data_8XC2
# 
_entry.id   8XC2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XC2         pdb_00008xc2 10.2210/pdb8xc2/pdb 
WWPDB D_1300043182 ?            ?                   
# 
_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       2024-12-11 
# 
_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                        8XC2 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              yuanhong119@163.com 
_pdbx_contact_author.name_first         yingwu 
_pdbx_contact_author.name_last          lin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2457-0871 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lin, Y.W.' 1 0000-0002-2457-0871 
'Yuan, H.'  2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_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                     'The X-ray structure of F46C myoglobin with a covalently linked Ni-complex' 
_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 'Lin, Y.W.' 1 0000-0002-2457-0871 
primary 'Yuan, H.'  2 ?                   
# 
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 Myoglobin                                                          17190.920 1   ? F46C ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                  616.487   1   ? ?    ? ? 
3 non-polymer syn '4-oxidanylidene-4-(1,10-phenanthrolin-5-ylamino)but-2-enoic acid' 293.277   2   ? ?    ? ? 
4 non-polymer syn 'NICKEL (II) ION'                                                  58.693    1   ? ?    ? ? 
5 water       nat water                                                              18.015    216 ? ?    ? ? 
# 
_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       
;VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRCKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRCKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                  HEM 
3 '4-oxidanylidene-4-(1,10-phenanthrolin-5-ylamino)but-2-enoic acid' Y6C 
4 'NICKEL (II) ION'                                                  NI  
5 water                                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   LEU n 
1 3   SER n 
1 4   GLU n 
1 5   GLY n 
1 6   GLU n 
1 7   TRP n 
1 8   GLN n 
1 9   LEU n 
1 10  VAL n 
1 11  LEU n 
1 12  HIS n 
1 13  VAL n 
1 14  TRP n 
1 15  ALA n 
1 16  LYS n 
1 17  VAL n 
1 18  GLU n 
1 19  ALA n 
1 20  ASP n 
1 21  VAL n 
1 22  ALA n 
1 23  GLY n 
1 24  HIS n 
1 25  GLY n 
1 26  GLN n 
1 27  ASP n 
1 28  ILE n 
1 29  LEU n 
1 30  ILE n 
1 31  ARG n 
1 32  LEU n 
1 33  PHE n 
1 34  LYS n 
1 35  SER n 
1 36  HIS n 
1 37  PRO n 
1 38  GLU n 
1 39  THR n 
1 40  LEU n 
1 41  GLU n 
1 42  LYS n 
1 43  PHE n 
1 44  ASP n 
1 45  ARG n 
1 46  CYS n 
1 47  LYS n 
1 48  HIS n 
1 49  LEU n 
1 50  LYS n 
1 51  THR n 
1 52  GLU n 
1 53  ALA n 
1 54  GLU n 
1 55  MET n 
1 56  LYS n 
1 57  ALA n 
1 58  SER n 
1 59  GLU n 
1 60  ASP n 
1 61  LEU n 
1 62  LYS n 
1 63  LYS n 
1 64  HIS n 
1 65  GLY n 
1 66  VAL n 
1 67  THR n 
1 68  VAL n 
1 69  LEU n 
1 70  THR n 
1 71  ALA n 
1 72  LEU n 
1 73  GLY n 
1 74  ALA n 
1 75  ILE n 
1 76  LEU n 
1 77  LYS n 
1 78  LYS n 
1 79  LYS n 
1 80  GLY n 
1 81  HIS n 
1 82  HIS n 
1 83  GLU n 
1 84  ALA n 
1 85  GLU n 
1 86  LEU n 
1 87  LYS n 
1 88  PRO n 
1 89  LEU n 
1 90  ALA n 
1 91  GLN n 
1 92  SER n 
1 93  HIS n 
1 94  ALA n 
1 95  THR n 
1 96  LYS n 
1 97  HIS n 
1 98  LYS n 
1 99  ILE n 
1 100 PRO n 
1 101 ILE n 
1 102 LYS n 
1 103 TYR n 
1 104 LEU n 
1 105 GLU n 
1 106 PHE n 
1 107 ILE n 
1 108 SER n 
1 109 GLU n 
1 110 ALA n 
1 111 ILE n 
1 112 ILE n 
1 113 HIS n 
1 114 VAL n 
1 115 LEU n 
1 116 HIS n 
1 117 SER n 
1 118 ARG n 
1 119 HIS n 
1 120 PRO n 
1 121 GLY n 
1 122 ASP n 
1 123 PHE n 
1 124 GLY n 
1 125 ALA n 
1 126 ASP n 
1 127 ALA n 
1 128 GLN n 
1 129 GLY n 
1 130 ALA n 
1 131 MET n 
1 132 ASN n 
1 133 LYS n 
1 134 ALA n 
1 135 LEU n 
1 136 GLU n 
1 137 LEU n 
1 138 PHE n 
1 139 ARG n 
1 140 LYS n 
1 141 ASP n 
1 142 ILE n 
1 143 ALA n 
1 144 ALA n 
1 145 LYS n 
1 146 TYR n 
1 147 LYS n 
1 148 GLU n 
1 149 LEU n 
1 150 GLY n 
1 151 TYR n 
1 152 GLN n 
1 153 GLY 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                   153 
_entity_src_gen.gene_src_common_name               'sperm whale' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MB 
_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      'Physeter catodon' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9755 
_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 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                  HEME 'C34 H32 Fe N4 O4' 616.487 
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 
NI  non-polymer         . 'NICKEL (II) ION'                                                  ?    'Ni 2'             58.693  
PHE 'L-peptide linking' y PHENYLALANINE                                                      ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                            ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                             ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                          ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                         ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                           ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                             ?    'C5 H11 N O2'      117.146 
Y6C non-polymer         . '4-oxidanylidene-4-(1,10-phenanthrolin-5-ylamino)but-2-enoic acid' ?    'C16 H11 N3 O3'    293.277 
# 
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   VAL 1   1   1   VAL VAL A . n 
A 1 2   LEU 2   2   2   LEU LEU A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  GLU 38  38  38  GLU GLU 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  GLU 41  41  41  GLU GLU A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  MET 55  55  55  MET MET A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  LYS 63  63  63  LYS LYS A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  HIS 82  82  82  HIS HIS A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  HIS 97  97  97  HIS HIS A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        Y6C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Y6C 
_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 
B 2 HEM 1   201 201 HEM HEM A . 
C 3 Y6C 1   202 202 Y6C PAM A . 
D 3 Y6C 1   203 203 Y6C PAM A . 
E 4 NI  1   204 1   NI  NI  A . 
F 5 HOH 1   301 196 HOH HOH A . 
F 5 HOH 2   302 1   HOH HOH A . 
F 5 HOH 3   303 117 HOH HOH A . 
F 5 HOH 4   304 191 HOH HOH A . 
F 5 HOH 5   305 216 HOH HOH A . 
F 5 HOH 6   306 48  HOH HOH A . 
F 5 HOH 7   307 76  HOH HOH A . 
F 5 HOH 8   308 23  HOH HOH A . 
F 5 HOH 9   309 135 HOH HOH A . 
F 5 HOH 10  310 15  HOH HOH A . 
F 5 HOH 11  311 203 HOH HOH A . 
F 5 HOH 12  312 146 HOH HOH A . 
F 5 HOH 13  313 118 HOH HOH A . 
F 5 HOH 14  314 206 HOH HOH A . 
F 5 HOH 15  315 49  HOH HOH A . 
F 5 HOH 16  316 37  HOH HOH A . 
F 5 HOH 17  317 38  HOH HOH A . 
F 5 HOH 18  318 53  HOH HOH A . 
F 5 HOH 19  319 65  HOH HOH A . 
F 5 HOH 20  320 44  HOH HOH A . 
F 5 HOH 21  321 142 HOH HOH A . 
F 5 HOH 22  322 21  HOH HOH A . 
F 5 HOH 23  323 161 HOH HOH A . 
F 5 HOH 24  324 215 HOH HOH A . 
F 5 HOH 25  325 83  HOH HOH A . 
F 5 HOH 26  326 103 HOH HOH A . 
F 5 HOH 27  327 52  HOH HOH A . 
F 5 HOH 28  328 148 HOH HOH A . 
F 5 HOH 29  329 124 HOH HOH A . 
F 5 HOH 30  330 19  HOH HOH A . 
F 5 HOH 31  331 144 HOH HOH A . 
F 5 HOH 32  332 82  HOH HOH A . 
F 5 HOH 33  333 54  HOH HOH A . 
F 5 HOH 34  334 61  HOH HOH A . 
F 5 HOH 35  335 122 HOH HOH A . 
F 5 HOH 36  336 30  HOH HOH A . 
F 5 HOH 37  337 147 HOH HOH A . 
F 5 HOH 38  338 182 HOH HOH A . 
F 5 HOH 39  339 73  HOH HOH A . 
F 5 HOH 40  340 66  HOH HOH A . 
F 5 HOH 41  341 72  HOH HOH A . 
F 5 HOH 42  342 3   HOH HOH A . 
F 5 HOH 43  343 27  HOH HOH A . 
F 5 HOH 44  344 46  HOH HOH A . 
F 5 HOH 45  345 25  HOH HOH A . 
F 5 HOH 46  346 183 HOH HOH A . 
F 5 HOH 47  347 18  HOH HOH A . 
F 5 HOH 48  348 79  HOH HOH A . 
F 5 HOH 49  349 31  HOH HOH A . 
F 5 HOH 50  350 120 HOH HOH A . 
F 5 HOH 51  351 74  HOH HOH A . 
F 5 HOH 52  352 80  HOH HOH A . 
F 5 HOH 53  353 104 HOH HOH A . 
F 5 HOH 54  354 153 HOH HOH A . 
F 5 HOH 55  355 98  HOH HOH A . 
F 5 HOH 56  356 17  HOH HOH A . 
F 5 HOH 57  357 42  HOH HOH A . 
F 5 HOH 58  358 143 HOH HOH A . 
F 5 HOH 59  359 36  HOH HOH A . 
F 5 HOH 60  360 96  HOH HOH A . 
F 5 HOH 61  361 214 HOH HOH A . 
F 5 HOH 62  362 16  HOH HOH A . 
F 5 HOH 63  363 71  HOH HOH A . 
F 5 HOH 64  364 132 HOH HOH A . 
F 5 HOH 65  365 60  HOH HOH A . 
F 5 HOH 66  366 39  HOH HOH A . 
F 5 HOH 67  367 177 HOH HOH A . 
F 5 HOH 68  368 166 HOH HOH A . 
F 5 HOH 69  369 12  HOH HOH A . 
F 5 HOH 70  370 8   HOH HOH A . 
F 5 HOH 71  371 181 HOH HOH A . 
F 5 HOH 72  372 68  HOH HOH A . 
F 5 HOH 73  373 100 HOH HOH A . 
F 5 HOH 74  374 130 HOH HOH A . 
F 5 HOH 75  375 173 HOH HOH A . 
F 5 HOH 76  376 6   HOH HOH A . 
F 5 HOH 77  377 163 HOH HOH A . 
F 5 HOH 78  378 58  HOH HOH A . 
F 5 HOH 79  379 192 HOH HOH A . 
F 5 HOH 80  380 20  HOH HOH A . 
F 5 HOH 81  381 5   HOH HOH A . 
F 5 HOH 82  382 64  HOH HOH A . 
F 5 HOH 83  383 95  HOH HOH A . 
F 5 HOH 84  384 86  HOH HOH A . 
F 5 HOH 85  385 4   HOH HOH A . 
F 5 HOH 86  386 9   HOH HOH A . 
F 5 HOH 87  387 139 HOH HOH A . 
F 5 HOH 88  388 56  HOH HOH A . 
F 5 HOH 89  389 107 HOH HOH A . 
F 5 HOH 90  390 119 HOH HOH A . 
F 5 HOH 91  391 101 HOH HOH A . 
F 5 HOH 92  392 51  HOH HOH A . 
F 5 HOH 93  393 29  HOH HOH A . 
F 5 HOH 94  394 35  HOH HOH A . 
F 5 HOH 95  395 50  HOH HOH A . 
F 5 HOH 96  396 69  HOH HOH A . 
F 5 HOH 97  397 125 HOH HOH A . 
F 5 HOH 98  398 14  HOH HOH A . 
F 5 HOH 99  399 7   HOH HOH A . 
F 5 HOH 100 400 11  HOH HOH A . 
F 5 HOH 101 401 205 HOH HOH A . 
F 5 HOH 102 402 62  HOH HOH A . 
F 5 HOH 103 403 89  HOH HOH A . 
F 5 HOH 104 404 28  HOH HOH A . 
F 5 HOH 105 405 55  HOH HOH A . 
F 5 HOH 106 406 195 HOH HOH A . 
F 5 HOH 107 407 197 HOH HOH A . 
F 5 HOH 108 408 26  HOH HOH A . 
F 5 HOH 109 409 88  HOH HOH A . 
F 5 HOH 110 410 209 HOH HOH A . 
F 5 HOH 111 411 78  HOH HOH A . 
F 5 HOH 112 412 59  HOH HOH A . 
F 5 HOH 113 413 193 HOH HOH A . 
F 5 HOH 114 414 112 HOH HOH A . 
F 5 HOH 115 415 152 HOH HOH A . 
F 5 HOH 116 416 90  HOH HOH A . 
F 5 HOH 117 417 126 HOH HOH A . 
F 5 HOH 118 418 22  HOH HOH A . 
F 5 HOH 119 419 116 HOH HOH A . 
F 5 HOH 120 420 159 HOH HOH A . 
F 5 HOH 121 421 84  HOH HOH A . 
F 5 HOH 122 422 200 HOH HOH A . 
F 5 HOH 123 423 102 HOH HOH A . 
F 5 HOH 124 424 43  HOH HOH A . 
F 5 HOH 125 425 158 HOH HOH A . 
F 5 HOH 126 426 175 HOH HOH A . 
F 5 HOH 127 427 97  HOH HOH A . 
F 5 HOH 128 428 185 HOH HOH A . 
F 5 HOH 129 429 85  HOH HOH A . 
F 5 HOH 130 430 115 HOH HOH A . 
F 5 HOH 131 431 207 HOH HOH A . 
F 5 HOH 132 432 108 HOH HOH A . 
F 5 HOH 133 433 154 HOH HOH A . 
F 5 HOH 134 434 150 HOH HOH A . 
F 5 HOH 135 435 140 HOH HOH A . 
F 5 HOH 136 436 91  HOH HOH A . 
F 5 HOH 137 437 67  HOH HOH A . 
F 5 HOH 138 438 75  HOH HOH A . 
F 5 HOH 139 439 212 HOH HOH A . 
F 5 HOH 140 440 92  HOH HOH A . 
F 5 HOH 141 441 171 HOH HOH A . 
F 5 HOH 142 442 211 HOH HOH A . 
F 5 HOH 143 443 145 HOH HOH A . 
F 5 HOH 144 444 114 HOH HOH A . 
F 5 HOH 145 445 77  HOH HOH A . 
F 5 HOH 146 446 57  HOH HOH A . 
F 5 HOH 147 447 13  HOH HOH A . 
F 5 HOH 148 448 176 HOH HOH A . 
F 5 HOH 149 449 111 HOH HOH A . 
F 5 HOH 150 450 47  HOH HOH A . 
F 5 HOH 151 451 167 HOH HOH A . 
F 5 HOH 152 452 198 HOH HOH A . 
F 5 HOH 153 453 81  HOH HOH A . 
F 5 HOH 154 454 87  HOH HOH A . 
F 5 HOH 155 455 210 HOH HOH A . 
F 5 HOH 156 456 113 HOH HOH A . 
F 5 HOH 157 457 141 HOH HOH A . 
F 5 HOH 158 458 169 HOH HOH A . 
F 5 HOH 159 459 134 HOH HOH A . 
F 5 HOH 160 460 151 HOH HOH A . 
F 5 HOH 161 461 164 HOH HOH A . 
F 5 HOH 162 462 121 HOH HOH A . 
F 5 HOH 163 463 136 HOH HOH A . 
F 5 HOH 164 464 170 HOH HOH A . 
F 5 HOH 165 465 186 HOH HOH A . 
F 5 HOH 166 466 123 HOH HOH A . 
F 5 HOH 167 467 160 HOH HOH A . 
F 5 HOH 168 468 99  HOH HOH A . 
F 5 HOH 169 469 129 HOH HOH A . 
F 5 HOH 170 470 110 HOH HOH A . 
F 5 HOH 171 471 157 HOH HOH A . 
F 5 HOH 172 472 179 HOH HOH A . 
F 5 HOH 173 473 174 HOH HOH A . 
F 5 HOH 174 474 109 HOH HOH A . 
F 5 HOH 175 475 137 HOH HOH A . 
F 5 HOH 176 476 156 HOH HOH A . 
F 5 HOH 177 477 138 HOH HOH A . 
F 5 HOH 178 478 93  HOH HOH A . 
F 5 HOH 179 479 41  HOH HOH A . 
F 5 HOH 180 480 131 HOH HOH A . 
F 5 HOH 181 481 155 HOH HOH A . 
F 5 HOH 182 482 94  HOH HOH A . 
F 5 HOH 183 483 45  HOH HOH A . 
F 5 HOH 184 484 149 HOH HOH A . 
F 5 HOH 185 485 162 HOH HOH A . 
F 5 HOH 186 486 190 HOH HOH A . 
F 5 HOH 187 487 168 HOH HOH A . 
F 5 HOH 188 488 63  HOH HOH A . 
F 5 HOH 189 489 184 HOH HOH A . 
F 5 HOH 190 490 202 HOH HOH A . 
F 5 HOH 191 491 24  HOH HOH A . 
F 5 HOH 192 492 188 HOH HOH A . 
F 5 HOH 193 493 32  HOH HOH A . 
F 5 HOH 194 494 34  HOH HOH A . 
F 5 HOH 195 495 10  HOH HOH A . 
F 5 HOH 196 496 194 HOH HOH A . 
F 5 HOH 197 497 180 HOH HOH A . 
F 5 HOH 198 498 187 HOH HOH A . 
F 5 HOH 199 499 213 HOH HOH A . 
F 5 HOH 200 500 2   HOH HOH A . 
F 5 HOH 201 501 178 HOH HOH A . 
F 5 HOH 202 502 189 HOH HOH A . 
F 5 HOH 203 503 105 HOH HOH A . 
F 5 HOH 204 504 128 HOH HOH A . 
F 5 HOH 205 505 133 HOH HOH A . 
F 5 HOH 206 506 201 HOH HOH A . 
F 5 HOH 207 507 40  HOH HOH A . 
F 5 HOH 208 508 33  HOH HOH A . 
F 5 HOH 209 509 199 HOH HOH A . 
F 5 HOH 210 510 172 HOH HOH A . 
F 5 HOH 211 511 70  HOH HOH A . 
F 5 HOH 212 512 127 HOH HOH A . 
F 5 HOH 213 513 208 HOH HOH A . 
F 5 HOH 214 514 106 HOH HOH A . 
F 5 HOH 215 515 204 HOH HOH A . 
F 5 HOH 216 516 165 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.18.1_3865 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XC2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.827 
_cell.length_a_esd                 ? 
_cell.length_b                     49.215 
_cell.length_b_esd                 ? 
_cell.length_c                     76.748 
_cell.length_c_esd                 ? 
_cell.volume                       150432.665 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8XC2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8XC2 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.78 
_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    PEG8000 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 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         2023-10-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9791 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          16.12 
_reflns.entry_id                                       8XC2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               50 
_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                                     496250 
_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                           99.88 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          29.18 
_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                                0.016 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.052 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.97 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2441 
_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                               8.6 
_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                               0.157 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.92 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.435 
_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                               21.69 
_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                                 8XC2 
_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                            1.50 
_refine.ls_d_res_low                             22.70 
_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                     46615 
_refine.ls_number_reflns_R_free                  2445 
_refine.ls_number_reflns_R_work                  44170 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_percent_reflns_R_free                 5.25 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1771 
_refine.ls_R_factor_R_free                       0.1863 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1766 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.8224 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1194 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        22.70 
_refine_hist.number_atoms_solvent             216 
_refine_hist.number_atoms_total               1515 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1211 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         88 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0158  ? 1394 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.6902  ? 1898 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0942  ? 189  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0106  ? 237  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 24.0853 ? 537  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.53  . . 145 2625 99.75  . . . . 0.2442 . . . . . . . . . . . 0.2393 
'X-RAY DIFFRACTION' 1.53 1.56  . . 137 2539 99.93  . . . . 0.2045 . . . . . . . . . . . 0.2533 
'X-RAY DIFFRACTION' 1.56 1.60  . . 139 2666 99.68  . . . . 0.1970 . . . . . . . . . . . 0.1856 
'X-RAY DIFFRACTION' 1.60 1.64  . . 143 2554 99.89  . . . . 0.1946 . . . . . . . . . . . 0.2116 
'X-RAY DIFFRACTION' 1.64 1.68  . . 147 2615 99.86  . . . . 0.1974 . . . . . . . . . . . 0.1990 
'X-RAY DIFFRACTION' 1.68 1.73  . . 144 2586 99.85  . . . . 0.1853 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 1.73 1.79  . . 148 2580 100.00 . . . . 0.1841 . . . . . . . . . . . 0.1956 
'X-RAY DIFFRACTION' 1.79 1.85  . . 137 2609 99.96  . . . . 0.1783 . . . . . . . . . . . 0.1831 
'X-RAY DIFFRACTION' 1.85 1.93  . . 142 2614 99.89  . . . . 0.1736 . . . . . . . . . . . 0.1799 
'X-RAY DIFFRACTION' 1.93 2.02  . . 148 2596 100.00 . . . . 0.1793 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.02 2.12  . . 145 2621 100.00 . . . . 0.1750 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 2.12 2.26  . . 147 2580 100.00 . . . . 0.1674 . . . . . . . . . . . 0.1679 
'X-RAY DIFFRACTION' 2.26 2.43  . . 142 2603 99.89  . . . . 0.1722 . . . . . . . . . . . 0.1704 
'X-RAY DIFFRACTION' 2.43 2.67  . . 143 2608 100.00 . . . . 0.1739 . . . . . . . . . . . 0.1884 
'X-RAY DIFFRACTION' 2.67 3.06  . . 144 2603 100.00 . . . . 0.1792 . . . . . . . . . . . 0.1968 
'X-RAY DIFFRACTION' 3.06 3.85  . . 149 2580 99.96  . . . . 0.1618 . . . . . . . . . . . 0.1910 
'X-RAY DIFFRACTION' 3.85 22.70 . . 145 2591 99.60  . . . . 0.1757 . . . . . . . . . . . 0.1705 
# 
_struct.entry_id                     8XC2 
_struct.title                        'The X-ray structure of F46C myoglobin with a covalently linked Ni-complex' 
_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        8XC2 
_struct_keywords.text            'MYOGLOBIN, OXYGEN STORAGE' 
_struct_keywords.pdbx_keywords   'OXYGEN STORAGE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MYG_PHYMC 
_struct_ref.pdbx_db_accession          P02185 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XC2 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 153 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02185 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  154 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       153 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8XC2 
_struct_ref_seq_dif.mon_id                       CYS 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      46 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P02185 
_struct_ref_seq_dif.db_mon_id                    PHE 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          47 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            46 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1230 ? 
1 MORE         -32  ? 
1 'SSA (A^2)'  8170 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 SER A 3   ? ALA A 19  ? SER A 3   ALA A 19  1 ? 17 
HELX_P HELX_P2 AA2 ASP A 20  ? HIS A 36  ? ASP A 20  HIS A 36  1 ? 17 
HELX_P HELX_P3 AA3 PRO A 37  ? PHE A 43  ? PRO A 37  PHE A 43  5 ? 7  
HELX_P HELX_P4 AA4 THR A 51  ? SER A 58  ? THR A 51  SER A 58  1 ? 8  
HELX_P HELX_P5 AA5 SER A 58  ? LYS A 78  ? SER A 58  LYS A 78  1 ? 21 
HELX_P HELX_P6 AA6 HIS A 82  ? LYS A 96  ? HIS A 82  LYS A 96  1 ? 15 
HELX_P HELX_P7 AA7 PRO A 100 ? HIS A 119 ? PRO A 100 HIS A 119 1 ? 20 
HELX_P HELX_P8 AA8 PRO A 120 ? PHE A 123 ? PRO A 120 PHE A 123 5 ? 4  
HELX_P HELX_P9 AA9 GLY A 124 ? LEU A 149 ? GLY A 124 LEU A 149 1 ? 26 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 46 SG  ? ? ? 1_555 C Y6C . CAT ? ? A CYS 46  A Y6C 202 1_555 ? ? ? ? ? ? ? 1.802 ? ? 
metalc1 metalc ?    ? A HIS 64 NE2 ? ? ? 1_555 E NI  . NI  ? ? A HIS 64  A NI  204 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc2 metalc ?    ? A HIS 93 NE2 ? ? ? 1_555 B HEM . FE  ? ? A HIS 93  A HEM 201 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc3 metalc ?    ? B HEM .  FE  ? ? ? 1_555 F HOH . O   ? ? A HEM 201 A HOH 369 1_555 ? ? ? ? ? ? ? 2.255 ? ? 
metalc4 metalc ?    ? C Y6C .  NAJ ? ? ? 1_555 E NI  . NI  ? ? A Y6C 202 A NI  204 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc5 metalc ?    ? C Y6C .  NAK ? ? ? 1_555 E NI  . NI  ? ? A Y6C 202 A NI  204 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc6 metalc ?    ? E NI  .  NI  ? ? ? 1_555 F HOH . O   ? ? A NI  204 A HOH 312 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc7 metalc ?    ? E NI  .  NI  ? ? ? 1_555 F HOH . O   ? ? A NI  204 A HOH 391 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 64 ? A HIS 64  ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 NAJ ? C Y6C . ? A Y6C 202 ? 1_555 92.7  ? 
2  NE2 ? A HIS 64 ? A HIS 64  ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 NAK ? C Y6C . ? A Y6C 202 ? 1_555 170.5 ? 
3  NAJ ? C Y6C .  ? A Y6C 202 ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 NAK ? C Y6C . ? A Y6C 202 ? 1_555 84.7  ? 
4  NE2 ? A HIS 64 ? A HIS 64  ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 312 ? 1_555 92.8  ? 
5  NAJ ? C Y6C .  ? A Y6C 202 ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 312 ? 1_555 170.9 ? 
6  NAK ? C Y6C .  ? A Y6C 202 ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 312 ? 1_555 88.7  ? 
7  NE2 ? A HIS 64 ? A HIS 64  ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 391 ? 1_555 89.7  ? 
8  NAJ ? C Y6C .  ? A Y6C 202 ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 391 ? 1_555 88.2  ? 
9  NAK ? C Y6C .  ? A Y6C 202 ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 391 ? 1_555 81.2  ? 
10 O   ? F HOH .  ? A HOH 312 ? 1_555 NI ? E NI  . ? A NI  204 ? 1_555 O   ? F HOH . ? A HOH 391 ? 1_555 84.7  ? 
11 NE2 ? A HIS 93 ? A HIS 93  ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 NA  ? B HEM . ? A HEM 201 ? 1_555 90.6  ? 
12 NE2 ? A HIS 93 ? A HIS 93  ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 NB  ? B HEM . ? A HEM 201 ? 1_555 93.1  ? 
13 NA  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 NB  ? B HEM . ? A HEM 201 ? 1_555 90.2  ? 
14 NE2 ? A HIS 93 ? A HIS 93  ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 NC  ? B HEM . ? A HEM 201 ? 1_555 97.3  ? 
15 NA  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 NC  ? B HEM . ? A HEM 201 ? 1_555 171.9 ? 
16 NB  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 NC  ? B HEM . ? A HEM 201 ? 1_555 88.0  ? 
17 NE2 ? A HIS 93 ? A HIS 93  ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 ND  ? B HEM . ? A HEM 201 ? 1_555 95.5  ? 
18 NA  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 ND  ? B HEM . ? A HEM 201 ? 1_555 90.0  ? 
19 NB  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 ND  ? B HEM . ? A HEM 201 ? 1_555 171.4 ? 
20 NC  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 ND  ? B HEM . ? A HEM 201 ? 1_555 90.6  ? 
21 NE2 ? A HIS 93 ? A HIS 93  ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 O   ? F HOH . ? A HOH 369 ? 1_555 175.5 ? 
22 NA  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 O   ? F HOH . ? A HOH 369 ? 1_555 89.8  ? 
23 NB  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 O   ? F HOH . ? A HOH 369 ? 1_555 91.5  ? 
24 NC  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 O   ? F HOH . ? A HOH 369 ? 1_555 82.5  ? 
25 ND  ? B HEM .  ? A HEM 201 ? 1_555 FE ? B HEM . ? A HEM 201 ? 1_555 O   ? F HOH . ? A HOH 369 ? 1_555 79.9  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      Y6C 
_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     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      46 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       Y6C 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        202 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       46 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               CAT 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        Y6C 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
_pdbx_entry_details.entry_id                   8XC2 
_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 OD2 A ASP 60  ? ? NI  A NI  204 ? ? 1.67 
2 1 SG  A CYS 46  ? ? CAT A Y6C 203 ? ? 1.86 
3 1 O   A HOH 302 ? ? O   A HOH 337 ? ? 2.03 
4 1 OAM A Y6C 203 ? ? O   A HOH 301 ? ? 2.03 
5 1 O   A HOH 369 ? ? O   A HOH 460 ? ? 2.09 
6 1 OD1 A ASP 122 ? ? O   A HOH 302 ? ? 2.13 
# 
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 ASP A 20  ? ? -155.45 80.46 
2 1 LYS A 98  ? ? 61.32   63.44 
3 1 PHE A 123 ? ? -148.99 50.57 
4 1 GLN A 152 ? ? -98.39  30.43 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ARG 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    45 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   CYS 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    46 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -94.38 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
HOH O    O  N N 233 
HOH H1   H  N N 234 
HOH H2   H  N N 235 
ILE N    N  N N 236 
ILE CA   C  N S 237 
ILE C    C  N N 238 
ILE O    O  N N 239 
ILE CB   C  N S 240 
ILE CG1  C  N N 241 
ILE CG2  C  N N 242 
ILE CD1  C  N N 243 
ILE OXT  O  N N 244 
ILE H    H  N N 245 
ILE H2   H  N N 246 
ILE HA   H  N N 247 
ILE HB   H  N N 248 
ILE HG12 H  N N 249 
ILE HG13 H  N N 250 
ILE HG21 H  N N 251 
ILE HG22 H  N N 252 
ILE HG23 H  N N 253 
ILE HD11 H  N N 254 
ILE HD12 H  N N 255 
ILE HD13 H  N N 256 
ILE HXT  H  N N 257 
LEU N    N  N N 258 
LEU CA   C  N S 259 
LEU C    C  N N 260 
LEU O    O  N N 261 
LEU CB   C  N N 262 
LEU CG   C  N N 263 
LEU CD1  C  N N 264 
LEU CD2  C  N N 265 
LEU OXT  O  N N 266 
LEU H    H  N N 267 
LEU H2   H  N N 268 
LEU HA   H  N N 269 
LEU HB2  H  N N 270 
LEU HB3  H  N N 271 
LEU HG   H  N N 272 
LEU HD11 H  N N 273 
LEU HD12 H  N N 274 
LEU HD13 H  N N 275 
LEU HD21 H  N N 276 
LEU HD22 H  N N 277 
LEU HD23 H  N N 278 
LEU HXT  H  N N 279 
LYS N    N  N N 280 
LYS CA   C  N S 281 
LYS C    C  N N 282 
LYS O    O  N N 283 
LYS CB   C  N N 284 
LYS CG   C  N N 285 
LYS CD   C  N N 286 
LYS CE   C  N N 287 
LYS NZ   N  N N 288 
LYS OXT  O  N N 289 
LYS H    H  N N 290 
LYS H2   H  N N 291 
LYS HA   H  N N 292 
LYS HB2  H  N N 293 
LYS HB3  H  N N 294 
LYS HG2  H  N N 295 
LYS HG3  H  N N 296 
LYS HD2  H  N N 297 
LYS HD3  H  N N 298 
LYS HE2  H  N N 299 
LYS HE3  H  N N 300 
LYS HZ1  H  N N 301 
LYS HZ2  H  N N 302 
LYS HZ3  H  N N 303 
LYS HXT  H  N N 304 
MET N    N  N N 305 
MET CA   C  N S 306 
MET C    C  N N 307 
MET O    O  N N 308 
MET CB   C  N N 309 
MET CG   C  N N 310 
MET SD   S  N N 311 
MET CE   C  N N 312 
MET OXT  O  N N 313 
MET H    H  N N 314 
MET H2   H  N N 315 
MET HA   H  N N 316 
MET HB2  H  N N 317 
MET HB3  H  N N 318 
MET HG2  H  N N 319 
MET HG3  H  N N 320 
MET HE1  H  N N 321 
MET HE2  H  N N 322 
MET HE3  H  N N 323 
MET HXT  H  N N 324 
NI  NI   NI N N 325 
PHE N    N  N N 326 
PHE CA   C  N S 327 
PHE C    C  N N 328 
PHE O    O  N N 329 
PHE CB   C  N N 330 
PHE CG   C  Y N 331 
PHE CD1  C  Y N 332 
PHE CD2  C  Y N 333 
PHE CE1  C  Y N 334 
PHE CE2  C  Y N 335 
PHE CZ   C  Y N 336 
PHE OXT  O  N N 337 
PHE H    H  N N 338 
PHE H2   H  N N 339 
PHE HA   H  N N 340 
PHE HB2  H  N N 341 
PHE HB3  H  N N 342 
PHE HD1  H  N N 343 
PHE HD2  H  N N 344 
PHE HE1  H  N N 345 
PHE HE2  H  N N 346 
PHE HZ   H  N N 347 
PHE HXT  H  N N 348 
PRO N    N  N N 349 
PRO CA   C  N S 350 
PRO C    C  N N 351 
PRO O    O  N N 352 
PRO CB   C  N N 353 
PRO CG   C  N N 354 
PRO CD   C  N N 355 
PRO OXT  O  N N 356 
PRO H    H  N N 357 
PRO HA   H  N N 358 
PRO HB2  H  N N 359 
PRO HB3  H  N N 360 
PRO HG2  H  N N 361 
PRO HG3  H  N N 362 
PRO HD2  H  N N 363 
PRO HD3  H  N N 364 
PRO HXT  H  N N 365 
SER N    N  N N 366 
SER CA   C  N S 367 
SER C    C  N N 368 
SER O    O  N N 369 
SER CB   C  N N 370 
SER OG   O  N N 371 
SER OXT  O  N N 372 
SER H    H  N N 373 
SER H2   H  N N 374 
SER HA   H  N N 375 
SER HB2  H  N N 376 
SER HB3  H  N N 377 
SER HG   H  N N 378 
SER HXT  H  N N 379 
THR N    N  N N 380 
THR CA   C  N S 381 
THR C    C  N N 382 
THR O    O  N N 383 
THR CB   C  N R 384 
THR OG1  O  N N 385 
THR CG2  C  N N 386 
THR OXT  O  N N 387 
THR H    H  N N 388 
THR H2   H  N N 389 
THR HA   H  N N 390 
THR HB   H  N N 391 
THR HG1  H  N N 392 
THR HG21 H  N N 393 
THR HG22 H  N N 394 
THR HG23 H  N N 395 
THR HXT  H  N N 396 
TRP N    N  N N 397 
TRP CA   C  N S 398 
TRP C    C  N N 399 
TRP O    O  N N 400 
TRP CB   C  N N 401 
TRP CG   C  Y N 402 
TRP CD1  C  Y N 403 
TRP CD2  C  Y N 404 
TRP NE1  N  Y N 405 
TRP CE2  C  Y N 406 
TRP CE3  C  Y N 407 
TRP CZ2  C  Y N 408 
TRP CZ3  C  Y N 409 
TRP CH2  C  Y N 410 
TRP OXT  O  N N 411 
TRP H    H  N N 412 
TRP H2   H  N N 413 
TRP HA   H  N N 414 
TRP HB2  H  N N 415 
TRP HB3  H  N N 416 
TRP HD1  H  N N 417 
TRP HE1  H  N N 418 
TRP HE3  H  N N 419 
TRP HZ2  H  N N 420 
TRP HZ3  H  N N 421 
TRP HH2  H  N N 422 
TRP HXT  H  N N 423 
TYR N    N  N N 424 
TYR CA   C  N S 425 
TYR C    C  N N 426 
TYR O    O  N N 427 
TYR CB   C  N N 428 
TYR CG   C  Y N 429 
TYR CD1  C  Y N 430 
TYR CD2  C  Y N 431 
TYR CE1  C  Y N 432 
TYR CE2  C  Y N 433 
TYR CZ   C  Y N 434 
TYR OH   O  N N 435 
TYR OXT  O  N N 436 
TYR H    H  N N 437 
TYR H2   H  N N 438 
TYR HA   H  N N 439 
TYR HB2  H  N N 440 
TYR HB3  H  N N 441 
TYR HD1  H  N N 442 
TYR HD2  H  N N 443 
TYR HE1  H  N N 444 
TYR HE2  H  N N 445 
TYR HH   H  N N 446 
TYR HXT  H  N N 447 
VAL N    N  N N 448 
VAL CA   C  N S 449 
VAL C    C  N N 450 
VAL O    O  N N 451 
VAL CB   C  N N 452 
VAL CG1  C  N N 453 
VAL CG2  C  N N 454 
VAL OXT  O  N N 455 
VAL H    H  N N 456 
VAL H2   H  N N 457 
VAL HA   H  N N 458 
VAL HB   H  N N 459 
VAL HG11 H  N N 460 
VAL HG12 H  N N 461 
VAL HG13 H  N N 462 
VAL HG21 H  N N 463 
VAL HG22 H  N N 464 
VAL HG23 H  N N 465 
VAL HXT  H  N N 466 
Y6C CAA  C  N N 467 
Y6C CAC  C  Y N 468 
Y6C CAD  C  Y N 469 
Y6C CAE  C  Y N 470 
Y6C CAF  C  Y N 471 
Y6C CAG  C  Y N 472 
Y6C CAH  C  Y N 473 
Y6C CAI  C  Y N 474 
Y6C CAM  C  N N 475 
Y6C CAN  C  Y N 476 
Y6C CAO  C  Y N 477 
Y6C CAP  C  Y N 478 
Y6C CAQ  C  Y N 479 
Y6C CAR  C  Y N 480 
Y6C NAJ  N  Y N 481 
Y6C NAK  N  Y N 482 
Y6C NAL  N  N N 483 
Y6C OAB  O  N N 484 
Y6C OAM  O  N N 485 
Y6C CAS  C  N N 486 
Y6C CAT  C  N N 487 
Y6C OAS  O  N N 488 
Y6C HAA  H  N N 489 
Y6C HAC  H  N N 490 
Y6C HAD  H  N N 491 
Y6C HAE  H  N N 492 
Y6C HAF  H  N N 493 
Y6C HAG  H  N N 494 
Y6C HAH  H  N N 495 
Y6C HAI  H  N N 496 
Y6C HNAL H  N N 497 
Y6C H1   H  N N 498 
Y6C HAAB H  N N 499 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
HOH O   H1   sing N N 232 
HOH O   H2   sing N N 233 
ILE N   CA   sing N N 234 
ILE N   H    sing N N 235 
ILE N   H2   sing N N 236 
ILE CA  C    sing N N 237 
ILE CA  CB   sing N N 238 
ILE CA  HA   sing N N 239 
ILE C   O    doub N N 240 
ILE C   OXT  sing N N 241 
ILE CB  CG1  sing N N 242 
ILE CB  CG2  sing N N 243 
ILE CB  HB   sing N N 244 
ILE CG1 CD1  sing N N 245 
ILE CG1 HG12 sing N N 246 
ILE CG1 HG13 sing N N 247 
ILE CG2 HG21 sing N N 248 
ILE CG2 HG22 sing N N 249 
ILE CG2 HG23 sing N N 250 
ILE CD1 HD11 sing N N 251 
ILE CD1 HD12 sing N N 252 
ILE CD1 HD13 sing N N 253 
ILE OXT HXT  sing N N 254 
LEU N   CA   sing N N 255 
LEU N   H    sing N N 256 
LEU N   H2   sing N N 257 
LEU CA  C    sing N N 258 
LEU CA  CB   sing N N 259 
LEU CA  HA   sing N N 260 
LEU C   O    doub N N 261 
LEU C   OXT  sing N N 262 
LEU CB  CG   sing N N 263 
LEU CB  HB2  sing N N 264 
LEU CB  HB3  sing N N 265 
LEU CG  CD1  sing N N 266 
LEU CG  CD2  sing N N 267 
LEU CG  HG   sing N N 268 
LEU CD1 HD11 sing N N 269 
LEU CD1 HD12 sing N N 270 
LEU CD1 HD13 sing N N 271 
LEU CD2 HD21 sing N N 272 
LEU CD2 HD22 sing N N 273 
LEU CD2 HD23 sing N N 274 
LEU OXT HXT  sing N N 275 
LYS N   CA   sing N N 276 
LYS N   H    sing N N 277 
LYS N   H2   sing N N 278 
LYS CA  C    sing N N 279 
LYS CA  CB   sing N N 280 
LYS CA  HA   sing N N 281 
LYS C   O    doub N N 282 
LYS C   OXT  sing N N 283 
LYS CB  CG   sing N N 284 
LYS CB  HB2  sing N N 285 
LYS CB  HB3  sing N N 286 
LYS CG  CD   sing N N 287 
LYS CG  HG2  sing N N 288 
LYS CG  HG3  sing N N 289 
LYS CD  CE   sing N N 290 
LYS CD  HD2  sing N N 291 
LYS CD  HD3  sing N N 292 
LYS CE  NZ   sing N N 293 
LYS CE  HE2  sing N N 294 
LYS CE  HE3  sing N N 295 
LYS NZ  HZ1  sing N N 296 
LYS NZ  HZ2  sing N N 297 
LYS NZ  HZ3  sing N N 298 
LYS OXT HXT  sing N N 299 
MET N   CA   sing N N 300 
MET N   H    sing N N 301 
MET N   H2   sing N N 302 
MET CA  C    sing N N 303 
MET CA  CB   sing N N 304 
MET CA  HA   sing N N 305 
MET C   O    doub N N 306 
MET C   OXT  sing N N 307 
MET CB  CG   sing N N 308 
MET CB  HB2  sing N N 309 
MET CB  HB3  sing N N 310 
MET CG  SD   sing N N 311 
MET CG  HG2  sing N N 312 
MET CG  HG3  sing N N 313 
MET SD  CE   sing N N 314 
MET CE  HE1  sing N N 315 
MET CE  HE2  sing N N 316 
MET CE  HE3  sing N N 317 
MET OXT HXT  sing N N 318 
PHE N   CA   sing N N 319 
PHE N   H    sing N N 320 
PHE N   H2   sing N N 321 
PHE CA  C    sing N N 322 
PHE CA  CB   sing N N 323 
PHE CA  HA   sing N N 324 
PHE C   O    doub N N 325 
PHE C   OXT  sing N N 326 
PHE CB  CG   sing N N 327 
PHE CB  HB2  sing N N 328 
PHE CB  HB3  sing N N 329 
PHE CG  CD1  doub Y N 330 
PHE CG  CD2  sing Y N 331 
PHE CD1 CE1  sing Y N 332 
PHE CD1 HD1  sing N N 333 
PHE CD2 CE2  doub Y N 334 
PHE CD2 HD2  sing N N 335 
PHE CE1 CZ   doub Y N 336 
PHE CE1 HE1  sing N N 337 
PHE CE2 CZ   sing Y N 338 
PHE CE2 HE2  sing N N 339 
PHE CZ  HZ   sing N N 340 
PHE OXT HXT  sing N N 341 
PRO N   CA   sing N N 342 
PRO N   CD   sing N N 343 
PRO N   H    sing N N 344 
PRO CA  C    sing N N 345 
PRO CA  CB   sing N N 346 
PRO CA  HA   sing N N 347 
PRO C   O    doub N N 348 
PRO C   OXT  sing N N 349 
PRO CB  CG   sing N N 350 
PRO CB  HB2  sing N N 351 
PRO CB  HB3  sing N N 352 
PRO CG  CD   sing N N 353 
PRO CG  HG2  sing N N 354 
PRO CG  HG3  sing N N 355 
PRO CD  HD2  sing N N 356 
PRO CD  HD3  sing N N 357 
PRO OXT HXT  sing N N 358 
SER N   CA   sing N N 359 
SER N   H    sing N N 360 
SER N   H2   sing N N 361 
SER CA  C    sing N N 362 
SER CA  CB   sing N N 363 
SER CA  HA   sing N N 364 
SER C   O    doub N N 365 
SER C   OXT  sing N N 366 
SER CB  OG   sing N N 367 
SER CB  HB2  sing N N 368 
SER CB  HB3  sing N N 369 
SER OG  HG   sing N N 370 
SER OXT HXT  sing N N 371 
THR N   CA   sing N N 372 
THR N   H    sing N N 373 
THR N   H2   sing N N 374 
THR CA  C    sing N N 375 
THR CA  CB   sing N N 376 
THR CA  HA   sing N N 377 
THR C   O    doub N N 378 
THR C   OXT  sing N N 379 
THR CB  OG1  sing N N 380 
THR CB  CG2  sing N N 381 
THR CB  HB   sing N N 382 
THR OG1 HG1  sing N N 383 
THR CG2 HG21 sing N N 384 
THR CG2 HG22 sing N N 385 
THR CG2 HG23 sing N N 386 
THR OXT HXT  sing N N 387 
TRP N   CA   sing N N 388 
TRP N   H    sing N N 389 
TRP N   H2   sing N N 390 
TRP CA  C    sing N N 391 
TRP CA  CB   sing N N 392 
TRP CA  HA   sing N N 393 
TRP C   O    doub N N 394 
TRP C   OXT  sing N N 395 
TRP CB  CG   sing N N 396 
TRP CB  HB2  sing N N 397 
TRP CB  HB3  sing N N 398 
TRP CG  CD1  doub Y N 399 
TRP CG  CD2  sing Y N 400 
TRP CD1 NE1  sing Y N 401 
TRP CD1 HD1  sing N N 402 
TRP CD2 CE2  doub Y N 403 
TRP CD2 CE3  sing Y N 404 
TRP NE1 CE2  sing Y N 405 
TRP NE1 HE1  sing N N 406 
TRP CE2 CZ2  sing Y N 407 
TRP CE3 CZ3  doub Y N 408 
TRP CE3 HE3  sing N N 409 
TRP CZ2 CH2  doub Y N 410 
TRP CZ2 HZ2  sing N N 411 
TRP CZ3 CH2  sing Y N 412 
TRP CZ3 HZ3  sing N N 413 
TRP CH2 HH2  sing N N 414 
TRP OXT HXT  sing N N 415 
TYR N   CA   sing N N 416 
TYR N   H    sing N N 417 
TYR N   H2   sing N N 418 
TYR CA  C    sing N N 419 
TYR CA  CB   sing N N 420 
TYR CA  HA   sing N N 421 
TYR C   O    doub N N 422 
TYR C   OXT  sing N N 423 
TYR CB  CG   sing N N 424 
TYR CB  HB2  sing N N 425 
TYR CB  HB3  sing N N 426 
TYR CG  CD1  doub Y N 427 
TYR CG  CD2  sing Y N 428 
TYR CD1 CE1  sing Y N 429 
TYR CD1 HD1  sing N N 430 
TYR CD2 CE2  doub Y N 431 
TYR CD2 HD2  sing N N 432 
TYR CE1 CZ   doub Y N 433 
TYR CE1 HE1  sing N N 434 
TYR CE2 CZ   sing Y N 435 
TYR CE2 HE2  sing N N 436 
TYR CZ  OH   sing N N 437 
TYR OH  HH   sing N N 438 
TYR OXT HXT  sing N N 439 
VAL N   CA   sing N N 440 
VAL N   H    sing N N 441 
VAL N   H2   sing N N 442 
VAL CA  C    sing N N 443 
VAL CA  CB   sing N N 444 
VAL CA  HA   sing N N 445 
VAL C   O    doub N N 446 
VAL C   OXT  sing N N 447 
VAL CB  CG1  sing N N 448 
VAL CB  CG2  sing N N 449 
VAL CB  HB   sing N N 450 
VAL CG1 HG11 sing N N 451 
VAL CG1 HG12 sing N N 452 
VAL CG1 HG13 sing N N 453 
VAL CG2 HG21 sing N N 454 
VAL CG2 HG22 sing N N 455 
VAL CG2 HG23 sing N N 456 
VAL OXT HXT  sing N N 457 
Y6C CAA CAM  sing N N 458 
Y6C CAA CAT  doub N Z 459 
Y6C CAM OAB  doub N N 460 
Y6C CAM OAM  sing N N 461 
Y6C NAL CAN  sing N N 462 
Y6C NAL CAS  sing N N 463 
Y6C CAN CAP  doub Y N 464 
Y6C CAN CAI  sing Y N 465 
Y6C CAP CAH  sing Y N 466 
Y6C CAP CAR  sing Y N 467 
Y6C CAH CAD  doub Y N 468 
Y6C CAD CAF  sing Y N 469 
Y6C CAF NAK  doub Y N 470 
Y6C NAK CAR  sing Y N 471 
Y6C CAR CAQ  doub Y N 472 
Y6C CAQ NAJ  sing Y N 473 
Y6C CAQ CAO  sing Y N 474 
Y6C NAJ CAE  doub Y N 475 
Y6C CAE CAC  sing Y N 476 
Y6C CAC CAG  doub Y N 477 
Y6C CAG CAO  sing Y N 478 
Y6C CAO CAI  doub Y N 479 
Y6C CAT CAS  sing N N 480 
Y6C CAS OAS  doub N N 481 
Y6C CAA HAA  sing N N 482 
Y6C CAC HAC  sing N N 483 
Y6C CAD HAD  sing N N 484 
Y6C CAE HAE  sing N N 485 
Y6C CAF HAF  sing N N 486 
Y6C CAG HAG  sing N N 487 
Y6C CAH HAH  sing N N 488 
Y6C CAI HAI  sing N N 489 
Y6C NAL HNAL sing N N 490 
Y6C OAM H1   sing N N 491 
Y6C CAT HAAB sing N N 492 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_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   7VW4 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8XC2 
_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]   0.025109 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020319 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.013030 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NI ? ? 22.93579 4.97432 ? ? 2.39430  34.99046 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL A 1 1   ? -8.23400  9.25500   -10.95300 1.000 45.47791  ? 1   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 1   ? -7.50800  8.48400   -12.00800 1.000 40.16227  ? 1   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 1   ? -6.02300  8.87200   -11.97700 1.000 43.21784  ? 1   VAL A C   1 
ATOM   4    O  O   . VAL A 1 1   ? -5.70500  10.07400  -11.83600 1.000 48.29213  ? 1   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 1   ? -8.10700  8.72100   -13.41000 1.000 44.98940  ? 1   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 1   ? -7.58700  10.00900  -14.03100 1.000 40.29900  ? 1   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 1   ? -7.85800  7.54400   -14.34400 1.000 48.15835  ? 1   VAL A CG2 1 
ATOM   8    N  N   . LEU A 1 2   ? -5.13900  7.87900   -12.09100 1.000 32.05340  ? 2   LEU A N   1 
ATOM   9    C  CA  . LEU A 1 2   ? -3.68700  8.12300   -12.25300 1.000 24.87411  ? 2   LEU A CA  1 
ATOM   10   C  C   . LEU A 1 2   ? -3.39400  8.06200   -13.75200 1.000 21.52036  ? 2   LEU A C   1 
ATOM   11   O  O   . LEU A 1 2   ? -4.08100  7.27800   -14.45300 1.000 24.94013  ? 2   LEU A O   1 
ATOM   12   C  CB  . LEU A 1 2   ? -2.88900  7.04600   -11.51300 1.000 18.88525  ? 2   LEU A CB  1 
ATOM   13   C  CG  . LEU A 1 2   ? -2.72600  7.25000   -10.00300 1.000 19.44158  ? 2   LEU A CG  1 
ATOM   14   C  CD1 . LEU A 1 2   ? -4.04500  6.99100   -9.31400  1.000 20.07842  ? 2   LEU A CD1 1 
ATOM   15   C  CD2 . LEU A 1 2   ? -1.63500  6.34500   -9.43000  1.000 20.64069  ? 2   LEU A CD2 1 
ATOM   16   N  N   . SER A 1 3   ? -2.34800  8.75500   -14.18100 1.000 23.46097  ? 3   SER A N   1 
ATOM   17   C  CA  . SER A 1 3   ? -1.80900  8.59000   -15.54500 1.000 21.74770  ? 3   SER A CA  1 
ATOM   18   C  C   . SER A 1 3   ? -1.10600  7.23400   -15.63500 1.000 22.00115  ? 3   SER A C   1 
ATOM   19   O  O   . SER A 1 3   ? -0.61300  6.73400   -14.60700 1.000 19.87481  ? 3   SER A O   1 
ATOM   20   C  CB  . SER A 1 3   ? -0.85100  9.68100   -15.88800 1.000 20.25630  ? 3   SER A CB  1 
ATOM   21   O  OG  . SER A 1 3   ? 0.30600   9.63600   -15.09000 1.000 23.56119  ? 3   SER A OG  1 
ATOM   22   N  N   . GLU A 1 4   ? -0.91700  6.72400   -16.84400 1.000 18.58835  ? 4   GLU A N   1 
ATOM   23   C  CA  . GLU A 1 4   ? -0.04500  5.54600   -17.04500 1.000 18.34081  ? 4   GLU A CA  1 
ATOM   24   C  C   . GLU A 1 4   ? 1.33100   5.82100   -16.45000 1.000 19.69307  ? 4   GLU A C   1 
ATOM   25   O  O   . GLU A 1 4   ? 1.91600   4.89700   -15.83800 1.000 19.22038  ? 4   GLU A O   1 
ATOM   26   C  CB  . GLU A 1 4   ? 0.07200   5.18800   -18.53300 1.000 24.06945  ? 4   GLU A CB  1 
ATOM   27   C  CG  . GLU A 1 4   ? 0.93000   3.97700   -18.81300 1.000 26.34235  ? 4   GLU A CG  1 
ATOM   28   C  CD  . GLU A 1 4   ? 0.61500   2.65500   -18.10700 1.000 25.97741  ? 4   GLU A CD  1 
ATOM   29   O  OE1 . GLU A 1 4   ? -0.57000  2.44300   -17.68200 1.000 31.64868  ? 4   GLU A OE1 1 
ATOM   30   O  OE2 . GLU A 1 4   ? 1.52700   1.80300   -18.01900 1.000 26.03900  ? 4   GLU A OE2 1 
ATOM   31   N  N   . GLY A 1 5   ? 1.91300   7.00600   -16.65400 1.000 16.45886  ? 5   GLY A N   1 
ATOM   32   C  CA  . GLY A 1 5   ? 3.24200   7.26100   -16.09300 1.000 17.35023  ? 5   GLY A CA  1 
ATOM   33   C  C   . GLY A 1 5   ? 3.24200   7.16000   -14.56200 1.000 17.80012  ? 5   GLY A C   1 
ATOM   34   O  O   . GLY A 1 5   ? 4.17300   6.63400   -13.97000 1.000 15.12212  ? 5   GLY A O   1 
ATOM   35   N  N   . GLU A 1 6   ? 2.22800   7.69600   -13.92300 1.000 18.98575  ? 6   GLU A N   1 
ATOM   36   C  CA  . GLU A 1 6   ? 2.10200   7.59700   -12.46300 1.000 15.07316  ? 6   GLU A CA  1 
ATOM   37   C  C   . GLU A 1 6   ? 1.98700   6.12600   -12.04200 1.000 12.02957  ? 6   GLU A C   1 
ATOM   38   O  O   . GLU A 1 6   ? 2.67500   5.72300   -11.11500 1.000 15.32420  ? 6   GLU A O   1 
ATOM   39   C  CB  . GLU A 1 6   ? 0.88900   8.39800   -11.98900 1.000 16.98693  ? 6   GLU A CB  1 
ATOM   40   C  CG  . GLU A 1 6   ? 1.09100   9.90700   -12.07700 1.000 19.51273  ? 6   GLU A CG  1 
ATOM   41   C  CD  . GLU A 1 6   ? -0.13900  10.72500  -11.75300 1.000 19.30033  ? 6   GLU A CD  1 
ATOM   42   O  OE1 . GLU A 1 6   ? -1.24400  10.28700  -12.02700 1.000 26.86339  ? 6   GLU A OE1 1 
ATOM   43   O  OE2 . GLU A 1 6   ? 0.06100   11.81800  -11.12600 1.000 30.95979  ? 6   GLU A OE2 1 
ATOM   44   N  N   . TRP A 1 7   ? 1.14400   5.34500   -12.70200 1.000 14.12089  ? 7   TRP A N   1 
ATOM   45   C  CA  . TRP A 1 7   ? 1.05700   3.88800   -12.38800 1.000 14.60376  ? 7   TRP A CA  1 
ATOM   46   C  C   . TRP A 1 7   ? 2.44500   3.26500   -12.49500 1.000 13.81655  ? 7   TRP A C   1 
ATOM   47   O  O   . TRP A 1 7   ? 2.83600   2.38600   -11.66300 1.000 13.82158  ? 7   TRP A O   1 
ATOM   48   C  CB  . TRP A 1 7   ? 0.04400   3.14200   -13.26300 1.000 16.16443  ? 7   TRP A CB  1 
ATOM   49   C  CG  . TRP A 1 7   ? -1.34500  3.36300   -12.82900 1.000 15.25144  ? 7   TRP A CG  1 
ATOM   50   C  CD1 . TRP A 1 7   ? -2.35000  3.92200   -13.54500 1.000 18.39359  ? 7   TRP A CD1 1 
ATOM   51   C  CD2 . TRP A 1 7   ? -1.91000  3.03100   -11.53200 1.000 15.89728  ? 7   TRP A CD2 1 
ATOM   52   N  NE1 . TRP A 1 7   ? -3.49400  4.02800   -12.78600 1.000 19.84664  ? 7   TRP A NE1 1 
ATOM   53   C  CE2 . TRP A 1 7   ? -3.26100  3.44600   -11.56800 1.000 15.90066  ? 7   TRP A CE2 1 
ATOM   54   C  CE3 . TRP A 1 7   ? -1.41200  2.41000   -10.37300 1.000 14.90070  ? 7   TRP A CE3 1 
ATOM   55   C  CZ2 . TRP A 1 7   ? -4.12400  3.28600   -10.47700 1.000 16.62706  ? 7   TRP A CZ2 1 
ATOM   56   C  CZ3 . TRP A 1 7   ? -2.27100  2.25200   -9.30100  1.000 15.81859  ? 7   TRP A CZ3 1 
ATOM   57   C  CH2 . TRP A 1 7   ? -3.58700  2.73100   -9.33400  1.000 14.48085  ? 7   TRP A CH2 1 
ATOM   58   N  N   . GLN A 1 8   ? 3.20600   3.58400   -13.55300 1.000 14.40485  ? 8   GLN A N   1 
ATOM   59   C  CA  . GLN A 1 8   ? 4.54700   3.01300   -13.75000 1.000 13.08322  ? 8   GLN A CA  1 
ATOM   60   C  C   . GLN A 1 8   ? 5.49900   3.36100   -12.59500 1.000 13.08976  ? 8   GLN A C   1 
ATOM   61   O  O   . GLN A 1 8   ? 6.29500   2.52400   -12.19700 1.000 14.53638  ? 8   GLN A O   1 
ATOM   62   C  CB  . GLN A 1 8   ? 5.15800   3.39800   -15.10000 1.000 13.92339  ? 8   GLN A CB  1 
ATOM   63   C  CG  . GLN A 1 8   ? 4.39900   2.80400   -16.27800 1.000 15.43587  ? 8   GLN A CG  1 
ATOM   64   C  CD  . GLN A 1 8   ? 5.06000   3.02800   -17.60300 1.000 23.12671  ? 8   GLN A CD  1 
ATOM   65   O  OE1 . GLN A 1 8   ? 6.20700   3.44000   -17.69200 1.000 21.41696  ? 8   GLN A OE1 1 
ATOM   66   N  NE2 . GLN A 1 8   ? 4.28600   2.91000   -18.67000 1.000 20.85039  ? 8   GLN A NE2 1 
ATOM   67   N  N   . LEU A 1 9   ? 5.42500   4.57100   -12.07400 1.000 12.07190  ? 9   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 9   ? 6.25800   4.96400   -10.92200 1.000 12.49409  ? 9   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 9   ? 5.87100   4.13100   -9.69100  1.000 12.61578  ? 9   LEU A C   1 
ATOM   70   O  O   . LEU A 1 9   ? 6.71700   3.73500   -8.93500  1.000 13.94399  ? 9   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 9   ? 6.09600   6.44800   -10.61200 1.000 14.63855  ? 9   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 9   ? 6.64100   7.41200   -11.67500 1.000 14.92808  ? 9   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 9   ? 6.27400   8.82700   -11.33500 1.000 17.16659  ? 9   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 9   ? 8.13800   7.24500   -11.85300 1.000 19.02800  ? 9   LEU A CD2 1 
ATOM   75   N  N   . VAL A 1 10  ? 4.57000   3.91100   -9.55000  1.000 14.30390  ? 10  VAL A N   1 
ATOM   76   C  CA  . VAL A 1 10  ? 4.02300   3.07300   -8.43700  1.000 12.67863  ? 10  VAL A CA  1 
ATOM   77   C  C   . VAL A 1 10  ? 4.60000   1.66300   -8.55900  1.000 12.73559  ? 10  VAL A C   1 
ATOM   78   O  O   . VAL A 1 10  ? 5.12400   1.10600   -7.57300  1.000 12.98113  ? 10  VAL A O   1 
ATOM   79   C  CB  . VAL A 1 10  ? 2.48300   3.05400   -8.45100  1.000 11.86267  ? 10  VAL A CB  1 
ATOM   80   C  CG1 . VAL A 1 10  ? 1.93200   1.98000   -7.50600  1.000 14.66991  ? 10  VAL A CG1 1 
ATOM   81   C  CG2 . VAL A 1 10  ? 1.93800   4.42100   -8.09300  1.000 15.89145  ? 10  VAL A CG2 1 
ATOM   82   N  N   . LEU A 1 11  ? 4.47600   1.06900   -9.72700  1.000 11.79159  ? 11  LEU A N   1 
ATOM   83   C  CA  . LEU A 1 11  ? 4.89100   -0.34000  -9.87700  1.000 14.48396  ? 11  LEU A CA  1 
ATOM   84   C  C   . LEU A 1 11  ? 6.41300   -0.46900  -9.90500  1.000 11.67066  ? 11  LEU A C   1 
ATOM   85   O  O   . LEU A 1 11  ? 6.93700   -1.51000  -9.56100  1.000 13.95916  ? 11  LEU A O   1 
ATOM   86   C  CB  . LEU A 1 11  ? 4.19300   -0.95600  -11.07800 1.000 13.95757  ? 11  LEU A CB  1 
ATOM   87   C  CG  . LEU A 1 11  ? 2.67800   -0.96900  -10.98500 1.000 14.59159  ? 11  LEU A CG  1 
ATOM   88   C  CD1 . LEU A 1 11  ? 2.12600   -1.54100  -12.28700 1.000 18.36115  ? 11  LEU A CD1 1 
ATOM   89   C  CD2 . LEU A 1 11  ? 2.21300   -1.78300  -9.77800  1.000 15.80085  ? 11  LEU A CD2 1 
ATOM   90   N  N   . HIS A 1 12  ? 7.09900   0.58700   -10.30400 1.000 13.29933  ? 12  HIS A N   1 
ATOM   91   C  CA  . HIS A 1 12  ? 8.57700   0.53700   -10.27100 1.000 15.78873  ? 12  HIS A CA  1 
ATOM   92   C  C   . HIS A 1 12  ? 9.10800   0.38900   -8.82800  1.000 12.61186  ? 12  HIS A C   1 
ATOM   93   O  O   . HIS A 1 12  ? 9.97400   -0.44000  -8.56900  1.000 15.15097  ? 12  HIS A O   1 
ATOM   94   C  CB  . HIS A 1 12  ? 9.11900   1.78700   -10.96400 1.000 14.31547  ? 12  HIS A CB  1 
ATOM   95   C  CG  . HIS A 1 12  ? 10.57000  1.66300   -11.21200 1.000 18.17119  ? 12  HIS A CG  1 
ATOM   96   N  ND1 . HIS A 1 12  ? 11.04700  0.89200   -12.23900 1.000 25.95307  ? 12  HIS A ND1 1 
ATOM   97   C  CD2 . HIS A 1 12  ? 11.63600  2.14000   -10.55000 1.000 29.00770  ? 12  HIS A CD2 1 
ATOM   98   C  CE1 . HIS A 1 12  ? 12.35000  0.91700   -12.22600 1.000 33.29286  ? 12  HIS A CE1 1 
ATOM   99   N  NE2 . HIS A 1 12  ? 12.72400  1.65500   -11.20800 1.000 25.33598  ? 12  HIS A NE2 1 
ATOM   100  N  N   . VAL A 1 13  ? 8.61100   1.23100   -7.92900  1.000 12.85130  ? 13  VAL A N   1 
ATOM   101  C  CA  . VAL A 1 13  ? 9.06200   1.13000   -6.51800  1.000 13.23842  ? 13  VAL A CA  1 
ATOM   102  C  C   . VAL A 1 13  ? 8.49400   -0.16600  -5.90000  1.000 11.76402  ? 13  VAL A C   1 
ATOM   103  O  O   . VAL A 1 13  ? 9.15800   -0.78100  -5.10400  1.000 13.47406  ? 13  VAL A O   1 
ATOM   104  C  CB  . VAL A 1 13  ? 8.69500   2.40200   -5.72800  1.000 13.76235  ? 13  VAL A CB  1 
ATOM   105  C  CG1 . VAL A 1 13  ? 7.20000   2.55400   -5.51400  1.000 15.67251  ? 13  VAL A CG1 1 
ATOM   106  C  CG2 . VAL A 1 13  ? 9.45000   2.46200   -4.40900  1.000 13.93844  ? 13  VAL A CG2 1 
ATOM   107  N  N   . TRP A 1 14  ? 7.30600   -0.56100  -6.35000  1.000 12.63391  ? 14  TRP A N   1 
ATOM   108  C  CA  . TRP A 1 14  ? 6.71400   -1.79500  -5.78400  1.000 12.67561  ? 14  TRP A CA  1 
ATOM   109  C  C   . TRP A 1 14  ? 7.60200   -3.01500  -6.08600  1.000 13.00000  ? 14  TRP A C   1 
ATOM   110  O  O   . TRP A 1 14  ? 7.66100   -3.92500  -5.28700  1.000 13.09879  ? 14  TRP A O   1 
ATOM   111  C  CB  . TRP A 1 14  ? 5.27200   -2.03300  -6.25100  1.000 12.60732  ? 14  TRP A CB  1 
ATOM   112  C  CG  . TRP A 1 14  ? 4.57700   -2.90800  -5.25100  1.000 12.70675  ? 14  TRP A CG  1 
ATOM   113  C  CD1 . TRP A 1 14  ? 4.34800   -4.24900  -5.33800  1.000 15.55389  ? 14  TRP A CD1 1 
ATOM   114  C  CD2 . TRP A 1 14  ? 4.11900   -2.51400  -3.94600  1.000 12.01170  ? 14  TRP A CD2 1 
ATOM   115  N  NE1 . TRP A 1 14  ? 3.74800   -4.70500  -4.19700  1.000 14.81570  ? 14  TRP A NE1 1 
ATOM   116  C  CE2 . TRP A 1 14  ? 3.58900   -3.66400  -3.32800  1.000 15.92486  ? 14  TRP A CE2 1 
ATOM   117  C  CE3 . TRP A 1 14  ? 4.08300   -1.30200  -3.25300  1.000 16.27077  ? 14  TRP A CE3 1 
ATOM   118  C  CZ2 . TRP A 1 14  ? 3.03200   -3.63200  -2.05100  1.000 15.62640  ? 14  TRP A CZ2 1 
ATOM   119  C  CZ3 . TRP A 1 14  ? 3.53000   -1.27100  -1.99400  1.000 19.81539  ? 14  TRP A CZ3 1 
ATOM   120  C  CH2 . TRP A 1 14  ? 3.01100   -2.42100  -1.40400  1.000 17.59763  ? 14  TRP A CH2 1 
ATOM   121  N  N   . ALA A 1 15  ? 8.28600   -2.97900  -7.21900  1.000 12.83124  ? 15  ALA A N   1 
ATOM   122  C  CA  . ALA A 1 15  ? 9.16000   -4.11600  -7.56600  1.000 15.27079  ? 15  ALA A CA  1 
ATOM   123  C  C   . ALA A 1 15  ? 10.28000  -4.25500  -6.52300  1.000 15.42072  ? 15  ALA A C   1 
ATOM   124  O  O   . ALA A 1 15  ? 10.75200  -5.36200  -6.30100  1.000 15.88291  ? 15  ALA A O   1 
ATOM   125  C  CB  . ALA A 1 15  ? 9.69100   -3.96300  -8.98000  1.000 15.35989  ? 15  ALA A CB  1 
ATOM   126  N  N   . LYS A 1 16  ? 10.70000  -3.14000  -5.94300  1.000 14.37867  ? 16  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 16  ? 11.72400  -3.18600  -4.87200  1.000 14.18312  ? 16  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 16  ? 11.14700  -3.85600  -3.62700  1.000 11.93771  ? 16  LYS A C   1 
ATOM   129  O  O   . LYS A 1 16  ? 11.86300  -4.57500  -2.96700  1.000 15.64361  ? 16  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 16  ? 12.17700  -1.76600  -4.52100  1.000 15.69615  ? 16  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 16  ? 12.90400  -1.04600  -5.64600  1.000 24.00432  ? 16  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 16  ? 14.08600  -1.84400  -6.13900  1.000 32.47466  ? 16  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 16  ? 14.78200  -1.23000  -7.33300  1.000 41.09780  ? 16  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 16  ? 15.89700  -2.08500  -7.80800  1.000 57.06866  ? 16  LYS A NZ  1 
ATOM   135  N  N   . VAL A 1 17  ? 9.88600   -3.57500  -3.32900  1.000 13.55882  ? 17  VAL A N   1 
ATOM   136  C  CA  . VAL A 1 17  ? 9.21600   -4.24100  -2.18400  1.000 11.91058  ? 17  VAL A CA  1 
ATOM   137  C  C   . VAL A 1 17  ? 9.20300   -5.75500  -2.44900  1.000 11.09868  ? 17  VAL A C   1 
ATOM   138  O  O   . VAL A 1 17  ? 9.47600   -6.51600  -1.54700  1.000 12.76988  ? 17  VAL A O   1 
ATOM   139  C  CB  . VAL A 1 17  ? 7.78400   -3.68900  -2.01600  1.000 12.97981  ? 17  VAL A CB  1 
ATOM   140  C  CG1 . VAL A 1 17  ? 6.99700   -4.44100  -0.95800  1.000 12.81053  ? 17  VAL A CG1 1 
ATOM   141  C  CG2 . VAL A 1 17  ? 7.77600   -2.19600  -1.74200  1.000 14.61629  ? 17  VAL A CG2 1 
ATOM   142  N  N   . GLU A 1 18  ? 8.92800   -6.14100  -3.68700  1.000 13.44487  ? 18  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 18  ? 8.76400   -7.58000  -4.01800  1.000 12.58191  ? 18  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 18  ? 10.07600  -8.36200  -3.87000  1.000 12.84497  ? 18  GLU A C   1 
ATOM   145  O  O   . GLU A 1 18  ? 9.99400   -9.57200  -3.75400  1.000 14.05496  ? 18  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 18  ? 8.20100   -7.74900  -5.43400  1.000 13.63504  ? 18  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 18  ? 6.79300   -7.21600  -5.62800  1.000 16.42018  ? 18  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 18  ? 6.28100   -7.37500  -7.05200  1.000 23.17009  ? 18  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 18  ? 6.33600   -6.39500  -7.81700  1.000 25.06652  ? 18  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 18  ? 5.84100   -8.47600  -7.39100  1.000 22.68851  ? 18  GLU A OE2 1 
ATOM   151  N  N   . ALA A 1 19  ? 11.21900  -7.68800  -3.88100  1.000 11.96638  ? 19  ALA A N   1 
ATOM   152  C  CA  . ALA A 1 19  ? 12.50800  -8.37300  -3.62900  1.000 12.84749  ? 19  ALA A CA  1 
ATOM   153  C  C   . ALA A 1 19  ? 12.58400  -8.92800  -2.19700  1.000 13.84748  ? 19  ALA A C   1 
ATOM   154  O  O   . ALA A 1 19  ? 13.32200  -9.87500  -1.97800  1.000 15.35520  ? 19  ALA A O   1 
ATOM   155  C  CB  . ALA A 1 19  ? 13.64200  -7.42300  -3.91100  1.000 15.71414  ? 19  ALA A CB  1 
ATOM   156  N  N   . ASP A 1 20  ? 11.85600  -8.32700  -1.26100  1.000 13.02748  ? 20  ASP A N   1 
ATOM   157  C  CA  . ASP A 1 20  ? 11.81000  -8.83700  0.13400   1.000 13.30311  ? 20  ASP A CA  1 
ATOM   158  C  C   . ASP A 1 20  ? 10.50200  -8.37100  0.76800   1.000 11.70715  ? 20  ASP A C   1 
ATOM   159  O  O   . ASP A 1 20  ? 10.49100  -7.40500  1.52100   1.000 12.90299  ? 20  ASP A O   1 
ATOM   160  C  CB  . ASP A 1 20  ? 13.02100  -8.40100  0.93800   1.000 13.11611  ? 20  ASP A CB  1 
ATOM   161  C  CG  . ASP A 1 20  ? 13.04300  -8.97400  2.34700   1.000 13.60447  ? 20  ASP A CG  1 
ATOM   162  O  OD1 . ASP A 1 20  ? 12.12100  -9.73200  2.69600   1.000 13.41446  ? 20  ASP A OD1 1 
ATOM   163  O  OD2 . ASP A 1 20  ? 13.98600  -8.65000  3.08100   1.000 18.94526  ? 20  ASP A OD2 1 
ATOM   164  N  N   . VAL A 1 21  ? 9.44800   -9.09700  0.44900   1.000 10.01860  ? 21  VAL A N   1 
ATOM   165  C  CA  . VAL A 1 21  ? 8.10700   -8.66400  0.93200   1.000 10.66856  ? 21  VAL A CA  1 
ATOM   166  C  C   . VAL A 1 21  ? 8.05800   -8.71000  2.46800   1.000 12.63395  ? 21  VAL A C   1 
ATOM   167  O  O   . VAL A 1 21  ? 7.48400   -7.81500  3.07200   1.000 11.99912  ? 21  VAL A O   1 
ATOM   168  C  CB  . VAL A 1 21  ? 7.02500   -9.55200  0.28800   1.000 9.91858   ? 21  VAL A CB  1 
ATOM   169  C  CG1 . VAL A 1 21  ? 5.63600   -9.20800  0.80400   1.000 13.50359  ? 21  VAL A CG1 1 
ATOM   170  C  CG2 . VAL A 1 21  ? 7.06000   -9.44900  -1.22600  1.000 12.73173  ? 21  VAL A CG2 1 
ATOM   171  N  N   . ALA A 1 22  ? 8.63200   -9.75700  3.05700   1.000 11.69280  ? 22  ALA A N   1 
ATOM   172  C  CA  . ALA A 1 22  ? 8.51500   -9.89700  4.52400   1.000 11.81241  ? 22  ALA A CA  1 
ATOM   173  C  C   . ALA A 1 22  ? 9.21500   -8.76200  5.28500   1.000 11.61931  ? 22  ALA A C   1 
ATOM   174  O  O   . ALA A 1 22  ? 8.66000   -8.26000  6.23800   1.000 12.43129  ? 22  ALA A O   1 
ATOM   175  C  CB  . ALA A 1 22  ? 9.06200   -11.23000 4.93500   1.000 14.22918  ? 22  ALA A CB  1 
ATOM   176  N  N   . GLY A 1 23  ? 10.43200  -8.44400  4.86300   1.000 11.84270  ? 23  GLY A N   1 
ATOM   177  C  CA  . GLY A 1 23  ? 11.15900  -7.35700  5.54100   1.000 12.07168  ? 23  GLY A CA  1 
ATOM   178  C  C   . GLY A 1 23  ? 10.43900  -6.02400  5.41000   1.000 11.61529  ? 23  GLY A C   1 
ATOM   179  O  O   . GLY A 1 23  ? 10.37600  -5.30700  6.39300   1.000 13.32628  ? 23  GLY A O   1 
ATOM   180  N  N   . HIS A 1 24  ? 9.92300   -5.73300  4.21900   1.000 12.08003  ? 24  HIS A N   1 
ATOM   181  C  CA  . HIS A 1 24  ? 9.13900   -4.48700  4.02500   1.000 13.26619  ? 24  HIS A CA  1 
ATOM   182  C  C   . HIS A 1 24  ? 7.90100   -4.53400  4.92000   1.000 12.46747  ? 24  HIS A C   1 
ATOM   183  O  O   . HIS A 1 24  ? 7.56600   -3.54200  5.52800   1.000 11.84635  ? 24  HIS A O   1 
ATOM   184  C  CB  . HIS A 1 24  ? 8.76800   -4.28100  2.54000   1.000 12.01391  ? 24  HIS A CB  1 
ATOM   185  C  CG  . HIS A 1 24  ? 9.89900   -3.79400  1.70000   1.000 12.04812  ? 24  HIS A CG  1 
ATOM   186  N  ND1 . HIS A 1 24  ? 10.85700  -4.64200  1.19600   1.000 12.66236  ? 24  HIS A ND1 1 
ATOM   187  C  CD2 . HIS A 1 24  ? 10.22700  -2.55500  1.27700   1.000 14.00966  ? 24  HIS A CD2 1 
ATOM   188  C  CE1 . HIS A 1 24  ? 11.73000  -3.94700  0.50200   1.000 14.40245  ? 24  HIS A CE1 1 
ATOM   189  N  NE2 . HIS A 1 24  ? 11.36700  -2.66900  0.53600   1.000 13.64786  ? 24  HIS A NE2 1 
ATOM   190  N  N   . GLY A 1 25  ? 7.25600   -5.69400  4.95100   1.000 12.57976  ? 25  GLY A N   1 
ATOM   191  C  CA  . GLY A 1 25  ? 6.01500   -5.80100  5.73900   1.000 12.11931  ? 25  GLY A CA  1 
ATOM   192  C  C   . GLY A 1 25  ? 6.27200   -5.59600  7.21900   1.000 12.45584  ? 25  GLY A C   1 
ATOM   193  O  O   . GLY A 1 25  ? 5.44700   -4.99300  7.87700   1.000 13.59297  ? 25  GLY A O   1 
ATOM   194  N  N   . GLN A 1 26  ? 7.38200   -6.15000  7.69800   1.000 12.52160  ? 26  GLN A N   1 
ATOM   195  C  CA  . GLN A 1 26  ? 7.75400   -5.95700  9.11700   1.000 11.56006  ? 26  GLN A CA  1 
ATOM   196  C  C   . GLN A 1 26  ? 7.95600   -4.46600  9.39200   1.000 13.43948  ? 26  GLN A C   1 
ATOM   197  O  O   . GLN A 1 26  ? 7.43300   -3.98400  10.38100  1.000 14.88319  ? 26  GLN A O   1 
ATOM   198  C  CB  . GLN A 1 26  ? 9.05300   -6.69600  9.44700   1.000 12.69270  ? 26  GLN A CB  1 
ATOM   199  C  CG  . GLN A 1 26  ? 8.89600   -8.20000  9.59300   1.000 15.95611  ? 26  GLN A CG  1 
ATOM   200  C  CD  . GLN A 1 26  ? 10.24800  -8.84500  9.76600   1.000 17.29527  ? 26  GLN A CD  1 
ATOM   201  O  OE1 . GLN A 1 26  ? 11.13800  -8.68600  8.94000   1.000 21.38281  ? 26  GLN A OE1 1 
ATOM   202  N  NE2 . GLN A 1 26  ? 10.41100  -9.57700  10.85300  1.000 16.76381  ? 26  GLN A NE2 1 
ATOM   203  N  N   . ASP A 1 27  ? 8.71400   -3.79300  8.53400   1.000 12.07209  ? 27  ASP A N   1 
ATOM   204  C  CA  . ASP A 1 27  ? 9.01900   -2.37800  8.83200   1.000 13.45657  ? 27  ASP A CA  1 
ATOM   205  C  C   . ASP A 1 27  ? 7.72000   -1.59100  8.78200   1.000 13.27268  ? 27  ASP A C   1 
ATOM   206  O  O   . ASP A 1 27  ? 7.55300   -0.64800  9.57200   1.000 13.32121  ? 27  ASP A O   1 
ATOM   207  C  CB  . ASP A 1 27  ? 10.07800  -1.78900  7.92500   1.000 12.79095  ? 27  ASP A CB  1 
ATOM   208  C  CG  . ASP A 1 27  ? 11.47300  -2.26000  8.23300   1.000 20.64308  ? 27  ASP A CG  1 
ATOM   209  O  OD1 . ASP A 1 27  ? 11.62600  -2.99900  9.21500   1.000 21.27717  ? 27  ASP A OD1 1 
ATOM   210  O  OD2 . ASP A 1 27  ? 12.38800  -1.78100  7.52700   1.000 24.86589  ? 27  ASP A OD2 1 
ATOM   211  N  N   . ILE A 1 28  ? 6.83200   -1.90600  7.83100   1.000 10.88257  ? 28  ILE A N   1 
ATOM   212  C  CA  . ILE A 1 28  ? 5.56100   -1.13900  7.69700   1.000 10.18374  ? 28  ILE A CA  1 
ATOM   213  C  C   . ILE A 1 28  ? 4.68700   -1.35600  8.92600   1.000 11.60022  ? 28  ILE A C   1 
ATOM   214  O  O   . ILE A 1 28  ? 4.15600   -0.39700  9.46600   1.000 12.39896  ? 28  ILE A O   1 
ATOM   215  C  CB  . ILE A 1 28  ? 4.87800   -1.52100  6.38100   1.000 9.90934   ? 28  ILE A CB  1 
ATOM   216  C  CG1 . ILE A 1 28  ? 5.66400   -0.89900  5.23300   1.000 12.88664  ? 28  ILE A CG1 1 
ATOM   217  C  CG2 . ILE A 1 28  ? 3.42900   -1.09800  6.36700   1.000 11.24253  ? 28  ILE A CG2 1 
ATOM   218  C  CD1 . ILE A 1 28  ? 5.36300   -1.48900  3.83200   1.000 13.45505  ? 28  ILE A CD1 1 
ATOM   219  N  N   . LEU A 1 29  ? 4.45300   -2.58600  9.35300   1.000 12.18638  ? 29  LEU A N   1 
ATOM   220  C  CA  . LEU A 1 29  ? 3.62100   -2.84700  10.55900  1.000 12.03775  ? 29  LEU A CA  1 
ATOM   221  C  C   . LEU A 1 29  ? 4.28100   -2.31100  11.82300  1.000 12.65300  ? 29  LEU A C   1 
ATOM   222  O  O   . LEU A 1 29  ? 3.54000   -1.75800  12.69200  1.000 13.76881  ? 29  LEU A O   1 
ATOM   223  C  CB  . LEU A 1 29  ? 3.29400   -4.32500  10.69600  1.000 12.48459  ? 29  LEU A CB  1 
ATOM   224  C  CG  . LEU A 1 29  ? 2.40700   -4.88100  9.58400   1.000 11.87178  ? 29  LEU A CG  1 
ATOM   225  C  CD1 . LEU A 1 29  ? 2.12000   -6.34300  9.90300   1.000 15.40968  ? 29  LEU A CD1 1 
ATOM   226  C  CD2 . LEU A 1 29  ? 1.10200   -4.09900  9.41400   1.000 12.87052  ? 29  LEU A CD2 1 
ATOM   227  N  N   . ILE A 1 30  ? 5.58400   -2.37900  11.94100  1.000 12.79964  ? 30  ILE A N   1 
ATOM   228  C  CA  . ILE A 1 30  ? 6.24200   -1.81500  13.15300  1.000 13.04264  ? 30  ILE A CA  1 
ATOM   229  C  C   . ILE A 1 30  ? 6.01800   -0.30500  13.13300  1.000 14.88991  ? 30  ILE A C   1 
ATOM   230  O  O   . ILE A 1 30  ? 5.68800   0.23800   14.21500  1.000 14.03921  ? 30  ILE A O   1 
ATOM   231  C  CB  . ILE A 1 30  ? 7.72800   -2.24200  13.20600  1.000 14.11012  ? 30  ILE A CB  1 
ATOM   232  C  CG1 . ILE A 1 30  ? 7.77600   -3.73600  13.51600  1.000 14.41367  ? 30  ILE A CG1 1 
ATOM   233  C  CG2 . ILE A 1 30  ? 8.50800   -1.40400  14.20800  1.000 18.97560  ? 30  ILE A CG2 1 
ATOM   234  C  CD1 . ILE A 1 30  ? 9.15400   -4.37400  13.41600  1.000 15.61724  ? 30  ILE A CD1 1 
ATOM   235  N  N   . ARG A 1 31  ? 6.16600   0.33600   11.98800  1.000 12.73515  ? 31  ARG A N   1 
ATOM   236  C  CA  . ARG A 1 31  ? 5.93300   1.80800   11.89900  1.000 12.13168  ? 31  ARG A CA  1 
ATOM   237  C  C   . ARG A 1 31  ? 4.48000   2.09700   12.29900  1.000 14.84751  ? 31  ARG A C   1 
ATOM   238  O  O   . ARG A 1 31  ? 4.19900   3.07100   13.03000  1.000 16.29316  ? 31  ARG A O   1 
ATOM   239  C  CB  . ARG A 1 31  ? 6.26300   2.31000   10.50100  1.000 11.59950  ? 31  ARG A CB  1 
ATOM   240  C  CG  . ARG A 1 31  ? 5.93100   3.77100   10.22100  1.000 16.17656  ? 31  ARG A CG  1 
ATOM   241  C  CD  . ARG A 1 31  ? 6.78700   4.69400   11.07100  1.000 19.03061  ? 31  ARG A CD  1 
ATOM   242  N  NE  . ARG A 1 31  ? 6.46500   6.06800   10.72400  1.000 18.72708  ? 31  ARG A NE  1 
ATOM   243  C  CZ  . ARG A 1 31  ? 7.16400   7.13100   11.10100  1.000 25.78201  ? 31  ARG A CZ  1 
ATOM   244  N  NH1 . ARG A 1 31  ? 8.28200   6.98300   11.78300  1.000 28.26404  ? 31  ARG A NH1 1 
ATOM   245  N  NH2 . ARG A 1 31  ? 6.76200   8.32400   10.72500  1.000 26.71380  ? 31  ARG A NH2 1 
ATOM   246  N  N   . LEU A 1 32  ? 3.53700   1.35900   11.75300  1.000 12.81677  ? 32  LEU A N   1 
ATOM   247  C  CA  . LEU A 1 32  ? 2.10900   1.56500   12.07800  1.000 13.13401  ? 32  LEU A CA  1 
ATOM   248  C  C   . LEU A 1 32  ? 1.86700   1.45700   13.57200  1.000 15.04474  ? 32  LEU A C   1 
ATOM   249  O  O   . LEU A 1 32  ? 1.20400   2.33900   14.13900  1.000 16.34581  ? 32  LEU A O   1 
ATOM   250  C  CB  . LEU A 1 32  ? 1.26800   0.54200   11.33100  1.000 11.62059  ? 32  LEU A CB  1 
ATOM   251  C  CG  . LEU A 1 32  ? -0.21400  0.51500   11.67700  1.000 11.68674  ? 32  LEU A CG  1 
ATOM   252  C  CD1 . LEU A 1 32  ? -0.88800  1.78000   11.22400  1.000 14.86343  ? 32  LEU A CD1 1 
ATOM   253  C  CD2 . LEU A 1 32  ? -0.88400  -0.68400  11.07000  1.000 12.68094  ? 32  LEU A CD2 1 
ATOM   254  N  N   . PHE A 1 33  ? 2.31300   0.38300   14.18600  1.000 15.87177  ? 33  PHE A N   1 
ATOM   255  C  CA  . PHE A 1 33  ? 2.00000   0.14600   15.61700  1.000 17.30472  ? 33  PHE A CA  1 
ATOM   256  C  C   . PHE A 1 33  ? 2.71300   1.14300   16.54900  1.000 19.91167  ? 33  PHE A C   1 
ATOM   257  O  O   . PHE A 1 33  ? 2.16800   1.47000   17.58100  1.000 19.29921  ? 33  PHE A O   1 
ATOM   258  C  CB  . PHE A 1 33  ? 2.34700   -1.29400  15.98200  1.000 16.75436  ? 33  PHE A CB  1 
ATOM   259  C  CG  . PHE A 1 33  ? 1.58400   -2.35100  15.23000  1.000 19.22082  ? 33  PHE A CG  1 
ATOM   260  C  CD1 . PHE A 1 33  ? 0.27700   -2.13800  14.83900  1.000 17.74476  ? 33  PHE A CD1 1 
ATOM   261  C  CD2 . PHE A 1 33  ? 2.17200   -3.56600  14.92900  1.000 19.04151  ? 33  PHE A CD2 1 
ATOM   262  C  CE1 . PHE A 1 33  ? -0.42500  -3.11800  14.15900  1.000 20.38135  ? 33  PHE A CE1 1 
ATOM   263  C  CE2 . PHE A 1 33  ? 1.47100   -4.54200  14.24300  1.000 21.47809  ? 33  PHE A CE2 1 
ATOM   264  C  CZ  . PHE A 1 33  ? 0.17300   -4.31700  13.86500  1.000 22.09898  ? 33  PHE A CZ  1 
ATOM   265  N  N   . LYS A 1 34  ? 3.91800   1.56000   16.18600  1.000 17.76316  ? 34  LYS A N   1 
ATOM   266  C  CA  . LYS A 1 34  ? 4.63800   2.56400   17.00200  1.000 20.26553  ? 34  LYS A CA  1 
ATOM   267  C  C   . LYS A 1 34  ? 3.96100   3.92600   16.84500  1.000 21.09262  ? 34  LYS A C   1 
ATOM   268  O  O   . LYS A 1 34  ? 3.79300   4.60300   17.86000  1.000 24.25118  ? 34  LYS A O   1 
ATOM   269  C  CB  . LYS A 1 34  ? 6.11400   2.63700   16.61200  1.000 21.29015  ? 34  LYS A CB  1 
ATOM   270  C  CG  . LYS A 1 34  ? 6.97700   1.47500   17.07500  1.000 29.78918  ? 34  LYS A CG  1 
ATOM   271  C  CD  . LYS A 1 34  ? 8.39700   1.68300   16.63500  1.000 33.92465  ? 34  LYS A CD  1 
ATOM   272  C  CE  . LYS A 1 34  ? 9.36100   0.62300   17.11200  1.000 40.62382  ? 34  LYS A CE  1 
ATOM   273  N  NZ  . LYS A 1 34  ? 10.72700  0.92200   16.62700  1.000 41.75142  ? 34  LYS A NZ  1 
ATOM   274  N  N   . SER A 1 35  ? 3.59600   4.29800   15.62600  1.000 16.63009  ? 35  SER A N   1 
ATOM   275  C  CA  . SER A 1 35  ? 3.01700   5.64300   15.36900  1.000 15.51682  ? 35  SER A CA  1 
ATOM   276  C  C   . SER A 1 35  ? 1.56500   5.70800   15.84800  1.000 17.07931  ? 35  SER A C   1 
ATOM   277  O  O   . SER A 1 35  ? 1.13800   6.79600   16.23500  1.000 17.82419  ? 35  SER A O   1 
ATOM   278  C  CB  . SER A 1 35  ? 3.09600   5.98800   13.91600  1.000 16.95833  ? 35  SER A CB  1 
ATOM   279  O  OG  . SER A 1 35  ? 4.44400   6.02900   13.48400  1.000 24.94294  ? 35  SER A OG  1 
ATOM   280  N  N   . HIS A 1 36  ? 0.85500   4.58800   15.79300  1.000 16.56861  ? 36  HIS A N   1 
ATOM   281  C  CA  . HIS A 1 36  ? -0.58700  4.57500   16.14400  1.000 18.75246  ? 36  HIS A CA  1 
ATOM   282  C  C   . HIS A 1 36  ? -0.87600  3.31400   16.95500  1.000 18.40963  ? 36  HIS A C   1 
ATOM   283  O  O   . HIS A 1 36  ? -1.50000  2.40000   16.43600  1.000 17.17075  ? 36  HIS A O   1 
ATOM   284  C  CB  . HIS A 1 36  ? -1.39400  4.66200   14.84800  1.000 17.00924  ? 36  HIS A CB  1 
ATOM   285  C  CG  . HIS A 1 36  ? -1.03700  5.83700   14.01000  1.000 15.61341  ? 36  HIS A CG  1 
ATOM   286  N  ND1 . HIS A 1 36  ? -1.49300  7.10200   14.29000  1.000 18.73718  ? 36  HIS A ND1 1 
ATOM   287  C  CD2 . HIS A 1 36  ? -0.25500  5.94700   12.91700  1.000 18.35376  ? 36  HIS A CD2 1 
ATOM   288  C  CE1 . HIS A 1 36  ? -1.01200  7.94300   13.40400  1.000 22.89171  ? 36  HIS A CE1 1 
ATOM   289  N  NE2 . HIS A 1 36  ? -0.24700  7.26000   12.55500  1.000 20.17185  ? 36  HIS A NE2 1 
ATOM   290  N  N   . PRO A 1 37  ? -0.43500  3.24400   18.22500  1.000 18.50633  ? 37  PRO A N   1 
ATOM   291  C  CA  . PRO A 1 37  ? -0.56300  2.01100   18.99700  1.000 21.05885  ? 37  PRO A CA  1 
ATOM   292  C  C   . PRO A 1 37  ? -2.00800  1.51400   19.18400  1.000 20.69755  ? 37  PRO A C   1 
ATOM   293  O  O   . PRO A 1 37  ? -2.18400  0.35800   19.42600  1.000 19.90435  ? 37  PRO A O   1 
ATOM   294  C  CB  . PRO A 1 37  ? 0.07300   2.41400   20.34300  1.000 27.27431  ? 37  PRO A CB  1 
ATOM   295  C  CG  . PRO A 1 37  ? 0.95700   3.59100   20.02700  1.000 26.27507  ? 37  PRO A CG  1 
ATOM   296  C  CD  . PRO A 1 37  ? 0.22000   4.33400   18.94000  1.000 22.36691  ? 37  PRO A CD  1 
ATOM   297  N  N   . GLU A 1 38  ? -2.97600  2.41900   19.04500  1.000 20.95463  ? 38  GLU A N   1 
ATOM   298  C  CA  . GLU A 1 38  ? -4.40200  2.02100   19.15100  1.000 20.52571  ? 38  GLU A CA  1 
ATOM   299  C  C   . GLU A 1 38  ? -4.72300  0.93200   18.13200  1.000 25.08407  ? 38  GLU A C   1 
ATOM   300  O  O   . GLU A 1 38  ? -5.64800  0.16600   18.37700  1.000 24.94011  ? 38  GLU A O   1 
ATOM   301  C  CB  . GLU A 1 38  ? -5.33900  3.20500   18.91700  1.000 22.09218  ? 38  GLU A CB  1 
ATOM   302  C  CG  . GLU A 1 38  ? -5.22300  3.85000   17.55300  1.000 24.76086  ? 38  GLU A CG  1 
ATOM   303  C  CD  . GLU A 1 38  ? -4.31000  5.05800   17.50300  1.000 26.08228  ? 38  GLU A CD  1 
ATOM   304  O  OE1 . GLU A 1 38  ? -3.26000  5.03100   18.15800  1.000 25.49765  ? 38  GLU A OE1 1 
ATOM   305  O  OE2 . GLU A 1 38  ? -4.66300  6.01900   16.81800  1.000 25.19880  ? 38  GLU A OE2 1 
ATOM   306  N  N   . THR A 1 39  ? -3.99500  0.90600   17.01700  1.000 19.92831  ? 39  THR A N   1 
ATOM   307  C  CA  . THR A 1 39  ? -4.25800  -0.09400  15.93600  1.000 17.66027  ? 39  THR A CA  1 
ATOM   308  C  C   . THR A 1 39  ? -3.96800  -1.51600  16.40100  1.000 24.73125  ? 39  THR A C   1 
ATOM   309  O  O   . THR A 1 39  ? -4.57100  -2.43600  15.85500  1.000 22.29269  ? 39  THR A O   1 
ATOM   310  C  CB  . THR A 1 39  ? -3.53000  0.24300   14.63800  1.000 16.34384  ? 39  THR A CB  1 
ATOM   311  O  OG1 . THR A 1 39  ? -2.12100  0.20500   14.86500  1.000 19.32410  ? 39  THR A OG1 1 
ATOM   312  C  CG2 . THR A 1 39  ? -3.96400  1.57500   14.08200  1.000 15.75109  ? 39  THR A CG2 1 
ATOM   313  N  N   . LEU A 1 40  ? -3.10600  -1.72400  17.39600  1.000 25.54929  ? 40  LEU A N   1 
ATOM   314  C  CA  . LEU A 1 40  ? -2.97600  -3.06200  18.02300  1.000 24.21026  ? 40  LEU A CA  1 
ATOM   315  C  C   . LEU A 1 40  ? -4.31200  -3.57400  18.61300  1.000 30.90347  ? 40  LEU A C   1 
ATOM   316  O  O   . LEU A 1 40  ? -4.48000  -4.78300  18.66600  1.000 35.85547  ? 40  LEU A O   1 
ATOM   317  C  CB  . LEU A 1 40  ? -1.91900  -2.93200  19.11400  1.000 30.40192  ? 40  LEU A CB  1 
ATOM   318  C  CG  . LEU A 1 40  ? -0.49400  -2.76000  18.61000  1.000 24.55911  ? 40  LEU A CG  1 
ATOM   319  C  CD1 . LEU A 1 40  ? 0.38400   -2.26400  19.75400  1.000 29.33897  ? 40  LEU A CD1 1 
ATOM   320  C  CD2 . LEU A 1 40  ? 0.03000   -4.07200  18.07600  1.000 26.57569  ? 40  LEU A CD2 1 
ATOM   321  N  N   . GLU A 1 41  ? -5.24800  -2.71200  19.00500  1.000 36.03279  ? 41  GLU A N   1 
ATOM   322  C  CA  . GLU A 1 41  ? -6.50800  -3.13400  19.68500  1.000 31.30340  ? 41  GLU A CA  1 
ATOM   323  C  C   . GLU A 1 41  ? -7.37300  -3.97200  18.72700  1.000 36.33409  ? 41  GLU A C   1 
ATOM   324  O  O   . GLU A 1 41  ? -8.34000  -4.62000  19.22100  1.000 34.00256  ? 41  GLU A O   1 
ATOM   325  C  CB  . GLU A 1 41  ? -7.28300  -1.92200  20.20300  1.000 41.20670  ? 41  GLU A CB  1 
ATOM   326  C  CG  . GLU A 1 41  ? -6.67200  -1.32000  21.46400  1.000 42.40969  ? 41  GLU A CG  1 
ATOM   327  C  CD  . GLU A 1 41  ? -6.95800  0.15000   21.70300  1.000 55.69616  ? 41  GLU A CD  1 
ATOM   328  O  OE1 . GLU A 1 41  ? -7.68100  0.78700   20.86900  1.000 48.43177  ? 41  GLU A OE1 1 
ATOM   329  O  OE2 . GLU A 1 41  ? -6.44200  0.67200   22.72700  1.000 62.57717  ? 41  GLU A OE2 1 
ATOM   330  N  N   . LYS A 1 42  ? -7.06100  -3.96000  17.41300  1.000 25.55389  ? 42  LYS A N   1 
ATOM   331  C  CA  . LYS A 1 42  ? -7.79900  -4.73600  16.37900  1.000 27.27023  ? 42  LYS A CA  1 
ATOM   332  C  C   . LYS A 1 42  ? -7.25700  -6.15900  16.32500  1.000 31.89062  ? 42  LYS A C   1 
ATOM   333  O  O   . LYS A 1 42  ? -7.84100  -6.99300  15.59000  1.000 33.80194  ? 42  LYS A O   1 
ATOM   334  C  CB  . LYS A 1 42  ? -7.71700  -4.03800  15.02100  1.000 25.47846  ? 42  LYS A CB  1 
ATOM   335  C  CG  . LYS A 1 42  ? -8.49000  -2.75500  14.96700  1.000 23.74902  ? 42  LYS A CG  1 
ATOM   336  C  CD  . LYS A 1 42  ? -9.98300  -2.87100  15.20100  1.000 23.82200  ? 42  LYS A CD  1 
ATOM   337  C  CE  . LYS A 1 42  ? -10.66800 -1.53500  15.12600  1.000 29.37969  ? 42  LYS A CE  1 
ATOM   338  N  NZ  . LYS A 1 42  ? -12.12700 -1.66400  15.40000  1.000 29.58261  ? 42  LYS A NZ  1 
ATOM   339  N  N   . PHE A 1 43  ? -6.22500  -6.44800  17.12700  1.000 39.89851  ? 43  PHE A N   1 
ATOM   340  C  CA  . PHE A 1 43  ? -5.62500  -7.79900  17.26900  1.000 44.12095  ? 43  PHE A CA  1 
ATOM   341  C  C   . PHE A 1 43  ? -5.72300  -8.18300  18.75500  1.000 44.78432  ? 43  PHE A C   1 
ATOM   342  O  O   . PHE A 1 43  ? -6.06900  -7.31300  19.58600  1.000 39.75262  ? 43  PHE A O   1 
ATOM   343  C  CB  . PHE A 1 43  ? -4.19400  -7.79600  16.71100  1.000 30.38758  ? 43  PHE A CB  1 
ATOM   344  C  CG  . PHE A 1 43  ? -4.02200  -7.18100  15.34200  1.000 30.10236  ? 43  PHE A CG  1 
ATOM   345  C  CD1 . PHE A 1 43  ? -3.79100  -5.81800  15.17400  1.000 32.21131  ? 43  PHE A CD1 1 
ATOM   346  C  CD2 . PHE A 1 43  ? -4.08500  -7.95200  14.19400  1.000 31.59956  ? 43  PHE A CD2 1 
ATOM   347  C  CE1 . PHE A 1 43  ? -3.59300  -5.27100  13.90900  1.000 23.71230  ? 43  PHE A CE1 1 
ATOM   348  C  CE2 . PHE A 1 43  ? -3.92100  -7.39700  12.92900  1.000 31.75353  ? 43  PHE A CE2 1 
ATOM   349  C  CZ  . PHE A 1 43  ? -3.67700  -6.04700  12.78900  1.000 26.81830  ? 43  PHE A CZ  1 
ATOM   350  N  N   . ASP A 1 44  ? -5.41100  -9.43100  19.10200  1.000 47.46102  ? 44  ASP A N   1 
ATOM   351  C  CA  . ASP A 1 44  ? -5.52000  -9.92100  20.50300  1.000 49.50093  ? 44  ASP A CA  1 
ATOM   352  C  C   . ASP A 1 44  ? -4.63700  -9.08800  21.43300  1.000 59.87491  ? 44  ASP A C   1 
ATOM   353  O  O   . ASP A 1 44  ? -3.48700  -8.76800  21.02800  1.000 51.81751  ? 44  ASP A O   1 
ATOM   354  C  CB  . ASP A 1 44  ? -5.12800  -11.39000 20.60500  1.000 49.19189  ? 44  ASP A CB  1 
ATOM   355  C  CG  . ASP A 1 44  ? -6.20900  -12.30900 20.07300  1.000 54.70826  ? 44  ASP A CG  1 
ATOM   356  O  OD1 . ASP A 1 44  ? -7.24200  -11.78700 19.56400  1.000 57.02572  ? 44  ASP A OD1 1 
ATOM   357  O  OD2 . ASP A 1 44  ? -6.01700  -13.52900 20.18500  1.000 54.21577  ? 44  ASP A OD2 1 
ATOM   358  N  N   . ARG A 1 45  ? -5.09100  -8.79700  22.64900  1.000 61.67935  ? 45  ARG A N   1 
ATOM   359  C  CA  . ARG A 1 45  ? -4.25300  -8.03200  23.60600  1.000 71.79033  ? 45  ARG A CA  1 
ATOM   360  C  C   . ARG A 1 45  ? -3.00400  -8.84400  23.99700  1.000 77.12584  ? 45  ARG A C   1 
ATOM   361  O  O   . ARG A 1 45  ? -2.95900  -10.05300 23.73100  1.000 70.73765  ? 45  ARG A O   1 
ATOM   362  C  CB  . ARG A 1 45  ? -5.06700  -7.63300  24.83600  1.000 77.36064  ? 45  ARG A CB  1 
ATOM   363  C  CG  . ARG A 1 45  ? -6.39700  -6.95300  24.54500  1.000 87.38007  ? 45  ARG A CG  1 
ATOM   364  C  CD  . ARG A 1 45  ? -6.79300  -6.06600  25.71400  1.000 97.92140  ? 45  ARG A CD  1 
ATOM   365  N  NE  . ARG A 1 45  ? -8.20900  -5.73600  25.82400  1.000 107.83011 ? 45  ARG A NE  1 
ATOM   366  C  CZ  . ARG A 1 45  ? -8.71600  -4.90600  26.73500  1.000 106.35395 ? 45  ARG A CZ  1 
ATOM   367  N  NH1 . ARG A 1 45  ? -7.91600  -4.31200  27.60300  1.000 103.90154 ? 45  ARG A NH1 1 
ATOM   368  N  NH2 . ARG A 1 45  ? -10.01500 -4.66600  26.77300  1.000 98.38000  ? 45  ARG A NH2 1 
ATOM   369  N  N   . CYS A 1 46  ? -2.00600  -8.15600  24.56800  1.000 78.25165  ? 46  CYS A N   1 
ATOM   370  C  CA  . CYS A 1 46  ? -0.87000  -7.61200  23.78300  1.000 82.64895  ? 46  CYS A CA  1 
ATOM   371  C  C   . CYS A 1 46  ? -1.34000  -6.32900  23.07500  1.000 88.31040  ? 46  CYS A C   1 
ATOM   372  O  O   . CYS A 1 46  ? -0.79400  -5.99100  21.99600  1.000 81.97115  ? 46  CYS A O   1 
ATOM   373  C  CB  . CYS A 1 46  ? -0.29200  -8.64000  22.82000  1.000 83.45000  ? 46  CYS A CB  1 
ATOM   374  S  SG  . CYS A 1 46  ? 0.47300   -10.06800 23.62100  1.000 98.19000  ? 46  CYS A SG  1 
ATOM   375  N  N   . LYS A 1 47  ? -2.37300  -5.67800  23.61800  1.000 79.96294  ? 47  LYS A N   1 
ATOM   376  C  CA  . LYS A 1 47  ? -2.74800  -4.36300  23.08100  1.000 75.87040  ? 47  LYS A CA  1 
ATOM   377  C  C   . LYS A 1 47  ? -1.54100  -3.48600  23.39700  1.000 74.37884  ? 47  LYS A C   1 
ATOM   378  O  O   . LYS A 1 47  ? -1.41700  -2.41200  22.78900  1.000 71.27512  ? 47  LYS A O   1 
ATOM   379  C  CB  . LYS A 1 47  ? -3.99900  -3.84300  23.78800  1.000 83.10822  ? 47  LYS A CB  1 
ATOM   380  C  CG  . LYS A 1 47  ? -3.81800  -3.44000  25.24500  1.000 83.41571  ? 47  LYS A CG  1 
ATOM   381  C  CD  . LYS A 1 47  ? -5.10300  -2.97200  25.88400  1.000 86.43404  ? 47  LYS A CD  1 
ATOM   382  C  CE  . LYS A 1 47  ? -5.86500  -1.99200  25.01700  1.000 91.32979  ? 47  LYS A CE  1 
ATOM   383  N  NZ  . LYS A 1 47  ? -7.19300  -1.66900  25.59100  1.000 85.24488  ? 47  LYS A NZ  1 
ATOM   384  N  N   . HIS A 1 48  ? -0.70700  -3.94400  24.34500  1.000 65.95731  ? 48  HIS A N   1 
ATOM   385  C  CA  . HIS A 1 48  ? 0.52200   -3.20500  24.74200  1.000 53.87296  ? 48  HIS A CA  1 
ATOM   386  C  C   . HIS A 1 48  ? 1.59000   -3.26200  23.64400  1.000 44.54621  ? 48  HIS A C   1 
ATOM   387  O  O   . HIS A 1 48  ? 1.79100   -4.36000  23.08700  1.000 38.42482  ? 48  HIS A O   1 
ATOM   388  C  CB  . HIS A 1 48  ? 1.05900   -3.75400  26.06800  1.000 52.37877  ? 48  HIS A CB  1 
ATOM   389  C  CG  . HIS A 1 48  ? 0.15200   -3.45300  27.21500  1.000 56.01965  ? 48  HIS A CG  1 
ATOM   390  N  ND1 . HIS A 1 48  ? 0.11100   -2.20900  27.81600  1.000 58.55110  ? 48  HIS A ND1 1 
ATOM   391  C  CD2 . HIS A 1 48  ? -0.76200  -4.21000  27.85800  1.000 57.92668  ? 48  HIS A CD2 1 
ATOM   392  C  CE1 . HIS A 1 48  ? -0.77900  -2.21700  28.78600  1.000 54.98021  ? 48  HIS A CE1 1 
ATOM   393  N  NE2 . HIS A 1 48  ? -1.32400  -3.43500  28.83600  1.000 59.85011  ? 48  HIS A NE2 1 
ATOM   394  N  N   . LEU A 1 49  ? 2.19600   -2.11500  23.33700  1.000 32.64263  ? 49  LEU A N   1 
ATOM   395  C  CA  . LEU A 1 49  ? 3.28200   -2.03100  22.32000  1.000 37.21971  ? 49  LEU A CA  1 
ATOM   396  C  C   . LEU A 1 49  ? 4.50700   -2.78200  22.86200  1.000 40.48142  ? 49  LEU A C   1 
ATOM   397  O  O   . LEU A 1 49  ? 4.93900   -2.50800  24.01100  1.000 43.22477  ? 49  LEU A O   1 
ATOM   398  C  CB  . LEU A 1 49  ? 3.57800   -0.55600  22.04400  1.000 33.80020  ? 49  LEU A CB  1 
ATOM   399  C  CG  . LEU A 1 49  ? 4.45600   -0.25600  20.83000  1.000 40.57944  ? 49  LEU A CG  1 
ATOM   400  C  CD1 . LEU A 1 49  ? 3.71700   -0.59500  19.54900  1.000 41.73628  ? 49  LEU A CD1 1 
ATOM   401  C  CD2 . LEU A 1 49  ? 4.88100   1.20900   20.81700  1.000 35.43837  ? 49  LEU A CD2 1 
ATOM   402  N  N   . LYS A 1 50  ? 4.98300   -3.75000  22.10100  1.000 32.97810  ? 50  LYS A N   1 
ATOM   403  C  CA  . LYS A 1 50  ? 6.16000   -4.51200  22.54500  1.000 30.28146  ? 50  LYS A CA  1 
ATOM   404  C  C   . LYS A 1 50  ? 7.39500   -3.77100  22.02800  1.000 26.85667  ? 50  LYS A C   1 
ATOM   405  O  O   . LYS A 1 50  ? 7.24300   -2.81900  21.25800  1.000 25.06746  ? 50  LYS A O   1 
ATOM   406  C  CB  . LYS A 1 50  ? 6.07000   -5.91700  21.96800  1.000 29.58365  ? 50  LYS A CB  1 
ATOM   407  C  CG  . LYS A 1 50  ? 4.90900   -6.78000  22.44600  1.000 43.61345  ? 50  LYS A CG  1 
ATOM   408  C  CD  . LYS A 1 50  ? 5.38400   -8.09500  23.02800  1.000 41.91071  ? 50  LYS A CD  1 
ATOM   409  C  CE  . LYS A 1 50  ? 4.32400   -8.85500  23.79700  1.000 59.65219  ? 50  LYS A CE  1 
ATOM   410  N  NZ  . LYS A 1 50  ? 4.92000   -9.82900  24.74600  1.000 50.89183  ? 50  LYS A NZ  1 
ATOM   411  N  N   . THR A 1 51  ? 8.56200   -4.24100  22.41000  1.000 18.79157  ? 51  THR A N   1 
ATOM   412  C  CA  . THR A 1 51  ? 9.80000   -3.64100  21.87200  1.000 15.76867  ? 51  THR A CA  1 
ATOM   413  C  C   . THR A 1 51  ? 9.92000   -3.91800  20.35200  1.000 14.92631  ? 51  THR A C   1 
ATOM   414  O  O   . THR A 1 51  ? 9.32600   -4.92400  19.85600  1.000 16.93589  ? 51  THR A O   1 
ATOM   415  C  CB  . THR A 1 51  ? 11.04100  -4.18500  22.59600  1.000 18.15700  ? 51  THR A CB  1 
ATOM   416  O  OG1 . THR A 1 51  ? 11.13000  -5.58200  22.34900  1.000 17.81315  ? 51  THR A OG1 1 
ATOM   417  C  CG2 . THR A 1 51  ? 11.02500  -3.96200  24.10400  1.000 19.19889  ? 51  THR A CG2 1 
ATOM   418  N  N   . GLU A 1 52  ? 10.71100  -3.11100  19.66700  1.000 17.10097  ? 52  GLU A N   1 
ATOM   419  C  CA  . GLU A 1 52  ? 10.98700  -3.35200  18.23100  1.000 19.09614  ? 52  GLU A CA  1 
ATOM   420  C  C   . GLU A 1 52  ? 11.59900  -4.73200  18.01300  1.000 17.36340  ? 52  GLU A C   1 
ATOM   421  O  O   . GLU A 1 52  ? 11.19600  -5.47600  17.09200  1.000 17.48484  ? 52  GLU A O   1 
ATOM   422  C  CB  . GLU A 1 52  ? 11.88600  -2.25700  17.68700  1.000 21.41532  ? 52  GLU A CB  1 
ATOM   423  C  CG  . GLU A 1 52  ? 12.07900  -2.40500  16.20600  1.000 25.96889  ? 52  GLU A CG  1 
ATOM   424  C  CD  . GLU A 1 52  ? 12.92200  -1.26800  15.68400  1.000 37.85647  ? 52  GLU A CD  1 
ATOM   425  O  OE1 . GLU A 1 52  ? 14.15100  -1.41000  15.72000  1.000 38.46314  ? 52  GLU A OE1 1 
ATOM   426  O  OE2 . GLU A 1 52  ? 12.34100  -0.24300  15.29400  1.000 41.87635  ? 52  GLU A OE2 1 
ATOM   427  N  N   . ALA A 1 53  ? 12.53300  -5.17400  18.86200  1.000 18.30617  ? 53  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 53  ? 13.13300  -6.49300  18.64300  1.000 16.84159  ? 53  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 53  ? 12.10100  -7.59800  18.77300  1.000 18.14398  ? 53  ALA A C   1 
ATOM   430  O  O   . ALA A 1 53  ? 12.17900  -8.61100  18.06700  1.000 17.93176  ? 53  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 53  ? 14.29400  -6.73900  19.58300  1.000 20.07194  ? 53  ALA A CB  1 
ATOM   432  N  N   . GLU A 1 54  ? 11.17000  -7.49700  19.72800  1.000 16.54570  ? 54  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 54  ? 10.10000  -8.50300  19.87000  1.000 17.82641  ? 54  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 54  ? 9.23200   -8.49600  18.62300  1.000 16.79265  ? 54  GLU A C   1 
ATOM   435  O  O   . GLU A 1 54  ? 8.85200   -9.59800  18.15200  1.000 18.73638  ? 54  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 54  ? 9.23700   -8.17700  21.07100  1.000 18.20775  ? 54  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 54  ? 9.86500   -8.57300  22.37600  1.000 22.29071  ? 54  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 54  ? 9.06500   -8.06600  23.55600  1.000 30.01858  ? 54  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 54  ? 9.07300   -6.81900  23.84500  1.000 30.81075  ? 54  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 54  ? 8.42800   -8.91100  24.16900  1.000 29.23215  ? 54  GLU A OE2 1 
ATOM   441  N  N   A MET A 1 55  ? 8.94000   -7.31000  18.08900  0.490 16.44494  ? 55  MET A N   1 
ATOM   442  N  N   B MET A 1 55  ? 8.95000   -7.31700  18.07800  0.510 16.45476  ? 55  MET A N   1 
ATOM   443  C  CA  A MET A 1 55  ? 8.12000   -7.21100  16.85300  0.490 14.45559  ? 55  MET A CA  1 
ATOM   444  C  CA  B MET A 1 55  ? 8.11600   -7.25100  16.85300  0.510 14.43071  ? 55  MET A CA  1 
ATOM   445  C  C   A MET A 1 55  ? 8.86700   -7.86100  15.68600  0.490 15.89785  ? 55  MET A C   1 
ATOM   446  C  C   B MET A 1 55  ? 8.86800   -7.86100  15.67200  0.510 15.90201  ? 55  MET A C   1 
ATOM   447  O  O   A MET A 1 55  ? 8.21900   -8.60900  14.94500  0.490 16.81279  ? 55  MET A O   1 
ATOM   448  O  O   B MET A 1 55  ? 8.22700   -8.59800  14.91900  0.510 16.79629  ? 55  MET A O   1 
ATOM   449  C  CB  A MET A 1 55  ? 7.75000   -5.76900  16.53400  0.490 16.64730  ? 55  MET A CB  1 
ATOM   450  C  CB  B MET A 1 55  ? 7.65500   -5.83200  16.56600  0.510 16.60373  ? 55  MET A CB  1 
ATOM   451  C  CG  A MET A 1 55  ? 6.81600   -5.17100  17.56500  0.490 15.50011  ? 55  MET A CG  1 
ATOM   452  C  CG  B MET A 1 55  ? 6.55700   -5.45400  17.52000  0.510 16.68032  ? 55  MET A CG  1 
ATOM   453  S  SD  A MET A 1 55  ? 6.18100   -3.56700  17.08500  0.490 20.82405  ? 55  MET A SD  1 
ATOM   454  S  SD  B MET A 1 55  ? 5.72000   -3.95700  17.09300  0.510 22.20293  ? 55  MET A SD  1 
ATOM   455  C  CE  A MET A 1 55  ? 6.03300   -2.74700  18.66600  0.490 32.43274  ? 55  MET A CE  1 
ATOM   456  C  CE  B MET A 1 55  ? 7.06700   -2.80700  17.33000  0.510 17.72468  ? 55  MET A CE  1 
ATOM   457  N  N   . LYS A 1 56  ? 10.17700  -7.67300  15.58300  1.000 18.24828  ? 56  LYS A N   1 
ATOM   458  C  CA  . LYS A 1 56  ? 10.98200  -8.25700  14.47000  1.000 17.17017  ? 56  LYS A CA  1 
ATOM   459  C  C   . LYS A 1 56  ? 11.07200  -9.76900  14.62600  1.000 20.22795  ? 56  LYS A C   1 
ATOM   460  O  O   . LYS A 1 56  ? 11.26800  -10.45000 13.58900  1.000 22.16376  ? 56  LYS A O   1 
ATOM   461  C  CB  . LYS A 1 56  ? 12.38000  -7.64600  14.34600  1.000 19.85904  ? 56  LYS A CB  1 
ATOM   462  C  CG  . LYS A 1 56  ? 12.35800  -6.17900  13.98600  1.000 21.66880  ? 56  LYS A CG  1 
ATOM   463  C  CD  . LYS A 1 56  ? 13.70600  -5.55500  13.72200  1.000 26.25945  ? 56  LYS A CD  1 
ATOM   464  C  CE  . LYS A 1 56  ? 13.56200  -4.11000  13.28500  1.000 39.64129  ? 56  LYS A CE  1 
ATOM   465  N  NZ  . LYS A 1 56  ? 14.38900  -3.81900  12.08900  1.000 46.56590  ? 56  LYS A NZ  1 
ATOM   466  N  N   . ALA A 1 57  ? 11.08200  -10.31600 15.85600  1.000 17.42071  ? 57  ALA A N   1 
ATOM   467  C  CA  . ALA A 1 57  ? 11.21700  -11.75300 16.10100  1.000 19.18740  ? 57  ALA A CA  1 
ATOM   468  C  C   . ALA A 1 57  ? 9.90400   -12.46600 15.88000  1.000 21.88082  ? 57  ALA A C   1 
ATOM   469  O  O   . ALA A 1 57  ? 9.91800   -13.69700 15.83100  1.000 24.50971  ? 57  ALA A O   1 
ATOM   470  C  CB  . ALA A 1 57  ? 11.68800  -12.00400 17.51100  1.000 19.54330  ? 57  ALA A CB  1 
ATOM   471  N  N   . SER A 1 58  ? 8.77600   -11.73700 15.81800  1.000 17.99361  ? 58  SER A N   1 
ATOM   472  C  CA  . SER A 1 58  ? 7.42500   -12.34000 15.77200  1.000 16.94757  ? 58  SER A CA  1 
ATOM   473  C  C   . SER A 1 58  ? 7.13900   -13.03900 14.42700  1.000 17.24275  ? 58  SER A C   1 
ATOM   474  O  O   . SER A 1 58  ? 7.06000   -12.33800 13.39700  1.000 16.22813  ? 58  SER A O   1 
ATOM   475  C  CB  . SER A 1 58  ? 6.40200   -11.28200 16.02400  1.000 16.19090  ? 58  SER A CB  1 
ATOM   476  O  OG  . SER A 1 58  ? 5.08200   -11.82800 15.94100  1.000 18.40076  ? 58  SER A OG  1 
ATOM   477  N  N   . GLU A 1 59  ? 6.96900   -14.35200 14.42800  1.000 18.39281  ? 59  GLU A N   1 
ATOM   478  C  CA  . GLU A 1 59  ? 6.48900   -15.09200 13.25000  1.000 19.15912  ? 59  GLU A CA  1 
ATOM   479  C  C   . GLU A 1 59  ? 5.10600   -14.56700 12.83700  1.000 16.95860  ? 59  GLU A C   1 
ATOM   480  O  O   . GLU A 1 59  ? 4.90400   -14.33500 11.62000  1.000 16.48382  ? 59  GLU A O   1 
ATOM   481  C  CB  . GLU A 1 59  ? 6.47500   -16.59100 13.56000  1.000 20.87270  ? 59  GLU A CB  1 
ATOM   482  C  CG  . GLU A 1 59  ? 5.94300   -17.44400 12.44100  1.000 24.93976  ? 59  GLU A CG  1 
ATOM   483  C  CD  . GLU A 1 59  ? 5.96700   -18.91400 12.83000  1.000 34.35381  ? 59  GLU A CD  1 
ATOM   484  O  OE1 . GLU A 1 59  ? 4.97300   -19.60000 12.55500  1.000 43.39623  ? 59  GLU A OE1 1 
ATOM   485  O  OE2 . GLU A 1 59  ? 6.97300   -19.33700 13.43100  1.000 34.20764  ? 59  GLU A OE2 1 
ATOM   486  N  N   . ASP A 1 60  ? 4.21700   -14.30300 13.79200  1.000 16.84824  ? 60  ASP A N   1 
ATOM   487  C  CA  . ASP A 1 60  ? 2.85200   -13.83300 13.44800  1.000 16.91515  ? 60  ASP A CA  1 
ATOM   488  C  C   . ASP A 1 60  ? 2.91800   -12.47300 12.75000  1.000 17.75255  ? 60  ASP A C   1 
ATOM   489  O  O   . ASP A 1 60  ? 2.21500   -12.30500 11.73400  1.000 16.62838  ? 60  ASP A O   1 
ATOM   490  C  CB  . ASP A 1 60  ? 1.91800   -13.71100 14.64900  1.000 21.40203  ? 60  ASP A CB  1 
ATOM   491  C  CG  . ASP A 1 60  ? 0.47800   -13.58600 14.18200  1.000 35.42853  ? 60  ASP A CG  1 
ATOM   492  O  OD1 . ASP A 1 60  ? 0.04100   -14.56900 13.50600  1.000 33.41806  ? 60  ASP A OD1 1 
ATOM   493  O  OD2 . ASP A 1 60  ? -0.22000  -12.50100 14.44500  1.000 31.56133  ? 60  ASP A OD2 1 
ATOM   494  N  N   . LEU A 1 61  ? 3.71400   -11.52600 13.25300  1.000 16.17014  ? 61  LEU A N   1 
ATOM   495  C  CA  . LEU A 1 61  ? 3.75600   -10.18400 12.63900  1.000 13.57727  ? 61  LEU A CA  1 
ATOM   496  C  C   . LEU A 1 61  ? 4.34600   -10.31800 11.23000  1.000 14.37647  ? 61  LEU A C   1 
ATOM   497  O  O   . LEU A 1 61  ? 3.85000   -9.66400  10.30700  1.000 13.32956  ? 61  LEU A O   1 
ATOM   498  C  CB  . LEU A 1 61  ? 4.52300   -9.21500  13.54400  1.000 14.50760  ? 61  LEU A CB  1 
ATOM   499  C  CG  . LEU A 1 61  ? 4.50700   -7.77100  13.12800  1.000 20.16116  ? 61  LEU A CG  1 
ATOM   500  C  CD1 . LEU A 1 61  ? 4.78400   -6.97600  14.38500  1.000 21.16945  ? 61  LEU A CD1 1 
ATOM   501  C  CD2 . LEU A 1 61  ? 5.58600   -7.49100  12.07600  1.000 23.55197  ? 61  LEU A CD2 1 
ATOM   502  N  N   . LYS A 1 62  ? 5.39200   -11.12400 11.03200  1.000 13.18002  ? 62  LYS A N   1 
ATOM   503  C  CA  . LYS A 1 62  ? 6.02600   -11.28400 9.70800   1.000 11.66943  ? 62  LYS A CA  1 
ATOM   504  C  C   . LYS A 1 62  ? 4.97500   -11.87400 8.75600   1.000 14.09976  ? 62  LYS A C   1 
ATOM   505  O  O   . LYS A 1 62  ? 4.95900   -11.47900 7.61600   1.000 15.08538  ? 62  LYS A O   1 
ATOM   506  C  CB  . LYS A 1 62  ? 7.28000   -12.15500 9.82000   1.000 15.29796  ? 62  LYS A CB  1 
ATOM   507  C  CG  . LYS A 1 62  ? 8.16000   -12.15500 8.58600   1.000 14.07395  ? 62  LYS A CG  1 
ATOM   508  C  CD  . LYS A 1 62  ? 9.53700   -12.80800 8.89500   1.000 18.99699  ? 62  LYS A CD  1 
ATOM   509  C  CE  . LYS A 1 62  ? 10.56400  -12.70900 7.79900   1.000 27.34358  ? 62  LYS A CE  1 
ATOM   510  N  NZ  . LYS A 1 62  ? 11.90100  -13.13700 8.31200   1.000 23.65690  ? 62  LYS A NZ  1 
ATOM   511  N  N   . LYS A 1 63  ? 4.19900   -12.84500 9.19900   1.000 13.37317  ? 63  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 63  ? 3.13000   -13.39800 8.32500   1.000 14.10882  ? 63  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 63  ? 2.12300   -12.29400 7.99800   1.000 13.11624  ? 63  LYS A C   1 
ATOM   514  O  O   . LYS A 1 63  ? 1.73800   -12.17300 6.81300   1.000 13.65084  ? 63  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 63  ? 2.45000   -14.61500 8.97900   1.000 13.84764  ? 63  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 63  ? 3.31300   -15.86400 9.02000   1.000 18.04237  ? 63  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 63  ? 2.80800   -16.88700 10.00500  1.000 19.62197  ? 63  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 63  ? 1.50000   -17.54800 9.67600   1.000 39.88477  ? 63  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 63  ? 1.12000   -18.53200 10.72900  1.000 42.80110  ? 63  LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 64  ? 1.67100   -11.50000 8.96400   1.000 14.40453  ? 64  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 64  ? 0.67100   -10.44500 8.69300   1.000 14.10877  ? 64  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 64  ? 1.23000   -9.49100  7.64400   1.000 12.98426  ? 64  HIS A C   1 
ATOM   523  O  O   . HIS A 1 64  ? 0.50000   -9.03200  6.75900   1.000 13.23668  ? 64  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 64  ? 0.33100   -9.59800  9.93300   1.000 16.69066  ? 64  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 64  ? -0.58200  -10.22000 10.91500  1.000 20.76407  ? 64  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 64  ? -1.94700  -10.25600 10.70400  1.000 27.66581  ? 64  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 64  ? -0.36400  -10.71600 12.14800  1.000 22.74689  ? 64  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 64  ? -2.52300  -10.84100 11.75200  1.000 30.64702  ? 64  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 64  ? -1.57600  -11.13500 12.64600  1.000 26.12227  ? 64  HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 65  ? 2.48400   -9.09000  7.77300   1.000 12.03813  ? 65  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 65  ? 3.02700   -8.08900  6.84000   1.000 12.69899  ? 65  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 65  ? 3.01100   -8.60700  5.40100   1.000 12.85236  ? 65  GLY A C   1 
ATOM   533  O  O   . GLY A 1 65  ? 2.72100   -7.88600  4.46200   1.000 11.55695  ? 65  GLY A O   1 
ATOM   534  N  N   . VAL A 1 66  ? 3.26800   -9.89600  5.23700   1.000 12.95157  ? 66  VAL A N   1 
ATOM   535  C  CA  . VAL A 1 66  ? 3.23300   -10.50200 3.89100   1.000 12.34934  ? 66  VAL A CA  1 
ATOM   536  C  C   . VAL A 1 66  ? 1.79200   -10.62300 3.42400   1.000 11.09836  ? 66  VAL A C   1 
ATOM   537  O  O   . VAL A 1 66  ? 1.54900   -10.31700 2.23600   1.000 12.43520  ? 66  VAL A O   1 
ATOM   538  C  CB  . VAL A 1 66  ? 3.91800   -11.88700 3.87300   1.000 10.79824  ? 66  VAL A CB  1 
ATOM   539  C  CG1 . VAL A 1 66  ? 3.71500   -12.59200 2.56300   1.000 13.28379  ? 66  VAL A CG1 1 
ATOM   540  C  CG2 . VAL A 1 66  ? 5.41800   -11.73900 4.15500   1.000 11.95650  ? 66  VAL A CG2 1 
ATOM   541  N  N   . THR A 1 67  ? 0.83700   -10.96200 4.30900   1.000 11.71085  ? 67  THR A N   1 
ATOM   542  C  CA  . THR A 1 67  ? -0.59400  -11.01800 3.91200   1.000 12.85992  ? 67  THR A CA  1 
ATOM   543  C  C   . THR A 1 67  ? -1.02200  -9.67800  3.35200   1.000 12.34419  ? 67  THR A C   1 
ATOM   544  O  O   . THR A 1 67  ? -1.65600  -9.57000  2.28700   1.000 13.38813  ? 67  THR A O   1 
ATOM   545  C  CB  . THR A 1 67  ? -1.40700  -11.42000 5.12300   1.000 12.74620  ? 67  THR A CB  1 
ATOM   546  O  OG1 . THR A 1 67  ? -1.04700  -12.76600 5.50700   1.000 15.44034  ? 67  THR A OG1 1 
ATOM   547  C  CG2 . THR A 1 67  ? -2.87900  -11.37200 4.80100   1.000 14.17107  ? 67  THR A CG2 1 
ATOM   548  N  N   . VAL A 1 68  ? -0.67300  -8.60300  4.05100   1.000 10.69389  ? 68  VAL A N   1 
ATOM   549  C  CA  . VAL A 1 68  ? -1.07900  -7.24600  3.63500   1.000 10.29920  ? 68  VAL A CA  1 
ATOM   550  C  C   . VAL A 1 68  ? -0.43700  -6.90000  2.29600   1.000 10.97020  ? 68  VAL A C   1 
ATOM   551  O  O   . VAL A 1 68  ? -1.11300  -6.42900  1.35400   1.000 11.94467  ? 68  VAL A O   1 
ATOM   552  C  CB  . VAL A 1 68  ? -0.73100  -6.18500  4.69800   1.000 13.27624  ? 68  VAL A CB  1 
ATOM   553  C  CG1 . VAL A 1 68  ? -0.91900  -4.76800  4.16100   1.000 12.93413  ? 68  VAL A CG1 1 
ATOM   554  C  CG2 . VAL A 1 68  ? -1.54100  -6.42600  5.96500   1.000 16.63459  ? 68  VAL A CG2 1 
ATOM   555  N  N   . LEU A 1 69  ? 0.89400   -7.03200  2.19000   1.000 11.15210  ? 69  LEU A N   1 
ATOM   556  C  CA  . LEU A 1 69  ? 1.59600   -6.52800  1.00500   1.000 11.39060  ? 69  LEU A CA  1 
ATOM   557  C  C   . LEU A 1 69  ? 1.27200   -7.41600  -0.21100  1.000 10.33048  ? 69  LEU A C   1 
ATOM   558  O  O   . LEU A 1 69  ? 1.23000   -6.88800  -1.30900  1.000 11.68934  ? 69  LEU A O   1 
ATOM   559  C  CB  . LEU A 1 69  ? 3.11500   -6.44800  1.23200   1.000 10.23813  ? 69  LEU A CB  1 
ATOM   560  C  CG  . LEU A 1 69  ? 3.55000   -5.42000  2.28900   1.000 9.97923   ? 69  LEU A CG  1 
ATOM   561  C  CD1 . LEU A 1 69  ? 5.07300   -5.40000  2.37300   1.000 11.67143  ? 69  LEU A CD1 1 
ATOM   562  C  CD2 . LEU A 1 69  ? 3.01100   -4.04700  1.99200   1.000 15.61772  ? 69  LEU A CD2 1 
ATOM   563  N  N   . THR A 1 70  ? 0.97400   -8.70100  -0.01800  1.000 11.31789  ? 70  THR A N   1 
ATOM   564  C  CA  . THR A 1 70  ? 0.59600   -9.55800  -1.18000  1.000 11.22256  ? 70  THR A CA  1 
ATOM   565  C  C   . THR A 1 70  ? -0.71300  -9.00300  -1.77900  1.000 10.01106  ? 70  THR A C   1 
ATOM   566  O  O   . THR A 1 70  ? -0.83300  -8.83200  -2.98500  1.000 11.44595  ? 70  THR A O   1 
ATOM   567  C  CB  . THR A 1 70  ? 0.46300   -11.00500 -0.75300  1.000 12.09163  ? 70  THR A CB  1 
ATOM   568  O  OG1 . THR A 1 70  ? 1.73900   -11.47800 -0.34100  1.000 14.24388  ? 70  THR A OG1 1 
ATOM   569  C  CG2 . THR A 1 70  ? -0.06900  -11.87500 -1.86300  1.000 14.18857  ? 70  THR A CG2 1 
ATOM   570  N  N   . ALA A 1 71  ? -1.69500  -8.76000  -0.90300  1.000 12.23463  ? 71  ALA A N   1 
ATOM   571  C  CA  . ALA A 1 71  ? -3.01300  -8.29700  -1.35100  1.000 10.13374  ? 71  ALA A CA  1 
ATOM   572  C  C   . ALA A 1 71  ? -2.85700  -6.91200  -1.97800  1.000 10.97364  ? 71  ALA A C   1 
ATOM   573  O  O   . ALA A 1 71  ? -3.48100  -6.63200  -3.01000  1.000 10.79354  ? 71  ALA A O   1 
ATOM   574  C  CB  . ALA A 1 71  ? -3.99400  -8.34100  -0.23800  1.000 11.74580  ? 71  ALA A CB  1 
ATOM   575  N  N   . LEU A 1 72  ? -2.15900  -5.99800  -1.29600  1.000 10.51629  ? 72  LEU A N   1 
ATOM   576  C  CA  . LEU A 1 72  ? -2.01000  -4.62300  -1.82200  1.000 12.05029  ? 72  LEU A CA  1 
ATOM   577  C  C   . LEU A 1 72  ? -1.26700  -4.62300  -3.16800  1.000 12.50719  ? 72  LEU A C   1 
ATOM   578  O  O   . LEU A 1 72  ? -1.67500  -3.86700  -4.09400  1.000 13.57334  ? 72  LEU A O   1 
ATOM   579  C  CB  . LEU A 1 72  ? -1.31300  -3.73700  -0.78900  1.000 12.85723  ? 72  LEU A CB  1 
ATOM   580  C  CG  . LEU A 1 72  ? -1.17900  -2.28800  -1.21300  1.000 11.42687  ? 72  LEU A CG  1 
ATOM   581  C  CD1 . LEU A 1 72  ? -2.50400  -1.65300  -1.53600  1.000 14.34843  ? 72  LEU A CD1 1 
ATOM   582  C  CD2 . LEU A 1 72  ? -0.39700  -1.54000  -0.13700  1.000 16.63585  ? 72  LEU A CD2 1 
ATOM   583  N  N   . GLY A 1 73  ? -0.22100  -5.42800  -3.30300  1.000 11.58882  ? 73  GLY A N   1 
ATOM   584  C  CA  . GLY A 1 73  ? 0.52000   -5.48900  -4.57000  1.000 13.56389  ? 73  GLY A CA  1 
ATOM   585  C  C   . GLY A 1 73  ? -0.38800  -5.94500  -5.70300  1.000 11.29316  ? 73  GLY A C   1 
ATOM   586  O  O   . GLY A 1 73  ? -0.36100  -5.35800  -6.78000  1.000 14.87188  ? 73  GLY A O   1 
ATOM   587  N  N   . ALA A 1 74  ? -1.22900  -6.93700  -5.46500  1.000 10.96869  ? 74  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 74  ? -2.18200  -7.39300  -6.50600  1.000 11.65917  ? 74  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 74  ? -3.14000  -6.26600  -6.86500  1.000 13.54441  ? 74  ALA A C   1 
ATOM   590  O  O   . ALA A 1 74  ? -3.44100  -6.06800  -8.06500  1.000 14.94745  ? 74  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 74  ? -2.90400  -8.65000  -6.09000  1.000 12.71682  ? 74  ALA A CB  1 
ATOM   592  N  N   . ILE A 1 75  ? -3.58100  -5.49100  -5.87000  1.000 11.95504  ? 75  ILE A N   1 
ATOM   593  C  CA  . ILE A 1 75  ? -4.48100  -4.33400  -6.12800  1.000 12.43316  ? 75  ILE A CA  1 
ATOM   594  C  C   . ILE A 1 75  ? -3.73600  -3.29700  -6.98100  1.000 10.25168  ? 75  ILE A C   1 
ATOM   595  O  O   . ILE A 1 75  ? -4.29100  -2.83900  -7.97900  1.000 12.98562  ? 75  ILE A O   1 
ATOM   596  C  CB  . ILE A 1 75  ? -5.01300  -3.78000  -4.79900  1.000 12.40294  ? 75  ILE A CB  1 
ATOM   597  C  CG1 . ILE A 1 75  ? -6.06700  -4.71100  -4.21200  1.000 13.10873  ? 75  ILE A CG1 1 
ATOM   598  C  CG2 . ILE A 1 75  ? -5.53200  -2.36000  -4.95000  1.000 12.45531  ? 75  ILE A CG2 1 
ATOM   599  C  CD1 . ILE A 1 75  ? -6.23000  -4.58000  -2.70000  1.000 15.28261  ? 75  ILE A CD1 1 
ATOM   600  N  N   . LEU A 1 76  ? -2.51800  -2.92000  -6.61300  1.000 12.60855  ? 76  LEU A N   1 
ATOM   601  C  CA  . LEU A 1 76  ? -1.77800  -1.85000  -7.33600  1.000 12.94309  ? 76  LEU A CA  1 
ATOM   602  C  C   . LEU A 1 76  ? -1.52000  -2.29300  -8.77400  1.000 13.07690  ? 76  LEU A C   1 
ATOM   603  O  O   . LEU A 1 76  ? -1.57900  -1.45500  -9.67400  1.000 14.52972  ? 76  LEU A O   1 
ATOM   604  C  CB  . LEU A 1 76  ? -0.46800  -1.53000  -6.63300  1.000 13.38510  ? 76  LEU A CB  1 
ATOM   605  C  CG  . LEU A 1 76  ? -0.58400  -0.87500  -5.25200  1.000 13.52061  ? 76  LEU A CG  1 
ATOM   606  C  CD1 . LEU A 1 76  ? 0.77900   -0.75300  -4.59800  1.000 16.26976  ? 76  LEU A CD1 1 
ATOM   607  C  CD2 . LEU A 1 76  ? -1.27900  0.47300   -5.32700  1.000 14.70703  ? 76  LEU A CD2 1 
ATOM   608  N  N   . LYS A 1 77  ? -1.26000  -3.57000  -8.98200  1.000 12.90181  ? 77  LYS A N   1 
ATOM   609  C  CA  . LYS A 1 77  ? -0.97300  -4.02600  -10.37900 1.000 12.92262  ? 77  LYS A CA  1 
ATOM   610  C  C   . LYS A 1 77  ? -2.20800  -3.91200  -11.26800 1.000 14.66489  ? 77  LYS A C   1 
ATOM   611  O  O   . LYS A 1 77  ? -2.03800  -3.95300  -12.50800 1.000 17.52126  ? 77  LYS A O   1 
ATOM   612  C  CB  . LYS A 1 77  ? -0.37500  -5.41800  -10.36100 1.000 14.42809  ? 77  LYS A CB  1 
ATOM   613  C  CG  . LYS A 1 77  ? 1.02000   -5.46800  -9.77400  1.000 16.13384  ? 77  LYS A CG  1 
ATOM   614  C  CD  . LYS A 1 77  ? 1.57400   -6.83100  -9.65300  1.000 15.80802  ? 77  LYS A CD  1 
ATOM   615  C  CE  . LYS A 1 77  ? 2.87100   -6.87700  -8.87300  1.000 16.97544  ? 77  LYS A CE  1 
ATOM   616  N  NZ  . LYS A 1 77  ? 3.35600   -8.27700  -8.75000  1.000 19.57255  ? 77  LYS A NZ  1 
ATOM   617  N  N   . LYS A 1 78  ? -3.40200  -3.80700  -10.68400 1.000 14.38431  ? 78  LYS A N   1 
ATOM   618  C  CA  . LYS A 1 78  ? -4.62200  -3.63900  -11.49500 1.000 15.73995  ? 78  LYS A CA  1 
ATOM   619  C  C   . LYS A 1 78  ? -4.75400  -2.20400  -11.99700 1.000 16.09878  ? 78  LYS A C   1 
ATOM   620  O  O   . LYS A 1 78  ? -5.64600  -1.94300  -12.78900 1.000 17.20017  ? 78  LYS A O   1 
ATOM   621  C  CB  . LYS A 1 78  ? -5.89300  -4.01400  -10.73000 1.000 15.31047  ? 78  LYS A CB  1 
ATOM   622  C  CG  . LYS A 1 78  ? -6.00000  -5.45500  -10.27700 1.000 16.97867  ? 78  LYS A CG  1 
ATOM   623  C  CD  . LYS A 1 78  ? -5.84900  -6.43000  -11.34100 1.000 23.10143  ? 78  LYS A CD  1 
ATOM   624  C  CE  . LYS A 1 78  ? -6.89400  -6.31600  -12.40700 1.000 28.65141  ? 78  LYS A CE  1 
ATOM   625  N  NZ  . LYS A 1 78  ? -7.94400  -7.32500  -12.18500 1.000 37.70926  ? 78  LYS A NZ  1 
ATOM   626  N  N   . LYS A 1 79  ? -3.94800  -1.27400  -11.50900 1.000 13.96600  ? 79  LYS A N   1 
ATOM   627  C  CA  . LYS A 1 79  ? -3.93500  0.13300   -11.96400 1.000 15.26700  ? 79  LYS A CA  1 
ATOM   628  C  C   . LYS A 1 79  ? -5.33900  0.71200   -11.92300 1.000 16.21321  ? 79  LYS A C   1 
ATOM   629  O  O   . LYS A 1 79  ? -5.81600  1.33600   -12.90500 1.000 17.98377  ? 79  LYS A O   1 
ATOM   630  C  CB  . LYS A 1 79  ? -3.25800  0.23400   -13.33700 1.000 17.85316  ? 79  LYS A CB  1 
ATOM   631  C  CG  . LYS A 1 79  ? -1.83300  -0.29400  -13.36000 1.000 17.64653  ? 79  LYS A CG  1 
ATOM   632  C  CD  . LYS A 1 79  ? -1.16600  -0.01600  -14.69900 1.000 23.07195  ? 79  LYS A CD  1 
ATOM   633  C  CE  . LYS A 1 79  ? -1.79300  -0.74400  -15.86000 1.000 31.25935  ? 79  LYS A CE  1 
ATOM   634  N  NZ  . LYS A 1 79  ? -0.97200  -0.56000  -17.09000 1.000 35.50220  ? 79  LYS A NZ  1 
ATOM   635  N  N   . GLY A 1 80  ? -6.00600  0.55600   -10.78000 1.000 15.02523  ? 80  GLY A N   1 
ATOM   636  C  CA  . GLY A 1 80  ? -7.33300  1.13000   -10.54500 1.000 14.71251  ? 80  GLY A CA  1 
ATOM   637  C  C   . GLY A 1 80  ? -8.47200  0.20100   -10.92300 1.000 16.35954  ? 80  GLY A C   1 
ATOM   638  O  O   . GLY A 1 80  ? -9.56500  0.43600   -10.42400 1.000 18.15565  ? 80  GLY A O   1 
ATOM   639  N  N   . HIS A 1 81  ? -8.21000  -0.82200  -11.71300 1.000 15.53565  ? 81  HIS A N   1 
ATOM   640  C  CA  . HIS A 1 81  ? -9.26000  -1.77400  -12.17700 1.000 18.92885  ? 81  HIS A CA  1 
ATOM   641  C  C   . HIS A 1 81  ? -9.37700  -2.90400  -11.15900 1.000 13.74025  ? 81  HIS A C   1 
ATOM   642  O  O   . HIS A 1 81  ? -9.22000  -4.06200  -11.52600 1.000 17.44598  ? 81  HIS A O   1 
ATOM   643  C  CB  . HIS A 1 81  ? -8.91000  -2.35800  -13.54200 1.000 19.40960  ? 81  HIS A CB  1 
ATOM   644  C  CG  . HIS A 1 81  ? -8.94800  -1.32600  -14.60100 1.000 27.51853  ? 81  HIS A CG  1 
ATOM   645  N  ND1 . HIS A 1 81  ? -7.83400  -0.61000  -15.01100 1.000 31.74983  ? 81  HIS A ND1 1 
ATOM   646  C  CD2 . HIS A 1 81  ? -9.99600  -0.83600  -15.28900 1.000 33.21161  ? 81  HIS A CD2 1 
ATOM   647  C  CE1 . HIS A 1 81  ? -8.21500  0.27500   -15.92100 1.000 29.61703  ? 81  HIS A CE1 1 
ATOM   648  N  NE2 . HIS A 1 81  ? -9.53200  0.17300   -16.08500 1.000 44.13996  ? 81  HIS A NE2 1 
ATOM   649  N  N   . HIS A 1 82  ? -9.66700  -2.56400  -9.91000  1.000 13.48096  ? 82  HIS A N   1 
ATOM   650  C  CA  . HIS A 1 82  ? -9.42800  -3.48900  -8.77100  1.000 12.67673  ? 82  HIS A CA  1 
ATOM   651  C  C   . HIS A 1 82  ? -10.72900 -3.84400  -8.02400  1.000 15.68696  ? 82  HIS A C   1 
ATOM   652  O  O   . HIS A 1 82  ? -10.67900 -4.35700  -6.89500  1.000 14.29560  ? 82  HIS A O   1 
ATOM   653  C  CB  . HIS A 1 82  ? -8.39500  -2.89100  -7.82200  1.000 12.40250  ? 82  HIS A CB  1 
ATOM   654  C  CG  . HIS A 1 82  ? -8.73500  -1.49900  -7.38400  1.000 14.14598  ? 82  HIS A CG  1 
ATOM   655  N  ND1 . HIS A 1 82  ? -7.78500  -0.54000  -7.18900  1.000 13.41724  ? 82  HIS A ND1 1 
ATOM   656  C  CD2 . HIS A 1 82  ? -9.91800  -0.90400  -7.12500  1.000 12.93054  ? 82  HIS A CD2 1 
ATOM   657  C  CE1 . HIS A 1 82  ? -8.38200  0.56900   -6.81100  1.000 13.15155  ? 82  HIS A CE1 1 
ATOM   658  N  NE2 . HIS A 1 82  ? -9.71000  0.39100   -6.73500  1.000 14.37380  ? 82  HIS A NE2 1 
ATOM   659  N  N   A GLU A 1 83  ? -11.88300 -3.62400  -8.65400  0.520 14.56193  ? 83  GLU A N   1 
ATOM   660  N  N   B GLU A 1 83  ? -11.89700 -3.63600  -8.62100  0.480 14.57744  ? 83  GLU A N   1 
ATOM   661  C  CA  A GLU A 1 83  ? -13.19200 -3.94800  -8.02500  0.520 15.11460  ? 83  GLU A CA  1 
ATOM   662  C  CA  B GLU A 1 83  ? -13.14500 -3.90800  -7.86200  0.480 15.27451  ? 83  GLU A CA  1 
ATOM   663  C  C   A GLU A 1 83  ? -13.19800 -5.38100  -7.47400  0.520 13.60112  ? 83  GLU A C   1 
ATOM   664  C  C   B GLU A 1 83  ? -13.22000 -5.39400  -7.45500  0.480 13.57403  ? 83  GLU A C   1 
ATOM   665  O  O   A GLU A 1 83  ? -13.65000 -5.58400  -6.33600  0.520 14.29041  ? 83  GLU A O   1 
ATOM   666  O  O   B GLU A 1 83  ? -13.67300 -5.64700  -6.33200  0.480 14.36218  ? 83  GLU A O   1 
ATOM   667  C  CB  A GLU A 1 83  ? -14.36600 -3.76300  -8.98100  0.520 17.11509  ? 83  GLU A CB  1 
ATOM   668  C  CB  B GLU A 1 83  ? -14.37500 -3.34400  -8.56900  0.480 17.97010  ? 83  GLU A CB  1 
ATOM   669  C  CG  A GLU A 1 83  ? -15.66700 -3.80700  -8.22100  0.520 18.40743  ? 83  GLU A CG  1 
ATOM   670  C  CG  B GLU A 1 83  ? -14.49700 -1.82000  -8.45300  0.480 20.92136  ? 83  GLU A CG  1 
ATOM   671  C  CD  A GLU A 1 83  ? -16.91900 -3.48700  -9.00100  0.520 24.23299  ? 83  GLU A CD  1 
ATOM   672  C  CD  B GLU A 1 83  ? -14.07300 -1.05500  -7.18200  0.480 24.95236  ? 83  GLU A CD  1 
ATOM   673  O  OE1 A GLU A 1 83  ? -17.97400 -3.94400  -8.56100  0.520 20.10842  ? 83  GLU A OE1 1 
ATOM   674  O  OE1 B GLU A 1 83  ? -14.64200 -1.26600  -6.04700  0.480 22.66155  ? 83  GLU A OE1 1 
ATOM   675  O  OE2 A GLU A 1 83  ? -16.80900 -2.71100  -9.99000  0.520 26.91915  ? 83  GLU A OE2 1 
ATOM   676  O  OE2 B GLU A 1 83  ? -13.18100 -0.18700  -7.32200  0.480 16.71963  ? 83  GLU A OE2 1 
ATOM   677  N  N   . ALA A 1 84  ? -12.74300 -6.34800  -8.25300  1.000 12.98599  ? 84  ALA A N   1 
ATOM   678  C  CA  . ALA A 1 84  ? -12.85200 -7.76400  -7.84600  1.000 13.52377  ? 84  ALA A CA  1 
ATOM   679  C  C   . ALA A 1 84  ? -11.90700 -8.09800  -6.70600  1.000 14.27717  ? 84  ALA A C   1 
ATOM   680  O  O   . ALA A 1 84  ? -12.23300 -8.97000  -5.88300  1.000 16.37748  ? 84  ALA A O   1 
ATOM   681  C  CB  . ALA A 1 84  ? -12.64000 -8.66000  -9.03600  1.000 16.17374  ? 84  ALA A CB  1 
ATOM   682  N  N   . GLU A 1 85  ? -10.76600 -7.42700  -6.64200  1.000 15.76997  ? 85  GLU A N   1 
ATOM   683  C  CA  . GLU A 1 85  ? -9.82300  -7.65800  -5.52000  1.000 14.15024  ? 85  GLU A CA  1 
ATOM   684  C  C   . GLU A 1 85  ? -10.28800 -6.93300  -4.24300  1.000 13.73765  ? 85  GLU A C   1 
ATOM   685  O  O   . GLU A 1 85  ? -10.03000 -7.42200  -3.15800  1.000 16.48444  ? 85  GLU A O   1 
ATOM   686  C  CB  . GLU A 1 85  ? -8.42100  -7.19500  -5.92700  1.000 17.60076  ? 85  GLU A CB  1 
ATOM   687  C  CG  . GLU A 1 85  ? -7.79000  -8.01800  -7.03400  1.000 20.43492  ? 85  GLU A CG  1 
ATOM   688  C  CD  . GLU A 1 85  ? -8.37300  -7.85300  -8.42700  1.000 23.74117  ? 85  GLU A CD  1 
ATOM   689  O  OE1 . GLU A 1 85  ? -8.30800  -8.81800  -9.20400  1.000 28.96050  ? 85  GLU A OE1 1 
ATOM   690  O  OE2 . GLU A 1 85  ? -8.87700  -6.76600  -8.73600  1.000 18.28444  ? 85  GLU A OE2 1 
ATOM   691  N  N   . LEU A 1 86  ? -10.94100 -5.78300  -4.39000  1.000 14.30219  ? 86  LEU A N   1 
ATOM   692  C  CA  . LEU A 1 86  ? -11.39100 -5.00700  -3.20700  1.000 13.75384  ? 86  LEU A CA  1 
ATOM   693  C  C   . LEU A 1 86  ? -12.61900 -5.67800  -2.58200  1.000 14.48628  ? 86  LEU A C   1 
ATOM   694  O  O   . LEU A 1 86  ? -12.82900 -5.53100  -1.39400  1.000 16.91638  ? 86  LEU A O   1 
ATOM   695  C  CB  . LEU A 1 86  ? -11.74400 -3.57100  -3.61200  1.000 16.86641  ? 86  LEU A CB  1 
ATOM   696  C  CG  . LEU A 1 86  ? -10.61900 -2.54700  -3.52400  1.000 22.30771  ? 86  LEU A CG  1 
ATOM   697  C  CD1 . LEU A 1 86  ? -11.16800 -1.14800  -3.73800  1.000 20.58455  ? 86  LEU A CD1 1 
ATOM   698  C  CD2 . LEU A 1 86  ? -9.94000  -2.63500  -2.17400  1.000 25.07891  ? 86  LEU A CD2 1 
ATOM   699  N  N   . LYS A 1 87  ? -13.41500 -6.36400  -3.40900  1.000 11.89105  ? 87  LYS A N   1 
ATOM   700  C  CA  . LYS A 1 87  ? -14.69300 -6.93700  -2.89500  1.000 13.02339  ? 87  LYS A CA  1 
ATOM   701  C  C   . LYS A 1 87  ? -14.45000 -7.81100  -1.66200  1.000 11.95360  ? 87  LYS A C   1 
ATOM   702  O  O   . LYS A 1 87  ? -15.06400 -7.55000  -0.64400  1.000 13.95844  ? 87  LYS A O   1 
ATOM   703  C  CB  . LYS A 1 87  ? -15.41100 -7.71800  -4.00100  1.000 12.44607  ? 87  LYS A CB  1 
ATOM   704  C  CG  . LYS A 1 87  ? -16.78300 -8.26900  -3.64000  1.000 15.49688  ? 87  LYS A CG  1 
ATOM   705  C  CD  . LYS A 1 87  ? -17.38000 -9.09300  -4.76100  1.000 16.54017  ? 87  LYS A CD  1 
ATOM   706  C  CE  . LYS A 1 87  ? -18.66000 -9.80200  -4.37600  1.000 16.30451  ? 87  LYS A CE  1 
ATOM   707  N  NZ  . LYS A 1 87  ? -19.79000 -8.85300  -4.26400  1.000 21.32968  ? 87  LYS A NZ  1 
ATOM   708  N  N   . PRO A 1 88  ? -13.61400 -8.86000  -1.71400  1.000 12.17829  ? 88  PRO A N   1 
ATOM   709  C  CA  . PRO A 1 88  ? -13.45400 -9.68500  -0.52000  1.000 13.12581  ? 88  PRO A CA  1 
ATOM   710  C  C   . PRO A 1 88  ? -12.74100 -8.97100  0.63400   1.000 12.07072  ? 88  PRO A C   1 
ATOM   711  O  O   . PRO A 1 88  ? -12.93800 -9.30700  1.78800   1.000 12.42933  ? 88  PRO A O   1 
ATOM   712  C  CB  . PRO A 1 88  ? -12.63200 -10.88400 -0.99700  1.000 11.62688  ? 88  PRO A CB  1 
ATOM   713  C  CG  . PRO A 1 88  ? -11.92300 -10.36400 -2.21400  1.000 12.68304  ? 88  PRO A CG  1 
ATOM   714  C  CD  . PRO A 1 88  ? -12.88600 -9.40500  -2.86300  1.000 11.67756  ? 88  PRO A CD  1 
ATOM   715  N  N   . LEU A 1 89  ? -11.91200 -7.96600  0.31500   1.000 11.87350  ? 89  LEU A N   1 
ATOM   716  C  CA  . LEU A 1 89  ? -11.15500 -7.23500  1.36100   1.000 11.92683  ? 89  LEU A CA  1 
ATOM   717  C  C   . LEU A 1 89  ? -12.12700 -6.30700  2.09900   1.000 11.29545  ? 89  LEU A C   1 
ATOM   718  O  O   . LEU A 1 89  ? -12.08700 -6.25500  3.33100   1.000 12.20559  ? 89  LEU A O   1 
ATOM   719  C  CB  . LEU A 1 89  ? -10.02400 -6.43900  0.70200   1.000 14.21921  ? 89  LEU A CB  1 
ATOM   720  C  CG  . LEU A 1 89  ? -9.00600  -5.87200  1.65900   1.000 14.24364  ? 89  LEU A CG  1 
ATOM   721  C  CD1 . LEU A 1 89  ? -8.13600  -6.96700  2.28200   1.000 16.44819  ? 89  LEU A CD1 1 
ATOM   722  C  CD2 . LEU A 1 89  ? -8.15500  -4.84700  0.97500   1.000 15.47322  ? 89  LEU A CD2 1 
ATOM   723  N  N   . ALA A 1 90  ? -12.98000 -5.62800  1.36100   1.000 11.45154  ? 90  ALA A N   1 
ATOM   724  C  CA  . ALA A 1 90  ? -14.00800 -4.78800  2.02300   1.000 12.59255  ? 90  ALA A CA  1 
ATOM   725  C  C   . ALA A 1 90  ? -14.91400 -5.65700  2.90100   1.000 12.20784  ? 90  ALA A C   1 
ATOM   726  O  O   . ALA A 1 90  ? -15.30300 -5.22600  3.96600   1.000 12.81127  ? 90  ALA A O   1 
ATOM   727  C  CB  . ALA A 1 90  ? -14.80200 -4.05800  0.96500   1.000 13.84420  ? 90  ALA A CB  1 
ATOM   728  N  N   . GLN A 1 91  ? -15.31400 -6.82100  2.38300   1.000 13.02064  ? 91  GLN A N   1 
ATOM   729  C  CA  . GLN A 1 91  ? -16.22600 -7.71200  3.14200   1.000 15.32045  ? 91  GLN A CA  1 
ATOM   730  C  C   . GLN A 1 91  ? -15.63000 -8.00200  4.52600   1.000 12.77498  ? 91  GLN A C   1 
ATOM   731  O  O   . GLN A 1 91  ? -16.34000 -7.85000  5.51700   1.000 15.97738  ? 91  GLN A O   1 
ATOM   732  C  CB  . GLN A 1 91  ? -16.44200 -8.99600  2.34300   1.000 15.47203  ? 91  GLN A CB  1 
ATOM   733  C  CG  . GLN A 1 91  ? -17.53200 -9.89500  2.89600   1.000 28.90648  ? 91  GLN A CG  1 
ATOM   734  C  CD  . GLN A 1 91  ? -18.87800 -9.27500  2.62700   1.000 23.20464  ? 91  GLN A CD  1 
ATOM   735  O  OE1 . GLN A 1 91  ? -19.64200 -9.01300  3.54500   1.000 39.95314  ? 91  GLN A OE1 1 
ATOM   736  N  NE2 . GLN A 1 91  ? -19.15500 -8.99600  1.36300   1.000 32.11190  ? 91  GLN A NE2 1 
ATOM   737  N  N   . SER A 1 92  ? -14.41400 -8.55400  4.56000   1.000 12.41885  ? 92  SER A N   1 
ATOM   738  C  CA  . SER A 1 92  ? -13.78400 -8.91800  5.84900   1.000 13.16684  ? 92  SER A CA  1 
ATOM   739  C  C   . SER A 1 92  ? -13.47400 -7.68600  6.70200   1.000 11.05548  ? 92  SER A C   1 
ATOM   740  O  O   . SER A 1 92  ? -13.71800 -7.72500  7.89500   1.000 13.65259  ? 92  SER A O   1 
ATOM   741  C  CB  . SER A 1 92  ? -12.52800 -9.72600  5.60300   1.000 13.66405  ? 92  SER A CB  1 
ATOM   742  O  OG  . SER A 1 92  ? -11.55900 -8.96600  4.92800   1.000 12.86598  ? 92  SER A OG  1 
ATOM   743  N  N   . HIS A 1 93  ? -12.95400 -6.63800  6.07500   1.000 12.14247  ? 93  HIS A N   1 
ATOM   744  C  CA  . HIS A 1 93  ? -12.48700 -5.49000  6.89100   1.000 11.66793  ? 93  HIS A CA  1 
ATOM   745  C  C   . HIS A 1 93  ? -13.66200 -4.64100  7.42400   1.000 13.12291  ? 93  HIS A C   1 
ATOM   746  O  O   . HIS A 1 93  ? -13.51000 -4.03300  8.46200   1.000 14.04194  ? 93  HIS A O   1 
ATOM   747  C  CB  . HIS A 1 93  ? -11.39300 -4.74400  6.10300   1.000 11.46751  ? 93  HIS A CB  1 
ATOM   748  C  CG  . HIS A 1 93  ? -10.09300 -5.47300  6.10300   1.000 11.26635  ? 93  HIS A CG  1 
ATOM   749  N  ND1 . HIS A 1 93  ? -9.95000  -6.71200  5.52600   1.000 13.49355  ? 93  HIS A ND1 1 
ATOM   750  C  CD2 . HIS A 1 93  ? -8.89300  -5.15700  6.63000   1.000 12.54771  ? 93  HIS A CD2 1 
ATOM   751  C  CE1 . HIS A 1 93  ? -8.71600  -7.13000  5.69100   1.000 11.75766  ? 93  HIS A CE1 1 
ATOM   752  N  NE2 . HIS A 1 93  ? -8.04700  -6.19500  6.36500   1.000 11.86995  ? 93  HIS A NE2 1 
ATOM   753  N  N   . ALA A 1 94  ? -14.79100 -4.67400  6.73300   1.000 13.41466  ? 94  ALA A N   1 
ATOM   754  C  CA  . ALA A 1 94  ? -15.96600 -3.93600  7.23700   1.000 14.06801  ? 94  ALA A CA  1 
ATOM   755  C  C   . ALA A 1 94  ? -16.76100 -4.76300  8.24600   1.000 15.93879  ? 94  ALA A C   1 
ATOM   756  O  O   . ALA A 1 94  ? -17.09500 -4.21600  9.26900   1.000 24.26943  ? 94  ALA A O   1 
ATOM   757  C  CB  . ALA A 1 94  ? -16.85600 -3.58400  6.07800   1.000 12.89426  ? 94  ALA A CB  1 
ATOM   758  N  N   . THR A 1 95  ? -17.01200 -6.03300  7.94300   1.000 15.19629  ? 95  THR A N   1 
ATOM   759  C  CA  . THR A 1 95  ? -17.94800 -6.85700  8.75200   1.000 17.85353  ? 95  THR A CA  1 
ATOM   760  C  C   . THR A 1 95  ? -17.26900 -7.66500  9.86100   1.000 21.53850  ? 95  THR A C   1 
ATOM   761  O  O   . THR A 1 95  ? -17.92400 -7.87100  10.87800  1.000 23.71014  ? 95  THR A O   1 
ATOM   762  C  CB  . THR A 1 95  ? -18.76600 -7.78500  7.83300   1.000 18.19050  ? 95  THR A CB  1 
ATOM   763  O  OG1 . THR A 1 95  ? -17.96100 -8.85600  7.35200   1.000 23.86443  ? 95  THR A OG1 1 
ATOM   764  C  CG2 . THR A 1 95  ? -19.39300 -7.04100  6.67300   1.000 26.23744  ? 95  THR A CG2 1 
ATOM   765  N  N   . LYS A 1 96  ? -16.03600 -8.10700  9.66800   1.000 15.60139  ? 96  LYS A N   1 
ATOM   766  C  CA  . LYS A 1 96  ? -15.37600 -8.97700  10.67500  1.000 18.13656  ? 96  LYS A CA  1 
ATOM   767  C  C   . LYS A 1 96  ? -14.32700 -8.19300  11.46800  1.000 17.92833  ? 96  LYS A C   1 
ATOM   768  O  O   . LYS A 1 96  ? -14.46000 -8.11000  12.67000  1.000 21.93672  ? 96  LYS A O   1 
ATOM   769  C  CB  . LYS A 1 96  ? -14.75600 -10.17400 9.96200   1.000 17.66925  ? 96  LYS A CB  1 
ATOM   770  C  CG  . LYS A 1 96  ? -14.00900 -11.20100 10.79900  1.000 19.81710  ? 96  LYS A CG  1 
ATOM   771  C  CD  . LYS A 1 96  ? -13.78600 -12.42900 9.94500   1.000 27.56550  ? 96  LYS A CD  1 
ATOM   772  C  CE  . LYS A 1 96  ? -12.76600 -13.42400 10.44700  1.000 39.47859  ? 96  LYS A CE  1 
ATOM   773  N  NZ  . LYS A 1 96  ? -12.39000 -14.36100 9.36000   1.000 31.03027  ? 96  LYS A NZ  1 
ATOM   774  N  N   . HIS A 1 97  ? -13.33400 -7.63400  10.78400  1.000 17.15625  ? 97  HIS A N   1 
ATOM   775  C  CA  . HIS A 1 97  ? -12.22500 -6.96000  11.49800  1.000 15.13665  ? 97  HIS A CA  1 
ATOM   776  C  C   . HIS A 1 97  ? -12.62200 -5.55400  11.96900  1.000 15.95091  ? 97  HIS A C   1 
ATOM   777  O  O   . HIS A 1 97  ? -12.05000 -5.10400  12.94300  1.000 18.50481  ? 97  HIS A O   1 
ATOM   778  C  CB  . HIS A 1 97  ? -10.97700 -6.91800  10.60400  1.000 14.93354  ? 97  HIS A CB  1 
ATOM   779  C  CG  . HIS A 1 97  ? -10.66900 -8.18700  9.88400   1.000 14.99226  ? 97  HIS A CG  1 
ATOM   780  N  ND1 . HIS A 1 97  ? -10.71000 -9.42200  10.49800  1.000 16.51388  ? 97  HIS A ND1 1 
ATOM   781  C  CD2 . HIS A 1 97  ? -10.29200 -8.41300  8.60900   1.000 14.53643  ? 97  HIS A CD2 1 
ATOM   782  C  CE1 . HIS A 1 97  ? -10.38000 -10.35100 9.62700   1.000 15.30324  ? 97  HIS A CE1 1 
ATOM   783  N  NE2 . HIS A 1 97  ? -10.11700 -9.75900  8.46200   1.000 15.00364  ? 97  HIS A NE2 1 
ATOM   784  N  N   . LYS A 1 98  ? -13.52400 -4.90000  11.24300  1.000 16.60403  ? 98  LYS A N   1 
ATOM   785  C  CA  . LYS A 1 98  ? -14.01200 -3.54100  11.60400  1.000 16.20881  ? 98  LYS A CA  1 
ATOM   786  C  C   . LYS A 1 98  ? -12.84200 -2.55000  11.59800  1.000 16.09941  ? 98  LYS A C   1 
ATOM   787  O  O   . LYS A 1 98  ? -12.53100 -1.97300  12.62600  1.000 17.15871  ? 98  LYS A O   1 
ATOM   788  C  CB  . LYS A 1 98  ? -14.79600 -3.57300  12.91600  1.000 20.96855  ? 98  LYS A CB  1 
ATOM   789  C  CG  . LYS A 1 98  ? -16.02700 -4.46500  12.85300  1.000 21.18202  ? 98  LYS A CG  1 
ATOM   790  C  CD  . LYS A 1 98  ? -16.75000 -4.61000  14.16600  1.000 31.61903  ? 98  LYS A CD  1 
ATOM   791  C  CE  . LYS A 1 98  ? -16.65400 -6.01100  14.72700  1.000 44.94377  ? 98  LYS A CE  1 
ATOM   792  N  NZ  . LYS A 1 98  ? -17.30500 -7.00000  13.83800  1.000 47.48029  ? 98  LYS A NZ  1 
ATOM   793  N  N   . ILE A 1 99  ? -12.25900 -2.37100  10.41900  1.000 13.36001  ? 99  ILE A N   1 
ATOM   794  C  CA  . ILE A 1 99  ? -11.10700 -1.44100  10.29600  1.000 11.88404  ? 99  ILE A CA  1 
ATOM   795  C  C   . ILE A 1 99  ? -11.58500 -0.12900  9.68200   1.000 12.80402  ? 99  ILE A C   1 
ATOM   796  O  O   . ILE A 1 99  ? -11.94200 -0.09200  8.52000   1.000 14.93100  ? 99  ILE A O   1 
ATOM   797  C  CB  . ILE A 1 99  ? -10.00200 -2.09000  9.44800   1.000 12.31004  ? 99  ILE A CB  1 
ATOM   798  C  CG1 . ILE A 1 99  ? -9.63500  -3.48600  9.95900   1.000 13.00815  ? 99  ILE A CG1 1 
ATOM   799  C  CG2 . ILE A 1 99  ? -8.78800  -1.17500  9.36600   1.000 11.55074  ? 99  ILE A CG2 1 
ATOM   800  C  CD1 . ILE A 1 99  ? -9.27200  -3.53000  11.42100  1.000 15.66748  ? 99  ILE A CD1 1 
ATOM   801  N  N   . PRO A 1 100 ? -11.57500 0.95900   10.46700  1.000 12.79524  ? 100 PRO A N   1 
ATOM   802  C  CA  . PRO A 1 100 ? -12.02100 2.23300   9.96000   1.000 14.18586  ? 100 PRO A CA  1 
ATOM   803  C  C   . PRO A 1 100 ? -11.07300 2.80200   8.89200   1.000 13.16261  ? 100 PRO A C   1 
ATOM   804  O  O   . PRO A 1 100 ? -9.92400  2.46200   8.88700   1.000 12.94843  ? 100 PRO A O   1 
ATOM   805  C  CB  . PRO A 1 100 ? -12.02400 3.10900   11.22000  1.000 18.30703  ? 100 PRO A CB  1 
ATOM   806  C  CG  . PRO A 1 100 ? -11.01000 2.47500   12.13000  1.000 19.28496  ? 100 PRO A CG  1 
ATOM   807  C  CD  . PRO A 1 100 ? -11.14300 0.99300   11.86100  1.000 17.48204  ? 100 PRO A CD  1 
ATOM   808  N  N   . ILE A 1 101 ? -11.60700 3.64600   8.03300   1.000 13.23084  ? 101 ILE A N   1 
ATOM   809  C  CA  . ILE A 1 101 ? -10.79100 4.28200   6.97700   1.000 12.23177  ? 101 ILE A CA  1 
ATOM   810  C  C   . ILE A 1 101 ? -9.61200  4.98400   7.65300   1.000 12.98711  ? 101 ILE A C   1 
ATOM   811  O  O   . ILE A 1 101 ? -8.51600  5.01700   7.06100   1.000 12.45511  ? 101 ILE A O   1 
ATOM   812  C  CB  . ILE A 1 101 ? -11.62500 5.21500   6.07800   1.000 13.38183  ? 101 ILE A CB  1 
ATOM   813  C  CG1 . ILE A 1 101 ? -12.71400 4.40200   5.35900   1.000 12.46051  ? 101 ILE A CG1 1 
ATOM   814  C  CG2 . ILE A 1 101 ? -10.73700 5.93400   5.08800   1.000 15.79446  ? 101 ILE A CG2 1 
ATOM   815  C  CD1 . ILE A 1 101 ? -12.14000 3.30900   4.42500   1.000 15.65220  ? 101 ILE A CD1 1 
ATOM   816  N  N   . LYS A 1 102 ? -9.79400  5.61000   8.81500   1.000 13.52796  ? 102 LYS A N   1 
ATOM   817  C  CA  . LYS A 1 102 ? -8.66000  6.33800   9.43700   1.000 13.29308  ? 102 LYS A CA  1 
ATOM   818  C  C   . LYS A 1 102 ? -7.49700  5.37600   9.74300   1.000 11.59856  ? 102 LYS A C   1 
ATOM   819  O  O   . LYS A 1 102 ? -6.31200  5.80500   9.62700   1.000 13.68639  ? 102 LYS A O   1 
ATOM   820  C  CB  . LYS A 1 102 ? -9.12300  7.06500   10.69900  1.000 16.74572  ? 102 LYS A CB  1 
ATOM   821  C  CG  . LYS A 1 102 ? -9.49900  6.21900   11.87000  1.000 21.13942  ? 102 LYS A CG  1 
ATOM   822  C  CD  . LYS A 1 102 ? -9.74200  7.11500   13.11900  1.000 34.48728  ? 102 LYS A CD  1 
ATOM   823  C  CE  . LYS A 1 102 ? -10.44300 6.38600   14.24400  1.000 36.91874  ? 102 LYS A CE  1 
ATOM   824  N  NZ  . LYS A 1 102 ? -11.47500 7.23800   14.90000  1.000 46.86083  ? 102 LYS A NZ  1 
ATOM   825  N  N   . TYR A 1 103 ? -7.75400  4.07200   9.95500   1.000 12.59128  ? 103 TYR A N   1 
ATOM   826  C  CA  . TYR A 1 103 ? -6.63100  3.12300   10.16600  1.000 12.82294  ? 103 TYR A CA  1 
ATOM   827  C  C   . TYR A 1 103 ? -5.99800  2.76700   8.80700   1.000 12.85168  ? 103 TYR A C   1 
ATOM   828  O  O   . TYR A 1 103 ? -4.78900  2.50400   8.72900   1.000 11.34478  ? 103 TYR A O   1 
ATOM   829  C  CB  . TYR A 1 103 ? -7.10500  1.86100   10.88800  1.000 14.42813  ? 103 TYR A CB  1 
ATOM   830  C  CG  . TYR A 1 103 ? -7.34200  2.01800   12.36900  1.000 14.11345  ? 103 TYR A CG  1 
ATOM   831  C  CD1 . TYR A 1 103 ? -7.30900  3.26600   12.98500  1.000 16.51527  ? 103 TYR A CD1 1 
ATOM   832  C  CD2 . TYR A 1 103 ? -7.64700  0.90800   13.13100  1.000 16.57528  ? 103 TYR A CD2 1 
ATOM   833  C  CE1 . TYR A 1 103 ? -7.59000  3.39500   14.33800  1.000 17.20941  ? 103 TYR A CE1 1 
ATOM   834  C  CE2 . TYR A 1 103 ? -7.94100  1.02200   14.47800  1.000 17.19972  ? 103 TYR A CE2 1 
ATOM   835  C  CZ  . TYR A 1 103 ? -7.89200  2.26900   15.06800  1.000 19.56847  ? 103 TYR A CZ  1 
ATOM   836  O  OH  . TYR A 1 103 ? -8.15500  2.42000   16.41400  1.000 25.10219  ? 103 TYR A OH  1 
ATOM   837  N  N   . LEU A 1 104 ? -6.77300  2.75700   7.72700   1.000 11.65191  ? 104 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 104 ? -6.19600  2.56900   6.37400   1.000 11.31475  ? 104 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 104 ? -5.36300  3.78900   6.02100   1.000 11.85561  ? 104 LEU A C   1 
ATOM   840  O  O   . LEU A 1 104 ? -4.34500  3.62500   5.34600   1.000 11.29523  ? 104 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 104 ? -7.31300  2.30700   5.37300   1.000 10.65395  ? 104 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 104 ? -8.15400  1.07600   5.64600   1.000 10.68272  ? 104 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 104 ? -9.09500  0.90700   4.47600   1.000 14.19713  ? 104 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 104 ? -7.28000  -0.16400  5.81600   1.000 13.95933  ? 104 LEU A CD2 1 
ATOM   845  N  N   . GLU A 1 105 ? -5.75500  5.00800   6.43400   1.000 11.30507  ? 105 GLU A N   1 
ATOM   846  C  CA  . GLU A 1 105 ? -4.87100  6.17900   6.26300   1.000 12.14713  ? 105 GLU A CA  1 
ATOM   847  C  C   . GLU A 1 105 ? -3.55800  5.95800   7.02500   1.000 12.68533  ? 105 GLU A C   1 
ATOM   848  O  O   . GLU A 1 105 ? -2.48600  6.21300   6.45200   1.000 11.38906  ? 105 GLU A O   1 
ATOM   849  C  CB  . GLU A 1 105 ? -5.58700  7.44700   6.76300   1.000 13.22528  ? 105 GLU A CB  1 
ATOM   850  C  CG  . GLU A 1 105 ? -6.71700  7.87200   5.85800   1.000 12.22402  ? 105 GLU A CG  1 
ATOM   851  C  CD  . GLU A 1 105 ? -7.53300  9.06500   6.35700   1.000 15.90342  ? 105 GLU A CD  1 
ATOM   852  O  OE1 . GLU A 1 105 ? -8.03200  9.75800   5.44500   1.000 18.15199  ? 105 GLU A OE1 1 
ATOM   853  O  OE2 . GLU A 1 105 ? -7.72400  9.23200   7.57300   1.000 15.98188  ? 105 GLU A OE2 1 
ATOM   854  N  N   . PHE A 1 106 ? -3.62800  5.51200   8.27300   1.000 12.49283  ? 106 PHE A N   1 
ATOM   855  C  CA  . PHE A 1 106 ? -2.41600  5.22800   9.08500   1.000 9.98512   ? 106 PHE A CA  1 
ATOM   856  C  C   . PHE A 1 106 ? -1.52200  4.21500   8.35400   1.000 12.17795  ? 106 PHE A C   1 
ATOM   857  O  O   . PHE A 1 106 ? -0.34100  4.45300   8.29200   1.000 12.41389  ? 106 PHE A O   1 
ATOM   858  C  CB  . PHE A 1 106 ? -2.78800  4.76600   10.48900  1.000 12.86775  ? 106 PHE A CB  1 
ATOM   859  C  CG  . PHE A 1 106 ? -3.52500  5.74500   11.38100  1.000 11.55997  ? 106 PHE A CG  1 
ATOM   860  C  CD1 . PHE A 1 106 ? -3.49300  7.10700   11.16200  1.000 14.72409  ? 106 PHE A CD1 1 
ATOM   861  C  CD2 . PHE A 1 106 ? -4.20400  5.25300   12.47500  1.000 15.70487  ? 106 PHE A CD2 1 
ATOM   862  C  CE1 . PHE A 1 106 ? -4.16200  7.95900   12.04100  1.000 15.15732  ? 106 PHE A CE1 1 
ATOM   863  C  CE2 . PHE A 1 106 ? -4.88700  6.10200   13.34400  1.000 18.60108  ? 106 PHE A CE2 1 
ATOM   864  C  CZ  . PHE A 1 106 ? -4.82700  7.45500   13.12400  1.000 16.37519  ? 106 PHE A CZ  1 
ATOM   865  N  N   . ILE A 1 107 ? -2.06800  3.13700   7.81300   1.000 11.23473  ? 107 ILE A N   1 
ATOM   866  C  CA  . ILE A 1 107 ? -1.14900  2.12400   7.23000   1.000 9.47233   ? 107 ILE A CA  1 
ATOM   867  C  C   . ILE A 1 107 ? -0.61300  2.66800   5.92000   1.000 11.43240  ? 107 ILE A C   1 
ATOM   868  O  O   . ILE A 1 107 ? 0.52300   2.39500   5.59800   1.000 12.03260  ? 107 ILE A O   1 
ATOM   869  C  CB  . ILE A 1 107 ? -1.77800  0.73500   7.07500   1.000 9.52248   ? 107 ILE A CB  1 
ATOM   870  C  CG1 . ILE A 1 107 ? -0.68400  -0.32900  6.97800   1.000 10.19303  ? 107 ILE A CG1 1 
ATOM   871  C  CG2 . ILE A 1 107 ? -2.73100  0.66900   5.91000   1.000 12.55258  ? 107 ILE A CG2 1 
ATOM   872  C  CD1 . ILE A 1 107 ? -1.18300  -1.75300  7.02400   1.000 11.69303  ? 107 ILE A CD1 1 
ATOM   873  N  N   . SER A 1 108 ? -1.38200  3.45800   5.18600   1.000 11.15791  ? 108 SER A N   1 
ATOM   874  C  CA  . SER A 1 108 ? -0.90800  4.12500   3.96100   1.000 9.00205   ? 108 SER A CA  1 
ATOM   875  C  C   . SER A 1 108 ? 0.28800   5.03600   4.29200   1.000 10.85301  ? 108 SER A C   1 
ATOM   876  O  O   . SER A 1 108 ? 1.30000   5.01700   3.55400   1.000 12.61754  ? 108 SER A O   1 
ATOM   877  C  CB  . SER A 1 108 ? -2.02000  4.93500   3.31700   1.000 9.56037   ? 108 SER A CB  1 
ATOM   878  O  OG  . SER A 1 108 ? -3.07500  4.09700   2.88400   1.000 11.12348  ? 108 SER A OG  1 
ATOM   879  N  N   . GLU A 1 109 ? 0.19700   5.79800   5.39600   1.000 12.68640  ? 109 GLU A N   1 
ATOM   880  C  CA  . GLU A 1 109 ? 1.30700   6.65000   5.85900   1.000 12.74536  ? 109 GLU A CA  1 
ATOM   881  C  C   . GLU A 1 109 ? 2.55400   5.80200   6.13800   1.000 11.86967  ? 109 GLU A C   1 
ATOM   882  O  O   . GLU A 1 109 ? 3.67600   6.23000   5.77400   1.000 12.31638  ? 109 GLU A O   1 
ATOM   883  C  CB  . GLU A 1 109 ? 0.81100   7.47500   7.03800   1.000 11.88750  ? 109 GLU A CB  1 
ATOM   884  C  CG  . GLU A 1 109 ? -0.23100  8.49400   6.61600   1.000 14.79575  ? 109 GLU A CG  1 
ATOM   885  C  CD  . GLU A 1 109 ? -1.18800  9.04100   7.66900   1.000 22.87874  ? 109 GLU A CD  1 
ATOM   886  O  OE1 . GLU A 1 109 ? -0.94600  8.83800   8.86100   1.000 21.61209  ? 109 GLU A OE1 1 
ATOM   887  O  OE2 . GLU A 1 109 ? -2.16400  9.73600   7.24900   1.000 26.08426  ? 109 GLU A OE2 1 
ATOM   888  N  N   . ALA A 1 110 ? 2.36600   4.65300   6.75600   1.000 11.72224  ? 110 ALA A N   1 
ATOM   889  C  CA  . ALA A 1 110 ? 3.48600   3.76300   7.16100   1.000 9.01592   ? 110 ALA A CA  1 
ATOM   890  C  C   . ALA A 1 110 ? 4.13400   3.20500   5.89500   1.000 12.04359  ? 110 ALA A C   1 
ATOM   891  O  O   . ALA A 1 110 ? 5.37700   3.13000   5.81200   1.000 12.13938  ? 110 ALA A O   1 
ATOM   892  C  CB  . ALA A 1 110 ? 3.01500   2.67900   8.04600   1.000 11.12832  ? 110 ALA A CB  1 
ATOM   893  N  N   . ILE A 1 111 ? 3.32500   2.81600   4.89200   1.000 10.99499  ? 111 ILE A N   1 
ATOM   894  C  CA  . ILE A 1 111 ? 3.88200   2.29000   3.62000   1.000 10.37815  ? 111 ILE A CA  1 
ATOM   895  C  C   . ILE A 1 111 ? 4.73200   3.39200   2.98800   1.000 12.53228  ? 111 ILE A C   1 
ATOM   896  O  O   . ILE A 1 111 ? 5.87200   3.13900   2.57200   1.000 13.16378  ? 111 ILE A O   1 
ATOM   897  C  CB  . ILE A 1 111 ? 2.71000   1.86900   2.70400   1.000 12.75076  ? 111 ILE A CB  1 
ATOM   898  C  CG1 . ILE A 1 111 ? 2.00400   0.64500   3.26600   1.000 10.21026  ? 111 ILE A CG1 1 
ATOM   899  C  CG2 . ILE A 1 111 ? 3.21700   1.67800   1.26300   1.000 15.07082  ? 111 ILE A CG2 1 
ATOM   900  C  CD1 . ILE A 1 111 ? 0.62300   0.40000   2.65600   1.000 10.90939  ? 111 ILE A CD1 1 
ATOM   901  N  N   A ILE A 1 112 ? 4.21200   4.60700   2.90500   0.660 12.80078  ? 112 ILE A N   1 
ATOM   902  N  N   B ILE A 1 112 ? 4.16800   4.59100   2.86400   0.340 12.74801  ? 112 ILE A N   1 
ATOM   903  C  CA  A ILE A 1 112 ? 4.94700   5.70600   2.23000   0.660 11.54118  ? 112 ILE A CA  1 
ATOM   904  C  CA  B ILE A 1 112 ? 4.87000   5.78800   2.32200   0.340 11.55420  ? 112 ILE A CA  1 
ATOM   905  C  C   A ILE A 1 112 ? 6.22700   5.99400   3.03700   0.660 13.92833  ? 112 ILE A C   1 
ATOM   906  C  C   B ILE A 1 112 ? 6.20900   5.94900   3.04100   0.340 13.87655  ? 112 ILE A C   1 
ATOM   907  O  O   A ILE A 1 112 ? 7.29700   6.27000   2.38100   0.660 13.03177  ? 112 ILE A O   1 
ATOM   908  O  O   B ILE A 1 112 ? 7.25400   6.13700   2.35000   0.340 13.08491  ? 112 ILE A O   1 
ATOM   909  C  CB  A ILE A 1 112 ? 4.01000   6.90500   1.97900   0.660 11.55350  ? 112 ILE A CB  1 
ATOM   910  C  CB  B ILE A 1 112 ? 3.99300   7.03800   2.49600   0.340 10.32480  ? 112 ILE A CB  1 
ATOM   911  C  CG1 A ILE A 1 112 ? 2.94100   6.51900   0.95800   0.660 10.09977  ? 112 ILE A CG1 1 
ATOM   912  C  CG1 B ILE A 1 112 ? 2.82100   7.01100   1.51500   0.340 16.70192  ? 112 ILE A CG1 1 
ATOM   913  C  CG2 A ILE A 1 112 ? 4.74500   8.14900   1.54600   0.660 11.46992  ? 112 ILE A CG2 1 
ATOM   914  C  CG2 B ILE A 1 112 ? 4.80500   8.31600   2.38100   0.340 11.88117  ? 112 ILE A CG2 1 
ATOM   915  C  CD1 A ILE A 1 112 ? 1.77200   7.51400   0.87100   0.660 12.18058  ? 112 ILE A CD1 1 
ATOM   916  C  CD1 B ILE A 1 112 ? 3.21000   6.97800   0.06000   0.340 14.26317  ? 112 ILE A CD1 1 
ATOM   917  N  N   . HIS A 1 113 ? 6.17500   5.93600   4.31700   1.000 11.31591  ? 113 HIS A N   1 
ATOM   918  C  CA  . HIS A 1 113 ? 7.37300   6.20500   5.15300   1.000 13.92939  ? 113 HIS A CA  1 
ATOM   919  C  C   . HIS A 1 113 ? 8.47400   5.17800   4.86600   1.000 12.18909  ? 113 HIS A C   1 
ATOM   920  O  O   . HIS A 1 113 ? 9.62300   5.57500   4.70400   1.000 13.20769  ? 113 HIS A O   1 
ATOM   921  C  CB  . HIS A 1 113 ? 6.98900   6.20800   6.63700   1.000 14.98199  ? 113 HIS A CB  1 
ATOM   922  C  CG  . HIS A 1 113 ? 8.17400   6.23300   7.54100   1.000 19.17995  ? 113 HIS A CG  1 
ATOM   923  N  ND1 . HIS A 1 113 ? 8.82400   7.40000   7.86400   1.000 28.52017  ? 113 HIS A ND1 1 
ATOM   924  C  CD2 . HIS A 1 113 ? 8.83300   5.24300   8.17500   1.000 19.87091  ? 113 HIS A CD2 1 
ATOM   925  C  CE1 . HIS A 1 113 ? 9.83500   7.12800   8.65800   1.000 25.96186  ? 113 HIS A CE1 1 
ATOM   926  N  NE2 . HIS A 1 113 ? 9.86000   5.81600   8.86800   1.000 24.56323  ? 113 HIS A NE2 1 
ATOM   927  N  N   . VAL A 1 114 ? 8.10000   3.90900   4.82800   1.000 11.37637  ? 114 VAL A N   1 
ATOM   928  C  CA  . VAL A 1 114 ? 9.12400   2.85000   4.63700   1.000 10.91188  ? 114 VAL A CA  1 
ATOM   929  C  C   . VAL A 1 114 ? 9.68700   2.92500   3.21400   1.000 12.65573  ? 114 VAL A C   1 
ATOM   930  O  O   . VAL A 1 114 ? 10.86500  2.73700   3.04800   1.000 11.63182  ? 114 VAL A O   1 
ATOM   931  C  CB  . VAL A 1 114 ? 8.52200   1.47200   4.94300   1.000 10.51476  ? 114 VAL A CB  1 
ATOM   932  C  CG1 . VAL A 1 114 ? 9.42200   0.33400   4.48100   1.000 10.94724  ? 114 VAL A CG1 1 
ATOM   933  C  CG2 . VAL A 1 114 ? 8.20900   1.33400   6.42500   1.000 12.16183  ? 114 VAL A CG2 1 
ATOM   934  N  N   . LEU A 1 115 ? 8.82400   3.20700   2.24100   1.000 11.93633  ? 115 LEU A N   1 
ATOM   935  C  CA  . LEU A 1 115 ? 9.31100   3.26300   0.84700   1.000 13.32169  ? 115 LEU A CA  1 
ATOM   936  C  C   . LEU A 1 115 ? 10.29700  4.43000   0.70500   1.000 12.76806  ? 115 LEU A C   1 
ATOM   937  O  O   . LEU A 1 115 ? 11.28800  4.28400   0.01800   1.000 14.90468  ? 115 LEU A O   1 
ATOM   938  C  CB  . LEU A 1 115 ? 8.14500   3.42000   -0.13300  1.000 12.25108  ? 115 LEU A CB  1 
ATOM   939  C  CG  . LEU A 1 115 ? 7.25200   2.19800   -0.31600  1.000 17.65161  ? 115 LEU A CG  1 
ATOM   940  C  CD1 . LEU A 1 115 ? 6.16500   2.48400   -1.33400  1.000 18.57870  ? 115 LEU A CD1 1 
ATOM   941  C  CD2 . LEU A 1 115 ? 8.06700   0.99700   -0.74300  1.000 20.22724  ? 115 LEU A CD2 1 
ATOM   942  N  N   . HIS A 1 116 ? 9.97100   5.54700   1.33400   1.000 12.24956  ? 116 HIS A N   1 
ATOM   943  C  CA  . HIS A 1 116 ? 10.90000  6.69700   1.29300   1.000 13.04098  ? 116 HIS A CA  1 
ATOM   944  C  C   . HIS A 1 116 ? 12.20900  6.37900   2.03800   1.000 15.18188  ? 116 HIS A C   1 
ATOM   945  O  O   . HIS A 1 116 ? 13.25500  6.82100   1.56500   1.000 17.86543  ? 116 HIS A O   1 
ATOM   946  C  CB  . HIS A 1 116 ? 10.23400  7.95400   1.85000   1.000 14.68373  ? 116 HIS A CB  1 
ATOM   947  C  CG  . HIS A 1 116 ? 11.14200  9.12800   1.74500   1.000 22.08298  ? 116 HIS A CG  1 
ATOM   948  N  ND1 . HIS A 1 116 ? 11.36800  9.76800   0.55100   1.000 34.98383  ? 116 HIS A ND1 1 
ATOM   949  C  CD2 . HIS A 1 116 ? 11.92900  9.73200   2.65800   1.000 35.35090  ? 116 HIS A CD2 1 
ATOM   950  C  CE1 . HIS A 1 116 ? 12.22700  10.74600  0.73600   1.000 35.41385  ? 116 HIS A CE1 1 
ATOM   951  N  NE2 . HIS A 1 116 ? 12.58500  10.74500  2.01900   1.000 34.43364  ? 116 HIS A NE2 1 
ATOM   952  N  N   A SER A 1 117 ? 12.11300  5.71800   3.18400   0.530 12.21620  ? 117 SER A N   1 
ATOM   953  N  N   B SER A 1 117 ? 12.10600  5.72200   3.16200   0.470 12.21035  ? 117 SER A N   1 
ATOM   954  C  CA  A SER A 1 117 ? 13.31800  5.38600   3.98900   0.530 12.66275  ? 117 SER A CA  1 
ATOM   955  C  CA  B SER A 1 117 ? 13.31700  5.40500   3.96600   0.470 12.67763  ? 117 SER A CA  1 
ATOM   956  C  C   A SER A 1 117 ? 14.24000  4.42300   3.23100   0.530 15.37153  ? 117 SER A C   1 
ATOM   957  C  C   B SER A 1 117 ? 14.24100  4.42300   3.23700   0.470 15.37325  ? 117 SER A C   1 
ATOM   958  O  O   A SER A 1 117 ? 15.45500  4.62100   3.26500   0.530 14.99841  ? 117 SER A O   1 
ATOM   959  O  O   B SER A 1 117 ? 15.45500  4.62400   3.26400   0.470 14.98449  ? 117 SER A O   1 
ATOM   960  C  CB  A SER A 1 117 ? 12.91600  4.79400   5.30400   0.530 16.50967  ? 117 SER A CB  1 
ATOM   961  C  CB  B SER A 1 117 ? 12.90900  4.84800   5.29600   0.470 16.51391  ? 117 SER A CB  1 
ATOM   962  O  OG  A SER A 1 117 ? 12.09600  5.68900   6.03600   0.530 17.98081  ? 117 SER A OG  1 
ATOM   963  O  OG  B SER A 1 117 ? 14.05200  4.52500   6.07100   0.470 19.94689  ? 117 SER A OG  1 
ATOM   964  N  N   . ARG A 1 118 ? 13.67000  3.42000   2.57000   1.000 13.68050  ? 118 ARG A N   1 
ATOM   965  C  CA  . ARG A 1 118 ? 14.50300  2.38400   1.90600   1.000 12.97139  ? 118 ARG A CA  1 
ATOM   966  C  C   . ARG A 1 118 ? 14.86500  2.66800   0.44900   1.000 14.07497  ? 118 ARG A C   1 
ATOM   967  O  O   . ARG A 1 118 ? 15.92500  2.23600   0.02400   1.000 15.63677  ? 118 ARG A O   1 
ATOM   968  C  CB  . ARG A 1 118 ? 13.71300  1.07300   1.95600   1.000 12.30771  ? 118 ARG A CB  1 
ATOM   969  C  CG  . ARG A 1 118 ? 13.52300  0.49500   3.34800   1.000 12.59767  ? 118 ARG A CG  1 
ATOM   970  C  CD  . ARG A 1 118 ? 13.05700  -0.92900  3.14400   1.000 16.63696  ? 118 ARG A CD  1 
ATOM   971  N  NE  . ARG A 1 118 ? 12.96300  -1.70700  4.36200   1.000 16.91037  ? 118 ARG A NE  1 
ATOM   972  C  CZ  . ARG A 1 118 ? 13.27100  -2.99300  4.44800   1.000 15.46401  ? 118 ARG A CZ  1 
ATOM   973  N  NH1 . ARG A 1 118 ? 13.15700  -3.62100  5.60200   1.000 17.82533  ? 118 ARG A NH1 1 
ATOM   974  N  NH2 . ARG A 1 118 ? 13.72600  -3.63900  3.39000   1.000 18.97387  ? 118 ARG A NH2 1 
ATOM   975  N  N   . HIS A 1 119 ? 14.00500  3.36300   -0.28900  1.000 12.40757  ? 119 HIS A N   1 
ATOM   976  C  CA  . HIS A 1 119 ? 14.21000  3.51400   -1.75100  1.000 10.62620  ? 119 HIS A CA  1 
ATOM   977  C  C   . HIS A 1 119 ? 14.10400  4.96700   -2.20800  1.000 12.77790  ? 119 HIS A C   1 
ATOM   978  O  O   . HIS A 1 119 ? 13.36800  5.24200   -3.13900  1.000 14.72414  ? 119 HIS A O   1 
ATOM   979  C  CB  . HIS A 1 119 ? 13.15300  2.67900   -2.47300  1.000 13.45946  ? 119 HIS A CB  1 
ATOM   980  C  CG  . HIS A 1 119 ? 13.07000  1.28100   -1.96000  1.000 12.88047  ? 119 HIS A CG  1 
ATOM   981  N  ND1 . HIS A 1 119 ? 14.08900  0.37400   -2.13400  1.000 14.03432  ? 119 HIS A ND1 1 
ATOM   982  C  CD2 . HIS A 1 119 ? 12.11000  0.64000   -1.26100  1.000 11.51343  ? 119 HIS A CD2 1 
ATOM   983  C  CE1 . HIS A 1 119 ? 13.75400  -0.77000  -1.57500  1.000 15.80381  ? 119 HIS A CE1 1 
ATOM   984  N  NE2 . HIS A 1 119 ? 12.54700  -0.63300  -1.03700  1.000 13.19870  ? 119 HIS A NE2 1 
ATOM   985  N  N   . PRO A 1 120 ? 14.82700  5.90100   -1.57400  1.000 14.45812  ? 120 PRO A N   1 
ATOM   986  C  CA  . PRO A 1 120 ? 14.63100  7.30000   -1.95100  1.000 16.55930  ? 120 PRO A CA  1 
ATOM   987  C  C   . PRO A 1 120 ? 14.92800  7.55700   -3.41900  1.000 16.59703  ? 120 PRO A C   1 
ATOM   988  O  O   . PRO A 1 120 ? 14.31200  8.45900   -4.01300  1.000 17.74887  ? 120 PRO A O   1 
ATOM   989  C  CB  . PRO A 1 120 ? 15.57000  8.04200   -0.99100  1.000 18.19505  ? 120 PRO A CB  1 
ATOM   990  C  CG  . PRO A 1 120 ? 16.60800  7.01400   -0.60100  1.000 16.51380  ? 120 PRO A CG  1 
ATOM   991  C  CD  . PRO A 1 120 ? 15.84500  5.70100   -0.54500  1.000 15.94010  ? 120 PRO A CD  1 
ATOM   992  N  N   . GLY A 1 121 ? 15.87900  6.84500   -4.00400  1.000 16.53766  ? 121 GLY A N   1 
ATOM   993  C  CA  . GLY A 1 121 ? 16.19600  7.01400   -5.43300  1.000 23.05132  ? 121 GLY A CA  1 
ATOM   994  C  C   . GLY A 1 121 ? 15.05900  6.65900   -6.36400  1.000 20.86511  ? 121 GLY A C   1 
ATOM   995  O  O   . GLY A 1 121 ? 15.03800  7.08900   -7.51400  1.000 26.18107  ? 121 GLY A O   1 
ATOM   996  N  N   . ASP A 1 122 ? 14.10100  5.85300   -5.89000  1.000 16.31384  ? 122 ASP A N   1 
ATOM   997  C  CA  . ASP A 1 122 ? 12.90700  5.42800   -6.63900  1.000 19.43868  ? 122 ASP A CA  1 
ATOM   998  C  C   . ASP A 1 122 ? 11.65100  6.05400   -6.05600  1.000 18.39257  ? 122 ASP A C   1 
ATOM   999  O  O   . ASP A 1 122 ? 10.52900  5.64600   -6.42400  1.000 17.84671  ? 122 ASP A O   1 
ATOM   1000 C  CB  . ASP A 1 122 ? 12.71800  3.91800   -6.53500  1.000 19.80482  ? 122 ASP A CB  1 
ATOM   1001 C  CG  . ASP A 1 122 ? 13.67100  3.14800   -7.39500  1.000 31.79011  ? 122 ASP A CG  1 
ATOM   1002 O  OD1 . ASP A 1 122 ? 14.02700  3.64700   -8.50200  1.000 33.52287  ? 122 ASP A OD1 1 
ATOM   1003 O  OD2 . ASP A 1 122 ? 13.95800  2.01200   -7.00100  1.000 30.30132  ? 122 ASP A OD2 1 
ATOM   1004 N  N   . PHE A 1 123 ? 11.82800  7.07000   -5.20800  1.000 15.19167  ? 123 PHE A N   1 
ATOM   1005 C  CA  . PHE A 1 123 ? 10.70200  7.61800   -4.42800  1.000 12.87035  ? 123 PHE A CA  1 
ATOM   1006 C  C   . PHE A 1 123 ? 10.88400  9.11000   -4.15700  1.000 13.04709  ? 123 PHE A C   1 
ATOM   1007 O  O   . PHE A 1 123 ? 10.66000  9.57200   -3.00600  1.000 14.87966  ? 123 PHE A O   1 
ATOM   1008 C  CB  . PHE A 1 123 ? 10.48200  6.77600   -3.18100  1.000 15.23633  ? 123 PHE A CB  1 
ATOM   1009 C  CG  . PHE A 1 123 ? 9.04400   6.71300   -2.71800  1.000 13.09146  ? 123 PHE A CG  1 
ATOM   1010 C  CD1 . PHE A 1 123 ? 8.10100   6.09900   -3.51100  1.000 14.73244  ? 123 PHE A CD1 1 
ATOM   1011 C  CD2 . PHE A 1 123 ? 8.66400   7.22300   -1.49400  1.000 14.54482  ? 123 PHE A CD2 1 
ATOM   1012 C  CE1 . PHE A 1 123 ? 6.79400   5.98100   -3.06800  1.000 13.20563  ? 123 PHE A CE1 1 
ATOM   1013 C  CE2 . PHE A 1 123 ? 7.34200   7.12600   -1.07200  1.000 16.27729  ? 123 PHE A CE2 1 
ATOM   1014 C  CZ  . PHE A 1 123 ? 6.42200   6.50300   -1.86400  1.000 15.19822  ? 123 PHE A CZ  1 
ATOM   1015 N  N   . GLY A 1 124 ? 11.16300  9.82700   -5.24100  1.000 14.29362  ? 124 GLY A N   1 
ATOM   1016 C  CA  . GLY A 1 124 ? 11.18400  11.29400  -5.16600  1.000 13.40959  ? 124 GLY A CA  1 
ATOM   1017 C  C   . GLY A 1 124 ? 9.76400   11.82700  -5.20400  1.000 14.39586  ? 124 GLY A C   1 
ATOM   1018 O  O   . GLY A 1 124 ? 8.83400   11.05000  -5.12400  1.000 13.96034  ? 124 GLY A O   1 
ATOM   1019 N  N   . ALA A 1 125 ? 9.62300   13.12700  -5.37800  1.000 12.66667  ? 125 ALA A N   1 
ATOM   1020 C  CA  . ALA A 1 125 ? 8.28600   13.73900  -5.23900  1.000 12.76301  ? 125 ALA A CA  1 
ATOM   1021 C  C   . ALA A 1 125 ? 7.25800   13.14500  -6.19500  1.000 15.50216  ? 125 ALA A C   1 
ATOM   1022 O  O   . ALA A 1 125 ? 6.11100   13.06500  -5.81900  1.000 14.83716  ? 125 ALA A O   1 
ATOM   1023 C  CB  . ALA A 1 125 ? 8.42400   15.22400  -5.46900  1.000 16.01860  ? 125 ALA A CB  1 
ATOM   1024 N  N   A ASP A 1 126 ? 7.63500   13.00200  -7.46400  0.500 16.42766  ? 126 ASP A N   1 
ATOM   1025 N  N   B ASP A 1 126 ? 7.62900   13.01400  -7.46800  0.500 16.43720  ? 126 ASP A N   1 
ATOM   1026 C  CA  A ASP A 1 126 ? 6.65600   12.51000  -8.46700  0.500 16.67970  ? 126 ASP A CA  1 
ATOM   1027 C  CA  B ASP A 1 126 ? 6.69300   12.47200  -8.48700  0.500 16.67711  ? 126 ASP A CA  1 
ATOM   1028 C  C   A ASP A 1 126 ? 6.20700   11.07700  -8.12300  0.500 16.79367  ? 126 ASP A C   1 
ATOM   1029 C  C   B ASP A 1 126 ? 6.20200   11.09500  -8.06000  0.500 16.80094  ? 126 ASP A C   1 
ATOM   1030 O  O   A ASP A 1 126 ? 5.00800   10.81000  -8.19900  0.500 16.11490  ? 126 ASP A O   1 
ATOM   1031 O  O   B ASP A 1 126 ? 5.01700   10.80800  -8.23400  0.500 16.14319  ? 126 ASP A O   1 
ATOM   1032 C  CB  A ASP A 1 126 ? 7.18300   12.71500  -9.88900  0.500 21.76512  ? 126 ASP A CB  1 
ATOM   1033 C  CB  B ASP A 1 126 ? 7.41500   12.35300  -9.83300  0.500 23.48706  ? 126 ASP A CB  1 
ATOM   1034 C  CG  A ASP A 1 126 ? 7.32400   14.18600  -10.26200 0.500 21.92954  ? 126 ASP A CG  1 
ATOM   1035 C  CG  B ASP A 1 126 ? 8.71600   11.54500  -9.81100  0.500 22.86296  ? 126 ASP A CG  1 
ATOM   1036 O  OD1 A ASP A 1 126 ? 6.95800   15.04800  -9.43600  0.500 20.67025  ? 126 ASP A OD1 1 
ATOM   1037 O  OD1 B ASP A 1 126 ? 9.25400   11.28400  -8.70800  0.500 19.40838  ? 126 ASP A OD1 1 
ATOM   1038 O  OD2 A ASP A 1 126 ? 7.80500   14.46200  -11.37500 0.500 25.65277  ? 126 ASP A OD2 1 
ATOM   1039 O  OD2 B ASP A 1 126 ? 9.20400   11.18800  -10.90700 0.500 22.43595  ? 126 ASP A OD2 1 
ATOM   1040 N  N   . ALA A 1 127 ? 7.13700   10.22500  -7.68500  1.000 15.38036  ? 127 ALA A N   1 
ATOM   1041 C  CA  . ALA A 1 127 ? 6.77500   8.84000   -7.32300  1.000 13.80587  ? 127 ALA A CA  1 
ATOM   1042 C  C   . ALA A 1 127 ? 5.98800   8.82000   -6.01700  1.000 16.47476  ? 127 ALA A C   1 
ATOM   1043 O  O   . ALA A 1 127 ? 5.07600   8.01500   -5.88100  1.000 15.17480  ? 127 ALA A O   1 
ATOM   1044 C  CB  . ALA A 1 127 ? 8.03100   8.02900   -7.21600  1.000 15.21790  ? 127 ALA A CB  1 
ATOM   1045 N  N   A GLN A 1 128 ? 6.38900   9.66200   -5.05900  0.530 15.58549  ? 128 GLN A N   1 
ATOM   1046 N  N   B GLN A 1 128 ? 6.38300   9.66900   -5.06600  0.470 15.59226  ? 128 GLN A N   1 
ATOM   1047 C  CA  A GLN A 1 128 ? 5.65900   9.75000   -3.76900  0.530 18.00573  ? 128 GLN A CA  1 
ATOM   1048 C  CA  B GLN A 1 128 ? 5.66000   9.73900   -3.77300  0.470 17.99989  ? 128 GLN A CA  1 
ATOM   1049 C  C   A GLN A 1 128 ? 4.22600   10.17100  -4.07300  0.530 17.83371  ? 128 GLN A C   1 
ATOM   1050 C  C   B GLN A 1 128 ? 4.22800   10.19000  -4.05300  0.470 17.81433  ? 128 GLN A C   1 
ATOM   1051 O  O   A GLN A 1 128 ? 3.30300   9.64400   -3.45300  0.530 16.17062  ? 128 GLN A O   1 
ATOM   1052 O  O   B GLN A 1 128 ? 3.30000   9.63100   -3.46800  0.470 16.20053  ? 128 GLN A O   1 
ATOM   1053 C  CB  A GLN A 1 128 ? 6.29700   10.80000  -2.85400  0.530 18.53807  ? 128 GLN A CB  1 
ATOM   1054 C  CB  B GLN A 1 128 ? 6.35000   10.69900  -2.80300  0.470 18.68689  ? 128 GLN A CB  1 
ATOM   1055 C  CG  A GLN A 1 128 ? 7.72800   10.50400  -2.43600  0.530 13.72187  ? 128 GLN A CG  1 
ATOM   1056 C  CG  B GLN A 1 128 ? 5.51300   10.94300  -1.55600  0.470 22.44951  ? 128 GLN A CG  1 
ATOM   1057 C  CD  A GLN A 1 128 ? 8.42200   11.72500  -1.87800  0.530 18.21098  ? 128 GLN A CD  1 
ATOM   1058 C  CD  B GLN A 1 128 ? 6.29600   10.94000  -0.26600  0.470 20.46458  ? 128 GLN A CD  1 
ATOM   1059 O  OE1 A GLN A 1 128 ? 7.78600   12.69700  -1.48100  0.530 25.85112  ? 128 GLN A OE1 1 
ATOM   1060 O  OE1 B GLN A 1 128 ? 7.44200   10.50000  -0.20700  0.470 24.29856  ? 128 GLN A OE1 1 
ATOM   1061 N  NE2 A GLN A 1 128 ? 9.74400   11.67900  -1.83300  0.530 14.21943  ? 128 GLN A NE2 1 
ATOM   1062 N  NE2 B GLN A 1 128 ? 5.66700   11.43100  0.78800   0.470 15.96458  ? 128 GLN A NE2 1 
ATOM   1063 N  N   . GLY A 1 129 ? 4.07000   11.18300  -4.92600  1.000 14.03335  ? 129 GLY A N   1 
ATOM   1064 C  CA  . GLY A 1 129 ? 2.73100   11.66800  -5.27700  1.000 14.75655  ? 129 GLY A CA  1 
ATOM   1065 C  C   . GLY A 1 129 ? 1.89000   10.62100  -5.97800  1.000 13.16339  ? 129 GLY A C   1 
ATOM   1066 O  O   . GLY A 1 129 ? 0.71200   10.57000  -5.71000  1.000 15.88160  ? 129 GLY A O   1 
ATOM   1067 N  N   . ALA A 1 130 ? 2.51800   9.84100   -6.85500  1.000 14.75881  ? 130 ALA A N   1 
ATOM   1068 C  CA  . ALA A 1 130 ? 1.79500   8.77000   -7.57300  1.000 13.39793  ? 130 ALA A CA  1 
ATOM   1069 C  C   . ALA A 1 130 ? 1.33600   7.71300   -6.56300  1.000 12.88307  ? 130 ALA A C   1 
ATOM   1070 O  O   . ALA A 1 130 ? 0.19800   7.28600   -6.64500  1.000 13.13881  ? 130 ALA A O   1 
ATOM   1071 C  CB  . ALA A 1 130 ? 2.69900   8.16800   -8.61300  1.000 13.98115  ? 130 ALA A CB  1 
ATOM   1072 N  N   . MET A 1 131 ? 2.22700   7.34200   -5.64900  1.000 14.21630  ? 131 MET A N   1 
ATOM   1073 C  CA  . MET A 1 131 ? 1.87400   6.32000   -4.63000  1.000 11.77208  ? 131 MET A CA  1 
ATOM   1074 C  C   . MET A 1 131 ? 0.78700   6.89000   -3.72000  1.000 13.64515  ? 131 MET A C   1 
ATOM   1075 O  O   . MET A 1 131 ? -0.18700  6.17500   -3.39000  1.000 13.31352  ? 131 MET A O   1 
ATOM   1076 C  CB  . MET A 1 131 ? 3.09000   5.89900   -3.81500  1.000 12.60406  ? 131 MET A CB  1 
ATOM   1077 C  CG  . MET A 1 131 ? 2.76500   4.81000   -2.81600  1.000 15.76444  ? 131 MET A CG  1 
ATOM   1078 S  SD  . MET A 1 131 ? 2.18900   3.23200   -3.51700  1.000 14.09852  ? 131 MET A SD  1 
ATOM   1079 C  CE  . MET A 1 131 ? 3.70800   2.59500   -4.21900  1.000 15.61545  ? 131 MET A CE  1 
ATOM   1080 N  N   . ASN A 1 132 ? 0.85800   8.18100   -3.35700  1.000 13.31324  ? 132 ASN A N   1 
ATOM   1081 C  CA  . ASN A 1 132 ? -0.20200  8.82700   -2.54300  1.000 13.29012  ? 132 ASN A CA  1 
ATOM   1082 C  C   . ASN A 1 132 ? -1.52800  8.69800   -3.28900  1.000 15.51576  ? 132 ASN A C   1 
ATOM   1083 O  O   . ASN A 1 132 ? -2.53800  8.32400   -2.65300  1.000 14.66417  ? 132 ASN A O   1 
ATOM   1084 C  CB  . ASN A 1 132 ? 0.26700   10.24400  -2.20200  1.000 15.10042  ? 132 ASN A CB  1 
ATOM   1085 C  CG  . ASN A 1 132 ? -0.75700  10.93100  -1.34200  1.000 21.23399  ? 132 ASN A CG  1 
ATOM   1086 O  OD1 . ASN A 1 132 ? -1.14800  10.38600  -0.30800  1.000 22.72463  ? 132 ASN A OD1 1 
ATOM   1087 N  ND2 . ASN A 1 132 ? -1.17000  12.12000  -1.75600  1.000 32.62691  ? 132 ASN A ND2 1 
ATOM   1088 N  N   . LYS A 1 133 ? -1.57800  9.00600   -4.57600  1.000 12.33813  ? 133 LYS A N   1 
ATOM   1089 C  CA  . LYS A 1 133 ? -2.81600  8.94400   -5.38300  1.000 14.11021  ? 133 LYS A CA  1 
ATOM   1090 C  C   . LYS A 1 133 ? -3.31500  7.50900   -5.42400  1.000 13.81642  ? 133 LYS A C   1 
ATOM   1091 O  O   . LYS A 1 133 ? -4.50500  7.29900   -5.30700  1.000 13.95311  ? 133 LYS A O   1 
ATOM   1092 C  CB  . LYS A 1 133 ? -2.55400  9.44600   -6.79400  1.000 15.87789  ? 133 LYS A CB  1 
ATOM   1093 C  CG  . LYS A 1 133 ? -2.35300  10.94600  -6.86800  1.000 17.95421  ? 133 LYS A CG  1 
ATOM   1094 C  CD  . LYS A 1 133 ? -2.23300  11.42500  -8.27300  1.000 24.23470  ? 133 LYS A CD  1 
ATOM   1095 C  CE  . LYS A 1 133 ? -1.64300  12.81400  -8.36100  1.000 31.31249  ? 133 LYS A CE  1 
ATOM   1096 N  NZ  . LYS A 1 133 ? -1.51000  13.20000  -9.78300  1.000 36.05769  ? 133 LYS A NZ  1 
ATOM   1097 N  N   . ALA A 1 134 ? -2.42600  6.54800   -5.59700  1.000 11.66872  ? 134 ALA A N   1 
ATOM   1098 C  CA  . ALA A 1 134 ? -2.83600  5.12700   -5.73100  1.000 10.75096  ? 134 ALA A CA  1 
ATOM   1099 C  C   . ALA A 1 134 ? -3.46700  4.65600   -4.43500  1.000 12.66980  ? 134 ALA A C   1 
ATOM   1100 O  O   . ALA A 1 134 ? -4.51300  3.96000   -4.44900  1.000 12.20825  ? 134 ALA A O   1 
ATOM   1101 C  CB  . ALA A 1 134 ? -1.66300  4.26400   -6.11300  1.000 10.92067  ? 134 ALA A CB  1 
ATOM   1102 N  N   . LEU A 1 135 ? -2.88000  4.99800   -3.30300  1.000 13.14868  ? 135 LEU A N   1 
ATOM   1103 C  CA  . LEU A 1 135 ? -3.41400  4.62600   -1.97900  1.000 12.97233  ? 135 LEU A CA  1 
ATOM   1104 C  C   . LEU A 1 135 ? -4.65300  5.44400   -1.63900  1.000 13.15010  ? 135 LEU A C   1 
ATOM   1105 O  O   . LEU A 1 135 ? -5.62700  4.82800   -1.09400  1.000 13.60444  ? 135 LEU A O   1 
ATOM   1106 C  CB  . LEU A 1 135 ? -2.35900  4.72100   -0.89300  1.000 14.87825  ? 135 LEU A CB  1 
ATOM   1107 C  CG  . LEU A 1 135 ? -1.15600  3.80700   -1.09900  1.000 11.57952  ? 135 LEU A CG  1 
ATOM   1108 C  CD1 . LEU A 1 135 ? -0.14300  4.03700   -0.03100  1.000 15.07666  ? 135 LEU A CD1 1 
ATOM   1109 C  CD2 . LEU A 1 135 ? -1.56400  2.32800   -1.16900  1.000 14.27297  ? 135 LEU A CD2 1 
ATOM   1110 N  N   . GLU A 1 136 ? -4.77700  6.68200   -2.09400  1.000 12.20443  ? 136 GLU A N   1 
ATOM   1111 C  CA  . GLU A 1 136 ? -6.04400  7.43300   -1.89200  1.000 12.36808  ? 136 GLU A CA  1 
ATOM   1112 C  C   . GLU A 1 136 ? -7.15400  6.74500   -2.68900  1.000 13.08431  ? 136 GLU A C   1 
ATOM   1113 O  O   . GLU A 1 136 ? -8.29900  6.69600   -2.19000  1.000 14.36682  ? 136 GLU A O   1 
ATOM   1114 C  CB  . GLU A 1 136 ? -5.84800  8.86800   -2.38700  1.000 16.86631  ? 136 GLU A CB  1 
ATOM   1115 C  CG  . GLU A 1 136 ? -5.09800  9.75600   -1.42500  1.000 20.48714  ? 136 GLU A CG  1 
ATOM   1116 C  CD  . GLU A 1 136 ? -4.96400  11.19100  -1.91100  1.000 27.85979  ? 136 GLU A CD  1 
ATOM   1117 O  OE1 . GLU A 1 136 ? -4.33700  11.99200  -1.16700  1.000 37.91996  ? 136 GLU A OE1 1 
ATOM   1118 O  OE2 . GLU A 1 136 ? -5.43500  11.48000  -3.05300  1.000 31.93945  ? 136 GLU A OE2 1 
ATOM   1119 N  N   . LEU A 1 137 ? -6.85300  6.29100   -3.91000  1.000 12.60048  ? 137 LEU A N   1 
ATOM   1120 C  CA  . LEU A 1 137 ? -7.92300  5.65400   -4.72900  1.000 11.49228  ? 137 LEU A CA  1 
ATOM   1121 C  C   . LEU A 1 137 ? -8.35500  4.34600   -4.06300  1.000 13.16634  ? 137 LEU A C   1 
ATOM   1122 O  O   . LEU A 1 137 ? -9.56300  4.07100   -3.98100  1.000 12.51439  ? 137 LEU A O   1 
ATOM   1123 C  CB  . LEU A 1 137 ? -7.37700  5.39700   -6.13500  1.000 12.33634  ? 137 LEU A CB  1 
ATOM   1124 C  CG  . LEU A 1 137 ? -8.32100  4.65000   -7.06200  1.000 14.43489  ? 137 LEU A CG  1 
ATOM   1125 C  CD1 . LEU A 1 137 ? -9.55200  5.51300   -7.31500  1.000 17.50825  ? 137 LEU A CD1 1 
ATOM   1126 C  CD2 . LEU A 1 137 ? -7.57900  4.29300   -8.35700  1.000 18.50592  ? 137 LEU A CD2 1 
ATOM   1127 N  N   . PHE A 1 138 ? -7.41000  3.56200   -3.59200  1.000 13.16604  ? 138 PHE A N   1 
ATOM   1128 C  CA  . PHE A 1 138 ? -7.73900  2.34300   -2.82600  1.000 12.18641  ? 138 PHE A CA  1 
ATOM   1129 C  C   . PHE A 1 138 ? -8.68200  2.70700   -1.68900  1.000 13.49563  ? 138 PHE A C   1 
ATOM   1130 O  O   . PHE A 1 138 ? -9.70400  2.02600   -1.45900  1.000 12.02185  ? 138 PHE A O   1 
ATOM   1131 C  CB  . PHE A 1 138 ? -6.43000  1.73000   -2.31800  1.000 11.79531  ? 138 PHE A CB  1 
ATOM   1132 C  CG  . PHE A 1 138 ? -6.52000  0.71600   -1.21700  1.000 12.07239  ? 138 PHE A CG  1 
ATOM   1133 C  CD1 . PHE A 1 138 ? -7.08400  -0.53300  -1.44500  1.000 12.97305  ? 138 PHE A CD1 1 
ATOM   1134 C  CD2 . PHE A 1 138 ? -6.13100  1.00700   0.08200   1.000 11.78040  ? 138 PHE A CD2 1 
ATOM   1135 C  CE1 . PHE A 1 138 ? -7.18900  -1.44300  -0.39900  1.000 13.39643  ? 138 PHE A CE1 1 
ATOM   1136 C  CE2 . PHE A 1 138 ? -6.25900  0.10000   1.10100   1.000 12.98158  ? 138 PHE A CE2 1 
ATOM   1137 C  CZ  . PHE A 1 138 ? -6.79000  -1.13400  0.85500   1.000 12.46993  ? 138 PHE A CZ  1 
ATOM   1138 N  N   . ARG A 1 139 ? -8.32600  3.69300   -0.86200  1.000 12.69128  ? 139 ARG A N   1 
ATOM   1139 C  CA  . ARG A 1 139 ? -9.16100  4.02200   0.32700   1.000 10.90277  ? 139 ARG A CA  1 
ATOM   1140 C  C   . ARG A 1 139 ? -10.54600 4.55500   -0.07700  1.000 14.01400  ? 139 ARG A C   1 
ATOM   1141 O  O   . ARG A 1 139 ? -11.52000 4.21600   0.57800   1.000 13.71854  ? 139 ARG A O   1 
ATOM   1142 C  CB  . ARG A 1 139 ? -8.44000  5.02700   1.23000   1.000 10.99275  ? 139 ARG A CB  1 
ATOM   1143 C  CG  . ARG A 1 139 ? -7.14800  4.50800   1.84200   1.000 11.42867  ? 139 ARG A CG  1 
ATOM   1144 C  CD  . ARG A 1 139 ? -6.60700  5.42400   2.92500   1.000 11.55344  ? 139 ARG A CD  1 
ATOM   1145 N  NE  . ARG A 1 139 ? -6.44400  6.81000   2.51100   1.000 14.59928  ? 139 ARG A NE  1 
ATOM   1146 C  CZ  . ARG A 1 139 ? -5.35700  7.31400   1.94300   1.000 11.65146  ? 139 ARG A CZ  1 
ATOM   1147 N  NH1 . ARG A 1 139 ? -4.30900  6.54800   1.70300   1.000 12.67214  ? 139 ARG A NH1 1 
ATOM   1148 N  NH2 . ARG A 1 139 ? -5.32200  8.59000   1.61100   1.000 14.30622  ? 139 ARG A NH2 1 
ATOM   1149 N  N   . LYS A 1 140 ? -10.59200 5.35800   -1.13400  1.000 12.79945  ? 140 LYS A N   1 
ATOM   1150 C  CA  . LYS A 1 140 ? -11.90000 5.88100   -1.60300  1.000 12.67086  ? 140 LYS A CA  1 
ATOM   1151 C  C   . LYS A 1 140 ? -12.79700 4.71800   -2.03000  1.000 12.48297  ? 140 LYS A C   1 
ATOM   1152 O  O   . LYS A 1 140 ? -13.96600 4.67300   -1.64600  1.000 13.11501  ? 140 LYS A O   1 
ATOM   1153 C  CB  . LYS A 1 140 ? -11.66600 6.82300   -2.78400  1.000 14.98567  ? 140 LYS A CB  1 
ATOM   1154 C  CG  . LYS A 1 140 ? -12.91800 7.26000   -3.52900  1.000 19.51043  ? 140 LYS A CG  1 
ATOM   1155 C  CD  . LYS A 1 140 ? -12.60900 8.17900   -4.68700  1.000 22.14657  ? 140 LYS A CD  1 
ATOM   1156 C  CE  . LYS A 1 140 ? -13.84800 8.76300   -5.32900  1.000 30.80263  ? 140 LYS A CE  1 
ATOM   1157 N  NZ  . LYS A 1 140 ? -14.57900 7.75300   -6.12700  1.000 38.09527  ? 140 LYS A NZ  1 
ATOM   1158 N  N   . ASP A 1 141 ? -12.23000 3.81800   -2.80500  1.000 12.27523  ? 141 ASP A N   1 
ATOM   1159 C  CA  . ASP A 1 141 ? -13.07000 2.73000   -3.34600  1.000 12.70686  ? 141 ASP A CA  1 
ATOM   1160 C  C   . ASP A 1 141 ? -13.48300 1.75700   -2.23100  1.000 14.33377  ? 141 ASP A C   1 
ATOM   1161 O  O   . ASP A 1 141 ? -14.59200 1.25900   -2.27500  1.000 13.69880  ? 141 ASP A O   1 
ATOM   1162 C  CB  . ASP A 1 141 ? -12.37700 2.01500   -4.51000  1.000 13.58121  ? 141 ASP A CB  1 
ATOM   1163 C  CG  . ASP A 1 141 ? -12.29100 2.84800   -5.78100  1.000 17.02958  ? 141 ASP A CG  1 
ATOM   1164 O  OD1 . ASP A 1 141 ? -12.93900 3.89800   -5.83900  1.000 17.78714  ? 141 ASP A OD1 1 
ATOM   1165 O  OD2 . ASP A 1 141 ? -11.57700 2.43500   -6.69500  1.000 16.59780  ? 141 ASP A OD2 1 
ATOM   1166 N  N   . ILE A 1 142 ? -12.56900 1.48700   -1.29800  1.000 12.04535  ? 142 ILE A N   1 
ATOM   1167 C  CA  . ILE A 1 142 ? -12.91800 0.53000   -0.21400  1.000 12.53602  ? 142 ILE A CA  1 
ATOM   1168 C  C   . ILE A 1 142 ? -14.00600 1.15000   0.68900   1.000 13.81190  ? 142 ILE A C   1 
ATOM   1169 O  O   . ILE A 1 142 ? -14.87200 0.42900   1.15000   1.000 13.56790  ? 142 ILE A O   1 
ATOM   1170 C  CB  . ILE A 1 142 ? -11.67700 0.01700   0.55000   1.000 14.80822  ? 142 ILE A CB  1 
ATOM   1171 C  CG1 . ILE A 1 142 ? -11.97600 -1.34900  1.17500   1.000 18.45170  ? 142 ILE A CG1 1 
ATOM   1172 C  CG2 . ILE A 1 142 ? -11.20100 1.01900   1.58000   1.000 15.40652  ? 142 ILE A CG2 1 
ATOM   1173 C  CD1 . ILE A 1 142 ? -10.78000 -2.05300  1.75800   1.000 14.88993  ? 142 ILE A CD1 1 
ATOM   1174 N  N   . ALA A 1 143 ? -13.93600 2.46200   0.88300   1.000 12.31140  ? 143 ALA A N   1 
ATOM   1175 C  CA  . ALA A 1 143 ? -14.94300 3.14500   1.72600   1.000 12.45697  ? 143 ALA A CA  1 
ATOM   1176 C  C   . ALA A 1 143 ? -16.34400 3.05400   1.09300   1.000 13.85244  ? 143 ALA A C   1 
ATOM   1177 O  O   . ALA A 1 143 ? -17.30400 2.88200   1.81700   1.000 13.86948  ? 143 ALA A O   1 
ATOM   1178 C  CB  . ALA A 1 143 ? -14.51900 4.57100   1.95500   1.000 13.39187  ? 143 ALA A CB  1 
ATOM   1179 N  N   . ALA A 1 144 ? -16.41800 3.16000   -0.22300  1.000 12.88686  ? 144 ALA A N   1 
ATOM   1180 C  CA  . ALA A 1 144 ? -17.72700 3.04600   -0.89700  1.000 13.59335  ? 144 ALA A CA  1 
ATOM   1181 C  C   . ALA A 1 144 ? -18.27500 1.62100   -0.71700  1.000 13.74146  ? 144 ALA A C   1 
ATOM   1182 O  O   . ALA A 1 144 ? -19.45300 1.46200   -0.47400  1.000 14.58672  ? 144 ALA A O   1 
ATOM   1183 C  CB  . ALA A 1 144 ? -17.56700 3.44700   -2.34300  1.000 14.60977  ? 144 ALA A CB  1 
ATOM   1184 N  N   . LYS A 1 145 ? -17.38300 0.63300   -0.76300  1.000 13.85547  ? 145 LYS A N   1 
ATOM   1185 C  CA  . LYS A 1 145 ? -17.80300 -0.78100  -0.55400  1.000 10.71294  ? 145 LYS A CA  1 
ATOM   1186 C  C   . LYS A 1 145 ? -18.18100 -1.00400  0.91700   1.000 13.29111  ? 145 LYS A C   1 
ATOM   1187 O  O   . LYS A 1 145 ? -19.12900 -1.70400  1.16500   1.000 13.94937  ? 145 LYS A O   1 
ATOM   1188 C  CB  . LYS A 1 145 ? -16.70900 -1.72800  -1.06100  1.000 15.26201  ? 145 LYS A CB  1 
ATOM   1189 C  CG  . LYS A 1 145 ? -16.58500 -1.78700  -2.57500  1.000 19.04157  ? 145 LYS A CG  1 
ATOM   1190 C  CD  . LYS A 1 145 ? -17.84300 -2.31300  -3.22500  1.000 28.92661  ? 145 LYS A CD  1 
ATOM   1191 C  CE  . LYS A 1 145 ? -17.92100 -2.03500  -4.71000  1.000 43.09611  ? 145 LYS A CE  1 
ATOM   1192 N  NZ  . LYS A 1 145 ? -19.12500 -2.65600  -5.30900  1.000 37.71426  ? 145 LYS A NZ  1 
ATOM   1193 N  N   . TYR A 1 146 ? -17.42900 -0.40900  1.83400   1.000 11.70015  ? 146 TYR A N   1 
ATOM   1194 C  CA  . TYR A 1 146 ? -17.79500 -0.48700  3.26600   1.000 11.46576  ? 146 TYR A CA  1 
ATOM   1195 C  C   . TYR A 1 146 ? -19.24900 -0.03700  3.43800   1.000 12.89617  ? 146 TYR A C   1 
ATOM   1196 O  O   . TYR A 1 146 ? -20.00800 -0.73700  4.09100   1.000 13.26535  ? 146 TYR A O   1 
ATOM   1197 C  CB  . TYR A 1 146 ? -16.90800 0.47100   4.06600   1.000 12.31779  ? 146 TYR A CB  1 
ATOM   1198 C  CG  . TYR A 1 146 ? -15.57600 -0.02000  4.57100   1.000 12.17805  ? 146 TYR A CG  1 
ATOM   1199 C  CD1 . TYR A 1 146 ? -15.04800 -1.24400  4.20600   1.000 12.34244  ? 146 TYR A CD1 1 
ATOM   1200 C  CD2 . TYR A 1 146 ? -14.84500 0.76800   5.43800   1.000 14.94367  ? 146 TYR A CD2 1 
ATOM   1201 C  CE1 . TYR A 1 146 ? -13.83000 -1.67400  4.70200   1.000 12.26348  ? 146 TYR A CE1 1 
ATOM   1202 C  CE2 . TYR A 1 146 ? -13.62800 0.35400   5.94600   1.000 11.71694  ? 146 TYR A CE2 1 
ATOM   1203 C  CZ  . TYR A 1 146 ? -13.12000 -0.87500  5.57900   1.000 11.52594  ? 146 TYR A CZ  1 
ATOM   1204 O  OH  . TYR A 1 146 ? -11.92300 -1.28300  6.08000   1.000 11.68131  ? 146 TYR A OH  1 
ATOM   1205 N  N   . LYS A 1 147 ? -19.57500 1.11500   2.84700   1.000 12.57741  ? 147 LYS A N   1 
ATOM   1206 C  CA  . LYS A 1 147 ? -20.93900 1.67300   3.01000   1.000 12.44879  ? 147 LYS A CA  1 
ATOM   1207 C  C   . LYS A 1 147 ? -21.96900 0.72800   2.38100   1.000 14.07468  ? 147 LYS A C   1 
ATOM   1208 O  O   . LYS A 1 147 ? -23.02000 0.54200   2.96800   1.000 12.97735  ? 147 LYS A O   1 
ATOM   1209 C  CB  . LYS A 1 147 ? -21.00200 3.08800   2.42900   1.000 11.69222  ? 147 LYS A CB  1 
ATOM   1210 C  CG  . LYS A 1 147 ? -20.22400 4.10700   3.24900   1.000 17.89250  ? 147 LYS A CG  1 
ATOM   1211 C  CD  . LYS A 1 147 ? -20.17700 5.48200   2.64200   1.000 21.47523  ? 147 LYS A CD  1 
ATOM   1212 C  CE  . LYS A 1 147 ? -19.39700 6.46100   3.49500   1.000 24.95077  ? 147 LYS A CE  1 
ATOM   1213 N  NZ  . LYS A 1 147 ? -17.95500 6.11800   3.57100   1.000 31.36673  ? 147 LYS A NZ  1 
ATOM   1214 N  N   . GLU A 1 148 ? -21.62200 0.13700   1.25200   1.000 13.44690  ? 148 GLU A N   1 
ATOM   1215 C  CA  . GLU A 1 148 ? -22.56800 -0.78700  0.60000   1.000 13.23219  ? 148 GLU A CA  1 
ATOM   1216 C  C   . GLU A 1 148 ? -22.91900 -1.90100  1.56700   1.000 13.31184  ? 148 GLU A C   1 
ATOM   1217 O  O   . GLU A 1 148 ? -24.05100 -2.45000  1.47500   1.000 14.00697  ? 148 GLU A O   1 
ATOM   1218 C  CB  . GLU A 1 148 ? -21.98700 -1.37200  -0.66800  1.000 16.09353  ? 148 GLU A CB  1 
ATOM   1219 C  CG  . GLU A 1 148 ? -21.99000 -0.44500  -1.82200  1.000 19.63958  ? 148 GLU A CG  1 
ATOM   1220 C  CD  . GLU A 1 148 ? -21.63100 -1.15200  -3.12400  1.000 33.35952  ? 148 GLU A CD  1 
ATOM   1221 O  OE1 . GLU A 1 148 ? -21.52100 -2.44500  -3.13200  1.000 27.55505  ? 148 GLU A OE1 1 
ATOM   1222 O  OE2 . GLU A 1 148 ? -21.53500 -0.43700  -4.11900  1.000 33.41739  ? 148 GLU A OE2 1 
ATOM   1223 N  N   . LEU A 1 149 ? -21.96300 -2.33200  2.40000   1.000 12.65882  ? 149 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 149 ? -22.14600 -3.40100  3.40600   1.000 12.69366  ? 149 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 149 ? -22.72400 -2.89800  4.71900   1.000 13.80907  ? 149 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 149 ? -22.88700 -3.70700  5.66000   1.000 17.05417  ? 149 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 149 ? -20.77400 -4.05700  3.58400   1.000 14.60220  ? 149 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 149 ? -20.19200 -4.66100  2.31300   1.000 15.95381  ? 149 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 149 ? -18.73500 -5.04200  2.57100   1.000 19.73670  ? 149 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 149 ? -21.00300 -5.84200  1.83500   1.000 23.87999  ? 149 LEU A CD2 1 
ATOM   1231 N  N   . GLY A 1 150 ? -23.01600 -1.60400  4.83800   1.000 12.95265  ? 150 GLY A N   1 
ATOM   1232 C  CA  . GLY A 1 150 ? -23.63400 -1.03100  6.05400   1.000 12.85624  ? 150 GLY A CA  1 
ATOM   1233 C  C   . GLY A 1 150 ? -22.63100 -0.53700  7.08800   1.000 15.56034  ? 150 GLY A C   1 
ATOM   1234 O  O   . GLY A 1 150 ? -23.03000 -0.25700  8.20700   1.000 18.07645  ? 150 GLY A O   1 
ATOM   1235 N  N   . TYR A 1 151 ? -21.33100 -0.48800  6.74100   1.000 12.33503  ? 151 TYR A N   1 
ATOM   1236 C  CA  . TYR A 1 151 ? -20.26300 -0.03300  7.65200   1.000 13.18799  ? 151 TYR A CA  1 
ATOM   1237 C  C   . TYR A 1 151 ? -19.85300 1.38300   7.29300   1.000 13.64942  ? 151 TYR A C   1 
ATOM   1238 O  O   . TYR A 1 151 ? -19.40700 1.65400   6.18000   1.000 14.86403  ? 151 TYR A O   1 
ATOM   1239 C  CB  . TYR A 1 151 ? -19.09700 -1.01600  7.58000   1.000 12.57331  ? 151 TYR A CB  1 
ATOM   1240 C  CG  . TYR A 1 151 ? -17.94800 -0.66300  8.51500   1.000 16.37474  ? 151 TYR A CG  1 
ATOM   1241 C  CD1 . TYR A 1 151 ? -18.12300 -0.44400  9.88200   1.000 17.23735  ? 151 TYR A CD1 1 
ATOM   1242 C  CD2 . TYR A 1 151 ? -16.66400 -0.51600  7.99800   1.000 15.23256  ? 151 TYR A CD2 1 
ATOM   1243 C  CE1 . TYR A 1 151 ? -17.05400 -0.12500  10.70500  1.000 18.45770  ? 151 TYR A CE1 1 
ATOM   1244 C  CE2 . TYR A 1 151 ? -15.58800 -0.23700  8.81800   1.000 15.91578  ? 151 TYR A CE2 1 
ATOM   1245 C  CZ  . TYR A 1 151 ? -15.78100 -0.06300  10.18100  1.000 20.37467  ? 151 TYR A CZ  1 
ATOM   1246 O  OH  . TYR A 1 151 ? -14.71800 0.25200   11.01500  1.000 20.29099  ? 151 TYR A OH  1 
ATOM   1247 N  N   . GLN A 1 152 ? -20.04400 2.30400   8.24000   1.000 16.88892  ? 152 GLN A N   1 
ATOM   1248 C  CA  . GLN A 1 152 ? -19.72600 3.73700   8.01500   1.000 16.78313  ? 152 GLN A CA  1 
ATOM   1249 C  C   . GLN A 1 152 ? -18.36800 4.13700   8.58500   1.000 25.48336  ? 152 GLN A C   1 
ATOM   1250 O  O   . GLN A 1 152 ? -18.15300 5.36200   8.82400   1.000 27.07506  ? 152 GLN A O   1 
ATOM   1251 C  CB  . GLN A 1 152 ? -20.79800 4.63300   8.66700   1.000 19.70380  ? 152 GLN A CB  1 
ATOM   1252 C  CG  . GLN A 1 152 ? -22.20500 4.38300   8.13400   1.000 20.00366  ? 152 GLN A CG  1 
ATOM   1253 C  CD  . GLN A 1 152 ? -22.35000 4.70700   6.67100   1.000 19.92932  ? 152 GLN A CD  1 
ATOM   1254 O  OE1 . GLN A 1 152 ? -21.76900 5.63200   6.14000   1.000 24.88766  ? 152 GLN A OE1 1 
ATOM   1255 N  NE2 . GLN A 1 152 ? -23.17500 3.94400   5.96900   1.000 18.43202  ? 152 GLN A NE2 1 
ATOM   1256 N  N   A GLY A 1 153 ? -17.47700 3.18100   8.84200   0.550 19.83670  ? 153 GLY A N   1 
ATOM   1257 N  N   B GLY A 1 153 ? -17.42400 3.19600   8.61600   0.450 19.69383  ? 153 GLY A N   1 
ATOM   1258 C  CA  A GLY A 1 153 ? -16.19100 3.48000   9.50200   0.550 23.99563  ? 153 GLY A CA  1 
ATOM   1259 C  CA  B GLY A 1 153 ? -16.06900 3.43500   9.14200   0.450 22.81681  ? 153 GLY A CA  1 
ATOM   1260 C  C   A GLY A 1 153 ? -15.19000 4.07200   8.52600   0.550 20.76902  ? 153 GLY A C   1 
ATOM   1261 C  C   B GLY A 1 153 ? -15.21100 4.17100   8.14200   0.450 19.55368  ? 153 GLY A C   1 
ATOM   1262 O  O   A GLY A 1 153 ? -14.16800 4.59300   9.01200   0.550 12.25655  ? 153 GLY A O   1 
ATOM   1263 O  O   B GLY A 1 153 ? -15.58400 4.25400   7.01600   0.450 14.05915  ? 153 GLY A O   1 
HETATM 1264 C  CHA . HEM B 2 .   ? -6.57200  -9.75700  7.66200   1.000 11.43172  ? 201 HEM A CHA 1 
HETATM 1265 C  CHB . HEM B 2 .   ? -5.13400  -7.18500  3.81900   1.000 11.16670  ? 201 HEM A CHB 1 
HETATM 1266 C  CHC . HEM B 2 .   ? -5.12900  -3.19500  6.56600   1.000 13.13354  ? 201 HEM A CHC 1 
HETATM 1267 C  CHD . HEM B 2 .   ? -6.55600  -5.77100  10.33900  1.000 12.77622  ? 201 HEM A CHD 1 
HETATM 1268 C  C1A . HEM B 2 .   ? -6.19800  -9.42700  6.35400   1.000 12.88638  ? 201 HEM A C1A 1 
HETATM 1269 C  C2A . HEM B 2 .   ? -6.11000  -10.28900 5.18400   1.000 13.32763  ? 201 HEM A C2A 1 
HETATM 1270 C  C3A . HEM B 2 .   ? -5.69500  -9.59500  4.12100   1.000 11.03355  ? 201 HEM A C3A 1 
HETATM 1271 C  C4A . HEM B 2 .   ? -5.53000  -8.22400  4.62800   1.000 10.26207  ? 201 HEM A C4A 1 
HETATM 1272 C  CMA . HEM B 2 .   ? -5.45600  -10.05100 2.75100   1.000 14.67183  ? 201 HEM A CMA 1 
HETATM 1273 C  CAA . HEM B 2 .   ? -6.47000  -11.79000 5.17300   1.000 12.18038  ? 201 HEM A CAA 1 
HETATM 1274 C  CBA . HEM B 2 .   ? -7.85900  -12.05100 4.55200   1.000 11.43914  ? 201 HEM A CBA 1 
HETATM 1275 C  CGA . HEM B 2 .   ? -8.94700  -11.29600 5.24900   1.000 15.32936  ? 201 HEM A CGA 1 
HETATM 1276 O  O1A . HEM B 2 .   ? -9.47100  -10.41500 4.52100   1.000 14.89850  ? 201 HEM A O1A 1 
HETATM 1277 O  O2A . HEM B 2 .   ? -9.26300  -11.45500 6.45500   1.000 16.80872  ? 201 HEM A O2A 1 
HETATM 1278 C  C1B . HEM B 2 .   ? -5.04300  -5.84600  4.24800   1.000 10.26307  ? 201 HEM A C1B 1 
HETATM 1279 C  C2B . HEM B 2 .   ? -4.60500  -4.82000  3.36600   1.000 11.30302  ? 201 HEM A C2B 1 
HETATM 1280 C  C3B . HEM B 2 .   ? -4.57100  -3.64900  4.14200   1.000 11.10155  ? 201 HEM A C3B 1 
HETATM 1281 C  C4B . HEM B 2 .   ? -5.01200  -4.02400  5.45700   1.000 10.57212  ? 201 HEM A C4B 1 
HETATM 1282 C  CMB . HEM B 2 .   ? -4.27700  -4.87400  1.91200   1.000 11.01025  ? 201 HEM A CMB 1 
HETATM 1283 C  CAB . HEM B 2 .   ? -4.18100  -2.29600  3.77400   1.000 12.11174  ? 201 HEM A CAB 1 
HETATM 1284 C  CBB . HEM B 2 .   ? -3.32900  -1.94600  2.86800   1.000 15.88295  ? 201 HEM A CBB 1 
HETATM 1285 C  C1C . HEM B 2 .   ? -5.43900  -3.53400  7.84400   1.000 11.22835  ? 201 HEM A C1C 1 
HETATM 1286 C  C2C . HEM B 2 .   ? -5.36300  -2.69400  9.00300   1.000 11.40606  ? 201 HEM A C2C 1 
HETATM 1287 C  C3C . HEM B 2 .   ? -5.75200  -3.43600  10.08600  1.000 12.79654  ? 201 HEM A C3C 1 
HETATM 1288 C  C4C . HEM B 2 .   ? -6.09700  -4.73700  9.57500   1.000 12.59633  ? 201 HEM A C4C 1 
HETATM 1289 C  CMC . HEM B 2 .   ? -4.92700  -1.27700  8.93800   1.000 13.96872  ? 201 HEM A CMC 1 
HETATM 1290 C  CAC . HEM B 2 .   ? -5.82900  -3.03200  11.52300  1.000 12.89129  ? 201 HEM A CAC 1 
HETATM 1291 C  CBC . HEM B 2 .   ? -5.50300  -1.85400  12.07000  1.000 16.02058  ? 201 HEM A CBC 1 
HETATM 1292 C  C1D . HEM B 2 .   ? -6.71300  -7.07600  9.89500   1.000 12.00020  ? 201 HEM A C1D 1 
HETATM 1293 C  C2D . HEM B 2 .   ? -7.05400  -8.15600  10.83200  1.000 17.02927  ? 201 HEM A C2D 1 
HETATM 1294 C  C3D . HEM B 2 .   ? -7.02500  -9.27400  10.10800  1.000 14.56500  ? 201 HEM A C3D 1 
HETATM 1295 C  C4D . HEM B 2 .   ? -6.68000  -8.88000  8.72100   1.000 11.66554  ? 201 HEM A C4D 1 
HETATM 1296 C  CMD . HEM B 2 .   ? -7.34900  -8.03600  12.33500  1.000 18.65356  ? 201 HEM A CMD 1 
HETATM 1297 C  CAD . HEM B 2 .   ? -7.28000  -10.67800 10.66600  1.000 18.16980  ? 201 HEM A CAD 1 
HETATM 1298 C  CBD . HEM B 2 .   ? -5.90200  -11.26200 11.08000  1.000 22.41512  ? 201 HEM A CBD 1 
HETATM 1299 C  CGD . HEM B 2 .   ? -6.11300  -12.58900 11.81500  1.000 28.86542  ? 201 HEM A CGD 1 
HETATM 1300 O  O1D . HEM B 2 .   ? -5.06300  -13.17100 12.11100  1.000 40.30642  ? 201 HEM A O1D 1 
HETATM 1301 O  O2D . HEM B 2 .   ? -7.27900  -13.04500 12.10300  1.000 32.83427  ? 201 HEM A O2D 1 
HETATM 1302 N  NA  . HEM B 2 .   ? -5.84500  -8.16100  5.95100   1.000 12.24778  ? 201 HEM A NA  1 
HETATM 1303 N  NB  . HEM B 2 .   ? -5.23100  -5.37400  5.47700   1.000 11.86458  ? 201 HEM A NB  1 
HETATM 1304 N  NC  . HEM B 2 .   ? -5.88800  -4.72900  8.20600   1.000 12.02516  ? 201 HEM A NC  1 
HETATM 1305 N  ND  . HEM B 2 .   ? -6.47800  -7.53400  8.64800   1.000 12.18038  ? 201 HEM A ND  1 
HETATM 1306 FE FE  . HEM B 2 .   ? -6.00900  -6.46000  7.04200   1.000 12.78193  ? 201 HEM A FE  1 
HETATM 1307 C  CAA . Y6C C 3 .   ? 1.98000   -10.97400 22.15700  0.500 78.03134  ? 202 Y6C A CAA 1 
HETATM 1308 C  CAC . Y6C C 3 .   ? -0.66700  -7.96300  15.90200  0.500 26.74241  ? 202 Y6C A CAC 1 
HETATM 1309 C  CAD . Y6C C 3 .   ? -2.72200  -14.24400 18.09900  0.500 38.11207  ? 202 Y6C A CAD 1 
HETATM 1310 C  CAE . Y6C C 3 .   ? -1.12300  -8.97600  15.03600  0.500 28.99728  ? 202 Y6C A CAE 1 
HETATM 1311 C  CAF . Y6C C 3 .   ? -2.71300  -13.86200 16.74300  0.500 38.21913  ? 202 Y6C A CAF 1 
HETATM 1312 C  CAG . Y6C C 3 .   ? -0.64200  -8.22400  17.24000  0.500 29.10248  ? 202 Y6C A CAG 1 
HETATM 1313 C  CAH . Y6C C 3 .   ? -2.30500  -13.34700 19.03000  0.500 37.28636  ? 202 Y6C A CAH 1 
HETATM 1314 C  CAI . Y6C C 3 .   ? -1.04000  -9.82000  19.09600  0.500 41.93502  ? 202 Y6C A CAI 1 
HETATM 1315 C  CAM . Y6C C 3 .   ? 2.91900   -12.11400 22.52400  0.500 79.71877  ? 202 Y6C A CAM 1 
HETATM 1316 C  CAN . Y6C C 3 .   ? -1.46400  -11.03700 19.52200  0.500 43.01384  ? 202 Y6C A CAN 1 
HETATM 1317 C  CAO . Y6C C 3 .   ? -1.04800  -9.48500  17.72100  0.500 35.67141  ? 202 Y6C A CAO 1 
HETATM 1318 C  CAP . Y6C C 3 .   ? -1.88000  -12.05600 18.61000  0.500 38.01680  ? 202 Y6C A CAP 1 
HETATM 1319 C  CAQ . Y6C C 3 .   ? -1.48400  -10.44700 16.77800  0.500 25.82295  ? 202 Y6C A CAQ 1 
HETATM 1320 C  CAR . Y6C C 3 .   ? -1.91700  -11.75700 17.23400  0.500 26.25383  ? 202 Y6C A CAR 1 
HETATM 1321 N  NAJ . Y6C C 3 .   ? -1.51300  -10.18500 15.43800  0.500 17.36611  ? 202 Y6C A NAJ 1 
HETATM 1322 N  NAK . Y6C C 3 .   ? -2.32600  -12.66700 16.31400  0.500 28.85476  ? 202 Y6C A NAK 1 
HETATM 1323 N  NAL . Y6C C 3 .   ? -1.36600  -11.40500 20.87400  0.500 54.56900  ? 202 Y6C A NAL 1 
HETATM 1324 O  OAB . Y6C C 3 .   ? 4.09300   -12.09100 22.10100  0.500 75.82252  ? 202 Y6C A OAB 1 
HETATM 1325 O  OAM . Y6C C 3 .   ? 2.48800   -12.99600 23.26800  0.500 80.30083  ? 202 Y6C A OAM 1 
HETATM 1326 C  CAS . Y6C C 3 .   ? -0.20800  -11.92000 21.33500  0.500 63.58036  ? 202 Y6C A CAS 1 
HETATM 1327 C  CAT . Y6C C 3 .   ? 0.64100   -10.96000 22.06400  0.500 76.59840  ? 202 Y6C A CAT 1 
HETATM 1328 O  OAS . Y6C C 3 .   ? 0.20200   -13.05700 21.07300  0.500 60.95701  ? 202 Y6C A OAS 1 
HETATM 1329 C  CAA . Y6C D 3 .   ? 0.18000   -10.37500 25.79300  0.500 64.74134  ? 203 Y6C A CAA 1 
HETATM 1330 C  CAC . Y6C D 3 .   ? 1.80700   -3.42100  30.62000  0.500 38.61035  ? 203 Y6C A CAC 1 
HETATM 1331 C  CAD . Y6C D 3 .   ? 5.62900   -6.58700  25.82000  0.500 41.33991  ? 203 Y6C A CAD 1 
HETATM 1332 C  CAE . Y6C D 3 .   ? 3.04400   -2.93100  30.16900  0.500 31.10680  ? 203 Y6C A CAE 1 
HETATM 1333 C  CAF . Y6C D 3 .   ? 6.00700   -5.38800  26.44600  0.500 30.78619  ? 203 Y6C A CAF 1 
HETATM 1334 C  CAG . Y6C D 3 .   ? 1.33400   -4.57500  30.09200  0.500 37.33639  ? 203 Y6C A CAG 1 
HETATM 1335 C  CAH . Y6C D 3 .   ? 4.45000   -7.16800  26.16800  0.500 44.11575  ? 203 Y6C A CAH 1 
HETATM 1336 C  CAI . Y6C D 3 .   ? 1.64200   -6.45000  28.51400  0.500 38.87877  ? 203 Y6C A CAI 1 
HETATM 1337 C  CAM . Y6C D 3 .   ? 1.15400   -11.48500 25.98100  0.500 64.44441  ? 203 Y6C A CAM 1 
HETATM 1338 C  CAN . Y6C D 3 .   ? 2.37900   -7.09400  27.58600  0.500 43.38422  ? 203 Y6C A CAN 1 
HETATM 1339 C  CAO . Y6C D 3 .   ? 2.07900   -5.24800  29.11300  0.500 36.79212  ? 203 Y6C A CAO 1 
HETATM 1340 C  CAP . Y6C D 3 .   ? 3.63200   -6.55300  27.14400  0.500 38.26381  ? 203 Y6C A CAP 1 
HETATM 1341 C  CAQ . Y6C D 3 .   ? 3.30600   -4.68400  28.72000  0.500 26.85361  ? 203 Y6C A CAQ 1 
HETATM 1342 C  CAR . Y6C D 3 .   ? 4.10100   -5.35200  27.71400  0.500 31.43879  ? 203 Y6C A CAR 1 
HETATM 1343 N  NAJ . Y6C D 3 .   ? 3.77900   -3.52700  29.24600  0.500 31.12089  ? 203 Y6C A NAJ 1 
HETATM 1344 N  NAK . Y6C D 3 .   ? 5.28000   -4.78200  27.36600  0.500 27.88174  ? 203 Y6C A NAK 1 
HETATM 1345 N  NAL . Y6C D 3 .   ? 1.84800   -8.26100  26.98200  0.500 53.77789  ? 203 Y6C A NAL 1 
HETATM 1346 O  OAB . Y6C D 3 .   ? 2.30500   -11.32400 25.57100  0.500 67.29415  ? 203 Y6C A OAB 1 
HETATM 1347 O  OAM . Y6C D 3 .   ? 0.75800   -12.50300 26.54900  0.500 59.11874  ? 203 Y6C A OAM 1 
HETATM 1348 C  CAS . Y6C D 3 .   ? 1.22400   -8.06900  25.79800  0.500 60.72762  ? 203 Y6C A CAS 1 
HETATM 1349 C  CAT . Y6C D 3 .   ? 0.40600   -9.18100  25.25200  0.500 65.78234  ? 203 Y6C A CAT 1 
HETATM 1350 O  OAS . Y6C D 3 .   ? 1.33300   -6.98600  25.21500  0.500 61.34198  ? 203 Y6C A OAS 1 
HETATM 1351 NI NI  . NI  E 4 .   ? -1.80100  -11.97500 14.47400  1.000 28.68039  ? 204 NI  A NI  1 
HETATM 1352 O  O   . HOH F 5 .   ? 1.659     -14.023   27.557    1.000 35.73633  ? 301 HOH A O   1 
HETATM 1353 O  O   . HOH F 5 .   ? 14.48400  2.62400   -10.31100 1.000 7.04396   ? 302 HOH A O   1 
HETATM 1354 O  O   . HOH F 5 .   ? -21.61000 -9.91200  4.07000   1.000 28.46718  ? 303 HOH A O   1 
HETATM 1355 O  O   . HOH F 5 .   ? -9.205    -1.010    24.598    1.000 51.13408  ? 304 HOH A O   1 
HETATM 1356 O  O   . HOH F 5 .   ? -18.58500 -10.68400 4.89100   1.000 26.36343  ? 305 HOH A O   1 
HETATM 1357 O  O   . HOH F 5 .   ? -3.02400  7.79700   16.43100  1.000 26.51172  ? 306 HOH A O   1 
HETATM 1358 O  O   . HOH F 5 .   ? -3.07900  14.10000  -0.98700  1.000 35.18729  ? 307 HOH A O   1 
HETATM 1359 O  O   . HOH F 5 .   ? 12.51500  0.60900   6.86700   1.000 26.24462  ? 308 HOH A O   1 
HETATM 1360 O  O   . HOH F 5 .   ? 14.75600  -6.28800  3.11600   1.000 31.74565  ? 309 HOH A O   1 
HETATM 1361 O  O   . HOH F 5 .   ? -8.919    -2.510    29.006    1.000 26.10305  ? 310 HOH A O   1 
HETATM 1362 O  O   . HOH F 5 .   ? -18.32800 -10.77600 8.91100   1.000 42.20654  ? 311 HOH A O   1 
HETATM 1363 O  O   . HOH F 5 .   ? -2.38900  -13.87500 13.64700  1.000 34.16855  ? 312 HOH A O   1 
HETATM 1364 O  O   . HOH F 5 .   ? 4.18300   -13.07700 17.95200  1.000 38.47036  ? 313 HOH A O   1 
HETATM 1365 O  O   . HOH F 5 .   ? 7.64300   10.39400  2.32000   1.000 39.84868  ? 314 HOH A O   1 
HETATM 1366 O  O   . HOH F 5 .   ? -4.02300  10.33500  8.89400   1.000 27.14149  ? 315 HOH A O   1 
HETATM 1367 O  O   . HOH F 5 .   ? -17.43700 3.76100   5.32700   1.000 22.93604  ? 316 HOH A O   1 
HETATM 1368 O  O   . HOH F 5 .   ? 10.28400  13.75400  -11.39300 1.000 24.53342  ? 317 HOH A O   1 
HETATM 1369 O  O   . HOH F 5 .   ? 3.40700   12.22400  -9.67500  1.000 26.28065  ? 318 HOH A O   1 
HETATM 1370 O  O   . HOH F 5 .   ? -15.25100 0.85000   13.47500  1.000 25.02115  ? 319 HOH A O   1 
HETATM 1371 O  O   . HOH F 5 .   ? -0.12300  -13.89600 11.01300  1.000 27.39283  ? 320 HOH A O   1 
HETATM 1372 O  O   . HOH F 5 .   ? 5.14200   4.51700   20.07300  1.000 35.90029  ? 321 HOH A O   1 
HETATM 1373 O  O   . HOH F 5 .   ? -8.02200  -8.64600  -2.06000  1.000 17.50279  ? 322 HOH A O   1 
HETATM 1374 O  O   . HOH F 5 .   ? -7.928    2.702     23.391    1.000 39.24510  ? 323 HOH A O   1 
HETATM 1375 O  O   . HOH F 5 .   ? 8.28900   -9.04800  26.77300  1.000 35.33863  ? 324 HOH A O   1 
HETATM 1376 O  O   . HOH F 5 .   ? 9.68100   4.95600   12.67700  1.000 35.21355  ? 325 HOH A O   1 
HETATM 1377 O  O   . HOH F 5 .   ? 1.04800   8.12400   10.41000  1.000 25.46984  ? 326 HOH A O   1 
HETATM 1378 O  O   . HOH F 5 .   ? 14.40300  -4.00800  -2.61500  1.000 21.06030  ? 327 HOH A O   1 
HETATM 1379 O  O   . HOH F 5 .   ? 14.77600  10.43200  -5.68400  1.000 30.42474  ? 328 HOH A O   1 
HETATM 1380 O  O   . HOH F 5 .   ? 5.13500   14.29900  -3.71300  1.000 32.42592  ? 329 HOH A O   1 
HETATM 1381 O  O   . HOH F 5 .   ? 11.20500  -7.48800  -7.78000  1.000 27.74456  ? 330 HOH A O   1 
HETATM 1382 O  O   . HOH F 5 .   ? 4.147     -1.785    26.415    1.000 31.39906  ? 331 HOH A O   1 
HETATM 1383 O  O   . HOH F 5 .   ? -15.08200 6.64700   6.02800   1.000 30.71424  ? 332 HOH A O   1 
HETATM 1384 O  O   . HOH F 5 .   ? -8.27800  -13.22800 8.14200   1.000 29.42659  ? 333 HOH A O   1 
HETATM 1385 O  O   . HOH F 5 .   ? -23.32000 -6.30700  5.51900   1.000 31.43767  ? 334 HOH A O   1 
HETATM 1386 O  O   . HOH F 5 .   ? -19.08200 -3.74500  10.94500  1.000 27.52149  ? 335 HOH A O   1 
HETATM 1387 O  O   . HOH F 5 .   ? -10.19600 -10.68000 1.98800   1.000 15.98328  ? 336 HOH A O   1 
HETATM 1388 O  O   . HOH F 5 .   ? 14.58300  0.86300   -9.30600  1.000 27.68178  ? 337 HOH A O   1 
HETATM 1389 O  O   . HOH F 5 .   ? 2.076     9.254     15.912    1.000 40.36941  ? 338 HOH A O   1 
HETATM 1390 O  O   . HOH F 5 .   ? 14.30000  9.59200   -8.00100  1.000 27.90533  ? 339 HOH A O   1 
HETATM 1391 O  O   . HOH F 5 .   ? 8.56900   11.12700  -13.48800 1.000 32.39360  ? 340 HOH A O   1 
HETATM 1392 O  O   . HOH F 5 .   ? 15.87400  -10.42100 -2.54500  1.000 21.10334  ? 341 HOH A O   1 
HETATM 1393 O  O   . HOH F 5 .   ? 8.13000   -9.87800  12.57400  1.000 17.58905  ? 342 HOH A O   1 
HETATM 1394 O  O   . HOH F 5 .   ? -9.62700  10.82000  8.57600   1.000 23.08063  ? 343 HOH A O   1 
HETATM 1395 O  O   . HOH F 5 .   ? -14.38800 -10.53300 -6.19800  1.000 21.40333  ? 344 HOH A O   1 
HETATM 1396 O  O   . HOH F 5 .   ? -12.40700 6.43500   9.84600   1.000 16.98883  ? 345 HOH A O   1 
HETATM 1397 O  O   . HOH F 5 .   ? 3.21200   6.92900   19.06100  1.000 34.67269  ? 346 HOH A O   1 
HETATM 1398 O  O   . HOH F 5 .   ? -6.14600  8.83800   9.70900   1.000 18.47824  ? 347 HOH A O   1 
HETATM 1399 O  O   . HOH F 5 .   ? 15.20300  8.38100   2.56100   1.000 26.28203  ? 348 HOH A O   1 
HETATM 1400 O  O   . HOH F 5 .   ? 0.14700   -4.19600  -14.05900 1.000 25.50236  ? 349 HOH A O   1 
HETATM 1401 O  O   . HOH F 5 .   ? -7.18300  6.65200   16.10900  1.000 27.41531  ? 350 HOH A O   1 
HETATM 1402 O  O   . HOH F 5 .   ? 3.88400   -11.37500 -1.96900  1.000 22.57654  ? 351 HOH A O   1 
HETATM 1403 O  O   . HOH F 5 .   ? -23.74100 1.10700   -3.97600  1.000 34.19449  ? 352 HOH A O   1 
HETATM 1404 O  O   . HOH F 5 .   ? 5.38200   -10.49900 -5.66600  1.000 24.36596  ? 353 HOH A O   1 
HETATM 1405 O  O   . HOH F 5 .   ? 11.23800  -12.86800 12.38800  1.000 38.02361  ? 354 HOH A O   1 
HETATM 1406 O  O   . HOH F 5 .   ? 13.98400  -9.96100  5.44400   1.000 30.03779  ? 355 HOH A O   1 
HETATM 1407 O  O   . HOH F 5 .   ? -21.572   2.952     -1.248    1.000 20.92654  ? 356 HOH A O   1 
HETATM 1408 O  O   . HOH F 5 .   ? 13.309    -7.019    23.065    1.000 19.02406  ? 357 HOH A O   1 
HETATM 1409 O  O   . HOH F 5 .   ? -5.33000  1.95600   -15.49700 1.000 31.84807  ? 358 HOH A O   1 
HETATM 1410 O  O   . HOH F 5 .   ? -15.67800 6.72000   -1.17200  1.000 19.75763  ? 359 HOH A O   1 
HETATM 1411 O  O   . HOH F 5 .   ? -1.31700  -13.32200 8.14700   1.000 24.88972  ? 360 HOH A O   1 
HETATM 1412 O  O   . HOH F 5 .   ? -15.25400 -3.94500  -4.88800  1.000 24.71591  ? 361 HOH A O   1 
HETATM 1413 O  O   . HOH F 5 .   ? 4.15200   8.88200   5.45200   1.000 20.47554  ? 362 HOH A O   1 
HETATM 1414 O  O   . HOH F 5 .   ? -3.41600  10.80800  1.12700   1.000 22.78500  ? 363 HOH A O   1 
HETATM 1415 O  O   . HOH F 5 .   ? -13.01700 6.67800   12.73000  1.000 36.92823  ? 364 HOH A O   1 
HETATM 1416 O  O   . HOH F 5 .   ? 8.55000   -12.00200 19.38900  1.000 29.73606  ? 365 HOH A O   1 
HETATM 1417 O  O   . HOH F 5 .   ? 14.52300  -9.51600  17.02400  1.000 23.24066  ? 366 HOH A O   1 
HETATM 1418 O  O   . HOH F 5 .   ? -8.22800  -0.19800  17.59000  1.000 40.97899  ? 367 HOH A O   1 
HETATM 1419 O  O   . HOH F 5 .   ? -0.26100  12.83600  -4.53600  1.000 36.25288  ? 368 HOH A O   1 
HETATM 1420 O  O   . HOH F 5 .   ? -3.95100  -6.81800  7.89200   1.000 21.55473  ? 369 HOH A O   1 
HETATM 1421 O  O   . HOH F 5 .   ? 0.65000   -10.02800 -4.94600  1.000 23.28065  ? 370 HOH A O   1 
HETATM 1422 O  O   . HOH F 5 .   ? -10.40100 -7.13600  14.63700  1.000 36.58137  ? 371 HOH A O   1 
HETATM 1423 O  O   . HOH F 5 .   ? -15.90800 0.86800   -4.64400  1.000 20.87715  ? 372 HOH A O   1 
HETATM 1424 O  O   . HOH F 5 .   ? -3.08700  -8.07100  -9.89800  1.000 17.10787  ? 373 HOH A O   1 
HETATM 1425 O  O   . HOH F 5 .   ? -22.97200 -3.93100  8.39000   1.000 31.56751  ? 374 HOH A O   1 
HETATM 1426 O  O   . HOH F 5 .   ? 10.79300  8.06700   5.58000   1.000 32.17293  ? 375 HOH A O   1 
HETATM 1427 O  O   . HOH F 5 .   ? -5.22200  -0.21800  -8.13400  1.000 14.85345  ? 376 HOH A O   1 
HETATM 1428 O  O   . HOH F 5 .   ? 12.10500  -15.37200 15.90600  1.000 40.98171  ? 377 HOH A O   1 
HETATM 1429 O  O   . HOH F 5 .   ? 12.29300  -1.39200  -9.71400  1.000 24.23369  ? 378 HOH A O   1 
HETATM 1430 O  O   . HOH F 5 .   ? -24.628   -4.888    0.323     1.000 33.22350  ? 379 HOH A O   1 
HETATM 1431 O  O   . HOH F 5 .   ? -8.62700  8.48000   3.06900   1.000 23.71852  ? 380 HOH A O   1 
HETATM 1432 O  O   . HOH F 5 .   ? 9.67700   0.54200   10.89300  1.000 17.99815  ? 381 HOH A O   1 
HETATM 1433 O  O   . HOH F 5 .   ? -10.88400 -10.03800 13.19300  1.000 27.15647  ? 382 HOH A O   1 
HETATM 1434 O  O   . HOH F 5 .   ? -11.57500 -12.88800 7.00900   1.000 24.12109  ? 383 HOH A O   1 
HETATM 1435 O  O   . HOH F 5 .   ? -13.64000 -11.91100 2.49000   1.000 19.43533  ? 384 HOH A O   1 
HETATM 1436 O  O   . HOH F 5 .   ? 6.07400   -9.00800  6.96100   1.000 14.48059  ? 385 HOH A O   1 
HETATM 1437 O  O   . HOH F 5 .   ? 10.50500  -11.90100 2.01100   1.000 13.18916  ? 386 HOH A O   1 
HETATM 1438 O  O   . HOH F 5 .   ? -21.37100 1.72700   10.62700  1.000 31.27837  ? 387 HOH A O   1 
HETATM 1439 O  O   . HOH F 5 .   ? -5.55900  -3.30800  -15.22400 1.000 33.64800  ? 388 HOH A O   1 
HETATM 1440 O  O   . HOH F 5 .   ? 14.076    -6.093    6.522     1.000 25.98416  ? 389 HOH A O   1 
HETATM 1441 O  O   . HOH F 5 .   ? -19.58200 -7.30300  -1.94700  1.000 28.13256  ? 390 HOH A O   1 
HETATM 1442 O  O   . HOH F 5 .   ? -4.01100  -11.50000 14.40500  1.000 32.81751  ? 391 HOH A O   1 
HETATM 1443 O  O   . HOH F 5 .   ? 9.36400   4.89700   -8.86200  1.000 18.85981  ? 392 HOH A O   1 
HETATM 1444 O  O   . HOH F 5 .   ? 7.76900   -11.20500 -4.29600  1.000 17.51307  ? 393 HOH A O   1 
HETATM 1445 O  O   . HOH F 5 .   ? 1.10400   -9.49100  -7.57600  1.000 22.50712  ? 394 HOH A O   1 
HETATM 1446 O  O   . HOH F 5 .   ? -9.37200  8.72200   -0.55600  1.000 29.46919  ? 395 HOH A O   1 
HETATM 1447 O  O   . HOH F 5 .   ? 14.607    -1.856    9.261     1.000 35.94659  ? 396 HOH A O   1 
HETATM 1448 O  O   . HOH F 5 .   ? 5.59900   5.28700   -6.36200  1.000 30.67488  ? 397 HOH A O   1 
HETATM 1449 O  O   . HOH F 5 .   ? -1.99100  7.88900   0.70400   1.000 20.04127  ? 398 HOH A O   1 
HETATM 1450 O  O   . HOH F 5 .   ? 10.12100  -11.19800 -1.44800  1.000 14.43707  ? 399 HOH A O   1 
HETATM 1451 O  O   . HOH F 5 .   ? -2.52800  -11.98200 1.09400   1.000 16.11796  ? 400 HOH A O   1 
HETATM 1452 O  O   . HOH F 5 .   ? -10.413   -16.386   9.268     1.000 43.47659  ? 401 HOH A O   1 
HETATM 1453 O  O   . HOH F 5 .   ? 6.90000   0.34500   -13.90900 1.000 24.76538  ? 402 HOH A O   1 
HETATM 1454 O  O   . HOH F 5 .   ? 16.38200  -9.82000  2.09900   1.000 22.43316  ? 403 HOH A O   1 
HETATM 1455 O  O   . HOH F 5 .   ? -6.44300  9.16400   -6.25000  1.000 23.13345  ? 404 HOH A O   1 
HETATM 1456 O  O   . HOH F 5 .   ? 5.59400   -4.03000  -9.46900  1.000 19.97476  ? 405 HOH A O   1 
HETATM 1457 O  O   . HOH F 5 .   ? 1.33100   -9.89300  15.26000  1.000 44.92333  ? 406 HOH A O   1 
HETATM 1458 O  O   . HOH F 5 .   ? -8.20100  2.85600   -13.37000 1.000 44.42952  ? 407 HOH A O   1 
HETATM 1459 O  O   . HOH F 5 .   ? 11.73600  9.16100   -7.97000  1.000 19.70131  ? 408 HOH A O   1 
HETATM 1460 O  O   . HOH F 5 .   ? -11.18300 -6.22200  -10.66100 1.000 23.97542  ? 409 HOH A O   1 
HETATM 1461 O  O   . HOH F 5 .   ? 7.50900   9.89000   7.28800   1.000 38.40661  ? 410 HOH A O   1 
HETATM 1462 O  O   . HOH F 5 .   ? -5.64500  1.98600   -6.20600  1.000 19.75994  ? 411 HOH A O   1 
HETATM 1463 O  O   . HOH F 5 .   ? 3.29400   -7.39100  -3.27600  1.000 23.47852  ? 412 HOH A O   1 
HETATM 1464 O  O   . HOH F 5 .   ? 16.82400  7.11000   3.73600   1.000 33.46238  ? 413 HOH A O   1 
HETATM 1465 O  O   . HOH F 5 .   ? 17.11900  4.27900   -3.60500  1.000 31.79331  ? 414 HOH A O   1 
HETATM 1466 O  O   . HOH F 5 .   ? 3.72500   -4.41300  19.59800  1.000 35.73962  ? 415 HOH A O   1 
HETATM 1467 O  O   . HOH F 5 .   ? -17.81600 -6.73700  -0.36200  1.000 26.41380  ? 416 HOH A O   1 
HETATM 1468 O  O   . HOH F 5 .   ? -2.80800  -14.90300 4.69000   1.000 31.56048  ? 417 HOH A O   1 
HETATM 1469 O  O   . HOH F 5 .   ? -5.75100  -8.32800  -3.57600  1.000 15.60514  ? 418 HOH A O   1 
HETATM 1470 O  O   . HOH F 5 .   ? -17.70000 6.29500   0.69600   1.000 22.96287  ? 419 HOH A O   1 
HETATM 1471 O  O   . HOH F 5 .   ? -5.30000  -11.19500 16.81300  1.000 33.06710  ? 420 HOH A O   1 
HETATM 1472 O  O   . HOH F 5 .   ? -2.20500  8.00600   -19.09400 1.000 30.33154  ? 421 HOH A O   1 
HETATM 1473 O  O   . HOH F 5 .   ? -9.08900  5.08000   17.06400  1.000 42.57245  ? 422 HOH A O   1 
HETATM 1474 O  O   . HOH F 5 .   ? 14.837    2.039     7.332     1.000 23.82461  ? 423 HOH A O   1 
HETATM 1475 O  O   . HOH F 5 .   ? 1.59400   4.95800   10.39200  1.000 20.09609  ? 424 HOH A O   1 
HETATM 1476 O  O   . HOH F 5 .   ? 11.87700  4.51700   10.49700  1.000 37.00005  ? 425 HOH A O   1 
HETATM 1477 O  O   . HOH F 5 .   ? 1.35300   -12.91100 18.41500  1.000 38.16094  ? 426 HOH A O   1 
HETATM 1478 O  O   . HOH F 5 .   ? 11.82800  -0.94100  21.23700  1.000 29.33010  ? 427 HOH A O   1 
HETATM 1479 O  O   . HOH F 5 .   ? -1.17800  16.05300  -9.34100  1.000 46.31996  ? 428 HOH A O   1 
HETATM 1480 O  O   . HOH F 5 .   ? 13.38600  -12.07500 -0.07700  1.000 15.31490  ? 429 HOH A O   1 
HETATM 1481 O  O   . HOH F 5 .   ? -20.20700 -6.14400  11.41900  1.000 30.94326  ? 430 HOH A O   1 
HETATM 1482 O  O   . HOH F 5 .   ? 13.63700  10.77300  -2.35900  1.000 37.54082  ? 431 HOH A O   1 
HETATM 1483 O  O   . HOH F 5 .   ? -3.35900  9.16000   4.64300   1.000 34.09893  ? 432 HOH A O   1 
HETATM 1484 O  O   . HOH F 5 .   ? -13.06900 5.70200   -8.13800  1.000 40.48118  ? 433 HOH A O   1 
HETATM 1485 O  O   . HOH F 5 .   ? -15.84700 3.52000   -5.88900  1.000 37.84671  ? 434 HOH A O   1 
HETATM 1486 O  O   . HOH F 5 .   ? 12.87200  -11.42700 10.48900  1.000 27.63600  ? 435 HOH A O   1 
HETATM 1487 O  O   . HOH F 5 .   ? 1.45300   9.07500   -18.70300 1.000 26.77097  ? 436 HOH A O   1 
HETATM 1488 O  O   . HOH F 5 .   ? 7.11400   -15.80800 16.99400  1.000 32.81383  ? 437 HOH A O   1 
HETATM 1489 O  O   . HOH F 5 .   ? -9.56600  -13.68500 10.34200  1.000 27.49728  ? 438 HOH A O   1 
HETATM 1490 O  O   . HOH F 5 .   ? -20.31800 -7.93100  -7.02600  1.000 33.76127  ? 439 HOH A O   1 
HETATM 1491 O  O   . HOH F 5 .   ? 4.51300   -15.35000 16.55700  1.000 27.71387  ? 440 HOH A O   1 
HETATM 1492 O  O   . HOH F 5 .   ? -10.00400 -9.44500  -11.86800 1.000 37.95102  ? 441 HOH A O   1 
HETATM 1493 O  O   . HOH F 5 .   ? -2.94000  -9.35000  8.03300   1.000 36.89712  ? 442 HOH A O   1 
HETATM 1494 O  O   . HOH F 5 .   ? 11.86400  13.66900  -1.08600  1.000 30.39163  ? 443 HOH A O   1 
HETATM 1495 O  O   . HOH F 5 .   ? -6.40600  5.23800   -12.80700 1.000 31.09062  ? 444 HOH A O   1 
HETATM 1496 O  O   . HOH F 5 .   ? -9.08000  -11.63600 14.07200  1.000 39.05506  ? 445 HOH A O   1 
HETATM 1497 O  O   . HOH F 5 .   ? 15.173    -3.993    16.908    1.000 33.75642  ? 446 HOH A O   1 
HETATM 1498 O  O   . HOH F 5 .   ? 3.85500   6.76400   9.35400   1.000 19.92256  ? 447 HOH A O   1 
HETATM 1499 O  O   . HOH F 5 .   ? -5.65100  11.05600  4.08600   1.000 36.33995  ? 448 HOH A O   1 
HETATM 1500 O  O   . HOH F 5 .   ? -11.74200 6.97400   1.83100   1.000 33.33033  ? 449 HOH A O   1 
HETATM 1501 O  O   . HOH F 5 .   ? -12.404   -2.783    -11.527   1.000 24.91801  ? 450 HOH A O   1 
HETATM 1502 O  O   . HOH F 5 .   ? 2.32500   0.00300   -15.64900 1.000 35.37913  ? 451 HOH A O   1 
HETATM 1503 O  O   . HOH F 5 .   ? -13.04000 1.29600   15.34600  1.000 42.87205  ? 452 HOH A O   1 
HETATM 1504 O  O   . HOH F 5 .   ? 17.85300  -0.44200  -9.57000  1.000 48.18945  ? 453 HOH A O   1 
HETATM 1505 O  O   . HOH F 5 .   ? -5.33500  -9.72500  -9.52400  1.000 21.36874  ? 454 HOH A O   1 
HETATM 1506 O  O   . HOH F 5 .   ? 2.52500   11.19400  0.72200   1.000 40.70129  ? 455 HOH A O   1 
HETATM 1507 O  O   . HOH F 5 .   ? 11.32000  -1.48200  11.98200  1.000 26.04853  ? 456 HOH A O   1 
HETATM 1508 O  O   . HOH F 5 .   ? -21.44600 -2.30200  10.06000  1.000 30.26744  ? 457 HOH A O   1 
HETATM 1509 O  O   . HOH F 5 .   ? 13.24300  -12.81100 5.42700   1.000 36.21469  ? 458 HOH A O   1 
HETATM 1510 O  O   . HOH F 5 .   ? -3.56500  -11.70600 8.35400   1.000 35.66676  ? 459 HOH A O   1 
HETATM 1511 O  O   . HOH F 5 .   ? -2.55400  -7.42400  9.32800   1.000 36.07321  ? 460 HOH A O   1 
HETATM 1512 O  O   . HOH F 5 .   ? 1.22100   -2.58300  -15.84200 1.000 40.06928  ? 461 HOH A O   1 
HETATM 1513 O  O   . HOH F 5 .   ? -16.77300 7.02700   -3.81800  1.000 30.62907  ? 462 HOH A O   1 
HETATM 1514 O  O   . HOH F 5 .   ? 4.23800   10.25500  -14.41900 1.000 31.27600  ? 463 HOH A O   1 
HETATM 1515 O  O   . HOH F 5 .   ? -3.32700  4.01300   -16.76000 1.000 37.78691  ? 464 HOH A O   1 
HETATM 1516 O  O   . HOH F 5 .   ? 4.69300   8.98800   8.22600   1.000 38.12211  ? 465 HOH A O   1 
HETATM 1517 O  O   . HOH F 5 .   ? 2.91900   -11.62800 -8.67100  1.000 35.66496  ? 466 HOH A O   1 
HETATM 1518 O  O   . HOH F 5 .   ? 11.51900  -2.46300  -12.12400 1.000 34.53634  ? 467 HOH A O   1 
HETATM 1519 O  O   . HOH F 5 .   ? -20.221   -10.901   -1.592    1.000 28.64799  ? 468 HOH A O   1 
HETATM 1520 O  O   . HOH F 5 .   ? 8.66800   -14.71600 18.85900  1.000 33.25164  ? 469 HOH A O   1 
HETATM 1521 O  O   . HOH F 5 .   ? -22.30300 -8.64500  -0.17600  1.000 27.14954  ? 470 HOH A O   1 
HETATM 1522 O  O   . HOH F 5 .   ? 3.24500   13.19100  -2.14300  1.000 33.32860  ? 471 HOH A O   1 
HETATM 1523 O  O   . HOH F 5 .   ? 13.33800  -4.04500  -9.33200  1.000 41.99572  ? 472 HOH A O   1 
HETATM 1524 O  O   . HOH F 5 .   ? -17.148   -6.094    17.287    1.000 49.96808  ? 473 HOH A O   1 
HETATM 1525 O  O   . HOH F 5 .   ? 14.67700  -10.84700 14.78500  1.000 31.18660  ? 474 HOH A O   1 
HETATM 1526 O  O   . HOH F 5 .   ? 12.712    -9.351    -6.760    1.000 28.40130  ? 475 HOH A O   1 
HETATM 1527 O  O   . HOH F 5 .   ? -5.56600  -13.37800 8.43700   1.000 30.97820  ? 476 HOH A O   1 
HETATM 1528 O  O   . HOH F 5 .   ? -8.94000  8.91200   -5.52000  1.000 25.66225  ? 477 HOH A O   1 
HETATM 1529 O  O   . HOH F 5 .   ? 9.20100   2.18700   13.11000  1.000 24.39373  ? 478 HOH A O   1 
HETATM 1530 O  O   . HOH F 5 .   ? 10.79600  2.20100   9.02600   1.000 38.84591  ? 479 HOH A O   1 
HETATM 1531 O  O   . HOH F 5 .   ? -1.00100  8.48200   3.07700   1.000 30.74936  ? 480 HOH A O   1 
HETATM 1532 O  O   . HOH F 5 .   ? -15.827   -11.767   6.225     1.000 34.58809  ? 481 HOH A O   1 
HETATM 1533 O  O   . HOH F 5 .   ? -2.62700  -7.69200  -12.61200 1.000 25.05239  ? 482 HOH A O   1 
HETATM 1534 O  O   . HOH F 5 .   ? -8.69000  -10.89100 -4.02100  1.000 22.16968  ? 483 HOH A O   1 
HETATM 1535 O  O   . HOH F 5 .   ? 12.428    -11.001   21.063    1.000 36.44065  ? 484 HOH A O   1 
HETATM 1536 O  O   . HOH F 5 .   ? 6.74600   9.75100   4.76300   1.000 33.91674  ? 485 HOH A O   1 
HETATM 1537 O  O   . HOH F 5 .   ? -22.70100 -8.67700  6.14000   1.000 35.93936  ? 486 HOH A O   1 
HETATM 1538 O  O   . HOH F 5 .   ? -1.37800  -12.16200 -5.26400  1.000 37.76247  ? 487 HOH A O   1 
HETATM 1539 O  O   . HOH F 5 .   ? 6.892     -14.861   23.295    1.000 44.74294  ? 488 HOH A O   1 
HETATM 1540 O  O   . HOH F 5 .   ? -4.49300  -6.92700  -14.42700 1.000 41.58397  ? 489 HOH A O   1 
HETATM 1541 O  O   . HOH F 5 .   ? -11.398   9.228     18.526    1.000 47.91048  ? 490 HOH A O   1 
HETATM 1542 O  O   . HOH F 5 .   ? -4.32700  -10.98800 -3.59600  1.000 23.11146  ? 491 HOH A O   1 
HETATM 1543 O  O   . HOH F 5 .   ? 10.08200  -12.66900 23.38300  1.000 38.46029  ? 492 HOH A O   1 
HETATM 1544 O  O   . HOH F 5 .   ? 6.78400   9.77900   -14.97700 1.000 26.59449  ? 493 HOH A O   1 
HETATM 1545 O  O   . HOH F 5 .   ? 3.31300   -9.97400  -3.94800  1.000 21.34325  ? 494 HOH A O   1 
HETATM 1546 O  O   . HOH F 5 .   ? -4.07600  -12.25100 -1.17400  1.000 18.10419  ? 495 HOH A O   1 
HETATM 1547 O  O   . HOH F 5 .   ? -14.002   7.759     3.408     1.000 33.59598  ? 496 HOH A O   1 
HETATM 1548 O  O   . HOH F 5 .   ? -4.62700  -14.85800 6.58700   1.000 33.62039  ? 497 HOH A O   1 
HETATM 1549 O  O   . HOH F 5 .   ? -16.98300 -0.57100  14.63800  1.000 36.21274  ? 498 HOH A O   1 
HETATM 1550 O  O   . HOH F 5 .   ? 15.88400  -7.09500  16.33000  1.000 35.62203  ? 499 HOH A O   1 
HETATM 1551 O  O   . HOH F 5 .   ? -8.49000  -10.66600 -0.28000  1.000 15.94454  ? 500 HOH A O   1 
HETATM 1552 O  O   . HOH F 5 .   ? -7.39300  -4.97400  -15.87000 1.000 47.82075  ? 501 HOH A O   1 
HETATM 1553 O  O   . HOH F 5 .   ? -22.21700 -6.25300  9.30900   1.000 36.61856  ? 502 HOH A O   1 
HETATM 1554 O  O   . HOH F 5 .   ? 0.19800   -7.81300  -13.23100 1.000 32.98847  ? 503 HOH A O   1 
HETATM 1555 O  O   . HOH F 5 .   ? 10.92700  -12.60800 20.83000  1.000 33.77306  ? 504 HOH A O   1 
HETATM 1556 O  O   . HOH F 5 .   ? 4.26400   -4.93400  -11.73800 1.000 35.09874  ? 505 HOH A O   1 
HETATM 1557 O  O   . HOH F 5 .   ? 0.25000   -10.17800 -11.55500 1.000 33.92154  ? 506 HOH A O   1 
HETATM 1558 O  O   . HOH F 5 .   ? -1.02500  -9.80900  -9.24400  1.000 20.08306  ? 507 HOH A O   1 
HETATM 1559 O  O   . HOH F 5 .   ? -7.04000  10.33300  12.04700  1.000 24.41058  ? 508 HOH A O   1 
HETATM 1560 O  O   . HOH F 5 .   ? 2.39800   -5.27500  -13.16500 1.000 43.31408  ? 509 HOH A O   1 
HETATM 1561 O  O   . HOH F 5 .   ? -23.35000 3.46200   11.35100  1.000 39.88759  ? 510 HOH A O   1 
HETATM 1562 O  O   . HOH F 5 .   ? 4.77400   -0.81100  -15.16600 1.000 27.12999  ? 511 HOH A O   1 
HETATM 1563 O  O   . HOH F 5 .   ? 1.62700   10.02800  3.84800   1.000 31.63553  ? 512 HOH A O   1 
HETATM 1564 O  O   . HOH F 5 .   ? -23.13800 -6.46500  -1.08600  1.000 40.00831  ? 513 HOH A O   1 
HETATM 1565 O  O   . HOH F 5 .   ? -19.14100 -2.03100  13.25600  1.000 32.77694  ? 514 HOH A O   1 
HETATM 1566 O  O   . HOH F 5 .   ? 5.02300   -3.44900  -13.97700 1.000 33.73669  ? 515 HOH A O   1 
HETATM 1567 O  O   . HOH F 5 .   ? -22.008   -12.570   7.782     1.000 40.11867  ? 516 HOH A O   1 
# 
