASP A OD2  1 
ATOM   517  N N    . PHE A 1 64  ? -7.79100  -20.32900 25.47200  1.000 12.78000 ? 64  PHE A N    1 
ATOM   518  C CA   . PHE A 1 64  ? -8.07800  -19.74300 26.77400  1.000 12.19000 ? 64  PHE A CA   1 
ATOM   519  C C    . PHE A 1 64  ? -8.93900  -20.69600 27.58400  1.000 11.80000 ? 64  PHE A C    1 
ATOM   520  O O    . PHE A 1 64  ? -9.57600  -21.61000 27.04900  1.000 12.47000 ? 64  PHE A O    1 
ATOM   521  C CB   . PHE A 1 64  ? -8.74600  -18.36300 26.66600  1.000 13.34000 ? 64  PHE A CB   1 
ATOM   522  C CG   . PHE A 1 64  ? -10.04500 -18.36400 25.90500  1.000 12.84000 ? 64  PHE A CG   1 
ATOM   523  C CD1  . PHE A 1 64  ? -11.22700 -18.75000 26.51500  1.000 13.76000 ? 64  PHE A CD1  1 
ATOM   524  C CD2  . PHE A 1 64  ? -10.08300 -17.95700 24.57900  1.000 15.02000 ? 64  PHE A CD2  1 
ATOM   525  C CE1  . PHE A 1 64  ? -12.41200 -18.75100 25.81800  1.000 11.91000 ? 64  PHE A CE1  1 
ATOM   526  C CE2  . PHE A 1 64  ? -11.27100 -17.95100 23.88000  1.000 12.95000 ? 64  PHE A CE2  1 
ATOM   527  C CZ   . PHE A 1 64  ? -12.43800 -18.35500 24.50000  1.000 13.81000 ? 64  PHE A CZ   1 
ATOM   528  N N    . THR A 1 65  ? -8.95400  -20.45700 28.89000  1.000 11.18000 ? 65  THR A N    1 
ATOM   529  C CA   . THR A 1 65  ? -9.81500  -21.16200 29.82400  1.000 11.36000 ? 65  THR A CA   1 
ATOM   530  C C    . THR A 1 65  ? -10.79400 -20.16000 30.42400  1.000 9.97000  ? 65  THR A C    1 
ATOM   531  O O    . THR A 1 65  ? -10.38100 -19.10800 30.92400  1.000 9.73000  ? 65  THR A O    1 
ATOM   532  C CB   . THR A 1 65  ? -8.97000  -21.80100 30.93400  1.000 12.03000 ? 65  THR A CB   1 
ATOM   533  O OG1  . THR A 1 65  ? -8.05100  -22.74000 30.36300  1.000 14.76000 ? 65  THR A OG1  1 
ATOM   534  C CG2  . THR A 1 65  ? -9.84400  -22.51900 31.95600  1.000 14.24000 ? 65  THR A CG2  1 
ATOM   535  N N    . VAL A 1 66  ? -12.09000 -20.46700 30.32300  1.000 10.08000 ? 66  VAL A N    1 
ATOM   536  C CA   . VAL A 1 66  ? -13.10600 -19.58400 30.88700  1.000 10.17000 ? 66  VAL A CA   1 
ATOM   537  C C    . VAL A 1 66  ? -12.79700 -19.35100 32.35400  1.000 9.51000  ? 66  VAL A C    1 
ATOM   538  O O    . VAL A 1 66  ? -12.50400 -20.29900 33.09500  1.000 10.35000 ? 66  VAL A O    1 
ATOM   539  C CB   . VAL A 1 66  ? -14.50600 -20.19300 30.68600  1.000 11.16000 ? 66  VAL A CB   1 
ATOM   540  C CG1  . VAL A 1 66  ? -15.53700 -19.47300 31.54600  1.000 12.68000 ? 66  VAL A CG1  1 
ATOM   541  C CG2  . VAL A 1 66  ? -14.90900 -20.14700 29.20900  1.000 13.71000 ? 66  VAL A CG2  1 
ATOM   542  N N    . GLY A 1 67  ? -12.82400 -18.08600 32.76900  1.000 8.28000  ? 67  GLY A N    1 
ATOM   543  C CA   . GLY A 1 67  ? -12.64100 -17.71900 34.15900  1.000 9.23000  ? 67  GLY A CA   1 
ATOM   544  C C    . GLY A 1 67  ? -11.21000 -17.50200 34.59400  1.000 8.38000  ? 67  GLY A C    1 
ATOM   545  O O    . GLY A 1 67  ? -10.98600 -17.19700 35.77500  1.000 9.65000  ? 67  GLY A O    1 
ATOM   546  N N    . VAL A 1 68  ? -10.23700 -17.66000 33.69200  1.000 8.74000  ? 68  VAL A N    1 
ATOM   547  C CA   . VAL A 1 68  ? -8.81400  -17.55700 34.00100  1.000 9.53000  ? 68  VAL A CA   1 
ATOM   548  C C    . VAL A 1 68  ? -8.21300  -16.42600 33.17700  1.000 9.36000  ? 68  VAL A C    1 
ATOM   549  O O    . VAL A 1 68  ? -8.13900  -16.51400 31.94100  1.000 9.81000  ? 68  VAL A O    1 
ATOM   550  C CB   . VAL A 1 68  ? -8.08100  -18.87600 33.71100  1.000 9.97000  ? 68  VAL A CB   1 
ATOM   551  C CG1  . VAL A 1 68  ? -6.56900  -18.73300 33.95800  1.000 12.74000 ? 68  VAL A CG1  1 
ATOM   552  C CG2  . VAL A 1 68  ? -8.65100  -20.00500 34.54100  1.000 12.81000 ? 68  VAL A CG2  1 
ATOM   553  N N    . GLU A 1 69  ? -7.76400  -15.37500 33.84200  1.000 9.63000  ? 69  GLU A N    1 
ATOM   554  C CA   . GLU A 1 69  ? -7.13800  -14.28100 33.11400  1.000 9.96000  ? 69  GLU A CA   1 
ATOM   555  C C    . GLU A 1 69  ? -5.85700  -14.76800 32.44800  1.000 9.68000  ? 69  GLU A C    1 
ATOM   556  O O    . GLU A 1 69  ? -5.13200  -15.60700 32.99700  1.000 11.05000 ? 69  GLU A O    1 
ATOM   557  C CB   . GLU A 1 69  ? -6.81700  -13.14800 34.08300  1.000 11.87000 ? 69  GLU A CB   1 
ATOM   558  C CG   . GLU A 1 69  ? -6.34400  -11.87200 33.39600  1.000 14.11000 ? 69  GLU A CG   1 
ATOM   559  C CD   . GLU A 1 69  ? -5.98200  -10.78400 34.38600  1.000 18.90000 ? 69  GLU A CD   1 
ATOM   560  O OE1  . GLU A 1 69  ? -5.01100  -10.97100 35.14900  1.000 22.39000 ? 69  GLU A OE1  1 
ATOM   561  O OE2  . GLU A 1 69  ? -6.67300  -9.75000  34.39500  1.000 22.65000 ? 69  GLU A OE2  1 
ATOM   562  N N    . PHE A 1 70  ? -5.57000  -14.25400 31.24700  1.000 9.13000  ? 70  PHE A N    1 
ATOM   563  C CA   . PHE A 1 70  ? -4.37100  -14.64900 30.51600  1.000 10.61000 ? 70  PHE A CA   1 
ATOM   564  C C    . PHE A 1 70  ? -3.72200  -13.43600 29.87000  1.000 11.33000 ? 70  PHE A C    1 
ATOM   565  O O    . PHE A 1 70  ? -4.39900  -12.51800 29.40400  1.000 11.05000 ? 70  PHE A O    1 
ATOM   566  C CB   . PHE A 1 70  ? -4.63500  -15.78900 29.50200  1.000 13.10000 ? 70  PHE A CB   1 
ATOM   567  C CG   . PHE A 1 70  ? -5.69200  -15.49300 28.46100  1.000 13.24000 ? 70  PHE A CG   1 
ATOM   568  C CD1  . PHE A 1 70  ? -7.03600  -15.47900 28.79100  1.000 14.01000 ? 70  PHE A CD1  1 
ATOM   569  C CD2  . PHE A 1 70  ? -5.32900  -15.30800 27.12800  1.000 16.81000 ? 70  PHE A CD2  1 
ATOM   570  C CE1  . PHE A 1 70  ? -7.99500  -15.23500 27.82400  1.000 16.10000 ? 70  PHE A CE1  1 
ATOM   571  C CE2  . PHE A 1 70  ? -6.28900  -15.07000 26.16500  1.000 17.31000 ? 70  PHE A CE2  1 
ATOM   572  C CZ   . PHE A 1 70  ? -7.61600  -15.03600 26.50900  1.000 19.56000 ? 70  PHE A CZ   1 
ATOM   573  N N    . ASP A 1 71  ? -2.38900  -13.42100 29.89100  1.000 12.77000 ? 71  ASP A N    1 
ATOM   574  C CA   . ASP A 1 71  ? -1.64100  -12.43300 29.13000  1.000 14.13000 ? 71  ASP A CA   1 
ATOM   575  C C    . ASP A 1 71  ? -1.74100  -12.76800 27.65700  1.000 15.27000 ? 71  ASP A C    1 
ATOM   576  O O    . ASP A 1 71  ? -1.49900  -13.90700 27.24700  1.000 20.13000 ? 71  ASP A O    1 
ATOM   577  C CB   . ASP A 1 71  ? -0.17500  -12.45800 29.54900  1.000 16.88000 ? 71  ASP A CB   1 
ATOM   578  C CG   . ASP A 1 71  ? 0.05000   -11.79300 30.87000  1.000 16.98000 ? 71  ASP A CG   1 
ATOM   579  O OD1  . ASP A 1 71  ? -0.19900  -10.58300 30.99700  1.000 17.33000 ? 71  ASP A OD1  1 
ATOM   580  O OD2  . ASP A 1 71  ? 0.47500   -12.50000 31.81000  1.000 21.27000 ? 71  ASP A OD2  1 
ATOM   581  N N    . GLU A 1 72  ? -2.09300  -11.78000 26.86700  1.000 13.21000 ? 72  GLU A N    1 
ATOM   582  C CA   . GLU A 1 72  ? -2.23700  -11.97300 25.44200  1.000 16.08000 ? 72  GLU A CA   1 
ATOM   583  C C    . GLU A 1 72  ? -1.38500  -10.94500 24.72700  1.000 14.19000 ? 72  GLU A C    1 
ATOM   584  O O    . GLU A 1 72  ? -1.33200  -9.77900  25.12500  1.000 14.26000 ? 72  GLU A O    1 
ATOM   585  C CB   . GLU A 1 72  ? -3.68000  -11.76300 25.06400  1.000 18.08000 ? 72  GLU A CB   1 
ATOM   586  C CG   . GLU A 1 72  ? -4.03200  -12.18300 23.68400  1.000 18.27000 ? 72  GLU A CG   1 
ATOM   587  C CD   . GLU A 1 72  ? -5.52000  -12.35400 23.55600  1.000 21.13000 ? 72  GLU A CD   1 
ATOM   588  O OE1  . GLU A 1 72  ? -6.28000  -11.48900 24.07300  1.000 17.91000 ? 72  GLU A OE1  1 
ATOM   589  O OE2  . GLU A 1 72  ? -5.92900  -13.38300 22.99100  1.000 24.84000 ? 72  GLU A OE2  1 
ATOM   590  N N    . TYR A 1 73  ? -0.71000  -11.39400 23.68000  1.000 14.34000 ? 73  TYR A N    1 
ATOM   591  C CA   . TYR A 1 73  ? 0.06600   -10.53000 22.80200  1.000 12.19000 ? 73  TYR A CA   1 
ATOM   592  C C    . TYR A 1 73  ? -0.52100  -10.75300 21.41800  1.000 15.58000 ? 73  TYR A C    1 
ATOM   593  O O    . TYR A 1 73  ? -0.40000  -11.84700 20.85200  1.000 17.00000 ? 73  TYR A O    1 
ATOM   594  C CB   . TYR A 1 73  ? 1.55400   -10.88400 22.87000  1.000 13.81000 ? 73  TYR A CB   1 
ATOM   595  C CG   . TYR A 1 73  ? 2.11300   -10.79400 24.27900  1.000 13.96000 ? 73  TYR A CG   1 
ATOM   596  C CD1  . TYR A 1 73  ? 2.05900   -11.87700 25.14000  1.000 14.81000 ? 73  TYR A CD1  1 
ATOM   597  C CD2  . TYR A 1 73  ? 2.67200   -9.61600  24.74800  1.000 15.49000 ? 73  TYR A CD2  1 
ATOM   598  C CE1  . TYR A 1 73  ? 2.55600   -11.79100 26.43400  1.000 16.44000 ? 73  TYR A CE1  1 
ATOM   599  C CE2  . TYR A 1 73  ? 3.17700   -9.52500  26.02700  1.000 19.89000 ? 73  TYR A CE2  1 
ATOM   600  C CZ   . TYR A 1 73  ? 3.11300   -10.61300 26.86000  1.000 16.49000 ? 73  TYR A CZ   1 
ATOM   601  O OH   . TYR A 1 73  ? 3.61500   -10.50500 28.13900  1.000 21.71000 ? 73  TYR A OH   1 
ATOM   602  N N    . THR A 1 74  ? -1.22100  -9.74200  20.90800  1.000 12.38000 ? 74  THR A N    1 
ATOM   603  C CA   . THR A 1 74  ? -1.98200  -9.85200  19.66300  1.000 10.50000 ? 74  THR A CA   1 
ATOM   604  C C    . THR A 1 74  ? -1.04000  -9.74600  18.45500  1.000 11.69000 ? 74  THR A C    1 
ATOM   605  O O    . THR A 1 74  ? -1.14800  -8.86100  17.61200  1.000 11.57000 ? 74  THR A O    1 
ATOM   606  C CB   . THR A 1 74  ? -3.07400  -8.79300  19.67300  1.000 11.02000 ? 74  THR A CB   1 
ATOM   607  O OG1  . THR A 1 74  ? -2.47400  -7.52200  19.94200  1.000 12.76000 ? 74  THR A OG1  1 
ATOM   608  C CG2  . THR A 1 74  ? -4.10200  -9.10400  20.76900  1.000 12.04000 ? 74  THR A CG2  1 
ATOM   609  N N    . LYS A 1 75  ? -0.10800  -10.70900 18.39000  1.000 11.90000 ? 75  LYS A N    1 
ATOM   610  C CA   . LYS A 1 75  ? 1.04200   -10.60500 17.48700  1.000 12.93000 ? 75  LYS A CA   1 
ATOM   611  C C    . LYS A 1 75  ? 0.62700   -10.45200 16.02800  1.000 13.54000 ? 75  LYS A C    1 
ATOM   612  O O    . LYS A 1 75  ? 1.30300   -9.75800  15.26000  1.000 15.06000 ? 75  LYS A O    1 
ATOM   613  C CB   . LYS A 1 75  ? 1.98000   -11.80900 17.64900  1.000 14.06000 ? 75  LYS A CB   1 
ATOM   614  C CG   . LYS A 1 75  ? 2.52500   -12.04500 19.06300  1.000 14.06000 ? 75  LYS A CG   1 
ATOM   615  C CD   . LYS A 1 75  ? 3.22900   -10.82400 19.65400  1.000 14.79000 ? 75  LYS A CD   1 
ATOM   616  C CE   . LYS A 1 75  ? 4.52400   -10.50500 18.92900  1.000 14.03000 ? 75  LYS A CE   1 
ATOM   617  N NZ   . LYS A 1 75  ? 5.17300   -9.29700  19.49400  1.000 14.83000 ? 75  LYS A NZ   1 
ATOM   618  N N    . SER A 1 76  ? -0.45200  -11.11500 15.61100  1.000 14.68000 ? 76  SER A N    1 
ATOM   619  C CA   . SER A 1 76  ? -0.89100  -11.05700 14.21800  1.000 16.72000 ? 76  SER A CA   1 
ATOM   620  C C    . SER A 1 76  ? -1.89000  -9.94000  13.95000  1.000 17.01000 ? 76  SER A C    1 
ATOM   621  O O    . SER A 1 76  ? -2.30600  -9.75800  12.79900  1.000 20.01000 ? 76  SER A O    1 
ATOM   622  C CB   . SER A 1 76  ? -1.46300  -12.40700 13.76600  0.000 19.50000 ? 76  SER A CB   1 
ATOM   623  O OG   . SER A 1 76  ? -2.70600  -12.68000 14.38800  1.000 18.97000 ? 76  SER A OG   1 
ATOM   624  N N    . LEU A 1 77  ? -2.27000  -9.18300  14.97600  1.000 13.82000 ? 77  LEU A N    1 
ATOM   625  C CA   . LEU A 1 77  ? -3.23100  -8.09900  14.83900  1.000 13.98000 ? 77  LEU A CA   1 
ATOM   626  C C    . LEU A 1 77  ? -2.53200  -6.76500  15.07400  1.000 13.54000 ? 77  LEU A C    1 
ATOM   627  O O    . LEU A 1 77  ? -1.74100  -6.32300  14.23500  1.000 14.81000 ? 77  LEU A O    1 
ATOM   628  C CB   . LEU A 1 77  ? -4.37200  -8.30700  15.83000  1.000 16.44000 ? 77  LEU A CB   1 
ATOM   629  C CG   . LEU A 1 77  ? -5.70100  -7.60000  15.58600  1.000 16.38000 ? 77  LEU A CG   1 
ATOM   630  C CD1  . LEU A 1 77  ? -6.24200  -7.86800  14.18400  1.000 21.14000 ? 77  LEU A CD1  1 
ATOM   631  C CD2  . LEU A 1 77  ? -6.70100  -8.03100  16.65100  1.000 17.31000 ? 77  LEU A CD2  1 
ATOM   632  N N    . ASP A 1 78  ? -2.79200  -6.12300  16.20700  1.000 12.45000 ? 78  ASP A N    1 
ATOM   633  C CA   . ASP A 1 78  ? -2.22500  -4.81600  16.49500  1.000 10.73000 ? 78  ASP A CA   1 
ATOM   634  C C    . ASP A 1 78  ? -0.95100  -4.88900  17.32800  1.000 10.36000 ? 78  ASP A C    1 
ATOM   635  O O    . ASP A 1 78  ? -0.37000  -3.84200  17.64500  1.000 11.70000 ? 78  ASP A O    1 
ATOM   636  C CB   . ASP A 1 78  ? -3.26200  -3.90100  17.16400  1.000 10.96000 ? 78  ASP A CB   1 
ATOM   637  C CG   . ASP A 1 78  ? -3.81500  -4.47000  18.46100  1.000 10.93000 ? 78  ASP A CG   1 
ATOM   638  O OD1  . ASP A 1 78  ? -4.13000  -5.68600  18.52200  1.000 10.96000 ? 78  ASP A OD1  1 
ATOM   639  O OD2  . ASP A 1 78  ? -3.93500  -3.67500  19.41400  1.000 11.45000 ? 78  ASP A OD2  1 
ATOM   640  N N    . ASN A 1 79  ? -0.52000  -6.09400  17.69900  1.000 10.44000 ? 79  ASN A N    1 
ATOM   641  C CA   . ASN A 1 79  ? 0.75200   -6.29800  18.39400  1.000 11.41000 ? 79  ASN A CA   1 
ATOM   642  C C    . ASN A 1 79  ? 0.80600   -5.56900  19.73700  1.000 11.27000 ? 79  ASN A C    1 
ATOM   643  O O    . ASN A 1 79  ? 1.75800   -4.83800  20.03700  1.000 13.58000 ? 79  ASN A O    1 
ATOM   644  C CB   . ASN A 1 79  ? 1.94600   -5.91600  17.51800  1.000 12.25000 ? 79  ASN A CB   1 
ATOM   645  C CG   . ASN A 1 79  ? 3.24700   -6.40800  18.09400  1.000 13.18000 ? 79  ASN A CG   1 
ATOM   646  O OD1  . ASN A 1 79  ? 3.28100   -7.44900  18.75000  1.000 14.80000 ? 79  ASN A OD1  1 
ATOM   647  N ND2  . ASN A 1 79  ? 4.32500   -5.65900  17.87000  1.000 13.21000 ? 79  ASN A ND2  1 
ATOM   648  N N    . ARG A 1 80  ? -0.21900  -5.78300  20.56700  1.000 11.01000 ? 80  ARG A N    1 
ATOM   649  C CA   . ARG A 1 80  ? -0.28400  -5.18700  21.89200  1.000 11.70000 ? 80  ARG A CA   1 
ATOM   650  C C    . ARG A 1 80  ? -0.42400  -6.27200  22.94800  1.000 10.20000 ? 80  ARG A C    1 
ATOM   651  O O    . ARG A 1 80  ? -0.92200  -7.37000  22.68300  1.000 12.83000 ? 80  ARG A O    1 
ATOM   652  C CB   . ARG A 1 80  ? -1.44800  -4.19500  22.02200  1.000 11.86000 ? 80  ARG A CB   1 
ATOM   653  C CG   . ARG A 1 80  ? -1.23700  -2.89200  21.27800  1.000 13.13000 ? 80  ARG A CG   1 
ATOM   654  C CD   . ARG A 1 80  ? -2.34200  -1.91100  21.62200  1.000 14.67000 ? 80  ARG A CD   1 
ATOM   655  N NE   . ARG A 1 80  ? -2.08500  -0.58300  21.07600  1.000 16.02000 ? 80  ARG A NE   1 
ATOM   656  C CZ   . ARG A 1 80  ? -2.56300  -0.13300  19.91900  1.000 16.88000 ? 80  ARG A CZ   1 
ATOM   657  N NH1  . ARG A 1 80  ? -3.35400  -0.89100  19.16100  1.000 16.00000 ? 80  ARG A NH1  1 
ATOM   658  N NH2  . ARG A 1 80  ? -2.25900  1.09700   19.52500  1.000 20.52000 ? 80  ARG A NH2  1 
ATOM   659  N N    . HIS A 1 81  ? 0.04600   -5.94600  24.14800  1.000 11.64000 ? 81  HIS A N    1 
ATOM   660  C CA   . HIS A 1 81  ? -0.13800  -6.77200  25.33100  1.000 12.29000 ? 81  HIS A CA   1 
ATOM   661  C C    . HIS A 1 81  ? -1.44600  -6.36800  26.00200  1.000 11.03000 ? 81  HIS A C    1 
ATOM   662  O O    . HIS A 1 81  ? -1.65300  -5.19400  26.32300  1.000 11.83000 ? 81  HIS A O    1 
ATOM   663  C CB   . HIS A 1 81  ? 1.04600   -6.56700  26.27400  1.000 13.20000 ? 81  HIS A CB   1 
ATOM   664  C CG   . HIS A 1 81  ? 0.95500   -7.34800  27.54800  1.000 14.06000 ? 81  HIS A CG   1 
ATOM   665  N ND1  . HIS A 1 81  ? 1.71700   -7.05100  28.65800  1.000 23.50000 ? 81  HIS A ND1  1 
ATOM   666  C CD2  . HIS A 1 81  ? 0.22100   -8.43800  27.87400  1.000 13.04000 ? 81  HIS A CD2  1 
ATOM   667  C CE1  . HIS A 1 81  ? 1.43300   -7.90800  29.62400  1.000 23.02000 ? 81  HIS A CE1  1 
ATOM   668  N NE2  . HIS A 1 81  ? 0.52500   -8.75600  29.17700  1.000 18.00000 ? 81  HIS A NE2  1 
ATOM   669  N N    . VAL A 1 82  ? -2.33500  -7.34000  26.19400  1.000 10.84000 ? 82  VAL A N    1 
ATOM   670  C CA   . VAL A 1 82  ? -3.55900  -7.12400  26.95500  1.000 10.98000 ? 82  VAL A CA   1 
ATOM   671  C C    . VAL A 1 82  ? -3.68600  -8.23100  27.99100  1.000 10.93000 ? 82  VAL A C    1 
ATOM   672  O O    . VAL A 1 82  ? -3.08500  -9.30000  27.87300  1.000 11.11000 ? 82  VAL A O    1 
ATOM   673  C CB   . VAL A 1 82  ? -4.82900  -7.06300  26.07300  1.000 10.33000 ? 82  VAL A CB   1 
ATOM   674  C CG1  . VAL A 1 82  ? -4.77300  -5.87200  25.13900  1.000 11.74000 ? 82  VAL A CG1  1 
ATOM   675  C CG2  . VAL A 1 82  ? -5.00900  -8.36400  25.29900  1.000 11.32000 ? 82  VAL A CG2  1 
ATOM   676  N N    . LYS A 1 83  ? -4.49700  -7.96900  29.01900  1.000 10.70000 ? 83  LYS A N    1 
ATOM   677  C CA   . LYS A 1 83  ? -4.85300  -8.98000  30.03000  1.000 11.39000 ? 83  LYS A CA   1 
ATOM   678  C C    . LYS A 1 83  ? -6.29900  -9.36900  29.65100  1.000 9.17000  ? 83  LYS A C    1 
ATOM   679  O O    . LYS A 1 83  ? -7.20800  -8.59100  29.79700  1.000 10.69000 ? 83  LYS A O    1 
ATOM   680  C CB   . LYS A 1 83  ? -4.75000  -8.44500  31.46600  1.000 13.51000 ? 83  LYS A CB   1 
ATOM   681  C CG   . LYS A 1 83  ? -3.30900  -8.30500  31.93600  1.000 18.35000 ? 83  LYS A CG   1 
ATOM   682  C CD   . LYS A 1 83  ? -3.18200  -8.59000  33.42400  0.000 19.86000 ? 83  LYS A CD   1 
ATOM   683  C CE   . LYS A 1 83  ? -1.73500  -8.50600  33.88000  0.000 21.77000 ? 83  LYS A CE   1 
ATOM   684  N NZ   . LYS A 1 83  ? -0.96200  -9.72200  33.50200  1.000 24.99000 ? 83  LYS A NZ   1 
ATOM   685  N N    . ALA A 1 84  ? -6.46900  -10.58100 29.15300  1.000 9.19000  ? 84  ALA A N    1 
ATOM   686  C CA   . ALA A 1 84  ? -7.73900  -11.04500 28.60600  1.000 9.33000  ? 84  ALA A CA   1 
ATOM   687  C C    . ALA A 1 84  ? -8.44700  -11.96800 29.58700  1.000 9.63000  ? 84  ALA A C    1 
ATOM   688  O O    . ALA A 1 84  ? -7.82100  -12.72300 30.32900  1.000 10.57000 ? 84  ALA A O    1 
ATOM   689  C CB   . ALA A 1 84  ? -7.50500  -11.78700 27.28600  1.000 10.50000 ? 84  ALA A CB   1 
ATOM   690  N N    . LEU A 1 85  ? -9.77400  -11.91800 29.55800  1.000 9.73000  ? 85  LEU A N    1 
ATOM   691  C CA   . LEU A 1 85  ? -10.58200 -12.74500 30.43900  1.000 9.00000  ? 85  LEU A CA   1 
ATOM   692  C C    . LEU A 1 85  ? -11.88400 -13.05300 29.71500  1.000 8.30000  ? 85  LEU A C    1 
ATOM   693  O O    . LEU A 1 85  ? -12.54300 -12.13100 29.22300  1.000 9.54000  ? 85  LEU A O    1 
ATOM   694  C CB   . LEU A 1 85  ? -10.85900 -12.00100 31.75300  1.000 10.28000 ? 85  LEU A CB   1 
ATOM   695  C CG   . LEU A 1 85  ? -11.82200 -12.69000 32.71800  1.000 10.29000 ? 85  LEU A CG   1 
ATOM   696  C CD1  . LEU A 1 85  ? -11.24300 -13.99300 33.22900  1.000 11.85000 ? 85  LEU A CD1  1 
ATOM   697  C CD2  . LEU A 1 85  ? -12.16300 -11.74400 33.86800  1.000 14.84000 ? 85  LEU A CD2  1 
ATOM   698  N N    . VAL A 1 86  ? -12.25500 -14.33100 29.66000  1.000 7.88000  ? 86  VAL A N    1 
ATOM   699  C CA   . VAL A 1 86  ? -13.48300 -14.77900 29.00400  1.000 8.45000  ? 86  VAL A CA   1 
ATOM   700  C C    . VAL A 1 86  ? -14.37400 -15.42800 30.05600  1.000 8.43000  ? 86  VAL A C    1 
ATOM   701  O O    . VAL A 1 86  ? -13.91600 -16.29800 30.80600  1.000 9.15000  ? 86  VAL A O    1 
ATOM   702  C CB   . VAL A 1 86  ? -13.19300 -15.73900 27.82800  1.000 9.36000  ? 86  VAL A CB   1 
ATOM   703  C CG1  . VAL A 1 86  ? -14.50200 -16.10000 27.09800  1.000 10.83000 ? 86  VAL A CG1  1 
ATOM   704  C CG2  . VAL A 1 86  ? -12.18400 -15.12500 26.84900  1.000 9.03000  ? 86  VAL A CG2  1 
ATOM   705  N N    . THR A 1 87  ? -15.63400 -14.99500 30.11500  1.000 7.96000  ? 87  THR A N    1 
ATOM   706  C CA   . THR A 1 87  ? -16.59000 -15.44300 31.12200  1.000 7.75000  ? 87  THR A CA   1 
ATOM   707  C C    . THR A 1 87  ? -17.96700 -15.59000 30.48300  1.000 8.08000  ? 87  THR A C    1 
ATOM   708  O O    . THR A 1 87  ? -18.21800 -15.09900 29.37700  1.000 8.99000  ? 87  THR A O    1 
ATOM   709  C CB   . THR A 1 87  ? -16.67000 -14.45200 32.29200  1.000 9.53000  ? 87  THR A CB   1 
ATOM   710  O OG1  . THR A 1 87  ? -16.99900 -13.15000 31.79600  1.000 11.24000 ? 87  THR A OG1  1 
ATOM   711  C CG2  . THR A 1 87  ? -15.35500 -14.40900 33.04300  1.000 12.04000 ? 87  THR A CG2  1 
ATOM   712  N N    . TRP A 1 88  ? -18.86600 -16.27400 31.19500  1.000 9.18000  ? 88  TRP A N    1 
ATOM   713  C CA   . TRP A 1 88  ? -20.26200 -16.39900 30.78900  1.000 9.78000  ? 88  TRP A CA   1 
ATOM   714  C C    . TRP A 1 88  ? -21.11900 -15.36600 31.50600  1.000 9.98000  ? 88  TRP A C    1 
ATOM   715  O O    . TRP A 1 88  ? -21.03700 -15.22500 32.73600  1.000 10.62000 ? 88  TRP A O    1 
ATOM   716  C CB   . TRP A 1 88  ? -20.81300 -17.77300 31.15200  1.000 11.31000 ? 88  TRP A CB   1 
ATOM   717  C CG   . TRP A 1 88  ? -20.21000 -18.87100 30.38100  1.000 11.34000 ? 88  TRP A CG   1 
ATOM   718  C CD1  . TRP A 1 88  ? -19.29800 -19.77600 30.83400  1.000 12.94000 ? 88  TRP A CD1  1 
ATOM   719  C CD2  . TRP A 1 88  ? -20.46600 -19.20400 29.01300  1.000 11.57000 ? 88  TRP A CD2  1 
ATOM   720  N NE1  . TRP A 1 88  ? -18.97400 -20.65400 29.83600  1.000 13.93000 ? 88  TRP A NE1  1 
ATOM   721  C CE2  . TRP A 1 88  ? -19.67700 -20.33000 28.70700  1.000 13.44000 ? 88  TRP A CE2  1 
ATOM   722  C CE3  . TRP A 1 88  ? -21.29900 -18.67200 28.02500  1.000 11.72000 ? 88  TRP A CE3  1 
ATOM   723  C CZ2  . TRP A 1 88  ? -19.68200 -20.92400 27.44500  1.000 17.19000 ? 88  TRP A CZ2  1 
ATOM   724  C CZ3  . TRP A 1 88  ? -21.30100 -19.26300 26.76700  1.000 15.35000 ? 88  TRP A CZ3  1 
ATOM   725  C CH2  . TRP A 1 88  ? -20.49600 -20.37800 26.49300  1.000 16.04000 ? 88  TRP A CH2  1 
ATOM   726  N N    . GLU A 1 89  ? -21.96300 -14.67300 30.75000  1.000 9.54000  ? 89  GLU A N    1 
ATOM   727  C CA   . GLU A 1 89  ? -23.00900 -13.80100 31.27100  1.000 10.82000 ? 89  GLU A CA   1 
ATOM   728  C C    . GLU A 1 89  ? -24.30000 -14.41300 30.75800  1.000 11.63000 ? 89  GLU A C    1 
ATOM   729  O O    . GLU A 1 89  ? -24.72400 -14.13400 29.63100  1.000 11.84000 ? 89  GLU A O    1 
ATOM   730  C CB   . GLU A 1 89  ? -22.82600 -12.40300 30.75400  1.000 14.89000 ? 89  GLU A CB   1 
ATOM   731  C CG   . GLU A 1 89  ? -21.71500 -11.66100 31.44100  1.000 18.46000 ? 89  GLU A CG   1 
ATOM   732  C CD   . GLU A 1 89  ? -21.64000 -10.20100 31.04800  1.000 22.55000 ? 89  GLU A CD   1 
ATOM   733  O OE1  . GLU A 1 89  ? -22.61200 -9.67500  30.45800  1.000 24.11000 ? 89  GLU A OE1  1 
ATOM   734  O OE2  . GLU A 1 89  ? -20.59400 -9.58300  31.32600  1.000 24.49000 ? 89  GLU A OE2  1 
ATOM   735  N N    . GLY A 1 90  ? -24.90300 -15.26600 31.57100  1.000 11.15000 ? 90  GLY A N    1 
ATOM   736  C CA   . GLY A 1 90  ? -25.99200 -16.07300 31.06600  1.000 13.18000 ? 90  GLY A CA   1 
ATOM   737  C C    . GLY A 1 90  ? -25.48200 -16.93500 29.93500  1.000 13.14000 ? 90  GLY A C    1 
ATOM   738  O O    . GLY A 1 90  ? -24.49800 -17.67100 30.07600  1.000 15.06000 ? 90  GLY A O    1 
ATOM   739  N N    . ASP A 1 91  ? -26.14000 -16.84200 28.78800  1.000 13.97000 ? 91  ASP A N    1 
ATOM   740  C CA   . ASP A 1 91  ? -25.70900 -17.61200 27.63200  1.000 16.95000 ? 91  ASP A CA   1 
ATOM   741  C C    . ASP A 1 91  ? -24.74700 -16.84900 26.72400  1.000 12.85000 ? 91  ASP A C    1 
ATOM   742  O O    . ASP A 1 91  ? -24.36900 -17.38000 25.66900  1.000 18.33000 ? 91  ASP A O    1 
ATOM   743  C CB   . ASP A 1 91  ? -26.91900 -18.12100 26.84000  1.000 20.27000 ? 91  ASP A CB   1 
ATOM   744  C CG   . ASP A 1 91  ? -27.68100 -19.21300 27.57600  1.000 23.59000 ? 91  ASP A CG   1 
ATOM   745  O OD1  . ASP A 1 91  ? -27.03800 -20.05400 28.24700  1.000 25.93000 ? 91  ASP A OD1  1 
ATOM   746  O OD2  . ASP A 1 91  ? -28.92700 -19.21700 27.48700  1.000 27.08000 ? 91  ASP A OD2  1 
ATOM   747  N N    . VAL A 1 92  ? -24.34000 -15.64200 27.09400  1.000 10.81000 ? 92  VAL A N    1 
ATOM   748  C CA   . VAL A 1 92  ? -23.42100 -14.84000 26.28700  1.000 11.00000 ? 92  VAL A CA   1 
ATOM   749  C C    . VAL A 1 92  ? -21.99600 -15.11300 26.74900  1.000 9.04000  ? 92  VAL A C    1 
ATOM   750  O O    . VAL A 1 92  ? -21.70700 -15.06100 27.95300  1.000 9.14000  ? 92  VAL A O    1 
ATOM   751  C CB   . VAL A 1 92  ? -23.75000 -13.34500 26.42500  1.000 10.22000 ? 92  VAL A CB   1 
ATOM   752  C CG1  . VAL A 1 92  ? -22.92400 -12.52300 25.43900  1.000 11.07000 ? 92  VAL A CG1  1 
ATOM   753  C CG2  . VAL A 1 92  ? -25.23600 -13.10500 26.21700  1.000 12.71000 ? 92  VAL A CG2  1 
ATOM   754  N N    . LEU A 1 93  ? -21.10000 -15.37600 25.80000  1.000 8.51000  ? 93  LEU A N    1 
ATOM   755  C CA   . LEU A 1 93  ? -19.67800 -15.51400 26.10500  1.000 8.15000  ? 93  LEU A CA   1 
ATOM   756  C C    . LEU A 1 93  ? -19.02200 -14.15200 25.91400  1.000 8.05000  ? 93  LEU A C    1 
ATOM   757  O O    . LEU A 1 93  ? -19.11900 -13.56900 24.82900  1.000 9.04000  ? 93  LEU A O    1 
ATOM   758  C CB   . LEU A 1 93  ? -19.04200 -16.56000 25.19300  1.000 8.88000  ? 93  LEU A CB   1 
ATOM   759  C CG   . LEU A 1 93  ? -17.64400 -17.04500 25.58300  1.000 8.86000  ? 93  LEU A CG   1 
ATOM   760  C CD1  . LEU A 1 93  ? -17.68300 -17.80700 26.89700  1.000 9.98000  ? 93  LEU A CD1  1 
ATOM   761  C CD2  . LEU A 1 93  ? -17.06400 -17.90900 24.46800  1.000 10.86000 ? 93  LEU A CD2  1 
ATOM   762  N N    . VAL A 1 94  ? -18.36000 -13.64600 26.95500  1.000 8.09000  ? 94  VAL A N    1 
ATOM   763  C CA   . VAL A 1 94  ? -17.86600 -12.27300 27.00900  1.000 8.12000  ? 94  VAL A CA   1 
ATOM   764  C C    . VAL A 1 94  ? -16.35100 -12.27400 27.21800  1.000 8.30000  ? 94  VAL A C    1 
ATOM   765  O O    . VAL A 1 94  ? -15.86200 -12.88300 28.17900  1.000 9.29000  ? 94  VAL A O    1 
ATOM   766  C CB   . VAL A 1 94  ? -18.55300 -11.50600 28.15600  1.000 9.05000  ? 94  VAL A CB   1 
ATOM   767  C CG1  . VAL A 1 94  ? -18.00200 -10.09300 28.24400  1.000 10.66000 ? 94  VAL A CG1  1 
ATOM   768  C CG2  . VAL A 1 94  ? -20.07600 -11.50600 27.98100  1.000 11.02000 ? 94  VAL A CG2  1 
ATOM   769  N N    . SER A 1 95  ? -15.61600 -11.55900 26.35600  1.000 8.19000  ? 95  SER A N    1 
ATOM   770  C CA   . SER A 1 95  ? -14.16600 -11.34300 26.51500  1.000 7.59000  ? 95  SER A CA   1 
ATOM   771  C C    . SER A 1 95  ? -13.91700 -9.86700  26.77800  1.000 8.31000  ? 95  SER A C    1 
ATOM   772  O O    . SER A 1 95  ? -14.39000 -9.00300  26.02800  1.000 8.97000  ? 95  SER A O    1 
ATOM   773  C CB   . SER A 1 95  ? -13.30600 -11.76600 25.27900  1.000 9.28000  ? 95  SER A CB   1 
ATOM   774  O OG   . SER A 1 95  ? -11.77500 -11.49200 25.26200  1.000 3.61000  ? 95  SER A OG   1 
ATOM   775  N N    . VAL A 1 96  ? -13.17300 -9.58200  27.83800  1.000 8.69000  ? 96  VAL A N    1 
ATOM   776  C CA   . VAL A 1 96  ? -12.63600 -8.25300  28.07600  1.000 9.83000  ? 96  VAL A CA   1 
ATOM   777  C C    . VAL A 1 96  ? -11.12200 -8.33600  27.96300  1.000 9.45000  ? 96  VAL A C    1 
ATOM   778  O O    . VAL A 1 96  ? -10.50000 -9.21000  28.57600  1.000 10.67000 ? 96  VAL A O    1 
ATOM   779  C CB   . VAL A 1 96  ? -13.05800 -7.71900  29.45500  1.000 10.39000 ? 96  VAL A CB   1 
ATOM   780  C CG1  . VAL A 1 96  ? -12.41700 -6.36400  29.70500  1.000 13.05000 ? 96  VAL A CG1  1 
ATOM   781  C CG2  . VAL A 1 96  ? -14.58000 -7.63600  29.54600  1.000 13.56000 ? 96  VAL A CG2  1 
ATOM   782  N N    . GLN A 1 97  ? -10.53500 -7.41700  27.20300  1.000 9.34000  ? 97  GLN A N    1 
ATOM   783  C CA   . GLN A 1 97  ? -9.08600  -7.31400  27.03400  1.000 9.75000  ? 97  GLN A CA   1 
ATOM   784  C C    . GLN A 1 97  ? -8.63900  -5.98900  27.64300  1.000 11.12000 ? 97  GLN A C    1 
ATOM   785  O O    . GLN A 1 97  ? -8.79200  -4.93300  27.02300  1.000 11.33000 ? 97  GLN A O    1 
ATOM   786  C CB   . GLN A 1 97  ? -8.72700  -7.40300  25.55500  1.000 11.23000 ? 97  GLN A CB   1 
ATOM   787  C CG   . GLN A 1 97  ? -8.93400  -8.79100  24.98900  1.000 11.06000 ? 97  GLN A CG   1 
ATOM   788  C CD   . GLN A 1 97  ? -8.97000  -8.78700  23.47300  1.000 11.35000 ? 97  GLN A CD   1 
ATOM   789  O OE1  . GLN A 1 97  ? -9.60000  -7.92500  22.85800  1.000 13.41000 ? 97  GLN A OE1  1 
ATOM   790  N NE2  . GLN A 1 97  ? -8.26800  -9.74000  22.85300  1.000 13.80000 ? 97  GLN A NE2  1 
ATOM   791  N N    . LYS A 1 98  ? -8.12200  -6.04500  28.87300  1.000 11.88000 ? 98  LYS A N    1 
ATOM   792  C CA   . LYS A 1 98  ? -7.66100  -4.84700  29.56600  1.000 11.51000 ? 98  LYS A CA   1 
ATOM   793  C C    . LYS A 1 98  ? -6.30500  -4.40800  29.03000  1.000 12.27000 ? 98  LYS A C    1 
ATOM   794  O O    . LYS A 1 98  ? -5.38900  -5.22300  28.87800  1.000 13.10000 ? 98  LYS A O    1 
ATOM   795  C CB   . LYS A 1 98  ? -7.53500  -5.12100  31.06000  1.000 12.83000 ? 98  LYS A CB   1 
ATOM   796  C CG   . LYS A 1 98  ? -8.84300  -5.43200  31.75200  1.000 18.28000 ? 98  LYS A CG   1 
ATOM   797  C CD   . LYS A 1 98  ? -8.62700  -5.54900  33.25200  1.000 20.93000 ? 98  LYS A CD   1 
ATOM   798  C CE   . LYS A 1 98  ? -9.93200  -5.77000  33.98400  1.000 29.33000 ? 98  LYS A CE   1 
ATOM   799  N NZ   . LYS A 1 98  ? -9.72200  -5.75500  35.45600  1.000 29.54000 ? 98  LYS A NZ   1 
ATOM   800  N N    . GLY A 1 99  ? -6.17600  -3.11300  28.77000  1.000 11.67000 ? 99  GLY A N    1 
ATOM   801  C CA   . GLY A 1 99  ? -4.93800  -2.58600  28.21400  1.000 13.07000 ? 99  GLY A CA   1 
ATOM   802  C C    . GLY A 1 99  ? -5.12800  -1.16900  27.72300  1.000 12.88000 ? 99  GLY A C    1 
ATOM   803  O O    . GLY A 1 99  ? -5.96600  -0.42100  28.23400  1.000 14.21000 ? 99  GLY A O    1 
ATOM   804  N N    . GLU A 1 100 ? -4.36200  -0.81700  26.68900  1.000 12.82000 ? 100 GLU A N    1 
ATOM   805  C CA   . GLU A 1 100 ? -4.34600  0.56500   26.22000  1.000 14.82000 ? 100 GLU A CA   1 
ATOM   806  C C    . GLU A 1 100 ? -5.70900  1.00100   25.68500  1.000 13.45000 ? 100 GLU A C    1 
ATOM   807  O O    . GLU A 1 100 ? -6.19100  2.09500   26.00000  1.000 16.14000 ? 100 GLU A O    1 
ATOM   808  C CB   . GLU A 1 100 ? -3.26900  0.74000   25.15100  1.000 15.52000 ? 100 GLU A CB   1 
ATOM   809  C CG   . GLU A 1 100 ? -3.16800  2.16000   24.61700  1.000 18.49000 ? 100 GLU A CG   1 
ATOM   810  C CD   . GLU A 1 100 ? -2.87600  3.17200   25.71500  1.000 19.52000 ? 100 GLU A CD   1 
ATOM   811  O OE1  . GLU A 1 100 ? -2.17800  2.80700   26.68600  1.000 23.60000 ? 100 GLU A OE1  1 
ATOM   812  O OE2  . GLU A 1 100 ? -3.33500  4.32800   25.60400  1.000 21.03000 ? 100 GLU A OE2  1 
ATOM   813  N N    . LYS A 1 101 ? -6.32800  0.17800   24.84200  1.000 13.90000 ? 101 LYS A N    1 
ATOM   814  C CA   . LYS A 1 101 ? -7.60900  0.52900   24.24300  1.000 15.17000 ? 101 LYS A CA   1 
ATOM   815  C C    . LYS A 1 101 ? -8.74400  0.34600   25.24400  1.000 15.33000 ? 101 LYS A C    1 
ATOM   816  O O    . LYS A 1 101 ? -8.80300  -0.64600  25.97000  1.000 15.64000 ? 101 LYS A O    1 
ATOM   817  C CB   . LYS A 1 101 ? -7.85900  -0.34600  23.01400  1.000 15.09000 ? 101 LYS A CB   1 
ATOM   818  C CG   . LYS A 1 101 ? -6.83000  -0.17100  21.91100  1.000 16.14000 ? 101 LYS A CG   1 
ATOM   819  C CD   . LYS A 1 101 ? -6.92300  1.21800   21.28100  1.000 16.00000 ? 101 LYS A CD   1 
ATOM   820  C CE   . LYS A 1 101 ? -5.85900  1.42100   20.20000  1.000 16.87000 ? 101 LYS A CE   1 
ATOM   821  N NZ   . LYS A 1 101 ? -6.12400  2.60800   19.32000  1.000 16.70000 ? 101 LYS A NZ   1 
ATOM   822  N N    . GLU A 1 102 ? -9.65900  1.31300   25.27000  1.000 18.56000 ? 102 GLU A N    1 
ATOM   823  C CA   . GLU A 1 102 ? -10.85300 1.20500   26.09300  1.000 19.77000 ? 102 GLU A CA   1 
ATOM   824  C C    . GLU A 1 102 ? -11.89500 0.34200   25.39500  1.000 14.10000 ? 102 GLU A C    1 
ATOM   825  O O    . GLU A 1 102 ? -11.90500 0.22000   24.16700  1.000 14.65000 ? 102 GLU A O    1 
ATOM   826  C CB   . GLU A 1 102 ? -11.45500 2.59000   26.32900  1.000 22.31000 ? 102 GLU A CB   1 
ATOM   827  C CG   . GLU A 1 102 ? -10.60100 3.51700   27.16600  1.000 25.57000 ? 102 GLU A CG   1 
ATOM   828  C CD   . GLU A 1 102 ? -11.43000 4.56900   27.87600  1.000 33.71000 ? 102 GLU A CD   1 
ATOM   829  O OE1  . GLU A 1 102 ? -12.35700 5.12400   27.24300  1.000 34.95000 ? 102 GLU A OE1  1 
ATOM   830  O OE2  . GLU A 1 102 ? -11.16300 4.83100   29.06800  1.000 41.16000 ? 102 GLU A OE2  1 
ATOM   831  N N    . ASN A 1 103 ? -12.77700 -0.25400  26.19900  1.000 16.44000 ? 103 ASN A N    1 
ATOM   832  C CA   . ASN A 1 103 ? -13.92400 -1.01100  25.69400  1.000 15.05000 ? 103 ASN A CA   1 
ATOM   833  C C    . ASN A 1 103 ? -13.50300 -2.08200  24.69500  1.000 13.59000 ? 103 ASN A C    1 
ATOM   834  O O    . ASN A 1 103 ? -14.17400 -2.31300  23.68600  1.000 13.16000 ? 103 ASN A O    1 
ATOM   835  C CB   . ASN A 1 103 ? -14.98400 -0.08700  25.09400  1.000 15.85000 ? 103 ASN A CB   1 
ATOM   836  C CG   . ASN A 1 103 ? -16.29800 -0.79600  24.82600  1.000 22.77000 ? 103 ASN A CG   1 
ATOM   837  O OD1  . ASN A 1 103 ? -16.94800 -0.55700  23.80600  1.000 27.27000 ? 103 ASN A OD1  1 
ATOM   838  N ND2  . ASN A 1 103 ? -16.69600 -1.67500  25.73900  1.000 22.32000 ? 103 ASN A ND2  1 
ATOM   839  N N    . ARG A 1 104 ? -12.38000 -2.74300  24.97200  1.000 11.22000 ? 104 ARG A N    1 
ATOM   840  C CA   . ARG A 1 104 ? -11.81200 -3.70500  24.04000  1.000 9.72000  ? 104 ARG A CA   1 
ATOM   841  C C    . ARG A 1 104 ? -12.21500 -5.12200  24.43000  1.000 9.36000  ? 104 ARG A C    1 
ATOM   842  O O    . ARG A 1 104 ? -12.02300 -5.53700  25.57800  1.000 9.71000  ? 104 ARG A O    1 
ATOM   843  C CB   . ARG A 1 104 ? -10.29000 -3.59000  23.99100  1.000 10.64000 ? 104 ARG A CB   1 
ATOM   844  C CG   . ARG A 1 104 ? -9.68800  -4.51400  22.96700  1.000 10.29000 ? 104 ARG A CG   1 
ATOM   845  C CD   . ARG A 1 104 ? -8.17200  -4.51600  22.98300  1.000 10.61000 ? 104 ARG A CD   1 
ATOM   846  N NE   . ARG A 1 104 ? -7.70100  -5.43000  21.94500  1.000 11.51000 ? 104 ARG A NE   1 
ATOM   847  C CZ   . ARG A 1 104 ? -6.56200  -5.31200  21.26600  1.000 10.47000 ? 104 ARG A CZ   1 
ATOM   848  N NH1  . ARG A 1 104 ? -5.72800  -4.31300  21.52400  1.000 10.60000 ? 104 ARG A NH1  1 
ATOM   849  N NH2  . ARG A 1 104 ? -6.29000  -6.17900  20.29500  1.000 11.05000 ? 104 ARG A NH2  1 
ATOM   850  N N    . GLY A 1 105 ? -12.72800 -5.87100  23.46000  1.000 9.73000  ? 105 GLY A N    1 
ATOM   851  C CA   . GLY A 1 105 ? -13.06500 -7.27000  23.66800  1.000 9.81000  ? 105 GLY A CA   1 
ATOM   852  C C    . GLY A 1 105 ? -14.08400 -7.72300  22.64300  1.000 8.86000  ? 105 GLY A C    1 
ATOM   853  O O    . GLY A 1 105 ? -14.12700 -7.20500  21.52400  1.000 9.46000  ? 105 GLY A O    1 
ATOM   854  N N    . TRP A 1 106 ? -14.87300 -8.72100  23.03300  1.000 8.74000  ? 106 TRP A N    1 
ATOM   855  C CA   . TRP A 1 106 ? -15.91300 -9.23300  22.15000  1.000 9.50000  ? 106 TRP A CA   1 
ATOM   856  C C    . TRP A 1 106 ? -16.96600 -9.94200  22.97300  1.000 9.35000  ? 106 TRP A C    1 
ATOM   857  O O    . TRP A 1 106 ? -16.75000 -10.27500 24.14300  1.000 9.16000  ? 106 TRP A O    1 
ATOM   858  C CB   . TRP A 1 106 ? -15.37900 -10.16100 21.04600  1.000 10.29000 ? 106 TRP A CB   1 
ATOM   859  C CG   . TRP A 1 106 ? -14.46400 -11.24900 21.48500  1.000 9.82000  ? 106 TRP A CG   1 
ATOM   860  C CD1  . TRP A 1 106 ? -13.11800 -11.26000 21.33400  1.000 11.07000 ? 106 TRP A CD1  1 
ATOM   861  C CD2  . TRP A 1 106 ? -14.80900 -12.51400 22.08900  1.000 9.46000  ? 106 TRP A CD2  1 
ATOM   862  N NE1  . TRP A 1 106 ? -12.59200 -12.42800 21.81100  1.000 11.26000 ? 106 TRP A NE1  1 
ATOM   863  C CE2  . TRP A 1 106 ? -13.60700 -13.21300 22.29200  1.000 9.90000  ? 106 TRP A CE2  1 
ATOM   864  C CE3  . TRP A 1 106 ? -16.00700 -13.10600 22.50600  1.000 9.44000  ? 106 TRP A CE3  1 
ATOM   865  C CZ2  . TRP A 1 106 ? -13.55700 -14.47700 22.88000  1.000 11.82000 ? 106 TRP A CZ2  1 
ATOM   866  C CZ3  . TRP A 1 106 ? -15.95300 -14.38000 23.10300  1.000 10.62000 ? 106 TRP A CZ3  1 
ATOM   867  C CH2  . TRP A 1 106 ? -14.73600 -15.04500 23.27000  1.000 12.08000 ? 106 TRP A CH2  1 
ATOM   868  N N    . LYS A 1 107 ? -18.11200 -10.16200 22.33500  1.000 9.27000  ? 107 LYS A N    1 
ATOM   869  C CA   . LYS A 1 107 ? -19.20500 -10.94500 22.88700  1.000 9.57000  ? 107 LYS A CA   1 
ATOM   870  C C    . LYS A 1 107 ? -19.73600 -11.86100 21.79700  1.000 8.76000  ? 107 LYS A C    1 
ATOM   871  O O    . LYS A 1 107 ? -19.85200 -11.46000 20.62300  1.000 9.86000  ? 107 LYS A O    1 
ATOM   872  C CB   . LYS A 1 107 ? -20.32700 -10.04700 23.41200  1.000 11.73000 ? 107 LYS A CB   1 
ATOM   873  C CG   . LYS A 1 107 ? -19.89200 -9.15700  24.56200  1.000 11.66000 ? 107 LYS A CG   1 
ATOM   874  C CD   . LYS A 1 107 ? -21.03500 -8.29700  25.07200  1.000 14.47000 ? 107 LYS A CD   1 
ATOM   875  C CE   . LYS A 1 107 ? -20.54400 -7.27800  26.08800  1.000 18.90000 ? 107 LYS A CE   1 
ATOM   876  N NZ   . LYS A 1 107 ? -21.66400 -6.45900  26.62000  1.000 20.97000 ? 107 LYS A NZ   1 
ATOM   877  N N    . LYS A 1 108 ? -20.06400 -13.08900 22.19100  1.000 9.59000  ? 108 LYS A N    1 
ATOM   878  C CA   . LYS A 1 108 ? -20.56500 -14.10800 21.28700  1.000 9.05000  ? 108 LYS A CA   1 
ATOM   879  C C    . LYS A 1 108 ? -21.90700 -14.62000 21.78100  1.000 8.78000  ? 108 LYS A C    1 
ATOM   880  O O    . LYS A 1 108 ? -22.03500 -15.03500 22.94500  1.000 9.75000  ? 108 LYS A O    1 
ATOM   881  C CB   . LYS A 1 108 ? -19.57200 -15.26000 21.23700  1.000 10.91000 ? 108 LYS A CB   1 
ATOM   882  C CG   . LYS A 1 108 ? -19.81100 -16.24800 20.13000  1.000 14.96000 ? 108 LYS A CG   1 
ATOM   883  C CD   . LYS A 1 108 ? -18.88900 -17.45800 20.27500  1.000 20.13000 ? 108 LYS A CD   1 
ATOM   884  C CE   . LYS A 1 108 ? -17.44400 -17.05400 20.54900  1.000 18.55000 ? 108 LYS A CE   1 
ATOM   885  N NZ   . LYS A 1 108 ? -16.63300 -16.75300 19.32300  1.000 18.76000 ? 108 LYS A NZ   1 
ATOM   886  N N    . TRP A 1 109 ? -22.89000 -14.62200 20.88600  1.000 9.21000  ? 109 TRP A N    1 
ATOM   887  C CA   . TRP A 1 109 ? -24.21400 -15.17800 21.12800  1.000 10.90000 ? 109 TRP A CA   1 
ATOM   888  C C    . TRP A 1 109 ? -24.37700 -16.33800 20.16600  1.000 11.76000 ? 109 TRP A C    1 
ATOM   889  O O    . TRP A 1 109 ? -24.29900 -16.15300 18.94700  1.000 15.40000 ? 109 TRP A O    1 
ATOM   890  C CB   . TRP A 1 109 ? -25.30100 -14.15400 20.81400  1.000 11.16000 ? 109 TRP A CB   1 
ATOM   891  C CG   . TRP A 1 109 ? -25.36700 -12.96100 21.69400  1.000 9.91000  ? 109 TRP A CG   1 
ATOM   892  C CD1  . TRP A 1 109 ? -26.24400 -12.76100 22.72700  1.000 11.31000 ? 109 TRP A CD1  1 
ATOM   893  C CD2  . TRP A 1 109 ? -24.58800 -11.76600 21.59600  1.000 9.91000  ? 109 TRP A CD2  1 
ATOM   894  N NE1  . TRP A 1 109 ? -26.05300 -11.52300 23.27800  1.000 12.53000 ? 109 TRP A NE1  1 
ATOM   895  C CE2  . TRP A 1 109 ? -25.04000 -10.89100 22.60800  1.000 12.34000 ? 109 TRP A CE2  1 
ATOM   896  C CE3  . TRP A 1 109 ? -23.55000 -11.34500 20.75500  1.000 10.59000 ? 109 TRP A CE3  1 
ATOM   897  C CZ2  . TRP A 1 109 ? -24.48900 -9.63700  22.80400  1.000 13.20000 ? 109 TRP A CZ2  1 
ATOM   898  C CZ3  . TRP A 1 109 ? -23.01000 -10.09300 20.95400  1.000 12.01000 ? 109 TRP A CZ3  1 
ATOM   899  C CH2  . TRP A 1 109 ? -23.48200 -9.25300  21.96500  1.000 13.88000 ? 109 TRP A CH2  1 
ATOM   900  N N    . ILE A 1 110 ? -24.58700 -17.53100 20.69600  1.000 15.79000 ? 110 ILE A N    1 
ATOM   901  C CA   . ILE A 1 110 ? -24.85400 -18.70400 19.88000  1.000 18.91000 ? 110 ILE A CA   1 
ATOM   902  C C    . ILE A 1 110 ? -26.35200 -18.94900 19.92100  1.000 22.54000 ? 110 ILE A C    1 
ATOM   903  O O    . ILE A 1 110 ? -26.93800 -19.09400 21.00100  1.000 22.30000 ? 110 ILE A O    1 
ATOM   904  C CB   . ILE A 1 110 ? -24.07900 -19.93300 20.38000  1.000 22.94000 ? 110 ILE A CB   1 
ATOM   905  C CG1  . ILE A 1 110 ? -22.57100 -19.72900 20.21400  1.000 24.38000 ? 110 ILE A CG1  1 
ATOM   906  C CG2  . ILE A 1 110 ? -24.54400 -21.17500 19.63800  1.000 26.61000 ? 110 ILE A CG2  1 
ATOM   907  C CD1  . ILE A 1 110 ? -21.79600 -19.71000 21.51500  1.000 26.03000 ? 110 ILE A CD1  1 
ATOM   908  N N    . GLU A 1 111 ? -26.97800 -18.97500 18.75200  0.640 19.10000 ? 111 GLU A N    1 
ATOM   909  C CA   . GLU A 1 111 ? -28.40200 -19.27000 18.62400  0.640 21.51000 ? 111 GLU A CA   1 
ATOM   910  C C    . GLU A 1 111 ? -28.50600 -20.40400 17.61200  0.640 21.90000 ? 111 GLU A C    1 
ATOM   911  O O    . GLU A 1 111 ? -28.58600 -20.17000 16.40300  0.640 19.33000 ? 111 GLU A O    1 
ATOM   912  C CB   . GLU A 1 111 ? -29.17700 -18.02300 18.20700  0.640 20.86000 ? 111 GLU A CB   1 
ATOM   913  C CG   . GLU A 1 111 ? -28.83200 -16.79700 19.05800  0.640 22.31000 ? 111 GLU A CG   1 
ATOM   914  C CD   . GLU A 1 111 ? -29.85600 -15.68600 18.95700  0.640 24.98000 ? 111 GLU A CD   1 
ATOM   915  O OE1  . GLU A 1 111 ? -29.93500 -14.85900 19.89200  0.640 24.93000 ? 111 GLU A OE1  1 
ATOM   916  O OE2  . GLU A 1 111 ? -30.58200 -15.63400 17.94400  0.640 26.80000 ? 111 GLU A OE2  1 
ATOM   917  N N    . GLY A 1 112 ? -28.47100 -21.63600 18.11400  1.000 27.94000 ? 112 GLY A N    1 
ATOM   918  C CA   . GLY A 1 112 ? -28.55000 -22.81100 17.27000  1.000 25.86000 ? 112 GLY A CA   1 
ATOM   919  C C    . GLY A 1 112 ? -27.53200 -22.83700 16.14800  1.000 27.52000 ? 112 GLY A C    1 
ATOM   920  O O    . GLY A 1 112 ? -26.35100 -23.12300 16.37400  1.000 30.44000 ? 112 GLY A O    1 
ATOM   921  N N    . ASP A 1 113 ? -27.99900 -22.53200 14.93400  1.000 28.91000 ? 113 ASP A N    1 
ATOM   922  C CA   . ASP A 1 113 ? -27.21100 -22.61200 13.70900  1.000 28.94000 ? 113 ASP A CA   1 
ATOM   923  C C    . ASP A 1 113 ? -26.32100 -21.39500 13.49400  1.000 23.24000 ? 113 ASP A C    1 
ATOM   924  O O    . ASP A 1 113 ? -25.42600 -21.43900 12.64100  1.000 19.80000 ? 113 ASP A O    1 
ATOM   925  C CB   . ASP A 1 113 ? -28.17200 -22.71500 12.51600  1.000 24.63000 ? 113 ASP A CB   1 
ATOM   926  C CG   . ASP A 1 113 ? -27.61700 -23.54700 11.38300  0.000 23.49000 ? 113 ASP A CG   1 
ATOM   927  O OD1  . ASP A 1 113 ? -27.64900 -24.79100 11.48700  0.000 23.60000 ? 113 ASP A OD1  1 
ATOM   928  O OD2  . ASP A 1 113 ? -27.16100 -22.95900 10.38100  0.000 22.96000 ? 113 ASP A OD2  1 
ATOM   929  N N    . LYS A 1 114 ? -26.55800 -20.31000 14.22400  1.000 21.45000 ? 114 LYS A N    1 
ATOM   930  C CA   . LYS A 1 114 ? -25.95300 -19.02000 13.92700  1.000 17.00000 ? 114 LYS A CA   1 
ATOM   931  C C    . LYS A 1 114 ? -25.13600 -18.53400 15.11300  1.000 14.05000 ? 114 LYS A C    1 
ATOM   932  O O    . LYS A 1 114 ? -25.51400 -18.73700 16.27500  1.000 17.97000 ? 114 LYS A O    1 
ATOM   933  C CB   . LYS A 1 114 ? -27.01400 -17.97400 13.57000  1.000 20.60000 ? 114 LYS A CB   1 
ATOM   934  C CG   . LYS A 1 114 ? -27.40800 -17.93300 12.09700  1.000 24.25000 ? 114 LYS A CG   1 
ATOM   935  C CD   . LYS A 1 114 ? -27.82000 -16.52400 11.69100  1.000 27.11000 ? 114 LYS A CD   1 
ATOM   936  C CE   . LYS A 1 114 ? -28.91200 -16.53000 10.63200  1.000 30.27000 ? 114 LYS A CE   1 
ATOM   937  N NZ   . LYS A 1 114 ? -28.42200 -17.05600 9.32900   1.000 31.70000 ? 114 LYS A NZ   1 
ATOM   938  N N    . LEU A 1 115 ? -24.01200 -17.90000 14.80700  1.000 12.04000 ? 115 LEU A N    1 
ATOM   939  C CA   . LEU A 1 115 ? -23.12100 -17.30800 15.78900  1.000 11.40000 ? 115 LEU A CA   1 
ATOM   940  C C    . LEU A 1 115 ? -23.04700 -15.82100 15.48100  1.000 11.39000 ? 115 LEU A C    1 
ATOM   941  O O    . LEU A 1 115 ? -22.64900 -15.43200 14.37300  1.000 11.76000 ? 115 LEU A O    1 
ATOM   942  C CB   . LEU A 1 115 ? -21.73600 -17.95100 15.68300  1.000 12.15000 ? 115 LEU A CB   1 
ATOM   943  C CG   . LEU A 1 115 ? -20.68300 -17.61400 16.73900  1.000 12.66000 ? 115 LEU A CG   1 
ATOM   944  C CD1  . LEU A 1 115 ? -19.63700 -18.72400 16.82300  1.000 15.39000 ? 115 LEU A CD1  1 
ATOM   945  C CD2  . LEU A 1 115 ? -20.02600 -16.29200 16.42200  1.000 14.53000 ? 115 LEU A CD2  1 
ATOM   946  N N    . TYR A 1 116 ? -23.45100 -15.00000 16.44400  1.000 10.00000 ? 116 TYR A N    1 
ATOM   947  C CA   . TYR A 1 116 ? -23.33400 -13.55200 16.36000  1.000 10.24000 ? 116 TYR A CA   1 
ATOM   948  C C    . TYR A 1 116 ? -22.13900 -13.12900 17.19900  1.000 9.97000  ? 116 TYR A C    1 
ATOM   949  O O    . TYR A 1 116 ? -22.03900 -13.48700 18.38200  1.000 10.76000 ? 116 TYR A O    1 
ATOM   950  C CB   . TYR A 1 116 ? -24.59200 -12.86900 16.89600  1.000 11.74000 ? 116 TYR A CB   1 
ATOM   951  C CG   . TYR A 1 116 ? -25.83100 -13.19500 16.10900  1.000 11.07000 ? 116 TYR A CG   1 
ATOM   952  C CD1  . TYR A 1 116 ? -26.52800 -14.37400 16.33200  1.000 13.81000 ? 116 TYR A CD1  1 
ATOM   953  C CD2  . TYR A 1 116 ? -26.30900 -12.32900 15.14200  1.000 12.18000 ? 116 TYR A CD2  1 
ATOM   954  C CE1  . TYR A 1 116 ? -27.65900 -14.68100 15.59900  1.000 14.96000 ? 116 TYR A CE1  1 
ATOM   955  C CE2  . TYR A 1 116 ? -27.44200 -12.63100 14.40600  1.000 13.74000 ? 116 TYR A CE2  1 
ATOM   956  C CZ   . TYR A 1 116 ? -28.10700 -13.80500 14.64700  1.000 15.56000 ? 116 TYR A CZ   1 
ATOM   957  O OH   . TYR A 1 116 ? -29.23800 -14.10600 13.91600  1.000 19.24000 ? 116 TYR A OH   1 
ATOM   958  N N    . LEU A 1 117 ? -21.23600 -12.38100 16.59100  1.000 10.14000 ? 117 LEU A N    1 
ATOM   959  C CA   . LEU A 1 117 ? -20.02000 -11.93500 17.25000  1.000 10.53000 ? 117 LEU A CA   1 
ATOM   960  C C    . LEU A 1 117 ? -19.96100 -10.42300 17.14300  1.000 10.97000 ? 117 LEU A C    1 
ATOM   961  O O    . LEU A 1 117 ? -20.06900 -9.87700  16.03700  1.000 12.30000 ? 117 LEU A O    1 
ATOM   962  C CB   . LEU A 1 117 ? -18.80900 -12.55300 16.55500  1.000 11.53000 ? 117 LEU A CB   1 
ATOM   963  C CG   . LEU A 1 117 ? -17.42300 -12.21000 17.09300  1.000 13.84000 ? 117 LEU A CG   1 
ATOM   964  C CD1  . LEU A 1 117 ? -17.23400 -12.69600 18.52100  1.000 12.59000 ? 117 LEU A CD1  1 
ATOM   965  C CD2  . LEU A 1 117 ? -16.36800 -12.79500 16.16500  1.000 14.21000 ? 117 LEU A CD2  1 
ATOM   966  N N    . GLU A 1 118 ? -19.79700 -9.74300  18.27500  1.000 9.37000  ? 118 GLU A N    1 
ATOM   967  C CA   . GLU A 1 118 ? -19.60800 -8.29600  18.28400  1.000 9.75000  ? 118 GLU A CA   1 
ATOM   968  C C    . GLU A 1 118 ? -18.23600 -7.99600  18.86100  1.000 9.41000  ? 118 GLU A C    1 
ATOM   969  O O    . GLU A 1 118 ? -17.98100 -8.27800  20.03600  1.000 10.26000 ? 118 GLU A O    1 
ATOM   970  C CB   . GLU A 1 118 ? -20.71500 -7.58100  19.06100  1.000 11.14000 ? 118 GLU A CB   1 
ATOM   971  C CG   . GLU A 1 118 ? -22.07400 -7.65400  18.34900  1.000 12.21000 ? 118 GLU A CG   1 
ATOM   972  C CD   . GLU A 1 118 ? -23.15000 -6.75800  18.94700  1.000 13.99000 ? 118 GLU A CD   1 
ATOM   973  O OE1  . GLU A 1 118 ? -22.85400 -5.92600  19.83000  1.000 15.65000 ? 118 GLU A OE1  1 
ATOM   974  O OE2  . GLU A 1 118 ? -24.31900 -6.90400  18.52000  1.000 17.53000 ? 118 GLU A OE2  1 
ATOM   975  N N    . LEU A 1 119 ? -17.36500 -7.43500  18.03400  1.000 9.40000  ? 119 LEU A N    1 
ATOM   976  C CA   . LEU A 1 119 ? -16.01800 -7.04500  18.42200  1.000 9.61000  ? 119 LEU A CA   1 
ATOM   977  C C    . LEU A 1 119 ? -16.01000 -5.55500  18.71300  1.000 9.23000  ? 119 LEU A C    1 
ATOM   978  O O    . LEU A 1 119 ? -16.53600 -4.76900  17.92000  1.000 10.76000 ? 119 LEU A O    1 
ATOM   979  C CB   . LEU A 1 119 ? -15.04500 -7.32100  17.27900  1.000 11.67000 ? 119 LEU A CB   1 
ATOM   980  C CG   . LEU A 1 119 ? -14.97300 -8.73200  16.70600  1.000 12.18000 ? 119 LEU A CG   1 
ATOM   981  C CD1  . LEU A 1 119 ? -14.49500 -8.66100  15.26600  1.000 17.53000 ? 119 LEU A CD1  1 
ATOM   982  C CD2  . LEU A 1 119 ? -14.00700 -9.57100  17.49900  1.000 18.33000 ? 119 LEU A CD2  1 
ATOM   983  N N    . THR A 1 120 ? -15.41900 -5.16400  19.83200  1.000 9.25000  ? 120 THR A N    1 
ATOM   984  C CA   . THR A 1 120 ? -15.40800 -3.76500  20.22700  1.000 10.31000 ? 120 THR A CA   1 
ATOM   985  C C    . THR A 1 120 ? -13.99100 -3.25900  20.44500  1.000 9.66000  ? 120 THR A C    1 
ATOM   986  O O    . THR A 1 120 ? -13.10800 -3.99000  20.90600  1.000 10.13000 ? 120 THR A O    1 
ATOM   987  C CB   . THR A 1 120 ? -16.22700 -3.53500  21.51300  1.000 11.15000 ? 120 THR A CB   1 
ATOM   988  O OG1  . THR A 1 120 ? -15.67800 -4.30700  22.59200  1.000 11.94000 ? 120 THR A OG1  1 
ATOM   989  C CG2  . THR A 1 120 ? -17.68600 -3.90700  21.30100  1.000 12.12000 ? 120 THR A CG2  1 
ATOM   990  N N    . CYS A 1 121 ? -13.79700 -1.98400  20.10800  1.000 10.27000 ? 121 CYS A N    1 
ATOM   991  C CA   . CYS A 1 121 ? -12.57700 -1.27100  20.45600  1.000 11.40000 ? 121 CYS A CA   1 
ATOM   992  C C    . CYS A 1 121 ? -12.90900 0.21100   20.44400  1.000 12.99000 ? 121 CYS A C    1 
ATOM   993  O O    . CYS A 1 121 ? -13.43700 0.71100   19.45200  1.000 12.63000 ? 121 CYS A O    1 
ATOM   994  C CB   . CYS A 1 121 ? -11.47900 -1.56300  19.43500  1.000 10.58000 ? 121 CYS A CB   1 
ATOM   995  S SG   . CYS A 1 121 ? -9.87900  -0.77000  19.85500  1.000 13.51000 ? 121 CYS A SG   1 
ATOM   996  N N    . GLY A 1 122 ? -12.62700 0.89600   21.55200  1.000 16.27000 ? 122 GLY A N    1 
ATOM   997  C CA   . GLY A 1 122 ? -12.96000 2.31300   21.62100  1.000 17.47000 ? 122 GLY A CA   1 
ATOM   998  C C    . GLY A 1 122 ? -14.44900 2.51300   21.42400  1.000 17.24000 ? 122 GLY A C    1 
ATOM   999  O O    . GLY A 1 122 ? -15.27400 1.86900   22.07900  1.000 17.71000 ? 122 GLY A O    1 
ATOM   1000 N N    . ASP A 1 123 ? -14.80500 3.40200   20.49500  1.000 16.30000 ? 123 ASP A N    1 
ATOM   1001 C CA   . ASP A 1 123 ? -16.20100 3.68200   20.18900  1.000 15.68000 ? 123 ASP A CA   1 
ATOM   1002 C C    . ASP A 1 123 ? -16.72700 2.89100   18.99800  1.000 16.36000 ? 123 ASP A C    1 
ATOM   1003 O O    . ASP A 1 123 ? -17.81000 3.20500   18.48800  1.000 19.91000 ? 123 ASP A O    1 
ATOM   1004 C CB   . ASP A 1 123 ? -16.43700 5.18800   20.00300  1.000 18.79000 ? 123 ASP A CB   1 
ATOM   1005 C CG   . ASP A 1 123 ? -15.64000 5.78100   18.85200  1.000 22.68000 ? 123 ASP A CG   1 
ATOM   1006 O OD1  . ASP A 1 123 ? -15.07100 5.02500   18.03800  1.000 23.12000 ? 123 ASP A OD1  1 
ATOM   1007 O OD2  . ASP A 1 123 ? -15.59100 7.02700   18.75400  1.000 27.16000 ? 123 ASP A OD2  1 
ATOM   1008 N N    . GLN A 1 124 ? -16.01100 1.85600   18.56700  1.000 13.46000 ? 124 GLN A N    1 
ATOM   1009 C CA   . GLN A 1 124 ? -16.36000 1.09800   17.37900  1.000 11.68000 ? 124 GLN A CA   1 
ATOM   1010 C C    . GLN A 1 124 ? -16.83500 -0.29800  17.75600  1.000 12.27000 ? 124 GLN A C    1 
ATOM   1011 O O    . GLN A 1 124 ? -16.27400 -0.94100  18.65200  1.000 12.96000 ? 124 GLN A O    1 
ATOM   1012 C CB   . GLN A 1 124 ? -15.14700 0.97900   16.45800  1.000 12.45000 ? 124 GLN A CB   1 
ATOM   1013 C CG   . GLN A 1 124 ? -14.63900 2.31500   15.95900  1.000 14.56000 ? 124 GLN A CG   1 
ATOM   1014 C CD   . GLN A 1 124 ? -15.66000 3.01000   15.09900  1.000 14.98000 ? 124 GLN A CD   1 
ATOM   1015 O OE1  . GLN A 1 124 ? -16.13800 2.44600   14.12100  1.000 15.07000 ? 124 GLN A OE1  1 
ATOM   1016 N NE2  . GLN A 1 124 ? -16.00900 4.24400   15.46000  1.000 20.38000 ? 124 GLN A NE2  1 
ATOM   1017 N N    . VAL A 1 125 ? -17.87000 -0.76100  17.06300  1.000 11.19000 ? 125 VAL A N    1 
ATOM   1018 C CA   . VAL A 1 125 ? -18.36700 -2.12700  17.16300  1.000 11.59000 ? 125 VAL A CA   1 
ATOM   1019 C C    . VAL A 1 125 ? -18.41600 -2.70600  15.76100  1.000 10.84000 ? 125 VAL A C    1 
ATOM   1020 O O    . VAL A 1 125 ? -18.96500 -2.07900  14.84600  1.000 11.90000 ? 125 VAL A O    1 
ATOM   1021 C CB   . VAL A 1 125 ? -19.76900 -2.19100  17.80200  1.000 13.97000 ? 125 VAL A CB   1 
ATOM   1022 C CG1  . VAL A 1 125 ? -20.18700 -3.63600  18.02300  1.000 16.17000 ? 125 VAL A CG1  1 
ATOM   1023 C CG2  . VAL A 1 125 ? -19.81500 -1.40700  19.10600  1.000 18.21000 ? 125 VAL A CG2  1 
ATOM   1024 N N    . CYS A 1 126 ? -17.85300 -3.89700  15.59500  1.000 11.00000 ? 126 CYS A N    1 
ATOM   1025 C CA   . CYS A 1 126 ? -17.98100 -4.66900  14.36800  1.000 10.89000 ? 126 CYS A CA   1 
ATOM   1026 C C    . CYS A 1 126 ? -18.91400 -5.83700  14.65200  1.000 10.15000 ? 126 CYS A C    1 
ATOM   1027 O O    . CYS A 1 126 ? -18.73200 -6.54700  15.65000  1.000 10.39000 ? 126 CYS A O    1 
ATOM   1028 C CB   . CYS A 1 126 ? -16.61000 -5.17700  13.92100  1.000 11.70000 ? 126 CYS A CB   1 
ATOM   1029 S SG   . CYS A 1 126 ? -16.64400 -6.45600  12.64000  1.000 11.00000 ? 126 CYS A SG   1 
ATOM   1030 N N    . ARG A 1 127 ? -19.94200 -5.99900  13.81900  1.000 9.71000  ? 127 ARG A N    1 
ATOM   1031 C CA   . ARG A 1 127 ? -20.95800 -7.02700  14.01200  1.000 10.53000 ? 127 ARG A CA   1 
ATOM   1032 C C    . ARG A 1 127 ? -20.80600 -8.08200  12.92900  1.000 10.32000 ? 127 ARG A C    1 
ATOM   1033 O O    . ARG A 1 127 ? -20.92300 -7.77400  11.73400  1.000 10.92000 ? 127 ARG A O    1 
ATOM   1034 C CB   . ARG A 1 127 ? -22.36300 -6.42800  13.96800  1.000 12.32000 ? 127 ARG A CB   1 
ATOM   1035 C CG   . ARG A 1 127 ? -22.61700 -5.35900  15.02300  1.000 13.83000 ? 127 ARG A CG   1 
ATOM   1036 C CD   . ARG A 1 127 ? -23.99600 -4.72300  14.86300  1.000 21.28000 ? 127 ARG A CD   1 
ATOM   1037 N NE   . ARG A 1 127 ? -24.26400 -4.34100  13.48100  1.000 30.02000 ? 127 ARG A NE   1 
ATOM   1038 C CZ   . ARG A 1 127 ? -23.85500 -3.20300  12.92900  1.000 26.27000 ? 127 ARG A CZ   1 
ATOM   1039 N NH1  . ARG A 1 127 ? -24.14000 -2.93500  11.66200  1.000 30.90000 ? 127 ARG A NH1  1 
ATOM   1040 N NH2  . ARG A 1 127 ? -23.16200 -2.33100  13.64800  1.000 31.36000 ? 127 ARG A NH2  1 
ATOM   1041 N N    . GLN A 1 128 ? -20.55300 -9.31600  13.33900  1.000 10.77000 ? 128 GLN A N    1 
ATOM   1042 C CA   . GLN A 1 128 ? -20.36800 -10.42400 12.42300  1.000 11.10000 ? 128 GLN A CA   1 
ATOM   1043 C C    . GLN A 1 128 ? -21.41600 -11.48600 12.70400  1.000 10.37000 ? 128 GLN A C    1 
ATOM   1044 O O    . GLN A 1 128 ? -21.83400 -11.68200 13.85000  1.000 11.17000 ? 128 GLN A O    1 
ATOM   1045 C CB   . GLN A 1 128 ? -18.96200 -11.00700 12.56200  1.000 12.03000 ? 128 GLN A CB   1 
ATOM   1046 C CG   . GLN A 1 128 ? -17.89200 -9.99100  12.19400  1.000 12.75000 ? 128 GLN A CG   1 
ATOM   1047 C CD   . GLN A 1 128 ? -16.49300 -10.54800 12.23400  1.000 12.68000 ? 128 GLN A CD   1 
ATOM   1048 O OE1  . GLN A 1 128 ? -16.25700 -11.63100 12.76300  1.000 15.64000 ? 128 GLN A OE1  1 
ATOM   1049 N NE2  . GLN A 1 128 ? -15.54600 -9.80900  11.66400  1.000 13.49000 ? 128 GLN A NE2  1 
ATOM   1050 N N    . VAL A 1 129 ? -21.81800 -12.19000 11.65100  1.000 10.78000 ? 129 VAL A N    1 
ATOM   1051 C CA   . VAL A 1 129 ? -22.71900 -13.32800 11.76000  1.000 11.03000 ? 129 VAL A CA   1 
ATOM   1052 C C    . VAL A 1 129 ? -22.09600 -14.47600 10.98700  1.000 10.77000 ? 129 VAL A C    1 
ATOM   1053 O O    . VAL A 1 129 ? -21.63100 -14.28800 9.85600   1.000 11.74000 ? 129 VAL A O    1 
ATOM   1054 C CB   . VAL A 1 129 ? -24.12200 -13.01800 11.20500  1.000 12.48000 ? 129 VAL A CB   1 
ATOM   1055 C CG1  . VAL A 1 129 ? -25.04400 -14.21900 11.41300  1.000 14.39000 ? 129 VAL A CG1  1 
ATOM   1056 C CG2  . VAL A 1 129 ? -24.71000 -11.77000 11.86300  1.000 13.27000 ? 129 VAL A CG2  1 
ATOM   1057 N N    . PHE A 1 130 ? -22.08200 -15.65600 11.59600  1.000 11.71000 ? 130 PHE A N    1 
ATOM   1058 C CA   . PHE A 1 130 ? -21.58200 -16.87700 10.98800  1.000 11.45000 ? 130 PHE A CA   1 
ATOM   1059 C C    . PHE A 1 130 ? -22.66100 -17.94900 11.06000  1.000 11.94000 ? 130 PHE A C    1 
ATOM   1060 O O    . PHE A 1 130 ? -23.51600 -17.94800 11.95900  1.000 11.88000 ? 130 PHE A O    1 
ATOM   1061 C CB   . PHE A 1 130 ? -20.35500 -17.43200 11.73100  1.000 14.13000 ? 130 PHE A CB   1 
ATOM   1062 C CG   . PHE A 1 130 ? -19.16500 -16.51500 11.74500  1.000 11.22000 ? 130 PHE A CG   1 
ATOM   1063 C CD1  . PHE A 1 130 ? -19.08100 -15.46300 12.64300  1.000 12.40000 ? 130 PHE A CD1  1 
ATOM   1064 C CD2  . PHE A 1 130 ? -18.09600 -16.74700 10.90300  1.000 13.00000 ? 130 PHE A CD2  1 
ATOM   1065 C CE1  . PHE A 1 130 ? -17.96800 -14.63600 12.66600  1.000 13.73000 ? 130 PHE A CE1  1 
ATOM   1066 C CE2  . PHE A 1 130 ? -16.99000 -15.92200 10.91800  1.000 13.67000 ? 130 PHE A CE2  1 
ATOM   1067 C CZ   . PHE A 1 130 ? -16.92100 -14.87600 11.80900  1.000 15.07000 ? 130 PHE A CZ   1 
ATOM   1068 N N    . LYS A 1 131 ? -22.61200 -18.87300 10.11000  1.000 13.89000 ? 131 LYS A N    1 
ATOM   1069 C CA   . LYS A 1 131 ? -23.45300 -20.05500 10.13000  1.000 15.18000 ? 131 LYS A CA   1 
ATOM   1070 C C    . LYS A 1 131 ? -22.56500 -21.28500 10.21500  1.000 14.08000 ? 131 LYS A C    1 
ATOM   1071 O O    . LYS A 1 131 ? -21.51400 -21.35700 9.57000   1.000 14.88000 ? 131 LYS A O    1 
ATOM   1072 C CB   . LYS A 1 131 ? -24.34500 -20.11700 8.88900   1.000 18.70000 ? 131 LYS A CB   1 
ATOM   1073 C CG   . LYS A 1 131 ? -25.44100 -21.15700 8.98600   1.000 21.61000 ? 131 LYS A CG   1 
ATOM   1074 C CD   . LYS A 1 131 ? -26.30600 -21.16800 7.74000   1.000 24.77000 ? 131 LYS A CD   1 
ATOM   1075 C CE   . LYS A 1 131 ? -25.46900 -21.45900 6.50400   1.000 29.64000 ? 131 LYS A CE   1 
ATOM   1076 N NZ   . LYS A 1 131 ? -24.81900 -22.79800 6.56600   1.000 31.89000 ? 131 LYS A NZ   1 
ATOM   1077 N N    . LYS A 1 132 ? -22.97800 -22.23500 11.04200  1.000 15.66000 ? 132 LYS A N    1 
ATOM   1078 C CA   . LYS A 1 132 ? -22.19700 -23.44300 11.20500  1.000 15.86000 ? 132 LYS A CA   1 
ATOM   1079 C C    . LYS A 1 132 ? -22.23700 -24.23000 9.90600   1.000 15.68000 ? 132 LYS A C    1 
ATOM   1080 O O    . LYS A 1 132 ? -23.31000 -24.43800 9.33400   1.000 18.10000 ? 132 LYS A O    1 
ATOM   1081 C CB   . LYS A 1 132 ? -22.77700 -24.27300 12.34300  1.000 18.90000 ? 132 LYS A CB   1 
ATOM   1082 C CG   . LYS A 1 132 ? -21.86200 -25.36200 12.81100  1.000 14.61000 ? 132 LYS A CG   1 
ATOM   1083 C CD   . LYS A 1 132 ? -22.49500 -26.10800 13.95200  1.000 17.23000 ? 132 LYS A CD   1 
ATOM   1084 C CE   . LYS A 1 132 ? -21.63900 -27.26000 14.40300  1.000 18.36000 ? 132 LYS A CE   1 
ATOM   1085 N NZ   . LYS A 1 132 ? -22.24800 -27.81500 15.63500  1.000 15.57000 ? 132 LYS A NZ   1 
ATOM   1086 N N    . LYS A 1 133 ? -21.07200 -24.63100 9.42600   1.000 15.74000 ? 133 LYS A N    1 
ATOM   1087 C CA   . LYS A 1 133 ? -20.98200 -25.39200 8.18500   1.000 17.62000 ? 133 LYS A CA   1 
ATOM   1088 C C    . LYS A 1 133 ? -21.47400 -26.83500 8.35700   1.000 22.17000 ? 133 LYS A C    1 
ATOM   1089 C CB   . LYS A 1 133 ? -19.55300 -25.37500 7.64600   1.000 22.06000 ? 133 LYS A CB   1 
ATOM   1090 C CG   . LYS A 1 133 ? -19.43500 -25.88400 6.22000   1.000 23.57000 ? 133 LYS A CG   1 
ATOM   1091 C CD   . LYS A 1 133 ? -18.16500 -25.38600 5.55700   1.000 30.86000 ? 133 LYS A CD   1 
ATOM   1092 C CE   . LYS A 1 133 ? -18.19700 -25.63600 4.05900   1.000 33.55000 ? 133 LYS A CE   1 
ATOM   1093 N NZ   . LYS A 1 133 ? -16.85600 -25.43700 3.43800   1.000 35.78000 ? 133 LYS A NZ   1 
ATOM   1094 N N    . THR B 1 1   ? -5.81800  -26.11100 -18.06800 1.000 34.44000 ? 1   THR B N    1 
ATOM   1095 C CA   . THR B 1 1   ? -6.23300  -24.75500 -17.72900 1.000 31.22000 ? 1   THR B CA   1 
ATOM   1096 C C    . THR B 1 1   ? -7.65100  -24.47300 -18.20900 1.000 26.96000 ? 1   THR B C    1 
ATOM   1097 O O    . THR B 1 1   ? -8.28300  -23.52500 -17.75300 1.000 27.83000 ? 1   THR B O    1 
ATOM   1098 C CB   . THR B 1 1   ? -5.28000  -23.70200 -18.32400 1.000 33.37000 ? 1   THR B CB   1 
ATOM   1099 O OG1  . THR B 1 1   ? -3.92500  -24.14800 -18.18700 1.000 38.20000 ? 1   THR B OG1  1 
ATOM   1100 C CG2  . THR B 1 1   ? -5.45000  -22.36700 -17.61400 1.000 28.54000 ? 1   THR B CG2  1 
ATOM   1101 N N    . ARG B 1 2   ? -8.14800  -25.29500 -19.13100 1.000 23.79000 ? 2   ARG B N    1 
ATOM   1102 C CA   . ARG B 1 2   ? -9.51600  -25.17200 -19.61900 1.000 24.44000 ? 2   ARG B CA   1 
ATOM   1103 C C    . ARG B 1 2   ? -10.51200 -26.00300 -18.81600 1.000 21.23000 ? 2   ARG B C    1 
ATOM   1104 O O    . ARG B 1 2   ? -11.71300 -25.93600 -19.09400 1.000 25.04000 ? 2   ARG B O    1 
ATOM   1105 C CB   . ARG B 1 2   ? -9.60000  -25.55300 -21.10500 1.000 26.42000 ? 2   ARG B CB   1 
ATOM   1106 C CG   . ARG B 1 2   ? -9.40900  -24.39000 -22.08400 1.000 25.36000 ? 2   ARG B CG   1 
ATOM   1107 C CD   . ARG B 1 2   ? -9.93600  -24.72400 -23.48400 1.000 23.46000 ? 2   ARG B CD   1 
ATOM   1108 N NE   . ARG B 1 2   ? -9.58500  -23.69800 -24.46700 1.000 22.78000 ? 2   ARG B NE   1 
ATOM   1109 C CZ   . ARG B 1 2   ? -9.76100  -23.81400 -25.78100 1.000 21.32000 ? 2   ARG B CZ   1 
ATOM   1110 N NH1  . ARG B 1 2   ? -10.28600 -24.92700 -26.28600 1.000 27.30000 ? 2   ARG B NH1  1 
ATOM   1111 N NH2  . ARG B 1 2   ? -9.40600  -22.82100 -26.59500 1.000 24.31000 ? 2   ARG B NH2  1 
ATOM   1112 N N    . ASP B 1 3   ? -10.05400 -26.77000 -17.82500 1.000 18.55000 ? 3   ASP B N    1 
ATOM   1113 C CA   . ASP B 1 3   ? -10.92100 -27.64400 -17.03600 1.000 16.38000 ? 3   ASP B CA   1 
ATOM   1114 C C    . ASP B 1 3   ? -11.34800 -26.92200 -15.76100 1.000 19.69000 ? 3   ASP B C    1 
ATOM   1115 O O    . ASP B 1 3   ? -10.56000 -26.79100 -14.81900 1.000 18.71000 ? 3   ASP B O    1 
ATOM   1116 C CB   . ASP B 1 3   ? -10.19600 -28.94300 -16.69700 1.000 19.41000 ? 3   ASP B CB   1 
ATOM   1117 C CG   . ASP B 1 3   ? -11.12400 -29.99200 -16.12500 1.000 20.24000 ? 3   ASP B CG   1 
ATOM   1118 O OD1  . ASP B 1 3   ? -12.29100 -29.66200 -15.82900 1.000 16.32000 ? 3   ASP B OD1  1 
ATOM   1119 O OD2  . ASP B 1 3   ? -10.67900 -31.14700 -15.95100 1.000 24.80000 ? 3   ASP B OD2  1 
ATOM   1120 N N    . ALA B 1 4   ? -12.61200 -26.49000 -15.72200 1.000 15.59000 ? 4   ALA B N    1 
ATOM   1121 C CA   . ALA B 1 4   ? -13.19200 -25.79500 -14.57900 1.000 16.78000 ? 4   ALA B CA   1 
ATOM   1122 C C    . ALA B 1 4   ? -13.99600 -26.71500 -13.67100 1.000 13.83000 ? 4   ALA B C    1 
ATOM   1123 O O    . ALA B 1 4   ? -14.60900 -26.24500 -12.70900 1.000 14.95000 ? 4   ALA B O    1 
ATOM   1124 C CB   . ALA B 1 4   ? -14.06900 -24.63300 -15.04900 1.000 17.51000 ? 4   ALA B CB   1 
ATOM   1125 N N    . ASN B 1 5   ? -14.00600 -28.01400 -13.95200 1.000 14.06000 ? 5   ASN B N    1 
ATOM   1126 C CA   . ASN B 1 5   ? -14.75400 -28.94200 -13.11900 1.000 13.55000 ? 5   ASN B CA   1 
ATOM   1127 C C    . ASN B 1 5   ? -14.32400 -28.81000 -11.66500 1.000 15.02000 ? 5   ASN B C    1 
ATOM   1128 O O    . ASN B 1 5   ? -13.14200 -28.61400 -11.36300 1.000 15.20000 ? 5   ASN B O    1 
ATOM   1129 C CB   . ASN B 1 5   ? -14.47400 -30.38200 -13.55600 1.000 14.99000 ? 5   ASN B CB   1 
ATOM   1130 C CG   . ASN B 1 5   ? -15.37900 -30.83700 -14.67100 1.000 12.98000 ? 5   ASN B CG   1 
ATOM   1131 O OD1  . ASN B 1 5   ? -16.57600 -31.04100 -14.46300 1.000 13.11000 ? 5   ASN B OD1  1 
ATOM   1132 N ND2  . ASN B 1 5   ? -14.81900 -30.99500 -15.86100 1.000 14.02000 ? 5   ASN B ND2  1 
ATOM   1133 N N    . GLY B 1 6   ? -15.28600 -28.94100 -10.76400 1.000 14.79000 ? 6   GLY B N    1 
ATOM   1134 C CA   . GLY B 1 6   ? -14.96200 -29.04500 -9.35700  1.000 15.95000 ? 6   GLY B CA   1 
ATOM   1135 C C    . GLY B 1 6   ? -15.90300 -28.29100 -8.44400  1.000 13.60000 ? 6   GLY B C    1 
ATOM   1136 O O    . GLY B 1 6   ? -16.88600 -27.66700 -8.87900  1.000 13.96000 ? 6   GLY B O    1 
ATOM   1137 N N    . THR B 1 7   ? -15.60200 -28.36800 -7.15500  1.000 13.86000 ? 7   THR B N    1 
ATOM   1138 C CA   . THR B 1 7   ? -16.26600 -27.59700 -6.12400  1.000 12.66000 ? 7   THR B CA   1 
ATOM   1139 C C    . THR B 1 7   ? -15.28900 -26.53200 -5.66500  1.000 12.49000 ? 7   THR B C    1 
ATOM   1140 O O    . THR B 1 7   ? -14.16000 -26.85200 -5.27400  1.000 14.78000 ? 7   THR B O    1 
ATOM   1141 C CB   . THR B 1 7   ? -16.64800 -28.51300 -4.96200  1.000 15.08000 ? 7   THR B CB   1 
ATOM   1142 O OG1  . THR B 1 7   ? -17.65600 -29.43000 -5.40800  1.000 17.37000 ? 7   THR B OG1  1 
ATOM   1143 C CG2  . THR B 1 7   ? -17.16900 -27.71400 -3.78500  1.000 14.90000 ? 7   THR B CG2  1 
ATOM   1144 N N    . TRP B 1 8   ? -15.72100 -25.27100 -5.71500  1.000 11.59000 ? 8   TRP B N    1 
ATOM   1145 C CA   . TRP B 1 8   ? -14.83600 -24.12400 -5.54400  1.000 12.57000 ? 8   TRP B CA   1 
ATOM   1146 C C    . TRP B 1 8   ? -15.33100 -23.26900 -4.38400  1.000 11.74000 ? 8   TRP B C    1 
ATOM   1147 O O    . TRP B 1 8   ? -16.46500 -22.77200 -4.41300  1.000 13.75000 ? 8   TRP B O    1 
ATOM   1148 C CB   . TRP B 1 8   ? -14.79500 -23.30600 -6.84000  1.000 12.31000 ? 8   TRP B CB   1 
ATOM   1149 C CG   . TRP B 1 8   ? -14.27800 -24.06400 -8.04100  1.000 12.29000 ? 8   TRP B CG   1 
ATOM   1150 C CD1  . TRP B 1 8   ? -15.01500 -24.75400 -8.96000  1.000 12.09000 ? 8   TRP B CD1  1 
ATOM   1151 C CD2  . TRP B 1 8   ? -12.91300 -24.19400 -8.43800  1.000 11.37000 ? 8   TRP B CD2  1 
ATOM   1152 N NE1  . TRP B 1 8   ? -14.18600 -25.29800 -9.91800  1.000 13.31000 ? 8   TRP B NE1  1 
ATOM   1153 C CE2  . TRP B 1 8   ? -12.88900 -24.97300 -9.61500  1.000 11.94000 ? 8   TRP B CE2  1 
ATOM   1154 C CE3  . TRP B 1 8   ? -11.70700 -23.72200 -7.91700  1.000 12.00000 ? 8   TRP B CE3  1 
ATOM   1155 C CZ2  . TRP B 1 8   ? -11.70800 -25.28200 -10.27800 1.000 13.77000 ? 8   TRP B CZ2  1 
ATOM   1156 C CZ3  . TRP B 1 8   ? -10.54100 -24.02800 -8.57300  1.000 12.66000 ? 8   TRP B CZ3  1 
ATOM   1157 C CH2  . TRP B 1 8   ? -10.54400 -24.80100 -9.74200  1.000 13.70000 ? 8   TRP B CH2  1 
ATOM   1158 N N    . GLU B 1 9   ? -14.48100 -23.08000 -3.37300  1.000 11.18000 ? 9   GLU B N    1 
ATOM   1159 C CA   . GLU B 1 9   ? -14.84900 -22.35000 -2.16300  1.000 10.88000 ? 9   GLU B CA   1 
ATOM   1160 C C    . GLU B 1 9   ? -14.21200 -20.96700 -2.16200  1.000 10.97000 ? 9   GLU B C    1 
ATOM   1161 O O    . GLU B 1 9   ? -13.00800 -20.82800 -2.37300  1.000 10.66000 ? 9   GLU B O    1 
ATOM   1162 C CB   . GLU B 1 9   ? -14.41900 -23.13000 -0.92000  1.000 14.32000 ? 9   GLU B CB   1 
ATOM   1163 C CG   . GLU B 1 9   ? -15.12300 -24.48000 -0.78800  1.000 18.03000 ? 9   GLU B CG   1 
ATOM   1164 C CD   . GLU B 1 9   ? -14.77500 -25.21100 0.49700   1.000 20.78000 ? 9   GLU B CD   1 
ATOM   1165 O OE1  . GLU B 1 9   ? -13.58200 -25.25800 0.85300   1.000 23.38000 ? 9   GLU B OE1  1 
ATOM   1166 O OE2  . GLU B 1 9   ? -15.70300 -25.73200 1.15300   1.000 25.15000 ? 9   GLU B OE2  1 
ATOM   1167 N N    . MET B 1 10  ? -15.01700 -19.94700 -1.89900  1.000 12.37000 ? 10  MET B N    1 
ATOM   1168 C CA   . MET B 1 10  ? -14.52200 -18.57700 -2.00600  1.000 12.00000 ? 10  MET B CA   1 
ATOM   1169 C C    . MET B 1 10  ? -13.41200 -18.30000 -0.99100  1.000 11.48000 ? 10  MET B C    1 
ATOM   1170 O O    . MET B 1 10  ? -13.52500 -18.65000 0.19300   1.000 13.82000 ? 10  MET B O    1 
ATOM   1171 C CB   . MET B 1 10  ? -15.68300 -17.61500 -1.78000  1.000 12.48000 ? 10  MET B CB   1 
ATOM   1172 C CG   . MET B 1 10  ? -15.29600 -16.15100 -1.72000  1.000 12.20000 ? 10  MET B CG   1 
ATOM   1173 S SD   . MET B 1 10  ? -16.73400 -15.07000 -1.77700  1.000 12.91000 ? 10  MET B SD   1 
ATOM   1174 C CE   . MET B 1 10  ? -16.95000 -14.89500 -3.53800  1.000 15.08000 ? 10  MET B CE   1 
ATOM   1175 N N    . GLU B 1 11  ? -12.34400 -17.65400 -1.45400  0.940 11.10000 ? 11  GLU B N    1 
ATOM   1176 C CA   . GLU B 1 11  ? -11.25700 -17.17100 -0.61700  0.940 12.81000 ? 11  GLU B CA   1 
ATOM   1177 C C    . GLU B 1 11  ? -11.16300 -15.65900 -0.56300  0.940 11.26000 ? 11  GLU B C    1 
ATOM   1178 O O    . GLU B 1 11  ? -10.57900 -15.12700 0.38500   0.940 12.10000 ? 11  GLU B O    1 
ATOM   1179 C CB   . GLU B 1 11  ? -9.90800  -17.67300 -1.14700  0.940 18.82000 ? 11  GLU B CB   1 
ATOM   1180 C CG   . GLU B 1 11  ? -9.68100  -19.16400 -1.10300  0.940 20.91000 ? 11  GLU B CG   1 
ATOM   1181 C CD   . GLU B 1 11  ? -8.22300  -19.51000 -1.33200  0.940 25.14000 ? 11  GLU B CD   1 
ATOM   1182 O OE1  . GLU B 1 11  ? -7.72800  -20.46900 -0.70700  0.940 34.12000 ? 11  GLU B OE1  1 
ATOM   1183 O OE2  . GLU B 1 11  ? -7.57400  -18.81200 -2.13800  0.940 27.43000 ? 11  GLU B OE2  1 
ATOM   1184 N N    . SER B 1 12  ? -11.65300 -14.94900 -1.58000  1.000 10.71000 ? 12  SER B N    1 
ATOM   1185 C CA   . SER B 1 12  ? -11.61100 -13.49500 -1.55600  1.000 12.03000 ? 12  SER B CA   1 
ATOM   1186 C C    . SER B 1 12  ? -12.65800 -12.94900 -2.51200  1.000 10.70000 ? 12  SER B C    1 
ATOM   1187 O O    . SER B 1 12  ? -13.06000 -13.60300 -3.48400  1.000 9.97000  ? 12  SER B O    1 
ATOM   1188 C CB   . SER B 1 12  ? -10.22400 -12.94900 -1.89100  1.000 14.66000 ? 12  SER B CB   1 
ATOM   1189 O OG   . SER B 1 12  ? -9.82400  -13.34100 -3.17300  1.000 17.00000 ? 12  SER B OG   1 
ATOM   1190 N N    . ASN B 1 13  ? -13.08300 -11.72600 -2.22200  1.000 10.41000 ? 13  ASN B N    1 
ATOM   1191 C CA   . ASN B 1 13  ? -14.14400 -11.07100 -2.97800  1.000 11.48000 ? 13  ASN B CA   1 
ATOM   1192 C C    . ASN B 1 13  ? -13.88800 -9.57100  -2.91400  1.000 11.29000 ? 13  ASN B C    1 
ATOM   1193 O O    . ASN B 1 13  ? -13.98800 -8.97400  -1.83500  1.000 13.34000 ? 13  ASN B O    1 
ATOM   1194 C CB   . ASN B 1 13  ? -15.50100 -11.42600 -2.37500  1.000 11.55000 ? 13  ASN B CB   1 
ATOM   1195 C CG   . ASN B 1 13  ? -16.65700 -11.15000 -3.31400  1.000 11.46000 ? 13  ASN B CG   1 
ATOM   1196 O OD1  . ASN B 1 13  ? -16.48200 -10.59400 -4.39200  1.000 10.88000 ? 13  ASN B OD1  1 
ATOM   1197 N ND2  . ASN B 1 13  ? -17.85200 -11.54800 -2.90700  1.000 12.78000 ? 13  ASN B ND2  1 
ATOM   1198 N N    . GLU B 1 14  ? -13.56900 -8.97000  -4.05600  1.000 10.75000 ? 14  GLU B N    1 
ATOM   1199 C CA   . GLU B 1 14  ? -13.21900 -7.55600  -4.15100  1.000 11.42000 ? 14  GLU B CA   1 
ATOM   1200 C C    . GLU B 1 14  ? -14.30100 -6.83100  -4.94200  1.000 11.15000 ? 14  GLU B C    1 
ATOM   1201 O O    . GLU B 1 14  ? -14.59900 -7.20600  -6.08300  1.000 10.21000 ? 14  GLU B O    1 
ATOM   1202 C CB   . GLU B 1 14  ? -11.85500 -7.38600  -4.82100  1.000 13.63000 ? 14  GLU B CB   1 
ATOM   1203 C CG   . GLU B 1 14  ? -11.51400 -5.93400  -5.14700  1.000 16.02000 ? 14  GLU B CG   1 
ATOM   1204 C CD   . GLU B 1 14  ? -10.12500 -5.74500  -5.73000  1.000 24.36000 ? 14  GLU B CD   1 
ATOM   1205 O OE1  . GLU B 1 14  ? -9.47600  -6.74700  -6.10100  1.000 22.89000 ? 14  GLU B OE1  1 
ATOM   1206 O OE2  . GLU B 1 14  ? -9.67500  -4.57900  -5.80400  1.000 25.23000 ? 14  GLU B OE2  1 
ATOM   1207 N N    . ASN B 1 15  ? -14.89300 -5.80300  -4.33100  1.000 11.63000 ? 15  ASN B N    1 
ATOM   1208 C CA   . ASN B 1 15  ? -15.84800 -4.92000  -4.99900  1.000 12.25000 ? 15  ASN B CA   1 
ATOM   1209 C C    . ASN B 1 15  ? -17.13500 -5.62800  -5.42100  1.000 11.48000 ? 15  ASN B C    1 
ATOM   1210 O O    . ASN B 1 15  ? -17.76900 -5.23900  -6.40500  1.000 11.34000 ? 15  ASN B O    1 
ATOM   1211 C CB   . ASN B 1 15  ? -15.22300 -4.16300  -6.16800  1.000 12.64000 ? 15  ASN B CB   1 
ATOM   1212 C CG   . ASN B 1 15  ? -16.08300 -3.01000  -6.63400  1.000 12.78000 ? 15  ASN B CG   1 
ATOM   1213 O OD1  . ASN B 1 15  ? -16.74800 -2.34600  -5.83000  1.000 13.80000 ? 15  ASN B OD1  1 
ATOM   1214 N ND2  . ASN B 1 15  ? -16.08500 -2.77000  -7.93500  1.000 13.69000 ? 15  ASN B ND2  1 
ATOM   1215 N N    . PHE B 1 16  ? -17.55700 -6.64400  -4.66900  1.000 11.55000 ? 16  PHE B N    1 
ATOM   1216 C CA   . PHE B 1 16  ? -18.87200 -7.23800  -4.89500  1.000 11.66000 ? 16  PHE B CA   1 
ATOM   1217 C C    . PHE B 1 16  ? -19.97000 -6.18500  -4.75300  1.000 11.22000 ? 16  PHE B C    1 
ATOM   1218 O O    . PHE B 1 16  ? -20.94000 -6.17200  -5.52200  1.000 11.38000 ? 16  PHE B O    1 
ATOM   1219 C CB   . PHE B 1 16  ? -19.06600 -8.37800  -3.89400  1.000 12.20000 ? 16  PHE B CB   1 
ATOM   1220 C CG   . PHE B 1 16  ? -20.09600 -9.40800  -4.28500  1.000 11.68000 ? 16  PHE B CG   1 
ATOM   1221 C CD1  . PHE B 1 16  ? -20.34800 -9.74500  -5.61000  1.000 12.81000 ? 16  PHE B CD1  1 
ATOM   1222 C CD2  . PHE B 1 16  ? -20.78400 -10.08400 -3.28700  1.000 12.62000 ? 16  PHE B CD2  1 
ATOM   1223 C CE1  . PHE B 1 16  ? -21.28900 -10.71700 -5.92300  1.000 14.84000 ? 16  PHE B CE1  1 
ATOM   1224 C CE2  . PHE B 1 16  ? -21.70700 -11.05800 -3.59000  1.000 15.06000 ? 16  PHE B CE2  1 
ATOM   1225 C CZ   . PHE B 1 16  ? -21.96400 -11.37900 -4.90800  1.000 16.14000 ? 16  PHE B CZ   1 
ATOM   1226 N N    . GLU B 1 17  ? -19.83600 -5.29100  -3.75900  1.000 12.22000 ? 17  GLU B N    1 
ATOM   1227 C CA   . GLU B 1 17  ? -20.81100 -4.21600  -3.55800  1.000 13.03000 ? 17  GLU B CA   1 
ATOM   1228 C C    . GLU B 1 17  ? -20.94100 -3.33300  -4.79000  1.000 12.37000 ? 17  GLU B C    1 
ATOM   1229 O O    . GLU B 1 17  ? -22.05400 -3.01900  -5.22500  1.000 13.54000 ? 17  GLU B O    1 
ATOM   1230 C CB   . GLU B 1 17  ? -20.41000 -3.37500  -2.34200  1.000 16.07000 ? 17  GLU B CB   1 
ATOM   1231 C CG   . GLU B 1 17  ? -21.00400 -1.96500  -2.31800  1.000 17.76000 ? 17  GLU B CG   1 
ATOM   1232 C CD   . GLU B 1 17  ? -22.49000 -1.95600  -2.01900  1.000 19.11000 ? 17  GLU B CD   1 
ATOM   1233 O OE1  . GLU B 1 17  ? -23.08100 -0.85000  -1.95500  1.000 23.24000 ? 17  GLU B OE1  1 
ATOM   1234 O OE2  . GLU B 1 17  ? -23.07500 -3.04900  -1.84600  1.000 20.51000 ? 17  GLU B OE2  1 
ATOM   1235 N N    . GLY B 1 18  ? -19.81700 -2.88600  -5.34600  1.000 14.54000 ? 18  GLY B N    1 
ATOM   1236 C CA   . GLY B 1 18  ? -19.88300 -2.00200  -6.49700  1.000 15.56000 ? 18  GLY B CA   1 
ATOM   1237 C C    . GLY B 1 18  ? -20.52600 -2.65900  -7.70300  1.000 13.36000 ? 18  GLY B C    1 
ATOM   1238 O O    . GLY B 1 18  ? -21.30500 -2.02800  -8.42400  1.000 12.52000 ? 18  GLY B O    1 
ATOM   1239 N N    . TRP B 1 19  ? -20.22300 -3.94200  -7.93000  1.000 12.02000 ? 19  TRP B N    1 
ATOM   1240 C CA   . TRP B 1 19  ? -20.82500 -4.66500  -9.04300  1.000 10.32000 ? 19  TRP B CA   1 
ATOM   1241 C C    . TRP B 1 19  ? -22.33000 -4.82300  -8.83900  1.000 10.40000 ? 19  TRP B C    1 
ATOM   1242 O O    . TRP B 1 19  ? -23.11700 -4.54800  -9.74900  1.000 10.99000 ? 19  TRP B O    1 
ATOM   1243 C CB   . TRP B 1 19  ? -20.10800 -6.01200  -9.21400  1.000 10.10000 ? 19  TRP B CB   1 
ATOM   1244 C CG   . TRP B 1 19  ? -20.68800 -6.89400  -10.26600 1.000 11.49000 ? 19  TRP B CG   1 
ATOM   1245 C CD1  . TRP B 1 19  ? -20.48600 -6.80900  -11.61500 1.000 11.70000 ? 19  TRP B CD1  1 
ATOM   1246 C CD2  . TRP B 1 19  ? -21.57600 -7.99800  -10.06200 1.000 11.68000 ? 19  TRP B CD2  1 
ATOM   1247 N NE1  . TRP B 1 19  ? -21.18600 -7.79900  -12.25500 1.000 12.45000 ? 19  TRP B NE1  1 
ATOM   1248 C CE2  . TRP B 1 19  ? -21.86200 -8.54200  -11.32800 1.000 13.41000 ? 19  TRP B CE2  1 
ATOM   1249 C CE3  . TRP B 1 19  ? -22.14400 -8.58600  -8.93200  1.000 13.15000 ? 19  TRP B CE3  1 
ATOM   1250 C CZ2  . TRP B 1 19  ? -22.69600 -9.64200  -11.49700 1.000 16.75000 ? 19  TRP B CZ2  1 
ATOM   1251 C CZ3  . TRP B 1 19  ? -22.97400 -9.67200  -9.10300  1.000 16.72000 ? 19  TRP B CZ3  1 
ATOM   1252 C CH2  . TRP B 1 19  ? -23.24000 -10.19100 -10.37400 1.000 17.19000 ? 19  TRP B CH2  1 
ATOM   1253 N N    . MET B 1 20  ? -22.75500 -5.23400  -7.63900  1.000 10.32000 ? 20  MET B N    1 
ATOM   1254 C CA   . MET B 1 20  ? -24.18900 -5.35000  -7.37800  1.000 10.50000 ? 20  MET B CA   1 
ATOM   1255 C C    . MET B 1 20  ? -24.89600 -4.00200  -7.49000  1.000 10.68000 ? 20  MET B C    1 
ATOM   1256 O O    . MET B 1 20  ? -26.02800 -3.92500  -7.97600  1.000 10.65000 ? 20  MET B O    1 
ATOM   1257 C CB   . MET B 1 20  ? -24.44700 -5.95300  -5.99800  1.000 10.60000 ? 20  MET B CB   1 
ATOM   1258 C CG   . MET B 1 20  ? -24.09900 -7.43600  -5.86600  1.000 11.32000 ? 20  MET B CG   1 
ATOM   1259 S SD   . MET B 1 20  ? -24.66100 -8.14600  -4.30200  1.000 12.38000 ? 20  MET B SD   1 
ATOM   1260 C CE   . MET B 1 20  ? -23.44700 -7.44900  -3.17400  1.000 16.11000 ? 20  MET B CE   1 
ATOM   1261 N N    . LYS B 1 21  ? -24.25700 -2.93700  -7.01900  1.000 10.54000 ? 21  LYS B N    1 
ATOM   1262 C CA   . LYS B 1 21  ? -24.86600 -1.61500  -7.10400  1.000 10.90000 ? 21  LYS B CA   1 
ATOM   1263 C C    . LYS B 1 21  ? -25.00400 -1.17500  -8.55500  1.000 11.67000 ? 21  LYS B C    1 
ATOM   1264 O O    . LYS B 1 21  ? -26.00600 -0.55100  -8.92500  1.000 11.56000 ? 21  LYS B O    1 
ATOM   1265 C CB   . LYS B 1 21  ? -24.03300 -0.62100  -6.30300  1.000 12.29000 ? 21  LYS B CB   1 
ATOM   1266 C CG   . LYS B 1 21  ? -24.65800 0.74600   -6.17200  1.000 12.96000 ? 21  LYS B CG   1 
ATOM   1267 C CD   . LYS B 1 21  ? -23.82600 1.56500   -5.21800  1.000 16.64000 ? 21  LYS B CD   1 
ATOM   1268 C CE   . LYS B 1 21  ? -24.52500 2.84700   -4.84700  1.000 19.22000 ? 21  LYS B CE   1 
ATOM   1269 N NZ   . LYS B 1 21  ? -23.76000 3.54100   -3.79100  1.000 20.39000 ? 21  LYS B NZ   1 
ATOM   1270 N N    . ALA B 1 22  ? -24.01800 -1.50900  -9.39900  1.000 12.74000 ? 22  ALA B N    1 
ATOM   1271 C CA   . ALA B 1 22  ? -24.10200 -1.20500  -10.82400 1.000 11.44000 ? 22  ALA B CA   1 
ATOM   1272 C C    . ALA B 1 22  ? -25.25600 -1.94200  -11.49700 1.000 12.01000 ? 22  ALA B C    1 
ATOM   1273 O O    . ALA B 1 22  ? -25.79200 -1.46200  -12.50700 1.000 13.15000 ? 22  ALA B O    1 
ATOM   1274 C CB   . ALA B 1 22  ? -22.77100 -1.53200  -11.51300 1.000 13.63000 ? 22  ALA B CB   1 
ATOM   1275 N N    . LEU B 1 23  ? -25.65800 -3.10100  -10.96300 1.000 11.40000 ? 23  LEU B N    1 
ATOM   1276 C CA   . LEU B 1 23  ? -26.81600 -3.84300  -11.45600 1.000 11.29000 ? 23  LEU B CA   1 
ATOM   1277 C C    . LEU B 1 23  ? -28.13000 -3.36800  -10.85300 1.000 12.70000 ? 23  LEU B C    1 
ATOM   1278 O O    . LEU B 1 23  ? -29.18700 -3.90900  -11.20300 1.000 12.74000 ? 23  LEU B O    1 
ATOM   1279 C CB   . LEU B 1 23  ? -26.65100 -5.33700  -11.16100 1.000 12.57000 ? 23  LEU B CB   1 
ATOM   1280 C CG   . LEU B 1 23  ? -25.60100 -6.08600  -11.97500 1.000 11.76000 ? 23  LEU B CG   1 
ATOM   1281 C CD1  . LEU B 1 23  ? -25.37900 -7.47300  -11.39600 1.000 15.71000 ? 23  LEU B CD1  1 
ATOM   1282 C CD2  . LEU B 1 23  ? -26.03000 -6.17100  -13.43200 1.000 13.88000 ? 23  LEU B CD2  1 
ATOM   1283 N N    . ASP B 1 24  ? -28.08900 -2.40800  -9.93600  1.000 11.85000 ? 24  ASP B N    1 
ATOM   1284 C CA   . ASP B 1 24  ? -29.29100 -1.86700  -9.29300  1.000 13.62000 ? 24  ASP B CA   1 
ATOM   1285 C C    . ASP B 1 24  ? -29.95900 -2.86200  -8.34500  1.000 15.39000 ? 24  ASP B C    1 
ATOM   1286 O O    . ASP B 1 24  ? -31.17500 -2.81100  -8.13100  1.000 17.84000 ? 24  ASP B O    1 
ATOM   1287 C CB   . ASP B 1 24  ? -30.28300 -1.28600  -10.30900 1.000 14.18000 ? 24  ASP B CB   1 
ATOM   1288 C CG   . ASP B 1 24  ? -29.59300 -0.45000  -11.34800 1.000 13.44000 ? 24  ASP B CG   1 
ATOM   1289 O OD1  . ASP B 1 24  ? -28.90200 0.50900   -10.94700 1.000 15.74000 ? 24  ASP B OD1  1 
ATOM   1290 O OD2  . ASP B 1 24  ? -29.70100 -0.76700  -12.55400 1.000 13.03000 ? 24  ASP B OD2  1 
ATOM   1291 N N    . ILE B 1 25  ? -29.17300 -3.76500  -7.75400  1.000 13.18000 ? 25  ILE B N    1 
ATOM   1292 C CA   . ILE B 1 25  ? -29.69400 -4.62600  -6.69900  1.000 14.12000 ? 25  ILE B CA   1 
ATOM   1293 C C    . ILE B 1 25  ? -30.10200 -3.77500  -5.50500  1.000 13.73000 ? 25  ILE B C    1 
ATOM   1294 O O    . ILE B 1 25  ? -29.38500 -2.85000  -5.10500  1.000 13.65000 ? 25  ILE B O    1 
ATOM   1295 C CB   . ILE B 1 25  ? -28.63700 -5.66900  -6.29100  1.000 13.53000 ? 25  ILE B CB   1 
ATOM   1296 C CG1  . ILE B 1 25  ? -28.19100 -6.50600  -7.48900  1.000 16.16000 ? 25  ILE B CG1  1 
ATOM   1297 C CG2  . ILE B 1 25  ? -29.16100 -6.55200  -5.15000  1.000 13.40000 ? 25  ILE B CG2  1 
ATOM   1298 C CD1  . ILE B 1 25  ? -29.28200 -7.27800  -8.12000  1.000 17.32000 ? 25  ILE B CD1  1 
ATOM   1299 N N    . ASP B 1 26  ? -31.25300 -4.10400  -4.91400  1.000 14.08000 ? 26  ASP B N    1 
ATOM   1300 C CA   . ASP B 1 26  ? -31.73700 -3.38500  -3.73900  1.000 15.51000 ? 26  ASP B CA   1 
ATOM   1301 C C    . ASP B 1 26  ? -30.69800 -3.39000  -2.62200  1.000 14.78000 ? 26  ASP B C    1 
ATOM   1302 O O    . ASP B 1 26  ? -30.05000 -4.40600  -2.35300  1.000 13.23000 ? 26  ASP B O    1 
ATOM   1303 C CB   . ASP B 1 26  ? -33.03300 -4.02400  -3.23400  1.000 18.37000 ? 26  ASP B CB   1 
ATOM   1304 C CG   . ASP B 1 26  ? -33.57100 -3.34900  -1.98400  1.000 23.21000 ? 26  ASP B CG   1 
ATOM   1305 O OD1  . ASP B 1 26  ? -33.15200 -3.72900  -0.86800  1.000 26.85000 ? 26  ASP B OD1  1 
ATOM   1306 O OD2  . ASP B 1 26  ? -34.40900 -2.43300  -2.12700  1.000 32.00000 ? 26  ASP B OD2  1 
ATOM   1307 N N    . PHE B 1 27  ? -30.56500 -2.24100  -1.95300  1.000 14.34000 ? 27  PHE B N    1 
ATOM   1308 C CA   . PHE B 1 27  ? -29.56300 -2.04900  -0.90800  1.000 17.10000 ? 27  PHE B CA   1 
ATOM   1309 C C    . PHE B 1 27  ? -29.61900 -3.14200  0.15500   1.000 15.69000 ? 27  PHE B C    1 
ATOM   1310 O O    . PHE B 1 27  ? -28.58100 -3.66900  0.56900   1.000 15.61000 ? 27  PHE B O    1 
ATOM   1311 C CB   . PHE B 1 27  ? -29.77800 -0.66800  -0.28300  1.000 17.24000 ? 27  PHE B CB   1 
ATOM   1312 C CG   . PHE B 1 27  ? -28.85000 -0.34500  0.85700   1.000 19.61000 ? 27  PHE B CG   1 
ATOM   1313 C CD1  . PHE B 1 27  ? -29.14600 -0.74500  2.15200   1.000 21.10000 ? 27  PHE B CD1  1 
ATOM   1314 C CD2  . PHE B 1 27  ? -27.70700 0.40500   0.64300   1.000 23.45000 ? 27  PHE B CD2  1 
ATOM   1315 C CE1  . PHE B 1 27  ? -28.29800 -0.43100  3.19800   1.000 26.21000 ? 27  PHE B CE1  1 
ATOM   1316 C CE2  . PHE B 1 27  ? -26.86000 0.72400   1.68900   1.000 26.83000 ? 27  PHE B CE2  1 
ATOM   1317 C CZ   . PHE B 1 27  ? -27.15800 0.30700   2.96600   1.000 26.27000 ? 27  PHE B CZ   1 
ATOM   1318 N N    . ALA B 1 28  ? -30.82200 -3.47900  0.63300   1.000 16.25000 ? 28  ALA B N    1 
ATOM   1319 C CA   . ALA B 1 28  ? -30.92300 -4.45900  1.71100   1.000 16.51000 ? 28  ALA B CA   1 
ATOM   1320 C C    . ALA B 1 28  ? -30.46100 -5.83700  1.25200   1.000 16.31000 ? 28  ALA B C    1 
ATOM   1321 O O    . ALA B 1 28  ? -29.82400 -6.57600  2.01200   1.000 16.76000 ? 28  ALA B O    1 
ATOM   1322 C CB   . ALA B 1 28  ? -32.35100 -4.50200  2.25600   1.000 19.55000 ? 28  ALA B CB   1 
ATOM   1323 N N    . LEU B 1 29  ? -30.75900 -6.19700  0.00200   1.000 15.79000 ? 29  LEU B N    1 
ATOM   1324 C CA   . LEU B 1 29  ? -30.28900 -7.47400  -0.52700  1.000 15.18000 ? 29  LEU B CA   1 
ATOM   1325 C C    . LEU B 1 29  ? -28.78500 -7.46400  -0.76700  1.000 14.58000 ? 29  LEU B C    1 
ATOM   1326 O O    . LEU B 1 29  ? -28.11900 -8.48600  -0.56300  1.000 14.14000 ? 29  LEU B O    1 
ATOM   1327 C CB   . LEU B 1 29  ? -31.04300 -7.82500  -1.80200  1.000 16.28000 ? 29  LEU B CB   1 
ATOM   1328 C CG   . LEU B 1 29  ? -32.56000 -7.92300  -1.63400  1.000 19.54000 ? 29  LEU B CG   1 
ATOM   1329 C CD1  . LEU B 1 29  ? -33.18800 -8.37800  -2.94000  1.000 23.62000 ? 29  LEU B CD1  1 
ATOM   1330 C CD2  . LEU B 1 29  ? -32.93900 -8.85700  -0.49200  1.000 23.49000 ? 29  LEU B CD2  1 
ATOM   1331 N N    . ARG B 1 30  ? -28.23000 -6.32700  -1.19300  1.000 14.08000 ? 30  ARG B N    1 
ATOM   1332 C CA   . ARG B 1 30  ? -26.77700 -6.22700  -1.29200  1.000 13.40000 ? 30  ARG B CA   1 
ATOM   1333 C C    . ARG B 1 30  ? -26.12500 -6.49200  0.05800   1.000 15.35000 ? 30  ARG B C    1 
ATOM   1334 O O    . ARG B 1 30  ? -25.10800 -7.19000  0.13500   1.000 16.18000 ? 30  ARG B O    1 
ATOM   1335 C CB   . ARG B 1 30  ? -26.33700 -4.85800  -1.82600  1.000 13.89000 ? 30  ARG B CB   1 
ATOM   1336 C CG   . ARG B 1 30  ? -26.86900 -4.50800  -3.20200  1.000 14.02000 ? 30  ARG B CG   1 
ATOM   1337 C CD   . ARG B 1 30  ? -26.04400 -3.45300  -3.94300  1.000 16.51000 ? 30  ARG B CD   1 
ATOM   1338 N NE   . ARG B 1 30  ? -25.68700 -2.25800  -3.17800  1.000 19.54000 ? 30  ARG B NE   1 
ATOM   1339 C CZ   . ARG B 1 30  ? -26.35200 -1.09900  -3.20700  1.000 16.19000 ? 30  ARG B CZ   1 
ATOM   1340 N NH1  . ARG B 1 30  ? -27.46300 -0.96500  -3.91500  1.000 16.78000 ? 30  ARG B NH1  1 
ATOM   1341 N NH2  . ARG B 1 30  ? -25.90700 -0.07800  -2.50100  1.000 19.55000 ? 30  ARG B NH2  1 
ATOM   1342 N N    . LYS B 1 31  ? -26.68900 -5.93600  1.13600   1.000 14.99000 ? 31  LYS B N    1 
ATOM   1343 C CA   . LYS B 1 31  ? -26.10500 -6.16000  2.45800   1.000 16.35000 ? 31  LYS B CA   1 
ATOM   1344 C C    . LYS B 1 31  ? -26.13600 -7.62800  2.85900   1.000 17.48000 ? 31  LYS B C    1 
ATOM   1345 O O    . LYS B 1 31  ? -25.23400 -8.09700  3.56100   1.000 17.55000 ? 31  LYS B O    1 
ATOM   1346 C CB   . LYS B 1 31  ? -26.81400 -5.31000  3.50800   1.000 21.97000 ? 31  LYS B CB   1 
ATOM   1347 C CG   . LYS B 1 31  ? -26.74700 -3.83700  3.19500   1.000 25.73000 ? 31  LYS B CG   1 
ATOM   1348 C CD   . LYS B 1 31  ? -25.34100 -3.46800  2.75500   1.000 26.55000 ? 31  LYS B CD   1 
ATOM   1349 C CE   . LYS B 1 31  ? -25.34400 -2.19000  1.93900   1.000 28.77000 ? 31  LYS B CE   1 
ATOM   1350 N NZ   . LYS B 1 31  ? -26.06400 -2.38400  0.65600   1.000 23.86000 ? 31  LYS B NZ   1 
ATOM   1351 N N    . ILE B 1 32  ? -27.16400 -8.36200  2.43900   1.000 16.65000 ? 32  ILE B N    1 
ATOM   1352 C CA   . ILE B 1 32  ? -27.24400 -9.78400  2.75400   1.000 17.11000 ? 32  ILE B CA   1 
ATOM   1353 C C    . ILE B 1 32  ? -26.18600 -10.56900 1.98500   1.000 17.64000 ? 32  ILE B C    1 
ATOM   1354 O O    . ILE B 1 32  ? -25.62000 -11.53900 2.49800   1.000 18.57000 ? 32  ILE B O    1 
ATOM   1355 C CB   . ILE B 1 32  ? -28.66800 -10.29500 2.47700   1.000 19.90000 ? 32  ILE B CB   1 
ATOM   1356 C CG1  . ILE B 1 32  ? -29.65700 -9.64100  3.44400   1.000 19.51000 ? 32  ILE B CG1  1 
ATOM   1357 C CG2  . ILE B 1 32  ? -28.73000 -11.80900 2.58600   1.000 20.73000 ? 32  ILE B CG2  1 
ATOM   1358 C CD1  . ILE B 1 32  ? -31.10300 -9.83200  3.05300   1.000 25.97000 ? 32  ILE B CD1  1 
ATOM   1359 N N    . ALA B 1 33  ? -25.89700 -10.16900 0.75000   1.000 14.69000 ? 33  ALA B N    1 
ATOM   1360 C CA   . ALA B 1 33  ? -24.98800 -10.92600 -0.09700  1.000 17.18000 ? 33  ALA B CA   1 
ATOM   1361 C C    . ALA B 1 33  ? -23.53200 -10.50600 0.03700   1.000 14.05000 ? 33  ALA B C    1 
ATOM   1362 O O    . ALA B 1 33  ? -22.64700 -11.31600 -0.24800  1.000 14.96000 ? 33  ALA B O    1 
ATOM   1363 C CB   . ALA B 1 33  ? -25.39900 -10.78600 -1.56900  1.000 17.05000 ? 33  ALA B CB   1 
ATOM   1364 N N    . VAL B 1 34  ? -23.25900 -9.26800  0.45000   1.000 14.26000 ? 34  VAL B N    1 
ATOM   1365 C CA   . VAL B 1 34  ? -21.95500 -8.66600  0.16500   1.000 15.21000 ? 34  VAL B CA   1 
ATOM   1366 C C    . VAL B 1 34  ? -20.81500 -9.45500  0.79900   1.000 14.66000 ? 34  VAL B C    1 
ATOM   1367 O O    . VAL B 1 34  ? -19.76800 -9.67300  0.17300   1.000 15.59000 ? 34  VAL B O    1 
ATOM   1368 C CB   . VAL B 1 34  ? -21.94100 -7.16900  0.54300   1.000 14.86000 ? 34  VAL B CB   1 
ATOM   1369 C CG1  . VAL B 1 34  ? -22.17300 -6.96300  2.04400   1.000 14.86000 ? 34  VAL B CG1  1 
ATOM   1370 C CG2  . VAL B 1 34  ? -20.63900 -6.51600  0.09200   1.000 17.99000 ? 34  VAL B CG2  1 
ATOM   1371 N N    . ARG B 1 35  ? -20.98600 -9.89100  2.04600   1.000 13.90000 ? 35  ARG B N    1 
ATOM   1372 C CA   . ARG B 1 35  ? -19.94700 -10.62200 2.75900   1.000 15.65000 ? 35  ARG B CA   1 
ATOM   1373 C C    . ARG B 1 35  ? -20.33700 -12.07100 3.00900   1.000 13.84000 ? 35  ARG B C    1 
ATOM   1374 O O    . ARG B 1 35  ? -19.78200 -12.71500 3.90800   1.000 17.30000 ? 35  ARG B O    1 
ATOM   1375 C CB   . ARG B 1 35  ? -19.57500 -9.90900  4.06300   1.000 18.63000 ? 35  ARG B CB   1 
ATOM   1376 C CG   . ARG B 1 35  ? -18.17900 -9.31600  4.09400   1.000 26.95000 ? 35  ARG B CG   1 
ATOM   1377 C CD   . ARG B 1 35  ? -18.16400 -7.87600  3.60400   1.000 25.87000 ? 35  ARG B CD   1 
ATOM   1378 N NE   . ARG B 1 35  ? -19.11000 -7.01300  4.31500   1.000 25.05000 ? 35  ARG B NE   1 
ATOM   1379 C CZ   . ARG B 1 35  ? -19.37900 -5.75600  3.96700   1.000 25.18000 ? 35  ARG B CZ   1 
ATOM   1380 N NH1  . ARG B 1 35  ? -20.25800 -5.04100  4.65400   1.000 28.63000 ? 35  ARG B NH1  1 
ATOM   1381 N NH2  . ARG B 1 35  ? -18.77100 -5.21300  2.91800   1.000 28.61000 ? 35  ARG B NH2  1 
ATOM   1382 N N    . LEU B 1 36  ? -21.27500 -12.59800 2.22600   1.000 14.37000 ? 36  LEU B N    1 
ATOM   1383 C CA   . LEU B 1 36  ? -21.70400 -13.98200 2.32600   1.000 14.21000 ? 36  LEU B CA   1 
ATOM   1384 C C    . LEU B 1 36  ? -20.70900 -14.86700 1.58900   1.000 16.05000 ? 36  LEU B C    1 
ATOM   1385 O O    . LEU B 1 36  ? -20.38600 -14.61000 0.42500   1.000 17.60000 ? 36  LEU B O    1 
ATOM   1386 C CB   . LEU B 1 36  ? -23.08700 -14.11400 1.68700   1.000 19.80000 ? 36  LEU B CB   1 
ATOM   1387 C CG   . LEU B 1 36  ? -23.80500 -15.46100 1.70000   1.000 19.31000 ? 36  LEU B CG   1 
ATOM   1388 C CD1  . LEU B 1 36  ? -23.96900 -15.98700 3.12100   1.000 19.51000 ? 36  LEU B CD1  1 
ATOM   1389 C CD2  . LEU B 1 36  ? -25.15600 -15.34100 1.00300   1.000 26.11000 ? 36  LEU B CD2  1 
ATOM   1390 N N    . THR B 1 37  ? -20.22300 -15.91000 2.25100   1.000 17.30000 ? 37  THR B N    1 
ATOM   1391 C CA   . THR B 1 37  ? -19.24800 -16.79500 1.62200   1.000 17.73000 ? 37  THR B CA   1 
ATOM   1392 C C    . THR B 1 37  ? -19.94100 -17.68400 0.60100   1.000 19.71000 ? 37  THR B C    1 
ATOM   1393 O O    . THR B 1 37  ? -20.95600 -18.31900 0.90500   1.000 21.28000 ? 37  THR B O    1 
ATOM   1394 C CB   . THR B 1 37  ? -18.55400 -17.64400 2.68300   1.000 19.31000 ? 37  THR B CB   1 
ATOM   1395 O OG1  . THR B 1 37  ? -17.82300 -16.78200 3.55900   1.000 21.36000 ? 37  THR B OG1  1 
ATOM   1396 C CG2  . THR B 1 37  ? -17.59700 -18.63000 2.03100   1.000 20.85000 ? 37  THR B CG2  1 
ATOM   1397 N N    . LEU B 1 38  ? -19.38900 -17.73400 -0.61100  1.000 17.12000 ? 38  LEU B N    1 
ATOM   1398 C CA   . LEU B 1 38  ? -20.01800 -18.40300 -1.74100  1.000 18.28000 ? 38  LEU B CA   1 
ATOM   1399 C C    . LEU B 1 38  ? -19.28700 -19.69300 -2.09000  1.000 16.29000 ? 38  LEU B C    1 
ATOM   1400 O O    . LEU B 1 38  ? -18.07400 -19.81800 -1.88700  1.000 15.70000 ? 38  LEU B O    1 
ATOM   1401 C CB   . LEU B 1 38  ? -20.01100 -17.50000 -2.97800  1.000 18.01000 ? 38  LEU B CB   1 
ATOM   1402 C CG   . LEU B 1 38  ? -20.59200 -16.09200 -2.82200  1.000 19.26000 ? 38  LEU B CG   1 
ATOM   1403 C CD1  . LEU B 1 38  ? -20.57300 -15.35800 -4.15600  1.000 23.17000 ? 38  LEU B CD1  1 
ATOM   1404 C CD2  . LEU B 1 38  ? -22.00800 -16.13300 -2.25700  1.000 20.55000 ? 38  LEU B CD2  1 
ATOM   1405 N N    . THR B 1 39  ? -20.04200 -20.64800 -2.63400  1.000 16.41000 ? 39  THR B N    1 
ATOM   1406 C CA   . THR B 1 39  ? -19.49300 -21.87700 -3.18900  1.000 17.46000 ? 39  THR B CA   1 
ATOM   1407 C C    . THR B 1 39  ? -19.98500 -22.03600 -4.61800  1.000 16.91000 ? 39  THR B C    1 
ATOM   1408 O O    . THR B 1 39  ? -21.16500 -21.81800 -4.91700  1.000 20.22000 ? 39  THR B O    1 
ATOM   1409 C CB   . THR B 1 39  ? -19.89700 -23.11600 -2.37600  1.000 22.68000 ? 39  THR B CB   1 
ATOM   1410 O OG1  . THR B 1 39  ? -19.36200 -23.01700 -1.05200  1.000 21.30000 ? 39  THR B OG1  1 
ATOM   1411 C CG2  . THR B 1 39  ? -19.36800 -24.38400 -3.02900  1.000 20.39000 ? 39  THR B CG2  1 
ATOM   1412 N N    . LEU B 1 40  ? -19.07100 -22.42300 -5.49400  1.000 14.45000 ? 40  LEU B N    1 
ATOM   1413 C CA   . LEU B 1 40  ? -19.32800 -22.57200 -6.91500  1.000 14.34000 ? 40  LEU B CA   1 
ATOM   1414 C C    . LEU B 1 40  ? -19.06100 -24.02700 -7.26400  1.000 17.05000 ? 40  LEU B C    1 
ATOM   1415 O O    . LEU B 1 40  ? -17.95300 -24.52400 -7.03800  1.000 18.93000 ? 40  LEU B O    1 
ATOM   1416 C CB   . LEU B 1 40  ? -18.37100 -21.65600 -7.68000  1.000 20.37000 ? 40  LEU B CB   1 
ATOM   1417 C CG   . LEU B 1 40  ? -18.51700 -21.36300 -9.16700  1.000 22.06000 ? 40  LEU B CG   1 
ATOM   1418 C CD1  . LEU B 1 40  ? -19.90900 -20.85400 -9.50100  1.000 25.14000 ? 40  LEU B CD1  1 
ATOM   1419 C CD2  . LEU B 1 40  ? -17.45700 -20.35000 -9.57700  1.000 19.67000 ? 40  LEU B CD2  1 
ATOM   1420 N N    . VAL B 1 41  ? -20.07700 -24.71900 -7.77300  1.000 15.32000 ? 41  VAL B N    1 
ATOM   1421 C CA   . VAL B 1 41  ? -19.95200 -26.10000 -8.22300  1.000 15.75000 ? 41  VAL B CA   1 
ATOM   1422 C C    . VAL B 1 41  ? -20.13500 -26.10600 -9.73000  1.000 15.80000 ? 41  VAL B C    1 
ATOM   1423 O O    . VAL B 1 41  ? -21.17100 -25.65400 -10.23800 1.000 17.69000 ? 41  VAL B O    1 
ATOM   1424 C CB   . VAL B 1 41  ? -20.96400 -27.03100 -7.53800  1.000 20.10000 ? 41  VAL B CB   1 
ATOM   1425 C CG1  . VAL B 1 41  ? -20.73100 -28.47000 -7.98500  1.000 21.46000 ? 41  VAL B CG1  1 
ATOM   1426 C CG2  . VAL B 1 41  ? -20.85900 -26.91800 -6.01400  1.000 17.64000 ? 41  VAL B CG2  1 
ATOM   1427 N N    . ILE B 1 42  ? -19.12700 -26.59900 -10.44200 1.000 14.09000 ? 42  ILE B N    1 
ATOM   1428 C CA   . ILE B 1 42  ? -19.09100 -26.56500 -11.89600 1.000 13.06000 ? 42  ILE B CA   1 
ATOM   1429 C C    . ILE B 1 42  ? -18.96800 -27.98700 -12.41700 1.000 13.11000 ? 42  ILE B C    1 
ATOM   1430 O O    . ILE B 1 42  ? -18.07900 -28.74000 -11.99800 1.000 14.35000 ? 42  ILE B O    1 
ATOM   1431 C CB   . ILE B 1 42  ? -17.93200 -25.69400 -12.40900 1.000 14.37000 ? 42  ILE B CB   1 
ATOM   1432 C CG1  . ILE B 1 42  ? -18.11700 -24.24100 -11.96900 1.000 15.70000 ? 42  ILE B CG1  1 
ATOM   1433 C CG2  . ILE B 1 42  ? -17.81500 -25.78500 -13.93100 1.000 13.82000 ? 42  ILE B CG2  1 
ATOM   1434 C CD1  . ILE B 1 42  ? -16.89600 -23.38800 -12.20000 1.000 16.80000 ? 42  ILE B CD1  1 
ATOM   1435 N N    . ASP B 1 43  ? -19.85500 -28.34400 -13.33800 1.000 13.32000 ? 43  ASP B N    1 
ATOM   1436 C CA   . ASP B 1 43  ? -19.80400 -29.58300 -14.09300 1.000 13.00000 ? 43  ASP B CA   1 
ATOM   1437 C C    . ASP B 1 43  ? -19.57600 -29.19200 -15.54600 1.000 12.95000 ? 43  ASP B C    1 
ATOM   1438 O O    . ASP B 1 43  ? -20.33300 -28.38600 -16.10100 1.000 15.34000 ? 43  ASP B O    1 
ATOM   1439 C CB   . ASP B 1 43  ? -21.13900 -30.31300 -13.94900 1.000 17.68000 ? 43  ASP B CB   1 
ATOM   1440 C CG   . ASP B 1 43  ? -21.10300 -31.72700 -14.48300 1.000 25.12000 ? 43  ASP B CG   1 
ATOM   1441 O OD1  . ASP B 1 43  ? -20.66100 -31.92300 -15.63300 1.000 28.26000 ? 43  ASP B OD1  1 
ATOM   1442 O OD2  . ASP B 1 43  ? -21.54100 -32.64400 -13.75400 1.000 33.62000 ? 43  ASP B OD2  1 
ATOM   1443 N N    . GLN B 1 44  ? -18.53200 -29.73800 -16.14900 1.000 12.63000 ? 44  GLN B N    1 
ATOM   1444 C CA   . GLN B 1 44  ? -18.12100 -29.35400 -17.49200 1.000 12.89000 ? 44  GLN B CA   1 
ATOM   1445 C C    . GLN B 1 44  ? -17.85200 -30.62500 -18.28000 1.000 13.53000 ? 44  GLN B C    1 
ATOM   1446 O O    . GLN B 1 44  ? -17.02500 -31.45300 -17.87400 1.000 13.73000 ? 44  GLN B O    1 
ATOM   1447 C CB   . GLN B 1 44  ? -16.85500 -28.49300 -17.42600 1.000 13.43000 ? 44  GLN B CB   1 
ATOM   1448 C CG   . GLN B 1 44  ? -16.16800 -28.23100 -18.75400 1.000 15.69000 ? 44  GLN B CG   1 
ATOM   1449 C CD   . GLN B 1 44  ? -14.88900 -27.43700 -18.57500 1.000 15.21000 ? 44  GLN B CD   1 
ATOM   1450 O OE1  . GLN B 1 44  ? -14.63900 -26.89100 -17.50200 1.000 17.92000 ? 44  GLN B OE1  1 
ATOM   1451 N NE2  . GLN B 1 44  ? -14.07900 -27.35600 -19.62700 1.000 17.29000 ? 44  GLN B NE2  1 
ATOM   1452 N N    . ASP B 1 45  ? -18.55000 -30.78800 -19.39500 1.000 12.93000 ? 45  ASP B N    1 
ATOM   1453 C CA   . ASP B 1 45  ? -18.35800 -31.94300 -20.26500 1.000 16.30000 ? 45  ASP B CA   1 
ATOM   1454 C C    . ASP B 1 45  ? -18.42000 -31.43400 -21.69700 1.000 15.64000 ? 45  ASP B C    1 
ATOM   1455 O O    . ASP B 1 45  ? -19.49800 -31.08600 -22.18900 1.000 15.77000 ? 45  ASP B O    1 
ATOM   1456 C CB   . ASP B 1 45  ? -19.43300 -32.99500 -20.01500 1.000 21.37000 ? 45  ASP B CB   1 
ATOM   1457 C CG   . ASP B 1 45  ? -19.18300 -34.26700 -20.79200 1.000 25.27000 ? 45  ASP B CG   1 
ATOM   1458 O OD1  . ASP B 1 45  ? -18.25300 -35.01700 -20.42300 1.000 28.66000 ? 45  ASP B OD1  1 
ATOM   1459 O OD2  . ASP B 1 45  ? -19.90400 -34.50900 -21.78000 1.000 29.26000 ? 45  ASP B OD2  1 
ATOM   1460 N N    . GLY B 1 46  ? -17.27400 -31.39400 -22.36100 1.000 16.71000 ? 46  GLY B N    1 
ATOM   1461 C CA   . GLY B 1 46  ? -17.23300 -30.80600 -23.69000 1.000 18.69000 ? 46  GLY B CA   1 
ATOM   1462 C C    . GLY B 1 46  ? -17.63800 -29.34500 -23.63000 1.000 15.51000 ? 46  GLY B C    1 
ATOM   1463 O O    . GLY B 1 46  ? -17.12600 -28.56800 -22.81900 1.000 15.89000 ? 46  GLY B O    1 
ATOM   1464 N N    . ASP B 1 47  ? -18.58900 -28.96400 -24.48500 1.000 14.80000 ? 47  ASP B N    1 
ATOM   1465 C CA   . ASP B 1 47  ? -19.11300 -27.60400 -24.49600 1.000 12.78000 ? 47  ASP B CA   1 
ATOM   1466 C C    . ASP B 1 47  ? -20.13700 -27.35200 -23.40500 1.000 13.01000 ? 47  ASP B C    1 
ATOM   1467 O O    . ASP B 1 47  ? -20.51200 -26.19400 -23.19300 1.000 12.83000 ? 47  ASP B O    1 
ATOM   1468 C CB   . ASP B 1 47  ? -19.84900 -27.33400 -25.80700 1.000 14.54000 ? 47  ASP B CB   1 
ATOM   1469 C CG   . ASP B 1 47  ? -18.93400 -27.21600 -26.98600 1.000 15.62000 ? 47  ASP B CG   1 
ATOM   1470 O OD1  . ASP B 1 47  ? -17.72700 -26.95000 -26.80500 0.000 16.14000 ? 47  ASP B OD1  1 
ATOM   1471 O OD2  . ASP B 1 47  ? -19.44900 -27.40100 -28.11400 1.000 18.03000 ? 47  ASP B OD2  1 
ATOM   1472 N N    . ASN B 1 48  ? -20.61200 -28.39900 -22.73100 1.000 12.21000 ? 48  ASN B N    1 
ATOM   1473 C CA   . ASN B 1 48  ? -21.77600 -28.29600 -21.86500 1.000 12.81000 ? 48  ASN B CA   1 
ATOM   1474 C C    . ASN B 1 48  ? -21.35200 -28.01800 -20.42600 1.000 12.61000 ? 48  ASN B C    1 
ATOM   1475 O O    . ASN B 1 48  ? -20.60400 -28.80000 -19.82200 1.000 13.23000 ? 48  ASN B O    1 
ATOM   1476 C CB   . ASN B 1 48  ? -22.62100 -29.56200 -21.96600 1.000 15.20000 ? 48  ASN B CB   1 
ATOM   1477 C CG   . ASN B 1 48  ? -23.21300 -29.75100 -23.35600 1.000 20.07000 ? 48  ASN B CG   1 
ATOM   1478 O OD1  . ASN B 1 48  ? -23.53800 -28.77900 -24.04500 1.000 20.85000 ? 48  ASN B OD1  1 
ATOM   1479 N ND2  . ASN B 1 48  ? -23.35300 -31.00300 -23.77500 1.000 28.29000 ? 48  ASN B ND2  1 
ATOM   1480 N N    . PHE B 1 49  ? -21.82900 -26.90900 -19.88500 1.000 11.27000 ? 49  PHE B N    1 
ATOM   1481 C CA   . PHE B 1 49  ? -21.53700 -26.48100 -18.52700 1.000 11.01000 ? 49  PHE B CA   1 
ATOM   1482 C C    . PHE B 1 49  ? -22.82100 -26.43800 -17.71600 1.000 12.02000 ? 49  PHE B C    1 
ATOM   1483 O O    . PHE B 1 49  ? -23.87600 -26.01100 -18.21300 1.000 12.82000 ? 49  PHE B O    1 
ATOM   1484 C CB   . PHE B 1 49  ? -20.96800 -25.05400 -18.51200 1.000 11.28000 ? 49  PHE B CB   1 
ATOM   1485 C CG   . PHE B 1 49  ? -19.50500 -24.96700 -18.83200 1.000 10.03000 ? 49  PHE B CG   1 
ATOM   1486 C CD1  . PHE B 1 49  ? -19.04700 -25.12600 -20.13700 1.000 11.48000 ? 49  PHE B CD1  1 
ATOM   1487 C CD2  . PHE B 1 49  ? -18.58100 -24.72200 -17.83000 1.000 11.85000 ? 49  PHE B CD2  1 
ATOM   1488 C CE1  . PHE B 1 49  ? -17.69100 -25.04000 -20.43300 1.000 10.78000 ? 49  PHE B CE1  1 
ATOM   1489 C CE2  . PHE B 1 49  ? -17.23200 -24.62600 -18.12400 1.000 13.50000 ? 49  PHE B CE2  1 
ATOM   1490 C CZ   . PHE B 1 49  ? -16.78900 -24.79100 -19.41700 1.000 12.13000 ? 49  PHE B CZ   1 
ATOM   1491 N N    . LYS B 1 50  ? -22.70900 -26.84800 -16.45600 1.000 12.68000 ? 50  LYS B N    1 
ATOM   1492 C CA   . LYS B 1 50  ? -23.71000 -26.59000 -15.43000 1.000 14.94000 ? 50  LYS B CA   1 
ATOM   1493 C C    . LYS B 1 50  ? -22.99000 -25.87900 -14.29200 1.000 15.19000 ? 50  LYS B C    1 
ATOM   1494 O O    . LYS B 1 50  ? -22.04400 -26.43300 -13.71600 1.000 16.60000 ? 50  LYS B O    1 
ATOM   1495 C CB   . LYS B 1 50  ? -24.32000 -27.89800 -14.92500 1.000 19.16000 ? 50  LYS B CB   1 
ATOM   1496 C CG   . LYS B 1 50  ? -24.89800 -28.77900 -16.01600 1.000 23.08000 ? 50  LYS B CG   1 
ATOM   1497 C CD   . LYS B 1 50  ? -25.71400 -29.90900 -15.41000 0.630 24.54000 ? 50  LYS B CD   1 
ATOM   1498 C CE   . LYS B 1 50  ? -26.05300 -30.96600 -16.44200 0.420 25.70000 ? 50  LYS B CE   1 
ATOM   1499 N NZ   . LYS B 1 50  ? -25.26700 -30.78400 -17.69100 1.000 31.79000 ? 50  LYS B NZ   1 
ATOM   1500 N N    . VAL B 1 51  ? -23.41000 -24.65500 -13.99200 1.000 15.91000 ? 51  VAL B N    1 
ATOM   1501 C CA   . VAL B 1 51  ? -22.77300 -23.83500 -12.96700 1.000 17.61000 ? 51  VAL B CA   1 
ATOM   1502 C C    . VAL B 1 51  ? -23.79200 -23.58500 -11.86500 1.000 17.78000 ? 51  VAL B C    1 
ATOM   1503 O O    . VAL B 1 51  ? -24.87100 -23.03400 -12.11900 1.000 19.40000 ? 51  VAL B O    1 
ATOM   1504 C CB   . VAL B 1 51  ? -22.23800 -22.51400 -13.54000 1.000 19.15000 ? 51  VAL B CB   1 
ATOM   1505 C CG1  . VAL B 1 51  ? -21.66800 -21.64500 -12.43000 1.000 21.83000 ? 51  VAL B CG1  1 
ATOM   1506 C CG2  . VAL B 1 51  ? -21.19200 -22.78500 -14.61800 1.000 17.15000 ? 51  VAL B CG2  1 
ATOM   1507 N N    . LYS B 1 52  ? -23.46100 -24.00400 -10.64900 1.000 17.34000 ? 52  LYS B N    1 
ATOM   1508 C CA   . LYS B 1 52  ? -24.36200 -23.87600 -9.51100  1.000 19.06000 ? 52  LYS B CA   1 
ATOM   1509 C C    . LYS B 1 52  ? -23.67400 -23.03700 -8.44800  1.000 21.76000 ? 52  LYS B C    1 
ATOM   1510 O O    . LYS B 1 52  ? -22.56800 -23.36900 -8.00400  1.000 18.60000 ? 52  LYS B O    1 
ATOM   1511 C CB   . LYS B 1 52  ? -24.75400 -25.25000 -8.96300  1.000 23.21000 ? 52  LYS B CB   1 
ATOM   1512 C CG   . LYS B 1 52  ? -25.95800 -25.86600 -9.67200  1.000 29.30000 ? 52  LYS B CG   1 
ATOM   1513 C CD   . LYS B 1 52  ? -25.95500 -27.38600 -9.59900  1.000 29.33000 ? 52  LYS B CD   1 
ATOM   1514 C CE   . LYS B 1 52  ? -26.64500 -28.00500 -10.80700 1.000 31.85000 ? 52  LYS B CE   1 
ATOM   1515 N NZ   . LYS B 1 52  ? -26.08600 -27.49600 -12.08900 1.000 30.14000 ? 52  LYS B NZ   1 
ATOM   1516 N N    . CYS B 1 53  ? -24.31300 -21.94300 -8.06200  1.000 22.71000 ? 53  CYS B N    1 
ATOM   1517 C CA   . CYS B 1 53  ? -23.83200 -21.11400 -6.97400  1.000 26.80000 ? 53  CYS B CA   1 
ATOM   1518 C C    . CYS B 1 53  ? -24.68800 -21.41400 -5.76000  1.000 26.57000 ? 53  CYS B C    1 
ATOM   1519 O O    . CYS B 1 53  ? -25.90700 -21.20400 -5.78700  1.000 29.01000 ? 53  CYS B O    1 
ATOM   1520 C CB   . CYS B 1 53  ? -23.92300 -19.63000 -7.30800  1.000 31.05000 ? 53  CYS B CB   1 
ATOM   1521 S SG   . CYS B 1 53  ? -23.51200 -18.58800 -5.88300  1.000 43.51000 ? 53  CYS B SG   1 
ATOM   1522 N N    . THR B 1 54  ? -24.05600 -21.91000 -4.70800  1.000 27.80000 ? 54  THR B N    1 
ATOM   1523 C CA   . THR B 1 54  ? -24.73400 -22.20800 -3.46200  1.000 28.25000 ? 54  THR B CA   1 
ATOM   1524 C C    . THR B 1 54  ? -24.30700 -21.19600 -2.40900  1.000 29.57000 ? 54  THR B C    1 
ATOM   1525 O O    . THR B 1 54  ? -23.11000 -20.93900 -2.22500  1.000 26.25000 ? 54  THR B O    1 
ATOM   1526 C CB   . THR B 1 54  ? -24.42100 -23.63300 -3.00500  1.000 32.08000 ? 54  THR B CB   1 
ATOM   1527 O OG1  . THR B 1 54  ? -23.00200 -23.80200 -2.90800  1.000 32.18000 ? 54  THR B OG1  1 
ATOM   1528 C CG2  . THR B 1 54  ? -24.98100 -24.64400 -4.00200  1.000 32.41000 ? 54  THR B CG2  1 
ATOM   1529 N N    . SER B 1 55  ? -25.29500 -20.59200 -1.76000  1.000 30.60000 ? 55  SER B N    1 
ATOM   1530 C CA   . SER B 1 55  ? -25.08600 -19.75400 -0.59300  1.000 27.03000 ? 55  SER B CA   1 
ATOM   1531 C C    . SER B 1 55  ? -26.29800 -19.94500 0.30000   1.000 27.41000 ? 55  SER B C    1 
ATOM   1532 O O    . SER B 1 55  ? -27.27000 -20.60300 -0.07800  1.000 27.92000 ? 55  SER B O    1 
ATOM   1533 C CB   . SER B 1 55  ? -24.90300 -18.28100 -0.97300  1.000 30.28000 ? 55  SER B CB   1 
ATOM   1534 O OG   . SER B 1 55  ? -26.15200 -17.66700 -1.24300  1.000 31.30000 ? 55  SER B OG   1 
ATOM   1535 N N    . THR B 1 56  ? -26.23800 -19.36500 1.49800   1.000 26.72000 ? 56  THR B N    1 
ATOM   1536 C CA   . THR B 1 56  ? -27.34200 -19.54000 2.43600   1.000 26.25000 ? 56  THR B CA   1 
ATOM   1537 C C    . THR B 1 56  ? -28.67300 -19.12500 1.82100   1.000 25.21000 ? 56  THR B C    1 
ATOM   1538 O O    . THR B 1 56  ? -29.69900 -19.77600 2.04700   1.000 27.74000 ? 56  THR B O    1 
ATOM   1539 C CB   . THR B 1 56  ? -27.08000 -18.75600 3.72200   1.000 26.87000 ? 56  THR B CB   1 
ATOM   1540 O OG1  . THR B 1 56  ? -25.85800 -19.20600 4.32100   1.000 25.95000 ? 56  THR B OG1  1 
ATOM   1541 C CG2  . THR B 1 56  ? -28.22500 -18.96500 4.70100   1.000 25.25000 ? 56  THR B CG2  1 
ATOM   1542 N N    . PHE B 1 57  ? -28.67800 -18.05100 1.02800   1.000 27.48000 ? 57  PHE B N    1 
ATOM   1543 C CA   . PHE B 1 57  ? -29.92300 -17.46300 0.55500   1.000 29.17000 ? 57  PHE B CA   1 
ATOM   1544 C C    . PHE B 1 57  ? -30.09700 -17.44700 -0.95900  1.000 31.97000 ? 57  PHE B C    1 
ATOM   1545 O O    . PHE B 1 57  ? -31.18500 -17.09000 -1.42700  1.000 32.10000 ? 57  PHE B O    1 
ATOM   1546 C CB   . PHE B 1 57  ? -30.07700 -16.02900 1.08700   1.000 29.47000 ? 57  PHE B CB   1 
ATOM   1547 C CG   . PHE B 1 57  ? -29.87700 -15.90900 2.56900   1.000 25.74000 ? 57  PHE B CG   1 
ATOM   1548 C CD1  . PHE B 1 57  ? -30.88500 -16.27400 3.44600   1.000 27.30000 ? 57  PHE B CD1  1 
ATOM   1549 C CD2  . PHE B 1 57  ? -28.68300 -15.43400 3.08700   1.000 26.89000 ? 57  PHE B CD2  1 
ATOM   1550 C CE1  . PHE B 1 57  ? -30.70900 -16.16700 4.81400   1.000 26.93000 ? 57  PHE B CE1  1 
ATOM   1551 C CE2  . PHE B 1 57  ? -28.49700 -15.32200 4.45300   1.000 29.01000 ? 57  PHE B CE2  1 
ATOM   1552 C CZ   . PHE B 1 57  ? -29.51200 -15.69000 5.31900   1.000 29.45000 ? 57  PHE B CZ   1 
ATOM   1553 N N    . TRP B 1 58  ? -29.07900 -17.81700 -1.73500  1.000 31.37000 ? 58  TRP B N    1 
ATOM   1554 C CA   . TRP B 1 58  ? -29.14400 -17.72200 -3.18800  1.000 33.31000 ? 58  TRP B CA   1 
ATOM   1555 C C    . TRP B 1 58  ? -28.70300 -19.02700 -3.83100  1.000 33.10000 ? 58  TRP B C    1 
ATOM   1556 O O    . TRP B 1 58  ? -27.77800 -19.69000 -3.35000  1.000 31.26000 ? 58  TRP B O    1 
ATOM   1557 C CB   . TRP B 1 58  ? -28.24900 -16.59800 -3.71600  1.000 34.22000 ? 58  TRP B CB   1 
ATOM   1558 C CG   . TRP B 1 58  ? -28.93100 -15.27600 -3.79100  1.000 34.67000 ? 58  TRP B CG   1 
ATOM   1559 C CD1  . TRP B 1 58  ? -29.70500 -14.80600 -4.81500  1.000 33.18000 ? 58  TRP B CD1  1 
ATOM   1560 C CD2  . TRP B 1 58  ? -28.90100 -14.24300 -2.80200  1.000 34.49000 ? 58  TRP B CD2  1 
ATOM   1561 N NE1  . TRP B 1 58  ? -30.15800 -13.54200 -4.52100  1.000 35.38000 ? 58  TRP B NE1  1 
ATOM   1562 C CE2  . TRP B 1 58  ? -29.67900 -13.17400 -3.29000  1.000 33.60000 ? 58  TRP B CE2  1 
ATOM   1563 C CE3  . TRP B 1 58  ? -28.28900 -14.11700 -1.55100  1.000 32.30000 ? 58  TRP B CE3  1 
ATOM   1564 C CZ2  . TRP B 1 58  ? -29.86300 -11.99400 -2.56900  1.000 34.57000 ? 58  TRP B CZ2  1 
ATOM   1565 C CZ3  . TRP B 1 58  ? -28.47300 -12.94400 -0.83700  1.000 27.94000 ? 58  TRP B CZ3  1 
ATOM   1566 C CH2  . TRP B 1 58  ? -29.25400 -11.90000 -1.34700  1.000 28.74000 ? 58  TRP B CH2  1 
ATOM   1567 N N    . ASN B 1 59  ? -29.36600 -19.37500 -4.94000  1.000 36.03000 ? 59  ASN B N    1 
ATOM   1568 C CA   . ASN B 1 59  ? -28.99300 -20.50600 -5.79400  1.000 34.40000 ? 59  ASN B CA   1 
ATOM   1569 C C    . ASN B 1 59  ? -28.96900 -19.99800 -7.23600  1.000 35.58000 ? 59  ASN B C    1 
ATOM   1570 O O    . ASN B 1 59  ? -29.89800 -20.24200 -8.01000  1.000 37.90000 ? 59  ASN B O    1 
ATOM   1571 C CB   . ASN B 1 59  ? -29.95300 -21.68600 -5.62000  1.000 33.81000 ? 59  ASN B CB   1 
ATOM   1572 C CG   . ASN B 1 59  ? -29.84200 -22.33200 -4.25300  1.000 38.29000 ? 59  ASN B CG   1 
ATOM   1573 O OD1  . ASN B 1 59  ? -29.01600 -21.93800 -3.43000  1.000 40.12000 ? 59  ASN B OD1  1 
ATOM   1574 N ND2  . ASN B 1 59  ? -30.67000 -23.34100 -4.00700  0.000 36.06000 ? 59  ASN B ND2  1 
ATOM   1575 N N    . TYR B 1 60  ? -27.90500 -19.27700 -7.58800  1.000 30.48000 ? 60  TYR B N    1 
ATOM   1576 C CA   . TYR B 1 60  ? -27.71400 -18.79000 -8.95300  1.000 27.09000 ? 60  TYR B CA   1 
ATOM   1577 C C    . TYR B 1 60  ? -27.21300 -19.96100 -9.78700  1.000 27.23000 ? 60  TYR B C    1 
ATOM   1578 O O    . TYR B 1 60  ? -26.04700 -20.35400 -9.69300  1.000 28.08000 ? 60  TYR B O    1 
ATOM   1579 C CB   . TYR B 1 60  ? -26.72600 -17.63000 -8.96700  1.000 28.42000 ? 60  TYR B CB   1 
ATOM   1580 C CG   . TYR B 1 60  ? -26.72800 -16.82800 -10.25100 1.000 26.91000 ? 60  TYR B CG   1 
ATOM   1581 C CD1  . TYR B 1 60  ? -27.72800 -15.90000 -10.51500 1.000 25.53000 ? 60  TYR B CD1  1 
ATOM   1582 C CD2  . TYR B 1 60  ? -25.72300 -16.99500 -11.19700 1.000 26.80000 ? 60  TYR B CD2  1 
ATOM   1583 C CE1  . TYR B 1 60  ? -27.73100 -15.16100 -11.68800 1.000 25.46000 ? 60  TYR B CE1  1 
ATOM   1584 C CE2  . TYR B 1 60  ? -25.71500 -16.26300 -12.37400 1.000 27.18000 ? 60  TYR B CE2  1 
ATOM   1585 C CZ   . TYR B 1 60  ? -26.72000 -15.34600 -12.61300 1.000 24.24000 ? 60  TYR B CZ   1 
ATOM   1586 O OH   . TYR B 1 60  ? -26.72400 -14.61600 -13.78100 1.000 24.76000 ? 60  TYR B OH   1 
ATOM   1587 N N    . ASP B 1 61  ? -28.09700 -20.53100 -10.60400 1.000 24.65000 ? 61  ASP B N    1 
ATOM   1588 C CA   . ASP B 1 61  ? -27.82200 -21.75700 -11.34100 1.000 23.80000 ? 61  ASP B CA   1 
ATOM   1589 C C    . ASP B 1 61  ? -28.04200 -21.51200 -12.82300 1.000 20.81000 ? 61  ASP B C    1 
ATOM   1590 O O    . ASP B 1 61  ? -29.12600 -21.08000 -13.22400 1.000 23.24000 ? 61  ASP B O    1 
ATOM   1591 C CB   . ASP B 1 61  ? -28.76500 -22.87100 -10.88500 1.000 23.72000 ? 61  ASP B CB   1 
ATOM   1592 C CG   . ASP B 1 61  ? -28.48300 -23.32800 -9.47900  1.000 29.32000 ? 61  ASP B CG   1 
ATOM   1593 O OD1  . ASP B 1 61  ? -29.23000 -24.19700 -8.98000  1.000 35.83000 ? 61  ASP B OD1  1 
ATOM   1594 O OD2  . ASP B 1 61  ? -27.51300 -22.81900 -8.87400  1.000 26.28000 ? 61  ASP B OD2  1 
ATOM   1595 N N    . VAL B 1 62  ? -27.02800 -21.80500 -13.63700 1.000 18.02000 ? 62  VAL B N    1 
ATOM   1596 C CA   . VAL B 1 62  ? -27.09100 -21.53400 -15.07100 1.000 17.56000 ? 62  VAL B CA   1 
ATOM   1597 C C    . VAL B 1 62  ? -26.43500 -22.67900 -15.82800 1.000 17.03000 ? 62  VAL B C    1 
ATOM   1598 O O    . VAL B 1 62  ? -25.33900 -23.12900 -15.47100 1.000 17.81000 ? 62  VAL B O    1 
ATOM   1599 C CB   . VAL B 1 62  ? -26.44400 -20.18100 -15.42800 1.000 20.44000 ? 62  VAL B CB   1 
ATOM   1600 C CG1  . VAL B 1 62  ? -24.96100 -20.19200 -15.11000 1.000 25.01000 ? 62  VAL B CG1  1 
ATOM   1601 C CG2  . VAL B 1 62  ? -26.69500 -19.83000 -16.89000 1.000 21.18000 ? 62  VAL B CG2  1 
ATOM   1602 N N    . ASP B 1 63  ? -27.11800 -23.16100 -16.86000 1.000 15.37000 ? 63  ASP B N    1 
ATOM   1603 C CA   . ASP B 1 63  ? -26.59600 -24.16700 -17.76800 1.000 15.81000 ? 63  ASP B CA   1 
ATOM   1604 C C    . ASP B 1 63  ? -26.42500 -23.52700 -19.13700 1.000 13.94000 ? 63  ASP B C    1 
ATOM   1605 O O    . ASP B 1 63  ? -27.26600 -22.72900 -19.56900 1.000 15.72000 ? 63  ASP B O    1 
ATOM   1606 C CB   . ASP B 1 63  ? -27.55700 -25.35500 -17.89500 1.000 21.14000 ? 63  ASP B CB   1 
ATOM   1607 C CG   . ASP B 1 63  ? -27.72800 -26.12600 -16.59300 1.000 23.21000 ? 63  ASP B CG   1 
ATOM   1608 O OD1  . ASP B 1 63  ? -27.04500 -25.80500 -15.60100 1.000 22.85000 ? 63  ASP B OD1  1 
ATOM   1609 O OD2  . ASP B 1 63  ? -28.56100 -27.06000 -16.56700 1.000 30.48000 ? 63  ASP B OD2  1 
ATOM   1610 N N    . PHE B 1 64  ? -25.34100 -23.86400 -19.82400 1.000 11.75000 ? 64  PHE B N    1 
ATOM   1611 C CA   . PHE B 1 64  ? -25.08900 -23.28800 -21.13300 1.000 11.73000 ? 64  PHE B CA   1 
ATOM   1612 C C    . PHE B 1 64  ? -24.19300 -24.21300 -21.93100 1.000 11.03000 ? 64  PHE B C    1 
ATOM   1613 O O    . PHE B 1 64  ? -23.54200 -25.12000 -21.39000 1.000 12.22000 ? 64  PHE B O    1 
ATOM   1614 C CB   . PHE B 1 64  ? -24.49800 -21.87200 -21.04200 1.000 12.66000 ? 64  PHE B CB   1 
ATOM   1615 C CG   . PHE B 1 64  ? -23.19500 -21.80500 -20.29800 1.000 11.89000 ? 64  PHE B CG   1 
ATOM   1616 C CD1  . PHE B 1 64  ? -21.99900 -22.12200 -20.92500 1.000 12.25000 ? 64  PHE B CD1  1 
ATOM   1617 C CD2  . PHE B 1 64  ? -23.17000 -21.41900 -18.96800 1.000 12.38000 ? 64  PHE B CD2  1 
ATOM   1618 C CE1  . PHE B 1 64  ? -20.80400 -22.06400 -20.23600 1.000 12.07000 ? 64  PHE B CE1  1 
ATOM   1619 C CE2  . PHE B 1 64  ? -21.97300 -21.35100 -18.28100 1.000 13.01000 ? 64  PHE B CE2  1 
ATOM   1620 C CZ   . PHE B 1 64  ? -20.78900 -21.68000 -18.91900 1.000 12.17000 ? 64  PHE B CZ   1 
ATOM   1621 N N    . THR B 1 65  ? -24.17100 -23.96800 -23.24000 1.000 11.48000 ? 65  THR B N    1 
ATOM   1622 C CA   . THR B 1 65  ? -23.28300 -24.64400 -24.17400 1.000 10.96000 ? 65  THR B CA   1 
ATOM   1623 C C    . THR B 1 65  ? -22.34700 -23.60600 -24.77900 1.000 10.81000 ? 65  THR B C    1 
ATOM   1624 O O    . THR B 1 65  ? -22.81000 -22.58200 -25.30000 1.000 9.76000  ? 65  THR B O    1 
ATOM   1625 C CB   . THR B 1 65  ? -24.09900 -25.32300 -25.28100 1.000 13.60000 ? 65  THR B CB   1 
ATOM   1626 O OG1  . THR B 1 65  ? -24.97800 -26.30300 -24.69300 1.000 16.41000 ? 65  THR B OG1  1 
ATOM   1627 C CG2  . THR B 1 65  ? -23.18300 -25.99400 -26.29600 1.000 13.07000 ? 65  THR B CG2  1 
ATOM   1628 N N    . VAL B 1 66  ? -21.03900 -23.85700 -24.70300 1.000 10.26000 ? 66  VAL B N    1 
ATOM   1629 C CA   . VAL B 1 66  ? -20.07500 -22.92300 -25.26300 1.000 8.99000  ? 66  VAL B CA   1 
ATOM   1630 C C    . VAL B 1 66  ? -20.39900 -22.69700 -26.72800 1.000 9.15000  ? 66  VAL B C    1 
ATOM   1631 O O    . VAL B 1 66  ? -20.67200 -23.64900 -27.46600 1.000 10.55000 ? 66  VAL B O    1 
ATOM   1632 C CB   . VAL B 1 66  ? -18.65200 -23.47500 -25.06700 1.000 10.13000 ? 66  VAL B CB   1 
ATOM   1633 C CG1  . VAL B 1 66  ? -17.65800 -22.71300 -25.92900 1.000 12.51000 ? 66  VAL B CG1  1 
ATOM   1634 C CG2  . VAL B 1 66  ? -18.25900 -23.41800 -23.59200 1.000 13.90000 ? 66  VAL B CG2  1 
ATOM   1635 N N    . GLY B 1 67  ? -20.39800 -21.43300 -27.14700 1.000 8.39000  ? 67  GLY B N    1 
ATOM   1636 C CA   . GLY B 1 67  ? -20.62700 -21.07700 -28.53300 1.000 9.60000  ? 67  GLY B CA   1 
ATOM   1637 C C    . GLY B 1 67  ? -22.07300 -20.90600 -28.94700 1.000 8.62000  ? 67  GLY B C    1 
ATOM   1638 O O    . GLY B 1 67  ? -22.31600 -20.59800 -30.12300 1.000 9.22000  ? 67  GLY B O    1 
ATOM   1639 N N    . VAL B 1 68  ? -23.03500 -21.09900 -28.03500 1.000 8.57000  ? 68  VAL B N    1 
ATOM   1640 C CA   . VAL B 1 68  ? -24.46200 -21.06400 -28.35000 1.000 9.09000  ? 68  VAL B CA   1 
ATOM   1641 C C    . VAL B 1 68  ? -25.11300 -19.96000 -27.51900 1.000 8.12000  ? 68  VAL B C    1 
ATOM   1642 O O    . VAL B 1 68  ? -25.18800 -20.06100 -26.28400 1.000 8.73000  ? 68  VAL B O    1 
ATOM   1643 C CB   . VAL B 1 68  ? -25.13100 -22.41800 -28.07500 1.000 10.27000 ? 68  VAL B CB   1 
ATOM   1644 C CG1  . VAL B 1 68  ? -26.62700 -22.35000 -28.34300 1.000 12.78000 ? 68  VAL B CG1  1 
ATOM   1645 C CG2  . VAL B 1 68  ? -24.47100 -23.51600 -28.89800 1.000 13.01000 ? 68  VAL B CG2  1 
ATOM   1646 N N    . GLU B 1 69  ? -25.60200 -18.91800 -28.17500 1.000 8.79000  ? 69  GLU B N    1 
ATOM   1647 C CA   . GLU B 1 69  ? -26.28400 -17.85000 -27.45700 1.000 9.52000  ? 69  GLU B CA   1 
ATOM   1648 C C    . GLU B 1 69  ? -27.50900 -18.40000 -26.73800 1.000 10.38000 ? 69  GLU B C    1 
ATOM   1649 O O    . GLU B 1 69  ? -28.20100 -19.28800 -27.24400 1.000 10.89000 ? 69  GLU B O    1 
ATOM   1650 C CB   . GLU B 1 69  ? -26.68400 -16.75300 -28.44000 1.000 10.78000 ? 69  GLU B CB   1 
ATOM   1651 C CG   . GLU B 1 69  ? -27.23500 -15.50400 -27.77500 1.000 13.10000 ? 69  GLU B CG   1 
ATOM   1652 C CD   . GLU B 1 69  ? -27.65800 -14.47400 -28.79800 1.000 17.97000 ? 69  GLU B CD   1 
ATOM   1653 O OE1  . GLU B 1 69  ? -28.65700 -14.72400 -29.49900 1.000 19.99000 ? 69  GLU B OE1  1 
ATOM   1654 O OE2  . GLU B 1 69  ? -26.98400 -13.43300 -28.90400 1.000 23.69000 ? 69  GLU B OE2  1 
ATOM   1655 N N    . PHE B 1 70  ? -27.75700 -17.88900 -25.52800 1.000 9.54000  ? 70  PHE B N    1 
ATOM   1656 C CA   . PHE B 1 70  ? -28.91100 -18.31900 -24.74100 1.000 11.54000 ? 70  PHE B CA   1 
ATOM   1657 C C    . PHE B 1 70  ? -29.60700 -17.13600 -24.08500 1.000 12.49000 ? 70  PHE B C    1 
ATOM   1658 O O    . PHE B 1 70  ? -28.98300 -16.13700 -23.71800 1.000 13.09000 ? 70  PHE B O    1 
ATOM   1659 C CB   . PHE B 1 70  ? -28.57900 -19.43300 -23.71800 1.000 13.07000 ? 70  PHE B CB   1 
ATOM   1660 C CG   . PHE B 1 70  ? -27.51000 -19.07700 -22.71200 1.000 13.59000 ? 70  PHE B CG   1 
ATOM   1661 C CD1  . PHE B 1 70  ? -26.17000 -19.05800 -23.06700 1.000 12.89000 ? 70  PHE B CD1  1 
ATOM   1662 C CD2  . PHE B 1 70  ? -27.84200 -18.82800 -21.37900 1.000 15.52000 ? 70  PHE B CD2  1 
ATOM   1663 C CE1  . PHE B 1 70  ? -25.18600 -18.76500 -22.12300 1.000 13.10000 ? 70  PHE B CE1  1 
ATOM   1664 C CE2  . PHE B 1 70  ? -26.85900 -18.53400 -20.44000 1.000 15.21000 ? 70  PHE B CE2  1 
ATOM   1665 C CZ   . PHE B 1 70  ? -25.53700 -18.50600 -20.81000 1.000 17.07000 ? 70  PHE B CZ   1 
ATOM   1666 N N    . ASP B 1 71  ? -30.92800 -17.25900 -23.95800 1.000 13.90000 ? 71  ASP B N    1 
ATOM   1667 C CA   . ASP B 1 71  ? -31.70400 -16.26600 -23.23300 1.000 16.54000 ? 71  ASP B CA   1 
ATOM   1668 C C    . ASP B 1 71  ? -31.52200 -16.48400 -21.74700 1.000 15.72000 ? 71  ASP B C    1 
ATOM   1669 O O    . ASP B 1 71  ? -31.59900 -17.61400 -21.25400 1.000 18.84000 ? 71  ASP B O    1 
ATOM   1670 C CB   . ASP B 1 71  ? -33.18300 -16.37800 -23.58200 1.000 19.54000 ? 71  ASP B CB   1 
ATOM   1671 C CG   . ASP B 1 71  ? -33.48800 -15.81900 -24.94400 1.000 18.03000 ? 71  ASP B CG   1 
ATOM   1672 O OD1  . ASP B 1 71  ? -33.26200 -14.61400 -25.16700 1.000 17.98000 ? 71  ASP B OD1  1 
ATOM   1673 O OD2  . ASP B 1 71  ? -33.92200 -16.60400 -25.81500 1.000 27.01000 ? 71  ASP B OD2  1 
ATOM   1674 N N    . GLU B 1 72  ? -31.27500 -15.39500 -21.04100 1.000 17.53000 ? 72  GLU B N    1 
ATOM   1675 C CA   . GLU B 1 72  ? -31.13300 -15.40700 -19.60300 1.000 17.68000 ? 72  GLU B CA   1 
ATOM   1676 C C    . GLU B 1 72  ? -32.08000 -14.36600 -19.04100 1.000 15.66000 ? 72  GLU B C    1 
ATOM   1677 O O    . GLU B 1 72  ? -32.17100 -13.25100 -19.56400 1.000 15.11000 ? 72  GLU B O    1 
ATOM   1678 C CB   . GLU B 1 72  ? -29.70700 -15.02800 -19.25100 1.000 21.23000 ? 72  GLU B CB   1 
ATOM   1679 C CG   . GLU B 1 72  ? -29.26500 -15.45900 -17.90900 1.000 23.72000 ? 72  GLU B CG   1 
ATOM   1680 C CD   . GLU B 1 72  ? -27.79600 -15.73900 -17.91300 1.000 27.68000 ? 72  GLU B CD   1 
ATOM   1681 O OE1  . GLU B 1 72  ? -27.04400 -14.92700 -18.50800 1.000 20.23000 ? 72  GLU B OE1  1 
ATOM   1682 O OE2  . GLU B 1 72  ? -27.40400 -16.78600 -17.36000 1.000 26.52000 ? 72  GLU B OE2  1 
ATOM   1683 N N    . TYR B 1 73  ? -32.81300 -14.75200 -18.00800 1.000 16.96000 ? 73  TYR B N    1 
ATOM   1684 C CA   . TYR B 1 73  ? -33.56700 -13.82200 -17.18800 1.000 12.44000 ? 73  TYR B CA   1 
ATOM   1685 C C    . TYR B 1 73  ? -32.99200 -13.97600 -15.79500 1.000 15.78000 ? 73  TYR B C    1 
ATOM   1686 O O    . TYR B 1 73  ? -33.04900 -15.06300 -15.21400 1.000 17.76000 ? 73  TYR B O    1 
ATOM   1687 C CB   . TYR B 1 73  ? -35.05800 -14.15500 -17.22400 1.000 14.75000 ? 73  TYR B CB   1 
ATOM   1688 C CG   . TYR B 1 73  ? -35.62500 -14.04500 -18.62400 1.000 17.98000 ? 73  TYR B CG   1 
ATOM   1689 C CD1  . TYR B 1 73  ? -35.57400 -15.11800 -19.50100 1.000 19.52000 ? 73  TYR B CD1  1 
ATOM   1690 C CD2  . TYR B 1 73  ? -36.18500 -12.86300 -19.06800 1.000 17.33000 ? 73  TYR B CD2  1 
ATOM   1691 C CE1  . TYR B 1 73  ? -36.07600 -15.01700 -20.78500 1.000 18.08000 ? 73  TYR B CE1  1 
ATOM   1692 C CE2  . TYR B 1 73  ? -36.70300 -12.75400 -20.34100 1.000 21.41000 ? 73  TYR B CE2  1 
ATOM   1693 C CZ   . TYR B 1 73  ? -36.64200 -13.83700 -21.19200 1.000 20.37000 ? 73  TYR B CZ   1 
ATOM   1694 O OH   . TYR B 1 73  ? -37.15200 -13.72300 -22.46800 1.000 28.47000 ? 73  TYR B OH   1 
ATOM   1695 N N    . THR B 1 74  ? -32.37100 -12.91400 -15.29300 1.000 13.59000 ? 74  THR B N    1 
ATOM   1696 C CA   . THR B 1 74  ? -31.62000 -12.97100 -14.04100 1.000 11.64000 ? 74  THR B CA   1 
ATOM   1697 C C    . THR B 1 74  ? -32.57700 -12.79900 -12.85000 1.000 12.07000 ? 74  THR B C    1 
ATOM   1698 O O    . THR B 1 74  ? -32.47700 -11.87200 -12.04700 1.000 12.06000 ? 74  THR B O    1 
ATOM   1699 C CB   . THR B 1 74  ? -30.53000 -11.90900 -14.09800 1.000 10.91000 ? 74  THR B CB   1 
ATOM   1700 O OG1  . THR B 1 74  ? -31.13200 -10.65300 -14.43700 1.000 11.63000 ? 74  THR B OG1  1 
ATOM   1701 C CG2  . THR B 1 74  ? -29.47300 -12.26100 -15.15200 1.000 12.61000 ? 74  THR B CG2  1 
ATOM   1702 N N    . LYS B 1 75  ? -33.52500 -13.74700 -12.75400 1.000 12.18000 ? 75  LYS B N    1 
ATOM   1703 C CA   . LYS B 1 75  ? -34.70400 -13.56800 -11.90300 1.000 13.03000 ? 75  LYS B CA   1 
ATOM   1704 C C    . LYS B 1 75  ? -34.33200 -13.34800 -10.44400 1.000 14.61000 ? 75  LYS B C    1 
ATOM   1705 O O    . LYS B 1 75  ? -35.01600 -12.61000 -9.72800  1.000 17.16000 ? 75  LYS B O    1 
ATOM   1706 C CB   . LYS B 1 75  ? -35.62700 -14.78800 -12.00900 1.000 13.04000 ? 75  LYS B CB   1 
ATOM   1707 C CG   . LYS B 1 75  ? -36.16400 -15.07800 -13.40200 1.000 14.05000 ? 75  LYS B CG   1 
ATOM   1708 C CD   . LYS B 1 75  ? -36.84200 -13.86600 -14.03000 1.000 14.30000 ? 75  LYS B CD   1 
ATOM   1709 C CE   . LYS B 1 75  ? -38.12500 -13.48500 -13.31500 1.000 14.86000 ? 75  LYS B CE   1 
ATOM   1710 N NZ   . LYS B 1 75  ? -38.76600 -12.31800 -13.97000 1.000 14.26000 ? 75  LYS B NZ   1 
ATOM   1711 N N    . SER B 1 76  ? -33.28000 -14.00400 -9.97700  1.000 15.04000 ? 76  SER B N    1 
ATOM   1712 C CA   . SER B 1 76  ? -32.87900 -13.90900 -8.57800  1.000 19.64000 ? 76  SER B CA   1 
ATOM   1713 C C    . SER B 1 76  ? -31.85700 -12.80700 -8.33400  1.000 17.62000 ? 76  SER B C    1 
ATOM   1714 O O    . SER B 1 76  ? -31.49000 -12.56000 -7.17900  1.000 20.21000 ? 76  SER B O    1 
ATOM   1715 C CB   . SER B 1 76  ? -32.31800 -15.25000 -8.09700  0.000 19.94000 ? 76  SER B CB   1 
ATOM   1716 O OG   . SER B 1 76  ? -31.04600 -15.49700 -8.67000  1.000 24.91000 ? 76  SER B OG   1 
ATOM   1717 N N    . LEU B 1 77  ? -31.39500 -12.14700 -9.39600  1.000 14.95000 ? 77  LEU B N    1 
ATOM   1718 C CA   . LEU B 1 77  ? -30.42800 -11.06100 -9.30600  1.000 14.23000 ? 77  LEU B CA   1 
ATOM   1719 C C    . LEU B 1 77  ? -31.12900 -9.73700  -9.60500  1.000 14.08000 ? 77  LEU B C    1 
ATOM   1720 O O    . LEU B 1 77  ? -31.94300 -9.26800  -8.80100  1.000 16.17000 ? 77  LEU B O    1 
ATOM   1721 C CB   . LEU B 1 77  ? -29.27000 -11.33900 -10.26400 1.000 17.15000 ? 77  LEU B CB   1 
ATOM   1722 C CG   . LEU B 1 77  ? -27.96300 -10.56200 -10.15700 1.000 15.28000 ? 77  LEU B CG   1 
ATOM   1723 C CD1  . LEU B 1 77  ? -27.35700 -10.65200 -8.75600  1.000 20.50000 ? 77  LEU B CD1  1 
ATOM   1724 C CD2  . LEU B 1 77  ? -26.98800 -11.05400 -11.22100 1.000 18.19000 ? 77  LEU B CD2  1 
ATOM   1725 N N    . ASP B 1 78  ? -30.85900 -9.13400  -10.76600 1.000 12.38000 ? 78  ASP B N    1 
ATOM   1726 C CA   . ASP B 1 78  ? -31.43000 -7.83900  -11.11400 1.000 11.16000 ? 78  ASP B CA   1 
ATOM   1727 C C    . ASP B 1 78  ? -32.67700 -7.94400  -11.97600 1.000 10.75000 ? 78  ASP B C    1 
ATOM   1728 O O    . ASP B 1 78  ? -33.24600 -6.91300  -12.34200 1.000 11.67000 ? 78  ASP B O    1 
ATOM   1729 C CB   . ASP B 1 78  ? -30.39000 -6.94000  -11.80700 1.000 12.08000 ? 78  ASP B CB   1 
ATOM   1730 C CG   . ASP B 1 78  ? -29.83900 -7.54800  -13.08800 1.000 10.75000 ? 78  ASP B CG   1 
ATOM   1731 O OD1  . ASP B 1 78  ? -29.49900 -8.75300  -13.07300 1.000 10.37000 ? 78  ASP B OD1  1 
ATOM   1732 O OD2  . ASP B 1 78  ? -29.73500 -6.80900  -14.09100 1.000 10.97000 ? 78  ASP B OD2  1 
ATOM   1733 N N    . ASN B 1 79  ? -33.12000 -9.15700  -12.29800 1.000 10.33000 ? 79  ASN B N    1 
ATOM   1734 C CA   . ASN B 1 79  ? -34.39800 -9.36700  -12.97800 1.000 10.84000 ? 79  ASN B CA   1 
ATOM   1735 C C    . ASN B 1 79  ? -34.44100 -8.70700  -14.35800 1.000 10.15000 ? 79  ASN B C    1 
ATOM   1736 O O    . ASN B 1 79  ? -35.38700 -7.99100  -14.70100 1.000 12.11000 ? 79  ASN B O    1 
ATOM   1737 C CB   . ASN B 1 79  ? -35.59800 -8.94500  -12.12000 1.000 11.97000 ? 79  ASN B CB   1 
ATOM   1738 C CG   . ASN B 1 79  ? -36.90300 -9.43100  -12.69200 1.000 12.71000 ? 79  ASN B CG   1 
ATOM   1739 O OD1  . ASN B 1 79  ? -36.95800 -10.48200 -13.33000 1.000 14.68000 ? 79  ASN B OD1  1 
ATOM   1740 N ND2  . ASN B 1 79  ? -37.96800 -8.66200  -12.48300 1.000 12.83000 ? 79  ASN B ND2  1 
ATOM   1741 N N    . ARG B 1 80  ? -33.41200 -8.96000  -15.16100 1.000 10.21000 ? 80  ARG B N    1 
ATOM   1742 C CA   . ARG B 1 80  ? -33.33000 -8.43300  -16.51400 1.000 10.06000 ? 80  ARG B CA   1 
ATOM   1743 C C    . ARG B 1 80  ? -33.17300 -9.56000  -17.52000 1.000 10.30000 ? 80  ARG B C    1 
ATOM   1744 O O    . ARG B 1 80  ? -32.65800 -10.63500 -17.20600 1.000 12.62000 ? 80  ARG B O    1 
ATOM   1745 C CB   . ARG B 1 80  ? -32.16400 -7.45100  -16.68200 1.000 11.12000 ? 80  ARG B CB   1 
ATOM   1746 C CG   . ARG B 1 80  ? -32.37300 -6.12700  -15.96700 1.000 11.10000 ? 80  ARG B CG   1 
ATOM   1747 C CD   . ARG B 1 80  ? -31.29800 -5.13400  -16.34800 1.000 12.31000 ? 80  ARG B CD   1 
ATOM   1748 N NE   . ARG B 1 80  ? -31.58100 -3.79000  -15.85000 1.000 11.89000 ? 80  ARG B NE   1 
ATOM   1749 C CZ   . ARG B 1 80  ? -31.11400 -3.30100  -14.70800 1.000 11.66000 ? 80  ARG B CZ   1 
ATOM   1750 N NH1  . ARG B 1 80  ? -30.31000 -4.03300  -13.93600 1.000 12.12000 ? 80  ARG B NH1  1 
ATOM   1751 N NH2  . ARG B 1 80  ? -31.43800 -2.06900  -14.33800 1.000 14.06000 ? 80  ARG B NH2  1 
ATOM   1752 N N    . HIS B 1 81  ? -33.64100 -9.29800  -18.73400 1.000 10.67000 ? 81  HIS B N    1 
ATOM   1753 C CA   . HIS B 1 81  ? -33.44300 -10.17700 -19.87800 1.000 11.57000 ? 81  HIS B CA   1 
ATOM   1754 C C    . HIS B 1 81  ? -32.13300 -9.80200  -20.56400 1.000 10.58000 ? 81  HIS B C    1 
ATOM   1755 O O    . HIS B 1 81  ? -31.94000 -8.64200  -20.93700 1.000 11.31000 ? 81  HIS B O    1 
ATOM   1756 C CB   . HIS B 1 81  ? -34.61200 -9.99800  -20.84400 1.000 13.99000 ? 81  HIS B CB   1 
ATOM   1757 C CG   . HIS B 1 81  ? -34.55900 -10.91000 -22.03000 1.000 15.49000 ? 81  HIS B CG   1 
ATOM   1758 N ND1  . HIS B 1 81  ? -35.42100 -10.78500 -23.09900 1.000 19.29000 ? 81  HIS B ND1  1 
ATOM   1759 C CD2  . HIS B 1 81  ? -33.76900 -11.97400 -22.30400 1.000 14.59000 ? 81  HIS B CD2  1 
ATOM   1760 C CE1  . HIS B 1 81  ? -35.15500 -11.73000 -23.98500 1.000 19.88000 ? 81  HIS B CE1  1 
ATOM   1761 N NE2  . HIS B 1 81  ? -34.15000 -12.45900 -23.53200 1.000 18.26000 ? 81  HIS B NE2  1 
ATOM   1762 N N    . VAL B 1 82  ? -31.23100 -10.77800 -20.70800 1.000 11.14000 ? 82  VAL B N    1 
ATOM   1763 C CA   . VAL B 1 82  ? -30.00300 -10.59800 -21.47400 1.000 11.79000 ? 82  VAL B CA   1 
ATOM   1764 C C    . VAL B 1 82  ? -29.85300 -11.74600 -22.46400 1.000 11.21000 ? 82  VAL B C    1 
ATOM   1765 O O    . VAL B 1 82  ? -30.42500 -12.82700 -22.30000 1.000 11.87000 ? 82  VAL B O    1 
ATOM   1766 C CB   . VAL B 1 82  ? -28.73700 -10.47000 -20.59500 1.000 10.86000 ? 82  VAL B CB   1 
ATOM   1767 C CG1  . VAL B 1 82  ? -28.84100 -9.25400  -19.69600 1.000 11.61000 ? 82  VAL B CG1  1 
ATOM   1768 C CG2  . VAL B 1 82  ? -28.50500 -11.73300 -19.78300 1.000 12.63000 ? 82  VAL B CG2  1 
ATOM   1769 N N    . LYS B 1 83  ? -29.07500 -11.48700 -23.51700 1.000 10.92000 ? 83  LYS B N    1 
ATOM   1770 C CA   . LYS B 1 83  ? -28.63500 -12.52000 -24.45200 1.000 11.26000 ? 83  LYS B CA   1 
ATOM   1771 C C    . LYS B 1 83  ? -27.19700 -12.87000 -24.09600 1.000 10.05000 ? 83  LYS B C    1 
ATOM   1772 O O    . LYS B 1 83  ? -26.29700 -12.04600 -24.27500 1.000 9.92000  ? 83  LYS B O    1 
ATOM   1773 C CB   . LYS B 1 83  ? -28.72500 -12.02000 -25.89000 1.000 12.13000 ? 83  LYS B CB   1 
ATOM   1774 C CG   . LYS B 1 83  ? -30.13700 -11.75100 -26.35400 1.000 17.11000 ? 83  LYS B CG   1 
ATOM   1775 C CD   . LYS B 1 83  ? -30.88300 -13.04800 -26.57300 0.000 17.42000 ? 83  LYS B CD   1 
ATOM   1776 C CE   . LYS B 1 83  ? -32.17400 -12.80900 -27.32200 0.000 20.11000 ? 83  LYS B CE   1 
ATOM   1777 N NZ   . LYS B 1 83  ? -32.84600 -14.09600 -27.60500 1.000 20.91000 ? 83  LYS B NZ   1 
ATOM   1778 N N    . ALA B 1 84  ? -26.99300 -14.06800 -23.56900 1.000 9.70000  ? 84  ALA B N    1 
ATOM   1779 C CA   . ALA B 1 84  ? -25.70400 -14.47700 -23.03100 1.000 9.26000  ? 84  ALA B CA   1 
ATOM   1780 C C    . ALA B 1 84  ? -24.97800 -15.40000 -24.00200 1.000 9.00000  ? 84  ALA B C    1 
ATOM   1781 O O    . ALA B 1 84  ? -25.58900 -16.19500 -24.71400 1.000 9.58000  ? 84  ALA B O    1 
ATOM   1782 C CB   . ALA B 1 84  ? -25.89600 -15.18900 -21.68900 1.000 10.31000 ? 84  ALA B CB   1 
ATOM   1783 N N    . LEU B 1 85  ? -23.65100 -15.30200 -24.00400 1.000 8.95000  ? 85  LEU B N    1 
ATOM   1784 C CA   . LEU B 1 85  ? -22.83900 -16.12000 -24.88700 1.000 8.24000  ? 85  LEU B CA   1 
ATOM   1785 C C    . LEU B 1 85  ? -21.52500 -16.38200 -24.16900 1.000 7.92000  ? 85  LEU B C    1 
ATOM   1786 O O    . LEU B 1 85  ? -20.88800 -15.43800 -23.69400 1.000 8.95000  ? 85  LEU B O    1 
ATOM   1787 C CB   . LEU B 1 85  ? -22.59600 -15.37000 -26.19400 1.000 10.18000 ? 85  LEU B CB   1 
ATOM   1788 C CG   . LEU B 1 85  ? -21.65000 -16.04700 -27.16900 1.000 9.77000  ? 85  LEU B CG   1 
ATOM   1789 C CD1  . LEU B 1 85  ? -22.23400 -17.35200 -27.67500 1.000 11.61000 ? 85  LEU B CD1  1 
ATOM   1790 C CD2  . LEU B 1 85  ? -21.36600 -15.11400 -28.33300 1.000 14.36000 ? 85  LEU B CD2  1 
ATOM   1791 N N    . VAL B 1 86  ? -21.14600 -17.65000 -24.07000 1.000 7.87000  ? 86  VAL B N    1 
ATOM   1792 C CA   . VAL B 1 86  ? -19.90800 -18.05500 -23.40800 1.000 7.91000  ? 86  VAL B CA   1 
ATOM   1793 C C    . VAL B 1 86  ? -18.98500 -18.68400 -24.44500 1.000 7.73000  ? 86  VAL B C    1 
ATOM   1794 O O    . VAL B 1 86  ? -19.39900 -19.60000 -25.16600 1.000 9.17000  ? 86  VAL B O    1 
ATOM   1795 C CB   . VAL B 1 86  ? -20.16900 -19.02000 -22.23300 1.000 7.96000  ? 86  VAL B CB   1 
ATOM   1796 C CG1  . VAL B 1 86  ? -18.85500 -19.35300 -21.53400 1.000 9.71000  ? 86  VAL B CG1  1 
ATOM   1797 C CG2  . VAL B 1 86  ? -21.17100 -18.40900 -21.23700 1.000 9.64000  ? 86  VAL B CG2  1 
ATOM   1798 N N    . THR B 1 87  ? -17.74100 -18.20700 -24.50400 1.000 8.12000  ? 87  THR B N    1 
ATOM   1799 C CA   . THR B 1 87  ? -16.76900 -18.65300 -25.49900 1.000 8.16000  ? 87  THR B CA   1 
ATOM   1800 C C    . THR B 1 87  ? -15.38800 -18.74200 -24.86000 1.000 8.09000  ? 87  THR B C    1 
ATOM   1801 O O    . THR B 1 87  ? -15.16000 -18.24200 -23.75400 1.000 8.62000  ? 87  THR B O    1 
ATOM   1802 C CB   . THR B 1 87  ? -16.71600 -17.68900 -26.69000 1.000 9.34000  ? 87  THR B CB   1 
ATOM   1803 O OG1  . THR B 1 87  ? -16.41000 -16.38000 -26.22300 1.000 10.61000 ? 87  THR B OG1  1 
ATOM   1804 C CG2  . THR B 1 87  ? -18.05600 -17.67200 -27.42500 1.000 10.22000 ? 87  THR B CG2  1 
ATOM   1805 N N    . TRP B 1 88  ? -14.45600 -19.37700 -25.56900 1.000 8.92000  ? 88  TRP B N    1 
ATOM   1806 C CA   . TRP B 1 88  ? -13.06500 -19.45600 -25.14100 1.000 8.95000  ? 88  TRP B CA   1 
ATOM   1807 C C    . TRP B 1 88  ? -12.23900 -18.38200 -25.83700 1.000 9.19000  ? 88  TRP B C    1 
ATOM   1808 O O    . TRP B 1 88  ? -12.32200 -18.21700 -27.06300 1.000 10.33000 ? 88  TRP B O    1 
ATOM   1809 C CB   . TRP B 1 88  ? -12.46700 -20.81800 -25.49100 1.000 10.98000 ? 88  TRP B CB   1 
ATOM   1810 C CG   . TRP B 1 88  ? -13.04600 -21.95000 -24.74200 1.000 11.30000 ? 88  TRP B CG   1 
ATOM   1811 C CD1  . TRP B 1 88  ? -13.92400 -22.88400 -25.22200 1.000 13.34000 ? 88  TRP B CD1  1 
ATOM   1812 C CD2  . TRP B 1 88  ? -12.81000 -22.28000 -23.37800 1.000 12.56000 ? 88  TRP B CD2  1 
ATOM   1813 N NE1  . TRP B 1 88  ? -14.23700 -23.78100 -24.23800 1.000 14.19000 ? 88  TRP B NE1  1 
ATOM   1814 C CE2  . TRP B 1 88  ? -13.56900 -23.43700 -23.09300 1.000 13.10000 ? 88  TRP B CE2  1 
ATOM   1815 C CE3  . TRP B 1 88  ? -12.02900 -21.71800 -22.37400 1.000 11.11000 ? 88  TRP B CE3  1 
ATOM   1816 C CZ2  . TRP B 1 88  ? -13.57200 -24.04000 -21.83800 1.000 14.14000 ? 88  TRP B CZ2  1 
ATOM   1817 C CZ3  . TRP B 1 88  ? -12.02700 -22.32600 -21.11500 1.000 15.75000 ? 88  TRP B CZ3  1 
ATOM   1818 C CH2  . TRP B 1 88  ? -12.80000 -23.47400 -20.86600 1.000 14.03000 ? 88  TRP B CH2  1 
ATOM   1819 N N    . GLU B 1 89  ? -11.40100 -17.69700 -25.07100 1.000 9.95000  ? 89  GLU B N    1 
ATOM   1820 C CA   . GLU B 1 89  ? -10.34000 -16.85000 -25.60900 1.000 11.35000 ? 89  GLU B CA   1 
ATOM   1821 C C    . GLU B 1 89  ? -9.05000  -17.46500 -25.08900 1.000 11.54000 ? 89  GLU B C    1 
ATOM   1822 O O    . GLU B 1 89  ? -8.62300  -17.18700 -23.96500 1.000 12.33000 ? 89  GLU B O    1 
ATOM   1823 C CB   . GLU B 1 89  ? -10.48700 -15.41500 -25.16300 1.000 14.06000 ? 89  GLU B CB   1 
ATOM   1824 C CG   . GLU B 1 89  ? -11.61200 -14.69800 -25.84700 1.000 16.03000 ? 89  GLU B CG   1 
ATOM   1825 C CD   . GLU B 1 89  ? -11.75300 -13.25700 -25.40800 1.000 19.77000 ? 89  GLU B CD   1 
ATOM   1826 O OE1  . GLU B 1 89  ? -10.79200 -12.70100 -24.83100 1.000 23.66000 ? 89  GLU B OE1  1 
ATOM   1827 O OE2  . GLU B 1 89  ? -12.83400 -12.68500 -25.65200 1.000 21.04000 ? 89  GLU B OE2  1 
ATOM   1828 N N    . GLY B 1 90  ? -8.45800  -18.35500 -25.87300 1.000 12.22000 ? 90  GLY B N    1 
ATOM   1829 C CA   . GLY B 1 90  ? -7.37500  -19.17000 -25.34100 1.000 13.18000 ? 90  GLY B CA   1 
ATOM   1830 C C    . GLY B 1 90  ? -7.91800  -20.05400 -24.23600 1.000 13.86000 ? 90  GLY B C    1 
ATOM   1831 O O    . GLY B 1 90  ? -8.89600  -20.79000 -24.42200 1.000 14.89000 ? 90  GLY B O    1 
ATOM   1832 N N    . ASP B 1 91  ? -7.29600  -19.99200 -23.06300 1.000 13.12000 ? 91  ASP B N    1 
ATOM   1833 C CA   . ASP B 1 91  ? -7.79500  -20.75000 -21.92500 1.000 14.11000 ? 91  ASP B CA   1 
ATOM   1834 C C    . ASP B 1 91  ? -8.74200  -19.95600 -21.02900 1.000 12.41000 ? 91  ASP B C    1 
ATOM   1835 O O    . ASP B 1 91  ? -9.15000  -20.47900 -19.98700 1.000 14.90000 ? 91  ASP B O    1 
ATOM   1836 C CB   . ASP B 1 91  ? -6.63400  -21.31900 -21.10100 1.000 18.10000 ? 91  ASP B CB   1 
ATOM   1837 C CG   . ASP B 1 91  ? -5.88400  -22.42000 -21.82600 1.000 22.46000 ? 91  ASP B CG   1 
ATOM   1838 O OD1  . ASP B 1 91  ? -6.44400  -23.01100 -22.77700 1.000 22.19000 ? 91  ASP B OD1  1 
ATOM   1839 O OD2  . ASP B 1 91  ? -4.73000  -22.69600 -21.43400 1.000 29.62000 ? 91  ASP B OD2  1 
ATOM   1840 N N    . VAL B 1 92  ? -9.08200  -18.72100 -21.38600 1.000 10.34000 ? 92  VAL B N    1 
ATOM   1841 C CA   . VAL B 1 92  ? -10.01200 -17.90100 -20.61100 1.000 10.16000 ? 92  VAL B CA   1 
ATOM   1842 C C    . VAL B 1 92  ? -11.43600 -18.17400 -21.08100 1.000 9.19000  ? 92  VAL B C    1 
ATOM   1843 O O    . VAL B 1 92  ? -11.72200 -18.12800 -22.28600 1.000 9.14000  ? 92  VAL B O    1 
ATOM   1844 C CB   . VAL B 1 92  ? -9.67700  -16.40700 -20.75800 1.000 10.63000 ? 92  VAL B CB   1 
ATOM   1845 C CG1  . VAL B 1 92  ? -10.46900 -15.60100 -19.75500 1.000 11.39000 ? 92  VAL B CG1  1 
ATOM   1846 C CG2  . VAL B 1 92  ? -8.17900  -16.15300 -20.58700 1.000 13.35000 ? 92  VAL B CG2  1 
ATOM   1847 N N    . LEU B 1 93  ? -12.33400 -18.43200 -20.13600 1.000 8.84000  ? 93  LEU B N    1 
ATOM   1848 C CA   . LEU B 1 93  ? -13.75000 -18.61000 -20.43900 1.000 7.51000  ? 93  LEU B CA   1 
ATOM   1849 C C    . LEU B 1 93  ? -14.42800 -17.25700 -20.29000 1.000 7.66000  ? 93  LEU B C    1 
ATOM   1850 O O    . LEU B 1 93  ? -14.35600 -16.64700 -19.21600 1.000 8.46000  ? 93  LEU B O    1 
ATOM   1851 C CB   . LEU B 1 93  ? -14.36200 -19.63600 -19.48400 1.000 9.01000  ? 93  LEU B CB   1 
ATOM   1852 C CG   . LEU B 1 93  ? -15.73800 -20.16100 -19.89800 1.000 9.33000  ? 93  LEU B CG   1 
ATOM   1853 C CD1  . LEU B 1 93  ? -15.68900 -20.90300 -21.22700 1.000 10.39000 ? 93  LEU B CD1  1 
ATOM   1854 C CD2  . LEU B 1 93  ? -16.31800 -21.02700 -18.78300 1.000 10.56000 ? 93  LEU B CD2  1 
ATOM   1855 N N    . VAL B 1 94  ? -15.07700 -16.79000 -21.35000 1.000 7.81000  ? 94  VAL B N    1 
ATOM   1856 C CA   . VAL B 1 94  ? -15.59200 -15.42600 -21.42400 1.000 7.64000  ? 94  VAL B CA   1 
ATOM   1857 C C    . VAL B 1 94  ? -17.09900 -15.45700 -21.66500 1.000 7.99000  ? 94  VAL B C    1 
ATOM   1858 O O    . VAL B 1 94  ? -17.55900 -16.09800 -22.61500 1.000 8.74000  ? 94  VAL B O    1 
ATOM   1859 C CB   . VAL B 1 94  ? -14.90100 -14.65100 -22.56000 1.000 8.40000  ? 94  VAL B CB   1 
ATOM   1860 C CG1  . VAL B 1 94  ? -15.46000 -13.23300 -22.68200 1.000 10.80000 ? 94  VAL B CG1  1 
ATOM   1861 C CG2  . VAL B 1 94  ? -13.38100 -14.63600 -22.35400 1.000 10.82000 ? 94  VAL B CG2  1 
ATOM   1862 N N    . SER B 1 95  ? -17.85600 -14.73700 -20.82600 1.000 7.79000  ? 95  SER B N    1 
ATOM   1863 C CA   . SER B 1 95  ? -19.30800 -14.55700 -21.00700 1.000 7.52000  ? 95  SER B CA   1 
ATOM   1864 C C    . SER B 1 95  ? -19.58500 -13.09000 -21.29900 1.000 8.51000  ? 95  SER B C    1 
ATOM   1865 O O    . SER B 1 95  ? -19.13500 -12.20900 -20.55900 1.000 8.22000  ? 95  SER B O    1 
ATOM   1866 C CB   . SER B 1 95  ? -20.18700 -14.98800 -19.77900 1.000 9.01000  ? 95  SER B CB   1 
ATOM   1867 O OG   . SER B 1 95  ? -21.73600 -14.75000 -19.83300 1.000 3.11000  ? 95  SER B OG   1 
ATOM   1868 N N    . VAL B 1 96  ? -20.32900 -12.83600 -22.36800 1.000 8.42000  ? 96  VAL B N    1 
ATOM   1869 C CA   . VAL B 1 96  ? -20.90300 -11.52100 -22.63100 1.000 8.61000  ? 96  VAL B CA   1 
ATOM   1870 C C    . VAL B 1 96  ? -22.41800 -11.63400 -22.50600 1.000 8.95000  ? 96  VAL B C    1 
ATOM   1871 O O    . VAL B 1 96  ? -23.02200 -12.54800 -23.07000 1.000 9.72000  ? 96  VAL B O    1 
ATOM   1872 C CB   . VAL B 1 96  ? -20.49100 -10.98300 -24.01700 1.000 9.80000  ? 96  VAL B CB   1 
ATOM   1873 C CG1  . VAL B 1 96  ? -21.15800 -9.65300  -24.31500 1.000 12.69000 ? 96  VAL B CG1  1 
ATOM   1874 C CG2  . VAL B 1 96  ? -18.96700 -10.88100 -24.09700 1.000 13.43000 ? 96  VAL B CG2  1 
ATOM   1875 N N    . GLN B 1 97  ? -23.01900 -10.73000 -21.74000 1.000 8.80000  ? 97  GLN B N    1 
ATOM   1876 C CA   . GLN B 1 97  ? -24.46900 -10.66000 -21.56500 1.000 9.10000  ? 97  GLN B CA   1 
ATOM   1877 C C    . GLN B 1 97  ? -24.96300 -9.36100  -22.20200 1.000 9.52000  ? 97  GLN B C    1 
ATOM   1878 O O    . GLN B 1 97  ? -24.82000 -8.28200  -21.62300 1.000 9.98000  ? 97  GLN B O    1 
ATOM   1879 C CB   . GLN B 1 97  ? -24.80600 -10.71600 -20.08400 1.000 9.75000  ? 97  GLN B CB   1 
ATOM   1880 C CG   . GLN B 1 97  ? -24.51300 -12.05200 -19.45400 1.000 10.51000 ? 97  GLN B CG   1 
ATOM   1881 C CD   . GLN B 1 97  ? -24.54900 -11.98200 -17.94900 1.000 11.92000 ? 97  GLN B CD   1 
ATOM   1882 O OE1  . GLN B 1 97  ? -23.98200 -11.07400 -17.34500 1.000 13.95000 ? 97  GLN B OE1  1 
ATOM   1883 N NE2  . GLN B 1 97  ? -25.24700 -12.92400 -17.32900 1.000 15.23000 ? 97  GLN B NE2  1 
ATOM   1884 N N    . LYS B 1 98  ? -25.50800 -9.47100  -23.41100 1.000 10.15000 ? 98  LYS B N    1 
ATOM   1885 C CA   . LYS B 1 98  ? -25.97800 -8.29600  -24.14000 1.000 11.02000 ? 98  LYS B CA   1 
ATOM   1886 C C    . LYS B 1 98  ? -27.34500 -7.85700  -23.63100 1.000 10.87000 ? 98  LYS B C    1 
ATOM   1887 O O    . LYS B 1 98  ? -28.24400 -8.68400  -23.46800 1.000 11.91000 ? 98  LYS B O    1 
ATOM   1888 C CB   . LYS B 1 98  ? -26.09600 -8.62000  -25.62700 1.000 12.12000 ? 98  LYS B CB   1 
ATOM   1889 C CG   . LYS B 1 98  ? -24.78500 -8.81500  -26.36100 1.000 16.96000 ? 98  LYS B CG   1 
ATOM   1890 C CD   . LYS B 1 98  ? -25.05700 -9.01100  -27.84800 1.000 21.69000 ? 98  LYS B CD   1 
ATOM   1891 C CE   . LYS B 1 98  ? -23.81400 -9.41900  -28.61100 1.000 22.83000 ? 98  LYS B CE   1 
ATOM   1892 N NZ   . LYS B 1 98  ? -24.12300 -9.67900  -30.05100 1.000 27.46000 ? 98  LYS B NZ   1 
ATOM   1893 N N    . GLY B 1 99  ? -27.50500 -6.55200  -23.42700 1.000 11.97000 ? 99  GLY B N    1 
ATOM   1894 C CA   . GLY B 1 99  ? -28.74100 -6.02400  -22.86000 1.000 12.35000 ? 99  GLY B CA   1 
ATOM   1895 C C    . GLY B 1 99  ? -28.57600 -4.57900  -22.44800 1.000 12.53000 ? 99  GLY B C    1 
ATOM   1896 O O    . GLY B 1 99  ? -27.76600 -3.84800  -23.01500 1.000 13.26000 ? 99  GLY B O    1 
ATOM   1897 N N    . GLU B 1 100 ? -29.33700 -4.18500  -21.42400 1.000 12.70000 ? 100 GLU B N    1 
ATOM   1898 C CA   . GLU B 1 100 ? -29.37700 -2.78100  -21.01600 1.000 12.60000 ? 100 GLU B CA   1 
ATOM   1899 C C    . GLU B 1 100 ? -28.03400 -2.29400  -20.49600 1.000 13.27000 ? 100 GLU B C    1 
ATOM   1900 O O    . GLU B 1 100 ? -27.60500 -1.17600  -20.80700 1.000 15.80000 ? 100 GLU B O    1 
ATOM   1901 C CB   . GLU B 1 100 ? -30.43900 -2.57400  -19.93700 1.000 14.58000 ? 100 GLU B CB   1 
ATOM   1902 C CG   . GLU B 1 100 ? -30.45800 -1.16000  -19.32700 1.000 17.72000 ? 100 GLU B CG   1 
ATOM   1903 C CD   . GLU B 1 100 ? -30.80300 -0.08200  -20.34900 1.000 18.95000 ? 100 GLU B CD   1 
ATOM   1904 O OE1  . GLU B 1 100 ? -31.37000 -0.43000  -21.40700 1.000 20.02000 ? 100 GLU B OE1  1 
ATOM   1905 O OE2  . GLU B 1 100 ? -30.50700 1.10400   -20.09200 1.000 22.19000 ? 100 GLU B OE2  1 
ATOM   1906 N N    . LYS B 1 101 ? -27.37500 -3.09600  -19.66400 1.000 11.15000 ? 101 LYS B N    1 
ATOM   1907 C CA   . LYS B 1 101 ? -26.09600 -2.70300  -19.10000 1.000 11.93000 ? 101 LYS B CA   1 
ATOM   1908 C C    . LYS B 1 101 ? -24.97400 -2.90400  -20.11000 1.000 12.31000 ? 101 LYS B C    1 
ATOM   1909 O O    . LYS B 1 101 ? -24.91700 -3.91900  -20.81000 1.000 13.46000 ? 101 LYS B O    1 
ATOM   1910 C CB   . LYS B 1 101 ? -25.81900 -3.52200  -17.84100 1.000 11.61000 ? 101 LYS B CB   1 
ATOM   1911 C CG   . LYS B 1 101 ? -26.85300 -3.31200  -16.74600 1.000 12.33000 ? 101 LYS B CG   1 
ATOM   1912 C CD   . LYS B 1 101 ? -26.75300 -1.92500  -16.12700 1.000 14.22000 ? 101 LYS B CD   1 
ATOM   1913 C CE   . LYS B 1 101 ? -27.86900 -1.69500  -15.12700 1.000 13.58000 ? 101 LYS B CE   1 
ATOM   1914 N NZ   . LYS B 1 101 ? -27.67100 -0.45900  -14.31100 1.000 14.50000 ? 101 LYS B NZ   1 
ATOM   1915 N N    . GLU B 1 102 ? -24.06600 -1.93600  -20.16800 1.000 14.05000 ? 102 GLU B N    1 
ATOM   1916 C CA   . GLU B 1 102 ? -22.87500 -2.07500  -20.98700 1.000 15.31000 ? 102 GLU B CA   1 
ATOM   1917 C C    . GLU B 1 102 ? -21.81600 -2.87000  -20.23700 1.000 12.41000 ? 102 GLU B C    1 
ATOM   1918 O O    . GLU B 1 102 ? -21.78500 -2.89100  -19.00200 1.000 13.55000 ? 102 GLU B O    1 
ATOM   1919 C CB   . GLU B 1 102 ? -22.29100 -0.70200  -21.31100 1.000 19.12000 ? 102 GLU B CB   1 
ATOM   1920 C CG   . GLU B 1 102 ? -23.16000 0.17700   -22.17700 1.000 24.14000 ? 102 GLU B CG   1 
ATOM   1921 C CD   . GLU B 1 102 ? -22.45600 1.47000   -22.54300 1.000 33.88000 ? 102 GLU B CD   1 
ATOM   1922 O OE1  . GLU B 1 102 ? -21.91500 2.12900   -21.62900 1.000 35.08000 ? 102 GLU B OE1  1 
ATOM   1923 O OE2  . GLU B 1 102 ? -22.43300 1.82000   -23.74200 1.000 39.68000 ? 102 GLU B OE2  1 
ATOM   1924 N N    . ASN B 1 103 ? -20.93400 -3.51100  -20.99900 1.000 13.33000 ? 103 ASN B N    1 
ATOM   1925 C CA   . ASN B 1 103 ? -19.78000 -4.21100  -20.43500 1.000 14.06000 ? 103 ASN B CA   1 
ATOM   1926 C C    . ASN B 1 103 ? -20.19200 -5.24300  -19.39200 1.000 11.94000 ? 103 ASN B C    1 
ATOM   1927 O O    . ASN B 1 103 ? -19.52400 -5.42300  -18.37200 1.000 12.30000 ? 103 ASN B O    1 
ATOM   1928 C CB   . ASN B 1 103 ? -18.76500 -3.23000  -19.85700 1.000 16.49000 ? 103 ASN B CB   1 
ATOM   1929 C CG   . ASN B 1 103 ? -17.44500 -3.88700  -19.54700 1.000 21.01000 ? 103 ASN B CG   1 
ATOM   1930 O OD1  . ASN B 1 103 ? -16.98300 -4.75800  -20.29000 1.000 21.34000 ? 103 ASN B OD1  1 
ATOM   1931 N ND2  . ASN B 1 103 ? -16.83300 -3.48700  -18.44000 1.000 22.03000 ? 103 ASN B ND2  1 
ATOM   1932 N N    . ARG B 1 104 ? -21.30700 -5.91600  -19.64300 1.000 10.34000 ? 104 ARG B N    1 
ATOM   1933 C CA   . ARG B 1 104 ? -21.85700 -6.86800  -18.69200 1.000 9.11000  ? 104 ARG B CA   1 
ATOM   1934 C C    . ARG B 1 104 ? -21.42000 -8.28400  -19.04400 1.000 9.22000  ? 104 ARG B C    1 
ATOM   1935 O O    . ARG B 1 104 ? -21.62300 -8.74100  -20.17200 1.000 9.44000  ? 104 ARG B O    1 
ATOM   1936 C CB   . ARG B 1 104 ? -23.38300 -6.79600  -18.65100 1.000 9.77000  ? 104 ARG B CB   1 
ATOM   1937 C CG   . ARG B 1 104 ? -23.95000 -7.65600  -17.53700 1.000 9.66000  ? 104 ARG B CG   1 
ATOM   1938 C CD   . ARG B 1 104 ? -25.46500 -7.75300  -17.60300 1.000 9.66000  ? 104 ARG B CD   1 
ATOM   1939 N NE   . ARG B 1 104 ? -25.92900 -8.63900  -16.54300 1.000 9.96000  ? 104 ARG B NE   1 
ATOM   1940 C CZ   . ARG B 1 104 ? -27.05100 -8.48700  -15.84900 1.000 8.73000  ? 104 ARG B CZ   1 
ATOM   1941 N NH1  . ARG B 1 104 ? -27.90400 -7.51200  -16.14900 1.000 9.37000  ? 104 ARG B NH1  1 
ATOM   1942 N NH2  . ARG B 1 104 ? -27.33800 -9.32400  -14.86400 1.000 10.85000 ? 104 ARG B NH2  1 
ATOM   1943 N N    . GLY B 1 105 ? -20.86600 -8.98800  -18.06600 1.000 9.18000  ? 105 GLY B N    1 
ATOM   1944 C CA   . GLY B 1 105 ? -20.49200 -10.37700 -18.27600 1.000 9.65000  ? 105 GLY B CA   1 
ATOM   1945 C C    . GLY B 1 105 ? -19.50000 -10.81800 -17.21700 1.000 9.49000  ? 105 GLY B C    1 
ATOM   1946 O O    . GLY B 1 105 ? -19.48000 -10.28500 -16.11300 1.000 8.59000  ? 105 GLY B O    1 
ATOM   1947 N N    . TRP B 1 106 ? -18.68900 -11.80700 -17.56900 1.000 8.62000  ? 106 TRP B N    1 
ATOM   1948 C CA   . TRP B 1 106 ? -17.67700 -12.31500 -16.65100 1.000 8.13000  ? 106 TRP B CA   1 
ATOM   1949 C C    . TRP B 1 106 ? -16.60400 -13.04300 -17.43700 1.000 9.16000  ? 106 TRP B C    1 
ATOM   1950 O O    . TRP B 1 106 ? -16.78400 -13.38400 -18.61200 1.000 8.98000  ? 106 TRP B O    1 
ATOM   1951 C CB   . TRP B 1 106 ? -18.25600 -13.19700 -15.53200 1.000 10.28000 ? 106 TRP B CB   1 
ATOM   1952 C CG   . TRP B 1 106 ? -19.15300 -14.32300 -15.96200 1.000 10.19000 ? 106 TRP B CG   1 
ATOM   1953 C CD1  . TRP B 1 106 ? -20.51000 -14.34600 -15.84500 1.000 12.02000 ? 106 TRP B CD1  1 
ATOM   1954 C CD2  . TRP B 1 106 ? -18.78400 -15.59600 -16.54900 1.000 9.64000  ? 106 TRP B CD2  1 
ATOM   1955 N NE1  . TRP B 1 106 ? -21.01200 -15.52900 -16.32700 1.000 12.77000 ? 106 TRP B NE1  1 
ATOM   1956 C CE2  . TRP B 1 106 ? -19.97800 -16.31600 -16.75900 1.000 10.35000 ? 106 TRP B CE2  1 
ATOM   1957 C CE3  . TRP B 1 106 ? -17.57400 -16.18400 -16.92500 1.000 10.24000 ? 106 TRP B CE3  1 
ATOM   1958 C CZ2  . TRP B 1 106 ? -19.99700 -17.59900 -17.32800 1.000 12.10000 ? 106 TRP B CZ2  1 
ATOM   1959 C CZ3  . TRP B 1 106 ? -17.60300 -17.46200 -17.49800 1.000 11.46000 ? 106 TRP B CZ3  1 
ATOM   1960 C CH2  . TRP B 1 106 ? -18.80200 -18.14600 -17.68500 1.000 11.58000 ? 106 TRP B CH2  1 
ATOM   1961 N N    . LYS B 1 107 ? -15.47400 -13.26500 -16.76500 1.000 9.00000  ? 107 LYS B N    1 
ATOM   1962 C CA   . LYS B 1 107 ? -14.37100 -14.05100 -17.29400 1.000 8.79000  ? 107 LYS B CA   1 
ATOM   1963 C C    . LYS B 1 107 ? -13.83700 -14.93700 -16.18100 1.000 8.94000  ? 107 LYS B C    1 
ATOM   1964 O O    . LYS B 1 107 ? -13.78800 -14.52700 -15.01100 1.000 8.75000  ? 107 LYS B O    1 
ATOM   1965 C CB   . LYS B 1 107 ? -13.24500 -13.15300 -17.81300 1.000 11.07000 ? 107 LYS B CB   1 
ATOM   1966 C CG   . LYS B 1 107 ? -13.64200 -12.32400 -19.02700 1.000 12.57000 ? 107 LYS B CG   1 
ATOM   1967 C CD   . LYS B 1 107 ? -12.52400 -11.38700 -19.46000 1.000 13.27000 ? 107 LYS B CD   1 
ATOM   1968 C CE   . LYS B 1 107 ? -13.01000 -10.42000 -20.52100 1.000 16.11000 ? 107 LYS B CE   1 
ATOM   1969 N NZ   . LYS B 1 107 ? -11.91400 -9.53900  -21.00700 1.000 20.56000 ? 107 LYS B NZ   1 
ATOM   1970 N N    . LYS B 1 108 ? -13.45400 -16.15700 -16.54900 1.000 8.63000  ? 108 LYS B N    1 
ATOM   1971 C CA   . LYS B 1 108 ? -12.94900 -17.15300 -15.62100 1.000 8.97000  ? 108 LYS B CA   1 
ATOM   1972 C C    . LYS B 1 108 ? -11.58300 -17.63900 -16.07500 1.000 8.55000  ? 108 LYS B C    1 
ATOM   1973 O O    . LYS B 1 108 ? -11.39900 -18.02100 -17.24600 1.000 9.46000  ? 108 LYS B O    1 
ATOM   1974 C CB   . LYS B 1 108 ? -13.90700 -18.33300 -15.58000 1.000 10.38000 ? 108 LYS B CB   1 
ATOM   1975 C CG   . LYS B 1 108 ? -13.70500 -19.24900 -14.39600 1.000 14.65000 ? 108 LYS B CG   1 
ATOM   1976 C CD   . LYS B 1 108 ? -14.60500 -20.47900 -14.46100 1.000 20.48000 ? 108 LYS B CD   1 
ATOM   1977 C CE   . LYS B 1 108 ? -16.05300 -20.12200 -14.78000 1.000 21.45000 ? 108 LYS B CE   1 
ATOM   1978 N NZ   . LYS B 1 108 ? -16.81800 -19.55600 -13.62100 1.000 22.83000 ? 108 LYS B NZ   1 
ATOM   1979 N N    . TRP B 1 109 ? -10.63400 -17.62300 -15.14600 1.000 8.52000  ? 109 TRP B N    1 
ATOM   1980 C CA   . TRP B 1 109 ? -9.30100  -18.17000 -15.34100 1.000 10.41000 ? 109 TRP B CA   1 
ATOM   1981 C C    . TRP B 1 109 ? -9.09700  -19.27200 -14.31200 1.000 10.68000 ? 109 TRP B C    1 
ATOM   1982 O O    . TRP B 1 109 ? -9.34600  -19.07100 -13.11600 1.000 11.29000 ? 109 TRP B O    1 
ATOM   1983 C CB   . TRP B 1 109 ? -8.21000  -17.12300 -15.11000 1.000 10.11000 ? 109 TRP B CB   1 
ATOM   1984 C CG   . TRP B 1 109 ? -8.18300  -15.92900 -16.01200 1.000 9.90000  ? 109 TRP B CG   1 
ATOM   1985 C CD1  . TRP B 1 109 ? -7.30900  -15.70100 -17.04700 1.000 11.22000 ? 109 TRP B CD1  1 
ATOM   1986 C CD2  . TRP B 1 109 ? -9.00400  -14.76200 -15.91700 1.000 9.33000  ? 109 TRP B CD2  1 
ATOM   1987 N NE1  . TRP B 1 109 ? -7.55600  -14.47500 -17.60400 1.000 11.23000 ? 109 TRP B NE1  1 
ATOM   1988 C CE2  . TRP B 1 109 ? -8.58800  -13.87600 -16.93200 1.000 10.96000 ? 109 TRP B CE2  1 
ATOM   1989 C CE3  . TRP B 1 109 ? -10.05700 -14.38000 -15.07500 1.000 9.95000  ? 109 TRP B CE3  1 
ATOM   1990 C CZ2  . TRP B 1 109 ? -9.19800  -12.63600 -17.13400 1.000 12.94000 ? 109 TRP B CZ2  1 
ATOM   1991 C CZ3  . TRP B 1 109 ? -10.65100 -13.14400 -15.27400 1.000 11.85000 ? 109 TRP B CZ3  1 
ATOM   1992 C CH2  . TRP B 1 109 ? -10.21900 -12.29200 -16.29400 1.000 13.61000 ? 109 TRP B CH2  1 
ATOM   1993 N N    . ILE B 1 110 ? -8.65700  -20.43600 -14.76300 1.000 12.49000 ? 110 ILE B N    1 
ATOM   1994 C CA   . ILE B 1 110 ? -8.35000  -21.55300 -13.88000 1.000 14.68000 ? 110 ILE B CA   1 
ATOM   1995 C C    . ILE B 1 110 ? -6.83800  -21.66100 -13.84000 1.000 15.61000 ? 110 ILE B C    1 
ATOM   1996 O O    . ILE B 1 110 ? -6.19700  -21.79800 -14.88900 1.000 18.21000 ? 110 ILE B O    1 
ATOM   1997 C CB   . ILE B 1 110 ? -8.96300  -22.86600 -14.39200 1.000 18.71000 ? 110 ILE B CB   1 
ATOM   1998 C CG1  . ILE B 1 110 ? -10.48000 -22.74400 -14.55100 1.000 21.89000 ? 110 ILE B CG1  1 
ATOM   1999 C CG2  . ILE B 1 110 ? -8.58900  -24.02400 -13.47300 1.000 22.15000 ? 110 ILE B CG2  1 
ATOM   2000 C CD1  . ILE B 1 110 ? -11.21000 -22.56600 -13.25200 1.000 20.43000 ? 110 ILE B CD1  1 
ATOM   2001 N N    . GLU B 1 111 ? -6.26200  -21.59100 -12.64600 0.850 14.07000 ? 111 GLU B N    1 
ATOM   2002 C CA   . GLU B 1 111 ? -4.82300  -21.76600 -12.46200 0.850 15.92000 ? 111 GLU B CA   1 
ATOM   2003 C C    . GLU B 1 111 ? -4.65300  -22.81400 -11.37200 0.850 17.58000 ? 111 GLU B C    1 
ATOM   2004 O O    . GLU B 1 111 ? -4.65000  -22.49300 -10.18100 0.850 15.79000 ? 111 GLU B O    1 
ATOM   2005 C CB   . GLU B 1 111 ? -4.15700  -20.45200 -12.11000 0.850 19.88000 ? 111 GLU B CB   1 
ATOM   2006 C CG   . GLU B 1 111 ? -4.32100  -19.41000 -13.19100 0.850 21.38000 ? 111 GLU B CG   1 
ATOM   2007 C CD   . GLU B 1 111 ? -3.30400  -18.30700 -13.08700 0.850 24.43000 ? 111 GLU B CD   1 
ATOM   2008 O OE1  . GLU B 1 111 ? -2.66800  -18.18500 -12.01800 0.850 28.07000 ? 111 GLU B OE1  1 
ATOM   2009 O OE2  . GLU B 1 111 ? -3.14000  -17.56700 -14.07800 0.850 27.14000 ? 111 GLU B OE2  1 
ATOM   2010 N N    . GLY B 1 112 ? -4.52700  -24.06500 -11.78700 1.000 22.22000 ? 112 GLY B N    1 
ATOM   2011 C CA   . GLY B 1 112 ? -4.32000  -25.13300 -10.82700 1.000 22.66000 ? 112 GLY B CA   1 
ATOM   2012 C C    . GLY B 1 112 ? -5.51900  -25.25600 -9.91800  1.000 17.43000 ? 112 GLY B C    1 
ATOM   2013 O O    . GLY B 1 112 ? -6.64500  -25.50800 -10.37000 1.000 22.95000 ? 112 GLY B O    1 
ATOM   2014 N N    . ASP B 1 113 ? -5.29000  -25.07300 -8.61900  1.000 17.18000 ? 113 ASP B N    1 
ATOM   2015 C CA   . ASP B 1 113 ? -6.34400  -25.19400 -7.62500  1.000 17.13000 ? 113 ASP B CA   1 
ATOM   2016 C C    . ASP B 1 113 ? -7.03800  -23.87300 -7.31400  1.000 13.18000 ? 113 ASP B C    1 
ATOM   2017 O O    . ASP B 1 113 ? -7.80800  -23.81500 -6.35200  1.000 14.99000 ? 113 ASP B O    1 
ATOM   2018 C CB   . ASP B 1 113 ? -5.80800  -25.83500 -6.34100  1.000 21.11000 ? 113 ASP B CB   1 
ATOM   2019 C CG   . ASP B 1 113 ? -6.08300  -27.32400 -6.27700  0.000 17.96000 ? 113 ASP B CG   1 
ATOM   2020 O OD1  . ASP B 1 113 ? -6.36500  -27.92400 -7.33600  0.000 18.45000 ? 113 ASP B OD1  1 
ATOM   2021 O OD2  . ASP B 1 113 ? -6.01800  -27.89400 -5.16700  0.000 17.65000 ? 113 ASP B OD2  1 
ATOM   2022 N N    . LYS B 1 114 ? -6.80800  -22.82700 -8.10900  1.000 14.99000 ? 114 LYS B N    1 
ATOM   2023 C CA   . LYS B 1 114 ? -7.45800  -21.53800 -7.92300  1.000 12.51000 ? 114 LYS B CA   1 
ATOM   2024 C C    . LYS B 1 114 ? -8.27400  -21.18100 -9.15500  1.000 10.53000 ? 114 LYS B C    1 
ATOM   2025 O O    . LYS B 1 114 ? -7.81500  -21.34100 -10.29300 1.000 13.82000 ? 114 LYS B O    1 
ATOM   2026 C CB   . LYS B 1 114 ? -6.43100  -20.42600 -7.67300  1.000 15.93000 ? 114 LYS B CB   1 
ATOM   2027 C CG   . LYS B 1 114 ? -5.54800  -20.64100 -6.44800  1.000 19.75000 ? 114 LYS B CG   1 
ATOM   2028 C CD   . LYS B 1 114 ? -6.35300  -20.58200 -5.16800  1.000 22.89000 ? 114 LYS B CD   1 
ATOM   2029 C CE   . LYS B 1 114 ? -5.45000  -20.51800 -3.93500  1.000 28.38000 ? 114 LYS B CE   1 
ATOM   2030 N NZ   . LYS B 1 114 ? -4.86900  -19.15800 -3.72400  1.000 31.99000 ? 114 LYS B NZ   1 
ATOM   2031 N N    . LEU B 1 115 ? -9.46400  -20.65700 -8.91000  1.000 10.46000 ? 115 LEU B N    1 
ATOM   2032 C CA   . LEU B 1 115 ? -10.33700 -20.12000 -9.94200  1.000 9.43000  ? 115 LEU B CA   1 
ATOM   2033 C C    . LEU B 1 115 ? -10.47600 -18.62100 -9.69500  1.000 10.08000 ? 115 LEU B C    1 
ATOM   2034 O O    . LEU B 1 115 ? -10.85700 -18.20000 -8.59000  1.000 10.12000 ? 115 LEU B O    1 
ATOM   2035 C CB   . LEU B 1 115 ? -11.68900 -20.82400 -9.88200  1.000 10.69000 ? 115 LEU B CB   1 
ATOM   2036 C CG   . LEU B 1 115 ? -12.73100 -20.48000 -10.95200 1.000 12.63000 ? 115 LEU B CG   1 
ATOM   2037 C CD1  . LEU B 1 115 ? -13.71000 -21.64300 -11.09300 1.000 14.84000 ? 115 LEU B CD1  1 
ATOM   2038 C CD2  . LEU B 1 115 ? -13.47500 -19.17700 -10.64600 1.000 13.29000 ? 115 LEU B CD2  1 
ATOM   2039 N N    . TYR B 1 116 ? -10.14000 -17.82600 -10.71100 1.000 9.10000  ? 116 TYR B N    1 
ATOM   2040 C CA   . TYR B 1 116 ? -10.27700 -16.37600 -10.67000 1.000 8.72000  ? 116 TYR B CA   1 
ATOM   2041 C C    . TYR B 1 116 ? -11.47600 -16.01100 -11.52400 1.000 8.69000  ? 116 TYR B C    1 
ATOM   2042 O O    . TYR B 1 116 ? -11.54900 -16.41200 -12.69000 1.000 8.93000  ? 116 TYR B O    1 
ATOM   2043 C CB   . TYR B 1 116 ? -9.03000  -15.68200 -11.21900 1.000 9.19000  ? 116 TYR B CB   1 
ATOM   2044 C CG   . TYR B 1 116 ? -7.80300  -15.99000 -10.41600 1.000 9.64000  ? 116 TYR B CG   1 
ATOM   2045 C CD1  . TYR B 1 116 ? -7.07800  -17.15500 -10.63400 1.000 11.24000 ? 116 TYR B CD1  1 
ATOM   2046 C CD2  . TYR B 1 116 ? -7.37000  -15.12500 -9.42600  1.000 9.67000  ? 116 TYR B CD2  1 
ATOM   2047 C CE1  . TYR B 1 116 ? -5.94500  -17.45200 -9.87500  1.000 12.25000 ? 116 TYR B CE1  1 
ATOM   2048 C CE2  . TYR B 1 116 ? -6.23600  -15.41600 -8.66200  1.000 12.38000 ? 116 TYR B CE2  1 
ATOM   2049 C CZ   . TYR B 1 116 ? -5.54300  -16.57500 -8.90100  1.000 12.56000 ? 116 TYR B CZ   1 
ATOM   2050 O OH   . TYR B 1 116 ? -4.42500  -16.85000 -8.14900  1.000 15.73000 ? 116 TYR B OH   1 
ATOM   2051 N N    . LEU B 1 117 ? -12.42100 -15.28600 -10.94100 1.000 8.36000  ? 117 LEU B N    1 
ATOM   2052 C CA   . LEU B 1 117 ? -13.63800 -14.87000 -11.62300 1.000 8.98000  ? 117 LEU B CA   1 
ATOM   2053 C C    . LEU B 1 117 ? -13.72900 -13.35400 -11.56000 1.000 8.71000  ? 117 LEU B C    1 
ATOM   2054 O O    . LEU B 1 117 ? -13.67100 -12.77400 -10.47100 1.000 10.64000 ? 117 LEU B O    1 
ATOM   2055 C CB   . LEU B 1 117 ? -14.83500 -15.49500 -10.91500 1.000 9.22000  ? 117 LEU B CB   1 
ATOM   2056 C CG   . LEU B 1 117 ? -16.21100 -15.12000 -11.46400 1.000 10.40000 ? 117 LEU B CG   1 
ATOM   2057 C CD1  . LEU B 1 117 ? -16.39100 -15.64000 -12.88500 1.000 11.79000 ? 117 LEU B CD1  1 
ATOM   2058 C CD2  . LEU B 1 117 ? -17.28200 -15.66000 -10.53600 1.000 13.39000 ? 117 LEU B CD2  1 
ATOM   2059 N N    . GLU B 1 118 ? -13.86800 -12.71100 -12.71400 1.000 8.27000  ? 118 GLU B N    1 
ATOM   2060 C CA   . GLU B 1 118 ? -14.06200 -11.26900 -12.76900 1.000 8.23000  ? 118 GLU B CA   1 
ATOM   2061 C C    . GLU B 1 118 ? -15.42900 -10.99100 -13.37000 1.000 8.77000  ? 118 GLU B C    1 
ATOM   2062 O O    . GLU B 1 118 ? -15.69200 -11.37100 -14.51800 1.000 10.09000 ? 118 GLU B O    1 
ATOM   2063 C CB   . GLU B 1 118 ? -12.94800 -10.59000 -13.55800 1.000 10.71000 ? 118 GLU B CB   1 
ATOM   2064 C CG   . GLU B 1 118 ? -11.64400 -10.60600 -12.76900 1.000 12.40000 ? 118 GLU B CG   1 
ATOM   2065 C CD   . GLU B 1 118 ? -10.55800 -9.71400  -13.34600 1.000 13.40000 ? 118 GLU B CD   1 
ATOM   2066 O OE1  . GLU B 1 118 ? -10.82900 -8.96400  -14.30400 1.000 15.20000 ? 118 GLU B OE1  1 
ATOM   2067 O OE2  . GLU B 1 118 ? -9.41500  -9.77900  -12.83900 1.000 16.76000 ? 118 GLU B OE2  1 
ATOM   2068 N N    . LEU B 1 119 ? -16.30400 -10.36600 -12.57900 1.000 8.49000  ? 119 LEU B N    1 
ATOM   2069 C CA   . LEU B 1 119 ? -17.64500 -9.98300  -13.00200 1.000 8.69000  ? 119 LEU B CA   1 
ATOM   2070 C C    . LEU B 1 119 ? -17.62800 -8.50400  -13.34700 1.000 8.19000  ? 119 LEU B C    1 
ATOM   2071 O O    . LEU B 1 119 ? -17.09200 -7.69400  -12.58400 1.000 9.72000  ? 119 LEU B O    1 
ATOM   2072 C CB   . LEU B 1 119 ? -18.63400 -10.20400 -11.85700 1.000 11.10000 ? 119 LEU B CB   1 
ATOM   2073 C CG   . LEU B 1 119 ? -18.69400 -11.57500 -11.18800 1.000 11.52000 ? 119 LEU B CG   1 
ATOM   2074 C CD1  . LEU B 1 119 ? -19.35600 -11.46600 -9.80800  1.000 14.30000 ? 119 LEU B CD1  1 
ATOM   2075 C CD2  . LEU B 1 119 ? -19.47000 -12.52200 -12.05500 1.000 18.71000 ? 119 LEU B CD2  1 
ATOM   2076 N N    . THR B 1 120 ? -18.22400 -8.14700  -14.47700 1.000 8.80000  ? 120 THR B N    1 
ATOM   2077 C CA   . THR B 1 120 ? -18.23400 -6.75200  -14.89700 1.000 10.31000 ? 120 THR B CA   1 
ATOM   2078 C C    . THR B 1 120 ? -19.65100 -6.24900  -15.14000 1.000 9.33000  ? 120 THR B C    1 
ATOM   2079 O O    . THR B 1 120 ? -20.53200 -6.99000  -15.58300 1.000 10.12000 ? 120 THR B O    1 
ATOM   2080 C CB   . THR B 1 120 ? -17.39300 -6.53700  -16.16800 1.000 11.01000 ? 120 THR B CB   1 
ATOM   2081 O OG1  . THR B 1 120 ? -17.90400 -7.34700  -17.23000 1.000 11.19000 ? 120 THR B OG1  1 
ATOM   2082 C CG2  . THR B 1 120 ? -15.93000 -6.89800  -15.92500 1.000 11.85000 ? 120 THR B CG2  1 
ATOM   2083 N N    . CYS B 1 121 ? -19.85500 -4.96800  -14.84400 1.000 10.08000 ? 121 CYS B N    1 
ATOM   2084 C CA   . CYS B 1 121 ? -21.07600 -4.28200  -15.24600 1.000 10.89000 ? 121 CYS B CA   1 
ATOM   2085 C C    . CYS B 1 121 ? -20.72600 -2.80400  -15.32700 1.000 11.51000 ? 121 CYS B C    1 
ATOM   2086 O O    . CYS B 1 121 ? -20.29200 -2.22300  -14.33200 1.000 12.34000 ? 121 CYS B O    1 
ATOM   2087 C CB   . CYS B 1 121 ? -22.22000 -4.53800  -14.24900 1.000 12.00000 ? 121 CYS B CB   1 
ATOM   2088 S SG   . CYS B 1 121 ? -23.76800 -3.74100  -14.68000 1.000 13.16000 ? 121 CYS B SG   1 
ATOM   2089 N N    . GLY B 1 122 ? -20.89900 -2.21100  -16.50600 1.000 13.69000 ? 122 GLY B N    1 
ATOM   2090 C CA   . GLY B 1 122 ? -20.53800 -0.81000  -16.68100 1.000 18.03000 ? 122 GLY B CA   1 
ATOM   2091 C C    . GLY B 1 122 ? -19.06500 -0.60400  -16.39300 1.000 15.63000 ? 122 GLY B C    1 
ATOM   2092 O O    . GLY B 1 122 ? -18.19300 -1.27800  -16.95400 1.000 17.57000 ? 122 GLY B O    1 
ATOM   2093 N N    . ASP B 1 123 ? -18.77000 0.33100   -15.49300 1.000 17.03000 ? 123 ASP B N    1 
ATOM   2094 C CA   . ASP B 1 123 ? -17.39200 0.60100   -15.12000 1.000 16.85000 ? 123 ASP B CA   1 
ATOM   2095 C C    . ASP B 1 123 ? -16.95600 -0.13200  -13.85700 1.000 16.04000 ? 123 ASP B C    1 
ATOM   2096 O O    . ASP B 1 123 ? -15.88100 0.16300   -13.32800 1.000 18.92000 ? 123 ASP B O    1 
ATOM   2097 C CB   . ASP B 1 123 ? -17.12700 2.10900   -15.01800 1.000 20.84000 ? 123 ASP B CB   1 
ATOM   2098 C CG   . ASP B 1 123 ? -17.87000 2.76500   -13.87200 1.000 26.04000 ? 123 ASP B CG   1 
ATOM   2099 O OD1  . ASP B 1 123 ? -18.63900 2.08200   -13.16100 1.000 26.31000 ? 123 ASP B OD1  1 
ATOM   2100 O OD2  . ASP B 1 123 ? -17.67700 3.98500   -13.67300 1.000 32.32000 ? 123 ASP B OD2  1 
ATOM   2101 N N    . GLN B 1 124 ? -17.74800 -1.08800  -13.37200 1.000 13.68000 ? 124 GLN B N    1 
ATOM   2102 C CA   . GLN B 1 124 ? -17.42700 -1.81800  -12.15300 1.000 14.03000 ? 124 GLN B CA   1 
ATOM   2103 C C    . GLN B 1 124 ? -16.91700 -3.21600  -12.47600 1.000 11.81000 ? 124 GLN B C    1 
ATOM   2104 O O    . GLN B 1 124 ? -17.46400 -3.90800  -13.33600 1.000 12.98000 ? 124 GLN B O    1 
ATOM   2105 C CB   . GLN B 1 124 ? -18.65500 -1.93400  -11.25200 1.000 13.61000 ? 124 GLN B CB   1 
ATOM   2106 C CG   . GLN B 1 124 ? -19.17100 -0.59700  -10.74600 1.000 13.96000 ? 124 GLN B CG   1 
ATOM   2107 C CD   . GLN B 1 124 ? -18.17700 0.10600   -9.85600  1.000 16.36000 ? 124 GLN B CD   1 
ATOM   2108 O OE1  . GLN B 1 124 ? -17.65800 -0.47000  -8.90100  1.000 16.55000 ? 124 GLN B OE1  1 
ATOM   2109 N NE2  . GLN B 1 124 ? -17.91700 1.37200   -10.15100 1.000 20.10000 ? 124 GLN B NE2  1 
ATOM   2110 N N    . VAL B 1 125 ? -15.87100 -3.62500  -11.76400 1.000 10.89000 ? 125 VAL B N    1 
ATOM   2111 C CA   . VAL B 1 125 ? -15.33900 -4.98000  -11.83300 1.000 11.77000 ? 125 VAL B CA   1 
ATOM   2112 C C    . VAL B 1 125 ? -15.30000 -5.54900  -10.42200 1.000 11.10000 ? 125 VAL B C    1 
ATOM   2113 O O    . VAL B 1 125 ? -14.79000 -4.90100  -9.50200  1.000 12.41000 ? 125 VAL B O    1 
ATOM   2114 C CB   . VAL B 1 125 ? -13.92900 -5.00900  -12.45200 1.000 14.87000 ? 125 VAL B CB   1 
ATOM   2115 C CG1  . VAL B 1 125 ? -13.46900 -6.44600  -12.66800 1.000 16.72000 ? 125 VAL B CG1  1 
ATOM   2116 C CG2  . VAL B 1 125 ? -13.88400 -4.21400  -13.75200 1.000 19.92000 ? 125 VAL B CG2  1 
ATOM   2117 N N    . CYS B 1 126 ? -15.85000 -6.75200  -10.25600 1.000 10.41000 ? 126 CYS B N    1 
ATOM   2118 C CA   . CYS B 1 126 ? -15.73000 -7.52500  -9.02500  1.000 11.30000 ? 126 CYS B CA   1 
ATOM   2119 C C    . CYS B 1 126 ? -14.78000 -8.69100  -9.28400  1.000 8.91000  ? 126 CYS B C    1 
ATOM   2120 O O    . CYS B 1 126 ? -14.91900 -9.39800  -10.29000 1.000 10.87000 ? 126 CYS B O    1 
ATOM   2121 C CB   . CYS B 1 126 ? -17.10800 -8.03100  -8.59100  1.000 11.07000 ? 126 CYS B CB   1 
ATOM   2122 S SG   . CYS B 1 126 ? -17.05600 -9.33400  -7.33700  1.000 10.31000 ? 126 CYS B SG   1 
ATOM   2123 N N    . ARG B 1 127 ? -13.78800 -8.86000  -8.41100  1.000 9.07000  ? 127 ARG B N    1 
ATOM   2124 C CA   . ARG B 1 127 ? -12.76700 -9.88900  -8.57100  1.000 9.46000  ? 127 ARG B CA   1 
ATOM   2125 C C    . ARG B 1 127 ? -12.91600 -10.89300 -7.43800  1.000 8.69000  ? 127 ARG B C    1 
ATOM   2126 O O    . ARG B 1 127 ? -12.77900 -10.53200 -6.26300  1.000 10.63000 ? 127 ARG B O    1 
ATOM   2127 C CB   . ARG B 1 127 ? -11.36700 -9.28000  -8.56900  1.000 11.64000 ? 127 ARG B CB   1 
ATOM   2128 C CG   . ARG B 1 127 ? -11.17200 -8.23600  -9.64800  1.000 13.69000 ? 127 ARG B CG   1 
ATOM   2129 C CD   . ARG B 1 127 ? -9.70400  -7.89900  -9.82800  1.000 17.31000 ? 127 ARG B CD   1 
ATOM   2130 N NE   . ARG B 1 127 ? -9.48800  -7.09000  -11.02300 1.000 22.56000 ? 127 ARG B NE   1 
ATOM   2131 C CZ   . ARG B 1 127 ? -9.63500  -5.77100  -11.06000 1.000 24.02000 ? 127 ARG B CZ   1 
ATOM   2132 N NH1  . ARG B 1 127 ? -9.41700  -5.10900  -12.18600 1.000 28.06000 ? 127 ARG B NH1  1 
ATOM   2133 N NH2  . ARG B 1 127 ? -9.99000  -5.11300  -9.96500  1.000 26.85000 ? 127 ARG B NH2  1 
ATOM   2134 N N    . GLN B 1 128 ? -13.17400 -12.15000 -7.78700  1.000 9.22000  ? 128 GLN B N    1 
ATOM   2135 C CA   . GLN B 1 128 ? -13.33500 -13.20900 -6.80700  1.000 9.82000  ? 128 GLN B CA   1 
ATOM   2136 C C    . GLN B 1 128 ? -12.27400 -14.27100 -7.03700  1.000 8.90000  ? 128 GLN B C    1 
ATOM   2137 O O    . GLN B 1 128 ? -11.84500 -14.50100 -8.17400  1.000 9.50000  ? 128 GLN B O    1 
ATOM   2138 C CB   . GLN B 1 128 ? -14.72500 -13.83700 -6.91400  1.000 10.23000 ? 128 GLN B CB   1 
ATOM   2139 C CG   . GLN B 1 128 ? -15.84500 -12.80600 -6.74200  1.000 10.44000 ? 128 GLN B CG   1 
ATOM   2140 C CD   . GLN B 1 128 ? -17.24400 -13.40800 -6.73300  1.000 10.98000 ? 128 GLN B CD   1 
ATOM   2141 O OE1  . GLN B 1 128 ? -17.44600 -14.54700 -7.14400  1.000 14.14000 ? 128 GLN B OE1  1 
ATOM   2142 N NE2  . GLN B 1 128 ? -18.22900 -12.62500 -6.28800  1.000 11.01000 ? 128 GLN B NE2  1 
ATOM   2143 N N    . VAL B 1 129 ? -11.84300 -14.91100 -5.95300  1.000 9.85000  ? 129 VAL B N    1 
ATOM   2144 C CA   . VAL B 1 129 ? -10.91000 -16.02800 -6.01500  1.000 9.84000  ? 129 VAL B CA   1 
ATOM   2145 C C    . VAL B 1 129 ? -11.52700 -17.17500 -5.23000  1.000 10.23000 ? 129 VAL B C    1 
ATOM   2146 O O    . VAL B 1 129 ? -12.04300 -16.96900 -4.11900  1.000 9.95000  ? 129 VAL B O    1 
ATOM   2147 C CB   . VAL B 1 129 ? -9.52800  -15.66300 -5.43100  1.000 10.97000 ? 129 VAL B CB   1 
ATOM   2148 C CG1  . VAL B 1 129 ? -8.55400  -16.81400 -5.63800  1.000 14.61000 ? 129 VAL B CG1  1 
ATOM   2149 C CG2  . VAL B 1 129 ? -8.98500  -14.40000 -6.06800  1.000 12.06000 ? 129 VAL B CG2  1 
ATOM   2150 N N    . PHE B 1 130 ? -11.48900 -18.37400 -5.80900  1.000 9.92000  ? 130 PHE B N    1 
ATOM   2151 C CA   . PHE B 1 130 ? -11.98100 -19.59600 -5.19100  1.000 11.13000 ? 130 PHE B CA   1 
ATOM   2152 C C    . PHE B 1 130 ? -10.86100 -20.62900 -5.17500  1.000 11.40000 ? 130 PHE B C    1 
ATOM   2153 O O    . PHE B 1 130 ? -10.00500 -20.66600 -6.06900  1.000 11.69000 ? 130 PHE B O    1 
ATOM   2154 C CB   . PHE B 1 130 ? -13.16300 -20.20500 -5.97800  1.000 12.17000 ? 130 PHE B CB   1 
ATOM   2155 C CG   . PHE B 1 130 ? -14.37400 -19.30300 -6.09600  1.000 11.17000 ? 130 PHE B CG   1 
ATOM   2156 C CD1  . PHE B 1 130 ? -14.41000 -18.25600 -7.01600  1.000 11.18000 ? 130 PHE B CD1  1 
ATOM   2157 C CD2  . PHE B 1 130 ? -15.49600 -19.53800 -5.33000  1.000 11.43000 ? 130 PHE B CD2  1 
ATOM   2158 C CE1  . PHE B 1 130 ? -15.52700 -17.44700 -7.12600  1.000 12.21000 ? 130 PHE B CE1  1 
ATOM   2159 C CE2  . PHE B 1 130 ? -16.61400 -18.73900 -5.44100  1.000 13.14000 ? 130 PHE B CE2  1 
ATOM   2160 C CZ   . PHE B 1 130 ? -16.62500 -17.68700 -6.34000  1.000 14.27000 ? 130 PHE B CZ   1 
ATOM   2161 N N    . LYS B 1 131 ? -10.89900 -21.49200 -4.16300  1.000 11.90000 ? 131 LYS B N    1 
ATOM   2162 C CA   . LYS B 1 131 ? -9.97200  -22.60800 -4.04200  1.000 12.27000 ? 131 LYS B CA   1 
ATOM   2163 C C    . LYS B 1 131 ? -10.72100 -23.91900 -4.24200  1.000 11.88000 ? 131 LYS B C    1 
ATOM   2164 O O    . LYS B 1 131 ? -11.79600 -24.12100 -3.67400  1.000 11.91000 ? 131 LYS B O    1 
ATOM   2165 C CB   . LYS B 1 131 ? -9.26900  -22.60000 -2.68400  1.000 16.79000 ? 131 LYS B CB   1 
ATOM   2166 N N    . LYS B 1 132 ? -10.14600 -24.80700 -5.04600  1.000 12.48000 ? 132 LYS B N    1 
ATOM   2167 C CA   . LYS B 1 132 ? -10.78700 -26.08600 -5.32100  1.000 12.75000 ? 132 LYS B CA   1 
ATOM   2168 C C    . LYS B 1 132 ? -10.78300 -26.95900 -4.07100  1.000 12.77000 ? 132 LYS B C    1 
ATOM   2169 O O    . LYS B 1 132 ? -9.73500  -27.16800 -3.45300  1.000 14.67000 ? 132 LYS B O    1 
ATOM   2170 C CB   . LYS B 1 132 ? -10.06400 -26.81300 -6.45700  1.000 15.54000 ? 132 LYS B CB   1 
ATOM   2171 C CG   . LYS B 1 132 ? -10.86000 -27.98300 -7.02400  1.000 16.71000 ? 132 LYS B CG   1 
ATOM   2172 C CD   . LYS B 1 132 ? -10.12800 -28.68600 -8.15600  1.000 19.32000 ? 132 LYS B CD   1 
ATOM   2173 C CE   . LYS B 1 132 ? -11.11000 -29.47800 -8.99000  1.000 24.69000 ? 132 LYS B CE   1 
ATOM   2174 N NZ   . LYS B 1 132 ? -10.47500 -30.29400 -10.05800 1.000 23.67000 ? 132 LYS B NZ   1 
ATOM   2175 N N    . LYS B 1 133 ? -11.94800 -27.47500 -3.71100  1.000 12.62000 ? 133 LYS B N    1 
ATOM   2176 C CA   . LYS B 1 133 ? -12.07700 -28.38600 -2.57500  1.000 13.91000 ? 133 LYS B CA   1 
ATOM   2177 C C    . LYS B 1 133 ? -11.70700 -29.81300 -2.97900  1.000 17.61000 ? 133 LYS B C    1 
ATOM   2178 C CB   . LYS B 1 133 ? -13.50300 -28.34700 -2.02100  1.000 15.73000 ? 133 LYS B CB   1 
ATOM   2179 C CG   . LYS B 1 133 ? -13.72300 -29.23900 -0.80900  1.000 18.07000 ? 133 LYS B CG   1 
ATOM   2180 C CD   . LYS B 1 133 ? -14.97200 -28.84900 -0.04000  1.000 26.02000 ? 133 LYS B CD   1 
ATOM   2181 C CE   . LYS B 1 133 ? -15.06200 -29.60800 1.28000   1.000 28.62000 ? 133 LYS B CE   1 
ATOM   2182 N NZ   . LYS B 1 133 ? -16.18000 -29.10300 2.13500   1.000 35.12000 ? 133 LYS B NZ   1 
HETATM 2183 C C10  . ZFJ C 2 .   ? -10.73700 -12.65600 17.23700  1.000 25.35000 ? 201 ZFJ A C10  1 
HETATM 2184 C C13  . ZFJ C 2 .   ? -13.15900 -13.69200 16.27700  1.000 23.46000 ? 201 ZFJ A C13  1 
HETATM 2185 C C15  . ZFJ C 2 .   ? -13.26300 -11.72600 13.59300  1.000 23.89000 ? 201 ZFJ A C15  1 
HETATM 2186 C C17  . ZFJ C 2 .   ? -8.51900  -11.96900 10.20400  1.000 27.46000 ? 201 ZFJ A C17  1 
HETATM 2187 C C20  . ZFJ C 2 .   ? -7.97200  -8.46000  11.11800  1.000 28.96000 ? 201 ZFJ A C20  1 
HETATM 2188 C C21  . ZFJ C 2 .   ? -13.84000 -14.37300 18.61500  1.000 19.80000 ? 201 ZFJ A C21  1 
HETATM 2189 C C22  . ZFJ C 2 .   ? -14.62200 -15.44000 18.41700  1.000 20.44000 ? 201 ZFJ A C22  1 
HETATM 2190 C C01  . ZFJ C 2 .   ? -10.96000 -12.26900 13.64400  1.000 26.92000 ? 201 ZFJ A C01  1 
HETATM 2191 C C02  . ZFJ C 2 .   ? -10.46500 -11.84500 12.43100  1.000 26.87000 ? 201 ZFJ A C02  1 
HETATM 2192 C C03  . ZFJ C 2 .   ? -9.19500  -11.23700 12.39800  1.000 26.71000 ? 201 ZFJ A C03  1 
HETATM 2193 C C04  . ZFJ C 2 .   ? -8.48100  -11.07500 13.58700  1.000 27.50000 ? 201 ZFJ A C04  1 
HETATM 2194 C C05  . ZFJ C 2 .   ? -9.01800  -11.48900 14.79800  1.000 28.19000 ? 201 ZFJ A C05  1 
HETATM 2195 C C06  . ZFJ C 2 .   ? -10.27100 -12.07300 14.80500  1.000 26.42000 ? 201 ZFJ A C06  1 
HETATM 2196 C C07  . ZFJ C 2 .   ? -11.04400 -12.59000 15.89600  1.000 23.97000 ? 201 ZFJ A C07  1 
HETATM 2197 C C08  . ZFJ C 2 .   ? -12.21600 -13.10500 15.42300  1.000 25.16000 ? 201 ZFJ A C08  1 
HETATM 2198 C C09  . ZFJ C 2 .   ? -12.29000 -12.87800 13.92800  1.000 26.48000 ? 201 ZFJ A C09  1 
HETATM 2199 C C11  . ZFJ C 2 .   ? -11.66500 -13.23500 18.10000  1.000 24.74000 ? 201 ZFJ A C11  1 
HETATM 2200 C C12  . ZFJ C 2 .   ? -12.88900 -13.76200 17.65600  1.000 20.19000 ? 201 ZFJ A C12  1 
HETATM 2201 C C14  . ZFJ C 2 .   ? -12.57100 -14.13600 13.12900  1.000 27.82000 ? 201 ZFJ A C14  1 
HETATM 2202 C C18  . ZFJ C 2 .   ? -7.72500  -13.24200 10.56800  1.000 26.38000 ? 201 ZFJ A C18  1 
HETATM 2203 C C19  . ZFJ C 2 .   ? -9.01100  -9.51500  10.78700  1.000 29.37000 ? 201 ZFJ A C19  1 
HETATM 2204 C C23  . ZFJ C 2 .   ? -15.50300 -15.91900 19.49900  1.000 19.67000 ? 201 ZFJ A C23  1 
HETATM 2205 N N16  . ZFJ C 2 .   ? -8.59700  -10.84800 11.17700  1.000 30.83000 ? 201 ZFJ A N16  1 
HETATM 2206 H H1   . ZFJ C 2 .   ? -9.92900  -12.32700 17.55800  1.000 30.44000 ? 201 ZFJ A H1   1 
HETATM 2207 H H2   . ZFJ C 2 .   ? -13.96300 -14.01300 15.93900  1.000 28.17000 ? 201 ZFJ A H2   1 
HETATM 2208 H H3   . ZFJ C 2 .   ? -12.77700 -11.00700 13.15900  1.000 28.69000 ? 201 ZFJ A H3   1 
HETATM 2209 H H4   . ZFJ C 2 .   ? -13.95700 -12.05100 12.99800  1.000 28.69000 ? 201 ZFJ A H4   1 
HETATM 2210 H H5   . ZFJ C 2 .   ? -13.66700 -11.39500 14.41000  1.000 28.69000 ? 201 ZFJ A H5   1 
HETATM 2211 H H6   . ZFJ C 2 .   ? -9.42900  -12.24300 10.00900  1.000 32.97000 ? 201 ZFJ A H6   1 
HETATM 2212 H H7   . ZFJ C 2 .   ? -8.13700  -11.61400 9.38600   1.000 32.97000 ? 201 ZFJ A H7   1 
HETATM 2213 H H8   . ZFJ C 2 .   ? -8.24100  -7.61000  10.73800  1.000 34.77000 ? 201 ZFJ A H8   1 
HETATM 2214 H H9   . ZFJ C 2 .   ? -7.89300  -8.37400  12.08100  1.000 34.77000 ? 201 ZFJ A H9   1 
HETATM 2215 H H10  . ZFJ C 2 .   ? -7.11500  -8.72300  10.74700  1.000 34.77000 ? 201 ZFJ A H10  1 
HETATM 2216 H H11  . ZFJ C 2 .   ? -13.88800 -13.96800 19.45100  1.000 23.78000 ? 201 ZFJ A H11  1 
HETATM 2217 H H12  . ZFJ C 2 .   ? -14.60600 -15.88400 17.60100  1.000 24.55000 ? 201 ZFJ A H12  1 
HETATM 2218 H H13  . ZFJ C 2 .   ? -10.95200 -11.97100 11.64900  1.000 32.27000 ? 201 ZFJ A H13  1 
HETATM 2219 H H14  . ZFJ C 2 .   ? -7.64300  -10.67300 13.57000  1.000 33.03000 ? 201 ZFJ A H14  1 
HETATM 2220 H H15  . ZFJ C 2 .   ? -8.53900  -11.38600 15.58900  1.000 33.85000 ? 201 ZFJ A H15  1 
HETATM 2221 H H16  . ZFJ C 2 .   ? -11.47000 -13.26600 19.00800  1.000 29.71000 ? 201 ZFJ A H16  1 
HETATM 2222 H H17  . ZFJ C 2 .   ? -13.43600 -14.05900 12.69700  1.000 33.41000 ? 201 ZFJ A H17  1 
HETATM 2223 H H18  . ZFJ C 2 .   ? -12.57500 -14.90300 13.72400  1.000 33.41000 ? 201 ZFJ A H18  1 
HETATM 2224 H H19  . ZFJ C 2 .   ? -11.88200 -14.25300 12.45600  1.000 33.41000 ? 201 ZFJ A H19  1 
HETATM 2225 H H20  . ZFJ C 2 .   ? -8.34300  -13.95200 10.80500  1.000 31.68000 ? 201 ZFJ A H20  1 
HETATM 2226 H H21  . ZFJ C 2 .   ? -7.14200  -13.05600 11.32100  1.000 31.68000 ? 201 ZFJ A H21  1 
HETATM 2227 H H22  . ZFJ C 2 .   ? -7.19100  -13.51900 9.80600   1.000 31.68000 ? 201 ZFJ A H22  1 
HETATM 2228 H H23  . ZFJ C 2 .   ? -9.17200  -9.50600  9.83100   1.000 35.26000 ? 201 ZFJ A H23  1 
HETATM 2229 H H24  . ZFJ C 2 .   ? -9.83600  -9.29700  11.24800  1.000 35.26000 ? 201 ZFJ A H24  1 
HETATM 2230 H H25  . ZFJ C 2 .   ? -15.31900 -15.63400 20.36500  1.000 23.62000 ? 201 ZFJ A H25  1 
HETATM 2231 H H161 . ZFJ C 2 .   ? -7.74300  -10.73000 11.40000  1.000 37.02000 ? 201 ZFJ A H161 1 
HETATM 2232 C C    . ACY D 3 .   ? -8.89400  -13.04900 22.05400  1.000 16.90000 ? 202 ACY A C    1 
HETATM 2233 O O    . ACY D 3 .   ? -9.21700  -13.43400 23.21600  1.000 19.84000 ? 202 ACY A O    1 
HETATM 2234 O OXT  . ACY D 3 .   ? -7.76300  -12.77800 21.58700  1.000 17.17000 ? 202 ACY A OXT  1 
HETATM 2235 C CH3  . ACY D 3 .   ? -9.99000  -12.91200 21.06700  1.000 13.56000 ? 202 ACY A CH3  1 
HETATM 2236 H H1   . ACY D 3 .   ? -9.63100  -13.00700 20.17100  1.000 16.29000 ? 202 ACY A H1   1 
HETATM 2237 H H2   . ACY D 3 .   ? -10.40200 -12.03800 21.16000  1.000 16.29000 ? 202 ACY A H2   1 
HETATM 2238 H H3   . ACY D 3 .   ? -10.65400 -13.60100 21.22400  1.000 16.29000 ? 202 ACY A H3   1 
HETATM 2239 C C10  . ZFJ E 2 .   ? -22.25100 -15.31200 -11.77400 1.000 28.27000 ? 301 ZFJ B C10  1 
HETATM 2240 C C13  . ZFJ E 2 .   ? -20.38300 -17.16700 -10.79400 1.000 25.12000 ? 301 ZFJ B C13  1 
HETATM 2241 C C15  . ZFJ E 2 .   ? -20.05700 -16.05100 -7.80400  1.000 27.75000 ? 301 ZFJ B C15  1 
HETATM 2242 C C17  . ZFJ E 2 .   ? -24.40800 -14.92400 -4.46500  1.000 29.60000 ? 301 ZFJ B C17  1 
HETATM 2243 C C20  . ZFJ E 2 .   ? -26.34900 -12.45800 -6.64600  1.000 35.37000 ? 301 ZFJ B C20  1 
HETATM 2244 C C21  . ZFJ E 2 .   ? -19.56100 -17.58600 -13.08100 1.000 21.55000 ? 301 ZFJ B C21  1 
HETATM 2245 C C22  . ZFJ E 2 .   ? -18.61700 -18.42500 -12.76200 1.000 24.17000 ? 301 ZFJ B C22  1 
HETATM 2246 C C01  . ZFJ E 2 .   ? -22.44400 -15.62900 -8.17300  1.000 28.13000 ? 301 ZFJ B C01  1 
HETATM 2247 C C02  . ZFJ E 2 .   ? -23.00300 -15.31000 -6.95100  1.000 29.40000 ? 301 ZFJ B C02  1 
HETATM 2248 C C03  . ZFJ E 2 .   ? -24.02600 -14.34900 -6.86000  1.000 29.16000 ? 301 ZFJ B C03  1 
HETATM 2249 C C04  . ZFJ E 2 .   ? -24.49200 -13.78500 -8.06800  1.000 30.32000 ? 301 ZFJ B C04  1 
HETATM 2250 C C05  . ZFJ E 2 .   ? -23.91900 -14.14700 -9.27800  1.000 28.73000 ? 301 ZFJ B C05  1 
HETATM 2251 C C06  . ZFJ E 2 .   ? -22.89100 -15.06400 -9.31900  1.000 30.01000 ? 301 ZFJ B C06  1 
HETATM 2252 C C07  . ZFJ E 2 .   ? -22.14600 -15.58100 -10.42500 1.000 26.49000 ? 301 ZFJ B C07  1 
HETATM 2253 C C08  . ZFJ E 2 .   ? -21.23600 -16.48200 -9.94200  1.000 26.32000 ? 301 ZFJ B C08  1 
HETATM 2254 C C09  . ZFJ E 2 .   ? -21.33700 -16.59300 -8.43700  1.000 27.55000 ? 301 ZFJ B C09  1 
HETATM 2255 C C11  . ZFJ E 2 .   ? -21.40300 -15.96200 -12.63600 1.000 28.06000 ? 301 ZFJ B C11  1 
HETATM 2256 C C12  . ZFJ E 2 .   ? -20.46800 -16.89600 -12.17700 1.000 26.21000 ? 301 ZFJ B C12  1 
HETATM 2257 C C14  . ZFJ E 2 .   ? -21.71900 -17.99200 -7.91100  1.000 30.02000 ? 301 ZFJ B C14  1 
HETATM 2258 C C18  . ZFJ E 2 .   ? -24.81800 -16.41000 -4.52600  1.000 34.50000 ? 301 ZFJ B C18  1 
HETATM 2259 C C19  . ZFJ E 2 .   ? -25.40800 -12.78800 -5.47500  1.000 31.30000 ? 301 ZFJ B C19  1 
HETATM 2260 C C23  . ZFJ E 2 .   ? -17.81500 -19.00300 -13.82700 1.000 20.28000 ? 301 ZFJ B C23  1 
HETATM 2261 N N16  . ZFJ E 2 .   ? -24.68700 -14.04700 -5.63400  1.000 33.31000 ? 301 ZFJ B N16  1 
HETATM 2262 H H1   . ZFJ E 2 .   ? -22.87400 -14.69700 -12.09100 1.000 33.94000 ? 301 ZFJ B H1   1 
HETATM 2263 H H2   . ZFJ E 2 .   ? -19.75600 -17.76800 -10.46100 1.000 30.17000 ? 301 ZFJ B H2   1 
HETATM 2264 H H3   . ZFJ E 2 .   ? -20.12200 -16.11300 -6.83800  1.000 33.32000 ? 301 ZFJ B H3   1 
HETATM 2265 H H4   . ZFJ E 2 .   ? -19.29900 -16.57000 -8.11100  1.000 33.32000 ? 301 ZFJ B H4   1 
HETATM 2266 H H5   . ZFJ E 2 .   ? -19.93800 -15.12200 -8.06000  1.000 33.32000 ? 301 ZFJ B H5   1 
HETATM 2267 H H6   . ZFJ E 2 .   ? -23.45100 -14.89500 -4.30300  1.000 35.55000 ? 301 ZFJ B H6   1 
HETATM 2268 H H7   . ZFJ E 2 .   ? -24.84900 -14.53300 -3.69600  1.000 35.55000 ? 301 ZFJ B H7   1 
HETATM 2269 H H8   . ZFJ E 2 .   ? -27.26000 -12.39800 -6.32200  1.000 42.46000 ? 301 ZFJ B H8   1 
HETATM 2270 H H9   . ZFJ E 2 .   ? -26.29000 -13.15700 -7.31600  1.000 42.46000 ? 301 ZFJ B H9   1 
HETATM 2271 H H10  . ZFJ E 2 .   ? -26.09000 -11.61000 -7.04000  1.000 42.46000 ? 301 ZFJ B H10  1 
HETATM 2272 H H11  . ZFJ E 2 .   ? -19.67100 -17.40100 -13.98600 1.000 25.88000 ? 301 ZFJ B H11  1 
HETATM 2273 H H12  . ZFJ E 2 .   ? -18.45700 -18.64800 -11.87400 1.000 29.03000 ? 301 ZFJ B H12  1 
HETATM 2274 H H13  . ZFJ E 2 .   ? -22.68100 -15.71400 -6.17700  1.000 35.30000 ? 301 ZFJ B H13  1 
HETATM 2275 H H14  . ZFJ E 2 .   ? -25.18700 -13.16700 -8.05300  1.000 36.40000 ? 301 ZFJ B H14  1 
HETATM 2276 H H15  . ZFJ E 2 .   ? -24.22100 -13.75900 -10.06700 1.000 34.49000 ? 301 ZFJ B H15  1 
HETATM 2277 H H16  . ZFJ E 2 .   ? -21.45500 -15.78100 -13.54700 1.000 33.70000 ? 301 ZFJ B H16  1 
HETATM 2278 H H17  . ZFJ E 2 .   ? -20.94200 -18.57100 -7.93400  1.000 36.04000 ? 301 ZFJ B H17  1 
HETATM 2279 H H18  . ZFJ E 2 .   ? -22.41900 -18.36600 -8.46900  1.000 36.04000 ? 301 ZFJ B H18  1 
HETATM 2280 H H19  . ZFJ E 2 .   ? -22.04000 -17.91700 -6.99700  1.000 36.04000 ? 301 ZFJ B H19  1 
HETATM 2281 H H20  . ZFJ E 2 .   ? -24.34500 -17.21800 -4.27200  1.000 41.43000 ? 301 ZFJ B H20  1 
HETATM 2282 H H21  . ZFJ E 2 .   ? -24.78700 -16.28800 -3.56400  1.000 41.43000 ? 301 ZFJ B H21  1 
HETATM 2283 H H22  . ZFJ E 2 .   ? -24.11800 -16.40600 -5.19800  1.000 41.43000 ? 301 ZFJ B H22  1 
HETATM 2284 H H23  . ZFJ E 2 .   ? -25.93200 -12.83300 -4.66200  1.000 37.58000 ? 301 ZFJ B H23  1 
HETATM 2285 H H24  . ZFJ E 2 .   ? -24.76100 -12.07000 -5.38800  1.000 37.58000 ? 301 ZFJ B H24  1 
HETATM 2286 H H25  . ZFJ E 2 .   ? -18.12400 -18.92400 -14.70100 1.000 24.36000 ? 301 ZFJ B H25  1 
HETATM 2287 H H161 . ZFJ E 2 .   ? -25.42400 -14.49600 -5.85400  1.000 39.99000 ? 301 ZFJ B H161 1 
HETATM 2288 C C    . ACY F 3 .   ? -24.46200 -15.97400 -16.10200 1.000 22.01000 ? 302 ACY B C    1 
HETATM 2289 O O    . ACY F 3 .   ? -23.49400 -15.67000 -15.37100 1.000 25.19000 ? 302 ACY B O    1 
HETATM 2290 O OXT  . ACY F 3 .   ? -25.69500 -15.98100 -15.81900 1.000 20.02000 ? 302 ACY B OXT  1 
HETATM 2291 C CH3  . ACY F 3 .   ? -24.10000 -16.35900 -17.53900 1.000 21.33000 ? 302 ACY B CH3  1 
HETATM 2292 H H1   . ACY F 3 .   ? -24.08400 -17.32500 -17.62000 1.000 25.62000 ? 302 ACY B H1   1 
HETATM 2293 H H2   . ACY F 3 .   ? -24.76200 -15.99400 -18.14800 1.000 25.62000 ? 302 ACY B H2   1 
HETATM 2294 H H3   . ACY F 3 .   ? -23.22600 -16.00000 -17.75900 1.000 25.62000 ? 302 ACY B H3   1 
HETATM 2295 O O    . HOH G 4 .   ? -10.63700 8.20700   9.30700   1.000 25.91000 ? 301 HOH A O    1 
HETATM 2296 O O    . HOH G 4 .   ? -15.22900 -4.48200  0.40700   1.000 30.84000 ? 302 HOH A O    1 
HETATM 2297 O O    . HOH G 4 .   ? -9.54000  -3.56100  35.90700  1.000 34.24000 ? 303 HOH A O    1 
HETATM 2298 O O    . HOH G 4 .   ? -29.81100 -17.14100 27.39700  1.000 29.68000 ? 304 HOH A O    1 
HETATM 2299 O O    . HOH G 4 .   ? -15.61000 -2.26700  4.29100   1.000 30.87000 ? 305 HOH A O    1 
HETATM 2300 O O    . HOH G 4 .   ? -17.48200 -23.73700 1.92900   1.000 32.93000 ? 306 HOH A O    1 
HETATM 2301 O O    . HOH G 4 .   ? -5.37500  -19.96400 12.26100  1.000 29.03000 ? 307 HOH A O    1 
HETATM 2302 O O    . HOH G 4 .   ? -19.14800 -0.76500  22.77300  1.000 29.71000 ? 308 HOH A O    1 
HETATM 2303 O O    . HOH G 4 .   ? -15.24400 -7.19500  4.03800   1.000 27.18000 ? 309 HOH A O    1 
HETATM 2304 O O    . HOH G 4 .   ? -12.96400 -10.14200 5.42200   1.000 29.44000 ? 310 HOH A O    1 
HETATM 2305 O O    . HOH G 4 .   ? -21.86800 -26.29400 18.00800  1.000 24.12000 ? 311 HOH A O    1 
HETATM 2306 O O    . HOH G 4 .   ? -16.30300 -7.34400  -1.99800  1.000 15.62000 ? 312 HOH A O    1 
HETATM 2307 O O    . HOH G 4 .   ? -22.99200 -8.54800  28.16500  1.000 30.93000 ? 313 HOH A O    1 
HETATM 2308 O O    . HOH G 4 .   ? -10.01000 -10.73500 6.22700   1.000 26.03000 ? 314 HOH A O    1 
HETATM 2309 O O    . HOH G 4 .   ? -22.96100 -17.65900 23.50700  1.000 20.28000 ? 315 HOH A O    1 
HETATM 2310 O O    . HOH G 4 .   ? -15.55700 -20.54300 5.51800   1.000 31.16000 ? 316 HOH A O    1 
HETATM 2311 O O    . HOH G 4 .   ? -21.29900 -5.21300  21.79500  1.000 19.33000 ? 317 HOH A O    1 
HETATM 2312 O O    . HOH G 4 .   ? -11.72000 4.53400   7.11300   1.000 36.11000 ? 318 HOH A O    1 
HETATM 2313 O O    . HOH G 4 .   ? -16.43800 -17.87200 5.69100   1.000 16.89000 ? 319 HOH A O    1 
HETATM 2314 O O    . HOH G 4 .   ? -2.52100  -12.30300 16.97300  1.000 28.56000 ? 320 HOH A O    1 
HETATM 2315 O O    . HOH G 4 .   ? -10.02700 -21.35100 10.82900  1.000 24.30000 ? 321 HOH A O    1 
HETATM 2316 O O    . HOH G 4 .   ? -17.02300 0.01100   21.24300  1.000 22.01000 ? 322 HOH A O    1 
HETATM 2317 O O    . HOH G 4 .   ? -20.19100 -7.44000  29.83000  1.000 25.82000 ? 323 HOH A O    1 
HETATM 2318 O O    . HOH G 4 .   ? -5.99100  -21.95900 18.71900  1.000 20.96000 ? 324 HOH A O    1 
HETATM 2319 O O    . HOH G 4 .   ? -7.41400  4.11700   24.78700  1.000 29.79000 ? 325 HOH A O    1 
HETATM 2320 O O    . HOH G 4 .   ? -30.62600 -16.25700 14.66600  1.000 32.05000 ? 326 HOH A O    1 
HETATM 2321 O O    . HOH G 4 .   ? -24.63900 -24.45900 18.96600  1.000 26.02000 ? 327 HOH A O    1 
HETATM 2322 O O    . HOH G 4 .   ? -16.34600 0.66000   8.66100   1.000 26.45000 ? 328 HOH A O    1 
HETATM 2323 O O    . HOH G 4 .   ? 0.82500   -7.04000  13.90000  1.000 25.60000 ? 329 HOH A O    1 
HETATM 2324 O O    . HOH G 4 .   ? -4.19700  -9.17600  36.97700  1.000 27.63000 ? 330 HOH A O    1 
HETATM 2325 O O    . HOH G 4 .   ? -8.98700  -7.47900  20.26800  1.000 21.94000 ? 331 HOH A O    1 
HETATM 2326 O O    . HOH G 4 .   ? -24.97500 -8.88300  16.77200  1.000 19.35000 ? 332 HOH A O    1 
HETATM 2327 O O    . HOH G 4 .   ? -11.26700 -25.15400 34.41400  1.000 28.63000 ? 333 HOH A O    1 
HETATM 2328 O O    . HOH G 4 .   ? -18.18200 -26.15700 27.39000  1.000 21.55000 ? 334 HOH A O    1 
HETATM 2329 O O    . HOH G 4 .   ? -7.21000  -2.86900  25.85300  1.000 11.65000 ? 335 HOH A O    1 
HETATM 2330 O O    . HOH G 4 .   ? -17.36500 -5.94700  24.00000  1.000 13.90000 ? 336 HOH A O    1 
HETATM 2331 O O    . HOH G 4 .   ? 3.87600   -12.89400 29.46200  1.000 19.52000 ? 337 HOH A O    1 
HETATM 2332 O O    . HOH G 4 .   ? -9.33900  -16.13800 2.72600   1.000 15.21000 ? 338 HOH A O    1 
HETATM 2333 O O    . HOH G 4 .   ? -11.36300 -18.53400 4.99600   1.000 21.68000 ? 339 HOH A O    1 
HETATM 2334 O O    . HOH G 4 .   ? -24.195   -16.594   33.888    1.000 15.48000 ? 340 HOH A O    1 
HETATM 2335 O O    . HOH G 4 .   ? -23.31600 -8.32300  10.44100  1.000 17.43000 ? 341 HOH A O    1 
HETATM 2336 O O    . HOH G 4 .   ? -17.31400 -23.01000 30.52000  1.000 22.72000 ? 342 HOH A O    1 
HETATM 2337 O O    . HOH G 4 .   ? -14.99400 -11.50400 30.81900  1.000 12.35000 ? 343 HOH A O    1 
HETATM 2338 O O    . HOH G 4 .   ? -10.34700 -16.40300 30.26000  1.000 10.15000 ? 344 HOH A O    1 
HETATM 2339 O O    . HOH G 4 .   ? -21.89300 -7.82500  5.64600   1.000 15.69000 ? 345 HOH A O    1 
HETATM 2340 O O    . HOH G 4 .   ? -32.901   -14.146   17.530    1.000 33.18000 ? 346 HOH A O    1 
HETATM 2341 O O    . HOH G 4 .   ? -9.55000  3.47000   23.50000  1.000 26.61000 ? 347 HOH A O    1 
HETATM 2342 O O    . HOH G 4 .   ? -16.33900 -7.02600  26.32900  1.000 13.77000 ? 348 HOH A O    1 
HETATM 2343 O O    . HOH G 4 .   ? -2.74100  -2.81400  25.34800  1.000 13.13000 ? 349 HOH A O    1 
HETATM 2344 O O    . HOH G 4 .   ? -17.61400 -4.30300  7.19300   1.000 17.22000 ? 350 HOH A O    1 
HETATM 2345 O O    . HOH G 4 .   ? -9.39700  -20.11100 5.80900   1.000 29.39000 ? 351 HOH A O    1 
HETATM 2346 O O    . HOH G 4 .   ? -12.64600 -26.93000 9.60600   1.000 27.56000 ? 352 HOH A O    1 
HETATM 2347 O O    . HOH G 4 .   ? -15.50700 -29.16600 17.59000  1.000 26.99000 ? 353 HOH A O    1 
HETATM 2348 O O    . HOH G 4 .   ? -15.47700 -30.68600 22.10200  1.000 24.84000 ? 354 HOH A O    1 
HETATM 2349 O O    . HOH G 4 .   ? -7.59500  -23.97600 25.75600  1.000 17.66000 ? 355 HOH A O    1 
HETATM 2350 O O    . HOH G 4 .   ? -12.88100 -27.61000 31.68100  1.000 25.95000 ? 356 HOH A O    1 
HETATM 2351 O O    . HOH G 4 .   ? -12.28700 3.74900   13.73700  1.000 16.93000 ? 357 HOH A O    1 
HETATM 2352 O O    . HOH G 4 .   ? -9.98900  -24.29900 16.79400  1.000 20.51000 ? 358 HOH A O    1 
HETATM 2353 O O    . HOH G 4 .   ? -8.81700  -1.63600  28.62800  1.000 17.62000 ? 359 HOH A O    1 
HETATM 2354 O O    . HOH G 4 .   ? -1.84700  -5.83600  11.43600  1.000 21.59000 ? 360 HOH A O    1 
HETATM 2355 O O    . HOH G 4 .   ? -29.03600 -27.03700 12.54800  1.000 28.96000 ? 361 HOH A O    1 
HETATM 2356 O O    . HOH G 4 .   ? -11.686   -21.721   35.420    1.000 16.55000 ? 362 HOH A O    1 
HETATM 2357 O O    . HOH G 4 .   ? -10.59600 -27.05200 23.64000  1.000 19.04000 ? 363 HOH A O    1 
HETATM 2358 O O    . HOH G 4 .   ? -6.54900  -22.70300 27.94400  1.000 19.92000 ? 364 HOH A O    1 
HETATM 2359 O O    . HOH G 4 .   ? -0.71800  -3.66000  28.53300  1.000 30.17000 ? 365 HOH A O    1 
HETATM 2360 O O    . HOH G 4 .   ? -28.42600 -15.14900 28.63700  1.000 19.91000 ? 366 HOH A O    1 
HETATM 2361 O O    . HOH G 4 .   ? 3.79600   -8.37900  15.32300  1.000 18.12000 ? 367 HOH A O    1 
HETATM 2362 O O    . HOH G 4 .   ? -11.73300 -6.20100  19.67300  1.000 17.37000 ? 368 HOH A O    1 
HETATM 2363 O O    . HOH G 4 .   ? -19.23000 -6.94400  22.23100  1.000 13.79000 ? 369 HOH A O    1 
HETATM 2364 O O    . HOH G 4 .   ? -7.16600  -18.59000 30.11100  1.000 11.75000 ? 370 HOH A O    1 
HETATM 2365 O O    . HOH G 4 .   ? -20.00300 -2.15800  7.10400   1.000 21.42000 ? 371 HOH A O    1 
HETATM 2366 O O    . HOH G 4 .   ? -23.67600 -9.61300  14.59900  1.000 16.15000 ? 372 HOH A O    1 
HETATM 2367 O O    . HOH G 4 .   ? -29.54100 -12.37000 11.64800  1.000 29.00000 ? 373 HOH A O    1 
HETATM 2368 O O    . HOH G 4 .   ? -2.68800  -12.41600 34.27300  1.000 27.55000 ? 374 HOH A O    1 
HETATM 2369 O O    . HOH G 4 .   ? -15.51300 -13.58000 5.18300   1.000 20.90000 ? 375 HOH A O    1 
HETATM 2370 O O    . HOH G 4 .   ? -3.18100  -17.58900 32.27600  1.000 18.34000 ? 376 HOH A O    1 
HETATM 2371 O O    . HOH G 4 .   ? 0.19900   -9.36200  36.10700  1.000 29.72000 ? 377 HOH A O    1 
HETATM 2372 O O    . HOH G 4 .   ? -6.138    -23.081   32.494    1.000 28.98000 ? 378 HOH A O    1 
HETATM 2373 O O    . HOH G 4 .   ? -26.10700 -22.61300 29.20800  1.000 34.91000 ? 379 HOH A O    1 
HETATM 2374 O O    . HOH G 4 .   ? -10.92300 -3.04200  27.53500  1.000 15.11000 ? 380 HOH A O    1 
HETATM 2375 O O    . HOH G 4 .   ? -9.09700  -29.46100 27.20700  1.000 29.49000 ? 381 HOH A O    1 
HETATM 2376 O O    . HOH G 4 .   ? 3.75800   -5.01800  28.31000  1.000 31.14000 ? 382 HOH A O    1 
HETATM 2377 O O    . HOH G 4 .   ? -22.67200 -5.18300  24.21500  1.000 24.31000 ? 383 HOH A O    1 
HETATM 2378 O O    . HOH G 4 .   ? -26.68100 -11.47800 8.68200   1.000 27.32000 ? 384 HOH A O    1 
HETATM 2379 O O    . HOH G 4 .   ? 1.147     -14.950   26.651    1.000 25.69000 ? 385 HOH A O    1 
HETATM 2380 O O    . HOH G 4 .   ? 1.37200   -3.37400  24.42600  1.000 19.47000 ? 386 HOH A O    1 
HETATM 2381 O O    . HOH G 4 .   ? -3.12400  -4.97600  30.69200  1.000 28.37000 ? 387 HOH A O    1 
HETATM 2382 O O    . HOH G 4 .   ? -14.58300 -4.92500  26.84900  1.000 18.64000 ? 388 HOH A O    1 
HETATM 2383 O O    . HOH G 4 .   ? -5.84000  -0.52600  31.15300  1.000 28.43000 ? 389 HOH A O    1 
HETATM 2384 O O    . HOH G 4 .   ? -2.25100  3.06600   8.72500   1.000 26.47000 ? 390 HOH A O    1 
HETATM 2385 O O    . HOH G 4 .   ? -15.48700 -9.55900  5.42200   1.000 21.01000 ? 391 HOH A O    1 
HETATM 2386 O O    . HOH G 4 .   ? -12.60700 -0.02200  29.12500  1.000 24.10000 ? 392 HOH A O    1 
HETATM 2387 O O    . HOH G 4 .   ? -1.15500  -3.26900  10.92200  1.000 20.28000 ? 393 HOH A O    1 
HETATM 2388 O O    . HOH G 4 .   ? -1.26300  -16.03300 30.64300  1.000 19.67000 ? 394 HOH A O    1 
HETATM 2389 O O    . HOH G 4 .   ? -0.49000  -14.31200 23.31800  1.000 25.48000 ? 395 HOH A O    1 
HETATM 2390 O O    . HOH G 4 .   ? -0.72400  -1.15000  16.48500  1.000 29.42000 ? 396 HOH A O    1 
HETATM 2391 O O    . HOH G 4 .   ? -3.34800  -18.33600 23.03700  1.000 26.79000 ? 397 HOH A O    1 
HETATM 2392 O O    . HOH G 4 .   ? -19.26500 -27.22000 11.64500  1.000 19.67000 ? 398 HOH A O    1 
HETATM 2393 O O    . HOH G 4 .   ? -19.54700 1.32000   15.79000  1.000 19.27000 ? 399 HOH A O    1 
HETATM 2394 O O    . HOH G 4 .   ? -5.27900  -2.60000  23.92200  1.000 11.33000 ? 400 HOH A O    1 
HETATM 2395 O O    . HOH G 4 .   ? -19.76600 -4.43600  27.71500  1.000 26.80000 ? 401 HOH A O    1 
HETATM 2396 O O    . HOH G 4 .   ? 3.02100   -7.54400  21.72000  1.000 23.66000 ? 402 HOH A O    1 
HETATM 2397 O O    . HOH G 4 .   ? -20.61200 2.29700   19.12000  1.000 30.79000 ? 403 HOH A O    1 
HETATM 2398 O O    . HOH G 4 .   ? -10.77300 2.08200   6.84800   1.000 27.26000 ? 404 HOH A O    1 
HETATM 2399 O O    . HOH G 4 .   ? -25.23600 -27.68600 15.18500  1.000 18.27000 ? 405 HOH A O    1 
HETATM 2400 O O    . HOH G 4 .   ? -14.31100 -27.82700 15.66600  1.000 27.22000 ? 406 HOH A O    1 
HETATM 2401 O O    . HOH G 4 .   ? -16.48900 -1.57800  7.30500   1.000 21.88000 ? 407 HOH A O    1 
HETATM 2402 O O    . HOH G 4 .   ? 3.84900   -3.44000  15.83900  1.000 26.97000 ? 408 HOH A O    1 
HETATM 2403 O O    . HOH G 4 .   ? -26.28800 -17.01600 23.18600  1.000 23.39000 ? 409 HOH A O    1 
HETATM 2404 O O    . HOH G 4 .   ? -16.05200 -28.71600 12.76400  1.000 28.87000 ? 410 HOH A O    1 
HETATM 2405 O O    . HOH G 4 .   ? -1.10800  -13.90300 10.44400  1.000 29.35000 ? 411 HOH A O    1 
HETATM 2406 O O    . HOH G 4 .   ? -2.34200  -15.52100 16.15400  1.000 27.21000 ? 412 HOH A O    1 
HETATM 2407 O O    . HOH G 4 .   ? -9.70500  3.12800   19.66200  1.000 27.21000 ? 413 HOH A O    1 
HETATM 2408 O O    . HOH G 4 .   ? -11.29700 -7.99600  20.23300  1.000 26.18000 ? 414 HOH A O    1 
HETATM 2409 O O    . HOH G 4 .   ? -10.22800 -26.34000 32.56400  1.000 30.20000 ? 415 HOH A O    1 
HETATM 2410 O O    . HOH G 4 .   ? -3.47000  -12.79300 20.74100  1.000 26.79000 ? 416 HOH A O    1 
HETATM 2411 O O    . HOH G 4 .   ? -9.81500  -8.64400  31.70300  1.000 23.01000 ? 417 HOH A O    1 
HETATM 2412 O O    . HOH G 4 .   ? 1.29400   -15.59000 31.04800  1.000 24.68000 ? 418 HOH A O    1 
HETATM 2413 O O    . HOH G 4 .   ? -18.93800 -4.03900  25.29800  1.000 27.26000 ? 419 HOH A O    1 
HETATM 2414 O O    . HOH G 4 .   ? -2.551    3.141     11.296    1.000 27.94000 ? 420 HOH A O    1 
HETATM 2415 O O    . HOH G 4 .   ? -2.60500  -16.08000 24.80300  1.000 29.58000 ? 421 HOH A O    1 
HETATM 2416 O O    . HOH G 4 .   ? -27.458   -5.766    14.283    1.000 28.79000 ? 422 HOH A O    1 
HETATM 2417 O O    . HOH G 4 .   ? -21.247   -23.803   34.525    1.000 34.35000 ? 423 HOH A O    1 
HETATM 2418 O O    . HOH G 4 .   ? -1.38900  -14.68300 34.21300  1.000 33.06000 ? 424 HOH A O    1 
HETATM 2419 O O    . HOH G 4 .   ? -19.013   -23.382   33.566    1.000 23.99000 ? 425 HOH A O    1 
HETATM 2420 O O    . HOH G 4 .   ? -15.14800 -3.35900  28.88900  1.000 24.93000 ? 426 HOH A O    1 
HETATM 2421 O O    . HOH G 4 .   ? -9.91200  -9.78500  19.30800  1.000 27.54000 ? 427 HOH A O    1 
HETATM 2422 O O    . HOH G 4 .   ? 0.20800   -7.39500  36.42400  1.000 33.76000 ? 428 HOH A O    1 
HETATM 2423 O O    . HOH G 4 .   ? -11.59700 -28.50100 15.52500  1.000 32.89000 ? 429 HOH A O    1 
HETATM 2424 O O    . HOH G 4 .   ? -0.41100  -1.32000  24.79100  1.000 20.42000 ? 430 HOH A O    1 
HETATM 2425 O O    . HOH G 4 .   ? -18.01600 -6.48500  28.59400  1.000 20.28000 ? 431 HOH A O    1 
HETATM 2426 O O    . HOH G 4 .   ? -12.32200 -7.94900  33.06800  1.000 22.62000 ? 432 HOH A O    1 
HETATM 2427 O O    . HOH G 4 .   ? -12.63100 -2.51700  29.71300  1.000 23.17000 ? 433 HOH A O    1 
HETATM 2428 O O    . HOH G 4 .   ? -13.517   -4.997    37.290    1.000 29.35000 ? 434 HOH A O    1 
HETATM 2429 O O    . HOH G 4 .   ? 2.70700   -15.43000 34.03100  1.000 35.10000 ? 435 HOH A O    1 
HETATM 2430 O O    . HOH G 4 .   ? -27.58000 -9.73900  11.09300  1.000 28.56000 ? 436 HOH A O    1 
HETATM 2431 O O    . HOH G 4 .   ? -32.447   -16.099   23.259    1.000 33.37000 ? 437 HOH A O    1 
HETATM 2432 O O    . HOH G 4 .   ? -13.59800 -5.49100  33.34200  1.000 30.23000 ? 438 HOH A O    1 
HETATM 2433 O O    . HOH G 4 .   ? 2.94100   -3.30200  26.64200  1.000 30.96000 ? 439 HOH A O    1 
HETATM 2434 O O    . HOH G 4 .   ? -14.50500 -9.54700  32.72200  1.000 27.23000 ? 440 HOH A O    1 
HETATM 2435 O O    . HOH G 4 .   ? -4.51700  -19.45200 30.65200  1.000 20.34000 ? 441 HOH A O    1 
HETATM 2436 O O    . HOH G 4 .   ? -11.58200 -3.13800  32.23400  1.000 31.09000 ? 442 HOH A O    1 
HETATM 2437 O O    . HOH G 4 .   ? -11.54900 -25.36200 8.17700   1.000 34.27000 ? 443 HOH A O    1 
HETATM 2438 O O    . HOH G 4 .   ? -25.75800 -8.84600  12.81700  1.000 25.62000 ? 444 HOH A O    1 
HETATM 2439 O O    . HOH G 4 .   ? -21.02400 -2.50700  22.39500  1.000 31.30000 ? 445 HOH A O    1 
HETATM 2440 O O    . HOH G 4 .   ? -11.52200 -29.18300 13.00800  1.000 33.79000 ? 446 HOH A O    1 
HETATM 2441 O O    . HOH H 4 .   ? -37.90500 -15.00100 -23.79900 1.000 24.13000 ? 401 HOH B O    1 
HETATM 2442 O O    . HOH H 4 .   ? -27.62500 -23.23000 -2.54100  1.000 35.62000 ? 402 HOH B O    1 
HETATM 2443 O O    . HOH H 4 .   ? -26.90000 -25.79100 -13.11400 1.000 28.14000 ? 403 HOH B O    1 
HETATM 2444 O O    . HOH H 4 .   ? -10.92700 -30.96100 -12.14900 1.000 25.55000 ? 404 HOH B O    1 
HETATM 2445 O O    . HOH H 4 .   ? -13.45300 -13.32600 -27.83100 1.000 26.59000 ? 405 HOH B O    1 
HETATM 2446 O O    . HOH H 4 .   ? -19.34100 -33.81600 -15.15200 1.000 32.03000 ? 406 HOH B O    1 
HETATM 2447 O O    . HOH H 4 .   ? -10.69200 -27.83000 -12.57300 1.000 27.07000 ? 407 HOH B O    1 
HETATM 2448 O O    . HOH H 4 .   ? -8.08400  -27.28700 -11.39700 1.000 27.28000 ? 408 HOH B O    1 
HETATM 2449 O O    . HOH H 4 .   ? -37.23600 -9.01700  -23.08500 1.000 32.38000 ? 409 HOH B O    1 
HETATM 2450 O O    . HOH H 4 .   ? -10.43900 -20.74400 -17.77100 1.000 24.11000 ? 410 HOH B O    1 
HETATM 2451 O O    . HOH H 4 .   ? -19.80800 -30.27100 -4.24600  1.000 24.33000 ? 411 HOH B O    1 
HETATM 2452 O O    . HOH H 4 .   ? -26.29600 -26.68200 -22.50000 1.000 24.64000 ? 412 HOH B O    1 
HETATM 2453 O O    . HOH H 4 .   ? -24.48900 -10.71500 -14.82300 1.000 25.01000 ? 413 HOH B O    1 
HETATM 2454 O O    . HOH H 4 .   ? -35.76800 -2.00600  0.05300   1.000 25.08000 ? 414 HOH B O    1 
HETATM 2455 O O    . HOH H 4 .   ? -17.59500 -14.09500 3.56400   1.000 21.24000 ? 415 HOH B O    1 
HETATM 2456 O O    . HOH H 4 .   ? -7.97900  -20.92900 -17.51700 1.000 21.94000 ? 416 HOH B O    1 
HETATM 2457 O O    . HOH H 4 .   ? -27.55600 -11.51100 -30.60100 1.000 30.95000 ? 417 HOH B O    1 
HETATM 2458 O O    . HOH H 4 .   ? -16.82400 -4.83800  -22.91100 1.000 28.59000 ? 418 HOH B O    1 
HETATM 2459 O O    . HOH H 4 .   ? -12.37600 -8.34100  -16.36600 1.000 17.62000 ? 419 HOH B O    1 
HETATM 2460 O O    . HOH H 4 .   ? -14.07300 -15.87300 -27.37800 1.000 15.70000 ? 420 HOH B O    1 
HETATM 2461 O O    . HOH H 4 .   ? -10.55400 -11.35300 -22.39200 1.000 28.36000 ? 421 HOH B O    1 
HETATM 2462 O O    . HOH H 4 .   ? -2.66200  -18.71100 -8.88600  1.000 28.28000 ? 422 HOH B O    1 
HETATM 2463 O O    . HOH H 4 .   ? -32.25700 -8.99300  -6.16200  1.000 24.06000 ? 423 HOH B O    1 
HETATM 2464 O O    . HOH H 4 .   ? -17.13700 -37.26700 -19.50500 1.000 20.43000 ? 424 HOH B O    1 
HETATM 2465 O O    . HOH H 4 .   ? -9.09300  -19.57500 -28.17300 1.000 17.39000 ? 425 HOH B O    1 
HETATM 2466 O O    . HOH H 4 .   ? -23.03100 -22.81600 -0.31200  1.000 30.91000 ? 426 HOH B O    1 
HETATM 2467 O O    . HOH H 4 .   ? -25.96100 -12.77600 4.85500   1.000 20.42000 ? 427 HOH B O    1 
HETATM 2468 O O    . HOH H 4 .   ? -14.75200 -29.36900 -21.84600 1.000 24.07000 ? 428 HOH B O    1 
HETATM 2469 O O    . HOH H 4 .   ? -21.87600 -28.44900 -28.66100 1.000 26.62000 ? 429 HOH B O    1 
HETATM 2470 O O    . HOH H 4 .   ? -17.25700 -33.71400 -16.41500 1.000 21.14000 ? 430 HOH B O    1 
HETATM 2471 O O    . HOH H 4 .   ? -8.68600  -11.80000 -11.20000 1.000 15.95000 ? 431 HOH B O    1 
HETATM 2472 O O    . HOH H 4 .   ? -17.18100 -8.86100  0.11600   1.000 21.66000 ? 432 HOH B O    1 
HETATM 2473 O O    . HOH H 4 .   ? -22.89100 -29.67600 -26.53100 1.000 28.79000 ? 433 HOH B O    1 
HETATM 2474 O O    . HOH H 4 .   ? -14.32500 -3.80200  -17.43100 1.000 28.01000 ? 434 HOH B O    1 
HETATM 2475 O O    . HOH H 4 .   ? -8.75200  -9.33200  -5.60000  1.000 21.79000 ? 435 HOH B O    1 
HETATM 2476 O O    . HOH H 4 .   ? -23.29500 -18.89500 2.19500   1.000 25.40000 ? 436 HOH B O    1 
HETATM 2477 O O    . HOH H 4 .   ? -30.95000 -6.26300  -20.01300 1.000 12.05000 ? 437 HOH B O    1 
HETATM 2478 O O    . HOH H 4 .   ? -12.80800 -26.36200 3.24000   1.000 30.64000 ? 438 HOH B O    1 
HETATM 2479 O O    . HOH H 4 .   ? -20.83800 -21.40700 0.61100   1.000 28.59000 ? 439 HOH B O    1 
HETATM 2480 O O    . HOH H 4 .   ? -9.13500  -6.80500  -14.43900 1.000 26.26000 ? 440 HOH B O    1 
HETATM 2481 O O    . HOH H 4 .   ? -33.27400 -17.12100 -28.43500 1.000 30.04000 ? 441 HOH B O    1 
HETATM 2482 O O    . HOH H 4 .   ? -26.45700 -6.17800  -20.52800 1.000 9.97000  ? 442 HOH B O    1 
HETATM 2483 O O    . HOH H 4 .   ? -11.46800 -25.14200 -0.90200  1.000 20.52000 ? 443 HOH B O    1 
HETATM 2484 O O    . HOH H 4 .   ? -30.80000 -16.03100 -28.36200 1.000 25.87000 ? 444 HOH B O    1 
HETATM 2485 O O    . HOH H 4 .   ? -22.37100 -10.93600 -15.11200 1.000 19.44000 ? 445 HOH B O    1 
HETATM 2486 O O    . HOH H 4 .   ? -16.19700 -9.02600  -18.60000 1.000 13.78000 ? 446 HOH B O    1 
HETATM 2487 O O    . HOH H 4 .   ? -34.69100 -19.21200 -25.33900 1.000 26.79000 ? 447 HOH B O    1 
HETATM 2488 O O    . HOH H 4 .   ? -28.42700 0.81600   -8.24100  1.000 20.33000 ? 448 HOH B O    1 
HETATM 2489 O O    . HOH H 4 .   ? -13.17000 -10.36100 -24.17600 1.000 24.87000 ? 449 HOH B O    1 
HETATM 2490 O O    . HOH H 4 .   ? -18.96300 -12.36500 -0.37700  1.000 18.56000 ? 450 HOH B O    1 
HETATM 2491 O O    . HOH H 4 .   ? -37.41800 -11.21400 -9.80600  1.000 20.77000 ? 451 HOH B O    1 
HETATM 2492 O O    . HOH H 4 .   ? -29.92400 0.24900   -23.68600 1.000 29.14000 ? 452 HOH B O    1 
HETATM 2493 O O    . HOH H 4 .   ? -17.91800 -35.92400 -17.81100 1.000 27.56000 ? 453 HOH B O    1 
HETATM 2494 O O    . HOH H 4 .   ? -29.710   -27.737   -14.119   1.000 33.51000 ? 454 HOH B O    1 
HETATM 2495 O O    . HOH H 4 .   ? -10.52800 -11.05300 -4.68700  1.000 14.89000 ? 455 HOH B O    1 
HETATM 2496 O O    . HOH H 4 .   ? -18.44800 -14.70000 -25.29100 1.000 13.19000 ? 456 HOH B O    1 
HETATM 2497 O O    . HOH H 4 .   ? -17.31200 -32.37100 -12.11000 1.000 23.45000 ? 457 HOH B O    1 
HETATM 2498 O O    . HOH H 4 .   ? -29.99800 -8.27900  -25.61500 1.000 27.26000 ? 458 HOH B O    1 
HETATM 2499 O O    . HOH H 4 .   ? -7.05400  -6.80100  -7.51000  1.000 28.24000 ? 459 HOH B O    1 
HETATM 2500 O O    . HOH H 4 .   ? -31.91500 -21.25700 -12.97600 1.000 31.02000 ? 460 HOH B O    1 
HETATM 2501 O O    . HOH H 4 .   ? -10.79800 -8.37200  -18.71100 1.000 24.01000 ? 461 HOH B O    1 
HETATM 2502 O O    . HOH H 4 .   ? -22.94500 -19.80600 -24.61500 1.000 9.89000  ? 462 HOH B O    1 
HETATM 2503 O O    . HOH H 4 .   ? -17.25400 -10.14400 -20.87800 1.000 13.32000 ? 463 HOH B O    1 
HETATM 2504 O O    . HOH H 4 .   ? -15.73300 -26.18300 -24.97600 1.000 22.35000 ? 464 HOH B O    1 
HETATM 2505 O O    . HOH H 4 .   ? -23.16000 -9.93100  4.06500   1.000 14.18000 ? 465 HOH B O    1 
HETATM 2506 O O    . HOH H 4 .   ? -12.23600 -4.42600  -8.40800  1.000 27.91000 ? 466 HOH B O    1 
HETATM 2507 O O    . HOH H 4 .   ? -21.77900 -9.35600  -14.53000 1.000 21.28000 ? 467 HOH B O    1 
HETATM 2508 O O    . HOH H 4 .   ? -30.07000 -21.24400 -26.41900 1.000 19.43000 ? 468 HOH B O    1 
HETATM 2509 O O    . HOH H 4 .   ? -31.69100 0.12300   -3.02800  1.000 22.26000 ? 469 HOH B O    1 
HETATM 2510 O O    . HOH H 4 .   ? -24.92100 -5.08600  -23.39300 1.000 15.44000 ? 470 HOH B O    1 
HETATM 2511 O O    . HOH H 4 .   ? -14.83600 -20.58800 1.80100   1.000 19.85000 ? 471 HOH B O    1 
HETATM 2512 O O    . HOH H 4 .   ? -26.56300 1.04400   -19.37500 1.000 26.50000 ? 472 HOH B O    1 
HETATM 2513 O O    . HOH H 4 .   ? -21.45100 0.81100   -8.40900  1.000 22.28000 ? 473 HOH B O    1 
HETATM 2514 O O    . HOH H 4 .   ? -9.95500  -12.54500 -9.01200  1.000 13.44000 ? 474 HOH B O    1 
HETATM 2515 O O    . HOH H 4 .   ? -26.02700 -22.18700 -24.46200 1.000 11.21000 ? 475 HOH B O    1 
HETATM 2516 O O    . HOH H 4 .   ? -17.65100 -5.10700  -1.94100  1.000 18.64000 ? 476 HOH B O    1 
HETATM 2517 O O    . HOH H 4 .   ? -18.45900 -25.18600 0.65200   1.000 31.31000 ? 477 HOH B O    1 
HETATM 2518 O O    . HOH H 4 .   ? -21.433   -25.088   -29.812   1.000 18.18000 ? 478 HOH B O    1 
HETATM 2519 O O    . HOH H 4 .   ? -16.99600 -31.18200 -7.56500  1.000 22.51000 ? 479 HOH B O    1 
HETATM 2520 O O    . HOH H 4 .   ? -25.32400 -27.57200 -20.12700 1.000 20.87000 ? 480 HOH B O    1 
HETATM 2521 O O    . HOH H 4 .   ? -4.87900  -18.46100 -22.88500 1.000 19.71000 ? 481 HOH B O    1 
HETATM 2522 O O    . HOH H 4 .   ? -26.91700 -26.87100 -26.72700 1.000 29.91000 ? 482 HOH B O    1 
HETATM 2523 O O    . HOH H 4 .   ? -14.44100 -9.99800  -16.71900 1.000 13.26000 ? 483 HOH B O    1 
HETATM 2524 O O    . HOH H 4 .   ? -22.70500 -6.38200  -22.21500 1.000 14.11000 ? 484 HOH B O    1 
HETATM 2525 O O    . HOH H 4 .   ? -25.93300 -11.87700 -14.34500 1.000 23.76000 ? 485 HOH B O    1 
HETATM 2526 O O    . HOH H 4 .   ? -20.79600 -33.35100 -24.29600 1.000 32.21000 ? 486 HOH B O    1 
HETATM 2527 O O    . HOH H 4 .   ? -21.04700 -3.32300  -23.90400 1.000 18.24000 ? 487 HOH B O    1 
HETATM 2528 O O    . HOH H 4 .   ? -2.63100  -21.41900 -8.37600  1.000 30.40000 ? 488 HOH B O    1 
HETATM 2529 O O    . HOH H 4 .   ? -36.37400 -10.98900 -16.14200 1.000 24.00000 ? 489 HOH B O    1 
HETATM 2530 O O    . HOH H 4 .   ? -8.47900  -8.18000  -15.85500 1.000 30.72000 ? 490 HOH B O    1 
HETATM 2531 O O    . HOH H 4 .   ? -18.10700 -30.83900 -9.96100  1.000 21.86000 ? 491 HOH B O    1 
HETATM 2532 O O    . HOH H 4 .   ? -34.98800 -6.73300  -19.14400 1.000 16.18000 ? 492 HOH B O    1 
HETATM 2533 O O    . HOH H 4 .   ? -13.51400 -30.23100 -6.29700  1.000 15.79000 ? 493 HOH B O    1 
HETATM 2534 O O    . HOH H 4 .   ? -33.20400 -11.56700 -5.00600  1.000 31.93000 ? 494 HOH B O    1 
HETATM 2535 O O    . HOH H 4 .   ? -10.72000 -26.06300 -28.97500 1.000 32.32000 ? 495 HOH B O    1 
HETATM 2536 O O    . HOH H 4 .   ? -16.53700 -6.51600  1.49200   1.000 29.71000 ? 496 HOH B O    1 
HETATM 2537 O O    . HOH H 4 .   ? -22.10900 -30.49100 -17.92300 1.000 20.49000 ? 497 HOH B O    1 
HETATM 2538 O O    . HOH H 4 .   ? -18.29600 -3.59400  0.49000   1.000 30.53000 ? 498 HOH B O    1 
HETATM 2539 O O    . HOH H 4 .   ? -31.99800 -19.87000 -24.84200 1.000 19.77000 ? 499 HOH B O    1 
HETATM 2540 O O    . HOH H 4 .   ? -32.92800 -6.26900  -6.04800  1.000 20.99000 ? 500 HOH B O    1 
HETATM 2541 O O    . HOH H 4 .   ? -33.70100 -3.25700  -9.61800  1.000 31.50000 ? 501 HOH B O    1 
HETATM 2542 O O    . HOH H 4 .   ? -20.23800 -30.88300 -26.04400 1.000 26.31000 ? 502 HOH B O    1 
HETATM 2543 O O    . HOH H 4 .   ? -19.01400 -8.01300  -21.40500 1.000 19.27000 ? 503 HOH B O    1 
HETATM 2544 O O    . HOH H 4 .   ? -32.87900 -7.26700  -23.40600 1.000 29.85000 ? 504 HOH B O    1 
HETATM 2545 O O    . HOH H 4 .   ? -14.91100 -6.86000  -19.87600 1.000 23.94000 ? 505 HOH B O    1 
HETATM 2546 O O    . HOH H 4 .   ? -23.68300 -13.10700 -13.84100 1.000 26.76000 ? 506 HOH B O    1 
HETATM 2547 O O    . HOH H 4 .   ? -11.51700 -19.35500 2.30700   1.000 27.59000 ? 507 HOH B O    1 
HETATM 2548 O O    . HOH H 4 .   ? -14.28200 -1.49900  -10.36600 1.000 18.37000 ? 508 HOH B O    1 
HETATM 2549 O O    . HOH H 4 .   ? -24.13900 0.27600   -18.13800 1.000 25.65000 ? 509 HOH B O    1 
HETATM 2550 O O    . HOH H 4 .   ? -28.37000 -5.88600  -18.64100 1.000 10.79000 ? 510 HOH B O    1 
HETATM 2551 O O    . HOH H 4 .   ? -32.33600 -17.61000 -17.15400 1.000 26.75000 ? 511 HOH B O    1 
HETATM 2552 O O    . HOH H 4 .   ? -21.34800 1.56600   -14.50300 1.000 26.45000 ? 512 HOH B O    1 
HETATM 2553 O O    . HOH H 4 .   ? -32.47600 -4.38500  -10.79900 1.000 28.06000 ? 513 HOH B O    1 
HETATM 2554 O O    . HOH H 4 .   ? -22.28400 -10.29300 -32.43600 1.000 32.17000 ? 514 HOH B O    1 
HETATM 2555 O O    . HOH H 4 .   ? -24.32200 -6.67400  -30.71100 1.000 35.56000 ? 515 HOH B O    1 
HETATM 2556 O O    . HOH H 4 .   ? -37.51500 -6.20500  -10.57100 1.000 28.10000 ? 516 HOH B O    1 
HETATM 2557 O O    . HOH H 4 .   ? -23.76400 -12.03000 -26.17000 1.000 21.15000 ? 517 HOH B O    1 
HETATM 2558 O O    . HOH H 4 .   ? -13.93800 -7.33400  -22.11700 1.000 29.64000 ? 518 HOH B O    1 
HETATM 2559 O O    . HOH H 4 .   ? -7.051    -30.426   -9.344    1.000 29.13000 ? 519 HOH B O    1 
HETATM 2560 O O    . HOH H 4 .   ? -9.19900  -26.45800 -0.21000  1.000 27.01000 ? 520 HOH B O    1 
HETATM 2561 O O    . HOH H 4 .   ? -32.89800 -5.68500  -8.72800  1.000 26.98000 ? 521 HOH B O    1 
HETATM 2562 O O    . HOH H 4 .   ? -16.53300 -11.72500 3.64800   1.000 26.20000 ? 522 HOH B O    1 
HETATM 2563 O O    . HOH H 4 .   ? -32.35300 -9.05700  -24.31000 1.000 32.20000 ? 523 HOH B O    1 
HETATM 2564 O O    . HOH H 4 .   ? -5.67900  -19.24500 -17.14000 1.000 23.30000 ? 524 HOH B O    1 
HETATM 2565 O O    . HOH H 4 .   ? -7.584    -32.403   -15.010   1.000 27.86000 ? 525 HOH B O    1 
HETATM 2566 O O    . HOH H 4 .   ? -8.89500  -5.34300  -2.49100  1.000 31.96000 ? 526 HOH B O    1 
HETATM 2567 O O    . HOH H 4 .   ? -22.49300 2.24200   -18.14500 1.000 31.63000 ? 527 HOH B O    1 
HETATM 2568 O O    . HOH H 4 .   ? -32.08000 -4.80300  -23.57900 1.000 31.54000 ? 528 HOH B O    1 
HETATM 2569 O O    . HOH H 4 .   ? -33.42100 0.78400   -0.96600  1.000 31.29000 ? 529 HOH B O    1 
HETATM 2570 O O    . HOH H 4 .   ? -37.322   -8.237    -8.955    1.000 29.02000 ? 530 HOH B O    1 
HETATM 2571 O O    . HOH H 4 .   ? -21.53600 -12.13200 -30.63200 1.000 29.36000 ? 531 HOH B O    1 
HETATM 2572 O O    . HOH H 4 .   ? -31.21700 0.28000   -5.60100  1.000 21.49000 ? 532 HOH B O    1 
HETATM 2573 O O    . HOH H 4 .   ? -10.18500 -4.64200  -15.76600 1.000 31.51000 ? 533 HOH B O    1 
HETATM 2574 O O    . HOH H 4 .   ? -10.60300 -23.07300 1.06900   1.000 29.60000 ? 534 HOH B O    1 
HETATM 2575 O O    . HOH H 4 .   ? -37.266   -13.736   -26.196   1.000 30.94000 ? 535 HOH B O    1 
HETATM 2576 O O    . HOH H 4 .   ? -7.04400  -5.95700  -3.36400  1.000 32.56000 ? 536 HOH B O    1 
HETATM 2577 O O    . HOH H 4 .   ? -31.51200 -17.91800 -28.38100 1.000 29.08000 ? 537 HOH B O    1 
HETATM 2578 O O    . HOH H 4 .   ? -9.12100  -18.99500 2.50100   1.000 29.55000 ? 538 HOH B O    1 
HETATM 2579 O O    . HOH H 4 .   ? -27.62500 -28.58400 -23.18500 1.000 34.91000 ? 539 HOH B O    1 
HETATM 2580 O O    . HOH H 4 .   ? -25.390   3.167     -0.252    1.000 28.02000 ? 540 HOH B O    1 
HETATM 2581 O O    . HOH H 4 .   ? -16.84900 -12.71900 1.30500   1.000 28.83000 ? 541 HOH B O    1 
HETATM 2582 O O    . HOH H 4 .   ? -14.00300 -26.59600 -28.07900 1.000 22.16000 ? 542 HOH B O    1 
HETATM 2583 O O    . HOH H 4 .   ? -33.384   -21.174   -6.242    1.000 34.61000 ? 543 HOH B O    1 
HETATM 2584 O O    . HOH H 4 .   ? -15.54700 -4.73600  5.46100   1.000 23.96000 ? 544 HOH B O    1 
HETATM 2585 O O    . HOH H 4 .   ? -21.24400 -11.38400 -27.57900 1.000 20.02000 ? 545 HOH B O    1 
HETATM 2586 O O    . HOH H 4 .   ? -18.50900 -6.63400  -23.74200 1.000 22.83000 ? 546 HOH B O    1 
HETATM 2587 O O    . HOH H 4 .   ? -15.57500 -9.74100  -23.11200 1.000 20.26000 ? 547 HOH B O    1 
HETATM 2588 O O    . HOH H 4 .   ? -21.07400 -6.02100  -24.41400 1.000 20.95000 ? 548 HOH B O    1 
HETATM 2589 O O    . HOH H 4 .   ? -20.58900 -31.92400 -9.58900  1.000 30.33000 ? 549 HOH B O    1 
HETATM 2590 O O    . HOH H 4 .   ? -36.48500 -6.82000  -21.56000 1.000 30.38000 ? 550 HOH B O    1 
HETATM 2591 O O    . HOH H 4 .   ? -29.00000 -25.34600 -26.21900 1.000 30.23000 ? 551 HOH B O    1 
HETATM 2592 O O    . HOH H 4 .   ? -12.42600 -5.64700  -16.73700 1.000 27.34000 ? 552 HOH B O    1 
HETATM 2593 O O    . HOH H 4 .   ? -27.68500 -11.70500 6.47500   1.000 32.83000 ? 553 HOH B O    1 
HETATM 2594 O O    . HOH H 4 .   ? -18.81400 -12.63100 -26.90500 1.000 27.03000 ? 554 HOH B O    1 
HETATM 2595 O O    . HOH H 4 .   ? -28.66200 -23.11500 -24.90200 1.000 22.95000 ? 555 HOH B O    1 
HETATM 2596 O O    . HOH H 4 .   ? -8.33400  -11.25300 -7.08800  1.000 24.27000 ? 556 HOH B O    1 
HETATM 2597 O O    . HOH H 4 .   ? -23.88200 0.21400   3.88800   1.000 37.13000 ? 557 HOH B O    1 
HETATM 2598 O O    . HOH H 4 .   ? -20.01600 -8.77500  -27.81500 1.000 30.08000 ? 558 HOH B O    1 
HETATM 2599 O O    . HOH H 4 .   ? -22.07400 -6.58500  -26.99100 1.000 32.34000 ? 559 HOH B O    1 
# 
